data_9BCA
# 
_entry.id   9BCA 
# 
_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   9BCA         pdb_00009bca 10.2210/pdb9bca/pdb 
WWPDB D_1000283047 ?            ?                   
# 
_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       2024-11-06 
# 
_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                        9BCA 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9BC9 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              schulman@biochem.mpg.de 
_pdbx_contact_author.name_first         Brenda 
_pdbx_contact_author.name_last          Schulman 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3083-1126 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Scott, D.C.'       1  ? 
'Dharuman, S.'      2  ? 
'Griffith, E.'      3  ? 
'Chai, S.C.'        4  ? 
'Ronnebaum, J.'     5  ? 
'King, M.T.'        6  ? 
'Tangallapally, R.' 7  ? 
'Lee, C.'           8  ? 
'Gee, C.T.'         9  ? 
'Lee, H.W.'         10 ? 
'Ochoada, J.'       11 ? 
'Miller, D.J.'      12 ? 
'Jayasinghe, T.'    13 ? 
'Paulo, J.A.'       14 ? 
'Elledge, S.J.'     15 ? 
'Harper, J.W.'      16 ? 
'Chen, T.'          17 ? 
'Lee, R.E.'         18 ? 
'Schulman, B.A.'    19 ? 
# 
_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                     'Principles of isoform-specific targeted protein degradation engaging the C-degron E3 KLHDC2' 
_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 'Scott, D.C.'       1  ? 
primary 'Dharuman, S.'      2  ? 
primary 'Griffith, E.'      3  ? 
primary 'Chai, S.C.'        4  ? 
primary 'Ronnebaum, J.'     5  ? 
primary 'King, M.T.'        6  ? 
primary 'Tangallapally, R.' 7  ? 
primary 'Lee, C.'           8  ? 
primary 'Gee, C.T.'         9  ? 
primary 'Lee, H.W.'         10 ? 
primary 'Ochoada, J.'       11 ? 
primary 'Miller, D.J.'      12 ? 
primary 'Jayasinghe, T.'    13 ? 
primary 'Paulo, J.A.'       14 ? 
primary 'Elledge, S.J.'     15 ? 
primary 'Harper, J.W.'      16 ? 
primary 'Chen, T.'          17 ? 
primary 'Lee, R.E.'         18 ? 
primary 'Schulman, B.A.'    19 ? 
# 
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 'Kelch domain-containing protein 2'                       39764.422 2   ? ? ? ? 
2 non-polymer syn 'N-{[2-(naphthalen-2-yl)-1,3-thiazol-4-yl]acetyl}glycine' 326.370   2   ? ? ? ? 
3 non-polymer syn 'COBALT HEXAMMINE(III)'                                   161.116   1   ? ? ? ? 
4 water       nat water                                                     18.015    475 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Hepatocellular carcinoma-associated antigen 33,Host cell factor homolog LCP,Host cell factor-like protein 1,HCLP-1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GSGPAFESYESMELACPAERSGHVAVSDGRHMFVWGGYKSNQVRGLYDFYLPREELWIYNMETGRWKKINTEGDVPPSMS
GSCAVCVDRVLYLFGGHHSRGNTNKFYMLDSRSTDRVLQWERIDCQGIPPSSKDKLGVWVYKNKLIFFGGYGYLPEDKVL
GTFEFDETSFWNSSHPRGWNDHVHILDTETFTWSQPITTGKAPSPRAAHACATVGNRGFVFGGRYRDARMNDLHYLNLDT
WEWNELIPQGICPVGRSWHSLTPVSSDHLFLFGGFTTDKQPLSDAWTYCISKNEWIQFNHPYTEKPRLWHTACASDEGEV
IVFGGCANNLLVHHRAAHSNEILIFSVQP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSGPAFESYESMELACPAERSGHVAVSDGRHMFVWGGYKSNQVRGLYDFYLPREELWIYNMETGRWKKINTEGDVPPSMS
GSCAVCVDRVLYLFGGHHSRGNTNKFYMLDSRSTDRVLQWERIDCQGIPPSSKDKLGVWVYKNKLIFFGGYGYLPEDKVL
GTFEFDETSFWNSSHPRGWNDHVHILDTETFTWSQPITTGKAPSPRAAHACATVGNRGFVFGGRYRDARMNDLHYLNLDT
WEWNELIPQGICPVGRSWHSLTPVSSDHLFLFGGFTTDKQPLSDAWTYCISKNEWIQFNHPYTEKPRLWHTACASDEGEV
IVFGGCANNLLVHHRAAHSNEILIFSVQP
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'N-{[2-(naphthalen-2-yl)-1,3-thiazol-4-yl]acetyl}glycine' A1APS 
3 'COBALT HEXAMMINE(III)'                                   NCO   
4 water                                                     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   GLY n 
1 4   PRO n 
1 5   ALA n 
1 6   PHE n 
1 7   GLU n 
1 8   SER n 
1 9   TYR n 
1 10  GLU n 
1 11  SER n 
1 12  MET n 
1 13  GLU n 
1 14  LEU n 
1 15  ALA n 
1 16  CYS n 
1 17  PRO n 
1 18  ALA n 
1 19  GLU n 
1 20  ARG n 
1 21  SER n 
1 22  GLY n 
1 23  HIS n 
1 24  VAL n 
1 25  ALA n 
1 26  VAL n 
1 27  SER n 
1 28  ASP n 
1 29  GLY n 
1 30  ARG n 
1 31  HIS n 
1 32  MET n 
1 33  PHE n 
1 34  VAL n 
1 35  TRP n 
1 36  GLY n 
1 37  GLY n 
1 38  TYR n 
1 39  LYS n 
1 40  SER n 
1 41  ASN n 
1 42  GLN n 
1 43  VAL n 
1 44  ARG n 
1 45  GLY n 
1 46  LEU n 
1 47  TYR n 
1 48  ASP n 
1 49  PHE n 
1 50  TYR n 
1 51  LEU n 
1 52  PRO n 
1 53  ARG n 
1 54  GLU n 
1 55  GLU n 
1 56  LEU n 
1 57  TRP n 
1 58  ILE n 
1 59  TYR n 
1 60  ASN n 
1 61  MET n 
1 62  GLU n 
1 63  THR n 
1 64  GLY n 
1 65  ARG n 
1 66  TRP n 
1 67  LYS n 
1 68  LYS n 
1 69  ILE n 
1 70  ASN n 
1 71  THR n 
1 72  GLU n 
1 73  GLY n 
1 74  ASP n 
1 75  VAL n 
1 76  PRO n 
1 77  PRO n 
1 78  SER n 
1 79  MET n 
1 80  SER n 
1 81  GLY n 
1 82  SER n 
1 83  CYS n 
1 84  ALA n 
1 85  VAL n 
1 86  CYS n 
1 87  VAL n 
1 88  ASP n 
1 89  ARG n 
1 90  VAL n 
1 91  LEU n 
1 92  TYR n 
1 93  LEU n 
1 94  PHE n 
1 95  GLY n 
1 96  GLY n 
1 97  HIS n 
1 98  HIS n 
1 99  SER n 
1 100 ARG n 
1 101 GLY n 
1 102 ASN n 
1 103 THR n 
1 104 ASN n 
1 105 LYS n 
1 106 PHE n 
1 107 TYR n 
1 108 MET n 
1 109 LEU n 
1 110 ASP n 
1 111 SER n 
1 112 ARG n 
1 113 SER n 
1 114 THR n 
1 115 ASP n 
1 116 ARG n 
1 117 VAL n 
1 118 LEU n 
1 119 GLN n 
1 120 TRP n 
1 121 GLU n 
1 122 ARG n 
1 123 ILE n 
1 124 ASP n 
1 125 CYS n 
1 126 GLN n 
1 127 GLY n 
1 128 ILE n 
1 129 PRO n 
1 130 PRO n 
1 131 SER n 
1 132 SER n 
1 133 LYS n 
1 134 ASP n 
1 135 LYS n 
1 136 LEU n 
1 137 GLY n 
1 138 VAL n 
1 139 TRP n 
1 140 VAL n 
1 141 TYR n 
1 142 LYS n 
1 143 ASN n 
1 144 LYS n 
1 145 LEU n 
1 146 ILE n 
1 147 PHE n 
1 148 PHE n 
1 149 GLY n 
1 150 GLY n 
1 151 TYR n 
1 152 GLY n 
1 153 TYR n 
1 154 LEU n 
1 155 PRO n 
1 156 GLU n 
1 157 ASP n 
1 158 LYS n 
1 159 VAL n 
1 160 LEU n 
1 161 GLY n 
1 162 THR n 
1 163 PHE n 
1 164 GLU n 
1 165 PHE n 
1 166 ASP n 
1 167 GLU n 
1 168 THR n 
1 169 SER n 
1 170 PHE n 
1 171 TRP n 
1 172 ASN n 
1 173 SER n 
1 174 SER n 
1 175 HIS n 
1 176 PRO n 
1 177 ARG n 
1 178 GLY n 
1 179 TRP n 
1 180 ASN n 
1 181 ASP n 
1 182 HIS n 
1 183 VAL n 
1 184 HIS n 
1 185 ILE n 
1 186 LEU n 
1 187 ASP n 
1 188 THR n 
1 189 GLU n 
1 190 THR n 
1 191 PHE n 
1 192 THR n 
1 193 TRP n 
1 194 SER n 
1 195 GLN n 
1 196 PRO n 
1 197 ILE n 
1 198 THR n 
1 199 THR n 
1 200 GLY n 
1 201 LYS n 
1 202 ALA n 
1 203 PRO n 
1 204 SER n 
1 205 PRO n 
1 206 ARG n 
1 207 ALA n 
1 208 ALA n 
1 209 HIS n 
1 210 ALA n 
1 211 CYS n 
1 212 ALA n 
1 213 THR n 
1 214 VAL n 
1 215 GLY n 
1 216 ASN n 
1 217 ARG n 
1 218 GLY n 
1 219 PHE n 
1 220 VAL n 
1 221 PHE n 
1 222 GLY n 
1 223 GLY n 
1 224 ARG n 
1 225 TYR n 
1 226 ARG n 
1 227 ASP n 
1 228 ALA n 
1 229 ARG n 
1 230 MET n 
1 231 ASN n 
1 232 ASP n 
1 233 LEU n 
1 234 HIS n 
1 235 TYR n 
1 236 LEU n 
1 237 ASN n 
1 238 LEU n 
1 239 ASP n 
1 240 THR n 
1 241 TRP n 
1 242 GLU n 
1 243 TRP n 
1 244 ASN n 
1 245 GLU n 
1 246 LEU n 
1 247 ILE n 
1 248 PRO n 
1 249 GLN n 
1 250 GLY n 
1 251 ILE n 
1 252 CYS n 
1 253 PRO n 
1 254 VAL n 
1 255 GLY n 
1 256 ARG n 
1 257 SER n 
1 258 TRP n 
1 259 HIS n 
1 260 SER n 
1 261 LEU n 
1 262 THR n 
1 263 PRO n 
1 264 VAL n 
1 265 SER n 
1 266 SER n 
1 267 ASP n 
1 268 HIS n 
1 269 LEU n 
1 270 PHE n 
1 271 LEU n 
1 272 PHE n 
1 273 GLY n 
1 274 GLY n 
1 275 PHE n 
1 276 THR n 
1 277 THR n 
1 278 ASP n 
1 279 LYS n 
1 280 GLN n 
1 281 PRO n 
1 282 LEU n 
1 283 SER n 
1 284 ASP n 
1 285 ALA n 
1 286 TRP n 
1 287 THR n 
1 288 TYR n 
1 289 CYS n 
1 290 ILE n 
1 291 SER n 
1 292 LYS n 
1 293 ASN n 
1 294 GLU n 
1 295 TRP n 
1 296 ILE n 
1 297 GLN n 
1 298 PHE n 
1 299 ASN n 
1 300 HIS n 
1 301 PRO n 
1 302 TYR n 
1 303 THR n 
1 304 GLU n 
1 305 LYS n 
1 306 PRO n 
1 307 ARG n 
1 308 LEU n 
1 309 TRP n 
1 310 HIS n 
1 311 THR n 
1 312 ALA n 
1 313 CYS n 
1 314 ALA n 
1 315 SER n 
1 316 ASP n 
1 317 GLU n 
1 318 GLY n 
1 319 GLU n 
1 320 VAL n 
1 321 ILE n 
1 322 VAL n 
1 323 PHE n 
1 324 GLY n 
1 325 GLY n 
1 326 CYS n 
1 327 ALA n 
1 328 ASN n 
1 329 ASN n 
1 330 LEU n 
1 331 LEU n 
1 332 VAL n 
1 333 HIS n 
1 334 HIS n 
1 335 ARG n 
1 336 ALA n 
1 337 ALA n 
1 338 HIS n 
1 339 SER n 
1 340 ASN n 
1 341 GLU n 
1 342 ILE n 
1 343 LEU n 
1 344 ILE n 
1 345 PHE n 
1 346 SER n 
1 347 VAL n 
1 348 GLN n 
1 349 PRO 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                   349 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'KLHDC2, HCA33' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1APS non-polymer         . 'N-{[2-(naphthalen-2-yl)-1,3-thiazol-4-yl]acetyl}glycine' SJ46411 'C17 H14 N2 O3 S' 326.370 
ALA   'L-peptide linking' y ALANINE                                                   ?       'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                                  ?       'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                ?       'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                           ?       'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                                  ?       'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                 ?       'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                           ?       'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                   ?       'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                                 ?       'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                     ?       'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                ?       'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                   ?       'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                    ?       'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                ?       'C5 H11 N O2 S'   149.211 
NCO   non-polymer         . 'COBALT HEXAMMINE(III)'                                   ?       'Co H18 N6 3'     161.116 
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   GLY 1   13  ?   ?   ?   A . n 
A 1 2   SER 2   14  ?   ?   ?   A . n 
A 1 3   GLY 3   15  ?   ?   ?   A . n 
A 1 4   PRO 4   16  ?   ?   ?   A . n 
A 1 5   ALA 5   17  ?   ?   ?   A . n 
A 1 6   PHE 6   18  ?   ?   ?   A . n 
A 1 7   GLU 7   19  ?   ?   ?   A . n 
A 1 8   SER 8   20  ?   ?   ?   A . n 
A 1 9   TYR 9   21  ?   ?   ?   A . n 
A 1 10  GLU 10  22  ?   ?   ?   A . n 
A 1 11  SER 11  23  ?   ?   ?   A . n 
A 1 12  MET 12  24  ?   ?   ?   A . n 
A 1 13  GLU 13  25  ?   ?   ?   A . n 
A 1 14  LEU 14  26  26  LEU LEU A . n 
A 1 15  ALA 15  27  27  ALA ALA A . n 
A 1 16  CYS 16  28  28  CYS CYS A . n 
A 1 17  PRO 17  29  29  PRO PRO A . n 
A 1 18  ALA 18  30  30  ALA ALA A . n 
A 1 19  GLU 19  31  31  GLU GLU A . n 
A 1 20  ARG 20  32  32  ARG ARG A . n 
A 1 21  SER 21  33  33  SER SER A . n 
A 1 22  GLY 22  34  34  GLY GLY A . n 
A 1 23  HIS 23  35  35  HIS HIS A . n 
A 1 24  VAL 24  36  36  VAL VAL A . n 
A 1 25  ALA 25  37  37  ALA ALA A . n 
A 1 26  VAL 26  38  38  VAL VAL A . n 
A 1 27  SER 27  39  39  SER SER A . n 
A 1 28  ASP 28  40  40  ASP ASP A . n 
A 1 29  GLY 29  41  41  GLY GLY A . n 
A 1 30  ARG 30  42  42  ARG ARG A . n 
A 1 31  HIS 31  43  43  HIS HIS A . n 
A 1 32  MET 32  44  44  MET MET A . n 
A 1 33  PHE 33  45  45  PHE PHE A . n 
A 1 34  VAL 34  46  46  VAL VAL A . n 
A 1 35  TRP 35  47  47  TRP TRP A . n 
A 1 36  GLY 36  48  48  GLY GLY A . n 
A 1 37  GLY 37  49  49  GLY GLY A . n 
A 1 38  TYR 38  50  50  TYR TYR A . n 
A 1 39  LYS 39  51  51  LYS LYS A . n 
A 1 40  SER 40  52  52  SER SER A . n 
A 1 41  ASN 41  53  53  ASN ASN A . n 
A 1 42  GLN 42  54  ?   ?   ?   A . n 
A 1 43  VAL 43  55  ?   ?   ?   A . n 
A 1 44  ARG 44  56  ?   ?   ?   A . n 
A 1 45  GLY 45  57  ?   ?   ?   A . n 
A 1 46  LEU 46  58  ?   ?   ?   A . n 
A 1 47  TYR 47  59  ?   ?   ?   A . n 
A 1 48  ASP 48  60  ?   ?   ?   A . n 
A 1 49  PHE 49  61  61  PHE PHE A . n 
A 1 50  TYR 50  62  62  TYR TYR A . n 
A 1 51  LEU 51  63  63  LEU LEU A . n 
A 1 52  PRO 52  64  64  PRO PRO A . n 
A 1 53  ARG 53  65  65  ARG ARG A . n 
A 1 54  GLU 54  66  66  GLU GLU A . n 
A 1 55  GLU 55  67  67  GLU GLU A . n 
A 1 56  LEU 56  68  68  LEU LEU A . n 
A 1 57  TRP 57  69  69  TRP TRP A . n 
A 1 58  ILE 58  70  70  ILE ILE A . n 
A 1 59  TYR 59  71  71  TYR TYR A . n 
A 1 60  ASN 60  72  72  ASN ASN A . n 
A 1 61  MET 61  73  73  MET MET A . n 
A 1 62  GLU 62  74  74  GLU GLU A . n 
A 1 63  THR 63  75  75  THR THR A . n 
A 1 64  GLY 64  76  76  GLY GLY A . n 
A 1 65  ARG 65  77  77  ARG ARG A . n 
A 1 66  TRP 66  78  78  TRP TRP A . n 
A 1 67  LYS 67  79  79  LYS LYS A . n 
A 1 68  LYS 68  80  80  LYS LYS A . n 
A 1 69  ILE 69  81  81  ILE ILE A . n 
A 1 70  ASN 70  82  82  ASN ASN A . n 
A 1 71  THR 71  83  83  THR THR A . n 
A 1 72  GLU 72  84  84  GLU GLU A . n 
A 1 73  GLY 73  85  85  GLY GLY A . n 
A 1 74  ASP 74  86  86  ASP ASP A . n 
A 1 75  VAL 75  87  87  VAL VAL A . n 
A 1 76  PRO 76  88  88  PRO PRO A . n 
A 1 77  PRO 77  89  89  PRO PRO A . n 
A 1 78  SER 78  90  90  SER SER A . n 
A 1 79  MET 79  91  91  MET MET A . n 
A 1 80  SER 80  92  92  SER SER A . n 
A 1 81  GLY 81  93  93  GLY GLY A . n 
A 1 82  SER 82  94  94  SER SER A . n 
A 1 83  CYS 83  95  95  CYS CYS A . n 
A 1 84  ALA 84  96  96  ALA ALA A . n 
A 1 85  VAL 85  97  97  VAL VAL A . n 
A 1 86  CYS 86  98  98  CYS CYS A . n 
A 1 87  VAL 87  99  99  VAL VAL A . n 
A 1 88  ASP 88  100 100 ASP ASP A . n 
A 1 89  ARG 89  101 101 ARG ARG A . n 
A 1 90  VAL 90  102 102 VAL VAL A . n 
A 1 91  LEU 91  103 103 LEU LEU A . n 
A 1 92  TYR 92  104 104 TYR TYR A . n 
A 1 93  LEU 93  105 105 LEU LEU A . n 
A 1 94  PHE 94  106 106 PHE PHE A . n 
A 1 95  GLY 95  107 107 GLY GLY A . n 
A 1 96  GLY 96  108 108 GLY GLY A . n 
A 1 97  HIS 97  109 109 HIS HIS A . n 
A 1 98  HIS 98  110 110 HIS HIS A . n 
A 1 99  SER 99  111 111 SER SER A . n 
A 1 100 ARG 100 112 112 ARG ARG A . n 
A 1 101 GLY 101 113 113 GLY GLY A . n 
A 1 102 ASN 102 114 114 ASN ASN A . n 
A 1 103 THR 103 115 115 THR THR A . n 
A 1 104 ASN 104 116 116 ASN ASN A . n 
A 1 105 LYS 105 117 117 LYS LYS A . n 
A 1 106 PHE 106 118 118 PHE PHE A . n 
A 1 107 TYR 107 119 119 TYR TYR A . n 
A 1 108 MET 108 120 120 MET MET A . n 
A 1 109 LEU 109 121 121 LEU LEU A . n 
A 1 110 ASP 110 122 122 ASP ASP A . n 
A 1 111 SER 111 123 123 SER SER A . n 
A 1 112 ARG 112 124 124 ARG ARG A . n 
A 1 113 SER 113 125 125 SER SER A . n 
A 1 114 THR 114 126 ?   ?   ?   A . n 
A 1 115 ASP 115 127 ?   ?   ?   A . n 
A 1 116 ARG 116 128 ?   ?   ?   A . n 
A 1 117 VAL 117 129 129 VAL VAL A . n 
A 1 118 LEU 118 130 130 LEU LEU A . n 
A 1 119 GLN 119 131 131 GLN GLN A . n 
A 1 120 TRP 120 132 132 TRP TRP A . n 
A 1 121 GLU 121 133 133 GLU GLU A . n 
A 1 122 ARG 122 134 134 ARG ARG A . n 
A 1 123 ILE 123 135 135 ILE ILE A . n 
A 1 124 ASP 124 136 136 ASP ASP A . n 
A 1 125 CYS 125 137 137 CYS CYS A . n 
A 1 126 GLN 126 138 138 GLN GLN A . n 
A 1 127 GLY 127 139 139 GLY GLY A . n 
A 1 128 ILE 128 140 140 ILE ILE A . n 
A 1 129 PRO 129 141 141 PRO PRO A . n 
A 1 130 PRO 130 142 142 PRO PRO A . n 
A 1 131 SER 131 143 143 SER SER A . n 
A 1 132 SER 132 144 144 SER SER A . n 
A 1 133 LYS 133 145 145 LYS LYS A . n 
A 1 134 ASP 134 146 146 ASP ASP A . n 
A 1 135 LYS 135 147 147 LYS LYS A . n 
A 1 136 LEU 136 148 148 LEU LEU A . n 
A 1 137 GLY 137 149 149 GLY GLY A . n 
A 1 138 VAL 138 150 150 VAL VAL A . n 
A 1 139 TRP 139 151 151 TRP TRP A . n 
A 1 140 VAL 140 152 152 VAL VAL A . n 
A 1 141 TYR 141 153 153 TYR TYR A . n 
A 1 142 LYS 142 154 154 LYS LYS A . n 
A 1 143 ASN 143 155 155 ASN ASN A . n 
A 1 144 LYS 144 156 156 LYS LYS A . n 
A 1 145 LEU 145 157 157 LEU LEU A . n 
A 1 146 ILE 146 158 158 ILE ILE A . n 
A 1 147 PHE 147 159 159 PHE PHE A . n 
A 1 148 PHE 148 160 160 PHE PHE A . n 
A 1 149 GLY 149 161 161 GLY GLY A . n 
A 1 150 GLY 150 162 162 GLY GLY A . n 
A 1 151 TYR 151 163 163 TYR TYR A . n 
A 1 152 GLY 152 164 164 GLY GLY A . n 
A 1 153 TYR 153 165 165 TYR TYR A . n 
A 1 154 LEU 154 166 166 LEU LEU A . n 
A 1 155 PRO 155 167 167 PRO PRO A . n 
A 1 156 GLU 156 168 168 GLU GLU A . n 
A 1 157 ASP 157 169 169 ASP ASP A . n 
A 1 158 LYS 158 170 170 LYS LYS A . n 
A 1 159 VAL 159 171 171 VAL VAL A . n 
A 1 160 LEU 160 172 172 LEU LEU A . n 
A 1 161 GLY 161 173 173 GLY GLY A . n 
A 1 162 THR 162 174 174 THR THR A . n 
A 1 163 PHE 163 175 175 PHE PHE A . n 
A 1 164 GLU 164 176 176 GLU GLU A . n 
A 1 165 PHE 165 177 177 PHE PHE A . n 
A 1 166 ASP 166 178 178 ASP ASP A . n 
A 1 167 GLU 167 179 179 GLU GLU A . n 
A 1 168 THR 168 180 180 THR THR A . n 
A 1 169 SER 169 181 181 SER SER A . n 
A 1 170 PHE 170 182 182 PHE PHE A . n 
A 1 171 TRP 171 183 183 TRP TRP A . n 
A 1 172 ASN 172 184 184 ASN ASN A . n 
A 1 173 SER 173 185 185 SER SER A . n 
A 1 174 SER 174 186 186 SER SER A . n 
A 1 175 HIS 175 187 187 HIS HIS A . n 
A 1 176 PRO 176 188 188 PRO PRO A . n 
A 1 177 ARG 177 189 189 ARG ARG A . n 
A 1 178 GLY 178 190 190 GLY GLY A . n 
A 1 179 TRP 179 191 191 TRP TRP A . n 
A 1 180 ASN 180 192 192 ASN ASN A . n 
A 1 181 ASP 181 193 193 ASP ASP A . n 
A 1 182 HIS 182 194 194 HIS HIS A . n 
A 1 183 VAL 183 195 195 VAL VAL A . n 
A 1 184 HIS 184 196 196 HIS HIS A . n 
A 1 185 ILE 185 197 197 ILE ILE A . n 
A 1 186 LEU 186 198 198 LEU LEU A . n 
A 1 187 ASP 187 199 199 ASP ASP A . n 
A 1 188 THR 188 200 200 THR THR A . n 
A 1 189 GLU 189 201 201 GLU GLU A . n 
A 1 190 THR 190 202 202 THR THR A . n 
A 1 191 PHE 191 203 203 PHE PHE A . n 
A 1 192 THR 192 204 204 THR THR A . n 
A 1 193 TRP 193 205 205 TRP TRP A . n 
A 1 194 SER 194 206 206 SER SER A . n 
A 1 195 GLN 195 207 207 GLN GLN A . n 
A 1 196 PRO 196 208 208 PRO PRO A . n 
A 1 197 ILE 197 209 209 ILE ILE A . n 
A 1 198 THR 198 210 210 THR THR A . n 
A 1 199 THR 199 211 211 THR THR A . n 
A 1 200 GLY 200 212 212 GLY GLY A . n 
A 1 201 LYS 201 213 213 LYS LYS A . n 
A 1 202 ALA 202 214 214 ALA ALA A . n 
A 1 203 PRO 203 215 215 PRO PRO A . n 
A 1 204 SER 204 216 216 SER SER A . n 
A 1 205 PRO 205 217 217 PRO PRO A . n 
A 1 206 ARG 206 218 218 ARG ARG A . n 
A 1 207 ALA 207 219 219 ALA ALA A . n 
A 1 208 ALA 208 220 220 ALA ALA A . n 
A 1 209 HIS 209 221 221 HIS HIS A . n 
A 1 210 ALA 210 222 222 ALA ALA A . n 
A 1 211 CYS 211 223 223 CYS CYS A . n 
A 1 212 ALA 212 224 224 ALA ALA A . n 
A 1 213 THR 213 225 225 THR THR A . n 
A 1 214 VAL 214 226 226 VAL VAL A . n 
A 1 215 GLY 215 227 227 GLY GLY A . n 
A 1 216 ASN 216 228 228 ASN ASN A . n 
A 1 217 ARG 217 229 229 ARG ARG A . n 
A 1 218 GLY 218 230 230 GLY GLY A . n 
A 1 219 PHE 219 231 231 PHE PHE A . n 
A 1 220 VAL 220 232 232 VAL VAL A . n 
A 1 221 PHE 221 233 233 PHE PHE A . n 
A 1 222 GLY 222 234 234 GLY GLY A . n 
A 1 223 GLY 223 235 235 GLY GLY A . n 
A 1 224 ARG 224 236 236 ARG ARG A . n 
A 1 225 TYR 225 237 237 TYR TYR A . n 
A 1 226 ARG 226 238 238 ARG ARG A . n 
A 1 227 ASP 227 239 239 ASP ASP A . n 
A 1 228 ALA 228 240 240 ALA ALA A . n 
A 1 229 ARG 229 241 241 ARG ARG A . n 
A 1 230 MET 230 242 242 MET MET A . n 
A 1 231 ASN 231 243 243 ASN ASN A . n 
A 1 232 ASP 232 244 244 ASP ASP A . n 
A 1 233 LEU 233 245 245 LEU LEU A . n 
A 1 234 HIS 234 246 246 HIS HIS A . n 
A 1 235 TYR 235 247 247 TYR TYR A . n 
A 1 236 LEU 236 248 248 LEU LEU A . n 
A 1 237 ASN 237 249 249 ASN ASN A . n 
A 1 238 LEU 238 250 250 LEU LEU A . n 
A 1 239 ASP 239 251 251 ASP ASP A . n 
A 1 240 THR 240 252 252 THR THR A . n 
A 1 241 TRP 241 253 253 TRP TRP A . n 
A 1 242 GLU 242 254 254 GLU GLU A . n 
A 1 243 TRP 243 255 255 TRP TRP A . n 
A 1 244 ASN 244 256 256 ASN ASN A . n 
A 1 245 GLU 245 257 257 GLU GLU A . n 
A 1 246 LEU 246 258 258 LEU LEU A . n 
A 1 247 ILE 247 259 259 ILE ILE A . n 
A 1 248 PRO 248 260 260 PRO PRO A . n 
A 1 249 GLN 249 261 261 GLN GLN A . n 
A 1 250 GLY 250 262 262 GLY GLY A . n 
A 1 251 ILE 251 263 263 ILE ILE A . n 
A 1 252 CYS 252 264 264 CYS CYS A . n 
A 1 253 PRO 253 265 265 PRO PRO A . n 
A 1 254 VAL 254 266 266 VAL VAL A . n 
A 1 255 GLY 255 267 267 GLY GLY A . n 
A 1 256 ARG 256 268 268 ARG ARG A . n 
A 1 257 SER 257 269 269 SER SER A . n 
A 1 258 TRP 258 270 270 TRP TRP A . n 
A 1 259 HIS 259 271 271 HIS HIS A . n 
A 1 260 SER 260 272 272 SER SER A . n 
A 1 261 LEU 261 273 273 LEU LEU A . n 
A 1 262 THR 262 274 274 THR THR A . n 
A 1 263 PRO 263 275 275 PRO PRO A . n 
A 1 264 VAL 264 276 276 VAL VAL A . n 
A 1 265 SER 265 277 277 SER SER A . n 
A 1 266 SER 266 278 278 SER SER A . n 
A 1 267 ASP 267 279 279 ASP ASP A . n 
A 1 268 HIS 268 280 280 HIS HIS A . n 
A 1 269 LEU 269 281 281 LEU LEU A . n 
A 1 270 PHE 270 282 282 PHE PHE A . n 
A 1 271 LEU 271 283 283 LEU LEU A . n 
A 1 272 PHE 272 284 284 PHE PHE A . n 
A 1 273 GLY 273 285 285 GLY GLY A . n 
A 1 274 GLY 274 286 286 GLY GLY A . n 
A 1 275 PHE 275 287 287 PHE PHE A . n 
A 1 276 THR 276 288 288 THR THR A . n 
A 1 277 THR 277 289 289 THR THR A . n 
A 1 278 ASP 278 290 290 ASP ASP A . n 
A 1 279 LYS 279 291 291 LYS LYS A . n 
A 1 280 GLN 280 292 292 GLN GLN A . n 
A 1 281 PRO 281 293 293 PRO PRO A . n 
A 1 282 LEU 282 294 294 LEU LEU A . n 
A 1 283 SER 283 295 295 SER SER A . n 
A 1 284 ASP 284 296 296 ASP ASP A . n 
A 1 285 ALA 285 297 297 ALA ALA A . n 
A 1 286 TRP 286 298 298 TRP TRP A . n 
A 1 287 THR 287 299 299 THR THR A . n 
A 1 288 TYR 288 300 300 TYR TYR A . n 
A 1 289 CYS 289 301 301 CYS CYS A . n 
A 1 290 ILE 290 302 302 ILE ILE A . n 
A 1 291 SER 291 303 303 SER SER A . n 
A 1 292 LYS 292 304 304 LYS LYS A . n 
A 1 293 ASN 293 305 305 ASN ASN A . n 
A 1 294 GLU 294 306 306 GLU GLU A . n 
A 1 295 TRP 295 307 307 TRP TRP A . n 
A 1 296 ILE 296 308 308 ILE ILE A . n 
A 1 297 GLN 297 309 309 GLN GLN A . n 
A 1 298 PHE 298 310 310 PHE PHE A . n 
A 1 299 ASN 299 311 311 ASN ASN A . n 
A 1 300 HIS 300 312 312 HIS HIS A . n 
A 1 301 PRO 301 313 313 PRO PRO A . n 
A 1 302 TYR 302 314 314 TYR TYR A . n 
A 1 303 THR 303 315 315 THR THR A . n 
A 1 304 GLU 304 316 316 GLU GLU A . n 
A 1 305 LYS 305 317 317 LYS LYS A . n 
A 1 306 PRO 306 318 318 PRO PRO A . n 
A 1 307 ARG 307 319 319 ARG ARG A . n 
A 1 308 LEU 308 320 320 LEU LEU A . n 
A 1 309 TRP 309 321 321 TRP TRP A . n 
A 1 310 HIS 310 322 322 HIS HIS A . n 
A 1 311 THR 311 323 323 THR THR A . n 
A 1 312 ALA 312 324 324 ALA ALA A . n 
A 1 313 CYS 313 325 325 CYS CYS A . n 
A 1 314 ALA 314 326 326 ALA ALA A . n 
A 1 315 SER 315 327 327 SER SER A . n 
A 1 316 ASP 316 328 328 ASP ASP A . n 
A 1 317 GLU 317 329 329 GLU GLU A . n 
A 1 318 GLY 318 330 330 GLY GLY A . n 
A 1 319 GLU 319 331 331 GLU GLU A . n 
A 1 320 VAL 320 332 332 VAL VAL A . n 
A 1 321 ILE 321 333 333 ILE ILE A . n 
A 1 322 VAL 322 334 334 VAL VAL A . n 
A 1 323 PHE 323 335 335 PHE PHE A . n 
A 1 324 GLY 324 336 336 GLY GLY A . n 
A 1 325 GLY 325 337 337 GLY GLY A . n 
A 1 326 CYS 326 338 338 CYS CYS A . n 
A 1 327 ALA 327 339 339 ALA ALA A . n 
A 1 328 ASN 328 340 340 ASN ASN A . n 
A 1 329 ASN 329 341 341 ASN ASN A . n 
A 1 330 LEU 330 342 342 LEU LEU A . n 
A 1 331 LEU 331 343 343 LEU LEU A . n 
A 1 332 VAL 332 344 344 VAL VAL A . n 
A 1 333 HIS 333 345 345 HIS HIS A . n 
A 1 334 HIS 334 346 346 HIS HIS A . n 
A 1 335 ARG 335 347 347 ARG ARG A . n 
A 1 336 ALA 336 348 348 ALA ALA A . n 
A 1 337 ALA 337 349 349 ALA ALA A . n 
A 1 338 HIS 338 350 350 HIS HIS A . n 
A 1 339 SER 339 351 351 SER SER A . n 
A 1 340 ASN 340 352 352 ASN ASN A . n 
A 1 341 GLU 341 353 353 GLU GLU A . n 
A 1 342 ILE 342 354 354 ILE ILE A . n 
A 1 343 LEU 343 355 355 LEU LEU A . n 
A 1 344 ILE 344 356 356 ILE ILE A . n 
A 1 345 PHE 345 357 357 PHE PHE A . n 
A 1 346 SER 346 358 358 SER SER A . n 
A 1 347 VAL 347 359 359 VAL VAL A . n 
A 1 348 GLN 348 360 360 GLN GLN A . n 
A 1 349 PRO 349 361 ?   ?   ?   A . n 
B 1 1   GLY 1   13  ?   ?   ?   B . n 
B 1 2   SER 2   14  ?   ?   ?   B . n 
B 1 3   GLY 3   15  ?   ?   ?   B . n 
B 1 4   PRO 4   16  ?   ?   ?   B . n 
B 1 5   ALA 5   17  ?   ?   ?   B . n 
B 1 6   PHE 6   18  ?   ?   ?   B . n 
B 1 7   GLU 7   19  ?   ?   ?   B . n 
B 1 8   SER 8   20  ?   ?   ?   B . n 
B 1 9   TYR 9   21  ?   ?   ?   B . n 
B 1 10  GLU 10  22  ?   ?   ?   B . n 
B 1 11  SER 11  23  ?   ?   ?   B . n 
B 1 12  MET 12  24  ?   ?   ?   B . n 
B 1 13  GLU 13  25  ?   ?   ?   B . n 
B 1 14  LEU 14  26  26  LEU LEU B . n 
B 1 15  ALA 15  27  27  ALA ALA B . n 
B 1 16  CYS 16  28  28  CYS CYS B . n 
B 1 17  PRO 17  29  29  PRO PRO B . n 
B 1 18  ALA 18  30  30  ALA ALA B . n 
B 1 19  GLU 19  31  31  GLU GLU B . n 
B 1 20  ARG 20  32  32  ARG ARG B . n 
B 1 21  SER 21  33  33  SER SER B . n 
B 1 22  GLY 22  34  34  GLY GLY B . n 
B 1 23  HIS 23  35  35  HIS HIS B . n 
B 1 24  VAL 24  36  36  VAL VAL B . n 
B 1 25  ALA 25  37  37  ALA ALA B . n 
B 1 26  VAL 26  38  38  VAL VAL B . n 
B 1 27  SER 27  39  39  SER SER B . n 
B 1 28  ASP 28  40  40  ASP ASP B . n 
B 1 29  GLY 29  41  41  GLY GLY B . n 
B 1 30  ARG 30  42  42  ARG ARG B . n 
B 1 31  HIS 31  43  43  HIS HIS B . n 
B 1 32  MET 32  44  44  MET MET B . n 
B 1 33  PHE 33  45  45  PHE PHE B . n 
B 1 34  VAL 34  46  46  VAL VAL B . n 
B 1 35  TRP 35  47  47  TRP TRP B . n 
B 1 36  GLY 36  48  48  GLY GLY B . n 
B 1 37  GLY 37  49  49  GLY GLY B . n 
B 1 38  TYR 38  50  50  TYR TYR B . n 
B 1 39  LYS 39  51  51  LYS LYS B . n 
B 1 40  SER 40  52  52  SER SER B . n 
B 1 41  ASN 41  53  53  ASN ASN B . n 
B 1 42  GLN 42  54  ?   ?   ?   B . n 
B 1 43  VAL 43  55  ?   ?   ?   B . n 
B 1 44  ARG 44  56  ?   ?   ?   B . n 
B 1 45  GLY 45  57  ?   ?   ?   B . n 
B 1 46  LEU 46  58  ?   ?   ?   B . n 
B 1 47  TYR 47  59  ?   ?   ?   B . n 
B 1 48  ASP 48  60  ?   ?   ?   B . n 
B 1 49  PHE 49  61  61  PHE PHE B . n 
B 1 50  TYR 50  62  62  TYR TYR B . n 
B 1 51  LEU 51  63  63  LEU LEU B . n 
B 1 52  PRO 52  64  64  PRO PRO B . n 
B 1 53  ARG 53  65  65  ARG ARG B . n 
B 1 54  GLU 54  66  66  GLU GLU B . n 
B 1 55  GLU 55  67  67  GLU GLU B . n 
B 1 56  LEU 56  68  68  LEU LEU B . n 
B 1 57  TRP 57  69  69  TRP TRP B . n 
B 1 58  ILE 58  70  70  ILE ILE B . n 
B 1 59  TYR 59  71  71  TYR TYR B . n 
B 1 60  ASN 60  72  72  ASN ASN B . n 
B 1 61  MET 61  73  73  MET MET B . n 
B 1 62  GLU 62  74  74  GLU GLU B . n 
B 1 63  THR 63  75  75  THR THR B . n 
B 1 64  GLY 64  76  76  GLY GLY B . n 
B 1 65  ARG 65  77  77  ARG ARG B . n 
B 1 66  TRP 66  78  78  TRP TRP B . n 
B 1 67  LYS 67  79  79  LYS LYS B . n 
B 1 68  LYS 68  80  80  LYS LYS B . n 
B 1 69  ILE 69  81  81  ILE ILE B . n 
B 1 70  ASN 70  82  82  ASN ASN B . n 
B 1 71  THR 71  83  83  THR THR B . n 
B 1 72  GLU 72  84  84  GLU GLU B . n 
B 1 73  GLY 73  85  85  GLY GLY B . n 
B 1 74  ASP 74  86  86  ASP ASP B . n 
B 1 75  VAL 75  87  87  VAL VAL B . n 
B 1 76  PRO 76  88  88  PRO PRO B . n 
B 1 77  PRO 77  89  89  PRO PRO B . n 
B 1 78  SER 78  90  90  SER SER B . n 
B 1 79  MET 79  91  91  MET MET B . n 
B 1 80  SER 80  92  92  SER SER B . n 
B 1 81  GLY 81  93  93  GLY GLY B . n 
B 1 82  SER 82  94  94  SER SER B . n 
B 1 83  CYS 83  95  95  CYS CYS B . n 
B 1 84  ALA 84  96  96  ALA ALA B . n 
B 1 85  VAL 85  97  97  VAL VAL B . n 
B 1 86  CYS 86  98  98  CYS CYS B . n 
B 1 87  VAL 87  99  99  VAL VAL B . n 
B 1 88  ASP 88  100 100 ASP ASP B . n 
B 1 89  ARG 89  101 101 ARG ARG B . n 
B 1 90  VAL 90  102 102 VAL VAL B . n 
B 1 91  LEU 91  103 103 LEU LEU B . n 
B 1 92  TYR 92  104 104 TYR TYR B . n 
B 1 93  LEU 93  105 105 LEU LEU B . n 
B 1 94  PHE 94  106 106 PHE PHE B . n 
B 1 95  GLY 95  107 107 GLY GLY B . n 
B 1 96  GLY 96  108 108 GLY GLY B . n 
B 1 97  HIS 97  109 109 HIS HIS B . n 
B 1 98  HIS 98  110 110 HIS HIS B . n 
B 1 99  SER 99  111 111 SER SER B . n 
B 1 100 ARG 100 112 112 ARG ARG B . n 
B 1 101 GLY 101 113 113 GLY GLY B . n 
B 1 102 ASN 102 114 114 ASN ASN B . n 
B 1 103 THR 103 115 115 THR THR B . n 
B 1 104 ASN 104 116 116 ASN ASN B . n 
B 1 105 LYS 105 117 117 LYS LYS B . n 
B 1 106 PHE 106 118 118 PHE PHE B . n 
B 1 107 TYR 107 119 119 TYR TYR B . n 
B 1 108 MET 108 120 120 MET MET B . n 
B 1 109 LEU 109 121 121 LEU LEU B . n 
B 1 110 ASP 110 122 122 ASP ASP B . n 
B 1 111 SER 111 123 123 SER SER B . n 
B 1 112 ARG 112 124 124 ARG ARG B . n 
B 1 113 SER 113 125 125 SER SER B . n 
B 1 114 THR 114 126 ?   ?   ?   B . n 
B 1 115 ASP 115 127 ?   ?   ?   B . n 
B 1 116 ARG 116 128 ?   ?   ?   B . n 
B 1 117 VAL 117 129 129 VAL VAL B . n 
B 1 118 LEU 118 130 130 LEU LEU B . n 
B 1 119 GLN 119 131 131 GLN GLN B . n 
B 1 120 TRP 120 132 132 TRP TRP B . n 
B 1 121 GLU 121 133 133 GLU GLU B . n 
B 1 122 ARG 122 134 134 ARG ARG B . n 
B 1 123 ILE 123 135 135 ILE ILE B . n 
B 1 124 ASP 124 136 136 ASP ASP B . n 
B 1 125 CYS 125 137 137 CYS CYS B . n 
B 1 126 GLN 126 138 138 GLN GLN B . n 
B 1 127 GLY 127 139 139 GLY GLY B . n 
B 1 128 ILE 128 140 140 ILE ILE B . n 
B 1 129 PRO 129 141 141 PRO PRO B . n 
B 1 130 PRO 130 142 142 PRO PRO B . n 
B 1 131 SER 131 143 143 SER SER B . n 
B 1 132 SER 132 144 144 SER SER B . n 
B 1 133 LYS 133 145 145 LYS LYS B . n 
B 1 134 ASP 134 146 146 ASP ASP B . n 
B 1 135 LYS 135 147 147 LYS LYS B . n 
B 1 136 LEU 136 148 148 LEU LEU B . n 
B 1 137 GLY 137 149 149 GLY GLY B . n 
B 1 138 VAL 138 150 150 VAL VAL B . n 
B 1 139 TRP 139 151 151 TRP TRP B . n 
B 1 140 VAL 140 152 152 VAL VAL B . n 
B 1 141 TYR 141 153 153 TYR TYR B . n 
B 1 142 LYS 142 154 154 LYS LYS B . n 
B 1 143 ASN 143 155 155 ASN ASN B . n 
B 1 144 LYS 144 156 156 LYS LYS B . n 
B 1 145 LEU 145 157 157 LEU LEU B . n 
B 1 146 ILE 146 158 158 ILE ILE B . n 
B 1 147 PHE 147 159 159 PHE PHE B . n 
B 1 148 PHE 148 160 160 PHE PHE B . n 
B 1 149 GLY 149 161 161 GLY GLY B . n 
B 1 150 GLY 150 162 162 GLY GLY B . n 
B 1 151 TYR 151 163 163 TYR TYR B . n 
B 1 152 GLY 152 164 164 GLY GLY B . n 
B 1 153 TYR 153 165 165 TYR TYR B . n 
B 1 154 LEU 154 166 166 LEU LEU B . n 
B 1 155 PRO 155 167 167 PRO PRO B . n 
B 1 156 GLU 156 168 168 GLU GLU B . n 
B 1 157 ASP 157 169 169 ASP ASP B . n 
B 1 158 LYS 158 170 170 LYS LYS B . n 
B 1 159 VAL 159 171 171 VAL VAL B . n 
B 1 160 LEU 160 172 172 LEU LEU B . n 
B 1 161 GLY 161 173 173 GLY GLY B . n 
B 1 162 THR 162 174 174 THR THR B . n 
B 1 163 PHE 163 175 175 PHE PHE B . n 
B 1 164 GLU 164 176 176 GLU GLU B . n 
B 1 165 PHE 165 177 177 PHE PHE B . n 
B 1 166 ASP 166 178 178 ASP ASP B . n 
B 1 167 GLU 167 179 179 GLU GLU B . n 
B 1 168 THR 168 180 180 THR THR B . n 
B 1 169 SER 169 181 181 SER SER B . n 
B 1 170 PHE 170 182 182 PHE PHE B . n 
B 1 171 TRP 171 183 183 TRP TRP B . n 
B 1 172 ASN 172 184 184 ASN ASN B . n 
B 1 173 SER 173 185 185 SER SER B . n 
B 1 174 SER 174 186 186 SER SER B . n 
B 1 175 HIS 175 187 187 HIS HIS B . n 
B 1 176 PRO 176 188 188 PRO PRO B . n 
B 1 177 ARG 177 189 189 ARG ARG B . n 
B 1 178 GLY 178 190 190 GLY GLY B . n 
B 1 179 TRP 179 191 191 TRP TRP B . n 
B 1 180 ASN 180 192 192 ASN ASN B . n 
B 1 181 ASP 181 193 193 ASP ASP B . n 
B 1 182 HIS 182 194 194 HIS HIS B . n 
B 1 183 VAL 183 195 195 VAL VAL B . n 
B 1 184 HIS 184 196 196 HIS HIS B . n 
B 1 185 ILE 185 197 197 ILE ILE B . n 
B 1 186 LEU 186 198 198 LEU LEU B . n 
B 1 187 ASP 187 199 199 ASP ASP B . n 
B 1 188 THR 188 200 200 THR THR B . n 
B 1 189 GLU 189 201 201 GLU GLU B . n 
B 1 190 THR 190 202 202 THR THR B . n 
B 1 191 PHE 191 203 203 PHE PHE B . n 
B 1 192 THR 192 204 204 THR THR B . n 
B 1 193 TRP 193 205 205 TRP TRP B . n 
B 1 194 SER 194 206 206 SER SER B . n 
B 1 195 GLN 195 207 207 GLN GLN B . n 
B 1 196 PRO 196 208 208 PRO PRO B . n 
B 1 197 ILE 197 209 209 ILE ILE B . n 
B 1 198 THR 198 210 210 THR THR B . n 
B 1 199 THR 199 211 211 THR THR B . n 
B 1 200 GLY 200 212 212 GLY GLY B . n 
B 1 201 LYS 201 213 213 LYS LYS B . n 
B 1 202 ALA 202 214 214 ALA ALA B . n 
B 1 203 PRO 203 215 215 PRO PRO B . n 
B 1 204 SER 204 216 216 SER SER B . n 
B 1 205 PRO 205 217 217 PRO PRO B . n 
B 1 206 ARG 206 218 218 ARG ARG B . n 
B 1 207 ALA 207 219 219 ALA ALA B . n 
B 1 208 ALA 208 220 220 ALA ALA B . n 
B 1 209 HIS 209 221 221 HIS HIS B . n 
B 1 210 ALA 210 222 222 ALA ALA B . n 
B 1 211 CYS 211 223 223 CYS CYS B . n 
B 1 212 ALA 212 224 224 ALA ALA B . n 
B 1 213 THR 213 225 225 THR THR B . n 
B 1 214 VAL 214 226 226 VAL VAL B . n 
B 1 215 GLY 215 227 227 GLY GLY B . n 
B 1 216 ASN 216 228 228 ASN ASN B . n 
B 1 217 ARG 217 229 229 ARG ARG B . n 
B 1 218 GLY 218 230 230 GLY GLY B . n 
B 1 219 PHE 219 231 231 PHE PHE B . n 
B 1 220 VAL 220 232 232 VAL VAL B . n 
B 1 221 PHE 221 233 233 PHE PHE B . n 
B 1 222 GLY 222 234 234 GLY GLY B . n 
B 1 223 GLY 223 235 235 GLY GLY B . n 
B 1 224 ARG 224 236 236 ARG ARG B . n 
B 1 225 TYR 225 237 237 TYR TYR B . n 
B 1 226 ARG 226 238 238 ARG ARG B . n 
B 1 227 ASP 227 239 239 ASP ASP B . n 
B 1 228 ALA 228 240 240 ALA ALA B . n 
B 1 229 ARG 229 241 241 ARG ARG B . n 
B 1 230 MET 230 242 242 MET MET B . n 
B 1 231 ASN 231 243 243 ASN ASN B . n 
B 1 232 ASP 232 244 244 ASP ASP B . n 
B 1 233 LEU 233 245 245 LEU LEU B . n 
B 1 234 HIS 234 246 246 HIS HIS B . n 
B 1 235 TYR 235 247 247 TYR TYR B . n 
B 1 236 LEU 236 248 248 LEU LEU B . n 
B 1 237 ASN 237 249 249 ASN ASN B . n 
B 1 238 LEU 238 250 250 LEU LEU B . n 
B 1 239 ASP 239 251 251 ASP ASP B . n 
B 1 240 THR 240 252 252 THR THR B . n 
B 1 241 TRP 241 253 253 TRP TRP B . n 
B 1 242 GLU 242 254 254 GLU GLU B . n 
B 1 243 TRP 243 255 255 TRP TRP B . n 
B 1 244 ASN 244 256 256 ASN ASN B . n 
B 1 245 GLU 245 257 257 GLU GLU B . n 
B 1 246 LEU 246 258 258 LEU LEU B . n 
B 1 247 ILE 247 259 259 ILE ILE B . n 
B 1 248 PRO 248 260 260 PRO PRO B . n 
B 1 249 GLN 249 261 261 GLN GLN B . n 
B 1 250 GLY 250 262 262 GLY GLY B . n 
B 1 251 ILE 251 263 263 ILE ILE B . n 
B 1 252 CYS 252 264 264 CYS CYS B . n 
B 1 253 PRO 253 265 265 PRO PRO B . n 
B 1 254 VAL 254 266 266 VAL VAL B . n 
B 1 255 GLY 255 267 267 GLY GLY B . n 
B 1 256 ARG 256 268 268 ARG ARG B . n 
B 1 257 SER 257 269 269 SER SER B . n 
B 1 258 TRP 258 270 270 TRP TRP B . n 
B 1 259 HIS 259 271 271 HIS HIS B . n 
B 1 260 SER 260 272 272 SER SER B . n 
B 1 261 LEU 261 273 273 LEU LEU B . n 
B 1 262 THR 262 274 274 THR THR B . n 
B 1 263 PRO 263 275 275 PRO PRO B . n 
B 1 264 VAL 264 276 276 VAL VAL B . n 
B 1 265 SER 265 277 277 SER SER B . n 
B 1 266 SER 266 278 278 SER SER B . n 
B 1 267 ASP 267 279 279 ASP ASP B . n 
B 1 268 HIS 268 280 280 HIS HIS B . n 
B 1 269 LEU 269 281 281 LEU LEU B . n 
B 1 270 PHE 270 282 282 PHE PHE B . n 
B 1 271 LEU 271 283 283 LEU LEU B . n 
B 1 272 PHE 272 284 284 PHE PHE B . n 
B 1 273 GLY 273 285 285 GLY GLY B . n 
B 1 274 GLY 274 286 286 GLY GLY B . n 
B 1 275 PHE 275 287 287 PHE PHE B . n 
B 1 276 THR 276 288 288 THR THR B . n 
B 1 277 THR 277 289 289 THR THR B . n 
B 1 278 ASP 278 290 290 ASP ASP B . n 
B 1 279 LYS 279 291 291 LYS LYS B . n 
B 1 280 GLN 280 292 292 GLN GLN B . n 
B 1 281 PRO 281 293 293 PRO PRO B . n 
B 1 282 LEU 282 294 294 LEU LEU B . n 
B 1 283 SER 283 295 295 SER SER B . n 
B 1 284 ASP 284 296 296 ASP ASP B . n 
B 1 285 ALA 285 297 297 ALA ALA B . n 
B 1 286 TRP 286 298 298 TRP TRP B . n 
B 1 287 THR 287 299 299 THR THR B . n 
B 1 288 TYR 288 300 300 TYR TYR B . n 
B 1 289 CYS 289 301 301 CYS CYS B . n 
B 1 290 ILE 290 302 302 ILE ILE B . n 
B 1 291 SER 291 303 303 SER SER B . n 
B 1 292 LYS 292 304 304 LYS LYS B . n 
B 1 293 ASN 293 305 305 ASN ASN B . n 
B 1 294 GLU 294 306 306 GLU GLU B . n 
B 1 295 TRP 295 307 307 TRP TRP B . n 
B 1 296 ILE 296 308 308 ILE ILE B . n 
B 1 297 GLN 297 309 309 GLN GLN B . n 
B 1 298 PHE 298 310 310 PHE PHE B . n 
B 1 299 ASN 299 311 311 ASN ASN B . n 
B 1 300 HIS 300 312 312 HIS HIS B . n 
B 1 301 PRO 301 313 313 PRO PRO B . n 
B 1 302 TYR 302 314 314 TYR TYR B . n 
B 1 303 THR 303 315 315 THR THR B . n 
B 1 304 GLU 304 316 316 GLU GLU B . n 
B 1 305 LYS 305 317 317 LYS LYS B . n 
B 1 306 PRO 306 318 318 PRO PRO B . n 
B 1 307 ARG 307 319 319 ARG ARG B . n 
B 1 308 LEU 308 320 320 LEU LEU B . n 
B 1 309 TRP 309 321 321 TRP TRP B . n 
B 1 310 HIS 310 322 322 HIS HIS B . n 
B 1 311 THR 311 323 323 THR THR B . n 
B 1 312 ALA 312 324 324 ALA ALA B . n 
B 1 313 CYS 313 325 325 CYS CYS B . n 
B 1 314 ALA 314 326 326 ALA ALA B . n 
B 1 315 SER 315 327 327 SER SER B . n 
B 1 316 ASP 316 328 328 ASP ASP B . n 
B 1 317 GLU 317 329 329 GLU GLU B . n 
B 1 318 GLY 318 330 330 GLY GLY B . n 
B 1 319 GLU 319 331 331 GLU GLU B . n 
B 1 320 VAL 320 332 332 VAL VAL B . n 
B 1 321 ILE 321 333 333 ILE ILE B . n 
B 1 322 VAL 322 334 334 VAL VAL B . n 
B 1 323 PHE 323 335 335 PHE PHE B . n 
B 1 324 GLY 324 336 336 GLY GLY B . n 
B 1 325 GLY 325 337 337 GLY GLY B . n 
B 1 326 CYS 326 338 338 CYS CYS B . n 
B 1 327 ALA 327 339 339 ALA ALA B . n 
B 1 328 ASN 328 340 340 ASN ASN B . n 
B 1 329 ASN 329 341 341 ASN ASN B . n 
B 1 330 LEU 330 342 342 LEU LEU B . n 
B 1 331 LEU 331 343 343 LEU LEU B . n 
B 1 332 VAL 332 344 344 VAL VAL B . n 
B 1 333 HIS 333 345 345 HIS HIS B . n 
B 1 334 HIS 334 346 346 HIS HIS B . n 
B 1 335 ARG 335 347 347 ARG ARG B . n 
B 1 336 ALA 336 348 348 ALA ALA B . n 
B 1 337 ALA 337 349 349 ALA ALA B . n 
B 1 338 HIS 338 350 350 HIS HIS B . n 
B 1 339 SER 339 351 351 SER SER B . n 
B 1 340 ASN 340 352 352 ASN ASN B . n 
B 1 341 GLU 341 353 353 GLU GLU B . n 
B 1 342 ILE 342 354 354 ILE ILE B . n 
B 1 343 LEU 343 355 355 LEU LEU B . n 
B 1 344 ILE 344 356 356 ILE ILE B . n 
B 1 345 PHE 345 357 357 PHE PHE B . n 
B 1 346 SER 346 358 358 SER SER B . n 
B 1 347 VAL 347 359 359 VAL VAL B . n 
B 1 348 GLN 348 360 360 GLN GLN B . n 
B 1 349 PRO 349 361 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1APS 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1APS 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1APS 1   401 1   A1APS LIG A . 
D 3 NCO   1   402 1   NCO   NCO A . 
E 2 A1APS 1   401 2   A1APS LIG B . 
F 4 HOH   1   501 88  HOH   HOH A . 
F 4 HOH   2   502 37  HOH   HOH A . 
F 4 HOH   3   503 451 HOH   HOH A . 
F 4 HOH   4   504 454 HOH   HOH A . 
F 4 HOH   5   505 377 HOH   HOH A . 
F 4 HOH   6   506 329 HOH   HOH A . 
F 4 HOH   7   507 335 HOH   HOH A . 
F 4 HOH   8   508 262 HOH   HOH A . 
F 4 HOH   9   509 135 HOH   HOH A . 
F 4 HOH   10  510 375 HOH   HOH A . 
F 4 HOH   11  511 208 HOH   HOH A . 
F 4 HOH   12  512 247 HOH   HOH A . 
F 4 HOH   13  513 439 HOH   HOH A . 
F 4 HOH   14  514 123 HOH   HOH A . 
F 4 HOH   15  515 172 HOH   HOH A . 
F 4 HOH   16  516 245 HOH   HOH A . 
F 4 HOH   17  517 471 HOH   HOH A . 
F 4 HOH   18  518 326 HOH   HOH A . 
F 4 HOH   19  519 260 HOH   HOH A . 
F 4 HOH   20  520 26  HOH   HOH A . 
F 4 HOH   21  521 191 HOH   HOH A . 
F 4 HOH   22  522 81  HOH   HOH A . 
F 4 HOH   23  523 476 HOH   HOH A . 
F 4 HOH   24  524 474 HOH   HOH A . 
F 4 HOH   25  525 157 HOH   HOH A . 
F 4 HOH   26  526 143 HOH   HOH A . 
F 4 HOH   27  527 160 HOH   HOH A . 
F 4 HOH   28  528 387 HOH   HOH A . 
F 4 HOH   29  529 68  HOH   HOH A . 
F 4 HOH   30  530 333 HOH   HOH A . 
F 4 HOH   31  531 2   HOH   HOH A . 
F 4 HOH   32  532 210 HOH   HOH A . 
F 4 HOH   33  533 253 HOH   HOH A . 
F 4 HOH   34  534 395 HOH   HOH A . 
F 4 HOH   35  535 46  HOH   HOH A . 
F 4 HOH   36  536 77  HOH   HOH A . 
F 4 HOH   37  537 142 HOH   HOH A . 
F 4 HOH   38  538 430 HOH   HOH A . 
F 4 HOH   39  539 100 HOH   HOH A . 
F 4 HOH   40  540 152 HOH   HOH A . 
F 4 HOH   41  541 354 HOH   HOH A . 
F 4 HOH   42  542 288 HOH   HOH A . 
F 4 HOH   43  543 274 HOH   HOH A . 
F 4 HOH   44  544 399 HOH   HOH A . 
F 4 HOH   45  545 118 HOH   HOH A . 
F 4 HOH   46  546 215 HOH   HOH A . 
F 4 HOH   47  547 419 HOH   HOH A . 
F 4 HOH   48  548 289 HOH   HOH A . 
F 4 HOH   49  549 258 HOH   HOH A . 
F 4 HOH   50  550 49  HOH   HOH A . 
F 4 HOH   51  551 32  HOH   HOH A . 
F 4 HOH   52  552 80  HOH   HOH A . 
F 4 HOH   53  553 435 HOH   HOH A . 
F 4 HOH   54  554 207 HOH   HOH A . 
F 4 HOH   55  555 103 HOH   HOH A . 
F 4 HOH   56  556 222 HOH   HOH A . 
F 4 HOH   57  557 312 HOH   HOH A . 
F 4 HOH   58  558 257 HOH   HOH A . 
F 4 HOH   59  559 362 HOH   HOH A . 
F 4 HOH   60  560 132 HOH   HOH A . 
F 4 HOH   61  561 14  HOH   HOH A . 
F 4 HOH   62  562 158 HOH   HOH A . 
F 4 HOH   63  563 416 HOH   HOH A . 
F 4 HOH   64  564 125 HOH   HOH A . 
F 4 HOH   65  565 177 HOH   HOH A . 
F 4 HOH   66  566 379 HOH   HOH A . 
F 4 HOH   67  567 5   HOH   HOH A . 
F 4 HOH   68  568 9   HOH   HOH A . 
F 4 HOH   69  569 213 HOH   HOH A . 
F 4 HOH   70  570 401 HOH   HOH A . 
F 4 HOH   71  571 221 HOH   HOH A . 
F 4 HOH   72  572 7   HOH   HOH A . 
F 4 HOH   73  573 147 HOH   HOH A . 
F 4 HOH   74  574 134 HOH   HOH A . 
F 4 HOH   75  575 462 HOH   HOH A . 
F 4 HOH   76  576 327 HOH   HOH A . 
F 4 HOH   77  577 145 HOH   HOH A . 
F 4 HOH   78  578 286 HOH   HOH A . 
F 4 HOH   79  579 137 HOH   HOH A . 
F 4 HOH   80  580 340 HOH   HOH A . 
F 4 HOH   81  581 12  HOH   HOH A . 
F 4 HOH   82  582 346 HOH   HOH A . 
F 4 HOH   83  583 370 HOH   HOH A . 
F 4 HOH   84  584 112 HOH   HOH A . 
F 4 HOH   85  585 22  HOH   HOH A . 
F 4 HOH   86  586 89  HOH   HOH A . 
F 4 HOH   87  587 440 HOH   HOH A . 
F 4 HOH   88  588 237 HOH   HOH A . 
F 4 HOH   89  589 287 HOH   HOH A . 
F 4 HOH   90  590 442 HOH   HOH A . 
F 4 HOH   91  591 233 HOH   HOH A . 
F 4 HOH   92  592 45  HOH   HOH A . 
F 4 HOH   93  593 428 HOH   HOH A . 
F 4 HOH   94  594 28  HOH   HOH A . 
F 4 HOH   95  595 209 HOH   HOH A . 
F 4 HOH   96  596 165 HOH   HOH A . 
F 4 HOH   97  597 341 HOH   HOH A . 
F 4 HOH   98  598 473 HOH   HOH A . 
F 4 HOH   99  599 113 HOH   HOH A . 
F 4 HOH   100 600 104 HOH   HOH A . 
F 4 HOH   101 601 79  HOH   HOH A . 
F 4 HOH   102 602 20  HOH   HOH A . 
F 4 HOH   103 603 190 HOH   HOH A . 
F 4 HOH   104 604 292 HOH   HOH A . 
F 4 HOH   105 605 64  HOH   HOH A . 
F 4 HOH   106 606 4   HOH   HOH A . 
F 4 HOH   107 607 38  HOH   HOH A . 
F 4 HOH   108 608 443 HOH   HOH A . 
F 4 HOH   109 609 53  HOH   HOH A . 
F 4 HOH   110 610 151 HOH   HOH A . 
F 4 HOH   111 611 169 HOH   HOH A . 
F 4 HOH   112 612 61  HOH   HOH A . 
F 4 HOH   113 613 138 HOH   HOH A . 
F 4 HOH   114 614 380 HOH   HOH A . 
F 4 HOH   115 615 93  HOH   HOH A . 
F 4 HOH   116 616 3   HOH   HOH A . 
F 4 HOH   117 617 108 HOH   HOH A . 
F 4 HOH   118 618 261 HOH   HOH A . 
F 4 HOH   119 619 293 HOH   HOH A . 
F 4 HOH   120 620 131 HOH   HOH A . 
F 4 HOH   121 621 404 HOH   HOH A . 
F 4 HOH   122 622 50  HOH   HOH A . 
F 4 HOH   123 623 129 HOH   HOH A . 
F 4 HOH   124 624 357 HOH   HOH A . 
F 4 HOH   125 625 220 HOH   HOH A . 
F 4 HOH   126 626 63  HOH   HOH A . 
F 4 HOH   127 627 57  HOH   HOH A . 
F 4 HOH   128 628 153 HOH   HOH A . 
F 4 HOH   129 629 36  HOH   HOH A . 
F 4 HOH   130 630 432 HOH   HOH A . 
F 4 HOH   131 631 198 HOH   HOH A . 
F 4 HOH   132 632 114 HOH   HOH A . 
F 4 HOH   133 633 384 HOH   HOH A . 
F 4 HOH   134 634 214 HOH   HOH A . 
F 4 HOH   135 635 176 HOH   HOH A . 
F 4 HOH   136 636 318 HOH   HOH A . 
F 4 HOH   137 637 230 HOH   HOH A . 
F 4 HOH   138 638 159 HOH   HOH A . 
F 4 HOH   139 639 139 HOH   HOH A . 
F 4 HOH   140 640 217 HOH   HOH A . 
F 4 HOH   141 641 51  HOH   HOH A . 
F 4 HOH   142 642 99  HOH   HOH A . 
F 4 HOH   143 643 110 HOH   HOH A . 
F 4 HOH   144 644 83  HOH   HOH A . 
F 4 HOH   145 645 156 HOH   HOH A . 
F 4 HOH   146 646 106 HOH   HOH A . 
F 4 HOH   147 647 54  HOH   HOH A . 
F 4 HOH   148 648 360 HOH   HOH A . 
F 4 HOH   149 649 58  HOH   HOH A . 
F 4 HOH   150 650 178 HOH   HOH A . 
F 4 HOH   151 651 120 HOH   HOH A . 
F 4 HOH   152 652 168 HOH   HOH A . 
F 4 HOH   153 653 144 HOH   HOH A . 
F 4 HOH   154 654 19  HOH   HOH A . 
F 4 HOH   155 655 127 HOH   HOH A . 
F 4 HOH   156 656 175 HOH   HOH A . 
F 4 HOH   157 657 229 HOH   HOH A . 
F 4 HOH   158 658 437 HOH   HOH A . 
F 4 HOH   159 659 121 HOH   HOH A . 
F 4 HOH   160 660 204 HOH   HOH A . 
F 4 HOH   161 661 71  HOH   HOH A . 
F 4 HOH   162 662 303 HOH   HOH A . 
F 4 HOH   163 663 403 HOH   HOH A . 
F 4 HOH   164 664 133 HOH   HOH A . 
F 4 HOH   165 665 13  HOH   HOH A . 
F 4 HOH   166 666 324 HOH   HOH A . 
F 4 HOH   167 667 199 HOH   HOH A . 
F 4 HOH   168 668 182 HOH   HOH A . 
F 4 HOH   169 669 150 HOH   HOH A . 
F 4 HOH   170 670 140 HOH   HOH A . 
F 4 HOH   171 671 248 HOH   HOH A . 
F 4 HOH   172 672 268 HOH   HOH A . 
F 4 HOH   173 673 56  HOH   HOH A . 
F 4 HOH   174 674 282 HOH   HOH A . 
F 4 HOH   175 675 328 HOH   HOH A . 
F 4 HOH   176 676 348 HOH   HOH A . 
F 4 HOH   177 677 211 HOH   HOH A . 
F 4 HOH   178 678 460 HOH   HOH A . 
F 4 HOH   179 679 304 HOH   HOH A . 
F 4 HOH   180 680 313 HOH   HOH A . 
F 4 HOH   181 681 317 HOH   HOH A . 
F 4 HOH   182 682 477 HOH   HOH A . 
F 4 HOH   183 683 332 HOH   HOH A . 
F 4 HOH   184 684 280 HOH   HOH A . 
F 4 HOH   185 685 270 HOH   HOH A . 
F 4 HOH   186 686 376 HOH   HOH A . 
F 4 HOH   187 687 455 HOH   HOH A . 
F 4 HOH   188 688 294 HOH   HOH A . 
F 4 HOH   189 689 438 HOH   HOH A . 
F 4 HOH   190 690 413 HOH   HOH A . 
F 4 HOH   191 691 424 HOH   HOH A . 
F 4 HOH   192 692 448 HOH   HOH A . 
F 4 HOH   193 693 330 HOH   HOH A . 
F 4 HOH   194 694 406 HOH   HOH A . 
F 4 HOH   195 695 163 HOH   HOH A . 
F 4 HOH   196 696 94  HOH   HOH A . 
F 4 HOH   197 697 224 HOH   HOH A . 
F 4 HOH   198 698 66  HOH   HOH A . 
F 4 HOH   199 699 446 HOH   HOH A . 
F 4 HOH   200 700 429 HOH   HOH A . 
F 4 HOH   201 701 295 HOH   HOH A . 
F 4 HOH   202 702 371 HOH   HOH A . 
F 4 HOH   203 703 17  HOH   HOH A . 
F 4 HOH   204 704 382 HOH   HOH A . 
F 4 HOH   205 705 305 HOH   HOH A . 
F 4 HOH   206 706 297 HOH   HOH A . 
F 4 HOH   207 707 465 HOH   HOH A . 
F 4 HOH   208 708 351 HOH   HOH A . 
F 4 HOH   209 709 411 HOH   HOH A . 
F 4 HOH   210 710 475 HOH   HOH A . 
F 4 HOH   211 711 243 HOH   HOH A . 
F 4 HOH   212 712 276 HOH   HOH A . 
F 4 HOH   213 713 449 HOH   HOH A . 
F 4 HOH   214 714 415 HOH   HOH A . 
F 4 HOH   215 715 251 HOH   HOH A . 
F 4 HOH   216 716 418 HOH   HOH A . 
F 4 HOH   217 717 250 HOH   HOH A . 
F 4 HOH   218 718 321 HOH   HOH A . 
F 4 HOH   219 719 290 HOH   HOH A . 
F 4 HOH   220 720 436 HOH   HOH A . 
F 4 HOH   221 721 369 HOH   HOH A . 
F 4 HOH   222 722 447 HOH   HOH A . 
F 4 HOH   223 723 405 HOH   HOH A . 
F 4 HOH   224 724 420 HOH   HOH A . 
F 4 HOH   225 725 339 HOH   HOH A . 
F 4 HOH   226 726 239 HOH   HOH A . 
G 4 HOH   1   501 238 HOH   HOH B . 
G 4 HOH   2   502 205 HOH   HOH B . 
G 4 HOH   3   503 285 HOH   HOH B . 
G 4 HOH   4   504 195 HOH   HOH B . 
G 4 HOH   5   505 21  HOH   HOH B . 
G 4 HOH   6   506 263 HOH   HOH B . 
G 4 HOH   7   507 126 HOH   HOH B . 
G 4 HOH   8   508 249 HOH   HOH B . 
G 4 HOH   9   509 389 HOH   HOH B . 
G 4 HOH   10  510 25  HOH   HOH B . 
G 4 HOH   11  511 255 HOH   HOH B . 
G 4 HOH   12  512 325 HOH   HOH B . 
G 4 HOH   13  513 167 HOH   HOH B . 
G 4 HOH   14  514 70  HOH   HOH B . 
G 4 HOH   15  515 397 HOH   HOH B . 
G 4 HOH   16  516 269 HOH   HOH B . 
G 4 HOH   17  517 124 HOH   HOH B . 
G 4 HOH   18  518 433 HOH   HOH B . 
G 4 HOH   19  519 69  HOH   HOH B . 
G 4 HOH   20  520 275 HOH   HOH B . 
G 4 HOH   21  521 359 HOH   HOH B . 
G 4 HOH   22  522 186 HOH   HOH B . 
G 4 HOH   23  523 33  HOH   HOH B . 
G 4 HOH   24  524 164 HOH   HOH B . 
G 4 HOH   25  525 202 HOH   HOH B . 
G 4 HOH   26  526 115 HOH   HOH B . 
G 4 HOH   27  527 417 HOH   HOH B . 
G 4 HOH   28  528 85  HOH   HOH B . 
G 4 HOH   29  529 148 HOH   HOH B . 
G 4 HOH   30  530 74  HOH   HOH B . 
G 4 HOH   31  531 218 HOH   HOH B . 
G 4 HOH   32  532 11  HOH   HOH B . 
G 4 HOH   33  533 273 HOH   HOH B . 
G 4 HOH   34  534 192 HOH   HOH B . 
G 4 HOH   35  535 302 HOH   HOH B . 
G 4 HOH   36  536 30  HOH   HOH B . 
G 4 HOH   37  537 52  HOH   HOH B . 
G 4 HOH   38  538 146 HOH   HOH B . 
G 4 HOH   39  539 246 HOH   HOH B . 
G 4 HOH   40  540 149 HOH   HOH B . 
G 4 HOH   41  541 179 HOH   HOH B . 
G 4 HOH   42  542 319 HOH   HOH B . 
G 4 HOH   43  543 235 HOH   HOH B . 
G 4 HOH   44  544 300 HOH   HOH B . 
G 4 HOH   45  545 136 HOH   HOH B . 
G 4 HOH   46  546 425 HOH   HOH B . 
G 4 HOH   47  547 6   HOH   HOH B . 
G 4 HOH   48  548 40  HOH   HOH B . 
G 4 HOH   49  549 308 HOH   HOH B . 
G 4 HOH   50  550 189 HOH   HOH B . 
G 4 HOH   51  551 41  HOH   HOH B . 
G 4 HOH   52  552 265 HOH   HOH B . 
G 4 HOH   53  553 15  HOH   HOH B . 
G 4 HOH   54  554 47  HOH   HOH B . 
G 4 HOH   55  555 232 HOH   HOH B . 
G 4 HOH   56  556 264 HOH   HOH B . 
G 4 HOH   57  557 73  HOH   HOH B . 
G 4 HOH   58  558 256 HOH   HOH B . 
G 4 HOH   59  559 386 HOH   HOH B . 
G 4 HOH   60  560 231 HOH   HOH B . 
G 4 HOH   61  561 216 HOH   HOH B . 
G 4 HOH   62  562 344 HOH   HOH B . 
G 4 HOH   63  563 116 HOH   HOH B . 
G 4 HOH   64  564 154 HOH   HOH B . 
G 4 HOH   65  565 457 HOH   HOH B . 
G 4 HOH   66  566 200 HOH   HOH B . 
G 4 HOH   67  567 128 HOH   HOH B . 
G 4 HOH   68  568 78  HOH   HOH B . 
G 4 HOH   69  569 408 HOH   HOH B . 
G 4 HOH   70  570 363 HOH   HOH B . 
G 4 HOH   71  571 445 HOH   HOH B . 
G 4 HOH   72  572 414 HOH   HOH B . 
G 4 HOH   73  573 31  HOH   HOH B . 
G 4 HOH   74  574 48  HOH   HOH B . 
G 4 HOH   75  575 107 HOH   HOH B . 
G 4 HOH   76  576 423 HOH   HOH B . 
G 4 HOH   77  577 86  HOH   HOH B . 
G 4 HOH   78  578 35  HOH   HOH B . 
G 4 HOH   79  579 42  HOH   HOH B . 
G 4 HOH   80  580 98  HOH   HOH B . 
G 4 HOH   81  581 92  HOH   HOH B . 
G 4 HOH   82  582 193 HOH   HOH B . 
G 4 HOH   83  583 342 HOH   HOH B . 
G 4 HOH   84  584 196 HOH   HOH B . 
G 4 HOH   85  585 291 HOH   HOH B . 
G 4 HOH   86  586 372 HOH   HOH B . 
G 4 HOH   87  587 109 HOH   HOH B . 
G 4 HOH   88  588 72  HOH   HOH B . 
G 4 HOH   89  589 331 HOH   HOH B . 
G 4 HOH   90  590 59  HOH   HOH B . 
G 4 HOH   91  591 102 HOH   HOH B . 
G 4 HOH   92  592 82  HOH   HOH B . 
G 4 HOH   93  593 8   HOH   HOH B . 
G 4 HOH   94  594 349 HOH   HOH B . 
G 4 HOH   95  595 355 HOH   HOH B . 
G 4 HOH   96  596 117 HOH   HOH B . 
G 4 HOH   97  597 388 HOH   HOH B . 
G 4 HOH   98  598 459 HOH   HOH B . 
G 4 HOH   99  599 162 HOH   HOH B . 
G 4 HOH   100 600 24  HOH   HOH B . 
G 4 HOH   101 601 43  HOH   HOH B . 
G 4 HOH   102 602 84  HOH   HOH B . 
G 4 HOH   103 603 350 HOH   HOH B . 
G 4 HOH   104 604 16  HOH   HOH B . 
G 4 HOH   105 605 315 HOH   HOH B . 
G 4 HOH   106 606 87  HOH   HOH B . 
G 4 HOH   107 607 10  HOH   HOH B . 
G 4 HOH   108 608 91  HOH   HOH B . 
G 4 HOH   109 609 194 HOH   HOH B . 
G 4 HOH   110 610 470 HOH   HOH B . 
G 4 HOH   111 611 267 HOH   HOH B . 
G 4 HOH   112 612 62  HOH   HOH B . 
G 4 HOH   113 613 76  HOH   HOH B . 
G 4 HOH   114 614 166 HOH   HOH B . 
G 4 HOH   115 615 431 HOH   HOH B . 
G 4 HOH   116 616 226 HOH   HOH B . 
G 4 HOH   117 617 367 HOH   HOH B . 
G 4 HOH   118 618 323 HOH   HOH B . 
G 4 HOH   119 619 173 HOH   HOH B . 
G 4 HOH   120 620 105 HOH   HOH B . 
G 4 HOH   121 621 456 HOH   HOH B . 
G 4 HOH   122 622 410 HOH   HOH B . 
G 4 HOH   123 623 67  HOH   HOH B . 
G 4 HOH   124 624 95  HOH   HOH B . 
G 4 HOH   125 625 450 HOH   HOH B . 
G 4 HOH   126 626 75  HOH   HOH B . 
G 4 HOH   127 627 29  HOH   HOH B . 
G 4 HOH   128 628 97  HOH   HOH B . 
G 4 HOH   129 629 228 HOH   HOH B . 
G 4 HOH   130 630 279 HOH   HOH B . 
G 4 HOH   131 631 284 HOH   HOH B . 
G 4 HOH   132 632 44  HOH   HOH B . 
G 4 HOH   133 633 119 HOH   HOH B . 
G 4 HOH   134 634 252 HOH   HOH B . 
G 4 HOH   135 635 161 HOH   HOH B . 
G 4 HOH   136 636 307 HOH   HOH B . 
G 4 HOH   137 637 39  HOH   HOH B . 
G 4 HOH   138 638 34  HOH   HOH B . 
G 4 HOH   139 639 281 HOH   HOH B . 
G 4 HOH   140 640 402 HOH   HOH B . 
G 4 HOH   141 641 55  HOH   HOH B . 
G 4 HOH   142 642 283 HOH   HOH B . 
G 4 HOH   143 643 254 HOH   HOH B . 
G 4 HOH   144 644 122 HOH   HOH B . 
G 4 HOH   145 645 184 HOH   HOH B . 
G 4 HOH   146 646 314 HOH   HOH B . 
G 4 HOH   147 647 96  HOH   HOH B . 
G 4 HOH   148 648 334 HOH   HOH B . 
G 4 HOH   149 649 374 HOH   HOH B . 
G 4 HOH   150 650 464 HOH   HOH B . 
G 4 HOH   151 651 201 HOH   HOH B . 
G 4 HOH   152 652 271 HOH   HOH B . 
G 4 HOH   153 653 378 HOH   HOH B . 
G 4 HOH   154 654 396 HOH   HOH B . 
G 4 HOH   155 655 463 HOH   HOH B . 
G 4 HOH   156 656 227 HOH   HOH B . 
G 4 HOH   157 657 203 HOH   HOH B . 
G 4 HOH   158 658 309 HOH   HOH B . 
G 4 HOH   159 659 101 HOH   HOH B . 
G 4 HOH   160 660 407 HOH   HOH B . 
G 4 HOH   161 661 422 HOH   HOH B . 
G 4 HOH   162 662 187 HOH   HOH B . 
G 4 HOH   163 663 18  HOH   HOH B . 
G 4 HOH   164 664 181 HOH   HOH B . 
G 4 HOH   165 665 206 HOH   HOH B . 
G 4 HOH   166 666 225 HOH   HOH B . 
G 4 HOH   167 667 185 HOH   HOH B . 
G 4 HOH   168 668 383 HOH   HOH B . 
G 4 HOH   169 669 278 HOH   HOH B . 
G 4 HOH   170 670 60  HOH   HOH B . 
G 4 HOH   171 671 306 HOH   HOH B . 
G 4 HOH   172 672 130 HOH   HOH B . 
G 4 HOH   173 673 180 HOH   HOH B . 
G 4 HOH   174 674 183 HOH   HOH B . 
G 4 HOH   175 675 391 HOH   HOH B . 
G 4 HOH   176 676 458 HOH   HOH B . 
G 4 HOH   177 677 27  HOH   HOH B . 
G 4 HOH   178 678 111 HOH   HOH B . 
G 4 HOH   179 679 301 HOH   HOH B . 
G 4 HOH   180 680 421 HOH   HOH B . 
G 4 HOH   181 681 322 HOH   HOH B . 
G 4 HOH   182 682 242 HOH   HOH B . 
G 4 HOH   183 683 366 HOH   HOH B . 
G 4 HOH   184 684 409 HOH   HOH B . 
G 4 HOH   185 685 398 HOH   HOH B . 
G 4 HOH   186 686 65  HOH   HOH B . 
G 4 HOH   187 687 361 HOH   HOH B . 
G 4 HOH   188 688 364 HOH   HOH B . 
G 4 HOH   189 689 373 HOH   HOH B . 
G 4 HOH   190 690 466 HOH   HOH B . 
G 4 HOH   191 691 90  HOH   HOH B . 
G 4 HOH   192 692 392 HOH   HOH B . 
G 4 HOH   193 693 434 HOH   HOH B . 
G 4 HOH   194 694 212 HOH   HOH B . 
G 4 HOH   195 695 426 HOH   HOH B . 
G 4 HOH   196 696 141 HOH   HOH B . 
G 4 HOH   197 697 412 HOH   HOH B . 
G 4 HOH   198 698 394 HOH   HOH B . 
G 4 HOH   199 699 453 HOH   HOH B . 
G 4 HOH   200 700 368 HOH   HOH B . 
G 4 HOH   201 701 320 HOH   HOH B . 
G 4 HOH   202 702 298 HOH   HOH B . 
G 4 HOH   203 703 356 HOH   HOH B . 
G 4 HOH   204 704 353 HOH   HOH B . 
G 4 HOH   205 705 171 HOH   HOH B . 
G 4 HOH   206 706 441 HOH   HOH B . 
G 4 HOH   207 707 352 HOH   HOH B . 
G 4 HOH   208 708 467 HOH   HOH B . 
G 4 HOH   209 709 365 HOH   HOH B . 
G 4 HOH   210 710 223 HOH   HOH B . 
G 4 HOH   211 711 241 HOH   HOH B . 
G 4 HOH   212 712 400 HOH   HOH B . 
G 4 HOH   213 713 461 HOH   HOH B . 
G 4 HOH   214 714 299 HOH   HOH B . 
G 4 HOH   215 715 347 HOH   HOH B . 
G 4 HOH   216 716 427 HOH   HOH B . 
G 4 HOH   217 717 311 HOH   HOH B . 
G 4 HOH   218 718 296 HOH   HOH B . 
G 4 HOH   219 719 381 HOH   HOH B . 
G 4 HOH   220 720 23  HOH   HOH B . 
G 4 HOH   221 721 188 HOH   HOH B . 
G 4 HOH   222 722 358 HOH   HOH B . 
G 4 HOH   223 723 393 HOH   HOH B . 
G 4 HOH   224 724 174 HOH   HOH B . 
G 4 HOH   225 725 343 HOH   HOH B . 
G 4 HOH   226 726 236 HOH   HOH B . 
G 4 HOH   227 727 444 HOH   HOH B . 
G 4 HOH   228 728 345 HOH   HOH B . 
G 4 HOH   229 729 197 HOH   HOH B . 
G 4 HOH   230 730 272 HOH   HOH B . 
G 4 HOH   231 731 452 HOH   HOH B . 
G 4 HOH   232 732 219 HOH   HOH B . 
G 4 HOH   233 733 336 HOH   HOH B . 
G 4 HOH   234 734 240 HOH   HOH B . 
G 4 HOH   235 735 385 HOH   HOH B . 
G 4 HOH   236 736 244 HOH   HOH B . 
G 4 HOH   237 737 469 HOH   HOH B . 
G 4 HOH   238 738 390 HOH   HOH B . 
G 4 HOH   239 739 234 HOH   HOH B . 
G 4 HOH   240 740 266 HOH   HOH B . 
G 4 HOH   241 741 338 HOH   HOH B . 
G 4 HOH   242 742 277 HOH   HOH B . 
G 4 HOH   243 743 155 HOH   HOH B . 
G 4 HOH   244 744 468 HOH   HOH B . 
G 4 HOH   245 745 259 HOH   HOH B . 
G 4 HOH   246 746 472 HOH   HOH B . 
G 4 HOH   247 747 337 HOH   HOH B . 
G 4 HOH   248 748 316 HOH   HOH B . 
G 4 HOH   249 749 170 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 74  ? CG  ? A GLU 62  CG  
2  1 Y 1 A GLU 74  ? CD  ? A GLU 62  CD  
3  1 Y 1 A GLU 74  ? OE1 ? A GLU 62  OE1 
4  1 Y 1 A GLU 74  ? OE2 ? A GLU 62  OE2 
5  1 Y 1 A ARG 112 ? CG  ? A ARG 100 CG  
6  1 Y 1 A ARG 112 ? CD  ? A ARG 100 CD  
7  1 Y 1 A ARG 112 ? NE  ? A ARG 100 NE  
8  1 Y 1 A ARG 112 ? CZ  ? A ARG 100 CZ  
9  1 Y 1 A ARG 112 ? NH1 ? A ARG 100 NH1 
10 1 Y 1 A ARG 112 ? NH2 ? A ARG 100 NH2 
11 1 Y 1 B LYS 117 ? CG  ? B LYS 105 CG  
12 1 Y 1 B LYS 117 ? CD  ? B LYS 105 CD  
13 1 Y 1 B LYS 117 ? CE  ? B LYS 105 CE  
14 1 Y 1 B LYS 117 ? NZ  ? B LYS 105 NZ  
15 1 Y 1 B TRP 183 ? CG  ? B TRP 171 CG  
16 1 Y 1 B TRP 183 ? CD1 ? B TRP 171 CD1 
17 1 Y 1 B TRP 183 ? CD2 ? B TRP 171 CD2 
18 1 Y 1 B TRP 183 ? NE1 ? B TRP 171 NE1 
19 1 Y 1 B TRP 183 ? CE2 ? B TRP 171 CE2 
20 1 Y 1 B TRP 183 ? CE3 ? B TRP 171 CE3 
21 1 Y 1 B TRP 183 ? CZ2 ? B TRP 171 CZ2 
22 1 Y 1 B TRP 183 ? CZ3 ? B TRP 171 CZ3 
23 1 Y 1 B TRP 183 ? CH2 ? B TRP 171 CH2 
24 1 Y 1 B ASN 184 ? CG  ? B ASN 172 CG  
25 1 Y 1 B ASN 184 ? OD1 ? B ASN 172 OD1 
26 1 Y 1 B ASN 184 ? ND2 ? B ASN 172 ND2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21_5207 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .         2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .         4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.44 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BCA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     44.528 
_cell.length_a_esd                 ? 
_cell.length_b                     87.933 
_cell.length_b_esd                 ? 
_cell.length_c                     89.241 
_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                         9BCA 
_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                   9BCA 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.18 
_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    '13-18% PEG3350, 0.2M NaSCN, 0.1 M Bis-Tris Propane, pH = 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-30 
_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   0.92010 
_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                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.92010 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BCA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.7 
_reflns.d_resolution_low                               50.0 
_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                                     72950 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.55 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.992 
_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                                    1.70 
_reflns_shell.d_res_low                                     1.76 
_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                             7280 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.873 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_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                                 9BCA 
_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                            1.70 
_refine.ls_d_res_low                             39.19 
_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                     72817 
_refine.ls_number_reflns_R_free                  3551 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.61 
_refine.ls_percent_reflns_R_free                 4.88 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2323 
_refine.ls_R_factor_R_free                       0.2739 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2302 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.39 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 27.33 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.26 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        5212 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         53 
_refine_hist.number_atoms_solvent             475 
_refine_hist.number_atoms_total               5740 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        39.19 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 5448 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.847  ? 7419 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.384 ? 1888 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055  ? 745  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 954  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.70 1.72  . . 143 2634 96.00  . . . . 0.3182 . . . . . . . . . . . 0.3458 
'X-RAY DIFFRACTION' 1.72 1.75  . . 147 2752 99.00  . . . . 0.2962 . . . . . . . . . . . 0.3749 
'X-RAY DIFFRACTION' 1.75 1.77  . . 128 2765 99.00  . . . . 0.2879 . . . . . . . . . . . 0.2864 
'X-RAY DIFFRACTION' 1.77 1.80  . . 138 2727 99.00  . . . . 0.2704 . . . . . . . . . . . 0.3354 
'X-RAY DIFFRACTION' 1.80 1.83  . . 141 2795 100.00 . . . . 0.2631 . . . . . . . . . . . 0.3373 
'X-RAY DIFFRACTION' 1.83 1.86  . . 158 2766 100.00 . . . . 0.2531 . . . . . . . . . . . 0.2763 
'X-RAY DIFFRACTION' 1.86 1.90  . . 145 2749 99.00  . . . . 0.2486 . . . . . . . . . . . 0.3083 
'X-RAY DIFFRACTION' 1.90 1.93  . . 164 2748 100.00 . . . . 0.2342 . . . . . . . . . . . 0.3070 
'X-RAY DIFFRACTION' 1.93 1.97  . . 125 2764 100.00 . . . . 0.2360 . . . . . . . . . . . 0.2644 
'X-RAY DIFFRACTION' 1.97 2.02  . . 121 2807 100.00 . . . . 0.2346 . . . . . . . . . . . 0.2490 
'X-RAY DIFFRACTION' 2.02 2.06  . . 159 2724 100.00 . . . . 0.2326 . . . . . . . . . . . 0.2511 
'X-RAY DIFFRACTION' 2.06 2.11  . . 158 2775 100.00 . . . . 0.2291 . . . . . . . . . . . 0.2751 
'X-RAY DIFFRACTION' 2.11 2.17  . . 175 2689 100.00 . . . . 0.2269 . . . . . . . . . . . 0.2876 
'X-RAY DIFFRACTION' 2.17 2.24  . . 159 2819 100.00 . . . . 0.2295 . . . . . . . . . . . 0.2568 
'X-RAY DIFFRACTION' 2.24 2.31  . . 185 2710 100.00 . . . . 0.2268 . . . . . . . . . . . 0.2997 
'X-RAY DIFFRACTION' 2.31 2.39  . . 129 2770 100.00 . . . . 0.2361 . . . . . . . . . . . 0.2974 
'X-RAY DIFFRACTION' 2.39 2.49  . . 140 2815 100.00 . . . . 0.2487 . . . . . . . . . . . 0.3184 
'X-RAY DIFFRACTION' 2.49 2.60  . . 114 2805 100.00 . . . . 0.2413 . . . . . . . . . . . 0.3013 
'X-RAY DIFFRACTION' 2.60 2.74  . . 142 2774 100.00 . . . . 0.2417 . . . . . . . . . . . 0.2854 
'X-RAY DIFFRACTION' 2.74 2.91  . . 117 2785 100.00 . . . . 0.2381 . . . . . . . . . . . 0.2798 
'X-RAY DIFFRACTION' 2.91 3.13  . . 136 2826 100.00 . . . . 0.2269 . . . . . . . . . . . 0.2832 
'X-RAY DIFFRACTION' 3.13 3.45  . . 141 2763 100.00 . . . . 0.2303 . . . . . . . . . . . 0.2700 
'X-RAY DIFFRACTION' 3.45 3.94  . . 138 2798 100.00 . . . . 0.2144 . . . . . . . . . . . 0.2635 
'X-RAY DIFFRACTION' 3.95 4.97  . . 112 2867 100.00 . . . . 0.1999 . . . . . . . . . . . 0.2570 
'X-RAY DIFFRACTION' 4.97 39.19 . . 136 2839 100.00 . . . . 0.2144 . . . . . . . . . . . 0.2037 
# 
_struct.entry_id                     9BCA 
_struct.title                        'Structure of KLHDC2 bound to SJ46411' 
_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        9BCA 
_struct_keywords.text            'Kelch domain, inhibitor, complex, KLHDC2, LIGASE, LIGASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   LIGASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    KLDC2_HUMAN 
_struct_ref.pdbx_db_accession          Q9Y2U9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GPAFESYESMELACPAERSGHVAVSDGRHMFVWGGYKSNQVRGLYDFYLPREELWIYNMETGRWKKINTEGDVPPSMSGS
CAVCVDRVLYLFGGHHSRGNTNKFYMLDSRSTDRVLQWERIDCQGIPPSSKDKLGVWVYKNKLIFFGGYGYLPEDKVLGT
FEFDETSFWNSSHPRGWNDHVHILDTETFTWSQPITTGKAPSPRAAHACATVGNRGFVFGGRYRDARMNDLHYLNLDTWE
WNELIPQGICPVGRSWHSLTPVSSDHLFLFGGFTTDKQPLSDAWTYCISKNEWIQFNHPYTEKPRLWHTACASDEGEVIV
FGGCANNLLVHHRAAHSNEILIFSVQP
;
_struct_ref.pdbx_align_begin           15 
# 
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 9BCA A 3 ? 349 ? Q9Y2U9 15 ? 361 ? 15 361 
2 1 9BCA B 3 ? 349 ? Q9Y2U9 15 ? 361 ? 15 361 
# 
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 9BCA GLY A 1 ? UNP Q9Y2U9 ? ? 'expression tag' 13 1 
1 9BCA SER A 2 ? UNP Q9Y2U9 ? ? 'expression tag' 14 2 
2 9BCA GLY B 1 ? UNP Q9Y2U9 ? ? 'expression tag' 13 3 
2 9BCA SER B 2 ? UNP Q9Y2U9 ? ? 'expression tag' 14 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,F 
2 1 B,E,G   
# 
_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 GLU A 167 ? PHE A 170 ? GLU A 179 PHE A 182 5 ? 4 
HELX_P HELX_P2 AA2 VAL A 332 ? ALA A 336 ? VAL A 344 ALA A 348 5 ? 5 
HELX_P HELX_P3 AA3 GLU B 167 ? ASN B 172 ? GLU B 179 ASN B 184 1 ? 6 
HELX_P HELX_P4 AA4 VAL B 332 ? ALA B 336 ? VAL B 344 ALA B 348 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 4 ? 
AA9 ? 3 ? 
AB1 ? 4 ? 
AB2 ? 5 ? 
AB3 ? 2 ? 
AB4 ? 4 ? 
AB5 ? 4 ? 
AB6 ? 4 ? 
AB7 ? 2 ? 
AB8 ? 4 ? 
AB9 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 24  ? SER A 27  ? VAL A 36  SER A 39  
AA1 2 HIS A 31  ? TRP A 35  ? HIS A 43  TRP A 47  
AA1 3 GLU A 55  ? ASN A 60  ? GLU A 67  ASN A 72  
AA1 4 TRP A 66  ? ASN A 70  ? TRP A 78  ASN A 82  
AA2 1 GLU A 72  ? GLY A 73  ? GLU A 84  GLY A 85  
AA2 2 GLN A 119 ? ARG A 122 ? GLN A 131 ARG A 134 
AA2 3 PHE A 106 ? ASP A 110 ? PHE A 118 ASP A 122 
AA2 4 VAL A 90  ? PHE A 94  ? VAL A 102 PHE A 106 
AA2 5 CYS A 83  ? VAL A 87  ? CYS A 95  VAL A 99  
AA3 1 HIS A 97  ? HIS A 98  ? HIS A 109 HIS A 110 
AA3 2 GLY A 101 ? ASN A 102 ? GLY A 113 ASN A 114 
AA4 1 LYS A 133 ? ASP A 134 ? LYS A 145 ASP A 146 
AA4 2 LYS A 144 ? GLY A 152 ? LYS A 156 GLY A 164 
AA4 3 GLY A 178 ? ASP A 187 ? GLY A 190 ASP A 199 
AA4 4 PHE A 163 ? PHE A 165 ? PHE A 175 PHE A 177 
AA5 1 GLY A 137 ? TYR A 141 ? GLY A 149 TYR A 153 
AA5 2 LYS A 144 ? GLY A 152 ? LYS A 156 GLY A 164 
AA5 3 GLY A 178 ? ASP A 187 ? GLY A 190 ASP A 199 
AA5 4 THR A 192 ? SER A 194 ? THR A 204 SER A 206 
AA6 1 ALA A 210 ? VAL A 214 ? ALA A 222 VAL A 226 
AA6 2 ARG A 217 ? PHE A 221 ? ARG A 229 PHE A 233 
AA6 3 LEU A 233 ? ASN A 237 ? LEU A 245 ASN A 249 
AA6 4 TRP A 243 ? LEU A 246 ? TRP A 255 LEU A 258 
AA7 1 ARG A 224 ? TYR A 225 ? ARG A 236 TYR A 237 
AA7 2 ALA A 228 ? ARG A 229 ? ALA A 240 ARG A 241 
AA8 1 SER A 260 ? SER A 265 ? SER A 272 SER A 277 
AA8 2 HIS A 268 ? PHE A 272 ? HIS A 280 PHE A 284 
AA8 3 ALA A 285 ? CYS A 289 ? ALA A 297 CYS A 301 
AA8 4 GLU A 294 ? GLN A 297 ? GLU A 306 GLN A 309 
AA9 1 THR A 311 ? ALA A 314 ? THR A 323 ALA A 326 
AA9 2 GLU A 319 ? PHE A 323 ? GLU A 331 PHE A 335 
AA9 3 ILE A 342 ? SER A 346 ? ILE A 354 SER A 358 
AB1 1 VAL B 24  ? SER B 27  ? VAL B 36  SER B 39  
AB1 2 HIS B 31  ? TRP B 35  ? HIS B 43  TRP B 47  
AB1 3 GLU B 55  ? ASN B 60  ? GLU B 67  ASN B 72  
AB1 4 TRP B 66  ? ASN B 70  ? TRP B 78  ASN B 82  
AB2 1 GLU B 72  ? GLY B 73  ? GLU B 84  GLY B 85  
AB2 2 GLN B 119 ? ARG B 122 ? GLN B 131 ARG B 134 
AB2 3 PHE B 106 ? ASP B 110 ? PHE B 118 ASP B 122 
AB2 4 VAL B 90  ? PHE B 94  ? VAL B 102 PHE B 106 
AB2 5 CYS B 83  ? VAL B 87  ? CYS B 95  VAL B 99  
AB3 1 HIS B 97  ? HIS B 98  ? HIS B 109 HIS B 110 
AB3 2 GLY B 101 ? ASN B 102 ? GLY B 113 ASN B 114 
AB4 1 LYS B 133 ? ASP B 134 ? LYS B 145 ASP B 146 
AB4 2 LYS B 144 ? GLY B 152 ? LYS B 156 GLY B 164 
AB4 3 GLY B 178 ? ASP B 187 ? GLY B 190 ASP B 199 
AB4 4 PHE B 163 ? PHE B 165 ? PHE B 175 PHE B 177 
AB5 1 GLY B 137 ? TYR B 141 ? GLY B 149 TYR B 153 
AB5 2 LYS B 144 ? GLY B 152 ? LYS B 156 GLY B 164 
AB5 3 GLY B 178 ? ASP B 187 ? GLY B 190 ASP B 199 
AB5 4 TRP B 193 ? SER B 194 ? TRP B 205 SER B 206 
AB6 1 ALA B 210 ? VAL B 214 ? ALA B 222 VAL B 226 
AB6 2 ARG B 217 ? PHE B 221 ? ARG B 229 PHE B 233 
AB6 3 LEU B 233 ? ASN B 237 ? LEU B 245 ASN B 249 
AB6 4 TRP B 243 ? LEU B 246 ? TRP B 255 LEU B 258 
AB7 1 ARG B 224 ? TYR B 225 ? ARG B 236 TYR B 237 
AB7 2 ALA B 228 ? ARG B 229 ? ALA B 240 ARG B 241 
AB8 1 SER B 260 ? PRO B 263 ? SER B 272 PRO B 275 
AB8 2 HIS B 268 ? PHE B 275 ? HIS B 280 PHE B 287 
AB8 3 PRO B 281 ? CYS B 289 ? PRO B 293 CYS B 301 
AB8 4 GLU B 294 ? PHE B 298 ? GLU B 306 PHE B 310 
AB9 1 THR B 311 ? ALA B 314 ? THR B 323 ALA B 326 
AB9 2 GLU B 319 ? PHE B 323 ? GLU B 331 PHE B 335 
AB9 3 ILE B 342 ? SER B 346 ? ILE B 354 SER B 358 
# 
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 VAL A 26  ? N VAL A 38  O PHE A 33  ? O PHE A 45  
AA1 2 3 N VAL A 34  ? N VAL A 46  O TRP A 57  ? O TRP A 69  
AA1 3 4 N ILE A 58  ? N ILE A 70  O LYS A 67  ? O LYS A 79  
AA2 1 2 N GLU A 72  ? N GLU A 84  O TRP A 120 ? O TRP A 132 
AA2 2 3 O GLU A 121 ? O GLU A 133 N MET A 108 ? N MET A 120 
AA2 3 4 O LEU A 109 ? O LEU A 121 N LEU A 91  ? N LEU A 103 
AA2 4 5 O PHE A 94  ? O PHE A 106 N CYS A 83  ? N CYS A 95  
AA3 1 2 N HIS A 98  ? N HIS A 110 O GLY A 101 ? O GLY A 113 
AA4 1 2 N ASP A 134 ? N ASP A 146 O TYR A 151 ? O TYR A 163 
AA4 2 3 N LEU A 145 ? N LEU A 157 O LEU A 186 ? O LEU A 198 
AA4 3 4 O TRP A 179 ? O TRP A 191 N GLU A 164 ? N GLU A 176 
AA5 1 2 N TRP A 139 ? N TRP A 151 O ILE A 146 ? O ILE A 158 
AA5 2 3 N LEU A 145 ? N LEU A 157 O LEU A 186 ? O LEU A 198 
AA5 3 4 N ILE A 185 ? N ILE A 197 O SER A 194 ? O SER A 206 
AA6 1 2 N ALA A 212 ? N ALA A 224 O PHE A 219 ? O PHE A 231 
AA6 2 3 N GLY A 218 ? N GLY A 230 O LEU A 236 ? O LEU A 248 
AA6 3 4 N TYR A 235 ? N TYR A 247 O ASN A 244 ? O ASN A 256 
AA7 1 2 N TYR A 225 ? N TYR A 237 O ALA A 228 ? O ALA A 240 
AA8 1 2 N THR A 262 ? N THR A 274 O PHE A 270 ? O PHE A 282 
AA8 2 3 N LEU A 269 ? N LEU A 281 O TYR A 288 ? O TYR A 300 
AA8 3 4 N CYS A 289 ? N CYS A 301 O GLU A 294 ? O GLU A 306 
AA9 1 2 N CYS A 313 ? N CYS A 325 O ILE A 321 ? O ILE A 333 
AA9 2 3 N VAL A 322 ? N VAL A 334 O LEU A 343 ? O LEU A 355 
AB1 1 2 N VAL B 26  ? N VAL B 38  O PHE B 33  ? O PHE B 45  
AB1 2 3 N VAL B 34  ? N VAL B 46  O TRP B 57  ? O TRP B 69  
AB1 3 4 N ILE B 58  ? N ILE B 70  O LYS B 67  ? O LYS B 79  
AB2 1 2 N GLU B 72  ? N GLU B 84  O TRP B 120 ? O TRP B 132 
AB2 2 3 O GLU B 121 ? O GLU B 133 N MET B 108 ? N MET B 120 
AB2 3 4 O LEU B 109 ? O LEU B 121 N LEU B 91  ? N LEU B 103 
AB2 4 5 O VAL B 90  ? O VAL B 102 N VAL B 87  ? N VAL B 99  
AB3 1 2 N HIS B 98  ? N HIS B 110 O GLY B 101 ? O GLY B 113 
AB4 1 2 N ASP B 134 ? N ASP B 146 O TYR B 151 ? O TYR B 163 
AB4 2 3 N LEU B 145 ? N LEU B 157 O LEU B 186 ? O LEU B 198 
AB4 3 4 O TRP B 179 ? O TRP B 191 N GLU B 164 ? N GLU B 176 
AB5 1 2 N TRP B 139 ? N TRP B 151 O ILE B 146 ? O ILE B 158 
AB5 2 3 N LEU B 145 ? N LEU B 157 O LEU B 186 ? O LEU B 198 
AB5 3 4 N ILE B 185 ? N ILE B 197 O SER B 194 ? O SER B 206 
AB6 1 2 N ALA B 212 ? N ALA B 224 O PHE B 219 ? O PHE B 231 
AB6 2 3 N GLY B 218 ? N GLY B 230 O LEU B 236 ? O LEU B 248 
AB6 3 4 N LEU B 233 ? N LEU B 245 O LEU B 246 ? O LEU B 258 
AB7 1 2 N TYR B 225 ? N TYR B 237 O ALA B 228 ? O ALA B 240 
AB8 1 2 N THR B 262 ? N THR B 274 O PHE B 270 ? O PHE B 282 
AB8 2 3 N LEU B 271 ? N LEU B 283 O TRP B 286 ? O TRP B 298 
AB8 3 4 N CYS B 289 ? N CYS B 301 O GLU B 294 ? O GLU B 306 
AB9 1 2 N CYS B 313 ? N CYS B 325 O ILE B 321 ? O ILE B 333 
AB9 2 3 N VAL B 322 ? N VAL B 334 O LEU B 343 ? O LEU B 355 
# 
_pdbx_entry_details.entry_id                   9BCA 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 84  ? ? -125.51 -169.21 
2  1 ARG A 101 ? ? 57.46   17.57   
3  1 LEU A 148 ? ? -122.71 -164.61 
4  1 LYS A 154 ? ? 55.95   -126.27 
5  1 ARG A 238 ? ? 55.69   -119.54 
6  1 SER A 278 ? ? -67.70  2.39    
7  1 LEU B 148 ? ? -118.35 -163.18 
8  1 LYS B 154 ? ? 55.42   -129.37 
9  1 ARG B 238 ? ? 59.36   -123.94 
10 1 SER B 277 ? ? -171.87 -179.44 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 9.8766  -4.3411  12.9619  0.1274 ? -0.0379 ? 0.0239  ? 0.1362 ? -0.0451 ? 0.1185 ? 0.4460 ? 
-0.0284 ? 0.1447  ? 0.2347 ? 0.0980  ? 0.2637 ? -0.0256 ? 0.2492  ? -0.0415 ? -0.0023 ? -0.0066 ? 0.0347  ? 0.0330  ? -0.1137 ? 
0.0180  ? 
2 'X-RAY DIFFRACTION' ? refined 13.8881 14.7307  18.9569  0.1310 ? -0.0057 ? -0.0036 ? 0.1102 ? 0.0384  ? 0.1757 ? 0.2323 ? 0.0156 
? 0.2144  ? 0.0131 ? -0.0324 ? 0.2482 ? -0.1133 ? -0.0294 ? 0.1033  ? 0.0466  ? 0.0804  ? 0.0082  ? -0.1338 ? -0.0525 ? -0.0266 ? 
3 'X-RAY DIFFRACTION' ? refined 15.3686 1.8868   30.6298  0.1232 ? 0.0115  ? 0.0128  ? 0.1378 ? 0.0312  ? 0.1224 ? 0.5904 ? 0.1253 
? 0.3403  ? 0.5897 ? -0.0596 ? 0.6462 ? -0.0938 ? -0.2041 ? -0.0650 ? 0.1068  ? 0.0620  ? -0.0185 ? -0.0273 ? -0.0633 ? -0.0003 ? 
4 'X-RAY DIFFRACTION' ? refined 14.1713 15.5473  -13.9360 0.1984 ? 0.0340  ? -0.0323 ? 0.1250 ? -0.0421 ? 0.1797 ? 0.1366 ? 0.1952 
? -0.1468 ? 0.2846 ? -0.2459 ? 0.2121 ? -0.0309 ? -0.0915 ? -0.0204 ? 0.0923  ? -0.0263 ? -0.0319 ? -0.2875 ? 0.0762  ? -0.0630 ? 
5 'X-RAY DIFFRACTION' ? refined 6.6283  -0.9616  -13.2120 0.1299 ? 0.0442  ? -0.0110 ? 0.1936 ? 0.0066  ? 0.1363 ? 0.4683 ? 0.1295 
? -0.2421 ? 0.1504 ? -0.1217 ? 0.5025 ? -0.1178 ? -0.2489 ? 0.0061  ? 0.0438  ? 0.0427  ? 0.0252  ? 0.0323  ? -0.1499 ? -0.1972 ? 
6 'X-RAY DIFFRACTION' ? refined 21.8284 -13.6958 -15.9251 0.1642 ? 0.0603  ? 0.0054  ? 0.1133 ? 0.0121  ? 0.2437 ? 0.1295 ? 0.0562 
? -0.0609 ? 0.0299 ? -0.0286 ? 0.0332 ? -0.0922 ? -0.0296 ? -0.1048 ? 0.0208  ? 0.0871  ? -0.1319 ? 0.1090  ? 0.0414  ? 0.0012  ? 
7 'X-RAY DIFFRACTION' ? refined 14.4495 1.0113   -30.5514 0.1305 ? -0.0203 ? -0.0113 ? 0.1289 ? 0.0131  ? 0.1152 ? 0.4597 ? 0.0119 
? -0.1724 ? 0.3863 ? -0.0830 ? 0.4861 ? -0.0866 ? 0.1562  ? 0.0293  ? -0.0520 ? 0.0566  ? -0.0143 ? -0.0131 ? -0.0389 ? -0.0000 ? 
8 'X-RAY DIFFRACTION' ? refined 23.6873 13.5656  -23.0456 0.1631 ? -0.0691 ? 0.0343  ? 0.0471 ? -0.0256 ? 0.2236 ? 0.4489 ? 
-0.1109 ? -0.6302 ? 0.0291 ? 0.1531  ? 0.8745 ? -0.0145 ? -0.1584 ? 0.0131  ? 0.0461  ? 0.0676  ? -0.2281 ? -0.0174 ? 0.3615  ? 
0.0662  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 26 through 148 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 149 through 189 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 190 through 360 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 26 through 82 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 83 through 174 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 175 through 194 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 195 through 344 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 345 through 360 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 723 ? 5.85 . 
2 1 O ? A HOH 724 ? 6.23 . 
3 1 O ? A HOH 725 ? 6.26 . 
4 1 O ? A HOH 726 ? 7.49 . 
5 1 O ? B HOH 748 ? 6.16 . 
6 1 O ? B HOH 749 ? 6.72 . 
