data_9KAU
# 
_entry.id   9KAU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   9KAU         pdb_00009kau 10.2210/pdb9kau/pdb 
WWPDB D_1300052920 ?            ?                   
# 
_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       2024-11-20 
# 
_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                        9KAU 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ycy21th@sdu.edu.cn 
_pdbx_contact_author.name_first         Yang 
_pdbx_contact_author.name_last          Chuyu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4202-9325 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Liu, Y.'  1 0000-0001-9838-0512 
'Yang, C.' 2 0000-0002-4202-9325 
# 
_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                     
'Homodimer of cystatohinine beta lyase PatB/PLP/L-(+)-alliin complex from Bacillus cereus(NCBI Reference Sequence: WP_001974105.1)' 
_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 'Liu, Y.'  1 ? 
primary 'Yang, C.' 2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'cysteine-S-conjugate beta-lyase' 44391.781 2  4.4.1.13 
'E51K, L179I, Q180K, E286K, Q296K, I302M, T304D, A308T, R326A, K328N, N332D, A336K' ? 
'Homodimer of cystatohinine beta lyase PatB/PLP/L-(+)-alliin complex from Bacillus cereus(NCBI Reference Sequence: WP_001974105.1)' 
2 non-polymer syn ALLIIN                            177.221   1  ?        ? ? ? 
3 water       nat water                             18.015    98 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MQLFHKAINRRGTHSIKWDTYKNEELIHAWIADMDFEVPKPIQTALKQRIKHPIFGYTLPPENIGDIICNWTKQQYDWDI
QKEWIVFSAGIVPALSTSIQAFTKENESVLVQPPIYPPFFEMVTTNNRQLCVSPLQKQNDTYVIDFKHLEKQFQQGIKLM
LLCSPHNPIGRVWTKEELIKLGSLCTKYNVIVVADEIHSDIIYADHTHTPFASLSEELAERTITCMAPS(LLP)TFNIAG
LQASIIIIPNEKLRHAFTAIQYRQGFHGLNIFAYTAMQSAYTECNDWLNKIRLYIEDNAKFACEYMKDHIPTLSVTKPEG
SFLLWIDCSALNLSQDERTKLLEEKGKIIVEPGEKYGLGGEEHIRINIGCPRSVLEEILNRLRHTFS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MQLFHKAINRRGTHSIKWDTYKNEELIHAWIADMDFEVPKPIQTALKQRIKHPIFGYTLPPENIGDIICNWTKQQYDWDI
QKEWIVFSAGIVPALSTSIQAFTKENESVLVQPPIYPPFFEMVTTNNRQLCVSPLQKQNDTYVIDFKHLEKQFQQGIKLM
LLCSPHNPIGRVWTKEELIKLGSLCTKYNVIVVADEIHSDIIYADHTHTPFASLSEELAERTITCMAPSKTFNIAGLQAS
IIIIPNEKLRHAFTAIQYRQGFHGLNIFAYTAMQSAYTECNDWLNKIRLYIEDNAKFACEYMKDHIPTLSVTKPEGSFLL
WIDCSALNLSQDERTKLLEEKGKIIVEPGEKYGLGGEEHIRINIGCPRSVLEEILNRLRHTFS
;
_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 ALLIIN OO0 
3 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   GLN n 
1 3   LEU n 
1 4   PHE n 
1 5   HIS n 
1 6   LYS n 
1 7   ALA n 
1 8   ILE n 
1 9   ASN n 
1 10  ARG n 
1 11  ARG n 
1 12  GLY n 
1 13  THR n 
1 14  HIS n 
1 15  SER n 
1 16  ILE n 
1 17  LYS n 
1 18  TRP n 
1 19  ASP n 
1 20  THR n 
1 21  TYR n 
1 22  LYS n 
1 23  ASN n 
1 24  GLU n 
1 25  GLU n 
1 26  LEU n 
1 27  ILE n 
1 28  HIS n 
1 29  ALA n 
1 30  TRP n 
1 31  ILE n 
1 32  ALA n 
1 33  ASP n 
1 34  MET n 
1 35  ASP n 
1 36  PHE n 
1 37  GLU n 
1 38  VAL n 
1 39  PRO n 
1 40  LYS n 
1 41  PRO n 
1 42  ILE n 
1 43  GLN n 
1 44  THR n 
1 45  ALA n 
1 46  LEU n 
1 47  LYS n 
1 48  GLN n 
1 49  ARG n 
1 50  ILE n 
1 51  LYS n 
1 52  HIS n 
1 53  PRO n 
1 54  ILE n 
1 55  PHE n 
1 56  GLY n 
1 57  TYR n 
1 58  THR n 
1 59  LEU n 
1 60  PRO n 
1 61  PRO n 
1 62  GLU n 
1 63  ASN n 
1 64  ILE n 
1 65  GLY n 
1 66  ASP n 
1 67  ILE n 
1 68  ILE n 
1 69  CYS n 
1 70  ASN n 
1 71  TRP n 
1 72  THR n 
1 73  LYS n 
1 74  GLN n 
1 75  GLN n 
1 76  TYR n 
1 77  ASP n 
1 78  TRP n 
1 79  ASP n 
1 80  ILE n 
1 81  GLN n 
1 82  LYS n 
1 83  GLU n 
1 84  TRP n 
1 85  ILE n 
1 86  VAL n 
1 87  PHE n 
1 88  SER n 
1 89  ALA n 
1 90  GLY n 
1 91  ILE n 
1 92  VAL n 
1 93  PRO n 
1 94  ALA n 
1 95  LEU n 
1 96  SER n 
1 97  THR n 
1 98  SER n 
1 99  ILE n 
1 100 GLN n 
1 101 ALA n 
1 102 PHE n 
1 103 THR n 
1 104 LYS n 
1 105 GLU n 
1 106 ASN n 
1 107 GLU n 
1 108 SER n 
1 109 VAL n 
1 110 LEU n 
1 111 VAL n 
1 112 GLN n 
1 113 PRO n 
1 114 PRO n 
1 115 ILE n 
1 116 TYR n 
1 117 PRO n 
1 118 PRO n 
1 119 PHE n 
1 120 PHE n 
1 121 GLU n 
1 122 MET n 
1 123 VAL n 
1 124 THR n 
1 125 THR n 
1 126 ASN n 
1 127 ASN n 
1 128 ARG n 
1 129 GLN n 
1 130 LEU n 
1 131 CYS n 
1 132 VAL n 
1 133 SER n 
1 134 PRO n 
1 135 LEU n 
1 136 GLN n 
1 137 LYS n 
1 138 GLN n 
1 139 ASN n 
1 140 ASP n 
1 141 THR n 
1 142 TYR n 
1 143 VAL n 
1 144 ILE n 
1 145 ASP n 
1 146 PHE n 
1 147 LYS n 
1 148 HIS n 
1 149 LEU n 
1 150 GLU n 
1 151 LYS n 
1 152 GLN n 
1 153 PHE n 
1 154 GLN n 
1 155 GLN n 
1 156 GLY n 
1 157 ILE n 
1 158 LYS n 
1 159 LEU n 
1 160 MET n 
1 161 LEU n 
1 162 LEU n 
1 163 CYS n 
1 164 SER n 
1 165 PRO n 
1 166 HIS n 
1 167 ASN n 
1 168 PRO n 
1 169 ILE n 
1 170 GLY n 
1 171 ARG n 
1 172 VAL n 
1 173 TRP n 
1 174 THR n 
1 175 LYS n 
1 176 GLU n 
1 177 GLU n 
1 178 LEU n 
1 179 ILE n 
1 180 LYS n 
1 181 LEU n 
1 182 GLY n 
1 183 SER n 
1 184 LEU n 
1 185 CYS n 
1 186 THR n 
1 187 LYS n 
1 188 TYR n 
1 189 ASN n 
1 190 VAL n 
1 191 ILE n 
1 192 VAL n 
1 193 VAL n 
1 194 ALA n 
1 195 ASP n 
1 196 GLU n 
1 197 ILE n 
1 198 HIS n 
1 199 SER n 
1 200 ASP n 
1 201 ILE n 
1 202 ILE n 
1 203 TYR n 
1 204 ALA n 
1 205 ASP n 
1 206 HIS n 
1 207 THR n 
1 208 HIS n 
1 209 THR n 
1 210 PRO n 
1 211 PHE n 
1 212 ALA n 
1 213 SER n 
1 214 LEU n 
1 215 SER n 
1 216 GLU n 
1 217 GLU n 
1 218 LEU n 
1 219 ALA n 
1 220 GLU n 
1 221 ARG n 
1 222 THR n 
1 223 ILE n 
1 224 THR n 
1 225 CYS n 
1 226 MET n 
1 227 ALA n 
1 228 PRO n 
1 229 SER n 
1 230 LLP n 
1 231 THR n 
1 232 PHE n 
1 233 ASN n 
1 234 ILE n 
1 235 ALA n 
1 236 GLY n 
1 237 LEU n 
1 238 GLN n 
1 239 ALA n 
1 240 SER n 
1 241 ILE n 
1 242 ILE n 
1 243 ILE n 
1 244 ILE n 
1 245 PRO n 
1 246 ASN n 
1 247 GLU n 
1 248 LYS n 
1 249 LEU n 
1 250 ARG n 
1 251 HIS n 
1 252 ALA n 
1 253 PHE n 
1 254 THR n 
1 255 ALA n 
1 256 ILE n 
1 257 GLN n 
1 258 TYR n 
1 259 ARG n 
1 260 GLN n 
1 261 GLY n 
1 262 PHE n 
1 263 HIS n 
1 264 GLY n 
1 265 LEU n 
1 266 ASN n 
1 267 ILE n 
1 268 PHE n 
1 269 ALA n 
1 270 TYR n 
1 271 THR n 
1 272 ALA n 
1 273 MET n 
1 274 GLN n 
1 275 SER n 
1 276 ALA n 
1 277 TYR n 
1 278 THR n 
1 279 GLU n 
1 280 CYS n 
1 281 ASN n 
1 282 ASP n 
1 283 TRP n 
1 284 LEU n 
1 285 ASN n 
1 286 LYS n 
1 287 ILE n 
1 288 ARG n 
1 289 LEU n 
1 290 TYR n 
1 291 ILE n 
1 292 GLU n 
1 293 ASP n 
1 294 ASN n 
1 295 ALA n 
1 296 LYS n 
1 297 PHE n 
1 298 ALA n 
1 299 CYS n 
1 300 GLU n 
1 301 TYR n 
1 302 MET n 
1 303 LYS n 
1 304 ASP n 
1 305 HIS n 
1 306 ILE n 
1 307 PRO n 
1 308 THR n 
1 309 LEU n 
1 310 SER n 
1 311 VAL n 
1 312 THR n 
1 313 LYS n 
1 314 PRO n 
1 315 GLU n 
1 316 GLY n 
1 317 SER n 
1 318 PHE n 
1 319 LEU n 
1 320 LEU n 
1 321 TRP n 
1 322 ILE n 
1 323 ASP n 
1 324 CYS n 
1 325 SER n 
1 326 ALA n 
1 327 LEU n 
1 328 ASN n 
1 329 LEU n 
1 330 SER n 
1 331 GLN n 
1 332 ASP n 
1 333 GLU n 
1 334 ARG n 
1 335 THR n 
1 336 LYS n 
1 337 LEU n 
1 338 LEU n 
1 339 GLU n 
1 340 GLU n 
1 341 LYS n 
1 342 GLY n 
1 343 LYS n 
1 344 ILE n 
1 345 ILE n 
1 346 VAL n 
1 347 GLU n 
1 348 PRO n 
1 349 GLY n 
1 350 GLU n 
1 351 LYS n 
1 352 TYR n 
1 353 GLY n 
1 354 LEU n 
1 355 GLY n 
1 356 GLY n 
1 357 GLU n 
1 358 GLU n 
1 359 HIS n 
1 360 ILE n 
1 361 ARG n 
1 362 ILE n 
1 363 ASN n 
1 364 ILE n 
1 365 GLY n 
1 366 CYS n 
1 367 PRO n 
1 368 ARG n 
1 369 SER n 
1 370 VAL n 
1 371 LEU n 
1 372 GLU n 
1 373 GLU n 
1 374 ILE n 
1 375 LEU n 
1 376 ASN n 
1 377 ARG n 
1 378 LEU n 
1 379 ARG n 
1 380 HIS n 
1 381 THR n 
1 382 PHE n 
1 383 SER 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                   383 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 BK746_00885 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    'ATCC 14579' 
_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      'Bacillus cereus ATCC 14579' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     226900 
_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               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                                 
?                                               'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                                                                                
?                                               'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                              
?                                               'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                                         
?                                               'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                                                
?                                               'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                                               
?                                               'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                         
?                                               'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                                                                                                 
?                                               'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                               
?                                               'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                                                                                                   
?                                               'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                              
?                                               'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                                 
?                                               'C6 H13 N O2'     131.173 
LLP 'L-peptide linking' n '(2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid' 
"N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE"          'C14 H22 N3 O7 P' 375.314 
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 
OO0 non-polymer         n ALLIIN                                                                                                  
'2-azanyl-3-prop-2-enylsulfinyl-propanoic acid' 'C6 H11 N O3 S'   177.221 
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   GLN 2   2   ?   ?   ?   A . n 
A 1 3   LEU 3   3   ?   ?   ?   A . n 
A 1 4   PHE 4   4   ?   ?   ?   A . n 
A 1 5   HIS 5   5   ?   ?   ?   A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   ASN 9   9   9   ASN ASN A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  ARG 11  11  11  ARG ARG A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  HIS 14  14  14  HIS HIS A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  TRP 18  18  18  TRP TRP A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  ILE 27  27  27  ILE ILE A . n 
A 1 28  HIS 28  28  28  HIS HIS A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  TRP 30  30  30  TRP TRP A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  MET 34  34  34  MET MET A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  PHE 36  36  36  PHE PHE A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  PRO 41  41  41  PRO PRO 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  THR 44  44  44  THR THR A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  HIS 52  52  52  HIS HIS A . n 
A 1 53  PRO 53  53  53  PRO PRO A . n 
A 1 54  ILE 54  54  54  ILE ILE A . n 
A 1 55  PHE 55  55  55  PHE PHE A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  CYS 69  69  69  CYS CYS A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  TRP 71  71  71  TRP TRP A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  GLN 75  75  75  GLN GLN A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  TRP 78  78  78  TRP TRP A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  TRP 84  84  84  TRP TRP A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  SER 88  88  88  SER SER A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLN 100 100 100 GLN GLN A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 PHE 102 102 102 PHE PHE A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 ASN 106 106 106 ASN ASN A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 GLN 112 112 112 GLN GLN A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 PRO 114 114 114 PRO PRO A . n 
A 1 115 ILE 115 115 115 ILE ILE A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 PRO 118 118 118 PRO PRO A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 PHE 120 120 120 PHE PHE A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 MET 122 122 122 MET MET A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 ARG 128 128 128 ARG ARG A . n 
A 1 129 GLN 129 129 129 GLN GLN A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 CYS 131 131 131 CYS CYS A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 PRO 134 134 134 PRO PRO A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 TYR 142 142 142 TYR TYR A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 HIS 148 148 148 HIS HIS A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 GLN 152 152 152 GLN GLN A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 GLN 154 154 154 GLN GLN A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 MET 160 160 160 MET MET A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 CYS 163 163 163 CYS CYS A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 HIS 166 166 166 HIS HIS A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 VAL 172 172 172 VAL VAL A . n 
A 1 173 TRP 173 173 173 TRP TRP A . n 
A 1 174 THR 174 174 174 THR THR A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 GLU 176 176 176 GLU GLU A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 LYS 180 180 180 LYS LYS A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 CYS 185 185 185 CYS CYS A . n 
A 1 186 THR 186 186 186 THR THR A . n 
A 1 187 LYS 187 187 187 LYS LYS A . n 
A 1 188 TYR 188 188 ?   ?   ?   A . n 
A 1 189 ASN 189 189 ?   ?   ?   A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 ILE 191 191 191 ILE ILE A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 VAL 193 193 193 VAL VAL 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 GLU 196 196 196 GLU GLU A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 HIS 198 198 198 HIS HIS A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 ILE 202 202 202 ILE ILE A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 HIS 206 206 206 HIS HIS A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 HIS 208 208 208 HIS HIS A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 PRO 210 210 210 PRO PRO A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 GLU 216 216 216 GLU GLU A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 THR 222 222 222 THR THR A . n 
A 1 223 ILE 223 223 223 ILE ILE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 CYS 225 225 225 CYS CYS A . n 
A 1 226 MET 226 226 226 MET MET A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 PRO 228 228 228 PRO PRO A . n 
A 1 229 SER 229 229 229 SER SER A . n 
A 1 230 LLP 230 230 401 LLP PLP A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 PHE 232 232 232 PHE PHE A . n 
A 1 233 ASN 233 233 233 ASN ASN A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 ALA 235 235 235 ALA ALA A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 GLN 238 238 238 GLN GLN A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 ILE 242 242 242 ILE ILE A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 PRO 245 245 245 PRO PRO A . n 
A 1 246 ASN 246 246 246 ASN ASN A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 ARG 250 250 250 ARG ARG A . n 
A 1 251 HIS 251 251 251 HIS HIS A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 ILE 256 256 256 ILE ILE A . n 
A 1 257 GLN 257 257 257 GLN GLN A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 ARG 259 259 259 ARG ARG A . n 
A 1 260 GLN 260 260 260 GLN GLN A . n 
A 1 261 GLY 261 261 261 GLY GLY A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 HIS 263 263 263 HIS HIS A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 LEU 265 265 265 LEU LEU A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 PHE 268 268 268 PHE PHE A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 TYR 270 270 270 TYR TYR A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 MET 273 273 273 MET MET A . n 
A 1 274 GLN 274 274 274 GLN GLN A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 TYR 277 277 277 TYR TYR A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 CYS 280 280 280 CYS CYS A . n 
A 1 281 ASN 281 281 281 ASN ASN A . n 
A 1 282 ASP 282 282 282 ASP ASP A . n 
A 1 283 TRP 283 283 283 TRP TRP A . n 
A 1 284 LEU 284 284 284 LEU LEU A . n 
A 1 285 ASN 285 285 285 ASN ASN A . n 
A 1 286 LYS 286 286 286 LYS LYS A . n 
A 1 287 ILE 287 287 287 ILE ILE A . n 
A 1 288 ARG 288 288 288 ARG ARG A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 ILE 291 291 291 ILE ILE A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 ASP 293 293 293 ASP ASP A . n 
A 1 294 ASN 294 294 294 ASN ASN A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 LYS 296 296 296 LYS LYS A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 CYS 299 299 299 CYS CYS A . n 
A 1 300 GLU 300 300 300 GLU GLU A . n 
A 1 301 TYR 301 301 301 TYR TYR A . n 
A 1 302 MET 302 302 302 MET MET A . n 
A 1 303 LYS 303 303 303 LYS LYS A . n 
A 1 304 ASP 304 304 304 ASP ASP A . n 
A 1 305 HIS 305 305 305 HIS HIS A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 PRO 307 307 307 PRO PRO A . n 
A 1 308 THR 308 308 308 THR THR A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 THR 312 312 312 THR THR A . n 
A 1 313 LYS 313 313 313 LYS LYS A . n 
A 1 314 PRO 314 314 314 PRO PRO A . n 
A 1 315 GLU 315 315 315 GLU GLU A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 PHE 318 318 318 PHE PHE A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 TRP 321 321 321 TRP TRP A . n 
A 1 322 ILE 322 322 322 ILE ILE A . n 
A 1 323 ASP 323 323 323 ASP ASP A . n 
A 1 324 CYS 324 324 324 CYS CYS A . n 
A 1 325 SER 325 325 325 SER SER A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 LEU 327 327 327 LEU LEU A . n 
A 1 328 ASN 328 328 328 ASN ASN A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 GLN 331 331 331 GLN GLN A . n 
A 1 332 ASP 332 332 332 ASP ASP A . n 
A 1 333 GLU 333 333 333 GLU GLU A . n 
A 1 334 ARG 334 334 334 ARG ARG A . n 
A 1 335 THR 335 335 335 THR THR A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 LEU 337 337 337 LEU LEU A . n 
A 1 338 LEU 338 338 338 LEU LEU A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 GLU 340 340 340 GLU GLU A . n 
A 1 341 LYS 341 341 341 LYS LYS A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 LYS 343 343 343 LYS LYS A . n 
A 1 344 ILE 344 344 344 ILE ILE A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 VAL 346 346 346 VAL VAL A . n 
A 1 347 GLU 347 347 347 GLU GLU A . n 
A 1 348 PRO 348 348 348 PRO PRO A . n 
A 1 349 GLY 349 349 349 GLY GLY A . n 
A 1 350 GLU 350 350 350 GLU GLU A . n 
A 1 351 LYS 351 351 351 LYS LYS A . n 
A 1 352 TYR 352 352 352 TYR TYR A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 LEU 354 354 354 LEU LEU A . n 
A 1 355 GLY 355 355 355 GLY GLY A . n 
A 1 356 GLY 356 356 356 GLY GLY A . n 
A 1 357 GLU 357 357 357 GLU GLU A . n 
A 1 358 GLU 358 358 358 GLU GLU A . n 
A 1 359 HIS 359 359 359 HIS HIS A . n 
A 1 360 ILE 360 360 360 ILE ILE A . n 
A 1 361 ARG 361 361 361 ARG ARG A . n 
A 1 362 ILE 362 362 362 ILE ILE A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 ILE 364 364 364 ILE ILE A . n 
A 1 365 GLY 365 365 365 GLY GLY A . n 
A 1 366 CYS 366 366 366 CYS CYS A . n 
A 1 367 PRO 367 367 367 PRO PRO A . n 
A 1 368 ARG 368 368 368 ARG ARG A . n 
A 1 369 SER 369 369 369 SER SER A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 GLU 373 373 373 GLU GLU A . n 
A 1 374 ILE 374 374 374 ILE ILE A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 ASN 376 376 376 ASN ASN A . n 
A 1 377 ARG 377 377 377 ARG ARG A . n 
A 1 378 LEU 378 378 378 LEU LEU A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 HIS 380 380 380 HIS HIS A . n 
A 1 381 THR 381 381 381 THR THR A . n 
A 1 382 PHE 382 382 382 PHE PHE A . n 
A 1 383 SER 383 383 383 SER SER A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLN 2   2   ?   ?   ?   B . n 
B 1 3   LEU 3   3   ?   ?   ?   B . n 
B 1 4   PHE 4   4   ?   ?   ?   B . n 
B 1 5   HIS 5   5   ?   ?   ?   B . n 
B 1 6   LYS 6   6   6   LYS LYS B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   ILE 8   8   8   ILE ILE B . n 
B 1 9   ASN 9   9   9   ASN ASN B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  ARG 11  11  11  ARG ARG B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  HIS 14  14  14  HIS HIS B . n 
B 1 15  SER 15  15  15  SER SER B . n 
B 1 16  ILE 16  16  16  ILE ILE B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  TRP 18  18  18  TRP TRP B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  THR 20  20  20  THR THR B . n 
B 1 21  TYR 21  21  21  TYR TYR B . n 
B 1 22  LYS 22  22  22  LYS LYS B . n 
B 1 23  ASN 23  23  23  ASN ASN B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  ILE 27  27  27  ILE ILE B . n 
B 1 28  HIS 28  28  28  HIS HIS B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  TRP 30  30  30  TRP TRP B . n 
B 1 31  ILE 31  31  31  ILE ILE B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  MET 34  34  34  MET MET B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  PHE 36  36  36  PHE PHE B . n 
B 1 37  GLU 37  37  37  GLU GLU B . n 
B 1 38  VAL 38  38  38  VAL VAL B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  LYS 40  40  40  LYS LYS B . n 
B 1 41  PRO 41  41  41  PRO PRO 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  THR 44  44  44  THR THR B . n 
B 1 45  ALA 45  45  45  ALA ALA B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  LYS 47  47  47  LYS LYS B . n 
B 1 48  GLN 48  48  48  GLN GLN B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  ILE 50  50  50  ILE ILE B . n 
B 1 51  LYS 51  51  51  LYS LYS B . n 
B 1 52  HIS 52  52  52  HIS HIS B . n 
B 1 53  PRO 53  53  53  PRO PRO B . n 
B 1 54  ILE 54  54  54  ILE ILE B . n 
B 1 55  PHE 55  55  55  PHE PHE B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  TYR 57  57  57  TYR TYR B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  LEU 59  59  59  LEU LEU B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  PRO 61  61  61  PRO PRO B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  ILE 64  64  64  ILE ILE B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ILE 67  67  67  ILE ILE B . n 
B 1 68  ILE 68  68  68  ILE ILE B . n 
B 1 69  CYS 69  69  69  CYS CYS B . n 
B 1 70  ASN 70  70  70  ASN ASN B . n 
B 1 71  TRP 71  71  71  TRP TRP B . n 
B 1 72  THR 72  72  ?   ?   ?   B . n 
B 1 73  LYS 73  73  73  LYS LYS B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  GLN 75  75  75  GLN GLN B . n 
B 1 76  TYR 76  76  76  TYR TYR B . n 
B 1 77  ASP 77  77  77  ASP ASP B . n 
B 1 78  TRP 78  78  78  TRP TRP B . n 
B 1 79  ASP 79  79  79  ASP ASP B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  GLN 81  81  81  GLN GLN B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  GLU 83  83  83  GLU GLU B . n 
B 1 84  TRP 84  84  84  TRP TRP B . n 
B 1 85  ILE 85  85  85  ILE ILE B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  PHE 87  87  87  PHE PHE B . n 
B 1 88  SER 88  88  88  SER SER B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  GLY 90  90  90  GLY GLY B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  VAL 92  92  92  VAL VAL B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  THR 97  97  97  THR THR B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 GLN 100 100 100 GLN GLN B . n 
B 1 101 ALA 101 101 101 ALA ALA B . n 
B 1 102 PHE 102 102 102 PHE PHE B . n 
B 1 103 THR 103 103 103 THR THR B . n 
B 1 104 LYS 104 104 104 LYS LYS B . n 
B 1 105 GLU 105 105 105 GLU GLU B . n 
B 1 106 ASN 106 106 106 ASN ASN B . n 
B 1 107 GLU 107 107 107 GLU GLU B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 VAL 111 111 111 VAL VAL B . n 
B 1 112 GLN 112 112 112 GLN GLN B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 PRO 114 114 114 PRO PRO B . n 
B 1 115 ILE 115 115 115 ILE ILE B . n 
B 1 116 TYR 116 116 116 TYR TYR B . n 
B 1 117 PRO 117 117 117 PRO PRO B . n 
B 1 118 PRO 118 118 118 PRO PRO B . n 
B 1 119 PHE 119 119 119 PHE PHE B . n 
B 1 120 PHE 120 120 120 PHE PHE B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 MET 122 122 122 MET MET B . n 
B 1 123 VAL 123 123 123 VAL VAL B . n 
B 1 124 THR 124 124 ?   ?   ?   B . n 
B 1 125 THR 125 125 125 THR THR B . n 
B 1 126 ASN 126 126 126 ASN ASN B . n 
B 1 127 ASN 127 127 ?   ?   ?   B . n 
B 1 128 ARG 128 128 128 ARG ARG B . n 
B 1 129 GLN 129 129 129 GLN GLN B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 CYS 131 131 131 CYS CYS B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 PRO 134 134 134 PRO PRO B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 GLN 136 136 136 GLN GLN B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 GLN 138 138 138 GLN GLN B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ASP 140 140 140 ASP ASP B . n 
B 1 141 THR 141 141 141 THR THR B . n 
B 1 142 TYR 142 142 142 TYR TYR B . n 
B 1 143 VAL 143 143 143 VAL VAL B . n 
B 1 144 ILE 144 144 144 ILE ILE B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 PHE 146 146 146 PHE PHE B . n 
B 1 147 LYS 147 147 147 LYS LYS B . n 
B 1 148 HIS 148 148 148 HIS HIS B . n 
B 1 149 LEU 149 149 149 LEU LEU B . n 
B 1 150 GLU 150 150 150 GLU GLU B . n 
B 1 151 LYS 151 151 151 LYS LYS B . n 
B 1 152 GLN 152 152 152 GLN GLN B . n 
B 1 153 PHE 153 153 153 PHE PHE B . n 
B 1 154 GLN 154 154 154 GLN GLN B . n 
B 1 155 GLN 155 155 155 GLN GLN B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 ILE 157 157 157 ILE ILE B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 MET 160 160 160 MET MET B . n 
B 1 161 LEU 161 161 161 LEU LEU B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 CYS 163 163 163 CYS CYS B . n 
B 1 164 SER 164 164 164 SER SER B . n 
B 1 165 PRO 165 165 165 PRO PRO B . n 
B 1 166 HIS 166 166 166 HIS HIS B . n 
B 1 167 ASN 167 167 167 ASN ASN B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 ILE 169 169 169 ILE ILE B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 ARG 171 171 171 ARG ARG B . n 
B 1 172 VAL 172 172 172 VAL VAL B . n 
B 1 173 TRP 173 173 173 TRP TRP B . n 
B 1 174 THR 174 174 174 THR THR B . n 
B 1 175 LYS 175 175 175 LYS LYS B . n 
B 1 176 GLU 176 176 176 GLU GLU B . n 
B 1 177 GLU 177 177 177 GLU GLU B . n 
B 1 178 LEU 178 178 178 LEU LEU B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 LYS 180 180 180 LYS LYS B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 GLY 182 182 182 GLY GLY B . n 
B 1 183 SER 183 183 183 SER SER B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 CYS 185 185 185 CYS CYS B . n 
B 1 186 THR 186 186 186 THR THR B . n 
B 1 187 LYS 187 187 187 LYS LYS B . n 
B 1 188 TYR 188 188 188 TYR TYR B . n 
B 1 189 ASN 189 189 189 ASN ASN B . n 
B 1 190 VAL 190 190 190 VAL VAL B . n 
B 1 191 ILE 191 191 191 ILE ILE B . n 
B 1 192 VAL 192 192 192 VAL VAL B . n 
B 1 193 VAL 193 193 193 VAL VAL 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 GLU 196 196 196 GLU GLU B . n 
B 1 197 ILE 197 197 197 ILE ILE B . n 
B 1 198 HIS 198 198 198 HIS HIS B . n 
B 1 199 SER 199 199 199 SER SER B . n 
B 1 200 ASP 200 200 200 ASP ASP B . n 
B 1 201 ILE 201 201 201 ILE ILE B . n 
B 1 202 ILE 202 202 202 ILE ILE B . n 
B 1 203 TYR 203 203 203 TYR TYR B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 ASP 205 205 205 ASP ASP B . n 
B 1 206 HIS 206 206 206 HIS HIS B . n 
B 1 207 THR 207 207 207 THR THR B . n 
B 1 208 HIS 208 208 208 HIS HIS B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 PRO 210 210 210 PRO PRO B . n 
B 1 211 PHE 211 211 211 PHE PHE B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 SER 213 213 213 SER SER B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 GLU 216 216 216 GLU GLU B . n 
B 1 217 GLU 217 217 217 GLU GLU B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 ALA 219 219 219 ALA ALA B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 ARG 221 221 221 ARG ARG B . n 
B 1 222 THR 222 222 222 THR THR B . n 
B 1 223 ILE 223 223 223 ILE ILE B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 CYS 225 225 225 CYS CYS B . n 
B 1 226 MET 226 226 226 MET MET B . n 
B 1 227 ALA 227 227 227 ALA ALA B . n 
B 1 228 PRO 228 228 228 PRO PRO B . n 
B 1 229 SER 229 229 229 SER SER B . n 
B 1 230 LLP 230 230 401 LLP PLP B . n 
B 1 231 THR 231 231 231 THR THR B . n 
B 1 232 PHE 232 232 232 PHE PHE B . n 
B 1 233 ASN 233 233 233 ASN ASN B . n 
B 1 234 ILE 234 234 234 ILE ILE B . n 
B 1 235 ALA 235 235 235 ALA ALA B . n 
B 1 236 GLY 236 236 236 GLY GLY B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 GLN 238 238 238 GLN GLN B . n 
B 1 239 ALA 239 239 239 ALA ALA B . n 
B 1 240 SER 240 240 240 SER SER B . n 
B 1 241 ILE 241 241 241 ILE ILE B . n 
B 1 242 ILE 242 242 242 ILE ILE B . n 
B 1 243 ILE 243 243 243 ILE ILE B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 PRO 245 245 245 PRO PRO B . n 
B 1 246 ASN 246 246 246 ASN ASN B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 LYS 248 248 248 LYS LYS B . n 
B 1 249 LEU 249 249 249 LEU LEU B . n 
B 1 250 ARG 250 250 250 ARG ARG B . n 
B 1 251 HIS 251 251 251 HIS HIS B . n 
B 1 252 ALA 252 252 252 ALA ALA B . n 
B 1 253 PHE 253 253 253 PHE PHE B . n 
B 1 254 THR 254 254 254 THR THR B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 ILE 256 256 256 ILE ILE B . n 
B 1 257 GLN 257 257 257 GLN GLN B . n 
B 1 258 TYR 258 258 258 TYR TYR B . n 
B 1 259 ARG 259 259 259 ARG ARG B . n 
B 1 260 GLN 260 260 260 GLN GLN B . n 
B 1 261 GLY 261 261 261 GLY GLY B . n 
B 1 262 PHE 262 262 262 PHE PHE B . n 
B 1 263 HIS 263 263 263 HIS HIS B . n 
B 1 264 GLY 264 264 264 GLY GLY B . n 
B 1 265 LEU 265 265 265 LEU LEU B . n 
B 1 266 ASN 266 266 266 ASN ASN B . n 
B 1 267 ILE 267 267 267 ILE ILE B . n 
B 1 268 PHE 268 268 268 PHE PHE B . n 
B 1 269 ALA 269 269 269 ALA ALA B . n 
B 1 270 TYR 270 270 270 TYR TYR B . n 
B 1 271 THR 271 271 271 THR THR B . n 
B 1 272 ALA 272 272 272 ALA ALA B . n 
B 1 273 MET 273 273 273 MET MET B . n 
B 1 274 GLN 274 274 274 GLN GLN B . n 
B 1 275 SER 275 275 275 SER SER B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 TYR 277 277 277 TYR TYR B . n 
B 1 278 THR 278 278 278 THR THR B . n 
B 1 279 GLU 279 279 279 GLU GLU B . n 
B 1 280 CYS 280 280 280 CYS CYS B . n 
B 1 281 ASN 281 281 281 ASN ASN B . n 
B 1 282 ASP 282 282 282 ASP ASP B . n 
B 1 283 TRP 283 283 283 TRP TRP B . n 
B 1 284 LEU 284 284 284 LEU LEU B . n 
B 1 285 ASN 285 285 285 ASN ASN B . n 
B 1 286 LYS 286 286 286 LYS LYS B . n 
B 1 287 ILE 287 287 287 ILE ILE B . n 
B 1 288 ARG 288 288 288 ARG ARG B . n 
B 1 289 LEU 289 289 289 LEU LEU B . n 
B 1 290 TYR 290 290 290 TYR TYR B . n 
B 1 291 ILE 291 291 291 ILE ILE B . n 
B 1 292 GLU 292 292 292 GLU GLU B . n 
B 1 293 ASP 293 293 293 ASP ASP B . n 
B 1 294 ASN 294 294 294 ASN ASN B . n 
B 1 295 ALA 295 295 295 ALA ALA B . n 
B 1 296 LYS 296 296 296 LYS LYS B . n 
B 1 297 PHE 297 297 297 PHE PHE B . n 
B 1 298 ALA 298 298 298 ALA ALA B . n 
B 1 299 CYS 299 299 299 CYS CYS B . n 
B 1 300 GLU 300 300 300 GLU GLU B . n 
B 1 301 TYR 301 301 301 TYR TYR B . n 
B 1 302 MET 302 302 302 MET MET B . n 
B 1 303 LYS 303 303 303 LYS LYS B . n 
B 1 304 ASP 304 304 304 ASP ASP B . n 
B 1 305 HIS 305 305 305 HIS HIS B . n 
B 1 306 ILE 306 306 306 ILE ILE B . n 
B 1 307 PRO 307 307 307 PRO PRO B . n 
B 1 308 THR 308 308 308 THR THR B . n 
B 1 309 LEU 309 309 309 LEU LEU B . n 
B 1 310 SER 310 310 310 SER SER B . n 
B 1 311 VAL 311 311 311 VAL VAL B . n 
B 1 312 THR 312 312 312 THR THR B . n 
B 1 313 LYS 313 313 313 LYS LYS B . n 
B 1 314 PRO 314 314 314 PRO PRO B . n 
B 1 315 GLU 315 315 315 GLU GLU B . n 
B 1 316 GLY 316 316 316 GLY GLY B . n 
B 1 317 SER 317 317 ?   ?   ?   B . n 
B 1 318 PHE 318 318 318 PHE PHE B . n 
B 1 319 LEU 319 319 319 LEU LEU B . n 
B 1 320 LEU 320 320 320 LEU LEU B . n 
B 1 321 TRP 321 321 321 TRP TRP B . n 
B 1 322 ILE 322 322 322 ILE ILE B . n 
B 1 323 ASP 323 323 323 ASP ASP B . n 
B 1 324 CYS 324 324 324 CYS CYS B . n 
B 1 325 SER 325 325 325 SER SER B . n 
B 1 326 ALA 326 326 326 ALA ALA B . n 
B 1 327 LEU 327 327 327 LEU LEU B . n 
B 1 328 ASN 328 328 328 ASN ASN B . n 
B 1 329 LEU 329 329 329 LEU LEU B . n 
B 1 330 SER 330 330 330 SER SER B . n 
B 1 331 GLN 331 331 331 GLN GLN B . n 
B 1 332 ASP 332 332 332 ASP ASP B . n 
B 1 333 GLU 333 333 333 GLU GLU B . n 
B 1 334 ARG 334 334 334 ARG ARG B . n 
B 1 335 THR 335 335 335 THR THR B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 LEU 337 337 337 LEU LEU B . n 
B 1 338 LEU 338 338 338 LEU LEU B . n 
B 1 339 GLU 339 339 339 GLU GLU B . n 
B 1 340 GLU 340 340 340 GLU GLU B . n 
B 1 341 LYS 341 341 341 LYS LYS B . n 
B 1 342 GLY 342 342 342 GLY GLY B . n 
B 1 343 LYS 343 343 343 LYS LYS B . n 
B 1 344 ILE 344 344 344 ILE ILE B . n 
B 1 345 ILE 345 345 345 ILE ILE B . n 
B 1 346 VAL 346 346 346 VAL VAL B . n 
B 1 347 GLU 347 347 347 GLU GLU B . n 
B 1 348 PRO 348 348 348 PRO PRO B . n 
B 1 349 GLY 349 349 349 GLY GLY B . n 
B 1 350 GLU 350 350 350 GLU GLU B . n 
B 1 351 LYS 351 351 351 LYS LYS B . n 
B 1 352 TYR 352 352 352 TYR TYR B . n 
B 1 353 GLY 353 353 353 GLY GLY B . n 
B 1 354 LEU 354 354 354 LEU LEU B . n 
B 1 355 GLY 355 355 355 GLY GLY B . n 
B 1 356 GLY 356 356 356 GLY GLY B . n 
B 1 357 GLU 357 357 357 GLU GLU B . n 
B 1 358 GLU 358 358 358 GLU GLU B . n 
B 1 359 HIS 359 359 359 HIS HIS B . n 
B 1 360 ILE 360 360 360 ILE ILE B . n 
B 1 361 ARG 361 361 361 ARG ARG B . n 
B 1 362 ILE 362 362 362 ILE ILE B . n 
B 1 363 ASN 363 363 363 ASN ASN B . n 
B 1 364 ILE 364 364 364 ILE ILE B . n 
B 1 365 GLY 365 365 365 GLY GLY B . n 
B 1 366 CYS 366 366 366 CYS CYS B . n 
B 1 367 PRO 367 367 367 PRO PRO B . n 
B 1 368 ARG 368 368 368 ARG ARG B . n 
B 1 369 SER 369 369 369 SER SER B . n 
B 1 370 VAL 370 370 370 VAL VAL B . n 
B 1 371 LEU 371 371 371 LEU LEU B . n 
B 1 372 GLU 372 372 372 GLU GLU B . n 
B 1 373 GLU 373 373 373 GLU GLU B . n 
B 1 374 ILE 374 374 374 ILE ILE B . n 
B 1 375 LEU 375 375 375 LEU LEU B . n 
B 1 376 ASN 376 376 376 ASN ASN B . n 
B 1 377 ARG 377 377 377 ARG ARG B . n 
B 1 378 LEU 378 378 378 LEU LEU B . n 
B 1 379 ARG 379 379 379 ARG ARG B . n 
B 1 380 HIS 380 380 380 HIS HIS B . n 
B 1 381 THR 381 381 381 THR THR B . n 
B 1 382 PHE 382 382 382 PHE PHE B . n 
B 1 383 SER 383 383 383 SER SER B . n 
# 
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 OO0 1  401 402 OO0 LIG A . 
D 3 HOH 1  501 87  HOH HOH A . 
D 3 HOH 2  502 65  HOH HOH A . 
D 3 HOH 3  503 7   HOH HOH A . 
D 3 HOH 4  504 9   HOH HOH A . 
D 3 HOH 5  505 19  HOH HOH A . 
D 3 HOH 6  506 24  HOH HOH A . 
D 3 HOH 7  507 82  HOH HOH A . 
D 3 HOH 8  508 88  HOH HOH A . 
D 3 HOH 9  509 17  HOH HOH A . 
D 3 HOH 10 510 48  HOH HOH A . 
D 3 HOH 11 511 61  HOH HOH A . 
D 3 HOH 12 512 4   HOH HOH A . 
D 3 HOH 13 513 56  HOH HOH A . 
D 3 HOH 14 514 86  HOH HOH A . 
D 3 HOH 15 515 39  HOH HOH A . 
D 3 HOH 16 516 72  HOH HOH A . 
D 3 HOH 17 517 3   HOH HOH A . 
D 3 HOH 18 518 96  HOH HOH A . 
D 3 HOH 19 519 55  HOH HOH A . 
D 3 HOH 20 520 91  HOH HOH A . 
D 3 HOH 21 521 84  HOH HOH A . 
D 3 HOH 22 522 62  HOH HOH A . 
D 3 HOH 23 523 60  HOH HOH A . 
D 3 HOH 24 524 26  HOH HOH A . 
D 3 HOH 25 525 30  HOH HOH A . 
D 3 HOH 26 526 80  HOH HOH A . 
D 3 HOH 27 527 2   HOH HOH A . 
D 3 HOH 28 528 40  HOH HOH A . 
D 3 HOH 29 529 37  HOH HOH A . 
D 3 HOH 30 530 103 HOH HOH A . 
D 3 HOH 31 531 16  HOH HOH A . 
D 3 HOH 32 532 28  HOH HOH A . 
D 3 HOH 33 533 64  HOH HOH A . 
D 3 HOH 34 534 100 HOH HOH A . 
D 3 HOH 35 535 44  HOH HOH A . 
D 3 HOH 36 536 49  HOH HOH A . 
D 3 HOH 37 537 83  HOH HOH A . 
D 3 HOH 38 538 5   HOH HOH A . 
D 3 HOH 39 539 42  HOH HOH A . 
D 3 HOH 40 540 10  HOH HOH A . 
D 3 HOH 41 541 13  HOH HOH A . 
D 3 HOH 42 542 47  HOH HOH A . 
D 3 HOH 43 543 12  HOH HOH A . 
D 3 HOH 44 544 53  HOH HOH A . 
D 3 HOH 45 545 20  HOH HOH A . 
D 3 HOH 46 546 81  HOH HOH A . 
D 3 HOH 47 547 36  HOH HOH A . 
D 3 HOH 48 548 33  HOH HOH A . 
D 3 HOH 49 549 75  HOH HOH A . 
D 3 HOH 50 550 101 HOH HOH A . 
D 3 HOH 51 551 32  HOH HOH A . 
D 3 HOH 52 552 98  HOH HOH A . 
D 3 HOH 53 553 8   HOH HOH A . 
D 3 HOH 54 554 18  HOH HOH A . 
E 3 HOH 1  401 79  HOH HOH B . 
E 3 HOH 2  402 46  HOH HOH B . 
E 3 HOH 3  403 14  HOH HOH B . 
E 3 HOH 4  404 97  HOH HOH B . 
E 3 HOH 5  405 58  HOH HOH B . 
E 3 HOH 6  406 31  HOH HOH B . 
E 3 HOH 7  407 95  HOH HOH B . 
E 3 HOH 8  408 76  HOH HOH B . 
E 3 HOH 9  409 93  HOH HOH B . 
E 3 HOH 10 410 71  HOH HOH B . 
E 3 HOH 11 411 57  HOH HOH B . 
E 3 HOH 12 412 52  HOH HOH B . 
E 3 HOH 13 413 106 HOH HOH B . 
E 3 HOH 14 414 66  HOH HOH B . 
E 3 HOH 15 415 67  HOH HOH B . 
E 3 HOH 16 416 107 HOH HOH B . 
E 3 HOH 17 417 94  HOH HOH B . 
E 3 HOH 18 418 29  HOH HOH B . 
E 3 HOH 19 419 38  HOH HOH B . 
E 3 HOH 20 420 23  HOH HOH B . 
E 3 HOH 21 421 74  HOH HOH B . 
E 3 HOH 22 422 41  HOH HOH B . 
E 3 HOH 23 423 85  HOH HOH B . 
E 3 HOH 24 424 89  HOH HOH B . 
E 3 HOH 25 425 69  HOH HOH B . 
E 3 HOH 26 426 92  HOH HOH B . 
E 3 HOH 27 427 73  HOH HOH B . 
E 3 HOH 28 428 25  HOH HOH B . 
E 3 HOH 29 429 11  HOH HOH B . 
E 3 HOH 30 430 102 HOH HOH B . 
E 3 HOH 31 431 51  HOH HOH B . 
E 3 HOH 32 432 21  HOH HOH B . 
E 3 HOH 33 433 35  HOH HOH B . 
E 3 HOH 34 434 22  HOH HOH B . 
E 3 HOH 35 435 105 HOH HOH B . 
E 3 HOH 36 436 104 HOH HOH B . 
E 3 HOH 37 437 45  HOH HOH B . 
E 3 HOH 38 438 59  HOH HOH B . 
E 3 HOH 39 439 99  HOH HOH B . 
E 3 HOH 40 440 34  HOH HOH B . 
E 3 HOH 41 441 43  HOH HOH B . 
E 3 HOH 42 442 54  HOH HOH B . 
E 3 HOH 43 443 70  HOH HOH B . 
E 3 HOH 44 444 78  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   ? ? ? 1.16 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.12 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KAU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     53.223 
_cell.length_a_esd                 ? 
_cell.length_b                     85.522 
_cell.length_b_esd                 ? 
_cell.length_c                     168.077 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9KAU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9KAU 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.2 M Magnesium formate dihydrate 
(15-25 % w/v) Polyethylene glycol 3350
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-25 
_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   0.997 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.997 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KAU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.88 
_reflns.d_resolution_low                               168.05 
_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                                     119803 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.0 
_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                                0.145 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_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                                    1.88 
_reflns_shell.d_res_low                                     1.98 
_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                             15330 
_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                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.415 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9KAU 
_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                            1.88 
_refine.ls_d_res_low                             35.46 
_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                     119563 
_refine.ls_number_reflns_R_free                  1993 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.8 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.3931 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.3594 
_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                    ? 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_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             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_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                            ? 
_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                       1.88 
_refine_hist.d_res_low                        35.46 
_refine_hist.number_atoms_solvent             98 
_refine_hist.number_atoms_total               6217 
_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        6078 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         41 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.88 
_refine_ls_shell.d_res_low                        1.95 
_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             4871 
_refine_ls_shell.percent_reflns_obs               95.6 
_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                  0.3594 
_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                  0.3931 
# 
_struct.entry_id                     9KAU 
_struct.title                        
'Three-dimensional structure of homo-dimer of cystathione beta lyase/PLP/+L-alliin complex from Bacillus cereus(BcPatB)' 
_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        9KAU 
_struct_keywords.text            'C-S cleavage reaction, L-cysteine-S-conjugate, BIOSYNTHETIC PROTEIN' 
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A9X6FDP0_BACTU 
_struct_ref.pdbx_db_accession          A0A9X6FDP0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MQLFHKAINRRGTHSIKWDTYKNEELIHAWIADMDFEVPKPIQTALKQRIEHPIFGYTLPPENIGDIICNWTKQQYDWDI
QKEWIVFSAGIVPALSTSIQAFTKENESVLVQPPIYPPFFEMVTTNNRQLCVSPLQKQNDTYVIDFKHLEKQFQQGIKLM
LLCSPHNPIGRVWTKEELVQLGSLCTKYDVIVVADEIHSDIIYADHTHTPFASLSEELAERTITCMAPSKTFNIAGLQAS
IIIIPNEKLRHAFTAIQYRQGFHGLNIFAYTAMQSAYTECNDWLNEIRLYIEDNAQFACEYIKTHIPALSVTKPEGSFLL
WIDCSRLKLSQNERTALLEEKGKIIVEPGEKYGLGGEEHIRINIGCPRSVLEEILNRLRHTFS
;
_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 9KAU A 1 ? 383 ? A0A9X6FDP0 1 ? 383 ? 1 383 
2 1 9KAU B 1 ? 383 ? A0A9X6FDP0 1 ? 383 ? 1 383 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9KAU LYS A 51  ? UNP A0A9X6FDP0 GLU 51  'engineered mutation' 51  1  
1 9KAU ILE A 179 ? UNP A0A9X6FDP0 VAL 179 'engineered mutation' 179 2  
1 9KAU LYS A 180 ? UNP A0A9X6FDP0 GLN 180 'engineered mutation' 180 3  
1 9KAU ASN A 189 ? UNP A0A9X6FDP0 ASP 189 'engineered mutation' 189 4  
1 9KAU LYS A 286 ? UNP A0A9X6FDP0 GLU 286 'engineered mutation' 286 5  
1 9KAU LYS A 296 ? UNP A0A9X6FDP0 GLN 296 'engineered mutation' 296 6  
1 9KAU MET A 302 ? UNP A0A9X6FDP0 ILE 302 'engineered mutation' 302 7  
1 9KAU ASP A 304 ? UNP A0A9X6FDP0 THR 304 'engineered mutation' 304 8  
1 9KAU THR A 308 ? UNP A0A9X6FDP0 ALA 308 'engineered mutation' 308 9  
1 9KAU ALA A 326 ? UNP A0A9X6FDP0 ARG 326 'engineered mutation' 326 10 
1 9KAU ASN A 328 ? UNP A0A9X6FDP0 LYS 328 'engineered mutation' 328 11 
1 9KAU ASP A 332 ? UNP A0A9X6FDP0 ASN 332 'engineered mutation' 332 12 
1 9KAU LYS A 336 ? UNP A0A9X6FDP0 ALA 336 'engineered mutation' 336 13 
2 9KAU LYS B 51  ? UNP A0A9X6FDP0 GLU 51  'engineered mutation' 51  14 
2 9KAU ILE B 179 ? UNP A0A9X6FDP0 VAL 179 'engineered mutation' 179 15 
2 9KAU LYS B 180 ? UNP A0A9X6FDP0 GLN 180 'engineered mutation' 180 16 
2 9KAU ASN B 189 ? UNP A0A9X6FDP0 ASP 189 'engineered mutation' 189 17 
2 9KAU LYS B 286 ? UNP A0A9X6FDP0 GLU 286 'engineered mutation' 286 18 
2 9KAU LYS B 296 ? UNP A0A9X6FDP0 GLN 296 'engineered mutation' 296 19 
2 9KAU MET B 302 ? UNP A0A9X6FDP0 ILE 302 'engineered mutation' 302 20 
2 9KAU ASP B 304 ? UNP A0A9X6FDP0 THR 304 'engineered mutation' 304 21 
2 9KAU THR B 308 ? UNP A0A9X6FDP0 ALA 308 'engineered mutation' 308 22 
2 9KAU ALA B 326 ? UNP A0A9X6FDP0 ARG 326 'engineered mutation' 326 23 
2 9KAU ASN B 328 ? UNP A0A9X6FDP0 LYS 328 'engineered mutation' 328 24 
2 9KAU ASP B 332 ? UNP A0A9X6FDP0 ASN 332 'engineered mutation' 332 25 
2 9KAU LYS B 336 ? UNP A0A9X6FDP0 ALA 336 'engineered mutation' 336 26 
# 
_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)' 4910  ? 
1 MORE         -34   ? 
1 'SSA (A^2)'  28820 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 15  ? THR A 20  ? SER A 15  THR A 20  1 ? 6  
HELX_P HELX_P2  AA2 PRO A 39  ? LYS A 51  ? PRO A 39  LYS A 51  1 ? 13 
HELX_P HELX_P3  AA3 ASN A 63  ? ASP A 77  ? ASN A 63  ASP A 77  1 ? 15 
HELX_P HELX_P4  AA4 GLN A 81  ? GLU A 83  ? GLN A 81  GLU A 83  5 ? 3  
HELX_P HELX_P5  AA5 GLY A 90  ? THR A 103 ? GLY A 90  THR A 103 1 ? 14 
HELX_P HELX_P6  AA6 PRO A 117 ? ASN A 126 ? PRO A 117 ASN A 126 1 ? 10 
HELX_P HELX_P7  AA7 ASP A 145 ? GLN A 154 ? ASP A 145 GLN A 154 1 ? 10 
HELX_P HELX_P8  AA8 THR A 174 ? LYS A 187 ? THR A 174 LYS A 187 1 ? 14 
HELX_P HELX_P9  AA9 SER A 215 ? GLU A 220 ? SER A 215 GLU A 220 1 ? 6  
HELX_P HELX_P10 AB1 ASN A 246 ? ARG A 259 ? ASN A 246 ARG A 259 1 ? 14 
HELX_P HELX_P11 AB2 ASN A 266 ? TYR A 277 ? ASN A 266 TYR A 277 1 ? 12 
HELX_P HELX_P12 AB3 CYS A 280 ? HIS A 305 ? CYS A 280 HIS A 305 1 ? 26 
HELX_P HELX_P13 AB4 SER A 325 ? ASN A 328 ? SER A 325 ASN A 328 5 ? 4  
HELX_P HELX_P14 AB5 SER A 330 ? LYS A 341 ? SER A 330 LYS A 341 1 ? 12 
HELX_P HELX_P15 AB6 GLU A 350 ? GLY A 353 ? GLU A 350 GLY A 353 5 ? 4  
HELX_P HELX_P16 AB7 PRO A 367 ? SER A 383 ? PRO A 367 SER A 383 1 ? 17 
HELX_P HELX_P17 AB8 SER B 15  ? THR B 20  ? SER B 15  THR B 20  1 ? 6  
HELX_P HELX_P18 AB9 PRO B 39  ? LYS B 51  ? PRO B 39  LYS B 51  1 ? 13 
HELX_P HELX_P19 AC1 ASN B 63  ? TRP B 71  ? ASN B 63  TRP B 71  1 ? 9  
HELX_P HELX_P20 AC2 LYS B 73  ? GLN B 75  ? LYS B 73  GLN B 75  5 ? 3  
HELX_P HELX_P21 AC3 GLN B 81  ? GLU B 83  ? GLN B 81  GLU B 83  5 ? 3  
HELX_P HELX_P22 AC4 GLY B 90  ? THR B 103 ? GLY B 90  THR B 103 1 ? 14 
HELX_P HELX_P23 AC5 TYR B 116 ? VAL B 123 ? TYR B 116 VAL B 123 1 ? 8  
HELX_P HELX_P24 AC6 ASP B 145 ? GLN B 154 ? ASP B 145 GLN B 154 1 ? 10 
HELX_P HELX_P25 AC7 THR B 174 ? ASN B 189 ? THR B 174 ASN B 189 1 ? 16 
HELX_P HELX_P26 AC8 PRO B 210 ? LEU B 214 ? PRO B 210 LEU B 214 5 ? 5  
HELX_P HELX_P27 AC9 SER B 215 ? GLU B 220 ? SER B 215 GLU B 220 1 ? 6  
HELX_P HELX_P28 AD1 ASN B 246 ? ARG B 259 ? ASN B 246 ARG B 259 1 ? 14 
HELX_P HELX_P29 AD2 ASN B 266 ? TYR B 277 ? ASN B 266 TYR B 277 1 ? 12 
HELX_P HELX_P30 AD3 CYS B 280 ? ILE B 306 ? CYS B 280 ILE B 306 1 ? 27 
HELX_P HELX_P31 AD4 SER B 325 ? ASN B 328 ? SER B 325 ASN B 328 5 ? 4  
HELX_P HELX_P32 AD5 SER B 330 ? LYS B 341 ? SER B 330 LYS B 341 1 ? 12 
HELX_P HELX_P33 AD6 GLU B 350 ? GLY B 353 ? GLU B 350 GLY B 353 5 ? 4  
HELX_P HELX_P34 AD7 PRO B 367 ? SER B 383 ? PRO B 367 SER B 383 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A SER 229 C ? ? ? 1_555 A LLP 230 N ? ? A SER 229 A LLP 230 1_555 ? ? ? ? ? ? ? 1.325 ? ? 
covale2 covale both ? A LLP 230 C ? ? ? 1_555 A THR 231 N ? ? A LLP 230 A THR 231 1_555 ? ? ? ? ? ? ? 1.340 ? ? 
covale3 covale both ? B SER 229 C ? ? ? 1_555 B LLP 230 N ? ? B SER 229 B LLP 230 1_555 ? ? ? ? ? ? ? 1.336 ? ? 
covale4 covale both ? B LLP 230 C ? ? ? 1_555 B THR 231 N ? ? B LLP 230 B THR 231 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 LLP A 230 ? . . . . LLP A 230 ? 1_555 . . . . . . . LYS 1 LLP 'Pyridoxal phosphate' 'Named protein modification' 
2 LLP B 230 ? . . . . LLP B 230 ? 1_555 . . . . . . . LYS 1 LLP 'Pyridoxal phosphate' 'Named protein modification' 
# 
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 PRO 113 A . ? PRO 113 A PRO 114 A ? PRO 114 A 1 0.04  
2 SER 164 A . ? SER 164 A PRO 165 A ? PRO 165 A 1 -3.14 
3 ASN 167 A . ? ASN 167 A PRO 168 A ? PRO 168 A 1 13.08 
4 PRO 113 B . ? PRO 113 B PRO 114 B ? PRO 114 B 1 1.74  
5 SER 164 B . ? SER 164 B PRO 165 B ? PRO 165 B 1 2.01  
6 ASN 167 B . ? ASN 167 B PRO 168 B ? PRO 168 B 1 10.68 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
AA6 ? 7 ? 
AA7 ? 2 ? 
AA8 ? 4 ? 
# 
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 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? parallel      
AA6 6 7 ? parallel      
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? 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 ILE A 27  ? HIS A 28  ? ILE A 27  HIS A 28  
AA1 2 ILE A 344 ? ILE A 345 ? ILE A 344 ILE A 345 
AA2 1 ILE A 85  ? SER A 88  ? ILE A 85  SER A 88  
AA2 2 SER A 240 ? ILE A 243 ? SER A 240 ILE A 243 
AA2 3 THR A 222 ? MET A 226 ? THR A 222 MET A 226 
AA2 4 ILE A 191 ? ASP A 195 ? ILE A 191 ASP A 195 
AA2 5 LEU A 159 ? CYS A 163 ? LEU A 159 CYS A 163 
AA2 6 SER A 108 ? VAL A 111 ? SER A 108 VAL A 111 
AA2 7 GLN A 129 ? VAL A 132 ? GLN A 129 VAL A 132 
AA3 1 GLN A 136 ? GLN A 138 ? GLN A 136 GLN A 138 
AA3 2 THR A 141 ? VAL A 143 ? THR A 141 VAL A 143 
AA4 1 SER A 310 ? THR A 312 ? SER A 310 THR A 312 
AA4 2 LEU A 319 ? ASP A 323 ? LEU A 319 ASP A 323 
AA4 3 HIS A 359 ? ASN A 363 ? HIS A 359 ASN A 363 
AA4 4 GLU A 347 ? PRO A 348 ? GLU A 347 PRO A 348 
AA5 1 ILE B 27  ? HIS B 28  ? ILE B 27  HIS B 28  
AA5 2 ILE B 344 ? ILE B 345 ? ILE B 344 ILE B 345 
AA6 1 ILE B 85  ? SER B 88  ? ILE B 85  SER B 88  
AA6 2 SER B 240 ? ILE B 243 ? SER B 240 ILE B 243 
AA6 3 THR B 222 ? MET B 226 ? THR B 222 MET B 226 
AA6 4 ILE B 191 ? ASP B 195 ? ILE B 191 ASP B 195 
AA6 5 LEU B 159 ? CYS B 163 ? LEU B 159 CYS B 163 
AA6 6 SER B 108 ? VAL B 111 ? SER B 108 VAL B 111 
AA6 7 GLN B 129 ? VAL B 132 ? GLN B 129 VAL B 132 
AA7 1 GLN B 136 ? GLN B 138 ? GLN B 136 GLN B 138 
AA7 2 THR B 141 ? VAL B 143 ? THR B 141 VAL B 143 
AA8 1 SER B 310 ? THR B 312 ? SER B 310 THR B 312 
AA8 2 LEU B 319 ? ASP B 323 ? LEU B 319 ASP B 323 
AA8 3 HIS B 359 ? ASN B 363 ? HIS B 359 ASN B 363 
AA8 4 GLU B 347 ? PRO B 348 ? GLU B 347 PRO B 348 
# 
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 27  ? N ILE A 27  O ILE A 345 ? O ILE A 345 
AA2 1 2 N VAL A 86  ? N VAL A 86  O ILE A 242 ? O ILE A 242 
AA2 2 3 O ILE A 241 ? O ILE A 241 N MET A 226 ? N MET A 226 
AA2 3 4 O ILE A 223 ? O ILE A 223 N ALA A 194 ? N ALA A 194 
AA2 4 5 O ASP A 195 ? O ASP A 195 N LEU A 162 ? N LEU A 162 
AA2 5 6 O LEU A 161 ? O LEU A 161 N LEU A 110 ? N LEU A 110 
AA2 6 7 N VAL A 109 ? N VAL A 109 O CYS A 131 ? O CYS A 131 
AA3 1 2 N GLN A 138 ? N GLN A 138 O THR A 141 ? O THR A 141 
AA4 1 2 N SER A 310 ? N SER A 310 O ASP A 323 ? O ASP A 323 
AA4 2 3 N ILE A 322 ? N ILE A 322 O ILE A 360 ? O ILE A 360 
AA4 3 4 O ARG A 361 ? O ARG A 361 N GLU A 347 ? N GLU A 347 
AA5 1 2 N ILE B 27  ? N ILE B 27  O ILE B 345 ? O ILE B 345 
AA6 1 2 N VAL B 86  ? N VAL B 86  O ILE B 242 ? O ILE B 242 
AA6 2 3 O ILE B 243 ? O ILE B 243 N THR B 224 ? N THR B 224 
AA6 3 4 O CYS B 225 ? O CYS B 225 N ALA B 194 ? N ALA B 194 
AA6 4 5 O ASP B 195 ? O ASP B 195 N LEU B 162 ? N LEU B 162 
AA6 5 6 O LEU B 161 ? O LEU B 161 N LEU B 110 ? N LEU B 110 
AA6 6 7 N VAL B 109 ? N VAL B 109 O GLN B 129 ? O GLN B 129 
AA7 1 2 N GLN B 136 ? N GLN B 136 O VAL B 143 ? O VAL B 143 
AA8 1 2 N SER B 310 ? N SER B 310 O ASP B 323 ? O ASP B 323 
AA8 2 3 N LEU B 320 ? N LEU B 320 O ILE B 362 ? O ILE B 362 
AA8 3 4 O ARG B 361 ? O ARG B 361 N GLU B 347 ? N GLU B 347 
# 
_pdbx_entry_details.entry_id                   9KAU 
_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     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 29  ? ? -143.61 33.62   
2  1 TRP A 30  ? ? -95.99  -63.06  
3  1 ALA A 32  ? ? -92.63  52.85   
4  1 ASP A 35  ? ? -97.10  39.23   
5  1 TYR A 116 ? ? -36.51  122.05  
6  1 GLU A 196 ? ? -107.08 42.81   
7  1 GLN A 238 ? ? 62.25   61.34   
8  1 SER A 317 ? ? 59.29   -144.59 
9  1 PHE A 318 ? ? -146.37 33.34   
10 1 HIS B 14  ? ? 57.42   16.28   
11 1 ALA B 29  ? ? -145.08 32.40   
12 1 TRP B 30  ? ? -97.82  -62.95  
13 1 ALA B 32  ? ? -90.44  55.59   
14 1 ASP B 35  ? ? -97.06  41.22   
15 1 PRO B 53  ? ? -76.53  44.49   
16 1 TYR B 116 ? ? -38.89  122.03  
17 1 GLU B 196 ? ? -105.95 44.71   
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A LLP 230 A LLP 230 ? LYS 'modified residue' 
2 B LLP 230 B LLP 230 ? LYS 'modified residue' 
# 
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 GLN 2   ? A GLN 2   
3  1 Y 1 A LEU 3   ? A LEU 3   
4  1 Y 1 A PHE 4   ? A PHE 4   
5  1 Y 1 A HIS 5   ? A HIS 5   
6  1 Y 1 A TYR 188 ? A TYR 188 
7  1 Y 1 A ASN 189 ? A ASN 189 
8  1 Y 1 B MET 1   ? B MET 1   
9  1 Y 1 B GLN 2   ? B GLN 2   
10 1 Y 1 B LEU 3   ? B LEU 3   
11 1 Y 1 B PHE 4   ? B PHE 4   
12 1 Y 1 B HIS 5   ? B HIS 5   
13 1 Y 1 B THR 72  ? B THR 72  
14 1 Y 1 B THR 124 ? B THR 124 
15 1 Y 1 B ASN 127 ? B ASN 127 
16 1 Y 1 B SER 317 ? B SER 317 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
GLN N      N N N 88  
GLN CA     C N S 89  
GLN C      C N N 90  
GLN O      O N N 91  
GLN CB     C N N 92  
GLN CG     C N N 93  
GLN CD     C N N 94  
GLN OE1    O N N 95  
GLN NE2    N N N 96  
GLN OXT    O N N 97  
GLN H      H N N 98  
GLN H2     H N N 99  
GLN HA     H N N 100 
GLN HB2    H N N 101 
GLN HB3    H N N 102 
GLN HG2    H N N 103 
GLN HG3    H N N 104 
GLN HE21   H N N 105 
GLN HE22   H N N 106 
GLN HXT    H N N 107 
GLU N      N N N 108 
GLU CA     C N S 109 
GLU C      C N N 110 
GLU O      O N N 111 
GLU CB     C N N 112 
GLU CG     C N N 113 
GLU CD     C N N 114 
GLU OE1    O N N 115 
GLU OE2    O N N 116 
GLU OXT    O N N 117 
GLU H      H N N 118 
GLU H2     H N N 119 
GLU HA     H N N 120 
GLU HB2    H N N 121 
GLU HB3    H N N 122 
GLU HG2    H N N 123 
GLU HG3    H N N 124 
GLU HE2    H N N 125 
GLU HXT    H N N 126 
GLY N      N N N 127 
GLY CA     C N N 128 
GLY C      C N N 129 
GLY O      O N N 130 
GLY OXT    O N N 131 
GLY H      H N N 132 
GLY H2     H N N 133 
GLY HA2    H N N 134 
GLY HA3    H N N 135 
GLY HXT    H N N 136 
HIS N      N N N 137 
HIS CA     C N S 138 
HIS C      C N N 139 
HIS O      O N N 140 
HIS CB     C N N 141 
HIS CG     C Y N 142 
HIS ND1    N Y N 143 
HIS CD2    C Y N 144 
HIS CE1    C Y N 145 
HIS NE2    N Y N 146 
HIS OXT    O N N 147 
HIS H      H N N 148 
HIS H2     H N N 149 
HIS HA     H N N 150 
HIS HB2    H N N 151 
HIS HB3    H N N 152 
HIS HD1    H N N 153 
HIS HD2    H N N 154 
HIS HE1    H N N 155 
HIS HE2    H N N 156 
HIS HXT    H N N 157 
HOH O      O N N 158 
HOH H1     H N N 159 
HOH H2     H N N 160 
ILE N      N N N 161 
ILE CA     C N S 162 
ILE C      C N N 163 
ILE O      O N N 164 
ILE CB     C N S 165 
ILE CG1    C N N 166 
ILE CG2    C N N 167 
ILE CD1    C N N 168 
ILE OXT    O N N 169 
ILE H      H N N 170 
ILE H2     H N N 171 
ILE HA     H N N 172 
ILE HB     H N N 173 
ILE HG12   H N N 174 
ILE HG13   H N N 175 
ILE HG21   H N N 176 
ILE HG22   H N N 177 
ILE HG23   H N N 178 
ILE HD11   H N N 179 
ILE HD12   H N N 180 
ILE HD13   H N N 181 
ILE HXT    H N N 182 
LEU N      N N N 183 
LEU CA     C N S 184 
LEU C      C N N 185 
LEU O      O N N 186 
LEU CB     C N N 187 
LEU CG     C N N 188 
LEU CD1    C N N 189 
LEU CD2    C N N 190 
LEU OXT    O N N 191 
LEU H      H N N 192 
LEU H2     H N N 193 
LEU HA     H N N 194 
LEU HB2    H N N 195 
LEU HB3    H N N 196 
LEU HG     H N N 197 
LEU HD11   H N N 198 
LEU HD12   H N N 199 
LEU HD13   H N N 200 
LEU HD21   H N N 201 
LEU HD22   H N N 202 
LEU HD23   H N N 203 
LEU HXT    H N N 204 
LLP N1     N Y N 205 
LLP C2     C Y N 206 
LLP "C2'"  C N N 207 
LLP C3     C Y N 208 
LLP O3     O N N 209 
LLP C4     C Y N 210 
LLP "C4'"  C N N 211 
LLP C5     C Y N 212 
LLP C6     C Y N 213 
LLP "C5'"  C N N 214 
LLP OP4    O N N 215 
LLP P      P N N 216 
LLP OP1    O N N 217 
LLP OP2    O N N 218 
LLP OP3    O N N 219 
LLP N      N N N 220 
LLP CA     C N S 221 
LLP CB     C N N 222 
LLP CG     C N N 223 
LLP CD     C N N 224 
LLP CE     C N N 225 
LLP NZ     N N N 226 
LLP C      C N N 227 
LLP O      O N N 228 
LLP OXT    O N N 229 
LLP "H2'1" H N N 230 
LLP "H2'2" H N N 231 
LLP "H2'3" H N N 232 
LLP HO3    H N N 233 
LLP "H4'1" H N N 234 
LLP H6     H N N 235 
LLP "H5'1" H N N 236 
LLP "H5'2" H N N 237 
LLP HOP2   H N N 238 
LLP HOP3   H N N 239 
LLP H      H N N 240 
LLP H2     H N N 241 
LLP HA     H N N 242 
LLP HB2    H N N 243 
LLP HB3    H N N 244 
LLP HG2    H N N 245 
LLP HG3    H N N 246 
LLP HD2    H N N 247 
LLP HD3    H N N 248 
LLP HE2    H N N 249 
LLP HE3    H N N 250 
LLP HXT    H N N 251 
LYS N      N N N 252 
LYS CA     C N S 253 
LYS C      C N N 254 
LYS O      O N N 255 
LYS CB     C N N 256 
LYS CG     C N N 257 
LYS CD     C N N 258 
LYS CE     C N N 259 
LYS NZ     N N N 260 
LYS OXT    O N N 261 
LYS H      H N N 262 
LYS H2     H N N 263 
LYS HA     H N N 264 
LYS HB2    H N N 265 
LYS HB3    H N N 266 
LYS HG2    H N N 267 
LYS HG3    H N N 268 
LYS HD2    H N N 269 
LYS HD3    H N N 270 
LYS HE2    H N N 271 
LYS HE3    H N N 272 
LYS HZ1    H N N 273 
LYS HZ2    H N N 274 
LYS HZ3    H N N 275 
LYS HXT    H N N 276 
MET N      N N N 277 
MET CA     C N S 278 
MET C      C N N 279 
MET O      O N N 280 
MET CB     C N N 281 
MET CG     C N N 282 
MET SD     S N N 283 
MET CE     C N N 284 
MET OXT    O N N 285 
MET H      H N N 286 
MET H2     H N N 287 
MET HA     H N N 288 
MET HB2    H N N 289 
MET HB3    H N N 290 
MET HG2    H N N 291 
MET HG3    H N N 292 
MET HE1    H N N 293 
MET HE2    H N N 294 
MET HE3    H N N 295 
MET HXT    H N N 296 
OO0 N      N N N 297 
OO0 CA     C N R 298 
OO0 CB     C N N 299 
OO0 SG     S N R 300 
OO0 O1     O N N 301 
OO0 C3     C N N 302 
OO0 C4     C N N 303 
OO0 C5     C N N 304 
OO0 C      C N N 305 
OO0 OXT    O N N 306 
OO0 O      O N N 307 
OO0 H      H N N 308 
OO0 H2     H N N 309 
OO0 HA     H N N 310 
OO0 HB2    H N N 311 
OO0 HB3    H N N 312 
OO0 H6     H N N 313 
OO0 H7     H N N 314 
OO0 H8     H N N 315 
OO0 H9     H N N 316 
OO0 H10    H N N 317 
OO0 HXT    H N N 318 
PHE N      N N N 319 
PHE CA     C N S 320 
PHE C      C N N 321 
PHE O      O N N 322 
PHE CB     C N N 323 
PHE CG     C Y N 324 
PHE CD1    C Y N 325 
PHE CD2    C Y N 326 
PHE CE1    C Y N 327 
PHE CE2    C Y N 328 
PHE CZ     C Y N 329 
PHE OXT    O N N 330 
PHE H      H N N 331 
PHE H2     H N N 332 
PHE HA     H N N 333 
PHE HB2    H N N 334 
PHE HB3    H N N 335 
PHE HD1    H N N 336 
PHE HD2    H N N 337 
PHE HE1    H N N 338 
PHE HE2    H N N 339 
PHE HZ     H N N 340 
PHE HXT    H N N 341 
PRO N      N N N 342 
PRO CA     C N S 343 
PRO C      C N N 344 
PRO O      O N N 345 
PRO CB     C N N 346 
PRO CG     C N N 347 
PRO CD     C N N 348 
PRO OXT    O N N 349 
PRO H      H N N 350 
PRO HA     H N N 351 
PRO HB2    H N N 352 
PRO HB3    H N N 353 
PRO HG2    H N N 354 
PRO HG3    H N N 355 
PRO HD2    H N N 356 
PRO HD3    H N N 357 
PRO HXT    H N N 358 
SER N      N N N 359 
SER CA     C N S 360 
SER C      C N N 361 
SER O      O N N 362 
SER CB     C N N 363 
SER OG     O N N 364 
SER OXT    O N N 365 
SER H      H N N 366 
SER H2     H N N 367 
SER HA     H N N 368 
SER HB2    H N N 369 
SER HB3    H N N 370 
SER HG     H N N 371 
SER HXT    H N N 372 
THR N      N N N 373 
THR CA     C N S 374 
THR C      C N N 375 
THR O      O N N 376 
THR CB     C N R 377 
THR OG1    O N N 378 
THR CG2    C N N 379 
THR OXT    O N N 380 
THR H      H N N 381 
THR H2     H N N 382 
THR HA     H N N 383 
THR HB     H N N 384 
THR HG1    H N N 385 
THR HG21   H N N 386 
THR HG22   H N N 387 
THR HG23   H N N 388 
THR HXT    H N N 389 
TRP N      N N N 390 
TRP CA     C N S 391 
TRP C      C N N 392 
TRP O      O N N 393 
TRP CB     C N N 394 
TRP CG     C Y N 395 
TRP CD1    C Y N 396 
TRP CD2    C Y N 397 
TRP NE1    N Y N 398 
TRP CE2    C Y N 399 
TRP CE3    C Y N 400 
TRP CZ2    C Y N 401 
TRP CZ3    C Y N 402 
TRP CH2    C Y N 403 
TRP OXT    O N N 404 
TRP H      H N N 405 
TRP H2     H N N 406 
TRP HA     H N N 407 
TRP HB2    H N N 408 
TRP HB3    H N N 409 
TRP HD1    H N N 410 
TRP HE1    H N N 411 
TRP HE3    H N N 412 
TRP HZ2    H N N 413 
TRP HZ3    H N N 414 
TRP HH2    H N N 415 
TRP HXT    H N N 416 
TYR N      N N N 417 
TYR CA     C N S 418 
TYR C      C N N 419 
TYR O      O N N 420 
TYR CB     C N N 421 
TYR CG     C Y N 422 
TYR CD1    C Y N 423 
TYR CD2    C Y N 424 
TYR CE1    C Y N 425 
TYR CE2    C Y N 426 
TYR CZ     C Y N 427 
TYR OH     O N N 428 
TYR OXT    O N N 429 
TYR H      H N N 430 
TYR H2     H N N 431 
TYR HA     H N N 432 
TYR HB2    H N N 433 
TYR HB3    H N N 434 
TYR HD1    H N N 435 
TYR HD2    H N N 436 
TYR HE1    H N N 437 
TYR HE2    H N N 438 
TYR HH     H N N 439 
TYR HXT    H N N 440 
VAL N      N N N 441 
VAL CA     C N S 442 
VAL C      C N N 443 
VAL O      O N N 444 
VAL CB     C N N 445 
VAL CG1    C N N 446 
VAL CG2    C N N 447 
VAL OXT    O N N 448 
VAL H      H N N 449 
VAL H2     H N N 450 
VAL HA     H N N 451 
VAL HB     H N N 452 
VAL HG11   H N N 453 
VAL HG12   H N N 454 
VAL HG13   H N N 455 
VAL HG21   H N N 456 
VAL HG22   H N N 457 
VAL HG23   H N N 458 
VAL HXT    H N N 459 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LLP N1    C2     doub Y N 194 
LLP N1    C6     sing Y N 195 
LLP C2    "C2'"  sing N N 196 
LLP C2    C3     sing Y N 197 
LLP C3    O3     sing N N 198 
LLP C3    C4     doub Y N 199 
LLP C4    "C4'"  sing N N 200 
LLP C4    C5     sing Y N 201 
LLP "C4'" NZ     doub N N 202 
LLP C5    C6     doub Y N 203 
LLP C5    "C5'"  sing N N 204 
LLP "C5'" OP4    sing N N 205 
LLP OP4   P      sing N N 206 
LLP P     OP1    doub N N 207 
LLP P     OP2    sing N N 208 
LLP P     OP3    sing N N 209 
LLP N     CA     sing N N 210 
LLP CA    CB     sing N N 211 
LLP CA    C      sing N N 212 
LLP CB    CG     sing N N 213 
LLP CG    CD     sing N N 214 
LLP CD    CE     sing N N 215 
LLP CE    NZ     sing N N 216 
LLP C     O      doub N N 217 
LLP C     OXT    sing N N 218 
LLP "C2'" "H2'1" sing N N 219 
LLP "C2'" "H2'2" sing N N 220 
LLP "C2'" "H2'3" sing N N 221 
LLP O3    HO3    sing N N 222 
LLP "C4'" "H4'1" sing N N 223 
LLP C6    H6     sing N N 224 
LLP "C5'" "H5'1" sing N N 225 
LLP "C5'" "H5'2" sing N N 226 
LLP OP2   HOP2   sing N N 227 
LLP OP3   HOP3   sing N N 228 
LLP N     H      sing N N 229 
LLP N     H2     sing N N 230 
LLP CA    HA     sing N N 231 
LLP CB    HB2    sing N N 232 
LLP CB    HB3    sing N N 233 
LLP CG    HG2    sing N N 234 
LLP CG    HG3    sing N N 235 
LLP CD    HD2    sing N N 236 
LLP CD    HD3    sing N N 237 
LLP CE    HE2    sing N N 238 
LLP CE    HE3    sing N N 239 
LLP OXT   HXT    sing N N 240 
LYS N     CA     sing N N 241 
LYS N     H      sing N N 242 
LYS N     H2     sing N N 243 
LYS CA    C      sing N N 244 
LYS CA    CB     sing N N 245 
LYS CA    HA     sing N N 246 
LYS C     O      doub N N 247 
LYS C     OXT    sing N N 248 
LYS CB    CG     sing N N 249 
LYS CB    HB2    sing N N 250 
LYS CB    HB3    sing N N 251 
LYS CG    CD     sing N N 252 
LYS CG    HG2    sing N N 253 
LYS CG    HG3    sing N N 254 
LYS CD    CE     sing N N 255 
LYS CD    HD2    sing N N 256 
LYS CD    HD3    sing N N 257 
LYS CE    NZ     sing N N 258 
LYS CE    HE2    sing N N 259 
LYS CE    HE3    sing N N 260 
LYS NZ    HZ1    sing N N 261 
LYS NZ    HZ2    sing N N 262 
LYS NZ    HZ3    sing N N 263 
LYS OXT   HXT    sing N N 264 
MET N     CA     sing N N 265 
MET N     H      sing N N 266 
MET N     H2     sing N N 267 
MET CA    C      sing N N 268 
MET CA    CB     sing N N 269 
MET CA    HA     sing N N 270 
MET C     O      doub N N 271 
MET C     OXT    sing N N 272 
MET CB    CG     sing N N 273 
MET CB    HB2    sing N N 274 
MET CB    HB3    sing N N 275 
MET CG    SD     sing N N 276 
MET CG    HG2    sing N N 277 
MET CG    HG3    sing N N 278 
MET SD    CE     sing N N 279 
MET CE    HE1    sing N N 280 
MET CE    HE2    sing N N 281 
MET CE    HE3    sing N N 282 
MET OXT   HXT    sing N N 283 
OO0 N     CA     sing N N 284 
OO0 CA    CB     sing N N 285 
OO0 CB    SG     sing N N 286 
OO0 SG    O1     doub N N 287 
OO0 SG    C3     sing N N 288 
OO0 C3    C4     sing N N 289 
OO0 C4    C5     doub N N 290 
OO0 CA    C      sing N N 291 
OO0 C     OXT    sing N N 292 
OO0 C     O      doub N N 293 
OO0 N     H      sing N N 294 
OO0 N     H2     sing N N 295 
OO0 CA    HA     sing N N 296 
OO0 CB    HB2    sing N N 297 
OO0 CB    HB3    sing N N 298 
OO0 C3    H6     sing N N 299 
OO0 C3    H7     sing N N 300 
OO0 C4    H8     sing N N 301 
OO0 C5    H9     sing N N 302 
OO0 C5    H10    sing N N 303 
OO0 OXT   HXT    sing N N 304 
PHE N     CA     sing N N 305 
PHE N     H      sing N N 306 
PHE N     H2     sing N N 307 
PHE CA    C      sing N N 308 
PHE CA    CB     sing N N 309 
PHE CA    HA     sing N N 310 
PHE C     O      doub N N 311 
PHE C     OXT    sing N N 312 
PHE CB    CG     sing N N 313 
PHE CB    HB2    sing N N 314 
PHE CB    HB3    sing N N 315 
PHE CG    CD1    doub Y N 316 
PHE CG    CD2    sing Y N 317 
PHE CD1   CE1    sing Y N 318 
PHE CD1   HD1    sing N N 319 
PHE CD2   CE2    doub Y N 320 
PHE CD2   HD2    sing N N 321 
PHE CE1   CZ     doub Y N 322 
PHE CE1   HE1    sing N N 323 
PHE CE2   CZ     sing Y N 324 
PHE CE2   HE2    sing N N 325 
PHE CZ    HZ     sing N N 326 
PHE OXT   HXT    sing N N 327 
PRO N     CA     sing N N 328 
PRO N     CD     sing N N 329 
PRO N     H      sing N N 330 
PRO CA    C      sing N N 331 
PRO CA    CB     sing N N 332 
PRO CA    HA     sing N N 333 
PRO C     O      doub N N 334 
PRO C     OXT    sing N N 335 
PRO CB    CG     sing N N 336 
PRO CB    HB2    sing N N 337 
PRO CB    HB3    sing N N 338 
PRO CG    CD     sing N N 339 
PRO CG    HG2    sing N N 340 
PRO CG    HG3    sing N N 341 
PRO CD    HD2    sing N N 342 
PRO CD    HD3    sing N N 343 
PRO OXT   HXT    sing N N 344 
SER N     CA     sing N N 345 
SER N     H      sing N N 346 
SER N     H2     sing N N 347 
SER CA    C      sing N N 348 
SER CA    CB     sing N N 349 
SER CA    HA     sing N N 350 
SER C     O      doub N N 351 
SER C     OXT    sing N N 352 
SER CB    OG     sing N N 353 
SER CB    HB2    sing N N 354 
SER CB    HB3    sing N N 355 
SER OG    HG     sing N N 356 
SER OXT   HXT    sing N N 357 
THR N     CA     sing N N 358 
THR N     H      sing N N 359 
THR N     H2     sing N N 360 
THR CA    C      sing N N 361 
THR CA    CB     sing N N 362 
THR CA    HA     sing N N 363 
THR C     O      doub N N 364 
THR C     OXT    sing N N 365 
THR CB    OG1    sing N N 366 
THR CB    CG2    sing N N 367 
THR CB    HB     sing N N 368 
THR OG1   HG1    sing N N 369 
THR CG2   HG21   sing N N 370 
THR CG2   HG22   sing N N 371 
THR CG2   HG23   sing N N 372 
THR OXT   HXT    sing N N 373 
TRP N     CA     sing N N 374 
TRP N     H      sing N N 375 
TRP N     H2     sing N N 376 
TRP CA    C      sing N N 377 
TRP CA    CB     sing N N 378 
TRP CA    HA     sing N N 379 
TRP C     O      doub N N 380 
TRP C     OXT    sing N N 381 
TRP CB    CG     sing N N 382 
TRP CB    HB2    sing N N 383 
TRP CB    HB3    sing N N 384 
TRP CG    CD1    doub Y N 385 
TRP CG    CD2    sing Y N 386 
TRP CD1   NE1    sing Y N 387 
TRP CD1   HD1    sing N N 388 
TRP CD2   CE2    doub Y N 389 
TRP CD2   CE3    sing Y N 390 
TRP NE1   CE2    sing Y N 391 
TRP NE1   HE1    sing N N 392 
TRP CE2   CZ2    sing Y N 393 
TRP CE3   CZ3    doub Y N 394 
TRP CE3   HE3    sing N N 395 
TRP CZ2   CH2    doub Y N 396 
TRP CZ2   HZ2    sing N N 397 
TRP CZ3   CH2    sing Y N 398 
TRP CZ3   HZ3    sing N N 399 
TRP CH2   HH2    sing N N 400 
TRP OXT   HXT    sing N N 401 
TYR N     CA     sing N N 402 
TYR N     H      sing N N 403 
TYR N     H2     sing N N 404 
TYR CA    C      sing N N 405 
TYR CA    CB     sing N N 406 
TYR CA    HA     sing N N 407 
TYR C     O      doub N N 408 
TYR C     OXT    sing N N 409 
TYR CB    CG     sing N N 410 
TYR CB    HB2    sing N N 411 
TYR CB    HB3    sing N N 412 
TYR CG    CD1    doub Y N 413 
TYR CG    CD2    sing Y N 414 
TYR CD1   CE1    sing Y N 415 
TYR CD1   HD1    sing N N 416 
TYR CD2   CE2    doub Y N 417 
TYR CD2   HD2    sing N N 418 
TYR CE1   CZ     doub Y N 419 
TYR CE1   HE1    sing N N 420 
TYR CE2   CZ     sing Y N 421 
TYR CE2   HE2    sing N N 422 
TYR CZ    OH     sing N N 423 
TYR OH    HH     sing N N 424 
TYR OXT   HXT    sing N N 425 
VAL N     CA     sing N N 426 
VAL N     H      sing N N 427 
VAL N     H2     sing N N 428 
VAL CA    C      sing N N 429 
VAL CA    CB     sing N N 430 
VAL CA    HA     sing N N 431 
VAL C     O      doub N N 432 
VAL C     OXT    sing N N 433 
VAL CB    CG1    sing N N 434 
VAL CB    CG2    sing N N 435 
VAL CB    HB     sing N N 436 
VAL CG1   HG11   sing N N 437 
VAL CG1   HG12   sing N N 438 
VAL CG1   HG13   sing N N 439 
VAL CG2   HG21   sing N N 440 
VAL CG2   HG22   sing N N 441 
VAL CG2   HG23   sing N N 442 
VAL OXT   HXT    sing N N 443 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           'Project no. 42077214' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      SwissModel 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9KAU 
_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]   0.018789 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000367 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011693 
_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]   0.005951 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . LYS A 1 6   ? 8.840   28.148  47.242 1.00 53.78 ?  6   LYS A N     1 
ATOM   2    C CA    . LYS A 1 6   ? 7.667   27.521  46.642 1.00 49.98 ?  6   LYS A CA    1 
ATOM   3    C C     . LYS A 1 6   ? 7.113   26.487  47.614 1.00 45.17 ?  6   LYS A C     1 
ATOM   4    O O     . LYS A 1 6   ? 7.787   25.502  47.933 1.00 45.29 ?  6   LYS A O     1 
ATOM   5    C CB    . LYS A 1 6   ? 8.007   26.873  45.302 1.00 56.11 ?  6   LYS A CB    1 
ATOM   6    C CG    . LYS A 1 6   ? 6.825   26.178  44.626 1.00 48.54 ?  6   LYS A CG    1 
ATOM   7    C CD    . LYS A 1 6   ? 6.963   24.658  44.632 1.00 45.05 ?  6   LYS A CD    1 
ATOM   8    C CE    . LYS A 1 6   ? 8.066   24.191  43.692 1.00 39.52 ?  6   LYS A CE    1 
ATOM   9    N NZ    . LYS A 1 6   ? 8.372   22.734  43.833 1.00 38.15 1  6   LYS A NZ    1 
ATOM   10   N N     . ALA A 1 7   ? 5.881   26.701  48.062 1.00 42.08 ?  7   ALA A N     1 
ATOM   11   C CA    . ALA A 1 7   ? 5.182   25.701  48.846 1.00 33.69 ?  7   ALA A CA    1 
ATOM   12   C C     . ALA A 1 7   ? 4.926   24.467  47.995 1.00 40.72 ?  7   ALA A C     1 
ATOM   13   O O     . ALA A 1 7   ? 4.498   24.571  46.841 1.00 53.36 ?  7   ALA A O     1 
ATOM   14   C CB    . ALA A 1 7   ? 3.867   26.276  49.368 1.00 33.87 ?  7   ALA A CB    1 
ATOM   15   N N     . ILE A 1 8   ? 5.216   23.299  48.562 1.00 29.85 ?  8   ILE A N     1 
ATOM   16   C CA    . ILE A 1 8   ? 5.074   22.018  47.885 1.00 25.34 ?  8   ILE A CA    1 
ATOM   17   C C     . ILE A 1 8   ? 3.915   21.275  48.533 1.00 24.69 ?  8   ILE A C     1 
ATOM   18   O O     . ILE A 1 8   ? 3.833   21.187  49.762 1.00 25.54 ?  8   ILE A O     1 
ATOM   19   C CB    . ILE A 1 8   ? 6.382   21.208  47.952 1.00 37.89 ?  8   ILE A CB    1 
ATOM   20   C CG1   . ILE A 1 8   ? 6.158   19.736  47.595 1.00 34.70 ?  8   ILE A CG1   1 
ATOM   21   C CG2   . ILE A 1 8   ? 7.038   21.354  49.316 1.00 40.04 ?  8   ILE A CG2   1 
ATOM   22   C CD1   . ILE A 1 8   ? 7.439   19.000  47.317 1.00 26.53 ?  8   ILE A CD1   1 
ATOM   23   N N     . ASN A 1 9   ? 3.015   20.753  47.703 1.00 40.39 ?  9   ASN A N     1 
ATOM   24   C CA    . ASN A 1 9   ? 1.831   20.047  48.183 1.00 34.59 ?  9   ASN A CA    1 
ATOM   25   C C     . ASN A 1 9   ? 2.220   18.803  48.971 1.00 36.36 ?  9   ASN A C     1 
ATOM   26   O O     . ASN A 1 9   ? 2.919   17.924  48.464 1.00 49.36 ?  9   ASN A O     1 
ATOM   27   C CB    . ASN A 1 9   ? 0.939   19.663  46.999 1.00 40.38 ?  9   ASN A CB    1 
ATOM   28   C CG    . ASN A 1 9   ? -0.363  18.978  47.425 1.00 54.06 ?  9   ASN A CG    1 
ATOM   29   O OD1   . ASN A 1 9   ? -0.771  19.023  48.594 1.00 52.96 ?  9   ASN A OD1   1 
ATOM   30   N ND2   . ASN A 1 9   ? -1.020  18.339  46.466 1.00 53.57 ?  9   ASN A ND2   1 
ATOM   31   N N     . ARG A 1 10  ? 1.770   18.739  50.221 1.00 30.18 ?  10  ARG A N     1 
ATOM   32   C CA    . ARG A 1 10  ? 1.996   17.582  51.069 1.00 30.28 ?  10  ARG A CA    1 
ATOM   33   C C     . ARG A 1 10  ? 0.705   16.862  51.449 1.00 40.27 ?  10  ARG A C     1 
ATOM   34   O O     . ARG A 1 10  ? 0.760   15.878  52.198 1.00 52.00 ?  10  ARG A O     1 
ATOM   35   C CB    . ARG A 1 10  ? 2.752   17.993  52.341 1.00 22.84 ?  10  ARG A CB    1 
ATOM   36   C CG    . ARG A 1 10  ? 4.240   18.237  52.131 1.00 25.81 ?  10  ARG A CG    1 
ATOM   37   C CD    . ARG A 1 10  ? 4.950   18.566  53.432 1.00 16.61 ?  10  ARG A CD    1 
ATOM   38   N NE    . ARG A 1 10  ? 4.928   17.462  54.388 1.00 12.67 ?  10  ARG A NE    1 
ATOM   39   C CZ    . ARG A 1 10  ? 5.463   17.511  55.605 1.00 10.98 ?  10  ARG A CZ    1 
ATOM   40   N NH1   . ARG A 1 10  ? 6.070   18.610  56.020 1.00 10.93 1  10  ARG A NH1   1 
ATOM   41   N NH2   . ARG A 1 10  ? 5.397   16.455  56.408 1.00 10.47 ?  10  ARG A NH2   1 
ATOM   42   N N     . ARG A 1 11  ? -0.449  17.308  50.962 1.00 28.86 ?  11  ARG A N     1 
ATOM   43   C CA    . ARG A 1 11  ? -1.682  16.572  51.199 1.00 38.13 ?  11  ARG A CA    1 
ATOM   44   C C     . ARG A 1 11  ? -1.701  15.271  50.392 1.00 38.93 ?  11  ARG A C     1 
ATOM   45   O O     . ARG A 1 11  ? -1.241  15.221  49.248 1.00 28.59 ?  11  ARG A O     1 
ATOM   46   C CB    . ARG A 1 11  ? -2.893  17.442  50.844 1.00 42.36 ?  11  ARG A CB    1 
ATOM   47   C CG    . ARG A 1 11  ? -3.163  18.587  51.815 1.00 31.70 ?  11  ARG A CG    1 
ATOM   48   C CD    . ARG A 1 11  ? -4.662  18.779  52.029 1.00 29.39 ?  11  ARG A CD    1 
ATOM   49   N NE    . ARG A 1 11  ? -4.960  19.955  52.849 1.00 37.85 ?  11  ARG A NE    1 
ATOM   50   C CZ    . ARG A 1 11  ? -5.226  19.933  54.155 1.00 30.61 ?  11  ARG A CZ    1 
ATOM   51   N NH1   . ARG A 1 11  ? -5.236  18.796  54.837 1.00 26.26 1  11  ARG A NH1   1 
ATOM   52   N NH2   . ARG A 1 11  ? -5.488  21.064  54.785 1.00 33.44 ?  11  ARG A NH2   1 
ATOM   53   N N     . GLY A 1 12  ? -2.212  14.202  51.006 1.00 49.01 ?  12  GLY A N     1 
ATOM   54   C CA    . GLY A 1 12  ? -2.253  12.903  50.348 1.00 46.32 ?  12  GLY A CA    1 
ATOM   55   C C     . GLY A 1 12  ? -0.942  12.146  50.317 1.00 44.44 ?  12  GLY A C     1 
ATOM   56   O O     . GLY A 1 12  ? -0.753  11.287  49.446 1.00 45.28 ?  12  GLY A O     1 
ATOM   57   N N     . THR A 1 13  ? -0.028  12.432  51.245 1.00 27.76 ?  13  THR A N     1 
ATOM   58   C CA    . THR A 1 13  ? 1.278   11.788  51.282 1.00 27.93 ?  13  THR A CA    1 
ATOM   59   C C     . THR A 1 13  ? 1.470   10.946  52.535 1.00 22.79 ?  13  THR A C     1 
ATOM   60   O O     . THR A 1 13  ? 2.574   10.465  52.780 1.00 27.68 ?  13  THR A O     1 
ATOM   61   C CB    . THR A 1 13  ? 2.397   12.837  51.171 1.00 30.77 ?  13  THR A CB    1 
ATOM   62   O OG1   . THR A 1 13  ? 2.294   13.787  52.239 1.00 25.61 ?  13  THR A OG1   1 
ATOM   63   C CG2   . THR A 1 13  ? 2.316   13.582  49.847 1.00 32.45 ?  13  THR A CG2   1 
ATOM   64   N N     . HIS A 1 14  ? 0.417   10.723  53.309 1.00 28.87 ?  14  HIS A N     1 
ATOM   65   C CA    . HIS A 1 14  ? 0.501   10.075  54.614 1.00 28.12 ?  14  HIS A CA    1 
ATOM   66   C C     . HIS A 1 14  ? 1.345   10.872  55.591 1.00 31.96 ?  14  HIS A C     1 
ATOM   67   O O     . HIS A 1 14  ? 1.875   10.320  56.556 1.00 48.63 ?  14  HIS A O     1 
ATOM   68   C CB    . HIS A 1 14  ? 1.009   8.636   54.495 1.00 27.62 ?  14  HIS A CB    1 
ATOM   69   C CG    . HIS A 1 14  ? 0.123   7.773   53.651 1.00 35.00 ?  14  HIS A CG    1 
ATOM   70   N ND1   . HIS A 1 14  ? -1.221  7.610   53.919 1.00 30.36 ?  14  HIS A ND1   1 
ATOM   71   C CD2   . HIS A 1 14  ? 0.375   7.054   52.530 1.00 35.96 ?  14  HIS A CD2   1 
ATOM   72   C CE1   . HIS A 1 14  ? -1.756  6.820   53.007 1.00 33.65 ?  14  HIS A CE1   1 
ATOM   73   N NE2   . HIS A 1 14  ? -0.810  6.467   52.154 1.00 39.99 ?  14  HIS A NE2   1 
ATOM   74   N N     . SER A 1 15  ? 1.473   12.170  55.349 1.00 27.28 ?  15  SER A N     1 
ATOM   75   C CA    . SER A 1 15  ? 2.027   13.073  56.342 1.00 20.86 ?  15  SER A CA    1 
ATOM   76   C C     . SER A 1 15  ? 1.099   13.182  57.541 1.00 21.21 ?  15  SER A C     1 
ATOM   77   O O     . SER A 1 15  ? -0.104  13.404  57.386 1.00 28.42 ?  15  SER A O     1 
ATOM   78   C CB    . SER A 1 15  ? 2.240   14.452  55.721 1.00 22.53 ?  15  SER A CB    1 
ATOM   79   O OG    . SER A 1 15  ? 2.677   15.379  56.694 1.00 29.24 ?  15  SER A OG    1 
ATOM   80   N N     . ILE A 1 16  ? 1.663   13.013  58.740 1.00 24.51 ?  16  ILE A N     1 
ATOM   81   C CA    . ILE A 1 16  ? 0.916   13.283  59.971 1.00 24.65 ?  16  ILE A CA    1 
ATOM   82   C C     . ILE A 1 16  ? 0.489   14.747  60.019 1.00 31.29 ?  16  ILE A C     1 
ATOM   83   O O     . ILE A 1 16  ? -0.561  15.085  60.578 1.00 17.29 ?  16  ILE A O     1 
ATOM   84   C CB    . ILE A 1 16  ? 1.750   12.903  61.215 1.00 17.04 ?  16  ILE A CB    1 
ATOM   85   C CG1   . ILE A 1 16  ? 2.161   11.447  61.161 1.00 18.49 ?  16  ILE A CG1   1 
ATOM   86   C CG2   . ILE A 1 16  ? 0.973   13.133  62.505 1.00 14.74 ?  16  ILE A CG2   1 
ATOM   87   C CD1   . ILE A 1 16  ? 2.365   10.857  62.531 1.00 25.56 ?  16  ILE A CD1   1 
ATOM   88   N N     . LYS A 1 17  ? 1.318   15.641  59.476 1.00 41.44 ?  17  LYS A N     1 
ATOM   89   C CA    . LYS A 1 17  ? 1.023   17.069  59.526 1.00 33.70 ?  17  LYS A CA    1 
ATOM   90   C C     . LYS A 1 17  ? -0.225  17.405  58.723 1.00 28.52 ?  17  LYS A C     1 
ATOM   91   O O     . LYS A 1 17  ? -1.099  18.135  59.197 1.00 36.40 ?  17  LYS A O     1 
ATOM   92   C CB    . LYS A 1 17  ? 2.219   17.859  58.993 1.00 21.16 ?  17  LYS A CB    1 
ATOM   93   C CG    . LYS A 1 17  ? 2.203   19.354  59.277 1.00 25.76 ?  17  LYS A CG    1 
ATOM   94   C CD    . LYS A 1 17  ? 3.509   19.960  58.785 1.00 24.68 ?  17  LYS A CD    1 
ATOM   95   C CE    . LYS A 1 17  ? 3.722   21.397  59.244 1.00 23.21 ?  17  LYS A CE    1 
ATOM   96   N NZ    . LYS A 1 17  ? 5.143   21.858  59.050 1.00 12.36 1  17  LYS A NZ    1 
ATOM   97   N N     . TRP A 1 18  ? -0.321  16.874  57.502 1.00 25.21 ?  18  TRP A N     1 
ATOM   98   C CA    . TRP A 1 18  ? -1.292  17.316  56.508 1.00 25.41 ?  18  TRP A CA    1 
ATOM   99   C C     . TRP A 1 18  ? -2.469  16.372  56.292 1.00 29.40 ?  18  TRP A C     1 
ATOM   100  O O     . TRP A 1 18  ? -3.487  16.799  55.738 1.00 38.76 ?  18  TRP A O     1 
ATOM   101  C CB    . TRP A 1 18  ? -0.577  17.525  55.171 1.00 33.74 ?  18  TRP A CB    1 
ATOM   102  C CG    . TRP A 1 18  ? 0.232   18.772  55.156 1.00 37.71 ?  18  TRP A CG    1 
ATOM   103  C CD1   . TRP A 1 18  ? 1.589   18.877  55.246 1.00 41.34 ?  18  TRP A CD1   1 
ATOM   104  C CD2   . TRP A 1 18  ? -0.271  20.106  55.080 1.00 39.42 ?  18  TRP A CD2   1 
ATOM   105  N NE1   . TRP A 1 18  ? 1.967   20.202  55.217 1.00 28.22 ?  18  TRP A NE1   1 
ATOM   106  C CE2   . TRP A 1 18  ? 0.838   20.975  55.114 1.00 48.08 ?  18  TRP A CE2   1 
ATOM   107  C CE3   . TRP A 1 18  ? -1.552  20.653  54.980 1.00 33.97 ?  18  TRP A CE3   1 
ATOM   108  C CZ2   . TRP A 1 18  ? 0.698   22.359  55.055 1.00 53.14 ?  18  TRP A CZ2   1 
ATOM   109  C CZ3   . TRP A 1 18  ? -1.686  22.021  54.916 1.00 29.98 ?  18  TRP A CZ3   1 
ATOM   110  C CH2   . TRP A 1 18  ? -0.571  22.859  54.956 1.00 44.33 ?  18  TRP A CH2   1 
ATOM   111  N N     . ASP A 1 19  ? -2.378  15.121  56.732 1.00 22.89 ?  19  ASP A N     1 
ATOM   112  C CA    . ASP A 1 19  ? -3.400  14.139  56.436 1.00 10.64 ?  19  ASP A CA    1 
ATOM   113  C C     . ASP A 1 19  ? -4.143  13.657  57.670 1.00 18.70 ?  19  ASP A C     1 
ATOM   114  O O     . ASP A 1 19  ? -5.138  12.930  57.538 1.00 22.67 ?  19  ASP A O     1 
ATOM   115  C CB    . ASP A 1 19  ? -2.761  12.977  55.678 1.00 34.45 ?  19  ASP A CB    1 
ATOM   116  C CG    . ASP A 1 19  ? -2.102  13.444  54.390 1.00 47.91 ?  19  ASP A CG    1 
ATOM   117  O OD1   . ASP A 1 19  ? -2.595  14.440  53.814 1.00 46.61 ?  19  ASP A OD1   1 
ATOM   118  O OD2   . ASP A 1 19  ? -1.088  12.851  53.967 1.00 49.82 -1 19  ASP A OD2   1 
ATOM   119  N N     . THR A 1 20  ? -3.730  14.089  58.864 1.00 20.31 ?  20  THR A N     1 
ATOM   120  C CA    . THR A 1 20  ? -4.456  13.709  60.071 1.00 20.98 ?  20  THR A CA    1 
ATOM   121  C C     . THR A 1 20  ? -5.825  14.388  60.130 1.00 34.14 ?  20  THR A C     1 
ATOM   122  O O     . THR A 1 20  ? -6.809  13.775  60.568 1.00 42.80 ?  20  THR A O     1 
ATOM   123  C CB    . THR A 1 20  ? -3.632  14.060  61.313 1.00 13.81 ?  20  THR A CB    1 
ATOM   124  O OG1   . THR A 1 20  ? -2.438  13.274  61.339 1.00 20.59 ?  20  THR A OG1   1 
ATOM   125  C CG2   . THR A 1 20  ? -4.420  13.789  62.589 1.00 20.75 ?  20  THR A CG2   1 
ATOM   126  N N     . TYR A 1 21  ? -5.923  15.624  59.638 1.00 22.89 ?  21  TYR A N     1 
ATOM   127  C CA    . TYR A 1 21  ? -7.190  16.337  59.550 1.00 27.14 ?  21  TYR A CA    1 
ATOM   128  C C     . TYR A 1 21  ? -7.741  16.244  58.133 1.00 41.97 ?  21  TYR A C     1 
ATOM   129  O O     . TYR A 1 21  ? -6.991  16.303  57.153 1.00 49.68 ?  21  TYR A O     1 
ATOM   130  C CB    . TYR A 1 21  ? -7.036  17.806  59.967 1.00 16.01 ?  21  TYR A CB    1 
ATOM   131  C CG    . TYR A 1 21  ? -6.897  18.010  61.474 1.00 14.81 ?  21  TYR A CG    1 
ATOM   132  C CD1   . TYR A 1 21  ? -5.678  17.832  62.108 1.00 33.89 ?  21  TYR A CD1   1 
ATOM   133  C CD2   . TYR A 1 21  ? -7.977  18.369  62.255 1.00 10.95 ?  21  TYR A CD2   1 
ATOM   134  C CE1   . TYR A 1 21  ? -5.545  18.002  63.473 1.00 36.48 ?  21  TYR A CE1   1 
ATOM   135  C CE2   . TYR A 1 21  ? -7.854  18.542  63.622 1.00 14.57 ?  21  TYR A CE2   1 
ATOM   136  C CZ    . TYR A 1 21  ? -6.635  18.358  64.228 1.00 26.14 ?  21  TYR A CZ    1 
ATOM   137  O OH    . TYR A 1 21  ? -6.495  18.531  65.592 1.00 27.61 ?  21  TYR A OH    1 
ATOM   138  N N     . LYS A 1 22  ? -9.062  16.096  58.033 1.00 43.21 ?  22  LYS A N     1 
ATOM   139  C CA    . LYS A 1 22  ? -9.730  15.915  56.752 1.00 42.66 ?  22  LYS A CA    1 
ATOM   140  C C     . LYS A 1 22  ? -10.376 17.195  56.234 1.00 46.51 ?  22  LYS A C     1 
ATOM   141  O O     . LYS A 1 22  ? -10.721 17.256  55.048 1.00 51.09 ?  22  LYS A O     1 
ATOM   142  C CB    . LYS A 1 22  ? -10.797 14.811  56.866 1.00 38.71 ?  22  LYS A CB    1 
ATOM   143  C CG    . LYS A 1 22  ? -10.363 13.589  57.691 1.00 27.71 ?  22  LYS A CG    1 
ATOM   144  C CD    . LYS A 1 22  ? -10.837 13.714  59.133 1.00 19.62 ?  22  LYS A CD    1 
ATOM   145  C CE    . LYS A 1 22  ? -10.195 12.694  60.036 1.00 23.99 ?  22  LYS A CE    1 
ATOM   146  N NZ    . LYS A 1 22  ? -10.468 13.014  61.462 1.00 24.51 1  22  LYS A NZ    1 
ATOM   147  N N     . ASN A 1 23  ? -10.529 18.216  57.085 1.00 45.65 ?  23  ASN A N     1 
ATOM   148  C CA    . ASN A 1 23  ? -11.010 19.564  56.675 1.00 28.99 ?  23  ASN A CA    1 
ATOM   149  C C     . ASN A 1 23  ? -9.912  20.155  55.801 1.00 22.57 ?  23  ASN A C     1 
ATOM   150  O O     . ASN A 1 23  ? -8.871  20.470  56.309 1.00 23.36 ?  23  ASN A O     1 
ATOM   151  C CB    . ASN A 1 23  ? -11.392 20.361  57.926 1.00 26.40 ?  23  ASN A CB    1 
ATOM   152  C CG    . ASN A 1 23  ? -12.085 21.694  57.748 1.00 24.98 ?  23  ASN A CG    1 
ATOM   153  O OD1   . ASN A 1 23  ? -12.124 22.258  56.667 1.00 28.08 ?  23  ASN A OD1   1 
ATOM   154  N ND2   . ASN A 1 23  ? -12.620 22.223  58.831 1.00 11.24 ?  23  ASN A ND2   1 
ATOM   155  N N     . GLU A 1 24  ? -10.173 20.274  54.510 1.00 27.57 ?  24  GLU A N     1 
ATOM   156  C CA    . GLU A 1 24  ? -9.141  20.715  53.582 1.00 29.11 ?  24  GLU A CA    1 
ATOM   157  C C     . GLU A 1 24  ? -8.830  22.199  53.669 1.00 35.47 ?  24  GLU A C     1 
ATOM   158  O O     . GLU A 1 24  ? -7.850  22.638  53.056 1.00 42.72 ?  24  GLU A O     1 
ATOM   159  C CB    . GLU A 1 24  ? -9.572  20.374  52.159 1.00 26.91 ?  24  GLU A CB    1 
ATOM   160  C CG    . GLU A 1 24  ? -10.253 19.036  52.059 1.00 31.14 ?  24  GLU A CG    1 
ATOM   161  C CD    . GLU A 1 24  ? -9.746  18.247  50.890 1.00 45.90 ?  24  GLU A CD    1 
ATOM   162  O OE1   . GLU A 1 24  ? -10.316 17.180  50.598 1.00 57.44 ?  24  GLU A OE1   1 
ATOM   163  O OE2   . GLU A 1 24  ? -8.769  18.696  50.259 1.00 53.57 -1 24  GLU A OE2   1 
ATOM   164  N N     . GLU A 1 25  ? -9.626  22.974  54.405 1.00 36.72 ?  25  GLU A N     1 
ATOM   165  C CA    . GLU A 1 25  ? -9.372  24.396  54.607 1.00 39.77 ?  25  GLU A CA    1 
ATOM   166  C C     . GLU A 1 25  ? -8.298  24.669  55.646 1.00 48.82 ?  25  GLU A C     1 
ATOM   167  O O     . GLU A 1 25  ? -7.902  25.828  55.805 1.00 61.20 ?  25  GLU A O     1 
ATOM   168  C CB    . GLU A 1 25  ? -10.657 25.118  55.021 1.00 48.12 ?  25  GLU A CB    1 
ATOM   169  C CG    . GLU A 1 25  ? -11.397 25.792  53.873 1.00 49.95 ?  25  GLU A CG    1 
ATOM   170  C CD    . GLU A 1 25  ? -12.715 26.400  54.309 1.00 52.20 ?  25  GLU A CD    1 
ATOM   171  O OE1   . GLU A 1 25  ? -13.375 27.051  53.478 1.00 52.89 ?  25  GLU A OE1   1 
ATOM   172  O OE2   . GLU A 1 25  ? -13.088 26.229  55.486 1.00 57.40 -1 25  GLU A OE2   1 
ATOM   173  N N     . LEU A 1 26  ? -7.834  23.650  56.363 1.00 40.80 ?  26  LEU A N     1 
ATOM   174  C CA    . LEU A 1 26  ? -6.934  23.864  57.487 1.00 34.01 ?  26  LEU A CA    1 
ATOM   175  C C     . LEU A 1 26  ? -5.503  24.079  57.015 1.00 29.89 ?  26  LEU A C     1 
ATOM   176  O O     . LEU A 1 26  ? -5.041  23.421  56.081 1.00 18.67 ?  26  LEU A O     1 
ATOM   177  C CB    . LEU A 1 26  ? -6.988  22.673  58.446 1.00 23.98 ?  26  LEU A CB    1 
ATOM   178  C CG    . LEU A 1 26  ? -8.383  22.392  59.020 1.00 32.56 ?  26  LEU A CG    1 
ATOM   179  C CD1   . LEU A 1 26  ? -8.411  21.049  59.702 1.00 29.71 ?  26  LEU A CD1   1 
ATOM   180  C CD2   . LEU A 1 26  ? -8.829  23.490  59.984 1.00 33.96 ?  26  LEU A CD2   1 
ATOM   181  N N     . ILE A 1 27  ? -4.827  25.050  57.654 1.00 31.25 ?  27  ILE A N     1 
ATOM   182  C CA    . ILE A 1 27  ? -3.377  25.255  57.572 1.00 23.36 ?  27  ILE A CA    1 
ATOM   183  C C     . ILE A 1 27  ? -2.749  24.625  58.806 1.00 23.21 ?  27  ILE A C     1 
ATOM   184  O O     . ILE A 1 27  ? -3.188  24.888  59.933 1.00 15.66 ?  27  ILE A O     1 
ATOM   185  C CB    . ILE A 1 27  ? -2.993  26.740  57.519 1.00 21.25 ?  27  ILE A CB    1 
ATOM   186  C CG1   . ILE A 1 27  ? -3.320  27.369  56.170 1.00 23.63 ?  27  ILE A CG1   1 
ATOM   187  C CG2   . ILE A 1 27  ? -1.515  26.875  57.810 1.00 36.43 ?  27  ILE A CG2   1 
ATOM   188  C CD1   . ILE A 1 27  ? -2.896  28.812  56.100 1.00 21.36 ?  27  ILE A CD1   1 
ATOM   189  N N     . HIS A 1 28  ? -1.697  23.833  58.605 1.00 26.02 ?  28  HIS A N     1 
ATOM   190  C CA    . HIS A 1 28  ? -1.109  23.018  59.660 1.00 27.84 ?  28  HIS A CA    1 
ATOM   191  C C     . HIS A 1 28  ? 0.307   23.446  60.004 1.00 37.93 ?  28  HIS A C     1 
ATOM   192  O O     . HIS A 1 28  ? 1.174   23.511  59.122 1.00 44.50 ?  28  HIS A O     1 
ATOM   193  C CB    . HIS A 1 28  ? -1.116  21.552  59.254 1.00 26.67 ?  28  HIS A CB    1 
ATOM   194  C CG    . HIS A 1 28  ? -2.487  21.014  59.031 1.00 8.54  ?  28  HIS A CG    1 
ATOM   195  N ND1   . HIS A 1 28  ? -3.012  20.811  57.775 1.00 11.98 ?  28  HIS A ND1   1 
ATOM   196  C CD2   . HIS A 1 28  ? -3.451  20.667  59.908 1.00 9.82  ?  28  HIS A CD2   1 
ATOM   197  C CE1   . HIS A 1 28  ? -4.235  20.331  57.886 1.00 17.12 ?  28  HIS A CE1   1 
ATOM   198  N NE2   . HIS A 1 28  ? -4.525  20.235  59.172 1.00 20.17 ?  28  HIS A NE2   1 
ATOM   199  N N     . ALA A 1 29  ? 0.547   23.690  61.305 1.00 30.34 ?  29  ALA A N     1 
ATOM   200  C CA    . ALA A 1 29  ? 1.861   24.088  61.788 1.00 27.87 ?  29  ALA A CA    1 
ATOM   201  C C     . ALA A 1 29  ? 2.176   23.486  63.157 1.00 24.99 ?  29  ALA A C     1 
ATOM   202  O O     . ALA A 1 29  ? 2.864   24.115  63.971 1.00 38.25 ?  29  ALA A O     1 
ATOM   203  C CB    . ALA A 1 29  ? 1.971   25.616  61.836 1.00 47.27 ?  29  ALA A CB    1 
ATOM   204  N N     . TRP A 1 30  ? 1.697   22.273  63.435 1.00 31.89 ?  30  TRP A N     1 
ATOM   205  C CA    . TRP A 1 30  ? 1.829   21.680  64.766 1.00 33.94 ?  30  TRP A CA    1 
ATOM   206  C C     . TRP A 1 30  ? 3.040   20.749  64.879 1.00 40.98 ?  30  TRP A C     1 
ATOM   207  O O     . TRP A 1 30  ? 3.974   21.040  65.632 1.00 48.23 ?  30  TRP A O     1 
ATOM   208  C CB    . TRP A 1 30  ? 0.518   20.955  65.169 1.00 12.93 ?  30  TRP A CB    1 
ATOM   209  C CG    . TRP A 1 30  ? -0.019  19.974  64.167 1.00 10.74 ?  30  TRP A CG    1 
ATOM   210  C CD1   . TRP A 1 30  ? -0.454  20.245  62.901 1.00 17.61 ?  30  TRP A CD1   1 
ATOM   211  C CD2   . TRP A 1 30  ? -0.180  18.560  64.349 1.00 18.91 ?  30  TRP A CD2   1 
ATOM   212  N NE1   . TRP A 1 30  ? -0.866  19.082  62.277 1.00 26.23 ?  30  TRP A NE1   1 
ATOM   213  C CE2   . TRP A 1 30  ? -0.711  18.038  63.152 1.00 20.10 ?  30  TRP A CE2   1 
ATOM   214  C CE3   . TRP A 1 30  ? 0.079   17.680  65.408 1.00 32.89 ?  30  TRP A CE3   1 
ATOM   215  C CZ2   . TRP A 1 30  ? -0.988  16.682  62.987 1.00 16.82 ?  30  TRP A CZ2   1 
ATOM   216  C CZ3   . TRP A 1 30  ? -0.202  16.322  65.237 1.00 21.00 ?  30  TRP A CZ3   1 
ATOM   217  C CH2   . TRP A 1 30  ? -0.724  15.844  64.038 1.00 9.32  ?  30  TRP A CH2   1 
ATOM   218  N N     . ILE A 1 31  ? 3.072   19.653  64.116 1.00 31.65 ?  31  ILE A N     1 
ATOM   219  C CA    . ILE A 1 31  ? 4.155   18.673  64.245 1.00 25.24 ?  31  ILE A CA    1 
ATOM   220  C C     . ILE A 1 31  ? 5.470   19.264  63.738 1.00 4.21  ?  31  ILE A C     1 
ATOM   221  O O     . ILE A 1 31  ? 5.483   20.155  62.889 1.00 35.93 ?  31  ILE A O     1 
ATOM   222  C CB    . ILE A 1 31  ? 3.773   17.380  63.494 1.00 22.47 ?  31  ILE A CB    1 
ATOM   223  C CG1   . ILE A 1 31  ? 4.381   16.153  64.169 1.00 13.47 ?  31  ILE A CG1   1 
ATOM   224  C CG2   . ILE A 1 31  ? 4.181   17.456  62.041 1.00 23.24 ?  31  ILE A CG2   1 
ATOM   225  C CD1   . ILE A 1 31  ? 3.932   14.884  63.574 1.00 4.00  ?  31  ILE A CD1   1 
ATOM   226  N N     . ALA A 1 32  ? 6.593   18.789  64.277 1.00 7.60  ?  32  ALA A N     1 
ATOM   227  C CA    . ALA A 1 32  ? 7.898   19.443  64.057 1.00 4.17  ?  32  ALA A CA    1 
ATOM   228  C C     . ALA A 1 32  ? 8.671   18.876  62.874 1.00 5.19  ?  32  ALA A C     1 
ATOM   229  O O     . ALA A 1 32  ? 9.834   18.527  63.019 1.00 26.39 ?  32  ALA A O     1 
ATOM   230  C CB    . ALA A 1 32  ? 8.750   19.341  65.315 1.00 3.71  ?  32  ALA A CB    1 
ATOM   231  N N     . ASP A 1 33  ? 8.058   18.807  61.695 1.00 22.45 ?  33  ASP A N     1 
ATOM   232  C CA    . ASP A 1 33  ? 8.745   18.500  60.449 1.00 5.76  ?  33  ASP A CA    1 
ATOM   233  C C     . ASP A 1 33  ? 8.552   19.652  59.476 1.00 6.33  ?  33  ASP A C     1 
ATOM   234  O O     . ASP A 1 33  ? 7.568   20.389  59.544 1.00 13.69 ?  33  ASP A O     1 
ATOM   235  C CB    . ASP A 1 33  ? 8.267   17.149  59.814 1.00 27.84 ?  33  ASP A CB    1 
ATOM   236  C CG    . ASP A 1 33  ? 6.778   17.135  59.400 1.00 33.11 ?  33  ASP A CG    1 
ATOM   237  O OD1   . ASP A 1 33  ? 6.027   18.114  59.635 1.00 28.45 ?  33  ASP A OD1   1 
ATOM   238  O OD2   . ASP A 1 33  ? 6.357   16.108  58.812 1.00 31.71 -1 33  ASP A OD2   1 
ATOM   239  N N     . MET A 1 34  ? 9.516   19.829  58.594 1.00 22.97 ?  34  MET A N     1 
ATOM   240  C CA    . MET A 1 34  ? 9.515   20.973  57.699 1.00 26.05 ?  34  MET A CA    1 
ATOM   241  C C     . MET A 1 34  ? 8.793   20.700  56.384 1.00 25.39 ?  34  MET A C     1 
ATOM   242  O O     . MET A 1 34  ? 8.667   19.558  55.942 1.00 30.89 ?  34  MET A O     1 
ATOM   243  C CB    . MET A 1 34  ? 10.947  21.404  57.426 1.00 19.88 ?  34  MET A CB    1 
ATOM   244  C CG    . MET A 1 34  ? 11.550  22.040  58.610 1.00 10.44 ?  34  MET A CG    1 
ATOM   245  S SD    . MET A 1 34  ? 13.237  22.404  58.192 1.00 29.66 ?  34  MET A SD    1 
ATOM   246  C CE    . MET A 1 34  ? 13.932  20.770  58.040 1.00 21.65 ?  34  MET A CE    1 
ATOM   247  N N     . ASP A 1 35  ? 8.300   21.770  55.770 1.00 18.07 ?  35  ASP A N     1 
ATOM   248  C CA    . ASP A 1 35  ? 7.711   21.700  54.437 1.00 31.36 ?  35  ASP A CA    1 
ATOM   249  C C     . ASP A 1 35  ? 8.721   22.100  53.375 1.00 41.17 ?  35  ASP A C     1 
ATOM   250  O O     . ASP A 1 35  ? 8.375   22.753  52.388 1.00 44.93 ?  35  ASP A O     1 
ATOM   251  C CB    . ASP A 1 35  ? 6.473   22.587  54.346 1.00 31.91 ?  35  ASP A CB    1 
ATOM   252  C CG    . ASP A 1 35  ? 5.335   22.077  55.187 1.00 33.32 ?  35  ASP A CG    1 
ATOM   253  O OD1   . ASP A 1 35  ? 5.280   20.861  55.435 1.00 39.57 ?  35  ASP A OD1   1 
ATOM   254  O OD2   . ASP A 1 35  ? 4.483   22.890  55.589 1.00 41.42 -1 35  ASP A OD2   1 
ATOM   255  N N     . PHE A 1 36  ? 9.973   21.693  53.532 1.00 32.91 ?  36  PHE A N     1 
ATOM   256  C CA    . PHE A 1 36  ? 11.019  22.093  52.612 1.00 30.48 ?  36  PHE A CA    1 
ATOM   257  C C     . PHE A 1 36  ? 11.538  20.885  51.856 1.00 42.04 ?  36  PHE A C     1 
ATOM   258  O O     . PHE A 1 36  ? 11.531  19.761  52.364 1.00 52.04 ?  36  PHE A O     1 
ATOM   259  C CB    . PHE A 1 36  ? 12.154  22.795  53.363 1.00 28.82 ?  36  PHE A CB    1 
ATOM   260  C CG    . PHE A 1 36  ? 11.792  24.187  53.802 1.00 33.82 ?  36  PHE A CG    1 
ATOM   261  C CD1   . PHE A 1 36  ? 11.188  25.061  52.916 1.00 20.72 ?  36  PHE A CD1   1 
ATOM   262  C CD2   . PHE A 1 36  ? 12.019  24.610  55.100 1.00 35.84 ?  36  PHE A CD2   1 
ATOM   263  C CE1   . PHE A 1 36  ? 10.839  26.323  53.312 1.00 30.69 ?  36  PHE A CE1   1 
ATOM   264  C CE2   . PHE A 1 36  ? 11.669  25.879  55.496 1.00 30.48 ?  36  PHE A CE2   1 
ATOM   265  C CZ    . PHE A 1 36  ? 11.083  26.736  54.602 1.00 33.74 ?  36  PHE A CZ    1 
ATOM   266  N N     . GLU A 1 37  ? 11.982  21.129  50.629 1.00 41.16 ?  37  GLU A N     1 
ATOM   267  C CA    . GLU A 1 37  ? 12.641  20.080  49.874 1.00 32.92 ?  37  GLU A CA    1 
ATOM   268  C C     . GLU A 1 37  ? 13.841  19.594  50.661 1.00 33.07 ?  37  GLU A C     1 
ATOM   269  O O     . GLU A 1 37  ? 14.602  20.393  51.210 1.00 34.12 ?  37  GLU A O     1 
ATOM   270  C CB    . GLU A 1 37  ? 13.084  20.597  48.507 1.00 33.94 ?  37  GLU A CB    1 
ATOM   271  C CG    . GLU A 1 37  ? 12.207  20.159  47.355 1.00 40.88 ?  37  GLU A CG    1 
ATOM   272  C CD    . GLU A 1 37  ? 12.798  20.552  46.025 1.00 47.54 ?  37  GLU A CD    1 
ATOM   273  O OE1   . GLU A 1 37  ? 13.868  21.190  46.029 1.00 45.64 ?  37  GLU A OE1   1 
ATOM   274  O OE2   . GLU A 1 37  ? 12.198  20.233  44.979 1.00 50.77 -1 37  GLU A OE2   1 
ATOM   275  N N     . VAL A 1 38  ? 13.954  18.282  50.797 1.00 37.91 ?  38  VAL A N     1 
ATOM   276  C CA    . VAL A 1 38  ? 15.161  17.688  51.352 1.00 28.99 ?  38  VAL A CA    1 
ATOM   277  C C     . VAL A 1 38  ? 16.301  18.066  50.416 1.00 26.71 ?  38  VAL A C     1 
ATOM   278  O O     . VAL A 1 38  ? 16.069  18.235  49.211 1.00 29.27 ?  38  VAL A O     1 
ATOM   279  C CB    . VAL A 1 38  ? 15.016  16.168  51.519 1.00 18.29 ?  38  VAL A CB    1 
ATOM   280  C CG1   . VAL A 1 38  ? 13.900  15.869  52.493 1.00 14.98 ?  38  VAL A CG1   1 
ATOM   281  C CG2   . VAL A 1 38  ? 14.766  15.487  50.176 1.00 17.39 ?  38  VAL A CG2   1 
ATOM   282  N N     . PRO A 1 39  ? 17.523  18.245  50.917 1.00 24.00 ?  39  PRO A N     1 
ATOM   283  C CA    . PRO A 1 39  ? 18.664  18.456  50.023 1.00 21.40 ?  39  PRO A CA    1 
ATOM   284  C C     . PRO A 1 39  ? 18.669  17.438  48.894 1.00 25.08 ?  39  PRO A C     1 
ATOM   285  O O     . PRO A 1 39  ? 18.382  16.257  49.097 1.00 26.25 ?  39  PRO A O     1 
ATOM   286  C CB    . PRO A 1 39  ? 19.875  18.274  50.939 1.00 25.42 ?  39  PRO A CB    1 
ATOM   287  C CG    . PRO A 1 39  ? 19.393  18.528  52.288 1.00 28.75 ?  39  PRO A CG    1 
ATOM   288  C CD    . PRO A 1 39  ? 17.897  18.370  52.333 1.00 26.52 ?  39  PRO A CD    1 
ATOM   289  N N     . LYS A 1 40  ? 18.966  17.920  47.693 1.00 26.40 ?  40  LYS A N     1 
ATOM   290  C CA    . LYS A 1 40  ? 19.001  17.048  46.523 1.00 42.85 ?  40  LYS A CA    1 
ATOM   291  C C     . LYS A 1 40  ? 19.975  15.870  46.653 1.00 48.23 ?  40  LYS A C     1 
ATOM   292  O O     . LYS A 1 40  ? 19.627  14.768  46.190 1.00 48.42 ?  40  LYS A O     1 
ATOM   293  C CB    . LYS A 1 40  ? 19.342  17.898  45.290 1.00 43.89 ?  40  LYS A CB    1 
ATOM   294  C CG    . LYS A 1 40  ? 19.104  17.223  43.951 1.00 45.11 ?  40  LYS A CG    1 
ATOM   295  C CD    . LYS A 1 40  ? 17.677  17.439  43.492 1.00 46.83 ?  40  LYS A CD    1 
ATOM   296  C CE    . LYS A 1 40  ? 17.473  16.985  42.047 1.00 47.65 ?  40  LYS A CE    1 
ATOM   297  N NZ    . LYS A 1 40  ? 16.136  17.370  41.499 1.00 47.43 1  40  LYS A NZ    1 
ATOM   298  N N     . PRO A 1 41  ? 21.175  16.013  47.233 1.00 45.95 ?  41  PRO A N     1 
ATOM   299  C CA    . PRO A 1 41  ? 22.064  14.845  47.367 1.00 44.50 ?  41  PRO A CA    1 
ATOM   300  C C     . PRO A 1 41  ? 21.494  13.720  48.219 1.00 40.58 ?  41  PRO A C     1 
ATOM   301  O O     . PRO A 1 41  ? 21.956  12.580  48.095 1.00 44.95 ?  41  PRO A O     1 
ATOM   302  C CB    . PRO A 1 41  ? 23.332  15.437  47.985 1.00 38.67 ?  41  PRO A CB    1 
ATOM   303  C CG    . PRO A 1 41  ? 23.276  16.875  47.675 1.00 34.27 ?  41  PRO A CG    1 
ATOM   304  C CD    . PRO A 1 41  ? 21.853  17.258  47.626 1.00 29.49 ?  41  PRO A CD    1 
ATOM   305  N N     . ILE A 1 42  ? 20.538  13.998  49.104 1.00 32.03 ?  42  ILE A N     1 
ATOM   306  C CA    . ILE A 1 42  ? 19.834  12.903  49.759 1.00 30.58 ?  42  ILE A CA    1 
ATOM   307  C C     . ILE A 1 42  ? 18.924  12.198  48.761 1.00 39.30 ?  42  ILE A C     1 
ATOM   308  O O     . ILE A 1 42  ? 18.846  10.964  48.733 1.00 43.09 ?  42  ILE A O     1 
ATOM   309  C CB    . ILE A 1 42  ? 19.048  13.414  50.977 1.00 27.37 ?  42  ILE A CB    1 
ATOM   310  C CG1   . ILE A 1 42  ? 20.003  13.813  52.101 1.00 25.78 ?  42  ILE A CG1   1 
ATOM   311  C CG2   . ILE A 1 42  ? 18.053  12.358  51.447 1.00 28.46 ?  42  ILE A CG2   1 
ATOM   312  C CD1   . ILE A 1 42  ? 19.299  14.406  53.309 1.00 33.80 ?  42  ILE A CD1   1 
ATOM   313  N N     . GLN A 1 43  ? 18.210  12.968  47.938 1.00 28.40 ?  43  GLN A N     1 
ATOM   314  C CA    . GLN A 1 43  ? 17.369  12.368  46.912 1.00 19.04 ?  43  GLN A CA    1 
ATOM   315  C C     . GLN A 1 43  ? 18.200  11.551  45.941 1.00 23.54 ?  43  GLN A C     1 
ATOM   316  O O     . GLN A 1 43  ? 17.754  10.507  45.457 1.00 33.74 ?  43  GLN A O     1 
ATOM   317  C CB    . GLN A 1 43  ? 16.636  13.466  46.150 1.00 31.44 ?  43  GLN A CB    1 
ATOM   318  C CG    . GLN A 1 43  ? 16.178  14.617  47.023 1.00 32.67 ?  43  GLN A CG    1 
ATOM   319  C CD    . GLN A 1 43  ? 15.393  15.633  46.250 1.00 37.39 ?  43  GLN A CD    1 
ATOM   320  O OE1   . GLN A 1 43  ? 14.488  15.285  45.490 1.00 46.21 ?  43  GLN A OE1   1 
ATOM   321  N NE2   . GLN A 1 43  ? 15.717  16.905  46.452 1.00 35.58 ?  43  GLN A NE2   1 
ATOM   322  N N     . THR A 1 44  ? 19.429  11.989  45.667 1.00 35.03 ?  44  THR A N     1 
ATOM   323  C CA    . THR A 1 44  ? 20.259  11.254  44.722 1.00 41.25 ?  44  THR A CA    1 
ATOM   324  C C     . THR A 1 44  ? 20.804  9.980   45.349 1.00 31.09 ?  44  THR A C     1 
ATOM   325  O O     . THR A 1 44  ? 20.884  8.948   44.679 1.00 45.79 ?  44  THR A O     1 
ATOM   326  C CB    . THR A 1 44  ? 21.402  12.137  44.218 1.00 43.70 ?  44  THR A CB    1 
ATOM   327  O OG1   . THR A 1 44  ? 20.868  13.306  43.586 1.00 47.80 ?  44  THR A OG1   1 
ATOM   328  C CG2   . THR A 1 44  ? 22.263  11.385  43.215 1.00 39.86 ?  44  THR A CG2   1 
ATOM   329  N N     . ALA A 1 45  ? 21.134  10.023  46.643 1.00 13.72 ?  45  ALA A N     1 
ATOM   330  C CA    . ALA A 1 45  ? 21.585  8.822   47.342 1.00 21.11 ?  45  ALA A CA    1 
ATOM   331  C C     . ALA A 1 45  ? 20.479  7.780   47.435 1.00 34.81 ?  45  ALA A C     1 
ATOM   332  O O     . ALA A 1 45  ? 20.745  6.575   47.346 1.00 44.59 ?  45  ALA A O     1 
ATOM   333  C CB    . ALA A 1 45  ? 22.084  9.188   48.738 1.00 23.44 ?  45  ALA A CB    1 
ATOM   334  N N     . LEU A 1 46  ? 19.235  8.225   47.645 1.00 42.76 ?  46  LEU A N     1 
ATOM   335  C CA    . LEU A 1 46  ? 18.104  7.304   47.734 1.00 28.82 ?  46  LEU A CA    1 
ATOM   336  C C     . LEU A 1 46  ? 17.745  6.717   46.375 1.00 24.45 ?  46  LEU A C     1 
ATOM   337  O O     . LEU A 1 46  ? 17.390  5.537   46.284 1.00 35.28 ?  46  LEU A O     1 
ATOM   338  C CB    . LEU A 1 46  ? 16.894  8.013   48.334 1.00 18.76 ?  46  LEU A CB    1 
ATOM   339  C CG    . LEU A 1 46  ? 16.994  8.363   49.810 1.00 22.72 ?  46  LEU A CG    1 
ATOM   340  C CD1   . LEU A 1 46  ? 15.644  8.779   50.356 1.00 22.15 ?  46  LEU A CD1   1 
ATOM   341  C CD2   . LEU A 1 46  ? 17.555  7.191   50.576 1.00 30.30 ?  46  LEU A CD2   1 
ATOM   342  N N     . LYS A 1 47  ? 17.814  7.519   45.309 1.00 18.86 ?  47  LYS A N     1 
ATOM   343  C CA    . LYS A 1 47  ? 17.516  6.989   43.982 1.00 27.24 ?  47  LYS A CA    1 
ATOM   344  C C     . LYS A 1 47  ? 18.652  6.117   43.457 1.00 40.44 ?  47  LYS A C     1 
ATOM   345  O O     . LYS A 1 47  ? 18.408  5.153   42.719 1.00 47.26 ?  47  LYS A O     1 
ATOM   346  C CB    . LYS A 1 47  ? 17.248  8.131   43.001 1.00 30.11 ?  47  LYS A CB    1 
ATOM   347  C CG    . LYS A 1 47  ? 17.074  7.672   41.560 1.00 33.83 ?  47  LYS A CG    1 
ATOM   348  C CD    . LYS A 1 47  ? 18.117  8.303   40.634 1.00 36.42 ?  47  LYS A CD    1 
ATOM   349  C CE    . LYS A 1 47  ? 19.435  7.527   40.617 1.00 34.74 ?  47  LYS A CE    1 
ATOM   350  N NZ    . LYS A 1 47  ? 20.326  7.963   39.517 1.00 36.68 1  47  LYS A NZ    1 
ATOM   351  N N     . GLN A 1 48  ? 19.890  6.421   43.849 1.00 37.54 ?  48  GLN A N     1 
ATOM   352  C CA    . GLN A 1 48  ? 21.014  5.558   43.503 1.00 31.95 ?  48  GLN A CA    1 
ATOM   353  C C     . GLN A 1 48  ? 20.850  4.174   44.116 1.00 36.25 ?  48  GLN A C     1 
ATOM   354  O O     . GLN A 1 48  ? 21.178  3.167   43.481 1.00 56.17 ?  48  GLN A O     1 
ATOM   355  C CB    . GLN A 1 48  ? 22.320  6.199   43.975 1.00 36.19 ?  48  GLN A CB    1 
ATOM   356  C CG    . GLN A 1 48  ? 23.593  5.656   43.345 1.00 47.14 ?  48  GLN A CG    1 
ATOM   357  C CD    . GLN A 1 48  ? 24.827  6.436   43.793 1.00 51.54 ?  48  GLN A CD    1 
ATOM   358  O OE1   . GLN A 1 48  ? 24.764  7.225   44.738 1.00 59.50 ?  48  GLN A OE1   1 
ATOM   359  N NE2   . GLN A 1 48  ? 25.946  6.231   43.106 1.00 40.18 ?  48  GLN A NE2   1 
ATOM   360  N N     . ARG A 1 49  ? 20.322  4.082   45.333 1.00 32.22 ?  49  ARG A N     1 
ATOM   361  C CA    . ARG A 1 49  ? 20.210  2.773   46.036 1.00 36.37 ?  49  ARG A CA    1 
ATOM   362  C C     . ARG A 1 49  ? 19.156  1.905   45.358 1.00 40.21 ?  49  ARG A C     1 
ATOM   363  O O     . ARG A 1 49  ? 19.357  0.712   45.227 1.00 42.85 ?  49  ARG A O     1 
ATOM   364  C CB    . ARG A 1 49  ? 19.923  2.957   47.528 1.00 33.02 ?  49  ARG A CB    1 
ATOM   365  C CG    . ARG A 1 49  ? 19.915  1.680   48.353 1.00 38.22 ?  49  ARG A CG    1 
ATOM   366  C CD    . ARG A 1 49  ? 21.024  0.697   48.025 1.00 40.78 ?  49  ARG A CD    1 
ATOM   367  N NE    . ARG A 1 49  ? 20.897  -0.529  48.791 1.00 39.34 ?  49  ARG A NE    1 
ATOM   368  C CZ    . ARG A 1 49  ? 20.091  -1.537  48.491 1.00 39.64 ?  49  ARG A CZ    1 
ATOM   369  N NH1   . ARG A 1 49  ? 19.331  -1.491  47.413 1.00 33.84 1  49  ARG A NH1   1 
ATOM   370  N NH2   . ARG A 1 49  ? 20.054  -2.595  49.275 1.00 34.75 ?  49  ARG A NH2   1 
ATOM   371  N N     . ILE A 1 50  ? 18.070  2.514   44.930 1.00 44.42 ?  50  ILE A N     1 
ATOM   372  C CA    . ILE A 1 50  ? 17.003  1.715   44.347 1.00 37.66 ?  50  ILE A CA    1 
ATOM   373  C C     . ILE A 1 50  ? 17.429  1.118   43.017 1.00 39.70 ?  50  ILE A C     1 
ATOM   374  O O     . ILE A 1 50  ? 16.848  0.128   42.570 1.00 60.00 ?  50  ILE A O     1 
ATOM   375  C CB    . ILE A 1 50  ? 15.732  2.568   44.225 1.00 35.96 ?  50  ILE A CB    1 
ATOM   376  C CG1   . ILE A 1 50  ? 15.316  3.050   45.615 1.00 32.20 ?  50  ILE A CG1   1 
ATOM   377  C CG2   . ILE A 1 50  ? 14.602  1.794   43.570 1.00 45.59 ?  50  ILE A CG2   1 
ATOM   378  C CD1   . ILE A 1 50  ? 13.850  3.311   45.764 1.00 33.90 ?  50  ILE A CD1   1 
ATOM   379  N N     . LYS A 1 51  ? 18.463  1.662   42.379 1.00 31.81 ?  51  LYS A N     1 
ATOM   380  C CA    . LYS A 1 51  ? 18.980  1.008   41.188 1.00 32.58 ?  51  LYS A CA    1 
ATOM   381  C C     . LYS A 1 51  ? 19.509  -0.390  41.498 1.00 43.89 ?  51  LYS A C     1 
ATOM   382  O O     . LYS A 1 51  ? 19.681  -1.196  40.577 1.00 51.14 ?  51  LYS A O     1 
ATOM   383  C CB    . LYS A 1 51  ? 20.077  1.860   40.550 1.00 29.44 ?  51  LYS A CB    1 
ATOM   384  C CG    . LYS A 1 51  ? 19.607  3.186   39.989 1.00 30.97 ?  51  LYS A CG    1 
ATOM   385  C CD    . LYS A 1 51  ? 18.793  3.006   38.729 1.00 40.25 ?  51  LYS A CD    1 
ATOM   386  C CE    . LYS A 1 51  ? 18.419  4.350   38.114 1.00 43.69 ?  51  LYS A CE    1 
ATOM   387  N NZ    . LYS A 1 51  ? 19.599  5.091   37.618 1.00 43.96 1  51  LYS A NZ    1 
ATOM   388  N N     . HIS A 1 52  ? 19.741  -0.709  42.776 1.00 40.47 ?  52  HIS A N     1 
ATOM   389  C CA    . HIS A 1 52  ? 20.098  -2.059  43.191 1.00 39.61 ?  52  HIS A CA    1 
ATOM   390  C C     . HIS A 1 52  ? 18.864  -2.727  43.799 1.00 43.11 ?  52  HIS A C     1 
ATOM   391  O O     . HIS A 1 52  ? 18.552  -2.490  44.976 1.00 35.92 ?  52  HIS A O     1 
ATOM   392  C CB    . HIS A 1 52  ? 21.254  -2.042  44.193 1.00 34.78 ?  52  HIS A CB    1 
ATOM   393  C CG    . HIS A 1 52  ? 21.789  -3.403  44.508 1.00 38.58 ?  52  HIS A CG    1 
ATOM   394  N ND1   . HIS A 1 52  ? 21.701  -3.966  45.763 1.00 36.07 ?  52  HIS A ND1   1 
ATOM   395  C CD2   . HIS A 1 52  ? 22.398  -4.322  43.723 1.00 37.33 ?  52  HIS A CD2   1 
ATOM   396  C CE1   . HIS A 1 52  ? 22.243  -5.169  45.740 1.00 37.01 ?  52  HIS A CE1   1 
ATOM   397  N NE2   . HIS A 1 52  ? 22.672  -5.410  44.514 1.00 38.07 ?  52  HIS A NE2   1 
ATOM   398  N N     . PRO A 1 53  ? 18.112  -3.571  43.022 1.00 44.28 ?  53  PRO A N     1 
ATOM   399  C CA    . PRO A 1 53  ? 16.801  -4.098  43.429 1.00 43.26 ?  53  PRO A CA    1 
ATOM   400  C C     . PRO A 1 53  ? 16.821  -5.273  44.409 1.00 40.62 ?  53  PRO A C     1 
ATOM   401  O O     . PRO A 1 53  ? 16.142  -6.282  44.209 1.00 41.33 ?  53  PRO A O     1 
ATOM   402  C CB    . PRO A 1 53  ? 16.183  -4.514  42.091 1.00 43.86 ?  53  PRO A CB    1 
ATOM   403  C CG    . PRO A 1 53  ? 17.343  -4.887  41.262 1.00 43.31 ?  53  PRO A CG    1 
ATOM   404  C CD    . PRO A 1 53  ? 18.475  -3.990  41.657 1.00 39.57 ?  53  PRO A CD    1 
ATOM   405  N N     . ILE A 1 54  ? 17.561  -5.121  45.504 1.00 30.81 ?  54  ILE A N     1 
ATOM   406  C CA    . ILE A 1 54  ? 17.620  -6.128  46.598 1.00 29.72 ?  54  ILE A CA    1 
ATOM   407  C C     . ILE A 1 54  ? 17.737  -5.302  47.875 1.00 30.15 ?  54  ILE A C     1 
ATOM   408  O O     . ILE A 1 54  ? 18.585  -4.420  47.918 1.00 36.71 ?  54  ILE A O     1 
ATOM   409  C CB    . ILE A 1 54  ? 18.829  -7.078  46.475 1.00 38.79 ?  54  ILE A CB    1 
ATOM   410  C CG1   . ILE A 1 54  ? 18.882  -7.817  45.136 1.00 50.05 ?  54  ILE A CG1   1 
ATOM   411  C CG2   . ILE A 1 54  ? 18.900  -8.035  47.645 1.00 42.67 ?  54  ILE A CG2   1 
ATOM   412  C CD1   . ILE A 1 54  ? 19.698  -9.076  45.160 1.00 53.38 ?  54  ILE A CD1   1 
ATOM   413  N N     . PHE A 1 55  ? 16.946  -5.608  48.877 1.00 10.66 ?  55  PHE A N     1 
ATOM   414  C CA    . PHE A 1 55  ? 16.906  -4.863  50.126 1.00 13.19 ?  55  PHE A CA    1 
ATOM   415  C C     . PHE A 1 55  ? 17.117  -5.807  51.294 1.00 10.22 ?  55  PHE A C     1 
ATOM   416  O O     . PHE A 1 55  ? 16.453  -5.742  52.329 1.00 15.68 ?  55  PHE A O     1 
ATOM   417  C CB    . PHE A 1 55  ? 15.591  -4.089  50.201 1.00 16.87 ?  55  PHE A CB    1 
ATOM   418  C CG    . PHE A 1 55  ? 15.278  -3.344  48.935 1.00 25.88 ?  55  PHE A CG    1 
ATOM   419  C CD1   . PHE A 1 55  ? 15.827  -2.097  48.701 1.00 33.07 ?  55  PHE A CD1   1 
ATOM   420  C CD2   . PHE A 1 55  ? 14.476  -3.904  47.956 1.00 26.04 ?  55  PHE A CD2   1 
ATOM   421  C CE1   . PHE A 1 55  ? 15.568  -1.415  47.520 1.00 24.80 ?  55  PHE A CE1   1 
ATOM   422  C CE2   . PHE A 1 55  ? 14.219  -3.226  46.776 1.00 32.43 ?  55  PHE A CE2   1 
ATOM   423  C CZ    . PHE A 1 55  ? 14.767  -1.978  46.562 1.00 24.13 ?  55  PHE A CZ    1 
ATOM   424  N N     . GLY A 1 56  ? 18.121  -6.663  51.167 1.00 19.65 ?  56  GLY A N     1 
ATOM   425  C CA    . GLY A 1 56  ? 18.378  -7.620  52.218 1.00 27.56 ?  56  GLY A CA    1 
ATOM   426  C C     . GLY A 1 56  ? 19.000  -6.956  53.416 1.00 28.51 ?  56  GLY A C     1 
ATOM   427  O O     . GLY A 1 56  ? 18.978  -5.729  53.528 1.00 40.36 ?  56  GLY A O     1 
ATOM   428  N N     . TYR A 1 57  ? 19.568  -7.750  54.292 1.00 25.18 ?  57  TYR A N     1 
ATOM   429  C CA    . TYR A 1 57  ? 20.220  -7.222  55.507 1.00 15.04 ?  57  TYR A CA    1 
ATOM   430  C C     . TYR A 1 57  ? 21.509  -6.523  55.132 1.00 24.06 ?  57  TYR A C     1 
ATOM   431  O O     . TYR A 1 57  ? 22.309  -7.066  54.384 1.00 20.10 ?  57  TYR A O     1 
ATOM   432  C CB    . TYR A 1 57  ? 20.507  -8.342  56.493 1.00 27.35 ?  57  TYR A CB    1 
ATOM   433  C CG    . TYR A 1 57  ? 19.300  -9.103  56.935 1.00 25.84 ?  57  TYR A CG    1 
ATOM   434  C CD1   . TYR A 1 57  ? 18.466  -8.576  57.894 1.00 21.06 ?  57  TYR A CD1   1 
ATOM   435  C CD2   . TYR A 1 57  ? 19.002  -10.333 56.386 1.00 28.92 ?  57  TYR A CD2   1 
ATOM   436  C CE1   . TYR A 1 57  ? 17.356  -9.273  58.313 1.00 34.95 ?  57  TYR A CE1   1 
ATOM   437  C CE2   . TYR A 1 57  ? 17.891  -11.041 56.787 1.00 29.18 ?  57  TYR A CE2   1 
ATOM   438  C CZ    . TYR A 1 57  ? 17.078  -10.507 57.761 1.00 33.38 ?  57  TYR A CZ    1 
ATOM   439  O OH    . TYR A 1 57  ? 15.973  -11.175 58.159 1.00 25.86 ?  57  TYR A OH    1 
ATOM   440  N N     . THR A 1 58  ? 21.680  -5.343  55.693 1.00 28.45 ?  58  THR A N     1 
ATOM   441  C CA    . THR A 1 58  ? 22.811  -4.514  55.323 1.00 26.14 ?  58  THR A CA    1 
ATOM   442  C C     . THR A 1 58  ? 23.568  -4.110  56.576 1.00 29.49 ?  58  THR A C     1 
ATOM   443  O O     . THR A 1 58  ? 22.995  -4.009  57.667 1.00 13.67 ?  58  THR A O     1 
ATOM   444  C CB    . THR A 1 58  ? 22.406  -3.242  54.541 1.00 34.63 ?  58  THR A CB    1 
ATOM   445  O OG1   . THR A 1 58  ? 21.766  -2.307  55.413 1.00 39.46 ?  58  THR A OG1   1 
ATOM   446  C CG2   . THR A 1 58  ? 21.485  -3.580  53.380 1.00 35.47 ?  58  THR A CG2   1 
ATOM   447  N N     . LEU A 1 59  ? 24.924  -3.910  56.400 1.00 39.56 ?  59  LEU A N     1 
ATOM   448  C CA    . LEU A 1 59  ? 25.853  -3.371  57.373 1.00 18.19 ?  59  LEU A CA    1 
ATOM   449  C C     . LEU A 1 59  ? 25.846  -1.850  57.302 1.00 7.39  ?  59  LEU A C     1 
ATOM   450  O O     . LEU A 1 59  ? 25.653  -1.268  56.228 1.00 13.75 ?  59  LEU A O     1 
ATOM   451  C CB    . LEU A 1 59  ? 27.263  -3.865  57.077 1.00 23.27 ?  59  LEU A CB    1 
ATOM   452  C CG    . LEU A 1 59  ? 27.558  -5.363  56.942 1.00 22.16 ?  59  LEU A CG    1 
ATOM   453  C CD1   . LEU A 1 59  ? 28.455  -5.652  55.734 1.00 12.57 ?  59  LEU A CD1   1 
ATOM   454  C CD2   . LEU A 1 59  ? 28.189  -5.923  58.228 1.00 11.46 ?  59  LEU A CD2   1 
ATOM   455  N N     . PRO A 1 60  ? 26.170  -1.203  58.415 1.00 8.89  ?  60  PRO A N     1 
ATOM   456  C CA    . PRO A 1 60  ? 26.521  0.215   58.359 1.00 10.04 ?  60  PRO A CA    1 
ATOM   457  C C     . PRO A 1 60  ? 27.643  0.439   57.357 1.00 19.04 ?  60  PRO A C     1 
ATOM   458  O O     . PRO A 1 60  ? 28.518  -0.427  57.183 1.00 28.03 ?  60  PRO A O     1 
ATOM   459  C CB    . PRO A 1 60  ? 26.988  0.522   59.788 1.00 8.97  ?  60  PRO A CB    1 
ATOM   460  C CG    . PRO A 1 60  ? 26.323  -0.528  60.643 1.00 21.15 ?  60  PRO A CG    1 
ATOM   461  C CD    . PRO A 1 60  ? 26.031  -1.725  59.785 1.00 6.51  ?  60  PRO A CD    1 
ATOM   462  N N     . PRO A 1 61  ? 27.615  1.560   56.632 1.00 13.24 ?  61  PRO A N     1 
ATOM   463  C CA    . PRO A 1 61  ? 28.653  1.807   55.615 1.00 13.69 ?  61  PRO A CA    1 
ATOM   464  C C     . PRO A 1 61  ? 30.063  1.836   56.211 1.00 19.15 ?  61  PRO A C     1 
ATOM   465  O O     . PRO A 1 61  ? 30.252  2.032   57.412 1.00 24.11 ?  61  PRO A O     1 
ATOM   466  C CB    . PRO A 1 61  ? 28.257  3.171   55.032 1.00 11.66 ?  61  PRO A CB    1 
ATOM   467  C CG    . PRO A 1 61  ? 26.788  3.293   55.324 1.00 10.62 ?  61  PRO A CG    1 
ATOM   468  C CD    . PRO A 1 61  ? 26.614  2.642   56.663 1.00 13.51 ?  61  PRO A CD    1 
ATOM   469  N N     . GLU A 1 62  ? 31.058  1.554   55.362 1.00 11.63 ?  62  GLU A N     1 
ATOM   470  C CA    . GLU A 1 62  ? 32.443  1.493   55.824 1.00 23.08 ?  62  GLU A CA    1 
ATOM   471  C C     . GLU A 1 62  ? 32.944  2.839   56.353 1.00 29.90 ?  62  GLU A C     1 
ATOM   472  O O     . GLU A 1 62  ? 33.654  2.888   57.365 1.00 48.18 ?  62  GLU A O     1 
ATOM   473  C CB    . GLU A 1 62  ? 33.348  1.016   54.685 1.00 35.86 ?  62  GLU A CB    1 
ATOM   474  C CG    . GLU A 1 62  ? 33.030  -0.355  54.143 1.00 39.65 ?  62  GLU A CG    1 
ATOM   475  C CD    . GLU A 1 62  ? 33.942  -0.736  52.990 1.00 54.64 ?  62  GLU A CD    1 
ATOM   476  O OE1   . GLU A 1 62  ? 34.532  0.179   52.372 1.00 43.35 ?  62  GLU A OE1   1 
ATOM   477  O OE2   . GLU A 1 62  ? 34.069  -1.947  52.700 1.00 62.85 -1 62  GLU A OE2   1 
ATOM   478  N N     . ASN A 1 63  ? 32.607  3.937   55.674 1.00 25.93 ?  63  ASN A N     1 
ATOM   479  C CA    . ASN A 1 63  ? 33.159  5.257   55.971 1.00 20.06 ?  63  ASN A CA    1 
ATOM   480  C C     . ASN A 1 63  ? 32.350  6.026   57.005 1.00 20.72 ?  63  ASN A C     1 
ATOM   481  O O     . ASN A 1 63  ? 32.829  7.051   57.503 1.00 18.77 ?  63  ASN A O     1 
ATOM   482  C CB    . ASN A 1 63  ? 33.249  6.090   54.691 1.00 22.43 ?  63  ASN A CB    1 
ATOM   483  C CG    . ASN A 1 63  ? 31.899  6.276   54.038 1.00 43.70 ?  63  ASN A CG    1 
ATOM   484  O OD1   . ASN A 1 63  ? 30.942  5.584   54.378 1.00 56.05 ?  63  ASN A OD1   1 
ATOM   485  N ND2   . ASN A 1 63  ? 31.810  7.206   53.099 1.00 50.17 ?  63  ASN A ND2   1 
ATOM   486  N N     . ILE A 1 64  ? 31.149  5.549   57.342 1.00 29.65 ?  64  ILE A N     1 
ATOM   487  C CA    . ILE A 1 64  ? 30.173  6.344   58.089 1.00 26.94 ?  64  ILE A CA    1 
ATOM   488  C C     . ILE A 1 64  ? 30.743  6.804   59.431 1.00 30.81 ?  64  ILE A C     1 
ATOM   489  O O     . ILE A 1 64  ? 30.295  7.812   59.992 1.00 30.01 ?  64  ILE A O     1 
ATOM   490  C CB    . ILE A 1 64  ? 28.863  5.534   58.251 1.00 23.00 ?  64  ILE A CB    1 
ATOM   491  C CG1   . ILE A 1 64  ? 27.697  6.408   58.735 1.00 12.02 ?  64  ILE A CG1   1 
ATOM   492  C CG2   . ILE A 1 64  ? 29.075  4.379   59.224 1.00 29.77 ?  64  ILE A CG2   1 
ATOM   493  C CD1   . ILE A 1 64  ? 27.230  7.441   57.756 1.00 16.33 ?  64  ILE A CD1   1 
ATOM   494  N N     . GLY A 1 65  ? 31.715  6.071   59.976 1.00 28.34 ?  65  GLY A N     1 
ATOM   495  C CA    . GLY A 1 65  ? 32.350  6.498   61.213 1.00 23.97 ?  65  GLY A CA    1 
ATOM   496  C C     . GLY A 1 65  ? 33.245  7.714   61.028 1.00 19.34 ?  65  GLY A C     1 
ATOM   497  O O     . GLY A 1 65  ? 33.375  8.543   61.932 1.00 14.28 ?  65  GLY A O     1 
ATOM   498  N N     . ASP A 1 66  ? 33.946  7.788   59.895 1.00 13.22 ?  66  ASP A N     1 
ATOM   499  C CA    . ASP A 1 66  ? 34.761  8.964   59.621 1.00 20.37 ?  66  ASP A CA    1 
ATOM   500  C C     . ASP A 1 66  ? 33.890  10.178  59.393 1.00 45.64 ?  66  ASP A C     1 
ATOM   501  O O     . ASP A 1 66  ? 34.158  11.262  59.931 1.00 43.62 ?  66  ASP A O     1 
ATOM   502  C CB    . ASP A 1 66  ? 35.628  8.751   58.393 1.00 13.43 ?  66  ASP A CB    1 
ATOM   503  C CG    . ASP A 1 66  ? 36.731  7.807   58.638 1.00 10.87 ?  66  ASP A CG    1 
ATOM   504  O OD1   . ASP A 1 66  ? 37.153  7.693   59.802 1.00 21.21 ?  66  ASP A OD1   1 
ATOM   505  O OD2   . ASP A 1 66  ? 37.208  7.214   57.663 1.00 19.51 -1 66  ASP A OD2   1 
ATOM   506  N N     . ILE A 1 67  ? 32.846  10.006  58.584 1.00 44.03 ?  67  ILE A N     1 
ATOM   507  C CA    . ILE A 1 67  ? 31.934  11.098  58.285 1.00 21.41 ?  67  ILE A CA    1 
ATOM   508  C C     . ILE A 1 67  ? 31.312  11.620  59.571 1.00 15.06 ?  67  ILE A C     1 
ATOM   509  O O     . ILE A 1 67  ? 31.216  12.835  59.785 1.00 11.97 ?  67  ILE A O     1 
ATOM   510  C CB    . ILE A 1 67  ? 30.884  10.617  57.275 1.00 15.88 ?  67  ILE A CB    1 
ATOM   511  C CG1   . ILE A 1 67  ? 31.553  10.381  55.922 1.00 9.97  ?  67  ILE A CG1   1 
ATOM   512  C CG2   . ILE A 1 67  ? 29.777  11.617  57.150 1.00 30.33 ?  67  ILE A CG2   1 
ATOM   513  C CD1   . ILE A 1 67  ? 30.719  9.588   54.953 1.00 19.85 ?  67  ILE A CD1   1 
ATOM   514  N N     . ILE A 1 68  ? 30.936  10.713  60.475 1.00 8.12  ?  68  ILE A N     1 
ATOM   515  C CA    . ILE A 1 68  ? 30.331  11.133  61.734 1.00 9.63  ?  68  ILE A CA    1 
ATOM   516  C C     . ILE A 1 68  ? 31.353  11.857  62.586 1.00 19.58 ?  68  ILE A C     1 
ATOM   517  O O     . ILE A 1 68  ? 31.069  12.910  63.165 1.00 33.07 ?  68  ILE A O     1 
ATOM   518  C CB    . ILE A 1 68  ? 29.727  9.914   62.459 1.00 7.86  ?  68  ILE A CB    1 
ATOM   519  C CG1   . ILE A 1 68  ? 28.447  9.485   61.756 1.00 7.08  ?  68  ILE A CG1   1 
ATOM   520  C CG2   . ILE A 1 68  ? 29.449  10.199  63.916 1.00 8.88  ?  68  ILE A CG2   1 
ATOM   521  C CD1   . ILE A 1 68  ? 27.710  8.375   62.458 1.00 23.02 ?  68  ILE A CD1   1 
ATOM   522  N N     . CYS A 1 69  ? 32.577  11.340  62.616 1.00 36.87 ?  69  CYS A N     1 
ATOM   523  C CA    . CYS A 1 69  ? 33.667  11.977  63.344 1.00 26.89 ?  69  CYS A CA    1 
ATOM   524  C C     . CYS A 1 69  ? 34.041  13.305  62.728 1.00 8.24  ?  69  CYS A C     1 
ATOM   525  O O     . CYS A 1 69  ? 34.418  14.242  63.435 1.00 14.46 ?  69  CYS A O     1 
ATOM   526  C CB    . CYS A 1 69  ? 34.888  11.074  63.279 1.00 27.54 ?  69  CYS A CB    1 
ATOM   527  S SG    . CYS A 1 69  ? 35.252  10.036  64.658 1.00 27.58 ?  69  CYS A SG    1 
ATOM   528  N N     . ASN A 1 70  ? 33.983  13.383  61.400 1.00 8.69  ?  70  ASN A N     1 
ATOM   529  C CA    . ASN A 1 70  ? 34.266  14.629  60.699 1.00 16.28 ?  70  ASN A CA    1 
ATOM   530  C C     . ASN A 1 70  ? 33.166  15.662  60.957 1.00 31.29 ?  70  ASN A C     1 
ATOM   531  O O     . ASN A 1 70  ? 33.455  16.812  61.314 1.00 31.08 ?  70  ASN A O     1 
ATOM   532  C CB    . ASN A 1 70  ? 34.446  14.339  59.202 1.00 19.21 ?  70  ASN A CB    1 
ATOM   533  C CG    . ASN A 1 70  ? 35.720  13.503  58.890 1.00 38.19 ?  70  ASN A CG    1 
ATOM   534  O OD1   . ASN A 1 70  ? 36.571  13.262  59.761 1.00 45.08 ?  70  ASN A OD1   1 
ATOM   535  N ND2   . ASN A 1 70  ? 35.845  13.070  57.636 1.00 37.18 ?  70  ASN A ND2   1 
ATOM   536  N N     . TRP A 1 71  ? 31.901  15.240  60.872 1.00 37.59 ?  71  TRP A N     1 
ATOM   537  C CA    . TRP A 1 71  ? 30.782  16.156  61.065 1.00 17.81 ?  71  TRP A CA    1 
ATOM   538  C C     . TRP A 1 71  ? 30.828  16.797  62.446 1.00 21.25 ?  71  TRP A C     1 
ATOM   539  O O     . TRP A 1 71  ? 30.627  18.008  62.585 1.00 44.07 ?  71  TRP A O     1 
ATOM   540  C CB    . TRP A 1 71  ? 29.460  15.413  60.863 1.00 13.52 ?  71  TRP A CB    1 
ATOM   541  C CG    . TRP A 1 71  ? 28.266  16.258  61.117 1.00 17.95 ?  71  TRP A CG    1 
ATOM   542  C CD1   . TRP A 1 71  ? 27.581  16.375  62.293 1.00 24.77 ?  71  TRP A CD1   1 
ATOM   543  C CD2   . TRP A 1 71  ? 27.609  17.120  60.184 1.00 17.58 ?  71  TRP A CD2   1 
ATOM   544  N NE1   . TRP A 1 71  ? 26.540  17.258  62.150 1.00 21.26 ?  71  TRP A NE1   1 
ATOM   545  C CE2   . TRP A 1 71  ? 26.536  17.729  60.863 1.00 22.53 ?  71  TRP A CE2   1 
ATOM   546  C CE3   . TRP A 1 71  ? 27.825  17.440  58.844 1.00 17.10 ?  71  TRP A CE3   1 
ATOM   547  C CZ2   . TRP A 1 71  ? 25.683  18.633  60.243 1.00 32.74 ?  71  TRP A CZ2   1 
ATOM   548  C CZ3   . TRP A 1 71  ? 26.977  18.335  58.232 1.00 22.79 ?  71  TRP A CZ3   1 
ATOM   549  C CH2   . TRP A 1 71  ? 25.922  18.922  58.927 1.00 29.33 ?  71  TRP A CH2   1 
ATOM   550  N N     . THR A 1 72  ? 31.072  15.997  63.491 1.00 18.25 ?  72  THR A N     1 
ATOM   551  C CA    . THR A 1 72  ? 31.093  16.545  64.848 1.00 16.31 ?  72  THR A CA    1 
ATOM   552  C C     . THR A 1 72  ? 32.301  17.447  65.111 1.00 27.78 ?  72  THR A C     1 
ATOM   553  O O     . THR A 1 72  ? 32.245  18.285  66.018 1.00 35.25 ?  72  THR A O     1 
ATOM   554  C CB    . THR A 1 72  ? 31.051  15.416  65.895 1.00 6.82  ?  72  THR A CB    1 
ATOM   555  O OG1   . THR A 1 72  ? 32.115  14.484  65.692 1.00 12.34 ?  72  THR A OG1   1 
ATOM   556  C CG2   . THR A 1 72  ? 29.768  14.673  65.796 1.00 34.91 ?  72  THR A CG2   1 
ATOM   557  N N     . LYS A 1 73  ? 33.379  17.313  64.342 1.00 23.79 ?  73  LYS A N     1 
ATOM   558  C CA    . LYS A 1 73  ? 34.501  18.228  64.477 1.00 29.32 ?  73  LYS A CA    1 
ATOM   559  C C     . LYS A 1 73  ? 34.337  19.484  63.629 1.00 24.55 ?  73  LYS A C     1 
ATOM   560  O O     . LYS A 1 73  ? 34.707  20.574  64.071 1.00 16.10 ?  73  LYS A O     1 
ATOM   561  C CB    . LYS A 1 73  ? 35.799  17.499  64.100 1.00 42.37 ?  73  LYS A CB    1 
ATOM   562  C CG    . LYS A 1 73  ? 37.058  18.153  64.622 1.00 32.09 ?  73  LYS A CG    1 
ATOM   563  C CD    . LYS A 1 73  ? 37.713  19.022  63.567 1.00 22.17 ?  73  LYS A CD    1 
ATOM   564  C CE    . LYS A 1 73  ? 38.935  19.611  64.165 1.00 16.83 ?  73  LYS A CE    1 
ATOM   565  N NZ    . LYS A 1 73  ? 38.658  19.826  65.604 1.00 14.16 1  73  LYS A NZ    1 
ATOM   566  N N     . GLN A 1 74  ? 33.745  19.362  62.443 1.00 27.20 ?  74  GLN A N     1 
ATOM   567  C CA    . GLN A 1 74  ? 33.573  20.516  61.569 1.00 16.42 ?  74  GLN A CA    1 
ATOM   568  C C     . GLN A 1 74  ? 32.510  21.477  62.099 1.00 26.38 ?  74  GLN A C     1 
ATOM   569  O O     . GLN A 1 74  ? 32.629  22.695  61.917 1.00 41.22 ?  74  GLN A O     1 
ATOM   570  C CB    . GLN A 1 74  ? 33.227  20.049  60.154 1.00 18.69 ?  74  GLN A CB    1 
ATOM   571  C CG    . GLN A 1 74  ? 32.470  21.071  59.313 1.00 34.56 ?  74  GLN A CG    1 
ATOM   572  C CD    . GLN A 1 74  ? 31.804  20.468  58.097 1.00 36.97 ?  74  GLN A CD    1 
ATOM   573  O OE1   . GLN A 1 74  ? 32.453  19.820  57.274 1.00 44.02 ?  74  GLN A OE1   1 
ATOM   574  N NE2   . GLN A 1 74  ? 30.504  20.681  57.972 1.00 26.85 ?  74  GLN A NE2   1 
ATOM   575  N N     . GLN A 1 75  ? 31.513  20.960  62.801 1.00 28.02 ?  75  GLN A N     1 
ATOM   576  C CA    . GLN A 1 75  ? 30.375  21.813  63.218 1.00 29.92 ?  75  GLN A CA    1 
ATOM   577  C C     . GLN A 1 75  ? 30.522  22.285  64.659 1.00 24.16 ?  75  GLN A C     1 
ATOM   578  O O     . GLN A 1 75  ? 30.124  23.400  64.951 1.00 32.16 ?  75  GLN A O     1 
ATOM   579  C CB    . GLN A 1 75  ? 29.050  21.113  62.884 1.00 29.50 ?  75  GLN A CB    1 
ATOM   580  C CG    . GLN A 1 75  ? 28.934  20.648  61.440 1.00 29.11 ?  75  GLN A CG    1 
ATOM   581  C CD    . GLN A 1 75  ? 28.534  21.687  60.420 1.00 32.68 ?  75  GLN A CD    1 
ATOM   582  O OE1   . GLN A 1 75  ? 28.271  21.375  59.268 1.00 40.81 ?  75  GLN A OE1   1 
ATOM   583  N NE2   . GLN A 1 75  ? 28.493  22.943  60.813 1.00 30.65 ?  75  GLN A NE2   1 
ATOM   584  N N     . TYR A 1 76  ? 31.130  21.485  65.495 1.00 12.94 ?  76  TYR A N     1 
ATOM   585  C CA    . TYR A 1 76  ? 31.229  21.804  66.905 1.00 18.58 ?  76  TYR A CA    1 
ATOM   586  C C     . TYR A 1 76  ? 32.664  21.758  67.412 1.00 32.52 ?  76  TYR A C     1 
ATOM   587  O O     . TYR A 1 76  ? 32.883  22.008  68.602 1.00 31.67 ?  76  TYR A O     1 
ATOM   588  C CB    . TYR A 1 76  ? 30.376  20.836  67.739 1.00 26.29 ?  76  TYR A CB    1 
ATOM   589  C CG    . TYR A 1 76  ? 29.060  20.412  67.101 1.00 29.67 ?  76  TYR A CG    1 
ATOM   590  C CD1   . TYR A 1 76  ? 27.931  21.217  67.169 1.00 27.21 ?  76  TYR A CD1   1 
ATOM   591  C CD2   . TYR A 1 76  ? 28.948  19.198  66.445 1.00 30.21 ?  76  TYR A CD2   1 
ATOM   592  C CE1   . TYR A 1 76  ? 26.734  20.819  66.590 1.00 22.43 ?  76  TYR A CE1   1 
ATOM   593  C CE2   . TYR A 1 76  ? 27.767  18.796  65.872 1.00 27.07 ?  76  TYR A CE2   1 
ATOM   594  C CZ    . TYR A 1 76  ? 26.661  19.610  65.942 1.00 34.33 ?  76  TYR A CZ    1 
ATOM   595  O OH    . TYR A 1 76  ? 25.474  19.203  65.361 1.00 48.21 ?  76  TYR A OH    1 
ATOM   596  N N     . ASP A 1 77  ? 33.666  21.447  66.533 1.00 27.11 ?  77  ASP A N     1 
ATOM   597  C CA    . ASP A 1 77  ? 35.112  21.199  66.849 1.00 11.33 ?  77  ASP A CA    1 
ATOM   598  C C     . ASP A 1 77  ? 35.071  20.178  67.985 1.00 13.34 ?  77  ASP A C     1 
ATOM   599  O O     . ASP A 1 77  ? 35.648  20.436  68.994 1.00 7.76  ?  77  ASP A O     1 
ATOM   600  C CB    . ASP A 1 77  ? 35.917  22.475  67.141 1.00 32.36 ?  77  ASP A CB    1 
ATOM   601  C CG    . ASP A 1 77  ? 37.420  22.359  67.270 1.00 18.77 ?  77  ASP A CG    1 
ATOM   602  O OD1   . ASP A 1 77  ? 38.082  22.362  66.239 1.00 16.95 ?  77  ASP A OD1   1 
ATOM   603  O OD2   . ASP A 1 77  ? 37.907  22.344  68.407 1.00 18.73 -1 77  ASP A OD2   1 
ATOM   604  N N     . TRP A 1 78  ? 34.329  19.093  67.845 1.00 34.06 ?  78  TRP A N     1 
ATOM   605  C CA    . TRP A 1 78  ? 34.209  17.939  68.777 1.00 28.05 ?  78  TRP A CA    1 
ATOM   606  C C     . TRP A 1 78  ? 34.962  16.727  68.221 1.00 23.84 ?  78  TRP A C     1 
ATOM   607  O O     . TRP A 1 78  ? 34.512  16.131  67.274 1.00 13.48 ?  78  TRP A O     1 
ATOM   608  C CB    . TRP A 1 78  ? 32.730  17.683  69.000 1.00 31.20 ?  78  TRP A CB    1 
ATOM   609  C CG    . TRP A 1 78  ? 32.392  16.684  70.054 1.00 41.75 ?  78  TRP A CG    1 
ATOM   610  C CD1   . TRP A 1 78  ? 33.219  16.166  71.003 1.00 40.00 ?  78  TRP A CD1   1 
ATOM   611  C CD2   . TRP A 1 78  ? 31.104  16.093  70.273 1.00 30.92 ?  78  TRP A CD2   1 
ATOM   612  N NE1   . TRP A 1 78  ? 32.534  15.272  71.773 1.00 30.64 ?  78  TRP A NE1   1 
ATOM   613  C CE2   . TRP A 1 78  ? 31.231  15.226  71.374 1.00 39.27 ?  78  TRP A CE2   1 
ATOM   614  C CE3   . TRP A 1 78  ? 29.866  16.209  69.644 1.00 14.51 ?  78  TRP A CE3   1 
ATOM   615  C CZ2   . TRP A 1 78  ? 30.176  14.468  71.862 1.00 29.03 ?  78  TRP A CZ2   1 
ATOM   616  C CZ3   . TRP A 1 78  ? 28.817  15.471  70.134 1.00 24.56 ?  78  TRP A CZ3   1 
ATOM   617  C CH2   . TRP A 1 78  ? 28.973  14.616  71.221 1.00 37.50 ?  78  TRP A CH2   1 
ATOM   618  N N     . ASP A 1 79  ? 36.130  16.449  68.789 1.00 27.05 ?  79  ASP A N     1 
ATOM   619  C CA    . ASP A 1 79  ? 36.927  15.313  68.349 1.00 18.15 ?  79  ASP A CA    1 
ATOM   620  C C     . ASP A 1 79  ? 36.418  14.093  69.105 1.00 12.04 ?  79  ASP A C     1 
ATOM   621  O O     . ASP A 1 79  ? 36.579  13.995  70.326 1.00 6.68  ?  79  ASP A O     1 
ATOM   622  C CB    . ASP A 1 79  ? 38.419  15.543  68.601 1.00 22.29 ?  79  ASP A CB    1 
ATOM   623  C CG    . ASP A 1 79  ? 38.869  16.980  68.316 1.00 47.45 ?  79  ASP A CG    1 
ATOM   624  O OD1   . ASP A 1 79  ? 38.938  17.374  67.132 1.00 53.76 ?  79  ASP A OD1   1 
ATOM   625  O OD2   . ASP A 1 79  ? 39.191  17.708  69.278 1.00 52.05 -1 79  ASP A OD2   1 
ATOM   626  N N     . ILE A 1 80  ? 35.794  13.175  68.382 1.00 17.38 ?  80  ILE A N     1 
ATOM   627  C CA    . ILE A 1 80  ? 35.257  11.942  68.941 1.00 29.22 ?  80  ILE A CA    1 
ATOM   628  C C     . ILE A 1 80  ? 35.971  10.777  68.274 1.00 31.09 ?  80  ILE A C     1 
ATOM   629  O O     . ILE A 1 80  ? 36.662  10.944  67.273 1.00 40.88 ?  80  ILE A O     1 
ATOM   630  C CB    . ILE A 1 80  ? 33.735  11.841  68.746 1.00 22.68 ?  80  ILE A CB    1 
ATOM   631  C CG1   . ILE A 1 80  ? 33.418  11.625  67.260 1.00 10.80 ?  80  ILE A CG1   1 
ATOM   632  C CG2   . ILE A 1 80  ? 33.077  13.106  69.272 1.00 20.56 ?  80  ILE A CG2   1 
ATOM   633  C CD1   . ILE A 1 80  ? 32.060  11.001  66.969 1.00 13.20 ?  80  ILE A CD1   1 
ATOM   634  N N     . GLN A 1 81  ? 35.813  9.590   68.842 1.00 25.09 ?  81  GLN A N     1 
ATOM   635  C CA    . GLN A 1 81  ? 36.385  8.395   68.238 1.00 23.76 ?  81  GLN A CA    1 
ATOM   636  C C     . GLN A 1 81  ? 35.303  7.456   67.700 1.00 29.23 ?  81  GLN A C     1 
ATOM   637  O O     . GLN A 1 81  ? 34.145  7.492   68.127 1.00 26.79 ?  81  GLN A O     1 
ATOM   638  C CB    . GLN A 1 81  ? 37.298  7.681   69.230 1.00 19.19 ?  81  GLN A CB    1 
ATOM   639  C CG    . GLN A 1 81  ? 38.414  8.592   69.693 1.00 20.37 ?  81  GLN A CG    1 
ATOM   640  C CD    . GLN A 1 81  ? 39.277  9.059   68.542 1.00 21.99 ?  81  GLN A CD    1 
ATOM   641  O OE1   . GLN A 1 81  ? 39.315  8.437   67.481 1.00 20.11 ?  81  GLN A OE1   1 
ATOM   642  N NE2   . GLN A 1 81  ? 39.959  10.180  68.735 1.00 40.41 ?  81  GLN A NE2   1 
ATOM   643  N N     . LYS A 1 82  ? 35.699  6.627   66.722 1.00 27.40 ?  82  LYS A N     1 
ATOM   644  C CA    . LYS A 1 82  ? 34.750  5.756   66.033 1.00 17.35 ?  82  LYS A CA    1 
ATOM   645  C C     . LYS A 1 82  ? 34.087  4.771   66.980 1.00 25.27 ?  82  LYS A C     1 
ATOM   646  O O     . LYS A 1 82  ? 32.991  4.277   66.689 1.00 34.27 ?  82  LYS A O     1 
ATOM   647  C CB    . LYS A 1 82  ? 35.444  4.991   64.903 1.00 9.71  ?  82  LYS A CB    1 
ATOM   648  C CG    . LYS A 1 82  ? 35.426  5.710   63.569 1.00 18.14 ?  82  LYS A CG    1 
ATOM   649  C CD    . LYS A 1 82  ? 35.528  4.759   62.394 1.00 21.30 ?  82  LYS A CD    1 
ATOM   650  C CE    . LYS A 1 82  ? 36.732  5.078   61.520 1.00 32.51 ?  82  LYS A CE    1 
ATOM   651  N NZ    . LYS A 1 82  ? 36.735  4.312   60.236 1.00 31.87 1  82  LYS A NZ    1 
ATOM   652  N N     . GLU A 1 83  ? 34.739  4.444   68.093 1.00 21.96 ?  83  GLU A N     1 
ATOM   653  C CA    . GLU A 1 83  ? 34.178  3.456   69.008 1.00 27.30 ?  83  GLU A CA    1 
ATOM   654  C C     . GLU A 1 83  ? 33.007  4.014   69.813 1.00 36.66 ?  83  GLU A C     1 
ATOM   655  O O     . GLU A 1 83  ? 32.303  3.239   70.473 1.00 35.76 ?  83  GLU A O     1 
ATOM   656  C CB    . GLU A 1 83  ? 35.273  2.918   69.935 1.00 24.26 ?  83  GLU A CB    1 
ATOM   657  C CG    . GLU A 1 83  ? 36.514  2.440   69.191 1.00 33.36 ?  83  GLU A CG    1 
ATOM   658  C CD    . GLU A 1 83  ? 37.517  3.550   68.901 1.00 33.81 ?  83  GLU A CD    1 
ATOM   659  O OE1   . GLU A 1 83  ? 37.943  3.676   67.734 1.00 29.77 ?  83  GLU A OE1   1 
ATOM   660  O OE2   . GLU A 1 83  ? 37.891  4.285   69.838 1.00 38.30 -1 83  GLU A OE2   1 
ATOM   661  N N     . TRP A 1 84  ? 32.795  5.333   69.780 1.00 13.04 ?  84  TRP A N     1 
ATOM   662  C CA    . TRP A 1 84  ? 31.764  6.002   70.562 1.00 15.56 ?  84  TRP A CA    1 
ATOM   663  C C     . TRP A 1 84  ? 30.399  6.003   69.884 1.00 25.18 ?  84  TRP A C     1 
ATOM   664  O O     . TRP A 1 84  ? 29.384  6.202   70.560 1.00 21.57 ?  84  TRP A O     1 
ATOM   665  C CB    . TRP A 1 84  ? 32.185  7.445   70.844 1.00 25.13 ?  84  TRP A CB    1 
ATOM   666  C CG    . TRP A 1 84  ? 33.436  7.559   71.677 1.00 35.00 ?  84  TRP A CG    1 
ATOM   667  C CD1   . TRP A 1 84  ? 34.128  6.538   72.242 1.00 34.47 ?  84  TRP A CD1   1 
ATOM   668  C CD2   . TRP A 1 84  ? 34.125  8.762   72.045 1.00 30.99 ?  84  TRP A CD2   1 
ATOM   669  N NE1   . TRP A 1 84  ? 35.204  7.022   72.940 1.00 29.74 ?  84  TRP A NE1   1 
ATOM   670  C CE2   . TRP A 1 84  ? 35.229  8.384   72.831 1.00 28.09 ?  84  TRP A CE2   1 
ATOM   671  C CE3   . TRP A 1 84  ? 33.917  10.116  71.784 1.00 24.39 ?  84  TRP A CE3   1 
ATOM   672  C CZ2   . TRP A 1 84  ? 36.122  9.312   73.366 1.00 19.79 ?  84  TRP A CZ2   1 
ATOM   673  C CZ3   . TRP A 1 84  ? 34.810  11.039  72.311 1.00 27.45 ?  84  TRP A CZ3   1 
ATOM   674  C CH2   . TRP A 1 84  ? 35.897  10.632  73.093 1.00 23.34 ?  84  TRP A CH2   1 
ATOM   675  N N     . ILE A 1 85  ? 30.349  5.801   68.573 1.00 24.91 ?  85  ILE A N     1 
ATOM   676  C CA    . ILE A 1 85  ? 29.110  5.934   67.818 1.00 8.49  ?  85  ILE A CA    1 
ATOM   677  C C     . ILE A 1 85  ? 28.261  4.694   68.032 1.00 19.33 ?  85  ILE A C     1 
ATOM   678  O O     . ILE A 1 85  ? 28.726  3.565   67.837 1.00 11.92 ?  85  ILE A O     1 
ATOM   679  C CB    . ILE A 1 85  ? 29.385  6.129   66.330 1.00 5.63  ?  85  ILE A CB    1 
ATOM   680  C CG1   . ILE A 1 85  ? 30.454  7.197   66.136 1.00 10.29 ?  85  ILE A CG1   1 
ATOM   681  C CG2   . ILE A 1 85  ? 28.099  6.443   65.614 1.00 6.74  ?  85  ILE A CG2   1 
ATOM   682  C CD1   . ILE A 1 85  ? 31.100  7.128   64.789 1.00 18.93 ?  85  ILE A CD1   1 
ATOM   683  N N     . VAL A 1 86  ? 27.028  4.906   68.478 1.00 32.14 ?  86  VAL A N     1 
ATOM   684  C CA    . VAL A 1 86  ? 25.983  3.895   68.564 1.00 9.25  ?  86  VAL A CA    1 
ATOM   685  C C     . VAL A 1 86  ? 24.855  4.366   67.663 1.00 24.67 ?  86  VAL A C     1 
ATOM   686  O O     . VAL A 1 86  ? 24.622  5.573   67.541 1.00 46.97 ?  86  VAL A O     1 
ATOM   687  C CB    . VAL A 1 86  ? 25.471  3.696   70.006 1.00 9.74  ?  86  VAL A CB    1 
ATOM   688  C CG1   . VAL A 1 86  ? 24.277  2.770   70.021 1.00 19.46 ?  86  VAL A CG1   1 
ATOM   689  C CG2   . VAL A 1 86  ? 26.559  3.126   70.873 1.00 17.83 ?  86  VAL A CG2   1 
ATOM   690  N N     . PHE A 1 87  ? 24.197  3.437   66.984 1.00 19.87 ?  87  PHE A N     1 
ATOM   691  C CA    . PHE A 1 87  ? 23.074  3.764   66.118 1.00 4.40  ?  87  PHE A CA    1 
ATOM   692  C C     . PHE A 1 87  ? 21.759  3.528   66.853 1.00 26.08 ?  87  PHE A C     1 
ATOM   693  O O     . PHE A 1 87  ? 21.680  2.710   67.769 1.00 17.37 ?  87  PHE A O     1 
ATOM   694  C CB    . PHE A 1 87  ? 23.129  2.954   64.825 1.00 13.66 ?  87  PHE A CB    1 
ATOM   695  C CG    . PHE A 1 87  ? 24.225  3.393   63.899 1.00 28.91 ?  87  PHE A CG    1 
ATOM   696  C CD1   . PHE A 1 87  ? 24.026  4.435   63.019 1.00 36.45 ?  87  PHE A CD1   1 
ATOM   697  C CD2   . PHE A 1 87  ? 25.472  2.801   63.939 1.00 22.65 ?  87  PHE A CD2   1 
ATOM   698  C CE1   . PHE A 1 87  ? 25.042  4.850   62.185 1.00 31.15 ?  87  PHE A CE1   1 
ATOM   699  C CE2   . PHE A 1 87  ? 26.483  3.229   63.106 1.00 13.09 ?  87  PHE A CE2   1 
ATOM   700  C CZ    . PHE A 1 87  ? 26.268  4.243   62.239 1.00 13.89 ?  87  PHE A CZ    1 
ATOM   701  N N     . SER A 1 88  ? 20.750  4.326   66.501 1.00 29.55 ?  88  SER A N     1 
ATOM   702  C CA    . SER A 1 88  ? 19.406  4.237   67.060 1.00 14.36 ?  88  SER A CA    1 
ATOM   703  C C     . SER A 1 88  ? 18.415  4.607   65.975 1.00 25.85 ?  88  SER A C     1 
ATOM   704  O O     . SER A 1 88  ? 18.733  5.395   65.084 1.00 45.00 ?  88  SER A O     1 
ATOM   705  C CB    . SER A 1 88  ? 19.224  5.161   68.256 1.00 4.35  ?  88  SER A CB    1 
ATOM   706  O OG    . SER A 1 88  ? 18.267  4.674   69.178 1.00 15.66 ?  88  SER A OG    1 
ATOM   707  N N     . ALA A 1 89  ? 17.212  4.036   66.038 1.00 15.91 ?  89  ALA A N     1 
ATOM   708  C CA    . ALA A 1 89  ? 16.199  4.410   65.058 1.00 22.43 ?  89  ALA A CA    1 
ATOM   709  C C     . ALA A 1 89  ? 15.505  5.738   65.386 1.00 31.82 ?  89  ALA A C     1 
ATOM   710  O O     . ALA A 1 89  ? 14.613  6.157   64.644 1.00 38.02 ?  89  ALA A O     1 
ATOM   711  C CB    . ALA A 1 89  ? 15.154  3.297   64.934 1.00 10.81 ?  89  ALA A CB    1 
ATOM   712  N N     . GLY A 1 90  ? 15.901  6.422   66.452 1.00 31.18 ?  90  GLY A N     1 
ATOM   713  C CA    . GLY A 1 90  ? 15.300  7.683   66.850 1.00 23.02 ?  90  GLY A CA    1 
ATOM   714  C C     . GLY A 1 90  ? 15.700  7.981   68.279 1.00 18.26 ?  90  GLY A C     1 
ATOM   715  O O     . GLY A 1 90  ? 16.132  7.062   68.983 1.00 30.86 ?  90  GLY A O     1 
ATOM   716  N N     . ILE A 1 91  ? 15.550  9.224   68.739 1.00 3.28  ?  91  ILE A N     1 
ATOM   717  C CA    . ILE A 1 91  ? 15.976  9.554   70.095 1.00 2.63  ?  91  ILE A CA    1 
ATOM   718  C C     . ILE A 1 91  ? 14.994  9.072   71.173 1.00 5.99  ?  91  ILE A C     1 
ATOM   719  O O     . ILE A 1 91  ? 15.392  8.823   72.306 1.00 23.90 ?  91  ILE A O     1 
ATOM   720  C CB    . ILE A 1 91  ? 16.238  11.062  70.172 1.00 15.74 ?  91  ILE A CB    1 
ATOM   721  C CG1   . ILE A 1 91  ? 17.145  11.491  69.011 1.00 23.13 ?  91  ILE A CG1   1 
ATOM   722  C CG2   . ILE A 1 91  ? 16.790  11.467  71.557 1.00 21.56 ?  91  ILE A CG2   1 
ATOM   723  C CD1   . ILE A 1 91  ? 17.966  12.727  69.231 1.00 22.14 ?  91  ILE A CD1   1 
ATOM   724  N N     . VAL A 1 92  ? 13.713  8.924   70.859 1.00 8.38  ?  92  VAL A N     1 
ATOM   725  C CA    . VAL A 1 92  ? 12.753  8.439   71.870 1.00 1.91  ?  92  VAL A CA    1 
ATOM   726  C C     . VAL A 1 92  ? 13.060  6.983   72.257 1.00 27.37 ?  92  VAL A C     1 
ATOM   727  O O     . VAL A 1 92  ? 12.973  6.618   73.444 1.00 1.79  ?  92  VAL A O     1 
ATOM   728  C CB    . VAL A 1 92  ? 11.286  8.586   71.424 1.00 12.97 ?  92  VAL A CB    1 
ATOM   729  C CG1   . VAL A 1 92  ? 10.398  8.343   72.614 1.00 12.53 ?  92  VAL A CG1   1 
ATOM   730  C CG2   . VAL A 1 92  ? 10.999  9.964   70.830 1.00 27.03 ?  92  VAL A CG2   1 
ATOM   731  N N     . PRO A 1 93  ? 13.388  6.097   71.320 1.00 2.06  ?  93  PRO A N     1 
ATOM   732  C CA    . PRO A 1 93  ? 13.951  4.816   71.768 1.00 7.48  ?  93  PRO A CA    1 
ATOM   733  C C     . PRO A 1 93  ? 15.241  4.989   72.572 1.00 21.99 ?  93  PRO A C     1 
ATOM   734  O O     . PRO A 1 93  ? 15.429  4.309   73.587 1.00 21.55 ?  93  PRO A O     1 
ATOM   735  C CB    . PRO A 1 93  ? 14.184  4.067   70.446 1.00 11.62 ?  93  PRO A CB    1 
ATOM   736  C CG    . PRO A 1 93  ? 13.151  4.652   69.492 1.00 5.59  ?  93  PRO A CG    1 
ATOM   737  C CD    . PRO A 1 93  ? 13.034  6.085   69.881 1.00 2.20  ?  93  PRO A CD    1 
ATOM   738  N N     . ALA A 1 94  ? 16.102  5.945   72.198 1.00 18.08 ?  94  ALA A N     1 
ATOM   739  C CA    . ALA A 1 94  ? 17.377  6.111   72.902 1.00 6.86  ?  94  ALA A CA    1 
ATOM   740  C C     . ALA A 1 94  ? 17.206  6.737   74.276 1.00 21.71 ?  94  ALA A C     1 
ATOM   741  O O     . ALA A 1 94  ? 17.970  6.420   75.197 1.00 21.90 ?  94  ALA A O     1 
ATOM   742  C CB    . ALA A 1 94  ? 18.334  6.946   72.056 1.00 11.68 ?  94  ALA A CB    1 
ATOM   743  N N     . LEU A 1 95  ? 16.210  7.614   74.436 1.00 19.41 ?  95  LEU A N     1 
ATOM   744  C CA    . LEU A 1 95  ? 15.865  8.091   75.768 1.00 10.19 ?  95  LEU A CA    1 
ATOM   745  C C     . LEU A 1 95  ? 15.347  6.945   76.612 1.00 14.77 ?  95  LEU A C     1 
ATOM   746  O O     . LEU A 1 95  ? 15.682  6.830   77.796 1.00 13.02 ?  95  LEU A O     1 
ATOM   747  C CB    . LEU A 1 95  ? 14.797  9.181   75.700 1.00 21.69 ?  95  LEU A CB    1 
ATOM   748  C CG    . LEU A 1 95  ? 14.955  10.486  74.932 1.00 28.27 ?  95  LEU A CG    1 
ATOM   749  C CD1   . LEU A 1 95  ? 13.620  11.237  75.023 1.00 1.63  ?  95  LEU A CD1   1 
ATOM   750  C CD2   . LEU A 1 95  ? 16.132  11.308  75.447 1.00 4.28  ?  95  LEU A CD2   1 
ATOM   751  N N     . SER A 1 96  ? 14.507  6.095   76.017 1.00 38.48 ?  96  SER A N     1 
ATOM   752  C CA    . SER A 1 96  ? 13.961  4.957   76.745 1.00 29.11 ?  96  SER A CA    1 
ATOM   753  C C     . SER A 1 96  ? 15.056  3.965   77.060 1.00 1.72  ?  96  SER A C     1 
ATOM   754  O O     . SER A 1 96  ? 15.135  3.456   78.181 1.00 27.33 ?  96  SER A O     1 
ATOM   755  C CB    . SER A 1 96  ? 12.845  4.286   75.948 1.00 35.86 ?  96  SER A CB    1 
ATOM   756  O OG    . SER A 1 96  ? 12.286  3.218   76.688 1.00 37.42 ?  96  SER A OG    1 
ATOM   757  N N     . THR A 1 97  ? 15.922  3.681   76.086 1.00 9.68  ?  97  THR A N     1 
ATOM   758  C CA    . THR A 1 97  ? 17.082  2.825   76.358 1.00 1.97  ?  97  THR A CA    1 
ATOM   759  C C     . THR A 1 97  ? 17.929  3.391   77.494 1.00 6.89  ?  97  THR A C     1 
ATOM   760  O O     . THR A 1 97  ? 18.384  2.647   78.371 1.00 27.03 ?  97  THR A O     1 
ATOM   761  C CB    . THR A 1 97  ? 17.934  2.695   75.104 1.00 2.16  ?  97  THR A CB    1 
ATOM   762  O OG1   . THR A 1 97  ? 17.099  2.380   73.984 1.00 2.20  ?  97  THR A OG1   1 
ATOM   763  C CG2   . THR A 1 97  ? 18.983  1.611   75.262 1.00 28.19 ?  97  THR A CG2   1 
ATOM   764  N N     . SER A 1 98  ? 18.126  4.716   77.514 1.00 9.08  ?  98  SER A N     1 
ATOM   765  C CA    . SER A 1 98  ? 18.940  5.339   78.551 1.00 2.64  ?  98  SER A CA    1 
ATOM   766  C C     . SER A 1 98  ? 18.302  5.211   79.920 1.00 1.72  ?  98  SER A C     1 
ATOM   767  O O     . SER A 1 98  ? 18.974  4.879   80.896 1.00 21.21 ?  98  SER A O     1 
ATOM   768  C CB    . SER A 1 98  ? 19.212  6.804   78.198 1.00 1.92  ?  98  SER A CB    1 
ATOM   769  O OG    . SER A 1 98  ? 19.446  6.947   76.801 1.00 10.98 ?  98  SER A OG    1 
ATOM   770  N N     . ILE A 1 99  ? 17.006  5.449   80.020 1.00 33.97 ?  99  ILE A N     1 
ATOM   771  C CA    . ILE A 1 99  ? 16.344  5.264   81.303 1.00 12.11 ?  99  ILE A CA    1 
ATOM   772  C C     . ILE A 1 99  ? 16.522  3.831   81.791 1.00 1.52  ?  99  ILE A C     1 
ATOM   773  O O     . ILE A 1 99  ? 16.699  3.586   82.987 1.00 1.48  ?  99  ILE A O     1 
ATOM   774  C CB    . ILE A 1 99  ? 14.872  5.645   81.177 1.00 6.68  ?  99  ILE A CB    1 
ATOM   775  C CG1   . ILE A 1 99  ? 14.787  7.132   80.881 1.00 10.25 ?  99  ILE A CG1   1 
ATOM   776  C CG2   . ILE A 1 99  ? 14.129  5.237   82.433 1.00 21.86 ?  99  ILE A CG2   1 
ATOM   777  C CD1   . ILE A 1 99  ? 13.599  7.515   80.092 1.00 17.22 ?  99  ILE A CD1   1 
ATOM   778  N N     . GLN A 1 100 ? 16.435  2.855   80.881 1.00 19.75 ?  100 GLN A N     1 
ATOM   779  C CA    . GLN A 1 100 ? 16.535  1.462   81.320 1.00 25.00 ?  100 GLN A CA    1 
ATOM   780  C C     . GLN A 1 100 ? 17.966  1.050   81.677 1.00 1.75  ?  100 GLN A C     1 
ATOM   781  O O     . GLN A 1 100 ? 18.149  0.271   82.613 1.00 1.76  ?  100 GLN A O     1 
ATOM   782  C CB    . GLN A 1 100 ? 15.974  0.516   80.273 1.00 20.94 ?  100 GLN A CB    1 
ATOM   783  C CG    . GLN A 1 100 ? 14.614  0.766   79.743 1.00 1.72  ?  100 GLN A CG    1 
ATOM   784  C CD    . GLN A 1 100 ? 14.299  -0.318  78.759 1.00 18.53 ?  100 GLN A CD    1 
ATOM   785  O OE1   . GLN A 1 100 ? 14.379  -0.092  77.557 1.00 1.89  ?  100 GLN A OE1   1 
ATOM   786  N NE2   . GLN A 1 100 ? 13.960  -1.516  79.258 1.00 1.90  ?  100 GLN A NE2   1 
ATOM   787  N N     . ALA A 1 101 ? 18.988  1.578   80.995 1.00 24.18 ?  101 ALA A N     1 
ATOM   788  C CA    . ALA A 1 101 ? 20.355  1.168   81.339 1.00 16.78 ?  101 ALA A CA    1 
ATOM   789  C C     . ALA A 1 101 ? 20.803  1.784   82.658 1.00 8.19  ?  101 ALA A C     1 
ATOM   790  O O     . ALA A 1 101 ? 21.361  1.091   83.511 1.00 5.14  ?  101 ALA A O     1 
ATOM   791  C CB    . ALA A 1 101 ? 21.348  1.550   80.241 1.00 2.08  ?  101 ALA A CB    1 
ATOM   792  N N     . PHE A 1 102 ? 20.478  3.054   82.893 1.00 13.32 ?  102 PHE A N     1 
ATOM   793  C CA    . PHE A 1 102 ? 21.165  3.828   83.912 1.00 1.74  ?  102 PHE A CA    1 
ATOM   794  C C     . PHE A 1 102 ? 20.374  4.083   85.180 1.00 1.59  ?  102 PHE A C     1 
ATOM   795  O O     . PHE A 1 102 ? 20.888  4.749   86.078 1.00 23.09 ?  102 PHE A O     1 
ATOM   796  C CB    . PHE A 1 102 ? 21.616  5.139   83.288 1.00 1.79  ?  102 PHE A CB    1 
ATOM   797  C CG    . PHE A 1 102 ? 22.274  4.940   81.973 1.00 4.96  ?  102 PHE A CG    1 
ATOM   798  C CD1   . PHE A 1 102 ? 23.357  4.073   81.861 1.00 2.10  ?  102 PHE A CD1   1 
ATOM   799  C CD2   . PHE A 1 102 ? 21.801  5.559   80.850 1.00 1.98  ?  102 PHE A CD2   1 
ATOM   800  C CE1   . PHE A 1 102 ? 23.944  3.860   80.647 1.00 2.28  ?  102 PHE A CE1   1 
ATOM   801  C CE2   . PHE A 1 102 ? 22.374  5.336   79.635 1.00 6.19  ?  102 PHE A CE2   1 
ATOM   802  C CZ    . PHE A 1 102 ? 23.453  4.496   79.531 1.00 8.77  ?  102 PHE A CZ    1 
ATOM   803  N N     . THR A 1 103 ? 19.163  3.562   85.293 1.00 8.13  ?  103 THR A N     1 
ATOM   804  C CA    . THR A 1 103 ? 18.401  3.610   86.526 1.00 1.42  ?  103 THR A CA    1 
ATOM   805  C C     . THR A 1 103 ? 17.838  2.231   86.800 1.00 1.45  ?  103 THR A C     1 
ATOM   806  O O     . THR A 1 103 ? 17.859  1.345   85.940 1.00 1.54  ?  103 THR A O     1 
ATOM   807  C CB    . THR A 1 103 ? 17.224  4.592   86.483 1.00 8.50  ?  103 THR A CB    1 
ATOM   808  O OG1   . THR A 1 103 ? 16.415  4.300   85.347 1.00 5.70  ?  103 THR A OG1   1 
ATOM   809  C CG2   . THR A 1 103 ? 17.704  6.023   86.428 1.00 1.34  ?  103 THR A CG2   1 
ATOM   810  N N     . LYS A 1 104 ? 17.433  2.046   88.047 1.00 6.09  ?  104 LYS A N     1 
ATOM   811  C CA    . LYS A 1 104 ? 16.583  0.951   88.486 1.00 20.88 ?  104 LYS A CA    1 
ATOM   812  C C     . LYS A 1 104 ? 15.142  1.457   88.605 1.00 11.33 ?  104 LYS A C     1 
ATOM   813  O O     . LYS A 1 104 ? 14.881  2.658   88.587 1.00 27.38 ?  104 LYS A O     1 
ATOM   814  C CB    . LYS A 1 104 ? 17.069  0.385   89.821 1.00 30.80 ?  104 LYS A CB    1 
ATOM   815  C CG    . LYS A 1 104 ? 18.453  -0.174  89.766 1.00 17.59 ?  104 LYS A CG    1 
ATOM   816  C CD    . LYS A 1 104 ? 19.017  -0.319  91.151 1.00 12.98 ?  104 LYS A CD    1 
ATOM   817  C CE    . LYS A 1 104 ? 20.308  -1.127  91.118 1.00 29.26 ?  104 LYS A CE    1 
ATOM   818  N NZ    . LYS A 1 104 ? 21.304  -0.610  90.149 1.00 24.78 1  104 LYS A NZ    1 
ATOM   819  N N     . GLU A 1 105 ? 14.212  0.528   88.757 1.00 3.78  ?  105 GLU A N     1 
ATOM   820  C CA    . GLU A 1 105 ? 12.801  0.885   88.827 1.00 21.97 ?  105 GLU A CA    1 
ATOM   821  C C     . GLU A 1 105 ? 12.489  1.788   90.019 1.00 33.64 ?  105 GLU A C     1 
ATOM   822  O O     . GLU A 1 105 ? 13.028  1.615   91.116 1.00 38.40 ?  105 GLU A O     1 
ATOM   823  C CB    . GLU A 1 105 ? 11.948  -0.385  88.885 1.00 11.70 ?  105 GLU A CB    1 
ATOM   824  C CG    . GLU A 1 105 ? 11.498  -0.861  87.511 1.00 6.80  ?  105 GLU A CG    1 
ATOM   825  C CD    . GLU A 1 105 ? 10.419  -1.908  87.603 1.00 18.59 ?  105 GLU A CD    1 
ATOM   826  O OE1   . GLU A 1 105 ? 9.976   -2.395  86.547 1.00 23.99 ?  105 GLU A OE1   1 
ATOM   827  O OE2   . GLU A 1 105 ? 10.013  -2.244  88.733 1.00 25.52 -1 105 GLU A OE2   1 
ATOM   828  N N     . ASN A 1 106 ? 11.606  2.765   89.790 1.00 35.20 ?  106 ASN A N     1 
ATOM   829  C CA    . ASN A 1 106 ? 11.172  3.750   90.782 1.00 18.99 ?  106 ASN A CA    1 
ATOM   830  C C     . ASN A 1 106 ? 12.300  4.663   91.268 1.00 10.14 ?  106 ASN A C     1 
ATOM   831  O O     . ASN A 1 106 ? 12.155  5.302   92.315 1.00 1.67  ?  106 ASN A O     1 
ATOM   832  C CB    . ASN A 1 106 ? 10.477  3.098   91.988 1.00 22.89 ?  106 ASN A CB    1 
ATOM   833  C CG    . ASN A 1 106 ? 9.122   2.506   91.636 1.00 27.14 ?  106 ASN A CG    1 
ATOM   834  O OD1   . ASN A 1 106 ? 9.005   1.307   91.355 1.00 24.96 ?  106 ASN A OD1   1 
ATOM   835  N ND2   . ASN A 1 106 ? 8.089   3.353   91.634 1.00 5.81  ?  106 ASN A ND2   1 
ATOM   836  N N     . GLU A 1 107 ? 13.440  4.702   90.577 1.00 15.85 ?  107 GLU A N     1 
ATOM   837  C CA    . GLU A 1 107 ? 14.440  5.739   90.834 1.00 26.43 ?  107 GLU A CA    1 
ATOM   838  C C     . GLU A 1 107 ? 14.097  7.012   90.053 1.00 23.78 ?  107 GLU A C     1 
ATOM   839  O O     . GLU A 1 107 ? 13.279  7.005   89.132 1.00 38.08 ?  107 GLU A O     1 
ATOM   840  C CB    . GLU A 1 107 ? 15.858  5.254   90.480 1.00 11.39 ?  107 GLU A CB    1 
ATOM   841  C CG    . GLU A 1 107 ? 16.489  4.255   91.481 1.00 15.17 ?  107 GLU A CG    1 
ATOM   842  C CD    . GLU A 1 107 ? 17.697  3.467   90.903 1.00 26.99 ?  107 GLU A CD    1 
ATOM   843  O OE1   . GLU A 1 107 ? 17.984  3.553   89.690 1.00 22.62 ?  107 GLU A OE1   1 
ATOM   844  O OE2   . GLU A 1 107 ? 18.342  2.721   91.665 1.00 33.37 -1 107 GLU A OE2   1 
ATOM   845  N N     . SER A 1 108 ? 14.746  8.111   90.422 1.00 17.05 ?  108 SER A N     1 
ATOM   846  C CA    . SER A 1 108 ? 14.368  9.435   89.938 1.00 3.80  ?  108 SER A CA    1 
ATOM   847  C C     . SER A 1 108 ? 15.142  9.795   88.679 1.00 1.38  ?  108 SER A C     1 
ATOM   848  O O     . SER A 1 108 ? 16.360  9.605   88.619 1.00 40.35 ?  108 SER A O     1 
ATOM   849  C CB    . SER A 1 108 ? 14.656  10.497  91.006 1.00 11.31 ?  108 SER A CB    1 
ATOM   850  O OG    . SER A 1 108 ? 13.973  10.241  92.218 1.00 23.97 ?  108 SER A OG    1 
ATOM   851  N N     . VAL A 1 109 ? 14.431  10.332  87.695 1.00 1.37  ?  109 VAL A N     1 
ATOM   852  C CA    . VAL A 1 109 ? 14.985  10.937  86.489 1.00 6.78  ?  109 VAL A CA    1 
ATOM   853  C C     . VAL A 1 109 ? 14.363  12.329  86.370 1.00 10.81 ?  109 VAL A C     1 
ATOM   854  O O     . VAL A 1 109 ? 13.149  12.496  86.575 1.00 1.37  ?  109 VAL A O     1 
ATOM   855  C CB    . VAL A 1 109 ? 14.693  10.074  85.237 1.00 4.49  ?  109 VAL A CB    1 
ATOM   856  C CG1   . VAL A 1 109 ? 15.270  10.695  83.965 1.00 1.35  ?  109 VAL A CG1   1 
ATOM   857  C CG2   . VAL A 1 109 ? 15.208  8.636   85.435 1.00 1.35  ?  109 VAL A CG2   1 
ATOM   858  N N     . LEU A 1 110 ? 15.201  13.330  86.070 1.00 10.16 ?  110 LEU A N     1 
ATOM   859  C CA    . LEU A 1 110 ? 14.810  14.737  86.112 1.00 5.96  ?  110 LEU A CA    1 
ATOM   860  C C     . LEU A 1 110 ? 14.738  15.357  84.718 1.00 9.90  ?  110 LEU A C     1 
ATOM   861  O O     . LEU A 1 110 ? 15.549  15.046  83.833 1.00 9.18  ?  110 LEU A O     1 