# 
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 GLY 13  ? A GLY 1   
2  1 Y 1 A SER 14  ? A SER 2   
3  1 Y 1 A GLY 15  ? A GLY 3   
4  1 Y 1 A PRO 16  ? A PRO 4   
5  1 Y 1 A ALA 17  ? A ALA 5   
6  1 Y 1 A PHE 18  ? A PHE 6   
7  1 Y 1 A GLU 19  ? A GLU 7   
8  1 Y 1 A SER 20  ? A SER 8   
9  1 Y 1 A TYR 21  ? A TYR 9   
10 1 Y 1 A GLU 22  ? A GLU 10  
11 1 Y 1 A SER 23  ? A SER 11  
12 1 Y 1 A MET 24  ? A MET 12  
13 1 Y 1 A GLU 25  ? A GLU 13  
14 1 Y 1 A GLN 54  ? A GLN 42  
15 1 Y 1 A VAL 55  ? A VAL 43  
16 1 Y 1 A ARG 56  ? A ARG 44  
17 1 Y 1 A GLY 57  ? A GLY 45  
18 1 Y 1 A LEU 58  ? A LEU 46  
19 1 Y 1 A TYR 59  ? A TYR 47  
20 1 Y 1 A ASP 60  ? A ASP 48  
21 1 Y 1 A THR 126 ? A THR 114 
22 1 Y 1 A ASP 127 ? A ASP 115 
23 1 Y 1 A ARG 128 ? A ARG 116 
24 1 Y 1 A PRO 361 ? A PRO 349 
25 1 Y 1 B GLY 13  ? B GLY 1   
26 1 Y 1 B SER 14  ? B SER 2   
27 1 Y 1 B GLY 15  ? B GLY 3   
28 1 Y 1 B PRO 16  ? B PRO 4   
29 1 Y 1 B ALA 17  ? B ALA 5   
30 1 Y 1 B PHE 18  ? B PHE 6   
31 1 Y 1 B GLU 19  ? B GLU 7   
32 1 Y 1 B SER 20  ? B SER 8   
33 1 Y 1 B TYR 21  ? B TYR 9   
34 1 Y 1 B GLU 22  ? B GLU 10  
35 1 Y 1 B SER 23  ? B SER 11  
36 1 Y 1 B MET 24  ? B MET 12  
37 1 Y 1 B GLU 25  ? B GLU 13  
38 1 Y 1 B GLN 54  ? B GLN 42  
39 1 Y 1 B VAL 55  ? B VAL 43  
40 1 Y 1 B ARG 56  ? B ARG 44  
41 1 Y 1 B GLY 57  ? B GLY 45  
42 1 Y 1 B LEU 58  ? B LEU 46  
43 1 Y 1 B TYR 59  ? B TYR 47  
44 1 Y 1 B ASP 60  ? B ASP 48  
45 1 Y 1 B THR 126 ? B THR 114 
46 1 Y 1 B ASP 127 ? B ASP 115 
47 1 Y 1 B ARG 128 ? B ARG 116 
48 1 Y 1 B PRO 361 ? B PRO 349 
# 
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 
A1APS C10  C  Y N 1   
A1APS C13  C  Y N 2   
A1APS C15  C  Y N 3   
A1APS C17  C  Y N 4   
A1APS C20  C  Y N 5   
A1APS C21  C  Y N 6   
A1APS C22  C  Y N 7   
A1APS C02  C  N N 8   
A1APS C04  C  N N 9   
A1APS C05  C  N N 10  
A1APS C08  C  N N 11  
A1APS C09  C  Y N 12  
A1APS C12  C  Y N 13  
A1APS C14  C  Y N 14  
A1APS C16  C  Y N 15  
A1APS C18  C  Y N 16  
A1APS C19  C  Y N 17  
A1APS N03  N  N N 18  
A1APS N23  N  Y N 19  
A1APS O01  O  N N 20  
A1APS O06  O  N N 21  
A1APS O07  O  N N 22  
A1APS S11  S  Y N 23  
A1APS H1   H  N N 24  
A1APS H2   H  N N 25  
A1APS H3   H  N N 26  
A1APS H4   H  N N 27  
A1APS H5   H  N N 28  
A1APS H6   H  N N 29  
A1APS H7   H  N N 30  
A1APS H8   H  N N 31  
A1APS H9   H  N N 32  
A1APS H10  H  N N 33  
A1APS H11  H  N N 34  
A1APS H12  H  N N 35  
A1APS H13  H  N N 36  
A1APS H14  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
GLN   N    N  N N 125 
GLN   CA   C  N S 126 
GLN   C    C  N N 127 
GLN   O    O  N N 128 
GLN   CB   C  N N 129 
GLN   CG   C  N N 130 
GLN   CD   C  N N 131 
GLN   OE1  O  N N 132 
GLN   NE2  N  N N 133 
GLN   OXT  O  N N 134 
GLN   H    H  N N 135 
GLN   H2   H  N N 136 
GLN   HA   H  N N 137 
GLN   HB2  H  N N 138 
GLN   HB3  H  N N 139 
GLN   HG2  H  N N 140 
GLN   HG3  H  N N 141 
GLN   HE21 H  N N 142 
GLN   HE22 H  N N 143 
GLN   HXT  H  N N 144 
GLU   N    N  N N 145 
GLU   CA   C  N S 146 
GLU   C    C  N N 147 
GLU   O    O  N N 148 
GLU   CB   C  N N 149 
GLU   CG   C  N N 150 
GLU   CD   C  N N 151 
GLU   OE1  O  N N 152 
GLU   OE2  O  N N 153 
GLU   OXT  O  N N 154 
GLU   H    H  N N 155 
GLU   H2   H  N N 156 
GLU   HA   H  N N 157 
GLU   HB2  H  N N 158 
GLU   HB3  H  N N 159 
GLU   HG2  H  N N 160 
GLU   HG3  H  N N 161 
GLU   HE2  H  N N 162 
GLU   HXT  H  N N 163 
GLY   N    N  N N 164 
GLY   CA   C  N N 165 
GLY   C    C  N N 166 
GLY   O    O  N N 167 
GLY   OXT  O  N N 168 
GLY   H    H  N N 169 
GLY   H2   H  N N 170 
GLY   HA2  H  N N 171 
GLY   HA3  H  N N 172 
GLY   HXT  H  N N 173 
HIS   N    N  N N 174 
HIS   CA   C  N S 175 
HIS   C    C  N N 176 
HIS   O    O  N N 177 
HIS   CB   C  N N 178 
HIS   CG   C  Y N 179 
HIS   ND1  N  Y N 180 
HIS   CD2  C  Y N 181 
HIS   CE1  C  Y N 182 
HIS   NE2  N  Y N 183 
HIS   OXT  O  N N 184 
HIS   H    H  N N 185 
HIS   H2   H  N N 186 
HIS   HA   H  N N 187 
HIS   HB2  H  N N 188 
HIS   HB3  H  N N 189 
HIS   HD1  H  N N 190 
HIS   HD2  H  N N 191 
HIS   HE1  H  N N 192 
HIS   HE2  H  N N 193 
HIS   HXT  H  N N 194 
HOH   O    O  N N 195 
HOH   H1   H  N N 196 
HOH   H2   H  N N 197 
ILE   N    N  N N 198 
ILE   CA   C  N S 199 
ILE   C    C  N N 200 
ILE   O    O  N N 201 
ILE   CB   C  N S 202 
ILE   CG1  C  N N 203 
ILE   CG2  C  N N 204 
ILE   CD1  C  N N 205 
ILE   OXT  O  N N 206 
ILE   H    H  N N 207 
ILE   H2   H  N N 208 
ILE   HA   H  N N 209 
ILE   HB   H  N N 210 
ILE   HG12 H  N N 211 
ILE   HG13 H  N N 212 
ILE   HG21 H  N N 213 
ILE   HG22 H  N N 214 
ILE   HG23 H  N N 215 
ILE   HD11 H  N N 216 
ILE   HD12 H  N N 217 
ILE   HD13 H  N N 218 
ILE   HXT  H  N N 219 
LEU   N    N  N N 220 
LEU   CA   C  N S 221 
LEU   C    C  N N 222 
LEU   O    O  N N 223 
LEU   CB   C  N N 224 
LEU   CG   C  N N 225 
LEU   CD1  C  N N 226 
LEU   CD2  C  N N 227 
LEU   OXT  O  N N 228 
LEU   H    H  N N 229 
LEU   H2   H  N N 230 
LEU   HA   H  N N 231 
LEU   HB2  H  N N 232 
LEU   HB3  H  N N 233 
LEU   HG   H  N N 234 
LEU   HD11 H  N N 235 
LEU   HD12 H  N N 236 
LEU   HD13 H  N N 237 
LEU   HD21 H  N N 238 
LEU   HD22 H  N N 239 
LEU   HD23 H  N N 240 
LEU   HXT  H  N N 241 
LYS   N    N  N N 242 
LYS   CA   C  N S 243 
LYS   C    C  N N 244 
LYS   O    O  N N 245 
LYS   CB   C  N N 246 
LYS   CG   C  N N 247 
LYS   CD   C  N N 248 
LYS   CE   C  N N 249 
LYS   NZ   N  N N 250 
LYS   OXT  O  N N 251 
LYS   H    H  N N 252 
LYS   H2   H  N N 253 
LYS   HA   H  N N 254 
LYS   HB2  H  N N 255 
LYS   HB3  H  N N 256 
LYS   HG2  H  N N 257 
LYS   HG3  H  N N 258 
LYS   HD2  H  N N 259 
LYS   HD3  H  N N 260 
LYS   HE2  H  N N 261 
LYS   HE3  H  N N 262 
LYS   HZ1  H  N N 263 
LYS   HZ2  H  N N 264 
LYS   HZ3  H  N N 265 
LYS   HXT  H  N N 266 
MET   N    N  N N 267 
MET   CA   C  N S 268 
MET   C    C  N N 269 
MET   O    O  N N 270 
MET   CB   C  N N 271 
MET   CG   C  N N 272 
MET   SD   S  N N 273 
MET   CE   C  N N 274 
MET   OXT  O  N N 275 
MET   H    H  N N 276 
MET   H2   H  N N 277 
MET   HA   H  N N 278 
MET   HB2  H  N N 279 
MET   HB3  H  N N 280 
MET   HG2  H  N N 281 
MET   HG3  H  N N 282 
MET   HE1  H  N N 283 
MET   HE2  H  N N 284 
MET   HE3  H  N N 285 
MET   HXT  H  N N 286 
NCO   CO   CO N N 287 
NCO   N1   N  N N 288 
NCO   N2   N  N N 289 
NCO   N3   N  N N 290 
NCO   N4   N  N N 291 
NCO   N5   N  N N 292 
NCO   N6   N  N N 293 
NCO   HN11 H  N N 294 
NCO   HN12 H  N N 295 
NCO   HN13 H  N N 296 
NCO   HN21 H  N N 297 
NCO   HN22 H  N N 298 
NCO   HN23 H  N N 299 
NCO   HN31 H  N N 300 
NCO   HN32 H  N N 301 
NCO   HN33 H  N N 302 
NCO   HN41 H  N N 303 
NCO   HN42 H  N N 304 
NCO   HN43 H  N N 305 
NCO   HN51 H  N N 306 
NCO   HN52 H  N N 307 
NCO   HN53 H  N N 308 
NCO   HN61 H  N N 309 
NCO   HN62 H  N N 310 
NCO   HN63 H  N N 311 
PHE   N    N  N N 312 
PHE   CA   C  N S 313 
PHE   C    C  N N 314 
PHE   O    O  N N 315 
PHE   CB   C  N N 316 
PHE   CG   C  Y N 317 
PHE   CD1  C  Y N 318 
PHE   CD2  C  Y N 319 
PHE   CE1  C  Y N 320 
PHE   CE2  C  Y N 321 
PHE   CZ   C  Y N 322 
PHE   OXT  O  N N 323 
PHE   H    H  N N 324 
PHE   H2   H  N N 325 
PHE   HA   H  N N 326 
PHE   HB2  H  N N 327 
PHE   HB3  H  N N 328 
PHE   HD1  H  N N 329 
PHE   HD2  H  N N 330 
PHE   HE1  H  N N 331 
PHE   HE2  H  N N 332 
PHE   HZ   H  N N 333 
PHE   HXT  H  N N 334 
PRO   N    N  N N 335 
PRO   CA   C  N S 336 
PRO   C    C  N N 337 
PRO   O    O  N N 338 
PRO   CB   C  N N 339 
PRO   CG   C  N N 340 
PRO   CD   C  N N 341 
PRO   OXT  O  N N 342 
PRO   H    H  N N 343 
PRO   HA   H  N N 344 
PRO   HB2  H  N N 345 
PRO   HB3  H  N N 346 
PRO   HG2  H  N N 347 
PRO   HG3  H  N N 348 
PRO   HD2  H  N N 349 
PRO   HD3  H  N N 350 
PRO   HXT  H  N N 351 
SER   N    N  N N 352 
SER   CA   C  N S 353 
SER   C    C  N N 354 
SER   O    O  N N 355 
SER   CB   C  N N 356 
SER   OG   O  N N 357 
SER   OXT  O  N N 358 
SER   H    H  N N 359 
SER   H2   H  N N 360 
SER   HA   H  N N 361 
SER   HB2  H  N N 362 
SER   HB3  H  N N 363 
SER   HG   H  N N 364 
SER   HXT  H  N N 365 
THR   N    N  N N 366 
THR   CA   C  N S 367 
THR   C    C  N N 368 
THR   O    O  N N 369 
THR   CB   C  N R 370 
THR   OG1  O  N N 371 
THR   CG2  C  N N 372 
THR   OXT  O  N N 373 
THR   H    H  N N 374 
THR   H2   H  N N 375 
THR   HA   H  N N 376 
THR   HB   H  N N 377 
THR   HG1  H  N N 378 
THR   HG21 H  N N 379 
THR   HG22 H  N N 380 
THR   HG23 H  N N 381 
THR   HXT  H  N N 382 
TRP   N    N  N N 383 
TRP   CA   C  N S 384 
TRP   C    C  N N 385 
TRP   O    O  N N 386 
TRP   CB   C  N N 387 
TRP   CG   C  Y N 388 
TRP   CD1  C  Y N 389 
TRP   CD2  C  Y N 390 
TRP   NE1  N  Y N 391 
TRP   CE2  C  Y N 392 
TRP   CE3  C  Y N 393 
TRP   CZ2  C  Y N 394 
TRP   CZ3  C  Y N 395 
TRP   CH2  C  Y N 396 
TRP   OXT  O  N N 397 
TRP   H    H  N N 398 
TRP   H2   H  N N 399 
TRP   HA   H  N N 400 
TRP   HB2  H  N N 401 
TRP   HB3  H  N N 402 
TRP   HD1  H  N N 403 
TRP   HE1  H  N N 404 
TRP   HE3  H  N N 405 
TRP   HZ2  H  N N 406 
TRP   HZ3  H  N N 407 
TRP   HH2  H  N N 408 
TRP   HXT  H  N N 409 
TYR   N    N  N N 410 
TYR   CA   C  N S 411 
TYR   C    C  N N 412 
TYR   O    O  N N 413 
TYR   CB   C  N N 414 
TYR   CG   C  Y N 415 
TYR   CD1  C  Y N 416 
TYR   CD2  C  Y N 417 
TYR   CE1  C  Y N 418 
TYR   CE2  C  Y N 419 
TYR   CZ   C  Y N 420 
TYR   OH   O  N N 421 
TYR   OXT  O  N N 422 
TYR   H    H  N N 423 
TYR   H2   H  N N 424 
TYR   HA   H  N N 425 
TYR   HB2  H  N N 426 
TYR   HB3  H  N N 427 
TYR   HD1  H  N N 428 
TYR   HD2  H  N N 429 
TYR   HE1  H  N N 430 
TYR   HE2  H  N N 431 
TYR   HH   H  N N 432 
TYR   HXT  H  N N 433 
VAL   N    N  N N 434 
VAL   CA   C  N S 435 
VAL   C    C  N N 436 
VAL   O    O  N N 437 
VAL   CB   C  N N 438 
VAL   CG1  C  N N 439 
VAL   CG2  C  N N 440 
VAL   OXT  O  N N 441 
VAL   H    H  N N 442 
VAL   H2   H  N N 443 
VAL   HA   H  N N 444 
VAL   HB   H  N N 445 
VAL   HG11 H  N N 446 
VAL   HG12 H  N N 447 
VAL   HG13 H  N N 448 
VAL   HG21 H  N N 449 
VAL   HG22 H  N N 450 
VAL   HG23 H  N N 451 
VAL   HXT  H  N N 452 
# 
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 
A1APS C19 C18  doub Y N 1   
A1APS C19 C20  sing Y N 2   
A1APS C18 C17  sing Y N 3   
A1APS C20 C21  doub Y N 4   
A1APS C17 C16  doub Y N 5   
A1APS C21 C16  sing Y N 6   
A1APS C21 C22  sing Y N 7   
A1APS C16 C15  sing Y N 8   
A1APS C22 C13  doub Y N 9   
A1APS C15 C14  doub Y N 10  
A1APS C13 C14  sing Y N 11  
A1APS C13 C12  sing N N 12  
A1APS S11 C12  sing Y N 13  
A1APS S11 C10  sing Y N 14  
A1APS C12 N23  doub Y N 15  
A1APS C10 C09  doub Y N 16  
A1APS N23 C09  sing Y N 17  
A1APS C09 C08  sing N N 18  
A1APS C08 C02  sing N N 19  
A1APS C02 N03  sing N N 20  
A1APS C02 O01  doub N N 21  
A1APS N03 C04  sing N N 22  
A1APS C04 C05  sing N N 23  
A1APS O07 C05  doub N N 24  
A1APS C05 O06  sing N N 25  
A1APS C10 H1   sing N N 26  
A1APS C15 H2   sing N N 27  
A1APS C17 H3   sing N N 28  
A1APS C20 H4   sing N N 29  
A1APS C22 H5   sing N N 30  
A1APS C04 H6   sing N N 31  
A1APS C04 H7   sing N N 32  
A1APS C08 H8   sing N N 33  
A1APS C08 H9   sing N N 34  
A1APS C14 H10  sing N N 35  
A1APS C18 H11  sing N N 36  
A1APS C19 H12  sing N N 37  
A1APS N03 H13  sing N N 38  
A1APS O06 H14  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
NCO   CO  N1   sing N N 276 
NCO   CO  N2   sing N N 277 
NCO   CO  N3   sing N N 278 
NCO   CO  N4   sing N N 279 
NCO   CO  N5   sing N N 280 
NCO   CO  N6   sing N N 281 
NCO   N1  HN11 sing N N 282 
NCO   N1  HN12 sing N N 283 
NCO   N1  HN13 sing N N 284 
NCO   N2  HN21 sing N N 285 
NCO   N2  HN22 sing N N 286 
NCO   N2  HN23 sing N N 287 
NCO   N3  HN31 sing N N 288 
NCO   N3  HN32 sing N N 289 
NCO   N3  HN33 sing N N 290 
NCO   N4  HN41 sing N N 291 
NCO   N4  HN42 sing N N 292 
NCO   N4  HN43 sing N N 293 
NCO   N5  HN51 sing N N 294 
NCO   N5  HN52 sing N N 295 
NCO   N5  HN53 sing N N 296 
NCO   N6  HN61 sing N N 297 
NCO   N6  HN62 sing N N 298 
NCO   N6  HN63 sing N N 299 
PHE   N   CA   sing N N 300 
PHE   N   H    sing N N 301 
PHE   N   H2   sing N N 302 
PHE   CA  C    sing N N 303 
PHE   CA  CB   sing N N 304 
PHE   CA  HA   sing N N 305 
PHE   C   O    doub N N 306 
PHE   C   OXT  sing N N 307 
PHE   CB  CG   sing N N 308 
PHE   CB  HB2  sing N N 309 
PHE   CB  HB3  sing N N 310 
PHE   CG  CD1  doub Y N 311 
PHE   CG  CD2  sing Y N 312 
PHE   CD1 CE1  sing Y N 313 
PHE   CD1 HD1  sing N N 314 
PHE   CD2 CE2  doub Y N 315 
PHE   CD2 HD2  sing N N 316 
PHE   CE1 CZ   doub Y N 317 
PHE   CE1 HE1  sing N N 318 
PHE   CE2 CZ   sing Y N 319 
PHE   CE2 HE2  sing N N 320 
PHE   CZ  HZ   sing N N 321 
PHE   OXT HXT  sing N N 322 
PRO   N   CA   sing N N 323 
PRO   N   CD   sing N N 324 
PRO   N   H    sing N N 325 
PRO   CA  C    sing N N 326 
PRO   CA  CB   sing N N 327 
PRO   CA  HA   sing N N 328 
PRO   C   O    doub N N 329 
PRO   C   OXT  sing N N 330 
PRO   CB  CG   sing N N 331 
PRO   CB  HB2  sing N N 332 
PRO   CB  HB3  sing N N 333 
PRO   CG  CD   sing N N 334 
PRO   CG  HG2  sing N N 335 
PRO   CG  HG3  sing N N 336 
PRO   CD  HD2  sing N N 337 
PRO   CD  HD3  sing N N 338 
PRO   OXT HXT  sing N N 339 
SER   N   CA   sing N N 340 
SER   N   H    sing N N 341 
SER   N   H2   sing N N 342 
SER   CA  C    sing N N 343 
SER   CA  CB   sing N N 344 
SER   CA  HA   sing N N 345 
SER   C   O    doub N N 346 
SER   C   OXT  sing N N 347 
SER   CB  OG   sing N N 348 
SER   CB  HB2  sing N N 349 
SER   CB  HB3  sing N N 350 
SER   OG  HG   sing N N 351 
SER   OXT HXT  sing N N 352 
THR   N   CA   sing N N 353 
THR   N   H    sing N N 354 
THR   N   H2   sing N N 355 
THR   CA  C    sing N N 356 
THR   CA  CB   sing N N 357 
THR   CA  HA   sing N N 358 
THR   C   O    doub N N 359 
THR   C   OXT  sing N N 360 
THR   CB  OG1  sing N N 361 
THR   CB  CG2  sing N N 362 
THR   CB  HB   sing N N 363 
THR   OG1 HG1  sing N N 364 
THR   CG2 HG21 sing N N 365 
THR   CG2 HG22 sing N N 366 
THR   CG2 HG23 sing N N 367 
THR   OXT HXT  sing N N 368 
TRP   N   CA   sing N N 369 
TRP   N   H    sing N N 370 
TRP   N   H2   sing N N 371 
TRP   CA  C    sing N N 372 
TRP   CA  CB   sing N N 373 
TRP   CA  HA   sing N N 374 
TRP   C   O    doub N N 375 
TRP   C   OXT  sing N N 376 
TRP   CB  CG   sing N N 377 
TRP   CB  HB2  sing N N 378 
TRP   CB  HB3  sing N N 379 
TRP   CG  CD1  doub Y N 380 
TRP   CG  CD2  sing Y N 381 
TRP   CD1 NE1  sing Y N 382 
TRP   CD1 HD1  sing N N 383 
TRP   CD2 CE2  doub Y N 384 
TRP   CD2 CE3  sing Y N 385 
TRP   NE1 CE2  sing Y N 386 
TRP   NE1 HE1  sing N N 387 
TRP   CE2 CZ2  sing Y N 388 
TRP   CE3 CZ3  doub Y N 389 
TRP   CE3 HE3  sing N N 390 
TRP   CZ2 CH2  doub Y N 391 
TRP   CZ2 HZ2  sing N N 392 
TRP   CZ3 CH2  sing Y N 393 
TRP   CZ3 HZ3  sing N N 394 
TRP   CH2 HH2  sing N N 395 
TRP   OXT HXT  sing N N 396 
TYR   N   CA   sing N N 397 
TYR   N   H    sing N N 398 
TYR   N   H2   sing N N 399 
TYR   CA  C    sing N N 400 
TYR   CA  CB   sing N N 401 
TYR   CA  HA   sing N N 402 
TYR   C   O    doub N N 403 
TYR   C   OXT  sing N N 404 
TYR   CB  CG   sing N N 405 
TYR   CB  HB2  sing N N 406 
TYR   CB  HB3  sing N N 407 
TYR   CG  CD1  doub Y N 408 
TYR   CG  CD2  sing Y N 409 
TYR   CD1 CE1  sing Y N 410 
TYR   CD1 HD1  sing N N 411 
TYR   CD2 CE2  doub Y N 412 
TYR   CD2 HD2  sing N N 413 
TYR   CE1 CZ   doub Y N 414 
TYR   CE1 HE1  sing N N 415 
TYR   CE2 CZ   sing Y N 416 
TYR   CE2 HE2  sing N N 417 
TYR   CZ  OH   sing N N 418 
TYR   OH  HH   sing N N 419 
TYR   OXT HXT  sing N N 420 
VAL   N   CA   sing N N 421 
VAL   N   H    sing N N 422 
VAL   N   H2   sing N N 423 
VAL   CA  C    sing N N 424 
VAL   CA  CB   sing N N 425 
VAL   CA  HA   sing N N 426 
VAL   C   O    doub N N 427 
VAL   C   OXT  sing N N 428 
VAL   CB  CG1  sing N N 429 
VAL   CB  CG2  sing N N 430 
VAL   CB  HB   sing N N 431 
VAL   CG1 HG11 sing N N 432 
VAL   CG1 HG12 sing N N 433 
VAL   CG1 HG13 sing N N 434 
VAL   CG2 HG21 sing N N 435 
VAL   CG2 HG22 sing N N 436 
VAL   CG2 HG23 sing N N 437 
VAL   OXT HXT  sing N N 438 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Cancer Institute (NIH/NCI)'                               'United States' R01CA247365-04 1 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' R01-AI157312   2 
# 
_pdbx_initial_refinement_model.accession_code   8EBL 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    9BCA 
_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]   0.022458 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005781 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011372 
_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]   0.011571 
_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  
CO 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LEU   A 1 14  ? 18.576  -25.669 13.257  1.00 50.25 ? 26  LEU   A N   1 
ATOM   2    C  CA  . LEU   A 1 14  ? 17.372  -24.849 13.187  1.00 55.84 ? 26  LEU   A CA  1 
ATOM   3    C  C   . LEU   A 1 14  ? 17.722  -23.406 12.832  1.00 57.72 ? 26  LEU   A C   1 
ATOM   4    O  O   . LEU   A 1 14  ? 18.820  -22.935 13.137  1.00 56.49 ? 26  LEU   A O   1 
ATOM   5    C  CB  . LEU   A 1 14  ? 16.609  -24.908 14.513  1.00 58.43 ? 26  LEU   A CB  1 
ATOM   6    C  CG  . LEU   A 1 14  ? 16.106  -26.289 14.948  1.00 56.89 ? 26  LEU   A CG  1 
ATOM   7    C  CD1 . LEU   A 1 14  ? 15.715  -26.288 16.421  1.00 56.85 ? 26  LEU   A CD1 1 
ATOM   8    C  CD2 . LEU   A 1 14  ? 14.934  -26.730 14.082  1.00 63.68 ? 26  LEU   A CD2 1 
ATOM   9    N  N   . ALA   A 1 15  ? 16.781  -22.711 12.194  1.00 58.38 ? 27  ALA   A N   1 
ATOM   10   C  CA  . ALA   A 1 15  ? 17.030  -21.357 11.715  1.00 53.55 ? 27  ALA   A CA  1 
ATOM   11   C  C   . ALA   A 1 15  ? 17.317  -20.414 12.878  1.00 47.47 ? 27  ALA   A C   1 
ATOM   12   O  O   . ALA   A 1 15  ? 16.756  -20.543 13.970  1.00 52.38 ? 27  ALA   A O   1 
ATOM   13   C  CB  . ALA   A 1 15  ? 15.836  -20.850 10.905  1.00 53.83 ? 27  ALA   A CB  1 
ATOM   14   N  N   . CYS   A 1 16  ? 18.195  -19.447 12.625  1.00 43.78 ? 28  CYS   A N   1 
ATOM   15   C  CA  . CYS   A 1 16  ? 18.750  -18.584 13.658  1.00 40.51 ? 28  CYS   A CA  1 
ATOM   16   C  C   . CYS   A 1 16  ? 18.963  -17.171 13.115  1.00 37.84 ? 28  CYS   A C   1 
ATOM   17   O  O   . CYS   A 1 16  ? 19.713  -16.985 12.149  1.00 32.15 ? 28  CYS   A O   1 
ATOM   18   C  CB  . CYS   A 1 16  ? 20.056  -19.198 14.173  1.00 39.36 ? 28  CYS   A CB  1 
ATOM   19   S  SG  . CYS   A 1 16  ? 21.273  -18.046 14.824  1.00 52.37 ? 28  CYS   A SG  1 
ATOM   20   N  N   . PRO   A 1 17  ? 18.315  -16.155 13.692  1.00 33.26 ? 29  PRO   A N   1 
ATOM   21   C  CA  . PRO   A 1 17  ? 18.493  -14.787 13.186  1.00 30.06 ? 29  PRO   A CA  1 
ATOM   22   C  C   . PRO   A 1 17  ? 19.904  -14.266 13.421  1.00 29.82 ? 29  PRO   A C   1 
ATOM   23   O  O   . PRO   A 1 17  ? 20.584  -14.643 14.376  1.00 29.14 ? 29  PRO   A O   1 
ATOM   24   C  CB  . PRO   A 1 17  ? 17.462  -13.979 13.983  1.00 32.44 ? 29  PRO   A CB  1 
ATOM   25   C  CG  . PRO   A 1 17  ? 17.268  -14.757 15.238  1.00 32.27 ? 29  PRO   A CG  1 
ATOM   26   C  CD  . PRO   A 1 17  ? 17.387  -16.205 14.833  1.00 32.47 ? 29  PRO   A CD  1 
ATOM   27   N  N   . ALA   A 1 18  ? 20.338  -13.378 12.530  1.00 27.05 ? 30  ALA   A N   1 
ATOM   28   C  CA  . ALA   A 1 18  ? 21.676  -12.812 12.614  1.00 27.51 ? 30  ALA   A CA  1 
ATOM   29   C  C   . ALA   A 1 18  ? 21.795  -11.852 13.793  1.00 26.42 ? 30  ALA   A C   1 
ATOM   30   O  O   . ALA   A 1 18  ? 20.804  -11.282 14.265  1.00 25.30 ? 30  ALA   A O   1 
ATOM   31   C  CB  . ALA   A 1 18  ? 22.030  -12.091 11.312  1.00 29.80 ? 30  ALA   A CB  1 
ATOM   32   N  N   . GLU   A 1 19  ? 23.030  -11.685 14.267  1.00 24.12 ? 31  GLU   A N   1 
ATOM   33   C  CA  . GLU   A 1 19  ? 23.331  -10.747 15.336  1.00 25.09 ? 31  GLU   A CA  1 
ATOM   34   C  C   . GLU   A 1 19  ? 22.947  -9.335  14.915  1.00 23.03 ? 31  GLU   A C   1 
ATOM   35   O  O   . GLU   A 1 19  ? 22.890  -9.006  13.729  1.00 23.99 ? 31  GLU   A O   1 
ATOM   36   C  CB  . GLU   A 1 19  ? 24.822  -10.805 15.709  1.00 23.62 ? 31  GLU   A CB  1 
ATOM   37   C  CG  . GLU   A 1 19  ? 25.774  -10.078 14.737  1.00 27.65 ? 31  GLU   A CG  1 
ATOM   38   C  CD  . GLU   A 1 19  ? 26.250  -10.951 13.574  1.00 32.98 ? 31  GLU   A CD  1 
ATOM   39   O  OE1 . GLU   A 1 19  ? 25.631  -12.006 13.313  1.00 32.78 ? 31  GLU   A OE1 1 
ATOM   40   O  OE2 . GLU   A 1 19  ? 27.261  -10.581 12.929  1.00 32.87 ? 31  GLU   A OE2 1 
ATOM   41   N  N   . ARG   A 1 20  ? 22.680  -8.489  15.908  1.00 19.68 ? 32  ARG   A N   1 
ATOM   42   C  CA  . ARG   A 1 20  ? 22.221  -7.137  15.611  1.00 18.10 ? 32  ARG   A CA  1 
ATOM   43   C  C   . ARG   A 1 20  ? 22.144  -6.329  16.900  1.00 17.23 ? 32  ARG   A C   1 
ATOM   44   O  O   . ARG   A 1 20  ? 22.076  -6.880  18.005  1.00 19.35 ? 32  ARG   A O   1 
ATOM   45   C  CB  . ARG   A 1 20  ? 20.845  -7.138  14.921  1.00 20.61 ? 32  ARG   A CB  1 
ATOM   46   C  CG  . ARG   A 1 20  ? 19.703  -7.560  15.845  1.00 17.40 ? 32  ARG   A CG  1 
ATOM   47   C  CD  . ARG   A 1 20  ? 18.476  -7.991  15.054  1.00 20.63 ? 32  ARG   A CD  1 
ATOM   48   N  NE  . ARG   A 1 20  ? 18.760  -9.193  14.281  1.00 23.08 ? 32  ARG   A NE  1 
ATOM   49   C  CZ  . ARG   A 1 20  ? 18.123  -9.538  13.169  1.00 21.79 ? 32  ARG   A CZ  1 
ATOM   50   N  NH1 . ARG   A 1 20  ? 17.146  -8.795  12.674  1.00 23.22 ? 32  ARG   A NH1 1 
ATOM   51   N  NH2 . ARG   A 1 20  ? 18.467  -10.661 12.548  1.00 24.84 ? 32  ARG   A NH2 1 
ATOM   52   N  N   . SER   A 1 21  ? 22.160  -5.010  16.734  1.00 17.89 ? 33  SER   A N   1 
ATOM   53   C  CA  . SER   A 1 21  ? 21.811  -4.049  17.769  1.00 16.52 ? 33  SER   A CA  1 
ATOM   54   C  C   . SER   A 1 21  ? 20.857  -3.029  17.166  1.00 19.13 ? 33  SER   A C   1 
ATOM   55   O  O   . SER   A 1 21  ? 20.703  -2.941  15.952  1.00 12.53 ? 33  SER   A O   1 
ATOM   56   C  CB  . SER   A 1 21  ? 23.037  -3.330  18.330  1.00 16.50 ? 33  SER   A CB  1 
ATOM   57   O  OG  . SER   A 1 21  ? 23.948  -4.241  18.908  1.00 17.35 ? 33  SER   A OG  1 
ATOM   58   N  N   . GLY   A 1 22  ? 20.202  -2.250  18.023  1.00 17.81 ? 34  GLY   A N   1 
ATOM   59   C  CA  . GLY   A 1 22  ? 19.318  -1.234  17.482  1.00 16.98 ? 34  GLY   A CA  1 
ATOM   60   C  C   . GLY   A 1 22  ? 18.059  -1.761  16.838  1.00 14.22 ? 34  GLY   A C   1 
ATOM   61   O  O   . GLY   A 1 22  ? 17.321  -0.987  16.228  1.00 13.79 ? 34  GLY   A O   1 
ATOM   62   N  N   . HIS   A 1 23  ? 17.808  -3.060  16.939  1.00 14.83 ? 35  HIS   A N   1 
ATOM   63   C  CA  . HIS   A 1 23  ? 16.575  -3.654  16.462  1.00 14.18 ? 35  HIS   A CA  1 
ATOM   64   C  C   . HIS   A 1 23  ? 15.418  -3.277  17.386  1.00 17.70 ? 35  HIS   A C   1 
ATOM   65   O  O   . HIS   A 1 23  ? 15.579  -2.589  18.412  1.00 15.48 ? 35  HIS   A O   1 
ATOM   66   C  CB  . HIS   A 1 23  ? 16.731  -5.168  16.400  1.00 16.07 ? 35  HIS   A CB  1 
ATOM   67   C  CG  . HIS   A 1 23  ? 17.090  -5.769  17.727  1.00 18.50 ? 35  HIS   A CG  1 
ATOM   68   N  ND1 . HIS   A 1 23  ? 18.322  -5.581  18.317  1.00 18.23 ? 35  HIS   A ND1 1 
ATOM   69   C  CD2 . HIS   A 1 23  ? 16.368  -6.514  18.594  1.00 18.64 ? 35  HIS   A CD2 1 
ATOM   70   C  CE1 . HIS   A 1 23  ? 18.351  -6.205  19.481  1.00 19.43 ? 35  HIS   A CE1 1 
ATOM   71   N  NE2 . HIS   A 1 23  ? 17.176  -6.779  19.672  1.00 18.80 ? 35  HIS   A NE2 1 
ATOM   72   N  N   . VAL   A 1 24  ? 14.232  -3.739  17.011  1.00 15.57 ? 36  VAL   A N   1 
ATOM   73   C  CA  . VAL   A 1 24  ? 13.056  -3.637  17.859  1.00 15.35 ? 36  VAL   A CA  1 
ATOM   74   C  C   . VAL   A 1 24  ? 12.633  -5.043  18.235  1.00 16.59 ? 36  VAL   A C   1 
ATOM   75   O  O   . VAL   A 1 24  ? 12.880  -6.009  17.508  1.00 15.69 ? 36  VAL   A O   1 
ATOM   76   C  CB  . VAL   A 1 24  ? 11.871  -2.884  17.217  1.00 16.29 ? 36  VAL   A CB  1 
ATOM   77   C  CG1 . VAL   A 1 24  ? 12.201  -1.399  17.025  1.00 16.75 ? 36  VAL   A CG1 1 
ATOM   78   C  CG2 . VAL   A 1 24  ? 11.454  -3.548  15.920  1.00 16.90 ? 36  VAL   A CG2 1 
ATOM   79   N  N   . ALA   A 1 25  ? 11.978  -5.150  19.390  1.00 15.01 ? 37  ALA   A N   1 
ATOM   80   C  CA  . ALA   A 1 25  ? 11.441  -6.423  19.859  1.00 19.61 ? 37  ALA   A CA  1 
ATOM   81   C  C   . ALA   A 1 25  ? 10.179  -6.148  20.659  1.00 19.97 ? 37  ALA   A C   1 
ATOM   82   O  O   . ALA   A 1 25  ? 10.203  -5.400  21.645  1.00 18.94 ? 37  ALA   A O   1 
ATOM   83   C  CB  . ALA   A 1 25  ? 12.459  -7.193  20.706  1.00 20.61 ? 37  ALA   A CB  1 
ATOM   84   N  N   . VAL   A 1 26  ? 9.084   -6.758  20.233  1.00 20.41 ? 38  VAL   A N   1 
ATOM   85   C  CA  . VAL   A 1 26  ? 7.792   -6.590  20.873  1.00 18.89 ? 38  VAL   A CA  1 
ATOM   86   C  C   . VAL   A 1 26  ? 7.214   -7.973  21.118  1.00 21.36 ? 38  VAL   A C   1 
ATOM   87   O  O   . VAL   A 1 26  ? 7.573   -8.944  20.449  1.00 22.90 ? 38  VAL   A O   1 
ATOM   88   C  CB  . VAL   A 1 26  ? 6.828   -5.716  20.043  1.00 23.25 ? 38  VAL   A CB  1 
ATOM   89   C  CG1 . VAL   A 1 26  ? 7.444   -4.362  19.787  1.00 20.71 ? 38  VAL   A CG1 1 
ATOM   90   C  CG2 . VAL   A 1 26  ? 6.436   -6.408  18.725  1.00 22.15 ? 38  VAL   A CG2 1 
ATOM   91   N  N   . SER   A 1 27  ? 6.330   -8.066  22.109  1.00 25.47 ? 39  SER   A N   1 
ATOM   92   C  CA  . SER   A 1 27  ? 5.870   -9.356  22.597  1.00 24.09 ? 39  SER   A CA  1 
ATOM   93   C  C   . SER   A 1 27  ? 4.404   -9.274  23.000  1.00 24.76 ? 39  SER   A C   1 
ATOM   94   O  O   . SER   A 1 27  ? 3.920   -8.226  23.439  1.00 24.73 ? 39  SER   A O   1 
ATOM   95   C  CB  . SER   A 1 27  ? 6.708   -9.828  23.799  1.00 28.41 ? 39  SER   A CB  1 
ATOM   96   O  OG  . SER   A 1 27  ? 6.313   -11.121 24.243  1.00 30.45 ? 39  SER   A OG  1 
ATOM   97   N  N   . ASP   A 1 28  ? 3.708   -10.400 22.843  1.00 28.25 ? 40  ASP   A N   1 
ATOM   98   C  CA  . ASP   A 1 28  ? 2.364   -10.586 23.375  1.00 32.09 ? 40  ASP   A CA  1 
ATOM   99   C  C   . ASP   A 1 28  ? 2.368   -11.435 24.647  1.00 33.42 ? 40  ASP   A C   1 
ATOM   100  O  O   . ASP   A 1 28  ? 1.323   -11.965 25.041  1.00 32.38 ? 40  ASP   A O   1 
ATOM   101  C  CB  . ASP   A 1 28  ? 1.447   -11.203 22.310  1.00 33.96 ? 40  ASP   A CB  1 
ATOM   102  C  CG  . ASP   A 1 28  ? 1.974   -12.528 21.755  1.00 33.53 ? 40  ASP   A CG  1 
ATOM   103  O  OD1 . ASP   A 1 28  ? 2.941   -13.092 22.303  1.00 32.30 ? 40  ASP   A OD1 1 
ATOM   104  O  OD2 . ASP   A 1 28  ? 1.407   -13.015 20.748  1.00 38.77 ? 40  ASP   A OD2 1 
ATOM   105  N  N   . GLY   A 1 29  ? 3.532   -11.600 25.274  1.00 27.55 ? 41  GLY   A N   1 
ATOM   106  C  CA  . GLY   A 1 29  ? 3.681   -12.443 26.434  1.00 33.54 ? 41  GLY   A CA  1 
ATOM   107  C  C   . GLY   A 1 29  ? 4.086   -13.874 26.140  1.00 33.11 ? 41  GLY   A C   1 
ATOM   108  O  O   . GLY   A 1 29  ? 4.556   -14.570 27.048  1.00 34.98 ? 41  GLY   A O   1 
ATOM   109  N  N   . ARG   A 1 30  ? 3.913   -14.330 24.920  1.00 30.13 ? 42  ARG   A N   1 
ATOM   110  C  CA  . ARG   A 1 30  ? 4.276   -15.688 24.533  1.00 32.89 ? 42  ARG   A CA  1 
ATOM   111  C  C   . ARG   A 1 30  ? 5.136   -15.732 23.282  1.00 31.67 ? 42  ARG   A C   1 
ATOM   112  O  O   . ARG   A 1 30  ? 6.048   -16.556 23.200  1.00 33.78 ? 42  ARG   A O   1 
ATOM   113  C  CB  . ARG   A 1 30  ? 3.002   -16.523 24.331  1.00 36.91 ? 42  ARG   A CB  1 
ATOM   114  C  CG  . ARG   A 1 30  ? 3.216   -18.026 24.376  1.00 36.91 ? 42  ARG   A CG  1 
ATOM   115  C  CD  . ARG   A 1 30  ? 1.873   -18.716 24.455  1.00 35.09 ? 42  ARG   A CD  1 
ATOM   116  N  NE  . ARG   A 1 30  ? 1.037   -18.348 23.321  1.00 41.79 ? 42  ARG   A NE  1 
ATOM   117  C  CZ  . ARG   A 1 30  ? -0.287  -18.277 23.353  1.00 40.83 ? 42  ARG   A CZ  1 
ATOM   118  N  NH1 . ARG   A 1 30  ? -0.962  -18.481 24.471  1.00 43.57 ? 42  ARG   A NH1 1 
ATOM   119  N  NH2 . ARG   A 1 30  ? -0.948  -17.978 22.238  1.00 44.06 ? 42  ARG   A NH2 1 
ATOM   120  N  N   . HIS   A 1 31  ? 4.885   -14.859 22.317  1.00 32.04 ? 43  HIS   A N   1 
ATOM   121  C  CA  . HIS   A 1 31  ? 5.733   -14.750 21.139  1.00 29.38 ? 43  HIS   A CA  1 
ATOM   122  C  C   . HIS   A 1 31  ? 6.393   -13.383 21.100  1.00 27.46 ? 43  HIS   A C   1 
ATOM   123  O  O   . HIS   A 1 31  ? 5.781   -12.375 21.466  1.00 27.36 ? 43  HIS   A O   1 
ATOM   124  C  CB  . HIS   A 1 31  ? 4.937   -14.989 19.867  1.00 27.76 ? 43  HIS   A CB  1 
ATOM   125  C  CG  . HIS   A 1 31  ? 4.308   -16.342 19.813  1.00 34.34 ? 43  HIS   A CG  1 
ATOM   126  N  ND1 . HIS   A 1 31  ? 3.163   -16.657 20.514  1.00 36.80 ? 43  HIS   A ND1 1 
ATOM   127  C  CD2 . HIS   A 1 31  ? 4.677   -17.470 19.164  1.00 36.46 ? 43  HIS   A CD2 1 
ATOM   128  C  CE1 . HIS   A 1 31  ? 2.852   -17.921 20.291  1.00 38.18 ? 43  HIS   A CE1 1 
ATOM   129  N  NE2 . HIS   A 1 31  ? 3.753   -18.436 19.475  1.00 36.19 ? 43  HIS   A NE2 1 
ATOM   130  N  N   . MET   A 1 32  ? 7.651   -13.366 20.669  1.00 25.22 ? 44  MET   A N   1 
ATOM   131  C  CA  . MET   A 1 32  ? 8.457   -12.158 20.596  1.00 26.84 ? 44  MET   A CA  1 
ATOM   132  C  C   . MET   A 1 32  ? 8.766   -11.879 19.135  1.00 23.51 ? 44  MET   A C   1 
ATOM   133  O  O   . MET   A 1 32  ? 9.257   -12.760 18.420  1.00 26.76 ? 44  MET   A O   1 
ATOM   134  C  CB  . MET   A 1 32  ? 9.747   -12.318 21.417  1.00 23.66 ? 44  MET   A CB  1 
ATOM   135  C  CG  . MET   A 1 32  ? 10.519  -11.033 21.662  1.00 25.07 ? 44  MET   A CG  1 
ATOM   136  S  SD  . MET   A 1 32  ? 11.987  -11.279 22.705  1.00 25.84 ? 44  MET   A SD  1 
ATOM   137  C  CE  . MET   A 1 32  ? 13.100  -11.979 21.479  1.00 22.39 ? 44  MET   A CE  1 
ATOM   138  N  N   . PHE   A 1 33  ? 8.458   -10.666 18.690  1.00 22.11 ? 45  PHE   A N   1 
ATOM   139  C  CA  . PHE   A 1 33  ? 8.653   -10.266 17.303  1.00 23.30 ? 45  PHE   A CA  1 
ATOM   140  C  C   . PHE   A 1 33  ? 9.869   -9.357  17.225  1.00 22.69 ? 45  PHE   A C   1 
ATOM   141  O  O   . PHE   A 1 33  ? 9.968   -8.380  17.974  1.00 21.65 ? 45  PHE   A O   1 
ATOM   142  C  CB  . PHE   A 1 33  ? 7.417   -9.547  16.757  1.00 26.07 ? 45  PHE   A CB  1 
ATOM   143  C  CG  . PHE   A 1 33  ? 6.167   -10.379 16.786  1.00 25.43 ? 45  PHE   A CG  1 
ATOM   144  C  CD1 . PHE   A 1 33  ? 5.434   -10.520 17.954  1.00 25.88 ? 45  PHE   A CD1 1 
ATOM   145  C  CD2 . PHE   A 1 33  ? 5.727   -11.020 15.645  1.00 28.06 ? 45  PHE   A CD2 1 
ATOM   146  C  CE1 . PHE   A 1 33  ? 4.281   -11.291 17.981  1.00 28.31 ? 45  PHE   A CE1 1 
ATOM   147  C  CE2 . PHE   A 1 33  ? 4.575   -11.787 15.668  1.00 32.95 ? 45  PHE   A CE2 1 
ATOM   148  C  CZ  . PHE   A 1 33  ? 3.856   -11.921 16.836  1.00 30.38 ? 45  PHE   A CZ  1 
ATOM   149  N  N   . VAL   A 1 34  ? 10.799  -9.693  16.336  1.00 20.00 ? 46  VAL   A N   1 
ATOM   150  C  CA  . VAL   A 1 34  ? 12.081  -9.012  16.228  1.00 19.93 ? 46  VAL   A CA  1 
ATOM   151  C  C   . VAL   A 1 34  ? 12.220  -8.479  14.811  1.00 18.92 ? 46  VAL   A C   1 
ATOM   152  O  O   . VAL   A 1 34  ? 12.015  -9.224  13.841  1.00 21.27 ? 46  VAL   A O   1 
ATOM   153  C  CB  . VAL   A 1 34  ? 13.247  -9.956  16.578  1.00 21.16 ? 46  VAL   A CB  1 
ATOM   154  C  CG1 . VAL   A 1 34  ? 14.578  -9.326  16.215  1.00 21.04 ? 46  VAL   A CG1 1 
ATOM   155  C  CG2 . VAL   A 1 34  ? 13.204  -10.304 18.056  1.00 20.90 ? 46  VAL   A CG2 1 
ATOM   156  N  N   . TRP   A 1 35  ? 12.542  -7.188  14.693  1.00 18.29 ? 47  TRP   A N   1 
ATOM   157  C  CA  . TRP   A 1 35  ? 12.674  -6.560  13.380  1.00 19.16 ? 47  TRP   A CA  1 
ATOM   158  C  C   . TRP   A 1 35  ? 13.817  -5.549  13.364  1.00 18.27 ? 47  TRP   A C   1 
ATOM   159  O  O   . TRP   A 1 35  ? 14.005  -4.798  14.321  1.00 15.79 ? 47  TRP   A O   1 
ATOM   160  C  CB  . TRP   A 1 35  ? 11.371  -5.845  12.960  1.00 18.28 ? 47  TRP   A CB  1 
ATOM   161  C  CG  . TRP   A 1 35  ? 11.518  -5.131  11.661  1.00 17.66 ? 47  TRP   A CG  1 
ATOM   162  C  CD1 . TRP   A 1 35  ? 11.276  -5.648  10.420  1.00 19.05 ? 47  TRP   A CD1 1 
ATOM   163  C  CD2 . TRP   A 1 35  ? 11.987  -3.783  11.446  1.00 19.41 ? 47  TRP   A CD2 1 
ATOM   164  N  NE1 . TRP   A 1 35  ? 11.548  -4.711  9.447   1.00 17.52 ? 47  TRP   A NE1 1 
ATOM   165  C  CE2 . TRP   A 1 35  ? 11.988  -3.561  10.045  1.00 17.26 ? 47  TRP   A CE2 1 
ATOM   166  C  CE3 . TRP   A 1 35  ? 12.413  -2.751  12.292  1.00 18.06 ? 47  TRP   A CE3 1 
ATOM   167  C  CZ2 . TRP   A 1 35  ? 12.390  -2.351  9.475   1.00 14.01 ? 47  TRP   A CZ2 1 
ATOM   168  C  CZ3 . TRP   A 1 35  ? 12.814  -1.538  11.717  1.00 16.59 ? 47  TRP   A CZ3 1 
ATOM   169  C  CH2 . TRP   A 1 35  ? 12.790  -1.352  10.318  1.00 17.35 ? 47  TRP   A CH2 1 
ATOM   170  N  N   . GLY   A 1 36  ? 14.544  -5.502  12.245  1.00 14.63 ? 48  GLY   A N   1 
ATOM   171  C  CA  . GLY   A 1 36  ? 15.464  -4.410  11.983  1.00 15.71 ? 48  GLY   A CA  1 
ATOM   172  C  C   . GLY   A 1 36  ? 16.792  -4.495  12.727  1.00 20.20 ? 48  GLY   A C   1 
ATOM   173  O  O   . GLY   A 1 36  ? 17.282  -5.567  13.110  1.00 16.77 ? 48  GLY   A O   1 
ATOM   174  N  N   . GLY   A 1 37  ? 17.381  -3.319  12.923  1.00 16.01 ? 49  GLY   A N   1 
ATOM   175  C  CA  . GLY   A 1 37  ? 18.694  -3.201  13.522  1.00 17.61 ? 49  GLY   A CA  1 
ATOM   176  C  C   . GLY   A 1 37  ? 19.796  -3.262  12.484  1.00 19.15 ? 49  GLY   A C   1 
ATOM   177  O  O   . GLY   A 1 37  ? 19.559  -3.384  11.280  1.00 16.09 ? 49  GLY   A O   1 
ATOM   178  N  N   . TYR   A 1 38  ? 21.034  -3.204  12.979  1.00 16.39 ? 50  TYR   A N   1 
ATOM   179  C  CA  . TYR   A 1 38  ? 22.224  -3.195  12.135  1.00 17.06 ? 50  TYR   A CA  1 
ATOM   180  C  C   . TYR   A 1 38  ? 23.264  -4.093  12.788  1.00 20.20 ? 50  TYR   A C   1 
ATOM   181  O  O   . TYR   A 1 38  ? 23.124  -4.493  13.946  1.00 17.87 ? 50  TYR   A O   1 
ATOM   182  C  CB  . TYR   A 1 38  ? 22.778  -1.773  11.953  1.00 17.68 ? 50  TYR   A CB  1 
ATOM   183  C  CG  . TYR   A 1 38  ? 23.647  -1.336  13.118  1.00 13.72 ? 50  TYR   A CG  1 
ATOM   184  C  CD1 . TYR   A 1 38  ? 23.094  -1.067  14.370  1.00 14.80 ? 50  TYR   A CD1 1 
ATOM   185  C  CD2 . TYR   A 1 38  ? 25.022  -1.219  12.981  1.00 16.37 ? 50  TYR   A CD2 1 
ATOM   186  C  CE1 . TYR   A 1 38  ? 23.893  -0.681  15.451  1.00 17.18 ? 50  TYR   A CE1 1 
ATOM   187  C  CE2 . TYR   A 1 38  ? 25.824  -0.830  14.050  1.00 13.82 ? 50  TYR   A CE2 1 
ATOM   188  C  CZ  . TYR   A 1 38  ? 25.256  -0.571  15.283  1.00 19.44 ? 50  TYR   A CZ  1 
ATOM   189  O  OH  . TYR   A 1 38  ? 26.051  -0.197  16.343  1.00 18.64 ? 50  TYR   A OH  1 
ATOM   190  N  N   . LYS   A 1 39  ? 24.316  -4.417  12.039  1.00 21.57 ? 51  LYS   A N   1 
ATOM   191  C  CA  . LYS   A 1 39  ? 25.444  -5.152  12.602  1.00 23.02 ? 51  LYS   A CA  1 
ATOM   192  C  C   . LYS   A 1 39  ? 26.725  -4.654  11.944  1.00 27.46 ? 51  LYS   A C   1 
ATOM   193  O  O   . LYS   A 1 39  ? 26.718  -3.679  11.191  1.00 25.75 ? 51  LYS   A O   1 
ATOM   194  C  CB  . LYS   A 1 39  ? 25.263  -6.668  12.428  1.00 24.16 ? 51  LYS   A CB  1 
ATOM   195  C  CG  . LYS   A 1 39  ? 25.125  -7.122  10.985  1.00 27.09 ? 51  LYS   A CG  1 
ATOM   196  C  CD  . LYS   A 1 39  ? 24.783  -8.606  10.901  1.00 30.35 ? 51  LYS   A CD  1 
ATOM   197  C  CE  . LYS   A 1 39  ? 24.775  -9.106  9.455   1.00 33.61 ? 51  LYS   A CE  1 
ATOM   198  N  NZ  . LYS   A 1 39  ? 26.142  -9.327  8.927   1.00 33.57 ? 51  LYS   A NZ  1 
ATOM   199  N  N   . SER   A 1 40  ? 27.839  -5.309  12.256  1.00 25.08 ? 52  SER   A N   1 
ATOM   200  C  CA  . SER   A 1 40  ? 29.100  -5.060  11.571  1.00 31.71 ? 52  SER   A CA  1 
ATOM   201  C  C   . SER   A 1 40  ? 29.435  -6.248  10.668  1.00 37.17 ? 52  SER   A C   1 
ATOM   202  O  O   . SER   A 1 40  ? 28.625  -7.167  10.489  1.00 38.29 ? 52  SER   A O   1 
ATOM   203  C  CB  . SER   A 1 40  ? 30.206  -4.778  12.589  1.00 31.04 ? 52  SER   A CB  1 
ATOM   204  O  OG  . SER   A 1 40  ? 29.807  -3.752  13.485  1.00 29.42 ? 52  SER   A OG  1 
ATOM   205  N  N   . ASN   A 1 41  ? 30.630  -6.219  10.083  1.00 43.11 ? 53  ASN   A N   1 
ATOM   206  C  CA  . ASN   A 1 41  ? 31.104  -7.294  9.206   1.00 46.32 ? 53  ASN   A CA  1 
ATOM   207  C  C   . ASN   A 1 41  ? 30.118  -7.604  8.084   1.00 47.36 ? 53  ASN   A C   1 
ATOM   208  O  O   . ASN   A 1 41  ? 29.348  -6.743  7.667   1.00 48.64 ? 53  ASN   A O   1 
ATOM   209  C  CB  . ASN   A 1 41  ? 31.383  -8.567  10.010  1.00 49.00 ? 53  ASN   A CB  1 
ATOM   210  C  CG  . ASN   A 1 41  ? 32.845  -8.967  9.980   1.00 53.00 ? 53  ASN   A CG  1 
ATOM   211  O  OD1 . ASN   A 1 41  ? 33.733  -8.116  9.909   1.00 52.21 ? 53  ASN   A OD1 1 
ATOM   212  N  ND2 . ASN   A 1 41  ? 33.103  -10.269 10.027  1.00 56.90 ? 53  ASN   A ND2 1 
ATOM   213  N  N   . PHE   A 1 49  ? 26.225  -2.866  7.972   1.00 38.32 ? 61  PHE   A N   1 
ATOM   214  C  CA  . PHE   A 1 49  ? 24.991  -2.547  7.269   1.00 29.44 ? 61  PHE   A CA  1 
ATOM   215  C  C   . PHE   A 1 49  ? 23.746  -3.056  8.019   1.00 26.26 ? 61  PHE   A C   1 
ATOM   216  O  O   . PHE   A 1 49  ? 23.829  -3.625  9.116   1.00 25.17 ? 61  PHE   A O   1 
ATOM   217  C  CB  . PHE   A 1 49  ? 25.032  -3.111  5.841   1.00 31.77 ? 61  PHE   A CB  1 
ATOM   218  C  CG  . PHE   A 1 49  ? 25.702  -4.452  5.737   1.00 41.09 ? 61  PHE   A CG  1 
ATOM   219  C  CD1 . PHE   A 1 49  ? 25.000  -5.621  5.987   1.00 39.41 ? 61  PHE   A CD1 1 
ATOM   220  C  CD2 . PHE   A 1 49  ? 27.050  -4.544  5.400   1.00 50.40 ? 61  PHE   A CD2 1 
ATOM   221  C  CE1 . PHE   A 1 49  ? 25.628  -6.862  5.898   1.00 47.10 ? 61  PHE   A CE1 1 
ATOM   222  C  CE2 . PHE   A 1 49  ? 27.683  -5.780  5.305   1.00 47.48 ? 61  PHE   A CE2 1 
ATOM   223  C  CZ  . PHE   A 1 49  ? 26.972  -6.939  5.554   1.00 46.21 ? 61  PHE   A CZ  1 
ATOM   224  N  N   . TYR   A 1 50  ? 22.588  -2.822  7.426   1.00 26.86 ? 62  TYR   A N   1 
ATOM   225  C  CA  . TYR   A 1 50  ? 21.320  -3.078  8.091   1.00 23.67 ? 62  TYR   A CA  1 
ATOM   226  C  C   . TYR   A 1 50  ? 20.852  -4.501  7.848   1.00 22.78 ? 62  TYR   A C   1 
ATOM   227  O  O   . TYR   A 1 50  ? 21.042  -5.059  6.764   1.00 24.15 ? 62  TYR   A O   1 
ATOM   228  C  CB  . TYR   A 1 50  ? 20.254  -2.108  7.600   1.00 23.01 ? 62  TYR   A CB  1 
ATOM   229  C  CG  . TYR   A 1 50  ? 20.496  -0.672  7.956   1.00 22.78 ? 62  TYR   A CG  1 
ATOM   230  C  CD1 . TYR   A 1 50  ? 20.204  -0.190  9.229   1.00 18.86 ? 62  TYR   A CD1 1 
ATOM   231  C  CD2 . TYR   A 1 50  ? 21.008  0.211   7.020   1.00 20.48 ? 62  TYR   A CD2 1 
ATOM   232  C  CE1 . TYR   A 1 50  ? 20.425  1.132   9.554   1.00 22.60 ? 62  TYR   A CE1 1 
ATOM   233  C  CE2 . TYR   A 1 50  ? 21.238  1.525   7.337   1.00 19.78 ? 62  TYR   A CE2 1 
ATOM   234  C  CZ  . TYR   A 1 50  ? 20.947  1.985   8.593   1.00 21.16 ? 62  TYR   A CZ  1 
ATOM   235  O  OH  . TYR   A 1 50  ? 21.190  3.301   8.886   1.00 22.82 ? 62  TYR   A OH  1 
ATOM   236  N  N   . LEU   A 1 51  ? 20.211  -5.080  8.868   1.00 21.40 ? 63  LEU   A N   1 
ATOM   237  C  CA  . LEU   A 1 51  ? 19.591  -6.380  8.701   1.00 19.77 ? 63  LEU   A CA  1 
ATOM   238  C  C   . LEU   A 1 51  ? 18.401  -6.233  7.749   1.00 18.11 ? 63  LEU   A C   1 
ATOM   239  O  O   . LEU   A 1 51  ? 17.831  -5.143  7.633   1.00 17.09 ? 63  LEU   A O   1 
ATOM   240  C  CB  . LEU   A 1 51  ? 19.146  -6.948  10.049  1.00 21.29 ? 63  LEU   A CB  1 
ATOM   241  C  CG  . LEU   A 1 51  ? 20.193  -7.565  11.006  1.00 20.97 ? 63  LEU   A CG  1 
ATOM   242  C  CD1 . LEU   A 1 51  ? 20.822  -8.829  10.445  1.00 23.66 ? 63  LEU   A CD1 1 
ATOM   243  C  CD2 . LEU   A 1 51  ? 21.259  -6.577  11.441  1.00 21.64 ? 63  LEU   A CD2 1 
ATOM   244  N  N   . PRO   A 1 52  ? 18.032  -7.297  7.036   1.00 21.17 ? 64  PRO   A N   1 
ATOM   245  C  CA  . PRO   A 1 52  ? 17.065  -7.148  5.934   1.00 21.47 ? 64  PRO   A CA  1 
ATOM   246  C  C   . PRO   A 1 52  ? 15.690  -6.690  6.408   1.00 21.31 ? 64  PRO   A C   1 
ATOM   247  O  O   . PRO   A 1 52  ? 15.137  -7.211  7.384   1.00 20.43 ? 64  PRO   A O   1 
ATOM   248  C  CB  . PRO   A 1 52  ? 17.008  -8.554  5.326   1.00 27.35 ? 64  PRO   A CB  1 
ATOM   249  C  CG  . PRO   A 1 52  ? 18.339  -9.161  5.691   1.00 24.19 ? 64  PRO   A CG  1 
ATOM   250  C  CD  . PRO   A 1 52  ? 18.576  -8.664  7.092   1.00 23.84 ? 64  PRO   A CD  1 
ATOM   251  N  N   . ARG   A 1 53  ? 15.126  -5.728  5.665   1.00 18.22 ? 65  ARG   A N   1 
ATOM   252  C  CA  . ARG   A 1 53  ? 13.895  -5.057  6.084   1.00 20.81 ? 65  ARG   A CA  1 
ATOM   253  C  C   . ARG   A 1 53  ? 12.679  -5.973  6.044   1.00 20.97 ? 65  ARG   A C   1 
ATOM   254  O  O   . ARG   A 1 53  ? 11.772  -5.833  6.877   1.00 21.10 ? 65  ARG   A O   1 
ATOM   255  C  CB  . ARG   A 1 53  ? 13.653  -3.831  5.204   1.00 19.20 ? 65  ARG   A CB  1 
ATOM   256  C  CG  . ARG   A 1 53  ? 13.631  -4.168  3.702   1.00 19.69 ? 65  ARG   A CG  1 
ATOM   257  C  CD  . ARG   A 1 53  ? 13.794  -2.927  2.858   1.00 22.31 ? 65  ARG   A CD  1 
ATOM   258  N  NE  . ARG   A 1 53  ? 12.649  -2.039  2.982   1.00 20.26 ? 65  ARG   A NE  1 
ATOM   259  C  CZ  . ARG   A 1 53  ? 12.383  -1.033  2.157   1.00 22.39 ? 65  ARG   A CZ  1 
ATOM   260  N  NH1 . ARG   A 1 53  ? 13.159  -0.763  1.115   1.00 24.22 ? 65  ARG   A NH1 1 
ATOM   261  N  NH2 . ARG   A 1 53  ? 11.293  -0.297  2.364   1.00 22.47 ? 65  ARG   A NH2 1 
ATOM   262  N  N   . GLU   A 1 54  ? 12.617  -6.898  5.082   1.00 20.74 ? 66  GLU   A N   1 
ATOM   263  C  CA  . GLU   A 1 54  ? 11.411  -7.692  4.911   1.00 21.91 ? 66  GLU   A CA  1 
ATOM   264  C  C   . GLU   A 1 54  ? 11.268  -8.798  5.945   1.00 24.31 ? 66  GLU   A C   1 
ATOM   265  O  O   . GLU   A 1 54  ? 10.170  -9.331  6.110   1.00 25.50 ? 66  GLU   A O   1 
ATOM   266  C  CB  . GLU   A 1 54  ? 11.374  -8.301  3.507   1.00 23.61 ? 66  GLU   A CB  1 
ATOM   267  C  CG  . GLU   A 1 54  ? 12.373  -9.411  3.300   1.00 24.77 ? 66  GLU   A CG  1 
ATOM   268  C  CD  . GLU   A 1 54  ? 13.787  -8.905  3.073   1.00 29.69 ? 66  GLU   A CD  1 
ATOM   269  O  OE1 . GLU   A 1 54  ? 14.696  -9.750  2.881   1.00 34.44 ? 66  GLU   A OE1 1 
ATOM   270  O  OE2 . GLU   A 1 54  ? 13.996  -7.671  3.069   1.00 29.33 ? 66  GLU   A OE2 1 
ATOM   271  N  N   . GLU   A 1 55  ? 12.333  -9.162  6.645   1.00 23.63 ? 67  GLU   A N   1 
ATOM   272  C  CA  . GLU   A 1 55  ? 12.250  -10.290 7.552   1.00 22.24 ? 67  GLU   A CA  1 
ATOM   273  C  C   . GLU   A 1 55  ? 11.610  -9.861  8.864   1.00 23.23 ? 67  GLU   A C   1 
ATOM   274  O  O   . GLU   A 1 55  ? 11.856  -8.756  9.356   1.00 22.80 ? 67  GLU   A O   1 
ATOM   275  C  CB  . GLU   A 1 55  ? 13.640  -10.874 7.807   1.00 24.32 ? 67  GLU   A CB  1 
ATOM   276  C  CG  . GLU   A 1 55  ? 14.461  -11.111 6.557   1.00 24.45 ? 67  GLU   A CG  1 
ATOM   277  C  CD  . GLU   A 1 55  ? 15.853  -11.665 6.848   1.00 30.18 ? 67  GLU   A CD  1 
ATOM   278  O  OE1 . GLU   A 1 55  ? 16.434  -11.347 7.914   1.00 29.65 ? 67  GLU   A OE1 1 
ATOM   279  O  OE2 . GLU   A 1 55  ? 16.372  -12.411 5.994   1.00 31.09 ? 67  GLU   A OE2 1 
ATOM   280  N  N   . LEU   A 1 56  ? 10.759  -10.728 9.404   1.00 21.74 ? 68  LEU   A N   1 
ATOM   281  C  CA  . LEU   A 1 56  ? 10.272  -10.629 10.777  1.00 24.91 ? 68  LEU   A CA  1 
ATOM   282  C  C   . LEU   A 1 56  ? 10.621  -11.939 11.460  1.00 26.00 ? 68  LEU   A C   1 
ATOM   283  O  O   . LEU   A 1 56  ? 10.245  -13.008 10.973  1.00 27.43 ? 68  LEU   A O   1 
ATOM   284  C  CB  . LEU   A 1 56  ? 8.763   -10.383 10.830  1.00 24.61 ? 68  LEU   A CB  1 
ATOM   285  C  CG  . LEU   A 1 56  ? 8.223   -10.119 12.239  1.00 24.85 ? 68  LEU   A CG  1 
ATOM   286  C  CD1 . LEU   A 1 56  ? 8.700   -8.761  12.741  1.00 22.28 ? 68  LEU   A CD1 1 
ATOM   287  C  CD2 . LEU   A 1 56  ? 6.708   -10.217 12.288  1.00 31.44 ? 68  LEU   A CD2 1 
ATOM   288  N  N   . TRP   A 1 57  ? 11.350  -11.867 12.567  1.00 28.02 ? 69  TRP   A N   1 
ATOM   289  C  CA  . TRP   A 1 57  ? 11.734  -13.065 13.300  1.00 26.18 ? 69  TRP   A CA  1 
ATOM   290  C  C   . TRP   A 1 57  ? 10.818  -13.237 14.503  1.00 28.01 ? 69  TRP   A C   1 
ATOM   291  O  O   . TRP   A 1 57  ? 10.565  -12.278 15.239  1.00 24.27 ? 69  TRP   A O   1 
ATOM   292  C  CB  . TRP   A 1 57  ? 13.193  -13.003 13.747  1.00 28.34 ? 69  TRP   A CB  1 
ATOM   293  C  CG  . TRP   A 1 57  ? 14.157  -13.211 12.626  1.00 27.36 ? 69  TRP   A CG  1 
ATOM   294  C  CD1 . TRP   A 1 57  ? 14.749  -12.248 11.874  1.00 26.94 ? 69  TRP   A CD1 1 
ATOM   295  C  CD2 . TRP   A 1 57  ? 14.650  -14.466 12.140  1.00 29.82 ? 69  TRP   A CD2 1 
ATOM   296  N  NE1 . TRP   A 1 57  ? 15.580  -12.822 10.941  1.00 30.10 ? 69  TRP   A NE1 1 
ATOM   297  C  CE2 . TRP   A 1 57  ? 15.533  -14.184 11.081  1.00 30.34 ? 69  TRP   A CE2 1 
ATOM   298  C  CE3 . TRP   A 1 57  ? 14.428  -15.800 12.496  1.00 32.75 ? 69  TRP   A CE3 1 
ATOM   299  C  CZ2 . TRP   A 1 57  ? 16.198  -15.182 10.379  1.00 31.31 ? 69  TRP   A CZ2 1 
ATOM   300  C  CZ3 . TRP   A 1 57  ? 15.089  -16.791 11.794  1.00 34.07 ? 69  TRP   A CZ3 1 
ATOM   301  C  CH2 . TRP   A 1 57  ? 15.960  -16.477 10.746  1.00 33.62 ? 69  TRP   A CH2 1 
ATOM   302  N  N   . ILE   A 1 58  ? 10.315  -14.454 14.688  1.00 29.41 ? 70  ILE   A N   1 
ATOM   303  C  CA  . ILE   A 1 58  ? 9.387   -14.770 15.763  1.00 26.75 ? 70  ILE   A CA  1 
ATOM   304  C  C   . ILE   A 1 58  ? 10.055  -15.791 16.670  1.00 28.66 ? 70  ILE   A C   1 
ATOM   305  O  O   . ILE   A 1 58  ? 10.391  -16.896 16.230  1.00 30.12 ? 70  ILE   A O   1 
ATOM   306  C  CB  . ILE   A 1 58  ? 8.049   -15.295 15.220  1.00 31.66 ? 70  ILE   A CB  1 
ATOM   307  C  CG1 . ILE   A 1 58  ? 7.359   -14.220 14.375  1.00 30.59 ? 70  ILE   A CG1 1 
ATOM   308  C  CG2 . ILE   A 1 58  ? 7.155   -15.763 16.356  1.00 31.15 ? 70  ILE   A CG2 1 
ATOM   309  C  CD1 . ILE   A 1 58  ? 5.969   -14.617 13.901  1.00 32.81 ? 70  ILE   A CD1 1 
ATOM   310  N  N   . TYR   A 1 59  ? 10.257  -15.411 17.931  1.00 30.83 ? 71  TYR   A N   1 
ATOM   311  C  CA  . TYR   A 1 59  ? 10.806  -16.286 18.960  1.00 31.53 ? 71  TYR   A CA  1 
ATOM   312  C  C   . TYR   A 1 59  ? 9.670   -16.769 19.852  1.00 28.68 ? 71  TYR   A C   1 
ATOM   313  O  O   . TYR   A 1 59  ? 8.973   -15.958 20.475  1.00 31.24 ? 71  TYR   A O   1 
ATOM   314  C  CB  . TYR   A 1 59  ? 11.860  -15.550 19.789  1.00 30.32 ? 71  TYR   A CB  1 
ATOM   315  C  CG  . TYR   A 1 59  ? 12.480  -16.367 20.903  1.00 29.45 ? 71  TYR   A CG  1 
ATOM   316  C  CD1 . TYR   A 1 59  ? 13.501  -17.277 20.637  1.00 31.12 ? 71  TYR   A CD1 1 
ATOM   317  C  CD2 . TYR   A 1 59  ? 12.057  -16.220 22.222  1.00 29.91 ? 71  TYR   A CD2 1 
ATOM   318  C  CE1 . TYR   A 1 59  ? 14.080  -18.025 21.650  1.00 28.99 ? 71  TYR   A CE1 1 
ATOM   319  C  CE2 . TYR   A 1 59  ? 12.633  -16.968 23.248  1.00 31.37 ? 71  TYR   A CE2 1 
ATOM   320  C  CZ  . TYR   A 1 59  ? 13.646  -17.867 22.947  1.00 34.38 ? 71  TYR   A CZ  1 
ATOM   321  O  OH  . TYR   A 1 59  ? 14.226  -18.610 23.950  1.00 39.72 ? 71  TYR   A OH  1 
ATOM   322  N  N   . ASN   A 1 60  ? 9.479   -18.084 19.912  1.00 35.72 ? 72  ASN   A N   1 
ATOM   323  C  CA  . ASN   A 1 60  ? 8.496   -18.656 20.824  1.00 33.03 ? 72  ASN   A CA  1 
ATOM   324  C  C   . ASN   A 1 60  ? 9.121   -18.711 22.211  1.00 35.90 ? 72  ASN   A C   1 
ATOM   325  O  O   . ASN   A 1 60  ? 10.043  -19.496 22.455  1.00 38.08 ? 72  ASN   A O   1 
ATOM   326  C  CB  . ASN   A 1 60  ? 8.053   -20.038 20.344  1.00 36.13 ? 72  ASN   A CB  1 
ATOM   327  C  CG  . ASN   A 1 60  ? 6.859   -20.576 21.122  1.00 35.31 ? 72  ASN   A CG  1 
ATOM   328  O  OD1 . ASN   A 1 60  ? 6.784   -20.432 22.339  1.00 37.76 ? 72  ASN   A OD1 1 
ATOM   329  N  ND2 . ASN   A 1 60  ? 5.919   -21.196 20.416  1.00 33.90 ? 72  ASN   A ND2 1 
ATOM   330  N  N   . MET   A 1 61  ? 8.630   -17.862 23.119  1.00 33.23 ? 73  MET   A N   1 
ATOM   331  C  CA  . MET   A 1 61  ? 9.153   -17.826 24.477  1.00 34.92 ? 73  MET   A CA  1 
ATOM   332  C  C   . MET   A 1 61  ? 8.980   -19.149 25.205  1.00 35.44 ? 73  MET   A C   1 
ATOM   333  O  O   . MET   A 1 61  ? 9.718   -19.414 26.159  1.00 33.97 ? 73  MET   A O   1 
ATOM   334  C  CB  . MET   A 1 61  ? 8.473   -16.711 25.268  1.00 32.92 ? 73  MET   A CB  1 
ATOM   335  C  CG  . MET   A 1 61  ? 9.082   -15.354 25.029  1.00 34.29 ? 73  MET   A CG  1 
ATOM   336  S  SD  . MET   A 1 61  ? 7.928   -14.004 25.311  1.00 35.63 ? 73  MET   A SD  1 
ATOM   337  C  CE  . MET   A 1 61  ? 9.066   -12.634 25.303  1.00 29.11 ? 73  MET   A CE  1 
ATOM   338  N  N   . GLU   A 1 62  ? 8.028   -19.981 24.783  1.00 37.89 ? 74  GLU   A N   1 
ATOM   339  C  CA  . GLU   A 1 62  ? 7.790   -21.257 25.447  1.00 44.39 ? 74  GLU   A CA  1 
ATOM   340  C  C   . GLU   A 1 62  ? 8.575   -22.410 24.833  1.00 40.24 ? 74  GLU   A C   1 
ATOM   341  O  O   . GLU   A 1 62  ? 8.880   -23.379 25.537  1.00 42.51 ? 74  GLU   A O   1 
ATOM   342  C  CB  . GLU   A 1 62  ? 6.294   -21.593 25.432  1.00 43.59 ? 74  GLU   A CB  1 
ATOM   343  N  N   . THR   A 1 63  ? 8.907   -22.343 23.546  1.00 39.46 ? 75  THR   A N   1 
ATOM   344  C  CA  . THR   A 1 63  ? 9.656   -23.409 22.892  1.00 41.54 ? 75  THR   A CA  1 
ATOM   345  C  C   . THR   A 1 63  ? 11.051  -22.987 22.459  1.00 41.66 ? 75  THR   A C   1 
ATOM   346  O  O   . THR   A 1 63  ? 11.775  -23.804 21.875  1.00 41.95 ? 75  THR   A O   1 
ATOM   347  C  CB  . THR   A 1 63  ? 8.897   -23.933 21.669  1.00 42.96 ? 75  THR   A CB  1 
ATOM   348  O  OG1 . THR   A 1 63  ? 9.139   -23.069 20.551  1.00 46.16 ? 75  THR   A OG1 1 
ATOM   349  C  CG2 . THR   A 1 63  ? 7.403   -24.001 21.947  1.00 42.52 ? 75  THR   A CG2 1 
ATOM   350  N  N   . GLY   A 1 64  ? 11.434  -21.732 22.687  1.00 40.39 ? 76  GLY   A N   1 
ATOM   351  C  CA  . GLY   A 1 64  ? 12.783  -21.294 22.379  1.00 39.62 ? 76  GLY   A CA  1 
ATOM   352  C  C   . GLY   A 1 64  ? 13.199  -21.458 20.936  1.00 36.60 ? 76  GLY   A C   1 
ATOM   353  O  O   . GLY   A 1 64  ? 14.397  -21.444 20.644  1.00 37.39 ? 76  GLY   A O   1 
ATOM   354  N  N   . ARG   A 1 65  ? 12.246  -21.611 20.020  1.00 38.43 ? 77  ARG   A N   1 
ATOM   355  C  CA  . ARG   A 1 65  ? 12.534  -21.791 18.605  1.00 38.17 ? 77  ARG   A CA  1 
ATOM   356  C  C   . ARG   A 1 65  ? 12.244  -20.501 17.853  1.00 36.70 ? 77  ARG   A C   1 
ATOM   357  O  O   . ARG   A 1 65  ? 11.250  -19.817 18.125  1.00 35.49 ? 77  ARG   A O   1 
ATOM   358  C  CB  . ARG   A 1 65  ? 11.716  -22.944 18.009  1.00 39.77 ? 77  ARG   A CB  1 
ATOM   359  C  CG  . ARG   A 1 65  ? 12.105  -24.304 18.567  1.00 45.62 ? 77  ARG   A CG  1 
ATOM   360  C  CD  . ARG   A 1 65  ? 11.125  -25.411 18.195  1.00 49.21 ? 77  ARG   A CD  1 
ATOM   361  N  NE  . ARG   A 1 65  ? 11.201  -26.523 19.138  1.00 49.75 ? 77  ARG   A NE  1 
ATOM   362  C  CZ  . ARG   A 1 65  ? 10.191  -26.962 19.881  1.00 49.59 ? 77  ARG   A CZ  1 
ATOM   363  N  NH1 . ARG   A 1 65  ? 8.974   -26.458 19.764  1.00 46.98 ? 77  ARG   A NH1 1 
ATOM   364  N  NH2 . ARG   A 1 65  ? 10.407  -27.940 20.755  1.00 50.05 ? 77  ARG   A NH2 1 
ATOM   365  N  N   . TRP   A 1 66  ? 13.133  -20.164 16.930  1.00 35.67 ? 78  TRP   A N   1 
ATOM   366  C  CA  . TRP   A 1 66  ? 12.935  -19.040 16.032  1.00 37.24 ? 78  TRP   A CA  1 
ATOM   367  C  C   . TRP   A 1 66  ? 12.176  -19.480 14.785  1.00 37.89 ? 78  TRP   A C   1 
ATOM   368  O  O   . TRP   A 1 66  ? 12.189  -20.650 14.397  1.00 38.74 ? 78  TRP   A O   1 
ATOM   369  C  CB  . TRP   A 1 66  ? 14.269  -18.426 15.625  1.00 34.07 ? 78  TRP   A CB  1 
ATOM   370  C  CG  . TRP   A 1 66  ? 14.989  -17.749 16.723  1.00 34.03 ? 78  TRP   A CG  1 
ATOM   371  C  CD1 . TRP   A 1 66  ? 15.942  -18.289 17.526  1.00 32.93 ? 78  TRP   A CD1 1 
ATOM   372  C  CD2 . TRP   A 1 66  ? 14.835  -16.387 17.139  1.00 30.86 ? 78  TRP   A CD2 1 
ATOM   373  N  NE1 . TRP   A 1 66  ? 16.391  -17.353 18.424  1.00 31.74 ? 78  TRP   A NE1 1 
ATOM   374  C  CE2 . TRP   A 1 66  ? 15.730  -16.175 18.204  1.00 29.56 ? 78  TRP   A CE2 1 
ATOM   375  C  CE3 . TRP   A 1 66  ? 14.029  -15.328 16.714  1.00 29.53 ? 78  TRP   A CE3 1 
ATOM   376  C  CZ2 . TRP   A 1 66  ? 15.847  -14.945 18.849  1.00 24.23 ? 78  TRP   A CZ2 1 
ATOM   377  C  CZ3 . TRP   A 1 66  ? 14.147  -14.108 17.356  1.00 26.13 ? 78  TRP   A CZ3 1 
ATOM   378  C  CH2 . TRP   A 1 66  ? 15.046  -13.928 18.415  1.00 26.89 ? 78  TRP   A CH2 1 
ATOM   379  N  N   . LYS   A 1 67  ? 11.515  -18.511 14.157  1.00 42.40 ? 79  LYS   A N   1 
ATOM   380  C  CA  . LYS   A 1 67  ? 10.804  -18.726 12.903  1.00 33.17 ? 79  LYS   A CA  1 
ATOM   381  C  C   . LYS   A 1 67  ? 10.782  -17.407 12.149  1.00 35.51 ? 79  LYS   A C   1 
ATOM   382  O  O   . LYS   A 1 67  ? 10.311  -16.394 12.677  1.00 34.47 ? 79  LYS   A O   1 
ATOM   383  C  CB  . LYS   A 1 67  ? 9.383   -19.238 13.151  1.00 38.87 ? 79  LYS   A CB  1 
ATOM   384  C  CG  . LYS   A 1 67  ? 8.639   -19.672 11.897  1.00 44.80 ? 79  LYS   A CG  1 
ATOM   385  C  CD  . LYS   A 1 67  ? 9.331   -20.846 11.221  1.00 50.49 ? 79  LYS   A CD  1 
ATOM   386  C  CE  . LYS   A 1 67  ? 9.503   -22.025 12.173  1.00 48.89 ? 79  LYS   A CE  1 
ATOM   387  N  NZ  . LYS   A 1 67  ? 10.166  -23.186 11.508  1.00 51.10 ? 79  LYS   A NZ  1 
ATOM   388  N  N   . LYS   A 1 68  ? 11.295  -17.421 10.925  1.00 29.08 ? 80  LYS   A N   1 
ATOM   389  C  CA  . LYS   A 1 68  ? 11.395  -16.237 10.088  1.00 30.47 ? 80  LYS   A CA  1 
ATOM   390  C  C   . LYS   A 1 68  ? 10.281  -16.230 9.055   1.00 33.82 ? 80  LYS   A C   1 
ATOM   391  O  O   . LYS   A 1 68  ? 9.931   -17.274 8.499   1.00 35.16 ? 80  LYS   A O   1 
ATOM   392  C  CB  . LYS   A 1 68  ? 12.751  -16.200 9.381   1.00 32.06 ? 80  LYS   A CB  1 
ATOM   393  C  CG  . LYS   A 1 68  ? 12.770  -15.464 8.056   1.00 34.10 ? 80  LYS   A CG  1 
ATOM   394  C  CD  . LYS   A 1 68  ? 14.047  -15.786 7.305   1.00 34.88 ? 80  LYS   A CD  1 
ATOM   395  C  CE  . LYS   A 1 68  ? 14.117  -15.078 5.964   1.00 34.80 ? 80  LYS   A CE  1 
ATOM   396  N  NZ  . LYS   A 1 68  ? 15.439  -15.301 5.311   1.00 36.06 ? 80  LYS   A NZ  1 
ATOM   397  N  N   . ILE   A 1 69  ? 9.728   -15.047 8.798   1.00 30.98 ? 81  ILE   A N   1 
ATOM   398  C  CA  . ILE   A 1 69  ? 8.756   -14.859 7.732   1.00 31.36 ? 81  ILE   A CA  1 
ATOM   399  C  C   . ILE   A 1 69  ? 9.120   -13.616 6.937   1.00 30.60 ? 81  ILE   A C   1 
ATOM   400  O  O   . ILE   A 1 69  ? 9.673   -12.650 7.473   1.00 29.79 ? 81  ILE   A O   1 
ATOM   401  C  CB  . ILE   A 1 69  ? 7.315   -14.752 8.271   1.00 31.24 ? 81  ILE   A CB  1 
ATOM   402  C  CG1 . ILE   A 1 69  ? 7.300   -13.989 9.594   1.00 33.82 ? 81  ILE   A CG1 1 
ATOM   403  C  CG2 . ILE   A 1 69  ? 6.706   -16.129 8.435   1.00 39.19 ? 81  ILE   A CG2 1 
ATOM   404  C  CD1 . ILE   A 1 69  ? 5.921   -13.845 10.197  1.00 36.15 ? 81  ILE   A CD1 1 
ATOM   405  N  N   . ASN   A 1 70  ? 8.810   -13.650 5.645   1.00 30.40 ? 82  ASN   A N   1 
ATOM   406  C  CA  . ASN   A 1 70  ? 8.937   -12.484 4.784   1.00 31.10 ? 82  ASN   A CA  1 
ATOM   407  C  C   . ASN   A 1 70  ? 7.639   -11.689 4.827   1.00 32.31 ? 82  ASN   A C   1 
ATOM   408  O  O   . ASN   A 1 70  ? 6.559   -12.240 4.594   1.00 32.69 ? 82  ASN   A O   1 
ATOM   409  C  CB  . ASN   A 1 70  ? 9.251   -12.894 3.342   1.00 31.86 ? 82  ASN   A CB  1 
ATOM   410  C  CG  . ASN   A 1 70  ? 10.667  -13.407 3.174   1.00 35.03 ? 82  ASN   A CG  1 
ATOM   411  O  OD1 . ASN   A 1 70  ? 11.576  -13.031 3.917   1.00 36.37 ? 82  ASN   A OD1 1 
ATOM   412  N  ND2 . ASN   A 1 70  ? 10.865  -14.266 2.181   1.00 48.17 ? 82  ASN   A ND2 1 
ATOM   413  N  N   . THR   A 1 71  ? 7.749   -10.401 5.127   1.00 27.87 ? 83  THR   A N   1 
ATOM   414  C  CA  . THR   A 1 71  ? 6.620   -9.491  5.100   1.00 24.76 ? 83  THR   A CA  1 
ATOM   415  C  C   . THR   A 1 71  ? 6.599   -8.732  3.784   1.00 26.77 ? 83  THR   A C   1 
ATOM   416  O  O   . THR   A 1 71  ? 7.640   -8.509  3.167   1.00 27.65 ? 83  THR   A O   1 
ATOM   417  C  CB  . THR   A 1 71  ? 6.697   -8.478  6.243   1.00 25.29 ? 83  THR   A CB  1 
ATOM   418  O  OG1 . THR   A 1 71  ? 7.847   -7.641  6.057   1.00 23.71 ? 83  THR   A OG1 1 
ATOM   419  C  CG2 . THR   A 1 71  ? 6.782   -9.186  7.601   1.00 26.12 ? 83  THR   A CG2 1 
ATOM   420  N  N   . GLU   A 1 72  ? 5.411   -8.294  3.395   1.00 24.27 ? 84  GLU   A N   1 
ATOM   421  C  CA  . GLU   A 1 72  ? 5.165   -7.531  2.180   1.00 23.71 ? 84  GLU   A CA  1 
ATOM   422  C  C   . GLU   A 1 72  ? 4.438   -6.238  2.546   1.00 26.92 ? 84  GLU   A C   1 
ATOM   423  O  O   . GLU   A 1 72  ? 4.342   -5.856  3.719   1.00 26.67 ? 84  GLU   A O   1 
ATOM   424  C  CB  . GLU   A 1 72  ? 4.377   -8.367  1.166   1.00 30.68 ? 84  GLU   A CB  1 
ATOM   425  C  CG  . GLU   A 1 72  ? 5.182   -9.492  0.533   1.00 34.81 ? 84  GLU   A CG  1 
ATOM   426  C  CD  . GLU   A 1 72  ? 4.374   -10.303 -0.478  1.00 38.80 ? 84  GLU   A CD  1 
ATOM   427  O  OE1 . GLU   A 1 72  ? 3.334   -9.806  -0.966  1.00 38.59 ? 84  GLU   A OE1 1 
ATOM   428  O  OE2 . GLU   A 1 72  ? 4.780   -11.445 -0.784  1.00 38.37 ? 84  GLU   A OE2 1 
ATOM   429  N  N   . GLY   A 1 73  ? 3.948   -5.542  1.531   1.00 24.21 ? 85  GLY   A N   1 
ATOM   430  C  CA  . GLY   A 1 73  ? 3.213   -4.312  1.758   1.00 26.48 ? 85  GLY   A CA  1 
ATOM   431  C  C   . GLY   A 1 73  ? 4.117   -3.098  1.792   1.00 21.00 ? 85  GLY   A C   1 
ATOM   432  O  O   . GLY   A 1 73  ? 5.072   -3.036  1.017   1.00 24.11 ? 85  GLY   A O   1 
ATOM   433  N  N   . ASP   A 1 74  ? 3.818   -2.122  2.659   1.00 19.79 ? 86  ASP   A N   1 
ATOM   434  C  CA  . ASP   A 1 74  ? 4.657   -0.934  2.845   1.00 17.95 ? 86  ASP   A CA  1 
ATOM   435  C  C   . ASP   A 1 74  ? 5.781   -1.267  3.828   1.00 20.36 ? 86  ASP   A C   1 
ATOM   436  O  O   . ASP   A 1 74  ? 5.840   -0.756  4.952   1.00 18.81 ? 86  ASP   A O   1 
ATOM   437  C  CB  . ASP   A 1 74  ? 3.849   0.244   3.373   1.00 20.26 ? 86  ASP   A CB  1 
ATOM   438  C  CG  . ASP   A 1 74  ? 2.563   0.482   2.618   1.00 22.86 ? 86  ASP   A CG  1 
ATOM   439  O  OD1 . ASP   A 1 74  ? 2.512   0.239   1.387   1.00 23.51 ? 86  ASP   A OD1 1 
ATOM   440  O  OD2 . ASP   A 1 74  ? 1.601   0.932   3.274   1.00 18.41 ? 86  ASP   A OD2 1 
ATOM   441  N  N   . VAL   A 1 75  ? 6.674   -2.149  3.386   1.00 19.44 ? 87  VAL   A N   1 
ATOM   442  C  CA  . VAL   A 1 75  ? 7.756   -2.593  4.271   1.00 21.60 ? 87  VAL   A CA  1 
ATOM   443  C  C   . VAL   A 1 75  ? 8.591   -1.384  4.673   1.00 20.39 ? 87  VAL   A C   1 
ATOM   444  O  O   . VAL   A 1 75  ? 9.043   -0.623  3.798   1.00 17.66 ? 87  VAL   A O   1 
ATOM   445  C  CB  . VAL   A 1 75  ? 8.628   -3.652  3.578   1.00 22.23 ? 87  VAL   A CB  1 
ATOM   446  C  CG1 . VAL   A 1 75  ? 9.623   -4.253  4.574   1.00 19.39 ? 87  VAL   A CG1 1 
ATOM   447  C  CG2 . VAL   A 1 75  ? 7.754   -4.730  2.944   1.00 19.72 ? 87  VAL   A CG2 1 
ATOM   448  N  N   . PRO   A 1 76  ? 8.815   -1.136  5.959   1.00 20.16 ? 88  PRO   A N   1 
ATOM   449  C  CA  . PRO   A 1 76  ? 9.598   0.032   6.338   1.00 15.95 ? 88  PRO   A CA  1 
ATOM   450  C  C   . PRO   A 1 76  ? 11.040  -0.136  5.894   1.00 16.58 ? 88  PRO   A C   1 
ATOM   451  O  O   . PRO   A 1 76  ? 11.501  -1.269  5.685   1.00 16.98 ? 88  PRO   A O   1 
ATOM   452  C  CB  . PRO   A 1 76  ? 9.464   0.074   7.874   1.00 20.79 ? 88  PRO   A CB  1 
ATOM   453  C  CG  . PRO   A 1 76  ? 9.100   -1.305  8.271   1.00 19.16 ? 88  PRO   A CG  1 
ATOM   454  C  CD  . PRO   A 1 76  ? 8.331   -1.899  7.125   1.00 18.07 ? 88  PRO   A CD  1 
ATOM   455  N  N   . PRO   A 1 77  ? 11.761  0.965   5.674   1.00 17.05 ? 89  PRO   A N   1 
ATOM   456  C  CA  . PRO   A 1 77  ? 13.196  0.870   5.372   1.00 18.40 ? 89  PRO   A CA  1 
ATOM   457  C  C   . PRO   A 1 77  ? 13.957  0.175   6.488   1.00 17.90 ? 89  PRO   A C   1 
ATOM   458  O  O   . PRO   A 1 77  ? 13.500  0.096   7.633   1.00 15.78 ? 89  PRO   A O   1 
ATOM   459  C  CB  . PRO   A 1 77  ? 13.633  2.334   5.248   1.00 21.48 ? 89  PRO   A CB  1 
ATOM   460  C  CG  . PRO   A 1 77  ? 12.627  3.106   5.969   1.00 15.21 ? 89  PRO   A CG  1 
ATOM   461  C  CD  . PRO   A 1 77  ? 11.321  2.364   5.794   1.00 17.08 ? 89  PRO   A CD  1 
ATOM   462  N  N   . SER   A 1 78  ? 15.117  -0.374  6.124   1.00 20.34 ? 90  SER   A N   1 
ATOM   463  C  CA  . SER   A 1 78  ? 16.005  -0.958  7.120   1.00 16.62 ? 90  SER   A CA  1 
ATOM   464  C  C   . SER   A 1 78  ? 16.448  0.128   8.090   1.00 19.28 ? 90  SER   A C   1 
ATOM   465  O  O   . SER   A 1 78  ? 16.893  1.200   7.667   1.00 17.82 ? 90  SER   A O   1 
ATOM   466  C  CB  . SER   A 1 78  ? 17.223  -1.585  6.440   1.00 22.33 ? 90  SER   A CB  1 
ATOM   467  O  OG  . SER   A 1 78  ? 16.932  -2.855  5.882   1.00 26.85 ? 90  SER   A OG  1 
ATOM   468  N  N   . MET   A 1 79  ? 16.315  -0.135  9.398   1.00 18.28 ? 91  MET   A N   1 
ATOM   469  C  CA  . MET   A 1 79  ? 16.528  0.940   10.358  1.00 19.30 ? 91  MET   A CA  1 
ATOM   470  C  C   . MET   A 1 79  ? 17.123  0.441   11.659  1.00 16.62 ? 91  MET   A C   1 
ATOM   471  O  O   . MET   A 1 79  ? 16.827  -0.662  12.123  1.00 18.23 ? 91  MET   A O   1 
ATOM   472  C  CB  . MET   A 1 79  ? 15.236  1.690   10.705  1.00 14.49 ? 91  MET   A CB  1 
ATOM   473  C  CG  . MET   A 1 79  ? 14.704  2.509   9.544   1.00 15.79 ? 91  MET   A CG  1 
ATOM   474  S  SD  . MET   A 1 79  ? 13.325  3.600   9.936   1.00 17.10 ? 91  MET   A SD  1 
ATOM   475  C  CE  . MET   A 1 79  ? 11.996  2.405   10.143  1.00 18.09 ? 91  MET   A CE  1 
ATOM   476  N  N   . SER   A 1 80  ? 17.903  1.311   12.275  1.00 15.79 ? 92  SER   A N   1 
ATOM   477  C  CA  . SER   A 1 80  ? 18.250  1.171   13.684  1.00 14.55 ? 92  SER   A CA  1 
ATOM   478  C  C   . SER   A 1 80  ? 17.506  2.229   14.488  1.00 12.67 ? 92  SER   A C   1 
ATOM   479  O  O   . SER   A 1 80  ? 17.140  3.284   13.961  1.00 13.29 ? 92  SER   A O   1 
ATOM   480  C  CB  . SER   A 1 80  ? 19.765  1.297   13.898  1.00 15.18 ? 92  SER   A CB  1 
ATOM   481  O  OG  . SER   A 1 80  ? 20.213  2.602   13.561  1.00 15.19 ? 92  SER   A OG  1 
ATOM   482  N  N   . GLY   A 1 81  ? 17.279  1.936   15.771  1.00 12.80 ? 93  GLY   A N   1 
ATOM   483  C  CA  . GLY   A 1 81  ? 16.722  2.926   16.685  1.00 12.11 ? 93  GLY   A CA  1 
ATOM   484  C  C   . GLY   A 1 81  ? 15.232  3.164   16.572  1.00 11.23 ? 93  GLY   A C   1 
ATOM   485  O  O   . GLY   A 1 81  ? 14.720  4.122   17.173  1.00 9.05  ? 93  GLY   A O   1 
ATOM   486  N  N   . SER   A 1 82  ? 14.517  2.318   15.834  1.00 13.28 ? 94  SER   A N   1 
ATOM   487  C  CA  . SER   A 1 82  ? 13.079  2.479   15.729  1.00 13.99 ? 94  SER   A CA  1 
ATOM   488  C  C   . SER   A 1 82  ? 12.413  2.133   17.057  1.00 13.99 ? 94  SER   A C   1 
ATOM   489  O  O   . SER   A 1 82  ? 13.000  1.479   17.923  1.00 13.84 ? 94  SER   A O   1 
ATOM   490  C  CB  . SER   A 1 82  ? 12.500  1.597   14.632  1.00 13.19 ? 94  SER   A CB  1 
ATOM   491  O  OG  . SER   A 1 82  ? 12.829  2.083   13.338  1.00 14.79 ? 94  SER   A OG  1 
ATOM   492  N  N   . CYS   A 1 83  ? 11.150  2.554   17.186  1.00 13.23 ? 95  CYS   A N   1 
ATOM   493  C  CA  . CYS   A 1 83  ? 10.374  2.421   18.418  1.00 14.54 ? 95  CYS   A CA  1 
ATOM   494  C  C   . CYS   A 1 83  ? 9.101   1.657   18.105  1.00 15.45 ? 95  CYS   A C   1 
ATOM   495  O  O   . CYS   A 1 83  ? 8.305   2.110   17.279  1.00 15.59 ? 95  CYS   A O   1 
ATOM   496  C  CB  . CYS   A 1 83  ? 10.025  3.787   18.999  1.00 11.91 ? 95  CYS   A CB  1 
ATOM   497  S  SG  . CYS   A 1 83  ? 9.272   3.673   20.670  1.00 18.45 ? 95  CYS   A SG  1 
ATOM   498  N  N   . ALA   A 1 84  ? 8.891   0.517   18.775  1.00 15.74 ? 96  ALA   A N   1 
ATOM   499  C  CA  . ALA   A 1 84  ? 7.793   -0.379  18.413  1.00 13.30 ? 96  ALA   A CA  1 
ATOM   500  C  C   . ALA   A 1 84  ? 6.991   -0.821  19.631  1.00 19.33 ? 96  ALA   A C   1 
ATOM   501  O  O   . ALA   A 1 84  ? 7.495   -0.846  20.758  1.00 19.56 ? 96  ALA   A O   1 
ATOM   502  C  CB  . ALA   A 1 84  ? 8.303   -1.621  17.693  1.00 16.18 ? 96  ALA   A CB  1 
ATOM   503  N  N   . VAL   A 1 85  ? 5.722   -1.157  19.375  1.00 20.72 ? 97  VAL   A N   1 
ATOM   504  C  CA  . VAL   A 1 85  ? 4.802   -1.690  20.373  1.00 18.44 ? 97  VAL   A CA  1 
ATOM   505  C  C   . VAL   A 1 85  ? 4.036   -2.856  19.775  1.00 20.36 ? 97  VAL   A C   1 
ATOM   506  O  O   . VAL   A 1 85  ? 3.899   -2.990  18.555  1.00 21.53 ? 97  VAL   A O   1 
ATOM   507  C  CB  . VAL   A 1 85  ? 3.798   -0.634  20.875  1.00 22.47 ? 97  VAL   A CB  1 
ATOM   508  C  CG1 . VAL   A 1 85  ? 4.501   0.485   21.568  1.00 21.61 ? 97  VAL   A CG1 1 
ATOM   509  C  CG2 . VAL   A 1 85  ? 2.959   -0.102  19.713  1.00 22.92 ? 97  VAL   A CG2 1 
ATOM   510  N  N   . CYS   A 1 86  ? 3.507   -3.699  20.653  1.00 21.89 ? 98  CYS   A N   1 
ATOM   511  C  CA  . CYS   A 1 86  ? 2.544   -4.715  20.253  1.00 18.66 ? 98  CYS   A CA  1 
ATOM   512  C  C   . CYS   A 1 86  ? 1.302   -4.546  21.106  1.00 21.15 ? 98  CYS   A C   1 
ATOM   513  O  O   . CYS   A 1 86  ? 1.383   -4.655  22.330  1.00 22.09 ? 98  CYS   A O   1 
ATOM   514  C  CB  . CYS   A 1 86  ? 3.122   -6.121  20.419  1.00 20.86 ? 98  CYS   A CB  1 
ATOM   515  S  SG  . CYS   A 1 86  ? 1.929   -7.407  20.062  1.00 30.48 ? 98  CYS   A SG  1 
ATOM   516  N  N   . VAL   A 1 87  ? 0.164   -4.268  20.471  1.00 23.54 ? 99  VAL   A N   1 
ATOM   517  C  CA  . VAL   A 1 87  ? -1.111  -4.102  21.165  1.00 22.90 ? 99  VAL   A CA  1 
ATOM   518  C  C   . VAL   A 1 87  ? -2.116  -5.030  20.502  1.00 27.27 ? 99  VAL   A C   1 
ATOM   519  O  O   . VAL   A 1 87  ? -2.459  -4.833  19.335  1.00 23.55 ? 99  VAL   A O   1 
ATOM   520  C  CB  . VAL   A 1 87  ? -1.621  -2.650  21.126  1.00 23.73 ? 99  VAL   A CB  1 
ATOM   521  C  CG1 . VAL   A 1 87  ? -2.808  -2.477  22.074  1.00 25.97 ? 99  VAL   A CG1 1 
ATOM   522  C  CG2 . VAL   A 1 87  ? -0.515  -1.671  21.456  1.00 22.36 ? 99  VAL   A CG2 1 
ATOM   523  N  N   . ASP   A 1 88  ? -2.597  -6.028  21.245  1.00 30.88 ? 100 ASP   A N   1 
ATOM   524  C  CA  . ASP   A 1 88  ? -3.533  -7.019  20.704  1.00 28.68 ? 100 ASP   A CA  1 
ATOM   525  C  C   . ASP   A 1 88  ? -3.033  -7.576  19.366  1.00 26.99 ? 100 ASP   A C   1 
ATOM   526  O  O   . ASP   A 1 88  ? -3.743  -7.575  18.354  1.00 28.81 ? 100 ASP   A O   1 
ATOM   527  C  CB  . ASP   A 1 88  ? -4.944  -6.431  20.558  1.00 29.82 ? 100 ASP   A CB  1 
ATOM   528  C  CG  . ASP   A 1 88  ? -5.541  -5.983  21.884  1.00 35.35 ? 100 ASP   A CG  1 
ATOM   529  O  OD1 . ASP   A 1 88  ? -4.776  -5.648  22.810  1.00 37.15 ? 100 ASP   A OD1 1 
ATOM   530  O  OD2 . ASP   A 1 88  ? -6.785  -5.975  22.001  1.00 43.77 ? 100 ASP   A OD2 1 
ATOM   531  N  N   . ARG   A 1 89  ? -1.779  -8.033  19.365  1.00 25.77 ? 101 ARG   A N   1 
ATOM   532  C  CA  . ARG   A 1 89  ? -1.117  -8.645  18.206  1.00 30.74 ? 101 ARG   A CA  1 
ATOM   533  C  C   . ARG   A 1 89  ? -1.081  -7.738  16.975  1.00 27.82 ? 101 ARG   A C   1 
ATOM   534  O  O   . ARG   A 1 89  ? -0.835  -8.209  15.852  1.00 29.34 ? 101 ARG   A O   1 
ATOM   535  C  CB  . ARG   A 1 89  ? -1.747  -9.995  17.849  1.00 32.91 ? 101 ARG   A CB  1 
ATOM   536  C  CG  . ARG   A 1 89  ? -1.588  -11.028 18.950  1.00 36.52 ? 101 ARG   A CG  1 
ATOM   537  C  CD  . ARG   A 1 89  ? -2.247  -12.360 18.595  1.00 35.76 ? 101 ARG   A CD  1 
ATOM   538  N  NE  . ARG   A 1 89  ? -1.756  -12.925 17.343  1.00 37.98 ? 101 ARG   A NE  1 
ATOM   539  C  CZ  . ARG   A 1 89  ? -0.518  -13.364 17.146  1.00 36.72 ? 101 ARG   A CZ  1 
ATOM   540  N  NH1 . ARG   A 1 89  ? 0.414   -13.259 18.082  1.00 39.67 ? 101 ARG   A NH1 1 
ATOM   541  N  NH2 . ARG   A 1 89  ? -0.206  -13.923 15.980  1.00 36.14 ? 101 ARG   A NH2 1 
ATOM   542  N  N   . VAL   A 1 90  ? -1.294  -6.439  17.149  1.00 24.06 ? 102 VAL   A N   1 
ATOM   543  C  CA  . VAL   A 1 90  ? -1.015  -5.464  16.106  1.00 24.96 ? 102 VAL   A CA  1 
ATOM   544  C  C   . VAL   A 1 90  ? 0.274   -4.743  16.468  1.00 23.62 ? 102 VAL   A C   1 
ATOM   545  O  O   . VAL   A 1 90  ? 0.422   -4.235  17.587  1.00 22.76 ? 102 VAL   A O   1 
ATOM   546  C  CB  . VAL   A 1 90  ? -2.180  -4.475  15.931  1.00 25.98 ? 102 VAL   A CB  1 
ATOM   547  C  CG1 . VAL   A 1 90  ? -1.841  -3.480  14.845  1.00 22.79 ? 102 VAL   A CG1 1 
ATOM   548  C  CG2 . VAL   A 1 90  ? -3.469  -5.227  15.602  1.00 25.36 ? 102 VAL   A CG2 1 
ATOM   549  N  N   . LEU   A 1 91  ? 1.222   -4.728  15.541  1.00 22.98 ? 103 LEU   A N   1 
ATOM   550  C  CA  . LEU   A 1 91  ? 2.529   -4.125  15.780  1.00 22.10 ? 103 LEU   A CA  1 
ATOM   551  C  C   . LEU   A 1 91  ? 2.526   -2.729  15.181  1.00 22.58 ? 103 LEU   A C   1 
ATOM   552  O  O   . LEU   A 1 91  ? 2.077   -2.544  14.050  1.00 21.45 ? 103 LEU   A O   1 
ATOM   553  C  CB  . LEU   A 1 91  ? 3.656   -4.943  15.153  1.00 19.03 ? 103 LEU   A CB  1 
ATOM   554  C  CG  . LEU   A 1 91  ? 3.583   -6.464  15.179  1.00 26.53 ? 103 LEU   A CG  1 
ATOM   555  C  CD1 . LEU   A 1 91  ? 4.898   -7.038  14.645  1.00 28.24 ? 103 LEU   A CD1 1 
ATOM   556  C  CD2 . LEU   A 1 91  ? 3.302   -6.957  16.597  1.00 27.93 ? 103 LEU   A CD2 1 
ATOM   557  N  N   . TYR   A 1 92  ? 3.006   -1.753  15.938  1.00 20.66 ? 104 TYR   A N   1 
ATOM   558  C  CA  . TYR   A 1 92  ? 3.127   -0.390  15.444  1.00 19.65 ? 104 TYR   A CA  1 
ATOM   559  C  C   . TYR   A 1 92  ? 4.583   0.028   15.548  1.00 19.50 ? 104 TYR   A C   1 
ATOM   560  O  O   . TYR   A 1 92  ? 5.237   -0.263  16.553  1.00 18.35 ? 104 TYR   A O   1 
ATOM   561  C  CB  . TYR   A 1 92  ? 2.259   0.577   16.244  1.00 17.28 ? 104 TYR   A CB  1 
ATOM   562  C  CG  . TYR   A 1 92  ? 0.788   0.215   16.297  1.00 20.71 ? 104 TYR   A CG  1 
ATOM   563  C  CD1 . TYR   A 1 92  ? -0.045  0.437   15.204  1.00 21.55 ? 104 TYR   A CD1 1 
ATOM   564  C  CD2 . TYR   A 1 92  ? 0.237   -0.336  17.445  1.00 21.98 ? 104 TYR   A CD2 1 
ATOM   565  C  CE1 . TYR   A 1 92  ? -1.395  0.113   15.257  1.00 17.64 ? 104 TYR   A CE1 1 
ATOM   566  C  CE2 . TYR   A 1 92  ? -1.110  -0.657  17.512  1.00 22.48 ? 104 TYR   A CE2 1 
ATOM   567  C  CZ  . TYR   A 1 92  ? -1.917  -0.434  16.413  1.00 23.70 ? 104 TYR   A CZ  1 
ATOM   568  O  OH  . TYR   A 1 92  ? -3.252  -0.757  16.499  1.00 25.18 ? 104 TYR   A OH  1 
ATOM   569  N  N   . LEU   A 1 93  ? 5.076   0.717   14.515  1.00 15.68 ? 105 LEU   A N   1 
ATOM   570  C  CA  . LEU   A 1 93  ? 6.483   1.108   14.398  1.00 12.60 ? 105 LEU   A CA  1 
ATOM   571  C  C   . LEU   A 1 93  ? 6.580   2.601   14.128  1.00 10.96 ? 105 LEU   A C   1 
ATOM   572  O  O   . LEU   A 1 93  ? 5.938   3.099   13.199  1.00 15.62 ? 105 LEU   A O   1 
ATOM   573  C  CB  . LEU   A 1 93  ? 7.181   0.355   13.267  1.00 14.24 ? 105 LEU   A CB  1 
ATOM   574  C  CG  . LEU   A 1 93  ? 8.713   0.455   13.321  1.00 16.27 ? 105 LEU   A CG  1 
ATOM   575  C  CD1 . LEU   A 1 93  ? 9.193   -0.697  14.145  1.00 18.25 ? 105 LEU   A CD1 1 
ATOM   576  C  CD2 . LEU   A 1 93  ? 9.325   0.398   11.947  1.00 21.90 ? 105 LEU   A CD2 1 
ATOM   577  N  N   . PHE   A 1 94  ? 7.383   3.313   14.926  1.00 10.98 ? 106 PHE   A N   1 
ATOM   578  C  CA  . PHE   A 1 94  ? 7.619   4.729   14.700  1.00 12.38 ? 106 PHE   A CA  1 
ATOM   579  C  C   . PHE   A 1 94  ? 9.105   5.060   14.638  1.00 12.78 ? 106 PHE   A C   1 
ATOM   580  O  O   . PHE   A 1 94  ? 9.888   4.583   15.460  1.00 13.95 ? 106 PHE   A O   1 
ATOM   581  C  CB  . PHE   A 1 94  ? 6.995   5.598   15.777  1.00 12.70 ? 106 PHE   A CB  1 
ATOM   582  C  CG  . PHE   A 1 94  ? 7.394   7.026   15.671  1.00 12.36 ? 106 PHE   A CG  1 
ATOM   583  C  CD1 . PHE   A 1 94  ? 6.775   7.851   14.739  1.00 13.78 ? 106 PHE   A CD1 1 
ATOM   584  C  CD2 . PHE   A 1 94  ? 8.438   7.546   16.457  1.00 12.19 ? 106 PHE   A CD2 1 
ATOM   585  C  CE1 . PHE   A 1 94  ? 7.150   9.164   14.599  1.00 16.21 ? 106 PHE   A CE1 1 
ATOM   586  C  CE2 . PHE   A 1 94  ? 8.824   8.875   16.325  1.00 15.36 ? 106 PHE   A CE2 1 
ATOM   587  C  CZ  . PHE   A 1 94  ? 8.191   9.685   15.390  1.00 18.12 ? 106 PHE   A CZ  1 
ATOM   588  N  N   . GLY   A 1 95  ? 9.474   5.930   13.684  1.00 14.55 ? 107 GLY   A N   1 
ATOM   589  C  CA  . GLY   A 1 95  ? 10.826  6.506   13.682  1.00 13.21 ? 107 GLY   A CA  1 
ATOM   590  C  C   . GLY   A 1 95  ? 11.922  5.488   13.403  1.00 14.51 ? 107 GLY   A C   1 
ATOM   591  O  O   . GLY   A 1 95  ? 11.689  4.370   12.919  1.00 16.93 ? 107 GLY   A O   1 
ATOM   592  N  N   . GLY   A 1 96  ? 13.150  5.913   13.691  1.00 11.68 ? 108 GLY   A N   1 
ATOM   593  C  CA  . GLY   A 1 96  ? 14.342  5.147   13.389  1.00 15.23 ? 108 GLY   A CA  1 
ATOM   594  C  C   . GLY   A 1 96  ? 15.304  5.913   12.491  1.00 12.47 ? 108 GLY   A C   1 
ATOM   595  O  O   . GLY   A 1 96  ? 15.109  7.084   12.174  1.00 13.88 ? 108 GLY   A O   1 
ATOM   596  N  N   . HIS   A 1 97  ? 16.390  5.232   12.130  1.00 14.08 ? 109 HIS   A N   1 
ATOM   597  C  CA  . HIS   A 1 97  ? 17.437  5.771   11.264  1.00 16.05 ? 109 HIS   A CA  1 
ATOM   598  C  C   . HIS   A 1 97  ? 17.665  4.782   10.129  1.00 18.42 ? 109 HIS   A C   1 
ATOM   599  O  O   . HIS   A 1 97  ? 18.026  3.630   10.386  1.00 17.07 ? 109 HIS   A O   1 
ATOM   600  C  CB  . HIS   A 1 97  ? 18.742  5.979   12.054  1.00 13.72 ? 109 HIS   A CB  1 
ATOM   601  C  CG  . HIS   A 1 97  ? 19.852  6.568   11.249  1.00 15.08 ? 109 HIS   A CG  1 
ATOM   602  N  ND1 . HIS   A 1 97  ? 20.691  5.808   10.464  1.00 16.13 ? 109 HIS   A ND1 1 
ATOM   603  C  CD2 . HIS   A 1 97  ? 20.254  7.852   11.097  1.00 18.17 ? 109 HIS   A CD2 1 
ATOM   604  C  CE1 . HIS   A 1 97  ? 21.559  6.596   9.861   1.00 14.82 ? 109 HIS   A CE1 1 
ATOM   605  N  NE2 . HIS   A 1 97  ? 21.314  7.842   10.224  1.00 20.68 ? 109 HIS   A NE2 1 
ATOM   606  N  N   . HIS   A 1 98  ? 17.454  5.217   8.879   1.00 14.55 ? 110 HIS   A N   1 
ATOM   607  C  CA  . HIS   A 1 98  ? 17.750  4.396   7.708   1.00 13.37 ? 110 HIS   A CA  1 
ATOM   608  C  C   . HIS   A 1 98  ? 18.948  4.993   6.965   1.00 17.82 ? 110 HIS   A C   1 
ATOM   609  O  O   . HIS   A 1 98  ? 19.659  5.869   7.485   1.00 17.99 ? 110 HIS   A O   1 
ATOM   610  C  CB  . HIS   A 1 98  ? 16.508  4.256   6.809   1.00 14.94 ? 110 HIS   A CB  1 
ATOM   611  C  CG  . HIS   A 1 98  ? 15.867  5.559   6.464   1.00 18.24 ? 110 HIS   A CG  1 
ATOM   612  N  ND1 . HIS   A 1 98  ? 16.445  6.462   5.603   1.00 19.07 ? 110 HIS   A ND1 1 
ATOM   613  C  CD2 . HIS   A 1 98  ? 14.701  6.114   6.868   1.00 18.16 ? 110 HIS   A CD2 1 
ATOM   614  C  CE1 . HIS   A 1 98  ? 15.657  7.514   5.479   1.00 20.50 ? 110 HIS   A CE1 1 
ATOM   615  N  NE2 . HIS   A 1 98  ? 14.595  7.333   6.243   1.00 16.75 ? 110 HIS   A NE2 1 
ATOM   616  N  N   . SER   A 1 99  ? 19.223  4.462   5.770   1.00 22.94 ? 111 SER   A N   1 
ATOM   617  C  CA  . SER   A 1 99  ? 20.424  4.859   5.034   1.00 20.98 ? 111 SER   A CA  1 
ATOM   618  C  C   . SER   A 1 99  ? 20.468  6.361   4.746   1.00 23.11 ? 111 SER   A C   1 
ATOM   619  O  O   . SER   A 1 99  ? 21.555  6.959   4.742   1.00 23.55 ? 111 SER   A O   1 
ATOM   620  C  CB  . SER   A 1 99  ? 20.530  4.056   3.729   1.00 23.51 ? 111 SER   A CB  1 
ATOM   621  O  OG  . SER   A 1 99  ? 19.377  4.188   2.910   1.00 26.80 ? 111 SER   A OG  1 
ATOM   622  N  N   . ARG   A 1 100 ? 19.315  6.986   4.506   1.00 17.43 ? 112 ARG   A N   1 
ATOM   623  C  CA  . ARG   A 1 100 ? 19.238  8.406   4.192   1.00 17.24 ? 112 ARG   A CA  1 
ATOM   624  C  C   . ARG   A 1 100 ? 18.809  9.269   5.379   1.00 19.01 ? 112 ARG   A C   1 
ATOM   625  O  O   . ARG   A 1 100 ? 18.464  10.438  5.186   1.00 24.44 ? 112 ARG   A O   1 
ATOM   626  C  CB  . ARG   A 1 100 ? 18.291  8.628   3.008   1.00 22.54 ? 112 ARG   A CB  1 
ATOM   627  N  N   . GLY   A 1 101 ? 18.804  8.725   6.600   1.00 20.07 ? 113 GLY   A N   1 
ATOM   628  C  CA  . GLY   A 1 101 ? 18.596  9.563   7.763   1.00 15.44 ? 113 GLY   A CA  1 
ATOM   629  C  C   . GLY   A 1 101 ? 17.488  9.051   8.656   1.00 15.82 ? 113 GLY   A C   1 
ATOM   630  O  O   . GLY   A 1 101 ? 17.083  7.883   8.580   1.00 15.99 ? 113 GLY   A O   1 
ATOM   631  N  N   . ASN   A 1 102 ? 17.017  9.941   9.538   1.00 16.54 ? 114 ASN   A N   1 
ATOM   632  C  CA  . ASN   A 1 102 ? 15.923  9.613   10.443  1.00 17.72 ? 114 ASN   A CA  1 
ATOM   633  C  C   . ASN   A 1 102 ? 14.568  9.760   9.757   1.00 19.23 ? 114 ASN   A C   1 
ATOM   634  O  O   . ASN   A 1 102 ? 14.432  10.367  8.687   1.00 22.78 ? 114 ASN   A O   1 
ATOM   635  C  CB  . ASN   A 1 102 ? 15.945  10.503  11.678  1.00 15.48 ? 114 ASN   A CB  1 
ATOM   636  C  CG  . ASN   A 1 102 ? 17.136  10.238  12.564  1.00 19.16 ? 114 ASN   A CG  1 
ATOM   637  O  OD1 . ASN   A 1 102 ? 17.980  11.099  12.716  1.00 19.95 ? 114 ASN   A OD1 1 
ATOM   638  N  ND2 . ASN   A 1 102 ? 17.202  9.046   13.155  1.00 16.36 ? 114 ASN   A ND2 1 
ATOM   639  N  N   . THR   A 1 103 ? 13.541  9.221   10.414  1.00 16.08 ? 115 THR   A N   1 
ATOM   640  C  CA  . THR   A 1 103 ? 12.186  9.308   9.884   1.00 15.73 ? 115 THR   A CA  1 
ATOM   641  C  C   . THR   A 1 103 ? 11.215  9.561   11.031  1.00 14.47 ? 115 THR   A C   1 
ATOM   642  O  O   . THR   A 1 103 ? 11.533  9.348   12.202  1.00 14.44 ? 115 THR   A O   1 
ATOM   643  C  CB  . THR   A 1 103 ? 11.784  8.038   9.110   1.00 18.27 ? 115 THR   A CB  1 
ATOM   644  O  OG1 . THR   A 1 103 ? 10.485  8.213   8.537   1.00 20.54 ? 115 THR   A OG1 1 
ATOM   645  C  CG2 . THR   A 1 103 ? 11.743  6.847   10.012  1.00 15.61 ? 115 THR   A CG2 1 
ATOM   646  N  N   . ASN   A 1 104 ? 10.034  10.066  10.668  1.00 16.86 ? 116 ASN   A N   1 
ATOM   647  C  CA  . ASN   A 1 104 ? 8.890   10.132  11.565  1.00 18.78 ? 116 ASN   A CA  1 
ATOM   648  C  C   . ASN   A 1 104 ? 7.671   9.432   10.972  1.00 15.43 ? 116 ASN   A C   1 
ATOM   649  O  O   . ASN   A 1 104 ? 6.550   9.764   11.337  1.00 19.19 ? 116 ASN   A O   1 
ATOM   650  C  CB  . ASN   A 1 104 ? 8.539   11.579  11.943  1.00 18.79 ? 116 ASN   A CB  1 
ATOM   651  C  CG  . ASN   A 1 104 ? 8.207   12.458  10.746  1.00 20.41 ? 116 ASN   A CG  1 
ATOM   652  O  OD1 . ASN   A 1 104 ? 7.976   11.978  9.630   1.00 22.21 ? 116 ASN   A OD1 1 
ATOM   653  N  ND2 . ASN   A 1 104 ? 8.163   13.760  10.980  1.00 19.01 ? 116 ASN   A ND2 1 
ATOM   654  N  N   . LYS   A 1 105 ? 7.875   8.469   10.065  1.00 19.98 ? 117 LYS   A N   1 
ATOM   655  C  CA  . LYS   A 1 105 ? 6.778   7.683   9.526   1.00 23.58 ? 117 LYS   A CA  1 
ATOM   656  C  C   . LYS   A 1 105 ? 6.306   6.648   10.541  1.00 20.39 ? 117 LYS   A C   1 
ATOM   657  O  O   . LYS   A 1 105 ? 7.052   6.209   11.427  1.00 15.64 ? 117 LYS   A O   1 
ATOM   658  C  CB  . LYS   A 1 105 ? 7.181   6.981   8.228   1.00 20.37 ? 117 LYS   A CB  1 
ATOM   659  C  CG  . LYS   A 1 105 ? 7.503   7.907   7.064   1.00 20.67 ? 117 LYS   A CG  1 
ATOM   660  C  CD  . LYS   A 1 105 ? 6.366   8.854   6.731   1.00 23.09 ? 117 LYS   A CD  1 
ATOM   661  C  CE  . LYS   A 1 105 ? 6.791   9.844   5.639   1.00 29.22 ? 117 LYS   A CE  1 
ATOM   662  N  NZ  . LYS   A 1 105 ? 5.892   11.049  5.563   1.00 29.35 ? 117 LYS   A NZ  1 
ATOM   663  N  N   . PHE   A 1 106 ? 5.043   6.257   10.391  1.00 16.42 ? 118 PHE   A N   1 
ATOM   664  C  CA  . PHE   A 1 106 ? 4.360   5.356   11.309  1.00 19.62 ? 118 PHE   A CA  1 
ATOM   665  C  C   . PHE   A 1 106 ? 3.832   4.170   10.519  1.00 18.95 ? 118 PHE   A C   1 
ATOM   666  O  O   . PHE   A 1 106 ? 3.134   4.358   9.518   1.00 19.71 ? 118 PHE   A O   1 
ATOM   667  C  CB  . PHE   A 1 106 ? 3.215   6.099   12.018  1.00 17.18 ? 118 PHE   A CB  1 
ATOM   668  C  CG  . PHE   A 1 106 ? 2.515   5.295   13.071  1.00 18.72 ? 118 PHE   A CG  1 
ATOM   669  C  CD1 . PHE   A 1 106 ? 1.500   4.412   12.726  1.00 18.45 ? 118 PHE   A CD1 1 
ATOM   670  C  CD2 . PHE   A 1 106 ? 2.858   5.432   14.414  1.00 17.68 ? 118 PHE   A CD2 1 
ATOM   671  C  CE1 . PHE   A 1 106 ? 0.852   3.672   13.684  1.00 20.68 ? 118 PHE   A CE1 1 
ATOM   672  C  CE2 . PHE   A 1 106 ? 2.189   4.695   15.391  1.00 21.30 ? 118 PHE   A CE2 1 
ATOM   673  C  CZ  . PHE   A 1 106 ? 1.190   3.818   15.024  1.00 20.80 ? 118 PHE   A CZ  1 
ATOM   674  N  N   . TYR   A 1 107 ? 4.176   2.955   10.949  1.00 16.01 ? 119 TYR   A N   1 
ATOM   675  C  CA  . TYR   A 1 107 ? 3.706   1.753   10.278  1.00 19.19 ? 119 TYR   A CA  1 
ATOM   676  C  C   . TYR   A 1 107 ? 2.939   0.858   11.239  1.00 19.36 ? 119 TYR   A C   1 
ATOM   677  O  O   . TYR   A 1 107 ? 3.106   0.916   12.460  1.00 16.85 ? 119 TYR   A O   1 
ATOM   678  C  CB  . TYR   A 1 107 ? 4.850   0.938   9.660   1.00 18.43 ? 119 TYR   A CB  1 
ATOM   679  C  CG  . TYR   A 1 107 ? 5.724   1.678   8.679   1.00 16.66 ? 119 TYR   A CG  1 
ATOM   680  C  CD1 . TYR   A 1 107 ? 6.705   2.536   9.128   1.00 18.80 ? 119 TYR   A CD1 1 
ATOM   681  C  CD2 . TYR   A 1 107 ? 5.604   1.479   7.316   1.00 15.97 ? 119 TYR   A CD2 1 
ATOM   682  C  CE1 . TYR   A 1 107 ? 7.510   3.204   8.269   1.00 18.11 ? 119 TYR   A CE1 1 
ATOM   683  C  CE2 . TYR   A 1 107 ? 6.418   2.155   6.439   1.00 21.35 ? 119 TYR   A CE2 1 
ATOM   684  C  CZ  . TYR   A 1 107 ? 7.381   3.016   6.932   1.00 18.62 ? 119 TYR   A CZ  1 
ATOM   685  O  OH  . TYR   A 1 107 ? 8.213   3.702   6.077   1.00 19.82 ? 119 TYR   A OH  1 
ATOM   686  N  N   . MET   A 1 108 ? 2.097   0.018   10.657  1.00 21.71 ? 120 MET   A N   1 
ATOM   687  C  CA  . MET   A 1 108 ? 1.340   -0.993  11.376  1.00 17.82 ? 120 MET   A CA  1 
ATOM   688  C  C   . MET   A 1 108 ? 1.551   -2.335  10.696  1.00 20.07 ? 120 MET   A C   1 
ATOM   689  O  O   . MET   A 1 108 ? 1.612   -2.408  9.467   1.00 18.06 ? 120 MET   A O   1 
ATOM   690  C  CB  . MET   A 1 108 ? -0.163  -0.658  11.400  1.00 21.11 ? 120 MET   A CB  1 
ATOM   691  C  CG  . MET   A 1 108 ? -1.026  -1.795  11.924  1.00 22.69 ? 120 MET   A CG  1 
ATOM   692  S  SD  . MET   A 1 108 ? -2.794  -1.442  12.020  1.00 29.90 ? 120 MET   A SD  1 
ATOM   693  C  CE  . MET   A 1 108 ? -2.743  0.333   11.969  1.00 26.02 ? 120 MET   A CE  1 
ATOM   694  N  N   . LEU   A 1 109 ? 1.694   -3.395  11.488  1.00 20.56 ? 121 LEU   A N   1 
ATOM   695  C  CA  . LEU   A 1 109 ? 1.677   -4.748  10.946  1.00 22.39 ? 121 LEU   A CA  1 
ATOM   696  C  C   . LEU   A 1 109 ? 0.746   -5.601  11.787  1.00 26.80 ? 121 LEU   A C   1 
ATOM   697  O  O   . LEU   A 1 109 ? 1.023   -5.850  12.967  1.00 24.57 ? 121 LEU   A O   1 
ATOM   698  C  CB  . LEU   A 1 109 ? 3.074   -5.364  10.901  1.00 22.64 ? 121 LEU   A CB  1 
ATOM   699  C  CG  . LEU   A 1 109 ? 3.003   -6.592  9.980   1.00 27.65 ? 121 LEU   A CG  1 
ATOM   700  C  CD1 . LEU   A 1 109 ? 4.082   -6.565  8.927   1.00 26.45 ? 121 LEU   A CD1 1 
ATOM   701  C  CD2 . LEU   A 1 109 ? 3.064   -7.875  10.797  1.00 31.30 ? 121 LEU   A CD2 1 
ATOM   702  N  N   . ASP   A 1 110 ? -0.354  -6.044  11.183  1.00 27.93 ? 122 ASP   A N   1 
ATOM   703  C  CA  . ASP   A 1 110 ? -1.310  -6.893  11.881  1.00 29.52 ? 122 ASP   A CA  1 
ATOM   704  C  C   . ASP   A 1 110 ? -0.785  -8.325  11.864  1.00 26.91 ? 122 ASP   A C   1 
ATOM   705  O  O   . ASP   A 1 110 ? -0.695  -8.951  10.809  1.00 28.75 ? 122 ASP   A O   1 
ATOM   706  C  CB  . ASP   A 1 110 ? -2.684  -6.776  11.234  1.00 31.18 ? 122 ASP   A CB  1 
ATOM   707  C  CG  . ASP   A 1 110 ? -3.764  -7.466  12.036  1.00 34.64 ? 122 ASP   A CG  1 
ATOM   708  O  OD1 . ASP   A 1 110 ? -3.436  -8.090  13.067  1.00 36.53 ? 122 ASP   A OD1 1 
ATOM   709  O  OD2 . ASP   A 1 110 ? -4.946  -7.378  11.638  1.00 38.86 ? 122 ASP   A OD2 1 
ATOM   710  N  N   . SER   A 1 111 ? -0.404  -8.843  13.030  1.00 33.78 ? 123 SER   A N   1 
ATOM   711  C  CA  . SER   A 1 111 ? 0.116   -10.201 13.127  1.00 32.48 ? 123 SER   A CA  1 
ATOM   712  C  C   . SER   A 1 111 ? -0.964  -11.200 13.536  1.00 36.34 ? 123 SER   A C   1 
ATOM   713  O  O   . SER   A 1 111 ? -0.650  -12.263 14.080  1.00 38.94 ? 123 SER   A O   1 
ATOM   714  C  CB  . SER   A 1 111 ? 1.297   -10.255 14.096  1.00 34.05 ? 123 SER   A CB  1 
ATOM   715  O  OG  . SER   A 1 111 ? 0.869   -10.173 15.443  1.00 33.33 ? 123 SER   A OG  1 
ATOM   716  N  N   . ARG   A 1 112 ? -2.234  -10.887 13.270  1.00 34.93 ? 124 ARG   A N   1 
ATOM   717  C  CA  . ARG   A 1 112 ? -3.324  -11.772 13.674  1.00 40.75 ? 124 ARG   A CA  1 
ATOM   718  C  C   . ARG   A 1 112 ? -3.659  -12.803 12.597  1.00 46.19 ? 124 ARG   A C   1 
ATOM   719  O  O   . ARG   A 1 112 ? -3.555  -14.009 12.833  1.00 51.71 ? 124 ARG   A O   1 
ATOM   720  C  CB  . ARG   A 1 112 ? -4.566  -10.950 14.035  1.00 38.29 ? 124 ARG   A CB  1 
ATOM   721  C  CG  . ARG   A 1 112 ? -4.507  -10.338 15.416  1.00 37.13 ? 124 ARG   A CG  1 
ATOM   722  C  CD  . ARG   A 1 112 ? -5.724  -9.475  15.689  1.00 36.64 ? 124 ARG   A CD  1 
ATOM   723  N  NE  . ARG   A 1 112 ? -5.728  -8.291  14.841  1.00 34.15 ? 124 ARG   A NE  1 
ATOM   724  C  CZ  . ARG   A 1 112 ? -6.668  -7.357  14.857  1.00 31.41 ? 124 ARG   A CZ  1 
ATOM   725  N  NH1 . ARG   A 1 112 ? -7.684  -7.415  15.699  1.00 31.08 ? 124 ARG   A NH1 1 
ATOM   726  N  NH2 . ARG   A 1 112 ? -6.593  -6.347  13.995  1.00 31.65 ? 124 ARG   A NH2 1 
ATOM   727  N  N   . SER   A 1 113 ? -4.051  -12.346 11.413  1.00 49.30 ? 125 SER   A N   1 
ATOM   728  C  CA  . SER   A 1 113 ? -4.477  -13.259 10.355  1.00 53.57 ? 125 SER   A CA  1 
ATOM   729  C  C   . SER   A 1 113 ? -3.322  -13.636 9.432   1.00 55.52 ? 125 SER   A C   1 
ATOM   730  O  O   . SER   A 1 113 ? -2.892  -14.791 9.403   1.00 57.75 ? 125 SER   A O   1 
ATOM   731  C  CB  . SER   A 1 113 ? -5.622  -12.641 9.546   1.00 56.62 ? 125 SER   A CB  1 
ATOM   732  O  OG  . SER   A 1 113 ? -5.351  -11.289 9.215   1.00 56.40 ? 125 SER   A OG  1 
ATOM   733  N  N   . VAL   A 1 117 ? 0.182   -13.905 4.036   1.00 43.84 ? 129 VAL   A N   1 
ATOM   734  C  CA  . VAL   A 1 117 ? 1.484   -13.284 4.245   1.00 39.31 ? 129 VAL   A CA  1 
ATOM   735  C  C   . VAL   A 1 117 ? 1.285   -11.921 4.903   1.00 39.00 ? 129 VAL   A C   1 
ATOM   736  O  O   . VAL   A 1 117 ? 0.355   -11.181 4.559   1.00 38.05 ? 129 VAL   A O   1 
ATOM   737  C  CB  . VAL   A 1 117 ? 2.278   -13.173 2.919   1.00 46.11 ? 129 VAL   A CB  1 
ATOM   738  C  CG1 . VAL   A 1 117 ? 1.462   -12.441 1.854   1.00 44.77 ? 129 VAL   A CG1 1 
ATOM   739  C  CG2 . VAL   A 1 117 ? 3.635   -12.500 3.144   1.00 34.16 ? 129 VAL   A CG2 1 
ATOM   740  N  N   . LEU   A 1 118 ? 2.144   -11.613 5.873   1.00 32.17 ? 130 LEU   A N   1 
ATOM   741  C  CA  . LEU   A 1 118 ? 1.994   -10.395 6.655   1.00 31.35 ? 130 LEU   A CA  1 
ATOM   742  C  C   . LEU   A 1 118 ? 2.326   -9.175  5.812   1.00 30.61 ? 130 LEU   A C   1 
ATOM   743  O  O   . LEU   A 1 118 ? 3.346   -9.138  5.121   1.00 28.68 ? 130 LEU   A O   1 
ATOM   744  C  CB  . LEU   A 1 118 ? 2.901   -10.425 7.885   1.00 31.76 ? 130 LEU   A CB  1 
ATOM   745  C  CG  . LEU   A 1 118 ? 2.785   -11.573 8.887   1.00 33.74 ? 130 LEU   A CG  1 
ATOM   746  C  CD1 . LEU   A 1 118 ? 3.682   -11.284 10.083  1.00 34.34 ? 130 LEU   A CD1 1 
ATOM   747  C  CD2 . LEU   A 1 118 ? 1.340   -11.783 9.335   1.00 31.38 ? 130 LEU   A CD2 1 
ATOM   748  N  N   . GLN   A 1 119 ? 1.479   -8.154  5.902   1.00 30.49 ? 131 GLN   A N   1 
ATOM   749  C  CA  . GLN   A 1 119 ? 1.650   -6.935  5.127   1.00 27.62 ? 131 GLN   A CA  1 
ATOM   750  C  C   . GLN   A 1 119 ? 1.746   -5.729  6.049   1.00 26.42 ? 131 GLN   A C   1 
ATOM   751  O  O   . GLN   A 1 119 ? 0.911   -5.553  6.951   1.00 24.87 ? 131 GLN   A O   1 
ATOM   752  C  CB  . GLN   A 1 119 ? 0.506   -6.753  4.134   1.00 30.67 ? 131 GLN   A CB  1 
ATOM   753  C  CG  . GLN   A 1 119 ? 0.467   -7.820  3.070   1.00 33.39 ? 131 GLN   A CG  1 
ATOM   754  C  CD  . GLN   A 1 119 ? -0.218  -7.336  1.825   1.00 36.37 ? 131 GLN   A CD  1 
ATOM   755  O  OE1 . GLN   A 1 119 ? -0.676  -6.196  1.767   1.00 40.34 ? 131 GLN   A OE1 1 
ATOM   756  N  NE2 . GLN   A 1 119 ? -0.294  -8.196  0.811   1.00 40.35 ? 131 GLN   A NE2 1 
ATOM   757  N  N   . TRP   A 1 120 ? 2.776   -4.918  5.824   1.00 24.45 ? 132 TRP   A N   1 
ATOM   758  C  CA  . TRP   A 1 120 ? 2.925   -3.643  6.507   1.00 21.68 ? 132 TRP   A CA  1 
ATOM   759  C  C   . TRP   A 1 120 ? 2.005   -2.600  5.891   1.00 21.45 ? 132 TRP   A C   1 
ATOM   760  O  O   . TRP   A 1 120 ? 1.783   -2.575  4.674   1.00 20.83 ? 132 TRP   A O   1 
ATOM   761  C  CB  . TRP   A 1 120 ? 4.366   -3.146  6.418   1.00 21.67 ? 132 TRP   A CB  1 
ATOM   762  C  CG  . TRP   A 1 120 ? 5.406   -3.902  7.213   1.00 21.58 ? 132 TRP   A CG  1 
ATOM   763  C  CD1 . TRP   A 1 120 ? 6.192   -4.930  6.779   1.00 22.78 ? 132 TRP   A CD1 1 
ATOM   764  C  CD2 . TRP   A 1 120 ? 5.816   -3.631  8.564   1.00 21.40 ? 132 TRP   A CD2 1 
ATOM   765  N  NE1 . TRP   A 1 120 ? 7.038   -5.338  7.784   1.00 21.36 ? 132 TRP   A NE1 1 
ATOM   766  C  CE2 . TRP   A 1 120 ? 6.838   -4.547  8.882   1.00 20.35 ? 132 TRP   A CE2 1 
ATOM   767  C  CE3 . TRP   A 1 120 ? 5.411   -2.705  9.534   1.00 20.48 ? 132 TRP   A CE3 1 
ATOM   768  C  CZ2 . TRP   A 1 120 ? 7.459   -4.570  10.136  1.00 20.43 ? 132 TRP   A CZ2 1 
ATOM   769  C  CZ3 . TRP   A 1 120 ? 6.021   -2.732  10.775  1.00 16.71 ? 132 TRP   A CZ3 1 
ATOM   770  C  CH2 . TRP   A 1 120 ? 7.032   -3.658  11.063  1.00 21.87 ? 132 TRP   A CH2 1 
ATOM   771  N  N   . GLU   A 1 121 ? 1.470   -1.732  6.740   1.00 21.09 ? 133 GLU   A N   1 
ATOM   772  C  CA  . GLU   A 1 121 ? 0.678   -0.594  6.297   1.00 18.06 ? 133 GLU   A CA  1 
ATOM   773  C  C   . GLU   A 1 121 ? 1.343   0.676   6.801   1.00 23.27 ? 133 GLU   A C   1 
ATOM   774  O  O   . GLU   A 1 121 ? 1.551   0.828   8.009   1.00 20.34 ? 133 GLU   A O   1 
ATOM   775  C  CB  . GLU   A 1 121 ? -0.754  -0.695  6.814   1.00 24.66 ? 133 GLU   A CB  1 
ATOM   776  C  CG  . GLU   A 1 121 ? -1.605  -1.707  6.063   1.00 28.45 ? 133 GLU   A CG  1 
ATOM   777  C  CD  . GLU   A 1 121 ? -2.352  -1.079  4.906   1.00 33.40 ? 133 GLU   A CD  1 
ATOM   778  O  OE1 . GLU   A 1 121 ? -1.930  0.005   4.448   1.00 38.16 ? 133 GLU   A OE1 1 
ATOM   779  O  OE2 . GLU   A 1 121 ? -3.375  -1.656  4.477   1.00 36.26 ? 133 GLU   A OE2 1 
ATOM   780  N  N   . ARG   A 1 122 ? 1.667   1.580   5.882   1.00 21.57 ? 134 ARG   A N   1 
ATOM   781  C  CA  . ARG   A 1 122 ? 2.150   2.903   6.249   1.00 22.74 ? 134 ARG   A CA  1 
ATOM   782  C  C   . ARG   A 1 122 ? 0.959   3.827   6.446   1.00 23.98 ? 134 ARG   A C   1 
ATOM   783  O  O   . ARG   A 1 122 ? 0.120   3.961   5.554   1.00 24.01 ? 134 ARG   A O   1 
ATOM   784  C  CB  . ARG   A 1 122 ? 3.085   3.468   5.176   1.00 22.40 ? 134 ARG   A CB  1 
ATOM   785  C  CG  . ARG   A 1 122 ? 3.882   4.672   5.663   1.00 22.01 ? 134 ARG   A CG  1 
ATOM   786  C  CD  . ARG   A 1 122 ? 4.636   5.369   4.551   1.00 26.43 ? 134 ARG   A CD  1 
ATOM   787  N  NE  . ARG   A 1 122 ? 3.745   5.854   3.500   1.00 27.00 ? 134 ARG   A NE  1 
ATOM   788  C  CZ  . ARG   A 1 122 ? 3.511   5.229   2.354   1.00 28.59 ? 134 ARG   A CZ  1 
ATOM   789  N  NH1 . ARG   A 1 122 ? 4.127   4.101   2.040   1.00 27.97 ? 134 ARG   A NH1 1 
ATOM   790  N  NH2 . ARG   A 1 122 ? 2.627   5.745   1.506   1.00 24.86 ? 134 ARG   A NH2 1 
ATOM   791  N  N   . ILE   A 1 123 ? 0.882   4.464   7.608   1.00 21.91 ? 135 ILE   A N   1 
ATOM   792  C  CA  . ILE   A 1 123 ? -0.319  5.191   8.010   1.00 20.26 ? 135 ILE   A CA  1 
ATOM   793  C  C   . ILE   A 1 123 ? -0.151  6.668   7.691   1.00 23.79 ? 135 ILE   A C   1 
ATOM   794  O  O   . ILE   A 1 123 ? 0.785   7.315   8.175   1.00 25.64 ? 135 ILE   A O   1 
ATOM   795  C  CB  . ILE   A 1 123 ? -0.614  4.986   9.504   1.00 20.14 ? 135 ILE   A CB  1 
ATOM   796  C  CG1 . ILE   A 1 123 ? -0.723  3.499   9.808   1.00 20.56 ? 135 ILE   A CG1 1 
ATOM   797  C  CG2 . ILE   A 1 123 ? -1.895  5.725   9.903   1.00 21.72 ? 135 ILE   A CG2 1 
ATOM   798  C  CD1 . ILE   A 1 123 ? -1.848  2.794   9.068   1.00 22.69 ? 135 ILE   A CD1 1 
ATOM   799  N  N   . ASP   A 1 124 ? -1.083  7.211   6.909   1.00 25.15 ? 136 ASP   A N   1 
ATOM   800  C  CA  . ASP   A 1 124 ? -1.175  8.651   6.667   1.00 28.77 ? 136 ASP   A CA  1 
ATOM   801  C  C   . ASP   A 1 124 ? -1.787  9.292   7.914   1.00 22.77 ? 136 ASP   A C   1 
ATOM   802  O  O   . ASP   A 1 124 ? -2.986  9.560   8.002   1.00 27.24 ? 136 ASP   A O   1 
ATOM   803  C  CB  . ASP   A 1 124 ? -2.010  8.930   5.418   1.00 24.55 ? 136 ASP   A CB  1 
ATOM   804  C  CG  . ASP   A 1 124 ? -1.470  8.237   4.172   1.00 33.50 ? 136 ASP   A CG  1 
ATOM   805  O  OD1 . ASP   A 1 124 ? -0.233  8.234   3.959   1.00 33.19 ? 136 ASP   A OD1 1 
ATOM   806  O  OD2 . ASP   A 1 124 ? -2.301  7.711   3.386   1.00 44.06 ? 136 ASP   A OD2 1 
ATOM   807  N  N   . CYS   A 1 125 ? -0.947  9.517   8.918   1.00 24.73 ? 137 CYS   A N   1 
ATOM   808  C  CA  . CYS   A 1 125 ? -1.452  10.007  10.190  1.00 26.16 ? 137 CYS   A CA  1 
ATOM   809  C  C   . CYS   A 1 125 ? -1.980  11.430  10.064  1.00 23.76 ? 137 CYS   A C   1 
ATOM   810  O  O   . CYS   A 1 125 ? -1.466  12.244  9.293   1.00 23.49 ? 137 CYS   A O   1 
ATOM   811  C  CB  . CYS   A 1 125 ? -0.356  9.940   11.252  1.00 20.31 ? 137 CYS   A CB  1 
ATOM   812  S  SG  . CYS   A 1 125 ? 0.037   8.248   11.734  1.00 22.25 ? 137 CYS   A SG  1 
ATOM   813  N  N   . GLN   A 1 126 ? -3.020  11.726  10.830  1.00 23.54 ? 138 GLN   A N   1 
ATOM   814  C  CA  . GLN   A 1 126 ? -3.489  13.096  10.938  1.00 26.38 ? 138 GLN   A CA  1 
ATOM   815  C  C   . GLN   A 1 126 ? -2.724  13.830  12.034  1.00 25.13 ? 138 GLN   A C   1 
ATOM   816  O  O   . GLN   A 1 126 ? -2.145  13.223  12.943  1.00 22.38 ? 138 GLN   A O   1 
ATOM   817  C  CB  . GLN   A 1 126 ? -4.995  13.144  11.212  1.00 29.95 ? 138 GLN   A CB  1 
ATOM   818  C  CG  . GLN   A 1 126 ? -5.844  12.552  10.089  1.00 31.32 ? 138 GLN   A CG  1 
ATOM   819  C  CD  . GLN   A 1 126 ? -7.271  13.094  10.064  1.00 42.59 ? 138 GLN   A CD  1 
ATOM   820  O  OE1 . GLN   A 1 126 ? -8.149  12.607  10.780  1.00 41.51 ? 138 GLN   A OE1 1 
ATOM   821  N  NE2 . GLN   A 1 126 ? -7.507  14.102  9.228   1.00 43.39 ? 138 GLN   A NE2 1 
ATOM   822  N  N   . GLY   A 1 127 ? -2.698  15.154  11.917  1.00 26.82 ? 139 GLY   A N   1 
ATOM   823  C  CA  . GLY   A 1 127 ? -2.068  15.983  12.924  1.00 25.78 ? 139 GLY   A CA  1 
ATOM   824  C  C   . GLY   A 1 127 ? -0.589  16.208  12.681  1.00 22.21 ? 139 GLY   A C   1 
ATOM   825  O  O   . GLY   A 1 127 ? 0.001   15.777  11.687  1.00 22.92 ? 139 GLY   A O   1 
ATOM   826  N  N   . ILE   A 1 128 ? 0.020   16.905  13.633  1.00 21.44 ? 140 ILE   A N   1 
ATOM   827  C  CA  . ILE   A 1 128 ? 1.429   17.278  13.555  1.00 27.52 ? 140 ILE   A CA  1 
ATOM   828  C  C   . ILE   A 1 128 ? 2.259   16.107  14.068  1.00 25.35 ? 140 ILE   A C   1 
ATOM   829  O  O   . ILE   A 1 128 ? 2.213   15.808  15.268  1.00 24.89 ? 140 ILE   A O   1 
ATOM   830  C  CB  . ILE   A 1 128 ? 1.703   18.552  14.375  1.00 28.53 ? 140 ILE   A CB  1 
ATOM   831  C  CG1 . ILE   A 1 128 ? 0.794   19.698  13.921  1.00 26.18 ? 140 ILE   A CG1 1 
ATOM   832  C  CG2 . ILE   A 1 128 ? 3.170   18.956  14.282  1.00 26.75 ? 140 ILE   A CG2 1 
ATOM   833  C  CD1 . ILE   A 1 128 ? 1.022   20.964  14.705  1.00 28.50 ? 140 ILE   A CD1 1 
ATOM   834  N  N   . PRO   A 1 129 ? 3.024   15.426  13.219  1.00 23.06 ? 141 PRO   A N   1 
ATOM   835  C  CA  . PRO   A 1 129 ? 3.831   14.284  13.685  1.00 20.53 ? 141 PRO   A CA  1 
ATOM   836  C  C   . PRO   A 1 129 ? 5.002   14.753  14.529  1.00 21.33 ? 141 PRO   A C   1 
ATOM   837  O  O   . PRO   A 1 129 ? 5.319   15.951  14.550  1.00 23.67 ? 141 PRO   A O   1 
ATOM   838  C  CB  . PRO   A 1 129 ? 4.311   13.634  12.376  1.00 22.99 ? 141 PRO   A CB  1 
ATOM   839  C  CG  . PRO   A 1 129 ? 4.307   14.764  11.392  1.00 19.72 ? 141 PRO   A CG  1 
ATOM   840  C  CD  . PRO   A 1 129 ? 3.129   15.621  11.760  1.00 20.70 ? 141 PRO   A CD  1 
ATOM   841  N  N   . PRO   A 1 130 ? 5.663   13.850  15.250  1.00 19.10 ? 142 PRO   A N   1 
ATOM   842  C  CA  . PRO   A 1 130 ? 6.921   14.227  15.900  1.00 17.08 ? 142 PRO   A CA  1 
ATOM   843  C  C   . PRO   A 1 130 ? 7.988   14.526  14.859  1.00 16.48 ? 142 PRO   A C   1 
ATOM   844  O  O   . PRO   A 1 130 ? 7.870   14.180  13.681  1.00 19.95 ? 142 PRO   A O   1 
ATOM   845  C  CB  . PRO   A 1 130 ? 7.291   12.991  16.736  1.00 17.38 ? 142 PRO   A CB  1 
ATOM   846  C  CG  . PRO   A 1 130 ? 6.022   12.174  16.847  1.00 15.93 ? 142 PRO   A CG  1 
ATOM   847  C  CD  . PRO   A 1 130 ? 5.290   12.452  15.539  1.00 13.27 ? 142 PRO   A CD  1 
ATOM   848  N  N   . SER   A 1 131 ? 9.052   15.179  15.312  1.00 20.58 ? 143 SER   A N   1 
ATOM   849  C  CA  . SER   A 1 131 ? 10.223  15.357  14.467  1.00 20.52 ? 143 SER   A CA  1 
ATOM   850  C  C   . SER   A 1 131 ? 10.846  13.999  14.151  1.00 18.17 ? 143 SER   A C   1 
ATOM   851  O  O   . SER   A 1 131 ? 10.664  13.027  14.883  1.00 18.57 ? 143 SER   A O   1 
ATOM   852  C  CB  . SER   A 1 131 ? 11.236  16.266  15.161  1.00 19.06 ? 143 SER   A CB  1 
ATOM   853  O  OG  . SER   A 1 131 ? 11.694  15.678  16.370  1.00 17.31 ? 143 SER   A OG  1 
ATOM   854  N  N   . SER   A 1 132 ? 11.561  13.923  13.025  1.00 17.67 ? 144 SER   A N   1 
ATOM   855  C  CA  . SER   A 1 132 ? 12.199  12.670  12.616  1.00 16.00 ? 144 SER   A CA  1 
ATOM   856  C  C   . SER   A 1 132 ? 13.331  12.317  13.577  1.00 13.79 ? 144 SER   A C   1 
ATOM   857  O  O   . SER   A 1 132 ? 14.253  13.114  13.775  1.00 15.51 ? 144 SER   A O   1 
ATOM   858  C  CB  . SER   A 1 132 ? 12.738  12.795  11.197  1.00 18.51 ? 144 SER   A CB  1 
ATOM   859  O  OG  . SER   A 1 132 ? 11.839  13.546  10.442  1.00 16.49 ? 144 SER   A OG  1 
ATOM   860  N  N   . LYS   A 1 133 ? 13.278  11.122  14.159  1.00 12.53 ? 145 LYS   A N   1 
ATOM   861  C  CA  . LYS   A 1 133 ? 14.160  10.828  15.284  1.00 12.73 ? 145 LYS   A CA  1 
ATOM   862  C  C   . LYS   A 1 133 ? 14.236  9.326   15.533  1.00 10.83 ? 145 LYS   A C   1 
ATOM   863  O  O   . LYS   A 1 133 ? 13.457  8.535   14.988  1.00 14.71 ? 145 LYS   A O   1 
ATOM   864  C  CB  . LYS   A 1 133 ? 13.689  11.538  16.555  1.00 13.21 ? 145 LYS   A CB  1 
ATOM   865  C  CG  . LYS   A 1 133 ? 12.288  11.133  16.993  1.00 13.99 ? 145 LYS   A CG  1 
ATOM   866  C  CD  . LYS   A 1 133 ? 11.882  11.970  18.186  1.00 13.90 ? 145 LYS   A CD  1 
ATOM   867  C  CE  . LYS   A 1 133 ? 10.555  11.545  18.745  1.00 15.18 ? 145 LYS   A CE  1 
ATOM   868  N  NZ  . LYS   A 1 133 ? 10.094  12.506  19.809  1.00 14.86 ? 145 LYS   A NZ  1 
ATOM   869  N  N   . ASP   A 1 134 ? 15.182  8.946   16.394  1.00 12.01 ? 146 ASP   A N   1 
ATOM   870  C  CA  . ASP   A 1 134 ? 15.373  7.551   16.753  1.00 10.49 ? 146 ASP   A CA  1 
ATOM   871  C  C   . ASP   A 1 134 ? 15.725  7.479   18.234  1.00 10.19 ? 146 ASP   A C   1 
ATOM   872  O  O   . ASP   A 1 134 ? 15.827  8.501   18.916  1.00 12.69 ? 146 ASP   A O   1 
ATOM   873  C  CB  . ASP   A 1 134 ? 16.441  6.873   15.875  1.00 10.71 ? 146 ASP   A CB  1 
ATOM   874  C  CG  . ASP   A 1 134 ? 17.828  7.498   16.017  1.00 13.82 ? 146 ASP   A CG  1 
ATOM   875  O  OD1 . ASP   A 1 134 ? 18.142  8.069   17.096  1.00 16.13 ? 146 ASP   A OD1 1 
ATOM   876  O  OD2 . ASP   A 1 134 ? 18.622  7.405   15.038  1.00 14.84 ? 146 ASP   A OD2 1 
ATOM   877  N  N   . LYS   A 1 135 ? 15.913  6.259   18.725  1.00 11.45 ? 147 LYS   A N   1 
ATOM   878  C  CA  . LYS   A 1 135 ? 16.393  6.021   20.092  1.00 12.80 ? 147 LYS   A CA  1 
ATOM   879  C  C   . LYS   A 1 135 ? 15.547  6.769   21.127  1.00 12.65 ? 147 LYS   A C   1 
ATOM   880  O  O   . LYS   A 1 135 ? 16.036  7.583   21.924  1.00 10.46 ? 147 LYS   A O   1 
ATOM   881  C  CB  . LYS   A 1 135 ? 17.873  6.393   20.213  1.00 11.59 ? 147 LYS   A CB  1 
ATOM   882  C  CG  . LYS   A 1 135 ? 18.807  5.538   19.351  1.00 16.55 ? 147 LYS   A CG  1 
ATOM   883  C  CD  . LYS   A 1 135 ? 20.286  5.847   19.645  1.00 13.12 ? 147 LYS   A CD  1 
ATOM   884  C  CE  . LYS   A 1 135 ? 20.738  7.193   19.079  1.00 15.58 ? 147 LYS   A CE  1 
ATOM   885  N  NZ  . LYS   A 1 135 ? 20.627  7.151   17.608  1.00 14.56 ? 147 LYS   A NZ  1 
ATOM   886  N  N   . LEU   A 1 136 ? 14.252  6.461   21.108  1.00 12.93 ? 148 LEU   A N   1 
ATOM   887  C  CA  . LEU   A 1 136 ? 13.273  7.077   21.998  1.00 12.40 ? 148 LEU   A CA  1 
ATOM   888  C  C   . LEU   A 1 136 ? 12.585  5.973   22.785  1.00 10.33 ? 148 LEU   A C   1 
ATOM   889  O  O   . LEU   A 1 136 ? 13.120  4.864   22.881  1.00 15.31 ? 148 LEU   A O   1 
ATOM   890  C  CB  . LEU   A 1 136 ? 12.265  7.926   21.217  1.00 12.85 ? 148 LEU   A CB  1 
ATOM   891  C  CG  . LEU   A 1 136 ? 11.396  7.212   20.175  1.00 10.56 ? 148 LEU   A CG  1 
ATOM   892  C  CD1 . LEU   A 1 136 ? 10.043  7.888   20.063  1.00 15.74 ? 148 LEU   A CD1 1 
ATOM   893  C  CD2 . LEU   A 1 136 ? 12.082  7.200   18.798  1.00 14.41 ? 148 LEU   A CD2 1 
ATOM   894  N  N   . GLY   A 1 137 ? 11.448  6.263   23.426  1.00 11.64 ? 149 GLY   A N   1 
ATOM   895  C  CA  . GLY   A 1 137 ? 10.673  5.216   24.053  1.00 11.67 ? 149 GLY   A CA  1 
ATOM   896  C  C   . GLY   A 1 137 ? 9.191   5.503   23.913  1.00 11.51 ? 149 GLY   A C   1 
ATOM   897  O  O   . GLY   A 1 137 ? 8.788   6.566   23.436  1.00 11.51 ? 149 GLY   A O   1 
ATOM   898  N  N   . VAL   A 1 138 ? 8.389   4.545   24.364  1.00 10.36 ? 150 VAL   A N   1 
ATOM   899  C  CA  . VAL   A 1 138 ? 6.940   4.669   24.241  1.00 12.71 ? 150 VAL   A CA  1 
ATOM   900  C  C   . VAL   A 1 138 ? 6.240   4.008   25.427  1.00 12.83 ? 150 VAL   A C   1 
ATOM   901  O  O   . VAL   A 1 138 ? 6.673   2.968   25.945  1.00 14.77 ? 150 VAL   A O   1 
ATOM   902  C  CB  . VAL   A 1 138 ? 6.464   4.080   22.903  1.00 16.42 ? 150 VAL   A CB  1 
ATOM   903  C  CG1 . VAL   A 1 138 ? 6.788   2.596   22.849  1.00 14.52 ? 150 VAL   A CG1 1 
ATOM   904  C  CG2 . VAL   A 1 138 ? 4.966   4.356   22.692  1.00 11.00 ? 150 VAL   A CG2 1 
ATOM   905  N  N   . TRP   A 1 139 ? 5.147   4.630   25.856  1.00 13.83 ? 151 TRP   A N   1 
ATOM   906  C  CA  . TRP   A 1 139 ? 4.199   4.025   26.770  1.00 14.62 ? 151 TRP   A CA  1 
ATOM   907  C  C   . TRP   A 1 139 ? 2.895   3.716   26.031  1.00 15.22 ? 151 TRP   A C   1 
ATOM   908  O  O   . TRP   A 1 139 ? 2.475   4.465   25.146  1.00 16.45 ? 151 TRP   A O   1 
ATOM   909  C  CB  . TRP   A 1 139 ? 3.922   4.964   27.953  1.00 14.62 ? 151 TRP   A CB  1 
ATOM   910  C  CG  . TRP   A 1 139 ? 5.154   5.509   28.662  1.00 14.32 ? 151 TRP   A CG  1 
ATOM   911  C  CD1 . TRP   A 1 139 ? 6.056   4.793   29.412  1.00 16.18 ? 151 TRP   A CD1 1 
ATOM   912  C  CD2 . TRP   A 1 139 ? 5.592   6.876   28.719  1.00 14.99 ? 151 TRP   A CD2 1 
ATOM   913  N  NE1 . TRP   A 1 139 ? 7.020   5.626   29.922  1.00 16.83 ? 151 TRP   A NE1 1 
ATOM   914  C  CE2 . TRP   A 1 139 ? 6.777   6.904   29.496  1.00 16.21 ? 151 TRP   A CE2 1 
ATOM   915  C  CE3 . TRP   A 1 139 ? 5.122   8.072   28.170  1.00 18.05 ? 151 TRP   A CE3 1 
ATOM   916  C  CZ2 . TRP   A 1 139 ? 7.464   8.084   29.767  1.00 14.98 ? 151 TRP   A CZ2 1 
ATOM   917  C  CZ3 . TRP   A 1 139 ? 5.832   9.249   28.432  1.00 16.26 ? 151 TRP   A CZ3 1 
ATOM   918  C  CH2 . TRP   A 1 139 ? 6.983   9.240   29.227  1.00 15.58 ? 151 TRP   A CH2 1 
ATOM   919  N  N   . VAL   A 1 140 ? 2.241   2.621   26.411  1.00 16.19 ? 152 VAL   A N   1 
ATOM   920  C  CA  . VAL   A 1 140 ? 0.925   2.268   25.881  1.00 17.46 ? 152 VAL   A CA  1 
ATOM   921  C  C   . VAL   A 1 140 ? -0.089  2.437   27.000  1.00 17.92 ? 152 VAL   A C   1 
ATOM   922  O  O   . VAL   A 1 140 ? 0.060   1.851   28.082  1.00 17.63 ? 152 VAL   A O   1 
ATOM   923  C  CB  . VAL   A 1 140 ? 0.889   0.836   25.327  1.00 21.65 ? 152 VAL   A CB  1 
ATOM   924  C  CG1 . VAL   A 1 140 ? -0.536  0.476   24.880  1.00 20.65 ? 152 VAL   A CG1 1 
ATOM   925  C  CG2 . VAL   A 1 140 ? 1.866   0.700   24.180  1.00 19.20 ? 152 VAL   A CG2 1 
ATOM   926  N  N   . TYR   A 1 141 ? -1.118  3.237   26.748  1.00 18.13 ? 153 TYR   A N   1 
ATOM   927  C  CA  . TYR   A 1 141 ? -2.179  3.437   27.726  1.00 22.35 ? 153 TYR   A CA  1 
ATOM   928  C  C   . TYR   A 1 141 ? -3.487  3.560   26.961  1.00 20.99 ? 153 TYR   A C   1 
ATOM   929  O  O   . TYR   A 1 141 ? -3.716  4.571   26.288  1.00 19.72 ? 153 TYR   A O   1 
ATOM   930  C  CB  . TYR   A 1 141 ? -1.918  4.669   28.587  1.00 20.76 ? 153 TYR   A CB  1 
ATOM   931  C  CG  . TYR   A 1 141 ? -2.896  4.798   29.729  1.00 19.03 ? 153 TYR   A CG  1 
ATOM   932  C  CD1 . TYR   A 1 141 ? -3.141  3.731   30.578  1.00 22.76 ? 153 TYR   A CD1 1 
ATOM   933  C  CD2 . TYR   A 1 141 ? -3.579  5.978   29.944  1.00 21.25 ? 153 TYR   A CD2 1 
ATOM   934  C  CE1 . TYR   A 1 141 ? -4.053  3.840   31.627  1.00 24.56 ? 153 TYR   A CE1 1 
ATOM   935  C  CE2 . TYR   A 1 141 ? -4.489  6.101   30.975  1.00 25.13 ? 153 TYR   A CE2 1 
ATOM   936  C  CZ  . TYR   A 1 141 ? -4.723  5.033   31.817  1.00 25.54 ? 153 TYR   A CZ  1 
ATOM   937  O  OH  . TYR   A 1 141 ? -5.631  5.171   32.854  1.00 29.26 ? 153 TYR   A OH  1 
ATOM   938  N  N   . LYS   A 1 142 ? -4.311  2.516   27.047  1.00 23.33 ? 154 LYS   A N   1 
ATOM   939  C  CA  . LYS   A 1 142 ? -5.624  2.430   26.390  1.00 20.26 ? 154 LYS   A CA  1 
ATOM   940  C  C   . LYS   A 1 142 ? -5.406  2.657   24.896  1.00 17.91 ? 154 LYS   A C   1 
ATOM   941  O  O   . LYS   A 1 142 ? -4.568  1.957   24.310  1.00 24.61 ? 154 LYS   A O   1 
ATOM   942  C  CB  . LYS   A 1 142 ? -6.587  3.383   27.085  1.00 18.39 ? 154 LYS   A CB  1 
ATOM   943  C  CG  . LYS   A 1 142 ? -6.886  2.959   28.544  1.00 20.55 ? 154 LYS   A CG  1 
ATOM   944  C  CD  . LYS   A 1 142 ? -7.615  4.036   29.315  1.00 24.41 ? 154 LYS   A CD  1 
ATOM   945  C  CE  . LYS   A 1 142 ? -7.694  3.723   30.827  1.00 27.04 ? 154 LYS   A CE  1 
ATOM   946  N  NZ  . LYS   A 1 142 ? -8.189  2.344   31.160  1.00 25.54 ? 154 LYS   A NZ  1 
ATOM   947  N  N   . ASN   A 1 143 ? -6.103  3.596   24.264  1.00 17.85 ? 155 ASN   A N   1 
ATOM   948  C  CA  . ASN   A 1 143 ? -6.011  3.830   22.824  1.00 17.23 ? 155 ASN   A CA  1 
ATOM   949  C  C   . ASN   A 1 143 ? -4.799  4.663   22.421  1.00 19.00 ? 155 ASN   A C   1 
ATOM   950  O  O   . ASN   A 1 143 ? -4.596  4.892   21.224  1.00 17.13 ? 155 ASN   A O   1 
ATOM   951  C  CB  . ASN   A 1 143 ? -7.296  4.512   22.328  1.00 19.48 ? 155 ASN   A CB  1 
ATOM   952  C  CG  . ASN   A 1 143 ? -7.621  5.781   23.099  1.00 22.05 ? 155 ASN   A CG  1 
ATOM   953  O  OD1 . ASN   A 1 143 ? -7.925  5.720   24.287  1.00 24.68 ? 155 ASN   A OD1 1 
ATOM   954  N  ND2 . ASN   A 1 143 ? -7.568  6.932   22.430  1.00 20.44 ? 155 ASN   A ND2 1 
ATOM   955  N  N   . LYS   A 1 144 ? -3.984  5.108   23.372  1.00 18.70 ? 156 LYS   A N   1 
ATOM   956  C  CA  . LYS   A 1 144 ? -2.907  6.041   23.095  1.00 18.02 ? 156 LYS   A CA  1 
ATOM   957  C  C   . LYS   A 1 144 ? -1.567  5.317   23.052  1.00 15.99 ? 156 LYS   A C   1 
ATOM   958  O  O   . LYS   A 1 144 ? -1.290  4.437   23.875  1.00 16.48 ? 156 LYS   A O   1 
ATOM   959  C  CB  . LYS   A 1 144 ? -2.885  7.164   24.142  1.00 18.04 ? 156 LYS   A CB  1 
ATOM   960  C  CG  . LYS   A 1 144 ? -4.134  8.048   24.129  1.00 19.60 ? 156 LYS   A CG  1 
ATOM   961  C  CD  . LYS   A 1 144 ? -4.023  9.227   25.087  1.00 25.79 ? 156 LYS   A CD  1 
ATOM   962  C  CE  . LYS   A 1 144 ? -5.396  9.696   25.542  1.00 30.54 ? 156 LYS   A CE  1 
ATOM   963  N  NZ  . LYS   A 1 144 ? -5.335  11.024  26.213  1.00 34.08 ? 156 LYS   A NZ  1 
ATOM   964  N  N   . LEU   A 1 145 ? -0.764  5.641   22.040  1.00 12.12 ? 157 LEU   A N   1 
ATOM   965  C  CA  . LEU   A 1 145 ? 0.671   5.395   22.060  1.00 14.24 ? 157 LEU   A CA  1 
ATOM   966  C  C   . LEU   A 1 145 ? 1.341   6.728   22.380  1.00 15.08 ? 157 LEU   A C   1 
ATOM   967  O  O   . LEU   A 1 145 ? 1.132   7.718   21.671  1.00 15.74 ? 157 LEU   A O   1 
ATOM   968  C  CB  . LEU   A 1 145 ? 1.169   4.832   20.719  1.00 14.08 ? 157 LEU   A CB  1 
ATOM   969  C  CG  . LEU   A 1 145 ? 0.326   3.678   20.149  1.00 14.90 ? 157 LEU   A CG  1 
ATOM   970  C  CD1 . LEU   A 1 145 ? 0.847   3.216   18.773  1.00 18.25 ? 157 LEU   A CD1 1 
ATOM   971  C  CD2 . LEU   A 1 145 ? 0.222   2.505   21.089  1.00 19.69 ? 157 LEU   A CD2 1 
ATOM   972  N  N   . ILE   A 1 146 ? 2.142   6.757   23.439  1.00 13.58 ? 158 ILE   A N   1 
ATOM   973  C  CA  . ILE   A 1 146 ? 2.739   7.992   23.937  1.00 13.47 ? 158 ILE   A CA  1 
ATOM   974  C  C   . ILE   A 1 146 ? 4.257   7.891   23.787  1.00 14.79 ? 158 ILE   A C   1 
ATOM   975  O  O   . ILE   A 1 146 ? 4.896   7.068   24.451  1.00 16.23 ? 158 ILE   A O   1 
ATOM   976  C  CB  . ILE   A 1 146 ? 2.342   8.245   25.398  1.00 14.03 ? 158 ILE   A CB  1 
ATOM   977  C  CG1 . ILE   A 1 146 ? 0.823   8.067   25.532  1.00 14.02 ? 158 ILE   A CG1 1 
ATOM   978  C  CG2 . ILE   A 1 146 ? 2.817   9.627   25.836  1.00 15.06 ? 158 ILE   A CG2 1 
ATOM   979  C  CD1 . ILE   A 1 146 ? 0.351   7.658   26.900  1.00 18.59 ? 158 ILE   A CD1 1 
ATOM   980  N  N   . PHE   A 1 147 ? 4.831   8.729   22.927  1.00 12.64 ? 159 PHE   A N   1 
ATOM   981  C  CA  . PHE   A 1 147 ? 6.250   8.691   22.593  1.00 14.43 ? 159 PHE   A CA  1 
ATOM   982  C  C   . PHE   A 1 147 ? 6.992   9.806   23.310  1.00 13.79 ? 159 PHE   A C   1 
ATOM   983  O  O   . PHE   A 1 147 ? 6.493   10.929  23.410  1.00 14.64 ? 159 PHE   A O   1 
ATOM   984  C  CB  . PHE   A 1 147 ? 6.448   8.828   21.079  1.00 13.23 ? 159 PHE   A CB  1 
ATOM   985  C  CG  . PHE   A 1 147 ? 5.815   7.718   20.298  1.00 14.02 ? 159 PHE   A CG  1 
ATOM   986  C  CD1 . PHE   A 1 147 ? 6.491   6.520   20.116  1.00 13.61 ? 159 PHE   A CD1 1 
ATOM   987  C  CD2 . PHE   A 1 147 ? 4.531   7.852   19.780  1.00 15.73 ? 159 PHE   A CD2 1 
ATOM   988  C  CE1 . PHE   A 1 147 ? 5.916   5.478   19.421  1.00 15.69 ? 159 PHE   A CE1 1 
ATOM   989  C  CE2 . PHE   A 1 147 ? 3.945   6.812   19.075  1.00 15.42 ? 159 PHE   A CE2 1 
ATOM   990  C  CZ  . PHE   A 1 147 ? 4.648   5.631   18.875  1.00 13.17 ? 159 PHE   A CZ  1 
ATOM   991  N  N   . PHE   A 1 148 ? 8.180   9.491   23.827  1.00 13.07 ? 160 PHE   A N   1 
ATOM   992  C  CA  . PHE   A 1 148 ? 8.965   10.475  24.562  1.00 15.04 ? 160 PHE   A CA  1 
ATOM   993  C  C   . PHE   A 1 148 ? 10.415  10.480  24.099  1.00 15.28 ? 160 PHE   A C   1 
ATOM   994  O  O   . PHE   A 1 148 ? 11.029  9.416   23.955  1.00 13.93 ? 160 PHE   A O   1 
ATOM   995  C  CB  . PHE   A 1 148 ? 8.919   10.224  26.079  1.00 12.81 ? 160 PHE   A CB  1 
ATOM   996  C  CG  . PHE   A 1 148 ? 9.937   11.027  26.843  1.00 13.37 ? 160 PHE   A CG  1 
ATOM   997  C  CD1 . PHE   A 1 148 ? 9.758   12.393  27.028  1.00 15.20 ? 160 PHE   A CD1 1 
ATOM   998  C  CD2 . PHE   A 1 148 ? 11.089  10.429  27.331  1.00 14.49 ? 160 PHE   A CD2 1 
ATOM   999  C  CE1 . PHE   A 1 148 ? 10.695  13.152  27.700  1.00 16.46 ? 160 PHE   A CE1 1 
ATOM   1000 C  CE2 . PHE   A 1 148 ? 12.043  11.178  28.019  1.00 16.55 ? 160 PHE   A CE2 1 
ATOM   1001 C  CZ  . PHE   A 1 148 ? 11.849  12.535  28.212  1.00 15.67 ? 160 PHE   A CZ  1 
ATOM   1002 N  N   . GLY   A 1 149 ? 10.945  11.686  23.846  1.00 11.96 ? 161 GLY   A N   1 
ATOM   1003 C  CA  . GLY   A 1 149 ? 12.368  11.962  23.662  1.00 12.86 ? 161 GLY   A CA  1 
ATOM   1004 C  C   . GLY   A 1 149 ? 12.958  11.462  22.347  1.00 12.97 ? 161 GLY   A C   1 
ATOM   1005 O  O   . GLY   A 1 149 ? 12.263  11.277  21.358  1.00 10.70 ? 161 GLY   A O   1 
ATOM   1006 N  N   . GLY   A 1 150 ? 14.284  11.279  22.344  1.00 13.99 ? 162 GLY   A N   1 
ATOM   1007 C  CA  . GLY   A 1 150 ? 14.993  10.681  21.219  1.00 12.37 ? 162 GLY   A CA  1 
ATOM   1008 C  C   . GLY   A 1 150 ? 16.004  11.626  20.594  1.00 13.79 ? 162 GLY   A C   1 
ATOM   1009 O  O   . GLY   A 1 150 ? 16.252  12.730  21.078  1.00 13.91 ? 162 GLY   A O   1 
ATOM   1010 N  N   . TYR   A 1 151 ? 16.558  11.188  19.457  1.00 15.51 ? 163 TYR   A N   1 
ATOM   1011 C  CA  . TYR   A 1 151 ? 17.655  11.859  18.758  1.00 15.12 ? 163 TYR   A CA  1 
ATOM   1012 C  C   . TYR   A 1 151 ? 17.264  12.046  17.302  1.00 14.93 ? 163 TYR   A C   1 
ATOM   1013 O  O   . TYR   A 1 151 ? 16.871  11.071  16.659  1.00 12.41 ? 163 TYR   A O   1 
ATOM   1014 C  CB  . TYR   A 1 151 ? 18.912  11.009  18.821  1.00 11.93 ? 163 TYR   A CB  1 
ATOM   1015 C  CG  . TYR   A 1 151 ? 20.212  11.691  18.411  1.00 13.43 ? 163 TYR   A CG  1 
ATOM   1016 C  CD1 . TYR   A 1 151 ? 20.749  12.726  19.174  1.00 17.01 ? 163 TYR   A CD1 1 
ATOM   1017 C  CD2 . TYR   A 1 151 ? 20.929  11.257  17.294  1.00 20.40 ? 163 TYR   A CD2 1 
ATOM   1018 C  CE1 . TYR   A 1 151 ? 21.947  13.334  18.825  1.00 18.17 ? 163 TYR   A CE1 1 
ATOM   1019 C  CE2 . TYR   A 1 151 ? 22.147  11.856  16.946  1.00 16.25 ? 163 TYR   A CE2 1 
ATOM   1020 C  CZ  . TYR   A 1 151 ? 22.636  12.897  17.713  1.00 19.73 ? 163 TYR   A CZ  1 
ATOM   1021 O  OH  . TYR   A 1 151 ? 23.824  13.509  17.383  1.00 18.98 ? 163 TYR   A OH  1 
ATOM   1022 N  N   . GLY   A 1 152 ? 17.402  13.264  16.782  1.00 14.92 ? 164 GLY   A N   1 
ATOM   1023 C  CA  . GLY   A 1 152 ? 17.100  13.500  15.376  1.00 19.93 ? 164 GLY   A CA  1 
ATOM   1024 C  C   . GLY   A 1 152 ? 17.284  14.949  14.966  1.00 20.46 ? 164 GLY   A C   1 
ATOM   1025 O  O   . GLY   A 1 152 ? 17.991  15.712  15.628  1.00 18.00 ? 164 GLY   A O   1 
ATOM   1026 N  N   . TYR   A 1 153 ? 16.634  15.325  13.859  1.00 18.05 ? 165 TYR   A N   1 
ATOM   1027 C  CA  . TYR   A 1 153 ? 16.802  16.658  13.277  1.00 22.73 ? 165 TYR   A CA  1 
ATOM   1028 C  C   . TYR   A 1 153 ? 16.070  17.714  14.105  1.00 21.04 ? 165 TYR   A C   1 
ATOM   1029 O  O   . TYR   A 1 153 ? 15.220  17.418  14.946  1.00 19.20 ? 165 TYR   A O   1 
ATOM   1030 C  CB  . TYR   A 1 153 ? 16.292  16.686  11.828  1.00 18.24 ? 165 TYR   A CB  1 
ATOM   1031 C  CG  . TYR   A 1 153 ? 16.877  15.565  11.017  1.00 21.43 ? 165 TYR   A CG  1 
ATOM   1032 C  CD1 . TYR   A 1 153 ? 18.242  15.340  11.027  1.00 29.03 ? 165 TYR   A CD1 1 
ATOM   1033 C  CD2 . TYR   A 1 153 ? 16.067  14.690  10.302  1.00 22.23 ? 165 TYR   A CD2 1 
ATOM   1034 C  CE1 . TYR   A 1 153 ? 18.800  14.312  10.324  1.00 27.57 ? 165 TYR   A CE1 1 
ATOM   1035 C  CE2 . TYR   A 1 153 ? 16.621  13.643  9.584   1.00 25.75 ? 165 TYR   A CE2 1 
ATOM   1036 C  CZ  . TYR   A 1 153 ? 17.992  13.467  9.599   1.00 26.47 ? 165 TYR   A CZ  1 
ATOM   1037 O  OH  . TYR   A 1 153 ? 18.593  12.441  8.908   1.00 25.92 ? 165 TYR   A OH  1 
ATOM   1038 N  N   . LEU   A 1 154 ? 16.404  18.969  13.841  1.00 23.61 ? 166 LEU   A N   1 
ATOM   1039 C  CA  . LEU   A 1 154 ? 15.641  20.062  14.417  1.00 23.38 ? 166 LEU   A CA  1 
ATOM   1040 C  C   . LEU   A 1 154 ? 14.177  19.937  13.995  1.00 25.23 ? 166 LEU   A C   1 
ATOM   1041 O  O   . LEU   A 1 154 ? 13.893  19.608  12.839  1.00 29.66 ? 166 LEU   A O   1 
ATOM   1042 C  CB  . LEU   A 1 154 ? 16.211  21.402  13.951  1.00 27.53 ? 166 LEU   A CB  1 
ATOM   1043 C  CG  . LEU   A 1 154 ? 15.524  22.665  14.452  1.00 26.02 ? 166 LEU   A CG  1 
ATOM   1044 C  CD1 . LEU   A 1 154 ? 15.882  22.948  15.895  1.00 27.78 ? 166 LEU   A CD1 1 
ATOM   1045 C  CD2 . LEU   A 1 154 ? 15.930  23.825  13.579  1.00 31.30 ? 166 LEU   A CD2 1 
ATOM   1046 N  N   . PRO   A 1 155 ? 13.231  20.144  14.911  1.00 27.84 ? 167 PRO   A N   1 
ATOM   1047 C  CA  . PRO   A 1 155 ? 11.809  20.029  14.550  1.00 33.10 ? 167 PRO   A CA  1 
ATOM   1048 C  C   . PRO   A 1 155 ? 11.393  21.068  13.515  1.00 40.38 ? 167 PRO   A C   1 
ATOM   1049 O  O   . PRO   A 1 155 ? 11.940  22.171  13.450  1.00 40.60 ? 167 PRO   A O   1 
ATOM   1050 C  CB  . PRO   A 1 155 ? 11.082  20.259  15.882  1.00 31.80 ? 167 PRO   A CB  1 
ATOM   1051 C  CG  . PRO   A 1 155 ? 12.084  20.006  16.931  1.00 27.94 ? 167 PRO   A CG  1 
ATOM   1052 C  CD  . PRO   A 1 155 ? 13.430  20.325  16.355  1.00 25.41 ? 167 PRO   A CD  1 
ATOM   1053 N  N   . GLU   A 1 156 ? 10.397  20.701  12.704  1.00 43.30 ? 168 GLU   A N   1 
ATOM   1054 C  CA  . GLU   A 1 156 ? 9.848   21.604  11.695  1.00 50.36 ? 168 GLU   A CA  1 
ATOM   1055 C  C   . GLU   A 1 156 ? 8.926   22.667  12.274  1.00 54.94 ? 168 GLU   A C   1 
ATOM   1056 O  O   . GLU   A 1 156 ? 8.497   23.561  11.535  1.00 59.24 ? 168 GLU   A O   1 
ATOM   1057 C  CB  . GLU   A 1 156 ? 9.080   20.815  10.634  1.00 51.66 ? 168 GLU   A CB  1 
ATOM   1058 C  CG  . GLU   A 1 156 ? 9.908   19.778  9.908   1.00 52.15 ? 168 GLU   A CG  1 
ATOM   1059 C  CD  . GLU   A 1 156 ? 11.258  20.305  9.488   1.00 45.27 ? 168 GLU   A CD  1 
ATOM   1060 O  OE1 . GLU   A 1 156 ? 12.254  19.580  9.673   1.00 47.07 ? 168 GLU   A OE1 1 
ATOM   1061 O  OE2 . GLU   A 1 156 ? 11.330  21.440  8.972   1.00 48.58 ? 168 GLU   A OE2 1 
ATOM   1062 N  N   . ASP   A 1 157 ? 8.604   22.583  13.562  1.00 61.35 ? 169 ASP   A N   1 
ATOM   1063 C  CA  . ASP   A 1 157 ? 7.721   23.530  14.223  1.00 66.36 ? 169 ASP   A CA  1 
ATOM   1064 C  C   . ASP   A 1 157 ? 8.237   23.763  15.637  1.00 63.87 ? 169 ASP   A C   1 
ATOM   1065 O  O   . ASP   A 1 157 ? 8.997   22.958  16.180  1.00 56.36 ? 169 ASP   A O   1 
ATOM   1066 C  CB  . ASP   A 1 157 ? 6.271   23.011  14.242  1.00 67.01 ? 169 ASP   A CB  1 
ATOM   1067 C  CG  . ASP   A 1 157 ? 5.339   23.875  15.075  1.00 70.66 ? 169 ASP   A CG  1 
ATOM   1068 O  OD1 . ASP   A 1 157 ? 4.879   24.924  14.575  1.00 75.97 ? 169 ASP   A OD1 1 
ATOM   1069 O  OD2 . ASP   A 1 157 ? 5.066   23.500  16.235  1.00 67.33 ? 169 ASP   A OD2 1 
ATOM   1070 N  N   . LYS   A 1 158 ? 7.832   24.890  16.224  1.00 70.75 ? 170 LYS   A N   1 
ATOM   1071 C  CA  . LYS   A 1 158 ? 8.036   25.132  17.651  1.00 67.70 ? 170 LYS   A CA  1 
ATOM   1072 C  C   . LYS   A 1 158 ? 6.989   24.357  18.458  1.00 61.79 ? 170 LYS   A C   1 
ATOM   1073 O  O   . LYS   A 1 158 ? 6.145   24.916  19.159  1.00 66.17 ? 170 LYS   A O   1 
ATOM   1074 C  CB  . LYS   A 1 158 ? 7.986   26.624  17.950  1.00 71.04 ? 170 LYS   A CB  1 
ATOM   1075 C  CG  . LYS   A 1 158 ? 9.172   27.401  17.411  1.00 76.96 ? 170 LYS   A CG  1 
ATOM   1076 C  CD  . LYS   A 1 158 ? 8.837   28.869  17.263  1.00 81.02 ? 170 LYS   A CD  1 
ATOM   1077 C  CE  . LYS   A 1 158 ? 7.667   29.058  16.314  1.00 85.60 ? 170 LYS   A CE  1 
ATOM   1078 N  NZ  . LYS   A 1 158 ? 7.915   28.411  14.994  1.00 87.13 ? 170 LYS   A NZ  1 
ATOM   1079 N  N   . VAL   A 1 159 ? 7.063   23.031  18.336  1.00 55.07 ? 171 VAL   A N   1 
ATOM   1080 C  CA  . VAL   A 1 159 ? 6.153   22.117  19.015  1.00 44.76 ? 171 VAL   A CA  1 
ATOM   1081 C  C   . VAL   A 1 159 ? 6.433   22.192  20.507  1.00 38.87 ? 171 VAL   A C   1 
ATOM   1082 O  O   . VAL   A 1 159 ? 7.436   22.777  20.929  1.00 41.43 ? 171 VAL   A O   1 
ATOM   1083 C  CB  . VAL   A 1 159 ? 6.309   20.681  18.478  1.00 44.87 ? 171 VAL   A CB  1 
ATOM   1084 C  CG1 . VAL   A 1 159 ? 6.732   20.705  17.013  1.00 50.52 ? 171 VAL   A CG1 1 
ATOM   1085 C  CG2 . VAL   A 1 159 ? 7.297   19.865  19.326  1.00 32.39 ? 171 VAL   A CG2 1 
ATOM   1086 N  N   . LEU   A 1 160 ? 5.548   21.623  21.321  1.00 34.14 ? 172 LEU   A N   1 
ATOM   1087 C  CA  . LEU   A 1 160 ? 5.736   21.691  22.763  1.00 27.68 ? 172 LEU   A CA  1 
ATOM   1088 C  C   . LEU   A 1 160 ? 6.922   20.833  23.192  1.00 26.97 ? 172 LEU   A C   1 
ATOM   1089 O  O   . LEU   A 1 160 ? 7.034   19.663  22.810  1.00 28.02 ? 172 LEU   A O   1 
ATOM   1090 C  CB  . LEU   A 1 160 ? 4.466   21.246  23.484  1.00 30.28 ? 172 LEU   A CB  1 
ATOM   1091 C  CG  . LEU   A 1 160 ? 3.189   22.018  23.155  1.00 31.31 ? 172 LEU   A CG  1 
ATOM   1092 C  CD1 . LEU   A 1 160 ? 2.013   21.444  23.932  1.00 29.31 ? 172 LEU   A CD1 1 
ATOM   1093 C  CD2 . LEU   A 1 160 ? 3.361   23.516  23.431  1.00 30.71 ? 172 LEU   A CD2 1 
ATOM   1094 N  N   . GLY   A 1 161 ? 7.798   21.415  23.995  1.00 27.78 ? 173 GLY   A N   1 
ATOM   1095 C  CA  . GLY   A 1 161 ? 9.009   20.776  24.469  1.00 23.03 ? 173 GLY   A CA  1 
ATOM   1096 C  C   . GLY   A 1 161 ? 10.227  21.615  24.148  1.00 24.05 ? 173 GLY   A C   1 
ATOM   1097 O  O   . GLY   A 1 161 ? 10.129  22.780  23.752  1.00 26.95 ? 173 GLY   A O   1 
ATOM   1098 N  N   . THR   A 1 162 ? 11.399  21.010  24.342  1.00 25.76 ? 174 THR   A N   1 
ATOM   1099 C  CA  . THR   A 1 162 ? 12.667  21.634  23.994  1.00 22.61 ? 174 THR   A CA  1 
ATOM   1100 C  C   . THR   A 1 162 ? 13.529  20.650  23.217  1.00 21.03 ? 174 THR   A C   1 
ATOM   1101 O  O   . THR   A 1 162 ? 13.355  19.432  23.297  1.00 20.27 ? 174 THR   A O   1 
ATOM   1102 C  CB  . THR   A 1 162 ? 13.458  22.119  25.224  1.00 21.58 ? 174 THR   A CB  1 
ATOM   1103 O  OG1 . THR   A 1 162 ? 13.962  21.000  25.963  1.00 26.18 ? 174 THR   A OG1 1 
ATOM   1104 C  CG2 . THR   A 1 162 ? 12.602  22.990  26.126  1.00 24.92 ? 174 THR   A CG2 1 
ATOM   1105 N  N   . PHE   A 1 163 ? 14.494  21.212  22.492  1.00 17.85 ? 175 PHE   A N   1 
ATOM   1106 C  CA  . PHE   A 1 163 ? 15.418  20.474  21.646  1.00 17.55 ? 175 PHE   A CA  1 
ATOM   1107 C  C   . PHE   A 1 163 ? 16.813  21.045  21.857  1.00 23.40 ? 175 PHE   A C   1 
ATOM   1108 O  O   . PHE   A 1 163 ? 16.990  22.265  21.861  1.00 24.97 ? 175 PHE   A O   1 
ATOM   1109 C  CB  . PHE   A 1 163 ? 14.986  20.588  20.164  1.00 21.84 ? 175 PHE   A CB  1 
ATOM   1110 C  CG  . PHE   A 1 163 ? 15.990  20.054  19.181  1.00 20.34 ? 175 PHE   A CG  1 
ATOM   1111 C  CD1 . PHE   A 1 163 ? 15.977  18.719  18.811  1.00 23.03 ? 175 PHE   A CD1 1 
ATOM   1112 C  CD2 . PHE   A 1 163 ? 16.940  20.891  18.613  1.00 21.76 ? 175 PHE   A CD2 1 
ATOM   1113 C  CE1 . PHE   A 1 163 ? 16.898  18.229  17.893  1.00 18.45 ? 175 PHE   A CE1 1 
ATOM   1114 C  CE2 . PHE   A 1 163 ? 17.858  20.410  17.703  1.00 23.05 ? 175 PHE   A CE2 1 
ATOM   1115 C  CZ  . PHE   A 1 163 ? 17.840  19.075  17.346  1.00 22.69 ? 175 PHE   A CZ  1 
ATOM   1116 N  N   . GLU   A 1 164 ? 17.798  20.167  22.036  1.00 21.53 ? 176 GLU   A N   1 
ATOM   1117 C  CA  . GLU   A 1 164 ? 19.179  20.565  22.297  1.00 24.20 ? 176 GLU   A CA  1 
ATOM   1118 C  C   . GLU   A 1 164 ? 20.087  19.923  21.260  1.00 20.11 ? 176 GLU   A C   1 
ATOM   1119 O  O   . GLU   A 1 164 ? 20.161  18.692  21.176  1.00 20.43 ? 176 GLU   A O   1 
ATOM   1120 C  CB  . GLU   A 1 164 ? 19.624  20.142  23.705  1.00 26.80 ? 176 GLU   A CB  1 
ATOM   1121 C  CG  . GLU   A 1 164 ? 18.726  20.616  24.819  1.00 27.72 ? 176 GLU   A CG  1 
ATOM   1122 C  CD  . GLU   A 1 164 ? 19.171  21.939  25.382  1.00 32.76 ? 176 GLU   A CD  1 
ATOM   1123 O  OE1 . GLU   A 1 164 ? 20.267  21.985  25.988  1.00 35.07 ? 176 GLU   A OE1 1 
ATOM   1124 O  OE2 . GLU   A 1 164 ? 18.431  22.930  25.209  1.00 37.13 ? 176 GLU   A OE2 1 
ATOM   1125 N  N   . PHE   A 1 165 ? 20.809  20.743  20.505  1.00 20.77 ? 177 PHE   A N   1 
ATOM   1126 C  CA  . PHE   A 1 165 ? 21.715  20.200  19.504  1.00 19.69 ? 177 PHE   A CA  1 
ATOM   1127 C  C   . PHE   A 1 165 ? 22.870  19.445  20.154  1.00 21.30 ? 177 PHE   A C   1 
ATOM   1128 O  O   . PHE   A 1 165 ? 23.396  19.851  21.193  1.00 19.06 ? 177 PHE   A O   1 
ATOM   1129 C  CB  . PHE   A 1 165 ? 22.268  21.315  18.612  1.00 22.93 ? 177 PHE   A CB  1 
ATOM   1130 C  CG  . PHE   A 1 165 ? 21.429  21.601  17.404  1.00 21.50 ? 177 PHE   A CG  1 
ATOM   1131 C  CD1 . PHE   A 1 165 ? 21.395  20.713  16.346  1.00 24.19 ? 177 PHE   A CD1 1 
ATOM   1132 C  CD2 . PHE   A 1 165 ? 20.698  22.773  17.318  1.00 23.39 ? 177 PHE   A CD2 1 
ATOM   1133 C  CE1 . PHE   A 1 165 ? 20.620  20.983  15.214  1.00 25.24 ? 177 PHE   A CE1 1 
ATOM   1134 C  CE2 . PHE   A 1 165 ? 19.929  23.060  16.191  1.00 21.82 ? 177 PHE   A CE2 1 
ATOM   1135 C  CZ  . PHE   A 1 165 ? 19.895  22.164  15.137  1.00 25.41 ? 177 PHE   A CZ  1 
ATOM   1136 N  N   . ASP   A 1 166 ? 23.261  18.338  19.529  1.00 19.82 ? 178 ASP   A N   1 
ATOM   1137 C  CA  . ASP   A 1 166 ? 24.492  17.629  19.869  1.00 23.69 ? 178 ASP   A CA  1 
ATOM   1138 C  C   . ASP   A 1 166 ? 25.624  18.234  19.043  1.00 22.29 ? 178 ASP   A C   1 
ATOM   1139 O  O   . ASP   A 1 166 ? 25.701  18.022  17.830  1.00 24.19 ? 178 ASP   A O   1 
ATOM   1140 C  CB  . ASP   A 1 166 ? 24.338  16.133  19.597  1.00 23.67 ? 178 ASP   A CB  1 
ATOM   1141 C  CG  . ASP   A 1 166 ? 25.619  15.344  19.835  1.00 23.90 ? 178 ASP   A CG  1 
ATOM   1142 O  OD1 . ASP   A 1 166 ? 26.655  15.927  20.231  1.00 25.01 ? 178 ASP   A OD1 1 
ATOM   1143 O  OD2 . ASP   A 1 166 ? 25.585  14.117  19.611  1.00 25.89 ? 178 ASP   A OD2 1 
ATOM   1144 N  N   . GLU   A 1 167 ? 26.525  18.956  19.718  1.00 23.69 ? 179 GLU   A N   1 
ATOM   1145 C  CA  . GLU   A 1 167 ? 27.576  19.701  19.027  1.00 24.11 ? 179 GLU   A CA  1 
ATOM   1146 C  C   . GLU   A 1 167 ? 28.500  18.799  18.211  1.00 27.28 ? 179 GLU   A C   1 
ATOM   1147 O  O   . GLU   A 1 167 ? 29.123  19.266  17.252  1.00 27.95 ? 179 GLU   A O   1 
ATOM   1148 C  CB  . GLU   A 1 167 ? 28.398  20.500  20.043  1.00 28.26 ? 179 GLU   A CB  1 
ATOM   1149 C  CG  . GLU   A 1 167 ? 29.006  19.622  21.136  1.00 29.07 ? 179 GLU   A CG  1 
ATOM   1150 C  CD  . GLU   A 1 167 ? 30.179  20.273  21.852  1.00 34.91 ? 179 GLU   A CD  1 
ATOM   1151 O  OE1 . GLU   A 1 167 ? 30.212  21.518  21.927  1.00 36.61 ? 179 GLU   A OE1 1 
ATOM   1152 O  OE2 . GLU   A 1 167 ? 31.065  19.537  22.340  1.00 34.08 ? 179 GLU   A OE2 1 
ATOM   1153 N  N   . THR   A 1 168 ? 28.616  17.517  18.580  1.00 25.37 ? 180 THR   A N   1 
ATOM   1154 C  CA  . THR   A 1 168 ? 29.463  16.580  17.849  1.00 27.42 ? 180 THR   A CA  1 
ATOM   1155 C  C   . THR   A 1 168 ? 28.923  16.246  16.466  1.00 32.10 ? 180 THR   A C   1 
ATOM   1156 O  O   . THR   A 1 168 ? 29.657  15.657  15.663  1.00 33.49 ? 180 THR   A O   1 
ATOM   1157 C  CB  . THR   A 1 168 ? 29.640  15.267  18.627  1.00 26.06 ? 180 THR   A CB  1 
ATOM   1158 O  OG1 . THR   A 1 168 ? 28.372  14.615  18.776  1.00 27.83 ? 180 THR   A OG1 1 
ATOM   1159 C  CG2 . THR   A 1 168 ? 30.275  15.500  19.984  1.00 30.87 ? 180 THR   A CG2 1 
ATOM   1160 N  N   . SER   A 1 169 ? 27.670  16.580  16.176  1.00 27.47 ? 181 SER   A N   1 
ATOM   1161 C  CA  . SER   A 1 169 ? 27.086  16.325  14.865  1.00 31.55 ? 181 SER   A CA  1 
ATOM   1162 C  C   . SER   A 1 169 ? 27.250  17.504  13.912  1.00 33.91 ? 181 SER   A C   1 
ATOM   1163 O  O   . SER   A 1 169 ? 26.782  17.429  12.771  1.00 33.82 ? 181 SER   A O   1 
ATOM   1164 C  CB  . SER   A 1 169 ? 25.599  15.968  15.000  1.00 29.35 ? 181 SER   A CB  1 
ATOM   1165 O  OG  . SER   A 1 169 ? 24.828  17.122  15.284  1.00 24.87 ? 181 SER   A OG  1 
ATOM   1166 N  N   . PHE   A 1 170 ? 27.897  18.589  14.352  1.00 32.52 ? 182 PHE   A N   1 
ATOM   1167 C  CA  . PHE   A 1 170 ? 28.017  19.773  13.505  1.00 35.20 ? 182 PHE   A CA  1 
ATOM   1168 C  C   . PHE   A 1 170 ? 29.002  19.552  12.363  1.00 40.93 ? 182 PHE   A C   1 
ATOM   1169 O  O   . PHE   A 1 170 ? 28.733  19.944  11.221  1.00 42.09 ? 182 PHE   A O   1 
ATOM   1170 C  CB  . PHE   A 1 170 ? 28.452  20.984  14.339  1.00 33.78 ? 182 PHE   A CB  1 
ATOM   1171 C  CG  . PHE   A 1 170 ? 27.423  21.452  15.339  1.00 29.59 ? 182 PHE   A CG  1 
ATOM   1172 C  CD1 . PHE   A 1 170 ? 26.105  21.042  15.249  1.00 30.11 ? 182 PHE   A CD1 1 
ATOM   1173 C  CD2 . PHE   A 1 170 ? 27.780  22.322  16.362  1.00 29.28 ? 182 PHE   A CD2 1 
ATOM   1174 C  CE1 . PHE   A 1 170 ? 25.159  21.479  16.173  1.00 31.61 ? 182 PHE   A CE1 1 
ATOM   1175 C  CE2 . PHE   A 1 170 ? 26.842  22.768  17.283  1.00 28.52 ? 182 PHE   A CE2 1 
ATOM   1176 C  CZ  . PHE   A 1 170 ? 25.531  22.343  17.194  1.00 27.83 ? 182 PHE   A CZ  1 
ATOM   1177 N  N   . TRP   A 1 171 ? 30.149  18.929  12.650  1.00 40.35 ? 183 TRP   A N   1 
ATOM   1178 C  CA  . TRP   A 1 171 ? 31.289  18.909  11.739  1.00 45.64 ? 183 TRP   A CA  1 
ATOM   1179 C  C   . TRP   A 1 171 ? 31.537  17.546  11.103  1.00 50.75 ? 183 TRP   A C   1 
ATOM   1180 O  O   . TRP   A 1 171 ? 32.566  17.362  10.445  1.00 55.80 ? 183 TRP   A O   1 
ATOM   1181 C  CB  . TRP   A 1 171 ? 32.559  19.362  12.467  1.00 47.87 ? 183 TRP   A CB  1 
ATOM   1182 C  CG  . TRP   A 1 171 ? 32.351  20.480  13.442  1.00 43.92 ? 183 TRP   A CG  1 
ATOM   1183 C  CD1 . TRP   A 1 171 ? 32.221  21.810  13.154  1.00 44.15 ? 183 TRP   A CD1 1 
ATOM   1184 C  CD2 . TRP   A 1 171 ? 32.265  20.367  14.867  1.00 42.22 ? 183 TRP   A CD2 1 
ATOM   1185 N  NE1 . TRP   A 1 171 ? 32.048  22.530  14.312  1.00 42.08 ? 183 TRP   A NE1 1 
ATOM   1186 C  CE2 . TRP   A 1 171 ? 32.070  21.667  15.378  1.00 42.63 ? 183 TRP   A CE2 1 
ATOM   1187 C  CE3 . TRP   A 1 171 ? 32.326  19.292  15.761  1.00 40.21 ? 183 TRP   A CE3 1 
ATOM   1188 C  CZ2 . TRP   A 1 171 ? 31.939  21.922  16.746  1.00 42.81 ? 183 TRP   A CZ2 1 
ATOM   1189 C  CZ3 . TRP   A 1 171 ? 32.196  19.546  17.120  1.00 41.78 ? 183 TRP   A CZ3 1 
ATOM   1190 C  CH2 . TRP   A 1 171 ? 32.004  20.851  17.599  1.00 37.54 ? 183 TRP   A CH2 1 
ATOM   1191 N  N   . ASN   A 1 172 ? 30.631  16.586  11.277  1.00 55.79 ? 184 ASN   A N   1 
ATOM   1192 C  CA  . ASN   A 1 172 ? 30.813  15.253  10.718  1.00 55.88 ? 184 ASN   A CA  1 
ATOM   1193 C  C   . ASN   A 1 172 ? 29.798  14.895  9.644   1.00 62.08 ? 184 ASN   A C   1 
ATOM   1194 O  O   . ASN   A 1 172 ? 30.115  14.106  8.752   1.00 61.78 ? 184 ASN   A O   1 
ATOM   1195 C  CB  . ASN   A 1 172 ? 30.754  14.198  11.831  1.00 56.00 ? 184 ASN   A CB  1 
ATOM   1196 C  CG  . ASN   A 1 172 ? 29.533  14.354  12.719  1.00 49.51 ? 184 ASN   A CG  1 
ATOM   1197 O  OD1 . ASN   A 1 172 ? 28.563  15.012  12.350  1.00 48.93 ? 184 ASN   A OD1 1 
ATOM   1198 N  ND2 . ASN   A 1 172 ? 29.577  13.745  13.899  1.00 48.26 ? 184 ASN   A ND2 1 
ATOM   1199 N  N   . SER   A 1 173 ? 28.598  15.457  9.704   1.00 55.45 ? 185 SER   A N   1 
ATOM   1200 C  CA  . SER   A 1 173 ? 27.525  15.156  8.770   1.00 55.64 ? 185 SER   A CA  1 
ATOM   1201 C  C   . SER   A 1 173 ? 27.143  16.427  8.011   1.00 57.16 ? 185 SER   A C   1 
ATOM   1202 O  O   . SER   A 1 173 ? 27.820  17.456  8.093   1.00 55.07 ? 185 SER   A O   1 
ATOM   1203 C  CB  . SER   A 1 173 ? 26.331  14.554  9.513   1.00 58.36 ? 185 SER   A CB  1 
ATOM   1204 O  OG  . SER   A 1 173 ? 25.890  15.410  10.557  1.00 52.05 ? 185 SER   A OG  1 
ATOM   1205 N  N   . SER   A 1 174 ? 26.055  16.339  7.245   1.00 58.41 ? 186 SER   A N   1 
ATOM   1206 C  CA  . SER   A 1 174 ? 25.496  17.502  6.569   1.00 59.90 ? 186 SER   A CA  1 
ATOM   1207 C  C   . SER   A 1 174 ? 24.255  18.045  7.259   1.00 56.87 ? 186 SER   A C   1 
ATOM   1208 O  O   . SER   A 1 174 ? 23.886  19.201  7.022   1.00 57.18 ? 186 SER   A O   1 
ATOM   1209 C  CB  . SER   A 1 174 ? 25.150  17.163  5.114   1.00 62.24 ? 186 SER   A CB  1 
ATOM   1210 O  OG  . SER   A 1 174 ? 24.100  16.214  5.046   1.00 66.51 ? 186 SER   A OG  1 
ATOM   1211 N  N   . HIS   A 1 175 ? 23.613  17.244  8.098   1.00 55.53 ? 187 HIS   A N   1 
ATOM   1212 C  CA  . HIS   A 1 175 ? 22.411  17.646  8.823   1.00 52.45 ? 187 HIS   A CA  1 
ATOM   1213 C  C   . HIS   A 1 175 ? 22.667  17.470  10.313  1.00 48.77 ? 187 HIS   A C   1 
ATOM   1214 O  O   . HIS   A 1 175 ? 22.840  16.325  10.772  1.00 48.97 ? 187 HIS   A O   1 
ATOM   1215 C  CB  . HIS   A 1 175 ? 21.216  16.805  8.371   1.00 53.14 ? 187 HIS   A CB  1 
ATOM   1216 C  CG  . HIS   A 1 175 ? 19.901  17.516  8.455   1.00 53.07 ? 187 HIS   A CG  1 
ATOM   1217 N  ND1 . HIS   A 1 175 ? 18.729  16.967  7.978   1.00 49.56 ? 187 HIS   A ND1 1 
ATOM   1218 C  CD2 . HIS   A 1 175 ? 19.570  18.729  8.957   1.00 53.09 ? 187 HIS   A CD2 1 
ATOM   1219 C  CE1 . HIS   A 1 175 ? 17.733  17.810  8.185   1.00 47.55 ? 187 HIS   A CE1 1 
ATOM   1220 N  NE2 . HIS   A 1 175 ? 18.217  18.887  8.778   1.00 52.62 ? 187 HIS   A NE2 1 
ATOM   1221 N  N   . PRO   A 1 176 ? 22.720  18.542  11.103  1.00 39.63 ? 188 PRO   A N   1 
ATOM   1222 C  CA  . PRO   A 1 176 ? 22.988  18.389  12.539  1.00 34.67 ? 188 PRO   A CA  1 
ATOM   1223 C  C   . PRO   A 1 176 ? 21.801  17.755  13.248  1.00 32.47 ? 188 PRO   A C   1 
ATOM   1224 O  O   . PRO   A 1 176 ? 20.683  17.709  12.730  1.00 25.47 ? 188 PRO   A O   1 
ATOM   1225 C  CB  . PRO   A 1 176 ? 23.218  19.826  13.014  1.00 33.83 ? 188 PRO   A CB  1 
ATOM   1226 C  CG  . PRO   A 1 176 ? 22.387  20.652  12.064  1.00 38.70 ? 188 PRO   A CG  1 
ATOM   1227 C  CD  . PRO   A 1 176 ? 22.447  19.942  10.732  1.00 40.60 ? 188 PRO   A CD  1 
ATOM   1228 N  N   . ARG   A 1 177 ? 22.062  17.219  14.437  1.00 25.10 ? 189 ARG   A N   1 
ATOM   1229 C  CA  . ARG   A 1 177 ? 21.028  16.481  15.150  1.00 24.01 ? 189 ARG   A CA  1 
ATOM   1230 C  C   . ARG   A 1 177 ? 21.153  16.749  16.643  1.00 23.01 ? 189 ARG   A C   1 
ATOM   1231 O  O   . ARG   A 1 177 ? 22.184  17.226  17.126  1.00 24.20 ? 189 ARG   A O   1 
ATOM   1232 C  CB  . ARG   A 1 177 ? 21.112  14.977  14.838  1.00 23.70 ? 189 ARG   A CB  1 
ATOM   1233 C  CG  . ARG   A 1 177 ? 20.961  14.661  13.337  1.00 26.26 ? 189 ARG   A CG  1 
ATOM   1234 C  CD  . ARG   A 1 177 ? 20.828  13.184  13.044  1.00 24.64 ? 189 ARG   A CD  1 
ATOM   1235 N  NE  . ARG   A 1 177 ? 21.992  12.428  13.484  1.00 28.82 ? 189 ARG   A NE  1 
ATOM   1236 C  CZ  . ARG   A 1 177 ? 22.059  11.103  13.483  1.00 30.01 ? 189 ARG   A CZ  1 
ATOM   1237 N  NH1 . ARG   A 1 177 ? 21.065  10.365  13.013  1.00 27.71 ? 189 ARG   A NH1 1 
ATOM   1238 N  NH2 . ARG   A 1 177 ? 23.141  10.505  13.982  1.00 26.36 ? 189 ARG   A NH2 1 
ATOM   1239 N  N   . GLY   A 1 178 ? 20.084  16.446  17.375  1.00 22.93 ? 190 GLY   A N   1 
ATOM   1240 C  CA  . GLY   A 1 178 ? 20.088  16.705  18.794  1.00 18.95 ? 190 GLY   A CA  1 
ATOM   1241 C  C   . GLY   A 1 178 ? 19.013  15.918  19.515  1.00 18.01 ? 190 GLY   A C   1 
ATOM   1242 O  O   . GLY   A 1 178 ? 18.325  15.086  18.927  1.00 14.53 ? 190 GLY   A O   1 
ATOM   1243 N  N   . TRP   A 1 179 ? 18.893  16.199  20.808  1.00 15.96 ? 191 TRP   A N   1 
ATOM   1244 C  CA  . TRP   A 1 179 ? 17.975  15.522  21.713  1.00 14.97 ? 191 TRP   A CA  1 
ATOM   1245 C  C   . TRP   A 1 179 ? 16.733  16.372  21.961  1.00 17.74 ? 191 TRP   A C   1 
ATOM   1246 O  O   . TRP   A 1 179 ? 16.789  17.605  21.969  1.00 16.35 ? 191 TRP   A O   1 
ATOM   1247 C  CB  . TRP   A 1 179 ? 18.665  15.230  23.056  1.00 18.00 ? 191 TRP   A CB  1 
ATOM   1248 C  CG  . TRP   A 1 179 ? 19.956  14.466  22.941  1.00 19.42 ? 191 TRP   A CG  1 
ATOM   1249 C  CD1 . TRP   A 1 179 ? 20.101  13.108  22.848  1.00 18.69 ? 191 TRP   A CD1 1 
ATOM   1250 C  CD2 . TRP   A 1 179 ? 21.286  15.010  22.943  1.00 18.94 ? 191 TRP   A CD2 1 
ATOM   1251 N  NE1 . TRP   A 1 179 ? 21.430  12.780  22.765  1.00 17.79 ? 191 TRP   A NE1 1 
ATOM   1252 C  CE2 . TRP   A 1 179 ? 22.179  13.926  22.832  1.00 17.44 ? 191 TRP   A CE2 1 
ATOM   1253 C  CE3 . TRP   A 1 179 ? 21.804  16.311  23.016  1.00 18.90 ? 191 TRP   A CE3 1 
ATOM   1254 C  CZ2 . TRP   A 1 179 ? 23.564  14.098  22.794  1.00 18.93 ? 191 TRP   A CZ2 1 
ATOM   1255 C  CZ3 . TRP   A 1 179 ? 23.191  16.478  22.983  1.00 17.87 ? 191 TRP   A CZ3 1 
ATOM   1256 C  CH2 . TRP   A 1 179 ? 24.045  15.379  22.881  1.00 17.25 ? 191 TRP   A CH2 1 
ATOM   1257 N  N   . ASN   A 1 180 ? 15.608  15.698  22.193  1.00 17.72 ? 192 ASN   A N   1 
ATOM   1258 C  CA  . ASN   A 1 180 ? 14.386  16.377  22.579  1.00 16.43 ? 192 ASN   A CA  1 
ATOM   1259 C  C   . ASN   A 1 180 ? 13.788  15.741  23.829  1.00 17.22 ? 192 ASN   A C   1 
ATOM   1260 O  O   . ASN   A 1 180 ? 14.104  14.604  24.203  1.00 14.61 ? 192 ASN   A O   1 
ATOM   1261 C  CB  . ASN   A 1 180 ? 13.335  16.359  21.459  1.00 13.59 ? 192 ASN   A CB  1 
ATOM   1262 C  CG  . ASN   A 1 180 ? 12.755  14.969  21.229  1.00 15.07 ? 192 ASN   A CG  1 
ATOM   1263 O  OD1 . ASN   A 1 180 ? 11.773  14.596  21.864  1.00 14.21 ? 192 ASN   A OD1 1 
ATOM   1264 N  ND2 . ASN   A 1 180 ? 13.361  14.193  20.315  1.00 17.73 ? 192 ASN   A ND2 1 
ATOM   1265 N  N   . ASP   A 1 181 ? 12.904  16.501  24.472  1.00 16.03 ? 193 ASP   A N   1 
ATOM   1266 C  CA  . ASP   A 1 181 ? 12.097  15.998  25.579  1.00 16.78 ? 193 ASP   A CA  1 
ATOM   1267 C  C   . ASP   A 1 181 ? 10.622  15.928  25.207  1.00 14.69 ? 193 ASP   A C   1 
ATOM   1268 O  O   . ASP   A 1 181 ? 9.754   15.973  26.092  1.00 16.58 ? 193 ASP   A O   1 
ATOM   1269 C  CB  . ASP   A 1 181 ? 12.286  16.861  26.831  1.00 21.68 ? 193 ASP   A CB  1 
ATOM   1270 C  CG  . ASP   A 1 181 ? 11.816  18.299  26.636  1.00 23.62 ? 193 ASP   A CG  1 
ATOM   1271 O  OD1 . ASP   A 1 181 ? 11.398  18.669  25.519  1.00 19.25 ? 193 ASP   A OD1 1 
ATOM   1272 O  OD2 . ASP   A 1 181 ? 11.881  19.076  27.607  1.00 27.90 ? 193 ASP   A OD2 1 
ATOM   1273 N  N   . HIS   A 1 182 ? 10.321  15.854  23.906  1.00 14.08 ? 194 HIS   A N   1 
ATOM   1274 C  CA  . HIS   A 1 182 ? 8.939   15.943  23.461  1.00 16.10 ? 194 HIS   A CA  1 
ATOM   1275 C  C   . HIS   A 1 182 ? 8.117   14.745  23.925  1.00 15.66 ? 194 HIS   A C   1 
ATOM   1276 O  O   . HIS   A 1 182 ? 8.600   13.612  23.955  1.00 14.67 ? 194 HIS   A O   1 
ATOM   1277 C  CB  . HIS   A 1 182 ? 8.889   16.048  21.932  1.00 17.24 ? 194 HIS   A CB  1 
ATOM   1278 C  CG  . HIS   A 1 182 ? 9.603   17.248  21.388  1.00 20.72 ? 194 HIS   A CG  1 
ATOM   1279 N  ND1 . HIS   A 1 182 ? 9.762   17.471  20.036  1.00 23.01 ? 194 HIS   A ND1 1 
ATOM   1280 C  CD2 . HIS   A 1 182 ? 10.187  18.297  22.013  1.00 21.25 ? 194 HIS   A CD2 1 
ATOM   1281 C  CE1 . HIS   A 1 182 ? 10.414  18.608  19.853  1.00 18.88 ? 194 HIS   A CE1 1 
ATOM   1282 N  NE2 . HIS   A 1 182 ? 10.690  19.124  21.038  1.00 20.19 ? 194 HIS   A NE2 1 
ATOM   1283 N  N   . VAL   A 1 183 ? 6.860   15.001  24.288  1.00 15.38 ? 195 VAL   A N   1 
ATOM   1284 C  CA  . VAL   A 1 183 ? 5.853   13.957  24.474  1.00 13.78 ? 195 VAL   A CA  1 
ATOM   1285 C  C   . VAL   A 1 183 ? 4.848   14.075  23.332  1.00 13.00 ? 195 VAL   A C   1 
ATOM   1286 O  O   . VAL   A 1 183 ? 4.317   15.160  23.084  1.00 15.68 ? 195 VAL   A O   1 
ATOM   1287 C  CB  . VAL   A 1 183 ? 5.148   14.081  25.838  1.00 13.00 ? 195 VAL   A CB  1 
ATOM   1288 C  CG1 . VAL   A 1 183 ? 4.043   13.056  25.973  1.00 13.19 ? 195 VAL   A CG1 1 
ATOM   1289 C  CG2 . VAL   A 1 183 ? 6.177   13.930  26.997  1.00 12.53 ? 195 VAL   A CG2 1 
ATOM   1290 N  N   . HIS   A 1 184 ? 4.613   12.978  22.619  1.00 13.33 ? 196 HIS   A N   1 
ATOM   1291 C  CA  . HIS   A 1 184 ? 3.608   12.983  21.557  1.00 14.22 ? 196 HIS   A CA  1 
ATOM   1292 C  C   . HIS   A 1 184 ? 2.635   11.837  21.766  1.00 14.10 ? 196 HIS   A C   1 
ATOM   1293 O  O   . HIS   A 1 184 ? 3.028   10.736  22.168  1.00 14.77 ? 196 HIS   A O   1 
ATOM   1294 C  CB  . HIS   A 1 184 ? 4.239   12.872  20.160  1.00 17.83 ? 196 HIS   A CB  1 
ATOM   1295 C  CG  . HIS   A 1 184 ? 4.840   14.149  19.664  1.00 17.31 ? 196 HIS   A CG  1 
ATOM   1296 N  ND1 . HIS   A 1 184 ? 6.085   14.587  20.058  1.00 18.70 ? 196 HIS   A ND1 1 
ATOM   1297 C  CD2 . HIS   A 1 184 ? 4.375   15.076  18.791  1.00 18.17 ? 196 HIS   A CD2 1 
ATOM   1298 C  CE1 . HIS   A 1 184 ? 6.361   15.728  19.455  1.00 17.33 ? 196 HIS   A CE1 1 
ATOM   1299 N  NE2 . HIS   A 1 184 ? 5.338   16.050  18.686  1.00 17.24 ? 196 HIS   A NE2 1 
ATOM   1300 N  N   . ILE   A 1 185 ? 1.364   12.094  21.472  1.00 15.26 ? 197 ILE   A N   1 
ATOM   1301 C  CA  . ILE   A 1 185 ? 0.325   11.077  21.524  1.00 14.07 ? 197 ILE   A CA  1 
ATOM   1302 C  C   . ILE   A 1 185 ? -0.054  10.713  20.097  1.00 14.78 ? 197 ILE   A C   1 
ATOM   1303 O  O   . ILE   A 1 185 ? -0.398  11.594  19.302  1.00 14.10 ? 197 ILE   A O   1 
ATOM   1304 C  CB  . ILE   A 1 185 ? -0.916  11.562  22.289  1.00 17.31 ? 197 ILE   A CB  1 
ATOM   1305 C  CG1 . ILE   A 1 185 ? -0.586  11.804  23.770  1.00 19.65 ? 197 ILE   A CG1 1 
ATOM   1306 C  CG2 . ILE   A 1 185 ? -2.048  10.560  22.092  1.00 18.89 ? 197 ILE   A CG2 1 
ATOM   1307 C  CD1 . ILE   A 1 185 ? -1.633  12.615  24.521  1.00 20.17 ? 197 ILE   A CD1 1 
ATOM   1308 N  N   . LEU   A 1 186 ? 0.008   9.424   19.780  1.00 13.70 ? 198 LEU   A N   1 
ATOM   1309 C  CA  . LEU   A 1 186 ? -0.678  8.870   18.618  1.00 16.67 ? 198 LEU   A CA  1 
ATOM   1310 C  C   . LEU   A 1 186 ? -1.915  8.149   19.135  1.00 16.40 ? 198 LEU   A C   1 
ATOM   1311 O  O   . LEU   A 1 186 ? -1.799  7.158   19.872  1.00 16.85 ? 198 LEU   A O   1 
ATOM   1312 C  CB  . LEU   A 1 186 ? 0.229   7.930   17.825  1.00 14.58 ? 198 LEU   A CB  1 
ATOM   1313 C  CG  . LEU   A 1 186 ? -0.193  7.476   16.414  1.00 17.41 ? 198 LEU   A CG  1 
ATOM   1314 C  CD1 . LEU   A 1 186 ? -1.217  6.346   16.473  1.00 21.80 ? 198 LEU   A CD1 1 
ATOM   1315 C  CD2 . LEU   A 1 186 ? -0.702  8.653   15.537  1.00 16.56 ? 198 LEU   A CD2 1 
ATOM   1316 N  N   . ASP   A 1 187 ? -3.087  8.664   18.762  1.00 20.55 ? 199 ASP   A N   1 
ATOM   1317 C  CA  . ASP   A 1 187 ? -4.376  8.110   19.162  1.00 19.27 ? 199 ASP   A CA  1 
ATOM   1318 C  C   . ASP   A 1 187 ? -4.790  7.092   18.109  1.00 18.47 ? 199 ASP   A C   1 
ATOM   1319 O  O   . ASP   A 1 187 ? -5.068  7.465   16.964  1.00 20.20 ? 199 ASP   A O   1 
ATOM   1320 C  CB  . ASP   A 1 187 ? -5.403  9.238   19.288  1.00 21.00 ? 199 ASP   A CB  1 
ATOM   1321 C  CG  . ASP   A 1 187 ? -6.760  8.766   19.790  1.00 22.55 ? 199 ASP   A CG  1 
ATOM   1322 O  OD1 . ASP   A 1 187 ? -7.086  7.567   19.668  1.00 21.27 ? 199 ASP   A OD1 1 
ATOM   1323 O  OD2 . ASP   A 1 187 ? -7.507  9.619   20.316  1.00 24.97 ? 199 ASP   A OD2 1 
ATOM   1324 N  N   . THR   A 1 188 ? -4.843  5.811   18.484  1.00 18.93 ? 200 THR   A N   1 
ATOM   1325 C  CA  . THR   A 1 188 ? -5.196  4.776   17.507  1.00 19.90 ? 200 THR   A CA  1 
ATOM   1326 C  C   . THR   A 1 188 ? -6.692  4.710   17.196  1.00 19.73 ? 200 THR   A C   1 
ATOM   1327 O  O   . THR   A 1 188 ? -7.083  3.901   16.347  1.00 17.92 ? 200 THR   A O   1 
ATOM   1328 C  CB  . THR   A 1 188 ? -4.732  3.390   17.965  1.00 20.77 ? 200 THR   A CB  1 
ATOM   1329 O  OG1 . THR   A 1 188 ? -5.318  3.074   19.240  1.00 22.25 ? 200 THR   A OG1 1 
ATOM   1330 C  CG2 . THR   A 1 188 ? -3.200  3.334   18.082  1.00 21.51 ? 200 THR   A CG2 1 
ATOM   1331 N  N   . GLU   A 1 189 ? -7.544  5.501   17.859  1.00 19.02 ? 201 GLU   A N   1 
ATOM   1332 C  CA  . GLU   A 1 189 ? -8.929  5.592   17.385  1.00 17.20 ? 201 GLU   A CA  1 
ATOM   1333 C  C   . GLU   A 1 189 ? -9.012  6.315   16.045  1.00 18.19 ? 201 GLU   A C   1 
ATOM   1334 O  O   . GLU   A 1 189 ? -9.888  6.006   15.233  1.00 22.78 ? 201 GLU   A O   1 
ATOM   1335 C  CB  . GLU   A 1 189 ? -9.822  6.296   18.410  1.00 24.47 ? 201 GLU   A CB  1 
ATOM   1336 C  CG  . GLU   A 1 189 ? -10.242 5.411   19.588  1.00 19.11 ? 201 GLU   A CG  1 
ATOM   1337 C  CD  . GLU   A 1 189 ? -10.715 6.191   20.827  1.00 21.93 ? 201 GLU   A CD  1 
ATOM   1338 O  OE1 . GLU   A 1 189 ? -11.098 7.380   20.715  1.00 24.72 ? 201 GLU   A OE1 1 
ATOM   1339 O  OE2 . GLU   A 1 189 ? -10.704 5.593   21.926  1.00 25.40 ? 201 GLU   A OE2 1 
ATOM   1340 N  N   . THR   A 1 190 ? -8.112  7.268   15.787  1.00 22.49 ? 202 THR   A N   1 
ATOM   1341 C  CA  . THR   A 1 190 ? -8.161  8.050   14.555  1.00 19.56 ? 202 THR   A CA  1 
ATOM   1342 C  C   . THR   A 1 190 ? -6.828  8.174   13.839  1.00 23.25 ? 202 THR   A C   1 
ATOM   1343 O  O   . THR   A 1 190 ? -6.774  8.858   12.805  1.00 21.55 ? 202 THR   A O   1 
ATOM   1344 C  CB  . THR   A 1 190 ? -8.666  9.468   14.840  1.00 20.95 ? 202 THR   A CB  1 
ATOM   1345 O  OG1 . THR   A 1 190 ? -7.818  10.077  15.827  1.00 23.46 ? 202 THR   A OG1 1 
ATOM   1346 C  CG2 . THR   A 1 190 ? -10.105 9.445   15.334  1.00 21.72 ? 202 THR   A CG2 1 
ATOM   1347 N  N   . PHE   A 1 191 ? -5.758  7.559   14.356  1.00 18.23 ? 203 PHE   A N   1 
ATOM   1348 C  CA  . PHE   A 1 191 ? -4.397  7.788   13.877  1.00 20.07 ? 203 PHE   A CA  1 
ATOM   1349 C  C   . PHE   A 1 191 ? -4.134  9.285   13.740  1.00 24.02 ? 203 PHE   A C   1 
ATOM   1350 O  O   . PHE   A 1 191 ? -3.817  9.804   12.667  1.00 22.63 ? 203 PHE   A O   1 
ATOM   1351 C  CB  . PHE   A 1 191 ? -4.137  7.041   12.565  1.00 22.08 ? 203 PHE   A CB  1 
ATOM   1352 C  CG  . PHE   A 1 191 ? -4.261  5.571   12.708  1.00 22.27 ? 203 PHE   A CG  1 
ATOM   1353 C  CD1 . PHE   A 1 191 ? -3.225  4.831   13.249  1.00 21.99 ? 203 PHE   A CD1 1 
ATOM   1354 C  CD2 . PHE   A 1 191 ? -5.440  4.932   12.374  1.00 27.31 ? 203 PHE   A CD2 1 
ATOM   1355 C  CE1 . PHE   A 1 191 ? -3.352  3.475   13.420  1.00 24.39 ? 203 PHE   A CE1 1 
ATOM   1356 C  CE2 . PHE   A 1 191 ? -5.569  3.575   12.539  1.00 26.45 ? 203 PHE   A CE2 1 
ATOM   1357 C  CZ  . PHE   A 1 191 ? -4.537  2.846   13.066  1.00 23.92 ? 203 PHE   A CZ  1 
ATOM   1358 N  N   . THR   A 1 192 ? -4.318  9.978   14.861  1.00 19.25 ? 204 THR   A N   1 
ATOM   1359 C  CA  . THR   A 1 192 ? -4.112  11.417  14.951  1.00 20.29 ? 204 THR   A CA  1 
ATOM   1360 C  C   . THR   A 1 192 ? -3.025  11.719  15.976  1.00 16.64 ? 204 THR   A C   1 
ATOM   1361 O  O   . THR   A 1 192 ? -3.124  11.289  17.132  1.00 16.41 ? 204 THR   A O   1 
ATOM   1362 C  CB  . THR   A 1 192 ? -5.405  12.133  15.345  1.00 21.73 ? 204 THR   A CB  1 
ATOM   1363 O  OG1 . THR   A 1 192 ? -6.420  11.896  14.350  1.00 21.34 ? 204 THR   A OG1 1 
ATOM   1364 C  CG2 . THR   A 1 192 ? -5.164  13.631  15.501  1.00 20.59 ? 204 THR   A CG2 1 
ATOM   1365 N  N   . TRP   A 1 193 ? -2.011  12.469  15.546  1.00 15.18 ? 205 TRP   A N   1 
ATOM   1366 C  CA  . TRP   A 1 193 ? -0.973  12.986  16.434  1.00 19.04 ? 205 TRP   A CA  1 
ATOM   1367 C  C   . TRP   A 1 193 ? -1.481  14.182  17.236  1.00 19.16 ? 205 TRP   A C   1 
ATOM   1368 O  O   . TRP   A 1 193 ? -2.145  15.075  16.698  1.00 22.36 ? 205 TRP   A O   1 
ATOM   1369 C  CB  . TRP   A 1 193 ? 0.256   13.412  15.620  1.00 18.67 ? 205 TRP   A CB  1 
ATOM   1370 C  CG  . TRP   A 1 193 ? 1.042   12.287  14.988  1.00 20.15 ? 205 TRP   A CG  1 
ATOM   1371 C  CD1 . TRP   A 1 193 ? 1.078   11.935  13.655  1.00 20.46 ? 205 TRP   A CD1 1 
ATOM   1372 C  CD2 . TRP   A 1 193 ? 1.917   11.379  15.662  1.00 18.17 ? 205 TRP   A CD2 1 
ATOM   1373 N  NE1 . TRP   A 1 193 ? 1.925   10.863  13.472  1.00 17.30 ? 205 TRP   A NE1 1 
ATOM   1374 C  CE2 . TRP   A 1 193 ? 2.451   10.504  14.687  1.00 16.63 ? 205 TRP   A CE2 1 
ATOM   1375 C  CE3 . TRP   A 1 193 ? 2.295   11.213  16.999  1.00 18.76 ? 205 TRP   A CE3 1 
ATOM   1376 C  CZ2 . TRP   A 1 193 ? 3.343   9.483   15.012  1.00 17.85 ? 205 TRP   A CZ2 1 
ATOM   1377 C  CZ3 . TRP   A 1 193 ? 3.182   10.192  17.321  1.00 17.35 ? 205 TRP   A CZ3 1 
ATOM   1378 C  CH2 . TRP   A 1 193 ? 3.697   9.345   16.330  1.00 15.23 ? 205 TRP   A CH2 1 
ATOM   1379 N  N   . SER   A 1 194 ? -1.146  14.210  18.525  1.00 16.58 ? 206 SER   A N   1 
ATOM   1380 C  CA  . SER   A 1 194 ? -1.365  15.382  19.358  1.00 17.19 ? 206 SER   A CA  1 
ATOM   1381 C  C   . SER   A 1 194 ? -0.238  15.437  20.376  1.00 15.45 ? 206 SER   A C   1 
ATOM   1382 O  O   . SER   A 1 194 ? 0.584   14.526  20.457  1.00 17.61 ? 206 SER   A O   1 
ATOM   1383 C  CB  . SER   A 1 194 ? -2.730  15.337  20.053  1.00 18.91 ? 206 SER   A CB  1 
ATOM   1384 O  OG  . SER   A 1 194 ? -2.793  14.269  20.990  1.00 20.60 ? 206 SER   A OG  1 
ATOM   1385 N  N   . GLN   A 1 195 ? -0.196  16.525  21.152  1.00 17.38 ? 207 GLN   A N   1 
ATOM   1386 C  CA  . GLN   A 1 195 ? 0.728   16.611  22.272  1.00 19.60 ? 207 GLN   A CA  1 
ATOM   1387 C  C   . GLN   A 1 195 ? -0.057  17.031  23.506  1.00 19.63 ? 207 GLN   A C   1 
ATOM   1388 O  O   . GLN   A 1 195 ? -0.816  18.014  23.452  1.00 21.29 ? 207 GLN   A O   1 
ATOM   1389 C  CB  . GLN   A 1 195 ? 1.867   17.607  22.026  1.00 20.87 ? 207 GLN   A CB  1 
ATOM   1390 C  CG  . GLN   A 1 195 ? 2.785   17.270  20.878  1.00 18.91 ? 207 GLN   A CG  1 
ATOM   1391 C  CD  . GLN   A 1 195 ? 4.009   18.162  20.861  1.00 25.88 ? 207 GLN   A CD  1 
ATOM   1392 O  OE1 . GLN   A 1 195 ? 4.011   19.231  20.241  1.00 25.10 ? 207 GLN   A OE1 1 
ATOM   1393 N  NE2 . GLN   A 1 195 ? 5.058   17.737  21.562  1.00 22.58 ? 207 GLN   A NE2 1 
ATOM   1394 N  N   . PRO   A 1 196 ? 0.083   16.328  24.620  1.00 21.54 ? 208 PRO   A N   1 
ATOM   1395 C  CA  . PRO   A 1 196 ? -0.606  16.749  25.839  1.00 19.73 ? 208 PRO   A CA  1 
ATOM   1396 C  C   . PRO   A 1 196 ? 0.097   17.935  26.481  1.00 23.48 ? 208 PRO   A C   1 
ATOM   1397 O  O   . PRO   A 1 196 ? 1.316   18.099  26.384  1.00 23.74 ? 208 PRO   A O   1 
ATOM   1398 C  CB  . PRO   A 1 196 ? -0.517  15.504  26.726  1.00 21.16 ? 208 PRO   A CB  1 
ATOM   1399 C  CG  . PRO   A 1 196 ? 0.825   14.918  26.344  1.00 18.99 ? 208 PRO   A CG  1 
ATOM   1400 C  CD  . PRO   A 1 196 ? 0.985   15.182  24.863  1.00 21.38 ? 208 PRO   A CD  1 
ATOM   1401 N  N   . ILE   A 1 197 ? -0.698  18.781  27.128  1.00 22.52 ? 209 ILE   A N   1 
ATOM   1402 C  CA  . ILE   A 1 197 ? -0.168  19.843  27.976  1.00 25.75 ? 209 ILE   A CA  1 
ATOM   1403 C  C   . ILE   A 1 197 ? 0.160   19.214  29.323  1.00 25.30 ? 209 ILE   A C   1 
ATOM   1404 O  O   . ILE   A 1 197 ? -0.741  18.807  30.063  1.00 29.59 ? 209 ILE   A O   1 
ATOM   1405 C  CB  . ILE   A 1 197 ? -1.169  20.990  28.139  1.00 28.30 ? 209 ILE   A CB  1 
ATOM   1406 C  CG1 . ILE   A 1 197 ? -1.664  21.479  26.781  1.00 26.45 ? 209 ILE   A CG1 1 
ATOM   1407 C  CG2 . ILE   A 1 197 ? -0.553  22.116  28.976  1.00 26.55 ? 209 ILE   A CG2 1 
ATOM   1408 C  CD1 . ILE   A 1 197 ? -0.659  22.288  26.025  1.00 30.84 ? 209 ILE   A CD1 1 
ATOM   1409 N  N   . THR   A 1 198 ? 1.441   19.122  29.646  1.00 27.75 ? 210 THR   A N   1 
ATOM   1410 C  CA  . THR   A 1 198 ? 1.852   18.479  30.880  1.00 26.66 ? 210 THR   A CA  1 
ATOM   1411 C  C   . THR   A 1 198 ? 2.148   19.510  31.958  1.00 29.71 ? 210 THR   A C   1 
ATOM   1412 O  O   . THR   A 1 198 ? 2.455   20.670  31.670  1.00 28.43 ? 210 THR   A O   1 
ATOM   1413 C  CB  . THR   A 1 198 ? 3.083   17.594  30.670  1.00 26.26 ? 210 THR   A CB  1 
ATOM   1414 O  OG1 . THR   A 1 198 ? 4.241   18.412  30.443  1.00 24.79 ? 210 THR   A OG1 1 
ATOM   1415 C  CG2 . THR   A 1 198 ? 2.866   16.653  29.493  1.00 24.72 ? 210 THR   A CG2 1 
ATOM   1416 N  N   . THR   A 1 199 ? 2.030   19.072  33.206  1.00 28.50 ? 211 THR   A N   1 
ATOM   1417 C  CA  . THR   A 1 199 ? 2.530   19.819  34.348  1.00 28.26 ? 211 THR   A CA  1 
ATOM   1418 C  C   . THR   A 1 199 ? 3.722   19.086  34.949  1.00 27.80 ? 211 THR   A C   1 
ATOM   1419 O  O   . THR   A 1 199 ? 3.963   17.907  34.669  1.00 27.13 ? 211 THR   A O   1 
ATOM   1420 C  CB  . THR   A 1 199 ? 1.442   20.027  35.411  1.00 30.70 ? 211 THR   A CB  1 
ATOM   1421 O  OG1 . THR   A 1 199 ? 1.037   18.767  35.957  1.00 30.16 ? 211 THR   A OG1 1 
ATOM   1422 C  CG2 . THR   A 1 199 ? 0.236   20.717  34.805  1.00 30.33 ? 211 THR   A CG2 1 
ATOM   1423 N  N   . GLY   A 1 200 ? 4.478   19.805  35.773  1.00 31.77 ? 212 GLY   A N   1 
ATOM   1424 C  CA  . GLY   A 1 200 ? 5.630   19.240  36.435  1.00 30.17 ? 212 GLY   A CA  1 
ATOM   1425 C  C   . GLY   A 1 200 ? 6.904   19.367  35.615  1.00 34.24 ? 212 GLY   A C   1 
ATOM   1426 O  O   . GLY   A 1 200 ? 6.900   19.710  34.430  1.00 31.90 ? 212 GLY   A O   1 
ATOM   1427 N  N   . LYS   A 1 201 ? 8.023   19.083  36.279  1.00 47.80 ? 213 LYS   A N   1 
ATOM   1428 C  CA  . LYS   A 1 201 ? 9.330   19.083  35.628  1.00 41.82 ? 213 LYS   A CA  1 
ATOM   1429 C  C   . LYS   A 1 201 ? 9.424   17.880  34.700  1.00 37.83 ? 213 LYS   A C   1 
ATOM   1430 O  O   . LYS   A 1 201 ? 9.450   16.735  35.162  1.00 37.18 ? 213 LYS   A O   1 
ATOM   1431 C  CB  . LYS   A 1 201 ? 10.441  19.052  36.675  1.00 46.39 ? 213 LYS   A CB  1 
ATOM   1432 C  CG  . LYS   A 1 201 ? 11.859  18.823  36.124  1.00 43.39 ? 213 LYS   A CG  1 
ATOM   1433 C  CD  . LYS   A 1 201 ? 12.304  17.355  36.224  1.00 42.89 ? 213 LYS   A CD  1 
ATOM   1434 C  CE  . LYS   A 1 201 ? 13.760  17.160  35.796  1.00 41.62 ? 213 LYS   A CE  1 
ATOM   1435 N  NZ  . LYS   A 1 201 ? 14.130  17.848  34.523  1.00 40.90 ? 213 LYS   A NZ  1 
ATOM   1436 N  N   . ALA   A 1 202 ? 9.439   18.132  33.395  1.00 33.54 ? 214 ALA   A N   1 
ATOM   1437 C  CA  . ALA   A 1 202 ? 9.734   17.077  32.447  1.00 26.70 ? 214 ALA   A CA  1 
ATOM   1438 C  C   . ALA   A 1 202 ? 11.208  16.690  32.557  1.00 28.82 ? 214 ALA   A C   1 
ATOM   1439 O  O   . ALA   A 1 202 ? 12.046  17.509  32.955  1.00 26.31 ? 214 ALA   A O   1 
ATOM   1440 C  CB  . ALA   A 1 202 ? 9.410   17.524  31.019  1.00 26.23 ? 214 ALA   A CB  1 
ATOM   1441 N  N   . PRO   A 1 203 ? 11.553  15.442  32.241  1.00 22.14 ? 215 PRO   A N   1 
ATOM   1442 C  CA  . PRO   A 1 203 ? 12.968  15.087  32.163  1.00 20.32 ? 215 PRO   A CA  1 
ATOM   1443 C  C   . PRO   A 1 203 ? 13.665  15.962  31.142  1.00 19.95 ? 215 PRO   A C   1 
ATOM   1444 O  O   . PRO   A 1 203 ? 13.054  16.494  30.209  1.00 23.01 ? 215 PRO   A O   1 
ATOM   1445 C  CB  . PRO   A 1 203 ? 12.962  13.616  31.720  1.00 18.31 ? 215 PRO   A CB  1 
ATOM   1446 C  CG  . PRO   A 1 203 ? 11.591  13.125  31.995  1.00 20.40 ? 215 PRO   A CG  1 
ATOM   1447 C  CD  . PRO   A 1 203 ? 10.684  14.311  31.885  1.00 23.22 ? 215 PRO   A CD  1 
ATOM   1448 N  N   . SER   A 1 204 ? 14.971  16.108  31.337  1.00 18.58 ? 216 SER   A N   1 
ATOM   1449 C  CA  . SER   A 1 204 ? 15.790  16.754  30.339  1.00 20.02 ? 216 SER   A CA  1 
ATOM   1450 C  C   . SER   A 1 204 ? 15.605  16.030  29.006  1.00 16.12 ? 216 SER   A C   1 
ATOM   1451 O  O   . SER   A 1 204 ? 15.281  14.839  28.982  1.00 16.37 ? 216 SER   A O   1 
ATOM   1452 C  CB  . SER   A 1 204 ? 17.258  16.719  30.765  1.00 20.48 ? 216 SER   A CB  1 
ATOM   1453 O  OG  . SER   A 1 204 ? 17.810  15.421  30.585  1.00 21.24 ? 216 SER   A OG  1 
ATOM   1454 N  N   . PRO   A 1 205 ? 15.804  16.723  27.886  1.00 18.80 ? 217 PRO   A N   1 
ATOM   1455 C  CA  . PRO   A 1 205 ? 15.867  16.014  26.608  1.00 16.49 ? 217 PRO   A CA  1 
ATOM   1456 C  C   . PRO   A 1 205 ? 16.913  14.916  26.680  1.00 18.21 ? 217 PRO   A C   1 
ATOM   1457 O  O   . PRO   A 1 205 ? 17.920  15.037  27.388  1.00 15.74 ? 217 PRO   A O   1 
ATOM   1458 C  CB  . PRO   A 1 205 ? 16.264  17.105  25.603  1.00 17.94 ? 217 PRO   A CB  1 
ATOM   1459 C  CG  . PRO   A 1 205 ? 15.949  18.404  26.269  1.00 21.46 ? 217 PRO   A CG  1 
ATOM   1460 C  CD  . PRO   A 1 205 ? 15.998  18.178  27.746  1.00 17.88 ? 217 PRO   A CD  1 
ATOM   1461 N  N   . ARG   A 1 206 ? 16.647  13.825  25.964  1.00 16.25 ? 218 ARG   A N   1 
ATOM   1462 C  CA  . ARG   A 1 206 ? 17.518  12.661  26.029  1.00 16.72 ? 218 ARG   A CA  1 
ATOM   1463 C  C   . ARG   A 1 206 ? 17.160  11.664  24.939  1.00 13.18 ? 218 ARG   A C   1 
ATOM   1464 O  O   . ARG   A 1 206 ? 16.039  11.655  24.410  1.00 13.16 ? 218 ARG   A O   1 
ATOM   1465 C  CB  . ARG   A 1 206 ? 17.426  11.975  27.392  1.00 15.98 ? 218 ARG   A CB  1 
ATOM   1466 C  CG  . ARG   A 1 206 ? 16.006  11.622  27.808  1.00 13.15 ? 218 ARG   A CG  1 
ATOM   1467 C  CD  . ARG   A 1 206 ? 15.978  11.236  29.308  1.00 13.21 ? 218 ARG   A CD  1 
ATOM   1468 N  NE  . ARG   A 1 206 ? 16.239  12.379  30.167  1.00 19.19 ? 218 ARG   A NE  1 
ATOM   1469 C  CZ  . ARG   A 1 206 ? 16.649  12.269  31.424  1.00 19.28 ? 218 ARG   A CZ  1 
ATOM   1470 N  NH1 . ARG   A 1 206 ? 16.862  11.084  31.978  1.00 20.78 ? 218 ARG   A NH1 1 
ATOM   1471 N  NH2 . ARG   A 1 206 ? 16.902  13.370  32.124  1.00 20.98 ? 218 ARG   A NH2 1 
ATOM   1472 N  N   . ALA   A 1 207 ? 18.114  10.769  24.676  1.00 11.48 ? 219 ALA   A N   1 
ATOM   1473 C  CA  . ALA   A 1 207 ? 17.917  9.629   23.796  1.00 11.09 ? 219 ALA   A CA  1 
ATOM   1474 C  C   . ALA   A 1 207 ? 18.537  8.391   24.427  1.00 13.94 ? 219 ALA   A C   1 
ATOM   1475 O  O   . ALA   A 1 207 ? 19.397  8.481   25.308  1.00 15.35 ? 219 ALA   A O   1 
ATOM   1476 C  CB  . ALA   A 1 207 ? 18.530  9.892   22.406  1.00 13.88 ? 219 ALA   A CB  1 
ATOM   1477 N  N   . ALA   A 1 208 ? 18.100  7.221   23.956  1.00 11.55 ? 220 ALA   A N   1 
ATOM   1478 C  CA  . ALA   A 1 208 ? 18.610  5.939   24.422  1.00 9.95  ? 220 ALA   A CA  1 
ATOM   1479 C  C   . ALA   A 1 208 ? 18.289  5.730   25.909  1.00 12.48 ? 220 ALA   A C   1 
ATOM   1480 O  O   . ALA   A 1 208 ? 18.967  4.960   26.601  1.00 13.64 ? 220 ALA   A O   1 
ATOM   1481 C  CB  . ALA   A 1 208 ? 20.124  5.792   24.170  1.00 10.86 ? 220 ALA   A CB  1 
ATOM   1482 N  N   . HIS   A 1 209 ? 17.283  6.450   26.391  1.00 13.51 ? 221 HIS   A N   1 
ATOM   1483 C  CA  . HIS   A 1 209 ? 16.614  6.170   27.653  1.00 14.65 ? 221 HIS   A CA  1 
ATOM   1484 C  C   . HIS   A 1 209 ? 15.777  4.902   27.515  1.00 15.99 ? 221 HIS   A C   1 
ATOM   1485 O  O   . HIS   A 1 209 ? 15.621  4.353   26.431  1.00 15.55 ? 221 HIS   A O   1 
ATOM   1486 C  CB  . HIS   A 1 209 ? 15.698  7.329   28.036  1.00 12.48 ? 221 HIS   A CB  1 
ATOM   1487 C  CG  . HIS   A 1 209 ? 14.852  7.815   26.897  1.00 15.08 ? 221 HIS   A CG  1 
ATOM   1488 N  ND1 . HIS   A 1 209 ? 15.391  8.442   25.793  1.00 13.01 ? 221 HIS   A ND1 1 
ATOM   1489 C  CD2 . HIS   A 1 209 ? 13.511  7.785   26.696  1.00 14.80 ? 221 HIS   A CD2 1 
ATOM   1490 C  CE1 . HIS   A 1 209 ? 14.422  8.762   24.955  1.00 14.97 ? 221 HIS   A CE1 1 
ATOM   1491 N  NE2 . HIS   A 1 209 ? 13.268  8.403   25.493  1.00 14.45 ? 221 HIS   A NE2 1 
ATOM   1492 N  N   . ALA   A 1 210 ? 15.196  4.452   28.623  1.00 12.30 ? 222 ALA   A N   1 
ATOM   1493 C  CA  . ALA   A 1 210 ? 14.279  3.322   28.556  1.00 12.68 ? 222 ALA   A CA  1 
ATOM   1494 C  C   . ALA   A 1 210 ? 12.986  3.681   29.274  1.00 16.78 ? 222 ALA   A C   1 
ATOM   1495 O  O   . ALA   A 1 210 ? 13.011  4.308   30.339  1.00 12.33 ? 222 ALA   A O   1 
ATOM   1496 C  CB  . ALA   A 1 210 ? 14.901  2.066   29.158  1.00 13.89 ? 222 ALA   A CB  1 
ATOM   1497 N  N   . CYS   A 1 211 ? 11.864  3.310   28.659  1.00 13.25 ? 223 CYS   A N   1 
ATOM   1498 C  CA  . CYS   A 1 211 ? 10.526  3.549   29.180  1.00 14.24 ? 223 CYS   A CA  1 
ATOM   1499 C  C   . CYS   A 1 211 ? 9.863   2.228   29.567  1.00 14.49 ? 223 CYS   A C   1 
ATOM   1500 O  O   . CYS   A 1 211 ? 10.096  1.190   28.941  1.00 17.18 ? 223 CYS   A O   1 
ATOM   1501 C  CB  . CYS   A 1 211 ? 9.672   4.282   28.135  1.00 14.68 ? 223 CYS   A CB  1 
ATOM   1502 S  SG  . CYS   A 1 211 ? 10.190  5.962   27.712  1.00 15.45 ? 223 CYS   A SG  1 
ATOM   1503 N  N   . ALA   A 1 212 ? 9.043   2.270   30.618  1.00 11.08 ? 224 ALA   A N   1 
ATOM   1504 C  CA  . ALA   A 1 212 ? 8.244   1.133   31.042  1.00 15.69 ? 224 ALA   A CA  1 
ATOM   1505 C  C   . ALA   A 1 212 ? 6.927   1.660   31.593  1.00 15.63 ? 224 ALA   A C   1 
ATOM   1506 O  O   . ALA   A 1 212 ? 6.899   2.709   32.244  1.00 14.47 ? 224 ALA   A O   1 
ATOM   1507 C  CB  . ALA   A 1 212 ? 8.957   0.292   32.104  1.00 17.50 ? 224 ALA   A CB  1 
ATOM   1508 N  N   . THR   A 1 213 ? 5.844   0.929   31.343  1.00 16.72 ? 225 THR   A N   1 
ATOM   1509 C  CA  . THR   A 1 213 ? 4.507   1.352   31.757  1.00 18.01 ? 225 THR   A CA  1 
ATOM   1510 C  C   . THR   A 1 213 ? 3.929   0.366   32.764  1.00 14.26 ? 225 THR   A C   1 
ATOM   1511 O  O   . THR   A 1 213 ? 3.896   -0.837  32.498  1.00 16.09 ? 225 THR   A O   1 
ATOM   1512 C  CB  . THR   A 1 213 ? 3.553   1.450   30.555  1.00 17.50 ? 225 THR   A CB  1 
ATOM   1513 O  OG1 . THR   A 1 213 ? 4.145   2.210   29.487  1.00 16.63 ? 225 THR   A OG1 1 
ATOM   1514 C  CG2 . THR   A 1 213 ? 2.206   2.089   30.960  1.00 16.93 ? 225 THR   A CG2 1 
ATOM   1515 N  N   . VAL   A 1 214 ? 3.473   0.868   33.914  1.00 14.52 ? 226 VAL   A N   1 
ATOM   1516 C  CA  . VAL   A 1 214 ? 2.643   0.102   34.845  1.00 13.93 ? 226 VAL   A CA  1 
ATOM   1517 C  C   . VAL   A 1 214 ? 1.410   0.942   35.133  1.00 22.79 ? 226 VAL   A C   1 
ATOM   1518 O  O   . VAL   A 1 214 ? 1.528   2.071   35.619  1.00 23.23 ? 226 VAL   A O   1 
ATOM   1519 C  CB  . VAL   A 1 214 ? 3.367   -0.235  36.164  1.00 18.02 ? 226 VAL   A CB  1 
ATOM   1520 C  CG1 . VAL   A 1 214 ? 2.524   -1.209  37.013  1.00 23.48 ? 226 VAL   A CG1 1 
ATOM   1521 C  CG2 . VAL   A 1 214 ? 4.729   -0.805  35.908  1.00 14.00 ? 226 VAL   A CG2 1 
ATOM   1522 N  N   . GLY   A 1 215 ? 0.236   0.389   34.854  1.00 23.99 ? 227 GLY   A N   1 
ATOM   1523 C  CA  . GLY   A 1 215 ? -0.995  1.134   35.061  1.00 27.51 ? 227 GLY   A CA  1 
ATOM   1524 C  C   . GLY   A 1 215 ? -1.013  2.406   34.239  1.00 22.48 ? 227 GLY   A C   1 
ATOM   1525 O  O   . GLY   A 1 215 ? -0.743  2.402   33.030  1.00 22.50 ? 227 GLY   A O   1 
ATOM   1526 N  N   . ASN   A 1 216 ? -1.334  3.516   34.908  1.00 22.90 ? 228 ASN   A N   1 
ATOM   1527 C  CA  . ASN   A 1 216 ? -1.341  4.845   34.307  1.00 25.26 ? 228 ASN   A CA  1 
ATOM   1528 C  C   . ASN   A 1 216 ? -0.060  5.625   34.594  1.00 18.66 ? 228 ASN   A C   1 
ATOM   1529 O  O   . ASN   A 1 216 ? -0.079  6.857   34.600  1.00 19.32 ? 228 ASN   A O   1 
ATOM   1530 C  CB  . ASN   A 1 216 ? -2.550  5.637   34.804  1.00 25.20 ? 228 ASN   A CB  1 
ATOM   1531 C  CG  . ASN   A 1 216 ? -2.428  6.028   36.270  1.00 26.27 ? 228 ASN   A CG  1 
ATOM   1532 O  OD1 . ASN   A 1 216 ? -1.498  5.595   36.969  1.00 21.19 ? 228 ASN   A OD1 1 
ATOM   1533 N  ND2 . ASN   A 1 216 ? -3.377  6.844   36.753  1.00 27.70 ? 228 ASN   A ND2 1 
ATOM   1534 N  N   . ARG   A 1 217 ? 1.047   4.938   34.860  1.00 17.35 ? 229 ARG   A N   1 
ATOM   1535 C  CA  . ARG   A 1 217 ? 2.326   5.600   35.126  1.00 14.75 ? 229 ARG   A CA  1 
ATOM   1536 C  C   . ARG   A 1 217 ? 3.321   5.189   34.052  1.00 13.43 ? 229 ARG   A C   1 
ATOM   1537 O  O   . ARG   A 1 217 ? 3.582   3.995   33.862  1.00 16.33 ? 229 ARG   A O   1 
ATOM   1538 C  CB  . ARG   A 1 217 ? 2.861   5.271   36.528  1.00 19.66 ? 229 ARG   A CB  1 
ATOM   1539 C  CG  . ARG   A 1 217 ? 2.040   5.909   37.627  1.00 19.85 ? 229 ARG   A CG  1 
ATOM   1540 C  CD  . ARG   A 1 217 ? 2.708   5.740   38.985  1.00 19.39 ? 229 ARG   A CD  1 
ATOM   1541 N  NE  . ARG   A 1 217 ? 1.757   5.984   40.060  1.00 23.04 ? 229 ARG   A NE  1 
ATOM   1542 C  CZ  . ARG   A 1 217 ? 2.101   6.107   41.333  1.00 24.53 ? 229 ARG   A CZ  1 
ATOM   1543 N  NH1 . ARG   A 1 217 ? 3.371   6.059   41.710  1.00 27.42 ? 229 ARG   A NH1 1 
ATOM   1544 N  NH2 . ARG   A 1 217 ? 1.148   6.282   42.249  1.00 24.46 ? 229 ARG   A NH2 1 
ATOM   1545 N  N   . GLY   A 1 218 ? 3.842   6.172   33.337  1.00 14.09 ? 230 GLY   A N   1 
ATOM   1546 C  CA  . GLY   A 1 218 ? 4.850   5.896   32.338  1.00 14.48 ? 230 GLY   A CA  1 
ATOM   1547 C  C   . GLY   A 1 218 ? 6.223   6.243   32.859  1.00 13.80 ? 230 GLY   A C   1 
ATOM   1548 O  O   . GLY   A 1 218 ? 6.570   7.425   32.947  1.00 18.20 ? 230 GLY   A O   1 
ATOM   1549 N  N   . PHE   A 1 219 ? 6.999   5.230   33.234  1.00 12.94 ? 231 PHE   A N   1 
ATOM   1550 C  CA  . PHE   A 1 219 ? 8.315   5.450   33.821  1.00 15.39 ? 231 PHE   A CA  1 
ATOM   1551 C  C   . PHE   A 1 219 ? 9.352   5.672   32.735  1.00 16.43 ? 231 PHE   A C   1 
ATOM   1552 O  O   . PHE   A 1 219 ? 9.215   5.184   31.616  1.00 14.55 ? 231 PHE   A O   1 
ATOM   1553 C  CB  . PHE   A 1 219 ? 8.740   4.261   34.681  1.00 16.12 ? 231 PHE   A CB  1 
ATOM   1554 C  CG  . PHE   A 1 219 ? 7.887   4.067   35.892  1.00 16.73 ? 231 PHE   A CG  1 
ATOM   1555 C  CD1 . PHE   A 1 219 ? 8.194   4.714   37.086  1.00 14.97 ? 231 PHE   A CD1 1 
ATOM   1556 C  CD2 . PHE   A 1 219 ? 6.762   3.261   35.841  1.00 17.77 ? 231 PHE   A CD2 1 
ATOM   1557 C  CE1 . PHE   A 1 219 ? 7.403   4.545   38.196  1.00 17.84 ? 231 PHE   A CE1 1 
ATOM   1558 C  CE2 . PHE   A 1 219 ? 5.967   3.085   36.977  1.00 16.99 ? 231 PHE   A CE2 1 
ATOM   1559 C  CZ  . PHE   A 1 219 ? 6.290   3.721   38.142  1.00 21.27 ? 231 PHE   A CZ  1 
ATOM   1560 N  N   . VAL   A 1 220 ? 10.399  6.418   33.071  1.00 12.79 ? 232 VAL   A N   1 
ATOM   1561 C  CA  . VAL   A 1 220 ? 11.545  6.536   32.176  1.00 17.80 ? 232 VAL   A CA  1 
ATOM   1562 C  C   . VAL   A 1 220 ? 12.788  6.642   33.036  1.00 15.64 ? 232 VAL   A C   1 
ATOM   1563 O  O   . VAL   A 1 220 ? 12.780  7.327   34.058  1.00 13.75 ? 232 VAL   A O   1 
ATOM   1564 C  CB  . VAL   A 1 220 ? 11.435  7.744   31.216  1.00 14.73 ? 232 VAL   A CB  1 
ATOM   1565 C  CG1 . VAL   A 1 220 ? 11.262  9.046   31.980  1.00 15.75 ? 232 VAL   A CG1 1 
ATOM   1566 C  CG2 . VAL   A 1 220 ? 12.675  7.822   30.359  1.00 16.75 ? 232 VAL   A CG2 1 
ATOM   1567 N  N   . PHE   A 1 221 ? 13.861  5.977   32.606  1.00 12.02 ? 233 PHE   A N   1 
ATOM   1568 C  CA  . PHE   A 1 221 ? 15.097  5.917   33.380  1.00 12.24 ? 233 PHE   A CA  1 
ATOM   1569 C  C   . PHE   A 1 221 ? 16.292  6.187   32.474  1.00 13.02 ? 233 PHE   A C   1 
ATOM   1570 O  O   . PHE   A 1 221 ? 16.398  5.602   31.397  1.00 13.55 ? 233 PHE   A O   1 
ATOM   1571 C  CB  . PHE   A 1 221 ? 15.251  4.545   34.049  1.00 14.51 ? 233 PHE   A CB  1 
ATOM   1572 C  CG  . PHE   A 1 221 ? 16.546  4.372   34.797  1.00 15.55 ? 233 PHE   A CG  1 
ATOM   1573 C  CD1 . PHE   A 1 221 ? 16.799  5.093   35.945  1.00 15.11 ? 233 PHE   A CD1 1 
ATOM   1574 C  CD2 . PHE   A 1 221 ? 17.503  3.462   34.359  1.00 15.65 ? 233 PHE   A CD2 1 
ATOM   1575 C  CE1 . PHE   A 1 221 ? 17.991  4.928   36.637  1.00 16.82 ? 233 PHE   A CE1 1 
ATOM   1576 C  CE2 . PHE   A 1 221 ? 18.679  3.291   35.045  1.00 16.61 ? 233 PHE   A CE2 1 
ATOM   1577 C  CZ  . PHE   A 1 221 ? 18.918  4.027   36.198  1.00 16.24 ? 233 PHE   A CZ  1 
ATOM   1578 N  N   . GLY   A 1 222 ? 17.206  7.047   32.928  1.00 13.42 ? 234 GLY   A N   1 
ATOM   1579 C  CA  . GLY   A 1 222 ? 18.493  7.151   32.262  1.00 15.31 ? 234 GLY   A CA  1 
ATOM   1580 C  C   . GLY   A 1 222 ? 18.389  7.816   30.897  1.00 13.95 ? 234 GLY   A C   1 
ATOM   1581 O  O   . GLY   A 1 222 ? 17.453  8.574   30.606  1.00 13.01 ? 234 GLY   A O   1 
ATOM   1582 N  N   . GLY   A 1 223 ? 19.352  7.495   30.043  1.00 13.26 ? 235 GLY   A N   1 
ATOM   1583 C  CA  . GLY   A 1 223 ? 19.473  8.078   28.719  1.00 16.32 ? 235 GLY   A CA  1 
ATOM   1584 C  C   . GLY   A 1 223 ? 20.742  8.909   28.579  1.00 18.47 ? 235 GLY   A C   1 
ATOM   1585 O  O   . GLY   A 1 223 ? 21.456  9.192   29.542  1.00 16.52 ? 235 GLY   A O   1 
ATOM   1586 N  N   . ARG   A 1 224 ? 21.016  9.296   27.335  1.00 13.31 ? 236 ARG   A N   1 
ATOM   1587 C  CA  . ARG   A 1 224 ? 22.136  10.171  27.030  1.00 16.11 ? 236 ARG   A CA  1 
ATOM   1588 C  C   . ARG   A 1 224 ? 21.645  11.602  26.861  1.00 15.87 ? 236 ARG   A C   1 
ATOM   1589 O  O   . ARG   A 1 224 ? 20.644  11.851  26.177  1.00 15.30 ? 236 ARG   A O   1 
ATOM   1590 C  CB  . ARG   A 1 224 ? 22.850  9.721   25.752  1.00 18.04 ? 236 ARG   A CB  1 
ATOM   1591 C  CG  . ARG   A 1 224 ? 23.716  10.799  25.132  1.00 19.35 ? 236 ARG   A CG  1 
ATOM   1592 C  CD  . ARG   A 1 224 ? 25.152  10.710  25.614  1.00 17.26 ? 236 ARG   A CD  1 
ATOM   1593 N  NE  . ARG   A 1 224 ? 25.911  11.873  25.166  1.00 17.35 ? 236 ARG   A NE  1 
ATOM   1594 C  CZ  . ARG   A 1 224 ? 26.405  12.027  23.945  1.00 21.40 ? 236 ARG   A CZ  1 
ATOM   1595 N  NH1 . ARG   A 1 224 ? 26.335  11.063  23.041  1.00 20.86 ? 236 ARG   A NH1 1 
ATOM   1596 N  NH2 . ARG   A 1 224 ? 26.971  13.187  23.616  1.00 20.70 ? 236 ARG   A NH2 1 
ATOM   1597 N  N   . TYR   A 1 225 ? 22.365  12.546  27.466  1.00 17.30 ? 237 TYR   A N   1 
ATOM   1598 C  CA  . TYR   A 1 225 ? 22.109  13.967  27.226  1.00 19.69 ? 237 TYR   A CA  1 
ATOM   1599 C  C   . TYR   A 1 225 ? 23.403  14.738  27.426  1.00 19.31 ? 237 TYR   A C   1 
ATOM   1600 O  O   . TYR   A 1 225 ? 23.984  14.683  28.511  1.00 17.44 ? 237 TYR   A O   1 
ATOM   1601 C  CB  . TYR   A 1 225 ? 21.021  14.501  28.159  1.00 18.92 ? 237 TYR   A CB  1 
ATOM   1602 C  CG  . TYR   A 1 225 ? 20.760  15.995  28.053  1.00 19.01 ? 237 TYR   A CG  1 
ATOM   1603 C  CD1 . TYR   A 1 225 ? 20.607  16.607  26.819  1.00 22.15 ? 237 TYR   A CD1 1 
ATOM   1604 C  CD2 . TYR   A 1 225 ? 20.646  16.783  29.191  1.00 25.60 ? 237 TYR   A CD2 1 
ATOM   1605 C  CE1 . TYR   A 1 225 ? 20.355  17.966  26.714  1.00 23.50 ? 237 TYR   A CE1 1 
ATOM   1606 C  CE2 . TYR   A 1 225 ? 20.397  18.150  29.099  1.00 27.90 ? 237 TYR   A CE2 1 
ATOM   1607 C  CZ  . TYR   A 1 225 ? 20.254  18.732  27.853  1.00 28.33 ? 237 TYR   A CZ  1 
ATOM   1608 O  OH  . TYR   A 1 225 ? 20.009  20.085  27.738  1.00 35.04 ? 237 TYR   A OH  1 
ATOM   1609 N  N   . ARG   A 1 226 ? 23.828  15.469  26.393  1.00 19.53 ? 238 ARG   A N   1 
ATOM   1610 C  CA  . ARG   A 1 226 ? 25.053  16.279  26.400  1.00 21.84 ? 238 ARG   A CA  1 
ATOM   1611 C  C   . ARG   A 1 226 ? 26.209  15.354  26.764  1.00 20.69 ? 238 ARG   A C   1 
ATOM   1612 O  O   . ARG   A 1 226 ? 26.426  14.365  26.046  1.00 21.03 ? 238 ARG   A O   1 
ATOM   1613 C  CB  . ARG   A 1 226 ? 24.855  17.506  27.296  1.00 24.51 ? 238 ARG   A CB  1 
ATOM   1614 C  CG  . ARG   A 1 226 ? 23.782  18.478  26.797  1.00 26.09 ? 238 ARG   A CG  1 
ATOM   1615 C  CD  . ARG   A 1 226 ? 23.590  19.641  27.785  1.00 26.97 ? 238 ARG   A CD  1 
ATOM   1616 N  NE  . ARG   A 1 226 ? 24.838  20.347  28.045  1.00 32.79 ? 238 ARG   A NE  1 
ATOM   1617 C  CZ  . ARG   A 1 226 ? 25.417  21.189  27.197  1.00 34.55 ? 238 ARG   A CZ  1 
ATOM   1618 N  NH1 . ARG   A 1 226 ? 24.888  21.456  26.016  1.00 33.69 ? 238 ARG   A NH1 1 
ATOM   1619 N  NH2 . ARG   A 1 226 ? 26.560  21.774  27.543  1.00 39.95 ? 238 ARG   A NH2 1 
ATOM   1620 N  N   . ASP   A 1 227 ? 26.941  15.582  27.852  1.00 23.50 ? 239 ASP   A N   1 
ATOM   1621 C  CA  . ASP   A 1 227 ? 28.120  14.768  28.126  1.00 21.30 ? 239 ASP   A CA  1 
ATOM   1622 C  C   . ASP   A 1 227 ? 27.914  13.774  29.273  1.00 21.84 ? 239 ASP   A C   1 
ATOM   1623 O  O   . ASP   A 1 227 ? 28.880  13.357  29.918  1.00 24.45 ? 239 ASP   A O   1 
ATOM   1624 C  CB  . ASP   A 1 227 ? 29.328  15.664  28.385  1.00 29.32 ? 239 ASP   A CB  1 
ATOM   1625 C  CG  . ASP   A 1 227 ? 29.868  16.292  27.104  1.00 30.62 ? 239 ASP   A CG  1 
ATOM   1626 O  OD1 . ASP   A 1 227 ? 29.679  15.697  26.017  1.00 28.56 ? 239 ASP   A OD1 1 
ATOM   1627 O  OD2 . ASP   A 1 227 ? 30.490  17.373  27.181  1.00 42.81 ? 239 ASP   A OD2 1 
ATOM   1628 N  N   . ALA   A 1 228 ? 26.672  13.353  29.526  1.00 21.19 ? 240 ALA   A N   1 
ATOM   1629 C  CA  . ALA   A 1 228 ? 26.415  12.326  30.527  1.00 17.64 ? 240 ALA   A CA  1 
ATOM   1630 C  C   . ALA   A 1 228 ? 25.449  11.267  30.016  1.00 17.37 ? 240 ALA   A C   1 
ATOM   1631 O  O   . ALA   A 1 228 ? 24.635  11.508  29.114  1.00 16.62 ? 240 ALA   A O   1 
ATOM   1632 C  CB  . ALA   A 1 228 ? 25.858  12.929  31.845  1.00 18.63 ? 240 ALA   A CB  1 
ATOM   1633 N  N   . ARG   A 1 229 ? 25.593  10.075  30.584  1.00 15.23 ? 241 ARG   A N   1 
ATOM   1634 C  CA  . ARG   A 1 229 ? 24.582  9.031   30.555  1.00 14.93 ? 241 ARG   A CA  1 
ATOM   1635 C  C   . ARG   A 1 229 ? 24.015  8.914   31.963  1.00 17.66 ? 241 ARG   A C   1 
ATOM   1636 O  O   . ARG   A 1 229 ? 24.765  8.700   32.917  1.00 17.63 ? 241 ARG   A O   1 
ATOM   1637 C  CB  . ARG   A 1 229 ? 25.179  7.722   30.047  1.00 17.25 ? 241 ARG   A CB  1 
ATOM   1638 C  CG  . ARG   A 1 229 ? 25.555  7.896   28.564  1.00 16.57 ? 241 ARG   A CG  1 
ATOM   1639 C  CD  . ARG   A 1 229 ? 26.232  6.716   27.874  1.00 15.46 ? 241 ARG   A CD  1 
ATOM   1640 N  NE  . ARG   A 1 229 ? 26.571  7.108   26.502  1.00 16.59 ? 241 ARG   A NE  1 
ATOM   1641 C  CZ  . ARG   A 1 229 ? 27.791  7.428   26.088  1.00 18.87 ? 241 ARG   A CZ  1 
ATOM   1642 N  NH1 . ARG   A 1 229 ? 28.854  7.270   26.868  1.00 16.96 ? 241 ARG   A NH1 1 
ATOM   1643 N  NH2 . ARG   A 1 229 ? 27.955  7.913   24.856  1.00 22.98 ? 241 ARG   A NH2 1 
ATOM   1644 N  N   . MET   A 1 230 ? 22.701  9.070   32.084  1.00 18.80 ? 242 MET   A N   1 
ATOM   1645 C  CA  . MET   A 1 230 ? 22.075  9.562   33.301  1.00 17.00 ? 242 MET   A CA  1 
ATOM   1646 C  C   . MET   A 1 230 ? 21.510  8.437   34.165  1.00 18.06 ? 242 MET   A C   1 
ATOM   1647 O  O   . MET   A 1 230 ? 21.334  7.300   33.727  1.00 16.44 ? 242 MET   A O   1 
ATOM   1648 C  CB  . MET   A 1 230 ? 20.986  10.573  32.939  1.00 18.31 ? 242 MET   A CB  1 
ATOM   1649 C  CG  . MET   A 1 230 ? 21.576  11.925  32.532  1.00 20.98 ? 242 MET   A CG  1 
ATOM   1650 S  SD  . MET   A 1 230 ? 20.366  13.030  31.828  1.00 26.88 ? 242 MET   A SD  1 
ATOM   1651 C  CE  . MET   A 1 230 ? 19.803  11.999  30.467  1.00 23.36 ? 242 MET   A CE  1 
ATOM   1652 N  N   . ASN   A 1 231 ? 21.265  8.768   35.437  1.00 22.81 ? 243 ASN   A N   1 
ATOM   1653 C  CA  . ASN   A 1 231 ? 20.772  7.799   36.409  1.00 18.52 ? 243 ASN   A CA  1 
ATOM   1654 C  C   . ASN   A 1 231 ? 19.422  8.197   36.977  1.00 20.99 ? 243 ASN   A C   1 
ATOM   1655 O  O   . ASN   A 1 231 ? 19.000  7.634   37.996  1.00 19.97 ? 243 ASN   A O   1 
ATOM   1656 C  CB  . ASN   A 1 231 ? 21.777  7.621   37.553  1.00 23.63 ? 243 ASN   A CB  1 
ATOM   1657 C  CG  . ASN   A 1 231 ? 21.753  8.780   38.530  1.00 18.85 ? 243 ASN   A CG  1 
ATOM   1658 O  OD1 . ASN   A 1 231 ? 21.462  9.917   38.159  1.00 25.18 ? 243 ASN   A OD1 1 
ATOM   1659 N  ND2 . ASN   A 1 231 ? 22.053  8.498   39.800  1.00 26.10 ? 243 ASN   A ND2 1 
ATOM   1660 N  N   . ASP   A 1 232 ? 18.753  9.174   36.375  1.00 17.30 ? 244 ASP   A N   1 
ATOM   1661 C  CA  . ASP   A 1 232 ? 17.547  9.699   36.983  1.00 16.32 ? 244 ASP   A CA  1 
ATOM   1662 C  C   . ASP   A 1 232 ? 16.332  8.881   36.568  1.00 18.24 ? 244 ASP   A C   1 
ATOM   1663 O  O   . ASP   A 1 232 ? 16.348  8.122   35.591  1.00 16.86 ? 244 ASP   A O   1 
ATOM   1664 C  CB  . ASP   A 1 232 ? 17.346  11.191  36.667  1.00 16.69 ? 244 ASP   A CB  1 
ATOM   1665 C  CG  . ASP   A 1 232 ? 17.309  11.496  35.180  1.00 19.71 ? 244 ASP   A CG  1 
ATOM   1666 O  OD1 . ASP   A 1 232 ? 17.822  10.686  34.397  1.00 17.47 ? 244 ASP   A OD1 1 
ATOM   1667 O  OD2 . ASP   A 1 232 ? 16.788  12.572  34.826  1.00 22.08 ? 244 ASP   A OD2 1 
ATOM   1668 N  N   . LEU   A 1 233 ? 15.277  9.020   37.364  1.00 17.63 ? 245 LEU   A N   1 
ATOM   1669 C  CA  . LEU   A 1 233 ? 14.074  8.225   37.210  1.00 17.25 ? 245 LEU   A CA  1 