ATOM   862  C CB    . LEU A 1 110 ? 15.748  15.548  87.015 1.00 12.58 ?  110 LEU A CB    1 
ATOM   863  C CG    . LEU A 1 110 ? 15.416  17.057  87.070 1.00 28.09 ?  110 LEU A CG    1 
ATOM   864  C CD1   . LEU A 1 110 ? 15.291  17.607  88.507 1.00 15.72 ?  110 LEU A CD1   1 
ATOM   865  C CD2   . LEU A 1 110 ? 16.407  17.890  86.237 1.00 25.79 ?  110 LEU A CD2   1 
ATOM   866  N N     . VAL A 1 111 ? 13.749  16.232  84.539 1.00 1.37  ?  111 VAL A N     1 
ATOM   867  C CA    . VAL A 1 111 ? 13.523  16.968  83.305 1.00 14.63 ?  111 VAL A CA    1 
ATOM   868  C C     . VAL A 1 111 ? 13.199  18.432  83.651 1.00 1.40  ?  111 VAL A C     1 
ATOM   869  O O     . VAL A 1 111 ? 12.888  18.776  84.794 1.00 1.39  ?  111 VAL A O     1 
ATOM   870  C CB    . VAL A 1 111 ? 12.407  16.280  82.470 1.00 22.91 ?  111 VAL A CB    1 
ATOM   871  C CG1   . VAL A 1 111 ? 12.841  14.862  82.036 1.00 9.07  ?  111 VAL A CG1   1 
ATOM   872  C CG2   . VAL A 1 111 ? 11.084  16.171  83.249 1.00 12.22 ?  111 VAL A CG2   1 
ATOM   873  N N     . GLN A 1 112 ? 13.266  19.307  82.652 1.00 15.01 ?  112 GLN A N     1 
ATOM   874  C CA    . GLN A 1 112 ? 13.048  20.744  82.879 1.00 27.66 ?  112 GLN A CA    1 
ATOM   875  C C     . GLN A 1 112 ? 11.944  21.262  81.964 1.00 12.33 ?  112 GLN A C     1 
ATOM   876  O O     . GLN A 1 112 ? 12.194  21.585  80.794 1.00 6.58  ?  112 GLN A O     1 
ATOM   877  C CB    . GLN A 1 112 ? 14.336  21.559  82.683 1.00 29.21 ?  112 GLN A CB    1 
ATOM   878  C CG    . GLN A 1 112 ? 15.597  20.935  83.279 1.00 6.97  ?  112 GLN A CG    1 
ATOM   879  C CD    . GLN A 1 112 ? 16.843  21.771  83.068 1.00 1.42  ?  112 GLN A CD    1 
ATOM   880  O OE1   . GLN A 1 112 ? 17.337  21.932  81.950 1.00 1.48  ?  112 GLN A OE1   1 
ATOM   881  N NE2   . GLN A 1 112 ? 17.375  22.284  84.155 1.00 9.88  ?  112 GLN A NE2   1 
ATOM   882  N N     . PRO A 1 113 ? 10.701  21.283  82.437 1.00 14.99 ?  113 PRO A N     1 
ATOM   883  C CA    . PRO A 1 113 ? 9.591   21.801  81.611 1.00 27.32 ?  113 PRO A CA    1 
ATOM   884  C C     . PRO A 1 113 ? 9.646   23.318  81.501 1.00 32.83 ?  113 PRO A C     1 
ATOM   885  O O     . PRO A 1 113 ? 10.236  23.986  82.363 1.00 28.81 ?  113 PRO A O     1 
ATOM   886  C CB    . PRO A 1 113 ? 8.343   21.341  82.375 1.00 25.83 ?  113 PRO A CB    1 
ATOM   887  C CG    . PRO A 1 113 ? 8.805   21.148  83.779 1.00 24.63 ?  113 PRO A CG    1 
ATOM   888  C CD    . PRO A 1 113 ? 10.235  20.729  83.719 1.00 6.59  ?  113 PRO A CD    1 
ATOM   889  N N     . PRO A 1 114 ? 9.036   23.915  80.450 1.00 33.50 ?  114 PRO A N     1 
ATOM   890  C CA    . PRO A 1 114 ? 8.304   23.239  79.372 1.00 27.72 ?  114 PRO A CA    1 
ATOM   891  C C     . PRO A 1 114 ? 9.211   22.496  78.409 1.00 21.23 ?  114 PRO A C     1 
ATOM   892  O O     . PRO A 1 114 ? 10.089  23.150  77.836 1.00 15.06 ?  114 PRO A O     1 
ATOM   893  C CB    . PRO A 1 114 ? 7.606   24.398  78.647 1.00 19.44 ?  114 PRO A CB    1 
ATOM   894  C CG    . PRO A 1 114 ? 8.391   25.604  78.994 1.00 9.94  ?  114 PRO A CG    1 
ATOM   895  C CD    . PRO A 1 114 ? 8.827   25.374  80.397 1.00 18.03 ?  114 PRO A CD    1 
ATOM   896  N N     . ILE A 1 115 ? 8.925   21.213  78.150 1.00 1.60  ?  115 ILE A N     1 
ATOM   897  C CA    . ILE A 1 115 ? 9.853   20.318  77.459 1.00 1.60  ?  115 ILE A CA    1 
ATOM   898  C C     . ILE A 1 115 ? 9.083   19.247  76.701 1.00 16.20 ?  115 ILE A C     1 
ATOM   899  O O     . ILE A 1 115 ? 7.957   18.895  77.061 1.00 29.50 ?  115 ILE A O     1 
ATOM   900  C CB    . ILE A 1 115 ? 10.820  19.661  78.469 1.00 19.16 ?  115 ILE A CB    1 
ATOM   901  C CG1   . ILE A 1 115 ? 11.896  18.824  77.767 1.00 36.94 ?  115 ILE A CG1   1 
ATOM   902  C CG2   . ILE A 1 115 ? 10.052  18.829  79.488 1.00 5.62  ?  115 ILE A CG2   1 
ATOM   903  C CD1   . ILE A 1 115 ? 12.712  19.608  76.779 1.00 37.23 ?  115 ILE A CD1   1 
ATOM   904  N N     . TYR A 1 116 ? 9.724   18.704  75.657 1.00 17.03 ?  116 TYR A N     1 
ATOM   905  C CA    . TYR A 1 116 ? 9.287   17.577  74.830 1.00 26.53 ?  116 TYR A CA    1 
ATOM   906  C C     . TYR A 1 116 ? 8.567   16.517  75.643 1.00 18.00 ?  116 TYR A C     1 
ATOM   907  O O     . TYR A 1 116 ? 9.154   15.960  76.576 1.00 14.02 ?  116 TYR A O     1 
ATOM   908  C CB    . TYR A 1 116 ? 10.498  16.913  74.187 1.00 20.53 ?  116 TYR A CB    1 
ATOM   909  C CG    . TYR A 1 116 ? 10.226  16.014  73.009 1.00 9.97  ?  116 TYR A CG    1 
ATOM   910  C CD1   . TYR A 1 116 ? 9.316   16.363  72.044 1.00 2.16  ?  116 TYR A CD1   1 
ATOM   911  C CD2   . TYR A 1 116 ? 10.945  14.843  72.834 1.00 19.41 ?  116 TYR A CD2   1 
ATOM   912  C CE1   . TYR A 1 116 ? 9.099   15.562  70.952 1.00 23.43 ?  116 TYR A CE1   1 
ATOM   913  C CE2   . TYR A 1 116 ? 10.737  14.035  71.742 1.00 15.51 ?  116 TYR A CE2   1 
ATOM   914  C CZ    . TYR A 1 116 ? 9.811   14.392  70.807 1.00 21.58 ?  116 TYR A CZ    1 
ATOM   915  O OH    . TYR A 1 116 ? 9.600   13.579  69.716 1.00 22.04 ?  116 TYR A OH    1 
ATOM   916  N N     . PRO A 1 117 ? 7.326   16.187  75.310 1.00 23.54 ?  117 PRO A N     1 
ATOM   917  C CA    . PRO A 1 117 ? 6.531   15.314  76.183 1.00 1.64  ?  117 PRO A CA    1 
ATOM   918  C C     . PRO A 1 117 ? 7.118   13.912  76.338 1.00 19.61 ?  117 PRO A C     1 
ATOM   919  O O     . PRO A 1 117 ? 7.013   13.341  77.436 1.00 18.76 ?  117 PRO A O     1 
ATOM   920  C CB    . PRO A 1 117 ? 5.159   15.286  75.499 1.00 13.24 ?  117 PRO A CB    1 
ATOM   921  C CG    . PRO A 1 117 ? 5.157   16.404  74.530 1.00 1.74  ?  117 PRO A CG    1 
ATOM   922  C CD    . PRO A 1 117 ? 6.556   16.713  74.165 1.00 10.20 ?  117 PRO A CD    1 
ATOM   923  N N     . PRO A 1 118 ? 7.769   13.287  75.278 1.00 7.23  ?  118 PRO A N     1 
ATOM   924  C CA    . PRO A 1 118 ? 8.391   11.962  75.493 1.00 7.07  ?  118 PRO A CA    1 
ATOM   925  C C     . PRO A 1 118 ? 9.371   11.892  76.660 1.00 18.40 ?  118 PRO A C     1 
ATOM   926  O O     . PRO A 1 118 ? 9.663   10.806  77.171 1.00 31.40 ?  118 PRO A O     1 
ATOM   927  C CB    . PRO A 1 118 ? 9.074   11.683  74.151 1.00 10.59 ?  118 PRO A CB    1 
ATOM   928  C CG    . PRO A 1 118 ? 8.125   12.270  73.180 1.00 16.71 ?  118 PRO A CG    1 
ATOM   929  C CD    . PRO A 1 118 ? 7.624   13.539  73.829 1.00 19.29 ?  118 PRO A CD    1 
ATOM   930  N N     . PHE A 1 119 ? 9.912   13.029  77.082 1.00 19.27 ?  119 PHE A N     1 
ATOM   931  C CA    . PHE A 1 119 ? 10.649  13.051  78.340 1.00 1.49  ?  119 PHE A CA    1 
ATOM   932  C C     . PHE A 1 119 ? 9.730   12.726  79.511 1.00 1.47  ?  119 PHE A C     1 
ATOM   933  O O     . PHE A 1 119 ? 10.186  12.209  80.527 1.00 15.78 ?  119 PHE A O     1 
ATOM   934  C CB    . PHE A 1 119 ? 11.304  14.420  78.570 1.00 1.49  ?  119 PHE A CB    1 
ATOM   935  C CG    . PHE A 1 119 ? 12.453  14.735  77.655 1.00 2.18  ?  119 PHE A CG    1 
ATOM   936  C CD1   . PHE A 1 119 ? 12.340  14.597  76.284 1.00 9.08  ?  119 PHE A CD1   1 
ATOM   937  C CD2   . PHE A 1 119 ? 13.625  15.251  78.168 1.00 14.46 ?  119 PHE A CD2   1 
ATOM   938  C CE1   . PHE A 1 119 ? 13.387  14.924  75.443 1.00 28.17 ?  119 PHE A CE1   1 
ATOM   939  C CE2   . PHE A 1 119 ? 14.685  15.594  77.328 1.00 26.61 ?  119 PHE A CE2   1 
ATOM   940  C CZ    . PHE A 1 119 ? 14.564  15.429  75.968 1.00 33.93 ?  119 PHE A CZ    1 
ATOM   941  N N     . PHE A 1 120 ? 8.453   13.119  79.432 1.00 7.97  ?  120 PHE A N     1 
ATOM   942  C CA    . PHE A 1 120 ? 7.495   12.767  80.483 1.00 4.51  ?  120 PHE A CA    1 
ATOM   943  C C     . PHE A 1 120 ? 7.067   11.300  80.370 1.00 1.52  ?  120 PHE A C     1 
ATOM   944  O O     . PHE A 1 120 ? 7.115   10.547  81.350 1.00 1.52  ?  120 PHE A O     1 
ATOM   945  C CB    . PHE A 1 120 ? 6.254   13.679  80.423 1.00 15.86 ?  120 PHE A CB    1 
ATOM   946  C CG    . PHE A 1 120 ? 6.527   15.165  80.655 1.00 15.10 ?  120 PHE A CG    1 
ATOM   947  C CD1   . PHE A 1 120 ? 6.750   15.668  81.923 1.00 9.97  ?  120 PHE A CD1   1 
ATOM   948  C CD2   . PHE A 1 120 ? 6.512   16.058  79.600 1.00 9.02  ?  120 PHE A CD2   1 
ATOM   949  C CE1   . PHE A 1 120 ? 6.976   17.010  82.121 1.00 4.61  ?  120 PHE A CE1   1 
ATOM   950  C CE2   . PHE A 1 120 ? 6.751   17.407  79.807 1.00 3.39  ?  120 PHE A CE2   1 
ATOM   951  C CZ    . PHE A 1 120 ? 6.973   17.874  81.061 1.00 1.54  ?  120 PHE A CZ    1 
ATOM   952  N N     . GLU A 1 121 ? 6.694   10.870  79.165 1.00 1.54  ?  121 GLU A N     1 
ATOM   953  C CA    . GLU A 1 121 ? 6.022   9.585   78.991 1.00 33.59 ?  121 GLU A CA    1 
ATOM   954  C C     . GLU A 1 121 ? 6.963   8.400   79.210 1.00 17.72 ?  121 GLU A C     1 
ATOM   955  O O     . GLU A 1 121 ? 6.593   7.433   79.882 1.00 18.59 ?  121 GLU A O     1 
ATOM   956  C CB    . GLU A 1 121 ? 5.383   9.544   77.599 1.00 27.06 ?  121 GLU A CB    1 
ATOM   957  C CG    . GLU A 1 121 ? 4.251   10.547  77.439 1.00 12.20 ?  121 GLU A CG    1 
ATOM   958  C CD    . GLU A 1 121 ? 3.050   10.192  78.270 1.00 9.41  ?  121 GLU A CD    1 
ATOM   959  O OE1   . GLU A 1 121 ? 2.959   10.683  79.410 1.00 11.90 ?  121 GLU A OE1   1 
ATOM   960  O OE2   . GLU A 1 121 ? 2.180   9.458   77.769 1.00 21.52 -1 121 GLU A OE2   1 
ATOM   961  N N     . MET A 1 122 ? 8.211   8.502   78.757 1.00 17.97 ?  122 MET A N     1 
ATOM   962  C CA    . MET A 1 122 ? 9.129   7.368   78.854 1.00 5.80  ?  122 MET A CA    1 
ATOM   963  C C     . MET A 1 122 ? 9.585   7.130   80.287 1.00 5.27  ?  122 MET A C     1 
ATOM   964  O O     . MET A 1 122 ? 9.882   5.996   80.668 1.00 24.74 ?  122 MET A O     1 
ATOM   965  C CB    . MET A 1 122 ? 10.351  7.602   77.980 1.00 6.57  ?  122 MET A CB    1 
ATOM   966  C CG    . MET A 1 122 ? 10.085  7.842   76.508 1.00 14.07 ?  122 MET A CG    1 
ATOM   967  S SD    . MET A 1 122 ? 9.200   6.537   75.673 1.00 16.27 ?  122 MET A SD    1 
ATOM   968  C CE    . MET A 1 122 ? 7.659   7.353   75.241 1.00 4.46  ?  122 MET A CE    1 
ATOM   969  N N     . VAL A 1 123 ? 9.719   8.190   81.074 1.00 20.32 ?  123 VAL A N     1 
ATOM   970  C CA    . VAL A 1 123 ? 10.128  8.040   82.469 1.00 26.02 ?  123 VAL A CA    1 
ATOM   971  C C     . VAL A 1 123 ? 9.082   7.262   83.266 1.00 1.48  ?  123 VAL A C     1 
ATOM   972  O O     . VAL A 1 123 ? 9.416   6.409   84.093 1.00 1.49  ?  123 VAL A O     1 
ATOM   973  C CB    . VAL A 1 123 ? 10.411  9.424   83.082 1.00 1.42  ?  123 VAL A CB    1 
ATOM   974  C CG1   . VAL A 1 123 ? 10.893  9.280   84.496 1.00 1.42  ?  123 VAL A CG1   1 
ATOM   975  C CG2   . VAL A 1 123 ? 11.417  10.131  82.255 1.00 1.40  ?  123 VAL A CG2   1 
ATOM   976  N N     . THR A 1 124 ? 7.812   7.650   83.120 1.00 1.52  ?  124 THR A N     1 
ATOM   977  C CA    . THR A 1 124 ? 6.724   7.115   83.932 1.00 12.67 ?  124 THR A CA    1 
ATOM   978  C C     . THR A 1 124 ? 6.240   5.754   83.432 1.00 1.64  ?  124 THR A C     1 
ATOM   979  O O     . THR A 1 124 ? 5.868   4.907   84.237 1.00 16.94 ?  124 THR A O     1 
ATOM   980  C CB    . THR A 1 124 ? 5.573   8.112   83.975 1.00 19.48 ?  124 THR A CB    1 
ATOM   981  O OG1   . THR A 1 124 ? 5.467   8.751   82.697 1.00 28.63 ?  124 THR A OG1   1 
ATOM   982  C CG2   . THR A 1 124 ? 5.802   9.181   85.050 1.00 10.27 ?  124 THR A CG2   1 
ATOM   983  N N     . THR A 1 125 ? 6.209   5.532   82.117 1.00 1.62  ?  125 THR A N     1 
ATOM   984  C CA    . THR A 1 125 ? 5.789   4.232   81.611 1.00 1.66  ?  125 THR A CA    1 
ATOM   985  C C     . THR A 1 125 ? 6.788   3.134   81.982 1.00 5.97  ?  125 THR A C     1 
ATOM   986  O O     . THR A 1 125 ? 6.407   1.960   82.066 1.00 8.23  ?  125 THR A O     1 
ATOM   987  C CB    . THR A 1 125 ? 5.561   4.271   80.083 1.00 5.53  ?  125 THR A CB    1 
ATOM   988  O OG1   . THR A 1 125 ? 6.640   4.927   79.415 1.00 6.45  ?  125 THR A OG1   1 
ATOM   989  C CG2   . THR A 1 125 ? 4.286   4.995   79.758 1.00 11.39 ?  125 THR A CG2   1 
ATOM   990  N N     . ASN A 1 126 ? 8.046   3.495   82.233 1.00 9.80  ?  126 ASN A N     1 
ATOM   991  C CA    . ASN A 1 126 ? 9.085   2.565   82.645 1.00 1.53  ?  126 ASN A CA    1 
ATOM   992  C C     . ASN A 1 126 ? 9.213   2.490   84.156 1.00 10.45 ?  126 ASN A C     1 
ATOM   993  O O     . ASN A 1 126 ? 10.252  2.063   84.670 1.00 2.07  ?  126 ASN A O     1 
ATOM   994  C CB    . ASN A 1 126 ? 10.411  2.947   82.013 1.00 1.45  ?  126 ASN A CB    1 
ATOM   995  C CG    . ASN A 1 126 ? 10.534  2.470   80.589 1.00 27.99 ?  126 ASN A CG    1 
ATOM   996  O OD1   . ASN A 1 126 ? 10.873  1.317   80.331 1.00 36.64 ?  126 ASN A OD1   1 
ATOM   997  N ND2   . ASN A 1 126 ? 10.251  3.361   79.645 1.00 6.56  ?  126 ASN A ND2   1 
ATOM   998  N N     . ASN A 1 127 ? 8.204   2.967   84.873 1.00 16.41 ?  127 ASN A N     1 
ATOM   999  C CA    . ASN A 1 127 ? 8.131   2.845   86.328 1.00 28.01 ?  127 ASN A CA    1 
ATOM   1000 C C     . ASN A 1 127 ? 9.367   3.432   86.985 1.00 18.43 ?  127 ASN A C     1 
ATOM   1001 O O     . ASN A 1 127 ? 9.956   2.850   87.901 1.00 29.13 ?  127 ASN A O     1 
ATOM   1002 C CB    . ASN A 1 127 ? 7.878   1.402   86.767 1.00 33.15 ?  127 ASN A CB    1 
ATOM   1003 C CG    . ASN A 1 127 ? 6.389   1.086   86.878 1.00 25.44 ?  127 ASN A CG    1 
ATOM   1004 O OD1   . ASN A 1 127 ? 5.869   0.873   87.970 1.00 16.31 ?  127 ASN A OD1   1 
ATOM   1005 N ND2   . ASN A 1 127 ? 5.704   1.060   85.744 1.00 21.19 ?  127 ASN A ND2   1 
ATOM   1006 N N     . ARG A 1 128 ? 9.776   4.583   86.493 1.00 13.85 ?  128 ARG A N     1 
ATOM   1007 C CA    . ARG A 1 128 ? 10.700  5.413   87.238 1.00 21.00 ?  128 ARG A CA    1 
ATOM   1008 C C     . ARG A 1 128 ? 9.955   6.645   87.742 1.00 28.33 ?  128 ARG A C     1 
ATOM   1009 O O     . ARG A 1 128 ? 8.808   6.916   87.370 1.00 15.09 ?  128 ARG A O     1 
ATOM   1010 C CB    . ARG A 1 128 ? 11.922  5.792   86.383 1.00 1.52  ?  128 ARG A CB    1 
ATOM   1011 C CG    . ARG A 1 128 ? 13.088  4.763   86.447 1.00 14.96 ?  128 ARG A CG    1 
ATOM   1012 C CD    . ARG A 1 128 ? 12.690  3.409   85.817 1.00 23.47 ?  128 ARG A CD    1 
ATOM   1013 N NE    . ARG A 1 128 ? 13.792  2.608   85.270 1.00 34.34 ?  128 ARG A NE    1 
ATOM   1014 C CZ    . ARG A 1 128 ? 13.642  1.388   84.760 1.00 16.28 ?  128 ARG A CZ    1 
ATOM   1015 N NH1   . ARG A 1 128 ? 12.442  0.832   84.720 1.00 34.80 1  128 ARG A NH1   1 
ATOM   1016 N NH2   . ARG A 1 128 ? 14.683  0.728   84.281 1.00 7.85  ?  128 ARG A NH2   1 
ATOM   1017 N N     . GLN A 1 129 ? 10.536  7.280   88.775 1.00 38.60 ?  129 GLN A N     1 
ATOM   1018 C CA    . GLN A 1 129 ? 9.993   8.518   89.371 1.00 18.64 ?  129 GLN A CA    1 
ATOM   1019 C C     . GLN A 1 129 ? 10.252  9.707   88.489 1.00 15.26 ?  129 GLN A C     1 
ATOM   1020 O O     . GLN A 1 129 ? 11.375  9.923   88.126 1.00 21.10 ?  129 GLN A O     1 
ATOM   1021 C CB    . GLN A 1 129 ? 10.639  8.848   90.706 1.00 13.67 ?  129 GLN A CB    1 
ATOM   1022 C CG    . GLN A 1 129 ? 9.915   9.890   91.535 1.00 12.62 ?  129 GLN A CG    1 
ATOM   1023 C CD    . GLN A 1 129 ? 10.469  9.884   92.935 1.00 26.39 ?  129 GLN A CD    1 
ATOM   1024 O OE1   . GLN A 1 129 ? 10.881  8.857   93.463 1.00 27.72 ?  129 GLN A OE1   1 
ATOM   1025 N NE2   . GLN A 1 129 ? 10.463  11.047  93.560 1.00 34.73 ?  129 GLN A NE2   1 
ATOM   1026 N N     . LEU A 1 130 ? 9.181   10.406  88.159 1.00 23.60 ?  130 LEU A N     1 
ATOM   1027 C CA    . LEU A 1 130 ? 9.303   11.669  87.452 1.00 19.15 ?  130 LEU A CA    1 
ATOM   1028 C C     . LEU A 1 130 ? 9.676   12.747  88.453 1.00 37.42 ?  130 LEU A C     1 
ATOM   1029 O O     . LEU A 1 130 ? 8.921   13.021  89.391 1.00 35.59 ?  130 LEU A O     1 
ATOM   1030 C CB    . LEU A 1 130 ? 8.006   12.015  86.749 1.00 8.94  ?  130 LEU A CB    1 
ATOM   1031 C CG    . LEU A 1 130 ? 8.162   13.161  85.783 1.00 1.50  ?  130 LEU A CG    1 
ATOM   1032 C CD1   . LEU A 1 130 ? 8.999   12.694  84.617 1.00 1.46  ?  130 LEU A CD1   1 
ATOM   1033 C CD2   . LEU A 1 130 ? 6.786   13.556  85.352 1.00 1.55  ?  130 LEU A CD2   1 
ATOM   1034 N N     . CYS A 1 131 ? 10.845  13.342  88.271 1.00 44.17 ?  131 CYS A N     1 
ATOM   1035 C CA    . CYS A 1 131 ? 11.203  14.554  88.978 1.00 21.99 ?  131 CYS A CA    1 
ATOM   1036 C C     . CYS A 1 131 ? 11.359  15.658  87.947 1.00 30.71 ?  131 CYS A C     1 
ATOM   1037 O O     . CYS A 1 131 ? 11.677  15.398  86.782 1.00 28.81 ?  131 CYS A O     1 
ATOM   1038 C CB    . CYS A 1 131 ? 12.474  14.364  89.792 1.00 28.57 ?  131 CYS A CB    1 
ATOM   1039 S SG    . CYS A 1 131 ? 12.345  12.993  90.965 1.00 36.42 ?  131 CYS A SG    1 
ATOM   1040 N N     . VAL A 1 132 ? 11.030  16.882  88.362 1.00 34.31 ?  132 VAL A N     1 
ATOM   1041 C CA    . VAL A 1 132 ? 11.096  18.058  87.504 1.00 13.18 ?  132 VAL A CA    1 
ATOM   1042 C C     . VAL A 1 132 ? 11.970  19.109  88.164 1.00 2.88  ?  132 VAL A C     1 
ATOM   1043 O O     . VAL A 1 132 ? 12.220  19.076  89.374 1.00 3.54  ?  132 VAL A O     1 
ATOM   1044 C CB    . VAL A 1 132 ? 9.705   18.676  87.170 1.00 9.29  ?  132 VAL A CB    1 
ATOM   1045 C CG1   . VAL A 1 132 ? 8.991   17.845  86.187 1.00 2.37  ?  132 VAL A CG1   1 
ATOM   1046 C CG2   . VAL A 1 132 ? 8.856   18.899  88.422 1.00 2.38  ?  132 VAL A CG2   1 
ATOM   1047 N N     . SER A 1 133 ? 12.525  19.972  87.326 1.00 1.38  ?  133 SER A N     1 
ATOM   1048 C CA    . SER A 1 133 ? 13.072  21.265  87.747 1.00 25.58 ?  133 SER A CA    1 
ATOM   1049 C C     . SER A 1 133 ? 12.653  22.294  86.700 1.00 31.58 ?  133 SER A C     1 
ATOM   1050 O O     . SER A 1 133 ? 13.408  22.602  85.769 1.00 30.60 ?  133 SER A O     1 
ATOM   1051 C CB    . SER A 1 133 ? 14.586  21.207  87.923 1.00 3.34  ?  133 SER A CB    1 
ATOM   1052 O OG    . SER A 1 133 ? 15.158  22.442  87.596 1.00 13.98 ?  133 SER A OG    1 
ATOM   1053 N N     . PRO A 1 134 ? 11.446  22.851  86.828 1.00 27.16 ?  134 PRO A N     1 
ATOM   1054 C CA    . PRO A 1 134 ? 10.884  23.727  85.777 1.00 5.89  ?  134 PRO A CA    1 
ATOM   1055 C C     . PRO A 1 134 ? 11.747  24.946  85.440 1.00 1.43  ?  134 PRO A C     1 
ATOM   1056 O O     . PRO A 1 134 ? 12.328  25.580  86.319 1.00 1.41  ?  134 PRO A O     1 
ATOM   1057 C CB    . PRO A 1 134 ? 9.543   24.175  86.374 1.00 6.05  ?  134 PRO A CB    1 
ATOM   1058 C CG    . PRO A 1 134 ? 9.292   23.298  87.547 1.00 4.29  ?  134 PRO A CG    1 
ATOM   1059 C CD    . PRO A 1 134 ? 10.597  22.768  88.022 1.00 1.42  ?  134 PRO A CD    1 
ATOM   1060 N N     . LEU A 1 135 ? 11.792  25.284  84.151 1.00 1.45  ?  135 LEU A N     1 
ATOM   1061 C CA    . LEU A 1 135 ? 12.483  26.475  83.672 1.00 30.09 ?  135 LEU A CA    1 
ATOM   1062 C C     . LEU A 1 135 ? 11.763  27.764  84.112 1.00 20.50 ?  135 LEU A C     1 
ATOM   1063 O O     . LEU A 1 135 ? 10.563  27.775  84.400 1.00 15.70 ?  135 LEU A O     1 
ATOM   1064 C CB    . LEU A 1 135 ? 12.611  26.422  82.143 1.00 29.43 ?  135 LEU A CB    1 
ATOM   1065 C CG    . LEU A 1 135 ? 13.415  25.281  81.483 1.00 14.36 ?  135 LEU A CG    1 
ATOM   1066 C CD1   . LEU A 1 135 ? 13.303  25.362  79.969 1.00 10.47 ?  135 LEU A CD1   1 
ATOM   1067 C CD2   . LEU A 1 135 ? 14.879  25.319  81.882 1.00 1.48  ?  135 LEU A CD2   1 
ATOM   1068 N N     . GLN A 1 136 ? 12.544  28.837  84.210 1.00 21.78 ?  136 GLN A N     1 
ATOM   1069 C CA    . GLN A 1 136 ? 12.011  30.155  84.661 1.00 22.77 ?  136 GLN A CA    1 
ATOM   1070 C C     . GLN A 1 136 ? 12.032  31.169  83.533 1.00 12.44 ?  136 GLN A C     1 
ATOM   1071 O O     . GLN A 1 136 ? 13.051  31.244  82.953 1.00 1.52  ?  136 GLN A O     1 
ATOM   1072 C CB    . GLN A 1 136 ? 12.639  30.665  85.948 1.00 14.66 ?  136 GLN A CB    1 
ATOM   1073 C CG    . GLN A 1 136 ? 12.505  29.695  87.106 1.00 20.33 ?  136 GLN A CG    1 
ATOM   1074 C CD    . GLN A 1 136 ? 12.149  30.447  88.361 1.00 28.62 ?  136 GLN A CD    1 
ATOM   1075 O OE1   . GLN A 1 136 ? 12.248  31.667  88.420 1.00 33.27 ?  136 GLN A OE1   1 
ATOM   1076 N NE2   . GLN A 1 136 ? 11.720  29.721  89.375 1.00 24.14 ?  136 GLN A NE2   1 
ATOM   1077 N N     . LYS A 1 137 ? 10.872  31.759  83.212 1.00 7.67  ?  137 LYS A N     1 
ATOM   1078 C CA    . LYS A 1 137 ? 10.673  32.752  82.162 1.00 14.34 ?  137 LYS A CA    1 
ATOM   1079 C C     . LYS A 1 137 ? 11.118  34.134  82.638 1.00 29.67 ?  137 LYS A C     1 
ATOM   1080 O O     . LYS A 1 137 ? 10.634  34.632  83.659 1.00 30.87 ?  137 LYS A O     1 
ATOM   1081 C CB    . LYS A 1 137 ? 9.207   32.782  81.747 1.00 1.62  ?  137 LYS A CB    1 
ATOM   1082 C CG    . LYS A 1 137 ? 8.960   33.182  80.301 1.00 26.23 ?  137 LYS A CG    1 
ATOM   1083 C CD    . LYS A 1 137 ? 7.526   33.713  80.167 1.00 27.44 ?  137 LYS A CD    1 
ATOM   1084 C CE    . LYS A 1 137 ? 7.041   33.751  78.726 1.00 24.52 ?  137 LYS A CE    1 
ATOM   1085 N NZ    . LYS A 1 137 ? 6.060   34.846  78.441 1.00 23.32 1  137 LYS A NZ    1 
ATOM   1086 N N     . GLN A 1 138 ? 12.108  34.709  81.964 1.00 24.58 ?  138 GLN A N     1 
ATOM   1087 C CA    . GLN A 1 138 ? 12.512  36.068  82.293 1.00 21.25 ?  138 GLN A CA    1 
ATOM   1088 C C     . GLN A 1 138 ? 12.791  36.839  81.017 1.00 27.39 ?  138 GLN A C     1 
ATOM   1089 O O     . GLN A 1 138 ? 13.509  36.357  80.134 1.00 21.52 ?  138 GLN A O     1 
ATOM   1090 C CB    . GLN A 1 138 ? 13.763  36.103  83.175 1.00 31.65 ?  138 GLN A CB    1 
ATOM   1091 C CG    . GLN A 1 138 ? 13.575  35.422  84.518 1.00 40.07 ?  138 GLN A CG    1 
ATOM   1092 C CD    . GLN A 1 138 ? 14.887  35.176  85.227 1.00 37.36 ?  138 GLN A CD    1 
ATOM   1093 O OE1   . GLN A 1 138 ? 15.948  35.555  84.732 1.00 44.38 ?  138 GLN A OE1   1 
ATOM   1094 N NE2   . GLN A 1 138 ? 14.824  34.540  86.395 1.00 31.15 ?  138 GLN A NE2   1 
ATOM   1095 N N     . ASN A 1 139 ? 12.241  38.052  80.954 1.00 30.39 ?  139 ASN A N     1 
ATOM   1096 C CA    . ASN A 1 139 ? 12.561  39.015  79.907 1.00 38.79 ?  139 ASN A CA    1 
ATOM   1097 C C     . ASN A 1 139 ? 12.434  38.402  78.509 1.00 41.54 ?  139 ASN A C     1 
ATOM   1098 O O     . ASN A 1 139 ? 13.259  38.646  77.623 1.00 51.33 ?  139 ASN A O     1 
ATOM   1099 C CB    . ASN A 1 139 ? 13.956  39.613  80.120 1.00 40.86 ?  139 ASN A CB    1 
ATOM   1100 C CG    . ASN A 1 139 ? 14.017  40.575  81.305 1.00 45.33 ?  139 ASN A CG    1 
ATOM   1101 O OD1   . ASN A 1 139 ? 13.026  41.219  81.660 1.00 43.53 ?  139 ASN A OD1   1 
ATOM   1102 N ND2   . ASN A 1 139 ? 15.201  40.689  81.909 1.00 46.16 ?  139 ASN A ND2   1 
ATOM   1103 N N     . ASP A 1 140 ? 11.373  37.613  78.316 1.00 13.33 ?  140 ASP A N     1 
ATOM   1104 C CA    . ASP A 1 140 ? 11.115  36.914  77.057 1.00 12.02 ?  140 ASP A CA    1 
ATOM   1105 C C     . ASP A 1 140 ? 12.262  35.980  76.636 1.00 16.88 ?  140 ASP A C     1 
ATOM   1106 O O     . ASP A 1 140 ? 12.596  35.850  75.453 1.00 15.09 ?  140 ASP A O     1 
ATOM   1107 C CB    . ASP A 1 140 ? 10.776  37.923  75.966 1.00 8.44  ?  140 ASP A CB    1 
ATOM   1108 C CG    . ASP A 1 140 ? 9.376   38.542  76.170 1.00 41.44 ?  140 ASP A CG    1 
ATOM   1109 O OD1   . ASP A 1 140 ? 8.380   37.796  76.067 1.00 46.31 ?  140 ASP A OD1   1 
ATOM   1110 O OD2   . ASP A 1 140 ? 9.262   39.759  76.459 1.00 42.02 -1 140 ASP A OD2   1 
ATOM   1111 N N     . THR A 1 141 ? 12.877  35.318  77.615 1.00 13.06 ?  141 THR A N     1 
ATOM   1112 C CA    . THR A 1 141 ? 13.660  34.115  77.351 1.00 16.56 ?  141 THR A CA    1 
ATOM   1113 C C     . THR A 1 141 ? 13.558  33.199  78.573 1.00 2.14  ?  141 THR A C     1 
ATOM   1114 O O     . THR A 1 141 ? 12.949  33.554  79.585 1.00 17.53 ?  141 THR A O     1 
ATOM   1115 C CB    . THR A 1 141 ? 15.113  34.508  77.037 1.00 13.75 ?  141 THR A CB    1 
ATOM   1116 O OG1   . THR A 1 141 ? 15.751  33.504  76.227 1.00 3.44  ?  141 THR A OG1   1 
ATOM   1117 C CG2   . THR A 1 141 ? 15.886  34.706  78.324 1.00 9.65  ?  141 THR A CG2   1 
ATOM   1118 N N     . TYR A 1 142 ? 14.233  32.056  78.536 1.00 19.88 ?  142 TYR A N     1 
ATOM   1119 C CA    . TYR A 1 142 ? 14.192  31.107  79.642 1.00 5.80  ?  142 TYR A CA    1 
ATOM   1120 C C     . TYR A 1 142 ? 15.571  30.993  80.266 1.00 15.35 ?  142 TYR A C     1 
ATOM   1121 O O     . TYR A 1 142 ? 16.588  31.106  79.570 1.00 13.24 ?  142 TYR A O     1 
ATOM   1122 C CB    . TYR A 1 142 ? 13.691  29.728  79.192 1.00 4.11  ?  142 TYR A CB    1 
ATOM   1123 C CG    . TYR A 1 142 ? 12.170  29.684  79.185 1.00 12.01 ?  142 TYR A CG    1 
ATOM   1124 C CD1   . TYR A 1 142 ? 11.458  30.286  78.175 1.00 1.69  ?  142 TYR A CD1   1 
ATOM   1125 C CD2   . TYR A 1 142 ? 11.465  29.096  80.218 1.00 1.60  ?  142 TYR A CD2   1 
ATOM   1126 C CE1   . TYR A 1 142 ? 10.112  30.285  78.169 1.00 15.45 ?  142 TYR A CE1   1 
ATOM   1127 C CE2   . TYR A 1 142 ? 10.101  29.099  80.226 1.00 8.19  ?  142 TYR A CE2   1 
ATOM   1128 C CZ    . TYR A 1 142 ? 9.418   29.694  79.189 1.00 18.49 ?  142 TYR A CZ    1 
ATOM   1129 O OH    . TYR A 1 142 ? 8.031   29.717  79.149 1.00 19.26 ?  142 TYR A OH    1 
ATOM   1130 N N     . VAL A 1 143 ? 15.604  30.839  81.590 1.00 9.13  ?  143 VAL A N     1 
ATOM   1131 C CA    . VAL A 1 143 ? 16.844  30.546  82.292 1.00 2.24  ?  143 VAL A CA    1 
ATOM   1132 C C     . VAL A 1 143 ? 16.557  29.422  83.268 1.00 5.38  ?  143 VAL A C     1 
ATOM   1133 O O     . VAL A 1 143 ? 15.432  29.268  83.755 1.00 10.47 ?  143 VAL A O     1 
ATOM   1134 C CB    . VAL A 1 143 ? 17.475  31.765  83.030 1.00 4.57  ?  143 VAL A CB    1 
ATOM   1135 C CG1   . VAL A 1 143 ? 17.561  32.955  82.124 1.00 2.14  ?  143 VAL A CG1   1 
ATOM   1136 C CG2   . VAL A 1 143 ? 16.764  32.087  84.335 1.00 2.59  ?  143 VAL A CG2   1 
ATOM   1137 N N     . ILE A 1 144 ? 17.602  28.667  83.584 1.00 17.90 ?  144 ILE A N     1 
ATOM   1138 C CA    . ILE A 1 144 ? 17.493  27.537  84.497 1.00 18.38 ?  144 ILE A CA    1 
ATOM   1139 C C     . ILE A 1 144 ? 17.489  28.041  85.933 1.00 28.61 ?  144 ILE A C     1 
ATOM   1140 O O     . ILE A 1 144 ? 18.252  28.945  86.310 1.00 31.09 ?  144 ILE A O     1 
ATOM   1141 C CB    . ILE A 1 144 ? 18.649  26.544  84.268 1.00 5.72  ?  144 ILE A CB    1 
ATOM   1142 C CG1   . ILE A 1 144 ? 18.686  26.077  82.798 1.00 4.22  ?  144 ILE A CG1   1 
ATOM   1143 C CG2   . ILE A 1 144 ? 18.545  25.418  85.265 1.00 1.89  ?  144 ILE A CG2   1 
ATOM   1144 C CD1   . ILE A 1 144 ? 19.949  25.380  82.373 1.00 4.57  ?  144 ILE A CD1   1 
ATOM   1145 N N     . ASP A 1 145 ? 16.639  27.431  86.754 1.00 27.15 ?  145 ASP A N     1 
ATOM   1146 C CA    . ASP A 1 145 ? 16.606  27.700  88.185 1.00 11.21 ?  145 ASP A CA    1 
ATOM   1147 C C     . ASP A 1 145 ? 17.626  26.771  88.844 1.00 23.25 ?  145 ASP A C     1 
ATOM   1148 O O     . ASP A 1 145 ? 17.315  25.697  89.357 1.00 39.88 ?  145 ASP A O     1 
ATOM   1149 C CB    . ASP A 1 145 ? 15.196  27.494  88.701 1.00 1.36  ?  145 ASP A CB    1 
ATOM   1150 C CG    . ASP A 1 145 ? 14.979  28.073  90.069 1.00 14.51 ?  145 ASP A CG    1 
ATOM   1151 O OD1   . ASP A 1 145 ? 15.954  28.197  90.830 1.00 12.51 ?  145 ASP A OD1   1 
ATOM   1152 O OD2   . ASP A 1 145 ? 13.806  28.338  90.417 1.00 11.16 -1 145 ASP A OD2   1 
ATOM   1153 N N     . PHE A 1 146 ? 18.880  27.222  88.822 1.00 29.55 ?  146 PHE A N     1 
ATOM   1154 C CA    . PHE A 1 146 ? 19.999  26.428  89.316 1.00 20.40 ?  146 PHE A CA    1 
ATOM   1155 C C     . PHE A 1 146 ? 19.915  26.210  90.817 1.00 23.44 ?  146 PHE A C     1 
ATOM   1156 O O     . PHE A 1 146 ? 20.447  25.216  91.329 1.00 32.82 ?  146 PHE A O     1 
ATOM   1157 C CB    . PHE A 1 146 ? 21.316  27.102  88.930 1.00 16.09 ?  146 PHE A CB    1 
ATOM   1158 C CG    . PHE A 1 146 ? 21.800  26.733  87.548 1.00 17.47 ?  146 PHE A CG    1 
ATOM   1159 C CD1   . PHE A 1 146 ? 22.549  25.583  87.347 1.00 6.69  ?  146 PHE A CD1   1 
ATOM   1160 C CD2   . PHE A 1 146 ? 21.513  27.529  86.457 1.00 18.53 ?  146 PHE A CD2   1 
ATOM   1161 C CE1   . PHE A 1 146 ? 22.989  25.240  86.097 1.00 6.89  ?  146 PHE A CE1   1 
ATOM   1162 C CE2   . PHE A 1 146 ? 21.970  27.174  85.187 1.00 22.19 ?  146 PHE A CE2   1 
ATOM   1163 C CZ    . PHE A 1 146 ? 22.702  26.037  85.017 1.00 9.49  ?  146 PHE A CZ    1 
ATOM   1164 N N     . LYS A 1 147 ? 19.304  27.150  91.539 1.00 11.24 ?  147 LYS A N     1 
ATOM   1165 C CA    . LYS A 1 147 ? 19.030  26.943  92.956 1.00 12.53 ?  147 LYS A CA    1 
ATOM   1166 C C     . LYS A 1 147 ? 17.981  25.848  93.149 1.00 15.28 ?  147 LYS A C     1 
ATOM   1167 O O     . LYS A 1 147 ? 18.078  25.042  94.082 1.00 16.15 ?  147 LYS A O     1 
ATOM   1168 C CB    . LYS A 1 147 ? 18.581  28.256  93.608 1.00 19.34 ?  147 LYS A CB    1 
ATOM   1169 C CG    . LYS A 1 147 ? 18.128  28.072  95.039 1.00 22.91 ?  147 LYS A CG    1 
ATOM   1170 C CD    . LYS A 1 147 ? 17.131  29.114  95.496 1.00 25.60 ?  147 LYS A CD    1 
ATOM   1171 C CE    . LYS A 1 147 ? 16.396  28.620  96.748 1.00 37.58 ?  147 LYS A CE    1 
ATOM   1172 N NZ    . LYS A 1 147 ? 15.262  29.493  97.185 1.00 38.82 1  147 LYS A NZ    1 
ATOM   1173 N N     . HIS A 1 148 ? 16.923  25.872  92.335 1.00 25.16 ?  148 HIS A N     1 
ATOM   1174 C CA    . HIS A 1 148 ? 15.929  24.798  92.338 1.00 14.03 ?  148 HIS A CA    1 
ATOM   1175 C C     . HIS A 1 148 ? 16.520  23.503  91.796 1.00 4.70  ?  148 HIS A C     1 
ATOM   1176 O O     . HIS A 1 148 ? 16.192  22.413  92.279 1.00 13.70 ?  148 HIS A O     1 
ATOM   1177 C CB    . HIS A 1 148 ? 14.707  25.221  91.514 1.00 1.35  ?  148 HIS A CB    1 
ATOM   1178 C CG    . HIS A 1 148 ? 13.606  24.213  91.464 1.00 14.16 ?  148 HIS A CG    1 
ATOM   1179 N ND1   . HIS A 1 148 ? 12.734  24.008  92.511 1.00 19.73 ?  148 HIS A ND1   1 
ATOM   1180 C CD2   . HIS A 1 148 ? 13.216  23.370  90.477 1.00 16.90 ?  148 HIS A CD2   1 
ATOM   1181 C CE1   . HIS A 1 148 ? 11.859  23.076  92.175 1.00 29.80 ?  148 HIS A CE1   1 
ATOM   1182 N NE2   . HIS A 1 148 ? 12.132  22.670  90.947 1.00 21.84 ?  148 HIS A NE2   1 
ATOM   1183 N N     . LEU A 1 149 ? 17.349  23.598  90.757 1.00 6.93  ?  149 LEU A N     1 
ATOM   1184 C CA    . LEU A 1 149 ? 17.982  22.403  90.198 1.00 19.28 ?  149 LEU A CA    1 
ATOM   1185 C C     . LEU A 1 149 ? 18.879  21.722  91.217 1.00 9.68  ?  149 LEU A C     1 
ATOM   1186 O O     . LEU A 1 149 ? 18.853  20.497  91.356 1.00 19.08 ?  149 LEU A O     1 
ATOM   1187 C CB    . LEU A 1 149 ? 18.779  22.758  88.952 1.00 2.40  ?  149 LEU A CB    1 
ATOM   1188 C CG    . LEU A 1 149 ? 19.526  21.684  88.198 1.00 2.00  ?  149 LEU A CG    1 
ATOM   1189 C CD1   . LEU A 1 149 ? 18.593  20.492  87.791 1.00 1.34  ?  149 LEU A CD1   1 
ATOM   1190 C CD2   . LEU A 1 149 ? 20.058  22.420  86.993 1.00 1.36  ?  149 LEU A CD2   1 
ATOM   1191 N N     . GLU A 1 150 ? 19.672  22.501  91.943 1.00 16.55 ?  150 GLU A N     1 
ATOM   1192 C CA    . GLU A 1 150 ? 20.549  21.901  92.935 1.00 24.89 ?  150 GLU A CA    1 
ATOM   1193 C C     . GLU A 1 150 ? 19.767  21.296  94.097 1.00 14.97 ?  150 GLU A C     1 
ATOM   1194 O O     . GLU A 1 150 ? 20.197  20.280  94.650 1.00 29.88 ?  150 GLU A O     1 
ATOM   1195 C CB    . GLU A 1 150 ? 21.557  22.956  93.418 1.00 27.82 ?  150 GLU A CB    1 
ATOM   1196 C CG    . GLU A 1 150 ? 22.538  22.503  94.498 1.00 28.33 ?  150 GLU A CG    1 
ATOM   1197 C CD    . GLU A 1 150 ? 23.739  23.442  94.641 1.00 26.54 ?  150 GLU A CD    1 
ATOM   1198 O OE1   . GLU A 1 150 ? 24.874  22.955  94.853 1.00 23.68 ?  150 GLU A OE1   1 
ATOM   1199 O OE2   . GLU A 1 150 ? 23.552  24.667  94.533 1.00 31.27 -1 150 GLU A OE2   1 
ATOM   1200 N N     . LYS A 1 151 ? 18.580  21.824  94.412 1.00 1.35  ?  151 LYS A N     1 
ATOM   1201 C CA    . LYS A 1 151 ? 17.763  21.229  95.472 1.00 8.54  ?  151 LYS A CA    1 
ATOM   1202 C C     . LYS A 1 151 ? 17.300  19.815  95.116 1.00 21.43 ?  151 LYS A C     1 
ATOM   1203 O O     . LYS A 1 151 ? 17.332  18.908  95.960 1.00 14.95 ?  151 LYS A O     1 
ATOM   1204 C CB    . LYS A 1 151 ? 16.529  22.088  95.741 1.00 1.38  ?  151 LYS A CB    1 
ATOM   1205 C CG    . LYS A 1 151 ? 16.701  23.167  96.795 1.00 24.96 ?  151 LYS A CG    1 
ATOM   1206 C CD    . LYS A 1 151 ? 15.422  24.004  96.947 1.00 7.13  ?  151 LYS A CD    1 
ATOM   1207 C CE    . LYS A 1 151 ? 15.643  25.132  97.943 1.00 26.32 ?  151 LYS A CE    1 
ATOM   1208 N NZ    . LYS A 1 151 ? 14.599  26.185  97.838 1.00 33.09 1  151 LYS A NZ    1 
ATOM   1209 N N     . GLN A 1 152 ? 16.935  19.591  93.853 1.00 22.32 ?  152 GLN A N     1 
ATOM   1210 C CA    . GLN A 1 152 ? 16.416  18.288  93.467 1.00 20.94 ?  152 GLN A CA    1 
ATOM   1211 C C     . GLN A 1 152 ? 17.525  17.246  93.409 1.00 20.26 ?  152 GLN A C     1 
ATOM   1212 O O     . GLN A 1 152 ? 17.298  16.084  93.755 1.00 17.55 ?  152 GLN A O     1 
ATOM   1213 C CB    . GLN A 1 152 ? 15.687  18.394  92.129 1.00 9.13  ?  152 GLN A CB    1 
ATOM   1214 C CG    . GLN A 1 152 ? 14.737  19.592  92.036 1.00 10.14 ?  152 GLN A CG    1 
ATOM   1215 C CD    . GLN A 1 152 ? 13.419  19.396  92.756 1.00 9.49  ?  152 GLN A CD    1 
ATOM   1216 O OE1   . GLN A 1 152 ? 12.408  19.045  92.145 1.00 1.42  ?  152 GLN A OE1   1 
ATOM   1217 N NE2   . GLN A 1 152 ? 13.437  19.578  94.069 1.00 2.50  ?  152 GLN A NE2   1 
ATOM   1218 N N     . PHE A 1 153 ? 18.734  17.656  93.021 1.00 22.60 ?  153 PHE A N     1 
ATOM   1219 C CA    . PHE A 1 153 ? 19.868  16.740  92.988 1.00 1.35  ?  153 PHE A CA    1 
ATOM   1220 C C     . PHE A 1 153 ? 20.195  16.194  94.365 1.00 1.38  ?  153 PHE A C     1 
ATOM   1221 O O     . PHE A 1 153 ? 20.714  15.082  94.475 1.00 20.86 ?  153 PHE A O     1 
ATOM   1222 C CB    . PHE A 1 153 ? 21.090  17.453  92.433 1.00 9.64  ?  153 PHE A CB    1 
ATOM   1223 C CG    . PHE A 1 153 ? 21.150  17.494  90.944 1.00 1.34  ?  153 PHE A CG    1 
ATOM   1224 C CD1   . PHE A 1 153 ? 20.203  16.838  90.186 1.00 14.71 ?  153 PHE A CD1   1 
ATOM   1225 C CD2   . PHE A 1 153 ? 22.163  18.169  90.307 1.00 1.35  ?  153 PHE A CD2   1 
ATOM   1226 C CE1   . PHE A 1 153 ? 20.256  16.868  88.820 1.00 14.15 ?  153 PHE A CE1   1 
ATOM   1227 C CE2   . PHE A 1 153 ? 22.227  18.200  88.937 1.00 1.39  ?  153 PHE A CE2   1 
ATOM   1228 C CZ    . PHE A 1 153 ? 21.276  17.552  88.195 1.00 13.00 ?  153 PHE A CZ    1 
ATOM   1229 N N     . GLN A 1 154 ? 19.911  16.954  95.421 1.00 1.39  ?  154 GLN A N     1 
ATOM   1230 C CA    . GLN A 1 154 ? 20.188  16.495  96.776 1.00 5.40  ?  154 GLN A CA    1 
ATOM   1231 C C     . GLN A 1 154 ? 19.304  15.326  97.209 1.00 24.53 ?  154 GLN A C     1 
ATOM   1232 O O     . GLN A 1 154 ? 19.600  14.703  98.237 1.00 34.26 ?  154 GLN A O     1 
ATOM   1233 C CB    . GLN A 1 154 ? 20.000  17.649  97.771 1.00 6.09  ?  154 GLN A CB    1 
ATOM   1234 C CG    . GLN A 1 154 ? 20.918  18.861  97.598 1.00 6.55  ?  154 GLN A CG    1 
ATOM   1235 C CD    . GLN A 1 154 ? 20.694  19.915  98.683 1.00 5.53  ?  154 GLN A CD    1 
ATOM   1236 O OE1   . GLN A 1 154 ? 19.618  20.015  99.259 1.00 16.10 ?  154 GLN A OE1   1 
ATOM   1237 N NE2   . GLN A 1 154 ? 21.725  20.676  98.982 1.00 16.08 ?  154 GLN A NE2   1 
ATOM   1238 N N     . GLN A 1 155 ? 18.262  14.984  96.443 1.00 34.94 ?  155 GLN A N     1 
ATOM   1239 C CA    . GLN A 1 155 ? 17.347  13.895  96.794 1.00 24.59 ?  155 GLN A CA    1 
ATOM   1240 C C     . GLN A 1 155 ? 17.738  12.555  96.187 1.00 24.37 ?  155 GLN A C     1 
ATOM   1241 O O     . GLN A 1 155 ? 16.997  11.583  96.357 1.00 28.71 ?  155 GLN A O     1 
ATOM   1242 C CB    . GLN A 1 155 ? 15.906  14.218  96.371 1.00 31.98 ?  155 GLN A CB    1 
ATOM   1243 C CG    . GLN A 1 155 ? 15.535  15.702  96.342 1.00 33.43 ?  155 GLN A CG    1 
ATOM   1244 C CD    . GLN A 1 155 ? 14.196  15.973  95.651 1.00 26.80 ?  155 GLN A CD    1 
ATOM   1245 O OE1   . GLN A 1 155 ? 14.081  15.888  94.429 1.00 28.25 ?  155 GLN A OE1   1 
ATOM   1246 N NE2   . GLN A 1 155 ? 13.180  16.299  96.440 1.00 21.47 ?  155 GLN A NE2   1 
ATOM   1247 N N     . GLY A 1 156 ? 18.859  12.496  95.476 1.00 17.58 ?  156 GLY A N     1 
ATOM   1248 C CA    . GLY A 1 156 ? 19.412  11.276  94.944 1.00 1.45  ?  156 GLY A CA    1 
ATOM   1249 C C     . GLY A 1 156 ? 19.218  11.054  93.465 1.00 5.73  ?  156 GLY A C     1 
ATOM   1250 O O     . GLY A 1 156 ? 19.405  9.920   93.006 1.00 7.72  ?  156 GLY A O     1 
ATOM   1251 N N     . ILE A 1 157 ? 19.030  12.122  92.681 1.00 13.22 ?  157 ILE A N     1 
ATOM   1252 C CA    . ILE A 1 157 ? 18.726  11.968  91.263 1.00 1.36  ?  157 ILE A CA    1 
ATOM   1253 C C     . ILE A 1 157 ? 19.830  11.192  90.574 1.00 30.87 ?  157 ILE A C     1 
ATOM   1254 O O     . ILE A 1 157 ? 21.011  11.553  90.642 1.00 40.43 ?  157 ILE A O     1 
ATOM   1255 C CB    . ILE A 1 157 ? 18.542  13.335  90.594 1.00 1.35  ?  157 ILE A CB    1 
ATOM   1256 C CG1   . ILE A 1 157 ? 17.424  14.112  91.275 1.00 6.85  ?  157 ILE A CG1   1 
ATOM   1257 C CG2   . ILE A 1 157 ? 18.244  13.155  89.126 1.00 1.33  ?  157 ILE A CG2   1 
ATOM   1258 C CD1   . ILE A 1 157 ? 16.052  13.754  90.814 1.00 16.34 ?  157 ILE A CD1   1 
ATOM   1259 N N     . LYS A 1 158 ? 19.436  10.131  89.876 1.00 42.25 ?  158 LYS A N     1 
ATOM   1260 C CA    . LYS A 1 158 ? 20.357  9.267   89.155 1.00 38.51 ?  158 LYS A CA    1 
ATOM   1261 C C     . LYS A 1 158 ? 20.550  9.720   87.724 1.00 29.18 ?  158 LYS A C     1 
ATOM   1262 O O     . LYS A 1 158 ? 21.658  9.581   87.190 1.00 41.44 ?  158 LYS A O     1 
ATOM   1263 C CB    . LYS A 1 158 ? 19.834  7.825   89.122 1.00 37.94 ?  158 LYS A CB    1 
ATOM   1264 C CG    . LYS A 1 158 ? 20.044  7.007   90.376 1.00 24.35 ?  158 LYS A CG    1 
ATOM   1265 C CD    . LYS A 1 158 ? 21.226  6.074   90.231 1.00 29.98 ?  158 LYS A CD    1 
ATOM   1266 C CE    . LYS A 1 158 ? 20.986  5.012   89.188 1.00 23.90 ?  158 LYS A CE    1 
ATOM   1267 N NZ    . LYS A 1 158 ? 21.790  3.799   89.461 1.00 27.47 1  158 LYS A NZ    1 
ATOM   1268 N N     . LEU A 1 159 ? 19.507  10.271  87.102 1.00 1.33  ?  159 LEU A N     1 
ATOM   1269 C CA    . LEU A 1 159 ? 19.534  10.620  85.688 1.00 1.73  ?  159 LEU A CA    1 
ATOM   1270 C C     . LEU A 1 159 ? 18.920  12.004  85.450 1.00 22.35 ?  159 LEU A C     1 
ATOM   1271 O O     . LEU A 1 159 ? 18.114  12.495  86.248 1.00 8.66  ?  159 LEU A O     1 
ATOM   1272 C CB    . LEU A 1 159 ? 18.801  9.539   84.869 1.00 1.33  ?  159 LEU A CB    1 
ATOM   1273 C CG    . LEU A 1 159 ? 18.877  9.668   83.351 1.00 13.06 ?  159 LEU A CG    1 
ATOM   1274 C CD1   . LEU A 1 159 ? 20.300  9.442   82.820 1.00 4.83  ?  159 LEU A CD1   1 
ATOM   1275 C CD2   . LEU A 1 159 ? 17.890  8.738   82.691 1.00 1.39  ?  159 LEU A CD2   1 
ATOM   1276 N N     . MET A 1 160 ? 19.379  12.673  84.391 1.00 18.79 ?  160 MET A N     1 
ATOM   1277 C CA    . MET A 1 160 ? 18.744  13.894  83.910 1.00 21.05 ?  160 MET A CA    1 
ATOM   1278 C C     . MET A 1 160 ? 18.630  13.832  82.393 1.00 23.30 ?  160 MET A C     1 
ATOM   1279 O O     . MET A 1 160 ? 19.620  13.537  81.715 1.00 21.38 ?  160 MET A O     1 
ATOM   1280 C CB    . MET A 1 160 ? 19.528  15.143  84.327 1.00 13.46 ?  160 MET A CB    1 
ATOM   1281 C CG    . MET A 1 160 ? 18.903  16.408  83.757 1.00 25.72 ?  160 MET A CG    1 
ATOM   1282 S SD    . MET A 1 160 ? 19.578  18.000  84.254 1.00 17.21 ?  160 MET A SD    1 
ATOM   1283 C CE    . MET A 1 160 ? 21.277  17.826  83.784 1.00 1.70  ?  160 MET A CE    1 
ATOM   1284 N N     . LEU A 1 161 ? 17.444  14.134  81.850 1.00 9.63  ?  161 LEU A N     1 
ATOM   1285 C CA    . LEU A 1 161 ? 17.281  14.227  80.399 1.00 8.96  ?  161 LEU A CA    1 
ATOM   1286 C C     . LEU A 1 161 ? 17.280  15.709  80.036 1.00 13.68 ?  161 LEU A C     1 
ATOM   1287 O O     . LEU A 1 161 ? 16.269  16.395  80.190 1.00 31.47 ?  161 LEU A O     1 
ATOM   1288 C CB    . LEU A 1 161 ? 16.008  13.527  79.939 1.00 16.72 ?  161 LEU A CB    1 
ATOM   1289 C CG    . LEU A 1 161 ? 15.789  12.036  80.235 1.00 10.17 ?  161 LEU A CG    1 
ATOM   1290 C CD1   . LEU A 1 161 ? 14.326  11.787  80.470 1.00 17.07 ?  161 LEU A CD1   1 
ATOM   1291 C CD2   . LEU A 1 161 ? 16.255  11.157  79.096 1.00 5.56  ?  161 LEU A CD2   1 
ATOM   1292 N N     . LEU A 1 162 ? 18.371  16.125  79.424 1.00 1.74  ?  162 LEU A N     1 
ATOM   1293 C CA    . LEU A 1 162 ? 18.558  17.519  79.041 1.00 9.05  ?  162 LEU A CA    1 
ATOM   1294 C C     . LEU A 1 162 ? 18.242  17.731  77.567 1.00 27.41 ?  162 LEU A C     1 
ATOM   1295 O O     . LEU A 1 162 ? 18.580  16.869  76.758 1.00 31.51 ?  162 LEU A O     1 
ATOM   1296 C CB    . LEU A 1 162 ? 20.009  17.890  79.374 1.00 11.97 ?  162 LEU A CB    1 
ATOM   1297 C CG    . LEU A 1 162 ? 20.507  19.288  79.009 1.00 16.33 ?  162 LEU A CG    1 
ATOM   1298 C CD1   . LEU A 1 162 ? 19.742  20.362  79.764 1.00 35.31 ?  162 LEU A CD1   1 
ATOM   1299 C CD2   . LEU A 1 162 ? 21.986  19.413  79.308 1.00 21.19 ?  162 LEU A CD2   1 
ATOM   1300 N N     . CYS A 1 163 ? 17.565  18.828  77.253 1.00 20.16 ?  163 CYS A N     1 
ATOM   1301 C CA    . CYS A 1 163 ? 17.336  19.229  75.865 1.00 13.70 ?  163 CYS A CA    1 
ATOM   1302 C C     . CYS A 1 163 ? 18.238  20.425  75.538 1.00 22.13 ?  163 CYS A C     1 
ATOM   1303 O O     . CYS A 1 163 ? 18.207  21.457  76.224 1.00 2.43  ?  163 CYS A O     1 
ATOM   1304 C CB    . CYS A 1 163 ? 15.866  19.582  75.605 1.00 2.07  ?  163 CYS A CB    1 
ATOM   1305 S SG    . CYS A 1 163 ? 15.284  19.433  73.867 1.00 18.01 ?  163 CYS A SG    1 
ATOM   1306 N N     . SER A 1 164 ? 19.069  20.250  74.533 1.00 15.80 ?  164 SER A N     1 
ATOM   1307 C CA    . SER A 1 164 ? 19.962  21.283  74.057 1.00 28.49 ?  164 SER A CA    1 
ATOM   1308 C C     . SER A 1 164 ? 20.094  21.163  72.545 1.00 23.62 ?  164 SER A C     1 
ATOM   1309 O O     . SER A 1 164 ? 20.681  20.191  72.044 1.00 11.54 ?  164 SER A O     1 
ATOM   1310 C CB    . SER A 1 164 ? 21.323  21.193  74.758 1.00 17.18 ?  164 SER A CB    1 
ATOM   1311 O OG    . SER A 1 164 ? 22.037  22.416  74.650 1.00 6.79  ?  164 SER A OG    1 
ATOM   1312 N N     . PRO A 1 165 ? 19.494  22.094  71.779 1.00 10.53 ?  165 PRO A N     1 
ATOM   1313 C CA    . PRO A 1 165 ? 18.648  23.219  72.194 1.00 4.50  ?  165 PRO A CA    1 
ATOM   1314 C C     . PRO A 1 165 ? 17.261  22.741  72.655 1.00 17.01 ?  165 PRO A C     1 
ATOM   1315 O O     . PRO A 1 165 ? 16.904  21.606  72.396 1.00 20.54 ?  165 PRO A O     1 
ATOM   1316 C CB    . PRO A 1 165 ? 18.576  24.105  70.942 1.00 12.20 ?  165 PRO A CB    1 
ATOM   1317 C CG    . PRO A 1 165 ? 18.894  23.236  69.838 1.00 18.75 ?  165 PRO A CG    1 
ATOM   1318 C CD    . PRO A 1 165 ? 19.794  22.136  70.345 1.00 20.31 ?  165 PRO A CD    1 
ATOM   1319 N N     . HIS A 1 166 ? 16.502  23.604  73.326 1.00 17.27 ?  166 HIS A N     1 
ATOM   1320 C CA    . HIS A 1 166 ? 15.340  23.190  74.104 1.00 25.59 ?  166 HIS A CA    1 
ATOM   1321 C C     . HIS A 1 166 ? 14.022  23.370  73.356 1.00 21.32 ?  166 HIS A C     1 
ATOM   1322 O O     . HIS A 1 166 ? 13.505  24.480  73.241 1.00 25.48 ?  166 HIS A O     1 
ATOM   1323 C CB    . HIS A 1 166 ? 15.312  23.970  75.409 1.00 14.44 ?  166 HIS A CB    1 
ATOM   1324 C CG    . HIS A 1 166 ? 14.292  23.478  76.378 1.00 6.75  ?  166 HIS A CG    1 
ATOM   1325 N ND1   . HIS A 1 166 ? 14.628  22.749  77.501 1.00 6.38  ?  166 HIS A ND1   1 
ATOM   1326 C CD2   . HIS A 1 166 ? 12.949  23.643  76.417 1.00 10.33 ?  166 HIS A CD2   1 
ATOM   1327 C CE1   . HIS A 1 166 ? 13.529  22.487  78.189 1.00 9.74  ?  166 HIS A CE1   1 
ATOM   1328 N NE2   . HIS A 1 166 ? 12.498  23.014  77.551 1.00 9.02  ?  166 HIS A NE2   1 
ATOM   1329 N N     . ASN A 1 167 ? 13.449  22.277  72.942 1.00 30.86 ?  167 ASN A N     1 
ATOM   1330 C CA    . ASN A 1 167 ? 12.100  22.232  72.410 1.00 24.70 ?  167 ASN A CA    1 
ATOM   1331 C C     . ASN A 1 167 ? 11.115  22.269  73.575 1.00 26.17 ?  167 ASN A C     1 
ATOM   1332 O O     . ASN A 1 167 ? 11.218  21.442  74.484 1.00 41.70 ?  167 ASN A O     1 
ATOM   1333 C CB    . ASN A 1 167 ? 11.970  20.948  71.586 1.00 19.50 ?  167 ASN A CB    1 
ATOM   1334 C CG    . ASN A 1 167 ? 10.580  20.683  71.057 1.00 16.12 ?  167 ASN A CG    1 
ATOM   1335 O OD1   . ASN A 1 167 ? 9.635   21.414  71.305 1.00 23.81 ?  167 ASN A OD1   1 
ATOM   1336 N ND2   . ASN A 1 167 ? 10.456  19.600  70.316 1.00 15.23 ?  167 ASN A ND2   1 
ATOM   1337 N N     . PRO A 1 168 ? 10.126  23.185  73.574 1.00 10.07 ?  168 PRO A N     1 
ATOM   1338 C CA    . PRO A 1 168 ? 9.641   24.049  72.496 1.00 2.07  ?  168 PRO A CA    1 
ATOM   1339 C C     . PRO A 1 168 ? 10.127  25.497  72.417 1.00 9.09  ?  168 PRO A C     1 
ATOM   1340 O O     . PRO A 1 168 ? 9.852   26.171  71.411 1.00 2.56  ?  168 PRO A O     1 
ATOM   1341 C CB    . PRO A 1 168 ? 8.137   24.038  72.756 1.00 19.84 ?  168 PRO A CB    1 
ATOM   1342 C CG    . PRO A 1 168 ? 8.019   23.936  74.226 1.00 19.31 ?  168 PRO A CG    1 
ATOM   1343 C CD    . PRO A 1 168 ? 9.256   23.267  74.759 1.00 1.76  ?  168 PRO A CD    1 
ATOM   1344 N N     . ILE A 1 169 ? 10.852  25.967  73.435 1.00 19.23 ?  169 ILE A N     1 
ATOM   1345 C CA    . ILE A 1 169 ? 11.177  27.393  73.541 1.00 28.12 ?  169 ILE A CA    1 
ATOM   1346 C C     . ILE A 1 169 ? 12.282  27.823  72.565 1.00 29.81 ?  169 ILE A C     1 
ATOM   1347 O O     . ILE A 1 169 ? 12.300  28.974  72.114 1.00 27.30 ?  169 ILE A O     1 
ATOM   1348 C CB    . ILE A 1 169 ? 11.562  27.708  75.001 1.00 22.32 ?  169 ILE A CB    1 
ATOM   1349 C CG1   . ILE A 1 169 ? 12.933  27.099  75.321 1.00 11.33 ?  169 ILE A CG1   1 
ATOM   1350 C CG2   . ILE A 1 169 ? 10.469  27.211  75.960 1.00 17.25 ?  169 ILE A CG2   1 
ATOM   1351 C CD1   . ILE A 1 169 ? 13.246  26.910  76.773 1.00 17.60 ?  169 ILE A CD1   1 
ATOM   1352 N N     . GLY A 1 170 ? 13.197  26.919  72.206 1.00 29.66 ?  170 GLY A N     1 
ATOM   1353 C CA    . GLY A 1 170 ? 14.301  27.221  71.300 1.00 14.43 ?  170 GLY A CA    1 
ATOM   1354 C C     . GLY A 1 170 ? 15.587  27.717  71.935 1.00 11.59 ?  170 GLY A C     1 
ATOM   1355 O O     . GLY A 1 170 ? 16.448  28.245  71.223 1.00 3.83  ?  170 GLY A O     1 
ATOM   1356 N N     . ARG A 1 171 ? 15.792  27.485  73.229 1.00 6.59  ?  171 ARG A N     1 
ATOM   1357 C CA    . ARG A 1 171 ? 16.991  27.981  73.880 1.00 3.22  ?  171 ARG A CA    1 
ATOM   1358 C C     . ARG A 1 171 ? 18.203  27.190  73.414 1.00 16.32 ?  171 ARG A C     1 
ATOM   1359 O O     . ARG A 1 171 ? 18.186  25.957  73.386 1.00 32.78 ?  171 ARG A O     1 
ATOM   1360 C CB    . ARG A 1 171 ? 16.865  27.875  75.399 1.00 12.79 ?  171 ARG A CB    1 
ATOM   1361 C CG    . ARG A 1 171 ? 16.426  29.132  76.100 1.00 25.14 ?  171 ARG A CG    1 
ATOM   1362 C CD    . ARG A 1 171 ? 17.164  30.385  75.644 1.00 44.16 ?  171 ARG A CD    1 
ATOM   1363 N NE    . ARG A 1 171 ? 18.624  30.292  75.607 1.00 3.33  ?  171 ARG A NE    1 
ATOM   1364 C CZ    . ARG A 1 171 ? 19.374  30.439  76.682 1.00 9.88  ?  171 ARG A CZ    1 
ATOM   1365 N NH1   . ARG A 1 171 ? 18.798  30.657  77.842 1.00 2.92  1  171 ARG A NH1   1 
ATOM   1366 N NH2   . ARG A 1 171 ? 20.698  30.361  76.606 1.00 33.62 ?  171 ARG A NH2   1 
ATOM   1367 N N     . VAL A 1 172 ? 19.245  27.906  73.040 1.00 23.84 ?  172 VAL A N     1 
ATOM   1368 C CA    . VAL A 1 172 ? 20.558  27.357  72.749 1.00 4.12  ?  172 VAL A CA    1 
ATOM   1369 C C     . VAL A 1 172 ? 21.437  27.729  73.932 1.00 21.13 ?  172 VAL A C     1 
ATOM   1370 O O     . VAL A 1 172 ? 21.808  28.896  74.091 1.00 26.04 ?  172 VAL A O     1 
ATOM   1371 C CB    . VAL A 1 172 ? 21.113  27.920  71.444 1.00 4.55  ?  172 VAL A CB    1 
ATOM   1372 C CG1   . VAL A 1 172 ? 22.571  27.556  71.266 1.00 4.83  ?  172 VAL A CG1   1 
ATOM   1373 C CG2   . VAL A 1 172 ? 20.258  27.462  70.264 1.00 21.40 ?  172 VAL A CG2   1 
ATOM   1374 N N     . TRP A 1 173 ? 21.728  26.762  74.799 1.00 22.46 ?  173 TRP A N     1 
ATOM   1375 C CA    . TRP A 1 173 ? 22.444  27.073  76.029 1.00 23.91 ?  173 TRP A CA    1 
ATOM   1376 C C     . TRP A 1 173 ? 23.851  27.575  75.726 1.00 19.25 ?  173 TRP A C     1 
ATOM   1377 O O     . TRP A 1 173 ? 24.533  27.084  74.822 1.00 27.67 ?  173 TRP A O     1 
ATOM   1378 C CB    . TRP A 1 173 ? 22.471  25.847  76.943 1.00 29.30 ?  173 TRP A CB    1 
ATOM   1379 C CG    . TRP A 1 173 ? 21.086  25.263  77.103 1.00 36.20 ?  173 TRP A CG    1 
ATOM   1380 C CD1   . TRP A 1 173 ? 20.637  24.062  76.626 1.00 25.01 ?  173 TRP A CD1   1 
ATOM   1381 C CD2   . TRP A 1 173 ? 19.959  25.877  77.755 1.00 33.55 ?  173 TRP A CD2   1 
ATOM   1382 N NE1   . TRP A 1 173 ? 19.312  23.888  76.950 1.00 21.13 ?  173 TRP A NE1   1 
ATOM   1383 C CE2   . TRP A 1 173 ? 18.874  24.985  77.644 1.00 25.16 ?  173 TRP A CE2   1 
ATOM   1384 C CE3   . TRP A 1 173 ? 19.769  27.084  78.432 1.00 31.02 ?  173 TRP A CE3   1 
ATOM   1385 C CZ2   . TRP A 1 173 ? 17.622  25.268  78.178 1.00 30.85 ?  173 TRP A CZ2   1 
ATOM   1386 C CZ3   . TRP A 1 173 ? 18.523  27.358  78.961 1.00 36.72 ?  173 TRP A CZ3   1 
ATOM   1387 C CH2   . TRP A 1 173 ? 17.466  26.457  78.829 1.00 37.74 ?  173 TRP A CH2   1 
ATOM   1388 N N     . THR A 1 174 ? 24.262  28.600  76.459 1.00 30.51 ?  174 THR A N     1 
ATOM   1389 C CA    . THR A 1 174 ? 25.615  29.108  76.335 1.00 11.87 ?  174 THR A CA    1 
ATOM   1390 C C     . THR A 1 174 ? 26.594  28.128  76.957 1.00 13.38 ?  174 THR A C     1 
ATOM   1391 O O     . THR A 1 174 ? 26.223  27.234  77.725 1.00 22.94 ?  174 THR A O     1 
ATOM   1392 C CB    . THR A 1 174 ? 25.752  30.443  77.046 1.00 6.57  ?  174 THR A CB    1 
ATOM   1393 O OG1   . THR A 1 174 ? 25.514  30.235  78.442 1.00 9.01  ?  174 THR A OG1   1 
ATOM   1394 C CG2   . THR A 1 174 ? 24.776  31.449  76.504 1.00 4.40  ?  174 THR A CG2   1 
ATOM   1395 N N     . LYS A 1 175 ? 27.876  28.365  76.705 1.00 22.03 ?  175 LYS A N     1 
ATOM   1396 C CA    . LYS A 1 175 ? 28.868  27.518  77.346 1.00 14.60 ?  175 LYS A CA    1 
ATOM   1397 C C     . LYS A 1 175 ? 28.885  27.727  78.849 1.00 20.71 ?  175 LYS A C     1 
ATOM   1398 O O     . LYS A 1 175 ? 29.037  26.754  79.597 1.00 32.12 ?  175 LYS A O     1 
ATOM   1399 C CB    . LYS A 1 175 ? 30.244  27.759  76.748 1.00 26.13 ?  175 LYS A CB    1 
ATOM   1400 C CG    . LYS A 1 175 ? 31.328  26.870  77.326 1.00 18.21 ?  175 LYS A CG    1 
ATOM   1401 C CD    . LYS A 1 175 ? 32.555  26.987  76.465 1.00 10.14 ?  175 LYS A CD    1 
ATOM   1402 C CE    . LYS A 1 175 ? 33.789  26.393  77.122 1.00 18.64 ?  175 LYS A CE    1 
ATOM   1403 N NZ    . LYS A 1 175 ? 34.925  26.321  76.163 1.00 6.11  1  175 LYS A NZ    1 
ATOM   1404 N N     . GLU A 1 176 ? 28.640  28.952  79.319 1.00 19.35 ?  176 GLU A N     1 
ATOM   1405 C CA    . GLU A 1 176 ? 28.695  29.179  80.761 1.00 14.37 ?  176 GLU A CA    1 
ATOM   1406 C C     . GLU A 1 176 ? 27.627  28.372  81.474 1.00 17.06 ?  176 GLU A C     1 
ATOM   1407 O O     . GLU A 1 176 ? 27.885  27.766  82.518 1.00 22.41 ?  176 GLU A O     1 
ATOM   1408 C CB    . GLU A 1 176 ? 28.506  30.668  81.088 1.00 13.91 ?  176 GLU A CB    1 
ATOM   1409 C CG    . GLU A 1 176 ? 29.366  31.638  80.283 1.00 28.62 ?  176 GLU A CG    1 
ATOM   1410 C CD    . GLU A 1 176 ? 28.600  32.353  79.176 1.00 30.89 ?  176 GLU A CD    1 
ATOM   1411 O OE1   . GLU A 1 176 ? 27.565  32.969  79.486 1.00 18.98 ?  176 GLU A OE1   1 
ATOM   1412 O OE2   . GLU A 1 176 ? 29.043  32.316  78.005 1.00 27.70 -1 176 GLU A OE2   1 
ATOM   1413 N N     . GLU A 1 177 ? 26.437  28.303  80.881 1.00 24.80 ?  177 GLU A N     1 
ATOM   1414 C CA    . GLU A 1 177 ? 25.349  27.546  81.474 1.00 13.26 ?  177 GLU A CA    1 
ATOM   1415 C C     . GLU A 1 177 ? 25.693  26.059  81.530 1.00 31.53 ?  177 GLU A C     1 
ATOM   1416 O O     . GLU A 1 177 ? 25.590  25.421  82.588 1.00 32.04 ?  177 GLU A O     1 
ATOM   1417 C CB    . GLU A 1 177 ? 24.076  27.789  80.664 1.00 24.11 ?  177 GLU A CB    1 
ATOM   1418 C CG    . GLU A 1 177 ? 23.351  29.100  80.968 1.00 3.05  ?  177 GLU A CG    1 
ATOM   1419 C CD    . GLU A 1 177 ? 22.407  29.442  79.852 1.00 3.08  ?  177 GLU A CD    1 
ATOM   1420 O OE1   . GLU A 1 177 ? 22.804  29.288  78.685 1.00 12.43 ?  177 GLU A OE1   1 
ATOM   1421 O OE2   . GLU A 1 177 ? 21.245  29.793  80.133 1.00 12.83 -1 177 GLU A OE2   1 
ATOM   1422 N N     . LEU A 1 178 ? 26.119  25.486  80.396 1.00 26.71 ?  178 LEU A N     1 
ATOM   1423 C CA    . LEU A 1 178 ? 26.460  24.071  80.398 1.00 8.55  ?  178 LEU A CA    1 
ATOM   1424 C C     . LEU A 1 178 ? 27.654  23.812  81.303 1.00 20.51 ?  178 LEU A C     1 
ATOM   1425 O O     . LEU A 1 178 ? 27.685  22.798  82.005 1.00 35.14 ?  178 LEU A O     1 
ATOM   1426 C CB    . LEU A 1 178 ? 26.719  23.562  78.976 1.00 5.65  ?  178 LEU A CB    1 
ATOM   1427 C CG    . LEU A 1 178 ? 25.510  23.599  78.022 1.00 10.27 ?  178 LEU A CG    1 
ATOM   1428 C CD1   . LEU A 1 178 ? 25.797  24.176  76.684 1.00 3.87  ?  178 LEU A CD1   1 
ATOM   1429 C CD2   . LEU A 1 178 ? 24.876  22.227  77.869 1.00 20.53 ?  178 LEU A CD2   1 
ATOM   1430 N N     . ILE A 1 179 ? 28.630  24.731  81.338 1.00 9.78  ?  179 ILE A N     1 
ATOM   1431 C CA    . ILE A 1 179 ? 29.703  24.619  82.337 1.00 20.71 ?  179 ILE A CA    1 
ATOM   1432 C C     . ILE A 1 179 ? 29.118  24.604  83.740 1.00 26.40 ?  179 ILE A C     1 
ATOM   1433 O O     . ILE A 1 179 ? 29.538  23.830  84.607 1.00 40.10 ?  179 ILE A O     1 
ATOM   1434 C CB    . ILE A 1 179 ? 30.715  25.767  82.192 1.00 21.11 ?  179 ILE A CB    1 
ATOM   1435 C CG1   . ILE A 1 179 ? 31.640  25.538  81.003 1.00 10.20 ?  179 ILE A CG1   1 
ATOM   1436 C CG2   . ILE A 1 179 ? 31.519  25.945  83.473 1.00 10.36 ?  179 ILE A CG2   1 
ATOM   1437 C CD1   . ILE A 1 179 ? 32.615  24.421  81.198 1.00 20.32 ?  179 ILE A CD1   1 
ATOM   1438 N N     . LYS A 1 180 ? 28.168  25.492  83.995 1.00 35.11 ?  180 LYS A N     1 
ATOM   1439 C CA    . LYS A 1 180 ? 27.549  25.531  85.310 1.00 38.66 ?  180 LYS A CA    1 
ATOM   1440 C C     . LYS A 1 180 ? 26.657  24.319  85.552 1.00 29.85 ?  180 LYS A C     1 
ATOM   1441 O O     . LYS A 1 180 ? 26.600  23.815  86.680 1.00 48.78 ?  180 LYS A O     1 
ATOM   1442 C CB    . LYS A 1 180 ? 26.749  26.819  85.437 1.00 2.82  ?  180 LYS A CB    1 
ATOM   1443 C CG    . LYS A 1 180 ? 26.404  27.227  86.849 1.00 9.24  ?  180 LYS A CG    1 
ATOM   1444 C CD    . LYS A 1 180 ? 25.284  28.284  86.769 1.00 8.49  ?  180 LYS A CD    1 
ATOM   1445 C CE    . LYS A 1 180 ? 25.244  29.172  87.989 1.00 20.53 ?  180 LYS A CE    1 
ATOM   1446 N NZ    . LYS A 1 180 ? 25.406  28.474  89.294 1.00 12.87 1  180 LYS A NZ    1 
ATOM   1447 N N     . LEU A 1 181 ? 25.997  23.797  84.508 1.00 27.47 ?  181 LEU A N     1 
ATOM   1448 C CA    . LEU A 1 181 ? 25.157  22.607  84.694 1.00 28.87 ?  181 LEU A CA    1 
ATOM   1449 C C     . LEU A 1 181 ? 25.975  21.329  84.898 1.00 9.96  ?  181 LEU A C     1 
ATOM   1450 O O     . LEU A 1 181 ? 25.661  20.526  85.780 1.00 20.63 ?  181 LEU A O     1 
ATOM   1451 C CB    . LEU A 1 181 ? 24.205  22.453  83.517 1.00 21.77 ?  181 LEU A CB    1 
ATOM   1452 C CG    . LEU A 1 181 ? 23.458  21.128  83.541 1.00 8.83  ?  181 LEU A CG    1 
ATOM   1453 C CD1   . LEU A 1 181 ? 22.619  20.968  84.839 1.00 1.89  ?  181 LEU A CD1   1 
ATOM   1454 C CD2   . LEU A 1 181 ? 22.646  20.980  82.261 1.00 3.94  ?  181 LEU A CD2   1 
ATOM   1455 N N     . GLY A 1 182 ? 27.032  21.128  84.115 1.00 18.29 ?  182 GLY A N     1 
ATOM   1456 C CA    . GLY A 1 182 ? 27.922  20.001  84.361 1.00 2.77  ?  182 GLY A CA    1 
ATOM   1457 C C     . GLY A 1 182 ? 28.515  20.018  85.757 1.00 6.86  ?  182 GLY A C     1 
ATOM   1458 O O     . GLY A 1 182 ? 28.735  18.970  86.360 1.00 2.92  ?  182 GLY A O     1 
ATOM   1459 N N     . SER A 1 183 ? 28.797  21.213  86.286 1.00 17.99 ?  183 SER A N     1 
ATOM   1460 C CA    . SER A 1 183 ? 29.359  21.306  87.628 1.00 2.72  ?  183 SER A CA    1 
ATOM   1461 C C     . SER A 1 183 ? 28.412  20.758  88.677 1.00 2.42  ?  183 SER A C     1 
ATOM   1462 O O     . SER A 1 183 ? 28.850  20.307  89.733 1.00 9.59  ?  183 SER A O     1 
ATOM   1463 C CB    . SER A 1 183 ? 29.703  22.757  87.957 1.00 13.16 ?  183 SER A CB    1 
ATOM   1464 O OG    . SER A 1 183 ? 30.977  23.101  87.447 1.00 9.20  ?  183 SER A OG    1 
ATOM   1465 N N     . LEU A 1 184 ? 27.113  20.848  88.440 1.00 22.96 ?  184 LEU A N     1 
ATOM   1466 C CA    . LEU A 1 184 ? 26.152  20.296  89.383 1.00 19.46 ?  184 LEU A CA    1 
ATOM   1467 C C     . LEU A 1 184 ? 25.958  18.810  89.147 1.00 19.71 ?  184 LEU A C     1 
ATOM   1468 O O     . LEU A 1 184 ? 25.735  18.049  90.096 1.00 29.71 ?  184 LEU A O     1 
ATOM   1469 C CB    . LEU A 1 184 ? 24.831  21.053  89.281 1.00 27.12 ?  184 LEU A CB    1 
ATOM   1470 C CG    . LEU A 1 184 ? 24.742  22.407  89.994 1.00 17.76 ?  184 LEU A CG    1 
ATOM   1471 C CD1   . LEU A 1 184 ? 25.946  23.306  89.753 1.00 24.72 ?  184 LEU A CD1   1 
ATOM   1472 C CD2   . LEU A 1 184 ? 23.486  23.109  89.545 1.00 9.83  ?  184 LEU A CD2   1 
ATOM   1473 N N     . CYS A 1 185 ? 26.091  18.376  87.899 1.00 10.78 ?  185 CYS A N     1 
ATOM   1474 C CA    . CYS A 1 185 ? 26.023  16.950  87.615 1.00 17.68 ?  185 CYS A CA    1 
ATOM   1475 C C     . CYS A 1 185 ? 27.244  16.229  88.172 1.00 34.51 ?  185 CYS A C     1 
ATOM   1476 O O     . CYS A 1 185 ? 27.118  15.170  88.798 1.00 53.05 ?  185 CYS A O     1 
ATOM   1477 C CB    . CYS A 1 185 ? 25.935  16.741  86.108 1.00 26.57 ?  185 CYS A CB    1 
ATOM   1478 S SG    . CYS A 1 185 ? 24.343  17.155  85.438 1.00 50.16 ?  185 CYS A SG    1 
ATOM   1479 N N     . THR A 1 186 ? 28.411  16.860  88.097 1.00 17.08 ?  186 THR A N     1 
ATOM   1480 C CA    . THR A 1 186 ? 29.648  16.339  88.696 1.00 15.41 ?  186 THR A CA    1 
ATOM   1481 C C     . THR A 1 186 ? 29.519  16.305  90.227 1.00 22.59 ?  186 THR A C     1 
ATOM   1482 O O     . THR A 1 186 ? 29.911  15.312  90.839 1.00 41.08 ?  186 THR A O     1 
ATOM   1483 C CB    . THR A 1 186 ? 30.865  17.070  88.102 1.00 2.74  ?  186 THR A CB    1 
ATOM   1484 O OG1   . THR A 1 186 ? 31.150  16.625  86.780 1.00 2.92  ?  186 THR A OG1   1 
ATOM   1485 C CG2   . THR A 1 186 ? 32.090  17.001  88.981 1.00 2.87  ?  186 THR A CG2   1 
ATOM   1486 N N     . LYS A 1 187 ? 28.970  17.321  90.852 1.00 32.33 ?  187 LYS A N     1 
ATOM   1487 C CA    . LYS A 1 187 ? 28.682  17.211  92.301 1.00 23.79 ?  187 LYS A CA    1 
ATOM   1488 C C     . LYS A 1 187 ? 27.581  16.168  92.417 1.00 17.88 ?  187 LYS A C     1 
ATOM   1489 O O     . LYS A 1 187 ? 27.517  15.588  93.450 1.00 30.91 ?  187 LYS A O     1 
ATOM   1490 C CB    . LYS A 1 187 ? 28.165  18.533  92.878 1.00 18.51 ?  187 LYS A CB    1 
ATOM   1491 C CG    . LYS A 1 187 ? 28.759  19.063  94.169 1.00 9.35  ?  187 LYS A CG    1 
ATOM   1492 C CD    . LYS A 1 187 ? 27.692  19.801  94.919 1.00 5.91  ?  187 LYS A CD    1 
ATOM   1493 C CE    . LYS A 1 187 ? 28.145  20.504  96.172 1.00 15.12 ?  187 LYS A CE    1 
ATOM   1494 N NZ    . LYS A 1 187 ? 27.409  21.775  96.353 1.00 20.66 1  187 LYS A NZ    1 
ATOM   1495 N N     . VAL A 1 190 ? 25.406  12.917  88.739 1.00 22.51 ?  190 VAL A N     1 
ATOM   1496 C CA    . VAL A 1 190 ? 24.218  12.749  87.929 1.00 22.90 ?  190 VAL A CA    1 
ATOM   1497 C C     . VAL A 1 190 ? 24.657  12.349  86.528 1.00 14.43 ?  190 VAL A C     1 
ATOM   1498 O O     . VAL A 1 190 ? 25.583  12.952  85.966 1.00 2.93  ?  190 VAL A O     1 
ATOM   1499 C CB    . VAL A 1 190 ? 23.378  14.043  87.920 1.00 11.53 ?  190 VAL A CB    1 
ATOM   1500 C CG1   . VAL A 1 190 ? 22.183  13.900  86.999 1.00 1.73  ?  190 VAL A CG1   1 
ATOM   1501 C CG2   . VAL A 1 190 ? 22.932  14.388  89.343 1.00 1.42  ?  190 VAL A CG2   1 
ATOM   1502 N N     . ILE A 1 191 ? 23.995  11.325  85.976 1.00 1.79  ?  191 ILE A N     1 
ATOM   1503 C CA    . ILE A 1 191 ? 24.172  10.888  84.594 1.00 10.89 ?  191 ILE A CA    1 
ATOM   1504 C C     . ILE A 1 191 ? 23.329  11.791  83.701 1.00 17.74 ?  191 ILE A C     1 
ATOM   1505 O O     . ILE A 1 191 ? 22.218  12.181  84.077 1.00 37.23 ?  191 ILE A O     1 
ATOM   1506 C CB    . ILE A 1 191 ? 23.740  9.415   84.422 1.00 18.79 ?  191 ILE A CB    1 
ATOM   1507 C CG1   . ILE A 1 191 ? 24.467  8.484   85.408 1.00 24.13 ?  191 ILE A CG1   1 
ATOM   1508 C CG2   . ILE A 1 191 ? 23.898  8.967   82.952 1.00 15.71 ?  191 ILE A CG2   1 
ATOM   1509 C CD1   . ILE A 1 191 ? 24.385  6.984   85.064 1.00 8.76  ?  191 ILE A CD1   1 
ATOM   1510 N N     . VAL A 1 192 ? 23.841  12.132  82.520 1.00 15.84 ?  192 VAL A N     1 
ATOM   1511 C CA    . VAL A 1 192 ? 23.213  13.104  81.627 1.00 2.10  ?  192 VAL A CA    1 
ATOM   1512 C C     . VAL A 1 192 ? 22.925  12.456  80.279 1.00 17.98 ?  192 VAL A C     1 
ATOM   1513 O O     . VAL A 1 192 ? 23.840  11.932  79.628 1.00 33.13 ?  192 VAL A O     1 
ATOM   1514 C CB    . VAL A 1 192 ? 24.101  14.345  81.446 1.00 13.70 ?  192 VAL A CB    1 
ATOM   1515 C CG1   . VAL A 1 192 ? 23.560  15.229  80.352 1.00 7.84  ?  192 VAL A CG1   1 
ATOM   1516 C CG2   . VAL A 1 192 ? 24.223  15.091  82.762 1.00 2.17  ?  192 VAL A CG2   1 
ATOM   1517 N N     . VAL A 1 193 ? 21.669  12.513  79.849 1.00 3.68  ?  193 VAL A N     1 
ATOM   1518 C CA    . VAL A 1 193 ? 21.279  12.176  78.482 1.00 12.07 ?  193 VAL A CA    1 
ATOM   1519 C C     . VAL A 1 193 ? 21.036  13.501  77.776 1.00 13.80 ?  193 VAL A C     1 
ATOM   1520 O O     . VAL A 1 193 ? 20.258  14.335  78.253 1.00 13.30 ?  193 VAL A O     1 
ATOM   1521 C CB    . VAL A 1 193 ? 20.041  11.257  78.454 1.00 9.83  ?  193 VAL A CB    1 
ATOM   1522 C CG1   . VAL A 1 193 ? 19.830  10.639  77.087 1.00 2.12  ?  193 VAL A CG1   1 
ATOM   1523 C CG2   . VAL A 1 193 ? 20.197  10.171  79.476 1.00 1.90  ?  193 VAL A CG2   1 
ATOM   1524 N N     . ALA A 1 194 ? 21.794  13.747  76.718 1.00 16.11 ?  194 ALA A N     1 
ATOM   1525 C CA    . ALA A 1 194 ? 21.785  15.024  76.016 1.00 6.19  ?  194 ALA A CA    1 
ATOM   1526 C C     . ALA A 1 194 ? 21.028  14.855  74.707 1.00 2.79  ?  194 ALA A C     1 
ATOM   1527 O O     . ALA A 1 194 ? 21.547  14.288  73.744 1.00 8.30  ?  194 ALA A O     1 
ATOM   1528 C CB    . ALA A 1 194 ? 23.214  15.514  75.805 1.00 3.19  ?  194 ALA A CB    1 
ATOM   1529 N N     . ASP A 1 195 ? 19.794  15.342  74.668 1.00 29.24 ?  195 ASP A N     1 
ATOM   1530 C CA    . ASP A 1 195 ? 18.985  15.287  73.451 1.00 24.76 ?  195 ASP A CA    1 
ATOM   1531 C C     . ASP A 1 195 ? 19.295  16.513  72.590 1.00 7.98  ?  195 ASP A C     1 
ATOM   1532 O O     . ASP A 1 195 ? 18.668  17.557  72.709 1.00 4.12  ?  195 ASP A O     1 
ATOM   1533 C CB    . ASP A 1 195 ? 17.513  15.168  73.819 1.00 2.41  ?  195 ASP A CB    1 
ATOM   1534 C CG    . ASP A 1 195 ? 16.660  14.903  72.629 1.00 19.22 ?  195 ASP A CG    1 
ATOM   1535 O OD1   . ASP A 1 195 ? 17.169  15.104  71.509 1.00 11.48 ?  195 ASP A OD1   1 
ATOM   1536 O OD2   . ASP A 1 195 ? 15.497  14.484  72.793 1.00 19.81 -1 195 ASP A OD2   1 
ATOM   1537 N N     . GLU A 1 196 ? 20.265  16.358  71.691 1.00 16.98 ?  196 GLU A N     1 
ATOM   1538 C CA    . GLU A 1 196 ? 20.751  17.411  70.804 1.00 25.82 ?  196 GLU A CA    1 
ATOM   1539 C C     . GLU A 1 196 ? 20.279  17.167  69.376 1.00 15.49 ?  196 GLU A C     1 
ATOM   1540 O O     . GLU A 1 196 ? 21.030  17.330  68.414 1.00 22.65 ?  196 GLU A O     1 
ATOM   1541 C CB    . GLU A 1 196 ? 22.287  17.520  70.849 1.00 22.53 ?  196 GLU A CB    1 
ATOM   1542 C CG    . GLU A 1 196 ? 22.922  17.729  72.263 1.00 19.76 ?  196 GLU A CG    1 
ATOM   1543 C CD    . GLU A 1 196 ? 24.474  17.652  72.327 1.00 6.42  ?  196 GLU A CD    1 
ATOM   1544 O OE1   . GLU A 1 196 ? 25.012  17.581  73.455 1.00 3.88  ?  196 GLU A OE1   1 
ATOM   1545 O OE2   . GLU A 1 196 ? 25.153  17.675  71.282 1.00 4.40  -1 196 GLU A OE2   1 
ATOM   1546 N N     . ILE A 1 197 ? 19.020  16.780  69.222 1.00 3.74  ?  197 ILE A N     1 
ATOM   1547 C CA    . ILE A 1 197 ? 18.522  16.482  67.886 1.00 3.99  ?  197 ILE A CA    1 
ATOM   1548 C C     . ILE A 1 197 ? 18.413  17.769  67.072 1.00 26.13 ?  197 ILE A C     1 
ATOM   1549 O O     . ILE A 1 197 ? 18.470  17.734  65.838 1.00 28.00 ?  197 ILE A O     1 
ATOM   1550 C CB    . ILE A 1 197 ? 17.188  15.688  68.007 1.00 3.67  ?  197 ILE A CB    1 
ATOM   1551 C CG1   . ILE A 1 197 ? 16.803  15.010  66.694 1.00 13.08 ?  197 ILE A CG1   1 
ATOM   1552 C CG2   . ILE A 1 197 ? 16.049  16.534  68.587 1.00 3.39  ?  197 ILE A CG2   1 
ATOM   1553 C CD1   . ILE A 1 197 ? 15.413  14.435  66.688 1.00 5.51  ?  197 ILE A CD1   1 
ATOM   1554 N N     . HIS A 1 198 ? 18.307  18.919  67.740 1.00 21.68 ?  198 HIS A N     1 
ATOM   1555 C CA    . HIS A 1 198 ? 18.255  20.215  67.078 1.00 27.34 ?  198 HIS A CA    1 
ATOM   1556 C C     . HIS A 1 198 ? 19.625  20.910  67.006 1.00 8.38  ?  198 HIS A C     1 
ATOM   1557 O O     . HIS A 1 198 ? 19.689  22.118  66.763 1.00 11.86 ?  198 HIS A O     1 
ATOM   1558 C CB    . HIS A 1 198 ? 17.243  21.129  67.778 1.00 17.97 ?  198 HIS A CB    1 
ATOM   1559 C CG    . HIS A 1 198 ? 15.847  20.591  67.822 1.00 14.66 ?  198 HIS A CG    1 
ATOM   1560 N ND1   . HIS A 1 198 ? 15.024  20.561  66.715 1.00 19.16 ?  198 HIS A ND1   1 
ATOM   1561 C CD2   . HIS A 1 198 ? 15.110  20.119  68.856 1.00 11.19 ?  198 HIS A CD2   1 
ATOM   1562 C CE1   . HIS A 1 198 ? 13.849  20.062  67.062 1.00 19.92 ?  198 HIS A CE1   1 
ATOM   1563 N NE2   . HIS A 1 198 ? 13.875  19.793  68.355 1.00 18.25 ?  198 HIS A NE2   1 
ATOM   1564 N N     . SER A 1 199 ? 20.710  20.169  67.192 1.00 4.90  ?  199 SER A N     1 
ATOM   1565 C CA    . SER A 1 199 ? 22.038  20.753  67.363 1.00 14.77 ?  199 SER A CA    1 
ATOM   1566 C C     . SER A 1 199 ? 22.567  21.503  66.139 1.00 13.94 ?  199 SER A C     1 
ATOM   1567 O O     . SER A 1 199 ? 23.537  22.249  66.273 1.00 15.14 ?  199 SER A O     1 
ATOM   1568 C CB    . SER A 1 199 ? 23.031  19.650  67.766 1.00 11.41 ?  199 SER A CB    1 
ATOM   1569 O OG    . SER A 1 199 ? 23.235  18.731  66.712 1.00 20.78 ?  199 SER A OG    1 
ATOM   1570 N N     . ASP A 1 200 ? 21.993  21.302  64.955 1.00 25.89 ?  200 ASP A N     1 
ATOM   1571 C CA    . ASP A 1 200 ? 22.548  21.837  63.714 1.00 23.08 ?  200 ASP A CA    1 
ATOM   1572 C C     . ASP A 1 200 ? 21.758  23.005  63.119 1.00 24.15 ?  200 ASP A C     1 
ATOM   1573 O O     . ASP A 1 200 ? 22.180  23.555  62.098 1.00 17.93 ?  200 ASP A O     1 
ATOM   1574 C CB    . ASP A 1 200 ? 22.670  20.718  62.675 1.00 27.03 ?  200 ASP A CB    1 
ATOM   1575 C CG    . ASP A 1 200 ? 23.823  19.779  62.964 1.00 33.12 ?  200 ASP A CG    1 
ATOM   1576 O OD1   . ASP A 1 200 ? 24.871  20.228  63.456 1.00 36.44 ?  200 ASP A OD1   1 
ATOM   1577 O OD2   . ASP A 1 200 ? 23.682  18.578  62.690 1.00 42.41 -1 200 ASP A OD2   1 
ATOM   1578 N N     . ILE A 1 201 ? 20.611  23.378  63.692 1.00 34.43 ?  201 ILE A N     1 
ATOM   1579 C CA    . ILE A 1 201 ? 19.890  24.570  63.245 1.00 23.57 ?  201 ILE A CA    1 
ATOM   1580 C C     . ILE A 1 201 ? 20.028  25.655  64.305 1.00 25.10 ?  201 ILE A C     1 
ATOM   1581 O O     . ILE A 1 201 ? 19.239  25.720  65.255 1.00 24.85 ?  201 ILE A O     1 
ATOM   1582 C CB    . ILE A 1 201 ? 18.415  24.269  62.959 1.00 14.08 ?  201 ILE A CB    1 
ATOM   1583 C CG1   . ILE A 1 201 ? 18.297  23.284  61.811 1.00 10.80 ?  201 ILE A CG1   1 
ATOM   1584 C CG2   . ILE A 1 201 ? 17.706  25.535  62.540 1.00 31.32 ?  201 ILE A CG2   1 
ATOM   1585 C CD1   . ILE A 1 201 ? 18.086  23.950  60.484 1.00 11.71 ?  201 ILE A CD1   1 
ATOM   1586 N N     . ILE A 1 202 ? 21.072  26.464  64.184 1.00 19.92 ?  202 ILE A N     1 
ATOM   1587 C CA    . ILE A 1 202 ? 21.428  27.468  65.179 1.00 23.46 ?  202 ILE A CA    1 
ATOM   1588 C C     . ILE A 1 202 ? 21.578  28.815  64.481 1.00 24.71 ?  202 ILE A C     1 
ATOM   1589 O O     . ILE A 1 202 ? 22.024  28.888  63.331 1.00 24.92 ?  202 ILE A O     1 
ATOM   1590 C CB    . ILE A 1 202 ? 22.723  27.082  65.923 1.00 10.69 ?  202 ILE A CB    1 
ATOM   1591 C CG1   . ILE A 1 202 ? 22.599  25.676  66.493 1.00 8.92  ?  202 ILE A CG1   1 
ATOM   1592 C CG2   . ILE A 1 202 ? 23.024  28.068  67.044 1.00 6.22  ?  202 ILE A CG2   1 
ATOM   1593 C CD1   . ILE A 1 202 ? 21.820  25.600  67.756 1.00 5.49  ?  202 ILE A CD1   1 
ATOM   1594 N N     . TYR A 1 203 ? 21.209  29.881  65.165 1.00 11.54 ?  203 TYR A N     1 
ATOM   1595 C CA    . TYR A 1 203 ? 21.178  31.161  64.490 1.00 18.11 ?  203 TYR A CA    1 
ATOM   1596 C C     . TYR A 1 203 ? 22.560  31.835  64.542 1.00 20.57 ?  203 TYR A C     1 
ATOM   1597 O O     . TYR A 1 203 ? 23.486  31.367  65.206 1.00 23.17 ?  203 TYR A O     1 
ATOM   1598 C CB    . TYR A 1 203 ? 20.064  32.002  65.105 1.00 19.29 ?  203 TYR A CB    1 
ATOM   1599 C CG    . TYR A 1 203 ? 18.663  31.427  64.872 1.00 17.88 ?  203 TYR A CG    1 
ATOM   1600 C CD1   . TYR A 1 203 ? 18.407  30.498  63.863 1.00 6.82  ?  203 TYR A CD1   1 
ATOM   1601 C CD2   . TYR A 1 203 ? 17.592  31.839  65.653 1.00 29.46 ?  203 TYR A CD2   1 
ATOM   1602 C CE1   . TYR A 1 203 ? 17.112  29.984  63.657 1.00 6.81  ?  203 TYR A CE1   1 
ATOM   1603 C CE2   . TYR A 1 203 ? 16.304  31.341  65.454 1.00 29.64 ?  203 TYR A CE2   1 
ATOM   1604 C CZ    . TYR A 1 203 ? 16.064  30.419  64.464 1.00 18.31 ?  203 TYR A CZ    1 
ATOM   1605 O OH    . TYR A 1 203 ? 14.773  29.957  64.309 1.00 16.24 ?  203 TYR A OH    1 
ATOM   1606 N N     . ALA A 1 204 ? 22.688  32.953  63.817 1.00 11.87 ?  204 ALA A N     1 
ATOM   1607 C CA    . ALA A 1 204 ? 24.001  33.546  63.562 1.00 9.34  ?  204 ALA A CA    1 
ATOM   1608 C C     . ALA A 1 204 ? 24.693  33.983  64.852 1.00 24.81 ?  204 ALA A C     1 
ATOM   1609 O O     . ALA A 1 204 ? 25.908  33.804  65.000 1.00 34.91 ?  204 ALA A O     1 
ATOM   1610 C CB    . ALA A 1 204 ? 23.869  34.709  62.577 1.00 8.85  ?  204 ALA A CB    1 
ATOM   1611 N N     . ASP A 1 205 ? 23.938  34.504  65.814 1.00 7.64  ?  205 ASP A N     1 
ATOM   1612 C CA    . ASP A 1 205 ? 24.487  35.010  67.063 1.00 7.40  ?  205 ASP A CA    1 
ATOM   1613 C C     . ASP A 1 205 ? 24.604  33.933  68.147 1.00 15.30 ?  205 ASP A C     1 
ATOM   1614 O O     . ASP A 1 205 ? 24.718  34.275  69.333 1.00 13.97 ?  205 ASP A O     1 
ATOM   1615 C CB    . ASP A 1 205 ? 23.632  36.168  67.594 1.00 12.06 ?  205 ASP A CB    1 
ATOM   1616 C CG    . ASP A 1 205 ? 23.278  37.179  66.526 1.00 24.01 ?  205 ASP A CG    1 
ATOM   1617 O OD1   . ASP A 1 205 ? 23.968  37.246  65.492 1.00 30.65 ?  205 ASP A OD1   1 
ATOM   1618 O OD2   . ASP A 1 205 ? 22.275  37.894  66.707 1.00 35.43 -1 205 ASP A OD2   1 
ATOM   1619 N N     . HIS A 1 206 ? 24.533  32.650  67.788 1.00 27.01 ?  206 HIS A N     1 
ATOM   1620 C CA    . HIS A 1 206 ? 24.559  31.583  68.788 1.00 32.02 ?  206 HIS A CA    1 
ATOM   1621 C C     . HIS A 1 206 ? 25.392  30.395  68.315 1.00 6.56  ?  206 HIS A C     1 
ATOM   1622 O O     . HIS A 1 206 ? 25.593  30.179  67.119 1.00 6.96  ?  206 HIS A O     1 
ATOM   1623 C CB    . HIS A 1 206 ? 23.147  31.115  69.132 1.00 13.77 ?  206 HIS A CB    1 
ATOM   1624 C CG    . HIS A 1 206 ? 22.234  32.231  69.487 1.00 5.82  ?  206 HIS A CG    1 
ATOM   1625 N ND1   . HIS A 1 206 ? 21.472  32.893  68.548 1.00 6.05  ?  206 HIS A ND1   1 
ATOM   1626 C CD2   . HIS A 1 206 ? 21.982  32.828  70.675 1.00 17.44 ?  206 HIS A CD2   1 
ATOM   1627 C CE1   . HIS A 1 206 ? 20.778  33.845  69.145 1.00 19.95 ?  206 HIS A CE1   1 
ATOM   1628 N NE2   . HIS A 1 206 ? 21.074  33.832  70.436 1.00 18.39 ?  206 HIS A NE2   1 
ATOM   1629 N N     . THR A 1 207 ? 25.817  29.583  69.275 1.00 6.26  ?  207 THR A N     1 
ATOM   1630 C CA    . THR A 1 207 ? 26.683  28.453  68.959 1.00 18.81 ?  207 THR A CA    1 
ATOM   1631 C C     . THR A 1 207 ? 26.256  27.245  69.786 1.00 18.65 ?  207 THR A C     1 
ATOM   1632 O O     . THR A 1 207 ? 26.082  27.337  71.008 1.00 13.37 ?  207 THR A O     1 
ATOM   1633 C CB    . THR A 1 207 ? 28.168  28.827  69.207 1.00 18.76 ?  207 THR A CB    1 
ATOM   1634 O OG1   . THR A 1 207 ? 28.622  29.675  68.137 1.00 28.55 ?  207 THR A OG1   1 
ATOM   1635 C CG2   . THR A 1 207 ? 29.077  27.614  69.292 1.00 21.13 ?  207 THR A CG2   1 
ATOM   1636 N N     . HIS A 1 208 ? 26.024  26.127  69.123 1.00 12.45 ?  208 HIS A N     1 
ATOM   1637 C CA    . HIS A 1 208 ? 25.696  24.948  69.899 1.00 22.28 ?  208 HIS A CA    1 
ATOM   1638 C C     . HIS A 1 208 ? 26.940  24.495  70.638 1.00 25.14 ?  208 HIS A C     1 
ATOM   1639 O O     . HIS A 1 208 ? 28.029  24.407  70.062 1.00 12.36 ?  208 HIS A O     1 
ATOM   1640 C CB    . HIS A 1 208 ? 25.157  23.816  69.038 1.00 28.54 ?  208 HIS A CB    1 
ATOM   1641 C CG    . HIS A 1 208 ? 24.977  22.544  69.805 1.00 23.15 ?  208 HIS A CG    1 
ATOM   1642 N ND1   . HIS A 1 208 ? 24.132  22.445  70.889 1.00 17.41 ?  208 HIS A ND1   1 
ATOM   1643 C CD2   . HIS A 1 208 ? 25.581  21.339  69.688 1.00 17.44 ?  208 HIS A CD2   1 
ATOM   1644 C CE1   . HIS A 1 208 ? 24.208  21.228  71.391 1.00 13.02 ?  208 HIS A CE1   1 
ATOM   1645 N NE2   . HIS A 1 208 ? 25.078  20.537  70.679 1.00 8.60  ?  208 HIS A NE2   1 
ATOM   1646 N N     . THR A 1 209 ? 26.765  24.234  71.923 1.00 24.92 ?  209 THR A N     1 
ATOM   1647 C CA    . THR A 1 209 ? 27.837  23.835  72.826 1.00 20.25 ?  209 THR A CA    1 
ATOM   1648 C C     . THR A 1 209 ? 27.574  22.392  73.240 1.00 31.38 ?  209 THR A C     1 
ATOM   1649 O O     . THR A 1 209 ? 26.696  22.135  74.082 1.00 34.50 ?  209 THR A O     1 
ATOM   1650 C CB    . THR A 1 209 ? 27.909  24.760  74.049 1.00 9.13  ?  209 THR A CB    1 
ATOM   1651 O OG1   . THR A 1 209 ? 28.383  26.049  73.644 1.00 23.33 ?  209 THR A OG1   1 
ATOM   1652 C CG2   . THR A 1 209 ? 28.829  24.221  75.096 1.00 16.90 ?  209 THR A CG2   1 
ATOM   1653 N N     . PRO A 1 210 ? 28.227  21.414  72.610 1.00 22.76 ?  210 PRO A N     1 
ATOM   1654 C CA    . PRO A 1 210 ? 28.086  20.027  73.070 1.00 9.23  ?  210 PRO A CA    1 
ATOM   1655 C C     . PRO A 1 210 ? 28.491  19.898  74.528 1.00 4.50  ?  210 PRO A C     1 
ATOM   1656 O O     . PRO A 1 210 ? 29.488  20.464  74.961 1.00 9.58  ?  210 PRO A O     1 
ATOM   1657 C CB    . PRO A 1 210 ? 29.021  19.252  72.142 1.00 5.08  ?  210 PRO A CB    1 
ATOM   1658 C CG    . PRO A 1 210 ? 29.085  20.092  70.911 1.00 5.47  ?  210 PRO A CG    1 
ATOM   1659 C CD    . PRO A 1 210 ? 29.029  21.507  71.377 1.00 5.47  ?  210 PRO A CD    1 
ATOM   1660 N N     . PHE A 1 211 ? 27.643  19.234  75.298 1.00 4.12  ?  211 PHE A N     1 
ATOM   1661 C CA    . PHE A 1 211 ? 27.870  19.042  76.731 1.00 9.34  ?  211 PHE A CA    1 
ATOM   1662 C C     . PHE A 1 211 ? 29.043  18.095  76.988 1.00 25.41 ?  211 PHE A C     1 
ATOM   1663 O O     . PHE A 1 211 ? 29.820  18.283  77.938 1.00 22.10 ?  211 PHE A O     1 
ATOM   1664 C CB    . PHE A 1 211 ? 26.581  18.506  77.357 1.00 3.48  ?  211 PHE A CB    1 
ATOM   1665 C CG    . PHE A 1 211 ? 26.577  18.452  78.855 1.00 3.23  ?  211 PHE A CG    1 
ATOM   1666 C CD1   . PHE A 1 211 ? 26.702  19.586  79.598 1.00 3.20  ?  211 PHE A CD1   1 
ATOM   1667 C CD2   . PHE A 1 211 ? 26.335  17.260  79.508 1.00 3.02  ?  211 PHE A CD2   1 
ATOM   1668 C CE1   . PHE A 1 211 ? 26.656  19.535  80.970 1.00 2.98  ?  211 PHE A CE1   1 
ATOM   1669 C CE2   . PHE A 1 211 ? 26.289  17.209  80.867 1.00 11.09 ?  211 PHE A CE2   1 
ATOM   1670 C CZ    . PHE A 1 211 ? 26.445  18.361  81.603 1.00 2.79  ?  211 PHE A CZ    1 
ATOM   1671 N N     . ALA A 1 212 ? 29.152  17.036  76.188 1.00 20.95 ?  212 ALA A N     1 
ATOM   1672 C CA    . ALA A 1 212 ? 30.249  16.104  76.377 1.00 25.82 ?  212 ALA A CA    1 
ATOM   1673 C C     . ALA A 1 212 ? 31.548  16.614  75.763 1.00 16.74 ?  212 ALA A C     1 
ATOM   1674 O O     . ALA A 1 212 ? 32.609  16.045  76.030 1.00 18.36 ?  212 ALA A O     1 
ATOM   1675 C CB    . ALA A 1 212 ? 29.865  14.734  75.805 1.00 4.15  ?  212 ALA A CB    1 
ATOM   1676 N N     . SER A 1 213 ? 31.482  17.666  74.945 1.00 13.31 ?  213 SER A N     1 
ATOM   1677 C CA    . SER A 1 213 ? 32.675  18.325  74.435 1.00 5.25  ?  213 SER A CA    1 
ATOM   1678 C C     . SER A 1 213 ? 33.404  19.120  75.513 1.00 19.04 ?  213 SER A C     1 
ATOM   1679 O O     . SER A 1 213 ? 34.600  19.375  75.359 1.00 22.78 ?  213 SER A O     1 
ATOM   1680 C CB    . SER A 1 213 ? 32.329  19.237  73.275 1.00 11.20 ?  213 SER A CB    1 
ATOM   1681 O OG    . SER A 1 213 ? 32.078  20.542  73.763 1.00 30.06 ?  213 SER A OG    1 
ATOM   1682 N N     . LEU A 1 214 ? 32.705  19.565  76.570 1.00 12.53 ?  214 LEU A N     1 
ATOM   1683 C CA    . LEU A 1 214 ? 33.314  20.495  77.521 1.00 11.27 ?  214 LEU A CA    1 
ATOM   1684 C C     . LEU A 1 214 ? 34.527  19.875  78.198 1.00 26.02 ?  214 LEU A C     1 
ATOM   1685 O O     . LEU A 1 214 ? 35.557  20.539  78.386 1.00 35.15 ?  214 LEU A O     1 
ATOM   1686 C CB    . LEU A 1 214 ? 32.295  20.920  78.583 1.00 4.55  ?  214 LEU A CB    1 
ATOM   1687 C CG    . LEU A 1 214 ? 31.014  21.607  78.074 1.00 13.21 ?  214 LEU A CG    1 
ATOM   1688 C CD1   . LEU A 1 214 ? 29.869  21.630  79.112 1.00 16.51 ?  214 LEU A CD1   1 
ATOM   1689 C CD2   . LEU A 1 214 ? 31.285  23.004  77.542 1.00 12.70 ?  214 LEU A CD2   1 
ATOM   1690 N N     . SER A 1 215 ? 34.423  18.609  78.583 1.00 18.00 ?  215 SER A N     1 
ATOM   1691 C CA    . SER A 1 215 ? 35.470  18.024  79.398 1.00 15.20 ?  215 SER A CA    1 
ATOM   1692 C C     . SER A 1 215 ? 35.428  16.504  79.316 1.00 21.39 ?  215 SER A C     1 
ATOM   1693 O O     . SER A 1 215 ? 34.402  15.898  78.987 1.00 16.96 ?  215 SER A O     1 
ATOM   1694 C CB    . SER A 1 215 ? 35.351  18.488  80.845 1.00 21.21 ?  215 SER A CB    1 
ATOM   1695 O OG    . SER A 1 215 ? 34.229  17.917  81.506 1.00 36.87 ?  215 SER A OG    1 
ATOM   1696 N N     . GLU A 1 216 ? 36.570  15.899  79.662 1.00 31.74 ?  216 GLU A N     1 
ATOM   1697 C CA    . GLU A 1 216 ? 36.643  14.459  79.880 1.00 29.07 ?  216 GLU A CA    1 
ATOM   1698 C C     . GLU A 1 216 ? 35.793  14.039  81.069 1.00 20.24 ?  216 GLU A C     1 
ATOM   1699 O O     . GLU A 1 216 ? 35.428  12.869  81.181 1.00 27.09 ?  216 GLU A O     1 
ATOM   1700 C CB    . GLU A 1 216 ? 38.088  14.020  80.123 1.00 41.18 ?  216 GLU A CB    1 
ATOM   1701 C CG    . GLU A 1 216 ? 39.101  14.449  79.056 1.00 46.93 ?  216 GLU A CG    1 
ATOM   1702 C CD    . GLU A 1 216 ? 40.358  13.605  79.091 1.00 34.35 ?  216 GLU A CD    1 
ATOM   1703 O OE1   . GLU A 1 216 ? 41.366  14.011  78.477 1.00 34.00 ?  216 GLU A OE1   1 
ATOM   1704 O OE2   . GLU A 1 216 ? 40.332  12.538  79.741 1.00 33.12 -1 216 GLU A OE2   1 
ATOM   1705 N N     . GLU A 1 217 ? 35.515  14.960  81.987 1.00 14.25 ?  217 GLU A N     1 
ATOM   1706 C CA    . GLU A 1 217 ? 34.712  14.658  83.164 1.00 13.37 ?  217 GLU A CA    1 
ATOM   1707 C C     . GLU A 1 217 ? 33.232  14.584  82.845 1.00 21.08 ?  217 GLU A C     1 
ATOM   1708 O O     . GLU A 1 217 ? 32.523  13.763  83.436 1.00 21.33 ?  217 GLU A O     1 
ATOM   1709 C CB    . GLU A 1 217 ? 34.964  15.731  84.228 1.00 3.90  ?  217 GLU A CB    1 
ATOM   1710 C CG    . GLU A 1 217 ? 34.150  15.554  85.473 1.00 19.87 ?  217 GLU A CG    1 
ATOM   1711 C CD    . GLU A 1 217 ? 35.021  15.416  86.680 1.00 30.14 ?  217 GLU A CD    1 
ATOM   1712 O OE1   . GLU A 1 217 ? 34.504  15.110  87.772 1.00 36.71 ?  217 GLU A OE1   1 
ATOM   1713 O OE2   . GLU A 1 217 ? 36.240  15.614  86.514 1.00 40.91 -1 217 GLU A OE2   1 
ATOM   1714 N N     . LEU A 1 218 ? 32.744  15.479  81.989 1.00 28.53 ?  218 LEU A N     1 
ATOM   1715 C CA    . LEU A 1 218 ? 31.355  15.402  81.561 1.00 18.80 ?  218 LEU A CA    1 
ATOM   1716 C C     . LEU A 1 218 ? 31.142  14.362  80.471 1.00 12.79 ?  218 LEU A C     1 
ATOM   1717 O O     . LEU A 1 218 ? 30.027  13.860  80.328 1.00 11.13 ?  218 LEU A O     1 
ATOM   1718 C CB    . LEU A 1 218 ? 30.861  16.775  81.105 1.00 3.59  ?  218 LEU A CB    1 
ATOM   1719 C CG    . LEU A 1 218 ? 31.065  17.777  82.235 1.00 3.52  ?  218 LEU A CG    1 
ATOM   1720 C CD1   . LEU A 1 218 ? 30.484  19.098  81.851 1.00 3.59  ?  218 LEU A CD1   1 
ATOM   1721 C CD2   . LEU A 1 218 ? 30.510  17.293  83.582 1.00 3.21  ?  218 LEU A CD2   1 
ATOM   1722 N N     . ALA A 1 219 ? 32.180  14.052  79.686 1.00 23.69 ?  219 ALA A N     1 
ATOM   1723 C CA    . ALA A 1 219 ? 32.063  13.044  78.633 1.00 25.31 ?  219 ALA A CA    1 
ATOM   1724 C C     . ALA A 1 219 ? 31.752  11.668  79.204 1.00 26.57 ?  219 ALA A C     1 
ATOM   1725 O O     . ALA A 1 219 ? 30.835  10.985  78.734 1.00 40.13 ?  219 ALA A O     1 
ATOM   1726 C CB    . ALA A 1 219 ? 33.358  12.996  77.806 1.00 18.36 ?  219 ALA A CB    1 
ATOM   1727 N N     . GLU A 1 220 ? 32.471  11.263  80.251 1.00 14.95 ?  220 GLU A N     1 
ATOM   1728 C CA    . GLU A 1 220 ? 32.256  9.920   80.781 1.00 30.45 ?  220 GLU A CA    1 
ATOM   1729 C C     . GLU A 1 220 ? 30.944  9.785   81.575 1.00 19.15 ?  220 GLU A C     1 
ATOM   1730 O O     . GLU A 1 220 ? 30.669  8.698   82.088 1.00 17.33 ?  220 GLU A O     1 
ATOM   1731 C CB    . GLU A 1 220 ? 33.443  9.493   81.654 1.00 37.81 ?  220 GLU A CB    1 
ATOM   1732 C CG    . GLU A 1 220 ? 34.845  9.613   81.009 1.00 26.09 ?  220 GLU A CG    1 
ATOM   1733 C CD    . GLU A 1 220 ? 35.294  8.385   80.251 1.00 7.14  ?  220 GLU A CD    1 
ATOM   1734 O OE1   . GLU A 1 220 ? 35.645  8.490   79.061 1.00 5.44  ?  220 GLU A OE1   1 
ATOM   1735 O OE2   . GLU A 1 220 ? 35.307  7.307   80.858 1.00 22.83 -1 220 GLU A OE2   1 
ATOM   1736 N N     . ARG A 1 221 ? 30.107  10.828  81.662 1.00 22.57 ?  221 ARG A N     1 
ATOM   1737 C CA    . ARG A 1 221 ? 28.836  10.752  82.381 1.00 2.83  ?  221 ARG A CA    1 
ATOM   1738 C C     . ARG A 1 221 ? 27.673  11.217  81.522 1.00 2.76  ?  221 ARG A C     1 
ATOM   1739 O O     . ARG A 1 221 ? 26.564  11.381  82.038 1.00 2.52  ?  221 ARG A O     1 
ATOM   1740 C CB    . ARG A 1 221 ? 28.881  11.567  83.678 1.00 13.91 ?  221 ARG A CB    1 
ATOM   1741 C CG    . ARG A 1 221 ? 29.067  13.073  83.434 1.00 11.27 ?  221 ARG A CG    1 
ATOM   1742 C CD    . ARG A 1 221 ? 28.593  13.843  84.629 1.00 2.62  ?  221 ARG A CD    1 
ATOM   1743 N NE    . ARG A 1 221 ? 29.498  13.702  85.758 1.00 2.65  ?  221 ARG A NE    1 
ATOM   1744 C CZ    . ARG A 1 221 ? 29.295  12.909  86.799 1.00 15.60 ?  221 ARG A CZ    1 
ATOM   1745 N NH1   . ARG A 1 221 ? 28.211  12.143  86.862 1.00 2.91  1  221 ARG A NH1   1 
ATOM   1746 N NH2   . ARG A 1 221 ? 30.188  12.873  87.776 1.00 18.35 ?  221 ARG A NH2   1 
ATOM   1747 N N     . THR A 1 222 ? 27.901  11.458  80.244 1.00 2.96  ?  222 THR A N     1 
ATOM   1748 C CA    . THR A 1 222 ? 26.882  11.994  79.359 1.00 19.22 ?  222 THR A CA    1 
ATOM   1749 C C     . THR A 1 222 ? 26.670  11.046  78.197 1.00 28.53 ?  222 THR A C     1 
ATOM   1750 O O     . THR A 1 222 ? 27.644  10.524  77.631 1.00 11.83 ?  222 THR A O     1 
ATOM   1751 C CB    . THR A 1 222 ? 27.268  13.376  78.825 1.00 8.90  ?  222 THR A CB    1 
ATOM   1752 O OG1   . THR A 1 222 ? 27.313  14.310  79.917 1.00 9.01  ?  222 THR A OG1   1 
ATOM   1753 C CG2   . THR A 1 222 ? 26.301  13.830  77.763 1.00 3.12  ?  222 THR A CG2   1 
ATOM   1754 N N     . ILE A 1 223 ? 25.396  10.850  77.835 1.00 2.85  ?  223 ILE A N     1 
ATOM   1755 C CA    . ILE A 1 223 ? 25.003  10.127  76.634 1.00 2.94  ?  223 ILE A CA    1 
ATOM   1756 C C     . ILE A 1 223 ? 24.422  11.144  75.669 1.00 11.34 ?  223 ILE A C     1 
ATOM   1757 O O     . ILE A 1 223 ? 23.451  11.834  75.997 1.00 24.09 ?  223 ILE A O     1 
ATOM   1758 C CB    . ILE A 1 223 ? 23.978  9.020   76.918 1.00 17.03 ?  223 ILE A CB    1 
ATOM   1759 C CG1   . ILE A 1 223 ? 24.526  8.014   77.935 1.00 9.61  ?  223 ILE A CG1   1 
ATOM   1760 C CG2   . ILE A 1 223 ? 23.616  8.334   75.611 1.00 2.83  ?  223 ILE A CG2   1 
ATOM   1761 C CD1   . ILE A 1 223 ? 24.112  8.258   79.377 1.00 12.12 ?  223 ILE A CD1   1 
ATOM   1762 N N     . THR A 1 224 ? 25.015  11.256  74.488 1.00 7.09  ?  224 THR A N     1 
ATOM   1763 C CA    . THR A 1 224 ? 24.684  12.310  73.545 1.00 3.88  ?  224 THR A CA    1 
ATOM   1764 C C     . THR A 1 224 ? 23.924  11.786  72.340 1.00 15.18 ?  224 THR A C     1 
ATOM   1765 O O     . THR A 1 224 ? 24.513  11.119  71.483 1.00 11.12 ?  224 THR A O     1 
ATOM   1766 C CB    . THR A 1 224 ? 25.935  13.011  73.047 1.00 4.33  ?  224 THR A CB    1 
ATOM   1767 O OG1   . THR A 1 224 ? 26.718  13.424  74.174 1.00 19.33 ?  224 THR A OG1   1 
ATOM   1768 C CG2   . THR A 1 224 ? 25.510  14.211  72.187 1.00 4.02  ?  224 THR A CG2   1 
ATOM   1769 N N     . CYS A 1 225 ? 22.709  12.306  72.157 1.00 3.42  ?  225 CYS A N     1 
ATOM   1770 C CA    . CYS A 1 225 ? 21.820  11.923  71.073 1.00 8.44  ?  225 CYS A CA    1 
ATOM   1771 C C     . CYS A 1 225 ? 21.817  13.042  70.045 1.00 7.78  ?  225 CYS A C     1 
ATOM   1772 O O     . CYS A 1 225 ? 21.697  14.217  70.406 1.00 3.73  ?  225 CYS A O     1 
ATOM   1773 C CB    . CYS A 1 225 ? 20.372  11.695  71.540 1.00 14.49 ?  225 CYS A CB    1 
ATOM   1774 S SG    . CYS A 1 225 ? 20.055  10.992  73.162 1.00 5.16  ?  225 CYS A SG    1 
ATOM   1775 N N     . MET A 1 226 ? 22.034  12.669  68.786 1.00 6.65  ?  226 MET A N     1 
ATOM   1776 C CA    . MET A 1 226 ? 22.077  13.566  67.640 1.00 12.49 ?  226 MET A CA    1 
ATOM   1777 C C     . MET A 1 226 ? 21.390  12.889  66.464 1.00 22.75 ?  226 MET A C     1 
ATOM   1778 O O     . MET A 1 226 ? 21.212  11.663  66.459 1.00 24.74 ?  226 MET A O     1 
ATOM   1779 C CB    . MET A 1 226 ? 23.516  13.909  67.241 1.00 21.67 ?  226 MET A CB    1 
ATOM   1780 C CG    . MET A 1 226 ? 24.150  14.931  68.141 1.00 32.90 ?  226 MET A CG    1 
ATOM   1781 S SD    . MET A 1 226 ? 25.941  14.952  68.058 1.00 21.10 ?  226 MET A SD    1 
ATOM   1782 C CE    . MET A 1 226 ? 26.264  14.004  66.584 1.00 5.54  ?  226 MET A CE    1 
ATOM   1783 N N     . ALA A 1 227 ? 20.948  13.697  65.516 1.00 4.90  ?  227 ALA A N     1 
ATOM   1784 C CA    . ALA A 1 227 ? 20.329  13.127  64.313 1.00 28.20 ?  227 ALA A CA    1 
ATOM   1785 C C     . ALA A 1 227 ? 20.342  14.075  63.112 1.00 32.98 ?  227 ALA A C     1 
ATOM   1786 O O     . ALA A 1 227 ? 20.622  15.204  63.371 1.00 37.15 ?  227 ALA A O     1 
ATOM   1787 C CB    . ALA A 1 227 ? 18.907  12.751  64.606 1.00 18.92 ?  227 ALA A CB    1 
ATOM   1788 N N     . PRO A 1 228 ? 20.311  13.650  61.817 1.00 23.66 ?  228 PRO A N     1 
ATOM   1789 C CA    . PRO A 1 228 ? 19.986  14.515  60.670 1.00 16.82 ?  228 PRO A CA    1 
ATOM   1790 C C     . PRO A 1 228 ? 18.499  14.621  60.383 1.00 20.98 ?  228 PRO A C     1 
ATOM   1791 O O     . PRO A 1 228 ? 18.109  15.359  59.467 1.00 37.58 ?  228 PRO A O     1 
ATOM   1792 C CB    . PRO A 1 228 ? 20.686  13.800  59.507 1.00 6.97  ?  228 PRO A CB    1 
ATOM   1793 C CG    . PRO A 1 228 ? 20.600  12.368  59.866 1.00 13.10 ?  228 PRO A CG    1 
ATOM   1794 C CD    . PRO A 1 228 ? 20.708  12.296  61.384 1.00 16.65 ?  228 PRO A CD    1 
ATOM   1795 N N     . SER A 1 229 ? 17.683  13.896  61.150 1.00 26.90 ?  229 SER A N     1 
ATOM   1796 C CA    . SER A 1 229 ? 16.269  13.756  60.825 1.00 31.99 ?  229 SER A CA    1 
ATOM   1797 C C     . SER A 1 229 ? 15.558  15.088  60.911 1.00 21.40 ?  229 SER A C     1 
ATOM   1798 O O     . SER A 1 229 ? 14.798  15.456  60.014 1.00 36.79 ?  229 SER A O     1 
ATOM   1799 C CB    . SER A 1 229 ? 15.609  12.738  61.759 1.00 33.58 ?  229 SER A CB    1 
ATOM   1800 O OG    . SER A 1 229 ? 16.258  11.476  61.709 1.00 37.33 ?  229 SER A OG    1 
HETATM 1801 N N1    . LLP A 1 230 ? 13.565  14.720  70.951 1.00 18.33 ?  230 LLP A N1    1 
HETATM 1802 C C2    . LLP A 1 230 ? 13.350  16.035  70.797 1.00 22.78 ?  230 LLP A C2    1 
HETATM 1803 C "C2'" . LLP A 1 230 ? 13.779  17.048  71.867 1.00 25.63 ?  230 LLP A "C2'" 1 
HETATM 1804 C C3    . LLP A 1 230 ? 12.722  16.489  69.628 1.00 17.30 ?  230 LLP A C3    1 
HETATM 1805 O O3    . LLP A 1 230 ? 12.461  17.813  69.382 1.00 6.83  ?  230 LLP A O3    1 
HETATM 1806 C C4    . LLP A 1 230 ? 12.336  15.584  68.637 1.00 24.71 ?  230 LLP A C4    1 
HETATM 1807 C "C4'" . LLP A 1 230 ? 11.633  16.256  67.398 1.00 18.81 ?  230 LLP A "C4'" 1 
HETATM 1808 C C5    . LLP A 1 230 ? 12.583  14.187  68.818 1.00 27.99 ?  230 LLP A C5    1 
HETATM 1809 C C6    . LLP A 1 230 ? 13.206  13.804  70.032 1.00 16.68 ?  230 LLP A C6    1 
HETATM 1810 C "C5'" . LLP A 1 230 ? 12.127  13.082  67.784 1.00 23.74 ?  230 LLP A "C5'" 1 
HETATM 1811 O OP4   . LLP A 1 230 ? 13.191  12.823  66.945 1.00 18.52 ?  230 LLP A OP4   1 
HETATM 1812 P P     . LLP A 1 230 ? 13.188  11.675  65.737 1.00 4.39  ?  230 LLP A P     1 
HETATM 1813 O OP1   . LLP A 1 230 ? 12.786  10.398  66.490 1.00 20.39 -1 230 LLP A OP1   1 
HETATM 1814 O OP2   . LLP A 1 230 ? 12.288  11.811  64.562 1.00 15.48 ?  230 LLP A OP2   1 
HETATM 1815 O OP3   . LLP A 1 230 ? 14.586  11.574  65.192 1.00 33.10 -1 230 LLP A OP3   1 
HETATM 1816 N N     . LLP A 1 230 ? 15.820  15.840  61.970 1.00 6.04  ?  230 LLP A N     1 
HETATM 1817 C CA    . LLP A 1 230 ? 15.220  17.161  62.071 1.00 11.74 ?  230 LLP A CA    1 
HETATM 1818 C CB    . LLP A 1 230 ? 15.199  17.630  63.529 1.00 11.27 ?  230 LLP A CB    1 
HETATM 1819 C CG    . LLP A 1 230 ? 14.169  16.920  64.397 1.00 25.34 ?  230 LLP A CG    1 
HETATM 1820 C CD    . LLP A 1 230 ? 12.721  17.344  64.091 1.00 12.08 ?  230 LLP A CD    1 
HETATM 1821 C CE    . LLP A 1 230 ? 11.763  16.696  65.076 1.00 5.56  ?  230 LLP A CE    1 
HETATM 1822 N NZ    . LLP A 1 230 ? 12.041  17.005  66.519 1.00 15.22 1  230 LLP A NZ    1 
HETATM 1823 C C     . LLP A 1 230 ? 15.965  18.169  61.210 1.00 22.52 ?  230 LLP A C     1 
HETATM 1824 O O     . LLP A 1 230 ? 15.337  18.993  60.542 1.00 22.87 ?  230 LLP A O     1 
ATOM   1825 N N     . THR A 1 231 ? 17.302  18.081  61.181 1.00 33.26 ?  231 THR A N     1 
ATOM   1826 C CA    . THR A 1 231 ? 18.113  19.073  60.474 1.00 37.23 ?  231 THR A CA    1 
ATOM   1827 C C     . THR A 1 231 ? 17.841  19.059  58.975 1.00 36.20 ?  231 THR A C     1 
ATOM   1828 O O     . THR A 1 231 ? 17.669  20.116  58.360 1.00 42.80 ?  231 THR A O     1 
ATOM   1829 C CB    . THR A 1 231 ? 19.605  18.821  60.722 1.00 39.72 ?  231 THR A CB    1 
ATOM   1830 O OG1   . THR A 1 231 ? 19.933  19.003  62.113 1.00 36.95 ?  231 THR A OG1   1 
ATOM   1831 C CG2   . THR A 1 231 ? 20.464  19.762  59.873 1.00 31.05 ?  231 THR A CG2   1 
ATOM   1832 N N     . PHE A 1 232 ? 17.781  17.876  58.372 1.00 30.76 ?  232 PHE A N     1 
ATOM   1833 C CA    . PHE A 1 232 ? 17.622  17.746  56.931 1.00 23.66 ?  232 PHE A CA    1 
ATOM   1834 C C     . PHE A 1 232 ? 16.216  17.306  56.538 1.00 28.16 ?  232 PHE A C     1 
ATOM   1835 O O     . PHE A 1 232 ? 15.955  17.092  55.350 1.00 29.51 ?  232 PHE A O     1 
ATOM   1836 C CB    . PHE A 1 232 ? 18.657  16.764  56.383 1.00 24.58 ?  232 PHE A CB    1 
ATOM   1837 C CG    . PHE A 1 232 ? 20.072  17.168  56.663 1.00 16.73 ?  232 PHE A CG    1 
ATOM   1838 C CD1   . PHE A 1 232 ? 20.755  17.986  55.790 1.00 17.81 ?  232 PHE A CD1   1 
ATOM   1839 C CD2   . PHE A 1 232 ? 20.709  16.744  57.800 1.00 13.42 ?  232 PHE A CD2   1 
ATOM   1840 C CE1   . PHE A 1 232 ? 22.041  18.365  56.048 1.00 11.13 ?  232 PHE A CE1   1 
ATOM   1841 C CE2   . PHE A 1 232 ? 22.011  17.121  58.062 1.00 10.64 ?  232 PHE A CE2   1 
ATOM   1842 C CZ    . PHE A 1 232 ? 22.669  17.929  57.193 1.00 13.08 ?  232 PHE A CZ    1 
ATOM   1843 N N     . ASN A 1 233 ? 15.301  17.197  57.504 1.00 22.66 ?  233 ASN A N     1 
ATOM   1844 C CA    . ASN A 1 233 ? 13.911  16.809  57.254 1.00 23.88 ?  233 ASN A CA    1 
ATOM   1845 C C     . ASN A 1 233 ? 13.820  15.408  56.648 1.00 24.53 ?  233 ASN A C     1 
ATOM   1846 O O     . ASN A 1 233 ? 13.188  15.195  55.612 1.00 25.39 ?  233 ASN A O     1 
ATOM   1847 C CB    . ASN A 1 233 ? 13.189  17.831  56.368 1.00 31.18 ?  233 ASN A CB    1 
ATOM   1848 C CG    . ASN A 1 233 ? 11.691  17.945  56.691 1.00 22.50 ?  233 ASN A CG    1 
ATOM   1849 O OD1   . ASN A 1 233 ? 11.295  17.914  57.851 1.00 19.30 ?  233 ASN A OD1   1 
ATOM   1850 N ND2   . ASN A 1 233 ? 10.861  18.042  55.655 1.00 13.50 ?  233 ASN A ND2   1 
ATOM   1851 N N     . ILE A 1 234 ? 14.478  14.443  57.293 1.00 24.58 ?  234 ILE A N     1 
ATOM   1852 C CA    . ILE A 1 234 ? 14.374  13.049  56.871 1.00 23.43 ?  234 ILE A CA    1 
ATOM   1853 C C     . ILE A 1 234 ? 13.936  12.199  58.066 1.00 20.48 ?  234 ILE A C     1 
ATOM   1854 O O     . ILE A 1 234 ? 14.352  11.047  58.215 1.00 20.14 ?  234 ILE A O     1 
ATOM   1855 C CB    . ILE A 1 234 ? 15.693  12.544  56.246 1.00 17.57 ?  234 ILE A CB    1 
ATOM   1856 C CG1   . ILE A 1 234 ? 16.826  12.518  57.253 1.00 13.40 ?  234 ILE A CG1   1 
ATOM   1857 C CG2   . ILE A 1 234 ? 16.144  13.457  55.137 1.00 16.58 ?  234 ILE A CG2   1 
ATOM   1858 C CD1   . ILE A 1 234 ? 17.928  11.592  56.849 1.00 9.05  ?  234 ILE A CD1   1 
ATOM   1859 N N     . ALA A 1 235 ? 13.065  12.764  58.912 1.00 21.99 ?  235 ALA A N     1 
ATOM   1860 C CA    . ALA A 1 235 ? 12.581  12.133  60.141 1.00 16.22 ?  235 ALA A CA    1 
ATOM   1861 C C     . ALA A 1 235 ? 11.699  10.903  59.919 1.00 24.03 ?  235 ALA A C     1 
ATOM   1862 O O     . ALA A 1 235 ? 11.429  10.188  60.890 1.00 30.64 ?  235 ALA A O     1 
ATOM   1863 C CB    . ALA A 1 235 ? 11.818  13.152  60.986 1.00 16.91 ?  235 ALA A CB    1 
ATOM   1864 N N     . GLY A 1 236 ? 11.192  10.672  58.710 1.00 14.62 ?  236 GLY A N     1 
ATOM   1865 C CA    . GLY A 1 236 ? 10.488  9.449   58.382 1.00 11.43 ?  236 GLY A CA    1 
ATOM   1866 C C     . GLY A 1 236 ? 11.362  8.292   57.968 1.00 23.06 ?  236 GLY A C     1 
ATOM   1867 O O     . GLY A 1 236 ? 10.855  7.194   57.680 1.00 6.26  ?  236 GLY A O     1 
ATOM   1868 N N     . LEU A 1 237 ? 12.673  8.539   57.866 1.00 23.66 ?  237 LEU A N     1 
ATOM   1869 C CA    . LEU A 1 237 ? 13.645  7.501   57.551 1.00 18.57 ?  237 LEU A CA    1 
ATOM   1870 C C     . LEU A 1 237 ? 14.297  6.897   58.790 1.00 24.81 ?  237 LEU A C     1 
ATOM   1871 O O     . LEU A 1 237 ? 14.912  5.829   58.688 1.00 28.30 ?  237 LEU A O     1 
ATOM   1872 C CB    . LEU A 1 237 ? 14.744  8.052   56.644 1.00 15.69 ?  237 LEU A CB    1 
ATOM   1873 C CG    . LEU A 1 237 ? 14.360  8.810   55.381 1.00 15.78 ?  237 LEU A CG    1 
ATOM   1874 C CD1   . LEU A 1 237 ? 15.545  8.806   54.409 1.00 12.30 ?  237 LEU A CD1   1 
ATOM   1875 C CD2   . LEU A 1 237 ? 13.100  8.255   54.747 1.00 7.93  ?  237 LEU A CD2   1 
ATOM   1876 N N     . GLN A 1 238 ? 14.173  7.552   59.945 1.00 13.18 ?  238 GLN A N     1 
ATOM   1877 C CA    . GLN A 1 238 ? 14.600  7.011   61.240 1.00 23.35 ?  238 GLN A CA    1 
ATOM   1878 C C     . GLN A 1 238 ? 16.114  6.740   61.311 1.00 32.76 ?  238 GLN A C     1 
ATOM   1879 O O     . GLN A 1 238 ? 16.560  5.608   61.505 1.00 49.11 ?  238 GLN A O     1 
ATOM   1880 C CB    . GLN A 1 238 ? 13.798  5.755   61.572 1.00 7.33  ?  238 GLN A CB    1 
ATOM   1881 C CG    . GLN A 1 238 ? 12.491  6.053   62.253 1.00 21.14 ?  238 GLN A CG    1 
ATOM   1882 C CD    . GLN A 1 238 ? 11.389  5.137   61.789 1.00 38.01 ?  238 GLN A CD    1 
ATOM   1883 O OE1   . GLN A 1 238 ? 11.597  3.939   61.595 1.00 42.84 ?  238 GLN A OE1   1 
ATOM   1884 N NE2   . GLN A 1 238 ? 10.196  5.697   61.616 1.00 50.31 ?  238 GLN A NE2   1 
ATOM   1885 N N     . ALA A 1 239 ? 16.904  7.805   61.153 1.00 43.38 ?  239 ALA A N     1 
ATOM   1886 C CA    . ALA A 1 239 ? 18.353  7.769   61.364 1.00 38.84 ?  239 ALA A CA    1 
ATOM   1887 C C     . ALA A 1 239 ? 18.713  8.579   62.606 1.00 28.11 ?  239 ALA A C     1 
ATOM   1888 O O     . ALA A 1 239 ? 18.252  9.718   62.757 1.00 40.09 ?  239 ALA A O     1 
ATOM   1889 C CB    . ALA A 1 239 ? 19.112  8.320   60.154 1.00 37.47 ?  239 ALA A CB    1 
ATOM   1890 N N     . SER A 1 240 ? 19.530  7.989   63.485 1.00 15.60 ?  240 SER A N     1 
ATOM   1891 C CA    . SER A 1 240 ? 19.987  8.623   64.719 1.00 17.57 ?  240 SER A CA    1 
ATOM   1892 C C     . SER A 1 240 ? 21.370  8.098   65.072 1.00 12.73 ?  240 SER A C     1 
ATOM   1893 O O     . SER A 1 240 ? 21.711  6.958   64.757 1.00 19.21 ?  240 SER A O     1 
ATOM   1894 C CB    . SER A 1 240 ? 19.025  8.372   65.888 1.00 15.39 ?  240 SER A CB    1 
ATOM   1895 O OG    . SER A 1 240 ? 18.084  9.414   66.002 1.00 32.38 ?  240 SER A OG    1 
ATOM   1896 N N     . ILE A 1 241 ? 22.145  8.930   65.765 1.00 21.14 ?  241 ILE A N     1 
ATOM   1897 C CA    . ILE A 1 241 ? 23.532  8.645   66.117 1.00 17.17 ?  241 ILE A CA    1 
ATOM   1898 C C     . ILE A 1 241 ? 23.712  8.902   67.604 1.00 21.43 ?  241 ILE A C     1 
ATOM   1899 O O     . ILE A 1 241 ? 23.477  10.024  68.068 1.00 11.96 ?  241 ILE A O     1 
ATOM   1900 C CB    . ILE A 1 241 ? 24.503  9.527   65.321 1.00 25.11 ?  241 ILE A CB    1 
ATOM   1901 C CG1   . ILE A 1 241 ? 24.344  9.253   63.841 1.00 30.46 ?  241 ILE A CG1   1 
ATOM   1902 C CG2   . ILE A 1 241 ? 25.934  9.270   65.725 1.00 41.93 ?  241 ILE A CG2   1 
ATOM   1903 C CD1   . ILE A 1 241 ? 24.410  7.813   63.553 1.00 28.85 ?  241 ILE A CD1   1 
ATOM   1904 N N     . ILE A 1 242 ? 24.141  7.884   68.351 1.00 4.26  ?  242 ILE A N     1 
ATOM   1905 C CA    . ILE A 1 242 ? 24.417  8.043   69.773 1.00 3.99  ?  242 ILE A CA    1 
ATOM   1906 C C     . ILE A 1 242 ? 25.912  7.903   70.015 1.00 24.54 ?  242 ILE A C     1 
ATOM   1907 O O     . ILE A 1 242 ? 26.535  6.930   69.577 1.00 32.64 ?  242 ILE A O     1 
ATOM   1908 C CB    . ILE A 1 242 ? 23.637  7.046   70.638 1.00 27.64 ?  242 ILE A CB    1 
ATOM   1909 C CG1   . ILE A 1 242 ? 22.222  6.885   70.093 1.00 29.05 ?  242 ILE A CG1   1 
ATOM   1910 C CG2   . ILE A 1 242 ? 23.626  7.538   72.076 1.00 15.61 ?  242 ILE A CG2   1 
ATOM   1911 C CD1   . ILE A 1 242 ? 21.414  8.145   70.148 1.00 29.76 ?  242 ILE A CD1   1 
ATOM   1912 N N     . ILE A 1 243 ? 26.478  8.878   70.719 1.00 14.98 ?  243 ILE A N     1 
ATOM   1913 C CA    . ILE A 1 243 ? 27.886  8.908   71.069 1.00 4.39  ?  243 ILE A CA    1 
ATOM   1914 C C     . ILE A 1 243 ? 27.982  8.698   72.581 1.00 16.08 ?  243 ILE A C     1 
ATOM   1915 O O     . ILE A 1 243 ? 27.252  9.341   73.349 1.00 3.84  ?  243 ILE A O     1 
ATOM   1916 C CB    . ILE A 1 243 ? 28.548  10.209  70.600 1.00 4.69  ?  243 ILE A CB    1 
ATOM   1917 C CG1   . ILE A 1 243 ? 28.432  10.320  69.078 1.00 8.75  ?  243 ILE A CG1   1 
ATOM   1918 C CG2   . ILE A 1 243 ? 30.013  10.284  71.031 1.00 4.88  ?  243 ILE A CG2   1 
ATOM   1919 C CD1   . ILE A 1 243 ? 28.416  11.732  68.603 1.00 5.23  ?  243 ILE A CD1   1 
ATOM   1920 N N     . ILE A 1 244 ? 28.765  7.693   72.992 1.00 19.70 ?  244 ILE A N     1 
ATOM   1921 C CA    . ILE A 1 244 ? 28.976  7.333   74.399 1.00 16.55 ?  244 ILE A CA    1 
ATOM   1922 C C     . ILE A 1 244 ? 30.462  7.114   74.674 1.00 26.40 ?  244 ILE A C     1 
ATOM   1923 O O     . ILE A 1 244 ? 30.950  5.989   74.507 1.00 32.11 ?  244 ILE A O     1 
ATOM   1924 C CB    . ILE A 1 244 ? 28.198  6.062   74.785 1.00 4.73  ?  244 ILE A CB    1 
ATOM   1925 C CG1   . ILE A 1 244 ? 26.792  6.051   74.177 1.00 16.38 ?  244 ILE A CG1   1 
ATOM   1926 C CG2   . ILE A 1 244 ? 28.154  5.914   76.292 1.00 3.40  ?  244 ILE A CG2   1 
ATOM   1927 C CD1   . ILE A 1 244 ? 25.882  4.930   74.695 1.00 18.75 ?  244 ILE A CD1   1 
ATOM   1928 N N     . PRO A 1 245 ? 31.211  8.119   75.135 1.00 25.88 ?  245 PRO A N     1 
ATOM   1929 C CA    . PRO A 1 245 ? 32.659  7.896   75.397 1.00 28.82 ?  245 PRO A CA    1 
ATOM   1930 C C     . PRO A 1 245 ? 33.006  6.874   76.490 1.00 4.26  ?  245 PRO A C     1 
ATOM   1931 O O     . PRO A 1 245 ? 33.961  6.119   76.315 1.00 7.67  ?  245 PRO A O     1 
ATOM   1932 C CB    . PRO A 1 245 ? 33.146  9.303   75.779 1.00 21.71 ?  245 PRO A CB    1 
ATOM   1933 C CG    . PRO A 1 245 ? 32.186  10.215  75.134 1.00 26.77 ?  245 PRO A CG    1 
ATOM   1934 C CD    . PRO A 1 245 ? 30.860  9.550   75.116 1.00 15.90 ?  245 PRO A CD    1 
ATOM   1935 N N     . ASN A 1 246 ? 32.362  6.855   77.658 1.00 3.95  ?  246 ASN A N     1 
ATOM   1936 C CA    . ASN A 1 246 ? 32.574  5.877   78.768 1.00 18.16 ?  246 ASN A CA    1 
ATOM   1937 C C     . ASN A 1 246 ? 32.233  4.449   78.299 1.00 23.05 ?  246 ASN A C     1 
ATOM   1938 O O     . ASN A 1 246 ? 31.077  4.214   78.013 1.00 39.51 ?  246 ASN A O     1 
ATOM   1939 C CB    . ASN A 1 246 ? 31.854  6.313   80.044 1.00 3.52  ?  246 ASN A CB    1 
ATOM   1940 C CG    . ASN A 1 246 ? 32.019  5.524   81.313 1.00 3.42  ?  246 ASN A CG    1 
ATOM   1941 O OD1   . ASN A 1 246 ? 31.668  4.366   81.381 1.00 6.68  ?  246 ASN A OD1   1 
ATOM   1942 N ND2   . ASN A 1 246 ? 32.438  6.186   82.367 1.00 21.71 ?  246 ASN A ND2   1 
ATOM   1943 N N     . GLU A 1 247 ? 33.208  3.548   78.234 1.00 11.90 ?  247 GLU A N     1 
ATOM   1944 C CA    . GLU A 1 247 ? 33.022  2.180   77.719 1.00 13.44 ?  247 GLU A CA    1 
ATOM   1945 C C     . GLU A 1 247 ? 31.955  1.411   78.484 1.00 3.67  ?  247 GLU A C     1 
ATOM   1946 O O     . GLU A 1 247 ? 31.105  0.750   77.882 1.00 25.05 ?  247 GLU A O     1 
ATOM   1947 C CB    . GLU A 1 247 ? 34.330  1.395   77.784 1.00 11.19 ?  247 GLU A CB    1 
ATOM   1948 C CG    . GLU A 1 247 ? 34.069  -0.072  77.605 1.00 14.31 ?  247 GLU A CG    1 
ATOM   1949 C CD    . GLU A 1 247 ? 35.295  -0.901  77.361 1.00 11.28 ?  247 GLU A CD    1 
ATOM   1950 O OE1   . GLU A 1 247 ? 35.446  -1.389  76.222 1.00 10.86 ?  247 GLU A OE1   1 
ATOM   1951 O OE2   . GLU A 1 247 ? 36.075  -1.101  78.307 1.00 8.60  -1 247 GLU A OE2   1 
ATOM   1952 N N     . LYS A 1 248 ? 31.971  1.526   79.811 1.00 10.48 ?  248 LYS A N     1 
ATOM   1953 C CA    . LYS A 1 248 ? 31.022  0.839   80.676 1.00 3.27  ?  248 LYS A CA    1 
ATOM   1954 C C     . LYS A 1 248 ? 29.599  1.347   80.447 1.00 25.03 ?  248 LYS A C     1 
ATOM   1955 O O     . LYS A 1 248 ? 28.637  0.569   80.512 1.00 19.49 ?  248 LYS A O     1 
ATOM   1956 C CB    . LYS A 1 248 ? 31.450  1.060   82.123 1.00 3.19  ?  248 LYS A CB    1 
ATOM   1957 C CG    . LYS A 1 248 ? 30.970  0.115   83.139 1.00 3.03  ?  248 LYS A CG    1 
ATOM   1958 C CD    . LYS A 1 248 ? 31.404  0.567   84.519 1.00 2.98  ?  248 LYS A CD    1 
ATOM   1959 C CE    . LYS A 1 248 ? 30.370  1.475   85.124 1.00 8.60  ?  248 LYS A CE    1 
ATOM   1960 N NZ    . LYS A 1 248 ? 30.336  1.384   86.601 1.00 14.00 1  248 LYS A NZ    1 
ATOM   1961 N N     . LEU A 1 249 ? 29.438  2.649   80.167 1.00 24.00 ?  249 LEU A N     1 
ATOM   1962 C CA    . LEU A 1 249 ? 28.107  3.146   79.816 1.00 9.87  ?  249 LEU A CA    1 
ATOM   1963 C C     . LEU A 1 249 ? 27.713  2.730   78.408 1.00 8.01  ?  249 LEU A C     1 
ATOM   1964 O O     . LEU A 1 249 ? 26.542  2.417   78.176 1.00 10.47 ?  249 LEU A O     1 
ATOM   1965 C CB    . LEU A 1 249 ? 28.020  4.677   79.940 1.00 2.90  ?  249 LEU A CB    1 
ATOM   1966 C CG    . LEU A 1 249 ? 28.118  5.376   81.296 1.00 2.77  ?  249 LEU A CG    1 
ATOM   1967 C CD1   . LEU A 1 249 ? 27.761  6.826   81.106 1.00 43.22 ?  249 LEU A CD1   1 
ATOM   1968 C CD2   . LEU A 1 249 ? 27.283  4.813   82.413 1.00 2.54  ?  249 LEU A CD2   1 
ATOM   1969 N N     . ARG A 1 250 ? 28.642  2.698   77.453 1.00 3.27  ?  250 ARG A N     1 
ATOM   1970 C CA    . ARG A 1 250 ? 28.212  2.331   76.103 1.00 18.03 ?  250 ARG A CA    1 
ATOM   1971 C C     . ARG A 1 250 ? 27.692  0.898   76.050 1.00 26.74 ?  250 ARG A C     1 
ATOM   1972 O O     . ARG A 1 250 ? 26.720  0.611   75.341 1.00 39.40 ?  250 ARG A O     1 
ATOM   1973 C CB    . ARG A 1 250 ? 29.334  2.504   75.092 1.00 17.72 ?  250 ARG A CB    1 
ATOM   1974 C CG    . ARG A 1 250 ? 28.881  2.366   73.638 1.00 12.18 ?  250 ARG A CG    1 
ATOM   1975 C CD    . ARG A 1 250 ? 29.858  3.083   72.738 1.00 13.39 ?  250 ARG A CD    1 
ATOM   1976 N NE    . ARG A 1 250 ? 31.213  2.526   72.765 1.00 24.51 ?  250 ARG A NE    1 
ATOM   1977 C CZ    . ARG A 1 250 ? 32.223  2.995   73.498 1.00 20.98 ?  250 ARG A CZ    1 
ATOM   1978 N NH1   . ARG A 1 250 ? 32.050  4.021   74.313 1.00 21.30 1  250 ARG A NH1   1 
ATOM   1979 N NH2   . ARG A 1 250 ? 33.418  2.428   73.420 1.00 23.23 ?  250 ARG A NH2   1 
ATOM   1980 N N     . HIS A 1 251 ? 28.317  -0.012  76.796 1.00 24.55 ?  251 HIS A N     1 
ATOM   1981 C CA    . HIS A 1 251 ? 27.956  -1.420  76.687 1.00 24.23 ?  251 HIS A CA    1 
ATOM   1982 C C     . HIS A 1 251 ? 26.602  -1.727  77.332 1.00 14.55 ?  251 HIS A C     1 
ATOM   1983 O O     . HIS A 1 251 ? 25.805  -2.478  76.760 1.00 2.99  ?  251 HIS A O     1 
ATOM   1984 C CB    . HIS A 1 251 ? 29.082  -2.266  77.283 1.00 23.62 ?  251 HIS A CB    1 
ATOM   1985 C CG    . HIS A 1 251 ? 30.353  -2.234  76.478 1.00 16.78 ?  251 HIS A CG    1 
ATOM   1986 N ND1   . HIS A 1 251 ? 30.440  -1.612  75.248 1.00 11.38 ?  251 HIS A ND1   1 
ATOM   1987 C CD2   . HIS A 1 251 ? 31.577  -2.765  76.720 1.00 3.87  ?  251 HIS A CD2   1 
ATOM   1988 C CE1   . HIS A 1 251 ? 31.663  -1.759  74.770 1.00 13.23 ?  251 HIS A CE1   1 
ATOM   1989 N NE2   . HIS A 1 251 ? 32.371  -2.456  75.643 1.00 4.09  ?  251 HIS A NE2   1 
ATOM   1990 N N     . ALA A 1 252 ? 26.283  -1.078  78.462 1.00 2.85  ?  252 ALA A N     1 
ATOM   1991 C CA    . ALA A 1 252 ? 24.995  -1.286  79.115 1.00 2.64  ?  252 ALA A CA    1 
ATOM   1992 C C     . ALA A 1 252 ? 23.849  -0.675  78.316 1.00 9.49  ?  252 ALA A C     1 
ATOM   1993 O O     . ALA A 1 252 ? 22.717  -1.149  78.414 1.00 34.88 ?  252 ALA A O     1 
ATOM   1994 C CB    . ALA A 1 252 ? 25.004  -0.710  80.527 1.00 2.51  ?  252 ALA A CB    1 
ATOM   1995 N N     . PHE A 1 253 ? 24.100  0.396   77.568 1.00 4.03  ?  253 PHE A N     1 
ATOM   1996 C CA    . PHE A 1 253 ? 23.101  0.905   76.633 1.00 13.98 ?  253 PHE A CA    1 
ATOM   1997 C C     . PHE A 1 253 ? 22.873  -0.069  75.489 1.00 22.86 ?  253 PHE A C     1 
ATOM   1998 O O     . PHE A 1 253 ? 21.726  -0.399  75.161 1.00 32.60 ?  253 PHE A O     1 
ATOM   1999 C CB    . PHE A 1 253 ? 23.537  2.262   76.088 1.00 10.33 ?  253 PHE A CB    1 
ATOM   2000 C CG    . PHE A 1 253 ? 22.629  2.841   75.015 1.00 2.71  ?  253 PHE A CG    1 
ATOM   2001 C CD1   . PHE A 1 253 ? 22.792  2.515   73.675 1.00 2.90  ?  253 PHE A CD1   1 
ATOM   2002 C CD2   . PHE A 1 253 ? 21.665  3.789   75.347 1.00 19.02 ?  253 PHE A CD2   1 
ATOM   2003 C CE1   . PHE A 1 253 ? 21.987  3.082   72.692 1.00 2.93  ?  253 PHE A CE1   1 
ATOM   2004 C CE2   . PHE A 1 253 ? 20.866  4.350   74.372 1.00 2.56  ?  253 PHE A CE2   1 
ATOM   2005 C CZ    . PHE A 1 253 ? 21.021  4.003   73.057 1.00 2.75  ?  253 PHE A CZ    1 
ATOM   2006 N N     . THR A 1 254 ? 23.957  -0.525  74.856 1.00 20.86 ?  254 THR A N     1 
ATOM   2007 C CA    . THR A 1 254 ? 23.850  -1.476  73.747 1.00 27.54 ?  254 THR A CA    1 
ATOM   2008 C C     . THR A 1 254 ? 23.316  -2.838  74.211 1.00 7.90  ?  254 THR A C     1 
ATOM   2009 O O     . THR A 1 254 ? 22.832  -3.616  73.398 1.00 3.01  ?  254 THR A O     1 
ATOM   2010 C CB    . THR A 1 254 ? 25.222  -1.655  73.066 1.00 29.10 ?  254 THR A CB    1 
ATOM   2011 O OG1   . THR A 1 254 ? 26.184  -2.068  74.046 1.00 18.38 ?  254 THR A OG1   1 
ATOM   2012 C CG2   . THR A 1 254 ? 25.700  -0.346  72.389 1.00 3.50  ?  254 THR A CG2   1 
ATOM   2013 N N     . ALA A 1 255 ? 23.443  -3.136  75.500 1.00 2.85  ?  255 ALA A N     1 
ATOM   2014 C CA    . ALA A 1 255 ? 22.874  -4.334  76.069 1.00 2.78  ?  255 ALA A CA    1 
ATOM   2015 C C     . ALA A 1 255 ? 21.362  -4.301  76.021 1.00 40.43 ?  255 ALA A C     1 
ATOM   2016 O O     . ALA A 1 255 ? 20.713  -5.298  75.681 1.00 36.43 ?  255 ALA A O     1 
ATOM   2017 C CB    . ALA A 1 255 ? 23.347  -4.466  77.510 1.00 15.06 ?  255 ALA A CB    1 
ATOM   2018 N N     . ILE A 1 256 ? 20.789  -3.141  76.332 1.00 66.31 ?  256 ILE A N     1 
ATOM   2019 C CA    . ILE A 1 256 ? 19.345  -2.959  76.348 1.00 2.38  ?  256 ILE A CA    1 
ATOM   2020 C C     . ILE A 1 256 ? 18.778  -2.995  74.940 1.00 12.58 ?  256 ILE A C     1 
ATOM   2021 O O     . ILE A 1 256 ? 17.681  -3.521  74.710 1.00 40.55 ?  256 ILE A O     1 
ATOM   2022 C CB    . ILE A 1 256 ? 19.034  -1.650  77.069 1.00 2.24  ?  256 ILE A CB    1 
ATOM   2023 C CG1   . ILE A 1 256 ? 19.705  -1.715  78.433 1.00 2.20  ?  256 ILE A CG1   1 
ATOM   2024 C CG2   . ILE A 1 256 ? 17.515  -1.406  77.182 1.00 2.12  ?  256 ILE A CG2   1 
ATOM   2025 C CD1   . ILE A 1 256 ? 19.396  -2.984  79.192 1.00 2.20  ?  256 ILE A CD1   1 
ATOM   2026 N N     . GLN A 1 257 ? 19.472  -2.379  73.989 1.00 2.56  ?  257 GLN A N     1 
ATOM   2027 C CA    . GLN A 1 257 ? 19.053  -2.499  72.603 1.00 2.66  ?  257 GLN A CA    1 
ATOM   2028 C C     . GLN A 1 257 ? 19.024  -3.959  72.183 1.00 4.73  ?  257 GLN A C     1 
ATOM   2029 O O     . GLN A 1 257 ? 18.134  -4.378  71.439 1.00 26.63 ?  257 GLN A O     1 
ATOM   2030 C CB    . GLN A 1 257 ? 19.976  -1.720  71.679 1.00 23.08 ?  257 GLN A CB    1 
ATOM   2031 C CG    . GLN A 1 257 ? 20.059  -0.249  71.899 1.00 16.02 ?  257 GLN A CG    1 
ATOM   2032 C CD    . GLN A 1 257 ? 21.017  0.346   70.918 1.00 21.37 ?  257 GLN A CD    1 
ATOM   2033 O OE1   . GLN A 1 257 ? 22.188  -0.054  70.860 1.00 18.88 ?  257 GLN A OE1   1 
ATOM   2034 N NE2   . GLN A 1 257 ? 20.532  1.289   70.115 1.00 20.82 ?  257 GLN A NE2   1 
ATOM   2035 N N     . TYR A 1 258 ? 20.036  -4.726  72.575 1.00 2.84  ?  258 TYR A N     1 
ATOM   2036 C CA    . TYR A 1 258 ? 20.139  -6.108  72.124 1.00 9.94  ?  258 TYR A CA    1 
ATOM   2037 C C     . TYR A 1 258 ? 18.996  -6.960  72.688 1.00 2.86  ?  258 TYR A C     1 
ATOM   2038 O O     . TYR A 1 258 ? 18.350  -7.705  71.952 1.00 2.92  ?  258 TYR A O     1 
ATOM   2039 C CB    . TYR A 1 258 ? 21.515  -6.670  72.508 1.00 8.00  ?  258 TYR A CB    1 
ATOM   2040 C CG    . TYR A 1 258 ? 21.757  -8.028  71.955 1.00 3.21  ?  258 TYR A CG    1 
ATOM   2041 C CD1   . TYR A 1 258 ? 22.085  -8.205  70.620 1.00 15.19 ?  258 TYR A CD1   1 
ATOM   2042 C CD2   . TYR A 1 258 ? 21.608  -9.138  72.742 1.00 3.18  ?  258 TYR A CD2   1 
ATOM   2043 C CE1   . TYR A 1 258 ? 22.279  -9.456  70.090 1.00 8.46  ?  258 TYR A CE1   1 
ATOM   2044 C CE2   . TYR A 1 258 ? 21.793  -10.403 72.224 1.00 7.10  ?  258 TYR A CE2   1 
ATOM   2045 C CZ    . TYR A 1 258 ? 22.135  -10.553 70.902 1.00 16.07 ?  258 TYR A CZ    1 
ATOM   2046 O OH    . TYR A 1 258 ? 22.329  -11.806 70.392 1.00 29.51 ?  258 TYR A OH    1 
ATOM   2047 N N     . ARG A 1 259 ? 18.713  -6.830  73.979 1.00 2.74  ?  259 ARG A N     1 
ATOM   2048 C CA    . ARG A 1 259 ? 17.594  -7.500  74.620 1.00 2.77  ?  259 ARG A CA    1 
ATOM   2049 C C     . ARG A 1 259 ? 16.220  -7.059  74.094 1.00 11.06 ?  259 ARG A C     1 
ATOM   2050 O O     . ARG A 1 259 ? 15.215  -7.645  74.512 1.00 10.32 ?  259 ARG A O     1 
ATOM   2051 C CB    . ARG A 1 259 ? 17.669  -7.262  76.141 1.00 2.58  ?  259 ARG A CB    1 
ATOM   2052 C CG    . ARG A 1 259 ? 17.375  -5.793  76.507 1.00 2.44  ?  259 ARG A CG    1 
ATOM   2053 C CD    . ARG A 1 259 ? 16.633  -5.540  77.806 1.00 2.33  ?  259 ARG A CD    1 
ATOM   2054 N NE    . ARG A 1 259 ? 17.446  -5.744  78.984 1.00 2.31  ?  259 ARG A NE    1 
ATOM   2055 C CZ    . ARG A 1 259 ? 17.131  -5.306  80.194 1.00 11.84 ?  259 ARG A CZ    1 
ATOM   2056 N NH1   . ARG A 1 259 ? 16.001  -4.645  80.391 1.00 18.32 1  259 ARG A NH1   1 
ATOM   2057 N NH2   . ARG A 1 259 ? 17.937  -5.544  81.207 1.00 8.96  ?  259 ARG A NH2   1 
ATOM   2058 N N     . GLN A 1 260 ? 16.123  -5.986  73.309 1.00 2.80  ?  260 GLN A N     1 
ATOM   2059 C CA    . GLN A 1 260 ? 14.852  -5.617  72.686 1.00 16.77 ?  260 GLN A CA    1 
ATOM   2060 C C     . GLN A 1 260 ? 14.911  -5.751  71.165 1.00 28.89 ?  260 GLN A C     1 
ATOM   2061 O O     . GLN A 1 260 ? 14.158  -5.064  70.463 1.00 27.59 ?  260 GLN A O     1 
ATOM   2062 C CB    . GLN A 1 260 ? 14.382  -4.220  73.103 1.00 9.94  ?  260 GLN A CB    1 
ATOM   2063 C CG    . GLN A 1 260 ? 14.273  -3.967  74.642 1.00 26.23 ?  260 GLN A CG    1 
ATOM   2064 C CD    . GLN A 1 260 ? 14.296  -2.477  75.033 1.00 33.46 ?  260 GLN A CD    1 
ATOM   2065 O OE1   . GLN A 1 260 ? 14.268  -1.616  74.160 1.00 2.11  ?  260 GLN A OE1   1 
ATOM   2066 N NE2   . GLN A 1 260 ? 14.363  -2.177  76.334 1.00 2.19  ?  260 GLN A NE2   1 
ATOM   2067 N N     . GLY A 1 261 ? 15.864  -6.550  70.650 1.00 12.54 ?  261 GLY A N     1 
ATOM   2068 C CA    . GLY A 1 261 ? 15.924  -7.014  69.269 1.00 2.97  ?  261 GLY A CA    1 
ATOM   2069 C C     . GLY A 1 261 ? 16.467  -6.054  68.231 1.00 17.82 ?  261 GLY A C     1 
ATOM   2070 O O     . GLY A 1 261 ? 16.480  -6.396  67.040 1.00 13.80 ?  261 GLY A O     1 
ATOM   2071 N N     . PHE A 1 262 ? 16.947  -4.876  68.639 1.00 26.24 ?  262 PHE A N     1 
ATOM   2072 C CA    . PHE A 1 262 ? 17.536  -3.872  67.717 1.00 28.13 ?  262 PHE A CA    1 
ATOM   2073 C C     . PHE A 1 262 ? 18.909  -4.270  67.205 1.00 31.20 ?  262 PHE A C     1 
ATOM   2074 O O     . PHE A 1 262 ? 19.762  -4.516  68.071 1.00 27.47 ?  262 PHE A O     1 
ATOM   2075 C CB    . PHE A 1 262 ? 17.723  -2.522  68.395 1.00 37.95 ?  262 PHE A CB    1 
ATOM   2076 C CG    . PHE A 1 262 ? 18.262  -1.432  67.513 1.00 29.44 ?  262 PHE A CG    1 
ATOM   2077 C CD1   . PHE A 1 262 ? 17.455  -0.824  66.573 1.00 27.95 ?  262 PHE A CD1   1 
ATOM   2078 C CD2   . PHE A 1 262 ? 19.570  -1.006  67.642 1.00 27.71 ?  262 PHE A CD2   1 
ATOM   2079 C CE1   . PHE A 1 262 ? 17.952  0.187   65.773 1.00 33.68 ?  262 PHE A CE1   1 
ATOM   2080 C CE2   . PHE A 1 262 ? 20.068  -0.004  66.835 1.00 31.84 ?  262 PHE A CE2   1 
ATOM   2081 C CZ    . PHE A 1 262 ? 19.254  0.593   65.912 1.00 35.54 ?  262 PHE A CZ    1 
ATOM   2082 N N     . HIS A 1 263 ? 19.092  -4.274  65.871 1.00 39.29 ?  263 HIS A N     1 
ATOM   2083 C CA    . HIS A 1 263 ? 20.358  -4.669  65.253 1.00 32.64 ?  263 HIS A CA    1 
ATOM   2084 C C     . HIS A 1 263 ? 20.830  -3.646  64.229 1.00 34.34 ?  263 HIS A C     1 
ATOM   2085 O O     . HIS A 1 263 ? 21.575  -3.997  63.306 1.00 33.63 ?  263 HIS A O     1 
ATOM   2086 C CB    . HIS A 1 263 ? 20.261  -6.056  64.605 1.00 35.60 ?  263 HIS A CB    1 
ATOM   2087 C CG    . HIS A 1 263 ? 19.851  -7.131  65.563 1.00 38.34 ?  263 HIS A CG    1 
ATOM   2088 N ND1   . HIS A 1 263 ? 20.131  -7.066  66.913 1.00 41.38 ?  263 HIS A ND1   1 
ATOM   2089 C CD2   . HIS A 1 263 ? 19.163  -8.281  65.377 1.00 39.01 ?  263 HIS A CD2   1 
ATOM   2090 C CE1   . HIS A 1 263 ? 19.635  -8.130  67.516 1.00 36.69 ?  263 HIS A CE1   1 
ATOM   2091 N NE2   . HIS A 1 263 ? 19.047  -8.886  66.606 1.00 44.14 ?  263 HIS A NE2   1 
ATOM   2092 N N     . GLY A 1 264 ? 20.423  -2.395  64.371 1.00 25.30 ?  264 GLY A N     1 
ATOM   2093 C CA    . GLY A 1 264 ? 20.778  -1.366  63.416 1.00 13.79 ?  264 GLY A CA    1 
ATOM   2094 C C     . GLY A 1 264 ? 19.569  -0.863  62.654 1.00 10.25 ?  264 GLY A C     1 
ATOM   2095 O O     . GLY A 1 264 ? 18.427  -1.261  62.892 1.00 44.46 ?  264 GLY A O     1 
ATOM   2096 N N     . LEU A 1 265 ? 19.862  0.029   61.715 1.00 12.89 ?  265 LEU A N     1 
ATOM   2097 C CA    . LEU A 1 265 ? 18.881  0.840   61.004 1.00 9.29  ?  265 LEU A CA    1 
ATOM   2098 C C     . LEU A 1 265 ? 18.587  0.279   59.615 1.00 17.70 ?  265 LEU A C     1 
ATOM   2099 O O     . LEU A 1 265 ? 19.228  -0.660  59.139 1.00 28.86 ?  265 LEU A O     1 
ATOM   2100 C CB    . LEU A 1 265 ? 19.363  2.294   60.880 1.00 22.78 ?  265 LEU A CB    1 
ATOM   2101 C CG    . LEU A 1 265 ? 19.855  3.107   62.075 1.00 4.99  ?  265 LEU A CG    1 
ATOM   2102 C CD1   . LEU A 1 265 ? 19.738  4.588   61.765 1.00 9.48  ?  265 LEU A CD1   1 
ATOM   2103 C CD2   . LEU A 1 265 ? 19.129  2.759   63.353 1.00 28.89 ?  265 LEU A CD2   1 
ATOM   2104 N N     . ASN A 1 266 ? 17.670  0.950   58.973 1.00 5.70  ?  266 ASN A N     1 
ATOM   2105 C CA    . ASN A 1 266 ? 17.190  0.552   57.650 1.00 9.10  ?  266 ASN A CA    1 
ATOM   2106 C C     . ASN A 1 266 ? 18.113  1.033   56.543 1.00 22.01 ?  266 ASN A C     1 
ATOM   2107 O O     . ASN A 1 266 ? 18.899  1.947   56.769 1.00 23.61 ?  266 ASN A O     1 
ATOM   2108 C CB    . ASN A 1 266 ? 15.743  1.038   57.526 1.00 19.88 ?  266 ASN A CB    1 
ATOM   2109 C CG    . ASN A 1 266 ? 15.485  2.491   57.871 1.00 16.50 ?  266 ASN A CG    1 
ATOM   2110 O OD1   . ASN A 1 266 ? 15.547  2.893   59.028 1.00 8.53  ?  266 ASN A OD1   1 
ATOM   2111 N ND2   . ASN A 1 266 ? 15.136  3.277   56.874 1.00 5.81  ?  266 ASN A ND2   1 
ATOM   2112 N N     . ILE A 1 267 ? 17.907  0.521   55.346 1.00 22.92 ?  267 ILE A N     1 
ATOM   2113 C CA    . ILE A 1 267 ? 18.832  0.779   54.239 1.00 31.51 ?  267 ILE A CA    1 
ATOM   2114 C C     . ILE A 1 267 ? 18.965  2.263   53.922 1.00 28.33 ?  267 ILE A C     1 
ATOM   2115 O O     . ILE A 1 267 ? 20.070  2.759   53.674 1.00 34.01 ?  267 ILE A O     1 
ATOM   2116 C CB    . ILE A 1 267 ? 18.388  -0.016  52.998 1.00 30.94 ?  267 ILE A CB    1 
ATOM   2117 C CG1   . ILE A 1 267 ? 18.727  -1.495  53.200 1.00 38.15 ?  267 ILE A CG1   1 
ATOM   2118 C CG2   . ILE A 1 267 ? 19.057  0.544   51.755 1.00 27.86 ?  267 ILE A CG2   1 
ATOM   2119 C CD1   . ILE A 1 267 ? 18.068  -2.420  52.250 1.00 41.72 ?  267 ILE A CD1   1 
ATOM   2120 N N     . PHE A 1 268 ? 17.840  2.980   53.860 1.00 37.88 ?  268 PHE A N     1 
ATOM   2121 C CA    . PHE A 1 268 ? 17.828  4.377   53.428 1.00 36.91 ?  268 PHE A CA    1 
ATOM   2122 C C     . PHE A 1 268 ? 18.156  5.357   54.556 1.00 18.90 ?  268 PHE A C     1 
ATOM   2123 O O     . PHE A 1 268 ? 18.570  6.483   54.275 1.00 21.99 ?  268 PHE A O     1 
ATOM   2124 C CB    . PHE A 1 268 ? 16.475  4.690   52.781 1.00 28.21 ?  268 PHE A CB    1 
ATOM   2125 C CG    . PHE A 1 268 ? 16.123  3.761   51.622 1.00 20.56 ?  268 PHE A CG    1 
ATOM   2126 C CD1   . PHE A 1 268 ? 16.678  3.940   50.375 1.00 10.19 ?  268 PHE A CD1   1 
ATOM   2127 C CD2   . PHE A 1 268 ? 15.236  2.721   51.790 1.00 12.35 ?  268 PHE A CD2   1 
ATOM   2128 C CE1   . PHE A 1 268 ? 16.355  3.099   49.331 1.00 13.10 ?  268 PHE A CE1   1 
ATOM   2129 C CE2   . PHE A 1 268 ? 14.916  1.882   50.749 1.00 15.19 ?  268 PHE A CE2   1 
ATOM   2130 C CZ    . PHE A 1 268 ? 15.474  2.069   49.521 1.00 12.99 ?  268 PHE A CZ    1 
ATOM   2131 N N     . ALA A 1 269 ? 17.970  4.952   55.816 1.00 22.47 ?  269 ALA A N     1 
ATOM   2132 C CA    . ALA A 1 269 ? 18.444  5.745   56.947 1.00 23.49 ?  269 ALA A CA    1 
ATOM   2133 C C     . ALA A 1 269 ? 19.961  5.873   56.930 1.00 20.45 ?  269 ALA A C     1 
ATOM   2134 O O     . ALA A 1 269 ? 20.504  6.947   57.202 1.00 18.24 ?  269 ALA A O     1 
ATOM   2135 C CB    . ALA A 1 269 ? 17.982  5.111   58.261 1.00 30.88 ?  269 ALA A CB    1 
ATOM   2136 N N     . TYR A 1 270 ? 20.671  4.780   56.643 1.00 20.15 ?  270 TYR A N     1 
ATOM   2137 C CA    . TYR A 1 270 ? 22.105  4.911   56.452 1.00 15.58 ?  270 TYR A CA    1 
ATOM   2138 C C     . TYR A 1 270 ? 22.383  5.749   55.212 1.00 22.54 ?  270 TYR A C     1 
ATOM   2139 O O     . TYR A 1 270 ? 23.202  6.673   55.249 1.00 32.60 ?  270 TYR A O     1 
ATOM   2140 C CB    . TYR A 1 270 ? 22.780  3.536   56.299 1.00 19.76 ?  270 TYR A CB    1 
ATOM   2141 C CG    . TYR A 1 270 ? 22.839  2.661   57.539 1.00 7.26  ?  270 TYR A CG    1 
ATOM   2142 C CD1   . TYR A 1 270 ? 23.237  3.160   58.759 1.00 6.74  ?  270 TYR A CD1   1 
ATOM   2143 C CD2   . TYR A 1 270 ? 22.485  1.336   57.475 1.00 7.01  ?  270 TYR A CD2   1 
ATOM   2144 C CE1   . TYR A 1 270 ? 23.270  2.357   59.884 1.00 6.26  ?  270 TYR A CE1   1 
ATOM   2145 C CE2   . TYR A 1 270 ? 22.509  0.537   58.579 1.00 6.51  ?  270 TYR A CE2   1 
ATOM   2146 C CZ    . TYR A 1 270 ? 22.909  1.036   59.781 1.00 6.15  ?  270 TYR A CZ    1 
ATOM   2147 O OH    . TYR A 1 270 ? 22.930  0.189   60.870 1.00 8.59  ?  270 TYR A OH    1 
ATOM   2148 N N     . THR A 1 271 ? 21.654  5.479   54.123 1.00 10.34 ?  271 THR A N     1 
ATOM   2149 C CA    . THR A 1 271 ? 21.950  6.087   52.831 1.00 10.46 ?  271 THR A CA    1 
ATOM   2150 C C     . THR A 1 271 ? 21.725  7.590   52.854 1.00 16.57 ?  271 THR A C     1 
ATOM   2151 O O     . THR A 1 271 ? 22.452  8.342   52.194 1.00 20.99 ?  271 THR A O     1 
ATOM   2152 C CB    . THR A 1 271 ? 21.098  5.426   51.755 1.00 9.86  ?  271 THR A CB    1 
ATOM   2153 O OG1   . THR A 1 271 ? 21.159  4.002   51.910 1.00 15.98 ?  271 THR A OG1   1 
ATOM   2154 C CG2   . THR A 1 271 ? 21.575  5.807   50.364 1.00 10.66 ?  271 THR A CG2   1 
ATOM   2155 N N     . ALA A 1 272 ? 20.674  8.034   53.541 1.00 26.49 ?  272 ALA A N     1 
ATOM   2156 C CA    . ALA A 1 272 ? 20.381  9.460   53.660 1.00 32.94 ?  272 ALA A CA    1 
ATOM   2157 C C     . ALA A 1 272 ? 21.330  10.157  54.632 1.00 26.57 ?  272 ALA A C     1 
ATOM   2158 O O     . ALA A 1 272 ? 21.745  11.299  54.394 1.00 36.10 ?  272 ALA A O     1 
ATOM   2159 C CB    . ALA A 1 272 ? 18.935  9.647   54.104 1.00 36.03 ?  272 ALA A CB    1 
ATOM   2160 N N     . MET A 1 273 ? 21.602  9.523   55.774 1.00 10.37 ?  273 MET A N     1 
ATOM   2161 C CA    . MET A 1 273 ? 22.476  10.106  56.785 1.00 18.44 ?  273 MET A CA    1 
ATOM   2162 C C     . MET A 1 273 ? 23.903  10.261  56.263 1.00 37.45 ?  273 MET A C     1 
ATOM   2163 O O     . MET A 1 273 ? 24.572  11.255  56.563 1.00 42.27 ?  273 MET A O     1 
ATOM   2164 C CB    . MET A 1 273 ? 22.436  9.237   58.046 1.00 29.61 ?  273 MET A CB    1 
ATOM   2165 C CG    . MET A 1 273 ? 23.156  9.765   59.290 1.00 38.99 ?  273 MET A CG    1 
ATOM   2166 S SD    . MET A 1 273 ? 23.902  8.468   60.332 1.00 34.88 ?  273 MET A SD    1 
ATOM   2167 C CE    . MET A 1 273 ? 22.665  7.174   60.339 1.00 37.02 ?  273 MET A CE    1 
ATOM   2168 N N     . GLN A 1 274 ? 24.383  9.296   55.470 1.00 32.44 ?  274 GLN A N     1 
ATOM   2169 C CA    . GLN A 1 274 ? 25.739  9.375   54.930 1.00 27.35 ?  274 GLN A CA    1 
ATOM   2170 C C     . GLN A 1 274 ? 25.906  10.587  54.026 1.00 33.53 ?  274 GLN A C     1 
ATOM   2171 O O     . GLN A 1 274 ? 26.954  11.249  54.038 1.00 47.79 ?  274 GLN A O     1 
ATOM   2172 C CB    . GLN A 1 274 ? 26.070  8.096   54.162 1.00 22.49 ?  274 GLN A CB    1 
ATOM   2173 C CG    . GLN A 1 274 ? 27.468  8.064   53.582 1.00 34.18 ?  274 GLN A CG    1 
ATOM   2174 C CD    . GLN A 1 274 ? 27.757  6.760   52.872 1.00 51.05 ?  274 GLN A CD    1 
ATOM   2175 O OE1   . GLN A 1 274 ? 26.937  6.267   52.098 1.00 57.72 ?  274 GLN A OE1   1 
ATOM   2176 N NE2   . GLN A 1 274 ? 28.917  6.181   53.148 1.00 53.53 ?  274 GLN A NE2   1 
ATOM   2177 N N     . SER A 1 275 ? 24.895  10.875  53.209 1.00 18.07 ?  275 SER A N     1 
ATOM   2178 C CA    . SER A 1 275 ? 24.963  12.035  52.334 1.00 29.75 ?  275 SER A CA    1 
ATOM   2179 C C     . SER A 1 275 ? 24.750  13.327  53.112 1.00 35.05 ?  275 SER A C     1 
ATOM   2180 O O     . SER A 1 275 ? 25.412  14.337  52.859 1.00 23.70 ?  275 SER A O     1 
ATOM   2181 C CB    . SER A 1 275 ? 23.922  11.906  51.230 1.00 42.32 ?  275 SER A CB    1 
ATOM   2182 O OG    . SER A 1 275 ? 24.417  11.100  50.186 1.00 46.98 ?  275 SER A OG    1 
ATOM   2183 N N     . ALA A 1 276 ? 23.816  13.308  54.055 1.00 37.80 ?  276 ALA A N     1 
ATOM   2184 C CA    . ALA A 1 276 ? 23.478  14.490  54.841 1.00 34.88 ?  276 ALA A CA    1 
ATOM   2185 C C     . ALA A 1 276 ? 24.688  15.109  55.502 1.00 26.60 ?  276 ALA A C     1 
ATOM   2186 O O     . ALA A 1 276 ? 24.738  16.325  55.699 1.00 34.70 ?  276 ALA A O     1 
ATOM   2187 C CB    . ALA A 1 276 ? 22.464  14.106  55.928 1.00 41.60 ?  276 ALA A CB    1 
ATOM   2188 N N     . TYR A 1 277 ? 25.655  14.293  55.879 1.00 23.07 ?  277 TYR A N     1 
ATOM   2189 C CA    . TYR A 1 277 ? 26.823  14.768  56.587 1.00 21.75 ?  277 TYR A CA    1 
ATOM   2190 C C     . TYR A 1 277 ? 28.009  15.014  55.673 1.00 18.37 ?  277 TYR A C     1 
ATOM   2191 O O     . TYR A 1 277 ? 29.075  15.343  56.173 1.00 11.24 ?  277 TYR A O     1 
ATOM   2192 C CB    . TYR A 1 277 ? 27.237  13.764  57.665 1.00 23.50 ?  277 TYR A CB    1 
ATOM   2193 C CG    . TYR A 1 277 ? 26.326  13.694  58.846 1.00 20.04 ?  277 TYR A CG    1 
ATOM   2194 C CD1   . TYR A 1 277 ? 25.346  14.648  59.040 1.00 26.53 ?  277 TYR A CD1   1 
ATOM   2195 C CD2   . TYR A 1 277 ? 26.455  12.682  59.782 1.00 15.93 ?  277 TYR A CD2   1 
ATOM   2196 C CE1   . TYR A 1 277 ? 24.505  14.592  60.129 1.00 36.62 ?  277 TYR A CE1   1 
ATOM   2197 C CE2   . TYR A 1 277 ? 25.614  12.613  60.878 1.00 28.87 ?  277 TYR A CE2   1 
ATOM   2198 C CZ    . TYR A 1 277 ? 24.640  13.577  61.046 1.00 35.03 ?  277 TYR A CZ    1 
ATOM   2199 O OH    . TYR A 1 277 ? 23.792  13.537  62.126 1.00 34.17 ?  277 TYR A OH    1 
ATOM   2200 N N     . THR A 1 278 ? 27.852  14.869  54.356 1.00 26.81 ?  278 THR A N     1 
ATOM   2201 C CA    . THR A 1 278 ? 28.985  14.961  53.440 1.00 15.06 ?  278 THR A CA    1 
ATOM   2202 C C     . THR A 1 278 ? 28.800  15.975  52.315 1.00 22.25 ?  278 THR A C     1 
ATOM   2203 O O     . THR A 1 278 ? 29.696  16.785  52.060 1.00 43.31 ?  278 THR A O     1 
ATOM   2204 C CB    . THR A 1 278 ? 29.287  13.576  52.843 1.00 30.65 ?  278 THR A CB    1 
ATOM   2205 O OG1   . THR A 1 278 ? 28.070  12.848  52.617 1.00 31.65 ?  278 THR A OG1   1 
ATOM   2206 C CG2   . THR A 1 278 ? 30.163  12.788  53.770 1.00 33.69 ?  278 THR A CG2   1 
ATOM   2207 N N     . GLU A 1 279 ? 27.669  15.936  51.614 1.00 18.75 ?  279 GLU A N     1 
ATOM   2208 C CA    . GLU A 1 279 ? 27.509  16.700  50.385 1.00 22.57 ?  279 GLU A CA    1 
ATOM   2209 C C     . GLU A 1 279 ? 26.383  17.740  50.449 1.00 27.61 ?  279 GLU A C     1 
ATOM   2210 O O     . GLU A 1 279 ? 25.981  18.269  49.403 1.00 37.52 ?  279 GLU A O     1 
ATOM   2211 C CB    . GLU A 1 279 ? 27.321  15.746  49.203 1.00 30.38 ?  279 GLU A CB    1 
ATOM   2212 C CG    . GLU A 1 279 ? 26.198  14.724  49.395 1.00 52.30 ?  279 GLU A CG    1 
ATOM   2213 C CD    . GLU A 1 279 ? 26.417  13.393  48.656 1.00 58.09 ?  279 GLU A CD    1 
ATOM   2214 O OE1   . GLU A 1 279 ? 27.469  13.222  47.998 1.00 53.77 ?  279 GLU A OE1   1 
ATOM   2215 O OE2   . GLU A 1 279 ? 25.487  12.549  48.673 1.00 54.89 -1 279 GLU A OE2   1 
ATOM   2216 N N     . CYS A 1 280 ? 25.833  18.031  51.633 1.00 18.84 ?  280 CYS A N     1 
ATOM   2217 C CA    . CYS A 1 280 ? 24.670  18.909  51.737 1.00 24.59 ?  280 CYS A CA    1 
ATOM   2218 C C     . CYS A 1 280 ? 24.952  20.167  52.559 1.00 33.81 ?  280 CYS A C     1 
ATOM   2219 O O     . CYS A 1 280 ? 24.010  20.826  53.009 1.00 41.14 ?  280 CYS A O     1 
ATOM   2220 C CB    . CYS A 1 280 ? 23.487  18.163  52.359 1.00 24.44 ?  280 CYS A CB    1 
ATOM   2221 S SG    . CYS A 1 280 ? 22.904  16.744  51.452 1.00 32.63 ?  280 CYS A SG    1 
ATOM   2222 N N     . ASN A 1 281 ? 26.224  20.527  52.740 1.00 31.44 ?  281 ASN A N     1 
ATOM   2223 C CA    . ASN A 1 281 ? 26.591  21.577  53.692 1.00 24.14 ?  281 ASN A CA    1 
ATOM   2224 C C     . ASN A 1 281 ? 26.025  22.944  53.308 1.00 20.32 ?  281 ASN A C     1 
ATOM   2225 O O     . ASN A 1 281 ? 25.595  23.707  54.181 1.00 12.24 ?  281 ASN A O     1 
ATOM   2226 C CB    . ASN A 1 281 ? 28.109  21.605  53.823 1.00 19.36 ?  281 ASN A CB    1 
ATOM   2227 C CG    . ASN A 1 281 ? 28.668  20.245  54.178 1.00 20.23 ?  281 ASN A CG    1 
ATOM   2228 O OD1   . ASN A 1 281 ? 28.687  19.848  55.347 1.00 25.11 ?  281 ASN A OD1   1 
ATOM   2229 N ND2   . ASN A 1 281 ? 29.071  19.493  53.159 1.00 18.48 ?  281 ASN A ND2   1 
ATOM   2230 N N     . ASP A 1 282 ? 26.024  23.281  52.014 1.00 15.43 ?  282 ASP A N     1 
ATOM   2231 C CA    . ASP A 1 282 ? 25.553  24.602  51.609 1.00 21.04 ?  282 ASP A CA    1 
ATOM   2232 C C     . ASP A 1 282 ? 24.040  24.728  51.749 1.00 32.20 ?  282 ASP A C     1 
ATOM   2233 O O     . ASP A 1 282 ? 23.530  25.830  52.000 1.00 20.24 ?  282 ASP A O     1 
ATOM   2234 C CB    . ASP A 1 282 ? 25.992  24.901  50.181 1.00 29.32 ?  282 ASP A CB    1 
ATOM   2235 C CG    . ASP A 1 282 ? 25.882  23.708  49.277 1.00 54.66 ?  282 ASP A CG    1 
ATOM   2236 O OD1   . ASP A 1 282 ? 25.696  22.572  49.781 1.00 61.91 ?  282 ASP A OD1   1 
ATOM   2237 O OD2   . ASP A 1 282 ? 25.988  23.911  48.048 1.00 66.24 -1 282 ASP A OD2   1 
ATOM   2238 N N     . TRP A 1 283 ? 23.311  23.619  51.567 1.00 49.25 ?  283 TRP A N     1 
ATOM   2239 C CA    . TRP A 1 283 ? 21.869  23.599  51.800 1.00 39.04 ?  283 TRP A CA    1 
ATOM   2240 C C     . TRP A 1 283 ? 21.533  23.901  53.257 1.00 40.88 ?  283 TRP A C     1 
ATOM   2241 O O     . TRP A 1 283 ? 20.454  24.431  53.550 1.00 56.38 ?  283 TRP A O     1 
ATOM   2242 C CB    . TRP A 1 283 ? 21.297  22.243  51.382 1.00 21.40 ?  283 TRP A CB    1 
ATOM   2243 C CG    . TRP A 1 283 ? 19.796  22.142  51.486 1.00 29.87 ?  283 TRP A CG    1 
ATOM   2244 C CD1   . TRP A 1 283 ? 18.890  22.349  50.488 1.00 24.81 ?  283 TRP A CD1   1 
ATOM   2245 C CD2   . TRP A 1 283 ? 19.035  21.788  52.649 1.00 28.37 ?  283 TRP A CD2   1 
ATOM   2246 N NE1   . TRP A 1 283 ? 17.613  22.150  50.960 1.00 18.53 ?  283 TRP A NE1   1 
ATOM   2247 C CE2   . TRP A 1 283 ? 17.682  21.803  52.284 1.00 17.08 ?  283 TRP A CE2   1 
ATOM   2248 C CE3   . TRP A 1 283 ? 19.371  21.458  53.962 1.00 38.47 ?  283 TRP A CE3   1 
ATOM   2249 C CZ2   . TRP A 1 283 ? 16.670  21.517  53.186 1.00 11.82 ?  283 TRP A CZ2   1 
ATOM   2250 C CZ3   . TRP A 1 283 ? 18.356  21.159  54.850 1.00 30.79 ?  283 TRP A CZ3   1 
ATOM   2251 C CH2   . TRP A 1 283 ? 17.029  21.193  54.460 1.00 12.25 ?  283 TRP A CH2   1 
ATOM   2252 N N     . LEU A 1 284 ? 22.419  23.527  54.183 1.00 22.33 ?  284 LEU A N     1 
ATOM   2253 C CA    . LEU A 1 284 ? 22.217  23.819  55.598 1.00 12.19 ?  284 LEU A CA    1 
ATOM   2254 C C     . LEU A 1 284 ? 22.569  25.270  55.935 1.00 26.14 ?  284 LEU A C     1 
ATOM   2255 O O     . LEU A 1 284 ? 22.027  25.824  56.898 1.00 30.18 ?  284 LEU A O     1 
ATOM   2256 C CB    . LEU A 1 284 ? 23.005  22.815  56.447 1.00 16.07 ?  284 LEU A CB    1 
ATOM   2257 C CG    . LEU A 1 284 ? 22.893  22.842  57.975 1.00 12.83 ?  284 LEU A CG    1 
ATOM   2258 C CD1   . LEU A 1 284 ? 21.444  22.870  58.395 1.00 8.55  ?  284 LEU A CD1   1 
ATOM   2259 C CD2   . LEU A 1 284 ? 23.625  21.663  58.630 1.00 8.66  ?  284 LEU A CD2   1 
ATOM   2260 N N     . ASN A 1 285 ? 23.486  25.896  55.181 1.00 36.29 ?  285 ASN A N     1 
ATOM   2261 C CA    . ASN A 1 285 ? 23.671  27.347  55.294 1.00 40.29 ?  285 ASN A CA    1 
ATOM   2262 C C     . ASN A 1 285 ? 22.418  28.074  54.839 1.00 37.87 ?  285 ASN A C     1 
ATOM   2263 O O     . ASN A 1 285 ? 21.976  29.035  55.479 1.00 30.81 ?  285 ASN A O     1 
ATOM   2264 C CB    . ASN A 1 285 ? 24.852  27.836  54.441 1.00 36.73 ?  285 ASN A CB    1 
ATOM   2265 C CG    . ASN A 1 285 ? 26.216  27.643  55.102 1.00 34.05 ?  285 ASN A CG    1 
ATOM   2266 O OD1   . ASN A 1 285 ? 26.342  27.563  56.326 1.00 44.35 ?  285 ASN A OD1   1 
ATOM   2267 N ND2   . ASN A 1 285 ? 27.253  27.588  54.273 1.00 14.06 ?  285 ASN A ND2   1 
ATOM   2268 N N     . LYS A 1 286 ? 21.840  27.619  53.724 1.00 39.15 ?  286 LYS A N     1 
ATOM   2269 C CA    . LYS A 1 286 ? 20.610  28.195  53.202 1.00 40.69 ?  286 LYS A CA    1 
ATOM   2270 C C     . LYS A 1 286 ? 19.524  28.186  54.269 1.00 47.40 ?  286 LYS A C     1 
ATOM   2271 O O     . LYS A 1 286 ? 19.027  29.237  54.688 1.00 48.44 ?  286 LYS A O     1 
ATOM   2272 C CB    . LYS A 1 286 ? 20.147  27.385  51.977 1.00 37.92 ?  286 LYS A CB    1 
ATOM   2273 C CG    . LYS A 1 286 ? 20.746  27.780  50.634 1.00 35.37 ?  286 LYS A CG    1 
ATOM   2274 C CD    . LYS A 1 286 ? 19.782  28.619  49.796 1.00 31.77 ?  286 LYS A CD    1 
ATOM   2275 C CE    . LYS A 1 286 ? 20.118  28.554  48.313 1.00 27.45 ?  286 LYS A CE    1 
ATOM   2276 N NZ    . LYS A 1 286 ? 21.581  28.674  48.048 1.00 26.09 1  286 LYS A NZ    1 
ATOM   2277 N N     . ILE A 1 287 ? 19.182  26.988  54.750 1.00 37.69 ?  287 ILE A N     1 
ATOM   2278 C CA    . ILE A 1 287 ? 18.069  26.818  55.672 1.00 25.00 ?  287 ILE A CA    1 
ATOM   2279 C C     . ILE A 1 287 ? 18.313  27.554  56.990 1.00 23.90 ?  287 ILE A C     1 
ATOM   2280 O O     . ILE A 1 287 ? 17.365  27.901  57.694 1.00 30.69 ?  287 ILE A O     1 
ATOM   2281 C CB    . ILE A 1 287 ? 17.804  25.310  55.861 1.00 30.58 ?  287 ILE A CB    1 
ATOM   2282 C CG1   . ILE A 1 287 ? 16.451  25.051  56.524 1.00 31.45 ?  287 ILE A CG1   1 
ATOM   2283 C CG2   . ILE A 1 287 ? 18.915  24.670  56.634 1.00 42.49 ?  287 ILE A CG2   1 
ATOM   2284 C CD1   . ILE A 1 287 ? 16.166  23.576  56.752 1.00 27.00 ?  287 ILE A CD1   1 
ATOM   2285 N N     . ARG A 1 288 ? 19.534  27.860  57.338 1.00 29.91 ?  288 ARG A N     1 
ATOM   2286 C CA    . ARG A 1 288 ? 19.702  28.574  58.615 1.00 31.60 ?  288 ARG A CA    1 
ATOM   2287 C C     . ARG A 1 288 ? 19.253  30.005  58.363 1.00 27.57 ?  288 ARG A C     1 
ATOM   2288 O O     . ARG A 1 288 ? 18.432  30.500  59.094 1.00 24.76 ?  288 ARG A O     1 
ATOM   2289 C CB    . ARG A 1 288 ? 21.150  28.473  59.102 1.00 33.54 ?  288 ARG A CB    1 
ATOM   2290 C CG    . ARG A 1 288 ? 21.479  27.277  59.977 1.00 30.59 ?  288 ARG A CG    1 
ATOM   2291 C CD    . ARG A 1 288 ? 22.969  27.329  60.250 1.00 36.25 ?  288 ARG A CD    1 
ATOM   2292 N NE    . ARG A 1 288 ? 23.439  26.156  60.963 1.00 40.99 ?  288 ARG A NE    1 
ATOM   2293 C CZ    . ARG A 1 288 ? 24.133  26.179  62.091 1.00 47.64 ?  288 ARG A CZ    1 
ATOM   2294 N NH1   . ARG A 1 288 ? 24.466  27.328  62.646 1.00 43.89 1  288 ARG A NH1   1 
ATOM   2295 N NH2   . ARG A 1 288 ? 24.501  25.048  62.659 1.00 50.36 ?  288 ARG A NH2   1 
ATOM   2296 N N     . LEU A 1 289 ? 19.708  30.588  57.277 1.00 22.63 ?  289 LEU A N     1 
ATOM   2297 C CA    . LEU A 1 289 ? 19.377  31.988  57.069 1.00 27.92 ?  289 LEU A CA    1 
ATOM   2298 C C     . LEU A 1 289 ? 17.906  32.167  56.732 1.00 20.69 ?  289 LEU A C     1 
ATOM   2299 O O     . LEU A 1 289 ? 17.320  33.207  57.042 1.00 24.76 ?  289 LEU A O     1 
ATOM   2300 C CB    . LEU A 1 289 ? 20.280  32.575  55.981 1.00 31.39 ?  289 LEU A CB    1 
ATOM   2301 C CG    . LEU A 1 289 ? 21.766  32.466  56.346 1.00 26.92 ?  289 LEU A CG    1 
ATOM   2302 C CD1   . LEU A 1 289 ? 22.674  32.852  55.172 1.00 30.86 ?  289 LEU A CD1   1 
ATOM   2303 C CD2   . LEU A 1 289 ? 22.100  33.264  57.622 1.00 21.88 ?  289 LEU A CD2   1 
ATOM   2304 N N     . TYR A 1 290 ? 17.290  31.160  56.128 1.00 19.19 ?  290 TYR A N     1 
ATOM   2305 C CA    . TYR A 1 290 ? 15.861  31.235  55.872 1.00 10.02 ?  290 TYR A CA    1 
ATOM   2306 C C     . TYR A 1 290 ? 15.063  31.106  57.162 1.00 12.50 ?  290 TYR A C     1 
ATOM   2307 O O     . TYR A 1 290 ? 14.061  31.805  57.351 1.00 29.53 ?  290 TYR A O     1 
ATOM   2308 C CB    . TYR A 1 290 ? 15.456  30.175  54.866 1.00 10.33 ?  290 TYR A CB    1 
ATOM   2309 C CG    . TYR A 1 290 ? 14.183  30.536  54.159 1.00 20.23 ?  290 TYR A CG    1 
ATOM   2310 C CD1   . TYR A 1 290 ? 12.966  30.426  54.807 1.00 26.81 ?  290 TYR A CD1   1 
ATOM   2311 C CD2   . TYR A 1 290 ? 14.190  31.013  52.861 1.00 19.57 ?  290 TYR A CD2   1 
ATOM   2312 C CE1   . TYR A 1 290 ? 11.800  30.762  54.186 1.00 24.79 ?  290 TYR A CE1   1 
ATOM   2313 C CE2   . TYR A 1 290 ? 13.016  31.346  52.229 1.00 19.52 ?  290 TYR A CE2   1 
ATOM   2314 C CZ    . TYR A 1 290 ? 11.824  31.218  52.904 1.00 18.45 ?  290 TYR A CZ    1 
ATOM   2315 O OH    . TYR A 1 290 ? 10.638  31.540  52.302 1.00 20.91 ?  290 TYR A OH    1 
ATOM   2316 N N     . ILE A 1 291 ? 15.469  30.204  58.051 1.00 13.51 ?  291 ILE A N     1 
ATOM   2317 C CA    . ILE A 1 291 ? 14.727  30.020  59.292 1.00 8.13  ?  291 ILE A CA    1 
ATOM   2318 C C     . ILE A 1 291 ? 14.822  31.266  60.169 1.00 31.93 ?  291 ILE A C     1 
ATOM   2319 O O     . ILE A 1 291 ? 13.806  31.749  60.677 1.00 42.24 ?  291 ILE A O     1 
ATOM   2320 C CB    . ILE A 1 291 ? 15.216  28.765  60.036 1.00 31.23 ?  291 ILE A CB    1 
ATOM   2321 C CG1   . ILE A 1 291 ? 14.928  27.485  59.227 1.00 26.72 ?  291 ILE A CG1   1 
ATOM   2322 C CG2   . ILE A 1 291 ? 14.593  28.693  61.411 1.00 36.69 ?  291 ILE A CG2   1 
ATOM   2323 C CD1   . ILE A 1 291 ? 13.601  27.434  58.537 1.00 28.16 ?  291 ILE A CD1   1 
ATOM   2324 N N     . GLU A 1 292 ? 16.033  31.836  60.327 1.00 32.65 ?  292 GLU A N     1 
ATOM   2325 C CA    . GLU A 1 292 ? 16.192  32.967  61.252 1.00 20.17 ?  292 GLU A CA    1 
ATOM   2326 C C     . GLU A 1 292 ? 15.364  34.163  60.817 1.00 18.72 ?  292 GLU A C     1 
ATOM   2327 O O     . GLU A 1 292 ? 14.650  34.753  61.633 1.00 18.84 ?  292 GLU A O     1 
ATOM   2328 C CB    . GLU A 1 292 ? 17.656  33.402  61.363 1.00 11.83 ?  292 GLU A CB    1 
ATOM   2329 C CG    . GLU A 1 292 ? 17.969  34.408  62.492 1.00 10.04 ?  292 GLU A CG    1 
ATOM   2330 C CD    . GLU A 1 292 ? 19.468  34.511  62.839 1.00 36.33 ?  292 GLU A CD    1 
ATOM   2331 O OE1   . GLU A 1 292 ? 20.321  34.198  61.980 1.00 40.99 ?  292 GLU A OE1   1 
ATOM   2332 O OE2   . GLU A 1 292 ? 19.795  34.885  63.992 1.00 32.65 -1 292 GLU A OE2   1 
ATOM   2333 N N     . ASP A 1 293 ? 15.372  34.478  59.520 1.00 12.92 ?  293 ASP A N     1 
ATOM   2334 C CA    . ASP A 1 293 ? 14.563  35.594  59.053 1.00 13.09 ?  293 ASP A CA    1 
ATOM   2335 C C     . ASP A 1 293 ? 13.092  35.247  59.131 1.00 14.46 ?  293 ASP A C     1 
ATOM   2336 O O     . ASP A 1 293 ? 12.265  36.138  59.331 1.00 22.82 ?  293 ASP A O     1 
ATOM   2337 C CB    . ASP A 1 293 ? 14.957  35.997  57.629 1.00 30.18 ?  293 ASP A CB    1 
ATOM   2338 C CG    . ASP A 1 293 ? 14.572  37.455  57.287 1.00 48.18 ?  293 ASP A CG    1 
ATOM   2339 O OD1   . ASP A 1 293 ? 14.181  38.216  58.200 1.00 49.73 ?  293 ASP A OD1   1 
ATOM   2340 O OD2   . ASP A 1 293 ? 14.674  37.854  56.104 1.00 46.25 -1 293 ASP A OD2   1 
ATOM   2341 N N     . ASN A 1 294 ? 12.750  33.960  59.014 1.00 11.64 ?  294 ASN A N     1 
ATOM   2342 C CA    . ASN A 1 294 ? 11.375  33.548  59.286 1.00 22.33 ?  294 ASN A CA    1 
ATOM   2343 C C     . ASN A 1 294 ? 11.038  33.739  60.764 1.00 27.69 ?  294 ASN A C     1 
ATOM   2344 O O     . ASN A 1 294 ? 9.919   34.151  61.104 1.00 21.86 ?  294 ASN A O     1 
ATOM   2345 C CB    . ASN A 1 294 ? 11.141  32.088  58.858 1.00 9.78  ?  294 ASN A CB    1 
ATOM   2346 C CG    . ASN A 1 294 ? 10.597  31.953  57.409 1.00 10.94 ?  294 ASN A CG    1 
ATOM   2347 O OD1   . ASN A 1 294 ? 10.789  32.824  56.562 1.00 14.18 ?  294 ASN A OD1   1 
ATOM   2348 N ND2   . ASN A 1 294 ? 9.909   30.855  57.144 1.00 16.50 ?  294 ASN A ND2   1 
ATOM   2349 N N     . ALA A 1 295 ? 12.006  33.474  61.653 1.00 25.31 ?  295 ALA A N     1 
ATOM   2350 C CA    . ALA A 1 295 ? 11.830  33.761  63.078 1.00 22.19 ?  295 ALA A CA    1 
ATOM   2351 C C     . ALA A 1 295 ? 11.799  35.259  63.341 1.00 22.45 ?  295 ALA A C     1 
ATOM   2352 O O     . ALA A 1 295 ? 11.120  35.718  64.264 1.00 37.75 ?  295 ALA A O     1 
ATOM   2353 C CB    . ALA A 1 295 ? 12.938  33.107  63.903 1.00 28.13 ?  295 ALA A CB    1 
ATOM   2354 N N     . LYS A 1 296 ? 12.573  36.033  62.583 1.00 18.03 ?  296 LYS A N     1 
ATOM   2355 C CA    . LYS A 1 296 ? 12.509  37.481  62.720 1.00 11.90 ?  296 LYS A CA    1 
ATOM   2356 C C     . LYS A 1 296 ? 11.168  38.009  62.220 1.00 22.23 ?  296 LYS A C     1 
ATOM   2357 O O     . LYS A 1 296 ? 10.458  38.707  62.951 1.00 13.78 ?  296 LYS A O     1 
ATOM   2358 C CB    . LYS A 1 296 ? 13.670  38.126  61.963 1.00 7.95  ?  296 LYS A CB    1 
ATOM   2359 C CG    . LYS A 1 296 ? 13.619  39.647  61.925 1.00 29.83 ?  296 LYS A CG    1 
ATOM   2360 C CD    . LYS A 1 296 ? 14.778  40.246  61.131 1.00 35.83 ?  296 LYS A CD    1 
ATOM   2361 C CE    . LYS A 1 296 ? 14.701  41.769  61.077 1.00 28.78 ?  296 LYS A CE    1 
ATOM   2362 N NZ    . LYS A 1 296 ? 13.779  42.303  60.038 1.00 18.82 1  296 LYS A NZ    1 
ATOM   2363 N N     . PHE A 1 297 ? 10.764  37.597  61.009 1.00 18.00 ?  297 PHE A N     1 
ATOM   2364 C CA    . PHE A 1 297 ? 9.496   38.044  60.428 1.00 21.35 ?  297 PHE A CA    1 
ATOM   2365 C C     . PHE A 1 297 ? 8.327   37.744  61.349 1.00 28.58 ?  297 PHE A C     1 
ATOM   2366 O O     . PHE A 1 297 ? 7.425   38.575  61.510 1.00 28.71 ?  297 PHE A O     1 
ATOM   2367 C CB    . PHE A 1 297 ? 9.279   37.382  59.061 1.00 31.98 ?  297 PHE A CB    1 
ATOM   2368 C CG    . PHE A 1 297 ? 7.884   37.592  58.466 1.00 44.77 ?  297 PHE A CG    1 
ATOM   2369 C CD1   . PHE A 1 297 ? 7.579   38.731  57.725 1.00 30.68 ?  297 PHE A CD1   1 
ATOM   2370 C CD2   . PHE A 1 297 ? 6.885   36.627  58.623 1.00 43.12 ?  297 PHE A CD2   1 
ATOM   2371 C CE1   . PHE A 1 297 ? 6.312   38.901  57.169 1.00 15.72 ?  297 PHE A CE1   1 
ATOM   2372 C CE2   . PHE A 1 297 ? 5.605   36.810  58.067 1.00 17.55 ?  297 PHE A CE2   1 
ATOM   2373 C CZ    . PHE A 1 297 ? 5.332   37.937  57.345 1.00 12.06 ?  297 PHE A CZ    1 
ATOM   2374 N N     . ALA A 1 298 ? 8.320   36.556  61.957 1.00 20.63 ?  298 ALA A N     1 
ATOM   2375 C CA    . ALA A 1 298 ? 7.198   36.167  62.797 1.00 6.64  ?  298 ALA A CA    1 
ATOM   2376 C C     . ALA A 1 298 ? 7.189   36.940  64.103 1.00 11.82 ?  298 ALA A C     1 
ATOM   2377 O O     . ALA A 1 298 ? 6.134   37.373  64.574 1.00 19.10 ?  298 ALA A O     1 
ATOM   2378 C CB    . ALA A 1 298 ? 7.261   34.667  63.086 1.00 9.99  ?  298 ALA A CB    1 
ATOM   2379 N N     . CYS A 1 299 ? 8.361   37.147  64.690 1.00 22.24 ?  299 CYS A N     1 
ATOM   2380 C CA    . CYS A 1 299 ? 8.419   37.769  66.002 1.00 23.23 ?  299 CYS A CA    1 
ATOM   2381 C C     . CYS A 1 299 ? 8.001   39.229  65.958 1.00 21.79 ?  299 CYS A C     1 
ATOM   2382 O O     . CYS A 1 299 ? 7.504   39.761  66.961 1.00 13.92 ?  299 CYS A O     1 
ATOM   2383 C CB    . CYS A 1 299 ? 9.828   37.641  66.555 1.00 21.52 ?  299 CYS A CB    1 
ATOM   2384 S SG    . CYS A 1 299 ? 9.985   36.206  67.560 1.00 38.43 ?  299 CYS A SG    1 
ATOM   2385 N N     . GLU A 1 300 ? 8.202   39.881  64.811 1.00 20.33 ?  300 GLU A N     1 
ATOM   2386 C CA    . GLU A 1 300 ? 7.824   41.276  64.620 1.00 22.98 ?  300 GLU A CA    1 
ATOM   2387 C C     . GLU A 1 300 ? 6.346   41.443  64.284 1.00 27.75 ?  300 GLU A C     1 
ATOM   2388 O O     . GLU A 1 300 ? 5.714   42.386  64.765 1.00 36.04 ?  300 GLU A O     1 
ATOM   2389 C CB    . GLU A 1 300 ? 8.686   41.885  63.515 1.00 14.64 ?  300 GLU A CB    1 
ATOM   2390 C CG    . GLU A 1 300 ? 10.147  42.005  63.886 1.00 7.66  ?  300 GLU A CG    1 
ATOM   2391 C CD    . GLU A 1 300 ? 11.030  42.054  62.675 1.00 14.66 ?  300 GLU A CD    1 
ATOM   2392 O OE1   . GLU A 1 300 ? 10.549  41.723  61.577 1.00 17.11 ?  300 GLU A OE1   1 
ATOM   2393 O OE2   . GLU A 1 300 ? 12.209  42.428  62.813 1.00 29.54 -1 300 GLU A OE2   1 
ATOM   2394 N N     . TYR A 1 301 ? 5.797   40.581  63.421 1.00 25.00 ?  301 TYR A N     1 
ATOM   2395 C CA    . TYR A 1 301 ? 4.374   40.648  63.088 1.00 21.95 ?  301 TYR A CA    1 
ATOM   2396 C C     . TYR A 1 301 ? 3.499   40.562  64.334 1.00 30.23 ?  301 TYR A C     1 
ATOM   2397 O O     . TYR A 1 301 ? 2.422   41.162  64.385 1.00 23.88 ?  301 TYR A O     1 
ATOM   2398 C CB    . TYR A 1 301 ? 4.010   39.525  62.110 1.00 25.09 ?  301 TYR A CB    1 
ATOM   2399 C CG    . TYR A 1 301 ? 2.549   39.495  61.667 1.00 18.75 ?  301 TYR A CG    1 
ATOM   2400 C CD1   . TYR A 1 301 ? 1.541   39.045  62.515 1.00 18.39 ?  301 TYR A CD1   1 
ATOM   2401 C CD2   . TYR A 1 301 ? 2.194   39.885  60.384 1.00 16.66 ?  301 TYR A CD2   1 
ATOM   2402 C CE1   . TYR A 1 301 ? 0.224   39.024  62.107 1.00 11.78 ?  301 TYR A CE1   1 
ATOM   2403 C CE2   . TYR A 1 301 ? 0.882   39.858  59.968 1.00 21.96 ?  301 TYR A CE2   1 
ATOM   2404 C CZ    . TYR A 1 301 ? -0.094  39.427  60.827 1.00 22.96 ?  301 TYR A CZ    1 
ATOM   2405 O OH    . TYR A 1 301 ? -1.391  39.405  60.399 1.00 49.73 ?  301 TYR A OH    1 
ATOM   2406 N N     . MET A 1 302 ? 3.903   39.751  65.312 1.00 28.99 ?  302 MET A N     1 
ATOM   2407 C CA    . MET A 1 302 ? 3.189   39.671  66.581 1.00 16.69 ?  302 MET A CA    1 
ATOM   2408 C C     . MET A 1 302 ? 3.570   40.794  67.521 1.00 16.39 ?  302 MET A C     1 
ATOM   2409 O O     . MET A 1 302 ? 2.910   40.965  68.548 1.00 8.93  ?  302 MET A O     1 
ATOM   2410 C CB    . MET A 1 302 ? 3.427   38.328  67.244 1.00 8.37  ?  302 MET A CB    1 
ATOM   2411 C CG    . MET A 1 302 ? 3.368   37.212  66.246 1.00 28.95 ?  302 MET A CG    1 
ATOM   2412 S SD    . MET A 1 302 ? 3.359   35.588  67.004 1.00 53.21 ?  302 MET A SD    1 
ATOM   2413 C CE    . MET A 1 302 ? 1.620   35.227  67.040 1.00 41.88 ?  302 MET A CE    1 
ATOM   2414 N N     . LYS A 1 303 ? 4.738   41.397  67.302 1.00 25.35 ?  303 LYS A N     1 
ATOM   2415 C CA    . LYS A 1 303 ? 5.064   42.681  67.910 1.00 20.67 ?  303 LYS A CA    1 
ATOM   2416 C C     . LYS A 1 303 ? 4.135   43.767  67.395 1.00 5.53  ?  303 LYS A C     1 
ATOM   2417 O O     . LYS A 1 303 ? 3.479   44.479  68.166 1.00 8.11  ?  303 LYS A O     1 
ATOM   2418 C CB    . LYS A 1 303 ? 6.509   43.053  67.574 1.00 20.58 ?  303 LYS A CB    1 
ATOM   2419 C CG    . LYS A 1 303 ? 7.037   44.339  68.193 1.00 14.22 ?  303 LYS A CG    1 
ATOM   2420 C CD    . LYS A 1 303 ? 8.367   44.754  67.628 1.00 21.99 ?  303 LYS A CD    1 
ATOM   2421 C CE    . LYS A 1 303 ? 8.849   45.995  68.350 1.00 34.25 ?  303 LYS A CE    1 
ATOM   2422 N NZ    . LYS A 1 303 ? 9.216   45.701  69.764 1.00 33.32 1  303 LYS A NZ    1 
ATOM   2423 N N     . ASP A 1 304 ? 4.113   43.925  66.075 1.00 6.09  ?  304 ASP A N     1 
ATOM   2424 C CA    . ASP A 1 304 ? 3.442   45.037  65.427 1.00 27.97 ?  304 ASP A CA    1 
ATOM   2425 C C     . ASP A 1 304 ? 1.936   44.831  65.338 1.00 24.18 ?  304 ASP A C     1 
ATOM   2426 O O     . ASP A 1 304 ? 1.167   45.695  65.767 1.00 39.26 ?  304 ASP A O     1 
ATOM   2427 C CB    . ASP A 1 304 ? 4.053   45.259  64.039 1.00 33.13 ?  304 ASP A CB    1 
ATOM   2428 C CG    . ASP A 1 304 ? 4.824   46.563  63.953 1.00 42.13 ?  304 ASP A CG    1 
ATOM   2429 O OD1   . ASP A 1 304 ? 4.881   47.254  64.989 1.00 39.88 ?  304 ASP A OD1   1 
ATOM   2430 O OD2   . ASP A 1 304 ? 5.346   46.909  62.865 1.00 37.94 -1 304 ASP A OD2   1 
ATOM   2431 N N     . HIS A 1 305 ? 1.495   43.678  64.828 1.00 25.45 ?  305 HIS A N     1 
ATOM   2432 C CA    . HIS A 1 305 ? 0.102   43.480  64.433 1.00 28.72 ?  305 HIS A CA    1 
ATOM   2433 C C     . HIS A 1 305 ? -0.691  42.529  65.322 1.00 25.16 ?  305 HIS A C     1 
ATOM   2434 O O     . HIS A 1 305 ? -1.903  42.392  65.125 1.00 35.51 ?  305 HIS A O     1 
ATOM   2435 C CB    . HIS A 1 305 ? 0.039   42.998  62.973 1.00 38.08 ?  305 HIS A CB    1 
ATOM   2436 C CG    . HIS A 1 305 ? 1.031   43.677  62.077 1.00 47.90 ?  305 HIS A CG    1 
ATOM   2437 N ND1   . HIS A 1 305 ? 0.834   44.945  61.576 1.00 39.93 ?  305 HIS A ND1   1 
ATOM   2438 C CD2   . HIS A 1 305 ? 2.227   43.264  61.593 1.00 50.61 ?  305 HIS A CD2   1 
ATOM   2439 C CE1   . HIS A 1 305 ? 1.866   45.286  60.826 1.00 38.43 ?  305 HIS A CE1   1 
ATOM   2440 N NE2   . HIS A 1 305 ? 2.726   44.284  60.818 1.00 47.06 ?  305 HIS A NE2   1 
ATOM   2441 N N     . ILE A 1 306 ? -0.056  41.858  66.276 1.00 27.89 ?  306 ILE A N     1 
ATOM   2442 C CA    . ILE A 1 306 ? -0.770  41.066  67.279 1.00 14.03 ?  306 ILE A CA    1 
ATOM   2443 C C     . ILE A 1 306 ? -0.179  41.432  68.638 1.00 17.43 ?  306 ILE A C     1 
ATOM   2444 O O     . ILE A 1 306 ? 0.308   40.550  69.356 1.00 38.32 ?  306 ILE A O     1 
ATOM   2445 C CB    . ILE A 1 306 ? -0.646  39.557  66.999 1.00 10.29 ?  306 ILE A CB    1 
ATOM   2446 C CG1   . ILE A 1 306 ? -0.779  39.259  65.508 1.00 23.75 ?  306 ILE A CG1   1 
ATOM   2447 C CG2   . ILE A 1 306 ? -1.679  38.751  67.772 1.00 6.51  ?  306 ILE A CG2   1 
ATOM   2448 C CD1   . ILE A 1 306 ? -0.668  37.787  65.173 1.00 32.52 ?  306 ILE A CD1   1 
ATOM   2449 N N     . PRO A 1 307 ? -0.278  42.690  69.073 1.00 13.11 ?  307 PRO A N     1 
ATOM   2450 C CA    . PRO A 1 307 ? 0.440   43.117  70.281 1.00 8.47  ?  307 PRO A CA    1 
ATOM   2451 C C     . PRO A 1 307 ? -0.044  42.462  71.548 1.00 11.15 ?  307 PRO A C     1 
ATOM   2452 O O     . PRO A 1 307 ? 0.616   42.620  72.587 1.00 15.46 ?  307 PRO A O     1 
ATOM   2453 C CB    . PRO A 1 307 ? 0.167   44.623  70.329 1.00 26.09 ?  307 PRO A CB    1 
ATOM   2454 C CG    . PRO A 1 307 ? -1.159  44.767  69.669 1.00 25.67 ?  307 PRO A CG    1 
ATOM   2455 C CD    . PRO A 1 307 ? -1.168  43.746  68.562 1.00 29.49 ?  307 PRO A CD    1 
ATOM   2456 N N     . THR A 1 308 ? -1.145  41.709  71.490 1.00 15.08 ?  308 THR A N     1 
ATOM   2457 C CA    . THR A 1 308 ? -1.706  41.039  72.660 1.00 25.85 ?  308 THR A CA    1 
ATOM   2458 C C     . THR A 1 308 ? -1.062  39.673  72.892 1.00 34.55 ?  308 THR A C     1 
ATOM   2459 O O     . THR A 1 308 ? -1.467  38.952  73.811 1.00 38.01 ?  308 THR A O     1 
ATOM   2460 C CB    . THR A 1 308 ? -3.269  40.958  72.556 1.00 12.28 ?  308 THR A CB    1 
ATOM   2461 O OG1   . THR A 1 308 ? -3.835  40.480  73.777 1.00 8.39  ?  308 THR A OG1   1 
ATOM   2462 C CG2   . THR A 1 308 ? -3.781  40.102  71.422 1.00 5.63  ?  308 THR A CG2   1 
ATOM   2463 N N     . LEU A 1 309 ? -0.058  39.316  72.084 1.00 24.48 ?  309 LEU A N     1 
ATOM   2464 C CA    . LEU A 1 309 ? 0.747   38.114  72.265 1.00 18.61 ?  309 LEU A CA    1 
ATOM   2465 C C     . LEU A 1 309 ? 2.214   38.480  72.478 1.00 24.83 ?  309 LEU A C     1 
ATOM   2466 O O     . LEU A 1 309 ? 2.747   39.385  71.817 1.00 8.21  ?  309 LEU A O     1 
ATOM   2467 C CB    . LEU A 1 309 ? 0.629   37.196  71.052 1.00 9.21  ?  309 LEU A CB    1 
ATOM   2468 C CG    . LEU A 1 309 ? -0.722  36.544  70.835 1.00 3.01  ?  309 LEU A CG    1 
ATOM   2469 C CD1   . LEU A 1 309 ? -0.742  35.787  69.549 1.00 3.43  ?  309 LEU A CD1   1 
ATOM   2470 C CD2   . LEU A 1 309 ? -0.993  35.635  71.974 1.00 2.47  ?  309 LEU A CD2   1 
ATOM   2471 N N     . SER A 1 310 ? 2.877   37.736  73.369 1.00 34.81 ?  310 SER A N     1 
ATOM   2472 C CA    . SER A 1 310 ? 4.307   37.879  73.622 1.00 36.13 ?  310 SER A CA    1 