ATOM   1670 C  C   . LEU   A 1 233 ? 12.895  9.167   37.366  1.00 18.46 ? 245 LEU   A C   1 
ATOM   1671 O  O   . LEU   A 1 233 ? 12.859  9.950   38.319  1.00 17.21 ? 245 LEU   A O   1 
ATOM   1672 C  CB  . LEU   A 1 233 ? 14.034  7.108   38.258  1.00 17.11 ? 245 LEU   A CB  1 
ATOM   1673 C  CG  . LEU   A 1 233 ? 12.881  6.105   38.282  1.00 16.29 ? 245 LEU   A CG  1 
ATOM   1674 C  CD1 . LEU   A 1 233 ? 12.858  5.254   37.019  1.00 17.28 ? 245 LEU   A CD1 1 
ATOM   1675 C  CD2 . LEU   A 1 233 ? 12.995  5.225   39.500  1.00 16.44 ? 245 LEU   A CD2 1 
ATOM   1676 N  N   . HIS   A 1 234 ? 11.976  9.127   36.406  1.00 14.40 ? 246 HIS   A N   1 
ATOM   1677 C  CA  . HIS   A 1 234 ? 10.765  9.931   36.418  1.00 17.73 ? 246 HIS   A CA  1 
ATOM   1678 C  C   . HIS   A 1 234 ? 9.605   9.061   35.986  1.00 17.50 ? 246 HIS   A C   1 
ATOM   1679 O  O   . HIS   A 1 234 ? 9.796   7.988   35.409  1.00 16.97 ? 246 HIS   A O   1 
ATOM   1680 C  CB  . HIS   A 1 234 ? 10.834  11.133  35.468  1.00 18.07 ? 246 HIS   A CB  1 
ATOM   1681 C  CG  . HIS   A 1 234 ? 12.093  11.930  35.573  1.00 20.81 ? 246 HIS   A CG  1 
ATOM   1682 N  ND1 . HIS   A 1 234 ? 12.127  13.194  36.118  1.00 24.52 ? 246 HIS   A ND1 1 
ATOM   1683 C  CD2 . HIS   A 1 234 ? 13.361  11.647  35.189  1.00 16.47 ? 246 HIS   A CD2 1 
ATOM   1684 C  CE1 . HIS   A 1 234 ? 13.363  13.657  36.066  1.00 24.30 ? 246 HIS   A CE1 1 
ATOM   1685 N  NE2 . HIS   A 1 234 ? 14.130  12.741  35.501  1.00 19.04 ? 246 HIS   A NE2 1 
ATOM   1686 N  N   . TYR   A 1 235 ? 8.384   9.546   36.233  1.00 20.45 ? 247 TYR   A N   1 
ATOM   1687 C  CA  . TYR   A 1 235 ? 7.211   8.969   35.582  1.00 20.15 ? 247 TYR   A CA  1 
ATOM   1688 C  C   . TYR   A 1 235 ? 6.224   10.061  35.193  1.00 16.09 ? 247 TYR   A C   1 
ATOM   1689 O  O   . TYR   A 1 235 ? 6.014   11.026  35.935  1.00 20.83 ? 247 TYR   A O   1 
ATOM   1690 C  CB  . TYR   A 1 235 ? 6.511   7.909   36.457  1.00 18.74 ? 247 TYR   A CB  1 
ATOM   1691 C  CG  . TYR   A 1 235 ? 5.578   8.442   37.531  1.00 20.02 ? 247 TYR   A CG  1 
ATOM   1692 C  CD1 . TYR   A 1 235 ? 4.259   8.780   37.251  1.00 16.62 ? 247 TYR   A CD1 1 
ATOM   1693 C  CD2 . TYR   A 1 235 ? 6.015   8.569   38.842  1.00 20.85 ? 247 TYR   A CD2 1 
ATOM   1694 C  CE1 . TYR   A 1 235 ? 3.413   9.255   38.238  1.00 21.68 ? 247 TYR   A CE1 1 
ATOM   1695 C  CE2 . TYR   A 1 235 ? 5.186   9.033   39.821  1.00 23.75 ? 247 TYR   A CE2 1 
ATOM   1696 C  CZ  . TYR   A 1 235 ? 3.888   9.369   39.523  1.00 26.28 ? 247 TYR   A CZ  1 
ATOM   1697 O  OH  . TYR   A 1 235 ? 3.071   9.828   40.529  1.00 26.98 ? 247 TYR   A OH  1 
ATOM   1698 N  N   . LEU   A 1 236 ? 5.649   9.927   34.009  1.00 20.40 ? 248 LEU   A N   1 
ATOM   1699 C  CA  . LEU   A 1 236 ? 4.569   10.795  33.571  1.00 16.00 ? 248 LEU   A CA  1 
ATOM   1700 C  C   . LEU   A 1 236 ? 3.263   10.070  33.853  1.00 14.24 ? 248 LEU   A C   1 
ATOM   1701 O  O   . LEU   A 1 236 ? 3.081   8.933   33.404  1.00 17.32 ? 248 LEU   A O   1 
ATOM   1702 C  CB  . LEU   A 1 236 ? 4.709   11.130  32.084  1.00 17.96 ? 248 LEU   A CB  1 
ATOM   1703 C  CG  . LEU   A 1 236 ? 3.583   11.897  31.389  1.00 19.74 ? 248 LEU   A CG  1 
ATOM   1704 C  CD1 . LEU   A 1 236 ? 3.438   13.329  31.933  1.00 19.02 ? 248 LEU   A CD1 1 
ATOM   1705 C  CD2 . LEU   A 1 236 ? 3.813   11.898  29.859  1.00 18.35 ? 248 LEU   A CD2 1 
ATOM   1706 N  N   . ASN   A 1 237 ? 2.382   10.704  34.633  1.00 18.53 ? 249 ASN   A N   1 
ATOM   1707 C  CA  . ASN   A 1 237 ? 1.045   10.168  34.877  1.00 19.05 ? 249 ASN   A CA  1 
ATOM   1708 C  C   . ASN   A 1 237 ? 0.218   10.296  33.599  1.00 18.33 ? 249 ASN   A C   1 
ATOM   1709 O  O   . ASN   A 1 237 ? -0.024  11.406  33.129  1.00 20.27 ? 249 ASN   A O   1 
ATOM   1710 C  CB  . ASN   A 1 237 ? 0.380   10.919  36.036  1.00 23.21 ? 249 ASN   A CB  1 
ATOM   1711 C  CG  . ASN   A 1 237 ? -0.997  10.382  36.370  1.00 22.28 ? 249 ASN   A CG  1 
ATOM   1712 O  OD1 . ASN   A 1 237 ? -1.857  10.233  35.493  1.00 21.78 ? 249 ASN   A OD1 1 
ATOM   1713 N  ND2 . ASN   A 1 237 ? -1.209  10.072  37.642  1.00 23.19 ? 249 ASN   A ND2 1 
ATOM   1714 N  N   . LEU   A 1 238 ? -0.218  9.168   33.038  1.00 20.16 ? 250 LEU   A N   1 
ATOM   1715 C  CA  . LEU   A 1 238 ? -0.821  9.185   31.705  1.00 19.95 ? 250 LEU   A CA  1 
ATOM   1716 C  C   . LEU   A 1 238 ? -2.302  9.525   31.718  1.00 22.40 ? 250 LEU   A C   1 
ATOM   1717 O  O   . LEU   A 1 238 ? -2.927  9.491   30.652  1.00 22.09 ? 250 LEU   A O   1 
ATOM   1718 C  CB  . LEU   A 1 238 ? -0.605  7.838   31.011  1.00 21.70 ? 250 LEU   A CB  1 
ATOM   1719 C  CG  . LEU   A 1 238 ? 0.866   7.428   31.056  1.00 18.15 ? 250 LEU   A CG  1 
ATOM   1720 C  CD1 . LEU   A 1 238 ? 1.074   5.987   30.614  1.00 12.98 ? 250 LEU   A CD1 1 
ATOM   1721 C  CD2 . LEU   A 1 238 ? 1.719   8.402   30.238  1.00 16.95 ? 250 LEU   A CD2 1 
ATOM   1722 N  N   . ASP   A 1 239 ? -2.867  9.815   32.894  1.00 24.90 ? 251 ASP   A N   1 
ATOM   1723 C  CA  . ASP   A 1 239 ? -4.232  10.304  33.093  1.00 21.49 ? 251 ASP   A CA  1 
ATOM   1724 C  C   . ASP   A 1 239 ? -4.274  11.802  33.356  1.00 24.20 ? 251 ASP   A C   1 
ATOM   1725 O  O   . ASP   A 1 239 ? -5.070  12.518  32.746  1.00 25.89 ? 251 ASP   A O   1 
ATOM   1726 C  CB  . ASP   A 1 239 ? -4.893  9.589   34.274  1.00 26.58 ? 251 ASP   A CB  1 
ATOM   1727 C  CG  . ASP   A 1 239 ? -5.406  8.233   33.911  1.00 28.96 ? 251 ASP   A CG  1 
ATOM   1728 O  OD1 . ASP   A 1 239 ? -5.764  8.053   32.729  1.00 26.83 ? 251 ASP   A OD1 1 
ATOM   1729 O  OD2 . ASP   A 1 239 ? -5.458  7.361   34.812  1.00 32.11 ? 251 ASP   A OD2 1 
ATOM   1730 N  N   . THR   A 1 240 ? -3.443  12.285  34.278  1.00 24.39 ? 252 THR   A N   1 
ATOM   1731 C  CA  . THR   A 1 240 ? -3.382  13.711  34.562  1.00 25.87 ? 252 THR   A CA  1 
ATOM   1732 C  C   . THR   A 1 240 ? -2.384  14.447  33.684  1.00 24.59 ? 252 THR   A C   1 
ATOM   1733 O  O   . THR   A 1 240 ? -2.571  15.644  33.449  1.00 28.03 ? 252 THR   A O   1 
ATOM   1734 C  CB  . THR   A 1 240 ? -3.035  13.961  36.037  1.00 26.23 ? 252 THR   A CB  1 
ATOM   1735 O  OG1 . THR   A 1 240 ? -1.654  13.657  36.284  1.00 24.18 ? 252 THR   A OG1 1 
ATOM   1736 C  CG2 . THR   A 1 240 ? -3.906  13.100  36.941  1.00 29.86 ? 252 THR   A CG2 1 
ATOM   1737 N  N   . TRP   A 1 241 ? -1.356  13.755  33.181  1.00 22.66 ? 253 TRP   A N   1 
ATOM   1738 C  CA  . TRP   A 1 241 ? -0.264  14.365  32.415  1.00 22.69 ? 253 TRP   A CA  1 
ATOM   1739 C  C   . TRP   A 1 241 ? 0.602   15.249  33.311  1.00 26.77 ? 253 TRP   A C   1 
ATOM   1740 O  O   . TRP   A 1 241 ? 0.999   16.351  32.940  1.00 29.69 ? 253 TRP   A O   1 
ATOM   1741 C  CB  . TRP   A 1 241 ? -0.792  15.131  31.195  1.00 24.82 ? 253 TRP   A CB  1 
ATOM   1742 C  CG  . TRP   A 1 241 ? -1.638  14.249  30.356  1.00 23.21 ? 253 TRP   A CG  1 
ATOM   1743 C  CD1 . TRP   A 1 241 ? -2.999  14.292  30.226  1.00 26.74 ? 253 TRP   A CD1 1 
ATOM   1744 C  CD2 . TRP   A 1 241 ? -1.195  13.139  29.571  1.00 22.02 ? 253 TRP   A CD2 1 
ATOM   1745 N  NE1 . TRP   A 1 241 ? -3.424  13.287  29.390  1.00 25.61 ? 253 TRP   A NE1 1 
ATOM   1746 C  CE2 . TRP   A 1 241 ? -2.335  12.575  28.962  1.00 22.66 ? 253 TRP   A CE2 1 
ATOM   1747 C  CE3 . TRP   A 1 241 ? 0.058   12.584  29.297  1.00 19.54 ? 253 TRP   A CE3 1 
ATOM   1748 C  CZ2 . TRP   A 1 241 ? -2.259  11.467  28.124  1.00 20.39 ? 253 TRP   A CZ2 1 
ATOM   1749 C  CZ3 . TRP   A 1 241 ? 0.128   11.487  28.454  1.00 21.98 ? 253 TRP   A CZ3 1 
ATOM   1750 C  CH2 . TRP   A 1 241 ? -1.022  10.943  27.877  1.00 20.66 ? 253 TRP   A CH2 1 
ATOM   1751 N  N   . GLU   A 1 242 ? 0.913   14.746  34.498  1.00 26.50 ? 254 GLU   A N   1 
ATOM   1752 C  CA  . GLU   A 1 242 ? 1.779   15.430  35.446  1.00 22.23 ? 254 GLU   A CA  1 
ATOM   1753 C  C   . GLU   A 1 242 ? 3.071   14.634  35.589  1.00 24.66 ? 254 GLU   A C   1 
ATOM   1754 O  O   . GLU   A 1 242 ? 3.039   13.435  35.895  1.00 23.92 ? 254 GLU   A O   1 
ATOM   1755 C  CB  . GLU   A 1 242 ? 1.075   15.593  36.797  1.00 28.99 ? 254 GLU   A CB  1 
ATOM   1756 C  CG  . GLU   A 1 242 ? 1.992   15.625  38.005  1.00 29.13 ? 254 GLU   A CG  1 
ATOM   1757 C  CD  . GLU   A 1 242 ? 1.229   15.882  39.292  1.00 34.75 ? 254 GLU   A CD  1 
ATOM   1758 O  OE1 . GLU   A 1 242 ? 0.687   17.003  39.457  1.00 36.71 ? 254 GLU   A OE1 1 
ATOM   1759 O  OE2 . GLU   A 1 242 ? 1.141   14.953  40.126  1.00 38.30 ? 254 GLU   A OE2 1 
ATOM   1760 N  N   . TRP   A 1 243 ? 4.199   15.296  35.362  1.00 22.71 ? 255 TRP   A N   1 
ATOM   1761 C  CA  . TRP   A 1 243 ? 5.495   14.658  35.548  1.00 23.93 ? 255 TRP   A CA  1 
ATOM   1762 C  C   . TRP   A 1 243 ? 5.833   14.566  37.034  1.00 24.99 ? 255 TRP   A C   1 
ATOM   1763 O  O   . TRP   A 1 243 ? 5.477   15.446  37.825  1.00 24.53 ? 255 TRP   A O   1 
ATOM   1764 C  CB  . TRP   A 1 243 ? 6.593   15.432  34.816  1.00 23.28 ? 255 TRP   A CB  1 
ATOM   1765 C  CG  . TRP   A 1 243 ? 6.687   15.200  33.332  1.00 24.15 ? 255 TRP   A CG  1 
ATOM   1766 C  CD1 . TRP   A 1 243 ? 6.257   16.041  32.340  1.00 23.97 ? 255 TRP   A CD1 1 
ATOM   1767 C  CD2 . TRP   A 1 243 ? 7.267   14.065  32.671  1.00 20.22 ? 255 TRP   A CD2 1 
ATOM   1768 N  NE1 . TRP   A 1 243 ? 6.531   15.497  31.101  1.00 22.12 ? 255 TRP   A NE1 1 
ATOM   1769 C  CE2 . TRP   A 1 243 ? 7.145   14.284  31.276  1.00 23.63 ? 255 TRP   A CE2 1 
ATOM   1770 C  CE3 . TRP   A 1 243 ? 7.863   12.877  33.119  1.00 22.18 ? 255 TRP   A CE3 1 
ATOM   1771 C  CZ2 . TRP   A 1 243 ? 7.612   13.373  30.332  1.00 19.24 ? 255 TRP   A CZ2 1 
ATOM   1772 C  CZ3 . TRP   A 1 243 ? 8.319   11.963  32.168  1.00 18.99 ? 255 TRP   A CZ3 1 
ATOM   1773 C  CH2 . TRP   A 1 243 ? 8.188   12.223  30.790  1.00 15.61 ? 255 TRP   A CH2 1 
ATOM   1774 N  N   . ASN   A 1 244 ? 6.518   13.485  37.404  1.00 23.20 ? 256 ASN   A N   1 
ATOM   1775 C  CA  . ASN   A 1 244 ? 7.044   13.279  38.747  1.00 21.93 ? 256 ASN   A CA  1 
ATOM   1776 C  C   . ASN   A 1 244 ? 8.461   12.742  38.641  1.00 25.37 ? 256 ASN   A C   1 
ATOM   1777 O  O   . ASN   A 1 244 ? 8.700   11.786  37.898  1.00 22.02 ? 256 ASN   A O   1 
ATOM   1778 C  CB  . ASN   A 1 244 ? 6.188   12.282  39.535  1.00 23.63 ? 256 ASN   A CB  1 
ATOM   1779 C  CG  . ASN   A 1 244 ? 4.769   12.753  39.719  1.00 30.08 ? 256 ASN   A CG  1 
ATOM   1780 O  OD1 . ASN   A 1 244 ? 3.877   12.424  38.929  1.00 29.34 ? 256 ASN   A OD1 1 
ATOM   1781 N  ND2 . ASN   A 1 244 ? 4.548   13.537  40.762  1.00 26.92 ? 256 ASN   A ND2 1 
ATOM   1782 N  N   . GLU   A 1 245 ? 9.396   13.329  39.386  1.00 25.69 ? 257 GLU   A N   1 
ATOM   1783 C  CA  . GLU   A 1 245 ? 10.736  12.762  39.498  1.00 25.21 ? 257 GLU   A CA  1 
ATOM   1784 C  C   . GLU   A 1 245 ? 10.823  11.920  40.760  1.00 23.63 ? 257 GLU   A C   1 
ATOM   1785 O  O   . GLU   A 1 245 ? 10.451  12.378  41.848  1.00 25.52 ? 257 GLU   A O   1 
ATOM   1786 C  CB  . GLU   A 1 245 ? 11.836  13.824  39.522  1.00 24.65 ? 257 GLU   A CB  1 
ATOM   1787 C  CG  . GLU   A 1 245 ? 13.211  13.171  39.631  1.00 23.01 ? 257 GLU   A CG  1 
ATOM   1788 C  CD  . GLU   A 1 245 ? 14.366  14.136  39.469  1.00 28.59 ? 257 GLU   A CD  1 
ATOM   1789 O  OE1 . GLU   A 1 245 ? 14.121  15.361  39.407  1.00 36.31 ? 257 GLU   A OE1 1 
ATOM   1790 O  OE2 . GLU   A 1 245 ? 15.525  13.658  39.414  1.00 28.76 ? 257 GLU   A OE2 1 
ATOM   1791 N  N   . LEU   A 1 246 ? 11.323  10.699  40.610  1.00 19.21 ? 258 LEU   A N   1 
ATOM   1792 C  CA  . LEU   A 1 246 ? 11.418  9.739   41.695  1.00 21.28 ? 258 LEU   A CA  1 
ATOM   1793 C  C   . LEU   A 1 246 ? 12.828  9.760   42.268  1.00 22.64 ? 258 LEU   A C   1 
ATOM   1794 O  O   . LEU   A 1 246 ? 13.806  9.761   41.520  1.00 23.94 ? 258 LEU   A O   1 
ATOM   1795 C  CB  . LEU   A 1 246 ? 11.058  8.338   41.199  1.00 25.58 ? 258 LEU   A CB  1 
ATOM   1796 C  CG  . LEU   A 1 246 ? 9.598   8.142   40.773  1.00 22.48 ? 258 LEU   A CG  1 
ATOM   1797 C  CD1 . LEU   A 1 246 ? 9.451   6.792   40.127  1.00 20.82 ? 258 LEU   A CD1 1 
ATOM   1798 C  CD2 . LEU   A 1 246 ? 8.698   8.256   42.004  1.00 23.62 ? 258 LEU   A CD2 1 
ATOM   1799 N  N   . ILE   A 1 247 ? 12.926  9.769   43.595  1.00 26.96 ? 259 ILE   A N   1 
ATOM   1800 C  CA  . ILE   A 1 247 ? 14.216  9.883   44.274  1.00 31.27 ? 259 ILE   A CA  1 
ATOM   1801 C  C   . ILE   A 1 247 ? 14.378  8.683   45.202  1.00 27.00 ? 259 ILE   A C   1 
ATOM   1802 O  O   . ILE   A 1 247 ? 14.135  8.811   46.407  1.00 28.13 ? 259 ILE   A O   1 
ATOM   1803 C  CB  . ILE   A 1 247 ? 14.313  11.204  45.059  1.00 31.99 ? 259 ILE   A CB  1 
ATOM   1804 C  CG1 . ILE   A 1 247 ? 13.641  12.344  44.288  1.00 34.92 ? 259 ILE   A CG1 1 
ATOM   1805 C  CG2 . ILE   A 1 247 ? 15.769  11.563  45.353  1.00 35.12 ? 259 ILE   A CG2 1 
ATOM   1806 C  CD1 . ILE   A 1 247 ? 14.431  12.824  43.091  1.00 30.46 ? 259 ILE   A CD1 1 
ATOM   1807 N  N   . PRO   A 1 248 ? 14.769  7.510   44.701  1.00 30.01 ? 260 PRO   A N   1 
ATOM   1808 C  CA  . PRO   A 1 248 ? 14.907  6.342   45.581  1.00 26.68 ? 260 PRO   A CA  1 
ATOM   1809 C  C   . PRO   A 1 248 ? 16.020  6.531   46.598  1.00 29.37 ? 260 PRO   A C   1 
ATOM   1810 O  O   . PRO   A 1 248 ? 17.052  7.144   46.320  1.00 33.20 ? 260 PRO   A O   1 
ATOM   1811 C  CB  . PRO   A 1 248 ? 15.239  5.191   44.621  1.00 24.37 ? 260 PRO   A CB  1 
ATOM   1812 C  CG  . PRO   A 1 248 ? 14.955  5.700   43.264  1.00 23.87 ? 260 PRO   A CG  1 
ATOM   1813 C  CD  . PRO   A 1 248 ? 15.110  7.191   43.309  1.00 24.63 ? 260 PRO   A CD  1 
ATOM   1814 N  N   . GLN   A 1 249 ? 15.796  5.980   47.785  1.00 27.02 ? 261 GLN   A N   1 
ATOM   1815 C  CA  . GLN   A 1 249 ? 16.757  6.061   48.874  1.00 32.45 ? 261 GLN   A CA  1 
ATOM   1816 C  C   . GLN   A 1 249 ? 17.800  4.959   48.752  1.00 26.54 ? 261 GLN   A C   1 
ATOM   1817 O  O   . GLN   A 1 249 ? 17.541  3.881   48.207  1.00 25.75 ? 261 GLN   A O   1 
ATOM   1818 C  CB  . GLN   A 1 249 ? 16.054  5.958   50.228  1.00 37.44 ? 261 GLN   A CB  1 
ATOM   1819 C  CG  . GLN   A 1 249 ? 15.076  7.093   50.502  1.00 44.65 ? 261 GLN   A CG  1 
ATOM   1820 C  CD  . GLN   A 1 249 ? 15.775  8.395   50.865  1.00 48.56 ? 261 GLN   A CD  1 
ATOM   1821 O  OE1 . GLN   A 1 249 ? 15.346  9.480   50.462  1.00 48.88 ? 261 GLN   A OE1 1 
ATOM   1822 N  NE2 . GLN   A 1 249 ? 16.853  8.292   51.638  1.00 49.03 ? 261 GLN   A NE2 1 
ATOM   1823 N  N   . GLY   A 1 250 ? 18.986  5.237   49.284  1.00 31.18 ? 262 GLY   A N   1 
ATOM   1824 C  CA  . GLY   A 1 250 ? 20.039  4.245   49.269  1.00 23.38 ? 262 GLY   A CA  1 
ATOM   1825 C  C   . GLY   A 1 250 ? 20.699  4.157   47.901  1.00 23.08 ? 262 GLY   A C   1 
ATOM   1826 O  O   . GLY   A 1 250 ? 20.777  5.136   47.158  1.00 24.18 ? 262 GLY   A O   1 
ATOM   1827 N  N   . ILE   A 1 251 ? 21.165  2.958   47.574  1.00 20.48 ? 263 ILE   A N   1 
ATOM   1828 C  CA  . ILE   A 1 251 ? 22.020  2.751   46.408  1.00 21.57 ? 263 ILE   A CA  1 
ATOM   1829 C  C   . ILE   A 1 251 ? 21.156  2.709   45.156  1.00 22.95 ? 263 ILE   A C   1 
ATOM   1830 O  O   . ILE   A 1 251 ? 20.117  2.039   45.123  1.00 24.47 ? 263 ILE   A O   1 
ATOM   1831 C  CB  . ILE   A 1 251 ? 22.841  1.460   46.562  1.00 19.85 ? 263 ILE   A CB  1 
ATOM   1832 C  CG1 . ILE   A 1 251 ? 23.575  1.454   47.913  1.00 22.98 ? 263 ILE   A CG1 1 
ATOM   1833 C  CG2 . ILE   A 1 251 ? 23.817  1.293   45.401  1.00 22.82 ? 263 ILE   A CG2 1 
ATOM   1834 C  CD1 . ILE   A 1 251 ? 24.864  2.226   47.891  1.00 22.93 ? 263 ILE   A CD1 1 
ATOM   1835 N  N   . CYS   A 1 252 ? 21.585  3.425   44.124  1.00 20.30 ? 264 CYS   A N   1 
ATOM   1836 C  CA  . CYS   A 1 252 ? 20.918  3.448   42.837  1.00 17.51 ? 264 CYS   A CA  1 
ATOM   1837 C  C   . CYS   A 1 252 ? 21.887  2.947   41.786  1.00 17.36 ? 264 CYS   A C   1 
ATOM   1838 O  O   . CYS   A 1 252 ? 23.104  3.060   41.957  1.00 16.39 ? 264 CYS   A O   1 
ATOM   1839 C  CB  . CYS   A 1 252 ? 20.459  4.865   42.465  1.00 21.93 ? 264 CYS   A CB  1 
ATOM   1840 S  SG  . CYS   A 1 252 ? 19.236  5.592   43.592  1.00 26.17 ? 264 CYS   A SG  1 
ATOM   1841 N  N   . PRO   A 1 253 ? 21.386  2.410   40.675  1.00 18.00 ? 265 PRO   A N   1 
ATOM   1842 C  CA  . PRO   A 1 253 ? 22.288  1.965   39.609  1.00 18.92 ? 265 PRO   A CA  1 
ATOM   1843 C  C   . PRO   A 1 253 ? 23.062  3.127   39.004  1.00 16.90 ? 265 PRO   A C   1 
ATOM   1844 O  O   . PRO   A 1 253 ? 22.601  4.272   38.978  1.00 15.28 ? 265 PRO   A O   1 
ATOM   1845 C  CB  . PRO   A 1 253 ? 21.342  1.336   38.576  1.00 14.95 ? 265 PRO   A CB  1 
ATOM   1846 C  CG  . PRO   A 1 253 ? 20.049  1.079   39.313  1.00 17.36 ? 265 PRO   A CG  1 
ATOM   1847 C  CD  . PRO   A 1 253 ? 19.971  2.156   40.349  1.00 15.43 ? 265 PRO   A CD  1 
ATOM   1848 N  N   . VAL   A 1 254 ? 24.251  2.801   38.482  1.00 17.77 ? 266 VAL   A N   1 
ATOM   1849 C  CA  . VAL   A 1 254 ? 25.062  3.792   37.793  1.00 19.26 ? 266 VAL   A CA  1 
ATOM   1850 C  C   . VAL   A 1 254 ? 24.294  4.327   36.583  1.00 15.85 ? 266 VAL   A C   1 
ATOM   1851 O  O   . VAL   A 1 254 ? 23.473  3.623   35.988  1.00 15.26 ? 266 VAL   A O   1 
ATOM   1852 C  CB  . VAL   A 1 254 ? 26.407  3.180   37.363  1.00 19.21 ? 266 VAL   A CB  1 
ATOM   1853 C  CG1 . VAL   A 1 254 ? 26.206  2.074   36.322  1.00 15.20 ? 266 VAL   A CG1 1 
ATOM   1854 C  CG2 . VAL   A 1 254 ? 27.354  4.251   36.839  1.00 17.17 ? 266 VAL   A CG2 1 
ATOM   1855 N  N   . GLY   A 1 255 ? 24.567  5.584   36.232  1.00 12.92 ? 267 GLY   A N   1 
ATOM   1856 C  CA  . GLY   A 1 255 ? 23.933  6.192   35.075  1.00 15.92 ? 267 GLY   A CA  1 
ATOM   1857 C  C   . GLY   A 1 255 ? 24.327  5.502   33.782  1.00 13.26 ? 267 GLY   A C   1 
ATOM   1858 O  O   . GLY   A 1 255 ? 25.435  4.977   33.638  1.00 13.24 ? 267 GLY   A O   1 
ATOM   1859 N  N   . ARG   A 1 256 ? 23.400  5.497   32.825  1.00 12.35 ? 268 ARG   A N   1 
ATOM   1860 C  CA  . ARG   A 1 256 ? 23.636  4.675   31.641  1.00 12.17 ? 268 ARG   A CA  1 
ATOM   1861 C  C   . ARG   A 1 256 ? 22.665  5.067   30.538  1.00 12.18 ? 268 ARG   A C   1 
ATOM   1862 O  O   . ARG   A 1 256 ? 21.610  5.654   30.793  1.00 13.35 ? 268 ARG   A O   1 
ATOM   1863 C  CB  . ARG   A 1 256 ? 23.456  3.186   31.958  1.00 11.69 ? 268 ARG   A CB  1 
ATOM   1864 C  CG  . ARG   A 1 256 ? 22.002  2.859   32.337  1.00 15.06 ? 268 ARG   A CG  1 
ATOM   1865 C  CD  . ARG   A 1 256 ? 21.806  1.477   32.935  1.00 14.85 ? 268 ARG   A CD  1 
ATOM   1866 N  NE  . ARG   A 1 256 ? 22.434  1.333   34.247  1.00 13.30 ? 268 ARG   A NE  1 
ATOM   1867 C  CZ  . ARG   A 1 256 ? 22.746  0.174   34.815  1.00 14.64 ? 268 ARG   A CZ  1 
ATOM   1868 N  NH1 . ARG   A 1 256 ? 22.459  -0.986  34.244  1.00 13.30 ? 268 ARG   A NH1 1 
ATOM   1869 N  NH2 . ARG   A 1 256 ? 23.363  0.176   35.994  1.00 13.11 ? 268 ARG   A NH2 1 
ATOM   1870 N  N   . SER   A 1 257 ? 23.027  4.688   29.308  1.00 12.11 ? 269 SER   A N   1 
ATOM   1871 C  CA  . SER   A 1 257 ? 22.109  4.662   28.173  1.00 14.48 ? 269 SER   A CA  1 
ATOM   1872 C  C   . SER   A 1 257 ? 22.115  3.267   27.563  1.00 12.62 ? 269 SER   A C   1 
ATOM   1873 O  O   . SER   A 1 257 ? 22.939  2.419   27.918  1.00 12.48 ? 269 SER   A O   1 
ATOM   1874 C  CB  . SER   A 1 257 ? 22.493  5.678   27.104  1.00 15.56 ? 269 SER   A CB  1 
ATOM   1875 O  OG  . SER   A 1 257 ? 23.708  5.273   26.501  1.00 15.52 ? 269 SER   A OG  1 
ATOM   1876 N  N   . TRP   A 1 258 ? 21.212  3.044   26.601  1.00 12.86 ? 270 TRP   A N   1 
ATOM   1877 C  CA  . TRP   A 1 258 ? 21.142  1.806   25.815  1.00 13.73 ? 270 TRP   A CA  1 
ATOM   1878 C  C   . TRP   A 1 258 ? 20.869  0.575   26.680  1.00 13.12 ? 270 TRP   A C   1 
ATOM   1879 O  O   . TRP   A 1 258 ? 21.223  -0.549  26.322  1.00 11.19 ? 270 TRP   A O   1 
ATOM   1880 C  CB  . TRP   A 1 258 ? 22.418  1.644   24.986  1.00 14.34 ? 270 TRP   A CB  1 
ATOM   1881 C  CG  . TRP   A 1 258 ? 22.344  2.363   23.667  1.00 15.47 ? 270 TRP   A CG  1 
ATOM   1882 C  CD1 . TRP   A 1 258 ? 21.246  2.504   22.879  1.00 14.30 ? 270 TRP   A CD1 1 
ATOM   1883 C  CD2 . TRP   A 1 258 ? 23.410  3.055   23.003  1.00 16.55 ? 270 TRP   A CD2 1 
ATOM   1884 N  NE1 . TRP   A 1 258 ? 21.566  3.217   21.735  1.00 15.91 ? 270 TRP   A NE1 1 
ATOM   1885 C  CE2 . TRP   A 1 258 ? 22.890  3.566   21.791  1.00 17.82 ? 270 TRP   A CE2 1 
ATOM   1886 C  CE3 . TRP   A 1 258 ? 24.761  3.274   23.304  1.00 17.88 ? 270 TRP   A CE3 1 
ATOM   1887 C  CZ2 . TRP   A 1 258 ? 23.669  4.289   20.883  1.00 17.85 ? 270 TRP   A CZ2 1 
ATOM   1888 C  CZ3 . TRP   A 1 258 ? 25.540  3.999   22.401  1.00 18.64 ? 270 TRP   A CZ3 1 
ATOM   1889 C  CH2 . TRP   A 1 258 ? 24.992  4.495   21.204  1.00 17.38 ? 270 TRP   A CH2 1 
ATOM   1890 N  N   . HIS   A 1 259 ? 20.265  0.795   27.848  1.00 12.42 ? 271 HIS   A N   1 
ATOM   1891 C  CA  . HIS   A 1 259 ? 19.789  -0.224  28.762  1.00 12.60 ? 271 HIS   A CA  1 
ATOM   1892 C  C   . HIS   A 1 259 ? 18.349  -0.596  28.437  1.00 14.52 ? 271 HIS   A C   1 
ATOM   1893 O  O   . HIS   A 1 259 ? 17.661  0.094   27.688  1.00 14.23 ? 271 HIS   A O   1 
ATOM   1894 C  CB  . HIS   A 1 259 ? 19.859  0.312   30.179  1.00 12.88 ? 271 HIS   A CB  1 
ATOM   1895 C  CG  . HIS   A 1 259 ? 19.125  1.604   30.355  1.00 13.35 ? 271 HIS   A CG  1 
ATOM   1896 N  ND1 . HIS   A 1 259 ? 19.566  2.796   29.820  1.00 11.71 ? 271 HIS   A ND1 1 
ATOM   1897 C  CD2 . HIS   A 1 259 ? 17.965  1.888   30.996  1.00 14.68 ? 271 HIS   A CD2 1 
ATOM   1898 C  CE1 . HIS   A 1 259 ? 18.715  3.758   30.130  1.00 11.73 ? 271 HIS   A CE1 1 
ATOM   1899 N  NE2 . HIS   A 1 259 ? 17.745  3.235   30.860  1.00 10.08 ? 271 HIS   A NE2 1 
ATOM   1900 N  N   . SER   A 1 260 ? 17.881  -1.687  29.036  1.00 12.48 ? 272 SER   A N   1 
ATOM   1901 C  CA  . SER   A 1 260 ? 16.483  -2.074  28.931  1.00 15.48 ? 272 SER   A CA  1 
ATOM   1902 C  C   . SER   A 1 260 ? 15.799  -1.916  30.280  1.00 15.31 ? 272 SER   A C   1 
ATOM   1903 O  O   . SER   A 1 260 ? 16.418  -2.107  31.332  1.00 12.59 ? 272 SER   A O   1 
ATOM   1904 C  CB  . SER   A 1 260 ? 16.331  -3.519  28.425  1.00 16.52 ? 272 SER   A CB  1 
ATOM   1905 O  OG  . SER   A 1 260 ? 17.020  -4.448  29.243  1.00 14.03 ? 272 SER   A OG  1 
ATOM   1906 N  N   . LEU   A 1 261 ? 14.529  -1.525  30.234  1.00 12.74 ? 273 LEU   A N   1 
ATOM   1907 C  CA  . LEU   A 1 261 ? 13.685  -1.388  31.424  1.00 13.28 ? 273 LEU   A CA  1 
ATOM   1908 C  C   . LEU   A 1 261 ? 12.348  -2.023  31.093  1.00 14.35 ? 273 LEU   A C   1 
ATOM   1909 O  O   . LEU   A 1 261 ? 11.699  -1.585  30.143  1.00 15.58 ? 273 LEU   A O   1 
ATOM   1910 C  CB  . LEU   A 1 261 ? 13.495  0.079   31.788  1.00 12.34 ? 273 LEU   A CB  1 
ATOM   1911 C  CG  . LEU   A 1 261 ? 12.827  0.357   33.129  1.00 14.21 ? 273 LEU   A CG  1 
ATOM   1912 C  CD1 . LEU   A 1 261 ? 13.846  0.078   34.195  1.00 15.56 ? 273 LEU   A CD1 1 
ATOM   1913 C  CD2 . LEU   A 1 261 ? 12.365  1.787   33.214  1.00 13.21 ? 273 LEU   A CD2 1 
ATOM   1914 N  N   . THR   A 1 262 ? 11.932  -3.034  31.876  1.00 14.67 ? 274 THR   A N   1 
ATOM   1915 C  CA  . THR   A 1 262 ? 10.777  -3.877  31.561  1.00 13.13 ? 274 THR   A CA  1 
ATOM   1916 C  C   . THR   A 1 262 ? 9.873   -4.123  32.766  1.00 16.24 ? 274 THR   A C   1 
ATOM   1917 O  O   . THR   A 1 262 ? 10.342  -4.630  33.797  1.00 18.17 ? 274 THR   A O   1 
ATOM   1918 C  CB  . THR   A 1 262 ? 11.260  -5.220  31.026  1.00 17.83 ? 274 THR   A CB  1 
ATOM   1919 O  OG1 . THR   A 1 262 ? 12.327  -5.010  30.081  1.00 17.73 ? 274 THR   A OG1 1 
ATOM   1920 C  CG2 . THR   A 1 262 ? 10.107  -5.930  30.343  1.00 18.17 ? 274 THR   A CG2 1 
ATOM   1921 N  N   . PRO   A 1 263 ? 8.569   -3.872  32.660  1.00 17.25 ? 275 PRO   A N   1 
ATOM   1922 C  CA  . PRO   A 1 263 ? 7.660   -4.257  33.756  1.00 16.49 ? 275 PRO   A CA  1 
ATOM   1923 C  C   . PRO   A 1 263 ? 7.685   -5.766  33.971  1.00 18.93 ? 275 PRO   A C   1 
ATOM   1924 O  O   . PRO   A 1 263 ? 7.618   -6.540  33.018  1.00 18.67 ? 275 PRO   A O   1 
ATOM   1925 C  CB  . PRO   A 1 263 ? 6.284   -3.779  33.267  1.00 20.50 ? 275 PRO   A CB  1 
ATOM   1926 C  CG  . PRO   A 1 263 ? 6.551   -2.864  32.122  1.00 19.88 ? 275 PRO   A CG  1 
ATOM   1927 C  CD  . PRO   A 1 263 ? 7.853   -3.281  31.518  1.00 21.24 ? 275 PRO   A CD  1 
ATOM   1928 N  N   . VAL   A 1 264 ? 7.818   -6.191  35.229  1.00 20.01 ? 276 VAL   A N   1 
ATOM   1929 C  CA  . VAL   A 1 264 ? 7.747   -7.614  35.543  1.00 19.70 ? 276 VAL   A CA  1 
ATOM   1930 C  C   . VAL   A 1 264 ? 6.614   -7.962  36.489  1.00 21.94 ? 276 VAL   A C   1 
ATOM   1931 O  O   . VAL   A 1 264 ? 6.256   -9.148  36.593  1.00 25.75 ? 276 VAL   A O   1 
ATOM   1932 C  CB  . VAL   A 1 264 ? 9.086   -8.158  36.085  1.00 20.96 ? 276 VAL   A CB  1 
ATOM   1933 C  CG1 . VAL   A 1 264 ? 10.041  -8.310  34.965  1.00 24.00 ? 276 VAL   A CG1 1 
ATOM   1934 C  CG2 . VAL   A 1 264 ? 9.666   -7.250  37.159  1.00 21.40 ? 276 VAL   A CG2 1 
ATOM   1935 N  N   . SER   A 1 265 ? 6.031   -6.983  37.167  1.00 23.53 ? 277 SER   A N   1 
ATOM   1936 C  CA  . SER   A 1 265 ? 4.831   -7.162  37.965  1.00 20.56 ? 277 SER   A CA  1 
ATOM   1937 C  C   . SER   A 1 265 ? 4.127   -5.817  37.991  1.00 24.59 ? 277 SER   A C   1 
ATOM   1938 O  O   . SER   A 1 265 ? 4.633   -4.823  37.462  1.00 24.92 ? 277 SER   A O   1 
ATOM   1939 C  CB  . SER   A 1 265 ? 5.174   -7.633  39.381  1.00 25.22 ? 277 SER   A CB  1 
ATOM   1940 O  OG  . SER   A 1 265 ? 5.842   -6.596  40.082  1.00 25.04 ? 277 SER   A OG  1 
ATOM   1941 N  N   . SER   A 1 266 ? 2.977   -5.768  38.657  1.00 22.94 ? 278 SER   A N   1 
ATOM   1942 C  CA  . SER   A 1 266 ? 2.360   -4.471  38.892  1.00 24.89 ? 278 SER   A CA  1 
ATOM   1943 C  C   . SER   A 1 266 ? 3.167   -3.601  39.850  1.00 24.82 ? 278 SER   A C   1 
ATOM   1944 O  O   . SER   A 1 266 ? 2.732   -2.482  40.156  1.00 25.60 ? 278 SER   A O   1 
ATOM   1945 C  CB  . SER   A 1 266 ? 0.943   -4.667  39.428  1.00 25.22 ? 278 SER   A CB  1 
ATOM   1946 O  OG  . SER   A 1 266 ? 0.959   -5.339  40.678  1.00 31.21 ? 278 SER   A OG  1 
ATOM   1947 N  N   . ASP   A 1 267 ? 4.332   -4.076  40.316  1.00 21.37 ? 279 ASP   A N   1 
ATOM   1948 C  CA  . ASP   A 1 267 ? 5.123   -3.331  41.284  1.00 22.06 ? 279 ASP   A CA  1 
ATOM   1949 C  C   . ASP   A 1 267 ? 6.623   -3.387  41.031  1.00 21.84 ? 279 ASP   A C   1 
ATOM   1950 O  O   . ASP   A 1 267 ? 7.388   -2.923  41.883  1.00 22.76 ? 279 ASP   A O   1 
ATOM   1951 C  CB  . ASP   A 1 267 ? 4.849   -3.856  42.696  1.00 21.25 ? 279 ASP   A CB  1 
ATOM   1952 C  CG  . ASP   A 1 267 ? 5.279   -2.877  43.778  1.00 20.31 ? 279 ASP   A CG  1 
ATOM   1953 O  OD1 . ASP   A 1 267 ? 5.000   -1.670  43.622  1.00 23.99 ? 279 ASP   A OD1 1 
ATOM   1954 O  OD2 . ASP   A 1 267 ? 5.890   -3.316  44.778  1.00 26.70 ? 279 ASP   A OD2 1 
ATOM   1955 N  N   . HIS   A 1 268 ? 7.089   -3.932  39.906  1.00 18.45 ? 280 HIS   A N   1 
ATOM   1956 C  CA  . HIS   A 1 268 ? 8.529   -4.065  39.735  1.00 15.69 ? 280 HIS   A CA  1 
ATOM   1957 C  C   . HIS   A 1 268 ? 8.896   -3.784  38.292  1.00 16.01 ? 280 HIS   A C   1 
ATOM   1958 O  O   . HIS   A 1 268 ? 8.210   -4.258  37.391  1.00 18.07 ? 280 HIS   A O   1 
ATOM   1959 C  CB  . HIS   A 1 268 ? 9.015   -5.460  40.098  1.00 18.43 ? 280 HIS   A CB  1 
ATOM   1960 C  CG  . HIS   A 1 268 ? 8.838   -5.802  41.541  1.00 22.87 ? 280 HIS   A CG  1 
ATOM   1961 N  ND1 . HIS   A 1 268 ? 7.638   -6.239  42.053  1.00 23.69 ? 280 HIS   A ND1 1 
ATOM   1962 C  CD2 . HIS   A 1 268 ? 9.707   -5.778  42.579  1.00 26.36 ? 280 HIS   A CD2 1 
ATOM   1963 C  CE1 . HIS   A 1 268 ? 7.772   -6.466  43.349  1.00 28.63 ? 280 HIS   A CE1 1 
ATOM   1964 N  NE2 . HIS   A 1 268 ? 9.020   -6.199  43.692  1.00 22.12 ? 280 HIS   A NE2 1 
ATOM   1965 N  N   . LEU   A 1 269 ? 9.975   -3.032  38.096  1.00 15.90 ? 281 LEU   A N   1 
ATOM   1966 C  CA  . LEU   A 1 269 ? 10.569  -2.813  36.778  1.00 16.78 ? 281 LEU   A CA  1 
ATOM   1967 C  C   . LEU   A 1 269 ? 11.930  -3.490  36.756  1.00 20.69 ? 281 LEU   A C   1 
ATOM   1968 O  O   . LEU   A 1 269 ? 12.708  -3.346  37.706  1.00 23.85 ? 281 LEU   A O   1 
ATOM   1969 C  CB  . LEU   A 1 269 ? 10.729  -1.322  36.475  1.00 16.63 ? 281 LEU   A CB  1 
ATOM   1970 C  CG  . LEU   A 1 269 ? 9.546   -0.394  36.789  1.00 16.88 ? 281 LEU   A CG  1 
ATOM   1971 C  CD1 . LEU   A 1 269 ? 9.917   1.054   36.517  1.00 18.80 ? 281 LEU   A CD1 1 
ATOM   1972 C  CD2 . LEU   A 1 269 ? 8.376   -0.796  35.955  1.00 18.82 ? 281 LEU   A CD2 1 
ATOM   1973 N  N   . PHE   A 1 270 ? 12.223  -4.218  35.682  1.00 15.92 ? 282 PHE   A N   1 
ATOM   1974 C  CA  . PHE   A 1 270 ? 13.482  -4.935  35.576  1.00 15.96 ? 282 PHE   A CA  1 
ATOM   1975 C  C   . PHE   A 1 270 ? 14.425  -4.169  34.660  1.00 13.86 ? 282 PHE   A C   1 
ATOM   1976 O  O   . PHE   A 1 270 ? 14.052  -3.848  33.528  1.00 14.74 ? 282 PHE   A O   1 
ATOM   1977 C  CB  . PHE   A 1 270 ? 13.273  -6.355  35.053  1.00 18.34 ? 282 PHE   A CB  1 
ATOM   1978 C  CG  . PHE   A 1 270 ? 14.542  -7.159  34.974  1.00 14.96 ? 282 PHE   A CG  1 
ATOM   1979 C  CD1 . PHE   A 1 270 ? 15.105  -7.710  36.126  1.00 18.80 ? 282 PHE   A CD1 1 
ATOM   1980 C  CD2 . PHE   A 1 270 ? 15.170  -7.379  33.757  1.00 17.87 ? 282 PHE   A CD2 1 
ATOM   1981 C  CE1 . PHE   A 1 270 ? 16.277  -8.450  36.060  1.00 21.49 ? 282 PHE   A CE1 1 
ATOM   1982 C  CE2 . PHE   A 1 270 ? 16.345  -8.126  33.686  1.00 20.36 ? 282 PHE   A CE2 1 
ATOM   1983 C  CZ  . PHE   A 1 270 ? 16.893  -8.658  34.837  1.00 22.12 ? 282 PHE   A CZ  1 
ATOM   1984 N  N   . LEU   A 1 271 ? 15.632  -3.879  35.165  1.00 15.77 ? 283 LEU   A N   1 
ATOM   1985 C  CA  . LEU   A 1 271 ? 16.683  -3.142  34.460  1.00 14.44 ? 283 LEU   A CA  1 
ATOM   1986 C  C   . LEU   A 1 271 ? 17.826  -4.089  34.114  1.00 14.91 ? 283 LEU   A C   1 
ATOM   1987 O  O   . LEU   A 1 271 ? 18.239  -4.899  34.948  1.00 16.01 ? 283 LEU   A O   1 
ATOM   1988 C  CB  . LEU   A 1 271 ? 17.209  -1.980  35.320  1.00 16.78 ? 283 LEU   A CB  1 
ATOM   1989 C  CG  . LEU   A 1 271 ? 18.486  -1.227  34.893  1.00 14.97 ? 283 LEU   A CG  1 
ATOM   1990 C  CD1 . LEU   A 1 271 ? 18.209  -0.342  33.662  1.00 15.09 ? 283 LEU   A CD1 1 
ATOM   1991 C  CD2 . LEU   A 1 271 ? 19.071  -0.402  36.045  1.00 15.49 ? 283 LEU   A CD2 1 
ATOM   1992 N  N   . PHE   A 1 272 ? 18.321  -4.013  32.879  1.00 11.28 ? 284 PHE   A N   1 
ATOM   1993 C  CA  . PHE   A 1 272 ? 19.506  -4.784  32.520  1.00 16.64 ? 284 PHE   A CA  1 
ATOM   1994 C  C   . PHE   A 1 272 ? 20.381  -4.026  31.539  1.00 16.20 ? 284 PHE   A C   1 
ATOM   1995 O  O   . PHE   A 1 272 ? 19.883  -3.442  30.577  1.00 15.12 ? 284 PHE   A O   1 
ATOM   1996 C  CB  . PHE   A 1 272 ? 19.177  -6.137  31.888  1.00 17.68 ? 284 PHE   A CB  1 
ATOM   1997 C  CG  . PHE   A 1 272 ? 20.403  -6.876  31.409  1.00 16.06 ? 284 PHE   A CG  1 
ATOM   1998 C  CD1 . PHE   A 1 272 ? 21.365  -7.306  32.327  1.00 18.58 ? 284 PHE   A CD1 1 
ATOM   1999 C  CD2 . PHE   A 1 272 ? 20.618  -7.113  30.053  1.00 16.12 ? 284 PHE   A CD2 1 
ATOM   2000 C  CE1 . PHE   A 1 272 ? 22.497  -7.983  31.901  1.00 19.38 ? 284 PHE   A CE1 1 
ATOM   2001 C  CE2 . PHE   A 1 272 ? 21.744  -7.796  29.633  1.00 18.77 ? 284 PHE   A CE2 1 
ATOM   2002 C  CZ  . PHE   A 1 272 ? 22.681  -8.233  30.549  1.00 17.34 ? 284 PHE   A CZ  1 
ATOM   2003 N  N   . GLY   A 1 273 ? 21.698  -4.065  31.794  1.00 14.98 ? 285 GLY   A N   1 
ATOM   2004 C  CA  . GLY   A 1 273 ? 22.722  -3.624  30.872  1.00 13.42 ? 285 GLY   A CA  1 
ATOM   2005 C  C   . GLY   A 1 273 ? 22.832  -2.122  30.651  1.00 13.41 ? 285 GLY   A C   1 
ATOM   2006 O  O   . GLY   A 1 273 ? 22.454  -1.288  31.480  1.00 13.91 ? 285 GLY   A O   1 
ATOM   2007 N  N   . GLY   A 1 274 ? 23.366  -1.790  29.487  1.00 16.38 ? 286 GLY   A N   1 
ATOM   2008 C  CA  . GLY   A 1 274 ? 23.553  -0.418  29.086  1.00 15.23 ? 286 GLY   A CA  1 
ATOM   2009 C  C   . GLY   A 1 274 ? 25.016  -0.038  29.003  1.00 13.97 ? 286 GLY   A C   1 
ATOM   2010 O  O   . GLY   A 1 274 ? 25.904  -0.880  28.863  1.00 13.00 ? 286 GLY   A O   1 
ATOM   2011 N  N   . PHE   A 1 275 ? 25.260  1.269   29.114  1.00 13.50 ? 287 PHE   A N   1 
ATOM   2012 C  CA  . PHE   A 1 275 ? 26.531  1.874   28.733  1.00 13.26 ? 287 PHE   A CA  1 
ATOM   2013 C  C   . PHE   A 1 275 ? 26.777  3.098   29.603  1.00 13.58 ? 287 PHE   A C   1 
ATOM   2014 O  O   . PHE   A 1 275 ? 25.982  4.038   29.551  1.00 13.77 ? 287 PHE   A O   1 
ATOM   2015 C  CB  . PHE   A 1 275 ? 26.441  2.264   27.253  1.00 13.55 ? 287 PHE   A CB  1 
ATOM   2016 C  CG  . PHE   A 1 275 ? 27.744  2.575   26.609  1.00 14.77 ? 287 PHE   A CG  1 
ATOM   2017 C  CD1 . PHE   A 1 275 ? 28.848  1.765   26.810  1.00 19.27 ? 287 PHE   A CD1 1 
ATOM   2018 C  CD2 . PHE   A 1 275 ? 27.848  3.661   25.754  1.00 15.92 ? 287 PHE   A CD2 1 
ATOM   2019 C  CE1 . PHE   A 1 275 ? 30.039  2.030   26.182  1.00 18.08 ? 287 PHE   A CE1 1 
ATOM   2020 C  CE2 . PHE   A 1 275 ? 29.053  3.947   25.116  1.00 19.28 ? 287 PHE   A CE2 1 
ATOM   2021 C  CZ  . PHE   A 1 275 ? 30.155  3.132   25.339  1.00 20.98 ? 287 PHE   A CZ  1 
ATOM   2022 N  N   . THR   A 1 276 ? 27.866  3.113   30.383  1.00 14.13 ? 288 THR   A N   1 
ATOM   2023 C  CA  . THR   A 1 276 ? 28.049  4.230   31.304  1.00 14.90 ? 288 THR   A CA  1 
ATOM   2024 C  C   . THR   A 1 276 ? 28.566  5.483   30.585  1.00 17.03 ? 288 THR   A C   1 
ATOM   2025 O  O   . THR   A 1 276 ? 28.939  5.460   29.405  1.00 16.45 ? 288 THR   A O   1 
ATOM   2026 C  CB  . THR   A 1 276 ? 29.013  3.868   32.441  1.00 19.62 ? 288 THR   A CB  1 
ATOM   2027 O  OG1 . THR   A 1 276 ? 30.352  3.768   31.932  1.00 20.83 ? 288 THR   A OG1 1 
ATOM   2028 C  CG2 . THR   A 1 276 ? 28.605  2.554   33.114  1.00 18.29 ? 288 THR   A CG2 1 
ATOM   2029 N  N   . THR   A 1 277 ? 28.577  6.595   31.334  1.00 15.07 ? 289 THR   A N   1 
ATOM   2030 C  CA  . THR   A 1 277 ? 29.170  7.849   30.868  1.00 18.72 ? 289 THR   A CA  1 
ATOM   2031 C  C   . THR   A 1 277 ? 30.602  7.652   30.375  1.00 19.91 ? 289 THR   A C   1 
ATOM   2032 O  O   . THR   A 1 277 ? 30.977  8.129   29.294  1.00 21.51 ? 289 THR   A O   1 
ATOM   2033 C  CB  . THR   A 1 277 ? 29.130  8.882   31.998  1.00 22.17 ? 289 THR   A CB  1 
ATOM   2034 O  OG1 . THR   A 1 277 ? 27.767  9.211   32.298  1.00 19.32 ? 289 THR   A OG1 1 
ATOM   2035 C  CG2 . THR   A 1 277 ? 29.886  10.144  31.624  1.00 21.23 ? 289 THR   A CG2 1 
ATOM   2036 N  N   . ASP   A 1 278 ? 31.418  6.930   31.138  1.00 21.42 ? 290 ASP   A N   1 
ATOM   2037 C  CA  A ASP   A 1 278 ? 32.805  6.695   30.774  0.45 21.40 ? 290 ASP   A CA  1 
ATOM   2038 C  CA  B ASP   A 1 278 ? 32.806  6.707   30.753  0.55 22.25 ? 290 ASP   A CA  1 
ATOM   2039 C  C   . ASP   A 1 278 ? 32.970  5.470   29.879  1.00 21.48 ? 290 ASP   A C   1 
ATOM   2040 O  O   . ASP   A 1 278 ? 34.069  4.916   29.797  1.00 25.77 ? 290 ASP   A O   1 
ATOM   2041 C  CB  A ASP   A 1 278 ? 33.659  6.581   32.041  0.45 23.35 ? 290 ASP   A CB  1 
ATOM   2042 C  CB  B ASP   A 1 278 ? 33.708  6.630   31.993  0.55 23.98 ? 290 ASP   A CB  1 
ATOM   2043 C  CG  A ASP   A 1 278 ? 33.462  7.763   32.983  0.45 25.25 ? 290 ASP   A CG  1 
ATOM   2044 C  CG  B ASP   A 1 278 ? 33.601  5.307   32.723  0.55 23.90 ? 290 ASP   A CG  1 
ATOM   2045 O  OD1 A ASP   A 1 278 ? 33.631  8.919   32.547  0.45 26.30 ? 290 ASP   A OD1 1 
ATOM   2046 O  OD1 B ASP   A 1 278 ? 32.529  4.679   32.658  0.55 25.11 ? 290 ASP   A OD1 1 
ATOM   2047 O  OD2 A ASP   A 1 278 ? 33.125  7.539   34.164  0.45 27.15 ? 290 ASP   A OD2 1 
ATOM   2048 O  OD2 B ASP   A 1 278 ? 34.591  4.902   33.372  0.55 26.66 ? 290 ASP   A OD2 1 
ATOM   2049 N  N   . LYS   A 1 279 ? 31.890  5.037   29.218  1.00 22.01 ? 291 LYS   A N   1 
ATOM   2050 C  CA  . LYS   A 1 279 ? 31.921  4.042   28.150  1.00 21.23 ? 291 LYS   A CA  1 
ATOM   2051 C  C   . LYS   A 1 279 ? 32.278  2.635   28.641  1.00 22.14 ? 291 LYS   A C   1 
ATOM   2052 O  O   . LYS   A 1 279 ? 33.028  1.908   27.992  1.00 23.37 ? 291 LYS   A O   1 
ATOM   2053 C  CB  . LYS   A 1 279 ? 32.856  4.493   27.022  1.00 22.46 ? 291 LYS   A CB  1 
ATOM   2054 C  CG  . LYS   A 1 279 ? 32.548  5.908   26.544  1.00 19.57 ? 291 LYS   A CG  1 
ATOM   2055 C  CD  . LYS   A 1 279 ? 33.076  6.156   25.136  1.00 22.19 ? 291 LYS   A CD  1 
ATOM   2056 C  CE  . LYS   A 1 279 ? 32.949  7.619   24.738  1.00 28.25 ? 291 LYS   A CE  1 
ATOM   2057 N  NZ  . LYS   A 1 279 ? 32.957  7.816   23.250  1.00 25.84 ? 291 LYS   A NZ  1 
ATOM   2058 N  N   . GLN   A 1 280 ? 31.708  2.225   29.777  1.00 19.24 ? 292 GLN   A N   1 
ATOM   2059 C  CA  . GLN   A 1 280 ? 31.799  0.834   30.209  1.00 20.16 ? 292 GLN   A CA  1 
ATOM   2060 C  C   . GLN   A 1 280 ? 30.550  0.074   29.775  1.00 21.60 ? 292 GLN   A C   1 
ATOM   2061 O  O   . GLN   A 1 280 ? 29.439  0.493   30.130  1.00 17.85 ? 292 GLN   A O   1 
ATOM   2062 C  CB  . GLN   A 1 280 ? 31.964  0.755   31.725  1.00 22.82 ? 292 GLN   A CB  1 
ATOM   2063 C  CG  . GLN   A 1 280 ? 33.410  0.673   32.207  1.00 29.78 ? 292 GLN   A CG  1 
ATOM   2064 C  CD  . GLN   A 1 280 ? 33.993  -0.719  32.047  1.00 33.72 ? 292 GLN   A CD  1 
ATOM   2065 O  OE1 . GLN   A 1 280 ? 33.290  -1.661  31.659  1.00 34.46 ? 292 GLN   A OE1 1 
ATOM   2066 N  NE2 . GLN   A 1 280 ? 35.278  -0.861  32.355  1.00 38.45 ? 292 GLN   A NE2 1 
ATOM   2067 N  N   . PRO   A 1 281 ? 30.669  -1.008  28.996  1.00 15.62 ? 293 PRO   A N   1 
ATOM   2068 C  CA  . PRO   A 1 281 ? 29.544  -1.943  28.845  1.00 17.57 ? 293 PRO   A CA  1 
ATOM   2069 C  C   . PRO   A 1 281 ? 29.137  -2.549  30.184  1.00 16.97 ? 293 PRO   A C   1 
ATOM   2070 O  O   . PRO   A 1 281 ? 29.981  -2.939  30.990  1.00 18.81 ? 293 PRO   A O   1 
ATOM   2071 C  CB  . PRO   A 1 281 ? 30.094  -3.014  27.904  1.00 18.49 ? 293 PRO   A CB  1 
ATOM   2072 C  CG  . PRO   A 1 281 ? 31.268  -2.344  27.182  1.00 16.48 ? 293 PRO   A CG  1 
ATOM   2073 C  CD  . PRO   A 1 281 ? 31.832  -1.373  28.164  1.00 20.11 ? 293 PRO   A CD  1 
ATOM   2074 N  N   . LEU   A 1 282 ? 27.828  -2.677  30.390  1.00 17.22 ? 294 LEU   A N   1 
ATOM   2075 C  CA  . LEU   A 1 282 ? 27.273  -3.113  31.664  1.00 15.16 ? 294 LEU   A CA  1 
ATOM   2076 C  C   . LEU   A 1 282 ? 26.616  -4.483  31.565  1.00 16.43 ? 294 LEU   A C   1 
ATOM   2077 O  O   . LEU   A 1 282 ? 25.909  -4.781  30.594  1.00 14.72 ? 294 LEU   A O   1 
ATOM   2078 C  CB  . LEU   A 1 282 ? 26.228  -2.124  32.186  1.00 14.56 ? 294 LEU   A CB  1 
ATOM   2079 C  CG  . LEU   A 1 282 ? 26.724  -0.720  32.481  1.00 12.06 ? 294 LEU   A CG  1 
ATOM   2080 C  CD1 . LEU   A 1 282 ? 25.550  0.202   32.795  1.00 12.23 ? 294 LEU   A CD1 1 
ATOM   2081 C  CD2 . LEU   A 1 282 ? 27.684  -0.786  33.640  1.00 15.82 ? 294 LEU   A CD2 1 
ATOM   2082 N  N   . SER   A 1 283 ? 26.813  -5.286  32.614  1.00 16.42 ? 295 SER   A N   1 
ATOM   2083 C  CA  . SER   A 1 283 ? 26.135  -6.562  32.794  1.00 18.32 ? 295 SER   A CA  1 
ATOM   2084 C  C   . SER   A 1 283 ? 25.318  -6.607  34.083  1.00 18.53 ? 295 SER   A C   1 
ATOM   2085 O  O   . SER   A 1 283 ? 24.888  -7.687  34.497  1.00 19.64 ? 295 SER   A O   1 
ATOM   2086 C  CB  . SER   A 1 283 ? 27.159  -7.701  32.790  1.00 20.47 ? 295 SER   A CB  1 
ATOM   2087 O  OG  . SER   A 1 283 ? 27.942  -7.618  33.962  1.00 18.83 ? 295 SER   A OG  1 
ATOM   2088 N  N   . ASP   A 1 284 ? 25.086  -5.473  34.727  1.00 19.68 ? 296 ASP   A N   1 
ATOM   2089 C  CA  . ASP   A 1 284 ? 24.324  -5.518  35.962  1.00 18.84 ? 296 ASP   A CA  1 
ATOM   2090 C  C   . ASP   A 1 284 ? 22.824  -5.551  35.679  1.00 19.68 ? 296 ASP   A C   1 
ATOM   2091 O  O   . ASP   A 1 284 ? 22.352  -5.180  34.605  1.00 17.30 ? 296 ASP   A O   1 
ATOM   2092 C  CB  . ASP   A 1 284 ? 24.675  -4.342  36.873  1.00 19.18 ? 296 ASP   A CB  1 
ATOM   2093 C  CG  . ASP   A 1 284 ? 24.442  -2.992  36.232  1.00 17.15 ? 296 ASP   A CG  1 
ATOM   2094 O  OD1 . ASP   A 1 284 ? 24.509  -2.856  34.986  1.00 21.52 ? 296 ASP   A OD1 1 
ATOM   2095 O  OD2 . ASP   A 1 284 ? 24.204  -2.036  36.992  1.00 20.24 ? 296 ASP   A OD2 1 
ATOM   2096 N  N   . ALA   A 1 285 ? 22.080  -6.028  36.669  1.00 19.48 ? 297 ALA   A N   1 
ATOM   2097 C  CA  . ALA   A 1 285 ? 20.634  -6.136  36.578  1.00 19.44 ? 297 ALA   A CA  1 
ATOM   2098 C  C   . ALA   A 1 285 ? 20.034  -5.739  37.912  1.00 18.34 ? 297 ALA   A C   1 
ATOM   2099 O  O   . ALA   A 1 285 ? 20.591  -6.064  38.964  1.00 23.40 ? 297 ALA   A O   1 
ATOM   2100 C  CB  . ALA   A 1 285 ? 20.208  -7.561  36.195  1.00 21.08 ? 297 ALA   A CB  1 
ATOM   2101 N  N   . TRP   A 1 286 ? 18.918  -5.009  37.864  1.00 15.46 ? 298 TRP   A N   1 
ATOM   2102 C  CA  . TRP   A 1 286 ? 18.242  -4.541  39.064  1.00 20.29 ? 298 TRP   A CA  1 
ATOM   2103 C  C   . TRP   A 1 286 ? 16.742  -4.698  38.885  1.00 18.41 ? 298 TRP   A C   1 
ATOM   2104 O  O   . TRP   A 1 286 ? 16.225  -4.735  37.766  1.00 19.15 ? 298 TRP   A O   1 
ATOM   2105 C  CB  . TRP   A 1 286 ? 18.523  -3.062  39.377  1.00 16.99 ? 298 TRP   A CB  1 
ATOM   2106 C  CG  . TRP   A 1 286 ? 19.948  -2.681  39.451  1.00 21.11 ? 298 TRP   A CG  1 
ATOM   2107 C  CD1 . TRP   A 1 286 ? 20.844  -2.651  38.423  1.00 17.61 ? 298 TRP   A CD1 1 
ATOM   2108 C  CD2 . TRP   A 1 286 ? 20.650  -2.232  40.616  1.00 18.25 ? 298 TRP   A CD2 1 
ATOM   2109 N  NE1 . TRP   A 1 286 ? 22.078  -2.239  38.882  1.00 18.53 ? 298 TRP   A NE1 1 
ATOM   2110 C  CE2 . TRP   A 1 286 ? 21.978  -1.953  40.220  1.00 18.33 ? 298 TRP   A CE2 1 
ATOM   2111 C  CE3 . TRP   A 1 286 ? 20.283  -2.032  41.957  1.00 17.63 ? 298 TRP   A CE3 1 
ATOM   2112 C  CZ2 . TRP   A 1 286 ? 22.948  -1.513  41.121  1.00 19.91 ? 298 TRP   A CZ2 1 
ATOM   2113 C  CZ3 . TRP   A 1 286 ? 21.241  -1.578  42.844  1.00 21.26 ? 298 TRP   A CZ3 1 
ATOM   2114 C  CH2 . TRP   A 1 286 ? 22.557  -1.323  42.424  1.00 18.68 ? 298 TRP   A CH2 1 
ATOM   2115 N  N   . THR   A 1 287 ? 16.033  -4.740  40.007  1.00 18.31 ? 299 THR   A N   1 
ATOM   2116 C  CA  . THR   A 1 287 ? 14.587  -4.576  39.971  1.00 20.09 ? 299 THR   A CA  1 
ATOM   2117 C  C   . THR   A 1 287 ? 14.245  -3.312  40.746  1.00 21.58 ? 299 THR   A C   1 
ATOM   2118 O  O   . THR   A 1 287 ? 14.751  -3.103  41.852  1.00 25.37 ? 299 THR   A O   1 
ATOM   2119 C  CB  . THR   A 1 287 ? 13.860  -5.796  40.549  1.00 24.54 ? 299 THR   A CB  1 
ATOM   2120 O  OG1 . THR   A 1 287 ? 14.162  -6.966  39.774  1.00 29.28 ? 299 THR   A OG1 1 
ATOM   2121 C  CG2 . THR   A 1 287 ? 12.391  -5.577  40.519  1.00 23.19 ? 299 THR   A CG2 1 
ATOM   2122 N  N   . TYR   A 1 288 ? 13.413  -2.456  40.157  1.00 20.28 ? 300 TYR   A N   1 
ATOM   2123 C  CA  . TYR   A 1 288 ? 12.919  -1.284  40.862  1.00 18.58 ? 300 TYR   A CA  1 
ATOM   2124 C  C   . TYR   A 1 288 ? 11.559  -1.615  41.455  1.00 17.91 ? 300 TYR   A C   1 
ATOM   2125 O  O   . TYR   A 1 288 ? 10.609  -1.897  40.721  1.00 19.75 ? 300 TYR   A O   1 
ATOM   2126 C  CB  . TYR   A 1 288 ? 12.830  -0.065  39.942  1.00 19.51 ? 300 TYR   A CB  1 
ATOM   2127 C  CG  . TYR   A 1 288 ? 12.204  1.130   40.621  1.00 16.96 ? 300 TYR   A CG  1 
ATOM   2128 C  CD1 . TYR   A 1 288 ? 12.894  1.826   41.613  1.00 17.30 ? 300 TYR   A CD1 1 
ATOM   2129 C  CD2 . TYR   A 1 288 ? 10.921  1.569   40.277  1.00 16.02 ? 300 TYR   A CD2 1 
ATOM   2130 C  CE1 . TYR   A 1 288 ? 12.323  2.918   42.261  1.00 24.91 ? 300 TYR   A CE1 1 
ATOM   2131 C  CE2 . TYR   A 1 288 ? 10.348  2.667   40.908  1.00 19.54 ? 300 TYR   A CE2 1 
ATOM   2132 C  CZ  . TYR   A 1 288 ? 11.048  3.335   41.906  1.00 16.94 ? 300 TYR   A CZ  1 
ATOM   2133 O  OH  . TYR   A 1 288 ? 10.488  4.422   42.537  1.00 22.61 ? 300 TYR   A OH  1 
ATOM   2134 N  N   . CYS   A 1 289 ? 11.481  -1.617  42.782  1.00 17.82 ? 301 CYS   A N   1 
ATOM   2135 C  CA  . CYS   A 1 289 ? 10.221  -1.826  43.488  1.00 18.34 ? 301 CYS   A CA  1 
ATOM   2136 C  C   . CYS   A 1 289 ? 9.509   -0.486  43.584  1.00 20.05 ? 301 CYS   A C   1 
ATOM   2137 O  O   . CYS   A 1 289 ? 10.022  0.449   44.211  1.00 20.20 ? 301 CYS   A O   1 
ATOM   2138 C  CB  . CYS   A 1 289 ? 10.463  -2.418  44.875  1.00 20.97 ? 301 CYS   A CB  1 
ATOM   2139 S  SG  . CYS   A 1 289 ? 8.932   -2.711  45.728  1.00 26.37 ? 301 CYS   A SG  1 
ATOM   2140 N  N   . ILE   A 1 290 ? 8.353   -0.385  42.921  1.00 19.22 ? 302 ILE   A N   1 
ATOM   2141 C  CA  . ILE   A 1 290 ? 7.635   0.881   42.824  1.00 18.87 ? 302 ILE   A CA  1 
ATOM   2142 C  C   . ILE   A 1 290 ? 7.100   1.295   44.188  1.00 21.06 ? 302 ILE   A C   1 
ATOM   2143 O  O   . ILE   A 1 290 ? 7.240   2.450   44.601  1.00 23.29 ? 302 ILE   A O   1 
ATOM   2144 C  CB  . ILE   A 1 290 ? 6.493   0.763   41.796  1.00 21.01 ? 302 ILE   A CB  1 
ATOM   2145 C  CG1 . ILE   A 1 290 ? 7.048   0.581   40.387  1.00 17.40 ? 302 ILE   A CG1 1 
ATOM   2146 C  CG2 . ILE   A 1 290 ? 5.577   1.978   41.850  1.00 20.13 ? 302 ILE   A CG2 1 
ATOM   2147 C  CD1 . ILE   A 1 290 ? 6.045   0.003   39.441  1.00 19.32 ? 302 ILE   A CD1 1 
ATOM   2148 N  N   . SER   A 1 291 ? 6.454   0.358   44.890  1.00 22.26 ? 303 SER   A N   1 
ATOM   2149 C  CA  . SER   A 1 291 ? 5.812   0.668   46.165  1.00 24.24 ? 303 SER   A CA  1 
ATOM   2150 C  C   . SER   A 1 291 ? 6.830   1.092   47.215  1.00 22.64 ? 303 SER   A C   1 
ATOM   2151 O  O   . SER   A 1 291 ? 6.548   1.956   48.055  1.00 23.82 ? 303 SER   A O   1 
ATOM   2152 C  CB  . SER   A 1 291 ? 5.031   -0.547  46.652  1.00 23.31 ? 303 SER   A CB  1 
ATOM   2153 O  OG  . SER   A 1 291 ? 5.915   -1.639  46.859  1.00 22.73 ? 303 SER   A OG  1 
ATOM   2154 N  N   . LYS   A 1 292 ? 8.005   0.479   47.206  1.00 23.64 ? 304 LYS   A N   1 
ATOM   2155 C  CA  . LYS   A 1 292 ? 9.044   0.838   48.158  1.00 25.04 ? 304 LYS   A CA  1 
ATOM   2156 C  C   . LYS   A 1 292 ? 9.954   1.957   47.676  1.00 22.03 ? 304 LYS   A C   1 
ATOM   2157 O  O   . LYS   A 1 292 ? 10.724  2.489   48.491  1.00 26.50 ? 304 LYS   A O   1 
ATOM   2158 C  CB  . LYS   A 1 292 ? 9.886   -0.393  48.506  1.00 27.47 ? 304 LYS   A CB  1 
ATOM   2159 C  CG  . LYS   A 1 292 ? 9.155   -1.398  49.389  1.00 29.62 ? 304 LYS   A CG  1 
ATOM   2160 C  CD  . LYS   A 1 292 ? 9.872   -2.742  49.473  1.00 30.27 ? 304 LYS   A CD  1 
ATOM   2161 C  CE  . LYS   A 1 292 ? 11.320  -2.595  49.901  1.00 37.47 ? 304 LYS   A CE  1 
ATOM   2162 N  NZ  . LYS   A 1 292 ? 12.253  -2.534  48.733  1.00 34.67 ? 304 LYS   A NZ  1 
ATOM   2163 N  N   . ASN   A 1 293 ? 9.865   2.341   46.399  1.00 24.12 ? 305 ASN   A N   1 
ATOM   2164 C  CA  . ASN   A 1 293 ? 10.773  3.320   45.802  1.00 21.42 ? 305 ASN   A CA  1 
ATOM   2165 C  C   . ASN   A 1 293 ? 12.217  2.953   46.132  1.00 23.10 ? 305 ASN   A C   1 
ATOM   2166 O  O   . ASN   A 1 293 ? 12.968  3.723   46.740  1.00 23.90 ? 305 ASN   A O   1 
ATOM   2167 C  CB  . ASN   A 1 293 ? 10.424  4.740   46.253  1.00 24.22 ? 305 ASN   A CB  1 
ATOM   2168 C  CG  . ASN   A 1 293 ? 11.275  5.813   45.584  1.00 24.71 ? 305 ASN   A CG  1 
ATOM   2169 O  OD1 . ASN   A 1 293 ? 11.653  5.697   44.416  1.00 23.54 ? 305 ASN   A OD1 1 
ATOM   2170 N  ND2 . ASN   A 1 293 ? 11.570  6.881   46.335  1.00 26.57 ? 305 ASN   A ND2 1 
ATOM   2171 N  N   . GLU   A 1 294 ? 12.586  1.726   45.770  1.00 21.10 ? 306 GLU   A N   1 
ATOM   2172 C  CA  . GLU   A 1 294 ? 13.901  1.187   46.097  1.00 24.15 ? 306 GLU   A CA  1 
ATOM   2173 C  C   . GLU   A 1 294 ? 14.391  0.284   44.976  1.00 23.79 ? 306 GLU   A C   1 
ATOM   2174 O  O   . GLU   A 1 294 ? 13.616  -0.502  44.423  1.00 20.70 ? 306 GLU   A O   1 
ATOM   2175 C  CB  . GLU   A 1 294 ? 13.877  0.395   47.416  1.00 25.58 ? 306 GLU   A CB  1 
ATOM   2176 C  CG  . GLU   A 1 294 ? 15.103  -0.490  47.640  1.00 29.75 ? 306 GLU   A CG  1 
ATOM   2177 C  CD  . GLU   A 1 294 ? 15.018  -1.333  48.909  1.00 34.76 ? 306 GLU   A CD  1 
ATOM   2178 O  OE1 . GLU   A 1 294 ? 15.228  -0.769  50.004  1.00 34.28 ? 306 GLU   A OE1 1 
ATOM   2179 O  OE2 . GLU   A 1 294 ? 14.739  -2.554  48.805  1.00 34.53 ? 306 GLU   A OE2 1 
ATOM   2180 N  N   . TRP   A 1 295 ? 15.688  0.382   44.664  1.00 19.21 ? 307 TRP   A N   1 
ATOM   2181 C  CA  . TRP   A 1 295 ? 16.346  -0.545  43.746  1.00 19.61 ? 307 TRP   A CA  1 
ATOM   2182 C  C   . TRP   A 1 295 ? 16.925  -1.738  44.495  1.00 23.28 ? 307 TRP   A C   1 
ATOM   2183 O  O   . TRP   A 1 295 ? 17.505  -1.587  45.577  1.00 18.64 ? 307 TRP   A O   1 
ATOM   2184 C  CB  . TRP   A 1 295 ? 17.480  0.142   42.991  1.00 17.22 ? 307 TRP   A CB  1 
ATOM   2185 C  CG  . TRP   A 1 295 ? 17.061  1.191   42.009  1.00 19.86 ? 307 TRP   A CG  1 
ATOM   2186 C  CD1 . TRP   A 1 295 ? 16.976  2.536   42.226  1.00 19.33 ? 307 TRP   A CD1 1 
ATOM   2187 C  CD2 . TRP   A 1 295 ? 16.731  0.982   40.632  1.00 14.94 ? 307 TRP   A CD2 1 
ATOM   2188 N  NE1 . TRP   A 1 295 ? 16.595  3.179   41.068  1.00 19.12 ? 307 TRP   A NE1 1 
ATOM   2189 C  CE2 . TRP   A 1 295 ? 16.442  2.244   40.076  1.00 15.01 ? 307 TRP   A CE2 1 
ATOM   2190 C  CE3 . TRP   A 1 295 ? 16.644  -0.151  39.823  1.00 15.99 ? 307 TRP   A CE3 1 
ATOM   2191 C  CZ2 . TRP   A 1 295 ? 16.077  2.406   38.733  1.00 17.89 ? 307 TRP   A CZ2 1 
ATOM   2192 C  CZ3 . TRP   A 1 295 ? 16.284  0.014   38.481  1.00 13.11 ? 307 TRP   A CZ3 1 
ATOM   2193 C  CH2 . TRP   A 1 295 ? 15.998  1.282   37.965  1.00 13.71 ? 307 TRP   A CH2 1 
ATOM   2194 N  N   . ILE   A 1 296 ? 16.771  -2.919  43.904  1.00 20.76 ? 308 ILE   A N   1 
ATOM   2195 C  CA  . ILE   A 1 296 ? 17.357  -4.158  44.394  1.00 21.74 ? 308 ILE   A CA  1 
ATOM   2196 C  C   . ILE   A 1 296 ? 18.255  -4.709  43.293  1.00 22.18 ? 308 ILE   A C   1 
ATOM   2197 O  O   . ILE   A 1 296 ? 17.813  -4.907  42.157  1.00 24.82 ? 308 ILE   A O   1 
ATOM   2198 C  CB  . ILE   A 1 296 ? 16.283  -5.181  44.819  1.00 25.46 ? 308 ILE   A CB  1 
ATOM   2199 C  CG1 . ILE   A 1 296 ? 15.470  -5.716  43.626  1.00 28.67 ? 308 ILE   A CG1 1 
ATOM   2200 C  CG2 . ILE   A 1 296 ? 15.313  -4.536  45.772  1.00 26.78 ? 308 ILE   A CG2 1 
ATOM   2201 C  CD1 . ILE   A 1 296 ? 15.924  -7.099  43.074  1.00 29.90 ? 308 ILE   A CD1 1 
ATOM   2202 N  N   . GLN   A 1 297 ? 19.521  -4.928  43.609  1.00 22.04 ? 309 GLN   A N   1 
ATOM   2203 C  CA  . GLN   A 1 297 ? 20.375  -5.566  42.626  1.00 21.08 ? 309 GLN   A CA  1 
ATOM   2204 C  C   . GLN   A 1 297 ? 19.965  -7.026  42.474  1.00 21.09 ? 309 GLN   A C   1 
ATOM   2205 O  O   . GLN   A 1 297 ? 19.614  -7.698  43.451  1.00 28.91 ? 309 GLN   A O   1 
ATOM   2206 C  CB  . GLN   A 1 297 ? 21.846  -5.438  43.027  1.00 22.54 ? 309 GLN   A CB  1 
ATOM   2207 C  CG  . GLN   A 1 297 ? 22.794  -6.013  41.987  1.00 23.82 ? 309 GLN   A CG  1 
ATOM   2208 C  CD  . GLN   A 1 297 ? 24.084  -5.223  41.871  1.00 27.75 ? 309 GLN   A CD  1 
ATOM   2209 O  OE1 . GLN   A 1 297 ? 24.342  -4.324  42.668  1.00 24.92 ? 309 GLN   A OE1 1 
ATOM   2210 N  NE2 . GLN   A 1 297 ? 24.890  -5.541  40.859  1.00 26.09 ? 309 GLN   A NE2 1 
ATOM   2211 N  N   . PHE   A 1 298 ? 19.981  -7.509  41.241  1.00 22.07 ? 310 PHE   A N   1 
ATOM   2212 C  CA  . PHE   A 1 298 ? 19.443  -8.816  40.893  1.00 25.50 ? 310 PHE   A CA  1 
ATOM   2213 C  C   . PHE   A 1 298 ? 20.592  -9.716  40.470  1.00 26.44 ? 310 PHE   A C   1 
ATOM   2214 O  O   . PHE   A 1 298 ? 21.431  -9.317  39.657  1.00 26.55 ? 310 PHE   A O   1 
ATOM   2215 C  CB  . PHE   A 1 298 ? 18.398  -8.679  39.780  1.00 25.01 ? 310 PHE   A CB  1 
ATOM   2216 C  CG  . PHE   A 1 298 ? 17.845  -9.982  39.291  1.00 24.12 ? 310 PHE   A CG  1 
ATOM   2217 C  CD1 . PHE   A 1 298 ? 18.426  -10.641 38.213  1.00 25.17 ? 310 PHE   A CD1 1 
ATOM   2218 C  CD2 . PHE   A 1 298 ? 16.728  -10.540 39.885  1.00 27.13 ? 310 PHE   A CD2 1 
ATOM   2219 C  CE1 . PHE   A 1 298 ? 17.923  -11.839 37.759  1.00 25.86 ? 310 PHE   A CE1 1 
ATOM   2220 C  CE2 . PHE   A 1 298 ? 16.216  -11.742 39.428  1.00 32.18 ? 310 PHE   A CE2 1 
ATOM   2221 C  CZ  . PHE   A 1 298 ? 16.814  -12.389 38.360  1.00 31.22 ? 310 PHE   A CZ  1 
ATOM   2222 N  N   . ASN   A 1 299 ? 20.649  -10.918 41.038  1.00 29.15 ? 311 ASN   A N   1 
ATOM   2223 C  CA  . ASN   A 1 299 ? 21.766  -11.820 40.789  1.00 29.73 ? 311 ASN   A CA  1 
ATOM   2224 C  C   . ASN   A 1 299 ? 21.429  -12.781 39.655  1.00 29.39 ? 311 ASN   A C   1 
ATOM   2225 O  O   . ASN   A 1 299 ? 20.369  -13.417 39.655  1.00 32.06 ? 311 ASN   A O   1 
ATOM   2226 C  CB  . ASN   A 1 299 ? 22.140  -12.569 42.069  1.00 34.58 ? 311 ASN   A CB  1 
ATOM   2227 C  CG  . ASN   A 1 299 ? 22.787  -11.654 43.086  1.00 38.05 ? 311 ASN   A CG  1 
ATOM   2228 O  OD1 . ASN   A 1 299 ? 23.224  -10.550 42.741  1.00 36.22 ? 311 ASN   A OD1 1 
ATOM   2229 N  ND2 . ASN   A 1 299 ? 22.864  -12.102 44.340  1.00 44.62 ? 311 ASN   A ND2 1 
ATOM   2230 N  N   . HIS   A 1 300 ? 22.327  -12.863 38.681  1.00 30.97 ? 312 HIS   A N   1 
ATOM   2231 C  CA  . HIS   A 1 300 ? 22.087  -13.615 37.461  1.00 29.60 ? 312 HIS   A CA  1 
ATOM   2232 C  C   . HIS   A 1 300 ? 23.405  -14.206 37.005  1.00 29.12 ? 312 HIS   A C   1 
ATOM   2233 O  O   . HIS   A 1 300 ? 24.473  -13.782 37.465  1.00 29.41 ? 312 HIS   A O   1 
ATOM   2234 C  CB  . HIS   A 1 300 ? 21.473  -12.722 36.375  1.00 29.21 ? 312 HIS   A CB  1 
ATOM   2235 C  CG  . HIS   A 1 300 ? 22.348  -11.588 35.965  1.00 28.31 ? 312 HIS   A CG  1 
ATOM   2236 N  ND1 . HIS   A 1 300 ? 23.368  -11.732 35.052  1.00 28.49 ? 312 HIS   A ND1 1 
ATOM   2237 C  CD2 . HIS   A 1 300 ? 22.360  -10.289 36.344  1.00 28.45 ? 312 HIS   A CD2 1 
ATOM   2238 C  CE1 . HIS   A 1 300 ? 23.964  -10.566 34.875  1.00 28.75 ? 312 HIS   A CE1 1 
ATOM   2239 N  NE2 . HIS   A 1 300 ? 23.372  -9.674  35.648  1.00 23.36 ? 312 HIS   A NE2 1 
ATOM   2240 N  N   . PRO   A 1 301 ? 23.374  -15.220 36.137  1.00 31.46 ? 313 PRO   A N   1 
ATOM   2241 C  CA  . PRO   A 1 301 ? 24.608  -15.869 35.683  1.00 33.57 ? 313 PRO   A CA  1 
ATOM   2242 C  C   . PRO   A 1 301 ? 25.212  -15.298 34.406  1.00 29.86 ? 313 PRO   A C   1 
ATOM   2243 O  O   . PRO   A 1 301 ? 26.105  -15.932 33.843  1.00 34.05 ? 313 PRO   A O   1 
ATOM   2244 C  CB  . PRO   A 1 301 ? 24.140  -17.312 35.454  1.00 32.05 ? 313 PRO   A CB  1 
ATOM   2245 C  CG  . PRO   A 1 301 ? 22.749  -17.150 34.955  1.00 32.98 ? 313 PRO   A CG  1 
ATOM   2246 C  CD  . PRO   A 1 301 ? 22.176  -15.938 35.655  1.00 33.60 ? 313 PRO   A CD  1 
ATOM   2247 N  N   . TYR   A 1 302 ? 24.756  -14.134 33.936  1.00 28.75 ? 314 TYR   A N   1 
ATOM   2248 C  CA  . TYR   A 1 302 ? 25.278  -13.503 32.732  1.00 27.14 ? 314 TYR   A CA  1 
ATOM   2249 C  C   . TYR   A 1 302 ? 26.197  -12.321 33.042  1.00 27.73 ? 314 TYR   A C   1 
ATOM   2250 O  O   . TYR   A 1 302 ? 26.297  -11.388 32.238  1.00 25.77 ? 314 TYR   A O   1 
ATOM   2251 C  CB  . TYR   A 1 302 ? 24.122  -13.058 31.834  1.00 28.30 ? 314 TYR   A CB  1 
ATOM   2252 C  CG  . TYR   A 1 302 ? 23.130  -14.157 31.517  1.00 28.34 ? 314 TYR   A CG  1 
ATOM   2253 C  CD1 . TYR   A 1 302 ? 23.465  -15.189 30.654  1.00 30.71 ? 314 TYR   A CD1 1 
ATOM   2254 C  CD2 . TYR   A 1 302 ? 21.854  -14.153 32.070  1.00 30.55 ? 314 TYR   A CD2 1 
ATOM   2255 C  CE1 . TYR   A 1 302 ? 22.565  -16.193 30.355  1.00 31.00 ? 314 TYR   A CE1 1 
ATOM   2256 C  CE2 . TYR   A 1 302 ? 20.948  -15.152 31.779  1.00 29.38 ? 314 TYR   A CE2 1 
ATOM   2257 C  CZ  . TYR   A 1 302 ? 21.310  -16.170 30.918  1.00 32.59 ? 314 TYR   A CZ  1 
ATOM   2258 O  OH  . TYR   A 1 302 ? 20.412  -17.167 30.616  1.00 36.53 ? 314 TYR   A OH  1 
ATOM   2259 N  N   . THR   A 1 303 ? 26.879  -12.339 34.194  1.00 27.13 ? 315 THR   A N   1 
ATOM   2260 C  CA  . THR   A 1 303 ? 27.717  -11.199 34.563  1.00 28.08 ? 315 THR   A CA  1 
ATOM   2261 C  C   . THR   A 1 303 ? 28.883  -10.985 33.599  1.00 25.62 ? 315 THR   A C   1 
ATOM   2262 O  O   . THR   A 1 303 ? 29.428  -9.876  33.541  1.00 21.27 ? 315 THR   A O   1 
ATOM   2263 C  CB  . THR   A 1 303 ? 28.228  -11.357 35.996  1.00 25.75 ? 315 THR   A CB  1 
ATOM   2264 O  OG1 . THR   A 1 303 ? 28.541  -12.731 36.250  1.00 33.35 ? 315 THR   A OG1 1 
ATOM   2265 C  CG2 . THR   A 1 303 ? 27.176  -10.903 36.977  1.00 28.40 ? 315 THR   A CG2 1 
ATOM   2266 N  N   . GLU   A 1 304 ? 29.247  -11.992 32.809  1.00 24.60 ? 316 GLU   A N   1 
ATOM   2267 C  CA  . GLU   A 1 304 ? 30.286  -11.840 31.799  1.00 29.03 ? 316 GLU   A CA  1 
ATOM   2268 C  C   . GLU   A 1 304 ? 29.709  -11.547 30.413  1.00 23.27 ? 316 GLU   A C   1 
ATOM   2269 O  O   . GLU   A 1 304 ? 30.417  -11.657 29.408  1.00 23.70 ? 316 GLU   A O   1 
ATOM   2270 C  CB  . GLU   A 1 304 ? 31.172  -13.086 31.765  1.00 29.58 ? 316 GLU   A CB  1 
ATOM   2271 C  CG  . GLU   A 1 304 ? 32.598  -12.835 31.306  1.00 33.13 ? 316 GLU   A CG  1 
ATOM   2272 C  CD  . GLU   A 1 304 ? 33.443  -14.097 31.334  1.00 37.17 ? 316 GLU   A CD  1 
ATOM   2273 O  OE1 . GLU   A 1 304 ? 33.044  -15.061 32.025  1.00 38.92 ? 316 GLU   A OE1 1 
ATOM   2274 O  OE2 . GLU   A 1 304 ? 34.502  -14.125 30.667  1.00 42.71 ? 316 GLU   A OE2 1 
ATOM   2275 N  N   . LYS   A 1 305 ? 28.442  -11.159 30.331  1.00 22.82 ? 317 LYS   A N   1 
ATOM   2276 C  CA  . LYS   A 1 305 ? 27.794  -10.883 29.048  1.00 22.95 ? 317 LYS   A CA  1 
ATOM   2277 C  C   . LYS   A 1 305 ? 27.127  -9.508  29.078  1.00 18.51 ? 317 LYS   A C   1 
ATOM   2278 O  O   . LYS   A 1 305 ? 25.898  -9.395  29.020  1.00 19.34 ? 317 LYS   A O   1 
ATOM   2279 C  CB  . LYS   A 1 305 ? 26.795  -11.990 28.698  1.00 26.50 ? 317 LYS   A CB  1 
ATOM   2280 C  CG  . LYS   A 1 305 ? 27.479  -13.308 28.314  1.00 26.52 ? 317 LYS   A CG  1 
ATOM   2281 C  CD  . LYS   A 1 305 ? 26.584  -14.237 27.517  1.00 28.66 ? 317 LYS   A CD  1 
ATOM   2282 C  CE  . LYS   A 1 305 ? 27.296  -15.540 27.197  1.00 32.47 ? 317 LYS   A CE  1 
ATOM   2283 N  NZ  . LYS   A 1 305 ? 26.346  -16.613 26.825  1.00 34.34 ? 317 LYS   A NZ  1 
ATOM   2284 N  N   . PRO   A 1 306 ? 27.917  -8.433  29.143  1.00 20.56 ? 318 PRO   A N   1 
ATOM   2285 C  CA  . PRO   A 1 306 ? 27.314  -7.099  29.107  1.00 18.39 ? 318 PRO   A CA  1 
ATOM   2286 C  C   . PRO   A 1 306 ? 26.612  -6.878  27.778  1.00 19.54 ? 318 PRO   A C   1 
ATOM   2287 O  O   . PRO   A 1 306 ? 26.997  -7.437  26.750  1.00 20.87 ? 318 PRO   A O   1 
ATOM   2288 C  CB  . PRO   A 1 306 ? 28.509  -6.154  29.289  1.00 17.00 ? 318 PRO   A CB  1 
ATOM   2289 C  CG  . PRO   A 1 306 ? 29.674  -6.933  28.829  1.00 17.49 ? 318 PRO   A CG  1 
ATOM   2290 C  CD  . PRO   A 1 306 ? 29.387  -8.360  29.200  1.00 20.05 ? 318 PRO   A CD  1 
ATOM   2291 N  N   . ARG   A 1 307 ? 25.542  -6.088  27.813  1.00 17.78 ? 319 ARG   A N   1 
ATOM   2292 C  CA  . ARG   A 1 307 ? 24.795  -5.800  26.595  1.00 18.41 ? 319 ARG   A CA  1 
ATOM   2293 C  C   . ARG   A 1 307 ? 24.353  -4.346  26.573  1.00 18.57 ? 319 ARG   A C   1 
ATOM   2294 O  O   . ARG   A 1 307 ? 23.903  -3.806  27.588  1.00 16.02 ? 319 ARG   A O   1 
ATOM   2295 C  CB  . ARG   A 1 307 ? 23.553  -6.686  26.456  1.00 18.94 ? 319 ARG   A CB  1 
ATOM   2296 C  CG  . ARG   A 1 307 ? 23.807  -8.163  26.246  1.00 19.57 ? 319 ARG   A CG  1 
ATOM   2297 C  CD  . ARG   A 1 307 ? 24.545  -8.438  24.943  1.00 17.40 ? 319 ARG   A CD  1 
ATOM   2298 N  NE  . ARG   A 1 307 ? 24.700  -9.870  24.703  1.00 21.75 ? 319 ARG   A NE  1 
ATOM   2299 C  CZ  . ARG   A 1 307 ? 25.834  -10.539 24.870  1.00 20.14 ? 319 ARG   A CZ  1 
ATOM   2300 N  NH1 . ARG   A 1 307 ? 26.930  -9.940  25.291  1.00 19.05 ? 319 ARG   A NH1 1 
ATOM   2301 N  NH2 . ARG   A 1 307 ? 25.868  -11.842 24.597  1.00 26.02 ? 319 ARG   A NH2 1 
ATOM   2302 N  N   . LEU   A 1 308 ? 24.467  -3.721  25.406  1.00 15.44 ? 320 LEU   A N   1 
ATOM   2303 C  CA  . LEU   A 1 308 ? 23.897  -2.403  25.191  1.00 16.71 ? 320 LEU   A CA  1 
ATOM   2304 C  C   . LEU   A 1 308 ? 23.216  -2.395  23.836  1.00 17.17 ? 320 LEU   A C   1 
ATOM   2305 O  O   . LEU   A 1 308 ? 23.701  -3.028  22.891  1.00 16.43 ? 320 LEU   A O   1 
ATOM   2306 C  CB  . LEU   A 1 308 ? 24.944  -1.288  25.262  1.00 15.93 ? 320 LEU   A CB  1 
ATOM   2307 C  CG  . LEU   A 1 308 ? 26.289  -1.425  24.552  1.00 18.00 ? 320 LEU   A CG  1 
ATOM   2308 C  CD1 . LEU   A 1 308 ? 26.716  -0.094  24.000  1.00 22.73 ? 320 LEU   A CD1 1 
ATOM   2309 C  CD2 . LEU   A 1 308 ? 27.330  -1.935  25.566  1.00 16.47 ? 320 LEU   A CD2 1 
ATOM   2310 N  N   . TRP   A 1 309 ? 22.088  -1.685  23.764  1.00 13.00 ? 321 TRP   A N   1 
ATOM   2311 C  CA  . TRP   A 1 309 ? 21.239  -1.599  22.574  1.00 15.00 ? 321 TRP   A CA  1 
ATOM   2312 C  C   . TRP   A 1 309 ? 20.630  -2.947  22.227  1.00 18.47 ? 321 TRP   A C   1 
ATOM   2313 O  O   . TRP   A 1 309 ? 20.269  -3.204  21.072  1.00 16.78 ? 321 TRP   A O   1 
ATOM   2314 C  CB  . TRP   A 1 309 ? 21.988  -1.015  21.367  1.00 16.17 ? 321 TRP   A CB  1 
ATOM   2315 C  CG  . TRP   A 1 309 ? 21.126  -0.054  20.600  1.00 13.99 ? 321 TRP   A CG  1 
ATOM   2316 C  CD1 . TRP   A 1 309 ? 19.816  0.237   20.847  1.00 13.52 ? 321 TRP   A CD1 1 
ATOM   2317 C  CD2 . TRP   A 1 309 ? 21.501  0.728   19.453  1.00 15.41 ? 321 TRP   A CD2 1 
ATOM   2318 N  NE1 . TRP   A 1 309 ? 19.358  1.166   19.950  1.00 12.73 ? 321 TRP   A NE1 1 
ATOM   2319 C  CE2 . TRP   A 1 309 ? 20.364  1.475   19.071  1.00 11.29 ? 321 TRP   A CE2 1 
ATOM   2320 C  CE3 . TRP   A 1 309 ? 22.689  0.887   18.731  1.00 15.84 ? 321 TRP   A CE3 1 
ATOM   2321 C  CZ2 . TRP   A 1 309 ? 20.382  2.371   18.002  1.00 12.81 ? 321 TRP   A CZ2 1 
ATOM   2322 C  CZ3 . TRP   A 1 309 ? 22.700  1.767   17.655  1.00 17.31 ? 321 TRP   A CZ3 1 
ATOM   2323 C  CH2 . TRP   A 1 309 ? 21.547  2.498   17.302  1.00 13.68 ? 321 TRP   A CH2 1 
ATOM   2324 N  N   . HIS   A 1 310 ? 20.538  -3.810  23.233  1.00 17.79 ? 322 HIS   A N   1 
ATOM   2325 C  CA  . HIS   A 1 310 ? 19.763  -5.027  23.193  1.00 17.79 ? 322 HIS   A CA  1 
ATOM   2326 C  C   . HIS   A 1 310 ? 18.293  -4.671  23.343  1.00 16.63 ? 322 HIS   A C   1 
ATOM   2327 O  O   . HIS   A 1 310 ? 17.927  -3.507  23.521  1.00 18.60 ? 322 HIS   A O   1 
ATOM   2328 C  CB  . HIS   A 1 310 ? 20.191  -5.938  24.330  1.00 17.18 ? 322 HIS   A CB  1 
ATOM   2329 C  CG  . HIS   A 1 310 ? 20.049  -5.286  25.664  1.00 19.64 ? 322 HIS   A CG  1 
ATOM   2330 N  ND1 . HIS   A 1 310 ? 20.877  -4.263  26.080  1.00 15.71 ? 322 HIS   A ND1 1 
ATOM   2331 C  CD2 . HIS   A 1 310 ? 19.153  -5.476  26.662  1.00 18.63 ? 322 HIS   A CD2 1 
ATOM   2332 C  CE1 . HIS   A 1 310 ? 20.507  -3.866  27.285  1.00 16.78 ? 322 HIS   A CE1 1 
ATOM   2333 N  NE2 . HIS   A 1 310 ? 19.461  -4.581  27.658  1.00 14.78 ? 322 HIS   A NE2 1 
ATOM   2334 N  N   . THR   A 1 311 ? 17.444  -5.690  23.331  1.00 15.17 ? 323 THR   A N   1 
ATOM   2335 C  CA  . THR   A 1 311 ? 16.039  -5.527  23.681  1.00 18.84 ? 323 THR   A CA  1 
ATOM   2336 C  C   . THR   A 1 311 ? 15.680  -6.511  24.781  1.00 20.74 ? 323 THR   A C   1 
ATOM   2337 O  O   . THR   A 1 311 ? 16.337  -7.544  24.954  1.00 17.46 ? 323 THR   A O   1 
ATOM   2338 C  CB  . THR   A 1 311 ? 15.118  -5.762  22.491  1.00 16.51 ? 323 THR   A CB  1 
ATOM   2339 O  OG1 . THR   A 1 311 ? 15.314  -7.096  22.005  1.00 16.16 ? 323 THR   A OG1 1 
ATOM   2340 C  CG2 . THR   A 1 311 ? 15.398  -4.750  21.389  1.00 15.15 ? 323 THR   A CG2 1 
ATOM   2341 N  N   . ALA   A 1 312 ? 14.618  -6.173  25.526  1.00 19.65 ? 324 ALA   A N   1 
ATOM   2342 C  CA  . ALA   A 1 312 ? 14.072  -7.030  26.565  1.00 18.61 ? 324 ALA   A CA  1 
ATOM   2343 C  C   . ALA   A 1 312 ? 12.556  -7.082  26.469  1.00 19.79 ? 324 ALA   A C   1 
ATOM   2344 O  O   . ALA   A 1 312 ? 11.902  -6.053  26.285  1.00 18.49 ? 324 ALA   A O   1 
ATOM   2345 C  CB  . ALA   A 1 312 ? 14.470  -6.547  27.977  1.00 19.51 ? 324 ALA   A CB  1 
ATOM   2346 N  N   . CYS   A 1 313 ? 12.011  -8.287  26.604  1.00 18.94 ? 325 CYS   A N   1 
ATOM   2347 C  CA  . CYS   A 1 313 ? 10.575  -8.530  26.651  1.00 18.77 ? 325 CYS   A CA  1 
ATOM   2348 C  C   . CYS   A 1 313 ? 10.250  -9.468  27.806  1.00 21.95 ? 325 CYS   A C   1 
ATOM   2349 O  O   . CYS   A 1 313 ? 10.957  -10.456 28.027  1.00 20.92 ? 325 CYS   A O   1 
ATOM   2350 C  CB  . CYS   A 1 313 ? 10.054  -9.168  25.350  1.00 20.92 ? 325 CYS   A CB  1 
ATOM   2351 S  SG  . CYS   A 1 313 ? 10.254  -8.181  23.860  1.00 22.12 ? 325 CYS   A SG  1 
ATOM   2352 N  N   . ALA   A 1 314 ? 9.174   -9.165  28.530  1.00 22.01 ? 326 ALA   A N   1 
ATOM   2353 C  CA  . ALA   A 1 314 ? 8.687   -10.045 29.583  1.00 23.08 ? 326 ALA   A CA  1 
ATOM   2354 C  C   . ALA   A 1 314 ? 7.746   -11.087 28.997  1.00 25.97 ? 326 ALA   A C   1 
ATOM   2355 O  O   . ALA   A 1 314 ? 6.930   -10.780 28.125  1.00 28.29 ? 326 ALA   A O   1 
ATOM   2356 C  CB  . ALA   A 1 314 ? 7.966   -9.248  30.673  1.00 23.26 ? 326 ALA   A CB  1 
ATOM   2357 N  N   . SER   A 1 315 ? 7.872   -12.320 29.469  1.00 26.95 ? 327 SER   A N   1 
ATOM   2358 C  CA  . SER   A 1 315 ? 6.992   -13.395 29.039  1.00 29.58 ? 327 SER   A CA  1 
ATOM   2359 C  C   . SER   A 1 315 ? 5.890   -13.606 30.067  1.00 34.28 ? 327 SER   A C   1 
ATOM   2360 O  O   . SER   A 1 315 ? 5.998   -13.194 31.227  1.00 28.65 ? 327 SER   A O   1 
ATOM   2361 C  CB  . SER   A 1 315 ? 7.763   -14.704 28.824  1.00 30.03 ? 327 SER   A CB  1 
ATOM   2362 O  OG  . SER   A 1 315 ? 8.104   -15.315 30.061  1.00 35.02 ? 327 SER   A OG  1 
ATOM   2363 N  N   . ASP   A 1 316 ? 4.817   -14.266 29.616  1.00 30.81 ? 328 ASP   A N   1 
ATOM   2364 C  CA  . ASP   A 1 316 ? 3.764   -14.703 30.520  1.00 35.49 ? 328 ASP   A CA  1 
ATOM   2365 C  C   . ASP   A 1 316 ? 4.295   -15.630 31.603  1.00 37.85 ? 328 ASP   A C   1 
ATOM   2366 O  O   . ASP   A 1 316 ? 3.648   -15.778 32.648  1.00 37.49 ? 328 ASP   A O   1 
ATOM   2367 C  CB  . ASP   A 1 316 ? 2.663   -15.431 29.746  1.00 35.08 ? 328 ASP   A CB  1 
ATOM   2368 C  CG  . ASP   A 1 316 ? 1.645   -14.490 29.130  1.00 36.58 ? 328 ASP   A CG  1 
ATOM   2369 O  OD1 . ASP   A 1 316 ? 1.829   -13.258 29.197  1.00 35.17 ? 328 ASP   A OD1 1 
ATOM   2370 O  OD2 . ASP   A 1 316 ? 0.643   -15.000 28.582  1.00 37.86 ? 328 ASP   A OD2 1 
ATOM   2371 N  N   . GLU   A 1 317 ? 5.452   -16.258 31.378  1.00 34.87 ? 329 GLU   A N   1 
ATOM   2372 C  CA  . GLU   A 1 317 ? 5.991   -17.269 32.277  1.00 38.71 ? 329 GLU   A CA  1 
ATOM   2373 C  C   . GLU   A 1 317 ? 7.071   -16.725 33.214  1.00 35.95 ? 329 GLU   A C   1 
ATOM   2374 O  O   . GLU   A 1 317 ? 7.952   -17.477 33.641  1.00 35.21 ? 329 GLU   A O   1 
ATOM   2375 C  CB  . GLU   A 1 317 ? 6.525   -18.448 31.466  1.00 38.81 ? 329 GLU   A CB  1 
ATOM   2376 C  CG  . GLU   A 1 317 ? 5.461   -19.093 30.602  1.00 44.04 ? 329 GLU   A CG  1 
ATOM   2377 C  CD  . GLU   A 1 317 ? 5.628   -20.593 30.489  1.00 48.67 ? 329 GLU   A CD  1 
ATOM   2378 O  OE1 . GLU   A 1 317 ? 6.511   -21.049 29.722  1.00 43.70 ? 329 GLU   A OE1 1 
ATOM   2379 O  OE2 . GLU   A 1 317 ? 4.873   -21.314 31.178  1.00 49.81 ? 329 GLU   A OE2 1 
ATOM   2380 N  N   . GLY   A 1 318 ? 7.016   -15.435 33.547  1.00 33.36 ? 330 GLY   A N   1 
ATOM   2381 C  CA  . GLY   A 1 318 ? 7.841   -14.869 34.598  1.00 38.01 ? 330 GLY   A CA  1 
ATOM   2382 C  C   . GLY   A 1 318 ? 9.248   -14.478 34.199  1.00 39.09 ? 330 GLY   A C   1 
ATOM   2383 O  O   . GLY   A 1 318 ? 9.981   -13.933 35.035  1.00 38.57 ? 330 GLY   A O   1 
ATOM   2384 N  N   . GLU   A 1 319 ? 9.639   -14.712 32.954  1.00 29.94 ? 331 GLU   A N   1 
ATOM   2385 C  CA  . GLU   A 1 319 ? 10.991  -14.471 32.482  1.00 32.52 ? 331 GLU   A CA  1 
ATOM   2386 C  C   . GLU   A 1 319 ? 11.087  -13.118 31.778  1.00 30.22 ? 331 GLU   A C   1 
ATOM   2387 O  O   . GLU   A 1 319 ? 10.089  -12.546 31.337  1.00 23.09 ? 331 GLU   A O   1 
ATOM   2388 C  CB  . GLU   A 1 319 ? 11.425  -15.600 31.537  1.00 32.04 ? 331 GLU   A CB  1 
ATOM   2389 C  CG  . GLU   A 1 319 ? 11.308  -16.991 32.165  1.00 36.65 ? 331 GLU   A CG  1 
ATOM   2390 C  CD  . GLU   A 1 319 ? 11.499  -18.143 31.174  1.00 37.11 ? 331 GLU   A CD  1 
ATOM   2391 O  OE1 . GLU   A 1 319 ? 11.649  -17.891 29.962  1.00 36.97 ? 331 GLU   A OE1 1 
ATOM   2392 O  OE2 . GLU   A 1 319 ? 11.501  -19.313 31.620  1.00 41.29 ? 331 GLU   A OE2 1 
ATOM   2393 N  N   . VAL   A 1 320 ? 12.309  -12.596 31.703  1.00 26.67 ? 332 VAL   A N   1 
ATOM   2394 C  CA  . VAL   A 1 320 ? 12.622  -11.465 30.835  1.00 25.58 ? 332 VAL   A CA  1 
ATOM   2395 C  C   . VAL   A 1 320 ? 13.597  -11.960 29.777  1.00 24.72 ? 332 VAL   A C   1 
ATOM   2396 O  O   . VAL   A 1 320 ? 14.678  -12.475 30.103  1.00 19.66 ? 332 VAL   A O   1 
ATOM   2397 C  CB  . VAL   A 1 320 ? 13.198  -10.266 31.604  1.00 24.44 ? 332 VAL   A CB  1 
ATOM   2398 C  CG1 . VAL   A 1 320 ? 13.683  -9.189  30.626  1.00 19.70 ? 332 VAL   A CG1 1 
ATOM   2399 C  CG2 . VAL   A 1 320 ? 12.136  -9.687  32.533  1.00 21.73 ? 332 VAL   A CG2 1 
ATOM   2400 N  N   . ILE   A 1 321 ? 13.217  -11.797 28.519  1.00 21.09 ? 333 ILE   A N   1 
ATOM   2401 C  CA  . ILE   A 1 321 ? 13.953  -12.341 27.388  1.00 23.56 ? 333 ILE   A CA  1 
ATOM   2402 C  C   . ILE   A 1 321 ? 14.729  -11.197 26.761  1.00 22.51 ? 333 ILE   A C   1 
ATOM   2403 O  O   . ILE   A 1 321 ? 14.136  -10.257 26.228  1.00 24.87 ? 333 ILE   A O   1 
ATOM   2404 C  CB  . ILE   A 1 321 ? 13.016  -12.994 26.364  1.00 22.53 ? 333 ILE   A CB  1 
ATOM   2405 C  CG1 . ILE   A 1 321 ? 12.186  -14.110 27.012  1.00 25.16 ? 333 ILE   A CG1 1 
ATOM   2406 C  CG2 . ILE   A 1 321 ? 13.807  -13.489 25.151  1.00 24.14 ? 333 ILE   A CG2 1 
ATOM   2407 C  CD1 . ILE   A 1 321 ? 13.003  -15.193 27.685  1.00 25.68 ? 333 ILE   A CD1 1 
ATOM   2408 N  N   . VAL   A 1 322 ? 16.052  -11.289 26.804  1.00 19.34 ? 334 VAL   A N   1 
ATOM   2409 C  CA  . VAL   A 1 322 ? 16.933  -10.287 26.222  1.00 20.77 ? 334 VAL   A CA  1 
ATOM   2410 C  C   . VAL   A 1 322 ? 17.519  -10.873 24.950  1.00 23.17 ? 334 VAL   A C   1 
ATOM   2411 O  O   . VAL   A 1 322 ? 17.920  -12.043 24.926  1.00 24.95 ? 334 VAL   A O   1 
ATOM   2412 C  CB  . VAL   A 1 322 ? 18.029  -9.867  27.216  1.00 19.81 ? 334 VAL   A CB  1 
ATOM   2413 C  CG1 . VAL   A 1 322 ? 19.213  -9.212  26.497  1.00 19.51 ? 334 VAL   A CG1 1 
ATOM   2414 C  CG2 . VAL   A 1 322 ? 17.449  -8.928  28.257  1.00 20.54 ? 334 VAL   A CG2 1 
ATOM   2415 N  N   . PHE   A 1 323 ? 17.517  -10.086 23.879  1.00 20.16 ? 335 PHE   A N   1 
ATOM   2416 C  CA  . PHE   A 1 323 ? 18.053  -10.522 22.603  1.00 20.51 ? 335 PHE   A CA  1 
ATOM   2417 C  C   . PHE   A 1 323 ? 18.902  -9.418  21.992  1.00 21.95 ? 335 PHE   A C   1 
ATOM   2418 O  O   . PHE   A 1 323 ? 18.639  -8.229  22.197  1.00 20.41 ? 335 PHE   A O   1 
ATOM   2419 C  CB  . PHE   A 1 323 ? 16.947  -10.900 21.617  1.00 19.38 ? 335 PHE   A CB  1 
ATOM   2420 C  CG  . PHE   A 1 323 ? 17.460  -11.240 20.250  1.00 21.82 ? 335 PHE   A CG  1 
ATOM   2421 C  CD1 . PHE   A 1 323 ? 18.049  -12.468 20.003  1.00 21.48 ? 335 PHE   A CD1 1 
ATOM   2422 C  CD2 . PHE   A 1 323 ? 17.387  -10.317 19.222  1.00 18.56 ? 335 PHE   A CD2 1 
ATOM   2423 C  CE1 . PHE   A 1 323 ? 18.542  -12.775 18.750  1.00 23.59 ? 335 PHE   A CE1 1 
ATOM   2424 C  CE2 . PHE   A 1 323 ? 17.873  -10.625 17.965  1.00 24.04 ? 335 PHE   A CE2 1 
ATOM   2425 C  CZ  . PHE   A 1 323 ? 18.448  -11.855 17.733  1.00 23.98 ? 335 PHE   A CZ  1 
ATOM   2426 N  N   . GLY   A 1 324 ? 19.930  -9.830  21.234  1.00 21.13 ? 336 GLY   A N   1 
ATOM   2427 C  CA  . GLY   A 1 324 ? 20.719  -8.913  20.449  1.00 23.15 ? 336 GLY   A CA  1 
ATOM   2428 C  C   . GLY   A 1 324 ? 21.547  -7.977  21.310  1.00 19.17 ? 336 GLY   A C   1 
ATOM   2429 O  O   . GLY   A 1 324 ? 21.844  -8.240  22.481  1.00 17.80 ? 336 GLY   A O   1 
ATOM   2430 N  N   . GLY   A 1 325 ? 21.907  -6.854  20.713  1.00 17.98 ? 337 GLY   A N   1 
ATOM   2431 C  CA  . GLY   A 1 325 ? 22.741  -5.885  21.393  1.00 18.26 ? 337 GLY   A CA  1 
ATOM   2432 C  C   . GLY   A 1 325 ? 24.213  -6.179  21.189  1.00 18.04 ? 337 GLY   A C   1 
ATOM   2433 O  O   . GLY   A 1 325 ? 24.601  -7.148  20.538  1.00 19.89 ? 337 GLY   A O   1 
ATOM   2434 N  N   . CYS   A 1 326 ? 25.050  -5.319  21.774  1.00 15.74 ? 338 CYS   A N   1 
ATOM   2435 C  CA  . CYS   A 1 326 ? 26.497  -5.361  21.580  1.00 17.75 ? 338 CYS   A CA  1 
ATOM   2436 C  C   . CYS   A 1 326 ? 27.199  -5.570  22.914  1.00 21.88 ? 338 CYS   A C   1 
ATOM   2437 O  O   . CYS   A 1 326 ? 26.789  -5.002  23.930  1.00 17.52 ? 338 CYS   A O   1 
ATOM   2438 C  CB  . CYS   A 1 326 ? 26.996  -4.070  20.930  1.00 18.12 ? 338 CYS   A CB  1 
ATOM   2439 S  SG  . CYS   A 1 326 ? 28.685  -4.142  20.346  1.00 17.48 ? 338 CYS   A SG  1 
ATOM   2440 N  N   . ALA   A 1 327 ? 28.257  -6.389  22.910  1.00 15.85 ? 339 ALA   A N   1 
ATOM   2441 C  CA  . ALA   A 1 327 ? 28.954  -6.754  24.138  1.00 17.80 ? 339 ALA   A CA  1 
ATOM   2442 C  C   . ALA   A 1 327 ? 30.077  -5.787  24.503  1.00 19.05 ? 339 ALA   A C   1 
ATOM   2443 O  O   . ALA   A 1 327 ? 30.620  -5.880  25.617  1.00 21.53 ? 339 ALA   A O   1 
ATOM   2444 C  CB  . ALA   A 1 327 ? 29.513  -8.178  24.037  1.00 19.36 ? 339 ALA   A CB  1 
ATOM   2445 N  N   . ASN   A 1 328 ? 30.413  -4.849  23.624  1.00 16.59 ? 340 ASN   A N   1 
ATOM   2446 C  CA  . ASN   A 1 328 ? 31.428  -3.846  23.920  1.00 17.79 ? 340 ASN   A CA  1 
ATOM   2447 C  C   . ASN   A 1 328 ? 30.947  -2.490  23.414  1.00 17.93 ? 340 ASN   A C   1 
ATOM   2448 O  O   . ASN   A 1 328 ? 29.753  -2.273  23.175  1.00 16.67 ? 340 ASN   A O   1 
ATOM   2449 C  CB  . ASN   A 1 328 ? 32.789  -4.243  23.323  1.00 15.97 ? 340 ASN   A CB  1 
ATOM   2450 C  CG  . ASN   A 1 328 ? 32.744  -4.387  21.820  1.00 19.15 ? 340 ASN   A CG  1 
ATOM   2451 O  OD1 . ASN   A 1 328 ? 31.724  -4.115  21.178  1.00 19.79 ? 340 ASN   A OD1 1 
ATOM   2452 N  ND2 . ASN   A 1 328 ? 33.850  -4.826  21.248  1.00 19.69 ? 340 ASN   A ND2 1 
ATOM   2453 N  N   . ASN   A 1 329 ? 31.887  -1.553  23.282  1.00 16.66 ? 341 ASN   A N   1 
ATOM   2454 C  CA  . ASN   A 1 329 ? 31.586  -0.198  22.827  1.00 17.88 ? 341 ASN   A CA  1 
ATOM   2455 C  C   . ASN   A 1 329 ? 31.284  -0.252  21.339  1.00 17.44 ? 341 ASN   A C   1 
ATOM   2456 O  O   . ASN   A 1 329 ? 32.196  -0.314  20.520  1.00 14.75 ? 341 ASN   A O   1 
ATOM   2457 C  CB  . ASN   A 1 329 ? 32.766  0.729   23.113  1.00 16.21 ? 341 ASN   A CB  1 
ATOM   2458 C  CG  . ASN   A 1 329 ? 32.493  2.171   22.719  1.00 15.45 ? 341 ASN   A CG  1 
ATOM   2459 O  OD1 . ASN   A 1 329 ? 31.499  2.483   22.059  1.00 16.77 ? 341 ASN   A OD1 1 
ATOM   2460 N  ND2 . ASN   A 1 329 ? 33.376  3.062   23.125  1.00 16.52 ? 341 ASN   A ND2 1 
ATOM   2461 N  N   . LEU   A 1 330 ? 29.992  -0.218  20.984  1.00 13.70 ? 342 LEU   A N   1 
ATOM   2462 C  CA  . LEU   A 1 330 ? 29.608  -0.302  19.576  1.00 15.51 ? 342 LEU   A CA  1 
ATOM   2463 C  C   . LEU   A 1 330 ? 30.059  0.910   18.777  1.00 14.09 ? 342 LEU   A C   1 
ATOM   2464 O  O   . LEU   A 1 330 ? 30.063  0.860   17.539  1.00 17.73 ? 342 LEU   A O   1 
ATOM   2465 C  CB  . LEU   A 1 330 ? 28.090  -0.481  19.471  1.00 17.67 ? 342 LEU   A CB  1 
ATOM   2466 C  CG  . LEU   A 1 330 ? 27.176  0.551   20.145  1.00 20.98 ? 342 LEU   A CG  1 
ATOM   2467 C  CD1 . LEU   A 1 330 ? 26.954  1.761   19.257  1.00 22.60 ? 342 LEU   A CD1 1 
ATOM   2468 C  CD2 . LEU   A 1 330 ? 25.832  -0.071  20.537  1.00 16.51 ? 342 LEU   A CD2 1 
ATOM   2469 N  N   . LEU   A 1 331 ? 30.424  2.001   19.453  1.00 15.91 ? 343 LEU   A N   1 
ATOM   2470 C  CA  . LEU   A 1 331 ? 30.888  3.191   18.761  1.00 16.02 ? 343 LEU   A CA  1 
ATOM   2471 C  C   . LEU   A 1 331 ? 32.236  2.966   18.087  1.00 17.17 ? 343 LEU   A C   1 
ATOM   2472 O  O   . LEU   A 1 331 ? 32.607  3.745   17.213  1.00 18.00 ? 343 LEU   A O   1 
ATOM   2473 C  CB  . LEU   A 1 331 ? 30.960  4.372   19.730  1.00 16.90 ? 343 LEU   A CB  1 
ATOM   2474 C  CG  . LEU   A 1 331 ? 29.666  4.684   20.492  1.00 15.83 ? 343 LEU   A CG  1 
ATOM   2475 C  CD1 . LEU   A 1 331 ? 29.906  5.695   21.605  1.00 19.63 ? 343 LEU   A CD1 1 
ATOM   2476 C  CD2 . LEU   A 1 331 ? 28.664  5.219   19.502  1.00 19.10 ? 343 LEU   A CD2 1 
ATOM   2477 N  N   . VAL   A 1 332 ? 32.977  1.939   18.490  1.00 16.96 ? 344 VAL   A N   1 
ATOM   2478 C  CA  . VAL   A 1 332 ? 34.169  1.508   17.740  1.00 18.12 ? 344 VAL   A CA  1 
ATOM   2479 C  C   . VAL   A 1 332 ? 33.670  0.439   16.777  1.00 17.71 ? 344 VAL   A C   1 
ATOM   2480 O  O   . VAL   A 1 332 ? 33.760  -0.766  17.016  1.00 16.54 ? 344 VAL   A O   1 
ATOM   2481 C  CB  . VAL   A 1 332 ? 35.286  1.009   18.660  1.00 19.73 ? 344 VAL   A CB  1 
ATOM   2482 C  CG1 . VAL   A 1 332 ? 36.502  0.636   17.826  1.00 20.23 ? 344 VAL   A CG1 1 
ATOM   2483 C  CG2 . VAL   A 1 332 ? 35.643  2.068   19.682  1.00 20.53 ? 344 VAL   A CG2 1 
ATOM   2484 N  N   . HIS   A 1 333 ? 33.123  0.899   15.652  1.00 17.31 ? 345 HIS   A N   1 
ATOM   2485 C  CA  . HIS   A 1 333 ? 32.276  0.026   14.845  1.00 21.94 ? 345 HIS   A CA  1 
ATOM   2486 C  C   . HIS   A 1 333 ? 33.066  -1.155  14.279  1.00 23.11 ? 345 HIS   A C   1 
ATOM   2487 O  O   . HIS   A 1 333 ? 32.540  -2.270  14.187  1.00 23.08 ? 345 HIS   A O   1 
ATOM   2488 C  CB  . HIS   A 1 333 ? 31.601  0.851   13.743  1.00 23.18 ? 345 HIS   A CB  1 
ATOM   2489 C  CG  . HIS   A 1 333 ? 30.690  0.060   12.858  1.00 22.07 ? 345 HIS   A CG  1 
ATOM   2490 N  ND1 . HIS   A 1 333 ? 29.459  -0.408  13.270  1.00 18.12 ? 345 HIS   A ND1 1 
ATOM   2491 C  CD2 . HIS   A 1 333 ? 30.832  -0.336  11.570  1.00 24.44 ? 345 HIS   A CD2 1 
ATOM   2492 C  CE1 . HIS   A 1 333 ? 28.884  -1.060  12.273  1.00 27.26 ? 345 HIS   A CE1 1 
ATOM   2493 N  NE2 . HIS   A 1 333 ? 29.699  -1.036  11.233  1.00 28.02 ? 345 HIS   A NE2 1 
ATOM   2494 N  N   . HIS   A 1 334 ? 34.346  -0.949  13.950  1.00 19.25 ? 346 HIS   A N   1 
ATOM   2495 C  CA  . HIS   A 1 334 ? 35.120  -2.037  13.361  1.00 20.20 ? 346 HIS   A CA  1 
ATOM   2496 C  C   . HIS   A 1 334 ? 35.503  -3.120  14.364  1.00 23.34 ? 346 HIS   A C   1 
ATOM   2497 O  O   . HIS   A 1 334 ? 35.915  -4.203  13.937  1.00 27.98 ? 346 HIS   A O   1 
ATOM   2498 C  CB  . HIS   A 1 334 ? 36.382  -1.497  12.666  1.00 24.24 ? 346 HIS   A CB  1 
ATOM   2499 C  CG  . HIS   A 1 334 ? 37.373  -0.847  13.586  1.00 20.12 ? 346 HIS   A CG  1 
ATOM   2500 N  ND1 . HIS   A 1 334 ? 37.210  0.430   14.080  1.00 25.04 ? 346 HIS   A ND1 1 
ATOM   2501 C  CD2 . HIS   A 1 334 ? 38.564  -1.285  14.064  1.00 22.22 ? 346 HIS   A CD2 1 
ATOM   2502 C  CE1 . HIS   A 1 334 ? 38.249  0.745   14.836  1.00 22.06 ? 346 HIS   A CE1 1 
ATOM   2503 N  NE2 . HIS   A 1 334 ? 39.087  -0.277  14.839  1.00 21.94 ? 346 HIS   A NE2 1 
ATOM   2504 N  N   . ARG   A 1 335 ? 35.380  -2.868  15.672  1.00 20.30 ? 347 ARG   A N   1 
ATOM   2505 C  CA  . ARG   A 1 335 ? 35.618  -3.887  16.686  1.00 22.60 ? 347 ARG   A CA  1 
ATOM   2506 C  C   . ARG   A 1 335 ? 34.336  -4.360  17.375  1.00 22.32 ? 347 ARG   A C   1 
ATOM   2507 O  O   . ARG   A 1 335 ? 34.409  -5.214  18.266  1.00 20.07 ? 347 ARG   A O   1 
ATOM   2508 C  CB  . ARG   A 1 335 ? 36.615  -3.367  17.740  1.00 20.02 ? 347 ARG   A CB  1 
ATOM   2509 C  CG  . ARG   A 1 335 ? 37.869  -2.694  17.158  1.00 22.94 ? 347 ARG   A CG  1 
ATOM   2510 C  CD  . ARG   A 1 335 ? 39.074  -2.709  18.112  1.00 25.81 ? 347 ARG   A CD  1 
ATOM   2511 N  NE  . ARG   A 1 335 ? 38.830  -2.004  19.370  1.00 25.65 ? 347 ARG   A NE  1 
ATOM   2512 C  CZ  . ARG   A 1 335 ? 39.229  -0.766  19.633  1.00 25.34 ? 347 ARG   A CZ  1 
ATOM   2513 N  NH1 . ARG   A 1 335 ? 39.915  -0.056  18.748  1.00 23.41 ? 347 ARG   A NH1 1 
ATOM   2514 N  NH2 . ARG   A 1 335 ? 38.928  -0.223  20.812  1.00 23.94 ? 347 ARG   A NH2 1 
ATOM   2515 N  N   . ALA   A 1 336 ? 33.167  -3.856  16.973  1.00 20.83 ? 348 ALA   A N   1 
ATOM   2516 C  CA  . ALA   A 1 336 ? 31.944  -4.101  17.731  1.00 21.53 ? 348 ALA   A CA  1 
ATOM   2517 C  C   . ALA   A 1 336 ? 31.570  -5.579  17.724  1.00 20.97 ? 348 ALA   A C   1 
ATOM   2518 O  O   . ALA   A 1 336 ? 31.689  -6.263  16.706  1.00 24.29 ? 348 ALA   A O   1 
ATOM   2519 C  CB  . ALA   A 1 336 ? 30.792  -3.271  17.172  1.00 20.81 ? 348 ALA   A CB  1 
ATOM   2520 N  N   . ALA   A 1 337 ? 31.133  -6.070  18.880  1.00 20.26 ? 349 ALA   A N   1 
ATOM   2521 C  CA  . ALA   A 1 337 ? 30.758  -7.469  19.074  1.00 20.13 ? 349 ALA   A CA  1 
ATOM   2522 C  C   . ALA   A 1 337 ? 29.241  -7.518  19.239  1.00 20.14 ? 349 ALA   A C   1 
ATOM   2523 O  O   . ALA   A 1 337 ? 28.711  -7.534  20.356  1.00 21.56 ? 349 ALA   A O   1 
ATOM   2524 C  CB  . ALA   A 1 337 ? 31.465  -8.065  20.275  1.00 20.75 ? 349 ALA   A CB  1 
ATOM   2525 N  N   . HIS   A 1 338 ? 28.544  -7.539  18.118  1.00 18.85 ? 350 HIS   A N   1 
ATOM   2526 C  CA  . HIS   A 1 338 ? 27.097  -7.667  18.147  1.00 23.00 ? 350 HIS   A CA  1 
ATOM   2527 C  C   . HIS   A 1 338 ? 26.726  -9.132  18.336  1.00 23.96 ? 350 HIS   A C   1 
ATOM   2528 O  O   . HIS   A 1 338 ? 27.432  -10.038 17.879  1.00 22.86 ? 350 HIS   A O   1 
ATOM   2529 C  CB  . HIS   A 1 338 ? 26.479  -7.109  16.866  1.00 21.32 ? 350 HIS   A CB  1 
ATOM   2530 C  CG  . HIS   A 1 338 ? 26.818  -5.671  16.614  1.00 20.81 ? 350 HIS   A CG  1 
ATOM   2531 N  ND1 . HIS   A 1 338 ? 26.126  -4.631  17.196  1.00 19.18 ? 350 HIS   A ND1 1 
ATOM   2532 C  CD2 . HIS   A 1 338 ? 27.782  -5.101  15.851  1.00 22.84 ? 350 HIS   A CD2 1 
ATOM   2533 C  CE1 . HIS   A 1 338 ? 26.643  -3.482  16.796  1.00 19.20 ? 350 HIS   A CE1 1 
ATOM   2534 N  NE2 . HIS   A 1 338 ? 27.649  -3.740  15.978  1.00 20.59 ? 350 HIS   A NE2 1 
ATOM   2535 N  N   . SER   A 1 339 ? 25.610  -9.354  19.025  1.00 20.73 ? 351 SER   A N   1 
ATOM   2536 C  CA  . SER   A 1 339 ? 25.229  -10.660 19.539  1.00 20.82 ? 351 SER   A CA  1 
ATOM   2537 C  C   . SER   A 1 339 ? 23.928  -11.136 18.917  1.00 20.25 ? 351 SER   A C   1 
ATOM   2538 O  O   . SER   A 1 339 ? 23.055  -10.338 18.578  1.00 18.02 ? 351 SER   A O   1 
ATOM   2539 C  CB  . SER   A 1 339 ? 25.055  -10.618 21.069  1.00 19.91 ? 351 SER   A CB  1 
ATOM   2540 O  OG  . SER   A 1 339 ? 24.735  -11.901 21.581  1.00 21.29 ? 351 SER   A OG  1 
ATOM   2541 N  N   . ASN   A 1 340 ? 23.793  -12.452 18.798  1.00 22.82 ? 352 ASN   A N   1 
ATOM   2542 C  CA  . ASN   A 1 340 ? 22.508  -13.064 18.492  1.00 24.93 ? 352 ASN   A CA  1 
ATOM   2543 C  C   . ASN   A 1 340 ? 21.986  -13.903 19.652  1.00 26.52 ? 352 ASN   A C   1 
ATOM   2544 O  O   . ASN   A 1 340 ? 21.070  -14.708 19.462  1.00 27.60 ? 352 ASN   A O   1 
ATOM   2545 C  CB  . ASN   A 1 340 ? 22.614  -13.902 17.215  1.00 27.55 ? 352 ASN   A CB  1 
ATOM   2546 C  CG  . ASN   A 1 340 ? 23.403  -15.188 17.408  1.00 28.68 ? 352 ASN   A CG  1 
ATOM   2547 O  OD1 . ASN   A 1 340 ? 24.099  -15.379 18.408  1.00 29.25 ? 352 ASN   A OD1 1 
ATOM   2548 N  ND2 . ASN   A 1 340 ? 23.299  -16.081 16.432  1.00 36.50 ? 352 ASN   A ND2 1 
ATOM   2549 N  N   . GLU   A 1 341 ? 22.561  -13.742 20.843  1.00 25.70 ? 353 GLU   A N   1 
ATOM   2550 C  CA  . GLU   A 1 341 ? 22.222  -14.591 21.973  1.00 24.81 ? 353 GLU   A CA  1 
ATOM   2551 C  C   . GLU   A 1 341 ? 20.875  -14.207 22.573  1.00 24.50 ? 353 GLU   A C   1 
ATOM   2552 O  O   . GLU   A 1 341 ? 20.458  -13.045 22.535  1.00 23.69 ? 353 GLU   A O   1 
ATOM   2553 C  CB  . GLU   A 1 341 ? 23.290  -14.495 23.060  1.00 24.76 ? 353 GLU   A CB  1 
ATOM   2554 C  CG  . GLU   A 1 341 ? 24.686  -14.921 22.658  1.00 27.24 ? 353 GLU   A CG  1 
ATOM   2555 C  CD  . GLU   A 1 341 ? 25.520  -15.281 23.876  1.00 30.25 ? 353 GLU   A CD  1 
ATOM   2556 O  OE1 . GLU   A 1 341 ? 25.085  -16.166 24.642  1.00 33.15 ? 353 GLU   A OE1 1 
ATOM   2557 O  OE2 . GLU   A 1 341 ? 26.585  -14.666 24.079  1.00 33.97 ? 353 GLU   A OE2 1 
ATOM   2558 N  N   . ILE   A 1 342 ? 20.215  -15.208 23.149  1.00 27.54 ? 354 ILE   A N   1 
ATOM   2559 C  CA  . ILE   A 1 342 ? 19.062  -15.037 24.024  1.00 24.27 ? 354 ILE   A CA  1 
ATOM   2560 C  C   . ILE   A 1 342 ? 19.540  -15.224 25.453  1.00 27.74 ? 354 ILE   A C   1 
ATOM   2561 O  O   . ILE   A 1 342 ? 20.067  -16.287 25.809  1.00 27.00 ? 354 ILE   A O   1 
ATOM   2562 C  CB  . ILE   A 1 342 ? 17.945  -16.038 23.696  1.00 26.12 ? 354 ILE   A CB  1 
ATOM   2563 C  CG1 . ILE   A 1 342 ? 17.268  -15.647 22.391  1.00 24.59 ? 354 ILE   A CG1 1 
ATOM   2564 C  CG2 . ILE   A 1 342 ? 16.937  -16.121 24.834  1.00 29.49 ? 354 ILE   A CG2 1 
ATOM   2565 C  CD1 . ILE   A 1 342 ? 16.552  -14.322 22.457  1.00 26.33 ? 354 ILE   A CD1 1 
ATOM   2566 N  N   . LEU   A 1 343 ? 19.349  -14.200 26.270  1.00 24.40 ? 355 LEU   A N   1 
ATOM   2567 C  CA  . LEU   A 1 343 ? 19.601  -14.269 27.700  1.00 24.01 ? 355 LEU   A CA  1 
ATOM   2568 C  C   . LEU   A 1 343 ? 18.246  -14.322 28.395  1.00 24.43 ? 355 LEU   A C   1 
ATOM   2569 O  O   . LEU   A 1 343 ? 17.409  -13.434 28.198  1.00 23.31 ? 355 LEU   A O   1 
ATOM   2570 C  CB  . LEU   A 1 343 ? 20.417  -13.062 28.167  1.00 24.62 ? 355 LEU   A CB  1 
ATOM   2571 C  CG  . LEU   A 1 343 ? 21.857  -12.846 27.662  1.00 26.13 ? 355 LEU   A CG  1 
ATOM   2572 C  CD1 . LEU   A 1 343 ? 21.952  -12.691 26.145  1.00 27.20 ? 355 LEU   A CD1 1 
ATOM   2573 C  CD2 . LEU   A 1 343 ? 22.469  -11.626 28.342  1.00 24.94 ? 355 LEU   A CD2 1 
ATOM   2574 N  N   . ILE   A 1 344 ? 18.022  -15.354 29.204  1.00 27.68 ? 356 ILE   A N   1 
ATOM   2575 C  CA  . ILE   A 1 344 ? 16.753  -15.522 29.905  1.00 24.45 ? 356 ILE   A CA  1 
ATOM   2576 C  C   . ILE   A 1 344 ? 16.974  -15.211 31.374  1.00 25.45 ? 356 ILE   A C   1 
ATOM   2577 O  O   . ILE   A 1 344 ? 17.732  -15.910 32.060  1.00 28.49 ? 356 ILE   A O   1 
ATOM   2578 C  CB  . ILE   A 1 344 ? 16.177  -16.932 29.730  1.00 25.71 ? 356 ILE   A CB  1 
ATOM   2579 C  CG1 . ILE   A 1 344 ? 16.002  -17.266 28.254  1.00 23.19 ? 356 ILE   A CG1 1 
ATOM   2580 C  CG2 . ILE   A 1 344 ? 14.828  -17.046 30.435  1.00 27.52 ? 356 ILE   A CG2 1 
ATOM   2581 C  CD1 . ILE   A 1 344 ? 15.458  -18.656 28.027  1.00 24.04 ? 356 ILE   A CD1 1 
ATOM   2582 N  N   . PHE   A 1 345 ? 16.293  -14.179 31.859  1.00 23.83 ? 357 PHE   A N   1 
ATOM   2583 C  CA  . PHE   A 1 345 ? 16.312  -13.811 33.263  1.00 25.26 ? 357 PHE   A CA  1 
ATOM   2584 C  C   . PHE   A 1 345 ? 15.052  -14.339 33.933  1.00 30.01 ? 357 PHE   A C   1 
ATOM   2585 O  O   . PHE   A 1 345 ? 13.941  -14.062 33.479  1.00 30.17 ? 357 PHE   A O   1 
ATOM   2586 C  CB  . PHE   A 1 345 ? 16.409  -12.293 33.416  1.00 23.36 ? 357 PHE   A CB  1 
ATOM   2587 C  CG  . PHE   A 1 345 ? 17.699  -11.728 32.905  1.00 27.54 ? 357 PHE   A CG  1 
ATOM   2588 C  CD1 . PHE   A 1 345 ? 17.828  -11.372 31.576  1.00 23.54 ? 357 PHE   A CD1 1 
ATOM   2589 C  CD2 . PHE   A 1 345 ? 18.795  -11.579 33.745  1.00 26.89 ? 357 PHE   A CD2 1 
ATOM   2590 C  CE1 . PHE   A 1 345 ? 19.018  -10.860 31.085  1.00 23.08 ? 357 PHE   A CE1 1 
ATOM   2591 C  CE2 . PHE   A 1 345 ? 19.993  -11.061 33.262  1.00 23.67 ? 357 PHE   A CE2 1 
ATOM   2592 C  CZ  . PHE   A 1 345 ? 20.101  -10.698 31.922  1.00 22.27 ? 357 PHE   A CZ  1 
ATOM   2593 N  N   . SER   A 1 346 ? 15.226  -15.087 35.021  1.00 31.41 ? 358 SER   A N   1 
ATOM   2594 C  CA  . SER   A 1 346 ? 14.102  -15.682 35.737  1.00 33.96 ? 358 SER   A CA  1 
ATOM   2595 C  C   . SER   A 1 346 ? 13.805  -14.792 36.938  1.00 37.18 ? 358 SER   A C   1 
ATOM   2596 O  O   . SER   A 1 346 ? 14.314  -15.008 38.037  1.00 39.53 ? 358 SER   A O   1 
ATOM   2597 C  CB  . SER   A 1 346 ? 14.430  -17.113 36.137  1.00 38.83 ? 358 SER   A CB  1 
ATOM   2598 O  OG  . SER   A 1 346 ? 15.041  -17.795 35.051  1.00 34.88 ? 358 SER   A OG  1 
ATOM   2599 N  N   . VAL   A 1 347 ? 12.970  -13.775 36.718  1.00 40.14 ? 359 VAL   A N   1 
ATOM   2600 C  CA  . VAL   A 1 347 ? 12.698  -12.786 37.756  1.00 43.74 ? 359 VAL   A CA  1 
ATOM   2601 C  C   . VAL   A 1 347 ? 11.514  -13.171 38.637  1.00 48.68 ? 359 VAL   A C   1 
ATOM   2602 O  O   . VAL   A 1 347 ? 11.361  -12.610 39.733  1.00 54.06 ? 359 VAL   A O   1 
ATOM   2603 C  CB  . VAL   A 1 347 ? 12.466  -11.399 37.127  1.00 44.94 ? 359 VAL   A CB  1 
ATOM   2604 C  CG1 . VAL   A 1 347 ? 12.618  -10.291 38.172  1.00 35.85 ? 359 VAL   A CG1 1 
ATOM   2605 C  CG2 . VAL   A 1 347 ? 13.420  -11.180 35.951  1.00 32.75 ? 359 VAL   A CG2 1 
ATOM   2606 N  N   . GLN   A 1 348 ? 10.688  -14.120 38.209  1.00 46.50 ? 360 GLN   A N   1 
ATOM   2607 C  CA  . GLN   A 1 348 ? 9.551   -14.556 39.019  1.00 48.26 ? 360 GLN   A CA  1 
ATOM   2608 C  C   . GLN   A 1 348 ? 9.550   -16.070 39.198  1.00 48.42 ? 360 GLN   A C   1 
ATOM   2609 O  O   . GLN   A 1 348 ? 10.164  -16.594 40.128  1.00 50.49 ? 360 GLN   A O   1 
ATOM   2610 C  CB  . GLN   A 1 348 ? 8.235   -14.097 38.386  1.00 48.21 ? 360 GLN   A CB  1 
ATOM   2611 C  CG  . GLN   A 1 348 ? 8.047   -12.587 38.365  1.00 46.98 ? 360 GLN   A CG  1 
ATOM   2612 C  CD  . GLN   A 1 348 ? 7.587   -12.034 39.701  1.00 54.12 ? 360 GLN   A CD  1 
ATOM   2613 O  OE1 . GLN   A 1 348 ? 6.822   -12.678 40.424  1.00 53.98 ? 360 GLN   A OE1 1 
ATOM   2614 N  NE2 . GLN   A 1 348 ? 8.053   -10.833 40.037  1.00 49.37 ? 360 GLN   A NE2 1 
ATOM   2615 N  N   . LEU   B 1 14  ? 18.929  29.171  -14.289 1.00 47.11 ? 26  LEU   B N   1 
ATOM   2616 C  CA  . LEU   B 1 14  ? 17.969  28.749  -13.273 1.00 55.96 ? 26  LEU   B CA  1 
ATOM   2617 C  C   . LEU   B 1 14  ? 18.227  27.321  -12.784 1.00 58.42 ? 26  LEU   B C   1 
ATOM   2618 O  O   . LEU   B 1 14  ? 19.261  26.727  -13.102 1.00 56.92 ? 26  LEU   B O   1 
ATOM   2619 C  CB  . LEU   B 1 14  ? 16.546  28.878  -13.815 1.00 58.44 ? 26  LEU   B CB  1 
ATOM   2620 C  CG  . LEU   B 1 14  ? 15.969  30.286  -13.673 1.00 59.91 ? 26  LEU   B CG  1 
ATOM   2621 C  CD1 . LEU   B 1 14  ? 14.657  30.422  -14.434 1.00 64.22 ? 26  LEU   B CD1 1 
ATOM   2622 C  CD2 . LEU   B 1 14  ? 15.775  30.618  -12.201 1.00 65.51 ? 26  LEU   B CD2 1 
ATOM   2623 N  N   . ALA   B 1 15  ? 17.283  26.786  -12.005 1.00 62.71 ? 27  ALA   B N   1 
ATOM   2624 C  CA  . ALA   B 1 15  ? 17.453  25.475  -11.385 1.00 55.93 ? 27  ALA   B CA  1 
ATOM   2625 C  C   . ALA   B 1 15  ? 17.669  24.397  -12.440 1.00 49.68 ? 27  ALA   B C   1 
ATOM   2626 O  O   . ALA   B 1 15  ? 16.926  24.311  -13.423 1.00 47.28 ? 27  ALA   B O   1 
ATOM   2627 C  CB  . ALA   B 1 15  ? 16.236  25.137  -10.524 1.00 55.39 ? 27  ALA   B CB  1 
ATOM   2628 N  N   . CYS   B 1 16  ? 18.682  23.561  -12.219 1.00 43.76 ? 28  CYS   B N   1 
ATOM   2629 C  CA  . CYS   B 1 16  ? 19.125  22.585  -13.200 1.00 41.63 ? 28  CYS   B CA  1 
ATOM   2630 C  C   . CYS   B 1 16  ? 19.227  21.217  -12.535 1.00 37.39 ? 28  CYS   B C   1 
ATOM   2631 O  O   . CYS   B 1 16  ? 19.813  21.102  -11.444 1.00 33.21 ? 28  CYS   B O   1 
ATOM   2632 C  CB  . CYS   B 1 16  ? 20.477  23.004  -13.795 1.00 42.00 ? 28  CYS   B CB  1 
ATOM   2633 S  SG  . CYS   B 1 16  ? 20.842  22.314  -15.418 1.00 48.75 ? 28  CYS   B SG  1 
ATOM   2634 N  N   . PRO   B 1 17  ? 18.664  20.170  -13.133 1.00 33.55 ? 29  PRO   B N   1 
ATOM   2635 C  CA  . PRO   B 1 17  ? 18.771  18.837  -12.534 1.00 31.43 ? 29  PRO   B CA  1 
ATOM   2636 C  C   . PRO   B 1 17  ? 20.200  18.317  -12.578 1.00 30.11 ? 29  PRO   B C   1 
ATOM   2637 O  O   . PRO   B 1 17  ? 21.009  18.717  -13.419 1.00 27.96 ? 29  PRO   B O   1 
ATOM   2638 C  CB  . PRO   B 1 17  ? 17.842  17.985  -13.404 1.00 30.89 ? 29  PRO   B CB  1 
ATOM   2639 C  CG  . PRO   B 1 17  ? 17.875  18.671  -14.729 1.00 31.43 ? 29  PRO   B CG  1 
ATOM   2640 C  CD  . PRO   B 1 17  ? 17.949  20.139  -14.422 1.00 35.79 ? 29  PRO   B CD  1 
ATOM   2641 N  N   . ALA   B 1 18  ? 20.511  17.431  -11.638 1.00 25.69 ? 30  ALA   B N   1 
ATOM   2642 C  CA  . ALA   B 1 18  ? 21.825  16.803  -11.604 1.00 27.04 ? 30  ALA   B CA  1 
ATOM   2643 C  C   . ALA   B 1 18  ? 21.982  15.823  -12.765 1.00 24.78 ? 30  ALA   B C   1 
ATOM   2644 O  O   . ALA   B 1 18  ? 21.005  15.262  -13.268 1.00 28.06 ? 30  ALA   B O   1 
ATOM   2645 C  CB  . ALA   B 1 18  ? 22.041  16.079  -10.276 1.00 27.14 ? 30  ALA   B CB  1 
ATOM   2646 N  N   . GLU   B 1 19  ? 23.233  15.620  -13.183 1.00 25.34 ? 31  GLU   B N   1 
ATOM   2647 C  CA  . GLU   B 1 19  ? 23.530  14.665  -14.241 1.00 23.47 ? 31  GLU   B CA  1 
ATOM   2648 C  C   . GLU   B 1 19  ? 23.118  13.257  -13.818 1.00 20.73 ? 31  GLU   B C   1 
ATOM   2649 O  O   . GLU   B 1 19  ? 23.047  12.934  -12.630 1.00 23.94 ? 31  GLU   B O   1 
ATOM   2650 C  CB  . GLU   B 1 19  ? 25.020  14.709  -14.597 1.00 27.01 ? 31  GLU   B CB  1 
ATOM   2651 C  CG  . GLU   B 1 19  ? 25.960  14.038  -13.595 1.00 30.15 ? 31  GLU   B CG  1 
ATOM   2652 C  CD  . GLU   B 1 19  ? 26.443  14.982  -12.499 1.00 34.91 ? 31  GLU   B CD  1 
ATOM   2653 O  OE1 . GLU   B 1 19  ? 25.934  16.124  -12.421 1.00 35.80 ? 31  GLU   B OE1 1 
ATOM   2654 O  OE2 . GLU   B 1 19  ? 27.341  14.580  -11.719 1.00 36.25 ? 31  GLU   B OE2 1 
ATOM   2655 N  N   . ARG   B 1 20  ? 22.813  12.414  -14.803 1.00 20.73 ? 32  ARG   B N   1 
ATOM   2656 C  CA  . ARG   B 1 20  ? 22.357  11.063  -14.495 1.00 18.91 ? 32  ARG   B CA  1 
ATOM   2657 C  C   . ARG   B 1 20  ? 22.304  10.235  -15.770 1.00 18.49 ? 32  ARG   B C   1 
ATOM   2658 O  O   . ARG   B 1 20  ? 22.146  10.771  -16.870 1.00 20.53 ? 32  ARG   B O   1 
ATOM   2659 C  CB  . ARG   B 1 20  ? 20.973  11.068  -13.844 1.00 19.22 ? 32  ARG   B CB  1 
ATOM   2660 C  CG  . ARG   B 1 20  ? 19.876  11.587  -14.755 1.00 18.29 ? 32  ARG   B CG  1 
ATOM   2661 C  CD  . ARG   B 1 20  ? 18.646  11.996  -13.947 1.00 22.93 ? 32  ARG   B CD  1 
ATOM   2662 N  NE  . ARG   B 1 20  ? 18.903  13.190  -13.150 1.00 21.42 ? 32  ARG   B NE  1 
ATOM   2663 C  CZ  . ARG   B 1 20  ? 18.224  13.521  -12.058 1.00 22.83 ? 32  ARG   B CZ  1 
ATOM   2664 N  NH1 . ARG   B 1 20  ? 17.247  12.757  -11.594 1.00 18.20 ? 32  ARG   B NH1 1 
ATOM   2665 N  NH2 . ARG   B 1 20  ? 18.555  14.629  -11.397 1.00 26.06 ? 32  ARG   B NH2 1 
ATOM   2666 N  N   . SER   B 1 21  ? 22.413  8.914   -15.598 1.00 18.73 ? 33  SER   B N   1 
ATOM   2667 C  CA  . SER   B 1 21  ? 22.034  7.953   -16.626 1.00 17.15 ? 33  SER   B CA  1 
ATOM   2668 C  C   . SER   B 1 21  ? 21.055  6.956   -16.028 1.00 17.67 ? 33  SER   B C   1 
ATOM   2669 O  O   . SER   B 1 21  ? 20.905  6.860   -14.811 1.00 14.74 ? 33  SER   B O   1 
ATOM   2670 C  CB  . SER   B 1 21  ? 23.237  7.197   -17.201 1.00 15.55 ? 33  SER   B CB  1 
ATOM   2671 O  OG  . SER   B 1 21  ? 24.159  8.091   -17.755 1.00 16.52 ? 33  SER   B OG  1 
ATOM   2672 N  N   . GLY   B 1 22  ? 20.391  6.205   -16.897 1.00 15.64 ? 34  GLY   B N   1 
ATOM   2673 C  CA  . GLY   B 1 22  ? 19.467  5.182   -16.441 1.00 13.44 ? 34  GLY   B CA  1 
ATOM   2674 C  C   . GLY   B 1 22  ? 18.234  5.695   -15.732 1.00 12.93 ? 34  GLY   B C   1 
ATOM   2675 O  O   . GLY   B 1 22  ? 17.559  4.915   -15.056 1.00 12.67 ? 34  GLY   B O   1 
ATOM   2676 N  N   . HIS   B 1 23  ? 17.924  6.984   -15.881 1.00 14.14 ? 35  HIS   B N   1 
ATOM   2677 C  CA  . HIS   B 1 23  ? 16.707  7.621   -15.383 1.00 13.66 ? 35  HIS   B CA  1 
ATOM   2678 C  C   . HIS   B 1 23  ? 15.519  7.264   -16.266 1.00 15.84 ? 35  HIS   B C   1 
ATOM   2679 O  O   . HIS   B 1 23  ? 15.660  6.600   -17.294 1.00 14.71 ? 35  HIS   B O   1 
ATOM   2680 C  CB  . HIS   B 1 23  ? 16.880  9.134   -15.382 1.00 15.89 ? 35  HIS   B CB  1 
ATOM   2681 C  CG  . HIS   B 1 23  ? 17.270  9.680   -16.726 1.00 14.38 ? 35  HIS   B CG  1 
ATOM   2682 N  ND1 . HIS   B 1 23  ? 18.491  9.411   -17.312 1.00 20.47 ? 35  HIS   B ND1 1 
ATOM   2683 C  CD2 . HIS   B 1 23  ? 16.613  10.494  -17.585 1.00 18.59 ? 35  HIS   B CD2 1 
ATOM   2684 C  CE1 . HIS   B 1 23  ? 18.556  10.014  -18.487 1.00 18.75 ? 35  HIS   B CE1 1 
ATOM   2685 N  NE2 . HIS   B 1 23  ? 17.426  10.673  -18.680 1.00 18.97 ? 35  HIS   B NE2 1 
ATOM   2686 N  N   . VAL   B 1 24  ? 14.329  7.728   -15.882 1.00 16.73 ? 36  VAL   B N   1 
ATOM   2687 C  CA  . VAL   B 1 24  ? 13.193  7.698   -16.804 1.00 14.26 ? 36  VAL   B CA  1 
ATOM   2688 C  C   . VAL   B 1 24  ? 12.800  9.123   -17.179 1.00 14.83 ? 36  VAL   B C   1 
ATOM   2689 O  O   . VAL   B 1 24  ? 13.025  10.090  -16.435 1.00 15.84 ? 36  VAL   B O   1 
ATOM   2690 C  CB  . VAL   B 1 24  ? 11.966  6.933   -16.257 1.00 14.18 ? 36  VAL   B CB  1 
ATOM   2691 C  CG1 . VAL   B 1 24  ? 12.305  5.464   -16.031 1.00 16.36 ? 36  VAL   B CG1 1 
ATOM   2692 C  CG2 . VAL   B 1 24  ? 11.444  7.590   -14.973 1.00 16.00 ? 36  VAL   B CG2 1 
ATOM   2693 N  N   . ALA   B 1 25  ? 12.221  9.243   -18.376 1.00 14.78 ? 37  ALA   B N   1 
ATOM   2694 C  CA  . ALA   B 1 25  ? 11.588  10.470  -18.833 1.00 18.77 ? 37  ALA   B CA  1 
ATOM   2695 C  C   . ALA   B 1 25  ? 10.361  10.109  -19.664 1.00 19.68 ? 37  ALA   B C   1 
ATOM   2696 O  O   . ALA   B 1 25  ? 10.439  9.296   -20.593 1.00 19.92 ? 37  ALA   B O   1 
ATOM   2697 C  CB  . ALA   B 1 25  ? 12.547  11.341  -19.644 1.00 17.46 ? 37  ALA   B CB  1 
ATOM   2698 N  N   . VAL   B 1 26  ? 9.218   10.683  -19.301 1.00 22.38 ? 38  VAL   B N   1 
ATOM   2699 C  CA  . VAL   B 1 26  ? 7.998   10.511  -20.073 1.00 20.90 ? 38  VAL   B CA  1 
ATOM   2700 C  C   . VAL   B 1 26  ? 7.327   11.866  -20.194 1.00 23.32 ? 38  VAL   B C   1 
ATOM   2701 O  O   . VAL   B 1 26  ? 7.584   12.788  -19.418 1.00 23.63 ? 38  VAL   B O   1 
ATOM   2702 C  CB  . VAL   B 1 26  ? 7.020   9.486   -19.465 1.00 22.24 ? 38  VAL   B CB  1 
ATOM   2703 C  CG1 . VAL   B 1 26  ? 7.634   8.104   -19.467 1.00 20.84 ? 38  VAL   B CG1 1 
ATOM   2704 C  CG2 . VAL   B 1 26  ? 6.597   9.918   -18.068 1.00 23.12 ? 38  VAL   B CG2 1 
ATOM   2705 N  N   . SER   B 1 27  ? 6.456   11.984  -21.189 1.00 23.63 ? 39  SER   B N   1 
ATOM   2706 C  CA  . SER   B 1 27  ? 5.866   13.282  -21.453 1.00 23.56 ? 39  SER   B CA  1 
ATOM   2707 C  C   . SER   B 1 27  ? 4.481   13.116  -22.055 1.00 24.73 ? 39  SER   B C   1 
ATOM   2708 O  O   . SER   B 1 27  ? 4.117   12.051  -22.562 1.00 22.06 ? 39  SER   B O   1 
ATOM   2709 C  CB  . SER   B 1 27  ? 6.751   14.123  -22.380 1.00 29.01 ? 39  SER   B CB  1 
ATOM   2710 O  OG  . SER   B 1 27  ? 6.451   13.870  -23.735 1.00 27.57 ? 39  SER   B OG  1 
ATOM   2711 N  N   . ASP   B 1 28  ? 3.714   14.200  -21.958 1.00 25.69 ? 40  ASP   B N   1 
ATOM   2712 C  CA  . ASP   B 1 28  ? 2.419   14.360  -22.600 1.00 28.84 ? 40  ASP   B CA  1 
ATOM   2713 C  C   . ASP   B 1 28  ? 2.521   15.121  -23.910 1.00 29.33 ? 40  ASP   B C   1 
ATOM   2714 O  O   . ASP   B 1 28  ? 1.495   15.519  -24.466 1.00 30.54 ? 40  ASP   B O   1 
ATOM   2715 C  CB  . ASP   B 1 28  ? 1.458   15.091  -21.657 1.00 27.59 ? 40  ASP   B CB  1 
ATOM   2716 C  CG  . ASP   B 1 28  ? 1.940   16.496  -21.287 1.00 30.04 ? 40  ASP   B CG  1 
ATOM   2717 O  OD1 . ASP   B 1 28  ? 2.899   17.014  -21.892 1.00 29.66 ? 40  ASP   B OD1 1 
ATOM   2718 O  OD2 . ASP   B 1 28  ? 1.359   17.097  -20.371 1.00 32.46 ? 40  ASP   B OD2 1 
ATOM   2719 N  N   . GLY   B 1 29  ? 3.735   15.377  -24.384 1.00 28.18 ? 41  GLY   B N   1 
ATOM   2720 C  CA  . GLY   B 1 29  ? 3.962   16.195  -25.554 1.00 32.33 ? 41  GLY   B CA  1 
ATOM   2721 C  C   . GLY   B 1 29  ? 4.281   17.645  -25.256 1.00 31.96 ? 41  GLY   B C   1 
ATOM   2722 O  O   . GLY   B 1 29  ? 4.663   18.375  -26.180 1.00 32.01 ? 41  GLY   B O   1 
ATOM   2723 N  N   . ARG   B 1 30  ? 4.112   18.088  -24.006 1.00 29.09 ? 42  ARG   B N   1 
ATOM   2724 C  CA  . ARG   B 1 30  ? 4.409   19.459  -23.599 1.00 28.74 ? 42  ARG   B CA  1 
ATOM   2725 C  C   . ARG   B 1 30  ? 5.307   19.560  -22.375 1.00 33.43 ? 42  ARG   B C   1 
ATOM   2726 O  O   . ARG   B 1 30  ? 6.181   20.431  -22.328 1.00 33.90 ? 42  ARG   B O   1 
ATOM   2727 C  CB  . ARG   B 1 30  ? 3.088   20.183  -23.337 1.00 32.46 ? 42  ARG   B CB  1 
ATOM   2728 C  CG  . ARG   B 1 30  ? 3.210   21.672  -23.148 1.00 35.52 ? 42  ARG   B CG  1 
ATOM   2729 C  CD  . ARG   B 1 30  ? 2.185   22.390  -24.017 1.00 38.47 ? 42  ARG   B CD  1 
ATOM   2730 N  NE  . ARG   B 1 30  ? 0.809   22.046  -23.680 1.00 38.84 ? 42  ARG   B NE  1 
ATOM   2731 C  CZ  . ARG   B 1 30  ? -0.230  22.241  -24.484 1.00 41.17 ? 42  ARG   B CZ  1 
ATOM   2732 N  NH1 . ARG   B 1 30  ? -0.077  22.711  -25.713 1.00 41.40 ? 42  ARG   B NH1 1 
ATOM   2733 N  NH2 . ARG   B 1 30  ? -1.453  21.960  -24.044 1.00 42.14 ? 42  ARG   B NH2 1 
ATOM   2734 N  N   . HIS   B 1 31  ? 5.096   18.713  -21.373 1.00 31.02 ? 43  HIS   B N   1 
ATOM   2735 C  CA  . HIS   B 1 31  ? 5.902   18.684  -20.163 1.00 28.71 ? 43  HIS   B CA  1 
ATOM   2736 C  C   . HIS   B 1 31  ? 6.586   17.329  -20.083 1.00 28.16 ? 43  HIS   B C   1 
ATOM   2737 O  O   . HIS   B 1 31  ? 5.938   16.299  -20.281 1.00 28.54 ? 43  HIS   B O   1 
ATOM   2738 C  CB  . HIS   B 1 31  ? 5.043   18.918  -18.915 1.00 31.04 ? 43  HIS   B CB  1 
ATOM   2739 C  CG  . HIS   B 1 31  ? 4.106   20.081  -19.029 1.00 31.51 ? 43  HIS   B CG  1 
ATOM   2740 N  ND1 . HIS   B 1 31  ? 2.872   19.987  -19.639 1.00 34.78 ? 43  HIS   B ND1 1 
ATOM   2741 C  CD2 . HIS   B 1 31  ? 4.226   21.364  -18.616 1.00 33.13 ? 43  HIS   B CD2 1 
ATOM   2742 C  CE1 . HIS   B 1 31  ? 2.269   21.161  -19.588 1.00 33.73 ? 43  HIS   B CE1 1 
ATOM   2743 N  NE2 . HIS   B 1 31  ? 3.071   22.015  -18.976 1.00 33.31 ? 43  HIS   B NE2 1 
ATOM   2744 N  N   . MET   B 1 32  ? 7.885   17.326  -19.794 1.00 27.87 ? 44  MET   B N   1 
ATOM   2745 C  CA  . MET   B 1 32  ? 8.660   16.094  -19.706 1.00 24.62 ? 44  MET   B CA  1 
ATOM   2746 C  C   . MET   B 1 32  ? 8.955   15.814  -18.242 1.00 25.79 ? 44  MET   B C   1 
ATOM   2747 O  O   . MET   B 1 32  ? 9.507   16.672  -17.546 1.00 21.32 ? 44  MET   B O   1 
ATOM   2748 C  CB  . MET   B 1 32  ? 9.953   16.200  -20.512 1.00 26.87 ? 44  MET   B CB  1 
ATOM   2749 C  CG  . MET   B 1 32  ? 10.663  14.886  -20.729 1.00 24.09 ? 44  MET   B CG  1 
ATOM   2750 S  SD  . MET   B 1 32  ? 12.203  15.112  -21.641 1.00 24.34 ? 44  MET   B SD  1 
ATOM   2751 C  CE  . MET   B 1 32  ? 13.250  15.909  -20.420 1.00 20.68 ? 44  MET   B CE  1 
ATOM   2752 N  N   . PHE   B 1 33  ? 8.575   14.627  -17.776 1.00 22.20 ? 45  PHE   B N   1 
ATOM   2753 C  CA  . PHE   B 1 33  ? 8.747   14.262  -16.375 1.00 24.15 ? 45  PHE   B CA  1 
ATOM   2754 C  C   . PHE   B 1 33  ? 9.931   13.320  -16.248 1.00 23.06 ? 45  PHE   B C   1 
ATOM   2755 O  O   . PHE   B 1 33  ? 9.999   12.299  -16.940 1.00 24.73 ? 45  PHE   B O   1 
ATOM   2756 C  CB  . PHE   B 1 33  ? 7.494   13.603  -15.809 1.00 25.25 ? 45  PHE   B CB  1 
ATOM   2757 C  CG  . PHE   B 1 33  ? 6.251   14.397  -16.031 1.00 29.49 ? 45  PHE   B CG  1 
ATOM   2758 C  CD1 . PHE   B 1 33  ? 5.515   14.243  -17.196 1.00 29.54 ? 45  PHE   B CD1 1 
ATOM   2759 C  CD2 . PHE   B 1 33  ? 5.820   15.309  -15.079 1.00 30.57 ? 45  PHE   B CD2 1 
ATOM   2760 C  CE1 . PHE   B 1 33  ? 4.368   14.979  -17.403 1.00 30.79 ? 45  PHE   B CE1 1 
ATOM   2761 C  CE2 . PHE   B 1 33  ? 4.672   16.047  -15.284 1.00 34.24 ? 45  PHE   B CE2 1 
ATOM   2762 C  CZ  . PHE   B 1 33  ? 3.948   15.880  -16.450 1.00 30.40 ? 45  PHE   B CZ  1 
ATOM   2763 N  N   . VAL   B 1 34  ? 10.856  13.666  -15.365 1.00 20.44 ? 46  VAL   B N   1 
ATOM   2764 C  CA  . VAL   B 1 34  ? 12.111  12.943  -15.207 1.00 19.43 ? 46  VAL   B CA  1 
ATOM   2765 C  C   . VAL   B 1 34  ? 12.194  12.423  -13.778 1.00 19.69 ? 46  VAL   B C   1 
ATOM   2766 O  O   . VAL   B 1 34  ? 11.906  13.161  -12.821 1.00 21.45 ? 46  VAL   B O   1 
ATOM   2767 C  CB  . VAL   B 1 34  ? 13.315  13.838  -15.549 1.00 22.53 ? 46  VAL   B CB  1 
ATOM   2768 C  CG1 . VAL   B 1 34  ? 14.622  13.102  -15.270 1.00 21.34 ? 46  VAL   B CG1 1 
ATOM   2769 C  CG2 . VAL   B 1 34  ? 13.243  14.309  -17.017 1.00 19.10 ? 46  VAL   B CG2 1 
ATOM   2770 N  N   . TRP   B 1 35  ? 12.561  11.146  -13.634 1.00 20.29 ? 47  TRP   B N   1 
ATOM   2771 C  CA  . TRP   B 1 35  ? 12.726  10.535  -12.315 1.00 18.42 ? 47  TRP   B CA  1 
ATOM   2772 C  C   . TRP   B 1 35  ? 13.929  9.590   -12.264 1.00 17.34 ? 47  TRP   B C   1 
ATOM   2773 O  O   . TRP   B 1 35  ? 14.198  8.852   -13.210 1.00 13.75 ? 47  TRP   B O   1 
ATOM   2774 C  CB  . TRP   B 1 35  ? 11.460  9.755   -11.926 1.00 20.53 ? 47  TRP   B CB  1 
ATOM   2775 C  CG  . TRP   B 1 35  ? 11.581  9.071   -10.603 1.00 20.41 ? 47  TRP   B CG  1 
ATOM   2776 C  CD1 . TRP   B 1 35  ? 11.290  9.600   -9.388  1.00 23.32 ? 47  TRP   B CD1 1 
ATOM   2777 C  CD2 . TRP   B 1 35  ? 12.039  7.737   -10.361 1.00 17.87 ? 47  TRP   B CD2 1 
ATOM   2778 N  NE1 . TRP   B 1 35  ? 11.547  8.683   -8.397  1.00 18.72 ? 47  TRP   B NE1 1 
ATOM   2779 C  CE2 . TRP   B 1 35  ? 12.001  7.528   -8.972  1.00 18.25 ? 47  TRP   B CE2 1 
ATOM   2780 C  CE3 . TRP   B 1 35  ? 12.496  6.703   -11.182 1.00 15.79 ? 47  TRP   B CE3 1 
ATOM   2781 C  CZ2 . TRP   B 1 35  ? 12.381  6.323   -8.390  1.00 15.74 ? 47  TRP   B CZ2 1 
ATOM   2782 C  CZ3 . TRP   B 1 35  ? 12.879  5.508   -10.600 1.00 14.90 ? 47  TRP   B CZ3 1 
ATOM   2783 C  CH2 . TRP   B 1 35  ? 12.817  5.327   -9.224  1.00 16.55 ? 47  TRP   B CH2 1 
ATOM   2784 N  N   . GLY   B 1 36  ? 14.639  9.588   -11.136 1.00 17.91 ? 48  GLY   B N   1 
ATOM   2785 C  CA  . GLY   B 1 36  ? 15.574  8.506   -10.856 1.00 19.62 ? 48  GLY   B CA  1 
ATOM   2786 C  C   . GLY   B 1 36  ? 16.905  8.573   -11.594 1.00 14.51 ? 48  GLY   B C   1 
ATOM   2787 O  O   . GLY   B 1 36  ? 17.379  9.637   -11.991 1.00 17.06 ? 48  GLY   B O   1 
ATOM   2788 N  N   . GLY   B 1 37  ? 17.503  7.397   -11.782 1.00 13.50 ? 49  GLY   B N   1 
ATOM   2789 C  CA  . GLY   B 1 37  ? 18.799  7.274   -12.423 1.00 15.96 ? 49  GLY   B CA  1 
ATOM   2790 C  C   . GLY   B 1 37  ? 19.902  7.303   -11.393 1.00 18.36 ? 49  GLY   B C   1 
ATOM   2791 O  O   . GLY   B 1 37  ? 19.653  7.280   -10.185 1.00 16.91 ? 49  GLY   B O   1 
ATOM   2792 N  N   . TYR   B 1 38  ? 21.135  7.372   -11.887 1.00 14.79 ? 50  TYR   B N   1 
ATOM   2793 C  CA  . TYR   B 1 38  ? 22.331  7.317   -11.050 1.00 18.46 ? 50  TYR   B CA  1 
ATOM   2794 C  C   . TYR   B 1 38  ? 23.437  8.116   -11.726 1.00 21.55 ? 50  TYR   B C   1 
ATOM   2795 O  O   . TYR   B 1 38  ? 23.339  8.479   -12.901 1.00 18.49 ? 50  TYR   B O   1 
ATOM   2796 C  CB  . TYR   B 1 38  ? 22.802  5.878   -10.826 1.00 21.19 ? 50  TYR   B CB  1 
ATOM   2797 C  CG  . TYR   B 1 38  ? 23.665  5.379   -11.957 1.00 15.85 ? 50  TYR   B CG  1 
ATOM   2798 C  CD1 . TYR   B 1 38  ? 23.107  5.053   -13.180 1.00 15.75 ? 50  TYR   B CD1 1 
ATOM   2799 C  CD2 . TYR   B 1 38  ? 25.055  5.281   -11.815 1.00 17.65 ? 50  TYR   B CD2 1 
ATOM   2800 C  CE1 . TYR   B 1 38  ? 23.894  4.614   -14.234 1.00 17.20 ? 50  TYR   B CE1 1 
ATOM   2801 C  CE2 . TYR   B 1 38  ? 25.850  4.850   -12.860 1.00 18.30 ? 50  TYR   B CE2 1 
ATOM   2802 C  CZ  . TYR   B 1 38  ? 25.264  4.521   -14.077 1.00 16.72 ? 50  TYR   B CZ  1 
ATOM   2803 O  OH  . TYR   B 1 38  ? 26.083  4.087   -15.104 1.00 17.60 ? 50  TYR   B OH  1 
ATOM   2804 N  N   . LYS   B 1 39  ? 24.499  8.384   -10.974 1.00 19.21 ? 51  LYS   B N   1 
ATOM   2805 C  CA  . LYS   B 1 39  ? 25.677  9.051   -11.518 1.00 24.00 ? 51  LYS   B CA  1 
ATOM   2806 C  C   . LYS   B 1 39  ? 26.891  8.538   -10.752 1.00 27.80 ? 51  LYS   B C   1 
ATOM   2807 O  O   . LYS   B 1 39  ? 26.812  7.527   -10.049 1.00 24.06 ? 51  LYS   B O   1 
ATOM   2808 C  CB  . LYS   B 1 39  ? 25.515  10.580  -11.468 1.00 21.11 ? 51  LYS   B CB  1 
ATOM   2809 C  CG  . LYS   B 1 39  ? 25.355  11.174  -10.079 1.00 31.82 ? 51  LYS   B CG  1 
ATOM   2810 C  CD  . LYS   B 1 39  ? 24.951  12.642  -10.177 1.00 31.78 ? 51  LYS   B CD  1 
ATOM   2811 C  CE  . LYS   B 1 39  ? 24.663  13.243  -8.815  1.00 37.50 ? 51  LYS   B CE  1 
ATOM   2812 N  NZ  . LYS   B 1 39  ? 25.916  13.439  -8.050  1.00 40.15 ? 51  LYS   B NZ  1 
ATOM   2813 N  N   . SER   B 1 40  ? 28.021  9.225   -10.892 1.00 30.89 ? 52  SER   B N   1 
ATOM   2814 C  CA  . SER   B 1 40  ? 29.266  8.836   -10.226 1.00 34.94 ? 52  SER   B CA  1 
ATOM   2815 C  C   . SER   B 1 40  ? 29.854  10.065  -9.541  1.00 39.31 ? 52  SER   B C   1 
ATOM   2816 O  O   . SER   B 1 40  ? 30.603  10.822  -10.162 1.00 42.85 ? 52  SER   B O   1 
ATOM   2817 C  CB  . SER   B 1 40  ? 30.244  8.234   -11.220 1.00 33.55 ? 52  SER   B CB  1 
ATOM   2818 O  OG  . SER   B 1 40  ? 30.634  9.207   -12.173 1.00 34.18 ? 52  SER   B OG  1 
ATOM   2819 N  N   . ASN   B 1 41  ? 29.511  10.260  -8.269  1.00 48.55 ? 53  ASN   B N   1 
ATOM   2820 C  CA  . ASN   B 1 41  ? 30.100  11.328  -7.462  1.00 52.32 ? 53  ASN   B CA  1 
ATOM   2821 C  C   . ASN   B 1 41  ? 29.713  11.173  -5.996  1.00 54.99 ? 53  ASN   B C   1 
ATOM   2822 O  O   . ASN   B 1 41  ? 28.989  12.004  -5.447  1.00 55.89 ? 53  ASN   B O   1 
ATOM   2823 C  CB  . ASN   B 1 41  ? 29.670  12.708  -7.970  1.00 58.30 ? 53  ASN   B CB  1 
ATOM   2824 C  CG  . ASN   B 1 41  ? 30.652  13.802  -7.587  1.00 62.40 ? 53  ASN   B CG  1 
ATOM   2825 O  OD1 . ASN   B 1 41  ? 31.814  13.529  -7.287  1.00 61.81 ? 53  ASN   B OD1 1 
ATOM   2826 N  ND2 . ASN   B 1 41  ? 30.190  15.049  -7.602  1.00 63.78 ? 53  ASN   B ND2 1 
ATOM   2827 N  N   . PHE   B 1 49  ? 26.245  7.124   -7.048  1.00 35.61 ? 61  PHE   B N   1 
ATOM   2828 C  CA  . PHE   B 1 49  ? 25.073  6.797   -6.254  1.00 25.69 ? 61  PHE   B CA  1 
ATOM   2829 C  C   . PHE   B 1 49  ? 23.776  7.007   -7.046  1.00 25.64 ? 61  PHE   B C   1 
ATOM   2830 O  O   . PHE   B 1 49  ? 23.784  7.469   -8.189  1.00 26.78 ? 61  PHE   B O   1 
ATOM   2831 C  CB  . PHE   B 1 49  ? 25.040  7.632   -4.963  1.00 34.90 ? 61  PHE   B CB  1 
ATOM   2832 C  CG  . PHE   B 1 49  ? 25.015  9.138   -5.186  1.00 38.90 ? 61  PHE   B CG  1 
ATOM   2833 C  CD1 . PHE   B 1 49  ? 23.921  9.763   -5.777  1.00 40.13 ? 61  PHE   B CD1 1 
ATOM   2834 C  CD2 . PHE   B 1 49  ? 26.069  9.927   -4.769  1.00 42.62 ? 61  PHE   B CD2 1 
ATOM   2835 C  CE1 . PHE   B 1 49  ? 23.896  11.131  -5.977  1.00 46.73 ? 61  PHE   B CE1 1 
ATOM   2836 C  CE2 . PHE   B 1 49  ? 26.049  11.303  -4.959  1.00 48.78 ? 61  PHE   B CE2 1 
ATOM   2837 C  CZ  . PHE   B 1 49  ? 24.953  11.903  -5.559  1.00 45.89 ? 61  PHE   B CZ  1 
ATOM   2838 N  N   . TYR   B 1 50  ? 22.654  6.731   -6.409  1.00 22.72 ? 62  TYR   B N   1 
ATOM   2839 C  CA  . TYR   B 1 50  ? 21.367  6.983   -7.041  1.00 23.43 ? 62  TYR   B CA  1 
ATOM   2840 C  C   . TYR   B 1 50  ? 20.897  8.407   -6.765  1.00 25.05 ? 62  TYR   B C   1 
ATOM   2841 O  O   . TYR   B 1 50  ? 21.133  8.967   -5.690  1.00 26.21 ? 62  TYR   B O   1 
ATOM   2842 C  CB  . TYR   B 1 50  ? 20.325  5.987   -6.549  1.00 20.55 ? 62  TYR   B CB  1 
ATOM   2843 C  CG  . TYR   B 1 50  ? 20.579  4.573   -6.996  1.00 21.63 ? 62  TYR   B CG  1 
ATOM   2844 C  CD1 . TYR   B 1 50  ? 20.179  4.129   -8.257  1.00 21.43 ? 62  TYR   B CD1 1 
ATOM   2845 C  CD2 . TYR   B 1 50  ? 21.226  3.677   -6.157  1.00 23.21 ? 62  TYR   B CD2 1 
ATOM   2846 C  CE1 . TYR   B 1 50  ? 20.421  2.830   -8.660  1.00 21.00 ? 62  TYR   B CE1 1 
ATOM   2847 C  CE2 . TYR   B 1 50  ? 21.470  2.392   -6.548  1.00 23.62 ? 62  TYR   B CE2 1 
ATOM   2848 C  CZ  . TYR   B 1 50  ? 21.064  1.967   -7.797  1.00 21.45 ? 62  TYR   B CZ  1 
ATOM   2849 O  OH  . TYR   B 1 50  ? 21.329  0.660   -8.145  1.00 25.24 ? 62  TYR   B OH  1 
ATOM   2850 N  N   . LEU   B 1 51  ? 20.235  8.995   -7.756  1.00 23.27 ? 63  LEU   B N   1 
ATOM   2851 C  CA  . LEU   B 1 51  ? 19.625  10.302  -7.574  1.00 23.35 ? 63  LEU   B CA  1 
ATOM   2852 C  C   . LEU   B 1 51  ? 18.447  10.194  -6.606  1.00 20.07 ? 63  LEU   B C   1 
ATOM   2853 O  O   . LEU   B 1 51  ? 17.876  9.115   -6.438  1.00 23.59 ? 63  LEU   B O   1 
ATOM   2854 C  CB  . LEU   B 1 51  ? 19.170  10.872  -8.912  1.00 19.16 ? 63  LEU   B CB  1 
ATOM   2855 C  CG  . LEU   B 1 51  ? 20.226  11.580  -9.776  1.00 20.86 ? 63  LEU   B CG  1 
ATOM   2856 C  CD1 . LEU   B 1 51  ? 20.903  12.715  -9.012  1.00 25.10 ? 63  LEU   B CD1 1 
ATOM   2857 C  CD2 . LEU   B 1 51  ? 21.240  10.599  -10.308 1.00 18.70 ? 63  LEU   B CD2 1 
ATOM   2858 N  N   . PRO   B 1 52  ? 18.094  11.288  -5.927  1.00 20.71 ? 64  PRO   B N   1 
ATOM   2859 C  CA  . PRO   B 1 52  ? 17.107  11.198  -4.838  1.00 21.81 ? 64  PRO   B CA  1 
ATOM   2860 C  C   . PRO   B 1 52  ? 15.750  10.719  -5.337  1.00 23.43 ? 64  PRO   B C   1 
ATOM   2861 O  O   . PRO   B 1 52  ? 15.236  11.200  -6.350  1.00 20.94 ? 64  PRO   B O   1 
ATOM   2862 C  CB  . PRO   B 1 52  ? 17.042  12.634  -4.303  1.00 24.93 ? 64  PRO   B CB  1 
ATOM   2863 C  CG  . PRO   B 1 52  ? 18.322  13.265  -4.729  1.00 26.41 ? 64  PRO   B CG  1 
ATOM   2864 C  CD  . PRO   B 1 52  ? 18.652  12.645  -6.054  1.00 24.07 ? 64  PRO   B CD  1 
ATOM   2865 N  N   . ARG   B 1 53  ? 15.165  9.769   -4.596  1.00 22.29 ? 65  ARG   B N   1 
ATOM   2866 C  CA  . ARG   B 1 53  ? 13.941  9.099   -5.038  1.00 19.70 ? 65  ARG   B CA  1 
ATOM   2867 C  C   . ARG   B 1 53  ? 12.728  10.012  -4.992  1.00 25.02 ? 65  ARG   B C   1 
ATOM   2868 O  O   . ARG   B 1 53  ? 11.766  9.803   -5.739  1.00 19.66 ? 65  ARG   B O   1 
ATOM   2869 C  CB  . ARG   B 1 53  ? 13.676  7.868   -4.176  1.00 19.27 ? 65  ARG   B CB  1 
ATOM   2870 C  CG  . ARG   B 1 53  ? 13.629  8.183   -2.679  1.00 22.38 ? 65  ARG   B CG  1 
ATOM   2871 C  CD  . ARG   B 1 53  ? 13.876  6.959   -1.833  1.00 20.45 ? 65  ARG   B CD  1 
ATOM   2872 N  NE  . ARG   B 1 53  ? 12.751  6.034   -1.849  1.00 21.68 ? 65  ARG   B NE  1 
ATOM   2873 C  CZ  . ARG   B 1 53  ? 12.531  5.121   -0.912  1.00 21.31 ? 65  ARG   B CZ  1 
ATOM   2874 N  NH1 . ARG   B 1 53  ? 13.314  5.020   0.154   1.00 20.96 ? 65  ARG   B NH1 1 
ATOM   2875 N  NH2 . ARG   B 1 53  ? 11.494  4.300   -1.037  1.00 18.95 ? 65  ARG   B NH2 1 
ATOM   2876 N  N   . GLU   B 1 54  ? 12.723  10.997  -4.107  1.00 22.86 ? 66  GLU   B N   1 
ATOM   2877 C  CA  . GLU   B 1 54  ? 11.522  11.790  -3.918  1.00 21.38 ? 66  GLU   B CA  1 
ATOM   2878 C  C   . GLU   B 1 54  ? 11.417  12.957  -4.895  1.00 28.51 ? 66  GLU   B C   1 
ATOM   2879 O  O   . GLU   B 1 54  ? 10.401  13.658  -4.892  1.00 26.43 ? 66  GLU   B O   1 
ATOM   2880 C  CB  . GLU   B 1 54  ? 11.466  12.304  -2.468  1.00 27.30 ? 66  GLU   B CB  1 
ATOM   2881 C  CG  . GLU   B 1 54  ? 12.507  13.351  -2.139  1.00 27.27 ? 66  GLU   B CG  1 
ATOM   2882 C  CD  . GLU   B 1 54  ? 13.872  12.763  -1.819  1.00 29.29 ? 66  GLU   B CD  1 
ATOM   2883 O  OE1 . GLU   B 1 54  ? 14.009  11.522  -1.820  1.00 21.99 ? 66  GLU   B OE1 1 
ATOM   2884 O  OE2 . GLU   B 1 54  ? 14.807  13.554  -1.555  1.00 31.24 ? 66  GLU   B OE2 1 
ATOM   2885 N  N   . GLU   B 1 55  ? 12.441  13.185  -5.720  1.00 27.23 ? 67  GLU   B N   1 
ATOM   2886 C  CA  . GLU   B 1 55  ? 12.458  14.304  -6.651  1.00 27.03 ? 67  GLU   B CA  1 
ATOM   2887 C  C   . GLU   B 1 55  ? 11.827  13.915  -7.979  1.00 26.38 ? 67  GLU   B C   1 
ATOM   2888 O  O   . GLU   B 1 55  ? 12.069  12.824  -8.499  1.00 23.72 ? 67  GLU   B O   1 
ATOM   2889 C  CB  . GLU   B 1 55  ? 13.887  14.786  -6.893  1.00 27.30 ? 67  GLU   B CB  1 
ATOM   2890 C  CG  . GLU   B 1 55  ? 14.572  15.271  -5.649  1.00 29.73 ? 67  GLU   B CG  1 
ATOM   2891 C  CD  . GLU   B 1 55  ? 15.937  15.864  -5.926  1.00 33.62 ? 67  GLU   B CD  1 
ATOM   2892 O  OE1 . GLU   B 1 55  ? 16.549  15.508  -6.963  1.00 29.69 ? 67  GLU   B OE1 1 
ATOM   2893 O  OE2 . GLU   B 1 55  ? 16.394  16.688  -5.099  1.00 31.60 ? 67  GLU   B OE2 1 
ATOM   2894 N  N   . LEU   B 1 56  ? 11.005  14.818  -8.505  1.00 26.74 ? 68  LEU   B N   1 
ATOM   2895 C  CA  . LEU   B 1 56  ? 10.378  14.693  -9.813  1.00 26.44 ? 68  LEU   B CA  1 
ATOM   2896 C  C   . LEU   B 1 56  ? 10.686  15.982  -10.561 1.00 32.34 ? 68  LEU   B C   1 
ATOM   2897 O  O   . LEU   B 1 56  ? 10.216  17.057  -10.169 1.00 29.27 ? 68  LEU   B O   1 
ATOM   2898 C  CB  . LEU   B 1 56  ? 8.869   14.476  -9.687  1.00 28.07 ? 68  LEU   B CB  1 
ATOM   2899 C  CG  . LEU   B 1 56  ? 8.094   14.191  -10.972 1.00 26.76 ? 68  LEU   B CG  1 
ATOM   2900 C  CD1 . LEU   B 1 56  ? 8.633   12.926  -11.609 1.00 24.40 ? 68  LEU   B CD1 1 
ATOM   2901 C  CD2 . LEU   B 1 56  ? 6.595   14.068  -10.702 1.00 33.67 ? 68  LEU   B CD2 1 
ATOM   2902 N  N   . TRP   B 1 57  ? 11.492  15.886  -11.614 1.00 23.98 ? 69  TRP   B N   1 
ATOM   2903 C  CA  . TRP   B 1 57  ? 11.887  17.046  -12.398 1.00 26.96 ? 69  TRP   B CA  1 
ATOM   2904 C  C   . TRP   B 1 57  ? 10.963  17.151  -13.603 1.00 28.00 ? 69  TRP   B C   1 
ATOM   2905 O  O   . TRP   B 1 57  ? 10.711  16.152  -14.285 1.00 24.54 ? 69  TRP   B O   1 
ATOM   2906 C  CB  . TRP   B 1 57  ? 13.352  16.946  -12.839 1.00 27.75 ? 69  TRP   B CB  1 
ATOM   2907 C  CG  . TRP   B 1 57  ? 14.338  17.228  -11.729 1.00 32.15 ? 69  TRP   B CG  1 
ATOM   2908 C  CD1 . TRP   B 1 57  ? 14.941  16.312  -10.906 1.00 30.02 ? 69  TRP   B CD1 1 
ATOM   2909 C  CD2 . TRP   B 1 57  ? 14.827  18.511  -11.322 1.00 34.01 ? 69  TRP   B CD2 1 
ATOM   2910 N  NE1 . TRP   B 1 57  ? 15.772  16.947  -10.020 1.00 32.60 ? 69  TRP   B NE1 1 
ATOM   2911 C  CE2 . TRP   B 1 57  ? 15.724  18.297  -10.255 1.00 34.96 ? 69  TRP   B CE2 1 
ATOM   2912 C  CE3 . TRP   B 1 57  ? 14.602  19.819  -11.761 1.00 34.86 ? 69  TRP   B CE3 1 
ATOM   2913 C  CZ2 . TRP   B 1 57  ? 16.390  19.343  -9.620  1.00 36.32 ? 69  TRP   B CZ2 1 
ATOM   2914 C  CZ3 . TRP   B 1 57  ? 15.265  20.857  -11.125 1.00 37.99 ? 69  TRP   B CZ3 1 
ATOM   2915 C  CH2 . TRP   B 1 57  ? 16.146  20.612  -10.067 1.00 35.20 ? 69  TRP   B CH2 1 
ATOM   2916 N  N   . ILE   B 1 58  ? 10.438  18.350  -13.839 1.00 31.04 ? 70  ILE   B N   1 
ATOM   2917 C  CA  . ILE   B 1 58  ? 9.495   18.613  -14.923 1.00 29.16 ? 70  ILE   B CA  1 
ATOM   2918 C  C   . ILE   B 1 58  ? 10.142  19.613  -15.869 1.00 29.12 ? 70  ILE   B C   1 
ATOM   2919 O  O   . ILE   B 1 58  ? 10.562  20.697  -15.444 1.00 31.09 ? 70  ILE   B O   1 
ATOM   2920 C  CB  . ILE   B 1 58  ? 8.155   19.141  -14.385 1.00 27.76 ? 70  ILE   B CB  1 
ATOM   2921 C  CG1 . ILE   B 1 58  ? 7.525   18.108  -13.442 1.00 27.35 ? 70  ILE   B CG1 1 
ATOM   2922 C  CG2 . ILE   B 1 58  ? 7.209   19.514  -15.513 1.00 28.08 ? 70  ILE   B CG2 1 
ATOM   2923 C  CD1 . ILE   B 1 58  ? 6.300   18.622  -12.700 1.00 32.13 ? 70  ILE   B CD1 1 
ATOM   2924 N  N   . TYR   B 1 59  ? 10.235  19.250  -17.141 1.00 30.26 ? 71  TYR   B N   1 
ATOM   2925 C  CA  . TYR   B 1 59  ? 10.812  20.111  -18.165 1.00 29.98 ? 71  TYR   B CA  1 
ATOM   2926 C  C   . TYR   B 1 59  ? 9.692   20.604  -19.073 1.00 30.30 ? 71  TYR   B C   1 
ATOM   2927 O  O   . TYR   B 1 59  ? 8.931   19.799  -19.613 1.00 31.09 ? 71  TYR   B O   1 
ATOM   2928 C  CB  . TYR   B 1 59  ? 11.880  19.362  -18.964 1.00 28.73 ? 71  TYR   B CB  1 
ATOM   2929 C  CG  . TYR   B 1 59  ? 12.418  20.094  -20.180 1.00 28.78 ? 71  TYR   B CG  1 
ATOM   2930 C  CD1 . TYR   B 1 59  ? 13.425  21.042  -20.055 1.00 29.60 ? 71  TYR   B CD1 1 
ATOM   2931 C  CD2 . TYR   B 1 59  ? 11.935  19.812  -21.461 1.00 26.33 ? 71  TYR   B CD2 1 
ATOM   2932 C  CE1 . TYR   B 1 59  ? 13.932  21.699  -21.167 1.00 31.40 ? 71  TYR   B CE1 1 
ATOM   2933 C  CE2 . TYR   B 1 59  ? 12.440  20.459  -22.581 1.00 28.98 ? 71  TYR   B CE2 1 
ATOM   2934 C  CZ  . TYR   B 1 59  ? 13.436  21.406  -22.424 1.00 28.69 ? 71  TYR   B CZ  1 
ATOM   2935 O  OH  . TYR   B 1 59  ? 13.941  22.063  -23.518 1.00 32.65 ? 71  TYR   B OH  1 
ATOM   2936 N  N   . ASN   B 1 60  ? 9.588   21.922  -19.218 1.00 31.16 ? 72  ASN   B N   1 
ATOM   2937 C  CA  . ASN   B 1 60  ? 8.618   22.533  -20.114 1.00 32.95 ? 72  ASN   B CA  1 
ATOM   2938 C  C   . ASN   B 1 60  ? 9.214   22.564  -21.516 1.00 32.10 ? 72  ASN   B C   1 
ATOM   2939 O  O   . ASN   B 1 60  ? 10.234  23.222  -21.742 1.00 30.68 ? 72  ASN   B O   1 
ATOM   2940 C  CB  . ASN   B 1 60  ? 8.270   23.939  -19.631 1.00 35.21 ? 72  ASN   B CB  1 
ATOM   2941 C  CG  . ASN   B 1 60  ? 7.043   24.513  -20.320 1.00 36.55 ? 72  ASN   B CG  1 
ATOM   2942 O  OD1 . ASN   B 1 60  ? 6.863   24.359  -21.525 1.00 38.10 ? 72  ASN   B OD1 1 
ATOM   2943 N  ND2 . ASN   B 1 60  ? 6.192   25.181  -19.549 1.00 35.79 ? 72  ASN   B ND2 1 
ATOM   2944 N  N   . MET   B 1 61  ? 8.583   21.848  -22.449 1.00 31.28 ? 73  MET   B N   1 
ATOM   2945 C  CA  . MET   B 1 61  ? 9.139   21.681  -23.786 1.00 32.48 ? 73  MET   B CA  1 
ATOM   2946 C  C   . MET   B 1 61  ? 8.947   22.905  -24.669 1.00 38.75 ? 73  MET   B C   1 
ATOM   2947 O  O   . MET   B 1 61  ? 9.629   23.023  -25.696 1.00 32.74 ? 73  MET   B O   1 
ATOM   2948 C  CB  . MET   B 1 61  ? 8.517   20.462  -24.464 1.00 34.46 ? 73  MET   B CB  1 
ATOM   2949 C  CG  . MET   B 1 61  ? 8.889   19.150  -23.812 1.00 33.42 ? 73  MET   B CG  1 
ATOM   2950 S  SD  . MET   B 1 61  ? 7.853   17.792  -24.357 1.00 38.07 ? 73  MET   B SD  1 
ATOM   2951 C  CE  . MET   B 1 61  ? 9.066   16.478  -24.408 1.00 28.07 ? 73  MET   B CE  1 
ATOM   2952 N  N   . GLU   B 1 62  ? 8.036   23.803  -24.300 1.00 36.29 ? 74  GLU   B N   1 
ATOM   2953 C  CA  . GLU   B 1 62  ? 7.783   25.020  -25.058 1.00 37.55 ? 74  GLU   B CA  1 
ATOM   2954 C  C   . GLU   B 1 62  ? 8.701   26.158  -24.633 1.00 40.16 ? 74  GLU   B C   1 
ATOM   2955 O  O   . GLU   B 1 62  ? 9.216   26.891  -25.485 1.00 41.71 ? 74  GLU   B O   1 
ATOM   2956 C  CB  . GLU   B 1 62  ? 6.322   25.445  -24.887 1.00 40.77 ? 74  GLU   B CB  1 
ATOM   2957 C  CG  . GLU   B 1 62  ? 5.308   24.451  -25.438 1.00 41.50 ? 74  GLU   B CG  1 
ATOM   2958 C  CD  . GLU   B 1 62  ? 3.873   24.905  -25.225 1.00 45.81 ? 74  GLU   B CD  1 
ATOM   2959 O  OE1 . GLU   B 1 62  ? 3.557   25.403  -24.121 1.00 46.62 ? 74  GLU   B OE1 1 
ATOM   2960 O  OE2 . GLU   B 1 62  ? 3.054   24.766  -26.160 1.00 43.15 ? 74  GLU   B OE2 1 
ATOM   2961 N  N   . THR   B 1 63  ? 8.906   26.313  -23.325 1.00 38.04 ? 75  THR   B N   1 
ATOM   2962 C  CA  . THR   B 1 63  ? 9.726   27.378  -22.758 1.00 41.01 ? 75  THR   B CA  1 
ATOM   2963 C  C   . THR   B 1 63  ? 11.166  26.960  -22.505 1.00 36.98 ? 75  THR   B C   1 
ATOM   2964 O  O   . THR   B 1 63  ? 12.063  27.805  -22.577 1.00 34.80 ? 75  THR   B O   1 
ATOM   2965 C  CB  . THR   B 1 63  ? 9.124   27.863  -21.439 1.00 39.89 ? 75  THR   B CB  1 
ATOM   2966 O  OG1 . THR   B 1 63  ? 9.407   26.903  -20.413 1.00 39.40 ? 75  THR   B OG1 1 
ATOM   2967 C  CG2 . THR   B 1 63  ? 7.617   28.011  -21.570 1.00 39.83 ? 75  THR   B CG2 1 
ATOM   2968 N  N   . GLY   B 1 64  ? 11.411  25.684  -22.218 1.00 37.25 ? 76  GLY   B N   1 
ATOM   2969 C  CA  . GLY   B 1 64  ? 12.757  25.210  -21.954 1.00 34.84 ? 76  GLY   B CA  1 
ATOM   2970 C  C   . GLY   B 1 64  ? 13.229  25.325  -20.523 1.00 37.67 ? 76  GLY   B C   1 
ATOM   2971 O  O   . GLY   B 1 64  ? 14.442  25.276  -20.286 1.00 37.51 ? 76  GLY   B O   1 
ATOM   2972 N  N   . ARG   B 1 65  ? 12.324  25.472  -19.561 1.00 38.32 ? 77  ARG   B N   1 
ATOM   2973 C  CA  . ARG   B 1 65  ? 12.696  25.640  -18.165 1.00 36.84 ? 77  ARG   B CA  1 
ATOM   2974 C  C   . ARG   B 1 65  ? 12.260  24.427  -17.348 1.00 36.30 ? 77  ARG   B C   1 
ATOM   2975 O  O   . ARG   B 1 65  ? 11.320  23.713  -17.715 1.00 35.62 ? 77  ARG   B O   1 
ATOM   2976 C  CB  . ARG   B 1 65  ? 12.097  26.934  -17.600 1.00 40.64 ? 77  ARG   B CB  1 
ATOM   2977 C  CG  . ARG   B 1 65  ? 12.535  28.169  -18.393 1.00 43.45 ? 77  ARG   B CG  1 
ATOM   2978 C  CD  . ARG   B 1 65  ? 12.211  29.493  -17.712 1.00 47.86 ? 77  ARG   B CD  1 
ATOM   2979 N  NE  . ARG   B 1 65  ? 10.870  29.983  -18.014 1.00 47.45 ? 77  ARG   B NE  1 
ATOM   2980 C  CZ  . ARG   B 1 65  ? 10.572  31.259  -18.230 1.00 47.52 ? 77  ARG   B CZ  1 
ATOM   2981 N  NH1 . ARG   B 1 65  ? 11.506  32.196  -18.238 1.00 45.55 ? 77  ARG   B NH1 1 
ATOM   2982 N  NH2 . ARG   B 1 65  ? 9.306   31.602  -18.454 1.00 45.61 ? 77  ARG   B NH2 1 
ATOM   2983 N  N   . TRP   B 1 66  ? 12.977  24.184  -16.252 1.00 35.06 ? 78  TRP   B N   1 
ATOM   2984 C  CA  . TRP   B 1 66  ? 12.784  23.029  -15.389 1.00 33.31 ? 78  TRP   B CA  1 
ATOM   2985 C  C   . TRP   B 1 66  ? 11.983  23.395  -14.142 1.00 38.11 ? 78  TRP   B C   1 
ATOM   2986 O  O   . TRP   B 1 66  ? 11.829  24.567  -13.791 1.00 40.55 ? 78  TRP   B O   1 
ATOM   2987 C  CB  . TRP   B 1 66  ? 14.131  22.446  -14.963 1.00 33.41 ? 78  TRP   B CB  1 
ATOM   2988 C  CG  . TRP   B 1 66  ? 14.898  21.744  -16.037 1.00 31.53 ? 78  TRP   B CG  1 
ATOM   2989 C  CD1 . TRP   B 1 66  ? 15.847  22.283  -16.855 1.00 33.69 ? 78  TRP   B CD1 1 
ATOM   2990 C  CD2 . TRP   B 1 66  ? 14.813  20.355  -16.381 1.00 31.10 ? 78  TRP   B CD2 1 
ATOM   2991 N  NE1 . TRP   B 1 66  ? 16.350  21.320  -17.699 1.00 28.31 ? 78  TRP   B NE1 1 
ATOM   2992 C  CE2 . TRP   B 1 66  ? 15.731  20.127  -17.431 1.00 31.67 ? 78  TRP   B CE2 1 
ATOM   2993 C  CE3 . TRP   B 1 66  ? 14.045  19.284  -15.910 1.00 30.01 ? 78  TRP   B CE3 1 
ATOM   2994 C  CZ2 . TRP   B 1 66  ? 15.904  18.871  -18.015 1.00 27.48 ? 78  TRP   B CZ2 1 
ATOM   2995 C  CZ3 . TRP   B 1 66  ? 14.214  18.037  -16.490 1.00 29.00 ? 78  TRP   B CZ3 1 
ATOM   2996 C  CH2 . TRP   B 1 66  ? 15.137  17.841  -17.539 1.00 27.65 ? 78  TRP   B CH2 1 
ATOM   2997 N  N   . LYS   B 1 67  ? 11.471  22.364  -13.472 1.00 40.07 ? 79  LYS   B N   1 
ATOM   2998 C  CA  . LYS   B 1 67  ? 10.795  22.510  -12.190 1.00 41.75 ? 79  LYS   B CA  1 
ATOM   2999 C  C   . LYS   B 1 67  ? 11.047  21.248  -11.374 1.00 37.68 ? 79  LYS   B C   1 
ATOM   3000 O  O   . LYS   B 1 67  ? 11.061  20.147  -11.926 1.00 35.28 ? 79  LYS   B O   1 
ATOM   3001 C  CB  . LYS   B 1 67  ? 9.290   22.753  -12.379 1.00 37.90 ? 79  LYS   B CB  1 
ATOM   3002 C  CG  . LYS   B 1 67  ? 8.470   22.848  -11.089 1.00 45.69 ? 79  LYS   B CG  1 
ATOM   3003 C  CD  . LYS   B 1 67  ? 9.099   23.784  -10.062 1.00 47.05 ? 79  LYS   B CD  1 
ATOM   3004 C  CE  . LYS   B 1 67  ? 8.047   24.501  -9.225  1.00 50.38 ? 79  LYS   B CE  1 
ATOM   3005 N  NZ  . LYS   B 1 67  ? 6.992   23.594  -8.694  1.00 52.43 ? 79  LYS   B NZ  1 
ATOM   3006 N  N   . LYS   B 1 68  ? 11.255  21.407  -10.067 1.00 38.72 ? 80  LYS   B N   1 
ATOM   3007 C  CA  . LYS   B 1 68  ? 11.508  20.277  -9.177  1.00 37.04 ? 80  LYS   B CA  1 
ATOM   3008 C  C   . LYS   B 1 68  ? 10.442  20.223  -8.091  1.00 39.88 ? 80  LYS   B C   1 
ATOM   3009 O  O   . LYS   B 1 68  ? 10.364  21.120  -7.243  1.00 39.43 ? 80  LYS   B O   1 
ATOM   3010 C  CB  . LYS   B 1 68  ? 12.893  20.358  -8.537  1.00 38.03 ? 80  LYS   B CB  1 
ATOM   3011 C  CG  . LYS   B 1 68  ? 13.201  19.141  -7.665  1.00 40.24 ? 80  LYS   B CG  1 
ATOM   3012 C  CD  . LYS   B 1 68  ? 14.405  19.349  -6.768  1.00 39.77 ? 80  LYS   B CD  1 
ATOM   3013 C  CE  . LYS   B 1 68  ? 14.099  20.317  -5.640  1.00 44.41 ? 80  LYS   B CE  1 
ATOM   3014 N  NZ  . LYS   B 1 68  ? 15.338  20.654  -4.892  1.00 44.69 ? 80  LYS   B NZ  1 
ATOM   3015 N  N   . ILE   B 1 69  ? 9.646   19.158  -8.098  1.00 35.34 ? 81  ILE   B N   1 
ATOM   3016 C  CA  . ILE   B 1 69  ? 8.667   18.911  -7.049  1.00 35.42 ? 81  ILE   B CA  1 
ATOM   3017 C  C   . ILE   B 1 69  ? 9.103   17.682  -6.268  1.00 35.23 ? 81  ILE   B C   1 
ATOM   3018 O  O   . ILE   B 1 69  ? 9.732   16.767  -6.808  1.00 34.71 ? 81  ILE   B O   1 
ATOM   3019 C  CB  . ILE   B 1 69  ? 7.242   18.725  -7.613  1.00 37.06 ? 81  ILE   B CB  1 
ATOM   3020 C  CG1 . ILE   B 1 69  ? 7.235   17.668  -8.717  1.00 37.20 ? 81  ILE   B CG1 1 
ATOM   3021 C  CG2 . ILE   B 1 69  ? 6.694   20.041  -8.145  1.00 37.23 ? 81  ILE   B CG2 1 
ATOM   3022 C  CD1 . ILE   B 1 69  ? 5.851   17.293  -9.170  1.00 36.77 ? 81  ILE   B CD1 1 
ATOM   3023 N  N   . ASN   B 1 70  ? 8.774   17.665  -4.984  1.00 33.40 ? 82  ASN   B N   1 
ATOM   3024 C  CA  . ASN   B 1 70  ? 9.028   16.499  -4.154  1.00 31.61 ? 82  ASN   B CA  1 
ATOM   3025 C  C   . ASN   B 1 70  ? 7.728   15.735  -3.959  1.00 36.29 ? 82  ASN   B C   1 
ATOM   3026 O  O   . ASN   B 1 70  ? 6.699   16.325  -3.612  1.00 38.36 ? 82  ASN   B O   1 
ATOM   3027 C  CB  . ASN   B 1 70  ? 9.632   16.896  -2.810  1.00 39.09 ? 82  ASN   B CB  1 
ATOM   3028 C  CG  . ASN   B 1 70  ? 11.082  17.307  -2.931  1.00 38.04 ? 82  ASN   B CG  1 
ATOM   3029 O  OD1 . ASN   B 1 70  ? 11.985  16.481  -2.800  1.00 36.38 ? 82  ASN   B OD1 1 
ATOM   3030 N  ND2 . ASN   B 1 70  ? 11.314  18.588  -3.196  1.00 44.18 ? 82  ASN   B ND2 1 
ATOM   3031 N  N   . THR   B 1 71  ? 7.781   14.432  -4.197  1.00 32.54 ? 83  THR   B N   1 
ATOM   3032 C  CA  . THR   B 1 71  ? 6.620   13.562  -4.114  1.00 34.48 ? 83  THR   B CA  1 
ATOM   3033 C  C   . THR   B 1 71  ? 6.525   12.945  -2.727  1.00 29.77 ? 83  THR   B C   1 
ATOM   3034 O  O   . THR   B 1 71  ? 7.473   12.971  -1.944  1.00 32.51 ? 83  THR   B O   1 
ATOM   3035 C  CB  . THR   B 1 71  ? 6.711   12.446  -5.152  1.00 27.81 ? 83  THR   B CB  1 
ATOM   3036 O  OG1 . THR   B 1 71  ? 7.858   11.635  -4.857  1.00 28.15 ? 83  THR   B OG1 1 
ATOM   3037 C  CG2 . THR   B 1 71  ? 6.830   13.016  -6.569  1.00 31.25 ? 83  THR   B CG2 1 
ATOM   3038 N  N   . GLU   B 1 72  ? 5.373   12.352  -2.438  1.00 28.22 ? 84  GLU   B N   1 
ATOM   3039 C  CA  . GLU   B 1 72  ? 5.187   11.624  -1.186  1.00 35.01 ? 84  GLU   B CA  1 
ATOM   3040 C  C   . GLU   B 1 72  ? 4.403   10.354  -1.505  1.00 31.26 ? 84  GLU   B C   1 
ATOM   3041 O  O   . GLU   B 1 72  ? 4.313   9.925   -2.662  1.00 27.56 ? 84  GLU   B O   1 
ATOM   3042 C  CB  . GLU   B 1 72  ? 4.518   12.510  -0.120  1.00 36.94 ? 84  GLU   B CB  1 
ATOM   3043 C  CG  . GLU   B 1 72  ? 5.427   13.592  0.468   1.00 34.77 ? 84  GLU   B CG  1 
ATOM   3044 C  CD  . GLU   B 1 72  ? 4.730   14.435  1.519   1.00 38.06 ? 84  GLU   B CD  1 
ATOM   3045 O  OE1 . GLU   B 1 72  ? 3.704   13.982  2.061   1.00 39.30 ? 84  GLU   B OE1 1 
ATOM   3046 O  OE2 . GLU   B 1 72  ? 5.205   15.553  1.810   1.00 41.68 ? 84  GLU   B OE2 1 
ATOM   3047 N  N   . GLY   B 1 73  ? 3.859   9.718   -0.468  1.00 32.24 ? 85  GLY   B N   1 
ATOM   3048 C  CA  . GLY   B 1 73  ? 3.171   8.453   -0.642  1.00 28.09 ? 85  GLY   B CA  1 
ATOM   3049 C  C   . GLY   B 1 73  ? 4.131   7.286   -0.754  1.00 25.77 ? 85  GLY   B C   1 
ATOM   3050 O  O   . GLY   B 1 73  ? 5.150   7.239   -0.052  1.00 24.79 ? 85  GLY   B O   1 
ATOM   3051 N  N   . ASP   B 1 74  ? 3.817   6.330   -1.628  1.00 21.44 ? 86  ASP   B N   1 
ATOM   3052 C  CA  . ASP   B 1 74  ? 4.639   5.135   -1.796  1.00 21.85 ? 86  ASP   B CA  1 
ATOM   3053 C  C   . ASP   B 1 74  ? 5.795   5.442   -2.747  1.00 23.15 ? 86  ASP   B C   1 
ATOM   3054 O  O   . ASP   B 1 74  ? 5.871   4.926   -3.864  1.00 23.04 ? 86  ASP   B O   1 
ATOM   3055 C  CB  . ASP   B 1 74  ? 3.816   3.976   -2.337  1.00 20.69 ? 86  ASP   B CB  1 
ATOM   3056 C  CG  . ASP   B 1 74  ? 2.556   3.726   -1.557  1.00 25.87 ? 86  ASP   B CG  1 
ATOM   3057 O  OD1 . ASP   B 1 74  ? 2.509   4.005   -0.331  1.00 21.85 ? 86  ASP   B OD1 1 
ATOM   3058 O  OD2 . ASP   B 1 74  ? 1.595   3.241   -2.184  1.00 22.24 ? 86  ASP   B OD2 1 
ATOM   3059 N  N   . VAL   B 1 75  ? 6.707   6.297   -2.286  1.00 23.31 ? 87  VAL   B N   1 
ATOM   3060 C  CA  . VAL   B 1 75  ? 7.828   6.698   -3.149  1.00 22.41 ? 87  VAL   B CA  1 
ATOM   3061 C  C   . VAL   B 1 75  ? 8.610   5.456   -3.553  1.00 21.05 ? 87  VAL   B C   1 
ATOM   3062 O  O   . VAL   B 1 75  ? 8.994   4.655   -2.681  1.00 24.00 ? 87  VAL   B O   1 
ATOM   3063 C  CB  . VAL   B 1 75  ? 8.747   7.706   -2.432  1.00 21.97 ? 87  VAL   B CB  1 
ATOM   3064 C  CG1 . VAL   B 1 75  ? 9.806   8.243   -3.400  1.00 19.03 ? 87  VAL   B CG1 1 
ATOM   3065 C  CG2 . VAL   B 1 75  ? 7.932   8.838   -1.820  1.00 22.35 ? 87  VAL   B CG2 1 
ATOM   3066 N  N   . PRO   B 1 76  ? 8.851   5.220   -4.838  1.00 19.61 ? 88  PRO   B N   1 
ATOM   3067 C  CA  . PRO   B 1 76  ? 9.654   4.072   -5.219  1.00 15.89 ? 88  PRO   B CA  1 
ATOM   3068 C  C   . PRO   B 1 76  ? 11.077  4.231   -4.709  1.00 19.30 ? 88  PRO   B C   1 
ATOM   3069 O  O   . PRO   B 1 76  ? 11.524  5.347   -4.392  1.00 17.67 ? 88  PRO   B O   1 
ATOM   3070 C  CB  . PRO   B 1 76  ? 9.596   4.069   -6.767  1.00 18.07 ? 88  PRO   B CB  1 
ATOM   3071 C  CG  . PRO   B 1 76  ? 9.044   5.399   -7.159  1.00 18.06 ? 88  PRO   B CG  1 
ATOM   3072 C  CD  . PRO   B 1 76  ? 8.283   5.943   -5.988  1.00 17.71 ? 88  PRO   B CD  1 
ATOM   3073 N  N   . PRO   B 1 77  ? 11.808  3.133   -4.563  1.00 16.29 ? 89  PRO   B N   1 
ATOM   3074 C  CA  . PRO   B 1 77  ? 13.236  3.244   -4.244  1.00 17.08 ? 89  PRO   B CA  1 
ATOM   3075 C  C   . PRO   B 1 77  ? 13.994  3.899   -5.398  1.00 15.48 ? 89  PRO   B C   1 
ATOM   3076 O  O   . PRO   B 1 77  ? 13.583  3.813   -6.550  1.00 17.04 ? 89  PRO   B O   1 
ATOM   3077 C  CB  . PRO   B 1 77  ? 13.660  1.790   -4.027  1.00 17.43 ? 89  PRO   B CB  1 
ATOM   3078 C  CG  . PRO   B 1 77  ? 12.699  0.989   -4.889  1.00 17.32 ? 89  PRO   B CG  1 
ATOM   3079 C  CD  . PRO   B 1 77  ? 11.387  1.734   -4.774  1.00 15.53 ? 89  PRO   B CD  1 
ATOM   3080 N  N   . SER   B 1 78  ? 15.071  4.612   -5.063  1.00 18.25 ? 90  SER   B N   1 
ATOM   3081 C  CA  . SER   B 1 78  ? 15.989  5.153   -6.062  1.00 18.52 ? 90  SER   B CA  1 
ATOM   3082 C  C   . SER   B 1 78  ? 16.526  4.028   -6.949  1.00 17.69 ? 90  SER   B C   1 
ATOM   3083 O  O   . SER   B 1 78  ? 17.174  3.094   -6.457  1.00 16.57 ? 90  SER   B O   1 
ATOM   3084 C  CB  . SER   B 1 78  ? 17.151  5.873   -5.370  1.00 22.55 ? 90  SER   B CB  1 
ATOM   3085 O  OG  . SER   B 1 78  ? 16.782  7.106   -4.771  1.00 24.57 ? 90  SER   B OG  1 
ATOM   3086 N  N   . MET   B 1 79  ? 16.291  4.135   -8.264  1.00 17.79 ? 91  MET   B N   1 
ATOM   3087 C  CA  . MET   B 1 79  ? 16.613  3.061   -9.198  1.00 15.78 ? 91  MET   B CA  1 
ATOM   3088 C  C   . MET   B 1 79  ? 17.180  3.599   -10.509 1.00 17.55 ? 91  MET   B C   1 
ATOM   3089 O  O   . MET   B 1 79  ? 16.784  4.666   -10.983 1.00 19.23 ? 91  MET   B O   1 
ATOM   3090 C  CB  . MET   B 1 79  ? 15.357  2.212   -9.550  1.00 15.26 ? 91  MET   B CB  1 
ATOM   3091 C  CG  . MET   B 1 79  ? 14.851  1.312   -8.413  1.00 16.88 ? 91  MET   B CG  1 
ATOM   3092 S  SD  . MET   B 1 79  ? 13.319  0.455   -8.853  1.00 18.13 ? 91  MET   B SD  1 
ATOM   3093 C  CE  . MET   B 1 79  ? 12.189  1.842   -8.846  1.00 16.51 ? 91  MET   B CE  1 
ATOM   3094 N  N   . SER   B 1 80  ? 18.074  2.815   -11.115 1.00 15.99 ? 92  SER   B N   1 
ATOM   3095 C  CA  . SER   B 1 80  ? 18.383  2.891   -12.541 1.00 17.33 ? 92  SER   B CA  1 
ATOM   3096 C  C   . SER   B 1 80  ? 17.571  1.854   -13.317 1.00 11.97 ? 92  SER   B C   1 
ATOM   3097 O  O   . SER   B 1 80  ? 17.138  0.839   -12.774 1.00 14.70 ? 92  SER   B O   1 
ATOM   3098 C  CB  . SER   B 1 80  ? 19.881  2.659   -12.773 1.00 14.83 ? 92  SER   B CB  1 
ATOM   3099 O  OG  . SER   B 1 80  ? 20.220  1.307   -12.492 1.00 14.28 ? 92  SER   B OG  1 
ATOM   3100 N  N   . GLY   B 1 81  ? 17.385  2.097   -14.615 1.00 14.57 ? 93  GLY   B N   1 
ATOM   3101 C  CA  . GLY   B 1 81  ? 16.841  1.041   -15.450 1.00 10.35 ? 93  GLY   B CA  1 
ATOM   3102 C  C   . GLY   B 1 81  ? 15.347  0.789   -15.356 1.00 12.72 ? 93  GLY   B C   1 
ATOM   3103 O  O   . GLY   B 1 81  ? 14.890  -0.235  -15.882 1.00 14.00 ? 93  GLY   B O   1 
ATOM   3104 N  N   . SER   B 1 82  ? 14.575  1.656   -14.696 1.00 12.42 ? 94  SER   B N   1 
ATOM   3105 C  CA  . SER   B 1 82  ? 13.130  1.466   -14.606 1.00 11.88 ? 94  SER   B CA  1 
ATOM   3106 C  C   . SER   B 1 82  ? 12.468  1.771   -15.955 1.00 12.50 ? 94  SER   B C   1 
ATOM   3107 O  O   . SER   B 1 82  ? 13.047  2.406   -16.830 1.00 13.21 ? 94  SER   B O   1 
ATOM   3108 C  CB  . SER   B 1 82  ? 12.527  2.360   -13.520 1.00 14.77 ? 94  SER   B CB  1 
ATOM   3109 O  OG  . SER   B 1 82  ? 12.947  1.971   -12.230 1.00 12.25 ? 94  SER   B OG  1 
ATOM   3110 N  N   . CYS   B 1 83  ? 11.226  1.319   -16.103 1.00 12.16 ? 95  CYS   B N   1 
ATOM   3111 C  CA  . CYS   B 1 83  ? 10.505  1.417   -17.372 1.00 12.97 ? 95  CYS   B CA  1 
ATOM   3112 C  C   . CYS   B 1 83  ? 9.192   2.135   -17.096 1.00 13.92 ? 95  CYS   B C   1 
ATOM   3113 O  O   . CYS   B 1 83  ? 8.368   1.643   -16.317 1.00 15.95 ? 95  CYS   B O   1 
ATOM   3114 C  CB  . CYS   B 1 83  ? 10.289  0.022   -17.945 1.00 12.65 ? 95  CYS   B CB  1 
ATOM   3115 S  SG  . CYS   B 1 83  ? 9.399   0.010   -19.527 1.00 15.85 ? 95  CYS   B SG  1 
ATOM   3116 N  N   . ALA   B 1 84  ? 9.015   3.322   -17.679 1.00 13.48 ? 96  ALA   B N   1 
ATOM   3117 C  CA  . ALA   B 1 84  ? 7.909   4.186   -17.284 1.00 16.02 ? 96  ALA   B CA  1 
ATOM   3118 C  C   . ALA   B 1 84  ? 7.164   4.721   -18.497 1.00 18.82 ? 96  ALA   B C   1 
ATOM   3119 O  O   . ALA   B 1 84  ? 7.730   4.851   -19.590 1.00 15.25 ? 96  ALA   B O   1 
ATOM   3120 C  CB  . ALA   B 1 84  ? 8.381   5.364   -16.438 1.00 16.12 ? 96  ALA   B CB  1 
ATOM   3121 N  N   . VAL   B 1 85  ? 5.873   5.025   -18.278 1.00 17.38 ? 97  VAL   B N   1 
ATOM   3122 C  CA  . VAL   B 1 85  ? 4.983   5.567   -19.302 1.00 17.35 ? 97  VAL   B CA  1 
ATOM   3123 C  C   . VAL   B 1 85  ? 4.174   6.708   -18.707 1.00 20.37 ? 97  VAL   B C   1 
ATOM   3124 O  O   . VAL   B 1 85  ? 4.012   6.829   -17.489 1.00 19.90 ? 97  VAL   B O   1 
ATOM   3125 C  CB  . VAL   B 1 85  ? 4.001   4.524   -19.877 1.00 19.31 ? 97  VAL   B CB  1 
ATOM   3126 C  CG1 . VAL   B 1 85  ? 4.697   3.261   -20.205 1.00 18.87 ? 97  VAL   B CG1 1 
ATOM   3127 C  CG2 . VAL   B 1 85  ? 2.860   4.264   -18.892 1.00 19.87 ? 97  VAL   B CG2 1 
ATOM   3128 N  N   . CYS   B 1 86  ? 3.659   7.552   -19.590 1.00 19.67 ? 98  CYS   B N   1 
ATOM   3129 C  CA  . CYS   B 1 86  ? 2.673   8.556   -19.211 1.00 18.89 ? 98  CYS   B CA  1 
ATOM   3130 C  C   . CYS   B 1 86  ? 1.447   8.335   -20.079 1.00 19.36 ? 98  CYS   B C   1 
ATOM   3131 O  O   . CYS   B 1 86  ? 1.546   8.356   -21.308 1.00 20.35 ? 98  CYS   B O   1 
ATOM   3132 C  CB  . CYS   B 1 86  ? 3.218   9.974   -19.385 1.00 21.92 ? 98  CYS   B CB  1 
ATOM   3133 S  SG  . CYS   B 1 86  ? 1.985   11.280  -19.012 1.00 27.71 ? 98  CYS   B SG  1 
ATOM   3134 N  N   . VAL   B 1 87  ? 0.305   8.094   -19.443 1.00 19.58 ? 99  VAL   B N   1 
ATOM   3135 C  CA  . VAL   B 1 87  ? -0.968  7.936   -20.139 1.00 26.71 ? 99  VAL   B CA  1 
ATOM   3136 C  C   . VAL   B 1 87  ? -1.978  8.830   -19.440 1.00 25.21 ? 99  VAL   B C   1 
ATOM   3137 O  O   . VAL   B 1 87  ? -2.226  8.663   -18.240 1.00 24.04 ? 99  VAL   B O   1 
ATOM   3138 C  CB  . VAL   B 1 87  ? -1.453  6.477   -20.147 1.00 25.76 ? 99  VAL   B CB  1 
ATOM   3139 C  CG1 . VAL   B 1 87  ? -2.819  6.378   -20.824 1.00 27.72 ? 99  VAL   B CG1 1 
ATOM   3140 C  CG2 . VAL   B 1 87  ? -0.433  5.572   -20.840 1.00 25.09 ? 99  VAL   B CG2 1 
ATOM   3141 N  N   . ASP   B 1 88  ? -2.562  9.771   -20.184 1.00 29.50 ? 100 ASP   B N   1 
ATOM   3142 C  CA  . ASP   B 1 88  ? -3.546  10.707  -19.627 1.00 28.29 ? 100 ASP   B CA  1 
ATOM   3143 C  C   . ASP   B 1 88  ? -2.962  11.486  -18.447 1.00 29.74 ? 100 ASP   B C   1 
ATOM   3144 O  O   . ASP   B 1 88  ? -3.648  11.757  -17.462 1.00 31.38 ? 100 ASP   B O   1 
ATOM   3145 C  CB  . ASP   B 1 88  ? -4.826  9.977   -19.206 1.00 34.90 ? 100 ASP   B CB  1 
ATOM   3146 C  CG  . ASP   B 1 88  ? -5.586  9.400   -20.382 1.00 37.31 ? 100 ASP   B CG  1 
ATOM   3147 O  OD1 . ASP   B 1 88  ? -5.778  10.131  -21.374 1.00 38.41 ? 100 ASP   B OD1 1 
ATOM   3148 O  OD2 . ASP   B 1 88  ? -5.982  8.211   -20.322 1.00 38.98 ? 100 ASP   B OD2 1 
ATOM   3149 N  N   . ARG   B 1 89  ? -1.675  11.837  -18.543 1.00 29.16 ? 101 ARG   B N   1 
ATOM   3150 C  CA  . ARG   B 1 89  ? -0.949  12.528  -17.474 1.00 30.13 ? 101 ARG   B CA  1 
ATOM   3151 C  C   . ARG   B 1 89  ? -0.940  11.726  -16.176 1.00 28.29 ? 101 ARG   B C   1 
ATOM   3152 O  O   . ARG   B 1 89  ? -0.832  12.284  -15.077 1.00 27.19 ? 101 ARG   B O   1 
ATOM   3153 C  CB  . ARG   B 1 89  ? -1.500  13.937  -17.241 1.00 32.45 ? 101 ARG   B CB  1 
ATOM   3154 C  CG  . ARG   B 1 89  ? -0.984  14.952  -18.240 1.00 32.31 ? 101 ARG   B CG  1 
ATOM   3155 C  CD  . ARG   B 1 89  ? 0.496   15.224  -18.028 1.00 34.97 ? 101 ARG   B CD  1 
ATOM   3156 N  NE  . ARG   B 1 89  ? 0.751   15.991  -16.813 1.00 36.27 ? 101 ARG   B NE  1 
ATOM   3157 C  CZ  . ARG   B 1 89  ? 0.523   17.292  -16.692 1.00 38.03 ? 101 ARG   B CZ  1 
ATOM   3158 N  NH1 . ARG   B 1 89  ? 0.022   18.003  -17.692 1.00 37.39 ? 101 ARG   B NH1 1 
ATOM   3159 N  NH2 . ARG   B 1 89  ? 0.802   17.896  -15.539 1.00 43.64 ? 101 ARG   B NH2 1 
ATOM   3160 N  N   . VAL   B 1 90  ? -1.024  10.406  -16.293 1.00 24.00 ? 102 VAL   B N   1 
ATOM   3161 C  CA  . VAL   B 1 90  ? -0.773  9.498   -15.184 1.00 22.44 ? 102 VAL   B CA  1 
ATOM   3162 C  C   . VAL   B 1 90  ? 0.518   8.755   -15.482 1.00 23.74 ? 102 VAL   B C   1 
ATOM   3163 O  O   . VAL   B 1 90  ? 0.701   8.226   -16.582 1.00 20.32 ? 102 VAL   B O   1 
ATOM   3164 C  CB  . VAL   B 1 90  ? -1.945  8.529   -14.961 1.00 27.71 ? 102 VAL   B CB  1 
ATOM   3165 C  CG1 . VAL   B 1 90  ? -1.583  7.487   -13.929 1.00 24.85 ? 102 VAL   B CG1 1 
ATOM   3166 C  CG2 . VAL   B 1 90  ? -3.152  9.305   -14.504 1.00 26.38 ? 102 VAL   B CG2 1 
ATOM   3167 N  N   . LEU   B 1 91  ? 1.425   8.747   -14.517 1.00 19.77 ? 103 LEU   B N   1 
ATOM   3168 C  CA  . LEU   B 1 91  ? 2.697   8.069   -14.684 1.00 21.25 ? 103 LEU   B CA  1 
ATOM   3169 C  C   . LEU   B 1 91  ? 2.603   6.672   -14.096 1.00 20.02 ? 103 LEU   B C   1 
ATOM   3170 O  O   . LEU   B 1 91  ? 2.059   6.481   -13.001 1.00 21.37 ? 103 LEU   B O   1 
ATOM   3171 C  CB  . LEU   B 1 91  ? 3.821   8.845   -14.004 1.00 20.48 ? 103 LEU   B CB  1 
ATOM   3172 C  CG  . LEU   B 1 91  ? 3.880   10.352  -14.219 1.00 24.51 ? 103 LEU   B CG  1 
ATOM   3173 C  CD1 . LEU   B 1 91  ? 5.151   10.882  -13.580 1.00 26.21 ? 103 LEU   B CD1 1 
ATOM   3174 C  CD2 . LEU   B 1 91  ? 3.841   10.706  -15.698 1.00 24.08 ? 103 LEU   B CD2 1 
ATOM   3175 N  N   . TYR   B 1 92  ? 3.106   5.701   -14.848 1.00 15.93 ? 104 TYR   B N   1 
ATOM   3176 C  CA  . TYR   B 1 92  ? 3.229   4.320   -14.417 1.00 17.82 ? 104 TYR   B CA  1 
ATOM   3177 C  C   . TYR   B 1 92  ? 4.684   3.900   -14.552 1.00 17.63 ? 104 TYR   B C   1 
ATOM   3178 O  O   . TYR   B 1 92  ? 5.329   4.192   -15.560 1.00 20.67 ? 104 TYR   B O   1 
ATOM   3179 C  CB  . TYR   B 1 92  ? 2.362   3.370   -15.250 1.00 16.96 ? 104 TYR   B CB  1 
ATOM   3180 C  CG  . TYR   B 1 92  ? 0.883   3.671   -15.253 1.00 18.66 ? 104 TYR   B CG  1 
ATOM   3181 C  CD1 . TYR   B 1 92  ? 0.051   3.237   -14.220 1.00 20.54 ? 104 TYR   B CD1 1 
ATOM   3182 C  CD2 . TYR   B 1 92  ? 0.315   4.378   -16.296 1.00 21.30 ? 104 TYR   B CD2 1 
ATOM   3183 C  CE1 . TYR   B 1 92  ? -1.316  3.513   -14.235 1.00 21.32 ? 104 TYR   B CE1 1 
ATOM   3184 C  CE2 . TYR   B 1 92  ? -1.032  4.667   -16.317 1.00 23.72 ? 104 TYR   B CE2 1 
ATOM   3185 C  CZ  . TYR   B 1 92  ? -1.849  4.226   -15.291 1.00 24.44 ? 104 TYR   B CZ  1 
ATOM   3186 O  OH  . TYR   B 1 92  ? -3.198  4.516   -15.353 1.00 25.53 ? 104 TYR   B OH  1 
ATOM   3187 N  N   . LEU   B 1 93  ? 5.174   3.173   -13.560 1.00 16.05 ? 105 LEU   B N   1 
ATOM   3188 C  CA  . LEU   B 1 93  ? 6.586   2.844   -13.444 1.00 13.85 ? 105 LEU   B CA  1 
ATOM   3189 C  C   . LEU   B 1 93  ? 6.689   1.376   -13.071 1.00 13.65 ? 105 LEU   B C   1 
ATOM   3190 O  O   . LEU   B 1 93  ? 6.007   0.922   -12.149 1.00 16.83 ? 105 LEU   B O   1 
ATOM   3191 C  CB  . LEU   B 1 93  ? 7.254   3.733   -12.390 1.00 15.09 ? 105 LEU   B CB  1 
ATOM   3192 C  CG  . LEU   B 1 93  ? 8.746   3.664   -12.061 1.00 16.36 ? 105 LEU   B CG  1 
ATOM   3193 C  CD1 . LEU   B 1 93  ? 9.587   4.339   -13.092 1.00 19.47 ? 105 LEU   B CD1 1 
ATOM   3194 C  CD2 . LEU   B 1 93  ? 8.924   4.389   -10.741 1.00 16.52 ? 105 LEU   B CD2 1 
ATOM   3195 N  N   . PHE   B 1 94  ? 7.502   0.625   -13.811 1.00 15.30 ? 106 PHE   B N   1 
ATOM   3196 C  CA  . PHE   B 1 94  ? 7.666   -0.794  -13.549 1.00 13.19 ? 106 PHE   B CA  1 
ATOM   3197 C  C   . PHE   B 1 94  ? 9.139   -1.140  -13.507 1.00 16.12 ? 106 PHE   B C   1 
ATOM   3198 O  O   . PHE   B 1 94  ? 9.920   -0.639  -14.316 1.00 14.25 ? 106 PHE   B O   1 
ATOM   3199 C  CB  . PHE   B 1 94  ? 6.992   -1.691  -14.616 1.00 13.91 ? 106 PHE   B CB  1 
ATOM   3200 C  CG  . PHE   B 1 94  ? 7.409   -3.128  -14.509 1.00 13.44 ? 106 PHE   B CG  1 
ATOM   3201 C  CD1 . PHE   B 1 94  ? 6.795   -3.968  -13.586 1.00 18.52 ? 106 PHE   B CD1 1 
ATOM   3202 C  CD2 . PHE   B 1 94  ? 8.476   -3.619  -15.267 1.00 14.46 ? 106 PHE   B CD2 1 
ATOM   3203 C  CE1 . PHE   B 1 94  ? 7.191   -5.277  -13.455 1.00 19.06 ? 106 PHE   B CE1 1 
ATOM   3204 C  CE2 . PHE   B 1 94  ? 8.891   -4.929  -15.134 1.00 17.28 ? 106 PHE   B CE2 1 
ATOM   3205 C  CZ  . PHE   B 1 94  ? 8.249   -5.766  -14.224 1.00 16.99 ? 106 PHE   B CZ  1 
ATOM   3206 N  N   . GLY   B 1 95  ? 9.508   -2.020  -12.576 1.00 15.34 ? 107 GLY   B N   1 
ATOM   3207 C  CA  . GLY   B 1 95  ? 10.846  -2.579  -12.583 1.00 17.24 ? 107 GLY   B CA  1 
ATOM   3208 C  C   . GLY   B 1 95  ? 11.926  -1.556  -12.236 1.00 14.07 ? 107 GLY   B C   1 
ATOM   3209 O  O   . GLY   B 1 95  ? 11.658  -0.442  -11.780 1.00 13.76 ? 107 GLY   B O   1 
ATOM   3210 N  N   . GLY   B 1 96  ? 13.162  -1.946  -12.530 1.00 13.25 ? 108 GLY   B N   1 
ATOM   3211 C  CA  . GLY   B 1 96  ? 14.340  -1.173  -12.183 1.00 16.07 ? 108 GLY   B CA  1 
ATOM   3212 C  C   . GLY   B 1 96  ? 15.298  -1.938  -11.284 1.00 16.14 ? 108 GLY   B C   1 
ATOM   3213 O  O   . GLY   B 1 96  ? 15.101  -3.108  -10.955 1.00 13.52 ? 108 GLY   B O   1 
ATOM   3214 N  N   . HIS   B 1 97  ? 16.356  -1.231  -10.882 1.00 15.30 ? 109 HIS   B N   1 
ATOM   3215 C  CA  . HIS   B 1 97  ? 17.401  -1.776  -10.023 1.00 15.73 ? 109 HIS   B CA  1 
ATOM   3216 C  C   . HIS   B 1 97  ? 17.738  -0.736  -8.969  1.00 14.92 ? 109 HIS   B C   1 
ATOM   3217 O  O   . HIS   B 1 97  ? 18.096  0.393   -9.309  1.00 15.80 ? 109 HIS   B O   1 
ATOM   3218 C  CB  . HIS   B 1 97  ? 18.653  -2.127  -10.835 1.00 17.19 ? 109 HIS   B CB  1 
ATOM   3219 C  CG  . HIS   B 1 97  ? 19.713  -2.829  -10.049 1.00 20.90 ? 109 HIS   B CG  1 
ATOM   3220 N  ND1 . HIS   B 1 97  ? 20.724  -2.157  -9.398  1.00 20.03 ? 109 HIS   B ND1 1 
ATOM   3221 C  CD2 . HIS   B 1 97  ? 19.940  -4.148  -9.842  1.00 19.62 ? 109 HIS   B CD2 1 
ATOM   3222 C  CE1 . HIS   B 1 97  ? 21.525  -3.032  -8.814  1.00 20.78 ? 109 HIS   B CE1 1 
ATOM   3223 N  NE2 . HIS   B 1 97  ? 21.070  -4.246  -9.064  1.00 20.38 ? 109 HIS   B NE2 1 
ATOM   3224 N  N   . HIS   B 1 98  ? 17.636  -1.111  -7.704  1.00 21.24 ? 110 HIS   B N   1 
ATOM   3225 C  CA  . HIS   B 1 98  ? 17.961  -0.223  -6.588  1.00 20.06 ? 110 HIS   B CA  1 
ATOM   3226 C  C   . HIS   B 1 98  ? 19.149  -0.804  -5.815  1.00 20.97 ? 110 HIS   B C   1 
ATOM   3227 O  O   . HIS   B 1 98  ? 19.797  -1.756  -6.260  1.00 17.70 ? 110 HIS   B O   1 
ATOM   3228 C  CB  . HIS   B 1 98  ? 16.715  0.001   -5.723  1.00 18.86 ? 110 HIS   B CB  1 
ATOM   3229 C  CG  . HIS   B 1 98  ? 16.008  -1.261  -5.347  1.00 21.35 ? 110 HIS   B CG  1 
ATOM   3230 N  ND1 . HIS   B 1 98  ? 16.436  -2.069  -4.319  1.00 20.21 ? 110 HIS   B ND1 1 
ATOM   3231 C  CD2 . HIS   B 1 98  ? 14.903  -1.854  -5.858  1.00 19.32 ? 110 HIS   B CD2 1 
ATOM   3232 C  CE1 . HIS   B 1 98  ? 15.634  -3.115  -4.221  1.00 20.44 ? 110 HIS   B CE1 1 
ATOM   3233 N  NE2 . HIS   B 1 98  ? 14.700  -3.013  -5.148  1.00 18.99 ? 110 HIS   B NE2 1 
ATOM   3234 N  N   . SER   B 1 99  ? 19.441  -0.213  -4.647  1.00 20.67 ? 111 SER   B N   1 
ATOM   3235 C  CA  . SER   B 1 99  ? 20.640  -0.571  -3.890  1.00 23.61 ? 111 SER   B CA  1 
ATOM   3236 C  C   . SER   B 1 99  ? 20.662  -2.035  -3.455  1.00 22.84 ? 111 SER   B C   1 
ATOM   3237 O  O   . SER   B 1 99  ? 21.734  -2.560  -3.136  1.00 25.79 ? 111 SER   B O   1 
ATOM   3238 C  CB  . SER   B 1 99  ? 20.764  0.329   -2.659  1.00 21.36 ? 111 SER   B CB  1 
ATOM   3239 O  OG  . SER   B 1 99  ? 19.600  0.241   -1.838  1.00 26.53 ? 111 SER   B OG  1 
ATOM   3240 N  N   . ARG   B 1 100 ? 19.511  -2.703  -3.433  1.00 20.31 ? 112 ARG   B N   1 
ATOM   3241 C  CA  . ARG   B 1 100 ? 19.415  -4.109  -3.072  1.00 19.07 ? 112 ARG   B CA  1 
ATOM   3242 C  C   . ARG   B 1 100 ? 18.883  -4.971  -4.219  1.00 23.99 ? 112 ARG   B C   1 
ATOM   3243 O  O   . ARG   B 1 100 ? 18.281  -6.020  -3.988  1.00 25.10 ? 112 ARG   B O   1 
ATOM   3244 C  CB  . ARG   B 1 100 ? 18.541  -4.264  -1.830  1.00 24.87 ? 112 ARG   B CB  1 
ATOM   3245 C  CG  . ARG   B 1 100 ? 18.924  -3.288  -0.717  1.00 26.66 ? 112 ARG   B CG  1 
ATOM   3246 C  CD  . ARG   B 1 100 ? 19.344  -4.020  0.525   1.00 29.82 ? 112 ARG   B CD  1 
ATOM   3247 N  NE  . ARG   B 1 100 ? 18.411  -5.087  0.871   1.00 35.73 ? 112 ARG   B NE  1 
ATOM   3248 C  CZ  . ARG   B 1 100 ? 17.273  -4.905  1.527   1.00 29.32 ? 112 ARG   B CZ  1 
ATOM   3249 N  NH1 . ARG   B 1 100 ? 16.905  -3.708  1.952   1.00 30.79 ? 112 ARG   B NH1 1 
ATOM   3250 N  NH2 . ARG   B 1 100 ? 16.479  -5.950  1.749   1.00 28.44 ? 112 ARG   B NH2 1 
ATOM   3251 N  N   . GLY   B 1 101 ? 19.074  -4.542  -5.456  1.00 19.99 ? 113 GLY   B N   1 
ATOM   3252 C  CA  . GLY   B 1 101 ? 18.812  -5.402  -6.591  1.00 19.87 ? 113 GLY   B CA  1 
ATOM   3253 C  C   . GLY   B 1 101 ? 17.600  -4.987  -7.406  1.00 19.45 ? 113 GLY   B C   1 
ATOM   3254 O  O   . GLY   B 1 101 ? 17.116  -3.853  -7.338  1.00 16.64 ? 113 GLY   B O   1 
ATOM   3255 N  N   . ASN   B 1 102 ? 17.102  -5.945  -8.191  1.00 19.80 ? 114 ASN   B N   1 
ATOM   3256 C  CA  . ASN   B 1 102 ? 16.017  -5.699  -9.133  1.00 17.47 ? 114 ASN   B CA  1 
ATOM   3257 C  C   . ASN   B 1 102 ? 14.656  -5.841  -8.462  1.00 19.29 ? 114 ASN   B C   1 
ATOM   3258 O  O   . ASN   B 1 102 ? 14.514  -6.428  -7.383  1.00 18.12 ? 114 ASN   B O   1 
ATOM   3259 C  CB  . ASN   B 1 102 ? 16.092  -6.659  -10.321 1.00 18.80 ? 114 ASN   B CB  1 
ATOM   3260 C  CG  . ASN   B 1 102 ? 17.251  -6.353  -11.262 1.00 19.72 ? 114 ASN   B CG  1 
ATOM   3261 O  OD1 . ASN   B 1 102 ? 18.089  -7.215  -11.511 1.00 20.25 ? 114 ASN   B OD1 1 
ATOM   3262 N  ND2 . ASN   B 1 102 ? 17.273  -5.144  -11.823 1.00 16.43 ? 114 ASN   B ND2 1 
ATOM   3263 N  N   . THR   B 1 103 ? 13.641  -5.311  -9.136  1.00 17.33 ? 115 THR   B N   1 
ATOM   3264 C  CA  . THR   B 1 103 ? 12.278  -5.342  -8.638  1.00 17.01 ? 115 THR   B CA  1 
ATOM   3265 C  C   . THR   B 1 103 ? 11.315  -5.591  -9.796  1.00 16.79 ? 115 THR   B C   1 
ATOM   3266 O  O   . THR   B 1 103 ? 11.646  -5.398  -10.968 1.00 17.40 ? 115 THR   B O   1 
ATOM   3267 C  CB  . THR   B 1 103 ? 11.918  -4.031  -7.912  1.00 19.43 ? 115 THR   B CB  1 
ATOM   3268 O  OG1 . THR   B 1 103 ? 10.635  -4.162  -7.283  1.00 19.41 ? 115 THR   B OG1 1 
ATOM   3269 C  CG2 . THR   B 1 103 ? 11.859  -2.868  -8.903  1.00 21.16 ? 115 THR   B CG2 1 
ATOM   3270 N  N   . ASN   B 1 104 ? 10.115  -6.048  -9.437  1.00 15.87 ? 116 ASN   B N   1 
ATOM   3271 C  CA  . ASN   B 1 104 ? 8.979   -6.158  -10.342 1.00 19.64 ? 116 ASN   B CA  1 
ATOM   3272 C  C   . ASN   B 1 104 ? 7.767   -5.446  -9.761  1.00 18.28 ? 116 ASN   B C   1 
ATOM   3273 O  O   . ASN   B 1 104 ? 6.632   -5.768  -10.129 1.00 21.37 ? 116 ASN   B O   1 
ATOM   3274 C  CB  . ASN   B 1 104 ? 8.649   -7.626  -10.657 1.00 17.54 ? 116 ASN   B CB  1 
ATOM   3275 C  CG  . ASN   B 1 104 ? 8.327   -8.435  -9.414  1.00 19.95 ? 116 ASN   B CG  1 
ATOM   3276 O  OD1 . ASN   B 1 104 ? 8.128   -7.885  -8.334  1.00 21.94 ? 116 ASN   B OD1 1 
ATOM   3277 N  ND2 . ASN   B 1 104 ? 8.249   -9.751  -9.569  1.00 22.13 ? 116 ASN   B ND2 1 
ATOM   3278 N  N   . LYS   B 1 105 ? 7.988   -4.513  -8.830  1.00 18.39 ? 117 LYS   B N   1 
ATOM   3279 C  CA  . LYS   B 1 105 ? 6.918   -3.690  -8.283  1.00 20.32 ? 117 LYS   B CA  1 
ATOM   3280 C  C   . LYS   B 1 105 ? 6.456   -2.643  -9.302  1.00 16.15 ? 117 LYS   B C   1 
ATOM   3281 O  O   . LYS   B 1 105 ? 7.233   -2.175  -10.143 1.00 16.66 ? 117 LYS   B O   1 
ATOM   3282 C  CB  . LYS   B 1 105 ? 7.389   -3.001  -7.002  1.00 17.16 ? 117 LYS   B CB  1 
ATOM   3283 N  N   . PHE   B 1 106 ? 5.167   -2.290  -9.223  1.00 16.72 ? 118 PHE   B N   1 
ATOM   3284 C  CA  . PHE   B 1 106 ? 4.493   -1.389  -10.158 1.00 20.26 ? 118 PHE   B CA  1 
ATOM   3285 C  C   . PHE   B 1 106 ? 3.941   -0.180  -9.411  1.00 16.52 ? 118 PHE   B C   1 
ATOM   3286 O  O   . PHE   B 1 106 ? 3.206   -0.339  -8.439  1.00 19.40 ? 118 PHE   B O   1 
ATOM   3287 C  CB  . PHE   B 1 106 ? 3.343   -2.118  -10.855 1.00 15.73 ? 118 PHE   B CB  1 
ATOM   3288 C  CG  . PHE   B 1 106 ? 2.656   -1.313  -11.934 1.00 20.17 ? 118 PHE   B CG  1 
ATOM   3289 C  CD1 . PHE   B 1 106 ? 3.154   -1.295  -13.227 1.00 18.69 ? 118 PHE   B CD1 1 
ATOM   3290 C  CD2 . PHE   B 1 106 ? 1.494   -0.602  -11.666 1.00 21.00 ? 118 PHE   B CD2 1 
ATOM   3291 C  CE1 . PHE   B 1 106 ? 2.526   -0.577  -14.221 1.00 20.09 ? 118 PHE   B CE1 1 
ATOM   3292 C  CE2 . PHE   B 1 106 ? 0.865   0.124   -12.661 1.00 20.53 ? 118 PHE   B CE2 1 
ATOM   3293 C  CZ  . PHE   B 1 106 ? 1.380   0.135   -13.944 1.00 18.54 ? 118 PHE   B CZ  1 
ATOM   3294 N  N   . TYR   B 1 107 ? 4.255   1.019   -9.885  1.00 16.73 ? 119 TYR   B N   1 
ATOM   3295 C  CA  . TYR   B 1 107 ? 3.828   2.241   -9.217  1.00 16.41 ? 119 TYR   B CA  1 
ATOM   3296 C  C   . TYR   B 1 107 ? 3.019   3.112   -10.160 1.00 19.01 ? 119 TYR   B C   1 
ATOM   3297 O  O   . TYR   B 1 107 ? 3.112   3.007   -11.389 1.00 19.38 ? 119 TYR   B O   1 
ATOM   3298 C  CB  . TYR   B 1 107 ? 5.009   3.061   -8.699  1.00 17.41 ? 119 TYR   B CB  1 
ATOM   3299 C  CG  . TYR   B 1 107 ? 5.856   2.326   -7.707  1.00 20.75 ? 119 TYR   B CG  1 
ATOM   3300 C  CD1 . TYR   B 1 107 ? 6.830   1.438   -8.131  1.00 20.38 ? 119 TYR   B CD1 1 
ATOM   3301 C  CD2 . TYR   B 1 107 ? 5.678   2.510   -6.347  1.00 20.51 ? 119 TYR   B CD2 1 
ATOM   3302 C  CE1 . TYR   B 1 107 ? 7.605   0.761   -7.246  1.00 18.31 ? 119 TYR   B CE1 1 
ATOM   3303 C  CE2 . TYR   B 1 107 ? 6.457   1.829   -5.436  1.00 18.55 ? 119 TYR   B CE2 1 
ATOM   3304 C  CZ  . TYR   B 1 107 ? 7.411   0.950   -5.893  1.00 19.20 ? 119 TYR   B CZ  1 
ATOM   3305 O  OH  . TYR   B 1 107 ? 8.203   0.259   -5.008  1.00 18.36 ? 119 TYR   B OH  1 
ATOM   3306 N  N   . MET   B 1 108 ? 2.220   3.983   -9.567  1.00 20.39 ? 120 MET   B N   1 
ATOM   3307 C  CA  . MET   B 1 108 ? 1.433   4.947   -10.315 1.00 18.78 ? 120 MET   B CA  1 
ATOM   3308 C  C   . MET   B 1 108 ? 1.612   6.317   -9.685  1.00 21.92 ? 120 MET   B C   1 
ATOM   3309 O  O   . MET   B 1 108 ? 1.717   6.430   -8.457  1.00 24.73 ? 120 MET   B O   1 
ATOM   3310 C  CB  . MET   B 1 108 ? -0.046  4.535   -10.336 1.00 24.53 ? 120 MET   B CB  1 
ATOM   3311 C  CG  . MET   B 1 108 ? -0.974  5.606   -10.830 1.00 25.74 ? 120 MET   B CG  1 
ATOM   3312 S  SD  . MET   B 1 108 ? -2.698  5.074   -10.754 1.00 36.09 ? 120 MET   B SD  1 
ATOM   3313 C  CE  . MET   B 1 108 ? -2.927  4.895   -8.987  1.00 32.24 ? 120 MET   B CE  1 
ATOM   3314 N  N   . LEU   B 1 109 ? 1.681   7.352   -10.520 1.00 20.21 ? 121 LEU   B N   1 
ATOM   3315 C  CA  . LEU   B 1 109 ? 1.767   8.727   -10.034 1.00 23.87 ? 121 LEU   B CA  1 
ATOM   3316 C  C   . LEU   B 1 109 ? 0.794   9.584   -10.822 1.00 25.32 ? 121 LEU   B C   1 
ATOM   3317 O  O   . LEU   B 1 109 ? 1.067   9.939   -11.973 1.00 24.82 ? 121 LEU   B O   1 
ATOM   3318 C  CB  . LEU   B 1 109 ? 3.172   9.300   -10.157 1.00 22.56 ? 121 LEU   B CB  1 
ATOM   3319 C  CG  . LEU   B 1 109 ? 3.212   10.657  -9.456  1.00 28.58 ? 121 LEU   B CG  1 
ATOM   3320 C  CD1 . LEU   B 1 109 ? 3.845   10.524  -8.064  1.00 27.11 ? 121 LEU   B CD1 1 
ATOM   3321 C  CD2 . LEU   B 1 109 ? 3.922   11.693  -10.292 1.00 31.86 ? 121 LEU   B CD2 1 
ATOM   3322 N  N   . ASP   B 1 110 ? -0.319  9.940   -10.192 1.00 27.65 ? 122 ASP   B N   1 
ATOM   3323 C  CA  . ASP   B 1 110 ? -1.315  10.791  -10.818 1.00 28.86 ? 122 ASP   B CA  1 
ATOM   3324 C  C   . ASP   B 1 110 ? -0.820  12.232  -10.794 1.00 30.46 ? 122 ASP   B C   1 
ATOM   3325 O  O   . ASP   B 1 110 ? -0.731  12.849  -9.728  1.00 36.12 ? 122 ASP   B O   1 
ATOM   3326 C  CB  . ASP   B 1 110 ? -2.647  10.648  -10.096 1.00 29.14 ? 122 ASP   B CB  1 
ATOM   3327 C  CG  . ASP   B 1 110 ? -3.805  11.094  -10.944 1.00 35.97 ? 122 ASP   B CG  1 
ATOM   3328 O  OD1 . ASP   B 1 110 ? -3.586  11.968  -11.811 1.00 33.11 ? 122 ASP   B OD1 1 
ATOM   3329 O  OD2 . ASP   B 1 110 ? -4.920  10.563  -10.747 1.00 35.70 ? 122 ASP   B OD2 1 
ATOM   3330 N  N   . SER   B 1 111 ? -0.510  12.775  -11.968 1.00 30.90 ? 123 SER   B N   1 
ATOM   3331 C  CA  . SER   B 1 111 ? 0.059   14.111  -12.091 1.00 37.32 ? 123 SER   B CA  1 
ATOM   3332 C  C   . SER   B 1 111 ? -0.949  15.123  -12.623 1.00 38.21 ? 123 SER   B C   1 
ATOM   3333 O  O   . SER   B 1 111 ? -0.563  16.224  -13.026 1.00 40.20 ? 123 SER   B O   1 
ATOM   3334 C  CB  . SER   B 1 111 ? 1.302   14.080  -12.986 1.00 37.08 ? 123 SER   B CB  1 
ATOM   3335 O  OG  . SER   B 1 111 ? 0.971   13.804  -14.337 1.00 36.94 ? 123 SER   B OG  1 
ATOM   3336 N  N   . ARG   B 1 112 ? -2.233  14.775  -12.626 1.00 37.78 ? 124 ARG   B N   1 
ATOM   3337 C  CA  . ARG   B 1 112 ? -3.219  15.626  -13.283 1.00 41.37 ? 124 ARG   B CA  1 
ATOM   3338 C  C   . ARG   B 1 112 ? -3.565  16.859  -12.458 1.00 46.56 ? 124 ARG   B C   1 
ATOM   3339 O  O   . ARG   B 1 112 ? -3.842  17.919  -13.031 1.00 49.96 ? 124 ARG   B O   1 
ATOM   3340 C  CB  . ARG   B 1 112 ? -4.474  14.817  -13.604 1.00 37.62 ? 124 ARG   B CB  1 
ATOM   3341 C  CG  . ARG   B 1 112 ? -4.262  13.821  -14.743 1.00 39.06 ? 124 ARG   B CG  1 
ATOM   3342 C  CD  . ARG   B 1 112 ? -5.560  13.134  -15.110 1.00 36.18 ? 124 ARG   B CD  1 
ATOM   3343 N  NE  . ARG   B 1 112 ? -6.105  12.433  -13.956 1.00 37.18 ? 124 ARG   B NE  1 
ATOM   3344 C  CZ  . ARG   B 1 112 ? -6.303  11.125  -13.896 1.00 36.68 ? 124 ARG   B CZ  1 
ATOM   3345 N  NH1 . ARG   B 1 112 ? -6.078  10.344  -14.938 1.00 39.87 ? 124 ARG   B NH1 1 
ATOM   3346 N  NH2 . ARG   B 1 112 ? -6.746  10.588  -12.765 1.00 35.81 ? 124 ARG   B NH2 1 
ATOM   3347 N  N   . SER   B 1 113 ? -3.549  16.750  -11.134 1.00 49.67 ? 125 SER   B N   1 
ATOM   3348 C  CA  . SER   B 1 113 ? -3.792  17.902  -10.270 1.00 50.06 ? 125 SER   B CA  1 
ATOM   3349 C  C   . SER   B 1 113 ? -2.611  18.128  -9.332  1.00 50.56 ? 125 SER   B C   1 
ATOM   3350 O  O   . SER   B 1 113 ? -1.894  17.187  -8.984  1.00 50.26 ? 125 SER   B O   1 
ATOM   3351 C  CB  . SER   B 1 113 ? -5.079  17.716  -9.465  1.00 52.55 ? 125 SER   B CB  1 
ATOM   3352 O  OG  . SER   B 1 113 ? -4.956  16.653  -8.537  1.00 56.77 ? 125 SER   B OG  1 
ATOM   3353 N  N   . VAL   B 1 117 ? 0.933   18.483  -3.588  1.00 47.03 ? 129 VAL   B N   1 
ATOM   3354 C  CA  . VAL   B 1 117 ? 2.062   17.563  -3.621  1.00 44.18 ? 129 VAL   B CA  1 
ATOM   3355 C  C   . VAL   B 1 117 ? 1.618   16.232  -4.216  1.00 42.83 ? 129 VAL   B C   1 
ATOM   3356 O  O   . VAL   B 1 117 ? 0.600   15.662  -3.817  1.00 41.75 ? 129 VAL   B O   1 
ATOM   3357 C  CB  . VAL   B 1 117 ? 2.685   17.382  -2.214  1.00 46.95 ? 129 VAL   B CB  1 
ATOM   3358 C  CG1 . VAL   B 1 117 ? 3.322   16.006  -2.065  1.00 38.53 ? 129 VAL   B CG1 1 
ATOM   3359 C  CG2 . VAL   B 1 117 ? 3.723   18.462  -1.967  1.00 48.88 ? 129 VAL   B CG2 1 
ATOM   3360 N  N   . LEU   B 1 118 ? 2.395   15.751  -5.183  1.00 41.66 ? 130 LEU   B N   1 
ATOM   3361 C  CA  . LEU   B 1 118 ? 2.032   14.560  -5.935  1.00 38.69 ? 130 LEU   B CA  1 
ATOM   3362 C  C   . LEU   B 1 118 ? 2.351   13.308  -5.126  1.00 36.82 ? 130 LEU   B C   1 
ATOM   3363 O  O   . LEU   B 1 118 ? 3.330   13.269  -4.375  1.00 34.31 ? 130 LEU   B O   1 
ATOM   3364 C  CB  . LEU   B 1 118 ? 2.754   14.548  -7.284  1.00 38.50 ? 130 LEU   B CB  1 
ATOM   3365 C  CG  . LEU   B 1 118 ? 2.111   15.410  -8.387  1.00 42.31 ? 130 LEU   B CG  1 
ATOM   3366 C  CD1 . LEU   B 1 118 ? 2.095   16.900  -8.045  1.00 44.93 ? 130 LEU   B CD1 1 
ATOM   3367 C  CD2 . LEU   B 1 118 ? 2.785   15.183  -9.740  1.00 40.19 ? 130 LEU   B CD2 1 
ATOM   3368 N  N   . GLN   B 1 119 ? 1.500   12.292  -5.267  1.00 35.12 ? 131 GLN   B N   1 
ATOM   3369 C  CA  . GLN   B 1 119 ? 1.488   11.123  -4.392  1.00 34.28 ? 131 GLN   B CA  1 
ATOM   3370 C  C   . GLN   B 1 119 ? 1.737   9.856   -5.197  1.00 25.94 ? 131 GLN   B C   1 
ATOM   3371 O  O   . GLN   B 1 119 ? 0.961   9.534   -6.098  1.00 26.18 ? 131 GLN   B O   1 
ATOM   3372 C  CB  . GLN   B 1 119 ? 0.142   11.015  -3.673  1.00 33.71 ? 131 GLN   B CB  1 
ATOM   3373 C  CG  . GLN   B 1 119 ? -0.094  12.090  -2.654  1.00 35.04 ? 131 GLN   B CG  1 
ATOM   3374 C  CD  . GLN   B 1 119 ? 0.662   11.815  -1.380  1.00 38.65 ? 131 GLN   B CD  1 
ATOM   3375 O  OE1 . GLN   B 1 119 ? 1.491   12.614  -0.951  1.00 40.90 ? 131 GLN   B OE1 1 
ATOM   3376 N  NE2 . GLN   B 1 119 ? 0.378   10.674  -0.762  1.00 40.29 ? 131 GLN   B NE2 1 
ATOM   3377 N  N   . TRP   B 1 120 ? 2.780   9.110   -4.840  1.00 25.52 ? 132 TRP   B N   1 
ATOM   3378 C  CA  . TRP   B 1 120 ? 3.017   7.816   -5.463  1.00 22.80 ? 132 TRP   B CA  1 
ATOM   3379 C  C   . TRP   B 1 120 ? 2.107   6.747   -4.871  1.00 21.30 ? 132 TRP   B C   1 
ATOM   3380 O  O   . TRP   B 1 120 ? 1.821   6.743   -3.671  1.00 25.93 ? 132 TRP   B O   1 
ATOM   3381 C  CB  . TRP   B 1 120 ? 4.473   7.385   -5.294  1.00 23.91 ? 132 TRP   B CB  1 
ATOM   3382 C  CG  . TRP   B 1 120 ? 5.464   8.094   -6.164  1.00 24.34 ? 132 TRP   B CG  1 
ATOM   3383 C  CD1 . TRP   B 1 120 ? 6.234   9.161   -5.818  1.00 25.44 ? 132 TRP   B CD1 1 
ATOM   3384 C  CD2 . TRP   B 1 120 ? 5.843   7.745   -7.502  1.00 23.37 ? 132 TRP   B CD2 1 
ATOM   3385 N  NE1 . TRP   B 1 120 ? 7.054   9.514   -6.860  1.00 23.02 ? 132 TRP   B NE1 1 
ATOM   3386 C  CE2 . TRP   B 1 120 ? 6.828   8.662   -7.909  1.00 22.20 ? 132 TRP   B CE2 1 
ATOM   3387 C  CE3 . TRP   B 1 120 ? 5.427   6.757   -8.399  1.00 21.41 ? 132 TRP   B CE3 1 
ATOM   3388 C  CZ2 . TRP   B 1 120 ? 7.416   8.620   -9.172  1.00 20.83 ? 132 TRP   B CZ2 1 
ATOM   3389 C  CZ3 . TRP   B 1 120 ? 6.002   6.718   -9.658  1.00 19.17 ? 132 TRP   B CZ3 1 
ATOM   3390 C  CH2 . TRP   B 1 120 ? 6.982   7.648   -10.036 1.00 22.89 ? 132 TRP   B CH2 1 
ATOM   3391 N  N   . GLU   B 1 121 ? 1.665   5.828   -5.723  1.00 19.71 ? 133 GLU   B N   1 
ATOM   3392 C  CA  . GLU   B 1 121 ? 0.821   4.703   -5.338  1.00 20.26 ? 133 GLU   B CA  1 
ATOM   3393 C  C   . GLU   B 1 121 ? 1.453   3.408   -5.835  1.00 22.16 ? 133 GLU   B C   1 
ATOM   3394 O  O   . GLU   B 1 121 ? 1.537   3.178   -7.049  1.00 21.85 ? 133 GLU   B O   1 
ATOM   3395 C  CB  . GLU   B 1 121 ? -0.588  4.854   -5.915  1.00 23.99 ? 133 GLU   B CB  1 
ATOM   3396 C  CG  . GLU   B 1 121 ? -1.306  6.114   -5.495  1.00 26.80 ? 133 GLU   B CG  1 
ATOM   3397 C  CD  . GLU   B 1 121 ? -2.159  5.911   -4.262  1.00 33.58 ? 133 GLU   B CD  1 
ATOM   3398 O  OE1 . GLU   B 1 121 ? -2.621  4.768   -4.021  1.00 36.10 ? 133 GLU   B OE1 1 
ATOM   3399 O  OE2 . GLU   B 1 121 ? -2.362  6.901   -3.527  1.00 34.28 ? 133 GLU   B OE2 1 
ATOM   3400 N  N   . ARG   B 1 122 ? 1.874   2.548   -4.906  1.00 23.70 ? 134 ARG   B N   1 
ATOM   3401 C  CA  . ARG   B 1 122 ? 2.281   1.197   -5.280  1.00 22.18 ? 134 ARG   B CA  1 
ATOM   3402 C  C   . ARG   B 1 122 ? 1.023   0.357   -5.449  1.00 23.57 ? 134 ARG   B C   1 
ATOM   3403 O  O   . ARG   B 1 122 ? 0.187   0.306   -4.546  1.00 25.53 ? 134 ARG   B O   1 
ATOM   3404 C  CB  . ARG   B 1 122 ? 3.207   0.596   -4.224  1.00 20.52 ? 134 ARG   B CB  1 
ATOM   3405 C  CG  . ARG   B 1 122 ? 3.893   -0.699  -4.643  1.00 20.00 ? 134 ARG   B CG  1 
ATOM   3406 C  CD  . ARG   B 1 122 ? 4.700   -1.304  -3.484  1.00 20.00 ? 134 ARG   B CD  1 
ATOM   3407 N  NE  . ARG   B 1 122 ? 3.831   -1.834  -2.435  1.00 26.54 ? 134 ARG   B NE  1 
ATOM   3408 C  CZ  . ARG   B 1 122 ? 3.468   -1.173  -1.341  1.00 24.99 ? 134 ARG   B CZ  1 
ATOM   3409 N  NH1 . ARG   B 1 122 ? 3.917   0.045   -1.085  1.00 27.85 ? 134 ARG   B NH1 1 
ATOM   3410 N  NH2 . ARG   B 1 122 ? 2.608   -1.736  -0.499  1.00 24.15 ? 134 ARG   B NH2 1 
ATOM   3411 N  N   . ILE   B 1 123 ? 0.866   -0.277  -6.609  1.00 16.77 ? 135 ILE   B N   1 
ATOM   3412 C  CA  . ILE   B 1 123 ? -0.349  -1.007  -6.942  1.00 23.83 ? 135 ILE   B CA  1 
ATOM   3413 C  C   . ILE   B 1 123 ? -0.147  -2.485  -6.652  1.00 22.10 ? 135 ILE   B C   1 
ATOM   3414 O  O   . ILE   B 1 123 ? 0.820   -3.095  -7.123  1.00 24.45 ? 135 ILE   B O   1 
ATOM   3415 C  CB  . ILE   B 1 123 ? -0.750  -0.790  -8.411  1.00 20.79 ? 135 ILE   B CB  1 
ATOM   3416 C  CG1 . ILE   B 1 123 ? -0.799  0.702   -8.716  1.00 25.01 ? 135 ILE   B CG1 1 
ATOM   3417 C  CG2 . ILE   B 1 123 ? -2.114  -1.420  -8.676  1.00 24.66 ? 135 ILE   B CG2 1 
ATOM   3418 C  CD1 . ILE   B 1 123 ? -1.802  1.458   -7.875  1.00 26.20 ? 135 ILE   B CD1 1 
ATOM   3419 N  N   . ASP   B 1 124 ? -1.066  -3.057  -5.868  1.00 29.99 ? 136 ASP   B N   1 
ATOM   3420 C  CA  . ASP   B 1 124 ? -1.134  -4.495  -5.606  1.00 29.42 ? 136 ASP   B CA  1 
ATOM   3421 C  C   . ASP   B 1 124 ? -1.738  -5.172  -6.833  1.00 26.45 ? 136 ASP   B C   1 
ATOM   3422 O  O   . ASP   B 1 124 ? -2.916  -5.532  -6.873  1.00 30.19 ? 136 ASP   B O   1 
ATOM   3423 C  CB  . ASP   B 1 124 ? -1.978  -4.783  -4.366  1.00 35.58 ? 136 ASP   B CB  1 
ATOM   3424 C  CG  . ASP   B 1 124 ? -1.234  -4.538  -3.057  1.00 42.66 ? 136 ASP   B CG  1 
ATOM   3425 O  OD1 . ASP   B 1 124 ? -0.018  -4.229  -3.072  1.00 36.08 ? 136 ASP   B OD1 1 
ATOM   3426 O  OD2 . ASP   B 1 124 ? -1.886  -4.673  -2.000  1.00 49.62 ? 136 ASP   B OD2 1 
ATOM   3427 N  N   . CYS   B 1 125 ? -0.919  -5.340  -7.864  1.00 22.39 ? 137 CYS   B N   1 
ATOM   3428 C  CA  . CYS   B 1 125 ? -1.426  -5.908  -9.107  1.00 25.86 ? 137 CYS   B CA  1 
ATOM   3429 C  C   . CYS   B 1 125 ? -1.829  -7.363  -8.916  1.00 22.72 ? 137 CYS   B C   1 
ATOM   3430 O  O   . CYS   B 1 125 ? -1.198  -8.102  -8.155  1.00 24.76 ? 137 CYS   B O   1 
ATOM   3431 C  CB  . CYS   B 1 125 ? -0.376  -5.810  -10.204 1.00 19.60 ? 137 CYS   B CB  1 
ATOM   3432 S  SG  . CYS   B 1 125 ? 0.092   -4.134  -10.546 1.00 23.99 ? 137 CYS   B SG  1 
ATOM   3433 N  N   . GLN   B 1 126 ? -2.883  -7.767  -9.620  1.00 22.37 ? 138 GLN   B N   1 
ATOM   3434 C  CA  . GLN   B 1 126 ? -3.329  -9.150  -9.651  1.00 24.47 ? 138 GLN   B CA  1 
ATOM   3435 C  C   . GLN   B 1 126 ? -2.517  -9.941  -10.673 1.00 25.65 ? 138 GLN   B C   1 
ATOM   3436 O  O   . GLN   B 1 126 ? -1.859  -9.379  -11.555 1.00 23.35 ? 138 GLN   B O   1 
ATOM   3437 C  CB  . GLN   B 1 126 ? -4.822  -9.229  -9.993  1.00 26.93 ? 138 GLN   B CB  1 
ATOM   3438 C  CG  . GLN   B 1 126 ? -5.687  -8.217  -9.237  1.00 27.56 ? 138 GLN   B CG  1 
ATOM   3439 C  CD  . GLN   B 1 126 ? -7.173  -8.327  -9.568  1.00 34.13 ? 138 GLN   B CD  1 
ATOM   3440 O  OE1 . GLN   B 1 126 ? -7.792  -7.359  -10.018 1.00 33.47 ? 138 GLN   B OE1 1 
ATOM   3441 N  NE2 . GLN   B 1 126 ? -7.753  -9.505  -9.335  1.00 35.32 ? 138 GLN   B NE2 1 
ATOM   3442 N  N   . GLY   B 1 127 ? -2.577  -11.262 -10.552 1.00 25.49 ? 139 GLY   B N   1 
ATOM   3443 C  CA  . GLY   B 1 127 ? -1.927  -12.120 -11.520 1.00 22.68 ? 139 GLY   B CA  1 
ATOM   3444 C  C   . GLY   B 1 127 ? -0.441  -12.272 -11.249 1.00 23.36 ? 139 GLY   B C   1 
ATOM   3445 O  O   . GLY   B 1 127 ? 0.106   -11.779 -10.259 1.00 25.61 ? 139 GLY   B O   1 
ATOM   3446 N  N   . ILE   B 1 128 ? 0.228   -12.960 -12.168 1.00 22.28 ? 140 ILE   B N   1 
ATOM   3447 C  CA  . ILE   B 1 128 ? 1.640   -13.293 -12.022 1.00 25.49 ? 140 ILE   B CA  1 
ATOM   3448 C  C   . ILE   B 1 128 ? 2.452   -12.171 -12.672 1.00 20.14 ? 140 ILE   B C   1 
ATOM   3449 O  O   . ILE   B 1 128 ? 2.417   -12.043 -13.908 1.00 25.88 ? 140 ILE   B O   1 
ATOM   3450 C  CB  . ILE   B 1 128 ? 1.975   -14.654 -12.639 1.00 23.67 ? 140 ILE   B CB  1 
ATOM   3451 C  CG1 . ILE   B 1 128 ? 1.109   -15.749 -12.019 1.00 26.99 ? 140 ILE   B CG1 1 
ATOM   3452 C  CG2 . ILE   B 1 128 ? 3.462   -14.958 -12.473 1.00 26.94 ? 140 ILE   B CG2 1 
ATOM   3453 C  CD1 . ILE   B 1 128 ? 1.511   -17.157 -12.408 1.00 26.29 ? 140 ILE   B CD1 1 
ATOM   3454 N  N   . PRO   B 1 129 ? 3.179   -11.374 -11.907 1.00 22.94 ? 141 PRO   B N   1 
ATOM   3455 C  CA  . PRO   B 1 129 ? 3.931   -10.279 -12.489 1.00 20.86 ? 141 PRO   B CA  1 
ATOM   3456 C  C   . PRO   B 1 129 ? 5.110   -10.820 -13.273 1.00 19.20 ? 141 PRO   B C   1 
ATOM   3457 O  O   . PRO   B 1 129 ? 5.391   -12.026 -13.227 1.00 19.21 ? 141 PRO   B O   1 
ATOM   3458 C  CB  . PRO   B 1 129 ? 4.385   -9.475  -11.258 1.00 21.60 ? 141 PRO   B CB  1 
ATOM   3459 C  CG  . PRO   B 1 129 ? 4.487   -10.471 -10.192 1.00 21.08 ? 141 PRO   B CG  1 
ATOM   3460 C  CD  . PRO   B 1 129 ? 3.413   -11.498 -10.456 1.00 22.53 ? 141 PRO   B CD  1 
ATOM   3461 N  N   . PRO   B 1 130 ? 5.799   -9.971  -14.024 1.00 18.33 ? 142 PRO   B N   1 
ATOM   3462 C  CA  . PRO   B 1 130 ? 7.053   -10.389 -14.657 1.00 19.86 ? 142 PRO   B CA  1 
ATOM   3463 C  C   . PRO   B 1 130 ? 8.128   -10.643 -13.607 1.00 19.31 ? 142 PRO   B C   1 
ATOM   3464 O  O   . PRO   B 1 130 ? 8.011   -10.282 -12.437 1.00 16.44 ? 142 PRO   B O   1 
ATOM   3465 C  CB  . PRO   B 1 130 ? 7.427   -9.197  -15.543 1.00 15.70 ? 142 PRO   B CB  1 
ATOM   3466 C  CG  . PRO   B 1 130 ? 6.196   -8.317  -15.595 1.00 15.83 ? 142 PRO   B CG  1 
ATOM   3467 C  CD  . PRO   B 1 130 ? 5.436   -8.578  -14.348 1.00 18.22 ? 142 PRO   B CD  1 
ATOM   3468 N  N   . SER   B 1 131 ? 9.207   -11.271 -14.050 1.00 18.79 ? 143 SER   B N   1 
ATOM   3469 C  CA  . SER   B 1 131 ? 10.352  -11.434 -13.164 1.00 18.92 ? 143 SER   B CA  1 
ATOM   3470 C  C   . SER   B 1 131 ? 10.972  -10.072 -12.841 1.00 18.99 ? 143 SER   B C   1 
ATOM   3471 O  O   . SER   B 1 131 ? 10.840  -9.106  -13.595 1.00 21.00 ? 143 SER   B O   1 
ATOM   3472 C  CB  . SER   B 1 131 ? 11.381  -12.373 -13.801 1.00 19.30 ? 143 SER   B CB  1 
ATOM   3473 O  OG  . SER   B 1 131 ? 11.844  -11.877 -15.046 1.00 22.56 ? 143 SER   B OG  1 
ATOM   3474 N  N   . SER   B 1 132 ? 11.654  -9.991  -11.695 1.00 14.56 ? 144 SER   B N   1 
ATOM   3475 C  CA  . SER   B 1 132 ? 12.295  -8.737  -11.321 1.00 13.91 ? 144 SER   B CA  1 
ATOM   3476 C  C   . SER   B 1 132 ? 13.387  -8.389  -12.330 1.00 17.63 ? 144 SER   B C   1 
ATOM   3477 O  O   . SER   B 1 132 ? 14.275  -9.201  -12.598 1.00 19.78 ? 144 SER   B O   1 
ATOM   3478 C  CB  . SER   B 1 132 ? 12.880  -8.851  -9.908  1.00 18.44 ? 144 SER   B CB  1 
ATOM   3479 O  OG  . SER   B 1 132 ? 11.846  -9.129  -8.975  1.00 22.38 ? 144 SER   B OG  1 
ATOM   3480 N  N   . LYS   B 1 133 ? 13.315  -7.190  -12.912 1.00 15.64 ? 145 LYS   B N   1 
ATOM   3481 C  CA  . LYS   B 1 133 ? 14.211  -6.894  -14.023 1.00 17.38 ? 145 LYS   B CA  1 
ATOM   3482 C  C   . LYS   B 1 133 ? 14.303  -5.394  -14.270 1.00 14.50 ? 145 LYS   B C   1 
ATOM   3483 O  O   . LYS   B 1 133 ? 13.534  -4.596  -13.724 1.00 13.74 ? 145 LYS   B O   1 
ATOM   3484 C  CB  . LYS   B 1 133 ? 13.752  -7.615  -15.295 1.00 14.76 ? 145 LYS   B CB  1 
ATOM   3485 C  CG  . LYS   B 1 133 ? 12.342  -7.289  -15.679 1.00 12.38 ? 145 LYS   B CG  1 
ATOM   3486 C  CD  . LYS   B 1 133 ? 11.970  -8.035  -16.948 1.00 13.90 ? 145 LYS   B CD  1 
ATOM   3487 C  CE  . LYS   B 1 133 ? 10.540  -7.812  -17.371 1.00 14.09 ? 145 LYS   B CE  1 
ATOM   3488 N  NZ  . LYS   B 1 133 ? 10.294  -8.635  -18.594 1.00 17.07 ? 145 LYS   B NZ  1 
ATOM   3489 N  N   . ASP   B 1 134 ? 15.254  -5.026  -15.135 1.00 12.98 ? 146 ASP   B N   1 
ATOM   3490 C  CA  . ASP   B 1 134 ? 15.457  -3.638  -15.540 1.00 11.69 ? 146 ASP   B CA  1 
ATOM   3491 C  C   . ASP   B 1 134 ? 15.798  -3.603  -17.026 1.00 10.75 ? 146 ASP   B C   1 
ATOM   3492 O  O   . ASP   B 1 134 ? 15.829  -4.641  -17.695 1.00 12.14 ? 146 ASP   B O   1 
ATOM   3493 C  CB  . ASP   B 1 134 ? 16.545  -2.938  -14.687 1.00 12.61 ? 146 ASP   B CB  1 
ATOM   3494 C  CG  . ASP   B 1 134 ? 17.968  -3.469  -14.917 1.00 19.02 ? 146 ASP   B CG  1 
ATOM   3495 O  OD1 . ASP   B 1 134 ? 18.293  -4.043  -15.982 1.00 13.91 ? 146 ASP   B OD1 1 
ATOM   3496 O  OD2 . ASP   B 1 134 ? 18.796  -3.273  -13.998 1.00 16.93 ? 146 ASP   B OD2 1 
ATOM   3497 N  N   . LYS   B 1 135 ? 16.026  -2.393  -17.528 1.00 9.92  ? 147 LYS   B N   1 
ATOM   3498 C  CA  . LYS   B 1 135 ? 16.516  -2.141  -18.896 1.00 10.74 ? 147 LYS   B CA  1 
ATOM   3499 C  C   . LYS   B 1 135 ? 15.682  -2.875  -19.950 1.00 11.89 ? 147 LYS   B C   1 
ATOM   3500 O  O   . LYS   B 1 135 ? 16.197  -3.653  -20.756 1.00 12.95 ? 147 LYS   B O   1 
ATOM   3501 C  CB  . LYS   B 1 135 ? 17.999  -2.511  -19.009 1.00 11.71 ? 147 LYS   B CB  1 
ATOM   3502 C  CG  . LYS   B 1 135 ? 18.945  -1.605  -18.188 1.00 14.05 ? 147 LYS   B CG  1 
ATOM   3503 C  CD  . LYS   B 1 135 ? 20.400  -1.909  -18.484 1.00 14.00 ? 147 LYS   B CD  1 
ATOM   3504 C  CE  . LYS   B 1 135 ? 20.765  -3.318  -18.062 1.00 15.66 ? 147 LYS   B CE  1 
ATOM   3505 N  NZ  . LYS   B 1 135 ? 20.630  -3.511  -16.602 1.00 15.63 ? 147 LYS   B NZ  1 
ATOM   3506 N  N   . LEU   B 1 136 ? 14.373  -2.616  -19.908 1.00 9.61  ? 148 LEU   B N   1 
ATOM   3507 C  CA  . LEU   B 1 136 ? 13.373  -3.206  -20.800 1.00 13.66 ? 148 LEU   B CA  1 
ATOM   3508 C  C   . LEU   B 1 136 ? 12.689  -2.115  -21.614 1.00 11.53 ? 148 LEU   B C   1 
ATOM   3509 O  O   . LEU   B 1 136 ? 13.225  -1.008  -21.766 1.00 15.09 ? 148 LEU   B O   1 
ATOM   3510 C  CB  . LEU   B 1 136 ? 12.316  -4.017  -20.031 1.00 11.64 ? 148 LEU   B CB  1 
ATOM   3511 C  CG  . LEU   B 1 136 ? 11.487  -3.234  -19.019 1.00 12.56 ? 148 LEU   B CG  1 
ATOM   3512 C  CD1 . LEU   B 1 136 ? 10.057  -3.699  -18.994 1.00 16.60 ? 148 LEU   B CD1 1 
ATOM   3513 C  CD2 . LEU   B 1 136 ? 12.105  -3.398  -17.616 1.00 12.13 ? 148 LEU   B CD2 1 
ATOM   3514 N  N   . GLY   B 1 137 ? 11.538  -2.439  -22.206 1.00 10.70 ? 149 GLY   B N   1 
ATOM   3515 C  CA  . GLY   B 1 137 ? 10.772  -1.457  -22.948 1.00 12.60 ? 149 GLY   B CA  1 
ATOM   3516 C  C   . GLY   B 1 137 ? 9.295   -1.774  -22.829 1.00 13.45 ? 149 GLY   B C   1 
ATOM   3517 O  O   . GLY   B 1 137 ? 8.904   -2.843  -22.346 1.00 12.77 ? 149 GLY   B O   1 
ATOM   3518 N  N   . VAL   B 1 138 ? 8.464   -0.829  -23.260 1.00 11.42 ? 150 VAL   B N   1 