ATOM   2473 C C     . SER A 1 310 ? 4.999   36.561  73.304 1.00 43.69 ?  310 SER A C     1 
ATOM   2474 O O     . SER A 1 310 ? 4.807   35.563  74.009 1.00 43.94 ?  310 SER A O     1 
ATOM   2475 C CB    . SER A 1 310 ? 4.585   38.296  75.072 1.00 19.69 ?  310 SER A CB    1 
ATOM   2476 O OG    . SER A 1 310 ? 4.001   37.418  76.014 1.00 13.61 ?  310 SER A OG    1 
ATOM   2477 N N     . VAL A 1 311 ? 5.864   36.586  72.296 1.00 37.87 ?  311 VAL A N     1 
ATOM   2478 C CA    . VAL A 1 311 ? 6.586   35.412  71.830 1.00 3.04  ?  311 VAL A CA    1 
ATOM   2479 C C     . VAL A 1 311 ? 8.034   35.587  72.238 1.00 16.75 ?  311 VAL A C     1 
ATOM   2480 O O     . VAL A 1 311 ? 8.625   36.650  72.015 1.00 33.58 ?  311 VAL A O     1 
ATOM   2481 C CB    . VAL A 1 311 ? 6.465   35.241  70.306 1.00 11.97 ?  311 VAL A CB    1 
ATOM   2482 C CG1   . VAL A 1 311 ? 6.734   36.550  69.595 1.00 26.67 ?  311 VAL A CG1   1 
ATOM   2483 C CG2   . VAL A 1 311 ? 7.454   34.211  69.833 1.00 30.54 ?  311 VAL A CG2   1 
ATOM   2484 N N     . THR A 1 312 ? 8.607   34.555  72.833 1.00 33.44 ?  312 THR A N     1 
ATOM   2485 C CA    . THR A 1 312 ? 10.009  34.597  73.194 1.00 20.50 ?  312 THR A CA    1 
ATOM   2486 C C     . THR A 1 312 ? 10.879  34.249  71.999 1.00 30.77 ?  312 THR A C     1 
ATOM   2487 O O     . THR A 1 312 ? 10.555  33.352  71.213 1.00 40.70 ?  312 THR A O     1 
ATOM   2488 C CB    . THR A 1 312 ? 10.315  33.674  74.362 1.00 14.59 ?  312 THR A CB    1 
ATOM   2489 O OG1   . THR A 1 312 ? 11.723  33.727  74.587 1.00 26.29 ?  312 THR A OG1   1 
ATOM   2490 C CG2   . THR A 1 312 ? 9.902   32.260  74.076 1.00 2.49  ?  312 THR A CG2   1 
ATOM   2491 N N     . LYS A 1 313 ? 11.958  35.007  71.834 1.00 36.13 ?  313 LYS A N     1 
ATOM   2492 C CA    . LYS A 1 313 ? 12.808  34.831  70.666 1.00 25.11 ?  313 LYS A CA    1 
ATOM   2493 C C     . LYS A 1 313 ? 13.555  33.503  70.733 1.00 31.34 ?  313 LYS A C     1 
ATOM   2494 O O     . LYS A 1 313 ? 14.252  33.223  71.727 1.00 3.88  ?  313 LYS A O     1 
ATOM   2495 C CB    . LYS A 1 313 ? 13.807  35.983  70.550 1.00 18.47 ?  313 LYS A CB    1 
ATOM   2496 C CG    . LYS A 1 313 ? 14.331  36.179  69.127 1.00 24.90 ?  313 LYS A CG    1 
ATOM   2497 C CD    . LYS A 1 313 ? 13.238  36.774  68.269 1.00 20.96 ?  313 LYS A CD    1 
ATOM   2498 C CE    . LYS A 1 313 ? 13.768  37.494  67.064 1.00 14.65 ?  313 LYS A CE    1 
ATOM   2499 N NZ    . LYS A 1 313 ? 13.765  36.565  65.941 1.00 13.59 1  313 LYS A NZ    1 
ATOM   2500 N N     . PRO A 1 314 ? 13.440  32.666  69.709 1.00 27.80 ?  314 PRO A N     1 
ATOM   2501 C CA    . PRO A 1 314 ? 14.285  31.474  69.630 1.00 32.83 ?  314 PRO A CA    1 
ATOM   2502 C C     . PRO A 1 314 ? 15.681  31.814  69.128 1.00 24.17 ?  314 PRO A C     1 
ATOM   2503 O O     . PRO A 1 314 ? 15.893  32.770  68.380 1.00 22.67 ?  314 PRO A O     1 
ATOM   2504 C CB    . PRO A 1 314 ? 13.540  30.585  68.626 1.00 40.22 ?  314 PRO A CB    1 
ATOM   2505 C CG    . PRO A 1 314 ? 12.790  31.564  67.762 1.00 40.34 ?  314 PRO A CG    1 
ATOM   2506 C CD    . PRO A 1 314 ? 12.419  32.715  68.648 1.00 22.85 ?  314 PRO A CD    1 
ATOM   2507 N N     . GLU A 1 315 ? 16.632  30.967  69.505 1.00 32.52 ?  315 GLU A N     1 
ATOM   2508 C CA    . GLU A 1 315 ? 18.017  31.077  69.069 1.00 20.86 ?  315 GLU A CA    1 
ATOM   2509 C C     . GLU A 1 315 ? 18.400  29.884  68.209 1.00 17.77 ?  315 GLU A C     1 
ATOM   2510 O O     . GLU A 1 315 ? 19.555  29.770  67.795 1.00 21.71 ?  315 GLU A O     1 
ATOM   2511 C CB    . GLU A 1 315 ? 18.950  31.183  70.282 1.00 4.85  ?  315 GLU A CB    1 
ATOM   2512 C CG    . GLU A 1 315 ? 18.343  31.991  71.425 1.00 4.51  ?  315 GLU A CG    1 
ATOM   2513 C CD    . GLU A 1 315 ? 18.898  31.607  72.788 1.00 8.77  ?  315 GLU A CD    1 
ATOM   2514 O OE1   . GLU A 1 315 ? 18.647  32.332  73.769 1.00 14.01 ?  315 GLU A OE1   1 
ATOM   2515 O OE2   . GLU A 1 315 ? 19.621  30.597  72.879 1.00 4.19  -1 315 GLU A OE2   1 
ATOM   2516 N N     . GLY A 1 316 ? 17.469  28.967  67.972 1.00 20.89 ?  316 GLY A N     1 
ATOM   2517 C CA    . GLY A 1 316 ? 17.712  27.879  67.051 1.00 18.22 ?  316 GLY A CA    1 
ATOM   2518 C C     . GLY A 1 316 ? 16.434  27.158  66.683 1.00 21.54 ?  316 GLY A C     1 
ATOM   2519 O O     . GLY A 1 316 ? 15.338  27.484  67.151 1.00 10.60 ?  316 GLY A O     1 
ATOM   2520 N N     . SER A 1 317 ? 16.615  26.172  65.751 1.00 28.76 ?  317 SER A N     1 
ATOM   2521 C CA    . SER A 1 317 ? 15.613  25.231  65.153 1.00 19.30 ?  317 SER A CA    1 
ATOM   2522 C C     . SER A 1 317 ? 14.532  26.057  64.460 1.00 27.13 ?  317 SER A C     1 
ATOM   2523 O O     . SER A 1 317 ? 14.884  27.119  64.021 1.00 26.37 ?  317 SER A O     1 
ATOM   2524 C CB    . SER A 1 317 ? 15.021  24.327  66.155 1.00 6.50  ?  317 SER A CB    1 
ATOM   2525 O OG    . SER A 1 317 ? 14.608  23.169  65.478 1.00 19.21 ?  317 SER A OG    1 
ATOM   2526 N N     . PHE A 1 318 ? 13.261  25.626  64.480 1.00 29.05 ?  318 PHE A N     1 
ATOM   2527 C CA    . PHE A 1 318 ? 12.216  26.262  63.687 1.00 5.49  ?  318 PHE A CA    1 
ATOM   2528 C C     . PHE A 1 318 ? 10.858  26.237  64.380 1.00 5.06  ?  318 PHE A C     1 
ATOM   2529 O O     . PHE A 1 318 ? 9.826   26.155  63.712 1.00 5.41  ?  318 PHE A O     1 
ATOM   2530 C CB    . PHE A 1 318 ? 12.091  25.592  62.303 1.00 27.84 ?  318 PHE A CB    1 
ATOM   2531 C CG    . PHE A 1 318 ? 12.013  24.057  62.342 1.00 29.85 ?  318 PHE A CG    1 
ATOM   2532 C CD1   . PHE A 1 318 ? 13.154  23.291  62.397 1.00 25.77 ?  318 PHE A CD1   1 
ATOM   2533 C CD2   . PHE A 1 318 ? 10.793  23.397  62.310 1.00 29.46 ?  318 PHE A CD2   1 
ATOM   2534 C CE1   . PHE A 1 318 ? 13.084  21.907  62.426 1.00 29.35 ?  318 PHE A CE1   1 
ATOM   2535 C CE2   . PHE A 1 318 ? 10.728  22.006  62.346 1.00 20.86 ?  318 PHE A CE2   1 
ATOM   2536 C CZ    . PHE A 1 318 ? 11.874  21.268  62.405 1.00 12.33 ?  318 PHE A CZ    1 
ATOM   2537 N N     . LEU A 1 319 ? 10.838  26.323  65.705 1.00 8.68  ?  319 LEU A N     1 
ATOM   2538 C CA    . LEU A 1 319 ? 9.613   26.345  66.497 1.00 4.12  ?  319 LEU A CA    1 
ATOM   2539 C C     . LEU A 1 319 ? 9.551   27.662  67.245 1.00 34.44 ?  319 LEU A C     1 
ATOM   2540 O O     . LEU A 1 319 ? 10.587  28.212  67.643 1.00 33.66 ?  319 LEU A O     1 
ATOM   2541 C CB    . LEU A 1 319 ? 9.565   25.218  67.518 1.00 20.81 ?  319 LEU A CB    1 
ATOM   2542 C CG    . LEU A 1 319 ? 9.829   23.777  67.070 1.00 32.18 ?  319 LEU A CG    1 
ATOM   2543 C CD1   . LEU A 1 319 ? 10.105  22.870  68.273 1.00 21.90 ?  319 LEU A CD1   1 
ATOM   2544 C CD2   . LEU A 1 319 ? 8.668   23.237  66.223 1.00 41.62 ?  319 LEU A CD2   1 
ATOM   2545 N N     . LEU A 1 320 ? 8.336   28.177  67.414 1.00 34.51 ?  320 LEU A N     1 
ATOM   2546 C CA    . LEU A 1 320 ? 8.109   29.468  68.045 1.00 18.41 ?  320 LEU A CA    1 
ATOM   2547 C C     . LEU A 1 320 ? 7.187   29.282  69.237 1.00 16.87 ?  320 LEU A C     1 
ATOM   2548 O O     . LEU A 1 320 ? 6.108   28.694  69.112 1.00 20.49 ?  320 LEU A O     1 
ATOM   2549 C CB    . LEU A 1 320 ? 7.513   30.452  67.043 1.00 26.36 ?  320 LEU A CB    1 
ATOM   2550 C CG    . LEU A 1 320 ? 7.689   31.959  67.246 1.00 27.03 ?  320 LEU A CG    1 
ATOM   2551 C CD1   . LEU A 1 320 ? 8.987   32.491  66.611 1.00 21.38 ?  320 LEU A CD1   1 
ATOM   2552 C CD2   . LEU A 1 320 ? 6.478   32.678  66.690 1.00 4.50  ?  320 LEU A CD2   1 
ATOM   2553 N N     . TRP A 1 321 ? 7.608   29.794  70.377 1.00 11.04 ?  321 TRP A N     1 
ATOM   2554 C CA    . TRP A 1 321 ? 6.942   29.597  71.656 1.00 4.40  ?  321 TRP A CA    1 
ATOM   2555 C C     . TRP A 1 321 ? 6.260   30.914  72.009 1.00 17.98 ?  321 TRP A C     1 
ATOM   2556 O O     . TRP A 1 321 ? 6.939   31.921  72.223 1.00 16.49 ?  321 TRP A O     1 
ATOM   2557 C CB    . TRP A 1 321 ? 7.977   29.203  72.697 1.00 2.26  ?  321 TRP A CB    1 
ATOM   2558 C CG    . TRP A 1 321 ? 7.464   28.936  74.021 1.00 1.90  ?  321 TRP A CG    1 
ATOM   2559 C CD1   . TRP A 1 321 ? 7.767   29.606  75.148 1.00 9.35  ?  321 TRP A CD1   1 
ATOM   2560 C CD2   . TRP A 1 321 ? 6.567   27.878  74.402 1.00 12.05 ?  321 TRP A CD2   1 
ATOM   2561 N NE1   . TRP A 1 321 ? 7.103   29.060  76.219 1.00 18.88 ?  321 TRP A NE1   1 
ATOM   2562 C CE2   . TRP A 1 321 ? 6.361   27.994  75.785 1.00 12.47 ?  321 TRP A CE2   1 
ATOM   2563 C CE3   . TRP A 1 321 ? 5.926   26.848  73.708 1.00 1.91  ?  321 TRP A CE3   1 
ATOM   2564 C CZ2   . TRP A 1 321 ? 5.533   27.131  76.490 1.00 14.55 ?  321 TRP A CZ2   1 
ATOM   2565 C CZ3   . TRP A 1 321 ? 5.101   26.003  74.404 1.00 1.88  ?  321 TRP A CZ3   1 
ATOM   2566 C CH2   . TRP A 1 321 ? 4.911   26.144  75.778 1.00 14.99 ?  321 TRP A CH2   1 
ATOM   2567 N N     . ILE A 1 322 ? 4.925   30.918  72.040 1.00 28.59 ?  322 ILE A N     1 
ATOM   2568 C CA    . ILE A 1 322 ? 4.135   32.148  72.100 1.00 28.61 ?  322 ILE A CA    1 
ATOM   2569 C C     . ILE A 1 322 ? 3.188   32.101  73.297 1.00 22.84 ?  322 ILE A C     1 
ATOM   2570 O O     . ILE A 1 322 ? 2.429   31.138  73.446 1.00 19.56 ?  322 ILE A O     1 
ATOM   2571 C CB    . ILE A 1 322 ? 3.332   32.360  70.802 1.00 19.68 ?  322 ILE A CB    1 
ATOM   2572 C CG1   . ILE A 1 322 ? 4.210   32.161  69.568 1.00 17.55 ?  322 ILE A CG1   1 
ATOM   2573 C CG2   . ILE A 1 322 ? 2.759   33.749  70.780 1.00 29.15 ?  322 ILE A CG2   1 
ATOM   2574 C CD1   . ILE A 1 322 ? 3.435   31.862  68.321 1.00 21.62 ?  322 ILE A CD1   1 
ATOM   2575 N N     . ASP A 1 323 ? 3.168   33.169  74.104 1.00 2.07  ?  323 ASP A N     1 
ATOM   2576 C CA    . ASP A 1 323 ? 2.245   33.228  75.239 1.00 11.60 ?  323 ASP A CA    1 
ATOM   2577 C C     . ASP A 1 323 ? 0.911   33.821  74.822 1.00 16.95 ?  323 ASP A C     1 
ATOM   2578 O O     . ASP A 1 323 ? 0.872   34.872  74.177 1.00 35.15 ?  323 ASP A O     1 
ATOM   2579 C CB    . ASP A 1 323 ? 2.794   34.020  76.424 1.00 8.42  ?  323 ASP A CB    1 
ATOM   2580 C CG    . ASP A 1 323 ? 1.916   33.849  77.665 1.00 25.51 ?  323 ASP A CG    1 
ATOM   2581 O OD1   . ASP A 1 323 ? 0.931   33.086  77.567 1.00 17.89 -1 323 ASP A OD1   1 
ATOM   2582 O OD2   . ASP A 1 323 ? 2.174   34.469  78.719 1.00 30.55 -1 323 ASP A OD2   1 
ATOM   2583 N N     . CYS A 1 324 ? -0.182  33.143  75.208 1.00 19.30 ?  324 CYS A N     1 
ATOM   2584 C CA    . CYS A 1 324 ? -1.548  33.579  74.917 1.00 18.95 ?  324 CYS A CA    1 
ATOM   2585 C C     . CYS A 1 324 ? -2.355  33.900  76.178 1.00 25.79 ?  324 CYS A C     1 
ATOM   2586 O O     . CYS A 1 324 ? -3.590  33.932  76.122 1.00 27.49 ?  324 CYS A O     1 
ATOM   2587 C CB    . CYS A 1 324 ? -2.281  32.497  74.118 1.00 3.89  ?  324 CYS A CB    1 
ATOM   2588 S SG    . CYS A 1 324 ? -1.696  32.206  72.455 1.00 14.15 ?  324 CYS A SG    1 
ATOM   2589 N N     . SER A 1 325 ? -1.684  34.207  77.291 1.00 3.08  ?  325 SER A N     1 
ATOM   2590 C CA    . SER A 1 325 ? -2.367  34.383  78.563 1.00 2.13  ?  325 SER A CA    1 
ATOM   2591 C C     . SER A 1 325 ? -3.099  35.725  78.649 1.00 28.17 ?  325 SER A C     1 
ATOM   2592 O O     . SER A 1 325 ? -4.117  35.833  79.343 1.00 16.67 ?  325 SER A O     1 
ATOM   2593 C CB    . SER A 1 325 ? -1.374  34.253  79.705 1.00 18.03 ?  325 SER A CB    1 
ATOM   2594 O OG    . SER A 1 325 ? -0.382  35.260  79.586 1.00 39.20 ?  325 SER A OG    1 
ATOM   2595 N N     . ALA A 1 326 ? -2.610  36.769  77.982 1.00 30.12 ?  326 ALA A N     1 
ATOM   2596 C CA    . ALA A 1 326 ? -3.361  38.015  78.071 1.00 20.22 ?  326 ALA A CA    1 
ATOM   2597 C C     . ALA A 1 326 ? -4.766  37.844  77.504 1.00 16.69 ?  326 ALA A C     1 
ATOM   2598 O O     . ALA A 1 326 ? -5.664  38.622  77.843 1.00 18.50 ?  326 ALA A O     1 
ATOM   2599 C CB    . ALA A 1 326 ? -2.608  39.154  77.375 1.00 9.62  ?  326 ALA A CB    1 
ATOM   2600 N N     . LEU A 1 327 ? -4.991  36.798  76.705 1.00 11.50 ?  327 LEU A N     1 
ATOM   2601 C CA    . LEU A 1 327 ? -6.323  36.546  76.167 1.00 10.99 ?  327 LEU A CA    1 
ATOM   2602 C C     . LEU A 1 327 ? -7.248  35.926  77.205 1.00 22.49 ?  327 LEU A C     1 
ATOM   2603 O O     . LEU A 1 327 ? -8.472  36.020  77.065 1.00 32.89 ?  327 LEU A O     1 
ATOM   2604 C CB    . LEU A 1 327 ? -6.253  35.654  74.930 1.00 5.16  ?  327 LEU A CB    1 
ATOM   2605 C CG    . LEU A 1 327 ? -5.334  36.177  73.826 1.00 12.45 ?  327 LEU A CG    1 
ATOM   2606 C CD1   . LEU A 1 327 ? -5.753  35.583  72.523 1.00 5.19  ?  327 LEU A CD1   1 
ATOM   2607 C CD2   . LEU A 1 327 ? -5.342  37.683  73.740 1.00 29.95 ?  327 LEU A CD2   1 
ATOM   2608 N N     . ASN A 1 328 ? -6.692  35.315  78.246 1.00 24.23 ?  328 ASN A N     1 
ATOM   2609 C CA    . ASN A 1 328 ? -7.470  34.702  79.312 1.00 16.06 ?  328 ASN A CA    1 
ATOM   2610 C C     . ASN A 1 328 ? -8.518  33.762  78.728 1.00 20.49 ?  328 ASN A C     1 
ATOM   2611 O O     . ASN A 1 328 ? -9.722  34.005  78.792 1.00 31.48 ?  328 ASN A O     1 
ATOM   2612 C CB    . ASN A 1 328 ? -8.104  35.759  80.212 1.00 19.80 ?  328 ASN A CB    1 
ATOM   2613 C CG    . ASN A 1 328 ? -8.501  35.211  81.565 1.00 28.43 ?  328 ASN A CG    1 
ATOM   2614 O OD1   . ASN A 1 328 ? -9.472  34.475  81.691 1.00 48.30 ?  328 ASN A OD1   1 
ATOM   2615 N ND2   . ASN A 1 328 ? -7.734  35.554  82.583 1.00 32.67 ?  328 ASN A ND2   1 
ATOM   2616 N N     . LEU A 1 329 ? -8.009  32.735  78.060 1.00 26.57 ?  329 LEU A N     1 
ATOM   2617 C CA    . LEU A 1 329 ? -8.799  31.659  77.497 1.00 23.47 ?  329 LEU A CA    1 
ATOM   2618 C C     . LEU A 1 329 ? -8.254  30.332  78.004 1.00 29.76 ?  329 LEU A C     1 
ATOM   2619 O O     . LEU A 1 329 ? -7.029  30.154  78.129 1.00 8.39  ?  329 LEU A O     1 
ATOM   2620 C CB    . LEU A 1 329 ? -8.767  31.662  75.964 1.00 22.91 ?  329 LEU A CB    1 
ATOM   2621 C CG    . LEU A 1 329 ? -8.731  32.987  75.206 1.00 25.39 ?  329 LEU A CG    1 
ATOM   2622 C CD1   . LEU A 1 329 ? -8.201  32.795  73.784 1.00 24.48 ?  329 LEU A CD1   1 
ATOM   2623 C CD2   . LEU A 1 329 ? -10.090 33.673  75.196 1.00 29.21 ?  329 LEU A CD2   1 
ATOM   2624 N N     . SER A 1 330 ? -9.176  29.403  78.269 1.00 24.23 ?  330 SER A N     1 
ATOM   2625 C CA    . SER A 1 330 ? -8.814  28.024  78.546 1.00 21.73 ?  330 SER A CA    1 
ATOM   2626 C C     . SER A 1 330 ? -8.329  27.378  77.261 1.00 13.38 ?  330 SER A C     1 
ATOM   2627 O O     . SER A 1 330 ? -8.586  27.867  76.159 1.00 12.51 ?  330 SER A O     1 
ATOM   2628 C CB    . SER A 1 330 ? -10.004 27.247  79.115 1.00 40.13 ?  330 SER A CB    1 
ATOM   2629 O OG    . SER A 1 330 ? -11.201 27.400  78.342 1.00 28.64 ?  330 SER A OG    1 
ATOM   2630 N N     . GLN A 1 331 ? -7.660  26.263  77.397 1.00 2.54  ?  331 GLN A N     1 
ATOM   2631 C CA    . GLN A 1 331 ? -7.098  25.568  76.235 1.00 2.51  ?  331 GLN A CA    1 
ATOM   2632 C C     . GLN A 1 331 ? -8.189  25.301  75.217 1.00 21.74 ?  331 GLN A C     1 
ATOM   2633 O O     . GLN A 1 331 ? -7.984  25.690  74.122 1.00 2.69  ?  331 GLN A O     1 
ATOM   2634 C CB    . GLN A 1 331 ? -6.448  24.292  76.720 1.00 11.67 ?  331 GLN A CB    1 
ATOM   2635 C CG    . GLN A 1 331 ? -5.974  23.376  75.611 1.00 17.30 ?  331 GLN A CG    1 
ATOM   2636 C CD    . GLN A 1 331 ? -5.379  22.120  76.184 1.00 8.45  ?  331 GLN A CD    1 
ATOM   2637 O OE1   . GLN A 1 331 ? -5.404  21.884  77.382 1.00 2.33  ?  331 GLN A OE1   1 
ATOM   2638 N NE2   . GLN A 1 331 ? -4.826  21.305  75.316 1.00 10.85 ?  331 GLN A NE2   1 
ATOM   2639 N N     . ASP A 1 332 ? -9.334  24.717  75.634 1.00 29.46 ?  332 ASP A N     1 
ATOM   2640 C CA    . ASP A 1 332 ? -10.419 24.397  74.711 1.00 10.48 ?  332 ASP A CA    1 
ATOM   2641 C C     . ASP A 1 332 ? -11.073 25.655  74.173 1.00 15.35 ?  332 ASP A C     1 
ATOM   2642 O O     . ASP A 1 332 ? -11.383 25.731  72.978 1.00 25.62 ?  332 ASP A O     1 
ATOM   2643 C CB    . ASP A 1 332 ? -11.416 23.464  75.385 1.00 17.35 ?  332 ASP A CB    1 
ATOM   2644 C CG    . ASP A 1 332 ? -10.999 21.993  75.256 1.00 37.04 ?  332 ASP A CG    1 
ATOM   2645 O OD1   . ASP A 1 332 ? -10.899 21.509  74.106 1.00 37.63 ?  332 ASP A OD1   1 
ATOM   2646 O OD2   . ASP A 1 332 ? -10.760 21.322  76.287 1.00 38.58 -1 332 ASP A OD2   1 
ATOM   2647 N N     . GLU A 1 333 ? -11.213 26.681  75.019 1.00 33.20 ?  333 GLU A N     1 
ATOM   2648 C CA    . GLU A 1 333 ? -11.611 27.995  74.522 1.00 27.87 ?  333 GLU A CA    1 
ATOM   2649 C C     . GLU A 1 333 ? -10.645 28.446  73.435 1.00 22.48 ?  333 GLU A C     1 
ATOM   2650 O O     . GLU A 1 333 ? -11.058 28.799  72.327 1.00 31.82 ?  333 GLU A O     1 
ATOM   2651 C CB    . GLU A 1 333 ? -11.614 29.014  75.670 1.00 33.17 ?  333 GLU A CB    1 
ATOM   2652 C CG    . GLU A 1 333 ? -12.932 29.174  76.429 1.00 46.60 ?  333 GLU A CG    1 
ATOM   2653 C CD    . GLU A 1 333 ? -12.850 30.106  77.657 1.00 41.68 ?  333 GLU A CD    1 
ATOM   2654 O OE1   . GLU A 1 333 ? -11.741 30.520  78.070 1.00 33.94 ?  333 GLU A OE1   1 
ATOM   2655 O OE2   . GLU A 1 333 ? -13.921 30.404  78.225 1.00 34.54 -1 333 GLU A OE2   1 
ATOM   2656 N N     . ARG A 1 334 ? -9.340  28.345  73.712 1.00 6.92  ?  334 ARG A N     1 
ATOM   2657 C CA    . ARG A 1 334 ? -8.325  28.781  72.756 1.00 8.56  ?  334 ARG A CA    1 
ATOM   2658 C C     . ARG A 1 334 ? -8.276  27.862  71.538 1.00 17.17 ?  334 ARG A C     1 
ATOM   2659 O O     . ARG A 1 334 ? -8.247  28.335  70.396 1.00 27.63 ?  334 ARG A O     1 
ATOM   2660 C CB    . ARG A 1 334 ? -6.965  28.848  73.461 1.00 8.16  ?  334 ARG A CB    1 
ATOM   2661 C CG    . ARG A 1 334 ? -5.781  29.305  72.626 1.00 26.14 ?  334 ARG A CG    1 
ATOM   2662 C CD    . ARG A 1 334 ? -4.432  29.047  73.371 1.00 26.01 ?  334 ARG A CD    1 
ATOM   2663 N NE    . ARG A 1 334 ? -4.010  27.642  73.416 1.00 12.39 ?  334 ARG A NE    1 
ATOM   2664 C CZ    . ARG A 1 334 ? -3.864  26.927  74.535 1.00 16.01 ?  334 ARG A CZ    1 
ATOM   2665 N NH1   . ARG A 1 334 ? -4.113  27.465  75.723 1.00 2.57  1  334 ARG A NH1   1 
ATOM   2666 N NH2   . ARG A 1 334 ? -3.441  25.665  74.468 1.00 2.24  ?  334 ARG A NH2   1 
ATOM   2667 N N     . THR A 1 335 ? -8.277  26.546  71.756 1.00 3.20  ?  335 THR A N     1 
ATOM   2668 C CA    . THR A 1 335 ? -8.117  25.612  70.645 1.00 5.28  ?  335 THR A CA    1 
ATOM   2669 C C     . THR A 1 335 ? -9.265  25.720  69.648 1.00 18.81 ?  335 THR A C     1 
ATOM   2670 O O     . THR A 1 335 ? -9.038  25.843  68.440 1.00 23.23 ?  335 THR A O     1 
ATOM   2671 C CB    . THR A 1 335 ? -8.028  24.189  71.181 1.00 11.07 ?  335 THR A CB    1 
ATOM   2672 O OG1   . THR A 1 335 ? -7.344  24.203  72.434 1.00 6.93  ?  335 THR A OG1   1 
ATOM   2673 C CG2   . THR A 1 335 ? -7.277  23.311  70.217 1.00 26.43 ?  335 THR A CG2   1 
ATOM   2674 N N     . LYS A 1 336 ? -10.510 25.675  70.146 1.00 9.67  ?  336 LYS A N     1 
ATOM   2675 C CA    . LYS A 1 336 ? -11.686 25.757  69.287 1.00 8.92  ?  336 LYS A CA    1 
ATOM   2676 C C     . LYS A 1 336 ? -11.652 26.998  68.405 1.00 25.85 ?  336 LYS A C     1 
ATOM   2677 O O     . LYS A 1 336 ? -11.990 26.933  67.220 1.00 31.53 ?  336 LYS A O     1 
ATOM   2678 C CB    . LYS A 1 336 ? -12.959 25.745  70.141 1.00 27.10 ?  336 LYS A CB    1 
ATOM   2679 C CG    . LYS A 1 336 ? -13.429 24.349  70.550 1.00 28.50 ?  336 LYS A CG    1 
ATOM   2680 C CD    . LYS A 1 336 ? -14.352 24.394  71.757 1.00 29.87 ?  336 LYS A CD    1 
ATOM   2681 C CE    . LYS A 1 336 ? -15.018 23.043  71.969 1.00 24.69 ?  336 LYS A CE    1 
ATOM   2682 N NZ    . LYS A 1 336 ? -15.824 22.708  70.782 1.00 23.57 1  336 LYS A NZ    1 
ATOM   2683 N N     . LEU A 1 337 ? -11.255 28.144  68.962 1.00 26.02 ?  337 LEU A N     1 
ATOM   2684 C CA    . LEU A 1 337 ? -11.191 29.348  68.144 1.00 17.47 ?  337 LEU A CA    1 
ATOM   2685 C C     . LEU A 1 337 ? -10.219 29.163  66.989 1.00 23.07 ?  337 LEU A C     1 
ATOM   2686 O O     . LEU A 1 337 ? -10.518 29.544  65.852 1.00 28.00 ?  337 LEU A O     1 
ATOM   2687 C CB    . LEU A 1 337 ? -10.800 30.558  68.998 1.00 15.83 ?  337 LEU A CB    1 
ATOM   2688 C CG    . LEU A 1 337 ? -11.857 30.989  70.028 1.00 13.95 ?  337 LEU A CG    1 
ATOM   2689 C CD1   . LEU A 1 337 ? -11.321 31.952  71.070 1.00 5.22  ?  337 LEU A CD1   1 
ATOM   2690 C CD2   . LEU A 1 337 ? -13.109 31.549  69.363 1.00 26.20 ?  337 LEU A CD2   1 
ATOM   2691 N N     . LEU A 1 338 ? -9.071  28.528  67.247 1.00 22.61 ?  338 LEU A N     1 
ATOM   2692 C CA    . LEU A 1 338 ? -8.081  28.322  66.192 1.00 10.23 ?  338 LEU A CA    1 
ATOM   2693 C C     . LEU A 1 338 ? -8.574  27.372  65.110 1.00 5.84  ?  338 LEU A C     1 
ATOM   2694 O O     . LEU A 1 338 ? -8.325  27.606  63.924 1.00 6.93  ?  338 LEU A O     1 
ATOM   2695 C CB    . LEU A 1 338 ? -6.783  27.802  66.796 1.00 8.90  ?  338 LEU A CB    1 
ATOM   2696 C CG    . LEU A 1 338 ? -6.056  28.820  67.662 1.00 14.44 ?  338 LEU A CG    1 
ATOM   2697 C CD1   . LEU A 1 338 ? -5.212  28.116  68.714 1.00 9.87  ?  338 LEU A CD1   1 
ATOM   2698 C CD2   . LEU A 1 338 ? -5.214  29.740  66.777 1.00 12.27 ?  338 LEU A CD2   1 
ATOM   2699 N N     . GLU A 1 339 ? -9.266  26.292  65.484 1.00 17.78 ?  339 GLU A N     1 
ATOM   2700 C CA    . GLU A 1 339 ? -9.735  25.335  64.478 1.00 20.31 ?  339 GLU A CA    1 
ATOM   2701 C C     . GLU A 1 339 ? -11.034 25.786  63.815 1.00 24.28 ?  339 GLU A C     1 
ATOM   2702 O O     . GLU A 1 339 ? -11.252 25.542  62.628 1.00 21.22 ?  339 GLU A O     1 
ATOM   2703 C CB    . GLU A 1 339 ? -9.911  23.946  65.077 1.00 26.58 ?  339 GLU A CB    1 
ATOM   2704 C CG    . GLU A 1 339 ? -9.809  22.875  63.998 1.00 46.49 ?  339 GLU A CG    1 
ATOM   2705 C CD    . GLU A 1 339 ? -10.697 21.659  64.223 1.00 54.86 ?  339 GLU A CD    1 
ATOM   2706 O OE1   . GLU A 1 339 ? -10.504 20.960  65.242 1.00 56.68 ?  339 GLU A OE1   1 
ATOM   2707 O OE2   . GLU A 1 339 ? -11.566 21.382  63.363 1.00 50.70 -1 339 GLU A OE2   1 
ATOM   2708 N N     . GLU A 1 340 ? -11.945 26.364  64.596 1.00 40.45 ?  340 GLU A N     1 
ATOM   2709 C CA    . GLU A 1 340 ? -13.186 26.931  64.059 1.00 37.94 ?  340 GLU A CA    1 
ATOM   2710 C C     . GLU A 1 340 ? -12.923 28.210  63.284 1.00 22.43 ?  340 GLU A C     1 
ATOM   2711 O O     . GLU A 1 340 ? -13.142 28.276  62.073 1.00 29.38 ?  340 GLU A O     1 
ATOM   2712 C CB    . GLU A 1 340 ? -14.179 27.229  65.189 1.00 48.69 ?  340 GLU A CB    1 
ATOM   2713 C CG    . GLU A 1 340 ? -14.938 26.041  65.738 1.00 50.47 ?  340 GLU A CG    1 
ATOM   2714 C CD    . GLU A 1 340 ? -15.965 26.468  66.768 1.00 47.30 ?  340 GLU A CD    1 
ATOM   2715 O OE1   . GLU A 1 340 ? -16.002 27.665  67.133 1.00 43.41 ?  340 GLU A OE1   1 
ATOM   2716 O OE2   . GLU A 1 340 ? -16.732 25.600  67.222 1.00 51.89 -1 340 GLU A OE2   1 
ATOM   2717 N N     . LYS A 1 341 ? -12.463 29.245  63.979 1.00 23.83 ?  341 LYS A N     1 
ATOM   2718 C CA    . LYS A 1 341 ? -12.343 30.567  63.380 1.00 33.35 ?  341 LYS A CA    1 
ATOM   2719 C C     . LYS A 1 341 ? -10.996 30.773  62.701 1.00 30.08 ?  341 LYS A C     1 
ATOM   2720 O O     . LYS A 1 341 ? -10.940 31.291  61.582 1.00 26.95 ?  341 LYS A O     1 
ATOM   2721 C CB    . LYS A 1 341 ? -12.540 31.642  64.462 1.00 34.26 ?  341 LYS A CB    1 
ATOM   2722 C CG    . LYS A 1 341 ? -12.979 33.028  63.975 1.00 28.64 ?  341 LYS A CG    1 
ATOM   2723 C CD    . LYS A 1 341 ? -13.017 34.040  65.140 1.00 12.25 ?  341 LYS A CD    1 
ATOM   2724 C CE    . LYS A 1 341 ? -13.572 35.397  64.687 1.00 16.48 ?  341 LYS A CE    1 
ATOM   2725 N NZ    . LYS A 1 341 ? -13.781 36.354  65.808 1.00 17.46 1  341 LYS A NZ    1 
ATOM   2726 N N     . GLY A 1 342 ? -9.911  30.315  63.320 1.00 34.22 ?  342 GLY A N     1 
ATOM   2727 C CA    . GLY A 1 342 ? -8.604  30.480  62.709 1.00 39.31 ?  342 GLY A CA    1 
ATOM   2728 C C     . GLY A 1 342 ? -8.392  29.610  61.490 1.00 41.68 ?  342 GLY A C     1 
ATOM   2729 O O     . GLY A 1 342 ? -7.695  30.012  60.553 1.00 47.46 ?  342 GLY A O     1 
ATOM   2730 N N     . LYS A 1 343 ? -8.986  28.416  61.485 1.00 28.28 ?  343 LYS A N     1 
ATOM   2731 C CA    . LYS A 1 343 ? -8.752  27.413  60.448 1.00 19.42 ?  343 LYS A CA    1 
ATOM   2732 C C     . LYS A 1 343 ? -7.259  27.089  60.351 1.00 14.33 ?  343 LYS A C     1 
ATOM   2733 O O     . LYS A 1 343 ? -6.668  27.091  59.271 1.00 12.50 ?  343 LYS A O     1 
ATOM   2734 C CB    . LYS A 1 343 ? -9.318  27.852  59.092 1.00 14.87 ?  343 LYS A CB    1 
ATOM   2735 C CG    . LYS A 1 343 ? -10.621 28.681  59.134 1.00 27.73 ?  343 LYS A CG    1 
ATOM   2736 C CD    . LYS A 1 343 ? -11.821 27.857  58.659 1.00 33.56 ?  343 LYS A CD    1 
ATOM   2737 C CE    . LYS A 1 343 ? -13.165 28.498  59.005 1.00 30.44 ?  343 LYS A CE    1 
ATOM   2738 N NZ    . LYS A 1 343 ? -14.271 27.483  59.204 1.00 25.00 1  343 LYS A NZ    1 
ATOM   2739 N N     . ILE A 1 344 ? -6.646  26.843  61.511 1.00 16.60 ?  344 ILE A N     1 
ATOM   2740 C CA    . ILE A 1 344 ? -5.217  26.547  61.610 1.00 24.65 ?  344 ILE A CA    1 
ATOM   2741 C C     . ILE A 1 344 ? -4.976  25.619  62.798 1.00 30.02 ?  344 ILE A C     1 
ATOM   2742 O O     . ILE A 1 344 ? -5.589  25.774  63.856 1.00 39.25 ?  344 ILE A O     1 
ATOM   2743 C CB    . ILE A 1 344 ? -4.361  27.831  61.738 1.00 25.78 ?  344 ILE A CB    1 
ATOM   2744 C CG1   . ILE A 1 344 ? -2.930  27.467  62.091 1.00 15.49 ?  344 ILE A CG1   1 
ATOM   2745 C CG2   . ILE A 1 344 ? -4.925  28.794  62.787 1.00 31.71 ?  344 ILE A CG2   1 
ATOM   2746 C CD1   . ILE A 1 344 ? -1.985  28.575  61.875 1.00 32.05 ?  344 ILE A CD1   1 
ATOM   2747 N N     . ILE A 1 345 ? -4.064  24.665  62.633 1.00 33.74 ?  345 ILE A N     1 
ATOM   2748 C CA    . ILE A 1 345 ? -3.718  23.724  63.694 1.00 23.50 ?  345 ILE A CA    1 
ATOM   2749 C C     . ILE A 1 345 ? -2.293  24.018  64.154 1.00 13.81 ?  345 ILE A C     1 
ATOM   2750 O O     . ILE A 1 345 ? -1.337  23.893  63.381 1.00 7.49  ?  345 ILE A O     1 
ATOM   2751 C CB    . ILE A 1 345 ? -3.887  22.269  63.232 1.00 22.44 ?  345 ILE A CB    1 
ATOM   2752 C CG1   . ILE A 1 345 ? -5.295  22.109  62.692 1.00 13.68 ?  345 ILE A CG1   1 
ATOM   2753 C CG2   . ILE A 1 345 ? -3.723  21.311  64.404 1.00 14.00 ?  345 ILE A CG2   1 
ATOM   2754 C CD1   . ILE A 1 345 ? -6.319  22.487  63.708 1.00 7.16  ?  345 ILE A CD1   1 
ATOM   2755 N N     . VAL A 1 346 ? -2.164  24.426  65.414 1.00 16.38 ?  346 VAL A N     1 
ATOM   2756 C CA    . VAL A 1 346 ? -0.891  24.696  66.060 1.00 15.21 ?  346 VAL A CA    1 
ATOM   2757 C C     . VAL A 1 346 ? -0.723  23.732  67.238 1.00 16.30 ?  346 VAL A C     1 
ATOM   2758 O O     . VAL A 1 346 ? -1.599  22.930  67.547 1.00 13.08 ?  346 VAL A O     1 
ATOM   2759 C CB    . VAL A 1 346 ? -0.786  26.167  66.529 1.00 19.89 ?  346 VAL A CB    1 
ATOM   2760 C CG1   . VAL A 1 346 ? -0.621  27.101  65.343 1.00 4.40  ?  346 VAL A CG1   1 
ATOM   2761 C CG2   . VAL A 1 346 ? -2.017  26.545  67.312 1.00 16.71 ?  346 VAL A CG2   1 
ATOM   2762 N N     . GLU A 1 347 ? 0.409   23.878  67.900 1.00 21.12 ?  347 GLU A N     1 
ATOM   2763 C CA    . GLU A 1 347 ? 0.741   22.982  69.017 1.00 20.79 ?  347 GLU A CA    1 
ATOM   2764 C C     . GLU A 1 347 ? 0.244   23.541  70.341 1.00 25.90 ?  347 GLU A C     1 
ATOM   2765 O O     . GLU A 1 347 ? 0.632   24.636  70.656 1.00 40.58 ?  347 GLU A O     1 
ATOM   2766 C CB    . GLU A 1 347 ? 2.212   22.583  69.019 1.00 14.14 ?  347 GLU A CB    1 
ATOM   2767 C CG    . GLU A 1 347 ? 2.431   21.148  69.402 1.00 18.62 ?  347 GLU A CG    1 
ATOM   2768 C CD    . GLU A 1 347 ? 1.681   20.151  68.547 1.00 25.47 ?  347 GLU A CD    1 
ATOM   2769 O OE1   . GLU A 1 347 ? 2.249   19.697  67.574 1.00 25.78 ?  347 GLU A OE1   1 
ATOM   2770 O OE2   . GLU A 1 347 ? 0.553   19.803  68.887 1.00 18.21 -1 347 GLU A OE2   1 
ATOM   2771 N N     . PRO A 1 348 ? -0.660  22.881  71.095 1.00 16.12 ?  348 PRO A N     1 
ATOM   2772 C CA    . PRO A 1 348 ? -0.955  23.347  72.459 1.00 10.94 ?  348 PRO A CA    1 
ATOM   2773 C C     . PRO A 1 348 ? 0.235   23.156  73.399 1.00 15.15 ?  348 PRO A C     1 
ATOM   2774 O O     . PRO A 1 348 ? 1.025   22.215  73.263 1.00 17.48 ?  348 PRO A O     1 
ATOM   2775 C CB    . PRO A 1 348 ? -2.161  22.499  72.887 1.00 4.63  ?  348 PRO A CB    1 
ATOM   2776 C CG    . PRO A 1 348 ? -2.203  21.376  71.925 1.00 2.23  ?  348 PRO A CG    1 
ATOM   2777 C CD    . PRO A 1 348 ? -1.590  21.832  70.649 1.00 28.38 ?  348 PRO A CD    1 
ATOM   2778 N N     . GLY A 1 349 ? 0.394   24.120  74.304 1.00 14.01 ?  349 GLY A N     1 
ATOM   2779 C CA    . GLY A 1 349 ? 1.495   24.190  75.228 1.00 10.20 ?  349 GLY A CA    1 
ATOM   2780 C C     . GLY A 1 349 ? 1.323   23.447  76.533 1.00 23.58 ?  349 GLY A C     1 
ATOM   2781 O O     . GLY A 1 349 ? 2.324   23.062  77.149 1.00 31.17 ?  349 GLY A O     1 
ATOM   2782 N N     . GLU A 1 350 ? 0.066   23.223  76.949 1.00 2.16  ?  350 GLU A N     1 
ATOM   2783 C CA    . GLU A 1 350 ? -0.220  22.665  78.272 1.00 1.91  ?  350 GLU A CA    1 
ATOM   2784 C C     . GLU A 1 350 ? 0.337   21.255  78.424 1.00 14.77 ?  350 GLU A C     1 
ATOM   2785 O O     . GLU A 1 350 ? 0.618   20.800  79.538 1.00 22.03 ?  350 GLU A O     1 
ATOM   2786 C CB    . GLU A 1 350 ? -1.731  22.632  78.540 1.00 17.09 ?  350 GLU A CB    1 
ATOM   2787 C CG    . GLU A 1 350 ? -2.487  23.990  78.701 1.00 2.05  ?  350 GLU A CG    1 
ATOM   2788 C CD    . GLU A 1 350 ? -2.882  24.687  77.402 1.00 5.40  ?  350 GLU A CD    1 
ATOM   2789 O OE1   . GLU A 1 350 ? -3.405  25.807  77.525 1.00 11.07 ?  350 GLU A OE1   1 
ATOM   2790 O OE2   . GLU A 1 350 ? -2.714  24.140  76.287 1.00 6.49  -1 350 GLU A OE2   1 
ATOM   2791 N N     . LYS A 1 351 ? 0.579   20.600  77.301 1.00 11.98 ?  351 LYS A N     1 
ATOM   2792 C CA    . LYS A 1 351 ? 1.134   19.231  77.263 1.00 14.29 ?  351 LYS A CA    1 
ATOM   2793 C C     . LYS A 1 351 ? 2.665   19.244  77.373 1.00 15.66 ?  351 LYS A C     1 
ATOM   2794 O O     . LYS A 1 351 ? 3.277   18.177  77.290 1.00 19.09 ?  351 LYS A O     1 
ATOM   2795 C CB    . LYS A 1 351 ? 0.691   18.627  75.936 1.00 1.89  ?  351 LYS A CB    1 
ATOM   2796 C CG    . LYS A 1 351 ? 1.031   19.428  74.708 1.00 1.91  ?  351 LYS A CG    1 
ATOM   2797 C CD    . LYS A 1 351 ? 0.898   18.573  73.510 1.00 4.88  ?  351 LYS A CD    1 
ATOM   2798 C CE    . LYS A 1 351 ? 2.047   18.766  72.560 1.00 7.80  ?  351 LYS A CE    1 
ATOM   2799 N NZ    . LYS A 1 351 ? 1.569   18.560  71.184 1.00 22.97 1  351 LYS A NZ    1 
ATOM   2800 N N     . TYR A 1 352 ? 3.256   20.417  77.518 1.00 10.38 ?  352 TYR A N     1 
ATOM   2801 C CA    . TYR A 1 352 ? 4.698   20.486  77.734 1.00 1.70  ?  352 TYR A CA    1 
ATOM   2802 C C     . TYR A 1 352 ? 5.053   20.590  79.199 1.00 1.65  ?  352 TYR A C     1 
ATOM   2803 O O     . TYR A 1 352 ? 6.232   20.564  79.528 1.00 26.46 ?  352 TYR A O     1 
ATOM   2804 C CB    . TYR A 1 352 ? 5.301   21.674  76.984 1.00 1.72  ?  352 TYR A CB    1 
ATOM   2805 C CG    . TYR A 1 352 ? 5.266   21.494  75.504 1.00 8.30  ?  352 TYR A CG    1 
ATOM   2806 C CD1   . TYR A 1 352 ? 6.248   20.777  74.863 1.00 1.76  ?  352 TYR A CD1   1 
ATOM   2807 C CD2   . TYR A 1 352 ? 4.239   22.015  74.744 1.00 12.33 ?  352 TYR A CD2   1 
ATOM   2808 C CE1   . TYR A 1 352 ? 6.226   20.580  73.522 1.00 1.82  ?  352 TYR A CE1   1 
ATOM   2809 C CE2   . TYR A 1 352 ? 4.216   21.820  73.377 1.00 10.82 ?  352 TYR A CE2   1 
ATOM   2810 C CZ    . TYR A 1 352 ? 5.226   21.090  72.780 1.00 1.88  ?  352 TYR A CZ    1 
ATOM   2811 O OH    . TYR A 1 352 ? 5.274   20.865  71.425 1.00 5.59  ?  352 TYR A OH    1 
ATOM   2812 N N     . GLY A 1 353 ? 4.062   20.603  80.077 1.00 4.14  ?  353 GLY A N     1 
ATOM   2813 C CA    . GLY A 1 353 ? 4.268   20.748  81.503 1.00 1.64  ?  353 GLY A CA    1 
ATOM   2814 C C     . GLY A 1 353 ? 4.311   22.178  81.998 1.00 5.15  ?  353 GLY A C     1 
ATOM   2815 O O     . GLY A 1 353 ? 4.015   23.140  81.290 1.00 9.25  ?  353 GLY A O     1 
ATOM   2816 N N     . LEU A 1 354 ? 4.754   22.305  83.246 1.00 10.70 ?  354 LEU A N     1 
ATOM   2817 C CA    . LEU A 1 354 ? 4.676   23.568  83.958 1.00 9.78  ?  354 LEU A CA    1 
ATOM   2818 C C     . LEU A 1 354 ? 5.262   24.688  83.109 1.00 16.42 ?  354 LEU A C     1 
ATOM   2819 O O     . LEU A 1 354 ? 6.385   24.577  82.610 1.00 32.98 ?  354 LEU A O     1 
ATOM   2820 C CB    . LEU A 1 354 ? 5.420   23.468  85.299 1.00 7.13  ?  354 LEU A CB    1 
ATOM   2821 C CG    . LEU A 1 354 ? 4.831   22.607  86.409 1.00 1.60  ?  354 LEU A CG    1 
ATOM   2822 C CD1   . LEU A 1 354 ? 5.626   22.832  87.658 1.00 4.35  ?  354 LEU A CD1   1 
ATOM   2823 C CD2   . LEU A 1 354 ? 3.451   23.024  86.634 1.00 13.17 ?  354 LEU A CD2   1 
ATOM   2824 N N     . GLY A 1 355 ? 4.455   25.740  82.883 1.00 20.85 ?  355 GLY A N     1 
ATOM   2825 C CA    . GLY A 1 355 ? 4.830   26.821  81.994 1.00 13.21 ?  355 GLY A CA    1 
ATOM   2826 C C     . GLY A 1 355 ? 4.346   26.672  80.569 1.00 17.32 ?  355 GLY A C     1 
ATOM   2827 O O     . GLY A 1 355 ? 4.744   27.478  79.711 1.00 8.33  ?  355 GLY A O     1 
ATOM   2828 N N     . GLY A 1 356 ? 3.622   25.593  80.264 1.00 1.72  ?  356 GLY A N     1 
ATOM   2829 C CA    . GLY A 1 356 ? 3.012   25.395  78.968 1.00 1.77  ?  356 GLY A CA    1 
ATOM   2830 C C     . GLY A 1 356 ? 1.554   25.813  78.987 1.00 13.32 ?  356 GLY A C     1 
ATOM   2831 O O     . GLY A 1 356 ? 0.904   25.882  77.945 1.00 8.24  ?  356 GLY A O     1 
ATOM   2832 N N     . GLU A 1 357 ? 1.026   26.060  80.184 1.00 1.84  ?  357 GLU A N     1 
ATOM   2833 C CA    . GLU A 1 357 ? -0.328  26.561  80.323 1.00 1.99  ?  357 GLU A CA    1 
ATOM   2834 C C     . GLU A 1 357 ? -0.485  27.901  79.602 1.00 11.93 ?  357 GLU A C     1 
ATOM   2835 O O     . GLU A 1 357 ? 0.336   28.808  79.755 1.00 28.24 ?  357 GLU A O     1 
ATOM   2836 C CB    . GLU A 1 357 ? -0.691  26.698  81.808 1.00 9.14  ?  357 GLU A CB    1 
ATOM   2837 C CG    . GLU A 1 357 ? 0.417   27.192  82.739 1.00 26.09 ?  357 GLU A CG    1 
ATOM   2838 C CD    . GLU A 1 357 ? 0.991   26.087  83.608 1.00 35.22 ?  357 GLU A CD    1 
ATOM   2839 O OE1   . GLU A 1 357 ? 1.586   25.150  83.048 1.00 42.93 ?  357 GLU A OE1   1 
ATOM   2840 O OE2   . GLU A 1 357 ? 0.845   26.148  84.847 1.00 31.53 -1 357 GLU A OE2   1 
ATOM   2841 N N     . GLU A 1 358 ? -1.567  27.979  78.768 1.00 12.97 ?  358 GLU A N     1 
ATOM   2842 C CA    . GLU A 1 358 ? -2.049  29.129  77.927 1.00 17.85 ?  358 GLU A CA    1 
ATOM   2843 C C     . GLU A 1 358 ? -0.985  29.548  76.905 1.00 26.49 ?  358 GLU A C     1 
ATOM   2844 O O     . GLU A 1 358 ? -0.995  30.693  76.535 1.00 26.70 ?  358 GLU A O     1 
ATOM   2845 C CB    . GLU A 1 358 ? -2.473  30.293  78.815 1.00 25.36 ?  358 GLU A CB    1 
ATOM   2846 C CG    . GLU A 1 358 ? -3.076  29.883  80.145 1.00 20.73 ?  358 GLU A CG    1 
ATOM   2847 C CD    . GLU A 1 358 ? -2.800  30.878  81.251 1.00 19.87 ?  358 GLU A CD    1 
ATOM   2848 O OE1   . GLU A 1 358 ? -3.118  32.027  81.051 1.00 27.95 ?  358 GLU A OE1   1 
ATOM   2849 O OE2   . GLU A 1 358 ? -2.272  30.499  82.296 1.00 19.22 -1 358 GLU A OE2   1 
ATOM   2850 N N     . HIS A 1 359 ? -0.065  28.688  76.536 1.00 2.01  ?  359 HIS A N     1 
ATOM   2851 C CA    . HIS A 1 359 ? 0.857   28.958  75.442 1.00 8.05  ?  359 HIS A CA    1 
ATOM   2852 C C     . HIS A 1 359 ? 0.506   28.096  74.232 1.00 19.52 ?  359 HIS A C     1 
ATOM   2853 O O     . HIS A 1 359 ? -0.246  27.124  74.331 1.00 15.71 ?  359 HIS A O     1 
ATOM   2854 C CB    . HIS A 1 359 ? 2.317   28.693  75.834 1.00 2.00  ?  359 HIS A CB    1 
ATOM   2855 C CG    . HIS A 1 359 ? 2.900   29.687  76.791 1.00 1.90  ?  359 HIS A CG    1 
ATOM   2856 N ND1   . HIS A 1 359 ? 2.674   29.639  78.151 1.00 17.93 ?  359 HIS A ND1   1 
ATOM   2857 C CD2   . HIS A 1 359 ? 3.755   30.715  76.592 1.00 1.90  ?  359 HIS A CD2   1 
ATOM   2858 C CE1   . HIS A 1 359 ? 3.336   30.618  78.743 1.00 1.83  ?  359 HIS A CE1   1 
ATOM   2859 N NE2   . HIS A 1 359 ? 4.003   31.282  77.819 1.00 1.85  ?  359 HIS A NE2   1 
ATOM   2860 N N     . ILE A 1 360 ? 1.078   28.456  73.076 1.00 13.86 ?  360 ILE A N     1 
ATOM   2861 C CA    . ILE A 1 360 ? 1.028   27.618  71.886 1.00 14.23 ?  360 ILE A CA    1 
ATOM   2862 C C     . ILE A 1 360 ? 2.408   27.570  71.236 1.00 23.19 ?  360 ILE A C     1 
ATOM   2863 O O     . ILE A 1 360 ? 3.233   28.469  71.419 1.00 25.00 ?  360 ILE A O     1 
ATOM   2864 C CB    . ILE A 1 360 ? -0.040  28.087  70.875 1.00 8.89  ?  360 ILE A CB    1 
ATOM   2865 C CG1   . ILE A 1 360 ? 0.233   29.507  70.398 1.00 14.96 ?  360 ILE A CG1   1 
ATOM   2866 C CG2   . ILE A 1 360 ? -1.425  27.977  71.486 1.00 14.78 ?  360 ILE A CG2   1 
ATOM   2867 C CD1   . ILE A 1 360 ? -0.565  29.909  69.185 1.00 2.95  ?  360 ILE A CD1   1 
ATOM   2868 N N     . ARG A 1 361 ? 2.668   26.488  70.496 1.00 21.71 ?  361 ARG A N     1 
ATOM   2869 C CA    . ARG A 1 361 ? 3.901   26.311  69.738 1.00 14.81 ?  361 ARG A CA    1 
ATOM   2870 C C     . ARG A 1 361 ? 3.545   26.151  68.269 1.00 15.61 ?  361 ARG A C     1 
ATOM   2871 O O     . ARG A 1 361 ? 2.714   25.314  67.916 1.00 38.24 ?  361 ARG A O     1 
ATOM   2872 C CB    . ARG A 1 361 ? 4.700   25.087  70.222 1.00 13.93 ?  361 ARG A CB    1 
ATOM   2873 C CG    . ARG A 1 361 ? 6.169   25.079  69.747 1.00 14.15 ?  361 ARG A CG    1 
ATOM   2874 C CD    . ARG A 1 361 ? 6.752   23.690  69.616 1.00 9.04  ?  361 ARG A CD    1 
ATOM   2875 N NE    . ARG A 1 361 ? 6.116   22.870  68.584 1.00 31.50 ?  361 ARG A NE    1 
ATOM   2876 C CZ    . ARG A 1 361 ? 6.337   21.564  68.431 1.00 19.62 ?  361 ARG A CZ    1 
ATOM   2877 N NH1   . ARG A 1 361 ? 7.168   20.947  69.245 1.00 17.10 1  361 ARG A NH1   1 
ATOM   2878 N NH2   . ARG A 1 361 ? 5.711   20.873  67.487 1.00 13.43 ?  361 ARG A NH2   1 
ATOM   2879 N N     . ILE A 1 362 ? 4.154   26.964  67.421 1.00 13.32 ?  362 ILE A N     1 
ATOM   2880 C CA    . ILE A 1 362 ? 3.893   26.933  65.992 1.00 17.75 ?  362 ILE A CA    1 
ATOM   2881 C C     . ILE A 1 362 ? 5.200   26.656  65.253 1.00 19.93 ?  362 ILE A C     1 
ATOM   2882 O O     . ILE A 1 362 ? 6.293   26.958  65.741 1.00 10.73 ?  362 ILE A O     1 
ATOM   2883 C CB    . ILE A 1 362 ? 3.234   28.251  65.508 1.00 16.46 ?  362 ILE A CB    1 
ATOM   2884 C CG1   . ILE A 1 362 ? 4.262   29.344  65.306 1.00 10.41 ?  362 ILE A CG1   1 
ATOM   2885 C CG2   . ILE A 1 362 ? 2.250   28.767  66.527 1.00 29.12 ?  362 ILE A CG2   1 
ATOM   2886 C CD1   . ILE A 1 362 ? 3.695   30.543  64.599 1.00 23.85 ?  362 ILE A CD1   1 
ATOM   2887 N N     . ASN A 1 363 ? 5.071   26.097  64.053 1.00 30.46 ?  363 ASN A N     1 
ATOM   2888 C CA    . ASN A 1 363 ? 6.199   25.704  63.219 1.00 20.09 ?  363 ASN A CA    1 
ATOM   2889 C C     . ASN A 1 363 ? 6.519   26.799  62.205 1.00 20.83 ?  363 ASN A C     1 
ATOM   2890 O O     . ASN A 1 363 ? 5.703   27.107  61.328 1.00 7.45  ?  363 ASN A O     1 
ATOM   2891 C CB    . ASN A 1 363 ? 5.864   24.393  62.504 1.00 35.44 ?  363 ASN A CB    1 
ATOM   2892 C CG    . ASN A 1 363 ? 7.090   23.645  62.021 1.00 32.29 ?  363 ASN A CG    1 
ATOM   2893 O OD1   . ASN A 1 363 ? 8.032   24.232  61.489 1.00 23.82 ?  363 ASN A OD1   1 
ATOM   2894 N ND2   . ASN A 1 363 ? 7.067   22.328  62.188 1.00 27.24 ?  363 ASN A ND2   1 
ATOM   2895 N N     . ILE A 1 364 ? 7.731   27.333  62.276 1.00 41.20 ?  364 ILE A N     1 
ATOM   2896 C CA    . ILE A 1 364 ? 8.181   28.336  61.319 1.00 35.81 ?  364 ILE A CA    1 
ATOM   2897 C C     . ILE A 1 364 ? 9.179   27.740  60.330 1.00 27.58 ?  364 ILE A C     1 
ATOM   2898 O O     . ILE A 1 364 ? 9.977   28.460  59.727 1.00 17.17 ?  364 ILE A O     1 
ATOM   2899 C CB    . ILE A 1 364 ? 8.745   29.572  62.025 1.00 20.61 ?  364 ILE A CB    1 
ATOM   2900 C CG1   . ILE A 1 364 ? 9.840   29.137  62.996 1.00 35.04 ?  364 ILE A CG1   1 
ATOM   2901 C CG2   . ILE A 1 364 ? 7.614   30.276  62.736 1.00 12.20 ?  364 ILE A CG2   1 
ATOM   2902 C CD1   . ILE A 1 364 ? 10.756  30.204  63.459 1.00 30.51 ?  364 ILE A CD1   1 
ATOM   2903 N N     . GLY A 1 365 ? 9.153   26.420  60.177 1.00 30.21 ?  365 GLY A N     1 
ATOM   2904 C CA    . GLY A 1 365 ? 9.897   25.792  59.111 1.00 31.36 ?  365 GLY A CA    1 
ATOM   2905 C C     . GLY A 1 365 ? 9.100   25.699  57.825 1.00 30.13 ?  365 GLY A C     1 
ATOM   2906 O O     . GLY A 1 365 ? 8.938   24.610  57.272 1.00 36.73 ?  365 GLY A O     1 
ATOM   2907 N N     . CYS A 1 366 ? 8.599   26.821  57.332 1.00 22.39 ?  366 CYS A N     1 
ATOM   2908 C CA    . CYS A 1 366 ? 7.737   26.829  56.163 1.00 29.14 ?  366 CYS A CA    1 
ATOM   2909 C C     . CYS A 1 366 ? 8.123   28.002  55.283 1.00 31.31 ?  366 CYS A C     1 
ATOM   2910 O O     . CYS A 1 366 ? 8.815   28.924  55.730 1.00 43.63 ?  366 CYS A O     1 
ATOM   2911 C CB    . CYS A 1 366 ? 6.242   26.889  56.523 1.00 17.51 ?  366 CYS A CB    1 
ATOM   2912 S SG    . CYS A 1 366 ? 5.848   27.890  57.975 1.00 19.05 ?  366 CYS A SG    1 
ATOM   2913 N N     . PRO A 1 367 ? 7.755   27.959  54.008 1.00 24.55 ?  367 PRO A N     1 
ATOM   2914 C CA    . PRO A 1 367 ? 7.914   29.135  53.158 1.00 25.80 ?  367 PRO A CA    1 
ATOM   2915 C C     . PRO A 1 367 ? 7.185   30.337  53.741 1.00 25.89 ?  367 PRO A C     1 
ATOM   2916 O O     . PRO A 1 367 ? 6.117   30.216  54.343 1.00 18.77 ?  367 PRO A O     1 
ATOM   2917 C CB    . PRO A 1 367 ? 7.286   28.695  51.833 1.00 29.56 ?  367 PRO A CB    1 
ATOM   2918 C CG    . PRO A 1 367 ? 7.329   27.238  51.858 1.00 14.52 ?  367 PRO A CG    1 
ATOM   2919 C CD    . PRO A 1 367 ? 7.162   26.834  53.273 1.00 15.70 ?  367 PRO A CD    1 
ATOM   2920 N N     . ARG A 1 368 ? 7.783   31.515  53.543 1.00 31.99 ?  368 ARG A N     1 
ATOM   2921 C CA    . ARG A 1 368 ? 7.181   32.750  54.035 1.00 33.10 ?  368 ARG A CA    1 
ATOM   2922 C C     . ARG A 1 368 ? 5.741   32.906  53.573 1.00 40.50 ?  368 ARG A C     1 
ATOM   2923 O O     . ARG A 1 368 ? 4.913   33.455  54.307 1.00 29.44 ?  368 ARG A O     1 
ATOM   2924 C CB    . ARG A 1 368 ? 7.995   33.953  53.571 1.00 22.96 ?  368 ARG A CB    1 
ATOM   2925 C CG    . ARG A 1 368 ? 7.386   35.308  53.943 1.00 13.70 ?  368 ARG A CG    1 
ATOM   2926 C CD    . ARG A 1 368 ? 7.708   35.707  55.380 1.00 16.67 ?  368 ARG A CD    1 
ATOM   2927 N NE    . ARG A 1 368 ? 9.122   35.524  55.698 1.00 29.24 ?  368 ARG A NE    1 
ATOM   2928 C CZ    . ARG A 1 368 ? 10.033  36.492  55.708 1.00 38.64 ?  368 ARG A CZ    1 
ATOM   2929 N NH1   . ARG A 1 368 ? 9.695   37.746  55.427 1.00 41.17 1  368 ARG A NH1   1 
ATOM   2930 N NH2   . ARG A 1 368 ? 11.293  36.204  56.004 1.00 36.38 ?  368 ARG A NH2   1 
ATOM   2931 N N     . SER A 1 369 ? 5.422   32.427  52.369 1.00 45.10 ?  369 SER A N     1 
ATOM   2932 C CA    . SER A 1 369 ? 4.037   32.424  51.915 1.00 35.75 ?  369 SER A CA    1 
ATOM   2933 C C     . SER A 1 369 ? 3.129   31.783  52.955 1.00 42.11 ?  369 SER A C     1 
ATOM   2934 O O     . SER A 1 369 ? 2.181   32.414  53.441 1.00 47.96 ?  369 SER A O     1 
ATOM   2935 C CB    . SER A 1 369 ? 3.938   31.680  50.584 1.00 27.35 ?  369 SER A CB    1 
ATOM   2936 O OG    . SER A 1 369 ? 4.277   30.314  50.750 1.00 23.51 ?  369 SER A OG    1 
ATOM   2937 N N     . VAL A 1 370 ? 3.457   30.555  53.368 1.00 25.92 ?  370 VAL A N     1 
ATOM   2938 C CA    . VAL A 1 370 ? 2.676   29.907  54.417 1.00 16.64 ?  370 VAL A CA    1 
ATOM   2939 C C     . VAL A 1 370 ? 2.806   30.684  55.718 1.00 13.43 ?  370 VAL A C     1 
ATOM   2940 O O     . VAL A 1 370 ? 1.832   30.874  56.451 1.00 18.20 ?  370 VAL A O     1 
ATOM   2941 C CB    . VAL A 1 370 ? 3.106   28.438  54.606 1.00 28.32 ?  370 VAL A CB    1 
ATOM   2942 C CG1   . VAL A 1 370 ? 2.240   27.762  55.680 1.00 29.70 ?  370 VAL A CG1   1 
ATOM   2943 C CG2   . VAL A 1 370 ? 3.064   27.659  53.289 1.00 30.07 ?  370 VAL A CG2   1 
ATOM   2944 N N     . LEU A 1 371 ? 4.010   31.154  56.021 1.00 29.23 ?  371 LEU A N     1 
ATOM   2945 C CA    . LEU A 1 371 ? 4.227   31.821  57.298 1.00 29.02 ?  371 LEU A CA    1 
ATOM   2946 C C     . LEU A 1 371 ? 3.404   33.106  57.430 1.00 20.62 ?  371 LEU A C     1 
ATOM   2947 O O     . LEU A 1 371 ? 2.935   33.430  58.527 1.00 17.27 ?  371 LEU A O     1 
ATOM   2948 C CB    . LEU A 1 371 ? 5.719   32.091  57.473 1.00 25.07 ?  371 LEU A CB    1 
ATOM   2949 C CG    . LEU A 1 371 ? 6.113   32.714  58.806 1.00 29.86 ?  371 LEU A CG    1 
ATOM   2950 C CD1   . LEU A 1 371 ? 5.588   31.876  59.971 1.00 7.32  ?  371 LEU A CD1   1 
ATOM   2951 C CD2   . LEU A 1 371 ? 7.631   32.914  58.856 1.00 13.57 ?  371 LEU A CD2   1 
ATOM   2952 N N     . GLU A 1 372 ? 3.220   33.860  56.335 1.00 13.28 ?  372 GLU A N     1 
ATOM   2953 C CA    . GLU A 1 372 ? 2.418   35.079  56.445 1.00 15.86 ?  372 GLU A CA    1 
ATOM   2954 C C     . GLU A 1 372 ? 0.942   34.751  56.585 1.00 28.40 ?  372 GLU A C     1 
ATOM   2955 O O     . GLU A 1 372 ? 0.218   35.428  57.323 1.00 34.73 ?  372 GLU A O     1 
ATOM   2956 C CB    . GLU A 1 372 ? 2.663   36.045  55.278 1.00 30.58 ?  372 GLU A CB    1 
ATOM   2957 C CG    . GLU A 1 372 ? 2.702   35.498  53.847 1.00 40.97 ?  372 GLU A CG    1 
ATOM   2958 C CD    . GLU A 1 372 ? 3.231   36.546  52.859 1.00 35.36 ?  372 GLU A CD    1 
ATOM   2959 O OE1   . GLU A 1 372 ? 4.156   37.289  53.234 1.00 38.66 ?  372 GLU A OE1   1 
ATOM   2960 O OE2   . GLU A 1 372 ? 2.732   36.638  51.721 1.00 32.29 -1 372 GLU A OE2   1 
ATOM   2961 N N     . GLU A 1 373 ? 0.469   33.718  55.884 1.00 26.86 ?  373 GLU A N     1 
ATOM   2962 C CA    . GLU A 1 373 ? -0.914  33.312  56.088 1.00 13.39 ?  373 GLU A CA    1 
ATOM   2963 C C     . GLU A 1 373 ? -1.103  32.694  57.463 1.00 26.89 ?  373 GLU A C     1 
ATOM   2964 O O     . GLU A 1 373 ? -2.174  32.846  58.054 1.00 50.67 ?  373 GLU A O     1 
ATOM   2965 C CB    . GLU A 1 373 ? -1.371  32.338  55.006 1.00 14.89 ?  373 GLU A CB    1 
ATOM   2966 C CG    . GLU A 1 373 ? -1.711  32.991  53.672 1.00 29.44 ?  373 GLU A CG    1 
ATOM   2967 C CD    . GLU A 1 373 ? -0.698  32.696  52.599 1.00 46.93 ?  373 GLU A CD    1 
ATOM   2968 O OE1   . GLU A 1 373 ? -0.288  33.629  51.883 1.00 52.40 ?  373 GLU A OE1   1 
ATOM   2969 O OE2   . GLU A 1 373 ? -0.336  31.514  52.456 1.00 50.73 -1 373 GLU A OE2   1 
ATOM   2970 N N     . ILE A 1 374 ? -0.082  32.017  58.001 1.00 23.17 ?  374 ILE A N     1 
ATOM   2971 C CA    . ILE A 1 374 ? -0.177  31.481  59.362 1.00 18.62 ?  374 ILE A CA    1 
ATOM   2972 C C     . ILE A 1 374 ? -0.406  32.605  60.368 1.00 17.75 ?  374 ILE A C     1 
ATOM   2973 O O     . ILE A 1 374 ? -1.166  32.448  61.331 1.00 13.85 ?  374 ILE A O     1 
ATOM   2974 C CB    . ILE A 1 374 ? 1.075   30.647  59.718 1.00 21.32 ?  374 ILE A CB    1 
ATOM   2975 C CG1   . ILE A 1 374 ? 1.060   29.279  59.015 1.00 20.05 ?  374 ILE A CG1   1 
ATOM   2976 C CG2   . ILE A 1 374 ? 1.182   30.433  61.235 1.00 6.95  ?  374 ILE A CG2   1 
ATOM   2977 C CD1   . ILE A 1 374 ? 2.365   28.459  59.190 1.00 10.58 ?  374 ILE A CD1   1 
ATOM   2978 N N     . LEU A 1 375 ? 0.242   33.759  60.159 1.00 20.81 ?  375 LEU A N     1 
ATOM   2979 C CA    . LEU A 1 375 ? 0.121   34.868  61.103 1.00 22.44 ?  375 LEU A CA    1 
ATOM   2980 C C     . LEU A 1 375 ? -1.137  35.696  60.865 1.00 34.17 ?  375 LEU A C     1 
ATOM   2981 O O     . LEU A 1 375 ? -1.730  36.205  61.822 1.00 54.79 ?  375 LEU A O     1 
ATOM   2982 C CB    . LEU A 1 375 ? 1.353   35.765  61.016 1.00 28.32 ?  375 LEU A CB    1 
ATOM   2983 C CG    . LEU A 1 375 ? 2.699   35.102  61.296 1.00 30.59 ?  375 LEU A CG    1 
ATOM   2984 C CD1   . LEU A 1 375 ? 3.810   36.068  60.942 1.00 30.72 ?  375 LEU A CD1   1 
ATOM   2985 C CD2   . LEU A 1 375 ? 2.792   34.670  62.743 1.00 26.26 ?  375 LEU A CD2   1 
ATOM   2986 N N     . ASN A 1 376 ? -1.550  35.856  59.610 1.00 28.38 ?  376 ASN A N     1 
ATOM   2987 C CA    . ASN A 1 376 ? -2.797  36.559  59.327 1.00 26.30 ?  376 ASN A CA    1 
ATOM   2988 C C     . ASN A 1 376 ? -3.974  35.893  60.035 1.00 32.95 ?  376 ASN A C     1 
ATOM   2989 O O     . ASN A 1 376 ? -4.860  36.576  60.565 1.00 24.71 ?  376 ASN A O     1 
ATOM   2990 C CB    . ASN A 1 376 ? -3.023  36.610  57.817 1.00 40.70 ?  376 ASN A CB    1 
ATOM   2991 C CG    . ASN A 1 376 ? -3.917  37.765  57.386 1.00 52.62 ?  376 ASN A CG    1 
ATOM   2992 O OD1   . ASN A 1 376 ? -5.135  37.602  57.225 1.00 52.82 ?  376 ASN A OD1   1 
ATOM   2993 N ND2   . ASN A 1 376 ? -3.311  38.931  57.155 1.00 42.43 ?  376 ASN A ND2   1 
ATOM   2994 N N     . ARG A 1 377 ? -3.947  34.570  60.076 1.00 27.82 ?  377 ARG A N     1 
ATOM   2995 C CA    . ARG A 1 377 ? -5.037  33.807  60.711 1.00 10.25 ?  377 ARG A CA    1 
ATOM   2996 C C     . ARG A 1 377 ? -4.886  33.837  62.220 1.00 8.49  ?  377 ARG A C     1 
ATOM   2997 O O     . ARG A 1 377 ? -5.870  33.830  62.828 1.00 18.97 ?  377 ARG A O     1 
ATOM   2998 C CB    . ARG A 1 377 ? -5.104  32.403  60.128 1.00 8.89  ?  377 ARG A CB    1 
ATOM   2999 C CG    . ARG A 1 377 ? -5.550  32.336  58.681 1.00 11.32 ?  377 ARG A CG    1 
ATOM   3000 C CD    . ARG A 1 377 ? -5.150  30.973  58.176 1.00 14.70 ?  377 ARG A CD    1 
ATOM   3001 N NE    . ARG A 1 377 ? -5.478  30.811  56.776 1.00 24.30 ?  377 ARG A NE    1 
ATOM   3002 C CZ    . ARG A 1 377 ? -6.145  29.781  56.285 1.00 31.56 ?  377 ARG A CZ    1 
ATOM   3003 N NH1   . ARG A 1 377 ? -6.547  28.812  57.083 1.00 23.99 1  377 ARG A NH1   1 
ATOM   3004 N NH2   . ARG A 1 377 ? -6.388  29.706  54.991 1.00 43.81 ?  377 ARG A NH2   1 
ATOM   3005 N N     . LEU A 1 378 ? -3.683  33.865  62.752 1.00 6.74  ?  378 LEU A N     1 
ATOM   3006 C CA    . LEU A 1 378 ? -3.497  33.901  64.196 1.00 17.36 ?  378 LEU A CA    1 
ATOM   3007 C C     . LEU A 1 378 ? -3.960  35.226  64.763 1.00 23.98 ?  378 LEU A C     1 
ATOM   3008 O O     . LEU A 1 378 ? -4.515  35.286  65.862 1.00 28.07 ?  378 LEU A O     1 
ATOM   3009 C CB    . LEU A 1 378 ? -2.036  33.648  64.544 1.00 23.84 ?  378 LEU A CB    1 
ATOM   3010 C CG    . LEU A 1 378 ? -1.730  32.169  64.782 1.00 30.60 ?  378 LEU A CG    1 
ATOM   3011 C CD1   . LEU A 1 378 ? -1.382  31.449  63.492 1.00 39.17 ?  378 LEU A CD1   1 
ATOM   3012 C CD2   . LEU A 1 378 ? -0.641  31.997  65.810 1.00 42.81 ?  378 LEU A CD2   1 
ATOM   3013 N N     . ARG A 1 379 ? -3.686  36.306  64.044 1.00 34.75 ?  379 ARG A N     1 
ATOM   3014 C CA    . ARG A 1 379 ? -4.274  37.590  64.383 1.00 34.97 ?  379 ARG A CA    1 
ATOM   3015 C C     . ARG A 1 379 ? -5.785  37.515  64.227 1.00 19.66 ?  379 ARG A C     1 
ATOM   3016 O O     . ARG A 1 379 ? -6.535  37.707  65.188 1.00 22.72 ?  379 ARG A O     1 
ATOM   3017 C CB    . ARG A 1 379 ? -3.678  38.670  63.471 1.00 36.51 ?  379 ARG A CB    1 
ATOM   3018 C CG    . ARG A 1 379 ? -4.104  40.079  63.787 1.00 19.52 ?  379 ARG A CG    1 
ATOM   3019 C CD    . ARG A 1 379 ? -3.764  40.998  62.633 1.00 23.85 ?  379 ARG A CD    1 
ATOM   3020 N NE    . ARG A 1 379 ? -4.250  40.498  61.345 1.00 24.72 ?  379 ARG A NE    1 
ATOM   3021 C CZ    . ARG A 1 379 ? -5.534  40.308  61.041 1.00 23.55 ?  379 ARG A CZ    1 
ATOM   3022 N NH1   . ARG A 1 379 ? -6.486  40.566  61.927 1.00 25.26 1  379 ARG A NH1   1 
ATOM   3023 N NH2   . ARG A 1 379 ? -5.874  39.858  59.838 1.00 25.96 ?  379 ARG A NH2   1 
ATOM   3024 N N     . HIS A 1 380 ? -6.236  37.132  63.028 1.00 11.30 ?  380 HIS A N     1 
ATOM   3025 C CA    . HIS A 1 380 ? -7.658  36.944  62.766 1.00 10.55 ?  380 HIS A CA    1 
ATOM   3026 C C     . HIS A 1 380 ? -8.326  36.149  63.877 1.00 11.64 ?  380 HIS A C     1 
ATOM   3027 O O     . HIS A 1 380 ? -9.407  36.519  64.345 1.00 33.80 ?  380 HIS A O     1 
ATOM   3028 C CB    . HIS A 1 380 ? -7.827  36.243  61.417 1.00 11.59 ?  380 HIS A CB    1 
ATOM   3029 C CG    . HIS A 1 380 ? -9.240  35.881  61.078 1.00 30.93 ?  380 HIS A CG    1 
ATOM   3030 N ND1   . HIS A 1 380 ? -10.254 36.815  61.003 1.00 39.08 ?  380 HIS A ND1   1 
ATOM   3031 C CD2   . HIS A 1 380 ? -9.802  34.689  60.760 1.00 34.09 ?  380 HIS A CD2   1 
ATOM   3032 C CE1   . HIS A 1 380 ? -11.380 36.213  60.666 1.00 34.14 ?  380 HIS A CE1   1 
ATOM   3033 N NE2   . HIS A 1 380 ? -11.136 34.921  60.528 1.00 30.12 ?  380 HIS A NE2   1 
ATOM   3034 N N     . THR A 1 381 ? -7.684  35.101  64.359 1.00 16.68 ?  381 THR A N     1 
ATOM   3035 C CA    . THR A 1 381 ? -8.284  34.213  65.388 1.00 20.47 ?  381 THR A CA    1 
ATOM   3036 C C     . THR A 1 381 ? -8.612  34.972  66.670 1.00 24.63 ?  381 THR A C     1 
ATOM   3037 O O     . THR A 1 381 ? -9.709  34.764  67.207 1.00 30.46 ?  381 THR A O     1 
ATOM   3038 C CB    . THR A 1 381 ? -7.367  33.035  65.739 1.00 18.95 ?  381 THR A CB    1 
ATOM   3039 O OG1   . THR A 1 381 ? -6.850  32.343  64.610 1.00 18.22 ?  381 THR A OG1   1 
ATOM   3040 C CG2   . THR A 1 381 ? -8.043  32.044  66.653 1.00 18.95 ?  381 THR A CG2   1 
ATOM   3041 N N     . PHE A 1 382 ? -7.751  35.873  67.102 1.00 11.06 ?  382 PHE A N     1 
ATOM   3042 C CA    . PHE A 1 382 ? -7.892  36.500  68.411 1.00 22.98 ?  382 PHE A CA    1 
ATOM   3043 C C     . PHE A 1 382 ? -8.273  37.975  68.331 1.00 37.00 ?  382 PHE A C     1 
ATOM   3044 O O     . PHE A 1 382 ? -8.244  38.671  69.357 1.00 34.05 ?  382 PHE A O     1 
ATOM   3045 C CB    . PHE A 1 382 ? -6.595  36.336  69.206 1.00 36.37 ?  382 PHE A CB    1 
ATOM   3046 C CG    . PHE A 1 382 ? -6.103  34.913  69.306 1.00 27.03 ?  382 PHE A CG    1 
ATOM   3047 C CD1   . PHE A 1 382 ? -6.896  33.917  69.841 1.00 37.29 ?  382 PHE A CD1   1 
ATOM   3048 C CD2   . PHE A 1 382 ? -4.846  34.579  68.865 1.00 27.77 ?  382 PHE A CD2   1 
ATOM   3049 C CE1   . PHE A 1 382 ? -6.437  32.624  69.936 1.00 27.07 ?  382 PHE A CE1   1 
ATOM   3050 C CE2   . PHE A 1 382 ? -4.389  33.275  68.952 1.00 27.18 ?  382 PHE A CE2   1 
ATOM   3051 C CZ    . PHE A 1 382 ? -5.180  32.305  69.488 1.00 15.66 ?  382 PHE A CZ    1 
ATOM   3052 N N     . SER A 1 383 ? -8.591  38.477  67.141 1.00 41.77 ?  383 SER A N     1 
ATOM   3053 C CA    . SER A 1 383 ? -9.011  39.865  66.991 1.00 47.89 ?  383 SER A CA    1 
ATOM   3054 C C     . SER A 1 383 ? -10.498 40.016  67.284 1.00 33.16 ?  383 SER A C     1 
ATOM   3055 O O     . SER A 1 383 ? -11.320 39.152  67.004 1.00 38.82 ?  383 SER A O     1 
ATOM   3056 C CB    . SER A 1 383 ? -8.696  40.377  65.582 1.00 61.64 ?  383 SER A CB    1 
ATOM   3057 O OG    . SER A 1 383 ? -7.310  40.661  65.430 1.00 68.99 ?  383 SER A OG    1 
ATOM   3058 O OXT   . SER A 1 383 ? -10.920 41.036  67.802 1.00 29.00 -1 383 SER A OXT   1 
ATOM   3059 N N     . LYS B 1 6   ? 19.597  -14.960 36.574 1.00 61.14 ?  6   LYS B N     1 
ATOM   3060 C CA    . LYS B 1 6   ? 20.719  -14.034 36.554 1.00 59.81 ?  6   LYS B CA    1 
ATOM   3061 C C     . LYS B 1 6   ? 21.293  -13.879 37.953 1.00 63.65 ?  6   LYS B C     1 
ATOM   3062 O O     . LYS B 1 6   ? 20.602  -13.418 38.868 1.00 66.05 ?  6   LYS B O     1 
ATOM   3063 C CB    . LYS B 1 6   ? 20.275  -12.675 36.019 1.00 62.97 ?  6   LYS B CB    1 
ATOM   3064 C CG    . LYS B 1 6   ? 21.199  -11.526 36.419 1.00 60.31 ?  6   LYS B CG    1 
ATOM   3065 C CD    . LYS B 1 6   ? 20.566  -10.162 36.172 1.00 51.65 ?  6   LYS B CD    1 
ATOM   3066 C CE    . LYS B 1 6   ? 21.489  -9.035  36.628 1.00 42.55 ?  6   LYS B CE    1 
ATOM   3067 N NZ    . LYS B 1 6   ? 20.836  -7.710  36.485 1.00 32.66 1  6   LYS B NZ    1 
ATOM   3068 N N     . ALA B 1 7   ? 22.547  -14.284 38.123 1.00 65.52 ?  7   ALA B N     1 
ATOM   3069 C CA    . ALA B 1 7   ? 23.274  -13.933 39.332 1.00 55.27 ?  7   ALA B CA    1 
ATOM   3070 C C     . ALA B 1 7   ? 23.506  -12.434 39.318 1.00 47.47 ?  7   ALA B C     1 
ATOM   3071 O O     . ALA B 1 7   ? 23.935  -11.877 38.303 1.00 48.02 ?  7   ALA B O     1 
ATOM   3072 C CB    . ALA B 1 7   ? 24.604  -14.682 39.404 1.00 57.64 ?  7   ALA B CB    1 
ATOM   3073 N N     . ILE B 1 8   ? 23.204  -11.773 40.428 1.00 42.01 ?  8   ILE B N     1 
ATOM   3074 C CA    . ILE B 1 8   ? 23.327  -10.325 40.532 1.00 51.83 ?  8   ILE B CA    1 
ATOM   3075 C C     . ILE B 1 8   ? 24.485  -10.015 41.469 1.00 46.25 ?  8   ILE B C     1 
ATOM   3076 O O     . ILE B 1 8   ? 24.593  -10.611 42.548 1.00 45.22 ?  8   ILE B O     1 
ATOM   3077 C CB    . ILE B 1 8   ? 22.023  -9.675  41.028 1.00 57.13 ?  8   ILE B CB    1 
ATOM   3078 C CG1   . ILE B 1 8   ? 20.802  -10.442 40.507 1.00 58.01 ?  8   ILE B CG1   1 
ATOM   3079 C CG2   . ILE B 1 8   ? 21.971  -8.203  40.608 1.00 45.48 ?  8   ILE B CG2   1 
ATOM   3080 C CD1   . ILE B 1 8   ? 19.454  -9.965  41.081 1.00 47.82 ?  8   ILE B CD1   1 
ATOM   3081 N N     . ASN B 1 9   ? 25.370  -9.119  41.045 1.00 40.93 ?  9   ASN B N     1 
ATOM   3082 C CA    . ASN B 1 9   ? 26.502  -8.755  41.886 1.00 36.02 ?  9   ASN B CA    1 
ATOM   3083 C C     . ASN B 1 9   ? 25.978  -8.085  43.141 1.00 35.71 ?  9   ASN B C     1 
ATOM   3084 O O     . ASN B 1 9   ? 25.254  -7.089  43.066 1.00 48.17 ?  9   ASN B O     1 
ATOM   3085 C CB    . ASN B 1 9   ? 27.476  -7.842  41.144 1.00 25.43 ?  9   ASN B CB    1 
ATOM   3086 C CG    . ASN B 1 9   ? 28.610  -7.341  42.037 1.00 27.93 ?  9   ASN B CG    1 
ATOM   3087 O OD1   . ASN B 1 9   ? 28.798  -7.807  43.162 1.00 27.60 ?  9   ASN B OD1   1 
ATOM   3088 N ND2   . ASN B 1 9   ? 29.387  -6.398  41.519 1.00 31.24 ?  9   ASN B ND2   1 
ATOM   3089 N N     . ARG B 1 10  ? 26.325  -8.641  44.294 1.00 42.76 ?  10  ARG B N     1 
ATOM   3090 C CA    . ARG B 1 10  ? 25.942  -8.051  45.562 1.00 49.41 ?  10  ARG B CA    1 
ATOM   3091 C C     . ARG B 1 10  ? 27.140  -7.594  46.380 1.00 55.34 ?  10  ARG B C     1 
ATOM   3092 O O     . ARG B 1 10  ? 26.953  -7.035  47.468 1.00 59.15 ?  10  ARG B O     1 
ATOM   3093 C CB    . ARG B 1 10  ? 25.095  -9.046  46.363 1.00 40.92 ?  10  ARG B CB    1 
ATOM   3094 C CG    . ARG B 1 10  ? 23.731  -9.308  45.742 1.00 32.60 ?  10  ARG B CG    1 
ATOM   3095 C CD    . ARG B 1 10  ? 22.807  -9.976  46.731 1.00 34.54 ?  10  ARG B CD    1 
ATOM   3096 N NE    . ARG B 1 10  ? 22.780  -9.264  48.005 1.00 31.62 ?  10  ARG B NE    1 
ATOM   3097 C CZ    . ARG B 1 10  ? 21.991  -9.597  49.019 1.00 37.62 ?  10  ARG B CZ    1 
ATOM   3098 N NH1   . ARG B 1 10  ? 21.153  -10.616 48.892 1.00 41.96 1  10  ARG B NH1   1 
ATOM   3099 N NH2   . ARG B 1 10  ? 22.033  -8.915  50.154 1.00 34.61 ?  10  ARG B NH2   1 
ATOM   3100 N N     . ARG B 1 11  ? 28.356  -7.787  45.878 1.00 50.99 ?  11  ARG B N     1 
ATOM   3101 C CA    . ARG B 1 11  ? 29.528  -7.215  46.523 1.00 48.51 ?  11  ARG B CA    1 
ATOM   3102 C C     . ARG B 1 11  ? 29.530  -5.708  46.306 1.00 46.71 ?  11  ARG B C     1 
ATOM   3103 O O     . ARG B 1 11  ? 29.122  -5.221  45.249 1.00 38.46 ?  11  ARG B O     1 
ATOM   3104 C CB    . ARG B 1 11  ? 30.813  -7.838  45.975 1.00 41.96 ?  11  ARG B CB    1 
ATOM   3105 C CG    . ARG B 1 11  ? 30.972  -9.310  46.304 1.00 38.65 ?  11  ARG B CG    1 
ATOM   3106 C CD    . ARG B 1 11  ? 32.430  -9.690  46.508 1.00 41.92 ?  11  ARG B CD    1 
ATOM   3107 N NE    . ARG B 1 11  ? 32.596  -11.131 46.669 1.00 44.10 ?  11  ARG B NE    1 
ATOM   3108 C CZ    . ARG B 1 11  ? 32.616  -11.746 47.846 1.00 53.29 ?  11  ARG B CZ    1 
ATOM   3109 N NH1   . ARG B 1 11  ? 32.474  -11.046 48.966 1.00 52.82 1  11  ARG B NH1   1 
ATOM   3110 N NH2   . ARG B 1 11  ? 32.777  -13.060 47.908 1.00 54.34 ?  11  ARG B NH2   1 
ATOM   3111 N N     . GLY B 1 12  ? 29.945  -4.968  47.334 1.00 55.38 ?  12  GLY B N     1 
ATOM   3112 C CA    . GLY B 1 12  ? 29.954  -3.520  47.266 1.00 48.21 ?  12  GLY B CA    1 
ATOM   3113 C C     . GLY B 1 12  ? 28.598  -2.884  47.448 1.00 48.68 ?  12  GLY B C     1 
ATOM   3114 O O     . GLY B 1 12  ? 28.388  -1.753  46.997 1.00 54.97 ?  12  GLY B O     1 
ATOM   3115 N N     . THR B 1 13  ? 27.659  -3.585  48.088 1.00 42.61 ?  13  THR B N     1 
ATOM   3116 C CA    . THR B 1 13  ? 26.309  -3.086  48.319 1.00 35.98 ?  13  THR B CA    1 
ATOM   3117 C C     . THR B 1 13  ? 26.001  -2.934  49.804 1.00 35.37 ?  13  THR B C     1 
ATOM   3118 O O     . THR B 1 13  ? 24.843  -2.679  50.165 1.00 30.44 ?  13  THR B O     1 
ATOM   3119 C CB    . THR B 1 13  ? 25.269  -4.010  47.666 1.00 40.78 ?  13  THR B CB    1 
ATOM   3120 O OG1   . THR B 1 13  ? 25.200  -5.253  48.377 1.00 45.22 ?  13  THR B OG1   1 
ATOM   3121 C CG2   . THR B 1 13  ? 25.630  -4.300  46.213 1.00 45.41 ?  13  THR B CG2   1 
ATOM   3122 N N     . HIS B 1 14  ? 27.015  -3.090  50.663 1.00 22.94 ?  14  HIS B N     1 
ATOM   3123 C CA    . HIS B 1 14  ? 26.908  -3.121  52.120 1.00 16.11 ?  14  HIS B CA    1 
ATOM   3124 C C     . HIS B 1 14  ? 25.958  -4.221  52.601 1.00 16.61 ?  14  HIS B C     1 
ATOM   3125 O O     . HIS B 1 14  ? 25.618  -4.289  53.791 1.00 18.37 ?  14  HIS B O     1 
ATOM   3126 C CB    . HIS B 1 14  ? 26.519  -1.740  52.669 1.00 15.07 ?  14  HIS B CB    1 
ATOM   3127 C CG    . HIS B 1 14  ? 27.456  -0.649  52.234 1.00 23.91 ?  14  HIS B CG    1 
ATOM   3128 N ND1   . HIS B 1 14  ? 28.810  -0.685  52.489 1.00 26.80 ?  14  HIS B ND1   1 
ATOM   3129 C CD2   . HIS B 1 14  ? 27.240  0.481   51.520 1.00 24.79 ?  14  HIS B CD2   1 
ATOM   3130 C CE1   . HIS B 1 14  ? 29.384  0.383   51.968 1.00 19.11 ?  14  HIS B CE1   1 
ATOM   3131 N NE2   . HIS B 1 14  ? 28.454  1.105   51.374 1.00 22.79 ?  14  HIS B NE2   1 
ATOM   3132 N N     . SER B 1 15  ? 25.643  -5.172  51.725 1.00 15.32 ?  15  SER B N     1 
ATOM   3133 C CA    . SER B 1 15  ? 24.931  -6.370  52.140 1.00 24.56 ?  15  SER B CA    1 
ATOM   3134 C C     . SER B 1 15  ? 25.792  -7.166  53.110 1.00 27.65 ?  15  SER B C     1 
ATOM   3135 O O     . SER B 1 15  ? 26.978  -7.407  52.851 1.00 35.26 ?  15  SER B O     1 
ATOM   3136 C CB    . SER B 1 15  ? 24.592  -7.228  50.923 1.00 35.44 ?  15  SER B CB    1 
ATOM   3137 O OG    . SER B 1 15  ? 24.559  -8.605  51.269 1.00 42.99 ?  15  SER B OG    1 
ATOM   3138 N N     . ILE B 1 16  ? 25.193  -7.577  54.235 1.00 13.21 ?  16  ILE B N     1 
ATOM   3139 C CA    . ILE B 1 16  ? 25.918  -8.403  55.199 1.00 17.63 ?  16  ILE B CA    1 
ATOM   3140 C C     . ILE B 1 16  ? 26.392  -9.707  54.556 1.00 22.63 ?  16  ILE B C     1 
ATOM   3141 O O     . ILE B 1 16  ? 27.465  -10.218 54.885 1.00 38.25 ?  16  ILE B O     1 
ATOM   3142 C CB    . ILE B 1 16  ? 25.059  -8.657  56.455 1.00 26.31 ?  16  ILE B CB    1 
ATOM   3143 C CG1   . ILE B 1 16  ? 24.756  -7.335  57.181 1.00 23.32 ?  16  ILE B CG1   1 
ATOM   3144 C CG2   . ILE B 1 16  ? 25.741  -9.663  57.389 1.00 30.21 ?  16  ILE B CG2   1 
ATOM   3145 C CD1   . ILE B 1 16  ? 24.516  -7.453  58.688 1.00 17.67 ?  16  ILE B CD1   1 
ATOM   3146 N N     . LYS B 1 17  ? 25.606  -10.267 53.635 1.00 16.69 ?  17  LYS B N     1 
ATOM   3147 C CA    . LYS B 1 17  ? 25.960  -11.557 53.046 1.00 23.10 ?  17  LYS B CA    1 
ATOM   3148 C C     . LYS B 1 17  ? 27.200  -11.459 52.179 1.00 25.24 ?  17  LYS B C     1 
ATOM   3149 O O     . LYS B 1 17  ? 28.098  -12.305 52.261 1.00 36.50 ?  17  LYS B O     1 
ATOM   3150 C CB    . LYS B 1 17  ? 24.799  -12.115 52.224 1.00 33.60 ?  17  LYS B CB    1 
ATOM   3151 C CG    . LYS B 1 17  ? 24.838  -13.627 52.134 1.00 35.79 ?  17  LYS B CG    1 
ATOM   3152 C CD    . LYS B 1 17  ? 24.097  -14.170 50.926 1.00 45.45 ?  17  LYS B CD    1 
ATOM   3153 C CE    . LYS B 1 17  ? 23.945  -15.682 51.035 1.00 45.20 ?  17  LYS B CE    1 
ATOM   3154 N NZ    . LYS B 1 17  ? 22.613  -16.192 50.601 1.00 47.76 1  17  LYS B NZ    1 
ATOM   3155 N N     . TRP B 1 18  ? 27.257  -10.443 51.328 1.00 28.63 ?  18  TRP B N     1 
ATOM   3156 C CA    . TRP B 1 18  ? 28.255  -10.358 50.267 1.00 19.55 ?  18  TRP B CA    1 
ATOM   3157 C C     . TRP B 1 18  ? 29.379  -9.382  50.564 1.00 24.94 ?  18  TRP B C     1 
ATOM   3158 O O     . TRP B 1 18  ? 30.390  -9.391  49.854 1.00 41.18 ?  18  TRP B O     1 
ATOM   3159 C CB    . TRP B 1 18  ? 27.575  -9.995  48.939 1.00 20.54 ?  18  TRP B CB    1 
ATOM   3160 C CG    . TRP B 1 18  ? 26.874  -11.188 48.419 1.00 41.56 ?  18  TRP B CG    1 
ATOM   3161 C CD1   . TRP B 1 18  ? 25.538  -11.462 48.510 1.00 39.53 ?  18  TRP B CD1   1 
ATOM   3162 C CD2   . TRP B 1 18  ? 27.479  -12.331 47.797 1.00 36.34 ?  18  TRP B CD2   1 
ATOM   3163 N NE1   . TRP B 1 18  ? 25.272  -12.690 47.952 1.00 37.12 ?  18  TRP B NE1   1 
ATOM   3164 C CE2   . TRP B 1 18  ? 26.447  -13.245 47.512 1.00 36.95 ?  18  TRP B CE2   1 
ATOM   3165 C CE3   . TRP B 1 18  ? 28.790  -12.660 47.441 1.00 36.56 ?  18  TRP B CE3   1 
ATOM   3166 C CZ2   . TRP B 1 18  ? 26.684  -14.464 46.883 1.00 30.43 ?  18  TRP B CZ2   1 
ATOM   3167 C CZ3   . TRP B 1 18  ? 29.020  -13.881 46.817 1.00 34.42 ?  18  TRP B CZ3   1 
ATOM   3168 C CH2   . TRP B 1 18  ? 27.974  -14.763 46.545 1.00 25.32 ?  18  TRP B CH2   1 
ATOM   3169 N N     . ASP B 1 19  ? 29.236  -8.534  51.571 1.00 32.18 ?  19  ASP B N     1 
ATOM   3170 C CA    . ASP B 1 19  ? 30.249  -7.526  51.815 1.00 29.39 ?  19  ASP B CA    1 
ATOM   3171 C C     . ASP B 1 19  ? 30.969  -7.680  53.144 1.00 21.15 ?  19  ASP B C     1 
ATOM   3172 O O     . ASP B 1 19  ? 32.024  -7.065  53.322 1.00 28.32 ?  19  ASP B O     1 
ATOM   3173 C CB    . ASP B 1 19  ? 29.605  -6.137  51.721 1.00 21.89 ?  19  ASP B CB    1 
ATOM   3174 C CG    . ASP B 1 19  ? 29.215  -5.787  50.298 1.00 34.86 ?  19  ASP B CG    1 
ATOM   3175 O OD1   . ASP B 1 19  ? 30.022  -6.031  49.384 1.00 42.74 ?  19  ASP B OD1   1 
ATOM   3176 O OD2   . ASP B 1 19  ? 28.086  -5.316  50.081 1.00 40.89 -1 19  ASP B OD2   1 
ATOM   3177 N N     . THR B 1 20  ? 30.518  -8.570  54.027 1.00 15.47 ?  20  THR B N     1 
ATOM   3178 C CA    . THR B 1 20  ? 31.192  -8.676  55.312 1.00 22.04 ?  20  THR B CA    1 
ATOM   3179 C C     . THR B 1 20  ? 32.579  -9.283  55.164 1.00 55.10 ?  20  THR B C     1 
ATOM   3180 O O     . THR B 1 20  ? 33.506  -8.898  55.888 1.00 65.31 ?  20  THR B O     1 
ATOM   3181 C CB    . THR B 1 20  ? 30.347  -9.490  56.274 1.00 21.26 ?  20  THR B CB    1 
ATOM   3182 O OG1   . THR B 1 20  ? 29.014  -8.967  56.275 1.00 36.54 ?  20  THR B OG1   1 
ATOM   3183 C CG2   . THR B 1 20  ? 30.912  -9.402  57.679 1.00 22.55 ?  20  THR B CG2   1 
ATOM   3184 N N     . TYR B 1 21  ? 32.744  -10.212 54.226 1.00 54.95 ?  21  TYR B N     1 
ATOM   3185 C CA    . TYR B 1 21  ? 34.045  -10.751 53.863 1.00 36.90 ?  21  TYR B CA    1 
ATOM   3186 C C     . TYR B 1 21  ? 34.519  -10.086 52.580 1.00 33.80 ?  21  TYR B C     1 
ATOM   3187 O O     . TYR B 1 21  ? 33.747  -9.935  51.625 1.00 41.79 ?  21  TYR B O     1 
ATOM   3188 C CB    . TYR B 1 21  ? 33.972  -12.256 53.633 1.00 35.75 ?  21  TYR B CB    1 
ATOM   3189 C CG    . TYR B 1 21  ? 33.664  -13.110 54.838 1.00 34.95 ?  21  TYR B CG    1 
ATOM   3190 C CD1   . TYR B 1 21  ? 32.371  -13.219 55.336 1.00 29.83 ?  21  TYR B CD1   1 
ATOM   3191 C CD2   . TYR B 1 21  ? 34.657  -13.852 55.445 1.00 32.26 ?  21  TYR B CD2   1 
ATOM   3192 C CE1   . TYR B 1 21  ? 32.091  -14.027 56.422 1.00 16.06 ?  21  TYR B CE1   1 
ATOM   3193 C CE2   . TYR B 1 21  ? 34.382  -14.654 56.525 1.00 35.94 ?  21  TYR B CE2   1 
ATOM   3194 C CZ    . TYR B 1 21  ? 33.102  -14.743 57.012 1.00 22.44 ?  21  TYR B CZ    1 
ATOM   3195 O OH    . TYR B 1 21  ? 32.857  -15.562 58.094 1.00 29.31 ?  21  TYR B OH    1 
ATOM   3196 N N     . LYS B 1 22  ? 35.799  -9.741  52.532 1.00 22.14 ?  22  LYS B N     1 
ATOM   3197 C CA    . LYS B 1 22  ? 36.320  -9.035  51.371 1.00 34.90 ?  22  LYS B CA    1 
ATOM   3198 C C     . LYS B 1 22  ? 37.108  -9.923  50.414 1.00 34.21 ?  22  LYS B C     1 
ATOM   3199 O O     . LYS B 1 22  ? 37.343  -9.511  49.273 1.00 29.77 ?  22  LYS B O     1 
ATOM   3200 C CB    . LYS B 1 22  ? 37.195  -7.850  51.815 1.00 41.03 ?  22  LYS B CB    1 
ATOM   3201 C CG    . LYS B 1 22  ? 36.442  -6.788  52.596 1.00 38.99 ?  22  LYS B CG    1 
ATOM   3202 C CD    . LYS B 1 22  ? 37.211  -5.492  52.637 1.00 37.34 ?  22  LYS B CD    1 
ATOM   3203 C CE    . LYS B 1 22  ? 36.275  -4.292  52.590 1.00 47.67 ?  22  LYS B CE    1 
ATOM   3204 N NZ    . LYS B 1 22  ? 37.012  -3.004  52.421 1.00 40.29 1  22  LYS B NZ    1 
ATOM   3205 N N     . ASN B 1 23  ? 37.465  -11.142 50.805 1.00 33.49 ?  23  ASN B N     1 
ATOM   3206 C CA    . ASN B 1 23  ? 38.151  -12.029 49.871 1.00 45.71 ?  23  ASN B CA    1 
ATOM   3207 C C     . ASN B 1 23  ? 37.164  -12.451 48.787 1.00 47.79 ?  23  ASN B C     1 
ATOM   3208 O O     . ASN B 1 23  ? 36.208  -13.187 49.051 1.00 44.51 ?  23  ASN B O     1 
ATOM   3209 C CB    . ASN B 1 23  ? 38.731  -13.241 50.595 1.00 50.36 ?  23  ASN B CB    1 
ATOM   3210 C CG    . ASN B 1 23  ? 39.280  -14.299 49.635 1.00 49.06 ?  23  ASN B CG    1 
ATOM   3211 O OD1   . ASN B 1 23  ? 39.906  -13.984 48.621 1.00 46.87 ?  23  ASN B OD1   1 
ATOM   3212 N ND2   . ASN B 1 23  ? 39.039  -15.562 49.959 1.00 45.06 ?  23  ASN B ND2   1 
ATOM   3213 N N     . GLU B 1 24  ? 37.381  -11.965 47.567 1.00 45.88 ?  24  GLU B N     1 
ATOM   3214 C CA    . GLU B 1 24  ? 36.429  -12.175 46.484 1.00 49.66 ?  24  GLU B CA    1 
ATOM   3215 C C     . GLU B 1 24  ? 36.367  -13.620 46.031 1.00 53.56 ?  24  GLU B C     1 
ATOM   3216 O O     . GLU B 1 24  ? 35.583  -13.933 45.127 1.00 65.10 ?  24  GLU B O     1 
ATOM   3217 C CB    . GLU B 1 24  ? 36.764  -11.268 45.301 1.00 50.73 ?  24  GLU B CB    1 
ATOM   3218 C CG    . GLU B 1 24  ? 36.988  -9.822  45.704 1.00 46.51 ?  24  GLU B CG    1 
ATOM   3219 C CD    . GLU B 1 24  ? 37.049  -8.887  44.519 1.00 47.40 ?  24  GLU B CD    1 
ATOM   3220 O OE1   . GLU B 1 24  ? 37.133  -9.369  43.371 1.00 46.08 ?  24  GLU B OE1   1 
ATOM   3221 O OE2   . GLU B 1 24  ? 37.039  -7.664  44.741 1.00 49.86 -1 24  GLU B OE2   1 
ATOM   3222 N N     . GLU B 1 25  ? 37.205  -14.492 46.585 1.00 48.92 ?  25  GLU B N     1 
ATOM   3223 C CA    . GLU B 1 25  ? 37.128  -15.910 46.275 1.00 43.79 ?  25  GLU B CA    1 
ATOM   3224 C C     . GLU B 1 25  ? 36.012  -16.621 47.030 1.00 42.55 ?  25  GLU B C     1 
ATOM   3225 O O     . GLU B 1 25  ? 35.658  -17.746 46.669 1.00 44.72 ?  25  GLU B O     1 
ATOM   3226 C CB    . GLU B 1 25  ? 38.467  -16.576 46.592 1.00 39.24 ?  25  GLU B CB    1 
ATOM   3227 C CG    . GLU B 1 25  ? 39.296  -16.899 45.374 1.00 41.40 ?  25  GLU B CG    1 
ATOM   3228 C CD    . GLU B 1 25  ? 40.603  -17.550 45.748 1.00 52.73 ?  25  GLU B CD    1 
ATOM   3229 O OE1   . GLU B 1 25  ? 41.278  -18.104 44.854 1.00 53.57 ?  25  GLU B OE1   1 
ATOM   3230 O OE2   . GLU B 1 25  ? 40.955  -17.500 46.946 1.00 57.63 -1 25  GLU B OE2   1 
ATOM   3231 N N     . LEU B 1 26  ? 35.430  -15.988 48.042 1.00 41.41 ?  26  LEU B N     1 
ATOM   3232 C CA    . LEU B 1 26  ? 34.455  -16.657 48.890 1.00 29.29 ?  26  LEU B CA    1 
ATOM   3233 C C     . LEU B 1 26  ? 33.089  -16.662 48.219 1.00 28.21 ?  26  LEU B C     1 
ATOM   3234 O O     . LEU B 1 26  ? 32.741  -15.742 47.475 1.00 24.64 ?  26  LEU B O     1 
ATOM   3235 C CB    . LEU B 1 26  ? 34.374  -15.987 50.265 1.00 23.83 ?  26  LEU B CB    1 
ATOM   3236 C CG    . LEU B 1 26  ? 35.638  -16.162 51.115 1.00 32.42 ?  26  LEU B CG    1 
ATOM   3237 C CD1   . LEU B 1 26  ? 35.591  -15.326 52.379 1.00 35.67 ?  26  LEU B CD1   1 
ATOM   3238 C CD2   . LEU B 1 26  ? 35.870  -17.628 51.447 1.00 28.47 ?  26  LEU B CD2   1 
ATOM   3239 N N     . ILE B 1 27  ? 32.384  -17.776 48.377 1.00 38.56 ?  27  ILE B N     1 
ATOM   3240 C CA    . ILE B 1 27  ? 30.969  -17.894 48.052 1.00 31.25 ?  27  ILE B CA    1 
ATOM   3241 C C     . ILE B 1 27  ? 30.188  -17.812 49.352 1.00 24.59 ?  27  ILE B C     1 
ATOM   3242 O O     . ILE B 1 27  ? 30.527  -18.492 50.324 1.00 20.95 ?  27  ILE B O     1 
ATOM   3243 C CB    . ILE B 1 27  ? 30.679  -19.207 47.308 1.00 34.16 ?  27  ILE B CB    1 
ATOM   3244 C CG1   . ILE B 1 27  ? 31.135  -19.087 45.855 1.00 30.34 ?  27  ILE B CG1   1 
ATOM   3245 C CG2   . ILE B 1 27  ? 29.209  -19.585 47.404 1.00 41.30 ?  27  ILE B CG2   1 
ATOM   3246 C CD1   . ILE B 1 27  ? 30.687  -17.830 45.179 1.00 19.73 ?  27  ILE B CD1   1 
ATOM   3247 N N     . HIS B 1 28  ? 29.141  -16.992 49.380 1.00 37.78 ?  28  HIS B N     1 
ATOM   3248 C CA    . HIS B 1 28  ? 28.386  -16.747 50.602 1.00 38.79 ?  28  HIS B CA    1 
ATOM   3249 C C     . HIS B 1 28  ? 26.988  -17.336 50.484 1.00 35.37 ?  28  HIS B C     1 
ATOM   3250 O O     . HIS B 1 28  ? 26.276  -17.074 49.505 1.00 32.19 ?  28  HIS B O     1 
ATOM   3251 C CB    . HIS B 1 28  ? 28.308  -15.254 50.904 1.00 36.86 ?  28  HIS B CB    1 
ATOM   3252 C CG    . HIS B 1 28  ? 29.637  -14.643 51.205 1.00 30.86 ?  28  HIS B CG    1 
ATOM   3253 N ND1   . HIS B 1 28  ? 30.402  -14.020 50.242 1.00 27.60 ?  28  HIS B ND1   1 
ATOM   3254 C CD2   . HIS B 1 28  ? 30.346  -14.573 52.355 1.00 27.65 ?  28  HIS B CD2   1 
ATOM   3255 C CE1   . HIS B 1 28  ? 31.521  -13.585 50.789 1.00 28.78 ?  28  HIS B CE1   1 
ATOM   3256 N NE2   . HIS B 1 28  ? 31.512  -13.907 52.070 1.00 29.45 ?  28  HIS B NE2   1 
ATOM   3257 N N     . ALA B 1 29  ? 26.621  -18.172 51.471 1.00 31.85 ?  29  ALA B N     1 
ATOM   3258 C CA    . ALA B 1 29  ? 25.313  -18.815 51.551 1.00 14.19 ?  29  ALA B CA    1 
ATOM   3259 C C     . ALA B 1 29  ? 24.851  -18.957 53.001 1.00 29.14 ?  29  ALA B C     1 
ATOM   3260 O O     . ALA B 1 29  ? 24.150  -19.917 53.344 1.00 31.09 ?  29  ALA B O     1 
ATOM   3261 C CB    . ALA B 1 29  ? 25.329  -20.177 50.854 1.00 14.53 ?  29  ALA B CB    1 
ATOM   3262 N N     . TRP B 1 30  ? 25.228  -18.009 53.863 1.00 39.90 ?  30  TRP B N     1 
ATOM   3263 C CA    . TRP B 1 30  ? 24.972  -18.083 55.298 1.00 24.24 ?  30  TRP B CA    1 
ATOM   3264 C C     . TRP B 1 30  ? 23.733  -17.290 55.720 1.00 30.13 ?  30  TRP B C     1 
ATOM   3265 O O     . TRP B 1 30  ? 22.763  -17.876 56.208 1.00 33.13 ?  30  TRP B O     1 
ATOM   3266 C CB    . TRP B 1 30  ? 26.224  -17.620 56.069 1.00 11.63 ?  30  TRP B CB    1 
ATOM   3267 C CG    . TRP B 1 30  ? 26.862  -16.337 55.606 1.00 9.00  ?  30  TRP B CG    1 
ATOM   3268 C CD1   . TRP B 1 30  ? 27.317  -16.048 54.351 1.00 22.60 ?  30  TRP B CD1   1 
ATOM   3269 C CD2   . TRP B 1 30  ? 27.144  -15.180 56.404 1.00 7.36  ?  30  TRP B CD2   1 
ATOM   3270 N NE1   . TRP B 1 30  ? 27.854  -14.780 54.315 1.00 26.49 ?  30  TRP B NE1   1 
ATOM   3271 C CE2   . TRP B 1 30  ? 27.757  -14.228 55.564 1.00 22.17 ?  30  TRP B CE2   1 
ATOM   3272 C CE3   . TRP B 1 30  ? 26.948  -14.861 57.746 1.00 6.85  ?  30  TRP B CE3   1 
ATOM   3273 C CZ2   . TRP B 1 30  ? 28.156  -12.976 56.021 1.00 15.56 ?  30  TRP B CZ2   1 
ATOM   3274 C CZ3   . TRP B 1 30  ? 27.334  -13.620 58.192 1.00 17.87 ?  30  TRP B CZ3   1 
ATOM   3275 C CH2   . TRP B 1 30  ? 27.935  -12.691 57.335 1.00 17.21 ?  30  TRP B CH2   1 
ATOM   3276 N N     . ILE B 1 31  ? 23.736  -15.962 55.535 1.00 34.18 ?  31  ILE B N     1 
ATOM   3277 C CA    . ILE B 1 31  ? 22.615  -15.139 55.992 1.00 12.46 ?  31  ILE B CA    1 
ATOM   3278 C C     . ILE B 1 31  ? 21.382  -15.412 55.134 1.00 7.19  ?  31  ILE B C     1 
ATOM   3279 O O     . ILE B 1 31  ? 21.463  -15.514 53.904 1.00 15.32 ?  31  ILE B O     1 
ATOM   3280 C CB    . ILE B 1 31  ? 23.026  -13.651 55.960 1.00 20.87 ?  31  ILE B CB    1 
ATOM   3281 C CG1   . ILE B 1 31  ? 24.050  -13.374 57.047 1.00 27.78 ?  31  ILE B CG1   1 
ATOM   3282 C CG2   . ILE B 1 31  ? 21.857  -12.699 56.183 1.00 25.58 ?  31  ILE B CG2   1 
ATOM   3283 C CD1   . ILE B 1 31  ? 23.701  -14.014 58.369 1.00 28.48 ?  31  ILE B CD1   1 
ATOM   3284 N N     . ALA B 1 32  ? 20.209  -15.377 55.766 1.00 17.07 ?  32  ALA B N     1 
ATOM   3285 C CA    . ALA B 1 32  ? 18.977  -15.890 55.157 1.00 12.16 ?  32  ALA B CA    1 
ATOM   3286 C C     . ALA B 1 32  ? 18.232  -14.811 54.377 1.00 28.56 ?  32  ALA B C     1 
ATOM   3287 O O     . ALA B 1 32  ? 17.060  -14.534 54.615 1.00 46.01 ?  32  ALA B O     1 
ATOM   3288 C CB    . ALA B 1 32  ? 18.071  -16.482 56.230 1.00 14.24 ?  32  ALA B CB    1 
ATOM   3289 N N     . ASP B 1 33  ? 18.932  -14.194 53.429 1.00 36.29 ?  33  ASP B N     1 
ATOM   3290 C CA    . ASP B 1 33  ? 18.300  -13.337 52.436 1.00 32.11 ?  33  ASP B CA    1 
ATOM   3291 C C     . ASP B 1 33  ? 18.575  -13.894 51.045 1.00 34.92 ?  33  ASP B C     1 
ATOM   3292 O O     . ASP B 1 33  ? 19.606  -14.523 50.806 1.00 51.42 ?  33  ASP B O     1 
ATOM   3293 C CB    . ASP B 1 33  ? 18.782  -11.860 52.540 1.00 34.57 ?  33  ASP B CB    1 
ATOM   3294 C CG    . ASP B 1 33  ? 20.299  -11.696 52.373 1.00 33.16 ?  33  ASP B CG    1 
ATOM   3295 O OD1   . ASP B 1 33  ? 21.031  -12.701 52.358 1.00 37.09 ?  33  ASP B OD1   1 
ATOM   3296 O OD2   . ASP B 1 33  ? 20.765  -10.546 52.241 1.00 26.04 -1 33  ASP B OD2   1 
ATOM   3297 N N     . MET B 1 34  ? 17.650  -13.673 50.123 1.00 36.03 ?  34  MET B N     1 
ATOM   3298 C CA    . MET B 1 34  ? 17.812  -14.246 48.797 1.00 35.97 ?  34  MET B CA    1 
ATOM   3299 C C     . MET B 1 34  ? 18.646  -13.312 47.931 1.00 38.87 ?  34  MET B C     1 
ATOM   3300 O O     . MET B 1 34  ? 18.674  -12.098 48.141 1.00 50.46 ?  34  MET B O     1 
ATOM   3301 C CB    . MET B 1 34  ? 16.452  -14.519 48.146 1.00 28.55 ?  34  MET B CB    1 
ATOM   3302 C CG    . MET B 1 34  ? 15.768  -15.721 48.773 1.00 31.67 ?  34  MET B CG    1 
ATOM   3303 S SD    . MET B 1 34  ? 14.111  -16.138 48.216 1.00 37.36 ?  34  MET B SD    1 
ATOM   3304 C CE    . MET B 1 34  ? 13.177  -14.679 48.667 1.00 23.16 ?  34  MET B CE    1 
ATOM   3305 N N     . ASP B 1 35  ? 19.345  -13.895 46.962 1.00 29.84 ?  35  ASP B N     1 
ATOM   3306 C CA    . ASP B 1 35  ? 20.124  -13.124 45.998 1.00 41.39 ?  35  ASP B CA    1 
ATOM   3307 C C     . ASP B 1 35  ? 19.355  -12.905 44.699 1.00 53.40 ?  35  ASP B C     1 
ATOM   3308 O O     . ASP B 1 35  ? 19.922  -12.988 43.602 1.00 61.24 ?  35  ASP B O     1 
ATOM   3309 C CB    . ASP B 1 35  ? 21.464  -13.806 45.741 1.00 34.45 ?  35  ASP B CB    1 
ATOM   3310 C CG    . ASP B 1 35  ? 22.327  -13.887 46.998 1.00 35.71 ?  35  ASP B CG    1 
ATOM   3311 O OD1   . ASP B 1 35  ? 22.151  -13.044 47.905 1.00 31.23 ?  35  ASP B OD1   1 
ATOM   3312 O OD2   . ASP B 1 35  ? 23.190  -14.787 47.077 1.00 31.98 -1 35  ASP B OD2   1 
ATOM   3313 N N     . PHE B 1 36  ? 18.055  -12.611 44.810 1.00 49.84 ?  36  PHE B N     1 
ATOM   3314 C CA    . PHE B 1 36  ? 17.161  -12.414 43.676 1.00 49.43 ?  36  PHE B CA    1 
ATOM   3315 C C     . PHE B 1 36  ? 16.656  -10.978 43.647 1.00 44.10 ?  36  PHE B C     1 
ATOM   3316 O O     . PHE B 1 36  ? 16.575  -10.310 44.680 1.00 37.41 ?  36  PHE B O     1 
ATOM   3317 C CB    . PHE B 1 36  ? 15.936  -13.365 43.723 1.00 48.34 ?  36  PHE B CB    1 
ATOM   3318 C CG    . PHE B 1 36  ? 16.262  -14.814 43.468 1.00 38.81 ?  36  PHE B CG    1 
ATOM   3319 C CD1   . PHE B 1 36  ? 17.116  -15.182 42.446 1.00 41.99 ?  36  PHE B CD1   1 
ATOM   3320 C CD2   . PHE B 1 36  ? 15.704  -15.811 44.256 1.00 32.70 ?  36  PHE B CD2   1 
ATOM   3321 C CE1   . PHE B 1 36  ? 17.410  -16.521 42.221 1.00 46.86 ?  36  PHE B CE1   1 
ATOM   3322 C CE2   . PHE B 1 36  ? 15.998  -17.146 44.034 1.00 27.91 ?  36  PHE B CE2   1 
ATOM   3323 C CZ    . PHE B 1 36  ? 16.848  -17.499 43.017 1.00 35.39 ?  36  PHE B CZ    1 
ATOM   3324 N N     . GLU B 1 37  ? 16.337  -10.505 42.444 1.00 48.08 ?  37  GLU B N     1 
ATOM   3325 C CA    . GLU B 1 37  ? 15.647  -9.230  42.298 1.00 39.03 ?  37  GLU B CA    1 
ATOM   3326 C C     . GLU B 1 37  ? 14.309  -9.273  43.021 1.00 38.32 ?  37  GLU B C     1 
ATOM   3327 O O     . GLU B 1 37  ? 13.519  -10.205 42.840 1.00 38.12 ?  37  GLU B O     1 
ATOM   3328 C CB    . GLU B 1 37  ? 15.427  -8.912  40.821 1.00 36.19 ?  37  GLU B CB    1 
ATOM   3329 C CG    . GLU B 1 37  ? 16.514  -8.059  40.224 1.00 45.48 ?  37  GLU B CG    1 
ATOM   3330 C CD    . GLU B 1 37  ? 16.192  -7.608  38.822 1.00 55.86 ?  37  GLU B CD    1 
ATOM   3331 O OE1   . GLU B 1 37  ? 17.021  -6.884  38.227 1.00 58.19 ?  37  GLU B OE1   1 
ATOM   3332 O OE2   . GLU B 1 37  ? 15.115  -7.984  38.314 1.00 55.20 -1 37  GLU B OE2   1 
ATOM   3333 N N     . VAL B 1 38  ? 14.052  -8.247  43.822 1.00 32.88 ?  38  VAL B N     1 
ATOM   3334 C CA    . VAL B 1 38  ? 12.769  -8.014  44.481 1.00 34.12 ?  38  VAL B CA    1 
ATOM   3335 C C     . VAL B 1 38  ? 11.678  -7.912  43.414 1.00 36.37 ?  38  VAL B C     1 
ATOM   3336 O O     . VAL B 1 38  ? 11.997  -7.648  42.243 1.00 36.12 ?  38  VAL B O     1 
ATOM   3337 C CB    . VAL B 1 38  ? 12.877  -6.765  45.375 1.00 40.81 ?  38  VAL B CB    1 
ATOM   3338 C CG1   . VAL B 1 38  ? 11.532  -6.297  45.895 1.00 42.75 ?  38  VAL B CG1   1 
ATOM   3339 C CG2   . VAL B 1 38  ? 13.830  -7.057  46.539 1.00 36.45 ?  38  VAL B CG2   1 
ATOM   3340 N N     . PRO B 1 39  ? 10.427  -8.278  43.711 1.00 34.04 ?  39  PRO B N     1 
ATOM   3341 C CA    . PRO B 1 39  ? 9.329   -8.019  42.763 1.00 32.22 ?  39  PRO B CA    1 
ATOM   3342 C C     . PRO B 1 39  ? 9.300   -6.571  42.289 1.00 42.26 ?  39  PRO B C     1 
ATOM   3343 O O     . PRO B 1 39  ? 9.420   -5.632  43.081 1.00 50.46 ?  39  PRO B O     1 
ATOM   3344 C CB    . PRO B 1 39  ? 8.074   -8.366  43.568 1.00 33.36 ?  39  PRO B CB    1 
ATOM   3345 C CG    . PRO B 1 39  ? 8.519   -9.301  44.607 1.00 34.48 ?  39  PRO B CG    1 
ATOM   3346 C CD    . PRO B 1 39  ? 10.001  -9.139  44.827 1.00 38.69 ?  39  PRO B CD    1 
ATOM   3347 N N     . LYS B 1 40  ? 9.128   -6.396  40.981 1.00 44.34 ?  40  LYS B N     1 
ATOM   3348 C CA    . LYS B 1 40  ? 9.125   -5.054  40.402 1.00 45.43 ?  40  LYS B CA    1 
ATOM   3349 C C     . LYS B 1 40  ? 8.024   -4.138  40.933 1.00 42.27 ?  40  LYS B C     1 
ATOM   3350 O O     . LYS B 1 40  ? 8.317   -2.953  41.166 1.00 40.76 ?  40  LYS B O     1 
ATOM   3351 C CB    . LYS B 1 40  ? 9.057   -5.163  38.873 1.00 49.30 ?  40  LYS B CB    1 
ATOM   3352 C CG    . LYS B 1 40  ? 9.850   -6.335  38.300 1.00 54.23 ?  40  LYS B CG    1 
ATOM   3353 C CD    . LYS B 1 40  ? 11.334  -6.295  38.708 1.00 56.43 ?  40  LYS B CD    1 
ATOM   3354 C CE    . LYS B 1 40  ? 12.010  -4.946  38.431 1.00 50.84 ?  40  LYS B CE    1 
ATOM   3355 N NZ    . LYS B 1 40  ? 13.503  -5.037  38.414 1.00 48.22 1  40  LYS B NZ    1 
ATOM   3356 N N     . PRO B 1 41  ? 6.774   -4.598  41.128 1.00 43.09 ?  41  PRO B N     1 
ATOM   3357 C CA    . PRO B 1 41  ? 5.810   -3.754  41.730 1.00 37.40 ?  41  PRO B CA    1 
ATOM   3358 C C     . PRO B 1 41  ? 6.362   -3.048  42.983 1.00 41.61 ?  41  PRO B C     1 
ATOM   3359 O O     . PRO B 1 41  ? 6.175   -1.892  43.130 1.00 45.75 ?  41  PRO B O     1 
ATOM   3360 C CB    . PRO B 1 41  ? 4.662   -4.718  42.029 1.00 37.78 ?  41  PRO B CB    1 
ATOM   3361 C CG    . PRO B 1 41  ? 4.633   -5.605  40.856 1.00 44.15 ?  41  PRO B CG    1 
ATOM   3362 C CD    . PRO B 1 41  ? 6.105   -5.877  40.715 1.00 49.18 ?  41  PRO B CD    1 
ATOM   3363 N N     . ILE B 1 42  ? 7.082   -3.744  43.843 1.00 48.54 ?  42  ILE B N     1 
ATOM   3364 C CA    . ILE B 1 42  ? 7.614   -3.134  45.061 1.00 45.07 ?  42  ILE B CA    1 
ATOM   3365 C C     . ILE B 1 42  ? 8.601   -2.021  44.714 1.00 52.31 ?  42  ILE B C     1 
ATOM   3366 O O     . ILE B 1 42  ? 8.518   -0.903  45.246 1.00 58.91 ?  42  ILE B O     1 
ATOM   3367 C CB    . ILE B 1 42  ? 8.282   -4.195  45.957 1.00 34.25 ?  42  ILE B CB    1 
ATOM   3368 C CG1   . ILE B 1 42  ? 7.336   -5.351  46.262 1.00 35.19 ?  42  ILE B CG1   1 
ATOM   3369 C CG2   . ILE B 1 42  ? 8.753   -3.569  47.253 1.00 25.83 ?  42  ILE B CG2   1 
ATOM   3370 C CD1   . ILE B 1 42  ? 7.920   -6.334  47.246 1.00 18.51 ?  42  ILE B CD1   1 
ATOM   3371 N N     . GLN B 1 43  ? 9.541   -2.314  43.804 1.00 32.48 ?  43  GLN B N     1 
ATOM   3372 C CA    . GLN B 1 43  ? 10.531  -1.328  43.385 1.00 22.05 ?  43  GLN B CA    1 
ATOM   3373 C C     . GLN B 1 43  ? 9.887   -0.137  42.698 1.00 37.25 ?  43  GLN B C     1 
ATOM   3374 O O     . GLN B 1 43  ? 10.392  0.983   42.779 1.00 29.33 ?  43  GLN B O     1 
ATOM   3375 C CB    . GLN B 1 43  ? 11.559  -1.969  42.465 1.00 19.11 ?  43  GLN B CB    1 
ATOM   3376 C CG    . GLN B 1 43  ? 11.975  -3.346  42.918 1.00 44.88 ?  43  GLN B CG    1 
ATOM   3377 C CD    . GLN B 1 43  ? 12.835  -4.075  41.899 1.00 60.35 ?  43  GLN B CD    1 
ATOM   3378 O OE1   . GLN B 1 43  ? 13.258  -3.489  40.904 1.00 62.02 ?  43  GLN B OE1   1 
ATOM   3379 N NE2   . GLN B 1 43  ? 13.079  -5.363  42.133 1.00 63.81 ?  43  GLN B NE2   1 
ATOM   3380 N N     . THR B 1 44  ? 8.767   -0.350  42.025 1.00 39.67 ?  44  THR B N     1 
ATOM   3381 C CA    . THR B 1 44  ? 8.128   0.773   41.355 1.00 36.30 ?  44  THR B CA    1 
ATOM   3382 C C     . THR B 1 44  ? 7.467   1.689   42.373 1.00 35.68 ?  44  THR B C     1 
ATOM   3383 O O     . THR B 1 44  ? 7.513   2.913   42.237 1.00 30.19 ?  44  THR B O     1 
ATOM   3384 C CB    . THR B 1 44  ? 7.111   0.273   40.317 1.00 30.97 ?  44  THR B CB    1 
ATOM   3385 O OG1   . THR B 1 44  ? 7.769   -0.614  39.399 1.00 33.59 ?  44  THR B OG1   1 
ATOM   3386 C CG2   . THR B 1 44  ? 6.557   1.425   39.534 1.00 34.70 ?  44  THR B CG2   1 
ATOM   3387 N N     . ALA B 1 45  ? 6.900   1.121   43.432 1.00 39.21 ?  45  ALA B N     1 
ATOM   3388 C CA    . ALA B 1 45  ? 6.358   1.962   44.494 1.00 47.43 ?  45  ALA B CA    1 
ATOM   3389 C C     . ALA B 1 45  ? 7.465   2.717   45.234 1.00 51.12 ?  45  ALA B C     1 
ATOM   3390 O O     . ALA B 1 45  ? 7.262   3.856   45.669 1.00 59.58 ?  45  ALA B O     1 
ATOM   3391 C CB    . ALA B 1 45  ? 5.521   1.122   45.462 1.00 50.54 ?  45  ALA B CB    1 
ATOM   3392 N N     . LEU B 1 46  ? 8.639   2.097   45.400 1.00 39.90 ?  46  LEU B N     1 
ATOM   3393 C CA    . LEU B 1 46  ? 9.716   2.737   46.154 1.00 21.22 ?  46  LEU B CA    1 
ATOM   3394 C C     . LEU B 1 46  ? 10.322  3.913   45.391 1.00 25.90 ?  46  LEU B C     1 
ATOM   3395 O O     . LEU B 1 46  ? 10.645  4.946   45.990 1.00 37.17 ?  46  LEU B O     1 
ATOM   3396 C CB    . LEU B 1 46  ? 10.793  1.708   46.511 1.00 20.82 ?  46  LEU B CB    1 
ATOM   3397 C CG    . LEU B 1 46  ? 10.386  0.575   47.476 1.00 30.10 ?  46  LEU B CG    1 
ATOM   3398 C CD1   . LEU B 1 46  ? 11.577  -0.329  47.816 1.00 22.45 ?  46  LEU B CD1   1 
ATOM   3399 C CD2   . LEU B 1 46  ? 9.707   1.087   48.760 1.00 34.81 ?  46  LEU B CD2   1 
ATOM   3400 N N     . LYS B 1 47  ? 10.497  3.782   44.076 1.00 26.39 ?  47  LYS B N     1 
ATOM   3401 C CA    . LYS B 1 47  ? 11.008  4.911   43.304 1.00 26.16 ?  47  LYS B CA    1 
ATOM   3402 C C     . LYS B 1 47  ? 9.920   5.950   43.054 1.00 39.91 ?  47  LYS B C     1 
ATOM   3403 O O     . LYS B 1 47  ? 10.228  7.131   42.869 1.00 27.95 ?  47  LYS B O     1 
ATOM   3404 C CB    . LYS B 1 47  ? 11.632  4.431   41.993 1.00 32.75 ?  47  LYS B CB    1 
ATOM   3405 C CG    . LYS B 1 47  ? 10.659  4.124   40.864 1.00 40.64 ?  47  LYS B CG    1 
ATOM   3406 C CD    . LYS B 1 47  ? 11.211  4.650   39.543 1.00 41.55 ?  47  LYS B CD    1 
ATOM   3407 C CE    . LYS B 1 47  ? 10.214  4.499   38.407 1.00 45.45 ?  47  LYS B CE    1 
ATOM   3408 N NZ    . LYS B 1 47  ? 10.901  4.446   37.082 1.00 45.38 1  47  LYS B NZ    1 
ATOM   3409 N N     . GLN B 1 48  ? 8.654   5.519   43.020 1.00 45.87 ?  48  GLN B N     1 
ATOM   3410 C CA    . GLN B 1 48  ? 7.535   6.452   42.953 1.00 39.40 ?  48  GLN B CA    1 
ATOM   3411 C C     . GLN B 1 48  ? 7.475   7.320   44.200 1.00 39.00 ?  48  GLN B C     1 
ATOM   3412 O O     . GLN B 1 48  ? 7.177   8.518   44.116 1.00 52.19 ?  48  GLN B O     1 
ATOM   3413 C CB    . GLN B 1 48  ? 6.225   5.688   42.783 1.00 37.83 ?  48  GLN B CB    1 
ATOM   3414 C CG    . GLN B 1 48  ? 5.097   6.510   42.221 1.00 42.48 ?  48  GLN B CG    1 
ATOM   3415 C CD    . GLN B 1 48  ? 3.871   5.676   41.986 1.00 48.98 ?  48  GLN B CD    1 
ATOM   3416 O OE1   . GLN B 1 48  ? 3.543   4.815   42.801 1.00 55.52 ?  48  GLN B OE1   1 
ATOM   3417 N NE2   . GLN B 1 48  ? 3.184   5.913   40.869 1.00 49.76 ?  48  GLN B NE2   1 
ATOM   3418 N N     . ARG B 1 49  ? 7.767   6.740   45.369 1.00 27.35 ?  49  ARG B N     1 
ATOM   3419 C CA    . ARG B 1 49  ? 7.655   7.506   46.605 1.00 31.58 ?  49  ARG B CA    1 
ATOM   3420 C C     . ARG B 1 49  ? 8.760   8.557   46.715 1.00 45.90 ?  49  ARG B C     1 
ATOM   3421 O O     . ARG B 1 49  ? 8.531   9.645   47.254 1.00 36.32 ?  49  ARG B O     1 
ATOM   3422 C CB    . ARG B 1 49  ? 7.696   6.578   47.820 1.00 21.29 ?  49  ARG B CB    1 
ATOM   3423 C CG    . ARG B 1 49  ? 7.717   7.315   49.181 1.00 27.24 ?  49  ARG B CG    1 
ATOM   3424 C CD    . ARG B 1 49  ? 6.605   8.359   49.238 1.00 34.65 ?  49  ARG B CD    1 
ATOM   3425 N NE    . ARG B 1 49  ? 6.416   8.950   50.559 1.00 33.86 ?  49  ARG B NE    1 
ATOM   3426 C CZ    . ARG B 1 49  ? 7.183   9.912   51.058 1.00 25.60 ?  49  ARG B CZ    1 
ATOM   3427 N NH1   . ARG B 1 49  ? 8.198   10.381  50.345 1.00 30.54 1  49  ARG B NH1   1 
ATOM   3428 N NH2   . ARG B 1 49  ? 6.932   10.410  52.259 1.00 19.23 ?  49  ARG B NH2   1 
ATOM   3429 N N     . ILE B 1 50  ? 9.947   8.273   46.167 1.00 51.80 ?  50  ILE B N     1 
ATOM   3430 C CA    . ILE B 1 50  ? 11.077  9.199   46.265 1.00 47.16 ?  50  ILE B CA    1 
ATOM   3431 C C     . ILE B 1 50  ? 10.812  10.456  45.455 1.00 43.46 ?  50  ILE B C     1 
ATOM   3432 O O     . ILE B 1 50  ? 11.401  11.510  45.726 1.00 38.70 ?  50  ILE B O     1 
ATOM   3433 C CB    . ILE B 1 50  ? 12.378  8.478   45.825 1.00 46.37 ?  50  ILE B CB    1 
ATOM   3434 C CG1   . ILE B 1 50  ? 12.767  7.437   46.866 1.00 51.82 ?  50  ILE B CG1   1 
ATOM   3435 C CG2   . ILE B 1 50  ? 13.560  9.432   45.652 1.00 35.50 ?  50  ILE B CG2   1 
ATOM   3436 C CD1   . ILE B 1 50  ? 14.078  6.728   46.570 1.00 53.32 ?  50  ILE B CD1   1 
ATOM   3437 N N     . LYS B 1 51  ? 9.870   10.389  44.513 1.00 48.63 ?  51  LYS B N     1 
ATOM   3438 C CA    . LYS B 1 51  ? 9.478   11.560  43.742 1.00 44.31 ?  51  LYS B CA    1 
ATOM   3439 C C     . LYS B 1 51  ? 8.936   12.689  44.609 1.00 44.68 ?  51  LYS B C     1 
ATOM   3440 O O     . LYS B 1 51  ? 8.866   13.823  44.129 1.00 45.52 ?  51  LYS B O     1 
ATOM   3441 C CB    . LYS B 1 51  ? 8.443   11.154  42.698 1.00 36.02 ?  51  LYS B CB    1 
ATOM   3442 C CG    . LYS B 1 51  ? 9.042   10.606  41.426 1.00 35.29 ?  51  LYS B CG    1 
ATOM   3443 C CD    . LYS B 1 51  ? 9.731   11.709  40.631 1.00 45.65 ?  51  LYS B CD    1 
ATOM   3444 C CE    . LYS B 1 51  ? 10.123  11.253  39.227 1.00 45.36 ?  51  LYS B CE    1 
ATOM   3445 N NZ    . LYS B 1 51  ? 8.954   10.951  38.362 1.00 42.58 1  51  LYS B NZ    1 
ATOM   3446 N N     . HIS B 1 52  ? 8.580   12.419  45.868 1.00 42.00 ?  52  HIS B N     1 
ATOM   3447 C CA    . HIS B 1 52  ? 8.177   13.453  46.811 1.00 39.82 ?  52  HIS B CA    1 
ATOM   3448 C C     . HIS B 1 52  ? 9.339   13.727  47.758 1.00 45.35 ?  52  HIS B C     1 
ATOM   3449 O O     . HIS B 1 52  ? 9.493   13.020  48.765 1.00 47.98 ?  52  HIS B O     1 
ATOM   3450 C CB    . HIS B 1 52  ? 6.928   13.026  47.591 1.00 28.88 ?  52  HIS B CB    1 
ATOM   3451 C CG    . HIS B 1 52  ? 6.317   14.129  48.390 1.00 31.90 ?  52  HIS B CG    1 
ATOM   3452 N ND1   . HIS B 1 52  ? 6.028   15.362  47.850 1.00 35.36 ?  52  HIS B ND1   1 
ATOM   3453 C CD2   . HIS B 1 52  ? 5.970   14.199  49.697 1.00 37.04 ?  52  HIS B CD2   1 
ATOM   3454 C CE1   . HIS B 1 52  ? 5.522   16.143  48.789 1.00 30.46 ?  52  HIS B CE1   1 
ATOM   3455 N NE2   . HIS B 1 52  ? 5.478   15.462  49.919 1.00 31.85 ?  52  HIS B NE2   1 
ATOM   3456 N N     . PRO B 1 53  ? 10.150  14.757  47.510 1.00 43.36 ?  53  PRO B N     1 
ATOM   3457 C CA    . PRO B 1 53  ? 11.396  14.937  48.268 1.00 32.58 ?  53  PRO B CA    1 
ATOM   3458 C C     . PRO B 1 53  ? 11.206  15.487  49.673 1.00 33.46 ?  53  PRO B C     1 
ATOM   3459 O O     . PRO B 1 53  ? 11.968  16.354  50.101 1.00 28.64 ?  53  PRO B O     1 
ATOM   3460 C CB    . PRO B 1 53  ? 12.168  15.935  47.405 1.00 26.86 ?  53  PRO B CB    1 
ATOM   3461 C CG    . PRO B 1 53  ? 11.095  16.750  46.772 1.00 41.69 ?  53  PRO B CG    1 
ATOM   3462 C CD    . PRO B 1 53  ? 9.950   15.820  46.511 1.00 48.99 ?  53  PRO B CD    1 
ATOM   3463 N N     . ILE B 1 54  ? 10.232  14.968  50.415 1.00 38.35 ?  54  ILE B N     1 
ATOM   3464 C CA    . ILE B 1 54  ? 10.086  15.259  51.837 1.00 36.91 ?  54  ILE B CA    1 
ATOM   3465 C C     . ILE B 1 54  ? 9.838   13.926  52.527 1.00 28.65 ?  54  ILE B C     1 
ATOM   3466 O O     . ILE B 1 54  ? 9.018   13.123  52.061 1.00 19.32 ?  54  ILE B O     1 
ATOM   3467 C CB    . ILE B 1 54  ? 8.940   16.255  52.135 1.00 28.74 ?  54  ILE B CB    1 
ATOM   3468 C CG1   . ILE B 1 54  ? 9.212   17.632  51.536 1.00 18.13 ?  54  ILE B CG1   1 
ATOM   3469 C CG2   . ILE B 1 54  ? 8.735   16.431  53.633 1.00 29.12 ?  54  ILE B CG2   1 
ATOM   3470 C CD1   . ILE B 1 54  ? 8.031   18.558  51.639 1.00 16.96 ?  54  ILE B CD1   1 
ATOM   3471 N N     . PHE B 1 55  ? 10.555  13.694  53.625 1.00 23.77 ?  55  PHE B N     1 
ATOM   3472 C CA    . PHE B 1 55  ? 10.561  12.433  54.356 1.00 23.50 ?  55  PHE B CA    1 
ATOM   3473 C C     . PHE B 1 55  ? 10.273  12.678  55.829 1.00 28.45 ?  55  PHE B C     1 
ATOM   3474 O O     . PHE B 1 55  ? 10.966  12.190  56.724 1.00 19.69 ?  55  PHE B O     1 
ATOM   3475 C CB    . PHE B 1 55  ? 11.890  11.700  54.175 1.00 26.77 ?  55  PHE B CB    1 
ATOM   3476 C CG    . PHE B 1 55  ? 12.306  11.528  52.732 1.00 31.67 ?  55  PHE B CG    1 
ATOM   3477 C CD1   . PHE B 1 55  ? 11.581  10.712  51.873 1.00 44.29 ?  55  PHE B CD1   1 
ATOM   3478 C CD2   . PHE B 1 55  ? 13.439  12.156  52.244 1.00 29.68 ?  55  PHE B CD2   1 
ATOM   3479 C CE1   . PHE B 1 55  ? 11.965  10.552  50.550 1.00 38.98 ?  55  PHE B CE1   1 
ATOM   3480 C CE2   . PHE B 1 55  ? 13.828  11.998  50.928 1.00 33.77 ?  55  PHE B CE2   1 
ATOM   3481 C CZ    . PHE B 1 55  ? 13.089  11.193  50.080 1.00 41.00 ?  55  PHE B CZ    1 
ATOM   3482 N N     . GLY B 1 56  ? 9.242   13.459  56.098 1.00 27.67 ?  56  GLY B N     1 
ATOM   3483 C CA    . GLY B 1 56  ? 8.840   13.724  57.459 1.00 27.84 ?  56  GLY B CA    1 
ATOM   3484 C C     . GLY B 1 56  ? 8.108   12.546  58.065 1.00 24.77 ?  56  GLY B C     1 
ATOM   3485 O O     . GLY B 1 56  ? 8.099   11.433  57.532 1.00 28.91 ?  56  GLY B O     1 
ATOM   3486 N N     . TYR B 1 57  ? 7.444   12.820  59.183 1.00 26.36 ?  57  TYR B N     1 
ATOM   3487 C CA    . TYR B 1 57  ? 6.730   11.779  59.898 1.00 23.21 ?  57  TYR B CA    1 
ATOM   3488 C C     . TYR B 1 57  ? 5.565   11.301  59.052 1.00 21.05 ?  57  TYR B C     1 
ATOM   3489 O O     . TYR B 1 57  ? 4.915   12.086  58.360 1.00 23.51 ?  57  TYR B O     1 
ATOM   3490 C CB    . TYR B 1 57  ? 6.216   12.288  61.237 1.00 20.38 ?  57  TYR B CB    1 
ATOM   3491 C CG    . TYR B 1 57  ? 7.293   12.715  62.193 1.00 18.21 ?  57  TYR B CG    1 
ATOM   3492 C CD1   . TYR B 1 57  ? 7.786   14.008  62.171 1.00 21.50 ?  57  TYR B CD1   1 
ATOM   3493 C CD2   . TYR B 1 57  ? 7.818   11.828  63.118 1.00 8.60  ?  57  TYR B CD2   1 
ATOM   3494 C CE1   . TYR B 1 57  ? 8.766   14.409  63.047 1.00 29.49 ?  57  TYR B CE1   1 
ATOM   3495 C CE2   . TYR B 1 57  ? 8.789   12.222  63.999 1.00 13.21 ?  57  TYR B CE2   1 
ATOM   3496 C CZ    . TYR B 1 57  ? 9.268   13.509  63.955 1.00 23.72 ?  57  TYR B CZ    1 
ATOM   3497 O OH    . TYR B 1 57  ? 10.239  13.899  64.836 1.00 29.17 ?  57  TYR B OH    1 
ATOM   3498 N N     . THR B 1 58  ? 5.340   10.001  59.070 1.00 8.34  ?  58  THR B N     1 
ATOM   3499 C CA    . THR B 1 58  ? 4.355   9.373   58.219 1.00 7.46  ?  58  THR B CA    1 
ATOM   3500 C C     . THR B 1 58  ? 3.435   8.541   59.094 1.00 6.10  ?  58  THR B C     1 
ATOM   3501 O O     . THR B 1 58  ? 3.823   8.118   60.184 1.00 5.48  ?  58  THR B O     1 
ATOM   3502 C CB    . THR B 1 58  ? 5.056   8.537   57.151 1.00 23.10 ?  58  THR B CB    1 
ATOM   3503 O OG1   . THR B 1 58  ? 5.915   9.389   56.377 1.00 31.39 ?  58  THR B OG1   1 
ATOM   3504 C CG2   . THR B 1 58  ? 4.067   7.858   56.237 1.00 27.82 ?  58  THR B CG2   1 
ATOM   3505 N N     . LEU B 1 59  ? 2.165   8.446   58.685 1.00 24.14 ?  59  LEU B N     1 
ATOM   3506 C CA    . LEU B 1 59  ? 1.151   7.555   59.249 1.00 27.45 ?  59  LEU B CA    1 
ATOM   3507 C C     . LEU B 1 59  ? 1.127   6.212   58.515 1.00 18.31 ?  59  LEU B C     1 
ATOM   3508 O O     . LEU B 1 59  ? 1.620   6.090   57.384 1.00 7.35  ?  59  LEU B O     1 
ATOM   3509 C CB    . LEU B 1 59  ? -0.242  8.210   59.177 1.00 34.99 ?  59  LEU B CB    1 
ATOM   3510 C CG    . LEU B 1 59  ? -0.639  9.501   59.927 1.00 21.07 ?  59  LEU B CG    1 
ATOM   3511 C CD1   . LEU B 1 59  ? -1.162  10.538  58.935 1.00 20.88 ?  59  LEU B CD1   1 
ATOM   3512 C CD2   . LEU B 1 59  ? -1.652  9.315   61.085 1.00 22.06 ?  59  LEU B CD2   1 
ATOM   3513 N N     . PRO B 1 60  ? 0.610   5.165   59.156 1.00 23.41 ?  60  PRO B N     1 
ATOM   3514 C CA    . PRO B 1 60  ? 0.217   3.948   58.417 1.00 7.91  ?  60  PRO B CA    1 
ATOM   3515 C C     . PRO B 1 60  ? -0.923  4.253   57.462 1.00 15.59 ?  60  PRO B C     1 
ATOM   3516 O O     . PRO B 1 60  ? -1.923  4.867   57.872 1.00 23.93 ?  60  PRO B O     1 
ATOM   3517 C CB    . PRO B 1 60  ? -0.241  2.996   59.528 1.00 12.54 ?  60  PRO B CB    1 
ATOM   3518 C CG    . PRO B 1 60  ? 0.334   3.527   60.771 1.00 24.41 ?  60  PRO B CG    1 
ATOM   3519 C CD    . PRO B 1 60  ? 0.484   4.999   60.611 1.00 34.60 ?  60  PRO B CD    1 
ATOM   3520 N N     . PRO B 1 61  ? -0.876  3.748   56.228 1.00 8.60  ?  61  PRO B N     1 
ATOM   3521 C CA    . PRO B 1 61  ? -1.898  4.124   55.237 1.00 23.44 ?  61  PRO B CA    1 
ATOM   3522 C C     . PRO B 1 61  ? -3.315  3.783   55.683 1.00 18.95 ?  61  PRO B C     1 
ATOM   3523 O O     . PRO B 1 61  ? -3.529  2.986   56.595 1.00 21.03 ?  61  PRO B O     1 
ATOM   3524 C CB    . PRO B 1 61  ? -1.483  3.333   53.993 1.00 27.51 ?  61  PRO B CB    1 
ATOM   3525 C CG    . PRO B 1 61  ? -0.032  3.142   54.159 1.00 12.76 ?  61  PRO B CG    1 
ATOM   3526 C CD    . PRO B 1 61  ? 0.157   2.900   55.626 1.00 8.77  ?  61  PRO B CD    1 
ATOM   3527 N N     . GLU B 1 62  ? -4.288  4.497   55.107 1.00 16.34 ?  62  GLU B N     1 
ATOM   3528 C CA    . GLU B 1 62  ? -5.681  4.281   55.492 1.00 29.35 ?  62  GLU B CA    1 
ATOM   3529 C C     . GLU B 1 62  ? -6.121  2.857   55.203 1.00 22.52 ?  62  GLU B C     1 
ATOM   3530 O O     . GLU B 1 62  ? -6.880  2.268   55.977 1.00 30.84 ?  62  GLU B O     1 
ATOM   3531 C CB    . GLU B 1 62  ? -6.595  5.265   54.767 1.00 34.71 ?  62  GLU B CB    1 
ATOM   3532 C CG    . GLU B 1 62  ? -6.500  6.671   55.297 1.00 35.73 ?  62  GLU B CG    1 
ATOM   3533 C CD    . GLU B 1 62  ? -7.474  7.622   54.625 1.00 31.72 ?  62  GLU B CD    1 
ATOM   3534 O OE1   . GLU B 1 62  ? -7.914  7.352   53.487 1.00 25.67 ?  62  GLU B OE1   1 
ATOM   3535 O OE2   . GLU B 1 62  ? -7.784  8.653   55.239 1.00 20.95 -1 62  GLU B OE2   1 
ATOM   3536 N N     . ASN B 1 63  ? -5.649  2.298   54.091 1.00 29.90 ?  63  ASN B N     1 
ATOM   3537 C CA    . ASN B 1 63  ? -6.071  1.027   53.511 1.00 37.46 ?  63  ASN B CA    1 
ATOM   3538 C C     . ASN B 1 63  ? -5.330  -0.186  54.066 1.00 30.32 ?  63  ASN B C     1 
ATOM   3539 O O     . ASN B 1 63  ? -5.745  -1.319  53.803 1.00 40.84 ?  63  ASN B O     1 
ATOM   3540 C CB    . ASN B 1 63  ? -5.840  1.106   52.010 1.00 46.55 ?  63  ASN B CB    1 
ATOM   3541 C CG    . ASN B 1 63  ? -4.572  1.848   51.684 1.00 50.63 ?  63  ASN B CG    1 
ATOM   3542 O OD1   . ASN B 1 63  ? -3.486  1.414   52.061 1.00 61.09 ?  63  ASN B OD1   1 
ATOM   3543 N ND2   . ASN B 1 63  ? -4.697  2.988   51.017 1.00 48.08 ?  63  ASN B ND2   1 
ATOM   3544 N N     . ILE B 1 64  ? -4.248  0.031   54.817 1.00 18.76 ?  64  ILE B N     1 
ATOM   3545 C CA    . ILE B 1 64  ? -3.309  -1.029  55.148 1.00 23.28 ?  64  ILE B CA    1 
ATOM   3546 C C     . ILE B 1 64  ? -3.980  -2.172  55.907 1.00 33.46 ?  64  ILE B C     1 
ATOM   3547 O O     . ILE B 1 64  ? -3.520  -3.319  55.851 1.00 27.99 ?  64  ILE B O     1 
ATOM   3548 C CB    . ILE B 1 64  ? -2.109  -0.426  55.914 1.00 18.74 ?  64  ILE B CB    1 
ATOM   3549 C CG1   . ILE B 1 64  ? -0.967  -1.436  55.961 1.00 10.29 ?  64  ILE B CG1   1 
ATOM   3550 C CG2   . ILE B 1 64  ? -2.506  0.079   57.295 1.00 8.77  ?  64  ILE B CG2   1 
ATOM   3551 C CD1   . ILE B 1 64  ? -0.470  -1.778  54.601 1.00 9.82  ?  64  ILE B CD1   1 
ATOM   3552 N N     . GLY B 1 65  ? -5.077  -1.890  56.610 1.00 46.65 ?  65  GLY B N     1 
ATOM   3553 C CA    . GLY B 1 65  ? -5.769  -2.944  57.340 1.00 35.35 ?  65  GLY B CA    1 
ATOM   3554 C C     . GLY B 1 65  ? -6.501  -3.928  56.447 1.00 28.12 ?  65  GLY B C     1 
ATOM   3555 O O     . GLY B 1 65  ? -6.509  -5.130  56.718 1.00 35.03 ?  65  GLY B O     1 
ATOM   3556 N N     . ASP B 1 66  ? -7.146  -3.435  55.386 1.00 25.96 ?  66  ASP B N     1 
ATOM   3557 C CA    . ASP B 1 66  ? -7.832  -4.327  54.458 1.00 25.08 ?  66  ASP B CA    1 
ATOM   3558 C C     . ASP B 1 66  ? -6.835  -5.202  53.722 1.00 35.55 ?  66  ASP B C     1 
ATOM   3559 O O     . ASP B 1 66  ? -7.046  -6.412  53.577 1.00 38.54 ?  66  ASP B O     1 
ATOM   3560 C CB    . ASP B 1 66  ? -8.644  -3.535  53.430 1.00 30.40 ?  66  ASP B CB    1 
ATOM   3561 C CG    . ASP B 1 66  ? -9.719  -2.669  54.053 1.00 33.38 ?  66  ASP B CG    1 
ATOM   3562 O OD1   . ASP B 1 66  ? -10.302 -3.061  55.083 1.00 37.18 ?  66  ASP B OD1   1 
ATOM   3563 O OD2   . ASP B 1 66  ? -9.989  -1.587  53.494 1.00 25.13 -1 66  ASP B OD2   1 
ATOM   3564 N N     . ILE B 1 67  ? -5.734  -4.604  53.263 1.00 48.43 ?  67  ILE B N     1 
ATOM   3565 C CA    . ILE B 1 67  ? -4.750  -5.330  52.462 1.00 39.93 ?  67  ILE B CA    1 
ATOM   3566 C C     . ILE B 1 67  ? -4.214  -6.534  53.226 1.00 27.86 ?  67  ILE B C     1 
ATOM   3567 O O     . ILE B 1 67  ? -4.180  -7.657  52.708 1.00 23.30 ?  67  ILE B O     1 
ATOM   3568 C CB    . ILE B 1 67  ? -3.614  -4.380  52.051 1.00 29.22 ?  67  ILE B CB    1 
ATOM   3569 C CG1   . ILE B 1 67  ? -4.119  -3.372  51.033 1.00 19.59 ?  67  ILE B CG1   1 
ATOM   3570 C CG2   . ILE B 1 67  ? -2.442  -5.160  51.504 1.00 36.75 ?  67  ILE B CG2   1 
ATOM   3571 C CD1   . ILE B 1 67  ? -3.146  -2.334  50.715 1.00 21.41 ?  67  ILE B CD1   1 
ATOM   3572 N N     . ILE B 1 68  ? -3.852  -6.331  54.490 1.00 21.98 ?  68  ILE B N     1 
ATOM   3573 C CA    . ILE B 1 68  ? -3.322  -7.418  55.298 1.00 22.31 ?  68  ILE B CA    1 
ATOM   3574 C C     . ILE B 1 68  ? -4.412  -8.434  55.604 1.00 30.13 ?  68  ILE B C     1 
ATOM   3575 O O     . ILE B 1 68  ? -4.164  -9.644  55.581 1.00 43.92 ?  68  ILE B O     1 
ATOM   3576 C CB    . ILE B 1 68  ? -2.675  -6.865  56.582 1.00 26.31 ?  68  ILE B CB    1 
ATOM   3577 C CG1   . ILE B 1 68  ? -1.556  -5.871  56.245 1.00 22.15 ?  68  ILE B CG1   1 
ATOM   3578 C CG2   . ILE B 1 68  ? -2.148  -8.006  57.435 1.00 25.55 ?  68  ILE B CG2   1 
ATOM   3579 C CD1   . ILE B 1 68  ? -1.011  -5.118  57.460 1.00 20.52 ?  68  ILE B CD1   1 
ATOM   3580 N N     . CYS B 1 69  ? -5.641  -7.971  55.881 1.00 39.40 ?  69  CYS B N     1 
ATOM   3581 C CA    . CYS B 1 69  ? -6.732  -8.912  56.150 1.00 30.61 ?  69  CYS B CA    1 
ATOM   3582 C C     . CYS B 1 69  ? -7.039  -9.737  54.919 1.00 25.98 ?  69  CYS B C     1 
ATOM   3583 O O     . CYS B 1 69  ? -7.340  -10.931 55.016 1.00 27.82 ?  69  CYS B O     1 
ATOM   3584 C CB    . CYS B 1 69  ? -8.006  -8.172  56.543 1.00 17.82 ?  69  CYS B CB    1 
ATOM   3585 S SG    . CYS B 1 69  ? -8.240  -7.686  58.238 1.00 24.61 ?  69  CYS B SG    1 
ATOM   3586 N N     . ASN B 1 70  ? -6.924  -9.118  53.748 1.00 24.34 ?  70  ASN B N     1 
ATOM   3587 C CA    . ASN B 1 70  ? -7.093  -9.844  52.499 1.00 35.29 ?  70  ASN B CA    1 
ATOM   3588 C C     . ASN B 1 70  ? -5.977  -10.855 52.311 1.00 46.50 ?  70  ASN B C     1 
ATOM   3589 O O     . ASN B 1 70  ? -6.238  -12.025 52.010 1.00 55.01 ?  70  ASN B O     1 
ATOM   3590 C CB    . ASN B 1 70  ? -7.120  -8.858  51.323 1.00 35.76 ?  70  ASN B CB    1 
ATOM   3591 C CG    . ASN B 1 70  ? -8.466  -8.194  51.152 1.00 50.05 ?  70  ASN B CG    1 
ATOM   3592 O OD1   . ASN B 1 70  ? -9.446  -8.601  51.780 1.00 56.37 ?  70  ASN B OD1   1 
ATOM   3593 N ND2   . ASN B 1 70  ? -8.529  -7.177  50.290 1.00 47.25 ?  70  ASN B ND2   1 
ATOM   3594 N N     . TRP B 1 71  ? -4.707  -10.437 52.442 1.00 41.53 ?  71  TRP B N     1 
ATOM   3595 C CA    . TRP B 1 71  ? -3.523  -11.338 52.351 1.00 27.26 ?  71  TRP B CA    1 
ATOM   3596 C C     . TRP B 1 71  ? -3.667  -12.547 53.245 1.00 23.18 ?  71  TRP B C     1 
ATOM   3597 O O     . TRP B 1 71  ? -3.531  -13.631 52.767 1.00 33.24 ?  71  TRP B O     1 
ATOM   3598 C CB    . TRP B 1 71  ? -2.272  -10.610 52.823 1.00 34.87 ?  71  TRP B CB    1 
ATOM   3599 C CG    . TRP B 1 71  ? -0.977  -11.304 52.536 1.00 24.69 ?  71  TRP B CG    1 
ATOM   3600 C CD1   . TRP B 1 71  ? -0.193  -11.969 53.430 1.00 27.52 ?  71  TRP B CD1   1 
ATOM   3601 C CD2   . TRP B 1 71  ? -0.293  -11.378 51.274 1.00 15.89 ?  71  TRP B CD2   1 
ATOM   3602 N NE1   . TRP B 1 71  ? 0.920   -12.459 52.811 1.00 35.33 ?  71  TRP B NE1   1 
ATOM   3603 C CE2   . TRP B 1 71  ? 0.889   -12.113 51.490 1.00 31.76 ?  71  TRP B CE2   1 
ATOM   3604 C CE3   . TRP B 1 71  ? -0.563  -10.910 49.986 1.00 24.67 ?  71  TRP B CE3   1 
ATOM   3605 C CZ2   . TRP B 1 71  ? 1.799   -12.378 50.469 1.00 41.31 ?  71  TRP B CZ2   1 
ATOM   3606 C CZ3   . TRP B 1 71  ? 0.338   -11.165 48.978 1.00 29.93 ?  71  TRP B CZ3   1 
ATOM   3607 C CH2   . TRP B 1 71  ? 1.501   -11.892 49.218 1.00 36.54 ?  71  TRP B CH2   1 
ATOM   3608 N N     . LYS B 1 73  ? -6.160  -13.996 54.431 1.00 44.14 ?  73  LYS B N     1 
ATOM   3609 C CA    . LYS B 1 73  ? -7.233  -14.935 54.072 1.00 51.13 ?  73  LYS B CA    1 
ATOM   3610 C C     . LYS B 1 73  ? -6.944  -15.406 52.647 1.00 55.35 ?  73  LYS B C     1 
ATOM   3611 O O     . LYS B 1 73  ? -7.119  -16.588 52.368 1.00 57.81 ?  73  LYS B O     1 
ATOM   3612 C CB    . LYS B 1 73  ? -8.600  -14.263 54.199 1.00 52.27 ?  73  LYS B CB    1 
ATOM   3613 C CG    . LYS B 1 73  ? -9.803  -15.135 53.879 1.00 44.15 ?  73  LYS B CG    1 
ATOM   3614 C CD    . LYS B 1 73  ? -10.667 -14.544 52.794 1.00 38.16 ?  73  LYS B CD    1 
ATOM   3615 C CE    . LYS B 1 73  ? -10.700 -15.386 51.539 1.00 38.29 ?  73  LYS B CE    1 
ATOM   3616 N NZ    . LYS B 1 73  ? -10.216 -14.633 50.361 1.00 42.70 1  73  LYS B NZ    1 
ATOM   3617 N N     . GLN B 1 74  ? -6.458  -14.523 51.787 1.00 51.68 ?  74  GLN B N     1 
ATOM   3618 C CA    . GLN B 1 74  ? -6.193  -15.024 50.444 1.00 45.10 ?  74  GLN B CA    1 
ATOM   3619 C C     . GLN B 1 74  ? -5.118  -16.104 50.477 1.00 41.33 ?  74  GLN B C     1 
ATOM   3620 O O     . GLN B 1 74  ? -5.197  -17.083 49.730 1.00 35.21 ?  74  GLN B O     1 
ATOM   3621 C CB    . GLN B 1 74  ? -5.783  -13.865 49.523 1.00 43.47 ?  74  GLN B CB    1 
ATOM   3622 C CG    . GLN B 1 74  ? -5.099  -14.272 48.200 1.00 51.98 ?  74  GLN B CG    1 
ATOM   3623 C CD    . GLN B 1 74  ? -4.415  -13.106 47.475 1.00 47.30 ?  74  GLN B CD    1 
ATOM   3624 O OE1   . GLN B 1 74  ? -4.184  -12.043 48.054 1.00 50.90 ?  74  GLN B OE1   1 
ATOM   3625 N NE2   . GLN B 1 74  ? -4.099  -13.306 46.200 1.00 44.45 ?  74  GLN B NE2   1 
ATOM   3626 N N     . GLN B 1 75  ? -4.135  -15.965 51.369 1.00 45.36 ?  75  GLN B N     1 
ATOM   3627 C CA    . GLN B 1 75  ? -3.001  -16.880 51.436 1.00 50.91 ?  75  GLN B CA    1 
ATOM   3628 C C     . GLN B 1 75  ? -3.239  -18.077 52.354 1.00 44.33 ?  75  GLN B C     1 
ATOM   3629 O O     . GLN B 1 75  ? -2.724  -19.168 52.075 1.00 31.69 ?  75  GLN B O     1 
ATOM   3630 C CB    . GLN B 1 75  ? -1.742  -16.128 51.889 1.00 43.79 ?  75  GLN B CB    1 
ATOM   3631 C CG    . GLN B 1 75  ? -1.310  -15.006 50.957 1.00 35.43 ?  75  GLN B CG    1 
ATOM   3632 C CD    . GLN B 1 75  ? -1.010  -15.489 49.561 1.00 39.40 ?  75  GLN B CD    1 
ATOM   3633 O OE1   . GLN B 1 75  ? -0.594  -16.630 49.363 1.00 44.10 ?  75  GLN B OE1   1 
ATOM   3634 N NE2   . GLN B 1 75  ? -1.225  -14.622 48.576 1.00 35.19 ?  75  GLN B NE2   1 
ATOM   3635 N N     . TYR B 1 76  ? -3.984  -17.868 53.438 1.00 42.01 ?  76  TYR B N     1 
ATOM   3636 C CA    . TYR B 1 76  ? -4.151  -18.949 54.437 1.00 35.05 ?  76  TYR B CA    1 
ATOM   3637 C C     . TYR B 1 76  ? -5.598  -19.126 54.930 1.00 33.58 ?  76  TYR B C     1 
ATOM   3638 O O     . TYR B 1 76  ? -5.772  -19.855 55.907 1.00 29.10 ?  76  TYR B O     1 
ATOM   3639 C CB    . TYR B 1 76  ? -3.177  -18.750 55.597 1.00 31.43 ?  76  TYR B CB    1 
ATOM   3640 C CG    . TYR B 1 76  ? -2.001  -17.843 55.368 1.00 35.06 ?  76  TYR B CG    1 
ATOM   3641 C CD1   . TYR B 1 76  ? -0.822  -18.320 54.827 1.00 32.87 ?  76  TYR B CD1   1 
ATOM   3642 C CD2   . TYR B 1 76  ? -2.055  -16.516 55.744 1.00 30.00 ?  76  TYR B CD2   1 
ATOM   3643 C CE1   . TYR B 1 76  ? 0.257   -17.483 54.619 1.00 40.80 ?  76  TYR B CE1   1 
ATOM   3644 C CE2   . TYR B 1 76  ? -0.989  -15.665 55.545 1.00 27.02 ?  76  TYR B CE2   1 
ATOM   3645 C CZ    . TYR B 1 76  ? 0.169   -16.152 54.981 1.00 38.72 ?  76  TYR B CZ    1 
ATOM   3646 O OH    . TYR B 1 76  ? 1.218   -15.306 54.804 1.00 43.20 ?  76  TYR B OH    1 
ATOM   3647 N N     . ASP B 1 77  ? -6.583  -18.503 54.284 1.00 43.64 ?  77  ASP B N     1 
ATOM   3648 C CA    . ASP B 1 77  ? -7.993  -18.633 54.667 1.00 48.67 ?  77  ASP B CA    1 
ATOM   3649 C C     . ASP B 1 77  ? -8.201  -18.430 56.167 1.00 54.62 ?  77  ASP B C     1 
ATOM   3650 O O     . ASP B 1 77  ? -8.895  -19.193 56.845 1.00 56.17 ?  77  ASP B O     1 
ATOM   3651 C CB    . ASP B 1 77  ? -8.541  -19.988 54.227 1.00 52.25 ?  77  ASP B CB    1 
ATOM   3652 C CG    . ASP B 1 77  ? -10.040 -20.043 54.278 1.00 47.25 ?  77  ASP B CG    1 
ATOM   3653 O OD1   . ASP B 1 77  ? -10.679 -19.465 53.378 1.00 45.98 ?  77  ASP B OD1   1 
ATOM   3654 O OD2   . ASP B 1 77  ? -10.573 -20.644 55.233 1.00 44.88 -1 77  ASP B OD2   1 
ATOM   3655 N N     . TRP B 1 78  ? -7.513  -17.437 56.694 1.00 50.59 ?  78  TRP B N     1 
ATOM   3656 C CA    . TRP B 1 78  ? -7.708  -17.070 58.109 1.00 39.20 ?  78  TRP B CA    1 
ATOM   3657 C C     . TRP B 1 78  ? -8.474  -15.741 58.073 1.00 44.14 ?  78  TRP B C     1 
ATOM   3658 O O     . TRP B 1 78  ? -8.089  -14.876 57.315 1.00 51.61 ?  78  TRP B O     1 
ATOM   3659 C CB    . TRP B 1 78  ? -6.327  -16.977 58.735 1.00 25.04 ?  78  TRP B CB    1 
ATOM   3660 C CG    . TRP B 1 78  ? -6.232  -16.657 60.188 1.00 21.28 ?  78  TRP B CG    1 
ATOM   3661 C CD1   . TRP B 1 78  ? -7.167  -16.824 61.164 1.00 26.30 ?  78  TRP B CD1   1 
ATOM   3662 C CD2   . TRP B 1 78  ? -5.067  -16.128 60.829 1.00 10.33 ?  78  TRP B CD2   1 
ATOM   3663 N NE1   . TRP B 1 78  ? -6.664  -16.418 62.369 1.00 21.11 ?  78  TRP B NE1   1 
ATOM   3664 C CE2   . TRP B 1 78  ? -5.376  -15.993 62.193 1.00 10.01 ?  78  TRP B CE2   1 
ATOM   3665 C CE3   . TRP B 1 78  ? -3.806  -15.745 60.370 1.00 9.94  ?  78  TRP B CE3   1 
ATOM   3666 C CZ2   . TRP B 1 78  ? -4.461  -15.484 63.105 1.00 12.75 ?  78  TRP B CZ2   1 
ATOM   3667 C CZ3   . TRP B 1 78  ? -2.901  -15.251 61.274 1.00 9.25  ?  78  TRP B CZ3   1 
ATOM   3668 C CH2   . TRP B 1 78  ? -3.228  -15.125 62.620 1.00 8.95  ?  78  TRP B CH2   1 
ATOM   3669 N N     . ASP B 1 79  ? -9.546  -15.670 58.845 1.00 31.16 ?  79  ASP B N     1 
ATOM   3670 C CA    . ASP B 1 79  ? -10.384 -14.458 58.878 1.00 33.71 ?  79  ASP B CA    1 
ATOM   3671 C C     . ASP B 1 79  ? -9.971  -13.677 60.116 1.00 43.31 ?  79  ASP B C     1 
ATOM   3672 O O     . ASP B 1 79  ? -10.174 -14.176 61.219 1.00 53.79 ?  79  ASP B O     1 
ATOM   3673 C CB    . ASP B 1 79  ? -11.867 -14.789 58.678 1.00 19.69 ?  79  ASP B CB    1 
ATOM   3674 C CG    . ASP B 1 79  ? -12.137 -15.416 57.330 1.00 28.71 ?  79  ASP B CG    1 
ATOM   3675 O OD1   . ASP B 1 79  ? -11.966 -16.626 57.216 1.00 38.15 -1 79  ASP B OD1   1 
ATOM   3676 O OD2   . ASP B 1 79  ? -12.490 -14.681 56.410 1.00 30.08 -1 79  ASP B OD2   1 
ATOM   3677 N N     . ILE B 1 80  ? -9.356  -12.525 59.911 1.00 18.42 ?  80  ILE B N     1 
ATOM   3678 C CA    . ILE B 1 80  ? -8.946  -11.689 61.022 1.00 25.77 ?  80  ILE B CA    1 
ATOM   3679 C C     . ILE B 1 80  ? -9.753  -10.399 60.955 1.00 35.06 ?  80  ILE B C     1 
ATOM   3680 O O     . ILE B 1 80  ? -10.499 -10.151 60.007 1.00 37.79 ?  80  ILE B O     1 
ATOM   3681 C CB    . ILE B 1 80  ? -7.429  -11.404 61.033 1.00 26.12 ?  80  ILE B CB    1 
ATOM   3682 C CG1   . ILE B 1 80  ? -6.976  -10.763 59.722 1.00 17.11 ?  80  ILE B CG1   1 
ATOM   3683 C CG2   . ILE B 1 80  ? -6.652  -12.683 61.302 1.00 42.76 ?  80  ILE B CG2   1 
ATOM   3684 C CD1   . ILE B 1 80  ? -5.660  -10.049 59.805 1.00 13.15 ?  80  ILE B CD1   1 
ATOM   3685 N N     . GLN B 1 81  ? -9.647  -9.614  62.016 1.00 25.55 ?  81  GLN B N     1 
ATOM   3686 C CA    . GLN B 1 81  ? -10.233 -8.290  62.086 1.00 31.55 ?  81  GLN B CA    1 
ATOM   3687 C C     . GLN B 1 81  ? -9.098  -7.278  62.012 1.00 38.90 ?  81  GLN B C     1 
ATOM   3688 O O     . GLN B 1 81  ? -7.940  -7.607  62.286 1.00 24.75 ?  81  GLN B O     1 
ATOM   3689 C CB    . GLN B 1 81  ? -11.035 -8.096  63.379 1.00 35.82 ?  81  GLN B CB    1 
ATOM   3690 C CG    . GLN B 1 81  ? -11.884 -9.286  63.785 1.00 34.24 ?  81  GLN B CG    1 
ATOM   3691 C CD    . GLN B 1 81  ? -13.104 -9.422  62.931 1.00 45.99 ?  81  GLN B CD    1 
ATOM   3692 O OE1   . GLN B 1 81  ? -13.448 -8.513  62.181 1.00 53.06 ?  81  GLN B OE1   1 
ATOM   3693 N NE2   . GLN B 1 81  ? -13.773 -10.564 63.029 1.00 61.98 ?  81  GLN B NE2   1 
ATOM   3694 N N     . LYS B 1 82  ? -9.426  -6.059  61.566 1.00 47.58 ?  82  LYS B N     1 
ATOM   3695 C CA    . LYS B 1 82  ? -8.408  -5.023  61.385 1.00 36.06 ?  82  LYS B CA    1 
ATOM   3696 C C     . LYS B 1 82  ? -7.763  -4.627  62.708 1.00 31.10 ?  82  LYS B C     1 
ATOM   3697 O O     . LYS B 1 82  ? -6.611  -4.178  62.739 1.00 36.82 ?  82  LYS B O     1 
ATOM   3698 C CB    . LYS B 1 82  ? -9.033  -3.793  60.719 1.00 39.78 ?  82  LYS B CB    1 
ATOM   3699 C CG    . LYS B 1 82  ? -9.037  -3.809  59.196 1.00 38.32 ?  82  LYS B CG    1 
ATOM   3700 C CD    . LYS B 1 82  ? -9.920  -2.687  58.654 1.00 42.13 ?  82  LYS B CD    1 
ATOM   3701 C CE    . LYS B 1 82  ? -11.341 -2.761  59.199 1.00 37.01 ?  82  LYS B CE    1 
ATOM   3702 N NZ    . LYS B 1 82  ? -12.280 -1.939  58.379 1.00 42.88 1  82  LYS B NZ    1 
ATOM   3703 N N     . GLU B 1 83  ? -8.481  -4.814  63.810 1.00 28.65 ?  83  GLU B N     1 
ATOM   3704 C CA    . GLU B 1 83  ? -8.053  -4.366  65.125 1.00 37.20 ?  83  GLU B CA    1 
ATOM   3705 C C     . GLU B 1 83  ? -6.889  -5.184  65.677 1.00 49.75 ?  83  GLU B C     1 
ATOM   3706 O O     . GLU B 1 83  ? -6.294  -4.797  66.692 1.00 51.20 ?  83  GLU B O     1 
ATOM   3707 C CB    . GLU B 1 83  ? -9.255  -4.435  66.082 1.00 42.46 ?  83  GLU B CB    1 
ATOM   3708 C CG    . GLU B 1 83  ? -10.503 -3.608  65.670 1.00 46.27 ?  83  GLU B CG    1 
ATOM   3709 C CD    . GLU B 1 83  ? -11.194 -4.079  64.384 1.00 55.45 ?  83  GLU B CD    1 
ATOM   3710 O OE1   . GLU B 1 83  ? -11.805 -5.165  64.382 1.00 59.41 ?  83  GLU B OE1   1 
ATOM   3711 O OE2   . GLU B 1 83  ? -11.131 -3.354  63.369 1.00 68.84 -1 83  GLU B OE2   1 
ATOM   3712 N N     . TRP B 1 84  ? -6.559  -6.307  65.048 1.00 47.59 ?  84  TRP B N     1 
ATOM   3713 C CA    . TRP B 1 84  ? -5.543  -7.197  65.594 1.00 31.70 ?  84  TRP B CA    1 
ATOM   3714 C C     . TRP B 1 84  ? -4.129  -6.822  65.173 1.00 18.84 ?  84  TRP B C     1 
ATOM   3715 O O     . TRP B 1 84  ? -3.178  -7.114  65.908 1.00 9.09  ?  84  TRP B O     1 
ATOM   3716 C CB    . TRP B 1 84  ? -5.852  -8.631  65.167 1.00 20.85 ?  84  TRP B CB    1 
ATOM   3717 C CG    . TRP B 1 84  ? -7.215  -9.074  65.564 1.00 16.59 ?  84  TRP B CG    1 
ATOM   3718 C CD1   . TRP B 1 84  ? -8.116  -8.377  66.310 1.00 13.72 ?  84  TRP B CD1   1 
ATOM   3719 C CD2   . TRP B 1 84  ? -7.837  -10.320 65.245 1.00 14.61 ?  84  TRP B CD2   1 
ATOM   3720 N NE1   . TRP B 1 84  ? -9.262  -9.113  66.481 1.00 18.74 ?  84  TRP B NE1   1 
ATOM   3721 C CE2   . TRP B 1 84  ? -9.118  -10.310 65.833 1.00 19.11 ?  84  TRP B CE2   1 
ATOM   3722 C CE3   . TRP B 1 84  ? -7.437  -11.444 64.515 1.00 9.65  ?  84  TRP B CE3   1 
ATOM   3723 C CZ2   . TRP B 1 84  ? -9.998  -11.380 65.719 1.00 27.13 ?  84  TRP B CZ2   1 
ATOM   3724 C CZ3   . TRP B 1 84  ? -8.310  -12.510 64.407 1.00 17.31 ?  84  TRP B CZ3   1 
ATOM   3725 C CH2   . TRP B 1 84  ? -9.576  -12.473 65.004 1.00 26.77 ?  84  TRP B CH2   1 
ATOM   3726 N N     . ILE B 1 85  ? -3.982  -6.092  64.070 1.00 23.32 ?  85  ILE B N     1 
ATOM   3727 C CA    . ILE B 1 85  ? -2.674  -5.880  63.466 1.00 20.92 ?  85  ILE B CA    1 
ATOM   3728 C C     . ILE B 1 85  ? -1.882  -4.900  64.316 1.00 19.09 ?  85  ILE B C     1 
ATOM   3729 O O     . ILE B 1 85  ? -2.344  -3.788  64.596 1.00 18.35 ?  85  ILE B O     1 
ATOM   3730 C CB    . ILE B 1 85  ? -2.821  -5.360  62.036 1.00 23.25 ?  85  ILE B CB    1 
ATOM   3731 C CG1   . ILE B 1 85  ? -3.522  -6.403  61.183 1.00 8.20  ?  85  ILE B CG1   1 
ATOM   3732 C CG2   . ILE B 1 85  ? -1.470  -4.951  61.469 1.00 30.82 ?  85  ILE B CG2   1 
ATOM   3733 C CD1   . ILE B 1 85  ? -3.806  -5.929  59.814 1.00 15.89 ?  85  ILE B CD1   1 
ATOM   3734 N N     . VAL B 1 86  ? -0.692  -5.319  64.748 1.00 25.55 ?  86  VAL B N     1 
ATOM   3735 C CA    . VAL B 1 86  ? 0.252   -4.453  65.456 1.00 31.23 ?  86  VAL B CA    1 
ATOM   3736 C C     . VAL B 1 86  ? 1.517   -4.338  64.615 1.00 25.96 ?  86  VAL B C     1 
ATOM   3737 O O     . VAL B 1 86  ? 1.876   -5.273  63.893 1.00 33.13 ?  86  VAL B O     1 
ATOM   3738 C CB    . VAL B 1 86  ? 0.579   -4.949  66.878 1.00 24.80 ?  86  VAL B CB    1 
ATOM   3739 C CG1   . VAL B 1 86  ? 1.229   -3.823  67.677 1.00 12.26 ?  86  VAL B CG1   1 
ATOM   3740 C CG2   . VAL B 1 86  ? -0.693  -5.446  67.578 1.00 35.89 ?  86  VAL B CG2   1 
ATOM   3741 N N     . PHE B 1 87  ? 2.157   -3.170  64.663 1.00 21.02 ?  87  PHE B N     1 
ATOM   3742 C CA    . PHE B 1 87  ? 3.348   -2.902  63.866 1.00 4.75  ?  87  PHE B CA    1 
ATOM   3743 C C     . PHE B 1 87  ? 4.622   -3.120  64.665 1.00 4.22  ?  87  PHE B C     1 
ATOM   3744 O O     . PHE B 1 87  ? 4.700   -2.802  65.855 1.00 3.90  ?  87  PHE B O     1 
ATOM   3745 C CB    . PHE B 1 87  ? 3.303   -1.480  63.295 1.00 4.78  ?  87  PHE B CB    1 
ATOM   3746 C CG    . PHE B 1 87  ? 2.388   -1.359  62.128 1.00 5.42  ?  87  PHE B CG    1 
ATOM   3747 C CD1   . PHE B 1 87  ? 2.835   -1.592  60.846 1.00 16.13 ?  87  PHE B CD1   1 
ATOM   3748 C CD2   . PHE B 1 87  ? 1.054   -1.101  62.325 1.00 5.72  ?  87  PHE B CD2   1 
ATOM   3749 C CE1   . PHE B 1 87  ? 1.966   -1.513  59.772 1.00 14.18 ?  87  PHE B CE1   1 
ATOM   3750 C CE2   . PHE B 1 87  ? 0.193   -1.030  61.266 1.00 15.05 ?  87  PHE B CE2   1 
ATOM   3751 C CZ    . PHE B 1 87  ? 0.653   -1.236  59.985 1.00 12.86 ?  87  PHE B CZ    1 
ATOM   3752 N N     . SER B 1 88  ? 5.619   -3.661  63.976 1.00 17.46 ?  88  SER B N     1 
ATOM   3753 C CA    . SER B 1 88  ? 6.930   -3.975  64.508 1.00 7.04  ?  88  SER B CA    1 
ATOM   3754 C C     . SER B 1 88  ? 7.952   -3.763  63.402 1.00 14.72 ?  88  SER B C     1 
ATOM   3755 O O     . SER B 1 88  ? 7.681   -3.999  62.224 1.00 21.46 ?  88  SER B O     1 
ATOM   3756 C CB    . SER B 1 88  ? 6.998   -5.418  65.009 1.00 7.17  ?  88  SER B CB    1 
ATOM   3757 O OG    . SER B 1 88  ? 8.103   -5.573  65.874 1.00 25.51 ?  88  SER B OG    1 
ATOM   3758 N N     . ALA B 1 89  ? 9.133   -3.323  63.799 1.00 8.75  ?  89  ALA B N     1 
ATOM   3759 C CA    . ALA B 1 89  ? 10.257  -3.134  62.896 1.00 3.75  ?  89  ALA B CA    1 
ATOM   3760 C C     . ALA B 1 89  ? 10.985  -4.439  62.582 1.00 25.61 ?  89  ALA B C     1 
ATOM   3761 O O     . ALA B 1 89  ? 12.076  -4.403  62.015 1.00 32.76 ?  89  ALA B O     1 
ATOM   3762 C CB    . ALA B 1 89  ? 11.231  -2.137  63.509 1.00 3.26  ?  89  ALA B CB    1 
ATOM   3763 N N     . GLY B 1 90  ? 10.471  -5.568  63.034 1.00 30.11 ?  90  GLY B N     1 
ATOM   3764 C CA    . GLY B 1 90  ? 11.096  -6.847  62.778 1.00 30.50 ?  90  GLY B CA    1 
ATOM   3765 C C     . GLY B 1 90  ? 10.555  -7.890  63.718 1.00 29.31 ?  90  GLY B C     1 
ATOM   3766 O O     . GLY B 1 90  ? 10.018  -7.595  64.784 1.00 42.35 ?  90  GLY B O     1 
ATOM   3767 N N     . ILE B 1 91  ? 10.756  -9.152  63.347 1.00 25.08 ?  91  ILE B N     1 
ATOM   3768 C CA    . ILE B 1 91  ? 10.214  -10.199 64.202 1.00 22.86 ?  91  ILE B CA    1 
ATOM   3769 C C     . ILE B 1 91  ? 11.039  -10.324 65.476 1.00 33.50 ?  91  ILE B C     1 
ATOM   3770 O O     . ILE B 1 91  ? 10.497  -10.678 66.527 1.00 35.27 ?  91  ILE B O     1 
ATOM   3771 C CB    . ILE B 1 91  ? 10.137  -11.548 63.456 1.00 20.53 ?  91  ILE B CB    1 
ATOM   3772 C CG1   . ILE B 1 91  ? 9.443   -11.384 62.094 1.00 32.58 ?  91  ILE B CG1   1 
ATOM   3773 C CG2   . ILE B 1 91  ? 9.437   -12.577 64.299 1.00 18.98 ?  91  ILE B CG2   1 
ATOM   3774 C CD1   . ILE B 1 91  ? 7.920   -11.170 62.136 1.00 22.94 ?  91  ILE B CD1   1 
ATOM   3775 N N     . VAL B 1 92  ? 12.336  -9.992  65.430 1.00 33.79 ?  92  VAL B N     1 
ATOM   3776 C CA    . VAL B 1 92  ? 13.166  -10.138 66.625 1.00 3.41  ?  92  VAL B CA    1 
ATOM   3777 C C     . VAL B 1 92  ? 12.747  -9.198  67.743 1.00 3.25  ?  92  VAL B C     1 
ATOM   3778 O O     . VAL B 1 92  ? 12.592  -9.668  68.886 1.00 28.68 ?  92  VAL B O     1 
ATOM   3779 C CB    . VAL B 1 92  ? 14.658  -10.022 66.240 1.00 18.22 ?  92  VAL B CB    1 
ATOM   3780 C CG1   . VAL B 1 92  ? 15.532  -10.651 67.309 1.00 16.05 ?  92  VAL B CG1   1 
ATOM   3781 C CG2   . VAL B 1 92  ? 14.910  -10.708 64.905 1.00 17.78 ?  92  VAL B CG2   1 
ATOM   3782 N N     . PRO B 1 93  ? 12.466  -7.910  67.512 1.00 13.86 ?  93  PRO B N     1 
ATOM   3783 C CA    . PRO B 1 93  ? 11.891  -7.110  68.606 1.00 14.65 ?  93  PRO B CA    1 
ATOM   3784 C C     . PRO B 1 93  ? 10.549  -7.649  69.102 1.00 19.90 ?  93  PRO B C     1 
ATOM   3785 O O     . PRO B 1 93  ? 10.279  -7.618  70.312 1.00 21.77 ?  93  PRO B O     1 
ATOM   3786 C CB    . PRO B 1 93  ? 11.774  -5.704  67.987 1.00 21.56 ?  93  PRO B CB    1 
ATOM   3787 C CG    . PRO B 1 93  ? 12.794  -5.672  66.899 1.00 2.97  ?  93  PRO B CG    1 
ATOM   3788 C CD    . PRO B 1 93  ? 12.803  -7.069  66.344 1.00 21.91 ?  93  PRO B CD    1 
ATOM   3789 N N     . ALA B 1 94  ? 9.718   -8.195  68.207 1.00 16.10 ?  94  ALA B N     1 
ATOM   3790 C CA    . ALA B 1 94  ? 8.431   -8.749  68.634 1.00 10.43 ?  94  ALA B CA    1 
ATOM   3791 C C     . ALA B 1 94  ? 8.602   -10.021 69.462 1.00 16.69 ?  94  ALA B C     1 
ATOM   3792 O O     . ALA B 1 94  ? 7.776   -10.299 70.337 1.00 14.66 ?  94  ALA B O     1 
ATOM   3793 C CB    . ALA B 1 94  ? 7.559   -9.054  67.423 1.00 11.77 ?  94  ALA B CB    1 
ATOM   3794 N N     . LEU B 1 95  ? 9.664   -10.799 69.220 1.00 14.21 ?  95  LEU B N     1 
ATOM   3795 C CA    . LEU B 1 95  ? 9.951   -11.916 70.117 1.00 10.99 ?  95  LEU B CA    1 
ATOM   3796 C C     . LEU B 1 95  ? 10.336  -11.404 71.492 1.00 10.48 ?  95  LEU B C     1 
ATOM   3797 O O     . LEU B 1 95  ? 9.907   -11.955 72.509 1.00 12.61 ?  95  LEU B O     1 
ATOM   3798 C CB    . LEU B 1 95  ? 11.069  -12.806 69.557 1.00 4.78  ?  95  LEU B CB    1 
ATOM   3799 C CG    . LEU B 1 95  ? 11.012  -13.177 68.071 1.00 9.89  ?  95  LEU B CG    1 
ATOM   3800 C CD1   . LEU B 1 95  ? 12.370  -13.621 67.495 1.00 5.41  ?  95  LEU B CD1   1 
ATOM   3801 C CD2   . LEU B 1 95  ? 9.961   -14.227 67.819 1.00 24.92 ?  95  LEU B CD2   1 
ATOM   3802 N N     . SER B 1 96  ? 11.097  -10.325 71.576 1.00 8.84  ?  96  SER B N     1 
ATOM   3803 C CA    . SER B 1 96  ? 11.564  -9.805  72.885 1.00 3.27  ?  96  SER B CA    1 
ATOM   3804 C C     . SER B 1 96  ? 10.408  -9.185  73.644 1.00 13.07 ?  96  SER B C     1 
ATOM   3805 O O     . SER B 1 96  ? 10.317  -9.446  74.802 1.00 13.57 ?  96  SER B O     1 
ATOM   3806 C CB    . SER B 1 96  ? 12.654  -8.831  72.701 1.00 13.06 ?  96  SER B CB    1 
ATOM   3807 O OG    . SER B 1 96  ? 12.787  -8.041  73.858 1.00 28.91 ?  96  SER B OG    1 
ATOM   3808 N N     . THR B 1 97  ? 9.572   -8.413  72.963 1.00 14.64 ?  97  THR B N     1 
ATOM   3809 C CA    . THR B 1 97  ? 8.385   -7.750  73.527 1.00 3.10  ?  97  THR B CA    1 
ATOM   3810 C C     . THR B 1 97  ? 7.363   -8.763  73.992 1.00 3.34  ?  97  THR B C     1 
ATOM   3811 O O     . THR B 1 97  ? 6.770   -8.523  75.003 1.00 3.32  ?  97  THR B O     1 
ATOM   3812 C CB    . THR B 1 97  ? 7.894   -6.780  72.452 1.00 23.60 ?  97  THR B CB    1 
ATOM   3813 O OG1   . THR B 1 97  ? 9.084   -6.045  72.211 1.00 17.01 ?  97  THR B OG1   1 
ATOM   3814 C CG2   . THR B 1 97  ? 6.795   -5.850  72.903 1.00 21.30 ?  97  THR B CG2   1 
ATOM   3815 N N     . SER B 1 98  ? 7.230   -9.865  73.268 1.00 7.87  ?  98  SER B N     1 
ATOM   3816 C CA    . SER B 1 98  ? 6.324   -10.968 73.640 1.00 3.83  ?  98  SER B CA    1 
ATOM   3817 C C     . SER B 1 98  ? 6.920   -11.669 74.846 1.00 11.04 ?  98  SER B C     1 
ATOM   3818 O O     . SER B 1 98  ? 6.143   -12.113 75.653 1.00 21.98 ?  98  SER B O     1 
ATOM   3819 C CB    . SER B 1 98  ? 6.048   -11.860 72.482 1.00 4.10  ?  98  SER B CB    1 
ATOM   3820 O OG    . SER B 1 98  ? 5.460   -11.176 71.403 1.00 4.21  ?  98  SER B OG    1 
ATOM   3821 N N     . ILE B 1 99  ? 8.255   -11.686 74.969 1.00 15.23 ?  99  ILE B N     1 
ATOM   3822 C CA    . ILE B 1 99  ? 8.904   -12.284 76.148 1.00 3.53  ?  99  ILE B CA    1 
ATOM   3823 C C     . ILE B 1 99  ? 8.589   -11.359 77.286 1.00 3.37  ?  99  ILE B C     1 
ATOM   3824 O O     . ILE B 1 99  ? 7.901   -11.815 78.078 1.00 11.77 ?  99  ILE B O     1 
ATOM   3825 C CB    . ILE B 1 99  ? 10.392  -12.620 75.939 1.00 3.41  ?  99  ILE B CB    1 
ATOM   3826 C CG1   . ILE B 1 99  ? 10.580  -13.948 75.208 1.00 14.08 ?  99  ILE B CG1   1 
ATOM   3827 C CG2   . ILE B 1 99  ? 11.177  -12.598 77.234 1.00 3.31  ?  99  ILE B CG2   1 
ATOM   3828 C CD1   . ILE B 1 99  ? 11.673  -13.936 74.177 1.00 30.47 ?  99  ILE B CD1   1 
ATOM   3829 N N     . GLN B 1 100 ? 8.867   -10.076 77.204 1.00 15.21 ?  100 GLN B N     1 
ATOM   3830 C CA    . GLN B 1 100 ? 8.703   -9.140  78.349 1.00 16.84 ?  100 GLN B CA    1 
ATOM   3831 C C     . GLN B 1 100 ? 7.228   -8.817  78.687 1.00 25.28 ?  100 GLN B C     1 
ATOM   3832 O O     . GLN B 1 100 ? 6.960   -8.498  79.859 1.00 3.07  ?  100 GLN B O     1 
ATOM   3833 C CB    . GLN B 1 100 ? 9.603   -7.910  78.248 1.00 15.26 ?  100 GLN B CB    1 
ATOM   3834 C CG    . GLN B 1 100 ? 10.868  -8.015  77.426 1.00 7.72  ?  100 GLN B CG    1 
ATOM   3835 C CD    . GLN B 1 100 ? 11.255  -6.620  77.006 1.00 8.31  ?  100 GLN B CD    1 
ATOM   3836 O OE1   . GLN B 1 100 ? 11.331  -6.291  75.829 1.00 5.54  ?  100 GLN B OE1   1 
ATOM   3837 N NE2   . GLN B 1 100 ? 11.461  -5.768  77.989 1.00 14.37 ?  100 GLN B NE2   1 
ATOM   3838 N N     . ALA B 1 101 ? 6.320   -9.028  77.728 1.00 13.19 ?  101 ALA B N     1 
ATOM   3839 C CA    . ALA B 1 101 ? 4.911   -8.773  78.022 1.00 14.04 ?  101 ALA B CA    1 
ATOM   3840 C C     . ALA B 1 101 ? 4.271   -9.888  78.837 1.00 3.96  ?  101 ALA B C     1 
ATOM   3841 O O     . ALA B 1 101 ? 3.595   -9.609  79.830 1.00 19.52 ?  101 ALA B O     1 
ATOM   3842 C CB    . ALA B 1 101 ? 4.131   -8.603  76.721 1.00 3.64  ?  101 ALA B CB    1 
ATOM   3843 N N     . PHE B 1 102 ? 4.530   -11.147 78.479 1.00 8.19  ?  102 PHE B N     1 
ATOM   3844 C CA    . PHE B 1 102 ? 3.741   -12.285 78.952 1.00 19.16 ?  102 PHE B CA    1 
ATOM   3845 C C     . PHE B 1 102 ? 4.450   -13.192 79.964 1.00 18.95 ?  102 PHE B C     1 
ATOM   3846 O O     . PHE B 1 102 ? 3.840   -14.147 80.437 1.00 15.23 ?  102 PHE B O     1 
ATOM   3847 C CB    . PHE B 1 102 ? 3.278   -13.130 77.748 1.00 18.31 ?  102 PHE B CB    1 
ATOM   3848 C CG    . PHE B 1 102 ? 2.598   -12.320 76.648 1.00 6.10  ?  102 PHE B CG    1 
ATOM   3849 C CD1   . PHE B 1 102 ? 1.592   -11.437 76.952 1.00 4.55  ?  102 PHE B CD1   1 
ATOM   3850 C CD2   . PHE B 1 102 ? 2.960   -12.464 75.326 1.00 5.59  ?  102 PHE B CD2   1 
ATOM   3851 C CE1   . PHE B 1 102 ? 0.975   -10.709 75.969 1.00 4.65  ?  102 PHE B CE1   1 
ATOM   3852 C CE2   . PHE B 1 102 ? 2.348   -11.733 74.347 1.00 6.50  ?  102 PHE B CE2   1 
ATOM   3853 C CZ    . PHE B 1 102 ? 1.352   -10.856 74.666 1.00 4.71  ?  102 PHE B CZ    1 
ATOM   3854 N N     . THR B 1 103 ? 5.656   -12.889 80.365 1.00 14.28 ?  103 THR B N     1 
ATOM   3855 C CA    . THR B 1 103 ? 6.370   -13.665 81.397 1.00 21.00 ?  103 THR B CA    1 
ATOM   3856 C C     . THR B 1 103 ? 6.976   -12.727 82.420 1.00 10.91 ?  103 THR B C     1 
ATOM   3857 O O     . THR B 1 103 ? 7.042   -11.564 82.196 1.00 15.34 ?  103 THR B O     1 
ATOM   3858 C CB    . THR B 1 103 ? 7.515   -14.539 80.863 1.00 25.35 ?  103 THR B CB    1 
ATOM   3859 O OG1   . THR B 1 103 ? 8.321   -13.948 79.848 1.00 15.81 ?  103 THR B OG1   1 
ATOM   3860 C CG2   . THR B 1 103 ? 7.027   -15.881 80.368 1.00 37.98 ?  103 THR B CG2   1 
ATOM   3861 N N     . LYS B 1 104 ? 7.252   -13.223 83.581 1.00 10.20 ?  104 LYS B N     1 
ATOM   3862 C CA    . LYS B 1 104 ? 7.978   -12.450 84.564 1.00 7.32  ?  104 LYS B CA    1 
ATOM   3863 C C     . LYS B 1 104 ? 9.457   -12.788 84.484 1.00 25.39 ?  104 LYS B C     1 
ATOM   3864 O O     . LYS B 1 104 ? 9.873   -13.735 83.809 1.00 33.83 ?  104 LYS B O     1 
ATOM   3865 C CB    . LYS B 1 104 ? 7.435   -12.736 85.958 1.00 4.18  ?  104 LYS B CB    1 
ATOM   3866 C CG    . LYS B 1 104 ? 5.966   -12.475 86.077 1.00 16.31 ?  104 LYS B CG    1 
ATOM   3867 C CD    . LYS B 1 104 ? 5.642   -11.167 85.412 1.00 23.66 ?  104 LYS B CD    1 
ATOM   3868 C CE    . LYS B 1 104 ? 4.216   -10.768 85.608 1.00 30.46 ?  104 LYS B CE    1 
ATOM   3869 N NZ    . LYS B 1 104 ? 3.249   -11.814 85.253 1.00 31.47 1  104 LYS B NZ    1 
ATOM   3870 N N     . GLU B 1 105 ? 10.265  -11.978 85.147 1.00 8.17  ?  105 GLU B N     1 
ATOM   3871 C CA    . GLU B 1 105 ? 11.683  -12.272 85.145 1.00 24.53 ?  105 GLU B CA    1 
ATOM   3872 C C     . GLU B 1 105 ? 11.892  -13.647 85.785 1.00 32.83 ?  105 GLU B C     1 
ATOM   3873 O O     . GLU B 1 105 ? 11.108  -14.071 86.641 1.00 3.26  ?  105 GLU B O     1 
ATOM   3874 C CB    . GLU B 1 105 ? 12.467  -11.164 85.873 1.00 31.59 ?  105 GLU B CB    1 
ATOM   3875 C CG    . GLU B 1 105 ? 13.103  -10.135 84.920 1.00 2.62  ?  105 GLU B CG    1 
ATOM   3876 C CD    . GLU B 1 105 ? 14.207  -9.329  85.561 1.00 10.25 ?  105 GLU B CD    1 
ATOM   3877 O OE1   . GLU B 1 105 ? 14.931  -8.627  84.824 1.00 19.90 ?  105 GLU B OE1   1 
ATOM   3878 O OE2   . GLU B 1 105 ? 14.340  -9.372  86.798 1.00 7.90  -1 105 GLU B OE2   1 
ATOM   3879 N N     . ASN B 1 106 ? 12.873  -14.395 85.270 1.00 27.16 ?  106 ASN B N     1 
ATOM   3880 C CA    . ASN B 1 106 ? 13.259  -15.723 85.750 1.00 22.13 ?  106 ASN B CA    1 
ATOM   3881 C C     . ASN B 1 106 ? 12.171  -16.781 85.574 1.00 15.88 ?  106 ASN B C     1 
ATOM   3882 O O     . ASN B 1 106 ? 12.232  -17.819 86.230 1.00 11.19 ?  106 ASN B O     1 
ATOM   3883 C CB    . ASN B 1 106 ? 13.703  -15.702 87.225 1.00 24.81 ?  106 ASN B CB    1 
ATOM   3884 C CG    . ASN B 1 106 ? 14.811  -14.689 87.505 1.00 34.52 ?  106 ASN B CG    1 
ATOM   3885 O OD1   . ASN B 1 106 ? 14.558  -13.575 87.971 1.00 31.80 ?  106 ASN B OD1   1 
ATOM   3886 N ND2   . ASN B 1 106 ? 16.038  -15.075 87.222 1.00 36.15 ?  106 ASN B ND2   1 
ATOM   3887 N N     . GLU B 1 107 ? 11.126  -16.504 84.794 1.00 6.89  ?  107 GLU B N     1 
ATOM   3888 C CA    . GLU B 1 107 ? 10.193  -17.515 84.332 1.00 14.23 ?  107 GLU B CA    1 
ATOM   3889 C C     . GLU B 1 107 ? 10.751  -18.149 83.059 1.00 19.24 ?  107 GLU B C     1 
ATOM   3890 O O     . GLU B 1 107 ? 11.536  -17.547 82.326 1.00 10.20 ?  107 GLU B O     1 
ATOM   3891 C CB    . GLU B 1 107 ? 8.794   -16.914 84.069 1.00 16.34 ?  107 GLU B CB    1 
ATOM   3892 C CG    . GLU B 1 107 ? 7.947   -16.627 85.328 1.00 7.57  ?  107 GLU B CG    1 
ATOM   3893 C CD    . GLU B 1 107 ? 6.567   -15.967 85.070 1.00 14.61 ?  107 GLU B CD    1 
ATOM   3894 O OE1   . GLU B 1 107 ? 5.786   -15.831 86.038 1.00 9.99  ?  107 GLU B OE1   1 
ATOM   3895 O OE2   . GLU B 1 107 ? 6.262   -15.578 83.926 1.00 12.47 -1 107 GLU B OE2   1 
ATOM   3896 N N     . SER B 1 108 ? 10.312  -19.367 82.831 1.00 14.27 ?  108 SER B N     1 
ATOM   3897 C CA    . SER B 1 108 ? 10.925  -20.142 81.755 1.00 16.15 ?  108 SER B CA    1 
ATOM   3898 C C     . SER B 1 108 ? 10.269  -19.892 80.416 1.00 22.40 ?  108 SER B C     1 
ATOM   3899 O O     . SER B 1 108 ? 9.186   -19.396 80.455 1.00 5.79  ?  108 SER B O     1 
ATOM   3900 C CB    . SER B 1 108 ? 11.087  -21.587 82.196 1.00 5.15  ?  108 SER B CB    1 
ATOM   3901 O OG    . SER B 1 108 ? 11.195  -21.672 83.603 1.00 4.48  ?  108 SER B OG    1 
ATOM   3902 N N     . VAL B 1 109 ? 11.026  -19.996 79.337 1.00 22.98 ?  109 VAL B N     1 
ATOM   3903 C CA    . VAL B 1 109 ? 10.583  -19.928 77.949 1.00 15.53 ?  109 VAL B CA    1 
ATOM   3904 C C     . VAL B 1 109 ? 11.142  -21.140 77.218 1.00 13.23 ?  109 VAL B C     1 
ATOM   3905 O O     . VAL B 1 109 ? 12.334  -21.432 77.345 1.00 4.48  ?  109 VAL B O     1 
ATOM   3906 C CB    . VAL B 1 109 ? 11.074  -18.628 77.285 1.00 4.18  ?  109 VAL B CB    1 
ATOM   3907 C CG1   . VAL B 1 109 ? 10.455  -18.435 75.893 1.00 4.28  ?  109 VAL B CG1   1 
ATOM   3908 C CG2   . VAL B 1 109 ? 10.850  -17.463 78.230 1.00 3.99  ?  109 VAL B CG2   1 
ATOM   3909 N N     . LEU B 1 110 ? 10.293  -21.799 76.412 1.00 18.08 ?  110 LEU B N     1 
ATOM   3910 C CA    . LEU B 1 110 ? 10.580  -23.089 75.782 1.00 13.66 ?  110 LEU B CA    1 
ATOM   3911 C C     . LEU B 1 110 ? 10.810  -22.957 74.281 1.00 8.62  ?  110 LEU B C     1 
ATOM   3912 O O     . LEU B 1 110 ? 10.048  -22.291 73.578 1.00 13.83 ?  110 LEU B O     1 
ATOM   3913 C CB    . LEU B 1 110 ? 9.427   -24.081 76.021 1.00 5.37  ?  110 LEU B CB    1 
ATOM   3914 C CG    . LEU B 1 110 ? 9.526   -25.533 75.496 1.00 9.94  ?  110 LEU B CG    1 
ATOM   3915 C CD1   . LEU B 1 110 ? 8.976   -26.577 76.476 1.00 9.07  ?  110 LEU B CD1   1 
ATOM   3916 C CD2   . LEU B 1 110 ? 8.895   -25.748 74.111 1.00 10.55 ?  110 LEU B CD2   1 
ATOM   3917 N N     . VAL B 1 111 ? 11.810  -23.676 73.777 1.00 5.06  ?  111 VAL B N     1 
ATOM   3918 C CA    . VAL B 1 111 ? 12.104  -23.706 72.354 1.00 5.09  ?  111 VAL B CA    1 
ATOM   3919 C C     . VAL B 1 111 ? 12.338  -25.160 71.964 1.00 18.39 ?  111 VAL B C     1 
ATOM   3920 O O     . VAL B 1 111 ? 12.498  -26.041 72.809 1.00 17.97 ?  111 VAL B O     1 
ATOM   3921 C CB    . VAL B 1 111 ? 13.318  -22.807 71.961 1.00 13.18 ?  111 VAL B CB    1 
ATOM   3922 C CG1   . VAL B 1 111 ? 13.087  -21.284 72.322 1.00 4.59  ?  111 VAL B CG1   1 
ATOM   3923 C CG2   . VAL B 1 111 ? 14.612  -23.301 72.565 1.00 4.74  ?  111 VAL B CG2   1 
ATOM   3924 N N     . GLN B 1 112 ? 12.271  -25.405 70.670 1.00 18.85 ?  112 GLN B N     1 
ATOM   3925 C CA    . GLN B 1 112 ? 12.397  -26.759 70.110 1.00 5.69  ?  112 GLN B CA    1 
ATOM   3926 C C     . GLN B 1 112 ? 13.616  -26.784 69.173 1.00 5.57  ?  112 GLN B C     1 
ATOM   3927 O O     . GLN B 1 112 ? 13.403  -26.637 67.983 1.00 10.73 ?  112 GLN B O     1 
ATOM   3928 C CB    . GLN B 1 112 ? 11.092  -27.132 69.421 1.00 26.55 ?  112 GLN B CB    1 
ATOM   3929 C CG    . GLN B 1 112 ? 9.887   -27.117 70.345 1.00 23.59 ?  112 GLN B CG    1 
ATOM   3930 C CD    . GLN B 1 112 ? 8.612   -27.260 69.559 1.00 33.12 ?  112 GLN B CD    1 
ATOM   3931 O OE1   . GLN B 1 112 ? 8.265   -26.406 68.753 1.00 28.69 ?  112 GLN B OE1   1 
ATOM   3932 N NE2   . GLN B 1 112 ? 7.909   -28.357 69.778 1.00 40.78 ?  112 GLN B NE2   1 
ATOM   3933 N N     . PRO B 1 113 ? 14.879  -26.945 69.660 1.00 5.43  ?  113 PRO B N     1 
ATOM   3934 C CA    . PRO B 1 113 ? 16.050  -26.954 68.779 1.00 5.36  ?  113 PRO B CA    1 
ATOM   3935 C C     . PRO B 1 113 ? 16.067  -28.196 67.904 1.00 27.45 ?  113 PRO B C     1 
ATOM   3936 O O     . PRO B 1 113 ? 15.481  -29.230 68.266 1.00 26.20 ?  113 PRO B O     1 
ATOM   3937 C CB    . PRO B 1 113 ? 17.229  -26.968 69.766 1.00 5.22  ?  113 PRO B CB    1 
ATOM   3938 C CG    . PRO B 1 113 ? 16.655  -27.464 71.028 1.00 5.28  ?  113 PRO B CG    1 
ATOM   3939 C CD    . PRO B 1 113 ? 15.260  -26.975 71.078 1.00 5.33  ?  113 PRO B CD    1 
ATOM   3940 N N     . PRO B 1 114 ? 16.788  -28.167 66.768 1.00 28.91 ?  114 PRO B N     1 
ATOM   3941 C CA    . PRO B 1 114 ? 17.602  -27.040 66.305 1.00 26.07 ?  114 PRO B CA    1 
ATOM   3942 C C     . PRO B 1 114 ? 16.753  -25.884 65.804 1.00 29.06 ?  114 PRO B C     1 
ATOM   3943 O O     . PRO B 1 114 ? 15.835  -26.100 65.023 1.00 49.50 ?  114 PRO B O     1 
ATOM   3944 C CB    . PRO B 1 114 ? 18.429  -27.647 65.169 1.00 14.84 ?  114 PRO B CB    1 
ATOM   3945 C CG    . PRO B 1 114 ? 17.608  -28.747 64.663 1.00 21.91 ?  114 PRO B CG    1 
ATOM   3946 C CD    . PRO B 1 114 ? 16.907  -29.324 65.865 1.00 24.53 ?  114 PRO B CD    1 
ATOM   3947 N N     . ILE B 1 115 ? 17.046  -24.669 66.253 1.00 23.50 ?  115 ILE B N     1 
ATOM   3948 C CA    . ILE B 1 115 ? 16.157  -23.541 66.008 1.00 29.92 ?  115 ILE B CA    1 
ATOM   3949 C C     . ILE B 1 115 ? 17.002  -22.273 65.974 1.00 31.69 ?  115 ILE B C     1 
ATOM   3950 O O     . ILE B 1 115 ? 18.093  -22.216 66.552 1.00 19.22 ?  115 ILE B O     1 
ATOM   3951 C CB    . ILE B 1 115 ? 15.023  -23.507 67.073 1.00 5.01  ?  115 ILE B CB    1 
ATOM   3952 C CG1   . ILE B 1 115 ? 13.876  -22.565 66.697 1.00 30.10 ?  115 ILE B CG1   1 
ATOM   3953 C CG2   . ILE B 1 115 ? 15.553  -23.179 68.418 1.00 4.84  ?  115 ILE B CG2   1 
ATOM   3954 C CD1   . ILE B 1 115 ? 12.493  -22.940 67.352 1.00 17.67 ?  115 ILE B CD1   1 
ATOM   3955 N N     . TYR B 1 116 ? 16.493  -21.264 65.233 1.00 40.01 ?  116 TYR B N     1 
ATOM   3956 C CA    . TYR B 1 116 ? 16.988  -19.903 65.038 1.00 21.76 ?  116 TYR B CA    1 
ATOM   3957 C C     . TYR B 1 116 ? 17.546  -19.347 66.333 1.00 16.59 ?  116 TYR B C     1 
ATOM   3958 O O     . TYR B 1 116 ? 16.822  -19.275 67.338 1.00 6.80  ?  116 TYR B O     1 
ATOM   3959 C CB    . TYR B 1 116 ? 15.860  -19.006 64.526 1.00 27.21 ?  116 TYR B CB    1 
ATOM   3960 C CG    . TYR B 1 116 ? 16.291  -17.658 63.972 1.00 33.74 ?  116 TYR B CG    1 
ATOM   3961 C CD1   . TYR B 1 116 ? 17.475  -17.514 63.270 1.00 27.91 ?  116 TYR B CD1   1 
ATOM   3962 C CD2   . TYR B 1 116 ? 15.488  -16.530 64.126 1.00 33.72 ?  116 TYR B CD2   1 
ATOM   3963 C CE1   . TYR B 1 116 ? 17.864  -16.286 62.757 1.00 25.30 ?  116 TYR B CE1   1 
ATOM   3964 C CE2   . TYR B 1 116 ? 15.867  -15.302 63.606 1.00 22.62 ?  116 TYR B CE2   1 
ATOM   3965 C CZ    . TYR B 1 116 ? 17.051  -15.189 62.929 1.00 31.10 ?  116 TYR B CZ    1 
ATOM   3966 O OH    . TYR B 1 116 ? 17.423  -13.966 62.423 1.00 45.80 ?  116 TYR B OH    1 
ATOM   3967 N N     . PRO B 1 117 ? 18.816  -18.944 66.343 1.00 21.86 ?  117 PRO B N     1 
ATOM   3968 C CA    . PRO B 1 117 ? 19.485  -18.585 67.605 1.00 4.19  ?  117 PRO B CA    1 
ATOM   3969 C C     . PRO B 1 117 ? 18.851  -17.403 68.325 1.00 5.08  ?  117 PRO B C     1 
ATOM   3970 O O     . PRO B 1 117 ? 18.820  -17.411 69.566 1.00 14.41 ?  117 PRO B O     1 
ATOM   3971 C CB    . PRO B 1 117 ? 20.919  -18.276 67.165 1.00 4.92  ?  117 PRO B CB    1 
ATOM   3972 C CG    . PRO B 1 117 ? 21.114  -19.033 65.892 1.00 6.60  ?  117 PRO B CG    1 
ATOM   3973 C CD    . PRO B 1 117 ? 19.774  -19.152 65.238 1.00 24.22 ?  117 PRO B CD    1 
ATOM   3974 N N     . PRO B 1 118 ? 18.310  -16.387 67.635 1.00 3.95  ?  118 PRO B N     1 
ATOM   3975 C CA    . PRO B 1 118 ? 17.692  -15.282 68.390 1.00 4.26  ?  118 PRO B CA    1 
ATOM   3976 C C     . PRO B 1 118 ? 16.638  -15.720 69.373 1.00 16.43 ?  118 PRO B C     1 
ATOM   3977 O O     . PRO B 1 118 ? 16.505  -15.113 70.446 1.00 17.81 ?  118 PRO B O     1 
ATOM   3978 C CB    . PRO B 1 118 ? 17.091  -14.412 67.284 1.00 3.76  ?  118 PRO B CB    1 
ATOM   3979 C CG    . PRO B 1 118 ? 18.025  -14.584 66.188 1.00 11.02 ?  118 PRO B CG    1 
ATOM   3980 C CD    . PRO B 1 118 ? 18.399  -16.039 66.206 1.00 17.32 ?  118 PRO B CD    1 
ATOM   3981 N N     . PHE B 1 119 ? 15.974  -16.841 69.101 1.00 12.96 ?  119 PHE B N     1 
ATOM   3982 C CA    . PHE B 1 119 ? 15.071  -17.399 70.089 1.00 3.98  ?  119 PHE B CA    1 
ATOM   3983 C C     . PHE B 1 119 ? 15.821  -17.709 71.377 1.00 19.98 ?  119 PHE B C     1 
ATOM   3984 O O     . PHE B 1 119 ? 15.316  -17.433 72.470 1.00 23.19 ?  119 PHE B O     1 
ATOM   3985 C CB    . PHE B 1 119 ? 14.418  -18.645 69.507 1.00 43.79 ?  119 PHE B CB    1 
ATOM   3986 C CG    . PHE B 1 119 ? 13.464  -18.353 68.381 1.00 37.74 ?  119 PHE B CG    1 
ATOM   3987 C CD1   . PHE B 1 119 ? 13.916  -17.853 67.169 1.00 30.56 ?  119 PHE B CD1   1 
ATOM   3988 C CD2   . PHE B 1 119 ? 12.113  -18.565 68.544 1.00 24.15 ?  119 PHE B CD2   1 
ATOM   3989 C CE1   . PHE B 1 119 ? 13.031  -17.581 66.151 1.00 21.36 ?  119 PHE B CE1   1 
ATOM   3990 C CE2   . PHE B 1 119 ? 11.239  -18.290 67.528 1.00 19.09 ?  119 PHE B CE2   1 
ATOM   3991 C CZ    . PHE B 1 119 ? 11.694  -17.799 66.339 1.00 12.05 ?  119 PHE B CZ    1 
ATOM   3992 N N     . PHE B 1 120 ? 17.069  -18.132 71.239 1.00 20.61 ?  120 PHE B N     1 
ATOM   3993 C CA    . PHE B 1 120 ? 17.934  -18.459 72.384 1.00 3.89  ?  120 PHE B CA    1 
ATOM   3994 C C     . PHE B 1 120 ? 18.418  -17.178 73.026 1.00 4.27  ?  120 PHE B C     1 
ATOM   3995 O O     . PHE B 1 120 ? 18.226  -17.097 74.181 1.00 11.69 ?  120 PHE B O     1 
ATOM   3996 C CB    . PHE B 1 120 ? 19.075  -19.388 71.958 1.00 15.18 ?  120 PHE B CB    1 
ATOM   3997 C CG    . PHE B 1 120 ? 18.782  -20.796 71.526 1.00 4.19  ?  120 PHE B CG    1 
ATOM   3998 C CD1   . PHE B 1 120 ? 18.552  -21.789 72.455 1.00 5.44  ?  120 PHE B CD1   1 
ATOM   3999 C CD2   . PHE B 1 120 ? 18.846  -21.142 70.193 1.00 4.29  ?  120 PHE B CD2   1 
ATOM   4000 C CE1   . PHE B 1 120 ? 18.332  -23.093 72.052 1.00 19.77 ?  120 PHE B CE1   1 
ATOM   4001 C CE2   . PHE B 1 120 ? 18.634  -22.445 69.792 1.00 11.33 ?  120 PHE B CE2   1 
ATOM   4002 C CZ    . PHE B 1 120 ? 18.369  -23.417 70.720 1.00 24.98 ?  120 PHE B CZ    1 
ATOM   4003 N N     . GLU B 1 121 ? 18.882  -16.205 72.268 1.00 4.41  ?  121 GLU B N     1 
ATOM   4004 C CA    . GLU B 1 121 ? 19.467  -15.020 72.881 1.00 15.08 ?  121 GLU B CA    1 
ATOM   4005 C C     . GLU B 1 121 ? 18.389  -14.125 73.508 1.00 21.69 ?  121 GLU B C     1 
ATOM   4006 O O     . GLU B 1 121 ? 18.590  -13.608 74.617 1.00 19.34 ?  121 GLU B O     1 
ATOM   4007 C CB    . GLU B 1 121 ? 20.306  -14.252 71.847 1.00 17.70 ?  121 GLU B CB    1 
ATOM   4008 C CG    . GLU B 1 121 ? 21.661  -14.881 71.502 1.00 18.62 ?  121 GLU B CG    1 
ATOM   4009 C CD    . GLU B 1 121 ? 22.589  -14.983 72.707 1.00 27.56 ?  121 GLU B CD    1 
ATOM   4010 O OE1   . GLU B 1 121 ? 22.701  -13.981 73.436 1.00 31.03 ?  121 GLU B OE1   1 
ATOM   4011 O OE2   . GLU B 1 121 ? 23.227  -16.044 72.910 1.00 23.34 -1 121 GLU B OE2   1 
ATOM   4012 N N     . MET B 1 122 ? 17.208  -14.022 72.880 1.00 3.37  ?  122 MET B N     1 
ATOM   4013 C CA    . MET B 1 122 ? 16.205  -13.056 73.340 1.00 12.46 ?  122 MET B CA    1 
ATOM   4014 C C     . MET B 1 122 ? 15.551  -13.491 74.645 1.00 3.26  ?  122 MET B C     1 
ATOM   4015 O O     . MET B 1 122 ? 15.300  -12.673 75.531 1.00 10.26 ?  122 MET B O     1 
ATOM   4016 C CB    . MET B 1 122 ? 15.144  -12.828 72.253 1.00 15.16 ?  122 MET B CB    1 
ATOM   4017 C CG    . MET B 1 122 ? 15.600  -12.190 70.931 1.00 17.76 ?  122 MET B CG    1 
ATOM   4018 S SD    . MET B 1 122 ? 16.914  -10.949 71.133 1.00 25.75 ?  122 MET B SD    1 
ATOM   4019 C CE    . MET B 1 122 ? 15.968  -9.700  71.939 1.00 21.39 ?  122 MET B CE    1 
ATOM   4020 N N     . VAL B 1 123 ? 15.306  -14.774 74.796 1.00 4.48  ?  123 VAL B N     1 
ATOM   4021 C CA    . VAL B 1 123 ? 14.893  -15.301 76.087 1.00 3.48  ?  123 VAL B CA    1 
ATOM   4022 C C     . VAL B 1 123 ? 15.992  -15.066 77.115 1.00 16.23 ?  123 VAL B C     1 
ATOM   4023 O O     . VAL B 1 123 ? 15.746  -14.587 78.230 1.00 32.60 ?  123 VAL B O     1 
ATOM   4024 C CB    . VAL B 1 123 ? 14.598  -16.804 75.949 1.00 10.36 ?  123 VAL B CB    1 
ATOM   4025 C CG1   . VAL B 1 123 ? 14.341  -17.421 77.296 1.00 10.48 ?  123 VAL B CG1   1 
ATOM   4026 C CG2   . VAL B 1 123 ? 13.489  -17.025 74.967 1.00 17.54 ?  123 VAL B CG2   1 
ATOM   4027 N N     . THR B 1 125 ? 18.984  -13.148 77.105 1.00 3.10  ?  125 THR B N     1 
ATOM   4028 C CA    . THR B 1 125 ? 19.490  -11.773 77.321 1.00 2.97  ?  125 THR B CA    1 
ATOM   4029 C C     . THR B 1 125 ? 18.522  -11.006 78.200 1.00 16.98 ?  125 THR B C     1 
ATOM   4030 O O     . THR B 1 125 ? 18.994  -10.145 78.946 1.00 23.57 ?  125 THR B O     1 
ATOM   4031 C CB    . THR B 1 125 ? 19.831  -11.063 76.014 1.00 2.97  ?  125 THR B CB    1 
ATOM   4032 O OG1   . THR B 1 125 ? 18.717  -11.067 75.126 1.00 23.14 ?  125 THR B OG1   1 
ATOM   4033 C CG2   . THR B 1 125 ? 21.072  -11.628 75.364 1.00 3.10  ?  125 THR B CG2   1 
ATOM   4034 N N     . ASN B 1 126 ? 17.253  -11.374 78.168 1.00 9.57  ?  126 ASN B N     1 
ATOM   4035 C CA    . ASN B 1 126 ? 16.237  -10.682 78.950 1.00 2.76  ?  126 ASN B CA    1 
ATOM   4036 C C     . ASN B 1 126 ? 15.981  -11.347 80.288 1.00 23.60 ?  126 ASN B C     1 
ATOM   4037 O O     . ASN B 1 126 ? 14.926  -11.130 80.886 1.00 23.22 ?  126 ASN B O     1 
ATOM   4038 C CB    . ASN B 1 126 ? 14.931  -10.586 78.174 1.00 2.80  ?  126 ASN B CB    1 
ATOM   4039 C CG    . ASN B 1 126 ? 14.876  -9.398  77.260 1.00 10.75 ?  126 ASN B CG    1 
ATOM   4040 O OD1   . ASN B 1 126 ? 14.673  -8.271  77.694 1.00 26.35 ?  126 ASN B OD1   1 
ATOM   4041 N ND2   . ASN B 1 126 ? 15.053  -9.644  75.974 1.00 2.79  ?  126 ASN B ND2   1 
ATOM   4042 N N     . ARG B 1 128 ? 15.183  -14.401 81.048 1.00 3.15  ?  128 ARG B N     1 
ATOM   4043 C CA    . ARG B 1 128 ? 14.230  -15.482 81.223 1.00 14.22 ?  128 ARG B CA    1 
ATOM   4044 C C     . ARG B 1 128 ? 14.933  -16.831 81.151 1.00 16.56 ?  128 ARG B C     1 
ATOM   4045 O O     . ARG B 1 128 ? 16.094  -16.942 80.740 1.00 34.74 ?  128 ARG B O     1 
ATOM   4046 C CB    . ARG B 1 128 ? 13.123  -15.412 80.190 1.00 12.40 ?  128 ARG B CB    1 
ATOM   4047 C CG    . ARG B 1 128 ? 11.940  -14.693 80.737 1.00 27.36 ?  128 ARG B CG    1 
ATOM   4048 C CD    . ARG B 1 128 ? 12.163  -13.215 80.619 1.00 30.45 ?  128 ARG B CD    1 
ATOM   4049 N NE    . ARG B 1 128 ? 10.938  -12.483 80.853 1.00 5.53  ?  128 ARG B NE    1 
ATOM   4050 C CZ    . ARG B 1 128 ? 10.895  -11.411 81.608 1.00 8.99  ?  128 ARG B CZ    1 
ATOM   4051 N NH1   . ARG B 1 128 ? 12.006  -10.980 82.167 1.00 2.85  1  128 ARG B NH1   1 
ATOM   4052 N NH2   . ARG B 1 128 ? 9.752   -10.779 81.794 1.00 19.88 ?  128 ARG B NH2   1 
ATOM   4053 N N     . GLN B 1 129 ? 14.224  -17.853 81.600 1.00 5.18  ?  129 GLN B N     1 
ATOM   4054 C CA    . GLN B 1 129 ? 14.808  -19.168 81.801 1.00 6.74  ?  129 GLN B CA    1 
ATOM   4055 C C     . GLN B 1 129 ? 14.621  -20.064 80.590 1.00 12.61 ?  129 GLN B C     1 
ATOM   4056 O O     . GLN B 1 129 ? 13.525  -20.156 80.030 1.00 17.33 ?  129 GLN B O     1 
ATOM   4057 C CB    . GLN B 1 129 ? 14.238  -19.845 83.033 1.00 7.37  ?  129 GLN B CB    1 
ATOM   4058 C CG    . GLN B 1 129 ? 14.966  -21.104 83.325 1.00 16.89 ?  129 GLN B CG    1 
ATOM   4059 C CD    . GLN B 1 129 ? 14.647  -21.606 84.676 1.00 24.31 ?  129 GLN B CD    1 
ATOM   4060 O OE1   . GLN B 1 129 ? 14.763  -20.877 85.671 1.00 9.20  ?  129 GLN B OE1   1 
ATOM   4061 N NE2   . GLN B 1 129 ? 14.177  -22.845 84.732 1.00 27.61 ?  129 GLN B NE2   1 
ATOM   4062 N N     . LEU B 1 130 ? 15.711  -20.699 80.181 1.00 14.67 ?  130 LEU B N     1 
ATOM   4063 C CA    . LEU B 1 130 ? 15.716  -21.642 79.069 1.00 18.47 ?  130 LEU B CA    1 
ATOM   4064 C C     . LEU B 1 130 ? 15.087  -22.987 79.461 1.00 22.33 ?  130 LEU B C     1 
ATOM   4065 O O     . LEU B 1 130 ? 15.481  -23.605 80.456 1.00 48.21 ?  130 LEU B O     1 
ATOM   4066 C CB    . LEU B 1 130 ? 17.144  -21.849 78.555 1.00 10.01 ?  130 LEU B CB    1 
ATOM   4067 C CG    . LEU B 1 130 ? 17.180  -22.579 77.210 1.00 15.80 ?  130 LEU B CG    1 
ATOM   4068 C CD1   . LEU B 1 130 ? 15.975  -22.224 76.340 1.00 21.39 ?  130 LEU B CD1   1 
ATOM   4069 C CD2   . LEU B 1 130 ? 18.434  -22.303 76.455 1.00 4.20  ?  130 LEU B CD2   1 
ATOM   4070 N N     . CYS B 1 131 ? 14.039  -23.370 78.743 1.00 16.82 ?  131 CYS B N     1 
ATOM   4071 C CA    . CYS B 1 131 ? 13.566  -24.747 78.683 1.00 11.68 ?  131 CYS B CA    1 
ATOM   4072 C C     . CYS B 1 131 ? 13.586  -25.241 77.246 1.00 6.50  ?  131 CYS B C     1 
ATOM   4073 O O     . CYS B 1 131 ? 13.074  -24.572 76.348 1.00 15.61 ?  131 CYS B O     1 
ATOM   4074 C CB    . CYS B 1 131 ? 12.148  -24.875 79.222 1.00 18.49 ?  131 CYS B CB    1 
ATOM   4075 S SG    . CYS B 1 131 ? 12.083  -24.694 80.978 1.00 37.02 ?  131 CYS B SG    1 
ATOM   4076 N N     . VAL B 1 132 ? 14.031  -26.469 77.039 1.00 12.58 ?  132 VAL B N     1 
ATOM   4077 C CA    . VAL B 1 132 ? 14.125  -26.964 75.673 1.00 21.73 ?  132 VAL B CA    1 
ATOM   4078 C C     . VAL B 1 132 ? 13.307  -28.232 75.545 1.00 22.97 ?  132 VAL B C     1 
ATOM   4079 O O     . VAL B 1 132 ? 13.192  -29.034 76.478 1.00 27.88 ?  132 VAL B O     1 
ATOM   4080 C CB    . VAL B 1 132 ? 15.576  -27.265 75.223 1.00 27.54 ?  132 VAL B CB    1 
ATOM   4081 C CG1   . VAL B 1 132 ? 16.322  -25.979 74.782 1.00 12.34 ?  132 VAL B CG1   1 
ATOM   4082 C CG2   . VAL B 1 132 ? 16.304  -28.027 76.320 1.00 5.21  ?  132 VAL B CG2   1 