ATOM   3519 C  CA  . VAL   B 1 138 ? 7.027   -0.987  -23.072 1.00 10.64 ? 150 VAL   B CA  1 
ATOM   3520 C  C   . VAL   B 1 138 ? 6.284   -0.307  -24.212 1.00 11.63 ? 150 VAL   B C   1 
ATOM   3521 O  O   . VAL   B 1 138 ? 6.701   0.735   -24.726 1.00 13.22 ? 150 VAL   B O   1 
ATOM   3522 C  CB  . VAL   B 1 138 ? 6.560   -0.438  -21.709 1.00 11.72 ? 150 VAL   B CB  1 
ATOM   3523 C  CG1 . VAL   B 1 138 ? 6.844   1.051   -21.638 1.00 16.56 ? 150 VAL   B CG1 1 
ATOM   3524 C  CG2 . VAL   B 1 138 ? 5.071   -0.684  -21.536 1.00 14.42 ? 150 VAL   B CG2 1 
ATOM   3525 N  N   . TRP   B 1 139 ? 5.167   -0.909  -24.596 1.00 13.76 ? 151 TRP   B N   1 
ATOM   3526 C  CA  . TRP   B 1 139 ? 4.266   -0.335  -25.575 1.00 13.33 ? 151 TRP   B CA  1 
ATOM   3527 C  C   . TRP   B 1 139 ? 2.944   -0.017  -24.894 1.00 15.69 ? 151 TRP   B C   1 
ATOM   3528 O  O   . TRP   B 1 139 ? 2.449   -0.808  -24.083 1.00 15.00 ? 151 TRP   B O   1 
ATOM   3529 C  CB  . TRP   B 1 139 ? 4.027   -1.305  -26.717 1.00 13.05 ? 151 TRP   B CB  1 
ATOM   3530 C  CG  . TRP   B 1 139 ? 5.243   -1.881  -27.394 1.00 13.98 ? 151 TRP   B CG  1 
ATOM   3531 C  CD1 . TRP   B 1 139 ? 6.134   -1.224  -28.186 1.00 13.57 ? 151 TRP   B CD1 1 
ATOM   3532 C  CD2 . TRP   B 1 139 ? 5.648   -3.256  -27.393 1.00 14.98 ? 151 TRP   B CD2 1 
ATOM   3533 N  NE1 . TRP   B 1 139 ? 7.079   -2.104  -28.680 1.00 11.03 ? 151 TRP   B NE1 1 
ATOM   3534 C  CE2 . TRP   B 1 139 ? 6.810   -3.354  -28.199 1.00 12.10 ? 151 TRP   B CE2 1 
ATOM   3535 C  CE3 . TRP   B 1 139 ? 5.157   -4.410  -26.772 1.00 12.66 ? 151 TRP   B CE3 1 
ATOM   3536 C  CZ2 . TRP   B 1 139 ? 7.474   -4.562  -28.416 1.00 16.67 ? 151 TRP   B CZ2 1 
ATOM   3537 C  CZ3 . TRP   B 1 139 ? 5.804   -5.611  -26.994 1.00 14.45 ? 151 TRP   B CZ3 1 
ATOM   3538 C  CH2 . TRP   B 1 139 ? 6.968   -5.676  -27.793 1.00 15.09 ? 151 TRP   B CH2 1 
ATOM   3539 N  N   . VAL   B 1 140 ? 2.369   1.130   -25.218 1.00 15.77 ? 152 VAL   B N   1 
ATOM   3540 C  CA  . VAL   B 1 140 ? 1.052   1.492   -24.709 1.00 18.82 ? 152 VAL   B CA  1 
ATOM   3541 C  C   . VAL   B 1 140 ? 0.040   1.229   -25.811 1.00 16.55 ? 152 VAL   B C   1 
ATOM   3542 O  O   . VAL   B 1 140 ? 0.231   1.668   -26.951 1.00 14.92 ? 152 VAL   B O   1 
ATOM   3543 C  CB  . VAL   B 1 140 ? 0.995   2.959   -24.256 1.00 20.16 ? 152 VAL   B CB  1 
ATOM   3544 C  CG1 . VAL   B 1 140 ? -0.443  3.321   -23.835 1.00 18.54 ? 152 VAL   B CG1 1 
ATOM   3545 C  CG2 . VAL   B 1 140 ? 1.982   3.230   -23.144 1.00 18.12 ? 152 VAL   B CG2 1 
ATOM   3546 N  N   . TYR   B 1 141 ? -1.045  0.537   -25.482 1.00 17.72 ? 153 TYR   B N   1 
ATOM   3547 C  CA  . TYR   B 1 141 ? -2.083  0.312   -26.488 1.00 17.49 ? 153 TYR   B CA  1 
ATOM   3548 C  C   . TYR   B 1 141 ? -3.424  0.145   -25.785 1.00 19.64 ? 153 TYR   B C   1 
ATOM   3549 O  O   . TYR   B 1 141 ? -3.656  -0.847  -25.080 1.00 17.31 ? 153 TYR   B O   1 
ATOM   3550 C  CB  . TYR   B 1 141 ? -1.738  -0.888  -27.371 1.00 17.57 ? 153 TYR   B CB  1 
ATOM   3551 C  CG  . TYR   B 1 141 ? -2.649  -1.047  -28.571 1.00 18.93 ? 153 TYR   B CG  1 
ATOM   3552 C  CD1 . TYR   B 1 141 ? -2.860  -0.001  -29.453 1.00 21.61 ? 153 TYR   B CD1 1 
ATOM   3553 C  CD2 . TYR   B 1 141 ? -3.296  -2.245  -28.801 1.00 21.17 ? 153 TYR   B CD2 1 
ATOM   3554 C  CE1 . TYR   B 1 141 ? -3.712  -0.155  -30.560 1.00 20.47 ? 153 TYR   B CE1 1 
ATOM   3555 C  CE2 . TYR   B 1 141 ? -4.132  -2.414  -29.883 1.00 25.28 ? 153 TYR   B CE2 1 
ATOM   3556 C  CZ  . TYR   B 1 141 ? -4.334  -1.376  -30.758 1.00 23.58 ? 153 TYR   B CZ  1 
ATOM   3557 O  OH  . TYR   B 1 141 ? -5.183  -1.596  -31.820 1.00 25.86 ? 153 TYR   B OH  1 
ATOM   3558 N  N   . LYS   B 1 142 ? -4.285  1.143   -25.956 1.00 19.21 ? 154 LYS   B N   1 
ATOM   3559 C  CA  . LYS   B 1 142 ? -5.607  1.180   -25.344 1.00 19.34 ? 154 LYS   B CA  1 
ATOM   3560 C  C   . LYS   B 1 142 ? -5.418  1.020   -23.837 1.00 17.90 ? 154 LYS   B C   1 
ATOM   3561 O  O   . LYS   B 1 142 ? -4.571  1.715   -23.248 1.00 24.40 ? 154 LYS   B O   1 
ATOM   3562 C  CB  . LYS   B 1 142 ? -6.484  0.137   -26.016 1.00 18.30 ? 154 LYS   B CB  1 
ATOM   3563 C  CG  . LYS   B 1 142 ? -6.888  0.521   -27.449 1.00 26.08 ? 154 LYS   B CG  1 
ATOM   3564 C  CD  . LYS   B 1 142 ? -6.988  -0.693  -28.356 1.00 24.06 ? 154 LYS   B CD  1 
ATOM   3565 C  CE  . LYS   B 1 142 ? -7.509  -0.310  -29.742 1.00 30.82 ? 154 LYS   B CE  1 
ATOM   3566 N  NZ  . LYS   B 1 142 ? -6.878  0.947   -30.220 1.00 27.71 ? 154 LYS   B NZ  1 
ATOM   3567 N  N   . ASN   B 1 143 ? -6.124  0.112   -23.184 1.00 21.74 ? 155 ASN   B N   1 
ATOM   3568 C  CA  . ASN   B 1 143 ? -6.024  -0.040  -21.737 1.00 19.92 ? 155 ASN   B CA  1 
ATOM   3569 C  C   . ASN   B 1 143 ? -4.809  -0.853  -21.298 1.00 20.50 ? 155 ASN   B C   1 
ATOM   3570 O  O   . ASN   B 1 143 ? -4.605  -1.036  -20.089 1.00 20.53 ? 155 ASN   B O   1 
ATOM   3571 C  CB  . ASN   B 1 143 ? -7.291  -0.712  -21.212 1.00 20.40 ? 155 ASN   B CB  1 
ATOM   3572 C  CG  . ASN   B 1 143 ? -7.576  -2.012  -21.920 1.00 20.25 ? 155 ASN   B CG  1 
ATOM   3573 O  OD1 . ASN   B 1 143 ? -7.899  -2.014  -23.111 1.00 25.68 ? 155 ASN   B OD1 1 
ATOM   3574 N  ND2 . ASN   B 1 143 ? -7.431  -3.129  -21.212 1.00 18.55 ? 155 ASN   B ND2 1 
ATOM   3575 N  N   . LYS   B 1 144 ? -4.011  -1.343  -22.236 1.00 18.44 ? 156 LYS   B N   1 
ATOM   3576 C  CA  . LYS   B 1 144 ? -2.916  -2.266  -21.958 1.00 16.48 ? 156 LYS   B CA  1 
ATOM   3577 C  C   . LYS   B 1 144 ? -1.576  -1.542  -21.939 1.00 17.15 ? 156 LYS   B C   1 
ATOM   3578 O  O   . LYS   B 1 144 ? -1.294  -0.701  -22.800 1.00 16.25 ? 156 LYS   B O   1 
ATOM   3579 C  CB  . LYS   B 1 144 ? -2.856  -3.385  -23.007 1.00 16.49 ? 156 LYS   B CB  1 
ATOM   3580 C  CG  . LYS   B 1 144 ? -4.112  -4.238  -23.196 1.00 16.73 ? 156 LYS   B CG  1 
ATOM   3581 C  CD  . LYS   B 1 144 ? -3.743  -5.510  -23.943 1.00 21.52 ? 156 LYS   B CD  1 
ATOM   3582 C  CE  . LYS   B 1 144 ? -4.907  -6.471  -24.096 1.00 22.73 ? 156 LYS   B CE  1 
ATOM   3583 N  NZ  . LYS   B 1 144 ? -6.024  -5.866  -24.858 1.00 24.12 ? 156 LYS   B NZ  1 
ATOM   3584 N  N   . LEU   B 1 145 ? -0.753  -1.886  -20.944 1.00 15.45 ? 157 LEU   B N   1 
ATOM   3585 C  CA  . LEU   B 1 145 ? 0.688   -1.638  -20.955 1.00 14.20 ? 157 LEU   B CA  1 
ATOM   3586 C  C   . LEU   B 1 145 ? 1.368   -2.963  -21.271 1.00 15.51 ? 157 LEU   B C   1 
ATOM   3587 O  O   . LEU   B 1 145 ? 1.151   -3.956  -20.562 1.00 16.25 ? 157 LEU   B O   1 
ATOM   3588 C  CB  . LEU   B 1 145 ? 1.179   -1.109  -19.601 1.00 16.23 ? 157 LEU   B CB  1 
ATOM   3589 C  CG  . LEU   B 1 145 ? 0.490   0.118   -18.984 1.00 15.83 ? 157 LEU   B CG  1 
ATOM   3590 C  CD1 . LEU   B 1 145 ? 1.117   0.503   -17.638 1.00 21.71 ? 157 LEU   B CD1 1 
ATOM   3591 C  CD2 . LEU   B 1 145 ? 0.555   1.284   -19.956 1.00 14.90 ? 157 LEU   B CD2 1 
ATOM   3592 N  N   . ILE   B 1 146 ? 2.195   -2.980  -22.312 1.00 12.86 ? 158 ILE   B N   1 
ATOM   3593 C  CA  . ILE   B 1 146 ? 2.768   -4.211  -22.859 1.00 11.73 ? 158 ILE   B CA  1 
ATOM   3594 C  C   . ILE   B 1 146 ? 4.286   -4.120  -22.695 1.00 14.32 ? 158 ILE   B C   1 
ATOM   3595 O  O   . ILE   B 1 146 ? 4.947   -3.335  -23.388 1.00 14.05 ? 158 ILE   B O   1 
ATOM   3596 C  CB  . ILE   B 1 146 ? 2.359   -4.436  -24.331 1.00 11.13 ? 158 ILE   B CB  1 
ATOM   3597 C  CG1 . ILE   B 1 146 ? 0.828   -4.352  -24.460 1.00 13.22 ? 158 ILE   B CG1 1 
ATOM   3598 C  CG2 . ILE   B 1 146 ? 2.776   -5.824  -24.777 1.00 16.70 ? 158 ILE   B CG2 1 
ATOM   3599 C  CD1 . ILE   B 1 146 ? 0.339   -3.654  -25.716 1.00 16.49 ? 158 ILE   B CD1 1 
ATOM   3600 N  N   . PHE   B 1 147 ? 4.837   -4.915  -21.776 1.00 12.22 ? 159 PHE   B N   1 
ATOM   3601 C  CA  . PHE   B 1 147 ? 6.266   -4.891  -21.461 1.00 13.53 ? 159 PHE   B CA  1 
ATOM   3602 C  C   . PHE   B 1 147 ? 7.012   -6.015  -22.174 1.00 12.91 ? 159 PHE   B C   1 
ATOM   3603 O  O   . PHE   B 1 147 ? 6.511   -7.136  -22.283 1.00 13.12 ? 159 PHE   B O   1 
ATOM   3604 C  CB  . PHE   B 1 147 ? 6.480   -5.003  -19.935 1.00 11.91 ? 159 PHE   B CB  1 
ATOM   3605 C  CG  . PHE   B 1 147 ? 5.874   -3.871  -19.154 1.00 11.83 ? 159 PHE   B CG  1 
ATOM   3606 C  CD1 . PHE   B 1 147 ? 6.573   -2.693  -18.955 1.00 14.50 ? 159 PHE   B CD1 1 
ATOM   3607 C  CD2 . PHE   B 1 147 ? 4.586   -3.975  -18.630 1.00 14.92 ? 159 PHE   B CD2 1 
ATOM   3608 C  CE1 . PHE   B 1 147 ? 6.015   -1.643  -18.224 1.00 14.03 ? 159 PHE   B CE1 1 
ATOM   3609 C  CE2 . PHE   B 1 147 ? 4.020   -2.928  -17.919 1.00 14.36 ? 159 PHE   B CE2 1 
ATOM   3610 C  CZ  . PHE   B 1 147 ? 4.729   -1.761  -17.721 1.00 16.27 ? 159 PHE   B CZ  1 
ATOM   3611 N  N   . PHE   B 1 148 ? 8.249   -5.735  -22.607 1.00 13.21 ? 160 PHE   B N   1 
ATOM   3612 C  CA  . PHE   B 1 148 ? 9.023   -6.731  -23.343 1.00 13.28 ? 160 PHE   B CA  1 
ATOM   3613 C  C   . PHE   B 1 148 ? 10.479  -6.726  -22.899 1.00 13.96 ? 160 PHE   B C   1 
ATOM   3614 O  O   . PHE   B 1 148 ? 11.088  -5.662  -22.751 1.00 13.48 ? 160 PHE   B O   1 
ATOM   3615 C  CB  . PHE   B 1 148 ? 8.954   -6.510  -24.853 1.00 15.39 ? 160 PHE   B CB  1 
ATOM   3616 C  CG  . PHE   B 1 148 ? 9.957   -7.339  -25.618 1.00 14.68 ? 160 PHE   B CG  1 
ATOM   3617 C  CD1 . PHE   B 1 148 ? 9.812   -8.719  -25.703 1.00 15.65 ? 160 PHE   B CD1 1 
ATOM   3618 C  CD2 . PHE   B 1 148 ? 11.060  -6.743  -26.210 1.00 18.51 ? 160 PHE   B CD2 1 
ATOM   3619 C  CE1 . PHE   B 1 148 ? 10.732  -9.497  -26.402 1.00 19.01 ? 160 PHE   B CE1 1 
ATOM   3620 C  CE2 . PHE   B 1 148 ? 11.999  -7.508  -26.911 1.00 15.51 ? 160 PHE   B CE2 1 
ATOM   3621 C  CZ  . PHE   B 1 148 ? 11.841  -8.881  -27.007 1.00 14.54 ? 160 PHE   B CZ  1 
ATOM   3622 N  N   . GLY   B 1 149 ? 11.012  -7.925  -22.669 1.00 11.88 ? 161 GLY   B N   1 
ATOM   3623 C  CA  . GLY   B 1 149 ? 12.440  -8.113  -22.503 1.00 12.91 ? 161 GLY   B CA  1 
ATOM   3624 C  C   . GLY   B 1 149 ? 12.931  -7.681  -21.132 1.00 11.01 ? 161 GLY   B C   1 
ATOM   3625 O  O   . GLY   B 1 149 ? 12.163  -7.512  -20.184 1.00 12.88 ? 161 GLY   B O   1 
ATOM   3626 N  N   . GLY   B 1 150 ? 14.246  -7.526  -21.029 1.00 14.51 ? 162 GLY   B N   1 
ATOM   3627 C  CA  . GLY   B 1 150 ? 14.866  -7.001  -19.830 1.00 14.01 ? 162 GLY   B CA  1 
ATOM   3628 C  C   . GLY   B 1 150 ? 15.974  -7.891  -19.303 1.00 15.80 ? 162 GLY   B C   1 
ATOM   3629 O  O   . GLY   B 1 150 ? 16.314  -8.931  -19.869 1.00 12.26 ? 162 GLY   B O   1 
ATOM   3630 N  N   . TYR   B 1 151 ? 16.530  -7.463  -18.168 1.00 10.84 ? 163 TYR   B N   1 
ATOM   3631 C  CA  . TYR   B 1 151 ? 17.680  -8.092  -17.543 1.00 16.18 ? 163 TYR   B CA  1 
ATOM   3632 C  C   . TYR   B 1 151 ? 17.401  -8.214  -16.056 1.00 14.37 ? 163 TYR   B C   1 
ATOM   3633 O  O   . TYR   B 1 151 ? 17.033  -7.225  -15.416 1.00 17.73 ? 163 TYR   B O   1 
ATOM   3634 C  CB  . TYR   B 1 151 ? 18.936  -7.260  -17.757 1.00 13.58 ? 163 TYR   B CB  1 
ATOM   3635 C  CG  . TYR   B 1 151 ? 20.229  -7.889  -17.279 1.00 16.39 ? 163 TYR   B CG  1 
ATOM   3636 C  CD1 . TYR   B 1 151 ? 20.813  -8.934  -17.978 1.00 16.46 ? 163 TYR   B CD1 1 
ATOM   3637 C  CD2 . TYR   B 1 151 ? 20.884  -7.410  -16.142 1.00 16.74 ? 163 TYR   B CD2 1 
ATOM   3638 C  CE1 . TYR   B 1 151 ? 22.015  -9.496  -17.561 1.00 20.55 ? 163 TYR   B CE1 1 
ATOM   3639 C  CE2 . TYR   B 1 151 ? 22.096  -7.966  -15.719 1.00 16.69 ? 163 TYR   B CE2 1 
ATOM   3640 C  CZ  . TYR   B 1 151 ? 22.644  -9.011  -16.427 1.00 19.15 ? 163 TYR   B CZ  1 
ATOM   3641 O  OH  . TYR   B 1 151 ? 23.827  -9.569  -16.014 1.00 23.59 ? 163 TYR   B OH  1 
ATOM   3642 N  N   . GLY   B 1 152 ? 17.599  -9.399  -15.493 1.00 16.11 ? 164 GLY   B N   1 
ATOM   3643 C  CA  . GLY   B 1 152 ? 17.320  -9.566  -14.076 1.00 12.38 ? 164 GLY   B CA  1 
ATOM   3644 C  C   . GLY   B 1 152 ? 17.376  -11.024 -13.676 1.00 16.77 ? 164 GLY   B C   1 
ATOM   3645 O  O   . GLY   B 1 152 ? 17.893  -11.861 -14.419 1.00 17.85 ? 164 GLY   B O   1 
ATOM   3646 N  N   . TYR   B 1 153 ? 16.801  -11.319 -12.501 1.00 16.93 ? 165 TYR   B N   1 
ATOM   3647 C  CA  . TYR   B 1 153 ? 16.946  -12.641 -11.917 1.00 22.72 ? 165 TYR   B CA  1 
ATOM   3648 C  C   . TYR   B 1 153 ? 16.189  -13.691 -12.717 1.00 24.77 ? 165 TYR   B C   1 
ATOM   3649 O  O   . TYR   B 1 153 ? 15.222  -13.406 -13.443 1.00 21.26 ? 165 TYR   B O   1 
ATOM   3650 C  CB  . TYR   B 1 153 ? 16.464  -12.660 -10.462 1.00 23.19 ? 165 TYR   B CB  1 
ATOM   3651 C  CG  . TYR   B 1 153 ? 17.045  -11.528 -9.654  1.00 19.67 ? 165 TYR   B CG  1 
ATOM   3652 C  CD1 . TYR   B 1 153 ? 18.414  -11.300 -9.634  1.00 24.15 ? 165 TYR   B CD1 1 
ATOM   3653 C  CD2 . TYR   B 1 153 ? 16.223  -10.653 -8.953  1.00 22.91 ? 165 TYR   B CD2 1 
ATOM   3654 C  CE1 . TYR   B 1 153 ? 18.945  -10.256 -8.924  1.00 29.12 ? 165 TYR   B CE1 1 
ATOM   3655 C  CE2 . TYR   B 1 153 ? 16.753  -9.600  -8.233  1.00 20.58 ? 165 TYR   B CE2 1 
ATOM   3656 C  CZ  . TYR   B 1 153 ? 18.105  -9.411  -8.225  1.00 22.60 ? 165 TYR   B CZ  1 
ATOM   3657 O  OH  . TYR   B 1 153 ? 18.645  -8.365  -7.531  1.00 26.60 ? 165 TYR   B OH  1 
ATOM   3658 N  N   . LEU   B 1 154 ? 16.667  -14.925 -12.572 1.00 25.94 ? 166 LEU   B N   1 
ATOM   3659 C  CA  . LEU   B 1 154 ? 15.918  -16.084 -13.013 1.00 27.06 ? 166 LEU   B CA  1 
ATOM   3660 C  C   . LEU   B 1 154 ? 14.463  -15.935 -12.584 1.00 29.22 ? 166 LEU   B C   1 
ATOM   3661 O  O   . LEU   B 1 154 ? 14.202  -15.600 -11.421 1.00 26.90 ? 166 LEU   B O   1 
ATOM   3662 C  CB  . LEU   B 1 154 ? 16.513  -17.351 -12.403 1.00 29.41 ? 166 LEU   B CB  1 
ATOM   3663 C  CG  . LEU   B 1 154 ? 15.720  -18.601 -12.755 1.00 29.36 ? 166 LEU   B CG  1 
ATOM   3664 C  CD1 . LEU   B 1 154 ? 16.023  -18.991 -14.196 1.00 26.26 ? 166 LEU   B CD1 1 
ATOM   3665 C  CD2 . LEU   B 1 154 ? 16.017  -19.729 -11.796 1.00 28.60 ? 166 LEU   B CD2 1 
ATOM   3666 N  N   . PRO   B 1 155 ? 13.502  -16.134 -13.480 1.00 25.46 ? 167 PRO   B N   1 
ATOM   3667 C  CA  . PRO   B 1 155 ? 12.096  -16.079 -13.062 1.00 31.08 ? 167 PRO   B CA  1 
ATOM   3668 C  C   . PRO   B 1 155 ? 11.829  -17.054 -11.925 1.00 37.69 ? 167 PRO   B C   1 
ATOM   3669 O  O   . PRO   B 1 155 ? 12.248  -18.214 -11.963 1.00 35.62 ? 167 PRO   B O   1 
ATOM   3670 C  CB  . PRO   B 1 155 ? 11.332  -16.469 -14.331 1.00 30.92 ? 167 PRO   B CB  1 
ATOM   3671 C  CG  . PRO   B 1 155 ? 12.244  -16.124 -15.447 1.00 32.71 ? 167 PRO   B CG  1 
ATOM   3672 C  CD  . PRO   B 1 155 ? 13.643  -16.335 -14.931 1.00 24.63 ? 167 PRO   B CD  1 
ATOM   3673 N  N   . GLU   B 1 156 ? 11.127  -16.570 -10.896 1.00 37.09 ? 168 GLU   B N   1 
ATOM   3674 C  CA  . GLU   B 1 156 ? 10.736  -17.437 -9.792  1.00 40.62 ? 168 GLU   B CA  1 
ATOM   3675 C  C   . GLU   B 1 156 ? 9.821   -18.555 -10.266 1.00 43.91 ? 168 GLU   B C   1 
ATOM   3676 O  O   . GLU   B 1 156 ? 9.763   -19.615 -9.632  1.00 46.46 ? 168 GLU   B O   1 
ATOM   3677 C  CB  . GLU   B 1 156 ? 10.049  -16.614 -8.699  1.00 44.22 ? 168 GLU   B CB  1 
ATOM   3678 C  CG  . GLU   B 1 156 ? 10.847  -15.397 -8.232  1.00 43.62 ? 168 GLU   B CG  1 
ATOM   3679 C  CD  . GLU   B 1 156 ? 12.030  -15.760 -7.340  1.00 50.95 ? 168 GLU   B CD  1 
ATOM   3680 O  OE1 . GLU   B 1 156 ? 11.812  -16.415 -6.294  1.00 48.89 ? 168 GLU   B OE1 1 
ATOM   3681 O  OE2 . GLU   B 1 156 ? 13.178  -15.391 -7.686  1.00 46.31 ? 168 GLU   B OE2 1 
ATOM   3682 N  N   . ASP   B 1 157 ? 9.129   -18.344 -11.381 1.00 44.45 ? 169 ASP   B N   1 
ATOM   3683 C  CA  . ASP   B 1 157 ? 8.215   -19.315 -11.952 1.00 46.62 ? 169 ASP   B CA  1 
ATOM   3684 C  C   . ASP   B 1 157 ? 8.462   -19.415 -13.449 1.00 46.69 ? 169 ASP   B C   1 
ATOM   3685 O  O   . ASP   B 1 157 ? 8.710   -18.405 -14.113 1.00 43.48 ? 169 ASP   B O   1 
ATOM   3686 C  CB  . ASP   B 1 157 ? 6.762   -18.915 -11.677 1.00 46.15 ? 169 ASP   B CB  1 
ATOM   3687 C  CG  . ASP   B 1 157 ? 5.771   -19.787 -12.407 1.00 51.41 ? 169 ASP   B CG  1 
ATOM   3688 O  OD1 . ASP   B 1 157 ? 5.594   -20.956 -11.996 1.00 50.94 ? 169 ASP   B OD1 1 
ATOM   3689 O  OD2 . ASP   B 1 157 ? 5.177   -19.304 -13.397 1.00 49.75 ? 169 ASP   B OD2 1 
ATOM   3690 N  N   . LYS   B 1 158 ? 8.404   -20.639 -13.972 1.00 50.86 ? 170 LYS   B N   1 
ATOM   3691 C  CA  . LYS   B 1 158 ? 8.487   -20.862 -15.411 1.00 47.46 ? 170 LYS   B CA  1 
ATOM   3692 C  C   . LYS   B 1 158 ? 7.236   -20.313 -16.090 1.00 45.01 ? 170 LYS   B C   1 
ATOM   3693 O  O   . LYS   B 1 158 ? 6.117   -20.707 -15.748 1.00 47.15 ? 170 LYS   B O   1 
ATOM   3694 C  CB  . LYS   B 1 158 ? 8.653   -22.355 -15.690 1.00 48.76 ? 170 LYS   B CB  1 
ATOM   3695 C  CG  . LYS   B 1 158 ? 8.147   -22.826 -17.044 1.00 46.15 ? 170 LYS   B CG  1 
ATOM   3696 C  CD  . LYS   B 1 158 ? 9.139   -22.524 -18.135 1.00 45.83 ? 170 LYS   B CD  1 
ATOM   3697 C  CE  . LYS   B 1 158 ? 8.792   -23.254 -19.424 1.00 43.63 ? 170 LYS   B CE  1 
ATOM   3698 N  NZ  . LYS   B 1 158 ? 9.628   -22.744 -20.553 1.00 32.11 ? 170 LYS   B NZ  1 
ATOM   3699 N  N   . VAL   B 1 159 ? 7.426   -19.406 -17.051 1.00 45.39 ? 171 VAL   B N   1 
ATOM   3700 C  CA  . VAL   B 1 159 ? 6.346   -18.717 -17.748 1.00 41.91 ? 171 VAL   B CA  1 
ATOM   3701 C  C   . VAL   B 1 159 ? 6.590   -18.802 -19.253 1.00 37.30 ? 171 VAL   B C   1 
ATOM   3702 O  O   . VAL   B 1 159 ? 7.534   -19.441 -19.713 1.00 37.34 ? 171 VAL   B O   1 
ATOM   3703 C  CB  . VAL   B 1 159 ? 6.210   -17.248 -17.300 1.00 42.31 ? 171 VAL   B CB  1 
ATOM   3704 C  CG1 . VAL   B 1 159 ? 5.817   -17.180 -15.832 1.00 48.32 ? 171 VAL   B CG1 1 
ATOM   3705 C  CG2 . VAL   B 1 159 ? 7.510   -16.495 -17.549 1.00 35.45 ? 171 VAL   B CG2 1 
ATOM   3706 N  N   . LEU   B 1 160 ? 5.725   -18.137 -20.022 1.00 29.07 ? 172 LEU   B N   1 
ATOM   3707 C  CA  . LEU   B 1 160 ? 5.827   -18.173 -21.478 1.00 30.86 ? 172 LEU   B CA  1 
ATOM   3708 C  C   . LEU   B 1 160 ? 7.030   -17.359 -21.939 1.00 27.63 ? 172 LEU   B C   1 
ATOM   3709 O  O   . LEU   B 1 160 ? 7.128   -16.161 -21.654 1.00 24.98 ? 172 LEU   B O   1 
ATOM   3710 C  CB  . LEU   B 1 160 ? 4.550   -17.636 -22.121 1.00 30.40 ? 172 LEU   B CB  1 
ATOM   3711 C  CG  . LEU   B 1 160 ? 3.239   -18.384 -21.859 1.00 31.43 ? 172 LEU   B CG  1 
ATOM   3712 C  CD1 . LEU   B 1 160 ? 2.079   -17.603 -22.440 1.00 31.93 ? 172 LEU   B CD1 1 
ATOM   3713 C  CD2 . LEU   B 1 160 ? 3.282   -19.791 -22.440 1.00 34.63 ? 172 LEU   B CD2 1 
ATOM   3714 N  N   . GLY   B 1 161 ? 7.930   -17.995 -22.663 1.00 26.77 ? 173 GLY   B N   1 
ATOM   3715 C  CA  . GLY   B 1 161 ? 9.098   -17.327 -23.195 1.00 24.63 ? 173 GLY   B CA  1 
ATOM   3716 C  C   . GLY   B 1 161 ? 10.368  -17.995 -22.721 1.00 25.25 ? 173 GLY   B C   1 
ATOM   3717 O  O   . GLY   B 1 161 ? 10.359  -19.094 -22.160 1.00 27.58 ? 173 GLY   B O   1 
ATOM   3718 N  N   . THR   B 1 162 ? 11.481  -17.312 -22.943 1.00 24.01 ? 174 THR   B N   1 
ATOM   3719 C  CA  . THR   B 1 162 ? 12.780  -17.886 -22.643 1.00 22.88 ? 174 THR   B CA  1 
ATOM   3720 C  C   . THR   B 1 162 ? 13.644  -16.895 -21.877 1.00 23.34 ? 174 THR   B C   1 
ATOM   3721 O  O   . THR   B 1 162 ? 13.534  -15.674 -22.037 1.00 22.69 ? 174 THR   B O   1 
ATOM   3722 C  CB  . THR   B 1 162 ? 13.505  -18.327 -23.924 1.00 26.99 ? 174 THR   B CB  1 
ATOM   3723 O  OG1 . THR   B 1 162 ? 13.749  -17.187 -24.746 1.00 23.27 ? 174 THR   B OG1 1 
ATOM   3724 C  CG2 . THR   B 1 162 ? 12.668  -19.337 -24.697 1.00 25.25 ? 174 THR   B CG2 1 
ATOM   3725 N  N   . PHE   B 1 163 ? 14.513  -17.452 -21.048 1.00 22.36 ? 175 PHE   B N   1 
ATOM   3726 C  CA  . PHE   B 1 163 ? 15.451  -16.705 -20.232 1.00 22.92 ? 175 PHE   B CA  1 
ATOM   3727 C  C   . PHE   B 1 163 ? 16.830  -17.301 -20.453 1.00 22.98 ? 175 PHE   B C   1 
ATOM   3728 O  O   . PHE   B 1 163 ? 16.976  -18.525 -20.550 1.00 23.34 ? 175 PHE   B O   1 
ATOM   3729 C  CB  . PHE   B 1 163 ? 15.040  -16.761 -18.748 1.00 22.49 ? 175 PHE   B CB  1 
ATOM   3730 C  CG  . PHE   B 1 163 ? 16.066  -16.209 -17.801 1.00 21.95 ? 175 PHE   B CG  1 
ATOM   3731 C  CD1 . PHE   B 1 163 ? 17.064  -17.021 -17.286 1.00 24.93 ? 175 PHE   B CD1 1 
ATOM   3732 C  CD2 . PHE   B 1 163 ? 16.014  -14.885 -17.406 1.00 20.76 ? 175 PHE   B CD2 1 
ATOM   3733 C  CE1 . PHE   B 1 163 ? 18.006  -16.519 -16.413 1.00 21.42 ? 175 PHE   B CE1 1 
ATOM   3734 C  CE2 . PHE   B 1 163 ? 16.951  -14.368 -16.527 1.00 19.25 ? 175 PHE   B CE2 1 
ATOM   3735 C  CZ  . PHE   B 1 163 ? 17.948  -15.190 -16.032 1.00 23.59 ? 175 PHE   B CZ  1 
ATOM   3736 N  N   . GLU   B 1 164 ? 17.831  -16.431 -20.560 1.00 22.95 ? 176 GLU   B N   1 
ATOM   3737 C  CA  . GLU   B 1 164 ? 19.195  -16.828 -20.887 1.00 24.64 ? 176 GLU   B CA  1 
ATOM   3738 C  C   . GLU   B 1 164 ? 20.147  -16.179 -19.894 1.00 22.79 ? 176 GLU   B C   1 
ATOM   3739 O  O   . GLU   B 1 164 ? 20.215  -14.949 -19.811 1.00 18.41 ? 176 GLU   B O   1 
ATOM   3740 C  CB  . GLU   B 1 164 ? 19.568  -16.419 -22.315 1.00 25.36 ? 176 GLU   B CB  1 
ATOM   3741 C  CG  . GLU   B 1 164 ? 21.011  -16.692 -22.642 1.00 29.02 ? 176 GLU   B CG  1 
ATOM   3742 C  CD  . GLU   B 1 164 ? 21.322  -18.163 -22.604 1.00 32.36 ? 176 GLU   B CD  1 
ATOM   3743 O  OE1 . GLU   B 1 164 ? 20.511  -18.955 -23.144 1.00 32.14 ? 176 GLU   B OE1 1 
ATOM   3744 O  OE2 . GLU   B 1 164 ? 22.371  -18.524 -22.021 1.00 37.15 ? 176 GLU   B OE2 1 
ATOM   3745 N  N   . PHE   B 1 165 ? 20.882  -16.999 -19.152 1.00 25.50 ? 177 PHE   B N   1 
ATOM   3746 C  CA  . PHE   B 1 165 ? 21.780  -16.463 -18.140 1.00 24.16 ? 177 PHE   B CA  1 
ATOM   3747 C  C   . PHE   B 1 165 ? 22.947  -15.715 -18.772 1.00 24.91 ? 177 PHE   B C   1 
ATOM   3748 O  O   . PHE   B 1 165 ? 23.474  -16.108 -19.818 1.00 23.52 ? 177 PHE   B O   1 
ATOM   3749 C  CB  . PHE   B 1 165 ? 22.302  -17.580 -17.244 1.00 25.55 ? 177 PHE   B CB  1 
ATOM   3750 C  CG  . PHE   B 1 165 ? 21.490  -17.782 -15.993 1.00 22.84 ? 177 PHE   B CG  1 
ATOM   3751 C  CD1 . PHE   B 1 165 ? 21.393  -16.773 -15.043 1.00 25.48 ? 177 PHE   B CD1 1 
ATOM   3752 C  CD2 . PHE   B 1 165 ? 20.845  -18.980 -15.759 1.00 25.36 ? 177 PHE   B CD2 1 
ATOM   3753 C  CE1 . PHE   B 1 165 ? 20.659  -16.952 -13.881 1.00 24.03 ? 177 PHE   B CE1 1 
ATOM   3754 C  CE2 . PHE   B 1 165 ? 20.106  -19.171 -14.598 1.00 27.07 ? 177 PHE   B CE2 1 
ATOM   3755 C  CZ  . PHE   B 1 165 ? 20.013  -18.152 -13.659 1.00 26.87 ? 177 PHE   B CZ  1 
ATOM   3756 N  N   . ASP   B 1 166 ? 23.320  -14.608 -18.138 1.00 23.18 ? 178 ASP   B N   1 
ATOM   3757 C  CA  . ASP   B 1 166 ? 24.566  -13.902 -18.418 1.00 28.75 ? 178 ASP   B CA  1 
ATOM   3758 C  C   . ASP   B 1 166 ? 25.629  -14.524 -17.519 1.00 28.91 ? 178 ASP   B C   1 
ATOM   3759 O  O   . ASP   B 1 166 ? 25.604  -14.340 -16.299 1.00 27.95 ? 178 ASP   B O   1 
ATOM   3760 C  CB  . ASP   B 1 166 ? 24.396  -12.406 -18.149 1.00 22.29 ? 178 ASP   B CB  1 
ATOM   3761 C  CG  . ASP   B 1 166 ? 25.650  -11.595 -18.421 1.00 26.44 ? 178 ASP   B CG  1 
ATOM   3762 O  OD1 . ASP   B 1 166 ? 26.679  -12.160 -18.853 1.00 29.34 ? 178 ASP   B OD1 1 
ATOM   3763 O  OD2 . ASP   B 1 166 ? 25.601  -10.370 -18.187 1.00 25.06 ? 178 ASP   B OD2 1 
ATOM   3764 N  N   . GLU   B 1 167 ? 26.551  -15.281 -18.116 1.00 30.53 ? 179 GLU   B N   1 
ATOM   3765 C  CA  . GLU   B 1 167 ? 27.487  -16.047 -17.300 1.00 29.61 ? 179 GLU   B CA  1 
ATOM   3766 C  C   . GLU   B 1 167 ? 28.400  -15.141 -16.482 1.00 30.79 ? 179 GLU   B C   1 
ATOM   3767 O  O   . GLU   B 1 167 ? 28.860  -15.542 -15.410 1.00 33.55 ? 179 GLU   B O   1 
ATOM   3768 C  CB  . GLU   B 1 167 ? 28.304  -16.993 -18.183 1.00 32.53 ? 179 GLU   B CB  1 
ATOM   3769 C  CG  . GLU   B 1 167 ? 29.089  -16.300 -19.278 1.00 35.08 ? 179 GLU   B CG  1 
ATOM   3770 C  CD  . GLU   B 1 167 ? 29.949  -17.267 -20.081 1.00 42.16 ? 179 GLU   B CD  1 
ATOM   3771 O  OE1 . GLU   B 1 167 ? 29.871  -18.489 -19.824 1.00 38.42 ? 179 GLU   B OE1 1 
ATOM   3772 O  OE2 . GLU   B 1 167 ? 30.705  -16.800 -20.964 1.00 43.13 ? 179 GLU   B OE2 1 
ATOM   3773 N  N   . THR   B 1 168 ? 28.659  -13.914 -16.950 1.00 29.28 ? 180 THR   B N   1 
ATOM   3774 C  CA  . THR   B 1 168 ? 29.507  -13.007 -16.183 1.00 33.32 ? 180 THR   B CA  1 
ATOM   3775 C  C   . THR   B 1 168 ? 28.897  -12.658 -14.827 1.00 36.49 ? 180 THR   B C   1 
ATOM   3776 O  O   . THR   B 1 168 ? 29.634  -12.300 -13.899 1.00 37.85 ? 180 THR   B O   1 
ATOM   3777 C  CB  . THR   B 1 168 ? 29.788  -11.725 -16.979 1.00 29.64 ? 180 THR   B CB  1 
ATOM   3778 O  OG1 . THR   B 1 168 ? 28.582  -10.971 -17.147 1.00 29.38 ? 180 THR   B OG1 1 
ATOM   3779 C  CG2 . THR   B 1 168 ? 30.369  -12.056 -18.349 1.00 34.54 ? 180 THR   B CG2 1 
ATOM   3780 N  N   . SER   B 1 169 ? 27.575  -12.780 -14.685 1.00 30.29 ? 181 SER   B N   1 
ATOM   3781 C  CA  . SER   B 1 169 ? 26.895  -12.452 -13.438 1.00 34.95 ? 181 SER   B CA  1 
ATOM   3782 C  C   . SER   B 1 169 ? 27.093  -13.500 -12.349 1.00 38.21 ? 181 SER   B C   1 
ATOM   3783 O  O   . SER   B 1 169 ? 26.734  -13.247 -11.198 1.00 39.61 ? 181 SER   B O   1 
ATOM   3784 C  CB  . SER   B 1 169 ? 25.393  -12.268 -13.691 1.00 30.97 ? 181 SER   B CB  1 
ATOM   3785 O  OG  . SER   B 1 169 ? 24.804  -13.485 -14.117 1.00 23.37 ? 181 SER   B OG  1 
ATOM   3786 N  N   . PHE   B 1 170 ? 27.616  -14.679 -12.678 1.00 36.99 ? 182 PHE   B N   1 
ATOM   3787 C  CA  . PHE   B 1 170 ? 27.888  -15.659 -11.632 1.00 38.17 ? 182 PHE   B CA  1 
ATOM   3788 C  C   . PHE   B 1 170 ? 29.157  -15.321 -10.864 1.00 43.19 ? 182 PHE   B C   1 
ATOM   3789 O  O   . PHE   B 1 170 ? 29.223  -15.534 -9.650  1.00 45.12 ? 182 PHE   B O   1 
ATOM   3790 C  CB  . PHE   B 1 170 ? 27.979  -17.061 -12.229 1.00 33.16 ? 182 PHE   B CB  1 
ATOM   3791 C  CG  . PHE   B 1 170 ? 26.641  -17.637 -12.612 1.00 32.32 ? 182 PHE   B CG  1 
ATOM   3792 C  CD1 . PHE   B 1 170 ? 26.032  -17.270 -13.804 1.00 32.90 ? 182 PHE   B CD1 1 
ATOM   3793 C  CD2 . PHE   B 1 170 ? 25.989  -18.538 -11.776 1.00 29.02 ? 182 PHE   B CD2 1 
ATOM   3794 C  CE1 . PHE   B 1 170 ? 24.791  -17.786 -14.156 1.00 30.08 ? 182 PHE   B CE1 1 
ATOM   3795 C  CE2 . PHE   B 1 170 ? 24.757  -19.065 -12.121 1.00 31.36 ? 182 PHE   B CE2 1 
ATOM   3796 C  CZ  . PHE   B 1 170 ? 24.153  -18.687 -13.321 1.00 28.48 ? 182 PHE   B CZ  1 
ATOM   3797 N  N   . TRP   B 1 171 ? 30.171  -14.797 -11.550 1.00 45.47 ? 183 TRP   B N   1 
ATOM   3798 C  CA  . TRP   B 1 171 ? 31.424  -14.470 -10.878 1.00 51.24 ? 183 TRP   B CA  1 
ATOM   3799 C  C   . TRP   B 1 171 ? 31.266  -13.239 -9.992  1.00 53.87 ? 183 TRP   B C   1 
ATOM   3800 O  O   . TRP   B 1 171 ? 31.414  -13.315 -8.766  1.00 51.55 ? 183 TRP   B O   1 
ATOM   3801 C  CB  . TRP   B 1 171 ? 32.530  -14.261 -11.916 1.00 47.20 ? 183 TRP   B CB  1 
ATOM   3802 N  N   . ASN   B 1 172 ? 30.932  -12.097 -10.598 1.00 55.51 ? 184 ASN   B N   1 
ATOM   3803 C  CA  . ASN   B 1 172 ? 30.916  -10.825 -9.880  1.00 61.20 ? 184 ASN   B CA  1 
ATOM   3804 C  C   . ASN   B 1 172 ? 29.680  -10.690 -8.997  1.00 64.13 ? 184 ASN   B C   1 
ATOM   3805 O  O   . ASN   B 1 172 ? 29.790  -10.507 -7.779  1.00 67.67 ? 184 ASN   B O   1 
ATOM   3806 C  CB  . ASN   B 1 172 ? 30.990  -9.664  -10.877 1.00 66.67 ? 184 ASN   B CB  1 
ATOM   3807 N  N   . SER   B 1 173 ? 28.496  -10.758 -9.599  1.00 63.18 ? 185 SER   B N   1 
ATOM   3808 C  CA  . SER   B 1 173 ? 27.268  -10.625 -8.829  1.00 62.18 ? 185 SER   B CA  1 
ATOM   3809 C  C   . SER   B 1 173 ? 27.141  -11.774 -7.837  1.00 59.09 ? 185 SER   B C   1 
ATOM   3810 O  O   . SER   B 1 173 ? 27.563  -12.903 -8.100  1.00 56.07 ? 185 SER   B O   1 
ATOM   3811 C  CB  . SER   B 1 173 ? 26.050  -10.600 -9.757  1.00 55.50 ? 185 SER   B CB  1 
ATOM   3812 O  OG  . SER   B 1 173 ? 26.277  -9.811  -10.912 1.00 50.28 ? 185 SER   B OG  1 
ATOM   3813 N  N   . SER   B 1 174 ? 26.571  -11.469 -6.669  1.00 62.29 ? 186 SER   B N   1 
ATOM   3814 C  CA  . SER   B 1 174 ? 26.222  -12.532 -5.734  1.00 60.93 ? 186 SER   B CA  1 
ATOM   3815 C  C   . SER   B 1 174 ? 24.996  -13.295 -6.212  1.00 57.06 ? 186 SER   B C   1 
ATOM   3816 O  O   . SER   B 1 174 ? 24.829  -14.474 -5.877  1.00 55.28 ? 186 SER   B O   1 
ATOM   3817 C  CB  . SER   B 1 174 ? 25.981  -11.959 -4.337  1.00 64.13 ? 186 SER   B CB  1 
ATOM   3818 O  OG  . SER   B 1 174 ? 24.779  -11.210 -4.294  1.00 64.80 ? 186 SER   B OG  1 
ATOM   3819 N  N   . HIS   B 1 175 ? 24.135  -12.639 -6.988  1.00 52.89 ? 187 HIS   B N   1 
ATOM   3820 C  CA  . HIS   B 1 175 ? 22.954  -13.253 -7.578  1.00 47.59 ? 187 HIS   B CA  1 
ATOM   3821 C  C   . HIS   B 1 175 ? 23.068  -13.180 -9.094  1.00 41.24 ? 187 HIS   B C   1 
ATOM   3822 O  O   . HIS   B 1 175 ? 23.245  -12.077 -9.643  1.00 39.52 ? 187 HIS   B O   1 
ATOM   3823 C  CB  . HIS   B 1 175 ? 21.677  -12.555 -7.102  1.00 44.81 ? 187 HIS   B CB  1 
ATOM   3824 C  CG  . HIS   B 1 175 ? 20.609  -13.501 -6.651  1.00 46.53 ? 187 HIS   B CG  1 
ATOM   3825 N  ND1 . HIS   B 1 175 ? 20.138  -14.524 -7.445  1.00 44.77 ? 187 HIS   B ND1 1 
ATOM   3826 C  CD2 . HIS   B 1 175 ? 19.924  -13.581 -5.486  1.00 50.50 ? 187 HIS   B CD2 1 
ATOM   3827 C  CE1 . HIS   B 1 175 ? 19.206  -15.193 -6.789  1.00 51.75 ? 187 HIS   B CE1 1 
ATOM   3828 N  NE2 . HIS   B 1 175 ? 19.056  -14.640 -5.598  1.00 53.62 ? 187 HIS   B NE2 1 
ATOM   3829 N  N   . PRO   B 1 176 ? 22.994  -14.296 -9.810  1.00 34.00 ? 188 PRO   B N   1 
ATOM   3830 C  CA  . PRO   B 1 176 ? 23.133  -14.246 -11.267 1.00 32.42 ? 188 PRO   B CA  1 
ATOM   3831 C  C   . PRO   B 1 176 ? 21.901  -13.644 -11.922 1.00 29.28 ? 188 PRO   B C   1 
ATOM   3832 O  O   . PRO   B 1 176 ? 20.793  -13.650 -11.374 1.00 26.02 ? 188 PRO   B O   1 
ATOM   3833 C  CB  . PRO   B 1 176 ? 23.310  -15.715 -11.660 1.00 33.67 ? 188 PRO   B CB  1 
ATOM   3834 C  CG  . PRO   B 1 176 ? 22.607  -16.467 -10.595 1.00 33.96 ? 188 PRO   B CG  1 
ATOM   3835 C  CD  . PRO   B 1 176 ? 22.754  -15.665 -9.324  1.00 39.98 ? 188 PRO   B CD  1 
ATOM   3836 N  N   . ARG   B 1 177 ? 22.115  -13.110 -13.122 1.00 27.26 ? 189 ARG   B N   1 
ATOM   3837 C  CA  . ARG   B 1 177 ? 21.054  -12.485 -13.893 1.00 19.13 ? 189 ARG   B CA  1 
ATOM   3838 C  C   . ARG   B 1 177 ? 21.204  -12.875 -15.357 1.00 23.39 ? 189 ARG   B C   1 
ATOM   3839 O  O   . ARG   B 1 177 ? 22.244  -13.374 -15.786 1.00 18.41 ? 189 ARG   B O   1 
ATOM   3840 C  CB  . ARG   B 1 177 ? 21.066  -10.958 -13.723 1.00 24.22 ? 189 ARG   B CB  1 
ATOM   3841 C  CG  . ARG   B 1 177 ? 20.830  -10.527 -12.274 1.00 26.19 ? 189 ARG   B CG  1 
ATOM   3842 C  CD  . ARG   B 1 177 ? 20.748  -9.020  -12.095 1.00 24.92 ? 189 ARG   B CD  1 
ATOM   3843 N  NE  . ARG   B 1 177 ? 22.062  -8.393  -12.072 1.00 31.23 ? 189 ARG   B NE  1 
ATOM   3844 C  CZ  . ARG   B 1 177 ? 22.249  -7.084  -11.991 1.00 32.86 ? 189 ARG   B CZ  1 
ATOM   3845 N  NH1 . ARG   B 1 177 ? 21.226  -6.248  -11.927 1.00 25.46 ? 189 ARG   B NH1 1 
ATOM   3846 N  NH2 . ARG   B 1 177 ? 23.491  -6.602  -11.986 1.00 34.05 ? 189 ARG   B NH2 1 
ATOM   3847 N  N   . GLY   B 1 178 ? 20.133  -12.658 -16.115 1.00 21.53 ? 190 GLY   B N   1 
ATOM   3848 C  CA  . GLY   B 1 178 ? 20.134  -12.966 -17.530 1.00 20.34 ? 190 GLY   B CA  1 
ATOM   3849 C  C   . GLY   B 1 178 ? 19.113  -12.119 -18.254 1.00 17.97 ? 190 GLY   B C   1 
ATOM   3850 O  O   . GLY   B 1 178 ? 18.448  -11.268 -17.658 1.00 18.17 ? 190 GLY   B O   1 
ATOM   3851 N  N   . TRP   B 1 179 ? 19.014  -12.364 -19.561 1.00 18.92 ? 191 TRP   B N   1 
ATOM   3852 C  CA  . TRP   B 1 179 ? 18.114  -11.676 -20.477 1.00 12.58 ? 191 TRP   B CA  1 
ATOM   3853 C  C   . TRP   B 1 179 ? 16.864  -12.516 -20.716 1.00 14.82 ? 191 TRP   B C   1 
ATOM   3854 O  O   . TRP   B 1 179 ? 16.902  -13.745 -20.662 1.00 15.99 ? 191 TRP   B O   1 
ATOM   3855 C  CB  . TRP   B 1 179 ? 18.810  -11.417 -21.833 1.00 15.47 ? 191 TRP   B CB  1 
ATOM   3856 C  CG  . TRP   B 1 179 ? 20.086  -10.622 -21.721 1.00 16.03 ? 191 TRP   B CG  1 
ATOM   3857 C  CD1 . TRP   B 1 179 ? 20.208  -9.256  -21.649 1.00 14.46 ? 191 TRP   B CD1 1 
ATOM   3858 C  CD2 . TRP   B 1 179 ? 21.420  -11.145 -21.680 1.00 18.49 ? 191 TRP   B CD2 1 
ATOM   3859 N  NE1 . TRP   B 1 179 ? 21.539  -8.904  -21.543 1.00 17.72 ? 191 TRP   B NE1 1 
ATOM   3860 C  CE2 . TRP   B 1 179 ? 22.302  -10.044 -21.572 1.00 19.62 ? 191 TRP   B CE2 1 
ATOM   3861 C  CE3 . TRP   B 1 179 ? 21.956  -12.439 -21.699 1.00 22.63 ? 191 TRP   B CE3 1 
ATOM   3862 C  CZ2 . TRP   B 1 179 ? 23.696  -10.200 -21.486 1.00 19.42 ? 191 TRP   B CZ2 1 
ATOM   3863 C  CZ3 . TRP   B 1 179 ? 23.344  -12.591 -21.634 1.00 19.69 ? 191 TRP   B CZ3 1 
ATOM   3864 C  CH2 . TRP   B 1 179 ? 24.192  -11.478 -21.525 1.00 17.75 ? 191 TRP   B CH2 1 
ATOM   3865 N  N   . ASN   B 1 180 ? 15.755  -11.841 -21.015 1.00 15.15 ? 192 ASN   B N   1 
ATOM   3866 C  CA  . ASN   B 1 180 ? 14.524  -12.536 -21.343 1.00 12.58 ? 192 ASN   B CA  1 
ATOM   3867 C  C   . ASN   B 1 180 ? 13.879  -11.900 -22.567 1.00 15.53 ? 192 ASN   B C   1 
ATOM   3868 O  O   . ASN   B 1 180 ? 14.139  -10.741 -22.906 1.00 13.89 ? 192 ASN   B O   1 
ATOM   3869 C  CB  . ASN   B 1 180 ? 13.540  -12.517 -20.166 1.00 15.96 ? 192 ASN   B CB  1 
ATOM   3870 C  CG  . ASN   B 1 180 ? 12.893  -11.164 -19.988 1.00 14.71 ? 192 ASN   B CG  1 
ATOM   3871 O  OD1 . ASN   B 1 180 ? 11.922  -10.852 -20.667 1.00 14.90 ? 192 ASN   B OD1 1 
ATOM   3872 N  ND2 . ASN   B 1 180 ? 13.433  -10.345 -19.074 1.00 13.14 ? 192 ASN   B ND2 1 
ATOM   3873 N  N   . ASP   B 1 181 ? 13.019  -12.687 -23.222 1.00 14.80 ? 193 ASP   B N   1 
ATOM   3874 C  CA  . ASP   B 1 181 ? 12.216  -12.226 -24.346 1.00 16.10 ? 193 ASP   B CA  1 
ATOM   3875 C  C   . ASP   B 1 181 ? 10.736  -12.152 -23.993 1.00 16.40 ? 193 ASP   B C   1 
ATOM   3876 O  O   . ASP   B 1 181 ? 9.888   -12.194 -24.889 1.00 16.59 ? 193 ASP   B O   1 
ATOM   3877 C  CB  . ASP   B 1 181 ? 12.418  -13.132 -25.577 1.00 18.34 ? 193 ASP   B CB  1 
ATOM   3878 C  CG  . ASP   B 1 181 ? 11.865  -14.560 -25.360 1.00 22.70 ? 193 ASP   B CG  1 
ATOM   3879 O  OD1 . ASP   B 1 181 ? 11.229  -14.837 -24.310 1.00 19.59 ? 193 ASP   B OD1 1 
ATOM   3880 O  OD2 . ASP   B 1 181 ? 12.066  -15.422 -26.234 1.00 23.99 ? 193 ASP   B OD2 1 
ATOM   3881 N  N   . HIS   B 1 182 ? 10.405  -12.056 -22.705 1.00 17.46 ? 194 HIS   B N   1 
ATOM   3882 C  CA  . HIS   B 1 182 ? 9.016   -12.173 -22.276 1.00 18.13 ? 194 HIS   B CA  1 
ATOM   3883 C  C   . HIS   B 1 182 ? 8.165   -10.986 -22.715 1.00 16.82 ? 194 HIS   B C   1 
ATOM   3884 O  O   . HIS   B 1 182 ? 8.612   -9.834  -22.732 1.00 14.30 ? 194 HIS   B O   1 
ATOM   3885 C  CB  . HIS   B 1 182 ? 8.935   -12.287 -20.763 1.00 19.56 ? 194 HIS   B CB  1 
ATOM   3886 C  CG  . HIS   B 1 182 ? 9.692   -13.444 -20.202 1.00 22.97 ? 194 HIS   B CG  1 
ATOM   3887 N  ND1 . HIS   B 1 182 ? 9.989   -13.551 -18.860 1.00 22.44 ? 194 HIS   B ND1 1 
ATOM   3888 C  CD2 . HIS   B 1 182 ? 10.202  -14.550 -20.793 1.00 20.43 ? 194 HIS   B CD2 1 
ATOM   3889 C  CE1 . HIS   B 1 182 ? 10.658  -14.671 -18.650 1.00 23.91 ? 194 HIS   B CE1 1 
ATOM   3890 N  NE2 . HIS   B 1 182 ? 10.798  -15.296 -19.807 1.00 22.09 ? 194 HIS   B NE2 1 
ATOM   3891 N  N   . VAL   B 1 183 ? 6.904   -11.277 -23.035 1.00 16.38 ? 195 VAL   B N   1 
ATOM   3892 C  CA  . VAL   B 1 183 ? 5.873   -10.262 -23.219 1.00 15.14 ? 195 VAL   B CA  1 
ATOM   3893 C  C   . VAL   B 1 183 ? 4.890   -10.396 -22.065 1.00 19.25 ? 195 VAL   B C   1 
ATOM   3894 O  O   . VAL   B 1 183 ? 4.390   -11.496 -21.802 1.00 17.62 ? 195 VAL   B O   1 
ATOM   3895 C  CB  . VAL   B 1 183 ? 5.162   -10.409 -24.580 1.00 13.80 ? 195 VAL   B CB  1 
ATOM   3896 C  CG1 . VAL   B 1 183 ? 4.106   -9.349  -24.733 1.00 13.58 ? 195 VAL   B CG1 1 
ATOM   3897 C  CG2 . VAL   B 1 183 ? 6.186   -10.273 -25.723 1.00 15.06 ? 195 VAL   B CG2 1 
ATOM   3898 N  N   . HIS   B 1 184 ? 4.640   -9.292  -21.356 1.00 15.07 ? 196 HIS   B N   1 
ATOM   3899 C  CA  . HIS   B 1 184 ? 3.623   -9.243  -20.309 1.00 17.26 ? 196 HIS   B CA  1 
ATOM   3900 C  C   . HIS   B 1 184 ? 2.683   -8.073  -20.548 1.00 14.60 ? 196 HIS   B C   1 
ATOM   3901 O  O   . HIS   B 1 184 ? 3.113   -6.989  -20.937 1.00 14.32 ? 196 HIS   B O   1 
ATOM   3902 C  CB  . HIS   B 1 184 ? 4.245   -9.096  -18.903 1.00 14.09 ? 196 HIS   B CB  1 
ATOM   3903 C  CG  . HIS   B 1 184 ? 4.870   -10.348 -18.374 1.00 16.90 ? 196 HIS   B CG  1 
ATOM   3904 N  ND1 . HIS   B 1 184 ? 6.133   -10.755 -18.738 1.00 16.59 ? 196 HIS   B ND1 1 
ATOM   3905 C  CD2 . HIS   B 1 184 ? 4.419   -11.268 -17.489 1.00 20.39 ? 196 HIS   B CD2 1 
ATOM   3906 C  CE1 . HIS   B 1 184 ? 6.431   -11.878 -18.108 1.00 22.25 ? 196 HIS   B CE1 1 
ATOM   3907 N  NE2 . HIS   B 1 184 ? 5.404   -12.217 -17.353 1.00 18.76 ? 196 HIS   B NE2 1 
ATOM   3908 N  N   . ILE   B 1 185 ? 1.400   -8.284  -20.268 1.00 18.24 ? 197 ILE   B N   1 
ATOM   3909 C  CA  . ILE   B 1 185 ? 0.377   -7.249  -20.333 1.00 14.09 ? 197 ILE   B CA  1 
ATOM   3910 C  C   . ILE   B 1 185 ? 0.007   -6.857  -18.907 1.00 14.44 ? 197 ILE   B C   1 
ATOM   3911 O  O   . ILE   B 1 185 ? -0.244  -7.732  -18.074 1.00 16.77 ? 197 ILE   B O   1 
ATOM   3912 C  CB  . ILE   B 1 185 ? -0.864  -7.758  -21.088 1.00 14.74 ? 197 ILE   B CB  1 
ATOM   3913 C  CG1 . ILE   B 1 185 ? -0.524  -8.025  -22.556 1.00 16.43 ? 197 ILE   B CG1 1 
ATOM   3914 C  CG2 . ILE   B 1 185 ? -2.033  -6.792  -20.937 1.00 18.71 ? 197 ILE   B CG2 1 
ATOM   3915 C  CD1 . ILE   B 1 185 ? -1.511  -8.898  -23.238 1.00 16.53 ? 197 ILE   B CD1 1 
ATOM   3916 N  N   . LEU   B 1 186 ? -0.016  -5.558  -18.626 1.00 13.58 ? 198 LEU   B N   1 
ATOM   3917 C  CA  . LEU   B 1 186 ? -0.715  -5.022  -17.450 1.00 15.75 ? 198 LEU   B CA  1 
ATOM   3918 C  C   . LEU   B 1 186 ? -1.977  -4.315  -17.933 1.00 13.90 ? 198 LEU   B C   1 
ATOM   3919 O  O   . LEU   B 1 186 ? -1.904  -3.282  -18.604 1.00 15.90 ? 198 LEU   B O   1 
ATOM   3920 C  CB  . LEU   B 1 186 ? 0.163   -4.076  -16.637 1.00 15.82 ? 198 LEU   B CB  1 
ATOM   3921 C  CG  . LEU   B 1 186 ? -0.308  -3.625  -15.237 1.00 21.21 ? 198 LEU   B CG  1 
ATOM   3922 C  CD1 . LEU   B 1 186 ? -1.179  -2.365  -15.260 1.00 22.06 ? 198 LEU   B CD1 1 
ATOM   3923 C  CD2 . LEU   B 1 186 ? -1.021  -4.753  -14.475 1.00 17.13 ? 198 LEU   B CD2 1 
ATOM   3924 N  N   . ASP   B 1 187 ? -3.132  -4.847  -17.559 1.00 16.68 ? 199 ASP   B N   1 
ATOM   3925 C  CA  . ASP   B 1 187 ? -4.413  -4.268  -17.960 1.00 17.94 ? 199 ASP   B CA  1 
ATOM   3926 C  C   . ASP   B 1 187 ? -4.801  -3.213  -16.932 1.00 20.03 ? 199 ASP   B C   1 
ATOM   3927 O  O   . ASP   B 1 187 ? -5.084  -3.539  -15.769 1.00 18.07 ? 199 ASP   B O   1 
ATOM   3928 C  CB  . ASP   B 1 187 ? -5.458  -5.369  -18.083 1.00 19.90 ? 199 ASP   B CB  1 
ATOM   3929 C  CG  . ASP   B 1 187 ? -6.770  -4.874  -18.632 1.00 22.87 ? 199 ASP   B CG  1 
ATOM   3930 O  OD1 . ASP   B 1 187 ? -7.076  -3.665  -18.523 1.00 24.35 ? 199 ASP   B OD1 1 
ATOM   3931 O  OD2 . ASP   B 1 187 ? -7.509  -5.719  -19.178 1.00 25.20 ? 199 ASP   B OD2 1 
ATOM   3932 N  N   . THR   B 1 188 ? -4.801  -1.948  -17.353 1.00 19.68 ? 200 THR   B N   1 
ATOM   3933 C  CA  . THR   B 1 188 ? -5.092  -0.860  -16.424 1.00 18.36 ? 200 THR   B CA  1 
ATOM   3934 C  C   . THR   B 1 188 ? -6.569  -0.794  -16.037 1.00 18.87 ? 200 THR   B C   1 
ATOM   3935 O  O   . THR   B 1 188 ? -6.924  -0.010  -15.147 1.00 18.57 ? 200 THR   B O   1 
ATOM   3936 C  CB  . THR   B 1 188 ? -4.632  0.490   -16.996 1.00 17.28 ? 200 THR   B CB  1 
ATOM   3937 O  OG1 . THR   B 1 188 ? -5.221  0.725   -18.282 1.00 20.88 ? 200 THR   B OG1 1 
ATOM   3938 C  CG2 . THR   B 1 188 ? -3.117  0.530   -17.127 1.00 20.11 ? 200 THR   B CG2 1 
ATOM   3939 N  N   . GLU   B 1 189 ? -7.432  -1.596  -16.662 1.00 20.72 ? 201 GLU   B N   1 
ATOM   3940 C  CA  . GLU   B 1 189 ? -8.815  -1.682  -16.183 1.00 17.55 ? 201 GLU   B CA  1 
ATOM   3941 C  C   . GLU   B 1 189 ? -8.909  -2.402  -14.844 1.00 19.75 ? 201 GLU   B C   1 
ATOM   3942 O  O   . GLU   B 1 189 ? -9.789  -2.093  -14.028 1.00 18.33 ? 201 GLU   B O   1 
ATOM   3943 C  CB  . GLU   B 1 189 ? -9.696  -2.399  -17.208 1.00 20.13 ? 201 GLU   B CB  1 
ATOM   3944 C  CG  . GLU   B 1 189 ? -9.949  -1.599  -18.476 1.00 18.04 ? 201 GLU   B CG  1 
ATOM   3945 C  CD  . GLU   B 1 189 ? -10.602 -2.430  -19.591 1.00 25.16 ? 201 GLU   B CD  1 
ATOM   3946 O  OE1 . GLU   B 1 189 ? -11.137 -3.523  -19.299 1.00 28.36 ? 201 GLU   B OE1 1 
ATOM   3947 O  OE2 . GLU   B 1 189 ? -10.576 -1.986  -20.762 1.00 20.32 ? 201 GLU   B OE2 1 
ATOM   3948 N  N   . THR   B 1 190 ? -8.057  -3.389  -14.614 1.00 22.52 ? 202 THR   B N   1 
ATOM   3949 C  CA  . THR   B 1 190 ? -8.107  -4.149  -13.373 1.00 22.25 ? 202 THR   B CA  1 
ATOM   3950 C  C   . THR   B 1 190 ? -6.762  -4.263  -12.663 1.00 24.83 ? 202 THR   B C   1 
ATOM   3951 O  O   . THR   B 1 190 ? -6.708  -4.836  -11.564 1.00 22.29 ? 202 THR   B O   1 
ATOM   3952 C  CB  . THR   B 1 190 ? -8.666  -5.550  -13.643 1.00 21.50 ? 202 THR   B CB  1 
ATOM   3953 O  OG1 . THR   B 1 190 ? -7.782  -6.251  -14.521 1.00 25.03 ? 202 THR   B OG1 1 
ATOM   3954 C  CG2 . THR   B 1 190 ? -10.048 -5.458  -14.293 1.00 22.06 ? 202 THR   B CG2 1 
ATOM   3955 N  N   . PHE   B 1 191 ? -5.691  -3.713  -13.241 1.00 20.93 ? 203 PHE   B N   1 
ATOM   3956 C  CA  . PHE   B 1 191 ? -4.320  -3.873  -12.755 1.00 19.46 ? 203 PHE   B CA  1 
ATOM   3957 C  C   . PHE   B 1 191 ? -4.000  -5.349  -12.550 1.00 24.85 ? 203 PHE   B C   1 
ATOM   3958 O  O   . PHE   B 1 191 ? -3.661  -5.809  -11.455 1.00 24.44 ? 203 PHE   B O   1 
ATOM   3959 C  CB  . PHE   B 1 191 ? -4.078  -3.050  -11.486 1.00 20.52 ? 203 PHE   B CB  1 
ATOM   3960 C  CG  . PHE   B 1 191 ? -4.180  -1.575  -11.713 1.00 22.65 ? 203 PHE   B CG  1 
ATOM   3961 C  CD1 . PHE   B 1 191 ? -3.123  -0.869  -12.273 1.00 21.31 ? 203 PHE   B CD1 1 
ATOM   3962 C  CD2 . PHE   B 1 191 ? -5.351  -0.901  -11.418 1.00 25.47 ? 203 PHE   B CD2 1 
ATOM   3963 C  CE1 . PHE   B 1 191 ? -3.226  0.494   -12.502 1.00 24.34 ? 203 PHE   B CE1 1 
ATOM   3964 C  CE2 . PHE   B 1 191 ? -5.464  0.457   -11.644 1.00 24.94 ? 203 PHE   B CE2 1 
ATOM   3965 C  CZ  . PHE   B 1 191 ? -4.405  1.155   -12.185 1.00 25.06 ? 203 PHE   B CZ  1 
ATOM   3966 N  N   . THR   B 1 192 ? -4.114  -6.091  -13.648 1.00 17.19 ? 204 THR   B N   1 
ATOM   3967 C  CA  . THR   B 1 192 ? -3.947  -7.535  -13.642 1.00 21.14 ? 204 THR   B CA  1 
ATOM   3968 C  C   . THR   B 1 192 ? -2.914  -7.923  -14.684 1.00 20.66 ? 204 THR   B C   1 
ATOM   3969 O  O   . THR   B 1 192 ? -3.044  -7.551  -15.854 1.00 21.78 ? 204 THR   B O   1 
ATOM   3970 C  CB  . THR   B 1 192 ? -5.261  -8.249  -13.940 1.00 22.78 ? 204 THR   B CB  1 
ATOM   3971 O  OG1 . THR   B 1 192 ? -6.170  -8.053  -12.851 1.00 23.38 ? 204 THR   B OG1 1 
ATOM   3972 C  CG2 . THR   B 1 192 ? -5.015  -9.735  -14.146 1.00 24.13 ? 204 THR   B CG2 1 
ATOM   3973 N  N   . TRP   B 1 193 ? -1.904  -8.672  -14.253 1.00 20.05 ? 205 TRP   B N   1 
ATOM   3974 C  CA  . TRP   B 1 193 ? -0.879  -9.172  -15.154 1.00 20.50 ? 205 TRP   B CA  1 
ATOM   3975 C  C   . TRP   B 1 193 ? -1.377  -10.395 -15.918 1.00 21.10 ? 205 TRP   B C   1 
ATOM   3976 O  O   . TRP   B 1 193 ? -2.137  -11.217 -15.394 1.00 21.47 ? 205 TRP   B O   1 
ATOM   3977 C  CB  . TRP   B 1 193 ? 0.384   -9.541  -14.382 1.00 20.56 ? 205 TRP   B CB  1 
ATOM   3978 C  CG  . TRP   B 1 193 ? 1.127   -8.387  -13.792 1.00 22.74 ? 205 TRP   B CG  1 
ATOM   3979 C  CD1 . TRP   B 1 193 ? 1.173   -8.014  -12.470 1.00 20.24 ? 205 TRP   B CD1 1 
ATOM   3980 C  CD2 . TRP   B 1 193 ? 1.967   -7.467  -14.496 1.00 21.79 ? 205 TRP   B CD2 1 
ATOM   3981 N  NE1 . TRP   B 1 193 ? 1.977   -6.906  -12.318 1.00 20.67 ? 205 TRP   B NE1 1 
ATOM   3982 C  CE2 . TRP   B 1 193 ? 2.482   -6.555  -13.546 1.00 21.52 ? 205 TRP   B CE2 1 
ATOM   3983 C  CE3 . TRP   B 1 193 ? 2.333   -7.324  -15.841 1.00 19.13 ? 205 TRP   B CE3 1 
ATOM   3984 C  CZ2 . TRP   B 1 193 ? 3.349   -5.513  -13.900 1.00 22.03 ? 205 TRP   B CZ2 1 
ATOM   3985 C  CZ3 . TRP   B 1 193 ? 3.205   -6.288  -16.193 1.00 17.84 ? 205 TRP   B CZ3 1 
ATOM   3986 C  CH2 . TRP   B 1 193 ? 3.694   -5.395  -15.229 1.00 17.59 ? 205 TRP   B CH2 1 
ATOM   3987 N  N   . SER   B 1 194 ? -0.916  -10.514 -17.159 1.00 19.03 ? 206 SER   B N   1 
ATOM   3988 C  CA  . SER   B 1 194 ? -1.221  -11.643 -18.026 1.00 21.04 ? 206 SER   B CA  1 
ATOM   3989 C  C   . SER   B 1 194 ? -0.154  -11.689 -19.114 1.00 21.05 ? 206 SER   B C   1 
ATOM   3990 O  O   . SER   B 1 194 ? 0.567   -10.714 -19.325 1.00 18.34 ? 206 SER   B O   1 
ATOM   3991 C  CB  . SER   B 1 194 ? -2.619  -11.510 -18.636 1.00 20.86 ? 206 SER   B CB  1 
ATOM   3992 O  OG  . SER   B 1 194 ? -2.600  -10.581 -19.713 1.00 25.71 ? 206 SER   B OG  1 
ATOM   3993 N  N   . GLN   B 1 195 ? -0.057  -12.828 -19.805 1.00 21.26 ? 207 GLN   B N   1 
ATOM   3994 C  CA  . GLN   B 1 195 ? 0.798   -12.900 -20.989 1.00 22.14 ? 207 GLN   B CA  1 
ATOM   3995 C  C   . GLN   B 1 195 ? -0.004  -13.326 -22.215 1.00 19.57 ? 207 GLN   B C   1 
ATOM   3996 O  O   . GLN   B 1 195 ? -0.827  -14.243 -22.127 1.00 23.72 ? 207 GLN   B O   1 
ATOM   3997 C  CB  . GLN   B 1 195 ? 1.959   -13.881 -20.798 1.00 24.55 ? 207 GLN   B CB  1 
ATOM   3998 C  CG  . GLN   B 1 195 ? 2.897   -13.529 -19.655 1.00 23.44 ? 207 GLN   B CG  1 
ATOM   3999 C  CD  . GLN   B 1 195 ? 4.132   -14.400 -19.638 1.00 23.98 ? 207 GLN   B CD  1 
ATOM   4000 O  OE1 . GLN   B 1 195 ? 4.194   -15.403 -18.924 1.00 25.82 ? 207 GLN   B OE1 1 
ATOM   4001 N  NE2 . GLN   B 1 195 ? 5.123   -14.026 -20.438 1.00 24.72 ? 207 GLN   B NE2 1 
ATOM   4002 N  N   . PRO   B 1 196 ? 0.224   -12.704 -23.367 1.00 19.21 ? 208 PRO   B N   1 
ATOM   4003 C  CA  . PRO   B 1 196 ? -0.502  -13.111 -24.578 1.00 21.42 ? 208 PRO   B CA  1 
ATOM   4004 C  C   . PRO   B 1 196 ? 0.137   -14.305 -25.265 1.00 22.47 ? 208 PRO   B C   1 
ATOM   4005 O  O   . PRO   B 1 196 ? 1.356   -14.491 -25.254 1.00 22.21 ? 208 PRO   B O   1 
ATOM   4006 C  CB  . PRO   B 1 196 ? -0.411  -11.864 -25.467 1.00 18.54 ? 208 PRO   B CB  1 
ATOM   4007 C  CG  . PRO   B 1 196 ? 0.890   -11.255 -25.095 1.00 21.03 ? 208 PRO   B CG  1 
ATOM   4008 C  CD  . PRO   B 1 196 ? 1.042   -11.501 -23.599 1.00 17.99 ? 208 PRO   B CD  1 
ATOM   4009 N  N   . ILE   B 1 197 ? -0.708  -15.110 -25.902 1.00 24.48 ? 209 ILE   B N   1 
ATOM   4010 C  CA  . ILE   B 1 197 ? -0.226  -16.174 -26.774 1.00 25.67 ? 209 ILE   B CA  1 
ATOM   4011 C  C   . ILE   B 1 197 ? 0.172   -15.544 -28.105 1.00 24.19 ? 209 ILE   B C   1 
ATOM   4012 O  O   . ILE   B 1 197 ? -0.687  -15.152 -28.898 1.00 21.11 ? 209 ILE   B O   1 
ATOM   4013 C  CB  . ILE   B 1 197 ? -1.283  -17.262 -26.972 1.00 24.36 ? 209 ILE   B CB  1 
ATOM   4014 C  CG1 . ILE   B 1 197 ? -1.731  -17.792 -25.616 1.00 28.05 ? 209 ILE   B CG1 1 
ATOM   4015 C  CG2 . ILE   B 1 197 ? -0.727  -18.398 -27.795 1.00 25.73 ? 209 ILE   B CG2 1 
ATOM   4016 C  CD1 . ILE   B 1 197 ? -0.591  -18.402 -24.812 1.00 28.42 ? 209 ILE   B CD1 1 
ATOM   4017 N  N   . THR   B 1 198 ? 1.476   -15.459 -28.358 1.00 27.73 ? 210 THR   B N   1 
ATOM   4018 C  CA  . THR   B 1 198 ? 1.991   -14.856 -29.579 1.00 24.47 ? 210 THR   B CA  1 
ATOM   4019 C  C   . THR   B 1 198 ? 2.338   -15.911 -30.621 1.00 27.13 ? 210 THR   B C   1 
ATOM   4020 O  O   . THR   B 1 198 ? 2.677   -17.053 -30.298 1.00 30.72 ? 210 THR   B O   1 
ATOM   4021 C  CB  . THR   B 1 198 ? 3.251   -14.021 -29.330 1.00 25.09 ? 210 THR   B CB  1 
ATOM   4022 O  OG1 . THR   B 1 198 ? 4.326   -14.877 -28.899 1.00 27.02 ? 210 THR   B OG1 1 
ATOM   4023 C  CG2 . THR   B 1 198 ? 2.988   -12.926 -28.307 1.00 21.25 ? 210 THR   B CG2 1 
ATOM   4024 N  N   . THR   B 1 199 ? 2.288   -15.494 -31.876 1.00 24.05 ? 211 THR   B N   1 
ATOM   4025 C  CA  . THR   B 1 199 ? 2.790   -16.286 -32.984 1.00 25.51 ? 211 THR   B CA  1 
ATOM   4026 C  C   . THR   B 1 199 ? 3.921   -15.534 -33.678 1.00 25.26 ? 211 THR   B C   1 
ATOM   4027 O  O   . THR   B 1 199 ? 4.174   -14.358 -33.412 1.00 25.26 ? 211 THR   B O   1 
ATOM   4028 C  CB  . THR   B 1 199 ? 1.682   -16.609 -33.983 1.00 26.75 ? 211 THR   B CB  1 
ATOM   4029 O  OG1 . THR   B 1 199 ? 1.125   -15.386 -34.481 1.00 26.53 ? 211 THR   B OG1 1 
ATOM   4030 C  CG2 . THR   B 1 199 ? 0.594   -17.448 -33.320 1.00 31.61 ? 211 THR   B CG2 1 
ATOM   4031 N  N   . GLY   B 1 200 ? 4.585   -16.229 -34.598 1.00 27.75 ? 212 GLY   B N   1 
ATOM   4032 C  CA  . GLY   B 1 200 ? 5.776   -15.713 -35.238 1.00 23.58 ? 212 GLY   B CA  1 
ATOM   4033 C  C   . GLY   B 1 200 ? 7.004   -15.993 -34.399 1.00 26.65 ? 212 GLY   B C   1 
ATOM   4034 O  O   . GLY   B 1 200 ? 6.928   -16.471 -33.268 1.00 26.90 ? 212 GLY   B O   1 
ATOM   4035 N  N   . LYS   B 1 201 ? 8.168   -15.701 -34.967 1.00 27.74 ? 213 LYS   B N   1 
ATOM   4036 C  CA  . LYS   B 1 201 ? 9.407   -15.804 -34.207 1.00 26.94 ? 213 LYS   B CA  1 
ATOM   4037 C  C   . LYS   B 1 201 ? 9.610   -14.497 -33.450 1.00 24.30 ? 213 LYS   B C   1 
ATOM   4038 O  O   . LYS   B 1 201 ? 9.686   -13.425 -34.057 1.00 24.61 ? 213 LYS   B O   1 
ATOM   4039 C  CB  . LYS   B 1 201 ? 10.601  -16.116 -35.108 1.00 29.84 ? 213 LYS   B CB  1 
ATOM   4040 C  CG  . LYS   B 1 201 ? 11.851  -16.495 -34.324 1.00 32.71 ? 213 LYS   B CG  1 
ATOM   4041 C  CD  . LYS   B 1 201 ? 12.795  -17.361 -35.130 1.00 35.41 ? 213 LYS   B CD  1 
ATOM   4042 C  CE  . LYS   B 1 201 ? 14.135  -16.670 -35.337 1.00 36.77 ? 213 LYS   B CE  1 
ATOM   4043 N  NZ  . LYS   B 1 201 ? 15.093  -17.557 -36.049 1.00 38.03 ? 213 LYS   B NZ  1 
ATOM   4044 N  N   . ALA   B 1 202 ? 9.644   -14.581 -32.125 1.00 26.83 ? 214 ALA   B N   1 
ATOM   4045 C  CA  . ALA   B 1 202 ? 9.910   -13.409 -31.317 1.00 22.40 ? 214 ALA   B CA  1 
ATOM   4046 C  C   . ALA   B 1 202 ? 11.370  -13.008 -31.489 1.00 21.58 ? 214 ALA   B C   1 
ATOM   4047 O  O   . ALA   B 1 202 ? 12.186  -13.809 -31.949 1.00 26.13 ? 214 ALA   B O   1 
ATOM   4048 C  CB  . ALA   B 1 202 ? 9.594   -13.700 -29.852 1.00 22.86 ? 214 ALA   B CB  1 
ATOM   4049 N  N   . PRO   B 1 203 ? 11.728  -11.766 -31.163 1.00 19.94 ? 215 PRO   B N   1 
ATOM   4050 C  CA  . PRO   B 1 203 ? 13.153  -11.430 -31.126 1.00 20.30 ? 215 PRO   B CA  1 
ATOM   4051 C  C   . PRO   B 1 203 ? 13.824  -12.244 -30.034 1.00 18.84 ? 215 PRO   B C   1 
ATOM   4052 O  O   . PRO   B 1 203 ? 13.170  -12.778 -29.135 1.00 20.43 ? 215 PRO   B O   1 
ATOM   4053 C  CB  . PRO   B 1 203 ? 13.176  -9.932  -30.796 1.00 18.65 ? 215 PRO   B CB  1 
ATOM   4054 C  CG  . PRO   B 1 203 ? 11.764  -9.465  -30.922 1.00 17.32 ? 215 PRO   B CG  1 
ATOM   4055 C  CD  . PRO   B 1 203 ? 10.898  -10.649 -30.687 1.00 19.07 ? 215 PRO   B CD  1 
ATOM   4056 N  N   . SER   B 1 204 ? 15.152  -12.309 -30.100 1.00 16.63 ? 216 SER   B N   1 
ATOM   4057 C  CA  . SER   B 1 204 ? 15.894  -12.995 -29.064 1.00 11.93 ? 216 SER   B CA  1 
ATOM   4058 C  C   . SER   B 1 204 ? 15.717  -12.273 -27.729 1.00 15.59 ? 216 SER   B C   1 
ATOM   4059 O  O   . SER   B 1 204 ? 15.393  -11.082 -27.694 1.00 16.05 ? 216 SER   B O   1 
ATOM   4060 C  CB  . SER   B 1 204 ? 17.389  -13.030 -29.410 1.00 15.76 ? 216 SER   B CB  1 
ATOM   4061 O  OG  . SER   B 1 204 ? 17.982  -11.749 -29.219 1.00 16.66 ? 216 SER   B OG  1 
ATOM   4062 N  N   . PRO   B 1 205 ? 15.958  -12.966 -26.614 1.00 18.82 ? 217 PRO   B N   1 
ATOM   4063 C  CA  . PRO   B 1 205 ? 16.044  -12.261 -25.331 1.00 16.29 ? 217 PRO   B CA  1 
ATOM   4064 C  C   . PRO   B 1 205 ? 17.041  -11.112 -25.433 1.00 17.92 ? 217 PRO   B C   1 
ATOM   4065 O  O   . PRO   B 1 205 ? 18.077  -11.221 -26.087 1.00 16.54 ? 217 PRO   B O   1 
ATOM   4066 C  CB  . PRO   B 1 205 ? 16.524  -13.350 -24.361 1.00 19.11 ? 217 PRO   B CB  1 
ATOM   4067 C  CG  . PRO   B 1 205 ? 16.031  -14.628 -24.968 1.00 18.23 ? 217 PRO   B CG  1 
ATOM   4068 C  CD  . PRO   B 1 205 ? 16.155  -14.418 -26.463 1.00 20.39 ? 217 PRO   B CD  1 
ATOM   4069 N  N   . ARG   B 1 206 ? 16.700  -9.982  -24.826 1.00 16.51 ? 218 ARG   B N   1 
ATOM   4070 C  CA  . ARG   B 1 206 ? 17.574  -8.822  -24.888 1.00 17.75 ? 218 ARG   B CA  1 
ATOM   4071 C  C   . ARG   B 1 206 ? 17.274  -7.880  -23.732 1.00 13.41 ? 218 ARG   B C   1 
ATOM   4072 O  O   . ARG   B 1 206 ? 16.209  -7.938  -23.113 1.00 15.77 ? 218 ARG   B O   1 
ATOM   4073 C  CB  . ARG   B 1 206 ? 17.426  -8.077  -26.218 1.00 15.82 ? 218 ARG   B CB  1 
ATOM   4074 C  CG  . ARG   B 1 206 ? 16.002  -7.661  -26.549 1.00 14.17 ? 218 ARG   B CG  1 
ATOM   4075 C  CD  . ARG   B 1 206 ? 15.922  -7.262  -28.020 1.00 16.09 ? 218 ARG   B CD  1 
ATOM   4076 N  NE  . ARG   B 1 206 ? 16.107  -8.421  -28.883 1.00 16.39 ? 218 ARG   B NE  1 
ATOM   4077 C  CZ  . ARG   B 1 206 ? 16.393  -8.341  -30.175 1.00 18.00 ? 218 ARG   B CZ  1 
ATOM   4078 N  NH1 . ARG   B 1 206 ? 16.526  -7.169  -30.780 1.00 14.11 ? 218 ARG   B NH1 1 
ATOM   4079 N  NH2 . ARG   B 1 206 ? 16.530  -9.460  -30.877 1.00 17.78 ? 218 ARG   B NH2 1 
ATOM   4080 N  N   . ALA   B 1 207 ? 18.229  -6.998  -23.468 1.00 10.32 ? 219 ALA   B N   1 
ATOM   4081 C  CA  . ALA   B 1 207 ? 18.015  -5.845  -22.610 1.00 11.61 ? 219 ALA   B CA  1 
ATOM   4082 C  C   . ALA   B 1 207 ? 18.638  -4.624  -23.265 1.00 13.70 ? 219 ALA   B C   1 
ATOM   4083 O  O   . ALA   B 1 207 ? 19.459  -4.739  -24.181 1.00 13.81 ? 219 ALA   B O   1 
ATOM   4084 C  CB  . ALA   B 1 207 ? 18.611  -6.061  -21.212 1.00 13.08 ? 219 ALA   B CB  1 
ATOM   4085 N  N   . ALA   B 1 208 ? 18.249  -3.444  -22.774 1.00 10.97 ? 220 ALA   B N   1 
ATOM   4086 C  CA  . ALA   B 1 208 ? 18.736  -2.171  -23.291 1.00 11.10 ? 220 ALA   B CA  1 
ATOM   4087 C  C   . ALA   B 1 208 ? 18.415  -2.009  -24.773 1.00 12.15 ? 220 ALA   B C   1 
ATOM   4088 O  O   . ALA   B 1 208 ? 19.123  -1.301  -25.497 1.00 10.59 ? 220 ALA   B O   1 
ATOM   4089 C  CB  . ALA   B 1 208 ? 20.243  -1.995  -23.041 1.00 14.46 ? 220 ALA   B CB  1 
ATOM   4090 N  N   . HIS   B 1 209 ? 17.350  -2.686  -25.212 1.00 11.31 ? 221 HIS   B N   1 
ATOM   4091 C  CA  . HIS   B 1 209 ? 16.676  -2.429  -26.478 1.00 13.24 ? 221 HIS   B CA  1 
ATOM   4092 C  C   . HIS   B 1 209 ? 15.849  -1.146  -26.373 1.00 13.48 ? 221 HIS   B C   1 
ATOM   4093 O  O   . HIS   B 1 209 ? 15.700  -0.556  -25.297 1.00 13.86 ? 221 HIS   B O   1 
ATOM   4094 C  CB  . HIS   B 1 209 ? 15.782  -3.614  -26.848 1.00 10.83 ? 221 HIS   B CB  1 
ATOM   4095 C  CG  . HIS   B 1 209 ? 14.913  -4.095  -25.728 1.00 12.82 ? 221 HIS   B CG  1 
ATOM   4096 N  ND1 . HIS   B 1 209 ? 15.417  -4.765  -24.634 1.00 12.26 ? 221 HIS   B ND1 1 
ATOM   4097 C  CD2 . HIS   B 1 209 ? 13.574  -4.020  -25.540 1.00 13.37 ? 221 HIS   B CD2 1 
ATOM   4098 C  CE1 . HIS   B 1 209 ? 14.425  -5.083  -23.819 1.00 12.61 ? 221 HIS   B CE1 1 
ATOM   4099 N  NE2 . HIS   B 1 209 ? 13.296  -4.643  -24.343 1.00 11.41 ? 221 HIS   B NE2 1 
ATOM   4100 N  N   . ALA   B 1 210 ? 15.315  -0.696  -27.504 1.00 12.99 ? 222 ALA   B N   1 
ATOM   4101 C  CA  . ALA   B 1 210 ? 14.378  0.418   -27.496 1.00 13.10 ? 222 ALA   B CA  1 
ATOM   4102 C  C   . ALA   B 1 210 ? 13.047  -0.000  -28.118 1.00 13.57 ? 222 ALA   B C   1 
ATOM   4103 O  O   . ALA   B 1 210 ? 13.006  -0.678  -29.147 1.00 13.63 ? 222 ALA   B O   1 
ATOM   4104 C  CB  . ALA   B 1 210 ? 14.946  1.631   -28.216 1.00 15.04 ? 222 ALA   B CB  1 
ATOM   4105 N  N   . CYS   B 1 211 ? 11.956  0.390   -27.469 1.00 16.22 ? 223 CYS   B N   1 
ATOM   4106 C  CA  . CYS   B 1 211 ? 10.612  0.086   -27.941 1.00 15.13 ? 223 CYS   B CA  1 
ATOM   4107 C  C   . CYS   B 1 211 ? 9.910   1.368   -28.364 1.00 14.59 ? 223 CYS   B C   1 
ATOM   4108 O  O   . CYS   B 1 211 ? 10.113  2.419   -27.755 1.00 15.08 ? 223 CYS   B O   1 
ATOM   4109 C  CB  . CYS   B 1 211 ? 9.800   -0.621  -26.851 1.00 13.89 ? 223 CYS   B CB  1 
ATOM   4110 S  SG  . CYS   B 1 211 ? 10.284  -2.307  -26.574 1.00 15.15 ? 223 CYS   B SG  1 
ATOM   4111 N  N   . ALA   B 1 212 ? 9.089   1.286   -29.419 1.00 13.51 ? 224 ALA   B N   1 
ATOM   4112 C  CA  . ALA   B 1 212 ? 8.282   2.425   -29.844 1.00 15.68 ? 224 ALA   B CA  1 
ATOM   4113 C  C   . ALA   B 1 212 ? 6.953   1.918   -30.401 1.00 14.08 ? 224 ALA   B C   1 
ATOM   4114 O  O   . ALA   B 1 212 ? 6.914   0.878   -31.059 1.00 14.66 ? 224 ALA   B O   1 
ATOM   4115 C  CB  . ALA   B 1 212 ? 9.019   3.270   -30.897 1.00 18.94 ? 224 ALA   B CB  1 
ATOM   4116 N  N   . THR   B 1 213 ? 5.875   2.647   -30.140 1.00 16.80 ? 225 THR   B N   1 
ATOM   4117 C  CA  . THR   B 1 213 ? 4.529   2.213   -30.519 1.00 14.94 ? 225 THR   B CA  1 
ATOM   4118 C  C   . THR   B 1 213 ? 3.948   3.173   -31.544 1.00 13.80 ? 225 THR   B C   1 
ATOM   4119 O  O   . THR   B 1 213 ? 3.979   4.389   -31.337 1.00 14.92 ? 225 THR   B O   1 
ATOM   4120 C  CB  . THR   B 1 213 ? 3.606   2.141   -29.290 1.00 13.84 ? 225 THR   B CB  1 
ATOM   4121 O  OG1 . THR   B 1 213 ? 4.215   1.315   -28.289 1.00 16.40 ? 225 THR   B OG1 1 
ATOM   4122 C  CG2 . THR   B 1 213 ? 2.218   1.558   -29.651 1.00 19.90 ? 225 THR   B CG2 1 
ATOM   4123 N  N   . VAL   B 1 214 ? 3.411   2.632   -32.638 1.00 18.54 ? 226 VAL   B N   1 
ATOM   4124 C  CA  . VAL   B 1 214 ? 2.658   3.427   -33.609 1.00 20.81 ? 226 VAL   B CA  1 
ATOM   4125 C  C   . VAL   B 1 214 ? 1.409   2.648   -34.003 1.00 20.48 ? 226 VAL   B C   1 
ATOM   4126 O  O   . VAL   B 1 214 ? 1.510   1.552   -34.569 1.00 18.21 ? 226 VAL   B O   1 
ATOM   4127 C  CB  . VAL   B 1 214 ? 3.491   3.790   -34.849 1.00 19.07 ? 226 VAL   B CB  1 
ATOM   4128 C  CG1 . VAL   B 1 214 ? 2.663   4.634   -35.794 1.00 21.95 ? 226 VAL   B CG1 1 
ATOM   4129 C  CG2 . VAL   B 1 214 ? 4.709   4.582   -34.414 1.00 14.71 ? 226 VAL   B CG2 1 
ATOM   4130 N  N   . GLY   B 1 215 ? 0.241   3.202   -33.689 1.00 25.66 ? 227 GLY   B N   1 
ATOM   4131 C  CA  . GLY   B 1 215 ? -1.008  2.477   -33.892 1.00 25.11 ? 227 GLY   B CA  1 
ATOM   4132 C  C   . GLY   B 1 215 ? -0.964  1.185   -33.105 1.00 20.66 ? 227 GLY   B C   1 
ATOM   4133 O  O   . GLY   B 1 215 ? -0.580  1.163   -31.929 1.00 28.41 ? 227 GLY   B O   1 
ATOM   4134 N  N   . ASN   B 1 216 ? -1.258  0.079   -33.782 1.00 20.75 ? 228 ASN   B N   1 
ATOM   4135 C  CA  . ASN   B 1 216 ? -1.226  -1.247  -33.177 1.00 19.51 ? 228 ASN   B CA  1 
ATOM   4136 C  C   . ASN   B 1 216 ? 0.078   -1.995  -33.458 1.00 17.82 ? 228 ASN   B C   1 
ATOM   4137 O  O   . ASN   B 1 216 ? 0.100   -3.228  -33.466 1.00 16.56 ? 228 ASN   B O   1 
ATOM   4138 C  CB  . ASN   B 1 216 ? -2.415  -2.074  -33.664 1.00 24.29 ? 228 ASN   B CB  1 
ATOM   4139 C  CG  . ASN   B 1 216 ? -2.352  -2.360  -35.160 1.00 21.67 ? 228 ASN   B CG  1 
ATOM   4140 O  OD1 . ASN   B 1 216 ? -1.426  -1.931  -35.859 1.00 20.67 ? 228 ASN   B OD1 1 
ATOM   4141 N  ND2 . ASN   B 1 216 ? -3.330  -3.109  -35.656 1.00 25.47 ? 228 ASN   B ND2 1 
ATOM   4142 N  N   . ARG   B 1 217 ? 1.168   -1.284  -33.719 1.00 17.24 ? 229 ARG   B N   1 
ATOM   4143 C  CA  . ARG   B 1 217 ? 2.456   -1.921  -33.943 1.00 16.58 ? 229 ARG   B CA  1 
ATOM   4144 C  C   . ARG   B 1 217 ? 3.404   -1.483  -32.843 1.00 15.24 ? 229 ARG   B C   1 
ATOM   4145 O  O   . ARG   B 1 217 ? 3.708   -0.291  -32.722 1.00 17.95 ? 229 ARG   B O   1 
ATOM   4146 C  CB  . ARG   B 1 217 ? 3.044   -1.574  -35.312 1.00 16.84 ? 229 ARG   B CB  1 
ATOM   4147 C  CG  . ARG   B 1 217 ? 2.181   -2.066  -36.459 1.00 17.55 ? 229 ARG   B CG  1 
ATOM   4148 C  CD  . ARG   B 1 217 ? 2.859   -1.915  -37.785 1.00 21.56 ? 229 ARG   B CD  1 
ATOM   4149 N  NE  . ARG   B 1 217 ? 1.947   -2.242  -38.879 1.00 20.34 ? 229 ARG   B NE  1 
ATOM   4150 C  CZ  . ARG   B 1 217 ? 2.337   -2.505  -40.120 1.00 21.87 ? 229 ARG   B CZ  1 
ATOM   4151 N  NH1 . ARG   B 1 217 ? 3.618   -2.513  -40.453 1.00 21.88 ? 229 ARG   B NH1 1 
ATOM   4152 N  NH2 . ARG   B 1 217 ? 1.419   -2.772  -41.046 1.00 25.58 ? 229 ARG   B NH2 1 
ATOM   4153 N  N   . GLY   B 1 218 ? 3.876   -2.450  -32.067 1.00 14.92 ? 230 GLY   B N   1 
ATOM   4154 C  CA  . GLY   B 1 218 ? 4.912   -2.200  -31.083 1.00 17.36 ? 230 GLY   B CA  1 
ATOM   4155 C  C   . GLY   B 1 218 ? 6.278   -2.575  -31.621 1.00 14.52 ? 230 GLY   B C   1 
ATOM   4156 O  O   . GLY   B 1 218 ? 6.618   -3.759  -31.672 1.00 15.13 ? 230 GLY   B O   1 
ATOM   4157 N  N   . PHE   B 1 219 ? 7.060   -1.584  -32.039 1.00 15.42 ? 231 PHE   B N   1 
ATOM   4158 C  CA  . PHE   B 1 219 ? 8.378   -1.831  -32.617 1.00 14.28 ? 231 PHE   B CA  1 
ATOM   4159 C  C   . PHE   B 1 219 ? 9.406   -2.036  -31.518 1.00 16.29 ? 231 PHE   B C   1 
ATOM   4160 O  O   . PHE   B 1 219 ? 9.278   -1.500  -30.418 1.00 18.29 ? 231 PHE   B O   1 
ATOM   4161 C  CB  . PHE   B 1 219 ? 8.814   -0.662  -33.498 1.00 11.56 ? 231 PHE   B CB  1 
ATOM   4162 C  CG  . PHE   B 1 219 ? 7.961   -0.473  -34.716 1.00 16.93 ? 231 PHE   B CG  1 
ATOM   4163 C  CD1 . PHE   B 1 219 ? 6.826   0.331   -34.669 1.00 17.49 ? 231 PHE   B CD1 1 
ATOM   4164 C  CD2 . PHE   B 1 219 ? 8.289   -1.096  -35.898 1.00 16.56 ? 231 PHE   B CD2 1 
ATOM   4165 C  CE1 . PHE   B 1 219 ? 6.039   0.514   -35.781 1.00 18.67 ? 231 PHE   B CE1 1 
ATOM   4166 C  CE2 . PHE   B 1 219 ? 7.509   -0.916  -37.021 1.00 17.39 ? 231 PHE   B CE2 1 
ATOM   4167 C  CZ  . PHE   B 1 219 ? 6.384   -0.105  -36.960 1.00 17.39 ? 231 PHE   B CZ  1 
ATOM   4168 N  N   . VAL   B 1 220 ? 10.420  -2.846  -31.816 1.00 15.52 ? 232 VAL   B N   1 
ATOM   4169 C  CA  . VAL   B 1 220 ? 11.569  -3.018  -30.927 1.00 15.53 ? 232 VAL   B CA  1 
ATOM   4170 C  C   . VAL   B 1 220 ? 12.820  -3.097  -31.800 1.00 15.44 ? 232 VAL   B C   1 
ATOM   4171 O  O   . VAL   B 1 220 ? 12.823  -3.789  -32.829 1.00 15.03 ? 232 VAL   B O   1 
ATOM   4172 C  CB  . VAL   B 1 220 ? 11.428  -4.251  -30.008 1.00 14.74 ? 232 VAL   B CB  1 
ATOM   4173 C  CG1 . VAL   B 1 220 ? 11.305  -5.550  -30.819 1.00 14.98 ? 232 VAL   B CG1 1 
ATOM   4174 C  CG2 . VAL   B 1 220 ? 12.603  -4.330  -29.052 1.00 14.93 ? 232 VAL   B CG2 1 
ATOM   4175 N  N   . PHE   B 1 221 ? 13.862  -2.345  -31.426 1.00 13.57 ? 233 PHE   B N   1 
ATOM   4176 C  CA  . PHE   B 1 221 ? 15.095  -2.282  -32.214 1.00 13.93 ? 233 PHE   B CA  1 
ATOM   4177 C  C   . PHE   B 1 221 ? 16.315  -2.502  -31.331 1.00 12.72 ? 233 PHE   B C   1 
ATOM   4178 O  O   . PHE   B 1 221 ? 16.421  -1.911  -30.247 1.00 15.87 ? 233 PHE   B O   1 
ATOM   4179 C  CB  . PHE   B 1 221 ? 15.255  -0.938  -32.943 1.00 13.04 ? 233 PHE   B CB  1 
ATOM   4180 C  CG  . PHE   B 1 221 ? 16.556  -0.826  -33.709 1.00 15.16 ? 233 PHE   B CG  1 
ATOM   4181 C  CD1 . PHE   B 1 221 ? 16.795  -1.629  -34.811 1.00 17.07 ? 233 PHE   B CD1 1 
ATOM   4182 C  CD2 . PHE   B 1 221 ? 17.543  0.072   -33.313 1.00 14.79 ? 233 PHE   B CD2 1 
ATOM   4183 C  CE1 . PHE   B 1 221 ? 17.988  -1.536  -35.517 1.00 16.54 ? 233 PHE   B CE1 1 
ATOM   4184 C  CE2 . PHE   B 1 221 ? 18.754  0.164   -34.019 1.00 16.40 ? 233 PHE   B CE2 1 
ATOM   4185 C  CZ  . PHE   B 1 221 ? 18.962  -0.639  -35.116 1.00 14.96 ? 233 PHE   B CZ  1 
ATOM   4186 N  N   . GLY   B 1 222 ? 17.232  -3.354  -31.790 1.00 11.05 ? 234 GLY   B N   1 
ATOM   4187 C  CA  . GLY   B 1 222 ? 18.525  -3.402  -31.119 1.00 14.53 ? 234 GLY   B CA  1 
ATOM   4188 C  C   . GLY   B 1 222 ? 18.466  -4.063  -29.748 1.00 13.03 ? 234 GLY   B C   1 
ATOM   4189 O  O   . GLY   B 1 222 ? 17.548  -4.824  -29.409 1.00 13.34 ? 234 GLY   B O   1 
ATOM   4190 N  N   . GLY   B 1 223 ? 19.486  -3.760  -28.956 1.00 14.90 ? 235 GLY   B N   1 
ATOM   4191 C  CA  . GLY   B 1 223 ? 19.620  -4.284  -27.611 1.00 14.78 ? 235 GLY   B CA  1 
ATOM   4192 C  C   . GLY   B 1 223 ? 20.807  -5.227  -27.480 1.00 17.93 ? 235 GLY   B C   1 
ATOM   4193 O  O   . GLY   B 1 223 ? 21.495  -5.567  -28.449 1.00 17.16 ? 235 GLY   B O   1 
ATOM   4194 N  N   . ARG   B 1 224 ? 21.018  -5.658  -26.239 1.00 12.78 ? 236 ARG   B N   1 
ATOM   4195 C  CA  . ARG   B 1 224 ? 22.165  -6.475  -25.864 1.00 16.35 ? 236 ARG   B CA  1 
ATOM   4196 C  C   . ARG   B 1 224 ? 21.699  -7.906  -25.662 1.00 17.26 ? 236 ARG   B C   1 
ATOM   4197 O  O   . ARG   B 1 224 ? 20.722  -8.145  -24.946 1.00 17.80 ? 236 ARG   B O   1 
ATOM   4198 C  CB  . ARG   B 1 224 ? 22.822  -5.954  -24.580 1.00 15.86 ? 236 ARG   B CB  1 
ATOM   4199 C  CG  . ARG   B 1 224 ? 23.723  -6.982  -23.889 1.00 18.58 ? 236 ARG   B CG  1 
ATOM   4200 C  CD  . ARG   B 1 224 ? 25.178  -6.894  -24.372 1.00 21.44 ? 236 ARG   B CD  1 
ATOM   4201 N  NE  . ARG   B 1 224 ? 25.977  -8.033  -23.921 1.00 18.82 ? 236 ARG   B NE  1 
ATOM   4202 C  CZ  . ARG   B 1 224 ? 26.544  -8.143  -22.721 1.00 20.94 ? 236 ARG   B CZ  1 
ATOM   4203 N  NH1 . ARG   B 1 224 ? 26.493  -7.160  -21.831 1.00 22.05 ? 236 ARG   B NH1 1 
ATOM   4204 N  NH2 . ARG   B 1 224 ? 27.174  -9.271  -22.401 1.00 21.20 ? 236 ARG   B NH2 1 
ATOM   4205 N  N   . TYR   B 1 225 ? 22.394  -8.852  -26.290 1.00 18.18 ? 237 TYR   B N   1 
ATOM   4206 C  CA  . TYR   B 1 225 ? 22.121  -10.273 -26.082 1.00 18.04 ? 237 TYR   B CA  1 
ATOM   4207 C  C   . TYR   B 1 225 ? 23.428  -11.039 -26.230 1.00 19.99 ? 237 TYR   B C   1 
ATOM   4208 O  O   . TYR   B 1 225 ? 24.030  -11.009 -27.307 1.00 21.82 ? 237 TYR   B O   1 
ATOM   4209 C  CB  . TYR   B 1 225 ? 21.083  -10.785 -27.078 1.00 23.16 ? 237 TYR   B CB  1 
ATOM   4210 C  CG  . TYR   B 1 225 ? 20.821  -12.267 -26.962 1.00 22.28 ? 237 TYR   B CG  1 
ATOM   4211 C  CD1 . TYR   B 1 225 ? 20.527  -12.838 -25.727 1.00 21.93 ? 237 TYR   B CD1 1 
ATOM   4212 C  CD2 . TYR   B 1 225 ? 20.861  -13.090 -28.075 1.00 21.43 ? 237 TYR   B CD2 1 
ATOM   4213 C  CE1 . TYR   B 1 225 ? 20.279  -14.194 -25.606 1.00 24.07 ? 237 TYR   B CE1 1 
ATOM   4214 C  CE2 . TYR   B 1 225 ? 20.622  -14.448 -27.968 1.00 23.61 ? 237 TYR   B CE2 1 
ATOM   4215 C  CZ  . TYR   B 1 225 ? 20.336  -14.995 -26.731 1.00 25.57 ? 237 TYR   B CZ  1 
ATOM   4216 O  OH  . TYR   B 1 225 ? 20.092  -16.344 -26.602 1.00 29.26 ? 237 TYR   B OH  1 
ATOM   4217 N  N   . ARG   B 1 226 ? 23.872  -11.700 -25.153 1.00 22.85 ? 238 ARG   B N   1 
ATOM   4218 C  CA  . ARG   B 1 226 ? 25.123  -12.477 -25.133 1.00 24.66 ? 238 ARG   B CA  1 
ATOM   4219 C  C   . ARG   B 1 226 ? 26.288  -11.546 -25.466 1.00 20.40 ? 238 ARG   B C   1 
ATOM   4220 O  O   . ARG   B 1 226 ? 26.434  -10.512 -24.794 1.00 22.06 ? 238 ARG   B O   1 
ATOM   4221 C  CB  . ARG   B 1 226 ? 24.953  -13.685 -26.058 1.00 23.51 ? 238 ARG   B CB  1 
ATOM   4222 C  CG  . ARG   B 1 226 ? 23.944  -14.722 -25.584 1.00 28.21 ? 238 ARG   B CG  1 
ATOM   4223 C  CD  . ARG   B 1 226 ? 23.804  -15.812 -26.625 1.00 30.31 ? 238 ARG   B CD  1 
ATOM   4224 N  NE  . ARG   B 1 226 ? 23.167  -17.019 -26.115 1.00 36.51 ? 238 ARG   B NE  1 
ATOM   4225 C  CZ  . ARG   B 1 226 ? 23.827  -18.079 -25.672 1.00 37.94 ? 238 ARG   B CZ  1 
ATOM   4226 N  NH1 . ARG   B 1 226 ? 25.145  -18.091 -25.608 1.00 41.66 ? 238 ARG   B NH1 1 
ATOM   4227 N  NH2 . ARG   B 1 226 ? 23.147  -19.160 -25.298 1.00 39.46 ? 238 ARG   B NH2 1 
ATOM   4228 N  N   . ASP   B 1 227 ? 27.104  -11.829 -26.488 1.00 27.54 ? 239 ASP   B N   1 
ATOM   4229 C  CA  . ASP   B 1 227 ? 28.247  -10.993 -26.848 1.00 26.06 ? 239 ASP   B CA  1 
ATOM   4230 C  C   . ASP   B 1 227 ? 27.932  -9.980  -27.943 1.00 26.17 ? 239 ASP   B C   1 
ATOM   4231 O  O   . ASP   B 1 227 ? 28.856  -9.507  -28.619 1.00 24.96 ? 239 ASP   B O   1 
ATOM   4232 C  CB  . ASP   B 1 227 ? 29.431  -11.851 -27.306 1.00 30.80 ? 239 ASP   B CB  1 
ATOM   4233 C  CG  . ASP   B 1 227 ? 29.942  -12.774 -26.225 1.00 33.18 ? 239 ASP   B CG  1 
ATOM   4234 O  OD1 . ASP   B 1 227 ? 30.256  -13.941 -26.549 1.00 35.28 ? 239 ASP   B OD1 1 
ATOM   4235 O  OD2 . ASP   B 1 227 ? 30.018  -12.335 -25.057 1.00 36.18 ? 239 ASP   B OD2 1 
ATOM   4236 N  N   . ALA   B 1 228 ? 26.665  -9.644  -28.151 1.00 21.53 ? 240 ALA   B N   1 
ATOM   4237 C  CA  . ALA   B 1 228 ? 26.316  -8.767  -29.256 1.00 22.25 ? 240 ALA   B CA  1 
ATOM   4238 C  C   . ALA   B 1 228 ? 25.411  -7.639  -28.797 1.00 22.30 ? 240 ALA   B C   1 
ATOM   4239 O  O   . ALA   B 1 228 ? 24.588  -7.811  -27.894 1.00 19.22 ? 240 ALA   B O   1 
ATOM   4240 C  CB  . ALA   B 1 228 ? 25.629  -9.540  -30.390 1.00 22.70 ? 240 ALA   B CB  1 
ATOM   4241 N  N   . ARG   B 1 229 ? 25.610  -6.475  -29.402 1.00 17.23 ? 241 ARG   B N   1 
ATOM   4242 C  CA  . ARG   B 1 229 ? 24.624  -5.406  -29.427 1.00 17.45 ? 241 ARG   B CA  1 
ATOM   4243 C  C   . ARG   B 1 229 ? 24.077  -5.363  -30.845 1.00 17.34 ? 241 ARG   B C   1 
ATOM   4244 O  O   . ARG   B 1 229 ? 24.831  -5.130  -31.790 1.00 16.17 ? 241 ARG   B O   1 
ATOM   4245 C  CB  . ARG   B 1 229 ? 25.259  -4.088  -28.999 1.00 15.44 ? 241 ARG   B CB  1 
ATOM   4246 C  CG  . ARG   B 1 229 ? 25.655  -4.187  -27.512 1.00 15.02 ? 241 ARG   B CG  1 
ATOM   4247 C  CD  . ARG   B 1 229 ? 26.366  -3.013  -26.910 1.00 14.26 ? 241 ARG   B CD  1 
ATOM   4248 N  NE  . ARG   B 1 229 ? 26.685  -3.349  -25.519 1.00 17.83 ? 241 ARG   B NE  1 
ATOM   4249 C  CZ  . ARG   B 1 229 ? 27.891  -3.682  -25.065 1.00 20.60 ? 241 ARG   B CZ  1 
ATOM   4250 N  NH1 . ARG   B 1 229 ? 28.975  -3.577  -25.821 1.00 15.92 ? 241 ARG   B NH1 1 
ATOM   4251 N  NH2 . ARG   B 1 229 ? 28.014  -4.141  -23.821 1.00 19.05 ? 241 ARG   B NH2 1 
ATOM   4252 N  N   . MET   B 1 230 ? 22.783  -5.607  -30.991 1.00 16.41 ? 242 MET   B N   1 
ATOM   4253 C  CA  . MET   B 1 230 ? 22.223  -6.078  -32.250 1.00 19.23 ? 242 MET   B CA  1 
ATOM   4254 C  C   . MET   B 1 230 ? 21.572  -4.958  -33.044 1.00 15.30 ? 242 MET   B C   1 
ATOM   4255 O  O   . MET   B 1 230 ? 21.274  -3.878  -32.524 1.00 15.19 ? 242 MET   B O   1 
ATOM   4256 C  CB  . MET   B 1 230 ? 21.217  -7.190  -31.970 1.00 21.83 ? 242 MET   B CB  1 
ATOM   4257 C  CG  . MET   B 1 230 ? 21.880  -8.389  -31.326 1.00 23.75 ? 242 MET   B CG  1 
ATOM   4258 S  SD  . MET   B 1 230 ? 20.664  -9.501  -30.632 1.00 26.18 ? 242 MET   B SD  1 
ATOM   4259 C  CE  . MET   B 1 230 ? 19.469  -9.622  -31.938 1.00 26.14 ? 242 MET   B CE  1 
ATOM   4260 N  N   . ASN   B 1 231 ? 21.382  -5.225  -34.342 1.00 18.98 ? 243 ASN   B N   1 
ATOM   4261 C  CA  . ASN   B 1 231 ? 20.870  -4.241  -35.287 1.00 18.08 ? 243 ASN   B CA  1 
ATOM   4262 C  C   . ASN   B 1 231 ? 19.503  -4.606  -35.843 1.00 19.23 ? 243 ASN   B C   1 
ATOM   4263 O  O   . ASN   B 1 231 ? 19.080  -4.018  -36.856 1.00 20.08 ? 243 ASN   B O   1 
ATOM   4264 C  CB  . ASN   B 1 231 ? 21.844  -4.079  -36.468 1.00 18.89 ? 243 ASN   B CB  1 
ATOM   4265 C  CG  . ASN   B 1 231 ? 21.881  -5.307  -37.353 1.00 17.85 ? 243 ASN   B CG  1 
ATOM   4266 O  OD1 . ASN   B 1 231 ? 21.555  -6.416  -36.910 1.00 27.50 ? 243 ASN   B OD1 1 
ATOM   4267 N  ND2 . ASN   B 1 231 ? 22.289  -5.131  -38.610 1.00 25.05 ? 243 ASN   B ND2 1 
ATOM   4268 N  N   . ASP   B 1 232 ? 18.819  -5.577  -35.247 1.00 16.41 ? 244 ASP   B N   1 
ATOM   4269 C  CA  . ASP   B 1 232 ? 17.616  -6.101  -35.862 1.00 15.03 ? 244 ASP   B CA  1 
ATOM   4270 C  C   . ASP   B 1 232 ? 16.381  -5.322  -35.415 1.00 18.01 ? 244 ASP   B C   1 
ATOM   4271 O  O   . ASP   B 1 232 ? 16.356  -4.679  -34.360 1.00 18.40 ? 244 ASP   B O   1 
ATOM   4272 C  CB  . ASP   B 1 232 ? 17.464  -7.600  -35.598 1.00 16.11 ? 244 ASP   B CB  1 
ATOM   4273 C  CG  . ASP   B 1 232 ? 17.482  -7.969  -34.104 1.00 20.73 ? 244 ASP   B CG  1 
ATOM   4274 O  OD1 . ASP   B 1 232 ? 17.959  -7.175  -33.255 1.00 18.76 ? 244 ASP   B OD1 1 
ATOM   4275 O  OD2 . ASP   B 1 232 ? 17.034  -9.094  -33.794 1.00 20.68 ? 244 ASP   B OD2 1 
ATOM   4276 N  N   . LEU   B 1 233 ? 15.355  -5.376  -36.258 1.00 19.11 ? 245 LEU   B N   1 
ATOM   4277 C  CA  . LEU   B 1 233 ? 14.131  -4.603  -36.091 1.00 17.50 ? 245 LEU   B CA  1 
ATOM   4278 C  C   . LEU   B 1 233 ? 12.936  -5.536  -36.186 1.00 17.94 ? 245 LEU   B C   1 
ATOM   4279 O  O   . LEU   B 1 233 ? 12.803  -6.283  -37.162 1.00 18.95 ? 245 LEU   B O   1 
ATOM   4280 C  CB  . LEU   B 1 233 ? 14.034  -3.500  -37.157 1.00 16.55 ? 245 LEU   B CB  1 
ATOM   4281 C  CG  . LEU   B 1 233 ? 12.859  -2.514  -37.147 1.00 15.08 ? 245 LEU   B CG  1 
ATOM   4282 C  CD1 . LEU   B 1 233 ? 12.765  -1.724  -35.835 1.00 15.75 ? 245 LEU   B CD1 1 
ATOM   4283 C  CD2 . LEU   B 1 233 ? 12.987  -1.558  -38.333 1.00 12.33 ? 245 LEU   B CD2 1 
ATOM   4284 N  N   . HIS   B 1 234 ? 12.054  -5.469  -35.187 1.00 14.79 ? 246 HIS   B N   1 
ATOM   4285 C  CA  . HIS   B 1 234 ? 10.845  -6.274  -35.176 1.00 17.17 ? 246 HIS   B CA  1 
ATOM   4286 C  C   . HIS   B 1 234 ? 9.681   -5.406  -34.740 1.00 17.64 ? 246 HIS   B C   1 
ATOM   4287 O  O   . HIS   B 1 234 ? 9.862   -4.327  -34.169 1.00 14.61 ? 246 HIS   B O   1 
ATOM   4288 C  CB  . HIS   B 1 234 ? 10.933  -7.475  -34.222 1.00 17.69 ? 246 HIS   B CB  1 
ATOM   4289 C  CG  . HIS   B 1 234 ? 12.127  -8.347  -34.441 1.00 20.03 ? 246 HIS   B CG  1 
ATOM   4290 N  ND1 . HIS   B 1 234 ? 12.030  -9.628  -34.939 1.00 21.42 ? 246 HIS   B ND1 1 
ATOM   4291 C  CD2 . HIS   B 1 234 ? 13.444  -8.135  -34.201 1.00 20.05 ? 246 HIS   B CD2 1 
ATOM   4292 C  CE1 . HIS   B 1 234 ? 13.235  -10.168 -34.999 1.00 20.43 ? 246 HIS   B CE1 1 
ATOM   4293 N  NE2 . HIS   B 1 234 ? 14.111  -9.279  -34.568 1.00 21.45 ? 246 HIS   B NE2 1 
ATOM   4294 N  N   . TYR   B 1 235 ? 8.475   -5.878  -35.029 1.00 17.81 ? 247 TYR   B N   1 
ATOM   4295 C  CA  . TYR   B 1 235 ? 7.312   -5.329  -34.356 1.00 17.77 ? 247 TYR   B CA  1 
ATOM   4296 C  C   . TYR   B 1 235 ? 6.330   -6.447  -34.039 1.00 19.42 ? 247 TYR   B C   1 
ATOM   4297 O  O   . TYR   B 1 235 ? 6.222   -7.437  -34.771 1.00 17.85 ? 247 TYR   B O   1 
ATOM   4298 C  CB  . TYR   B 1 235 ? 6.661   -4.218  -35.194 1.00 19.37 ? 247 TYR   B CB  1 
ATOM   4299 C  CG  . TYR   B 1 235 ? 5.741   -4.694  -36.289 1.00 20.38 ? 247 TYR   B CG  1 
ATOM   4300 C  CD1 . TYR   B 1 235 ? 6.231   -4.999  -37.546 1.00 18.55 ? 247 TYR   B CD1 1 
ATOM   4301 C  CD2 . TYR   B 1 235 ? 4.384   -4.817  -36.066 1.00 19.86 ? 247 TYR   B CD2 1 
ATOM   4302 C  CE1 . TYR   B 1 235 ? 5.380   -5.424  -38.557 1.00 22.51 ? 247 TYR   B CE1 1 
ATOM   4303 C  CE2 . TYR   B 1 235 ? 3.528   -5.243  -37.048 1.00 20.02 ? 247 TYR   B CE2 1 
ATOM   4304 C  CZ  . TYR   B 1 235 ? 4.025   -5.541  -38.291 1.00 23.02 ? 247 TYR   B CZ  1 
ATOM   4305 O  OH  . TYR   B 1 235 ? 3.154   -5.952  -39.261 1.00 28.91 ? 247 TYR   B OH  1 
ATOM   4306 N  N   . LEU   B 1 236 ? 5.647   -6.285  -32.910 1.00 17.67 ? 248 LEU   B N   1 
ATOM   4307 C  CA  . LEU   B 1 236 ? 4.546   -7.143  -32.497 1.00 14.59 ? 248 LEU   B CA  1 
ATOM   4308 C  C   . LEU   B 1 236 ? 3.241   -6.432  -32.821 1.00 14.52 ? 248 LEU   B C   1 
ATOM   4309 O  O   . LEU   B 1 236 ? 3.080   -5.248  -32.502 1.00 15.54 ? 248 LEU   B O   1 
ATOM   4310 C  CB  . LEU   B 1 236 ? 4.634   -7.420  -30.989 1.00 13.43 ? 248 LEU   B CB  1 
ATOM   4311 C  CG  . LEU   B 1 236 ? 3.602   -8.339  -30.323 1.00 17.82 ? 248 LEU   B CG  1 
ATOM   4312 C  CD1 . LEU   B 1 236 ? 3.749   -9.748  -30.845 1.00 16.51 ? 248 LEU   B CD1 1 
ATOM   4313 C  CD2 . LEU   B 1 236 ? 3.816   -8.313  -28.792 1.00 16.84 ? 248 LEU   B CD2 1 
ATOM   4314 N  N   . ASN   B 1 237 ? 2.313   -7.143  -33.463 1.00 15.87 ? 249 ASN   B N   1 
ATOM   4315 C  CA  . ASN   B 1 237 ? 0.984   -6.592  -33.706 1.00 17.92 ? 249 ASN   B CA  1 
ATOM   4316 C  C   . ASN   B 1 237 ? 0.180   -6.687  -32.413 1.00 17.86 ? 249 ASN   B C   1 
ATOM   4317 O  O   . ASN   B 1 237 ? -0.018  -7.776  -31.871 1.00 20.02 ? 249 ASN   B O   1 
ATOM   4318 C  CB  . ASN   B 1 237 ? 0.294   -7.333  -34.855 1.00 14.33 ? 249 ASN   B CB  1 
ATOM   4319 C  CG  . ASN   B 1 237 ? -1.071  -6.761  -35.196 1.00 18.58 ? 249 ASN   B CG  1 
ATOM   4320 O  OD1 . ASN   B 1 237 ? -1.860  -6.409  -34.309 1.00 24.25 ? 249 ASN   B OD1 1 
ATOM   4321 N  ND2 . ASN   B 1 237 ? -1.376  -6.685  -36.506 1.00 20.19 ? 249 ASN   B ND2 1 
ATOM   4322 N  N   . LEU   B 1 238 ? -0.254  -5.547  -31.901 1.00 14.51 ? 250 LEU   B N   1 
ATOM   4323 C  CA  . LEU   B 1 238 ? -0.834  -5.525  -30.572 1.00 19.71 ? 250 LEU   B CA  1 
ATOM   4324 C  C   . LEU   B 1 238 ? -2.324  -5.849  -30.574 1.00 18.61 ? 250 LEU   B C   1 
ATOM   4325 O  O   . LEU   B 1 238 ? -2.934  -5.842  -29.498 1.00 24.17 ? 250 LEU   B O   1 
ATOM   4326 C  CB  . LEU   B 1 238 ? -0.545  -4.168  -29.922 1.00 18.26 ? 250 LEU   B CB  1 
ATOM   4327 C  CG  . LEU   B 1 238 ? 0.950   -3.808  -29.952 1.00 18.49 ? 250 LEU   B CG  1 
ATOM   4328 C  CD1 . LEU   B 1 238 ? 1.209   -2.365  -29.541 1.00 16.65 ? 250 LEU   B CD1 1 
ATOM   4329 C  CD2 . LEU   B 1 238 ? 1.748   -4.765  -29.089 1.00 19.22 ? 250 LEU   B CD2 1 
ATOM   4330 N  N   . ASP   B 1 239 ? -2.912  -6.106  -31.753 1.00 23.50 ? 251 ASP   B N   1 
ATOM   4331 C  CA  . ASP   B 1 239 ? -4.233  -6.709  -31.948 1.00 22.75 ? 251 ASP   B CA  1 
ATOM   4332 C  C   . ASP   B 1 239 ? -4.152  -8.228  -32.082 1.00 24.73 ? 251 ASP   B C   1 
ATOM   4333 O  O   . ASP   B 1 239 ? -4.835  -8.969  -31.364 1.00 24.14 ? 251 ASP   B O   1 
ATOM   4334 C  CB  . ASP   B 1 239 ? -4.897  -6.161  -33.220 1.00 23.38 ? 251 ASP   B CB  1 
ATOM   4335 C  CG  . ASP   B 1 239 ? -5.432  -4.758  -33.059 1.00 25.57 ? 251 ASP   B CG  1 
ATOM   4336 O  OD1 . ASP   B 1 239 ? -5.839  -4.391  -31.938 1.00 28.80 ? 251 ASP   B OD1 1 
ATOM   4337 O  OD2 . ASP   B 1 239 ? -5.484  -4.034  -34.077 1.00 28.49 ? 251 ASP   B OD2 1 
ATOM   4338 N  N   . THR   B 1 240 ? -3.345  -8.696  -33.031 1.00 24.76 ? 252 THR   B N   1 
ATOM   4339 C  CA  . THR   B 1 240 ? -3.273  -10.100 -33.404 1.00 24.55 ? 252 THR   B CA  1 
ATOM   4340 C  C   . THR   B 1 240 ? -2.242  -10.884 -32.610 1.00 22.02 ? 252 THR   B C   1 
ATOM   4341 O  O   . THR   B 1 240 ? -2.296  -12.118 -32.622 1.00 26.32 ? 252 THR   B O   1 
ATOM   4342 C  CB  . THR   B 1 240 ? -2.924  -10.239 -34.887 1.00 22.43 ? 252 THR   B CB  1 
ATOM   4343 O  OG1 . THR   B 1 240 ? -1.511  -10.053 -35.040 1.00 24.70 ? 252 THR   B OG1 1 
ATOM   4344 C  CG2 . THR   B 1 240 ? -3.647  -9.195  -35.698 1.00 26.44 ? 252 THR   B CG2 1 
ATOM   4345 N  N   . TRP   B 1 241 ? -1.299  -10.201 -31.951 1.00 21.39 ? 253 TRP   B N   1 
ATOM   4346 C  CA  . TRP   B 1 241 ? -0.219  -10.843 -31.198 1.00 20.78 ? 253 TRP   B CA  1 
ATOM   4347 C  C   . TRP   B 1 241 ? 0.699   -11.673 -32.098 1.00 22.28 ? 253 TRP   B C   1 
ATOM   4348 O  O   . TRP   B 1 241 ? 1.207   -12.725 -31.704 1.00 25.94 ? 253 TRP   B O   1 
ATOM   4349 C  CB  . TRP   B 1 241 ? -0.781  -11.679 -30.046 1.00 22.57 ? 253 TRP   B CB  1 
ATOM   4350 C  CG  . TRP   B 1 241 ? -1.637  -10.842 -29.174 1.00 24.34 ? 253 TRP   B CG  1 
ATOM   4351 C  CD1 . TRP   B 1 241 ? -2.989  -10.928 -29.019 1.00 22.78 ? 253 TRP   B CD1 1 
ATOM   4352 C  CD2 . TRP   B 1 241 ? -1.212  -9.724  -28.389 1.00 18.48 ? 253 TRP   B CD2 1 
ATOM   4353 N  NE1 . TRP   B 1 241 ? -3.427  -9.953  -28.157 1.00 21.63 ? 253 TRP   B NE1 1 
ATOM   4354 C  CE2 . TRP   B 1 241 ? -2.354  -9.199  -27.761 1.00 21.56 ? 253 TRP   B CE2 1 
ATOM   4355 C  CE3 . TRP   B 1 241 ? 0.032   -9.134  -28.135 1.00 21.98 ? 253 TRP   B CE3 1 
ATOM   4356 C  CZ2 . TRP   B 1 241 ? -2.292  -8.106  -26.898 1.00 24.42 ? 253 TRP   B CZ2 1 
ATOM   4357 C  CZ3 . TRP   B 1 241 ? 0.092   -8.051  -27.274 1.00 20.91 ? 253 TRP   B CZ3 1 
ATOM   4358 C  CH2 . TRP   B 1 241 ? -1.065  -7.547  -26.669 1.00 24.03 ? 253 TRP   B CH2 1 
ATOM   4359 N  N   . GLU   B 1 242 ? 0.962   -11.168 -33.297 1.00 24.56 ? 254 GLU   B N   1 
ATOM   4360 C  CA  . GLU   B 1 242 ? 1.855   -11.804 -34.255 1.00 23.21 ? 254 GLU   B CA  1 
ATOM   4361 C  C   . GLU   B 1 242 ? 3.156   -11.018 -34.346 1.00 19.40 ? 254 GLU   B C   1 
ATOM   4362 O  O   . GLU   B 1 242 ? 3.130   -9.801  -34.542 1.00 18.33 ? 254 GLU   B O   1 
ATOM   4363 C  CB  . GLU   B 1 242 ? 1.203   -11.870 -35.634 1.00 25.54 ? 254 GLU   B CB  1 
ATOM   4364 C  CG  . GLU   B 1 242 ? 2.040   -12.536 -36.688 1.00 27.75 ? 254 GLU   B CG  1 
ATOM   4365 C  CD  . GLU   B 1 242 ? 1.376   -12.443 -38.055 1.00 29.80 ? 254 GLU   B CD  1 
ATOM   4366 O  OE1 . GLU   B 1 242 ? 1.423   -11.349 -38.669 1.00 27.03 ? 254 GLU   B OE1 1 
ATOM   4367 O  OE2 . GLU   B 1 242 ? 0.770   -13.448 -38.491 1.00 36.17 ? 254 GLU   B OE2 1 
ATOM   4368 N  N   . TRP   B 1 243 ? 4.279   -11.717 -34.211 1.00 21.60 ? 255 TRP   B N   1 
ATOM   4369 C  CA  . TRP   B 1 243 ? 5.610   -11.127 -34.340 1.00 20.96 ? 255 TRP   B CA  1 
ATOM   4370 C  C   . TRP   B 1 243 ? 6.045   -11.088 -35.799 1.00 22.21 ? 255 TRP   B C   1 
ATOM   4371 O  O   . TRP   B 1 243 ? 5.916   -12.080 -36.515 1.00 24.86 ? 255 TRP   B O   1 
ATOM   4372 C  CB  . TRP   B 1 243 ? 6.637   -11.944 -33.560 1.00 21.66 ? 255 TRP   B CB  1 
ATOM   4373 C  CG  . TRP   B 1 243 ? 6.802   -11.616 -32.106 1.00 20.29 ? 255 TRP   B CG  1 
ATOM   4374 C  CD1 . TRP   B 1 243 ? 6.467   -12.412 -31.048 1.00 20.69 ? 255 TRP   B CD1 1 
ATOM   4375 C  CD2 . TRP   B 1 243 ? 7.367   -10.421 -31.550 1.00 15.32 ? 255 TRP   B CD2 1 
ATOM   4376 N  NE1 . TRP   B 1 243 ? 6.788   -11.782 -29.867 1.00 19.20 ? 255 TRP   B NE1 1 
ATOM   4377 C  CE2 . TRP   B 1 243 ? 7.336   -10.559 -30.150 1.00 19.05 ? 255 TRP   B CE2 1 
ATOM   4378 C  CE3 . TRP   B 1 243 ? 7.888   -9.250  -32.101 1.00 16.45 ? 255 TRP   B CE3 1 
ATOM   4379 C  CZ2 . TRP   B 1 243 ? 7.821   -9.573  -29.294 1.00 16.87 ? 255 TRP   B CZ2 1 
ATOM   4380 C  CZ3 . TRP   B 1 243 ? 8.356   -8.272  -31.267 1.00 17.16 ? 255 TRP   B CZ3 1 
ATOM   4381 C  CH2 . TRP   B 1 243 ? 8.326   -8.436  -29.870 1.00 15.82 ? 255 TRP   B CH2 1 
ATOM   4382 N  N   . ASN   B 1 244 ? 6.620   -9.960  -36.215 1.00 21.15 ? 256 ASN   B N   1 
ATOM   4383 C  CA  . ASN   B 1 244 ? 7.158   -9.803  -37.560 1.00 23.01 ? 256 ASN   B CA  1 
ATOM   4384 C  C   . ASN   B 1 244 ? 8.573   -9.243  -37.484 1.00 18.82 ? 256 ASN   B C   1 
ATOM   4385 O  O   . ASN   B 1 244 ? 8.829   -8.299  -36.730 1.00 19.37 ? 256 ASN   B O   1 
ATOM   4386 C  CB  . ASN   B 1 244 ? 6.270   -8.874  -38.401 1.00 23.80 ? 256 ASN   B CB  1 
ATOM   4387 C  CG  . ASN   B 1 244 ? 4.832   -9.341  -38.468 1.00 27.55 ? 256 ASN   B CG  1 
ATOM   4388 O  OD1 . ASN   B 1 244 ? 4.459   -10.143 -39.338 1.00 28.71 ? 256 ASN   B OD1 1 
ATOM   4389 N  ND2 . ASN   B 1 244 ? 4.002   -8.821  -37.565 1.00 25.59 ? 256 ASN   B ND2 1 
ATOM   4390 N  N   . GLU   B 1 245 ? 9.489   -9.814  -38.266 1.00 22.89 ? 257 GLU   B N   1 
ATOM   4391 C  CA  . GLU   B 1 245 ? 10.813  -9.223  -38.422 1.00 22.55 ? 257 GLU   B CA  1 
ATOM   4392 C  C   . GLU   B 1 245 ? 10.838  -8.322  -39.650 1.00 24.47 ? 257 GLU   B C   1 
ATOM   4393 O  O   . GLU   B 1 245 ? 10.370  -8.712  -40.726 1.00 26.52 ? 257 GLU   B O   1 
ATOM   4394 C  CB  . GLU   B 1 245 ? 11.911  -10.278 -38.553 1.00 24.82 ? 257 GLU   B CB  1 
ATOM   4395 C  CG  . GLU   B 1 245 ? 13.299  -9.633  -38.471 1.00 26.33 ? 257 GLU   B CG  1 
ATOM   4396 C  CD  . GLU   B 1 245 ? 14.454  -10.597 -38.655 1.00 31.82 ? 257 GLU   B CD  1 
ATOM   4397 O  OE1 . GLU   B 1 245 ? 14.264  -11.664 -39.279 1.00 39.83 ? 257 GLU   B OE1 1 
ATOM   4398 O  OE2 . GLU   B 1 245 ? 15.566  -10.268 -38.183 1.00 31.45 ? 257 GLU   B OE2 1 
ATOM   4399 N  N   . LEU   B 1 246 ? 11.389  -7.124  -39.485 1.00 20.78 ? 258 LEU   B N   1 
ATOM   4400 C  CA  . LEU   B 1 246 ? 11.541  -6.165  -40.568 1.00 20.57 ? 258 LEU   B CA  1 
ATOM   4401 C  C   . LEU   B 1 246 ? 12.968  -6.218  -41.097 1.00 25.53 ? 258 LEU   B C   1 
ATOM   4402 O  O   . LEU   B 1 246 ? 13.929  -6.133  -40.324 1.00 23.30 ? 258 LEU   B O   1 
ATOM   4403 C  CB  . LEU   B 1 246 ? 11.193  -4.755  -40.089 1.00 24.23 ? 258 LEU   B CB  1 
ATOM   4404 C  CG  . LEU   B 1 246 ? 9.717   -4.571  -39.708 1.00 21.54 ? 258 LEU   B CG  1 
ATOM   4405 C  CD1 . LEU   B 1 246 ? 9.509   -3.271  -38.973 1.00 23.74 ? 258 LEU   B CD1 1 
ATOM   4406 C  CD2 . LEU   B 1 246 ? 8.881   -4.586  -40.964 1.00 23.46 ? 258 LEU   B CD2 1 
ATOM   4407 N  N   . ILE   B 1 247 ? 13.095  -6.344  -42.415 1.00 27.09 ? 259 ILE   B N   1 
ATOM   4408 C  CA  . ILE   B 1 247 ? 14.382  -6.423  -43.096 1.00 26.78 ? 259 ILE   B CA  1 
ATOM   4409 C  C   . ILE   B 1 247 ? 14.436  -5.252  -44.074 1.00 26.78 ? 259 ILE   B C   1 
ATOM   4410 O  O   . ILE   B 1 247 ? 14.045  -5.387  -45.248 1.00 27.82 ? 259 ILE   B O   1 
ATOM   4411 C  CB  . ILE   B 1 247 ? 14.553  -7.788  -43.787 1.00 29.11 ? 259 ILE   B CB  1 
ATOM   4412 C  CG1 . ILE   B 1 247 ? 14.639  -8.910  -42.748 1.00 30.47 ? 259 ILE   B CG1 1 
ATOM   4413 C  CG2 . ILE   B 1 247 ? 15.782  -7.809  -44.694 1.00 34.13 ? 259 ILE   B CG2 1 
ATOM   4414 C  CD1 . ILE   B 1 247 ? 15.952  -8.950  -42.021 1.00 30.58 ? 259 ILE   B CD1 1 
ATOM   4415 N  N   . PRO   B 1 248 ? 14.866  -4.076  -43.625 1.00 27.78 ? 260 PRO   B N   1 
ATOM   4416 C  CA  . PRO   B 1 248 ? 14.904  -2.917  -44.520 1.00 26.91 ? 260 PRO   B CA  1 
ATOM   4417 C  C   . PRO   B 1 248 ? 15.951  -3.092  -45.606 1.00 27.87 ? 260 PRO   B C   1 
ATOM   4418 O  O   . PRO   B 1 248 ? 17.017  -3.673  -45.386 1.00 31.81 ? 260 PRO   B O   1 
ATOM   4419 C  CB  . PRO   B 1 248 ? 15.264  -1.750  -43.589 1.00 27.12 ? 260 PRO   B CB  1 
ATOM   4420 C  CG  . PRO   B 1 248 ? 15.090  -2.272  -42.211 1.00 20.77 ? 260 PRO   B CG  1 
ATOM   4421 C  CD  . PRO   B 1 248 ? 15.332  -3.737  -42.270 1.00 25.50 ? 260 PRO   B CD  1 
ATOM   4422 N  N   . GLN   B 1 249 ? 15.637  -2.577  -46.788 1.00 30.10 ? 261 GLN   B N   1 
ATOM   4423 C  CA  . GLN   B 1 249 ? 16.606  -2.573  -47.867 1.00 31.53 ? 261 GLN   B CA  1 
ATOM   4424 C  C   . GLN   B 1 249 ? 17.568  -1.408  -47.690 1.00 26.76 ? 261 GLN   B C   1 
ATOM   4425 O  O   . GLN   B 1 249 ? 17.185  -0.325  -47.232 1.00 25.86 ? 261 GLN   B O   1 
ATOM   4426 C  CB  . GLN   B 1 249 ? 15.910  -2.489  -49.225 1.00 32.55 ? 261 GLN   B CB  1 
ATOM   4427 C  CG  . GLN   B 1 249 ? 14.955  -3.642  -49.538 1.00 41.12 ? 261 GLN   B CG  1 
ATOM   4428 C  CD  . GLN   B 1 249 ? 15.662  -4.955  -49.866 1.00 37.90 ? 261 GLN   B CD  1 
ATOM   4429 O  OE1 . GLN   B 1 249 ? 16.652  -5.322  -49.235 1.00 37.89 ? 261 GLN   B OE1 1 
ATOM   4430 N  NE2 . GLN   B 1 249 ? 15.139  -5.674  -50.853 1.00 40.33 ? 261 GLN   B NE2 1 
ATOM   4431 N  N   . GLY   B 1 250 ? 18.820  -1.641  -48.051 1.00 24.38 ? 262 GLY   B N   1 
ATOM   4432 C  CA  . GLY   B 1 250 ? 19.816  -0.597  -48.039 1.00 21.14 ? 262 GLY   B CA  1 
ATOM   4433 C  C   . GLY   B 1 250 ? 20.552  -0.544  -46.713 1.00 21.59 ? 262 GLY   B C   1 
ATOM   4434 O  O   . GLY   B 1 250 ? 20.539  -1.483  -45.913 1.00 26.52 ? 262 GLY   B O   1 
ATOM   4435 N  N   . ILE   B 1 251 ? 21.187  0.600   -46.477 1.00 20.03 ? 263 ILE   B N   1 
ATOM   4436 C  CA  . ILE   B 1 251 ? 22.031  0.738   -45.299 1.00 17.07 ? 263 ILE   B CA  1 
ATOM   4437 C  C   . ILE   B 1 251 ? 21.157  0.802   -44.052 1.00 18.35 ? 263 ILE   B C   1 
ATOM   4438 O  O   . ILE   B 1 251 ? 20.067  1.381   -44.059 1.00 16.74 ? 263 ILE   B O   1 
ATOM   4439 C  CB  . ILE   B 1 251 ? 22.922  1.986   -45.407 1.00 18.86 ? 263 ILE   B CB  1 
ATOM   4440 C  CG1 . ILE   B 1 251 ? 23.541  2.087   -46.814 1.00 24.01 ? 263 ILE   B CG1 1 
ATOM   4441 C  CG2 . ILE   B 1 251 ? 23.991  1.964   -44.314 1.00 23.48 ? 263 ILE   B CG2 1 
ATOM   4442 C  CD1 . ILE   B 1 251 ? 24.827  1.348   -46.936 1.00 21.61 ? 263 ILE   B CD1 1 
ATOM   4443 N  N   . CYS   B 1 252 ? 21.657  0.221   -42.967 1.00 17.50 ? 264 CYS   B N   1 
ATOM   4444 C  CA  . CYS   B 1 252 ? 20.992  0.167   -41.675 1.00 20.43 ? 264 CYS   B CA  1 
ATOM   4445 C  C   . CYS   B 1 252 ? 21.924  0.681   -40.588 1.00 18.15 ? 264 CYS   B C   1 
ATOM   4446 O  O   . CYS   B 1 252 ? 23.146  0.569   -40.708 1.00 17.56 ? 264 CYS   B O   1 
ATOM   4447 C  CB  . CYS   B 1 252 ? 20.552  -1.268  -41.332 1.00 20.64 ? 264 CYS   B CB  1 
ATOM   4448 S  SG  . CYS   B 1 252 ? 19.320  -1.981  -42.470 1.00 23.52 ? 264 CYS   B SG  1 
ATOM   4449 N  N   . PRO   B 1 253 ? 21.372  1.224   -39.503 1.00 16.63 ? 265 PRO   B N   1 
ATOM   4450 C  CA  . PRO   B 1 253 ? 22.221  1.653   -38.377 1.00 18.28 ? 265 PRO   B CA  1 
ATOM   4451 C  C   . PRO   B 1 253 ? 23.016  0.497   -37.781 1.00 16.01 ? 265 PRO   B C   1 
ATOM   4452 O  O   . PRO   B 1 253 ? 22.612  -0.666  -37.833 1.00 14.65 ? 265 PRO   B O   1 
ATOM   4453 C  CB  . PRO   B 1 253 ? 21.222  2.220   -37.360 1.00 15.55 ? 265 PRO   B CB  1 
ATOM   4454 C  CG  . PRO   B 1 253 ? 19.972  2.526   -38.148 1.00 14.82 ? 265 PRO   B CG  1 
ATOM   4455 C  CD  . PRO   B 1 253 ? 19.949  1.554   -39.309 1.00 19.36 ? 265 PRO   B CD  1 
ATOM   4456 N  N   . VAL   B 1 254 ? 24.195  0.832   -37.258 1.00 16.05 ? 266 VAL   B N   1 
ATOM   4457 C  CA  . VAL   B 1 254 ? 25.037  -0.179  -36.641 1.00 15.84 ? 266 VAL   B CA  1 
ATOM   4458 C  C   . VAL   B 1 254 ? 24.337  -0.698  -35.390 1.00 12.44 ? 266 VAL   B C   1 
ATOM   4459 O  O   . VAL   B 1 254 ? 23.589  0.029   -34.733 1.00 14.70 ? 266 VAL   B O   1 
ATOM   4460 C  CB  . VAL   B 1 254 ? 26.423  0.395   -36.311 1.00 15.53 ? 266 VAL   B CB  1 
ATOM   4461 C  CG1 . VAL   B 1 254 ? 26.316  1.488   -35.232 1.00 15.90 ? 266 VAL   B CG1 1 
ATOM   4462 C  CG2 . VAL   B 1 254 ? 27.381  -0.728  -35.933 1.00 15.81 ? 266 VAL   B CG2 1 
ATOM   4463 N  N   . GLY   B 1 255 ? 24.537  -1.978  -35.090 1.00 11.20 ? 267 GLY   B N   1 
ATOM   4464 C  CA  . GLY   B 1 255 ? 23.865  -2.568  -33.939 1.00 11.31 ? 267 GLY   B CA  1 
ATOM   4465 C  C   . GLY   B 1 255 ? 24.267  -1.874  -32.653 1.00 14.85 ? 267 GLY   B C   1 
ATOM   4466 O  O   . GLY   B 1 255 ? 25.365  -1.332  -32.545 1.00 13.61 ? 267 GLY   B O   1 
ATOM   4467 N  N   . ARG   B 1 256 ? 23.349  -1.856  -31.679 1.00 13.03 ? 268 ARG   B N   1 
ATOM   4468 C  CA  . ARG   B 1 256 ? 23.569  -1.010  -30.513 1.00 10.74 ? 268 ARG   B CA  1 
ATOM   4469 C  C   . ARG   B 1 256 ? 22.609  -1.383  -29.389 1.00 13.66 ? 268 ARG   B C   1 
ATOM   4470 O  O   . ARG   B 1 256 ? 21.543  -1.966  -29.624 1.00 11.50 ? 268 ARG   B O   1 
ATOM   4471 C  CB  . ARG   B 1 256 ? 23.392  0.470   -30.869 1.00 10.25 ? 268 ARG   B CB  1 
ATOM   4472 C  CG  . ARG   B 1 256 ? 21.937  0.766   -31.280 1.00 12.15 ? 268 ARG   B CG  1 
ATOM   4473 C  CD  . ARG   B 1 256 ? 21.778  2.165   -31.850 1.00 16.09 ? 268 ARG   B CD  1 
ATOM   4474 N  NE  . ARG   B 1 256 ? 22.421  2.316   -33.156 1.00 10.75 ? 268 ARG   B NE  1 
ATOM   4475 C  CZ  . ARG   B 1 256 ? 22.752  3.485   -33.687 1.00 14.79 ? 268 ARG   B CZ  1 
ATOM   4476 N  NH1 . ARG   B 1 256 ? 22.494  4.622   -33.063 1.00 13.90 ? 268 ARG   B NH1 1 
ATOM   4477 N  NH2 . ARG   B 1 256 ? 23.346  3.514   -34.886 1.00 16.35 ? 268 ARG   B NH2 1 
ATOM   4478 N  N   . SER   B 1 257 ? 23.019  -1.049  -28.161 1.00 12.52 ? 269 SER   B N   1 
ATOM   4479 C  CA  . SER   B 1 257 ? 22.132  -0.983  -26.999 1.00 14.17 ? 269 SER   B CA  1 
ATOM   4480 C  C   . SER   B 1 257 ? 22.154  0.426   -26.407 1.00 13.57 ? 269 SER   B C   1 
ATOM   4481 O  O   . SER   B 1 257 ? 22.962  1.278   -26.789 1.00 12.86 ? 269 SER   B O   1 
ATOM   4482 C  CB  . SER   B 1 257 ? 22.546  -1.991  -25.928 1.00 11.72 ? 269 SER   B CB  1 
ATOM   4483 O  OG  . SER   B 1 257 ? 23.777  -1.577  -25.342 1.00 15.60 ? 269 SER   B OG  1 
ATOM   4484 N  N   . TRP   B 1 258 ? 21.259  0.670   -25.449 1.00 12.26 ? 270 TRP   B N   1 
ATOM   4485 C  CA  . TRP   B 1 258 ? 21.202  1.931   -24.692 1.00 11.31 ? 270 TRP   B CA  1 
ATOM   4486 C  C   . TRP   B 1 258 ? 20.923  3.157   -25.575 1.00 11.41 ? 270 TRP   B C   1 
ATOM   4487 O  O   . TRP   B 1 258 ? 21.212  4.300   -25.201 1.00 12.62 ? 270 TRP   B O   1 
ATOM   4488 C  CB  . TRP   B 1 258 ? 22.483  2.115   -23.875 1.00 13.84 ? 270 TRP   B CB  1 
ATOM   4489 C  CG  . TRP   B 1 258 ? 22.405  1.416   -22.563 1.00 13.65 ? 270 TRP   B CG  1 
ATOM   4490 C  CD1 . TRP   B 1 258 ? 21.302  1.293   -21.767 1.00 11.74 ? 270 TRP   B CD1 1 
ATOM   4491 C  CD2 . TRP   B 1 258 ? 23.479  0.743   -21.873 1.00 11.55 ? 270 TRP   B CD2 1 
ATOM   4492 N  NE1 . TRP   B 1 258 ? 21.617  0.585   -20.626 1.00 13.66 ? 270 TRP   B NE1 1 
ATOM   4493 C  CE2 . TRP   B 1 258 ? 22.943  0.238   -20.666 1.00 14.41 ? 270 TRP   B CE2 1 
ATOM   4494 C  CE3 . TRP   B 1 258 ? 24.824  0.516   -22.161 1.00 17.11 ? 270 TRP   B CE3 1 
ATOM   4495 C  CZ2 . TRP   B 1 258 ? 23.706  -0.479  -19.746 1.00 14.21 ? 270 TRP   B CZ2 1 
ATOM   4496 C  CZ3 . TRP   B 1 258 ? 25.598  -0.206  -21.232 1.00 14.12 ? 270 TRP   B CZ3 1 
ATOM   4497 C  CH2 . TRP   B 1 258 ? 25.034  -0.680  -20.040 1.00 15.68 ? 270 TRP   B CH2 1 
ATOM   4498 N  N   . HIS   B 1 259 ? 20.313  2.927   -26.727 1.00 14.46 ? 271 HIS   B N   1 
ATOM   4499 C  CA  . HIS   B 1 259 ? 19.849  3.939   -27.659 1.00 13.39 ? 271 HIS   B CA  1 
ATOM   4500 C  C   . HIS   B 1 259 ? 18.407  4.328   -27.333 1.00 13.84 ? 271 HIS   B C   1 
ATOM   4501 O  O   . HIS   B 1 259 ? 17.720  3.659   -26.562 1.00 12.08 ? 271 HIS   B O   1 
ATOM   4502 C  CB  . HIS   B 1 259 ? 19.923  3.367   -29.065 1.00 11.29 ? 271 HIS   B CB  1 
ATOM   4503 C  CG  . HIS   B 1 259 ? 19.221  2.050   -29.199 1.00 13.94 ? 271 HIS   B CG  1 
ATOM   4504 N  ND1 . HIS   B 1 259 ? 19.637  0.906   -28.552 1.00 13.12 ? 271 HIS   B ND1 1 
ATOM   4505 C  CD2 . HIS   B 1 259 ? 18.103  1.704   -29.885 1.00 12.23 ? 271 HIS   B CD2 1 
ATOM   4506 C  CE1 . HIS   B 1 259 ? 18.818  -0.089  -28.846 1.00 14.96 ? 271 HIS   B CE1 1 
ATOM   4507 N  NE2 . HIS   B 1 259 ? 17.890  0.365   -29.670 1.00 10.68 ? 271 HIS   B NE2 1 
ATOM   4508 N  N   . SER   B 1 260 ? 17.918  5.391   -27.968 1.00 13.73 ? 272 SER   B N   1 
ATOM   4509 C  CA  . SER   B 1 260 ? 16.523  5.781   -27.803 1.00 15.86 ? 272 SER   B CA  1 
ATOM   4510 C  C   . SER   B 1 260 ? 15.809  5.623   -29.135 1.00 14.67 ? 272 SER   B C   1 
ATOM   4511 O  O   . SER   B 1 260 ? 16.424  5.808   -30.192 1.00 14.23 ? 272 SER   B O   1 
ATOM   4512 C  CB  . SER   B 1 260 ? 16.387  7.225   -27.283 1.00 16.97 ? 272 SER   B CB  1 
ATOM   4513 O  OG  . SER   B 1 260 ? 16.936  8.170   -28.188 1.00 13.69 ? 272 SER   B OG  1 
ATOM   4514 N  N   . LEU   B 1 261 ? 14.519  5.257   -29.085 1.00 14.49 ? 273 LEU   B N   1 
ATOM   4515 C  CA  . LEU   B 1 261 ? 13.714  5.076   -30.299 1.00 16.58 ? 273 LEU   B CA  1 
ATOM   4516 C  C   . LEU   B 1 261 ? 12.339  5.676   -30.046 1.00 16.74 ? 273 LEU   B C   1 
ATOM   4517 O  O   . LEU   B 1 261 ? 11.625  5.224   -29.142 1.00 16.06 ? 273 LEU   B O   1 
ATOM   4518 C  CB  . LEU   B 1 261 ? 13.584  3.598   -30.692 1.00 13.45 ? 273 LEU   B CB  1 
ATOM   4519 C  CG  . LEU   B 1 261 ? 12.798  3.380   -32.000 1.00 11.73 ? 273 LEU   B CG  1 
ATOM   4520 C  CD1 . LEU   B 1 261 ? 13.656  3.806   -33.151 1.00 16.80 ? 273 LEU   B CD1 1 
ATOM   4521 C  CD2 . LEU   B 1 261 ? 12.294  1.929   -32.160 1.00 14.88 ? 273 LEU   B CD2 1 
ATOM   4522 N  N   . THR   B 1 262 ? 11.976  6.697   -30.821 1.00 15.15 ? 274 THR   B N   1 
ATOM   4523 C  CA  . THR   B 1 262 ? 10.857  7.565   -30.471 1.00 16.34 ? 274 THR   B CA  1 
ATOM   4524 C  C   . THR   B 1 262 ? 9.965   7.797   -31.683 1.00 16.79 ? 274 THR   B C   1 
ATOM   4525 O  O   . THR   B 1 262 ? 10.453  8.300   -32.708 1.00 16.03 ? 274 THR   B O   1 
ATOM   4526 C  CB  . THR   B 1 262 ? 11.416  8.888   -29.939 1.00 17.16 ? 274 THR   B CB  1 
ATOM   4527 O  OG1 . THR   B 1 262 ? 12.318  8.623   -28.851 1.00 19.54 ? 274 THR   B OG1 1 
ATOM   4528 C  CG2 . THR   B 1 262 ? 10.303  9.795   -29.454 1.00 21.53 ? 274 THR   B CG2 1 
ATOM   4529 N  N   . PRO   B 1 263 ? 8.667   7.484   -31.629 1.00 16.52 ? 275 PRO   B N   1 
ATOM   4530 C  CA  . PRO   B 1 263 ? 7.800   7.834   -32.765 1.00 15.03 ? 275 PRO   B CA  1 
ATOM   4531 C  C   . PRO   B 1 263 ? 7.672   9.343   -32.879 1.00 19.22 ? 275 PRO   B C   1 
ATOM   4532 O  O   . PRO   B 1 263 ? 7.524   10.049  -31.878 1.00 20.23 ? 275 PRO   B O   1 
ATOM   4533 C  CB  . PRO   B 1 263 ? 6.456   7.175   -32.415 1.00 16.79 ? 275 PRO   B CB  1 
ATOM   4534 C  CG  . PRO   B 1 263 ? 6.806   6.128   -31.380 1.00 17.04 ? 275 PRO   B CG  1 
ATOM   4535 C  CD  . PRO   B 1 263 ? 7.910   6.777   -30.586 1.00 15.55 ? 275 PRO   B CD  1 
ATOM   4536 N  N   . VAL   B 1 264 ? 7.761   9.837   -34.115 1.00 16.23 ? 276 VAL   B N   1 
ATOM   4537 C  CA  . VAL   B 1 264 ? 7.722   11.266  -34.388 1.00 18.71 ? 276 VAL   B CA  1 
ATOM   4538 C  C   . VAL   B 1 264 ? 6.668   11.615  -35.430 1.00 23.29 ? 276 VAL   B C   1 
ATOM   4539 O  O   . VAL   B 1 264 ? 6.543   12.782  -35.807 1.00 26.25 ? 276 VAL   B O   1 
ATOM   4540 C  CB  . VAL   B 1 264 ? 9.110   11.805  -34.815 1.00 20.04 ? 276 VAL   B CB  1 
ATOM   4541 C  CG1 . VAL   B 1 264 ? 10.101  11.774  -33.650 1.00 20.53 ? 276 VAL   B CG1 1 
ATOM   4542 C  CG2 . VAL   B 1 264 ? 9.658   11.018  -35.978 1.00 23.35 ? 276 VAL   B CG2 1 
ATOM   4543 N  N   . SER   B 1 265 ? 5.892   10.636  -35.878 1.00 21.20 ? 277 SER   B N   1 
ATOM   4544 C  CA  . SER   B 1 265 ? 4.753   10.792  -36.776 1.00 22.02 ? 277 SER   B CA  1 
ATOM   4545 C  C   . SER   B 1 265 ? 4.072   9.432   -36.831 1.00 22.50 ? 277 SER   B C   1 
ATOM   4546 O  O   . SER   B 1 265 ? 4.515   8.472   -36.191 1.00 24.06 ? 277 SER   B O   1 
ATOM   4547 C  CB  . SER   B 1 265 ? 5.165   11.254  -38.177 1.00 22.52 ? 277 SER   B CB  1 
ATOM   4548 O  OG  . SER   B 1 265 ? 5.628   10.145  -38.923 1.00 22.85 ? 277 SER   B OG  1 
ATOM   4549 N  N   . SER   B 1 266 ? 2.997   9.348   -37.617 1.00 22.11 ? 278 SER   B N   1 
ATOM   4550 C  CA  . SER   B 1 266 ? 2.360   8.062   -37.857 1.00 24.01 ? 278 SER   B CA  1 
ATOM   4551 C  C   . SER   B 1 266 ? 3.199   7.160   -38.739 1.00 20.08 ? 278 SER   B C   1 
ATOM   4552 O  O   . SER   B 1 266 ? 2.805   6.014   -38.989 1.00 23.33 ? 278 SER   B O   1 
ATOM   4553 C  CB  . SER   B 1 266 ? 0.985   8.256   -38.509 1.00 24.64 ? 278 SER   B CB  1 
ATOM   4554 O  OG  . SER   B 1 266 ? 1.098   8.897   -39.779 1.00 28.52 ? 278 SER   B OG  1 
ATOM   4555 N  N   . ASP   B 1 267 ? 4.321   7.652   -39.247 1.00 19.42 ? 279 ASP   B N   1 
ATOM   4556 C  CA  . ASP   B 1 267 ? 5.066   6.872   -40.214 1.00 18.42 ? 279 ASP   B CA  1 
ATOM   4557 C  C   . ASP   B 1 267 ? 6.573   6.933   -39.979 1.00 19.20 ? 279 ASP   B C   1 
ATOM   4558 O  O   . ASP   B 1 267 ? 7.331   6.451   -40.831 1.00 18.21 ? 279 ASP   B O   1 
ATOM   4559 C  CB  . ASP   B 1 267 ? 4.698   7.361   -41.627 1.00 21.23 ? 279 ASP   B CB  1 
ATOM   4560 C  CG  . ASP   B 1 267 ? 5.257   6.477   -42.713 1.00 23.19 ? 279 ASP   B CG  1 
ATOM   4561 O  OD1 . ASP   B 1 267 ? 5.229   5.237   -42.537 1.00 20.66 ? 279 ASP   B OD1 1 
ATOM   4562 O  OD2 . ASP   B 1 267 ? 5.726   7.035   -43.730 1.00 25.20 ? 279 ASP   B OD2 1 
ATOM   4563 N  N   . HIS   B 1 268 ? 7.041   7.484   -38.847 1.00 19.59 ? 280 HIS   B N   1 
ATOM   4564 C  CA  . HIS   B 1 268 ? 8.476   7.643   -38.624 1.00 18.05 ? 280 HIS   B CA  1 
ATOM   4565 C  C   . HIS   B 1 268 ? 8.880   7.405   -37.171 1.00 18.16 ? 280 HIS   B C   1 
ATOM   4566 O  O   . HIS   B 1 268 ? 8.226   7.880   -36.239 1.00 23.12 ? 280 HIS   B O   1 
ATOM   4567 C  CB  . HIS   B 1 268 ? 8.952   9.039   -39.017 1.00 21.18 ? 280 HIS   B CB  1 
ATOM   4568 C  CG  . HIS   B 1 268 ? 8.826   9.324   -40.478 1.00 23.44 ? 280 HIS   B CG  1 
ATOM   4569 N  ND1 . HIS   B 1 268 ? 7.724   9.952   -41.014 1.00 25.27 ? 280 HIS   B ND1 1 
ATOM   4570 C  CD2 . HIS   B 1 268 ? 9.651   9.057   -41.514 1.00 22.21 ? 280 HIS   B CD2 1 
ATOM   4571 C  CE1 . HIS   B 1 268 ? 7.880   10.072  -42.319 1.00 22.22 ? 280 HIS   B CE1 1 
ATOM   4572 N  NE2 . HIS   B 1 268 ? 9.037   9.531   -42.650 1.00 22.78 ? 280 HIS   B NE2 1 
ATOM   4573 N  N   . LEU   B 1 269 ? 9.987   6.696   -36.992 1.00 18.29 ? 281 LEU   B N   1 
ATOM   4574 C  CA  . LEU   B 1 269 ? 10.591  6.493   -35.683 1.00 16.46 ? 281 LEU   B CA  1 
ATOM   4575 C  C   . LEU   B 1 269 ? 11.937  7.196   -35.675 1.00 19.99 ? 281 LEU   B C   1 
ATOM   4576 O  O   . LEU   B 1 269 ? 12.648  7.186   -36.677 1.00 18.76 ? 281 LEU   B O   1 
ATOM   4577 C  CB  . LEU   B 1 269 ? 10.768  5.003   -35.369 1.00 16.34 ? 281 LEU   B CB  1 
ATOM   4578 C  CG  . LEU   B 1 269 ? 9.578   4.075   -35.649 1.00 14.04 ? 281 LEU   B CG  1 
ATOM   4579 C  CD1 . LEU   B 1 269 ? 9.941   2.611   -35.451 1.00 14.62 ? 281 LEU   B CD1 1 
ATOM   4580 C  CD2 . LEU   B 1 269 ? 8.322   4.460   -34.889 1.00 17.22 ? 281 LEU   B CD2 1 
ATOM   4581 N  N   . PHE   B 1 270 ? 12.283  7.826   -34.558 1.00 18.45 ? 282 PHE   B N   1 
ATOM   4582 C  CA  . PHE   B 1 270 ? 13.536  8.557   -34.458 1.00 15.59 ? 282 PHE   B CA  1 
ATOM   4583 C  C   . PHE   B 1 270 ? 14.480  7.806   -33.531 1.00 17.39 ? 282 PHE   B C   1 
ATOM   4584 O  O   . PHE   B 1 270 ? 14.134  7.514   -32.377 1.00 14.74 ? 282 PHE   B O   1 
ATOM   4585 C  CB  . PHE   B 1 270 ? 13.312  9.995   -33.974 1.00 14.68 ? 282 PHE   B CB  1 
ATOM   4586 C  CG  . PHE   B 1 270 ? 14.567  10.798  -33.898 1.00 16.46 ? 282 PHE   B CG  1 
ATOM   4587 C  CD1 . PHE   B 1 270 ? 15.079  11.428  -35.020 1.00 19.47 ? 282 PHE   B CD1 1 
ATOM   4588 C  CD2 . PHE   B 1 270 ? 15.257  10.915  -32.695 1.00 16.92 ? 282 PHE   B CD2 1 
ATOM   4589 C  CE1 . PHE   B 1 270 ? 16.251  12.172  -34.936 1.00 17.60 ? 282 PHE   B CE1 1 
ATOM   4590 C  CE2 . PHE   B 1 270 ? 16.430  11.641  -32.618 1.00 19.40 ? 282 PHE   B CE2 1 
ATOM   4591 C  CZ  . PHE   B 1 270 ? 16.923  12.271  -33.743 1.00 19.76 ? 282 PHE   B CZ  1 
ATOM   4592 N  N   . LEU   B 1 271 ? 15.672  7.512   -34.039 1.00 14.00 ? 283 LEU   B N   1 
ATOM   4593 C  CA  . LEU   B 1 271 ? 16.675  6.703   -33.368 1.00 15.22 ? 283 LEU   B CA  1 
ATOM   4594 C  C   . LEU   B 1 271 ? 17.874  7.577   -33.027 1.00 15.87 ? 283 LEU   B C   1 
ATOM   4595 O  O   . LEU   B 1 271 ? 18.355  8.329   -33.882 1.00 16.28 ? 283 LEU   B O   1 
ATOM   4596 C  CB  . LEU   B 1 271 ? 17.098  5.535   -34.269 1.00 16.34 ? 283 LEU   B CB  1 
ATOM   4597 C  CG  . LEU   B 1 271 ? 18.376  4.836   -33.821 1.00 17.65 ? 283 LEU   B CG  1 
ATOM   4598 C  CD1 . LEU   B 1 271 ? 18.082  3.984   -32.609 1.00 14.16 ? 283 LEU   B CD1 1 
ATOM   4599 C  CD2 . LEU   B 1 271 ? 19.006  4.020   -34.935 1.00 15.42 ? 283 LEU   B CD2 1 
ATOM   4600 N  N   . PHE   B 1 272 ? 18.350  7.502   -31.785 1.00 12.46 ? 284 PHE   B N   1 
ATOM   4601 C  CA  . PHE   B 1 272 ? 19.528  8.289   -31.433 1.00 14.41 ? 284 PHE   B CA  1 
ATOM   4602 C  C   . PHE   B 1 272 ? 20.428  7.594   -30.425 1.00 17.73 ? 284 PHE   B C   1 
ATOM   4603 O  O   . PHE   B 1 272 ? 19.967  7.108   -29.390 1.00 17.02 ? 284 PHE   B O   1 
ATOM   4604 C  CB  . PHE   B 1 272 ? 19.160  9.662   -30.866 1.00 14.16 ? 284 PHE   B CB  1 
ATOM   4605 C  CG  . PHE   B 1 272 ? 20.353  10.438  -30.370 1.00 15.14 ? 284 PHE   B CG  1 
ATOM   4606 C  CD1 . PHE   B 1 272 ? 21.278  10.937  -31.278 1.00 17.49 ? 284 PHE   B CD1 1 
ATOM   4607 C  CD2 . PHE   B 1 272 ? 20.564  10.648  -29.006 1.00 17.73 ? 284 PHE   B CD2 1 
ATOM   4608 C  CE1 . PHE   B 1 272 ? 22.384  11.651  -30.849 1.00 17.07 ? 284 PHE   B CE1 1 
ATOM   4609 C  CE2 . PHE   B 1 272 ? 21.673  11.363  -28.565 1.00 19.81 ? 284 PHE   B CE2 1 
ATOM   4610 C  CZ  . PHE   B 1 272 ? 22.588  11.860  -29.487 1.00 20.78 ? 284 PHE   B CZ  1 
ATOM   4611 N  N   . GLY   B 1 273 ? 21.732  7.620   -30.719 1.00 14.09 ? 285 GLY   B N   1 
ATOM   4612 C  CA  . GLY   B 1 273 ? 22.752  7.291   -29.753 1.00 17.60 ? 285 GLY   B CA  1 
ATOM   4613 C  C   . GLY   B 1 273 ? 22.908  5.804   -29.508 1.00 15.02 ? 285 GLY   B C   1 
ATOM   4614 O  O   . GLY   B 1 273 ? 22.596  4.953   -30.341 1.00 15.95 ? 285 GLY   B O   1 
ATOM   4615 N  N   . GLY   B 1 274 ? 23.448  5.499   -28.341 1.00 12.68 ? 286 GLY   B N   1 
ATOM   4616 C  CA  . GLY   B 1 274 ? 23.646  4.133   -27.938 1.00 12.97 ? 286 GLY   B CA  1 
ATOM   4617 C  C   . GLY   B 1 274 ? 25.103  3.720   -27.938 1.00 12.00 ? 286 GLY   B C   1 
ATOM   4618 O  O   . GLY   B 1 274 ? 26.023  4.543   -27.899 1.00 15.23 ? 286 GLY   B O   1 
ATOM   4619 N  N   . PHE   B 1 275 ? 25.303  2.408   -27.987 1.00 13.57 ? 287 PHE   B N   1 
ATOM   4620 C  CA  . PHE   B 1 275 ? 26.562  1.786   -27.599 1.00 15.62 ? 287 PHE   B CA  1 
ATOM   4621 C  C   . PHE   B 1 275 ? 26.741  0.541   -28.454 1.00 11.63 ? 287 PHE   B C   1 
ATOM   4622 O  O   . PHE   B 1 275 ? 25.858  -0.319  -28.489 1.00 14.50 ? 287 PHE   B O   1 
ATOM   4623 C  CB  . PHE   B 1 275 ? 26.492  1.454   -26.093 1.00 15.93 ? 287 PHE   B CB  1 
ATOM   4624 C  CG  . PHE   B 1 275 ? 27.798  1.095   -25.450 1.00 16.11 ? 287 PHE   B CG  1 
ATOM   4625 C  CD1 . PHE   B 1 275 ? 28.951  1.827   -25.694 1.00 18.66 ? 287 PHE   B CD1 1 
ATOM   4626 C  CD2 . PHE   B 1 275 ? 27.858  0.031   -24.560 1.00 17.96 ? 287 PHE   B CD2 1 
ATOM   4627 C  CE1 . PHE   B 1 275 ? 30.138  1.500   -25.066 1.00 21.90 ? 287 PHE   B CE1 1 
ATOM   4628 C  CE2 . PHE   B 1 275 ? 29.050  -0.315  -23.938 1.00 18.53 ? 287 PHE   B CE2 1 
ATOM   4629 C  CZ  . PHE   B 1 275 ? 30.191  0.413   -24.192 1.00 17.43 ? 287 PHE   B CZ  1 
ATOM   4630 N  N   . THR   B 1 276 ? 27.868  0.438   -29.137 1.00 14.57 ? 288 THR   B N   1 
ATOM   4631 C  CA  . THR   B 1 276 ? 28.054  -0.640  -30.099 1.00 14.72 ? 288 THR   B CA  1 
ATOM   4632 C  C   . THR   B 1 276 ? 28.629  -1.888  -29.430 1.00 16.46 ? 288 THR   B C   1 
ATOM   4633 O  O   . THR   B 1 276 ? 29.075  -1.869  -28.280 1.00 16.55 ? 288 THR   B O   1 
ATOM   4634 C  CB  . THR   B 1 276 ? 28.971  -0.197  -31.237 1.00 19.04 ? 288 THR   B CB  1 
ATOM   4635 O  OG1 . THR   B 1 276 ? 30.310  -0.063  -30.737 1.00 17.60 ? 288 THR   B OG1 1 
ATOM   4636 C  CG2 . THR   B 1 276 ? 28.517  1.126   -31.797 1.00 17.21 ? 288 THR   B CG2 1 
ATOM   4637 N  N   . THR   B 1 277 ? 28.624  -2.985  -30.186 1.00 14.70 ? 289 THR   B N   1 
ATOM   4638 C  CA  . THR   B 1 277 ? 29.226  -4.231  -29.718 1.00 19.26 ? 289 THR   B CA  1 
ATOM   4639 C  C   . THR   B 1 277 ? 30.668  -4.008  -29.274 1.00 19.90 ? 289 THR   B C   1 
ATOM   4640 O  O   . THR   B 1 277 ? 31.093  -4.509  -28.221 1.00 20.04 ? 289 THR   B O   1 
ATOM   4641 C  CB  . THR   B 1 277 ? 29.169  -5.293  -30.827 1.00 18.60 ? 289 THR   B CB  1 
ATOM   4642 O  OG1 . THR   B 1 277 ? 27.809  -5.647  -31.102 1.00 17.40 ? 289 THR   B OG1 1 
ATOM   4643 C  CG2 . THR   B 1 277 ? 29.921  -6.558  -30.412 1.00 17.27 ? 289 THR   B CG2 1 
ATOM   4644 N  N   . ASP   B 1 278 ? 31.414  -3.225  -30.049 1.00 20.62 ? 290 ASP   B N   1 
ATOM   4645 C  CA  . ASP   B 1 278 ? 32.809  -2.871  -29.805 1.00 21.52 ? 290 ASP   B CA  1 
ATOM   4646 C  C   . ASP   B 1 278 ? 32.960  -1.694  -28.860 1.00 20.51 ? 290 ASP   B C   1 
ATOM   4647 O  O   . ASP   B 1 278 ? 33.984  -1.000  -28.912 1.00 25.94 ? 290 ASP   B O   1 
ATOM   4648 C  CB  . ASP   B 1 278 ? 33.507  -2.556  -31.134 1.00 26.00 ? 290 ASP   B CB  1 
ATOM   4649 C  CG  . ASP   B 1 278 ? 33.507  -3.737  -32.081 1.00 31.11 ? 290 ASP   B CG  1 
ATOM   4650 O  OD1 . ASP   B 1 278 ? 33.681  -4.881  -31.608 1.00 31.94 ? 290 ASP   B OD1 1 
ATOM   4651 O  OD2 . ASP   B 1 278 ? 33.326  -3.523  -33.300 1.00 35.15 ? 290 ASP   B OD2 1 
ATOM   4652 N  N   . LYS   B 1 279 ? 31.944  -1.438  -28.038 1.00 20.75 ? 291 LYS   B N   1 
ATOM   4653 C  CA  . LYS   B 1 279 ? 32.015  -0.454  -26.967 1.00 20.19 ? 291 LYS   B CA  1 
ATOM   4654 C  C   . LYS   B 1 279 ? 32.321  0.948   -27.491 1.00 20.46 ? 291 LYS   B C   1 
ATOM   4655 O  O   . LYS   B 1 279 ? 33.045  1.717   -26.855 1.00 26.05 ? 291 LYS   B O   1 
ATOM   4656 C  CB  . LYS   B 1 279 ? 33.028  -0.901  -25.907 1.00 19.51 ? 291 LYS   B CB  1 
ATOM   4657 C  CG  . LYS   B 1 279 ? 32.786  -2.360  -25.496 1.00 21.65 ? 291 LYS   B CG  1 
ATOM   4658 C  CD  . LYS   B 1 279 ? 33.357  -2.742  -24.134 1.00 21.73 ? 291 LYS   B CD  1 
ATOM   4659 C  CE  . LYS   B 1 279 ? 32.425  -3.764  -23.452 1.00 29.07 ? 291 LYS   B CE  1 
ATOM   4660 N  NZ  . LYS   B 1 279 ? 32.814  -4.151  -22.058 1.00 23.91 ? 291 LYS   B NZ  1 
ATOM   4661 N  N   . GLN   B 1 280 ? 31.724  1.303   -28.645 1.00 17.97 ? 292 GLN   B N   1 
ATOM   4662 C  CA  . GLN   B 1 280 ? 31.819  2.656   -29.171 1.00 18.79 ? 292 GLN   B CA  1 
ATOM   4663 C  C   . GLN   B 1 280 ? 30.579  3.452   -28.789 1.00 20.80 ? 292 GLN   B C   1 
ATOM   4664 O  O   . GLN   B 1 280 ? 29.459  3.041   -29.140 1.00 16.30 ? 292 GLN   B O   1 
ATOM   4665 C  CB  . GLN   B 1 280 ? 31.983  2.641   -30.688 1.00 19.59 ? 292 GLN   B CB  1 
ATOM   4666 C  CG  . GLN   B 1 280 ? 32.804  3.798   -31.226 1.00 24.97 ? 292 GLN   B CG  1 
ATOM   4667 C  CD  . GLN   B 1 280 ? 34.302  3.603   -31.001 1.00 23.74 ? 292 GLN   B CD  1 
ATOM   4668 O  OE1 . GLN   B 1 280 ? 35.101  4.504   -31.253 1.00 29.22 ? 292 GLN   B OE1 1 
ATOM   4669 N  NE2 . GLN   B 1 280 ? 34.685  2.419   -30.529 1.00 31.75 ? 292 GLN   B NE2 1 
ATOM   4670 N  N   . PRO   B 1 281 ? 30.721  4.568   -28.071 1.00 19.39 ? 293 PRO   B N   1 
ATOM   4671 C  CA  . PRO   B 1 281 ? 29.580  5.470   -27.854 1.00 18.83 ? 293 PRO   B CA  1 
ATOM   4672 C  C   . PRO   B 1 281 ? 29.118  6.101   -29.162 1.00 18.38 ? 293 PRO   B C   1 
ATOM   4673 O  O   . PRO   B 1 281 ? 29.937  6.536   -29.970 1.00 18.02 ? 293 PRO   B O   1 
ATOM   4674 C  CB  . PRO   B 1 281 ? 30.150  6.533   -26.904 1.00 19.60 ? 293 PRO   B CB  1 
ATOM   4675 C  CG  . PRO   B 1 281 ? 31.395  5.938   -26.347 1.00 17.53 ? 293 PRO   B CG  1 
ATOM   4676 C  CD  . PRO   B 1 281 ? 31.940  5.054   -27.406 1.00 22.70 ? 293 PRO   B CD  1 
ATOM   4677 N  N   . LEU   B 1 282 ? 27.793  6.221   -29.332 1.00 15.58 ? 294 LEU   B N   1 
ATOM   4678 C  CA  . LEU   B 1 282 ? 27.184  6.649   -30.591 1.00 17.84 ? 294 LEU   B CA  1 
ATOM   4679 C  C   . LEU   B 1 282 ? 26.541  8.026   -30.487 1.00 15.80 ? 294 LEU   B C   1 
ATOM   4680 O  O   . LEU   B 1 282 ? 25.872  8.340   -29.495 1.00 14.52 ? 294 LEU   B O   1 
ATOM   4681 C  CB  . LEU   B 1 282 ? 26.122  5.648   -31.048 1.00 15.91 ? 294 LEU   B CB  1 
ATOM   4682 C  CG  . LEU   B 1 282 ? 26.704  4.313   -31.504 1.00 18.25 ? 294 LEU   B CG  1 
ATOM   4683 C  CD1 . LEU   B 1 282 ? 25.647  3.256   -31.790 1.00 16.01 ? 294 LEU   B CD1 1 
ATOM   4684 C  CD2 . LEU   B 1 282 ? 27.612  4.536   -32.694 1.00 19.70 ? 294 LEU   B CD2 1 
ATOM   4685 N  N   . SER   B 1 283 ? 26.729  8.833   -31.543 1.00 15.30 ? 295 SER   B N   1 
ATOM   4686 C  CA  . SER   B 1 283 ? 26.068  10.120  -31.698 1.00 15.74 ? 295 SER   B CA  1 
ATOM   4687 C  C   . SER   B 1 283 ? 25.346  10.232  -33.038 1.00 15.88 ? 295 SER   B C   1 
ATOM   4688 O  O   . SER   B 1 283 ? 24.968  11.337  -33.423 1.00 18.62 ? 295 SER   B O   1 
ATOM   4689 C  CB  . SER   B 1 283 ? 27.064  11.283  -31.549 1.00 20.02 ? 295 SER   B CB  1 
ATOM   4690 O  OG  . SER   B 1 283 ? 28.134  11.181  -32.481 1.00 23.40 ? 295 SER   B OG  1 
ATOM   4691 N  N   . ASP   B 1 284 ? 25.159  9.128   -33.755 1.00 17.51 ? 296 ASP   B N   1 
ATOM   4692 C  CA  . ASP   B 1 284 ? 24.379  9.156   -34.989 1.00 17.84 ? 296 ASP   B CA  1 
ATOM   4693 C  C   . ASP   B 1 284 ? 22.882  9.161   -34.690 1.00 17.67 ? 296 ASP   B C   1 
ATOM   4694 O  O   . ASP   B 1 284 ? 22.425  8.669   -33.658 1.00 18.58 ? 296 ASP   B O   1 
ATOM   4695 C  CB  . ASP   B 1 284 ? 24.733  7.978   -35.906 1.00 15.73 ? 296 ASP   B CB  1 
ATOM   4696 C  CG  . ASP   B 1 284 ? 24.494  6.629   -35.279 1.00 16.80 ? 296 ASP   B CG  1 
ATOM   4697 O  OD1 . ASP   B 1 284 ? 24.682  6.450   -34.055 1.00 18.88 ? 296 ASP   B OD1 1 
ATOM   4698 O  OD2 . ASP   B 1 284 ? 24.149  5.702   -36.022 1.00 19.35 ? 296 ASP   B OD2 1 
ATOM   4699 N  N   . ALA   B 1 285 ? 22.116  9.738   -35.610 1.00 16.76 ? 297 ALA   B N   1 
ATOM   4700 C  CA  . ALA   B 1 285 ? 20.668  9.818   -35.495 1.00 17.29 ? 297 ALA   B CA  1 
ATOM   4701 C  C   . ALA   B 1 285 ? 20.045  9.393   -36.813 1.00 16.19 ? 297 ALA   B C   1 
ATOM   4702 O  O   . ALA   B 1 285 ? 20.595  9.680   -37.877 1.00 18.06 ? 297 ALA   B O   1 
ATOM   4703 C  CB  . ALA   B 1 285 ? 20.203  11.231  -35.146 1.00 18.42 ? 297 ALA   B CB  1 
ATOM   4704 N  N   . TRP   B 1 286 ? 18.916  8.691   -36.738 1.00 13.29 ? 298 TRP   B N   1 
ATOM   4705 C  CA  . TRP   B 1 286 ? 18.225  8.207   -37.928 1.00 15.68 ? 298 TRP   B CA  1 
ATOM   4706 C  C   . TRP   B 1 286 ? 16.716  8.343   -37.765 1.00 16.65 ? 298 TRP   B C   1 
ATOM   4707 O  O   . TRP   B 1 286 ? 16.178  8.429   -36.645 1.00 13.50 ? 298 TRP   B O   1 
ATOM   4708 C  CB  . TRP   B 1 286 ? 18.518  6.726   -38.232 1.00 15.29 ? 298 TRP   B CB  1 
ATOM   4709 C  CG  . TRP   B 1 286 ? 19.959  6.353   -38.371 1.00 18.03 ? 298 TRP   B CG  1 
ATOM   4710 C  CD1 . TRP   B 1 286 ? 20.917  6.422   -37.411 1.00 16.92 ? 298 TRP   B CD1 1 
ATOM   4711 C  CD2 . TRP   B 1 286 ? 20.592  5.794   -39.531 1.00 17.08 ? 298 TRP   B CD2 1 
ATOM   4712 N  NE1 . TRP   B 1 286 ? 22.124  5.971   -37.902 1.00 15.23 ? 298 TRP   B NE1 1 
ATOM   4713 C  CE2 . TRP   B 1 286 ? 21.947  5.584   -39.208 1.00 15.46 ? 298 TRP   B CE2 1 
ATOM   4714 C  CE3 . TRP   B 1 286 ? 20.147  5.458   -40.812 1.00 17.44 ? 298 TRP   B CE3 1 
ATOM   4715 C  CZ2 . TRP   B 1 286 ? 22.859  5.043   -40.114 1.00 16.13 ? 298 TRP   B CZ2 1 
ATOM   4716 C  CZ3 . TRP   B 1 286 ? 21.051  4.937   -41.713 1.00 16.33 ? 298 TRP   B CZ3 1 
ATOM   4717 C  CH2 . TRP   B 1 286 ? 22.391  4.728   -41.366 1.00 17.67 ? 298 TRP   B CH2 1 
ATOM   4718 N  N   . THR   B 1 287 ? 16.029  8.306   -38.907 1.00 15.42 ? 299 THR   B N   1 
ATOM   4719 C  CA  . THR   B 1 287 ? 14.609  7.979   -38.920 1.00 19.49 ? 299 THR   B CA  1 
ATOM   4720 C  C   . THR   B 1 287 ? 14.398  6.647   -39.626 1.00 20.92 ? 299 THR   B C   1 
ATOM   4721 O  O   . THR   B 1 287 ? 15.018  6.372   -40.662 1.00 18.41 ? 299 THR   B O   1 
ATOM   4722 C  CB  . THR   B 1 287 ? 13.763  9.063   -39.605 1.00 20.64 ? 299 THR   B CB  1 
ATOM   4723 O  OG1 . THR   B 1 287 ? 14.172  9.202   -40.974 1.00 23.53 ? 299 THR   B OG1 1 
ATOM   4724 C  CG2 . THR   B 1 287 ? 13.912  10.396  -38.887 1.00 22.25 ? 299 THR   B CG2 1 
ATOM   4725 N  N   . TYR   B 1 288 ? 13.533  5.813   -39.056 1.00 19.14 ? 300 TYR   B N   1 
ATOM   4726 C  CA  . TYR   B 1 288 ? 13.008  4.656   -39.762 1.00 16.34 ? 300 TYR   B CA  1 
ATOM   4727 C  C   . TYR   B 1 288 ? 11.668  5.045   -40.375 1.00 18.43 ? 300 TYR   B C   1 
ATOM   4728 O  O   . TYR   B 1 288 ? 10.768  5.531   -39.676 1.00 19.94 ? 300 TYR   B O   1 
ATOM   4729 C  CB  . TYR   B 1 288 ? 12.863  3.441   -38.853 1.00 17.22 ? 300 TYR   B CB  1 
ATOM   4730 C  CG  . TYR   B 1 288 ? 12.241  2.253   -39.543 1.00 15.53 ? 300 TYR   B CG  1 
ATOM   4731 C  CD1 . TYR   B 1 288 ? 12.935  1.548   -40.522 1.00 18.80 ? 300 TYR   B CD1 1 
ATOM   4732 C  CD2 . TYR   B 1 288 ? 10.945  1.850   -39.230 1.00 15.77 ? 300 TYR   B CD2 1 
ATOM   4733 C  CE1 . TYR   B 1 288 ? 12.357  0.464   -41.161 1.00 20.26 ? 300 TYR   B CE1 1 
ATOM   4734 C  CE2 . TYR   B 1 288 ? 10.379  0.768   -39.828 1.00 18.42 ? 300 TYR   B CE2 1 
ATOM   4735 C  CZ  . TYR   B 1 288 ? 11.080  0.078   -40.810 1.00 17.18 ? 300 TYR   B CZ  1 
ATOM   4736 O  OH  . TYR   B 1 288 ? 10.464  -1.001  -41.407 1.00 18.90 ? 300 TYR   B OH  1 
ATOM   4737 N  N   . CYS   B 1 289 ? 11.564  4.901   -41.688 1.00 16.99 ? 301 CYS   B N   1 
ATOM   4738 C  CA  . CYS   B 1 289 ? 10.338  5.227   -42.395 1.00 17.36 ? 301 CYS   B CA  1 
ATOM   4739 C  C   . CYS   B 1 289 ? 9.514   3.951   -42.495 1.00 19.51 ? 301 CYS   B C   1 
ATOM   4740 O  O   . CYS   B 1 289 ? 9.901   3.001   -43.185 1.00 21.52 ? 301 CYS   B O   1 
ATOM   4741 C  CB  . CYS   B 1 289 ? 10.634  5.824   -43.770 1.00 16.28 ? 301 CYS   B CB  1 
ATOM   4742 S  SG  . CYS   B 1 289 ? 9.110   6.198   -44.669 1.00 26.63 ? 301 CYS   B SG  1 
ATOM   4743 N  N   . ILE   B 1 290 ? 8.382   3.927   -41.791 1.00 18.80 ? 302 ILE   B N   1 
ATOM   4744 C  CA  . ILE   B 1 290 ? 7.622   2.694   -41.678 1.00 17.72 ? 302 ILE   B CA  1 
ATOM   4745 C  C   . ILE   B 1 290 ? 7.052   2.302   -43.039 1.00 19.44 ? 302 ILE   B C   1 
ATOM   4746 O  O   . ILE   B 1 290 ? 7.123   1.139   -43.446 1.00 22.37 ? 302 ILE   B O   1 
ATOM   4747 C  CB  . ILE   B 1 290 ? 6.518   2.849   -40.615 1.00 17.11 ? 302 ILE   B CB  1 
ATOM   4748 C  CG1 . ILE   B 1 290 ? 7.119   2.924   -39.201 1.00 19.79 ? 302 ILE   B CG1 1 
ATOM   4749 C  CG2 . ILE   B 1 290 ? 5.488   1.713   -40.747 1.00 17.34 ? 302 ILE   B CG2 1 
ATOM   4750 C  CD1 . ILE   B 1 290 ? 6.183   3.481   -38.143 1.00 23.11 ? 302 ILE   B CD1 1 
ATOM   4751 N  N   . SER   B 1 291 ? 6.516   3.274   -43.776 1.00 21.97 ? 303 SER   B N   1 
ATOM   4752 C  CA  . SER   B 1 291 ? 5.852   2.955   -45.037 1.00 20.70 ? 303 SER   B CA  1 
ATOM   4753 C  C   . SER   B 1 291 ? 6.848   2.558   -46.115 1.00 21.21 ? 303 SER   B C   1 
ATOM   4754 O  O   . SER   B 1 291 ? 6.496   1.802   -47.031 1.00 22.55 ? 303 SER   B O   1 
ATOM   4755 C  CB  . SER   B 1 291 ? 5.013   4.140   -45.510 1.00 20.47 ? 303 SER   B CB  1 
ATOM   4756 O  OG  . SER   B 1 291 ? 5.852   5.235   -45.826 1.00 22.47 ? 303 SER   B OG  1 
ATOM   4757 N  N   . LYS   B 1 292 ? 8.077   3.073   -46.051 1.00 17.07 ? 304 LYS   B N   1 
ATOM   4758 C  CA  . LYS   B 1 292 ? 9.094   2.700   -47.023 1.00 23.84 ? 304 LYS   B CA  1 
ATOM   4759 C  C   . LYS   B 1 292 ? 9.982   1.558   -46.547 1.00 22.83 ? 304 LYS   B C   1 
ATOM   4760 O  O   . LYS   B 1 292 ? 10.743  1.012   -47.355 1.00 24.18 ? 304 LYS   B O   1 
ATOM   4761 C  CB  . LYS   B 1 292 ? 9.965   3.910   -47.389 1.00 22.93 ? 304 LYS   B CB  1 
ATOM   4762 C  CG  . LYS   B 1 292 ? 9.198   5.075   -47.994 1.00 28.12 ? 304 LYS   B CG  1 
ATOM   4763 C  CD  . LYS   B 1 292 ? 10.128  6.015   -48.732 1.00 29.09 ? 304 LYS   B CD  1 
ATOM   4764 C  CE  . LYS   B 1 292 ? 9.536   7.410   -48.857 1.00 31.86 ? 304 LYS   B CE  1 
ATOM   4765 N  NZ  . LYS   B 1 292 ? 9.463   8.077   -47.521 1.00 33.78 ? 304 LYS   B NZ  1 
ATOM   4766 N  N   . ASN   B 1 293 ? 9.891   1.172   -45.273 1.00 21.15 ? 305 ASN   B N   1 
ATOM   4767 C  CA  . ASN   B 1 293 ? 10.752  0.129   -44.715 1.00 21.24 ? 305 ASN   B CA  1 
ATOM   4768 C  C   . ASN   B 1 293 ? 12.223  0.477   -44.982 1.00 23.37 ? 305 ASN   B C   1 
ATOM   4769 O  O   . ASN   B 1 293 ? 13.009  -0.333  -45.481 1.00 21.94 ? 305 ASN   B O   1 
ATOM   4770 C  CB  . ASN   B 1 293 ? 10.368  -1.245  -45.277 1.00 22.32 ? 305 ASN   B CB  1 
ATOM   4771 C  CG  . ASN   B 1 293 ? 11.111  -2.395  -44.616 1.00 28.11 ? 305 ASN   B CG  1 
ATOM   4772 O  OD1 . ASN   B 1 293 ? 11.557  -2.298  -43.466 1.00 22.92 ? 305 ASN   B OD1 1 
ATOM   4773 N  ND2 . ASN   B 1 293 ? 11.257  -3.496  -45.356 1.00 25.82 ? 305 ASN   B ND2 1 
ATOM   4774 N  N   . GLU   B 1 294 ? 12.578  1.720   -44.657 1.00 19.74 ? 306 GLU   B N   1 
ATOM   4775 C  CA  . GLU   B 1 294 ? 13.870  2.299   -44.993 1.00 18.99 ? 306 GLU   B CA  1 
ATOM   4776 C  C   . GLU   B 1 294 ? 14.357  3.190   -43.859 1.00 19.29 ? 306 GLU   B C   1 
ATOM   4777 O  O   . GLU   B 1 294 ? 13.593  3.992   -43.315 1.00 20.14 ? 306 GLU   B O   1 
ATOM   4778 C  CB  . GLU   B 1 294 ? 13.782  3.114   -46.295 1.00 20.48 ? 306 GLU   B CB  1 
ATOM   4779 C  CG  . GLU   B 1 294 ? 14.827  4.217   -46.457 1.00 27.22 ? 306 GLU   B CG  1 
ATOM   4780 C  CD  . GLU   B 1 294 ? 14.800  4.847   -47.857 1.00 29.02 ? 306 GLU   B CD  1 
ATOM   4781 O  OE1 . GLU   B 1 294 ? 14.987  4.096   -48.834 1.00 34.07 ? 306 GLU   B OE1 1 
ATOM   4782 O  OE2 . GLU   B 1 294 ? 14.588  6.083   -47.970 1.00 29.18 ? 306 GLU   B OE2 1 
ATOM   4783 N  N   . TRP   B 1 295 ? 15.640  3.060   -43.530 1.00 21.25 ? 307 TRP   B N   1 
ATOM   4784 C  CA  . TRP   B 1 295 ? 16.322  3.955   -42.599 1.00 18.30 ? 307 TRP   B CA  1 
ATOM   4785 C  C   . TRP   B 1 295 ? 16.930  5.141   -43.334 1.00 19.31 ? 307 TRP   B C   1 
ATOM   4786 O  O   . TRP   B 1 295 ? 17.523  4.979   -44.399 1.00 21.14 ? 307 TRP   B O   1 
ATOM   4787 C  CB  . TRP   B 1 295 ? 17.440  3.220   -41.877 1.00 18.78 ? 307 TRP   B CB  1 
ATOM   4788 C  CG  . TRP   B 1 295 ? 16.979  2.211   -40.947 1.00 17.78 ? 307 TRP   B CG  1 
ATOM   4789 C  CD1 . TRP   B 1 295 ? 16.827  0.881   -41.182 1.00 16.92 ? 307 TRP   B CD1 1 
ATOM   4790 C  CD2 . TRP   B 1 295 ? 16.631  2.433   -39.583 1.00 15.90 ? 307 TRP   B CD2 1 
ATOM   4791 N  NE1 . TRP   B 1 295 ? 16.401  0.254   -40.034 1.00 19.24 ? 307 TRP   B NE1 1 
ATOM   4792 C  CE2 . TRP   B 1 295 ? 16.271  1.188   -39.039 1.00 18.09 ? 307 TRP   B CE2 1 
ATOM   4793 C  CE3 . TRP   B 1 295 ? 16.609  3.569   -38.761 1.00 18.06 ? 307 TRP   B CE3 1 
ATOM   4794 C  CZ2 . TRP   B 1 295 ? 15.902  1.038   -37.702 1.00 18.13 ? 307 TRP   B CZ2 1 
ATOM   4795 C  CZ3 . TRP   B 1 295 ? 16.227  3.418   -37.428 1.00 12.54 ? 307 TRP   B CZ3 1 
ATOM   4796 C  CH2 . TRP   B 1 295 ? 15.865  2.167   -36.925 1.00 14.39 ? 307 TRP   B CH2 1 
ATOM   4797 N  N   . ILE   B 1 296 ? 16.812  6.324   -42.737 1.00 18.63 ? 308 ILE   B N   1 
ATOM   4798 C  CA  . ILE   B 1 296 ? 17.306  7.567   -43.319 1.00 20.31 ? 308 ILE   B CA  1 
ATOM   4799 C  C   . ILE   B 1 296 ? 18.173  8.259   -42.274 1.00 20.12 ? 308 ILE   B C   1 
ATOM   4800 O  O   . ILE   B 1 296 ? 17.685  8.605   -41.191 1.00 19.98 ? 308 ILE   B O   1 
ATOM   4801 C  CB  . ILE   B 1 296 ? 16.148  8.479   -43.766 1.00 19.08 ? 308 ILE   B CB  1 
ATOM   4802 C  CG1 . ILE   B 1 296 ? 15.378  7.826   -44.920 1.00 23.38 ? 308 ILE   B CG1 1 
ATOM   4803 C  CG2 . ILE   B 1 296 ? 16.657  9.873   -44.098 1.00 21.33 ? 308 ILE   B CG2 1 
ATOM   4804 C  CD1 . ILE   B 1 296 ? 14.436  8.761   -45.651 1.00 33.57 ? 308 ILE   B CD1 1 
ATOM   4805 N  N   . GLN   B 1 297 ? 19.450  8.462   -42.586 1.00 20.18 ? 309 GLN   B N   1 
ATOM   4806 C  CA  . GLN   B 1 297 ? 20.341  9.074   -41.608 1.00 19.12 ? 309 GLN   B CA  1 
ATOM   4807 C  C   . GLN   B 1 297 ? 20.010  10.552  -41.442 1.00 21.97 ? 309 GLN   B C   1 
ATOM   4808 O  O   . GLN   B 1 297 ? 19.751  11.268  -42.420 1.00 26.54 ? 309 GLN   B O   1 
ATOM   4809 C  CB  . GLN   B 1 297 ? 21.810  8.886   -42.020 1.00 18.80 ? 309 GLN   B CB  1 
ATOM   4810 C  CG  . GLN   B 1 297 ? 22.796  9.452   -40.999 1.00 21.36 ? 309 GLN   B CG  1 
ATOM   4811 C  CD  . GLN   B 1 297 ? 24.112  8.678   -40.910 1.00 22.79 ? 309 GLN   B CD  1 
ATOM   4812 O  OE1 . GLN   B 1 297 ? 24.418  7.837   -41.753 1.00 26.55 ? 309 GLN   B OE1 1 
ATOM   4813 N  NE2 . GLN   B 1 297 ? 24.889  8.956   -39.864 1.00 27.36 ? 309 GLN   B NE2 1 
ATOM   4814 N  N   . PHE   B 1 298 ? 20.028  11.012  -40.195 1.00 23.81 ? 310 PHE   B N   1 
ATOM   4815 C  CA  . PHE   B 1 298 ? 19.559  12.344  -39.834 1.00 24.88 ? 310 PHE   B CA  1 
ATOM   4816 C  C   . PHE   B 1 298 ? 20.758  13.194  -39.449 1.00 27.34 ? 310 PHE   B C   1 
ATOM   4817 O  O   . PHE   B 1 298 ? 21.505  12.838  -38.533 1.00 24.95 ? 310 PHE   B O   1 
ATOM   4818 C  CB  . PHE   B 1 298 ? 18.541  12.274  -38.689 1.00 26.27 ? 310 PHE   B CB  1 
ATOM   4819 C  CG  . PHE   B 1 298 ? 17.934  13.605  -38.323 1.00 26.64 ? 310 PHE   B CG  1 
ATOM   4820 C  CD1 . PHE   B 1 298 ? 16.863  14.117  -39.042 1.00 30.86 ? 310 PHE   B CD1 1 
ATOM   4821 C  CD2 . PHE   B 1 298 ? 18.421  14.334  -37.251 1.00 22.42 ? 310 PHE   B CD2 1 
ATOM   4822 C  CE1 . PHE   B 1 298 ? 16.297  15.339  -38.707 1.00 30.62 ? 310 PHE   B CE1 1 
ATOM   4823 C  CE2 . PHE   B 1 298 ? 17.865  15.553  -36.908 1.00 21.96 ? 310 PHE   B CE2 1 
ATOM   4824 C  CZ  . PHE   B 1 298 ? 16.799  16.055  -37.633 1.00 31.11 ? 310 PHE   B CZ  1 
ATOM   4825 N  N   . ASN   B 1 299 ? 20.943  14.307  -40.151 1.00 29.31 ? 311 ASN   B N   1 
ATOM   4826 C  CA  . ASN   B 1 299 ? 22.077  15.186  -39.907 1.00 28.21 ? 311 ASN   B CA  1 
ATOM   4827 C  C   . ASN   B 1 299 ? 21.699  16.200  -38.842 1.00 28.44 ? 311 ASN   B C   1 
ATOM   4828 O  O   . ASN   B 1 299 ? 20.606  16.769  -38.874 1.00 31.95 ? 311 ASN   B O   1 
ATOM   4829 C  CB  . ASN   B 1 299 ? 22.515  15.878  -41.195 1.00 31.94 ? 311 ASN   B CB  1 
ATOM   4830 C  CG  . ASN   B 1 299 ? 22.850  14.886  -42.292 1.00 39.70 ? 311 ASN   B CG  1 
ATOM   4831 O  OD1 . ASN   B 1 299 ? 23.979  14.393  -42.376 1.00 46.60 ? 311 ASN   B OD1 1 
ATOM   4832 N  ND2 . ASN   B 1 299 ? 21.860  14.568  -43.129 1.00 39.09 ? 311 ASN   B ND2 1 
ATOM   4833 N  N   . HIS   B 1 300 ? 22.588  16.387  -37.877 1.00 30.71 ? 312 HIS   B N   1 
ATOM   4834 C  CA  . HIS   B 1 300 ? 22.284  17.161  -36.686 1.00 26.12 ? 312 HIS   B CA  1 
ATOM   4835 C  C   . HIS   B 1 300 ? 23.581  17.761  -36.177 1.00 26.75 ? 312 HIS   B C   1 
ATOM   4836 O  O   . HIS   B 1 300 ? 24.669  17.311  -36.559 1.00 25.19 ? 312 HIS   B O   1 
ATOM   4837 C  CB  . HIS   B 1 300 ? 21.623  16.289  -35.607 1.00 25.60 ? 312 HIS   B CB  1 
ATOM   4838 C  CG  . HIS   B 1 300 ? 22.468  15.141  -35.167 1.00 25.71 ? 312 HIS   B CG  1 
ATOM   4839 N  ND1 . HIS   B 1 300 ? 23.332  15.224  -34.098 1.00 26.40 ? 312 HIS   B ND1 1 
ATOM   4840 C  CD2 . HIS   B 1 300 ? 22.594  13.886  -35.658 1.00 25.42 ? 312 HIS   B CD2 1 
ATOM   4841 C  CE1 . HIS   B 1 300 ? 23.947  14.067  -33.942 1.00 20.83 ? 312 HIS   B CE1 1 
ATOM   4842 N  NE2 . HIS   B 1 300 ? 23.519  13.237  -34.877 1.00 22.46 ? 312 HIS   B NE2 1 
ATOM   4843 N  N   . PRO   B 1 301 ? 23.507  18.786  -35.331 1.00 25.92 ? 313 PRO   B N   1 
ATOM   4844 C  CA  . PRO   B 1 301 ? 24.729  19.430  -34.833 1.00 28.86 ? 313 PRO   B CA  1 
ATOM   4845 C  C   . PRO   B 1 301 ? 25.287  18.842  -33.546 1.00 26.19 ? 313 PRO   B C   1 
ATOM   4846 O  O   . PRO   B 1 301 ? 26.195  19.444  -32.966 1.00 27.68 ? 313 PRO   B O   1 
ATOM   4847 C  CB  . PRO   B 1 301 ? 24.264  20.876  -34.609 1.00 26.83 ? 313 PRO   B CB  1 
ATOM   4848 C  CG  . PRO   B 1 301 ? 22.829  20.742  -34.239 1.00 28.55 ? 313 PRO   B CG  1 
ATOM   4849 C  CD  . PRO   B 1 301 ? 22.291  19.514  -34.914 1.00 28.72 ? 313 PRO   B CD  1 
ATOM   4850 N  N   . TYR   B 1 302 ? 24.793  17.689  -33.093 1.00 22.78 ? 314 TYR   B N   1 
ATOM   4851 C  CA  . TYR   B 1 302 ? 25.272  17.067  -31.864 1.00 27.96 ? 314 TYR   B CA  1 
ATOM   4852 C  C   . TYR   B 1 302 ? 26.183  15.870  -32.129 1.00 24.43 ? 314 TYR   B C   1 
ATOM   4853 O  O   . TYR   B 1 302 ? 26.195  14.917  -31.339 1.00 23.13 ? 314 TYR   B O   1 
ATOM   4854 C  CB  . TYR   B 1 302 ? 24.099  16.637  -30.986 1.00 26.74 ? 314 TYR   B CB  1 
ATOM   4855 C  CG  . TYR   B 1 302 ? 23.078  17.710  -30.705 1.00 28.12 ? 314 TYR   B CG  1 
ATOM   4856 C  CD1 . TYR   B 1 302 ? 23.297  18.679  -29.731 1.00 29.56 ? 314 TYR   B CD1 1 
ATOM   4857 C  CD2 . TYR   B 1 302 ? 21.869  17.730  -31.392 1.00 28.32 ? 314 TYR   B CD2 1 
ATOM   4858 C  CE1 . TYR   B 1 302 ? 22.338  19.657  -29.460 1.00 32.06 ? 314 TYR   B CE1 1 
ATOM   4859 C  CE2 . TYR   B 1 302 ? 20.913  18.693  -31.135 1.00 28.18 ? 314 TYR   B CE2 1 
ATOM   4860 C  CZ  . TYR   B 1 302 ? 21.147  19.656  -30.173 1.00 30.23 ? 314 TYR   B CZ  1 
ATOM   4861 O  OH  . TYR   B 1 302 ? 20.176  20.605  -29.930 1.00 28.57 ? 314 TYR   B OH  1 
ATOM   4862 N  N   . THR   B 1 303 ? 26.960  15.908  -33.214 1.00 22.85 ? 315 THR   B N   1 
ATOM   4863 C  CA  . THR   B 1 303 ? 27.851  14.795  -33.536 1.00 24.34 ? 315 THR   B CA  1 
ATOM   4864 C  C   . THR   B 1 303 ? 28.903  14.560  -32.457 1.00 25.86 ? 315 THR   B C   1 
ATOM   4865 O  O   . THR   B 1 303 ? 29.371  13.429  -32.285 1.00 22.31 ? 315 THR   B O   1 
ATOM   4866 C  CB  . THR   B 1 303 ? 28.543  15.052  -34.871 1.00 27.38 ? 315 THR   B CB  1 
ATOM   4867 O  OG1 . THR   B 1 303 ? 29.590  16.014  -34.677 1.00 31.94 ? 315 THR   B OG1 1 
ATOM   4868 C  CG2 . THR   B 1 303 ? 27.553  15.591  -35.869 1.00 29.08 ? 315 THR   B CG2 1 
ATOM   4869 N  N   . GLU   B 1 304 ? 29.311  15.607  -31.744 1.00 23.81 ? 316 GLU   B N   1 
ATOM   4870 C  CA  . GLU   B 1 304 ? 30.322  15.489  -30.701 1.00 26.35 ? 316 GLU   B CA  1 
ATOM   4871 C  C   . GLU   B 1 304 ? 29.708  15.244  -29.332 1.00 26.96 ? 316 GLU   B C   1 
ATOM   4872 O  O   . GLU   B 1 304 ? 30.389  15.398  -28.309 1.00 25.68 ? 316 GLU   B O   1 
ATOM   4873 C  CB  . GLU   B 1 304 ? 31.213  16.736  -30.672 1.00 31.51 ? 316 GLU   B CB  1 
ATOM   4874 C  CG  . GLU   B 1 304 ? 32.115  16.872  -31.885 1.00 34.28 ? 316 GLU   B CG  1 
ATOM   4875 C  CD  . GLU   B 1 304 ? 33.260  17.850  -31.663 1.00 41.40 ? 316 GLU   B CD  1 
ATOM   4876 O  OE1 . GLU   B 1 304 ? 33.126  18.755  -30.809 1.00 44.43 ? 316 GLU   B OE1 1 
ATOM   4877 O  OE2 . GLU   B 1 304 ? 34.301  17.707  -32.340 1.00 49.60 ? 316 GLU   B OE2 1 
ATOM   4878 N  N   . LYS   B 1 305 ? 28.438  14.851  -29.294 1.00 25.44 ? 317 LYS   B N   1 
ATOM   4879 C  CA  . LYS   B 1 305 ? 27.731  14.576  -28.046 1.00 21.04 ? 317 LYS   B CA  1 
ATOM   4880 C  C   . LYS   B 1 305 ? 27.091  13.192  -28.121 1.00 20.15 ? 317 LYS   B C   1 
ATOM   4881 O  O   . LYS   B 1 305 ? 25.861  13.055  -28.104 1.00 22.45 ? 317 LYS   B O   1 
ATOM   4882 C  CB  . LYS   B 1 305 ? 26.687  15.658  -27.771 1.00 24.67 ? 317 LYS   B CB  1 
ATOM   4883 C  CG  . LYS   B 1 305 ? 27.255  17.063  -27.769 1.00 25.93 ? 317 LYS   B CG  1 
ATOM   4884 C  CD  . LYS   B 1 305 ? 26.403  18.030  -26.953 1.00 32.85 ? 317 LYS   B CD  1 
ATOM   4885 C  CE  . LYS   B 1 305 ? 27.123  19.360  -26.761 1.00 32.93 ? 317 LYS   B CE  1 
ATOM   4886 N  NZ  . LYS   B 1 305 ? 26.190  20.484  -26.442 1.00 38.45 ? 317 LYS   B NZ  1 
ATOM   4887 N  N   . PRO   B 1 306 ? 27.901  12.134  -28.188 1.00 18.69 ? 318 PRO   B N   1 
ATOM   4888 C  CA  . PRO   B 1 306 ? 27.332  10.790  -28.056 1.00 17.35 ? 318 PRO   B CA  1 
ATOM   4889 C  C   . PRO   B 1 306 ? 26.664  10.637  -26.697 1.00 16.33 ? 318 PRO   B C   1 
ATOM   4890 O  O   . PRO   B 1 306 ? 27.030  11.306  -25.724 1.00 16.33 ? 318 PRO   B O   1 
ATOM   4891 C  CB  . PRO   B 1 306 ? 28.543  9.866   -28.206 1.00 19.54 ? 318 PRO   B CB  1 
ATOM   4892 C  CG  . PRO   B 1 306 ? 29.731  10.725  -27.882 1.00 18.15 ? 318 PRO   B CG  1 
ATOM   4893 C  CD  . PRO   B 1 306 ? 29.377  12.109  -28.295 1.00 17.19 ? 318 PRO   B CD  1 
ATOM   4894 N  N   . ARG   B 1 307 ? 25.616  9.801   -26.658 1.00 14.92 ? 319 ARG   B N   1 
ATOM   4895 C  CA  . ARG   B 1 307 ? 24.896  9.510   -25.423 1.00 16.52 ? 319 ARG   B CA  1 
ATOM   4896 C  C   . ARG   B 1 307 ? 24.477  8.050   -25.404 1.00 15.05 ? 319 ARG   B C   1 
ATOM   4897 O  O   . ARG   B 1 307 ? 24.033  7.510   -26.422 1.00 14.57 ? 319 ARG   B O   1 
ATOM   4898 C  CB  . ARG   B 1 307 ? 23.637  10.370  -25.254 1.00 14.09 ? 319 ARG   B CB  1 
ATOM   4899 C  CG  . ARG   B 1 307 ? 23.871  11.857  -25.180 1.00 15.91 ? 319 ARG   B CG  1 
ATOM   4900 C  CD  . ARG   B 1 307 ? 24.549  12.190  -23.860 1.00 18.21 ? 319 ARG   B CD  1 
ATOM   4901 N  NE  . ARG   B 1 307 ? 24.748  13.620  -23.657 1.00 19.98 ? 319 ARG   B NE  1 
ATOM   4902 C  CZ  . ARG   B 1 307 ? 25.883  14.253  -23.920 1.00 21.60 ? 319 ARG   B CZ  1 
ATOM   4903 N  NH1 . ARG   B 1 307 ? 26.911  13.628  -24.471 1.00 19.68 ? 319 ARG   B NH1 1 
ATOM   4904 N  NH2 . ARG   B 1 307 ? 26.004  15.537  -23.588 1.00 28.42 ? 319 ARG   B NH2 1 
ATOM   4905 N  N   . LEU   B 1 308 ? 24.577  7.433   -24.230 1.00 14.31 ? 320 LEU   B N   1 
ATOM   4906 C  CA  . LEU   B 1 308 ? 24.032  6.104   -23.983 1.00 12.65 ? 320 LEU   B CA  1 
ATOM   4907 C  C   . LEU   B 1 308 ? 23.290  6.111   -22.655 1.00 16.80 ? 320 LEU   B C   1 
ATOM   4908 O  O   . LEU   B 1 308 ? 23.728  6.760   -21.699 1.00 16.60 ? 320 LEU   B O   1 
ATOM   4909 C  CB  . LEU   B 1 308 ? 25.138  5.004   -23.970 1.00 14.47 ? 320 LEU   B CB  1 
ATOM   4910 C  CG  . LEU   B 1 308 ? 26.498  5.269   -23.326 1.00 17.30 ? 320 LEU   B CG  1 
ATOM   4911 C  CD1 . LEU   B 1 308 ? 27.170  3.982   -22.940 1.00 17.00 ? 320 LEU   B CD1 1 
ATOM   4912 C  CD2 . LEU   B 1 308 ? 27.389  6.007   -24.295 1.00 16.86 ? 320 LEU   B CD2 1 
ATOM   4913 N  N   . TRP   B 1 309 ? 22.169  5.376   -22.605 1.00 12.80 ? 321 TRP   B N   1 
ATOM   4914 C  CA  . TRP   B 1 309 ? 21.287  5.321   -21.436 1.00 13.57 ? 321 TRP   B CA  1 
ATOM   4915 C  C   . TRP   B 1 309 ? 20.681  6.690   -21.129 1.00 16.67 ? 321 TRP   B C   1 
ATOM   4916 O  O   . TRP   B 1 309 ? 20.303  6.986   -19.986 1.00 16.30 ? 321 TRP   B O   1 
ATOM   4917 C  CB  . TRP   B 1 309 ? 22.002  4.764   -20.196 1.00 15.02 ? 321 TRP   B CB  1 
ATOM   4918 C  CG  . TRP   B 1 309 ? 21.176  3.789   -19.406 1.00 15.17 ? 321 TRP   B CG  1 
ATOM   4919 C  CD1 . TRP   B 1 309 ? 19.873  3.426   -19.641 1.00 12.21 ? 321 TRP   B CD1 1 
ATOM   4920 C  CD2 . TRP   B 1 309 ? 21.590  3.063   -18.235 1.00 14.84 ? 321 TRP   B CD2 1 
ATOM   4921 N  NE1 . TRP   B 1 309 ? 19.459  2.510   -18.690 1.00 13.68 ? 321 TRP   B NE1 1 
ATOM   4922 C  CE2 . TRP   B 1 309 ? 20.493  2.274   -17.817 1.00 11.96 ? 321 TRP   B CE2 1 
ATOM   4923 C  CE3 . TRP   B 1 309 ? 22.784  3.003   -17.503 1.00 13.02 ? 321 TRP   B CE3 1 
ATOM   4924 C  CZ2 . TRP   B 1 309 ? 20.555  1.428   -16.703 1.00 13.94 ? 321 TRP   B CZ2 1 
ATOM   4925 C  CZ3 . TRP   B 1 309 ? 22.852  2.147   -16.393 1.00 14.83 ? 321 TRP   B CZ3 1 
ATOM   4926 C  CH2 . TRP   B 1 309 ? 21.745  1.383   -15.999 1.00 14.39 ? 321 TRP   B CH2 1 
ATOM   4927 N  N   . HIS   B 1 310 ? 20.570  7.521   -22.155 1.00 15.00 ? 322 HIS   B N   1 
ATOM   4928 C  CA  . HIS   B 1 310 ? 19.813  8.757   -22.107 1.00 15.38 ? 322 HIS   B CA  1 
ATOM   4929 C  C   . HIS   B 1 310 ? 18.333  8.439   -22.291 1.00 15.65 ? 322 HIS   B C   1 
ATOM   4930 O  O   . HIS   B 1 310 ? 17.938  7.282   -22.455 1.00 16.65 ? 322 HIS   B O   1 
ATOM   4931 C  CB  . HIS   B 1 310 ? 20.296  9.695   -23.201 1.00 17.58 ? 322 HIS   B CB  1 
ATOM   4932 C  CG  . HIS   B 1 310 ? 20.194  9.084   -24.563 1.00 15.08 ? 322 HIS   B CG  1 
ATOM   4933 N  ND1 . HIS   B 1 310 ? 20.977  8.019   -24.950 1.00 15.00 ? 322 HIS   B ND1 1 
ATOM   4934 C  CD2 . HIS   B 1 310 ? 19.362  9.338   -25.601 1.00 16.61 ? 322 HIS   B CD2 1 
ATOM   4935 C  CE1 . HIS   B 1 310 ? 20.664  7.671   -26.187 1.00 17.11 ? 322 HIS   B CE1 1 
ATOM   4936 N  NE2 . HIS   B 1 310 ? 19.678  8.448   -26.600 1.00 17.52 ? 322 HIS   B NE2 1 
ATOM   4937 N  N   . THR   B 1 311 ? 17.508  9.476   -22.291 1.00 15.58 ? 323 THR   B N   1 
ATOM   4938 C  CA  . THR   B 1 311 ? 16.085  9.352   -22.568 1.00 17.43 ? 323 THR   B CA  1 
ATOM   4939 C  C   . THR   B 1 311 ? 15.711  10.328  -23.667 1.00 17.36 ? 323 THR   B C   1 
ATOM   4940 O  O   . THR   B 1 311 ? 16.387  11.345  -23.878 1.00 17.00 ? 323 THR   B O   1 
ATOM   4941 C  CB  . THR   B 1 311 ? 15.220  9.620   -21.321 1.00 15.66 ? 323 THR   B CB  1 
ATOM   4942 O  OG1 . THR   B 1 311 ? 15.485  10.939  -20.819 1.00 14.37 ? 323 THR   B OG1 1 
ATOM   4943 C  CG2 . THR   B 1 311 ? 15.496  8.591   -20.257 1.00 16.60 ? 323 THR   B CG2 1 
ATOM   4944 N  N   . ALA   B 1 312 ? 14.636  9.992   -24.385 1.00 18.57 ? 324 ALA   B N   1 
ATOM   4945 C  CA  . ALA   B 1 312 ? 14.119  10.820  -25.465 1.00 18.20 ? 324 ALA   B CA  1 
ATOM   4946 C  C   . ALA   B 1 312 ? 12.608  10.919  -25.356 1.00 15.66 ? 324 ALA   B C   1 
ATOM   4947 O  O   . ALA   B 1 312 ? 11.940  9.903   -25.157 1.00 16.59 ? 324 ALA   B O   1 
ATOM   4948 C  CB  . ALA   B 1 312 ? 14.501  10.244  -26.827 1.00 14.17 ? 324 ALA   B CB  1 
ATOM   4949 N  N   . CYS   B 1 313 ? 12.071  12.128  -25.512 1.00 15.55 ? 325 CYS   B N   1 
ATOM   4950 C  CA  . CYS   B 1 313 ? 10.630  12.341  -25.568 1.00 19.55 ? 325 CYS   B CA  1 
ATOM   4951 C  C   . CYS   B 1 313 ? 10.289  13.234  -26.749 1.00 21.50 ? 325 CYS   B C   1 
ATOM   4952 O  O   . CYS   B 1 313 ? 10.949  14.252  -26.980 1.00 20.87 ? 325 CYS   B O   1 
ATOM   4953 C  CB  . CYS   B 1 313 ? 10.094  12.988  -24.289 1.00 18.67 ? 325 CYS   B CB  1 
ATOM   4954 S  SG  . CYS   B 1 313 ? 10.331  11.974  -22.817 1.00 21.74 ? 325 CYS   B SG  1 
ATOM   4955 N  N   . ALA   B 1 314 ? 9.243   12.861  -27.479 1.00 21.51 ? 326 ALA   B N   1 
ATOM   4956 C  CA  . ALA   B 1 314 ? 8.730   13.707  -28.548 1.00 25.41 ? 326 ALA   B CA  1 
ATOM   4957 C  C   . ALA   B 1 314 ? 7.807   14.783  -27.990 1.00 25.81 ? 326 ALA   B C   1 
ATOM   4958 O  O   . ALA   B 1 314 ? 6.984   14.517  -27.109 1.00 23.67 ? 326 ALA   B O   1 
ATOM   4959 C  CB  . ALA   B 1 314 ? 7.981   12.869  -29.578 1.00 22.73 ? 326 ALA   B CB  1 
ATOM   4960 N  N   . SER   B 1 315 ? 7.943   16.000  -28.514 1.00 27.81 ? 327 SER   B N   1 
ATOM   4961 C  CA  . SER   B 1 315 ? 7.083   17.119  -28.152 1.00 29.74 ? 327 SER   B CA  1 
ATOM   4962 C  C   . SER   B 1 315 ? 5.978   17.289  -29.190 1.00 33.34 ? 327 SER   B C   1 
ATOM   4963 O  O   . SER   B 1 315 ? 6.042   16.743  -30.292 1.00 31.77 ? 327 SER   B O   1 
ATOM   4964 C  CB  . SER   B 1 315 ? 7.884   18.418  -28.033 1.00 31.87 ? 327 SER   B CB  1 
ATOM   4965 O  OG  . SER   B 1 315 ? 8.033   19.040  -29.298 1.00 33.98 ? 327 SER   B OG  1 
ATOM   4966 N  N   . ASP   B 1 316 ? 4.952   18.060  -28.815 1.00 31.81 ? 328 ASP   B N   1 
ATOM   4967 C  CA  . ASP   B 1 316 ? 3.818   18.331  -29.696 1.00 37.53 ? 328 ASP   B CA  1 
ATOM   4968 C  C   . ASP   B 1 316 ? 4.156   19.292  -30.826 1.00 38.47 ? 328 ASP   B C   1 
ATOM   4969 O  O   . ASP   B 1 316 ? 3.329   19.474  -31.728 1.00 41.87 ? 328 ASP   B O   1 
ATOM   4970 C  CB  . ASP   B 1 316 ? 2.637   18.900  -28.897 1.00 38.41 ? 328 ASP   B CB  1 
ATOM   4971 C  CG  . ASP   B 1 316 ? 1.825   17.826  -28.182 1.00 37.94 ? 328 ASP   B CG  1 
ATOM   4972 O  OD1 . ASP   B 1 316 ? 1.648   16.720  -28.741 1.00 39.73 ? 328 ASP   B OD1 1 
ATOM   4973 O  OD2 . ASP   B 1 316 ? 1.348   18.095  -27.058 1.00 39.76 ? 328 ASP   B OD2 1 
ATOM   4974 N  N   . GLU   B 1 317 ? 5.328   19.919  -30.802 1.00 39.89 ? 329 GLU   B N   1 
ATOM   4975 C  CA  . GLU   B 1 317 ? 5.726   20.879  -31.825 1.00 46.86 ? 329 GLU   B CA  1 
ATOM   4976 C  C   . GLU   B 1 317 ? 6.935   20.382  -32.618 1.00 47.75 ? 329 GLU   B C   1 
ATOM   4977 O  O   . GLU   B 1 317 ? 7.855   21.143  -32.925 1.00 47.76 ? 329 GLU   B O   1 
ATOM   4978 C  CB  . GLU   B 1 317 ? 6.005   22.248  -31.207 1.00 46.67 ? 329 GLU   B CB  1 
ATOM   4979 C  CG  . GLU   B 1 317 ? 4.762   23.106  -30.983 1.00 53.00 ? 329 GLU   B CG  1 
ATOM   4980 C  CD  . GLU   B 1 317 ? 4.392   23.934  -32.205 1.00 59.88 ? 329 GLU   B CD  1 
ATOM   4981 O  OE1 . GLU   B 1 317 ? 3.200   24.280  -32.359 1.00 60.67 ? 329 GLU   B OE1 1 
ATOM   4982 O  OE2 . GLU   B 1 317 ? 5.298   24.241  -33.012 1.00 61.37 ? 329 GLU   B OE2 1 
ATOM   4983 N  N   . GLY   B 1 318 ? 6.948   19.092  -32.943 1.00 41.72 ? 330 GLY   B N   1 
ATOM   4984 C  CA  . GLY   B 1 318 ? 7.935   18.526  -33.851 1.00 40.73 ? 330 GLY   B CA  1 
ATOM   4985 C  C   . GLY   B 1 318 ? 9.381   18.543  -33.398 1.00 39.40 ? 330 GLY   B C   1 
ATOM   4986 O  O   . GLY   B 1 318 ? 10.268  18.879  -34.193 1.00 38.79 ? 330 GLY   B O   1 
ATOM   4987 N  N   . GLU   B 1 319 ? 9.650   18.185  -32.144 1.00 33.55 ? 331 GLU   B N   1 
ATOM   4988 C  CA  . GLU   B 1 319 ? 11.019  18.071  -31.659 1.00 31.20 ? 331 GLU   B CA  1 
ATOM   4989 C  C   . GLU   B 1 319 ? 11.183  16.763  -30.891 1.00 28.61 ? 331 GLU   B C   1 
ATOM   4990 O  O   . GLU   B 1 319 ? 10.205  16.117  -30.510 1.00 28.12 ? 331 GLU   B O   1 
ATOM   4991 C  CB  . GLU   B 1 319 ? 11.416  19.270  -30.767 1.00 31.39 ? 331 GLU   B CB  1 
ATOM   4992 C  CG  . GLU   B 1 319 ? 11.709  20.582  -31.524 1.00 34.82 ? 331 GLU   B CG  1 
ATOM   4993 C  CD  . GLU   B 1 319 ? 12.001  21.768  -30.597 1.00 34.85 ? 331 GLU   B CD  1 
ATOM   4994 O  OE1 . GLU   B 1 319 ? 11.603  21.727  -29.415 1.00 35.59 ? 331 GLU   B OE1 1 
ATOM   4995 O  OE2 . GLU   B 1 319 ? 12.634  22.745  -31.048 1.00 32.57 ? 331 GLU   B OE2 1 
ATOM   4996 N  N   . VAL   B 1 320 ? 12.439  16.364  -30.694 1.00 27.52 ? 332 VAL   B N   1 
ATOM   4997 C  CA  . VAL   B 1 320 ? 12.803  15.249  -29.824 1.00 23.65 ? 332 VAL   B CA  1 
ATOM   4998 C  C   . VAL   B 1 320 ? 13.716  15.798  -28.737 1.00 22.62 ? 332 VAL   B C   1 
ATOM   4999 O  O   . VAL   B 1 320 ? 14.784  16.352  -29.028 1.00 22.66 ? 332 VAL   B O   1 
ATOM   5000 C  CB  . VAL   B 1 320 ? 13.485  14.101  -30.591 1.00 20.68 ? 332 VAL   B CB  1 
ATOM   5001 C  CG1 . VAL   B 1 320 ? 13.875  12.967  -29.624 1.00 20.54 ? 332 VAL   B CG1 1 
ATOM   5002 C  CG2 . VAL   B 1 320 ? 12.560  13.574  -31.691 1.00 23.73 ? 332 VAL   B CG2 1 
ATOM   5003 N  N   . ILE   B 1 321 ? 13.296  15.647  -27.490 1.00 21.34 ? 333 ILE   B N   1 
ATOM   5004 C  CA  . ILE   B 1 321 ? 14.035  16.169  -26.349 1.00 22.47 ? 333 ILE   B CA  1 
ATOM   5005 C  C   . ILE   B 1 321 ? 14.844  15.014  -25.769 1.00 18.89 ? 333 ILE   B C   1 
ATOM   5006 O  O   . ILE   B 1 321 ? 14.271  14.053  -25.243 1.00 21.04 ? 333 ILE   B O   1 
ATOM   5007 C  CB  . ILE   B 1 321 ? 13.085  16.781  -25.312 1.00 22.82 ? 333 ILE   B CB  1 
ATOM   5008 C  CG1 . ILE   B 1 321 ? 12.200  17.864  -25.959 1.00 26.33 ? 333 ILE   B CG1 1 
ATOM   5009 C  CG2 . ILE   B 1 321 ? 13.842  17.300  -24.102 1.00 22.15 ? 333 ILE   B CG2 1 
ATOM   5010 C  CD1 . ILE   B 1 321 ? 12.947  18.868  -26.785 1.00 26.41 ? 333 ILE   B CD1 1 
ATOM   5011 N  N   . VAL   B 1 322 ? 16.174  15.085  -25.876 1.00 17.36 ? 334 VAL   B N   1 
ATOM   5012 C  CA  . VAL   B 1 322 ? 17.067  14.088  -25.291 1.00 19.57 ? 334 VAL   B CA  1 
ATOM   5013 C  C   . VAL   B 1 322 ? 17.646  14.653  -23.999 1.00 17.60 ? 334 VAL   B C   1 
ATOM   5014 O  O   . VAL   B 1 322 ? 18.091  15.808  -23.965 1.00 19.09 ? 334 VAL   B O   1 
ATOM   5015 C  CB  . VAL   B 1 322 ? 18.189  13.688  -26.267 1.00 19.83 ? 334 VAL   B CB  1 
ATOM   5016 C  CG1 . VAL   B 1 322 ? 19.324  13.012  -25.517 1.00 19.30 ? 334 VAL   B CG1 1 
ATOM   5017 C  CG2 . VAL   B 1 322 ? 17.635  12.775  -27.371 1.00 21.28 ? 334 VAL   B CG2 1 
ATOM   5018 N  N   . PHE   B 1 323 ? 17.615  13.860  -22.935 1.00 15.26 ? 335 PHE   B N   1 
ATOM   5019 C  CA  . PHE   B 1 323 ? 18.157  14.287  -21.647 1.00 22.10 ? 335 PHE   B CA  1 
ATOM   5020 C  C   . PHE   B 1 323 ? 19.016  13.217  -20.994 1.00 19.91 ? 335 PHE   B C   1 
ATOM   5021 O  O   . PHE   B 1 323 ? 18.683  12.026  -21.017 1.00 18.84 ? 335 PHE   B O   1 
ATOM   5022 C  CB  . PHE   B 1 323 ? 17.068  14.661  -20.655 1.00 19.48 ? 335 PHE   B CB  1 
ATOM   5023 C  CG  . PHE   B 1 323 ? 17.616  15.033  -19.315 1.00 17.60 ? 335 PHE   B CG  1 
ATOM   5024 C  CD1 . PHE   B 1 323 ? 18.328  16.206  -19.161 1.00 20.28 ? 335 PHE   B CD1 1 
ATOM   5025 C  CD2 . PHE   B 1 323 ? 17.473  14.185  -18.234 1.00 20.09 ? 335 PHE   B CD2 1 
ATOM   5026 C  CE1 . PHE   B 1 323 ? 18.864  16.549  -17.936 1.00 23.36 ? 335 PHE   B CE1 1 
ATOM   5027 C  CE2 . PHE   B 1 323 ? 18.006  14.524  -16.999 1.00 20.71 ? 335 PHE   B CE2 1 
ATOM   5028 C  CZ  . PHE   B 1 323 ? 18.693  15.711  -16.852 1.00 20.50 ? 335 PHE   B CZ  1 
ATOM   5029 N  N   . GLY   B 1 324 ? 20.106  13.667  -20.366 1.00 20.21 ? 336 GLY   B N   1 
ATOM   5030 C  CA  . GLY   B 1 324 ? 20.909  12.793  -19.545 1.00 19.45 ? 336 GLY   B CA  1 
ATOM   5031 C  C   . GLY   B 1 324 ? 21.693  11.787  -20.367 1.00 21.19 ? 336 GLY   B C   1 
ATOM   5032 O  O   . GLY   B 1 324 ? 21.996  11.994  -21.551 1.00 16.96 ? 336 GLY   B O   1 
ATOM   5033 N  N   . GLY   B 1 325 ? 21.990  10.660  -19.733 1.00 18.17 ? 337 GLY   B N   1 
ATOM   5034 C  CA  . GLY   B 1 325 ? 22.813  9.651   -20.363 1.00 16.29 ? 337 GLY   B CA  1 
ATOM   5035 C  C   . GLY   B 1 325 ? 24.279  9.970   -20.187 1.00 18.92 ? 337 GLY   B C   1 
ATOM   5036 O  O   . GLY   B 1 325 ? 24.667  11.002  -19.644 1.00 20.21 ? 337 GLY   B O   1 
ATOM   5037 N  N   . CYS   B 1 326 ? 25.111  9.068   -20.687 1.00 16.33 ? 338 CYS   B N   1 
ATOM   5038 C  CA  . CYS   B 1 326 ? 26.545  9.126   -20.464 1.00 19.07 ? 338 CYS   B CA  1 
ATOM   5039 C  C   . CYS   B 1 326 ? 27.236  9.349   -21.800 1.00 18.59 ? 338 CYS   B C   1 
ATOM   5040 O  O   . CYS   B 1 326 ? 26.809  8.808   -22.823 1.00 17.96 ? 338 CYS   B O   1 
ATOM   5041 C  CB  . CYS   B 1 326 ? 27.019  7.833   -19.799 1.00 12.38 ? 338 CYS   B CB  1 
ATOM   5042 S  SG  . CYS   B 1 326 ? 28.766  7.841   -19.310 1.00 17.52 ? 338 CYS   B SG  1 
ATOM   5043 N  N   . ALA   B 1 327 ? 28.299  10.154  -21.797 1.00 17.88 ? 339 ALA   B N   1 
ATOM   5044 C  CA  . ALA   B 1 327 ? 29.003  10.469  -23.032 1.00 17.32 ? 339 ALA   B CA  1 
ATOM   5045 C  C   . ALA   B 1 327 ? 30.079  9.460   -23.411 1.00 18.68 ? 339 ALA   B C   1 
ATOM   5046 O  O   . ALA   B 1 327 ? 30.590  9.530   -24.535 1.00 20.27 ? 339 ALA   B O   1 
ATOM   5047 C  CB  . ALA   B 1 327 ? 29.634  11.858  -22.946 1.00 20.03 ? 339 ALA   B CB  1 
ATOM   5048 N  N   . ASN   B 1 328 ? 30.451  8.545   -22.524 1.00 17.31 ? 340 ASN   B N   1 
ATOM   5049 C  CA  . ASN   B 1 328 ? 31.515  7.597   -22.818 1.00 16.07 ? 340 ASN   B CA  1 
ATOM   5050 C  C   . ASN   B 1 328 ? 31.085  6.227   -22.304 1.00 17.58 ? 340 ASN   B C   1 
ATOM   5051 O  O   . ASN   B 1 328 ? 29.896  5.955   -22.096 1.00 17.23 ? 340 ASN   B O   1 
ATOM   5052 C  CB  . ASN   B 1 328 ? 32.867  8.093   -22.262 1.00 17.60 ? 340 ASN   B CB  1 
ATOM   5053 C  CG  . ASN   B 1 328 ? 32.865  8.275   -20.754 1.00 19.46 ? 340 ASN   B CG  1 
ATOM   5054 O  OD1 . ASN   B 1 328 ? 31.890  7.970   -20.085 1.00 17.83 ? 340 ASN   B OD1 1 
ATOM   5055 N  ND2 . ASN   B 1 328 ? 33.983  8.766   -20.209 1.00 19.07 ? 340 ASN   B ND2 1 
ATOM   5056 N  N   . ASN   B 1 329 ? 32.042  5.314   -22.186 1.00 13.67 ? 341 ASN   B N   1 
ATOM   5057 C  CA  . ASN   B 1 329 ? 31.741  3.953   -21.751 1.00 14.32 ? 341 ASN   B CA  1 
ATOM   5058 C  C   . ASN   B 1 329 ? 31.431  3.995   -20.264 1.00 16.29 ? 341 ASN   B C   1 
ATOM   5059 O  O   . ASN   B 1 329 ? 32.333  4.005   -19.423 1.00 19.99 ? 341 ASN   B O   1 
ATOM   5060 C  CB  . ASN   B 1 329 ? 32.901  3.016   -22.058 1.00 16.08 ? 341 ASN   B CB  1 
ATOM   5061 C  CG  . ASN   B 1 329 ? 32.664  1.585   -21.591 1.00 17.86 ? 341 ASN   B CG  1 
ATOM   5062 O  OD1 . ASN   B 1 329 ? 31.591  1.236   -21.073 1.00 21.85 ? 341 ASN   B OD1 1 
ATOM   5063 N  ND2 . ASN   B 1 329 ? 33.668  0.738   -21.803 1.00 15.34 ? 341 ASN   B ND2 1 
ATOM   5064 N  N   . LEU   B 1 330 ? 30.139  4.011   -19.933 1.00 13.50 ? 342 LEU   B N   1 
ATOM   5065 C  CA  . LEU   B 1 330 ? 29.738  4.098   -18.536 1.00 15.09 ? 342 LEU   B CA  1 
ATOM   5066 C  C   . LEU   B 1 330 ? 30.117  2.869   -17.725 1.00 16.08 ? 342 LEU   B C   1 
ATOM   5067 O  O   . LEU   B 1 330 ? 30.001  2.911   -16.497 1.00 14.83 ? 342 LEU   B O   1 
ATOM   5068 C  CB  . LEU   B 1 330 ? 28.228  4.343   -18.440 1.00 13.93 ? 342 LEU   B CB  1 
ATOM   5069 C  CG  . LEU   B 1 330 ? 27.291  3.406   -19.190 1.00 15.61 ? 342 LEU   B CG  1 
ATOM   5070 C  CD1 . LEU   B 1 330 ? 27.016  2.146   -18.409 1.00 18.60 ? 342 LEU   B CD1 1 
ATOM   5071 C  CD2 . LEU   B 1 330 ? 25.983  4.115   -19.506 1.00 20.64 ? 342 LEU   B CD2 1 
ATOM   5072 N  N   . LEU   B 1 331 ? 30.510  1.767   -18.362 1.00 15.86 ? 343 LEU   B N   1 
ATOM   5073 C  CA  . LEU   B 1 331 ? 30.977  0.610   -17.612 1.00 18.37 ? 343 LEU   B CA  1 
ATOM   5074 C  C   . LEU   B 1 331 ? 32.320  0.867   -16.920 1.00 18.43 ? 343 LEU   B C   1 
ATOM   5075 O  O   . LEU   B 1 331 ? 32.687  0.118   -16.014 1.00 19.71 ? 343 LEU   B O   1 
ATOM   5076 C  CB  . LEU   B 1 331 ? 31.081  -0.598  -18.533 1.00 18.23 ? 343 LEU   B CB  1 
ATOM   5077 C  CG  . LEU   B 1 331 ? 29.836  -0.880  -19.377 1.00 18.73 ? 343 LEU   B CG  1 
ATOM   5078 C  CD1 . LEU   B 1 331 ? 30.158  -1.813  -20.540 1.00 21.91 ? 343 LEU   B CD1 1 
ATOM   5079 C  CD2 . LEU   B 1 331 ? 28.761  -1.485  -18.513 1.00 18.67 ? 343 LEU   B CD2 1 
ATOM   5080 N  N   . VAL   B 1 332 ? 33.065  1.883   -17.339 1.00 18.19 ? 344 VAL   B N   1 
ATOM   5081 C  CA  . VAL   B 1 332 ? 34.267  2.321   -16.603 1.00 20.25 ? 344 VAL   B CA  1 
ATOM   5082 C  C   . VAL   B 1 332 ? 33.778  3.383   -15.628 1.00 20.98 ? 344 VAL   B C   1 
ATOM   5083 O  O   . VAL   B 1 332 ? 33.858  4.590   -15.866 1.00 20.59 ? 344 VAL   B O   1 
ATOM   5084 C  CB  . VAL   B 1 332 ? 35.362  2.832   -17.547 1.00 19.35 ? 344 VAL   B CB  1 
ATOM   5085 C  CG1 . VAL   B 1 332 ? 36.706  2.969   -16.814 1.00 21.87 ? 344 VAL   B CG1 1 
ATOM   5086 C  CG2 . VAL   B 1 332 ? 35.481  1.912   -18.729 1.00 21.89 ? 344 VAL   B CG2 1 
ATOM   5087 N  N   . HIS   B 1 333 ? 33.262  2.915   -14.487 1.00 20.93 ? 345 HIS   B N   1 
ATOM   5088 C  CA  . HIS   B 1 333 ? 32.393  3.768   -13.686 1.00 20.42 ? 345 HIS   B CA  1 
ATOM   5089 C  C   . HIS   B 1 333 ? 33.139  4.974   -13.142 1.00 20.97 ? 345 HIS   B C   1 
ATOM   5090 O  O   . HIS   B 1 333 ? 32.558  6.061   -13.055 1.00 24.58 ? 345 HIS   B O   1 
ATOM   5091 C  CB  . HIS   B 1 333 ? 31.747  2.943   -12.557 1.00 21.59 ? 345 HIS   B CB  1 
ATOM   5092 C  CG  . HIS   B 1 333 ? 30.834  3.725   -11.661 1.00 25.51 ? 345 HIS   B CG  1 
ATOM   5093 N  ND1 . HIS   B 1 333 ? 29.572  4.130   -12.044 1.00 22.40 ? 345 HIS   B ND1 1 
ATOM   5094 C  CD2 . HIS   B 1 333 ? 30.990  4.140   -10.378 1.00 25.10 ? 345 HIS   B CD2 1 
ATOM   5095 C  CE1 . HIS   B 1 333 ? 29.001  4.779   -11.040 1.00 25.09 ? 345 HIS   B CE1 1 
ATOM   5096 N  NE2 . HIS   B 1 333 ? 29.840  4.796   -10.018 1.00 25.55 ? 345 HIS   B NE2 1 
ATOM   5097 N  N   . HIS   B 1 334 ? 34.436  4.823   -12.821 1.00 22.13 ? 346 HIS   B N   1 
ATOM   5098 C  CA  . HIS   B 1 334 ? 35.202  5.921   -12.245 1.00 25.19 ? 346 HIS   B CA  1 
ATOM   5099 C  C   . HIS   B 1 334 ? 35.622  6.967   -13.270 1.00 25.16 ? 346 HIS   B C   1 
ATOM   5100 O  O   . HIS   B 1 334 ? 36.128  8.024   -12.875 1.00 26.03 ? 346 HIS   B O   1 
ATOM   5101 C  CB  . HIS   B 1 334 ? 36.441  5.387   -11.504 1.00 24.20 ? 346 HIS   B CB  1 
ATOM   5102 C  CG  . HIS   B 1 334 ? 37.493  4.805   -12.402 1.00 27.36 ? 346 HIS   B CG  1 
ATOM   5103 N  ND1 . HIS   B 1 334 ? 37.289  3.662   -13.147 1.00 27.18 ? 346 HIS   B ND1 1 
ATOM   5104 C  CD2 . HIS   B 1 334 ? 38.761  5.204   -12.665 1.00 25.67 ? 346 HIS   B CD2 1 
ATOM   5105 C  CE1 . HIS   B 1 334 ? 38.387  3.384   -13.829 1.00 28.43 ? 346 HIS   B CE1 1 
ATOM   5106 N  NE2 . HIS   B 1 334 ? 39.297  4.298   -13.547 1.00 25.88 ? 346 HIS   B NE2 1 
ATOM   5107 N  N   . ARG   B 1 335 ? 35.441  6.703   -14.564 1.00 22.11 ? 347 ARG   B N   1 
ATOM   5108 C  CA  . ARG   B 1 335 ? 35.690  7.687   -15.607 1.00 24.00 ? 347 ARG   B CA  1 
ATOM   5109 C  C   . ARG   B 1 335 ? 34.402  8.154   -16.284 1.00 21.58 ? 347 ARG   B C   1 
ATOM   5110 O  O   . ARG   B 1 335 ? 34.464  8.979   -17.203 1.00 23.35 ? 347 ARG   B O   1 
ATOM   5111 C  CB  . ARG   B 1 335 ? 36.654  7.119   -16.670 1.00 25.54 ? 347 ARG   B CB  1 
ATOM   5112 C  CG  . ARG   B 1 335 ? 37.913  6.416   -16.130 1.00 29.94 ? 347 ARG   B CG  1 
ATOM   5113 C  CD  . ARG   B 1 335 ? 39.101  6.432   -17.125 1.00 29.91 ? 347 ARG   B CD  1 
ATOM   5114 N  NE  . ARG   B 1 335 ? 38.817  5.764   -18.394 1.00 32.04 ? 347 ARG   B NE  1 
ATOM   5115 C  CZ  . ARG   B 1 335 ? 39.255  4.556   -18.730 1.00 34.09 ? 347 ARG   B CZ  1 
ATOM   5116 N  NH1 . ARG   B 1 335 ? 40.026  3.849   -17.922 1.00 31.20 ? 347 ARG   B NH1 1 
ATOM   5117 N  NH2 . ARG   B 1 335 ? 38.913  4.045   -19.912 1.00 33.43 ? 347 ARG   B NH2 1 
ATOM   5118 N  N   . ALA   B 1 336 ? 33.240  7.667   -15.846 1.00 20.67 ? 348 ALA   B N   1 
ATOM   5119 C  CA  . ALA   B 1 336 ? 32.014  7.900   -16.602 1.00 20.42 ? 348 ALA   B CA  1 
ATOM   5120 C  C   . ALA   B 1 336 ? 31.708  9.389   -16.704 1.00 21.81 ? 348 ALA   B C   1 
ATOM   5121 O  O   . ALA   B 1 336 ? 31.931  10.151  -15.755 1.00 22.70 ? 348 ALA   B O   1 
ATOM   5122 C  CB  . ALA   B 1 336 ? 30.836  7.166   -15.957 1.00 19.03 ? 348 ALA   B CB  1 
ATOM   5123 N  N   . ALA   B 1 337 ? 31.200  9.805   -17.865 1.00 17.41 ? 349 ALA   B N   1 
ATOM   5124 C  CA  . ALA   B 1 337 ? 30.832  11.198  -18.104 1.00 19.56 ? 349 ALA   B CA  1 
ATOM   5125 C  C   . ALA   B 1 337 ? 29.313  11.289  -18.246 1.00 20.96 ? 349 ALA   B C   1 
ATOM   5126 O  O   . ALA   B 1 337 ? 28.774  11.381  -19.347 1.00 21.70 ? 349 ALA   B O   1 
ATOM   5127 C  CB  . ALA   B 1 337 ? 31.533  11.725  -19.331 1.00 21.51 ? 349 ALA   B CB  1 
ATOM   5128 N  N   . HIS   B 1 338 ? 28.629  11.320  -17.112 1.00 24.36 ? 350 HIS   B N   1 
ATOM   5129 C  CA  . HIS   B 1 338 ? 27.183  11.463  -17.115 1.00 21.45 ? 350 HIS   B CA  1 
ATOM   5130 C  C   . HIS   B 1 338 ? 26.808  12.914  -17.379 1.00 23.85 ? 350 HIS   B C   1 
ATOM   5131 O  O   . HIS   B 1 338 ? 27.560  13.838  -17.066 1.00 25.02 ? 350 HIS   B O   1 
ATOM   5132 C  CB  . HIS   B 1 338 ? 26.603  10.968  -15.796 1.00 19.81 ? 350 HIS   B CB  1 
ATOM   5133 C  CG  . HIS   B 1 338 ? 26.907  9.527   -15.532 1.00 20.31 ? 350 HIS   B CG  1 
ATOM   5134 N  ND1 . HIS   B 1 338 ? 26.248  8.503   -16.177 1.00 21.94 ? 350 HIS   B ND1 1 
ATOM   5135 C  CD2 . HIS   B 1 338 ? 27.829  8.937   -14.734 1.00 18.98 ? 350 HIS   B CD2 1 
ATOM   5136 C  CE1 . HIS   B 1 338 ? 26.731  7.344   -15.771 1.00 20.02 ? 350 HIS   B CE1 1 
ATOM   5137 N  NE2 . HIS   B 1 338 ? 27.697  7.579   -14.899 1.00 22.05 ? 350 HIS   B NE2 1 
ATOM   5138 N  N   . SER   B 1 339 ? 25.628  13.106  -17.964 1.00 23.67 ? 351 SER   B N   1 
ATOM   5139 C  CA  . SER   B 1 339 ? 25.240  14.403  -18.497 1.00 23.87 ? 351 SER   B CA  1 
ATOM   5140 C  C   . SER   B 1 339 ? 23.922  14.869  -17.890 1.00 20.57 ? 351 SER   B C   1 
ATOM   5141 O  O   . SER   B 1 339 ? 23.104  14.064  -17.455 1.00 19.28 ? 351 SER   B O   1 
ATOM   5142 C  CB  . SER   B 1 339 ? 25.103  14.349  -20.032 1.00 17.26 ? 351 SER   B CB  1 
ATOM   5143 O  OG  . SER   B 1 339 ? 24.800  15.635  -20.533 1.00 23.75 ? 351 SER   B OG  1 
ATOM   5144 N  N   . ASN   B 1 340 ? 23.738  16.193  -17.852 1.00 24.38 ? 352 ASN   B N   1 
ATOM   5145 C  CA  . ASN   B 1 340 ? 22.419  16.791  -17.661 1.00 22.60 ? 352 ASN   B CA  1 
ATOM   5146 C  C   . ASN   B 1 340 ? 22.063  17.716  -18.819 1.00 25.91 ? 352 ASN   B C   1 
ATOM   5147 O  O   . ASN   B 1 340 ? 21.214  18.606  -18.677 1.00 25.94 ? 352 ASN   B O   1 
ATOM   5148 C  CB  . ASN   B 1 340 ? 22.330  17.526  -16.318 1.00 31.08 ? 352 ASN   B CB  1 
ATOM   5149 C  CG  . ASN   B 1 340 ? 23.145  18.803  -16.285 1.00 28.80 ? 352 ASN   B CG  1 
ATOM   5150 O  OD1 . ASN   B 1 340 ? 24.018  19.024  -17.126 1.00 31.15 ? 352 ASN   B OD1 1 
ATOM   5151 N  ND2 . ASN   B 1 340 ? 22.876  19.648  -15.283 1.00 33.80 ? 352 ASN   B ND2 1 
ATOM   5152 N  N   . GLU   B 1 341 ? 22.717  17.541  -19.961 1.00 24.10 ? 353 GLU   B N   1 
ATOM   5153 C  CA  . GLU   B 1 341 ? 22.408  18.377  -21.108 1.00 23.90 ? 353 GLU   B CA  1 
ATOM   5154 C  C   . GLU   B 1 341 ? 21.067  17.971  -21.706 1.00 26.79 ? 353 GLU   B C   1 
ATOM   5155 O  O   . GLU   B 1 341 ? 20.699  16.792  -21.714 1.00 24.83 ? 353 GLU   B O   1 
ATOM   5156 C  CB  . GLU   B 1 341 ? 23.516  18.280  -22.155 1.00 28.43 ? 353 GLU   B CB  1 
ATOM   5157 C  CG  . GLU   B 1 341 ? 24.890  18.725  -21.663 1.00 30.89 ? 353 GLU   B CG  1 
ATOM   5158 C  CD  . GLU   B 1 341 ? 25.878  18.923  -22.802 1.00 37.63 ? 353 GLU   B CD  1 
ATOM   5159 O  OE1 . GLU   B 1 341 ? 25.498  19.552  -23.813 1.00 41.64 ? 353 GLU   B OE1 1 
ATOM   5160 O  OE2 . GLU   B 1 341 ? 27.029  18.445  -22.692 1.00 41.82 ? 353 GLU   B OE2 1 
ATOM   5161 N  N   . ILE   B 1 342 ? 20.315  18.965  -22.153 1.00 26.10 ? 354 ILE   B N   1 
ATOM   5162 C  CA  . ILE   B 1 342 ? 19.174  18.749  -23.028 1.00 27.43 ? 354 ILE   B CA  1 
ATOM   5163 C  C   . ILE   B 1 342 ? 19.661  18.900  -24.459 1.00 26.12 ? 354 ILE   B C   1 
ATOM   5164 O  O   . ILE   B 1 342 ? 20.374  19.859  -24.782 1.00 24.17 ? 354 ILE   B O   1 
ATOM   5165 C  CB  . ILE   B 1 342 ? 18.041  19.741  -22.718 1.00 25.16 ? 354 ILE   B CB  1 
ATOM   5166 C  CG1 . ILE   B 1 342 ? 17.338  19.348  -21.423 1.00 23.48 ? 354 ILE   B CG1 1 
ATOM   5167 C  CG2 . ILE   B 1 342 ? 17.046  19.784  -23.857 1.00 24.11 ? 354 ILE   B CG2 1 
ATOM   5168 C  CD1 . ILE   B 1 342 ? 16.471  18.102  -21.549 1.00 25.32 ? 354 ILE   B CD1 1 
ATOM   5169 N  N   . LEU   B 1 343 ? 19.329  17.927  -25.304 1.00 25.09 ? 355 LEU   B N   1 
ATOM   5170 C  CA  . LEU   B 1 343 ? 19.629  17.975  -26.728 1.00 21.87 ? 355 LEU   B CA  1 
ATOM   5171 C  C   . LEU   B 1 343 ? 18.308  17.987  -27.480 1.00 24.13 ? 355 LEU   B C   1 
ATOM   5172 O  O   . LEU   B 1 343 ? 17.449  17.141  -27.233 1.00 25.02 ? 355 LEU   B O   1 
ATOM   5173 C  CB  . LEU   B 1 343 ? 20.485  16.775  -27.156 1.00 25.89 ? 355 LEU   B CB  1 
ATOM   5174 C  CG  . LEU   B 1 343 ? 22.015  16.860  -27.020 1.00 25.45 ? 355 LEU   B CG  1 
ATOM   5175 C  CD1 . LEU   B 1 343 ? 22.464  17.446  -25.675 1.00 29.46 ? 355 LEU   B CD1 1 
ATOM   5176 C  CD2 . LEU   B 1 343 ? 22.658  15.506  -27.256 1.00 26.13 ? 355 LEU   B CD2 1 
ATOM   5177 N  N   . ILE   B 1 344 ? 18.143  18.939  -28.393 1.00 24.95 ? 356 ILE   B N   1 
ATOM   5178 C  CA  . ILE   B 1 344 ? 16.864  19.151  -29.065 1.00 26.75 ? 356 ILE   B CA  1 
ATOM   5179 C  C   . ILE   B 1 344 ? 17.034  18.868  -30.553 1.00 25.31 ? 356 ILE   B C   1 
ATOM   5180 O  O   . ILE   B 1 344 ? 17.807  19.545  -31.238 1.00 28.71 ? 356 ILE   B O   1 
ATOM   5181 C  CB  . ILE   B 1 344 ? 16.330  20.572  -28.825 1.00 28.40 ? 356 ILE   B CB  1 
ATOM   5182 C  CG1 . ILE   B 1 344 ? 16.015  20.760  -27.337 1.00 27.04 ? 356 ILE   B CG1 1 
ATOM   5183 C  CG2 . ILE   B 1 344 ? 15.095  20.828  -29.667 1.00 25.14 ? 356 ILE   B CG2 1 
ATOM   5184 C  CD1 . ILE   B 1 344 ? 15.737  22.179  -26.944 1.00 29.01 ? 356 ILE   B CD1 1 
ATOM   5185 N  N   . PHE   B 1 345 ? 16.318  17.866  -31.041 1.00 24.43 ? 357 PHE   B N   1 
ATOM   5186 C  CA  . PHE   B 1 345 ? 16.294  17.505  -32.450 1.00 22.06 ? 357 PHE   B CA  1 
ATOM   5187 C  C   . PHE   B 1 345 ? 14.990  18.006  -33.056 1.00 28.92 ? 357 PHE   B C   1 
ATOM   5188 O  O   . PHE   B 1 345 ? 13.908  17.721  -32.530 1.00 25.77 ? 357 PHE   B O   1 
ATOM   5189 C  CB  . PHE   B 1 345 ? 16.418  15.989  -32.615 1.00 22.02 ? 357 PHE   B CB  1 
ATOM   5190 C  CG  . PHE   B 1 345 ? 17.683  15.421  -32.037 1.00 24.14 ? 357 PHE   B CG  1 
ATOM   5191 C  CD1 . PHE   B 1 345 ? 17.758  15.056  -30.706 1.00 24.09 ? 357 PHE   B CD1 1 
ATOM   5192 C  CD2 . PHE   B 1 345 ? 18.804  15.262  -32.827 1.00 24.92 ? 357 PHE   B CD2 1 
ATOM   5193 C  CE1 . PHE   B 1 345 ? 18.935  14.547  -30.175 1.00 23.25 ? 357 PHE   B CE1 1 
ATOM   5194 C  CE2 . PHE   B 1 345 ? 19.978  14.747  -32.308 1.00 24.32 ? 357 PHE   B CE2 1 
ATOM   5195 C  CZ  . PHE   B 1 345 ? 20.048  14.394  -30.980 1.00 20.78 ? 357 PHE   B CZ  1 
ATOM   5196 N  N   . SER   B 1 346 ? 15.087  18.770  -34.145 1.00 32.95 ? 358 SER   B N   1 
ATOM   5197 C  CA  . SER   B 1 346 ? 13.901  19.250  -34.858 1.00 33.57 ? 358 SER   B CA  1 
ATOM   5198 C  C   . SER   B 1 346 ? 13.670  18.320  -36.043 1.00 37.80 ? 358 SER   B C   1 
ATOM   5199 O  O   . SER   B 1 346 ? 14.267  18.489  -37.108 1.00 40.20 ? 358 SER   B O   1 
ATOM   5200 C  CB  . SER   B 1 346 ? 14.061  20.704  -35.298 1.00 38.09 ? 358 SER   B CB  1 
ATOM   5201 O  OG  . SER   B 1 346 ? 12.805  21.271  -35.642 1.00 38.71 ? 358 SER   B OG  1 
ATOM   5202 N  N   . VAL   B 1 347 ? 12.791  17.338  -35.856 1.00 38.23 ? 359 VAL   B N   1 
ATOM   5203 C  CA  . VAL   B 1 347 ? 12.577  16.311  -36.868 1.00 40.17 ? 359 VAL   B CA  1 
ATOM   5204 C  C   . VAL   B 1 347 ? 11.422  16.650  -37.806 1.00 47.78 ? 359 VAL   B C   1 
ATOM   5205 O  O   . VAL   B 1 347 ? 11.309  16.043  -38.881 1.00 50.57 ? 359 VAL   B O   1 
ATOM   5206 C  CB  . VAL   B 1 347 ? 12.364  14.951  -36.176 1.00 33.48 ? 359 VAL   B CB  1 
ATOM   5207 C  CG1 . VAL   B 1 347 ? 12.456  13.805  -37.168 1.00 34.00 ? 359 VAL   B CG1 1 
ATOM   5208 C  CG2 . VAL   B 1 347 ? 13.406  14.763  -35.087 1.00 30.24 ? 359 VAL   B CG2 1 
ATOM   5209 N  N   . GLN   B 1 348 ? 10.577  17.610  -37.446 1.00 49.65 ? 360 GLN   B N   1 
ATOM   5210 C  CA  . GLN   B 1 348 ? 9.555   18.106  -38.363 1.00 53.98 ? 360 GLN   B CA  1 
ATOM   5211 C  C   . GLN   B 1 348 ? 9.871   19.538  -38.785 1.00 55.82 ? 360 GLN   B C   1 
ATOM   5212 O  O   . GLN   B 1 348 ? 9.892   20.447  -37.955 1.00 56.61 ? 360 GLN   B O   1 
ATOM   5213 C  CB  . GLN   B 1 348 ? 8.166   18.037  -37.725 1.00 58.12 ? 360 GLN   B CB  1 
ATOM   5214 C  CG  . GLN   B 1 348 ? 7.664   16.621  -37.470 1.00 58.08 ? 360 GLN   B CG  1 
ATOM   5215 C  CD  . GLN   B 1 348 ? 7.374   15.858  -38.753 1.00 62.38 ? 360 GLN   B CD  1 
ATOM   5216 O  OE1 . GLN   B 1 348 ? 6.830   16.410  -39.710 1.00 60.72 ? 360 GLN   B OE1 1 
ATOM   5217 N  NE2 . GLN   B 1 348 ? 7.739   14.580  -38.776 1.00 56.61 ? 360 GLN   B NE2 1 
HETATM 5218 C  C10 . A1APS C 2 .   ? 25.380  10.677  18.830  1.00 22.50 ? 401 A1APS A C10 1 
HETATM 5219 C  C13 . A1APS C 2 .   ? 25.895  6.884   17.503  1.00 18.96 ? 401 A1APS A C13 1 
HETATM 5220 C  C15 . A1APS C 2 .   ? 25.347  4.564   17.166  1.00 20.88 ? 401 A1APS A C15 1 
HETATM 5221 C  C17 . A1APS C 2 .   ? 26.875  3.127   15.926  1.00 18.99 ? 401 A1APS A C17 1 
HETATM 5222 C  C20 . A1APS C 2 .   ? 28.609  5.274   15.561  1.00 20.67 ? 401 A1APS A C20 1 
HETATM 5223 C  C21 . A1APS C 2 .   ? 27.409  5.452   16.270  1.00 20.74 ? 401 A1APS A C21 1 
HETATM 5224 C  C22 . A1APS C 2 .   ? 27.079  6.719   16.794  1.00 22.85 ? 401 A1APS A C22 1 
HETATM 5225 C  C02 . A1APS C 2 .   ? 22.869  9.505   21.358  1.00 14.52 ? 401 A1APS A C02 1 
HETATM 5226 C  C04 . A1APS C 2 .   ? 23.264  7.358   22.646  1.00 19.51 ? 401 A1APS A C04 1 
HETATM 5227 C  C05 . A1APS C 2 .   ? 24.478  7.530   23.551  1.00 19.49 ? 401 A1APS A C05 1 
HETATM 5228 C  C08 . A1APS C 2 .   ? 23.166  10.328  20.103  1.00 18.73 ? 401 A1APS A C08 1 
HETATM 5229 C  C09 . A1APS C 2 .   ? 24.344  9.825   19.255  1.00 18.43 ? 401 A1APS A C09 1 
HETATM 5230 C  C12 . A1APS C 2 .   ? 25.533  8.243   18.085  1.00 21.63 ? 401 A1APS A C12 1 
HETATM 5231 C  C14 . A1APS C 2 .   ? 25.034  5.809   17.695  1.00 18.75 ? 401 A1APS A C14 1 
HETATM 5232 C  C16 . A1APS C 2 .   ? 26.553  4.389   16.451  1.00 20.02 ? 401 A1APS A C16 1 
HETATM 5233 C  C18 . A1APS C 2 .   ? 28.064  2.950   15.221  1.00 23.20 ? 401 A1APS A C18 1 
HETATM 5234 C  C19 . A1APS C 2 .   ? 28.936  4.022   15.042  1.00 22.07 ? 401 A1APS A C19 1 
HETATM 5235 N  N03 . A1APS C 2 .   ? 23.475  8.203   21.477  1.00 14.71 ? 401 A1APS A N03 1 
HETATM 5236 N  N23 . A1APS C 2 .   ? 24.461  8.529   18.831  1.00 16.76 ? 401 A1APS A N23 1 
HETATM 5237 O  O01 . A1APS C 2 .   ? 22.139  9.950   22.180  1.00 15.26 ? 401 A1APS A O01 1 
HETATM 5238 O  O06 . A1APS C 2 .   ? 24.541  6.925   24.654  1.00 19.70 ? 401 A1APS A O06 1 
HETATM 5239 O  O07 . A1APS C 2 .   ? 25.430  8.276   23.193  1.00 18.23 ? 401 A1APS A O07 1 
HETATM 5240 S  S11 . A1APS C 2 .   ? 26.405  9.689   17.911  1.00 21.63 ? 401 A1APS A S11 1 
HETATM 5241 CO CO  . NCO   D 3 .   ? -1.187  2.098   0.512   1.00 27.67 ? 402 NCO   A CO  1 
HETATM 5242 N  N1  . NCO   D 3 .   ? 0.289   2.857   1.594   1.00 25.39 ? 402 NCO   A N1  1 
HETATM 5243 N  N2  . NCO   D 3 .   ? -2.656  1.354   -0.607  1.00 31.55 ? 402 NCO   A N2  1 
HETATM 5244 N  N3  . NCO   D 3 .   ? 0.180   1.352   -0.712  1.00 29.12 ? 402 NCO   A N3  1 
HETATM 5245 N  N4  . NCO   D 3 .   ? -1.234  3.785   -0.525  1.00 34.80 ? 402 NCO   A N4  1 
HETATM 5246 N  N5  . NCO   D 3 .   ? -2.542  2.836   1.776   1.00 30.77 ? 402 NCO   A N5  1 
HETATM 5247 N  N6  . NCO   D 3 .   ? -1.103  0.410   1.537   1.00 28.68 ? 402 NCO   A N6  1 
HETATM 5248 C  C10 . A1APS E 2 .   ? 25.363  -6.822  -17.581 1.00 21.97 ? 401 A1APS B C10 1 
HETATM 5249 C  C13 . A1APS E 2 .   ? 25.943  -3.012  -16.342 1.00 22.71 ? 401 A1APS B C13 1 
HETATM 5250 C  C15 . A1APS E 2 .   ? 25.386  -0.722  -15.901 1.00 23.56 ? 401 A1APS B C15 1 
HETATM 5251 C  C17 . A1APS E 2 .   ? 26.911  0.691   -14.634 1.00 18.84 ? 401 A1APS B C17 1 
HETATM 5252 C  C20 . A1APS E 2 .   ? 28.693  -1.455  -14.407 1.00 19.69 ? 401 A1APS B C20 1 
HETATM 5253 C  C21 . A1APS E 2 .   ? 27.472  -1.620  -15.079 1.00 20.88 ? 401 A1APS B C21 1 
HETATM 5254 C  C22 . A1APS E 2 .   ? 27.146  -2.864  -15.655 1.00 24.54 ? 401 A1APS B C22 1 
HETATM 5255 C  C02 . A1APS E 2 .   ? 22.953  -5.672  -20.161 1.00 16.72 ? 401 A1APS B C02 1 
HETATM 5256 C  C04 . A1APS E 2 .   ? 23.259  -3.624  -21.557 1.00 17.43 ? 401 A1APS B C04 1 
HETATM 5257 C  C05 . A1APS E 2 .   ? 24.522  -3.699  -22.406 1.00 17.78 ? 401 A1APS B C05 1 
HETATM 5258 C  C08 . A1APS E 2 .   ? 23.205  -6.466  -18.888 1.00 20.04 ? 401 A1APS B C08 1 
HETATM 5259 C  C09 . A1APS E 2 .   ? 24.361  -5.955  -18.043 1.00 20.59 ? 401 A1APS B C09 1 
HETATM 5260 C  C12 . A1APS E 2 .   ? 25.563  -4.363  -16.924 1.00 20.26 ? 401 A1APS B C12 1 
HETATM 5261 C  C14 . A1APS E 2 .   ? 25.057  -1.944  -16.465 1.00 18.75 ? 401 A1APS B C14 1 
HETATM 5262 C  C16 . A1APS E 2 .   ? 26.597  -0.562  -15.196 1.00 21.06 ? 401 A1APS B C16 1 
HETATM 5263 C  C18 . A1APS E 2 .   ? 28.121  0.859   -13.966 1.00 22.97 ? 401 A1APS B C18 1 
HETATM 5264 C  C19 . A1APS E 2 .   ? 29.001  -0.217  -13.853 1.00 20.63 ? 401 A1APS B C19 1 
HETATM 5265 N  N03 . A1APS E 2 .   ? 23.506  -4.353  -20.319 1.00 15.67 ? 401 A1APS B N03 1 
HETATM 5266 N  N23 . A1APS E 2 .   ? 24.487  -4.649  -17.660 1.00 19.23 ? 401 A1APS B N23 1 
HETATM 5267 O  O01 . A1APS E 2 .   ? 22.296  -6.151  -21.016 1.00 17.08 ? 401 A1APS B O01 1 
HETATM 5268 O  O06 . A1APS E 2 .   ? 24.539  -3.160  -23.547 1.00 19.70 ? 401 A1APS B O06 1 
HETATM 5269 O  O07 . A1APS E 2 .   ? 25.545  -4.312  -21.983 1.00 16.25 ? 401 A1APS B O07 1 
HETATM 5270 S  S11 . A1APS E 2 .   ? 26.396  -5.820  -16.677 1.00 23.35 ? 401 A1APS B S11 1 
HETATM 5271 O  O   . HOH   F 4 .   ? 32.115  3.468   34.526  1.00 27.89 ? 501 HOH   A O   1 
HETATM 5272 O  O   . HOH   F 4 .   ? 13.018  18.795  29.569  1.00 22.74 ? 502 HOH   A O   1 
HETATM 5273 O  O   . HOH   F 4 .   ? 2.688   -21.421 30.403  1.00 40.58 ? 503 HOH   A O   1 
HETATM 5274 O  O   . HOH   F 4 .   ? 5.670   19.788  32.460  1.00 31.01 ? 504 HOH   A O   1 
HETATM 5275 O  O   . HOH   F 4 .   ? 22.281  5.701   16.850  1.00 24.07 ? 505 HOH   A O   1 
HETATM 5276 O  O   . HOH   F 4 .   ? 20.932  7.862   15.006  1.00 24.33 ? 506 HOH   A O   1 
HETATM 5277 O  O   . HOH   F 4 .   ? 7.719   -22.980 18.672  1.00 41.53 ? 507 HOH   A O   1 
HETATM 5278 O  O   . HOH   F 4 .   ? 6.229   12.443  3.692   1.00 36.27 ? 508 HOH   A O   1 
HETATM 5279 O  O   . HOH   F 4 .   ? 18.519  -14.222 40.876  1.00 34.33 ? 509 HOH   A O   1 
HETATM 5280 O  O   . HOH   F 4 .   ? -1.469  4.640   3.911   1.00 35.02 ? 510 HOH   A O   1 
HETATM 5281 O  O   . HOH   F 4 .   ? -0.080  -17.607 20.004  1.00 45.92 ? 511 HOH   A O   1 
HETATM 5282 O  O   . HOH   F 4 .   ? 29.947  23.730  20.919  1.00 30.46 ? 512 HOH   A O   1 
HETATM 5283 O  O   . HOH   F 4 .   ? -3.358  17.181  17.025  1.00 28.11 ? 513 HOH   A O   1 
HETATM 5284 O  O   . HOH   F 4 .   ? 9.653   -6.862  7.593   1.00 27.53 ? 514 HOH   A O   1 
HETATM 5285 O  O   . HOH   F 4 .   ? 35.872  -7.009  19.108  1.00 30.58 ? 515 HOH   A O   1 
HETATM 5286 O  O   . HOH   F 4 .   ? -9.914  9.570   20.897  1.00 29.85 ? 516 HOH   A O   1 
HETATM 5287 O  O   . HOH   F 4 .   ? 5.095   12.156  7.632   1.00 31.19 ? 517 HOH   A O   1 
HETATM 5288 O  O   . HOH   F 4 .   ? 0.937   -15.571 20.669  1.00 40.93 ? 518 HOH   A O   1 
HETATM 5289 O  O   . HOH   F 4 .   ? 18.218  -17.200 34.140  1.00 34.84 ? 519 HOH   A O   1 
HETATM 5290 O  O   . HOH   F 4 .   ? 15.667  10.386  39.976  1.00 21.03 ? 520 HOH   A O   1 
HETATM 5291 O  O   . HOH   F 4 .   ? 28.525  -14.375 33.057  1.00 29.38 ? 521 HOH   A O   1 
HETATM 5292 O  O   . HOH   F 4 .   ? 5.764   -4.174  -1.109  1.00 25.73 ? 522 HOH   A O   1 
HETATM 5293 O  O   . HOH   F 4 .   ? 9.869   14.841  36.785  1.00 28.07 ? 523 HOH   A O   1 
HETATM 5294 O  O   . HOH   F 4 .   ? 23.778  -18.523 15.949  1.00 47.37 ? 524 HOH   A O   1 
HETATM 5295 O  O   . HOH   F 4 .   ? -3.253  2.036   22.140  1.00 29.55 ? 525 HOH   A O   1 
HETATM 5296 O  O   . HOH   F 4 .   ? 7.683   18.009  38.559  1.00 36.83 ? 526 HOH   A O   1 
HETATM 5297 O  O   . HOH   F 4 .   ? -7.293  6.987   26.404  1.00 25.08 ? 527 HOH   A O   1 
HETATM 5298 O  O   . HOH   F 4 .   ? 3.725   9.861   43.005  1.00 27.04 ? 528 HOH   A O   1 
HETATM 5299 O  O   . HOH   F 4 .   ? 18.900  19.394  11.993  1.00 28.12 ? 529 HOH   A O   1 
HETATM 5300 O  O   . HOH   F 4 .   ? 6.354   13.609  42.579  1.00 26.36 ? 530 HOH   A O   1 
HETATM 5301 O  O   . HOH   F 4 .   ? 10.974  -0.855  27.665  1.00 11.22 ? 531 HOH   A O   1 
HETATM 5302 O  O   . HOH   F 4 .   ? 30.787  6.470   34.264  1.00 27.04 ? 532 HOH   A O   1 
HETATM 5303 O  O   . HOH   F 4 .   ? -1.697  19.840  32.221  1.00 32.12 ? 533 HOH   A O   1 
HETATM 5304 O  O   . HOH   F 4 .   ? 28.547  -0.645  15.875  1.00 18.63 ? 534 HOH   A O   1 
HETATM 5305 O  O   . HOH   F 4 .   ? 15.746  4.663   23.869  1.00 13.73 ? 535 HOH   A O   1 
HETATM 5306 O  O   . HOH   F 4 .   ? 9.558   24.228  21.274  1.00 33.86 ? 536 HOH   A O   1 
HETATM 5307 O  O   . HOH   F 4 .   ? 15.754  11.226  6.627   1.00 23.88 ? 537 HOH   A O   1 
HETATM 5308 O  O   . HOH   F 4 .   ? 16.288  9.203   47.802  1.00 37.34 ? 538 HOH   A O   1 
HETATM 5309 O  O   . HOH   F 4 .   ? -1.013  -4.943  8.583   1.00 25.67 ? 539 HOH   A O   1 
HETATM 5310 O  O   . HOH   F 4 .   ? 22.436  -10.687 23.714  1.00 23.73 ? 540 HOH   A O   1 
HETATM 5311 O  O   . HOH   F 4 .   ? 8.016   4.610   43.331  1.00 24.20 ? 541 HOH   A O   1 
HETATM 5312 O  O   . HOH   F 4 .   ? 25.060  21.486  7.492   1.00 46.38 ? 542 HOH   A O   1 
HETATM 5313 O  O   . HOH   F 4 .   ? -3.964  12.080  19.481  1.00 22.28 ? 543 HOH   A O   1 
HETATM 5314 O  O   . HOH   F 4 .   ? 12.464  23.232  15.796  1.00 38.26 ? 544 HOH   A O   1 
HETATM 5315 O  O   . HOH   F 4 .   ? 16.116  21.750  27.269  1.00 27.68 ? 545 HOH   A O   1 
HETATM 5316 O  O   . HOH   F 4 .   ? -0.461  15.370  9.130   1.00 27.01 ? 546 HOH   A O   1 
HETATM 5317 O  O   . HOH   F 4 .   ? 26.674  -14.594 38.657  1.00 40.62 ? 547 HOH   A O   1 
HETATM 5318 O  O   . HOH   F 4 .   ? -0.261  -11.787 28.559  1.00 37.68 ? 548 HOH   A O   1 
HETATM 5319 O  O   . HOH   F 4 .   ? 33.389  -5.811  14.745  1.00 29.62 ? 549 HOH   A O   1 
HETATM 5320 O  O   . HOH   F 4 .   ? -1.158  0.828   30.182  1.00 27.16 ? 550 HOH   A O   1 
HETATM 5321 O  O   . HOH   F 4 .   ? 17.349  2.388   46.043  1.00 21.50 ? 551 HOH   A O   1 
HETATM 5322 O  O   . HOH   F 4 .   ? 6.399   1.535   28.297  1.00 18.41 ? 552 HOH   A O   1 
HETATM 5323 O  O   . HOH   F 4 .   ? 3.740   17.077  26.189  1.00 26.87 ? 553 HOH   A O   1 
HETATM 5324 O  O   . HOH   F 4 .   ? 30.036  -8.004  15.611  1.00 32.72 ? 554 HOH   A O   1 
HETATM 5325 O  O   . HOH   F 4 .   ? -1.092  5.429   39.571  1.00 23.55 ? 555 HOH   A O   1 
HETATM 5326 O  O   . HOH   F 4 .   ? 5.216   17.771  16.687  1.00 27.74 ? 556 HOH   A O   1 
HETATM 5327 O  O   . HOH   F 4 .   ? 27.839  -18.788 26.670  1.00 31.47 ? 557 HOH   A O   1 
HETATM 5328 O  O   . HOH   F 4 .   ? 19.703  0.002   46.758  1.00 19.50 ? 558 HOH   A O   1 
HETATM 5329 O  O   . HOH   F 4 .   ? 15.613  20.411  10.989  1.00 34.31 ? 559 HOH   A O   1 
HETATM 5330 O  O   . HOH   F 4 .   ? 15.373  0.038   18.742  1.00 19.71 ? 560 HOH   A O   1 
HETATM 5331 O  O   . HOH   F 4 .   ? 15.381  15.244  18.946  1.00 20.25 ? 561 HOH   A O   1 
HETATM 5332 O  O   . HOH   F 4 .   ? 0.912   13.679  10.333  1.00 27.82 ? 562 HOH   A O   1 
HETATM 5333 O  O   . HOH   F 4 .   ? 18.673  -11.759 10.136  1.00 31.66 ? 563 HOH   A O   1 
HETATM 5334 O  O   . HOH   F 4 .   ? -4.371  15.230  22.909  1.00 26.22 ? 564 HOH   A O   1 
HETATM 5335 O  O   . HOH   F 4 .   ? 5.873   5.527   40.964  1.00 27.26 ? 565 HOH   A O   1 
HETATM 5336 O  O   . HOH   F 4 .   ? 7.586   -1.346  23.377  1.00 23.20 ? 566 HOH   A O   1 
HETATM 5337 O  O   . HOH   F 4 .   ? 17.657  2.330   26.228  1.00 13.77 ? 567 HOH   A O   1 
HETATM 5338 O  O   . HOH   F 4 .   ? 15.218  -0.448  14.671  1.00 13.73 ? 568 HOH   A O   1 
HETATM 5339 O  O   . HOH   F 4 .   ? -5.159  10.013  29.275  1.00 28.53 ? 569 HOH   A O   1 
HETATM 5340 O  O   . HOH   F 4 .   ? 16.813  4.948   2.938   1.00 26.70 ? 570 HOH   A O   1 
HETATM 5341 O  O   . HOH   F 4 .   ? 18.125  1.797   5.355   1.00 22.23 ? 571 HOH   A O   1 
HETATM 5342 O  O   . HOH   F 4 .   ? 14.334  15.103  16.000  1.00 16.51 ? 572 HOH   A O   1 
HETATM 5343 O  O   . HOH   F 4 .   ? 11.802  12.827  7.845   1.00 23.27 ? 573 HOH   A O   1 
HETATM 5344 O  O   . HOH   F 4 .   ? 18.741  -1.489  25.113  1.00 19.64 ? 574 HOH   A O   1 
HETATM 5345 O  O   . HOH   F 4 .   ? 9.628   -6.236  46.323  1.00 30.40 ? 575 HOH   A O   1 
HETATM 5346 O  O   . HOH   F 4 .   ? 2.603   -6.960  42.083  1.00 32.02 ? 576 HOH   A O   1 
HETATM 5347 O  O   . HOH   F 4 .   ? 25.166  12.605  15.218  1.00 26.71 ? 577 HOH   A O   1 
HETATM 5348 O  O   . HOH   F 4 .   ? 26.882  8.201   20.909  1.00 24.39 ? 578 HOH   A O   1 
HETATM 5349 O  O   . HOH   F 4 .   ? 27.309  12.498  20.953  1.00 22.56 ? 579 HOH   A O   1 
HETATM 5350 O  O   . HOH   F 4 .   ? -3.700  0.376   28.602  1.00 26.25 ? 580 HOH   A O   1 
HETATM 5351 O  O   . HOH   F 4 .   ? 27.384  6.861   33.824  1.00 15.16 ? 581 HOH   A O   1 
HETATM 5352 O  O   . HOH   F 4 .   ? 8.695   -19.104 17.460  1.00 33.61 ? 582 HOH   A O   1 
HETATM 5353 O  O   . HOH   F 4 .   ? 6.785   24.984  9.945   1.00 45.19 ? 583 HOH   A O   1 
HETATM 5354 O  O   . HOH   F 4 .   ? 21.640  11.909  36.292  1.00 30.06 ? 584 HOH   A O   1 
HETATM 5355 O  O   . HOH   F 4 .   ? 11.364  -3.833  27.792  1.00 22.90 ? 585 HOH   A O   1 
HETATM 5356 O  O   . HOH   F 4 .   ? 23.411  -7.648  38.767  1.00 23.39 ? 586 HOH   A O   1 
HETATM 5357 O  O   . HOH   F 4 .   ? 22.218  19.296  4.841   1.00 51.62 ? 587 HOH   A O   1 
HETATM 5358 O  O   . HOH   F 4 .   ? 25.172  0.293   39.157  1.00 22.28 ? 588 HOH   A O   1 
HETATM 5359 O  O   . HOH   F 4 .   ? 10.039  5.007   7.686   1.00 28.69 ? 589 HOH   A O   1 
HETATM 5360 O  O   . HOH   F 4 .   ? 35.756  7.020   34.829  1.00 33.37 ? 590 HOH   A O   1 
HETATM 5361 O  O   . HOH   F 4 .   ? 17.705  -2.795  48.055  1.00 25.11 ? 591 HOH   A O   1 
HETATM 5362 O  O   . HOH   F 4 .   ? 11.454  21.772  20.810  1.00 23.60 ? 592 HOH   A O   1 
HETATM 5363 O  O   . HOH   F 4 .   ? 34.172  3.995   35.958  1.00 34.51 ? 593 HOH   A O   1 
HETATM 5364 O  O   . HOH   F 4 .   ? 7.618   12.428  21.062  1.00 17.85 ? 594 HOH   A O   1 
HETATM 5365 O  O   . HOH   F 4 .   ? 6.513   0.259   25.347  1.00 26.09 ? 595 HOH   A O   1 
HETATM 5366 O  O   . HOH   F 4 .   ? 14.179  -9.026  23.656  1.00 20.17 ? 596 HOH   A O   1 
HETATM 5367 O  O   . HOH   F 4 .   ? 7.905   -11.934 32.950  1.00 33.15 ? 597 HOH   A O   1 