ATOM   4083 N N     . SER B 1 133 ? 12.772  -28.423 74.348 1.00 5.73  ?  133 SER B N     1 
ATOM   4084 C CA    . SER B 1 133 ? 12.203  -29.697 73.936 1.00 10.63 ?  133 SER B CA    1 
ATOM   4085 C C     . SER B 1 133 ? 12.645  -29.972 72.507 1.00 18.20 ?  133 SER B C     1 
ATOM   4086 O O     . SER B 1 133 ? 11.876  -29.791 71.557 1.00 35.20 ?  133 SER B O     1 
ATOM   4087 C CB    . SER B 1 133 ? 10.680  -29.682 74.060 1.00 6.30  ?  133 SER B CB    1 
ATOM   4088 O OG    . SER B 1 133 ? 10.103  -30.786 73.391 1.00 26.34 ?  133 SER B OG    1 
ATOM   4089 N N     . PRO B 1 134 ? 13.878  -30.457 72.325 1.00 8.49  ?  134 PRO B N     1 
ATOM   4090 C CA    . PRO B 1 134 ? 14.393  -30.690 70.968 1.00 6.08  ?  134 PRO B CA    1 
ATOM   4091 C C     . PRO B 1 134 ? 13.520  -31.681 70.194 1.00 19.13 ?  134 PRO B C     1 
ATOM   4092 O O     . PRO B 1 134 ? 13.054  -32.687 70.732 1.00 14.34 ?  134 PRO B O     1 
ATOM   4093 C CB    . PRO B 1 134 ? 15.792  -31.286 71.216 1.00 6.00  ?  134 PRO B CB    1 
ATOM   4094 C CG    . PRO B 1 134 ? 16.103  -31.071 72.651 1.00 5.87  ?  134 PRO B CG    1 
ATOM   4095 C CD    . PRO B 1 134 ? 14.812  -30.906 73.376 1.00 11.63 ?  134 PRO B CD    1 
ATOM   4096 N N     . LEU B 1 135 ? 13.338  -31.402 68.907 1.00 17.93 ?  135 LEU B N     1 
ATOM   4097 C CA    . LEU B 1 135 ? 12.615  -32.269 67.986 1.00 26.48 ?  135 LEU B CA    1 
ATOM   4098 C C     . LEU B 1 135 ? 13.357  -33.582 67.737 1.00 23.86 ?  135 LEU B C     1 
ATOM   4099 O O     . LEU B 1 135 ? 14.567  -33.681 67.930 1.00 27.70 ?  135 LEU B O     1 
ATOM   4100 C CB    . LEU B 1 135 ? 12.422  -31.563 66.646 1.00 32.94 ?  135 LEU B CB    1 
ATOM   4101 C CG    . LEU B 1 135 ? 11.721  -30.240 66.837 1.00 17.24 ?  135 LEU B CG    1 
ATOM   4102 C CD1   . LEU B 1 135 ? 11.809  -29.325 65.623 1.00 6.58  ?  135 LEU B CD1   1 
ATOM   4103 C CD2   . LEU B 1 135 ? 10.306  -30.636 67.149 1.00 23.37 ?  135 LEU B CD2   1 
ATOM   4104 N N     . GLN B 1 136 ? 12.619  -34.578 67.234 1.00 22.55 ?  136 GLN B N     1 
ATOM   4105 C CA    . GLN B 1 136 ? 13.139  -35.914 66.971 1.00 7.50  ?  136 GLN B CA    1 
ATOM   4106 C C     . GLN B 1 136 ? 13.281  -36.125 65.467 1.00 28.84 ?  136 GLN B C     1 
ATOM   4107 O O     . GLN B 1 136 ? 12.343  -35.863 64.704 1.00 29.95 ?  136 GLN B O     1 
ATOM   4108 C CB    . GLN B 1 136 ? 12.216  -36.985 67.543 1.00 9.84  ?  136 GLN B CB    1 
ATOM   4109 C CG    . GLN B 1 136 ? 12.052  -36.958 69.042 1.00 18.76 ?  136 GLN B CG    1 
ATOM   4110 C CD    . GLN B 1 136 ? 11.826  -38.342 69.601 1.00 33.86 ?  136 GLN B CD    1 
ATOM   4111 O OE1   . GLN B 1 136 ? 11.762  -39.312 68.856 1.00 45.86 ?  136 GLN B OE1   1 
ATOM   4112 N NE2   . GLN B 1 136 ? 11.699  -38.444 70.913 1.00 41.29 ?  136 GLN B NE2   1 
ATOM   4113 N N     . LYS B 1 137 ? 14.474  -36.548 65.046 1.00 15.78 ?  137 LYS B N     1 
ATOM   4114 C CA    . LYS B 1 137 ? 14.788  -36.806 63.641 1.00 20.11 ?  137 LYS B CA    1 
ATOM   4115 C C     . LYS B 1 137 ? 14.241  -38.179 63.257 1.00 18.03 ?  137 LYS B C     1 
ATOM   4116 O O     . LYS B 1 137 ? 14.714  -39.203 63.761 1.00 22.02 ?  137 LYS B O     1 
ATOM   4117 C CB    . LYS B 1 137 ? 16.302  -36.713 63.440 1.00 22.20 ?  137 LYS B CB    1 
ATOM   4118 C CG    . LYS B 1 137 ? 16.811  -36.749 61.993 1.00 19.17 ?  137 LYS B CG    1 
ATOM   4119 C CD    . LYS B 1 137 ? 18.342  -36.615 61.981 1.00 22.60 ?  137 LYS B CD    1 
ATOM   4120 C CE    . LYS B 1 137 ? 18.883  -36.202 60.621 1.00 30.65 ?  137 LYS B CE    1 
ATOM   4121 N NZ    . LYS B 1 137 ? 18.727  -34.747 60.362 1.00 29.19 1  137 LYS B NZ    1 
ATOM   4122 N N     . GLN B 1 138 ? 13.251  -38.198 62.365 1.00 19.40 ?  138 GLN B N     1 
ATOM   4123 C CA    . GLN B 1 138 ? 12.609  -39.419 61.892 1.00 21.50 ?  138 GLN B CA    1 
ATOM   4124 C C     . GLN B 1 138 ? 12.323  -39.339 60.399 1.00 46.75 ?  138 GLN B C     1 
ATOM   4125 O O     . GLN B 1 138 ? 11.918  -38.288 59.894 1.00 59.93 ?  138 GLN B O     1 
ATOM   4126 C CB    . GLN B 1 138 ? 11.279  -39.682 62.605 1.00 20.50 ?  138 GLN B CB    1 
ATOM   4127 C CG    . GLN B 1 138 ? 11.380  -39.960 64.070 1.00 21.45 ?  138 GLN B CG    1 
ATOM   4128 C CD    . GLN B 1 138 ? 10.028  -40.178 64.675 1.00 18.83 ?  138 GLN B CD    1 
ATOM   4129 O OE1   . GLN B 1 138 ? 9.018   -40.157 63.974 1.00 22.54 ?  138 GLN B OE1   1 
ATOM   4130 N NE2   . GLN B 1 138 ? 9.991   -40.377 65.983 1.00 19.43 ?  138 GLN B NE2   1 
ATOM   4131 N N     . ASN B 1 139 ? 12.508  -40.465 59.703 1.00 53.23 ?  139 ASN B N     1 
ATOM   4132 C CA    . ASN B 1 139 ? 12.106  -40.622 58.298 1.00 52.79 ?  139 ASN B CA    1 
ATOM   4133 C C     . ASN B 1 139 ? 12.693  -39.515 57.425 1.00 62.99 ?  139 ASN B C     1 
ATOM   4134 O O     . ASN B 1 139 ? 12.029  -38.984 56.537 1.00 73.26 ?  139 ASN B O     1 
ATOM   4135 C CB    . ASN B 1 139 ? 10.578  -40.640 58.163 1.00 48.88 ?  139 ASN B CB    1 
ATOM   4136 C CG    . ASN B 1 139 ? 9.908   -41.656 59.090 1.00 62.04 ?  139 ASN B CG    1 
ATOM   4137 O OD1   . ASN B 1 139 ? 10.300  -42.836 59.159 1.00 71.42 ?  139 ASN B OD1   1 
ATOM   4138 N ND2   . ASN B 1 139 ? 8.901   -41.198 59.813 1.00 56.31 ?  139 ASN B ND2   1 
ATOM   4139 N N     . ASP B 1 140 ? 13.973  -39.178 57.651 1.00 40.87 ?  140 ASP B N     1 
ATOM   4140 C CA    . ASP B 1 140 ? 14.579  -38.034 56.910 1.00 37.57 ?  140 ASP B CA    1 
ATOM   4141 C C     . ASP B 1 140 ? 13.808  -36.712 57.146 1.00 38.00 ?  140 ASP B C     1 
ATOM   4142 O O     . ASP B 1 140 ? 13.799  -35.855 56.242 1.00 27.83 ?  140 ASP B O     1 
ATOM   4143 C CB    . ASP B 1 140 ? 14.871  -38.366 55.446 1.00 34.52 ?  140 ASP B CB    1 
ATOM   4144 C CG    . ASP B 1 140 ? 16.255  -38.942 55.218 1.00 46.01 ?  140 ASP B CG    1 
ATOM   4145 O OD1   . ASP B 1 140 ? 17.083  -38.837 56.134 1.00 50.16 ?  140 ASP B OD1   1 
ATOM   4146 O OD2   . ASP B 1 140 ? 16.496  -39.472 54.119 1.00 52.36 -1 140 ASP B OD2   1 
ATOM   4147 N N     . THR B 1 141 ? 13.253  -36.525 58.337 1.00 24.66 ?  141 THR B N     1 
ATOM   4148 C CA    . THR B 1 141 ? 12.596  -35.244 58.662 1.00 31.95 ?  141 THR B CA    1 
ATOM   4149 C C     . THR B 1 141 ? 12.618  -35.135 60.185 1.00 34.22 ?  141 THR B C     1 
ATOM   4150 O O     . THR B 1 141 ? 13.295  -35.925 60.792 1.00 39.27 ?  141 THR B O     1 
ATOM   4151 C CB    . THR B 1 141 ? 11.251  -35.049 57.944 1.00 42.96 ?  141 THR B CB    1 
ATOM   4152 O OG1   . THR B 1 141 ? 10.670  -33.796 58.283 1.00 37.69 ?  141 THR B OG1   1 
ATOM   4153 C CG2   . THR B 1 141 ? 10.245  -36.151 58.195 1.00 50.68 ?  141 THR B CG2   1 
ATOM   4154 N N     . TYR B 1 142 ? 11.947  -34.155 60.753 1.00 25.05 ?  142 TYR B N     1 
ATOM   4155 C CA    . TYR B 1 142 ? 11.849  -33.943 62.191 1.00 14.07 ?  142 TYR B CA    1 
ATOM   4156 C C     . TYR B 1 142 ? 10.399  -34.023 62.623 1.00 14.83 ?  142 TYR B C     1 
ATOM   4157 O O     . TYR B 1 142 ? 9.485   -33.656 61.882 1.00 22.56 ?  142 TYR B O     1 
ATOM   4158 C CB    . TYR B 1 142 ? 12.429  -32.586 62.625 1.00 14.11 ?  142 TYR B CB    1 
ATOM   4159 C CG    . TYR B 1 142 ? 13.929  -32.558 62.549 1.00 17.98 ?  142 TYR B CG    1 
ATOM   4160 C CD1   . TYR B 1 142 ? 14.567  -32.331 61.341 1.00 11.41 ?  142 TYR B CD1   1 
ATOM   4161 C CD2   . TYR B 1 142 ? 14.714  -32.799 63.670 1.00 32.59 ?  142 TYR B CD2   1 
ATOM   4162 C CE1   . TYR B 1 142 ? 15.945  -32.328 61.249 1.00 13.23 ?  142 TYR B CE1   1 
ATOM   4163 C CE2   . TYR B 1 142 ? 16.115  -32.798 63.579 1.00 6.65  ?  142 TYR B CE2   1 
ATOM   4164 C CZ    . TYR B 1 142 ? 16.710  -32.565 62.366 1.00 6.61  ?  142 TYR B CZ    1 
ATOM   4165 O OH    . TYR B 1 142 ? 18.077  -32.567 62.259 1.00 12.25 ?  142 TYR B OH    1 
ATOM   4166 N N     . VAL B 1 143 ? 10.204  -34.532 63.834 1.00 8.13  ?  143 VAL B N     1 
ATOM   4167 C CA    . VAL B 1 143 ? 8.895   -34.611 64.449 1.00 11.27 ?  143 VAL B CA    1 
ATOM   4168 C C     . VAL B 1 143 ? 9.003   -34.108 65.879 1.00 19.61 ?  143 VAL B C     1 
ATOM   4169 O O     . VAL B 1 143 ? 10.078  -34.105 66.489 1.00 19.80 ?  143 VAL B O     1 
ATOM   4170 C CB    . VAL B 1 143 ? 8.330   -36.049 64.413 1.00 25.32 ?  143 VAL B CB    1 
ATOM   4171 C CG1   . VAL B 1 143 ? 8.269   -36.552 62.965 1.00 34.07 ?  143 VAL B CG1   1 
ATOM   4172 C CG2   . VAL B 1 143 ? 9.179   -36.979 65.280 1.00 21.83 ?  143 VAL B CG2   1 
ATOM   4173 N N     . ILE B 1 144 ? 7.870   -33.665 66.404 1.00 25.75 ?  144 ILE B N     1 
ATOM   4174 C CA    . ILE B 1 144 ? 7.792   -33.165 67.769 1.00 24.24 ?  144 ILE B CA    1 
ATOM   4175 C C     . ILE B 1 144 ? 7.670   -34.345 68.723 1.00 21.60 ?  144 ILE B C     1 
ATOM   4176 O O     . ILE B 1 144 ? 6.935   -35.302 68.463 1.00 32.79 ?  144 ILE B O     1 
ATOM   4177 C CB    . ILE B 1 144 ? 6.608   -32.185 67.903 1.00 21.57 ?  144 ILE B CB    1 
ATOM   4178 C CG1   . ILE B 1 144 ? 6.798   -30.987 66.968 1.00 23.46 ?  144 ILE B CG1   1 
ATOM   4179 C CG2   . ILE B 1 144 ? 6.449   -31.694 69.318 1.00 16.63 ?  144 ILE B CG2   1 
ATOM   4180 C CD1   . ILE B 1 144 ? 5.779   -29.909 67.159 1.00 14.94 ?  144 ILE B CD1   1 
ATOM   4181 N N     . ASP B 1 145 ? 8.387   -34.274 69.838 1.00 17.05 ?  145 ASP B N     1 
ATOM   4182 C CA    . ASP B 1 145 ? 8.284   -35.262 70.906 1.00 15.47 ?  145 ASP B CA    1 
ATOM   4183 C C     . ASP B 1 145 ? 7.185   -34.809 71.853 1.00 20.50 ?  145 ASP B C     1 
ATOM   4184 O O     . ASP B 1 145 ? 7.444   -34.224 72.907 1.00 22.04 ?  145 ASP B O     1 
ATOM   4185 C CB    . ASP B 1 145 ? 9.614   -35.408 71.624 1.00 15.22 ?  145 ASP B CB    1 
ATOM   4186 C CG    . ASP B 1 145 ? 9.744   -36.720 72.320 1.00 18.91 ?  145 ASP B CG    1 
ATOM   4187 O OD1   . ASP B 1 145 ? 8.711   -37.328 72.661 1.00 12.96 ?  145 ASP B OD1   1 
ATOM   4188 O OD2   . ASP B 1 145 ? 10.900  -37.142 72.531 1.00 28.72 -1 145 ASP B OD2   1 
ATOM   4189 N N     . PHE B 1 146 ? 5.944   -35.148 71.503 1.00 24.50 ?  146 PHE B N     1 
ATOM   4190 C CA    . PHE B 1 146 ? 4.802   -34.646 72.261 1.00 26.28 ?  146 PHE B CA    1 
ATOM   4191 C C     . PHE B 1 146 ? 4.771   -35.179 73.689 1.00 24.01 ?  146 PHE B C     1 
ATOM   4192 O O     . PHE B 1 146 ? 4.293   -34.483 74.586 1.00 40.53 ?  146 PHE B O     1 
ATOM   4193 C CB    . PHE B 1 146 ? 3.496   -34.981 71.536 1.00 9.18  ?  146 PHE B CB    1 
ATOM   4194 C CG    . PHE B 1 146 ? 3.262   -34.165 70.293 1.00 9.19  ?  146 PHE B CG    1 
ATOM   4195 C CD1   . PHE B 1 146 ? 2.857   -32.843 70.377 1.00 9.00  ?  146 PHE B CD1   1 
ATOM   4196 C CD2   . PHE B 1 146 ? 3.425   -34.721 69.041 1.00 9.41  ?  146 PHE B CD2   1 
ATOM   4197 C CE1   . PHE B 1 146 ? 2.646   -32.095 69.234 1.00 9.03  ?  146 PHE B CE1   1 
ATOM   4198 C CE2   . PHE B 1 146 ? 3.208   -33.971 67.890 1.00 9.44  ?  146 PHE B CE2   1 
ATOM   4199 C CZ    . PHE B 1 146 ? 2.815   -32.658 67.995 1.00 9.26  ?  146 PHE B CZ    1 
ATOM   4200 N N     . LYS B 1 147 ? 5.271   -36.388 73.944 1.00 15.16 ?  147 LYS B N     1 
ATOM   4201 C CA    . LYS B 1 147 ? 5.276   -36.855 75.328 1.00 27.29 ?  147 LYS B CA    1 
ATOM   4202 C C     . LYS B 1 147 ? 6.251   -36.045 76.160 1.00 40.37 ?  147 LYS B C     1 
ATOM   4203 O O     . LYS B 1 147 ? 5.935   -35.609 77.274 1.00 50.06 ?  147 LYS B O     1 
ATOM   4204 C CB    . LYS B 1 147 ? 5.614   -38.340 75.404 1.00 23.19 ?  147 LYS B CB    1 
ATOM   4205 C CG    . LYS B 1 147 ? 5.625   -38.860 76.836 1.00 21.61 ?  147 LYS B CG    1 
ATOM   4206 C CD    . LYS B 1 147 ? 6.287   -40.240 76.942 1.00 20.50 ?  147 LYS B CD    1 
ATOM   4207 C CE    . LYS B 1 147 ? 6.821   -40.517 78.341 1.00 11.07 ?  147 LYS B CE    1 
ATOM   4208 N NZ    . LYS B 1 147 ? 5.853   -40.248 79.440 1.00 17.43 1  147 LYS B NZ    1 
ATOM   4209 N N     . HIS B 1 148 ? 7.448   -35.843 75.623 1.00 45.48 ?  148 HIS B N     1 
ATOM   4210 C CA    . HIS B 1 148 ? 8.448   -35.015 76.277 1.00 28.98 ?  148 HIS B CA    1 
ATOM   4211 C C     . HIS B 1 148 ? 8.031   -33.549 76.306 1.00 19.45 ?  148 HIS B C     1 
ATOM   4212 O O     . HIS B 1 148 ? 8.189   -32.867 77.327 1.00 17.88 ?  148 HIS B O     1 
ATOM   4213 C CB    . HIS B 1 148 ? 9.780   -35.198 75.557 1.00 36.06 ?  148 HIS B CB    1 
ATOM   4214 C CG    . HIS B 1 148 ? 10.898  -34.427 76.165 1.00 28.44 ?  148 HIS B CG    1 
ATOM   4215 N ND1   . HIS B 1 148 ? 11.217  -33.156 75.763 1.00 20.88 ?  148 HIS B ND1   1 
ATOM   4216 C CD2   . HIS B 1 148 ? 11.752  -34.736 77.166 1.00 25.47 ?  148 HIS B CD2   1 
ATOM   4217 C CE1   . HIS B 1 148 ? 12.234  -32.717 76.477 1.00 32.87 ?  148 HIS B CE1   1 
ATOM   4218 N NE2   . HIS B 1 148 ? 12.576  -33.656 77.338 1.00 30.66 ?  148 HIS B NE2   1 
ATOM   4219 N N     . LEU B 1 149 ? 7.441   -33.053 75.223 1.00 22.29 ?  149 LEU B N     1 
ATOM   4220 C CA    . LEU B 1 149 ? 7.020   -31.660 75.238 1.00 21.28 ?  149 LEU B CA    1 
ATOM   4221 C C     . LEU B 1 149 ? 6.061   -31.408 76.390 1.00 26.34 ?  149 LEU B C     1 
ATOM   4222 O O     . LEU B 1 149 ? 6.242   -30.466 77.166 1.00 44.87 ?  149 LEU B O     1 
ATOM   4223 C CB    . LEU B 1 149 ? 6.368   -31.282 73.913 1.00 13.21 ?  149 LEU B CB    1 
ATOM   4224 C CG    . LEU B 1 149 ? 5.908   -29.832 73.979 1.00 15.10 ?  149 LEU B CG    1 
ATOM   4225 C CD1   . LEU B 1 149 ? 7.083   -28.935 74.279 1.00 24.38 ?  149 LEU B CD1   1 
ATOM   4226 C CD2   . LEU B 1 149 ? 5.303   -29.468 72.658 1.00 28.17 ?  149 LEU B CD2   1 
ATOM   4227 N N     . GLU B 1 150 ? 5.067   -32.276 76.555 1.00 7.81  ?  150 GLU B N     1 
ATOM   4228 C CA    . GLU B 1 150 ? 4.170   -32.138 77.691 1.00 7.92  ?  150 GLU B CA    1 
ATOM   4229 C C     . GLU B 1 150 ? 4.877   -32.429 79.004 1.00 23.22 ?  150 GLU B C     1 
ATOM   4230 O O     . GLU B 1 150 ? 4.434   -31.946 80.052 1.00 27.59 ?  150 GLU B O     1 
ATOM   4231 C CB    . GLU B 1 150 ? 2.968   -33.054 77.526 1.00 29.79 ?  150 GLU B CB    1 
ATOM   4232 C CG    . GLU B 1 150 ? 2.034   -33.048 78.717 1.00 38.18 ?  150 GLU B CG    1 
ATOM   4233 C CD    . GLU B 1 150 ? 0.854   -33.957 78.525 1.00 33.60 ?  150 GLU B CD    1 
ATOM   4234 O OE1   . GLU B 1 150 ? -0.281  -33.460 78.581 1.00 18.81 ?  150 GLU B OE1   1 
ATOM   4235 O OE2   . GLU B 1 150 ? 1.065   -35.167 78.316 1.00 32.87 -1 150 GLU B OE2   1 
ATOM   4236 N N     . LYS B 1 151 ? 5.958   -33.181 78.958 1.00 27.48 ?  151 LYS B N     1 
ATOM   4237 C CA    . LYS B 1 151 ? 6.737   -33.392 80.199 1.00 30.08 ?  151 LYS B CA    1 
ATOM   4238 C C     . LYS B 1 151 ? 7.392   -32.069 80.600 1.00 7.62  ?  151 LYS B C     1 
ATOM   4239 O O     . LYS B 1 151 ? 7.485   -31.840 81.725 1.00 6.99  ?  151 LYS B O     1 
ATOM   4240 C CB    . LYS B 1 151 ? 7.628   -34.637 80.091 1.00 42.45 ?  151 LYS B CB    1 
ATOM   4241 C CG    . LYS B 1 151 ? 6.948   -35.996 80.058 1.00 41.41 ?  151 LYS B CG    1 
ATOM   4242 C CD    . LYS B 1 151 ? 7.948   -37.107 79.803 1.00 38.32 ?  151 LYS B CD    1 
ATOM   4243 C CE    . LYS B 1 151 ? 8.972   -37.294 80.903 1.00 28.49 ?  151 LYS B CE    1 
ATOM   4244 N NZ    . LYS B 1 151 ? 9.845   -38.465 80.656 1.00 13.61 1  151 LYS B NZ    1 
ATOM   4245 N N     . GLN B 1 152 ? 7.701   -31.181 79.677 1.00 11.07 ?  152 GLN B N     1 
ATOM   4246 C CA    . GLN B 1 152 ? 8.210   -29.862 80.069 1.00 21.42 ?  152 GLN B CA    1 
ATOM   4247 C C     . GLN B 1 152 ? 7.108   -28.952 80.598 1.00 18.66 ?  152 GLN B C     1 
ATOM   4248 O O     . GLN B 1 152 ? 7.347   -28.198 81.545 1.00 17.45 ?  152 GLN B O     1 
ATOM   4249 C CB    . GLN B 1 152 ? 8.879   -29.137 78.901 1.00 6.29  ?  152 GLN B CB    1 
ATOM   4250 C CG    . GLN B 1 152 ? 10.049  -29.821 78.273 1.00 8.32  ?  152 GLN B CG    1 
ATOM   4251 C CD    . GLN B 1 152 ? 11.189  -29.870 79.210 1.00 20.70 ?  152 GLN B CD    1 
ATOM   4252 O OE1   . GLN B 1 152 ? 12.066  -28.998 79.208 1.00 31.56 ?  152 GLN B OE1   1 
ATOM   4253 N NE2   . GLN B 1 152 ? 11.164  -30.867 80.086 1.00 6.23  ?  152 GLN B NE2   1 
ATOM   4254 N N     . PHE B 1 153 ? 5.902   -29.003 80.002 1.00 19.75 ?  153 PHE B N     1 
ATOM   4255 C CA    . PHE B 1 153 ? 4.787   -28.151 80.451 1.00 16.87 ?  153 PHE B CA    1 
ATOM   4256 C C     . PHE B 1 153 ? 4.332   -28.501 81.856 1.00 18.41 ?  153 PHE B C     1 
ATOM   4257 O O     . PHE B 1 153 ? 3.687   -27.680 82.512 1.00 22.75 ?  153 PHE B O     1 
ATOM   4258 C CB    . PHE B 1 153 ? 3.582   -28.232 79.518 1.00 7.12  ?  153 PHE B CB    1 
ATOM   4259 C CG    . PHE B 1 153 ? 3.810   -27.627 78.159 1.00 7.02  ?  153 PHE B CG    1 
ATOM   4260 C CD1   . PHE B 1 153 ? 5.007   -27.071 77.829 1.00 6.66  ?  153 PHE B CD1   1 
ATOM   4261 C CD2   . PHE B 1 153 ? 2.824   -27.657 77.196 1.00 33.62 ?  153 PHE B CD2   1 
ATOM   4262 C CE1   . PHE B 1 153 ? 5.220   -26.554 76.589 1.00 6.58  ?  153 PHE B CE1   1 
ATOM   4263 C CE2   . PHE B 1 153 ? 3.050   -27.116 75.937 1.00 22.48 ?  153 PHE B CE2   1 
ATOM   4264 C CZ    . PHE B 1 153 ? 4.245   -26.578 75.647 1.00 6.86  ?  153 PHE B CZ    1 
ATOM   4265 N N     . GLN B 1 154 ? 4.553   -29.746 82.289 1.00 25.22 ?  154 GLN B N     1 
ATOM   4266 C CA    . GLN B 1 154 ? 4.187   -30.134 83.646 1.00 25.92 ?  154 GLN B CA    1 
ATOM   4267 C C     . GLN B 1 154 ? 5.073   -29.474 84.692 1.00 25.16 ?  154 GLN B C     1 
ATOM   4268 O O     . GLN B 1 154 ? 4.759   -29.545 85.885 1.00 23.12 ?  154 GLN B O     1 
ATOM   4269 C CB    . GLN B 1 154 ? 4.207   -31.667 83.786 1.00 19.96 ?  154 GLN B CB    1 
ATOM   4270 C CG    . GLN B 1 154 ? 2.938   -32.307 83.203 1.00 20.89 ?  154 GLN B CG    1 
ATOM   4271 C CD    . GLN B 1 154 ? 2.818   -33.815 83.385 1.00 28.61 ?  154 GLN B CD    1 
ATOM   4272 O OE1   . GLN B 1 154 ? 3.805   -34.538 83.488 1.00 33.55 ?  154 GLN B OE1   1 
ATOM   4273 N NE2   . GLN B 1 154 ? 1.583   -34.291 83.413 1.00 26.96 ?  154 GLN B NE2   1 
ATOM   4274 N N     . GLN B 1 155 ? 6.145   -28.809 84.272 1.00 41.77 ?  155 GLN B N     1 
ATOM   4275 C CA    . GLN B 1 155 ? 7.054   -28.097 85.160 1.00 25.64 ?  155 GLN B CA    1 
ATOM   4276 C C     . GLN B 1 155 ? 6.717   -26.616 85.289 1.00 37.21 ?  155 GLN B C     1 
ATOM   4277 O O     . GLN B 1 155 ? 7.415   -25.896 86.009 1.00 44.97 ?  155 GLN B O     1 
ATOM   4278 C CB    . GLN B 1 155 ? 8.489   -28.241 84.649 1.00 20.80 ?  155 GLN B CB    1 
ATOM   4279 C CG    . GLN B 1 155 ? 9.086   -29.635 84.742 1.00 21.93 ?  155 GLN B CG    1 
ATOM   4280 C CD    . GLN B 1 155 ? 10.361  -29.762 83.916 1.00 35.02 ?  155 GLN B CD    1 
ATOM   4281 O OE1   . GLN B 1 155 ? 10.628  -28.934 83.042 1.00 57.54 ?  155 GLN B OE1   1 
ATOM   4282 N NE2   . GLN B 1 155 ? 11.187  -30.749 84.240 1.00 17.98 ?  155 GLN B NE2   1 
ATOM   4283 N N     . GLY B 1 156 ? 5.813   -26.074 84.498 1.00 35.82 ?  156 GLY B N     1 
ATOM   4284 C CA    . GLY B 1 156 ? 5.511   -24.657 84.740 1.00 32.41 ?  156 GLY B CA    1 
ATOM   4285 C C     . GLY B 1 156 ? 5.780   -23.801 83.556 1.00 27.24 ?  156 GLY B C     1 
ATOM   4286 O O     . GLY B 1 156 ? 6.113   -22.648 83.728 1.00 23.99 ?  156 GLY B O     1 
ATOM   4287 N N     . ILE B 1 157 ? 5.707   -24.371 82.389 1.00 20.82 ?  157 ILE B N     1 
ATOM   4288 C CA    . ILE B 1 157 ? 6.066   -23.527 81.258 1.00 28.67 ?  157 ILE B CA    1 
ATOM   4289 C C     . ILE B 1 157 ? 4.980   -22.490 81.017 1.00 39.60 ?  157 ILE B C     1 
ATOM   4290 O O     . ILE B 1 157 ? 3.803   -22.830 80.839 1.00 54.39 ?  157 ILE B O     1 
ATOM   4291 C CB    . ILE B 1 157 ? 6.298   -24.373 80.001 1.00 31.47 ?  157 ILE B CB    1 
ATOM   4292 C CG1   . ILE B 1 157 ? 7.455   -25.340 80.221 1.00 39.82 ?  157 ILE B CG1   1 
ATOM   4293 C CG2   . ILE B 1 157 ? 6.576   -23.479 78.812 1.00 36.19 ?  157 ILE B CG2   1 
ATOM   4294 C CD1   . ILE B 1 157 ? 8.760   -24.666 80.343 1.00 47.01 ?  157 ILE B CD1   1 
ATOM   4295 N N     . LYS B 1 158 ? 5.381   -21.216 80.987 1.00 42.96 ?  158 LYS B N     1 
ATOM   4296 C CA    . LYS B 1 158 ? 4.478   -20.092 80.767 1.00 33.03 ?  158 LYS B CA    1 
ATOM   4297 C C     . LYS B 1 158 ? 4.414   -19.631 79.320 1.00 26.65 ?  158 LYS B C     1 
ATOM   4298 O O     . LYS B 1 158 ? 3.327   -19.283 78.853 1.00 25.81 ?  158 LYS B O     1 
ATOM   4299 C CB    . LYS B 1 158 ? 4.883   -18.907 81.652 1.00 26.58 ?  158 LYS B CB    1 
ATOM   4300 C CG    . LYS B 1 158 ? 4.289   -18.984 83.058 1.00 35.34 ?  158 LYS B CG    1 
ATOM   4301 C CD    . LYS B 1 158 ? 2.872   -18.381 83.093 1.00 37.23 ?  158 LYS B CD    1 
ATOM   4302 C CE    . LYS B 1 158 ? 2.163   -18.575 84.444 1.00 37.82 ?  158 LYS B CE    1 
ATOM   4303 N NZ    . LYS B 1 158 ? 0.988   -17.635 84.647 1.00 27.64 1  158 LYS B NZ    1 
ATOM   4304 N N     . LEU B 1 159 ? 5.499   -19.590 78.589 1.00 26.64 ?  159 LEU B N     1 
ATOM   4305 C CA    . LEU B 1 159 ? 5.583   -19.201 77.164 1.00 33.38 ?  159 LEU B CA    1 
ATOM   4306 C C     . LEU B 1 159 ? 6.324   -20.233 76.319 1.00 34.43 ?  159 LEU B C     1 
ATOM   4307 O O     . LEU B 1 159 ? 7.231   -20.888 76.796 1.00 5.16  ?  159 LEU B O     1 
ATOM   4308 C CB    . LEU B 1 159 ? 6.232   -17.818 76.987 1.00 36.29 ?  159 LEU B CB    1 
ATOM   4309 C CG    . LEU B 1 159 ? 6.095   -17.148 75.623 1.00 30.13 ?  159 LEU B CG    1 
ATOM   4310 C CD1   . LEU B 1 159 ? 4.954   -16.159 75.628 1.00 20.82 ?  159 LEU B CD1   1 
ATOM   4311 C CD2   . LEU B 1 159 ? 7.385   -16.448 75.234 1.00 16.28 ?  159 LEU B CD2   1 
ATOM   4312 N N     . MET B 1 160 ? 5.884   -20.301 75.084 1.00 31.71 ?  160 MET B N     1 
ATOM   4313 C CA    . MET B 1 160 ? 6.467   -21.163 74.071 1.00 21.62 ?  160 MET B CA    1 
ATOM   4314 C C     . MET B 1 160 ? 6.748   -20.345 72.821 1.00 15.20 ?  160 MET B C     1 
ATOM   4315 O O     . MET B 1 160 ? 5.908   -19.548 72.388 1.00 21.66 ?  160 MET B O     1 
ATOM   4316 C CB    . MET B 1 160 ? 5.530   -22.333 73.721 1.00 12.43 ?  160 MET B CB    1 
ATOM   4317 C CG    . MET B 1 160 ? 5.877   -22.955 72.392 1.00 14.03 ?  160 MET B CG    1 
ATOM   4318 S SD    . MET B 1 160 ? 5.020   -24.467 71.988 1.00 40.91 ?  160 MET B SD    1 
ATOM   4319 C CE    . MET B 1 160 ? 5.621   -24.756 70.324 1.00 34.99 ?  160 MET B CE    1 
ATOM   4320 N N     . LEU B 1 161 ? 7.919   -20.538 72.260 1.00 5.22  ?  161 LEU B N     1 
ATOM   4321 C CA    . LEU B 1 161 ? 8.212   -19.833 71.023 1.00 14.59 ?  161 LEU B CA    1 
ATOM   4322 C C     . LEU B 1 161 ? 8.132   -20.818 69.881 1.00 13.10 ?  161 LEU B C     1 
ATOM   4323 O O     . LEU B 1 161 ? 9.076   -21.528 69.728 1.00 23.30 ?  161 LEU B O     1 
ATOM   4324 C CB    . LEU B 1 161 ? 9.619   -19.247 71.125 1.00 19.03 ?  161 LEU B CB    1 
ATOM   4325 C CG    . LEU B 1 161 ? 9.774   -17.923 71.854 1.00 25.84 ?  161 LEU B CG    1 
ATOM   4326 C CD1   . LEU B 1 161 ? 11.242  -17.694 72.159 1.00 4.27  ?  161 LEU B CD1   1 
ATOM   4327 C CD2   . LEU B 1 161 ? 9.213   -16.789 71.016 1.00 4.47  ?  161 LEU B CD2   1 
ATOM   4328 N N     . LEU B 1 162 ? 7.130   -20.717 69.044 1.00 7.57  ?  162 LEU B N     1 
ATOM   4329 C CA    . LEU B 1 162 ? 6.916   -21.596 67.913 1.00 14.04 ?  162 LEU B CA    1 
ATOM   4330 C C     . LEU B 1 162 ? 7.463   -20.974 66.641 1.00 14.06 ?  162 LEU B C     1 
ATOM   4331 O O     . LEU B 1 162 ? 7.257   -19.789 66.365 1.00 22.38 ?  162 LEU B O     1 
ATOM   4332 C CB    . LEU B 1 162 ? 5.431   -21.903 67.731 1.00 7.56  ?  162 LEU B CB    1 
ATOM   4333 C CG    . LEU B 1 162 ? 5.158   -22.629 66.427 1.00 7.98  ?  162 LEU B CG    1 
ATOM   4334 C CD1   . LEU B 1 162 ? 5.220   -24.115 66.714 1.00 7.02  ?  162 LEU B CD1   1 
ATOM   4335 C CD2   . LEU B 1 162 ? 3.816   -22.186 65.860 1.00 24.77 ?  162 LEU B CD2   1 
ATOM   4336 N N     . CYS B 1 163 ? 8.138   -21.793 65.859 1.00 23.04 ?  163 CYS B N     1 
ATOM   4337 C CA    . CYS B 1 163 ? 8.589   -21.422 64.531 1.00 23.56 ?  163 CYS B CA    1 
ATOM   4338 C C     . CYS B 1 163 ? 7.777   -22.234 63.535 1.00 22.97 ?  163 CYS B C     1 
ATOM   4339 O O     . CYS B 1 163 ? 7.842   -23.468 63.533 1.00 13.20 ?  163 CYS B O     1 
ATOM   4340 C CB    . CYS B 1 163 ? 10.092  -21.662 64.377 1.00 10.42 ?  163 CYS B CB    1 
ATOM   4341 S SG    . CYS B 1 163 ? 10.769  -20.912 62.904 1.00 25.24 ?  163 CYS B SG    1 
ATOM   4342 N N     . SER B 1 164 ? 7.006   -21.549 62.708 1.00 18.85 ?  164 SER B N     1 
ATOM   4343 C CA    . SER B 1 164 ? 6.228   -22.274 61.723 1.00 10.88 ?  164 SER B CA    1 
ATOM   4344 C C     . SER B 1 164 ? 6.082   -21.454 60.450 1.00 13.77 ?  164 SER B C     1 
ATOM   4345 O O     . SER B 1 164 ? 5.295   -20.516 60.421 1.00 27.95 ?  164 SER B O     1 
ATOM   4346 C CB    . SER B 1 164 ? 4.855   -22.635 62.267 1.00 7.64  ?  164 SER B CB    1 
ATOM   4347 O OG    . SER B 1 164 ? 4.375   -23.698 61.482 1.00 11.45 ?  164 SER B OG    1 
ATOM   4348 N N     . PRO B 1 165 ? 6.754   -21.797 59.370 1.00 7.93  ?  165 PRO B N     1 
ATOM   4349 C CA    . PRO B 1 165 ? 7.646   -22.940 59.187 1.00 17.71 ?  165 PRO B CA    1 
ATOM   4350 C C     . PRO B 1 165 ? 8.910   -22.882 60.044 1.00 40.74 ?  165 PRO B C     1 
ATOM   4351 O O     . PRO B 1 165 ? 9.284   -21.802 60.503 1.00 54.00 ?  165 PRO B O     1 
ATOM   4352 C CB    . PRO B 1 165 ? 8.004   -22.842 57.702 1.00 16.16 ?  165 PRO B CB    1 
ATOM   4353 C CG    . PRO B 1 165 ? 6.843   -22.106 57.085 1.00 25.10 ?  165 PRO B CG    1 
ATOM   4354 C CD    . PRO B 1 165 ? 6.424   -21.119 58.103 1.00 8.56  ?  165 PRO B CD    1 
ATOM   4355 N N     . HIS B 1 166 ? 9.563   -24.034 60.264 1.00 34.36 ?  166 HIS B N     1 
ATOM   4356 C CA    . HIS B 1 166 ? 10.616  -24.158 61.268 1.00 14.42 ?  166 HIS B CA    1 
ATOM   4357 C C     . HIS B 1 166 ? 11.988  -24.063 60.601 1.00 15.53 ?  166 HIS B C     1 
ATOM   4358 O O     . HIS B 1 166 ? 12.421  -25.005 59.929 1.00 23.33 ?  166 HIS B O     1 
ATOM   4359 C CB    . HIS B 1 166 ? 10.462  -25.473 62.030 1.00 19.66 ?  166 HIS B CB    1 
ATOM   4360 C CG    . HIS B 1 166 ? 11.455  -25.645 63.140 1.00 22.57 ?  166 HIS B CG    1 
ATOM   4361 N ND1   . HIS B 1 166 ? 11.108  -25.534 64.474 1.00 18.78 ?  166 HIS B ND1   1 
ATOM   4362 C CD2   . HIS B 1 166 ? 12.790  -25.887 63.114 1.00 6.00  ?  166 HIS B CD2   1 
ATOM   4363 C CE1   . HIS B 1 166 ? 12.186  -25.709 65.221 1.00 9.74  ?  166 HIS B CE1   1 
ATOM   4364 N NE2   . HIS B 1 166 ? 13.217  -25.927 64.419 1.00 14.43 ?  166 HIS B NE2   1 
ATOM   4365 N N     . ASN B 1 167 ? 12.683  -22.923 60.802 1.00 14.09 ?  167 ASN B N     1 
ATOM   4366 C CA    . ASN B 1 167 ? 14.106  -22.787 60.455 1.00 7.86  ?  167 ASN B CA    1 
ATOM   4367 C C     . ASN B 1 167 ? 14.926  -23.442 61.551 1.00 5.43  ?  167 ASN B C     1 
ATOM   4368 O O     . ASN B 1 167 ? 14.660  -23.203 62.734 1.00 17.88 ?  167 ASN B O     1 
ATOM   4369 C CB    . ASN B 1 167 ? 14.513  -21.297 60.313 1.00 21.22 ?  167 ASN B CB    1 
ATOM   4370 C CG    . ASN B 1 167 ? 16.057  -21.045 60.385 1.00 18.81 ?  167 ASN B CG    1 
ATOM   4371 O OD1   . ASN B 1 167 ? 16.846  -21.517 59.561 1.00 19.93 ?  167 ASN B OD1   1 
ATOM   4372 N ND2   . ASN B 1 167 ? 16.463  -20.272 61.379 1.00 27.48 ?  167 ASN B ND2   1 
ATOM   4373 N N     . PRO B 1 168 ? 15.902  -24.295 61.215 1.00 5.53  ?  168 PRO B N     1 
ATOM   4374 C CA    . PRO B 1 168 ? 16.484  -24.577 59.898 1.00 15.10 ?  168 PRO B CA    1 
ATOM   4375 C C     . PRO B 1 168 ? 16.004  -25.850 59.188 1.00 22.71 ?  168 PRO B C     1 
ATOM   4376 O O     . PRO B 1 168 ? 16.297  -26.027 58.002 1.00 13.61 ?  168 PRO B O     1 
ATOM   4377 C CB    . PRO B 1 168 ? 17.962  -24.674 60.226 1.00 5.70  ?  168 PRO B CB    1 
ATOM   4378 C CG    . PRO B 1 168 ? 17.984  -25.212 61.625 1.00 9.01  ?  168 PRO B CG    1 
ATOM   4379 C CD    . PRO B 1 168 ? 16.676  -24.932 62.288 1.00 5.38  ?  168 PRO B CD    1 
ATOM   4380 N N     . ILE B 1 169 ? 15.226  -26.691 59.875 1.00 36.50 ?  169 ILE B N     1 
ATOM   4381 C CA    . ILE B 1 169 ? 14.929  -28.017 59.335 1.00 29.45 ?  169 ILE B CA    1 
ATOM   4382 C C     . ILE B 1 169 ? 13.950  -27.927 58.178 1.00 19.01 ?  169 ILE B C     1 
ATOM   4383 O O     . ILE B 1 169 ? 13.951  -28.787 57.295 1.00 11.74 ?  169 ILE B O     1 
ATOM   4384 C CB    . ILE B 1 169 ? 14.414  -28.951 60.448 1.00 6.75  ?  169 ILE B CB    1 
ATOM   4385 C CG1   . ILE B 1 169 ? 12.940  -28.722 60.720 1.00 14.70 ?  169 ILE B CG1   1 
ATOM   4386 C CG2   . ILE B 1 169 ? 15.229  -28.771 61.742 1.00 6.20  ?  169 ILE B CG2   1 
ATOM   4387 C CD1   . ILE B 1 169 ? 12.458  -29.347 62.023 1.00 20.99 ?  169 ILE B CD1   1 
ATOM   4388 N N     . GLY B 1 170 ? 13.122  -26.891 58.136 1.00 23.86 ?  170 GLY B N     1 
ATOM   4389 C CA    . GLY B 1 170 ? 12.175  -26.747 57.049 1.00 17.97 ?  170 GLY B CA    1 
ATOM   4390 C C     . GLY B 1 170 ? 10.838  -27.432 57.241 1.00 12.53 ?  170 GLY B C     1 
ATOM   4391 O O     . GLY B 1 170 ? 10.219  -27.813 56.246 1.00 16.04 ?  170 GLY B O     1 
ATOM   4392 N N     . ARG B 1 171 ? 10.428  -27.702 58.474 1.00 8.39  ?  171 ARG B N     1 
ATOM   4393 C CA    . ARG B 1 171 ? 9.149   -28.348 58.726 1.00 14.76 ?  171 ARG B CA    1 
ATOM   4394 C C     . ARG B 1 171 ? 7.999   -27.355 58.602 1.00 20.57 ?  171 ARG B C     1 
ATOM   4395 O O     . ARG B 1 171 ? 8.045   -26.271 59.189 1.00 31.03 ?  171 ARG B O     1 
ATOM   4396 C CB    . ARG B 1 171 ? 9.132   -28.979 60.111 1.00 20.95 ?  171 ARG B CB    1 
ATOM   4397 C CG    . ARG B 1 171 ? 9.634   -30.403 60.149 1.00 32.02 ?  171 ARG B CG    1 
ATOM   4398 C CD    . ARG B 1 171 ? 9.031   -31.308 59.070 1.00 26.31 ?  171 ARG B CD    1 
ATOM   4399 N NE    . ARG B 1 171 ? 7.590   -31.190 58.874 1.00 14.15 ?  171 ARG B NE    1 
ATOM   4400 C CZ    . ARG B 1 171 ? 6.677   -31.533 59.772 1.00 11.70 ?  171 ARG B CZ    1 
ATOM   4401 N NH1   . ARG B 1 171 ? 7.044   -31.995 60.957 1.00 13.76 1  171 ARG B NH1   1 
ATOM   4402 N NH2   . ARG B 1 171 ? 5.395   -31.418 59.482 1.00 12.10 ?  171 ARG B NH2   1 
ATOM   4403 N N     . VAL B 1 172 ? 6.978   -27.728 57.834 1.00 15.03 ?  172 VAL B N     1 
ATOM   4404 C CA    . VAL B 1 172 ? 5.703   -27.020 57.787 1.00 20.36 ?  172 VAL B CA    1 
ATOM   4405 C C     . VAL B 1 172 ? 4.697   -27.903 58.506 1.00 20.85 ?  172 VAL B C     1 
ATOM   4406 O O     . VAL B 1 172 ? 4.135   -28.826 57.912 1.00 17.46 ?  172 VAL B O     1 
ATOM   4407 C CB    . VAL B 1 172 ? 5.239   -26.737 56.354 1.00 28.28 ?  172 VAL B CB    1 
ATOM   4408 C CG1   . VAL B 1 172 ? 3.856   -26.103 56.378 1.00 20.79 ?  172 VAL B CG1   1 
ATOM   4409 C CG2   . VAL B 1 172 ? 6.247   -25.866 55.591 1.00 28.99 ?  172 VAL B CG2   1 
ATOM   4410 N N     . TRP B 1 173 ? 4.401   -27.564 59.751 1.00 20.03 ?  173 TRP B N     1 
ATOM   4411 C CA    . TRP B 1 173 ? 3.594   -28.423 60.600 1.00 15.04 ?  173 TRP B CA    1 
ATOM   4412 C C     . TRP B 1 173 ? 2.187   -28.627 60.041 1.00 30.54 ?  173 TRP B C     1 
ATOM   4413 O O     . TRP B 1 173 ? 1.567   -27.702 59.505 1.00 35.76 ?  173 TRP B O     1 
ATOM   4414 C CB    . TRP B 1 173 ? 3.520   -27.810 61.994 1.00 23.36 ?  173 TRP B CB    1 
ATOM   4415 C CG    . TRP B 1 173 ? 4.858   -27.490 62.552 1.00 26.89 ?  173 TRP B CG    1 
ATOM   4416 C CD1   . TRP B 1 173 ? 5.401   -26.252 62.744 1.00 26.80 ?  173 TRP B CD1   1 
ATOM   4417 C CD2   . TRP B 1 173 ? 5.835   -28.427 63.003 1.00 30.10 ?  173 TRP B CD2   1 
ATOM   4418 N NE1   . TRP B 1 173 ? 6.661   -26.363 63.283 1.00 18.17 ?  173 TRP B NE1   1 
ATOM   4419 C CE2   . TRP B 1 173 ? 6.948   -27.690 63.453 1.00 28.81 ?  173 TRP B CE2   1 
ATOM   4420 C CE3   . TRP B 1 173 ? 5.882   -29.822 63.067 1.00 21.68 ?  173 TRP B CE3   1 
ATOM   4421 C CZ2   . TRP B 1 173 ? 8.078   -28.303 63.957 1.00 38.55 ?  173 TRP B CZ2   1 
ATOM   4422 C CZ3   . TRP B 1 173 ? 6.993   -30.418 63.565 1.00 8.45  ?  173 TRP B CZ3   1 
ATOM   4423 C CH2   . TRP B 1 173 ? 8.080   -29.670 64.002 1.00 25.63 ?  173 TRP B CH2   1 
ATOM   4424 N N     . THR B 1 174 ? 1.689   -29.858 60.161 1.00 30.53 ?  174 THR B N     1 
ATOM   4425 C CA    . THR B 1 174 ? 0.320   -30.160 59.772 1.00 26.72 ?  174 THR B CA    1 
ATOM   4426 C C     . THR B 1 174 ? -0.677  -29.551 60.752 1.00 17.08 ?  174 THR B C     1 
ATOM   4427 O O     . THR B 1 174 ? -0.348  -29.180 61.880 1.00 15.88 ?  174 THR B O     1 
ATOM   4428 C CB    . THR B 1 174 ? 0.053   -31.675 59.752 1.00 21.76 ?  174 THR B CB    1 
ATOM   4429 O OG1   . THR B 1 174 ? 0.333   -32.226 61.049 1.00 11.30 ?  174 THR B OG1   1 
ATOM   4430 C CG2   . THR B 1 174 ? 0.822   -32.381 58.672 1.00 11.84 ?  174 THR B CG2   1 
ATOM   4431 N N     . LYS B 1 175 ? -1.942  -29.588 60.341 1.00 15.93 ?  175 LYS B N     1 
ATOM   4432 C CA    . LYS B 1 175 ? -3.023  -29.221 61.238 1.00 15.49 ?  175 LYS B CA    1 
ATOM   4433 C C     . LYS B 1 175 ? -3.119  -30.203 62.400 1.00 17.19 ?  175 LYS B C     1 
ATOM   4434 O O     . LYS B 1 175 ? -3.398  -29.806 63.534 1.00 25.10 ?  175 LYS B O     1 
ATOM   4435 C CB    . LYS B 1 175 ? -4.343  -29.170 60.451 1.00 22.96 ?  175 LYS B CB    1 
ATOM   4436 C CG    . LYS B 1 175 ? -5.617  -29.124 61.298 1.00 30.65 ?  175 LYS B CG    1 
ATOM   4437 C CD    . LYS B 1 175 ? -6.875  -29.378 60.444 1.00 46.14 ?  175 LYS B CD    1 
ATOM   4438 C CE    . LYS B 1 175 ? -8.174  -29.144 61.232 1.00 39.75 ?  175 LYS B CE    1 
ATOM   4439 N NZ    . LYS B 1 175 ? -8.481  -30.212 62.219 1.00 31.17 1  175 LYS B NZ    1 
ATOM   4440 N N     . GLU B 1 176 ? -2.850  -31.486 62.159 1.00 20.28 ?  176 GLU B N     1 
ATOM   4441 C CA    . GLU B 1 176 ? -2.936  -32.441 63.259 1.00 22.90 ?  176 GLU B CA    1 
ATOM   4442 C C     . GLU B 1 176 ? -1.833  -32.198 64.284 1.00 30.77 ?  176 GLU B C     1 
ATOM   4443 O O     . GLU B 1 176 ? -2.087  -32.226 65.495 1.00 29.36 ?  176 GLU B O     1 
ATOM   4444 C CB    . GLU B 1 176 ? -2.882  -33.869 62.719 1.00 17.67 ?  176 GLU B CB    1 
ATOM   4445 C CG    . GLU B 1 176 ? -4.040  -34.231 61.789 1.00 27.16 ?  176 GLU B CG    1 
ATOM   4446 C CD    . GLU B 1 176 ? -3.821  -33.769 60.350 1.00 49.73 ?  176 GLU B CD    1 
ATOM   4447 O OE1   . GLU B 1 176 ? -2.940  -34.320 59.655 1.00 58.82 ?  176 GLU B OE1   1 
ATOM   4448 O OE2   . GLU B 1 176 ? -4.549  -32.859 59.902 1.00 61.98 -1 176 GLU B OE2   1 
ATOM   4449 N N     . GLU B 1 177 ? -0.619  -31.878 63.818 1.00 30.07 ?  177 GLU B N     1 
ATOM   4450 C CA    . GLU B 1 177 ? 0.470   -31.573 64.738 1.00 10.30 ?  177 GLU B CA    1 
ATOM   4451 C C     . GLU B 1 177 ? 0.126   -30.361 65.583 1.00 10.00 ?  177 GLU B C     1 
ATOM   4452 O O     . GLU B 1 177 ? 0.196   -30.401 66.816 1.00 9.77  ?  177 GLU B O     1 
ATOM   4453 C CB    . GLU B 1 177 ? 1.755   -31.326 63.953 1.00 33.75 ?  177 GLU B CB    1 
ATOM   4454 C CG    . GLU B 1 177 ? 2.520   -32.580 63.558 1.00 16.73 ?  177 GLU B CG    1 
ATOM   4455 C CD    . GLU B 1 177 ? 3.282   -32.403 62.259 1.00 10.02 ?  177 GLU B CD    1 
ATOM   4456 O OE1   . GLU B 1 177 ? 2.779   -31.756 61.319 1.00 10.27 ?  177 GLU B OE1   1 
ATOM   4457 O OE2   . GLU B 1 177 ? 4.406   -32.911 62.181 1.00 24.92 -1 177 GLU B OE2   1 
ATOM   4458 N N     . LEU B 1 178 ? -0.308  -29.286 64.936 1.00 10.04 ?  178 LEU B N     1 
ATOM   4459 C CA    . LEU B 1 178 ? -0.614  -28.072 65.678 1.00 14.64 ?  178 LEU B CA    1 
ATOM   4460 C C     . LEU B 1 178 ? -1.763  -28.281 66.651 1.00 13.51 ?  178 LEU B C     1 
ATOM   4461 O O     . LEU B 1 178 ? -1.684  -27.828 67.803 1.00 9.67  ?  178 LEU B O     1 
ATOM   4462 C CB    . LEU B 1 178 ? -0.949  -26.956 64.704 1.00 13.23 ?  178 LEU B CB    1 
ATOM   4463 C CG    . LEU B 1 178 ? 0.224   -26.799 63.756 1.00 17.54 ?  178 LEU B CG    1 
ATOM   4464 C CD1   . LEU B 1 178 ? -0.257  -26.164 62.487 1.00 19.96 ?  178 LEU B CD1   1 
ATOM   4465 C CD2   . LEU B 1 178 ? 1.335   -25.987 64.417 1.00 32.12 ?  178 LEU B CD2   1 
ATOM   4466 N N     . ILE B 1 179 ? -2.797  -29.037 66.241 1.00 11.46 ?  179 ILE B N     1 
ATOM   4467 C CA    . ILE B 1 179 ? -3.921  -29.315 67.132 1.00 10.88 ?  179 ILE B CA    1 
ATOM   4468 C C     . ILE B 1 179 ? -3.443  -30.043 68.381 1.00 10.65 ?  179 ILE B C     1 
ATOM   4469 O O     . ILE B 1 179 ? -3.723  -29.614 69.507 1.00 16.01 ?  179 ILE B O     1 
ATOM   4470 C CB    . ILE B 1 179 ? -5.031  -30.089 66.379 1.00 30.98 ?  179 ILE B CB    1 
ATOM   4471 C CG1   . ILE B 1 179 ? -5.844  -29.126 65.484 1.00 34.41 ?  179 ILE B CG1   1 
ATOM   4472 C CG2   . ILE B 1 179 ? -5.976  -30.904 67.315 1.00 11.94 ?  179 ILE B CG2   1 
ATOM   4473 C CD1   . ILE B 1 179 ? -6.644  -28.055 66.243 1.00 16.59 ?  179 ILE B CD1   1 
ATOM   4474 N N     . LYS B 1 180 ? -2.638  -31.102 68.209 1.00 15.18 ?  180 LYS B N     1 
ATOM   4475 C CA    . LYS B 1 180 ? -2.228  -31.890 69.372 1.00 10.49 ?  180 LYS B CA    1 
ATOM   4476 C C     . LYS B 1 180 ? -1.223  -31.141 70.235 1.00 9.87  ?  180 LYS B C     1 
ATOM   4477 O O     . LYS B 1 180 ? -1.145  -31.368 71.432 1.00 20.49 ?  180 LYS B O     1 
ATOM   4478 C CB    . LYS B 1 180 ? -1.721  -33.259 68.933 1.00 34.05 ?  180 LYS B CB    1 
ATOM   4479 C CG    . LYS B 1 180 ? -0.445  -33.308 68.103 1.00 40.06 ?  180 LYS B CG    1 
ATOM   4480 C CD    . LYS B 1 180 ? 0.011   -34.765 68.006 1.00 29.55 ?  180 LYS B CD    1 
ATOM   4481 C CE    . LYS B 1 180 ? -0.012  -35.240 66.583 1.00 21.03 ?  180 LYS B CE    1 
ATOM   4482 N NZ    . LYS B 1 180 ? 0.616   -36.554 66.412 1.00 30.44 1  180 LYS B NZ    1 
ATOM   4483 N N     . LEU B 1 181 ? -0.443  -30.265 69.637 1.00 24.68 ?  181 LEU B N     1 
ATOM   4484 C CA    . LEU B 1 181 ? 0.295   -29.251 70.403 1.00 28.33 ?  181 LEU B CA    1 
ATOM   4485 C C     . LEU B 1 181 ? -0.645  -28.143 70.904 1.00 17.66 ?  181 LEU B C     1 
ATOM   4486 O O     . LEU B 1 181 ? -0.529  -27.685 72.042 1.00 11.95 ?  181 LEU B O     1 
ATOM   4487 C CB    . LEU B 1 181 ? 1.434   -28.655 69.542 1.00 26.98 ?  181 LEU B CB    1 
ATOM   4488 C CG    . LEU B 1 181 ? 2.045   -27.319 69.974 1.00 11.49 ?  181 LEU B CG    1 
ATOM   4489 C CD1   . LEU B 1 181 ? 2.806   -27.404 71.300 1.00 7.76  ?  181 LEU B CD1   1 
ATOM   4490 C CD2   . LEU B 1 181 ? 2.942   -26.686 68.908 1.00 7.86  ?  181 LEU B CD2   1 
ATOM   4491 N N     . GLY B 1 182 ? -1.586  -27.702 70.072 1.00 9.26  ?  182 GLY B N     1 
ATOM   4492 C CA    . GLY B 1 182 ? -2.602  -26.787 70.570 1.00 24.01 ?  182 GLY B CA    1 
ATOM   4493 C C     . GLY B 1 182 ? -3.385  -27.372 71.736 1.00 32.90 ?  182 GLY B C     1 
ATOM   4494 O O     . GLY B 1 182 ? -3.778  -26.650 72.658 1.00 24.47 ?  182 GLY B O     1 
ATOM   4495 N N     . SER B 1 183 ? -3.636  -28.695 71.700 1.00 19.39 ?  183 SER B N     1 
ATOM   4496 C CA    . SER B 1 183 ? -4.344  -29.373 72.785 1.00 10.78 ?  183 SER B CA    1 
ATOM   4497 C C     . SER B 1 183 ? -3.549  -29.335 74.083 1.00 9.71  ?  183 SER B C     1 
ATOM   4498 O O     . SER B 1 183 ? -4.127  -29.301 75.174 1.00 9.76  ?  183 SER B O     1 
ATOM   4499 C CB    . SER B 1 183 ? -4.640  -30.830 72.388 1.00 17.71 ?  183 SER B CB    1 
ATOM   4500 O OG    . SER B 1 183 ? -5.743  -30.943 71.486 1.00 22.72 ?  183 SER B OG    1 
ATOM   4501 N N     . LEU B 1 184 ? -2.221  -29.323 73.987 1.00 10.91 ?  184 LEU B N     1 
ATOM   4502 C CA    . LEU B 1 184 ? -1.388  -29.208 75.181 1.00 22.54 ?  184 LEU B CA    1 
ATOM   4503 C C     . LEU B 1 184 ? -1.262  -27.761 75.648 1.00 11.94 ?  184 LEU B C     1 
ATOM   4504 O O     . LEU B 1 184 ? -1.150  -27.515 76.856 1.00 14.36 ?  184 LEU B O     1 
ATOM   4505 C CB    . LEU B 1 184 ? -0.001  -29.816 74.919 1.00 35.45 ?  184 LEU B CB    1 
ATOM   4506 C CG    . LEU B 1 184 ? 0.009   -31.339 74.681 1.00 22.86 ?  184 LEU B CG    1 
ATOM   4507 C CD1   . LEU B 1 184 ? 1.435   -31.856 74.524 1.00 8.77  ?  184 LEU B CD1   1 
ATOM   4508 C CD2   . LEU B 1 184 ? -0.734  -32.090 75.788 1.00 9.45  ?  184 LEU B CD2   1 
ATOM   4509 N N     . CYS B 1 185 ? -1.307  -26.791 74.731 1.00 17.27 ?  185 CYS B N     1 
ATOM   4510 C CA    . CYS B 1 185 ? -1.229  -25.391 75.160 1.00 26.61 ?  185 CYS B CA    1 
ATOM   4511 C C     . CYS B 1 185 ? -2.507  -24.943 75.844 1.00 23.58 ?  185 CYS B C     1 
ATOM   4512 O O     . CYS B 1 185 ? -2.469  -24.185 76.813 1.00 16.86 ?  185 CYS B O     1 
ATOM   4513 C CB    . CYS B 1 185 ? -0.945  -24.467 73.986 1.00 25.71 ?  185 CYS B CB    1 
ATOM   4514 S SG    . CYS B 1 185 ? 0.459   -24.975 73.012 1.00 32.50 ?  185 CYS B SG    1 
ATOM   4515 N N     . THR B 1 186 ? -3.650  -25.364 75.326 1.00 28.59 ?  186 THR B N     1 
ATOM   4516 C CA    . THR B 1 186 ? -4.900  -25.123 76.026 1.00 8.97  ?  186 THR B CA    1 
ATOM   4517 C C     . THR B 1 186 ? -4.920  -25.829 77.372 1.00 9.13  ?  186 THR B C     1 
ATOM   4518 O O     . THR B 1 186 ? -5.336  -25.260 78.386 1.00 9.43  ?  186 THR B O     1 
ATOM   4519 C CB    . THR B 1 186 ? -6.046  -25.580 75.142 1.00 9.53  ?  186 THR B CB    1 
ATOM   4520 O OG1   . THR B 1 186 ? -6.181  -24.646 74.058 1.00 13.35 ?  186 THR B OG1   1 
ATOM   4521 C CG2   . THR B 1 186 ? -7.337  -25.674 75.922 1.00 9.88  ?  186 THR B CG2   1 
ATOM   4522 N N     . LYS B 1 187 ? -4.498  -27.089 77.390 1.00 20.47 ?  187 LYS B N     1 
ATOM   4523 C CA    . LYS B 1 187 ? -4.584  -27.899 78.599 1.00 18.22 ?  187 LYS B CA    1 
ATOM   4524 C C     . LYS B 1 187 ? -3.664  -27.369 79.710 1.00 20.99 ?  187 LYS B C     1 
ATOM   4525 O O     . LYS B 1 187 ? -4.036  -27.400 80.886 1.00 30.89 ?  187 LYS B O     1 
ATOM   4526 C CB    . LYS B 1 187 ? -4.314  -29.360 78.199 1.00 9.53  ?  187 LYS B CB    1 
ATOM   4527 C CG    . LYS B 1 187 ? -4.125  -30.365 79.310 1.00 15.78 ?  187 LYS B CG    1 
ATOM   4528 C CD    . LYS B 1 187 ? -3.638  -31.705 78.742 1.00 10.60 ?  187 LYS B CD    1 
ATOM   4529 C CE    . LYS B 1 187 ? -3.659  -32.774 79.816 1.00 16.09 ?  187 LYS B CE    1 
ATOM   4530 N NZ    . LYS B 1 187 ? -3.205  -32.289 81.152 1.00 9.67  1  187 LYS B NZ    1 
ATOM   4531 N N     . TYR B 1 188 ? -2.505  -26.804 79.367 1.00 20.68 ?  188 TYR B N     1 
ATOM   4532 C CA    . TYR B 1 188 ? -1.592  -26.271 80.382 1.00 23.71 ?  188 TYR B CA    1 
ATOM   4533 C C     . TYR B 1 188 ? -1.552  -24.752 80.379 1.00 13.21 ?  188 TYR B C     1 
ATOM   4534 O O     . TYR B 1 188 ? -0.961  -24.163 81.277 1.00 7.77  ?  188 TYR B O     1 
ATOM   4535 C CB    . TYR B 1 188 ? -0.170  -26.825 80.193 1.00 29.69 ?  188 TYR B CB    1 
ATOM   4536 C CG    . TYR B 1 188 ? -0.130  -28.311 80.421 1.00 7.97  ?  188 TYR B CG    1 
ATOM   4537 C CD1   . TYR B 1 188 ? -0.061  -28.850 81.702 1.00 8.00  ?  188 TYR B CD1   1 
ATOM   4538 C CD2   . TYR B 1 188 ? -0.243  -29.175 79.361 1.00 8.26  ?  188 TYR B CD2   1 
ATOM   4539 C CE1   . TYR B 1 188 ? -0.083  -30.217 81.895 1.00 8.30  ?  188 TYR B CE1   1 
ATOM   4540 C CE2   . TYR B 1 188 ? -0.269  -30.527 79.549 1.00 8.89  ?  188 TYR B CE2   1 
ATOM   4541 C CZ    . TYR B 1 188 ? -0.190  -31.050 80.808 1.00 11.48 ?  188 TYR B CZ    1 
ATOM   4542 O OH    . TYR B 1 188 ? -0.213  -32.420 80.958 1.00 26.73 ?  188 TYR B OH    1 
ATOM   4543 N N     . ASN B 1 189 ? -2.350  -24.129 79.525 1.00 9.18  ?  189 ASN B N     1 
ATOM   4544 C CA    . ASN B 1 189 ? -2.386  -22.693 79.360 1.00 26.02 ?  189 ASN B CA    1 
ATOM   4545 C C     . ASN B 1 189 ? -1.002  -22.097 79.147 1.00 29.90 ?  189 ASN B C     1 
ATOM   4546 O O     . ASN B 1 189 ? -0.548  -21.206 79.871 1.00 10.31 ?  189 ASN B O     1 
ATOM   4547 C CB    . ASN B 1 189 ? -3.054  -22.048 80.555 1.00 24.07 ?  189 ASN B CB    1 
ATOM   4548 C CG    . ASN B 1 189 ? -3.518  -20.722 80.226 1.00 7.24  ?  189 ASN B CG    1 
ATOM   4549 O OD1   . ASN B 1 189 ? -3.921  -20.484 79.083 1.00 7.39  ?  189 ASN B OD1   1 
ATOM   4550 N ND2   . ASN B 1 189 ? -3.438  -19.816 81.176 1.00 6.96  ?  189 ASN B ND2   1 
ATOM   4551 N N     . VAL B 1 190 ? -0.413  -22.517 78.090 1.00 31.53 ?  190 VAL B N     1 
ATOM   4552 C CA    . VAL B 1 190 ? 0.838   -21.962 77.626 1.00 32.08 ?  190 VAL B CA    1 
ATOM   4553 C C     . VAL B 1 190 ? 0.520   -20.877 76.607 1.00 37.33 ?  190 VAL B C     1 
ATOM   4554 O O     . VAL B 1 190 ? -0.333  -21.048 75.731 1.00 43.56 ?  190 VAL B O     1 
ATOM   4555 C CB    . VAL B 1 190 ? 1.746   -23.062 77.036 1.00 17.90 ?  190 VAL B CB    1 
ATOM   4556 C CG1   . VAL B 1 190 ? 3.138   -22.526 76.801 1.00 6.52  ?  190 VAL B CG1   1 
ATOM   4557 C CG2   . VAL B 1 190 ? 1.804   -24.258 77.978 1.00 29.12 ?  190 VAL B CG2   1 
ATOM   4558 N N     . ILE B 1 191 ? 1.181   -19.743 76.732 1.00 27.62 ?  191 ILE B N     1 
ATOM   4559 C CA    . ILE B 1 191 ? 1.028   -18.684 75.750 1.00 7.38  ?  191 ILE B CA    1 
ATOM   4560 C C     . ILE B 1 191 ? 1.938   -19.017 74.582 1.00 6.02  ?  191 ILE B C     1 
ATOM   4561 O O     . ILE B 1 191 ? 3.021   -19.571 74.780 1.00 46.73 ?  191 ILE B O     1 
ATOM   4562 C CB    . ILE B 1 191 ? 1.361   -17.327 76.396 1.00 11.92 ?  191 ILE B CB    1 
ATOM   4563 C CG1   . ILE B 1 191 ? 0.388   -17.059 77.555 1.00 15.59 ?  191 ILE B CG1   1 
ATOM   4564 C CG2   . ILE B 1 191 ? 1.360   -16.198 75.369 1.00 20.29 ?  191 ILE B CG2   1 
ATOM   4565 C CD1   . ILE B 1 191 ? -1.082  -17.093 77.170 1.00 7.16  ?  191 ILE B CD1   1 
ATOM   4566 N N     . VAL B 1 192 ? 1.490   -18.769 73.356 1.00 6.20  ?  192 VAL B N     1 
ATOM   4567 C CA    . VAL B 1 192 ? 2.231   -19.165 72.161 1.00 22.67 ?  192 VAL B CA    1 
ATOM   4568 C C     . VAL B 1 192 ? 2.543   -17.920 71.348 1.00 27.49 ?  192 VAL B C     1 
ATOM   4569 O O     . VAL B 1 192 ? 1.643   -17.134 71.037 1.00 38.06 ?  192 VAL B O     1 
ATOM   4570 C CB    . VAL B 1 192 ? 1.475   -20.197 71.302 1.00 13.53 ?  192 VAL B CB    1 
ATOM   4571 C CG1   . VAL B 1 192 ? 2.255   -20.504 69.996 1.00 8.12  ?  192 VAL B CG1   1 
ATOM   4572 C CG2   . VAL B 1 192 ? 1.219   -21.463 72.111 1.00 10.46 ?  192 VAL B CG2   1 
ATOM   4573 N N     . VAL B 1 193 ? 3.820   -17.737 71.033 1.00 24.91 ?  193 VAL B N     1 
ATOM   4574 C CA    . VAL B 1 193 ? 4.282   -16.760 70.058 1.00 14.10 ?  193 VAL B CA    1 
ATOM   4575 C C     . VAL B 1 193 ? 4.605   -17.526 68.786 1.00 22.41 ?  193 VAL B C     1 
ATOM   4576 O O     . VAL B 1 193 ? 5.492   -18.386 68.782 1.00 23.05 ?  193 VAL B O     1 
ATOM   4577 C CB    . VAL B 1 193 ? 5.516   -16.003 70.570 1.00 5.06  ?  193 VAL B CB    1 
ATOM   4578 C CG1   . VAL B 1 193 ? 6.000   -15.000 69.550 1.00 14.24 ?  193 VAL B CG1   1 
ATOM   4579 C CG2   . VAL B 1 193 ? 5.200   -15.345 71.899 1.00 6.04  ?  193 VAL B CG2   1 
ATOM   4580 N N     . ALA B 1 194 ? 3.893   -17.226 67.705 1.00 26.66 ?  194 ALA B N     1 
ATOM   4581 C CA    . ALA B 1 194 ? 4.036   -17.972 66.457 1.00 21.74 ?  194 ALA B CA    1 
ATOM   4582 C C     . ALA B 1 194 ? 4.871   -17.148 65.498 1.00 21.49 ?  194 ALA B C     1 
ATOM   4583 O O     . ALA B 1 194 ? 4.383   -16.199 64.887 1.00 42.08 ?  194 ALA B O     1 
ATOM   4584 C CB    . ALA B 1 194 ? 2.676   -18.297 65.854 1.00 30.28 ?  194 ALA B CB    1 
ATOM   4585 N N     . ASP B 1 195 ? 6.133   -17.510 65.363 1.00 13.59 ?  195 ASP B N     1 
ATOM   4586 C CA    . ASP B 1 195 ? 6.992   -16.865 64.387 1.00 6.83  ?  195 ASP B CA    1 
ATOM   4587 C C     . ASP B 1 195 ? 6.790   -17.582 63.062 1.00 19.68 ?  195 ASP B C     1 
ATOM   4588 O O     . ASP B 1 195 ? 7.460   -18.568 62.744 1.00 29.06 ?  195 ASP B O     1 
ATOM   4589 C CB    . ASP B 1 195 ? 8.439   -16.881 64.850 1.00 12.15 ?  195 ASP B CB    1 
ATOM   4590 C CG    . ASP B 1 195 ? 9.328   -16.012 64.004 1.00 4.99  ?  195 ASP B CG    1 
ATOM   4591 O OD1   . ASP B 1 195 ? 9.029   -15.784 62.820 1.00 8.05  ?  195 ASP B OD1   1 
ATOM   4592 O OD2   . ASP B 1 195 ? 10.330  -15.527 64.537 1.00 22.90 -1 195 ASP B OD2   1 
ATOM   4593 N N     . GLU B 1 196 ? 5.869   -17.051 62.272 1.00 6.40  ?  196 GLU B N     1 
ATOM   4594 C CA    . GLU B 1 196 ? 5.520   -17.577 60.965 1.00 7.68  ?  196 GLU B CA    1 
ATOM   4595 C C     . GLU B 1 196 ? 6.088   -16.676 59.878 1.00 21.49 ?  196 GLU B C     1 
ATOM   4596 O O     . GLU B 1 196 ? 5.421   -16.349 58.900 1.00 41.04 ?  196 GLU B O     1 
ATOM   4597 C CB    . GLU B 1 196 ? 4.006   -17.737 60.843 1.00 7.46  ?  196 GLU B CB    1 
ATOM   4598 C CG    . GLU B 1 196 ? 3.409   -18.515 62.024 1.00 7.45  ?  196 GLU B CG    1 
ATOM   4599 C CD    . GLU B 1 196 ? 1.932   -18.825 61.859 1.00 8.02  ?  196 GLU B CD    1 
ATOM   4600 O OE1   . GLU B 1 196 ? 1.279   -19.208 62.849 1.00 8.04  ?  196 GLU B OE1   1 
ATOM   4601 O OE2   . GLU B 1 196 ? 1.427   -18.686 60.734 1.00 16.91 -1 196 GLU B OE2   1 
ATOM   4602 N N     . ILE B 1 197 ? 7.349   -16.273 60.047 1.00 21.89 ?  197 ILE B N     1 
ATOM   4603 C CA    . ILE B 1 197 ? 7.970   -15.325 59.126 1.00 29.15 ?  197 ILE B CA    1 
ATOM   4604 C C     . ILE B 1 197 ? 8.213   -15.946 57.752 1.00 28.17 ?  197 ILE B C     1 
ATOM   4605 O O     . ILE B 1 197 ? 8.305   -15.227 56.750 1.00 45.69 ?  197 ILE B O     1 
ATOM   4606 C CB    . ILE B 1 197 ? 9.258   -14.754 59.765 1.00 18.06 ?  197 ILE B CB    1 
ATOM   4607 C CG1   . ILE B 1 197 ? 9.781   -13.539 58.976 1.00 24.73 ?  197 ILE B CG1   1 
ATOM   4608 C CG2   . ILE B 1 197 ? 10.285  -15.829 59.914 1.00 14.89 ?  197 ILE B CG2   1 
ATOM   4609 C CD1   . ILE B 1 197 ? 11.165  -13.000 59.420 1.00 16.67 ?  197 ILE B CD1   1 
ATOM   4610 N N     . HIS B 1 198 ? 8.295   -17.265 57.668 1.00 28.62 ?  198 HIS B N     1 
ATOM   4611 C CA    . HIS B 1 198 ? 8.465   -17.948 56.395 1.00 33.88 ?  198 HIS B CA    1 
ATOM   4612 C C     . HIS B 1 198 ? 7.134   -18.431 55.825 1.00 29.00 ?  198 HIS B C     1 
ATOM   4613 O O     . HIS B 1 198 ? 7.128   -19.276 54.923 1.00 40.91 ?  198 HIS B O     1 
ATOM   4614 C CB    . HIS B 1 198 ? 9.434   -19.122 56.549 1.00 25.23 ?  198 HIS B CB    1 
ATOM   4615 C CG    . HIS B 1 198 ? 10.836  -18.711 56.875 1.00 9.45  ?  198 HIS B CG    1 
ATOM   4616 N ND1   . HIS B 1 198 ? 11.770  -18.403 55.906 1.00 8.31  ?  198 HIS B ND1   1 
ATOM   4617 C CD2   . HIS B 1 198 ? 11.459  -18.547 58.068 1.00 9.59  ?  198 HIS B CD2   1 
ATOM   4618 C CE1   . HIS B 1 198 ? 12.912  -18.082 56.491 1.00 19.82 ?  198 HIS B CE1   1 
ATOM   4619 N NE2   . HIS B 1 198 ? 12.748  -18.156 57.802 1.00 7.11  ?  198 HIS B NE2   1 
ATOM   4620 N N     . SER B 1 199 ? 6.008   -17.883 56.309 1.00 14.33 ?  199 SER B N     1 
ATOM   4621 C CA    . SER B 1 199 ? 4.690   -18.435 55.990 1.00 20.55 ?  199 SER B CA    1 
ATOM   4622 C C     . SER B 1 199 ? 4.382   -18.413 54.503 1.00 25.18 ?  199 SER B C     1 
ATOM   4623 O O     . SER B 1 199 ? 3.426   -19.073 54.082 1.00 38.50 ?  199 SER B O     1 
ATOM   4624 C CB    . SER B 1 199 ? 3.563   -17.711 56.766 1.00 27.89 ?  199 SER B CB    1 
ATOM   4625 O OG    . SER B 1 199 ? 3.299   -16.370 56.344 1.00 27.91 ?  199 SER B OG    1 
ATOM   4626 N N     . ASP B 1 200 ? 5.160   -17.690 53.701 1.00 23.89 ?  200 ASP B N     1 
ATOM   4627 C CA    . ASP B 1 200 ? 4.818   -17.451 52.307 1.00 34.73 ?  200 ASP B CA    1 
ATOM   4628 C C     . ASP B 1 200 ? 5.652   -18.243 51.321 1.00 46.64 ?  200 ASP B C     1 
ATOM   4629 O O     . ASP B 1 200 ? 5.390   -18.167 50.114 1.00 48.33 ?  200 ASP B O     1 
ATOM   4630 C CB    . ASP B 1 200 ? 4.923   -15.959 52.009 1.00 32.05 ?  200 ASP B CB    1 
ATOM   4631 C CG    . ASP B 1 200 ? 3.836   -15.189 52.698 1.00 33.04 ?  200 ASP B CG    1 
ATOM   4632 O OD1   . ASP B 1 200 ? 2.762   -15.796 52.853 1.00 32.43 ?  200 ASP B OD1   1 
ATOM   4633 O OD2   . ASP B 1 200 ? 4.030   -14.019 53.083 1.00 29.85 -1 200 ASP B OD2   1 
ATOM   4634 N N     . ILE B 1 201 ? 6.656   -18.976 51.789 1.00 46.66 ?  201 ILE B N     1 
ATOM   4635 C CA    . ILE B 1 201 ? 7.415   -19.856 50.915 1.00 43.26 ?  201 ILE B CA    1 
ATOM   4636 C C     . ILE B 1 201 ? 7.052   -21.291 51.266 1.00 37.99 ?  201 ILE B C     1 
ATOM   4637 O O     . ILE B 1 201 ? 7.684   -21.908 52.128 1.00 51.63 ?  201 ILE B O     1 
ATOM   4638 C CB    . ILE B 1 201 ? 8.928   -19.611 51.036 1.00 46.62 ?  201 ILE B CB    1 
ATOM   4639 C CG1   . ILE B 1 201 ? 9.312   -18.246 50.435 1.00 43.11 ?  201 ILE B CG1   1 
ATOM   4640 C CG2   . ILE B 1 201 ? 9.684   -20.756 50.398 1.00 35.70 ?  201 ILE B CG2   1 
ATOM   4641 C CD1   . ILE B 1 201 ? 9.583   -18.242 48.938 1.00 43.64 ?  201 ILE B CD1   1 
ATOM   4642 N N     . ILE B 1 202 ? 6.017   -21.818 50.620 1.00 29.56 ?  202 ILE B N     1 
ATOM   4643 C CA    . ILE B 1 202 ? 5.488   -23.145 50.901 1.00 32.34 ?  202 ILE B CA    1 
ATOM   4644 C C     . ILE B 1 202 ? 5.496   -23.941 49.604 1.00 41.04 ?  202 ILE B C     1 
ATOM   4645 O O     . ILE B 1 202 ? 5.181   -23.407 48.536 1.00 46.45 ?  202 ILE B O     1 
ATOM   4646 C CB    . ILE B 1 202 ? 4.066   -23.067 51.492 1.00 35.15 ?  202 ILE B CB    1 
ATOM   4647 C CG1   . ILE B 1 202 ? 4.058   -22.116 52.680 1.00 25.15 ?  202 ILE B CG1   1 
ATOM   4648 C CG2   . ILE B 1 202 ? 3.573   -24.432 51.911 1.00 50.37 ?  202 ILE B CG2   1 
ATOM   4649 C CD1   . ILE B 1 202 ? 4.986   -22.540 53.777 1.00 18.69 ?  202 ILE B CD1   1 
ATOM   4650 N N     . TYR B 1 203 ? 5.838   -25.221 49.698 1.00 36.79 ?  203 TYR B N     1 
ATOM   4651 C CA    . TYR B 1 203 ? 6.026   -26.033 48.508 1.00 39.71 ?  203 TYR B CA    1 
ATOM   4652 C C     . TYR B 1 203 ? 4.706   -26.660 48.048 1.00 37.02 ?  203 TYR B C     1 
ATOM   4653 O O     . TYR B 1 203 ? 3.663   -26.542 48.698 1.00 24.87 ?  203 TYR B O     1 
ATOM   4654 C CB    . TYR B 1 203 ? 7.100   -27.084 48.762 1.00 30.36 ?  203 TYR B CB    1 
ATOM   4655 C CG    . TYR B 1 203 ? 8.488   -26.494 48.894 1.00 35.01 ?  203 TYR B CG    1 
ATOM   4656 C CD1   . TYR B 1 203 ? 8.742   -25.164 48.577 1.00 24.15 ?  203 TYR B CD1   1 
ATOM   4657 C CD2   . TYR B 1 203 ? 9.548   -27.269 49.335 1.00 33.67 ?  203 TYR B CD2   1 
ATOM   4658 C CE1   . TYR B 1 203 ? 10.012  -24.635 48.698 1.00 26.68 ?  203 TYR B CE1   1 
ATOM   4659 C CE2   . TYR B 1 203 ? 10.807  -26.746 49.461 1.00 14.24 ?  203 TYR B CE2   1 
ATOM   4660 C CZ    . TYR B 1 203 ? 11.044  -25.437 49.143 1.00 24.71 ?  203 TYR B CZ    1 
ATOM   4661 O OH    . TYR B 1 203 ? 12.331  -24.940 49.278 1.00 30.84 ?  203 TYR B OH    1 
ATOM   4662 N N     . ALA B 1 204 ? 4.767   -27.352 46.906 1.00 41.12 ?  204 ALA B N     1 
ATOM   4663 C CA    . ALA B 1 204 ? 3.557   -27.806 46.219 1.00 38.27 ?  204 ALA B CA    1 
ATOM   4664 C C     . ALA B 1 204 ? 2.748   -28.787 47.067 1.00 48.95 ?  204 ALA B C     1 
ATOM   4665 O O     . ALA B 1 204 ? 1.513   -28.792 47.005 1.00 58.57 ?  204 ALA B O     1 
ATOM   4666 C CB    . ALA B 1 204 ? 3.923   -28.433 44.876 1.00 33.93 ?  204 ALA B CB    1 
ATOM   4667 N N     . ASP B 1 205 ? 3.419   -29.646 47.832 1.00 43.08 ?  205 ASP B N     1 
ATOM   4668 C CA    . ASP B 1 205 ? 2.763   -30.681 48.625 1.00 39.40 ?  205 ASP B CA    1 
ATOM   4669 C C     . ASP B 1 205 ? 2.430   -30.249 50.058 1.00 32.26 ?  205 ASP B C     1 
ATOM   4670 O O     . ASP B 1 205 ? 2.130   -31.110 50.889 1.00 32.29 ?  205 ASP B O     1 
ATOM   4671 C CB    . ASP B 1 205 ? 3.649   -31.931 48.681 1.00 50.16 ?  205 ASP B CB    1 
ATOM   4672 C CG    . ASP B 1 205 ? 4.078   -32.412 47.307 1.00 62.25 ?  205 ASP B CG    1 
ATOM   4673 O OD1   . ASP B 1 205 ? 3.839   -31.690 46.317 1.00 67.70 -1 205 ASP B OD1   1 
ATOM   4674 O OD2   . ASP B 1 205 ? 4.655   -33.514 47.217 1.00 65.73 -1 205 ASP B OD2   1 
ATOM   4675 N N     . HIS B 1 206 ? 2.499   -28.958 50.386 1.00 29.42 ?  206 HIS B N     1 
ATOM   4676 C CA    . HIS B 1 206 ? 2.296   -28.536 51.768 1.00 25.11 ?  206 HIS B CA    1 
ATOM   4677 C C     . HIS B 1 206 ? 1.501   -27.240 51.811 1.00 31.11 ?  206 HIS B C     1 
ATOM   4678 O O     . HIS B 1 206 ? 1.422   -26.500 50.830 1.00 42.29 ?  206 HIS B O     1 
ATOM   4679 C CB    . HIS B 1 206 ? 3.642   -28.373 52.515 1.00 33.22 ?  206 HIS B CB    1 
ATOM   4680 C CG    . HIS B 1 206 ? 4.383   -29.668 52.721 1.00 32.43 ?  206 HIS B CG    1 
ATOM   4681 N ND1   . HIS B 1 206 ? 5.394   -30.083 51.877 1.00 36.72 ?  206 HIS B ND1   1 
ATOM   4682 C CD2   . HIS B 1 206 ? 4.263   -30.636 53.663 1.00 28.91 ?  206 HIS B CD2   1 
ATOM   4683 C CE1   . HIS B 1 206 ? 5.868   -31.244 52.296 1.00 34.53 ?  206 HIS B CE1   1 
ATOM   4684 N NE2   . HIS B 1 206 ? 5.196   -31.604 53.375 1.00 31.61 ?  206 HIS B NE2   1 
ATOM   4685 N N     . THR B 1 207 ? 0.916   -26.969 52.973 1.00 36.15 ?  207 THR B N     1 
ATOM   4686 C CA    . THR B 1 207 ? 0.082   -25.792 53.181 1.00 32.36 ?  207 THR B CA    1 
ATOM   4687 C C     . THR B 1 207 ? 0.335   -25.259 54.581 1.00 35.83 ?  207 THR B C     1 
ATOM   4688 O O     . THR B 1 207 ? 0.286   -26.017 55.556 1.00 38.19 ?  207 THR B O     1 
ATOM   4689 C CB    . THR B 1 207 ? -1.403  -26.114 52.997 1.00 25.45 ?  207 THR B CB    1 
ATOM   4690 O OG1   . THR B 1 207 ? -1.610  -26.618 51.678 1.00 34.11 ?  207 THR B OG1   1 
ATOM   4691 C CG2   . THR B 1 207 ? -2.243  -24.860 53.160 1.00 42.10 ?  207 THR B CG2   1 
ATOM   4692 N N     . HIS B 1 208 ? 0.638   -23.967 54.673 1.00 20.23 ?  208 HIS B N     1 
ATOM   4693 C CA    . HIS B 1 208 ? 0.857   -23.367 55.978 1.00 14.89 ?  208 HIS B CA    1 
ATOM   4694 C C     . HIS B 1 208 ? -0.452  -23.235 56.732 1.00 17.29 ?  208 HIS B C     1 
ATOM   4695 O O     . HIS B 1 208 ? -1.471  -22.819 56.174 1.00 27.41 ?  208 HIS B O     1 
ATOM   4696 C CB    . HIS B 1 208 ? 1.529   -22.008 55.863 1.00 14.78 ?  208 HIS B CB    1 
ATOM   4697 C CG    . HIS B 1 208 ? 1.722   -21.347 57.187 1.00 19.12 ?  208 HIS B CG    1 
ATOM   4698 N ND1   . HIS B 1 208 ? 2.380   -21.964 58.230 1.00 18.22 ?  208 HIS B ND1   1 
ATOM   4699 C CD2   . HIS B 1 208 ? 1.321   -20.141 57.653 1.00 21.79 ?  208 HIS B CD2   1 
ATOM   4700 C CE1   . HIS B 1 208 ? 2.383   -21.163 59.280 1.00 21.34 ?  208 HIS B CE1   1 
ATOM   4701 N NE2   . HIS B 1 208 ? 1.748   -20.050 58.955 1.00 23.16 ?  208 HIS B NE2   1 
ATOM   4702 N N     . THR B 1 209 ? -0.429  -23.637 57.993 1.00 18.20 ?  209 THR B N     1 
ATOM   4703 C CA    . THR B 1 209 ? -1.604  -23.604 58.858 1.00 26.16 ?  209 THR B CA    1 
ATOM   4704 C C     . THR B 1 209 ? -1.346  -22.642 60.008 1.00 32.88 ?  209 THR B C     1 
ATOM   4705 O O     . THR B 1 209 ? -0.677  -23.015 60.990 1.00 34.53 ?  209 THR B O     1 
ATOM   4706 C CB    . THR B 1 209 ? -1.940  -25.006 59.371 1.00 22.66 ?  209 THR B CB    1 
ATOM   4707 O OG1   . THR B 1 209 ? -2.198  -25.870 58.255 1.00 29.43 ?  209 THR B OG1   1 
ATOM   4708 C CG2   . THR B 1 209 ? -3.156  -24.981 60.259 1.00 16.42 ?  209 THR B CG2   1 
ATOM   4709 N N     . PRO B 1 210 ? -1.837  -21.405 59.939 1.00 22.27 ?  210 PRO B N     1 
ATOM   4710 C CA    . PRO B 1 210 ? -1.707  -20.500 61.083 1.00 12.72 ?  210 PRO B CA    1 
ATOM   4711 C C     . PRO B 1 210 ? -2.270  -21.148 62.340 1.00 10.29 ?  210 PRO B C     1 
ATOM   4712 O O     . PRO B 1 210 ? -3.333  -21.761 62.320 1.00 12.60 ?  210 PRO B O     1 
ATOM   4713 C CB    . PRO B 1 210 ? -2.531  -19.273 60.661 1.00 17.71 ?  210 PRO B CB    1 
ATOM   4714 C CG    . PRO B 1 210 ? -2.504  -19.285 59.170 1.00 20.41 ?  210 PRO B CG    1 
ATOM   4715 C CD    . PRO B 1 210 ? -2.460  -20.742 58.776 1.00 32.79 ?  210 PRO B CD    1 
ATOM   4716 N N     . PHE B 1 211 ? -1.512  -21.045 63.427 1.00 9.17  ?  211 PHE B N     1 
ATOM   4717 C CA    . PHE B 1 211 ? -1.880  -21.671 64.692 1.00 9.11  ?  211 PHE B CA    1 
ATOM   4718 C C     . PHE B 1 211 ? -3.178  -21.105 65.252 1.00 25.53 ?  211 PHE B C     1 
ATOM   4719 O O     . PHE B 1 211 ? -4.002  -21.844 65.808 1.00 36.12 ?  211 PHE B O     1 
ATOM   4720 C CB    . PHE B 1 211 ? -0.752  -21.444 65.675 1.00 8.48  ?  211 PHE B CB    1 
ATOM   4721 C CG    . PHE B 1 211 ? -0.785  -22.302 66.886 1.00 8.42  ?  211 PHE B CG    1 
ATOM   4722 C CD1   . PHE B 1 211 ? -0.424  -23.633 66.817 1.00 8.58  ?  211 PHE B CD1   1 
ATOM   4723 C CD2   . PHE B 1 211 ? -1.074  -21.748 68.123 1.00 8.19  ?  211 PHE B CD2   1 
ATOM   4724 C CE1   . PHE B 1 211 ? -0.392  -24.395 67.950 1.00 8.52  ?  211 PHE B CE1   1 
ATOM   4725 C CE2   . PHE B 1 211 ? -1.044  -22.518 69.257 1.00 10.76 ?  211 PHE B CE2   1 
ATOM   4726 C CZ    . PHE B 1 211 ? -0.695  -23.846 69.164 1.00 8.32  ?  211 PHE B CZ    1 
ATOM   4727 N N     . ALA B 1 212 ? -3.377  -19.795 65.129 1.00 24.91 ?  212 ALA B N     1 
ATOM   4728 C CA    . ALA B 1 212 ? -4.588  -19.186 65.645 1.00 14.58 ?  212 ALA B CA    1 
ATOM   4729 C C     . ALA B 1 212 ? -5.785  -19.405 64.738 1.00 20.79 ?  212 ALA B C     1 
ATOM   4730 O O     . ALA B 1 212 ? -6.910  -19.157 65.167 1.00 32.62 ?  212 ALA B O     1 
ATOM   4731 C CB    . ALA B 1 212 ? -4.373  -17.684 65.847 1.00 20.57 ?  212 ALA B CB    1 
ATOM   4732 N N     . SER B 1 213 ? -5.568  -19.886 63.510 1.00 31.44 ?  213 SER B N     1 
ATOM   4733 C CA    . SER B 1 213 ? -6.657  -20.216 62.595 1.00 26.27 ?  213 SER B CA    1 
ATOM   4734 C C     . SER B 1 213 ? -7.467  -21.406 63.095 1.00 37.63 ?  213 SER B C     1 
ATOM   4735 O O     . SER B 1 213 ? -8.665  -21.514 62.794 1.00 31.16 ?  213 SER B O     1 
ATOM   4736 C CB    . SER B 1 213 ? -6.076  -20.474 61.203 1.00 17.38 ?  213 SER B CB    1 
ATOM   4737 O OG    . SER B 1 213 ? -7.074  -20.797 60.262 1.00 26.76 ?  213 SER B OG    1 
ATOM   4738 N N     . LEU B 1 214 ? -6.831  -22.296 63.859 1.00 41.84 ?  214 LEU B N     1 
ATOM   4739 C CA    . LEU B 1 214 ? -7.477  -23.538 64.258 1.00 34.68 ?  214 LEU B CA    1 
ATOM   4740 C C     . LEU B 1 214 ? -8.685  -23.295 65.154 1.00 31.14 ?  214 LEU B C     1 
ATOM   4741 O O     . LEU B 1 214 ? -9.703  -23.979 65.015 1.00 44.41 ?  214 LEU B O     1 
ATOM   4742 C CB    . LEU B 1 214 ? -6.479  -24.454 64.957 1.00 32.37 ?  214 LEU B CB    1 
ATOM   4743 C CG    . LEU B 1 214 ? -5.309  -24.891 64.078 1.00 23.71 ?  214 LEU B CG    1 
ATOM   4744 C CD1   . LEU B 1 214 ? -4.372  -25.800 64.844 1.00 21.92 ?  214 LEU B CD1   1 
ATOM   4745 C CD2   . LEU B 1 214 ? -5.772  -25.525 62.761 1.00 19.13 ?  214 LEU B CD2   1 
ATOM   4746 N N     . SER B 1 215 ? -8.608  -22.332 66.072 1.00 22.84 ?  215 SER B N     1 
ATOM   4747 C CA    . SER B 1 215 ? -9.631  -22.262 67.107 1.00 26.31 ?  215 SER B CA    1 
ATOM   4748 C C     . SER B 1 215 ? -9.829  -20.831 67.595 1.00 32.03 ?  215 SER B C     1 
ATOM   4749 O O     . SER B 1 215 ? -8.958  -19.967 67.453 1.00 24.48 ?  215 SER B O     1 
ATOM   4750 C CB    . SER B 1 215 ? -9.268  -23.189 68.279 1.00 34.13 ?  215 SER B CB    1 
ATOM   4751 O OG    . SER B 1 215 ? -9.858  -22.765 69.495 1.00 36.05 ?  215 SER B OG    1 
ATOM   4752 N N     . GLU B 1 216 ? -11.027 -20.593 68.145 1.00 40.21 ?  216 GLU B N     1 
ATOM   4753 C CA    . GLU B 1 216 ? -11.326 -19.342 68.838 1.00 40.33 ?  216 GLU B CA    1 
ATOM   4754 C C     . GLU B 1 216 ? -10.548 -19.214 70.135 1.00 43.51 ?  216 GLU B C     1 
ATOM   4755 O O     . GLU B 1 216 ? -10.241 -18.092 70.563 1.00 41.13 ?  216 GLU B O     1 
ATOM   4756 C CB    . GLU B 1 216 ? -12.830 -19.248 69.141 1.00 27.81 ?  216 GLU B CB    1 
ATOM   4757 C CG    . GLU B 1 216 ? -13.691 -18.945 67.934 1.00 26.70 ?  216 GLU B CG    1 
ATOM   4758 C CD    . GLU B 1 216 ? -14.852 -18.001 68.259 1.00 34.58 ?  216 GLU B CD    1 
ATOM   4759 O OE1   . GLU B 1 216 ? -15.725 -17.829 67.393 1.00 33.03 ?  216 GLU B OE1   1 
ATOM   4760 O OE2   . GLU B 1 216 ? -14.891 -17.419 69.367 1.00 35.41 -1 216 GLU B OE2   1 
ATOM   4761 N N     . GLU B 1 217 ? -10.248 -20.348 70.778 1.00 27.66 ?  217 GLU B N     1 
ATOM   4762 C CA    . GLU B 1 217 ? -9.549  -20.362 72.053 1.00 25.72 ?  217 GLU B CA    1 
ATOM   4763 C C     . GLU B 1 217 ? -8.032  -20.294 71.892 1.00 30.19 ?  217 GLU B C     1 
ATOM   4764 O O     . GLU B 1 217 ? -7.354  -19.652 72.700 1.00 29.98 ?  217 GLU B O     1 
ATOM   4765 C CB    . GLU B 1 217 ? -9.943  -21.595 72.865 1.00 13.72 ?  217 GLU B CB    1 
ATOM   4766 C CG    . GLU B 1 217 ? -9.564  -21.462 74.312 1.00 22.89 ?  217 GLU B CG    1 
ATOM   4767 C CD    . GLU B 1 217 ? -9.360  -22.784 74.989 1.00 50.63 ?  217 GLU B CD    1 
ATOM   4768 O OE1   . GLU B 1 217 ? -8.631  -22.811 76.002 1.00 61.32 ?  217 GLU B OE1   1 
ATOM   4769 O OE2   . GLU B 1 217 ? -9.943  -23.790 74.530 1.00 59.97 -1 217 GLU B OE2   1 
ATOM   4770 N N     . LEU B 1 218 ? -7.480  -20.957 70.872 1.00 25.76 ?  218 LEU B N     1 
ATOM   4771 C CA    . LEU B 1 218 ? -6.052  -20.842 70.608 1.00 15.26 ?  218 LEU B CA    1 
ATOM   4772 C C     . LEU B 1 218 ? -5.739  -19.482 70.024 1.00 19.45 ?  218 LEU B C     1 
ATOM   4773 O O     . LEU B 1 218 ? -4.586  -19.047 70.061 1.00 13.81 ?  218 LEU B O     1 
ATOM   4774 C CB    . LEU B 1 218 ? -5.574  -21.927 69.641 1.00 16.81 ?  218 LEU B CB    1 
ATOM   4775 C CG    . LEU B 1 218 ? -5.893  -23.427 69.781 1.00 27.17 ?  218 LEU B CG    1 
ATOM   4776 C CD1   . LEU B 1 218 ? -5.279  -24.173 68.598 1.00 9.98  ?  218 LEU B CD1   1 
ATOM   4777 C CD2   . LEU B 1 218 ? -5.499  -24.060 71.124 1.00 9.59  ?  218 LEU B CD2   1 
ATOM   4778 N N     . ALA B 1 219 ? -6.734  -18.840 69.404 1.00 23.20 ?  219 ALA B N     1 
ATOM   4779 C CA    . ALA B 1 219 ? -6.560  -17.471 68.936 1.00 30.48 ?  219 ALA B CA    1 
ATOM   4780 C C     . ALA B 1 219 ? -6.310  -16.519 70.105 1.00 32.23 ?  219 ALA B C     1 
ATOM   4781 O O     . ALA B 1 219 ? -5.453  -15.633 70.021 1.00 29.41 ?  219 ALA B O     1 
ATOM   4782 C CB    . ALA B 1 219 ? -7.775  -17.045 68.122 1.00 27.88 ?  219 ALA B CB    1 
ATOM   4783 N N     . GLU B 1 220 ? -7.045  -16.693 71.205 1.00 23.42 ?  220 GLU B N     1 
ATOM   4784 C CA    . GLU B 1 220 ? -6.939  -15.850 72.393 1.00 24.75 ?  220 GLU B CA    1 
ATOM   4785 C C     . GLU B 1 220 ? -5.682  -16.120 73.210 1.00 26.08 ?  220 GLU B C     1 
ATOM   4786 O O     . GLU B 1 220 ? -5.530  -15.557 74.306 1.00 7.41  ?  220 GLU B O     1 
ATOM   4787 C CB    . GLU B 1 220 ? -8.172  -16.046 73.283 1.00 32.01 ?  220 GLU B CB    1 
ATOM   4788 C CG    . GLU B 1 220 ? -9.435  -15.519 72.665 1.00 31.79 ?  220 GLU B CG    1 
ATOM   4789 C CD    . GLU B 1 220 ? -9.482  -14.007 72.654 1.00 25.02 ?  220 GLU B CD    1 
ATOM   4790 O OE1   . GLU B 1 220 ? -9.469  -13.414 71.556 1.00 22.61 ?  220 GLU B OE1   1 
ATOM   4791 O OE2   . GLU B 1 220 ? -9.547  -13.417 73.750 1.00 19.27 -1 220 GLU B OE2   1 
ATOM   4792 N N     . ARG B 1 221 ? -4.803  -17.008 72.756 1.00 21.80 ?  221 ARG B N     1 
ATOM   4793 C CA    . ARG B 1 221 ? -3.571  -17.260 73.487 1.00 19.57 ?  221 ARG B CA    1 
ATOM   4794 C C     . ARG B 1 221 ? -2.338  -17.207 72.592 1.00 7.08  ?  221 ARG B C     1 
ATOM   4795 O O     . ARG B 1 221 ? -1.231  -17.373 73.094 1.00 14.42 ?  221 ARG B O     1 
ATOM   4796 C CB    . ARG B 1 221 ? -3.655  -18.608 74.230 1.00 18.91 ?  221 ARG B CB    1 
ATOM   4797 C CG    . ARG B 1 221 ? -3.851  -19.812 73.300 1.00 22.49 ?  221 ARG B CG    1 
ATOM   4798 C CD    . ARG B 1 221 ? -3.679  -21.174 73.982 1.00 25.33 ?  221 ARG B CD    1 
ATOM   4799 N NE    . ARG B 1 221 ? -4.726  -21.420 74.963 1.00 8.25  ?  221 ARG B NE    1 
ATOM   4800 C CZ    . ARG B 1 221 ? -4.562  -21.256 76.268 1.00 18.60 ?  221 ARG B CZ    1 
ATOM   4801 N NH1   . ARG B 1 221 ? -3.408  -20.839 76.743 1.00 10.42 1  221 ARG B NH1   1 
ATOM   4802 N NH2   . ARG B 1 221 ? -5.556  -21.491 77.100 1.00 30.48 ?  221 ARG B NH2   1 
ATOM   4803 N N     . THR B 1 222 ? -2.480  -16.864 71.314 1.00 17.15 ?  222 THR B N     1 
ATOM   4804 C CA    . THR B 1 222 ? -1.378  -16.912 70.355 1.00 15.38 ?  222 THR B CA    1 
ATOM   4805 C C     . THR B 1 222 ? -1.072  -15.515 69.819 1.00 18.11 ?  222 THR B C     1 
ATOM   4806 O O     . THR B 1 222 ? -1.987  -14.741 69.515 1.00 10.37 ?  222 THR B O     1 
ATOM   4807 C CB    . THR B 1 222 ? -1.710  -17.853 69.179 1.00 11.25 ?  222 THR B CB    1 
ATOM   4808 O OG1   . THR B 1 222 ? -1.897  -19.189 69.665 1.00 28.56 ?  222 THR B OG1   1 
ATOM   4809 C CG2   . THR B 1 222 ? -0.609  -17.849 68.136 1.00 7.31  ?  222 THR B CG2   1 
ATOM   4810 N N     . ILE B 1 223 ? 0.225   -15.197 69.727 1.00 12.15 ?  223 ILE B N     1 
ATOM   4811 C CA    . ILE B 1 223 ? 0.724   -13.966 69.125 1.00 6.07  ?  223 ILE B CA    1 
ATOM   4812 C C     . ILE B 1 223 ? 1.496   -14.349 67.867 1.00 10.39 ?  223 ILE B C     1 
ATOM   4813 O O     . ILE B 1 223 ? 2.636   -14.826 67.949 1.00 15.48 ?  223 ILE B O     1 
ATOM   4814 C CB    . ILE B 1 223 ? 1.614   -13.185 70.109 1.00 31.62 ?  223 ILE B CB    1 
ATOM   4815 C CG1   . ILE B 1 223 ? 0.927   -13.034 71.471 1.00 30.93 ?  223 ILE B CG1   1 
ATOM   4816 C CG2   . ILE B 1 223 ? 2.044   -11.835 69.546 1.00 5.30  ?  223 ILE B CG2   1 
ATOM   4817 C CD1   . ILE B 1 223 ? 1.290   -14.140 72.467 1.00 36.54 ?  223 ILE B CD1   1 
ATOM   4818 N N     . THR B 1 224 ? 0.952   -14.000 66.703 1.00 11.92 ?  224 THR B N     1 
ATOM   4819 C CA    . THR B 1 224 ? 1.454   -14.453 65.409 1.00 9.47  ?  224 THR B CA    1 
ATOM   4820 C C     . THR B 1 224 ? 2.225   -13.312 64.765 1.00 14.33 ?  224 THR B C     1 
ATOM   4821 O O     . THR B 1 224 ? 1.686   -12.218 64.589 1.00 17.57 ?  224 THR B O     1 
ATOM   4822 C CB    . THR B 1 224 ? 0.307   -14.922 64.509 1.00 7.24  ?  224 THR B CB    1 
ATOM   4823 O OG1   . THR B 1 224 ? -0.107  -16.235 64.904 1.00 26.89 ?  224 THR B OG1   1 
ATOM   4824 C CG2   . THR B 1 224 ? 0.706   -14.958 63.065 1.00 7.47  ?  224 THR B CG2   1 
ATOM   4825 N N     . CYS B 1 225 ? 3.490   -13.570 64.433 1.00 30.02 ?  225 CYS B N     1 
ATOM   4826 C CA    . CYS B 1 225 ? 4.393   -12.584 63.857 1.00 5.78  ?  225 CYS B CA    1 
ATOM   4827 C C     . CYS B 1 225 ? 4.686   -12.956 62.421 1.00 6.09  ?  225 CYS B C     1 
ATOM   4828 O O     . CYS B 1 225 ? 5.333   -13.971 62.165 1.00 8.23  ?  225 CYS B O     1 
ATOM   4829 C CB    . CYS B 1 225 ? 5.716   -12.539 64.613 1.00 9.60  ?  225 CYS B CB    1 
ATOM   4830 S SG    . CYS B 1 225 ? 5.667   -12.717 66.370 1.00 28.84 ?  225 CYS B SG    1 
ATOM   4831 N N     . MET B 1 226 ? 4.381   -12.053 61.514 1.00 6.31  ?  226 MET B N     1 
ATOM   4832 C CA    . MET B 1 226 ? 4.551   -12.279 60.095 1.00 7.22  ?  226 MET B CA    1 
ATOM   4833 C C     . MET B 1 226 ? 5.224   -11.057 59.498 1.00 25.12 ?  226 MET B C     1 
ATOM   4834 O O     . MET B 1 226 ? 5.279   -9.988  60.119 1.00 31.15 ?  226 MET B O     1 
ATOM   4835 C CB    . MET B 1 226 ? 3.206   -12.507 59.414 1.00 15.48 ?  226 MET B CB    1 
ATOM   4836 C CG    . MET B 1 226 ? 2.510   -13.769 59.860 1.00 20.72 ?  226 MET B CG    1 
ATOM   4837 S SD    . MET B 1 226 ? 0.731   -13.592 59.882 1.00 24.93 ?  226 MET B SD    1 
ATOM   4838 C CE    . MET B 1 226 ? 0.318   -15.287 59.474 1.00 15.60 ?  226 MET B CE    1 
ATOM   4839 N N     . ALA B 1 227 ? 5.742   -11.232 58.289 1.00 23.40 ?  227 ALA B N     1 
ATOM   4840 C CA    . ALA B 1 227 ? 6.408   -10.148 57.591 1.00 16.82 ?  227 ALA B CA    1 
ATOM   4841 C C     . ALA B 1 227 ? 6.649   -10.548 56.147 1.00 31.29 ?  227 ALA B C     1 
ATOM   4842 O O     . ALA B 1 227 ? 6.798   -11.739 55.852 1.00 45.88 ?  227 ALA B O     1 
ATOM   4843 C CB    . ALA B 1 227 ? 7.729   -9.798  58.267 1.00 22.65 ?  227 ALA B CB    1 
ATOM   4844 N N     . PRO B 1 228 ? 6.680   -9.591  55.222 1.00 25.42 ?  228 PRO B N     1 
ATOM   4845 C CA    . PRO B 1 228 ? 7.171   -9.866  53.869 1.00 28.58 ?  228 PRO B CA    1 
ATOM   4846 C C     . PRO B 1 228 ? 8.683   -9.761  53.741 1.00 40.63 ?  228 PRO B C     1 
ATOM   4847 O O     . PRO B 1 228 ? 9.205   -9.895  52.631 1.00 45.28 ?  228 PRO B O     1 
ATOM   4848 C CB    . PRO B 1 228 ? 6.487   -8.777  53.038 1.00 14.92 ?  228 PRO B CB    1 
ATOM   4849 C CG    . PRO B 1 228 ? 6.337   -7.655  53.966 1.00 10.94 ?  228 PRO B CG    1 
ATOM   4850 C CD    . PRO B 1 228 ? 6.133   -8.230  55.342 1.00 18.70 ?  228 PRO B CD    1 
ATOM   4851 N N     . SER B 1 229 ? 9.390   -9.491  54.838 1.00 39.93 ?  229 SER B N     1 
ATOM   4852 C CA    . SER B 1 229 ? 10.810  -9.178  54.747 1.00 36.83 ?  229 SER B CA    1 
ATOM   4853 C C     . SER B 1 229 ? 11.602  -10.357 54.192 1.00 38.56 ?  229 SER B C     1 
ATOM   4854 O O     . SER B 1 229 ? 12.449  -10.183 53.307 1.00 35.89 ?  229 SER B O     1 
ATOM   4855 C CB    . SER B 1 229 ? 11.325  -8.767  56.130 1.00 30.09 ?  229 SER B CB    1 
ATOM   4856 O OG    . SER B 1 229 ? 10.660  -7.601  56.592 1.00 34.77 ?  229 SER B OG    1 
HETATM 4857 N N1    . LLP B 1 230 ? 12.354  -15.861 62.822 1.00 6.69  ?  230 LLP B N1    1 
HETATM 4858 C C2    . LLP B 1 230 ? 12.686  -16.753 61.884 1.00 12.30 ?  230 LLP B C2    1 
HETATM 4859 C "C2'" . LLP B 1 230 ? 12.140  -18.189 61.858 1.00 9.52  ?  230 LLP B "C2'" 1 
HETATM 4860 C C3    . LLP B 1 230 ? 13.537  -16.402 60.843 1.00 21.72 ?  230 LLP B C3    1 
HETATM 4861 O O3    . LLP B 1 230 ? 13.802  -17.400 59.896 1.00 19.39 ?  230 LLP B O3    1 
HETATM 4862 C C4    . LLP B 1 230 ? 14.075  -15.085 60.808 1.00 11.10 ?  230 LLP B C4    1 
HETATM 4863 C "C4'" . LLP B 1 230 ? 15.061  -14.619 59.679 1.00 18.04 ?  230 LLP B "C4'" 1 
HETATM 4864 C C5    . LLP B 1 230 ? 13.749  -14.183 61.832 1.00 21.89 ?  230 LLP B C5    1 
HETATM 4865 C C6    . LLP B 1 230 ? 12.836  -14.614 62.821 1.00 19.16 ?  230 LLP B C6    1 
HETATM 4866 C "C5'" . LLP B 1 230 ? 14.289  -12.703 61.807 1.00 34.19 ?  230 LLP B "C5'" 1 
HETATM 4867 O OP4   . LLP B 1 230 ? 13.484  -12.016 60.897 1.00 44.66 ?  230 LLP B OP4   1 
HETATM 4868 P P     . LLP B 1 230 ? 13.718  -10.376 60.656 1.00 45.78 ?  230 LLP B P     1 
HETATM 4869 O OP1   . LLP B 1 230 ? 15.113  -10.168 60.171 1.00 39.44 ?  230 LLP B OP1   1 
HETATM 4870 O OP2   . LLP B 1 230 ? 13.483  -9.627  61.966 1.00 46.64 -1 230 LLP B OP2   1 
HETATM 4871 O OP3   . LLP B 1 230 ? 12.786  -9.878  59.593 1.00 37.84 -1 230 LLP B OP3   1 
HETATM 4872 N N     . LLP B 1 230 ? 11.319  -11.573 54.668 1.00 39.43 ?  230 LLP B N     1 
HETATM 4873 C CA    . LLP B 1 230 ? 12.047  -12.734 54.170 1.00 35.68 ?  230 LLP B CA    1 
HETATM 4874 C CB    . LLP B 1 230 ? 11.995  -13.852 55.202 1.00 31.71 ?  230 LLP B CB    1 
HETATM 4875 C CG    . LLP B 1 230 ? 12.889  -13.596 56.401 1.00 29.61 ?  230 LLP B CG    1 
HETATM 4876 C CD    . LLP B 1 230 ? 14.284  -14.114 56.149 1.00 24.01 ?  230 LLP B CD    1 
HETATM 4877 C CE    . LLP B 1 230 ? 15.197  -13.848 57.317 1.00 19.66 ?  230 LLP B CE    1 
HETATM 4878 N NZ    . LLP B 1 230 ? 14.722  -14.449 58.590 1.00 14.80 1  230 LLP B NZ    1 
HETATM 4879 C C     . LLP B 1 230 ? 11.498  -13.208 52.831 1.00 44.59 ?  230 LLP B C     1 
HETATM 4880 O O     . LLP B 1 230 ? 12.269  -13.569 51.935 1.00 52.29 ?  230 LLP B O     1 
ATOM   4881 N N     . THR B 1 231 ? 10.175  -13.175 52.669 1.00 37.31 ?  231 THR B N     1 
ATOM   4882 C CA    . THR B 1 231 ? 9.542   -13.710 51.468 1.00 24.36 ?  231 THR B CA    1 
ATOM   4883 C C     . THR B 1 231 ? 9.937   -12.937 50.220 1.00 24.92 ?  231 THR B C     1 
ATOM   4884 O O     . THR B 1 231 ? 10.214  -13.523 49.167 1.00 27.37 ?  231 THR B O     1 
ATOM   4885 C CB    . THR B 1 231 ? 8.034   -13.661 51.628 1.00 18.22 ?  231 THR B CB    1 
ATOM   4886 O OG1   . THR B 1 231 ? 7.642   -14.536 52.692 1.00 23.80 ?  231 THR B OG1   1 
ATOM   4887 C CG2   . THR B 1 231 ? 7.385   -14.072 50.328 1.00 22.15 ?  231 THR B CG2   1 
ATOM   4888 N N     . PHE B 1 232 ? 9.933   -11.615 50.302 1.00 20.70 ?  232 PHE B N     1 
ATOM   4889 C CA    . PHE B 1 232 ? 10.163  -10.787 49.134 1.00 24.10 ?  232 PHE B CA    1 
ATOM   4890 C C     . PHE B 1 232 ? 11.550  -10.174 49.137 1.00 26.37 ?  232 PHE B C     1 
ATOM   4891 O O     . PHE B 1 232 ? 11.867  -9.397  48.235 1.00 34.16 ?  232 PHE B O     1 
ATOM   4892 C CB    . PHE B 1 232 ? 9.090   -9.696  49.044 1.00 24.79 ?  232 PHE B CB    1 
ATOM   4893 C CG    . PHE B 1 232 ? 7.704   -10.228 48.861 1.00 17.59 ?  232 PHE B CG    1 
ATOM   4894 C CD1   . PHE B 1 232 ? 7.248   -10.580 47.610 1.00 19.30 ?  232 PHE B CD1   1 
ATOM   4895 C CD2   . PHE B 1 232 ? 6.860   -10.388 49.944 1.00 23.36 ?  232 PHE B CD2   1 
ATOM   4896 C CE1   . PHE B 1 232 ? 5.971   -11.071 47.443 1.00 29.34 ?  232 PHE B CE1   1 
ATOM   4897 C CE2   . PHE B 1 232 ? 5.584   -10.889 49.779 1.00 14.17 ?  232 PHE B CE2   1 
ATOM   4898 C CZ    . PHE B 1 232 ? 5.143   -11.230 48.530 1.00 19.44 ?  232 PHE B CZ    1 
ATOM   4899 N N     . ASN B 1 233 ? 12.389  -10.543 50.108 1.00 30.41 ?  233 ASN B N     1 
ATOM   4900 C CA    . ASN B 1 233 ? 13.772  -10.072 50.223 1.00 30.49 ?  233 ASN B CA    1 
ATOM   4901 C C     . ASN B 1 233 ? 13.834  -8.559  50.428 1.00 40.80 ?  233 ASN B C     1 
ATOM   4902 O O     . ASN B 1 233 ? 14.588  -7.842  49.767 1.00 51.45 ?  233 ASN B O     1 
ATOM   4903 C CB    . ASN B 1 233 ? 14.601  -10.502 49.010 1.00 20.24 ?  233 ASN B CB    1 
ATOM   4904 C CG    . ASN B 1 233 ? 16.074  -10.625 49.327 1.00 20.33 ?  233 ASN B CG    1 
ATOM   4905 O OD1   . ASN B 1 233 ? 16.467  -10.766 50.484 1.00 17.90 ?  233 ASN B OD1   1 
ATOM   4906 N ND2   . ASN B 1 233 ? 16.898  -10.589 48.295 1.00 22.24 ?  233 ASN B ND2   1 
ATOM   4907 N N     . ILE B 1 234 ? 13.045  -8.081  51.388 1.00 37.64 ?  234 ILE B N     1 
ATOM   4908 C CA    . ILE B 1 234 ? 13.035  -6.674  51.766 1.00 18.12 ?  234 ILE B CA    1 
ATOM   4909 C C     . ILE B 1 234 ? 13.315  -6.575  53.262 1.00 16.33 ?  234 ILE B C     1 
ATOM   4910 O O     . ILE B 1 234 ? 12.751  -5.732  53.968 1.00 24.25 ?  234 ILE B O     1 
ATOM   4911 C CB    . ILE B 1 234 ? 11.703  -6.010  51.379 1.00 14.98 ?  234 ILE B CB    1 
ATOM   4912 C CG1   . ILE B 1 234 ? 10.534  -6.648  52.127 1.00 23.69 ?  234 ILE B CG1   1 
ATOM   4913 C CG2   . ILE B 1 234 ? 11.488  -6.139  49.891 1.00 12.33 ?  234 ILE B CG2   1 
ATOM   4914 C CD1   . ILE B 1 234 ? 9.295   -5.782  52.177 1.00 30.14 ?  234 ILE B CD1   1 
ATOM   4915 N N     . ALA B 1 235 ? 14.180  -7.457  53.760 1.00 18.79 ?  235 ALA B N     1 
ATOM   4916 C CA    . ALA B 1 235 ? 14.500  -7.469  55.180 1.00 19.34 ?  235 ALA B CA    1 
ATOM   4917 C C     . ALA B 1 235 ? 15.274  -6.225  55.615 1.00 31.70 ?  235 ALA B C     1 
ATOM   4918 O O     . ALA B 1 235 ? 15.388  -5.981  56.820 1.00 41.53 ?  235 ALA B O     1 
ATOM   4919 C CB    . ALA B 1 235 ? 15.255  -8.754  55.529 1.00 13.41 ?  235 ALA B CB    1 
ATOM   4920 N N     . GLY B 1 236 ? 15.821  -5.445  54.676 1.00 23.92 ?  236 GLY B N     1 
ATOM   4921 C CA    . GLY B 1 236 ? 16.374  -4.152  55.018 1.00 27.09 ?  236 GLY B CA    1 
ATOM   4922 C C     . GLY B 1 236 ? 15.347  -3.040  55.113 1.00 27.97 ?  236 GLY B C     1 
ATOM   4923 O O     . GLY B 1 236 ? 15.684  -1.905  55.455 1.00 31.72 ?  236 GLY B O     1 
ATOM   4924 N N     . LEU B 1 237 ? 14.089  -3.325  54.805 1.00 24.46 ?  237 LEU B N     1 
ATOM   4925 C CA    . LEU B 1 237 ? 13.049  -2.314  54.908 1.00 25.12 ?  237 LEU B CA    1 
ATOM   4926 C C     . LEU B 1 237 ? 12.313  -2.359  56.234 1.00 25.32 ?  237 LEU B C     1 
ATOM   4927 O O     . LEU B 1 237 ? 11.512  -1.466  56.496 1.00 32.56 ?  237 LEU B O     1 
ATOM   4928 C CB    . LEU B 1 237 ? 12.048  -2.447  53.758 1.00 17.24 ?  237 LEU B CB    1 
ATOM   4929 C CG    . LEU B 1 237 ? 12.715  -2.432  52.380 1.00 20.52 ?  237 LEU B CG    1 
ATOM   4930 C CD1   . LEU B 1 237 ? 11.733  -2.065  51.300 1.00 18.62 ?  237 LEU B CD1   1 
ATOM   4931 C CD2   . LEU B 1 237 ? 13.918  -1.489  52.339 1.00 23.75 ?  237 LEU B CD2   1 
ATOM   4932 N N     . GLN B 1 238 ? 12.502  -3.409  57.031 1.00 19.15 ?  238 GLN B N     1 
ATOM   4933 C CA    . GLN B 1 238 ? 12.017  -3.467  58.413 1.00 19.97 ?  238 GLN B CA    1 
ATOM   4934 C C     . GLN B 1 238 ? 10.496  -3.280  58.519 1.00 21.12 ?  238 GLN B C     1 
ATOM   4935 O O     . GLN B 1 238 ? 10.010  -2.366  59.188 1.00 18.20 ?  238 GLN B O     1 
ATOM   4936 C CB    . GLN B 1 238 ? 12.757  -2.462  59.290 1.00 5.16  ?  238 GLN B CB    1 
ATOM   4937 C CG    . GLN B 1 238 ? 14.199  -2.843  59.553 1.00 12.62 ?  238 GLN B CG    1 
ATOM   4938 C CD    . GLN B 1 238 ? 15.037  -1.690  60.076 1.00 21.54 ?  238 GLN B CD    1 
ATOM   4939 O OE1   . GLN B 1 238 ? 14.699  -0.525  59.880 1.00 26.60 ?  238 GLN B OE1   1 
ATOM   4940 N NE2   . GLN B 1 238 ? 16.142  -2.013  60.734 1.00 21.27 ?  238 GLN B NE2   1 
ATOM   4941 N N     . ALA B 1 239 ? 9.747   -4.178  57.867 1.00 24.59 ?  239 ALA B N     1 
ATOM   4942 C CA    . ALA B 1 239 ? 8.288   -4.255  57.995 1.00 16.27 ?  239 ALA B CA    1 
ATOM   4943 C C     . ALA B 1 239 ? 7.894   -5.541  58.704 1.00 24.57 ?  239 ALA B C     1 
ATOM   4944 O O     . ALA B 1 239 ? 8.387   -6.620  58.361 1.00 27.51 ?  239 ALA B O     1 
ATOM   4945 C CB    . ALA B 1 239 ? 7.588   -4.212  56.636 1.00 7.40  ?  239 ALA B CB    1 
ATOM   4946 N N     . SER B 1 240 ? 7.013   -5.431  59.688 1.00 22.70 ?  240 SER B N     1 
ATOM   4947 C CA    . SER B 1 240 ? 6.517   -6.623  60.351 1.00 11.59 ?  240 SER B CA    1 
ATOM   4948 C C     . SER B 1 240 ? 5.101   -6.368  60.845 1.00 9.33  ?  240 SER B C     1 
ATOM   4949 O O     . SER B 1 240 ? 4.739   -5.244  61.170 1.00 17.52 ?  240 SER B O     1 
ATOM   4950 C CB    . SER B 1 240 ? 7.445   -7.031  61.486 1.00 11.09 ?  240 SER B CB    1 
ATOM   4951 O OG    . SER B 1 240 ? 8.663   -7.463  60.931 1.00 17.58 ?  240 SER B OG    1 
ATOM   4952 N N     . ILE B 1 241 ? 4.257   -7.375  60.817 1.00 31.00 ?  241 ILE B N     1 
ATOM   4953 C CA    . ILE B 1 241 ? 2.846   -7.306  61.299 1.00 30.34 ?  241 ILE B CA    1 
ATOM   4954 C C     . ILE B 1 241 ? 2.734   -8.369  62.369 1.00 38.41 ?  241 ILE B C     1 
ATOM   4955 O O     . ILE B 1 241 ? 3.209   -9.443  62.121 1.00 41.52 ?  241 ILE B O     1 
ATOM   4956 C CB    . ILE B 1 241 ? 1.832   -7.618  60.182 1.00 21.86 ?  241 ILE B CB    1 
ATOM   4957 C CG1   . ILE B 1 241 ? 1.981   -6.686  58.987 1.00 20.96 ?  241 ILE B CG1   1 
ATOM   4958 C CG2   . ILE B 1 241 ? 0.409   -7.665  60.695 1.00 14.18 ?  241 ILE B CG2   1 
ATOM   4959 C CD1   . ILE B 1 241 ? 2.608   -7.363  57.828 1.00 10.46 ?  241 ILE B CD1   1 
ATOM   4960 N N     . ILE B 1 242 ? 2.286   -8.030  63.552 1.00 32.17 ?  242 ILE B N     1 
ATOM   4961 C CA    . ILE B 1 242 ? 2.000   -8.955  64.637 1.00 18.90 ?  242 ILE B CA    1 
ATOM   4962 C C     . ILE B 1 242 ? 0.494   -8.937  64.846 1.00 30.05 ?  242 ILE B C     1 
ATOM   4963 O O     . ILE B 1 242 ? -0.106  -7.862  64.985 1.00 31.89 ?  242 ILE B O     1 
ATOM   4964 C CB    . ILE B 1 242 ? 2.751   -8.566  65.921 1.00 8.17  ?  242 ILE B CB    1 
ATOM   4965 C CG1   . ILE B 1 242 ? 4.140   -8.007  65.597 1.00 5.95  ?  242 ILE B CG1   1 
ATOM   4966 C CG2   . ILE B 1 242 ? 2.852   -9.716  66.854 1.00 6.36  ?  242 ILE B CG2   1 
ATOM   4967 C CD1   . ILE B 1 242 ? 5.024   -8.904  64.801 1.00 5.67  ?  242 ILE B CD1   1 
ATOM   4968 N N     . ILE B 1 243 ? -0.116  -10.117 64.859 1.00 39.29 ?  243 ILE B N     1 
ATOM   4969 C CA    . ILE B 1 243 ? -1.561  -10.270 64.974 1.00 6.97  ?  243 ILE B CA    1 
ATOM   4970 C C     . ILE B 1 243 ? -1.871  -10.867 66.338 1.00 6.85  ?  243 ILE B C     1 
ATOM   4971 O O     . ILE B 1 243 ? -1.304  -11.896 66.714 1.00 23.07 ?  243 ILE B O     1 
ATOM   4972 C CB    . ILE B 1 243 ? -2.101  -11.119 63.821 1.00 7.58  ?  243 ILE B CB    1 
ATOM   4973 C CG1   . ILE B 1 243 ? -1.758  -10.420 62.510 1.00 7.73  ?  243 ILE B CG1   1 
ATOM   4974 C CG2   . ILE B 1 243 ? -3.599  -11.286 63.927 1.00 35.70 ?  243 ILE B CG2   1 
ATOM   4975 C CD1   . ILE B 1 243 ? -1.944  -11.228 61.311 1.00 8.29  ?  243 ILE B CD1   1 
ATOM   4976 N N     . ILE B 1 244 ? -2.636  -10.163 67.133 1.00 6.83  ?  244 ILE B N     1 
ATOM   4977 C CA    . ILE B 1 244 ? -2.941  -10.598 68.512 1.00 8.01  ?  244 ILE B CA    1 
ATOM   4978 C C     . ILE B 1 244 ? -4.475  -10.550 68.669 1.00 9.35  ?  244 ILE B C     1 
ATOM   4979 O O     . ILE B 1 244 ? -4.920  -9.514  68.908 1.00 10.89 ?  244 ILE B O     1 
ATOM   4980 C CB    . ILE B 1 244 ? -2.184  -9.800  69.595 1.00 11.12 ?  244 ILE B CB    1 
ATOM   4981 C CG1   . ILE B 1 244 ? -0.801  -9.342  69.126 1.00 10.20 ?  244 ILE B CG1   1 
ATOM   4982 C CG2   . ILE B 1 244 ? -2.143  -10.558 70.911 1.00 6.05  ?  244 ILE B CG2   1 
ATOM   4983 C CD1   . ILE B 1 244 ? 0.018   -8.672  70.178 1.00 5.27  ?  244 ILE B CD1   1 
ATOM   4984 N N     . PRO B 1 245 ? -5.289  -11.623 68.493 1.00 9.05  ?  245 PRO B N     1 
ATOM   4985 C CA    . PRO B 1 245 ? -6.748  -11.544 68.680 1.00 12.37 ?  245 PRO B CA    1 
ATOM   4986 C C     . PRO B 1 245 ? -7.178  -11.153 70.091 1.00 7.81  ?  245 PRO B C     1 
ATOM   4987 O O     . PRO B 1 245 ? -8.222  -10.510 70.244 1.00 11.89 ?  245 PRO B O     1 
ATOM   4988 C CB    . PRO B 1 245 ? -7.217  -12.957 68.301 1.00 20.23 ?  245 PRO B CB    1 
ATOM   4989 C CG    . PRO B 1 245 ? -6.190  -13.458 67.397 1.00 11.25 ?  245 PRO B CG    1 
ATOM   4990 C CD    . PRO B 1 245 ? -4.890  -12.902 67.891 1.00 7.82  ?  245 PRO B CD    1 
ATOM   4991 N N     . ASN B 1 246 ? -6.462  -11.582 71.132 1.00 7.46  ?  246 ASN B N     1 
ATOM   4992 C CA    . ASN B 1 246 ? -6.827  -11.238 72.501 1.00 7.27  ?  246 ASN B CA    1 
ATOM   4993 C C     . ASN B 1 246 ? -6.513  -9.772  72.758 1.00 34.84 ?  246 ASN B C     1 
ATOM   4994 O O     . ASN B 1 246 ? -5.349  -9.345  72.697 1.00 40.58 ?  246 ASN B O     1 
ATOM   4995 C CB    . ASN B 1 246 ? -6.105  -12.156 73.479 1.00 7.06  ?  246 ASN B CB    1 
ATOM   4996 C CG    . ASN B 1 246 ? -6.435  -11.863 74.942 1.00 19.29 ?  246 ASN B CG    1 
ATOM   4997 O OD1   . ASN B 1 246 ? -6.991  -10.820 75.283 1.00 22.08 ?  246 ASN B OD1   1 
ATOM   4998 N ND2   . ASN B 1 246 ? -6.091  -12.809 75.820 1.00 19.99 ?  246 ASN B ND2   1 
ATOM   4999 N N     . GLU B 1 247 ? -7.565  -9.006  73.044 1.00 42.39 ?  247 GLU B N     1 
ATOM   5000 C CA    . GLU B 1 247 ? -7.409  -7.582  73.294 1.00 42.41 ?  247 GLU B CA    1 
ATOM   5001 C C     . GLU B 1 247 ? -6.544  -7.331  74.526 1.00 25.44 ?  247 GLU B C     1 
ATOM   5002 O O     . GLU B 1 247 ? -5.736  -6.396  74.542 1.00 22.39 ?  247 GLU B O     1 
ATOM   5003 C CB    . GLU B 1 247 ? -8.787  -6.943  73.429 1.00 36.58 ?  247 GLU B CB    1 
ATOM   5004 C CG    . GLU B 1 247 ? -8.766  -5.534  73.928 1.00 31.75 ?  247 GLU B CG    1 
ATOM   5005 C CD    . GLU B 1 247 ? -10.132 -4.930  73.902 1.00 34.89 ?  247 GLU B CD    1 
ATOM   5006 O OE1   . GLU B 1 247 ? -10.318 -3.913  73.198 1.00 23.16 ?  247 GLU B OE1   1 
ATOM   5007 O OE2   . GLU B 1 247 ? -11.024 -5.491  74.569 1.00 45.36 -1 247 GLU B OE2   1 
ATOM   5008 N N     . LYS B 1 248 ? -6.704  -8.163  75.566 1.00 10.86 ?  248 LYS B N     1 
ATOM   5009 C CA    . LYS B 1 248 ? -5.991  -7.969  76.829 1.00 5.81  ?  248 LYS B CA    1 
ATOM   5010 C C     . LYS B 1 248 ? -4.488  -8.228  76.695 1.00 25.95 ?  248 LYS B C     1 
ATOM   5011 O O     . LYS B 1 248 ? -3.681  -7.584  77.377 1.00 33.41 ?  248 LYS B O     1 
ATOM   5012 C CB    . LYS B 1 248 ? -6.589  -8.869  77.906 1.00 27.19 ?  248 LYS B CB    1 
ATOM   5013 C CG    . LYS B 1 248 ? -6.150  -8.493  79.307 1.00 29.36 ?  248 LYS B CG    1 
ATOM   5014 C CD    . LYS B 1 248 ? -6.725  -9.410  80.365 1.00 26.83 ?  248 LYS B CD    1 
ATOM   5015 C CE    . LYS B 1 248 ? -6.126  -9.103  81.716 1.00 17.53 ?  248 LYS B CE    1 
ATOM   5016 N NZ    . LYS B 1 248 ? -4.687  -9.459  81.738 1.00 31.35 1  248 LYS B NZ    1 
ATOM   5017 N N     . LEU B 1 249 ? -4.092  -9.196  75.868 1.00 17.87 ?  249 LEU B N     1 
ATOM   5018 C CA    . LEU B 1 249 ? -2.673  -9.400  75.583 1.00 14.62 ?  249 LEU B CA    1 
ATOM   5019 C C     . LEU B 1 249 ? -2.162  -8.346  74.601 1.00 22.48 ?  249 LEU B C     1 
ATOM   5020 O O     . LEU B 1 249 ? -1.012  -7.914  74.701 1.00 16.35 ?  249 LEU B O     1 
ATOM   5021 C CB    . LEU B 1 249 ? -2.420  -10.828 75.054 1.00 25.27 ?  249 LEU B CB    1 
ATOM   5022 C CG    . LEU B 1 249 ? -2.897  -12.030 75.930 1.00 31.39 ?  249 LEU B CG    1 
ATOM   5023 C CD1   . LEU B 1 249 ? -2.865  -13.421 75.242 1.00 6.13  ?  249 LEU B CD1   1 
ATOM   5024 C CD2   . LEU B 1 249 ? -2.208  -12.090 77.313 1.00 38.02 ?  249 LEU B CD2   1 
ATOM   5025 N N     . ARG B 1 250 ? -2.948  -7.901  73.628 1.00 33.57 ?  250 ARG B N     1 
ATOM   5026 C CA    . ARG B 1 250 ? -2.484  -6.917  72.610 1.00 21.81 ?  250 ARG B CA    1 
ATOM   5027 C C     . ARG B 1 250 ? -2.067  -5.609  73.285 1.00 16.72 ?  250 ARG B C     1 
ATOM   5028 O O     . ARG B 1 250 ? -1.109  -5.034  72.860 1.00 12.99 ?  250 ARG B O     1 
ATOM   5029 C CB    . ARG B 1 250 ? -3.559  -6.651  71.563 1.00 11.99 ?  250 ARG B CB    1 
ATOM   5030 C CG    . ARG B 1 250 ? -3.093  -6.052  70.251 1.00 17.94 ?  250 ARG B CG    1 
ATOM   5031 C CD    . ARG B 1 250 ? -4.056  -6.399  69.139 1.00 15.82 ?  250 ARG B CD    1 
ATOM   5032 N NE    . ARG B 1 250 ? -5.372  -5.779  69.175 1.00 16.68 ?  250 ARG B NE    1 
ATOM   5033 C CZ    . ARG B 1 250 ? -6.505  -6.397  69.495 1.00 31.15 ?  250 ARG B CZ    1 
ATOM   5034 N NH1   . ARG B 1 250 ? -6.501  -7.668  69.843 1.00 15.44 1  250 ARG B NH1   1 
ATOM   5035 N NH2   . ARG B 1 250 ? -7.643  -5.733  69.488 1.00 35.45 ?  250 ARG B NH2   1 
ATOM   5036 N N     . HIS B 1 251 ? -2.794  -5.207  74.314 1.00 17.65 ?  251 HIS B N     1 
ATOM   5037 C CA    . HIS B 1 251 ? -2.446  -3.960  74.983 1.00 21.85 ?  251 HIS B CA    1 
ATOM   5038 C C     . HIS B 1 251 ? -1.162  -4.079  75.793 1.00 25.73 ?  251 HIS B C     1 
ATOM   5039 O O     . HIS B 1 251 ? -0.416  -3.099  75.916 1.00 25.65 ?  251 HIS B O     1 
ATOM   5040 C CB    . HIS B 1 251 ? -3.598  -3.526  75.883 1.00 14.65 ?  251 HIS B CB    1 
ATOM   5041 C CG    . HIS B 1 251 ? -4.842  -3.188  75.129 1.00 14.04 ?  251 HIS B CG    1 
ATOM   5042 N ND1   . HIS B 1 251 ? -6.065  -3.017  75.745 1.00 15.66 ?  251 HIS B ND1   1 
ATOM   5043 C CD2   . HIS B 1 251 ? -5.052  -3.001  73.804 1.00 5.15  ?  251 HIS B CD2   1 
ATOM   5044 C CE1   . HIS B 1 251 ? -6.975  -2.730  74.832 1.00 12.76 ?  251 HIS B CE1   1 
ATOM   5045 N NE2   . HIS B 1 251 ? -6.386  -2.712  73.647 1.00 15.94 ?  251 HIS B NE2   1 
ATOM   5046 N N     . ALA B 1 252 ? -0.890  -5.251  76.371 1.00 24.28 ?  252 ALA B N     1 
ATOM   5047 C CA    . ALA B 1 252 ? 0.355   -5.410  77.115 1.00 14.87 ?  252 ALA B CA    1 
ATOM   5048 C C     . ALA B 1 252 ? 1.554   -5.510  76.175 1.00 22.92 ?  252 ALA B C     1 
ATOM   5049 O O     . ALA B 1 252 ? 2.673   -5.162  76.564 1.00 21.36 ?  252 ALA B O     1 
ATOM   5050 C CB    . ALA B 1 252 ? 0.268   -6.615  78.044 1.00 12.09 ?  252 ALA B CB    1 
ATOM   5051 N N     . PHE B 1 253 ? 1.350   -6.024  74.961 1.00 21.43 ?  253 PHE B N     1 
ATOM   5052 C CA    . PHE B 1 253 ? 2.391   -5.969  73.938 1.00 20.20 ?  253 PHE B CA    1 
ATOM   5053 C C     . PHE B 1 253 ? 2.659   -4.536  73.515 1.00 26.63 ?  253 PHE B C     1 
ATOM   5054 O O     . PHE B 1 253 ? 3.814   -4.124  73.376 1.00 52.82 ?  253 PHE B O     1 
ATOM   5055 C CB    . PHE B 1 253 ? 1.982   -6.800  72.721 1.00 18.84 ?  253 PHE B CB    1 
ATOM   5056 C CG    . PHE B 1 253 ? 3.005   -6.815  71.603 1.00 14.98 ?  253 PHE B CG    1 
ATOM   5057 C CD1   . PHE B 1 253 ? 3.030   -5.824  70.631 1.00 12.61 ?  253 PHE B CD1   1 
ATOM   5058 C CD2   . PHE B 1 253 ? 3.923   -7.847  71.510 1.00 17.08 ?  253 PHE B CD2   1 
ATOM   5059 C CE1   . PHE B 1 253 ? 3.960   -5.861  69.600 1.00 8.29  ?  253 PHE B CE1   1 
ATOM   5060 C CE2   . PHE B 1 253 ? 4.846   -7.886  70.484 1.00 7.42  ?  253 PHE B CE2   1 
ATOM   5061 C CZ    . PHE B 1 253 ? 4.869   -6.895  69.533 1.00 8.72  ?  253 PHE B CZ    1 
ATOM   5062 N N     . THR B 1 254 ? 1.596   -3.776  73.238 1.00 19.84 ?  254 THR B N     1 
ATOM   5063 C CA    . THR B 1 254 ? 1.775   -2.411  72.767 1.00 15.62 ?  254 THR B CA    1 
ATOM   5064 C C     . THR B 1 254 ? 2.325   -1.496  73.861 1.00 15.06 ?  254 THR B C     1 
ATOM   5065 O O     . THR B 1 254 ? 3.017   -0.524  73.551 1.00 5.14  ?  254 THR B O     1 
ATOM   5066 C CB    . THR B 1 254 ? 0.456   -1.873  72.194 1.00 20.71 ?  254 THR B CB    1 
ATOM   5067 O OG1   . THR B 1 254 ? -0.603  -2.021  73.150 1.00 25.69 ?  254 THR B OG1   1 
ATOM   5068 C CG2   . THR B 1 254 ? 0.086   -2.618  70.910 1.00 25.18 ?  254 THR B CG2   1 
ATOM   5069 N N     . ALA B 1 255 ? 2.071   -1.811  75.136 1.00 22.27 ?  255 ALA B N     1 
ATOM   5070 C CA    . ALA B 1 255 ? 2.688   -1.054  76.222 1.00 10.05 ?  255 ALA B CA    1 
ATOM   5071 C C     . ALA B 1 255 ? 4.195   -1.263  76.235 1.00 17.53 ?  255 ALA B C     1 
ATOM   5072 O O     . ALA B 1 255 ? 4.949   -0.322  76.507 1.00 35.14 ?  255 ALA B O     1 
ATOM   5073 C CB    . ALA B 1 255 ? 2.084   -1.449  77.569 1.00 2.89  ?  255 ALA B CB    1 
ATOM   5074 N N     . ILE B 1 256 ? 4.654   -2.484  75.928 1.00 10.54 ?  256 ILE B N     1 
ATOM   5075 C CA    . ILE B 1 256 ? 6.091   -2.849  75.935 1.00 2.60  ?  256 ILE B CA    1 
ATOM   5076 C C     . ILE B 1 256 ? 6.722   -2.316  74.667 1.00 2.51  ?  256 ILE B C     1 
ATOM   5077 O O     . ILE B 1 256 ? 7.890   -2.142  74.684 1.00 28.28 ?  256 ILE B O     1 
ATOM   5078 C CB    . ILE B 1 256 ? 6.361   -4.345  76.246 1.00 26.28 ?  256 ILE B CB    1 
ATOM   5079 C CG1   . ILE B 1 256 ? 5.673   -4.827  77.523 1.00 21.39 ?  256 ILE B CG1   1 
ATOM   5080 C CG2   . ILE B 1 256 ? 7.841   -4.691  76.285 1.00 17.71 ?  256 ILE B CG2   1 
ATOM   5081 C CD1   . ILE B 1 256 ? 5.878   -3.940  78.716 1.00 18.83 ?  256 ILE B CD1   1 
ATOM   5082 N N     . GLN B 1 257 ? 5.968   -2.014  73.636 1.00 2.66  ?  257 GLN B N     1 
ATOM   5083 C CA    . GLN B 1 257 ? 6.512   -1.316  72.450 1.00 2.58  ?  257 GLN B CA    1 
ATOM   5084 C C     . GLN B 1 257 ? 6.511   0.208   72.677 1.00 8.57  ?  257 GLN B C     1 
ATOM   5085 O O     . GLN B 1 257 ? 7.447   0.844   72.225 1.00 16.27 ?  257 GLN B O     1 
ATOM   5086 C CB    . GLN B 1 257 ? 5.594   -1.516  71.279 1.00 2.82  ?  257 GLN B CB    1 
ATOM   5087 C CG    . GLN B 1 257 ? 5.570   -2.888  70.674 1.00 18.25 ?  257 GLN B CG    1 
ATOM   5088 C CD    . GLN B 1 257 ? 4.828   -2.718  69.380 1.00 8.78  ?  257 GLN B CD    1 
ATOM   5089 O OE1   . GLN B 1 257 ? 3.703   -2.241  69.359 1.00 21.91 ?  257 GLN B OE1   1 
ATOM   5090 N NE2   . GLN B 1 257 ? 5.476   -3.080  68.294 1.00 3.42  ?  257 GLN B NE2   1 
ATOM   5091 N N     . TYR B 1 258 ? 5.601   0.801   73.446 1.00 22.12 ?  258 TYR B N     1 
ATOM   5092 C CA    . TYR B 1 258 ? 5.459   2.279   73.604 1.00 29.35 ?  258 TYR B CA    1 
ATOM   5093 C C     . TYR B 1 258 ? 6.468   2.879   74.583 1.00 24.64 ?  258 TYR B C     1 
ATOM   5094 O O     . TYR B 1 258 ? 6.881   4.013   74.361 1.00 28.74 ?  258 TYR B O     1 
ATOM   5095 C CB    . TYR B 1 258 ? 4.047   2.640   74.088 1.00 19.27 ?  258 TYR B CB    1 
ATOM   5096 C CG    . TYR B 1 258 ? 3.800   4.102   74.354 1.00 9.22  ?  258 TYR B CG    1 
ATOM   5097 C CD1   . TYR B 1 258 ? 3.692   5.005   73.313 1.00 2.17  ?  258 TYR B CD1   1 
ATOM   5098 C CD2   . TYR B 1 258 ? 3.681   4.579   75.646 1.00 2.02  ?  258 TYR B CD2   1 
ATOM   5099 C CE1   . TYR B 1 258 ? 3.482   6.350   73.548 1.00 2.03  ?  258 TYR B CE1   1 
ATOM   5100 C CE2   . TYR B 1 258 ? 3.464   5.920   75.896 1.00 4.26  ?  258 TYR B CE2   1 
ATOM   5101 C CZ    . TYR B 1 258 ? 3.365   6.806   74.844 1.00 1.88  ?  258 TYR B CZ    1 
ATOM   5102 O OH    . TYR B 1 258 ? 3.141   8.123   75.084 1.00 15.80 ?  258 TYR B OH    1 
ATOM   5103 N N     . ARG B 1 259 ? 6.804   2.143   75.631 1.00 20.30 ?  259 ARG B N     1 
ATOM   5104 C CA    . ARG B 1 259 ? 7.789   2.587   76.634 1.00 16.32 ?  259 ARG B CA    1 
ATOM   5105 C C     . ARG B 1 259 ? 9.240   2.328   76.205 1.00 27.18 ?  259 ARG B C     1 
ATOM   5106 O O     . ARG B 1 259 ? 10.085  2.377   77.063 1.00 1.70  ?  259 ARG B O     1 
ATOM   5107 C CB    . ARG B 1 259 ? 7.521   1.796   77.920 1.00 5.87  ?  259 ARG B CB    1 
ATOM   5108 C CG    . ARG B 1 259 ? 7.977   0.347   77.917 1.00 11.90 ?  259 ARG B CG    1 
ATOM   5109 C CD    . ARG B 1 259 ? 7.764   -0.380  79.215 1.00 13.42 ?  259 ARG B CD    1 
ATOM   5110 N NE    . ARG B 1 259 ? 8.658   -1.514  79.270 1.00 2.07  ?  259 ARG B NE    1 
ATOM   5111 C CZ    . ARG B 1 259 ? 8.735   -2.330  80.299 1.00 22.82 ?  259 ARG B CZ    1 
ATOM   5112 N NH1   . ARG B 1 259 ? 7.954   -2.142  81.344 1.00 19.23 1  259 ARG B NH1   1 
ATOM   5113 N NH2   . ARG B 1 259 ? 9.578   -3.338  80.282 1.00 38.26 ?  259 ARG B NH2   1 
ATOM   5114 N N     . GLN B 1 260 ? 9.470   2.079   74.916 1.00 38.15 ?  260 GLN B N     1 
ATOM   5115 C CA    . GLN B 1 260 ? 10.779  1.772   74.287 1.00 26.39 ?  260 GLN B CA    1 
ATOM   5116 C C     . GLN B 1 260 ? 10.801  2.780   73.155 1.00 31.72 ?  260 GLN B C     1 
ATOM   5117 O O     . GLN B 1 260 ? 11.668  2.652   72.322 1.00 5.61  ?  260 GLN B O     1 
ATOM   5118 C CB    . GLN B 1 260 ? 10.955  0.305   73.893 1.00 2.03  ?  260 GLN B CB    1 
ATOM   5119 C CG    . GLN B 1 260 ? 11.142  -0.657  75.049 1.00 2.06  ?  260 GLN B CG    1 
ATOM   5120 C CD    . GLN B 1 260 ? 11.044  -2.098  74.613 1.00 3.37  ?  260 GLN B CD    1 
ATOM   5121 O OE1   . GLN B 1 260 ? 11.067  -2.422  73.436 1.00 2.30  ?  260 GLN B OE1   1 
ATOM   5122 N NE2   . GLN B 1 260 ? 10.953  -2.990  75.578 1.00 10.77 ?  260 GLN B NE2   1 
ATOM   5123 N N     . GLY B 1 261 ? 9.758   3.622   73.098 1.00 1.84  ?  261 GLY B N     1 
ATOM   5124 C CA    . GLY B 1 261 ? 9.823   4.721   72.161 1.00 1.82  ?  261 GLY B CA    1 
ATOM   5125 C C     . GLY B 1 261 ? 9.507   4.383   70.724 1.00 1.94  ?  261 GLY B C     1 
ATOM   5126 O O     . GLY B 1 261 ? 9.728   5.227   69.845 1.00 1.97  ?  261 GLY B O     1 
ATOM   5127 N N     . PHE B 1 262 ? 9.004   3.179   70.453 1.00 5.34  ?  262 PHE B N     1 
ATOM   5128 C CA    . PHE B 1 262 ? 8.633   2.774   69.101 1.00 5.51  ?  262 PHE B CA    1 
ATOM   5129 C C     . PHE B 1 262 ? 7.308   3.424   68.738 1.00 27.78 ?  262 PHE B C     1 
ATOM   5130 O O     . PHE B 1 262 ? 6.341   3.353   69.503 1.00 20.91 ?  262 PHE B O     1 
ATOM   5131 C CB    . PHE B 1 262 ? 8.512   1.253   69.013 1.00 6.90  ?  262 PHE B CB    1 
ATOM   5132 C CG    . PHE B 1 262 ? 8.056   0.754   67.665 1.00 9.96  ?  262 PHE B CG    1 
ATOM   5133 C CD1   . PHE B 1 262 ? 8.859   0.900   66.566 1.00 13.31 ?  262 PHE B CD1   1 
ATOM   5134 C CD2   . PHE B 1 262 ? 6.840   0.123   67.507 1.00 4.97  ?  262 PHE B CD2   1 
ATOM   5135 C CE1   . PHE B 1 262 ? 8.457   0.445   65.336 1.00 21.34 ?  262 PHE B CE1   1 
ATOM   5136 C CE2   . PHE B 1 262 ? 6.445   -0.327  66.275 1.00 9.35  ?  262 PHE B CE2   1 
ATOM   5137 C CZ    . PHE B 1 262 ? 7.256   -0.164  65.190 1.00 3.07  ?  262 PHE B CZ    1 
ATOM   5138 N N     . HIS B 1 263 ? 7.255   4.037   67.558 1.00 37.51 ?  263 HIS B N     1 
ATOM   5139 C CA    . HIS B 1 263 ? 6.078   4.788   67.137 1.00 14.74 ?  263 HIS B CA    1 
ATOM   5140 C C     . HIS B 1 263 ? 5.640   4.432   65.729 1.00 15.75 ?  263 HIS B C     1 
ATOM   5141 O O     . HIS B 1 263 ? 5.015   5.257   65.063 1.00 36.02 ?  263 HIS B O     1 
ATOM   5142 C CB    . HIS B 1 263 ? 6.337   6.292   67.188 1.00 2.21  ?  263 HIS B CB    1 
ATOM   5143 C CG    . HIS B 1 263 ? 6.889   6.773   68.492 1.00 14.30 ?  263 HIS B CG    1 
ATOM   5144 N ND1   . HIS B 1 263 ? 6.329   6.444   69.707 1.00 9.66  ?  263 HIS B ND1   1 
ATOM   5145 C CD2   . HIS B 1 263 ? 7.958   7.562   68.770 1.00 16.54 ?  263 HIS B CD2   1 
ATOM   5146 C CE1   . HIS B 1 263 ? 7.026   7.007   70.678 1.00 21.55 ?  263 HIS B CE1   1 
ATOM   5147 N NE2   . HIS B 1 263 ? 8.019   7.691   70.136 1.00 19.11 ?  263 HIS B NE2   1 
ATOM   5148 N N     . GLY B 1 264 ? 5.972   3.252   65.251 1.00 13.70 ?  264 GLY B N     1 
ATOM   5149 C CA    . GLY B 1 264 ? 5.620   2.854   63.908 1.00 9.86  ?  264 GLY B CA    1 
ATOM   5150 C C     . GLY B 1 264 ? 6.845   2.742   63.024 1.00 9.90  ?  264 GLY B C     1 
ATOM   5151 O O     . GLY B 1 264 ? 7.981   2.946   63.447 1.00 10.03 ?  264 GLY B O     1 
ATOM   5152 N N     . LEU B 1 265 ? 6.576   2.434   61.763 1.00 20.98 ?  265 LEU B N     1 
ATOM   5153 C CA    . LEU B 1 265 ? 7.609   2.062   60.814 1.00 23.89 ?  265 LEU B CA    1 
ATOM   5154 C C     . LEU B 1 265 ? 7.996   3.238   59.932 1.00 36.89 ?  265 LEU B C     1 
ATOM   5155 O O     . LEU B 1 265 ? 7.331   4.276   59.891 1.00 53.92 ?  265 LEU B O     1 
ATOM   5156 C CB    . LEU B 1 265 ? 7.144   0.891   59.943 1.00 21.55 ?  265 LEU B CB    1 
ATOM   5157 C CG    . LEU B 1 265 ? 6.347   -0.218  60.613 1.00 10.61 ?  265 LEU B CG    1 
ATOM   5158 C CD1   . LEU B 1 265 ? 6.062   -1.300  59.594 1.00 15.29 ?  265 LEU B CD1   1 
ATOM   5159 C CD2   . LEU B 1 265 ? 7.119   -0.750  61.800 1.00 11.32 ?  265 LEU B CD2   1 
ATOM   5160 N N     . ASN B 1 266 ? 9.085   3.047   59.203 1.00 26.53 ?  266 ASN B N     1 
ATOM   5161 C CA    . ASN B 1 266 ? 9.613   4.082   58.338 1.00 25.01 ?  266 ASN B CA    1 
ATOM   5162 C C     . ASN B 1 266 ? 8.909   4.067   56.976 1.00 31.50 ?  266 ASN B C     1 
ATOM   5163 O O     . ASN B 1 266 ? 8.221   3.113   56.609 1.00 32.57 ?  266 ASN B O     1 
ATOM   5164 C CB    . ASN B 1 266 ? 11.140  3.935   58.214 1.00 11.97 ?  266 ASN B CB    1 
ATOM   5165 C CG    . ASN B 1 266 ? 11.570  2.706   57.443 1.00 12.27 ?  266 ASN B CG    1 
ATOM   5166 O OD1   . ASN B 1 266 ? 11.688  2.753   56.229 1.00 19.33 ?  266 ASN B OD1   1 
ATOM   5167 N ND2   . ASN B 1 266 ? 11.865  1.620   58.148 1.00 5.70  ?  266 ASN B ND2   1 
ATOM   5168 N N     . ILE B 1 267 ? 9.114   5.152   56.223 1.00 31.09 ?  267 ILE B N     1 
ATOM   5169 C CA    . ILE B 1 267 ? 8.392   5.411   54.972 1.00 21.21 ?  267 ILE B CA    1 
ATOM   5170 C C     . ILE B 1 267 ? 8.464   4.220   54.016 1.00 19.92 ?  267 ILE B C     1 
ATOM   5171 O O     . ILE B 1 267 ? 7.476   3.875   53.357 1.00 29.58 ?  267 ILE B O     1 
ATOM   5172 C CB    . ILE B 1 267 ? 8.936   6.697   54.321 1.00 11.48 ?  267 ILE B CB    1 
ATOM   5173 C CG1   . ILE B 1 267 ? 8.285   7.922   54.953 1.00 30.37 ?  267 ILE B CG1   1 
ATOM   5174 C CG2   . ILE B 1 267 ? 8.701   6.695   52.844 1.00 8.96  ?  267 ILE B CG2   1 
ATOM   5175 C CD1   . ILE B 1 267 ? 8.994   9.212   54.634 1.00 45.27 ?  267 ILE B CD1   1 
ATOM   5176 N N     . PHE B 1 268 ? 9.631   3.591   53.903 1.00 21.10 ?  268 PHE B N     1 
ATOM   5177 C CA    . PHE B 1 268 ? 9.805   2.521   52.918 1.00 25.99 ?  268 PHE B CA    1 
ATOM   5178 C C     . PHE B 1 268 ? 9.259   1.184   53.403 1.00 16.99 ?  268 PHE B C     1 
ATOM   5179 O O     . PHE B 1 268 ? 8.890   0.339   52.583 1.00 22.35 ?  268 PHE B O     1 
ATOM   5180 C CB    . PHE B 1 268 ? 11.282  2.389   52.559 1.00 21.51 ?  268 PHE B CB    1 
ATOM   5181 C CG    . PHE B 1 268 ? 11.881  3.668   52.074 1.00 17.12 ?  268 PHE B CG    1 
ATOM   5182 C CD1   . PHE B 1 268 ? 11.821  4.003   50.740 1.00 22.60 ?  268 PHE B CD1   1 
ATOM   5183 C CD2   . PHE B 1 268 ? 12.459  4.552   52.958 1.00 12.47 ?  268 PHE B CD2   1 
ATOM   5184 C CE1   . PHE B 1 268 ? 12.349  5.182   50.286 1.00 24.08 ?  268 PHE B CE1   1 
ATOM   5185 C CE2   . PHE B 1 268 ? 12.985  5.730   52.505 1.00 23.15 ?  268 PHE B CE2   1 
ATOM   5186 C CZ    . PHE B 1 268 ? 12.929  6.048   51.167 1.00 24.09 ?  268 PHE B CZ    1 
ATOM   5187 N N     . ALA B 1 269 ? 9.187   0.984   54.719 1.00 12.22 ?  269 ALA B N     1 
ATOM   5188 C CA    . ALA B 1 269 ? 8.500   -0.185  55.255 1.00 8.45  ?  269 ALA B CA    1 
ATOM   5189 C C     . ALA B 1 269 ? 7.008   -0.137  54.957 1.00 25.48 ?  269 ALA B C     1 
ATOM   5190 O O     . ALA B 1 269 ? 6.421   -1.138  54.536 1.00 39.61 ?  269 ALA B O     1 
ATOM   5191 C CB    . ALA B 1 269 ? 8.738   -0.287  56.761 1.00 6.91  ?  269 ALA B CB    1 
ATOM   5192 N N     . TYR B 1 270 ? 6.373   1.024   55.140 1.00 24.40 ?  270 TYR B N     1 
ATOM   5193 C CA    . TYR B 1 270 ? 4.958   1.118   54.802 1.00 27.80 ?  270 TYR B CA    1 
ATOM   5194 C C     . TYR B 1 270 ? 4.754   0.920   53.308 1.00 40.05 ?  270 TYR B C     1 
ATOM   5195 O O     . TYR B 1 270 ? 3.864   0.168   52.889 1.00 47.59 ?  270 TYR B O     1 
ATOM   5196 C CB    . TYR B 1 270 ? 4.377   2.463   55.256 1.00 25.59 ?  270 TYR B CB    1 
ATOM   5197 C CG    . TYR B 1 270 ? 4.144   2.562   56.746 1.00 7.47  ?  270 TYR B CG    1 
ATOM   5198 C CD1   . TYR B 1 270 ? 3.300   1.696   57.390 1.00 11.23 ?  270 TYR B CD1   1 
ATOM   5199 C CD2   . TYR B 1 270 ? 4.798   3.513   57.505 1.00 20.48 ?  270 TYR B CD2   1 
ATOM   5200 C CE1   . TYR B 1 270 ? 3.101   1.767   58.746 1.00 11.76 ?  270 TYR B CE1   1 
ATOM   5201 C CE2   . TYR B 1 270 ? 4.596   3.593   58.870 1.00 22.06 ?  270 TYR B CE2   1 
ATOM   5202 C CZ    . TYR B 1 270 ? 3.746   2.714   59.486 1.00 6.08  ?  270 TYR B CZ    1 
ATOM   5203 O OH    . TYR B 1 270 ? 3.534   2.778   60.843 1.00 5.42  ?  270 TYR B OH    1 
ATOM   5204 N N     . THR B 1 271 ? 5.594   1.552   52.486 1.00 32.84 ?  271 THR B N     1 
ATOM   5205 C CA    . THR B 1 271 ? 5.363   1.497   51.046 1.00 32.73 ?  271 THR B CA    1 
ATOM   5206 C C     . THR B 1 271 ? 5.573   0.094   50.494 1.00 29.75 ?  271 THR B C     1 
ATOM   5207 O O     . THR B 1 271 ? 4.766   -0.383  49.694 1.00 37.63 ?  271 THR B O     1 
ATOM   5208 C CB    . THR B 1 271 ? 6.280   2.481   50.321 1.00 35.72 ?  271 THR B CB    1 
ATOM   5209 O OG1   . THR B 1 271 ? 6.437   3.669   51.107 1.00 40.22 ?  271 THR B OG1   1 
ATOM   5210 C CG2   . THR B 1 271 ? 5.706   2.842   48.948 1.00 34.54 ?  271 THR B CG2   1 
ATOM   5211 N N     . ALA B 1 272 ? 6.622   -0.600  50.941 1.00 29.91 ?  272 ALA B N     1 
ATOM   5212 C CA    . ALA B 1 272 ? 6.917   -1.925  50.396 1.00 19.74 ?  272 ALA B CA    1 
ATOM   5213 C C     . ALA B 1 272 ? 5.895   -2.958  50.848 1.00 13.31 ?  272 ALA B C     1 
ATOM   5214 O O     . ALA B 1 272 ? 5.360   -3.708  50.028 1.00 15.34 ?  272 ALA B O     1 
ATOM   5215 C CB    . ALA B 1 272 ? 8.325   -2.358  50.804 1.00 16.93 ?  272 ALA B CB    1 
ATOM   5216 N N     . MET B 1 273 ? 5.564   -2.968  52.139 1.00 10.14 ?  273 MET B N     1 
ATOM   5217 C CA    . MET B 1 273 ? 4.606   -3.944  52.643 1.00 25.63 ?  273 MET B CA    1 
ATOM   5218 C C     . MET B 1 273 ? 3.249   -3.799  51.940 1.00 38.58 ?  273 MET B C     1 
ATOM   5219 O O     . MET B 1 273 ? 2.571   -4.799  51.683 1.00 47.58 ?  273 MET B O     1 
ATOM   5220 C CB    . MET B 1 273 ? 4.471   -3.799  54.166 1.00 31.62 ?  273 MET B CB    1 
ATOM   5221 C CG    . MET B 1 273 ? 3.510   -4.804  54.832 1.00 42.69 ?  273 MET B CG    1 
ATOM   5222 S SD    . MET B 1 273 ? 2.575   -4.218  56.273 1.00 30.40 ?  273 MET B SD    1 
ATOM   5223 C CE    . MET B 1 273 ? 3.913   -3.747  57.360 1.00 29.55 ?  273 MET B CE    1 
ATOM   5224 N N     . GLN B 1 274 ? 2.834   -2.565  51.621 1.00 31.50 ?  274 GLN B N     1 
ATOM   5225 C CA    . GLN B 1 274 ? 1.574   -2.361  50.901 1.00 34.95 ?  274 GLN B CA    1 
ATOM   5226 C C     . GLN B 1 274 ? 1.607   -2.938  49.487 1.00 30.57 ?  274 GLN B C     1 
ATOM   5227 O O     . GLN B 1 274 ? 0.611   -3.505  49.022 1.00 43.11 ?  274 GLN B O     1 
ATOM   5228 C CB    . GLN B 1 274 ? 1.212   -0.871  50.837 1.00 37.61 ?  274 GLN B CB    1 
ATOM   5229 C CG    . GLN B 1 274 ? -0.111  -0.609  50.113 1.00 33.39 ?  274 GLN B CG    1 
ATOM   5230 C CD    . GLN B 1 274 ? -0.501  0.854   50.050 1.00 42.29 ?  274 GLN B CD    1 
ATOM   5231 O OE1   . GLN B 1 274 ? -1.665  1.194   50.241 1.00 37.06 ?  274 GLN B OE1   1 
ATOM   5232 N NE2   . GLN B 1 274 ? 0.458   1.720   49.745 1.00 46.92 ?  274 GLN B NE2   1 
ATOM   5233 N N     . SER B 1 275 ? 2.716   -2.756  48.765 1.00 26.47 ?  275 SER B N     1 
ATOM   5234 C CA    . SER B 1 275 ? 2.813   -3.307  47.415 1.00 27.91 ?  275 SER B CA    1 
ATOM   5235 C C     . SER B 1 275 ? 3.021   -4.824  47.446 1.00 43.65 ?  275 SER B C     1 
ATOM   5236 O O     . SER B 1 275 ? 2.403   -5.560  46.664 1.00 40.45 ?  275 SER B O     1 
ATOM   5237 C CB    . SER B 1 275 ? 3.954   -2.621  46.664 1.00 23.92 ?  275 SER B CB    1 
ATOM   5238 O OG    . SER B 1 275 ? 4.100   -3.120  45.347 1.00 31.88 ?  275 SER B OG    1 
ATOM   5239 N N     . ALA B 1 276 ? 3.894   -5.306  48.346 1.00 42.16 ?  276 ALA B N     1 
ATOM   5240 C CA    . ALA B 1 276 ? 4.178   -6.736  48.461 1.00 30.38 ?  276 ALA B CA    1 
ATOM   5241 C C     . ALA B 1 276 ? 2.921   -7.537  48.733 1.00 29.22 ?  276 ALA B C     1 
ATOM   5242 O O     . ALA B 1 276 ? 2.803   -8.686  48.300 1.00 46.78 ?  276 ALA B O     1 
ATOM   5243 C CB    . ALA B 1 276 ? 5.199   -6.989  49.570 1.00 41.14 ?  276 ALA B CB    1 
ATOM   5244 N N     . TYR B 1 277 ? 1.977   -6.951  49.451 1.00 28.41 ?  277 TYR B N     1 
ATOM   5245 C CA    . TYR B 1 277 ? 0.765   -7.636  49.854 1.00 23.05 ?  277 TYR B CA    1 
ATOM   5246 C C     . TYR B 1 277 ? -0.397  -7.385  48.909 1.00 24.52 ?  277 TYR B C     1 
ATOM   5247 O O     . TYR B 1 277 ? -1.519  -7.796  49.213 1.00 33.39 ?  277 TYR B O     1 
ATOM   5248 C CB    . TYR B 1 277 ? 0.373   -7.210  51.259 1.00 22.81 ?  277 TYR B CB    1 
ATOM   5249 C CG    . TYR B 1 277 ? 1.163   -7.856  52.348 1.00 16.61 ?  277 TYR B CG    1 
ATOM   5250 C CD1   . TYR B 1 277 ? 2.000   -8.929  52.094 1.00 21.13 ?  277 TYR B CD1   1 
ATOM   5251 C CD2   . TYR B 1 277 ? 1.055   -7.407  53.639 1.00 19.32 ?  277 TYR B CD2   1 
ATOM   5252 C CE1   . TYR B 1 277 ? 2.713   -9.524  53.116 1.00 24.73 ?  277 TYR B CE1   1 
ATOM   5253 C CE2   . TYR B 1 277 ? 1.755   -7.989  54.645 1.00 14.70 ?  277 TYR B CE2   1 
ATOM   5254 C CZ    . TYR B 1 277 ? 2.580   -9.038  54.394 1.00 15.82 ?  277 TYR B CZ    1 
ATOM   5255 O OH    . TYR B 1 277 ? 3.255   -9.583  55.450 1.00 19.65 ?  277 TYR B OH    1 
ATOM   5256 N N     . THR B 1 278 ? -0.170  -6.693  47.793 1.00 21.36 ?  278 THR B N     1 
ATOM   5257 C CA    . THR B 1 278 ? -1.271  -6.408  46.880 1.00 39.61 ?  278 THR B CA    1 
ATOM   5258 C C     . THR B 1 278 ? -0.959  -6.852  45.456 1.00 48.07 ?  278 THR B C     1 
ATOM   5259 O O     . THR B 1 278 ? -1.777  -7.517  44.813 1.00 64.48 ?  278 THR B O     1 
ATOM   5260 C CB    . THR B 1 278 ? -1.638  -4.912  46.872 1.00 43.47 ?  278 THR B CB    1 
ATOM   5261 O OG1   . THR B 1 278 ? -0.465  -4.102  47.005 1.00 45.53 ?  278 THR B OG1   1 
ATOM   5262 C CG2   . THR B 1 278 ? -2.615  -4.578  47.986 1.00 43.48 ?  278 THR B CG2   1 
ATOM   5263 N N     . GLU B 1 279 ? 0.220   -6.504  44.956 1.00 41.30 ?  279 GLU B N     1 
ATOM   5264 C CA    . GLU B 1 279 ? 0.488   -6.567  43.528 1.00 42.40 ?  279 GLU B CA    1 
ATOM   5265 C C     . GLU B 1 279 ? 1.567   -7.573  43.162 1.00 45.39 ?  279 GLU B C     1 
ATOM   5266 O O     . GLU B 1 279 ? 2.026   -7.588  42.016 1.00 50.42 ?  279 GLU B O     1 
ATOM   5267 C CB    . GLU B 1 279 ? 0.880   -5.176  43.034 1.00 40.00 ?  279 GLU B CB    1 
ATOM   5268 C CG    . GLU B 1 279 ? 0.004   -4.058  43.598 1.00 41.34 ?  279 GLU B CG    1 
ATOM   5269 C CD    . GLU B 1 279 ? 0.617   -2.687  43.393 1.00 48.70 ?  279 GLU B CD    1 
ATOM   5270 O OE1   . GLU B 1 279 ? -0.118  -1.766  42.981 1.00 54.47 ?  279 GLU B OE1   1 
ATOM   5271 O OE2   . GLU B 1 279 ? 1.830   -2.526  43.663 1.00 43.39 -1 279 GLU B OE2   1 
ATOM   5272 N N     . CYS B 1 280 ? 1.983   -8.419  44.096 1.00 43.44 ?  280 CYS B N     1 
ATOM   5273 C CA    . CYS B 1 280 ? 3.154   -9.253  43.868 1.00 46.86 ?  280 CYS B CA    1 
ATOM   5274 C C     . CYS B 1 280 ? 2.816   -10.743 43.862 1.00 38.01 ?  280 CYS B C     1 
ATOM   5275 O O     . CYS B 1 280 ? 3.704   -11.582 44.026 1.00 46.70 ?  280 CYS B O     1 
ATOM   5276 C CB    . CYS B 1 280 ? 4.212   -8.896  44.914 1.00 55.98 ?  280 CYS B CB    1 
ATOM   5277 S SG    . CYS B 1 280 ? 4.469   -7.076  45.078 1.00 41.36 ?  280 CYS B SG    1 
ATOM   5278 N N     . ASN B 1 281 ? 1.545   -11.082 43.622 1.00 30.37 ?  281 ASN B N     1 
ATOM   5279 C CA    . ASN B 1 281 ? 1.065   -12.458 43.748 1.00 37.59 ?  281 ASN B CA    1 
ATOM   5280 C C     . ASN B 1 281 ? 1.713   -13.407 42.744 1.00 42.99 ?  281 ASN B C     1 
ATOM   5281 O O     . ASN B 1 281 ? 1.985   -14.570 43.071 1.00 42.56 ?  281 ASN B O     1 
ATOM   5282 C CB    . ASN B 1 281 ? -0.454  -12.490 43.589 1.00 46.72 ?  281 ASN B CB    1 
ATOM   5283 C CG    . ASN B 1 281 ? -1.168  -11.864 44.761 1.00 50.09 ?  281 ASN B CG    1 
ATOM   5284 O OD1   . ASN B 1 281 ? -1.309  -12.488 45.810 1.00 52.94 ?  281 ASN B OD1   1 
ATOM   5285 N ND2   . ASN B 1 281 ? -1.615  -10.619 44.596 1.00 48.65 ?  281 ASN B ND2   1 
ATOM   5286 N N     . ASP B 1 282 ? 1.902   -12.961 41.500 1.00 48.37 ?  282 ASP B N     1 
ATOM   5287 C CA    . ASP B 1 282 ? 2.435   -13.860 40.479 1.00 55.41 ?  282 ASP B CA    1 
ATOM   5288 C C     . ASP B 1 282 ? 3.934   -14.108 40.651 1.00 47.60 ?  282 ASP B C     1 
ATOM   5289 O O     . ASP B 1 282 ? 4.414   -15.214 40.389 1.00 46.03 ?  282 ASP B O     1 
ATOM   5290 C CB    . ASP B 1 282 ? 2.152   -13.300 39.094 1.00 59.72 ?  282 ASP B CB    1 
ATOM   5291 C CG    . ASP B 1 282 ? 0.733   -13.526 38.657 1.00 69.10 ?  282 ASP B CG    1 
ATOM   5292 O OD1   . ASP B 1 282 ? -0.173  -12.906 39.251 1.00 75.40 ?  282 ASP B OD1   1 
ATOM   5293 O OD2   . ASP B 1 282 ? 0.518   -14.332 37.724 1.00 66.07 -1 282 ASP B OD2   1 
ATOM   5294 N N     . TRP B 1 283 ? 4.688   -13.104 41.105 1.00 37.67 ?  283 TRP B N     1 
ATOM   5295 C CA    . TRP B 1 283 ? 6.106   -13.323 41.378 1.00 37.18 ?  283 TRP B CA    1 
ATOM   5296 C C     . TRP B 1 283 ? 6.305   -14.336 42.497 1.00 34.41 ?  283 TRP B C     1 
ATOM   5297 O O     . TRP B 1 283 ? 7.259   -15.118 42.465 1.00 35.31 ?  283 TRP B O     1 
ATOM   5298 C CB    . TRP B 1 283 ? 6.795   -11.996 41.728 1.00 38.26 ?  283 TRP B CB    1 
ATOM   5299 C CG    . TRP B 1 283 ? 8.272   -12.143 42.061 1.00 42.84 ?  283 TRP B CG    1 
ATOM   5300 C CD1   . TRP B 1 283 ? 9.325   -12.044 41.195 1.00 39.37 ?  283 TRP B CD1   1 
ATOM   5301 C CD2   . TRP B 1 283 ? 8.846   -12.409 43.353 1.00 39.98 ?  283 TRP B CD2   1 
ATOM   5302 N NE1   . TRP B 1 283 ? 10.510  -12.238 41.865 1.00 36.66 ?  283 TRP B NE1   1 
ATOM   5303 C CE2   . TRP B 1 283 ? 10.240  -12.462 43.190 1.00 37.90 ?  283 TRP B CE2   1 
ATOM   5304 C CE3   . TRP B 1 283 ? 8.312   -12.615 44.627 1.00 30.81 ?  283 TRP B CE3   1 
ATOM   5305 C CZ2   . TRP B 1 283 ? 11.103  -12.705 44.257 1.00 37.55 ?  283 TRP B CZ2   1 
ATOM   5306 C CZ3   . TRP B 1 283 ? 9.167   -12.849 45.672 1.00 22.61 ?  283 TRP B CZ3   1 
ATOM   5307 C CH2   . TRP B 1 283 ? 10.543  -12.898 45.485 1.00 23.05 ?  283 TRP B CH2   1 
ATOM   5308 N N     . LEU B 1 284 ? 5.391   -14.372 43.462 1.00 33.95 ?  284 LEU B N     1 
ATOM   5309 C CA    . LEU B 1 284 ? 5.527   -15.319 44.559 1.00 32.58 ?  284 LEU B CA    1 
ATOM   5310 C C     . LEU B 1 284 ? 5.195   -16.736 44.118 1.00 46.30 ?  284 LEU B C     1 
ATOM   5311 O O     . LEU B 1 284 ? 5.760   -17.695 44.654 1.00 57.29 ?  284 LEU B O     1 
ATOM   5312 C CB    . LEU B 1 284 ? 4.622   -14.896 45.714 1.00 29.73 ?  284 LEU B CB    1 
ATOM   5313 C CG    . LEU B 1 284 ? 4.420   -15.837 46.899 1.00 28.97 ?  284 LEU B CG    1 
ATOM   5314 C CD1   . LEU B 1 284 ? 5.748   -16.189 47.558 1.00 30.78 ?  284 LEU B CD1   1 
ATOM   5315 C CD2   . LEU B 1 284 ? 3.463   -15.218 47.909 1.00 37.58 ?  284 LEU B CD2   1 
ATOM   5316 N N     . ASN B 1 285 ? 4.316   -16.891 43.123 1.00 48.37 ?  285 ASN B N     1 
ATOM   5317 C CA    . ASN B 1 285 ? 4.070   -18.210 42.547 1.00 41.85 ?  285 ASN B CA    1 
ATOM   5318 C C     . ASN B 1 285 ? 5.315   -18.744 41.863 1.00 41.33 ?  285 ASN B C     1 
ATOM   5319 O O     . ASN B 1 285 ? 5.663   -19.922 42.011 1.00 51.67 ?  285 ASN B O     1 
ATOM   5320 C CB    . ASN B 1 285 ? 2.906   -18.130 41.566 1.00 39.74 ?  285 ASN B CB    1 
ATOM   5321 C CG    . ASN B 1 285 ? 1.647   -17.639 42.224 1.00 39.79 ?  285 ASN B CG    1 
ATOM   5322 O OD1   . ASN B 1 285 ? 1.475   -17.786 43.434 1.00 36.19 ?  285 ASN B OD1   1 
ATOM   5323 N ND2   . ASN B 1 285 ? 0.768   -17.029 41.443 1.00 41.82 ?  285 ASN B ND2   1 
ATOM   5324 N N     . LYS B 1 286 ? 5.995   -17.889 41.102 1.00 34.84 ?  286 LYS B N     1 
ATOM   5325 C CA    . LYS B 1 286 ? 7.251   -18.268 40.472 1.00 38.92 ?  286 LYS B CA    1 
ATOM   5326 C C     . LYS B 1 286 ? 8.287   -18.710 41.505 1.00 40.53 ?  286 LYS B C     1 
ATOM   5327 O O     . LYS B 1 286 ? 8.834   -19.814 41.416 1.00 44.19 ?  286 LYS B O     1 
ATOM   5328 C CB    . LYS B 1 286 ? 7.782   -17.107 39.634 1.00 44.23 ?  286 LYS B CB    1 
ATOM   5329 C CG    . LYS B 1 286 ? 7.442   -17.194 38.155 1.00 41.64 ?  286 LYS B CG    1 
ATOM   5330 C CD    . LYS B 1 286 ? 5.981   -16.900 37.912 1.00 42.90 ?  286 LYS B CD    1 
ATOM   5331 C CE    . LYS B 1 286 ? 5.671   -16.878 36.433 1.00 44.40 ?  286 LYS B CE    1 
ATOM   5332 N NZ    . LYS B 1 286 ? 6.536   -15.901 35.734 1.00 41.29 1  286 LYS B NZ    1 
ATOM   5333 N N     . ILE B 1 287 ? 8.575   -17.856 42.495 1.00 28.55 ?  287 ILE B N     1 
ATOM   5334 C CA    . ILE B 1 287 ? 9.685   -18.125 43.413 1.00 32.02 ?  287 ILE B CA    1 
ATOM   5335 C C     . ILE B 1 287 ? 9.490   -19.438 44.164 1.00 30.93 ?  287 ILE B C     1 
ATOM   5336 O O     . ILE B 1 287 ? 10.463  -20.053 44.617 1.00 29.10 ?  287 ILE B O     1 
ATOM   5337 C CB    . ILE B 1 287 ? 9.891   -16.945 44.386 1.00 30.56 ?  287 ILE B CB    1 
ATOM   5338 C CG1   . ILE B 1 287 ? 11.255  -17.064 45.081 1.00 37.64 ?  287 ILE B CG1   1 
ATOM   5339 C CG2   . ILE B 1 287 ? 8.810   -16.914 45.459 1.00 24.13 ?  287 ILE B CG2   1 
ATOM   5340 C CD1   . ILE B 1 287 ? 12.458  -16.957 44.157 1.00 31.18 ?  287 ILE B CD1   1 
ATOM   5341 N N     . ARG B 1 288 ? 8.248   -19.884 44.324 1.00 36.01 ?  288 ARG B N     1 
ATOM   5342 C CA    . ARG B 1 288 ? 8.001   -21.143 45.017 1.00 34.55 ?  288 ARG B CA    1 
ATOM   5343 C C     . ARG B 1 288 ? 8.496   -22.339 44.219 1.00 33.42 ?  288 ARG B C     1 
ATOM   5344 O O     . ARG B 1 288 ? 8.991   -23.315 44.789 1.00 21.81 ?  288 ARG B O     1 
ATOM   5345 C CB    . ARG B 1 288 ? 6.518   -21.289 45.298 1.00 31.57 ?  288 ARG B CB    1 
ATOM   5346 C CG    . ARG B 1 288 ? 6.086   -20.439 46.417 1.00 29.49 ?  288 ARG B CG    1 
ATOM   5347 C CD    . ARG B 1 288 ? 4.588   -20.167 46.404 1.00 26.03 ?  288 ARG B CD    1 
ATOM   5348 N NE    . ARG B 1 288 ? 4.082   -20.418 47.744 1.00 31.38 ?  288 ARG B NE    1 
ATOM   5349 C CZ    . ARG B 1 288 ? 2.928   -19.967 48.233 1.00 51.91 ?  288 ARG B CZ    1 
ATOM   5350 N NH1   . ARG B 1 288 ? 2.155   -19.226 47.466 1.00 60.10 1  288 ARG B NH1   1 
ATOM   5351 N NH2   . ARG B 1 288 ? 2.533   -20.244 49.489 1.00 52.47 ?  288 ARG B NH2   1 
ATOM   5352 N N     . LEU B 1 289 ? 8.300   -22.311 42.907 1.00 38.95 ?  289 LEU B N     1 
ATOM   5353 C CA    . LEU B 1 289 ? 8.718   -23.423 42.063 1.00 44.89 ?  289 LEU B CA    1 
ATOM   5354 C C     . LEU B 1 289 ? 10.213  -23.389 41.772 1.00 46.52 ?  289 LEU B C     1 
ATOM   5355 O O     . LEU B 1 289 ? 10.831  -24.437 41.561 1.00 55.31 ?  289 LEU B O     1 
ATOM   5356 C CB    . LEU B 1 289 ? 7.916   -23.411 40.758 1.00 46.13 ?  289 LEU B CB    1 
ATOM   5357 C CG    . LEU B 1 289 ? 6.391   -23.433 40.911 1.00 43.80 ?  289 LEU B CG    1 
ATOM   5358 C CD1   . LEU B 1 289 ? 5.756   -22.995 39.603 1.00 49.81 ?  289 LEU B CD1   1 
ATOM   5359 C CD2   . LEU B 1 289 ? 5.852   -24.807 41.364 1.00 32.97 ?  289 LEU B CD2   1 
ATOM   5360 N N     . TYR B 1 290 ? 10.809  -22.202 41.755 1.00 38.89 ?  290 TYR B N     1 
ATOM   5361 C CA    . TYR B 1 290 ? 12.254  -22.125 41.607 1.00 29.31 ?  290 TYR B CA    1 
ATOM   5362 C C     . TYR B 1 290 ? 12.942  -22.609 42.874 1.00 30.71 ?  290 TYR B C     1 
ATOM   5363 O O     . TYR B 1 290 ? 13.905  -23.380 42.806 1.00 38.40 ?  290 TYR B O     1 
ATOM   5364 C CB    . TYR B 1 290 ? 12.670  -20.694 41.277 1.00 30.00 ?  290 TYR B CB    1 
ATOM   5365 C CG    . TYR B 1 290 ? 14.019  -20.575 40.618 1.00 29.09 ?  290 TYR B CG    1 
ATOM   5366 C CD1   . TYR B 1 290 ? 14.165  -20.793 39.260 1.00 31.74 ?  290 TYR B CD1   1 
ATOM   5367 C CD2   . TYR B 1 290 ? 15.142  -20.220 41.349 1.00 34.48 ?  290 TYR B CD2   1 
ATOM   5368 C CE1   . TYR B 1 290 ? 15.387  -20.683 38.641 1.00 35.14 ?  290 TYR B CE1   1 
ATOM   5369 C CE2   . TYR B 1 290 ? 16.384  -20.104 40.737 1.00 43.97 ?  290 TYR B CE2   1 
ATOM   5370 C CZ    . TYR B 1 290 ? 16.499  -20.338 39.379 1.00 46.98 ?  290 TYR B CZ    1 
ATOM   5371 O OH    . TYR B 1 290 ? 17.722  -20.229 38.751 1.00 42.73 ?  290 TYR B OH    1 
ATOM   5372 N N     . ILE B 1 291 ? 12.449  -22.188 44.042 1.00 24.27 ?  291 ILE B N     1 
ATOM   5373 C CA    . ILE B 1 291 ? 13.069  -22.612 45.296 1.00 34.36 ?  291 ILE B CA    1 
ATOM   5374 C C     . ILE B 1 291 ? 12.896  -24.112 45.499 1.00 31.60 ?  291 ILE B C     1 
ATOM   5375 O O     . ILE B 1 291 ? 13.842  -24.810 45.870 1.00 32.89 ?  291 ILE B O     1 
ATOM   5376 C CB    . ILE B 1 291 ? 12.512  -21.810 46.486 1.00 38.58 ?  291 ILE B CB    1 
ATOM   5377 C CG1   . ILE B 1 291 ? 12.980  -20.356 46.431 1.00 38.49 ?  291 ILE B CG1   1 
ATOM   5378 C CG2   . ILE B 1 291 ? 12.965  -22.416 47.788 1.00 41.74 ?  291 ILE B CG2   1 
ATOM   5379 C CD1   . ILE B 1 291 ? 14.365  -20.186 45.912 1.00 31.00 ?  291 ILE B CD1   1 
ATOM   5380 N N     . GLU B 1 292 ? 11.688  -24.628 45.251 1.00 31.02 ?  292 GLU B N     1 
ATOM   5381 C CA    . GLU B 1 292 ? 11.402  -26.045 45.465 1.00 29.39 ?  292 GLU B CA    1 
ATOM   5382 C C     . GLU B 1 292 ? 12.245  -26.924 44.558 1.00 24.83 ?  292 GLU B C     1 
ATOM   5383 O O     . GLU B 1 292 ? 12.614  -28.043 44.930 1.00 18.49 ?  292 GLU B O     1 
ATOM   5384 C CB    . GLU B 1 292 ? 9.921   -26.326 45.227 1.00 46.57 ?  292 GLU B CB    1 
ATOM   5385 C CG    . GLU B 1 292 ? 9.509   -27.777 45.471 1.00 43.97 ?  292 GLU B CG    1 
ATOM   5386 C CD    . GLU B 1 292 ? 8.018   -27.906 45.555 1.00 44.91 ?  292 GLU B CD    1 
ATOM   5387 O OE1   . GLU B 1 292 ? 7.339   -26.973 45.095 1.00 50.84 ?  292 GLU B OE1   1 
ATOM   5388 O OE2   . GLU B 1 292 ? 7.519   -28.907 46.101 1.00 54.15 -1 292 GLU B OE2   1 
ATOM   5389 N N     . ASP B 1 293 ? 12.491  -26.464 43.336 1.00 33.37 ?  293 ASP B N     1 
ATOM   5390 C CA    . ASP B 1 293 ? 13.357  -27.200 42.428 1.00 42.45 ?  293 ASP B CA    1 
ATOM   5391 C C     . ASP B 1 293 ? 14.821  -27.099 42.852 1.00 44.89 ?  293 ASP B C     1 
ATOM   5392 O O     . ASP B 1 293 ? 15.588  -28.046 42.651 1.00 36.69 ?  293 ASP B O     1 
ATOM   5393 C CB    . ASP B 1 293 ? 13.151  -26.671 41.002 1.00 47.28 ?  293 ASP B CB    1 
ATOM   5394 C CG    . ASP B 1 293 ? 13.579  -27.662 39.932 1.00 57.63 ?  293 ASP B CG    1 
ATOM   5395 O OD1   . ASP B 1 293 ? 14.246  -28.666 40.262 1.00 65.40 -1 293 ASP B OD1   1 
ATOM   5396 O OD2   . ASP B 1 293 ? 13.253  -27.430 38.748 1.00 59.04 -1 293 ASP B OD2   1 
ATOM   5397 N N     . ASN B 1 294 ? 15.214  -25.983 43.482 1.00 52.70 ?  294 ASN B N     1 
ATOM   5398 C CA    . ASN B 1 294 ? 16.563  -25.856 44.036 1.00 39.80 ?  294 ASN B CA    1 
ATOM   5399 C C     . ASN B 1 294 ? 16.777  -26.823 45.195 1.00 35.04 ?  294 ASN B C     1 
ATOM   5400 O O     . ASN B 1 294 ? 17.884  -27.339 45.388 1.00 35.82 ?  294 ASN B O     1 
ATOM   5401 C CB    . ASN B 1 294 ? 16.815  -24.417 44.487 1.00 30.21 ?  294 ASN B CB    1 
ATOM   5402 C CG    . ASN B 1 294 ? 17.153  -23.497 43.330 1.00 26.74 ?  294 ASN B CG    1 
ATOM   5403 O OD1   . ASN B 1 294 ? 17.045  -23.882 42.172 1.00 34.67 ?  294 ASN B OD1   1 
ATOM   5404 N ND2   . ASN B 1 294 ? 17.537  -22.271 43.640 1.00 23.09 ?  294 ASN B ND2   1 
ATOM   5405 N N     . ALA B 1 295 ? 15.736  -27.056 45.995 1.00 21.02 ?  295 ALA B N     1 
ATOM   5406 C CA    . ALA B 1 295 ? 15.808  -28.084 47.024 1.00 21.46 ?  295 ALA B CA    1 
ATOM   5407 C C     . ALA B 1 295 ? 15.851  -29.482 46.412 1.00 39.92 ?  295 ALA B C     1 
ATOM   5408 O O     . ALA B 1 295 ? 16.562  -30.362 46.913 1.00 38.83 ?  295 ALA B O     1 
ATOM   5409 C CB    . ALA B 1 295 ? 14.618  -27.958 47.972 1.00 14.64 ?  295 ALA B CB    1 
ATOM   5410 N N     . LYS B 1 296 ? 15.098  -29.707 45.329 1.00 43.83 ?  296 LYS B N     1 
ATOM   5411 C CA    . LYS B 1 296 ? 15.097  -31.015 44.677 1.00 36.56 ?  296 LYS B CA    1 
ATOM   5412 C C     . LYS B 1 296 ? 16.437  -31.291 44.003 1.00 29.78 ?  296 LYS B C     1 
ATOM   5413 O O     . LYS B 1 296 ? 17.005  -32.378 44.150 1.00 42.23 ?  296 LYS B O     1 
ATOM   5414 C CB    . LYS B 1 296 ? 13.948  -31.100 43.671 1.00 41.04 ?  296 LYS B CB    1 
ATOM   5415 C CG    . LYS B 1 296 ? 13.962  -32.360 42.818 1.00 55.38 ?  296 LYS B CG    1 
ATOM   5416 C CD    . LYS B 1 296 ? 13.475  -32.091 41.393 1.00 57.63 ?  296 LYS B CD    1 
ATOM   5417 C CE    . LYS B 1 296 ? 14.632  -31.970 40.409 1.00 50.54 ?  296 LYS B CE    1 
ATOM   5418 N NZ    . LYS B 1 296 ? 14.177  -31.432 39.100 1.00 46.84 1  296 LYS B NZ    1 
ATOM   5419 N N     . PHE B 1 297 ? 16.954  -30.317 43.256 1.00 22.95 ?  297 PHE B N     1 
ATOM   5420 C CA    . PHE B 1 297 ? 18.272  -30.459 42.644 1.00 29.49 ?  297 PHE B CA    1 
ATOM   5421 C C     . PHE B 1 297 ? 19.347  -30.740 43.692 1.00 34.60 ?  297 PHE B C     1 
ATOM   5422 O O     . PHE B 1 297 ? 20.205  -31.605 43.493 1.00 36.17 ?  297 PHE B O     1 
ATOM   5423 C CB    . PHE B 1 297 ? 18.604  -29.189 41.855 1.00 28.57 ?  297 PHE B CB    1 
ATOM   5424 C CG    . PHE B 1 297 ? 20.015  -29.118 41.368 1.00 33.75 ?  297 PHE B CG    1 
ATOM   5425 C CD1   . PHE B 1 297 ? 20.371  -29.681 40.161 1.00 41.55 ?  297 PHE B CD1   1 
ATOM   5426 C CD2   . PHE B 1 297 ? 20.990  -28.482 42.112 1.00 39.51 ?  297 PHE B CD2   1 
ATOM   5427 C CE1   . PHE B 1 297 ? 21.674  -29.611 39.712 1.00 42.99 ?  297 PHE B CE1   1 
ATOM   5428 C CE2   . PHE B 1 297 ? 22.291  -28.414 41.664 1.00 37.45 ?  297 PHE B CE2   1 
ATOM   5429 C CZ    . PHE B 1 297 ? 22.629  -28.978 40.468 1.00 37.83 ?  297 PHE B CZ    1 
ATOM   5430 N N     . ALA B 1 298 ? 19.310  -30.033 44.823 1.00 33.70 ?  298 ALA B N     1 
ATOM   5431 C CA    . ALA B 1 298 ? 20.360  -30.188 45.823 1.00 21.25 ?  298 ALA B CA    1 
ATOM   5432 C C     . ALA B 1 298 ? 20.270  -31.541 46.521 1.00 19.81 ?  298 ALA B C     1 
ATOM   5433 O O     . ALA B 1 298 ? 21.296  -32.142 46.851 1.00 25.47 ?  298 ALA B O     1 
ATOM   5434 C CB    . ALA B 1 298 ? 20.299  -29.040 46.832 1.00 19.51 ?  298 ALA B CB    1 
ATOM   5435 N N     . CYS B 1 299 ? 19.057  -32.038 46.760 1.00 23.47 ?  299 CYS B N     1 
ATOM   5436 C CA    . CYS B 1 299 ? 18.901  -33.297 47.490 1.00 28.79 ?  299 CYS B CA    1 
ATOM   5437 C C     . CYS B 1 299 ? 19.396  -34.500 46.690 1.00 26.92 ?  299 CYS B C     1 
ATOM   5438 O O     . CYS B 1 299 ? 19.809  -35.504 47.281 1.00 19.14 ?  299 CYS B O     1 
ATOM   5439 C CB    . CYS B 1 299 ? 17.440  -33.481 47.885 1.00 26.00 ?  299 CYS B CB    1 
ATOM   5440 S SG    . CYS B 1 299 ? 16.945  -32.332 49.174 1.00 35.28 ?  299 CYS B SG    1 
ATOM   5441 N N     . GLU B 1 300 ? 19.356  -34.418 45.357 1.00 31.69 ?  300 GLU B N     1 
ATOM   5442 C CA    . GLU B 1 300 ? 19.875  -35.479 44.501 1.00 47.34 ?  300 GLU B CA    1 
ATOM   5443 C C     . GLU B 1 300 ? 21.391  -35.378 44.325 1.00 53.71 ?  300 GLU B C     1 
ATOM   5444 O O     . GLU B 1 300 ? 22.088  -36.398 44.319 1.00 54.51 ?  300 GLU B O     1 
ATOM   5445 C CB    . GLU B 1 300 ? 19.180  -35.447 43.142 1.00 47.71 ?  300 GLU B CB    1 
ATOM   5446 C CG    . GLU B 1 300 ? 17.681  -35.405 43.248 1.00 57.84 ?  300 GLU B CG    1 
ATOM   5447 C CD    . GLU B 1 300 ? 17.023  -35.035 41.943 1.00 68.77 ?  300 GLU B CD    1 
ATOM   5448 O OE1   . GLU B 1 300 ? 17.661  -34.314 41.140 1.00 73.65 ?  300 GLU B OE1   1 
ATOM   5449 O OE2   . GLU B 1 300 ? 15.858  -35.444 41.729 1.00 70.01 -1 300 GLU B OE2   1 
ATOM   5450 N N     . TYR B 1 301 ? 21.917  -34.160 44.148 1.00 31.19 ?  301 TYR B N     1 
ATOM   5451 C CA    . TYR B 1 301 ? 23.371  -33.994 44.069 1.00 31.85 ?  301 TYR B CA    1 
ATOM   5452 C C     . TYR B 1 301 ? 24.057  -34.570 45.300 1.00 29.97 ?  301 TYR B C     1 
ATOM   5453 O O     . TYR B 1 301 ? 25.201  -35.025 45.213 1.00 35.08 ?  301 TYR B O     1 
ATOM   5454 C CB    . TYR B 1 301 ? 23.745  -32.519 43.880 1.00 34.73 ?  301 TYR B CB    1 
ATOM   5455 C CG    . TYR B 1 301 ? 25.239  -32.240 43.718 1.00 33.59 ?  301 TYR B CG    1 
ATOM   5456 C CD1   . TYR B 1 301 ? 26.088  -32.219 44.817 1.00 34.81 ?  301 TYR B CD1   1 
ATOM   5457 C CD2   . TYR B 1 301 ? 25.786  -31.935 42.483 1.00 32.25 ?  301 TYR B CD2   1 
ATOM   5458 C CE1   . TYR B 1 301 ? 27.437  -31.947 44.686 1.00 31.54 ?  301 TYR B CE1   1 
ATOM   5459 C CE2   . TYR B 1 301 ? 27.144  -31.647 42.350 1.00 34.32 ?  301 TYR B CE2   1 
ATOM   5460 C CZ    . TYR B 1 301 ? 27.959  -31.657 43.456 1.00 33.14 ?  301 TYR B CZ    1 
ATOM   5461 O OH    . TYR B 1 301 ? 29.300  -31.381 43.334 1.00 36.22 ?  301 TYR B OH    1 
ATOM   5462 N N     . MET B 1 302 ? 23.399  -34.523 46.459 1.00 30.65 ?  302 MET B N     1 
ATOM   5463 C CA    . MET B 1 302 ? 23.974  -35.144 47.647 1.00 42.16 ?  302 MET B CA    1 
ATOM   5464 C C     . MET B 1 302 ? 23.830  -36.662 47.605 1.00 56.76 ?  302 MET B C     1 
ATOM   5465 O O     . MET B 1 302 ? 24.676  -37.375 48.155 1.00 66.23 ?  302 MET B O     1 
ATOM   5466 C CB    . MET B 1 302 ? 23.300  -34.599 48.915 1.00 31.33 ?  302 MET B CB    1 
ATOM   5467 C CG    . MET B 1 302 ? 24.227  -34.301 50.095 1.00 39.95 ?  302 MET B CG    1 
ATOM   5468 S SD    . MET B 1 302 ? 25.075  -32.697 49.944 1.00 51.02 ?  302 MET B SD    1 
ATOM   5469 C CE    . MET B 1 302 ? 23.793  -31.594 50.524 1.00 23.54 ?  302 MET B CE    1 
ATOM   5470 N N     . LYS B 1 303 ? 22.790  -37.174 46.939 1.00 44.89 ?  303 LYS B N     1 
ATOM   5471 C CA    . LYS B 1 303 ? 22.713  -38.607 46.665 1.00 47.23 ?  303 LYS B CA    1 
ATOM   5472 C C     . LYS B 1 303 ? 23.872  -39.051 45.777 1.00 46.82 ?  303 LYS B C     1 
ATOM   5473 O O     . LYS B 1 303 ? 24.599  -39.999 46.105 1.00 26.57 ?  303 LYS B O     1 
ATOM   5474 C CB    . LYS B 1 303 ? 21.362  -38.950 46.027 1.00 48.17 ?  303 LYS B CB    1 
ATOM   5475 C CG    . LYS B 1 303 ? 20.934  -40.412 46.163 1.00 42.49 ?  303 LYS B CG    1 
ATOM   5476 C CD    . LYS B 1 303 ? 19.468  -40.582 45.792 1.00 46.31 ?  303 LYS B CD    1 
ATOM   5477 C CE    . LYS B 1 303 ? 19.081  -42.047 45.726 1.00 53.22 ?  303 LYS B CE    1 
ATOM   5478 N NZ    . LYS B 1 303 ? 17.752  -42.266 45.086 1.00 50.97 1  303 LYS B NZ    1 
ATOM   5479 N N     . ASP B 1 304 ? 24.051  -38.370 44.641 1.00 52.45 ?  304 ASP B N     1 
ATOM   5480 C CA    . ASP B 1 304 ? 25.015  -38.805 43.638 1.00 52.50 ?  304 ASP B CA    1 
ATOM   5481 C C     . ASP B 1 304 ? 26.446  -38.491 44.055 1.00 60.86 ?  304 ASP B C     1 
ATOM   5482 O O     . ASP B 1 304 ? 27.321  -39.362 43.994 1.00 71.22 ?  304 ASP B O     1 
ATOM   5483 C CB    . ASP B 1 304 ? 24.709  -38.138 42.295 1.00 46.39 ?  304 ASP B CB    1 
ATOM   5484 C CG    . ASP B 1 304 ? 23.281  -38.345 41.852 1.00 53.02 ?  304 ASP B CG    1 
ATOM   5485 O OD1   . ASP B 1 304 ? 22.684  -39.371 42.229 1.00 52.95 ?  304 ASP B OD1   1 
ATOM   5486 O OD2   . ASP B 1 304 ? 22.756  -37.488 41.114 1.00 52.14 -1 304 ASP B OD2   1 
ATOM   5487 N N     . HIS B 1 305 ? 26.716  -37.250 44.467 1.00 52.07 ?  305 HIS B N     1 
ATOM   5488 C CA    . HIS B 1 305 ? 28.097  -36.802 44.598 1.00 47.83 ?  305 HIS B CA    1 
ATOM   5489 C C     . HIS B 1 305 ? 28.580  -36.590 46.027 1.00 48.78 ?  305 HIS B C     1 
ATOM   5490 O O     . HIS B 1 305 ? 29.784  -36.381 46.220 1.00 55.19 ?  305 HIS B O     1 
ATOM   5491 C CB    . HIS B 1 305 ? 28.304  -35.497 43.820 1.00 27.28 ?  305 HIS B CB    1 
ATOM   5492 C CG    . HIS B 1 305 ? 28.103  -35.641 42.349 1.00 31.20 ?  305 HIS B CG    1 
ATOM   5493 N ND1   . HIS B 1 305 ? 27.799  -34.573 41.534 1.00 37.61 ?  305 HIS B ND1   1 
ATOM   5494 C CD2   . HIS B 1 305 ? 28.140  -36.732 41.546 1.00 39.02 ?  305 HIS B CD2   1 
ATOM   5495 C CE1   . HIS B 1 305 ? 27.664  -34.997 40.289 1.00 42.76 ?  305 HIS B CE1   1 
ATOM   5496 N NE2   . HIS B 1 305 ? 27.865  -36.303 40.269 1.00 40.77 ?  305 HIS B NE2   1 
ATOM   5497 N N     . ILE B 1 306 ? 27.707  -36.608 47.029 1.00 38.89 ?  306 ILE B N     1 
ATOM   5498 C CA    . ILE B 1 306 ? 28.202  -36.509 48.402 1.00 31.62 ?  306 ILE B CA    1 
ATOM   5499 C C     . ILE B 1 306 ? 27.478  -37.517 49.292 1.00 26.21 ?  306 ILE B C     1 
ATOM   5500 O O     . ILE B 1 306 ? 26.774  -37.111 50.228 1.00 26.46 ?  306 ILE B O     1 
ATOM   5501 C CB    . ILE B 1 306 ? 28.069  -35.065 48.936 1.00 26.13 ?  306 ILE B CB    1 
ATOM   5502 C CG1   . ILE B 1 306 ? 28.599  -34.042 47.928 1.00 28.71 ?  306 ILE B CG1   1 
ATOM   5503 C CG2   . ILE B 1 306 ? 28.867  -34.865 50.199 1.00 10.80 ?  306 ILE B CG2   1 
ATOM   5504 C CD1   . ILE B 1 306 ? 28.457  -32.615 48.364 1.00 34.06 ?  306 ILE B CD1   1 
ATOM   5505 N N     . PRO B 1 307 ? 27.632  -38.830 49.076 1.00 31.90 ?  307 PRO B N     1 
ATOM   5506 C CA    . PRO B 1 307 ? 26.851  -39.798 49.872 1.00 36.62 ?  307 PRO B CA    1 
ATOM   5507 C C     . PRO B 1 307 ? 27.212  -39.809 51.351 1.00 24.52 ?  307 PRO B C     1 
ATOM   5508 O O     . PRO B 1 307 ? 26.562  -40.523 52.127 1.00 17.37 ?  307 PRO B O     1 
ATOM   5509 C CB    . PRO B 1 307 ? 27.157  -41.144 49.199 1.00 35.83 ?  307 PRO B CB    1 
ATOM   5510 C CG    . PRO B 1 307 ? 28.428  -40.937 48.487 1.00 41.37 ?  307 PRO B CG    1 
ATOM   5511 C CD    . PRO B 1 307 ? 28.418  -39.502 48.030 1.00 41.11 ?  307 PRO B CD    1 
ATOM   5512 N N     . THR B 1 308 ? 28.221  -39.046 51.763 1.00 22.42 ?  308 THR B N     1 
ATOM   5513 C CA    . THR B 1 308 ? 28.595  -38.949 53.167 1.00 33.42 ?  308 THR B CA    1 
ATOM   5514 C C     . THR B 1 308 ? 27.822  -37.855 53.910 1.00 28.61 ?  308 THR B C     1 
ATOM   5515 O O     . THR B 1 308 ? 28.000  -37.692 55.121 1.00 29.40 ?  308 THR B O     1 
ATOM   5516 C CB    . THR B 1 308 ? 30.110  -38.707 53.302 1.00 27.81 ?  308 THR B CB    1 
ATOM   5517 O OG1   . THR B 1 308 ? 30.438  -37.409 52.808 1.00 32.50 ?  308 THR B OG1   1 
ATOM   5518 C CG2   . THR B 1 308 ? 30.896  -39.729 52.507 1.00 23.84 ?  308 THR B CG2   1 
ATOM   5519 N N     . LEU B 1 309 ? 26.918  -37.148 53.248 1.00 27.34 ?  309 LEU B N     1 
ATOM   5520 C CA    . LEU B 1 309 ? 26.087  -36.158 53.917 1.00 29.28 ?  309 LEU B CA    1 
ATOM   5521 C C     . LEU B 1 309 ? 24.623  -36.590 53.877 1.00 13.74 ?  309 LEU B C     1 
ATOM   5522 O O     . LEU B 1 309 ? 24.182  -37.263 52.944 1.00 13.85 ?  309 LEU B O     1 
ATOM   5523 C CB    . LEU B 1 309 ? 26.240  -34.768 53.276 1.00 30.95 ?  309 LEU B CB    1 
ATOM   5524 C CG    . LEU B 1 309 ? 27.626  -34.149 53.446 1.00 28.93 ?  309 LEU B CG    1 
ATOM   5525 C CD1   . LEU B 1 309 ? 27.699  -32.745 52.883 1.00 33.47 ?  309 LEU B CD1   1 
ATOM   5526 C CD2   . LEU B 1 309 ? 28.015  -34.147 54.907 1.00 24.37 ?  309 LEU B CD2   1 
ATOM   5527 N N     . SER B 1 310 ? 23.889  -36.232 54.923 1.00 8.78  ?  310 SER B N     1 
ATOM   5528 C CA    . SER B 1 310 ? 22.446  -36.436 54.983 1.00 35.77 ?  310 SER B CA    1 
ATOM   5529 C C     . SER B 1 310 ? 21.784  -35.075 55.060 1.00 35.36 ?  310 SER B C     1 
ATOM   5530 O O     . SER B 1 310 ? 22.051  -34.305 55.988 1.00 29.75 ?  310 SER B O     1 
ATOM   5531 C CB    . SER B 1 310 ? 22.017  -37.266 56.192 1.00 35.22 ?  310 SER B CB    1 
ATOM   5532 O OG    . SER B 1 310 ? 20.727  -36.863 56.637 1.00 36.23 ?  310 SER B OG    1 
ATOM   5533 N N     . VAL B 1 311 ? 20.955  -34.767 54.057 1.00 41.08 ?  311 VAL B N     1 
ATOM   5534 C CA    . VAL B 1 311 ? 20.195  -33.487 53.962 1.00 32.47 ?  311 VAL B CA    1 
ATOM   5535 C C     . VAL B 1 311 ? 18.748  -33.716 54.393 1.00 33.39 ?  311 VAL B C     1 
ATOM   5536 O O     . VAL B 1 311 ? 18.111  -34.566 53.802 1.00 38.26 ?  311 VAL B O     1 
ATOM   5537 C CB    . VAL B 1 311 ? 20.239  -32.946 52.520 1.00 23.12 ?  311 VAL B CB    1 
ATOM   5538 C CG1   . VAL B 1 311 ? 19.388  -31.710 52.320 1.00 12.13 ?  311 VAL B CG1   1 
ATOM   5539 C CG2   . VAL B 1 311 ? 21.649  -32.732 52.017 1.00 16.61 ?  311 VAL B CG2   1 
ATOM   5540 N N     . THR B 1 312 ? 18.245  -32.966 55.372 1.00 35.62 ?  312 THR B N     1 
ATOM   5541 C CA    . THR B 1 312 ? 16.845  -33.062 55.728 1.00 28.04 ?  312 THR B CA    1 
ATOM   5542 C C     . THR B 1 312 ? 16.066  -32.293 54.675 1.00 38.62 ?  312 THR B C     1 
ATOM   5543 O O     . THR B 1 312 ? 16.339  -31.111 54.436 1.00 46.21 ?  312 THR B O     1 
ATOM   5544 C CB    . THR B 1 312 ? 16.600  -32.486 57.123 1.00 17.44 ?  312 THR B CB    1 
ATOM   5545 O OG1   . THR B 1 312 ? 16.356  -31.085 57.029 1.00 33.27 ?  312 THR B OG1   1 
ATOM   5546 C CG2   . THR B 1 312 ? 17.790  -32.695 57.994 1.00 11.89 ?  312 THR B CG2   1 
ATOM   5547 N N     . LYS B 1 313 ? 15.096  -32.953 54.053 1.00 32.70 ?  313 LYS B N     1 
ATOM   5548 C CA    . LYS B 1 313 ? 14.368  -32.314 52.966 1.00 26.79 ?  313 LYS B CA    1 
ATOM   5549 C C     . LYS B 1 313 ? 13.483  -31.227 53.546 1.00 32.19 ?  313 LYS B C     1 
ATOM   5550 O O     . LYS B 1 313 ? 12.754  -31.479 54.511 1.00 29.74 ?  313 LYS B O     1 
ATOM   5551 C CB    . LYS B 1 313 ? 13.521  -33.298 52.170 1.00 26.59 ?  313 LYS B CB    1 
ATOM   5552 C CG    . LYS B 1 313 ? 12.758  -32.618 51.041 1.00 35.24 ?  313 LYS B CG    1 
ATOM   5553 C CD    . LYS B 1 313 ? 13.263  -33.017 49.657 1.00 35.00 ?  313 LYS B CD    1 
ATOM   5554 C CE    . LYS B 1 313 ? 12.390  -32.430 48.564 1.00 32.46 ?  313 LYS B CE    1 
ATOM   5555 N NZ    . LYS B 1 313 ? 12.822  -31.059 48.194 1.00 33.21 1  313 LYS B NZ    1 
ATOM   5556 N N     . PRO B 1 314 ? 13.555  -30.006 53.031 1.00 40.14 ?  314 PRO B N     1 
ATOM   5557 C CA    . PRO B 1 314 ? 12.632  -28.965 53.471 1.00 36.87 ?  314 PRO B CA    1 
ATOM   5558 C C     . PRO B 1 314 ? 11.261  -29.105 52.819 1.00 23.78 ?  314 PRO B C     1 
ATOM   5559 O O     . PRO B 1 314 ? 11.079  -29.757 51.789 1.00 15.39 ?  314 PRO B O     1 
ATOM   5560 C CB    . PRO B 1 314 ? 13.332  -27.675 53.026 1.00 23.69 ?  314 PRO B CB    1 
ATOM   5561 C CG    . PRO B 1 314 ? 14.087  -28.075 51.826 1.00 15.24 ?  314 PRO B CG    1 
ATOM   5562 C CD    . PRO B 1 314 ? 14.535  -29.496 52.054 1.00 32.75 ?  314 PRO B CD    1 
ATOM   5563 N N     . GLU B 1 315 ? 10.274  -28.524 53.485 1.00 33.25 ?  315 GLU B N     1 
ATOM   5564 C CA    . GLU B 1 315 ? 8.924   -28.424 52.948 1.00 41.21 ?  315 GLU B CA    1 
ATOM   5565 C C     . GLU B 1 315 ? 8.492   -26.969 52.818 1.00 37.09 ?  315 GLU B C     1 
ATOM   5566 O O     . GLU B 1 315 ? 7.388   -26.692 52.333 1.00 24.03 ?  315 GLU B O     1 
ATOM   5567 C CB    . GLU B 1 315 ? 7.963   -29.233 53.824 1.00 28.05 ?  315 GLU B CB    1 
ATOM   5568 C CG    . GLU B 1 315 ? 8.582   -30.576 54.172 1.00 28.14 ?  315 GLU B CG    1 
ATOM   5569 C CD    . GLU B 1 315 ? 7.970   -31.192 55.381 1.00 36.89 ?  315 GLU B CD    1 
ATOM   5570 O OE1   . GLU B 1 315 ? 8.014   -32.438 55.499 1.00 42.44 ?  315 GLU B OE1   1 
ATOM   5571 O OE2   . GLU B 1 315 ? 7.437   -30.426 56.208 1.00 32.65 -1 315 GLU B OE2   1 
ATOM   5572 N N     . GLY B 1 316 ? 9.419   -26.116 53.224 1.00 28.73 ?  316 GLY B N     1 
ATOM   5573 C CA    . GLY B 1 316 ? 9.182   -24.685 53.177 1.00 32.38 ?  316 GLY B CA    1 
ATOM   5574 C C     . GLY B 1 316 ? 10.480  -23.922 53.205 1.00 28.80 ?  316 GLY B C     1 
ATOM   5575 O O     . GLY B 1 316 ? 11.522  -24.562 53.313 1.00 28.43 ?  316 GLY B O     1 
ATOM   5576 N N     . PHE B 1 318 ? 13.787  -21.475 52.169 1.00 15.94 ?  318 PHE B N     1 
ATOM   5577 C CA    . PHE B 1 318 ? 14.853  -21.559 51.156 1.00 30.95 ?  318 PHE B CA    1 
ATOM   5578 C C     . PHE B 1 318 ? 16.178  -21.895 51.855 1.00 36.56 ?  318 PHE B C     1 
ATOM   5579 O O     . PHE B 1 318 ? 17.229  -21.431 51.420 1.00 30.17 ?  318 PHE B O     1 
ATOM   5580 C CB    . PHE B 1 318 ? 14.906  -20.230 50.384 1.00 34.61 ?  318 PHE B CB    1 
ATOM   5581 C CG    . PHE B 1 318 ? 14.923  -18.956 51.190 1.00 26.47 ?  318 PHE B CG    1 
ATOM   5582 C CD1   . PHE B 1 318 ? 13.746  -18.345 51.586 1.00 22.06 ?  318 PHE B CD1   1 
ATOM   5583 C CD2   . PHE B 1 318 ? 16.118  -18.333 51.498 1.00 24.58 ?  318 PHE B CD2   1 
ATOM   5584 C CE1   . PHE B 1 318 ? 13.767  -17.167 52.312 1.00 19.94 ?  318 PHE B CE1   1 
ATOM   5585 C CE2   . PHE B 1 318 ? 16.139  -17.155 52.221 1.00 22.80 ?  318 PHE B CE2   1 
ATOM   5586 C CZ    . PHE B 1 318 ? 14.963  -16.572 52.623 1.00 20.52 ?  318 PHE B CZ    1 
ATOM   5587 N N     . LEU B 1 319 ? 16.111  -22.667 52.935 1.00 33.38 ?  319 LEU B N     1 
ATOM   5588 C CA    . LEU B 1 319 ? 17.305  -23.025 53.681 1.00 25.43 ?  319 LEU B CA    1 
ATOM   5589 C C     . LEU B 1 319 ? 17.450  -24.543 53.691 1.00 33.43 ?  319 LEU B C     1 
ATOM   5590 O O     . LEU B 1 319 ? 16.447  -25.268 53.739 1.00 30.71 ?  319 LEU B O     1 
ATOM   5591 C CB    . LEU B 1 319 ? 17.207  -22.461 55.099 1.00 19.19 ?  319 LEU B CB    1 
ATOM   5592 C CG    . LEU B 1 319 ? 16.909  -20.961 55.117 1.00 18.35 ?  319 LEU B CG    1 
ATOM   5593 C CD1   . LEU B 1 319 ? 16.510  -20.533 56.513 1.00 22.80 ?  319 LEU B CD1   1 
ATOM   5594 C CD2   . LEU B 1 319 ? 18.113  -20.155 54.637 1.00 13.69 ?  319 LEU B CD2   1 
ATOM   5595 N N     . LEU B 1 320 ? 18.690  -25.034 53.639 1.00 21.32 ?  320 LEU B N     1 
ATOM   5596 C CA    . LEU B 1 320 ? 18.945  -26.468 53.547 1.00 23.90 ?  320 LEU B CA    1 
ATOM   5597 C C     . LEU B 1 320 ? 19.771  -26.931 54.739 1.00 17.12 ?  320 LEU B C     1 
ATOM   5598 O O     . LEU B 1 320 ? 20.802  -26.337 55.054 1.00 29.08 ?  320 LEU B O     1 
ATOM   5599 C CB    . LEU B 1 320 ? 19.639  -26.823 52.235 1.00 29.13 ?  320 LEU B CB    1 
ATOM   5600 C CG    . LEU B 1 320 ? 19.455  -28.282 51.817 1.00 27.39 ?  320 LEU B CG    1 
ATOM   5601 C CD1   . LEU B 1 320 ? 18.115  -28.484 51.111 1.00 17.63 ?  320 LEU B CD1   1 
ATOM   5602 C CD2   . LEU B 1 320 ? 20.607  -28.733 50.937 1.00 26.15 ?  320 LEU B CD2   1 
ATOM   5603 N N     . TRP B 1 321 ? 19.291  -27.971 55.409 1.00 13.38 ?  321 TRP B N     1 
ATOM   5604 C CA    . TRP B 1 321 ? 19.832  -28.456 56.678 1.00 20.63 ?  321 TRP B CA    1 
ATOM   5605 C C     . TRP B 1 321 ? 20.474  -29.820 56.444 1.00 20.43 ?  321 TRP B C     1 
ATOM   5606 O O     . TRP B 1 321 ? 19.771  -30.808 56.202 1.00 17.12 ?  321 TRP B O     1 
ATOM   5607 C CB    . TRP B 1 321 ? 18.709  -28.533 57.712 1.00 7.27  ?  321 TRP B CB    1 
ATOM   5608 C CG    . TRP B 1 321 ? 19.119  -28.798 59.115 1.00 14.50 ?  321 TRP B CG    1 
ATOM   5609 C CD1   . TRP B 1 321 ? 18.723  -29.841 59.892 1.00 30.14 ?  321 TRP B CD1   1 
ATOM   5610 C CD2   . TRP B 1 321 ? 19.958  -27.989 59.932 1.00 8.91  ?  321 TRP B CD2   1 
ATOM   5611 N NE1   . TRP B 1 321 ? 19.274  -29.742 61.140 1.00 22.89 ?  321 TRP B NE1   1 
ATOM   5612 C CE2   . TRP B 1 321 ? 20.041  -28.612 61.189 1.00 16.76 ?  321 TRP B CE2   1 
ATOM   5613 C CE3   . TRP B 1 321 ? 20.658  -26.807 59.722 1.00 15.22 ?  321 TRP B CE3   1 
ATOM   5614 C CZ2   . TRP B 1 321 ? 20.799  -28.099 62.222 1.00 13.25 ?  321 TRP B CZ2   1 
ATOM   5615 C CZ3   . TRP B 1 321 ? 21.396  -26.303 60.748 1.00 17.01 ?  321 TRP B CZ3   1 
ATOM   5616 C CH2   . TRP B 1 321 ? 21.463  -26.945 61.984 1.00 7.05  ?  321 TRP B CH2   1 
ATOM   5617 N N     . ILE B 1 322 ? 21.798  -29.892 56.576 1.00 26.09 ?  322 ILE B N     1 
ATOM   5618 C CA    . ILE B 1 322 ? 22.569  -31.039 56.107 1.00 24.59 ?  322 ILE B CA    1 
ATOM   5619 C C     . ILE B 1 322 ? 23.325  -31.644 57.279 1.00 18.42 ?  322 ILE B C     1 
ATOM   5620 O O     . ILE B 1 322 ? 23.914  -30.920 58.087 1.00 19.51 ?  322 ILE B O     1 
ATOM   5621 C CB    . ILE B 1 322 ? 23.538  -30.653 54.980 1.00 17.38 ?  322 ILE B CB    1 
ATOM   5622 C CG1   . ILE B 1 322 ? 22.880  -29.664 54.026 1.00 17.63 ?  322 ILE B CG1   1 
ATOM   5623 C CG2   . ILE B 1 322 ? 23.952  -31.871 54.218 1.00 21.12 ?  322 ILE B CG2   1 
ATOM   5624 C CD1   . ILE B 1 322 ? 23.856  -28.790 53.282 1.00 22.24 ?  322 ILE B CD1   1 
ATOM   5625 N N     . ASP B 1 323 ? 23.261  -32.969 57.396 1.00 26.33 ?  323 ASP B N     1 
ATOM   5626 C CA    . ASP B 1 323 ? 23.984  -33.681 58.436 1.00 7.06  ?  323 ASP B CA    1 
ATOM   5627 C C     . ASP B 1 323 ? 25.373  -34.042 57.940 1.00 14.19 ?  323 ASP B C     1 
ATOM   5628 O O     . ASP B 1 323 ? 25.522  -34.674 56.886 1.00 27.64 ?  323 ASP B O     1 
ATOM   5629 C CB    . ASP B 1 323 ? 23.225  -34.926 58.866 1.00 9.83  ?  323 ASP B CB    1 
ATOM   5630 C CG    . ASP B 1 323 ? 23.691  -35.428 60.193 1.00 19.72 ?  323 ASP B CG    1 
ATOM   5631 O OD1   . ASP B 1 323 ? 24.557  -34.740 60.778 1.00 17.97 ?  323 ASP B OD1   1 
ATOM   5632 O OD2   . ASP B 1 323 ? 23.216  -36.497 60.643 1.00 16.43 -1 323 ASP B OD2   1 
ATOM   5633 N N     . CYS B 1 324 ? 26.352  -33.649 58.746 1.00 23.65 ?  324 CYS B N     1 
ATOM   5634 C CA    . CYS B 1 324 ? 27.768  -33.884 58.410 1.00 28.35 ?  324 CYS B CA    1 
ATOM   5635 C C     . CYS B 1 324 ? 28.350  -34.754 59.527 1.00 27.52 ?  324 CYS B C     1 
ATOM   5636 O O     . CYS B 1 324 ? 29.545  -34.766 59.589 1.00 15.00 ?  324 CYS B O     1 
ATOM   5637 C CB    . CYS B 1 324 ? 28.503  -32.545 58.275 1.00 29.99 ?  324 CYS B CB    1 
ATOM   5638 S SG    . CYS B 1 324 ? 27.928  -31.356 57.040 1.00 17.97 ?  324 CYS B SG    1 
ATOM   5639 N N     . SER B 1 325 ? 27.526  -35.600 60.200 1.00 30.33 ?  325 SER B N     1 
ATOM   5640 C CA    . SER B 1 325 ? 27.940  -36.361 61.375 1.00 23.42 ?  325 SER B CA    1 
ATOM   5641 C C     . SER B 1 325 ? 28.826  -37.549 60.992 1.00 32.69 ?  325 SER B C     1 
ATOM   5642 O O     . SER B 1 325 ? 29.762  -37.887 61.727 1.00 40.87 ?  325 SER B O     1 
ATOM   5643 C CB    . SER B 1 325 ? 26.688  -36.831 62.137 1.00 9.72  ?  325 SER B CB    1 
ATOM   5644 O OG    . SER B 1 325 ? 26.934  -37.256 63.478 1.00 24.28 ?  325 SER B OG    1 
ATOM   5645 N N     . ALA B 1 326 ? 28.575  -38.166 59.837 1.00 27.43 ?  326 ALA B N     1 
ATOM   5646 C CA    . ALA B 1 326 ? 29.382  -39.304 59.406 1.00 32.02 ?  326 ALA B CA    1 
ATOM   5647 C C     . ALA B 1 326 ? 30.842  -38.922 59.121 1.00 29.52 ?  326 ALA B C     1 
ATOM   5648 O O     . ALA B 1 326 ? 31.717  -39.800 59.109 1.00 29.21 ?  326 ALA B O     1 
ATOM   5649 C CB    . ALA B 1 326 ? 28.712  -39.969 58.198 1.00 24.85 ?  326 ALA B CB    1 
ATOM   5650 N N     . LEU B 1 327 ? 31.127  -37.632 58.943 1.00 30.06 ?  327 LEU B N     1 
ATOM   5651 C CA    . LEU B 1 327 ? 32.473  -37.144 58.653 1.00 21.78 ?  327 LEU B CA    1 
ATOM   5652 C C     . LEU B 1 327 ? 33.386  -37.149 59.882 1.00 28.10 ?  327 LEU B C     1 
ATOM   5653 O O     . LEU B 1 327 ? 34.611  -37.159 59.722 1.00 41.84 ?  327 LEU B O     1 
ATOM   5654 C CB    . LEU B 1 327 ? 32.397  -35.716 58.077 1.00 8.09  ?  327 LEU B CB    1 
ATOM   5655 C CG    . LEU B 1 327 ? 31.818  -35.495 56.677 1.00 19.55 ?  327 LEU B CG    1 
ATOM   5656 C CD1   . LEU B 1 327 ? 32.382  -34.239 56.057 1.00 30.49 ?  327 LEU B CD1   1 
ATOM   5657 C CD2   . LEU B 1 327 ? 32.099  -36.687 55.766 1.00 24.24 ?  327 LEU B CD2   1 
ATOM   5658 N N     . ASN B 1 328 ? 32.826  -37.154 61.091 1.00 25.13 ?  328 ASN B N     1 
ATOM   5659 C CA    . ASN B 1 328 ? 33.597  -37.114 62.332 1.00 28.22 ?  328 ASN B CA    1 
ATOM   5660 C C     . ASN B 1 328 ? 34.584  -35.950 62.289 1.00 32.23 ?  328 ASN B C     1 
ATOM   5661 O O     . ASN B 1 328 ? 35.796  -36.106 62.449 1.00 19.64 ?  328 ASN B O     1 
ATOM   5662 C CB    . ASN B 1 328 ? 34.324  -38.444 62.586 1.00 26.85 ?  328 ASN B CB    1 
ATOM   5663 C CG    . ASN B 1 328 ? 33.377  -39.634 62.719 1.00 36.20 ?  328 ASN B CG    1 
ATOM   5664 O OD1   . ASN B 1 328 ? 32.203  -39.493 63.065 1.00 39.19 ?  328 ASN B OD1   1 
ATOM   5665 N ND2   . ASN B 1 328 ? 33.896  -40.825 62.438 1.00 45.39 ?  328 ASN B ND2   1 
ATOM   5666 N N     . LEU B 1 329 ? 34.019  -34.758 62.130 1.00 32.56 ?  329 LEU B N     1 
ATOM   5667 C CA    . LEU B 1 329 ? 34.767  -33.516 62.035 1.00 14.80 ?  329 LEU B CA    1 
ATOM   5668 C C     . LEU B 1 329 ? 34.314  -32.580 63.133 1.00 9.16  ?  329 LEU B C     1 
ATOM   5669 O O     . LEU B 1 329 ? 33.141  -32.568 63.506 1.00 36.27 ?  329 LEU B O     1 
ATOM   5670 C CB    . LEU B 1 329 ? 34.566  -32.844 60.670 1.00 7.66  ?  329 LEU B CB    1 
ATOM   5671 C CG    . LEU B 1 329 ? 35.053  -33.606 59.430 1.00 18.98 ?  329 LEU B CG    1 
ATOM   5672 C CD1   . LEU B 1 329 ? 34.661  -32.859 58.189 1.00 8.22  ?  329 LEU B CD1   1 
ATOM   5673 C CD2   . LEU B 1 329 ? 36.577  -33.854 59.447 1.00 22.78 ?  329 LEU B CD2   1 
ATOM   5674 N N     . SER B 1 330 ? 35.254  -31.826 63.676 1.00 14.39 ?  330 SER B N     1 
ATOM   5675 C CA    . SER B 1 330 ? 34.890  -30.760 64.590 1.00 21.82 ?  330 SER B CA    1 
ATOM   5676 C C     . SER B 1 330 ? 34.297  -29.582 63.822 1.00 34.51 ?  330 SER B C     1 
ATOM   5677 O O     . SER B 1 330 ? 34.393  -29.484 62.593 1.00 27.22 ?  330 SER B O     1 
ATOM   5678 C CB    . SER B 1 330 ? 36.118  -30.289 65.385 1.00 16.48 ?  330 SER B CB    1 
ATOM   5679 O OG    . SER B 1 330 ? 36.708  -29.155 64.768 1.00 22.17 ?  330 SER B OG    1 
ATOM   5680 N N     . GLN B 1 331 ? 33.669  -28.634 64.554 1.00 34.90 ?  331 GLN B N     1 
ATOM   5681 C CA    . GLN B 1 331 ? 33.213  -27.364 63.932 1.00 12.47 ?  331 GLN B CA    1 
ATOM   5682 C C     . GLN B 1 331 ? 34.443  -26.577 63.487 1.00 14.74 ?  331 GLN B C     1 
ATOM   5683 O O     . GLN B 1 331 ? 34.423  -26.058 62.398 1.00 10.52 ?  331 GLN B O     1 
ATOM   5684 C CB    . GLN B 1 331 ? 32.421  -26.532 64.918 1.00 16.36 ?  331 GLN B CB    1 
ATOM   5685 C CG    . GLN B 1 331 ? 31.787  -25.302 64.319 1.00 6.16  ?  331 GLN B CG    1 
ATOM   5686 C CD    . GLN B 1 331 ? 31.275  -24.505 65.482 1.00 18.43 ?  331 GLN B CD    1 
ATOM   5687 O OE1   . GLN B 1 331 ? 31.176  -25.007 66.594 1.00 21.30 ?  331 GLN B OE1   1 
ATOM   5688 N NE2   . GLN B 1 331 ? 30.979  -23.246 65.234 1.00 25.07 ?  331 GLN B NE2   1 
ATOM   5689 N N     . ASP B 1 332 ? 35.506  -26.597 64.290 1.00 24.19 ?  332 ASP B N     1 
ATOM   5690 C CA    . ASP B 1 332 ? 36.719  -25.926 63.832 1.00 19.64 ?  332 ASP B CA    1 
ATOM   5691 C C     . ASP B 1 332 ? 37.323  -26.653 62.642 1.00 21.27 ?  332 ASP B C     1 
ATOM   5692 O O     . ASP B 1 332 ? 37.805  -26.019 61.699 1.00 28.28 ?  332 ASP B O     1 
ATOM   5693 C CB    . ASP B 1 332 ? 37.746  -25.857 64.962 1.00 7.99  ?  332 ASP B CB    1 
ATOM   5694 C CG    . ASP B 1 332 ? 37.162  -25.348 66.266 1.00 26.17 ?  332 ASP B CG    1 
ATOM   5695 O OD1   . ASP B 1 332 ? 36.812  -24.150 66.359 1.00 33.24 ?  332 ASP B OD1   1 
ATOM   5696 O OD2   . ASP B 1 332 ? 37.028  -26.161 67.202 1.00 27.89 -1 332 ASP B OD2   1 
ATOM   5697 N N     . GLU B 1 333 ? 37.285  -27.986 62.652 1.00 30.13 ?  333 GLU B N     1 
ATOM   5698 C CA    . GLU B 1 333 ? 37.734  -28.745 61.488 1.00 35.17 ?  333 GLU B CA    1 
ATOM   5699 C C     . GLU B 1 333 ? 36.885  -28.444 60.263 1.00 29.28 ?  333 GLU B C     1 
ATOM   5700 O O     . GLU B 1 333 ? 37.412  -28.205 59.174 1.00 26.40 ?  333 GLU B O     1 
ATOM   5701 C CB    . GLU B 1 333 ? 37.732  -30.237 61.805 1.00 39.35 ?  333 GLU B CB    1 
ATOM   5702 C CG    . GLU B 1 333 ? 39.087  -30.747 62.255 1.00 26.06 ?  333 GLU B CG    1 
ATOM   5703 C CD    . GLU B 1 333 ? 38.994  -32.059 62.962 1.00 17.87 ?  333 GLU B CD    1 
ATOM   5704 O OE1   . GLU B 1 333 ? 37.884  -32.431 63.379 1.00 20.01 ?  333 GLU B OE1   1 
ATOM   5705 O OE2   . GLU B 1 333 ? 40.036  -32.712 63.121 1.00 20.99 -1 333 GLU B OE2   1 
ATOM   5706 N N     . ARG B 1 334 ? 35.560  -28.449 60.428 1.00 38.43 ?  334 ARG B N     1 
ATOM   5707 C CA    . ARG B 1 334 ? 34.650  -28.220 59.306 1.00 33.84 ?  334 ARG B CA    1 
ATOM   5708 C C     . ARG B 1 334 ? 34.725  -26.782 58.800 1.00 28.51 ?  334 ARG B C     1 
ATOM   5709 O O     . ARG B 1 334 ? 34.792  -26.552 57.586 1.00 23.38 ?  334 ARG B O     1 
ATOM   5710 C CB    . ARG B 1 334 ? 33.222  -28.569 59.733 1.00 33.59 ?  334 ARG B CB    1 
ATOM   5711 C CG    . ARG B 1 334 ? 32.181  -28.509 58.639 1.00 25.88 ?  334 ARG B CG    1 
ATOM   5712 C CD    . ARG B 1 334 ? 30.846  -29.022 59.140 1.00 14.77 ?  334 ARG B CD    1 
ATOM   5713 N NE    . ARG B 1 334 ? 30.206  -28.224 60.188 1.00 6.89  ?  334 ARG B NE    1 
ATOM   5714 C CZ    . ARG B 1 334 ? 29.968  -28.672 61.416 1.00 13.54 ?  334 ARG B CZ    1 
ATOM   5715 N NH1   . ARG B 1 334 ? 30.341  -29.902 61.743 1.00 42.01 1  334 ARG B NH1   1 
ATOM   5716 N NH2   . ARG B 1 334 ? 29.360  -27.914 62.308 1.00 6.36  ?  334 ARG B NH2   1 
ATOM   5717 N N     . THR B 1 335 ? 34.710  -25.799 59.710 1.00 19.36 ?  335 THR B N     1 
ATOM   5718 C CA    . THR B 1 335 ? 34.700  -24.398 59.282 1.00 22.65 ?  335 THR B CA    1 
ATOM   5719 C C     . THR B 1 335 ? 35.953  -24.045 58.487 1.00 30.14 ?  335 THR B C     1 
ATOM   5720 O O     . THR B 1 335 ? 35.874  -23.479 57.390 1.00 29.97 ?  335 THR B O     1 
ATOM   5721 C CB    . THR B 1 335 ? 34.598  -23.473 60.490 1.00 7.41  ?  335 THR B CB    1 
ATOM   5722 O OG1   . THR B 1 335 ? 33.247  -23.426 60.953 1.00 21.41 ?  335 THR B OG1   1 
ATOM   5723 C CG2   . THR B 1 335 ? 35.046  -22.103 60.100 1.00 7.51  ?  335 THR B CG2   1 
ATOM   5724 N N     . LYS B 1 336 ? 37.112  -24.450 58.979 1.00 25.91 ?  336 LYS B N     1 
ATOM   5725 C CA    . LYS B 1 336 ? 38.370  -24.072 58.330 1.00 26.03 ?  336 LYS B CA    1 
ATOM   5726 C C     . LYS B 1 336 ? 38.397  -24.752 56.976 1.00 34.90 ?  336 LYS B C     1 
ATOM   5727 O O     . LYS B 1 336 ? 38.704  -24.097 56.001 1.00 38.58 ?  336 LYS B O     1 
ATOM   5728 C CB    . LYS B 1 336 ? 39.506  -24.442 59.274 1.00 25.54 ?  336 LYS B CB    1 
ATOM   5729 C CG    . LYS B 1 336 ? 40.866  -23.834 58.996 1.00 24.65 ?  336 LYS B CG    1 
ATOM   5730 C CD    . LYS B 1 336 ? 41.957  -24.641 59.649 1.00 24.47 ?  336 LYS B CD    1 
ATOM   5731 C CE    . LYS B 1 336 ? 43.189  -23.829 59.978 1.00 28.26 ?  336 LYS B CE    1 
ATOM   5732 N NZ    . LYS B 1 336 ? 44.238  -23.997 58.947 1.00 33.15 1  336 LYS B NZ    1 
ATOM   5733 N N     . LEU B 1 337 ? 38.014  -26.011 56.946 1.00 29.78 ?  337 LEU B N     1 
ATOM   5734 C CA    . LEU B 1 337 ? 38.079  -26.739 55.687 1.00 26.12 ?  337 LEU B CA    1 
ATOM   5735 C C     . LEU B 1 337 ? 37.185  -26.104 54.635 1.00 13.31 ?  337 LEU B C     1 
ATOM   5736 O O     . LEU B 1 337 ? 37.636  -25.828 53.523 1.00 17.69 ?  337 LEU B O     1 
ATOM   5737 C CB    . LEU B 1 337 ? 37.683  -28.196 55.919 1.00 32.37 ?  337 LEU B CB    1 
ATOM   5738 C CG    . LEU B 1 337 ? 38.394  -29.233 55.061 1.00 30.28 ?  337 LEU B CG    1 
ATOM   5739 C CD1   . LEU B 1 337 ? 39.891  -29.013 55.109 1.00 27.32 ?  337 LEU B CD1   1 
ATOM   5740 C CD2   . LEU B 1 337 ? 38.027  -30.627 55.563 1.00 36.46 ?  337 LEU B CD2   1 
ATOM   5741 N N     . LEU B 1 338 ? 35.951  -25.757 55.013 1.00 18.53 ?  338 LEU B N     1 
ATOM   5742 C CA    . LEU B 1 338 ? 35.003  -25.188 54.060 1.00 11.78 ?  338 LEU B CA    1 
ATOM   5743 C C     . LEU B 1 338 ? 35.499  -23.852 53.525 1.00 23.33 ?  338 LEU B C     1 
ATOM   5744 O O     . LEU B 1 338 ? 35.322  -23.544 52.343 1.00 30.43 ?  338 LEU B O     1 
ATOM   5745 C CB    . LEU B 1 338 ? 33.633  -25.034 54.715 1.00 24.90 ?  338 LEU B CB    1 
ATOM   5746 C CG    . LEU B 1 338 ? 32.852  -26.291 55.125 1.00 22.84 ?  338 LEU B CG    1 
ATOM   5747 C CD1   . LEU B 1 338 ? 31.897  -25.988 56.266 1.00 25.98 ?  338 LEU B CD1   1 
ATOM   5748 C CD2   . LEU B 1 338 ? 32.085  -26.896 53.969 1.00 16.66 ?  338 LEU B CD2   1 
ATOM   5749 N N     . GLU B 1 339 ? 36.161  -23.064 54.371 1.00 33.33 ?  339 GLU B N     1 
ATOM   5750 C CA    . GLU B 1 339 ? 36.681  -21.769 53.943 1.00 30.49 ?  339 GLU B CA    1 
ATOM   5751 C C     . GLU B 1 339 ? 37.935  -21.924 53.083 1.00 32.36 ?  339 GLU B C     1 
ATOM   5752 O O     . GLU B 1 339 ? 38.058  -21.281 52.034 1.00 31.68 ?  339 GLU B O     1 
ATOM   5753 C CB    . GLU B 1 339 ? 36.979  -20.937 55.193 1.00 42.02 ?  339 GLU B CB    1 
ATOM   5754 C CG    . GLU B 1 339 ? 37.513  -19.538 54.993 1.00 49.98 ?  339 GLU B CG    1 
ATOM   5755 C CD    . GLU B 1 339 ? 37.825  -18.858 56.329 1.00 61.46 ?  339 GLU B CD    1 
ATOM   5756 O OE1   . GLU B 1 339 ? 37.769  -19.540 57.380 1.00 63.32 ?  339 GLU B OE1   1 
ATOM   5757 O OE2   . GLU B 1 339 ? 38.110  -17.642 56.333 1.00 63.95 -1 339 GLU B OE2   1 
ATOM   5758 N N     . GLU B 1 340 ? 38.835  -22.830 53.458 1.00 35.35 ?  340 GLU B N     1 
ATOM   5759 C CA    . GLU B 1 340 ? 40.139  -23.004 52.768 1.00 27.14 ?  340 GLU B CA    1 
ATOM   5760 C C     . GLU B 1 340 ? 40.007  -23.623 51.379 1.00 24.48 ?  340 GLU B C     1 
ATOM   5761 O O     . GLU B 1 340 ? 40.480  -23.033 50.442 1.00 35.07 ?  340 GLU B O     1 
ATOM   5762 C CB    . GLU B 1 340 ? 40.993  -23.925 53.617 1.00 34.92 ?  340 GLU B CB    1 
ATOM   5763 C CG    . GLU B 1 340 ? 41.619  -23.298 54.830 1.00 42.14 ?  340 GLU B CG    1 
ATOM   5764 C CD    . GLU B 1 340 ? 42.235  -24.410 55.649 1.00 51.05 ?  340 GLU B CD    1 
ATOM   5765 O OE1   . GLU B 1 340 ? 41.772  -25.549 55.507 1.00 51.46 ?  340 GLU B OE1   1 
ATOM   5766 O OE2   . GLU B 1 340 ? 43.181  -24.144 56.396 1.00 49.24 -1 340 GLU B OE2   1 
ATOM   5767 N N     . LYS B 1 341 ? 39.484  -24.831 51.283 1.00 24.42 ?  341 LYS B N     1 
ATOM   5768 C CA    . LYS B 1 341 ? 39.391  -25.476 49.983 1.00 35.41 ?  341 LYS B CA    1 
ATOM   5769 C C     . LYS B 1 341 ? 38.023  -25.279 49.353 1.00 35.24 ?  341 LYS B C     1 
ATOM   5770 O O     . LYS B 1 341 ? 37.921  -25.150 48.127 1.00 39.14 ?  341 LYS B O     1 
ATOM   5771 C CB    . LYS B 1 341 ? 39.737  -26.963 50.096 1.00 42.59 ?  341 LYS B CB    1 
ATOM   5772 C CG    . LYS B 1 341 ? 38.940  -27.723 51.122 1.00 46.00 ?  341 LYS B CG    1 
ATOM   5773 C CD    . LYS B 1 341 ? 39.582  -29.068 51.402 1.00 44.25 ?  341 LYS B CD    1 
ATOM   5774 C CE    . LYS B 1 341 ? 39.791  -29.862 50.118 1.00 43.07 ?  341 LYS B CE    1 
ATOM   5775 N NZ    . LYS B 1 341 ? 40.699  -31.018 50.328 1.00 30.81 1  341 LYS B NZ    1 
ATOM   5776 N N     . GLY B 1 342 ? 36.967  -25.259 50.164 1.00 33.50 ?  342 GLY B N     1 
ATOM   5777 C CA    . GLY B 1 342 ? 35.647  -24.995 49.627 1.00 23.52 ?  342 GLY B CA    1 
ATOM   5778 C C     . GLY B 1 342 ? 35.483  -23.563 49.157 1.00 32.30 ?  342 GLY B C     1 
ATOM   5779 O O     . GLY B 1 342 ? 34.818  -23.313 48.154 1.00 41.11 ?  342 GLY B O     1 
ATOM   5780 N N     . LYS B 1 343 ? 36.101  -22.607 49.859 1.00 32.71 ?  343 LYS B N     1 
ATOM   5781 C CA    . LYS B 1 343 ? 35.931  -21.182 49.564 1.00 26.16 ?  343 LYS B CA    1 
ATOM   5782 C C     . LYS B 1 343 ? 34.449  -20.808 49.571 1.00 30.28 ?  343 LYS B C     1 
ATOM   5783 O O     . LYS B 1 343 ? 33.930  -20.186 48.642 1.00 31.86 ?  343 LYS B O     1 
ATOM   5784 C CB    . LYS B 1 343 ? 36.589  -20.799 48.237 1.00 29.24 ?  343 LYS B CB    1 
ATOM   5785 C CG    . LYS B 1 343 ? 38.054  -21.220 48.099 1.00 43.77 ?  343 LYS B CG    1 
ATOM   5786 C CD    . LYS B 1 343 ? 39.026  -20.193 48.694 1.00 38.55 ?  343 LYS B CD    1 
ATOM   5787 C CE    . LYS B 1 343 ? 40.460  -20.515 48.284 1.00 26.92 ?  343 LYS B CE    1 
ATOM   5788 N NZ    . LYS B 1 343 ? 41.437  -20.323 49.404 1.00 24.93 1  343 LYS B NZ    1 
ATOM   5789 N N     . ILE B 1 344 ? 33.762  -21.213 50.633 1.00 16.68 ?  344 ILE B N     1 
ATOM   5790 C CA    . ILE B 1 344 ? 32.326  -21.032 50.755 1.00 16.03 ?  344 ILE B CA    1 
ATOM   5791 C C     . ILE B 1 344 ? 32.021  -20.754 52.222 1.00 22.64 ?  344 ILE B C     1 
ATOM   5792 O O     . ILE B 1 344 ? 32.711  -21.253 53.119 1.00 28.15 ?  344 ILE B O     1 
ATOM   5793 C CB    . ILE B 1 344 ? 31.551  -22.256 50.191 1.00 26.14 ?  344 ILE B CB    1 
ATOM   5794 C CG1   . ILE B 1 344 ? 30.067  -22.203 50.538 1.00 36.16 ?  344 ILE B CG1   1 
ATOM   5795 C CG2   . ILE B 1 344 ? 32.123  -23.579 50.663 1.00 25.84 ?  344 ILE B CG2   1 
ATOM   5796 C CD1   . ILE B 1 344 ? 29.270  -23.285 49.851 1.00 41.87 ?  344 ILE B CD1   1 
ATOM   5797 N N     . ILE B 1 345 ? 31.060  -19.865 52.462 1.00 33.43 ?  345 ILE B N     1 
ATOM   5798 C CA    . ILE B 1 345 ? 30.667  -19.471 53.811 1.00 29.36 ?  345 ILE B CA    1 
ATOM   5799 C C     . ILE B 1 345 ? 29.257  -19.959 54.084 1.00 37.07 ?  345 ILE B C     1 
ATOM   5800 O O     . ILE B 1 345 ? 28.298  -19.534 53.422 1.00 39.70 ?  345 ILE B O     1 
ATOM   5801 C CB    . ILE B 1 345 ? 30.735  -17.957 54.017 1.00 26.25 ?  345 ILE B CB    1 
ATOM   5802 C CG1   . ILE B 1 345 ? 32.146  -17.440 53.695 1.00 27.13 ?  345 ILE B CG1   1 
ATOM   5803 C CG2   . ILE B 1 345 ? 30.248  -17.625 55.423 1.00 8.16  ?  345 ILE B CG2   1 
ATOM   5804 C CD1   . ILE B 1 345 ? 33.296  -18.148 54.410 1.00 19.42 ?  345 ILE B CD1   1 
ATOM   5805 N N     . VAL B 1 346 ? 29.132  -20.849 55.059 1.00 37.66 ?  346 VAL B N     1 
ATOM   5806 C CA    . VAL B 1 346 ? 27.823  -21.316 55.490 1.00 32.82 ?  346 VAL B CA    1 
ATOM   5807 C C     . VAL B 1 346 ? 27.599  -20.993 56.963 1.00 24.96 ?  346 VAL B C     1 
ATOM   5808 O O     . VAL B 1 346 ? 28.487  -20.476 57.660 1.00 9.87  ?  346 VAL B O     1 
ATOM   5809 C CB    . VAL B 1 346 ? 27.669  -22.823 55.238 1.00 17.81 ?  346 VAL B CB    1 
ATOM   5810 C CG1   . VAL B 1 346 ? 27.879  -23.134 53.780 1.00 25.88 ?  346 VAL B CG1   1 
ATOM   5811 C CG2   . VAL B 1 346 ? 28.651  -23.579 56.097 1.00 10.14 ?  346 VAL B CG2   1 
ATOM   5812 N N     . GLU B 1 347 ? 26.446  -21.303 57.432 1.00 12.72 ?  347 GLU B N     1 
ATOM   5813 C CA    . GLU B 1 347 ? 26.172  -21.119 58.841 1.00 17.09 ?  347 GLU B CA    1 
ATOM   5814 C C     . GLU B 1 347 ? 26.657  -22.347 59.600 1.00 35.72 ?  347 GLU B C     1 
ATOM   5815 O O     . GLU B 1 347 ? 26.432  -23.478 59.146 1.00 35.84 ?  347 GLU B O     1 
ATOM   5816 C CB    . GLU B 1 347 ? 24.683  -20.897 59.080 1.00 22.74 ?  347 GLU B CB    1 
ATOM   5817 C CG    . GLU B 1 347 ? 24.356  -19.909 60.199 1.00 29.66 ?  347 GLU B CG    1 
ATOM   5818 C CD    . GLU B 1 347 ? 24.630  -18.461 59.805 1.00 44.71 ?  347 GLU B CD    1 
ATOM   5819 O OE1   . GLU B 1 347 ? 23.678  -17.732 59.453 1.00 60.43 ?  347 GLU B OE1   1 
ATOM   5820 O OE2   . GLU B 1 347 ? 25.802  -18.038 59.852 1.00 48.05 -1 347 GLU B OE2   1 
ATOM   5821 N N     . PRO B 1 348 ? 27.435  -22.189 60.666 1.00 38.18 ?  348 PRO B N     1 
ATOM   5822 C CA    . PRO B 1 348 ? 27.689  -23.341 61.532 1.00 17.39 ?  348 PRO B CA    1 
ATOM   5823 C C     . PRO B 1 348 ? 26.416  -23.668 62.290 1.00 23.37 ?  348 PRO B C     1 
ATOM   5824 O O     . PRO B 1 348 ? 25.743  -22.783 62.822 1.00 29.65 ?  348 PRO B O     1 
ATOM   5825 C CB    . PRO B 1 348 ? 28.793  -22.847 62.473 1.00 12.82 ?  348 PRO B CB    1 
ATOM   5826 C CG    . PRO B 1 348 ? 28.669  -21.357 62.442 1.00 14.45 ?  348 PRO B CG    1 
ATOM   5827 C CD    . PRO B 1 348 ? 28.220  -21.009 61.063 1.00 28.11 ?  348 PRO B CD    1 
ATOM   5828 N N     . GLY B 1 349 ? 26.106  -24.958 62.365 1.00 5.78  ?  349 GLY B N     1 
ATOM   5829 C CA    . GLY B 1 349 ? 24.881  -25.391 62.981 1.00 20.89 ?  349 GLY B CA    1 
ATOM   5830 C C     . GLY B 1 349 ? 24.946  -25.544 64.482 1.00 17.30 ?  349 GLY B C     1 
ATOM   5831 O O     . GLY B 1 349 ? 23.895  -25.668 65.126 1.00 13.50 ?  349 GLY B O     1 
ATOM   5832 N N     . GLU B 1 350 ? 26.145  -25.616 65.057 1.00 10.02 ?  350 GLU B N     1 
ATOM   5833 C CA    . GLU B 1 350 ? 26.213  -25.884 66.491 1.00 13.12 ?  350 GLU B CA    1 
ATOM   5834 C C     . GLU B 1 350 ? 25.483  -24.807 67.286 1.00 5.11  ?  350 GLU B C     1 
ATOM   5835 O O     . GLU B 1 350 ? 24.880  -25.108 68.325 1.00 5.53  ?  350 GLU B O     1 
ATOM   5836 C CB    . GLU B 1 350 ? 27.678  -25.991 66.949 1.00 9.67  ?  350 GLU B CB    1 
ATOM   5837 C CG    . GLU B 1 350 ? 28.343  -27.340 66.707 1.00 5.63  ?  350 GLU B CG    1 
ATOM   5838 C CD    . GLU B 1 350 ? 28.886  -27.459 65.307 1.00 5.85  ?  350 GLU B CD    1 
ATOM   5839 O OE1   . GLU B 1 350 ? 29.408  -28.529 64.928 1.00 10.85 ?  350 GLU B OE1   1 
ATOM   5840 O OE2   . GLU B 1 350 ? 28.767  -26.470 64.566 1.00 19.90 -1 350 GLU B OE2   1 
ATOM   5841 N N     . LYS B 1 351 ? 25.410  -23.592 66.756 1.00 5.05  ?  351 LYS B N     1 
ATOM   5842 C CA    . LYS B 1 351 ? 24.672  -22.525 67.423 1.00 25.54 ?  351 LYS B CA    1 
ATOM   5843 C C     . LYS B 1 351 ? 23.144  -22.652 67.264 1.00 21.98 ?  351 LYS B C     1 
ATOM   5844 O O     . LYS B 1 351 ? 22.427  -21.740 67.682 1.00 28.62 ?  351 LYS B O     1 
ATOM   5845 C CB    . LYS B 1 351 ? 25.150  -21.143 66.943 1.00 14.32 ?  351 LYS B CB    1 
ATOM   5846 C CG    . LYS B 1 351 ? 24.973  -20.894 65.443 1.00 21.29 ?  351 LYS B CG    1 
ATOM   5847 C CD    . LYS B 1 351 ? 25.151  -19.414 65.089 1.00 18.89 ?  351 LYS B CD    1 
ATOM   5848 C CE    . LYS B 1 351 ? 24.867  -19.139 63.610 1.00 15.22 ?  351 LYS B CE    1 
ATOM   5849 N NZ    . LYS B 1 351 ? 25.047  -17.705 63.247 1.00 20.26 1  351 LYS B NZ    1 
ATOM   5850 N N     . TYR B 1 352 ? 22.620  -23.732 66.672 1.00 29.62 ?  352 TYR B N     1 
ATOM   5851 C CA    . TYR B 1 352 ? 21.175  -23.967 66.644 1.00 9.70  ?  352 TYR B CA    1 
ATOM   5852 C C     . TYR B 1 352 ? 20.703  -24.828 67.797 1.00 9.26  ?  352 TYR B C     1 
ATOM   5853 O O     . TYR B 1 352 ? 19.521  -25.160 67.860 1.00 31.57 ?  352 TYR B O     1 
ATOM   5854 C CB    . TYR B 1 352 ? 20.745  -24.619 65.329 1.00 5.04  ?  352 TYR B CB    1 
ATOM   5855 C CG    . TYR B 1 352 ? 20.789  -23.680 64.160 1.00 30.15 ?  352 TYR B CG    1 
ATOM   5856 C CD1   . TYR B 1 352 ? 19.743  -22.808 63.906 1.00 27.61 ?  352 TYR B CD1   1 
ATOM   5857 C CD2   . TYR B 1 352 ? 21.890  -23.640 63.323 1.00 38.93 ?  352 TYR B CD2   1 
ATOM   5858 C CE1   . TYR B 1 352 ? 19.794  -21.931 62.849 1.00 8.85  ?  352 TYR B CE1   1 
ATOM   5859 C CE2   . TYR B 1 352 ? 21.942  -22.763 62.256 1.00 31.42 ?  352 TYR B CE2   1 
ATOM   5860 C CZ    . TYR B 1 352 ? 20.886  -21.912 62.029 1.00 8.95  ?  352 TYR B CZ    1 
ATOM   5861 O OH    . TYR B 1 352 ? 20.917  -21.059 60.959 1.00 12.08 ?  352 TYR B OH    1 
ATOM   5862 N N     . GLY B 1 353 ? 21.584  -25.201 68.694 1.00 19.79 ?  353 GLY B N     1 
ATOM   5863 C CA    . GLY B 1 353 ? 21.208  -25.995 69.839 1.00 18.66 ?  353 GLY B CA    1 
ATOM   5864 C C     . GLY B 1 353 ? 21.146  -27.490 69.591 1.00 17.05 ?  353 GLY B C     1 
ATOM   5865 O O     . GLY B 1 353 ? 21.526  -28.007 68.529 1.00 12.18 ?  353 GLY B O     1 
ATOM   5866 N N     . LEU B 1 354 ? 20.600  -28.185 70.587 1.00 9.02  ?  354 LEU B N     1 
ATOM   5867 C CA    . LEU B 1 354 ? 20.575  -29.642 70.585 1.00 5.41  ?  354 LEU B CA    1 
ATOM   5868 C C     . LEU B 1 354 ? 19.966  -30.168 69.299 1.00 7.39  ?  354 LEU B C     1 
ATOM   5869 O O     . LEU B 1 354 ? 18.797  -29.914 69.001 1.00 5.61  ?  354 LEU B O     1 
ATOM   5870 C CB    . LEU B 1 354 ? 19.764  -30.130 71.787 1.00 5.67  ?  354 LEU B CB    1 
ATOM   5871 C CG    . LEU B 1 354 ? 20.495  -29.895 73.104 1.00 5.34  ?  354 LEU B CG    1 
ATOM   5872 C CD1   . LEU B 1 354 ? 19.588  -30.008 74.315 1.00 6.89  ?  354 LEU B CD1   1 
ATOM   5873 C CD2   . LEU B 1 354 ? 21.682  -30.862 73.230 1.00 5.44  ?  354 LEU B CD2   1 
ATOM   5874 N N     . GLY B 1 355 ? 20.745  -30.960 68.572 1.00 8.48  ?  355 GLY B N     1 
ATOM   5875 C CA    . GLY B 1 355 ? 20.377  -31.414 67.248 1.00 10.73 ?  355 GLY B CA    1 
ATOM   5876 C C     . GLY B 1 355 ? 20.976  -30.623 66.112 1.00 21.23 ?  355 GLY B C     1 
ATOM   5877 O O     . GLY B 1 355 ? 20.760  -30.980 64.950 1.00 34.17 ?  355 GLY B O     1 
ATOM   5878 N N     . GLY B 1 356 ? 21.712  -29.560 66.412 1.00 17.51 ?  356 GLY B N     1 
ATOM   5879 C CA    . GLY B 1 356 ? 22.440  -28.818 65.415 1.00 8.16  ?  356 GLY B CA    1 
ATOM   5880 C C     . GLY B 1 356 ? 23.903  -29.198 65.356 1.00 15.86 ?  356 GLY B C     1 
ATOM   5881 O O     . GLY B 1 356 ? 24.627  -28.706 64.489 1.00 21.77 ?  356 GLY B O     1 
ATOM   5882 N N     . GLU B 1 357 ? 24.361  -30.018 66.302 1.00 16.81 ?  357 GLU B N     1 
ATOM   5883 C CA    . GLU B 1 357 ? 25.764  -30.454 66.333 1.00 26.52 ?  357 GLU B CA    1 
ATOM   5884 C C     . GLU B 1 357 ? 26.193  -31.202 65.070 1.00 20.97 ?  357 GLU B C     1 
ATOM   5885 O O     . GLU B 1 357 ? 25.550  -32.161 64.643 1.00 31.10 ?  357 GLU B O     1 
ATOM   5886 C CB    . GLU B 1 357 ? 26.020  -31.332 67.571 1.00 18.84 ?  357 GLU B CB    1 
ATOM   5887 C CG    . GLU B 1 357 ? 24.879  -32.260 67.982 1.00 24.95 ?  357 GLU B CG    1 
ATOM   5888 C CD    . GLU B 1 357 ? 23.791  -31.583 68.817 1.00 30.94 ?  357 GLU B CD    1 
ATOM   5889 O OE1   . GLU B 1 357 ? 23.318  -32.185 69.802 1.00 36.66 ?  357 GLU B OE1   1 
ATOM   5890 O OE2   . GLU B 1 357 ? 23.387  -30.457 68.472 1.00 38.17 -1 357 GLU B OE2   1 
ATOM   5891 N N     . GLU B 1 358 ? 27.331  -30.769 64.579 1.00 25.09 ?  358 GLU B N     1 
ATOM   5892 C CA    . GLU B 1 358 ? 27.949  -31.364 63.391 1.00 22.23 ?  358 GLU B CA    1 
ATOM   5893 C C     . GLU B 1 358 ? 27.044  -31.230 62.158 1.00 17.99 ?  358 GLU B C     1 
ATOM   5894 O O     . GLU B 1 358 ? 27.143  -32.066 61.292 1.00 24.29 ?  358 GLU B O     1 
ATOM   5895 C CB    . GLU B 1 358 ? 28.394  -32.797 63.660 1.00 18.87 ?  358 GLU B CB    1 
ATOM   5896 C CG    . GLU B 1 358 ? 29.542  -32.908 64.619 1.00 19.99 ?  358 GLU B CG    1 
ATOM   5897 C CD    . GLU B 1 358 ? 29.709  -34.356 65.007 1.00 26.02 ?  358 GLU B CD    1 
ATOM   5898 O OE1   . GLU B 1 358 ? 30.380  -35.087 64.274 1.00 35.60 ?  358 GLU B OE1   1 
ATOM   5899 O OE2   . GLU B 1 358 ? 29.134  -34.746 66.024 1.00 26.46 -1 358 GLU B OE2   1 
ATOM   5900 N N     . HIS B 1 359 ? 26.227  -30.200 62.070 1.00 11.34 ?  359 HIS B N     1 
ATOM   5901 C CA    . HIS B 1 359 ? 25.416  -29.879 60.906 1.00 22.95 ?  359 HIS B CA    1 
ATOM   5902 C C     . HIS B 1 359 ? 25.867  -28.558 60.305 1.00 23.47 ?  359 HIS B C     1 
ATOM   5903 O O     . HIS B 1 359 ? 26.603  -27.800 60.923 1.00 20.62 ?  359 HIS B O     1 
ATOM   5904 C CB    . HIS B 1 359 ? 23.939  -29.766 61.266 1.00 25.36 ?  359 HIS B CB    1 
ATOM   5905 C CG    . HIS B 1 359 ? 23.291  -31.058 61.631 1.00 6.19  ?  359 HIS B CG    1 
ATOM   5906 N ND1   . HIS B 1 359 ? 23.286  -31.548 62.917 1.00 6.12  ?  359 HIS B ND1   1 
ATOM   5907 C CD2   . HIS B 1 359 ? 22.574  -31.930 60.892 1.00 6.35  ?  359 HIS B CD2   1 
ATOM   5908 C CE1   . HIS B 1 359 ? 22.609  -32.680 62.953 1.00 6.26  ?  359 HIS B CE1   1 
ATOM   5909 N NE2   . HIS B 1 359 ? 22.168  -32.935 61.736 1.00 9.86  ?  359 HIS B NE2   1 
ATOM   5910 N N     . ILE B 1 360 ? 25.405  -28.295 59.078 1.00 30.86 ?  360 ILE B N     1 
ATOM   5911 C CA    . ILE B 1 360 ? 25.534  -26.990 58.433 1.00 27.42 ?  360 ILE B CA    1 
ATOM   5912 C C     . ILE B 1 360 ? 24.217  -26.612 57.768 1.00 26.89 ?  360 ILE B C     1 
ATOM   5913 O O     . ILE B 1 360 ? 23.422  -27.476 57.386 1.00 16.10 ?  360 ILE B O     1 
ATOM   5914 C CB    . ILE B 1 360 ? 26.653  -26.962 57.384 1.00 18.08 ?  360 ILE B CB    1 
ATOM   5915 C CG1   . ILE B 1 360 ? 26.354  -27.985 56.284 1.00 24.84 ?  360 ILE B CG1   1 
ATOM   5916 C CG2   . ILE B 1 360 ? 27.959  -27.201 58.037 1.00 7.04  ?  360 ILE B CG2   1 
ATOM   5917 C CD1   . ILE B 1 360 ? 27.389  -28.078 55.187 1.00 26.31 ?  360 ILE B CD1   1 
ATOM   5918 N N     . ARG B 1 361 ? 24.002  -25.304 57.607 1.00 26.22 ?  361 ARG B N     1 
ATOM   5919 C CA    . ARG B 1 361 ? 22.835  -24.766 56.921 1.00 6.67  ?  361 ARG B CA    1 
ATOM   5920 C C     . ARG B 1 361 ? 23.252  -23.900 55.745 1.00 7.14  ?  361 ARG B C     1 
ATOM   5921 O O     . ARG B 1 361 ? 24.102  -23.017 55.887 1.00 7.14  ?  361 ARG B O     1 
ATOM   5922 C CB    . ARG B 1 361 ? 21.969  -23.961 57.867 1.00 15.50 ?  361 ARG B CB    1 
ATOM   5923 C CG    . ARG B 1 361 ? 20.554  -23.818 57.374 1.00 13.27 ?  361 ARG B CG    1 
ATOM   5924 C CD    . ARG B 1 361 ? 19.906  -22.662 58.036 1.00 22.17 ?  361 ARG B CD    1 
ATOM   5925 N NE    . ARG B 1 361 ? 20.500  -21.393 57.657 1.00 18.13 ?  361 ARG B NE    1 
ATOM   5926 C CZ    . ARG B 1 361 ? 20.144  -20.256 58.222 1.00 17.73 ?  361 ARG B CZ    1 
ATOM   5927 N NH1   . ARG B 1 361 ? 19.225  -20.280 59.170 1.00 19.20 1  361 ARG B NH1   1 
ATOM   5928 N NH2   . ARG B 1 361 ? 20.701  -19.110 57.858 1.00 30.24 ?  361 ARG B NH2   1 
ATOM   5929 N N     . ILE B 1 362 ? 22.672  -24.162 54.578 1.00 9.95  ?  362 ILE B N     1 
ATOM   5930 C CA    . ILE B 1 362 ? 23.001  -23.405 53.379 1.00 13.50 ?  362 ILE B CA    1 
ATOM   5931 C C     . ILE B 1 362 ? 21.751  -22.720 52.835 1.00 25.35 ?  362 ILE B C     1 
ATOM   5932 O O     . ILE B 1 362 ? 20.616  -23.146 53.076 1.00 15.89 ?  362 ILE B O     1 
ATOM   5933 C CB    . ILE B 1 362 ? 23.654  -24.308 52.313 1.00 35.25 ?  362 ILE B CB    1 
ATOM   5934 C CG1   . ILE B 1 362 ? 22.683  -25.378 51.830 1.00 34.50 ?  362 ILE B CG1   1 
ATOM   5935 C CG2   . ILE B 1 362 ? 24.907  -24.977 52.877 1.00 47.43 ?  362 ILE B CG2   1 
ATOM   5936 C CD1   . ILE B 1 362 ? 23.269  -26.325 50.830 1.00 31.97 ?  362 ILE B CD1   1 
ATOM   5937 N N     . ASN B 1 363 ? 21.974  -21.618 52.117 1.00 32.90 ?  363 ASN B N     1 
ATOM   5938 C CA    . ASN B 1 363 ? 20.912  -20.827 51.513 1.00 24.09 ?  363 ASN B CA    1 
ATOM   5939 C C     . ASN B 1 363 ? 20.761  -21.299 50.077 1.00 18.61 ?  363 ASN B C     1 
ATOM   5940 O O     . ASN B 1 363 ? 21.724  -21.246 49.303 1.00 20.91 ?  363 ASN B O     1 
ATOM   5941 C CB    . ASN B 1 363 ? 21.232  -19.328 51.549 1.00 37.84 ?  363 ASN B CB    1 
ATOM   5942 C CG    . ASN B 1 363 ? 20.024  -18.431 51.173 1.00 38.60 ?  363 ASN B CG    1 
ATOM   5943 O OD1   . ASN B 1 363 ? 19.182  -18.787 50.340 1.00 41.53 ?  363 ASN B OD1   1 
ATOM   5944 N ND2   . ASN B 1 363 ? 19.976  -17.245 51.762 1.00 19.98 ?  363 ASN B ND2   1 
ATOM   5945 N N     . ILE B 1 364 ? 19.563  -21.765 49.733 1.00 10.72 ?  364 ILE B N     1 
ATOM   5946 C CA    . ILE B 1 364 ? 19.233  -22.186 48.379 1.00 21.51 ?  364 ILE B CA    1 
ATOM   5947 C C     . ILE B 1 364 ? 18.323  -21.162 47.702 1.00 27.96 ?  364 ILE B C     1 
ATOM   5948 O O     . ILE B 1 364 ? 17.657  -21.473 46.715 1.00 25.88 ?  364 ILE B O     1 
ATOM   5949 C CB    . ILE B 1 364 ? 18.605  -23.595 48.360 1.00 30.63 ?  364 ILE B CB    1 
ATOM   5950 C CG1   . ILE B 1 364 ? 17.333  -23.653 49.210 1.00 19.80 ?  364 ILE B CG1   1 
ATOM   5951 C CG2   . ILE B 1 364 ? 19.605  -24.658 48.847 1.00 24.98 ?  364 ILE B CG2   1 
ATOM   5952 C CD1   . ILE B 1 364 ? 16.583  -24.945 49.104 1.00 17.57 ?  364 ILE B CD1   1 
ATOM   5953 N N     . GLY B 1 365 ? 18.286  -19.938 48.223 1.00 32.13 ?  365 GLY B N     1 
ATOM   5954 C CA    . GLY B 1 365 ? 17.585  -18.858 47.558 1.00 33.25 ?  365 GLY B CA    1 
ATOM   5955 C C     . GLY B 1 365 ? 18.480  -18.152 46.566 1.00 34.06 ?  365 GLY B C     1 
ATOM   5956 O O     . GLY B 1 365 ? 18.737  -16.955 46.691 1.00 39.49 ?  365 GLY B O     1 
ATOM   5957 N N     . CYS B 1 366 ? 19.009  -18.896 45.610 1.00 36.54 ?  366 CYS B N     1 
ATOM   5958 C CA    . CYS B 1 366 ? 20.010  -18.390 44.688 1.00 37.10 ?  366 CYS B CA    1 
ATOM   5959 C C     . CYS B 1 366 ? 19.707  -18.957 43.313 1.00 35.72 ?  366 CYS B C     1 
ATOM   5960 O O     . CYS B 1 366 ? 18.934  -19.911 43.190 1.00 38.37 ?  366 CYS B O     1 
ATOM   5961 C CB    . CYS B 1 366 ? 21.430  -18.766 45.126 1.00 44.25 ?  366 CYS B CB    1 
ATOM   5962 S SG    . CYS B 1 366 ? 21.749  -20.525 45.163 1.00 45.99 ?  366 CYS B SG    1 
ATOM   5963 N N     . PRO B 1 367 ? 20.231  -18.343 42.255 1.00 38.53 ?  367 PRO B N     1 
ATOM   5964 C CA    . PRO B 1 367 ? 20.141  -18.976 40.932 1.00 39.87 ?  367 PRO B CA    1 
ATOM   5965 C C     . PRO B 1 367 ? 20.781  -20.363 40.936 1.00 46.71 ?  367 PRO B C     1 
ATOM   5966 O O     . PRO B 1 367 ? 21.751  -20.622 41.651 1.00 47.37 ?  367 PRO B O     1 
ATOM   5967 C CB    . PRO B 1 367 ? 20.898  -18.001 40.018 1.00 31.64 ?  367 PRO B CB    1 
ATOM   5968 C CG    . PRO B 1 367 ? 20.858  -16.686 40.746 1.00 26.76 ?  367 PRO B CG    1 
ATOM   5969 C CD    . PRO B 1 367 ? 20.882  -17.020 42.202 1.00 23.02 ?  367 PRO B CD    1 
ATOM   5970 N N     . ARG B 1 368 ? 20.195  -21.277 40.150 1.00 54.88 ?  368 ARG B N     1 
ATOM   5971 C CA    . ARG B 1 368 ? 20.724  -22.637 40.044 1.00 46.37 ?  368 ARG B CA    1 
ATOM   5972 C C     . ARG B 1 368 ? 22.194  -22.645 39.657 1.00 50.76 ?  368 ARG B C     1 
ATOM   5973 O O     . ARG B 1 368 ? 22.942  -23.538 40.071 1.00 53.38 ?  368 ARG B O     1 
ATOM   5974 C CB    . ARG B 1 368 ? 19.916  -23.436 39.024 1.00 43.75 ?  368 ARG B CB    1 
ATOM   5975 C CG    . ARG B 1 368 ? 20.435  -24.844 38.775 1.00 46.92 ?  368 ARG B CG    1 
ATOM   5976 C CD    . ARG B 1 368 ? 20.061  -25.808 39.901 1.00 39.67 ?  368 ARG B CD    1 
ATOM   5977 N NE    . ARG B 1 368 ? 18.654  -25.739 40.294 1.00 28.02 ?  368 ARG B NE    1 
ATOM   5978 C CZ    . ARG B 1 368 ? 17.693  -26.523 39.813 1.00 31.70 ?  368 ARG B CZ    1 
ATOM   5979 N NH1   . ARG B 1 368 ? 17.975  -27.452 38.908 1.00 36.21 1  368 ARG B NH1   1 
ATOM   5980 N NH2   . ARG B 1 368 ? 16.447  -26.389 40.248 1.00 28.80 ?  368 ARG B NH2   1 
ATOM   5981 N N     . SER B 1 369 ? 22.616  -21.682 38.830 1.00 52.33 ?  369 SER B N     1 
ATOM   5982 C CA    . SER B 1 369 ? 24.036  -21.492 38.545 1.00 44.37 ?  369 SER B CA    1 
ATOM   5983 C C     . SER B 1 369 ? 24.835  -21.344 39.833 1.00 38.13 ?  369 SER B C     1 
ATOM   5984 O O     . SER B 1 369 ? 25.867  -21.996 40.021 1.00 43.80 ?  369 SER B O     1 
ATOM   5985 C CB    . SER B 1 369 ? 24.233  -20.266 37.648 1.00 41.18 ?  369 SER B CB    1 
ATOM   5986 O OG    . SER B 1 369 ? 24.106  -19.060 38.382 1.00 32.22 ?  369 SER B OG    1 
ATOM   5987 N N     . VAL B 1 370 ? 24.371  -20.468 40.725 1.00 25.18 ?  370 VAL B N     1 
ATOM   5988 C CA    . VAL B 1 370 ? 25.021  -20.282 42.018 1.00 29.30 ?  370 VAL B CA    1 
ATOM   5989 C C     . VAL B 1 370 ? 24.946  -21.565 42.837 1.00 38.13 ?  370 VAL B C     1 
ATOM   5990 O O     . VAL B 1 370 ? 25.935  -21.992 43.442 1.00 42.17 ?  370 VAL B O     1 
ATOM   5991 C CB    . VAL B 1 370 ? 24.375  -19.088 42.756 1.00 32.79 ?  370 VAL B CB    1 
ATOM   5992 C CG1   . VAL B 1 370 ? 24.992  -18.876 44.129 1.00 35.71 ?  370 VAL B CG1   1 
ATOM   5993 C CG2   . VAL B 1 370 ? 24.468  -17.809 41.913 1.00 29.60 ?  370 VAL B CG2   1 
ATOM   5994 N N     . LEU B 1 371 ? 23.784  -22.229 42.829 1.00 51.07 ?  371 LEU B N     1 
ATOM   5995 C CA    . LEU B 1 371 ? 23.601  -23.433 43.637 1.00 30.80 ?  371 LEU B CA    1 
ATOM   5996 C C     . LEU B 1 371 ? 24.573  -24.529 43.235 1.00 31.53 ?  371 LEU B C     1 
ATOM   5997 O O     . LEU B 1 371 ? 25.037  -25.288 44.091 1.00 40.12 ?  371 LEU B O     1 
ATOM   5998 C CB    . LEU B 1 371 ? 22.165  -23.948 43.511 1.00 23.12 ?  371 LEU B CB    1 
ATOM   5999 C CG    . LEU B 1 371 ? 21.663  -24.865 44.634 1.00 26.03 ?  371 LEU B CG    1 
ATOM   6000 C CD1   . LEU B 1 371 ? 21.250  -24.002 45.797 1.00 40.18 ?  371 LEU B CD1   1 
ATOM   6001 C CD2   . LEU B 1 371 ? 20.503  -25.741 44.219 1.00 21.36 ?  371 LEU B CD2   1 
ATOM   6002 N N     . GLU B 1 372 ? 24.922  -24.607 41.951 1.00 35.78 ?  372 GLU B N     1 
ATOM   6003 C CA    . GLU B 1 372 ? 25.830  -25.658 41.505 1.00 40.46 ?  372 GLU B CA    1 
ATOM   6004 C C     . GLU B 1 372 ? 27.225  -25.469 42.090 1.00 42.84 ?  372 GLU B C     1 
ATOM   6005 O O     . GLU B 1 372 ? 27.852  -26.431 42.545 1.00 59.19 ?  372 GLU B O     1 
ATOM   6006 C CB    . GLU B 1 372 ? 25.891  -25.671 39.976 1.00 44.01 ?  372 GLU B CB    1 
ATOM   6007 C CG    . GLU B 1 372 ? 24.596  -26.070 39.276 1.00 50.61 ?  372 GLU B CG    1 
ATOM   6008 C CD    . GLU B 1 372 ? 24.526  -25.517 37.856 1.00 62.70 ?  372 GLU B CD    1 
ATOM   6009 O OE1   . GLU B 1 372 ? 25.519  -24.898 37.412 1.00 65.35 ?  372 GLU B OE1   1 
ATOM   6010 O OE2   . GLU B 1 372 ? 23.483  -25.686 37.188 1.00 66.04 -1 372 GLU B OE2   1 
ATOM   6011 N N     . GLU B 1 373 ? 27.707  -24.230 42.134 1.00 34.90 ?  373 GLU B N     1 
ATOM   6012 C CA    . GLU B 1 373 ? 29.006  -23.960 42.739 1.00 39.44 ?  373 GLU B CA    1 
ATOM   6013 C C     . GLU B 1 373 ? 28.958  -24.133 44.247 1.00 36.52 ?  373 GLU B C     1 
ATOM   6014 O O     . GLU B 1 373 ? 29.977  -24.454 44.868 1.00 28.10 ?  373 GLU B O     1 
ATOM   6015 C CB    . GLU B 1 373 ? 29.465  -22.543 42.381 1.00 46.08 ?  373 GLU B CB    1 
ATOM   6016 C CG    . GLU B 1 373 ? 30.843  -22.172 42.888 1.00 46.43 ?  373 GLU B CG    1 
ATOM   6017 C CD    . GLU B 1 373 ? 31.969  -22.825 42.098 1.00 51.98 ?  373 GLU B CD    1 
ATOM   6018 O OE1   . GLU B 1 373 ? 31.690  -23.512 41.090 1.00 48.55 ?  373 GLU B OE1   1 
ATOM   6019 O OE2   . GLU B 1 373 ? 33.142  -22.642 42.482 1.00 50.20 -1 373 GLU B OE2   1 
ATOM   6020 N N     . ILE B 1 374 ? 27.801  -23.863 44.856 1.00 41.12 ?  374 ILE B N     1 
ATOM   6021 C CA    . ILE B 1 374 ? 27.627  -24.109 46.283 1.00 29.54 ?  374 ILE B CA    1 
ATOM   6022 C C     . ILE B 1 374 ? 27.826  -25.587 46.592 1.00 25.36 ?  374 ILE B C     1 
ATOM   6023 O O     . ILE B 1 374 ? 28.393  -25.948 47.628 1.00 28.49 ?  374 ILE B O     1 
ATOM   6024 C CB    . ILE B 1 374 ? 26.247  -23.604 46.745 1.00 26.69 ?  374 ILE B CB    1 
ATOM   6025 C CG1   . ILE B 1 374 ? 26.150  -22.078 46.569 1.00 29.00 ?  374 ILE B CG1   1 
ATOM   6026 C CG2   . ILE B 1 374 ? 25.985  -24.024 48.190 1.00 20.23 ?  374 ILE B CG2   1 
ATOM   6027 C CD1   . ILE B 1 374 ? 24.777  -21.490 46.839 1.00 20.06 ?  374 ILE B CD1   1 
ATOM   6028 N N     . LEU B 1 375 ? 27.337  -26.464 45.714 1.00 28.48 ?  375 LEU B N     1 
ATOM   6029 C CA    . LEU B 1 375 ? 27.492  -27.903 45.899 1.00 30.28 ?  375 LEU B CA    1 
ATOM   6030 C C     . LEU B 1 375 ? 28.828  -28.400 45.352 1.00 33.96 ?  375 LEU B C     1 
ATOM   6031 O O     . LEU B 1 375 ? 29.449  -29.289 45.940 1.00 31.24 ?  375 LEU B O     1 
ATOM   6032 C CB    . LEU B 1 375 ? 26.320  -28.654 45.240 1.00 27.00 ?  375 LEU B CB    1 
ATOM   6033 C CG    . LEU B 1 375 ? 24.893  -28.299 45.714 1.00 21.54 ?  375 LEU B CG    1 
ATOM   6034 C CD1   . LEU B 1 375 ? 23.852  -28.861 44.783 1.00 24.30 ?  375 LEU B CD1   1 
ATOM   6035 C CD2   . LEU B 1 375 ? 24.602  -28.738 47.138 1.00 13.35 ?  375 LEU B CD2   1 
ATOM   6036 N N     . ASN B 1 376 ? 29.292  -27.822 44.244 1.00 47.58 ?  376 ASN B N     1 
ATOM   6037 C CA    . ASN B 1 376 ? 30.597  -28.189 43.704 1.00 49.01 ?  376 ASN B CA    1 
ATOM   6038 C C     . ASN B 1 376 ? 31.697  -27.966 44.732 1.00 39.81 ?  376 ASN B C     1 
ATOM   6039 O O     . ASN B 1 376 ? 32.631  -28.768 44.838 1.00 46.04 ?  376 ASN B O     1 
ATOM   6040 C CB    . ASN B 1 376 ? 30.880  -27.399 42.428 1.00 51.92 ?  376 ASN B CB    1 
ATOM   6041 C CG    . ASN B 1 376 ? 31.856  -28.103 41.517 1.00 50.50 ?  376 ASN B CG    1 
ATOM   6042 O OD1   . ASN B 1 376 ? 33.056  -27.848 41.567 1.00 47.70 ?  376 ASN B OD1   1 
ATOM   6043 N ND2   . ASN B 1 376 ? 31.345  -28.997 40.678 1.00 51.30 ?  376 ASN B ND2   1 
ATOM   6044 N N     . ARG B 1 377 ? 31.612  -26.876 45.487 1.00 29.94 ?  377 ARG B N     1 
ATOM   6045 C CA    . ARG B 1 377 ? 32.597  -26.611 46.528 1.00 22.23 ?  377 ARG B CA    1 
ATOM   6046 C C     . ARG B 1 377 ? 32.352  -27.457 47.776 1.00 27.45 ?  377 ARG B C     1 
ATOM   6047 O O     . ARG B 1 377 ? 33.282  -27.672 48.561 1.00 46.14 ?  377 ARG B O     1 
ATOM   6048 C CB    . ARG B 1 377 ? 32.623  -25.116 46.852 1.00 18.31 ?  377 ARG B CB    1 
ATOM   6049 C CG    . ARG B 1 377 ? 33.091  -24.255 45.670 1.00 20.83 ?  377 ARG B CG    1 
ATOM   6050 C CD    . ARG B 1 377 ? 32.848  -22.763 45.889 1.00 28.16 ?  377 ARG B CD    1 
ATOM   6051 N NE    . ARG B 1 377 ? 33.365  -21.970 44.775 1.00 32.09 ?  377 ARG B NE    1 
ATOM   6052 C CZ    . ARG B 1 377 ? 34.001  -20.808 44.899 1.00 21.15 ?  377 ARG B CZ    1 
ATOM   6053 N NH1   . ARG B 1 377 ? 34.210  -20.281 46.095 1.00 21.36 1  377 ARG B NH1   1 
ATOM   6054 N NH2   . ARG B 1 377 ? 34.432  -20.173 43.822 1.00 14.16 ?  377 ARG B NH2   1 
ATOM   6055 N N     . LEU B 1 378 ? 31.113  -27.897 48.014 1.00 16.63 ?  378 LEU B N     1 
ATOM   6056 C CA    . LEU B 1 378 ? 30.862  -28.819 49.122 1.00 23.56 ?  378 LEU B CA    1 
ATOM   6057 C C     . LEU B 1 378 ? 31.499  -30.182 48.849 1.00 32.12 ?  378 LEU B C     1 
ATOM   6058 O O     . LEU B 1 378 ? 32.079  -30.809 49.746 1.00 30.26 ?  378 LEU B O     1 
ATOM   6059 C CB    . LEU B 1 378 ? 29.354  -28.991 49.330 1.00 22.24 ?  378 LEU B CB    1 
ATOM   6060 C CG    . LEU B 1 378 ? 28.560  -28.046 50.235 1.00 30.86 ?  378 LEU B CG    1 
ATOM   6061 C CD1   . LEU B 1 378 ? 27.081  -28.394 50.150 1.00 33.89 ?  378 LEU B CD1   1 
ATOM   6062 C CD2   . LEU B 1 378 ? 29.045  -28.097 51.693 1.00 28.92 ?  378 LEU B CD2   1 
ATOM   6063 N N     . ARG B 1 379 ? 31.405  -30.648 47.604 1.00 26.61 ?  379 ARG B N     1 
ATOM   6064 C CA    . ARG B 1 379 ? 32.043  -31.893 47.204 1.00 29.05 ?  379 ARG B CA    1 
ATOM   6065 C C     . ARG B 1 379 ? 33.559  -31.785 47.323 1.00 34.47 ?  379 ARG B C     1 
ATOM   6066 O O     . ARG B 1 379 ? 34.211  -32.615 47.969 1.00 39.27 ?  379 ARG B O     1 
ATOM   6067 C CB    . ARG B 1 379 ? 31.614  -32.228 45.771 1.00 25.13 ?  379 ARG B CB    1 
ATOM   6068 C CG    . ARG B 1 379 ? 31.791  -33.661 45.362 1.00 16.99 ?  379 ARG B CG    1 
ATOM   6069 C CD    . ARG B 1 379 ? 31.307  -33.871 43.955 1.00 25.75 ?  379 ARG B CD    1 
ATOM   6070 N NE    . ARG B 1 379 ? 32.022  -33.054 42.982 1.00 39.55 ?  379 ARG B NE    1 
ATOM   6071 C CZ    . ARG B 1 379 ? 31.915  -33.213 41.664 1.00 40.95 ?  379 ARG B CZ    1 
ATOM   6072 N NH1   . ARG B 1 379 ? 31.127  -34.165 41.171 1.00 35.16 1  379 ARG B NH1   1 
ATOM   6073 N NH2   . ARG B 1 379 ? 32.596  -32.428 40.837 1.00 34.44 ?  379 ARG B NH2   1 
ATOM   6074 N N     . HIS B 1 380 ? 34.140  -30.773 46.683 1.00 26.97 ?  380 HIS B N     1 
ATOM   6075 C CA    . HIS B 1 380 ? 35.576  -30.556 46.790 1.00 33.01 ?  380 HIS B CA    1 
ATOM   6076 C C     . HIS B 1 380 ? 36.031  -30.537 48.246 1.00 43.83 ?  380 HIS B C     1 
ATOM   6077 O O     . HIS B 1 380 ? 37.040  -31.159 48.595 1.00 53.40 ?  380 HIS B O     1 
ATOM   6078 C CB    . HIS B 1 380 ? 35.947  -29.251 46.079 1.00 44.79 ?  380 HIS B CB    1 
ATOM   6079 C CG    . HIS B 1 380 ? 37.412  -28.941 46.090 1.00 46.97 ?  380 HIS B CG    1 
ATOM   6080 N ND1   . HIS B 1 380 ? 38.335  -29.665 45.365 1.00 49.22 ?  380 HIS B ND1   1 
ATOM   6081 C CD2   . HIS B 1 380 ? 38.113  -27.978 46.734 1.00 47.77 ?  380 HIS B CD2   1 
ATOM   6082 C CE1   . HIS B 1 380 ? 39.540  -29.162 45.563 1.00 49.94 ?  380 HIS B CE1   1 
ATOM   6083 N NE2   . HIS B 1 380 ? 39.434  -28.139 46.392 1.00 48.92 ?  380 HIS B NE2   1 
ATOM   6084 N N     . THR B 1 381 ? 35.284  -29.848 49.117 1.00 50.31 ?  381 THR B N     1 
ATOM   6085 C CA    . THR B 1 381 ? 35.677  -29.729 50.524 1.00 39.90 ?  381 THR B CA    1 
ATOM   6086 C C     . THR B 1 381 ? 35.807  -31.096 51.181 1.00 29.88 ?  381 THR B C     1 
ATOM   6087 O O     . THR B 1 381 ? 36.765  -31.350 51.918 1.00 31.00 ?  381 THR B O     1 
ATOM   6088 C CB    . THR B 1 381 ? 34.677  -28.846 51.283 1.00 30.06 ?  381 THR B CB    1 
ATOM   6089 O OG1   . THR B 1 381 ? 34.497  -27.611 50.579 1.00 22.89 ?  381 THR B OG1   1 
ATOM   6090 C CG2   . THR B 1 381 ? 35.158  -28.545 52.698 1.00 26.48 ?  381 THR B CG2   1 
ATOM   6091 N N     . PHE B 1 382 ? 34.860  -31.995 50.919 1.00 34.64 ?  382 PHE B N     1 
ATOM   6092 C CA    . PHE B 1 382 ? 34.778  -33.276 51.613 1.00 38.35 ?  382 PHE B CA    1 
ATOM   6093 C C     . PHE B 1 382 ? 35.193  -34.459 50.750 1.00 40.99 ?  382 PHE B C     1 
ATOM   6094 O O     . PHE B 1 382 ? 34.962  -35.604 51.151 1.00 52.15 ?  382 PHE B O     1 
ATOM   6095 C CB    . PHE B 1 382 ? 33.365  -33.509 52.138 1.00 50.95 ?  382 PHE B CB    1 
ATOM   6096 C CG    . PHE B 1 382 ? 32.835  -32.382 52.963 1.00 41.65 ?  382 PHE B CG    1 
ATOM   6097 C CD1   . PHE B 1 382 ? 33.590  -31.849 53.993 1.00 40.53 ?  382 PHE B CD1   1 
ATOM   6098 C CD2   . PHE B 1 382 ? 31.585  -31.856 52.706 1.00 23.09 ?  382 PHE B CD2   1 
ATOM   6099 C CE1   . PHE B 1 382 ? 33.100  -30.815 54.751 1.00 38.16 ?  382 PHE B CE1   1 
ATOM   6100 C CE2   . PHE B 1 382 ? 31.100  -30.827 53.461 1.00 27.32 ?  382 PHE B CE2   1 
ATOM   6101 C CZ    . PHE B 1 382 ? 31.855  -30.307 54.486 1.00 31.00 ?  382 PHE B CZ    1 
ATOM   6102 N N     . SER B 1 383 ? 35.767  -34.222 49.572 1.00 40.04 ?  383 SER B N     1 
ATOM   6103 C CA    . SER B 1 383 ? 36.184  -35.319 48.700 1.00 44.90 ?  383 SER B CA    1 
ATOM   6104 C C     . SER B 1 383 ? 37.541  -35.896 49.119 1.00 51.00 ?  383 SER B C     1 
ATOM   6105 O O     . SER B 1 383 ? 38.419  -35.192 49.617 1.00 56.48 ?  383 SER B O     1 
ATOM   6106 C CB    . SER B 1 383 ? 36.248  -34.851 47.241 1.00 46.22 ?  383 SER B CB    1 
ATOM   6107 O OG    . SER B 1 383 ? 34.961  -34.555 46.718 1.00 44.04 ?  383 SER B OG    1 
ATOM   6108 O OXT   . SER B 1 383 ? 37.812  -37.089 48.956 1.00 50.50 -1 383 SER B OXT   1 
HETATM 6109 N N     . OO0 C 2 .   ? 9.102   15.355  67.353 1.00 46.11 ?  401 OO0 A N     1 
HETATM 6110 C CA    . OO0 C 2 .   ? 7.890   16.159  67.277 1.00 41.62 ?  401 OO0 A CA    1 
HETATM 6111 C CB    . OO0 C 2 .   ? 6.686   15.369  67.820 1.00 35.95 ?  401 OO0 A CB    1 
HETATM 6112 S SG    . OO0 C 2 .   ? 5.496   16.555  68.530 1.00 48.62 ?  401 OO0 A SG    1 
HETATM 6113 O O1    . OO0 C 2 .   ? 5.069   17.697  67.395 1.00 55.33 ?  401 OO0 A O1    1 
HETATM 6114 C C3    . OO0 C 2 .   ? 3.981   15.738  69.116 1.00 20.98 ?  401 OO0 A C3    1 
HETATM 6115 C C4    . OO0 C 2 .   ? 2.927   16.132  68.088 1.00 22.48 ?  401 OO0 A C4    1 
HETATM 6116 C C5    . OO0 C 2 .   ? 1.840   16.788  68.434 1.00 26.53 ?  401 OO0 A C5    1 
HETATM 6117 C C     . OO0 C 2 .   ? 8.071   17.502  68.007 1.00 31.86 ?  401 OO0 A C     1 
HETATM 6118 O OXT   . OO0 C 2 .   ? 7.145   18.341  67.977 1.00 40.13 ?  401 OO0 A OXT   1 
HETATM 6119 O O     . OO0 C 2 .   ? 9.127   17.810  68.613 1.00 30.68 -1 401 OO0 A O     1 
HETATM 6120 O O     . HOH D 3 .   ? 25.784  24.270  56.300 1.00 20.56 ?  501 HOH A O     1 
HETATM 6121 O O     . HOH D 3 .   ? 5.960   4.806   86.444 1.00 16.47 ?  502 HOH A O     1 
HETATM 6122 O O     . HOH D 3 .   ? 21.271  17.185  61.971 1.00 19.54 ?  503 HOH A O     1 
HETATM 6123 O O     . HOH D 3 .   ? 13.657  33.054  81.715 1.00 25.61 ?  504 HOH A O     1 
HETATM 6124 O O     . HOH D 3 .   ? 30.706  1.504   59.583 1.00 1.91  ?  505 HOH A O     1 
HETATM 6125 O O     . HOH D 3 .   ? 17.316  -0.698  84.520 1.00 18.55 ?  506 HOH A O     1 
HETATM 6126 O O     . HOH D 3 .   ? 13.297  -2.067  81.399 1.00 13.14 ?  507 HOH A O     1 
HETATM 6127 O O     . HOH D 3 .   ? 33.777  15.597  74.042 1.00 23.14 ?  508 HOH A O     1 
HETATM 6128 O O     . HOH D 3 .   ? 22.272  24.391  73.397 1.00 1.91  ?  509 HOH A O     1 
HETATM 6129 O O     . HOH D 3 .   ? 12.666  39.959  57.753 1.00 17.14 ?  510 HOH A O     1 
HETATM 6130 O O     . HOH D 3 .   ? 24.850  24.363  73.289 1.00 18.69 ?  511 HOH A O     1 
HETATM 6131 O O     . HOH D 3 .   ? 19.395  31.314  61.089 1.00 14.82 ?  512 HOH A O     1 
HETATM 6132 O O     . HOH D 3 .   ? 18.679  16.556  63.508 1.00 32.35 ?  513 HOH A O     1 
HETATM 6133 O O     . HOH D 3 .   ? 12.479  22.468  66.417 1.00 30.55 ?  514 HOH A O     1 
HETATM 6134 O O     . HOH D 3 .   ? 28.359  21.385  91.857 1.00 11.17 ?  515 HOH A O     1 
HETATM 6135 O O     . HOH D 3 .   ? 27.612  16.660  95.635 1.00 18.96 ?  516 HOH A O     1 
HETATM 6136 O O     . HOH D 3 .   ? 7.275   39.979  69.377 1.00 4.16  ?  517 HOH A O     1 
HETATM 6137 O O     . HOH D 3 .   ? 35.081  20.352  71.365 1.00 13.14 ?  518 HOH A O     1 
HETATM 6138 O O     . HOH D 3 .   ? -11.042 35.136  63.156 1.00 16.47 ?  519 HOH A O     1 
HETATM 6139 O O     . HOH D 3 .   ? -4.780  33.086  82.521 1.00 31.67 ?  520 HOH A O     1 
HETATM 6140 O O     . HOH D 3 .   ? -10.446 40.263  70.106 1.00 23.92 ?  521 HOH A O     1 
HETATM 6141 O O     . HOH D 3 .   ? 12.695  26.927  67.874 1.00 12.69 ?  522 HOH A O     1 
HETATM 6142 O O     . HOH D 3 .   ? 10.873  17.109  91.866 1.00 12.24 ?  523 HOH A O     1 
HETATM 6143 O O     . HOH D 3 .   ? -12.430 21.707  54.258 1.00 20.82 ?  524 HOH A O     1 
HETATM 6144 O O     . HOH D 3 .   ? 15.661  24.136  85.814 1.00 13.07 ?  525 HOH A O     1 
HETATM 6145 O O     . HOH D 3 .   ? 33.907  3.187   81.568 1.00 21.51 ?  526 HOH A O     1 
HETATM 6146 O O     . HOH D 3 .   ? 30.252  8.324   77.579 1.00 1.91  ?  527 HOH A O     1 
HETATM 6147 O O     . HOH D 3 .   ? 22.693  16.303  64.470 1.00 7.13  ?  528 HOH A O     1 
HETATM 6148 O O     . HOH D 3 .   ? 27.770  24.015  63.057 1.00 13.77 ?  529 HOH A O     1 
HETATM 6149 O O     . HOH D 3 .   ? 15.360  1.785   54.768 1.00 13.14 ?  530 HOH A O     1 
HETATM 6150 O O     . HOH D 3 .   ? 1.780   26.502  87.256 1.00 10.26 ?  531 HOH A O     1 
HETATM 6151 O O     . HOH D 3 .   ? 27.604  32.777  66.705 1.00 14.60 ?  532 HOH A O     1 
HETATM 6152 O O     . HOH D 3 .   ? 27.156  28.850  58.495 1.00 22.54 ?  533 HOH A O     1 
HETATM 6153 O O     . HOH D 3 .   ? 36.214  8.308   76.475 1.00 14.81 ?  534 HOH A O     1 
HETATM 6154 O O     . HOH D 3 .   ? -5.752  21.297  72.795 1.00 9.15  ?  535 HOH A O     1 
HETATM 6155 O O     . HOH D 3 .   ? 15.766  19.462  43.160 1.00 16.36 ?  536 HOH A O     1 
HETATM 6156 O O     . HOH D 3 .   ? -5.062  32.462  77.872 1.00 20.53 ?  537 HOH A O     1 
HETATM 6157 O O     . HOH D 3 .   ? 18.903  20.019  83.148 1.00 10.77 ?  538 HOH A O     1 
HETATM 6158 O O     . HOH D 3 .   ? -2.573  20.110  76.406 1.00 4.14  ?  539 HOH A O     1 
HETATM 6159 O O     . HOH D 3 .   ? 9.111   -0.339  93.605 1.00 6.13  ?  540 HOH A O     1 
HETATM 6160 O O     . HOH D 3 .   ? 14.583  43.238  64.045 1.00 14.18 ?  541 HOH A O     1 
HETATM 6161 O O     . HOH D 3 .   ? 8.572   7.231   93.311 1.00 12.78 ?  542 HOH A O     1 
HETATM 6162 O O     . HOH D 3 .   ? 17.506  -2.462  82.983 1.00 1.91  ?  543 HOH A O     1 
HETATM 6163 O O     . HOH D 3 .   ? 6.914   29.521  81.790 1.00 6.93  ?  544 HOH A O     1 
HETATM 6164 O O     . HOH D 3 .   ? 20.487  12.208  99.518 1.00 11.39 ?  545 HOH A O     1 
HETATM 6165 O O     . HOH D 3 .   ? -12.197 19.632  72.240 1.00 16.73 ?  546 HOH A O     1 
HETATM 6166 O O     . HOH D 3 .   ? -3.214  9.998   48.328 1.00 14.61 ?  547 HOH A O     1 
HETATM 6167 O O     . HOH D 3 .   ? -4.648  24.983  71.376 1.00 14.75 ?  548 HOH A O     1 
HETATM 6168 O O     . HOH D 3 .   ? 12.953  21.900  42.383 1.00 30.11 ?  549 HOH A O     1 
HETATM 6169 O O     . HOH D 3 .   ? 34.112  -1.619  80.781 1.00 14.80 ?  550 HOH A O     1 
HETATM 6170 O O     . HOH D 3 .   ? 31.614  -0.669  70.772 1.00 11.55 ?  551 HOH A O     1 
HETATM 6171 O O     . HOH D 3 .   ? 29.799  33.542  65.230 1.00 15.84 ?  552 HOH A O     1 
HETATM 6172 O O     . HOH D 3 .   ? 12.022  -0.478  94.449 1.00 1.91  ?  553 HOH A O     1 
HETATM 6173 O O     . HOH D 3 .   ? 29.213  -1.328  71.019 1.00 15.90 ?  554 HOH A O     1 
HETATM 6174 O O     . HOH E 3 .   ? 8.203   -11.424 80.240 1.00 20.99 ?  401 HOH B O     1 
HETATM 6175 O O     . HOH E 3 .   ? 7.387   -20.371 79.481 1.00 22.64 ?  402 HOH B O     1 
HETATM 6176 O O     . HOH E 3 .   ? 27.230  -37.031 58.458 1.00 6.07  ?  403 HOH B O     1 
HETATM 6177 O O     . HOH E 3 .   ? 8.009   -32.318 83.880 1.00 15.29 ?  404 HOH B O     1 
HETATM 6178 O O     . HOH E 3 .   ? 9.052   -23.802 69.223 1.00 18.21 ?  405 HOH B O     1 
HETATM 6179 O O     . HOH E 3 .   ? 30.383  -34.383 61.730 1.00 25.20 ?  406 HOH B O     1 
HETATM 6180 O O     . HOH E 3 .   ? 8.084   0.200   74.895 1.00 29.41 ?  407 HOH B O     1 
HETATM 6181 O O     . HOH E 3 .   ? 5.106   -21.514 85.520 1.00 13.14 ?  408 HOH B O     1 
HETATM 6182 O O     . HOH E 3 .   ? 3.924   -1.846  42.428 1.00 34.08 ?  409 HOH B O     1 
HETATM 6183 O O     . HOH E 3 .   ? 14.901  -13.191 85.103 1.00 26.63 ?  410 HOH B O     1 
HETATM 6184 O O     . HOH E 3 .   ? 1.170   -20.584 51.407 1.00 37.22 ?  411 HOH B O     1 
HETATM 6185 O O     . HOH E 3 .   ? 17.245  -36.076 55.426 1.00 36.34 ?  412 HOH B O     1 
HETATM 6186 O O     . HOH E 3 .   ? -6.145  -23.813 80.112 1.00 17.80 ?  413 HOH B O     1 
HETATM 6187 O O     . HOH E 3 .   ? -6.238  -13.729 58.331 1.00 38.05 ?  414 HOH B O     1 
HETATM 6188 O O     . HOH E 3 .   ? 13.859  -11.834 89.474 1.00 12.62 ?  415 HOH B O     1 
HETATM 6189 O O     . HOH E 3 .   ? 1.211   -10.645 61.516 1.00 39.79 ?  416 HOH B O     1 
HETATM 6190 O O     . HOH E 3 .   ? 19.389  -13.118 40.928 1.00 14.08 ?  417 HOH B O     1 
HETATM 6191 O O     . HOH E 3 .   ? 8.562   -4.315  70.608 1.00 14.71 ?  418 HOH B O     1 
HETATM 6192 O O     . HOH E 3 .   ? 4.853   -28.751 49.881 1.00 27.44 ?  419 HOH B O     1 
HETATM 6193 O O     . HOH E 3 .   ? 3.514   -26.747 85.200 1.00 9.49  ?  420 HOH B O     1 
HETATM 6194 O O     . HOH E 3 .   ? 5.257   -9.720  82.534 1.00 13.14 ?  421 HOH B O     1 
HETATM 6195 O O     . HOH E 3 .   ? 32.612  -21.595 55.691 1.00 13.76 ?  422 HOH B O     1 
HETATM 6196 O O     . HOH E 3 .   ? 30.568  -36.877 66.470 1.00 19.85 ?  423 HOH B O     1 
HETATM 6197 O O     . HOH E 3 .   ? 9.300   -25.905 66.399 1.00 21.65 ?  424 HOH B O     1 
HETATM 6198 O O     . HOH E 3 .   ? 35.464  -36.039 65.062 1.00 20.68 ?  425 HOH B O     1 
HETATM 6199 O O     . HOH E 3 .   ? 15.860  -8.088  82.414 1.00 13.14 ?  426 HOH B O     1 
HETATM 6200 O O     . HOH E 3 .   ? 28.687  -22.654 66.422 1.00 23.89 ?  427 HOH B O     1 
HETATM 6201 O O     . HOH E 3 .   ? 3.664   -14.818 83.991 1.00 12.40 ?  428 HOH B O     1 
HETATM 6202 O O     . HOH E 3 .   ? 5.643   -38.069 71.838 1.00 1.91  ?  429 HOH B O     1 
HETATM 6203 O O     . HOH E 3 .   ? -15.498 -10.814 60.893 1.00 13.46 ?  430 HOH B O     1 
HETATM 6204 O O     . HOH E 3 .   ? 11.003  -2.327  70.667 1.00 5.31  ?  431 HOH B O     1 
HETATM 6205 O O     . HOH E 3 .   ? 1.514   -22.782 62.725 1.00 5.44  ?  432 HOH B O     1 
HETATM 6206 O O     . HOH E 3 .   ? -13.137 -18.449 59.027 1.00 26.04 ?  433 HOH B O     1 
HETATM 6207 O O     . HOH E 3 .   ? 15.404  -33.482 77.202 1.00 13.90 ?  434 HOH B O     1 
HETATM 6208 O O     . HOH E 3 .   ? 31.744  -21.258 62.023 1.00 13.14 ?  435 HOH B O     1 
HETATM 6209 O O     . HOH E 3 .   ? 20.022  -40.741 42.207 1.00 21.23 ?  436 HOH B O     1 
HETATM 6210 O O     . HOH E 3 .   ? 37.603  -16.791 59.362 1.00 21.84 ?  437 HOH B O     1 
HETATM 6211 O O     . HOH E 3 .   ? 44.735  -26.969 57.490 1.00 6.48  ?  438 HOH B O     1 
HETATM 6212 O O     . HOH E 3 .   ? 46.740  -26.202 58.469 1.00 24.11 ?  439 HOH B O     1 
HETATM 6213 O O     . HOH E 3 .   ? 3.621   11.575  73.374 1.00 6.27  ?  440 HOH B O     1 
HETATM 6214 O O     . HOH E 3 .   ? 2.520   10.454  71.744 1.00 6.90  ?  441 HOH B O     1 
HETATM 6215 O O     . HOH E 3 .   ? 21.736  -11.924 81.953 1.00 13.31 ?  442 HOH B O     1 
HETATM 6216 O O     . HOH E 3 .   ? 34.705  -38.609 66.655 1.00 13.14 ?  443 HOH B O     1 
HETATM 6217 O O     . HOH E 3 .   ? 36.592  -15.499 60.902 1.00 17.07 ?  444 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 6   ? 0.7986 0.6627 0.5821 0.0213  0.0145  0.0125  6   LYS A N     
2    C CA    . LYS A 6   ? 0.7536 0.6143 0.5310 0.0236  0.0078  0.0114  6   LYS A CA    
3    C C     . LYS A 6   ? 0.6848 0.5571 0.4742 0.0211  0.0040  0.0107  6   LYS A C     
4    O O     . LYS A 6   ? 0.6830 0.5601 0.4775 0.0193  0.0056  0.0100  6   LYS A O     
5    C CB    . LYS A 6   ? 0.8396 0.6888 0.6034 0.0269  0.0075  0.0103  6   LYS A CB    
6    C CG    . LYS A 6   ? 0.7474 0.5924 0.5046 0.0297  0.0002  0.0088  6   LYS A CG    
7    C CD    . LYS A 6   ? 0.7012 0.5494 0.4610 0.0290  -0.0019 0.0072  6   LYS A CD    
8    C CE    . LYS A 6   ? 0.6373 0.4769 0.3875 0.0307  0.0020  0.0068  6   LYS A CE    
9    N NZ    . LYS A 6   ? 0.6172 0.4611 0.3713 0.0295  0.0010  0.0054  6   LYS A NZ    
10   N N     . ALA A 7   ? 0.6427 0.5195 0.4366 0.0209  -0.0011 0.0107  7   ALA A N     
11   C CA    . ALA A 7   ? 0.5299 0.4162 0.3338 0.0191  -0.0054 0.0100  7   ALA A CA    
12   C C     . ALA A 7   ? 0.6231 0.5041 0.4201 0.0212  -0.0094 0.0080  7   ALA A C     
13   O O     . ALA A 7   ? 0.7908 0.6611 0.5755 0.0248  -0.0124 0.0072  7   ALA A O     
14   C CB    . ALA A 7   ? 0.5291 0.4196 0.3381 0.0190  -0.0101 0.0105  7   ALA A CB    
15   N N     . ILE A 8   ? 0.4802 0.3687 0.2851 0.0192  -0.0095 0.0073  8   ILE A N     
16   C CA    . ILE A 8   ? 0.4260 0.3109 0.2261 0.0208  -0.0130 0.0053  8   ILE A CA    
17   C C     . ILE A 8   ? 0.4121 0.3047 0.2213 0.0199  -0.0193 0.0044  8   ILE A C     
18   O O     . ILE A 8   ? 0.4148 0.3187 0.2370 0.0169  -0.0184 0.0052  8   ILE A O     
19   C CB    . ILE A 8   ? 0.5837 0.4706 0.3853 0.0192  -0.0080 0.0050  8   ILE A CB    
20   C CG1   . ILE A 8   ? 0.5438 0.4305 0.3443 0.0200  -0.0119 0.0029  8   ILE A CG1   
21   C CG2   . ILE A 8   ? 0.6022 0.5012 0.4178 0.0152  -0.0035 0.0063  8   ILE A CG2   
22   C CD1   . ILE A 8   ? 0.4414 0.3267 0.2398 0.0193  -0.0071 0.0025  8   ILE A CD1   
23   N N     . ASN A 9   ? 0.6154 0.5015 0.4178 0.0228  -0.0256 0.0026  9   ASN A N     
24   C CA    . ASN A 9   ? 0.5374 0.4291 0.3480 0.0225  -0.0322 0.0014  9   ASN A CA    
25   C C     . ASN A 9   ? 0.5531 0.4544 0.3741 0.0198  -0.0314 0.0008  9   ASN A C     
26   O O     . ASN A 9   ? 0.7202 0.6186 0.5367 0.0202  -0.0301 -0.0004 9   ASN A O     
27   C CB    . ASN A 9   ? 0.6174 0.4990 0.4179 0.0264  -0.0390 -0.0008 9   ASN A CB    
28   C CG    . ASN A 9   ? 0.7860 0.6725 0.5955 0.0264  -0.0463 -0.0022 9   ASN A CG    
29   O OD1   . ASN A 9   ? 0.7644 0.6611 0.5868 0.0236  -0.0465 -0.0012 9   ASN A OD1   
30   N ND2   . ASN A 9   ? 0.7847 0.6635 0.5872 0.0295  -0.0524 -0.0046 9   ASN A ND2   
31   N N     . ARG A 10  ? 0.4665 0.3790 0.3012 0.0171  -0.0320 0.0017  10  ARG A N     
32   C CA    . ARG A 10  ? 0.4609 0.3832 0.3065 0.0147  -0.0317 0.0011  10  ARG A CA    
33   C C     . ARG A 10  ? 0.5833 0.5097 0.4371 0.0149  -0.0387 -0.0001 10  ARG A C     
34   O O     . ARG A 10  ? 0.7258 0.6605 0.5894 0.0130  -0.0389 -0.0006 10  ARG A O     
35   C CB    . ARG A 10  ? 0.3595 0.2925 0.2157 0.0112  -0.0257 0.0033  10  ARG A CB    
36   C CG    . ARG A 10  ? 0.3994 0.3303 0.2510 0.0104  -0.0185 0.0039  10  ARG A CG    
37   C CD    . ARG A 10  ? 0.2752 0.2171 0.1386 0.0072  -0.0132 0.0057  10  ARG A CD    
38   N NE    . ARG A 10  ? 0.2180 0.1705 0.0929 0.0053  -0.0138 0.0053  10  ARG A NE    
39   C CZ    . ARG A 10  ? 0.1893 0.1523 0.0755 0.0028  -0.0099 0.0066  10  ARG A CZ    
40   N NH1   . ARG A 10  ? 0.1875 0.1520 0.0758 0.0019  -0.0054 0.0082  10  ARG A NH1   
41   N NH2   . ARG A 10  ? 0.1766 0.1485 0.0725 0.0016  -0.0106 0.0061  10  ARG A NH2   
42   N N     . ARG A 11  ? 0.4417 0.3625 0.2922 0.0172  -0.0443 -0.0007 11  ARG A N     
43   C CA    . ARG A 11  ? 0.5558 0.4791 0.4141 0.0177  -0.0512 -0.0022 11  ARG A CA    
44   C C     . ARG A 11  ? 0.5688 0.4874 0.4229 0.0194  -0.0549 -0.0050 11  ARG A C     
45   O O     . ARG A 11  ? 0.4454 0.3544 0.2864 0.0218  -0.0547 -0.0061 11  ARG A O     
46   C CB    . ARG A 11  ? 0.6119 0.5299 0.4677 0.0198  -0.0561 -0.0022 11  ARG A CB    
47   C CG    . ARG A 11  ? 0.4723 0.3966 0.3354 0.0179  -0.0537 0.0004  11  ARG A CG    
48   C CD    . ARG A 11  ? 0.4409 0.3656 0.3103 0.0188  -0.0600 -0.0001 11  ARG A CD    
49   N NE    . ARG A 11  ? 0.5445 0.4740 0.4195 0.0173  -0.0578 0.0024  11  ARG A NE    
50   C CZ    . ARG A 11  ? 0.4447 0.3848 0.3336 0.0147  -0.0564 0.0038  11  ARG A CZ    
51   N NH1   . ARG A 11  ? 0.3838 0.3310 0.2830 0.0132  -0.0570 0.0032  11  ARG A NH1   
52   N NH2   . ARG A 11  ? 0.4782 0.4217 0.3708 0.0136  -0.0545 0.0059  11  ARG A NH2   
53   N N     . GLY A 12  ? 0.6906 0.6158 0.5558 0.0183  -0.0582 -0.0062 12  GLY A N     
54   C CA    . GLY A 12  ? 0.6584 0.5801 0.5214 0.0198  -0.0618 -0.0090 12  GLY A CA    
55   C C     . GLY A 12  ? 0.6348 0.5586 0.4953 0.0184  -0.0567 -0.0093 12  GLY A C     
56   O O     . GLY A 12  ? 0.6496 0.5675 0.5034 0.0201  -0.0588 -0.0116 12  GLY A O     
57   N N     . THR A 13  ? 0.4189 0.3508 0.2849 0.0153  -0.0501 -0.0071 13  THR A N     
58   C CA    . THR A 13  ? 0.4209 0.3551 0.2851 0.0138  -0.0446 -0.0073 13  THR A CA    
59   C C     . THR A 13  ? 0.3470 0.2936 0.2255 0.0107  -0.0429 -0.0070 13  THR A C     
60   O O     . THR A 13  ? 0.4074 0.3578 0.2865 0.0090  -0.0378 -0.0069 13  THR A O     
61   C CB    . THR A 13  ? 0.4600 0.3920 0.3172 0.0132  -0.0374 -0.0052 13  THR A CB    
62   O OG1   . THR A 13  ? 0.3892 0.3288 0.2549 0.0111  -0.0348 -0.0027 13  THR A OG1   
63   C CG2   . THR A 13  ? 0.4907 0.4096 0.3328 0.0165  -0.0386 -0.0055 13  THR A CG2   
64   N N     . HIS A 14  ? 0.4180 0.3707 0.3083 0.0101  -0.0471 -0.0069 14  HIS A N     
65   C CA    . HIS A 14  ? 0.3996 0.3644 0.3045 0.0074  -0.0454 -0.0061 14  HIS A CA    
66   C C     . HIS A 14  ? 0.4443 0.4169 0.3533 0.0050  -0.0385 -0.0033 14  HIS A C     
67   O O     . HIS A 14  ? 0.6491 0.6312 0.5673 0.0029  -0.0352 -0.0028 14  HIS A O     
68   C CB    . HIS A 14  ? 0.3920 0.3587 0.2987 0.0068  -0.0454 -0.0083 14  HIS A CB    
69   C CG    . HIS A 14  ? 0.4884 0.4484 0.3931 0.0091  -0.0524 -0.0112 14  HIS A CG    
70   N ND1   . HIS A 14  ? 0.4264 0.3872 0.3400 0.0101  -0.0584 -0.0117 14  HIS A ND1   
71   C CD2   . HIS A 14  ? 0.5063 0.4585 0.4015 0.0110  -0.0544 -0.0138 14  HIS A CD2   
72   C CE1   . HIS A 14  ? 0.4715 0.4254 0.3815 0.0124  -0.0639 -0.0146 14  HIS A CE1   
73   N NE2   . HIS A 14  ? 0.5574 0.5060 0.4559 0.0131  -0.0618 -0.0159 14  HIS A NE2   
74   N N     . SER A 15  ? 0.3886 0.3570 0.2911 0.0056  -0.0363 -0.0017 15  SER A N     
75   C CA    . SER A 15  ? 0.3030 0.2788 0.2110 0.0037  -0.0308 0.0009  15  SER A CA    
76   C C     . SER A 15  ? 0.2998 0.2845 0.2216 0.0028  -0.0328 0.0022  15  SER A C     
77   O O     . SER A 15  ? 0.3915 0.3733 0.3149 0.0040  -0.0380 0.0019  15  SER A O     
78   C CB    . SER A 15  ? 0.3299 0.2982 0.2280 0.0047  -0.0287 0.0022  15  SER A CB    
79   O OG    . SER A 15  ? 0.4105 0.3858 0.3149 0.0031  -0.0239 0.0046  15  SER A OG    
80   N N     . ILE A 16  ? 0.3347 0.3299 0.2665 0.0012  -0.0285 0.0034  16  ILE A N     
81   C CA    . ILE A 16  ? 0.3297 0.3327 0.2741 0.0012  -0.0291 0.0047  16  ILE A CA    
82   C C     . ILE A 16  ? 0.4155 0.4160 0.3574 0.0016  -0.0287 0.0065  16  ILE A C     
83   O O     . ILE A 16  ? 0.2351 0.2375 0.1842 0.0018  -0.0314 0.0070  16  ILE A O     
84   C CB    . ILE A 16  ? 0.2282 0.2382 0.1811 0.0019  -0.0243 0.0045  16  ILE A CB    
85   C CG1   . ILE A 16  ? 0.2449 0.2569 0.2006 0.0016  -0.0246 0.0025  16  ILE A CG1   
86   C CG2   . ILE A 16  ? 0.1944 0.2063 0.1591 0.0016  -0.0253 0.0050  16  ILE A CG2   
87   C CD1   . ILE A 16  ? 0.3309 0.3430 0.2973 0.0008  -0.0238 0.0024  16  ILE A CD1   
88   N N     . LYS A 17  ? 0.5486 0.5447 0.4812 0.0016  -0.0250 0.0073  17  LYS A N     
89   C CA    . LYS A 17  ? 0.4521 0.4459 0.3824 0.0018  -0.0241 0.0090  17  LYS A CA    
90   C C     . LYS A 17  ? 0.3907 0.3769 0.3160 0.0030  -0.0303 0.0084  17  LYS A C     
91   O O     . LYS A 17  ? 0.4885 0.4762 0.4185 0.0032  -0.0320 0.0094  17  LYS A O     
92   C CB    . LYS A 17  ? 0.2977 0.2871 0.2191 0.0014  -0.0189 0.0097  17  LYS A CB    
93   C CG    . LYS A 17  ? 0.3562 0.3453 0.2774 0.0014  -0.0165 0.0116  17  LYS A CG    
94   C CD    . LYS A 17  ? 0.3462 0.3311 0.2604 0.0008  -0.0111 0.0119  17  LYS A CD    
95   C CE    . LYS A 17  ? 0.3266 0.3127 0.2426 0.0003  -0.0080 0.0136  17  LYS A CE    
96   N NZ    . LYS A 17  ? 0.1909 0.1747 0.1039 -0.0006 -0.0023 0.0136  17  LYS A NZ    
97   N N     . TRP A 18  ? 0.3551 0.3322 0.2705 0.0044  -0.0336 0.0064  18  TRP A N     
98   C CA    . TRP A 18  ? 0.3636 0.3309 0.2710 0.0067  -0.0389 0.0055  18  TRP A CA    
99   C C     . TRP A 18  ? 0.4133 0.3789 0.3249 0.0080  -0.0459 0.0035  18  TRP A C     
100  O O     . TRP A 18  ? 0.5350 0.4943 0.4434 0.0098  -0.0507 0.0028  18  TRP A O     
101  C CB    . TRP A 18  ? 0.4778 0.4343 0.3698 0.0084  -0.0378 0.0044  18  TRP A CB    
102  C CG    . TRP A 18  ? 0.5304 0.4853 0.4172 0.0079  -0.0321 0.0063  18  TRP A CG    
103  C CD1   . TRP A 18  ? 0.5766 0.5328 0.4614 0.0066  -0.0257 0.0069  18  TRP A CD1   
104  C CD2   . TRP A 18  ? 0.5540 0.5058 0.4381 0.0086  -0.0324 0.0076  18  TRP A CD2   
105  N NE1   . TRP A 18  ? 0.4124 0.3663 0.2937 0.0065  -0.0221 0.0085  18  TRP A NE1   
106  C CE2   . TRP A 18  ? 0.6651 0.6164 0.5455 0.0077  -0.0261 0.0090  18  TRP A CE2   
107  C CE3   . TRP A 18  ? 0.4856 0.4348 0.3703 0.0100  -0.0375 0.0076  18  TRP A CE3   
108  C CZ2   . TRP A 18  ? 0.7312 0.6795 0.6084 0.0081  -0.0246 0.0104  18  TRP A CZ2   
109  C CZ3   . TRP A 18  ? 0.4371 0.3836 0.3182 0.0103  -0.0360 0.0091  18  TRP A CZ3   
110  C CH2   . TRP A 18  ? 0.6204 0.5665 0.4977 0.0094  -0.0296 0.0105  18  TRP A CH2   
111  N N     . ASP A 19  ? 0.3264 0.2974 0.2458 0.0070  -0.0465 0.0024  19  ASP A N     
112  C CA    . ASP A 19  ? 0.1708 0.1393 0.0942 0.0083  -0.0529 0.0002  19  ASP A CA    
113  C C     . ASP A 19  ? 0.2646 0.2419 0.2042 0.0069  -0.0538 0.0008  19  ASP A C     
114  O O     . ASP A 19  ? 0.3138 0.2890 0.2586 0.0079  -0.0590 -0.0009 19  ASP A O     
115  C CB    . ASP A 19  ? 0.4754 0.4405 0.3931 0.0090  -0.0535 -0.0021 19  ASP A CB    
116  C CG    . ASP A 19  ? 0.6547 0.6096 0.5559 0.0108  -0.0525 -0.0028 19  ASP A CG    
117  O OD1   . ASP A 19  ? 0.6430 0.5911 0.5370 0.0126  -0.0543 -0.0024 19  ASP A OD1   
118  O OD2   . ASP A 19  ? 0.6815 0.6348 0.5767 0.0106  -0.0496 -0.0036 19  ASP A OD2   
119  N N     . THR A 20  ? 0.2792 0.2655 0.2268 0.0048  -0.0488 0.0031  20  THR A N     
120  C CA    . THR A 20  ? 0.2803 0.2739 0.2428 0.0037  -0.0489 0.0037  20  THR A CA    
121  C C     . THR A 20  ? 0.4473 0.4373 0.4127 0.0045  -0.0529 0.0040  20  THR A C     
122  O O     . THR A 20  ? 0.5536 0.5442 0.5285 0.0044  -0.0558 0.0033  20  THR A O     
123  C CB    . THR A 20  ? 0.1843 0.1872 0.1533 0.0020  -0.0423 0.0057  20  THR A CB    
124  O OG1   . THR A 20  ? 0.2693 0.2758 0.2370 0.0015  -0.0389 0.0051  20  THR A OG1   
125  C CG2   . THR A 20  ? 0.2659 0.2740 0.2488 0.0010  -0.0418 0.0064  20  THR A CG2   
126  N N     . TYR A 21  ? 0.3090 0.2945 0.2662 0.0053  -0.0531 0.0048  21  TYR A N     
127  C CA    . TYR A 21  ? 0.3638 0.3452 0.3223 0.0062  -0.0571 0.0049  21  TYR A CA    
128  C C     . TYR A 21  ? 0.5586 0.5293 0.5068 0.0089  -0.0631 0.0026  21  TYR A C     
129  O O     . TYR A 21  ? 0.6620 0.6273 0.5982 0.0101  -0.0626 0.0019  21  TYR A O     
130  C CB    . TYR A 21  ? 0.2228 0.2060 0.1793 0.0056  -0.0535 0.0073  21  TYR A CB    
131  C CG    . TYR A 21  ? 0.2007 0.1933 0.1688 0.0035  -0.0487 0.0092  21  TYR A CG    
132  C CD1   . TYR A 21  ? 0.4396 0.4386 0.4095 0.0024  -0.0430 0.0100  21  TYR A CD1   
133  C CD2   . TYR A 21  ? 0.1484 0.1424 0.1251 0.0027  -0.0499 0.0099  21  TYR A CD2   
134  C CE1   . TYR A 21  ? 0.4670 0.4725 0.4466 0.0008  -0.0388 0.0111  21  TYR A CE1   
135  C CE2   . TYR A 21  ? 0.1889 0.1895 0.1751 0.0008  -0.0453 0.0114  21  TYR A CE2   
136  C CZ    . TYR A 21  ? 0.3333 0.3392 0.3207 -0.0001 -0.0399 0.0120  21  TYR A CZ    
137  O OH    . TYR A 21  ? 0.3475 0.3579 0.3435 -0.0023 -0.0354 0.0135  21  TYR A OH    
138  N N     . LYS A 22  ? 0.5740 0.5411 0.5268 0.0099  -0.0685 0.0014  22  LYS A N     
139  C CA    . LYS A 22  ? 0.5732 0.5302 0.5177 0.0128  -0.0749 -0.0011 22  LYS A CA    
140  C C     . LYS A 22  ? 0.6263 0.5773 0.5636 0.0142  -0.0771 -0.0007 22  LYS A C     
141  O O     . LYS A 22  ? 0.6907 0.6325 0.6181 0.0170  -0.0817 -0.0026 22  LYS A O     
142  C CB    . LYS A 22  ? 0.5202 0.4764 0.4743 0.0134  -0.0801 -0.0033 22  LYS A CB    
143  C CG    . LYS A 22  ? 0.3749 0.3384 0.3395 0.0115  -0.0775 -0.0033 22  LYS A CG    
144  C CD    . LYS A 22  ? 0.2654 0.2363 0.2438 0.0091  -0.0746 -0.0013 22  LYS A CD    
145  C CE    . LYS A 22  ? 0.3152 0.2936 0.3026 0.0073  -0.0704 -0.0008 22  LYS A CE    
146  N NZ    . LYS A 22  ? 0.3161 0.3009 0.3143 0.0050  -0.0663 0.0016  22  LYS A NZ    
147  N N     . ASN A 23  ? 0.6123 0.5681 0.5542 0.0126  -0.0739 0.0018  23  ASN A N     
148  C CA    . ASN A 23  ? 0.4052 0.3560 0.3403 0.0137  -0.0751 0.0025  23  ASN A CA    
149  C C     . ASN A 23  ? 0.3301 0.2763 0.2509 0.0148  -0.0721 0.0031  23  ASN A C     
150  O O     . ASN A 23  ? 0.3386 0.2900 0.2590 0.0131  -0.0660 0.0051  23  ASN A O     
151  C CB    . ASN A 23  ? 0.3669 0.3248 0.3115 0.0115  -0.0719 0.0050  23  ASN A CB    
152  C CG    . ASN A 23  ? 0.3521 0.3054 0.2916 0.0126  -0.0738 0.0057  23  ASN A CG    
153  O OD1   . ASN A 23  ? 0.3982 0.3427 0.3261 0.0151  -0.0770 0.0045  23  ASN A OD1   
154  N ND2   . ASN A 23  ? 0.1735 0.1322 0.1214 0.0108  -0.0717 0.0076  23  ASN A ND2   
155  N N     . GLU A 24  ? 0.4010 0.3369 0.3098 0.0178  -0.0762 0.0012  24  GLU A N     
156  C CA    . GLU A 24  ? 0.4273 0.3571 0.3216 0.0191  -0.0734 0.0013  24  GLU A CA    
157  C C     . GLU A 24  ? 0.5099 0.4391 0.3989 0.0187  -0.0694 0.0037  24  GLU A C     
158  O O     . GLU A 24  ? 0.6067 0.5316 0.4849 0.0194  -0.0657 0.0042  24  GLU A O     
159  C CB    . GLU A 24  ? 0.4071 0.3254 0.2900 0.0228  -0.0791 -0.0014 24  GLU A CB    
160  C CG    . GLU A 24  ? 0.4586 0.3767 0.3480 0.0235  -0.0846 -0.0040 24  GLU A CG    
161  C CD    . GLU A 24  ? 0.6516 0.5621 0.5302 0.0260  -0.0865 -0.0064 24  GLU A CD    
162  O OE1   . GLU A 24  ? 0.7973 0.7059 0.6793 0.0272  -0.0916 -0.0089 24  GLU A OE1   
163  O OE2   . GLU A 24  ? 0.7543 0.6602 0.6208 0.0268  -0.0828 -0.0058 24  GLU A OE2   
164  N N     . GLU A 25  ? 0.5218 0.4550 0.4183 0.0177  -0.0699 0.0051  25  GLU A N     
165  C CA    . GLU A 25  ? 0.5614 0.4950 0.4545 0.0172  -0.0660 0.0073  25  GLU A CA    
166  C C     . GLU A 25  ? 0.6710 0.6139 0.5699 0.0142  -0.0588 0.0097  25  GLU A C     
167  O O     . GLU A 25  ? 0.8288 0.7721 0.7246 0.0137  -0.0549 0.0115  25  GLU A O     
168  C CB    . GLU A 25  ? 0.6650 0.5994 0.5641 0.0172  -0.0693 0.0079  25  GLU A CB    
169  C CG    . GLU A 25  ? 0.6953 0.6191 0.5834 0.0203  -0.0739 0.0067  25  GLU A CG    
170  C CD    . GLU A 25  ? 0.7211 0.6461 0.6161 0.0202  -0.0774 0.0071  25  GLU A CD    
171  O OE1   . GLU A 25  ? 0.7353 0.6523 0.6221 0.0226  -0.0811 0.0064  25  GLU A OE1   
172  O OE2   . GLU A 25  ? 0.7798 0.7132 0.6880 0.0177  -0.0764 0.0081  25  GLU A OE2   
173  N N     . LEU A 26  ? 0.5642 0.5143 0.4716 0.0124  -0.0570 0.0096  26  LEU A N     
174  C CA    . LEU A 26  ? 0.4725 0.4324 0.3873 0.0098  -0.0506 0.0117  26  LEU A CA    
175  C C     . LEU A 26  ? 0.4241 0.3818 0.3298 0.0097  -0.0454 0.0122  26  LEU A C     
176  O O     . LEU A 26  ? 0.2869 0.2383 0.1841 0.0109  -0.0463 0.0106  26  LEU A O     
177  C CB    . LEU A 26  ? 0.3386 0.3068 0.2659 0.0082  -0.0504 0.0113  26  LEU A CB    
178  C CG    . LEU A 26  ? 0.4430 0.4132 0.3808 0.0080  -0.0549 0.0108  26  LEU A CG    
179  C CD1   . LEU A 26  ? 0.4016 0.3774 0.3497 0.0068  -0.0551 0.0100  26  LEU A CD1   
180  C CD2   . LEU A 26  ? 0.4570 0.4320 0.4014 0.0068  -0.0526 0.0129  26  LEU A CD2   
181  N N     . ILE A 27  ? 0.4392 0.4015 0.3467 0.0082  -0.0399 0.0143  27  ILE A N     
182  C CA    . ILE A 27  ? 0.3406 0.3033 0.2435 0.0073  -0.0338 0.0149  27  ILE A CA    
183  C C     . ILE A 27  ? 0.3310 0.3051 0.2458 0.0052  -0.0300 0.0157  27  ILE A C     
184  O O     . ILE A 27  ? 0.2293 0.2111 0.1546 0.0043  -0.0293 0.0167  27  ILE A O     
185  C CB    . ILE A 27  ? 0.3162 0.2768 0.2146 0.0072  -0.0301 0.0165  27  ILE A CB    
186  C CG1   . ILE A 27  ? 0.3550 0.3033 0.2395 0.0098  -0.0325 0.0157  27  ILE A CG1   
187  C CG2   . ILE A 27  ? 0.5073 0.4710 0.4058 0.0057  -0.0234 0.0172  27  ILE A CG2   
188  C CD1   . ILE A 27  ? 0.3285 0.2743 0.2086 0.0097  -0.0286 0.0172  27  ILE A CD1   
189  N N     . HIS A 28  ? 0.3672 0.3417 0.2798 0.0046  -0.0273 0.0149  28  HIS A N     
190  C CA    . HIS A 28  ? 0.3836 0.3679 0.3065 0.0032  -0.0243 0.0151  28  HIS A CA    
191  C C     . HIS A 28  ? 0.5103 0.4975 0.4332 0.0022  -0.0176 0.0160  28  HIS A C     
192  O O     . HIS A 28  ? 0.5987 0.5796 0.5124 0.0021  -0.0154 0.0155  28  HIS A O     
193  C CB    . HIS A 28  ? 0.3692 0.3525 0.2916 0.0035  -0.0271 0.0133  28  HIS A CB    
194  C CG    . HIS A 28  ? 0.1396 0.1205 0.0644 0.0045  -0.0338 0.0121  28  HIS A CG    
195  N ND1   . HIS A 28  ? 0.1898 0.1605 0.1047 0.0064  -0.0386 0.0104  28  HIS A ND1   
196  C CD2   . HIS A 28  ? 0.1502 0.1366 0.0862 0.0041  -0.0364 0.0121  28  HIS A CD2   
197  C CE1   . HIS A 28  ? 0.2530 0.2237 0.1737 0.0071  -0.0441 0.0094  28  HIS A CE1   
198  N NE2   . HIS A 28  ? 0.2842 0.2643 0.2179 0.0055  -0.0427 0.0105  28  HIS A NE2   
199  N N     . ALA A 29  ? 0.4083 0.4032 0.3414 0.0023  -0.0143 0.0168  29  ALA A N     
200  C CA    . ALA A 29  ? 0.3759 0.3724 0.3105 0.0021  -0.0082 0.0171  29  ALA A CA    
201  C C     . ALA A 29  ? 0.3366 0.3330 0.2800 0.0009  -0.0064 0.0157  29  ALA A C     
202  O O     . ALA A 29  ? 0.5022 0.5001 0.4512 -0.0018 -0.0030 0.0157  29  ALA A O     
203  C CB    . ALA A 29  ? 0.6223 0.6180 0.5556 0.0017  -0.0060 0.0185  29  ALA A CB    
204  N N     . TRP A 30  ? 0.4216 0.4202 0.3699 -0.0001 -0.0095 0.0147  30  TRP A N     
205  C CA    . TRP A 30  ? 0.4394 0.4471 0.4032 -0.0051 -0.0084 0.0147  30  TRP A CA    
206  C C     . TRP A 30  ? 0.5266 0.5374 0.4931 -0.0066 -0.0054 0.0138  30  TRP A C     
207  O O     . TRP A 30  ? 0.6132 0.6310 0.5882 -0.0088 -0.0023 0.0136  30  TRP A O     
208  C CB    . TRP A 30  ? 0.1695 0.1809 0.1408 -0.0056 -0.0127 0.0149  30  TRP A CB    
209  C CG    . TRP A 30  ? 0.1463 0.1523 0.1097 -0.0018 -0.0174 0.0134  30  TRP A CG    
210  C CD1   . TRP A 30  ? 0.2379 0.2404 0.1909 0.0020  -0.0204 0.0130  30  TRP A CD1   
211  C CD2   . TRP A 30  ? 0.2468 0.2558 0.2158 -0.0024 -0.0193 0.0124  30  TRP A CD2   
212  N NE1   . TRP A 30  ? 0.3469 0.3503 0.2993 0.0024  -0.0242 0.0119  30  TRP A NE1   
213  C CE2   . TRP A 30  ? 0.2653 0.2718 0.2265 0.0013  -0.0238 0.0109  30  TRP A CE2   
214  C CE3   . TRP A 30  ? 0.4171 0.4339 0.3986 -0.0061 -0.0165 0.0133  30  TRP A CE3   
215  C CZ2   . TRP A 30  ? 0.2218 0.2307 0.1866 0.0015  -0.0266 0.0094  30  TRP A CZ2   
216  C CZ3   . TRP A 30  ? 0.2659 0.2827 0.2493 -0.0050 -0.0194 0.0118  30  TRP A CZ3   
217  C CH2   . TRP A 30  ? 0.1222 0.1346 0.0972 -0.0007 -0.0249 0.0093  30  TRP A CH2   
218  N N     . ILE A 31  ? 0.4124 0.4184 0.3718 -0.0046 -0.0070 0.0129  31  ILE A N     
219  C CA    . ILE A 31  ? 0.3292 0.3382 0.2916 -0.0061 -0.0042 0.0121  31  ILE A CA    
220  C C     . ILE A 31  ? 0.0672 0.0708 0.0218 -0.0050 0.0004  0.0119  31  ILE A C     
221  O O     . ILE A 31  ? 0.4743 0.4721 0.4187 -0.0015 0.0012  0.0127  31  ILE A O     
222  C CB    . ILE A 31  ? 0.2975 0.3025 0.2537 -0.0038 -0.0076 0.0110  31  ILE A CB    
223  C CG1   . ILE A 31  ? 0.1774 0.1904 0.1440 -0.0069 -0.0058 0.0106  31  ILE A CG1   
224  C CG2   . ILE A 31  ? 0.3141 0.3131 0.2559 0.0009  -0.0074 0.0105  31  ILE A CG2   
225  C CD1   . ILE A 31  ? 0.0600 0.0697 0.0223 -0.0049 -0.0098 0.0092  31  ILE A CD1   
226  N N     . ALA A 32  ? 0.1061 0.1147 0.0678 -0.0071 0.0033  0.0111  32  ALA A N     
227  C CA    . ALA A 32  ? 0.0654 0.0702 0.0229 -0.0063 0.0077  0.0111  32  ALA A CA    
228  C C     . ALA A 32  ? 0.0832 0.0831 0.0307 -0.0034 0.0100  0.0113  32  ALA A C     
229  O O     . ALA A 32  ? 0.3504 0.3517 0.3006 -0.0042 0.0128  0.0107  32  ALA A O     
230  C CB    . ALA A 32  ? 0.0523 0.0660 0.0229 -0.0090 0.0081  0.0100  32  ALA A CB    
231  N N     . ASP A 33  ? 0.3051 0.3040 0.2438 -0.0011 0.0075  0.0118  33  ASP A N     
232  C CA    . ASP A 33  ? 0.0972 0.0940 0.0274 -0.0022 0.0083  0.0112  33  ASP A CA    
233  C C     . ASP A 33  ? 0.1102 0.0999 0.0305 -0.0027 0.0078  0.0114  33  ASP A C     
234  O O     . ASP A 33  ? 0.2037 0.1932 0.1234 -0.0022 0.0053  0.0123  33  ASP A O     
235  C CB    . ASP A 33  ? 0.3787 0.3743 0.3048 -0.0017 0.0051  0.0097  33  ASP A CB    
236  C CG    . ASP A 33  ? 0.4472 0.4412 0.3695 -0.0009 -0.0007 0.0095  33  ASP A CG    
237  O OD1   . ASP A 33  ? 0.3879 0.3820 0.3111 -0.0006 -0.0023 0.0107  33  ASP A OD1   
238  O OD2   . ASP A 33  ? 0.4315 0.4233 0.3500 -0.0006 -0.0042 0.0080  33  ASP A OD2   
239  N N     . MET A 34  ? 0.3262 0.3082 0.2382 -0.0030 0.0107  0.0107  34  MET A N     
240  C CA    . MET A 34  ? 0.3718 0.3444 0.2737 -0.0023 0.0114  0.0110  34  MET A CA    
241  C C     . MET A 34  ? 0.3711 0.3337 0.2601 -0.0003 0.0080  0.0102  34  MET A C     
242  O O     . MET A 34  ? 0.4421 0.4033 0.3283 0.0003  0.0060  0.0090  34  MET A O     
243  C CB    . MET A 34  ? 0.2959 0.2641 0.1953 -0.0028 0.0165  0.0108  34  MET A CB    
244  C CG    . MET A 34  ? 0.1702 0.1459 0.0805 -0.0044 0.0190  0.0115  34  MET A CG    
245  S SD    . MET A 34  ? 0.4170 0.3863 0.3238 -0.0049 0.0244  0.0108  34  MET A SD    
246  C CE    . MET A 34  ? 0.3147 0.2853 0.2227 -0.0053 0.0250  0.0096  34  MET A CE    
247  N N     . ASP A 35  ? 0.2834 0.2387 0.1646 0.0011  0.0070  0.0108  35  ASP A N     
248  C CA    . ASP A 35  ? 0.4598 0.4039 0.3276 0.0038  0.0038  0.0100  35  ASP A CA    
249  C C     . ASP A 35  ? 0.5914 0.5248 0.4481 0.0051  0.0078  0.0097  35  ASP A C     
250  O O     . ASP A 35  ? 0.6461 0.5695 0.4916 0.0075  0.0067  0.0097  35  ASP A O     
251  C CB    . ASP A 35  ? 0.4683 0.4103 0.3338 0.0050  -0.0001 0.0107  35  ASP A CB    
252  C CG    . ASP A 35  ? 0.4802 0.4308 0.3550 0.0042  -0.0048 0.0108  35  ASP A CG    
253  O OD1   . ASP A 35  ? 0.5564 0.5115 0.4357 0.0037  -0.0064 0.0099  35  ASP A OD1   
254  O OD2   . ASP A 35  ? 0.5811 0.5337 0.4590 0.0043  -0.0069 0.0119  35  ASP A OD2   
255  N N     . PHE A 36  ? 0.4854 0.4202 0.3448 0.0038  0.0123  0.0094  36  PHE A N     
256  C CA    . PHE A 36  ? 0.4611 0.3861 0.3111 0.0050  0.0166  0.0094  36  PHE A CA    
257  C C     . PHE A 36  ? 0.6108 0.5314 0.4550 0.0059  0.0169  0.0081  36  PHE A C     
258  O O     . PHE A 36  ? 0.7329 0.6605 0.5839 0.0046  0.0157  0.0073  36  PHE A O     
259  C CB    . PHE A 36  ? 0.4361 0.3652 0.2937 0.0030  0.0219  0.0101  36  PHE A CB    
260  C CG    . PHE A 36  ? 0.4983 0.4285 0.3583 0.0027  0.0223  0.0113  36  PHE A CG    
261  C CD1   . PHE A 36  ? 0.3390 0.2600 0.1883 0.0051  0.0210  0.0118  36  PHE A CD1   
262  C CD2   . PHE A 36  ? 0.5162 0.4565 0.3889 0.0004  0.0235  0.0119  36  PHE A CD2   
263  C CE1   . PHE A 36  ? 0.4642 0.3862 0.3156 0.0049  0.0214  0.0129  36  PHE A CE1   
264  C CE2   . PHE A 36  ? 0.4474 0.3887 0.3221 0.0003  0.0237  0.0129  36  PHE A CE2   
265  C CZ    . PHE A 36  ? 0.4952 0.4275 0.3594 0.0024  0.0227  0.0134  36  PHE A CZ    
266  N N     . GLU A 37  ? 0.6080 0.5165 0.4393 0.0082  0.0186  0.0079  37  GLU A N     
267  C CA    . GLU A 37  ? 0.5073 0.4108 0.3325 0.0091  0.0197  0.0068  37  GLU A CA    
268  C C     . GLU A 37  ? 0.5036 0.4142 0.3388 0.0064  0.0242  0.0068  37  GLU A C     
269  O O     . GLU A 37  ? 0.5144 0.4272 0.3549 0.0049  0.0282  0.0076  37  GLU A O     
270  C CB    . GLU A 37  ? 0.5300 0.4194 0.3403 0.0121  0.0219  0.0069  37  GLU A CB    
271  C CG    . GLU A 37  ? 0.6250 0.5055 0.4229 0.0155  0.0170  0.0058  37  GLU A CG    
272  C CD    . GLU A 37  ? 0.7189 0.5854 0.5021 0.0186  0.0197  0.0060  37  GLU A CD    
273  O OE1   . GLU A 37  ? 0.6956 0.5596 0.4787 0.0180  0.0255  0.0070  37  GLU A OE1   
274  O OE2   . GLU A 37  ? 0.7665 0.6243 0.5382 0.0219  0.0160  0.0051  37  GLU A OE2   
275  N N     . VAL A 38  ? 0.5624 0.4771 0.4009 0.0056  0.0231  0.0056  38  VAL A N     
276  C CA    . VAL A 38  ? 0.4452 0.3649 0.2913 0.0035  0.0272  0.0054  38  VAL A CA    
277  C C     . VAL A 38  ? 0.4229 0.3321 0.2598 0.0047  0.0319  0.0057  38  VAL A C     
278  O O     . VAL A 38  ? 0.4635 0.3617 0.2872 0.0075  0.0312  0.0055  38  VAL A O     
279  C CB    . VAL A 38  ? 0.3067 0.2317 0.1565 0.0029  0.0249  0.0041  38  VAL A CB    
280  C CG1   . VAL A 38  ? 0.2581 0.1935 0.1175 0.0018  0.0206  0.0040  38  VAL A CG1   
281  C CG2   . VAL A 38  ? 0.3031 0.2180 0.1396 0.0056  0.0229  0.0029  38  VAL A CG2   
282  N N     . PRO A 39  ? 0.3857 0.2972 0.2290 0.0028  0.0366  0.0060  39  PRO A N     
283  C CA    . PRO A 39  ? 0.3590 0.2603 0.1938 0.0039  0.0413  0.0061  39  PRO A CA    
284  C C     . PRO A 39  ? 0.4117 0.3055 0.2359 0.0060  0.0404  0.0053  39  PRO A C     
285  O O     . PRO A 39  ? 0.4237 0.3226 0.2512 0.0054  0.0379  0.0042  39  PRO A O     
286  C CB    . PRO A 39  ? 0.4040 0.3119 0.2501 0.0012  0.0450  0.0060  39  PRO A CB    
287  C CG    . PRO A 39  ? 0.4378 0.3575 0.2969 -0.0009 0.0429  0.0062  39  PRO A CG    
288  C CD    . PRO A 39  ? 0.4089 0.3318 0.2670 -0.0001 0.0376  0.0062  39  PRO A CD    
289  N N     . LYS A 40  ? 0.4369 0.3181 0.2479 0.0087  0.0424  0.0056  40  LYS A N     
290  C CA    . LYS A 40  ? 0.6521 0.5246 0.4514 0.0111  0.0416  0.0048  40  LYS A CA    
291  C C     . LYS A 40  ? 0.7180 0.5932 0.5215 0.0096  0.0441  0.0040  40  LYS A C     
292  O O     . LYS A 40  ? 0.7220 0.5963 0.5214 0.0107  0.0413  0.0028  40  LYS A O     
293  C CB    . LYS A 40  ? 0.6748 0.5331 0.4598 0.0143  0.0443  0.0056  40  LYS A CB    
294  C CG    . LYS A 40  ? 0.6985 0.5463 0.4691 0.0178  0.0425  0.0048  40  LYS A CG    
295  C CD    . LYS A 40  ? 0.7238 0.5685 0.4873 0.0203  0.0364  0.0043  40  LYS A CD    
296  C CE    . LYS A 40  ? 0.7436 0.5757 0.4911 0.0245  0.0346  0.0035  40  LYS A CE    
297  N NZ    . LYS A 40  ? 0.7451 0.5724 0.4845 0.0274  0.0287  0.0030  40  LYS A NZ    
298  N N     . PRO A 41  ? 0.6855 0.5638 0.4966 0.0074  0.0488  0.0044  41  PRO A N     
299  C CA    . PRO A 41  ? 0.6649 0.5458 0.4802 0.0061  0.0508  0.0036  41  PRO A CA    
300  C C     . PRO A 41  ? 0.6081 0.5005 0.4333 0.0042  0.0471  0.0026  41  PRO A C     
301  O O     . PRO A 41  ? 0.6629 0.5563 0.4889 0.0038  0.0476  0.0017  41  PRO A O     
302  C CB    . PRO A 41  ? 0.5879 0.4705 0.4107 0.0040  0.0559  0.0043  41  PRO A CB    
303  C CG    . PRO A 41  ? 0.5360 0.4124 0.3537 0.0052  0.0576  0.0054  41  PRO A CG    
304  C CD    . PRO A 41  ? 0.4761 0.3536 0.2908 0.0065  0.0528  0.0056  41  PRO A CD    
305  N N     . ILE A 42  ? 0.4942 0.3954 0.3273 0.0031  0.0435  0.0027  42  ILE A N     
306  C CA    . ILE A 42  ? 0.4701 0.3810 0.3109 0.0020  0.0396  0.0016  42  ILE A CA    
307  C C     . ILE A 42  ? 0.5860 0.4911 0.4161 0.0046  0.0355  0.0005  42  ILE A C     
308  O O     . ILE A 42  ? 0.6326 0.5406 0.4640 0.0044  0.0339  -0.0008 42  ILE A O     
309  C CB    . ILE A 42  ? 0.4222 0.3436 0.2742 0.0004  0.0371  0.0021  42  ILE A CB    
310  C CG1   . ILE A 42  ? 0.3956 0.3240 0.2598 -0.0022 0.0404  0.0027  42  ILE A CG1   
311  C CG2   . ILE A 42  ? 0.4315 0.3610 0.2888 0.0001  0.0324  0.0011  42  ILE A CG2   
312  C CD1   . ILE A 42  ? 0.4904 0.4286 0.3652 -0.0035 0.0381  0.0033  42  ILE A CD1   
313  N N     . GLN A 43  ? 0.4543 0.3511 0.2737 0.0071  0.0335  0.0008  43  GLN A N     
314  C CA    . GLN A 43  ? 0.3417 0.2316 0.1499 0.0100  0.0290  -0.0005 43  GLN A CA    
315  C C     . GLN A 43  ? 0.4044 0.2863 0.2039 0.0114  0.0313  -0.0013 43  GLN A C     
316  O O     . GLN A 43  ? 0.5354 0.4160 0.3306 0.0127  0.0279  -0.0029 43  GLN A O     
317  C CB    . GLN A 43  ? 0.5054 0.3864 0.3030 0.0128  0.0270  0.0001  43  GLN A CB    
318  C CG    . GLN A 43  ? 0.5165 0.4032 0.3216 0.0114  0.0267  0.0015  43  GLN A CG    
319  C CD    . GLN A 43  ? 0.5828 0.4606 0.3773 0.0142  0.0244  0.0020  43  GLN A CD    
320  O OE1   . GLN A 43  ? 0.6952 0.5710 0.4895 0.0141  0.0271  0.0034  43  GLN A OE1   
321  N NE2   . GLN A 43  ? 0.5647 0.4370 0.3503 0.0170  0.0191  0.0007  43  GLN A NE2   
322  N N     . THR A 44  ? 0.5524 0.4291 0.3495 0.0112  0.0371  -0.0002 44  THR A N     
323  C CA    . THR A 44  ? 0.6367 0.5053 0.4253 0.0126  0.0396  -0.0008 44  THR A CA    
324  C C     . THR A 44  ? 0.5021 0.3790 0.3001 0.0102  0.0405  -0.0017 44  THR A C     
325  O O     . THR A 44  ? 0.6915 0.5647 0.4836 0.0115  0.0395  -0.0030 44  THR A O     
326  C CB    . THR A 44  ? 0.6725 0.5324 0.4556 0.0133  0.0456  0.0007  44  THR A CB    
327  O OG1   . THR A 44  ? 0.7302 0.5819 0.5039 0.0158  0.0448  0.0016  44  THR A OG1   
328  C CG2   . THR A 44  ? 0.6298 0.4809 0.4037 0.0149  0.0484  0.0003  44  THR A CG2   
329  N N     . ALA A 45  ? 0.2735 0.1616 0.0861 0.0069  0.0419  -0.0013 45  ALA A N     
330  C CA    . ALA A 45  ? 0.3609 0.2577 0.1834 0.0047  0.0424  -0.0022 45  ALA A CA    
331  C C     . ALA A 45  ? 0.5323 0.4342 0.3560 0.0051  0.0370  -0.0039 45  ALA A C     
332  O O     . ALA A 45  ? 0.6552 0.5590 0.4800 0.0048  0.0368  -0.0051 45  ALA A O     
333  C CB    . ALA A 45  ? 0.3819 0.2893 0.2196 0.0015  0.0445  -0.0013 45  ALA A CB    
334  N N     . LEU A 46  ? 0.6321 0.5366 0.4561 0.0058  0.0324  -0.0040 46  LEU A N     
335  C CA    . LEU A 46  ? 0.4536 0.3626 0.2788 0.0063  0.0268  -0.0058 46  LEU A CA    
336  C C     . LEU A 46  ? 0.4064 0.3050 0.2175 0.0095  0.0238  -0.0075 46  LEU A C     
337  O O     . LEU A 46  ? 0.5426 0.4436 0.3544 0.0097  0.0208  -0.0096 46  LEU A O     
338  C CB    . LEU A 46  ? 0.3231 0.2371 0.1526 0.0062  0.0226  -0.0055 46  LEU A CB    
339  C CG    . LEU A 46  ? 0.3641 0.2903 0.2088 0.0032  0.0241  -0.0042 46  LEU A CG    
340  C CD1   . LEU A 46  ? 0.3538 0.2853 0.2025 0.0033  0.0193  -0.0042 46  LEU A CD1   
341  C CD2   . LEU A 46  ? 0.4537 0.3887 0.3088 0.0012  0.0256  -0.0049 46  LEU A CD2   
342  N N     . LYS A 47  ? 0.3439 0.2306 0.1421 0.0121  0.0245  -0.0068 47  LYS A N     
343  C CA    . LYS A 47  ? 0.4583 0.3341 0.2424 0.0156  0.0216  -0.0084 47  LYS A CA    
344  C C     . LYS A 47  ? 0.6280 0.4999 0.4086 0.0157  0.0256  -0.0089 47  LYS A C     
345  O O     . LYS A 47  ? 0.7181 0.5857 0.4917 0.0175  0.0227  -0.0109 47  LYS A O     
346  C CB    . LYS A 47  ? 0.5030 0.3669 0.2741 0.0187  0.0212  -0.0074 47  LYS A CB    
347  C CG    . LYS A 47  ? 0.5594 0.4108 0.3150 0.0227  0.0187  -0.0089 47  LYS A CG    
348  C CD    . LYS A 47  ? 0.5998 0.4396 0.3444 0.0247  0.0242  -0.0073 47  LYS A CD    
349  C CE    . LYS A 47  ? 0.5777 0.4178 0.3243 0.0232  0.0296  -0.0072 47  LYS A CE    
350  N NZ    . LYS A 47  ? 0.6109 0.4380 0.3448 0.0258  0.0340  -0.0060 47  LYS A NZ    
351  N N     . GLN A 48  ? 0.5892 0.4626 0.3747 0.0137  0.0319  -0.0072 48  GLN A N     
352  C CA    . GLN A 48  ? 0.5197 0.3905 0.3037 0.0133  0.0358  -0.0075 48  GLN A CA    
353  C C     . GLN A 48  ? 0.5680 0.4484 0.3610 0.0116  0.0338  -0.0094 48  GLN A C     
354  O O     . GLN A 48  ? 0.8233 0.6999 0.6110 0.0126  0.0338  -0.0108 48  GLN A O     
355  C CB    . GLN A 48  ? 0.5712 0.4428 0.3610 0.0112  0.0425  -0.0055 48  GLN A CB    
356  C CG    . GLN A 48  ? 0.7137 0.5788 0.4987 0.0115  0.0473  -0.0054 48  GLN A CG    
357  C CD    . GLN A 48  ? 0.7675 0.6326 0.5581 0.0096  0.0533  -0.0035 48  GLN A CD    
358  O OE1   . GLN A 48  ? 0.8629 0.7347 0.6630 0.0076  0.0538  -0.0026 48  GLN A OE1   
359  N NE2   . GLN A 48  ? 0.6283 0.4854 0.4129 0.0103  0.0579  -0.0031 48  GLN A NE2   
360  N N     . ARG A 49  ? 0.5085 0.4011 0.3147 0.0091  0.0319  -0.0094 49  ARG A N     
361  C CA    . ARG A 49  ? 0.5546 0.4568 0.3703 0.0074  0.0305  -0.0111 49  ARG A CA    
362  C C     . ARG A 49  ? 0.6060 0.5061 0.4156 0.0095  0.0244  -0.0139 49  ARG A C     
363  O O     . ARG A 49  ? 0.6384 0.5405 0.4492 0.0093  0.0239  -0.0158 49  ARG A O     
364  C CB    . ARG A 49  ? 0.5027 0.4181 0.3340 0.0045  0.0302  -0.0103 49  ARG A CB    
365  C CG    . ARG A 49  ? 0.5616 0.4874 0.4033 0.0030  0.0284  -0.0120 49  ARG A CG    
366  C CD    . ARG A 49  ? 0.5943 0.5191 0.4362 0.0024  0.0320  -0.0125 49  ARG A CD    
367  N NE    . ARG A 49  ? 0.5699 0.5040 0.4210 0.0014  0.0302  -0.0143 49  ARG A NE    
368  C CZ    . ARG A 49  ? 0.5755 0.5086 0.4222 0.0028  0.0260  -0.0171 49  ARG A CZ    
369  N NH1   . ARG A 49  ? 0.5097 0.4328 0.3431 0.0054  0.0227  -0.0185 49  ARG A NH1   
370  N NH2   . ARG A 49  ? 0.5075 0.4494 0.3635 0.0018  0.0247  -0.0188 49  ARG A NH2   
371  N N     . ILE A 50  ? 0.6632 0.5586 0.4658 0.0116  0.0196  -0.0144 50  ILE A N     
372  C CA    . ILE A 50  ? 0.5802 0.4731 0.3775 0.0136  0.0130  -0.0173 50  ILE A CA    
373  C C     . ILE A 50  ? 0.6143 0.4958 0.3982 0.0164  0.0131  -0.0187 50  ILE A C     
374  O O     . ILE A 50  ? 0.8728 0.7531 0.6539 0.0177  0.0084  -0.0215 50  ILE A O     
375  C CB    . ILE A 50  ? 0.5605 0.4511 0.3547 0.0152  0.0075  -0.0173 50  ILE A CB    
376  C CG1   . ILE A 50  ? 0.5042 0.4068 0.3124 0.0123  0.0075  -0.0161 50  ILE A CG1   
377  C CG2   . ILE A 50  ? 0.6855 0.5724 0.4743 0.0176  -0.0001 -0.0205 50  ILE A CG2   
378  C CD1   . ILE A 50  ? 0.5249 0.4290 0.3343 0.0132  0.0006  -0.0171 50  ILE A CD1   
379  N N     . LYS A 51  ? 0.5197 0.3930 0.2958 0.0173  0.0183  -0.0167 51  LYS A N     
380  C CA    . LYS A 51  ? 0.5369 0.4000 0.3010 0.0198  0.0191  -0.0179 51  LYS A CA    
381  C C     . LYS A 51  ? 0.6760 0.5451 0.4466 0.0181  0.0203  -0.0196 51  LYS A C     
382  O O     . LYS A 51  ? 0.7730 0.6352 0.5347 0.0202  0.0194  -0.0213 51  LYS A O     
383  C CB    . LYS A 51  ? 0.5031 0.3567 0.2589 0.0209  0.0252  -0.0153 51  LYS A CB    
384  C CG    . LYS A 51  ? 0.5282 0.3734 0.2749 0.0233  0.0241  -0.0139 51  LYS A CG    
385  C CD    . LYS A 51  ? 0.6543 0.4885 0.3864 0.0277  0.0187  -0.0157 51  LYS A CD    
386  C CE    . LYS A 51  ? 0.7042 0.5292 0.4265 0.0305  0.0181  -0.0142 51  LYS A CE    
387  N NZ    . LYS A 51  ? 0.7126 0.5294 0.4283 0.0312  0.0251  -0.0117 51  LYS A NZ    
388  N N     . HIS A 52  ? 0.6234 0.5052 0.4091 0.0146  0.0222  -0.0192 52  HIS A N     
389  C CA    . HIS A 52  ? 0.6078 0.4965 0.4009 0.0129  0.0228  -0.0209 52  HIS A CA    
390  C C     . HIS A 52  ? 0.6465 0.5439 0.4474 0.0123  0.0166  -0.0237 52  HIS A C     
391  O O     . HIS A 52  ? 0.5480 0.4559 0.3611 0.0100  0.0165  -0.0229 52  HIS A O     
392  C CB    . HIS A 52  ? 0.5400 0.4366 0.3448 0.0097  0.0291  -0.0187 52  HIS A CB    
393  C CG    . HIS A 52  ? 0.5841 0.4863 0.3954 0.0083  0.0305  -0.0202 52  HIS A CG    
394  N ND1   . HIS A 52  ? 0.5431 0.4581 0.3692 0.0057  0.0304  -0.0205 52  HIS A ND1   
395  C CD2   . HIS A 52  ? 0.5723 0.4689 0.3771 0.0094  0.0319  -0.0215 52  HIS A CD2   
396  C CE1   . HIS A 52  ? 0.5536 0.4706 0.3822 0.0052  0.0318  -0.0219 52  HIS A CE1   
397  N NE2   . HIS A 52  ? 0.5748 0.4810 0.3907 0.0073  0.0327  -0.0226 52  HIS A NE2   
398  N N     . PRO A 53  ? 0.6651 0.5579 0.4593 0.0145  0.0111  -0.0270 53  PRO A N     
399  C CA    . PRO A 53  ? 0.6483 0.5469 0.4485 0.0143  0.0041  -0.0299 53  PRO A CA    
400  C C     . PRO A 53  ? 0.6064 0.5168 0.4202 0.0116  0.0042  -0.0320 53  PRO A C     
401  O O     . PRO A 53  ? 0.6148 0.5258 0.4297 0.0121  -0.0007 -0.0356 53  PRO A O     
402  C CB    . PRO A 53  ? 0.6641 0.5513 0.4510 0.0179  -0.0014 -0.0326 53  PRO A CB    
403  C CG    . PRO A 53  ? 0.6626 0.5423 0.4406 0.0190  0.0033  -0.0321 53  PRO A CG    
404  C CD    . PRO A 53  ? 0.6143 0.4950 0.3942 0.0175  0.0109  -0.0281 53  PRO A CD    
405  N N     . ILE A 54  ? 0.4756 0.3951 0.3002 0.0090  0.0097  -0.0297 54  ILE A N     
406  C CA    . ILE A 54  ? 0.4528 0.3846 0.2917 0.0066  0.0101  -0.0311 54  ILE A CA    
407  C C     . ILE A 54  ? 0.4512 0.3925 0.3016 0.0045  0.0130  -0.0280 54  ILE A C     
408  O O     . ILE A 54  ? 0.5354 0.4747 0.3848 0.0040  0.0179  -0.0245 54  ILE A O     
409  C CB    . ILE A 54  ? 0.5670 0.4995 0.4072 0.0061  0.0145  -0.0316 54  ILE A CB    
410  C CG1   . ILE A 54  ? 0.7159 0.6399 0.5457 0.0082  0.0111  -0.0350 54  ILE A CG1   
411  C CG2   . ILE A 54  ? 0.6067 0.5521 0.4623 0.0041  0.0155  -0.0323 54  ILE A CG2   
412  C CD1   . ILE A 54  ? 0.7596 0.6814 0.5874 0.0082  0.0158  -0.0352 54  ILE A CD1   
413  N N     . PHE A 55  ? 0.1973 0.1486 0.0590 0.0033  0.0099  -0.0293 55  PHE A N     
414  C CA    . PHE A 55  ? 0.2228 0.1830 0.0953 0.0019  0.0118  -0.0266 55  PHE A CA    
415  C C     . PHE A 55  ? 0.1769 0.1482 0.0632 0.0009  0.0131  -0.0270 55  PHE A C     
416  O O     . PHE A 55  ? 0.2400 0.2195 0.1362 0.0007  0.0111  -0.0269 55  PHE A O     
417  C CB    . PHE A 55  ? 0.2697 0.2298 0.1414 0.0022  0.0064  -0.0270 55  PHE A CB    
418  C CG    . PHE A 55  ? 0.3928 0.3404 0.2500 0.0041  0.0041  -0.0268 55  PHE A CG    
419  C CD1   . PHE A 55  ? 0.4875 0.4299 0.3391 0.0046  0.0077  -0.0234 55  PHE A CD1   
420  C CD2   . PHE A 55  ? 0.4001 0.3403 0.2492 0.0059  -0.0017 -0.0300 55  PHE A CD2   
421  C CE1   . PHE A 55  ? 0.3913 0.3218 0.2292 0.0070  0.0058  -0.0232 55  PHE A CE1   
422  C CE2   . PHE A 55  ? 0.4896 0.4177 0.3249 0.0086  -0.0040 -0.0295 55  PHE A CE2   
423  C CZ    . PHE A 55  ? 0.3880 0.3113 0.2174 0.0092  -0.0001 -0.0261 55  PHE A CZ    
424  N N     . GLY A 56  ? 0.2964 0.2671 0.1832 0.0008  0.0168  -0.0270 56  GLY A N     
425  C CA    . GLY A 56  ? 0.3899 0.3687 0.2886 0.0005  0.0181  -0.0268 56  GLY A CA    
426  C C     . GLY A 56  ? 0.3970 0.3806 0.3055 -0.0013 0.0226  -0.0219 56  GLY A C     
427  O O     . GLY A 56  ? 0.5479 0.5305 0.4552 -0.0020 0.0233  -0.0196 56  GLY A O     
428  N N     . TYR A 57  ? 0.3500 0.3381 0.2687 -0.0028 0.0253  -0.0205 57  TYR A N     
429  C CA    . TYR A 57  ? 0.2163 0.2090 0.1464 -0.0060 0.0287  -0.0167 57  TYR A CA    
430  C C     . TYR A 57  ? 0.3331 0.3214 0.2597 -0.0075 0.0327  -0.0150 57  TYR A C     
431  O O     . TYR A 57  ? 0.2865 0.2701 0.2073 -0.0073 0.0348  -0.0158 57  TYR A O     
432  C CB    . TYR A 57  ? 0.3660 0.3645 0.3088 -0.0085 0.0299  -0.0164 57  TYR A CB    
433  C CG    . TYR A 57  ? 0.3438 0.3463 0.2918 -0.0079 0.0266  -0.0180 57  TYR A CG    
434  C CD1   . TYR A 57  ? 0.2783 0.2864 0.2355 -0.0095 0.0250  -0.0169 57  TYR A CD1   
435  C CD2   . TYR A 57  ? 0.3847 0.3851 0.3289 -0.0060 0.0247  -0.0213 57  TYR A CD2   
436  C CE1   . TYR A 57  ? 0.4509 0.4631 0.4141 -0.0097 0.0220  -0.0187 57  TYR A CE1   
437  C CE2   . TYR A 57  ? 0.3854 0.3886 0.3346 -0.0071 0.0217  -0.0243 57  TYR A CE2   
438  C CZ    . TYR A 57  ? 0.4327 0.4434 0.3923 -0.0100 0.0208  -0.0235 57  TYR A CZ    
439  O OH    . TYR A 57  ? 0.3318 0.3505 0.3001 -0.0129 0.0178  -0.0284 57  TYR A OH    
440  N N     . THR A 58  ? 0.3871 0.3764 0.3174 -0.0088 0.0337  -0.0128 58  THR A N     
441  C CA    . THR A 58  ? 0.3609 0.3451 0.2873 -0.0098 0.0370  -0.0116 58  THR A CA    
442  C C     . THR A 58  ? 0.3980 0.3866 0.3360 -0.0123 0.0383  -0.0102 58  THR A C     
443  O O     . THR A 58  ? 0.1924 0.1874 0.1397 -0.0131 0.0361  -0.0097 58  THR A O     
444  C CB    . THR A 58  ? 0.4736 0.4521 0.3899 -0.0083 0.0364  -0.0112 58  THR A CB    
445  O OG1   . THR A 58  ? 0.5312 0.5144 0.4538 -0.0088 0.0347  -0.0098 58  THR A OG1   
446  C CG2   . THR A 58  ? 0.4897 0.4635 0.3943 -0.0057 0.0334  -0.0134 58  THR A CG2   
447  N N     . LEU A 59  ? 0.5273 0.5118 0.4641 -0.0134 0.0417  -0.0099 59  LEU A N     
448  C CA    . LEU A 59  ? 0.2534 0.2399 0.1980 -0.0153 0.0428  -0.0093 59  LEU A CA    
449  C C     . LEU A 59  ? 0.1185 0.1024 0.0599 -0.0150 0.0433  -0.0082 59  LEU A C     
450  O O     . LEU A 59  ? 0.2046 0.1822 0.1358 -0.0137 0.0443  -0.0079 59  LEU A O     
451  C CB    . LEU A 59  ? 0.3195 0.3018 0.2628 -0.0162 0.0461  -0.0098 59  LEU A CB    
452  C CG    . LEU A 59  ? 0.3046 0.2878 0.2495 -0.0165 0.0465  -0.0109 59  LEU A CG    
453  C CD1   . LEU A 59  ? 0.1890 0.1640 0.1245 -0.0161 0.0501  -0.0113 59  LEU A CD1   
454  C CD2   . LEU A 59  ? 0.1636 0.1521 0.1196 -0.0182 0.0458  -0.0115 59  LEU A CD2   
455  N N     . PRO A 60  ? 0.1336 0.1213 0.0829 -0.0161 0.0426  -0.0078 60  PRO A N     
456  C CA    . PRO A 60  ? 0.1502 0.1346 0.0968 -0.0160 0.0439  -0.0070 60  PRO A CA    
457  C C     . PRO A 60  ? 0.2696 0.2456 0.2082 -0.0160 0.0480  -0.0070 60  PRO A C     
458  O O     . PRO A 60  ? 0.3840 0.3581 0.3227 -0.0166 0.0499  -0.0078 60  PRO A O     
459  C CB    . PRO A 60  ? 0.1315 0.1212 0.0881 -0.0172 0.0427  -0.0071 60  PRO A CB    
460  C CG    . PRO A 60  ? 0.2811 0.2774 0.2452 -0.0173 0.0394  -0.0076 60  PRO A CG    
461  C CD    . PRO A 60  ? 0.0973 0.0923 0.0576 -0.0170 0.0400  -0.0082 60  PRO A CD    
462  N N     . PRO A 61  ? 0.2007 0.1707 0.1316 -0.0152 0.0495  -0.0062 61  PRO A N     
463  C CA    . PRO A 61  ? 0.2123 0.1730 0.1347 -0.0150 0.0537  -0.0062 61  PRO A CA    
464  C C     . PRO A 61  ? 0.2797 0.2402 0.2076 -0.0164 0.0562  -0.0066 61  PRO A C     
465  O O     . PRO A 61  ? 0.3374 0.3040 0.2746 -0.0175 0.0546  -0.0069 61  PRO A O     
466  C CB    . PRO A 61  ? 0.1908 0.1463 0.1059 -0.0139 0.0542  -0.0052 61  PRO A CB    
467  C CG    . PRO A 61  ? 0.1754 0.1363 0.0919 -0.0131 0.0502  -0.0049 61  PRO A CG    
468  C CD    . PRO A 61  ? 0.2044 0.1753 0.1335 -0.0144 0.0476  -0.0053 61  PRO A CD    
469  N N     . GLU A 62  ? 0.1890 0.1422 0.1108 -0.0163 0.0599  -0.0068 62  GLU A N     
470  C CA    . GLU A 62  ? 0.3329 0.2850 0.2590 -0.0176 0.0624  -0.0073 62  GLU A CA    
471  C C     . GLU A 62  ? 0.4187 0.3701 0.3473 -0.0180 0.0635  -0.0070 62  GLU A C     
472  O O     . GLU A 62  ? 0.6463 0.6015 0.5827 -0.0191 0.0632  -0.0076 62  GLU A O     
473  C CB    . GLU A 62  ? 0.5004 0.4438 0.4184 -0.0171 0.0665  -0.0074 62  GLU A CB    
474  C CG    . GLU A 62  ? 0.5492 0.4927 0.4645 -0.0167 0.0658  -0.0080 62  GLU A CG    
475  C CD    . GLU A 62  ? 0.7452 0.6794 0.6516 -0.0160 0.0700  -0.0080 62  GLU A CD    
476  O OE1   . GLU A 62  ? 0.6069 0.5333 0.5069 -0.0153 0.0732  -0.0073 62  GLU A OE1   
477  O OE2   . GLU A 62  ? 0.8493 0.7836 0.7550 -0.0160 0.0701  -0.0086 62  GLU A OE2   
478  N N     . ASN A 63  ? 0.3725 0.3186 0.2941 -0.0170 0.0646  -0.0060 63  ASN A N     
479  C CA    . ASN A 63  ? 0.2987 0.2425 0.2211 -0.0172 0.0663  -0.0057 63  ASN A CA    
480  C C     . ASN A 63  ? 0.3025 0.2535 0.2314 -0.0175 0.0628  -0.0054 63  ASN A C     
481  O O     . ASN A 63  ? 0.2770 0.2277 0.2085 -0.0179 0.0638  -0.0054 63  ASN A O     
482  C CB    . ASN A 63  ? 0.3360 0.2695 0.2468 -0.0158 0.0696  -0.0047 63  ASN A CB    
483  C CG    . ASN A 63  ? 0.6080 0.5405 0.5121 -0.0143 0.0673  -0.0039 63  ASN A CG    
484  O OD1   . ASN A 63  ? 0.7611 0.7000 0.6685 -0.0143 0.0637  -0.0042 63  ASN A OD1   
485  N ND2   . ASN A 63  ? 0.6960 0.6200 0.5904 -0.0129 0.0694  -0.0030 63  ASN A ND2   
486  N N     . ILE A 64  ? 0.4124 0.3698 0.3442 -0.0173 0.0589  -0.0053 64  ILE A N     
487  C CA    . ILE A 64  ? 0.3748 0.3378 0.3109 -0.0171 0.0557  -0.0048 64  ILE A CA    
488  C C     . ILE A 64  ? 0.4191 0.3873 0.3643 -0.0181 0.0547  -0.0053 64  ILE A C     
489  O O     . ILE A 64  ? 0.4073 0.3781 0.3549 -0.0180 0.0532  -0.0049 64  ILE A O     
490  C CB    . ILE A 64  ? 0.3222 0.2912 0.2603 -0.0166 0.0518  -0.0047 64  ILE A CB    
491  C CG1   . ILE A 64  ? 0.1811 0.1544 0.1214 -0.0161 0.0488  -0.0039 64  ILE A CG1   
492  C CG2   . ILE A 64  ? 0.4029 0.3786 0.3498 -0.0175 0.0499  -0.0057 64  ILE A CG2   
493  C CD1   . ILE A 64  ? 0.2407 0.2077 0.1718 -0.0150 0.0500  -0.0030 64  ILE A CD1   
494  N N     . GLY A 65  ? 0.3857 0.3553 0.3356 -0.0190 0.0554  -0.0064 65  GLY A N     
495  C CA    . GLY A 65  ? 0.3267 0.3003 0.2839 -0.0197 0.0545  -0.0070 65  GLY A CA    
496  C C     . GLY A 65  ? 0.2707 0.2388 0.2253 -0.0199 0.0578  -0.0069 65  GLY A C     
497  O O     . GLY A 65  ? 0.2042 0.1752 0.1632 -0.0201 0.0567  -0.0070 65  GLY A O     
498  N N     . ASP A 66  ? 0.1983 0.1583 0.1458 -0.0197 0.0619  -0.0067 66  ASP A N     
499  C CA    . ASP A 66  ? 0.2919 0.2458 0.2364 -0.0197 0.0654  -0.0065 66  ASP A CA    
500  C C     . ASP A 66  ? 0.6133 0.5663 0.5546 -0.0190 0.0648  -0.0055 66  ASP A C     
501  O O     . ASP A 66  ? 0.5868 0.5400 0.5304 -0.0192 0.0652  -0.0055 66  ASP A O     
502  C CB    . ASP A 66  ? 0.2096 0.1543 0.1464 -0.0194 0.0702  -0.0064 66  ASP A CB    
503  C CG    . ASP A 66  ? 0.1760 0.1207 0.1161 -0.0203 0.0716  -0.0075 66  ASP A CG    
504  O OD1   . ASP A 66  ? 0.3026 0.2529 0.2505 -0.0211 0.0699  -0.0084 66  ASP A OD1   
505  O OD2   . ASP A 66  ? 0.2894 0.2280 0.2237 -0.0200 0.0746  -0.0074 66  ASP A OD2   
506  N N     . ILE A 67  ? 0.5953 0.5468 0.5309 -0.0180 0.0638  -0.0046 67  ILE A N     
507  C CA    . ILE A 67  ? 0.3106 0.2607 0.2423 -0.0172 0.0631  -0.0035 67  ILE A CA    
508  C C     . ILE A 67  ? 0.2246 0.1832 0.1646 -0.0176 0.0593  -0.0036 67  ILE A C     
509  O O     . ILE A 67  ? 0.1857 0.1435 0.1256 -0.0174 0.0596  -0.0032 67  ILE A O     
510  C CB    . ILE A 67  ? 0.2438 0.1916 0.1681 -0.0160 0.0621  -0.0028 67  ILE A CB    
511  C CG1   . ILE A 67  ? 0.1757 0.1132 0.0899 -0.0151 0.0662  -0.0026 67  ILE A CG1   
512  C CG2   . ILE A 67  ? 0.4276 0.3756 0.3491 -0.0151 0.0603  -0.0018 67  ILE A CG2   
513  C CD1   . ILE A 67  ? 0.3043 0.2392 0.2109 -0.0139 0.0651  -0.0022 67  ILE A CD1   
514  N N     . ILE A 68  ? 0.1317 0.0982 0.0788 -0.0180 0.0558  -0.0042 68  ILE A N     
515  C CA    . ILE A 68  ? 0.1458 0.1199 0.1004 -0.0181 0.0521  -0.0041 68  ILE A CA    
516  C C     . ILE A 68  ? 0.2702 0.2446 0.2290 -0.0188 0.0531  -0.0048 68  ILE A C     
517  O O     . ILE A 68  ? 0.4398 0.4161 0.4007 -0.0186 0.0520  -0.0045 68  ILE A O     
518  C CB    . ILE A 68  ? 0.1190 0.1004 0.0794 -0.0182 0.0483  -0.0045 68  ILE A CB    
519  C CG1   . ILE A 68  ? 0.1100 0.0922 0.0669 -0.0174 0.0467  -0.0037 68  ILE A CG1   
520  C CG2   . ILE A 68  ? 0.1270 0.1154 0.0952 -0.0182 0.0449  -0.0047 68  ILE A CG2   
521  C CD1   . ILE A 68  ? 0.3077 0.2967 0.2703 -0.0173 0.0430  -0.0039 68  ILE A CD1   
522  N N     . CYS A 69  ? 0.4897 0.4617 0.4494 -0.0195 0.0554  -0.0058 69  CYS A N     
523  C CA    . CYS A 69  ? 0.3624 0.3339 0.3255 -0.0201 0.0568  -0.0066 69  CYS A CA    
524  C C     . CYS A 69  ? 0.1299 0.0950 0.0883 -0.0199 0.0603  -0.0061 69  CYS A C     
525  O O     . CYS A 69  ? 0.2074 0.1733 0.1687 -0.0202 0.0604  -0.0064 69  CYS A O     
526  C CB    . CYS A 69  ? 0.3711 0.3403 0.3349 -0.0207 0.0591  -0.0076 69  CYS A CB    
527  S SG    . CYS A 69  ? 0.3666 0.3429 0.3384 -0.0211 0.0559  -0.0088 69  CYS A SG    
528  N N     . ASN A 70  ? 0.1405 0.0985 0.0910 -0.0194 0.0633  -0.0054 70  ASN A N     
529  C CA    . ASN A 70  ? 0.2410 0.1918 0.1858 -0.0190 0.0668  -0.0047 70  ASN A CA    
530  C C     . ASN A 70  ? 0.4302 0.3837 0.3751 -0.0184 0.0644  -0.0039 70  ASN A C     
531  O O     . ASN A 70  ? 0.4274 0.3798 0.3735 -0.0185 0.0654  -0.0038 70  ASN A O     
532  C CB    . ASN A 70  ? 0.2842 0.2262 0.2195 -0.0182 0.0704  -0.0041 70  ASN A CB    
533  C CG    . ASN A 70  ? 0.5261 0.4641 0.4608 -0.0188 0.0736  -0.0049 70  ASN A CG    
534  O OD1   . ASN A 70  ? 0.6101 0.5513 0.5513 -0.0197 0.0735  -0.0060 70  ASN A OD1   
535  N ND2   . ASN A 70  ? 0.5185 0.4492 0.4450 -0.0180 0.0764  -0.0043 70  ASN A ND2   
536  N N     . TRP A 71  ? 0.5088 0.4663 0.4533 -0.0179 0.0611  -0.0032 71  TRP A N     
537  C CA    . TRP A 71  ? 0.2574 0.2174 0.2018 -0.0173 0.0588  -0.0022 71  TRP A CA    
538  C C     . TRP A 71  ? 0.2963 0.2626 0.2486 -0.0178 0.0564  -0.0027 71  TRP A C     
539  O O     . TRP A 71  ? 0.5857 0.5511 0.5376 -0.0176 0.0568  -0.0022 71  TRP A O     
540  C CB    . TRP A 71  ? 0.2020 0.1661 0.1457 -0.0167 0.0554  -0.0016 71  TRP A CB    
541  C CG    . TRP A 71  ? 0.2569 0.2241 0.2010 -0.0161 0.0527  -0.0006 71  TRP A CG    
542  C CD1   . TRP A 71  ? 0.3380 0.3134 0.2896 -0.0162 0.0489  -0.0006 71  TRP A CD1   
543  C CD2   . TRP A 71  ? 0.2566 0.2184 0.1931 -0.0151 0.0538  0.0005  71  TRP A CD2   
544  N NE1   . TRP A 71  ? 0.2941 0.2700 0.2437 -0.0155 0.0475  0.0005  71  TRP A NE1   
545  C CE2   . TRP A 71  ? 0.3161 0.2837 0.2563 -0.0148 0.0505  0.0011  71  TRP A CE2   
546  C CE3   . TRP A 71  ? 0.2571 0.2092 0.1833 -0.0142 0.0572  0.0010  71  TRP A CE3   
547  C CZ2   . TRP A 71  ? 0.4484 0.4127 0.3828 -0.0139 0.0504  0.0022  71  TRP A CZ2   
548  C CZ3   . TRP A 71  ? 0.3326 0.2810 0.2525 -0.0130 0.0571  0.0021  71  TRP A CZ3   
549  C CH2   . TRP A 71  ? 0.4120 0.3665 0.3361 -0.0130 0.0537  0.0027  71  TRP A CH2   
550  N N     . THR A 72  ? 0.2538 0.2265 0.2132 -0.0183 0.0540  -0.0036 72  THR A N     
551  C CA    . THR A 72  ? 0.2251 0.2034 0.1913 -0.0185 0.0515  -0.0040 72  THR A CA    
552  C C     . THR A 72  ? 0.3715 0.3461 0.3382 -0.0191 0.0545  -0.0047 72  THR A C     
553  O O     . THR A 72  ? 0.4638 0.4413 0.4341 -0.0190 0.0531  -0.0048 72  THR A O     
554  C CB    . THR A 72  ? 0.1006 0.0856 0.0730 -0.0186 0.0480  -0.0046 72  THR A CB    
555  O OG1   . THR A 72  ? 0.1713 0.1540 0.1437 -0.0192 0.0501  -0.0056 72  THR A OG1   
556  C CG2   . THR A 72  ? 0.4548 0.4440 0.4276 -0.0180 0.0448  -0.0039 72  THR A CG2   
557  N N     . LYS A 73  ? 0.3243 0.2922 0.2873 -0.0195 0.0587  -0.0052 73  LYS A N     
558  C CA    . LYS A 73  ? 0.3957 0.3594 0.3588 -0.0199 0.0620  -0.0058 73  LYS A CA    
559  C C     . LYS A 73  ? 0.3393 0.2967 0.2967 -0.0195 0.0649  -0.0049 73  LYS A C     
560  O O     . LYS A 73  ? 0.2321 0.1887 0.1911 -0.0196 0.0660  -0.0051 73  LYS A O     
561  C CB    . LYS A 73  ? 0.5628 0.5222 0.5250 -0.0206 0.0654  -0.0068 73  LYS A CB    
562  C CG    . LYS A 73  ? 0.4324 0.3897 0.3973 -0.0212 0.0679  -0.0078 73  LYS A CG    
563  C CD    . LYS A 73  ? 0.3118 0.2599 0.2708 -0.0210 0.0732  -0.0074 73  LYS A CD    
564  C CE    . LYS A 73  ? 0.2435 0.1901 0.2059 -0.0217 0.0756  -0.0085 73  LYS A CE    
565  N NZ    . LYS A 73  ? 0.2048 0.1592 0.1741 -0.0220 0.0714  -0.0092 73  LYS A NZ    
566  N N     . GLN A 74  ? 0.3767 0.3296 0.3272 -0.0187 0.0662  -0.0039 74  GLN A N     
567  C CA    . GLN A 74  ? 0.2447 0.1906 0.1886 -0.0180 0.0691  -0.0029 74  GLN A CA    
568  C C     . GLN A 74  ? 0.3688 0.3190 0.3146 -0.0176 0.0662  -0.0022 74  GLN A C     
569  O O     . GLN A 74  ? 0.5589 0.5050 0.5024 -0.0173 0.0683  -0.0018 74  GLN A O     
570  C CB    . GLN A 74  ? 0.2786 0.2179 0.2135 -0.0170 0.0710  -0.0019 74  GLN A CB    
571  C CG    . GLN A 74  ? 0.4838 0.4178 0.4114 -0.0158 0.0721  -0.0006 74  GLN A CG    
572  C CD    . GLN A 74  ? 0.5188 0.4480 0.4378 -0.0146 0.0723  0.0004  74  GLN A CD    
573  O OE1   . GLN A 74  ? 0.6084 0.5394 0.5249 -0.0138 0.0696  0.0012  74  GLN A OE1   
574  N NE2   . GLN A 74  ? 0.3945 0.3174 0.3085 -0.0143 0.0755  0.0002  74  GLN A NE2   
575  N N     . GLN A 75  ? 0.3857 0.3436 0.3355 -0.0175 0.0615  -0.0019 75  GLN A N     
576  C CA    . GLN A 75  ? 0.4078 0.3699 0.3592 -0.0171 0.0585  -0.0011 75  GLN A CA    
577  C C     . GLN A 75  ? 0.3302 0.2985 0.2894 -0.0175 0.0562  -0.0018 75  GLN A C     
578  O O     . GLN A 75  ? 0.4310 0.4000 0.3908 -0.0173 0.0557  -0.0013 75  GLN A O     
579  C CB    . GLN A 75  ? 0.4008 0.3678 0.3523 -0.0165 0.0547  -0.0004 75  GLN A CB    
580  C CG    . GLN A 75  ? 0.4008 0.3616 0.3436 -0.0158 0.0565  0.0005  75  GLN A CG    
581  C CD    . GLN A 75  ? 0.4510 0.4044 0.3863 -0.0149 0.0592  0.0014  75  GLN A CD    
582  O OE1   . GLN A 75  ? 0.5527 0.5077 0.4900 -0.0148 0.0584  0.0018  75  GLN A OE1   
583  N NE2   . GLN A 75  ? 0.4312 0.3760 0.3575 -0.0141 0.0623  0.0019  75  GLN A NE2   
584  N N     . TYR A 76  ? 0.1849 0.1573 0.1495 -0.0181 0.0549  -0.0028 76  TYR A N     
585  C CA    . TYR A 76  ? 0.2520 0.2304 0.2234 -0.0183 0.0522  -0.0034 76  TYR A CA    
586  C C     . TYR A 76  ? 0.4284 0.4051 0.4022 -0.0191 0.0543  -0.0049 76  TYR A C     
587  O O     . TYR A 76  ? 0.4145 0.3954 0.3933 -0.0192 0.0523  -0.0055 76  TYR A O     
588  C CB    . TYR A 76  ? 0.3457 0.3318 0.3216 -0.0179 0.0473  -0.0032 76  TYR A CB    
589  C CG    . TYR A 76  ? 0.3888 0.3765 0.3622 -0.0172 0.0454  -0.0020 76  TYR A CG    
590  C CD1   . TYR A 76  ? 0.3569 0.3467 0.3300 -0.0165 0.0436  -0.0009 76  TYR A CD1   
591  C CD2   . TYR A 76  ? 0.3964 0.3835 0.3679 -0.0172 0.0455  -0.0021 76  TYR A CD2   
592  C CE1   . TYR A 76  ? 0.2968 0.2879 0.2677 -0.0159 0.0418  0.0002  76  TYR A CE1   
593  C CE2   . TYR A 76  ? 0.3570 0.3454 0.3262 -0.0166 0.0438  -0.0010 76  TYR A CE2   
594  C CZ    . TYR A 76  ? 0.4483 0.4388 0.4173 -0.0159 0.0420  0.0001  76  TYR A CZ    
595  O OH    . TYR A 76  ? 0.6246 0.6162 0.5911 -0.0152 0.0403  0.0011  76  TYR A OH    
596  N N     . ASP A 77  ? 0.3631 0.3336 0.3335 -0.0196 0.0583  -0.0054 77  ASP A N     
597  C CA    . ASP A 77  ? 0.1628 0.1319 0.1359 -0.0203 0.0603  -0.0067 77  ASP A CA    
598  C C     . ASP A 77  ? 0.1840 0.1601 0.1627 -0.0204 0.0565  -0.0074 77  ASP A C     
599  O O     . ASP A 77  ? 0.1109 0.0901 0.0940 -0.0206 0.0552  -0.0082 77  ASP A O     
600  C CB    . ASP A 77  ? 0.4296 0.3962 0.4037 -0.0206 0.0626  -0.0072 77  ASP A CB    
601  C CG    . ASP A 77  ? 0.2585 0.2211 0.2335 -0.0214 0.0661  -0.0086 77  ASP A CG    
602  O OD1   . ASP A 77  ? 0.2392 0.1949 0.2098 -0.0215 0.0703  -0.0085 77  ASP A OD1   
603  O OD2   . ASP A 77  ? 0.2552 0.2213 0.2353 -0.0219 0.0649  -0.0096 77  ASP A OD2   
604  N N     . TRP A 78  ? 0.4458 0.4243 0.4240 -0.0202 0.0545  -0.0070 78  TRP A N     
605  C CA    . TRP A 78  ? 0.3662 0.3508 0.3490 -0.0200 0.0510  -0.0075 78  TRP A CA    
606  C C     . TRP A 78  ? 0.3140 0.2961 0.2955 -0.0205 0.0529  -0.0081 78  TRP A C     
607  O O     . TRP A 78  ? 0.1848 0.1647 0.1625 -0.0204 0.0537  -0.0076 78  TRP A O     
608  C CB    . TRP A 78  ? 0.4039 0.3939 0.3878 -0.0191 0.0468  -0.0064 78  TRP A CB    
609  C CG    . TRP A 78  ? 0.5340 0.5299 0.5225 -0.0187 0.0430  -0.0067 78  TRP A CG    
610  C CD1   . TRP A 78  ? 0.5103 0.5076 0.5020 -0.0190 0.0427  -0.0077 78  TRP A CD1   
611  C CD2   . TRP A 78  ? 0.3947 0.3956 0.3847 -0.0178 0.0391  -0.0058 78  TRP A CD2   
612  N NE1   . TRP A 78  ? 0.3890 0.3915 0.3838 -0.0182 0.0389  -0.0075 78  TRP A NE1   
613  C CE2   . TRP A 78  ? 0.4978 0.5024 0.4917 -0.0175 0.0367  -0.0063 78  TRP A CE2   
614  C CE3   . TRP A 78  ? 0.1868 0.1891 0.1753 -0.0172 0.0376  -0.0046 78  TRP A CE3   
615  C CZ2   . TRP A 78  ? 0.3659 0.3751 0.3619 -0.0165 0.0330  -0.0056 78  TRP A CZ2   
616  C CZ3   . TRP A 78  ? 0.3117 0.3187 0.3027 -0.0163 0.0339  -0.0040 78  TRP A CZ3   
617  C CH2   . TRP A 78  ? 0.4733 0.4835 0.4680 -0.0159 0.0317  -0.0045 78  TRP A CH2   
618  N N     . ASP A 79  ? 0.3540 0.3358 0.3382 -0.0211 0.0539  -0.0093 79  ASP A N     
619  C CA    . ASP A 79  ? 0.2422 0.2218 0.2257 -0.0216 0.0558  -0.0100 79  ASP A CA    
620  C C     . ASP A 79  ? 0.1616 0.1473 0.1485 -0.0212 0.0517  -0.0101 79  ASP A C     
621  O O     . ASP A 79  ? 0.0910 0.0809 0.0821 -0.0210 0.0493  -0.0106 79  ASP A O     
622  C CB    . ASP A 79  ? 0.2953 0.2716 0.2801 -0.0223 0.0589  -0.0113 79  ASP A CB    
623  C CG    . ASP A 79  ? 0.6161 0.5878 0.5991 -0.0226 0.0621  -0.0113 79  ASP A CG    
624  O OD1   . ASP A 79  ? 0.6997 0.6652 0.6777 -0.0226 0.0656  -0.0107 79  ASP A OD1   
625  O OD2   . ASP A 79  ? 0.6725 0.6462 0.6589 -0.0227 0.0613  -0.0119 79  ASP A OD2   
626  N N     . ILE A 80  ? 0.2299 0.2158 0.2148 -0.0210 0.0512  -0.0096 80  ILE A N     
627  C CA    . ILE A 80  ? 0.3772 0.3681 0.3649 -0.0205 0.0477  -0.0096 80  ILE A CA    
628  C C     . ILE A 80  ? 0.4023 0.3905 0.3886 -0.0211 0.0499  -0.0102 80  ILE A C     
629  O O     . ILE A 80  ? 0.5295 0.5118 0.5120 -0.0216 0.0539  -0.0104 80  ILE A O     
630  C CB    . ILE A 80  ? 0.2936 0.2877 0.2806 -0.0197 0.0448  -0.0084 80  ILE A CB    
631  C CG1   . ILE A 80  ? 0.1462 0.1360 0.1279 -0.0199 0.0472  -0.0079 80  ILE A CG1   
632  C CG2   . ILE A 80  ? 0.2658 0.2618 0.2537 -0.0192 0.0432  -0.0077 80  ILE A CG2   
633  C CD1   . ILE A 80  ? 0.1758 0.1688 0.1570 -0.0192 0.0444  -0.0070 80  ILE A CD1   
634  N N     . GLN A 81  ? 0.3240 0.3161 0.3131 -0.0208 0.0474  -0.0105 81  GLN A N     
635  C CA    . GLN A 81  ? 0.3082 0.2982 0.2962 -0.0213 0.0492  -0.0111 81  GLN A CA    
636  C C     . GLN A 81  ? 0.3773 0.3692 0.3641 -0.0209 0.0474  -0.0105 81  GLN A C     
637  O O     . GLN A 81  ? 0.3445 0.3406 0.3328 -0.0201 0.0440  -0.0097 81  GLN A O     
638  C CB    . GLN A 81  ? 0.2484 0.2404 0.2403 -0.0214 0.0485  -0.0121 81  GLN A CB    
639  C CG    . GLN A 81  ? 0.2637 0.2536 0.2567 -0.0219 0.0506  -0.0128 81  GLN A CG    
640  C CD    . GLN A 81  ? 0.2878 0.2708 0.2769 -0.0227 0.0555  -0.0131 81  GLN A CD    
641  O OE1   . GLN A 81  ? 0.2663 0.2459 0.2520 -0.0229 0.0575  -0.0129 81  GLN A OE1   
642  N NE2   . GLN A 81  ? 0.5219 0.5025 0.5112 -0.0230 0.0575  -0.0134 81  GLN A NE2   
643  N N     . LYS A 82  ? 0.3563 0.3446 0.3402 -0.0213 0.0498  -0.0107 82  LYS A N     
644  C CA    . LYS A 82  ? 0.2295 0.2185 0.2114 -0.0210 0.0487  -0.0102 82  LYS A CA    
645  C C     . LYS A 82  ? 0.3262 0.3214 0.3127 -0.0205 0.0447  -0.0103 82  LYS A C     
646  O O     . LYS A 82  ? 0.4395 0.4369 0.4256 -0.0200 0.0427  -0.0098 82  LYS A O     
647  C CB    . LYS A 82  ? 0.1358 0.1196 0.1137 -0.0216 0.0522  -0.0106 82  LYS A CB    
648  C CG    . LYS A 82  ? 0.2470 0.2243 0.2179 -0.0216 0.0557  -0.0099 82  LYS A CG    
649  C CD    . LYS A 82  ? 0.2902 0.2632 0.2561 -0.0216 0.0579  -0.0099 82  LYS A CD    
650  C CE    . LYS A 82  ? 0.4364 0.4014 0.3973 -0.0219 0.0629  -0.0100 82  LYS A CE    
651  N NZ    . LYS A 82  ? 0.4324 0.3920 0.3867 -0.0217 0.0653  -0.0097 82  LYS A NZ    
652  N N     . GLU A 83  ? 0.2820 0.2797 0.2726 -0.0204 0.0435  -0.0110 83  GLU A N     
653  C CA    . GLU A 83  ? 0.3467 0.3494 0.3411 -0.0197 0.0400  -0.0110 83  GLU A CA    
654  C C     . GLU A 83  ? 0.4633 0.4701 0.4595 -0.0187 0.0364  -0.0101 83  GLU A C     
655  O O     . GLU A 83  ? 0.4499 0.4603 0.4485 -0.0179 0.0335  -0.0098 83  GLU A O     
656  C CB    . GLU A 83  ? 0.3071 0.3104 0.3043 -0.0198 0.0401  -0.0118 83  GLU A CB    
657  C CG    . GLU A 83  ? 0.4243 0.4232 0.4199 -0.0208 0.0439  -0.0128 83  GLU A CG    
658  C CD    . GLU A 83  ? 0.4320 0.4267 0.4259 -0.0215 0.0472  -0.0131 83  GLU A CD    
659  O OE1   . GLU A 83  ? 0.3838 0.3734 0.3738 -0.0222 0.0506  -0.0132 83  GLU A OE1   
660  O OE2   . GLU A 83  ? 0.4877 0.4838 0.4839 -0.0214 0.0464  -0.0133 83  GLU A OE2   
661  N N     . TRP A 84  ? 0.1647 0.1708 0.1599 -0.0186 0.0367  -0.0095 84  TRP A N     
662  C CA    . TRP A 84  ? 0.1949 0.2046 0.1918 -0.0176 0.0335  -0.0086 84  TRP A CA    
663  C C     . TRP A 84  ? 0.3168 0.3275 0.3122 -0.0172 0.0322  -0.0077 84  TRP A C     
664  O O     . TRP A 84  ? 0.2695 0.2835 0.2667 -0.0162 0.0291  -0.0069 84  TRP A O     
665  C CB    . TRP A 84  ? 0.3166 0.3250 0.3132 -0.0178 0.0345  -0.0085 84  TRP A CB    
666  C CG    . TRP A 84  ? 0.4411 0.4491 0.4397 -0.0181 0.0354  -0.0093 84  TRP A CG    
667  C CD1   . TRP A 84  ? 0.4335 0.4423 0.4339 -0.0181 0.0352  -0.0100 84  TRP A CD1   
668  C CD2   . TRP A 84  ? 0.3908 0.3973 0.3895 -0.0184 0.0368  -0.0096 84  TRP A CD2   
669  N NE1   . TRP A 84  ? 0.3734 0.3814 0.3751 -0.0184 0.0362  -0.0107 84  TRP A NE1   
670  C CE2   . TRP A 84  ? 0.3533 0.3600 0.3541 -0.0187 0.0372  -0.0105 84  TRP A CE2   
671  C CE3   . TRP A 84  ? 0.3081 0.3132 0.3054 -0.0185 0.0377  -0.0092 84  TRP A CE3   
672  C CZ2   . TRP A 84  ? 0.2482 0.2537 0.2499 -0.0190 0.0386  -0.0111 84  TRP A CZ2   
673  C CZ3   . TRP A 84  ? 0.3470 0.3508 0.3451 -0.0189 0.0390  -0.0098 84  TRP A CZ3   
674  C CH2   . TRP A 84  ? 0.2941 0.2982 0.2945 -0.0192 0.0395  -0.0108 84  TRP A CH2   
675  N N     . ILE A 85  ? 0.3158 0.3233 0.3075 -0.0179 0.0345  -0.0077 85  ILE A N     
676  C CA    . ILE A 85  ? 0.1083 0.1163 0.0979 -0.0175 0.0337  -0.0068 85  ILE A CA    
677  C C     . ILE A 85  ? 0.2439 0.2551 0.2356 -0.0170 0.0311  -0.0068 85  ILE A C     
678  O O     . ILE A 85  ? 0.1501 0.1608 0.1420 -0.0174 0.0318  -0.0076 85  ILE A O     
679  C CB    . ILE A 85  ? 0.0758 0.0785 0.0597 -0.0181 0.0373  -0.0068 85  ILE A CB    
680  C CG1   . ILE A 85  ? 0.1370 0.1354 0.1187 -0.0187 0.0404  -0.0070 85  ILE A CG1   
681  C CG2   . ILE A 85  ? 0.0907 0.0937 0.0717 -0.0176 0.0364  -0.0057 85  ILE A CG2   
682  C CD1   . ILE A 85  ? 0.2506 0.2425 0.2262 -0.0193 0.0445  -0.0072 85  ILE A CD1   
683  N N     . VAL A 86  ? 0.4045 0.4190 0.3978 -0.0161 0.0281  -0.0060 86  VAL A N     
684  C CA    . VAL A 86  ? 0.1132 0.1302 0.1080 -0.0156 0.0256  -0.0060 86  VAL A CA    
685  C C     . VAL A 86  ? 0.3095 0.3262 0.3017 -0.0155 0.0255  -0.0052 86  VAL A C     
686  O O     . VAL A 86  ? 0.5927 0.6086 0.5835 -0.0153 0.0258  -0.0044 86  VAL A O     
687  C CB    . VAL A 86  ? 0.1170 0.1375 0.1157 -0.0145 0.0222  -0.0057 86  VAL A CB    
688  C CG1   . VAL A 86  ? 0.2390 0.2617 0.2388 -0.0141 0.0198  -0.0056 86  VAL A CG1   
689  C CG2   . VAL A 86  ? 0.2188 0.2394 0.2194 -0.0145 0.0225  -0.0063 86  VAL A CG2   
690  N N     . PHE A 87  ? 0.2490 0.2659 0.2402 -0.0156 0.0252  -0.0054 87  PHE A N     
691  C CA    . PHE A 87  ? 0.0541 0.0706 0.0424 -0.0154 0.0249  -0.0047 87  PHE A CA    
692  C C     . PHE A 87  ? 0.3261 0.3466 0.3181 -0.0148 0.0211  -0.0045 87  PHE A C     
693  O O     . PHE A 87  ? 0.2138 0.2369 0.2094 -0.0145 0.0189  -0.0051 87  PHE A O     
694  C CB    . PHE A 87  ? 0.1738 0.1875 0.1577 -0.0157 0.0271  -0.0050 87  PHE A CB    
695  C CG    . PHE A 87  ? 0.3705 0.3790 0.3488 -0.0162 0.0310  -0.0049 87  PHE A CG    
696  C CD1   . PHE A 87  ? 0.4694 0.4741 0.4415 -0.0158 0.0327  -0.0040 87  PHE A CD1   
697  C CD2   . PHE A 87  ? 0.2917 0.2985 0.2704 -0.0169 0.0330  -0.0059 87  PHE A CD2   
698  C CE1   . PHE A 87  ? 0.4061 0.4050 0.3724 -0.0161 0.0363  -0.0042 87  PHE A CE1   
699  C CE2   . PHE A 87  ? 0.1742 0.1755 0.1476 -0.0173 0.0366  -0.0060 87  PHE A CE2   
700  C CZ    . PHE A 87  ? 0.1879 0.1850 0.1550 -0.0169 0.0383  -0.0051 87  PHE A CZ    
701  N N     . SER A 88  ? 0.3704 0.3912 0.3610 -0.0145 0.0202  -0.0037 88  SER A N     
702  C CA    . SER A 88  ? 0.1760 0.2003 0.1693 -0.0141 0.0166  -0.0036 88  SER A CA    
703  C C     . SER A 88  ? 0.3231 0.3463 0.3128 -0.0142 0.0170  -0.0029 88  SER A C     
704  O O     . SER A 88  ? 0.5687 0.5879 0.5532 -0.0139 0.0198  -0.0021 88  SER A O     
705  C CB    . SER A 88  ? 0.0477 0.0739 0.0436 -0.0134 0.0143  -0.0030 88  SER A CB    
706  O OG    . SER A 88  ? 0.1891 0.2186 0.1874 -0.0127 0.0105  -0.0030 88  SER A OG    
707  N N     . ALA A 89  ? 0.1954 0.2218 0.1871 -0.0142 0.0141  -0.0032 89  ALA A N     
708  C CA    . ALA A 89  ? 0.2797 0.3049 0.2676 -0.0141 0.0143  -0.0025 89  ALA A CA    
709  C C     . ALA A 89  ? 0.3982 0.4243 0.3864 -0.0137 0.0128  -0.0014 89  ALA A C     
710  O O     . ALA A 89  ? 0.4786 0.5031 0.4629 -0.0134 0.0128  -0.0007 89  ALA A O     
711  C CB    . ALA A 89  ? 0.1307 0.1594 0.1207 -0.0143 0.0118  -0.0032 89  ALA A CB    
712  N N     . GLY A 90  ? 0.3885 0.4162 0.3800 -0.0136 0.0116  -0.0013 90  GLY A N     
713  C CA    . GLY A 90  ? 0.2846 0.3134 0.2767 -0.0132 0.0100  -0.0004 90  GLY A CA    
714  C C     . GLY A 90  ? 0.2224 0.2535 0.2179 -0.0125 0.0079  -0.0004 90  GLY A C     
715  O O     . GLY A 90  ? 0.3812 0.4131 0.3783 -0.0122 0.0071  -0.0010 90  GLY A O     
716  N N     . ILE A 91  ? 0.0326 0.0639 0.0283 -0.0121 0.0072  0.0003  91  ILE A N     
717  C CA    . ILE A 91  ? 0.0233 0.0557 0.0208 -0.0112 0.0055  0.0006  91  ILE A CA    
718  C C     . ILE A 91  ? 0.0646 0.1001 0.0630 -0.0097 0.0013  0.0016  91  ILE A C     
719  O O     . ILE A 91  ? 0.2914 0.3267 0.2901 -0.0087 0.0005  0.0019  91  ILE A O     
720  C CB    . ILE A 91  ? 0.1900 0.2210 0.1870 -0.0112 0.0067  0.0011  91  ILE A CB    
721  C CG1   . ILE A 91  ? 0.2862 0.3124 0.2801 -0.0120 0.0117  0.0009  91  ILE A CG1   
722  C CG2   . ILE A 91  ? 0.2630 0.2947 0.2615 -0.0103 0.0055  0.0013  91  ILE A CG2   
723  C CD1   . ILE A 91  ? 0.2748 0.2986 0.2678 -0.0118 0.0140  0.0013  91  ILE A CD1   
724  N N     . VAL A 92  ? 0.0945 0.1311 0.0925 -0.0091 -0.0006 0.0024  92  VAL A N     
725  C CA    . VAL A 92  ? 0.0141 0.0460 0.0127 -0.0064 -0.0013 0.0038  92  VAL A CA    
726  C C     . VAL A 92  ? 0.3363 0.3686 0.3350 -0.0063 -0.0011 0.0035  92  VAL A C     
727  O O     . VAL A 92  ? 0.0129 0.0431 0.0120 -0.0050 -0.0012 0.0044  92  VAL A O     
728  C CB    . VAL A 92  ? 0.1549 0.1843 0.1536 -0.0056 -0.0017 0.0044  92  VAL A CB    
729  C CG1   . VAL A 92  ? 0.1484 0.1763 0.1513 -0.0045 -0.0008 0.0054  92  VAL A CG1   
730  C CG2   . VAL A 92  ? 0.3328 0.3627 0.3316 -0.0060 -0.0019 0.0045  92  VAL A CG2   
731  N N     . PRO A 93  ? 0.0150 0.0501 0.0132 -0.0079 -0.0007 0.0022  93  PRO A N     
732  C CA    . PRO A 93  ? 0.0832 0.1192 0.0816 -0.0080 -0.0003 0.0016  93  PRO A CA    
733  C C     . PRO A 93  ? 0.2671 0.3018 0.2665 -0.0080 0.0009  0.0011  93  PRO A C     
734  O O     . PRO A 93  ? 0.2616 0.2955 0.2617 -0.0070 0.0008  0.0018  93  PRO A O     
735  C CB    . PRO A 93  ? 0.1355 0.1717 0.1343 -0.0096 0.0013  -0.0002 93  PRO A CB    
736  C CG    . PRO A 93  ? 0.0590 0.0967 0.0566 -0.0101 0.0002  0.0001  93  PRO A CG    
737  C CD    . PRO A 93  ? 0.0164 0.0534 0.0140 -0.0095 -0.0004 0.0012  93  PRO A CD    
738  N N     . ALA A 94  ? 0.2177 0.2519 0.2174 -0.0090 0.0023  0.0003  94  ALA A N     
739  C CA    . ALA A 94  ? 0.0758 0.1085 0.0763 -0.0090 0.0038  -0.0001 94  ALA A CA    
740  C C     . ALA A 94  ? 0.2639 0.2969 0.2643 -0.0076 0.0020  0.0013  94  ALA A C     
741  O O     . ALA A 94  ? 0.2663 0.2984 0.2674 -0.0071 0.0024  0.0013  94  ALA A O     
742  C CB    . ALA A 94  ? 0.1374 0.1686 0.1378 -0.0103 0.0067  -0.0010 94  ALA A CB    
743  N N     . LEU A 95  ? 0.2347 0.2687 0.2340 -0.0068 -0.0001 0.0027  95  LEU A N     
744  C CA    . LEU A 95  ? 0.1187 0.1501 0.1183 -0.0050 -0.0009 0.0042  95  LEU A CA    
745  C C     . LEU A 95  ? 0.1774 0.2066 0.1774 -0.0037 -0.0010 0.0052  95  LEU A C     
746  O O     . LEU A 95  ? 0.1556 0.1833 0.1559 -0.0029 -0.0010 0.0058  95  LEU A O     
747  C CB    . LEU A 95  ? 0.2654 0.2938 0.2650 -0.0040 -0.0013 0.0049  95  LEU A CB    
748  C CG    . LEU A 95  ? 0.3481 0.3784 0.3476 -0.0050 -0.0012 0.0045  95  LEU A CG    
749  C CD1   . LEU A 95  ? 0.0120 0.0384 0.0116 -0.0037 -0.0017 0.0052  95  LEU A CD1   
750  C CD2   . LEU A 95  ? 0.0436 0.0760 0.0430 -0.0057 -0.0009 0.0042  95  LEU A CD2   
751  N N     . SER A 96  ? 0.4776 0.5068 0.4776 -0.0037 -0.0010 0.0053  96  SER A N     
752  C CA    . SER A 96  ? 0.3592 0.3872 0.3597 -0.0029 -0.0010 0.0064  96  SER A CA    
753  C C     . SER A 96  ? 0.0113 0.0421 0.0121 -0.0034 -0.0007 0.0061  96  SER A C     
754  O O     . SER A 96  ? 0.3358 0.3653 0.3373 -0.0024 -0.0006 0.0073  96  SER A O     
755  C CB    . SER A 96  ? 0.4444 0.4729 0.4451 -0.0031 -0.0010 0.0067  96  SER A CB    
756  O OG    . SER A 96  ? 0.4639 0.4922 0.4658 -0.0024 -0.0008 0.0083  96  SER A OG    
757  N N     . THR A 97  ? 0.1115 0.1433 0.1129 -0.0048 0.0005  0.0038  97  THR A N     
758  C CA    . THR A 97  ? 0.0135 0.0446 0.0166 -0.0052 0.0021  0.0026  97  THR A CA    
759  C C     . THR A 97  ? 0.0761 0.1065 0.0793 -0.0047 0.0021  0.0031  97  THR A C     
760  O O     . THR A 97  ? 0.3310 0.3607 0.3354 -0.0042 0.0026  0.0034  97  THR A O     
761  C CB    . THR A 97  ? 0.0158 0.0471 0.0192 -0.0069 0.0039  0.0005  97  THR A CB    
762  O OG1   . THR A 97  ? 0.0161 0.0483 0.0190 -0.0074 0.0037  0.0000  97  THR A OG1   
763  C CG2   . THR A 97  ? 0.3452 0.3757 0.3503 -0.0072 0.0057  -0.0005 97  THR A CG2   
764  N N     . SER A 98  ? 0.1040 0.1348 0.1062 -0.0049 0.0016  0.0031  98  SER A N     
765  C CA    . SER A 98  ? 0.0225 0.0529 0.0249 -0.0045 0.0017  0.0034  98  SER A CA    
766  C C     . SER A 98  ? 0.0112 0.0410 0.0130 -0.0029 0.0001  0.0057  98  SER A C     
767  O O     . SER A 98  ? 0.2581 0.2873 0.2606 -0.0025 0.0005  0.0060  98  SER A O     
768  C CB    . SER A 98  ? 0.0134 0.0442 0.0153 -0.0051 0.0017  0.0029  98  SER A CB    
769  O OG    . SER A 98  ? 0.1280 0.1589 0.1302 -0.0066 0.0033  0.0014  98  SER A OG    
770  N N     . ILE A 99  ? 0.4206 0.4483 0.4219 -0.0019 -0.0007 0.0069  99  ILE A N     
771  C CA    . ILE A 99  ? 0.1448 0.1686 0.1467 -0.0007 -0.0007 0.0080  99  ILE A CA    
772  C C     . ILE A 99  ? 0.0101 0.0348 0.0128 -0.0004 -0.0004 0.0090  99  ILE A C     
773  O O     . ILE A 99  ? 0.0100 0.0330 0.0133 0.0003  -0.0003 0.0096  99  ILE A O     
774  C CB    . ILE A 99  ? 0.0772 0.0978 0.0789 -0.0003 -0.0009 0.0081  99  ILE A CB    
775  C CG1   . ILE A 99  ? 0.1208 0.1432 0.1253 -0.0008 -0.0003 0.0071  99  ILE A CG1   
776  C CG2   . ILE A 99  ? 0.2680 0.2888 0.2739 0.0001  0.0000  0.0085  99  ILE A CG2   
777  C CD1   . ILE A 99  ? 0.2090 0.2316 0.2137 -0.0010 -0.0004 0.0073  99  ILE A CD1   
778  N N     . GLN A 100 ? 0.2400 0.2676 0.2430 -0.0009 -0.0003 0.0091  100 GLN A N     
779  C CA    . GLN A 100 ? 0.3060 0.3327 0.3111 -0.0007 0.0007  0.0091  100 GLN A CA    
780  C C     . GLN A 100 ? 0.0111 0.0380 0.0174 -0.0012 0.0019  0.0076  100 GLN A C     
781  O O     . GLN A 100 ? 0.0111 0.0370 0.0186 -0.0006 0.0022  0.0085  100 GLN A O     
782  C CB    . GLN A 100 ? 0.2541 0.2810 0.2607 -0.0013 0.0016  0.0081  100 GLN A CB    
783  C CG    . GLN A 100 ? 0.0108 0.0376 0.0169 -0.0011 0.0009  0.0092  100 GLN A CG    
784  C CD    . GLN A 100 ? 0.2228 0.2500 0.2311 -0.0019 0.0021  0.0076  100 GLN A CD    
785  O OE1   . GLN A 100 ? 0.0119 0.0405 0.0193 -0.0029 0.0022  0.0061  100 GLN A OE1   
786  N NE2   . GLN A 100 ? 0.0115 0.0377 0.0229 -0.0016 0.0029  0.0080  100 GLN A NE2   
787  N N     . ALA A 101 ? 0.2950 0.3228 0.3011 -0.0023 0.0026  0.0056  101 ALA A N     
788  C CA    . ALA A 101 ? 0.2009 0.2285 0.2084 -0.0029 0.0041  0.0043  101 ALA A CA    
789  C C     . ALA A 101 ? 0.0924 0.1197 0.0993 -0.0021 0.0033  0.0054  101 ALA A C     
790  O O     . ALA A 101 ? 0.0535 0.0804 0.0615 -0.0018 0.0039  0.0057  101 ALA A O     
791  C CB    . ALA A 101 ? 0.0144 0.0425 0.0221 -0.0043 0.0055  0.0022  101 ALA A CB    
792  N N     . PHE A 102 ? 0.1577 0.1854 0.1629 -0.0017 0.0020  0.0063  102 PHE A N     
793  C CA    . PHE A 102 ? 0.0113 0.0390 0.0159 -0.0014 0.0017  0.0067  102 PHE A CA    
794  C C     . PHE A 102 ? 0.0101 0.0370 0.0134 0.0002  0.0001  0.0095  102 PHE A C     
795  O O     . PHE A 102 ? 0.2827 0.3087 0.2859 0.0004  0.0000  0.0094  102 PHE A O     
796  C CB    . PHE A 102 ? 0.0118 0.0402 0.0159 -0.0023 0.0019  0.0054  102 PHE A CB    
797  C CG    . PHE A 102 ? 0.0516 0.0801 0.0569 -0.0038 0.0038  0.0032  102 PHE A CG    
798  C CD1   . PHE A 102 ? 0.0149 0.0430 0.0220 -0.0045 0.0058  0.0020  102 PHE A CD1   
799  C CD2   . PHE A 102 ? 0.0139 0.0429 0.0186 -0.0045 0.0038  0.0026  102 PHE A CD2   
800  C CE1   . PHE A 102 ? 0.0169 0.0448 0.0247 -0.0057 0.0076  0.0005  102 PHE A CE1   
801  C CE2   . PHE A 102 ? 0.0669 0.0957 0.0724 -0.0058 0.0057  0.0010  102 PHE A CE2   
802  C CZ    . PHE A 102 ? 0.0994 0.1275 0.1063 -0.0064 0.0076  0.0000  102 PHE A CZ    
803  N N     . THR A 103 ? 0.0938 0.1177 0.0975 0.0007  0.0001  0.0100  103 THR A N     
804  C CA    . THR A 103 ? 0.0101 0.0298 0.0139 0.0014  0.0001  0.0102  103 THR A CA    
805  C C     . THR A 103 ? 0.0103 0.0295 0.0154 0.0018  0.0004  0.0112  103 THR A C     
806  O O     . THR A 103 ? 0.0104 0.0318 0.0163 0.0017  0.0006  0.0120  103 THR A O     
807  C CB    . THR A 103 ? 0.1009 0.1183 0.1038 0.0010  0.0005  0.0099  103 THR A CB    
808  O OG1   . THR A 103 ? 0.0633 0.0833 0.0698 0.0009  0.0004  0.0090  103 THR A OG1   
809  C CG2   . THR A 103 ? 0.0102 0.0283 0.0124 0.0007  0.0003  0.0093  103 THR A CG2   
810  N N     . LYS A 104 ? 0.0701 0.0864 0.0749 0.0017  0.0011  0.0114  104 LYS A N     
811  C CA    . LYS A 104 ? 0.2551 0.2733 0.2650 0.0022  0.0016  0.0114  104 LYS A CA    
812  C C     . LYS A 104 ? 0.1339 0.1520 0.1447 0.0022  0.0016  0.0119  104 LYS A C     
813  O O     . LYS A 104 ? 0.3395 0.3549 0.3460 0.0019  0.0013  0.0127  104 LYS A O     
814  C CB    . LYS A 104 ? 0.3827 0.3978 0.3898 0.0024  0.0018  0.0131  104 LYS A CB    
815  C CG    . LYS A 104 ? 0.2147 0.2315 0.2223 0.0030  0.0014  0.0132  104 LYS A CG    
816  C CD    . LYS A 104 ? 0.1567 0.1725 0.1641 0.0032  0.0014  0.0133  104 LYS A CD    
817  C CE    . LYS A 104 ? 0.3615 0.3800 0.3702 0.0035  0.0020  0.0144  104 LYS A CE    
818  N NZ    . LYS A 104 ? 0.3038 0.3258 0.3121 0.0033  0.0019  0.0144  104 LYS A NZ    
819  N N     . GLU A 105 ? 0.0403 0.0545 0.0490 0.0022  0.0018  0.0139  105 GLU A N     
820  C CA    . GLU A 105 ? 0.2679 0.2854 0.2816 0.0023  0.0020  0.0133  105 GLU A CA    
821  C C     . GLU A 105 ? 0.4155 0.4333 0.4295 0.0024  0.0021  0.0136  105 GLU A C     
822  O O     . GLU A 105 ? 0.4755 0.4936 0.4899 0.0027  0.0024  0.0139  105 GLU A O     
823  C CB    . GLU A 105 ? 0.1373 0.1541 0.1533 0.0025  0.0024  0.0142  105 GLU A CB    
824  C CG    . GLU A 105 ? 0.0778 0.0904 0.0901 0.0021  0.0021  0.0153  105 GLU A CG    
825  C CD    . GLU A 105 ? 0.2265 0.2380 0.2416 0.0022  0.0024  0.0163  105 GLU A CD    
826  O OE1   . GLU A 105 ? 0.2946 0.3060 0.3110 0.0025  0.0020  0.0164  105 GLU A OE1   
827  O OE2   . GLU A 105 ? 0.3109 0.3267 0.3320 0.0026  0.0030  0.0157  105 GLU A OE2   
828  N N     . ASN A 106 ? 0.4376 0.4520 0.4477 0.0021  0.0018  0.0149  106 ASN A N     
829  C CA    . ASN A 106 ? 0.2322 0.2469 0.2425 0.0021  0.0018  0.0152  106 ASN A CA    
830  C C     . ASN A 106 ? 0.1179 0.1366 0.1307 0.0023  0.0019  0.0132  106 ASN A C     
831  O O     . ASN A 106 ? 0.0130 0.0285 0.0221 0.0022  0.0018  0.0148  106 ASN A O     
832  C CB    . ASN A 106 ? 0.2783 0.2967 0.2948 0.0026  0.0025  0.0151  106 ASN A CB    
833  C CG    . ASN A 106 ? 0.3344 0.3482 0.3487 0.0023  0.0024  0.0174  106 ASN A CG    
834  O OD1   . ASN A 106 ? 0.3065 0.3197 0.3221 0.0024  0.0026  0.0178  106 ASN A OD1   
835  N ND2   . ASN A 106 ? 0.0640 0.0779 0.0789 0.0022  0.0023  0.0177  106 ASN A ND2   
836  N N     . GLU A 107 ? 0.1931 0.2086 0.2006 0.0020  0.0015  0.0135  107 GLU A N     
837  C CA    . GLU A 107 ? 0.3251 0.3441 0.3352 0.0021  0.0014  0.0117  107 GLU A CA    
838  C C     . GLU A 107 ? 0.2939 0.3101 0.2995 0.0016  0.0011  0.0122  107 GLU A C     
839  O O     . GLU A 107 ? 0.4749 0.4911 0.4807 0.0015  0.0010  0.0122  107 GLU A O     
840  C CB    . GLU A 107 ? 0.1348 0.1540 0.1441 0.0020  0.0013  0.0111  107 GLU A CB    
841  C CG    . GLU A 107 ? 0.1825 0.2016 0.1923 0.0024  0.0016  0.0116  107 GLU A CG    
842  C CD    . GLU A 107 ? 0.3324 0.3516 0.3415 0.0023  0.0015  0.0111  107 GLU A CD    
843  O OE1   . GLU A 107 ? 0.2772 0.2966 0.2855 0.0020  0.0012  0.0105  107 GLU A OE1   
844  O OE2   . GLU A 107 ? 0.4153 0.4316 0.4209 0.0023  0.0016  0.0125  107 GLU A OE2   
845  N N     . SER A 108 ? 0.2066 0.2260 0.2153 0.0017  0.0010  0.0107  108 SER A N     
846  C CA    . SER A 108 ? 0.0411 0.0579 0.0455 0.0013  0.0008  0.0114  108 SER A CA    
847  C C     . SER A 108 ? 0.0105 0.0278 0.0140 0.0010  0.0006  0.0105  108 SER A C     
848  O O     . SER A 108 ? 0.5042 0.5218 0.5071 0.0010  0.0005  0.0100  108 SER A O     
849  C CB    . SER A 108 ? 0.1361 0.1531 0.1405 0.0014  0.0008  0.0114  108 SER A CB    
850  O OG    . SER A 108 ? 0.2963 0.3130 0.3016 0.0017  0.0011  0.0122  108 SER A OG    
851  N N     . VAL A 109 ? 0.0105 0.0279 0.0138 0.0008  0.0004  0.0103  109 VAL A N     
852  C CA    . VAL A 109 ? 0.0770 0.0975 0.0832 0.0005  0.0003  0.0087  109 VAL A CA    
853  C C     . VAL A 109 ? 0.1300 0.1481 0.1325 0.0004  0.0002  0.0095  109 VAL A C     
854  O O     . VAL A 109 ? 0.0104 0.0282 0.0135 0.0005  0.0003  0.0101  109 VAL A O     
855  C CB    . VAL A 109 ? 0.0480 0.0686 0.0539 0.0003  0.0002  0.0086  109 VAL A CB    
856  C CG1   . VAL A 109 ? 0.0102 0.0293 0.0116 -0.0001 -0.0001 0.0085  109 VAL A CG1   
857  C CG2   . VAL A 109 ? 0.0102 0.0283 0.0126 0.0004  0.0002  0.0094  109 VAL A CG2   
858  N N     . LEU A 110 ? 0.1219 0.1405 0.1238 0.0002  0.0001  0.0090  110 LEU A N     
859  C CA    . LEU A 110 ? 0.0666 0.0875 0.0722 0.0001  0.0001  0.0082  110 LEU A CA    
860  C C     . LEU A 110 ? 0.1165 0.1380 0.1217 -0.0003 -0.0001 0.0079  110 LEU A C     
861  O O     . LEU A 110 ? 0.1094 0.1292 0.1102 -0.0005 -0.0002 0.0080  110 LEU A O     
862  C CB    . LEU A 110 ? 0.1526 0.1712 0.1543 0.0002  0.0001  0.0088  110 LEU A CB    
863  C CG    . LEU A 110 ? 0.3469 0.3680 0.3524 0.0001  0.0001  0.0081  110 LEU A CG    
864  C CD1   . LEU A 110 ? 0.1923 0.2106 0.1943 0.0004  0.0002  0.0091  110 LEU A CD1   
865  C CD2   . LEU A 110 ? 0.3178 0.3395 0.3227 -0.0002 -0.0001 0.0074  110 LEU A CD2   
866  N N     . VAL A 111 ? 0.0104 0.0296 0.0121 -0.0002 -0.0001 0.0089  111 VAL A N     
867  C CA    . VAL A 111 ? 0.1762 0.1984 0.1814 -0.0006 -0.0002 0.0079  111 VAL A CA    
868  C C     . VAL A 111 ? 0.0106 0.0304 0.0121 -0.0005 -0.0002 0.0088  111 VAL A C     
869  O O     . VAL A 111 ? 0.0105 0.0297 0.0124 -0.0002 -0.0001 0.0092  111 VAL A O     
870  C CB    . VAL A 111 ? 0.2809 0.3033 0.2864 -0.0007 -0.0003 0.0082  111 VAL A CB    
871  C CG1   . VAL A 111 ? 0.1057 0.1281 0.1109 -0.0008 -0.0003 0.0080  111 VAL A CG1   
872  C CG2   . VAL A 111 ? 0.1455 0.1672 0.1517 -0.0004 -0.0002 0.0090  111 VAL A CG2   
873  N N     . GLN A 112 ? 0.1829 0.2033 0.1840 -0.0008 -0.0003 0.0086  112 GLN A N     
874  C CA    . GLN A 112 ? 0.3432 0.3636 0.3444 -0.0008 -0.0003 0.0088  112 GLN A CA    
875  C C     . GLN A 112 ? 0.1488 0.1695 0.1501 -0.0009 -0.0004 0.0091  112 GLN A C     
876  O O     . GLN A 112 ? 0.0737 0.0977 0.0788 -0.0014 -0.0005 0.0080  112 GLN A O     
877  C CB    . GLN A 112 ? 0.3606 0.3839 0.3653 -0.0011 -0.0004 0.0075  112 GLN A CB    
878  C CG    . GLN A 112 ? 0.0812 0.1021 0.0816 -0.0010 -0.0003 0.0077  112 GLN A CG    
879  C CD    . GLN A 112 ? 0.0109 0.0323 0.0108 -0.0014 -0.0004 0.0071  112 GLN A CD    
880  O OE1   . GLN A 112 ? 0.0106 0.0344 0.0114 -0.0018 -0.0015 0.0065  112 GLN A OE1   
881  N NE2   . GLN A 112 ? 0.1159 0.1393 0.1200 -0.0013 -0.0004 0.0065  112 GLN A NE2   
882  N N     . PRO A 113 ? 0.1802 0.2030 0.1862 -0.0008 -0.0003 0.0089  113 PRO A N     
883  C CA    . PRO A 113 ? 0.3362 0.3595 0.3425 -0.0010 -0.0004 0.0092  113 PRO A CA    
884  C C     . PRO A 113 ? 0.4058 0.4294 0.4120 -0.0011 -0.0005 0.0092  113 PRO A C     
885  O O     . PRO A 113 ? 0.3573 0.3779 0.3593 -0.0008 -0.0004 0.0099  113 PRO A O     
886  C CB    . PRO A 113 ? 0.3173 0.3400 0.3243 -0.0008 -0.0004 0.0099  113 PRO A CB    
887  C CG    . PRO A 113 ? 0.3044 0.3238 0.3075 -0.0004 -0.0002 0.0107  113 PRO A CG    
888  C CD    . PRO A 113 ? 0.0761 0.0956 0.0786 -0.0004 -0.0002 0.0101  113 PRO A CD    
889  N N     . PRO A 114 ? 0.4141 0.4384 0.4204 -0.0014 -0.0006 0.0094  114 PRO A N     
890  C CA    . PRO A 114 ? 0.3431 0.3651 0.3449 -0.0015 -0.0006 0.0104  114 PRO A CA    
891  C C     . PRO A 114 ? 0.2609 0.2837 0.2622 -0.0018 -0.0007 0.0098  114 PRO A C     
892  O O     . PRO A 114 ? 0.1827 0.2060 0.1834 -0.0021 -0.0008 0.0094  114 PRO A O     
893  C CB    . PRO A 114 ? 0.2379 0.2606 0.2399 -0.0018 -0.0007 0.0108  114 PRO A CB    
894  C CG    . PRO A 114 ? 0.1153 0.1408 0.1216 -0.0018 -0.0008 0.0096  114 PRO A CG    
895  C CD    . PRO A 114 ? 0.2204 0.2422 0.2224 -0.0013 -0.0005 0.0104  114 PRO A CD    
896  N N     . ILE A 115 ? 0.0099 0.0353 0.0157 -0.0021 -0.0008 0.0090  115 ILE A N     
897  C CA    . ILE A 115 ? 0.0124 0.0355 0.0130 -0.0022 -0.0008 0.0092  115 ILE A CA    
898  C C     . ILE A 115 ? 0.1971 0.2205 0.1978 -0.0024 -0.0008 0.0093  115 ILE A C     
899  O O     . ILE A 115 ? 0.3655 0.3884 0.3668 -0.0022 -0.0009 0.0100  115 ILE A O     
900  C CB    . ILE A 115 ? 0.2349 0.2574 0.2356 -0.0019 -0.0007 0.0089  115 ILE A CB    
901  C CG1   . ILE A 115 ? 0.4578 0.4834 0.4623 -0.0024 -0.0008 0.0074  115 ILE A CG1   
902  C CG2   . ILE A 115 ? 0.0635 0.0851 0.0648 -0.0014 -0.0006 0.0094  115 ILE A CG2   
903  C CD1   . ILE A 115 ? 0.4613 0.4879 0.4653 -0.0031 -0.0009 0.0068  115 ILE A CD1   
904  N N     . TYR A 116 ? 0.2076 0.2318 0.2076 -0.0028 -0.0009 0.0087  116 TYR A N     
905  C CA    . TYR A 116 ? 0.3279 0.3525 0.3276 -0.0031 -0.0010 0.0086  116 TYR A CA    
906  C C     . TYR A 116 ? 0.2175 0.2439 0.2226 -0.0029 -0.0010 0.0084  116 TYR A C     
907  O O     . TYR A 116 ? 0.1673 0.1929 0.1724 -0.0025 -0.0009 0.0083  116 TYR A O     
908  C CB    . TYR A 116 ? 0.2519 0.2772 0.2509 -0.0036 -0.0010 0.0076  116 TYR A CB    
909  C CG    . TYR A 116 ? 0.1181 0.1441 0.1165 -0.0042 -0.0011 0.0073  116 TYR A CG    
910  C CD1   . TYR A 116 ? 0.0148 0.0514 0.0161 -0.0064 -0.0016 0.0094  116 TYR A CD1   
911  C CD2   . TYR A 116 ? 0.2351 0.2639 0.2383 -0.0049 -0.0010 0.0060  116 TYR A CD2   
912  C CE1   . TYR A 116 ? 0.2883 0.3157 0.2861 -0.0053 -0.0013 0.0072  116 TYR A CE1   
913  C CE2   . TYR A 116 ? 0.1883 0.2151 0.1858 -0.0051 -0.0011 0.0061  116 TYR A CE2   
914  C CZ    . TYR A 116 ? 0.2607 0.2984 0.2609 -0.0076 -0.0015 0.0080  116 TYR A CZ    
915  O OH    . TYR A 116 ? 0.2688 0.3001 0.2684 -0.0068 -0.0024 0.0057  116 TYR A OH    
916  N N     . PRO A 117 ? 0.2875 0.3138 0.2930 -0.0030 -0.0011 0.0090  117 PRO A N     
917  C CA    . PRO A 117 ? 0.0127 0.0352 0.0144 -0.0024 -0.0010 0.0106  117 PRO A CA    
918  C C     . PRO A 117 ? 0.2380 0.2631 0.2441 -0.0025 -0.0010 0.0094  117 PRO A C     
919  O O     . PRO A 117 ? 0.2297 0.2510 0.2319 -0.0018 -0.0008 0.0106  117 PRO A O     
920  C CB    . PRO A 117 ? 0.1569 0.1825 0.1637 -0.0030 -0.0013 0.0104  117 PRO A CB    
921  C CG    . PRO A 117 ? 0.0137 0.0374 0.0152 -0.0032 -0.0013 0.0111  117 PRO A CG    
922  C CD    . PRO A 117 ? 0.1183 0.1455 0.1238 -0.0036 -0.0013 0.0092  117 PRO A CD    
923  N N     . PRO A 118 ? 0.0812 0.1070 0.0865 -0.0029 -0.0011 0.0086  118 PRO A N     
924  C CA    . PRO A 118 ? 0.0793 0.1049 0.0844 -0.0028 -0.0010 0.0083  118 PRO A CA    
925  C C     . PRO A 118 ? 0.2254 0.2477 0.2261 -0.0021 -0.0007 0.0089  118 PRO A C     
926  O O     . PRO A 118 ? 0.3879 0.4122 0.3931 -0.0020 -0.0007 0.0081  118 PRO A O     
927  C CB    . PRO A 118 ? 0.1237 0.1505 0.1280 -0.0035 -0.0010 0.0073  118 PRO A CB    
928  C CG    . PRO A 118 ? 0.2010 0.2286 0.2053 -0.0040 -0.0012 0.0076  118 PRO A CG    
929  C CD    . PRO A 118 ? 0.2337 0.2608 0.2385 -0.0037 -0.0012 0.0083  118 PRO A CD    
930  N N     . PHE A 119 ? 0.2342 0.2590 0.2391 -0.0022 -0.0008 0.0080  119 PHE A N     
931  C CA    . PHE A 119 ? 0.0092 0.0332 0.0142 -0.0017 -0.0006 0.0080  119 PHE A CA    
932  C C     . PHE A 119 ? 0.0113 0.0317 0.0130 -0.0011 -0.0005 0.0096  119 PHE A C     
933  O O     . PHE A 119 ? 0.1903 0.2126 0.1964 -0.0009 -0.0004 0.0089  119 PHE A O     
934  C CB    . PHE A 119 ? 0.0115 0.0332 0.0120 -0.0016 -0.0006 0.0084  119 PHE A CB    
935  C CG    . PHE A 119 ? 0.0202 0.0429 0.0199 -0.0022 -0.0006 0.0075  119 PHE A CG    
936  C CD1   . PHE A 119 ? 0.1051 0.1313 0.1088 -0.0030 -0.0008 0.0064  119 PHE A CD1   
937  C CD2   . PHE A 119 ? 0.1758 0.1985 0.1752 -0.0022 -0.0006 0.0071  119 PHE A CD2   
938  C CE1   . PHE A 119 ? 0.3491 0.3737 0.3475 -0.0035 -0.0008 0.0061  119 PHE A CE1   
939  C CE2   . PHE A 119 ? 0.3258 0.3583 0.3271 -0.0039 -0.0009 0.0076  119 PHE A CE2   
940  C CZ    . PHE A 119 ? 0.4206 0.4481 0.4206 -0.0038 -0.0017 0.0056  119 PHE A CZ    
941  N N     . PHE A 120 ? 0.0934 0.1136 0.0958 -0.0011 -0.0005 0.0103  120 PHE A N     
942  C CA    . PHE A 120 ? 0.0495 0.0688 0.0530 -0.0008 -0.0004 0.0113  120 PHE A CA    
943  C C     . PHE A 120 ? 0.0093 0.0310 0.0175 -0.0009 -0.0005 0.0107  120 PHE A C     
944  O O     . PHE A 120 ? 0.0115 0.0297 0.0164 -0.0005 -0.0003 0.0121  120 PHE A O     
945  C CB    . PHE A 120 ? 0.1907 0.2129 0.1991 -0.0010 -0.0006 0.0110  120 PHE A CB    
946  C CG    . PHE A 120 ? 0.1834 0.2030 0.1873 -0.0010 -0.0005 0.0117  120 PHE A CG    
947  C CD1   . PHE A 120 ? 0.1185 0.1376 0.1227 -0.0006 -0.0004 0.0118  120 PHE A CD1   
948  C CD2   . PHE A 120 ? 0.1064 0.1267 0.1096 -0.0013 -0.0006 0.0114  120 PHE A CD2   
949  C CE1   . PHE A 120 ? 0.0506 0.0699 0.0545 -0.0006 -0.0003 0.0116  120 PHE A CE1   
950  C CE2   . PHE A 120 ? 0.0350 0.0556 0.0380 -0.0013 -0.0006 0.0112  120 PHE A CE2   
951  C CZ    . PHE A 120 ? 0.0118 0.0317 0.0151 -0.0009 -0.0005 0.0113  120 PHE A CZ    
952  N N     . GLU A 121 ? 0.0118 0.0312 0.0156 -0.0011 -0.0006 0.0117  121 GLU A N     
953  C CA    . GLU A 121 ? 0.4152 0.4371 0.4241 -0.0012 -0.0007 0.0113  121 GLU A CA    
954  C C     . GLU A 121 ? 0.2144 0.2360 0.2229 -0.0010 -0.0006 0.0109  121 GLU A C     
955  O O     . GLU A 121 ? 0.2277 0.2454 0.2333 -0.0007 -0.0004 0.0127  121 GLU A O     
956  C CB    . GLU A 121 ? 0.3348 0.3543 0.3391 -0.0016 -0.0009 0.0124  121 GLU A CB    
957  C CG    . GLU A 121 ? 0.1439 0.1665 0.1533 -0.0021 -0.0012 0.0120  121 GLU A CG    
958  C CD    . GLU A 121 ? 0.1107 0.1289 0.1180 -0.0018 -0.0012 0.0145  121 GLU A CD    
959  O OE1   . GLU A 121 ? 0.1421 0.1599 0.1501 -0.0014 -0.0010 0.0148  121 GLU A OE1   
960  O OE2   . GLU A 121 ? 0.2638 0.2814 0.2725 -0.0021 -0.0016 0.0154  121 GLU A OE2   
961  N N     . MET A 122 ? 0.2178 0.2401 0.2249 -0.0012 -0.0006 0.0099  122 MET A N     
962  C CA    . MET A 122 ? 0.0639 0.0860 0.0706 -0.0010 -0.0005 0.0095  122 MET A CA    
963  C C     . MET A 122 ? 0.0595 0.0780 0.0628 -0.0005 -0.0002 0.0107  122 MET A C     
964  O O     . MET A 122 ? 0.3060 0.3241 0.3098 -0.0003 -0.0001 0.0109  122 MET A O     
965  C CB    . MET A 122 ? 0.0738 0.0969 0.0791 -0.0015 -0.0006 0.0082  122 MET A CB    
966  C CG    . MET A 122 ? 0.1708 0.1926 0.1712 -0.0020 -0.0007 0.0084  122 MET A CG    
967  S SD    . MET A 122 ? 0.1963 0.2208 0.2011 -0.0024 -0.0008 0.0079  122 MET A SD    
968  C CE    . MET A 122 ? 0.0488 0.0707 0.0499 -0.0023 -0.0009 0.0097  122 MET A CE    
969  N N     . VAL A 123 ? 0.2501 0.2685 0.2535 -0.0003 -0.0002 0.0107  123 VAL A N     
970  C CA    . VAL A 123 ? 0.3222 0.3400 0.3262 0.0000  0.0000  0.0111  123 VAL A CA    
971  C C     . VAL A 123 ? 0.0112 0.0280 0.0168 0.0003  0.0002  0.0122  123 VAL A C     
972  O O     . VAL A 123 ? 0.0091 0.0283 0.0191 0.0006  0.0004  0.0115  123 VAL A O     
973  C CB    . VAL A 123 ? 0.0108 0.0287 0.0145 0.0001  0.0000  0.0109  123 VAL A CB    
974  C CG1   . VAL A 123 ? 0.0086 0.0287 0.0166 0.0004  0.0002  0.0102  123 VAL A CG1   
975  C CG2   . VAL A 123 ? 0.0106 0.0293 0.0132 -0.0002 -0.0001 0.0099  123 VAL A CG2   
976  N N     . THR A 124 ? 0.0116 0.0282 0.0181 0.0002  0.0001  0.0129  124 THR A N     
977  C CA    . THR A 124 ? 0.1524 0.1682 0.1610 0.0004  0.0003  0.0141  124 THR A CA    
978  C C     . THR A 124 ? 0.0125 0.0276 0.0223 0.0003  0.0003  0.0147  124 THR A C     
979  O O     . THR A 124 ? 0.2033 0.2214 0.2190 0.0006  0.0005  0.0143  124 THR A O     
980  C CB    . THR A 124 ? 0.2358 0.2551 0.2491 0.0002  0.0002  0.0135  124 THR A CB    
981  O OG1   . THR A 124 ? 0.3519 0.3718 0.3641 -0.0002 -0.0001 0.0130  124 THR A OG1   
982  C CG2   . THR A 124 ? 0.1193 0.1387 0.1323 0.0004  0.0003  0.0134  124 THR A CG2   
983  N N     . THR A 125 ? 0.0123 0.0278 0.0213 0.0000  0.0000  0.0144  125 THR A N     
984  C CA    . THR A 125 ? 0.0101 0.0284 0.0245 0.0000  0.0000  0.0137  125 THR A CA    
985  C C     . THR A 125 ? 0.0674 0.0818 0.0777 0.0003  0.0003  0.0147  125 THR A C     
986  O O     . THR A 125 ? 0.0953 0.1092 0.1083 0.0007  0.0001  0.0156  125 THR A O     
987  C CB    . THR A 125 ? 0.0592 0.0781 0.0727 -0.0005 -0.0004 0.0134  125 THR A CB    
988  O OG1   . THR A 125 ? 0.0739 0.0908 0.0806 -0.0006 -0.0004 0.0132  125 THR A OG1   
989  C CG2   . THR A 125 ? 0.1356 0.1508 0.1463 -0.0007 -0.0006 0.0154  125 THR A CG2   
990  N N     . ASN A 126 ? 0.1163 0.1315 0.1246 0.0004  0.0003  0.0137  126 ASN A N     
991  C CA    . ASN A 126 ? 0.0116 0.0266 0.0197 0.0006  0.0005  0.0135  126 ASN A CA    
992  C C     . ASN A 126 ? 0.1245 0.1389 0.1337 0.0010  0.0008  0.0140  126 ASN A C     
993  O O     . ASN A 126 ? 0.0162 0.0339 0.0287 0.0013  0.0010  0.0126  126 ASN A O     
994  C CB    . ASN A 126 ? 0.0110 0.0272 0.0168 0.0005  0.0003  0.0121  126 ASN A CB    
995  C CG    . ASN A 126 ? 0.3459 0.3656 0.3521 0.0003  -0.0003 0.0124  126 ASN A CG    
996  O OD1   . ASN A 126 ? 0.4541 0.4761 0.4619 0.0003  0.0000  0.0136  126 ASN A OD1   
997  N ND2   . ASN A 126 ? 0.0748 0.0949 0.0796 -0.0001 -0.0006 0.0115  126 ASN A ND2   
998  N N     . ASN A 127 ? 0.1972 0.2148 0.2117 0.0011  0.0010  0.0136  127 ASN A N     
999  C CA    . ASN A 127 ? 0.3462 0.3599 0.3582 0.0013  0.0012  0.0155  127 ASN A CA    
1000 C C     . ASN A 127 ? 0.2228 0.2406 0.2369 0.0016  0.0014  0.0135  127 ASN A C     
1001 O O     . ASN A 127 ? 0.3606 0.3747 0.3713 0.0017  0.0015  0.0150  127 ASN A O     
1002 C CB    . ASN A 127 ? 0.4108 0.4235 0.4250 0.0015  0.0016  0.0163  127 ASN A CB    
1003 C CG    . ASN A 127 ? 0.3125 0.3244 0.3297 0.0014  0.0016  0.0175  127 ASN A CG    
1004 O OD1   . ASN A 127 ? 0.1963 0.2079 0.2155 0.0016  0.0019  0.0183  127 ASN A OD1   
1005 N ND2   . ASN A 127 ? 0.2585 0.2702 0.2763 0.0011  0.0013  0.0175  127 ASN A ND2   
1006 N N     . ARG A 128 ? 0.1676 0.1825 0.1761 0.0012  0.0010  0.0139  128 ARG A N     
1007 C CA    . ARG A 128 ? 0.2583 0.2737 0.2659 0.0013  0.0010  0.0134  128 ARG A CA    
1008 C C     . ARG A 128 ? 0.3486 0.3674 0.3603 0.0014  0.0010  0.0125  128 ARG A C     
1009 O O     . ARG A 128 ? 0.1807 0.1994 0.1931 0.0013  0.0010  0.0129  128 ARG A O     
1010 C CB    . ARG A 128 ? 0.0119 0.0280 0.0177 0.0011  0.0007  0.0122  128 ARG A CB    
1011 C CG    . ARG A 128 ? 0.1823 0.1983 0.1878 0.0012  0.0008  0.0119  128 ARG A CG    
1012 C CD    . ARG A 128 ? 0.2901 0.3057 0.2962 0.0013  0.0009  0.0123  128 ARG A CD    
1013 N NE    . ARG A 128 ? 0.4278 0.4438 0.4332 0.0012  0.0008  0.0117  128 ARG A NE    
1014 C CZ    . ARG A 128 ? 0.1985 0.2150 0.2051 0.0017  0.0004  0.0122  128 ARG A CZ    
1015 N NH1   . ARG A 128 ? 0.4330 0.4484 0.4410 0.0018  0.0006  0.0131  128 ARG A NH1   
1016 N NH2   . ARG A 128 ? 0.0906 0.1100 0.0977 0.0016  0.0006  0.0128  128 ARG A NH2   
1017 N N     . GLN A 129 ? 0.4789 0.4978 0.4901 0.0015  0.0011  0.0122  129 GLN A N     
1018 C CA    . GLN A 129 ? 0.2259 0.2450 0.2375 0.0015  0.0011  0.0125  129 GLN A CA    
1019 C C     . GLN A 129 ? 0.1834 0.2027 0.1937 0.0012  0.0009  0.0117  129 GLN A C     
1020 O O     . GLN A 129 ? 0.2599 0.2765 0.2653 0.0010  0.0007  0.0120  129 GLN A O     
1021 C CB    . GLN A 129 ? 0.1628 0.1820 0.1745 0.0018  0.0013  0.0127  129 GLN A CB    
1022 C CG    . GLN A 129 ? 0.1518 0.1679 0.1598 0.0017  0.0012  0.0141  129 GLN A CG    
1023 C CD    . GLN A 129 ? 0.3261 0.3422 0.3346 0.0019  0.0015  0.0146  129 GLN A CD    
1024 O OE1   . GLN A 129 ? 0.3426 0.3585 0.3520 0.0021  0.0017  0.0153  129 GLN A OE1   
1025 N NE2   . GLN A 129 ? 0.4294 0.4491 0.4413 0.0021  0.0016  0.0130  129 GLN A NE2   
1026 N N     . LEU A 130 ? 0.2889 0.3083 0.2995 0.0011  0.0008  0.0120  130 LEU A N     
1027 C CA    . LEU A 130 ? 0.2350 0.2517 0.2409 0.0008  0.0005  0.0125  130 LEU A CA    
1028 C C     . LEU A 130 ? 0.4664 0.4832 0.4721 0.0009  0.0006  0.0124  130 LEU A C     
1029 O O     . LEU A 130 ? 0.4407 0.4604 0.4512 0.0011  0.0008  0.0119  130 LEU A O     
1030 C CB    . LEU A 130 ? 0.1055 0.1222 0.1119 0.0006  0.0004  0.0129  130 LEU A CB    
1031 C CG    . LEU A 130 ? 0.0114 0.0287 0.0169 0.0004  0.0002  0.0123  130 LEU A CG    
1032 C CD1   . LEU A 130 ? 0.0111 0.0288 0.0156 0.0002  0.0001  0.0116  130 LEU A CD1   
1033 C CD2   . LEU A 130 ? 0.0117 0.0290 0.0179 0.0002  0.0001  0.0130  130 LEU A CD2   
1034 N N     . CYS A 131 ? 0.5522 0.5692 0.5569 0.0008  0.0005  0.0116  131 CYS A N     
1035 C CA    . CYS A 131 ? 0.2713 0.2885 0.2758 0.0008  0.0005  0.0114  131 CYS A CA    
1036 C C     . CYS A 131 ? 0.3797 0.3999 0.3873 0.0007  0.0004  0.0100  131 CYS A C     
1037 O O     . CYS A 131 ? 0.3578 0.3756 0.3611 0.0004  0.0002  0.0105  131 CYS A O     
1038 C CB    . CYS A 131 ? 0.3547 0.3719 0.3589 0.0010  0.0006  0.0111  131 CYS A CB    
1039 S SG    . CYS A 131 ? 0.4540 0.4709 0.4589 0.0013  0.0008  0.0118  131 CYS A SG    
1040 N N     . VAL A 132 ? 0.4252 0.4455 0.4330 0.0007  0.0004  0.0100  132 VAL A N     
1041 C CA    . VAL A 132 ? 0.1598 0.1777 0.1632 0.0004  0.0002  0.0106  132 VAL A CA    
1042 C C     . VAL A 132 ? 0.0274 0.0479 0.0343 0.0005  0.0002  0.0094  132 VAL A C     
1043 O O     . VAL A 132 ? 0.0357 0.0560 0.0428 0.0007  0.0004  0.0096  132 VAL A O     
1044 C CB    . VAL A 132 ? 0.1104 0.1283 0.1143 0.0003  0.0002  0.0111  132 VAL A CB    
1045 C CG1   . VAL A 132 ? 0.0204 0.0412 0.0284 0.0002  0.0001  0.0104  132 VAL A CG1   
1046 C CG2   . VAL A 132 ? 0.0227 0.0403 0.0274 0.0005  0.0003  0.0117  132 VAL A CG2   
1047 N N     . SER A 133 ? 0.0084 0.0292 0.0148 0.0002  0.0001  0.0090  133 SER A N     
1048 C CA    . SER A 133 ? 0.3149 0.3359 0.3211 0.0002  0.0001  0.0088  133 SER A CA    
1049 C C     . SER A 133 ? 0.3909 0.4122 0.3970 0.0000  0.0000  0.0087  133 SER A C     
1050 O O     . SER A 133 ? 0.3784 0.4002 0.3840 -0.0003 -0.0001 0.0083  133 SER A O     
1051 C CB    . SER A 133 ? 0.0334 0.0545 0.0391 0.0001  0.0001  0.0083  133 SER A CB    
1052 O OG    . SER A 133 ? 0.1702 0.1893 0.1718 0.0000  0.0000  0.0087  133 SER A OG    
1053 N N     . PRO A 134 ? 0.3368 0.3555 0.3395 0.0001  0.0000  0.0100  134 PRO A N     
1054 C CA    . PRO A 134 ? 0.0652 0.0869 0.0718 -0.0001 -0.0001 0.0092  134 PRO A CA    
1055 C C     . PRO A 134 ? 0.0087 0.0307 0.0148 -0.0003 -0.0001 0.0089  134 PRO A C     
1056 O O     . PRO A 134 ? 0.0107 0.0300 0.0129 -0.0002 -0.0001 0.0096  134 PRO A O     
1057 C CB    . PRO A 134 ? 0.0693 0.0881 0.0725 0.0000  0.0000  0.0107  134 PRO A CB    
1058 C CG    . PRO A 134 ? 0.0470 0.0654 0.0507 0.0002  0.0001  0.0110  134 PRO A CG    
1059 C CD    . PRO A 134 ? 0.0086 0.0295 0.0158 0.0003  0.0002  0.0097  134 PRO A CD    
1060 N N     . LEU A 135 ? 0.0088 0.0315 0.0148 -0.0006 -0.0002 0.0088  135 LEU A N     
1061 C CA    . LEU A 135 ? 0.3715 0.3946 0.3772 -0.0008 -0.0003 0.0085  135 LEU A CA    
1062 C C     . LEU A 135 ? 0.2500 0.2730 0.2560 -0.0006 -0.0003 0.0089  135 LEU A C     
1063 O O     . LEU A 135 ? 0.1914 0.2115 0.1937 -0.0005 -0.0002 0.0102  135 LEU A O     
1064 C CB    . LEU A 135 ? 0.3630 0.3870 0.3684 -0.0012 -0.0004 0.0083  135 LEU A CB    
1065 C CG    . LEU A 135 ? 0.1743 0.1961 0.1750 -0.0013 -0.0005 0.0086  135 LEU A CG    
1066 C CD1   . LEU A 135 ? 0.1249 0.1477 0.1252 -0.0018 -0.0006 0.0084  135 LEU A CD1   
1067 C CD2   . LEU A 135 ? 0.0114 0.0333 0.0117 -0.0015 -0.0005 0.0080  135 LEU A CD2   
1068 N N     . GLN A 136 ? 0.2662 0.2893 0.2720 -0.0007 -0.0003 0.0087  136 GLN A N     
1069 C CA    . GLN A 136 ? 0.2786 0.3017 0.2847 -0.0005 -0.0002 0.0090  136 GLN A CA    
1070 C C     . GLN A 136 ? 0.1476 0.1714 0.1537 -0.0008 -0.0003 0.0090  136 GLN A C     
1071 O O     . GLN A 136 ? 0.0116 0.0332 0.0130 -0.0009 -0.0004 0.0095  136 GLN A O     
1072 C CB    . GLN A 136 ? 0.1784 0.1984 0.1804 -0.0003 -0.0001 0.0096  136 GLN A CB    
1073 C CG    . GLN A 136 ? 0.2481 0.2701 0.2543 -0.0001 -0.0001 0.0089  136 GLN A CG    
1074 C CD    . GLN A 136 ? 0.3554 0.3744 0.3579 0.0001  0.0000  0.0099  136 GLN A CD    
1075 O OE1   . GLN A 136 ? 0.4142 0.4332 0.4166 0.0001  0.0000  0.0099  136 GLN A OE1   
1076 N NE2   . GLN A 136 ? 0.2965 0.3176 0.3030 0.0003  0.0001  0.0092  136 GLN A NE2   
1077 N N     . LYS A 137 ? 0.0894 0.1106 0.0916 -0.0007 -0.0003 0.0103  137 LYS A N     
1078 C CA    . LYS A 137 ? 0.1711 0.1959 0.1777 -0.0009 -0.0004 0.0097  137 LYS A CA    
1079 C C     . LYS A 137 ? 0.3678 0.3897 0.3700 -0.0007 -0.0003 0.0106  137 LYS A C     
1080 O O     . LYS A 137 ? 0.3806 0.4047 0.3875 -0.0005 -0.0002 0.0099  137 LYS A O     
1081 C CB    . LYS A 137 ? 0.0099 0.0349 0.0169 -0.0009 -0.0004 0.0102  137 LYS A CB    
1082 C CG    . LYS A 137 ? 0.3211 0.3472 0.3282 -0.0013 -0.0005 0.0103  137 LYS A CG    
1083 C CD    . LYS A 137 ? 0.3363 0.3625 0.3438 -0.0013 -0.0006 0.0109  137 LYS A CD    
1084 C CE    . LYS A 137 ? 0.3017 0.3258 0.3043 -0.0015 -0.0007 0.0121  137 LYS A CE    
1085 N NZ    . LYS A 137 ? 0.2861 0.3106 0.2892 -0.0016 -0.0007 0.0127  137 LYS A NZ    
1086 N N     . GLN A 138 ? 0.3033 0.3257 0.3051 -0.0008 -0.0004 0.0103  138 GLN A N     
1087 C CA    . GLN A 138 ? 0.2610 0.2834 0.2629 -0.0007 -0.0003 0.0105  138 GLN A CA    
1088 C C     . GLN A 138 ? 0.3351 0.3654 0.3401 -0.0010 -0.0008 0.0124  138 GLN A C     
1089 O O     . GLN A 138 ? 0.2606 0.2918 0.2652 -0.0023 0.0014  0.0122  138 GLN A O     
1090 C CB    . GLN A 138 ? 0.3913 0.4161 0.3951 -0.0004 -0.0012 0.0102  138 GLN A CB    
1091 C CG    . GLN A 138 ? 0.4975 0.5214 0.5036 -0.0005 -0.0002 0.0090  138 GLN A CG    
1092 C CD    . GLN A 138 ? 0.4656 0.4867 0.4671 -0.0006 -0.0002 0.0093  138 GLN A CD    
1093 O OE1   . GLN A 138 ? 0.5517 0.5792 0.5554 -0.0009 -0.0007 0.0104  138 GLN A OE1   
1094 N NE2   . GLN A 138 ? 0.3872 0.4077 0.3888 -0.0004 -0.0002 0.0093  138 GLN A NE2   
1095 N N     . ASN A 139 ? 0.3728 0.4034 0.3784 -0.0007 -0.0006 0.0131  139 ASN A N     
1096 C CA    . ASN A 139 ? 0.4796 0.5096 0.4848 -0.0022 0.0032  0.0131  139 ASN A CA    
1097 C C     . ASN A 139 ? 0.5155 0.5437 0.5191 -0.0034 0.0055  0.0125  139 ASN A C     
1098 O O     . ASN A 139 ? 0.6423 0.6650 0.6429 -0.0054 0.0110  0.0111  139 ASN A O     
1099 C CB    . ASN A 139 ? 0.5077 0.5333 0.5117 -0.0038 0.0078  0.0112  139 ASN A CB    
1100 C CG    . ASN A 139 ? 0.5636 0.5900 0.5688 -0.0030 0.0065  0.0117  139 ASN A CG    
1101 O OD1   . ASN A 139 ? 0.5397 0.5685 0.5458 -0.0015 0.0037  0.0133  139 ASN A OD1   
1102 N ND2   . ASN A 139 ? 0.5748 0.5990 0.5799 -0.0040 0.0088  0.0102  139 ASN A ND2   
1103 N N     . ASP A 140 ? 0.1563 0.1887 0.1613 -0.0023 0.0017  0.0138  140 ASP A N     
1104 C CA    . ASP A 140 ? 0.1406 0.1718 0.1442 -0.0034 0.0033  0.0133  140 ASP A CA    
1105 C C     . ASP A 140 ? 0.2041 0.2318 0.2055 -0.0047 0.0065  0.0118  140 ASP A C     
1106 O O     . ASP A 140 ? 0.1842 0.2070 0.1820 -0.0062 0.0108  0.0111  140 ASP A O     
1107 C CB    . ASP A 140 ? 0.0978 0.1247 0.0983 -0.0045 0.0072  0.0133  140 ASP A CB    
1108 C CG    . ASP A 140 ? 0.5132 0.5447 0.5167 -0.0032 0.0036  0.0149  140 ASP A CG    
1109 O OD1   . ASP A 140 ? 0.5724 0.6087 0.5786 -0.0023 -0.0001 0.0158  140 ASP A OD1   
1110 O OD2   . ASP A 140 ? 0.5209 0.5514 0.5243 -0.0029 0.0044  0.0152  140 ASP A OD2   
1111 N N     . THR A 141 ? 0.1546 0.1841 0.1574 -0.0041 0.0045  0.0115  141 THR A N     
1112 C CA    . THR A 141 ? 0.1996 0.2279 0.2016 -0.0049 0.0058  0.0105  141 THR A CA    
1113 C C     . THR A 141 ? 0.0152 0.0475 0.0188 -0.0033 0.0010  0.0113  141 THR A C     
1114 O O     . THR A 141 ? 0.2104 0.2411 0.2144 -0.0019 -0.0011 0.0113  141 THR A O     
1115 C CB    . THR A 141 ? 0.1668 0.1891 0.1667 -0.0065 0.0117  0.0089  141 THR A CB    
1116 O OG1   . THR A 141 ? 0.0376 0.0573 0.0359 -0.0073 0.0144  0.0082  141 THR A OG1   
1117 C CG2   . THR A 141 ? 0.1140 0.1372 0.1156 -0.0062 0.0108  0.0084  141 THR A CG2   
1118 N N     . TYR A 142 ? 0.2401 0.2719 0.2433 -0.0038 0.0015  0.0104  142 TYR A N     
1119 C CA    . TYR A 142 ? 0.0620 0.0932 0.0651 -0.0025 -0.0011 0.0103  142 TYR A CA    
1120 C C     . TYR A 142 ? 0.1828 0.2147 0.1858 -0.0032 0.0001  0.0098  142 TYR A C     
1121 O O     . TYR A 142 ? 0.1572 0.1858 0.1601 -0.0050 0.0047  0.0081  142 TYR A O     
1122 C CB    . TYR A 142 ? 0.0416 0.0703 0.0443 -0.0023 -0.0015 0.0095  142 TYR A CB    
1123 C CG    . TYR A 142 ? 0.1440 0.1677 0.1447 -0.0018 -0.0007 0.0094  142 TYR A CG    
1124 C CD1   . TYR A 142 ? 0.0104 0.0377 0.0160 -0.0022 -0.0008 0.0089  142 TYR A CD1   
1125 C CD2   . TYR A 142 ? 0.0098 0.0353 0.0155 -0.0016 -0.0006 0.0089  142 TYR A CD2   
1126 C CE1   . TYR A 142 ? 0.1847 0.2118 0.1907 -0.0021 -0.0008 0.0094  142 TYR A CE1   
1127 C CE2   . TYR A 142 ? 0.0931 0.1185 0.0993 -0.0015 -0.0006 0.0094  142 TYR A CE2   
1128 C CZ    . TYR A 142 ? 0.2259 0.2492 0.2275 -0.0016 -0.0006 0.0106  142 TYR A CZ    
1129 O OH    . TYR A 142 ? 0.2355 0.2588 0.2376 -0.0016 -0.0007 0.0111  142 TYR A OH    
1130 N N     . VAL A 143 ? 0.1050 0.1341 0.1077 -0.0021 -0.0011 0.0095  143 VAL A N     
1131 C CA    . VAL A 143 ? 0.0171 0.0484 0.0197 -0.0026 -0.0008 0.0095  143 VAL A CA    
1132 C C     . VAL A 143 ? 0.0590 0.0843 0.0611 -0.0015 -0.0013 0.0082  143 VAL A C     
1133 O O     . VAL A 143 ? 0.1230 0.1469 0.1278 -0.0012 -0.0004 0.0076  143 VAL A O     
1134 C CB    . VAL A 143 ? 0.0468 0.0769 0.0500 -0.0030 0.0008  0.0089  143 VAL A CB    
1135 C CG1   . VAL A 143 ? 0.0165 0.0446 0.0204 -0.0042 0.0042  0.0080  143 VAL A CG1   
1136 C CG2   . VAL A 143 ? 0.0231 0.0496 0.0257 -0.0014 -0.0010 0.0090  143 VAL A CG2   
1137 N N     . ILE A 144 ? 0.2170 0.2444 0.2189 -0.0020 -0.0010 0.0081  144 ILE A N     
1138 C CA    . ILE A 144 ? 0.2248 0.2475 0.2262 -0.0011 -0.0014 0.0072  144 ILE A CA    
1139 C C     . ILE A 144 ? 0.3553 0.3761 0.3556 -0.0010 -0.0003 0.0076  144 ILE A C     
1140 O O     . ILE A 144 ? 0.3858 0.4081 0.3872 -0.0009 -0.0012 0.0072  144 ILE A O     
1141 C CB    . ILE A 144 ? 0.0630 0.0899 0.0645 -0.0021 -0.0010 0.0074  144 ILE A CB    
1142 C CG1   . ILE A 144 ? 0.0426 0.0735 0.0441 -0.0032 -0.0008 0.0076  144 ILE A CG1   
1143 C CG2   . ILE A 144 ? 0.0161 0.0385 0.0172 -0.0012 -0.0013 0.0067  144 ILE A CG2   
1144 C CD1   . ILE A 144 ? 0.0472 0.0767 0.0496 -0.0047 0.0024  0.0056  144 ILE A CD1   
1145 N N     . ASP A 145 ? 0.3369 0.3571 0.3377 -0.0006 -0.0002 0.0080  145 ASP A N     
1146 C CA    . ASP A 145 ? 0.1330 0.1550 0.1379 -0.0004 -0.0001 0.0075  145 ASP A CA    
1147 C C     . ASP A 145 ? 0.2856 0.3076 0.2903 -0.0004 -0.0001 0.0072  145 ASP A C     
1148 O O     . ASP A 145 ? 0.4963 0.5179 0.5011 -0.0002 -0.0001 0.0074  145 ASP A O     
1149 C CB    . ASP A 145 ? 0.0083 0.0298 0.0137 0.0000  0.0000  0.0081  145 ASP A CB    
1150 C CG    . ASP A 145 ? 0.1749 0.1960 0.1806 0.0002  0.0001  0.0083  145 ASP A CG    
1151 O OD1   . ASP A 145 ? 0.1496 0.1707 0.1551 0.0002  0.0001  0.0080  145 ASP A OD1   
1152 O OD2   . ASP A 145 ? 0.1324 0.1532 0.1384 0.0003  0.0002  0.0087  145 ASP A OD2   
1153 N N     . PHE A 146 ? 0.3653 0.3878 0.3696 -0.0007 -0.0002 0.0067  146 PHE A N     
1154 C CA    . PHE A 146 ? 0.2495 0.2721 0.2534 -0.0008 -0.0003 0.0063  146 PHE A CA    
1155 C C     . PHE A 146 ? 0.2881 0.3103 0.2923 -0.0004 -0.0001 0.0066  146 PHE A C     
1156 O O     . PHE A 146 ? 0.4089 0.4289 0.4091 -0.0004 -0.0001 0.0071  146 PHE A O     
1157 C CB    . PHE A 146 ? 0.1947 0.2207 0.1959 -0.0016 -0.0008 0.0067  146 PHE A CB    
1158 C CG    . PHE A 146 ? 0.2109 0.2405 0.2126 -0.0029 0.0001  0.0063  146 PHE A CG    
1159 C CD1   . PHE A 146 ? 0.0742 0.1035 0.0764 -0.0036 0.0013  0.0052  146 PHE A CD1   
1160 C CD2   . PHE A 146 ? 0.2241 0.2532 0.2268 -0.0036 0.0015  0.0058  146 PHE A CD2   
1161 C CE1   . PHE A 146 ? 0.0765 0.1049 0.0802 -0.0048 0.0038  0.0038  146 PHE A CE1   
1162 C CE2   . PHE A 146 ? 0.2704 0.2983 0.2742 -0.0049 0.0043  0.0044  146 PHE A CE2   
1163 C CZ    . PHE A 146 ? 0.1096 0.1372 0.1139 -0.0054 0.0054  0.0036  146 PHE A CZ    
1164 N N     . LYS A 147 ? 0.1337 0.1555 0.1381 -0.0002 -0.0001 0.0069  147 LYS A N     
1165 C CA    . LYS A 147 ? 0.1520 0.1713 0.1529 0.0001  0.0000  0.0079  147 LYS A CA    
1166 C C     . LYS A 147 ? 0.1848 0.2059 0.1899 0.0004  0.0002  0.0077  147 LYS A C     
1167 O O     . LYS A 147 ? 0.1977 0.2165 0.1993 0.0005  0.0002  0.0086  147 LYS A O     
1168 C CB    . LYS A 147 ? 0.2382 0.2572 0.2393 0.0002  0.0001  0.0081  147 LYS A CB    
1169 C CG    . LYS A 147 ? 0.2834 0.3022 0.2849 0.0005  0.0002  0.0085  147 LYS A CG    
1170 C CD    . LYS A 147 ? 0.3154 0.3363 0.3209 0.0007  0.0003  0.0081  147 LYS A CD    
1171 C CE    . LYS A 147 ? 0.4691 0.4875 0.4713 0.0009  0.0004  0.0094  147 LYS A CE    
1172 N NZ    . LYS A 147 ? 0.4848 0.5029 0.4874 0.0010  0.0005  0.0098  147 LYS A NZ    
1173 N N     . HIS A 148 ? 0.3100 0.3309 0.3153 0.0004  0.0002  0.0080  148 HIS A N     
1174 C CA    . HIS A 148 ? 0.1689 0.1895 0.1746 0.0006  0.0003  0.0083  148 HIS A CA    
1175 C C     . HIS A 148 ? 0.0528 0.0712 0.0546 0.0005  0.0002  0.0089  148 HIS A C     
1176 O O     . HIS A 148 ? 0.1668 0.1850 0.1689 0.0006  0.0003  0.0092  148 HIS A O     
1177 C CB    . HIS A 148 ? 0.0082 0.0288 0.0143 0.0006  0.0003  0.0086  148 HIS A CB    
1178 C CG    . HIS A 148 ? 0.1704 0.1908 0.1769 0.0007  0.0003  0.0090  148 HIS A CG    
1179 N ND1   . HIS A 148 ? 0.2408 0.2611 0.2478 0.0009  0.0005  0.0095  148 HIS A ND1   
1180 C CD2   . HIS A 148 ? 0.2071 0.2251 0.2099 0.0005  0.0003  0.0099  148 HIS A CD2   
1181 C CE1   . HIS A 148 ? 0.3682 0.3884 0.3756 0.0009  0.0005  0.0098  148 HIS A CE1   
1182 N NE2   . HIS A 148 ? 0.2675 0.2878 0.2746 0.0007  0.0004  0.0096  148 HIS A NE2   
1183 N N     . LEU A 149 ? 0.0790 0.1002 0.0841 0.0002  0.0001  0.0077  149 LEU A N     
1184 C CA    . LEU A 149 ? 0.2354 0.2568 0.2403 0.0001  0.0000  0.0074  149 LEU A CA    
1185 C C     . LEU A 149 ? 0.1159 0.1351 0.1169 0.0002  0.0001  0.0080  149 LEU A C     
1186 O O     . LEU A 149 ? 0.2329 0.2542 0.2378 0.0003  0.0001  0.0075  149 LEU A O     
1187 C CB    . LEU A 149 ? 0.0215 0.0435 0.0259 -0.0003 -0.0001 0.0069  149 LEU A CB    
1188 C CG    . LEU A 149 ? 0.0166 0.0390 0.0206 -0.0006 -0.0002 0.0065  149 LEU A CG    
1189 C CD1   . LEU A 149 ? 0.0081 0.0302 0.0125 -0.0004 -0.0001 0.0068  149 LEU A CD1   
1190 C CD2   . LEU A 149 ? 0.0104 0.0313 0.0101 -0.0011 -0.0003 0.0064  149 LEU A CD2   
1191 N N     . GLU A 150 ? 0.2028 0.2222 0.2036 0.0001  0.0000  0.0078  150 GLU A N     
1192 C CA    . GLU A 150 ? 0.3064 0.3282 0.3109 0.0002  0.0001  0.0070  150 GLU A CA    
1193 C C     . GLU A 150 ? 0.1807 0.2022 0.1858 0.0006  0.0002  0.0076  150 GLU A C     
1194 O O     . GLU A 150 ? 0.3695 0.3911 0.3746 0.0008  0.0003  0.0077  150 GLU A O     
1195 C CB    . GLU A 150 ? 0.3435 0.3659 0.3477 0.0000  0.0000  0.0066  150 GLU A CB    
1196 C CG    . GLU A 150 ? 0.3498 0.3726 0.3539 0.0000  0.0000  0.0064  150 GLU A CG    
1197 C CD    . GLU A 150 ? 0.3292 0.3505 0.3287 -0.0005 -0.0001 0.0062  150 GLU A CD    
1198 O OE1   . GLU A 150 ? 0.2916 0.3161 0.2920 -0.0007 -0.0008 0.0058  150 GLU A OE1   
1199 O OE2   . GLU A 150 ? 0.3891 0.4104 0.3886 -0.0006 -0.0001 0.0061  150 GLU A OE2   
1200 N N     . LYS A 151 ? 0.0082 0.0293 0.0137 0.0008  0.0003  0.0081  151 LYS A N     
1201 C CA    . LYS A 151 ? 0.0992 0.1201 0.1052 0.0011  0.0005  0.0087  151 LYS A CA    
1202 C C     . LYS A 151 ? 0.2624 0.2832 0.2687 0.0012  0.0006  0.0089  151 LYS A C     
1203 O O     . LYS A 151 ? 0.1802 0.2011 0.1868 0.0015  0.0007  0.0093  151 LYS A O     
1204 C CB    . LYS A 151 ? 0.0085 0.0292 0.0149 0.0012  0.0006  0.0090  151 LYS A CB    
1205 C CG    . LYS A 151 ? 0.3071 0.3280 0.3135 0.0013  0.0006  0.0090  151 LYS A CG    
1206 C CD    . LYS A 151 ? 0.0811 0.1018 0.0879 0.0014  0.0007  0.0094  151 LYS A CD    
1207 C CE    . LYS A 151 ? 0.3263 0.3445 0.3291 0.0013  0.0007  0.0102  151 LYS A CE    
1208 N NZ    . LYS A 151 ? 0.4120 0.4300 0.4151 0.0013  0.0007  0.0105  151 LYS A NZ    
1209 N N     . GLN A 152 ? 0.2738 0.2944 0.2799 0.0011  0.0005  0.0088  152 GLN A N     
1210 C CA    . GLN A 152 ? 0.2583 0.2763 0.2610 0.0011  0.0005  0.0099  152 GLN A CA    
1211 C C     . GLN A 152 ? 0.2497 0.2679 0.2521 0.0010  0.0005  0.0096  152 GLN A C     
1212 O O     . GLN A 152 ? 0.2132 0.2338 0.2198 0.0013  0.0007  0.0092  152 GLN A O     
1213 C CB    . GLN A 152 ? 0.1087 0.1266 0.1114 0.0009  0.0004  0.0098  152 GLN A CB    
1214 C CG    . GLN A 152 ? 0.1215 0.1393 0.1244 0.0009  0.0004  0.0100  152 GLN A CG    
1215 C CD    . GLN A 152 ? 0.1131 0.1306 0.1167 0.0011  0.0006  0.0107  152 GLN A CD    
1216 O OE1   . GLN A 152 ? 0.0109 0.0284 0.0148 0.0012  0.0007  0.0110  152 GLN A OE1   
1217 N NE2   . GLN A 152 ? 0.0245 0.0419 0.0284 0.0010  0.0006  0.0110  152 GLN A NE2   
1218 N N     . PHE A 153 ? 0.2795 0.2981 0.2813 0.0008  0.0004  0.0090  153 PHE A N     
1219 C CA    . PHE A 153 ? 0.0083 0.0296 0.0136 0.0008  0.0003  0.0080  153 PHE A CA    
1220 C C     . PHE A 153 ? 0.0105 0.0296 0.0122 0.0010  0.0004  0.0091  153 PHE A C     
1221 O O     . PHE A 153 ? 0.2552 0.2768 0.2608 0.0012  0.0005  0.0083  153 PHE A O     
1222 C CB    . PHE A 153 ? 0.1153 0.1349 0.1161 0.0004  0.0001  0.0079  153 PHE A CB    
1223 C CG    . PHE A 153 ? 0.0081 0.0302 0.0125 0.0001  0.0000  0.0068  153 PHE A CG    
1224 C CD1   . PHE A 153 ? 0.1795 0.1990 0.1803 0.0001  0.0001  0.0077  153 PHE A CD1   
1225 C CD2   . PHE A 153 ? 0.0102 0.0308 0.0101 -0.0004 -0.0001 0.0066  153 PHE A CD2   
1226 C CE1   . PHE A 153 ? 0.1705 0.1926 0.1747 -0.0002 -0.0001 0.0066  153 PHE A CE1   
1227 C CE2   . PHE A 153 ? 0.0099 0.0324 0.0106 -0.0007 -0.0010 0.0061  153 PHE A CE2   
1228 C CZ    . PHE A 153 ? 0.1579 0.1785 0.1576 -0.0007 -0.0002 0.0064  153 PHE A CZ    
1229 N N     . GLN A 154 ? 0.0107 0.0297 0.0126 0.0012  0.0005  0.0093  154 GLN A N     
1230 C CA    . GLN A 154 ? 0.0591 0.0808 0.0652 0.0015  0.0007  0.0089  154 GLN A CA    
1231 C C     . GLN A 154 ? 0.3012 0.3228 0.3080 0.0019  0.0009  0.0096  154 GLN A C     
1232 O O     . GLN A 154 ? 0.4242 0.4461 0.4313 0.0021  0.0011  0.0100  154 GLN A O     
1233 C CB    . GLN A 154 ? 0.0678 0.0897 0.0740 0.0016  0.0007  0.0091  154 GLN A CB    
1234 C CG    . GLN A 154 ? 0.0759 0.0956 0.0775 0.0012  0.0005  0.0092  154 GLN A CG    
1235 C CD    . GLN A 154 ? 0.0629 0.0827 0.0646 0.0013  0.0006  0.0094  154 GLN A CD    
1236 O OE1   . GLN A 154 ? 0.1966 0.2162 0.1988 0.0015  0.0007  0.0100  154 GLN A OE1   
1237 N NE2   . GLN A 154 ? 0.1964 0.2169 0.1977 0.0011  0.0004  0.0089  154 GLN A NE2   
1238 N N     . GLN A 155 ? 0.4354 0.4539 0.4385 0.0017  0.0009  0.0107  155 GLN A N     
1239 C CA    . GLN A 155 ? 0.3040 0.3223 0.3079 0.0019  0.0011  0.0115  155 GLN A CA    
1240 C C     . GLN A 155 ? 0.3013 0.3195 0.3052 0.0019  0.0011  0.0115  155 GLN A C     
1241 O O     . GLN A 155 ? 0.3561 0.3741 0.3607 0.0021  0.0013  0.0121  155 GLN A O     
1242 C CB    . GLN A 155 ? 0.3976 0.4155 0.4020 0.0019  0.0011  0.0118  155 GLN A CB    
1243 C CG    . GLN A 155 ? 0.4138 0.4344 0.4219 0.0020  0.0011  0.0106  155 GLN A CG    
1244 C CD    . GLN A 155 ? 0.3321 0.3496 0.3367 0.0017  0.0010  0.0119  155 GLN A CD    
1245 O OE1   . GLN A 155 ? 0.3505 0.3679 0.3549 0.0015  0.0009  0.0115  155 GLN A OE1   
1246 N NE2   . GLN A 155 ? 0.2644 0.2819 0.2696 0.0019  0.0012  0.0125  155 GLN A NE2   
1247 N N     . GLY A 156 ? 0.2132 0.2342 0.2204 0.0019  0.0010  0.0099  156 GLY A N     
1248 C CA    . GLY A 156 ? 0.0112 0.0296 0.0143 0.0017  0.0009  0.0107  156 GLY A CA    
1249 C C     . GLY A 156 ? 0.0634 0.0842 0.0701 0.0017  0.0008  0.0094  156 GLY A C     
1250 O O     . GLY A 156 ? 0.0907 0.1089 0.0936 0.0015  0.0008  0.0103  156 GLY A O     
1251 N N     . ILE A 157 ? 0.1584 0.1791 0.1647 0.0014  0.0007  0.0090  157 ILE A N     
1252 C CA    . ILE A 157 ? 0.0083 0.0290 0.0144 0.0011  0.0005  0.0087  157 ILE A CA    
1253 C C     . ILE A 157 ? 0.3842 0.4029 0.3860 0.0009  0.0004  0.0089  157 ILE A C     
1254 O O     . ILE A 157 ? 0.5032 0.5247 0.5082 0.0007  0.0003  0.0077  157 ILE A O     
1255 C CB    . ILE A 157 ? 0.0082 0.0290 0.0139 0.0009  0.0004  0.0083  157 ILE A CB    
1256 C CG1   . ILE A 157 ? 0.0799 0.0980 0.0823 0.0010  0.0005  0.0096  157 ILE A CG1   
1257 C CG2   . ILE A 157 ? 0.0081 0.0290 0.0135 0.0006  0.0002  0.0080  157 ILE A CG2   
1258 C CD1   . ILE A 157 ? 0.2000 0.2178 0.2030 0.0010  0.0005  0.0100  157 ILE A CD1   
1259 N N     . LYS A 158 ? 0.5263 0.5471 0.5319 0.0010  0.0004  0.0083  158 LYS A N     
1260 C CA    . LYS A 158 ? 0.4810 0.4999 0.4824 0.0007  0.0003  0.0085  158 LYS A CA    
1261 C C     . LYS A 158 ? 0.3628 0.3824 0.3636 0.0002  0.0001  0.0077  158 LYS A C     
1262 O O     . LYS A 158 ? 0.5164 0.5401 0.5180 -0.0001 -0.0005 0.0075  158 LYS A O     
1263 C CB    . LYS A 158 ? 0.4716 0.4925 0.4773 0.0010  0.0004  0.0083  158 LYS A CB    
1264 C CG    . LYS A 158 ? 0.3016 0.3197 0.3041 0.0013  0.0006  0.0098  158 LYS A CG    
1265 C CD    . LYS A 158 ? 0.3728 0.3914 0.3750 0.0013  0.0006  0.0095  158 LYS A CD    
1266 C CE    . LYS A 158 ? 0.2948 0.3151 0.2982 0.0016  0.0000  0.0098  158 LYS A CE    
1267 N NZ    . LYS A 158 ? 0.3390 0.3616 0.3433 0.0018  0.0004  0.0108  158 LYS A NZ    
1268 N N     . LEU A 159 ? 0.0101 0.0294 0.0110 0.0002  0.0001  0.0078  159 LEU A N     
1269 C CA    . LEU A 159 ? 0.0132 0.0353 0.0173 -0.0004 -0.0001 0.0065  159 LEU A CA    
1270 C C     . LEU A 159 ? 0.2763 0.2963 0.2766 -0.0004 -0.0001 0.0072  159 LEU A C     
1271 O O     . LEU A 159 ? 0.1009 0.1225 0.1056 -0.0001 0.0000  0.0072  159 LEU A O     
1272 C CB    . LEU A 159 ? 0.0101 0.0300 0.0105 -0.0003 -0.0001 0.0073  159 LEU A CB    
1273 C CG    . LEU A 159 ? 0.1575 0.1804 0.1584 -0.0009 -0.0009 0.0067  159 LEU A CG    
1274 C CD1   . LEU A 159 ? 0.0513 0.0798 0.0523 -0.0021 -0.0006 0.0062  159 LEU A CD1   
1275 C CD2   . LEU A 159 ? 0.0099 0.0320 0.0109 -0.0007 -0.0010 0.0069  159 LEU A CD2   
1276 N N     . MET A 160 ? 0.2305 0.2520 0.2312 -0.0007 -0.0011 0.0063  160 MET A N     
1277 C CA    . MET A 160 ? 0.2597 0.2805 0.2594 -0.0011 -0.0003 0.0065  160 MET A CA    
1278 C C     . MET A 160 ? 0.2871 0.3106 0.2876 -0.0016 -0.0012 0.0060  160 MET A C     
1279 O O     . MET A 160 ? 0.2611 0.2895 0.2616 -0.0028 -0.0008 0.0056  160 MET A O     
1280 C CB    . MET A 160 ? 0.1629 0.1850 0.1635 -0.0011 -0.0012 0.0061  160 MET A CB    
1281 C CG    . MET A 160 ? 0.3188 0.3401 0.3183 -0.0014 -0.0004 0.0062  160 MET A CG    
1282 S SD    . MET A 160 ? 0.2100 0.2333 0.2106 -0.0015 -0.0012 0.0060  160 MET A SD    
1283 C CE    . MET A 160 ? 0.0112 0.0418 0.0118 -0.0033 -0.0006 0.0056  160 MET A CE    
1284 N N     . LEU A 161 ? 0.1150 0.1365 0.1145 -0.0015 -0.0004 0.0063  161 LEU A N     
1285 C CA    . LEU A 161 ? 0.1054 0.1294 0.1057 -0.0021 -0.0014 0.0058  161 LEU A CA    
1286 C C     . LEU A 161 ? 0.1647 0.1899 0.1651 -0.0025 -0.0014 0.0058  161 LEU A C     
1287 O O     . LEU A 161 ? 0.3892 0.4138 0.3927 -0.0022 -0.0006 0.0058  161 LEU A O     
1288 C CB    . LEU A 161 ? 0.2024 0.2268 0.2060 -0.0021 -0.0005 0.0058  161 LEU A CB    
1289 C CG    . LEU A 161 ? 0.1218 0.1434 0.1214 -0.0016 -0.0004 0.0066  161 LEU A CG    
1290 C CD1   . LEU A 161 ? 0.2092 0.2301 0.2094 -0.0012 -0.0004 0.0075  161 LEU A CD1   
1291 C CD2   . LEU A 161 ? 0.0623 0.0864 0.0625 -0.0022 -0.0013 0.0057  161 LEU A CD2   
1292 N N     . LEU A 162 ? 0.0118 0.0424 0.0121 -0.0041 -0.0009 0.0055  162 LEU A N     
1293 C CA    . LEU A 162 ? 0.1037 0.1361 0.1040 -0.0049 -0.0006 0.0054  162 LEU A CA    
1294 C C     . LEU A 162 ? 0.3362 0.3683 0.3369 -0.0061 0.0011  0.0046  162 LEU A C     
1295 O O     . LEU A 162 ? 0.3883 0.4197 0.3891 -0.0070 0.0028  0.0036  162 LEU A O     
1296 C CB    . LEU A 162 ? 0.1408 0.1715 0.1423 -0.0058 0.0022  0.0040  162 LEU A CB    
1297 C CG    . LEU A 162 ? 0.1966 0.2249 0.1991 -0.0073 0.0063  0.0023  162 LEU A CG    
1298 C CD1   . LEU A 162 ? 0.4375 0.4640 0.4400 -0.0083 0.0095  0.0019  162 LEU A CD1   
1299 C CD2   . LEU A 162 ? 0.2581 0.2857 0.2614 -0.0073 0.0072  0.0019  162 LEU A CD2   
1300 N N     . CYS A 163 ? 0.2443 0.2769 0.2448 -0.0061 0.0007  0.0052  163 CYS A N     
1301 C CA    . CYS A 163 ? 0.1628 0.1944 0.1632 -0.0072 0.0030  0.0046  163 CYS A CA    
1302 C C     . CYS A 163 ? 0.2706 0.2991 0.2710 -0.0082 0.0069  0.0039  163 CYS A C     
1303 O O     . CYS A 163 ? 0.0209 0.0496 0.0217 -0.0077 0.0063  0.0043  163 CYS A O     
1304 C CB    . CYS A 163 ? 0.0148 0.0488 0.0150 -0.0064 0.0000  0.0060  163 CYS A CB    
1305 S SG    . CYS A 163 ? 0.2172 0.2504 0.2167 -0.0078 0.0020  0.0056  163 CYS A SG    
1306 N N     . SER A 164 ? 0.1919 0.2171 0.1913 -0.0091 0.0111  0.0033  164 SER A N     
1307 C CA    . SER A 164 ? 0.3541 0.3759 0.3524 -0.0094 0.0153  0.0035  164 SER A CA    
1308 C C     . SER A 164 ? 0.2942 0.3136 0.2896 -0.0097 0.0186  0.0042  164 SER A C     
1309 O O     . SER A 164 ? 0.1417 0.1605 0.1363 -0.0101 0.0198  0.0038  164 SER A O     
1310 C CB    . SER A 164 ? 0.2106 0.2320 0.2101 -0.0095 0.0167  0.0030  164 SER A CB    
1311 O OG    . SER A 164 ? 0.0797 0.0997 0.0787 -0.0096 0.0192  0.0035  164 SER A OG    
1312 N N     . PRO A 165 ? 0.1297 0.1476 0.1228 -0.0095 0.0198  0.0052  165 PRO A N     
1313 C CA    . PRO A 165 ? 0.0530 0.0713 0.0467 -0.0092 0.0185  0.0056  165 PRO A CA    
1314 C C     . PRO A 165 ? 0.2096 0.2317 0.2051 -0.0093 0.0136  0.0052  165 PRO A C     
1315 O O     . PRO A 165 ? 0.2536 0.2773 0.2494 -0.0095 0.0121  0.0049  165 PRO A O     
1316 C CB    . PRO A 165 ? 0.1527 0.1685 0.1423 -0.0088 0.0217  0.0072  165 PRO A CB    
1317 C CG    . PRO A 165 ? 0.2371 0.2518 0.2234 -0.0092 0.0232  0.0073  165 PRO A CG    
1318 C CD    . PRO A 165 ? 0.2558 0.2715 0.2444 -0.0098 0.0229  0.0060  165 PRO A CD    
1319 N N     . HIS A 166 ? 0.2115 0.2361 0.2085 -0.0088 0.0109  0.0056  166 HIS A N     
1320 C CA    . HIS A 166 ? 0.3143 0.3444 0.3135 -0.0078 0.0052  0.0064  166 HIS A CA    
1321 C C     . HIS A 166 ? 0.2598 0.2915 0.2588 -0.0077 0.0036  0.0073  166 HIS A C     
1322 O O     . HIS A 166 ? 0.3125 0.3441 0.3114 -0.0076 0.0038  0.0079  166 HIS A O     
1323 C CB    . HIS A 166 ? 0.1721 0.2040 0.1726 -0.0067 0.0027  0.0070  166 HIS A CB    
1324 C CG    . HIS A 166 ? 0.0741 0.1068 0.0754 -0.0046 -0.0014 0.0080  166 HIS A CG    
1325 N ND1   . HIS A 166 ? 0.0708 0.0997 0.0720 -0.0035 -0.0016 0.0074  166 HIS A ND1   
1326 C CD2   . HIS A 166 ? 0.1211 0.1489 0.1226 -0.0032 -0.0019 0.0077  166 HIS A CD2   
1327 C CE1   . HIS A 166 ? 0.1132 0.1394 0.1174 -0.0027 -0.0008 0.0070  166 HIS A CE1   
1328 N NE2   . HIS A 166 ? 0.1063 0.1303 0.1060 -0.0025 -0.0008 0.0081  166 HIS A NE2   
1329 N N     . ASN A 167 ? 0.3798 0.4135 0.3791 -0.0077 0.0019  0.0074  167 ASN A N     
1330 C CA    . ASN A 167 ? 0.3007 0.3372 0.3008 -0.0075 -0.0004 0.0083  167 ASN A CA    
1331 C C     . ASN A 167 ? 0.3207 0.3516 0.3221 -0.0047 -0.0022 0.0080  167 ASN A C     
1332 O O     . ASN A 167 ? 0.5198 0.5457 0.5188 -0.0037 -0.0010 0.0079  167 ASN A O     
1333 C CB    . ASN A 167 ? 0.2352 0.2714 0.2345 -0.0083 0.0001  0.0078  167 ASN A CB    
1334 C CG    . ASN A 167 ? 0.1914 0.2292 0.1917 -0.0080 -0.0019 0.0085  167 ASN A CG    
1335 O OD1   . ASN A 167 ? 0.2896 0.3244 0.2908 -0.0067 -0.0023 0.0087  167 ASN A OD1   
1336 N ND2   . ASN A 167 ? 0.1800 0.2189 0.1797 -0.0090 -0.0017 0.0082  167 ASN A ND2   
1337 N N     . PRO A 168 ? 0.1173 0.1461 0.1192 -0.0040 -0.0025 0.0081  168 PRO A N     
1338 C CA    . PRO A 168 ? 0.0143 0.0479 0.0164 -0.0055 -0.0023 0.0094  168 PRO A CA    
1339 C C     . PRO A 168 ? 0.1019 0.1399 0.1037 -0.0066 -0.0018 0.0107  168 PRO A C     
1340 O O     . PRO A 168 ? 0.0212 0.0559 0.0201 -0.0076 0.0013  0.0108  168 PRO A O     
1341 C CB    . PRO A 168 ? 0.2424 0.2696 0.2419 -0.0043 -0.0013 0.0096  168 PRO A CB    
1342 C CG    . PRO A 168 ? 0.2358 0.2617 0.2360 -0.0035 -0.0012 0.0099  168 PRO A CG    
1343 C CD    . PRO A 168 ? 0.0138 0.0394 0.0137 -0.0033 -0.0011 0.0093  168 PRO A CD    
1344 N N     . ILE A 169 ? 0.2308 0.2673 0.2328 -0.0057 -0.0018 0.0103  169 ILE A N     
1345 C CA    . ILE A 169 ? 0.3437 0.3795 0.3452 -0.0061 0.0000  0.0107  169 ILE A CA    
1346 C C     . ILE A 169 ? 0.3693 0.3974 0.3659 -0.0076 0.0066  0.0095  169 ILE A C     
1347 O O     . ILE A 169 ? 0.3399 0.3638 0.3335 -0.0079 0.0097  0.0098  169 ILE A O     
1348 C CB    . ILE A 169 ? 0.2703 0.3051 0.2728 -0.0046 -0.0016 0.0105  169 ILE A CB    
1349 C CG1   . ILE A 169 ? 0.1312 0.1662 0.1330 -0.0053 -0.0003 0.0098  169 ILE A CG1   
1350 C CG2   . ILE A 169 ? 0.2100 0.2354 0.2101 -0.0029 -0.0010 0.0094  169 ILE A CG2   
1351 C CD1   . ILE A 169 ? 0.2115 0.2437 0.2137 -0.0038 -0.0015 0.0093  169 ILE A CD1   
1352 N N     . GLY A 170 ? 0.3690 0.3943 0.3638 -0.0082 0.0091  0.0086  170 GLY A N     
1353 C CA    . GLY A 170 ? 0.1803 0.1979 0.1700 -0.0086 0.0153  0.0085  170 GLY A CA    
1354 C C     . GLY A 170 ? 0.1446 0.1607 0.1352 -0.0083 0.0176  0.0082  170 GLY A C     
1355 O O     . GLY A 170 ? 0.0481 0.0613 0.0360 -0.0073 0.0218  0.0097  170 GLY A O     
1356 N N     . ARG A 171 ? 0.0785 0.0988 0.0733 -0.0084 0.0142  0.0073  171 ARG A N     
1357 C CA    . ARG A 171 ? 0.0360 0.0546 0.0316 -0.0083 0.0164  0.0069  171 ARG A CA    
1358 C C     . ARG A 171 ? 0.2028 0.2197 0.1976 -0.0082 0.0193  0.0071  171 ARG A C     
1359 O O     . ARG A 171 ? 0.4106 0.4288 0.4059 -0.0085 0.0179  0.0063  171 ARG A O     
1360 C CB    . ARG A 171 ? 0.1547 0.1778 0.1535 -0.0079 0.0118  0.0065  171 ARG A CB    
1361 C CG    . ARG A 171 ? 0.3104 0.3347 0.3101 -0.0073 0.0103  0.0070  171 ARG A CG    
1362 C CD    . ARG A 171 ? 0.5535 0.5729 0.5517 -0.0078 0.0155  0.0070  171 ARG A CD    
1363 N NE    . ARG A 171 ? 0.0370 0.0541 0.0353 -0.0076 0.0192  0.0071  171 ARG A NE    
1364 C CZ    . ARG A 171 ? 0.1191 0.1370 0.1193 -0.0075 0.0186  0.0065  171 ARG A CZ    
1365 N NH1   . ARG A 171 ? 0.0297 0.0502 0.0311 -0.0075 0.0148  0.0059  171 ARG A NH1   
1366 N NH2   . ARG A 171 ? 0.4194 0.4380 0.4201 -0.0075 0.0207  0.0071  171 ARG A NH2   
1367 N N     . VAL A 172 ? 0.2986 0.3152 0.2922 -0.0080 0.0222  0.0082  172 VAL A N     
1368 C CA    . VAL A 172 ? 0.0490 0.0658 0.0417 -0.0092 0.0239  0.0073  172 VAL A CA    
1369 C C     . VAL A 172 ? 0.2632 0.2809 0.2587 -0.0093 0.0235  0.0065  172 VAL A C     
1370 O O     . VAL A 172 ? 0.3257 0.3428 0.3208 -0.0098 0.0246  0.0064  172 VAL A O     
1371 C CB    . VAL A 172 ? 0.0574 0.0706 0.0449 -0.0107 0.0273  0.0069  172 VAL A CB    
1372 C CG1   . VAL A 172 ? 0.0624 0.0724 0.0488 -0.0120 0.0299  0.0052  172 VAL A CG1   
1373 C CG2   . VAL A 172 ? 0.2724 0.2844 0.2562 -0.0105 0.0275  0.0077  172 VAL A CG2   
1374 N N     . TRP A 173 ? 0.2790 0.2976 0.2769 -0.0090 0.0219  0.0057  173 TRP A N     
1375 C CA    . TRP A 173 ? 0.2963 0.3157 0.2964 -0.0090 0.0212  0.0050  173 TRP A CA    
1376 C C     . TRP A 173 ? 0.2382 0.2562 0.2371 -0.0105 0.0242  0.0039  173 TRP A C     
1377 O O     . TRP A 173 ? 0.3463 0.3619 0.3431 -0.0117 0.0265  0.0030  173 TRP A O     
1378 C CB    . TRP A 173 ? 0.3637 0.3840 0.3655 -0.0087 0.0189  0.0041  173 TRP A CB    
1379 C CG    . TRP A 173 ? 0.4508 0.4723 0.4525 -0.0084 0.0155  0.0039  173 TRP A CG    
1380 C CD1   . TRP A 173 ? 0.3088 0.3313 0.3101 -0.0085 0.0142  0.0037  173 TRP A CD1   
1381 C CD2   . TRP A 173 ? 0.4164 0.4400 0.4184 -0.0079 0.0121  0.0042  173 TRP A CD2   
1382 N NE1   . TRP A 173 ? 0.2587 0.2841 0.2600 -0.0080 0.0100  0.0041  173 TRP A NE1   
1383 C CE2   . TRP A 173 ? 0.3093 0.3357 0.3110 -0.0074 0.0084  0.0047  173 TRP A CE2   
1384 C CE3   . TRP A 173 ? 0.3841 0.4079 0.3865 -0.0075 0.0114  0.0045  173 TRP A CE3   
1385 C CZ2   . TRP A 173 ? 0.3803 0.4100 0.3820 -0.0061 0.0041  0.0061  173 TRP A CZ2   
1386 C CZ3   . TRP A 173 ? 0.4553 0.4823 0.4577 -0.0065 0.0071  0.0056  173 TRP A CZ3   
1387 C CH2   . TRP A 173 ? 0.4673 0.4972 0.4693 -0.0056 0.0035  0.0066  173 TRP A CH2   
1388 N N     . THR A 174 ? 0.3804 0.3983 0.3803 -0.0107 0.0244  0.0036  174 THR A N     
1389 C CA    . THR A 174 ? 0.1458 0.1606 0.1448 -0.0122 0.0275  0.0019  174 THR A CA    
1390 C C     . THR A 174 ? 0.1642 0.1794 0.1647 -0.0125 0.0274  0.0007  174 THR A C     
1391 O O     . THR A 174 ? 0.2838 0.3018 0.2861 -0.0115 0.0246  0.0012  174 THR A O     
1392 C CB    . THR A 174 ? 0.0783 0.0931 0.0783 -0.0122 0.0277  0.0019  174 THR A CB    
1393 O OG1   . THR A 174 ? 0.1071 0.1252 0.1099 -0.0111 0.0247  0.0023  174 THR A OG1   
1394 C CG2   . THR A 174 ? 0.0513 0.0659 0.0499 -0.0118 0.0278  0.0031  174 THR A CG2   
1395 N N     . LYS A 175 ? 0.2752 0.2869 0.2751 -0.0139 0.0305  -0.0009 175 LYS A N     
1396 C CA    . LYS A 175 ? 0.1804 0.1924 0.1818 -0.0142 0.0305  -0.0021 175 LYS A CA    
1397 C C     . LYS A 175 ? 0.2559 0.2710 0.2600 -0.0135 0.0280  -0.0021 175 LYS A C     
1398 O O     . LYS A 175 ? 0.3994 0.4164 0.4047 -0.0130 0.0262  -0.0022 175 LYS A O     
1399 C CB    . LYS A 175 ? 0.3284 0.3357 0.3288 -0.0157 0.0347  -0.0038 175 LYS A CB    
1400 C CG    . LYS A 175 ? 0.2275 0.2349 0.2295 -0.0162 0.0350  -0.0052 175 LYS A CG    
1401 C CD    . LYS A 175 ? 0.1276 0.1297 0.1281 -0.0175 0.0394  -0.0066 175 LYS A CD    
1402 C CE    . LYS A 175 ? 0.2345 0.2364 0.2371 -0.0181 0.0402  -0.0081 175 LYS A CE    
1403 N NZ    . LYS A 175 ? 0.0782 0.0747 0.0792 -0.0193 0.0446  -0.0092 175 LYS A NZ    
1404 N N     . GLU A 176 ? 0.2384 0.2537 0.2429 -0.0133 0.0278  -0.0018 176 GLU A N     
1405 C CA    . GLU A 176 ? 0.1740 0.1916 0.1805 -0.0126 0.0257  -0.0017 176 GLU A CA    
1406 C C     . GLU A 176 ? 0.2068 0.2275 0.2140 -0.0109 0.0220  -0.0002 176 GLU A C     
1407 O O     . GLU A 176 ? 0.2737 0.2956 0.2820 -0.0104 0.0204  -0.0004 176 GLU A O     
1408 C CB    . GLU A 176 ? 0.1682 0.1854 0.1749 -0.0126 0.0261  -0.0016 176 GLU A CB    
1409 C CG    . GLU A 176 ? 0.3562 0.3692 0.3619 -0.0141 0.0301  -0.0029 176 GLU A CG    
1410 C CD    . GLU A 176 ? 0.3863 0.3975 0.3899 -0.0141 0.0314  -0.0019 176 GLU A CD    
1411 O OE1   . GLU A 176 ? 0.2347 0.2481 0.2385 -0.0131 0.0293  -0.0005 176 GLU A OE1   
1412 O OE2   . GLU A 176 ? 0.3479 0.3552 0.3493 -0.0150 0.0345  -0.0025 176 GLU A OE2   
1413 N N     . GLU A 177 ? 0.3049 0.3261 0.3114 -0.0100 0.0208  0.0012  177 GLU A N     
1414 C CA    . GLU A 177 ? 0.1582 0.1805 0.1651 -0.0086 0.0178  0.0021  177 GLU A CA    
1415 C C     . GLU A 177 ? 0.3895 0.4121 0.3964 -0.0087 0.0171  0.0015  177 GLU A C     
1416 O O     . GLU A 177 ? 0.3956 0.4190 0.4029 -0.0082 0.0150  0.0013  177 GLU A O     
1417 C CB    . GLU A 177 ? 0.2961 0.3179 0.3021 -0.0082 0.0172  0.0030  177 GLU A CB    
1418 C CG    . GLU A 177 ? 0.0294 0.0509 0.0356 -0.0077 0.0167  0.0036  177 GLU A CG    
1419 C CD    . GLU A 177 ? 0.0305 0.0512 0.0354 -0.0077 0.0173  0.0044  177 GLU A CD    
1420 O OE1   . GLU A 177 ? 0.1494 0.1698 0.1532 -0.0081 0.0195  0.0049  177 GLU A OE1   
1421 O OE2   . GLU A 177 ? 0.1539 0.1752 0.1583 -0.0074 0.0148  0.0044  177 GLU A OE2   
1422 N N     . LEU A 178 ? 0.3289 0.3509 0.3351 -0.0096 0.0190  0.0012  178 LEU A N     
1423 C CA    . LEU A 178 ? 0.0987 0.1211 0.1050 -0.0097 0.0185  0.0006  178 LEU A CA    
1424 C C     . LEU A 178 ? 0.2498 0.2723 0.2571 -0.0101 0.0189  -0.0005 178 LEU A C     
1425 O O     . LEU A 178 ? 0.4347 0.4581 0.4424 -0.0096 0.0174  -0.0005 178 LEU A O     
1426 C CB    . LEU A 178 ? 0.0629 0.0840 0.0678 -0.0106 0.0207  0.0003  178 LEU A CB    
1427 C CG    . LEU A 178 ? 0.1219 0.1429 0.1256 -0.0102 0.0202  0.0014  178 LEU A CG    
1428 C CD1   . LEU A 178 ? 0.0422 0.0612 0.0438 -0.0112 0.0232  0.0012  178 LEU A CD1   
1429 C CD2   . LEU A 178 ? 0.2515 0.2732 0.2552 -0.0097 0.0185  0.0014  178 LEU A CD2   
1430 N N     . ILE A 179 ? 0.1142 0.1357 0.1217 -0.0111 0.0211  -0.0015 179 ILE A N     
1431 C CA    . ILE A 179 ? 0.2522 0.2739 0.2609 -0.0115 0.0214  -0.0026 179 ILE A CA    
1432 C C     . ILE A 179 ? 0.3234 0.3469 0.3328 -0.0102 0.0185  -0.0017 179 ILE A C     
1433 O O     . ILE A 179 ? 0.4965 0.5208 0.5064 -0.0099 0.0175  -0.0020 179 ILE A O     
1434 C CB    . ILE A 179 ? 0.2579 0.2775 0.2668 -0.0128 0.0242  -0.0040 179 ILE A CB    
1435 C CG1   . ILE A 179 ? 0.1211 0.1374 0.1290 -0.0143 0.0277  -0.0054 179 ILE A CG1   
1436 C CG2   . ILE A 179 ? 0.1210 0.1413 0.1312 -0.0129 0.0239  -0.0049 179 ILE A CG2   
1437 C CD1   . ILE A 179 ? 0.2491 0.2652 0.2577 -0.0148 0.0283  -0.0065 179 ILE A CD1   
1438 N N     . LYS A 180 ? 0.4337 0.4574 0.4428 -0.0094 0.0172  -0.0007 180 LYS A N     
1439 C CA    . LYS A 180 ? 0.4784 0.5030 0.4876 -0.0083 0.0146  -0.0002 180 LYS A CA    
1440 C C     . LYS A 180 ? 0.3669 0.3924 0.3750 -0.0075 0.0119  0.0003  180 LYS A C     
1441 O O     . LYS A 180 ? 0.6065 0.6329 0.6140 -0.0069 0.0098  0.0004  180 LYS A O     
1442 C CB    . LYS A 180 ? 0.0246 0.0490 0.0335 -0.0079 0.0140  0.0005  180 LYS A CB    
1443 C CG    . LYS A 180 ? 0.1057 0.1309 0.1143 -0.0072 0.0118  0.0007  180 LYS A CG    
1444 C CD    . LYS A 180 ? 0.0965 0.1217 0.1043 -0.0068 0.0106  0.0015  180 LYS A CD    
1445 C CE    . LYS A 180 ? 0.2489 0.2746 0.2565 -0.0064 0.0095  0.0016  180 LYS A CE    
1446 N NZ    . LYS A 180 ? 0.1518 0.1789 0.1584 -0.0058 0.0073  0.0017  180 LYS A NZ    
1447 N N     . LEU A 181 ? 0.3371 0.3623 0.3445 -0.0075 0.0117  0.0007  181 LEU A N     
1448 C CA    . LEU A 181 ? 0.3548 0.3813 0.3609 -0.0068 0.0088  0.0012  181 LEU A CA    
1449 C C     . LEU A 181 ? 0.1151 0.1416 0.1217 -0.0070 0.0094  0.0006  181 LEU A C     
1450 O O     . LEU A 181 ? 0.2501 0.2777 0.2558 -0.0062 0.0071  0.0012  181 LEU A O     
1451 C CB    . LEU A 181 ? 0.2651 0.2916 0.2704 -0.0068 0.0085  0.0017  181 LEU A CB    
1452 C CG    . LEU A 181 ? 0.1012 0.1290 0.1053 -0.0060 0.0059  0.0024  181 LEU A CG    
1453 C CD1   . LEU A 181 ? 0.0133 0.0427 0.0157 -0.0044 0.0021  0.0042  181 LEU A CD1   
1454 C CD2   . LEU A 181 ? 0.0394 0.0673 0.0431 -0.0063 0.0059  0.0026  181 LEU A CD2   
1455 N N     . GLY A 182 ? 0.2205 0.2460 0.2283 -0.0079 0.0124  -0.0002 182 GLY A N     
1456 C CA    . GLY A 182 ? 0.0238 0.0495 0.0322 -0.0082 0.0130  -0.0008 182 GLY A CA    
1457 C C     . GLY A 182 ? 0.0752 0.1016 0.0841 -0.0079 0.0122  -0.0010 182 GLY A C     
1458 O O     . GLY A 182 ? 0.0251 0.0520 0.0339 -0.0075 0.0114  -0.0010 182 GLY A O     
1459 N N     . SER A 183 ? 0.2160 0.2422 0.2252 -0.0080 0.0127  -0.0012 183 SER A N     
1460 C CA    . SER A 183 ? 0.0222 0.0492 0.0318 -0.0078 0.0121  -0.0014 183 SER A CA    
1461 C C     . SER A 183 ? 0.0187 0.0467 0.0266 -0.0066 0.0089  -0.0004 183 SER A C     
1462 O O     . SER A 183 ? 0.1093 0.1380 0.1171 -0.0063 0.0082  -0.0004 183 SER A O     
1463 C CB    . SER A 183 ? 0.1544 0.1811 0.1646 -0.0082 0.0130  -0.0018 183 SER A CB    
1464 O OG    . SER A 183 ? 0.1040 0.1302 0.1154 -0.0095 0.0158  -0.0031 183 SER A OG    
1465 N N     . LEU A 184 ? 0.2793 0.3077 0.2856 -0.0058 0.0067  0.0008  184 LEU A N     
1466 C CA    . LEU A 184 ? 0.2353 0.2648 0.2393 -0.0044 0.0034  0.0026  184 LEU A CA    
1467 C C     . LEU A 184 ? 0.2385 0.2683 0.2420 -0.0040 0.0027  0.0031  184 LEU A C     
1468 O O     . LEU A 184 ? 0.3654 0.3957 0.3676 -0.0029 0.0011  0.0043  184 LEU A O     
1469 C CB    . LEU A 184 ? 0.3328 0.3628 0.3350 -0.0034 0.0012  0.0042  184 LEU A CB    
1470 C CG    . LEU A 184 ? 0.2142 0.2442 0.2161 -0.0032 0.0009  0.0045  184 LEU A CG    
1471 C CD1   . LEU A 184 ? 0.3019 0.3310 0.3063 -0.0047 0.0041  0.0023  184 LEU A CD1   
1472 C CD2   . LEU A 184 ? 0.1144 0.1438 0.1152 -0.0024 -0.0005 0.0058  184 LEU A CD2   
1473 N N     . CYS A 185 ? 0.1253 0.1544 0.1298 -0.0048 0.0043  0.0021  185 CYS A N     
1474 C CA    . CYS A 185 ? 0.2128 0.2420 0.2171 -0.0046 0.0040  0.0023  185 CYS A CA    
1475 C C     . CYS A 185 ? 0.4255 0.4546 0.4312 -0.0050 0.0055  0.0014  185 CYS A C     
1476 O O     . CYS A 185 ? 0.6603 0.6899 0.6654 -0.0043 0.0043  0.0022  185 CYS A O     
1477 C CB    . CYS A 185 ? 0.3253 0.3539 0.3305 -0.0054 0.0055  0.0015  185 CYS A CB    
1478 S SG    . CYS A 185 ? 0.6244 0.6536 0.6279 -0.0047 0.0033  0.0029  185 CYS A SG    
1479 N N     . THR A 186 ? 0.2043 0.2328 0.2118 -0.0061 0.0080  0.0000  186 THR A N     
1480 C CA    . THR A 186 ? 0.1827 0.2114 0.1916 -0.0064 0.0092  -0.0008 186 THR A CA    
1481 C C     . THR A 186 ? 0.2736 0.3032 0.2815 -0.0056 0.0073  0.0000  186 THR A C     
1482 O O     . THR A 186 ? 0.5076 0.5378 0.5156 -0.0052 0.0070  0.0002  186 THR A O     
1483 C CB    . THR A 186 ? 0.0219 0.0500 0.0323 -0.0076 0.0119  -0.0020 186 THR A CB    
1484 O OG1   . THR A 186 ? 0.0243 0.0516 0.0352 -0.0084 0.0138  -0.0026 186 THR A OG1   
1485 C CG2   . THR A 186 ? 0.0229 0.0516 0.0344 -0.0079 0.0128  -0.0028 186 THR A CG2   
1486 N N     . LYS A 187 ? 0.3973 0.4272 0.4041 -0.0052 0.0062  0.0005  187 LYS A N     
1487 C CA    . LYS A 187 ? 0.2891 0.3200 0.2948 -0.0044 0.0046  0.0014  187 LYS A CA    
1488 C C     . LYS A 187 ? 0.2149 0.2463 0.2184 -0.0029 0.0021  0.0035  187 LYS A C     
1489 O O     . LYS A 187 ? 0.3798 0.4119 0.3827 -0.0023 0.0014  0.0043  187 LYS A O     
1490 C CB    . LYS A 187 ? 0.2225 0.2535 0.2274 -0.0042 0.0038  0.0018  187 LYS A CB    
1491 C CG    . LYS A 187 ? 0.1069 0.1388 0.1094 -0.0028 0.0013  0.0038  187 LYS A CG    
1492 C CD    . LYS A 187 ? 0.0630 0.0955 0.0659 -0.0030 0.0017  0.0032  187 LYS A CD    
1493 C CE    . LYS A 187 ? 0.1803 0.2132 0.1809 -0.0018 -0.0003 0.0050  187 LYS A CE    
1494 N NZ    . LYS A 187 ? 0.2505 0.2833 0.2511 -0.0021 -0.0003 0.0047  187 LYS A NZ    
1495 N N     . VAL A 190 ? 0.2743 0.3042 0.2770 -0.0023 0.0012  0.0050  190 VAL A N     
1496 C CA    . VAL A 190 ? 0.2795 0.3093 0.2811 -0.0018 0.0000  0.0060  190 VAL A CA    
1497 C C     . VAL A 190 ? 0.1719 0.2014 0.1751 -0.0032 0.0020  0.0041  190 VAL A C     
1498 O O     . VAL A 190 ? 0.0259 0.0549 0.0306 -0.0045 0.0042  0.0024  190 VAL A O     
1499 C CB    . VAL A 190 ? 0.1365 0.1642 0.1376 -0.0014 -0.0005 0.0064  190 VAL A CB    
1500 C CG1   . VAL A 190 ? 0.0131 0.0384 0.0141 -0.0011 -0.0007 0.0064  190 VAL A CG1   
1501 C CG2   . VAL A 190 ? 0.0100 0.0332 0.0109 -0.0004 -0.0008 0.0066  190 VAL A CG2   
1502 N N     . ILE A 191 ? 0.0119 0.0414 0.0147 -0.0028 0.0015  0.0046  191 ILE A N     
1503 C CA    . ILE A 191 ? 0.1269 0.1561 0.1308 -0.0040 0.0031  0.0032  191 ILE A CA    
1504 C C     . ILE A 191 ? 0.2138 0.2433 0.2169 -0.0041 0.0025  0.0034  191 ILE A C     
1505 O O     . ILE A 191 ? 0.4610 0.4910 0.4625 -0.0030 0.0002  0.0051  191 ILE A O     
1506 C CB    . ILE A 191 ? 0.2269 0.2560 0.2308 -0.0035 0.0027  0.0037  191 ILE A CB    
1507 C CG1   . ILE A 191 ? 0.2944 0.3233 0.2990 -0.0032 0.0031  0.0038  191 ILE A CG1   
1508 C CG2   . ILE A 191 ? 0.1878 0.2166 0.1926 -0.0047 0.0044  0.0022  191 ILE A CG2   
1509 C CD1   . ILE A 191 ? 0.0997 0.1282 0.1051 -0.0032 0.0037  0.0037  191 ILE A CD1   
1510 N N     . VAL A 192 ? 0.1896 0.2184 0.1937 -0.0055 0.0048  0.0018  192 VAL A N     
1511 C CA    . VAL A 192 ? 0.0158 0.0447 0.0194 -0.0059 0.0047  0.0018  192 VAL A CA    
1512 C C     . VAL A 192 ? 0.2169 0.2456 0.2206 -0.0066 0.0057  0.0012  192 VAL A C     
1513 O O     . VAL A 192 ? 0.4088 0.4365 0.4135 -0.0075 0.0082  0.0001  192 VAL A O     
1514 C CB    . VAL A 192 ? 0.1626 0.1906 0.1672 -0.0068 0.0070  0.0009  192 VAL A CB    
1515 C CG1   . VAL A 192 ? 0.0886 0.1163 0.0929 -0.0073 0.0077  0.0009  192 VAL A CG1   
1516 C CG2   . VAL A 192 ? 0.0166 0.0449 0.0210 -0.0061 0.0058  0.0015  192 VAL A CG2   
1517 N N     . VAL A 193 ? 0.0358 0.0655 0.0384 -0.0061 0.0038  0.0021  193 VAL A N     
1518 C CA    . VAL A 193 ? 0.1422 0.1719 0.1447 -0.0069 0.0047  0.0016  193 VAL A CA    
1519 C C     . VAL A 193 ? 0.1643 0.1937 0.1666 -0.0075 0.0055  0.0015  193 VAL A C     
1520 O O     . VAL A 193 ? 0.1578 0.1882 0.1594 -0.0067 0.0034  0.0026  193 VAL A O     
1521 C CB    . VAL A 193 ? 0.1136 0.1446 0.1151 -0.0060 0.0022  0.0027  193 VAL A CB    
1522 C CG1   . VAL A 193 ? 0.0161 0.0470 0.0177 -0.0070 0.0034  0.0018  193 VAL A CG1   
1523 C CG2   . VAL A 193 ? 0.0133 0.0440 0.0148 -0.0050 0.0014  0.0033  193 VAL A CG2   
1524 N N     . ALA A 194 ? 0.1940 0.2216 0.1965 -0.0087 0.0088  0.0006  194 ALA A N     
1525 C CA    . ALA A 194 ? 0.0689 0.0953 0.0710 -0.0092 0.0106  0.0007  194 ALA A CA    
1526 C C     . ALA A 194 ? 0.0263 0.0524 0.0272 -0.0097 0.0112  0.0008  194 ALA A C     
1527 O O     . ALA A 194 ? 0.0969 0.1215 0.0970 -0.0105 0.0137  0.0004  194 ALA A O     
1528 C CB    . ALA A 194 ? 0.0316 0.0558 0.0339 -0.0099 0.0142  0.0002  194 ALA A CB    
1529 N N     . ASP A 195 ? 0.3609 0.3887 0.3614 -0.0093 0.0088  0.0015  195 ASP A N     
1530 C CA    . ASP A 195 ? 0.3046 0.3323 0.3040 -0.0098 0.0092  0.0017  195 ASP A CA    
1531 C C     . ASP A 195 ? 0.0935 0.1182 0.0913 -0.0103 0.0126  0.0021  195 ASP A C     
1532 O O     . ASP A 195 ? 0.0446 0.0698 0.0423 -0.0100 0.0118  0.0027  195 ASP A O     
1533 C CB    . ASP A 195 ? 0.0203 0.0513 0.0199 -0.0089 0.0048  0.0027  195 ASP A CB    
1534 C CG    . ASP A 195 ? 0.2333 0.2647 0.2321 -0.0094 0.0049  0.0028  195 ASP A CG    
1535 O OD1   . ASP A 195 ? 0.1370 0.1652 0.1341 -0.0104 0.0088  0.0024  195 ASP A OD1   
1536 O OD2   . ASP A 195 ? 0.2398 0.2741 0.2388 -0.0086 0.0015  0.0037  195 ASP A OD2   
1537 N N     . GLU A 196 ? 0.2092 0.2310 0.2051 -0.0108 0.0165  0.0020  196 GLU A N     
1538 C CA    . GLU A 196 ? 0.3231 0.3419 0.3160 -0.0109 0.0200  0.0028  196 GLU A CA    
1539 C C     . GLU A 196 ? 0.1943 0.2111 0.1832 -0.0111 0.0217  0.0034  196 GLU A C     
1540 O O     . GLU A 196 ? 0.2873 0.3012 0.2721 -0.0116 0.0248  0.0034  196 GLU A O     
1541 C CB    . GLU A 196 ? 0.2821 0.2995 0.2746 -0.0116 0.0226  0.0022  196 GLU A CB    
1542 C CG    . GLU A 196 ? 0.2454 0.2643 0.2412 -0.0113 0.0213  0.0016  196 GLU A CG    
1543 C CD    . GLU A 196 ? 0.0770 0.0944 0.0725 -0.0122 0.0237  0.0006  196 GLU A CD    
1544 O OE1   . GLU A 196 ? 0.0436 0.0623 0.0416 -0.0120 0.0227  0.0001  196 GLU A OE1   
1545 O OE2   . GLU A 196 ? 0.0534 0.0678 0.0460 -0.0133 0.0268  0.0001  196 GLU A OE2   
1546 N N     . ILE A 197 ? 0.0450 0.0629 0.0341 -0.0109 0.0195  0.0035  197 ILE A N     
1547 C CA    . ILE A 197 ? 0.0504 0.0661 0.0349 -0.0109 0.0210  0.0042  197 ILE A CA    
1548 C C     . ILE A 197 ? 0.3335 0.3463 0.3130 -0.0103 0.0232  0.0055  197 ILE A C     
1549 O O     . ILE A 197 ? 0.3604 0.3701 0.3336 -0.0104 0.0253  0.0059  197 ILE A O     
1550 C CB    . ILE A 197 ? 0.0448 0.0632 0.0313 -0.0111 0.0176  0.0038  197 ILE A CB    
1551 C CG1   . ILE A 197 ? 0.1666 0.1824 0.1480 -0.0109 0.0191  0.0042  197 ILE A CG1   
1552 C CG2   . ILE A 197 ? 0.0397 0.0608 0.0284 -0.0110 0.0145  0.0041  197 ILE A CG2   
1553 C CD1   . ILE A 197 ? 0.0693 0.0878 0.0523 -0.0113 0.0158  0.0040  197 ILE A CD1   
1554 N N     . HIS A 198 ? 0.2762 0.2898 0.2577 -0.0100 0.0227  0.0059  198 HIS A N     
1555 C CA    . HIS A 198 ? 0.3501 0.3615 0.3273 -0.0098 0.0246  0.0070  198 HIS A CA    
1556 C C     . HIS A 198 ? 0.1112 0.1204 0.0867 -0.0108 0.0273  0.0064  198 HIS A C     
1557 O O     . HIS A 198 ? 0.1568 0.1639 0.1297 -0.0110 0.0286  0.0068  198 HIS A O     
1558 C CB    . HIS A 198 ? 0.2302 0.2428 0.2100 -0.0090 0.0226  0.0077  198 HIS A CB    
1559 C CG    . HIS A 198 ? 0.1875 0.2010 0.1683 -0.0091 0.0198  0.0074  198 HIS A CG    
1560 N ND1   . HIS A 198 ? 0.2473 0.2583 0.2226 -0.0085 0.0204  0.0084  198 HIS A ND1   
1561 C CD2   . HIS A 198 ? 0.1399 0.1585 0.1266 -0.0100 0.0153  0.0062  198 HIS A CD2   
1562 C CE1   . HIS A 198 ? 0.2550 0.2687 0.2333 -0.0093 0.0168  0.0077  198 HIS A CE1   
1563 N NE2   . HIS A 198 ? 0.2292 0.2491 0.2151 -0.0102 0.0133  0.0066  198 HIS A NE2   
1564 N N     . SER A 199 ? 0.0668 0.0756 0.0436 -0.0116 0.0283  0.0052  199 SER A N     
1565 C CA    . SER A 199 ? 0.1929 0.1991 0.1693 -0.0126 0.0308  0.0042  199 SER A CA    
1566 C C     . SER A 199 ? 0.1872 0.1862 0.1562 -0.0133 0.0347  0.0041  199 SER A C     
1567 O O     . SER A 199 ? 0.2035 0.1995 0.1721 -0.0139 0.0370  0.0034  199 SER A O     
1568 C CB    . SER A 199 ? 0.1493 0.1561 0.1283 -0.0132 0.0310  0.0029  199 SER A CB    
1569 O OG    . SER A 199 ? 0.2704 0.2740 0.2452 -0.0136 0.0328  0.0026  199 SER A OG    
1570 N N     . ASP A 200 ? 0.3419 0.3372 0.3046 -0.0130 0.0356  0.0047  200 ASP A N     
1571 C CA    . ASP A 200 ? 0.3120 0.2986 0.2662 -0.0132 0.0395  0.0046  200 ASP A CA    
1572 C C     . ASP A 200 ? 0.3286 0.3117 0.2774 -0.0125 0.0399  0.0057  200 ASP A C     
1573 O O     . ASP A 200 ? 0.2551 0.2300 0.1961 -0.0123 0.0432  0.0058  200 ASP A O     
1574 C CB    . ASP A 200 ? 0.3652 0.3479 0.3140 -0.0131 0.0408  0.0043  200 ASP A CB    
1575 C CG    . ASP A 200 ? 0.4413 0.4243 0.3931 -0.0139 0.0420  0.0031  200 ASP A CG    
1576 O OD1   . ASP A 200 ? 0.4827 0.4647 0.4370 -0.0146 0.0437  0.0023  200 ASP A OD1   
1577 O OD2   . ASP A 200 ? 0.5586 0.5426 0.5101 -0.0139 0.0412  0.0028  200 ASP A OD2   
1578 N N     . ILE A 201 ? 0.4557 0.4444 0.4081 -0.0120 0.0367  0.0067  201 ILE A N     
1579 C CA    . ILE A 201 ? 0.3207 0.3064 0.2685 -0.0114 0.0370  0.0077  201 ILE A CA    
1580 C C     . ILE A 201 ? 0.3369 0.3262 0.2905 -0.0117 0.0364  0.0078  201 ILE A C     
1581 O O     . ILE A 201 ? 0.3294 0.3257 0.2893 -0.0113 0.0331  0.0084  201 ILE A O     
1582 C CB    . ILE A 201 ? 0.2001 0.1884 0.1464 -0.0105 0.0339  0.0088  201 ILE A CB    
1583 C CG1   . ILE A 201 ? 0.1627 0.1461 0.1016 -0.0102 0.0346  0.0086  201 ILE A CG1   
1584 C CG2   . ILE A 201 ? 0.4213 0.4062 0.3627 -0.0100 0.0341  0.0098  201 ILE A CG2   
1585 C CD1   . ILE A 201 ? 0.1814 0.1551 0.1086 -0.0092 0.0365  0.0091  201 ILE A CD1   
1586 N N     . ILE A 202 ? 0.2736 0.2579 0.2253 -0.0122 0.0397  0.0072  202 ILE A N     
1587 C CA    . ILE A 202 ? 0.3160 0.3028 0.2727 -0.0125 0.0395  0.0070  202 ILE A CA    
1588 C C     . ILE A 202 ? 0.3362 0.3158 0.2868 -0.0122 0.0426  0.0074  202 ILE A C     
1589 O O     . ILE A 202 ? 0.3443 0.3156 0.2871 -0.0120 0.0460  0.0074  202 ILE A O     
1590 C CB    . ILE A 202 ? 0.1524 0.1402 0.1137 -0.0133 0.0405  0.0056  202 ILE A CB    
1591 C CG1   . ILE A 202 ? 0.1263 0.1200 0.0926 -0.0133 0.0377  0.0052  202 ILE A CG1   
1592 C CG2   . ILE A 202 ? 0.0930 0.0838 0.0595 -0.0134 0.0399  0.0053  202 ILE A CG2   
1593 C CD1   . ILE A 202 ? 0.0779 0.0795 0.0511 -0.0126 0.0335  0.0057  202 ILE A CD1   
1594 N N     . TYR A 203 ? 0.1674 0.1497 0.1212 -0.0121 0.0416  0.0078  203 TYR A N     
1595 C CA    . TYR A 203 ? 0.2549 0.2305 0.2027 -0.0117 0.0442  0.0084  203 TYR A CA    
1596 C C     . TYR A 203 ? 0.2878 0.2583 0.2353 -0.0122 0.0482  0.0074  203 TYR A C     
1597 O O     . TYR A 203 ? 0.3184 0.2912 0.2707 -0.0130 0.0484  0.0063  203 TYR A O     
1598 C CB    . TYR A 203 ? 0.2671 0.2477 0.2180 -0.0114 0.0414  0.0094  203 TYR A CB    
1599 C CG    . TYR A 203 ? 0.2482 0.2325 0.1985 -0.0108 0.0380  0.0105  203 TYR A CG    
1600 C CD1   . TYR A 203 ? 0.1113 0.0921 0.0558 -0.0104 0.0383  0.0107  203 TYR A CD1   
1601 C CD2   . TYR A 203 ? 0.3911 0.3820 0.3462 -0.0104 0.0346  0.0115  203 TYR A CD2   
1602 C CE1   . TYR A 203 ? 0.1103 0.0943 0.0540 -0.0098 0.0351  0.0116  203 TYR A CE1   
1603 C CE2   . TYR A 203 ? 0.3924 0.3867 0.3472 -0.0098 0.0317  0.0125  203 TYR A CE2   
1604 C CZ    . TYR A 203 ? 0.2519 0.2427 0.2011 -0.0095 0.0319  0.0126  203 TYR A CZ    
1605 O OH    . TYR A 203 ? 0.2247 0.2186 0.1736 -0.0089 0.0289  0.0136  203 TYR A OH    
1606 N N     . ALA A 204 ? 0.1822 0.1453 0.1236 -0.0117 0.0513  0.0079  204 ALA A N     
1607 C CA    . ALA A 204 ? 0.1531 0.1095 0.0925 -0.0120 0.0559  0.0072  204 ALA A CA    
1608 C C     . ALA A 204 ? 0.3447 0.3059 0.2922 -0.0129 0.0554  0.0061  204 ALA A C     
1609 O O     . ALA A 204 ? 0.4729 0.4318 0.4218 -0.0135 0.0579  0.0049  204 ALA A O     
1610 C CB    . ALA A 204 ? 0.1524 0.1001 0.0837 -0.0109 0.0592  0.0081  204 ALA A CB    
1611 N N     . ASP A 205 ? 0.1233 0.0911 0.0760 -0.0129 0.0521  0.0064  205 ASP A N     
1612 C CA    . ASP A 205 ? 0.1166 0.0885 0.0760 -0.0135 0.0513  0.0055  205 ASP A CA    
1613 C C     . ASP A 205 ? 0.2118 0.1914 0.1780 -0.0139 0.0478  0.0048  205 ASP A C     
1614 O O     . ASP A 205 ? 0.1916 0.1760 0.1634 -0.0141 0.0458  0.0043  205 ASP A O     
1615 C CB    . ASP A 205 ? 0.1742 0.1488 0.1353 -0.0131 0.0496  0.0064  205 ASP A CB    
1616 C CG    . ASP A 205 ? 0.3303 0.2977 0.2843 -0.0124 0.0525  0.0074  205 ASP A CG    
1617 O OD1   . ASP A 205 ? 0.4191 0.3784 0.3671 -0.0122 0.0566  0.0073  205 ASP A OD1   
1618 O OD2   . ASP A 205 ? 0.4740 0.4437 0.4283 -0.0119 0.0506  0.0084  205 ASP A OD2   
1619 N N     . HIS A 206 ? 0.3600 0.3408 0.3255 -0.0140 0.0468  0.0047  206 HIS A N     
1620 C CA    . HIS A 206 ? 0.4191 0.4069 0.3906 -0.0142 0.0434  0.0041  206 HIS A CA    
1621 C C     . HIS A 206 ? 0.0979 0.0834 0.0682 -0.0147 0.0450  0.0032  206 HIS A C     
1622 O O     . HIS A 206 ? 0.1068 0.0863 0.0712 -0.0147 0.0478  0.0034  206 HIS A O     
1623 C CB    . HIS A 206 ? 0.1849 0.1794 0.1588 -0.0134 0.0390  0.0054  206 HIS A CB    
1624 C CG    . HIS A 206 ? 0.0833 0.0798 0.0580 -0.0128 0.0375  0.0064  206 HIS A CG    
1625 N ND1   . HIS A 206 ? 0.0890 0.0821 0.0587 -0.0125 0.0385  0.0075  206 HIS A ND1   
1626 C CD2   . HIS A 206 ? 0.2273 0.2286 0.2069 -0.0125 0.0351  0.0066  206 HIS A CD2   
1627 C CE1   . HIS A 206 ? 0.2633 0.2594 0.2352 -0.0121 0.0369  0.0083  206 HIS A CE1   
1628 N NE2   . HIS A 206 ? 0.2400 0.2410 0.2179 -0.0121 0.0348  0.0078  206 HIS A NE2   
1629 N N     . THR A 207 ? 0.0907 0.0810 0.0662 -0.0149 0.0429  0.0024  207 THR A N     
1630 C CA    . THR A 207 ? 0.2505 0.2389 0.2254 -0.0154 0.0443  0.0014  207 THR A CA    
1631 C C     . THR A 207 ? 0.2446 0.2399 0.2242 -0.0151 0.0402  0.0014  207 THR A C     
1632 O O     . THR A 207 ? 0.1744 0.1748 0.1587 -0.0147 0.0373  0.0014  207 THR A O     
1633 C CB    . THR A 207 ? 0.2509 0.2355 0.2266 -0.0163 0.0475  0.0000  207 THR A CB    
1634 O OG1   . THR A 207 ? 0.3794 0.3560 0.3495 -0.0164 0.0520  0.0001  207 THR A OG1   
1635 C CG2   . THR A 207 ? 0.2804 0.2650 0.2574 -0.0168 0.0480  -0.0011 207 THR A CG2   
1636 N N     . HIS A 208 ? 0.1668 0.1619 0.1445 -0.0151 0.0400  0.0016  208 HIS A N     
1637 C CA    . HIS A 208 ? 0.2878 0.2888 0.2699 -0.0146 0.0365  0.0015  208 HIS A CA    
1638 C C     . HIS A 208 ? 0.3230 0.3241 0.3080 -0.0152 0.0371  0.0001  208 HIS A C     
1639 O O     . HIS A 208 ? 0.1635 0.1597 0.1462 -0.0161 0.0406  -0.0009 208 HIS A O     
1640 C CB    . HIS A 208 ? 0.3680 0.3688 0.3477 -0.0145 0.0361  0.0019  208 HIS A CB    
1641 C CG    . HIS A 208 ? 0.2966 0.3024 0.2806 -0.0140 0.0331  0.0017  208 HIS A CG    
1642 N ND1   . HIS A 208 ? 0.2208 0.2318 0.2091 -0.0129 0.0293  0.0025  208 HIS A ND1   
1643 C CD2   . HIS A 208 ? 0.2243 0.2297 0.2085 -0.0144 0.0335  0.0009  208 HIS A CD2   
1644 C CE1   . HIS A 208 ? 0.1635 0.1769 0.1544 -0.0126 0.0275  0.0021  208 HIS A CE1   
1645 N NE2   . HIS A 208 ? 0.1091 0.1196 0.0978 -0.0136 0.0299  0.0011  208 HIS A NE2   
1646 N N     . THR A 209 ? 0.3170 0.3232 0.3066 -0.0146 0.0338  0.0001  209 THR A N     
1647 C CA    . THR A 209 ? 0.2567 0.2636 0.2491 -0.0150 0.0338  -0.0012 209 THR A CA    
1648 C C     . THR A 209 ? 0.3959 0.4061 0.3903 -0.0145 0.0312  -0.0011 209 THR A C     
1649 O O     . THR A 209 ? 0.4332 0.4475 0.4300 -0.0133 0.0277  -0.0002 209 THR A O     
1650 C CB    . THR A 209 ? 0.1142 0.1232 0.1094 -0.0146 0.0324  -0.0012 209 THR A CB    
1651 O OG1   . THR A 209 ? 0.2959 0.3010 0.2893 -0.0153 0.0354  -0.0016 209 THR A OG1   
1652 C CG2   . THR A 209 ? 0.2112 0.2216 0.2092 -0.0148 0.0317  -0.0023 209 THR A CG2   
1653 N N     . PRO A 210 ? 0.2878 0.2960 0.2810 -0.0152 0.0329  -0.0019 210 PRO A N     
1654 C CA    . PRO A 210 ? 0.1149 0.1260 0.1100 -0.0147 0.0306  -0.0021 210 PRO A CA    
1655 C C     . PRO A 210 ? 0.0528 0.0666 0.0514 -0.0142 0.0286  -0.0025 210 PRO A C     
1656 O O     . PRO A 210 ? 0.1175 0.1299 0.1167 -0.0149 0.0301  -0.0034 210 PRO A O     
1657 C CB    . PRO A 210 ? 0.0642 0.0717 0.0572 -0.0158 0.0337  -0.0031 210 PRO A CB    
1658 C CG    . PRO A 210 ? 0.0722 0.0748 0.0609 -0.0164 0.0370  -0.0029 210 PRO A CG    
1659 C CD    . PRO A 210 ? 0.0721 0.0745 0.0613 -0.0163 0.0371  -0.0026 210 PRO A CD    
1660 N N     . PHE A 211 ? 0.0462 0.0636 0.0468 -0.0130 0.0252  -0.0016 211 PHE A N     
1661 C CA    . PHE A 211 ? 0.1109 0.1303 0.1138 -0.0123 0.0230  -0.0018 211 PHE A CA    
1662 C C     . PHE A 211 ? 0.3143 0.3332 0.3179 -0.0130 0.0240  -0.0030 211 PHE A C     
1663 O O     . PHE A 211 ? 0.2719 0.2911 0.2768 -0.0130 0.0240  -0.0036 211 PHE A O     
1664 C CB    . PHE A 211 ? 0.0356 0.0573 0.0395 -0.0109 0.0195  -0.0007 211 PHE A CB    
1665 C CG    . PHE A 211 ? 0.0314 0.0545 0.0368 -0.0100 0.0173  -0.0006 211 PHE A CG    
1666 C CD1   . PHE A 211 ? 0.0308 0.0540 0.0367 -0.0098 0.0171  -0.0004 211 PHE A CD1   
1667 C CD2   . PHE A 211 ? 0.0282 0.0524 0.0341 -0.0094 0.0153  -0.0006 211 PHE A CD2   
1668 C CE1   . PHE A 211 ? 0.0274 0.0516 0.0342 -0.0091 0.0151  -0.0003 211 PHE A CE1   
1669 C CE2   . PHE A 211 ? 0.1299 0.1550 0.1363 -0.0087 0.0133  -0.0005 211 PHE A CE2   
1670 C CZ    . PHE A 211 ? 0.0248 0.0499 0.0315 -0.0085 0.0131  -0.0003 211 PHE A CZ    
1671 N N     . ALA A 212 ? 0.2584 0.2765 0.2611 -0.0134 0.0249  -0.0034 212 ALA A N     
1672 C CA    . ALA A 212 ? 0.3200 0.3374 0.3234 -0.0140 0.0259  -0.0045 212 ALA A CA    
1673 C C     . ALA A 212 ? 0.2067 0.2204 0.2090 -0.0155 0.0298  -0.0059 212 ALA A C     
1674 O O     . ALA A 212 ? 0.2271 0.2400 0.2303 -0.0160 0.0309  -0.0070 212 ALA A O     
1675 C CB    . ALA A 212 ? 0.0456 0.0635 0.0486 -0.0139 0.0254  -0.0044 212 ALA A CB    
1676 N N     . SER A 213 ? 0.1647 0.1758 0.1651 -0.0160 0.0319  -0.0058 213 SER A N     
1677 C CA    . SER A 213 ? 0.0645 0.0712 0.0637 -0.0173 0.0358  -0.0069 213 SER A CA    
1678 C C     . SER A 213 ? 0.2383 0.2454 0.2396 -0.0174 0.0358  -0.0076 213 SER A C     
1679 O O     . SER A 213 ? 0.2869 0.2908 0.2881 -0.0184 0.0388  -0.0089 213 SER A O     
1680 C CB    . SER A 213 ? 0.1421 0.1454 0.1381 -0.0176 0.0382  -0.0064 213 SER A CB    
1681 O OG    . SER A 213 ? 0.3807 0.3844 0.3772 -0.0174 0.0378  -0.0061 213 SER A OG    
1682 N N     . LEU A 214 ? 0.1541 0.1648 0.1571 -0.0164 0.0327  -0.0068 214 LEU A N     
1683 C CA    . LEU A 214 ? 0.1377 0.1485 0.1422 -0.0165 0.0329  -0.0074 214 LEU A CA    
1684 C C     . LEU A 214 ? 0.3239 0.3347 0.3301 -0.0170 0.0337  -0.0088 214 LEU A C     
1685 O O     . LEU A 214 ? 0.4401 0.4486 0.4469 -0.0179 0.0360  -0.0100 214 LEU A O     
1686 C CB    . LEU A 214 ? 0.0509 0.0655 0.0566 -0.0152 0.0294  -0.0062 214 LEU A CB    
1687 C CG    . LEU A 214 ? 0.1607 0.1759 0.1652 -0.0145 0.0283  -0.0048 214 LEU A CG    
1688 C CD1   . LEU A 214 ? 0.2010 0.2198 0.2067 -0.0129 0.0245  -0.0033 214 LEU A CD1   
1689 C CD2   . LEU A 214 ? 0.1556 0.1679 0.1590 -0.0153 0.0309  -0.0051 214 LEU A CD2   
1690 N N     . SER A 215 ? 0.2213 0.2342 0.2283 -0.0165 0.0318  -0.0086 215 SER A N     
1691 C CA    . SER A 215 ? 0.1852 0.1986 0.1938 -0.0167 0.0320  -0.0096 215 SER A CA    
1692 C C     . SER A 215 ? 0.2631 0.2776 0.2719 -0.0164 0.0310  -0.0095 215 SER A C     
1693 O O     . SER A 215 ? 0.2068 0.2228 0.2149 -0.0156 0.0292  -0.0084 215 SER A O     
1694 C CB    . SER A 215 ? 0.2598 0.2760 0.2700 -0.0159 0.0296  -0.0093 215 SER A CB    
1695 O OG    . SER A 215 ? 0.4571 0.4764 0.4674 -0.0144 0.0261  -0.0077 215 SER A OG    
1696 N N     . GLU A 216 ? 0.3940 0.4079 0.4039 -0.0170 0.0322  -0.0106 216 GLU A N     
1697 C CA    . GLU A 216 ? 0.3596 0.3750 0.3701 -0.0166 0.0311  -0.0105 216 GLU A CA    
1698 C C     . GLU A 216 ? 0.2462 0.2653 0.2576 -0.0150 0.0273  -0.0092 216 GLU A C     
1699 O O     . GLU A 216 ? 0.3325 0.3529 0.3439 -0.0144 0.0259  -0.0086 216 GLU A O     
1700 C CB    . GLU A 216 ? 0.5129 0.5270 0.5246 -0.0174 0.0332  -0.0120 216 GLU A CB    
1701 C CG    . GLU A 216 ? 0.5876 0.5972 0.5985 -0.0189 0.0374  -0.0133 216 GLU A CG    
1702 C CD    . GLU A 216 ? 0.4282 0.4365 0.4403 -0.0196 0.0393  -0.0145 216 GLU A CD    
1703 O OE1   . GLU A 216 ? 0.4252 0.4298 0.4371 -0.0208 0.0429  -0.0157 216 GLU A OE1   
1704 O OE2   . GLU A 216 ? 0.4115 0.4224 0.4246 -0.0190 0.0374  -0.0143 216 GLU A OE2   
1705 N N     . GLU A 217 ? 0.1697 0.1901 0.1815 -0.0145 0.0260  -0.0087 217 GLU A N     
1706 C CA    . GLU A 217 ? 0.1575 0.1806 0.1697 -0.0129 0.0228  -0.0073 217 GLU A CA    
1707 C C     . GLU A 217 ? 0.2552 0.2792 0.2664 -0.0119 0.0207  -0.0058 217 GLU A C     
1708 O O     . GLU A 217 ? 0.2580 0.2833 0.2692 -0.0107 0.0185  -0.0047 217 GLU A O     
1709 C CB    . GLU A 217 ? 0.0372 0.0610 0.0500 -0.0128 0.0223  -0.0074 217 GLU A CB    
1710 C CG    . GLU A 217 ? 0.2387 0.2646 0.2516 -0.0112 0.0193  -0.0060 217 GLU A CG    
1711 C CD    . GLU A 217 ? 0.3681 0.3950 0.3821 -0.0112 0.0192  -0.0065 217 GLU A CD    
1712 O OE1   . GLU A 217 ? 0.4509 0.4791 0.4647 -0.0100 0.0171  -0.0053 217 GLU A OE1   
1713 O OE2   . GLU A 217 ? 0.5046 0.5305 0.5194 -0.0124 0.0214  -0.0081 217 GLU A OE2   
1714 N N     . LEU A 218 ? 0.3503 0.3733 0.3606 -0.0123 0.0215  -0.0057 218 LEU A N     
1715 C CA    . LEU A 218 ? 0.2271 0.2508 0.2365 -0.0114 0.0197  -0.0043 218 LEU A CA    
1716 C C     . LEU A 218 ? 0.1514 0.1744 0.1600 -0.0117 0.0203  -0.0045 218 LEU A C     
1717 O O     . LEU A 218 ? 0.1302 0.1541 0.1385 -0.0109 0.0185  -0.0035 218 LEU A O     
1718 C CB    . LEU A 218 ? 0.0349 0.0578 0.0435 -0.0116 0.0202  -0.0040 218 LEU A CB    
1719 C CG    . LEU A 218 ? 0.0335 0.0571 0.0429 -0.0112 0.0195  -0.0039 218 LEU A CG    
1720 C CD1   . LEU A 218 ? 0.0349 0.0579 0.0437 -0.0113 0.0198  -0.0034 218 LEU A CD1   
1721 C CD2   . LEU A 218 ? 0.0289 0.0542 0.0388 -0.0099 0.0167  -0.0030 218 LEU A CD2   
1722 N N     . ALA A 219 ? 0.2902 0.3114 0.2986 -0.0130 0.0230  -0.0058 219 ALA A N     
1723 C CA    . ALA A 219 ? 0.3112 0.3316 0.3188 -0.0134 0.0239  -0.0060 219 ALA A CA    
1724 C C     . ALA A 219 ? 0.3263 0.3485 0.3347 -0.0126 0.0219  -0.0055 219 ALA A C     
1725 O O     . ALA A 219 ? 0.4981 0.5208 0.5060 -0.0121 0.0208  -0.0049 219 ALA A O     
1726 C CB    . ALA A 219 ? 0.2244 0.2418 0.2314 -0.0150 0.0274  -0.0075 219 ALA A CB    
1727 N N     . GLU A 220 ? 0.1785 0.2014 0.1881 -0.0123 0.0215  -0.0058 220 GLU A N     
1728 C CA    . GLU A 220 ? 0.3741 0.3983 0.3844 -0.0115 0.0200  -0.0053 220 GLU A CA    
1729 C C     . GLU A 220 ? 0.2306 0.2562 0.2408 -0.0099 0.0170  -0.0038 220 GLU A C     
1730 O O     . GLU A 220 ? 0.2071 0.2334 0.2178 -0.0092 0.0159  -0.0032 220 GLU A O     
1731 C CB    . GLU A 220 ? 0.4669 0.4914 0.4785 -0.0116 0.0206  -0.0060 220 GLU A CB    
1732 C CG    . GLU A 220 ? 0.3190 0.3414 0.3307 -0.0132 0.0238  -0.0078 220 GLU A CG    
1733 C CD    . GLU A 220 ? 0.0795 0.1009 0.0911 -0.0138 0.0251  -0.0085 220 GLU A CD    
1734 O OE1   . GLU A 220 ? 0.0591 0.0781 0.0697 -0.0150 0.0275  -0.0093 220 GLU A OE1   
1735 O OE2   . GLU A 220 ? 0.2774 0.3001 0.2898 -0.0131 0.0240  -0.0081 220 GLU A OE2   
1736 N N     . ARG A 221 ? 0.2740 0.2998 0.2837 -0.0095 0.0160  -0.0031 221 ARG A N     
1737 C CA    . ARG A 221 ? 0.0240 0.0505 0.0332 -0.0082 0.0133  -0.0019 221 ARG A CA    
1738 C C     . ARG A 221 ? 0.0234 0.0498 0.0315 -0.0082 0.0125  -0.0015 221 ARG A C     
1739 O O     . ARG A 221 ? 0.0206 0.0476 0.0278 -0.0073 0.0101  -0.0006 221 ARG A O     
1740 C CB    . ARG A 221 ? 0.1641 0.1910 0.1734 -0.0076 0.0121  -0.0015 221 ARG A CB    
1741 C CG    . ARG A 221 ? 0.1308 0.1574 0.1400 -0.0082 0.0131  -0.0017 221 ARG A CG    
1742 C CD    . ARG A 221 ? 0.0213 0.0484 0.0300 -0.0074 0.0112  -0.0011 221 ARG A CD    
1743 N NE    . ARG A 221 ? 0.0213 0.0488 0.0308 -0.0073 0.0114  -0.0013 221 ARG A NE    
1744 C CZ    . ARG A 221 ? 0.1852 0.2133 0.1943 -0.0064 0.0098  -0.0007 221 ARG A CZ    
1745 N NH1   . ARG A 221 ? 0.0248 0.0533 0.0327 -0.0056 0.0078  0.0004  221 ARG A NH1   
1746 N NH2   . ARG A 221 ? 0.2196 0.2482 0.2296 -0.0064 0.0102  -0.0010 221 ARG A NH2   
1747 N N     . THR A 222 ? 0.0263 0.0519 0.0341 -0.0092 0.0144  -0.0021 222 THR A N     
1748 C CA    . THR A 222 ? 0.2327 0.2582 0.2394 -0.0093 0.0140  -0.0017 222 THR A CA    
1749 C C     . THR A 222 ? 0.3509 0.3760 0.3570 -0.0098 0.0148  -0.0020 222 THR A C     
1750 O O     . THR A 222 ? 0.1397 0.1640 0.1460 -0.0107 0.0169  -0.0029 222 THR A O     
1751 C CB    . THR A 222 ? 0.1024 0.1269 0.1087 -0.0100 0.0159  -0.0019 222 THR A CB    
1752 O OG1   . THR A 222 ? 0.1036 0.1285 0.1104 -0.0094 0.0149  -0.0016 222 THR A OG1   
1753 C CG2   . THR A 222 ? 0.0298 0.0539 0.0349 -0.0101 0.0159  -0.0015 222 THR A CG2   
1754 N N     . ILE A 223 ? 0.0257 0.0515 0.0312 -0.0094 0.0131  -0.0015 223 ILE A N     
1755 C CA    . ILE A 223 ? 0.0272 0.0527 0.0319 -0.0099 0.0137  -0.0018 223 ILE A CA    
1756 C C     . ILE A 223 ? 0.1341 0.1590 0.1376 -0.0104 0.0144  -0.0015 223 ILE A C     
1757 O O     . ILE A 223 ? 0.2954 0.3212 0.2987 -0.0098 0.0125  -0.0009 223 ILE A O     
1758 C CB    . ILE A 223 ? 0.2052 0.2320 0.2099 -0.0092 0.0112  -0.0014 223 ILE A CB    
1759 C CG1   . ILE A 223 ? 0.1108 0.1379 0.1166 -0.0086 0.0108  -0.0014 223 ILE A CG1   
1760 C CG2   . ILE A 223 ? 0.0256 0.0522 0.0296 -0.0099 0.0121  -0.0018 223 ILE A CG2   
1761 C CD1   . ILE A 223 ? 0.1423 0.1701 0.1480 -0.0074 0.0085  -0.0004 223 ILE A CD1   
1762 N N     . THR A 224 ? 0.0813 0.1045 0.0836 -0.0114 0.0173  -0.0019 224 THR A N     
1763 C CA    . THR A 224 ? 0.0416 0.0636 0.0421 -0.0118 0.0188  -0.0015 224 THR A CA    
1764 C C     . THR A 224 ? 0.1855 0.2070 0.1843 -0.0121 0.0191  -0.0014 224 THR A C     
1765 O O     . THR A 224 ? 0.1351 0.1550 0.1324 -0.0129 0.0213  -0.0019 224 THR A O     
1766 C CB    . THR A 224 ? 0.0486 0.0682 0.0478 -0.0128 0.0221  -0.0020 224 THR A CB    
1767 O OG1   . THR A 224 ? 0.2378 0.2579 0.2387 -0.0126 0.0218  -0.0023 224 THR A OG1   
1768 C CG2   . THR A 224 ? 0.0459 0.0639 0.0428 -0.0130 0.0236  -0.0013 224 THR A CG2   
1769 N N     . CYS A 225 ? 0.0364 0.0587 0.0348 -0.0117 0.0176  -0.0007 225 CYS A N     
1770 C CA    . CYS A 225 ? 0.1006 0.1227 0.0973 -0.0120 0.0176  -0.0004 225 CYS A CA    
1771 C C     . CYS A 225 ? 0.0943 0.1138 0.0877 -0.0122 0.0203  0.0003  225 CYS A C     
1772 O O     . CYS A 225 ? 0.0428 0.0623 0.0365 -0.0119 0.0201  0.0009  225 CYS A O     
1773 C CB    . CYS A 225 ? 0.1759 0.2009 0.1739 -0.0114 0.0137  -0.0002 225 CYS A CB    
1774 S SG    . CYS A 225 ? 0.0559 0.0839 0.0562 -0.0103 0.0097  -0.0002 225 CYS A SG    
1775 N N     . MET A 226 ? 0.0819 0.0990 0.0717 -0.0128 0.0228  0.0004  226 MET A N     
1776 C CA    . MET A 226 ? 0.1587 0.1724 0.1434 -0.0129 0.0255  0.0011  226 MET A CA    
1777 C C     . MET A 226 ? 0.2906 0.3027 0.2712 -0.0129 0.0261  0.0014  226 MET A C     
1778 O O     . MET A 226 ? 0.3149 0.3283 0.2969 -0.0130 0.0251  0.0008  226 MET A O     
1779 C CB    . MET A 226 ? 0.2771 0.2871 0.2592 -0.0139 0.0290  0.0004  226 MET A CB    
1780 C CG    . MET A 226 ? 0.4183 0.4288 0.4028 -0.0139 0.0291  0.0002  226 MET A CG    
1781 S SD    . MET A 226 ? 0.2706 0.2773 0.2540 -0.0152 0.0326  -0.0012 226 MET A SD    
1782 C CE    . MET A 226 ? 0.0768 0.0788 0.0548 -0.0158 0.0355  -0.0016 226 MET A CE    
1783 N N     . ALA A 227 ? 0.0675 0.0763 0.0423 -0.0126 0.0278  0.0023  227 ALA A N     
1784 C CA    . ALA A 227 ? 0.3653 0.3716 0.3343 -0.0123 0.0284  0.0027  227 ALA A CA    
1785 C C     . ALA A 227 ? 0.4307 0.4314 0.3910 -0.0120 0.0307  0.0033  227 ALA A C     
1786 O O     . ALA A 227 ? 0.4838 0.4839 0.4440 -0.0120 0.0311  0.0039  227 ALA A O     
1787 C CB    . ALA A 227 ? 0.2458 0.2555 0.2177 -0.0115 0.0252  0.0031  227 ALA A CB    
1788 N N     . PRO A 228 ? 0.3170 0.3126 0.2692 -0.0118 0.0322  0.0032  228 PRO A N     
1789 C CA    . PRO A 228 ? 0.2359 0.2248 0.1782 -0.0112 0.0336  0.0038  228 PRO A CA    
1790 C C     . PRO A 228 ? 0.2892 0.2793 0.2287 -0.0100 0.0307  0.0046  228 PRO A C     
1791 O O     . PRO A 228 ? 0.5044 0.4885 0.4350 -0.0092 0.0312  0.0051  228 PRO A O     
1792 C CB    . PRO A 228 ? 0.1163 0.0981 0.0505 -0.0111 0.0362  0.0030  228 PRO A CB    
1793 C CG    . PRO A 228 ? 0.1907 0.1773 0.1298 -0.0114 0.0347  0.0023  228 PRO A CG    
1794 C CD    . PRO A 228 ? 0.2290 0.2236 0.1800 -0.0121 0.0329  0.0023  228 PRO A CD    
1795 N N     . SER A 229 ? 0.3596 0.3563 0.3060 -0.0096 0.0278  0.0048  229 SER A N     
1796 C CA    . SER A 229 ? 0.4249 0.4224 0.3684 -0.0082 0.0249  0.0054  229 SER A CA    
1797 C C     . SER A 229 ? 0.2913 0.2885 0.2335 -0.0077 0.0240  0.0066  229 SER A C     
1798 O O     . SER A 229 ? 0.4904 0.4834 0.4241 -0.0069 0.0228  0.0068  229 SER A O     
1799 C CB    . SER A 229 ? 0.4403 0.4433 0.3923 -0.0080 0.0225  0.0053  229 SER A CB    
1800 O OG    . SER A 229 ? 0.4871 0.4906 0.4406 -0.0087 0.0233  0.0042  229 SER A OG    
1801 N N1    . LLP A 230 ? 0.2168 0.2465 0.2332 -0.0002 0.0150  -0.0005 230 LLP A N1    
1802 C C2    . LLP A 230 ? 0.2739 0.3027 0.2888 -0.0006 0.0156  0.0002  230 LLP A C2    
1803 C "C2'" . LLP A 230 ? 0.3099 0.3377 0.3264 -0.0009 0.0155  0.0006  230 LLP A "C2'" 
1804 C C3    . LLP A 230 ? 0.2062 0.2345 0.2167 -0.0006 0.0166  0.0004  230 LLP A C3    
1805 O O3    . LLP A 230 ? 0.0747 0.1026 0.0823 -0.0010 0.0172  0.0015  230 LLP A O3    
1806 C C4    . LLP A 230 ? 0.2994 0.3337 0.3056 -0.0001 0.0162  -0.0006 230 LLP A C4    
1807 C "C4'" . LLP A 230 ? 0.2282 0.2631 0.2232 0.0002  0.0152  0.0002  230 LLP A "C4'" 
1808 C C5    . LLP A 230 ? 0.3398 0.3744 0.3492 0.0002  0.0157  -0.0020 230 LLP A C5    
1809 C C6    . LLP A 230 ? 0.1960 0.2267 0.2109 0.0002  0.0152  -0.0013 230 LLP A C6    
1810 C "C5'" . LLP A 230 ? 0.2854 0.3266 0.2900 0.0009  0.0150  -0.0050 230 LLP A "C5'" 
1811 O OP4   . LLP A 230 ? 0.2253 0.2588 0.2196 0.0006  0.0183  -0.0062 230 LLP A OP4   
1812 P P     . LLP A 230 ? 0.0514 0.0802 0.0352 0.0012  0.0169  -0.0093 230 LLP A P     
1813 O OP1   . LLP A 230 ? 0.2480 0.2832 0.2436 0.0016  0.0146  -0.0107 230 LLP A OP1   
1814 O OP2   . LLP A 230 ? 0.1985 0.2180 0.1716 0.0020  0.0108  -0.0092 230 LLP A OP2   
1815 O OP3   . LLP A 230 ? 0.4199 0.4413 0.3966 0.0012  0.0218  -0.0091 230 LLP A OP3   
1816 N N     . LLP A 230 ? 0.0929 0.0937 0.0428 -0.0081 0.0242  0.0070  230 LLP A N     
1817 C CA    . LLP A 230 ? 0.1656 0.1662 0.1144 -0.0077 0.0236  0.0081  230 LLP A CA    
1818 C CB    . LLP A 230 ? 0.1546 0.1599 0.1136 -0.0078 0.0227  0.0084  230 LLP A CB    
1819 C CG    . LLP A 230 ? 0.3298 0.3378 0.2952 -0.0081 0.0197  0.0078  230 LLP A CG    
1820 C CD    . LLP A 230 ? 0.1634 0.1700 0.1256 -0.0073 0.0176  0.0086  230 LLP A CD    
1821 C CE    . LLP A 230 ? 0.0757 0.0886 0.0469 -0.0095 0.0134  0.0074  230 LLP A CE    
1822 N NZ    . LLP A 230 ? 0.1921 0.2124 0.1737 -0.0108 0.0109  0.0066  230 LLP A NZ    
1823 C C     . LLP A 230 ? 0.3070 0.3008 0.2478 -0.0084 0.0264  0.0080  230 LLP A C     
1824 O O     . LLP A 230 ? 0.3151 0.3047 0.2490 -0.0078 0.0260  0.0086  230 LLP A O     
1825 N N     . THR A 231 ? 0.4439 0.4352 0.3848 -0.0094 0.0293  0.0071  231 THR A N     
1826 C CA    . THR A 231 ? 0.4990 0.4825 0.4330 -0.0097 0.0326  0.0070  231 THR A CA    
1827 C C     . THR A 231 ? 0.4935 0.4676 0.4146 -0.0086 0.0336  0.0070  231 THR A C     
1828 O O     . THR A 231 ? 0.5815 0.5492 0.4955 -0.0078 0.0346  0.0076  231 THR A O     
1829 C CB    . THR A 231 ? 0.5300 0.5123 0.4667 -0.0107 0.0356  0.0059  231 THR A CB    
1830 O OG1   . THR A 231 ? 0.4891 0.4785 0.4362 -0.0114 0.0344  0.0057  231 THR A OG1   
1831 C CG2   . THR A 231 ? 0.4260 0.3989 0.3547 -0.0107 0.0395  0.0059  231 THR A CG2   
1832 N N     . PHE A 232 ? 0.4263 0.3987 0.3436 -0.0082 0.0331  0.0064  232 PHE A N     
1833 C CA    . PHE A 232 ? 0.3442 0.3066 0.2483 -0.0067 0.0337  0.0063  232 PHE A CA    
1834 C C     . PHE A 232 ? 0.4024 0.3651 0.3023 -0.0055 0.0295  0.0063  232 PHE A C     
1835 O O     . PHE A 232 ? 0.4262 0.3804 0.3146 -0.0038 0.0290  0.0060  232 PHE A O     
1836 C CB    . PHE A 232 ? 0.3582 0.3166 0.2593 -0.0069 0.0362  0.0053  232 PHE A CB    
1837 C CG    . PHE A 232 ? 0.2583 0.2150 0.1624 -0.0080 0.0403  0.0051  232 PHE A CG    
1838 C CD1   . PHE A 232 ? 0.2782 0.2250 0.1736 -0.0072 0.0437  0.0054  232 PHE A CD1   
1839 C CD2   . PHE A 232 ? 0.2101 0.1746 0.1254 -0.0096 0.0404  0.0045  232 PHE A CD2   
1840 C CE1   . PHE A 232 ? 0.1933 0.1383 0.0915 -0.0082 0.0474  0.0051  232 PHE A CE1   
1841 C CE2   . PHE A 232 ? 0.1747 0.1372 0.0925 -0.0105 0.0437  0.0041  232 PHE A CE2   
1842 C CZ    . PHE A 232 ? 0.2114 0.1645 0.1209 -0.0099 0.0472  0.0044  232 PHE A CZ    
1843 N N     . ASN A 233 ? 0.3267 0.2987 0.2354 -0.0059 0.0263  0.0068  233 ASN A N     
1844 C CA    . ASN A 233 ? 0.3429 0.3158 0.2487 -0.0048 0.0220  0.0068  233 ASN A CA    
1845 C C     . ASN A 233 ? 0.3530 0.3243 0.2548 -0.0041 0.0206  0.0055  233 ASN A C     
1846 O O     . ASN A 233 ? 0.3697 0.3339 0.2611 -0.0026 0.0181  0.0048  233 ASN A O     
1847 C CB    . ASN A 233 ? 0.4417 0.4063 0.3369 -0.0033 0.0206  0.0073  233 ASN A CB    
1848 C CG    . ASN A 233 ? 0.3297 0.2983 0.2269 -0.0027 0.0157  0.0078  233 ASN A CG    
1849 O OD1   . ASN A 233 ? 0.2822 0.2606 0.1905 -0.0036 0.0146  0.0084  233 ASN A OD1   
1850 N ND2   . ASN A 233 ? 0.2220 0.1826 0.1083 -0.0009 0.0125  0.0074  233 ASN A ND2   
1851 N N     . ILE A 234 ? 0.3489 0.3262 0.2587 -0.0051 0.0219  0.0050  234 ILE A N     
1852 C CA    . ILE A 234 ? 0.3351 0.3123 0.2427 -0.0047 0.0206  0.0037  234 ILE A CA    
1853 C C     . ILE A 234 ? 0.2903 0.2779 0.2099 -0.0050 0.0188  0.0038  234 ILE A C     
1854 O O     . ILE A 234 ? 0.2841 0.2741 0.2069 -0.0052 0.0193  0.0029  234 ILE A O     
1855 C CB    . ILE A 234 ? 0.2642 0.2358 0.1674 -0.0050 0.0243  0.0029  234 ILE A CB    
1856 C CG1   . ILE A 234 ? 0.2060 0.1832 0.1198 -0.0068 0.0275  0.0032  234 ILE A CG1   
1857 C CG2   . ILE A 234 ? 0.2594 0.2197 0.1508 -0.0041 0.0266  0.0031  234 ILE A CG2   
1858 C CD1   . ILE A 234 ? 0.1524 0.1267 0.0646 -0.0073 0.0301  0.0022  234 ILE A CD1   
1859 N N     . ALA A 235 ? 0.3056 0.2985 0.2315 -0.0046 0.0167  0.0049  235 ALA A N     
1860 C CA    . ALA A 235 ? 0.2267 0.2260 0.1635 -0.0042 0.0154  0.0053  235 ALA A CA    
1861 C C     . ALA A 235 ? 0.3261 0.3256 0.2612 -0.0029 0.0121  0.0041  235 ALA A C     
1862 O O     . ALA A 235 ? 0.4064 0.4082 0.3498 -0.0041 0.0115  0.0039  235 ALA A O     
1863 C CB    . ALA A 235 ? 0.2333 0.2342 0.1751 -0.0040 0.0143  0.0066  235 ALA A CB    
1864 N N     . GLY A 236 ? 0.2114 0.2077 0.1363 -0.0022 0.0092  0.0028  236 GLY A N     
1865 C CA    . GLY A 236 ? 0.1713 0.1684 0.0945 -0.0013 0.0052  0.0008  236 GLY A CA    
1866 C C     . GLY A 236 ? 0.3196 0.3155 0.2410 -0.0016 0.0072  -0.0007 236 GLY A C     
1867 O O     . GLY A 236 ? 0.1070 0.1037 0.0272 -0.0010 0.0039  -0.0029 236 GLY A O     
1868 N N     . LEU A 237 ? 0.3280 0.3217 0.2492 -0.0029 0.0122  0.0000  237 LEU A N     
1869 C CA    . LEU A 237 ? 0.2642 0.2567 0.1846 -0.0034 0.0146  -0.0011 237 LEU A CA    
1870 C C     . LEU A 237 ? 0.3374 0.3353 0.2701 -0.0045 0.0172  -0.0002 237 LEU A C     
1871 O O     . LEU A 237 ? 0.3812 0.3793 0.3150 -0.0049 0.0185  -0.0012 237 LEU A O     
1872 C CB    . LEU A 237 ? 0.2330 0.2178 0.1453 -0.0041 0.0183  -0.0010 237 LEU A CB    
1873 C CG    . LEU A 237 ? 0.2421 0.2168 0.1408 -0.0030 0.0169  -0.0014 237 LEU A CG    
1874 C CD1   . LEU A 237 ? 0.2039 0.1695 0.0940 -0.0029 0.0208  -0.0017 237 LEU A CD1   
1875 C CD2   . LEU A 237 ? 0.1456 0.1179 0.0380 -0.0015 0.0113  -0.0032 237 LEU A CD2   
1876 N N     . GLN A 238 ? 0.1858 0.1871 0.1277 -0.0055 0.0176  0.0012  238 GLN A N     
1877 C CA    . GLN A 238 ? 0.3087 0.3152 0.2634 -0.0082 0.0184  0.0011  238 GLN A CA    
1878 C C     . GLN A 238 ? 0.4271 0.4337 0.3840 -0.0093 0.0215  0.0007  238 GLN A C     
1879 O O     . GLN A 238 ? 0.6324 0.6407 0.5930 -0.0103 0.0218  -0.0003 238 GLN A O     
1880 C CB    . GLN A 238 ? 0.1030 0.1130 0.0624 -0.0091 0.0158  -0.0001 238 GLN A CB    
1881 C CG    . GLN A 238 ? 0.2746 0.2891 0.2397 -0.0101 0.0122  0.0002  238 GLN A CG    
1882 C CD    . GLN A 238 ? 0.4899 0.5033 0.4508 -0.0090 0.0088  -0.0008 238 GLN A CD    
1883 O OE1   . GLN A 238 ? 0.5535 0.5644 0.5099 -0.0075 0.0048  -0.0007 238 GLN A OE1   
1884 N NE2   . GLN A 238 ? 0.6453 0.6595 0.6068 -0.0092 0.0092  -0.0022 238 GLN A NE2   
1885 N N     . ALA A 239 ? 0.5631 0.5675 0.5176 -0.0094 0.0236  0.0013  239 ALA A N     
1886 C CA    . ALA A 239 ? 0.5050 0.5089 0.4619 -0.0107 0.0262  0.0008  239 ALA A CA    
1887 C C     . ALA A 239 ? 0.3652 0.3726 0.3301 -0.0116 0.0257  0.0011  239 ALA A C     
1888 O O     . ALA A 239 ? 0.5172 0.5244 0.4815 -0.0111 0.0251  0.0020  239 ALA A O     
1889 C CB    . ALA A 239 ? 0.4933 0.4903 0.4400 -0.0105 0.0291  0.0008  239 ALA A CB    
1890 N N     . SER A 240 ? 0.2037 0.2138 0.1752 -0.0126 0.0255  0.0001  240 SER A N     
1891 C CA    . SER A 240 ? 0.2256 0.2385 0.2033 -0.0131 0.0245  0.0000  240 SER A CA    
1892 C C     . SER A 240 ? 0.1638 0.1763 0.1434 -0.0138 0.0260  -0.0010 240 SER A C     
1893 O O     . SER A 240 ? 0.2462 0.2583 0.2254 -0.0142 0.0266  -0.0018 240 SER A O     
1894 C CB    . SER A 240 ? 0.1941 0.2120 0.1785 -0.0132 0.0204  -0.0003 240 SER A CB    
1895 O OG    . SER A 240 ? 0.4092 0.4277 0.3934 -0.0128 0.0190  0.0005  240 SER A OG    
1896 N N     . ILE A 241 ? 0.2697 0.2823 0.2512 -0.0140 0.0265  -0.0010 241 ILE A N     
1897 C CA    . ILE A 241 ? 0.2193 0.2309 0.2020 -0.0147 0.0281  -0.0020 241 ILE A CA    
1898 C C     . ILE A 241 ? 0.2703 0.2853 0.2586 -0.0144 0.0257  -0.0022 241 ILE A C     
1899 O O     . ILE A 241 ? 0.1500 0.1655 0.1389 -0.0140 0.0251  -0.0016 241 ILE A O     
1900 C CB    . ILE A 241 ? 0.3234 0.3298 0.3010 -0.0153 0.0318  -0.0020 241 ILE A CB    
1901 C CG1   . ILE A 241 ? 0.3951 0.3968 0.3654 -0.0153 0.0342  -0.0018 241 ILE A CG1   
1902 C CG2   . ILE A 241 ? 0.5363 0.5413 0.5155 -0.0161 0.0336  -0.0031 241 ILE A CG2   
1903 C CD1   . ILE A 241 ? 0.3745 0.3767 0.3450 -0.0155 0.0341  -0.0025 241 ILE A CD1   
1904 N N     . ILE A 242 ? 0.0511 0.0679 0.0427 -0.0145 0.0246  -0.0031 242 ILE A N     
1905 C CA    . ILE A 242 ? 0.0458 0.0648 0.0411 -0.0139 0.0225  -0.0032 242 ILE A CA    
1906 C C     . ILE A 242 ? 0.3064 0.3239 0.3020 -0.0146 0.0247  -0.0041 242 ILE A C     
1907 O O     . ILE A 242 ? 0.4096 0.4259 0.4045 -0.0152 0.0261  -0.0049 242 ILE A O     
1908 C CB    . ILE A 242 ? 0.3433 0.3654 0.3415 -0.0132 0.0192  -0.0033 242 ILE A CB    
1909 C CG1   . ILE A 242 ? 0.3609 0.3842 0.3585 -0.0130 0.0175  -0.0029 242 ILE A CG1   
1910 C CG2   . ILE A 242 ? 0.1896 0.2134 0.1901 -0.0123 0.0170  -0.0030 242 ILE A CG2   
1911 C CD1   . ILE A 242 ? 0.3700 0.3937 0.3671 -0.0127 0.0165  -0.0021 242 ILE A CD1   
1912 N N     . ILE A 243 ? 0.1852 0.2025 0.1816 -0.0145 0.0249  -0.0040 243 ILE A N     
1913 C CA    . ILE A 243 ? 0.0513 0.0671 0.0482 -0.0151 0.0268  -0.0049 243 ILE A CA    
1914 C C     . ILE A 243 ? 0.1973 0.2159 0.1976 -0.0142 0.0243  -0.0048 243 ILE A C     
1915 O O     . ILE A 243 ? 0.0414 0.0618 0.0428 -0.0133 0.0220  -0.0040 243 ILE A O     
1916 C CB    . ILE A 243 ? 0.0569 0.0696 0.0516 -0.0158 0.0296  -0.0050 243 ILE A CB    
1917 C CG1   . ILE A 243 ? 0.1111 0.1201 0.1013 -0.0164 0.0323  -0.0048 243 ILE A CG1   
1918 C CG2   . ILE A 243 ? 0.0596 0.0706 0.0551 -0.0165 0.0315  -0.0060 243 ILE A CG2   
1919 C CD1   . ILE A 243 ? 0.0684 0.0747 0.0558 -0.0166 0.0341  -0.0043 243 ILE A CD1   
1920 N N     . ILE A 244 ? 0.2428 0.2615 0.2442 -0.0144 0.0245  -0.0056 244 ILE A N     
1921 C CA    . ILE A 244 ? 0.2014 0.2221 0.2053 -0.0135 0.0225  -0.0055 244 ILE A CA    
1922 C C     . ILE A 244 ? 0.3265 0.3458 0.3309 -0.0142 0.0245  -0.0065 244 ILE A C     
1923 O O     . ILE A 244 ? 0.3987 0.4177 0.4035 -0.0146 0.0252  -0.0072 244 ILE A O     
1924 C CB    . ILE A 244 ? 0.0507 0.0732 0.0557 -0.0126 0.0203  -0.0051 244 ILE A CB    
1925 C CG1   . ILE A 244 ? 0.1984 0.2216 0.2025 -0.0123 0.0188  -0.0044 244 ILE A CG1   
1926 C CG2   . ILE A 244 ? 0.0328 0.0569 0.0395 -0.0114 0.0181  -0.0044 244 ILE A CG2   
1927 C CD1   . ILE A 244 ? 0.2275 0.2524 0.2327 -0.0113 0.0164  -0.0040 244 ILE A CD1   
1928 N N     . PRO A 245 ? 0.3200 0.3386 0.3247 -0.0145 0.0255  -0.0068 245 PRO A N     
1929 C CA    . PRO A 245 ? 0.3575 0.3746 0.3629 -0.0153 0.0276  -0.0080 245 PRO A CA    
1930 C C     . PRO A 245 ? 0.0451 0.0641 0.0525 -0.0146 0.0261  -0.0080 245 PRO A C     
1931 O O     . PRO A 245 ? 0.0887 0.1065 0.0964 -0.0153 0.0278  -0.0089 245 PRO A O     
1932 C CB    . PRO A 245 ? 0.2677 0.2840 0.2732 -0.0156 0.0285  -0.0081 245 PRO A CB    
1933 C CG    . PRO A 245 ? 0.3324 0.3483 0.3363 -0.0154 0.0282  -0.0073 245 PRO A CG    
1934 C CD    . PRO A 245 ? 0.1939 0.2122 0.1980 -0.0144 0.0256  -0.0063 245 PRO A CD    
1935 N N     . ASN A 246 ? 0.0400 0.0615 0.0485 -0.0133 0.0232  -0.0069 246 ASN A N     
1936 C CA    . ASN A 246 ? 0.2191 0.2420 0.2291 -0.0124 0.0220  -0.0066 246 ASN A CA    
1937 C C     . ASN A 246 ? 0.2809 0.3040 0.2909 -0.0123 0.0217  -0.0066 246 ASN A C     
1938 O O     . ASN A 246 ? 0.4893 0.5131 0.4988 -0.0118 0.0203  -0.0059 246 ASN A O     
1939 C CB    . ASN A 246 ? 0.0328 0.0575 0.0433 -0.0110 0.0193  -0.0052 246 ASN A CB    
1940 C CG    . ASN A 246 ? 0.0308 0.0566 0.0426 -0.0102 0.0184  -0.0047 246 ASN A CG    
1941 O OD1   . ASN A 246 ? 0.0718 0.0983 0.0840 -0.0094 0.0172  -0.0040 246 ASN A OD1   
1942 N ND2   . ASN A 246 ? 0.2623 0.2880 0.2747 -0.0103 0.0190  -0.0051 246 ASN A ND2   
1943 N N     . GLU A 247 ? 0.1396 0.1621 0.1504 -0.0128 0.0231  -0.0075 247 GLU A N     
1944 C CA    . GLU A 247 ? 0.1592 0.1816 0.1700 -0.0129 0.0232  -0.0077 247 GLU A CA    
1945 C C     . GLU A 247 ? 0.0344 0.0588 0.0461 -0.0114 0.0206  -0.0063 247 GLU A C     
1946 O O     . GLU A 247 ? 0.3054 0.3299 0.3166 -0.0112 0.0200  -0.0061 247 GLU A O     
1947 C CB    . GLU A 247 ? 0.1307 0.1522 0.1423 -0.0136 0.0250  -0.0088 247 GLU A CB    
1948 C CG    . GLU A 247 ? 0.1699 0.1918 0.1820 -0.0133 0.0247  -0.0087 247 GLU A CG    
1949 C CD    . GLU A 247 ? 0.1318 0.1523 0.1445 -0.0141 0.0268  -0.0099 247 GLU A CD    
1950 O OE1   . GLU A 247 ? 0.1274 0.1461 0.1391 -0.0151 0.0286  -0.0107 247 GLU A OE1   
1951 O OE2   . GLU A 247 ? 0.0972 0.1183 0.1112 -0.0138 0.0268  -0.0099 247 GLU A OE2   
1952 N N     . LYS A 248 ? 0.1200 0.1456 0.1327 -0.0103 0.0192  -0.0053 248 LYS A N     
1953 C CA    . LYS A 248 ? 0.0281 0.0547 0.0414 -0.0088 0.0172  -0.0038 248 LYS A CA    
1954 C C     . LYS A 248 ? 0.3039 0.3307 0.3163 -0.0082 0.0156  -0.0030 248 LYS A C     
1955 O O     . LYS A 248 ? 0.2337 0.2607 0.2464 -0.0075 0.0145  -0.0022 248 LYS A O     
1956 C CB    . LYS A 248 ? 0.0265 0.0539 0.0408 -0.0079 0.0165  -0.0029 248 LYS A CB    
1957 C CG    . LYS A 248 ? 0.0241 0.0519 0.0393 -0.0066 0.0154  -0.0015 248 LYS A CG    
1958 C CD    . LYS A 248 ? 0.0230 0.0511 0.0389 -0.0059 0.0149  -0.0008 248 LYS A CD    
1959 C CE    . LYS A 248 ? 0.0947 0.1224 0.1098 -0.0053 0.0133  0.0000  248 LYS A CE    
1960 N NZ    . LYS A 248 ? 0.1630 0.1906 0.1783 -0.0045 0.0124  0.0007  248 LYS A NZ    
1961 N N     . LEU A 249 ? 0.2912 0.3178 0.3027 -0.0086 0.0155  -0.0032 249 LEU A N     
1962 C CA    . LEU A 249 ? 0.1126 0.1392 0.1231 -0.0082 0.0141  -0.0026 249 LEU A CA    
1963 C C     . LEU A 249 ? 0.0894 0.1158 0.0992 -0.0091 0.0148  -0.0033 249 LEU A C     
1964 O O     . LEU A 249 ? 0.1206 0.1473 0.1300 -0.0086 0.0135  -0.0028 249 LEU A O     
1965 C CB    . LEU A 249 ? 0.0246 0.0511 0.0344 -0.0084 0.0138  -0.0024 249 LEU A CB    
1966 C CG    . LEU A 249 ? 0.0227 0.0496 0.0329 -0.0076 0.0128  -0.0017 249 LEU A CG    
1967 C CD1   . LEU A 249 ? 0.5354 0.5622 0.5447 -0.0078 0.0124  -0.0017 249 LEU A CD1   
1968 C CD2   . LEU A 249 ? 0.0197 0.0469 0.0298 -0.0063 0.0107  -0.0006 249 LEU A CD2   
1969 N N     . ARG A 250 ? 0.0299 0.0553 0.0392 -0.0104 0.0171  -0.0045 250 ARG A N     
1970 C CA    . ARG A 250 ? 0.2173 0.2421 0.2255 -0.0112 0.0179  -0.0051 250 ARG A CA    
1971 C C     . ARG A 250 ? 0.3273 0.3526 0.3361 -0.0108 0.0171  -0.0051 250 ARG A C     
1972 O O     . ARG A 250 ? 0.4878 0.5134 0.4960 -0.0108 0.0165  -0.0050 250 ARG A O     
1973 C CB    . ARG A 250 ? 0.2144 0.2373 0.2216 -0.0127 0.0208  -0.0064 250 ARG A CB    
1974 C CG    . ARG A 250 ? 0.1452 0.1669 0.1506 -0.0136 0.0220  -0.0069 250 ARG A CG    
1975 C CD    . ARG A 250 ? 0.1621 0.1811 0.1657 -0.0149 0.0252  -0.0077 250 ARG A CD    
1976 N NE    . ARG A 250 ? 0.3034 0.3207 0.3073 -0.0157 0.0273  -0.0087 250 ARG A NE    
1977 C CZ    . ARG A 250 ? 0.2584 0.2753 0.2633 -0.0158 0.0280  -0.0090 250 ARG A CZ    
1978 N NH1   . ARG A 250 ? 0.2620 0.2800 0.2675 -0.0152 0.0268  -0.0084 250 ARG A NH1   
1979 N NH2   . ARG A 250 ? 0.2875 0.3026 0.2926 -0.0165 0.0301  -0.0100 250 ARG A NH2   
1980 N N     . HIS A 251 ? 0.2990 0.3246 0.3092 -0.0104 0.0172  -0.0050 251 HIS A N     
1981 C CA    . HIS A 251 ? 0.2945 0.3205 0.3055 -0.0101 0.0169  -0.0050 251 HIS A CA    
1982 C C     . HIS A 251 ? 0.1714 0.1982 0.1830 -0.0087 0.0148  -0.0036 251 HIS A C     
1983 O O     . HIS A 251 ? 0.0250 0.0520 0.0366 -0.0087 0.0144  -0.0037 251 HIS A O     
1984 C CB    . HIS A 251 ? 0.2864 0.3122 0.2986 -0.0101 0.0179  -0.0053 251 HIS A CB    
1985 C CG    . HIS A 251 ? 0.2005 0.2249 0.2121 -0.0116 0.0204  -0.0069 251 HIS A CG    
1986 N ND1   . HIS A 251 ? 0.1333 0.1562 0.1431 -0.0128 0.0219  -0.0078 251 HIS A ND1   
1987 C CD2   . HIS A 251 ? 0.0370 0.0607 0.0493 -0.0120 0.0219  -0.0076 251 HIS A CD2   
1988 C CE1   . HIS A 251 ? 0.1574 0.1785 0.1669 -0.0139 0.0244  -0.0090 251 HIS A CE1   
1989 N NE2   . HIS A 251 ? 0.0409 0.0625 0.0519 -0.0135 0.0243  -0.0090 251 HIS A NE2   
1990 N N     . ALA A 252 ? 0.0231 0.0502 0.0350 -0.0076 0.0135  -0.0024 252 ALA A N     
1991 C CA    . ALA A 252 ? 0.0203 0.0475 0.0325 -0.0065 0.0117  -0.0011 252 ALA A CA    
1992 C C     . ALA A 252 ? 0.1075 0.1349 0.1182 -0.0067 0.0107  -0.0012 252 ALA A C     
1993 O O     . ALA A 252 ? 0.4289 0.4565 0.4398 -0.0060 0.0096  -0.0005 252 ALA A O     
1994 C CB    . ALA A 252 ? 0.0186 0.0455 0.0310 -0.0055 0.0107  -0.0001 252 ALA A CB    
1995 N N     . PHE A 253 ? 0.0387 0.0662 0.0481 -0.0076 0.0111  -0.0019 253 PHE A N     
1996 C CA    . PHE A 253 ? 0.1650 0.1930 0.1732 -0.0080 0.0104  -0.0021 253 PHE A CA    
1997 C C     . PHE A 253 ? 0.2775 0.3056 0.2856 -0.0087 0.0112  -0.0030 253 PHE A C     
1998 O O     . PHE A 253 ? 0.4008 0.4295 0.4086 -0.0084 0.0100  -0.0027 253 PHE A O     
1999 C CB    . PHE A 253 ? 0.1192 0.1469 0.1262 -0.0088 0.0111  -0.0026 253 PHE A CB    
2000 C CG    . PHE A 253 ? 0.0231 0.0511 0.0287 -0.0094 0.0107  -0.0027 253 PHE A CG    
2001 C CD1   . PHE A 253 ? 0.0260 0.0535 0.0309 -0.0106 0.0124  -0.0037 253 PHE A CD1   
2002 C CD2   . PHE A 253 ? 0.2296 0.2585 0.2345 -0.0087 0.0088  -0.0018 253 PHE A CD2   
2003 C CE1   . PHE A 253 ? 0.0267 0.0545 0.0302 -0.0111 0.0122  -0.0037 253 PHE A CE1   
2004 C CE2   . PHE A 253 ? 0.0213 0.0507 0.0251 -0.0093 0.0084  -0.0019 253 PHE A CE2   
2005 C CZ    . PHE A 253 ? 0.0242 0.0530 0.0273 -0.0104 0.0102  -0.0028 253 PHE A CZ    
2006 N N     . THR A 254 ? 0.2523 0.2797 0.2605 -0.0097 0.0132  -0.0041 254 THR A N     
2007 C CA    . THR A 254 ? 0.3371 0.3643 0.3449 -0.0106 0.0142  -0.0051 254 THR A CA    
2008 C C     . THR A 254 ? 0.0876 0.1154 0.0970 -0.0098 0.0134  -0.0047 254 THR A C     
2009 O O     . THR A 254 ? 0.0257 0.0537 0.0350 -0.0102 0.0136  -0.0054 254 THR A O     
2010 C CB    . THR A 254 ? 0.3575 0.3833 0.3647 -0.0119 0.0168  -0.0063 254 THR A CB    
2011 O OG1   . THR A 254 ? 0.2213 0.2471 0.2300 -0.0114 0.0171  -0.0062 254 THR A OG1   
2012 C CG2   . THR A 254 ? 0.0343 0.0589 0.0398 -0.0128 0.0183  -0.0066 254 THR A CG2   
2013 N N     . ALA A 255 ? 0.0232 0.0510 0.0341 -0.0086 0.0127  -0.0036 255 ALA A N     
2014 C CA    . ALA A 255 ? 0.0216 0.0495 0.0344 -0.0076 0.0123  -0.0028 255 ALA A CA    
2015 C C     . ALA A 255 ? 0.4982 0.5266 0.5112 -0.0069 0.0109  -0.0020 255 ALA A C     
2016 O O     . ALA A 255 ? 0.4471 0.4756 0.4613 -0.0068 0.0110  -0.0020 255 ALA A O     
2017 C CB    . ALA A 255 ? 0.1768 0.2044 0.1911 -0.0065 0.0122  -0.0015 255 ALA A CB    
2018 N N     . ILE A 256 ? 0.8265 0.8549 0.8382 -0.0066 0.0096  -0.0013 256 ILE A N     
2019 C CA    . ILE A 256 ? 0.0168 0.0455 0.0283 -0.0060 0.0082  -0.0004 256 ILE A CA    
2020 C C     . ILE A 256 ? 0.1460 0.1756 0.1565 -0.0069 0.0082  -0.0015 256 ILE A C     
2021 O O     . ILE A 256 ? 0.4998 0.5297 0.5113 -0.0065 0.0078  -0.0011 256 ILE A O     
2022 C CB    . ILE A 256 ? 0.0156 0.0442 0.0255 -0.0054 0.0068  0.0007  256 ILE A CB    
2023 C CG1   . ILE A 256 ? 0.0150 0.0428 0.0258 -0.0046 0.0069  0.0015  256 ILE A CG1   
2024 C CG2   . ILE A 256 ? 0.0141 0.0429 0.0236 -0.0046 0.0054  0.0020  256 ILE A CG2   
2025 C CD1   . ILE A 256 ? 0.0145 0.0414 0.0278 -0.0039 0.0074  0.0022  256 ILE A CD1   
2026 N N     . GLN A 257 ? 0.0196 0.0495 0.0283 -0.0082 0.0089  -0.0028 257 GLN A N     
2027 C CA    . GLN A 257 ? 0.0210 0.0516 0.0286 -0.0093 0.0092  -0.0040 257 GLN A CA    
2028 C C     . GLN A 257 ? 0.0467 0.0774 0.0557 -0.0095 0.0101  -0.0048 257 GLN A C     
2029 O O     . GLN A 257 ? 0.3238 0.3553 0.3329 -0.0097 0.0097  -0.0053 257 GLN A O     
2030 C CB    . GLN A 257 ? 0.2803 0.3104 0.2862 -0.0107 0.0107  -0.0050 257 GLN A CB    
2031 C CG    . GLN A 257 ? 0.1913 0.2212 0.1960 -0.0107 0.0102  -0.0044 257 GLN A CG    
2032 C CD    . GLN A 257 ? 0.2601 0.2886 0.2634 -0.0121 0.0127  -0.0052 257 GLN A CD    
2033 O OE1   . GLN A 257 ? 0.2289 0.2561 0.2324 -0.0126 0.0146  -0.0058 257 GLN A OE1   
2034 N NE2   . GLN A 257 ? 0.2537 0.2820 0.2553 -0.0126 0.0129  -0.0050 257 GLN A NE2   
2035 N N     . TYR A 258 ? 0.0226 0.0525 0.0328 -0.0095 0.0113  -0.0051 258 TYR A N     
2036 C CA    . TYR A 258 ? 0.1120 0.1420 0.1235 -0.0099 0.0122  -0.0061 258 TYR A CA    
2037 C C     . TYR A 258 ? 0.0213 0.0518 0.0356 -0.0086 0.0114  -0.0050 258 TYR A C     
2038 O O     . TYR A 258 ? 0.0216 0.0527 0.0368 -0.0089 0.0114  -0.0058 258 TYR A O     
2039 C CB    . TYR A 258 ? 0.0875 0.1166 0.0997 -0.0101 0.0137  -0.0065 258 TYR A CB    
2040 C CG    . TYR A 258 ? 0.0266 0.0555 0.0397 -0.0107 0.0148  -0.0077 258 TYR A CG    
2041 C CD1   . TYR A 258 ? 0.1791 0.2076 0.1905 -0.0122 0.0161  -0.0095 258 TYR A CD1   
2042 C CD2   . TYR A 258 ? 0.0253 0.0543 0.0411 -0.0097 0.0146  -0.0070 258 TYR A CD2   
2043 C CE1   . TYR A 258 ? 0.0936 0.1219 0.1058 -0.0128 0.0171  -0.0107 258 TYR A CE1   
2044 C CE2   . TYR A 258 ? 0.0746 0.1036 0.0915 -0.0102 0.0156  -0.0083 258 TYR A CE2   
2045 C CZ    . TYR A 258 ? 0.1890 0.2176 0.2040 -0.0118 0.0168  -0.0102 258 TYR A CZ    
2046 O OH    . TYR A 258 ? 0.3589 0.3873 0.3750 -0.0123 0.0178  -0.0116 258 TYR A OH    
2047 N N     . ARG A 259 ? 0.0193 0.0493 0.0354 -0.0072 0.0107  -0.0030 259 ARG A N     
2048 C CA    . ARG A 259 ? 0.0187 0.0484 0.0383 -0.0060 0.0104  -0.0014 259 ARG A CA    
2049 C C     . ARG A 259 ? 0.1233 0.1536 0.1433 -0.0059 0.0094  -0.0012 259 ARG A C     
2050 O O     . ARG A 259 ? 0.1126 0.1428 0.1369 -0.0051 0.0093  0.0002  259 ARG A O     
2051 C CB    . ARG A 259 ? 0.0162 0.0445 0.0375 -0.0048 0.0103  0.0005  259 ARG A CB    
2052 C CG    . ARG A 259 ? 0.0154 0.0434 0.0340 -0.0047 0.0091  0.0008  259 ARG A CG    
2053 C CD    . ARG A 259 ? 0.0140 0.0408 0.0338 -0.0039 0.0084  0.0019  259 ARG A CD    
2054 N NE    . ARG A 259 ? 0.0140 0.0399 0.0339 -0.0035 0.0087  0.0021  259 ARG A NE    
2055 C CZ    . ARG A 259 ? 0.1351 0.1607 0.1539 -0.0027 0.0075  0.0037  259 ARG A CZ    
2056 N NH1   . ARG A 259 ? 0.2177 0.2430 0.2354 -0.0020 0.0061  0.0054  259 ARG A NH1   
2057 N NH2   . ARG A 259 ? 0.0988 0.1240 0.1175 -0.0024 0.0076  0.0041  259 ARG A NH2   
2058 N N     . GLN A 260 ? 0.0197 0.0507 0.0360 -0.0067 0.0087  -0.0021 260 GLN A N     
2059 C CA    . GLN A 260 ? 0.1963 0.2282 0.2128 -0.0067 0.0078  -0.0019 260 GLN A CA    
2060 C C     . GLN A 260 ? 0.3500 0.3834 0.3644 -0.0081 0.0080  -0.0041 260 GLN A C     
2061 O O     . GLN A 260 ? 0.3337 0.3682 0.3466 -0.0084 0.0071  -0.0043 260 GLN A O     
2062 C CB    . GLN A 260 ? 0.1105 0.1423 0.1247 -0.0063 0.0065  -0.0008 260 GLN A CB    
2063 C CG    . GLN A 260 ? 0.3170 0.3472 0.3326 -0.0051 0.0062  0.0011  260 GLN A CG    
2064 C CD    . GLN A 260 ? 0.4098 0.4400 0.4216 -0.0049 0.0048  0.0021  260 GLN A CD    
2065 O OE1   . GLN A 260 ? 0.0130 0.0422 0.0248 -0.0040 0.0044  0.0034  260 GLN A OE1   
2066 N NE2   . GLN A 260 ? 0.0144 0.0458 0.0231 -0.0057 0.0042  0.0014  260 GLN A NE2   
2067 N N     . GLY A 261 ? 0.1430 0.1764 0.1570 -0.0090 0.0092  -0.0057 261 GLY A N     
2068 C CA    . GLY A 261 ? 0.0219 0.0562 0.0346 -0.0103 0.0098  -0.0079 261 GLY A CA    
2069 C C     . GLY A 261 ? 0.2114 0.2457 0.2200 -0.0119 0.0102  -0.0089 261 GLY A C     
2070 O O     . GLY A 261 ? 0.1608 0.1955 0.1680 -0.0132 0.0111  -0.0104 261 GLY A O     
2071 N N     . PHE A 262 ? 0.3189 0.3524 0.3257 -0.0120 0.0101  -0.0080 262 PHE A N     
2072 C CA    . PHE A 262 ? 0.3440 0.3768 0.3479 -0.0133 0.0112  -0.0084 262 PHE A CA    
2073 C C     . PHE A 262 ? 0.3840 0.4146 0.3869 -0.0144 0.0139  -0.0093 262 PHE A C     
2074 O O     . PHE A 262 ? 0.3364 0.3664 0.3408 -0.0140 0.0144  -0.0093 262 PHE A O     
2075 C CB    . PHE A 262 ? 0.4688 0.5011 0.4719 -0.0128 0.0104  -0.0071 262 PHE A CB    
2076 C CG    . PHE A 262 ? 0.3625 0.3933 0.3630 -0.0140 0.0122  -0.0071 262 PHE A CG    
2077 C CD1   . PHE A 262 ? 0.3442 0.3751 0.3426 -0.0145 0.0122  -0.0068 262 PHE A CD1   
2078 C CD2   . PHE A 262 ? 0.3414 0.3700 0.3413 -0.0143 0.0144  -0.0070 262 PHE A CD2   
2079 C CE1   . PHE A 262 ? 0.4190 0.4470 0.4138 -0.0150 0.0148  -0.0062 262 PHE A CE1   
2080 C CE2   . PHE A 262 ? 0.3957 0.4217 0.3923 -0.0149 0.0168  -0.0066 262 PHE A CE2   
2081 C CZ    . PHE A 262 ? 0.4438 0.4691 0.4375 -0.0151 0.0172  -0.0061 262 PHE A CZ    
2082 N N     . HIS A 263 ? 0.4879 0.5171 0.4878 -0.0155 0.0160  -0.0098 263 HIS A N     
2083 C CA    . HIS A 263 ? 0.4055 0.4316 0.4031 -0.0163 0.0192  -0.0102 263 HIS A CA    
2084 C C     . HIS A 263 ? 0.4301 0.4525 0.4222 -0.0166 0.0220  -0.0094 263 HIS A C     
2085 O O     . HIS A 263 ? 0.4237 0.4427 0.4115 -0.0169 0.0250  -0.0096 263 HIS A O     
2086 C CB    . HIS A 263 ? 0.4428 0.4691 0.4406 -0.0167 0.0199  -0.0115 263 HIS A CB    
2087 C CG    . HIS A 263 ? 0.4751 0.5041 0.4777 -0.0161 0.0177  -0.0123 263 HIS A CG    
2088 N ND1   . HIS A 263 ? 0.5126 0.5421 0.5177 -0.0151 0.0165  -0.0115 263 HIS A ND1   
2089 C CD2   . HIS A 263 ? 0.4824 0.5130 0.4869 -0.0160 0.0170  -0.0134 263 HIS A CD2   
2090 C CE1   . HIS A 263 ? 0.4518 0.4825 0.4599 -0.0142 0.0154  -0.0118 263 HIS A CE1   
2091 N NE2   . HIS A 263 ? 0.5458 0.5774 0.5540 -0.0148 0.0156  -0.0130 263 HIS A NE2   
2092 N N     . GLY A 264 ? 0.3159 0.3384 0.3071 -0.0162 0.0213  -0.0083 264 GLY A N     
2093 C CA    . GLY A 264 ? 0.1737 0.1919 0.1584 -0.0159 0.0241  -0.0073 264 GLY A CA    
2094 C C     . GLY A 264 ? 0.1306 0.1479 0.1110 -0.0151 0.0235  -0.0066 264 GLY A C     
2095 O O     . GLY A 264 ? 0.5617 0.5825 0.5451 -0.0151 0.0208  -0.0070 264 GLY A O     
2096 N N     . LEU A 265 ? 0.1684 0.1807 0.1407 -0.0142 0.0259  -0.0056 265 LEU A N     
2097 C CA    . LEU A 265 ? 0.1259 0.1357 0.0913 -0.0126 0.0254  -0.0047 265 LEU A CA    
2098 C C     . LEU A 265 ? 0.2377 0.2426 0.1921 -0.0107 0.0260  -0.0054 265 LEU A C     
2099 O O     . LEU A 265 ? 0.3804 0.3836 0.3326 -0.0108 0.0275  -0.0064 265 LEU A O     
2100 C CB    . LEU A 265 ? 0.2989 0.3058 0.2608 -0.0123 0.0268  -0.0036 265 LEU A CB    
2101 C CG    . LEU A 265 ? 0.0700 0.0800 0.0395 -0.0135 0.0263  -0.0032 265 LEU A CG    
2102 C CD1   . LEU A 265 ? 0.1293 0.1366 0.0942 -0.0127 0.0271  -0.0020 265 LEU A CD1   
2103 C CD2   . LEU A 265 ? 0.3676 0.3837 0.3464 -0.0142 0.0227  -0.0036 265 LEU A CD2   
2104 N N     . ASN A 266 ? 0.0893 0.0914 0.0357 -0.0085 0.0242  -0.0053 266 ASN A N     
2105 C CA    . ASN A 266 ? 0.1381 0.1353 0.0722 -0.0060 0.0227  -0.0070 266 ASN A CA    
2106 C C     . ASN A 266 ? 0.3073 0.2977 0.2314 -0.0059 0.0251  -0.0071 266 ASN A C     
2107 O O     . ASN A 266 ? 0.3275 0.3166 0.2531 -0.0072 0.0277  -0.0056 266 ASN A O     
2108 C CB    . ASN A 266 ? 0.2763 0.2733 0.2057 -0.0037 0.0179  -0.0078 266 ASN A CB    
2109 C CG    . ASN A 266 ? 0.2348 0.2306 0.1616 -0.0036 0.0176  -0.0063 266 ASN A CG    
2110 O OD1   . ASN A 266 ? 0.1391 0.1298 0.0554 -0.0028 0.0160  -0.0073 266 ASN A OD1   
2111 N ND2   . ASN A 266 ? 0.0950 0.0944 0.0314 -0.0052 0.0190  -0.0041 266 ASN A ND2   
2112 N N     . ILE A 267 ? 0.3241 0.3091 0.2376 -0.0045 0.0240  -0.0092 267 ILE A N     
2113 C CA    . ILE A 267 ? 0.4392 0.4153 0.3426 -0.0046 0.0269  -0.0094 267 ILE A CA    
2114 C C     . ILE A 267 ? 0.4025 0.3733 0.3007 -0.0046 0.0281  -0.0078 267 ILE A C     
2115 O O     . ILE A 267 ? 0.4768 0.4427 0.3728 -0.0054 0.0320  -0.0068 267 ILE A O     
2116 C CB    . ILE A 267 ? 0.4379 0.4078 0.3299 -0.0027 0.0242  -0.0122 267 ILE A CB    
2117 C CG1   . ILE A 267 ? 0.5264 0.5001 0.4231 -0.0029 0.0247  -0.0137 267 ILE A CG1   
2118 C CG2   . ILE A 267 ? 0.4071 0.3654 0.2863 -0.0019 0.0265  -0.0118 267 ILE A CG2   
2119 C CD1   . ILE A 267 ? 0.5755 0.5455 0.4640 -0.0012 0.0208  -0.0173 267 ILE A CD1   
2120 N N     . PHE A 268 ? 0.5244 0.4951 0.4197 -0.0036 0.0246  -0.0077 268 PHE A N     
2121 C CA    . PHE A 268 ? 0.5163 0.4808 0.4052 -0.0033 0.0253  -0.0064 268 PHE A CA    
2122 C C     . PHE A 268 ? 0.2829 0.2532 0.1819 -0.0049 0.0274  -0.0043 268 PHE A C     
2123 O O     . PHE A 268 ? 0.3251 0.2902 0.2201 -0.0050 0.0294  -0.0032 268 PHE A O     
2124 C CB    . PHE A 268 ? 0.4102 0.3709 0.2908 -0.0015 0.0202  -0.0074 268 PHE A CB    
2125 C CG    . PHE A 268 ? 0.3192 0.2729 0.1893 0.0004  0.0173  -0.0100 268 PHE A CG    
2126 C CD1   . PHE A 268 ? 0.1958 0.1380 0.0532 0.0019  0.0189  -0.0101 268 PHE A CD1   
2127 C CD2   . PHE A 268 ? 0.2126 0.1710 0.0857 0.0007  0.0127  -0.0124 268 PHE A CD2   
2128 C CE1   . PHE A 268 ? 0.2382 0.1735 0.0860 0.0039  0.0159  -0.0125 268 PHE A CE1   
2129 C CE2   . PHE A 268 ? 0.2538 0.2056 0.1179 0.0023  0.0095  -0.0151 268 PHE A CE2   
2130 C CZ    . PHE A 268 ? 0.2340 0.1742 0.0853 0.0040  0.0111  -0.0151 268 PHE A CZ    
2131 N N     . ALA A 269 ? 0.3207 0.3007 0.2323 -0.0059 0.0266  -0.0038 269 ALA A N     
2132 C CA    . ALA A 269 ? 0.3286 0.3135 0.2504 -0.0075 0.0283  -0.0022 269 ALA A CA    
2133 C C     . ALA A 269 ? 0.2909 0.2726 0.2135 -0.0089 0.0325  -0.0021 269 ALA A C     
2134 O O     . ALA A 269 ? 0.2628 0.2433 0.1868 -0.0097 0.0342  -0.0013 269 ALA A O     
2135 C CB    . ALA A 269 ? 0.4151 0.4089 0.3494 -0.0080 0.0265  -0.0019 269 ALA A CB    
2136 N N     . TYR A 270 ? 0.2876 0.2682 0.2098 -0.0093 0.0340  -0.0031 270 TYR A N     
2137 C CA    . TYR A 270 ? 0.2315 0.2077 0.1528 -0.0104 0.0379  -0.0031 270 TYR A CA    
2138 C C     . TYR A 270 ? 0.3273 0.2931 0.2360 -0.0093 0.0400  -0.0029 270 TYR A C     
2139 O O     . TYR A 270 ? 0.4560 0.4183 0.3643 -0.0099 0.0427  -0.0022 270 TYR A O     
2140 C CB    . TYR A 270 ? 0.2841 0.2603 0.2065 -0.0109 0.0391  -0.0042 270 TYR A CB    
2141 C CG    . TYR A 270 ? 0.1187 0.1035 0.0536 -0.0121 0.0377  -0.0045 270 TYR A CG    
2142 C CD1   . TYR A 270 ? 0.1074 0.0970 0.0519 -0.0134 0.0374  -0.0041 270 TYR A CD1   
2143 C CD2   . TYR A 270 ? 0.1143 0.1016 0.0506 -0.0118 0.0365  -0.0055 270 TYR A CD2   
2144 C CE1   . TYR A 270 ? 0.0958 0.0918 0.0504 -0.0144 0.0357  -0.0046 270 TYR A CE1   
2145 C CE2   . TYR A 270 ? 0.1022 0.0962 0.0492 -0.0130 0.0352  -0.0058 270 TYR A CE2   
2146 C CZ    . TYR A 270 ? 0.0933 0.0913 0.0492 -0.0142 0.0347  -0.0054 270 TYR A CZ    
2147 O OH    . TYR A 270 ? 0.1191 0.1227 0.0844 -0.0152 0.0329  -0.0061 270 TYR A OH    
2148 N N     . THR A 271 ? 0.1782 0.1385 0.0762 -0.0074 0.0384  -0.0035 271 THR A N     
2149 C CA    . THR A 271 ? 0.1880 0.1367 0.0725 -0.0059 0.0403  -0.0033 271 THR A CA    
2150 C C     . THR A 271 ? 0.2672 0.2131 0.1495 -0.0056 0.0406  -0.0020 271 THR A C     
2151 O O     . THR A 271 ? 0.3282 0.2657 0.2035 -0.0051 0.0438  -0.0014 271 THR A O     
2152 C CB    . THR A 271 ? 0.1858 0.1293 0.0594 -0.0037 0.0373  -0.0046 271 THR A CB    
2153 O OG1   . THR A 271 ? 0.2606 0.2085 0.1380 -0.0041 0.0365  -0.0059 271 THR A OG1   
2154 C CG2   . THR A 271 ? 0.2052 0.1356 0.0644 -0.0018 0.0394  -0.0045 271 THR A CG2   
2155 N N     . ALA A 272 ? 0.3889 0.3412 0.2764 -0.0058 0.0373  -0.0016 272 ALA A N     
2156 C CA    . ALA A 272 ? 0.4716 0.4221 0.3579 -0.0056 0.0374  -0.0004 272 ALA A CA    
2157 C C     . ALA A 272 ? 0.3864 0.3409 0.2822 -0.0075 0.0402  0.0003  272 ALA A C     
2158 O O     . ALA A 272 ? 0.5101 0.4593 0.4023 -0.0073 0.0424  0.0010  272 ALA A O     
2159 C CB    . ALA A 272 ? 0.5079 0.4641 0.3970 -0.0050 0.0328  -0.0003 272 ALA A CB    
2160 N N     . MET A 273 ? 0.1742 0.1378 0.0820 -0.0090 0.0397  0.0000  273 MET A N     
2161 C CA    . MET A 273 ? 0.2721 0.2395 0.1890 -0.0106 0.0414  0.0002  273 MET A CA    
2162 C C     . MET A 273 ? 0.5166 0.4768 0.4295 -0.0111 0.0458  -0.0001 273 MET A C     
2163 O O     . MET A 273 ? 0.5778 0.5363 0.4922 -0.0116 0.0478  0.0003  273 MET A O     
2164 C CB    . MET A 273 ? 0.4062 0.3835 0.3353 -0.0118 0.0393  -0.0002 273 MET A CB    
2165 C CG    . MET A 273 ? 0.5203 0.5022 0.4591 -0.0131 0.0397  -0.0002 273 MET A CG    
2166 S SD    . MET A 273 ? 0.4628 0.4508 0.4116 -0.0142 0.0390  -0.0014 273 MET A SD    
2167 C CE    . MET A 273 ? 0.4877 0.4805 0.4383 -0.0135 0.0358  -0.0014 273 MET A CE    
2168 N N     . GLN A 274 ? 0.4566 0.4122 0.3640 -0.0107 0.0473  -0.0007 274 GLN A N     
2169 C CA    . GLN A 274 ? 0.3959 0.3442 0.2991 -0.0110 0.0517  -0.0009 274 GLN A CA    
2170 C C     . GLN A 274 ? 0.4806 0.4193 0.3740 -0.0097 0.0541  -0.0001 274 GLN A C     
2171 O O     . GLN A 274 ? 0.6626 0.5973 0.5560 -0.0102 0.0576  0.0001  274 GLN A O     
2172 C CB    . GLN A 274 ? 0.3371 0.2819 0.2354 -0.0105 0.0526  -0.0016 274 GLN A CB    
2173 C CG    . GLN A 274 ? 0.4892 0.4263 0.3832 -0.0107 0.0572  -0.0018 274 GLN A CG    
2174 C CD    . GLN A 274 ? 0.7053 0.6394 0.5948 -0.0102 0.0580  -0.0025 274 GLN A CD    
2175 O OE1   . GLN A 274 ? 0.7932 0.7247 0.6752 -0.0086 0.0561  -0.0027 274 GLN A OE1   
2176 N NE2   . GLN A 274 ? 0.7352 0.6696 0.6291 -0.0115 0.0605  -0.0031 274 GLN A NE2   
2177 N N     . SER A 275 ? 0.2893 0.2235 0.1736 -0.0079 0.0524  0.0004  275 SER A N     
2178 C CA    . SER A 275 ? 0.4439 0.3684 0.3181 -0.0063 0.0545  0.0013  275 SER A CA    
2179 C C     . SER A 275 ? 0.5079 0.4360 0.3877 -0.0070 0.0541  0.0020  275 SER A C     
2180 O O     . SER A 275 ? 0.3673 0.2894 0.2439 -0.0068 0.0573  0.0025  275 SER A O     
2181 C CB    . SER A 275 ? 0.6092 0.5274 0.4714 -0.0039 0.0521  0.0013  275 SER A CB    
2182 O OG    . SER A 275 ? 0.6738 0.5842 0.5269 -0.0026 0.0538  0.0008  275 SER A OG    
2183 N N     . ALA A 276 ? 0.5369 0.4745 0.4249 -0.0078 0.0503  0.0020  276 ALA A N     
2184 C CA    . ALA A 276 ? 0.4968 0.4383 0.3902 -0.0084 0.0495  0.0027  276 ALA A CA    
2185 C C     . ALA A 276 ? 0.3896 0.3318 0.2892 -0.0098 0.0525  0.0025  276 ALA A C     
2186 O O     . ALA A 276 ? 0.4926 0.4334 0.3924 -0.0097 0.0535  0.0031  276 ALA A O     
2187 C CB    . ALA A 276 ? 0.5748 0.5277 0.4782 -0.0092 0.0451  0.0026  276 ALA A CB    
2188 N N     . TYR A 277 ? 0.3425 0.2869 0.2473 -0.0110 0.0539  0.0016  277 TYR A N     
2189 C CA    . TYR A 277 ? 0.3234 0.2688 0.2344 -0.0122 0.0563  0.0012  277 TYR A CA    
2190 C C     . TYR A 277 ? 0.2864 0.2216 0.1900 -0.0118 0.0612  0.0012  277 TYR A C     
2191 O O     . TYR A 277 ? 0.1946 0.1298 0.1028 -0.0128 0.0635  0.0007  277 TYR A O     
2192 C CB    . TYR A 277 ? 0.3393 0.2930 0.2608 -0.0137 0.0547  0.0002  277 TYR A CB    
2193 C CG    . TYR A 277 ? 0.2890 0.2529 0.2196 -0.0142 0.0504  0.0002  277 TYR A CG    
2194 C CD1   . TYR A 277 ? 0.3706 0.3364 0.3011 -0.0136 0.0484  0.0011  277 TYR A CD1   
2195 C CD2   . TYR A 277 ? 0.2317 0.2029 0.1708 -0.0150 0.0482  -0.0006 277 TYR A CD2   
2196 C CE1   . TYR A 277 ? 0.4927 0.4674 0.4314 -0.0138 0.0445  0.0013  277 TYR A CE1   
2197 C CE2   . TYR A 277 ? 0.3900 0.3698 0.3370 -0.0151 0.0443  -0.0004 277 TYR A CE2   
2198 C CZ    . TYR A 277 ? 0.4676 0.4491 0.4144 -0.0144 0.0425  0.0005  277 TYR A CZ    
2199 O OH    . TYR A 277 ? 0.4516 0.4410 0.4059 -0.0143 0.0388  0.0008  277 TYR A OH    
2200 N N     . THR A 278 ? 0.4000 0.3264 0.2921 -0.0102 0.0628  0.0017  278 THR A N     
2201 C CA    . THR A 278 ? 0.2570 0.1733 0.1417 -0.0095 0.0676  0.0018  278 THR A CA    
2202 C C     . THR A 278 ? 0.3557 0.2613 0.2284 -0.0074 0.0699  0.0029  278 THR A C     
2203 O O     . THR A 278 ? 0.6253 0.5246 0.4956 -0.0072 0.0739  0.0032  278 THR A O     
2204 C CB    . THR A 278 ? 0.4564 0.3706 0.3377 -0.0092 0.0681  0.0012  278 THR A CB    
2205 O OG1   . THR A 278 ? 0.4687 0.3861 0.3477 -0.0084 0.0642  0.0012  278 THR A OG1   
2206 C CG2   . THR A 278 ? 0.4892 0.4100 0.3808 -0.0112 0.0684  0.0001  278 THR A CG2   
2207 N N     . GLU A 279 ? 0.3149 0.2178 0.1797 -0.0056 0.0674  0.0034  279 GLU A N     
2208 C CA    . GLU A 279 ? 0.3716 0.2629 0.2232 -0.0031 0.0693  0.0044  279 GLU A CA    
2209 C C     . GLU A 279 ? 0.4359 0.3277 0.2854 -0.0021 0.0667  0.0052  279 GLU A C     
2210 O O     . GLU A 279 ? 0.5685 0.4510 0.4062 0.0003  0.0672  0.0059  279 GLU A O     
2211 C CB    . GLU A 279 ? 0.4766 0.3607 0.3171 -0.0011 0.0691  0.0043  279 GLU A CB    
2212 C CG    . GLU A 279 ? 0.7513 0.6422 0.5937 -0.0011 0.0640  0.0036  279 GLU A CG    
2213 C CD    . GLU A 279 ? 0.8277 0.7151 0.6643 -0.0003 0.0641  0.0029  279 GLU A CD    
2214 O OE1   . GLU A 279 ? 0.7773 0.6571 0.6087 0.0003  0.0682  0.0029  279 GLU A OE1   
2215 O OE2   . GLU A 279 ? 0.7857 0.6774 0.6224 0.0000  0.0600  0.0022  279 GLU A OE2   
2216 N N     . CYS A 280 ? 0.3177 0.2200 0.1780 -0.0039 0.0638  0.0050  280 CYS A N     
2217 C CA    . CYS A 280 ? 0.3906 0.2942 0.2494 -0.0030 0.0609  0.0057  280 CYS A CA    
2218 C C     . CYS A 280 ? 0.5042 0.4108 0.3698 -0.0042 0.0622  0.0061  280 CYS A C     
2219 O O     . CYS A 280 ? 0.5947 0.5055 0.4628 -0.0042 0.0594  0.0066  280 CYS A O     
2220 C CB    . CYS A 280 ? 0.3836 0.2968 0.2483 -0.0037 0.0557  0.0053  280 CYS A CB    
2221 S SG    . CYS A 280 ? 0.4909 0.4012 0.3477 -0.0022 0.0532  0.0047  280 CYS A SG    
2222 N N     . ASN A 281 ? 0.4740 0.3782 0.3423 -0.0050 0.0663  0.0058  281 ASN A N     
2223 C CA    . ASN A 281 ? 0.3775 0.2859 0.2538 -0.0063 0.0672  0.0058  281 ASN A CA    
2224 C C     . ASN A 281 ? 0.3328 0.2360 0.2032 -0.0049 0.0677  0.0069  281 ASN A C     
2225 O O     . ASN A 281 ? 0.2262 0.1355 0.1033 -0.0058 0.0659  0.0070  281 ASN A O     
2226 C CB    . ASN A 281 ? 0.3171 0.2225 0.1961 -0.0073 0.0715  0.0052  281 ASN A CB    
2227 C CG    . ASN A 281 ? 0.3248 0.2348 0.2091 -0.0086 0.0710  0.0041  281 ASN A CG    
2228 O OD1   . ASN A 281 ? 0.3797 0.2995 0.2748 -0.0103 0.0685  0.0033  281 ASN A OD1   
2229 N ND2   . ASN A 281 ? 0.3075 0.2105 0.1840 -0.0076 0.0731  0.0042  281 ASN A ND2   
2230 N N     . ASP A 282 ? 0.2789 0.1707 0.1366 -0.0026 0.0700  0.0077  282 ASP A N     
2231 C CA    . ASP A 282 ? 0.3539 0.2400 0.2055 -0.0011 0.0708  0.0087  282 ASP A CA    
2232 C C     . ASP A 282 ? 0.4940 0.3845 0.3451 -0.0005 0.0658  0.0092  282 ASP A C     
2233 O O     . ASP A 282 ? 0.3422 0.2331 0.1937 -0.0002 0.0652  0.0098  282 ASP A O     
2234 C CB    . ASP A 282 ? 0.4681 0.3402 0.3058 0.0016  0.0747  0.0095  282 ASP A CB    
2235 C CG    . ASP A 282 ? 0.7932 0.6608 0.6230 0.0030  0.0739  0.0093  282 ASP A CG    
2236 O OD1   . ASP A 282 ? 0.8803 0.7557 0.7163 0.0015  0.0711  0.0084  282 ASP A OD1   
2237 O OD2   . ASP A 282 ? 0.9479 0.8039 0.7649 0.0057  0.0762  0.0100  282 ASP A OD2   
2238 N N     . TRP A 283 ? 0.7094 0.6027 0.5591 -0.0002 0.0622  0.0088  283 TRP A N     
2239 C CA    . TRP A 283 ? 0.5782 0.4766 0.4286 0.0002  0.0572  0.0091  283 TRP A CA    
2240 C C     . TRP A 283 ? 0.5929 0.5035 0.4569 -0.0021 0.0549  0.0089  283 TRP A C     
2241 O O     . TRP A 283 ? 0.7877 0.7017 0.6528 -0.0018 0.0518  0.0095  283 TRP A O     
2242 C CB    . TRP A 283 ? 0.3556 0.2549 0.2028 0.0008  0.0541  0.0085  283 TRP A CB    
2243 C CG    . TRP A 283 ? 0.4617 0.3650 0.3083 0.0015  0.0488  0.0086  283 TRP A CG    
2244 C CD1   . TRP A 283 ? 0.4041 0.2997 0.2391 0.0041  0.0465  0.0090  283 TRP A CD1   
2245 C CD2   . TRP A 283 ? 0.4348 0.3503 0.2929 -0.0003 0.0450  0.0084  283 TRP A CD2   
2246 N NE1   . TRP A 283 ? 0.3210 0.2233 0.1597 0.0039  0.0415  0.0089  283 TRP A NE1   
2247 C CE2   . TRP A 283 ? 0.2939 0.2085 0.1468 0.0012  0.0406  0.0086  283 TRP A CE2   
2248 C CE3   . TRP A 283 ? 0.5543 0.4811 0.4263 -0.0029 0.0447  0.0080  283 TRP A CE3   
2249 C CZ2   . TRP A 283 ? 0.2210 0.1457 0.0825 0.0001  0.0364  0.0086  283 TRP A CZ2   
2250 C CZ3   . TRP A 283 ? 0.4511 0.3877 0.3312 -0.0038 0.0405  0.0080  283 TRP A CZ3   
2251 C CH2   . TRP A 283 ? 0.2182 0.1539 0.0932 -0.0024 0.0366  0.0084  283 TRP A CH2   
2252 N N     . LEU A 284 ? 0.3523 0.2695 0.2266 -0.0042 0.0561  0.0081  284 LEU A N     
2253 C CA    . LEU A 284 ? 0.2159 0.1442 0.1029 -0.0061 0.0540  0.0079  284 LEU A CA    
2254 C C     . LEU A 284 ? 0.3928 0.3193 0.2812 -0.0063 0.0561  0.0083  284 LEU A C     
2255 O O     . LEU A 284 ? 0.4389 0.3728 0.3348 -0.0071 0.0538  0.0085  284 LEU A O     
2256 C CB    . LEU A 284 ? 0.2595 0.1949 0.1561 -0.0080 0.0539  0.0068  284 LEU A CB    
2257 C CG    . LEU A 284 ? 0.2103 0.1572 0.1200 -0.0097 0.0513  0.0063  284 LEU A CG    
2258 C CD1   . LEU A 284 ? 0.1530 0.1064 0.0655 -0.0094 0.0469  0.0070  284 LEU A CD1   
2259 C CD2   . LEU A 284 ? 0.1532 0.1056 0.0703 -0.0109 0.0510  0.0052  284 LEU A CD2   
2260 N N     . ASN A 285 ? 0.5267 0.4436 0.4083 -0.0054 0.0607  0.0085  285 ASN A N     
2261 C CA    . ASN A 285 ? 0.5786 0.4924 0.4597 -0.0052 0.0628  0.0091  285 ASN A CA    
2262 C C     . ASN A 285 ? 0.5510 0.4622 0.4257 -0.0036 0.0607  0.0102  285 ASN A C     
2263 O O     . ASN A 285 ? 0.4588 0.3739 0.3379 -0.0040 0.0596  0.0106  285 ASN A O     
2264 C CB    . ASN A 285 ? 0.5396 0.4425 0.4135 -0.0042 0.0684  0.0092  285 ASN A CB    
2265 C CG    . ASN A 285 ? 0.5024 0.4076 0.3838 -0.0059 0.0711  0.0081  285 ASN A CG    
2266 O OD1   . ASN A 285 ? 0.6261 0.5406 0.5184 -0.0078 0.0691  0.0073  285 ASN A OD1   
2267 N ND2   . ASN A 285 ? 0.2543 0.1504 0.1294 -0.0052 0.0757  0.0081  285 ASN A ND2   
2268 N N     . LYS A 286 ? 0.5729 0.4775 0.4371 -0.0016 0.0598  0.0106  286 LYS A N     
2269 C CA    . LYS A 286 ? 0.5958 0.4972 0.4529 0.0001  0.0573  0.0116  286 LYS A CA    
2270 C C     . LYS A 286 ? 0.6741 0.5866 0.5405 -0.0012 0.0526  0.0116  286 LYS A C     
2271 O O     . LYS A 286 ? 0.6858 0.6002 0.5544 -0.0012 0.0519  0.0122  286 LYS A O     
2272 C CB    . LYS A 286 ? 0.5672 0.4611 0.4127 0.0024  0.0561  0.0117  286 LYS A CB    
2273 C CG    . LYS A 286 ? 0.5440 0.4239 0.3761 0.0049  0.0600  0.0122  286 LYS A CG    
2274 C CD    . LYS A 286 ? 0.5045 0.3767 0.3257 0.0077  0.0586  0.0131  286 LYS A CD    
2275 C CE    . LYS A 286 ? 0.4595 0.3178 0.2656 0.0109  0.0611  0.0135  286 LYS A CE    
2276 N NZ    . LYS A 286 ? 0.4444 0.2973 0.2497 0.0107  0.0670  0.0135  286 LYS A NZ    
2277 N N     . ILE A 287 ? 0.5465 0.4667 0.4187 -0.0022 0.0495  0.0110  287 ILE A N     
2278 C CA    . ILE A 287 ? 0.3798 0.3102 0.2601 -0.0032 0.0450  0.0111  287 ILE A CA    
2279 C C     . ILE A 287 ? 0.3591 0.2979 0.2509 -0.0049 0.0451  0.0111  287 ILE A C     
2280 O O     . ILE A 287 ? 0.4411 0.3866 0.3383 -0.0053 0.0419  0.0116  287 ILE A O     
2281 C CB    . ILE A 287 ? 0.4474 0.3834 0.3312 -0.0038 0.0423  0.0104  287 ILE A CB    
2282 C CG1   . ILE A 287 ? 0.4537 0.3983 0.3431 -0.0041 0.0374  0.0108  287 ILE A CG1   
2283 C CG2   . ILE A 287 ? 0.5933 0.5349 0.4861 -0.0056 0.0441  0.0095  287 ILE A CG2   
2284 C CD1   . ILE A 287 ? 0.3940 0.3444 0.2874 -0.0046 0.0349  0.0101  287 ILE A CD1   
2285 N N     . ARG A 288 ? 0.4340 0.3725 0.3299 -0.0060 0.0484  0.0105  288 ARG A N     
2286 C CA    . ARG A 288 ? 0.4498 0.3953 0.3556 -0.0073 0.0482  0.0103  288 ARG A CA    
2287 C C     . ARG A 288 ? 0.4013 0.3428 0.3034 -0.0065 0.0490  0.0113  288 ARG A C     
2288 O O     . ARG A 288 ? 0.3612 0.3095 0.2698 -0.0070 0.0466  0.0116  288 ARG A O     
2289 C CB    . ARG A 288 ? 0.4731 0.4180 0.3831 -0.0084 0.0515  0.0093  288 ARG A CB    
2290 C CG    . ARG A 288 ? 0.4305 0.3830 0.3488 -0.0097 0.0499  0.0083  288 ARG A CG    
2291 C CD    . ARG A 288 ? 0.5016 0.4525 0.4232 -0.0107 0.0532  0.0072  288 ARG A CD    
2292 N NE    . ARG A 288 ? 0.5582 0.5138 0.4853 -0.0116 0.0523  0.0062  288 ARG A NE    
2293 C CZ    . ARG A 288 ? 0.6366 0.5999 0.5734 -0.0127 0.0506  0.0054  288 ARG A CZ    
2294 N NH1   . ARG A 288 ? 0.5864 0.5533 0.5281 -0.0129 0.0496  0.0054  288 ARG A NH1   
2295 N NH2   . ARG A 288 ? 0.6685 0.6354 0.6095 -0.0134 0.0497  0.0045  288 ARG A NH2   
2296 N N     . LEU A 289 ? 0.3459 0.2765 0.2375 -0.0050 0.0522  0.0117  289 LEU A N     
2297 C CA    . LEU A 289 ? 0.4157 0.3419 0.3033 -0.0040 0.0533  0.0126  289 LEU A CA    
2298 C C     . LEU A 289 ? 0.3256 0.2518 0.2087 -0.0028 0.0497  0.0136  289 LEU A C     
2299 O O     . LEU A 289 ? 0.3763 0.3038 0.2606 -0.0026 0.0489  0.0143  289 LEU A O     
2300 C CB    . LEU A 289 ? 0.4669 0.3809 0.3448 -0.0026 0.0584  0.0128  289 LEU A CB    
2301 C CG    . LEU A 289 ? 0.4088 0.3225 0.2914 -0.0038 0.0621  0.0118  289 LEU A CG    
2302 C CD1   . LEU A 289 ? 0.4663 0.3675 0.3387 -0.0022 0.0673  0.0121  289 LEU A CD1   
2303 C CD2   . LEU A 289 ? 0.3392 0.2600 0.2323 -0.0054 0.0620  0.0114  289 LEU A CD2   
2304 N N     . TYR A 290 ? 0.3086 0.2337 0.1869 -0.0020 0.0473  0.0136  290 TYR A N     
2305 C CA    . TYR A 290 ? 0.1935 0.1191 0.0682 -0.0009 0.0433  0.0143  290 TYR A CA    
2306 C C     . TYR A 290 ? 0.2168 0.1548 0.1032 -0.0026 0.0394  0.0144  290 TYR A C     
2307 O O     . TYR A 290 ? 0.4319 0.3716 0.3186 -0.0022 0.0371  0.0153  290 TYR A O     
2308 C CB    . TYR A 290 ? 0.2021 0.1225 0.0680 0.0006  0.0416  0.0141  290 TYR A CB    
2309 C CG    . TYR A 290 ? 0.3320 0.2475 0.1893 0.0027  0.0383  0.0148  290 TYR A CG    
2310 C CD1   . TYR A 290 ? 0.4108 0.3341 0.2737 0.0021  0.0337  0.0152  290 TYR A CD1   
2311 C CD2   . TYR A 290 ? 0.3323 0.2353 0.1758 0.0054  0.0398  0.0152  290 TYR A CD2   
2312 C CE1   . TYR A 290 ? 0.3894 0.3080 0.2446 0.0040  0.0304  0.0158  290 TYR A CE1   
2313 C CE2   . TYR A 290 ? 0.3359 0.2342 0.1714 0.0075  0.0363  0.0158  290 TYR A CE2   
2314 C CZ    . TYR A 290 ? 0.3177 0.2240 0.1593 0.0067  0.0316  0.0160  290 TYR A CZ    
2315 O OH    . TYR A 290 ? 0.3530 0.2546 0.1870 0.0088  0.0278  0.0164  290 TYR A OH    
2316 N N     . ILE A 291 ? 0.2235 0.1701 0.1197 -0.0043 0.0387  0.0137  291 ILE A N     
2317 C CA    . ILE A 291 ? 0.1478 0.1060 0.0551 -0.0055 0.0351  0.0139  291 ILE A CA    
2318 C C     . ILE A 291 ? 0.4460 0.4078 0.3594 -0.0062 0.0357  0.0142  291 ILE A C     
2319 O O     . ILE A 291 ? 0.5738 0.5405 0.4906 -0.0062 0.0330  0.0151  291 ILE A O     
2320 C CB    . ILE A 291 ? 0.4350 0.4009 0.3508 -0.0068 0.0343  0.0130  291 ILE A CB    
2321 C CG1   . ILE A 291 ? 0.3806 0.3438 0.2909 -0.0061 0.0331  0.0126  291 ILE A CG1   
2322 C CG2   . ILE A 291 ? 0.4963 0.4738 0.4239 -0.0076 0.0311  0.0133  291 ILE A CG2   
2323 C CD1   . ILE A 291 ? 0.4020 0.3623 0.3054 -0.0047 0.0300  0.0133  291 ILE A CD1   
2324 N N     . GLU A 292 ? 0.4557 0.4148 0.3701 -0.0067 0.0394  0.0136  292 GLU A N     
2325 C CA    . GLU A 292 ? 0.2943 0.2571 0.2150 -0.0073 0.0398  0.0138  292 GLU A CA    
2326 C C     . GLU A 292 ? 0.2791 0.2378 0.1944 -0.0063 0.0396  0.0149  292 GLU A C     
2327 O O     . GLU A 292 ? 0.2767 0.2415 0.1977 -0.0067 0.0373  0.0155  292 GLU A O     
2328 C CB    . GLU A 292 ? 0.1897 0.1488 0.1112 -0.0078 0.0439  0.0128  292 GLU A CB    
2329 C CG    . GLU A 292 ? 0.1628 0.1266 0.0920 -0.0086 0.0440  0.0126  292 GLU A CG    
2330 C CD    . GLU A 292 ? 0.4955 0.4575 0.4275 -0.0094 0.0472  0.0114  292 GLU A CD    
2331 O OE1   . GLU A 292 ? 0.5589 0.5136 0.4851 -0.0092 0.0506  0.0109  292 GLU A OE1   
2332 O OE2   . GLU A 292 ? 0.4444 0.4121 0.3842 -0.0102 0.0463  0.0108  292 GLU A OE2   
2333 N N     . ASP A 293 ? 0.2131 0.1611 0.1167 -0.0047 0.0417  0.0153  293 ASP A N     
2334 C CA    . ASP A 293 ? 0.2188 0.1621 0.1164 -0.0035 0.0414  0.0164  293 ASP A CA    
2335 C C     . ASP A 293 ? 0.2347 0.1823 0.1326 -0.0031 0.0367  0.0172  293 ASP A C     
2336 O O     . ASP A 293 ? 0.3401 0.2887 0.2382 -0.0028 0.0352  0.0181  293 ASP A O     
2337 C CB    . ASP A 293 ? 0.4440 0.3741 0.3284 -0.0014 0.0448  0.0167  293 ASP A CB    
2338 C CG    . ASP A 293 ? 0.6757 0.6002 0.5548 -0.0002 0.0460  0.0177  293 ASP A CG    
2339 O OD1   . ASP A 293 ? 0.6908 0.6216 0.5770 -0.0011 0.0448  0.0181  293 ASP A OD1   
2340 O OD2   . ASP A 293 ? 0.6587 0.5722 0.5263 0.0019  0.0482  0.0182  293 ASP A OD2   
2341 N N     . ASN A 294 ? 0.1978 0.1482 0.0962 -0.0033 0.0343  0.0169  294 ASN A N     
2342 C CA    . ASN A 294 ? 0.3306 0.2865 0.2314 -0.0032 0.0296  0.0175  294 ASN A CA    
2343 C C     . ASN A 294 ? 0.3901 0.3580 0.3041 -0.0048 0.0277  0.0179  294 ASN A C     
2344 O O     . ASN A 294 ? 0.3143 0.2858 0.2304 -0.0047 0.0248  0.0189  294 ASN A O     
2345 C CB    . ASN A 294 ? 0.1722 0.1285 0.0710 -0.0029 0.0276  0.0170  294 ASN A CB    
2346 C CG    . ASN A 294 ? 0.1952 0.1405 0.0800 -0.0006 0.0266  0.0171  294 ASN A CG    
2347 O OD1   . ASN A 294 ? 0.2425 0.1784 0.1180 0.0009  0.0287  0.0175  294 ASN A OD1   
2348 N ND2   . ASN A 294 ? 0.2657 0.2122 0.1490 -0.0002 0.0232  0.0168  294 ASN A ND2   
2349 N N     . ALA A 295 ? 0.3552 0.3288 0.2776 -0.0061 0.0291  0.0170  295 ALA A N     
2350 C CA    . ALA A 295 ? 0.3083 0.2922 0.2424 -0.0071 0.0273  0.0173  295 ALA A CA    
2351 C C     . ALA A 295 ? 0.3122 0.2946 0.2463 -0.0071 0.0285  0.0178  295 ALA A C     
2352 O O     . ALA A 295 ? 0.5013 0.4907 0.4422 -0.0074 0.0262  0.0185  295 ALA A O     
2353 C CB    . ALA A 295 ? 0.3795 0.3683 0.3211 -0.0080 0.0283  0.0161  295 ALA A CB    
2354 N N     . LYS A 296 ? 0.2617 0.2350 0.1885 -0.0066 0.0322  0.0174  296 LYS A N     
2355 C CA    . LYS A 296 ? 0.1851 0.1561 0.1110 -0.0063 0.0335  0.0180  296 LYS A CA    
2356 C C     . LYS A 296 ? 0.3184 0.2872 0.2391 -0.0053 0.0313  0.0193  296 LYS A C     
2357 O O     . LYS A 296 ? 0.2079 0.1819 0.1337 -0.0057 0.0294  0.0201  296 LYS A O     
2358 C CB    . LYS A 296 ? 0.1406 0.1018 0.0596 -0.0057 0.0383  0.0174  296 LYS A CB    
2359 C CG    . LYS A 296 ? 0.4199 0.3771 0.3365 -0.0052 0.0402  0.0180  296 LYS A CG    
2360 C CD    . LYS A 296 ? 0.5015 0.4486 0.4112 -0.0044 0.0453  0.0176  296 LYS A CD    
2361 C CE    . LYS A 296 ? 0.4144 0.3575 0.3217 -0.0037 0.0473  0.0182  296 LYS A CE    
2362 N NZ    . LYS A 296 ? 0.2940 0.2298 0.1912 -0.0019 0.0470  0.0195  296 LYS A NZ    
2363 N N     . PHE A 297 ? 0.2707 0.2319 0.1813 -0.0040 0.0311  0.0196  297 PHE A N     
2364 C CA    . PHE A 297 ? 0.3163 0.2741 0.2207 -0.0027 0.0286  0.0208  297 PHE A CA    
2365 C C     . PHE A 297 ? 0.4017 0.3695 0.3146 -0.0036 0.0242  0.0215  297 PHE A C     
2366 O O     . PHE A 297 ? 0.4030 0.3716 0.3160 -0.0033 0.0225  0.0226  297 PHE A O     
2367 C CB    . PHE A 297 ? 0.4580 0.4066 0.3506 -0.0009 0.0282  0.0207  297 PHE A CB    
2368 C CG    . PHE A 297 ? 0.6233 0.5684 0.5093 0.0006  0.0245  0.0216  297 PHE A CG    
2369 C CD1   . PHE A 297 ? 0.4506 0.3872 0.3277 0.0024  0.0254  0.0223  297 PHE A CD1   
2370 C CD2   . PHE A 297 ? 0.6000 0.5499 0.4885 0.0005  0.0201  0.0218  297 PHE A CD2   
2371 C CE1   . PHE A 297 ? 0.2644 0.1975 0.1354 0.0040  0.0217  0.0231  297 PHE A CE1   
2372 C CE2   . PHE A 297 ? 0.2794 0.2255 0.1618 0.0020  0.0162  0.0225  297 PHE A CE2   
2373 C CZ    . PHE A 297 ? 0.2155 0.1533 0.0892 0.0038  0.0169  0.0231  297 PHE A CZ    
2374 N N     . ALA A 298 ? 0.2961 0.2715 0.2162 -0.0046 0.0224  0.0211  298 ALA A N     
2375 C CA    . ALA A 298 ? 0.1132 0.0979 0.0413 -0.0051 0.0184  0.0220  298 ALA A CA    
2376 C C     . ALA A 298 ? 0.1726 0.1656 0.1110 -0.0061 0.0182  0.0225  298 ALA A C     
2377 O O     . ALA A 298 ? 0.2620 0.2591 0.2045 -0.0060 0.0156  0.0235  298 ALA A O     
2378 C CB    . ALA A 298 ? 0.1521 0.1423 0.0852 -0.0053 0.0170  0.0215  298 ALA A CB    
2379 N N     . CYS A 299 ? 0.3025 0.2973 0.2453 -0.0069 0.0206  0.0215  299 CYS A N     
2380 C CA    . CYS A 299 ? 0.3094 0.3113 0.2621 -0.0077 0.0196  0.0212  299 CYS A CA    
2381 C C     . CYS A 299 ? 0.2930 0.2923 0.2427 -0.0079 0.0203  0.0222  299 CYS A C     
2382 O O     . CYS A 299 ? 0.1891 0.1935 0.1463 -0.0087 0.0179  0.0216  299 CYS A O     
2383 C CB    . CYS A 299 ? 0.2861 0.2892 0.2423 -0.0082 0.0219  0.0199  299 CYS A CB    
2384 S SG    . CYS A 299 ? 0.4942 0.5049 0.4611 -0.0070 0.0192  0.0188  299 CYS A SG    
2385 N N     . GLU A 300 ? 0.2813 0.2706 0.2208 -0.0068 0.0229  0.0223  300 GLU A N     
2386 C CA    . GLU A 300 ? 0.3174 0.3026 0.2533 -0.0063 0.0238  0.0231  300 GLU A CA    
2387 C C     . GLU A 300 ? 0.3787 0.3638 0.3117 -0.0057 0.0206  0.0246  300 GLU A C     
2388 O O     . GLU A 300 ? 0.4821 0.4696 0.4178 -0.0061 0.0196  0.0254  300 GLU A O     
2389 C CB    . GLU A 300 ? 0.2188 0.1928 0.1447 -0.0051 0.0280  0.0226  300 GLU A CB    
2390 C CG    . GLU A 300 ? 0.1296 0.1030 0.0584 -0.0057 0.0314  0.0213  300 GLU A CG    
2391 C CD    . GLU A 300 ? 0.2253 0.1877 0.1442 -0.0045 0.0354  0.0208  300 GLU A CD    
2392 O OE1   . GLU A 300 ? 0.2614 0.2173 0.1713 -0.0033 0.0351  0.0213  300 GLU A OE1   
2393 O OE2   . GLU A 300 ? 0.4142 0.3741 0.3340 -0.0048 0.0388  0.0199  300 GLU A OE2   
2394 N N     . TYR A 301 ? 0.3471 0.3287 0.2742 -0.0048 0.0190  0.0248  301 TYR A N     
2395 C CA    . TYR A 301 ? 0.3096 0.2905 0.2338 -0.0039 0.0155  0.0262  301 TYR A CA    
2396 C C     . TYR A 301 ? 0.4068 0.3989 0.3427 -0.0051 0.0123  0.0271  301 TYR A C     
2397 O O     . TYR A 301 ? 0.3263 0.3186 0.2624 -0.0046 0.0102  0.0281  301 TYR A O     
2398 C CB    . TYR A 301 ? 0.3534 0.3294 0.2705 -0.0027 0.0137  0.0259  301 TYR A CB    
2399 C CG    . TYR A 301 ? 0.2750 0.2491 0.1882 -0.0015 0.0095  0.0270  301 TYR A CG    
2400 C CD1   . TYR A 301 ? 0.2645 0.2476 0.1868 -0.0019 0.0061  0.0280  301 TYR A CD1   
2401 C CD2   . TYR A 301 ? 0.2566 0.2194 0.1570 0.0006  0.0089  0.0270  301 TYR A CD2   
2402 C CE1   . TYR A 301 ? 0.1828 0.1634 0.1016 -0.0005 0.0022  0.0288  301 TYR A CE1   
2403 C CE2   . TYR A 301 ? 0.3258 0.2862 0.2224 0.0020  0.0046  0.0277  301 TYR A CE2   
2404 C CZ    . TYR A 301 ? 0.3324 0.3016 0.2384 0.0012  0.0012  0.0285  301 TYR A CZ    
2405 O OH    . TYR A 301 ? 0.6736 0.6398 0.5761 0.0027  -0.0033 0.0290  301 TYR A OH    
2406 N N     . MET A 302 ? 0.3850 0.3847 0.3318 -0.0059 0.0117  0.0255  302 MET A N     
2407 C CA    . MET A 302 ? 0.2364 0.2176 0.1804 -0.0026 0.0136  0.0202  302 MET A CA    
2408 C C     . MET A 302 ? 0.2296 0.2147 0.1786 -0.0063 0.0139  0.0196  302 MET A C     
2409 O O     . MET A 302 ? 0.1290 0.1231 0.0871 -0.0056 0.0122  0.0208  302 MET A O     
2410 C CB    . MET A 302 ? 0.1256 0.1150 0.0774 -0.0041 0.0122  0.0199  302 MET A CB    
2411 C CG    . MET A 302 ? 0.3887 0.3755 0.3358 -0.0010 0.0121  0.0205  302 MET A CG    
2412 S SD    . MET A 302 ? 0.6907 0.6853 0.6457 -0.0042 0.0095  0.0196  302 MET A SD    
2413 C CE    . MET A 302 ? 0.5445 0.5434 0.5032 -0.0043 0.0044  0.0205  302 MET A CE    
2414 N N     . LYS A 303 ? 0.3365 0.3358 0.2909 -0.0118 0.0126  0.0213  303 LYS A N     
2415 C CA    . LYS A 303 ? 0.2773 0.2754 0.2326 -0.0119 0.0144  0.0209  303 LYS A CA    
2416 C C     . LYS A 303 ? 0.0862 0.0848 0.0390 -0.0105 0.0137  0.0238  303 LYS A C     
2417 O O     . LYS A 303 ? 0.1217 0.1131 0.0732 -0.0111 0.0136  0.0215  303 LYS A O     
2418 C CB    . LYS A 303 ? 0.2750 0.2761 0.2306 -0.0096 0.0183  0.0228  303 LYS A CB    
2419 C CG    . LYS A 303 ? 0.1940 0.1948 0.1514 -0.0099 0.0202  0.0225  303 LYS A CG    
2420 C CD    . LYS A 303 ? 0.2902 0.2915 0.2538 -0.0119 0.0187  0.0187  303 LYS A CD    
2421 C CE    . LYS A 303 ? 0.4433 0.4478 0.4102 -0.0113 0.0210  0.0192  303 LYS A CE    
2422 N NZ    . LYS A 303 ? 0.4353 0.4349 0.3959 -0.0094 0.0253  0.0213  303 LYS A NZ    
2423 N N     . ASP A 304 ? 0.0974 0.0922 0.0417 -0.0076 0.0157  0.0267  304 ASP A N     
2424 C CA    . ASP A 304 ? 0.3788 0.3680 0.3161 -0.0063 0.0161  0.0283  304 ASP A CA    
2425 C C     . ASP A 304 ? 0.3298 0.3209 0.2678 -0.0060 0.0120  0.0296  304 ASP A C     
2426 O O     . ASP A 304 ? 0.5196 0.5119 0.4602 -0.0065 0.0105  0.0300  304 ASP A O     
2427 C CB    . ASP A 304 ? 0.4518 0.4296 0.3772 -0.0041 0.0193  0.0280  304 ASP A CB    
2428 C CG    . ASP A 304 ? 0.5684 0.5411 0.4911 -0.0036 0.0232  0.0277  304 ASP A CG    
2429 O OD1   . ASP A 304 ? 0.5356 0.5140 0.4658 -0.0048 0.0231  0.0276  304 ASP A OD1   
2430 O OD2   . ASP A 304 ? 0.5220 0.4847 0.4348 -0.0020 0.0262  0.0275  304 ASP A OD2   
2431 N N     . HIS A 305 ? 0.3466 0.3376 0.2828 -0.0050 0.0100  0.0298  305 HIS A N     
2432 C CA    . HIS A 305 ? 0.3889 0.3792 0.3232 -0.0035 0.0065  0.0311  305 HIS A CA    
2433 C C     . HIS A 305 ? 0.3369 0.3358 0.2833 -0.0015 0.0045  0.0304  305 HIS A C     
2434 O O     . HIS A 305 ? 0.4695 0.4660 0.4138 0.0018  0.0026  0.0309  305 HIS A O     
2435 C CB    . HIS A 305 ? 0.5152 0.4953 0.4362 -0.0016 0.0061  0.0311  305 HIS A CB    
2436 C CG    . HIS A 305 ? 0.6463 0.6165 0.5573 -0.0007 0.0099  0.0302  305 HIS A CG    
2437 N ND1   . HIS A 305 ? 0.5498 0.5133 0.4542 0.0004  0.0110  0.0308  305 HIS A ND1   
2438 C CD2   . HIS A 305 ? 0.6835 0.6492 0.5903 -0.0005 0.0131  0.0289  305 HIS A CD2   
2439 C CE1   . HIS A 305 ? 0.5361 0.4915 0.4327 0.0014  0.0149  0.0299  305 HIS A CE1   
2440 N NE2   . HIS A 305 ? 0.6446 0.6011 0.5426 0.0008  0.0162  0.0287  305 HIS A NE2   
2441 N N     . ILE A 306 ? 0.3797 0.3599 0.3199 0.0017  0.0086  0.0241  306 ILE A N     
2442 C CA    . ILE A 306 ? 0.1988 0.1868 0.1474 -0.0020 0.0047  0.0241  306 ILE A CA    
2443 C C     . ILE A 306 ? 0.2329 0.2330 0.1961 -0.0044 0.0052  0.0232  306 ILE A C     
2444 O O     . ILE A 306 ? 0.4908 0.5004 0.4646 -0.0053 0.0043  0.0223  306 ILE A O     
2445 C CB    . ILE A 306 ? 0.1508 0.1403 0.0999 -0.0017 0.0036  0.0237  306 ILE A CB    
2446 C CG1   . ILE A 306 ? 0.3243 0.3117 0.2663 0.0037  0.0041  0.0253  306 ILE A CG1   
2447 C CG2   . ILE A 306 ? 0.0948 0.0955 0.0571 -0.0039 -0.0006 0.0236  306 ILE A CG2   
2448 C CD1   . ILE A 306 ? 0.4349 0.4239 0.3768 0.0036  0.0026  0.0249  306 ILE A CD1   
2449 N N     . PRO A 307 ? 0.1774 0.1784 0.1423 -0.0045 0.0059  0.0236  307 PRO A N     
2450 C CA    . PRO A 307 ? 0.1114 0.1224 0.0882 -0.0050 0.0061  0.0227  307 PRO A CA    
2451 C C     . PRO A 307 ? 0.1343 0.1612 0.1282 -0.0052 0.0019  0.0225  307 PRO A C     
2452 O O     . PRO A 307 ? 0.1837 0.2178 0.1859 -0.0044 0.0008  0.0219  307 PRO A O     
2453 C CB    . PRO A 307 ? 0.3368 0.3442 0.3103 -0.0048 0.0073  0.0234  307 PRO A CB    
2454 C CG    . PRO A 307 ? 0.3350 0.3378 0.3027 -0.0043 0.0055  0.0247  307 PRO A CG    
2455 C CD    . PRO A 307 ? 0.3899 0.3837 0.3468 -0.0036 0.0056  0.0248  307 PRO A CD    
2456 N N     . THR A 308 ? 0.1810 0.2124 0.1795 -0.0060 -0.0006 0.0230  308 THR A N     
2457 C CA    . THR A 308 ? 0.3101 0.3507 0.3213 -0.0060 -0.0033 0.0214  308 THR A CA    
2458 C C     . THR A 308 ? 0.4216 0.4589 0.4323 -0.0053 -0.0032 0.0187  308 THR A C     
2459 O O     . THR A 308 ? 0.4701 0.4988 0.4752 -0.0044 -0.0023 0.0176  308 THR A O     
2460 C CB    . THR A 308 ? 0.1383 0.1777 0.1504 -0.0071 -0.0040 0.0217  308 THR A CB    
2461 O OG1   . THR A 308 ? 0.0945 0.1233 0.1009 -0.0053 -0.0031 0.0194  308 THR A OG1   
2462 C CG2   . THR A 308 ? 0.0556 0.0945 0.0637 -0.0092 -0.0050 0.0244  308 THR A CG2   
2463 N N     . LEU A 309 ? 0.2931 0.3349 0.3021 -0.0062 -0.0029 0.0213  309 LEU A N     
2464 C CA    . LEU A 309 ? 0.2192 0.2596 0.2282 -0.0057 -0.0029 0.0194  309 LEU A CA    
2465 C C     . LEU A 309 ? 0.2987 0.3390 0.3058 -0.0050 -0.0017 0.0196  309 LEU A C     
2466 O O     . LEU A 309 ? 0.0948 0.1251 0.0920 -0.0052 0.0024  0.0195  309 LEU A O     
2467 C CB    . LEU A 309 ? 0.1037 0.1401 0.1061 -0.0070 -0.0018 0.0203  309 LEU A CB    
2468 C CG    . LEU A 309 ? 0.0233 0.0622 0.0288 -0.0084 -0.0037 0.0211  309 LEU A CG    
2469 C CD1   . LEU A 309 ? 0.0371 0.0641 0.0291 -0.0081 -0.0026 0.0213  309 LEU A CD1   
2470 C CD2   . LEU A 309 ? 0.0164 0.0511 0.0262 -0.0065 -0.0036 0.0165  309 LEU A CD2   
2471 N N     . SER A 310 ? 0.4257 0.4629 0.4339 -0.0038 -0.0023 0.0168  310 SER A N     
2472 C CA    . SER A 310 ? 0.4418 0.4813 0.4496 -0.0036 -0.0017 0.0177  310 SER A CA    
2473 C C     . SER A 310 ? 0.5375 0.5778 0.5445 -0.0041 -0.0017 0.0173  310 SER A C     
2474 O O     . SER A 310 ? 0.5430 0.5766 0.5499 -0.0031 -0.0023 0.0141  310 SER A O     
2475 C CB    . SER A 310 ? 0.2357 0.2688 0.2435 -0.0021 -0.0020 0.0148  310 SER A CB    
2476 O OG    . SER A 310 ? 0.1622 0.1891 0.1657 -0.0021 -0.0010 0.0143  310 SER A OG    
2477 N N     . VAL A 311 ? 0.4701 0.5007 0.4681 -0.0054 0.0035  0.0165  311 VAL A N     
2478 C CA    . VAL A 311 ? 0.0308 0.0587 0.0259 -0.0060 0.0050  0.0157  311 VAL A CA    
2479 C C     . VAL A 311 ? 0.2062 0.2308 0.1996 -0.0061 0.0076  0.0146  311 VAL A C     
2480 O O     . VAL A 311 ? 0.4230 0.4412 0.4115 -0.0066 0.0115  0.0144  311 VAL A O     
2481 C CB    . VAL A 311 ? 0.1510 0.1686 0.1351 -0.0068 0.0091  0.0159  311 VAL A CB    
2482 C CG1   . VAL A 311 ? 0.3441 0.3512 0.3180 -0.0068 0.0137  0.0163  311 VAL A CG1   
2483 C CG2   . VAL A 311 ? 0.3889 0.4025 0.3691 -0.0071 0.0115  0.0150  311 VAL A CG2   
2484 N N     . THR A 312 ? 0.4151 0.4435 0.4122 -0.0059 0.0056  0.0140  312 THR A N     
2485 C CA    . THR A 312 ? 0.2529 0.2778 0.2483 -0.0062 0.0083  0.0129  312 THR A CA    
2486 C C     . THR A 312 ? 0.3883 0.4045 0.3763 -0.0074 0.0141  0.0121  312 THR A C     
2487 O O     . THR A 312 ? 0.5153 0.5302 0.5008 -0.0076 0.0143  0.0123  312 THR A O     
2488 C CB    . THR A 312 ? 0.1744 0.2053 0.1749 -0.0052 0.0040  0.0127  312 THR A CB    
2489 O OG1   . THR A 312 ? 0.3246 0.3512 0.3230 -0.0060 0.0075  0.0115  312 THR A OG1   
2490 C CG2   . THR A 312 ? 0.0195 0.0535 0.0214 -0.0051 0.0016  0.0128  312 THR A CG2   
2491 N N     . LYS A 313 ? 0.4598 0.4693 0.4437 -0.0077 0.0191  0.0117  313 LYS A N     
2492 C CA    . LYS A 313 ? 0.3236 0.3274 0.3032 -0.0054 0.0230  0.0129  313 LYS A CA    
2493 C C     . LYS A 313 ? 0.4009 0.4073 0.3826 -0.0055 0.0227  0.0126  313 LYS A C     
2494 O O     . LYS A 313 ? 0.0513 0.0595 0.0366 -0.0066 0.0220  0.0111  313 LYS A O     
2495 C CB    . LYS A 313 ? 0.2348 0.2505 0.2165 -0.0071 0.0217  0.0154  313 LYS A CB    
2496 C CG    . LYS A 313 ? 0.3212 0.3312 0.2936 -0.0092 0.0258  0.0154  313 LYS A CG    
2497 C CD    . LYS A 313 ? 0.2741 0.2813 0.2412 -0.0092 0.0257  0.0165  313 LYS A CD    
2498 C CE    . LYS A 313 ? 0.2005 0.1975 0.1586 -0.0092 0.0297  0.0162  313 LYS A CE    
2499 N NZ    . LYS A 313 ? 0.1908 0.1831 0.1425 -0.0089 0.0306  0.0161  313 LYS A NZ    
2500 N N     . PRO A 314 ? 0.3562 0.3646 0.3356 -0.0047 0.0226  0.0142  314 PRO A N     
2501 C CA    . PRO A 314 ? 0.4188 0.4293 0.3991 -0.0053 0.0227  0.0136  314 PRO A CA    
2502 C C     . PRO A 314 ? 0.3096 0.3221 0.2868 -0.0080 0.0248  0.0135  314 PRO A C     
2503 O O     . PRO A 314 ? 0.2938 0.3021 0.2654 -0.0093 0.0272  0.0133  314 PRO A O     
2504 C CB    . PRO A 314 ? 0.5142 0.5233 0.4905 -0.0051 0.0224  0.0141  314 PRO A CB    
2505 C CG    . PRO A 314 ? 0.5169 0.5271 0.4888 -0.0054 0.0219  0.0157  314 PRO A CG    
2506 C CD    . PRO A 314 ? 0.2949 0.3033 0.2699 -0.0041 0.0220  0.0156  314 PRO A CD    
2507 N N     . GLU A 315 ? 0.4144 0.4275 0.3937 -0.0083 0.0254  0.0125  315 GLU A N     
2508 C CA    . GLU A 315 ? 0.2694 0.2779 0.2453 -0.0101 0.0285  0.0108  315 GLU A CA    
2509 C C     . GLU A 315 ? 0.2324 0.2381 0.2049 -0.0105 0.0298  0.0102  315 GLU A C     
2510 O O     . GLU A 315 ? 0.2847 0.2856 0.2545 -0.0114 0.0327  0.0089  315 GLU A O     
2511 C CB    . GLU A 315 ? 0.0642 0.0749 0.0453 -0.0102 0.0282  0.0099  315 GLU A CB    
2512 C CG    . GLU A 315 ? 0.0569 0.0717 0.0427 -0.0090 0.0258  0.0109  315 GLU A CG    
2513 C CD    . GLU A 315 ? 0.1084 0.1253 0.0993 -0.0083 0.0243  0.0103  315 GLU A CD    
2514 O OE1   . GLU A 315 ? 0.1738 0.1910 0.1676 -0.0073 0.0229  0.0103  315 GLU A OE1   
2515 O OE2   . GLU A 315 ? 0.0503 0.0671 0.0418 -0.0087 0.0246  0.0093  315 GLU A OE2   
2516 N N     . GLY A 316 ? 0.2709 0.2791 0.2438 -0.0096 0.0277  0.0110  316 GLY A N     
2517 C CA    . GLY A 316 ? 0.2394 0.2446 0.2082 -0.0100 0.0288  0.0104  316 GLY A CA    
2518 C C     . GLY A 316 ? 0.2810 0.2883 0.2492 -0.0089 0.0266  0.0115  316 GLY A C     
2519 O O     . GLY A 316 ? 0.1407 0.1506 0.1117 -0.0075 0.0245  0.0127  316 GLY A O     
2520 N N     . SER A 317 ? 0.3747 0.3794 0.3388 -0.0093 0.0274  0.0110  317 SER A N     
2521 C CA    . SER A 317 ? 0.2553 0.2606 0.2174 -0.0084 0.0256  0.0117  317 SER A CA    
2522 C C     . SER A 317 ? 0.3570 0.3600 0.3136 -0.0079 0.0250  0.0128  317 SER A C     
2523 O O     . SER A 317 ? 0.3504 0.3491 0.3026 -0.0085 0.0268  0.0128  317 SER A O     
2524 C CB    . SER A 317 ? 0.0894 0.0984 0.0593 -0.0070 0.0232  0.0116  317 SER A CB    
2525 O OG    . SER A 317 ? 0.2516 0.2593 0.2190 -0.0064 0.0219  0.0117  317 SER A OG    
2526 N N     . PHE A 318 ? 0.3809 0.3854 0.3373 -0.0066 0.0227  0.0137  318 PHE A N     
2527 C CA    . PHE A 318 ? 0.0858 0.0874 0.0355 -0.0064 0.0216  0.0146  318 PHE A CA    
2528 C C     . PHE A 318 ? 0.0778 0.0817 0.0326 -0.0042 0.0188  0.0153  318 PHE A C     
2529 O O     . PHE A 318 ? 0.0845 0.0869 0.0343 -0.0037 0.0168  0.0160  318 PHE A O     
2530 C CB    . PHE A 318 ? 0.3745 0.3693 0.3138 -0.0065 0.0217  0.0141  318 PHE A CB    
2531 C CG    . PHE A 318 ? 0.3983 0.3958 0.3399 -0.0061 0.0205  0.0135  318 PHE A CG    
2532 C CD1   . PHE A 318 ? 0.3462 0.3435 0.2894 -0.0069 0.0225  0.0124  318 PHE A CD1   
2533 C CD2   . PHE A 318 ? 0.3928 0.3922 0.3345 -0.0048 0.0174  0.0141  318 PHE A CD2   
2534 C CE1   . PHE A 318 ? 0.3902 0.3896 0.3354 -0.0064 0.0215  0.0119  318 PHE A CE1   
2535 C CE2   . PHE A 318 ? 0.2829 0.2835 0.2263 -0.0041 0.0166  0.0134  318 PHE A CE2   
2536 C CZ    . PHE A 318 ? 0.1741 0.1750 0.1194 -0.0051 0.0187  0.0123  318 PHE A CZ    
2537 N N     . LEU A 319 ? 0.1216 0.1246 0.0835 -0.0044 0.0188  0.0140  319 LEU A N     
2538 C CA    . LEU A 319 ? 0.0619 0.0667 0.0280 -0.0065 0.0153  0.0129  319 LEU A CA    
2539 C C     . LEU A 319 ? 0.4441 0.4507 0.4139 -0.0070 0.0151  0.0129  319 LEU A C     
2540 O O     . LEU A 319 ? 0.4341 0.4400 0.4050 -0.0068 0.0174  0.0127  319 LEU A O     
2541 C CB    . LEU A 319 ? 0.2664 0.2808 0.2435 -0.0086 0.0113  0.0114  319 LEU A CB    
2542 C CG    . LEU A 319 ? 0.4108 0.4249 0.3868 -0.0087 0.0114  0.0108  319 LEU A CG    
2543 C CD1   . LEU A 319 ? 0.2739 0.2976 0.2605 -0.0096 0.0076  0.0096  319 LEU A CD1   
2544 C CD2   . LEU A 319 ? 0.5328 0.5445 0.5039 -0.0083 0.0100  0.0116  319 LEU A CD2   
2545 N N     . LEU A 320 ? 0.4436 0.4526 0.4151 -0.0074 0.0122  0.0134  320 LEU A N     
2546 C CA    . LEU A 320 ? 0.2379 0.2489 0.2125 -0.0076 0.0116  0.0137  320 LEU A CA    
2547 C C     . LEU A 320 ? 0.2100 0.2337 0.1973 -0.0081 0.0058  0.0136  320 LEU A C     
2548 O O     . LEU A 320 ? 0.2535 0.2812 0.2440 -0.0084 0.0030  0.0142  320 LEU A O     
2549 C CB    . LEU A 320 ? 0.3454 0.3472 0.3092 -0.0060 0.0139  0.0152  320 LEU A CB    
2550 C CG    . LEU A 320 ? 0.3551 0.3543 0.3175 -0.0055 0.0158  0.0157  320 LEU A CG    
2551 C CD1   . LEU A 320 ? 0.2832 0.2840 0.2451 -0.0022 0.0190  0.0175  320 LEU A CD1   
2552 C CD2   . LEU A 320 ? 0.0727 0.0685 0.0300 -0.0043 0.0145  0.0169  320 LEU A CD2   
2553 N N     . TRP A 321 ? 0.1322 0.1613 0.1259 -0.0077 0.0039  0.0134  321 TRP A N     
2554 C CA    . TRP A 321 ? 0.0412 0.0811 0.0449 -0.0065 -0.0021 0.0139  321 TRP A CA    
2555 C C     . TRP A 321 ? 0.2132 0.2521 0.2178 -0.0058 -0.0023 0.0143  321 TRP A C     
2556 O O     . TRP A 321 ? 0.1953 0.2330 0.1982 -0.0058 -0.0007 0.0146  321 TRP A O     
2557 C CB    . TRP A 321 ? 0.0152 0.0519 0.0189 -0.0053 -0.0021 0.0124  321 TRP A CB    
2558 C CG    . TRP A 321 ? 0.0149 0.0419 0.0156 -0.0035 -0.0013 0.0110  321 TRP A CG    
2559 C CD1   . TRP A 321 ? 0.1093 0.1355 0.1103 -0.0029 -0.0011 0.0111  321 TRP A CD1   
2560 C CD2   . TRP A 321 ? 0.1406 0.1701 0.1470 -0.0036 -0.0014 0.0103  321 TRP A CD2   
2561 N NE1   . TRP A 321 ? 0.2274 0.2557 0.2341 -0.0028 -0.0011 0.0104  321 TRP A NE1   
2562 C CE2   . TRP A 321 ? 0.1462 0.1746 0.1530 -0.0030 -0.0012 0.0105  321 TRP A CE2   
2563 C CE3   . TRP A 321 ? 0.0150 0.0417 0.0160 -0.0037 -0.0014 0.0114  321 TRP A CE3   
2564 C CZ2   . TRP A 321 ? 0.1727 0.2003 0.1799 -0.0028 -0.0012 0.0109  321 TRP A CZ2   
2565 C CZ3   . TRP A 321 ? 0.0148 0.0406 0.0163 -0.0034 -0.0014 0.0118  321 TRP A CZ3   
2566 C CH2   . TRP A 321 ? 0.1782 0.2061 0.1854 -0.0031 -0.0014 0.0110  321 TRP A CH2   
2567 N N     . ILE A 322 ? 0.3486 0.3837 0.3540 -0.0051 -0.0027 0.0133  322 ILE A N     
2568 C CA    . ILE A 322 ? 0.3485 0.3840 0.3546 -0.0051 -0.0028 0.0140  322 ILE A CA    
2569 C C     . ILE A 322 ? 0.2792 0.3070 0.2815 -0.0040 -0.0017 0.0137  322 ILE A C     
2570 O O     . ILE A 322 ? 0.2377 0.2651 0.2403 -0.0041 -0.0019 0.0140  322 ILE A O     
2571 C CB    . ILE A 322 ? 0.2342 0.2746 0.2389 -0.0074 -0.0027 0.0170  322 ILE A CB    
2572 C CG1   . ILE A 322 ? 0.2160 0.2436 0.2071 -0.0077 0.0021  0.0165  322 ILE A CG1   
2573 C CG2   . ILE A 322 ? 0.3556 0.3937 0.3584 -0.0073 -0.0019 0.0178  322 ILE A CG2   
2574 C CD1   . ILE A 322 ? 0.2742 0.2927 0.2546 -0.0075 0.0030  0.0174  322 ILE A CD1   
2575 N N     . ASP A 323 ? 0.0130 0.0441 0.0214 -0.0038 -0.0017 0.0127  323 ASP A N     
2576 C CA    . ASP A 323 ? 0.1369 0.1634 0.1403 -0.0032 -0.0015 0.0144  323 ASP A CA    
2577 C C     . ASP A 323 ? 0.2013 0.2319 0.2109 -0.0040 -0.0020 0.0139  323 ASP A C     
2578 O O     . ASP A 323 ? 0.4315 0.4630 0.4412 -0.0042 -0.0021 0.0141  323 ASP A O     
2579 C CB    . ASP A 323 ? 0.0969 0.1227 0.1005 -0.0026 -0.0013 0.0142  323 ASP A CB    
2580 C CG    . ASP A 323 ? 0.3104 0.3388 0.3200 -0.0026 -0.0013 0.0133  323 ASP A CG    
2581 O OD1   . ASP A 323 ? 0.2137 0.2422 0.2239 -0.0029 -0.0016 0.0138  323 ASP A OD1   
2582 O OD2   . ASP A 323 ? 0.3744 0.4022 0.3841 -0.0022 -0.0011 0.0132  323 ASP A OD2   
2583 N N     . CYS A 324 ? 0.2309 0.2611 0.2412 -0.0042 -0.0022 0.0145  324 CYS A N     
2584 C CA    . CYS A 324 ? 0.2263 0.2566 0.2373 -0.0048 -0.0027 0.0153  324 CYS A CA    
2585 C C     . CYS A 324 ? 0.3161 0.3416 0.3223 -0.0041 -0.0024 0.0173  324 CYS A C     
2586 O O     . CYS A 324 ? 0.3374 0.3627 0.3445 -0.0046 -0.0028 0.0182  324 CYS A O     
2587 C CB    . CYS A 324 ? 0.0388 0.0650 0.0440 -0.0053 -0.0030 0.0173  324 CYS A CB    
2588 S SG    . CYS A 324 ? 0.1634 0.2015 0.1727 -0.0084 -0.0044 0.0210  324 CYS A SG    
2589 N N     . SER A 325 ? 0.0286 0.0536 0.0347 -0.0034 -0.0020 0.0168  325 SER A N     
2590 C CA    . SER A 325 ? 0.0166 0.0409 0.0236 -0.0031 -0.0019 0.0172  325 SER A CA    
2591 C C     . SER A 325 ? 0.3461 0.3706 0.3536 -0.0032 -0.0020 0.0178  325 SER A C     
2592 O O     . SER A 325 ? 0.2002 0.2244 0.2087 -0.0033 -0.0022 0.0185  325 SER A O     
2593 C CB    . SER A 325 ? 0.2182 0.2418 0.2249 -0.0024 -0.0015 0.0165  325 SER A CB    
2594 O OG    . SER A 325 ? 0.4834 0.5111 0.4948 -0.0024 -0.0014 0.0146  325 SER A OG    
2595 N N     . ALA A 326 ? 0.3708 0.3960 0.3777 -0.0032 -0.0020 0.0176  326 ALA A N     
2596 C CA    . ALA A 326 ? 0.2417 0.2716 0.2551 -0.0036 -0.0023 0.0167  326 ALA A CA    
2597 C C     . ALA A 326 ? 0.2001 0.2258 0.2084 -0.0041 -0.0027 0.0193  326 ALA A C     
2598 O O     . ALA A 326 ? 0.2227 0.2483 0.2318 -0.0043 -0.0029 0.0200  326 ALA A O     
2599 C CB    . ALA A 326 ? 0.1108 0.1371 0.1177 -0.0032 -0.0019 0.0179  326 ALA A CB    
2600 N N     . LEU A 327 ? 0.1344 0.1600 0.1426 -0.0047 -0.0030 0.0195  327 LEU A N     
2601 C CA    . LEU A 327 ? 0.1277 0.1530 0.1368 -0.0057 -0.0038 0.0206  327 LEU A CA    
2602 C C     . LEU A 327 ? 0.2733 0.2976 0.2837 -0.0056 -0.0040 0.0213  327 LEU A C     
2603 O O     . LEU A 327 ? 0.4048 0.4286 0.4164 -0.0063 -0.0048 0.0224  327 LEU A O     
2604 C CB    . LEU A 327 ? 0.0503 0.0805 0.0651 -0.0071 -0.0048 0.0188  327 LEU A CB    
2605 C CG    . LEU A 327 ? 0.1428 0.1739 0.1564 -0.0073 -0.0046 0.0182  327 LEU A CG    
2606 C CD1   . LEU A 327 ? 0.0548 0.0808 0.0615 -0.0082 -0.0052 0.0204  327 LEU A CD1   
2607 C CD2   . LEU A 327 ? 0.3679 0.3950 0.3750 -0.0066 -0.0041 0.0201  327 LEU A CD2   
2608 N N     . ASN A 328 ? 0.2918 0.3207 0.3082 -0.0052 -0.0038 0.0189  328 ASN A N     
2609 C CA    . ASN A 328 ? 0.1918 0.2149 0.2035 -0.0046 -0.0035 0.0213  328 ASN A CA    
2610 C C     . ASN A 328 ? 0.2477 0.2702 0.2606 -0.0055 -0.0044 0.0223  328 ASN A C     
2611 O O     . ASN A 328 ? 0.3865 0.4085 0.4010 -0.0060 -0.0052 0.0235  328 ASN A O     
2612 C CB    . ASN A 328 ? 0.2328 0.2663 0.2531 -0.0060 -0.0047 0.0272  328 ASN A CB    
2613 C CG    . ASN A 328 ? 0.3480 0.3705 0.3617 -0.0040 -0.0033 0.0221  328 ASN A CG    
2614 O OD1   . ASN A 328 ? 0.5994 0.6213 0.6145 -0.0044 -0.0038 0.0230  328 ASN A OD1   
2615 N ND2   . ASN A 328 ? 0.4019 0.4244 0.4149 -0.0033 -0.0026 0.0213  328 ASN A ND2   
2616 N N     . LEU A 329 ? 0.3249 0.3473 0.3372 -0.0057 -0.0045 0.0219  329 LEU A N     
2617 C CA    . LEU A 329 ? 0.2796 0.3111 0.3011 -0.0088 -0.0074 0.0284  329 LEU A CA    
2618 C C     . LEU A 329 ? 0.3594 0.3904 0.3808 -0.0081 -0.0068 0.0278  329 LEU A C     
2619 O O     . LEU A 329 ? 0.0915 0.1182 0.1092 -0.0057 -0.0045 0.0193  329 LEU A O     
2620 C CB    . LEU A 329 ? 0.2788 0.3002 0.2914 -0.0075 -0.0062 0.0229  329 LEU A CB    
2621 C CG    . LEU A 329 ? 0.3044 0.3366 0.3237 -0.0109 -0.0087 0.0284  329 LEU A CG    
2622 C CD1   . LEU A 329 ? 0.2934 0.3257 0.3109 -0.0122 -0.0094 0.0280  329 LEU A CD1   
2623 C CD2   . LEU A 329 ? 0.3586 0.3795 0.3718 -0.0089 -0.0076 0.0242  329 LEU A CD2   
2624 N N     . SER A 330 ? 0.2951 0.3150 0.3105 -0.0063 -0.0057 0.0233  330 SER A N     
2625 C CA    . SER A 330 ? 0.2635 0.2830 0.2792 -0.0060 -0.0055 0.0231  330 SER A CA    
2626 C C     . SER A 330 ? 0.1522 0.1811 0.1751 -0.0089 -0.0080 0.0283  330 SER A C     
2627 O O     . SER A 330 ? 0.1473 0.1666 0.1614 -0.0074 -0.0067 0.0230  330 SER A O     
2628 C CB    . SER A 330 ? 0.4897 0.5172 0.5178 -0.0086 -0.0087 0.0303  330 SER A CB    
2629 O OG    . SER A 330 ? 0.3504 0.3670 0.3709 -0.0074 -0.0080 0.0255  330 SER A OG    
2630 N N     . GLN A 331 ? 0.0209 0.0403 0.0351 -0.0061 -0.0055 0.0221  331 GLN A N     
2631 C CA    . GLN A 331 ? 0.0174 0.0420 0.0362 -0.0072 -0.0062 0.0198  331 GLN A CA    
2632 C C     . GLN A 331 ? 0.2647 0.2822 0.2791 -0.0080 -0.0075 0.0229  331 GLN A C     
2633 O O     . GLN A 331 ? 0.0202 0.0430 0.0392 -0.0097 -0.0088 0.0205  331 GLN A O     
2634 C CB    . GLN A 331 ? 0.1335 0.1579 0.1521 -0.0065 -0.0056 0.0193  331 GLN A CB    
2635 C CG    . GLN A 331 ? 0.2087 0.2280 0.2205 -0.0065 -0.0054 0.0208  331 GLN A CG    
2636 C CD    . GLN A 331 ? 0.0932 0.1173 0.1106 -0.0064 -0.0054 0.0185  331 GLN A CD    
2637 O OE1   . GLN A 331 ? 0.0155 0.0393 0.0337 -0.0057 -0.0049 0.0186  331 GLN A OE1   
2638 N NE2   . GLN A 331 ? 0.1273 0.1466 0.1382 -0.0062 -0.0051 0.0200  331 GLN A NE2   
2639 N N     . ASP A 332 ? 0.3622 0.3777 0.3795 -0.0083 -0.0086 0.0240  332 ASP A N     
2640 C CA    . ASP A 332 ? 0.1209 0.1346 0.1427 -0.0114 -0.0106 0.0249  332 ASP A CA    
2641 C C     . ASP A 332 ? 0.1818 0.1961 0.2052 -0.0129 -0.0129 0.0265  332 ASP A C     
2642 O O     . ASP A 332 ? 0.3111 0.3249 0.3373 -0.0155 -0.0180 0.0294  332 ASP A O     
2643 C CB    . ASP A 332 ? 0.2073 0.2189 0.2332 -0.0114 -0.0122 0.0260  332 ASP A CB    
2644 C CG    . ASP A 332 ? 0.4562 0.4676 0.4836 -0.0113 -0.0129 0.0263  332 ASP A CG    
2645 O OD1   . ASP A 332 ? 0.4628 0.4740 0.4931 -0.0130 -0.0167 0.0282  332 ASP A OD1   
2646 O OD2   . ASP A 332 ? 0.4707 0.4888 0.5066 -0.0115 -0.0153 0.0314  332 ASP A OD2   
2647 N N     . GLU A 333 ? 0.4036 0.4252 0.4325 -0.0136 -0.0152 0.0316  333 GLU A N     
2648 C CA    . GLU A 333 ? 0.3408 0.3558 0.3625 -0.0127 -0.0112 0.0255  333 GLU A CA    
2649 C C     . GLU A 333 ? 0.2722 0.2898 0.2922 -0.0136 -0.0118 0.0259  333 GLU A C     
2650 O O     . GLU A 333 ? 0.3899 0.4075 0.4118 -0.0166 -0.0170 0.0294  333 GLU A O     
2651 C CB    . GLU A 333 ? 0.4088 0.4242 0.4273 -0.0096 -0.0102 0.0258  333 GLU A CB    
2652 C CG    . GLU A 333 ? 0.5739 0.5950 0.6018 -0.0107 -0.0123 0.0243  333 GLU A CG    
2653 C CD    . GLU A 333 ? 0.5087 0.5342 0.5408 -0.0119 -0.0132 0.0333  333 GLU A CD    
2654 O OE1   . GLU A 333 ? 0.4132 0.4377 0.4387 -0.0085 -0.0087 0.0234  333 GLU A OE1   
2655 O OE2   . GLU A 333 ? 0.4176 0.4422 0.4528 -0.0122 -0.0142 0.0345  333 GLU A OE2   
2656 N N     . ARG A 334 ? 0.0736 0.0964 0.0931 -0.0109 -0.0101 0.0215  334 ARG A N     
2657 C CA    . ARG A 334 ? 0.0966 0.1174 0.1114 -0.0121 -0.0078 0.0222  334 ARG A CA    
2658 C C     . ARG A 334 ? 0.2046 0.2271 0.2206 -0.0151 -0.0124 0.0262  334 ARG A C     
2659 O O     . ARG A 334 ? 0.3383 0.3601 0.3513 -0.0158 -0.0166 0.0272  334 ARG A O     
2660 C CB    . ARG A 334 ? 0.0931 0.1143 0.1028 -0.0086 -0.0066 0.0215  334 ARG A CB    
2661 C CG    . ARG A 334 ? 0.3210 0.3437 0.3286 -0.0086 -0.0060 0.0204  334 ARG A CG    
2662 C CD    . ARG A 334 ? 0.3157 0.3441 0.3285 -0.0077 -0.0050 0.0173  334 ARG A CD    
2663 N NE    . ARG A 334 ? 0.1415 0.1752 0.1540 -0.0093 -0.0060 0.0232  334 ARG A NE    
2664 C CZ    . ARG A 334 ? 0.1893 0.2168 0.2024 -0.0065 -0.0043 0.0168  334 ARG A CZ    
2665 N NH1   . ARG A 334 ? 0.0189 0.0462 0.0327 -0.0058 -0.0040 0.0170  334 ARG A NH1   
2666 N NH2   . ARG A 334 ? 0.0151 0.0423 0.0279 -0.0064 -0.0042 0.0165  334 ARG A NH2   
2667 N N     . THR A 335 ? 0.0279 0.0490 0.0448 -0.0147 -0.0124 0.0261  335 THR A N     
2668 C CA    . THR A 335 ? 0.0549 0.0749 0.0708 -0.0157 -0.0170 0.0273  335 THR A CA    
2669 C C     . THR A 335 ? 0.2295 0.2437 0.2416 -0.0124 -0.0244 0.0249  335 THR A C     
2670 O O     . THR A 335 ? 0.2892 0.3004 0.2932 -0.0092 -0.0279 0.0227  335 THR A O     
2671 C CB    . THR A 335 ? 0.1275 0.1471 0.1462 -0.0160 -0.0157 0.0280  335 THR A CB    
2672 O OG1   . THR A 335 ? 0.0761 0.0956 0.0917 -0.0121 -0.0092 0.0234  335 THR A OG1   
2673 C CG2   . THR A 335 ? 0.3233 0.3427 0.3382 -0.0141 -0.0178 0.0255  335 THR A CG2   
2674 N N     . LYS A 336 ? 0.1128 0.1249 0.1297 -0.0130 -0.0264 0.0260  336 LYS A N     
2675 C CA    . LYS A 336 ? 0.1057 0.1130 0.1203 -0.0105 -0.0330 0.0242  336 LYS A CA    
2676 C C     . LYS A 336 ? 0.3234 0.3288 0.3300 -0.0084 -0.0349 0.0233  336 LYS A C     
2677 O O     . LYS A 336 ? 0.3991 0.4001 0.3987 -0.0053 -0.0397 0.0216  336 LYS A O     
2678 C CB    . LYS A 336 ? 0.3340 0.3398 0.3560 -0.0122 -0.0338 0.0258  336 LYS A CB    
2679 C CG    . LYS A 336 ? 0.3502 0.3545 0.3780 -0.0124 -0.0349 0.0259  336 LYS A CG    
2680 C CD    . LYS A 336 ? 0.3656 0.3686 0.4005 -0.0147 -0.0334 0.0286  336 LYS A CD    
2681 C CE    . LYS A 336 ? 0.2993 0.2994 0.3396 -0.0142 -0.0358 0.0282  336 LYS A CE    
2682 N NZ    . LYS A 336 ? 0.2865 0.2832 0.3259 -0.0119 -0.0428 0.0251  336 LYS A NZ    
2683 N N     . LEU A 337 ? 0.3244 0.3326 0.3316 -0.0101 -0.0309 0.0248  337 LEU A N     
2684 C CA    . LEU A 337 ? 0.2197 0.2253 0.2186 -0.0078 -0.0325 0.0241  337 LEU A CA    
2685 C C     . LEU A 337 ? 0.2950 0.2980 0.2835 -0.0046 -0.0331 0.0226  337 LEU A C     
2686 O O     . LEU A 337 ? 0.3622 0.3602 0.3416 -0.0016 -0.0366 0.0220  337 LEU A O     
2687 C CB    . LEU A 337 ? 0.1964 0.2064 0.1988 -0.0104 -0.0277 0.0258  337 LEU A CB    
2688 C CG    . LEU A 337 ? 0.1693 0.1809 0.1800 -0.0132 -0.0269 0.0278  337 LEU A CG    
2689 C CD1   . LEU A 337 ? 0.0547 0.0727 0.0708 -0.0166 -0.0209 0.0299  337 LEU A CD1   
2690 C CD2   . LEU A 337 ? 0.3274 0.3337 0.3345 -0.0108 -0.0324 0.0272  337 LEU A CD2   
2691 N N     . LEU A 338 ? 0.2877 0.2938 0.2773 -0.0057 -0.0296 0.0223  338 LEU A N     
2692 C CA    . LEU A 338 ? 0.1355 0.1386 0.1148 -0.0028 -0.0296 0.0211  338 LEU A CA    
2693 C C     . LEU A 338 ? 0.0828 0.0820 0.0570 -0.0003 -0.0346 0.0199  338 LEU A C     
2694 O O     . LEU A 338 ? 0.1016 0.0963 0.0653 0.0020  -0.0362 0.0197  338 LEU A O     
2695 C CB    . LEU A 338 ? 0.1157 0.1234 0.0989 -0.0051 -0.0248 0.0212  338 LEU A CB    
2696 C CG    . LEU A 338 ? 0.1824 0.1954 0.1708 -0.0081 -0.0196 0.0224  338 LEU A CG    
2697 C CD1   . LEU A 338 ? 0.1176 0.1401 0.1172 -0.0121 -0.0145 0.0231  338 LEU A CD1   
2698 C CD2   . LEU A 338 ? 0.1607 0.1683 0.1373 -0.0052 -0.0187 0.0217  338 LEU A CD2   
2699 N N     . GLU A 339 ? 0.2312 0.2315 0.2129 -0.0014 -0.0370 0.0194  339 GLU A N     
2700 C CA    . GLU A 339 ? 0.2659 0.2621 0.2439 0.0004  -0.0420 0.0179  339 GLU A CA    
2701 C C     . GLU A 339 ? 0.3188 0.3093 0.2942 0.0016  -0.0475 0.0176  339 GLU A C     
2702 O O     . GLU A 339 ? 0.2848 0.2691 0.2523 0.0035  -0.0518 0.0163  339 GLU A O     
2703 C CB    . GLU A 339 ? 0.3414 0.3403 0.3282 -0.0010 -0.0424 0.0172  339 GLU A CB    
2704 C CG    . GLU A 339 ? 0.5965 0.5917 0.5781 0.0008  -0.0462 0.0154  339 GLU A CG    
2705 C CD    . GLU A 339 ? 0.7000 0.6945 0.6897 0.0004  -0.0496 0.0143  339 GLU A CD    
2706 O OE1   . GLU A 339 ? 0.7187 0.7177 0.7170 -0.0014 -0.0466 0.0148  339 GLU A OE1   
2707 O OE2   . GLU A 339 ? 0.6503 0.6388 0.6372 0.0019  -0.0554 0.0128  339 GLU A OE2   
2708 N N     . GLU A 340 ? 0.5210 0.5127 0.5032 0.0003  -0.0478 0.0185  340 GLU A N     
2709 C CA    . GLU A 340 ? 0.4917 0.4780 0.4719 0.0013  -0.0527 0.0182  340 GLU A CA    
2710 C C     . GLU A 340 ? 0.2998 0.2828 0.2696 0.0030  -0.0525 0.0189  340 GLU A C     
2711 O O     . GLU A 340 ? 0.3932 0.3693 0.3538 0.0052  -0.0565 0.0179  340 GLU A O     
2712 C CB    . GLU A 340 ? 0.6235 0.6123 0.6142 -0.0009 -0.0524 0.0194  340 GLU A CB    
2713 C CG    . GLU A 340 ? 0.6428 0.6317 0.6430 -0.0021 -0.0543 0.0189  340 GLU A CG    
2714 C CD    . GLU A 340 ? 0.5995 0.5892 0.6084 -0.0043 -0.0539 0.0204  340 GLU A CD    
2715 O OE1   . GLU A 340 ? 0.5501 0.5412 0.5582 -0.0051 -0.0517 0.0218  340 GLU A OE1   
2716 O OE2   . GLU A 340 ? 0.6554 0.6441 0.6720 -0.0053 -0.0556 0.0202  340 GLU A OE2   
2717 N N     . LYS A 341 ? 0.3159 0.3028 0.2868 0.0020  -0.0479 0.0205  341 LYS A N     
2718 C CA    . LYS A 341 ? 0.4403 0.4241 0.4026 0.0034  -0.0474 0.0214  341 LYS A CA    
2719 C C     . LYS A 341 ? 0.4025 0.3851 0.3552 0.0046  -0.0441 0.0216  341 LYS A C     
2720 O O     . LYS A 341 ? 0.3686 0.3446 0.3106 0.0063  -0.0458 0.0216  341 LYS A O     
2721 C CB    . LYS A 341 ? 0.4484 0.4365 0.4168 0.0018  -0.0441 0.0228  341 LYS A CB    
2722 C CG    . LYS A 341 ? 0.3806 0.3651 0.3426 0.0032  -0.0450 0.0238  341 LYS A CG    
2723 C CD    . LYS A 341 ? 0.1692 0.1585 0.1378 0.0013  -0.0412 0.0250  341 LYS A CD    
2724 C CE    . LYS A 341 ? 0.2258 0.2116 0.1888 0.0027  -0.0424 0.0260  341 LYS A CE    
2725 N NZ    . LYS A 341 ? 0.2346 0.2245 0.2044 0.0007  -0.0395 0.0271  341 LYS A NZ    
2726 N N     . GLY A 342 ? 0.4521 0.4399 0.4081 0.0036  -0.0395 0.0217  342 GLY A N     
2727 C CA    . GLY A 342 ? 0.5199 0.5064 0.4675 0.0044  -0.0361 0.0220  342 GLY A CA    
2728 C C     . GLY A 342 ? 0.5546 0.5353 0.4939 0.0055  -0.0391 0.0208  342 GLY A C     
2729 O O     . GLY A 342 ? 0.6332 0.6084 0.5618 0.0064  -0.0380 0.0209  342 GLY A O     
2730 N N     . LYS A 343 ? 0.3833 0.3639 0.3271 0.0054  -0.0429 0.0193  343 LYS A N     
2731 C CA    . LYS A 343 ? 0.2752 0.2504 0.2121 0.0066  -0.0458 0.0177  343 LYS A CA    
2732 C C     . LYS A 343 ? 0.2114 0.1885 0.1445 0.0061  -0.0409 0.0179  343 LYS A C     
2733 O O     . LYS A 343 ? 0.1942 0.1645 0.1162 0.0072  -0.0409 0.0173  343 LYS A O     
2734 C CB    . LYS A 343 ? 0.2251 0.1896 0.1503 0.0089  -0.0504 0.0167  343 LYS A CB    
2735 C CG    . LYS A 343 ? 0.3882 0.3503 0.3150 0.0095  -0.0541 0.0170  343 LYS A CG    
2736 C CD    . LYS A 343 ? 0.4631 0.4205 0.3916 0.0107  -0.0610 0.0148  343 LYS A CD    
2737 C CE    . LYS A 343 ? 0.4219 0.3789 0.3557 0.0107  -0.0643 0.0151  343 LYS A CE    
2738 N NZ    . LYS A 343 ? 0.3504 0.3070 0.2926 0.0106  -0.0694 0.0134  343 LYS A NZ    
2739 N N     . ILE A 344 ? 0.2343 0.2200 0.1764 0.0046  -0.0365 0.0186  344 ILE A N     
2740 C CA    . ILE A 344 ? 0.3359 0.3244 0.2762 0.0041  -0.0314 0.0187  344 ILE A CA    
2741 C C     . ILE A 344 ? 0.3980 0.3935 0.3493 0.0031  -0.0295 0.0181  344 ILE A C     
2742 O O     . ILE A 344 ? 0.5106 0.5094 0.4713 0.0018  -0.0294 0.0182  344 ILE A O     
2743 C CB    . ILE A 344 ? 0.3512 0.3402 0.2880 0.0040  -0.0263 0.0202  344 ILE A CB    
2744 C CG1   . ILE A 344 ? 0.2195 0.2119 0.1572 0.0036  -0.0209 0.0201  344 ILE A CG1   
2745 C CG2   . ILE A 344 ? 0.4228 0.4153 0.3668 0.0038  -0.0252 0.0210  344 ILE A CG2   
2746 C CD1   . ILE A 344 ? 0.4313 0.4225 0.3641 0.0033  -0.0165 0.0213  344 ILE A CD1   
2747 N N     . ILE A 345 ? 0.4451 0.4417 0.3952 0.0030  -0.0278 0.0173  345 ILE A N     
2748 C CA    . ILE A 345 ? 0.3106 0.3119 0.2702 0.0017  -0.0260 0.0164  345 ILE A CA    
2749 C C     . ILE A 345 ? 0.1882 0.1897 0.1470 0.0004  -0.0203 0.0166  345 ILE A C     
2750 O O     . ILE A 345 ? 0.1115 0.1108 0.0622 0.0020  -0.0181 0.0164  345 ILE A O     
2751 C CB    . ILE A 345 ? 0.2968 0.2985 0.2571 0.0020  -0.0291 0.0151  345 ILE A CB    
2752 C CG1   . ILE A 345 ? 0.1869 0.1853 0.1475 0.0025  -0.0352 0.0147  345 ILE A CG1   
2753 C CG2   . ILE A 345 ? 0.1847 0.1911 0.1562 -0.0002 -0.0275 0.0146  345 ILE A CG2   
2754 C CD1   . ILE A 345 ? 0.1002 0.1011 0.0706 0.0013  -0.0360 0.0153  345 ILE A CD1   
2755 N N     . VAL A 346 ? 0.2153 0.2222 0.1850 -0.0036 -0.0173 0.0175  346 VAL A N     
2756 C CA    . VAL A 346 ? 0.1968 0.2092 0.1718 -0.0066 -0.0120 0.0177  346 VAL A CA    
2757 C C     . VAL A 346 ? 0.2012 0.2258 0.1923 -0.0106 -0.0096 0.0183  346 VAL A C     
2758 O O     . VAL A 346 ? 0.1587 0.1841 0.1542 -0.0113 -0.0112 0.0190  346 VAL A O     
2759 C CB    . VAL A 346 ? 0.2545 0.2693 0.2321 -0.0076 -0.0099 0.0185  346 VAL A CB    
2760 C CG1   . VAL A 346 ? 0.0677 0.0707 0.0287 -0.0034 -0.0101 0.0184  346 VAL A CG1   
2761 C CG2   . VAL A 346 ? 0.2094 0.2292 0.1962 -0.0094 -0.0112 0.0197  346 VAL A CG2   
2762 N N     . GLU A 347 ? 0.2562 0.2902 0.2560 -0.0124 -0.0061 0.0177  347 GLU A N     
2763 C CA    . GLU A 347 ? 0.2508 0.2823 0.2567 -0.0098 -0.0037 0.0140  347 GLU A CA    
2764 C C     . GLU A 347 ? 0.3156 0.3454 0.3232 -0.0079 -0.0037 0.0134  347 GLU A C     
2765 O O     . GLU A 347 ? 0.5045 0.5312 0.5062 -0.0068 -0.0031 0.0145  347 GLU A O     
2766 C CB    . GLU A 347 ? 0.1668 0.1978 0.1726 -0.0083 -0.0030 0.0117  347 GLU A CB    
2767 C CG    . GLU A 347 ? 0.2229 0.2579 0.2266 -0.0101 -0.0037 0.0131  347 GLU A CG    
2768 C CD    . GLU A 347 ? 0.3104 0.3424 0.3151 -0.0098 -0.0034 0.0128  347 GLU A CD    
2769 O OE1   . GLU A 347 ? 0.3135 0.3506 0.3153 -0.0131 -0.0050 0.0156  347 GLU A OE1   
2770 O OE2   . GLU A 347 ? 0.2217 0.2480 0.2222 -0.0073 -0.0035 0.0134  347 GLU A OE2   
2771 N N     . PRO A 348 ? 0.1899 0.2250 0.1975 -0.0096 -0.0049 0.0194  348 PRO A N     
2772 C CA    . PRO A 348 ? 0.1291 0.1536 0.1331 -0.0061 -0.0033 0.0159  348 PRO A CA    
2773 C C     . PRO A 348 ? 0.1795 0.2077 0.1886 -0.0054 -0.0028 0.0136  348 PRO A C     
2774 O O     . PRO A 348 ? 0.2121 0.2368 0.2152 -0.0048 -0.0024 0.0142  348 PRO A O     
2775 C CB    . PRO A 348 ? 0.0459 0.0729 0.0570 -0.0069 -0.0042 0.0155  348 PRO A CB    
2776 C CG    . PRO A 348 ? 0.0157 0.0424 0.0265 -0.0078 -0.0048 0.0156  348 PRO A CG    
2777 C CD    . PRO A 348 ? 0.3504 0.3741 0.3539 -0.0079 -0.0045 0.0165  348 PRO A CD    
2778 N N     . GLY A 349 ? 0.1632 0.1974 0.1718 -0.0060 -0.0032 0.0185  349 GLY A N     
2779 C CA    . GLY A 349 ? 0.1199 0.1440 0.1235 -0.0037 -0.0019 0.0140  349 GLY A CA    
2780 C C     . GLY A 349 ? 0.2867 0.3132 0.2961 -0.0034 -0.0019 0.0130  349 GLY A C     
2781 O O     . GLY A 349 ? 0.3859 0.4086 0.3899 -0.0027 -0.0014 0.0136  349 GLY A O     
2782 N N     . GLU A 350 ? 0.0151 0.0411 0.0257 -0.0036 -0.0021 0.0139  350 GLU A N     
2783 C CA    . GLU A 350 ? 0.0149 0.0364 0.0214 -0.0028 -0.0018 0.0156  350 GLU A CA    
2784 C C     . GLU A 350 ? 0.1779 0.1991 0.1843 -0.0026 -0.0016 0.0152  350 GLU A C     
2785 O O     . GLU A 350 ? 0.2672 0.2913 0.2787 -0.0024 -0.0015 0.0139  350 GLU A O     
2786 C CB    . GLU A 350 ? 0.2068 0.2277 0.2149 -0.0032 -0.0022 0.0169  350 GLU A CB    
2787 C CG    . GLU A 350 ? 0.0130 0.0382 0.0268 -0.0036 -0.0025 0.0159  350 GLU A CG    
2788 C CD    . GLU A 350 ? 0.0584 0.0801 0.0667 -0.0040 -0.0028 0.0177  350 GLU A CD    
2789 O OE1   . GLU A 350 ? 0.1268 0.1529 0.1408 -0.0045 -0.0031 0.0165  350 GLU A OE1   
2790 O OE2   . GLU A 350 ? 0.0691 0.0953 0.0821 -0.0049 -0.0033 0.0160  350 GLU A OE2   
2791 N N     . LYS A 351 ? 0.1398 0.1649 0.1505 -0.0033 -0.0020 0.0138  351 LYS A N     
2792 C CA    . LYS A 351 ? 0.1720 0.1933 0.1775 -0.0028 -0.0017 0.0146  351 LYS A CA    
2793 C C     . LYS A 351 ? 0.1896 0.2113 0.1940 -0.0025 -0.0014 0.0134  351 LYS A C     
2794 O O     . LYS A 351 ? 0.2307 0.2555 0.2394 -0.0026 -0.0014 0.0119  351 LYS A O     
2795 C CB    . LYS A 351 ? 0.0149 0.0366 0.0204 -0.0035 -0.0021 0.0149  351 LYS A CB    
2796 C CG    . LYS A 351 ? 0.0151 0.0380 0.0193 -0.0039 -0.0021 0.0143  351 LYS A CG    
2797 C CD    . LYS A 351 ? 0.0482 0.0808 0.0565 -0.0063 -0.0033 0.0179  351 LYS A CD    
2798 C CE    . LYS A 351 ? 0.0898 0.1144 0.0922 -0.0051 -0.0024 0.0135  351 LYS A CE    
2799 N NZ    . LYS A 351 ? 0.2790 0.3075 0.2863 -0.0066 -0.0030 0.0124  351 LYS A NZ    
2800 N N     . TYR A 352 ? 0.1229 0.1449 0.1267 -0.0024 -0.0012 0.0130  352 TYR A N     
2801 C CA    . TYR A 352 ? 0.0131 0.0353 0.0162 -0.0021 -0.0010 0.0121  352 TYR A CA    
2802 C C     . TYR A 352 ? 0.0127 0.0340 0.0161 -0.0016 -0.0008 0.0121  352 TYR A C     
2803 O O     . TYR A 352 ? 0.3246 0.3487 0.3319 -0.0016 -0.0008 0.0105  352 TYR A O     
2804 C CB    . TYR A 352 ? 0.0133 0.0363 0.0157 -0.0024 -0.0011 0.0116  352 TYR A CB    
2805 C CG    . TYR A 352 ? 0.0938 0.1209 0.1005 -0.0032 -0.0014 0.0105  352 TYR A CG    
2806 C CD1   . TYR A 352 ? 0.0138 0.0384 0.0149 -0.0031 -0.0012 0.0107  352 TYR A CD1   
2807 C CD2   . TYR A 352 ? 0.1445 0.1722 0.1516 -0.0037 -0.0016 0.0110  352 TYR A CD2   
2808 C CE1   . TYR A 352 ? 0.0117 0.0402 0.0173 -0.0041 -0.0015 0.0095  352 TYR A CE1   
2809 C CE2   . TYR A 352 ? 0.1281 0.1536 0.1294 -0.0040 -0.0016 0.0118  352 TYR A CE2   
2810 C CZ    . TYR A 352 ? 0.0122 0.0413 0.0180 -0.0046 -0.0017 0.0100  352 TYR A CZ    
2811 O OH    . TYR A 352 ? 0.0572 0.0946 0.0606 -0.0069 -0.0024 0.0133  352 TYR A OH    
2812 N N     . GLY A 353 ? 0.0441 0.0648 0.0485 -0.0015 -0.0008 0.0128  353 GLY A N     
2813 C CA    . GLY A 353 ? 0.0100 0.0332 0.0192 -0.0012 -0.0007 0.0118  353 GLY A CA    
2814 C C     . GLY A 353 ? 0.0545 0.0777 0.0636 -0.0011 -0.0006 0.0118  353 GLY A C     
2815 O O     . GLY A 353 ? 0.1087 0.1293 0.1133 -0.0012 -0.0007 0.0129  353 GLY A O     
2816 N N     . LEU A 354 ? 0.1249 0.1475 0.1340 -0.0008 -0.0004 0.0117  354 LEU A N     
2817 C CA    . LEU A 354 ? 0.1158 0.1352 0.1208 -0.0006 -0.0003 0.0128  354 LEU A CA    
2818 C C     . LEU A 354 ? 0.1999 0.2199 0.2042 -0.0007 -0.0004 0.0124  354 LEU A C     
2819 O O     . LEU A 354 ? 0.4074 0.4306 0.4153 -0.0009 -0.0004 0.0108  354 LEU A O     
2820 C CB    . LEU A 354 ? 0.0823 0.1013 0.0873 -0.0003 -0.0002 0.0126  354 LEU A CB    
2821 C CG    . LEU A 354 ? 0.0121 0.0306 0.0179 -0.0001 0.0000  0.0131  354 LEU A CG    
2822 C CD1   . LEU A 354 ? 0.0471 0.0653 0.0527 0.0002  0.0001  0.0128  354 LEU A CD1   
2823 C CD2   . LEU A 354 ? 0.1584 0.1770 0.1651 -0.0001 -0.0001 0.0139  354 LEU A CD2   
2824 N N     . GLY A 355 ? 0.2557 0.2761 0.2603 -0.0008 -0.0005 0.0128  355 GLY A N     
2825 C CA    . GLY A 355 ? 0.1589 0.1799 0.1630 -0.0010 -0.0005 0.0125  355 GLY A CA    
2826 C C     . GLY A 355 ? 0.2108 0.2325 0.2147 -0.0014 -0.0007 0.0127  355 GLY A C     
2827 O O     . GLY A 355 ? 0.0969 0.1193 0.1004 -0.0016 -0.0008 0.0125  355 GLY A O     
2828 N N     . GLY A 356 ? 0.0132 0.0348 0.0175 -0.0016 -0.0008 0.0130  356 GLY A N     
2829 C CA    . GLY A 356 ? 0.0110 0.0365 0.0199 -0.0022 -0.0012 0.0122  356 GLY A CA    
2830 C C     . GLY A 356 ? 0.1569 0.1826 0.1668 -0.0024 -0.0014 0.0130  356 GLY A C     
2831 O O     . GLY A 356 ? 0.0951 0.1179 0.1002 -0.0027 -0.0015 0.0146  356 GLY A O     
2832 N N     . GLU A 357 ? 0.0141 0.0357 0.0199 -0.0019 -0.0012 0.0147  357 GLU A N     
2833 C CA    . GLU A 357 ? 0.0158 0.0373 0.0226 -0.0022 -0.0014 0.0156  357 GLU A CA    
2834 C C     . GLU A 357 ? 0.1386 0.1646 0.1501 -0.0026 -0.0016 0.0143  357 GLU A C     
2835 O O     . GLU A 357 ? 0.3483 0.3707 0.3541 -0.0022 -0.0013 0.0151  357 GLU A O     
2836 C CB    . GLU A 357 ? 0.1033 0.1280 0.1158 -0.0020 -0.0013 0.0146  357 GLU A CB    
2837 C CG    . GLU A 357 ? 0.3213 0.3419 0.3282 -0.0014 -0.0009 0.0152  357 GLU A CG    
2838 C CD    . GLU A 357 ? 0.4343 0.4579 0.4459 -0.0012 -0.0008 0.0137  357 GLU A CD    
2839 O OE1   . GLU A 357 ? 0.5349 0.5550 0.5414 -0.0011 -0.0007 0.0145  357 GLU A OE1   
2840 O OE2   . GLU A 357 ? 0.3876 0.4108 0.3997 -0.0009 -0.0006 0.0139  357 GLU A OE2   
2841 N N     . GLU A 358 ? 0.1514 0.1778 0.1636 -0.0032 -0.0020 0.0150  358 GLU A N     
2842 C CA    . GLU A 358 ? 0.2160 0.2392 0.2229 -0.0033 -0.0021 0.0167  358 GLU A CA    
2843 C C     . GLU A 358 ? 0.3225 0.3504 0.3336 -0.0038 -0.0022 0.0146  358 GLU A C     
2844 O O     . GLU A 358 ? 0.3282 0.3528 0.3336 -0.0036 -0.0020 0.0160  358 GLU A O     
2845 C CB    . GLU A 358 ? 0.3111 0.3341 0.3183 -0.0030 -0.0019 0.0169  358 GLU A CB    
2846 C CG    . GLU A 358 ? 0.2524 0.2746 0.2608 -0.0028 -0.0019 0.0175  358 GLU A CG    
2847 C CD    . GLU A 358 ? 0.2383 0.2645 0.2522 -0.0026 -0.0018 0.0160  358 GLU A CD    
2848 O OE1   . GLU A 358 ? 0.3435 0.3658 0.3526 -0.0027 -0.0018 0.0181  358 GLU A OE1   
2849 O OE2   . GLU A 358 ? 0.2334 0.2551 0.2419 -0.0019 -0.0013 0.0170  358 GLU A OE2   
2850 N N     . HIS A 359 ? 0.0127 0.0407 0.0231 -0.0038 -0.0021 0.0140  359 HIS A N     
2851 C CA    . HIS A 359 ? 0.0922 0.1173 0.0962 -0.0037 -0.0019 0.0147  359 HIS A CA    
2852 C C     . HIS A 359 ? 0.2344 0.2637 0.2437 -0.0048 -0.0024 0.0136  359 HIS A C     
2853 O O     . HIS A 359 ? 0.1861 0.2149 0.1958 -0.0050 -0.0026 0.0140  359 HIS A O     
2854 C CB    . HIS A 359 ? 0.0159 0.0409 0.0193 -0.0032 -0.0015 0.0138  359 HIS A CB    
2855 C CG    . HIS A 359 ? 0.0147 0.0393 0.0182 -0.0027 -0.0013 0.0136  359 HIS A CG    
2856 N ND1   . HIS A 359 ? 0.2179 0.2415 0.2219 -0.0023 -0.0012 0.0137  359 HIS A ND1   
2857 C CD2   . HIS A 359 ? 0.0147 0.0397 0.0178 -0.0026 -0.0012 0.0132  359 HIS A CD2   
2858 C CE1   . HIS A 359 ? 0.0141 0.0376 0.0180 -0.0020 -0.0010 0.0134  359 HIS A CE1   
2859 N NE2   . HIS A 359 ? 0.0143 0.0386 0.0176 -0.0021 -0.0010 0.0132  359 HIS A NE2   
2860 N N     . ILE A 360 ? 0.1658 0.1924 0.1686 -0.0048 -0.0023 0.0145  360 ILE A N     
2861 C CA    . ILE A 360 ? 0.1704 0.1975 0.1726 -0.0056 -0.0026 0.0144  360 ILE A CA    
2862 C C     . ILE A 360 ? 0.2809 0.3124 0.2880 -0.0062 -0.0026 0.0122  360 ILE A C     
2863 O O     . ILE A 360 ? 0.3019 0.3411 0.3071 -0.0073 -0.0029 0.0163  360 ILE A O     
2864 C CB    . ILE A 360 ? 0.0995 0.1306 0.1077 -0.0075 -0.0035 0.0139  360 ILE A CB    
2865 C CG1   . ILE A 360 ? 0.1757 0.2093 0.1833 -0.0081 -0.0038 0.0149  360 ILE A CG1   
2866 C CG2   . ILE A 360 ? 0.1741 0.2042 0.1834 -0.0076 -0.0040 0.0149  360 ILE A CG2   
2867 C CD1   . ILE A 360 ? 0.0240 0.0609 0.0274 -0.0115 -0.0054 0.0196  360 ILE A CD1   
2868 N N     . ARG A 361 ? 0.2622 0.2940 0.2688 -0.0068 -0.0027 0.0119  361 ARG A N     
2869 C CA    . ARG A 361 ? 0.1739 0.2108 0.1781 -0.0081 -0.0033 0.0133  361 ARG A CA    
2870 C C     . ARG A 361 ? 0.1882 0.2216 0.1834 -0.0100 -0.0021 0.0153  361 ARG A C     
2871 O O     . ARG A 361 ? 0.4751 0.5080 0.4701 -0.0106 -0.0032 0.0158  361 ARG A O     
2872 C CB    . ARG A 361 ? 0.1639 0.1972 0.1682 -0.0066 -0.0032 0.0112  361 ARG A CB    
2873 C CG    . ARG A 361 ? 0.1653 0.2047 0.1675 -0.0086 -0.0027 0.0126  361 ARG A CG    
2874 C CD    . ARG A 361 ? 0.1009 0.1400 0.1027 -0.0087 -0.0027 0.0117  361 ARG A CD    
2875 N NE    . ARG A 361 ? 0.3863 0.4249 0.3857 -0.0101 -0.0021 0.0122  361 ARG A NE    
2876 C CZ    . ARG A 361 ? 0.2351 0.2750 0.2353 -0.0104 -0.0026 0.0116  361 ARG A CZ    
2877 N NH1   . ARG A 361 ? 0.2038 0.2409 0.2051 -0.0086 -0.0027 0.0100  361 ARG A NH1   
2878 N NH2   . ARG A 361 ? 0.1600 0.1953 0.1551 -0.0109 -0.0015 0.0120  361 ARG A NH2   
2879 N N     . ILE A 362 ? 0.1675 0.1891 0.1494 -0.0088 0.0012  0.0154  362 ILE A N     
2880 C CA    . ILE A 362 ? 0.2339 0.2416 0.1991 -0.0065 0.0023  0.0160  362 ILE A CA    
2881 C C     . ILE A 362 ? 0.2669 0.2675 0.2231 -0.0048 0.0063  0.0156  362 ILE A C     
2882 O O     . ILE A 362 ? 0.1484 0.1510 0.1084 -0.0057 0.0090  0.0150  362 ILE A O     
2883 C CB    . ILE A 362 ? 0.2225 0.2233 0.1793 -0.0045 0.0023  0.0172  362 ILE A CB    
2884 C CG1   . ILE A 362 ? 0.1494 0.1455 0.1008 -0.0031 0.0067  0.0175  362 ILE A CG1   
2885 C CG2   . ILE A 362 ? 0.3759 0.3859 0.3447 -0.0067 -0.0004 0.0176  362 ILE A CG2   
2886 C CD1   . ILE A 362 ? 0.3226 0.3155 0.2680 0.0000  0.0067  0.0191  362 ILE A CD1   
2887 N N     . ASN A 363 ? 0.4052 0.4007 0.3514 -0.0014 0.0061  0.0164  363 ASN A N     
2888 C CA    . ASN A 363 ? 0.2741 0.2717 0.2175 -0.0005 0.0085  0.0168  363 ASN A CA    
2889 C C     . ASN A 363 ? 0.2860 0.2834 0.2219 -0.0022 0.0091  0.0182  363 ASN A C     
2890 O O     . ASN A 363 ? 0.1211 0.1134 0.0485 -0.0022 0.0065  0.0186  363 ASN A O     
2891 C CB    . ASN A 363 ? 0.4697 0.4675 0.4093 -0.0002 0.0060  0.0163  363 ASN A CB    
2892 C CG    . ASN A 363 ? 0.4302 0.4287 0.3677 -0.0014 0.0084  0.0157  363 ASN A CG    
2893 O OD1   . ASN A 363 ? 0.3253 0.3214 0.2581 -0.0030 0.0110  0.0158  363 ASN A OD1   
2894 N ND2   . ASN A 363 ? 0.3656 0.3642 0.3051 -0.0008 0.0076  0.0146  363 ASN A ND2   
2895 N N     . ILE A 364 ? 0.5441 0.5411 0.4801 -0.0035 0.0126  0.0180  364 ILE A N     
2896 C CA    . ILE A 364 ? 0.4821 0.4703 0.4082 -0.0043 0.0144  0.0177  364 ILE A CA    
2897 C C     . ILE A 364 ? 0.3831 0.3636 0.3010 -0.0043 0.0168  0.0164  364 ILE A C     
2898 O O     . ILE A 364 ? 0.2559 0.2290 0.1674 -0.0041 0.0200  0.0161  364 ILE A O     
2899 C CB    . ILE A 364 ? 0.2872 0.2777 0.2181 -0.0050 0.0168  0.0181  364 ILE A CB    
2900 C CG1   . ILE A 364 ? 0.4648 0.4615 0.4050 -0.0057 0.0187  0.0174  364 ILE A CG1   
2901 C CG2   . ILE A 364 ? 0.1771 0.1729 0.1134 -0.0044 0.0144  0.0195  364 ILE A CG2   
2902 C CD1   . ILE A 364 ? 0.4067 0.4031 0.3493 -0.0066 0.0213  0.0171  364 ILE A CD1   
2903 N N     . GLY A 365 ? 0.4158 0.3978 0.3341 -0.0042 0.0156  0.0157  365 GLY A N     
2904 C CA    . GLY A 365 ? 0.4362 0.4101 0.3454 -0.0037 0.0173  0.0146  365 GLY A CA    
2905 C C     . GLY A 365 ? 0.4280 0.3923 0.3246 -0.0018 0.0148  0.0144  365 GLY A C     
2906 O O     . GLY A 365 ? 0.5136 0.4756 0.4062 -0.0011 0.0130  0.0135  365 GLY A O     
2907 N N     . CYS A 366 ? 0.3342 0.2924 0.2242 -0.0007 0.0143  0.0151  366 CYS A N     
2908 C CA    . CYS A 366 ? 0.4268 0.3755 0.3048 0.0017  0.0110  0.0149  366 CYS A CA    
2909 C C     . CYS A 366 ? 0.4612 0.3995 0.3289 0.0032  0.0137  0.0152  366 CYS A C     
2910 O O     . CYS A 366 ? 0.6156 0.5552 0.4869 0.0023  0.0174  0.0158  366 CYS A O     
2911 C CB    . CYS A 366 ? 0.2771 0.2298 0.1583 0.0020  0.0058  0.0155  366 CYS A CB    
2912 S SG    . CYS A 366 ? 0.2887 0.2522 0.1828 0.0002  0.0062  0.0171  366 CYS A SG    
2913 N N     . PRO A 367 ? 0.3836 0.3110 0.2383 0.0059  0.0119  0.0148  367 PRO A N     
2914 C CA    . PRO A 367 ? 0.4062 0.3234 0.2506 0.0079  0.0139  0.0153  367 PRO A CA    
2915 C C     . PRO A 367 ? 0.4050 0.3254 0.2534 0.0075  0.0129  0.0165  367 PRO A C     
2916 O O     . PRO A 367 ? 0.3107 0.2375 0.1651 0.0069  0.0088  0.0169  367 PRO A O     
2917 C CB    . PRO A 367 ? 0.4619 0.3684 0.2929 0.0111  0.0103  0.0145  367 PRO A CB    
2918 C CG    . PRO A 367 ? 0.2696 0.1794 0.1029 0.0106  0.0084  0.0133  367 PRO A CG    
2919 C CD    . PRO A 367 ? 0.2749 0.1984 0.1234 0.0075  0.0078  0.0137  367 PRO A CD    
2920 N N     . ARG A 368 ? 0.4849 0.4005 0.3299 0.0079  0.0169  0.0172  368 ARG A N     
2921 C CA    . ARG A 368 ? 0.4972 0.4152 0.3454 0.0076  0.0164  0.0183  368 ARG A CA    
2922 C C     . ARG A 368 ? 0.5938 0.5084 0.4364 0.0095  0.0110  0.0186  368 ARG A C     
2923 O O     . ARG A 368 ? 0.4496 0.3703 0.2988 0.0086  0.0087  0.0194  368 ARG A O     
2924 C CB    . ARG A 368 ? 0.3733 0.2837 0.2155 0.0085  0.0212  0.0188  368 ARG A CB    
2925 C CG    . ARG A 368 ? 0.2551 0.1665 0.0989 0.0086  0.0209  0.0199  368 ARG A CG    
2926 C CD    . ARG A 368 ? 0.2841 0.2071 0.1422 0.0056  0.0224  0.0203  368 ARG A CD    
2927 N NE    . ARG A 368 ? 0.4413 0.3658 0.3037 0.0042  0.0270  0.0197  368 ARG A NE    
2928 C CZ    . ARG A 368 ? 0.5617 0.4828 0.4234 0.0041  0.0315  0.0198  368 ARG A CZ    
2929 N NH1   . ARG A 368 ? 0.5970 0.5133 0.4541 0.0053  0.0323  0.0207  368 ARG A NH1   
2930 N NH2   . ARG A 368 ? 0.5312 0.4537 0.3972 0.0029  0.0351  0.0191  368 ARG A NH2   
2931 N N     . SER A 369 ? 0.6593 0.5643 0.4901 0.0123  0.0086  0.0178  369 SER A N     
2932 C CA    . SER A 369 ? 0.5436 0.4453 0.3695 0.0143  0.0026  0.0177  369 SER A CA    
2933 C C     . SER A 369 ? 0.6165 0.5293 0.4542 0.0123  -0.0017 0.0177  369 SER A C     
2934 O O     . SER A 369 ? 0.6879 0.6043 0.5299 0.0121  -0.0043 0.0186  369 SER A O     
2935 C CB    . SER A 369 ? 0.4450 0.3361 0.2581 0.0174  0.0002  0.0164  369 SER A CB    
2936 O OG    . SER A 369 ? 0.3938 0.2889 0.2107 0.0163  -0.0005 0.0153  369 SER A OG    
2937 N N     . VAL A 370 ? 0.4074 0.3261 0.2512 0.0109  -0.0019 0.0169  370 VAL A N     
2938 C CA    . VAL A 370 ? 0.2823 0.2119 0.1381 0.0090  -0.0054 0.0171  370 VAL A CA    
2939 C C     . VAL A 370 ? 0.2343 0.1739 0.1020 0.0065  -0.0028 0.0186  370 VAL A C     
2940 O O     . VAL A 370 ? 0.2902 0.2362 0.1653 0.0058  -0.0059 0.0194  370 VAL A O     
2941 C CB    . VAL A 370 ? 0.4274 0.3613 0.2872 0.0080  -0.0057 0.0160  370 VAL A CB    
2942 C CG1   . VAL A 370 ? 0.4372 0.3819 0.3093 0.0065  -0.0093 0.0162  370 VAL A CG1   
2943 C CG2   . VAL A 370 ? 0.4571 0.3807 0.3048 0.0107  -0.0081 0.0144  370 VAL A CG2   
2944 N N     . LEU A 371 ? 0.4333 0.3743 0.3031 0.0052  0.0027  0.0188  371 LEU A N     
2945 C CA    . LEU A 371 ? 0.4233 0.3741 0.3050 0.0029  0.0049  0.0199  371 LEU A CA    
2946 C C     . LEU A 371 ? 0.3174 0.2673 0.1986 0.0034  0.0037  0.0211  371 LEU A C     
2947 O O     . LEU A 371 ? 0.2685 0.2276 0.1601 0.0020  0.0029  0.0221  371 LEU A O     
2948 C CB    . LEU A 371 ? 0.3728 0.3236 0.2560 0.0018  0.0106  0.0196  371 LEU A CB    
2949 C CG    . LEU A 371 ? 0.4261 0.3868 0.3217 -0.0004 0.0128  0.0202  371 LEU A CG    
2950 C CD1   . LEU A 371 ? 0.1325 0.1052 0.0404 -0.0017 0.0103  0.0205  371 LEU A CD1   
2951 C CD2   . LEU A 371 ? 0.2201 0.1792 0.1162 -0.0012 0.0179  0.0195  371 LEU A CD2   
2952 N N     . GLU A 372 ? 0.2322 0.1711 0.1013 0.0057  0.0036  0.0211  372 GLU A N     
2953 C CA    . GLU A 372 ? 0.2654 0.2034 0.1339 0.0063  0.0023  0.0223  372 GLU A CA    
2954 C C     . GLU A 372 ? 0.4226 0.3631 0.2933 0.0069  -0.0037 0.0225  372 GLU A C     
2955 O O     . GLU A 372 ? 0.4988 0.4448 0.3762 0.0061  -0.0050 0.0237  372 GLU A O     
2956 C CB    . GLU A 372 ? 0.4604 0.3861 0.3156 0.0087  0.0042  0.0223  372 GLU A CB    
2957 C CG    . GLU A 372 ? 0.6004 0.5144 0.4418 0.0116  0.0029  0.0212  372 GLU A CG    
2958 C CD    . GLU A 372 ? 0.5371 0.4398 0.3667 0.0139  0.0064  0.0214  372 GLU A CD    
2959 O OE1   . GLU A 372 ? 0.5775 0.4814 0.4101 0.0127  0.0114  0.0220  372 GLU A OE1   
2960 O OE2   . GLU A 372 ? 0.5056 0.3981 0.3231 0.0170  0.0040  0.0211  372 GLU A OE2   
2961 N N     . GLU A 373 ? 0.4062 0.3425 0.2718 0.0084  -0.0075 0.0214  373 GLU A N     
2962 C CA    . GLU A 373 ? 0.2335 0.1725 0.1027 0.0089  -0.0135 0.0214  373 GLU A CA    
2963 C C     . GLU A 373 ? 0.3952 0.3472 0.2794 0.0064  -0.0138 0.0220  373 GLU A C     
2964 O O     . GLU A 373 ? 0.6926 0.6493 0.5833 0.0062  -0.0171 0.0227  373 GLU A O     
2965 C CB    . GLU A 373 ? 0.2581 0.1893 0.1185 0.0112  -0.0180 0.0197  373 GLU A CB    
2966 C CG    . GLU A 373 ? 0.4514 0.3697 0.2974 0.0145  -0.0197 0.0192  373 GLU A CG    
2967 C CD    . GLU A 373 ? 0.6799 0.5890 0.5143 0.0162  -0.0169 0.0182  373 GLU A CD    
2968 O OE1   . GLU A 373 ? 0.7550 0.6559 0.5801 0.0178  -0.0141 0.0185  373 GLU A OE1   
2969 O OE2   . GLU A 373 ? 0.7276 0.6374 0.5625 0.0160  -0.0174 0.0170  373 GLU A OE2   
2970 N N     . ILE A 374 ? 0.3443 0.3020 0.2340 0.0047  -0.0103 0.0217  374 ILE A N     
2971 C CA    . ILE A 374 ? 0.2777 0.2480 0.1818 0.0029  -0.0100 0.0224  374 ILE A CA    
2972 C C     . ILE A 374 ? 0.2618 0.2387 0.1739 0.0020  -0.0083 0.0240  374 ILE A C     
2973 O O     . ILE A 374 ? 0.2067 0.1911 0.1285 0.0022  -0.0099 0.0246  374 ILE A O     
2974 C CB    . ILE A 374 ? 0.3091 0.2837 0.2171 0.0015  -0.0062 0.0217  374 ILE A CB    
2975 C CG1   . ILE A 374 ? 0.2958 0.2668 0.1992 0.0023  -0.0087 0.0202  374 ILE A CG1   
2976 C CG2   . ILE A 374 ? 0.1181 0.1053 0.0408 0.0006  -0.0045 0.0225  374 ILE A CG2   
2977 C CD1   . ILE A 374 ? 0.1742 0.1480 0.0798 0.0011  -0.0047 0.0194  374 ILE A CD1   
2978 N N     . LEU A 375 ? 0.3031 0.2764 0.2111 0.0017  -0.0049 0.0244  375 LEU A N     
2979 C CA    . LEU A 375 ? 0.3193 0.2987 0.2347 0.0009  -0.0032 0.0258  375 LEU A CA    
2980 C C     . LEU A 375 ? 0.4699 0.4461 0.3825 0.0020  -0.0066 0.0267  375 LEU A C     
2981 O O     . LEU A 375 ? 0.7258 0.7089 0.6470 0.0020  -0.0068 0.0278  375 LEU A O     
2982 C CB    . LEU A 375 ? 0.3955 0.3723 0.3083 -0.0001 0.0016  0.0257  375 LEU A CB    
2983 C CG    . LEU A 375 ? 0.4221 0.4018 0.3383 -0.0013 0.0051  0.0246  375 LEU A CG    
2984 C CD1   . LEU A 375 ? 0.4273 0.4012 0.3385 -0.0015 0.0094  0.0242  375 LEU A CD1   
2985 C CD2   . LEU A 375 ? 0.3584 0.3504 0.2891 -0.0019 0.0056  0.0250  375 LEU A CD2   
2986 N N     . ASN A 376 ? 0.4041 0.3695 0.3045 0.0037  -0.0090 0.0261  376 ASN A N     
2987 C CA    . ASN A 376 ? 0.3800 0.3419 0.2774 0.0051  -0.0127 0.0268  376 ASN A CA    
2988 C C     . ASN A 376 ? 0.4589 0.4274 0.3655 0.0051  -0.0170 0.0269  376 ASN A C     
2989 O O     . ASN A 376 ? 0.3521 0.3236 0.2633 0.0053  -0.0184 0.0279  376 ASN A O     
2990 C CB    . ASN A 376 ? 0.5716 0.5205 0.4542 0.0077  -0.0151 0.0257  376 ASN A CB    
2991 C CG    . ASN A 376 ? 0.7262 0.6696 0.6034 0.0092  -0.0172 0.0264  376 ASN A CG    
2992 O OD1   . ASN A 376 ? 0.7292 0.6714 0.6065 0.0104  -0.0223 0.0262  376 ASN A OD1   
2993 N ND2   . ASN A 376 ? 0.6001 0.5396 0.4724 0.0094  -0.0133 0.0271  376 ASN A ND2   
2994 N N     . ARG A 377 ? 0.3925 0.3629 0.3016 0.0051  -0.0188 0.0258  377 ARG A N     
2995 C CA    . ARG A 377 ? 0.1652 0.1410 0.0831 0.0052  -0.0226 0.0256  377 ARG A CA    
2996 C C     . ARG A 377 ? 0.1353 0.1213 0.0660 0.0046  -0.0194 0.0260  377 ARG A C     
2997 O O     . ARG A 377 ? 0.2649 0.2534 0.2025 0.0048  -0.0217 0.0256  377 ARG A O     
2998 C CB    . ARG A 377 ? 0.1494 0.1229 0.0655 0.0057  -0.0258 0.0239  377 ARG A CB    
2999 C CG    . ARG A 377 ? 0.1885 0.1503 0.0912 0.0075  -0.0292 0.0226  377 ARG A CG    
3000 C CD    . ARG A 377 ? 0.2327 0.1925 0.1333 0.0079  -0.0310 0.0209  377 ARG A CD    
3001 N NE    . ARG A 377 ? 0.3624 0.3107 0.2502 0.0104  -0.0347 0.0193  377 ARG A NE    
3002 C CZ    . ARG A 377 ? 0.4558 0.4008 0.3424 0.0117  -0.0399 0.0175  377 ARG A CZ    
3003 N NH1   . ARG A 377 ? 0.3538 0.3062 0.2514 0.0105  -0.0417 0.0171  377 ARG A NH1   
3004 N NH2   . ARG A 377 ? 0.6187 0.5527 0.4931 0.0144  -0.0432 0.0159  377 ARG A NH2   
3005 N N     . LEU A 378 ? 0.1112 0.1007 0.0443 0.0042  -0.0143 0.0260  378 LEU A N     
3006 C CA    . LEU A 378 ? 0.2420 0.2339 0.1837 0.0042  -0.0116 0.0246  378 LEU A CA    
3007 C C     . LEU A 378 ? 0.3255 0.3166 0.2690 0.0039  -0.0110 0.0251  378 LEU A C     
3008 O O     . LEU A 378 ? 0.3730 0.3674 0.3262 0.0006  -0.0123 0.0243  378 LEU A O     
3009 C CB    . LEU A 378 ? 0.3240 0.3154 0.2663 0.0033  -0.0070 0.0235  378 LEU A CB    
3010 C CG    . LEU A 378 ? 0.4080 0.4009 0.3539 0.0017  -0.0079 0.0220  378 LEU A CG    
3011 C CD1   . LEU A 378 ? 0.5187 0.5120 0.4578 0.0036  -0.0084 0.0229  378 LEU A CD1   
3012 C CD2   . LEU A 378 ? 0.5580 0.5557 0.5130 -0.0024 -0.0047 0.0208  378 LEU A CD2   
3013 N N     . ARG A 379 ? 0.4636 0.4546 0.4020 0.0048  -0.0092 0.0270  379 ARG A N     
3014 C CA    . ARG A 379 ? 0.4665 0.4567 0.4057 0.0052  -0.0091 0.0277  379 ARG A CA    
3015 C C     . ARG A 379 ? 0.2727 0.2623 0.2121 0.0055  -0.0143 0.0283  379 ARG A C     
3016 O O     . ARG A 379 ? 0.3089 0.2992 0.2549 0.0042  -0.0157 0.0272  379 ARG A O     
3017 C CB    . ARG A 379 ? 0.4882 0.4779 0.4213 0.0039  -0.0075 0.0301  379 ARG A CB    
3018 C CG    . ARG A 379 ? 0.2725 0.2624 0.2068 0.0041  -0.0067 0.0311  379 ARG A CG    
3019 C CD    . ARG A 379 ? 0.3335 0.3162 0.2565 0.0027  -0.0068 0.0325  379 ARG A CD    
3020 N NE    . ARG A 379 ? 0.3515 0.3244 0.2633 0.0039  -0.0104 0.0315  379 ARG A NE    
3021 C CZ    . ARG A 379 ? 0.3381 0.3085 0.2483 0.0053  -0.0152 0.0315  379 ARG A CZ    
3022 N NH1   . ARG A 379 ? 0.3548 0.3314 0.2737 0.0055  -0.0166 0.0323  379 ARG A NH1   
3023 N NH2   . ARG A 379 ? 0.3752 0.3363 0.2750 0.0069  -0.0185 0.0303  379 ARG A NH2   
3024 N N     . HIS A 380 ? 0.1701 0.1562 0.1028 0.0054  -0.0182 0.0289  380 HIS A N     
3025 C CA    . HIS A 380 ? 0.1615 0.1449 0.0942 0.0059  -0.0238 0.0286  380 HIS A CA    
3026 C C     . HIS A 380 ? 0.1703 0.1583 0.1137 0.0051  -0.0253 0.0272  380 HIS A C     
3027 O O     . HIS A 380 ? 0.4492 0.4377 0.3973 0.0046  -0.0277 0.0273  380 HIS A O     
3028 C CB    . HIS A 380 ? 0.1805 0.1562 0.1037 0.0065  -0.0279 0.0277  380 HIS A CB    
3029 C CG    . HIS A 380 ? 0.4266 0.3987 0.3499 0.0074  -0.0341 0.0268  380 HIS A CG    
3030 N ND1   . HIS A 380 ? 0.5309 0.5005 0.4534 0.0081  -0.0366 0.0275  380 HIS A ND1   
3031 C CD2   . HIS A 380 ? 0.4670 0.4371 0.3911 0.0078  -0.0386 0.0252  380 HIS A CD2   
3032 C CE1   . HIS A 380 ? 0.4693 0.4356 0.3924 0.0088  -0.0423 0.0263  380 HIS A CE1   
3033 N NE2   . HIS A 380 ? 0.4178 0.3844 0.3422 0.0086  -0.0436 0.0248  380 HIS A NE2   
3034 N N     . THR A 381 ? 0.2319 0.2225 0.1795 0.0042  -0.0238 0.0260  381 THR A N     
3035 C CA    . THR A 381 ? 0.2748 0.2693 0.2335 0.0016  -0.0254 0.0249  381 THR A CA    
3036 C C     . THR A 381 ? 0.3227 0.3218 0.2914 -0.0017 -0.0238 0.0253  381 THR A C     
3037 O O     . THR A 381 ? 0.3931 0.3947 0.3697 -0.0036 -0.0260 0.0257  381 THR A O     
3038 C CB    . THR A 381 ? 0.2534 0.2508 0.2157 0.0001  -0.0231 0.0238  381 THR A CB    
3039 O OG1   . THR A 381 ? 0.2485 0.2424 0.2014 0.0028  -0.0238 0.0236  381 THR A OG1   
3040 C CG2   . THR A 381 ? 0.2480 0.2502 0.2219 -0.0030 -0.0247 0.0235  381 THR A CG2   
3041 N N     . PHE A 382 ? 0.1497 0.1510 0.1194 -0.0029 -0.0196 0.0256  382 PHE A N     
3042 C CA    . PHE A 382 ? 0.2935 0.3035 0.2761 -0.0070 -0.0172 0.0263  382 PHE A CA    
3043 C C     . PHE A 382 ? 0.4733 0.4805 0.4520 -0.0058 -0.0172 0.0270  382 PHE A C     
3044 O O     . PHE A 382 ? 0.4298 0.4451 0.4188 -0.0087 -0.0148 0.0275  382 PHE A O     
3045 C CB    . PHE A 382 ? 0.4571 0.4762 0.4484 -0.0096 -0.0128 0.0258  382 PHE A CB    
3046 C CG    . PHE A 382 ? 0.3364 0.3587 0.3317 -0.0108 -0.0122 0.0252  382 PHE A CG    
3047 C CD1   . PHE A 382 ? 0.4626 0.4884 0.4657 -0.0131 -0.0130 0.0260  382 PHE A CD1   
3048 C CD2   . PHE A 382 ? 0.3481 0.3687 0.3383 -0.0095 -0.0106 0.0241  382 PHE A CD2   
3049 C CE1   . PHE A 382 ? 0.3314 0.3596 0.3376 -0.0141 -0.0121 0.0256  382 PHE A CE1   
3050 C CE2   . PHE A 382 ? 0.3383 0.3621 0.3322 -0.0105 -0.0101 0.0235  382 PHE A CE2   
3051 C CZ    . PHE A 382 ? 0.1883 0.2164 0.1905 -0.0128 -0.0108 0.0243  382 PHE A CZ    
3052 N N     . SER A 383 ? 0.5413 0.5393 0.5065 -0.0013 -0.0193 0.0273  383 SER A N     
3053 C CA    . SER A 383 ? 0.6211 0.6163 0.5822 0.0001  -0.0191 0.0282  383 SER A CA    
3054 C C     . SER A 383 ? 0.4324 0.4288 0.3987 -0.0008 -0.0228 0.0288  383 SER A C     
3055 O O     . SER A 383 ? 0.5040 0.4996 0.4714 -0.0005 -0.0265 0.0286  383 SER A O     
3056 C CB    . SER A 383 ? 0.8019 0.7908 0.7492 0.0047  -0.0186 0.0295  383 SER A CB    
3057 O OG    . SER A 383 ? 0.8967 0.8848 0.8399 0.0055  -0.0139 0.0296  383 SER A OG    
3058 O OXT   . SER A 383 ? 0.3780 0.3762 0.3477 -0.0019 -0.0222 0.0295  383 SER A OXT   
3059 N N     . LYS B 6   ? 0.9045 0.7618 0.6568 0.0258  -0.0022 -0.0561 6   LYS B N     
3060 C CA    . LYS B 6   ? 0.8901 0.7445 0.6378 0.0256  0.0052  -0.0513 6   LYS B CA    
3061 C C     . LYS B 6   ? 0.9293 0.7967 0.6924 0.0215  0.0106  -0.0489 6   LYS B C     
3062 O O     . LYS B 6   ? 0.9538 0.8293 0.7267 0.0197  0.0085  -0.0486 6   LYS B O     
3063 C CB    . LYS B 6   ? 0.9363 0.7825 0.6739 0.0281  0.0034  -0.0489 6   LYS B CB    
3064 C CG    . LYS B 6   ? 0.9022 0.7489 0.6404 0.0267  0.0105  -0.0438 6   LYS B CG    
3065 C CD    . LYS B 6   ? 0.7965 0.6378 0.5283 0.0285  0.0082  -0.0418 6   LYS B CD    
3066 C CE    . LYS B 6   ? 0.6802 0.5225 0.4141 0.0269  0.0153  -0.0371 6   LYS B CE    
3067 N NZ    . LYS B 6   ? 0.5580 0.3960 0.2870 0.0284  0.0132  -0.0353 6   LYS B NZ    
3068 N N     . ALA B 7   ? 0.9517 0.8207 0.7171 0.0202  0.0172  -0.0471 7   ALA B N     
3069 C CA    . ALA B 7   ? 0.8143 0.6933 0.5923 0.0169  0.0229  -0.0439 7   ALA B CA    
3070 C C     . ALA B 7   ? 0.7183 0.5932 0.4920 0.0171  0.0255  -0.0396 7   ALA B C     
3071 O O     . ALA B 7   ? 0.7337 0.5969 0.4940 0.0195  0.0273  -0.0380 7   ALA B O     
3072 C CB    . ALA B 7   ? 0.8431 0.7232 0.6236 0.0157  0.0292  -0.0426 7   ALA B CB    
3073 N N     . ILE B 8   ? 0.6425 0.5266 0.4272 0.0149  0.0258  -0.0379 8   ILE B N     
3074 C CA    . ILE B 8   ? 0.7686 0.6499 0.5509 0.0148  0.0279  -0.0343 8   ILE B CA    
3075 C C     . ILE B 8   ? 0.6924 0.5799 0.4848 0.0118  0.0348  -0.0307 8   ILE B C     
3076 O O     . ILE B 8   ? 0.6712 0.5699 0.4772 0.0093  0.0356  -0.0309 8   ILE B O     
3077 C CB    . ILE B 8   ? 0.8329 0.7186 0.6192 0.0148  0.0225  -0.0350 8   ILE B CB    
3078 C CG1   . ILE B 8   ? 0.8458 0.7297 0.6285 0.0166  0.0147  -0.0396 8   ILE B CG1   
3079 C CG2   . ILE B 8   ? 0.6907 0.5688 0.4686 0.0162  0.0232  -0.0320 8   ILE B CG2   
3080 C CD1   . ILE B 8   ? 0.7131 0.6021 0.5016 0.0162  0.0088  -0.0407 8   ILE B CD1   
3081 N N     . ASN B 9   ? 0.6298 0.5097 0.4158 0.0122  0.0395  -0.0275 9   ASN B N     
3082 C CA    . ASN B 9   ? 0.5627 0.4473 0.3584 0.0093  0.0456  -0.0243 9   ASN B CA    
3083 C C     . ASN B 9   ? 0.5511 0.4463 0.3594 0.0070  0.0445  -0.0231 9   ASN B C     
3084 O O     . ASN B 9   ? 0.7107 0.6040 0.5156 0.0080  0.0420  -0.0225 9   ASN B O     
3085 C CB    . ASN B 9   ? 0.4355 0.3091 0.2218 0.0102  0.0505  -0.0215 9   ASN B CB    
3086 C CG    . ASN B 9   ? 0.4622 0.3402 0.2590 0.0071  0.0562  -0.0186 9   ASN B CG    
3087 O OD1   . ASN B 9   ? 0.4497 0.3384 0.2604 0.0043  0.0568  -0.0185 9   ASN B OD1   
3088 N ND2   . ASN B 9   ? 0.5092 0.3783 0.2994 0.0078  0.0602  -0.0163 9   ASN B ND2   
3089 N N     . ARG B 10  ? 0.6321 0.5381 0.4546 0.0042  0.0460  -0.0227 10  ARG B N     
3090 C CA    . ARG B 10  ? 0.7087 0.6248 0.5438 0.0021  0.0453  -0.0214 10  ARG B CA    
3091 C C     . ARG B 10  ? 0.7798 0.6989 0.6242 -0.0006 0.0506  -0.0184 10  ARG B C     
3092 O O     . ARG B 10  ? 0.8219 0.7487 0.6768 -0.0024 0.0503  -0.0171 10  ARG B O     
3093 C CB    . ARG B 10  ? 0.5942 0.5211 0.4393 0.0015  0.0415  -0.0238 10  ARG B CB    
3094 C CG    . ARG B 10  ? 0.4919 0.4168 0.3300 0.0039  0.0351  -0.0273 10  ARG B CG    
3095 C CD    . ARG B 10  ? 0.5087 0.4450 0.3585 0.0031  0.0312  -0.0295 10  ARG B CD    
3096 N NE    . ARG B 10  ? 0.4649 0.4098 0.3265 0.0012  0.0325  -0.0267 10  ARG B NE    
3097 C CZ    . ARG B 10  ? 0.5340 0.4888 0.4065 0.0006  0.0297  -0.0277 10  ARG B CZ    
3098 N NH1   . ARG B 10  ? 0.5878 0.5451 0.4613 0.0018  0.0251  -0.0319 10  ARG B NH1   
3099 N NH2   . ARG B 10  ? 0.4904 0.4518 0.3729 -0.0010 0.0311  -0.0248 10  ARG B NH2   
3100 N N     . ARG B 11  ? 0.7281 0.6408 0.5686 -0.0009 0.0551  -0.0175 11  ARG B N     
3101 C CA    . ARG B 11  ? 0.6939 0.6075 0.5418 -0.0033 0.0597  -0.0152 11  ARG B CA    
3102 C C     . ARG B 11  ? 0.6745 0.5827 0.5175 -0.0027 0.0607  -0.0135 11  ARG B C     
3103 O O     . ARG B 11  ? 0.5773 0.4766 0.4074 -0.0002 0.0598  -0.0136 11  ARG B O     
3104 C CB    . ARG B 11  ? 0.6141 0.5215 0.4586 -0.0036 0.0641  -0.0149 11  ARG B CB    
3105 C CG    . ARG B 11  ? 0.5682 0.4814 0.4190 -0.0045 0.0637  -0.0164 11  ARG B CG    
3106 C CD    . ARG B 11  ? 0.6086 0.5203 0.4639 -0.0064 0.0685  -0.0155 11  ARG B CD    
3107 N NE    . ARG B 11  ? 0.6334 0.5491 0.4931 -0.0070 0.0683  -0.0169 11  ARG B NE    
3108 C CZ    . ARG B 11  ? 0.7419 0.6676 0.6152 -0.0092 0.0674  -0.0171 11  ARG B CZ    
3109 N NH1   . ARG B 11  ? 0.7303 0.6628 0.6138 -0.0110 0.0664  -0.0160 11  ARG B NH1   
3110 N NH2   . ARG B 11  ? 0.7533 0.6818 0.6297 -0.0096 0.0674  -0.0183 11  ARG B NH2   
3111 N N     . GLY B 12  ? 0.7790 0.6926 0.6325 -0.0050 0.0621  -0.0120 12  GLY B N     
3112 C CA    . GLY B 12  ? 0.6906 0.6001 0.5410 -0.0047 0.0631  -0.0105 12  GLY B CA    
3113 C C     . GLY B 12  ? 0.6957 0.6085 0.5454 -0.0037 0.0587  -0.0106 12  GLY B C     
3114 O O     . GLY B 12  ? 0.7796 0.6864 0.6224 -0.0025 0.0589  -0.0097 12  GLY B O     
3115 N N     . THR B 13  ? 0.6136 0.5354 0.4702 -0.0041 0.0548  -0.0119 13  THR B N     
3116 C CA    . THR B 13  ? 0.5283 0.4539 0.3850 -0.0032 0.0503  -0.0122 13  THR B CA    
3117 C C     . THR B 13  ? 0.5116 0.4491 0.3834 -0.0054 0.0489  -0.0116 13  THR B C     
3118 O O     . THR B 13  ? 0.4468 0.3891 0.3207 -0.0049 0.0451  -0.0120 13  THR B O     
3119 C CB    . THR B 13  ? 0.5916 0.5164 0.4416 -0.0011 0.0459  -0.0147 13  THR B CB    
3120 O OG1   . THR B 13  ? 0.6415 0.5752 0.5013 -0.0023 0.0449  -0.0161 13  THR B OG1   
3121 C CG2   . THR B 13  ? 0.6592 0.5720 0.4943 0.0013  0.0469  -0.0156 13  THR B CG2   
3122 N N     . HIS B 14  ? 0.3492 0.2910 0.2312 -0.0078 0.0518  -0.0107 14  HIS B N     
3123 C CA    . HIS B 14  ? 0.2544 0.2068 0.1510 -0.0099 0.0506  -0.0103 14  HIS B CA    
3124 C C     . HIS B 14  ? 0.2562 0.2164 0.1586 -0.0097 0.0471  -0.0115 14  HIS B C     
3125 O O     . HIS B 14  ? 0.2718 0.2405 0.1856 -0.0109 0.0454  -0.0112 14  HIS B O     
3126 C CB    . HIS B 14  ? 0.2396 0.1939 0.1390 -0.0102 0.0497  -0.0090 14  HIS B CB    
3127 C CG    . HIS B 14  ? 0.3558 0.3024 0.2501 -0.0103 0.0533  -0.0079 14  HIS B CG    
3128 N ND1   . HIS B 14  ? 0.3918 0.3367 0.2897 -0.0118 0.0568  -0.0077 14  HIS B ND1   
3129 C CD2   . HIS B 14  ? 0.3724 0.3120 0.2576 -0.0090 0.0538  -0.0072 14  HIS B CD2   
3130 C CE1   . HIS B 14  ? 0.2989 0.2364 0.1907 -0.0113 0.0596  -0.0069 14  HIS B CE1   
3131 N NE2   . HIS B 14  ? 0.3493 0.2834 0.2333 -0.0096 0.0579  -0.0064 14  HIS B NE2   
3132 N N     . SER B 15  ? 0.2434 0.2004 0.1383 -0.0080 0.0461  -0.0132 15  SER B N     
3133 C CA    . SER B 15  ? 0.3563 0.3201 0.2567 -0.0078 0.0434  -0.0148 15  SER B CA    
3134 C C     . SER B 15  ? 0.3897 0.3591 0.3020 -0.0101 0.0454  -0.0143 15  SER B C     
3135 O O     . SER B 15  ? 0.4878 0.4532 0.3989 -0.0111 0.0488  -0.0140 15  SER B O     
3136 C CB    . SER B 15  ? 0.4997 0.4579 0.3889 -0.0055 0.0419  -0.0173 15  SER B CB    
3137 O OG    . SER B 15  ? 0.5917 0.5549 0.4869 -0.0057 0.0413  -0.0189 15  SER B OG    
3138 N N     . ILE B 16  ? 0.2001 0.1781 0.1236 -0.0110 0.0431  -0.0143 16  ILE B N     
3139 C CA    . ILE B 16  ? 0.2508 0.2337 0.1855 -0.0133 0.0442  -0.0142 16  ILE B CA    
3140 C C     . ILE B 16  ? 0.3159 0.2964 0.2474 -0.0130 0.0457  -0.0156 16  ILE B C     
3141 O O     . ILE B 16  ? 0.5122 0.4926 0.4483 -0.0147 0.0479  -0.0154 16  ILE B O     
3142 C CB    . ILE B 16  ? 0.3540 0.3454 0.3002 -0.0142 0.0411  -0.0141 16  ILE B CB    
3143 C CG1   . ILE B 16  ? 0.3142 0.3078 0.2641 -0.0147 0.0399  -0.0126 16  ILE B CG1   
3144 C CG2   . ILE B 16  ? 0.3986 0.3941 0.3551 -0.0163 0.0414  -0.0145 16  ILE B CG2   
3145 C CD1   . ILE B 16  ? 0.2360 0.2369 0.1987 -0.0163 0.0375  -0.0125 16  ILE B CD1   
3146 N N     . LYS B 17  ? 0.2444 0.2225 0.1674 -0.0106 0.0440  -0.0174 17  LYS B N     
3147 C CA    . LYS B 17  ? 0.3272 0.3032 0.2472 -0.0100 0.0449  -0.0191 17  LYS B CA    
3148 C C     . LYS B 17  ? 0.3596 0.3276 0.2718 -0.0103 0.0487  -0.0187 17  LYS B C     
3149 O O     . LYS B 17  ? 0.5012 0.4690 0.4166 -0.0115 0.0511  -0.0188 17  LYS B O     
3150 C CB    . LYS B 17  ? 0.4635 0.4381 0.3752 -0.0068 0.0412  -0.0222 17  LYS B CB    
3151 C CG    . LYS B 17  ? 0.4899 0.4661 0.4039 -0.0064 0.0409  -0.0244 17  LYS B CG    
3152 C CD    . LYS B 17  ? 0.6177 0.5890 0.5200 -0.0029 0.0373  -0.0286 17  LYS B CD    
3153 C CE    . LYS B 17  ? 0.6122 0.5863 0.5187 -0.0022 0.0362  -0.0313 17  LYS B CE    
3154 N NZ    . LYS B 17  ? 0.6460 0.6199 0.5489 0.0011  0.0296  -0.0366 17  LYS B NZ    
3155 N N     . TRP B 18  ? 0.4084 0.3693 0.3102 -0.0090 0.0494  -0.0182 18  TRP B N     
3156 C CA    . TRP B 18  ? 0.2999 0.2512 0.1916 -0.0086 0.0528  -0.0179 18  TRP B CA    
3157 C C     . TRP B 18  ? 0.3684 0.3168 0.2624 -0.0103 0.0565  -0.0158 18  TRP B C     
3158 O O     . TRP B 18  ? 0.5787 0.5196 0.4664 -0.0102 0.0600  -0.0154 18  TRP B O     
3159 C CB    . TRP B 18  ? 0.3203 0.2634 0.1969 -0.0056 0.0510  -0.0193 18  TRP B CB    
3160 C CG    . TRP B 18  ? 0.5876 0.5313 0.4603 -0.0037 0.0479  -0.0224 18  TRP B CG    
3161 C CD1   . TRP B 18  ? 0.5604 0.5083 0.4335 -0.0022 0.0427  -0.0249 18  TRP B CD1   
3162 C CD2   . TRP B 18  ? 0.5239 0.4641 0.3927 -0.0032 0.0495  -0.0238 18  TRP B CD2   
3163 N NE1   . TRP B 18  ? 0.5312 0.4782 0.4009 -0.0007 0.0407  -0.0283 18  TRP B NE1   
3164 C CE2   . TRP B 18  ? 0.5315 0.4739 0.3984 -0.0013 0.0450  -0.0275 18  TRP B CE2   
3165 C CE3   . TRP B 18  ? 0.5291 0.4641 0.3959 -0.0042 0.0541  -0.0227 18  TRP B CE3   
3166 C CZ2   . TRP B 18  ? 0.4511 0.3910 0.3141 -0.0003 0.0450  -0.0300 18  TRP B CZ2   
3167 C CZ3   . TRP B 18  ? 0.5042 0.4368 0.3670 -0.0032 0.0544  -0.0248 18  TRP B CZ3   
3168 C CH2   . TRP B 18  ? 0.3887 0.3237 0.2495 -0.0013 0.0499  -0.0283 18  TRP B CH2   
3169 N N     . ASP B 19  ? 0.4555 0.4092 0.3580 -0.0117 0.0557  -0.0145 19  ASP B N     
3170 C CA    . ASP B 19  ? 0.4208 0.3713 0.3246 -0.0130 0.0586  -0.0131 19  ASP B CA    
3171 C C     . ASP B 19  ? 0.3097 0.2668 0.2269 -0.0154 0.0590  -0.0128 19  ASP B C     
3172 O O     . ASP B 19  ? 0.4012 0.3552 0.3195 -0.0164 0.0616  -0.0122 19  ASP B O     
3173 C CB    . ASP B 19  ? 0.3276 0.2765 0.2277 -0.0121 0.0574  -0.0121 19  ASP B CB    
3174 C CG    . ASP B 19  ? 0.5000 0.4395 0.3850 -0.0095 0.0576  -0.0124 19  ASP B CG    
3175 O OD1   . ASP B 19  ? 0.6053 0.5366 0.4821 -0.0088 0.0606  -0.0124 19  ASP B OD1   
3176 O OD2   . ASP B 19  ? 0.5776 0.5175 0.4584 -0.0080 0.0544  -0.0126 19  ASP B OD2   
3177 N N     . THR B 20  ? 0.2321 0.1971 0.1586 -0.0163 0.0565  -0.0135 20  THR B N     
3178 C CA    . THR B 20  ? 0.3097 0.2800 0.2477 -0.0183 0.0562  -0.0135 20  THR B CA    
3179 C C     . THR B 20  ? 0.7296 0.6962 0.6677 -0.0192 0.0595  -0.0139 20  THR B C     
3180 O O     . THR B 20  ? 0.8571 0.8241 0.8004 -0.0204 0.0604  -0.0138 20  THR B O     
3181 C CB    . THR B 20  ? 0.2939 0.2726 0.2411 -0.0188 0.0527  -0.0141 20  THR B CB    
3182 O OG1   . THR B 20  ? 0.4870 0.4685 0.4331 -0.0177 0.0499  -0.0138 20  THR B OG1   
3183 C CG2   . THR B 20  ? 0.3052 0.2888 0.2629 -0.0203 0.0515  -0.0143 20  THR B CG2   
3184 N N     . TYR B 21  ? 0.7311 0.6937 0.6631 -0.0186 0.0611  -0.0145 21  TYR B N     
3185 C CA    . TYR B 21  ? 0.5047 0.4624 0.4349 -0.0192 0.0647  -0.0148 21  TYR B CA    
3186 C C     . TYR B 21  ? 0.4728 0.4205 0.3909 -0.0179 0.0680  -0.0141 21  TYR B C     
3187 O O     . TYR B 21  ? 0.5784 0.5224 0.4871 -0.0161 0.0675  -0.0141 21  TYR B O     
3188 C CB    . TYR B 21  ? 0.4894 0.4485 0.4203 -0.0192 0.0645  -0.0159 21  TYR B CB    
3189 C CG    . TYR B 21  ? 0.4726 0.4402 0.4151 -0.0204 0.0617  -0.0167 21  TYR B CG    
3190 C CD1   . TYR B 21  ? 0.4043 0.3782 0.3510 -0.0201 0.0580  -0.0169 21  TYR B CD1   
3191 C CD2   . TYR B 21  ? 0.4361 0.4049 0.3848 -0.0218 0.0627  -0.0173 21  TYR B CD2   
3192 C CE1   . TYR B 21  ? 0.2242 0.2051 0.1810 -0.0211 0.0555  -0.0176 21  TYR B CE1   
3193 C CE2   . TYR B 21  ? 0.4773 0.4528 0.4354 -0.0226 0.0600  -0.0181 21  TYR B CE2   
3194 C CZ    . TYR B 21  ? 0.3031 0.2845 0.2652 -0.0223 0.0565  -0.0182 21  TYR B CZ    
3195 O OH    . TYR B 21  ? 0.3851 0.3724 0.3562 -0.0230 0.0539  -0.0190 21  TYR B OH    
3196 N N     . LYS B 22  ? 0.3269 0.2698 0.2445 -0.0186 0.0714  -0.0138 22  LYS B N     
3197 C CA    . LYS B 22  ? 0.4956 0.4285 0.4021 -0.0174 0.0750  -0.0130 22  LYS B CA    
3198 C C     . LYS B 22  ? 0.4914 0.4174 0.3910 -0.0168 0.0782  -0.0133 22  LYS B C     
3199 O O     . LYS B 22  ? 0.4421 0.3588 0.3304 -0.0152 0.0808  -0.0127 22  LYS B O     
3200 C CB    . LYS B 22  ? 0.5730 0.5038 0.4820 -0.0182 0.0770  -0.0123 22  LYS B CB    
3201 C CG    . LYS B 22  ? 0.5440 0.4799 0.4577 -0.0184 0.0741  -0.0118 22  LYS B CG    
3202 C CD    . LYS B 22  ? 0.5249 0.4563 0.4374 -0.0186 0.0767  -0.0111 22  LYS B CD    
3203 C CE    . LYS B 22  ? 0.6567 0.5883 0.5664 -0.0177 0.0749  -0.0102 22  LYS B CE    
3204 N NZ    . LYS B 22  ? 0.5661 0.4919 0.4729 -0.0176 0.0779  -0.0095 22  LYS B NZ    
3205 N N     . ASN B 23  ? 0.4791 0.4089 0.3846 -0.0179 0.0781  -0.0142 23  ASN B N     
3206 C CA    . ASN B 23  ? 0.6382 0.5615 0.5370 -0.0173 0.0812  -0.0146 23  ASN B CA    
3207 C C     . ASN B 23  ? 0.6692 0.5892 0.5575 -0.0150 0.0798  -0.0150 23  ASN B C     
3208 O O     . ASN B 23  ? 0.6245 0.5508 0.5159 -0.0148 0.0765  -0.0160 23  ASN B O     
3209 C CB    . ASN B 23  ? 0.6924 0.6207 0.6002 -0.0189 0.0811  -0.0155 23  ASN B CB    
3210 C CG    . ASN B 23  ? 0.6801 0.6026 0.5813 -0.0182 0.0839  -0.0160 23  ASN B CG    
3211 O OD1   . ASN B 23  ? 0.6587 0.5719 0.5502 -0.0171 0.0873  -0.0154 23  ASN B OD1   
3212 N ND2   . ASN B 23  ? 0.6260 0.5537 0.5323 -0.0188 0.0823  -0.0171 23  ASN B ND2   
3213 N N     . GLU B 24  ? 0.6526 0.5625 0.5281 -0.0131 0.0823  -0.0145 24  GLU B N     
3214 C CA    . GLU B 24  ? 0.7060 0.6114 0.5696 -0.0104 0.0805  -0.0152 24  GLU B CA    
3215 C C     . GLU B 24  ? 0.7561 0.6616 0.6174 -0.0098 0.0801  -0.0167 24  GLU B C     
3216 O O     . GLU B 24  ? 0.9068 0.8086 0.7580 -0.0073 0.0781  -0.0179 24  GLU B O     
3217 C CB    . GLU B 24  ? 0.7280 0.6214 0.5780 -0.0083 0.0832  -0.0142 24  GLU B CB    
3218 C CG    . GLU B 24  ? 0.6742 0.5666 0.5264 -0.0089 0.0842  -0.0127 24  GLU B CG    
3219 C CD    . GLU B 24  ? 0.6941 0.5748 0.5322 -0.0064 0.0862  -0.0117 24  GLU B CD    
3220 O OE1   . GLU B 24  ? 0.6841 0.5564 0.5104 -0.0042 0.0874  -0.0121 24  GLU B OE1   
3221 O OE2   . GLU B 24  ? 0.7254 0.6050 0.5640 -0.0065 0.0867  -0.0106 24  GLU B OE2   
3222 N N     . GLU B 25  ? 0.6935 0.6023 0.5630 -0.0117 0.0819  -0.0169 25  GLU B N     
3223 C CA    . GLU B 25  ? 0.6284 0.5384 0.4971 -0.0113 0.0815  -0.0184 25  GLU B CA    
3224 C C     . GLU B 25  ? 0.6065 0.5267 0.4834 -0.0117 0.0771  -0.0198 25  GLU B C     
3225 O O     . GLU B 25  ? 0.6344 0.5556 0.5093 -0.0108 0.0760  -0.0214 25  GLU B O     
3226 C CB    . GLU B 25  ? 0.5691 0.4784 0.4436 -0.0132 0.0851  -0.0180 25  GLU B CB    
3227 C CG    . GLU B 25  ? 0.6037 0.5024 0.4669 -0.0117 0.0889  -0.0179 25  GLU B CG    
3228 C CD    . GLU B 25  ? 0.7452 0.6436 0.6147 -0.0137 0.0923  -0.0177 25  GLU B CD    
3229 O OE1   . GLU B 25  ? 0.7609 0.6517 0.6227 -0.0127 0.0954  -0.0178 25  GLU B OE1   
3230 O OE2   . GLU B 25  ? 0.8008 0.7062 0.6827 -0.0160 0.0918  -0.0175 25  GLU B OE2   
3231 N N     . LEU B 26  ? 0.5867 0.5143 0.4724 -0.0129 0.0746  -0.0192 26  LEU B N     
3232 C CA    . LEU B 26  ? 0.4268 0.3643 0.3216 -0.0134 0.0708  -0.0203 26  LEU B CA    
3233 C C     . LEU B 26  ? 0.4160 0.3532 0.3028 -0.0107 0.0671  -0.0219 26  LEU B C     
3234 O O     . LEU B 26  ? 0.3760 0.3073 0.2529 -0.0089 0.0666  -0.0217 26  LEU B O     
3235 C CB    . LEU B 26  ? 0.3511 0.2961 0.2582 -0.0156 0.0693  -0.0192 26  LEU B CB    
3236 C CG    . LEU B 26  ? 0.4564 0.4029 0.3727 -0.0180 0.0716  -0.0187 26  LEU B CG    
3237 C CD1   . LEU B 26  ? 0.4922 0.4446 0.4184 -0.0195 0.0698  -0.0179 26  LEU B CD1   
3238 C CD2   . LEU B 26  ? 0.4031 0.3533 0.3254 -0.0189 0.0715  -0.0198 26  LEU B CD2   
3239 N N     . ILE B 27  ? 0.5442 0.4866 0.4343 -0.0101 0.0646  -0.0239 27  ILE B N     
3240 C CA    . ILE B 27  ? 0.4524 0.3968 0.3381 -0.0076 0.0600  -0.0263 27  ILE B CA    
3241 C C     . ILE B 27  ? 0.3603 0.3150 0.2589 -0.0090 0.0573  -0.0259 27  ILE B C     
3242 O O     . ILE B 27  ? 0.3083 0.2691 0.2187 -0.0112 0.0581  -0.0253 27  ILE B O     
3243 C CB    . ILE B 27  ? 0.4915 0.4343 0.3720 -0.0056 0.0586  -0.0295 27  ILE B CB    
3244 C CG1   . ILE B 27  ? 0.4521 0.3835 0.3170 -0.0035 0.0601  -0.0303 27  ILE B CG1   
3245 C CG2   . ILE B 27  ? 0.5801 0.5278 0.4613 -0.0035 0.0530  -0.0329 27  ILE B CG2   
3246 C CD1   . ILE B 27  ? 0.3234 0.2483 0.1779 -0.0018 0.0588  -0.0299 27  ILE B CD1   
3247 N N     . HIS B 28  ? 0.5277 0.4836 0.4240 -0.0076 0.0540  -0.0263 28  HIS B N     
3248 C CA    . HIS B 28  ? 0.5337 0.4985 0.4416 -0.0087 0.0516  -0.0255 28  HIS B CA    
3249 C C     . HIS B 28  ? 0.4897 0.4577 0.3965 -0.0061 0.0468  -0.0288 28  HIS B C     
3250 O O     . HIS B 28  ? 0.4548 0.4179 0.3505 -0.0032 0.0437  -0.0315 28  HIS B O     
3251 C CB    . HIS B 28  ? 0.5095 0.4738 0.4173 -0.0093 0.0516  -0.0233 28  HIS B CB    
3252 C CG    . HIS B 28  ? 0.4334 0.3951 0.3440 -0.0117 0.0556  -0.0209 28  HIS B CG    
3253 N ND1   . HIS B 28  ? 0.3986 0.3512 0.2988 -0.0110 0.0584  -0.0202 28  HIS B ND1   
3254 C CD2   . HIS B 28  ? 0.3873 0.3536 0.3097 -0.0145 0.0568  -0.0195 28  HIS B CD2   
3255 C CE1   . HIS B 28  ? 0.4118 0.3640 0.3176 -0.0132 0.0614  -0.0185 28  HIS B CE1   
3256 N NE2   . HIS B 28  ? 0.4132 0.3736 0.3321 -0.0152 0.0602  -0.0183 28  HIS B NE2   
3257 N N     . ALA B 29  ? 0.4386 0.4141 0.3573 -0.0073 0.0458  -0.0291 29  ALA B N     
3258 C CA    . ALA B 29  ? 0.2136 0.1921 0.1335 -0.0048 0.0412  -0.0325 29  ALA B CA    
3259 C C     . ALA B 29  ? 0.3950 0.3821 0.3302 -0.0074 0.0408  -0.0307 29  ALA B C     
3260 O O     . ALA B 29  ? 0.4166 0.4069 0.3576 -0.0069 0.0387  -0.0329 29  ALA B O     
3261 C CB    . ALA B 29  ? 0.2201 0.1959 0.1361 -0.0029 0.0402  -0.0362 29  ALA B CB    
3262 N N     . TRP B 30  ? 0.5279 0.5182 0.4701 -0.0102 0.0424  -0.0273 30  TRP B N     
3263 C CA    . TRP B 30  ? 0.3217 0.3202 0.2791 -0.0134 0.0417  -0.0258 30  TRP B CA    
3264 C C     . TRP B 30  ? 0.3947 0.3962 0.3540 -0.0125 0.0385  -0.0257 30  TRP B C     
3265 O O     . TRP B 30  ? 0.4288 0.4349 0.3950 -0.0124 0.0361  -0.0273 30  TRP B O     
3266 C CB    . TRP B 30  ? 0.1597 0.1588 0.1233 -0.0165 0.0440  -0.0233 30  TRP B CB    
3267 C CG    . TRP B 30  ? 0.1307 0.1246 0.0866 -0.0161 0.0457  -0.0216 30  TRP B CG    
3268 C CD1   . TRP B 30  ? 0.3096 0.2961 0.2530 -0.0143 0.0477  -0.0219 30  TRP B CD1   
3269 C CD2   . TRP B 30  ? 0.1081 0.1033 0.0683 -0.0175 0.0454  -0.0198 30  TRP B CD2   
3270 N NE1   . TRP B 30  ? 0.3610 0.3443 0.3013 -0.0148 0.0490  -0.0201 30  TRP B NE1   
3271 C CE2   . TRP B 30  ? 0.3010 0.2898 0.2516 -0.0166 0.0476  -0.0189 30  TRP B CE2   
3272 C CE3   . TRP B 30  ? 0.0963 0.0971 0.0670 -0.0190 0.0431  -0.0193 30  TRP B CE3   
3273 C CZ2   . TRP B 30  ? 0.2171 0.2053 0.1690 -0.0174 0.0480  -0.0174 30  TRP B CZ2   
3274 C CZ3   . TRP B 30  ? 0.2360 0.2361 0.2070 -0.0194 0.0432  -0.0179 30  TRP B CZ3   
3275 C CH2   . TRP B 30  ? 0.2326 0.2266 0.1948 -0.0187 0.0457  -0.0170 30  TRP B CH2   
3276 N N     . ILE B 31  ? 0.4488 0.4476 0.4024 -0.0118 0.0384  -0.0241 31  ILE B N     
3277 C CA    . ILE B 31  ? 0.1721 0.1737 0.1277 -0.0111 0.0355  -0.0238 31  ILE B CA    
3278 C C     . ILE B 31  ? 0.1100 0.1073 0.0557 -0.0068 0.0313  -0.0276 31  ILE B C     
3279 O O     . ILE B 31  ? 0.2198 0.2101 0.1523 -0.0035 0.0299  -0.0302 31  ILE B O     
3280 C CB    . ILE B 31  ? 0.2807 0.2799 0.2323 -0.0114 0.0365  -0.0214 31  ILE B CB    
3281 C CG1   . ILE B 31  ? 0.3637 0.3661 0.3256 -0.0150 0.0383  -0.0192 31  ILE B CG1   
3282 C CG2   . ILE B 31  ? 0.3403 0.3407 0.2909 -0.0101 0.0335  -0.0211 31  ILE B CG2   
3283 C CD1   . ILE B 31  ? 0.3657 0.3754 0.3412 -0.0171 0.0361  -0.0195 31  ILE B CD1   
3284 N N     . ALA B 32  ? 0.2320 0.2329 0.1836 -0.0068 0.0281  -0.0287 32  ALA B N     
3285 C CA    . ALA B 32  ? 0.1738 0.1696 0.1184 -0.0065 0.0235  -0.0356 32  ALA B CA    
3286 C C     . ALA B 32  ? 0.3889 0.3766 0.3197 -0.0033 0.0184  -0.0373 32  ALA B C     
3287 O O     . ALA B 32  ? 0.6097 0.5970 0.5415 -0.0043 0.0134  -0.0401 32  ALA B O     
3288 C CB    . ALA B 32  ? 0.1909 0.1977 0.1526 -0.0107 0.0224  -0.0385 32  ALA B CB    
3289 N N     . ASP B 33  ? 0.4914 0.4753 0.4119 0.0001  0.0190  -0.0360 33  ASP B N     
3290 C CA    . ASP B 33  ? 0.4434 0.4233 0.3532 0.0023  0.0142  -0.0390 33  ASP B CA    
3291 C C     . ASP B 33  ? 0.4838 0.4589 0.3843 0.0031  0.0130  -0.0431 33  ASP B C     
3292 O O     . ASP B 33  ? 0.6927 0.6679 0.5932 0.0034  0.0169  -0.0418 33  ASP B O     
3293 C CB    . ASP B 33  ? 0.4737 0.4566 0.3834 0.0022  0.0171  -0.0340 33  ASP B CB    
3294 C CG    . ASP B 33  ? 0.4566 0.4381 0.3653 0.0003  0.0241  -0.0299 33  ASP B CG    
3295 O OD1   . ASP B 33  ? 0.5057 0.4871 0.4166 -0.0004 0.0267  -0.0300 33  ASP B OD1   
3296 O OD2   . ASP B 33  ? 0.3683 0.3475 0.2737 -0.0009 0.0266  -0.0270 33  ASP B OD2   
3297 N N     . MET B 34  ? 0.5025 0.4716 0.3947 0.0024  0.0079  -0.0471 34  MET B N     
3298 C CA    . MET B 34  ? 0.5083 0.4687 0.3898 0.0028  0.0068  -0.0498 34  MET B CA    
3299 C C     . MET B 34  ? 0.5498 0.5055 0.4215 0.0038  0.0105  -0.0462 34  MET B C     
3300 O O     . MET B 34  ? 0.6963 0.6534 0.5677 0.0036  0.0117  -0.0428 34  MET B O     
3301 C CB    . MET B 34  ? 0.4193 0.3709 0.2947 0.0025  -0.0010 -0.0539 34  MET B CB    
3302 C CG    . MET B 34  ? 0.4546 0.4089 0.3398 0.0007  -0.0046 -0.0579 34  MET B CG    
3303 S SD    . MET B 34  ? 0.5308 0.4755 0.4133 0.0016  -0.0159 -0.0609 34  MET B SD    
3304 C CE    . MET B 34  ? 0.3502 0.2961 0.2337 0.0020  -0.0198 -0.0577 34  MET B CE    
3305 N N     . ASP B 35  ? 0.4399 0.3899 0.3040 0.0047  0.0122  -0.0471 35  ASP B N     
3306 C CA    . ASP B 35  ? 0.5936 0.5342 0.4450 0.0058  0.0154  -0.0440 35  ASP B CA    
3307 C C     . ASP B 35  ? 0.7541 0.6833 0.5917 0.0079  0.0103  -0.0463 35  ASP B C     
3308 O O     . ASP B 35  ? 0.8607 0.7799 0.6861 0.0097  0.0117  -0.0460 35  ASP B O     
3309 C CB    . ASP B 35  ? 0.5068 0.4454 0.3565 0.0058  0.0210  -0.0427 35  ASP B CB    
3310 C CG    . ASP B 35  ? 0.5155 0.4633 0.3779 0.0039  0.0262  -0.0391 35  ASP B CG    
3311 O OD1   . ASP B 35  ? 0.4546 0.4078 0.3240 0.0028  0.0269  -0.0363 35  ASP B OD1   
3312 O OD2   . ASP B 35  ? 0.4670 0.4158 0.3324 0.0034  0.0296  -0.0388 35  ASP B OD2   
3313 N N     . PHE B 36  ? 0.7093 0.6374 0.5471 0.0081  0.0041  -0.0480 36  PHE B N     
3314 C CA    . PHE B 36  ? 0.7124 0.6285 0.5373 0.0107  -0.0022 -0.0497 36  PHE B CA    
3315 C C     . PHE B 36  ? 0.6468 0.5607 0.4680 0.0115  -0.0036 -0.0468 36  PHE B C     
3316 O O     . PHE B 36  ? 0.5564 0.4785 0.3867 0.0095  -0.0018 -0.0446 36  PHE B O     
3317 C CB    . PHE B 36  ? 0.6985 0.6124 0.5259 0.0112  -0.0101 -0.0541 36  PHE B CB    
3318 C CG    . PHE B 36  ? 0.5775 0.4908 0.4063 0.0111  -0.0101 -0.0576 36  PHE B CG    
3319 C CD1   . PHE B 36  ? 0.6232 0.5302 0.4422 0.0127  -0.0072 -0.0579 36  PHE B CD1   
3320 C CD2   . PHE B 36  ? 0.4945 0.4132 0.3346 0.0094  -0.0130 -0.0607 36  PHE B CD2   
3321 C CE1   . PHE B 36  ? 0.6845 0.5910 0.5049 0.0126  -0.0071 -0.0612 36  PHE B CE1   
3322 C CE2   . PHE B 36  ? 0.4334 0.3515 0.2754 0.0092  -0.0129 -0.0640 36  PHE B CE2   
3323 C CZ    . PHE B 36  ? 0.5336 0.4457 0.3655 0.0108  -0.0100 -0.0643 36  PHE B CZ    
3324 N N     . GLU B 37  ? 0.7056 0.6081 0.5130 0.0145  -0.0067 -0.0469 37  GLU B N     
3325 C CA    . GLU B 37  ? 0.5938 0.4926 0.3967 0.0158  -0.0095 -0.0448 37  GLU B CA    
3326 C C     . GLU B 37  ? 0.5811 0.4832 0.3915 0.0154  -0.0163 -0.0463 37  GLU B C     
3327 O O     . GLU B 37  ? 0.5791 0.4787 0.3904 0.0164  -0.0226 -0.0497 37  GLU B O     
3328 C CB    . GLU B 37  ? 0.5678 0.4529 0.3543 0.0197  -0.0127 -0.0452 37  GLU B CB    
3329 C CG    . GLU B 37  ? 0.6915 0.5691 0.4674 0.0210  -0.0064 -0.0416 37  GLU B CG    
3330 C CD    . GLU B 37  ? 0.8334 0.6966 0.5924 0.0254  -0.0099 -0.0419 37  GLU B CD    
3331 O OE1   . GLU B 37  ? 0.8687 0.7243 0.6180 0.0268  -0.0051 -0.0391 37  GLU B OE1   
3332 O OE2   . GLU B 37  ? 0.8273 0.6868 0.5832 0.0275  -0.0174 -0.0448 37  GLU B OE2   
3333 N N     . VAL B 38  ? 0.5085 0.4162 0.3247 0.0139  -0.0152 -0.0436 38  VAL B N     
3334 C CA    . VAL B 38  ? 0.5210 0.4314 0.3440 0.0137  -0.0216 -0.0442 38  VAL B CA    
3335 C C     . VAL B 38  ? 0.5564 0.4560 0.3695 0.0176  -0.0300 -0.0459 38  VAL B C     
3336 O O     . VAL B 38  ? 0.5607 0.4508 0.3607 0.0203  -0.0295 -0.0457 38  VAL B O     
3337 C CB    . VAL B 38  ? 0.6015 0.5189 0.4304 0.0118  -0.0178 -0.0404 38  VAL B CB    
3338 C CG1   . VAL B 38  ? 0.6239 0.5426 0.4578 0.0121  -0.0245 -0.0404 38  VAL B CG1   
3339 C CG2   . VAL B 38  ? 0.5382 0.4675 0.3792 0.0084  -0.0108 -0.0392 38  VAL B CG2   
3340 N N     . PRO B 39  ? 0.5246 0.4249 0.3440 0.0183  -0.0379 -0.0479 39  PRO B N     
3341 C CA    . PRO B 39  ? 0.5072 0.3981 0.3187 0.0222  -0.0462 -0.0492 39  PRO B CA    
3342 C C     . PRO B 39  ? 0.6393 0.5250 0.4415 0.0238  -0.0449 -0.0462 39  PRO B C     
3343 O O     . PRO B 39  ? 0.7394 0.6311 0.5468 0.0218  -0.0412 -0.0432 39  PRO B O     
3344 C CB    . PRO B 39  ? 0.5153 0.4119 0.3402 0.0218  -0.0535 -0.0506 39  PRO B CB    
3345 C CG    . PRO B 39  ? 0.5222 0.4284 0.3597 0.0183  -0.0503 -0.0515 39  PRO B CG    
3346 C CD    . PRO B 39  ? 0.5754 0.4848 0.4098 0.0159  -0.0401 -0.0496 39  PRO B CD    
3347 N N     . LYS B 40  ? 0.6740 0.5483 0.4625 0.0277  -0.0479 -0.0470 40  LYS B N     
3348 C CA    . LYS B 40  ? 0.6932 0.5613 0.4718 0.0296  -0.0466 -0.0443 40  LYS B CA    
3349 C C     . LYS B 40  ? 0.6504 0.5209 0.4345 0.0298  -0.0511 -0.0430 40  LYS B C     
3350 O O     . LYS B 40  ? 0.6315 0.5032 0.4141 0.0289  -0.0468 -0.0398 40  LYS B O     
3351 C CB    . LYS B 40  ? 0.7518 0.6066 0.5146 0.0341  -0.0498 -0.0459 40  LYS B CB    
3352 C CG    . LYS B 40  ? 0.8168 0.6687 0.5750 0.0344  -0.0478 -0.0481 40  LYS B CG    
3353 C CD    . LYS B 40  ? 0.8422 0.6995 0.6023 0.0312  -0.0375 -0.0458 40  LYS B CD    
3354 C CE    . LYS B 40  ? 0.7748 0.6289 0.5278 0.0315  -0.0316 -0.0419 40  LYS B CE    
3355 N NZ    . LYS B 40  ? 0.7426 0.5966 0.4930 0.0301  -0.0228 -0.0400 40  LYS B NZ    
3356 N N     . PRO B 41  ? 0.6580 0.5298 0.4493 0.0308  -0.0594 -0.0452 41  PRO B N     
3357 C CA    . PRO B 41  ? 0.5829 0.4577 0.3805 0.0307  -0.0630 -0.0436 41  PRO B CA    
3358 C C     . PRO B 41  ? 0.6287 0.5148 0.4374 0.0265  -0.0571 -0.0406 41  PRO B C     
3359 O O     . PRO B 41  ? 0.6796 0.5675 0.4910 0.0263  -0.0580 -0.0385 41  PRO B O     
3360 C CB    . PRO B 41  ? 0.5844 0.4602 0.3908 0.0321  -0.0723 -0.0467 41  PRO B CB    
3361 C CG    . PRO B 41  ? 0.6691 0.5390 0.4696 0.0340  -0.0747 -0.0500 41  PRO B CG    
3362 C CD    . PRO B 41  ? 0.7343 0.6048 0.5293 0.0321  -0.0659 -0.0491 41  PRO B CD    
3363 N N     . ILE B 42  ? 0.7116 0.6054 0.5273 0.0232  -0.0514 -0.0405 42  ILE B N     
3364 C CA    . ILE B 42  ? 0.6613 0.5652 0.4860 0.0194  -0.0451 -0.0376 42  ILE B CA    
3365 C C     . ILE B 42  ? 0.7566 0.6581 0.5728 0.0192  -0.0377 -0.0345 42  ILE B C     
3366 O O     . ILE B 42  ? 0.8381 0.7431 0.6572 0.0180  -0.0355 -0.0317 42  ILE B O     
3367 C CB    . ILE B 42  ? 0.5179 0.4308 0.3529 0.0162  -0.0413 -0.0386 42  ILE B CB    
3368 C CG1   . ILE B 42  ? 0.5258 0.4410 0.3703 0.0165  -0.0486 -0.0417 42  ILE B CG1   
3369 C CG2   . ILE B 42  ? 0.4043 0.3279 0.2492 0.0126  -0.0353 -0.0357 42  ILE B CG2   
3370 C CD1   . ILE B 42  ? 0.3077 0.2322 0.1634 0.0132  -0.0450 -0.0427 42  ILE B CD1   
3371 N N     . GLN B 43  ? 0.5108 0.4063 0.3171 0.0202  -0.0339 -0.0349 43  GLN B N     
3372 C CA    . GLN B 43  ? 0.3821 0.2748 0.1811 0.0202  -0.0270 -0.0320 43  GLN B CA    
3373 C C     . GLN B 43  ? 0.5807 0.4644 0.3700 0.0232  -0.0301 -0.0307 43  GLN B C     
3374 O O     . GLN B 43  ? 0.4820 0.3642 0.2682 0.0230  -0.0254 -0.0276 43  GLN B O     
3375 C CB    . GLN B 43  ? 0.3505 0.2361 0.1397 0.0216  -0.0234 -0.0329 43  GLN B CB    
3376 C CG    . GLN B 43  ? 0.6716 0.5644 0.4691 0.0193  -0.0222 -0.0352 43  GLN B CG    
3377 C CD    . GLN B 43  ? 0.8736 0.7585 0.6609 0.0211  -0.0198 -0.0365 43  GLN B CD    
3378 O OE1   . GLN B 43  ? 0.8919 0.7806 0.6839 0.0199  -0.0195 -0.0388 43  GLN B OE1   
3379 N NE2   . GLN B 43  ? 0.9259 0.7995 0.6991 0.0239  -0.0180 -0.0349 43  GLN B NE2   
3380 N N     . THR B 44  ? 0.6150 0.4924 0.3998 0.0262  -0.0380 -0.0329 44  THR B N     
3381 C CA    . THR B 44  ? 0.5781 0.4472 0.3539 0.0292  -0.0411 -0.0317 44  THR B CA    
3382 C C     . THR B 44  ? 0.5645 0.4410 0.3500 0.0273  -0.0418 -0.0297 44  THR B C     
3383 O O     . THR B 44  ? 0.4980 0.3707 0.2783 0.0282  -0.0397 -0.0272 44  THR B O     
3384 C CB    . THR B 44  ? 0.5163 0.3761 0.2844 0.0334  -0.0497 -0.0348 44  THR B CB    
3385 O OG1   . THR B 44  ? 0.5545 0.4079 0.3137 0.0351  -0.0488 -0.0367 44  THR B OG1   
3386 C CG2   . THR B 44  ? 0.5701 0.4207 0.3278 0.0368  -0.0523 -0.0337 44  THR B CG2   
3387 N N     . ALA B 45  ? 0.6015 0.4875 0.4006 0.0250  -0.0445 -0.0305 45  ALA B N     
3388 C CA    . ALA B 45  ? 0.6997 0.5935 0.5088 0.0230  -0.0445 -0.0283 45  ALA B CA    
3389 C C     . ALA B 45  ? 0.7430 0.6436 0.5558 0.0198  -0.0356 -0.0251 45  ALA B C     
3390 O O     . ALA B 45  ? 0.8490 0.7512 0.6635 0.0193  -0.0343 -0.0227 45  ALA B O     
3391 C CB    . ALA B 45  ? 0.7320 0.6336 0.5549 0.0215  -0.0495 -0.0299 45  ALA B CB    
3392 N N     . LEU B 46  ? 0.5996 0.5032 0.4134 0.0180  -0.0296 -0.0251 46  LEU B N     
3393 C CA    . LEU B 46  ? 0.3596 0.2690 0.1778 0.0154  -0.0216 -0.0222 46  LEU B CA    
3394 C C     . LEU B 46  ? 0.4258 0.3258 0.2323 0.0172  -0.0177 -0.0199 46  LEU B C     
3395 O O     . LEU B 46  ? 0.5664 0.4695 0.3763 0.0158  -0.0137 -0.0172 46  LEU B O     
3396 C CB    . LEU B 46  ? 0.3510 0.2660 0.1741 0.0133  -0.0166 -0.0230 46  LEU B CB    
3397 C CG    . LEU B 46  ? 0.4604 0.3864 0.2969 0.0109  -0.0189 -0.0250 46  LEU B CG    
3398 C CD1   . LEU B 46  ? 0.3604 0.2915 0.2012 0.0089  -0.0131 -0.0255 46  LEU B CD1   
3399 C CD2   . LEU B 46  ? 0.5129 0.4484 0.3615 0.0088  -0.0201 -0.0236 46  LEU B CD2   
3400 N N     . LYS B 47  ? 0.4406 0.3287 0.2333 0.0205  -0.0188 -0.0209 47  LYS B N     
3401 C CA    . LYS B 47  ? 0.4448 0.3230 0.2260 0.0225  -0.0153 -0.0188 47  LYS B CA    
3402 C C     . LYS B 47  ? 0.6218 0.4955 0.3990 0.0246  -0.0201 -0.0182 47  LYS B C     
3403 O O     . LYS B 47  ? 0.4736 0.3428 0.2457 0.0253  -0.0168 -0.0159 47  LYS B O     
3404 C CB    . LYS B 47  ? 0.5367 0.4035 0.3042 0.0254  -0.0144 -0.0199 47  LYS B CB    
3405 C CG    . LYS B 47  ? 0.6435 0.5005 0.4003 0.0296  -0.0218 -0.0224 47  LYS B CG    
3406 C CD    . LYS B 47  ? 0.6651 0.5081 0.4053 0.0332  -0.0196 -0.0216 47  LYS B CD    
3407 C CE    . LYS B 47  ? 0.7218 0.5545 0.4508 0.0378  -0.0272 -0.0239 47  LYS B CE    
3408 N NZ    . LYS B 47  ? 0.7305 0.5501 0.4436 0.0414  -0.0251 -0.0241 47  LYS B NZ    
3409 N N     . GLN B 48  ? 0.6962 0.5707 0.4758 0.0258  -0.0278 -0.0203 48  GLN B N     
3410 C CA    . GLN B 48  ? 0.6156 0.4874 0.3939 0.0274  -0.0327 -0.0198 48  GLN B CA    
3411 C C     . GLN B 48  ? 0.6036 0.4851 0.3931 0.0243  -0.0298 -0.0172 48  GLN B C     
3412 O O     . GLN B 48  ? 0.7730 0.6511 0.5590 0.0252  -0.0296 -0.0154 48  GLN B O     
3413 C CB    . GLN B 48  ? 0.5949 0.4667 0.3760 0.0290  -0.0417 -0.0226 48  GLN B CB    
3414 C CG    . GLN B 48  ? 0.6581 0.5228 0.4333 0.0322  -0.0476 -0.0227 48  GLN B CG    
3415 C CD    . GLN B 48  ? 0.7395 0.6035 0.5179 0.0340  -0.0565 -0.0258 48  GLN B CD    
3416 O OE1   . GLN B 48  ? 0.8150 0.6882 0.6061 0.0316  -0.0585 -0.0269 48  GLN B OE1   
3417 N NE2   . GLN B 48  ? 0.7567 0.6098 0.5242 0.0383  -0.0619 -0.0272 48  GLN B NE2   
3418 N N     . ARG B 49  ? 0.4476 0.3411 0.2504 0.0206  -0.0274 -0.0170 49  ARG B N     
3419 C CA    . ARG B 49  ? 0.4942 0.3974 0.3082 0.0178  -0.0251 -0.0147 49  ARG B CA    
3420 C C     . ARG B 49  ? 0.6769 0.5789 0.4882 0.0168  -0.0174 -0.0119 49  ARG B C     
3421 O O     . ARG B 49  ? 0.5536 0.4582 0.3684 0.0160  -0.0163 -0.0099 49  ARG B O     
3422 C CB    . ARG B 49  ? 0.3547 0.2709 0.1834 0.0144  -0.0246 -0.0153 49  ARG B CB    
3423 C CG    . ARG B 49  ? 0.4224 0.3494 0.2631 0.0114  -0.0214 -0.0128 49  ARG B CG    
3424 C CD    . ARG B 49  ? 0.5171 0.4421 0.3575 0.0126  -0.0256 -0.0117 49  ARG B CD    
3425 N NE    . ARG B 49  ? 0.4994 0.4350 0.3520 0.0099  -0.0239 -0.0096 49  ARG B NE    
3426 C CZ    . ARG B 49  ? 0.3934 0.3317 0.2477 0.0085  -0.0179 -0.0072 49  ARG B CZ    
3427 N NH1   . ARG B 49  ? 0.4613 0.3924 0.3065 0.0093  -0.0131 -0.0064 49  ARG B NH1   
3428 N NH2   . ARG B 49  ? 0.3058 0.2537 0.1712 0.0064  -0.0169 -0.0054 49  ARG B NH2   
3429 N N     . ILE B 50  ? 0.7552 0.6527 0.5603 0.0170  -0.0123 -0.0118 50  ILE B N     
3430 C CA    . ILE B 50  ? 0.6974 0.5935 0.5011 0.0161  -0.0051 -0.0093 50  ILE B CA    
3431 C C     . ILE B 50  ? 0.6576 0.5433 0.4504 0.0187  -0.0055 -0.0081 50  ILE B C     
3432 O O     . ILE B 50  ? 0.5971 0.4827 0.3907 0.0178  -0.0006 -0.0059 50  ILE B O     
3433 C CB    . ILE B 50  ? 0.6895 0.5827 0.4896 0.0158  0.0000  -0.0097 50  ILE B CB    
3434 C CG1   . ILE B 50  ? 0.7503 0.6553 0.5634 0.0127  0.0017  -0.0103 50  ILE B CG1   
3435 C CG2   . ILE B 50  ? 0.5545 0.4432 0.3511 0.0155  0.0070  -0.0073 50  ILE B CG2   
3436 C CD1   . ILE B 50  ? 0.7704 0.6738 0.5818 0.0121  0.0069  -0.0105 50  ILE B CD1   
3437 N N     . LYS B 51  ? 0.7290 0.6064 0.5123 0.0221  -0.0115 -0.0096 51  LYS B N     
3438 C CA    . LYS B 51  ? 0.6810 0.5486 0.4538 0.0250  -0.0126 -0.0087 51  LYS B CA    
3439 C C     . LYS B 51  ? 0.6813 0.5546 0.4615 0.0234  -0.0126 -0.0068 51  LYS B C     
3440 O O     . LYS B 51  ? 0.6968 0.5631 0.4697 0.0252  -0.0116 -0.0055 51  LYS B O     
3441 C CB    . LYS B 51  ? 0.5822 0.4411 0.3453 0.0289  -0.0201 -0.0110 51  LYS B CB    
3442 C CG    . LYS B 51  ? 0.5811 0.4289 0.3308 0.0319  -0.0193 -0.0122 51  LYS B CG    
3443 C CD    . LYS B 51  ? 0.7197 0.5571 0.4577 0.0341  -0.0145 -0.0103 51  LYS B CD    
3444 C CE    . LYS B 51  ? 0.7253 0.5499 0.4481 0.0379  -0.0148 -0.0115 51  LYS B CE    
3445 N NZ    . LYS B 51  ? 0.6952 0.5127 0.4099 0.0419  -0.0230 -0.0138 51  LYS B NZ    
3446 N N     . HIS B 52  ? 0.6385 0.5243 0.4330 0.0203  -0.0134 -0.0066 52  HIS B N     
3447 C CA    . HIS B 52  ? 0.6060 0.4983 0.4087 0.0185  -0.0128 -0.0047 52  HIS B CA    
3448 C C     . HIS B 52  ? 0.6704 0.5707 0.4821 0.0151  -0.0055 -0.0029 52  HIS B C     
3449 O O     . HIS B 52  ? 0.6962 0.6072 0.5196 0.0124  -0.0048 -0.0031 52  HIS B O     
3450 C CB    . HIS B 52  ? 0.4613 0.3619 0.2741 0.0175  -0.0189 -0.0055 52  HIS B CB    
3451 C CG    . HIS B 52  ? 0.4956 0.4012 0.3151 0.0164  -0.0193 -0.0037 52  HIS B CG    
3452 N ND1   . HIS B 52  ? 0.5446 0.4427 0.3562 0.0183  -0.0194 -0.0026 52  HIS B ND1   
3453 C CD2   . HIS B 52  ? 0.5524 0.4696 0.3854 0.0136  -0.0193 -0.0027 52  HIS B CD2   
3454 C CE1   . HIS B 52  ? 0.4774 0.3824 0.2977 0.0166  -0.0196 -0.0010 52  HIS B CE1   
3455 N NE2   . HIS B 52  ? 0.4868 0.4034 0.3201 0.0138  -0.0195 -0.0010 52  HIS B NE2   
3456 N N     . PRO B 53  ? 0.6484 0.5437 0.4555 0.0153  -0.0003 -0.0012 53  PRO B N     
3457 C CA    . PRO B 53  ? 0.5072 0.4086 0.3222 0.0124  0.0065  0.0001  53  PRO B CA    
3458 C C     . PRO B 53  ? 0.5097 0.4228 0.3387 0.0095  0.0074  0.0015  53  PRO B C     
3459 O O     . PRO B 53  ? 0.4471 0.3616 0.2795 0.0081  0.0122  0.0030  53  PRO B O     
3460 C CB    . PRO B 53  ? 0.4418 0.3324 0.2463 0.0141  0.0108  0.0013  53  PRO B CB    
3461 C CG    . PRO B 53  ? 0.6349 0.5184 0.4310 0.0169  0.0065  0.0014  53  PRO B CG    
3462 C CD    . PRO B 53  ? 0.7276 0.6114 0.5223 0.0183  -0.0006 -0.0006 53  PRO B CD    
3463 N N     . ILE B 54  ? 0.5661 0.4876 0.4034 0.0085  0.0029  0.0009  54  ILE B N     
3464 C CA    . ILE B 54  ? 0.5391 0.4728 0.3905 0.0058  0.0038  0.0021  54  ILE B CA    
3465 C C     . ILE B 54  ? 0.4285 0.3713 0.2889 0.0044  0.0017  0.0009  54  ILE B C     
3466 O O     . ILE B 54  ? 0.3122 0.2527 0.1692 0.0057  -0.0035 -0.0007 54  ILE B O     
3467 C CB    . ILE B 54  ? 0.4349 0.3695 0.2876 0.0062  0.0003  0.0031  54  ILE B CB    
3468 C CG1   . ILE B 54  ? 0.3060 0.2322 0.1505 0.0075  0.0028  0.0043  54  ILE B CG1   
3469 C CG2   . ILE B 54  ? 0.4304 0.3779 0.2980 0.0036  0.0009  0.0043  54  ILE B CG2   
3470 C CD1   . ILE B 54  ? 0.2917 0.2172 0.1357 0.0084  -0.0011 0.0051  54  ILE B CD1   
3471 N N     . PHE B 55  ? 0.3595 0.3121 0.2315 0.0019  0.0054  0.0017  55  PHE B N     
3472 C CA    . PHE B 55  ? 0.3501 0.3117 0.2312 0.0007  0.0047  0.0007  55  PHE B CA    
3473 C C     . PHE B 55  ? 0.4040 0.3777 0.2992 -0.0010 0.0050  0.0021  55  PHE B C     
3474 O O     . PHE B 55  ? 0.2873 0.2687 0.1921 -0.0021 0.0080  0.0025  55  PHE B O     
3475 C CB    . PHE B 55  ? 0.3917 0.3527 0.2727 0.0000  0.0093  0.0001  55  PHE B CB    
3476 C CG    . PHE B 55  ? 0.4626 0.4113 0.3295 0.0019  0.0097  -0.0009 55  PHE B CG    
3477 C CD1   . PHE B 55  ? 0.6268 0.5702 0.4860 0.0038  0.0050  -0.0029 55  PHE B CD1   
3478 C CD2   . PHE B 55  ? 0.4413 0.3834 0.3029 0.0020  0.0147  -0.0001 55  PHE B CD2   
3479 C CE1   . PHE B 55  ? 0.5677 0.4995 0.4138 0.0060  0.0053  -0.0038 55  PHE B CE1   
3480 C CE2   . PHE B 55  ? 0.5013 0.4319 0.3499 0.0041  0.0154  -0.0008 55  PHE B CE2   
3481 C CZ    . PHE B 55  ? 0.5973 0.5227 0.4378 0.0062  0.0108  -0.0027 55  PHE B CZ    
3482 N N     . GLY B 56  ? 0.3934 0.3682 0.2899 -0.0006 0.0019  0.0030  56  GLY B N     
3483 C CA    . GLY B 56  ? 0.3878 0.3732 0.2968 -0.0015 0.0018  0.0045  56  GLY B CA    
3484 C C     . GLY B 56  ? 0.3441 0.3365 0.2605 -0.0010 -0.0018 0.0035  56  GLY B C     
3485 O O     . GLY B 56  ? 0.3982 0.3889 0.3114 -0.0009 -0.0036 0.0016  56  GLY B O     
3486 N N     . TYR B 57  ? 0.3591 0.3578 0.2848 -0.0002 -0.0029 0.0047  57  TYR B N     
3487 C CA    . TYR B 57  ? 0.3157 0.3173 0.2488 0.0011  -0.0062 0.0036  57  TYR B CA    
3488 C C     . TYR B 57  ? 0.2895 0.2915 0.2188 0.0003  -0.0131 0.0020  57  TYR B C     
3489 O O     . TYR B 57  ? 0.3248 0.3208 0.2477 0.0000  -0.0159 0.0024  57  TYR B O     
3490 C CB    . TYR B 57  ? 0.2778 0.2781 0.2185 0.0002  -0.0064 0.0050  57  TYR B CB    
3491 C CG    . TYR B 57  ? 0.2465 0.2498 0.1954 -0.0041 -0.0003 0.0064  57  TYR B CG    
3492 C CD1   . TYR B 57  ? 0.2895 0.2911 0.2364 -0.0037 0.0029  0.0075  57  TYR B CD1   
3493 C CD2   . TYR B 57  ? 0.1176 0.1298 0.0794 -0.0078 0.0015  0.0061  57  TYR B CD2   
3494 C CE1   . TYR B 57  ? 0.3859 0.3924 0.3421 -0.0067 0.0066  0.0077  57  TYR B CE1   
3495 C CE2   . TYR B 57  ? 0.1704 0.1893 0.1421 -0.0102 0.0045  0.0062  57  TYR B CE2   
3496 C CZ    . TYR B 57  ? 0.3059 0.3210 0.2742 -0.0095 0.0067  0.0068  57  TYR B CZ    
3497 O OH    . TYR B 57  ? 0.3708 0.3907 0.3469 -0.0108 0.0079  0.0063  57  TYR B OH    
3498 N N     . THR B 58  ? 0.1265 0.1310 0.0595 0.0002  -0.0158 0.0000  58  THR B N     
3499 C CA    . THR B 58  ? 0.1181 0.1179 0.0473 -0.0006 -0.0224 -0.0018 58  THR B CA    
3500 C C     . THR B 58  ? 0.0940 0.1015 0.0364 -0.0010 -0.0264 -0.0024 58  THR B C     
3501 O O     . THR B 58  ? 0.0805 0.0943 0.0334 0.0001  -0.0234 -0.0026 58  THR B O     
3502 C CB    . THR B 58  ? 0.3217 0.3146 0.2414 -0.0004 -0.0219 -0.0041 58  THR B CB    
3503 O OG1   . THR B 58  ? 0.4329 0.4182 0.3416 0.0003  -0.0177 -0.0033 58  THR B OG1   
3504 C CG2   . THR B 58  ? 0.3853 0.3709 0.3009 0.0009  -0.0289 -0.0064 58  THR B CG2   
3505 N N     . LEU B 59  ? 0.3237 0.3265 0.2670 -0.0005 -0.0328 -0.0029 59  LEU B N     
3506 C CA    . LEU B 59  ? 0.3601 0.3671 0.3159 -0.0007 -0.0371 -0.0036 59  LEU B CA    
3507 C C     . LEU B 59  ? 0.2463 0.2492 0.2001 -0.0004 -0.0404 -0.0064 59  LEU B C     
3508 O O     . LEU B 59  ? 0.1145 0.1092 0.0556 0.0006  -0.0409 -0.0081 59  LEU B O     
3509 C CB    . LEU B 59  ? 0.4561 0.4589 0.4143 0.0007  -0.0420 -0.0030 59  LEU B CB    
3510 C CG    . LEU B 59  ? 0.2776 0.2835 0.2396 0.0007  -0.0402 -0.0005 59  LEU B CG    
3511 C CD1   . LEU B 59  ? 0.2820 0.2782 0.2331 0.0023  -0.0432 -0.0004 59  LEU B CD1   
3512 C CD2   . LEU B 59  ? 0.2833 0.2948 0.2602 0.0003  -0.0411 0.0004  59  LEU B CD2   
3513 N N     . PRO B 60  ? 0.3050 0.3130 0.2713 -0.0010 -0.0423 -0.0070 60  PRO B N     
3514 C CA    . PRO B 60  ? 0.1106 0.1136 0.0765 0.0001  -0.0470 -0.0098 60  PRO B CA    
3515 C C     . PRO B 60  ? 0.2129 0.2061 0.1735 0.0030  -0.0535 -0.0112 60  PRO B C     
3516 O O     . PRO B 60  ? 0.3165 0.3099 0.2830 0.0037  -0.0556 -0.0100 60  PRO B O     
3517 C CB    . PRO B 60  ? 0.1612 0.1718 0.1437 -0.0009 -0.0467 -0.0094 60  PRO B CB    
3518 C CG    . PRO B 60  ? 0.3061 0.3261 0.2952 -0.0028 -0.0406 -0.0066 60  PRO B CG    
3519 C CD    . PRO B 60  ? 0.4384 0.4567 0.4195 -0.0024 -0.0392 -0.0051 60  PRO B CD    
3520 N N     . PRO B 61  ? 0.1305 0.1152 0.0811 0.0049  -0.0569 -0.0140 61  PRO B N     
3521 C CA    . PRO B 61  ? 0.3239 0.2988 0.2680 0.0079  -0.0631 -0.0154 61  PRO B CA    
3522 C C     . PRO B 61  ? 0.2626 0.2384 0.2193 0.0090  -0.0682 -0.0158 61  PRO B C     
3523 O O     . PRO B 61  ? 0.2821 0.2647 0.2522 0.0077  -0.0673 -0.0156 61  PRO B O     
3524 C CB    . PRO B 61  ? 0.3819 0.3486 0.3148 0.0097  -0.0655 -0.0186 61  PRO B CB    
3525 C CG    . PRO B 61  ? 0.1961 0.1649 0.1237 0.0079  -0.0595 -0.0182 61  PRO B CG    
3526 C CD    . PRO B 61  ? 0.1364 0.1177 0.0790 0.0048  -0.0557 -0.0162 61  PRO B CD    
3527 N N     . GLU B 62  ? 0.2331 0.2019 0.1857 0.0112  -0.0728 -0.0162 62  GLU B N     
3528 C CA    . GLU B 62  ? 0.3942 0.3628 0.3582 0.0122  -0.0775 -0.0167 62  GLU B CA    
3529 C C     . GLU B 62  ? 0.3063 0.2732 0.2763 0.0134  -0.0817 -0.0197 62  GLU B C     
3530 O O     . GLU B 62  ? 0.4058 0.3763 0.3895 0.0130  -0.0827 -0.0197 62  GLU B O     
3531 C CB    . GLU B 62  ? 0.4672 0.4276 0.4240 0.0146  -0.0821 -0.0171 62  GLU B CB    
3532 C CG    . GLU B 62  ? 0.4799 0.4428 0.4350 0.0133  -0.0784 -0.0140 62  GLU B CG    
3533 C CD    . GLU B 62  ? 0.4337 0.3886 0.3828 0.0156  -0.0831 -0.0144 62  GLU B CD    
3534 O OE1   . GLU B 62  ? 0.3626 0.3088 0.3039 0.0185  -0.0885 -0.0171 62  GLU B OE1   
3535 O OE2   . GLU B 62  ? 0.2955 0.2530 0.2473 0.0146  -0.0812 -0.0121 62  GLU B OE2   
3536 N N     . ASN B 63  ? 0.4052 0.3662 0.3648 0.0150  -0.0838 -0.0222 63  ASN B N     
3537 C CA    . ASN B 63  ? 0.5011 0.4586 0.4635 0.0168  -0.0888 -0.0255 63  ASN B CA    
3538 C C     . ASN B 63  ? 0.4059 0.3702 0.3758 0.0148  -0.0854 -0.0259 63  ASN B C     
3539 O O     . ASN B 63  ? 0.5380 0.5007 0.5132 0.0160  -0.0891 -0.0285 63  ASN B O     
3540 C CB    . ASN B 63  ? 0.6253 0.5725 0.5711 0.0195  -0.0922 -0.0279 63  ASN B CB    
3541 C CG    . ASN B 63  ? 0.6818 0.6280 0.6139 0.0184  -0.0867 -0.0264 63  ASN B CG    
3542 O OD1   . ASN B 63  ? 0.8125 0.7638 0.7447 0.0162  -0.0816 -0.0259 63  ASN B OD1   
3543 N ND2   . ASN B 63  ? 0.6556 0.5949 0.5762 0.0201  -0.0875 -0.0257 63  ASN B ND2   
3544 N N     . ILE B 64  ? 0.2568 0.2285 0.2274 0.0119  -0.0786 -0.0236 64  ILE B N     
3545 C CA    . ILE B 64  ? 0.3111 0.2883 0.2852 0.0100  -0.0749 -0.0242 64  ILE B CA    
3546 C C     . ILE B 64  ? 0.4331 0.4147 0.4236 0.0100  -0.0762 -0.0248 64  ILE B C     
3547 O O     . ILE B 64  ? 0.3622 0.3457 0.3557 0.0095  -0.0756 -0.0265 64  ILE B O     
3548 C CB    . ILE B 64  ? 0.2517 0.2362 0.2242 0.0069  -0.0673 -0.0213 64  ILE B CB    
3549 C CG1   . ILE B 64  ? 0.1441 0.1312 0.1159 0.0055  -0.0643 -0.0227 64  ILE B CG1   
3550 C CG2   . ILE B 64  ? 0.1185 0.1109 0.1037 0.0054  -0.0642 -0.0182 64  ILE B CG2   
3551 C CD1   . ILE B 64  ? 0.1466 0.1234 0.1033 0.0077  -0.0672 -0.0260 64  ILE B CD1   
3552 N N     . GLY B 65  ? 0.5962 0.5789 0.5973 0.0104  -0.0777 -0.0236 65  GLY B N     
3553 C CA    . GLY B 65  ? 0.4472 0.4327 0.4633 0.0105  -0.0784 -0.0242 65  GLY B CA    
3554 C C     . GLY B 65  ? 0.3574 0.3364 0.3745 0.0132  -0.0851 -0.0279 65  GLY B C     
3555 O O     . GLY B 65  ? 0.4415 0.4225 0.4672 0.0132  -0.0850 -0.0292 65  GLY B O     
3556 N N     . ASP B 66  ? 0.3357 0.3064 0.3442 0.0157  -0.0910 -0.0297 66  ASP B N     
3557 C CA    . ASP B 66  ? 0.3268 0.2908 0.3352 0.0185  -0.0978 -0.0334 66  ASP B CA    
3558 C C     . ASP B 66  ? 0.4621 0.4254 0.4631 0.0186  -0.0974 -0.0356 66  ASP B C     
3559 O O     . ASP B 66  ? 0.4979 0.4609 0.5055 0.0195  -0.0999 -0.0380 66  ASP B O     
3560 C CB    . ASP B 66  ? 0.4003 0.3553 0.3994 0.0213  -0.1040 -0.0348 66  ASP B CB    
3561 C CG    . ASP B 66  ? 0.4359 0.3906 0.4417 0.0213  -0.1051 -0.0331 66  ASP B CG    
3562 O OD1   . ASP B 66  ? 0.4779 0.4368 0.4980 0.0202  -0.1037 -0.0322 66  ASP B OD1   
3563 O OD2   . ASP B 66  ? 0.3362 0.2860 0.3326 0.0224  -0.1072 -0.0327 66  ASP B OD2   
3564 N N     . ILE B 67  ? 0.6300 0.5926 0.6173 0.0176  -0.0941 -0.0348 67  ILE B N     
3565 C CA    . ILE B 67  ? 0.5264 0.4865 0.5042 0.0177  -0.0936 -0.0370 67  ILE B CA    
3566 C C     . ILE B 67  ? 0.3673 0.3349 0.3562 0.0156  -0.0901 -0.0372 67  ILE B C     
3567 O O     . ILE B 67  ? 0.3102 0.2750 0.3000 0.0170  -0.0932 -0.0403 67  ILE B O     
3568 C CB    . ILE B 67  ? 0.3971 0.3541 0.3589 0.0171  -0.0900 -0.0360 67  ILE B CB    
3569 C CG1   . ILE B 67  ? 0.2827 0.2301 0.2314 0.0198  -0.0940 -0.0364 67  ILE B CG1   
3570 C CG2   . ILE B 67  ? 0.4964 0.4506 0.4494 0.0170  -0.0884 -0.0382 67  ILE B CG2   
3571 C CD1   . ILE B 67  ? 0.3117 0.2560 0.2459 0.0193  -0.0898 -0.0348 67  ILE B CD1   
3572 N N     . ILE B 68  ? 0.2867 0.2635 0.2849 0.0127  -0.0840 -0.0340 68  ILE B N     
3573 C CA    . ILE B 68  ? 0.2850 0.2690 0.2938 0.0109  -0.0800 -0.0338 68  ILE B CA    
3574 C C     . ILE B 68  ? 0.3794 0.3630 0.4025 0.0126  -0.0837 -0.0353 68  ILE B C     
3575 O O     . ILE B 68  ? 0.5518 0.5369 0.5800 0.0126  -0.0837 -0.0372 68  ILE B O     
3576 C CB    . ILE B 68  ? 0.3308 0.3236 0.3451 0.0079  -0.0727 -0.0300 68  ILE B CB    
3577 C CG1   . ILE B 68  ? 0.2830 0.2755 0.2832 0.0063  -0.0692 -0.0289 68  ILE B CG1   
3578 C CG2   . ILE B 68  ? 0.3152 0.3150 0.3405 0.0063  -0.0683 -0.0297 68  ILE B CG2   
3579 C CD1   . ILE B 68  ? 0.2578 0.2589 0.2627 0.0034  -0.0623 -0.0249 68  ILE B CD1   
3580 N N     . CYS B 69  ? 0.4954 0.4766 0.5249 0.0141  -0.0870 -0.0348 69  CYS B N     
3581 C CA    . CYS B 69  ? 0.3803 0.3599 0.4229 0.0158  -0.0905 -0.0364 69  CYS B CA    
3582 C C     . CYS B 69  ? 0.3251 0.2982 0.3637 0.0184  -0.0972 -0.0405 69  CYS B C     
3583 O O     . CYS B 69  ? 0.3452 0.3187 0.3931 0.0192  -0.0987 -0.0425 69  CYS B O     
3584 C CB    . CYS B 69  ? 0.2174 0.1941 0.2656 0.0167  -0.0931 -0.0354 69  CYS B CB    
3585 S SG    . CYS B 69  ? 0.2975 0.2804 0.3571 0.0143  -0.0867 -0.0313 69  CYS B SG    
3586 N N     . ASN B 70  ? 0.3114 0.2781 0.3353 0.0198  -0.1009 -0.0419 70  ASN B N     
3587 C CA    . ASN B 70  ? 0.4546 0.4143 0.4719 0.0225  -0.1070 -0.0459 70  ASN B CA    
3588 C C     . ASN B 70  ? 0.5964 0.5589 0.6113 0.0211  -0.1040 -0.0472 70  ASN B C     
3589 O O     . ASN B 70  ? 0.7027 0.6640 0.7234 0.0224  -0.1071 -0.0500 70  ASN B O     
3590 C CB    . ASN B 70  ? 0.4690 0.4204 0.4693 0.0243  -0.1106 -0.0467 70  ASN B CB    
3591 C CG    . ASN B 70  ? 0.6509 0.5972 0.6537 0.0267  -0.1162 -0.0470 70  ASN B CG    
3592 O OD1   . ASN B 70  ? 0.7257 0.6735 0.7428 0.0272  -0.1182 -0.0472 70  ASN B OD1   
3593 N ND2   . ASN B 70  ? 0.6224 0.5619 0.6111 0.0283  -0.1187 -0.0470 70  ASN B ND2   
3594 N N     . TRP B 71  ? 0.5348 0.5008 0.5425 0.0187  -0.0982 -0.0454 71  TRP B N     
3595 C CA    . TRP B 71  ? 0.3552 0.3217 0.3588 0.0179  -0.0960 -0.0473 71  TRP B CA    
3596 C C     . TRP B 71  ? 0.2957 0.2695 0.3155 0.0167  -0.0936 -0.0473 71  TRP B C     
3597 O O     . TRP B 71  ? 0.4236 0.3951 0.4443 0.0179  -0.0963 -0.0505 71  TRP B O     
3598 C CB    . TRP B 71  ? 0.4537 0.4229 0.4481 0.0154  -0.0897 -0.0451 71  TRP B CB    
3599 C CG    . TRP B 71  ? 0.3266 0.2961 0.3154 0.0141  -0.0865 -0.0469 71  TRP B CG    
3600 C CD1   . TRP B 71  ? 0.3563 0.3343 0.3549 0.0115  -0.0811 -0.0459 71  TRP B CD1   
3601 C CD2   . TRP B 71  ? 0.2241 0.1845 0.1952 0.0156  -0.0878 -0.0498 71  TRP B CD2   
3602 N NE1   . TRP B 71  ? 0.4595 0.4345 0.4483 0.0110  -0.0792 -0.0483 71  TRP B NE1   
3603 C CE2   . TRP B 71  ? 0.4238 0.3878 0.3952 0.0134  -0.0829 -0.0506 71  TRP B CE2   
3604 C CE3   . TRP B 71  ? 0.3444 0.2937 0.2992 0.0186  -0.0921 -0.0515 71  TRP B CE3   
3605 C CZ2   . TRP B 71  ? 0.5525 0.5090 0.5082 0.0140  -0.0818 -0.0532 71  TRP B CZ2   
3606 C CZ3   . TRP B 71  ? 0.4187 0.3607 0.3579 0.0193  -0.0908 -0.0538 71  TRP B CZ3   
3607 C CH2   . TRP B 71  ? 0.5011 0.4466 0.4407 0.0170  -0.0855 -0.0546 71  TRP B CH2   
3608 N N     . LYS B 73  ? 0.5486 0.5252 0.6032 0.0194  -0.0982 -0.0476 73  LYS B N     
3609 C CA    . LYS B 73  ? 0.6361 0.6079 0.6986 0.0222  -0.1046 -0.0507 73  LYS B CA    
3610 C C     . LYS B 73  ? 0.6949 0.6610 0.7472 0.0241  -0.1100 -0.0546 73  LYS B C     
3611 O O     . LYS B 73  ? 0.7240 0.6892 0.7833 0.0255  -0.1128 -0.0573 73  LYS B O     
3612 C CB    . LYS B 73  ? 0.6509 0.6181 0.7169 0.0240  -0.1091 -0.0504 73  LYS B CB    
3613 C CG    . LYS B 73  ? 0.5457 0.5087 0.6230 0.0267  -0.1150 -0.0534 73  LYS B CG    
3614 C CD    . LYS B 73  ? 0.4752 0.4297 0.5448 0.0298  -0.1234 -0.0561 73  LYS B CD    
3615 C CE    . LYS B 73  ? 0.4817 0.4321 0.5410 0.0315  -0.1276 -0.0596 73  LYS B CE    
3616 N NZ    . LYS B 73  ? 0.5442 0.4858 0.5926 0.0346  -0.1350 -0.0618 73  LYS B NZ    
3617 N N     . GLN B 74  ? 0.6555 0.6175 0.6907 0.0240  -0.1107 -0.0548 74  GLN B N     
3618 C CA    . GLN B 74  ? 0.5785 0.5326 0.6024 0.0266  -0.1163 -0.0590 74  GLN B CA    
3619 C C     . GLN B 74  ? 0.5296 0.4867 0.5542 0.0254  -0.1132 -0.0605 74  GLN B C     
3620 O O     . GLN B 74  ? 0.4536 0.4067 0.4776 0.0273  -0.1176 -0.0642 74  GLN B O     
3621 C CB    . GLN B 74  ? 0.5667 0.5135 0.5713 0.0277  -0.1179 -0.0591 74  GLN B CB    
3622 C CG    . GLN B 74  ? 0.6827 0.6209 0.6713 0.0298  -0.1210 -0.0627 74  GLN B CG    
3623 C CD    . GLN B 74  ? 0.6325 0.5640 0.6009 0.0302  -0.1197 -0.0618 74  GLN B CD    
3624 O OE1   . GLN B 74  ? 0.6776 0.6122 0.6442 0.0283  -0.1154 -0.0585 74  GLN B OE1   
3625 N NE2   . GLN B 74  ? 0.6046 0.5265 0.5577 0.0328  -0.1230 -0.0648 74  GLN B NE2   
3626 N N     . GLN B 75  ? 0.5775 0.5420 0.6041 0.0220  -0.1057 -0.0578 75  GLN B N     
3627 C CA    . GLN B 75  ? 0.6469 0.6144 0.6732 0.0205  -0.1020 -0.0591 75  GLN B CA    
3628 C C     . GLN B 75  ? 0.5550 0.5298 0.5996 0.0196  -0.0994 -0.0587 75  GLN B C     
3629 O O     . GLN B 75  ? 0.3944 0.3693 0.4405 0.0197  -0.0995 -0.0613 75  GLN B O     
3630 C CB    . GLN B 75  ? 0.5582 0.5292 0.5764 0.0174  -0.0950 -0.0566 75  GLN B CB    
3631 C CG    . GLN B 75  ? 0.4617 0.4247 0.4599 0.0183  -0.0962 -0.0569 75  GLN B CG    
3632 C CD    . GLN B 75  ? 0.5201 0.4731 0.5039 0.0207  -0.1004 -0.0610 75  GLN B CD    
3633 O OE1   . GLN B 75  ? 0.5788 0.5320 0.5648 0.0206  -0.1003 -0.0635 75  GLN B OE1   
3634 N NE2   . GLN B 75  ? 0.4750 0.4188 0.4434 0.0230  -0.1038 -0.0615 75  GLN B NE2   
3635 N N     . TYR B 76  ? 0.5194 0.4997 0.5770 0.0186  -0.0965 -0.0555 76  TYR B N     
3636 C CA    . TYR B 76  ? 0.4239 0.4101 0.4977 0.0180  -0.0927 -0.0546 76  TYR B CA    
3637 C C     . TYR B 76  ? 0.4016 0.3853 0.4888 0.0205  -0.0967 -0.0551 76  TYR B C     
3638 O O     . TYR B 76  ? 0.3395 0.3260 0.4402 0.0204  -0.0939 -0.0548 76  TYR B O     
3639 C CB    . TYR B 76  ? 0.3742 0.3681 0.4517 0.0150  -0.0841 -0.0506 76  TYR B CB    
3640 C CG    . TYR B 76  ? 0.4244 0.4197 0.4879 0.0126  -0.0806 -0.0497 76  TYR B CG    
3641 C CD1   . TYR B 76  ? 0.3988 0.3934 0.4569 0.0122  -0.0802 -0.0525 76  TYR B CD1   
3642 C CD2   . TYR B 76  ? 0.3625 0.3585 0.4189 0.0113  -0.0786 -0.0468 76  TYR B CD2   
3643 C CE1   . TYR B 76  ? 0.5037 0.4976 0.5489 0.0105  -0.0776 -0.0526 76  TYR B CE1   
3644 C CE2   . TYR B 76  ? 0.3290 0.3246 0.3732 0.0099  -0.0762 -0.0469 76  TYR B CE2   
3645 C CZ    . TYR B 76  ? 0.4795 0.4737 0.5178 0.0094  -0.0756 -0.0498 76  TYR B CZ    
3646 O OH    . TYR B 76  ? 0.5414 0.5340 0.5661 0.0078  -0.0726 -0.0500 76  TYR B OH    
3647 N N     . ASP B 77  ? 0.5322 0.5099 0.6160 0.0226  -0.1028 -0.0560 77  ASP B N     
3648 C CA    . ASP B 77  ? 0.5929 0.5675 0.6888 0.0246  -0.1065 -0.0565 77  ASP B CA    
3649 C C     . ASP B 77  ? 0.6632 0.6420 0.7702 0.0228  -0.1003 -0.0530 77  ASP B C     
3650 O O     . ASP B 77  ? 0.6786 0.6568 0.7987 0.0234  -0.1000 -0.0534 77  ASP B O     
3651 C CB    . ASP B 77  ? 0.6363 0.6082 0.7408 0.0269  -0.1112 -0.0603 77  ASP B CB    
3652 C CG    . ASP B 77  ? 0.5715 0.5382 0.6858 0.0294  -0.1168 -0.0616 77  ASP B CG    
3653 O OD1   . ASP B 77  ? 0.5595 0.5204 0.6670 0.0315  -0.1233 -0.0633 77  ASP B OD1   
3654 O OD2   . ASP B 77  ? 0.5363 0.5042 0.6647 0.0291  -0.1144 -0.0610 77  ASP B OD2   
3655 N N     . TRP B 78  ? 0.6131 0.5952 0.7137 0.0206  -0.0955 -0.0496 78  TRP B N     
3656 C CA    . TRP B 78  ? 0.4652 0.4511 0.5732 0.0186  -0.0892 -0.0460 78  TRP B CA    
3657 C C     . TRP B 78  ? 0.5298 0.5130 0.6344 0.0187  -0.0910 -0.0441 78  TRP B C     
3658 O O     . TRP B 78  ? 0.6280 0.6119 0.7210 0.0180  -0.0907 -0.0430 78  TRP B O     
3659 C CB    . TRP B 78  ? 0.2849 0.2777 0.3887 0.0159  -0.0815 -0.0435 78  TRP B CB    
3660 C CG    . TRP B 78  ? 0.2342 0.2304 0.3440 0.0139  -0.0747 -0.0398 78  TRP B CG    
3661 C CD1   . TRP B 78  ? 0.2951 0.2888 0.4153 0.0141  -0.0741 -0.0388 78  TRP B CD1   
3662 C CD2   . TRP B 78  ? 0.0951 0.0972 0.2002 0.0114  -0.0676 -0.0367 78  TRP B CD2   
3663 N NE1   . TRP B 78  ? 0.2278 0.2252 0.3492 0.0118  -0.0671 -0.0351 78  TRP B NE1   
3664 C CE2   . TRP B 78  ? 0.0884 0.0911 0.2008 0.0103  -0.0630 -0.0338 78  TRP B CE2   
3665 C CE3   . TRP B 78  ? 0.0920 0.0985 0.1871 0.0099  -0.0647 -0.0361 78  TRP B CE3   
3666 C CZ2   . TRP B 78  ? 0.1224 0.1298 0.2321 0.0081  -0.0559 -0.0305 78  TRP B CZ2   
3667 C CZ3   . TRP B 78  ? 0.0820 0.0937 0.1756 0.0076  -0.0576 -0.0329 78  TRP B CZ3   
3668 C CH2   . TRP B 78  ? 0.0758 0.0880 0.1764 0.0069  -0.0533 -0.0301 78  TRP B CH2   
3669 N N     . ASP B 79  ? 0.3634 0.3430 0.4776 0.0195  -0.0930 -0.0440 79  ASP B N     
3670 C CA    . ASP B 79  ? 0.3974 0.3743 0.5093 0.0195  -0.0948 -0.0424 79  ASP B CA    
3671 C C     . ASP B 79  ? 0.5172 0.4988 0.6297 0.0167  -0.0874 -0.0381 79  ASP B C     
3672 O O     . ASP B 79  ? 0.6464 0.6289 0.7683 0.0155  -0.0834 -0.0365 79  ASP B O     
3673 C CB    . ASP B 79  ? 0.2184 0.1893 0.3402 0.0213  -0.1002 -0.0441 79  ASP B CB    
3674 C CG    . ASP B 79  ? 0.3338 0.3002 0.4568 0.0242  -0.1072 -0.0485 79  ASP B CG    
3675 O OD1   . ASP B 79  ? 0.4500 0.4158 0.5836 0.0248  -0.1075 -0.0501 79  ASP B OD1   
3676 O OD2   . ASP B 79  ? 0.3556 0.3189 0.4684 0.0259  -0.1124 -0.0504 79  ASP B OD2   
3677 N N     . ILE B 80  ? 0.2047 0.1886 0.3067 0.0156  -0.0856 -0.0361 80  ILE B N     
3678 C CA    . ILE B 80  ? 0.2965 0.2847 0.3980 0.0132  -0.0791 -0.0321 80  ILE B CA    
3679 C C     . ILE B 80  ? 0.4163 0.4014 0.5145 0.0134  -0.0817 -0.0308 80  ILE B C     
3680 O O     . ILE B 80  ? 0.4536 0.4334 0.5489 0.0154  -0.0883 -0.0331 80  ILE B O     
3681 C CB    . ILE B 80  ? 0.3017 0.2962 0.3945 0.0114  -0.0736 -0.0305 80  ILE B CB    
3682 C CG1   . ILE B 80  ? 0.1924 0.1854 0.2722 0.0122  -0.0774 -0.0320 80  ILE B CG1   
3683 C CG2   . ILE B 80  ? 0.5098 0.5076 0.6070 0.0109  -0.0702 -0.0313 80  ILE B CG2   
3684 C CD1   . ILE B 80  ? 0.1436 0.1420 0.2140 0.0100  -0.0722 -0.0298 80  ILE B CD1   
3685 N N     . GLN B 81  ? 0.2946 0.2826 0.3936 0.0114  -0.0765 -0.0272 81  GLN B N     
3686 C CA    . GLN B 81  ? 0.3724 0.3586 0.4679 0.0112  -0.0777 -0.0255 81  GLN B CA    
3687 C C     . GLN B 81  ? 0.4674 0.4585 0.5521 0.0098  -0.0737 -0.0234 81  GLN B C     
3688 O O     . GLN B 81  ? 0.2872 0.2835 0.3697 0.0085  -0.0688 -0.0225 81  GLN B O     
3689 C CB    . GLN B 81  ? 0.4238 0.4091 0.5282 0.0100  -0.0751 -0.0229 81  GLN B CB    
3690 C CG    . GLN B 81  ? 0.4010 0.3827 0.5172 0.0106  -0.0768 -0.0244 81  GLN B CG    
3691 C CD    . GLN B 81  ? 0.5509 0.5261 0.6703 0.0128  -0.0846 -0.0275 81  GLN B CD    
3692 O OE1   . GLN B 81  ? 0.6434 0.6163 0.7562 0.0138  -0.0886 -0.0281 81  GLN B OE1   
3693 N NE2   . GLN B 81  ? 0.7512 0.7231 0.8805 0.0138  -0.0870 -0.0295 81  GLN B NE2   
3694 N N     . LYS B 82  ? 0.5803 0.5693 0.6582 0.0101  -0.0761 -0.0227 82  LYS B N     
3695 C CA    . LYS B 82  ? 0.4367 0.4295 0.5039 0.0089  -0.0729 -0.0209 82  LYS B CA    
3696 C C     . LYS B 82  ? 0.3709 0.3700 0.4407 0.0064  -0.0652 -0.0172 82  LYS B C     
3697 O O     . LYS B 82  ? 0.4439 0.4479 0.5070 0.0051  -0.0610 -0.0158 82  LYS B O     
3698 C CB    . LYS B 82  ? 0.4876 0.4761 0.5476 0.0098  -0.0771 -0.0209 82  LYS B CB    
3699 C CG    . LYS B 82  ? 0.4744 0.4573 0.5244 0.0121  -0.0833 -0.0240 82  LYS B CG    
3700 C CD    . LYS B 82  ? 0.5263 0.5035 0.5710 0.0134  -0.0878 -0.0241 82  LYS B CD    
3701 C CE    . LYS B 82  ? 0.4588 0.4329 0.5144 0.0139  -0.0907 -0.0242 82  LYS B CE    
3702 N NZ    . LYS B 82  ? 0.5373 0.5045 0.5874 0.0159  -0.0968 -0.0255 82  LYS B NZ    
3703 N N     . GLU B 83  ? 0.3370 0.3354 0.4161 0.0059  -0.0633 -0.0156 83  GLU B N     
3704 C CA    . GLU B 83  ? 0.4434 0.4458 0.5242 0.0039  -0.0566 -0.0120 83  GLU B CA    
3705 C C     . GLU B 83  ? 0.6004 0.6078 0.6819 0.0029  -0.0511 -0.0114 83  GLU B C     
3706 O O     . GLU B 83  ? 0.6180 0.6288 0.6987 0.0015  -0.0453 -0.0085 83  GLU B O     
3707 C CB    . GLU B 83  ? 0.5083 0.5068 0.5981 0.0037  -0.0569 -0.0107 83  GLU B CB    
3708 C CG    . GLU B 83  ? 0.5581 0.5516 0.6483 0.0045  -0.0622 -0.0112 83  GLU B CG    
3709 C CD    . GLU B 83  ? 0.6760 0.6645 0.7663 0.0068  -0.0698 -0.0151 83  GLU B CD    
3710 O OE1   . GLU B 83  ? 0.7246 0.7100 0.8228 0.0077  -0.0723 -0.0170 83  GLU B OE1   
3711 O OE2   . GLU B 83  ? 0.8489 0.8361 0.9308 0.0077  -0.0733 -0.0162 83  GLU B OE2   
3712 N N     . TRP B 84  ? 0.5727 0.5800 0.6554 0.0037  -0.0528 -0.0140 84  TRP B N     
3713 C CA    . TRP B 84  ? 0.3697 0.3810 0.4539 0.0028  -0.0477 -0.0136 84  TRP B CA    
3714 C C     . TRP B 84  ? 0.2078 0.2248 0.2832 0.0018  -0.0446 -0.0132 84  TRP B C     
3715 O O     . TRP B 84  ? 0.0830 0.1041 0.1582 0.0006  -0.0389 -0.0117 84  TRP B O     
3716 C CB    . TRP B 84  ? 0.2310 0.2397 0.3214 0.0041  -0.0508 -0.0166 84  TRP B CB    
3717 C CG    . TRP B 84  ? 0.1759 0.1789 0.2756 0.0050  -0.0539 -0.0171 84  TRP B CG    
3718 C CD1   . TRP B 84  ? 0.1393 0.1396 0.2423 0.0046  -0.0539 -0.0150 84  TRP B CD1   
3719 C CD2   . TRP B 84  ? 0.1495 0.1488 0.2568 0.0064  -0.0576 -0.0199 84  TRP B CD2   
3720 N NE1   . TRP B 84  ? 0.2016 0.1967 0.3139 0.0055  -0.0572 -0.0162 84  TRP B NE1   
3721 C CE2   . TRP B 84  ? 0.2056 0.1999 0.3208 0.0067  -0.0596 -0.0194 84  TRP B CE2   
3722 C CE3   . TRP B 84  ? 0.0863 0.0859 0.1946 0.0074  -0.0594 -0.0230 84  TRP B CE3   
3723 C CZ2   . TRP B 84  ? 0.3056 0.2954 0.4300 0.0079  -0.0633 -0.0217 84  TRP B CZ2   
3724 C CZ3   . TRP B 84  ? 0.1817 0.1768 0.2990 0.0088  -0.0631 -0.0253 84  TRP B CZ3   
3725 C CH2   . TRP B 84  ? 0.3005 0.2907 0.4258 0.0090  -0.0650 -0.0247 84  TRP B CH2   
3726 N N     . ILE B 85  ? 0.2674 0.2840 0.3348 0.0021  -0.0480 -0.0143 85  ILE B N     
3727 C CA    . ILE B 85  ? 0.2384 0.2592 0.2972 0.0010  -0.0459 -0.0145 85  ILE B CA    
3728 C C     . ILE B 85  ? 0.2146 0.2406 0.2701 -0.0008 -0.0398 -0.0112 85  ILE B C     
3729 O O     . ILE B 85  ? 0.2060 0.2313 0.2599 -0.0009 -0.0399 -0.0095 85  ILE B O     
3730 C CB    . ILE B 85  ? 0.2725 0.2891 0.3218 0.0020  -0.0517 -0.0167 85  ILE B CB    
3731 C CG1   . ILE B 85  ? 0.0828 0.0940 0.1346 0.0041  -0.0578 -0.0202 85  ILE B CG1   
3732 C CG2   . ILE B 85  ? 0.3708 0.3906 0.4095 0.0004  -0.0493 -0.0165 85  ILE B CG2   
3733 C CD1   . ILE B 85  ? 0.1858 0.1908 0.2273 0.0057  -0.0640 -0.0225 85  ILE B CD1   
3734 N N     . VAL B 86  ? 0.2951 0.3260 0.3497 -0.0022 -0.0346 -0.0103 86  VAL B N     
3735 C CA    . VAL B 86  ? 0.3666 0.4027 0.4172 -0.0038 -0.0288 -0.0075 86  VAL B CA    
3736 C C     . VAL B 86  ? 0.3014 0.3407 0.3442 -0.0055 -0.0279 -0.0079 86  VAL B C     
3737 O O     . VAL B 86  ? 0.3928 0.4311 0.4349 -0.0056 -0.0297 -0.0101 86  VAL B O     
3738 C CB    . VAL B 86  ? 0.2833 0.3207 0.3383 -0.0041 -0.0233 -0.0056 86  VAL B CB    
3739 C CG1   . VAL B 86  ? 0.1251 0.1657 0.1752 -0.0050 -0.0187 -0.0030 86  VAL B CG1   
3740 C CG2   . VAL B 86  ? 0.4229 0.4550 0.4858 -0.0028 -0.0252 -0.0055 86  VAL B CG2   
3741 N N     . PHE B 87  ? 0.2400 0.2821 0.2765 -0.0070 -0.0255 -0.0059 87  PHE B N     
3742 C CA    . PHE B 87  ? 0.0370 0.0785 0.0651 -0.0094 -0.0253 -0.0052 87  PHE B CA    
3743 C C     . PHE B 87  ? 0.0298 0.0686 0.0618 -0.0094 -0.0202 -0.0028 87  PHE B C     
3744 O O     . PHE B 87  ? 0.0243 0.0627 0.0611 -0.0081 -0.0159 -0.0012 87  PHE B O     
3745 C CB    . PHE B 87  ? 0.0416 0.0797 0.0602 -0.0098 -0.0267 -0.0046 87  PHE B CB    
3746 C CG    . PHE B 87  ? 0.0530 0.0873 0.0658 -0.0078 -0.0333 -0.0085 87  PHE B CG    
3747 C CD1   . PHE B 87  ? 0.1949 0.2225 0.1957 -0.0077 -0.0364 -0.0117 87  PHE B CD1   
3748 C CD2   . PHE B 87  ? 0.0557 0.0876 0.0740 -0.0053 -0.0364 -0.0087 87  PHE B CD2   
3749 C CE1   . PHE B 87  ? 0.1749 0.1942 0.1696 -0.0048 -0.0425 -0.0145 87  PHE B CE1   
3750 C CE2   . PHE B 87  ? 0.1781 0.2023 0.1913 -0.0032 -0.0428 -0.0111 87  PHE B CE2   
3751 C CZ    . PHE B 87  ? 0.1563 0.1746 0.1577 -0.0029 -0.0457 -0.0138 87  PHE B CZ    
3752 N N     . SER B 88  ? 0.1988 0.2368 0.2278 -0.0097 -0.0201 -0.0058 88  SER B N     
3753 C CA    . SER B 88  ? 0.0657 0.1069 0.0947 -0.0093 -0.0120 -0.0070 88  SER B CA    
3754 C C     . SER B 88  ? 0.1658 0.2097 0.1836 -0.0110 -0.0108 -0.0112 88  SER B C     
3755 O O     . SER B 88  ? 0.2554 0.2954 0.2646 -0.0111 -0.0172 -0.0153 88  SER B O     
3756 C CB    . SER B 88  ? 0.0648 0.1075 0.1001 -0.0090 -0.0104 -0.0067 88  SER B CB    
3757 O OG    . SER B 88  ? 0.2978 0.3411 0.3303 -0.0087 -0.0036 -0.0066 88  SER B OG    
3758 N N     . ALA B 89  ? 0.0906 0.1387 0.1031 -0.0124 -0.0025 -0.0105 89  ALA B N     
3759 C CA    . ALA B 89  ? 0.0292 0.0835 0.0296 -0.0166 0.0015  -0.0144 89  ALA B CA    
3760 C C     . ALA B 89  ? 0.3053 0.3614 0.3064 -0.0178 0.0040  -0.0179 89  ALA B C     
3761 O O     . ALA B 89  ? 0.4026 0.4483 0.3938 -0.0171 0.0082  -0.0165 89  ALA B O     
3762 C CB    . ALA B 89  ? 0.0264 0.0738 0.0238 -0.0161 0.0045  -0.0104 89  ALA B CB    
3763 N N     . GLY B 90  ? 0.3598 0.4124 0.3720 -0.0146 0.0013  -0.0167 90  GLY B N     
3764 C CA    . GLY B 90  ? 0.3639 0.4174 0.3777 -0.0151 0.0033  -0.0195 90  GLY B CA    
3765 C C     . GLY B 90  ? 0.3476 0.3940 0.3721 -0.0114 0.0011  -0.0145 90  GLY B C     
3766 O O     . GLY B 90  ? 0.5121 0.5571 0.5400 -0.0101 0.0008  -0.0116 90  GLY B O     
3767 N N     . ILE B 91  ? 0.2925 0.3403 0.3200 -0.0117 0.0009  -0.0173 91  ILE B N     
3768 C CA    . ILE B 91  ? 0.2624 0.3084 0.2979 -0.0100 -0.0003 -0.0151 91  ILE B CA    
3769 C C     . ILE B 91  ? 0.3985 0.4426 0.4316 -0.0096 0.0041  -0.0133 91  ILE B C     
3770 O O     . ILE B 91  ? 0.4197 0.4629 0.4577 -0.0086 0.0034  -0.0111 91  ILE B O     
3771 C CB    . ILE B 91  ? 0.2314 0.2779 0.2707 -0.0102 -0.0027 -0.0179 91  ILE B CB    
3772 C CG1   . ILE B 91  ? 0.3844 0.4315 0.4220 -0.0110 -0.0102 -0.0241 91  ILE B CG1   
3773 C CG2   . ILE B 91  ? 0.2094 0.2556 0.2563 -0.0089 -0.0036 -0.0170 91  ILE B CG2   
3774 C CD1   . ILE B 91  ? 0.2627 0.3059 0.3030 -0.0099 -0.0172 -0.0211 91  ILE B CD1   
3775 N N     . VAL B 92  ? 0.4054 0.4479 0.4306 -0.0107 0.0073  -0.0141 92  VAL B N     
3776 C CA    . VAL B 92  ? 0.0219 0.0619 0.0458 -0.0103 0.0088  -0.0125 92  VAL B CA    
3777 C C     . VAL B 92  ? 0.0201 0.0591 0.0444 -0.0093 0.0080  -0.0095 92  VAL B C     
3778 O O     . VAL B 92  ? 0.3412 0.3792 0.3695 -0.0083 0.0079  -0.0076 92  VAL B O     
3779 C CB    . VAL B 92  ? 0.2121 0.2504 0.2296 -0.0119 0.0107  -0.0138 92  VAL B CB    
3780 C CG1   . VAL B 92  ? 0.1849 0.2214 0.2038 -0.0114 0.0117  -0.0128 92  VAL B CG1   
3781 C CG2   . VAL B 92  ? 0.2067 0.2459 0.2230 -0.0132 0.0117  -0.0165 92  VAL B CG2   
3782 N N     . PRO B 93  ? 0.1555 0.1947 0.1763 -0.0096 0.0073  -0.0090 93  PRO B N     
3783 C CA    . PRO B 93  ? 0.1654 0.2036 0.1878 -0.0085 0.0064  -0.0062 93  PRO B CA    
3784 C C     . PRO B 93  ? 0.2288 0.2675 0.2598 -0.0074 0.0048  -0.0043 93  PRO B C     
3785 O O     . PRO B 93  ? 0.2520 0.2893 0.2859 -0.0064 0.0047  -0.0018 93  PRO B O     
3786 C CB    . PRO B 93  ? 0.2545 0.2933 0.2713 -0.0092 0.0058  -0.0064 93  PRO B CB    
3787 C CG    . PRO B 93  ? 0.0207 0.0598 0.0321 -0.0109 0.0069  -0.0087 93  PRO B CG    
3788 C CD    . PRO B 93  ? 0.2593 0.2993 0.2740 -0.0111 0.0075  -0.0105 93  PRO B CD    
3789 N N     . ALA B 94  ? 0.1784 0.2192 0.2140 -0.0076 0.0029  -0.0053 94  ALA B N     
3790 C CA    . ALA B 94  ? 0.1037 0.1459 0.1466 -0.0071 0.0001  -0.0035 94  ALA B CA    
3791 C C     . ALA B 94  ? 0.1824 0.2243 0.2276 -0.0066 0.0012  -0.0036 94  ALA B C     
3792 O O     . ALA B 94  ? 0.1557 0.1974 0.2040 -0.0061 0.0004  -0.0032 94  ALA B O     
3793 C CB    . ALA B 94  ? 0.1189 0.1631 0.1652 -0.0075 -0.0035 -0.0057 94  ALA B CB    
3794 N N     . LEU B 95  ? 0.1518 0.1929 0.1953 -0.0069 0.0032  -0.0054 95  LEU B N     
3795 C CA    . LEU B 95  ? 0.1107 0.1508 0.1562 -0.0064 0.0043  -0.0053 95  LEU B CA    
3796 C C     . LEU B 95  ? 0.1054 0.1444 0.1482 -0.0059 0.0053  -0.0026 95  LEU B C     
3797 O O     . LEU B 95  ? 0.1319 0.1697 0.1773 -0.0054 0.0052  -0.0024 95  LEU B O     
3798 C CB    . LEU B 95  ? 0.0327 0.0723 0.0766 -0.0069 0.0061  -0.0077 95  LEU B CB    
3799 C CG    . LEU B 95  ? 0.0968 0.1379 0.1412 -0.0076 0.0054  -0.0110 95  LEU B CG    
3800 C CD1   . LEU B 95  ? 0.0419 0.0823 0.0815 -0.0086 0.0079  -0.0133 95  LEU B CD1   
3801 C CD2   . LEU B 95  ? 0.2844 0.3262 0.3363 -0.0070 0.0030  -0.0125 95  LEU B CD2   
3802 N N     . SER B 96  ? 0.0867 0.1244 0.1248 -0.0060 0.0063  -0.0015 96  SER B N     
3803 C CA    . SER B 96  ? 0.0172 0.0538 0.0533 -0.0053 0.0067  0.0011  96  SER B CA    
3804 C C     . SER B 96  ? 0.1414 0.1790 0.1763 -0.0051 0.0051  0.0019  96  SER B C     
3805 O O     . SER B 96  ? 0.1476 0.1845 0.1836 -0.0049 0.0055  0.0007  96  SER B O     
3806 C CB    . SER B 96  ? 0.1436 0.1775 0.1749 -0.0055 0.0080  -0.0002 96  SER B CB    
3807 O OG    . SER B 96  ? 0.3454 0.3770 0.3760 -0.0047 0.0083  0.0014  96  SER B OG    
3808 N N     . THR B 97  ? 0.1612 0.1987 0.1966 -0.0051 0.0040  0.0027  97  THR B N     
3809 C CA    . THR B 97  ? 0.0145 0.0532 0.0502 -0.0053 0.0031  0.0003  97  THR B CA    
3810 C C     . THR B 97  ? 0.0155 0.0520 0.0592 -0.0046 0.0024  0.0007  97  THR B C     
3811 O O     . THR B 97  ? 0.0161 0.0485 0.0617 -0.0037 0.0022  0.0023  97  THR B O     
3812 C CB    . THR B 97  ? 0.2741 0.3142 0.3085 -0.0057 0.0017  0.0007  97  THR B CB    
3813 O OG1   . THR B 97  ? 0.1918 0.2257 0.2288 -0.0052 0.0031  0.0010  97  THR B OG1   
3814 C CG2   . THR B 97  ? 0.2447 0.2829 0.2817 -0.0053 0.0012  -0.0007 97  THR B CG2   
3815 N N     . SER B 98  ? 0.0713 0.1082 0.1193 -0.0047 0.0018  -0.0005 98  SER B N     
3816 C CA    . SER B 98  ? 0.0191 0.0519 0.0744 -0.0038 0.0009  -0.0007 98  SER B CA    
3817 C C     . SER B 98  ? 0.1114 0.1411 0.1668 -0.0033 0.0026  0.0006  98  SER B C     
3818 O O     . SER B 98  ? 0.2500 0.2754 0.3099 -0.0025 0.0022  0.0022  98  SER B O     
3819 C CB    . SER B 98  ? 0.0207 0.0545 0.0806 -0.0040 -0.0002 -0.0032 98  SER B CB    
3820 O OG    . SER B 98  ? 0.0212 0.0575 0.0812 -0.0044 -0.0024 -0.0043 98  SER B OG    
3821 N N     . ILE B 99  ? 0.1655 0.1969 0.2162 -0.0037 0.0042  0.0002  99  ILE B N     
3822 C CA    . ILE B 99  ? 0.0183 0.0469 0.0688 -0.0031 0.0055  0.0014  99  ILE B CA    
3823 C C     . ILE B 99  ? 0.0178 0.0437 0.0665 -0.0024 0.0054  0.0039  99  ILE B C     
3824 O O     . ILE B 99  ? 0.1245 0.1464 0.1763 -0.0016 0.0055  0.0059  99  ILE B O     
3825 C CB    . ILE B 99  ? 0.0175 0.0486 0.0635 -0.0037 0.0068  0.0004  99  ILE B CB    
3826 C CG1   . ILE B 99  ? 0.1514 0.1830 0.2006 -0.0040 0.0072  -0.0015 99  ILE B CG1   
3827 C CG2   . ILE B 99  ? 0.0175 0.0461 0.0620 -0.0031 0.0078  0.0017  99  ILE B CG2   
3828 C CD1   . ILE B 99  ? 0.3595 0.3937 0.4046 -0.0049 0.0081  -0.0025 99  ILE B CD1   
3829 N N     . GLN B 100 ? 0.1688 0.1965 0.2126 -0.0027 0.0051  0.0040  100 GLN B N     
3830 C CA    . GLN B 100 ? 0.1911 0.2160 0.2329 -0.0019 0.0049  0.0065  100 GLN B CA    
3831 C C     . GLN B 100 ? 0.2976 0.3192 0.3436 -0.0014 0.0038  0.0087  100 GLN B C     
3832 O O     . GLN B 100 ? 0.0175 0.0355 0.0636 -0.0005 0.0038  0.0116  100 GLN B O     
3833 C CB    . GLN B 100 ? 0.1723 0.1993 0.2081 -0.0024 0.0049  0.0057  100 GLN B CB    
3834 C CG    . GLN B 100 ? 0.0773 0.1065 0.1095 -0.0032 0.0060  0.0035  100 GLN B CG    
3835 C CD    . GLN B 100 ? 0.0861 0.1151 0.1145 -0.0035 0.0060  0.0027  100 GLN B CD    
3836 O OE1   . GLN B 100 ? 0.0507 0.0802 0.0795 -0.0042 0.0064  0.0009  100 GLN B OE1   
3837 N NE2   . GLN B 100 ? 0.1646 0.1914 0.1901 -0.0026 0.0053  0.0053  100 GLN B NE2   
3838 N N     . ALA B 101 ? 0.1429 0.1657 0.1926 -0.0018 0.0028  0.0075  101 ALA B N     
3839 C CA    . ALA B 101 ? 0.1532 0.1728 0.2076 -0.0014 0.0014  0.0092  101 ALA B CA    
3840 C C     . ALA B 101 ? 0.0248 0.0399 0.0858 -0.0009 0.0014  0.0106  101 ALA B C     
3841 O O     . ALA B 101 ? 0.2225 0.2337 0.2853 -0.0004 0.0012  0.0134  101 ALA B O     
3842 C CB    . ALA B 101 ? 0.0197 0.0418 0.0768 -0.0020 -0.0002 0.0072  101 ALA B CB    
3843 N N     . PHE B 102 ? 0.0771 0.0926 0.1415 -0.0010 0.0017  0.0088  102 PHE B N     
3844 C CA    . PHE B 102 ? 0.2148 0.2262 0.2870 -0.0006 0.0013  0.0094  102 PHE B CA    
3845 C C     . PHE B 102 ? 0.2128 0.2220 0.2852 -0.0001 0.0029  0.0106  102 PHE B C     
3846 O O     . PHE B 102 ? 0.1648 0.1703 0.2436 0.0001  0.0028  0.0114  102 PHE B O     
3847 C CB    . PHE B 102 ? 0.2017 0.2145 0.2793 -0.0010 -0.0002 0.0062  102 PHE B CB    
3848 C CG    . PHE B 102 ? 0.0463 0.0615 0.1240 -0.0013 -0.0023 0.0047  102 PHE B CG    
3849 C CD1   . PHE B 102 ? 0.0270 0.0400 0.1061 -0.0012 -0.0036 0.0065  102 PHE B CD1   
3850 C CD2   . PHE B 102 ? 0.0388 0.0581 0.1153 -0.0018 -0.0030 0.0017  102 PHE B CD2   
3851 C CE1   . PHE B 102 ? 0.0274 0.0424 0.1068 -0.0015 -0.0058 0.0051  102 PHE B CE1   
3852 C CE2   . PHE B 102 ? 0.0497 0.0711 0.1264 -0.0020 -0.0053 0.0005  102 PHE B CE2   
3853 C CZ    . PHE B 102 ? 0.0272 0.0464 0.1053 -0.0018 -0.0067 0.0021  102 PHE B CZ    
3854 N N     . THR B 103 ? 0.1552 0.1662 0.2212 0.0000  0.0043  0.0110  103 THR B N     
3855 C CA    . THR B 103 ? 0.2411 0.2497 0.3072 0.0005  0.0056  0.0125  103 THR B CA    
3856 C C     . THR B 103 ? 0.1153 0.1236 0.1755 0.0011  0.0060  0.0148  103 THR B C     
3857 O O     . THR B 103 ? 0.1723 0.1832 0.2271 0.0009  0.0057  0.0143  103 THR B O     
3858 C CB    . THR B 103 ? 0.2956 0.3067 0.3610 0.0002  0.0066  0.0099  103 THR B CB    
3859 O OG1   . THR B 103 ? 0.1756 0.1910 0.2342 -0.0003 0.0069  0.0083  103 THR B OG1   
3860 C CG2   . THR B 103 ? 0.4534 0.4650 0.5246 -0.0003 0.0059  0.0074  103 THR B CG2   
3861 N N     . LYS B 104 ? 0.1070 0.1123 0.1682 0.0018  0.0068  0.0172  104 LYS B N     
3862 C CA    . LYS B 104 ? 0.0724 0.0778 0.1278 0.0024  0.0070  0.0190  104 LYS B CA    
3863 C C     . LYS B 104 ? 0.3018 0.3093 0.3538 0.0024  0.0078  0.0176  104 LYS B C     
3864 O O     . LYS B 104 ? 0.4075 0.4166 0.4614 0.0018  0.0084  0.0152  104 LYS B O     
3865 C CB    . LYS B 104 ? 0.0332 0.0379 0.0877 0.0025  0.0069  0.0197  104 LYS B CB    
3866 C CG    . LYS B 104 ? 0.1864 0.1904 0.2431 0.0022  0.0060  0.0199  104 LYS B CG    
3867 C CD    . LYS B 104 ? 0.2799 0.2847 0.3343 0.0020  0.0052  0.0199  104 LYS B CD    
3868 C CE    . LYS B 104 ? 0.3657 0.3698 0.4218 0.0017  0.0044  0.0202  104 LYS B CE    
3869 N NZ    . LYS B 104 ? 0.3765 0.3795 0.4397 0.0014  0.0041  0.0197  104 LYS B NZ    
3870 N N     . GLU B 105 ? 0.0850 0.0932 0.1321 0.0028  0.0077  0.0186  105 GLU B N     
3871 C CA    . GLU B 105 ? 0.2926 0.3029 0.3367 0.0027  0.0083  0.0170  105 GLU B CA    
3872 C C     . GLU B 105 ? 0.3971 0.4053 0.4450 0.0031  0.0093  0.0179  105 GLU B C     
3873 O O     . GLU B 105 ? 0.0225 0.0281 0.0732 0.0035  0.0093  0.0198  105 GLU B O     
3874 C CB    . GLU B 105 ? 0.3835 0.3944 0.4224 0.0032  0.0078  0.0182  105 GLU B CB    
3875 C CG    . GLU B 105 ? 0.0169 0.0314 0.0514 0.0023  0.0073  0.0156  105 GLU B CG    
3876 C CD    . GLU B 105 ? 0.1145 0.1299 0.1449 0.0026  0.0070  0.0159  105 GLU B CD    
3877 O OE1   . GLU B 105 ? 0.2369 0.2550 0.2643 0.0018  0.0069  0.0135  105 GLU B OE1   
3878 O OE2   . GLU B 105 ? 0.0855 0.0987 0.1158 0.0036  0.0069  0.0185  105 GLU B OE2   
3879 N N     . ASN B 106 ? 0.3247 0.3350 0.3722 0.0025  0.0100  0.0154  106 ASN B N     
3880 C CA    . ASN B 106 ? 0.2604 0.2692 0.3112 0.0028  0.0110  0.0158  106 ASN B CA    
3881 C C     . ASN B 106 ? 0.1801 0.1862 0.2372 0.0028  0.0114  0.0162  106 ASN B C     
3882 O O     . ASN B 106 ? 0.1203 0.1241 0.1809 0.0033  0.0122  0.0174  106 ASN B O     
3883 C CB    . ASN B 106 ? 0.2954 0.3020 0.3452 0.0039  0.0112  0.0189  106 ASN B CB    
3884 C CG    . ASN B 106 ? 0.4195 0.4284 0.4637 0.0040  0.0107  0.0185  106 ASN B CG    
3885 O OD1   . ASN B 106 ? 0.3861 0.3946 0.4276 0.0044  0.0099  0.0200  106 ASN B OD1   
3886 N ND2   . ASN B 106 ? 0.4399 0.4511 0.4826 0.0035  0.0113  0.0164  106 ASN B ND2   
3887 N N     . GLU B 107 ? 0.0654 0.0717 0.1247 0.0024  0.0107  0.0153  107 GLU B N     
3888 C CA    . GLU B 107 ? 0.1568 0.1613 0.2226 0.0021  0.0108  0.0146  107 GLU B CA    
3889 C C     . GLU B 107 ? 0.2191 0.2268 0.2850 0.0012  0.0111  0.0109  107 GLU B C     
3890 O O     . GLU B 107 ? 0.1051 0.1166 0.1660 0.0006  0.0111  0.0090  107 GLU B O     
3891 C CB    . GLU B 107 ? 0.1829 0.1861 0.2517 0.0020  0.0096  0.0153  107 GLU B CB    
3892 C CG    . GLU B 107 ? 0.0726 0.0748 0.1403 0.0024  0.0091  0.0175  107 GLU B CG    
3893 C CD    . GLU B 107 ? 0.1612 0.1633 0.2305 0.0020  0.0078  0.0176  107 GLU B CD    
3894 O OE1   . GLU B 107 ? 0.1030 0.1048 0.1717 0.0021  0.0074  0.0188  107 GLU B OE1   
3895 O OE2   . GLU B 107 ? 0.1334 0.1357 0.2048 0.0017  0.0072  0.0164  107 GLU B OE2   
3896 N N     . SER B 108 ? 0.1548 0.1609 0.2266 0.0011  0.0114  0.0100  108 SER B N     
3897 C CA    . SER B 108 ? 0.1777 0.1863 0.2498 0.0004  0.0120  0.0069  108 SER B CA    
3898 C C     . SER B 108 ? 0.2556 0.2663 0.3292 -0.0003 0.0110  0.0043  108 SER B C     
3899 O O     . SER B 108 ? 0.0445 0.0537 0.1219 -0.0001 0.0098  0.0049  108 SER B O     
3900 C CB    . SER B 108 ? 0.0375 0.0433 0.1150 0.0007  0.0130  0.0071  108 SER B CB    
3901 O OG    . SER B 108 ? 0.0301 0.0332 0.1071 0.0015  0.0137  0.0101  108 SER B OG    
3902 N N     . VAL B 109 ? 0.2628 0.2772 0.3331 -0.0011 0.0113  0.0016  109 VAL B N     
3903 C CA    . VAL B 109 ? 0.1672 0.1843 0.2385 -0.0018 0.0104  -0.0011 109 VAL B CA    
3904 C C     . VAL B 109 ? 0.1372 0.1550 0.2105 -0.0022 0.0113  -0.0036 109 VAL B C     
3905 O O     . VAL B 109 ? 0.0273 0.0459 0.0970 -0.0025 0.0126  -0.0038 109 VAL B O     
3906 C CB    . VAL B 109 ? 0.0244 0.0454 0.0889 -0.0024 0.0101  -0.0016 109 VAL B CB    
3907 C CG1   . VAL B 109 ? 0.0244 0.0480 0.0902 -0.0030 0.0090  -0.0039 109 VAL B CG1   
3908 C CG2   . VAL B 109 ? 0.0233 0.0434 0.0849 -0.0019 0.0097  0.0010  109 VAL B CG2   
3909 N N     . LEU B 110 ? 0.1968 0.2143 0.2759 -0.0023 0.0103  -0.0056 110 LEU B N     
3910 C CA    . LEU B 110 ? 0.1396 0.1570 0.2222 -0.0026 0.0108  -0.0081 110 LEU B CA    
3911 C C     . LEU B 110 ? 0.0752 0.0964 0.1559 -0.0034 0.0103  -0.0111 110 LEU B C     
3912 O O     . LEU B 110 ? 0.1405 0.1632 0.2218 -0.0034 0.0086  -0.0119 110 LEU B O     
3913 C CB    . LEU B 110 ? 0.0328 0.0465 0.1247 -0.0020 0.0099  -0.0083 110 LEU B CB    
3914 C CG    . LEU B 110 ? 0.0892 0.1020 0.1864 -0.0022 0.0102  -0.0108 110 LEU B CG    
3915 C CD1   . LEU B 110 ? 0.0774 0.0854 0.1819 -0.0016 0.0105  -0.0094 110 LEU B CD1   
3916 C CD2   . LEU B 110 ? 0.0951 0.1098 0.1960 -0.0023 0.0082  -0.0143 110 LEU B CD2   
3917 N N     . VAL B 111 ? 0.0304 0.0526 0.1092 -0.0040 0.0117  -0.0128 111 VAL B N     
3918 C CA    . VAL B 111 ? 0.0304 0.0556 0.1075 -0.0048 0.0115  -0.0158 111 VAL B CA    
3919 C C     . VAL B 111 ? 0.1976 0.2218 0.2792 -0.0049 0.0122  -0.0181 111 VAL B C     
3920 O O     . VAL B 111 ? 0.1923 0.2137 0.2769 -0.0046 0.0132  -0.0172 111 VAL B O     
3921 C CB    . VAL B 111 ? 0.1349 0.1626 0.2034 -0.0057 0.0128  -0.0155 111 VAL B CB    
3922 C CG1   . VAL B 111 ? 0.0270 0.0560 0.0912 -0.0056 0.0120  -0.0132 111 VAL B CG1   
3923 C CG2   . VAL B 111 ? 0.0293 0.0559 0.0947 -0.0060 0.0148  -0.0148 111 VAL B CG2   
3924 N N     . GLN B 112 ? 0.2026 0.2289 0.2846 -0.0054 0.0116  -0.0212 112 GLN B N     
3925 C CA    . GLN B 112 ? 0.0346 0.0603 0.1211 -0.0055 0.0120  -0.0239 112 GLN B CA    
3926 C C     . GLN B 112 ? 0.0344 0.0624 0.1149 -0.0067 0.0135  -0.0258 112 GLN B C     
3927 O O     . GLN B 112 ? 0.0991 0.1295 0.1791 -0.0070 0.0124  -0.0282 112 GLN B O     
3928 C CB    . GLN B 112 ? 0.2963 0.3217 0.3908 -0.0046 0.0091  -0.0264 112 GLN B CB    
3929 C CG    . GLN B 112 ? 0.2577 0.2808 0.3576 -0.0036 0.0069  -0.0246 112 GLN B CG    
3930 C CD    . GLN B 112 ? 0.3765 0.4006 0.4815 -0.0028 0.0032  -0.0271 112 GLN B CD    
3931 O OE1   . GLN B 112 ? 0.3207 0.3478 0.4216 -0.0030 0.0018  -0.0276 112 GLN B OE1   
3932 N NE2   . GLN B 112 ? 0.4714 0.4927 0.5854 -0.0019 0.0011  -0.0286 112 GLN B NE2   
3933 N N     . PRO B 113 ? 0.0345 0.0615 0.1104 -0.0074 0.0160  -0.0247 113 PRO B N     
3934 C CA    . PRO B 113 ? 0.0350 0.0633 0.1053 -0.0087 0.0176  -0.0264 113 PRO B CA    
3935 C C     . PRO B 113 ? 0.3135 0.3419 0.3877 -0.0090 0.0179  -0.0297 113 PRO B C     
3936 O O     . PRO B 113 ? 0.2958 0.3225 0.3769 -0.0082 0.0173  -0.0303 113 PRO B O     
3937 C CB    . PRO B 113 ? 0.0351 0.0616 0.1014 -0.0090 0.0195  -0.0241 113 PRO B CB    
3938 C CG    . PRO B 113 ? 0.0350 0.0593 0.1063 -0.0078 0.0191  -0.0220 113 PRO B CG    
3939 C CD    . PRO B 113 ? 0.0342 0.0589 0.1094 -0.0069 0.0170  -0.0216 113 PRO B CD    
3940 N N     . PRO B 114 ? 0.3329 0.3628 0.4029 -0.0103 0.0189  -0.0320 114 PRO B N     
3941 C CA    . PRO B 114 ? 0.2993 0.3302 0.3611 -0.0115 0.0200  -0.0314 114 PRO B CA    
3942 C C     . PRO B 114 ? 0.3368 0.3699 0.3975 -0.0111 0.0180  -0.0313 114 PRO B C     
3943 O O     . PRO B 114 ? 0.5935 0.6286 0.6586 -0.0105 0.0160  -0.0336 114 PRO B O     
3944 C CB    . PRO B 114 ? 0.1578 0.1889 0.2170 -0.0130 0.0216  -0.0342 114 PRO B CB    
3945 C CG    . PRO B 114 ? 0.2447 0.2766 0.3111 -0.0122 0.0203  -0.0371 114 PRO B CG    
3946 C CD    . PRO B 114 ? 0.2763 0.3064 0.3493 -0.0107 0.0193  -0.0354 114 PRO B CD    
3947 N N     . ILE B 115 ? 0.2680 0.3011 0.3236 -0.0113 0.0183  -0.0289 115 ILE B N     
3948 C CA    . ILE B 115 ? 0.3490 0.3840 0.4041 -0.0108 0.0163  -0.0282 115 ILE B CA    
3949 C C     . ILE B 115 ? 0.3741 0.4088 0.4212 -0.0119 0.0175  -0.0266 115 ILE B C     
3950 O O     . ILE B 115 ? 0.2180 0.2508 0.2615 -0.0124 0.0191  -0.0253 115 ILE B O     
3951 C CB    . ILE B 115 ? 0.0317 0.0661 0.0926 -0.0092 0.0144  -0.0261 115 ILE B CB    
3952 C CG1   . ILE B 115 ? 0.3483 0.3847 0.4107 -0.0085 0.0118  -0.0258 115 ILE B CG1   
3953 C CG2   . ILE B 115 ? 0.0309 0.0634 0.0895 -0.0089 0.0155  -0.0228 115 ILE B CG2   
3954 C CD1   . ILE B 115 ? 0.1884 0.2239 0.2591 -0.0070 0.0092  -0.0251 115 ILE B CD1   
3955 N N     . TYR B 116 ? 0.4796 0.5162 0.5244 -0.0121 0.0164  -0.0270 116 TYR B N     
3956 C CA    . TYR B 116 ? 0.2507 0.2872 0.2887 -0.0130 0.0170  -0.0258 116 TYR B CA    
3957 C C     . TYR B 116 ? 0.1866 0.2211 0.2227 -0.0125 0.0174  -0.0227 116 TYR B C     
3958 O O     . TYR B 116 ? 0.0613 0.0960 0.1011 -0.0111 0.0161  -0.0207 116 TYR B O     
3959 C CB    . TYR B 116 ? 0.3187 0.3576 0.3575 -0.0124 0.0149  -0.0259 116 TYR B CB    
3960 C CG    . TYR B 116 ? 0.4038 0.4427 0.4354 -0.0136 0.0156  -0.0253 116 TYR B CG    
3961 C CD1   . TYR B 116 ? 0.3326 0.3697 0.3580 -0.0154 0.0180  -0.0259 116 TYR B CD1   
3962 C CD2   . TYR B 116 ? 0.4032 0.4434 0.4346 -0.0129 0.0140  -0.0239 116 TYR B CD2   
3963 C CE1   . TYR B 116 ? 0.3020 0.3382 0.3212 -0.0164 0.0189  -0.0248 116 TYR B CE1   
3964 C CE2   . TYR B 116 ? 0.2650 0.3047 0.2898 -0.0140 0.0147  -0.0234 116 TYR B CE2   
3965 C CZ    . TYR B 116 ? 0.3751 0.4127 0.3939 -0.0158 0.0172  -0.0237 116 TYR B CZ    
3966 O OH    . TYR B 116 ? 0.5639 0.6000 0.5764 -0.0166 0.0183  -0.0224 116 TYR B OH    
3967 N N     . PRO B 117 ? 0.2556 0.2884 0.2866 -0.0136 0.0190  -0.0222 117 PRO B N     
3968 C CA    . PRO B 117 ? 0.0325 0.0639 0.0629 -0.0130 0.0191  -0.0198 117 PRO B CA    
3969 C C     . PRO B 117 ? 0.0437 0.0757 0.0737 -0.0119 0.0176  -0.0174 117 PRO B C     
3970 O O     . PRO B 117 ? 0.1614 0.1929 0.1932 -0.0108 0.0172  -0.0153 117 PRO B O     
3971 C CB    . PRO B 117 ? 0.0438 0.0735 0.0695 -0.0145 0.0209  -0.0202 117 PRO B CB    
3972 C CG    . PRO B 117 ? 0.0654 0.0950 0.0904 -0.0159 0.0222  -0.0226 117 PRO B CG    
3973 C CD    . PRO B 117 ? 0.2870 0.3189 0.3142 -0.0155 0.0209  -0.0240 117 PRO B CD    
3974 N N     . PRO B 118 ? 0.0298 0.0629 0.0573 -0.0123 0.0169  -0.0176 118 PRO B N     
3975 C CA    . PRO B 118 ? 0.0336 0.0671 0.0610 -0.0113 0.0155  -0.0153 118 PRO B CA    
3976 C C     . PRO B 118 ? 0.1858 0.2199 0.2186 -0.0097 0.0142  -0.0135 118 PRO B C     
3977 O O     . PRO B 118 ? 0.2034 0.2371 0.2363 -0.0088 0.0136  -0.0110 118 PRO B O     
3978 C CB    . PRO B 118 ? 0.0277 0.0626 0.0525 -0.0120 0.0148  -0.0163 118 PRO B CB    
3979 C CG    . PRO B 118 ? 0.1212 0.1554 0.1423 -0.0138 0.0165  -0.0183 118 PRO B CG    
3980 C CD    . PRO B 118 ? 0.2002 0.2339 0.2242 -0.0139 0.0174  -0.0196 118 PRO B CD    
3981 N N     . PHE B 119 ? 0.1401 0.1748 0.1776 -0.0094 0.0139  -0.0148 119 PHE B N     
3982 C CA    . PHE B 119 ? 0.0244 0.0590 0.0676 -0.0081 0.0129  -0.0132 119 PHE B CA    
3983 C C     . PHE B 119 ? 0.2278 0.2607 0.2706 -0.0076 0.0138  -0.0113 119 PHE B C     
3984 O O     . PHE B 119 ? 0.2681 0.3006 0.3125 -0.0067 0.0130  -0.0090 119 PHE B O     
3985 C CB    . PHE B 119 ? 0.5267 0.5616 0.5755 -0.0080 0.0125  -0.0155 119 PHE B CB    
3986 C CG    . PHE B 119 ? 0.4487 0.4857 0.4994 -0.0081 0.0107  -0.0172 119 PHE B CG    
3987 C CD1   . PHE B 119 ? 0.3588 0.3973 0.4051 -0.0092 0.0112  -0.0191 119 PHE B CD1   
3988 C CD2   . PHE B 119 ? 0.2743 0.3117 0.3315 -0.0071 0.0084  -0.0170 119 PHE B CD2   
3989 C CE1   . PHE B 119 ? 0.2408 0.2815 0.2893 -0.0091 0.0091  -0.0206 119 PHE B CE1   
3990 C CE2   . PHE B 119 ? 0.2087 0.2481 0.2685 -0.0070 0.0059  -0.0186 119 PHE B CE2   
3991 C CZ    . PHE B 119 ? 0.1203 0.1616 0.1758 -0.0079 0.0061  -0.0203 119 PHE B CZ    
3992 N N     . PHE B 120 ? 0.2370 0.2688 0.2773 -0.0083 0.0153  -0.0123 120 PHE B N     
3993 C CA    . PHE B 120 ? 0.0257 0.0563 0.0657 -0.0079 0.0160  -0.0108 120 PHE B CA    
3994 C C     . PHE B 120 ? 0.0317 0.0623 0.0680 -0.0076 0.0156  -0.0088 120 PHE B C     
3995 O O     . PHE B 120 ? 0.1256 0.1559 0.1626 -0.0066 0.0152  -0.0066 120 PHE B O     
3996 C CB    . PHE B 120 ? 0.1695 0.1990 0.2083 -0.0088 0.0177  -0.0126 120 PHE B CB    
3997 C CG    . PHE B 120 ? 0.0291 0.0583 0.0718 -0.0090 0.0182  -0.0146 120 PHE B CG    
3998 C CD1   . PHE B 120 ? 0.0439 0.0719 0.0911 -0.0082 0.0183  -0.0139 120 PHE B CD1   
3999 C CD2   . PHE B 120 ? 0.0304 0.0603 0.0725 -0.0101 0.0187  -0.0173 120 PHE B CD2   
4000 C CE1   . PHE B 120 ? 0.2242 0.2516 0.2754 -0.0083 0.0188  -0.0158 120 PHE B CE1   
4001 C CE2   . PHE B 120 ? 0.1183 0.1480 0.1642 -0.0102 0.0191  -0.0193 120 PHE B CE2   
4002 C CZ    . PHE B 120 ? 0.2899 0.3184 0.3407 -0.0093 0.0191  -0.0186 120 PHE B CZ    
4003 N N     . GLU B 121 ? 0.0349 0.0657 0.0671 -0.0084 0.0158  -0.0096 121 GLU B N     
4004 C CA    . GLU B 121 ? 0.1710 0.2015 0.2002 -0.0082 0.0155  -0.0081 121 GLU B CA    
4005 C C     . GLU B 121 ? 0.2543 0.2856 0.2843 -0.0071 0.0140  -0.0058 121 GLU B C     
4006 O O     . GLU B 121 ? 0.2247 0.2558 0.2543 -0.0063 0.0136  -0.0037 121 GLU B O     
4007 C CB    . GLU B 121 ? 0.2059 0.2359 0.2308 -0.0096 0.0162  -0.0098 121 GLU B CB    
4008 C CG    . GLU B 121 ? 0.2183 0.2471 0.2420 -0.0106 0.0179  -0.0114 121 GLU B CG    
4009 C CD    . GLU B 121 ? 0.3315 0.3597 0.3560 -0.0099 0.0182  -0.0100 121 GLU B CD    
4010 O OE1   . GLU B 121 ? 0.3758 0.4041 0.3992 -0.0093 0.0175  -0.0085 121 GLU B OE1   
4011 O OE2   . GLU B 121 ? 0.2778 0.3053 0.3036 -0.0100 0.0192  -0.0106 121 GLU B OE2   
4012 N N     . MET B 122 ? 0.0215 0.0538 0.0529 -0.0071 0.0132  -0.0061 122 MET B N     
4013 C CA    . MET B 122 ? 0.1362 0.1692 0.1681 -0.0063 0.0119  -0.0039 122 MET B CA    
4014 C C     . MET B 122 ? 0.0185 0.0518 0.0534 -0.0054 0.0112  -0.0019 122 MET B C     
4015 O O     . MET B 122 ? 0.1074 0.1412 0.1411 -0.0048 0.0104  0.0000  122 MET B O     
4016 C CB    . MET B 122 ? 0.1697 0.2038 0.2026 -0.0067 0.0112  -0.0050 122 MET B CB    
4017 C CG    . MET B 122 ? 0.2040 0.2382 0.2326 -0.0080 0.0116  -0.0074 122 MET B CG    
4018 S SD    . MET B 122 ? 0.3076 0.3404 0.3305 -0.0086 0.0121  -0.0073 122 MET B SD    
4019 C CE    . MET B 122 ? 0.2523 0.2850 0.2755 -0.0074 0.0107  -0.0048 122 MET B CE    
4020 N N     . VAL B 123 ? 0.0330 0.0658 0.0715 -0.0053 0.0116  -0.0029 123 VAL B N     
4021 C CA    . VAL B 123 ? 0.0199 0.0511 0.0611 -0.0045 0.0114  -0.0019 123 VAL B CA    
4022 C C     . VAL B 123 ? 0.1826 0.2132 0.2210 -0.0043 0.0119  -0.0009 123 VAL B C     
4023 O O     . VAL B 123 ? 0.3903 0.4197 0.4285 -0.0036 0.0114  0.0005  123 VAL B O     
4024 C CB    . VAL B 123 ? 0.1060 0.1354 0.1522 -0.0044 0.0120  -0.0032 123 VAL B CB    
4025 C CG1   . VAL B 123 ? 0.1074 0.1337 0.1569 -0.0035 0.0122  -0.0018 123 VAL B CG1   
4026 C CG2   . VAL B 123 ? 0.1956 0.2256 0.2454 -0.0047 0.0111  -0.0046 123 VAL B CG2   
4027 N N     . THR B 125 ? 0.0188 0.0504 0.0485 -0.0047 0.0128  0.0000  125 THR B N     
4028 C CA    . THR B 125 ? 0.0180 0.0493 0.0453 -0.0044 0.0125  0.0012  125 THR B CA    
4029 C C     . THR B 125 ? 0.1959 0.2275 0.2218 -0.0037 0.0107  0.0028  125 THR B C     
4030 O O     . THR B 125 ? 0.2803 0.3117 0.3036 -0.0034 0.0099  0.0033  125 THR B O     
4031 C CB    . THR B 125 ? 0.0193 0.0493 0.0442 -0.0054 0.0130  -0.0008 125 THR B CB    
4032 O OG1   . THR B 125 ? 0.2743 0.3049 0.3001 -0.0057 0.0126  -0.0015 125 THR B OG1   
4033 C CG2   . THR B 125 ? 0.0217 0.0512 0.0450 -0.0066 0.0142  -0.0032 125 THR B CG2   
4034 N N     . ASN B 126 ? 0.1013 0.1339 0.1284 -0.0041 0.0101  0.0018  126 ASN B N     
4035 C CA    . ASN B 126 ? 0.0152 0.0466 0.0430 -0.0041 0.0095  0.0009  126 ASN B CA    
4036 C C     . ASN B 126 ? 0.2793 0.3073 0.3102 -0.0028 0.0097  0.0029  126 ASN B C     
4037 O O     . ASN B 126 ? 0.2748 0.3002 0.3073 -0.0018 0.0091  0.0049  126 ASN B O     
4038 C CB    . ASN B 126 ? 0.0150 0.0471 0.0443 -0.0041 0.0090  0.0010  126 ASN B CB    
4039 C CG    . ASN B 126 ? 0.1169 0.1493 0.1420 -0.0048 0.0082  -0.0003 126 ASN B CG    
4040 O OD1   . ASN B 126 ? 0.3156 0.3435 0.3421 -0.0044 0.0088  -0.0007 126 ASN B OD1   
4041 N ND2   . ASN B 126 ? 0.0155 0.0461 0.0443 -0.0037 0.0091  0.0034  126 ASN B ND2   
4042 N N     . ARG B 128 ? 0.0187 0.0418 0.0592 -0.0014 0.0110  0.0046  128 ARG B N     
4043 C CA    . ARG B 128 ? 0.1580 0.1784 0.2040 -0.0009 0.0112  0.0054  128 ARG B CA    
4044 C C     . ARG B 128 ? 0.1871 0.2071 0.2351 -0.0011 0.0123  0.0044  128 ARG B C     
4045 O O     . ARG B 128 ? 0.4174 0.4397 0.4627 -0.0017 0.0129  0.0030  128 ARG B O     
4046 C CB    . ARG B 128 ? 0.1339 0.1551 0.1821 -0.0013 0.0105  0.0044  128 ARG B CB    
4047 C CG    . ARG B 128 ? 0.3237 0.3426 0.3734 -0.0007 0.0095  0.0065  128 ARG B CG    
4048 C CD    . ARG B 128 ? 0.3639 0.3848 0.4084 -0.0009 0.0089  0.0066  128 ARG B CD    
4049 N NE    . ARG B 128 ? 0.0484 0.0675 0.0942 -0.0004 0.0079  0.0083  128 ARG B NE    
4050 C CZ    . ARG B 128 ? 0.0935 0.1115 0.1364 0.0001  0.0074  0.0103  128 ARG B CZ    
4051 N NH1   . ARG B 128 ? 0.0170 0.0355 0.0558 0.0003  0.0077  0.0105  128 ARG B NH1   
4052 N NH2   . ARG B 128 ? 0.2316 0.2478 0.2759 0.0005  0.0066  0.0121  128 ARG B NH2   
4053 N N     . GLN B 129 ? 0.0422 0.0591 0.0955 -0.0005 0.0126  0.0055  129 GLN B N     
4054 C CA    . GLN B 129 ? 0.0615 0.0773 0.1174 -0.0004 0.0137  0.0051  129 GLN B CA    
4055 C C     . GLN B 129 ? 0.1345 0.1514 0.1933 -0.0012 0.0141  0.0024  129 GLN B C     
4056 O O     . GLN B 129 ? 0.1933 0.2097 0.2555 -0.0013 0.0134  0.0018  129 GLN B O     
4057 C CB    . GLN B 129 ? 0.0694 0.0809 0.1296 0.0007  0.0140  0.0078  129 GLN B CB    
4058 C CG    . GLN B 129 ? 0.1896 0.2001 0.2520 0.0008  0.0152  0.0076  129 GLN B CG    
4059 C CD    . GLN B 129 ? 0.2839 0.2905 0.3494 0.0018  0.0155  0.0107  129 GLN B CD    
4060 O OE1   . GLN B 129 ? 0.0936 0.0994 0.1566 0.0026  0.0152  0.0132  129 GLN B OE1   
4061 N NE2   . GLN B 129 ? 0.3245 0.3287 0.3958 0.0020  0.0162  0.0109  129 GLN B NE2   
4062 N N     . LEU B 130 ? 0.1606 0.1788 0.2179 -0.0017 0.0151  0.0009  130 LEU B N     
4063 C CA    . LEU B 130 ? 0.2077 0.2266 0.2674 -0.0025 0.0156  -0.0017 130 LEU B CA    
4064 C C     . LEU B 130 ? 0.2555 0.2711 0.3219 -0.0019 0.0161  -0.0014 130 LEU B C     
4065 O O     . LEU B 130 ? 0.5835 0.5969 0.6513 -0.0013 0.0168  0.0002  130 LEU B O     
4066 C CB    . LEU B 130 ? 0.1012 0.1221 0.1572 -0.0032 0.0166  -0.0032 130 LEU B CB    
4067 C CG    . LEU B 130 ? 0.1737 0.1956 0.2310 -0.0042 0.0172  -0.0060 130 LEU B CG    
4068 C CD1   . LEU B 130 ? 0.2435 0.2664 0.3028 -0.0043 0.0160  -0.0070 130 LEU B CD1   
4069 C CD2   . LEU B 130 ? 0.0278 0.0516 0.0803 -0.0051 0.0179  -0.0073 130 LEU B CD2   
4070 N N     . CYS B 131 ? 0.1843 0.1995 0.2553 -0.0021 0.0154  -0.0027 131 CYS B N     
4071 C CA    . CYS B 131 ? 0.1177 0.1304 0.1955 -0.0019 0.0158  -0.0035 131 CYS B CA    
4072 C C     . CYS B 131 ? 0.0511 0.0660 0.1300 -0.0028 0.0157  -0.0070 131 CYS B C     
4073 O O     . CYS B 131 ? 0.1660 0.1831 0.2440 -0.0032 0.0146  -0.0083 131 CYS B O     
4074 C CB    . CYS B 131 ? 0.2030 0.2125 0.2871 -0.0012 0.0148  -0.0020 131 CYS B CB    
4075 S SG    . CYS B 131 ? 0.4388 0.4446 0.5231 -0.0002 0.0153  0.0022  131 CYS B SG    
4076 N N     . VAL B 132 ? 0.1275 0.1414 0.2091 -0.0030 0.0168  -0.0084 132 VAL B N     
4077 C CA    . VAL B 132 ? 0.2425 0.2584 0.3249 -0.0038 0.0168  -0.0118 132 VAL B CA    
4078 C C     . VAL B 132 ? 0.2561 0.2696 0.3469 -0.0035 0.0165  -0.0131 132 VAL B C     
4079 O O     . VAL B 132 ? 0.3181 0.3283 0.4130 -0.0029 0.0172  -0.0116 132 VAL B O     
4080 C CB    . VAL B 132 ? 0.3171 0.3346 0.3946 -0.0047 0.0184  -0.0131 132 VAL B CB    
4081 C CG1   . VAL B 132 ? 0.1262 0.1467 0.1961 -0.0053 0.0184  -0.0129 132 VAL B CG1   
4082 C CG2   . VAL B 132 ? 0.0348 0.0500 0.1131 -0.0042 0.0198  -0.0113 132 VAL B CG2   
4083 N N     . SER B 133 ? 0.0365 0.0515 0.1299 -0.0038 0.0154  -0.0161 133 SER B N     
4084 C CA    . SER B 133 ? 0.0965 0.1098 0.1977 -0.0037 0.0149  -0.0183 133 SER B CA    
4085 C C     . SER B 133 ? 0.1919 0.2082 0.2915 -0.0044 0.0149  -0.0220 133 SER B C     
4086 O O     . SER B 133 ? 0.4058 0.4236 0.5081 -0.0043 0.0128  -0.0243 133 SER B O     
4087 C CB    . SER B 133 ? 0.0398 0.0510 0.1485 -0.0029 0.0126  -0.0182 133 SER B CB    
4088 O OG    . SER B 133 ? 0.2915 0.3016 0.4078 -0.0027 0.0115  -0.0212 133 SER B OG    
4089 N N     . PRO B 134 ? 0.0700 0.0870 0.1657 -0.0052 0.0169  -0.0227 134 PRO B N     
4090 C CA    . PRO B 134 ? 0.0392 0.0588 0.1328 -0.0061 0.0172  -0.0260 134 PRO B CA    
4091 C C     . PRO B 134 ? 0.2020 0.2212 0.3035 -0.0057 0.0156  -0.0293 134 PRO B C     
4092 O O     . PRO B 134 ? 0.1400 0.1562 0.2485 -0.0051 0.0155  -0.0292 134 PRO B O     
4093 C CB    . PRO B 134 ? 0.0398 0.0587 0.1295 -0.0068 0.0198  -0.0257 134 PRO B CB    
4094 C CG    . PRO B 134 ? 0.0393 0.0561 0.1276 -0.0063 0.0206  -0.0221 134 PRO B CG    
4095 C CD    . PRO B 134 ? 0.1111 0.1261 0.2049 -0.0052 0.0190  -0.0205 134 PRO B CD    
4096 N N     . LEU B 135 ? 0.1862 0.2083 0.2869 -0.0059 0.0143  -0.0322 135 LEU B N     
4097 C CA    . LEU B 135 ? 0.2919 0.3144 0.3998 -0.0053 0.0122  -0.0358 135 LEU B CA    
4098 C C     . LEU B 135 ? 0.2585 0.2800 0.3681 -0.0059 0.0141  -0.0378 135 LEU B C     
4099 O O     . LEU B 135 ? 0.3091 0.3305 0.4128 -0.0070 0.0170  -0.0369 135 LEU B O     
4100 C CB    . LEU B 135 ? 0.3733 0.3996 0.4788 -0.0053 0.0102  -0.0383 135 LEU B CB    
4101 C CG    . LEU B 135 ? 0.1747 0.2020 0.2782 -0.0048 0.0083  -0.0364 135 LEU B CG    
4102 C CD1   . LEU B 135 ? 0.0399 0.0713 0.1388 -0.0051 0.0069  -0.0380 135 LEU B CD1   
4103 C CD2   . LEU B 135 ? 0.2501 0.2749 0.3630 -0.0033 0.0051  -0.0367 135 LEU B CD2   
4104 N N     . GLN B 136 ? 0.2395 0.2601 0.3573 -0.0050 0.0122  -0.0408 136 GLN B N     
4105 C CA    . GLN B 136 ? 0.0482 0.0677 0.1690 -0.0054 0.0136  -0.0430 136 GLN B CA    
4106 C C     . GLN B 136 ? 0.3175 0.3404 0.4380 -0.0055 0.0124  -0.0472 136 GLN B C     
4107 O O     . GLN B 136 ? 0.3297 0.3542 0.4541 -0.0042 0.0086  -0.0494 136 GLN B O     
4108 C CB    . GLN B 136 ? 0.0756 0.0914 0.2068 -0.0043 0.0124  -0.0433 136 GLN B CB    
4109 C CG    . GLN B 136 ? 0.1894 0.2016 0.3219 -0.0042 0.0137  -0.0392 136 GLN B CG    
4110 C CD    . GLN B 136 ? 0.3792 0.3883 0.5189 -0.0039 0.0143  -0.0389 136 GLN B CD    
4111 O OE1   . GLN B 136 ? 0.5296 0.5397 0.6730 -0.0038 0.0135  -0.0416 136 GLN B OE1   
4112 N NE2   . GLN B 136 ? 0.4740 0.4804 0.6144 -0.0037 0.0154  -0.0350 136 GLN B NE2   
4113 N N     . LYS B 137 ? 0.1534 0.1770 0.2690 -0.0069 0.0152  -0.0482 137 LYS B N     
4114 C CA    . LYS B 137 ? 0.2078 0.2344 0.3221 -0.0072 0.0147  -0.0522 137 LYS B CA    
4115 C C     . LYS B 137 ? 0.1786 0.2041 0.3023 -0.0061 0.0130  -0.0556 137 LYS B C     
4116 O O     . LYS B 137 ? 0.2294 0.2522 0.3552 -0.0067 0.0153  -0.0553 137 LYS B O     
4117 C CB    . LYS B 137 ? 0.2371 0.2640 0.3423 -0.0095 0.0187  -0.0516 137 LYS B CB    
4118 C CG    . LYS B 137 ? 0.1989 0.2288 0.3006 -0.0104 0.0189  -0.0551 137 LYS B CG    
4119 C CD    . LYS B 137 ? 0.2457 0.2747 0.3383 -0.0130 0.0231  -0.0536 137 LYS B CD    
4120 C CE    . LYS B 137 ? 0.3487 0.3804 0.4355 -0.0145 0.0238  -0.0559 137 LYS B CE    
4121 N NZ    . LYS B 137 ? 0.3314 0.3651 0.4126 -0.0146 0.0231  -0.0546 137 LYS B NZ    
4122 N N     . GLN B 138 ? 0.1934 0.2209 0.3228 -0.0041 0.0085  -0.0586 138 GLN B N     
4123 C CA    . GLN B 138 ? 0.2171 0.2441 0.3556 -0.0025 0.0058  -0.0617 138 GLN B CA    
4124 C C     . GLN B 138 ? 0.5350 0.5662 0.6750 -0.0008 0.0017  -0.0659 138 GLN B C     
4125 O O     . GLN B 138 ? 0.7018 0.7359 0.8393 -0.0002 -0.0016 -0.0657 138 GLN B O     
4126 C CB    . GLN B 138 ? 0.2025 0.2268 0.3497 -0.0010 0.0026  -0.0603 138 GLN B CB    
4127 C CG    . GLN B 138 ? 0.2157 0.2361 0.3633 -0.0021 0.0057  -0.0562 138 GLN B CG    
4128 C CD    . GLN B 138 ? 0.1806 0.1987 0.3363 -0.0008 0.0026  -0.0548 138 GLN B CD    
4129 O OE1   . GLN B 138 ? 0.2254 0.2444 0.3866 0.0009  -0.0021 -0.0571 138 GLN B OE1   
4130 N NE2   . GLN B 138 ? 0.1889 0.2040 0.3454 -0.0014 0.0049  -0.0509 138 GLN B NE2   
4131 N N     . ASN B 139 ? 0.6152 0.6478 0.7594 -0.0004 0.0010  -0.0689 139 ASN B N     
4132 C CA    . ASN B 139 ? 0.6044 0.6422 0.7590 0.0023  -0.0045 -0.0768 139 ASN B CA    
4133 C C     . ASN B 139 ? 0.7333 0.7764 0.8836 0.0016  -0.0051 -0.0802 139 ASN B C     
4134 O O     . ASN B 139 ? 0.8638 0.9071 1.0126 0.0018  -0.0132 -0.0822 139 ASN B O     
4135 C CB    . ASN B 139 ? 0.5527 0.5889 0.7157 0.0054  -0.0121 -0.0775 139 ASN B CB    
4136 C CG    . ASN B 139 ? 0.7201 0.7513 0.8857 0.0051  -0.0112 -0.0733 139 ASN B CG    
4137 O OD1   . ASN B 139 ? 0.8385 0.8693 1.0059 0.0043  -0.0089 -0.0734 139 ASN B OD1   
4138 N ND2   . ASN B 139 ? 0.6479 0.6760 0.8157 0.0057  -0.0132 -0.0707 139 ASN B ND2   
4139 N N     . ASP B 140 ? 0.4558 0.4995 0.5974 -0.0012 0.0024  -0.0789 140 ASP B N     
4140 C CA    . ASP B 140 ? 0.4148 0.4630 0.5497 -0.0033 0.0033  -0.0809 140 ASP B CA    
4141 C C     . ASP B 140 ? 0.4221 0.4689 0.5528 -0.0029 -0.0016 -0.0783 140 ASP B C     
4142 O O     . ASP B 140 ? 0.2981 0.3416 0.4179 -0.0045 -0.0065 -0.0803 140 ASP B O     
4143 C CB    . ASP B 140 ? 0.3809 0.4243 0.5062 -0.0056 -0.0021 -0.0856 140 ASP B CB    
4144 C CG    . ASP B 140 ? 0.5288 0.5721 0.6472 -0.0086 0.0060  -0.0866 140 ASP B CG    
4145 O OD1   . ASP B 140 ? 0.5798 0.6288 0.6972 -0.0111 0.0141  -0.0839 140 ASP B OD1   
4146 O OD2   . ASP B 140 ? 0.6135 0.6501 0.7260 -0.0084 0.0043  -0.0895 140 ASP B OD2   
4147 N N     . THR B 141 ? 0.2542 0.2971 0.3856 -0.0015 -0.0010 -0.0729 141 THR B N     
4148 C CA    . THR B 141 ? 0.3486 0.3908 0.4746 -0.0017 -0.0027 -0.0690 141 THR B CA    
4149 C C     . THR B 141 ? 0.3812 0.4185 0.5006 -0.0029 0.0010  -0.0600 141 THR B C     
4150 O O     . THR B 141 ? 0.4459 0.4803 0.5660 -0.0038 0.0048  -0.0591 141 THR B O     
4151 C CB    . THR B 141 ? 0.4867 0.5285 0.6172 0.0003  -0.0124 -0.0710 141 THR B CB    
4152 O OG1   . THR B 141 ? 0.4216 0.4620 0.5485 0.0005  -0.0136 -0.0665 141 THR B OG1   
4153 C CG2   . THR B 141 ? 0.5819 0.6213 0.7222 0.0027  -0.0163 -0.0720 141 THR B CG2   
4154 N N     . TYR B 142 ? 0.2658 0.3026 0.3834 -0.0026 -0.0005 -0.0568 142 TYR B N     
4155 C CA    . TYR B 142 ? 0.1278 0.1611 0.2456 -0.0031 0.0023  -0.0532 142 TYR B CA    
4156 C C     . TYR B 142 ? 0.1354 0.1662 0.2618 -0.0011 -0.0019 -0.0529 142 TYR B C     
4157 O O     . TYR B 142 ? 0.2320 0.2640 0.3613 0.0004  -0.0073 -0.0545 142 TYR B O     
4158 C CB    . TYR B 142 ? 0.1311 0.1654 0.2397 -0.0046 0.0049  -0.0498 142 TYR B CB    
4159 C CG    . TYR B 142 ? 0.1828 0.2175 0.2829 -0.0068 0.0098  -0.0493 142 TYR B CG    
4160 C CD1   . TYR B 142 ? 0.1003 0.1380 0.1953 -0.0077 0.0103  -0.0516 142 TYR B CD1   
4161 C CD2   . TYR B 142 ? 0.3698 0.4015 0.4669 -0.0079 0.0136  -0.0464 142 TYR B CD2   
4162 C CE1   . TYR B 142 ? 0.1262 0.1632 0.2133 -0.0100 0.0149  -0.0511 142 TYR B CE1   
4163 C CE2   . TYR B 142 ? 0.0439 0.0753 0.1334 -0.0099 0.0173  -0.0459 142 TYR B CE2   
4164 C CZ    . TYR B 142 ? 0.0443 0.0780 0.1288 -0.0111 0.0181  -0.0482 142 TYR B CZ    
4165 O OH    . TYR B 142 ? 0.1186 0.1511 0.1957 -0.0133 0.0217  -0.0475 142 TYR B OH    
4166 N N     . VAL B 143 ? 0.0507 0.0774 0.1810 -0.0013 0.0001  -0.0508 143 VAL B N     
4167 C CA    . VAL B 143 ? 0.0888 0.1122 0.2272 0.0001  -0.0029 -0.0500 143 VAL B CA    
4168 C C     . VAL B 143 ? 0.1962 0.2170 0.3320 -0.0008 0.0001  -0.0455 143 VAL B C     
4169 O O     . VAL B 143 ? 0.2006 0.2213 0.3303 -0.0023 0.0043  -0.0434 143 VAL B O     
4170 C CB    . VAL B 143 ? 0.2644 0.2847 0.4129 0.0013  -0.0045 -0.0527 143 VAL B CB    
4171 C CG1   . VAL B 143 ? 0.3735 0.3967 0.5243 0.0026  -0.0081 -0.0572 143 VAL B CG1   
4172 C CG2   . VAL B 143 ? 0.2211 0.2389 0.3694 -0.0001 0.0003  -0.0513 143 VAL B CG2   
4173 N N     . ILE B 144 ? 0.2732 0.2916 0.4135 0.0001  -0.0024 -0.0441 144 ILE B N     
4174 C CA    . ILE B 144 ? 0.2554 0.2713 0.3941 -0.0005 -0.0002 -0.0398 144 ILE B CA    
4175 C C     . ILE B 144 ? 0.2214 0.2327 0.3666 -0.0005 0.0015  -0.0388 144 ILE B C     
4176 O O     . ILE B 144 ? 0.3609 0.3712 0.5137 0.0002  -0.0007 -0.0404 144 ILE B O     
4177 C CB    . ILE B 144 ? 0.2212 0.2362 0.3621 0.0004  -0.0035 -0.0386 144 ILE B CB    
4178 C CG1   . ILE B 144 ? 0.2460 0.2655 0.3799 0.0003  -0.0051 -0.0392 144 ILE B CG1   
4179 C CG2   . ILE B 144 ? 0.1600 0.1721 0.2997 -0.0001 -0.0015 -0.0342 144 ILE B CG2   
4180 C CD1   . ILE B 144 ? 0.1382 0.1569 0.2727 0.0010  -0.0079 -0.0376 144 ILE B CD1   
4181 N N     . ASP B 145 ? 0.1656 0.1755 0.3066 -0.0014 0.0051  -0.0353 145 ASP B N     
4182 C CA    . ASP B 145 ? 0.1453 0.1520 0.2904 -0.0015 0.0066  -0.0329 145 ASP B CA    
4183 C C     . ASP B 145 ? 0.2087 0.2135 0.3566 -0.0010 0.0052  -0.0295 145 ASP B C     
4184 O O     . ASP B 145 ? 0.2299 0.2334 0.3739 -0.0012 0.0070  -0.0259 145 ASP B O     
4185 C CB    . ASP B 145 ? 0.1443 0.1503 0.2836 -0.0023 0.0106  -0.0310 145 ASP B CB    
4186 C CG    . ASP B 145 ? 0.1904 0.1948 0.3333 -0.0024 0.0121  -0.0295 145 ASP B CG    
4187 O OD1   . ASP B 145 ? 0.1133 0.1166 0.2626 -0.0019 0.0104  -0.0286 145 ASP B OD1   
4188 O OD2   . ASP B 145 ? 0.3160 0.3201 0.4552 -0.0030 0.0148  -0.0293 145 ASP B OD2   
4189 N N     . PHE B 146 ? 0.2571 0.2617 0.4120 -0.0003 0.0019  -0.0307 146 PHE B N     
4190 C CA    . PHE B 146 ? 0.2792 0.2823 0.4369 0.0001  0.0003  -0.0278 146 PHE B CA    
4191 C C     . PHE B 146 ? 0.2510 0.2520 0.4092 -0.0002 0.0027  -0.0238 146 PHE B C     
4192 O O     . PHE B 146 ? 0.4611 0.4611 0.6180 -0.0002 0.0028  -0.0205 146 PHE B O     
4193 C CB    . PHE B 146 ? 0.0602 0.0632 0.2255 0.0009  -0.0040 -0.0302 146 PHE B CB    
4194 C CG    . PHE B 146 ? 0.0600 0.0647 0.2245 0.0017  -0.0073 -0.0335 146 PHE B CG    
4195 C CD1   . PHE B 146 ? 0.0586 0.0632 0.2203 0.0018  -0.0086 -0.0323 146 PHE B CD1   
4196 C CD2   . PHE B 146 ? 0.0614 0.0678 0.2282 0.0023  -0.0094 -0.0379 146 PHE B CD2   
4197 C CE1   . PHE B 146 ? 0.0588 0.0647 0.2196 0.0027  -0.0119 -0.0353 146 PHE B CE1   
4198 C CE2   . PHE B 146 ? 0.0617 0.0696 0.2275 0.0033  -0.0130 -0.0410 146 PHE B CE2   
4199 C CZ    . PHE B 146 ? 0.0604 0.0681 0.2233 0.0035  -0.0143 -0.0397 146 PHE B CZ    
4200 N N     . LYS B 147 ? 0.1385 0.1391 0.2985 -0.0005 0.0046  -0.0238 147 LYS B N     
4201 C CA    . LYS B 147 ? 0.2926 0.2914 0.4528 -0.0006 0.0067  -0.0199 147 LYS B CA    
4202 C C     . LYS B 147 ? 0.4610 0.4595 0.6133 -0.0009 0.0093  -0.0170 147 LYS B C     
4203 O O     . LYS B 147 ? 0.5847 0.5820 0.7353 -0.0007 0.0098  -0.0134 147 LYS B O     
4204 C CB    . LYS B 147 ? 0.2396 0.2379 0.4036 -0.0008 0.0081  -0.0206 147 LYS B CB    
4205 C CG    . LYS B 147 ? 0.2201 0.2167 0.3844 -0.0008 0.0102  -0.0166 147 LYS B CG    
4206 C CD    . LYS B 147 ? 0.2054 0.2016 0.3719 -0.0010 0.0121  -0.0171 147 LYS B CD    
4207 C CE    . LYS B 147 ? 0.0874 0.0821 0.2510 -0.0010 0.0147  -0.0132 147 LYS B CE    
4208 N NZ    . LYS B 147 ? 0.1677 0.1613 0.3330 -0.0007 0.0142  -0.0098 147 LYS B NZ    
4209 N N     . HIS B 148 ? 0.5272 0.5266 0.6743 -0.0012 0.0108  -0.0186 148 HIS B N     
4210 C CA    . HIS B 148 ? 0.3208 0.3200 0.4604 -0.0014 0.0129  -0.0162 148 HIS B CA    
4211 C C     . HIS B 148 ? 0.2010 0.2005 0.3373 -0.0012 0.0117  -0.0152 148 HIS B C     
4212 O O     . HIS B 148 ? 0.1827 0.1814 0.3151 -0.0010 0.0126  -0.0118 148 HIS B O     
4213 C CB    . HIS B 148 ? 0.4114 0.4116 0.5470 -0.0020 0.0147  -0.0188 148 HIS B CB    
4214 C CG    . HIS B 148 ? 0.3175 0.3173 0.4458 -0.0021 0.0168  -0.0168 148 HIS B CG    
4215 N ND1   . HIS B 148 ? 0.2231 0.2254 0.3448 -0.0024 0.0164  -0.0170 148 HIS B ND1   
4216 C CD2   . HIS B 148 ? 0.2813 0.2797 0.4067 -0.0021 0.0189  -0.0141 148 HIS B CD2   
4217 C CE1   . HIS B 148 ? 0.3770 0.3800 0.4919 -0.0025 0.0181  -0.0146 148 HIS B CE1   
4218 N NE2   . HIS B 148 ? 0.3491 0.3491 0.4667 -0.0022 0.0196  -0.0130 148 HIS B NE2   
4219 N N     . LEU B 149 ? 0.2360 0.2368 0.3741 -0.0012 0.0093  -0.0181 149 LEU B N     
4220 C CA    . LEU B 149 ? 0.2240 0.2252 0.3593 -0.0010 0.0081  -0.0171 149 LEU B CA    
4221 C C     . LEU B 149 ? 0.2881 0.2877 0.4250 -0.0007 0.0075  -0.0133 149 LEU B C     
4222 O O     . LEU B 149 ? 0.5245 0.5237 0.6566 -0.0006 0.0083  -0.0104 149 LEU B O     
4223 C CB    . LEU B 149 ? 0.1205 0.1231 0.2585 -0.0008 0.0052  -0.0208 149 LEU B CB    
4224 C CG    . LEU B 149 ? 0.1452 0.1482 0.2801 -0.0006 0.0039  -0.0194 149 LEU B CG    
4225 C CD1   . LEU B 149 ? 0.2653 0.2714 0.3896 -0.0012 0.0063  -0.0175 149 LEU B CD1   
4226 C CD2   . LEU B 149 ? 0.3094 0.3150 0.4459 -0.0002 0.0006  -0.0228 149 LEU B CD2   
4227 N N     . GLU B 150 ? 0.0515 0.0503 0.1950 -0.0005 0.0062  -0.0132 150 GLU B N     
4228 C CA    . GLU B 150 ? 0.0528 0.0503 0.1979 -0.0003 0.0060  -0.0098 150 GLU B CA    
4229 C C     . GLU B 150 ? 0.2481 0.2447 0.3894 -0.0003 0.0087  -0.0063 150 GLU B C     
4230 O O     . GLU B 150 ? 0.3043 0.3002 0.4440 -0.0001 0.0089  -0.0031 150 GLU B O     
4231 C CB    . GLU B 150 ? 0.3272 0.3241 0.4807 -0.0001 0.0040  -0.0108 150 GLU B CB    
4232 C CG    . GLU B 150 ? 0.4332 0.4287 0.5887 0.0000  0.0040  -0.0074 150 GLU B CG    
4233 C CD    . GLU B 150 ? 0.3725 0.3674 0.5368 0.0001  0.0021  -0.0086 150 GLU B CD    
4234 O OE1   . GLU B 150 ? 0.1844 0.1788 0.3516 0.0002  0.0001  -0.0081 150 GLU B OE1   
4235 O OE2   . GLU B 150 ? 0.3619 0.3566 0.5302 0.0000  0.0027  -0.0100 150 GLU B OE2   
4236 N N     . LYS B 151 ? 0.3025 0.2992 0.4424 -0.0004 0.0107  -0.0070 151 LYS B N     
4237 C CA    . LYS B 151 ? 0.3371 0.3329 0.4729 -0.0002 0.0130  -0.0039 151 LYS B CA    
4238 C C     . LYS B 151 ? 0.0550 0.0511 0.1834 -0.0001 0.0136  -0.0020 151 LYS B C     
4239 O O     . LYS B 151 ? 0.0483 0.0438 0.1736 0.0003  0.0145  0.0013  151 LYS B O     
4240 C CB    . LYS B 151 ? 0.4938 0.4896 0.6296 -0.0004 0.0148  -0.0052 151 LYS B CB    
4241 C CG    . LYS B 151 ? 0.4791 0.4739 0.6203 -0.0004 0.0153  -0.0045 151 LYS B CG    
4242 C CD    . LYS B 151 ? 0.4404 0.4351 0.5806 -0.0006 0.0173  -0.0057 151 LYS B CD    
4243 C CE    . LYS B 151 ? 0.3146 0.3083 0.4597 -0.0004 0.0182  -0.0047 151 LYS B CE    
4244 N NZ    . LYS B 151 ? 0.1263 0.1200 0.2706 -0.0007 0.0199  -0.0062 151 LYS B NZ    
4245 N N     . GLN B 152 ? 0.0993 0.0964 0.2249 -0.0003 0.0130  -0.0040 152 GLN B N     
4246 C CA    . GLN B 152 ? 0.2325 0.2299 0.3515 -0.0002 0.0134  -0.0022 152 GLN B CA    
4247 C C     . GLN B 152 ? 0.1976 0.1949 0.3166 0.0001  0.0119  -0.0001 152 GLN B C     
4248 O O     . GLN B 152 ? 0.1840 0.1810 0.2982 0.0004  0.0124  0.0028  152 GLN B O     
4249 C CB    . GLN B 152 ? 0.0415 0.0400 0.1576 -0.0006 0.0134  -0.0051 152 GLN B CB    
4250 C CG    . GLN B 152 ? 0.0674 0.0678 0.1810 -0.0011 0.0148  -0.0075 152 GLN B CG    
4251 C CD    . GLN B 152 ? 0.2259 0.2260 0.3344 -0.0009 0.0167  -0.0052 152 GLN B CD    
4252 O OE1   . GLN B 152 ? 0.3651 0.3681 0.4660 -0.0011 0.0171  -0.0047 152 GLN B OE1   
4253 N NE2   . GLN B 152 ? 0.0423 0.0395 0.1549 -0.0005 0.0177  -0.0034 152 GLN B NE2   
4254 N N     . PHE B 153 ? 0.2096 0.2069 0.3339 0.0000  0.0098  -0.0015 153 PHE B N     
4255 C CA    . PHE B 153 ? 0.1731 0.1702 0.2977 0.0001  0.0083  0.0004  153 PHE B CA    
4256 C C     . PHE B 153 ? 0.1928 0.1889 0.3178 0.0004  0.0090  0.0037  153 PHE B C     
4257 O O     . PHE B 153 ? 0.2484 0.2444 0.3716 0.0005  0.0085  0.0058  153 PHE B O     
4258 C CB    . PHE B 153 ? 0.0475 0.0447 0.1784 0.0000  0.0057  -0.0020 153 PHE B CB    
4259 C CG    . PHE B 153 ? 0.0459 0.0444 0.1763 -0.0001 0.0044  -0.0052 153 PHE B CG    
4260 C CD1   . PHE B 153 ? 0.0431 0.0424 0.1677 -0.0002 0.0058  -0.0059 153 PHE B CD1   
4261 C CD2   . PHE B 153 ? 0.3810 0.3797 0.5168 0.0000  0.0015  -0.0078 153 PHE B CD2   
4262 C CE1   . PHE B 153 ? 0.0418 0.0425 0.1658 -0.0004 0.0048  -0.0091 153 PHE B CE1   
4263 C CE2   . PHE B 153 ? 0.2396 0.2396 0.3747 0.0001  0.0001  -0.0110 153 PHE B CE2   
4264 C CZ    . PHE B 153 ? 0.0435 0.0445 0.1727 -0.0002 0.0018  -0.0117 153 PHE B CZ    
4265 N N     . GLN B 154 ? 0.2783 0.2738 0.4060 0.0004  0.0102  0.0040  154 GLN B N     
4266 C CA    . GLN B 154 ? 0.2874 0.2820 0.4154 0.0007  0.0110  0.0070  154 GLN B CA    
4267 C C     . GLN B 154 ? 0.2802 0.2750 0.4009 0.0011  0.0124  0.0096  154 GLN B C     
4268 O O     . GLN B 154 ? 0.2547 0.2491 0.3745 0.0014  0.0129  0.0122  154 GLN B O     
4269 C CB    . GLN B 154 ? 0.2104 0.2043 0.3437 0.0007  0.0119  0.0064  154 GLN B CB    
4270 C CG    . GLN B 154 ? 0.2196 0.2131 0.3611 0.0005  0.0102  0.0047  154 GLN B CG    
4271 C CD    . GLN B 154 ? 0.3157 0.3084 0.4631 0.0004  0.0109  0.0043  154 GLN B CD    
4272 O OE1   . GLN B 154 ? 0.3787 0.3714 0.5247 0.0005  0.0126  0.0042  154 GLN B OE1   
4273 N NE2   . GLN B 154 ? 0.2927 0.2848 0.4469 0.0004  0.0097  0.0041  154 GLN B NE2   
4274 N N     . GLN B 155 ? 0.4921 0.4876 0.6075 0.0011  0.0129  0.0090  155 GLN B N     
4275 C CA    . GLN B 155 ? 0.2900 0.2858 0.3985 0.0015  0.0139  0.0112  155 GLN B CA    
4276 C C     . GLN B 155 ? 0.4377 0.4341 0.5420 0.0016  0.0129  0.0122  155 GLN B C     
4277 O O     . GLN B 155 ? 0.5377 0.5346 0.6362 0.0020  0.0134  0.0139  155 GLN B O     
4278 C CB    . GLN B 155 ? 0.2295 0.2257 0.3351 0.0015  0.0151  0.0099  155 GLN B CB    
4279 C CG    . GLN B 155 ? 0.2431 0.2386 0.3514 0.0015  0.0164  0.0093  155 GLN B CG    
4280 C CD    . GLN B 155 ? 0.4094 0.4053 0.5159 0.0012  0.0175  0.0072  155 GLN B CD    
4281 O OE1   . GLN B 155 ? 0.6952 0.6917 0.7995 0.0009  0.0171  0.0055  155 GLN B OE1   
4282 N NE2   . GLN B 155 ? 0.1936 0.1890 0.3004 0.0013  0.0189  0.0074  155 GLN B NE2   
4283 N N     . GLY B 156 ? 0.4191 0.4156 0.5262 0.0013  0.0114  0.0112  156 GLY B N     
4284 C CA    . GLY B 156 ? 0.3769 0.3739 0.4804 0.0013  0.0104  0.0123  156 GLY B CA    
4285 C C     . GLY B 156 ? 0.3119 0.3097 0.4135 0.0011  0.0098  0.0105  156 GLY B C     
4286 O O     . GLY B 156 ? 0.2722 0.2706 0.3689 0.0012  0.0095  0.0117  156 GLY B O     
4287 N N     . ILE B 157 ? 0.2293 0.2272 0.3346 0.0007  0.0094  0.0075  157 ILE B N     
4288 C CA    . ILE B 157 ? 0.3290 0.3277 0.4326 0.0005  0.0089  0.0055  157 ILE B CA    
4289 C C     . ILE B 157 ? 0.4671 0.4661 0.5713 0.0004  0.0070  0.0059  157 ILE B C     
4290 O O     . ILE B 157 ? 0.6529 0.6515 0.7624 0.0003  0.0055  0.0053  157 ILE B O     
4291 C CB    . ILE B 157 ? 0.3629 0.3619 0.4708 0.0002  0.0087  0.0018  157 ILE B CB    
4292 C CG1   . ILE B 157 ? 0.4691 0.4679 0.5760 0.0001  0.0107  0.0014  157 ILE B CG1   
4293 C CG2   . ILE B 157 ? 0.4228 0.4257 0.5265 -0.0003 0.0078  -0.0007 157 ILE B CG2   
4294 C CD1   . ILE B 157 ? 0.5621 0.5636 0.6605 0.0000  0.0120  0.0018  157 ILE B CD1   
4295 N N     . LYS B 158 ? 0.5112 0.5109 0.6101 0.0005  0.0071  0.0068  158 LYS B N     
4296 C CA    . LYS B 158 ? 0.3855 0.3854 0.4840 0.0004  0.0055  0.0073  158 LYS B CA    
4297 C C     . LYS B 158 ? 0.3038 0.3066 0.4021 0.0000  0.0041  0.0042  158 LYS B C     
4298 O O     . LYS B 158 ? 0.2921 0.2941 0.3943 0.0000  0.0021  0.0036  158 LYS B O     
4299 C CB    . LYS B 158 ? 0.3060 0.3063 0.3975 0.0007  0.0062  0.0102  158 LYS B CB    
4300 C CG    . LYS B 158 ? 0.4175 0.4173 0.5078 0.0010  0.0063  0.0128  158 LYS B CG    
4301 C CD    . LYS B 158 ? 0.4409 0.4404 0.5334 0.0008  0.0047  0.0133  158 LYS B CD    
4302 C CE    . LYS B 158 ? 0.4486 0.4475 0.5409 0.0009  0.0050  0.0154  158 LYS B CE    
4303 N NZ    . LYS B 158 ? 0.3197 0.3184 0.4120 0.0008  0.0037  0.0163  158 LYS B NZ    
4304 N N     . LEU B 159 ? 0.3042 0.3110 0.3971 -0.0004 0.0050  0.0021  159 LEU B N     
4305 C CA    . LEU B 159 ? 0.3888 0.4000 0.4793 -0.0009 0.0038  -0.0008 159 LEU B CA    
4306 C C     . LEU B 159 ? 0.4012 0.4144 0.4926 -0.0013 0.0044  -0.0038 159 LEU B C     
4307 O O     . LEU B 159 ? 0.0310 0.0435 0.1215 -0.0013 0.0062  -0.0035 159 LEU B O     
4308 C CB    . LEU B 159 ? 0.4275 0.4424 0.5090 -0.0013 0.0045  -0.0001 159 LEU B CB    
4309 C CG    . LEU B 159 ? 0.3489 0.3683 0.4275 -0.0019 0.0033  -0.0024 159 LEU B CG    
4310 C CD1   . LEU B 159 ? 0.2302 0.2486 0.3124 -0.0017 0.0009  -0.0021 159 LEU B CD1   
4311 C CD2   . LEU B 159 ? 0.1753 0.1984 0.2449 -0.0024 0.0047  -0.0020 159 LEU B CD2   
4312 N N     . MET B 160 ? 0.3654 0.3808 0.4588 -0.0015 0.0026  -0.0067 160 MET B N     
4313 C CA    . MET B 160 ? 0.2366 0.2544 0.3306 -0.0018 0.0028  -0.0098 160 MET B CA    
4314 C C     . MET B 160 ? 0.1553 0.1778 0.2445 -0.0024 0.0019  -0.0116 160 MET B C     
4315 O O     . MET B 160 ? 0.2367 0.2598 0.3267 -0.0022 -0.0004 -0.0117 160 MET B O     
4316 C CB    . MET B 160 ? 0.1178 0.1329 0.2214 -0.0013 0.0009  -0.0119 160 MET B CB    
4317 C CG    . MET B 160 ? 0.1369 0.1548 0.2412 -0.0015 0.0001  -0.0157 160 MET B CG    
4318 S SD    . MET B 160 ? 0.4748 0.4896 0.5901 -0.0008 -0.0021 -0.0186 160 MET B SD    
4319 C CE    . MET B 160 ? 0.3990 0.4184 0.5120 -0.0010 -0.0032 -0.0228 160 MET B CE    
4320 N N     . LEU B 161 ? 0.0296 0.0549 0.1137 -0.0031 0.0036  -0.0129 161 LEU B N     
4321 C CA    . LEU B 161 ? 0.1483 0.1778 0.2281 -0.0037 0.0030  -0.0146 161 LEU B CA    
4322 C C     . LEU B 161 ? 0.1277 0.1580 0.2119 -0.0036 0.0016  -0.0181 161 LEU B C     
4323 O O     . LEU B 161 ? 0.2570 0.2872 0.3409 -0.0040 0.0033  -0.0194 161 LEU B O     
4324 C CB    . LEU B 161 ? 0.2067 0.2384 0.2779 -0.0046 0.0056  -0.0136 161 LEU B CB    
4325 C CG    . LEU B 161 ? 0.2946 0.3264 0.3607 -0.0046 0.0062  -0.0106 161 LEU B CG    
4326 C CD1   . LEU B 161 ? 0.0235 0.0559 0.0829 -0.0052 0.0085  -0.0097 161 LEU B CD1   
4327 C CD2   . LEU B 161 ? 0.0238 0.0579 0.0883 -0.0048 0.0043  -0.0104 161 LEU B CD2   
4328 N N     . LEU B 162 ? 0.0562 0.0871 0.1444 -0.0031 -0.0019 -0.0199 162 LEU B N     
4329 C CA    . LEU B 162 ? 0.1365 0.1681 0.2290 -0.0027 -0.0042 -0.0235 162 LEU B CA    
4330 C C     . LEU B 162 ? 0.1371 0.1728 0.2241 -0.0034 -0.0050 -0.0250 162 LEU B C     
4331 O O     . LEU B 162 ? 0.2432 0.2806 0.3264 -0.0036 -0.0062 -0.0239 162 LEU B O     
4332 C CB    . LEU B 162 ? 0.0525 0.0813 0.1536 -0.0013 -0.0087 -0.0249 162 LEU B CB    
4333 C CG    . LEU B 162 ? 0.0563 0.0860 0.1611 -0.0005 -0.0124 -0.0289 162 LEU B CG    
4334 C CD1   . LEU B 162 ? 0.0428 0.0700 0.1539 -0.0001 -0.0114 -0.0304 162 LEU B CD1   
4335 C CD2   . LEU B 162 ? 0.2680 0.2960 0.3770 0.0008  -0.0182 -0.0300 162 LEU B CD2   
4336 N N     . CYS B 163 ? 0.2506 0.2876 0.3373 -0.0037 -0.0045 -0.0276 163 CYS B N     
4337 C CA    . CYS B 163 ? 0.2575 0.2977 0.3399 -0.0044 -0.0059 -0.0297 163 CYS B CA    
4338 C C     . CYS B 163 ? 0.2483 0.2879 0.3366 -0.0032 -0.0112 -0.0332 163 CYS B C     
4339 O O     . CYS B 163 ? 0.1233 0.1618 0.2165 -0.0026 -0.0108 -0.0352 163 CYS B O     
4340 C CB    . CYS B 163 ? 0.0927 0.1342 0.1689 -0.0058 -0.0011 -0.0299 163 CYS B CB    
4341 S SG    . CYS B 163 ? 0.2818 0.3264 0.3509 -0.0072 -0.0019 -0.0317 163 CYS B SG    
4342 N N     . SER B 164 ? 0.1965 0.2360 0.2838 -0.0027 -0.0167 -0.0342 164 SER B N     
4343 C CA    . SER B 164 ? 0.0951 0.1324 0.1861 -0.0014 -0.0230 -0.0377 164 SER B CA    
4344 C C     . SER B 164 ? 0.1349 0.1709 0.2172 -0.0022 -0.0288 -0.0393 164 SER B C     
4345 O O     . SER B 164 ? 0.3157 0.3500 0.3963 -0.0016 -0.0321 -0.0382 164 SER B O     
4346 C CB    . SER B 164 ? 0.0521 0.0858 0.1522 0.0007  -0.0260 -0.0378 164 SER B CB    
4347 O OG    . SER B 164 ? 0.0995 0.1311 0.2044 0.0022  -0.0306 -0.0415 164 SER B OG    
4348 N N     . PRO B 165 ? 0.0626 0.0972 0.1414 -0.0023 -0.0316 -0.0448 165 PRO B N     
4349 C CA    . PRO B 165 ? 0.1850 0.2212 0.2665 -0.0027 -0.0286 -0.0477 165 PRO B CA    
4350 C C     . PRO B 165 ? 0.4754 0.5166 0.5561 -0.0046 -0.0193 -0.0447 165 PRO B C     
4351 O O     . PRO B 165 ? 0.6443 0.6872 0.7201 -0.0058 -0.0159 -0.0415 165 PRO B O     
4352 C CB    . PRO B 165 ? 0.1712 0.2013 0.2415 -0.0027 -0.0345 -0.0543 165 PRO B CB    
4353 C CG    . PRO B 165 ? 0.2886 0.3121 0.3530 -0.0009 -0.0424 -0.0545 165 PRO B CG    
4354 C CD    . PRO B 165 ? 0.0762 0.1043 0.1448 -0.0015 -0.0394 -0.0490 165 PRO B CD    
4355 N N     . HIS B 166 ? 0.3929 0.4354 0.4773 -0.0048 -0.0151 -0.0454 166 HIS B N     
4356 C CA    . HIS B 166 ? 0.1411 0.1850 0.2218 -0.0061 -0.0068 -0.0405 166 HIS B CA    
4357 C C     . HIS B 166 ? 0.1555 0.2021 0.2323 -0.0078 -0.0024 -0.0456 166 HIS B C     
4358 O O     . HIS B 166 ? 0.2531 0.3006 0.3328 -0.0081 -0.0021 -0.0510 166 HIS B O     
4359 C CB    . HIS B 166 ? 0.2058 0.2478 0.2936 -0.0049 -0.0049 -0.0406 166 HIS B CB    
4360 C CG    . HIS B 166 ? 0.2441 0.2847 0.3287 -0.0059 0.0015  -0.0383 166 HIS B CG    
4361 N ND1   . HIS B 166 ? 0.1963 0.2343 0.2828 -0.0054 0.0027  -0.0353 166 HIS B ND1   
4362 C CD2   . HIS B 166 ? 0.0362 0.0769 0.1150 -0.0074 0.0061  -0.0384 166 HIS B CD2   
4363 C CE1   . HIS B 166 ? 0.0839 0.1205 0.1659 -0.0065 0.0069  -0.0336 166 HIS B CE1   
4364 N NE2   . HIS B 166 ? 0.1444 0.1823 0.2217 -0.0077 0.0090  -0.0354 166 HIS B NE2   
4365 N N     . ASN B 167 ? 0.1393 0.1872 0.2087 -0.0093 0.0016  -0.0439 167 ASN B N     
4366 C CA    . ASN B 167 ? 0.0622 0.1119 0.1248 -0.0118 0.0083  -0.0471 167 ASN B CA    
4367 C C     . ASN B 167 ? 0.0350 0.0791 0.0924 -0.0116 0.0118  -0.0388 167 ASN B C     
4368 O O     . ASN B 167 ? 0.1930 0.2351 0.2513 -0.0107 0.0117  -0.0351 167 ASN B O     
4369 C CB    . ASN B 167 ? 0.2335 0.2849 0.2878 -0.0138 0.0109  -0.0473 167 ASN B CB    
4370 C CG    . ASN B 167 ? 0.2083 0.2560 0.2507 -0.0167 0.0174  -0.0445 167 ASN B CG    
4371 O OD1   . ASN B 167 ? 0.2237 0.2714 0.2621 -0.0189 0.0208  -0.0480 167 ASN B OD1   
4372 N ND2   . ASN B 167 ? 0.3219 0.3642 0.3581 -0.0151 0.0172  -0.0348 167 ASN B ND2   
4373 N N     . PRO B 168 ? 0.0372 0.0802 0.0925 -0.0129 0.0150  -0.0412 168 PRO B N     
4374 C CA    . PRO B 168 ? 0.1572 0.2039 0.2126 -0.0160 0.0181  -0.0513 168 PRO B CA    
4375 C C     . PRO B 168 ? 0.2489 0.2990 0.3149 -0.0148 0.0162  -0.0592 168 PRO B C     
4376 O O     . PRO B 168 ? 0.1363 0.1847 0.1963 -0.0159 0.0156  -0.0647 168 PRO B O     
4377 C CB    . PRO B 168 ? 0.0435 0.0846 0.0886 -0.0173 0.0218  -0.0441 168 PRO B CB    
4378 C CG    . PRO B 168 ? 0.0857 0.1235 0.1333 -0.0153 0.0205  -0.0387 168 PRO B CG    
4379 C CD    . PRO B 168 ? 0.0371 0.0763 0.0910 -0.0131 0.0172  -0.0378 168 PRO B CD    
4380 N N     . ILE B 169 ? 0.4221 0.4695 0.4951 -0.0118 0.0123  -0.0546 169 ILE B N     
4381 C CA    . ILE B 169 ? 0.3296 0.3780 0.4114 -0.0106 0.0101  -0.0595 169 ILE B CA    
4382 C C     . ILE B 169 ? 0.1966 0.2446 0.2810 -0.0096 0.0007  -0.0647 169 ILE B C     
4383 O O     . ILE B 169 ? 0.1071 0.1502 0.1888 -0.0094 -0.0030 -0.0691 169 ILE B O     
4384 C CB    . ILE B 169 ? 0.0428 0.0864 0.1273 -0.0088 0.0087  -0.0521 169 ILE B CB    
4385 C CG1   . ILE B 169 ? 0.1417 0.1848 0.2318 -0.0067 0.0026  -0.0497 169 ILE B CG1   
4386 C CG2   . ILE B 169 ? 0.0397 0.0795 0.1163 -0.0099 0.0127  -0.0451 169 ILE B CG2   
4387 C CD1   . ILE B 169 ? 0.2212 0.2607 0.3154 -0.0057 0.0034  -0.0462 169 ILE B CD1   
4388 N N     . GLY B 170 ? 0.2600 0.3057 0.3409 -0.0089 -0.0049 -0.0630 170 GLY B N     
4389 C CA    . GLY B 170 ? 0.1914 0.2275 0.2640 -0.0073 -0.0154 -0.0661 170 GLY B CA    
4390 C C     . GLY B 170 ? 0.1184 0.1547 0.2030 -0.0045 -0.0217 -0.0646 170 GLY B C     
4391 O O     . GLY B 170 ? 0.1672 0.1957 0.2464 -0.0030 -0.0294 -0.0681 170 GLY B O     
4392 N N     . ARG B 171 ? 0.0606 0.1018 0.1564 -0.0035 -0.0178 -0.0593 171 ARG B N     
4393 C CA    . ARG B 171 ? 0.1394 0.1783 0.2432 -0.0011 -0.0223 -0.0577 171 ARG B CA    
4394 C C     . ARG B 171 ? 0.2147 0.2507 0.3162 -0.0001 -0.0283 -0.0561 171 ARG B C     
4395 O O     . ARG B 171 ? 0.3481 0.3854 0.4455 -0.0011 -0.0257 -0.0521 171 ARG B O     
4396 C CB    . ARG B 171 ? 0.2165 0.2556 0.3238 -0.0013 -0.0159 -0.0517 171 ARG B CB    
4397 C CG    . ARG B 171 ? 0.3554 0.3943 0.4671 -0.0011 -0.0131 -0.0535 171 ARG B CG    
4398 C CD    . ARG B 171 ? 0.2807 0.3187 0.4002 0.0009  -0.0199 -0.0598 171 ARG B CD    
4399 N NE    . ARG B 171 ? 0.1265 0.1613 0.2499 0.0029  -0.0270 -0.0598 171 ARG B NE    
4400 C CZ    . ARG B 171 ? 0.0943 0.1268 0.2236 0.0040  -0.0264 -0.0568 171 ARG B CZ    
4401 N NH1   . ARG B 171 ? 0.1195 0.1510 0.2522 0.0035  -0.0202 -0.0549 171 ARG B NH1   
4402 N NH2   . ARG B 171 ? 0.0988 0.1283 0.2326 0.0060  -0.0329 -0.0579 171 ARG B NH2   
4403 N N     . VAL B 172 ? 0.1453 0.1768 0.2489 0.0019  -0.0363 -0.0591 172 VAL B N     
4404 C CA    . VAL B 172 ? 0.2140 0.2422 0.3173 0.0034  -0.0419 -0.0576 172 VAL B CA    
4405 C C     . VAL B 172 ? 0.2166 0.2446 0.3309 0.0050  -0.0415 -0.0555 172 VAL B C     
4406 O O     . VAL B 172 ? 0.1729 0.1981 0.2925 0.0069  -0.0463 -0.0590 172 VAL B O     
4407 C CB    . VAL B 172 ? 0.3198 0.3407 0.4140 0.0048  -0.0512 -0.0623 172 VAL B CB    
4408 C CG1   . VAL B 172 ? 0.2253 0.2433 0.3213 0.0067  -0.0564 -0.0606 172 VAL B CG1   
4409 C CG2   . VAL B 172 ? 0.3358 0.3527 0.4130 0.0031  -0.0511 -0.0644 172 VAL B CG2   
4410 N N     . TRP B 173 ? 0.2046 0.2334 0.3229 0.0049  -0.0368 -0.0515 173 TRP B N     
4411 C CA    . TRP B 173 ? 0.1384 0.1645 0.2684 0.0066  -0.0362 -0.0515 173 TRP B CA    
4412 C C     . TRP B 173 ? 0.3341 0.3560 0.4701 0.0092  -0.0439 -0.0539 173 TRP B C     
4413 O O     . TRP B 173 ? 0.4023 0.4226 0.5339 0.0098  -0.0488 -0.0539 173 TRP B O     
4414 C CB    . TRP B 173 ? 0.2437 0.2692 0.3746 0.0057  -0.0311 -0.0476 173 TRP B CB    
4415 C CG    . TRP B 173 ? 0.2896 0.3184 0.4135 0.0035  -0.0241 -0.0451 173 TRP B CG    
4416 C CD1   . TRP B 173 ? 0.2904 0.3217 0.4062 0.0020  -0.0217 -0.0424 173 TRP B CD1   
4417 C CD2   . TRP B 173 ? 0.3300 0.3595 0.4543 0.0025  -0.0189 -0.0452 173 TRP B CD2   
4418 N NE1   . TRP B 173 ? 0.1820 0.2153 0.2930 0.0003  -0.0154 -0.0408 173 TRP B NE1   
4419 C CE2   . TRP B 173 ? 0.3155 0.3476 0.4314 0.0005  -0.0136 -0.0424 173 TRP B CE2   
4420 C CE3   . TRP B 173 ? 0.2217 0.2494 0.3526 0.0030  -0.0182 -0.0473 173 TRP B CE3   
4421 C CZ2   . TRP B 173 ? 0.4397 0.4720 0.5531 -0.0008 -0.0082 -0.0418 173 TRP B CZ2   
4422 C CZ3   . TRP B 173 ? 0.0548 0.0831 0.1833 0.0016  -0.0126 -0.0465 173 TRP B CZ3   
4423 C CH2   . TRP B 173 ? 0.2746 0.3050 0.3942 -0.0003 -0.0078 -0.0438 173 TRP B CH2   
4424 N N     . THR B 174 ? 0.3315 0.3510 0.4773 0.0107  -0.0450 -0.0561 174 THR B N     
4425 C CA    . THR B 174 ? 0.2824 0.2973 0.4356 0.0133  -0.0519 -0.0583 174 THR B CA    
4426 C C     . THR B 174 ? 0.1598 0.1711 0.3179 0.0136  -0.0515 -0.0558 174 THR B C     
4427 O O     . THR B 174 ? 0.1446 0.1565 0.3021 0.0118  -0.0457 -0.0525 174 THR B O     
4428 C CB    . THR B 174 ? 0.2167 0.2298 0.3803 0.0147  -0.0526 -0.0612 174 THR B CB    
4429 O OG1   . THR B 174 ? 0.0828 0.0950 0.2517 0.0135  -0.0458 -0.0591 174 THR B OG1   
4430 C CG2   . THR B 174 ? 0.0915 0.1072 0.2512 0.0147  -0.0544 -0.0641 174 THR B CG2   
4431 N N     . LYS B 175 ? 0.1448 0.1518 0.3086 0.0158  -0.0581 -0.0577 175 LYS B N     
4432 C CA    . LYS B 175 ? 0.1385 0.1413 0.3088 0.0160  -0.0583 -0.0559 175 LYS B CA    
4433 C C     . LYS B 175 ? 0.1577 0.1583 0.3370 0.0151  -0.0536 -0.0548 175 LYS B C     
4434 O O     . LYS B 175 ? 0.2580 0.2581 0.4376 0.0133  -0.0498 -0.0508 175 LYS B O     
4435 C CB    . LYS B 175 ? 0.2332 0.2314 0.4080 0.0187  -0.0667 -0.0586 175 LYS B CB    
4436 C CG    . LYS B 175 ? 0.3291 0.3226 0.5127 0.0188  -0.0675 -0.0572 175 LYS B CG    
4437 C CD    . LYS B 175 ? 0.5249 0.5146 0.7137 0.0213  -0.0757 -0.0602 175 LYS B CD    
4438 C CE    . LYS B 175 ? 0.4428 0.4303 0.6373 0.0202  -0.0761 -0.0577 175 LYS B CE    
4439 N NZ    . LYS B 175 ? 0.3311 0.3197 0.5335 0.0183  -0.0717 -0.0558 175 LYS B NZ    
4440 N N     . GLU B 176 ? 0.1952 0.1968 0.3787 0.0153  -0.0531 -0.0567 176 GLU B N     
4441 C CA    . GLU B 176 ? 0.2267 0.2284 0.4152 0.0133  -0.0482 -0.0542 176 GLU B CA    
4442 C C     . GLU B 176 ? 0.3275 0.3312 0.5104 0.0110  -0.0406 -0.0507 176 GLU B C     
4443 O O     . GLU B 176 ? 0.3096 0.3122 0.4937 0.0094  -0.0369 -0.0469 176 GLU B O     
4444 C CB    . GLU B 176 ? 0.1583 0.1606 0.3525 0.0142  -0.0496 -0.0572 176 GLU B CB    
4445 C CG    . GLU B 176 ? 0.2772 0.2772 0.4777 0.0166  -0.0573 -0.0606 176 GLU B CG    
4446 C CD    . GLU B 176 ? 0.5644 0.5643 0.7608 0.0194  -0.0636 -0.0648 176 GLU B CD    
4447 O OE1   . GLU B 176 ? 0.6794 0.6814 0.8739 0.0203  -0.0636 -0.0675 176 GLU B OE1   
4448 O OE2   . GLU B 176 ? 0.7210 0.7183 0.9158 0.0210  -0.0688 -0.0653 176 GLU B OE2   
4449 N N     . GLU B 177 ? 0.3200 0.3263 0.4963 0.0109  -0.0385 -0.0519 177 GLU B N     
4450 C CA    . GLU B 177 ? 0.0710 0.0787 0.2414 0.0088  -0.0317 -0.0489 177 GLU B CA    
4451 C C     . GLU B 177 ? 0.0687 0.0751 0.2360 0.0080  -0.0304 -0.0452 177 GLU B C     
4452 O O     . GLU B 177 ? 0.0662 0.0718 0.2331 0.0064  -0.0262 -0.0413 177 GLU B O     
4453 C CB    . GLU B 177 ? 0.3693 0.3823 0.5308 0.0082  -0.0299 -0.0499 177 GLU B CB    
4454 C CG    . GLU B 177 ? 0.1526 0.1670 0.3160 0.0082  -0.0282 -0.0525 177 GLU B CG    
4455 C CD    . GLU B 177 ? 0.0683 0.0875 0.2248 0.0083  -0.0299 -0.0548 177 GLU B CD    
4456 O OE1   . GLU B 177 ? 0.0721 0.0921 0.2260 0.0095  -0.0355 -0.0561 177 GLU B OE1   
4457 O OE2   . GLU B 177 ? 0.2573 0.2792 0.4104 0.0071  -0.0258 -0.0552 177 GLU B OE2   
4458 N N     . LEU B 178 ? 0.0701 0.0777 0.2336 0.0087  -0.0342 -0.0454 178 LEU B N     
4459 C CA    . LEU B 178 ? 0.1298 0.1368 0.2896 0.0078  -0.0330 -0.0418 178 LEU B CA    
4460 C C     . LEU B 178 ? 0.1145 0.1169 0.2820 0.0077  -0.0335 -0.0398 178 LEU B C     
4461 O O     . LEU B 178 ? 0.0668 0.0687 0.2320 0.0063  -0.0296 -0.0358 178 LEU B O     
4462 C CB    . LEU B 178 ? 0.1130 0.1220 0.2675 0.0086  -0.0376 -0.0426 178 LEU B CB    
4463 C CG    . LEU B 178 ? 0.1688 0.1831 0.3146 0.0081  -0.0368 -0.0439 178 LEU B CG    
4464 C CD1   . LEU B 178 ? 0.2006 0.2151 0.3427 0.0095  -0.0434 -0.0460 178 LEU B CD1   
4465 C CD2   . LEU B 178 ? 0.3552 0.3732 0.4923 0.0059  -0.0307 -0.0404 178 LEU B CD2   
4466 N N     . ILE B 179 ? 0.0867 0.0875 0.2614 0.0088  -0.0378 -0.0417 179 ILE B N     
4467 C CA    . ILE B 179 ? 0.0781 0.0767 0.2586 0.0081  -0.0378 -0.0391 179 ILE B CA    
4468 C C     . ILE B 179 ? 0.0749 0.0739 0.2557 0.0065  -0.0320 -0.0359 179 ILE B C     
4469 O O     . ILE B 179 ? 0.1436 0.1416 0.3233 0.0054  -0.0294 -0.0320 179 ILE B O     
4470 C CB    . ILE B 179 ? 0.3305 0.3275 0.5190 0.0096  -0.0435 -0.0423 179 ILE B CB    
4471 C CG1   . ILE B 179 ? 0.3747 0.3699 0.5627 0.0113  -0.0498 -0.0442 179 ILE B CG1   
4472 C CG2   . ILE B 179 ? 0.0875 0.0829 0.2834 0.0088  -0.0425 -0.0402 179 ILE B CG2   
4473 C CD1   . ILE B 179 ? 0.1498 0.1435 0.3371 0.0105  -0.0496 -0.0408 179 ILE B CD1   
4474 N N     . LYS B 180 ? 0.1318 0.1320 0.3131 0.0063  -0.0299 -0.0374 180 LYS B N     
4475 C CA    . LYS B 180 ? 0.0723 0.0723 0.2541 0.0050  -0.0250 -0.0344 180 LYS B CA    
4476 C C     . LYS B 180 ? 0.0669 0.0676 0.2407 0.0038  -0.0201 -0.0311 180 LYS B C     
4477 O O     . LYS B 180 ? 0.2019 0.2017 0.3751 0.0029  -0.0168 -0.0276 180 LYS B O     
4478 C CB    . LYS B 180 ? 0.3693 0.3702 0.5543 0.0051  -0.0244 -0.0369 180 LYS B CB    
4479 C CG    . LYS B 180 ? 0.4463 0.4496 0.6263 0.0053  -0.0232 -0.0396 180 LYS B CG    
4480 C CD    . LYS B 180 ? 0.3118 0.3156 0.4952 0.0051  -0.0216 -0.0411 180 LYS B CD    
4481 C CE    . LYS B 180 ? 0.2026 0.2077 0.3887 0.0066  -0.0257 -0.0460 180 LYS B CE    
4482 N NZ    . LYS B 180 ? 0.3207 0.3267 0.5091 0.0063  -0.0238 -0.0475 180 LYS B NZ    
4483 N N     . LEU B 181 ? 0.2559 0.2582 0.4236 0.0039  -0.0199 -0.0323 181 LEU B N     
4484 C CA    . LEU B 181 ? 0.3046 0.3071 0.4649 0.0030  -0.0163 -0.0291 181 LEU B CA    
4485 C C     . LEU B 181 ? 0.1700 0.1712 0.3299 0.0030  -0.0178 -0.0266 181 LEU B C     
4486 O O     . LEU B 181 ? 0.0990 0.0995 0.2557 0.0022  -0.0149 -0.0227 181 LEU B O     
4487 C CB    . LEU B 181 ? 0.2888 0.2936 0.4429 0.0031  -0.0155 -0.0316 181 LEU B CB    
4488 C CG    . LEU B 181 ? 0.0949 0.1026 0.2392 0.0022  -0.0130 -0.0283 181 LEU B CG    
4489 C CD1   . LEU B 181 ? 0.0492 0.0557 0.1900 0.0012  -0.0082 -0.0246 181 LEU B CD1   
4490 C CD2   . LEU B 181 ? 0.0497 0.0631 0.1856 0.0018  -0.0129 -0.0298 181 LEU B CD2   
4491 N N     . GLY B 182 ? 0.0626 0.0634 0.2257 0.0040  -0.0226 -0.0287 182 GLY B N     
4492 C CA    . GLY B 182 ? 0.2498 0.2489 0.4134 0.0039  -0.0242 -0.0262 182 GLY B CA    
4493 C C     . GLY B 182 ? 0.3615 0.3590 0.5295 0.0033  -0.0227 -0.0232 182 GLY B C     
4494 O O     . GLY B 182 ? 0.2556 0.2524 0.4217 0.0027  -0.0214 -0.0198 182 GLY B O     
4495 N N     . SER B 183 ? 0.1886 0.1858 0.3626 0.0034  -0.0231 -0.0245 183 SER B N     
4496 C CA    . SER B 183 ? 0.0784 0.0742 0.2569 0.0029  -0.0217 -0.0218 183 SER B CA    
4497 C C     . SER B 183 ? 0.0667 0.0626 0.2398 0.0019  -0.0166 -0.0179 183 SER B C     
4498 O O     . SER B 183 ? 0.0674 0.0622 0.2414 0.0015  -0.0153 -0.0147 183 SER B O     
4499 C CB    . SER B 183 ? 0.1638 0.1593 0.3497 0.0033  -0.0230 -0.0243 183 SER B CB    
4500 O OG    . SER B 183 ? 0.2255 0.2200 0.4179 0.0043  -0.0282 -0.0273 183 SER B OG    
4501 N N     . LEU B 184 ? 0.0833 0.0805 0.2507 0.0017  -0.0139 -0.0181 184 LEU B N     
4502 C CA    . LEU B 184 ? 0.2326 0.2297 0.3942 0.0010  -0.0095 -0.0145 184 LEU B CA    
4503 C C     . LEU B 184 ? 0.1004 0.0977 0.2556 0.0008  -0.0088 -0.0120 184 LEU B C     
4504 O O     . LEU B 184 ? 0.1323 0.1290 0.2842 0.0005  -0.0063 -0.0084 184 LEU B O     
4505 C CB    . LEU B 184 ? 0.3968 0.3951 0.5551 0.0009  -0.0070 -0.0158 184 LEU B CB    
4506 C CG    . LEU B 184 ? 0.2354 0.2335 0.3995 0.0010  -0.0070 -0.0177 184 LEU B CG    
4507 C CD1   . LEU B 184 ? 0.0581 0.0572 0.2181 0.0007  -0.0041 -0.0186 184 LEU B CD1   
4508 C CD2   . LEU B 184 ? 0.0646 0.0611 0.2331 0.0008  -0.0061 -0.0151 184 LEU B CD2   
4509 N N     . CYS B 185 ? 0.1682 0.1663 0.3216 0.0011  -0.0110 -0.0138 185 CYS B N     
4510 C CA    . CYS B 185 ? 0.2885 0.2866 0.4360 0.0009  -0.0103 -0.0114 185 CYS B CA    
4511 C C     . CYS B 185 ? 0.2496 0.2465 0.3997 0.0008  -0.0116 -0.0090 185 CYS B C     
4512 O O     . CYS B 185 ? 0.1661 0.1627 0.3116 0.0005  -0.0098 -0.0057 185 CYS B O     
4513 C CB    . CYS B 185 ? 0.2776 0.2768 0.4226 0.0012  -0.0123 -0.0140 185 CYS B CB    
4514 S SG    . CYS B 185 ? 0.3637 0.3648 0.5062 0.0014  -0.0110 -0.0175 185 CYS B SG    
4515 N N     . THR B 186 ? 0.3111 0.3071 0.4682 0.0012  -0.0150 -0.0108 186 THR B N     
4516 C CA    . THR B 186 ? 0.0619 0.0566 0.2224 0.0010  -0.0160 -0.0087 186 THR B CA    
4517 C C     . THR B 186 ? 0.0640 0.0581 0.2248 0.0006  -0.0129 -0.0057 186 THR B C     
4518 O O     . THR B 186 ? 0.0687 0.0623 0.2274 0.0003  -0.0117 -0.0026 186 THR B O     
4519 C CB    . THR B 186 ? 0.0667 0.0604 0.2352 0.0016  -0.0204 -0.0117 186 THR B CB    
4520 O OG1   . THR B 186 ? 0.1154 0.1094 0.2826 0.0021  -0.0238 -0.0139 186 THR B OG1   
4521 C CG2   . THR B 186 ? 0.0699 0.0621 0.2433 0.0014  -0.0212 -0.0097 186 THR B CG2   
4522 N N     . LYS B 187 ? 0.2066 0.2007 0.3703 0.0007  -0.0118 -0.0067 187 LYS B N     
4523 C CA    . LYS B 187 ? 0.1780 0.1713 0.3430 0.0004  -0.0093 -0.0041 187 LYS B CA    
4524 C C     . LYS B 187 ? 0.2157 0.2094 0.3725 0.0002  -0.0058 -0.0008 187 LYS B C     
4525 O O     . LYS B 187 ? 0.3415 0.3345 0.4977 0.0001  -0.0043 0.0021  187 LYS B O     
4526 C CB    . LYS B 187 ? 0.0662 0.0595 0.2364 0.0005  -0.0091 -0.0063 187 LYS B CB    
4527 C CG    . LYS B 187 ? 0.1452 0.1378 0.3164 0.0003  -0.0063 -0.0041 187 LYS B CG    
4528 C CD    . LYS B 187 ? 0.0783 0.0711 0.2536 0.0004  -0.0061 -0.0066 187 LYS B CD    
4529 C CE    . LYS B 187 ? 0.1473 0.1392 0.3250 0.0003  -0.0038 -0.0044 187 LYS B CE    
4530 N NZ    . LYS B 187 ? 0.0682 0.0599 0.2394 0.0001  -0.0009 -0.0005 187 LYS B NZ    
4531 N N     . TYR B 188 ? 0.2136 0.2084 0.3639 0.0002  -0.0046 -0.0012 188 TYR B N     
4532 C CA    . TYR B 188 ? 0.2544 0.2494 0.3970 0.0001  -0.0017 0.0018  188 TYR B CA    
4533 C C     . TYR B 188 ? 0.1232 0.1188 0.2601 0.0001  -0.0021 0.0030  188 TYR B C     
4534 O O     . TYR B 188 ? 0.0563 0.0521 0.1868 0.0001  -0.0001 0.0055  188 TYR B O     
4535 C CB    . TYR B 188 ? 0.3310 0.3267 0.4702 0.0001  0.0004  0.0009  188 TYR B CB    
4536 C CG    . TYR B 188 ? 0.0545 0.0497 0.1986 0.0002  0.0012  0.0004  188 TYR B CG    
4537 C CD1   . TYR B 188 ? 0.0554 0.0498 0.1987 0.0002  0.0032  0.0032  188 TYR B CD1   
4538 C CD2   . TYR B 188 ? 0.0562 0.0515 0.2059 0.0002  -0.0002 -0.0029 188 TYR B CD2   
4539 C CE1   . TYR B 188 ? 0.0579 0.0516 0.2060 0.0002  0.0039  0.0028  188 TYR B CE1   
4540 C CE2   . TYR B 188 ? 0.0628 0.0576 0.2173 0.0002  0.0005  -0.0034 188 TYR B CE2   
4541 C CZ    . TYR B 188 ? 0.0962 0.0901 0.2499 0.0001  0.0026  -0.0005 188 TYR B CZ    
4542 O OH    . TYR B 188 ? 0.2878 0.2811 0.4466 0.0001  0.0033  -0.0010 188 TYR B OH    
4543 N N     . ASN B 189 ? 0.0712 0.0668 0.2108 0.0001  -0.0048 0.0014  189 ASN B N     
4544 C CA    . ASN B 189 ? 0.2859 0.2820 0.4208 0.0000  -0.0054 0.0021  189 ASN B CA    
4545 C C     . ASN B 189 ? 0.3370 0.3342 0.4648 0.0000  -0.0037 0.0021  189 ASN B C     
4546 O O     . ASN B 189 ? 0.0909 0.0885 0.2124 0.0000  -0.0021 0.0046  189 ASN B O     
4547 C CB    . ASN B 189 ? 0.2621 0.2576 0.3947 -0.0001 -0.0047 0.0054  189 ASN B CB    
4548 C CG    . ASN B 189 ? 0.0496 0.0454 0.1800 -0.0002 -0.0062 0.0057  189 ASN B CG    
4549 O OD1   . ASN B 189 ? 0.0505 0.0463 0.1842 -0.0001 -0.0089 0.0033  189 ASN B OD1   
4550 N ND2   . ASN B 189 ? 0.0479 0.0439 0.1726 -0.0002 -0.0048 0.0085  189 ASN B ND2   
4551 N N     . VAL B 190 ? 0.3570 0.3549 0.4862 0.0001  -0.0042 -0.0009 190 VAL B N     
4552 C CA    . VAL B 190 ? 0.3654 0.3644 0.4890 0.0001  -0.0028 -0.0017 190 VAL B CA    
4553 C C     . VAL B 190 ? 0.4319 0.4315 0.5551 0.0002  -0.0052 -0.0033 190 VAL B C     
4554 O O     . VAL B 190 ? 0.5090 0.5084 0.6375 0.0004  -0.0083 -0.0058 190 VAL B O     
4555 C CB    . VAL B 190 ? 0.1852 0.1848 0.3102 0.0001  -0.0018 -0.0043 190 VAL B CB    
4556 C CG1   . VAL B 190 ? 0.0429 0.0448 0.1601 -0.0001 0.0003  -0.0046 190 VAL B CG1   
4557 C CG2   . VAL B 190 ? 0.3270 0.3256 0.4539 0.0001  -0.0001 -0.0028 190 VAL B CG2   
4558 N N     . ILE B 191 ? 0.3107 0.3123 0.4263 0.0000  -0.0039 -0.0019 191 ILE B N     
4559 C CA    . ILE B 191 ? 0.0545 0.0597 0.1663 -0.0002 -0.0058 -0.0033 191 ILE B CA    
4560 C C     . ILE B 191 ? 0.0368 0.0467 0.1451 -0.0004 -0.0056 -0.0065 191 ILE B C     
4561 O O     . ILE B 191 ? 0.5531 0.5643 0.6581 -0.0007 -0.0031 -0.0066 191 ILE B O     
4562 C CB    . ILE B 191 ? 0.1141 0.1205 0.2183 -0.0004 -0.0043 -0.0004 191 ILE B CB    
4563 C CG1   . ILE B 191 ? 0.1610 0.1624 0.2692 -0.0002 -0.0046 0.0029  191 ILE B CG1   
4564 C CG2   . ILE B 191 ? 0.2203 0.2308 0.3197 -0.0007 -0.0058 -0.0017 191 ILE B CG2   
4565 C CD1   . ILE B 191 ? 0.0525 0.0518 0.1680 -0.0001 -0.0078 0.0020  191 ILE B CD1   
4566 N N     . VAL B 192 ? 0.0380 0.0500 0.1474 -0.0003 -0.0085 -0.0092 192 VAL B N     
4567 C CA    . VAL B 192 ? 0.2460 0.2621 0.3531 -0.0004 -0.0089 -0.0123 192 VAL B CA    
4568 C C     . VAL B 192 ? 0.3079 0.3284 0.4080 -0.0009 -0.0096 -0.0126 192 VAL B C     
4569 O O     . VAL B 192 ? 0.4417 0.4616 0.5429 -0.0006 -0.0124 -0.0125 192 VAL B O     
4570 C CB    . VAL B 192 ? 0.1281 0.1426 0.2434 0.0003  -0.0123 -0.0158 192 VAL B CB    
4571 C CG1   . VAL B 192 ? 0.0592 0.0780 0.1713 0.0002  -0.0129 -0.0190 192 VAL B CG1   
4572 C CG2   . VAL B 192 ? 0.0883 0.0984 0.2108 0.0006  -0.0113 -0.0155 192 VAL B CG2   
4573 N N     . VAL B 193 ? 0.2763 0.3009 0.3692 -0.0016 -0.0070 -0.0128 193 VAL B N     
4574 C CA    . VAL B 193 ? 0.1401 0.1691 0.2265 -0.0022 -0.0075 -0.0134 193 VAL B CA    
4575 C C     . VAL B 193 ? 0.2442 0.2753 0.3318 -0.0022 -0.0090 -0.0168 193 VAL B C     
4576 O O     . VAL B 193 ? 0.2525 0.2842 0.3393 -0.0026 -0.0067 -0.0177 193 VAL B O     
4577 C CB    . VAL B 193 ? 0.0276 0.0592 0.1054 -0.0032 -0.0038 -0.0111 193 VAL B CB    
4578 C CG1   . VAL B 193 ? 0.1445 0.1803 0.2161 -0.0040 -0.0041 -0.0115 193 VAL B CG1   
4579 C CG2   . VAL B 193 ? 0.0413 0.0702 0.1181 -0.0029 -0.0027 -0.0080 193 VAL B CG2   
4580 N N     . ALA B 194 ? 0.2973 0.3291 0.3865 -0.0017 -0.0133 -0.0188 194 ALA B N     
4581 C CA    . ALA B 194 ? 0.2341 0.2671 0.3247 -0.0014 -0.0160 -0.0223 194 ALA B CA    
4582 C C     . ALA B 194 ? 0.2323 0.2694 0.3148 -0.0025 -0.0159 -0.0226 194 ALA B C     
4583 O O     . ALA B 194 ? 0.4938 0.5313 0.5736 -0.0025 -0.0193 -0.0226 194 ALA B O     
4584 C CB    . ALA B 194 ? 0.3412 0.3709 0.4386 0.0002  -0.0220 -0.0247 194 ALA B CB    
4585 N N     . ASP B 195 ? 0.1328 0.1723 0.2113 -0.0036 -0.0121 -0.0228 195 ASP B N     
4586 C CA    . ASP B 195 ? 0.0486 0.0910 0.1199 -0.0050 -0.0120 -0.0234 195 ASP B CA    
4587 C C     . ASP B 195 ? 0.2112 0.2531 0.2834 -0.0047 -0.0168 -0.0272 195 ASP B C     
4588 O O     . ASP B 195 ? 0.3295 0.3720 0.4025 -0.0050 -0.0153 -0.0292 195 ASP B O     
4589 C CB    . ASP B 195 ? 0.1173 0.1609 0.1833 -0.0062 -0.0059 -0.0220 195 ASP B CB    
4590 C CG    . ASP B 195 ? 0.0285 0.0741 0.0871 -0.0076 -0.0048 -0.0223 195 ASP B CG    
4591 O OD1   . ASP B 195 ? 0.0679 0.1135 0.1245 -0.0082 -0.0094 -0.0243 195 ASP B OD1   
4592 O OD2   . ASP B 195 ? 0.2572 0.3026 0.3104 -0.0083 -0.0001 -0.0207 195 ASP B OD2   
4593 N N     . GLU B 196 ? 0.0442 0.0840 0.1149 -0.0042 -0.0231 -0.0284 196 GLU B N     
4594 C CA    . GLU B 196 ? 0.0624 0.0989 0.1306 -0.0039 -0.0295 -0.0323 196 GLU B CA    
4595 C C     . GLU B 196 ? 0.2418 0.2756 0.2990 -0.0047 -0.0329 -0.0358 196 GLU B C     
4596 O O     . GLU B 196 ? 0.4936 0.5211 0.5446 -0.0033 -0.0400 -0.0389 196 GLU B O     
4597 C CB    . GLU B 196 ? 0.0589 0.0915 0.1331 -0.0013 -0.0354 -0.0336 196 GLU B CB    
4598 C CG    . GLU B 196 ? 0.0549 0.0874 0.1408 0.0002  -0.0327 -0.0326 196 GLU B CG    
4599 C CD    . GLU B 196 ? 0.0614 0.0891 0.1542 0.0026  -0.0386 -0.0342 196 GLU B CD    
4600 O OE1   . GLU B 196 ? 0.0596 0.0855 0.1606 0.0034  -0.0370 -0.0331 196 GLU B OE1   
4601 O OE2   . GLU B 196 ? 0.1763 0.2009 0.2654 0.0036  -0.0450 -0.0367 196 GLU B OE2   
4602 N N     . ILE B 197 ? 0.2472 0.2842 0.3003 -0.0065 -0.0277 -0.0358 197 ILE B N     
4603 C CA    . ILE B 197 ? 0.3455 0.3779 0.3842 -0.0072 -0.0298 -0.0398 197 ILE B CA    
4604 C C     . ILE B 197 ? 0.3405 0.3631 0.3665 -0.0061 -0.0343 -0.0460 197 ILE B C     
4605 O O     . ILE B 197 ? 0.5722 0.5844 0.5796 -0.0053 -0.0372 -0.0480 197 ILE B O     
4606 C CB    . ILE B 197 ? 0.2032 0.2422 0.2408 -0.0095 -0.0211 -0.0385 197 ILE B CB    
4607 C CG1   . ILE B 197 ? 0.2962 0.3288 0.3148 -0.0101 -0.0215 -0.0414 197 ILE B CG1   
4608 C CG2   . ILE B 197 ? 0.1601 0.2036 0.2021 -0.0105 -0.0150 -0.0406 197 ILE B CG2   
4609 C CD1   . ILE B 197 ? 0.1935 0.2324 0.2075 -0.0129 -0.0111 -0.0412 197 ILE B CD1   
4610 N N     . HIS B 198 ? 0.3433 0.3672 0.3767 -0.0057 -0.0343 -0.0480 198 HIS B N     
4611 C CA    . HIS B 198 ? 0.4177 0.4312 0.4385 -0.0044 -0.0382 -0.0531 198 HIS B CA    
4612 C C     . HIS B 198 ? 0.3562 0.3651 0.3806 -0.0018 -0.0464 -0.0539 198 HIS B C     
4613 O O     . HIS B 198 ? 0.5111 0.5134 0.5299 -0.0005 -0.0497 -0.0576 198 HIS B O     
4614 C CB    . HIS B 198 ? 0.3051 0.3224 0.3310 -0.0056 -0.0330 -0.0554 198 HIS B CB    
4615 C CG    . HIS B 198 ? 0.1062 0.1267 0.1260 -0.0079 -0.0239 -0.0556 198 HIS B CG    
4616 N ND1   . HIS B 198 ? 0.1030 0.1124 0.1003 -0.0076 -0.0207 -0.0578 198 HIS B ND1   
4617 C CD2   . HIS B 198 ? 0.0995 0.1329 0.1319 -0.0103 -0.0158 -0.0527 198 HIS B CD2   
4618 C CE1   . HIS B 198 ? 0.2469 0.2626 0.2436 -0.0098 -0.0108 -0.0563 198 HIS B CE1   
4619 N NE2   . HIS B 198 ? 0.0736 0.1046 0.0920 -0.0120 -0.0080 -0.0542 198 HIS B NE2   
4620 N N     . SER B 199 ? 0.1667 0.1785 0.1993 -0.0009 -0.0493 -0.0506 199 SER B N     
4621 C CA    . SER B 199 ? 0.2440 0.2532 0.2835 0.0017  -0.0557 -0.0513 199 SER B CA    
4622 C C     . SER B 199 ? 0.3116 0.3091 0.3360 0.0041  -0.0627 -0.0554 199 SER B C     
4623 O O     . SER B 199 ? 0.4795 0.4742 0.5092 0.0064  -0.0683 -0.0571 199 SER B O     
4624 C CB    . SER B 199 ? 0.3330 0.3456 0.3810 0.0022  -0.0562 -0.0470 199 SER B CB    
4625 O OG    . SER B 199 ? 0.3384 0.3465 0.3754 0.0026  -0.0588 -0.0462 199 SER B OG    
4626 N N     . ASP B 200 ? 0.3043 0.2940 0.3093 0.0038  -0.0618 -0.0568 200 ASP B N     
4627 C CA    . ASP B 200 ? 0.4511 0.4289 0.4397 0.0064  -0.0673 -0.0594 200 ASP B CA    
4628 C C     . ASP B 200 ? 0.6088 0.5788 0.5846 0.0069  -0.0664 -0.0632 200 ASP B C     
4629 O O     . ASP B 200 ? 0.6379 0.5980 0.6004 0.0095  -0.0707 -0.0653 200 ASP B O     
4630 C CB    . ASP B 200 ? 0.4235 0.3965 0.3979 0.0066  -0.0665 -0.0574 200 ASP B CB    
4631 C CG    . ASP B 200 ? 0.4307 0.4088 0.4159 0.0070  -0.0691 -0.0542 200 ASP B CG    
4632 O OD1   . ASP B 200 ? 0.4179 0.3982 0.4160 0.0085  -0.0737 -0.0545 200 ASP B OD1   
4633 O OD2   . ASP B 200 ? 0.3912 0.3708 0.3721 0.0058  -0.0662 -0.0514 200 ASP B OD2   
4634 N N     . ILE B 201 ? 0.6064 0.5807 0.5858 0.0046  -0.0606 -0.0639 201 ILE B N     
4635 C CA    . ILE B 201 ? 0.5691 0.5364 0.5380 0.0050  -0.0591 -0.0674 201 ILE B CA    
4636 C C     . ILE B 201 ? 0.4948 0.4678 0.4808 0.0052  -0.0614 -0.0692 201 ILE B C     
4637 O O     . ILE B 201 ? 0.6612 0.6423 0.6583 0.0030  -0.0561 -0.0687 201 ILE B O     
4638 C CB    . ILE B 201 ? 0.6158 0.5819 0.5734 0.0026  -0.0498 -0.0669 201 ILE B CB    
4639 C CG1   . ILE B 201 ? 0.5802 0.5390 0.5188 0.0030  -0.0471 -0.0651 201 ILE B CG1   
4640 C CG2   . ILE B 201 ? 0.4812 0.4425 0.4329 0.0026  -0.0473 -0.0701 201 ILE B CG2   
4641 C CD1   . ILE B 201 ? 0.5973 0.5442 0.5168 0.0053  -0.0479 -0.0671 201 ILE B CD1   
4642 N N     . ILE B 202 ? 0.3883 0.3576 0.3774 0.0079  -0.0689 -0.0712 202 ILE B N     
4643 C CA    . ILE B 202 ? 0.4162 0.3906 0.4222 0.0085  -0.0716 -0.0727 202 ILE B CA    
4644 C C     . ILE B 202 ? 0.5333 0.4978 0.5284 0.0107  -0.0758 -0.0770 202 ILE B C     
4645 O O     . ILE B 202 ? 0.6099 0.5649 0.5901 0.0130  -0.0801 -0.0783 202 ILE B O     
4646 C CB    . ILE B 202 ? 0.4443 0.4243 0.4672 0.0101  -0.0766 -0.0707 202 ILE B CB    
4647 C CG1   . ILE B 202 ? 0.3122 0.3004 0.3428 0.0082  -0.0720 -0.0661 202 ILE B CG1   
4648 C CG2   . ILE B 202 ? 0.6291 0.6147 0.6702 0.0108  -0.0778 -0.0717 202 ILE B CG2   
4649 C CD1   . ILE B 202 ? 0.2239 0.2216 0.2646 0.0054  -0.0640 -0.0642 202 ILE B CD1   
4650 N N     . TYR B 203 ? 0.4759 0.4430 0.4788 0.0101  -0.0745 -0.0792 203 TYR B N     
4651 C CA    . TYR B 203 ? 0.5196 0.4776 0.5116 0.0118  -0.0773 -0.0833 203 TYR B CA    
4652 C C     . TYR B 203 ? 0.4830 0.4396 0.4840 0.0150  -0.0863 -0.0853 203 TYR B C     
4653 O O     . TYR B 203 ? 0.3219 0.2847 0.3383 0.0158  -0.0896 -0.0836 203 TYR B O     
4654 C CB    . TYR B 203 ? 0.3994 0.3600 0.3942 0.0097  -0.0712 -0.0847 203 TYR B CB    
4655 C CG    . TYR B 203 ? 0.4633 0.4221 0.4447 0.0072  -0.0624 -0.0834 203 TYR B CG    
4656 C CD1   . TYR B 203 ? 0.3328 0.2863 0.2986 0.0072  -0.0606 -0.0815 203 TYR B CD1   
4657 C CD2   . TYR B 203 ? 0.4441 0.4064 0.4289 0.0050  -0.0554 -0.0839 203 TYR B CD2   
4658 C CE1   . TYR B 203 ? 0.3693 0.3211 0.3234 0.0051  -0.0519 -0.0801 203 TYR B CE1   
4659 C CE2   . TYR B 203 ? 0.2026 0.1629 0.1755 0.0030  -0.0469 -0.0825 203 TYR B CE2   
4660 C CZ    . TYR B 203 ? 0.3422 0.2972 0.2997 0.0030  -0.0450 -0.0806 203 TYR B CZ    
4661 O OH    . TYR B 203 ? 0.4241 0.3773 0.3702 0.0011  -0.0357 -0.0790 203 TYR B OH    
4662 N N     . ALA B 204 ? 0.5411 0.4891 0.5321 0.0169  -0.0898 -0.0892 204 ALA B N     
4663 C CA    . ALA B 204 ? 0.5049 0.4491 0.5000 0.0204  -0.0989 -0.0917 204 ALA B CA    
4664 C C     . ALA B 204 ? 0.6289 0.5826 0.6485 0.0205  -0.1010 -0.0916 204 ALA B C     
4665 O O     . ALA B 204 ? 0.7477 0.7016 0.7762 0.0231  -0.1075 -0.0919 204 ALA B O     
4666 C CB    . ALA B 204 ? 0.4586 0.3922 0.4382 0.0222  -0.1014 -0.0958 204 ALA B CB    
4667 N N     . ASP B 205 ? 0.5484 0.5094 0.5790 0.0182  -0.0954 -0.0913 205 ASP B N     
4668 C CA    . ASP B 205 ? 0.4912 0.4610 0.5447 0.0185  -0.0961 -0.0911 205 ASP B CA    
4669 C C     . ASP B 205 ? 0.3918 0.3722 0.4619 0.0173  -0.0919 -0.0863 205 ASP B C     
4670 O O     . ASP B 205 ? 0.3836 0.3715 0.4720 0.0173  -0.0897 -0.0854 205 ASP B O     
4671 C CB    . ASP B 205 ? 0.6255 0.5975 0.6827 0.0170  -0.0920 -0.0931 205 ASP B CB    
4672 C CG    . ASP B 205 ? 0.7881 0.7490 0.8280 0.0181  -0.0949 -0.0976 205 ASP B CG    
4673 O OD1   . ASP B 205 ? 0.8658 0.8173 0.8892 0.0200  -0.0993 -0.0988 205 ASP B OD1   
4674 O OD2   . ASP B 205 ? 0.8310 0.7926 0.8737 0.0173  -0.0926 -0.0998 205 ASP B OD2   
4675 N N     . HIS B 206 ? 0.3578 0.3386 0.4215 0.0163  -0.0899 -0.0832 206 HIS B N     
4676 C CA    . HIS B 206 ? 0.2953 0.2857 0.3730 0.0149  -0.0847 -0.0785 206 HIS B CA    
4677 C C     . HIS B 206 ? 0.3734 0.3616 0.4471 0.0159  -0.0876 -0.0761 206 HIS B C     
4678 O O     . HIS B 206 ? 0.5229 0.5029 0.5808 0.0170  -0.0920 -0.0776 206 HIS B O     
4679 C CB    . HIS B 206 ? 0.3965 0.3928 0.4729 0.0115  -0.0757 -0.0764 206 HIS B CB    
4680 C CG    . HIS B 206 ? 0.3827 0.3829 0.4665 0.0105  -0.0717 -0.0781 206 HIS B CG    
4681 N ND1   . HIS B 206 ? 0.4280 0.4364 0.5307 0.0107  -0.0679 -0.0761 206 HIS B ND1   
4682 C CD2   . HIS B 206 ? 0.3430 0.3389 0.4166 0.0094  -0.0702 -0.0814 206 HIS B CD2   
4683 C CE1   . HIS B 206 ? 0.3988 0.4090 0.5042 0.0099  -0.0648 -0.0782 206 HIS B CE1   
4684 N NE2   . HIS B 206 ? 0.3699 0.3729 0.4582 0.0089  -0.0661 -0.0815 206 HIS B NE2   
4685 N N     . THR B 207 ? 0.4304 0.4254 0.5176 0.0155  -0.0844 -0.0721 207 THR B N     
4686 C CA    . THR B 207 ? 0.3834 0.3771 0.4690 0.0162  -0.0863 -0.0694 207 THR B CA    
4687 C C     . THR B 207 ? 0.4223 0.4238 0.5151 0.0138  -0.0783 -0.0642 207 THR B C     
4688 O O     . THR B 207 ? 0.4463 0.4531 0.5515 0.0132  -0.0732 -0.0622 207 THR B O     
4689 C CB    . THR B 207 ? 0.2940 0.2846 0.3885 0.0192  -0.0927 -0.0704 207 THR B CB    
4690 O OG1   . THR B 207 ? 0.4085 0.3917 0.4957 0.0216  -0.1002 -0.0752 207 THR B OG1   
4691 C CG2   . THR B 207 ? 0.5064 0.4950 0.5981 0.0198  -0.0945 -0.0678 207 THR B CG2   
4692 N N     . HIS B 208 ? 0.2280 0.2293 0.3114 0.0125  -0.0767 -0.0619 208 HIS B N     
4693 C CA    . HIS B 208 ? 0.1564 0.1645 0.2450 0.0103  -0.0692 -0.0568 208 HIS B CA    
4694 C C     . HIS B 208 ? 0.1834 0.1918 0.2818 0.0114  -0.0695 -0.0541 208 HIS B C     
4695 O O     . HIS B 208 ? 0.3136 0.3170 0.4107 0.0134  -0.0758 -0.0553 208 HIS B O     
4696 C CB    . HIS B 208 ? 0.1592 0.1670 0.2354 0.0086  -0.0675 -0.0553 208 HIS B CB    
4697 C CG    . HIS B 208 ? 0.2103 0.2249 0.2911 0.0064  -0.0601 -0.0499 208 HIS B CG    
4698 N ND1   . HIS B 208 ? 0.1946 0.2153 0.2824 0.0047  -0.0524 -0.0473 208 HIS B ND1   
4699 C CD2   . HIS B 208 ? 0.2448 0.2601 0.3231 0.0057  -0.0589 -0.0464 208 HIS B CD2   
4700 C CE1   . HIS B 208 ? 0.2323 0.2562 0.3221 0.0038  -0.0476 -0.0433 208 HIS B CE1   
4701 N NE2   . HIS B 208 ? 0.2581 0.2793 0.3426 0.0043  -0.0514 -0.0427 208 HIS B NE2   
4702 N N     . THR B 209 ? 0.1899 0.2022 0.2995 0.0111  -0.0637 -0.0518 209 THR B N     
4703 C CA    . THR B 209 ? 0.2878 0.2978 0.4082 0.0126  -0.0642 -0.0506 209 THR B CA    
4704 C C     . THR B 209 ? 0.3724 0.3851 0.4918 0.0108  -0.0581 -0.0464 209 THR B C     
4705 O O     . THR B 209 ? 0.3912 0.4070 0.5138 0.0093  -0.0514 -0.0444 209 THR B O     
4706 C CB    . THR B 209 ? 0.2397 0.2488 0.3726 0.0137  -0.0630 -0.0521 209 THR B CB    
4707 O OG1   . THR B 209 ? 0.3260 0.3327 0.4597 0.0155  -0.0691 -0.0561 209 THR B OG1   
4708 C CG2   . THR B 209 ? 0.1586 0.1638 0.3015 0.0147  -0.0636 -0.0510 209 THR B CG2   
4709 N N     . PRO B 210 ? 0.2401 0.2514 0.3547 0.0108  -0.0602 -0.0448 210 PRO B N     
4710 C CA    . PRO B 210 ? 0.1185 0.1320 0.2328 0.0092  -0.0548 -0.0408 210 PRO B CA    
4711 C C     . PRO B 210 ? 0.0847 0.0963 0.2098 0.0093  -0.0516 -0.0395 210 PRO B C     
4712 O O     . PRO B 210 ? 0.1126 0.1198 0.2462 0.0109  -0.0555 -0.0412 210 PRO B O     
4713 C CB    . PRO B 210 ? 0.1843 0.1948 0.2940 0.0100  -0.0595 -0.0403 210 PRO B CB    
4714 C CG    . PRO B 210 ? 0.2219 0.2299 0.3237 0.0111  -0.0659 -0.0435 210 PRO B CG    
4715 C CD    . PRO B 210 ? 0.3771 0.3842 0.4846 0.0122  -0.0676 -0.0467 210 PRO B CD    
4716 N N     . PHE B 211 ? 0.0698 0.0843 0.1942 0.0074  -0.0446 -0.0364 211 PHE B N     
4717 C CA    . PHE B 211 ? 0.0673 0.0792 0.1996 0.0071  -0.0411 -0.0348 211 PHE B CA    
4718 C C     . PHE B 211 ? 0.2751 0.2825 0.4123 0.0076  -0.0436 -0.0334 211 PHE B C     
4719 O O     . PHE B 211 ? 0.4077 0.4107 0.5540 0.0082  -0.0444 -0.0337 211 PHE B O     
4720 C CB    . PHE B 211 ? 0.0598 0.0751 0.1873 0.0051  -0.0339 -0.0316 211 PHE B CB    
4721 C CG    . PHE B 211 ? 0.0579 0.0705 0.1915 0.0046  -0.0301 -0.0301 211 PHE B CG    
4722 C CD1   . PHE B 211 ? 0.0586 0.0707 0.1966 0.0049  -0.0291 -0.0321 211 PHE B CD1   
4723 C CD2   . PHE B 211 ? 0.0555 0.0661 0.1894 0.0038  -0.0273 -0.0264 211 PHE B CD2   
4724 C CE1   . PHE B 211 ? 0.0573 0.0666 0.2000 0.0043  -0.0256 -0.0304 211 PHE B CE1   
4725 C CE2   . PHE B 211 ? 0.0876 0.0953 0.2259 0.0034  -0.0241 -0.0247 211 PHE B CE2   
4726 C CZ    . PHE B 211 ? 0.0555 0.0624 0.1981 0.0036  -0.0232 -0.0267 211 PHE B CZ    
4727 N N     . ALA B 212 ? 0.2690 0.2772 0.4004 0.0073  -0.0446 -0.0318 212 ALA B N     
4728 C CA    . ALA B 212 ? 0.1382 0.1421 0.2738 0.0076  -0.0468 -0.0303 212 ALA B CA    
4729 C C     . ALA B 212 ? 0.2166 0.2160 0.3572 0.0097  -0.0543 -0.0335 212 ALA B C     
4730 O O     . ALA B 212 ? 0.3660 0.3611 0.5124 0.0101  -0.0565 -0.0328 212 ALA B O     
4731 C CB    . ALA B 212 ? 0.2159 0.2222 0.3435 0.0065  -0.0452 -0.0275 212 ALA B CB    
4732 N N     . SER B 213 ? 0.3520 0.3520 0.4906 0.0111  -0.0584 -0.0370 213 SER B N     
4733 C CA    . SER B 213 ? 0.2867 0.2818 0.4296 0.0135  -0.0661 -0.0404 213 SER B CA    
4734 C C     . SER B 213 ? 0.4278 0.4189 0.5832 0.0143  -0.0669 -0.0417 213 SER B C     
4735 O O     . SER B 213 ? 0.3454 0.3314 0.5070 0.0159  -0.0725 -0.0435 213 SER B O     
4736 C CB    . SER B 213 ? 0.1759 0.1725 0.3119 0.0147  -0.0700 -0.0435 213 SER B CB    
4737 O OG    . SER B 213 ? 0.2955 0.2871 0.4344 0.0173  -0.0778 -0.0469 213 SER B OG    
4738 N N     . LEU B 214 ? 0.4792 0.4720 0.6385 0.0132  -0.0616 -0.0409 214 LEU B N     
4739 C CA    . LEU B 214 ? 0.3860 0.3750 0.5565 0.0138  -0.0622 -0.0423 214 LEU B CA    
4740 C C     . LEU B 214 ? 0.3402 0.3275 0.5155 0.0126  -0.0619 -0.0394 214 LEU B C     
4741 O O     . LEU B 214 ? 0.5064 0.4920 0.6889 0.0133  -0.0653 -0.0407 214 LEU B O     
4742 C CB    . LEU B 214 ? 0.3556 0.3478 0.5267 0.0123  -0.0558 -0.0411 214 LEU B CB    
4743 C CG    . LEU B 214 ? 0.2463 0.2424 0.4121 0.0127  -0.0553 -0.0435 214 LEU B CG    
4744 C CD1   . LEU B 214 ? 0.2226 0.2205 0.3898 0.0113  -0.0491 -0.0425 214 LEU B CD1   
4745 C CD2   . LEU B 214 ? 0.1880 0.1824 0.3564 0.0153  -0.0623 -0.0481 214 LEU B CD2   
4746 N N     . SER B 215 ? 0.2360 0.2240 0.4079 0.0110  -0.0581 -0.0356 215 SER B N     
4747 C CA    . SER B 215 ? 0.2787 0.2657 0.4552 0.0097  -0.0567 -0.0324 215 SER B CA    
4748 C C     . SER B 215 ? 0.3529 0.3394 0.5245 0.0089  -0.0557 -0.0294 215 SER B C     
4749 O O     . SER B 215 ? 0.2593 0.2469 0.4239 0.0087  -0.0542 -0.0288 215 SER B O     
4750 C CB    . SER B 215 ? 0.3763 0.3650 0.5553 0.0081  -0.0508 -0.0298 215 SER B CB    
4751 O OG    . SER B 215 ? 0.4005 0.3889 0.5803 0.0067  -0.0479 -0.0258 215 SER B OG    
4752 N N     . GLU B 216 ? 0.4557 0.4406 0.6316 0.0084  -0.0568 -0.0277 216 GLU B N     
4753 C CA    . GLU B 216 ? 0.4584 0.4431 0.6307 0.0073  -0.0551 -0.0243 216 GLU B CA    
4754 C C     . GLU B 216 ? 0.4992 0.4862 0.6677 0.0055  -0.0481 -0.0202 216 GLU B C     
4755 O O     . GLU B 216 ? 0.4708 0.4585 0.6336 0.0048  -0.0460 -0.0177 216 GLU B O     
4756 C CB    . GLU B 216 ? 0.2985 0.2810 0.4770 0.0072  -0.0579 -0.0236 216 GLU B CB    
4757 C CG    . GLU B 216 ? 0.2848 0.2643 0.4653 0.0090  -0.0652 -0.0270 216 GLU B CG    
4758 C CD    . GLU B 216 ? 0.3848 0.3624 0.5667 0.0085  -0.0671 -0.0253 216 GLU B CD    
4759 O OE1   . GLU B 216 ? 0.3654 0.3400 0.5498 0.0100  -0.0733 -0.0279 216 GLU B OE1   
4760 O OE2   . GLU B 216 ? 0.3956 0.3744 0.5756 0.0069  -0.0627 -0.0214 216 GLU B OE2   
4761 N N     . GLU B 217 ? 0.2971 0.2852 0.4685 0.0050  -0.0448 -0.0195 217 GLU B N     
4762 C CA    . GLU B 217 ? 0.2733 0.2630 0.4410 0.0036  -0.0386 -0.0158 217 GLU B CA    
4763 C C     . GLU B 217 ? 0.3313 0.3232 0.4926 0.0035  -0.0355 -0.0160 217 GLU B C     
4764 O O     . GLU B 217 ? 0.3303 0.3232 0.4857 0.0026  -0.0314 -0.0129 217 GLU B O     
4765 C CB    . GLU B 217 ? 0.1194 0.1090 0.2928 0.0032  -0.0366 -0.0147 217 GLU B CB    
4766 C CG    . GLU B 217 ? 0.2365 0.2269 0.4061 0.0021  -0.0313 -0.0105 217 GLU B CG    
4767 C CD    . GLU B 217 ? 0.5868 0.5774 0.7596 0.0018  -0.0286 -0.0099 217 GLU B CD    
4768 O OE1   . GLU B 217 ? 0.7234 0.7149 0.8916 0.0012  -0.0242 -0.0070 217 GLU B OE1   
4769 O OE2   . GLU B 217 ? 0.7029 0.6927 0.8829 0.0023  -0.0310 -0.0122 217 GLU B OE2   
4770 N N     . LEU B 218 ? 0.2747 0.2671 0.4370 0.0044  -0.0373 -0.0196 218 LEU B N     
4771 C CA    . LEU B 218 ? 0.1430 0.1374 0.2993 0.0043  -0.0346 -0.0202 218 LEU B CA    
4772 C C     . LEU B 218 ? 0.1980 0.1928 0.3482 0.0046  -0.0360 -0.0205 218 LEU B C     
4773 O O     . LEU B 218 ? 0.1278 0.1273 0.2696 0.0038  -0.0324 -0.0193 218 LEU B O     
4774 C CB    . LEU B 218 ? 0.1616 0.1566 0.3204 0.0053  -0.0362 -0.0242 218 LEU B CB    
4775 C CG    . LEU B 218 ? 0.2907 0.2854 0.4562 0.0054  -0.0362 -0.0253 218 LEU B CG    
4776 C CD1   . LEU B 218 ? 0.0724 0.0681 0.2386 0.0066  -0.0384 -0.0297 218 LEU B CD1   
4777 C CD2   . LEU B 218 ? 0.0679 0.0632 0.2333 0.0041  -0.0307 -0.0219 218 LEU B CD2   
4778 N N     . ALA B 219 ? 0.2456 0.2385 0.3975 0.0054  -0.0409 -0.0216 219 ALA B N     
4779 C CA    . ALA B 219 ? 0.3396 0.3355 0.4832 0.0052  -0.0417 -0.0208 219 ALA B CA    
4780 C C     . ALA B 219 ? 0.3629 0.3596 0.5021 0.0038  -0.0372 -0.0164 219 ALA B C     
4781 O O     . ALA B 219 ? 0.3287 0.3297 0.4591 0.0031  -0.0347 -0.0151 219 ALA B O     
4782 C CB    . ALA B 219 ? 0.3067 0.2992 0.4534 0.0065  -0.0483 -0.0229 219 ALA B CB    
4783 N N     . GLU B 220 ? 0.2507 0.2434 0.3956 0.0033  -0.0360 -0.0140 220 GLU B N     
4784 C CA    . GLU B 220 ? 0.2688 0.2622 0.4095 0.0021  -0.0320 -0.0097 220 GLU B CA    
4785 C C     . GLU B 220 ? 0.2866 0.2818 0.4226 0.0014  -0.0265 -0.0076 220 GLU B C     
4786 O O     . GLU B 220 ? 0.0513 0.0469 0.1832 0.0007  -0.0232 -0.0040 220 GLU B O     
4787 C CB    . GLU B 220 ? 0.3597 0.3518 0.5048 0.0017  -0.0321 -0.0075 220 GLU B CB    
4788 C CG    . GLU B 220 ? 0.3564 0.3465 0.5051 0.0022  -0.0370 -0.0088 220 GLU B CG    
4789 C CD    . GLU B 220 ? 0.2724 0.2624 0.4159 0.0018  -0.0374 -0.0072 220 GLU B CD    
4790 O OE1   . GLU B 220 ? 0.2426 0.2317 0.3847 0.0026  -0.0412 -0.0095 220 GLU B OE1   
4791 O OE2   . GLU B 220 ? 0.2003 0.1910 0.3408 0.0009  -0.0339 -0.0036 220 GLU B OE2   
4792 N N     . ARG B 221 ? 0.2319 0.2290 0.3675 0.0017  -0.0255 -0.0097 221 ARG B N     
4793 C CA    . ARG B 221 ? 0.2047 0.2040 0.3349 0.0011  -0.0205 -0.0079 221 ARG B CA    
4794 C C     . ARG B 221 ? 0.0470 0.0521 0.1699 0.0010  -0.0194 -0.0098 221 ARG B C     
4795 O O     . ARG B 221 ? 0.1410 0.1481 0.2589 0.0005  -0.0155 -0.0086 221 ARG B O     
4796 C CB    . ARG B 221 ? 0.1953 0.1927 0.3307 0.0010  -0.0189 -0.0074 221 ARG B CB    
4797 C CG    . ARG B 221 ? 0.2386 0.2358 0.3802 0.0017  -0.0215 -0.0113 221 ARG B CG    
4798 C CD    . ARG B 221 ? 0.2736 0.2706 0.4181 0.0015  -0.0191 -0.0107 221 ARG B CD    
4799 N NE    . ARG B 221 ? 0.0566 0.0523 0.2046 0.0012  -0.0189 -0.0082 221 ARG B NE    
4800 C CZ    . ARG B 221 ? 0.1888 0.1845 0.3334 0.0006  -0.0156 -0.0045 221 ARG B CZ    
4801 N NH1   . ARG B 221 ? 0.0872 0.0839 0.2249 0.0004  -0.0124 -0.0028 221 ARG B NH1   
4802 N NH2   . ARG B 221 ? 0.3385 0.3331 0.4865 0.0004  -0.0156 -0.0026 221 ARG B NH2   
4803 N N     . THR B 222 ? 0.1743 0.1818 0.2957 0.0014  -0.0228 -0.0126 222 THR B N     
4804 C CA    . THR B 222 ? 0.1522 0.1648 0.2675 0.0012  -0.0221 -0.0146 222 THR B CA    
4805 C C     . THR B 222 ? 0.1881 0.2045 0.2954 0.0008  -0.0224 -0.0139 222 THR B C     
4806 O O     . THR B 222 ? 0.0903 0.1053 0.1986 0.0012  -0.0258 -0.0138 222 THR B O     
4807 C CB    . THR B 222 ? 0.0983 0.1105 0.2185 0.0023  -0.0262 -0.0187 222 THR B CB    
4808 O OG1   . THR B 222 ? 0.3161 0.3251 0.4438 0.0026  -0.0255 -0.0194 222 THR B OG1   
4809 C CG2   . THR B 222 ? 0.0489 0.0662 0.1625 0.0020  -0.0257 -0.0206 222 THR B CG2   
4810 N N     . ILE B 223 ? 0.1137 0.1348 0.2133 -0.0001 -0.0189 -0.0132 223 ILE B N     
4811 C CA    . ILE B 223 ? 0.0379 0.0632 0.1296 -0.0008 -0.0188 -0.0127 223 ILE B CA    
4812 C C     . ILE B 223 ? 0.0924 0.1213 0.1811 -0.0009 -0.0198 -0.0155 223 ILE B C     
4813 O O     . ILE B 223 ? 0.1572 0.1885 0.2426 -0.0017 -0.0163 -0.0155 223 ILE B O     
4814 C CB    . ILE B 223 ? 0.3630 0.3902 0.4481 -0.0017 -0.0140 -0.0095 223 ILE B CB    
4815 C CG1   . ILE B 223 ? 0.3547 0.3775 0.4429 -0.0014 -0.0131 -0.0067 223 ILE B CG1   
4816 C CG2   . ILE B 223 ? 0.0309 0.0621 0.1085 -0.0025 -0.0139 -0.0088 223 ILE B CG2   
4817 C CD1   . ILE B 223 ? 0.4257 0.4458 0.5168 -0.0013 -0.0105 -0.0059 223 ILE B CD1   
4818 N N     . THR B 224 ? 0.1119 0.1408 0.2001 -0.0004 -0.0247 -0.0175 224 THR B N     
4819 C CA    . THR B 224 ? 0.0812 0.1119 0.1668 -0.0003 -0.0272 -0.0205 224 THR B CA    
4820 C C     . THR B 224 ? 0.1446 0.1789 0.2208 -0.0016 -0.0267 -0.0197 224 THR B C     
4821 O O     . THR B 224 ? 0.1868 0.2205 0.2602 -0.0016 -0.0289 -0.0187 224 THR B O     
4822 C CB    . THR B 224 ? 0.0527 0.0793 0.1430 0.0015  -0.0341 -0.0236 224 THR B CB    
4823 O OG1   . THR B 224 ? 0.2997 0.3235 0.3986 0.0024  -0.0342 -0.0250 224 THR B OG1   
4824 C CG2   . THR B 224 ? 0.0574 0.0847 0.1416 0.0016  -0.0381 -0.0264 224 THR B CG2   
4825 N N     . CYS B 225 ? 0.3437 0.3814 0.4154 -0.0030 -0.0237 -0.0200 225 CYS B N     
4826 C CA    . CYS B 225 ? 0.0387 0.0792 0.1015 -0.0047 -0.0226 -0.0190 225 CYS B CA    
4827 C C     . CYS B 225 ? 0.0449 0.0839 0.1026 -0.0053 -0.0270 -0.0224 225 CYS B C     
4828 O O     . CYS B 225 ? 0.0716 0.1111 0.1302 -0.0056 -0.0258 -0.0241 225 CYS B O     
4829 C CB    . CYS B 225 ? 0.0870 0.1304 0.1472 -0.0060 -0.0158 -0.0167 225 CYS B CB    
4830 S SG    . CYS B 225 ? 0.3300 0.3724 0.3935 -0.0054 -0.0110 -0.0138 225 CYS B SG    
4831 N N     . MET B 226 ? 0.0514 0.0873 0.1008 -0.0057 -0.0317 -0.0232 226 MET B N     
4832 C CA    . MET B 226 ? 0.0678 0.0980 0.1086 -0.0053 -0.0375 -0.0283 226 MET B CA    
4833 C C     . MET B 226 ? 0.3001 0.3268 0.3276 -0.0060 -0.0384 -0.0297 226 MET B C     
4834 O O     . MET B 226 ? 0.3755 0.4053 0.4026 -0.0072 -0.0355 -0.0260 226 MET B O     
4835 C CB    . MET B 226 ? 0.1740 0.1985 0.2156 -0.0028 -0.0445 -0.0304 226 MET B CB    
4836 C CG    . MET B 226 ? 0.2360 0.2617 0.2897 -0.0013 -0.0447 -0.0306 226 MET B CG    
4837 S SD    . MET B 226 ? 0.2885 0.3095 0.3492 0.0019  -0.0507 -0.0312 226 MET B SD    
4838 C CE    . MET B 226 ? 0.1685 0.1869 0.2371 0.0038  -0.0541 -0.0349 226 MET B CE    
4839 N N     . ALA B 227 ? 0.2855 0.3042 0.2994 -0.0052 -0.0416 -0.0348 227 ALA B N     
4840 C CA    . ALA B 227 ? 0.2108 0.2223 0.2059 -0.0053 -0.0410 -0.0360 227 ALA B CA    
4841 C C     . ALA B 227 ? 0.4038 0.4033 0.3820 -0.0034 -0.0439 -0.0403 227 ALA B C     
4842 O O     . ALA B 227 ? 0.5878 0.5864 0.5690 -0.0030 -0.0448 -0.0431 227 ALA B O     
4843 C CB    . ALA B 227 ? 0.2832 0.3003 0.2771 -0.0076 -0.0333 -0.0352 227 ALA B CB    
4844 N N     . PRO B 228 ? 0.3383 0.3284 0.2989 -0.0021 -0.0447 -0.0404 228 PRO B N     
4845 C CA    . PRO B 228 ? 0.3880 0.3668 0.3310 -0.0003 -0.0446 -0.0433 228 PRO B CA    
4846 C C     . PRO B 228 ? 0.5452 0.5220 0.4763 -0.0020 -0.0357 -0.0434 228 PRO B C     
4847 O O     . PRO B 228 ? 0.6116 0.5801 0.5289 -0.0006 -0.0340 -0.0450 228 PRO B O     
4848 C CB    . PRO B 228 ? 0.2211 0.1925 0.1534 0.0022  -0.0483 -0.0422 228 PRO B CB    
4849 C CG    . PRO B 228 ? 0.1668 0.1446 0.1044 0.0006  -0.0461 -0.0386 228 PRO B CG    
4850 C CD    . PRO B 228 ? 0.2544 0.2441 0.2120 -0.0017 -0.0456 -0.0374 228 PRO B CD    
4851 N N     . SER B 229 ? 0.5320 0.5164 0.4689 -0.0047 -0.0296 -0.0414 229 SER B N     
4852 C CA    . SER B 229 ? 0.4971 0.4797 0.4228 -0.0065 -0.0197 -0.0405 229 SER B CA    
4853 C C     . SER B 229 ? 0.5213 0.5006 0.4430 -0.0066 -0.0165 -0.0433 229 SER B C     
4854 O O     . SER B 229 ? 0.4912 0.4689 0.4037 -0.0051 -0.0117 -0.0440 229 SER B O     
4855 C CB    . SER B 229 ? 0.4064 0.3961 0.3409 -0.0069 -0.0148 -0.0370 229 SER B CB    
4856 O OG    . SER B 229 ? 0.4637 0.4565 0.4009 -0.0073 -0.0171 -0.0343 229 SER B OG    
4857 N N1    . LLP B 230 ? 0.0633 0.0901 0.1007 0.0088  -0.0054 -0.0565 230 LLP B N1    
4858 C C2    . LLP B 230 ? 0.1396 0.1596 0.1683 0.0087  -0.0052 -0.0582 230 LLP B C2    
4859 C "C2'" . LLP B 230 ? 0.1017 0.1223 0.1377 0.0092  -0.0082 -0.0601 230 LLP B "C2'" 
4860 C C3    . LLP B 230 ? 0.2673 0.2787 0.2794 0.0083  -0.0022 -0.0582 230 LLP B C3    
4861 O O3    . LLP B 230 ? 0.2429 0.2471 0.2467 0.0084  -0.0024 -0.0601 230 LLP B O3    
4862 C C4    . LLP B 230 ? 0.1354 0.1457 0.1404 0.0080  0.0007  -0.0562 230 LLP B C4    
4863 C "C4'" . LLP B 230 ? 0.2326 0.2332 0.2196 0.0076  0.0044  -0.0555 230 LLP B "C4'" 
4864 C C5    . LLP B 230 ? 0.2663 0.2844 0.2810 0.0079  0.0007  -0.0544 230 LLP B C5    
4865 C C6    . LLP B 230 ? 0.2236 0.2497 0.2545 0.0084  -0.0027 -0.0548 230 LLP B C6    
4866 C "C5'" . LLP B 230 ? 0.4248 0.4419 0.4321 0.0074  0.0038  -0.0519 230 LLP B "C5'" 
4867 O OP4   . LLP B 230 ? 0.5634 0.5728 0.5606 0.0079  -0.0019 -0.0538 230 LLP B OP4   
4868 P P     . LLP B 230 ? 0.5816 0.5883 0.5695 0.0076  -0.0006 -0.0519 230 LLP B P     
4869 O OP1   . LLP B 230 ? 0.5063 0.5086 0.4838 0.0070  0.0065  -0.0496 230 LLP B OP1   
4870 O OP2   . LLP B 230 ? 0.5848 0.6016 0.5858 0.0076  0.0005  -0.0500 230 LLP B OP2   
4871 O OP3   . LLP B 230 ? 0.4878 0.4855 0.4646 0.0081  -0.0077 -0.0532 230 LLP B OP3   
4872 N N     . LLP B 230 ? 0.5274 0.5098 0.4611 -0.0062 -0.0200 -0.0454 230 LLP B N     
4873 C CA    . LLP B 230 ? 0.4824 0.4609 0.4123 -0.0062 -0.0171 -0.0479 230 LLP B CA    
4874 C CB    . LLP B 230 ? 0.4207 0.4120 0.3722 -0.0066 -0.0174 -0.0495 230 LLP B CB    
4875 C CG    . LLP B 230 ? 0.3858 0.3907 0.3485 -0.0091 -0.0077 -0.0468 230 LLP B CG    
4876 C CD    . LLP B 230 ? 0.3179 0.3203 0.2739 -0.0093 0.0013  -0.0455 230 LLP B CD    
4877 C CE    . LLP B 230 ? 0.2544 0.2697 0.2227 -0.0123 0.0111  -0.0406 230 LLP B CE    
4878 N NZ    . LLP B 230 ? 0.1794 0.2118 0.1713 -0.0153 0.0116  -0.0426 230 LLP B NZ    
4879 C C     . LLP B 230 ? 0.6002 0.5712 0.5226 -0.0041 -0.0229 -0.0512 230 LLP B C     
4880 O O     . LLP B 230 ? 0.7030 0.6688 0.6149 -0.0036 -0.0191 -0.0527 230 LLP B O     
4881 N N     . THR B 231 ? 0.5063 0.4767 0.4347 -0.0021 -0.0322 -0.0517 231 THR B N     
4882 C CA    . THR B 231 ? 0.3469 0.3092 0.2693 0.0008  -0.0387 -0.0544 231 THR B CA    
4883 C C     . THR B 231 ? 0.3636 0.3162 0.2670 0.0028  -0.0369 -0.0540 231 THR B C     
4884 O O     . THR B 231 ? 0.4002 0.3455 0.2943 0.0045  -0.0375 -0.0563 231 THR B O     
4885 C CB    . THR B 231 ? 0.2647 0.2291 0.1983 0.0026  -0.0479 -0.0543 231 THR B CB    
4886 O OG1   . THR B 231 ? 0.3252 0.2997 0.2794 0.0013  -0.0494 -0.0544 231 THR B OG1   
4887 C CG2   . THR B 231 ? 0.3203 0.2753 0.2459 0.0060  -0.0545 -0.0569 231 THR B CG2   
4888 N N     . PHE B 232 ? 0.3119 0.2645 0.2101 0.0029  -0.0350 -0.0509 232 PHE B N     
4889 C CA    . PHE B 232 ? 0.3632 0.3070 0.2456 0.0053  -0.0342 -0.0500 232 PHE B CA    
4890 C C     . PHE B 232 ? 0.3933 0.3390 0.2695 0.0040  -0.0244 -0.0476 232 PHE B C     
4891 O O     . PHE B 232 ? 0.4980 0.4373 0.3625 0.0058  -0.0228 -0.0460 232 PHE B O     
4892 C CB    . PHE B 232 ? 0.3729 0.3146 0.2544 0.0070  -0.0398 -0.0481 232 PHE B CB    
4893 C CG    . PHE B 232 ? 0.2801 0.2200 0.1684 0.0091  -0.0497 -0.0502 232 PHE B CG    
4894 C CD1   . PHE B 232 ? 0.3079 0.2382 0.1871 0.0125  -0.0552 -0.0525 232 PHE B CD1   
4895 C CD2   . PHE B 232 ? 0.3448 0.2931 0.2498 0.0079  -0.0534 -0.0496 232 PHE B CD2   
4896 C CE1   . PHE B 232 ? 0.4330 0.3623 0.3197 0.0146  -0.0641 -0.0544 232 PHE B CE1   
4897 C CE2   . PHE B 232 ? 0.2256 0.1734 0.1392 0.0100  -0.0619 -0.0512 232 PHE B CE2   
4898 C CZ    . PHE B 232 ? 0.2987 0.2370 0.2031 0.0133  -0.0673 -0.0537 232 PHE B CZ    
4899 N N     . ASN B 233 ? 0.4386 0.3933 0.3234 0.0011  -0.0178 -0.0471 233 ASN B N     
4900 C CA    . ASN B 233 ? 0.4386 0.3980 0.3219 0.0007  -0.0087 -0.0446 233 ASN B CA    
4901 C C     . ASN B 233 ? 0.5691 0.5302 0.4507 0.0009  -0.0065 -0.0405 233 ASN B C     
4902 O O     . ASN B 233 ? 0.7076 0.6655 0.5818 0.0021  -0.0027 -0.0380 233 ASN B O     
4903 C CB    . ASN B 233 ? 0.3147 0.2670 0.1875 0.0024  -0.0063 -0.0454 233 ASN B CB    
4904 C CG    . ASN B 233 ? 0.3122 0.2713 0.1891 0.0021  0.0019  -0.0432 233 ASN B CG    
4905 O OD1   . ASN B 233 ? 0.2742 0.2432 0.1627 0.0014  0.0051  -0.0417 233 ASN B OD1   
4906 N ND2   . ASN B 233 ? 0.3414 0.2946 0.2091 0.0034  0.0047  -0.0424 233 ASN B ND2   
4907 N N     . ILE B 234 ? 0.5248 0.4912 0.4143 -0.0003 -0.0091 -0.0396 234 ILE B N     
4908 C CA    . ILE B 234 ? 0.2764 0.2457 0.1663 -0.0003 -0.0071 -0.0358 234 ILE B CA    
4909 C C     . ILE B 234 ? 0.2452 0.2266 0.1485 -0.0014 -0.0035 -0.0341 234 ILE B C     
4910 O O     . ILE B 234 ? 0.3428 0.3279 0.2506 -0.0019 -0.0048 -0.0321 234 ILE B O     
4911 C CB    . ILE B 234 ? 0.2405 0.2031 0.1257 0.0007  -0.0146 -0.0358 234 ILE B CB    
4912 C CG1   . ILE B 234 ? 0.3464 0.3121 0.2418 -0.0003 -0.0215 -0.0376 234 ILE B CG1   
4913 C CG2   . ILE B 234 ? 0.2153 0.1659 0.0873 0.0036  -0.0183 -0.0373 234 ILE B CG2   
4914 C CD1   . ILE B 234 ? 0.4283 0.3922 0.3249 0.0009  -0.0280 -0.0362 234 ILE B CD1   
4915 N N     . ALA B 235 ? 0.2731 0.2587 0.1823 -0.0002 0.0004  -0.0340 235 ALA B N     
4916 C CA    . ALA B 235 ? 0.2761 0.2643 0.1943 -0.0001 0.0040  -0.0298 235 ALA B CA    
4917 C C     . ALA B 235 ? 0.4304 0.4223 0.3519 0.0000  0.0097  -0.0238 235 ALA B C     
4918 O O     . ALA B 235 ? 0.5498 0.5462 0.4820 -0.0027 0.0129  -0.0202 235 ALA B O     
4919 C CB    . ALA B 235 ? 0.1988 0.1881 0.1227 -0.0020 0.0083  -0.0297 235 ALA B CB    
4920 N N     . GLY B 236 ? 0.3340 0.3257 0.2493 0.0012  0.0109  -0.0232 236 GLY B N     
4921 C CA    . GLY B 236 ? 0.3740 0.3653 0.2901 -0.0004 0.0150  -0.0188 236 GLY B CA    
4922 C C     . GLY B 236 ? 0.3852 0.3774 0.3000 0.0001  0.0114  -0.0186 236 GLY B C     
4923 O O     . GLY B 236 ? 0.4324 0.4243 0.3484 -0.0010 0.0142  -0.0152 236 GLY B O     
4924 N N     . LEU B 237 ? 0.3417 0.3336 0.2539 0.0005  0.0050  -0.0224 237 LEU B N     
4925 C CA    . LEU B 237 ? 0.3505 0.3422 0.2615 -0.0003 0.0012  -0.0221 237 LEU B CA    
4926 C C     . LEU B 237 ? 0.3490 0.3440 0.2689 0.0000  -0.0011 -0.0211 237 LEU B C     
4927 O O     . LEU B 237 ? 0.4399 0.4363 0.3611 -0.0004 -0.0040 -0.0201 237 LEU B O     
4928 C CB    . LEU B 237 ? 0.2576 0.2397 0.1580 -0.0012 -0.0051 -0.0251 237 LEU B CB    
4929 C CG    . LEU B 237 ? 0.3060 0.2791 0.1945 0.0002  -0.0034 -0.0255 237 LEU B CG    
4930 C CD1   . LEU B 237 ? 0.2895 0.2513 0.1668 0.0019  -0.0096 -0.0266 237 LEU B CD1   
4931 C CD2   . LEU B 237 ? 0.3473 0.3207 0.2345 0.0004  0.0034  -0.0218 237 LEU B CD2   
4932 N N     . GLN B 238 ? 0.2694 0.2634 0.1948 -0.0017 0.0002  -0.0210 238 GLN B N     
4933 C CA    . GLN B 238 ? 0.2719 0.2751 0.2117 -0.0071 0.0008  -0.0195 238 GLN B CA    
4934 C C     . GLN B 238 ? 0.2854 0.2896 0.2276 -0.0075 -0.0088 -0.0215 238 GLN B C     
4935 O O     . GLN B 238 ? 0.2445 0.2540 0.1928 -0.0084 -0.0094 -0.0190 238 GLN B O     
4936 C CB    . GLN B 238 ? 0.0797 0.0882 0.0280 -0.0081 0.0076  -0.0142 238 GLN B CB    
4937 C CG    . GLN B 238 ? 0.1717 0.1815 0.1263 -0.0076 0.0137  -0.0115 238 GLN B CG    
4938 C CD    . GLN B 238 ? 0.2823 0.2943 0.2419 -0.0094 0.0171  -0.0085 238 GLN B CD    
4939 O OE1   . GLN B 238 ? 0.3490 0.3580 0.3034 -0.0082 0.0163  -0.0074 238 GLN B OE1   
4940 N NE2   . GLN B 238 ? 0.2746 0.2904 0.2430 -0.0119 0.0195  -0.0080 238 GLN B NE2   
4941 N N     . ALA B 239 ? 0.3321 0.3306 0.2717 -0.0069 -0.0169 -0.0254 239 ALA B N     
4942 C CA    . ALA B 239 ? 0.2219 0.2245 0.1717 -0.0083 -0.0256 -0.0257 239 ALA B CA    
4943 C C     . ALA B 239 ? 0.3169 0.3295 0.2870 -0.0085 -0.0283 -0.0271 239 ALA B C     
4944 O O     . ALA B 239 ? 0.3547 0.3663 0.3242 -0.0083 -0.0273 -0.0302 239 ALA B O     
4945 C CB    . ALA B 239 ? 0.1151 0.1103 0.0557 -0.0059 -0.0305 -0.0280 239 ALA B CB    
4946 N N     . SER B 240 ? 0.2843 0.3058 0.2725 -0.0091 -0.0303 -0.0237 240 SER B N     
4947 C CA    . SER B 240 ? 0.1352 0.1637 0.1415 -0.0094 -0.0306 -0.0226 240 SER B CA    
4948 C C     . SER B 240 ? 0.1029 0.1335 0.1182 -0.0091 -0.0330 -0.0185 240 SER B C     
4949 O O     . SER B 240 ? 0.2068 0.2382 0.2207 -0.0096 -0.0325 -0.0155 240 SER B O     
4950 C CB    . SER B 240 ? 0.1218 0.1597 0.1400 -0.0105 -0.0225 -0.0204 240 SER B CB    
4951 O OG    . SER B 240 ? 0.2064 0.2454 0.2163 -0.0114 -0.0185 -0.0253 240 SER B OG    
4952 N N     . ILE B 241 ? 0.3743 0.4058 0.3979 -0.0080 -0.0346 -0.0189 241 ILE B N     
4953 C CA    . ILE B 241 ? 0.3632 0.3950 0.3946 -0.0060 -0.0367 -0.0178 241 ILE B CA    
4954 C C     . ILE B 241 ? 0.4600 0.4952 0.5043 -0.0051 -0.0336 -0.0170 241 ILE B C     
4955 O O     . ILE B 241 ? 0.4985 0.5331 0.5458 -0.0046 -0.0342 -0.0193 241 ILE B O     
4956 C CB    . ILE B 241 ? 0.2598 0.2841 0.2868 -0.0037 -0.0441 -0.0214 241 ILE B CB    
4957 C CG1   . ILE B 241 ? 0.2556 0.2730 0.2677 -0.0031 -0.0477 -0.0231 241 ILE B CG1   
4958 C CG2   . ILE B 241 ? 0.1595 0.1823 0.1972 -0.0011 -0.0472 -0.0213 241 ILE B CG2   
4959 C CD1   . ILE B 241 ? 0.1290 0.1370 0.1313 -0.0007 -0.0534 -0.0278 241 ILE B CD1   
4960 N N     . ILE B 242 ? 0.3783 0.4155 0.4285 -0.0047 -0.0302 -0.0143 242 ILE B N     
4961 C CA    . ILE B 242 ? 0.2073 0.2446 0.2664 -0.0038 -0.0273 -0.0137 242 ILE B CA    
4962 C C     . ILE B 242 ? 0.3480 0.3806 0.4131 -0.0019 -0.0314 -0.0142 242 ILE B C     
4963 O O     . ILE B 242 ? 0.3722 0.4037 0.4357 -0.0018 -0.0326 -0.0129 242 ILE B O     
4964 C CB    . ILE B 242 ? 0.0705 0.1110 0.1289 -0.0048 -0.0207 -0.0103 242 ILE B CB    
4965 C CG1   . ILE B 242 ? 0.0436 0.0876 0.0947 -0.0068 -0.0175 -0.0088 242 ILE B CG1   
4966 C CG2   . ILE B 242 ? 0.0462 0.0855 0.1101 -0.0042 -0.0178 -0.0103 242 ILE B CG2   
4967 C CD1   . ILE B 242 ? 0.0405 0.0848 0.0903 -0.0074 -0.0175 -0.0109 242 ILE B CD1   
4968 N N     . ILE B 243 ? 0.4637 0.4932 0.5361 -0.0006 -0.0335 -0.0162 243 ILE B N     
4969 C CA    . ILE B 243 ? 0.0539 0.0780 0.1330 0.0010  -0.0379 -0.0170 243 ILE B CA    
4970 C C     . ILE B 243 ? 0.0503 0.0730 0.1368 0.0009  -0.0343 -0.0152 243 ILE B C     
4971 O O     . ILE B 243 ? 0.2546 0.2782 0.3438 0.0007  -0.0314 -0.0156 243 ILE B O     
4972 C CB    . ILE B 243 ? 0.0622 0.0826 0.1432 0.0026  -0.0441 -0.0208 243 ILE B CB    
4973 C CG1   . ILE B 243 ? 0.0676 0.0878 0.1384 0.0027  -0.0479 -0.0223 243 ILE B CG1   
4974 C CG2   . ILE B 243 ? 0.4177 0.4324 0.5061 0.0043  -0.0487 -0.0217 243 ILE B CG2   
4975 C CD1   . ILE B 243 ? 0.0764 0.0930 0.1456 0.0041  -0.0535 -0.0261 243 ILE B CD1   
4976 N N     . ILE B 244 ? 0.0502 0.0702 0.1390 0.0009  -0.0342 -0.0131 244 ILE B N     
4977 C CA    . ILE B 244 ? 0.0641 0.0816 0.1585 0.0007  -0.0311 -0.0110 244 ILE B CA    
4978 C C     . ILE B 244 ? 0.0806 0.0925 0.1820 0.0015  -0.0350 -0.0110 244 ILE B C     
4979 O O     . ILE B 244 ? 0.1010 0.1118 0.2009 0.0011  -0.0351 -0.0090 244 ILE B O     
4980 C CB    . ILE B 244 ? 0.1045 0.1245 0.1935 -0.0005 -0.0257 -0.0074 244 ILE B CB    
4981 C CG1   . ILE B 244 ? 0.0936 0.1195 0.1746 -0.0014 -0.0226 -0.0075 244 ILE B CG1   
4982 C CG2   . ILE B 244 ? 0.0400 0.0568 0.1332 -0.0006 -0.0225 -0.0052 244 ILE B CG2   
4983 C CD1   . ILE B 244 ? 0.0322 0.0600 0.1079 -0.0023 -0.0175 -0.0046 244 ILE B CD1   
4984 N N     . PRO B 245 ? 0.0756 0.0835 0.1849 0.0025  -0.0382 -0.0132 245 PRO B N     
4985 C CA    . PRO B 245 ? 0.1171 0.1194 0.2335 0.0031  -0.0421 -0.0133 245 PRO B CA    
4986 C C     . PRO B 245 ? 0.0592 0.0593 0.1784 0.0021  -0.0388 -0.0096 245 PRO B C     
4987 O O     . PRO B 245 ? 0.1110 0.1077 0.2328 0.0022  -0.0413 -0.0087 245 PRO B O     
4988 C CB    . PRO B 245 ? 0.2149 0.2141 0.3394 0.0043  -0.0452 -0.0163 245 PRO B CB    
4989 C CG    . PRO B 245 ? 0.1015 0.1047 0.2214 0.0046  -0.0451 -0.0187 245 PRO B CG    
4990 C CD    . PRO B 245 ? 0.0589 0.0674 0.1709 0.0032  -0.0392 -0.0161 245 PRO B CD    
4991 N N     . ASN B 246 ? 0.0546 0.0556 0.1733 0.0014  -0.0337 -0.0074 246 ASN B N     
4992 C CA    . ASN B 246 ? 0.0526 0.0508 0.1730 0.0006  -0.0309 -0.0037 246 ASN B CA    
4993 C C     . ASN B 246 ? 0.4035 0.4042 0.5161 -0.0001 -0.0290 -0.0012 246 ASN B C     
4994 O O     . ASN B 246 ? 0.4773 0.4825 0.5821 -0.0005 -0.0259 -0.0006 246 ASN B O     
4995 C CB    . ASN B 246 ? 0.0497 0.0476 0.1710 0.0003  -0.0266 -0.0022 246 ASN B CB    
4996 C CG    . ASN B 246 ? 0.2053 0.2007 0.3270 -0.0003 -0.0237 0.0018  246 ASN B CG    
4997 O OD1   . ASN B 246 ? 0.2415 0.2366 0.3610 -0.0007 -0.0239 0.0038  246 ASN B OD1   
4998 N ND2   . ASN B 246 ? 0.2139 0.2098 0.3359 -0.0005 -0.0206 0.0029  246 ASN B ND2   
4999 N N     . GLU B 247 ? 0.4994 0.4968 0.6144 -0.0003 -0.0309 0.0002  247 GLU B N     
5000 C CA    . GLU B 247 ? 0.5013 0.5005 0.6097 -0.0009 -0.0294 0.0026  247 GLU B CA    
5001 C C     . GLU B 247 ? 0.2876 0.2879 0.3913 -0.0015 -0.0241 0.0060  247 GLU B C     
5002 O O     . GLU B 247 ? 0.2503 0.2542 0.3461 -0.0019 -0.0218 0.0071  247 GLU B O     
5003 C CB    . GLU B 247 ? 0.4273 0.4222 0.5403 -0.0010 -0.0326 0.0034  247 GLU B CB    
5004 C CG    . GLU B 247 ? 0.3677 0.3636 0.4752 -0.0018 -0.0308 0.0063  247 GLU B CG    
5005 C CD    . GLU B 247 ? 0.4073 0.3991 0.5193 -0.0019 -0.0343 0.0067  247 GLU B CD    
5006 O OE1   . GLU B 247 ? 0.2595 0.2527 0.3676 -0.0019 -0.0364 0.0061  247 GLU B OE1   
5007 O OE2   . GLU B 247 ? 0.5386 0.5290 0.6557 -0.0020 -0.0343 0.0073  247 GLU B OE2   
5008 N N     . LYS B 248 ? 0.1025 0.0994 0.2109 -0.0015 -0.0223 0.0076  248 LYS B N     
5009 C CA    . LYS B 248 ? 0.0401 0.0379 0.1430 -0.0018 -0.0178 0.0108  248 LYS B CA    
5010 C C     . LYS B 248 ? 0.2959 0.2969 0.3930 -0.0017 -0.0151 0.0103  248 LYS B C     
5011 O O     . LYS B 248 ? 0.3923 0.3947 0.4826 -0.0018 -0.0122 0.0125  248 LYS B O     
5012 C CB    . LYS B 248 ? 0.3101 0.3073 0.4157 -0.0017 -0.0165 0.0117  248 LYS B CB    
5013 C CG    . LYS B 248 ? 0.3395 0.3377 0.4385 -0.0018 -0.0128 0.0146  248 LYS B CG    
5014 C CD    . LYS B 248 ? 0.3067 0.3043 0.4085 -0.0017 -0.0118 0.0153  248 LYS B CD    
5015 C CE    . LYS B 248 ? 0.1910 0.1894 0.2856 -0.0015 -0.0086 0.0176  248 LYS B CE    
5016 N NZ    . LYS B 248 ? 0.3672 0.3666 0.4575 -0.0012 -0.0067 0.0175  248 LYS B NZ    
5017 N N     . LEU B 249 ? 0.1924 0.1954 0.2913 -0.0014 -0.0159 0.0072  249 LEU B N     
5018 C CA    . LEU B 249 ? 0.1518 0.1594 0.2442 -0.0014 -0.0134 0.0062  249 LEU B CA    
5019 C C     . LEU B 249 ? 0.2520 0.2646 0.3376 -0.0017 -0.0138 0.0050  249 LEU B C     
5020 O O     . LEU B 249 ? 0.1756 0.1917 0.2539 -0.0020 -0.0111 0.0055  249 LEU B O     
5021 C CB    . LEU B 249 ? 0.2852 0.2931 0.3820 -0.0011 -0.0140 0.0034  249 LEU B CB    
5022 C CG    . LEU B 249 ? 0.3617 0.3648 0.4661 -0.0008 -0.0136 0.0043  249 LEU B CG    
5023 C CD1   . LEU B 249 ? 0.0400 0.0429 0.1500 -0.0004 -0.0149 0.0011  249 LEU B CD1   
5024 C CD2   . LEU B 249 ? 0.4473 0.4489 0.5483 -0.0008 -0.0099 0.0076  249 LEU B CD2   
5025 N N     . ARG B 250 ? 0.3917 0.4043 0.4795 -0.0017 -0.0174 0.0034  250 ARG B N     
5026 C CA    . ARG B 250 ? 0.2433 0.2605 0.3249 -0.0020 -0.0182 0.0022  250 ARG B CA    
5027 C C     . ARG B 250 ? 0.1807 0.1993 0.2554 -0.0025 -0.0155 0.0049  250 ARG B C     
5028 O O     . ARG B 250 ? 0.1341 0.1572 0.2021 -0.0029 -0.0139 0.0045  250 ARG B O     
5029 C CB    . ARG B 250 ? 0.1182 0.1340 0.2034 -0.0015 -0.0233 0.0003  250 ARG B CB    
5030 C CG    . ARG B 250 ? 0.1939 0.2141 0.2735 -0.0016 -0.0249 -0.0018 250 ARG B CG    
5031 C CD    . ARG B 250 ? 0.1666 0.1845 0.2500 -0.0007 -0.0309 -0.0048 250 ARG B CD    
5032 N NE    . ARG B 250 ? 0.1779 0.1913 0.2648 -0.0002 -0.0344 -0.0043 250 ARG B NE    
5033 C CZ    . ARG B 250 ? 0.3600 0.3683 0.4552 0.0004  -0.0369 -0.0048 250 ARG B CZ    
5034 N NH1   . ARG B 250 ? 0.1596 0.1665 0.2603 0.0007  -0.0363 -0.0057 250 ARG B NH1   
5035 N NH2   . ARG B 250 ? 0.4148 0.4192 0.5129 0.0006  -0.0401 -0.0042 250 ARG B NH2   
5036 N N     . HIS B 251 ? 0.1931 0.2077 0.2698 -0.0025 -0.0150 0.0077  251 HIS B N     
5037 C CA    . HIS B 251 ? 0.2482 0.2633 0.3187 -0.0028 -0.0128 0.0104  251 HIS B CA    
5038 C C     . HIS B 251 ? 0.2989 0.3151 0.3637 -0.0027 -0.0091 0.0116  251 HIS B C     
5039 O O     . HIS B 251 ? 0.2995 0.3177 0.3573 -0.0028 -0.0074 0.0125  251 HIS B O     
5040 C CB    . HIS B 251 ? 0.1575 0.1674 0.2318 -0.0028 -0.0136 0.0131  251 HIS B CB    
5041 C CG    . HIS B 251 ? 0.1486 0.1571 0.2277 -0.0030 -0.0175 0.0119  251 HIS B CG    
5042 N ND1   . HIS B 251 ? 0.1689 0.1725 0.2535 -0.0031 -0.0190 0.0137  251 HIS B ND1   
5043 C CD2   . HIS B 251 ? 0.0352 0.0461 0.1143 -0.0029 -0.0207 0.0091  251 HIS B CD2   
5044 C CE1   . HIS B 251 ? 0.1314 0.1344 0.2192 -0.0031 -0.0230 0.0118  251 HIS B CE1   
5045 N NE2   . HIS B 251 ? 0.1714 0.1785 0.2557 -0.0028 -0.0242 0.0090  251 HIS B NE2   
5046 N N     . ALA B 252 ? 0.2801 0.2946 0.3478 -0.0023 -0.0081 0.0117  252 ALA B N     
5047 C CA    . ALA B 252 ? 0.1625 0.1777 0.2248 -0.0020 -0.0052 0.0127  252 ALA B CA    
5048 C C     . ALA B 252 ? 0.2643 0.2848 0.3217 -0.0024 -0.0043 0.0099  252 ALA B C     
5049 O O     . ALA B 252 ? 0.2462 0.2679 0.2974 -0.0023 -0.0024 0.0104  252 ALA B O     
5050 C CB    . ALA B 252 ? 0.1270 0.1385 0.1939 -0.0015 -0.0045 0.0137  252 ALA B CB    
5051 N N     . PHE B 253 ? 0.2435 0.2667 0.3038 -0.0027 -0.0059 0.0071  253 PHE B N     
5052 C CA    . PHE B 253 ? 0.2278 0.2563 0.2833 -0.0033 -0.0052 0.0047  253 PHE B CA    
5053 C C     . PHE B 253 ? 0.3103 0.3415 0.3599 -0.0038 -0.0049 0.0047  253 PHE B C     
5054 O O     . PHE B 253 ? 0.6431 0.6768 0.6868 -0.0042 -0.0030 0.0038  253 PHE B O     
5055 C CB    . PHE B 253 ? 0.2085 0.2387 0.2687 -0.0034 -0.0076 0.0020  253 PHE B CB    
5056 C CG    . PHE B 253 ? 0.1594 0.1950 0.2150 -0.0042 -0.0070 0.0000  253 PHE B CG    
5057 C CD1   . PHE B 253 ? 0.1293 0.1684 0.1812 -0.0049 -0.0082 -0.0006 253 PHE B CD1   
5058 C CD2   . PHE B 253 ? 0.1856 0.2225 0.2407 -0.0044 -0.0054 -0.0010 253 PHE B CD2   
5059 C CE1   . PHE B 253 ? 0.0745 0.1181 0.1224 -0.0060 -0.0078 -0.0015 253 PHE B CE1   
5060 C CE2   . PHE B 253 ? 0.0631 0.1043 0.1144 -0.0054 -0.0049 -0.0020 253 PHE B CE2   
5061 C CZ    . PHE B 253 ? 0.0798 0.1240 0.1277 -0.0063 -0.0061 -0.0017 253 PHE B CZ    
5062 N N     . THR B 254 ? 0.2241 0.2541 0.2757 -0.0037 -0.0071 0.0054  254 THR B N     
5063 C CA    . THR B 254 ? 0.1716 0.2036 0.2181 -0.0042 -0.0070 0.0053  254 THR B CA    
5064 C C     . THR B 254 ? 0.1671 0.1966 0.2084 -0.0039 -0.0047 0.0079  254 THR B C     
5065 O O     . THR B 254 ? 0.0429 0.0735 0.0787 -0.0042 -0.0037 0.0078  254 THR B O     
5066 C CB    . THR B 254 ? 0.2353 0.2663 0.2855 -0.0041 -0.0104 0.0055  254 THR B CB    
5067 O OG1   . THR B 254 ? 0.2983 0.3241 0.3535 -0.0037 -0.0113 0.0077  254 THR B OG1   
5068 C CG2   . THR B 254 ? 0.2901 0.3229 0.3438 -0.0041 -0.0138 0.0027  254 THR B CG2   
5069 N N     . ALA B 255 ? 0.2592 0.2848 0.3021 -0.0033 -0.0040 0.0106  255 ALA B N     
5070 C CA    . ALA B 255 ? 0.1070 0.1304 0.1444 -0.0028 -0.0025 0.0133  255 ALA B CA    
5071 C C     . ALA B 255 ? 0.2030 0.2280 0.2353 -0.0027 -0.0009 0.0120  255 ALA B C     
5072 O O     . ALA B 255 ? 0.4281 0.4528 0.4543 -0.0025 -0.0004 0.0132  255 ALA B O     
5073 C CB    . ALA B 255 ? 0.0168 0.0356 0.0575 -0.0021 -0.0024 0.0163  255 ALA B CB    
5074 N N     . ILE B 256 ? 0.1129 0.1395 0.1479 -0.0029 -0.0004 0.0098  256 ILE B N     
5075 C CA    . ILE B 256 ? 0.0132 0.0411 0.0444 -0.0030 0.0010  0.0082  256 ILE B CA    
5076 C C     . ILE B 256 ? 0.0126 0.0426 0.0402 -0.0037 0.0012  0.0063  256 ILE B C     
5077 O O     . ILE B 256 ? 0.3408 0.3705 0.3632 -0.0037 0.0018  0.0066  256 ILE B O     
5078 C CB    . ILE B 256 ? 0.3115 0.3404 0.3465 -0.0032 0.0015  0.0065  256 ILE B CB    
5079 C CG1   . ILE B 256 ? 0.2496 0.2747 0.2885 -0.0023 0.0013  0.0092  256 ILE B CG1   
5080 C CG2   . ILE B 256 ? 0.2038 0.2336 0.2353 -0.0035 0.0029  0.0047  256 ILE B CG2   
5081 C CD1   . ILE B 256 ? 0.2194 0.2413 0.2548 -0.0014 0.0016  0.0122  256 ILE B CD1   
5082 N N     . GLN B 257 ? 0.0128 0.0449 0.0434 -0.0044 0.0003  0.0044  257 GLN B N     
5083 C CA    . GLN B 257 ? 0.0129 0.0459 0.0393 -0.0049 0.0003  0.0042  257 GLN B CA    
5084 C C     . GLN B 257 ? 0.0913 0.1234 0.1109 -0.0047 0.0001  0.0069  257 GLN B C     
5085 O O     . GLN B 257 ? 0.1910 0.2237 0.2036 -0.0050 0.0003  0.0069  257 GLN B O     
5086 C CB    . GLN B 257 ? 0.0134 0.0485 0.0453 -0.0054 -0.0015 0.0020  257 GLN B CB    
5087 C CG    . GLN B 257 ? 0.2064 0.2425 0.2444 -0.0054 -0.0024 -0.0011 257 GLN B CG    
5088 C CD    . GLN B 257 ? 0.0853 0.1227 0.1256 -0.0052 -0.0057 -0.0035 257 GLN B CD    
5089 O OE1   . GLN B 257 ? 0.2504 0.2926 0.2896 -0.0055 -0.0076 -0.0025 257 GLN B OE1   
5090 N NE2   . GLN B 257 ? 0.0173 0.0543 0.0583 -0.0062 -0.0076 -0.0008 257 GLN B NE2   
5091 N N     . TYR B 258 ? 0.2628 0.2935 0.2842 -0.0043 -0.0007 0.0088  258 TYR B N     
5092 C CA    . TYR B 258 ? 0.3565 0.3862 0.3724 -0.0041 -0.0011 0.0114  258 TYR B CA    
5093 C C     . TYR B 258 ? 0.2992 0.3278 0.3091 -0.0032 -0.0010 0.0129  258 TYR B C     
5094 O O     . TYR B 258 ? 0.3529 0.3812 0.3579 -0.0031 -0.0014 0.0128  258 TYR B O     
5095 C CB    . TYR B 258 ? 0.2280 0.2559 0.2482 -0.0039 -0.0021 0.0133  258 TYR B CB    
5096 C CG    . TYR B 258 ? 0.1029 0.1296 0.1179 -0.0038 -0.0023 0.0160  258 TYR B CG    
5097 C CD1   . TYR B 258 ? 0.0139 0.0424 0.0264 -0.0047 -0.0027 0.0155  258 TYR B CD1   
5098 C CD2   . TYR B 258 ? 0.0133 0.0372 0.0263 -0.0029 -0.0022 0.0182  258 TYR B CD2   
5099 C CE1   . TYR B 258 ? 0.0139 0.0407 0.0226 -0.0044 -0.0026 0.0165  258 TYR B CE1   
5100 C CE2   . TYR B 258 ? 0.0434 0.0649 0.0535 -0.0026 -0.0020 0.0164  258 TYR B CE2   
5101 C CZ    . TYR B 258 ? 0.0136 0.0363 0.0218 -0.0033 -0.0022 0.0157  258 TYR B CZ    
5102 O OH    . TYR B 258 ? 0.1916 0.2114 0.1976 -0.0028 -0.0020 0.0142  258 TYR B OH    
5103 N N     . ARG B 259 ? 0.2442 0.2712 0.2560 -0.0025 -0.0006 0.0135  259 ARG B N     
5104 C CA    . ARG B 259 ? 0.1953 0.2214 0.2035 -0.0016 -0.0008 0.0145  259 ARG B CA    
5105 C C     . ARG B 259 ? 0.3331 0.3611 0.3385 -0.0021 -0.0008 0.0120  259 ARG B C     
5106 O O     . ARG B 259 ? 0.0110 0.0378 0.0156 -0.0016 -0.0007 0.0115  259 ARG B O     
5107 C CB    . ARG B 259 ? 0.0626 0.0863 0.0744 -0.0009 -0.0004 0.0158  259 ARG B CB    
5108 C CG    . ARG B 259 ? 0.1377 0.1621 0.1524 -0.0012 0.0006  0.0136  259 ARG B CG    
5109 C CD    . ARG B 259 ? 0.1569 0.1788 0.1743 -0.0004 0.0009  0.0155  259 ARG B CD    
5110 N NE    . ARG B 259 ? 0.0121 0.0346 0.0318 -0.0006 0.0018  0.0136  259 ARG B NE    
5111 C CZ    . ARG B 259 ? 0.2750 0.2955 0.2968 0.0001  0.0021  0.0150  259 ARG B CZ    
5112 N NH1   . ARG B 259 ? 0.2303 0.2478 0.2525 0.0010  0.0017  0.0182  259 ARG B NH1   
5113 N NH2   . ARG B 259 ? 0.4696 0.4909 0.4933 -0.0002 0.0030  0.0132  259 ARG B NH2   
5114 N N     . GLN B 260 ? 0.4712 0.5011 0.4772 -0.0031 -0.0002 0.0096  260 GLN B N     
5115 C CA    . GLN B 260 ? 0.3224 0.3539 0.3262 -0.0039 0.0000  0.0072  260 GLN B CA    
5116 C C     . GLN B 260 ? 0.3904 0.4238 0.3909 -0.0048 -0.0009 0.0063  260 GLN B C     
5117 O O     . GLN B 260 ? 0.0595 0.0942 0.0593 -0.0060 -0.0005 0.0040  260 GLN B O     
5118 C CB    . GLN B 260 ? 0.0128 0.0447 0.0198 -0.0046 0.0013  0.0052  260 GLN B CB    
5119 C CG    . GLN B 260 ? 0.0124 0.0426 0.0235 -0.0039 0.0022  0.0057  260 GLN B CG    
5120 C CD    . GLN B 260 ? 0.0274 0.0581 0.0427 -0.0044 0.0035  0.0038  260 GLN B CD    
5121 O OE1   . GLN B 260 ? 0.0136 0.0457 0.0282 -0.0053 0.0038  0.0023  260 GLN B OE1   
5122 N NE2   . GLN B 260 ? 0.1202 0.1496 0.1394 -0.0039 0.0043  0.0040  260 GLN B NE2   
5123 N N     . GLY B 261 ? 0.0126 0.0439 0.0132 -0.0044 -0.0011 0.0072  261 GLY B N     
5124 C CA    . GLY B 261 ? 0.0132 0.0435 0.0126 -0.0048 -0.0013 0.0060  261 GLY B CA    
5125 C C     . GLY B 261 ? 0.0141 0.0467 0.0129 -0.0060 -0.0012 0.0049  261 GLY B C     
5126 O O     . GLY B 261 ? 0.0148 0.0470 0.0129 -0.0066 -0.0013 0.0040  261 GLY B O     
5127 N N     . PHE B 262 ? 0.0559 0.0915 0.0553 -0.0066 -0.0010 0.0051  262 PHE B N     
5128 C CA    . PHE B 262 ? 0.0575 0.0955 0.0563 -0.0078 -0.0008 0.0039  262 PHE B CA    
5129 C C     . PHE B 262 ? 0.3391 0.3773 0.3394 -0.0079 -0.0010 0.0055  262 PHE B C     
5130 O O     . PHE B 262 ? 0.2506 0.2873 0.2564 -0.0071 -0.0014 0.0070  262 PHE B O     
5131 C CB    . PHE B 262 ? 0.0732 0.1113 0.0777 -0.0078 0.0003  0.0025  262 PHE B CB    
5132 C CG    . PHE B 262 ? 0.1104 0.1505 0.1175 -0.0087 0.0001  0.0008  262 PHE B CG    
5133 C CD1   . PHE B 262 ? 0.1543 0.1958 0.1556 -0.0101 0.0006  -0.0010 262 PHE B CD1   
5134 C CD2   . PHE B 262 ? 0.0438 0.0839 0.0611 -0.0081 -0.0023 0.0004  262 PHE B CD2   
5135 C CE1   . PHE B 262 ? 0.2545 0.2977 0.2585 -0.0110 -0.0002 -0.0026 262 PHE B CE1   
5136 C CE2   . PHE B 262 ? 0.0978 0.1387 0.1187 -0.0085 -0.0059 -0.0017 262 PHE B CE2   
5137 C CZ    . PHE B 262 ? 0.0203 0.0624 0.0341 -0.0098 -0.0053 -0.0032 262 PHE B CZ    
5138 N N     . HIS B 263 ? 0.4628 0.5013 0.4610 -0.0088 -0.0010 0.0046  263 HIS B N     
5139 C CA    . HIS B 263 ? 0.1732 0.2129 0.1739 -0.0095 -0.0018 0.0061  263 HIS B CA    
5140 C C     . HIS B 263 ? 0.1848 0.2242 0.1895 -0.0098 -0.0063 0.0031  263 HIS B C     
5141 O O     . HIS B 263 ? 0.4439 0.4793 0.4456 -0.0090 -0.0110 0.0025  263 HIS B O     
5142 C CB    . HIS B 263 ? 0.0171 0.0519 0.0148 -0.0086 -0.0013 0.0063  263 HIS B CB    
5143 C CG    . HIS B 263 ? 0.1719 0.2022 0.1694 -0.0067 -0.0016 0.0062  263 HIS B CG    
5144 N ND1   . HIS B 263 ? 0.1124 0.1430 0.1116 -0.0061 -0.0017 0.0081  263 HIS B ND1   
5145 C CD2   . HIS B 263 ? 0.1984 0.2293 0.2006 -0.0068 -0.0010 0.0049  263 HIS B CD2   
5146 C CE1   . HIS B 263 ? 0.2642 0.2914 0.2630 -0.0048 -0.0017 0.0075  263 HIS B CE1   
5147 N NE2   . HIS B 263 ? 0.2297 0.2666 0.2299 -0.0072 -0.0014 0.0077  263 HIS B NE2   
5148 N N     . GLY B 264 ? 0.1583 0.1975 0.1646 -0.0096 -0.0078 0.0008  264 GLY B N     
5149 C CA    . GLY B 264 ? 0.1137 0.1468 0.1141 -0.0084 -0.0158 -0.0026 264 GLY B CA    
5150 C C     . GLY B 264 ? 0.1188 0.1521 0.1053 -0.0103 -0.0126 -0.0039 264 GLY B C     
5151 O O     . GLY B 264 ? 0.1179 0.1582 0.1051 -0.0131 -0.0045 -0.0024 264 GLY B O     
5152 N N     . LEU B 265 ? 0.2675 0.2889 0.2406 -0.0078 -0.0188 -0.0070 265 LEU B N     
5153 C CA    . LEU B 265 ? 0.3118 0.3258 0.2700 -0.0072 -0.0155 -0.0090 265 LEU B CA    
5154 C C     . LEU B 265 ? 0.4853 0.4884 0.4278 -0.0032 -0.0132 -0.0084 265 LEU B C     
5155 O O     . LEU B 265 ? 0.7014 0.7040 0.6435 -0.0011 -0.0154 -0.0075 265 LEU B O     
5156 C CB    . LEU B 265 ? 0.2861 0.2932 0.2397 -0.0056 -0.0228 -0.0130 265 LEU B CB    
5157 C CG    . LEU B 265 ? 0.1385 0.1539 0.1107 -0.0078 -0.0276 -0.0130 265 LEU B CG    
5158 C CD1   . LEU B 265 ? 0.2001 0.2136 0.1672 -0.0096 -0.0308 -0.0159 265 LEU B CD1   
5159 C CD2   . LEU B 265 ? 0.1373 0.1678 0.1252 -0.0099 -0.0195 -0.0119 265 LEU B CD2   
5160 N N     . ASN B 266 ? 0.3579 0.3576 0.2925 -0.0010 -0.0080 -0.0091 266 ASN B N     
5161 C CA    . ASN B 266 ? 0.3395 0.3411 0.2698 0.0013  -0.0046 -0.0081 266 ASN B CA    
5162 C C     . ASN B 266 ? 0.4256 0.4252 0.3461 -0.0013 -0.0094 -0.0109 266 ASN B C     
5163 O O     . ASN B 266 ? 0.4409 0.4368 0.3596 -0.0023 -0.0148 -0.0135 266 ASN B O     
5164 C CB    . ASN B 266 ? 0.1758 0.1756 0.1036 0.0005  0.0025  -0.0068 266 ASN B CB    
5165 C CG    . ASN B 266 ? 0.1809 0.1803 0.1051 0.0006  0.0022  -0.0097 266 ASN B CG    
5166 O OD1   . ASN B 266 ? 0.2747 0.2701 0.1895 -0.0005 0.0015  -0.0115 266 ASN B OD1   
5167 N ND2   . ASN B 266 ? 0.0961 0.0949 0.0256 0.0005  0.0035  -0.0098 266 ASN B ND2   
5168 N N     . ILE B 267 ? 0.4254 0.4184 0.3375 -0.0011 -0.0079 -0.0094 267 ILE B N     
5169 C CA    . ILE B 267 ? 0.3077 0.2897 0.2084 -0.0002 -0.0126 -0.0105 267 ILE B CA    
5170 C C     . ILE B 267 ? 0.2956 0.2713 0.1897 0.0006  -0.0151 -0.0136 267 ILE B C     
5171 O O     . ILE B 267 ? 0.4221 0.3904 0.3112 0.0022  -0.0218 -0.0154 267 ILE B O     
5172 C CB    . ILE B 267 ? 0.1904 0.1643 0.0815 0.0008  -0.0092 -0.0085 267 ILE B CB    
5173 C CG1   . ILE B 267 ? 0.4273 0.4040 0.3225 0.0005  -0.0101 -0.0062 267 ILE B CG1   
5174 C CG2   . ILE B 267 ? 0.1675 0.1285 0.0446 0.0031  -0.0123 -0.0100 267 ILE B CG2   
5175 C CD1   . ILE B 267 ? 0.6199 0.5912 0.5091 0.0008  -0.0056 -0.0041 267 ILE B CD1   
5176 N N     . PHE B 268 ? 0.3107 0.2873 0.2039 0.0002  -0.0101 -0.0142 268 PHE B N     
5177 C CA    . PHE B 268 ? 0.3772 0.3471 0.2631 0.0012  -0.0118 -0.0171 268 PHE B CA    
5178 C C     . PHE B 268 ? 0.2604 0.2329 0.1522 0.0005  -0.0160 -0.0198 268 PHE B C     
5179 O O     . PHE B 268 ? 0.3326 0.2978 0.2187 0.0019  -0.0205 -0.0225 268 PHE B O     
5180 C CB    . PHE B 268 ? 0.3227 0.2903 0.2043 0.0013  -0.0050 -0.0164 268 PHE B CB    
5181 C CG    . PHE B 268 ? 0.2720 0.2327 0.1459 0.0021  -0.0013 -0.0138 268 PHE B CG    
5182 C CD1   . PHE B 268 ? 0.3502 0.2983 0.2101 0.0044  -0.0028 -0.0143 268 PHE B CD1   
5183 C CD2   . PHE B 268 ? 0.2090 0.1751 0.0898 0.0007  0.0033  -0.0109 268 PHE B CD2   
5184 C CE1   . PHE B 268 ? 0.3736 0.3150 0.2265 0.0051  0.0006  -0.0121 268 PHE B CE1   
5185 C CE2   . PHE B 268 ? 0.3486 0.3080 0.2228 0.0012  0.0064  -0.0089 268 PHE B CE2   
5186 C CZ    . PHE B 268 ? 0.3694 0.3164 0.2296 0.0034  0.0052  -0.0094 268 PHE B CZ    
5187 N N     . ALA B 269 ? 0.1925 0.1753 0.0965 -0.0014 -0.0150 -0.0191 269 ALA B N     
5188 C CA    . ALA B 269 ? 0.1413 0.1269 0.0530 -0.0025 -0.0200 -0.0214 269 ALA B CA    
5189 C C     . ALA B 269 ? 0.3580 0.3390 0.2710 -0.0011 -0.0290 -0.0220 269 ALA B C     
5190 O O     . ALA B 269 ? 0.5376 0.5151 0.4521 0.0000  -0.0346 -0.0246 269 ALA B O     
5191 C CB    . ALA B 269 ? 0.1132 0.1111 0.0381 -0.0043 -0.0170 -0.0202 269 ALA B CB    
5192 N N     . TYR B 270 ? 0.3439 0.3255 0.2578 -0.0006 -0.0304 -0.0196 270 TYR B N     
5193 C CA    . TYR B 270 ? 0.3875 0.3651 0.3036 0.0013  -0.0384 -0.0201 270 TYR B CA    
5194 C C     . TYR B 270 ? 0.5511 0.5166 0.4543 0.0045  -0.0420 -0.0224 270 TYR B C     
5195 O O     . TYR B 270 ? 0.6467 0.6089 0.5525 0.0063  -0.0487 -0.0246 270 TYR B O     
5196 C CB    . TYR B 270 ? 0.3577 0.3380 0.2766 0.0012  -0.0383 -0.0170 270 TYR B CB    
5197 C CG    . TYR B 270 ? 0.1191 0.1115 0.0534 -0.0013 -0.0370 -0.0148 270 TYR B CG    
5198 C CD1   . TYR B 270 ? 0.1601 0.1581 0.1086 -0.0018 -0.0410 -0.0152 270 TYR B CD1   
5199 C CD2   . TYR B 270 ? 0.2813 0.2800 0.2169 -0.0027 -0.0310 -0.0122 270 TYR B CD2   
5200 C CE1   . TYR B 270 ? 0.1580 0.1673 0.1213 -0.0040 -0.0388 -0.0127 270 TYR B CE1   
5201 C CE2   . TYR B 270 ? 0.2928 0.3029 0.2426 -0.0045 -0.0297 -0.0102 270 TYR B CE2   
5202 C CZ    . TYR B 270 ? 0.0841 0.0994 0.0477 -0.0054 -0.0334 -0.0102 270 TYR B CZ    
5203 O OH    . TYR B 270 ? 0.0671 0.0925 0.0463 -0.0065 -0.0300 -0.0076 270 TYR B OH    
5204 N N     . THR B 271 ? 0.4662 0.4254 0.3563 0.0053  -0.0375 -0.0218 271 THR B N     
5205 C CA    . THR B 271 ? 0.4729 0.4203 0.3502 0.0086  -0.0410 -0.0236 271 THR B CA    
5206 C C     . THR B 271 ? 0.4370 0.3810 0.3123 0.0094  -0.0432 -0.0269 271 THR B C     
5207 O O     . THR B 271 ? 0.5403 0.4773 0.4122 0.0121  -0.0499 -0.0292 271 THR B O     
5208 C CB    . THR B 271 ? 0.5166 0.4587 0.3821 0.0092  -0.0351 -0.0218 271 THR B CB    
5209 O OG1   . THR B 271 ? 0.5699 0.5182 0.4401 0.0074  -0.0310 -0.0186 271 THR B OG1   
5210 C CG2   . THR B 271 ? 0.5100 0.4398 0.3627 0.0129  -0.0398 -0.0228 271 THR B CG2   
5211 N N     . ALA B 272 ? 0.4365 0.3854 0.3145 0.0072  -0.0376 -0.0273 272 ALA B N     
5212 C CA    . ALA B 272 ? 0.3096 0.2552 0.1852 0.0079  -0.0389 -0.0305 272 ALA B CA    
5213 C C     . ALA B 272 ? 0.2231 0.1722 0.1105 0.0080  -0.0461 -0.0328 272 ALA B C     
5214 O O     . ALA B 272 ? 0.2520 0.1947 0.1364 0.0104  -0.0517 -0.0355 272 ALA B O     
5215 C CB    . ALA B 272 ? 0.2720 0.2228 0.1486 0.0054  -0.0306 -0.0302 272 ALA B CB    
5216 N N     . MET B 273 ? 0.1749 0.1340 0.0766 0.0056  -0.0460 -0.0314 273 MET B N     
5217 C CA    . MET B 273 ? 0.3647 0.3284 0.2807 0.0056  -0.0521 -0.0330 273 MET B CA    
5218 C C     . MET B 273 ? 0.5308 0.4885 0.4466 0.0088  -0.0602 -0.0339 273 MET B C     
5219 O O     . MET B 273 ? 0.6431 0.5998 0.5650 0.0102  -0.0656 -0.0364 273 MET B O     
5220 C CB    . MET B 273 ? 0.4311 0.4072 0.3633 0.0027  -0.0500 -0.0305 273 MET B CB    
5221 C CG    . MET B 273 ? 0.5630 0.5456 0.5133 0.0025  -0.0546 -0.0312 273 MET B CG    
5222 S SD    . MET B 273 ? 0.3975 0.3914 0.3664 0.0009  -0.0542 -0.0271 273 MET B SD    
5223 C CE    . MET B 273 ? 0.3835 0.3858 0.3535 -0.0028 -0.0459 -0.0245 273 MET B CE    
5224 N N     . GLN B 274 ? 0.4445 0.3984 0.3538 0.0101  -0.0609 -0.0320 274 GLN B N     
5225 C CA    . GLN B 274 ? 0.4908 0.4383 0.3988 0.0132  -0.0683 -0.0330 274 GLN B CA    
5226 C C     . GLN B 274 ? 0.4433 0.3797 0.3387 0.0165  -0.0720 -0.0362 274 GLN B C     
5227 O O     . GLN B 274 ? 0.6021 0.5350 0.5009 0.0188  -0.0789 -0.0384 274 GLN B O     
5228 C CB    . GLN B 274 ? 0.5269 0.4722 0.4298 0.0138  -0.0677 -0.0303 274 GLN B CB    
5229 C CG    . GLN B 274 ? 0.4761 0.4147 0.3776 0.0171  -0.0752 -0.0314 274 GLN B CG    
5230 C CD    . GLN B 274 ? 0.5912 0.5276 0.4879 0.0176  -0.0747 -0.0289 274 GLN B CD    
5231 O OE1   . GLN B 274 ? 0.5224 0.4597 0.4262 0.0185  -0.0791 -0.0285 274 GLN B OE1   
5232 N NE2   . GLN B 274 ? 0.6548 0.5883 0.5398 0.0172  -0.0691 -0.0272 274 GLN B NE2   
5233 N N     . SER B 275 ? 0.3981 0.3287 0.2790 0.0167  -0.0672 -0.0363 275 SER B N     
5234 C CA    . SER B 275 ? 0.4240 0.3440 0.2925 0.0199  -0.0701 -0.0391 275 SER B CA    
5235 C C     . SER B 275 ? 0.6207 0.5427 0.4949 0.0194  -0.0715 -0.0421 275 SER B C     
5236 O O     . SER B 275 ? 0.5827 0.4989 0.4552 0.0221  -0.0777 -0.0451 275 SER B O     
5237 C CB    . SER B 275 ? 0.3809 0.2945 0.2333 0.0203  -0.0637 -0.0378 275 SER B CB    
5238 O OG    . SER B 275 ? 0.4893 0.3927 0.3293 0.0234  -0.0660 -0.0402 275 SER B OG    
5239 N N     . ALA B 276 ? 0.5969 0.5270 0.4780 0.0160  -0.0657 -0.0416 276 ALA B N     
5240 C CA    . ALA B 276 ? 0.4448 0.3775 0.3320 0.0153  -0.0662 -0.0444 276 ALA B CA    
5241 C C     . ALA B 276 ? 0.4244 0.3601 0.3258 0.0163  -0.0739 -0.0462 276 ALA B C     
5242 O O     . ALA B 276 ? 0.6470 0.5805 0.5502 0.0174  -0.0772 -0.0493 276 ALA B O     
5243 C CB    . ALA B 276 ? 0.5756 0.5176 0.4699 0.0113  -0.0588 -0.0432 276 ALA B CB    
5244 N N     . TYR B 277 ? 0.4088 0.3496 0.3209 0.0160  -0.0765 -0.0442 277 TYR B N     
5245 C CA    . TYR B 277 ? 0.3343 0.2792 0.2623 0.0167  -0.0825 -0.0452 277 TYR B CA    
5246 C C     . TYR B 277 ? 0.3572 0.2938 0.2808 0.0205  -0.0901 -0.0466 277 TYR B C     
5247 O O     . TYR B 277 ? 0.4642 0.4036 0.4009 0.0214  -0.0949 -0.0472 277 TYR B O     
5248 C CB    . TYR B 277 ? 0.3224 0.2782 0.2662 0.0141  -0.0801 -0.0420 277 TYR B CB    
5249 C CG    . TYR B 277 ? 0.2370 0.2026 0.1914 0.0108  -0.0746 -0.0411 277 TYR B CG    
5250 C CD1   . TYR B 277 ? 0.2952 0.2602 0.2474 0.0102  -0.0729 -0.0436 277 TYR B CD1   
5251 C CD2   . TYR B 277 ? 0.2639 0.2395 0.2307 0.0082  -0.0709 -0.0377 277 TYR B CD2   
5252 C CE1   . TYR B 277 ? 0.3344 0.3084 0.2968 0.0072  -0.0677 -0.0429 277 TYR B CE1   
5253 C CE2   . TYR B 277 ? 0.1991 0.1837 0.1759 0.0054  -0.0658 -0.0367 277 TYR B CE2   
5254 C CZ    . TYR B 277 ? 0.2141 0.1980 0.1890 0.0049  -0.0643 -0.0393 277 TYR B CZ    
5255 O OH    . TYR B 277 ? 0.2559 0.2492 0.2417 0.0021  -0.0590 -0.0381 277 TYR B OH    
5256 N N     . THR B 278 ? 0.3263 0.2529 0.2324 0.0228  -0.0908 -0.0470 278 THR B N     
5257 C CA    . THR B 278 ? 0.5617 0.4802 0.4632 0.0266  -0.0980 -0.0484 278 THR B CA    
5258 C C     . THR B 278 ? 0.6777 0.5850 0.5636 0.0298  -0.1007 -0.0515 278 THR B C     
5259 O O     . THR B 278 ? 0.8866 0.7893 0.7740 0.0327  -0.1077 -0.0544 278 THR B O     
5260 C CB    . THR B 278 ? 0.6131 0.5294 0.5091 0.0271  -0.0975 -0.0456 278 THR B CB    
5261 O OG1   . THR B 278 ? 0.6424 0.5591 0.5286 0.0252  -0.0899 -0.0431 278 THR B OG1   
5262 C CG2   . THR B 278 ? 0.6048 0.5296 0.5175 0.0255  -0.0986 -0.0436 278 THR B CG2   
5263 N N     . GLU B 279 ? 0.5984 0.5013 0.4696 0.0295  -0.0950 -0.0507 279 GLU B N     
5264 C CA    . GLU B 279 ? 0.6220 0.5131 0.4760 0.0330  -0.0968 -0.0527 279 GLU B CA    
5265 C C     . GLU B 279 ? 0.6622 0.5518 0.5106 0.0323  -0.0932 -0.0546 279 GLU B C     
5266 O O     . GLU B 279 ? 0.7342 0.6142 0.5673 0.0348  -0.0929 -0.0557 279 GLU B O     
5267 C CB    . GLU B 279 ? 0.5984 0.4835 0.4381 0.0339  -0.0932 -0.0500 279 GLU B CB    
5268 C CG    . GLU B 279 ? 0.6123 0.5005 0.4581 0.0336  -0.0949 -0.0476 279 GLU B CG    
5269 C CD    . GLU B 279 ? 0.7104 0.5954 0.5447 0.0334  -0.0892 -0.0444 279 GLU B CD    
5270 O OE1   . GLU B 279 ? 0.7866 0.6667 0.6164 0.0356  -0.0925 -0.0437 279 GLU B OE1   
5271 O OE2   . GLU B 279 ? 0.6436 0.5310 0.4740 0.0310  -0.0814 -0.0427 279 GLU B OE2   
5272 N N     . CYS B 280 ? 0.6305 0.5291 0.4909 0.0291  -0.0902 -0.0549 280 CYS B N     
5273 C CA    . CYS B 280 ? 0.6758 0.5736 0.5309 0.0279  -0.0852 -0.0563 280 CYS B CA    
5274 C C     . CYS B 280 ? 0.5601 0.4598 0.4245 0.0282  -0.0897 -0.0599 280 CYS B C     
5275 O O     . CYS B 280 ? 0.6690 0.5712 0.5341 0.0263  -0.0853 -0.0610 280 CYS B O     
5276 C CB    . CYS B 280 ? 0.7873 0.6935 0.6462 0.0237  -0.0762 -0.0535 280 CYS B CB    
5277 S SG    . CYS B 280 ? 0.6049 0.5105 0.4561 0.0231  -0.0713 -0.0490 280 CYS B SG    
5278 N N     . ASN B 281 ? 0.4614 0.3596 0.3328 0.0307  -0.0982 -0.0618 281 ASN B N     
5279 C CA    . ASN B 281 ? 0.5478 0.4491 0.4314 0.0310  -0.1028 -0.0649 281 ASN B CA    
5280 C C     . ASN B 281 ? 0.6221 0.5163 0.4951 0.0325  -0.1028 -0.0682 281 ASN B C     
5281 O O     . ASN B 281 ? 0.6123 0.5110 0.4938 0.0310  -0.1022 -0.0701 281 ASN B O     
5282 C CB    . ASN B 281 ? 0.6609 0.5610 0.5531 0.0338  -0.1116 -0.0661 281 ASN B CB    
5283 C CG    . ASN B 281 ? 0.6958 0.6046 0.6029 0.0319  -0.1114 -0.0632 281 ASN B CG    
5284 O OD1   . ASN B 281 ? 0.7230 0.6413 0.6469 0.0294  -0.1100 -0.0627 281 ASN B OD1   
5285 N ND2   . ASN B 281 ? 0.6806 0.5861 0.5817 0.0330  -0.1123 -0.0611 281 ASN B ND2   
5286 N N     . ASP B 282 ? 0.6999 0.5831 0.5548 0.0356  -0.1039 -0.0688 282 ASP B N     
5287 C CA    . ASP B 282 ? 0.7949 0.6709 0.6395 0.0375  -0.1044 -0.0719 282 ASP B CA    
5288 C C     . ASP B 282 ? 0.6974 0.5751 0.5361 0.0346  -0.0950 -0.0710 282 ASP B C     
5289 O O     . ASP B 282 ? 0.6778 0.5548 0.5164 0.0343  -0.0943 -0.0736 282 ASP B O     
5290 C CB    . ASP B 282 ? 0.8594 0.7229 0.6869 0.0420  -0.1085 -0.0727 282 ASP B CB    
5291 C CG    . ASP B 282 ? 0.9776 0.8377 0.8101 0.0456  -0.1187 -0.0752 282 ASP B CG    
5292 O OD1   . ASP B 282 ? 1.0529 0.9172 0.8949 0.0454  -0.1217 -0.0737 282 ASP B OD1   
5293 O OD2   . ASP B 282 ? 0.9431 0.7966 0.7705 0.0486  -0.1237 -0.0787 282 ASP B OD2   
5294 N N     . TRP B 283 ? 0.5722 0.4524 0.4066 0.0323  -0.0877 -0.0675 283 TRP B N     
5295 C CA    . TRP B 283 ? 0.5663 0.4492 0.3971 0.0294  -0.0783 -0.0665 283 TRP B CA    
5296 C C     . TRP B 283 ? 0.5224 0.4156 0.3694 0.0258  -0.0763 -0.0675 283 TRP B C     
5297 O O     . TRP B 283 ? 0.5341 0.4281 0.3795 0.0242  -0.0713 -0.0687 283 TRP B O     
5298 C CB    . TRP B 283 ? 0.5813 0.4657 0.4065 0.0277  -0.0710 -0.0623 283 TRP B CB    
5299 C CG    . TRP B 283 ? 0.6389 0.5270 0.4619 0.0246  -0.0609 -0.0609 283 TRP B CG    
5300 C CD1   . TRP B 283 ? 0.6016 0.4833 0.4109 0.0255  -0.0554 -0.0604 283 TRP B CD1   
5301 C CD2   . TRP B 283 ? 0.5949 0.4940 0.4302 0.0203  -0.0551 -0.0599 283 TRP B CD2   
5302 N NE1   . TRP B 283 ? 0.5637 0.4522 0.3770 0.0220  -0.0466 -0.0591 283 TRP B NE1   
5303 C CE2   . TRP B 283 ? 0.5707 0.4698 0.3995 0.0188  -0.0463 -0.0589 283 TRP B CE2   
5304 C CE3   . TRP B 283 ? 0.4698 0.3789 0.3218 0.0178  -0.0566 -0.0596 283 TRP B CE3   
5305 C CZ2   . TRP B 283 ? 0.5600 0.4686 0.3980 0.0150  -0.0390 -0.0578 283 TRP B CZ2   
5306 C CZ3   . TRP B 283 ? 0.3603 0.2783 0.2204 0.0140  -0.0495 -0.0586 283 TRP B CZ3   
5307 C CH2   . TRP B 283 ? 0.3683 0.2860 0.2213 0.0126  -0.0407 -0.0578 283 TRP B CH2   
5308 N N     . LEU B 284 ? 0.5086 0.4096 0.3717 0.0247  -0.0803 -0.0671 284 LEU B N     
5309 C CA    . LEU B 284 ? 0.4824 0.3934 0.3620 0.0215  -0.0785 -0.0678 284 LEU B CA    
5310 C C     . LEU B 284 ? 0.6551 0.5644 0.5397 0.0229  -0.0834 -0.0718 284 LEU B C     
5311 O O     . LEU B 284 ? 0.7899 0.7046 0.6824 0.0205  -0.0800 -0.0729 284 LEU B O     
5312 C CB    . LEU B 284 ? 0.4378 0.3579 0.3340 0.0202  -0.0811 -0.0657 284 LEU B CB    
5313 C CG    . LEU B 284 ? 0.4177 0.3487 0.3343 0.0177  -0.0809 -0.0660 284 LEU B CG    
5314 C CD1   . LEU B 284 ? 0.4387 0.3749 0.3559 0.0141  -0.0721 -0.0655 284 LEU B CD1   
5315 C CD2   . LEU B 284 ? 0.5192 0.4581 0.4505 0.0170  -0.0832 -0.0633 284 LEU B CD2   
5316 N N     . ASN B 285 ? 0.6855 0.5873 0.5653 0.0268  -0.0913 -0.0740 285 ASN B N     
5317 C CA    . ASN B 285 ? 0.6029 0.5018 0.4852 0.0284  -0.0959 -0.0780 285 ASN B CA    
5318 C C     . ASN B 285 ? 0.6026 0.4962 0.4717 0.0280  -0.0903 -0.0794 285 ASN B C     
5319 O O     . ASN B 285 ? 0.7305 0.6267 0.6059 0.0268  -0.0893 -0.0818 285 ASN B O     
5320 C CB    . ASN B 285 ? 0.5802 0.4714 0.4585 0.0329  -0.1053 -0.0800 285 ASN B CB    
5321 C CG    . ASN B 285 ? 0.5745 0.4708 0.4665 0.0334  -0.1106 -0.0786 285 ASN B CG    
5322 O OD1   . ASN B 285 ? 0.5199 0.4265 0.4285 0.0305  -0.1087 -0.0770 285 ASN B OD1   
5323 N ND2   . ASN B 285 ? 0.6049 0.4940 0.4902 0.0370  -0.1169 -0.0790 285 ASN B ND2   
5324 N N     . LYS B 286 ? 0.5288 0.4149 0.3802 0.0291  -0.0864 -0.0779 286 LYS B N     
5325 C CA    . LYS B 286 ? 0.5862 0.4676 0.4251 0.0287  -0.0799 -0.0786 286 LYS B CA    
5326 C C     . LYS B 286 ? 0.6009 0.4911 0.4480 0.0242  -0.0713 -0.0777 286 LYS B C     
5327 O O     . LYS B 286 ? 0.6465 0.5371 0.4953 0.0233  -0.0692 -0.0800 286 LYS B O     
5328 C CB    . LYS B 286 ? 0.6621 0.5355 0.4830 0.0306  -0.0764 -0.0762 286 LYS B CB    
5329 C CG    . LYS B 286 ? 0.6382 0.4993 0.4445 0.0353  -0.0820 -0.0783 286 LYS B CG    
5330 C CD    . LYS B 286 ? 0.6538 0.5124 0.4636 0.0384  -0.0919 -0.0794 286 LYS B CD    
5331 C CE    . LYS B 286 ? 0.6822 0.5282 0.4765 0.0434  -0.0973 -0.0814 286 LYS B CE    
5332 N NZ    . LYS B 286 ? 0.6510 0.4899 0.4281 0.0446  -0.0913 -0.0786 286 LYS B NZ    
5333 N N     . ILE B 287 ? 0.4451 0.3423 0.2974 0.0214  -0.0662 -0.0743 287 ILE B N     
5334 C CA    . ILE B 287 ? 0.4846 0.3895 0.3426 0.0174  -0.0572 -0.0731 287 ILE B CA    
5335 C C     . ILE B 287 ? 0.4632 0.3749 0.3370 0.0155  -0.0587 -0.0756 287 ILE B C     
5336 O O     . ILE B 287 ? 0.4378 0.3534 0.3145 0.0128  -0.0519 -0.0759 287 ILE B O     
5337 C CB    . ILE B 287 ? 0.4627 0.3742 0.3245 0.0150  -0.0525 -0.0691 287 ILE B CB    
5338 C CG1   . ILE B 287 ? 0.5496 0.4672 0.4132 0.0115  -0.0420 -0.0678 287 ILE B CG1   
5339 C CG2   . ILE B 287 ? 0.3729 0.2923 0.2515 0.0141  -0.0577 -0.0686 287 ILE B CG2   
5340 C CD1   . ILE B 287 ? 0.4745 0.3864 0.3238 0.0122  -0.0355 -0.0673 287 ILE B CD1   
5341 N N     . ARG B 288 ? 0.5232 0.4367 0.4084 0.0169  -0.0673 -0.0771 288 ARG B N     
5342 C CA    . ARG B 288 ? 0.4968 0.4172 0.3987 0.0155  -0.0690 -0.0791 288 ARG B CA    
5343 C C     . ARG B 288 ? 0.4861 0.4012 0.3826 0.0163  -0.0687 -0.0827 288 ARG B C     
5344 O O     . ARG B 288 ? 0.3342 0.2545 0.2399 0.0141  -0.0652 -0.0838 288 ARG B O     
5345 C CB    . ARG B 288 ? 0.4531 0.3771 0.3695 0.0173  -0.0781 -0.0796 288 ARG B CB    
5346 C CG    . ARG B 288 ? 0.4203 0.3525 0.3477 0.0156  -0.0774 -0.0762 288 ARG B CG    
5347 C CD    . ARG B 288 ? 0.3732 0.3061 0.3096 0.0182  -0.0860 -0.0759 288 ARG B CD    
5348 N NE    . ARG B 288 ? 0.4299 0.3746 0.3880 0.0162  -0.0858 -0.0741 288 ARG B NE    
5349 C CZ    . ARG B 288 ? 0.6847 0.6334 0.6543 0.0172  -0.0902 -0.0722 288 ARG B CZ    
5350 N NH1   . ARG B 288 ? 0.7936 0.7352 0.7547 0.0201  -0.0956 -0.0724 288 ARG B NH1   
5351 N NH2   . ARG B 288 ? 0.6815 0.6411 0.6711 0.0156  -0.0886 -0.0701 288 ARG B NH2   
5352 N N     . LEU B 289 ? 0.5642 0.4691 0.4467 0.0197  -0.0728 -0.0845 289 LEU B N     
5353 C CA    . LEU B 289 ? 0.6433 0.5426 0.5198 0.0208  -0.0730 -0.0880 289 LEU B CA    
5354 C C     . LEU B 289 ? 0.6690 0.5655 0.5331 0.0191  -0.0632 -0.0872 289 LEU B C     
5355 O O     . LEU B 289 ? 0.7806 0.6763 0.6445 0.0184  -0.0605 -0.0895 289 LEU B O     
5356 C CB    . LEU B 289 ? 0.6657 0.5551 0.5321 0.0254  -0.0814 -0.0902 289 LEU B CB    
5357 C CG    . LEU B 289 ? 0.6315 0.5229 0.5099 0.0275  -0.0913 -0.0911 289 LEU B CG    
5358 C CD1   . LEU B 289 ? 0.7158 0.5964 0.5803 0.0321  -0.0981 -0.0924 289 LEU B CD1   
5359 C CD2   . LEU B 289 ? 0.4864 0.3837 0.3825 0.0270  -0.0954 -0.0939 289 LEU B CD2   
5360 N N     . TYR B 290 ? 0.5758 0.4713 0.4303 0.0187  -0.0577 -0.0839 290 TYR B N     
5361 C CA    . TYR B 290 ? 0.4575 0.3525 0.3034 0.0170  -0.0478 -0.0827 290 TYR B CA    
5362 C C     . TYR B 290 ? 0.4676 0.3728 0.3265 0.0127  -0.0408 -0.0821 290 TYR B C     
5363 O O     . TYR B 290 ? 0.5651 0.4709 0.4231 0.0113  -0.0349 -0.0832 290 TYR B O     
5364 C CB    . TYR B 290 ? 0.4712 0.3632 0.3053 0.0179  -0.0440 -0.0790 290 TYR B CB    
5365 C CG    . TYR B 290 ? 0.4648 0.3533 0.2871 0.0180  -0.0360 -0.0778 290 TYR B CG    
5366 C CD1   . TYR B 290 ? 0.5065 0.3846 0.3146 0.0213  -0.0380 -0.0792 290 TYR B CD1   
5367 C CD2   . TYR B 290 ? 0.5293 0.4253 0.3553 0.0150  -0.0265 -0.0750 290 TYR B CD2   
5368 C CE1   . TYR B 290 ? 0.5541 0.4290 0.3521 0.0217  -0.0309 -0.0778 290 TYR B CE1   
5369 C CE2   . TYR B 290 ? 0.6533 0.5469 0.4703 0.0155  -0.0196 -0.0735 290 TYR B CE2   
5370 C CZ    . TYR B 290 ? 0.6997 0.5825 0.5026 0.0188  -0.0218 -0.0748 290 TYR B CZ    
5371 O OH    . TYR B 290 ? 0.6498 0.5297 0.4441 0.0194  -0.0151 -0.0730 290 TYR B OH    
5372 N N     . ILE B 291 ? 0.3792 0.2923 0.2506 0.0107  -0.0415 -0.0802 291 ILE B N     
5373 C CA    . ILE B 291 ? 0.4997 0.4222 0.3836 0.0069  -0.0350 -0.0794 291 ILE B CA    
5374 C C     . ILE B 291 ? 0.4608 0.3849 0.3551 0.0064  -0.0374 -0.0825 291 ILE B C     
5375 O O     . ILE B 291 ? 0.4754 0.4021 0.3723 0.0041  -0.0304 -0.0829 291 ILE B O     
5376 C CB    . ILE B 291 ? 0.5469 0.4771 0.4419 0.0054  -0.0359 -0.0765 291 ILE B CB    
5377 C CG1   . ILE B 291 ? 0.5490 0.4789 0.4344 0.0052  -0.0312 -0.0731 291 ILE B CG1   
5378 C CG2   . ILE B 291 ? 0.5791 0.5183 0.4885 0.0022  -0.0310 -0.0759 291 ILE B CG2   
5379 C CD1   . ILE B 291 ? 0.4582 0.3866 0.3330 0.0048  -0.0224 -0.0723 291 ILE B CD1   
5380 N N     . GLU B 292 ? 0.4514 0.3743 0.3527 0.0086  -0.0470 -0.0846 292 GLU B N     
5381 C CA    . GLU B 292 ? 0.4257 0.3515 0.3396 0.0085  -0.0500 -0.0875 292 GLU B CA    
5382 C C     . GLU B 292 ? 0.3738 0.2927 0.2770 0.0088  -0.0466 -0.0902 292 GLU B C     
5383 O O     . GLU B 292 ? 0.2897 0.2116 0.2013 0.0075  -0.0443 -0.0917 292 GLU B O     
5384 C CB    . GLU B 292 ? 0.6402 0.5661 0.5633 0.0113  -0.0610 -0.0891 292 GLU B CB    
5385 C CG    . GLU B 292 ? 0.6007 0.5307 0.5392 0.0114  -0.0646 -0.0918 292 GLU B CG    
5386 C CD    . GLU B 292 ? 0.6071 0.5403 0.5591 0.0137  -0.0743 -0.0924 292 GLU B CD    
5387 O OE1   . GLU B 292 ? 0.6860 0.6149 0.6309 0.0157  -0.0789 -0.0916 292 GLU B OE1   
5388 O OE2   . GLU B 292 ? 0.7159 0.6558 0.6858 0.0135  -0.0768 -0.0935 292 GLU B OE2   
5389 N N     . ASP B 293 ? 0.4909 0.4007 0.3765 0.0111  -0.0469 -0.0908 293 ASP B N     
5390 C CA    . ASP B 293 ? 0.6114 0.5150 0.4863 0.0117  -0.0432 -0.0930 293 ASP B CA    
5391 C C     . ASP B 293 ? 0.6420 0.5493 0.5144 0.0086  -0.0315 -0.0912 293 ASP B C     
5392 O O     . ASP B 293 ? 0.5386 0.4452 0.4103 0.0077  -0.0271 -0.0930 293 ASP B O     
5393 C CB    . ASP B 293 ? 0.6819 0.5750 0.5395 0.0156  -0.0473 -0.0937 293 ASP B CB    
5394 C CG    . ASP B 293 ? 0.8183 0.7042 0.6672 0.0173  -0.0475 -0.0970 293 ASP B CG    
5395 O OD1   . ASP B 293 ? 0.9139 0.8028 0.7684 0.0151  -0.0428 -0.0985 293 ASP B OD1   
5396 O OD2   . ASP B 293 ? 0.8435 0.7203 0.6795 0.0210  -0.0524 -0.0981 293 ASP B OD2   
5397 N N     . ASN B 294 ? 0.7393 0.6515 0.6116 0.0071  -0.0264 -0.0876 294 ASN B N     
5398 C CA    . ASN B 294 ? 0.5733 0.4919 0.4470 0.0044  -0.0156 -0.0858 294 ASN B CA    
5399 C C     . ASN B 294 ? 0.5062 0.4311 0.3941 0.0010  -0.0119 -0.0863 294 ASN B C     
5400 O O     . ASN B 294 ? 0.5141 0.4430 0.4040 -0.0008 -0.0040 -0.0866 294 ASN B O     
5401 C CB    . ASN B 294 ? 0.4508 0.3741 0.3231 0.0040  -0.0121 -0.0819 294 ASN B CB    
5402 C CG    . ASN B 294 ? 0.4144 0.3308 0.2708 0.0071  -0.0120 -0.0801 294 ASN B CG    
5403 O OD1   . ASN B 294 ? 0.5214 0.4287 0.3671 0.0096  -0.0155 -0.0820 294 ASN B OD1   
5404 N ND2   . ASN B 294 ? 0.3676 0.2876 0.2221 0.0069  -0.0083 -0.0761 294 ASN B ND2   
5405 N N     . ALA B 295 ? 0.3240 0.2512 0.2236 0.0008  -0.0182 -0.0859 295 ALA B N     
5406 C CA    . ALA B 295 ? 0.3231 0.2553 0.2371 -0.0004 -0.0171 -0.0856 295 ALA B CA    
5407 C C     . ALA B 295 ? 0.5578 0.4863 0.4728 0.0005  -0.0192 -0.0892 295 ALA B C     
5408 O O     . ALA B 295 ? 0.5414 0.4720 0.4619 -0.0003 -0.0143 -0.0888 295 ALA B O     
5409 C CB    . ALA B 295 ? 0.2274 0.1688 0.1601 0.0003  -0.0245 -0.0849 295 ALA B CB    
5410 N N     . LYS B 296 ? 0.6110 0.5337 0.5206 0.0030  -0.0267 -0.0925 296 LYS B N     
5411 C CA    . LYS B 296 ? 0.5203 0.4389 0.4301 0.0040  -0.0291 -0.0961 296 LYS B CA    
5412 C C     . LYS B 296 ? 0.4405 0.3540 0.3369 0.0029  -0.0203 -0.0968 296 LYS B C     
5413 O O     . LYS B 296 ? 0.5971 0.5104 0.4970 0.0019  -0.0167 -0.0979 296 LYS B O     
5414 C CB    . LYS B 296 ? 0.5799 0.4930 0.4864 0.0074  -0.0397 -0.0990 296 LYS B CB    
5415 C CG    . LYS B 296 ? 0.7642 0.6717 0.6682 0.0089  -0.0424 -0.1030 296 LYS B CG    
5416 C CD    . LYS B 296 ? 0.8008 0.6986 0.6902 0.0125  -0.0489 -0.1052 296 LYS B CD    
5417 C CE    . LYS B 296 ? 0.7195 0.6100 0.5907 0.0130  -0.0423 -0.1056 296 LYS B CE    
5418 N NZ    . LYS B 296 ? 0.6808 0.5620 0.5370 0.0170  -0.0483 -0.1066 296 LYS B NZ    
5419 N N     . PHE B 297 ? 0.3595 0.2702 0.2425 0.0037  -0.0173 -0.0960 297 PHE B N     
5420 C CA    . PHE B 297 ? 0.4450 0.3556 0.3198 0.0036  -0.0094 -0.0966 297 PHE B CA    
5421 C C     . PHE B 297 ? 0.5029 0.4236 0.3882 0.0003  0.0004  -0.0954 297 PHE B C     
5422 O O     . PHE B 297 ? 0.5208 0.4446 0.4091 0.0008  0.0043  -0.0963 297 PHE B O     
5423 C CB    . PHE B 297 ? 0.4386 0.3467 0.3003 0.0063  -0.0089 -0.0944 297 PHE B CB    
5424 C CG    . PHE B 297 ? 0.5056 0.4156 0.3610 0.0075  -0.0018 -0.0932 297 PHE B CG    
5425 C CD1   . PHE B 297 ? 0.6110 0.5126 0.4549 0.0099  -0.0026 -0.0950 297 PHE B CD1   
5426 C CD2   . PHE B 297 ? 0.5735 0.4934 0.4343 0.0073  0.0048  -0.0894 297 PHE B CD2   
5427 C CE1   . PHE B 297 ? 0.6310 0.5334 0.4688 0.0113  0.0036  -0.0929 297 PHE B CE1   
5428 C CE2   . PHE B 297 ? 0.5493 0.4697 0.4040 0.0093  0.0102  -0.0866 297 PHE B CE2   
5429 C CZ    . PHE B 297 ? 0.5608 0.4723 0.4041 0.0108  0.0099  -0.0884 297 PHE B CZ    
5430 N N     . ALA B 298 ? 0.4862 0.4139 0.3802 -0.0015 0.0030  -0.0908 298 ALA B N     
5431 C CA    . ALA B 298 ? 0.3156 0.2633 0.2285 0.0035  0.0054  -0.0888 298 ALA B CA    
5432 C C     . ALA B 298 ? 0.3121 0.2315 0.2091 0.0054  0.0040  -0.0815 298 ALA B C     
5433 O O     . ALA B 298 ? 0.3783 0.3069 0.2826 0.0083  0.0080  -0.0818 298 ALA B O     
5434 C CB    . ALA B 298 ? 0.3013 0.2376 0.2025 0.0111  0.0013  -0.0790 298 ALA B CB    
5435 N N     . CYS B 299 ? 0.3537 0.2760 0.2622 0.0006  0.0000  -0.0867 299 CYS B N     
5436 C CA    . CYS B 299 ? 0.4098 0.3439 0.3402 0.0007  -0.0014 -0.0885 299 CYS B CA    
5437 C C     . CYS B 299 ? 0.3912 0.3172 0.3142 0.0015  -0.0004 -0.0911 299 CYS B C     
5438 O O     . CYS B 299 ? 0.2847 0.2201 0.2226 0.0013  0.0023  -0.0913 299 CYS B O     
5439 C CB    . CYS B 299 ? 0.3656 0.3080 0.3144 -0.0002 -0.0101 -0.0913 299 CYS B CB    
5440 S SG    . CYS B 299 ? 0.4736 0.4295 0.4376 -0.0014 -0.0101 -0.0880 299 CYS B SG    
5441 N N     . GLU B 300 ? 0.4625 0.3750 0.3666 0.0004  -0.0007 -0.0938 300 GLU B N     
5442 C CA    . GLU B 300 ? 0.6650 0.5712 0.5626 0.0003  0.0015  -0.0964 300 GLU B CA    
5443 C C     . GLU B 300 ? 0.7519 0.6526 0.6364 0.0042  0.0078  -0.0891 300 GLU B C     
5444 O O     . GLU B 300 ? 0.7597 0.6634 0.6479 0.0104  0.0059  -0.0903 300 GLU B O     
5445 C CB    . GLU B 300 ? 0.6722 0.5761 0.5646 0.0002  -0.0040 -0.1029 300 GLU B CB    
5446 C CG    . GLU B 300 ? 0.7967 0.7025 0.6983 0.0025  -0.0158 -0.1043 300 GLU B CG    
5447 C CD    . GLU B 300 ? 0.9409 0.8404 0.8318 0.0054  -0.0230 -0.1073 300 GLU B CD    
5448 O OE1   . GLU B 300 ? 1.0085 0.9045 0.8854 0.0061  -0.0194 -0.1071 300 GLU B OE1   
5449 O OE2   . GLU B 300 ? 0.9547 0.8535 0.8521 0.0076  -0.0328 -0.1095 300 GLU B OE2   
5450 N N     . TYR B 301 ? 0.4469 0.3835 0.3546 0.0119  0.0033  -0.0962 301 TYR B N     
5451 C CA    . TYR B 301 ? 0.4600 0.3938 0.3563 0.0143  0.0103  -0.0914 301 TYR B CA    
5452 C C     . TYR B 301 ? 0.4357 0.3680 0.3349 0.0133  0.0169  -0.0853 301 TYR B C     
5453 O O     . TYR B 301 ? 0.4989 0.4351 0.3988 0.0124  0.0234  -0.0827 301 TYR B O     
5454 C CB    . TYR B 301 ? 0.4975 0.4348 0.3875 0.0128  0.0143  -0.0890 301 TYR B CB    
5455 C CG    . TYR B 301 ? 0.4850 0.4230 0.3681 0.0130  0.0222  -0.0833 301 TYR B CG    
5456 C CD1   . TYR B 301 ? 0.4965 0.4396 0.3864 0.0117  0.0285  -0.0756 301 TYR B CD1   
5457 C CD2   . TYR B 301 ? 0.4737 0.4068 0.3449 0.0127  0.0241  -0.0838 301 TYR B CD2   
5458 C CE1   . TYR B 301 ? 0.4549 0.4006 0.3428 0.0105  0.0352  -0.0701 301 TYR B CE1   
5459 C CE2   . TYR B 301 ? 0.5010 0.4348 0.3682 0.0125  0.0308  -0.0777 301 TYR B CE2   
5460 C CZ    . TYR B 301 ? 0.4810 0.4212 0.3569 0.0111  0.0361  -0.0712 301 TYR B CZ    
5461 O OH    . TYR B 301 ? 0.5224 0.4600 0.3939 0.0088  0.0436  -0.0655 301 TYR B OH    
5462 N N     . MET B 302 ? 0.4399 0.3748 0.3499 0.0092  0.0180  -0.0826 302 MET B N     
5463 C CA    . MET B 302 ? 0.5751 0.5232 0.5036 0.0041  0.0260  -0.0787 302 MET B CA    
5464 C C     . MET B 302 ? 0.7575 0.7053 0.6938 0.0030  0.0254  -0.0822 302 MET B C     
5465 O O     . MET B 302 ? 0.8709 0.8277 0.8178 0.0005  0.0320  -0.0795 302 MET B O     
5466 C CB    . MET B 302 ? 0.4285 0.3880 0.3738 -0.0001 0.0270  -0.0767 302 MET B CB    
5467 C CG    . MET B 302 ? 0.5285 0.5023 0.4872 -0.0040 0.0355  -0.0699 302 MET B CG    
5468 S SD    . MET B 302 ? 0.6731 0.6456 0.6197 -0.0026 0.0384  -0.0636 302 MET B SD    
5469 C CE    . MET B 302 ? 0.3229 0.2977 0.2737 -0.0035 0.0342  -0.0647 302 MET B CE    
5470 N N     . LYS B 303 ? 0.6123 0.5496 0.5435 0.0043  0.0174  -0.0877 303 LYS B N     
5471 C CA    . LYS B 303 ? 0.6409 0.5764 0.5772 0.0039  0.0163  -0.0913 303 LYS B CA    
5472 C C     . LYS B 303 ? 0.6429 0.5713 0.5647 0.0074  0.0192  -0.0910 303 LYS B C     
5473 O O     . LYS B 303 ? 0.3810 0.3164 0.3122 0.0058  0.0246  -0.0900 303 LYS B O     
5474 C CB    . LYS B 303 ? 0.6569 0.5828 0.5905 0.0036  0.0072  -0.0965 303 LYS B CB    
5475 C CG    . LYS B 303 ? 0.5778 0.5091 0.5277 0.0023  0.0048  -0.1002 303 LYS B CG    
5476 C CD    . LYS B 303 ? 0.6250 0.5542 0.5804 0.0021  -0.0050 -0.1044 303 LYS B CD    
5477 C CE    . LYS B 303 ? 0.7068 0.6394 0.6759 0.0021  -0.0083 -0.1080 303 LYS B CE    
5478 N NZ    . LYS B 303 ? 0.6787 0.6077 0.6502 0.0031  -0.0186 -0.1120 303 LYS B NZ    
5479 N N     . ASP B 304 ? 0.7244 0.6421 0.6263 0.0130  0.0150  -0.0926 304 ASP B N     
5480 C CA    . ASP B 304 ? 0.7268 0.6455 0.6224 0.0165  0.0159  -0.0946 304 ASP B CA    
5481 C C     . ASP B 304 ? 0.8283 0.7570 0.7272 0.0142  0.0261  -0.0887 304 ASP B C     
5482 O O     . ASP B 304 ? 0.9582 0.8886 0.8591 0.0133  0.0309  -0.0874 304 ASP B O     
5483 C CB    . ASP B 304 ? 0.6485 0.5722 0.5420 0.0174  0.0111  -0.1009 304 ASP B CB    
5484 C CG    . ASP B 304 ? 0.7269 0.6548 0.6328 0.0078  0.0102  -0.1090 304 ASP B CG    
5485 O OD1   . ASP B 304 ? 0.7487 0.6363 0.6268 0.0020  0.0140  -0.0986 304 ASP B OD1   
5486 O OD2   . ASP B 304 ? 0.7248 0.6412 0.6150 0.0040  0.0110  -0.1094 304 ASP B OD2   
5487 N N     . HIS B 305 ? 0.7150 0.6493 0.6142 0.0128  0.0293  -0.0841 305 HIS B N     
5488 C CA    . HIS B 305 ? 0.6591 0.5997 0.5584 0.0109  0.0372  -0.0776 305 HIS B CA    
5489 C C     . HIS B 305 ? 0.6631 0.6137 0.5765 0.0063  0.0434  -0.0703 305 HIS B C     
5490 O O     . HIS B 305 ? 0.7423 0.6973 0.6575 0.0042  0.0493  -0.0649 305 HIS B O     
5491 C CB    . HIS B 305 ? 0.4028 0.3420 0.2917 0.0122  0.0366  -0.0771 305 HIS B CB    
5492 C CG    . HIS B 305 ? 0.4586 0.3909 0.3359 0.0144  0.0328  -0.0835 305 HIS B CG    
5493 N ND1   . HIS B 305 ? 0.5441 0.4730 0.4120 0.0144  0.0310  -0.0848 305 HIS B ND1   
5494 C CD2   . HIS B 305 ? 0.5603 0.4881 0.4342 0.0156  0.0311  -0.0887 305 HIS B CD2   
5495 C CE1   . HIS B 305 ? 0.6150 0.5364 0.4734 0.0150  0.0289  -0.0899 305 HIS B CE1   
5496 N NE2   . HIS B 305 ? 0.5885 0.5098 0.4509 0.0158  0.0288  -0.0927 305 HIS B NE2   
5497 N N     . ILE B 306 ? 0.5326 0.4876 0.4574 0.0038  0.0424  -0.0703 306 ILE B N     
5498 C CA    . ILE B 306 ? 0.4310 0.3982 0.3722 -0.0010 0.0480  -0.0639 306 ILE B CA    
5499 C C     . ILE B 306 ? 0.3546 0.3285 0.3128 -0.0043 0.0479  -0.0662 306 ILE B C     
5500 O O     . ILE B 306 ? 0.3512 0.3326 0.3215 -0.0069 0.0473  -0.0655 306 ILE B O     
5501 C CB    . ILE B 306 ? 0.3600 0.3310 0.3020 -0.0018 0.0480  -0.0599 306 ILE B CB    
5502 C CG1   . ILE B 306 ? 0.4000 0.3647 0.3263 0.0012  0.0474  -0.0591 306 ILE B CG1   
5503 C CG2   . ILE B 306 ? 0.1574 0.1388 0.1140 -0.0071 0.0531  -0.0534 306 ILE B CG2   
5504 C CD1   . ILE B 306 ? 0.4669 0.4341 0.3933 0.0000  0.0478  -0.0558 306 ILE B CD1   
5505 N N     . PRO B 307 ? 0.4257 0.3989 0.3875 -0.0045 0.0486  -0.0689 307 PRO B N     
5506 C CA    . PRO B 307 ? 0.4766 0.4578 0.4571 -0.0075 0.0479  -0.0717 307 PRO B CA    
5507 C C     . PRO B 307 ? 0.3122 0.3076 0.3120 -0.0124 0.0519  -0.0660 307 PRO B C     
5508 O O     . PRO B 307 ? 0.2129 0.2167 0.2304 -0.0150 0.0511  -0.0678 307 PRO B O     
5509 C CB    . PRO B 307 ? 0.4692 0.4453 0.4471 -0.0062 0.0480  -0.0751 307 PRO B CB    
5510 C CG    . PRO B 307 ? 0.5460 0.5165 0.5093 -0.0042 0.0512  -0.0717 307 PRO B CG    
5511 C CD    . PRO B 307 ? 0.5489 0.5144 0.4987 -0.0017 0.0493  -0.0702 307 PRO B CD    
5512 N N     . THR B 308 ? 0.2859 0.2832 0.2828 -0.0134 0.0545  -0.0590 308 THR B N     
5513 C CA    . THR B 308 ? 0.4174 0.4234 0.4289 -0.0179 0.0556  -0.0539 308 THR B CA    
5514 C C     . THR B 308 ? 0.3535 0.3637 0.3699 -0.0187 0.0530  -0.0525 308 THR B C     
5515 O O     . THR B 308 ? 0.3587 0.3729 0.3853 -0.0224 0.0525  -0.0500 308 THR B O     
5516 C CB    . THR B 308 ? 0.3486 0.3517 0.3563 -0.0206 0.0596  -0.0501 308 THR B CB    
5517 O OG1   . THR B 308 ? 0.4135 0.4121 0.4095 -0.0193 0.0603  -0.0482 308 THR B OG1   
5518 C CG2   . THR B 308 ? 0.3017 0.3004 0.3039 -0.0198 0.0624  -0.0513 308 THR B CG2   
5519 N N     . LEU B 309 ? 0.3409 0.3479 0.3500 -0.0161 0.0510  -0.0561 309 LEU B N     
5520 C CA    . LEU B 309 ? 0.3620 0.3735 0.3768 -0.0171 0.0488  -0.0556 309 LEU B CA    
5521 C C     . LEU B 309 ? 0.1607 0.1757 0.1857 -0.0170 0.0454  -0.0630 309 LEU B C     
5522 O O     . LEU B 309 ? 0.1661 0.1746 0.1856 -0.0144 0.0430  -0.0690 309 LEU B O     
5523 C CB    . LEU B 309 ? 0.3908 0.3957 0.3897 -0.0145 0.0485  -0.0540 309 LEU B CB    
5524 C CG    . LEU B 309 ? 0.3672 0.3708 0.3613 -0.0157 0.0516  -0.0480 309 LEU B CG    
5525 C CD1   . LEU B 309 ? 0.4307 0.4292 0.4120 -0.0136 0.0514  -0.0467 309 LEU B CD1   
5526 C CD2   . LEU B 309 ? 0.3025 0.3124 0.3110 -0.0206 0.0520  -0.0449 309 LEU B CD2   
5527 N N     . SER B 310 ? 0.0903 0.1138 0.1297 -0.0194 0.0434  -0.0622 310 SER B N     
5528 C CA    . SER B 310 ? 0.4262 0.4546 0.4782 -0.0187 0.0388  -0.0688 310 SER B CA    
5529 C C     . SER B 310 ? 0.4224 0.4506 0.4704 -0.0177 0.0363  -0.0688 310 SER B C     
5530 O O     . SER B 310 ? 0.3489 0.3814 0.4002 -0.0202 0.0376  -0.0632 310 SER B O     
5531 C CB    . SER B 310 ? 0.4094 0.4464 0.4825 -0.0220 0.0371  -0.0682 310 SER B CB    
5532 O OG    . SER B 310 ? 0.4163 0.4586 0.5019 -0.0219 0.0321  -0.0715 310 SER B OG    
5533 N N     . VAL B 311 ? 0.5012 0.5205 0.5392 -0.0140 0.0301  -0.0742 311 VAL B N     
5534 C CA    . VAL B 311 ? 0.3950 0.4116 0.4271 -0.0128 0.0260  -0.0744 311 VAL B CA    
5535 C C     . VAL B 311 ? 0.3989 0.4214 0.4485 -0.0122 0.0183  -0.0783 311 VAL B C     
5536 O O     . VAL B 311 ? 0.4606 0.4793 0.5137 -0.0105 0.0122  -0.0821 311 VAL B O     
5537 C CB    . VAL B 311 ? 0.2915 0.2903 0.2965 -0.0094 0.0221  -0.0757 311 VAL B CB    
5538 C CG1   . VAL B 311 ? 0.1587 0.1464 0.1557 -0.0069 0.0163  -0.0806 311 VAL B CG1   
5539 C CG2   . VAL B 311 ? 0.2116 0.2072 0.2121 -0.0083 0.0159  -0.0765 311 VAL B CG2   
5540 N N     . THR B 312 ? 0.4202 0.4520 0.4813 -0.0134 0.0182  -0.0764 312 THR B N     
5541 C CA    . THR B 312 ? 0.3176 0.3539 0.3940 -0.0119 0.0101  -0.0782 312 THR B CA    
5542 C C     . THR B 312 ? 0.4621 0.4847 0.5208 -0.0093 0.0009  -0.0799 312 THR B C     
5543 O O     . THR B 312 ? 0.5649 0.5822 0.6087 -0.0094 0.0021  -0.0784 312 THR B O     
5544 C CB    . THR B 312 ? 0.1729 0.2230 0.2668 -0.0126 0.0143  -0.0748 312 THR B CB    
5545 O OG1   . THR B 312 ? 0.3780 0.4248 0.4615 -0.0129 0.0120  -0.0733 312 THR B OG1   
5546 C CG2   . THR B 312 ? 0.1067 0.1524 0.1926 -0.0160 0.0210  -0.0688 312 THR B CG2   
5547 N N     . LYS B 313 ? 0.3884 0.4055 0.4487 -0.0071 -0.0081 -0.0827 313 LYS B N     
5548 C CA    . LYS B 313 ? 0.3238 0.3273 0.3666 -0.0049 -0.0167 -0.0843 313 LYS B CA    
5549 C C     . LYS B 313 ? 0.3885 0.3969 0.4376 -0.0047 -0.0204 -0.0817 313 LYS B C     
5550 O O     . LYS B 313 ? 0.3467 0.3663 0.4169 -0.0046 -0.0215 -0.0796 313 LYS B O     
5551 C CB    . LYS B 313 ? 0.3230 0.3204 0.3669 -0.0027 -0.0250 -0.0875 313 LYS B CB    
5552 C CG    . LYS B 313 ? 0.4427 0.4271 0.4691 -0.0006 -0.0332 -0.0890 313 LYS B CG    
5553 C CD    . LYS B 313 ? 0.4519 0.4214 0.4565 0.0006  -0.0339 -0.0921 313 LYS B CD    
5554 C CE    . LYS B 313 ? 0.4279 0.3868 0.4185 0.0028  -0.0420 -0.0936 313 LYS B CE    
5555 N NZ    . LYS B 313 ? 0.4462 0.3981 0.4177 0.0026  -0.0392 -0.0917 313 LYS B NZ    
5556 N N     . PRO B 314 ? 0.4982 0.4980 0.5291 -0.0043 -0.0215 -0.0810 314 PRO B N     
5557 C CA    . PRO B 314 ? 0.4540 0.4573 0.4897 -0.0039 -0.0259 -0.0786 314 PRO B CA    
5558 C C     . PRO B 314 ? 0.2899 0.2876 0.3260 -0.0014 -0.0364 -0.0799 314 PRO B C     
5559 O O     . PRO B 314 ? 0.1896 0.1781 0.2168 0.0001  -0.0408 -0.0831 314 PRO B O     
5560 C CB    . PRO B 314 ? 0.2971 0.2921 0.3110 -0.0043 -0.0224 -0.0775 314 PRO B CB    
5561 C CG    . PRO B 314 ? 0.2015 0.1830 0.1946 -0.0033 -0.0208 -0.0798 314 PRO B CG    
5562 C CD    . PRO B 314 ? 0.4176 0.4043 0.4223 -0.0039 -0.0177 -0.0815 314 PRO B CD    
5563 N N     . GLU B 315 ? 0.4038 0.4079 0.4517 -0.0009 -0.0399 -0.0771 315 GLU B N     
5564 C CA    . GLU B 315 ? 0.5060 0.5055 0.5544 0.0017  -0.0491 -0.0777 315 GLU B CA    
5565 C C     . GLU B 315 ? 0.4584 0.4542 0.4967 0.0021  -0.0516 -0.0756 315 GLU B C     
5566 O O     . GLU B 315 ? 0.2947 0.2864 0.3320 0.0043  -0.0589 -0.0759 315 GLU B O     
5567 C CB    . GLU B 315 ? 0.3282 0.3373 0.4002 0.0029  -0.0507 -0.0759 315 GLU B CB    
5568 C CG    . GLU B 315 ? 0.3240 0.3385 0.4068 0.0022  -0.0460 -0.0771 315 GLU B CG    
5569 C CD    . GLU B 315 ? 0.4246 0.4487 0.5285 0.0032  -0.0432 -0.0736 315 GLU B CD    
5570 O OE1   . GLU B 315 ? 0.4909 0.5173 0.6044 0.0039  -0.0420 -0.0749 315 GLU B OE1   
5571 O OE2   . GLU B 315 ? 0.3683 0.3956 0.4766 0.0035  -0.0418 -0.0693 315 GLU B OE2   
5572 N N     . GLY B 316 ? 0.3547 0.3516 0.3852 0.0001  -0.0455 -0.0737 316 GLY B N     
5573 C CA    . GLY B 316 ? 0.4060 0.3989 0.4252 0.0003  -0.0469 -0.0718 316 GLY B CA    
5574 C C     . GLY B 316 ? 0.3659 0.3569 0.3716 -0.0017 -0.0389 -0.0710 316 GLY B C     
5575 O O     . GLY B 316 ? 0.3610 0.3535 0.3657 -0.0030 -0.0322 -0.0720 316 GLY B O     
5576 N N     . PHE B 318 ? 0.2281 0.1996 0.1781 -0.0038 -0.0182 -0.0673 318 PHE B N     
5577 C CA    . PHE B 318 ? 0.4289 0.3885 0.3587 -0.0037 -0.0124 -0.0674 318 PHE B CA    
5578 C C     . PHE B 318 ? 0.4968 0.4621 0.4303 -0.0034 -0.0032 -0.0646 318 PHE B C     
5579 O O     . PHE B 318 ? 0.4227 0.3818 0.3420 -0.0004 0.0018  -0.0617 318 PHE B O     
5580 C CB    . PHE B 318 ? 0.4830 0.4361 0.3958 -0.0044 -0.0106 -0.0664 318 PHE B CB    
5581 C CG    . PHE B 318 ? 0.3789 0.3353 0.2916 -0.0054 -0.0074 -0.0621 318 PHE B CG    
5582 C CD1   . PHE B 318 ? 0.3182 0.2799 0.2402 -0.0045 -0.0144 -0.0617 318 PHE B CD1   
5583 C CD2   . PHE B 318 ? 0.3553 0.3138 0.2649 0.0030  -0.0039 -0.0570 318 PHE B CD2   
5584 C CE1   . PHE B 318 ? 0.2902 0.2552 0.2123 -0.0052 -0.0115 -0.0579 318 PHE B CE1   
5585 C CE2   . PHE B 318 ? 0.3294 0.2949 0.2422 0.0021  -0.0006 -0.0539 318 PHE B CE2   
5586 C CZ    . PHE B 318 ? 0.3009 0.2635 0.2152 -0.0022 -0.0044 -0.0531 318 PHE B CZ    
5587 N N     . LEU B 319 ? 0.4435 0.4246 0.4000 -0.0055 -0.0009 -0.0652 319 LEU B N     
5588 C CA    . LEU B 319 ? 0.3367 0.3277 0.3018 -0.0075 0.0093  -0.0621 319 LEU B CA    
5589 C C     . LEU B 319 ? 0.4335 0.4279 0.4088 -0.0081 0.0096  -0.0651 319 LEU B C     
5590 O O     . LEU B 319 ? 0.3944 0.3911 0.3811 -0.0079 0.0025  -0.0691 319 LEU B O     
5591 C CB    . LEU B 319 ? 0.2462 0.2534 0.2297 -0.0107 0.0134  -0.0592 319 LEU B CB    
5592 C CG    . LEU B 319 ? 0.2394 0.2437 0.2142 -0.0102 0.0121  -0.0565 319 LEU B CG    
5593 C CD1   . LEU B 319 ? 0.2838 0.3040 0.2786 -0.0131 0.0141  -0.0550 319 LEU B CD1   
5594 C CD2   . LEU B 319 ? 0.1883 0.1851 0.1468 -0.0087 0.0181  -0.0508 319 LEU B CD2   
5595 N N     . LEU B 320 ? 0.2811 0.2758 0.2533 -0.0085 0.0172  -0.0624 320 LEU B N     
5596 C CA    . LEU B 320 ? 0.3107 0.3072 0.2902 -0.0089 0.0181  -0.0650 320 LEU B CA    
5597 C C     . LEU B 320 ? 0.2141 0.2253 0.2113 -0.0125 0.0264  -0.0608 320 LEU B C     
5598 O O     . LEU B 320 ? 0.3662 0.3788 0.3599 -0.0135 0.0318  -0.0543 320 LEU B O     
5599 C CB    . LEU B 320 ? 0.3889 0.3705 0.3476 -0.0057 0.0180  -0.0656 320 LEU B CB    
5600 C CG    . LEU B 320 ? 0.3663 0.3455 0.3290 -0.0053 0.0152  -0.0702 320 LEU B CG    
5601 C CD1   . LEU B 320 ? 0.2469 0.2172 0.2058 -0.0037 0.0044  -0.0754 320 LEU B CD1   
5602 C CD2   . LEU B 320 ? 0.3585 0.3289 0.3062 -0.0029 0.0190  -0.0689 320 LEU B CD2   
5603 N N     . TRP B 321 ? 0.1567 0.1780 0.1738 -0.0141 0.0255  -0.0637 321 TRP B N     
5604 C CA    . TRP B 321 ? 0.2381 0.2722 0.2734 -0.0179 0.0305  -0.0593 321 TRP B CA    
5605 C C     . TRP B 321 ? 0.2353 0.2683 0.2728 -0.0184 0.0326  -0.0599 321 TRP B C     
5606 O O     . TRP B 321 ? 0.1898 0.2245 0.2363 -0.0173 0.0294  -0.0657 321 TRP B O     
5607 C CB    . TRP B 321 ? 0.0585 0.1032 0.1147 -0.0194 0.0265  -0.0614 321 TRP B CB    
5608 C CG    . TRP B 321 ? 0.1516 0.1918 0.2077 -0.0194 0.0257  -0.0532 321 TRP B CG    
5609 C CD1   . TRP B 321 ? 0.3485 0.3866 0.4102 -0.0169 0.0234  -0.0508 321 TRP B CD1   
5610 C CD2   . TRP B 321 ? 0.0857 0.1213 0.1317 -0.0181 0.0262  -0.0434 321 TRP B CD2   
5611 N NE1   . TRP B 321 ? 0.2589 0.2935 0.3172 -0.0163 0.0241  -0.0448 321 TRP B NE1   
5612 C CE2   . TRP B 321 ? 0.1843 0.2179 0.2347 -0.0176 0.0258  -0.0422 321 TRP B CE2   
5613 C CE3   . TRP B 321 ? 0.1691 0.2030 0.2064 -0.0190 0.0283  -0.0407 321 TRP B CE3   
5614 C CZ2   . TRP B 321 ? 0.1419 0.1728 0.1889 -0.0179 0.0269  -0.0389 321 TRP B CZ2   
5615 C CZ3   . TRP B 321 ? 0.1932 0.2245 0.2284 -0.0197 0.0288  -0.0377 321 TRP B CZ3   
5616 C CH2   . TRP B 321 ? 0.0659 0.0960 0.1058 -0.0190 0.0280  -0.0370 321 TRP B CH2   
5617 N N     . ILE B 322 ? 0.3105 0.3399 0.3407 -0.0193 0.0364  -0.0534 322 ILE B N     
5618 C CA    . ILE B 322 ? 0.2935 0.3196 0.3211 -0.0190 0.0387  -0.0538 322 ILE B CA    
5619 C C     . ILE B 322 ? 0.2125 0.2403 0.2472 -0.0204 0.0382  -0.0476 322 ILE B C     
5620 O O     . ILE B 322 ? 0.2272 0.2536 0.2603 -0.0215 0.0381  -0.0435 322 ILE B O     
5621 C CB    . ILE B 322 ? 0.2125 0.2281 0.2199 -0.0162 0.0412  -0.0520 322 ILE B CB    
5622 C CG1   . ILE B 322 ? 0.2237 0.2304 0.2155 -0.0130 0.0382  -0.0554 322 ILE B CG1   
5623 C CG2   . ILE B 322 ? 0.2627 0.2736 0.2660 -0.0150 0.0423  -0.0550 322 ILE B CG2   
5624 C CD1   . ILE B 322 ? 0.2909 0.2890 0.2650 -0.0103 0.0399  -0.0512 322 ILE B CD1   
5625 N N     . ASP B 323 ? 0.3095 0.3388 0.3521 -0.0212 0.0380  -0.0500 323 ASP B N     
5626 C CA    . ASP B 323 ? 0.0649 0.0921 0.1111 -0.0224 0.0380  -0.0475 323 ASP B CA    
5627 C C     . ASP B 323 ? 0.1588 0.1823 0.1982 -0.0234 0.0420  -0.0462 323 ASP B C     
5628 O O     . ASP B 323 ? 0.3305 0.3533 0.3663 -0.0223 0.0439  -0.0478 323 ASP B O     
5629 C CB    . ASP B 323 ? 0.0961 0.1248 0.1526 -0.0219 0.0357  -0.0503 323 ASP B CB    
5630 C CG    . ASP B 323 ? 0.2216 0.2471 0.2807 -0.0220 0.0359  -0.0486 323 ASP B CG    
5631 O OD1   . ASP B 323 ? 0.2020 0.2251 0.2558 -0.0224 0.0372  -0.0456 323 ASP B OD1   
5632 O OD2   . ASP B 323 ? 0.1777 0.2028 0.2439 -0.0211 0.0349  -0.0502 323 ASP B OD2   
5633 N N     . CYS B 324 ? 0.2805 0.3008 0.3173 -0.0245 0.0430  -0.0435 324 CYS B N     
5634 C CA    . CYS B 324 ? 0.3430 0.3594 0.3746 -0.0254 0.0464  -0.0421 324 CYS B CA    
5635 C C     . CYS B 324 ? 0.3313 0.3462 0.3682 -0.0258 0.0462  -0.0419 324 CYS B C     
5636 O O     . CYS B 324 ? 0.1748 0.1865 0.2086 -0.0262 0.0482  -0.0404 324 CYS B O     
5637 C CB    . CYS B 324 ? 0.3673 0.3808 0.3912 -0.0255 0.0478  -0.0394 324 CYS B CB    
5638 S SG    . CYS B 324 ? 0.2187 0.2315 0.2328 -0.0240 0.0486  -0.0387 324 CYS B SG    
5639 N N     . SER B 325 ? 0.3637 0.3804 0.4082 -0.0251 0.0441  -0.0436 325 SER B N     
5640 C CA    . SER B 325 ? 0.2754 0.2903 0.3240 -0.0245 0.0439  -0.0429 325 SER B CA    
5641 C C     . SER B 325 ? 0.3935 0.4063 0.4423 -0.0254 0.0465  -0.0438 325 SER B C     
5642 O O     . SER B 325 ? 0.4979 0.5083 0.5467 -0.0252 0.0476  -0.0424 325 SER B O     
5643 C CB    . SER B 325 ? 0.0989 0.1156 0.1550 -0.0229 0.0412  -0.0440 325 SER B CB    
5644 O OG    . SER B 325 ? 0.2828 0.2978 0.3420 -0.0216 0.0410  -0.0422 325 SER B OG    
5645 N N     . ALA B 326 ? 0.3264 0.3404 0.3754 -0.0262 0.0476  -0.0459 326 ALA B N     
5646 C CA    . ALA B 326 ? 0.3851 0.3972 0.4342 -0.0270 0.0502  -0.0468 326 ALA B CA    
5647 C C     . ALA B 326 ? 0.3572 0.3656 0.3989 -0.0278 0.0532  -0.0446 326 ALA B C     
5648 O O     . ALA B 326 ? 0.3540 0.3599 0.3958 -0.0283 0.0553  -0.0447 326 ALA B O     
5649 C CB    . ALA B 326 ? 0.2930 0.3076 0.3435 -0.0272 0.0505  -0.0496 326 ALA B CB    
5650 N N     . LEU B 327 ? 0.3663 0.3739 0.4020 -0.0278 0.0535  -0.0428 327 LEU B N     
5651 C CA    . LEU B 327 ? 0.2649 0.2686 0.2940 -0.0283 0.0563  -0.0409 327 LEU B CA    
5652 C C     . LEU B 327 ? 0.3449 0.3468 0.3761 -0.0280 0.0561  -0.0395 327 LEU B C     
5653 O O     . LEU B 327 ? 0.5211 0.5198 0.5489 -0.0285 0.0586  -0.0385 327 LEU B O     
5654 C CB    . LEU B 327 ? 0.0940 0.0971 0.1162 -0.0280 0.0565  -0.0395 327 LEU B CB    
5655 C CG    . LEU B 327 ? 0.2412 0.2445 0.2571 -0.0271 0.0577  -0.0402 327 LEU B CG    
5656 C CD1   . LEU B 327 ? 0.3842 0.3838 0.3905 -0.0266 0.0594  -0.0383 327 LEU B CD1   
5657 C CD2   . LEU B 327 ? 0.3018 0.3035 0.3155 -0.0269 0.0602  -0.0418 327 LEU B CD2   
5658 N N     . ASN B 328 ? 0.3048 0.3087 0.3413 -0.0270 0.0534  -0.0393 328 ASN B N     
5659 C CA    . ASN B 328 ? 0.3438 0.3465 0.3818 -0.0261 0.0531  -0.0377 328 ASN B CA    
5660 C C     . ASN B 328 ? 0.3970 0.3978 0.4297 -0.0263 0.0542  -0.0359 328 ASN B C     
5661 O O     . ASN B 328 ? 0.2389 0.2372 0.2703 -0.0265 0.0561  -0.0352 328 ASN B O     
5662 C CB    . ASN B 328 ? 0.3262 0.3270 0.3670 -0.0262 0.0548  -0.0382 328 ASN B CB    
5663 C CG    . ASN B 328 ? 0.4421 0.4444 0.4888 -0.0259 0.0538  -0.0399 328 ASN B CG    
5664 O OD1   . ASN B 328 ? 0.4781 0.4828 0.5282 -0.0250 0.0514  -0.0404 328 ASN B OD1   
5665 N ND2   . ASN B 328 ? 0.5585 0.5592 0.6069 -0.0264 0.0557  -0.0409 328 ASN B ND2   
5666 N N     . LEU B 329 ? 0.4016 0.4037 0.4319 -0.0262 0.0528  -0.0353 329 LEU B N     
5667 C CA    . LEU B 329 ? 0.1787 0.1792 0.2042 -0.0264 0.0536  -0.0338 329 LEU B CA    
5668 C C     . LEU B 329 ? 0.1060 0.1087 0.1333 -0.0252 0.0509  -0.0325 329 LEU B C     
5669 O O     . LEU B 329 ? 0.4475 0.4529 0.4777 -0.0245 0.0485  -0.0329 329 LEU B O     
5670 C CB    . LEU B 329 ? 0.0906 0.0901 0.1103 -0.0272 0.0551  -0.0339 329 LEU B CB    
5671 C CG    . LEU B 329 ? 0.2362 0.2329 0.2522 -0.0280 0.0583  -0.0347 329 LEU B CG    
5672 C CD1   . LEU B 329 ? 0.1024 0.0981 0.1116 -0.0280 0.0595  -0.0344 329 LEU B CD1   
5673 C CD2   . LEU B 329 ? 0.2863 0.2789 0.3002 -0.0285 0.0612  -0.0340 329 LEU B CD2   
5674 N N     . SER B 330 ? 0.1732 0.1747 0.1989 -0.0249 0.0513  -0.0312 330 SER B N     
5675 C CA    . SER B 330 ? 0.2665 0.2698 0.2927 -0.0239 0.0490  -0.0299 330 SER B CA    
5676 C C     . SER B 330 ? 0.4283 0.4322 0.4509 -0.0243 0.0486  -0.0297 330 SER B C     
5677 O O     . SER B 330 ? 0.3379 0.3400 0.3564 -0.0254 0.0505  -0.0302 330 SER B O     
5678 C CB    . SER B 330 ? 0.1994 0.2015 0.2252 -0.0234 0.0497  -0.0286 330 SER B CB    
5679 O OG    . SER B 330 ? 0.2735 0.2738 0.2949 -0.0241 0.0510  -0.0281 330 SER B OG    
5680 N N     . GLN B 331 ? 0.4321 0.4382 0.4556 -0.0234 0.0461  -0.0287 331 GLN B N     
5681 C CA    . GLN B 331 ? 0.1492 0.1555 0.1691 -0.0237 0.0456  -0.0282 331 GLN B CA    
5682 C C     . GLN B 331 ? 0.1804 0.1836 0.1959 -0.0244 0.0481  -0.0275 331 GLN B C     
5683 O O     . GLN B 331 ? 0.1291 0.1305 0.1400 -0.0252 0.0498  -0.0275 331 GLN B O     
5684 C CB    . GLN B 331 ? 0.1969 0.2059 0.2189 -0.0224 0.0427  -0.0271 331 GLN B CB    
5685 C CG    . GLN B 331 ? 0.0682 0.0782 0.0875 -0.0225 0.0417  -0.0266 331 GLN B CG    
5686 C CD    . GLN B 331 ? 0.2221 0.2345 0.2437 -0.0211 0.0389  -0.0255 331 GLN B CD    
5687 O OE1   . GLN B 331 ? 0.2572 0.2702 0.2818 -0.0200 0.0380  -0.0248 331 GLN B OE1   
5688 N NE2   . GLN B 331 ? 0.3063 0.3200 0.3263 -0.0211 0.0376  -0.0251 331 GLN B NE2   
5689 N N     . ASP B 332 ? 0.3001 0.3022 0.3166 -0.0241 0.0488  -0.0269 332 ASP B N     
5690 C CA    . ASP B 332 ? 0.2449 0.2436 0.2576 -0.0247 0.0514  -0.0264 332 ASP B CA    
5691 C C     . ASP B 332 ? 0.2677 0.2629 0.2774 -0.0258 0.0547  -0.0272 332 ASP B C     
5692 O O     . ASP B 332 ? 0.3593 0.3512 0.3639 -0.0264 0.0571  -0.0268 332 ASP B O     
5693 C CB    . ASP B 332 ? 0.0966 0.0952 0.1117 -0.0241 0.0513  -0.0258 332 ASP B CB    
5694 C CG    . ASP B 332 ? 0.3247 0.3268 0.3429 -0.0228 0.0482  -0.0248 332 ASP B CG    
5695 O OD1   . ASP B 332 ? 0.4145 0.4174 0.4312 -0.0226 0.0471  -0.0241 332 ASP B OD1   
5696 O OD2   . ASP B 332 ? 0.3447 0.3484 0.3665 -0.0219 0.0469  -0.0247 332 ASP B OD2   
5697 N N     . GLU B 333 ? 0.3791 0.3746 0.3913 -0.0259 0.0550  -0.0281 333 GLU B N     
5698 C CA    . GLU B 333 ? 0.4450 0.4373 0.4541 -0.0268 0.0580  -0.0288 333 GLU B CA    
5699 C C     . GLU B 333 ? 0.3721 0.3639 0.3767 -0.0272 0.0586  -0.0290 333 GLU B C     
5700 O O     . GLU B 333 ? 0.3389 0.3267 0.3375 -0.0276 0.0615  -0.0287 333 GLU B O     
5701 C CB    . GLU B 333 ? 0.4963 0.4895 0.5095 -0.0268 0.0579  -0.0299 333 GLU B CB    
5702 C CG    . GLU B 333 ? 0.3283 0.3193 0.3426 -0.0269 0.0598  -0.0297 333 GLU B CG    
5703 C CD    . GLU B 333 ? 0.2225 0.2149 0.2418 -0.0264 0.0589  -0.0304 333 GLU B CD    
5704 O OE1   . GLU B 333 ? 0.2474 0.2429 0.2700 -0.0259 0.0565  -0.0308 333 GLU B OE1   
5705 O OE2   . GLU B 333 ? 0.2623 0.2528 0.2823 -0.0266 0.0608  -0.0305 333 GLU B OE2   
5706 N N     . ARG B 334 ? 0.4858 0.4814 0.4928 -0.0268 0.0558  -0.0295 334 ARG B N     
5707 C CA    . ARG B 334 ? 0.4291 0.4247 0.4319 -0.0268 0.0561  -0.0297 334 ARG B CA    
5708 C C     . ARG B 334 ? 0.3642 0.3578 0.3611 -0.0266 0.0569  -0.0284 334 ARG B C     
5709 O O     . ARG B 334 ? 0.3028 0.2929 0.2925 -0.0263 0.0592  -0.0281 334 ARG B O     
5710 C CB    . ARG B 334 ? 0.4227 0.4232 0.4305 -0.0264 0.0528  -0.0307 334 ARG B CB    
5711 C CG    . ARG B 334 ? 0.3259 0.3273 0.3301 -0.0261 0.0529  -0.0313 334 ARG B CG    
5712 C CD    . ARG B 334 ? 0.1814 0.1877 0.1921 -0.0258 0.0497  -0.0326 334 ARG B CD    
5713 N NE    . ARG B 334 ? 0.0795 0.0885 0.0937 -0.0252 0.0466  -0.0319 334 ARG B NE    
5714 C CZ    . ARG B 334 ? 0.1611 0.1720 0.1814 -0.0247 0.0444  -0.0322 334 ARG B CZ    
5715 N NH1   . ARG B 334 ? 0.5207 0.5311 0.5445 -0.0248 0.0450  -0.0331 334 ARG B NH1   
5716 N NH2   . ARG B 334 ? 0.0688 0.0818 0.0912 -0.0238 0.0418  -0.0313 334 ARG B NH2   
5717 N N     . THR B 335 ? 0.2471 0.2423 0.2463 -0.0263 0.0549  -0.0275 335 THR B N     
5718 C CA    . THR B 335 ? 0.2910 0.2844 0.2851 -0.0260 0.0555  -0.0263 335 THR B CA    
5719 C C     . THR B 335 ? 0.3899 0.3775 0.3779 -0.0263 0.0594  -0.0256 335 THR B C     
5720 O O     . THR B 335 ? 0.3914 0.3753 0.3720 -0.0259 0.0613  -0.0250 335 THR B O     
5721 C CB    . THR B 335 ? 0.0958 0.0919 0.0939 -0.0256 0.0529  -0.0255 335 THR B CB    
5722 O OG1   . THR B 335 ? 0.2705 0.2711 0.2720 -0.0251 0.0496  -0.0258 335 THR B OG1   
5723 C CG2   . THR B 335 ? 0.0997 0.0929 0.0928 -0.0256 0.0543  -0.0243 335 THR B CG2   
5724 N N     . LYS B 336 ? 0.3359 0.3220 0.3264 -0.0267 0.0606  -0.0257 336 LYS B N     
5725 C CA    . LYS B 336 ? 0.3412 0.3215 0.3264 -0.0270 0.0644  -0.0252 336 LYS B CA    
5726 C C     . LYS B 336 ? 0.4570 0.4332 0.4358 -0.0270 0.0672  -0.0255 336 LYS B C     
5727 O O     . LYS B 336 ? 0.5080 0.4789 0.4790 -0.0266 0.0699  -0.0247 336 LYS B O     
5728 C CB    . LYS B 336 ? 0.3336 0.3136 0.3233 -0.0274 0.0650  -0.0255 336 LYS B CB    
5729 C CG    . LYS B 336 ? 0.3255 0.3000 0.3112 -0.0277 0.0686  -0.0250 336 LYS B CG    
5730 C CD    . LYS B 336 ? 0.3212 0.2964 0.3120 -0.0278 0.0688  -0.0254 336 LYS B CD    
5731 C CE    . LYS B 336 ? 0.3716 0.3423 0.3599 -0.0280 0.0717  -0.0249 336 LYS B CE    
5732 N NZ    . LYS B 336 ? 0.4375 0.4020 0.4201 -0.0284 0.0759  -0.0249 336 LYS B NZ    
5733 N N     . LEU B 337 ? 0.3906 0.3689 0.3721 -0.0271 0.0667  -0.0266 337 LEU B N     
5734 C CA    . LEU B 337 ? 0.3477 0.3221 0.3227 -0.0268 0.0694  -0.0270 337 LEU B CA    
5735 C C     . LEU B 337 ? 0.1886 0.1614 0.1555 -0.0255 0.0694  -0.0266 337 LEU B C     
5736 O O     . LEU B 337 ? 0.2494 0.2159 0.2069 -0.0247 0.0723  -0.0262 337 LEU B O     
5737 C CB    . LEU B 337 ? 0.4240 0.4018 0.4042 -0.0272 0.0683  -0.0284 337 LEU B CB    
5738 C CG    . LEU B 337 ? 0.4002 0.3739 0.3765 -0.0273 0.0716  -0.0290 337 LEU B CG    
5739 C CD1   . LEU B 337 ? 0.3648 0.3336 0.3396 -0.0278 0.0745  -0.0283 337 LEU B CD1   
5740 C CD2   . LEU B 337 ? 0.4747 0.4524 0.4581 -0.0278 0.0702  -0.0304 337 LEU B CD2   
5741 N N     . LEU B 338 ? 0.2523 0.2299 0.2220 -0.0251 0.0662  -0.0268 338 LEU B N     
5742 C CA    . LEU B 338 ? 0.1699 0.1462 0.1316 -0.0234 0.0657  -0.0268 338 LEU B CA    
5743 C C     . LEU B 338 ? 0.3205 0.2914 0.2744 -0.0227 0.0675  -0.0253 338 LEU B C     
5744 O O     . LEU B 338 ? 0.4159 0.3815 0.3589 -0.0209 0.0688  -0.0253 338 LEU B O     
5745 C CB    . LEU B 338 ? 0.3319 0.3148 0.2993 -0.0231 0.0618  -0.0272 338 LEU B CB    
5746 C CG    . LEU B 338 ? 0.3017 0.2899 0.2764 -0.0234 0.0598  -0.0289 338 LEU B CG    
5747 C CD1   . LEU B 338 ? 0.3364 0.3309 0.3199 -0.0239 0.0560  -0.0290 338 LEU B CD1   
5748 C CD2   . LEU B 338 ? 0.2263 0.2131 0.1937 -0.0212 0.0600  -0.0306 338 LEU B CD2   
5749 N N     . GLU B 339 ? 0.4455 0.4169 0.4041 -0.0239 0.0675  -0.0243 339 GLU B N     
5750 C CA    . GLU B 339 ? 0.4133 0.3796 0.3656 -0.0235 0.0693  -0.0230 339 GLU B CA    
5751 C C     . GLU B 339 ? 0.4419 0.4005 0.3873 -0.0234 0.0736  -0.0227 339 GLU B C     
5752 O O     . GLU B 339 ? 0.4388 0.3909 0.3741 -0.0221 0.0756  -0.0221 339 GLU B O     
5753 C CB    . GLU B 339 ? 0.5556 0.5254 0.5156 -0.0245 0.0676  -0.0224 339 GLU B CB    
5754 C CG    . GLU B 339 ? 0.6593 0.6249 0.6149 -0.0243 0.0692  -0.0212 339 GLU B CG    
5755 C CD    . GLU B 339 ? 0.8007 0.7703 0.7642 -0.0251 0.0673  -0.0210 339 GLU B CD    
5756 O OE1   . GLU B 339 ? 0.8199 0.7946 0.7914 -0.0257 0.0650  -0.0217 339 GLU B OE1   
5757 O OE2   . GLU B 339 ? 0.8337 0.8010 0.7949 -0.0249 0.0680  -0.0201 339 GLU B OE2   
5758 N N     . GLU B 340 ? 0.4781 0.4368 0.4283 -0.0245 0.0749  -0.0233 340 GLU B N     
5759 C CA    . GLU B 340 ? 0.3783 0.3298 0.3231 -0.0246 0.0791  -0.0230 340 GLU B CA    
5760 C C     . GLU B 340 ? 0.3500 0.2959 0.2844 -0.0231 0.0812  -0.0233 340 GLU B C     
5761 O O     . GLU B 340 ? 0.4898 0.4284 0.4142 -0.0219 0.0836  -0.0226 340 GLU B O     
5762 C CB    . GLU B 340 ? 0.4736 0.4270 0.4261 -0.0259 0.0796  -0.0237 340 GLU B CB    
5763 C CG    . GLU B 340 ? 0.5609 0.5182 0.5219 -0.0269 0.0780  -0.0236 340 GLU B CG    
5764 C CD    . GLU B 340 ? 0.6716 0.6298 0.6384 -0.0277 0.0787  -0.0244 340 GLU B CD    
5765 O OE1   . GLU B 340 ? 0.6781 0.6342 0.6428 -0.0277 0.0804  -0.0249 340 GLU B OE1   
5766 O OE2   . GLU B 340 ? 0.6458 0.6065 0.6186 -0.0281 0.0775  -0.0245 340 GLU B OE2   
5767 N N     . LYS B 341 ? 0.3475 0.2964 0.2838 -0.0230 0.0802  -0.0245 341 LYS B N     
5768 C CA    . LYS B 341 ? 0.4919 0.4354 0.4180 -0.0213 0.0821  -0.0253 341 LYS B CA    
5769 C C     . LYS B 341 ? 0.4918 0.4361 0.4111 -0.0191 0.0794  -0.0262 341 LYS B C     
5770 O O     . LYS B 341 ? 0.5476 0.4851 0.4544 -0.0168 0.0805  -0.0266 341 LYS B O     
5771 C CB    . LYS B 341 ? 0.5809 0.5260 0.5113 -0.0221 0.0828  -0.0264 341 LYS B CB    
5772 C CG    . LYS B 341 ? 0.6175 0.5715 0.5589 -0.0231 0.0794  -0.0275 341 LYS B CG    
5773 C CD    . LYS B 341 ? 0.5931 0.5481 0.5400 -0.0243 0.0807  -0.0283 341 LYS B CD    
5774 C CE    . LYS B 341 ? 0.5832 0.5325 0.5206 -0.0229 0.0832  -0.0292 341 LYS B CE    
5775 N NZ    . LYS B 341 ? 0.4267 0.3754 0.3685 -0.0242 0.0853  -0.0296 341 LYS B NZ    
5776 N N     . GLY B 342 ? 0.4646 0.4167 0.3915 -0.0194 0.0757  -0.0267 342 GLY B N     
5777 C CA    . GLY B 342 ? 0.3400 0.2930 0.2607 -0.0169 0.0728  -0.0278 342 GLY B CA    
5778 C C     . GLY B 342 ? 0.4554 0.4039 0.3680 -0.0157 0.0727  -0.0267 342 GLY B C     
5779 O O     . GLY B 342 ? 0.5721 0.5163 0.4735 -0.0129 0.0715  -0.0279 342 GLY B O     
5780 N N     . LYS B 343 ? 0.4587 0.4076 0.3764 -0.0176 0.0738  -0.0247 343 LYS B N     
5781 C CA    . LYS B 343 ? 0.3790 0.3244 0.2907 -0.0167 0.0737  -0.0235 343 LYS B CA    
5782 C C     . LYS B 343 ? 0.4304 0.3797 0.3406 -0.0150 0.0696  -0.0244 343 LYS B C     
5783 O O     . LYS B 343 ? 0.4558 0.4000 0.3548 -0.0126 0.0688  -0.0248 343 LYS B O     
5784 C CB    . LYS B 343 ? 0.4262 0.3608 0.3241 -0.0150 0.0769  -0.0232 343 LYS B CB    
5785 C CG    . LYS B 343 ? 0.6116 0.5414 0.5100 -0.0163 0.0811  -0.0225 343 LYS B CG    
5786 C CD    . LYS B 343 ? 0.5445 0.4729 0.4473 -0.0179 0.0832  -0.0208 343 LYS B CD    
5787 C CE    . LYS B 343 ? 0.4003 0.3219 0.3005 -0.0185 0.0877  -0.0204 343 LYS B CE    
5788 N NZ    . LYS B 343 ? 0.3705 0.2953 0.2815 -0.0208 0.0886  -0.0200 343 LYS B NZ    
5789 N N     . ILE B 344 ? 0.2515 0.2096 0.1728 -0.0161 0.0668  -0.0248 344 ILE B N     
5790 C CA    . ILE B 344 ? 0.2416 0.2042 0.1631 -0.0146 0.0629  -0.0259 344 ILE B CA    
5791 C C     . ILE B 344 ? 0.3181 0.2889 0.2533 -0.0168 0.0609  -0.0248 344 ILE B C     
5792 O O     . ILE B 344 ? 0.3836 0.3575 0.3284 -0.0192 0.0617  -0.0244 344 ILE B O     
5793 C CB    . ILE B 344 ? 0.3705 0.3339 0.2887 -0.0124 0.0610  -0.0288 344 ILE B CB    
5794 C CG1   . ILE B 344 ? 0.4947 0.4636 0.4156 -0.0107 0.0564  -0.0305 344 ILE B CG1   
5795 C CG2   . ILE B 344 ? 0.3629 0.3294 0.2894 -0.0142 0.0624  -0.0293 344 ILE B CG2   
5796 C CD1   . ILE B 344 ? 0.5690 0.5371 0.4848 -0.0077 0.0537  -0.0346 344 ILE B CD1   
5797 N N     . ILE B 345 ? 0.4538 0.4271 0.3890 -0.0160 0.0583  -0.0245 345 ILE B N     
5798 C CA    . ILE B 345 ? 0.3961 0.3765 0.3430 -0.0178 0.0561  -0.0235 345 ILE B CA    
5799 C C     . ILE B 345 ? 0.4906 0.4766 0.4414 -0.0168 0.0526  -0.0249 345 ILE B C     
5800 O O     . ILE B 345 ? 0.5270 0.5115 0.4700 -0.0141 0.0508  -0.0259 345 ILE B O     
5801 C CB    . ILE B 345 ? 0.3576 0.3367 0.3029 -0.0180 0.0560  -0.0218 345 ILE B CB    
5802 C CG1   . ILE B 345 ? 0.3722 0.3450 0.3136 -0.0188 0.0596  -0.0207 345 ILE B CG1   
5803 C CG2   . ILE B 345 ? 0.1223 0.1086 0.0793 -0.0195 0.0531  -0.0213 345 ILE B CG2   
5804 C CD1   . ILE B 345 ? 0.2717 0.2456 0.2207 -0.0208 0.0611  -0.0209 345 ILE B CD1   
5805 N N     . VAL B 346 ? 0.4923 0.4842 0.4544 -0.0186 0.0515  -0.0255 346 VAL B N     
5806 C CA    . VAL B 346 ? 0.4271 0.4247 0.3950 -0.0181 0.0483  -0.0268 346 VAL B CA    
5807 C C     . VAL B 346 ? 0.3217 0.3252 0.3015 -0.0202 0.0460  -0.0259 346 VAL B C     
5808 O O     . VAL B 346 ? 0.1298 0.1327 0.1124 -0.0216 0.0465  -0.0246 346 VAL B O     
5809 C CB    . VAL B 346 ? 0.2359 0.2347 0.2060 -0.0178 0.0485  -0.0290 346 VAL B CB    
5810 C CG1   . VAL B 346 ? 0.3450 0.3368 0.3015 -0.0148 0.0500  -0.0307 346 VAL B CG1   
5811 C CG2   . VAL B 346 ? 0.1352 0.1358 0.1144 -0.0206 0.0496  -0.0285 346 VAL B CG2   
5812 N N     . GLU B 347 ? 0.1630 0.1715 0.1488 -0.0201 0.0431  -0.0269 347 GLU B N     
5813 C CA    . GLU B 347 ? 0.2135 0.2267 0.2092 -0.0215 0.0403  -0.0265 347 GLU B CA    
5814 C C     . GLU B 347 ? 0.4467 0.4612 0.4494 -0.0225 0.0400  -0.0276 347 GLU B C     
5815 O O     . GLU B 347 ? 0.4475 0.4627 0.4515 -0.0224 0.0405  -0.0292 347 GLU B O     
5816 C CB    . GLU B 347 ? 0.2823 0.2999 0.2817 -0.0207 0.0372  -0.0273 347 GLU B CB    
5817 C CG    . GLU B 347 ? 0.3679 0.3878 0.3714 -0.0210 0.0346  -0.0260 347 GLU B CG    
5818 C CD    . GLU B 347 ? 0.5617 0.5788 0.5585 -0.0206 0.0357  -0.0241 347 GLU B CD    
5819 O OE1   . GLU B 347 ? 0.7613 0.7793 0.7556 -0.0196 0.0345  -0.0238 347 GLU B OE1   
5820 O OE2   . GLU B 347 ? 0.6059 0.6197 0.6000 -0.0211 0.0376  -0.0229 347 GLU B OE2   
5821 N N     . PRO B 348 ? 0.4769 0.4911 0.4828 -0.0229 0.0395  -0.0268 348 PRO B N     
5822 C CA    . PRO B 348 ? 0.2113 0.2265 0.2230 -0.0230 0.0388  -0.0277 348 PRO B CA    
5823 C C     . PRO B 348 ? 0.2839 0.3029 0.3013 -0.0221 0.0355  -0.0285 348 PRO B C     
5824 O O     . PRO B 348 ? 0.3625 0.3832 0.3807 -0.0214 0.0335  -0.0276 348 PRO B O     
5825 C CB    . PRO B 348 ? 0.1539 0.1675 0.1658 -0.0229 0.0391  -0.0264 348 PRO B CB    
5826 C CG    . PRO B 348 ? 0.1756 0.1890 0.1844 -0.0227 0.0386  -0.0250 348 PRO B CG    
5827 C CD    . PRO B 348 ? 0.3508 0.3630 0.3543 -0.0229 0.0400  -0.0250 348 PRO B CD    
5828 N N     . GLY B 349 ? 0.0593 0.0793 0.0809 -0.0220 0.0353  -0.0301 349 GLY B N     
5829 C CA    . GLY B 349 ? 0.2480 0.2707 0.2752 -0.0209 0.0326  -0.0309 349 GLY B CA    
5830 C C     . GLY B 349 ? 0.2013 0.2239 0.2320 -0.0195 0.0314  -0.0295 349 GLY B C     
5831 O O     . GLY B 349 ? 0.1513 0.1756 0.1860 -0.0181 0.0294  -0.0294 349 GLY B O     
5832 N N     . GLU B 350 ? 0.1102 0.1307 0.1397 -0.0196 0.0326  -0.0284 350 GLU B N     
5833 C CA    . GLU B 350 ? 0.1484 0.1689 0.1813 -0.0181 0.0317  -0.0269 350 GLU B CA    
5834 C C     . GLU B 350 ? 0.0465 0.0684 0.0794 -0.0169 0.0296  -0.0251 350 GLU B C     
5835 O O     . GLU B 350 ? 0.0503 0.0728 0.0869 -0.0154 0.0283  -0.0240 350 GLU B O     
5836 C CB    . GLU B 350 ? 0.1059 0.1243 0.1373 -0.0184 0.0333  -0.0261 350 GLU B CB    
5837 C CG    . GLU B 350 ? 0.0547 0.0715 0.0876 -0.0190 0.0351  -0.0273 350 GLU B CG    
5838 C CD    . GLU B 350 ? 0.0591 0.0746 0.0886 -0.0207 0.0373  -0.0287 350 GLU B CD    
5839 O OE1   . GLU B 350 ? 0.1226 0.1367 0.1529 -0.0214 0.0390  -0.0298 350 GLU B OE1   
5840 O OE2   . GLU B 350 ? 0.2382 0.2538 0.2640 -0.0214 0.0375  -0.0286 350 GLU B OE2   
5841 N N     . LYS B 351 ? 0.0468 0.0691 0.0760 -0.0174 0.0293  -0.0248 351 LYS B N     
5842 C CA    . LYS B 351 ? 0.3059 0.3295 0.3351 -0.0163 0.0273  -0.0232 351 LYS B CA    
5843 C C     . LYS B 351 ? 0.2591 0.2848 0.2912 -0.0155 0.0256  -0.0237 351 LYS B C     
5844 O O     . LYS B 351 ? 0.3429 0.3697 0.3748 -0.0147 0.0240  -0.0224 351 LYS B O     
5845 C CB    . LYS B 351 ? 0.1655 0.1887 0.1900 -0.0172 0.0276  -0.0226 351 LYS B CB    
5846 C CG    . LYS B 351 ? 0.2548 0.2779 0.2762 -0.0186 0.0287  -0.0240 351 LYS B CG    
5847 C CD    . LYS B 351 ? 0.2260 0.2486 0.2432 -0.0191 0.0288  -0.0228 351 LYS B CD    
5848 C CE    . LYS B 351 ? 0.1809 0.2031 0.1943 -0.0202 0.0301  -0.0237 351 LYS B CE    
5849 N NZ    . LYS B 351 ? 0.2465 0.2676 0.2555 -0.0204 0.0306  -0.0223 351 LYS B NZ    
5850 N N     . TYR B 352 ? 0.3547 0.3810 0.3899 -0.0157 0.0258  -0.0257 352 TYR B N     
5851 C CA    . TYR B 352 ? 0.1004 0.1285 0.1398 -0.0147 0.0240  -0.0264 352 TYR B CA    
5852 C C     . TYR B 352 ? 0.0931 0.1206 0.1381 -0.0132 0.0234  -0.0253 352 TYR B C     
5853 O O     . TYR B 352 ? 0.3736 0.4022 0.4235 -0.0122 0.0220  -0.0257 352 TYR B O     
5854 C CB    . TYR B 352 ? 0.0405 0.0698 0.0811 -0.0155 0.0243  -0.0294 352 TYR B CB    
5855 C CG    . TYR B 352 ? 0.3598 0.3901 0.3954 -0.0168 0.0246  -0.0302 352 TYR B CG    
5856 C CD1   . TYR B 352 ? 0.3269 0.3594 0.3627 -0.0162 0.0227  -0.0302 352 TYR B CD1   
5857 C CD2   . TYR B 352 ? 0.4733 0.5020 0.5039 -0.0185 0.0269  -0.0306 352 TYR B CD2   
5858 C CE1   . TYR B 352 ? 0.0908 0.1240 0.1216 -0.0173 0.0232  -0.0306 352 TYR B CE1   
5859 C CE2   . TYR B 352 ? 0.3799 0.4088 0.4053 -0.0195 0.0277  -0.0306 352 TYR B CE2   
5860 C CZ    . TYR B 352 ? 0.0945 0.1256 0.1199 -0.0189 0.0259  -0.0307 352 TYR B CZ    
5861 O OH    . TYR B 352 ? 0.1363 0.1671 0.1556 -0.0193 0.0271  -0.0303 352 TYR B OH    
5862 N N     . GLY B 353 ? 0.2270 0.2529 0.2719 -0.0129 0.0243  -0.0239 353 GLY B N     
5863 C CA    . GLY B 353 ? 0.2113 0.2363 0.2611 -0.0116 0.0240  -0.0225 353 GLY B CA    
5864 C C     . GLY B 353 ? 0.1899 0.2140 0.2441 -0.0117 0.0248  -0.0244 353 GLY B C     
5865 O O     . GLY B 353 ? 0.1284 0.1526 0.1818 -0.0129 0.0258  -0.0268 353 GLY B O     
5866 N N     . LEU B 354 ? 0.0869 0.1098 0.1462 -0.0105 0.0244  -0.0231 354 LEU B N     
5867 C CA    . LEU B 354 ? 0.0399 0.0614 0.1041 -0.0104 0.0252  -0.0245 354 LEU B CA    
5868 C C     . LEU B 354 ? 0.0638 0.0865 0.1306 -0.0110 0.0249  -0.0278 354 LEU B C     
5869 O O     . LEU B 354 ? 0.0397 0.0636 0.1097 -0.0104 0.0231  -0.0285 354 LEU B O     
5870 C CB    . LEU B 354 ? 0.0419 0.0619 0.1118 -0.0089 0.0244  -0.0226 354 LEU B CB    
5871 C CG    . LEU B 354 ? 0.0388 0.0575 0.1067 -0.0083 0.0250  -0.0196 354 LEU B CG    
5872 C CD1   . LEU B 354 ? 0.0575 0.0745 0.1298 -0.0069 0.0241  -0.0172 354 LEU B CD1   
5873 C CD2   . LEU B 354 ? 0.0406 0.0580 0.1081 -0.0088 0.0268  -0.0200 354 LEU B CD2   
5874 N N     . GLY B 355 ? 0.0779 0.1002 0.1439 -0.0121 0.0264  -0.0299 355 GLY B N     
5875 C CA    . GLY B 355 ? 0.1056 0.1292 0.1730 -0.0129 0.0263  -0.0333 355 GLY B CA    
5876 C C     . GLY B 355 ? 0.2402 0.2653 0.3011 -0.0144 0.0270  -0.0345 355 GLY B C     
5877 O O     . GLY B 355 ? 0.4035 0.4299 0.4650 -0.0152 0.0270  -0.0374 355 GLY B O     
5878 N N     . GLY B 356 ? 0.1952 0.2199 0.2502 -0.0149 0.0275  -0.0324 356 GLY B N     
5879 C CA    . GLY B 356 ? 0.0787 0.1038 0.1275 -0.0165 0.0285  -0.0331 356 GLY B CA    
5880 C C     . GLY B 356 ? 0.1781 0.2010 0.2236 -0.0177 0.0309  -0.0328 356 GLY B C     
5881 O O     . GLY B 356 ? 0.2548 0.2771 0.2952 -0.0192 0.0323  -0.0331 356 GLY B O     
5882 N N     . GLU B 357 ? 0.1898 0.2111 0.2380 -0.0170 0.0315  -0.0318 357 GLU B N     
5883 C CA    . GLU B 357 ? 0.3142 0.3333 0.3600 -0.0179 0.0336  -0.0315 357 GLU B CA    
5884 C C     . GLU B 357 ? 0.2444 0.2630 0.2892 -0.0195 0.0355  -0.0339 357 GLU B C     
5885 O O     . GLU B 357 ? 0.3712 0.3905 0.4199 -0.0195 0.0353  -0.0360 357 GLU B O     
5886 C CB    . GLU B 357 ? 0.2161 0.2339 0.2658 -0.0166 0.0338  -0.0302 357 GLU B CB    
5887 C CG    . GLU B 357 ? 0.2912 0.3094 0.3474 -0.0155 0.0327  -0.0308 357 GLU B CG    
5888 C CD    . GLU B 357 ? 0.3660 0.3852 0.4244 -0.0139 0.0306  -0.0290 357 GLU B CD    
5889 O OE1   . GLU B 357 ? 0.4372 0.4555 0.5002 -0.0127 0.0302  -0.0277 357 GLU B OE1   
5890 O OE2   . GLU B 357 ? 0.4581 0.4788 0.5136 -0.0141 0.0296  -0.0288 357 GLU B OE2   
5891 N N     . GLU B 358 ? 0.2988 0.3159 0.3385 -0.0208 0.0374  -0.0336 358 GLU B N     
5892 C CA    . GLU B 358 ? 0.2637 0.2796 0.3013 -0.0224 0.0397  -0.0352 358 GLU B CA    
5893 C C     . GLU B 358 ? 0.2097 0.2276 0.2462 -0.0231 0.0394  -0.0369 358 GLU B C     
5894 O O     . GLU B 358 ? 0.2897 0.3074 0.3260 -0.0239 0.0409  -0.0386 358 GLU B O     
5895 C CB    . GLU B 358 ? 0.2202 0.2350 0.2618 -0.0223 0.0407  -0.0362 358 GLU B CB    
5896 C CG    . GLU B 358 ? 0.2349 0.2478 0.2767 -0.0217 0.0415  -0.0345 358 GLU B CG    
5897 C CD    . GLU B 358 ? 0.3109 0.3222 0.3556 -0.0219 0.0430  -0.0354 358 GLU B CD    
5898 O OE1   . GLU B 358 ? 0.4335 0.4434 0.4758 -0.0233 0.0452  -0.0364 358 GLU B OE1   
5899 O OE2   . GLU B 358 ? 0.3148 0.3262 0.3642 -0.0207 0.0421  -0.0350 358 GLU B OE2   
5900 N N     . HIS B 359 ? 0.1252 0.1449 0.1607 -0.0226 0.0376  -0.0364 359 HIS B N     
5901 C CA    . HIS B 359 ? 0.2721 0.2940 0.3061 -0.0229 0.0373  -0.0378 359 HIS B CA    
5902 C C     . HIS B 359 ? 0.2817 0.3022 0.3081 -0.0233 0.0386  -0.0360 359 HIS B C     
5903 O O     . HIS B 359 ? 0.2469 0.2656 0.2710 -0.0234 0.0389  -0.0339 359 HIS B O     
5904 C CB    . HIS B 359 ? 0.2997 0.3248 0.3391 -0.0216 0.0341  -0.0390 359 HIS B CB    
5905 C CG    . HIS B 359 ? 0.0542 0.0801 0.1011 -0.0207 0.0329  -0.0410 359 HIS B CG    
5906 N ND1   . HIS B 359 ? 0.0524 0.0769 0.1034 -0.0195 0.0323  -0.0398 359 HIS B ND1   
5907 C CD2   . HIS B 359 ? 0.0540 0.0819 0.1055 -0.0205 0.0322  -0.0442 359 HIS B CD2   
5908 C CE1   . HIS B 359 ? 0.0517 0.0767 0.1093 -0.0187 0.0315  -0.0418 359 HIS B CE1   
5909 N NE2   . HIS B 359 ? 0.0964 0.1235 0.1549 -0.0193 0.0312  -0.0448 359 HIS B NE2   
5910 N N     . ILE B 360 ? 0.3764 0.3977 0.3985 -0.0229 0.0395  -0.0368 360 ILE B N     
5911 C CA    . ILE B 360 ? 0.3363 0.3556 0.3500 -0.0223 0.0406  -0.0351 360 ILE B CA    
5912 C C     . ILE B 360 ? 0.3295 0.3510 0.3413 -0.0202 0.0390  -0.0366 360 ILE B C     
5913 O O     . ILE B 360 ? 0.1911 0.2146 0.2061 -0.0189 0.0378  -0.0396 360 ILE B O     
5914 C CB    . ILE B 360 ? 0.2232 0.2370 0.2269 -0.0219 0.0444  -0.0343 360 ILE B CB    
5915 C CG1   . ILE B 360 ? 0.3106 0.3232 0.3102 -0.0199 0.0455  -0.0369 360 ILE B CG1   
5916 C CG2   . ILE B 360 ? 0.0833 0.0950 0.0891 -0.0236 0.0459  -0.0330 360 ILE B CG2   
5917 C CD1   . ILE B 360 ? 0.3354 0.3411 0.3232 -0.0187 0.0489  -0.0366 360 ILE B CD1   
5918 N N     . ARG B 361 ? 0.3233 0.3436 0.3293 -0.0194 0.0386  -0.0351 361 ARG B N     
5919 C CA    . ARG B 361 ? 0.0779 0.0974 0.0782 -0.0162 0.0367  -0.0370 361 ARG B CA    
5920 C C     . ARG B 361 ? 0.0927 0.1033 0.0754 -0.0132 0.0379  -0.0366 361 ARG B C     
5921 O O     . ARG B 361 ? 0.0940 0.1033 0.0741 -0.0147 0.0400  -0.0334 361 ARG B O     
5922 C CB    . ARG B 361 ? 0.1853 0.2101 0.1936 -0.0173 0.0339  -0.0359 361 ARG B CB    
5923 C CG    . ARG B 361 ? 0.1558 0.1831 0.1652 -0.0175 0.0323  -0.0432 361 ARG B CG    
5924 C CD    . ARG B 361 ? 0.2661 0.2972 0.2792 -0.0181 0.0303  -0.0415 361 ARG B CD    
5925 N NE    . ARG B 361 ? 0.2216 0.2459 0.2212 -0.0163 0.0314  -0.0369 361 ARG B NE    
5926 C CZ    . ARG B 361 ? 0.2154 0.2418 0.2166 -0.0165 0.0300  -0.0342 361 ARG B CZ    
5927 N NH1   . ARG B 361 ? 0.2274 0.2611 0.2410 -0.0180 0.0270  -0.0354 361 ARG B NH1   
5928 N NH2   . ARG B 361 ? 0.3794 0.3998 0.3697 -0.0145 0.0308  -0.0303 361 ARG B NH2   
5929 N N     . ILE B 362 ? 0.1349 0.1377 0.1054 -0.0106 0.0364  -0.0422 362 ILE B N     
5930 C CA    . ILE B 362 ? 0.1896 0.1820 0.1414 -0.0065 0.0353  -0.0422 362 ILE B CA    
5931 C C     . ILE B 362 ? 0.3451 0.3308 0.2872 -0.0045 0.0299  -0.0468 362 ILE B C     
5932 O O     . ILE B 362 ? 0.2231 0.2097 0.1708 -0.0057 0.0259  -0.0516 362 ILE B O     
5933 C CB    . ILE B 362 ? 0.4705 0.4561 0.4127 -0.0040 0.0357  -0.0445 362 ILE B CB    
5934 C CG1   . ILE B 362 ? 0.4635 0.4439 0.4035 -0.0033 0.0316  -0.0518 362 ILE B CG1   
5935 C CG2   . ILE B 362 ? 0.6195 0.6110 0.5714 -0.0071 0.0409  -0.0405 362 ILE B CG2   
5936 C CD1   . ILE B 362 ? 0.4366 0.4104 0.3679 -0.0007 0.0315  -0.0543 362 ILE B CD1   
5937 N N     . ASN B 363 ? 0.4468 0.4271 0.3764 -0.0013 0.0287  -0.0453 363 ASN B N     
5938 C CA    . ASN B 363 ? 0.3407 0.3145 0.2602 0.0012  0.0224  -0.0490 363 ASN B CA    
5939 C C     . ASN B 363 ? 0.2779 0.2441 0.1852 0.0048  0.0176  -0.0549 363 ASN B C     
5940 O O     . ASN B 363 ? 0.3090 0.2749 0.2105 0.0056  0.0207  -0.0539 363 ASN B O     
5941 C CB    . ASN B 363 ? 0.5149 0.4911 0.4315 0.0017  0.0240  -0.0446 363 ASN B CB    
5942 C CG    . ASN B 363 ? 0.5281 0.5005 0.4380 0.0033  0.0176  -0.0480 363 ASN B CG    
5943 O OD1   . ASN B 363 ? 0.5686 0.5366 0.4729 0.0048  0.0112  -0.0545 363 ASN B OD1   
5944 N ND2   . ASN B 363 ? 0.2901 0.2662 0.2027 0.0024  0.0192  -0.0438 363 ASN B ND2   
5945 N N     . ILE B 364 ? 0.1801 0.1414 0.0858 0.0061  0.0097  -0.0614 364 ILE B N     
5946 C CA    . ILE B 364 ? 0.3187 0.2785 0.2202 0.0053  0.0061  -0.0678 364 ILE B CA    
5947 C C     . ILE B 364 ? 0.4048 0.3598 0.2979 0.0021  0.0033  -0.0697 364 ILE B C     
5948 O O     . ILE B 364 ? 0.3850 0.3294 0.2688 0.0016  -0.0012 -0.0722 364 ILE B O     
5949 C CB    . ILE B 364 ? 0.4317 0.3908 0.3414 0.0040  0.0022  -0.0727 364 ILE B CB    
5950 C CG1   . ILE B 364 ? 0.3027 0.2434 0.2061 -0.0033 0.0006  -0.0682 364 ILE B CG1   
5951 C CG2   . ILE B 364 ? 0.3638 0.3155 0.2698 0.0075  0.0056  -0.0685 364 ILE B CG2   
5952 C CD1   . ILE B 364 ? 0.2712 0.2129 0.1836 -0.0031 -0.0058 -0.0742 364 ILE B CD1   
5953 N N     . GLY B 365 ? 0.4562 0.4147 0.3498 0.0026  0.0042  -0.0657 365 GLY B N     
5954 C CA    . GLY B 365 ? 0.4763 0.4274 0.3595 0.0021  0.0010  -0.0645 365 GLY B CA    
5955 C C     . GLY B 365 ? 0.4925 0.4383 0.3632 0.0042  0.0045  -0.0613 365 GLY B C     
5956 O O     . GLY B 365 ? 0.5616 0.5088 0.4300 0.0045  0.0067  -0.0572 365 GLY B O     
5957 N N     . CYS B 366 ? 0.5284 0.4683 0.3917 0.0054  0.0053  -0.0630 366 CYS B N     
5958 C CA    . CYS B 366 ? 0.5408 0.4757 0.3933 0.0069  0.0093  -0.0599 366 CYS B CA    
5959 C C     . CYS B 366 ? 0.5316 0.4545 0.3711 0.0088  0.0054  -0.0632 366 CYS B C     
5960 O O     . CYS B 366 ? 0.5655 0.4857 0.4065 0.0088  0.0004  -0.0675 366 CYS B O     
5961 C CB    . CYS B 366 ? 0.6268 0.5688 0.4856 0.0067  0.0163  -0.0570 366 CYS B CB    
5962 S SG    . CYS B 366 ? 0.6466 0.5903 0.5106 0.0069  0.0166  -0.0610 366 CYS B SG    
5963 N N     . PRO B 367 ? 0.5741 0.4891 0.4007 0.0107  0.0070  -0.0610 367 PRO B N     
5964 C CA    . PRO B 367 ? 0.5990 0.5027 0.4130 0.0132  0.0040  -0.0638 367 PRO B CA    
5965 C C     . PRO B 367 ? 0.6835 0.5896 0.5018 0.0126  0.0064  -0.0665 367 PRO B C     
5966 O O     . PRO B 367 ? 0.6859 0.6008 0.5132 0.0110  0.0123  -0.0646 367 PRO B O     
5967 C CB    . PRO B 367 ? 0.5014 0.3978 0.3028 0.0150  0.0076  -0.0601 367 PRO B CB    
5968 C CG    . PRO B 367 ? 0.4371 0.3376 0.2421 0.0140  0.0095  -0.0560 367 PRO B CG    
5969 C CD    . PRO B 367 ? 0.3792 0.2938 0.2018 0.0109  0.0113  -0.0560 367 PRO B CD    
5970 N N     . ARG B 368 ? 0.7915 0.6898 0.6038 0.0141  0.0012  -0.0708 368 ARG B N     
5971 C CA    . ARG B 368 ? 0.6823 0.5818 0.4978 0.0137  0.0030  -0.0737 368 ARG B CA    
5972 C C     . ARG B 368 ? 0.7391 0.6390 0.5506 0.0141  0.0103  -0.0708 368 ARG B C     
5973 O O     . ARG B 368 ? 0.7677 0.6736 0.5868 0.0130  0.0141  -0.0713 368 ARG B O     
5974 C CB    . ARG B 368 ? 0.6554 0.5446 0.4625 0.0159  -0.0040 -0.0782 368 ARG B CB    
5975 C CG    . ARG B 368 ? 0.6949 0.5839 0.5039 0.0157  -0.0025 -0.0815 368 ARG B CG    
5976 C CD    . ARG B 368 ? 0.5946 0.4926 0.4202 0.0128  -0.0031 -0.0844 368 ARG B CD    
5977 N NE    . ARG B 368 ? 0.4455 0.3427 0.2763 0.0123  -0.0106 -0.0862 368 ARG B NE    
5978 C CZ    . ARG B 368 ? 0.4945 0.3855 0.3244 0.0136  -0.0183 -0.0900 368 ARG B CZ    
5979 N NH1   . ARG B 368 ? 0.5559 0.4407 0.3792 0.0152  -0.0191 -0.0929 368 ARG B NH1   
5980 N NH2   . ARG B 368 ? 0.4554 0.3469 0.2919 0.0136  -0.0255 -0.0908 368 ARG B NH2   
5981 N N     . SER B 369 ? 0.7655 0.6580 0.5647 0.0158  0.0120  -0.0675 369 SER B N     
5982 C CA    . SER B 369 ? 0.6680 0.5567 0.4610 0.0163  0.0192  -0.0633 369 SER B CA    
5983 C C     . SER B 369 ? 0.5809 0.4806 0.3872 0.0136  0.0251  -0.0597 369 SER B C     
5984 O O     . SER B 369 ? 0.6510 0.5527 0.4605 0.0128  0.0300  -0.0583 369 SER B O     
5985 C CB    . SER B 369 ? 0.6366 0.5139 0.4144 0.0185  0.0201  -0.0598 369 SER B CB    
5986 O OG    . SER B 369 ? 0.5201 0.4017 0.3025 0.0173  0.0214  -0.0562 369 SER B OG    
5987 N N     . VAL B 370 ? 0.4121 0.3185 0.2261 0.0122  0.0245  -0.0577 370 VAL B N     
5988 C CA    . VAL B 370 ? 0.4566 0.3732 0.2836 0.0099  0.0293  -0.0540 370 VAL B CA    
5989 C C     . VAL B 370 ? 0.5607 0.4871 0.4011 0.0089  0.0287  -0.0568 370 VAL B C     
5990 O O     . VAL B 370 ? 0.6082 0.5387 0.4551 0.0077  0.0338  -0.0539 370 VAL B O     
5991 C CB    . VAL B 370 ? 0.4976 0.4188 0.3294 0.0090  0.0278  -0.0519 370 VAL B CB    
5992 C CG1   . VAL B 370 ? 0.5267 0.4579 0.3720 0.0067  0.0323  -0.0478 370 VAL B CG1   
5993 C CG2   . VAL B 370 ? 0.4652 0.3760 0.2834 0.0103  0.0284  -0.0490 370 VAL B CG2   
5994 N N     . LEU B 371 ? 0.7222 0.6513 0.5669 0.0093  0.0224  -0.0626 371 LEU B N     
5995 C CA    . LEU B 371 ? 0.4588 0.3955 0.3160 0.0088  0.0214  -0.0656 371 LEU B CA    
5996 C C     . LEU B 371 ? 0.4686 0.4044 0.3250 0.0094  0.0247  -0.0661 371 LEU B C     
5997 O O     . LEU B 371 ? 0.5718 0.5142 0.4384 0.0091  0.0270  -0.0650 371 LEU B O     
5998 C CB    . LEU B 371 ? 0.3625 0.2956 0.2202 0.0083  0.0144  -0.0717 371 LEU B CB    
5999 C CG    . LEU B 371 ? 0.3917 0.3328 0.2646 0.0073  0.0126  -0.0747 371 LEU B CG    
6000 C CD1   . LEU B 371 ? 0.5656 0.5138 0.4471 0.0068  0.0123  -0.0718 371 LEU B CD1   
6001 C CD2   . LEU B 371 ? 0.3344 0.2696 0.2075 0.0057  0.0067  -0.0809 371 LEU B CD2   
6002 N N     . GLU B 372 ? 0.5306 0.4558 0.3729 0.0104  0.0252  -0.0669 372 GLU B N     
6003 C CA    . GLU B 372 ? 0.5918 0.5141 0.4315 0.0109  0.0284  -0.0674 372 GLU B CA    
6004 C C     . GLU B 372 ? 0.6202 0.5447 0.4628 0.0095  0.0362  -0.0610 372 GLU B C     
6005 O O     . GLU B 372 ? 0.8236 0.7521 0.6733 0.0089  0.0390  -0.0605 372 GLU B O     
6006 C CB    . GLU B 372 ? 0.6468 0.5560 0.4695 0.0128  0.0272  -0.0691 372 GLU B CB    
6007 C CG    . GLU B 372 ? 0.7334 0.6377 0.5520 0.0138  0.0196  -0.0751 372 GLU B CG    
6008 C CD    . GLU B 372 ? 0.8972 0.7878 0.6974 0.0164  0.0178  -0.0747 372 GLU B CD    
6009 O OE1   . GLU B 372 ? 0.9360 0.8205 0.7266 0.0174  0.0229  -0.0702 372 GLU B OE1   
6010 O OE2   . GLU B 372 ? 0.9443 0.8273 0.7376 0.0179  0.0112  -0.0784 372 GLU B OE2   
6011 N N     . GLU B 373 ? 0.5221 0.4436 0.3604 0.0087  0.0396  -0.0559 373 GLU B N     
6012 C CA    . GLU B 373 ? 0.5775 0.5007 0.4204 0.0063  0.0467  -0.0500 373 GLU B CA    
6013 C C     . GLU B 373 ? 0.5313 0.4659 0.3906 0.0040  0.0477  -0.0479 373 GLU B C     
6014 O O     . GLU B 373 ? 0.4213 0.3586 0.2878 0.0015  0.0527  -0.0444 373 GLU B O     
6015 C CB    . GLU B 373 ? 0.6666 0.5830 0.5013 0.0059  0.0495  -0.0458 373 GLU B CB    
6016 C CG    . GLU B 373 ? 0.6694 0.5859 0.5088 0.0032  0.0564  -0.0405 373 GLU B CG    
6017 C CD    . GLU B 373 ? 0.7445 0.6535 0.5770 0.0034  0.0606  -0.0400 373 GLU B CD    
6018 O OE1   . GLU B 373 ? 0.7063 0.6094 0.5291 0.0059  0.0583  -0.0435 373 GLU B OE1   
6019 O OE2   . GLU B 373 ? 0.7206 0.6292 0.5575 0.0010  0.0659  -0.0363 373 GLU B OE2   
6020 N N     . ILE B 374 ? 0.5855 0.5262 0.4509 0.0047  0.0429  -0.0498 374 ILE B N     
6021 C CA    . ILE B 374 ? 0.4305 0.3810 0.3110 0.0030  0.0434  -0.0478 374 ILE B CA    
6022 C C     . ILE B 374 ? 0.3741 0.3278 0.2617 0.0029  0.0439  -0.0496 374 ILE B C     
6023 O O     . ILE B 374 ? 0.4080 0.3674 0.3070 -0.0001 0.0477  -0.0460 374 ILE B O     
6024 C CB    . ILE B 374 ? 0.3916 0.3465 0.2760 0.0044  0.0375  -0.0502 374 ILE B CB    
6025 C CG1   . ILE B 374 ? 0.4237 0.3760 0.3022 0.0039  0.0378  -0.0476 374 ILE B CG1   
6026 C CG2   . ILE B 374 ? 0.3019 0.2653 0.2012 0.0029  0.0380  -0.0482 374 ILE B CG2   
6027 C CD1   . ILE B 374 ? 0.3088 0.2642 0.1894 0.0052  0.0318  -0.0502 374 ILE B CD1   
6028 N N     . LEU B 375 ? 0.4168 0.3668 0.2985 0.0057  0.0398  -0.0553 375 LEU B N     
6029 C CA    . LEU B 375 ? 0.4370 0.3890 0.3245 0.0061  0.0399  -0.0574 375 LEU B CA    
6030 C C     . LEU B 375 ? 0.4867 0.4344 0.3694 0.0047  0.0458  -0.0552 375 LEU B C     
6031 O O     . LEU B 375 ? 0.4483 0.3994 0.3391 0.0028  0.0492  -0.0534 375 LEU B O     
6032 C CB    . LEU B 375 ? 0.3972 0.3467 0.2822 0.0095  0.0321  -0.0655 375 LEU B CB    
6033 C CG    . LEU B 375 ? 0.3269 0.2764 0.2152 0.0098  0.0262  -0.0688 375 LEU B CG    
6034 C CD1   . LEU B 375 ? 0.3650 0.3091 0.2491 0.0108  0.0193  -0.0774 375 LEU B CD1   
6035 C CD2   . LEU B 375 ? 0.2175 0.1713 0.1183 0.0082  0.0274  -0.0660 375 LEU B CD2   
6036 N N     . ASN B 376 ? 0.6662 0.6057 0.5358 0.0053  0.0471  -0.0551 376 ASN B N     
6037 C CA    . ASN B 376 ? 0.6880 0.6220 0.5523 0.0042  0.0527  -0.0527 376 ASN B CA    
6038 C C     . ASN B 376 ? 0.5667 0.5050 0.4411 0.0002  0.0588  -0.0466 376 ASN B C     
6039 O O     . ASN B 376 ? 0.6444 0.5826 0.5222 -0.0015 0.0627  -0.0453 376 ASN B O     
6040 C CB    . ASN B 376 ? 0.7336 0.6569 0.5821 0.0056  0.0533  -0.0525 376 ASN B CB    
6041 C CG    . ASN B 376 ? 0.7210 0.6366 0.5612 0.0061  0.0568  -0.0526 376 ASN B CG    
6042 O OD1   . ASN B 376 ? 0.6867 0.5994 0.5264 0.0041  0.0626  -0.0482 376 ASN B OD1   
6043 N ND2   . ASN B 376 ? 0.7343 0.6464 0.5684 0.0086  0.0530  -0.0580 376 ASN B ND2   
6044 N N     . ARG B 377 ? 0.4387 0.3805 0.3184 -0.0016 0.0594  -0.0433 377 ARG B N     
6045 C CA    . ARG B 377 ? 0.3360 0.2818 0.2266 -0.0057 0.0639  -0.0385 377 ARG B CA    
6046 C C     . ARG B 377 ? 0.3939 0.3491 0.2999 -0.0079 0.0634  -0.0382 377 ARG B C     
6047 O O     . ARG B 377 ? 0.6266 0.5846 0.5421 -0.0114 0.0667  -0.0355 377 ARG B O     
6048 C CB    . ARG B 377 ? 0.2866 0.2320 0.1770 -0.0068 0.0643  -0.0355 377 ARG B CB    
6049 C CG    . ARG B 377 ? 0.3269 0.2619 0.2027 -0.0052 0.0660  -0.0349 377 ARG B CG    
6050 C CD    . ARG B 377 ? 0.4203 0.3546 0.2949 -0.0055 0.0655  -0.0328 377 ARG B CD    
6051 N NE    . ARG B 377 ? 0.4783 0.4018 0.3393 -0.0041 0.0675  -0.0319 377 ARG B NE    
6052 C CZ    . ARG B 377 ? 0.3410 0.2612 0.2014 -0.0054 0.0702  -0.0288 377 ARG B CZ    
6053 N NH1   . ARG B 377 ? 0.3374 0.2643 0.2099 -0.0081 0.0709  -0.0267 377 ARG B NH1   
6054 N NH2   . ARG B 377 ? 0.2603 0.1699 0.1078 -0.0037 0.0722  -0.0282 377 ARG B NH2   
6055 N N     . LEU B 378 ? 0.2543 0.2141 0.1636 -0.0060 0.0590  -0.0413 378 LEU B N     
6056 C CA    . LEU B 378 ? 0.3345 0.3023 0.2583 -0.0082 0.0588  -0.0411 378 LEU B CA    
6057 C C     . LEU B 378 ? 0.4429 0.4096 0.3679 -0.0086 0.0609  -0.0424 378 LEU B C     
6058 O O     . LEU B 378 ? 0.4138 0.3853 0.3506 -0.0121 0.0633  -0.0404 378 LEU B O     
6059 C CB    . LEU B 378 ? 0.3159 0.2871 0.2420 -0.0055 0.0534  -0.0445 378 LEU B CB    
6060 C CG    . LEU B 378 ? 0.4211 0.3975 0.3540 -0.0065 0.0513  -0.0429 378 LEU B CG    
6061 C CD1   . LEU B 378 ? 0.4596 0.4360 0.3920 -0.0030 0.0453  -0.0475 378 LEU B CD1   
6062 C CD2   . LEU B 378 ? 0.3883 0.3728 0.3378 -0.0117 0.0540  -0.0389 378 LEU B CD2   
6063 N N     . ARG B 379 ? 0.3794 0.3394 0.2921 -0.0050 0.0597  -0.0460 379 ARG B N     
6064 C CA    . ARG B 379 ? 0.4113 0.3692 0.3234 -0.0051 0.0618  -0.0473 379 ARG B CA    
6065 C C     . ARG B 379 ? 0.4801 0.4359 0.3936 -0.0085 0.0676  -0.0432 379 ARG B C     
6066 O O     . ARG B 379 ? 0.5366 0.4957 0.4597 -0.0114 0.0701  -0.0418 379 ARG B O     
6067 C CB    . ARG B 379 ? 0.3691 0.3192 0.2665 -0.0003 0.0583  -0.0526 379 ARG B CB    
6068 C CG    . ARG B 379 ? 0.2665 0.2151 0.1638 0.0008  0.0583  -0.0558 379 ARG B CG    
6069 C CD    . ARG B 379 ? 0.3847 0.3254 0.2681 0.0053  0.0538  -0.0617 379 ARG B CD    
6070 N NE    . ARG B 379 ? 0.5664 0.4993 0.4368 0.0053  0.0565  -0.0600 379 ARG B NE    
6071 C CZ    . ARG B 379 ? 0.5913 0.5160 0.4486 0.0080  0.0543  -0.0640 379 ARG B CZ    
6072 N NH1   . ARG B 379 ? 0.5186 0.4425 0.3750 0.0107  0.0488  -0.0707 379 ARG B NH1   
6073 N NH2   . ARG B 379 ? 0.5156 0.4321 0.3610 0.0079  0.0573  -0.0615 379 ARG B NH2   
6074 N N     . HIS B 380 ? 0.3905 0.3398 0.2943 -0.0082 0.0694  -0.0414 380 HIS B N     
6075 C CA    . HIS B 380 ? 0.4679 0.4138 0.3728 -0.0110 0.0744  -0.0379 380 HIS B CA    
6076 C C     . HIS B 380 ? 0.5973 0.5502 0.5178 -0.0151 0.0754  -0.0353 380 HIS B C     
6077 O O     . HIS B 380 ? 0.7169 0.6695 0.6428 -0.0174 0.0781  -0.0342 380 HIS B O     
6078 C CB    . HIS B 380 ? 0.6232 0.5616 0.5171 -0.0101 0.0756  -0.0363 380 HIS B CB    
6079 C CG    . HIS B 380 ? 0.6523 0.5858 0.5464 -0.0124 0.0805  -0.0334 380 HIS B CG    
6080 N ND1   . HIS B 380 ? 0.6847 0.6121 0.5732 -0.0121 0.0837  -0.0336 380 HIS B ND1   
6081 C CD2   . HIS B 380 ? 0.6609 0.5944 0.5599 -0.0146 0.0822  -0.0306 380 HIS B CD2   
6082 C CE1   . HIS B 380 ? 0.6945 0.6182 0.5846 -0.0141 0.0874  -0.0310 380 HIS B CE1   
6083 N NE2   . HIS B 380 ? 0.6783 0.6057 0.5748 -0.0156 0.0865  -0.0294 380 HIS B NE2   
6084 N N     . THR B 381 ? 0.6750 0.6338 0.6026 -0.0159 0.0727  -0.0345 381 THR B N     
6085 C CA    . THR B 381 ? 0.5367 0.5013 0.4782 -0.0194 0.0727  -0.0326 381 THR B CA    
6086 C C     . THR B 381 ? 0.4049 0.3739 0.3564 -0.0211 0.0726  -0.0335 381 THR B C     
6087 O O     . THR B 381 ? 0.4166 0.3861 0.3751 -0.0234 0.0740  -0.0325 381 THR B O     
6088 C CB    . THR B 381 ? 0.4085 0.3785 0.3552 -0.0195 0.0693  -0.0321 381 THR B CB    
6089 O OG1   . THR B 381 ? 0.3226 0.2880 0.2590 -0.0177 0.0693  -0.0314 381 THR B OG1   
6090 C CG2   . THR B 381 ? 0.3576 0.3320 0.3163 -0.0225 0.0687  -0.0305 381 THR B CG2   
6091 N N     . PHE B 382 ? 0.4640 0.4359 0.4161 -0.0196 0.0708  -0.0360 382 PHE B N     
6092 C CA    . PHE B 382 ? 0.5057 0.4826 0.4686 -0.0212 0.0703  -0.0370 382 PHE B CA    
6093 C C     . PHE B 382 ? 0.5421 0.5154 0.5000 -0.0201 0.0725  -0.0388 382 PHE B C     
6094 O O     . PHE B 382 ? 0.6795 0.6566 0.6452 -0.0210 0.0720  -0.0402 382 PHE B O     
6095 C CB    . PHE B 382 ? 0.6608 0.6443 0.6307 -0.0207 0.0666  -0.0387 382 PHE B CB    
6096 C CG    . PHE B 382 ? 0.5403 0.5275 0.5149 -0.0215 0.0642  -0.0372 382 PHE B CG    
6097 C CD1   . PHE B 382 ? 0.5237 0.5117 0.5046 -0.0240 0.0644  -0.0350 382 PHE B CD1   
6098 C CD2   . PHE B 382 ? 0.3056 0.2946 0.2773 -0.0192 0.0615  -0.0384 382 PHE B CD2   
6099 C CE1   . PHE B 382 ? 0.4915 0.4825 0.4760 -0.0244 0.0620  -0.0339 382 PHE B CE1   
6100 C CE2   . PHE B 382 ? 0.3566 0.3488 0.3326 -0.0201 0.0594  -0.0370 382 PHE B CE2   
6101 C CZ    . PHE B 382 ? 0.4006 0.3940 0.3832 -0.0228 0.0597  -0.0346 382 PHE B CZ    
6102 N N     . SER B 383 ? 0.5369 0.5027 0.4818 -0.0182 0.0747  -0.0389 383 SER B N     
6103 C CA    . SER B 383 ? 0.6017 0.5633 0.5408 -0.0168 0.0766  -0.0408 383 SER B CA    
6104 C C     . SER B 383 ? 0.6776 0.6380 0.6223 -0.0199 0.0802  -0.0389 383 SER B C     
6105 O O     . SER B 383 ? 0.7467 0.7056 0.6938 -0.0219 0.0817  -0.0365 383 SER B O     
6106 C CB    . SER B 383 ? 0.6271 0.5800 0.5490 -0.0132 0.0770  -0.0422 383 SER B CB    
6107 O OG    . SER B 383 ? 0.6019 0.5545 0.5170 -0.0094 0.0726  -0.0454 383 SER B OG    
6108 O OXT   . SER B 383 ? 0.6706 0.6309 0.6172 -0.0201 0.0814  -0.0402 383 SER B OXT   
6109 N N     . OO0 C .   ? 0.5730 0.6102 0.5686 -0.0116 -0.0001 0.0071  401 OO0 A N     
6110 C CA    . OO0 C .   ? 0.5151 0.5540 0.5123 -0.0116 -0.0016 0.0084  401 OO0 A CA    
6111 C CB    . OO0 C .   ? 0.4436 0.4779 0.4446 -0.0089 -0.0028 0.0078  401 OO0 A CB    
6112 S SG    . OO0 C .   ? 0.6071 0.6355 0.6048 -0.0071 -0.0022 0.0092  401 OO0 A SG    
6113 O O1    . OO0 C .   ? 0.6880 0.7255 0.6888 -0.0109 -0.0031 0.0108  401 OO0 A O1    
6114 C C3    . OO0 C .   ? 0.2541 0.2844 0.2587 -0.0074 -0.0022 0.0097  401 OO0 A C3    
6115 C C4    . OO0 C .   ? 0.2716 0.3090 0.2736 -0.0110 -0.0039 0.0143  401 OO0 A C4    
6116 C C5    . OO0 C .   ? 0.3252 0.3539 0.3290 -0.0094 -0.0023 0.0124  401 OO0 A C5    
6117 C C     . OO0 C .   ? 0.3905 0.4305 0.3895 -0.0109 -0.0023 0.0088  401 OO0 A C     
6118 O OXT   . OO0 C .   ? 0.4952 0.5346 0.4950 -0.0106 -0.0026 0.0096  401 OO0 A OXT   
6119 O O     . OO0 C .   ? 0.3760 0.4152 0.3746 -0.0104 -0.0016 0.0082  401 OO0 A O     
# 