HETATM 5368 O  O   . HOH   F 4 .   ? 12.164  -4.963  23.573  1.00 26.10 ? 598 HOH   A O   1 
HETATM 5369 O  O   . HOH   F 4 .   ? 11.955  -2.924  21.064  1.00 17.66 ? 599 HOH   A O   1 
HETATM 5370 O  O   . HOH   F 4 .   ? 25.641  7.504   37.943  1.00 22.48 ? 600 HOH   A O   1 
HETATM 5371 O  O   . HOH   F 4 .   ? 6.166   17.859  24.753  1.00 20.90 ? 601 HOH   A O   1 
HETATM 5372 O  O   . HOH   F 4 .   ? 15.072  -5.059  31.148  1.00 18.06 ? 602 HOH   A O   1 
HETATM 5373 O  O   . HOH   F 4 .   ? 27.861  15.740  22.744  1.00 28.71 ? 603 HOH   A O   1 
HETATM 5374 O  O   . HOH   F 4 .   ? 35.530  2.662   14.121  1.00 28.00 ? 604 HOH   A O   1 
HETATM 5375 O  O   . HOH   F 4 .   ? 17.239  -3.118  9.467   1.00 19.34 ? 605 HOH   A O   1 
HETATM 5376 O  O   . HOH   F 4 .   ? 9.900   15.146  18.486  1.00 19.66 ? 606 HOH   A O   1 
HETATM 5377 O  O   . HOH   F 4 .   ? 13.489  4.051   19.689  1.00 15.32 ? 607 HOH   A O   1 
HETATM 5378 O  O   . HOH   F 4 .   ? -1.269  17.667  16.087  1.00 26.56 ? 608 HOH   A O   1 
HETATM 5379 O  O   . HOH   F 4 .   ? 17.612  -1.982  20.253  1.00 18.47 ? 609 HOH   A O   1 
HETATM 5380 O  O   . HOH   F 4 .   ? 14.397  -7.366  10.090  1.00 21.77 ? 610 HOH   A O   1 
HETATM 5381 O  O   . HOH   F 4 .   ? -7.924  14.065  13.174  1.00 29.02 ? 611 HOH   A O   1 
HETATM 5382 O  O   . HOH   F 4 .   ? 28.425  -8.047  13.298  1.00 28.14 ? 612 HOH   A O   1 
HETATM 5383 O  O   . HOH   F 4 .   ? 16.021  -9.495  10.192  1.00 23.28 ? 613 HOH   A O   1 
HETATM 5384 O  O   . HOH   F 4 .   ? 30.184  -10.474 17.453  1.00 29.71 ? 614 HOH   A O   1 
HETATM 5385 O  O   . HOH   F 4 .   ? 7.984   17.994  26.969  1.00 24.18 ? 615 HOH   A O   1 
HETATM 5386 O  O   . HOH   F 4 .   ? 19.636  4.793   15.413  1.00 12.40 ? 616 HOH   A O   1 
HETATM 5387 O  O   . HOH   F 4 .   ? 31.782  6.165   16.002  1.00 24.98 ? 617 HOH   A O   1 
HETATM 5388 O  O   . HOH   F 4 .   ? 9.460   4.867   10.743  1.00 18.00 ? 618 HOH   A O   1 
HETATM 5389 O  O   . HOH   F 4 .   ? 34.055  -2.206  19.500  1.00 23.59 ? 619 HOH   A O   1 
HETATM 5390 O  O   . HOH   F 4 .   ? 3.510   22.443  36.211  1.00 36.14 ? 620 HOH   A O   1 
HETATM 5391 O  O   . HOH   F 4 .   ? -0.762  -8.436  8.012   1.00 32.40 ? 621 HOH   A O   1 
HETATM 5392 O  O   . HOH   F 4 .   ? 6.009   17.013  28.697  1.00 23.83 ? 622 HOH   A O   1 
HETATM 5393 O  O   . HOH   F 4 .   ? 6.619   16.800  12.156  1.00 26.79 ? 623 HOH   A O   1 
HETATM 5394 O  O   . HOH   F 4 .   ? 13.884  -3.417  25.334  1.00 26.08 ? 624 HOH   A O   1 
HETATM 5395 O  O   . HOH   F 4 .   ? 4.687   -17.297 27.907  1.00 33.18 ? 625 HOH   A O   1 
HETATM 5396 O  O   . HOH   F 4 .   ? -1.985  18.513  20.123  1.00 26.59 ? 626 HOH   A O   1 
HETATM 5397 O  O   . HOH   F 4 .   ? 13.655  -1.315  27.513  1.00 20.76 ? 627 HOH   A O   1 
HETATM 5398 O  O   . HOH   F 4 .   ? 9.395   20.442  28.085  1.00 24.92 ? 628 HOH   A O   1 
HETATM 5399 O  O   . HOH   F 4 .   ? 12.211  1.456   26.483  1.00 19.65 ? 629 HOH   A O   1 
HETATM 5400 O  O   . HOH   F 4 .   ? 16.719  -15.690 39.482  1.00 35.85 ? 630 HOH   A O   1 
HETATM 5401 O  O   . HOH   F 4 .   ? 15.805  -0.722  25.630  1.00 16.26 ? 631 HOH   A O   1 
HETATM 5402 O  O   . HOH   F 4 .   ? 10.455  -0.480  20.992  1.00 22.89 ? 632 HOH   A O   1 
HETATM 5403 O  O   . HOH   F 4 .   ? -1.814  -14.337 6.095   1.00 50.69 ? 633 HOH   A O   1 
HETATM 5404 O  O   . HOH   F 4 .   ? 10.887  25.425  24.675  1.00 36.48 ? 634 HOH   A O   1 
HETATM 5405 O  O   . HOH   F 4 .   ? 23.892  6.693   41.144  1.00 26.85 ? 635 HOH   A O   1 
HETATM 5406 O  O   . HOH   F 4 .   ? 33.022  -5.686  27.244  1.00 23.18 ? 636 HOH   A O   1 
HETATM 5407 O  O   . HOH   F 4 .   ? 28.326  -4.195  34.845  1.00 22.25 ? 637 HOH   A O   1 
HETATM 5408 O  O   . HOH   F 4 .   ? 0.172   9.940   40.200  1.00 26.64 ? 638 HOH   A O   1 
HETATM 5409 O  O   . HOH   F 4 .   ? 16.160  15.784  33.979  1.00 24.87 ? 639 HOH   A O   1 
HETATM 5410 O  O   . HOH   F 4 .   ? 8.297   14.738  41.690  1.00 30.58 ? 640 HOH   A O   1 
HETATM 5411 O  O   . HOH   F 4 .   ? 5.951   -5.500  23.476  1.00 25.15 ? 641 HOH   A O   1 
HETATM 5412 O  O   . HOH   F 4 .   ? -0.314  -7.939  21.904  1.00 30.18 ? 642 HOH   A O   1 
HETATM 5413 O  O   . HOH   F 4 .   ? -12.670 8.471   18.483  1.00 24.64 ? 643 HOH   A O   1 
HETATM 5414 O  O   . HOH   F 4 .   ? 26.230  -2.081  42.918  1.00 27.56 ? 644 HOH   A O   1 
HETATM 5415 O  O   . HOH   F 4 .   ? 2.537   7.713   5.459   1.00 29.55 ? 645 HOH   A O   1 
HETATM 5416 O  O   . HOH   F 4 .   ? 19.999  7.947   46.634  1.00 30.66 ? 646 HOH   A O   1 
HETATM 5417 O  O   . HOH   F 4 .   ? 3.585   8.318   8.832   1.00 22.28 ? 647 HOH   A O   1 
HETATM 5418 O  O   . HOH   F 4 .   ? 1.162   17.249  17.651  1.00 26.74 ? 648 HOH   A O   1 
HETATM 5419 O  O   . HOH   F 4 .   ? -8.519  1.868   24.459  1.00 20.60 ? 649 HOH   A O   1 
HETATM 5420 O  O   . HOH   F 4 .   ? 25.062  10.150  35.507  1.00 28.26 ? 650 HOH   A O   1 
HETATM 5421 O  O   . HOH   F 4 .   ? -6.414  13.939  35.000  1.00 31.90 ? 651 HOH   A O   1 
HETATM 5422 O  O   . HOH   F 4 .   ? 20.738  -4.550  46.314  1.00 20.50 ? 652 HOH   A O   1 
HETATM 5423 O  O   . HOH   F 4 .   ? 7.951   11.268  43.066  1.00 27.57 ? 653 HOH   A O   1 
HETATM 5424 O  O   . HOH   F 4 .   ? 16.556  2.250   19.973  1.00 12.42 ? 654 HOH   A O   1 
HETATM 5425 O  O   . HOH   F 4 .   ? 7.435   -18.648 28.123  1.00 35.45 ? 655 HOH   A O   1 
HETATM 5426 O  O   . HOH   F 4 .   ? 16.469  -1.061  22.407  1.00 20.99 ? 656 HOH   A O   1 
HETATM 5427 O  O   . HOH   F 4 .   ? -11.155 3.555   13.876  1.00 27.42 ? 657 HOH   A O   1 
HETATM 5428 O  O   . HOH   F 4 .   ? 8.699   0.092   26.423  1.00 25.49 ? 658 HOH   A O   1 
HETATM 5429 O  O   . HOH   F 4 .   ? 10.436  10.468  45.279  1.00 25.65 ? 659 HOH   A O   1 
HETATM 5430 O  O   . HOH   F 4 .   ? 19.603  -5.370  4.049   1.00 26.14 ? 660 HOH   A O   1 
HETATM 5431 O  O   . HOH   F 4 .   ? 7.734   -6.470  28.036  1.00 17.67 ? 661 HOH   A O   1 
HETATM 5432 O  O   . HOH   F 4 .   ? 22.495  -1.768  4.514   1.00 28.94 ? 662 HOH   A O   1 
HETATM 5433 O  O   . HOH   F 4 .   ? 4.692   -3.028  23.437  1.00 24.90 ? 663 HOH   A O   1 
HETATM 5434 O  O   . HOH   F 4 .   ? 6.095   -5.773  30.418  1.00 26.44 ? 664 HOH   A O   1 
HETATM 5435 O  O   . HOH   F 4 .   ? 6.248   -1.254  29.134  1.00 15.24 ? 665 HOH   A O   1 
HETATM 5436 O  O   . HOH   F 4 .   ? 25.223  -11.493 39.467  1.00 32.91 ? 666 HOH   A O   1 
HETATM 5437 O  O   . HOH   F 4 .   ? -6.337  12.174  29.067  1.00 29.47 ? 667 HOH   A O   1 
HETATM 5438 O  O   . HOH   F 4 .   ? 17.281  6.164   40.388  1.00 24.35 ? 668 HOH   A O   1 
HETATM 5439 O  O   . HOH   F 4 .   ? 3.838   0.024   27.167  1.00 19.39 ? 669 HOH   A O   1 
HETATM 5440 O  O   . HOH   F 4 .   ? 14.563  1.542   25.489  1.00 20.65 ? 670 HOH   A O   1 
HETATM 5441 O  O   . HOH   F 4 .   ? -1.502  12.625  39.461  1.00 26.08 ? 671 HOH   A O   1 
HETATM 5442 O  O   . HOH   F 4 .   ? 6.304   -3.925  49.016  1.00 20.38 ? 672 HOH   A O   1 
HETATM 5443 O  O   . HOH   F 4 .   ? 9.970   1.847   24.913  1.00 17.97 ? 673 HOH   A O   1 
HETATM 5444 O  O   . HOH   F 4 .   ? 0.984   23.389  32.411  1.00 30.95 ? 674 HOH   A O   1 
HETATM 5445 O  O   . HOH   F 4 .   ? 19.419  -19.174 24.558  1.00 38.35 ? 675 HOH   A O   1 
HETATM 5446 O  O   . HOH   F 4 .   ? 36.141  -2.017  21.140  1.00 21.30 ? 676 HOH   A O   1 
HETATM 5447 O  O   . HOH   F 4 .   ? 18.338  -15.450 35.763  1.00 30.31 ? 677 HOH   A O   1 
HETATM 5448 O  O   . HOH   F 4 .   ? 6.240   2.331   0.373   1.00 33.56 ? 678 HOH   A O   1 
HETATM 5449 O  O   . HOH   F 4 .   ? 16.060  0.735   3.243   1.00 22.92 ? 679 HOH   A O   1 
HETATM 5450 O  O   . HOH   F 4 .   ? -3.347  5.119   5.857   1.00 28.55 ? 680 HOH   A O   1 
HETATM 5451 O  O   . HOH   F 4 .   ? 25.175  -8.378  44.234  1.00 33.36 ? 681 HOH   A O   1 
HETATM 5452 O  O   . HOH   F 4 .   ? 27.923  -18.726 33.351  1.00 34.64 ? 682 HOH   A O   1 
HETATM 5453 O  O   . HOH   F 4 .   ? -6.134  12.706  20.720  1.00 31.27 ? 683 HOH   A O   1 
HETATM 5454 O  O   . HOH   F 4 .   ? 17.629  8.478   41.005  1.00 32.10 ? 684 HOH   A O   1 
HETATM 5455 O  O   . HOH   F 4 .   ? 8.495   2.246   1.949   1.00 33.15 ? 685 HOH   A O   1 
HETATM 5456 O  O   . HOH   F 4 .   ? 17.438  9.527   43.736  1.00 32.65 ? 686 HOH   A O   1 
HETATM 5457 O  O   . HOH   F 4 .   ? 19.835  9.173   42.407  1.00 30.85 ? 687 HOH   A O   1 
HETATM 5458 O  O   . HOH   F 4 .   ? 13.623  1.632   21.524  1.00 23.24 ? 688 HOH   A O   1 
HETATM 5459 O  O   . HOH   F 4 .   ? -1.292  -14.331 25.558  1.00 39.74 ? 689 HOH   A O   1 
HETATM 5460 O  O   . HOH   F 4 .   ? 20.576  13.319  38.779  1.00 36.13 ? 690 HOH   A O   1 
HETATM 5461 O  O   . HOH   F 4 .   ? 8.109   -5.259  24.560  1.00 29.30 ? 691 HOH   A O   1 
HETATM 5462 O  O   . HOH   F 4 .   ? 5.394   22.823  33.384  1.00 32.38 ? 692 HOH   A O   1 
HETATM 5463 O  O   . HOH   F 4 .   ? -2.422  -6.724  40.445  1.00 32.63 ? 693 HOH   A O   1 
HETATM 5464 O  O   . HOH   F 4 .   ? 5.627   21.068  11.838  1.00 49.55 ? 694 HOH   A O   1 
HETATM 5465 O  O   . HOH   F 4 .   ? 17.224  3.392   22.160  1.00 18.41 ? 695 HOH   A O   1 
HETATM 5466 O  O   . HOH   F 4 .   ? 31.449  11.180  24.224  1.00 34.01 ? 696 HOH   A O   1 
HETATM 5467 O  O   . HOH   F 4 .   ? 25.878  -8.372  38.306  1.00 29.50 ? 697 HOH   A O   1 
HETATM 5468 O  O   . HOH   F 4 .   ? 30.096  11.673  26.622  1.00 28.59 ? 698 HOH   A O   1 
HETATM 5469 O  O   . HOH   F 4 .   ? -3.376  20.760  22.314  1.00 32.95 ? 699 HOH   A O   1 
HETATM 5470 O  O   . HOH   F 4 .   ? 2.820   -23.767 28.871  1.00 37.67 ? 700 HOH   A O   1 
HETATM 5471 O  O   . HOH   F 4 .   ? 29.652  9.910   35.710  1.00 29.74 ? 701 HOH   A O   1 
HETATM 5472 O  O   . HOH   F 4 .   ? -5.914  16.615  21.666  1.00 35.97 ? 702 HOH   A O   1 
HETATM 5473 O  O   . HOH   F 4 .   ? 18.302  1.128   23.857  1.00 16.19 ? 703 HOH   A O   1 
HETATM 5474 O  O   . HOH   F 4 .   ? 3.012   -3.190  25.712  1.00 36.02 ? 704 HOH   A O   1 
HETATM 5475 O  O   . HOH   F 4 .   ? -13.007 4.840   12.816  1.00 27.95 ? 705 HOH   A O   1 
HETATM 5476 O  O   . HOH   F 4 .   ? 27.359  21.559  7.563   1.00 42.10 ? 706 HOH   A O   1 
HETATM 5477 O  O   . HOH   F 4 .   ? 7.445   10.750  1.711   1.00 33.71 ? 707 HOH   A O   1 
HETATM 5478 O  O   . HOH   F 4 .   ? 18.243  -19.246 22.598  1.00 36.98 ? 708 HOH   A O   1 
HETATM 5479 O  O   . HOH   F 4 .   ? -2.286  -3.129  34.403  1.00 26.98 ? 709 HOH   A O   1 
HETATM 5480 O  O   . HOH   F 4 .   ? -7.515  11.044  36.043  1.00 27.65 ? 710 HOH   A O   1 
HETATM 5481 O  O   . HOH   F 4 .   ? -4.657  18.501  21.418  1.00 28.92 ? 711 HOH   A O   1 
HETATM 5482 O  O   . HOH   F 4 .   ? 24.575  12.300  35.464  1.00 37.28 ? 712 HOH   A O   1 
HETATM 5483 O  O   . HOH   F 4 .   ? -0.421  19.350  17.750  1.00 29.96 ? 713 HOH   A O   1 
HETATM 5484 O  O   . HOH   F 4 .   ? 19.303  11.362  42.169  1.00 35.21 ? 714 HOH   A O   1 
HETATM 5485 O  O   . HOH   F 4 .   ? -1.569  22.861  33.118  1.00 29.67 ? 715 HOH   A O   1 
HETATM 5486 O  O   . HOH   F 4 .   ? -2.046  -2.320  26.015  1.00 25.36 ? 716 HOH   A O   1 
HETATM 5487 O  O   . HOH   F 4 .   ? 38.831  2.523   9.664   1.00 36.03 ? 717 HOH   A O   1 
HETATM 5488 O  O   . HOH   F 4 .   ? 27.497  19.737  3.268   1.00 35.24 ? 718 HOH   A O   1 
HETATM 5489 O  O   . HOH   F 4 .   ? -6.066  1.018   8.045   1.00 40.81 ? 719 HOH   A O   1 
HETATM 5490 O  O   . HOH   F 4 .   ? 6.661   27.355  7.975   1.00 34.70 ? 720 HOH   A O   1 
HETATM 5491 O  O   . HOH   F 4 .   ? 2.148   -7.604  33.222  1.00 40.65 ? 721 HOH   A O   1 
HETATM 5492 O  O   . HOH   F 4 .   ? 26.741  24.059  7.610   1.00 44.48 ? 722 HOH   A O   1 
HETATM 5493 O  O   . HOH   F 4 .   ? 30.866  14.614  35.280  1.00 36.73 ? 723 HOH   A O   1 
HETATM 5494 O  O   . HOH   F 4 .   ? 33.189  14.477  35.334  1.00 35.55 ? 724 HOH   A O   1 
HETATM 5495 O  O   . HOH   F 4 .   ? 27.327  22.547  3.004   1.00 39.03 ? 725 HOH   A O   1 
HETATM 5496 O  O   . HOH   F 4 .   ? -8.267  2.609   8.753   1.00 32.37 ? 726 HOH   A O   1 
HETATM 5497 O  O   . HOH   G 4 .   ? 9.829   -7.917  -42.757 1.00 32.97 ? 501 HOH   B O   1 
HETATM 5498 O  O   . HOH   G 4 .   ? 9.457   -20.385 -20.416 1.00 33.85 ? 502 HOH   B O   1 
HETATM 5499 O  O   . HOH   G 4 .   ? 10.472  -10.246 -42.395 1.00 36.71 ? 503 HOH   B O   1 
HETATM 5500 O  O   . HOH   G 4 .   ? 6.186   6.474   -47.714 1.00 25.62 ? 504 HOH   B O   1 
HETATM 5501 O  O   . HOH   G 4 .   ? 10.012  10.876  -6.760  1.00 23.14 ? 505 HOH   B O   1 
HETATM 5502 O  O   . HOH   G 4 .   ? 12.819  22.147  -25.537 1.00 35.02 ? 506 HOH   B O   1 
HETATM 5503 O  O   . HOH   G 4 .   ? 23.500  -20.170 -20.851 1.00 30.37 ? 507 HOH   B O   1 
HETATM 5504 O  O   . HOH   G 4 .   ? 22.174  -7.632  -35.039 1.00 28.11 ? 508 HOH   B O   1 
HETATM 5505 O  O   . HOH   G 4 .   ? -3.085  2.005   -21.486 1.00 29.45 ? 509 HOH   B O   1 
HETATM 5506 O  O   . HOH   G 4 .   ? 11.810  7.352   -26.920 1.00 20.06 ? 510 HOH   B O   1 
HETATM 5507 O  O   . HOH   G 4 .   ? -1.344  18.027  -3.058  1.00 42.12 ? 511 HOH   B O   1 
HETATM 5508 O  O   . HOH   G 4 .   ? 13.551  2.450   -49.847 1.00 33.02 ? 512 HOH   B O   1 
HETATM 5509 O  O   . HOH   G 4 .   ? 9.592   21.059  -28.258 1.00 35.14 ? 513 HOH   B O   1 
HETATM 5510 O  O   . HOH   G 4 .   ? 15.683  -6.802  -38.784 1.00 21.12 ? 514 HOH   B O   1 
HETATM 5511 O  O   . HOH   G 4 .   ? 8.781   20.986  -30.556 1.00 39.99 ? 515 HOH   B O   1 
HETATM 5512 O  O   . HOH   G 4 .   ? 6.166   7.819   2.090   1.00 29.43 ? 516 HOH   B O   1 
HETATM 5513 O  O   . HOH   G 4 .   ? 13.529  -15.456 -28.193 1.00 25.49 ? 517 HOH   B O   1 
HETATM 5514 O  O   . HOH   G 4 .   ? 10.046  15.194  -40.806 1.00 46.89 ? 518 HOH   B O   1 
HETATM 5515 O  O   . HOH   G 4 .   ? -1.196  -2.138  -38.308 1.00 21.68 ? 519 HOH   B O   1 
HETATM 5516 O  O   . HOH   G 4 .   ? 9.899   -11.224 -35.186 1.00 27.46 ? 520 HOH   B O   1 
HETATM 5517 O  O   . HOH   G 4 .   ? 34.912  2.538   -25.405 1.00 26.33 ? 521 HOH   B O   1 
HETATM 5518 O  O   . HOH   G 4 .   ? 20.055  -2.320  -38.446 1.00 25.75 ? 522 HOH   B O   1 
HETATM 5519 O  O   . HOH   G 4 .   ? 17.707  1.638   -25.046 1.00 14.75 ? 523 HOH   B O   1 
HETATM 5520 O  O   . HOH   G 4 .   ? -3.771  -11.756 -21.634 1.00 28.36 ? 524 HOH   B O   1 
HETATM 5521 O  O   . HOH   G 4 .   ? 5.967   -16.201 -30.931 1.00 31.09 ? 525 HOH   B O   1 
HETATM 5522 O  O   . HOH   G 4 .   ? 30.836  -2.984  -33.138 1.00 25.68 ? 526 HOH   B O   1 
HETATM 5523 O  O   . HOH   G 4 .   ? 12.441  -9.470  -6.515  1.00 34.87 ? 527 HOH   B O   1 
HETATM 5524 O  O   . HOH   G 4 .   ? -4.047  -12.559 -8.863  1.00 32.71 ? 528 HOH   B O   1 
HETATM 5525 O  O   . HOH   G 4 .   ? -3.886  3.266   -27.390 1.00 26.75 ? 529 HOH   B O   1 
HETATM 5526 O  O   . HOH   G 4 .   ? 25.362  -8.536  -14.191 1.00 28.12 ? 530 HOH   B O   1 
HETATM 5527 O  O   . HOH   G 4 .   ? -8.375  -9.321  -12.307 1.00 28.62 ? 531 HOH   B O   1 
HETATM 5528 O  O   . HOH   G 4 .   ? 19.683  -0.852  -14.343 1.00 16.88 ? 532 HOH   B O   1 
HETATM 5529 O  O   . HOH   G 4 .   ? 7.444   4.882   -22.177 1.00 25.12 ? 533 HOH   B O   1 
HETATM 5530 O  O   . HOH   G 4 .   ? 11.074  -22.530 -22.711 1.00 34.66 ? 534 HOH   B O   1 
HETATM 5531 O  O   . HOH   G 4 .   ? 3.468   -6.134  -41.843 1.00 24.33 ? 535 HOH   B O   1 
HETATM 5532 O  O   . HOH   G 4 .   ? 14.341  -11.180 -14.752 1.00 18.66 ? 536 HOH   B O   1 
HETATM 5533 O  O   . HOH   G 4 .   ? 18.774  5.345   -24.005 1.00 15.01 ? 537 HOH   B O   1 
HETATM 5534 O  O   . HOH   G 4 .   ? -3.124  -1.651  -5.060  1.00 31.07 ? 538 HOH   B O   1 
HETATM 5535 O  O   . HOH   G 4 .   ? -0.177  6.789   -1.976  1.00 29.48 ? 539 HOH   B O   1 
HETATM 5536 O  O   . HOH   G 4 .   ? 6.230   1.025   -1.841  1.00 26.80 ? 540 HOH   B O   1 
HETATM 5537 O  O   . HOH   G 4 .   ? 26.519  -15.290 -20.741 1.00 32.95 ? 541 HOH   B O   1 
HETATM 5538 O  O   . HOH   G 4 .   ? 8.835   2.056   -2.340  1.00 30.64 ? 542 HOH   B O   1 
HETATM 5539 O  O   . HOH   G 4 .   ? 19.606  -4.138  -45.489 1.00 30.22 ? 543 HOH   B O   1 
HETATM 5540 O  O   . HOH   G 4 .   ? 10.990  4.559   -26.490 1.00 13.16 ? 544 HOH   B O   1 
HETATM 5541 O  O   . HOH   G 4 .   ? 7.899   -1.314  -41.946 1.00 16.91 ? 545 HOH   B O   1 
HETATM 5542 O  O   . HOH   G 4 .   ? 15.269  25.779  -14.881 1.00 46.51 ? 546 HOH   B O   1 
HETATM 5543 O  O   . HOH   G 4 .   ? 15.763  -1.088  -22.555 1.00 12.67 ? 547 HOH   B O   1 
HETATM 5544 O  O   . HOH   G 4 .   ? 22.527  14.477  -22.344 1.00 22.62 ? 548 HOH   B O   1 
HETATM 5545 O  O   . HOH   G 4 .   ? 1.891   5.646   -41.465 1.00 24.78 ? 549 HOH   B O   1 
HETATM 5546 O  O   . HOH   G 4 .   ? 15.703  -2.212  0.099   1.00 23.80 ? 550 HOH   B O   1 
HETATM 5547 O  O   . HOH   G 4 .   ? 17.679  5.907   -46.897 1.00 20.82 ? 551 HOH   B O   1 
HETATM 5548 O  O   . HOH   G 4 .   ? -3.732  14.426  -7.707  1.00 41.86 ? 552 HOH   B O   1 
HETATM 5549 O  O   . HOH   G 4 .   ? 15.037  8.948   -29.908 1.00 17.25 ? 553 HOH   B O   1 
HETATM 5550 O  O   . HOH   G 4 .   ? 14.334  11.473  -8.965  1.00 20.60 ? 554 HOH   B O   1 
HETATM 5551 O  O   . HOH   G 4 .   ? 23.375  11.037  -37.869 1.00 23.96 ? 555 HOH   B O   1 
HETATM 5552 O  O   . HOH   G 4 .   ? 19.914  9.839   -3.467  1.00 24.84 ? 556 HOH   B O   1 
HETATM 5553 O  O   . HOH   G 4 .   ? 7.760   10.685  -26.961 1.00 21.68 ? 557 HOH   B O   1 
HETATM 5554 O  O   . HOH   G 4 .   ? 27.801  -12.316 -21.290 1.00 27.95 ? 558 HOH   B O   1 
HETATM 5555 O  O   . HOH   G 4 .   ? 26.063  17.755  -18.323 1.00 31.69 ? 559 HOH   B O   1 
HETATM 5556 O  O   . HOH   G 4 .   ? 15.663  -7.856  -5.404  1.00 27.97 ? 560 HOH   B O   1 
HETATM 5557 O  O   . HOH   G 4 .   ? -0.611  12.242  -7.101  1.00 30.80 ? 561 HOH   B O   1 
HETATM 5558 O  O   . HOH   G 4 .   ? 27.255  -4.764  -19.943 1.00 24.01 ? 562 HOH   B O   1 
HETATM 5559 O  O   . HOH   G 4 .   ? 17.273  7.293   -8.352  1.00 19.85 ? 563 HOH   B O   1 
HETATM 5560 O  O   . HOH   G 4 .   ? 30.125  14.497  -16.487 1.00 32.67 ? 564 HOH   B O   1 
HETATM 5561 O  O   . HOH   G 4 .   ? 6.310   9.961   -29.454 1.00 22.38 ? 565 HOH   B O   1 
HETATM 5562 O  O   . HOH   G 4 .   ? 16.749  5.062   -21.437 1.00 21.82 ? 566 HOH   B O   1 
HETATM 5563 O  O   . HOH   G 4 .   ? 1.312   -13.111 -16.148 1.00 28.18 ? 567 HOH   B O   1 
HETATM 5564 O  O   . HOH   G 4 .   ? 16.272  13.676  -9.227  1.00 25.45 ? 568 HOH   B O   1 
HETATM 5565 O  O   . HOH   G 4 .   ? 28.181  18.433  -34.535 1.00 35.53 ? 569 HOH   B O   1 
HETATM 5566 O  O   . HOH   G 4 .   ? 14.732  2.728   -0.287  1.00 28.80 ? 570 HOH   B O   1 
HETATM 5567 O  O   . HOH   G 4 .   ? 8.845   12.415  0.351   1.00 36.06 ? 571 HOH   B O   1 
HETATM 5568 O  O   . HOH   G 4 .   ? -3.835  22.886  -23.074 1.00 43.00 ? 572 HOH   B O   1 
HETATM 5569 O  O   . HOH   G 4 .   ? 27.354  -3.191  -32.795 1.00 17.93 ? 573 HOH   B O   1 
HETATM 5570 O  O   . HOH   G 4 .   ? 33.978  5.981   -18.488 1.00 18.56 ? 574 HOH   B O   1 
HETATM 5571 O  O   . HOH   G 4 .   ? -3.738  -8.425  -18.360 1.00 26.26 ? 575 HOH   B O   1 
HETATM 5572 O  O   . HOH   G 4 .   ? 28.795  4.811   -14.589 1.00 18.93 ? 576 HOH   B O   1 
HETATM 5573 O  O   . HOH   G 4 .   ? 15.809  4.464   -24.760 1.00 21.06 ? 577 HOH   B O   1 
HETATM 5574 O  O   . HOH   G 4 .   ? 12.188  2.154   -25.373 1.00 20.52 ? 578 HOH   B O   1 
HETATM 5575 O  O   . HOH   G 4 .   ? 6.234   -14.245 -23.412 1.00 20.77 ? 579 HOH   B O   1 
HETATM 5576 O  O   . HOH   G 4 .   ? 17.434  1.030   -44.848 1.00 21.71 ? 580 HOH   B O   1 
HETATM 5577 O  O   . HOH   G 4 .   ? 17.609  6.062   -19.175 1.00 19.15 ? 581 HOH   B O   1 
HETATM 5578 O  O   . HOH   G 4 .   ? 28.479  12.136  -12.337 1.00 31.30 ? 582 HOH   B O   1 
HETATM 5579 O  O   . HOH   G 4 .   ? 27.669  11.585  -35.182 1.00 26.54 ? 583 HOH   B O   1 
HETATM 5580 O  O   . HOH   G 4 .   ? 15.507  3.605   -17.277 1.00 21.42 ? 584 HOH   B O   1 
HETATM 5581 O  O   . HOH   G 4 .   ? 19.053  19.050  -38.569 1.00 36.50 ? 585 HOH   B O   1 
HETATM 5582 O  O   . HOH   G 4 .   ? 7.930   -3.478  -24.870 1.00 21.94 ? 586 HOH   B O   1 
HETATM 5583 O  O   . HOH   G 4 .   ? 9.566   -0.712  -9.758  1.00 23.17 ? 587 HOH   B O   1 
HETATM 5584 O  O   . HOH   G 4 .   ? 6.447   -13.540 -27.696 1.00 26.46 ? 588 HOH   B O   1 
HETATM 5585 O  O   . HOH   G 4 .   ? 6.514   2.608   -26.774 1.00 22.18 ? 589 HOH   B O   1 
HETATM 5586 O  O   . HOH   G 4 .   ? 18.820  -15.520 -10.781 1.00 28.58 ? 590 HOH   B O   1 
HETATM 5587 O  O   . HOH   G 4 .   ? 31.141  -20.110 -21.696 1.00 30.01 ? 591 HOH   B O   1 
HETATM 5588 O  O   . HOH   G 4 .   ? 6.732   -13.435 -11.231 1.00 29.54 ? 592 HOH   B O   1 
HETATM 5589 O  O   . HOH   G 4 .   ? 10.046  -11.327 -17.104 1.00 20.08 ? 593 HOH   B O   1 
HETATM 5590 O  O   . HOH   G 4 .   ? -2.511  10.366  -22.909 1.00 32.13 ? 594 HOH   B O   1 
HETATM 5591 O  O   . HOH   G 4 .   ? 14.613  -13.770 -33.348 1.00 28.01 ? 595 HOH   B O   1 
HETATM 5592 O  O   . HOH   G 4 .   ? 24.208  -13.065 -29.208 1.00 28.11 ? 596 HOH   B O   1 
HETATM 5593 O  O   . HOH   G 4 .   ? -1.771  2.184   -3.324  1.00 29.61 ? 597 HOH   B O   1 
HETATM 5594 O  O   . HOH   G 4 .   ? 9.168   -4.334  -47.042 1.00 37.21 ? 598 HOH   B O   1 
HETATM 5595 O  O   . HOH   G 4 .   ? 5.586   -7.911  -7.113  1.00 23.80 ? 599 HOH   B O   1 
HETATM 5596 O  O   . HOH   G 4 .   ? 7.725   -8.536  -19.769 1.00 14.29 ? 600 HOH   B O   1 
HETATM 5597 O  O   . HOH   G 4 .   ? 15.402  -11.449 -17.371 1.00 18.65 ? 601 HOH   B O   1 
HETATM 5598 O  O   . HOH   G 4 .   ? 19.841  3.738   -45.619 1.00 22.03 ? 602 HOH   B O   1 
HETATM 5599 O  O   . HOH   G 4 .   ? -10.897 0.325   -13.045 1.00 21.35 ? 603 HOH   B O   1 
HETATM 5600 O  O   . HOH   G 4 .   ? 13.771  -0.186  -18.492 1.00 11.31 ? 604 HOH   B O   1 
HETATM 5601 O  O   . HOH   G 4 .   ? 16.230  11.161  -41.001 1.00 24.77 ? 605 HOH   B O   1 
HETATM 5602 O  O   . HOH   G 4 .   ? 14.218  12.875  -22.469 1.00 22.85 ? 606 HOH   B O   1 
HETATM 5603 O  O   . HOH   G 4 .   ? 15.214  4.392   -13.533 1.00 13.25 ? 607 HOH   B O   1 
HETATM 5604 O  O   . HOH   G 4 .   ? 3.614   -3.791  -7.367  1.00 21.82 ? 608 HOH   B O   1 
HETATM 5605 O  O   . HOH   G 4 .   ? 15.646  6.421   1.006   1.00 23.38 ? 609 HOH   B O   1 
HETATM 5606 O  O   . HOH   G 4 .   ? 19.961  -4.239  -48.364 1.00 29.12 ? 610 HOH   B O   1 
HETATM 5607 O  O   . HOH   G 4 .   ? 12.349  3.076   2.014   1.00 24.32 ? 611 HOH   B O   1 
HETATM 5608 O  O   . HOH   G 4 .   ? 13.904  7.242   -24.054 1.00 20.46 ? 612 HOH   B O   1 
HETATM 5609 O  O   . HOH   G 4 .   ? 29.880  11.793  -14.578 1.00 25.29 ? 613 HOH   B O   1 
HETATM 5610 O  O   . HOH   G 4 .   ? 18.100  17.625  -39.972 1.00 34.58 ? 614 HOH   B O   1 
HETATM 5611 O  O   . HOH   G 4 .   ? 23.797  -0.270  -7.019  1.00 25.51 ? 615 HOH   B O   1 
HETATM 5612 O  O   . HOH   G 4 .   ? 9.445   -16.546 -26.650 1.00 25.90 ? 616 HOH   B O   1 
HETATM 5613 O  O   . HOH   G 4 .   ? 15.952  8.543   -48.601 1.00 33.60 ? 617 HOH   B O   1 
HETATM 5614 O  O   . HOH   G 4 .   ? 15.665  -11.840 -32.903 1.00 26.49 ? 618 HOH   B O   1 
HETATM 5615 O  O   . HOH   G 4 .   ? -8.302  -3.925  -33.387 1.00 37.39 ? 619 HOH   B O   1 
HETATM 5616 O  O   . HOH   G 4 .   ? 28.798  18.458  -31.804 1.00 31.19 ? 620 HOH   B O   1 
HETATM 5617 O  O   . HOH   G 4 .   ? 4.197   27.297  -27.004 1.00 42.14 ? 621 HOH   B O   1 
HETATM 5618 O  O   . HOH   G 4 .   ? 1.316   -13.722 -8.464  1.00 29.23 ? 622 HOH   B O   1 
HETATM 5619 O  O   . HOH   G 4 .   ? 11.688  -17.976 -19.091 1.00 28.61 ? 623 HOH   B O   1 
HETATM 5620 O  O   . HOH   G 4 .   ? 11.698  1.395   -0.950  1.00 25.92 ? 624 HOH   B O   1 
HETATM 5621 O  O   . HOH   G 4 .   ? 2.716   8.586   -33.900 1.00 29.66 ? 625 HOH   B O   1 
HETATM 5622 O  O   . HOH   G 4 .   ? 4.694   7.299   -22.304 1.00 25.10 ? 626 HOH   B O   1 
HETATM 5623 O  O   . HOH   G 4 .   ? 10.636  4.408   -19.846 1.00 23.67 ? 627 HOH   B O   1 
HETATM 5624 O  O   . HOH   G 4 .   ? 31.710  -0.341  -33.284 1.00 25.48 ? 628 HOH   B O   1 
HETATM 5625 O  O   . HOH   G 4 .   ? 13.707  5.165   -26.280 1.00 20.21 ? 629 HOH   B O   1 
HETATM 5626 O  O   . HOH   G 4 .   ? 0.631   24.311  -30.965 1.00 43.05 ? 630 HOH   B O   1 
HETATM 5627 O  O   . HOH   G 4 .   ? -3.836  -5.818  -37.844 1.00 26.47 ? 631 HOH   B O   1 
HETATM 5628 O  O   . HOH   G 4 .   ? 8.088   -14.299 -25.854 1.00 20.11 ? 632 HOH   B O   1 
HETATM 5629 O  O   . HOH   G 4 .   ? 21.042  -19.867 -19.775 1.00 30.09 ? 633 HOH   B O   1 
HETATM 5630 O  O   . HOH   G 4 .   ? 26.828  -12.773 -29.260 1.00 29.14 ? 634 HOH   B O   1 
HETATM 5631 O  O   . HOH   G 4 .   ? 25.589  -3.968  -36.986 1.00 19.62 ? 635 HOH   B O   1 
HETATM 5632 O  O   . HOH   G 4 .   ? 15.376  -17.111 -8.620  1.00 38.42 ? 636 HOH   B O   1 
HETATM 5633 O  O   . HOH   G 4 .   ? 6.192   4.814   -28.168 1.00 16.29 ? 637 HOH   B O   1 
HETATM 5634 O  O   . HOH   G 4 .   ? 9.933   1.704   -23.635 1.00 15.99 ? 638 HOH   B O   1 
HETATM 5635 O  O   . HOH   G 4 .   ? 27.797  -8.340  -19.459 1.00 24.81 ? 639 HOH   B O   1 
HETATM 5636 O  O   . HOH   G 4 .   ? -1.930  -8.745  -5.367  1.00 27.24 ? 640 HOH   B O   1 
HETATM 5637 O  O   . HOH   G 4 .   ? -3.588  -14.477 -25.677 1.00 27.03 ? 641 HOH   B O   1 
HETATM 5638 O  O   . HOH   G 4 .   ? -7.437  -6.013  -22.122 1.00 30.11 ? 642 HOH   B O   1 
HETATM 5639 O  O   . HOH   G 4 .   ? 35.933  9.338   -22.362 1.00 29.59 ? 643 HOH   B O   1 
HETATM 5640 O  O   . HOH   G 4 .   ? 16.438  4.147   -2.477  1.00 23.63 ? 644 HOH   B O   1 
HETATM 5641 O  O   . HOH   G 4 .   ? -1.260  2.711   -29.493 1.00 28.71 ? 645 HOH   B O   1 
HETATM 5642 O  O   . HOH   G 4 .   ? 28.930  14.070  -20.590 1.00 24.87 ? 646 HOH   B O   1 
HETATM 5643 O  O   . HOH   G 4 .   ? 11.877  7.672   -22.624 1.00 27.05 ? 647 HOH   B O   1 
HETATM 5644 O  O   . HOH   G 4 .   ? -5.267  3.415   -29.819 1.00 28.23 ? 648 HOH   B O   1 
HETATM 5645 O  O   . HOH   G 4 .   ? 0.265   8.161   -42.538 1.00 30.87 ? 649 HOH   B O   1 
HETATM 5646 O  O   . HOH   G 4 .   ? 7.593   22.494  -27.800 1.00 38.42 ? 650 HOH   B O   1 
HETATM 5647 O  O   . HOH   G 4 .   ? 10.824  -6.668  -44.334 1.00 28.01 ? 651 HOH   B O   1 
HETATM 5648 O  O   . HOH   G 4 .   ? 22.478  -1.902  -14.885 1.00 26.34 ? 652 HOH   B O   1 
HETATM 5649 O  O   . HOH   G 4 .   ? 23.923  -1.693  -43.411 1.00 26.75 ? 653 HOH   B O   1 
HETATM 5650 O  O   . HOH   G 4 .   ? 22.416  6.708   -3.418  1.00 33.36 ? 654 HOH   B O   1 
HETATM 5651 O  O   . HOH   G 4 .   ? 24.969  -18.726 -19.781 1.00 28.62 ? 655 HOH   B O   1 
HETATM 5652 O  O   . HOH   G 4 .   ? 23.022  -6.176  -7.813  1.00 30.17 ? 656 HOH   B O   1 
HETATM 5653 O  O   . HOH   G 4 .   ? 3.947   3.543   -26.106 1.00 19.35 ? 657 HOH   B O   1 
HETATM 5654 O  O   . HOH   G 4 .   ? -8.453  2.002   -23.514 1.00 24.77 ? 658 HOH   B O   1 
HETATM 5655 O  O   . HOH   G 4 .   ? 14.689  2.088   -24.244 1.00 22.43 ? 659 HOH   B O   1 
HETATM 5656 O  O   . HOH   G 4 .   ? 5.380   21.199  -26.980 1.00 33.73 ? 660 HOH   B O   1 
HETATM 5657 O  O   . HOH   G 4 .   ? -13.823 -4.654  -18.457 1.00 30.46 ? 661 HOH   B O   1 
HETATM 5658 O  O   . HOH   G 4 .   ? 4.171   -14.569 -24.111 1.00 28.66 ? 662 HOH   B O   1 
HETATM 5659 O  O   . HOH   G 4 .   ? 16.590  1.508   -18.838 1.00 14.56 ? 663 HOH   B O   1 
HETATM 5660 O  O   . HOH   G 4 .   ? 20.708  7.957   -45.311 1.00 22.92 ? 664 HOH   B O   1 
HETATM 5661 O  O   . HOH   G 4 .   ? 32.670  12.381  -11.796 1.00 42.95 ? 665 HOH   B O   1 
HETATM 5662 O  O   . HOH   G 4 .   ? 22.825  0.604   -11.034 1.00 26.47 ? 666 HOH   B O   1 
HETATM 5663 O  O   . HOH   G 4 .   ? 11.011  -1.865  -5.274  1.00 24.74 ? 667 HOH   B O   1 
HETATM 5664 O  O   . HOH   G 4 .   ? 18.709  17.696  -6.909  1.00 36.78 ? 668 HOH   B O   1 
HETATM 5665 O  O   . HOH   G 4 .   ? 34.455  5.460   -24.118 1.00 24.66 ? 669 HOH   B O   1 
HETATM 5666 O  O   . HOH   G 4 .   ? 12.280  6.642   -20.060 1.00 19.95 ? 670 HOH   B O   1 
HETATM 5667 O  O   . HOH   G 4 .   ? 10.927  -5.695  -4.593  1.00 31.85 ? 671 HOH   B O   1 
HETATM 5668 O  O   . HOH   G 4 .   ? 11.791  24.030  -8.457  1.00 40.25 ? 672 HOH   B O   1 
HETATM 5669 O  O   . HOH   G 4 .   ? 14.725  17.072  -1.417  1.00 38.46 ? 673 HOH   B O   1 
HETATM 5670 O  O   . HOH   G 4 .   ? 31.818  -2.714  -15.002 1.00 24.98 ? 674 HOH   B O   1 
HETATM 5671 O  O   . HOH   G 4 .   ? 28.309  -8.167  -15.758 1.00 31.21 ? 675 HOH   B O   1 
HETATM 5672 O  O   . HOH   G 4 .   ? 25.523  3.587   -37.988 1.00 23.21 ? 676 HOH   B O   1 
HETATM 5673 O  O   . HOH   G 4 .   ? 17.270  -2.609  -39.052 1.00 21.80 ? 677 HOH   B O   1 
HETATM 5674 O  O   . HOH   G 4 .   ? 6.013   9.225   -22.641 1.00 24.54 ? 678 HOH   B O   1 
HETATM 5675 O  O   . HOH   G 4 .   ? 18.049  18.984  -35.202 1.00 29.07 ? 679 HOH   B O   1 
HETATM 5676 O  O   . HOH   G 4 .   ? 8.319   13.307  -41.611 1.00 35.84 ? 680 HOH   B O   1 
HETATM 5677 O  O   . HOH   G 4 .   ? 10.103  -12.865 -37.145 1.00 29.70 ? 681 HOH   B O   1 
HETATM 5678 O  O   . HOH   G 4 .   ? 8.985   3.755   -25.113 1.00 22.92 ? 682 HOH   B O   1 
HETATM 5679 O  O   . HOH   G 4 .   ? 10.163  -7.715  -5.902  1.00 26.86 ? 683 HOH   B O   1 
HETATM 5680 O  O   . HOH   G 4 .   ? 5.554   3.664   -24.205 1.00 24.25 ? 684 HOH   B O   1 
HETATM 5681 O  O   . HOH   G 4 .   ? 19.604  2.837   -48.124 1.00 29.05 ? 685 HOH   B O   1 
HETATM 5682 O  O   . HOH   G 4 .   ? -1.919  -15.138 -18.595 1.00 28.12 ? 686 HOH   B O   1 
HETATM 5683 O  O   . HOH   G 4 .   ? -0.367  11.940  -21.512 1.00 28.21 ? 687 HOH   B O   1 
HETATM 5684 O  O   . HOH   G 4 .   ? 18.337  -1.109  -51.241 1.00 38.66 ? 688 HOH   B O   1 
HETATM 5685 O  O   . HOH   G 4 .   ? 0.946   15.761  1.983   1.00 40.64 ? 689 HOH   B O   1 
HETATM 5686 O  O   . HOH   G 4 .   ? 12.996  13.543  -40.204 1.00 36.00 ? 690 HOH   B O   1 
HETATM 5687 O  O   . HOH   G 4 .   ? 14.471  4.888   -19.880 1.00 21.55 ? 691 HOH   B O   1 
HETATM 5688 O  O   . HOH   G 4 .   ? 30.894  -6.311  -25.436 1.00 32.87 ? 692 HOH   B O   1 
HETATM 5689 O  O   . HOH   G 4 .   ? 30.003  14.813  -24.819 1.00 30.27 ? 693 HOH   B O   1 
HETATM 5690 O  O   . HOH   G 4 .   ? 13.497  2.158   -20.767 1.00 24.03 ? 694 HOH   B O   1 
HETATM 5691 O  O   . HOH   G 4 .   ? 8.408   -16.799 -29.941 1.00 34.24 ? 695 HOH   B O   1 
HETATM 5692 O  O   . HOH   G 4 .   ? -1.248  -17.311 -20.628 1.00 31.62 ? 696 HOH   B O   1 
HETATM 5693 O  O   . HOH   G 4 .   ? -1.893  18.002  -28.227 1.00 48.67 ? 697 HOH   B O   1 
HETATM 5694 O  O   . HOH   G 4 .   ? -3.246  0.670   -4.438  1.00 36.70 ? 698 HOH   B O   1 
HETATM 5695 O  O   . HOH   G 4 .   ? 7.580   17.072  -0.343  1.00 38.80 ? 699 HOH   B O   1 
HETATM 5696 O  O   . HOH   G 4 .   ? 29.759  -8.108  -24.461 1.00 31.33 ? 700 HOH   B O   1 
HETATM 5697 O  O   . HOH   G 4 .   ? 16.836  13.233  -42.458 1.00 27.50 ? 701 HOH   B O   1 
HETATM 5698 O  O   . HOH   G 4 .   ? 33.645  14.981  -9.931  1.00 53.93 ? 702 HOH   B O   1 
HETATM 5699 O  O   . HOH   G 4 .   ? 32.962  21.826  -29.070 1.00 29.49 ? 703 HOH   B O   1 
HETATM 5700 O  O   . HOH   G 4 .   ? 17.759  -5.350  -39.862 1.00 27.67 ? 704 HOH   B O   1 
HETATM 5701 O  O   . HOH   G 4 .   ? 17.105  1.390   -21.140 1.00 20.30 ? 705 HOH   B O   1 
HETATM 5702 O  O   . HOH   G 4 .   ? 13.744  27.431  -14.883 1.00 50.95 ? 706 HOH   B O   1 
HETATM 5703 O  O   . HOH   G 4 .   ? 27.997  -16.109 -5.138  1.00 46.86 ? 707 HOH   B O   1 
HETATM 5704 O  O   . HOH   G 4 .   ? 9.337   -13.396 -10.802 1.00 30.35 ? 708 HOH   B O   1 
HETATM 5705 O  O   . HOH   G 4 .   ? 17.444  5.969   -1.312  1.00 23.88 ? 709 HOH   B O   1 
HETATM 5706 O  O   . HOH   G 4 .   ? 28.412  -12.384 -30.945 1.00 35.39 ? 710 HOH   B O   1 
HETATM 5707 O  O   . HOH   G 4 .   ? 7.865   23.254  -15.734 1.00 36.98 ? 711 HOH   B O   1 
HETATM 5708 O  O   . HOH   G 4 .   ? 12.426  -20.399 -19.345 1.00 34.99 ? 712 HOH   B O   1 
HETATM 5709 O  O   . HOH   G 4 .   ? 12.994  24.493  -27.227 1.00 34.69 ? 713 HOH   B O   1 
HETATM 5710 O  O   . HOH   G 4 .   ? 7.646   25.511  -16.039 1.00 42.98 ? 714 HOH   B O   1 
HETATM 5711 O  O   . HOH   G 4 .   ? 17.876  1.220   -50.657 1.00 35.08 ? 715 HOH   B O   1 
HETATM 5712 O  O   . HOH   G 4 .   ? 36.330  5.474   -22.338 1.00 29.80 ? 716 HOH   B O   1 
HETATM 5713 O  O   . HOH   G 4 .   ? 26.226  11.705  -37.533 1.00 29.58 ? 717 HOH   B O   1 
HETATM 5714 O  O   . HOH   G 4 .   ? 4.122   -0.810  -45.410 1.00 28.27 ? 718 HOH   B O   1 
HETATM 5715 O  O   . HOH   G 4 .   ? -7.520  4.183   -24.065 1.00 28.07 ? 719 HOH   B O   1 
HETATM 5716 O  O   . HOH   G 4 .   ? 18.269  2.680   -22.713 1.00 13.46 ? 720 HOH   B O   1 
HETATM 5717 O  O   . HOH   G 4 .   ? 6.630   7.729   -50.339 1.00 20.80 ? 721 HOH   B O   1 
HETATM 5718 O  O   . HOH   G 4 .   ? -1.070  -10.786 -5.158  1.00 33.73 ? 722 HOH   B O   1 
HETATM 5719 O  O   . HOH   G 4 .   ? -6.190  -12.446 -19.684 1.00 38.61 ? 723 HOH   B O   1 
HETATM 5720 O  O   . HOH   G 4 .   ? -0.607  -15.094 -16.496 1.00 30.49 ? 724 HOH   B O   1 
HETATM 5721 O  O   . HOH   G 4 .   ? 9.091   11.714  -49.285 1.00 40.29 ? 725 HOH   B O   1 
HETATM 5722 O  O   . HOH   G 4 .   ? -2.688  19.062  -5.456  1.00 33.78 ? 726 HOH   B O   1 
HETATM 5723 O  O   . HOH   G 4 .   ? 3.560   10.971  -31.358 1.00 40.11 ? 727 HOH   B O   1 
HETATM 5724 O  O   . HOH   G 4 .   ? 9.926   -23.520 -24.605 1.00 36.83 ? 728 HOH   B O   1 
HETATM 5725 O  O   . HOH   G 4 .   ? 29.418  -3.782  -34.717 1.00 27.99 ? 729 HOH   B O   1 
HETATM 5726 O  O   . HOH   G 4 .   ? 24.876  -8.754  -34.070 1.00 33.20 ? 730 HOH   B O   1 
HETATM 5727 O  O   . HOH   G 4 .   ? 20.172  5.117   -2.846  1.00 29.60 ? 731 HOH   B O   1 
HETATM 5728 O  O   . HOH   G 4 .   ? 3.502   6.569   -24.808 1.00 27.64 ? 732 HOH   B O   1 
HETATM 5729 O  O   . HOH   G 4 .   ? -1.844  -18.901 -31.002 1.00 33.70 ? 733 HOH   B O   1 
HETATM 5730 O  O   . HOH   G 4 .   ? 10.631  -3.416  -2.821  1.00 29.14 ? 734 HOH   B O   1 
HETATM 5731 O  O   . HOH   G 4 .   ? 33.108  14.059  -2.851  1.00 37.05 ? 735 HOH   B O   1 
HETATM 5732 O  O   . HOH   G 4 .   ? -0.536  10.050  -34.669 1.00 32.47 ? 736 HOH   B O   1 
HETATM 5733 O  O   . HOH   G 4 .   ? 5.780   27.708  -28.533 1.00 41.27 ? 737 HOH   B O   1 
HETATM 5734 O  O   . HOH   G 4 .   ? 33.110  11.779  -3.009  1.00 39.21 ? 738 HOH   B O   1 
HETATM 5735 O  O   . HOH   G 4 .   ? 1.206   10.341  -33.074 1.00 33.37 ? 739 HOH   B O   1 
HETATM 5736 O  O   . HOH   G 4 .   ? 33.177  14.577  -12.054 1.00 47.66 ? 740 HOH   B O   1 
HETATM 5737 O  O   . HOH   G 4 .   ? 35.117  7.627   -25.347 1.00 31.45 ? 741 HOH   B O   1 
HETATM 5738 O  O   . HOH   G 4 .   ? 23.968  1.743   0.146   1.00 41.37 ? 742 HOH   B O   1 
HETATM 5739 O  O   . HOH   G 4 .   ? 24.973  6.976   -1.828  1.00 41.46 ? 743 HOH   B O   1 
HETATM 5740 O  O   . HOH   G 4 .   ? -3.910  13.325  -4.662  1.00 40.06 ? 744 HOH   B O   1 
HETATM 5741 O  O   . HOH   G 4 .   ? 24.652  -0.759  1.176   1.00 43.71 ? 745 HOH   B O   1 
HETATM 5742 O  O   . HOH   G 4 .   ? 4.822   30.775  -23.948 1.00 39.66 ? 746 HOH   B O   1 
HETATM 5743 O  O   . HOH   G 4 .   ? 7.697   -23.894 -25.820 1.00 33.96 ? 747 HOH   B O   1 
HETATM 5744 O  O   . HOH   G 4 .   ? 30.628  -15.926 -3.241  1.00 40.93 ? 748 HOH   B O   1 
HETATM 5745 O  O   . HOH   G 4 .   ? 25.268  4.859   -0.512  1.00 40.57 ? 749 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   . LEU A 14  ? 0.6526 0.5988 0.6578 -0.0357 0.0102  -0.0840 26  LEU A N   
2    C CA  . LEU A 14  ? 0.7219 0.6726 0.7270 -0.0373 0.0116  -0.0829 26  LEU A CA  
3    C C   . LEU A 14  ? 0.7440 0.7006 0.7486 -0.0367 0.0135  -0.0819 26  LEU A C   
4    O O   . LEU A 14  ? 0.7299 0.6836 0.7327 -0.0345 0.0128  -0.0795 26  LEU A O   
5    C CB  . LEU A 14  ? 0.7576 0.7010 0.7615 -0.0382 0.0114  -0.0790 26  LEU A CB  
6    C CG  . LEU A 14  ? 0.7393 0.6775 0.7448 -0.0399 0.0105  -0.0806 26  LEU A CG  
7    C CD1 . LEU A 14  ? 0.7419 0.6723 0.7459 -0.0403 0.0105  -0.0765 26  LEU A CD1 
8    C CD2 . LEU A 14  ? 0.8225 0.7666 0.8303 -0.0423 0.0109  -0.0842 26  LEU A CD2 
9    N N   . ALA A 15  ? 0.7489 0.7140 0.7552 -0.0388 0.0157  -0.0837 27  ALA A N   
10   C CA  . ALA A 15  ? 0.6859 0.6574 0.6915 -0.0386 0.0174  -0.0833 27  ALA A CA  
11   C C   . ALA A 15  ? 0.6121 0.5767 0.6149 -0.0372 0.0173  -0.0777 27  ALA A C   
12   O O   . ALA A 15  ? 0.6768 0.6347 0.6786 -0.0373 0.0168  -0.0744 27  ALA A O   
13   C CB  . ALA A 15  ? 0.6856 0.6671 0.6928 -0.0413 0.0192  -0.0861 27  ALA A CB  
14   N N   . CYS A 16  ? 0.5650 0.5318 0.5668 -0.0360 0.0179  -0.0767 28  CYS A N   
15   C CA  . CYS A 16  ? 0.5266 0.4868 0.5259 -0.0341 0.0175  -0.0716 28  CYS A CA  
16   C C   . CYS A 16  ? 0.4910 0.4571 0.4898 -0.0345 0.0193  -0.0715 28  CYS A C   
17   O O   . CYS A 16  ? 0.4167 0.3889 0.4162 -0.0344 0.0198  -0.0742 28  CYS A O   
18   C CB  . CYS A 16  ? 0.5146 0.4679 0.5129 -0.0314 0.0151  -0.0700 28  CYS A CB  
19   S SG  . CYS A 16  ? 0.6816 0.6307 0.6777 -0.0287 0.0145  -0.0657 28  CYS A SG  
20   N N   . PRO A 17  ? 0.4338 0.3986 0.4313 -0.0351 0.0203  -0.0685 29  PRO A N   
21   C CA  . PRO A 17  ? 0.3919 0.3617 0.3884 -0.0356 0.0218  -0.0683 29  PRO A CA  
22   C C   . PRO A 17  ? 0.3904 0.3566 0.3859 -0.0333 0.0212  -0.0661 29  PRO A C   
23   O O   . PRO A 17  ? 0.3848 0.3428 0.3797 -0.0309 0.0193  -0.0630 29  PRO A O   
24   C CB  . PRO A 17  ? 0.4234 0.3904 0.4187 -0.0365 0.0226  -0.0652 29  PRO A CB  
25   C CG  . PRO A 17  ? 0.4243 0.3825 0.4194 -0.0351 0.0211  -0.0622 29  PRO A CG  
26   C CD  . PRO A 17  ? 0.4260 0.3849 0.4227 -0.0353 0.0200  -0.0653 29  PRO A CD  
27   N N   . ALA A 18  ? 0.3533 0.3261 0.3484 -0.0342 0.0226  -0.0679 30  ALA A N   
28   C CA  . ALA A 18  ? 0.3600 0.3305 0.3546 -0.0324 0.0223  -0.0663 30  ALA A CA  
29   C C   . ALA A 18  ? 0.3496 0.3118 0.3426 -0.0310 0.0219  -0.0609 30  ALA A C   
30   O O   . ALA A 18  ? 0.3362 0.2968 0.3282 -0.0318 0.0224  -0.0589 30  ALA A O   
31   C CB  . ALA A 18  ? 0.3857 0.3667 0.3798 -0.0341 0.0241  -0.0699 30  ALA A CB  
32   N N   . GLU A 19  ? 0.3221 0.2794 0.3151 -0.0286 0.0207  -0.0586 31  GLU A N   
33   C CA  . GLU A 19  ? 0.3371 0.2874 0.3288 -0.0268 0.0198  -0.0535 31  GLU A CA  
34   C C   . GLU A 19  ? 0.3104 0.2634 0.3011 -0.0287 0.0220  -0.0531 31  GLU A C   
35   O O   . GLU A 19  ? 0.3201 0.2811 0.3104 -0.0312 0.0240  -0.0570 31  GLU A O   
36   C CB  . GLU A 19  ? 0.3196 0.2661 0.3118 -0.0242 0.0180  -0.0518 31  GLU A CB  
37   C CG  . GLU A 19  ? 0.3688 0.3201 0.3617 -0.0252 0.0199  -0.0541 31  GLU A CG  
38   C CD  . GLU A 19  ? 0.4333 0.3920 0.4277 -0.0262 0.0208  -0.0596 31  GLU A CD  
39   O OE1 . GLU A 19  ? 0.4298 0.3907 0.4248 -0.0267 0.0203  -0.0620 31  GLU A OE1 
40   O OE2 . GLU A 19  ? 0.4303 0.3929 0.4256 -0.0264 0.0219  -0.0615 31  GLU A OE2 
41   N N   . ARG A 20  ? 0.2704 0.2174 0.2601 -0.0275 0.0213  -0.0485 32  ARG A N   
42   C CA  . ARG A 20  ? 0.2505 0.1984 0.2388 -0.0293 0.0232  -0.0476 32  ARG A CA  
43   C C   . ARG A 20  ? 0.2423 0.1824 0.2301 -0.0268 0.0216  -0.0418 32  ARG A C   
44   O O   . ARG A 20  ? 0.2703 0.2065 0.2585 -0.0242 0.0193  -0.0392 32  ARG A O   
45   C CB  . ARG A 20  ? 0.2806 0.2347 0.2679 -0.0325 0.0249  -0.0509 32  ARG A CB  
46   C CG  . ARG A 20  ? 0.2410 0.1917 0.2285 -0.0319 0.0241  -0.0490 32  ARG A CG  
47   C CD  . ARG A 20  ? 0.2794 0.2377 0.2669 -0.0350 0.0254  -0.0532 32  ARG A CD  
48   N NE  . ARG A 20  ? 0.3080 0.2719 0.2971 -0.0355 0.0251  -0.0573 32  ARG A NE  
49   C CZ  . ARG A 20  ? 0.2883 0.2620 0.2776 -0.0380 0.0260  -0.0620 32  ARG A CZ  
50   N NH1 . ARG A 20  ? 0.3047 0.2849 0.2927 -0.0401 0.0268  -0.0629 32  ARG A NH1 
51   N NH2 . ARG A 20  ? 0.3250 0.3028 0.3161 -0.0379 0.0255  -0.0652 32  ARG A NH2 
52   N N   . SER A 21  ? 0.2514 0.1900 0.2383 -0.0276 0.0228  -0.0399 33  SER A N   
53   C CA  . SER A 21  ? 0.2362 0.1690 0.2227 -0.0255 0.0215  -0.0347 33  SER A CA  
54   C C   . SER A 21  ? 0.2679 0.2054 0.2537 -0.0270 0.0225  -0.0330 33  SER A C   
55   O O   . SER A 21  ? 0.1804 0.1292 0.1665 -0.0279 0.0227  -0.0332 33  SER A O   
56   C CB  . SER A 21  ? 0.2370 0.1656 0.2245 -0.0226 0.0196  -0.0306 33  SER A CB  
57   O OG  . SER A 21  ? 0.2474 0.1758 0.2362 -0.0200 0.0170  -0.0305 33  SER A OG  
58   N N   . GLY A 22  ? 0.2530 0.1854 0.2383 -0.0257 0.0219  -0.0294 34  GLY A N   
59   C CA  . GLY A 22  ? 0.2396 0.1803 0.2255 -0.0251 0.0211  -0.0255 34  GLY A CA  
60   C C   . GLY A 22  ? 0.2017 0.1511 0.1874 -0.0270 0.0219  -0.0282 34  GLY A C   
61   O O   . GLY A 22  ? 0.1934 0.1511 0.1796 -0.0266 0.0212  -0.0253 34  GLY A O   
62   N N   . HIS A 23  ? 0.2101 0.1580 0.1954 -0.0290 0.0232  -0.0336 35  HIS A N   
63   C CA  . HIS A 23  ? 0.1992 0.1545 0.1849 -0.0310 0.0240  -0.0367 35  HIS A CA  
64   C C   . HIS A 23  ? 0.2451 0.1968 0.2308 -0.0305 0.0240  -0.0350 35  HIS A C   
65   O O   . HIS A 23  ? 0.2199 0.1632 0.2051 -0.0286 0.0235  -0.0317 35  HIS A O   
66   C CB  . HIS A 23  ? 0.2239 0.1772 0.2095 -0.0334 0.0252  -0.0430 35  HIS A CB  
67   C CG  . HIS A 23  ? 0.2583 0.2009 0.2438 -0.0318 0.0247  -0.0422 35  HIS A CG  
68   N ND1 . HIS A 23  ? 0.2565 0.1941 0.2422 -0.0286 0.0229  -0.0387 35  HIS A ND1 
69   C CD2 . HIS A 23  ? 0.2604 0.2012 0.2465 -0.0310 0.0241  -0.0414 35  HIS A CD2 
70   C CE1 . HIS A 23  ? 0.2726 0.2067 0.2589 -0.0260 0.0209  -0.0363 35  HIS A CE1 
71   N NE2 . HIS A 23  ? 0.2641 0.1997 0.2504 -0.0275 0.0217  -0.0377 35  HIS A NE2 
72   N N   . VAL A 24  ? 0.2156 0.1741 0.2020 -0.0323 0.0247  -0.0375 36  VAL A N   
73   C CA  . VAL A 24  ? 0.2135 0.1695 0.2002 -0.0324 0.0252  -0.0371 36  VAL A CA  
74   C C   . VAL A 24  ? 0.2304 0.1828 0.2171 -0.0353 0.0268  -0.0424 36  VAL A C   
75   O O   . VAL A 24  ? 0.2177 0.1736 0.2048 -0.0374 0.0272  -0.0466 36  VAL A O   
76   C CB  . VAL A 24  ? 0.2213 0.1881 0.2094 -0.0320 0.0244  -0.0352 36  VAL A CB  
77   C CG1 . VAL A 24  ? 0.2266 0.1952 0.2148 -0.0290 0.0225  -0.0293 36  VAL A CG1 
78   C CG2 . VAL A 24  ? 0.2250 0.2034 0.2139 -0.0343 0.0246  -0.0388 36  VAL A CG2 
79   N N   . ALA A 25  ? 0.2128 0.1584 0.1991 -0.0355 0.0277  -0.0421 37  ALA A N   
80   C CA  . ALA A 25  ? 0.2709 0.2162 0.2582 -0.0367 0.0282  -0.0440 37  ALA A CA  
81   C C   . ALA A 25  ? 0.2756 0.2199 0.2631 -0.0373 0.0293  -0.0434 37  ALA A C   
82   O O   . ALA A 25  ? 0.2647 0.2037 0.2512 -0.0349 0.0289  -0.0398 37  ALA A O   
83   C CB  . ALA A 25  ? 0.2855 0.2253 0.2723 -0.0336 0.0264  -0.0410 37  ALA A CB  
84   N N   . VAL A 26  ? 0.2787 0.2290 0.2679 -0.0406 0.0306  -0.0472 38  VAL A N   
85   C CA  . VAL A 26  ? 0.2589 0.2098 0.2490 -0.0419 0.0320  -0.0477 38  VAL A CA  
86   C C   . VAL A 26  ? 0.2892 0.2416 0.2808 -0.0437 0.0328  -0.0494 38  VAL A C   
87   O O   . VAL A 26  ? 0.3076 0.2626 0.3000 -0.0446 0.0322  -0.0514 38  VAL A O   
88   C CB  . VAL A 26  ? 0.3091 0.2726 0.3016 -0.0410 0.0311  -0.0465 38  VAL A CB  
89   C CG1 . VAL A 26  ? 0.2769 0.2415 0.2686 -0.0372 0.0291  -0.0419 38  VAL A CG1 
90   C CG2 . VAL A 26  ? 0.2910 0.2652 0.2855 -0.0435 0.0309  -0.0504 38  VAL A CG2 
91   N N   . SER A 27  ? 0.3419 0.2921 0.3337 -0.0443 0.0340  -0.0485 39  SER A N   
92   C CA  . SER A 27  ? 0.3244 0.2739 0.3170 -0.0457 0.0348  -0.0491 39  SER A CA  
93   C C   . SER A 27  ? 0.3313 0.2840 0.3257 -0.0486 0.0370  -0.0509 39  SER A C   
94   O O   . SER A 27  ? 0.3311 0.2834 0.3252 -0.0482 0.0379  -0.0502 39  SER A O   
95   C CB  . SER A 27  ? 0.3827 0.3240 0.3728 -0.0427 0.0335  -0.0450 39  SER A CB  
96   O OG  . SER A 27  ? 0.4087 0.3488 0.3994 -0.0443 0.0340  -0.0457 39  SER A OG  
97   N N   . ASP A 28  ? 0.3736 0.3295 0.3701 -0.0515 0.0380  -0.0535 40  ASP A N   
98   C CA  . ASP A 28  ? 0.4208 0.3793 0.4192 -0.0545 0.0402  -0.0550 40  ASP A CA  
99   C C   . ASP A 28  ? 0.4407 0.3920 0.4373 -0.0542 0.0411  -0.0524 40  ASP A C   
100  O O   . ASP A 28  ? 0.4262 0.3794 0.4245 -0.0572 0.0431  -0.0538 40  ASP A O   
101  C CB  . ASP A 28  ? 0.4398 0.4080 0.4424 -0.0583 0.0407  -0.0599 40  ASP A CB  
102  C CG  . ASP A 28  ? 0.4343 0.4022 0.4375 -0.0586 0.0395  -0.0610 40  ASP A CG  
103  O OD1 . ASP A 28  ? 0.4222 0.3822 0.4227 -0.0563 0.0385  -0.0581 40  ASP A OD1 
104  O OD2 . ASP A 28  ? 0.4969 0.4728 0.5033 -0.0612 0.0394  -0.0651 40  ASP A OD2 
105  N N   . GLY A 29  ? 0.3698 0.3137 0.3632 -0.0507 0.0393  -0.0487 41  GLY A N   
106  C CA  . GLY A 29  ? 0.4485 0.3861 0.4399 -0.0502 0.0393  -0.0463 41  GLY A CA  
107  C C   . GLY A 29  ? 0.4431 0.3795 0.4353 -0.0509 0.0379  -0.0471 41  GLY A C   
108  O O   . GLY A 29  ? 0.4694 0.4000 0.4597 -0.0497 0.0369  -0.0447 41  GLY A O   
109  N N   . ARG A 30  ? 0.4026 0.3446 0.3977 -0.0528 0.0377  -0.0506 42  ARG A N   
110  C CA  . ARG A 30  ? 0.4374 0.3785 0.4337 -0.0535 0.0362  -0.0519 42  ARG A CA  
111  C C   . ARG A 30  ? 0.4206 0.3648 0.4179 -0.0523 0.0343  -0.0538 42  ARG A C   
112  O O   . ARG A 30  ? 0.4486 0.3894 0.4455 -0.0507 0.0321  -0.0533 42  ARG A O   
113  C CB  . ARG A 30  ? 0.4860 0.4310 0.4854 -0.0578 0.0381  -0.0552 42  ARG A CB  
114  C CG  . ARG A 30  ? 0.4869 0.4284 0.4871 -0.0587 0.0368  -0.0557 42  ARG A CG  
115  C CD  . ARG A 30  ? 0.4619 0.4064 0.4649 -0.0630 0.0389  -0.0582 42  ARG A CD  
116  N NE  . ARG A 30  ? 0.5422 0.4965 0.5489 -0.0654 0.0400  -0.0623 42  ARG A NE  
117  C CZ  . ARG A 30  ? 0.5274 0.4872 0.5369 -0.0688 0.0423  -0.0645 42  ARG A CZ  
118  N NH1 . ARG A 30  ? 0.5634 0.5197 0.5722 -0.0706 0.0442  -0.0628 42  ARG A NH1 
119  N NH2 . ARG A 30  ? 0.5638 0.5333 0.5769 -0.0707 0.0425  -0.0685 42  ARG A NH2 
120  N N   . HIS A 31  ? 0.4227 0.3736 0.4212 -0.0529 0.0349  -0.0560 43  HIS A N   
121  C CA  . HIS A 31  ? 0.3876 0.3420 0.3866 -0.0518 0.0333  -0.0577 43  HIS A CA  
122  C C   . HIS A 31  ? 0.3643 0.3181 0.3612 -0.0493 0.0329  -0.0556 43  HIS A C   
123  O O   . HIS A 31  ? 0.3629 0.3175 0.3593 -0.0497 0.0342  -0.0547 43  HIS A O   
124  C CB  . HIS A 31  ? 0.3628 0.3268 0.3652 -0.0549 0.0340  -0.0627 43  HIS A CB  
125  C CG  . HIS A 31  ? 0.4451 0.4098 0.4500 -0.0573 0.0342  -0.0651 43  HIS A CG  
126  N ND1 . HIS A 31  ? 0.4759 0.4404 0.4820 -0.0598 0.0359  -0.0652 43  HIS A ND1 
127  C CD2 . HIS A 31  ? 0.4712 0.4365 0.4776 -0.0576 0.0328  -0.0674 43  HIS A CD2 
128  C CE1 . HIS A 31  ? 0.4925 0.4572 0.5009 -0.0617 0.0356  -0.0674 43  HIS A CE1 
129  N NE2 . HIS A 31  ? 0.4671 0.4322 0.4757 -0.0603 0.0336  -0.0688 43  HIS A NE2 
130  N N   . MET A 32  ? 0.3368 0.2890 0.3326 -0.0469 0.0310  -0.0547 44  MET A N   
131  C CA  . MET A 32  ? 0.3584 0.3093 0.3522 -0.0445 0.0304  -0.0526 44  MET A CA  
132  C C   . MET A 32  ? 0.3134 0.2715 0.3083 -0.0455 0.0301  -0.0560 44  MET A C   
133  O O   . MET A 32  ? 0.3535 0.3138 0.3495 -0.0457 0.0293  -0.0582 44  MET A O   
134  C CB  . MET A 32  ? 0.3212 0.2647 0.3130 -0.0408 0.0282  -0.0486 44  MET A CB  
135  C CG  . MET A 32  ? 0.3405 0.2815 0.3304 -0.0381 0.0275  -0.0455 44  MET A CG  
136  S SD  . MET A 32  ? 0.3532 0.2870 0.3415 -0.0338 0.0244  -0.0412 44  MET A SD  
137  C CE  . MET A 32  ? 0.3083 0.2446 0.2976 -0.0336 0.0231  -0.0438 44  MET A CE  
138  N N   . PHE A 33  ? 0.2945 0.2567 0.2890 -0.0461 0.0308  -0.0565 45  PHE A N   
139  C CA  . PHE A 33  ? 0.3066 0.2771 0.3015 -0.0473 0.0305  -0.0600 45  PHE A CA  
140  C C   . PHE A 33  ? 0.3008 0.2678 0.2934 -0.0449 0.0296  -0.0575 45  PHE A C   
141  O O   . PHE A 33  ? 0.2901 0.2517 0.2811 -0.0433 0.0297  -0.0541 45  PHE A O   
142  C CB  . PHE A 33  ? 0.3385 0.3176 0.3345 -0.0500 0.0312  -0.0628 45  PHE A CB  
143  C CG  . PHE A 33  ? 0.3279 0.3115 0.3269 -0.0527 0.0321  -0.0655 45  PHE A CG  
144  C CD1 . PHE A 33  ? 0.3351 0.3135 0.3346 -0.0530 0.0333  -0.0635 45  PHE A CD1 
145  C CD2 . PHE A 33  ? 0.3571 0.3506 0.3583 -0.0548 0.0316  -0.0700 45  PHE A CD2 
146  C CE1 . PHE A 33  ? 0.3635 0.3461 0.3659 -0.0557 0.0343  -0.0661 45  PHE A CE1 
147  C CE2 . PHE A 33  ? 0.4168 0.4142 0.4211 -0.0572 0.0323  -0.0725 45  PHE A CE2 
148  C CZ  . PHE A 33  ? 0.3858 0.3777 0.3907 -0.0578 0.0338  -0.0705 45  PHE A CZ  
149  N N   . VAL A 34  ? 0.2659 0.2358 0.2583 -0.0445 0.0289  -0.0592 46  VAL A N   
150  C CA  . VAL A 34  ? 0.2667 0.2334 0.2573 -0.0425 0.0282  -0.0572 46  VAL A CA  
151  C C   . VAL A 34  ? 0.2505 0.2277 0.2406 -0.0436 0.0280  -0.0597 46  VAL A C   
152  O O   . VAL A 34  ? 0.2773 0.2625 0.2685 -0.0454 0.0280  -0.0642 46  VAL A O   
153  C CB  . VAL A 34  ? 0.2839 0.2451 0.2748 -0.0400 0.0269  -0.0557 46  VAL A CB  
154  C CG1 . VAL A 34  ? 0.2832 0.2433 0.2729 -0.0384 0.0263  -0.0546 46  VAL A CG1 
155  C CG2 . VAL A 34  ? 0.2837 0.2362 0.2742 -0.0379 0.0261  -0.0515 46  VAL A CG2 
156  N N   . TRP A 35  ? 0.2421 0.2215 0.2313 -0.0409 0.0270  -0.0543 47  TRP A N   
157  C CA  . TRP A 35  ? 0.2490 0.2407 0.2381 -0.0401 0.0260  -0.0529 47  TRP A CA  
158  C C   . TRP A 35  ? 0.2390 0.2283 0.2268 -0.0375 0.0252  -0.0480 47  TRP A C   
159  O O   . TRP A 35  ? 0.2105 0.1916 0.1978 -0.0357 0.0249  -0.0438 47  TRP A O   
160  C CB  . TRP A 35  ? 0.2345 0.2356 0.2245 -0.0399 0.0253  -0.0508 47  TRP A CB  
161  C CG  . TRP A 35  ? 0.2229 0.2360 0.2123 -0.0389 0.0240  -0.0486 47  TRP A CG  
162  C CD1 . TRP A 35  ? 0.2365 0.2611 0.2261 -0.0403 0.0238  -0.0522 47  TRP A CD1 
163  C CD2 . TRP A 35  ? 0.2448 0.2596 0.2332 -0.0363 0.0227  -0.0422 47  TRP A CD2 
164  N NE1 . TRP A 35  ? 0.2145 0.2482 0.2028 -0.0388 0.0226  -0.0483 47  TRP A NE1 
165  C CE2 . TRP A 35  ? 0.2134 0.2411 0.2011 -0.0365 0.0219  -0.0420 47  TRP A CE2 
166  C CE3 . TRP A 35  ? 0.2305 0.2372 0.2185 -0.0340 0.0221  -0.0368 47  TRP A CE3 
167  C CZ2 . TRP A 35  ? 0.1710 0.2035 0.1577 -0.0346 0.0205  -0.0362 47  TRP A CZ2 
168  C CZ3 . TRP A 35  ? 0.2105 0.2219 0.1980 -0.0320 0.0206  -0.0312 47  TRP A CZ3 
169  C CH2 . TRP A 35  ? 0.2161 0.2402 0.2028 -0.0324 0.0199  -0.0307 47  TRP A CH2 
170  N N   . GLY A 36  ? 0.1905 0.1876 0.1778 -0.0374 0.0248  -0.0484 48  GLY A N   
171  C CA  . GLY A 36  ? 0.2042 0.2022 0.1906 -0.0353 0.0239  -0.0432 48  GLY A CA  
172  C C   . GLY A 36  ? 0.2647 0.2519 0.2509 -0.0343 0.0242  -0.0427 48  GLY A C   
173  O O   . GLY A 36  ? 0.2234 0.2043 0.2097 -0.0353 0.0251  -0.0473 48  GLY A O   
174  N N   . GLY A 37  ? 0.2125 0.1974 0.1984 -0.0322 0.0233  -0.0369 49  GLY A N   
175  C CA  . GLY A 37  ? 0.2357 0.2118 0.2217 -0.0310 0.0233  -0.0357 49  GLY A CA  
176  C C   . GLY A 37  ? 0.2529 0.2358 0.2388 -0.0313 0.0235  -0.0364 49  GLY A C   
177  O O   . GLY A 37  ? 0.2102 0.2052 0.1958 -0.0323 0.0237  -0.0376 49  GLY A O   
178  N N   . TYR A 38  ? 0.2202 0.1958 0.2067 -0.0303 0.0235  -0.0357 50  TYR A N   
179  C CA  . TYR A 38  ? 0.2267 0.2079 0.2135 -0.0303 0.0238  -0.0360 50  TYR A CA  
180  C C   . TYR A 38  ? 0.2693 0.2413 0.2569 -0.0301 0.0243  -0.0402 50  TYR A C   
181  O O   . TYR A 38  ? 0.2436 0.2041 0.2311 -0.0297 0.0242  -0.0415 50  TYR A O   
182  C CB  . TYR A 38  ? 0.2338 0.2169 0.2210 -0.0289 0.0228  -0.0289 50  TYR A CB  
183  C CG  . TYR A 38  ? 0.1874 0.1580 0.1757 -0.0272 0.0222  -0.0265 50  TYR A CG  
184  C CD1 . TYR A 38  ? 0.2048 0.1647 0.1930 -0.0261 0.0214  -0.0250 50  TYR A CD1 
185  C CD2 . TYR A 38  ? 0.2210 0.1907 0.2105 -0.0268 0.0223  -0.0260 50  TYR A CD2 
186  C CE1 . TYR A 38  ? 0.2384 0.1869 0.2274 -0.0244 0.0206  -0.0230 50  TYR A CE1 
187  C CE2 . TYR A 38  ? 0.1920 0.1503 0.1828 -0.0252 0.0215  -0.0240 50  TYR A CE2 
188  C CZ  . TYR A 38  ? 0.2669 0.2145 0.2572 -0.0240 0.0206  -0.0226 50  TYR A CZ  
189  O OH  . TYR A 38  ? 0.2601 0.1967 0.2514 -0.0223 0.0196  -0.0209 50  TYR A OH  
190  N N   . LYS A 39  ? 0.2846 0.2619 0.2729 -0.0304 0.0249  -0.0425 51  LYS A N   
191  C CA  . LYS A 39  ? 0.3053 0.2744 0.2949 -0.0298 0.0251  -0.0461 51  LYS A CA  
192  C C   . LYS A 39  ? 0.3592 0.3339 0.3501 -0.0293 0.0253  -0.0444 51  LYS A C   
193  O O   . LYS A 39  ? 0.3348 0.3183 0.3254 -0.0293 0.0253  -0.0396 51  LYS A O   
194  C CB  . LYS A 39  ? 0.3198 0.2888 0.3095 -0.0312 0.0258  -0.0539 51  LYS A CB  
195  C CG  . LYS A 39  ? 0.3521 0.3355 0.3418 -0.0326 0.0266  -0.0576 51  LYS A CG  
196  C CD  . LYS A 39  ? 0.3935 0.3759 0.3837 -0.0339 0.0269  -0.0654 51  LYS A CD  
197  C CE  . LYS A 39  ? 0.4300 0.4268 0.4202 -0.0350 0.0276  -0.0698 51  LYS A CE  
198  N NZ  . LYS A 39  ? 0.4278 0.4284 0.4193 -0.0342 0.0281  -0.0723 51  LYS A NZ  
199  N N   . SER A 40  ? 0.3303 0.2998 0.3227 -0.0287 0.0255  -0.0480 52  SER A N   
200  C CA  . SER A 40  ? 0.4116 0.3875 0.4057 -0.0284 0.0260  -0.0477 52  SER A CA  
201  C C   . SER A 40  ? 0.4780 0.4617 0.4726 -0.0293 0.0271  -0.0551 52  SER A C   
202  O O   . SER A 40  ? 0.4920 0.4770 0.4857 -0.0303 0.0273  -0.0598 52  SER A O   
203  C CB  . SER A 40  ? 0.4063 0.3709 0.4022 -0.0267 0.0252  -0.0462 52  SER A CB  
204  O OG  . SER A 40  ? 0.3885 0.3453 0.3839 -0.0257 0.0240  -0.0401 52  SER A OG  
205  N N   . ASN A 41  ? 0.5508 0.5403 0.5471 -0.0290 0.0277  -0.0561 53  ASN A N   
206  C CA  . ASN A 41  ? 0.5884 0.5860 0.5856 -0.0296 0.0288  -0.0633 53  ASN A CA  
207  C C   . ASN A 41  ? 0.5981 0.6081 0.5932 -0.0311 0.0295  -0.0655 53  ASN A C   
208  O O   . ASN A 41  ? 0.6130 0.6290 0.6062 -0.0318 0.0295  -0.0604 53  ASN A O   
209  C CB  . ASN A 41  ? 0.6255 0.6121 0.6241 -0.0289 0.0281  -0.0700 53  ASN A CB  
210  C CG  . ASN A 41  ? 0.6753 0.6616 0.6770 -0.0276 0.0281  -0.0730 53  ASN A CG  
211  O OD1 . ASN A 41  ? 0.6641 0.6524 0.6671 -0.0271 0.0286  -0.0695 53  ASN A OD1 
212  N ND2 . ASN A 41  ? 0.7242 0.7099 0.7281 -0.0256 0.0262  -0.0746 53  ASN A ND2 
213  N N   . PHE A 49  ? 0.4833 0.5015 0.4712 -0.0317 0.0265  -0.0364 61  PHE A N   
214  C CA  . PHE A 49  ? 0.3685 0.3956 0.3543 -0.0325 0.0261  -0.0347 61  PHE A CA  
215  C C   . PHE A 49  ? 0.3307 0.3510 0.3162 -0.0326 0.0255  -0.0372 61  PHE A C   
216  O O   . PHE A 49  ? 0.3205 0.3290 0.3070 -0.0322 0.0255  -0.0398 61  PHE A O   
217  C CB  . PHE A 49  ? 0.3935 0.4355 0.3780 -0.0338 0.0272  -0.0385 61  PHE A CB  
218  C CG  . PHE A 49  ? 0.5113 0.5530 0.4968 -0.0342 0.0283  -0.0467 61  PHE A CG  
219  C CD1 . PHE A 49  ? 0.4911 0.5297 0.4768 -0.0349 0.0283  -0.0534 61  PHE A CD1 
220  C CD2 . PHE A 49  ? 0.6279 0.6723 0.6146 -0.0340 0.0293  -0.0479 61  PHE A CD2 
221  C CE1 . PHE A 49  ? 0.5882 0.6260 0.5753 -0.0351 0.0291  -0.0611 61  PHE A CE1 
222  C CE2 . PHE A 49  ? 0.5906 0.6348 0.5788 -0.0341 0.0302  -0.0557 61  PHE A CE2 
223  C CZ  . PHE A 49  ? 0.5756 0.6162 0.5639 -0.0346 0.0299  -0.0624 61  PHE A CZ  
224  N N   . TYR A 50  ? 0.3360 0.3643 0.3201 -0.0332 0.0251  -0.0361 62  TYR A N   
225  C CA  . TYR A 50  ? 0.2973 0.3205 0.2814 -0.0334 0.0245  -0.0373 62  TYR A CA  
226  C C   . TYR A 50  ? 0.2853 0.3108 0.2695 -0.0349 0.0253  -0.0453 62  TYR A C   
227  O O   . TYR A 50  ? 0.2994 0.3353 0.2830 -0.0359 0.0259  -0.0492 62  TYR A O   
228  C CB  . TYR A 50  ? 0.2869 0.3176 0.2699 -0.0331 0.0233  -0.0323 62  TYR A CB  
229  C CG  . TYR A 50  ? 0.2850 0.3122 0.2684 -0.0315 0.0221  -0.0242 62  TYR A CG  
230  C CD1 . TYR A 50  ? 0.2389 0.2542 0.2233 -0.0301 0.0212  -0.0216 62  TYR A CD1 
231  C CD2 . TYR A 50  ? 0.2532 0.2891 0.2357 -0.0314 0.0217  -0.0193 62  TYR A CD2 
232  C CE1 . TYR A 50  ? 0.2872 0.2991 0.2723 -0.0286 0.0198  -0.0145 62  TYR A CE1 
233  C CE2 . TYR A 50  ? 0.2454 0.2776 0.2286 -0.0301 0.0203  -0.0118 62  TYR A CE2 
234  C CZ  . TYR A 50  ? 0.2664 0.2867 0.2510 -0.0286 0.0193  -0.0096 62  TYR A CZ  
235  O OH  . TYR A 50  ? 0.2883 0.3050 0.2739 -0.0272 0.0177  -0.0025 62  TYR A OH  
236  N N   . LEU A 51  ? 0.2708 0.2866 0.2558 -0.0352 0.0253  -0.0478 63  LEU A N   
237  C CA  . LEU A 51  ? 0.2495 0.2667 0.2349 -0.0369 0.0258  -0.0550 63  LEU A CA  
238  C C   . LEU A 51  ? 0.2246 0.2541 0.2093 -0.0379 0.0254  -0.0551 63  LEU A C   
239  O O   . LEU A 51  ? 0.2107 0.2438 0.1947 -0.0370 0.0245  -0.0494 63  LEU A O   
240  C CB  . LEU A 51  ? 0.2730 0.2768 0.2593 -0.0372 0.0259  -0.0567 63  LEU A CB  
241  C CG  . LEU A 51  ? 0.2728 0.2639 0.2599 -0.0367 0.0263  -0.0588 63  LEU A CG  
242  C CD1 . LEU A 51  ? 0.3058 0.2992 0.2939 -0.0377 0.0268  -0.0660 63  LEU A CD1 
243  C CD2 . LEU A 51  ? 0.2831 0.2691 0.2701 -0.0346 0.0259  -0.0535 63  LEU A CD2 
244  N N   . PRO A 52  ? 0.2610 0.2973 0.2460 -0.0395 0.0258  -0.0617 64  PRO A N   
245  C CA  . PRO A 52  ? 0.2606 0.3106 0.2447 -0.0403 0.0252  -0.0622 64  PRO A CA  
246  C C   . PRO A 52  ? 0.2587 0.3076 0.2433 -0.0404 0.0244  -0.0595 64  PRO A C   
247  O O   . PRO A 52  ? 0.2501 0.2899 0.2362 -0.0411 0.0247  -0.0614 64  PRO A O   
248  C CB  . PRO A 52  ? 0.3332 0.3878 0.3181 -0.0420 0.0257  -0.0708 64  PRO A CB  
249  C CG  . PRO A 52  ? 0.2954 0.3425 0.2811 -0.0416 0.0265  -0.0737 64  PRO A CG  
250  C CD  . PRO A 52  ? 0.2956 0.3283 0.2819 -0.0405 0.0265  -0.0691 64  PRO A CD  
251  N N   . ARG A 53  ? 0.2168 0.2755 0.2001 -0.0397 0.0234  -0.0550 65  ARG A N   
252  C CA  . ARG A 53  ? 0.2495 0.3078 0.2334 -0.0393 0.0224  -0.0515 65  ARG A CA  
253  C C   . ARG A 53  ? 0.2499 0.3112 0.2355 -0.0412 0.0225  -0.0571 65  ARG A C   
254  O O   . ARG A 53  ? 0.2528 0.3089 0.2398 -0.0412 0.0223  -0.0560 65  ARG A O   
255  C CB  . ARG A 53  ? 0.2262 0.2948 0.2085 -0.0380 0.0210  -0.0455 65  ARG A CB  
256  C CG  . ARG A 53  ? 0.2281 0.3116 0.2086 -0.0389 0.0207  -0.0484 65  ARG A CG  
257  C CD  . ARG A 53  ? 0.2590 0.3513 0.2373 -0.0376 0.0195  -0.0415 65  ARG A CD  
258  N NE  . ARG A 53  ? 0.2324 0.3265 0.2111 -0.0366 0.0177  -0.0370 65  ARG A NE  
259  C CZ  . ARG A 53  ? 0.2569 0.3601 0.2338 -0.0355 0.0161  -0.0315 65  ARG A CZ  
260  N NH1 . ARG A 53  ? 0.2781 0.3899 0.2523 -0.0356 0.0161  -0.0296 65  ARG A NH1 
261  N NH2 . ARG A 53  ? 0.2573 0.3613 0.2352 -0.0344 0.0143  -0.0280 65  ARG A NH2 
262  N N   . GLU A 54  ? 0.2442 0.3142 0.2296 -0.0427 0.0227  -0.0631 66  GLU A N   
263  C CA  . GLU A 54  ? 0.2570 0.3314 0.2443 -0.0446 0.0224  -0.0683 66  GLU A CA  
264  C C   . GLU A 54  ? 0.2903 0.3534 0.2800 -0.0463 0.0235  -0.0731 66  GLU A C   
265  O O   . GLU A 54  ? 0.3043 0.3685 0.2961 -0.0480 0.0235  -0.0762 66  GLU A O   
266  C CB  . GLU A 54  ? 0.2743 0.3622 0.2608 -0.0456 0.0220  -0.0734 66  GLU A CB  
267  C CG  . GLU A 54  ? 0.2895 0.3753 0.2762 -0.0465 0.0230  -0.0796 66  GLU A CG  
268  C CD  . GLU A 54  ? 0.3527 0.4379 0.3373 -0.0449 0.0236  -0.0765 66  GLU A CD  
269  O OE1 . GLU A 54  ? 0.4132 0.4972 0.3981 -0.0453 0.0243  -0.0815 66  GLU A OE1 
270  O OE2 . GLU A 54  ? 0.3484 0.4346 0.3313 -0.0433 0.0231  -0.0692 66  GLU A OE2 
271  N N   . GLU A 55  ? 0.2853 0.3376 0.2748 -0.0460 0.0245  -0.0736 67  GLU A N   
272  C CA  . GLU A 55  ? 0.2706 0.3123 0.2621 -0.0477 0.0253  -0.0783 67  GLU A CA  
273  C C   . GLU A 55  ? 0.2863 0.3180 0.2785 -0.0476 0.0257  -0.0744 67  GLU A C   
274  O O   . GLU A 55  ? 0.2824 0.3105 0.2734 -0.0455 0.0255  -0.0681 67  GLU A O   
275  C CB  . GLU A 55  ? 0.2997 0.3336 0.2908 -0.0473 0.0260  -0.0806 67  GLU A CB  
276  C CG  . GLU A 55  ? 0.2983 0.3421 0.2885 -0.0470 0.0258  -0.0837 67  GLU A CG  
277  C CD  . GLU A 55  ? 0.3731 0.4093 0.3642 -0.0456 0.0261  -0.0843 67  GLU A CD  
278  O OE1 . GLU A 55  ? 0.3704 0.3949 0.3612 -0.0446 0.0264  -0.0810 67  GLU A OE1 
279  O OE2 . GLU A 55  ? 0.3822 0.4244 0.3748 -0.0452 0.0258  -0.0875 67  GLU A OE2 
280  N N   . LEU A 56  ? 0.2680 0.2958 0.2623 -0.0498 0.0262  -0.0781 68  LEU A N   
281  C CA  . LEU A 56  ? 0.3115 0.3284 0.3065 -0.0501 0.0270  -0.0757 68  LEU A CA  
282  C C   . LEU A 56  ? 0.3277 0.3352 0.3249 -0.0499 0.0274  -0.0765 68  LEU A C   
283  O O   . LEU A 56  ? 0.3437 0.3550 0.3434 -0.0508 0.0271  -0.0796 68  LEU A O   
284  C CB  . LEU A 56  ? 0.3052 0.3278 0.3019 -0.0511 0.0269  -0.0751 68  LEU A CB  
285  C CG  . LEU A 56  ? 0.3115 0.3242 0.3087 -0.0511 0.0279  -0.0721 68  LEU A CG  
286  C CD1 . LEU A 56  ? 0.2808 0.2897 0.2760 -0.0478 0.0274  -0.0652 68  LEU A CD1 
287  C CD2 . LEU A 56  ? 0.3921 0.4106 0.3919 -0.0529 0.0281  -0.0733 68  LEU A CD2 
288  N N   . TRP A 57  ? 0.3576 0.3533 0.3539 -0.0480 0.0275  -0.0725 69  TRP A N   
289  C CA  . TRP A 57  ? 0.3366 0.3239 0.3343 -0.0467 0.0271  -0.0712 69  TRP A CA  
290  C C   . TRP A 57  ? 0.3617 0.3425 0.3599 -0.0471 0.0277  -0.0687 69  TRP A C   
291  O O   . TRP A 57  ? 0.3161 0.2933 0.3127 -0.0467 0.0282  -0.0657 69  TRP A O   
292  C CB  . TRP A 57  ? 0.3670 0.3467 0.3632 -0.0438 0.0263  -0.0683 69  TRP A CB  
293  C CG  . TRP A 57  ? 0.3526 0.3381 0.3490 -0.0434 0.0258  -0.0712 69  TRP A CG  
294  C CD1 . TRP A 57  ? 0.3459 0.3369 0.3406 -0.0434 0.0261  -0.0719 69  TRP A CD1 
295  C CD2 . TRP A 57  ? 0.3827 0.3693 0.3811 -0.0429 0.0249  -0.0740 69  TRP A CD2 
296  N NE1 . TRP A 57  ? 0.3840 0.3802 0.3795 -0.0430 0.0257  -0.0750 69  TRP A NE1 
297  C CE2 . TRP A 57  ? 0.3871 0.3805 0.3850 -0.0426 0.0249  -0.0764 69  TRP A CE2 
298  C CE3 . TRP A 57  ? 0.4205 0.4030 0.4207 -0.0428 0.0240  -0.0747 69  TRP A CE3 
299  C CZ2 . TRP A 57  ? 0.3980 0.3942 0.3976 -0.0419 0.0241  -0.0796 69  TRP A CZ2 
300  C CZ3 . TRP A 57  ? 0.4361 0.4207 0.4377 -0.0422 0.0231  -0.0778 69  TRP A CZ3 
301  C CH2 . TRP A 57  ? 0.4280 0.4196 0.4296 -0.0417 0.0232  -0.0803 69  TRP A CH2 
302  N N   . ILE A 58  ? 0.3792 0.3589 0.3794 -0.0480 0.0275  -0.0701 70  ILE A N   
303  C CA  . ILE A 58  ? 0.3470 0.3217 0.3477 -0.0488 0.0282  -0.0682 70  ILE A CA  
304  C C   . ILE A 58  ? 0.3744 0.3398 0.3746 -0.0470 0.0269  -0.0657 70  ILE A C   
305  O O   . ILE A 58  ? 0.3924 0.3581 0.3940 -0.0470 0.0258  -0.0680 70  ILE A O   
306  C CB  . ILE A 58  ? 0.4057 0.3879 0.4094 -0.0520 0.0290  -0.0722 70  ILE A CB  
307  C CG1 . ILE A 58  ? 0.3887 0.3811 0.3926 -0.0537 0.0296  -0.0745 70  ILE A CG1 
308  C CG2 . ILE A 58  ? 0.4008 0.3776 0.4051 -0.0531 0.0299  -0.0704 70  ILE A CG2 
309  C CD1 . ILE A 58  ? 0.4130 0.4137 0.4201 -0.0567 0.0302  -0.0782 70  ILE A CD1 
310  N N   . TYR A 59  ? 0.4052 0.3629 0.4033 -0.0452 0.0267  -0.0612 71  TYR A N   
311  C CA  . TYR A 59  ? 0.4171 0.3666 0.4143 -0.0434 0.0251  -0.0585 71  TYR A CA  
312  C C   . TYR A 59  ? 0.3817 0.3287 0.3794 -0.0452 0.0261  -0.0577 71  TYR A C   
313  O O   . TYR A 59  ? 0.4144 0.3612 0.4112 -0.0457 0.0276  -0.0560 71  TYR A O   
314  C CB  . TYR A 59  ? 0.4046 0.3482 0.3992 -0.0399 0.0237  -0.0540 71  TYR A CB  
315  C CG  . TYR A 59  ? 0.3965 0.3325 0.3899 -0.0378 0.0214  -0.0511 71  TYR A CG  
316  C CD1 . TYR A 59  ? 0.4183 0.3522 0.4120 -0.0364 0.0190  -0.0519 71  TYR A CD1 
317  C CD2 . TYR A 59  ? 0.4042 0.3357 0.3964 -0.0373 0.0214  -0.0478 71  TYR A CD2 
318  C CE1 . TYR A 59  ? 0.3938 0.3212 0.3866 -0.0347 0.0167  -0.0496 71  TYR A CE1 
319  C CE2 . TYR A 59  ? 0.4251 0.3505 0.4163 -0.0354 0.0189  -0.0454 71  TYR A CE2 
320  C CZ  . TYR A 59  ? 0.4638 0.3871 0.4554 -0.0347 0.0175  -0.0468 71  TYR A CZ  
321  O OH  . TYR A 59  ? 0.5337 0.4510 0.5246 -0.0341 0.0168  -0.0456 71  TYR A OH  
322  N N   . ASN A 60  ? 0.4710 0.4162 0.4700 -0.0463 0.0253  -0.0592 72  ASN A N   
323  C CA  . ASN A 60  ? 0.4378 0.3799 0.4372 -0.0482 0.0262  -0.0584 72  ASN A CA  
324  C C   . ASN A 60  ? 0.4778 0.4116 0.4745 -0.0456 0.0247  -0.0538 72  ASN A C   
325  O O   . ASN A 60  ? 0.5072 0.4364 0.5033 -0.0438 0.0220  -0.0529 72  ASN A O   
326  C CB  . ASN A 60  ? 0.4759 0.4190 0.4779 -0.0505 0.0257  -0.0618 72  ASN A CB  
327  C CG  . ASN A 60  ? 0.4657 0.4071 0.4687 -0.0533 0.0271  -0.0616 72  ASN A CG  
328  O OD1 . ASN A 60  ? 0.4993 0.4352 0.5002 -0.0526 0.0274  -0.0581 72  ASN A OD1 
329  N ND2 . ASN A 60  ? 0.4452 0.3916 0.4513 -0.0564 0.0281  -0.0655 72  ASN A ND2 
330  N N   . MET A 61  ? 0.4450 0.3775 0.4402 -0.0455 0.0262  -0.0511 73  MET A N   
331  C CA  . MET A 61  ? 0.4695 0.3953 0.4622 -0.0431 0.0248  -0.0470 73  MET A CA  
332  C C   . MET A 61  ? 0.4775 0.3985 0.4705 -0.0441 0.0237  -0.0467 73  MET A C   
333  O O   . MET A 61  ? 0.4613 0.3768 0.4526 -0.0422 0.0222  -0.0441 73  MET A O   
334  C CB  . MET A 61  ? 0.4446 0.3704 0.4357 -0.0432 0.0269  -0.0449 73  MET A CB  
335  C CG  . MET A 61  ? 0.4618 0.3892 0.4518 -0.0407 0.0267  -0.0434 73  MET A CG  
336  S SD  . MET A 61  ? 0.4781 0.4082 0.4676 -0.0420 0.0298  -0.0431 73  MET A SD  
337  C CE  . MET A 61  ? 0.3965 0.3254 0.3843 -0.0381 0.0281  -0.0402 73  MET A CE  
338  N N   . GLU A 62  ? 0.5071 0.4301 0.5023 -0.0476 0.0250  -0.0496 74  GLU A N   
339  C CA  . GLU A 62  ? 0.5910 0.5090 0.5866 -0.0490 0.0241  -0.0493 74  GLU A CA  
340  C C   . GLU A 62  ? 0.5387 0.4547 0.5356 -0.0485 0.0213  -0.0513 74  GLU A C   
341  O O   . GLU A 62  ? 0.5696 0.4795 0.5661 -0.0490 0.0206  -0.0507 74  GLU A O   
342  C CB  . GLU A 62  ? 0.5793 0.5000 0.5768 -0.0533 0.0271  -0.0514 74  GLU A CB  
343  N N   . THR A 63  ? 0.5267 0.4474 0.5250 -0.0481 0.0206  -0.0541 75  THR A N   
344  C CA  . THR A 63  ? 0.5533 0.4724 0.5527 -0.0478 0.0186  -0.0566 75  THR A CA  
345  C C   . THR A 63  ? 0.5553 0.4743 0.5534 -0.0447 0.0173  -0.0565 75  THR A C   
346  O O   . THR A 63  ? 0.5590 0.4769 0.5579 -0.0443 0.0159  -0.0589 75  THR A O   
347  C CB  . THR A 63  ? 0.5683 0.4932 0.5707 -0.0504 0.0191  -0.0611 75  THR A CB  
348  O OG1 . THR A 63  ? 0.6063 0.5383 0.6093 -0.0497 0.0202  -0.0632 75  THR A OG1 
349  C CG2 . THR A 63  ? 0.5613 0.4886 0.5655 -0.0541 0.0219  -0.0619 75  THR A CG2 
350  N N   . GLY A 64  ? 0.5392 0.4597 0.5356 -0.0426 0.0178  -0.0540 76  GLY A N   
351  C CA  . GLY A 64  ? 0.5299 0.4500 0.5253 -0.0398 0.0166  -0.0535 76  GLY A CA  
352  C C   . GLY A 64  ? 0.4896 0.4147 0.4863 -0.0396 0.0159  -0.0570 76  GLY A C   
353  O O   . GLY A 64  ? 0.5001 0.4243 0.4963 -0.0376 0.0148  -0.0572 76  GLY A O   
354  N N   . ARG A 65  ? 0.5102 0.4410 0.5088 -0.0419 0.0168  -0.0600 77  ARG A N   
355  C CA  . ARG A 65  ? 0.5044 0.4412 0.5047 -0.0424 0.0171  -0.0642 77  ARG A CA  
356  C C   . ARG A 65  ? 0.4830 0.4276 0.4838 -0.0430 0.0195  -0.0652 77  ARG A C   
357  O O   . ARG A 65  ? 0.4669 0.4138 0.4679 -0.0447 0.0216  -0.0646 77  ARG A O   
358  C CB  . ARG A 65  ? 0.5230 0.4621 0.5261 -0.0452 0.0172  -0.0683 77  ARG A CB  
359  C CG  . ARG A 65  ? 0.5997 0.5312 0.6025 -0.0448 0.0147  -0.0680 77  ARG A CG  
360  C CD  . ARG A 65  ? 0.6440 0.5765 0.6495 -0.0478 0.0147  -0.0713 77  ARG A CD  
361  N NE  . ARG A 65  ? 0.6535 0.5777 0.6590 -0.0486 0.0137  -0.0705 77  ARG A NE  
362  C CZ  . ARG A 65  ? 0.6522 0.5737 0.6584 -0.0510 0.0143  -0.0695 77  ARG A CZ  
363  N NH1 . ARG A 65  ? 0.6171 0.5435 0.6244 -0.0530 0.0160  -0.0695 77  ARG A NH1 
364  N NH2 . ARG A 65  ? 0.6608 0.5743 0.6667 -0.0516 0.0132  -0.0686 77  ARG A NH2 
365  N N   . TRP A 66  ? 0.4687 0.4170 0.4695 -0.0418 0.0192  -0.0669 78  TRP A N   
366  C CA  . TRP A 66  ? 0.4857 0.4422 0.4870 -0.0426 0.0211  -0.0686 78  TRP A CA  
367  C C   . TRP A 66  ? 0.4900 0.4555 0.4942 -0.0452 0.0221  -0.0739 78  TRP A C   
368  O O   . TRP A 66  ? 0.5002 0.4657 0.5060 -0.0458 0.0210  -0.0767 78  TRP A O   
369  C CB  . TRP A 66  ? 0.4458 0.4028 0.4458 -0.0402 0.0205  -0.0679 78  TRP A CB  
370  C CG  . TRP A 66  ? 0.4485 0.3984 0.4459 -0.0377 0.0195  -0.0629 78  TRP A CG  
371  C CD1 . TRP A 66  ? 0.4375 0.3801 0.4335 -0.0351 0.0170  -0.0603 78  TRP A CD1 
372  C CD2 . TRP A 66  ? 0.4089 0.3588 0.4048 -0.0372 0.0207  -0.0600 78  TRP A CD2 
373  N NE1 . TRP A 66  ? 0.4245 0.3631 0.4185 -0.0330 0.0165  -0.0560 78  TRP A NE1 
374  C CE2 . TRP A 66  ? 0.3955 0.3382 0.3895 -0.0343 0.0188  -0.0557 78  TRP A CE2 
375  C CE3 . TRP A 66  ? 0.3902 0.3456 0.3862 -0.0391 0.0228  -0.0608 78  TRP A CE3 
376  C CZ2 . TRP A 66  ? 0.3291 0.2699 0.3216 -0.0330 0.0192  -0.0521 78  TRP A CZ2 
377  C CZ3 . TRP A 66  ? 0.3487 0.3014 0.3429 -0.0379 0.0232  -0.0572 78  TRP A CZ3 
378  C CH2 . TRP A 66  ? 0.3613 0.3066 0.3538 -0.0348 0.0215  -0.0529 78  TRP A CH2 
379  N N   . LYS A 67  ? 0.5443 0.5177 0.5489 -0.0468 0.0238  -0.0754 79  LYS A N   
380  C CA  . LYS A 67  ? 0.4231 0.4071 0.4302 -0.0491 0.0244  -0.0805 79  LYS A CA  
381  C C   . LYS A 67  ? 0.4502 0.4426 0.4563 -0.0494 0.0253  -0.0812 79  LYS A C   
382  O O   . LYS A 67  ? 0.4378 0.4294 0.4425 -0.0498 0.0263  -0.0787 79  LYS A O   
383  C CB  . LYS A 67  ? 0.4941 0.4794 0.5034 -0.0518 0.0252  -0.0818 79  LYS A CB  
384  C CG  . LYS A 67  ? 0.5646 0.5606 0.5769 -0.0539 0.0253  -0.0872 79  LYS A CG  
385  C CD  . LYS A 67  ? 0.6361 0.6323 0.6500 -0.0531 0.0237  -0.0903 79  LYS A CD  
386  C CE  . LYS A 67  ? 0.6194 0.6048 0.6334 -0.0527 0.0226  -0.0886 79  LYS A CE  
387  N NZ  . LYS A 67  ? 0.6470 0.6322 0.6625 -0.0519 0.0209  -0.0919 79  LYS A NZ  
388  N N   . LYS A 68  ? 0.3659 0.3664 0.3725 -0.0492 0.0249  -0.0846 80  LYS A N   
389  C CA  . LYS A 68  ? 0.3811 0.3906 0.3861 -0.0495 0.0254  -0.0855 80  LYS A CA  
390  C C   . LYS A 68  ? 0.4188 0.4407 0.4255 -0.0517 0.0255  -0.0896 80  LYS A C   
391  O O   . LYS A 68  ? 0.4337 0.4592 0.4430 -0.0525 0.0250  -0.0931 80  LYS A O   
392  C CB  . LYS A 68  ? 0.4008 0.4125 0.4048 -0.0477 0.0248  -0.0865 80  LYS A CB  
393  C CG  . LYS A 68  ? 0.4226 0.4476 0.4254 -0.0484 0.0249  -0.0893 80  LYS A CG  
394  C CD  . LYS A 68  ? 0.4315 0.4593 0.4343 -0.0468 0.0245  -0.0912 80  LYS A CD  
395  C CE  . LYS A 68  ? 0.4264 0.4684 0.4274 -0.0473 0.0245  -0.0936 80  LYS A CE  
396  N NZ  . LYS A 68  ? 0.4415 0.4862 0.4423 -0.0457 0.0244  -0.0951 80  LYS A NZ  
397  N N   . ILE A 69  ? 0.3813 0.4098 0.3862 -0.0526 0.0258  -0.0891 81  ILE A N   
398  C CA  . ILE A 69  ? 0.3813 0.4233 0.3870 -0.0543 0.0254  -0.0926 81  ILE A CA  
399  C C   . ILE A 69  ? 0.3699 0.4210 0.3719 -0.0538 0.0249  -0.0921 81  ILE A C   
400  O O   . ILE A 69  ? 0.3623 0.4086 0.3612 -0.0529 0.0253  -0.0887 81  ILE A O   
401  C CB  . ILE A 69  ? 0.3790 0.4215 0.3864 -0.0563 0.0259  -0.0924 81  ILE A CB  
402  C CG1 . ILE A 69  ? 0.4156 0.4480 0.4213 -0.0560 0.0268  -0.0879 81  ILE A CG1 
403  C CG2 . ILE A 69  ? 0.4793 0.5193 0.4907 -0.0575 0.0260  -0.0947 81  ILE A CG2 
404  C CD1 . ILE A 69  ? 0.4444 0.4773 0.4519 -0.0580 0.0275  -0.0877 81  ILE A CD1 
405  N N   . ASN A 70  ? 0.3628 0.4274 0.3648 -0.0541 0.0240  -0.0953 82  ASN A N   
406  C CA  . ASN A 70  ? 0.3694 0.4450 0.3671 -0.0536 0.0232  -0.0945 82  ASN A CA  
407  C C   . ASN A 70  ? 0.3827 0.4644 0.3806 -0.0541 0.0225  -0.0921 82  ASN A C   
408  O O   . ASN A 70  ? 0.3850 0.4718 0.3854 -0.0561 0.0221  -0.0961 82  ASN A O   
409  C CB  . ASN A 70  ? 0.3749 0.4629 0.3726 -0.0531 0.0224  -0.0977 82  ASN A CB  
410  C CG  . ASN A 70  ? 0.4165 0.5003 0.4142 -0.0516 0.0229  -0.0983 82  ASN A CG  
411  O OD1 . ASN A 70  ? 0.4371 0.5117 0.4332 -0.0507 0.0236  -0.0954 82  ASN A OD1 
412  N ND2 . ASN A 70  ? 0.5799 0.6708 0.5796 -0.0513 0.0224  -0.1021 82  ASN A ND2 
413  N N   . THR A 71  ? 0.3275 0.4081 0.3235 -0.0517 0.0223  -0.0847 83  THR A N   
414  C CA  . THR A 71  ? 0.2859 0.3723 0.2824 -0.0509 0.0213  -0.0807 83  THR A CA  
415  C C   . THR A 71  ? 0.3075 0.4079 0.3017 -0.0493 0.0197  -0.0784 83  THR A C   
416  O O   . THR A 71  ? 0.3188 0.4218 0.3101 -0.0482 0.0196  -0.0773 83  THR A O   
417  C CB  . THR A 71  ? 0.2961 0.3728 0.2921 -0.0490 0.0217  -0.0737 83  THR A CB  
418  O OG1 . THR A 71  ? 0.2775 0.3528 0.2705 -0.0466 0.0215  -0.0688 83  THR A OG1 
419  C CG2 . THR A 71  ? 0.3108 0.3733 0.3084 -0.0504 0.0234  -0.0754 83  THR A CG2 
420  N N   . GLU A 72  ? 0.2726 0.3818 0.2679 -0.0492 0.0183  -0.0775 84  GLU A N   
421  C CA  . GLU A 72  ? 0.2616 0.3844 0.2547 -0.0477 0.0164  -0.0750 84  GLU A CA  
422  C C   . GLU A 72  ? 0.3021 0.4254 0.2955 -0.0456 0.0152  -0.0681 84  GLU A C   
423  O O   . GLU A 72  ? 0.3019 0.4147 0.2966 -0.0450 0.0159  -0.0650 84  GLU A O   
424  C CB  . GLU A 72  ? 0.3455 0.4804 0.3399 -0.0495 0.0155  -0.0818 84  GLU A CB  
425  C CG  . GLU A 72  ? 0.3974 0.5343 0.3910 -0.0510 0.0162  -0.0884 84  GLU A CG  
426  C CD  . GLU A 72  ? 0.4434 0.5925 0.4385 -0.0527 0.0149  -0.0954 84  GLU A CD  
427  O OE1 . GLU A 72  ? 0.4373 0.5959 0.4329 -0.0523 0.0133  -0.0942 84  GLU A OE1 
428  O OE2 . GLU A 72  ? 0.4376 0.5867 0.4336 -0.0544 0.0155  -0.1023 84  GLU A OE2 
429  N N   . GLY A 73  ? 0.2641 0.3996 0.2561 -0.0443 0.0131  -0.0658 85  GLY A N   
430  C CA  . GLY A 73  ? 0.2922 0.4291 0.2847 -0.0421 0.0114  -0.0595 85  GLY A CA  
431  C C   . GLY A 73  ? 0.2250 0.3584 0.2144 -0.0395 0.0109  -0.0516 85  GLY A C   
432  O O   . GLY A 73  ? 0.2643 0.4015 0.2504 -0.0393 0.0109  -0.0506 85  GLY A O   
433  N N   . ASP A 74  ? 0.2115 0.3382 0.2022 -0.0376 0.0103  -0.0461 86  ASP A N   
434  C CA  . ASP A 74  ? 0.1906 0.3124 0.1791 -0.0352 0.0096  -0.0385 86  ASP A CA  
435  C C   . ASP A 74  ? 0.2257 0.3340 0.2140 -0.0356 0.0119  -0.0386 86  ASP A C   
436  O O   . ASP A 74  ? 0.2090 0.3068 0.1986 -0.0344 0.0122  -0.0355 86  ASP A O   
437  C CB  . ASP A 74  ? 0.2198 0.3399 0.2102 -0.0327 0.0077  -0.0330 86  ASP A CB  
438  C CG  . ASP A 74  ? 0.2483 0.3805 0.2399 -0.0322 0.0054  -0.0336 86  ASP A CG  
439  O OD1 . ASP A 74  ? 0.2534 0.3971 0.2428 -0.0328 0.0044  -0.0352 86  ASP A OD1 
440  O OD2 . ASP A 74  ? 0.1915 0.3219 0.1862 -0.0310 0.0045  -0.0325 86  ASP A OD2 
441  N N   . VAL A 75  ? 0.2144 0.3233 0.2010 -0.0373 0.0133  -0.0427 87  VAL A N   
442  C CA  . VAL A 75  ? 0.2459 0.3424 0.2325 -0.0377 0.0153  -0.0436 87  VAL A CA  
443  C C   . VAL A 75  ? 0.2331 0.3233 0.2184 -0.0354 0.0148  -0.0361 87  VAL A C   
444  O O   . VAL A 75  ? 0.1970 0.2941 0.1800 -0.0344 0.0136  -0.0317 87  VAL A O   
445  C CB  . VAL A 75  ? 0.2533 0.3531 0.2384 -0.0395 0.0166  -0.0490 87  VAL A CB  
446  C CG1 . VAL A 75  ? 0.2215 0.3080 0.2071 -0.0400 0.0185  -0.0508 87  VAL A CG1 
447  C CG2 . VAL A 75  ? 0.2182 0.3265 0.2046 -0.0416 0.0166  -0.0563 87  VAL A CG2 
448  N N   . PRO A 76  ? 0.2339 0.3114 0.2205 -0.0346 0.0155  -0.0341 88  PRO A N   
449  C CA  . PRO A 76  ? 0.1829 0.2544 0.1687 -0.0324 0.0147  -0.0272 88  PRO A CA  
450  C C   . PRO A 76  ? 0.1918 0.2626 0.1755 -0.0328 0.0156  -0.0268 88  PRO A C   
451  O O   . PRO A 76  ? 0.1969 0.2681 0.1803 -0.0346 0.0172  -0.0326 88  PRO A O   
452  C CB  . PRO A 76  ? 0.2481 0.3061 0.2359 -0.0317 0.0155  -0.0269 88  PRO A CB  
453  C CG  . PRO A 76  ? 0.2279 0.2833 0.2167 -0.0340 0.0173  -0.0340 88  PRO A CG  
454  C CD  . PRO A 76  ? 0.2098 0.2781 0.1987 -0.0357 0.0169  -0.0381 88  PRO A CD  
455  N N   . PRO A 77  ? 0.1983 0.2688 0.1808 -0.0312 0.0146  -0.0203 89  PRO A N   
456  C CA  . PRO A 77  ? 0.2163 0.2856 0.1973 -0.0316 0.0156  -0.0196 89  PRO A CA  
457  C C   . PRO A 77  ? 0.2138 0.2704 0.1960 -0.0320 0.0173  -0.0228 89  PRO A C   
458  O O   . PRO A 77  ? 0.1895 0.2366 0.1733 -0.0315 0.0175  -0.0235 89  PRO A O   
459  C CB  . PRO A 77  ? 0.2556 0.3245 0.2361 -0.0297 0.0139  -0.0111 89  PRO A CB  
460  C CG  . PRO A 77  ? 0.1770 0.2416 0.1594 -0.0280 0.0122  -0.0080 89  PRO A CG  
461  C CD  . PRO A 77  ? 0.1985 0.2689 0.1815 -0.0289 0.0123  -0.0131 89  PRO A CD  
462  N N   . SER A 78  ? 0.2449 0.3019 0.2261 -0.0328 0.0187  -0.0251 90  SER A N   
463  C CA  . SER A 78  ? 0.2015 0.2465 0.1837 -0.0329 0.0200  -0.0276 90  SER A CA  
464  C C   . SER A 78  ? 0.2383 0.2730 0.2214 -0.0310 0.0191  -0.0215 90  SER A C   
465  O O   . SER A 78  ? 0.2189 0.2566 0.2015 -0.0299 0.0181  -0.0155 90  SER A O   
466  C CB  . SER A 78  ? 0.2728 0.3214 0.2541 -0.0339 0.0213  -0.0307 90  SER A CB  
467  O OG  . SER A 78  ? 0.3282 0.3825 0.3094 -0.0356 0.0222  -0.0381 90  SER A OG  
468  N N   . MET A 79  ? 0.2292 0.2519 0.2136 -0.0305 0.0195  -0.0228 91  MET A N   
469  C CA  . MET A 79  ? 0.2449 0.2582 0.2301 -0.0284 0.0184  -0.0172 91  MET A CA  
470  C C   . MET A 79  ? 0.2153 0.2150 0.2012 -0.0280 0.0193  -0.0194 91  MET A C   
471  O O   . MET A 79  ? 0.2370 0.2328 0.2229 -0.0293 0.0205  -0.0248 91  MET A O   
472  C CB  . MET A 79  ? 0.1835 0.1974 0.1695 -0.0271 0.0170  -0.0143 91  MET A CB  
473  C CG  . MET A 79  ? 0.1961 0.2220 0.1817 -0.0268 0.0154  -0.0104 91  MET A CG  
474  S SD  . MET A 79  ? 0.2122 0.2384 0.1992 -0.0247 0.0132  -0.0062 91  MET A SD  
475  C CE  . MET A 79  ? 0.2235 0.2525 0.2112 -0.0264 0.0145  -0.0132 91  MET A CE  
476  N N   . SER A 80  ? 0.2070 0.1993 0.1936 -0.0263 0.0185  -0.0149 92  SER A N   
477  C CA  . SER A 80  ? 0.1957 0.1743 0.1828 -0.0253 0.0187  -0.0155 92  SER A CA  
478  C C   . SER A 80  ? 0.1732 0.1470 0.1611 -0.0232 0.0172  -0.0112 92  SER A C   
479  O O   . SER A 80  ? 0.1790 0.1586 0.1674 -0.0222 0.0156  -0.0065 92  SER A O   
480  C CB  . SER A 80  ? 0.2055 0.1783 0.1930 -0.0247 0.0187  -0.0144 92  SER A CB  
481  O OG  . SER A 80  ? 0.2046 0.1796 0.1929 -0.0234 0.0172  -0.0081 92  SER A OG  
482  N N   . GLY A 81  ? 0.1783 0.1417 0.1662 -0.0226 0.0176  -0.0129 93  GLY A N   
483  C CA  . GLY A 81  ? 0.1713 0.1290 0.1600 -0.0203 0.0162  -0.0092 93  GLY A CA  
484  C C   . GLY A 81  ? 0.1580 0.1215 0.1472 -0.0201 0.0158  -0.0091 93  GLY A C   
485  O O   . GLY A 81  ? 0.1310 0.0916 0.1212 -0.0179 0.0144  -0.0058 93  GLY A O   
486  N N   . SER A 82  ? 0.1812 0.1532 0.1700 -0.0223 0.0169  -0.0129 94  SER A N   
487  C CA  . SER A 82  ? 0.1880 0.1660 0.1776 -0.0222 0.0166  -0.0132 94  SER A CA  
488  C C   . SER A 82  ? 0.1907 0.1605 0.1805 -0.0220 0.0176  -0.0154 94  SER A C   
489  O O   . SER A 82  ? 0.1923 0.1526 0.1811 -0.0225 0.0188  -0.0176 94  SER A O   
490  C CB  . SER A 82  ? 0.1743 0.1632 0.1637 -0.0247 0.0175  -0.0171 94  SER A CB  
491  O OG  . SER A 82  ? 0.1914 0.1901 0.1804 -0.0247 0.0164  -0.0146 94  SER A OG  
492  N N   . CYS A 83  ? 0.1792 0.1531 0.1703 -0.0212 0.0171  -0.0148 95  CYS A N   
493  C CA  . CYS A 83  ? 0.1977 0.1654 0.1892 -0.0207 0.0180  -0.0162 95  CYS A CA  
494  C C   . CYS A 83  ? 0.2063 0.1818 0.1989 -0.0229 0.0192  -0.0201 95  CYS A C   
495  O O   . CYS A 83  ? 0.2042 0.1898 0.1982 -0.0226 0.0180  -0.0192 95  CYS A O   
496  C CB  . CYS A 83  ? 0.1647 0.1301 0.1577 -0.0173 0.0160  -0.0118 95  CYS A CB  
497  S SG  . CYS A 83  ? 0.2505 0.2072 0.2434 -0.0163 0.0173  -0.0136 95  CYS A SG  
498  N N   . ALA A 84  ? 0.2119 0.1826 0.2037 -0.0252 0.0214  -0.0244 96  ALA A N   
499  C CA  . ALA A 84  ? 0.1781 0.1560 0.1712 -0.0279 0.0228  -0.0286 96  ALA A CA  
500  C C   . ALA A 84  ? 0.2562 0.2287 0.2496 -0.0287 0.0246  -0.0306 96  ALA A C   
501  O O   . ALA A 84  ? 0.2633 0.2250 0.2551 -0.0279 0.0253  -0.0299 96  ALA A O   
502  C CB  . ALA A 84  ? 0.2142 0.1941 0.2064 -0.0310 0.0239  -0.0328 96  ALA A CB  
503  N N   . VAL A 85  ? 0.2704 0.2509 0.2660 -0.0304 0.0253  -0.0330 97  VAL A N   
504  C CA  . VAL A 85  ? 0.2423 0.2199 0.2385 -0.0318 0.0273  -0.0353 97  VAL A CA  
505  C C   . VAL A 85  ? 0.2636 0.2482 0.2616 -0.0357 0.0287  -0.0400 97  VAL A C   
506  O O   . VAL A 85  ? 0.2750 0.2690 0.2741 -0.0366 0.0277  -0.0413 97  VAL A O   
507  C CB  . VAL A 85  ? 0.2916 0.2724 0.2898 -0.0292 0.0266  -0.0330 97  VAL A CB  
508  C CG1 . VAL A 85  ? 0.2836 0.2569 0.2805 -0.0254 0.0252  -0.0287 97  VAL A CG1 
509  C CG2 . VAL A 85  ? 0.2918 0.2859 0.2929 -0.0286 0.0248  -0.0326 97  VAL A CG2 
510  N N   . CYS A 86  ? 0.2844 0.2646 0.2826 -0.0382 0.0310  -0.0426 98  CYS A N   
511  C CA  . CYS A 86  ? 0.2405 0.2274 0.2411 -0.0420 0.0323  -0.0470 98  CYS A CA  
512  C C   . CYS A 86  ? 0.2708 0.2594 0.2734 -0.0423 0.0337  -0.0471 98  CYS A C   
513  O O   . CYS A 86  ? 0.2863 0.2659 0.2872 -0.0423 0.0353  -0.0463 98  CYS A O   
514  C CB  . CYS A 86  ? 0.2712 0.2511 0.2705 -0.0455 0.0339  -0.0505 98  CYS A CB  
515  S SG  . CYS A 86  ? 0.3895 0.3764 0.3923 -0.0504 0.0355  -0.0560 98  CYS A SG  
516  N N   . VAL A 87  ? 0.2960 0.2964 0.3022 -0.0425 0.0332  -0.0481 99  VAL A N   
517  C CA  . VAL A 87  ? 0.2857 0.2898 0.2946 -0.0429 0.0345  -0.0487 99  VAL A CA  
518  C C   . VAL A 87  ? 0.3368 0.3502 0.3493 -0.0468 0.0354  -0.0531 99  VAL A C   
519  O O   . VAL A 87  ? 0.2855 0.3093 0.3001 -0.0465 0.0336  -0.0541 99  VAL A O   
520  C CB  . VAL A 87  ? 0.2938 0.3036 0.3043 -0.0385 0.0326  -0.0454 99  VAL A CB  
521  C CG1 . VAL A 87  ? 0.3207 0.3326 0.3337 -0.0386 0.0343  -0.0461 99  VAL A CG1 
522  C CG2 . VAL A 87  ? 0.2802 0.2820 0.2876 -0.0346 0.0309  -0.0411 99  VAL A CG2 
523  N N   . ASP A 88  ? 0.3833 0.3932 0.3966 -0.0505 0.0381  -0.0557 100 ASP A N   
524  C CA  . ASP A 88  ? 0.3516 0.3695 0.3688 -0.0548 0.0391  -0.0602 100 ASP A CA  
525  C C   . ASP A 88  ? 0.3287 0.3510 0.3459 -0.0560 0.0374  -0.0628 100 ASP A C   
526  O O   . ASP A 88  ? 0.3467 0.3807 0.3672 -0.0566 0.0361  -0.0650 100 ASP A O   
527  C CB  . ASP A 88  ? 0.3605 0.3902 0.3822 -0.0541 0.0389  -0.0607 100 ASP A CB  
528  C CG  . ASP A 88  ? 0.4316 0.4581 0.4536 -0.0532 0.0409  -0.0589 100 ASP A CG  
529  O OD1 . ASP A 88  ? 0.4591 0.4750 0.4773 -0.0513 0.0415  -0.0561 100 ASP A OD1 
530  O OD2 . ASP A 88  ? 0.5339 0.5688 0.5602 -0.0544 0.0419  -0.0606 100 ASP A OD2 
531  N N   . ARG A 89  ? 0.3175 0.3307 0.3312 -0.0562 0.0372  -0.0626 101 ARG A N   
532  C CA  . ARG A 89  ? 0.3795 0.3955 0.3928 -0.0573 0.0359  -0.0654 101 ARG A CA  
533  C C   . ARG A 89  ? 0.3389 0.3655 0.3525 -0.0544 0.0332  -0.0640 101 ARG A C   
534  O O   . ARG A 89  ? 0.3561 0.3886 0.3700 -0.0555 0.0320  -0.0668 101 ARG A O   
535  C CB  . ARG A 89  ? 0.4048 0.4243 0.4213 -0.0622 0.0369  -0.0708 101 ARG A CB  
536  C CG  . ARG A 89  ? 0.4546 0.4626 0.4703 -0.0655 0.0394  -0.0721 101 ARG A CG  
537  C CD  . ARG A 89  ? 0.4427 0.4540 0.4621 -0.0702 0.0402  -0.0771 101 ARG A CD  
538  N NE  . ARG A 89  ? 0.4690 0.4851 0.4888 -0.0698 0.0383  -0.0797 101 ARG A NE  
539  C CZ  . ARG A 89  ? 0.4563 0.4658 0.4729 -0.0676 0.0373  -0.0783 101 ARG A CZ  
540  N NH1 . ARG A 89  ? 0.4988 0.4968 0.5117 -0.0652 0.0377  -0.0741 101 ARG A NH1 
541  N NH2 . ARG A 89  ? 0.4468 0.4620 0.4644 -0.0676 0.0358  -0.0813 101 ARG A NH2 
542  N N   . VAL A 90  ? 0.2906 0.3197 0.3040 -0.0506 0.0320  -0.0598 102 VAL A N   
543  C CA  . VAL A 90  ? 0.2997 0.3362 0.3124 -0.0475 0.0293  -0.0572 102 VAL A CA  
544  C C   . VAL A 90  ? 0.2871 0.3144 0.2959 -0.0444 0.0286  -0.0528 102 VAL A C   
545  O O   . VAL A 90  ? 0.2793 0.2984 0.2871 -0.0426 0.0293  -0.0500 102 VAL A O   
546  C CB  . VAL A 90  ? 0.3083 0.3546 0.3241 -0.0453 0.0279  -0.0555 102 VAL A CB  
547  C CG1 . VAL A 90  ? 0.2659 0.3193 0.2807 -0.0421 0.0249  -0.0524 102 VAL A CG1 
548  C CG2 . VAL A 90  ? 0.2959 0.3516 0.3160 -0.0485 0.0287  -0.0602 102 VAL A CG2 
549  N N   . LEU A 91  ? 0.2791 0.3079 0.2859 -0.0437 0.0272  -0.0525 103 LEU A N   
550  C CA  . LEU A 91  ? 0.2719 0.2925 0.2754 -0.0412 0.0265  -0.0486 103 LEU A CA  
551  C C   . LEU A 91  ? 0.2759 0.3027 0.2792 -0.0376 0.0240  -0.0439 103 LEU A C   
552  O O   . LEU A 91  ? 0.2575 0.2956 0.2620 -0.0375 0.0224  -0.0443 103 LEU A O   
553  C CB  . LEU A 91  ? 0.2344 0.2529 0.2359 -0.0427 0.0266  -0.0510 103 LEU A CB  
554  C CG  . LEU A 91  ? 0.3298 0.3461 0.3320 -0.0467 0.0283  -0.0568 103 LEU A CG  
555  C CD1 . LEU A 91  ? 0.3533 0.3663 0.3533 -0.0471 0.0281  -0.0584 103 LEU A CD1 
556  C CD2 . LEU A 91  ? 0.3509 0.3568 0.3533 -0.0481 0.0305  -0.0573 103 LEU A CD2 
557  N N   . TYR A 92  ? 0.2544 0.2739 0.2566 -0.0345 0.0234  -0.0393 104 TYR A N   
558  C CA  . TYR A 92  ? 0.2403 0.2640 0.2424 -0.0310 0.0208  -0.0344 104 TYR A CA  
559  C C   . TYR A 92  ? 0.2420 0.2576 0.2413 -0.0294 0.0202  -0.0310 104 TYR A C   
560  O O   . TYR A 92  ? 0.2316 0.2362 0.2295 -0.0295 0.0215  -0.0312 104 TYR A O   
561  C CB  . TYR A 92  ? 0.2098 0.2328 0.2139 -0.0284 0.0201  -0.0318 104 TYR A CB  
562  C CG  . TYR A 92  ? 0.2496 0.2803 0.2571 -0.0298 0.0208  -0.0351 104 TYR A CG  
563  C CD1 . TYR A 92  ? 0.2553 0.2986 0.2649 -0.0298 0.0191  -0.0356 104 TYR A CD1 
564  C CD2 . TYR A 92  ? 0.2671 0.2925 0.2756 -0.0313 0.0233  -0.0374 104 TYR A CD2 
565  C CE1 . TYR A 92  ? 0.2021 0.2528 0.2153 -0.0311 0.0197  -0.0388 104 TYR A CE1 
566  C CE2 . TYR A 92  ? 0.2699 0.3027 0.2818 -0.0328 0.0241  -0.0404 104 TYR A CE2 
567  C CZ  . TYR A 92  ? 0.2801 0.3256 0.2946 -0.0326 0.0223  -0.0412 104 TYR A CZ  
568  O OH  . TYR A 92  ? 0.2951 0.3481 0.3134 -0.0341 0.0231  -0.0443 104 TYR A OH  
569  N N   . LEU A 93  ? 0.1920 0.2133 0.1904 -0.0280 0.0181  -0.0279 105 LEU A N   
570  C CA  . LEU A 93  ? 0.1557 0.1714 0.1518 -0.0269 0.0175  -0.0248 105 LEU A CA  
571  C C   . LEU A 93  ? 0.1340 0.1517 0.1306 -0.0236 0.0149  -0.0186 105 LEU A C   
572  O O   . LEU A 93  ? 0.1894 0.2173 0.1868 -0.0229 0.0131  -0.0172 105 LEU A O   
573  C CB  . LEU A 93  ? 0.1751 0.1963 0.1697 -0.0290 0.0179  -0.0272 105 LEU A CB  
574  C CG  . LEU A 93  ? 0.2038 0.2181 0.1963 -0.0285 0.0180  -0.0252 105 LEU A CG  
575  C CD1 . LEU A 93  ? 0.2322 0.2371 0.2240 -0.0303 0.0203  -0.0295 105 LEU A CD1 
576  C CD2 . LEU A 93  ? 0.2726 0.2958 0.2638 -0.0292 0.0174  -0.0250 105 LEU A CD2 
577  N N   . PHE A 94  ? 0.1378 0.1457 0.1337 -0.0214 0.0143  -0.0151 106 PHE A N   
578  C CA  . PHE A 94  ? 0.1551 0.1636 0.1517 -0.0184 0.0116  -0.0090 106 PHE A CA  
579  C C   . PHE A 94  ? 0.1627 0.1651 0.1576 -0.0179 0.0112  -0.0059 106 PHE A C   
580  O O   . PHE A 94  ? 0.1812 0.1740 0.1751 -0.0184 0.0127  -0.0074 106 PHE A O   
581  C CB  . PHE A 94  ? 0.1603 0.1633 0.1588 -0.0156 0.0106  -0.0070 106 PHE A CB  
582  C CG  . PHE A 94  ? 0.1563 0.1577 0.1557 -0.0124 0.0076  -0.0009 106 PHE A CG  
583  C CD1 . PHE A 94  ? 0.1708 0.1814 0.1715 -0.0111 0.0051  0.0023  106 PHE A CD1 
584  C CD2 . PHE A 94  ? 0.1579 0.1485 0.1568 -0.0108 0.0072  0.0018  106 PHE A CD2 
585  C CE1 . PHE A 94  ? 0.2017 0.2106 0.2034 -0.0083 0.0021  0.0082  106 PHE A CE1 
586  C CE2 . PHE A 94  ? 0.1983 0.1872 0.1983 -0.0081 0.0043  0.0075  106 PHE A CE2 
587  C CZ  . PHE A 94  ? 0.2297 0.2276 0.2312 -0.0069 0.0018  0.0108  106 PHE A CZ  
588  N N   . GLY A 95  ? 0.1833 0.1913 0.1781 -0.0169 0.0091  -0.0013 107 GLY A N   
589  C CA  . GLY A 95  ? 0.1685 0.1709 0.1625 -0.0161 0.0084  0.0026  107 GLY A CA  
590  C C   . GLY A 95  ? 0.1861 0.1870 0.1780 -0.0185 0.0106  -0.0004 107 GLY A C   
591  O O   . GLY A 95  ? 0.2154 0.2216 0.2064 -0.0209 0.0123  -0.0053 107 GLY A O   
592  N N   . GLY A 96  ? 0.1527 0.1467 0.1444 -0.0177 0.0102  0.0024  108 GLY A N   
593  C CA  . GLY A 96  ? 0.1986 0.1914 0.1889 -0.0196 0.0119  0.0002  108 GLY A CA  
594  C C   . GLY A 96  ? 0.1623 0.1592 0.1523 -0.0194 0.0107  0.0051  108 GLY A C   
595  O O   . GLY A 96  ? 0.1790 0.1786 0.1699 -0.0178 0.0085  0.0107  108 GLY A O   
596  N N   . HIS A 97  ? 0.1829 0.1801 0.1718 -0.0210 0.0123  0.0030  109 HIS A N   
597  C CA  . HIS A 97  ? 0.2065 0.2082 0.1951 -0.0213 0.0118  0.0069  109 HIS A CA  
598  C C   . HIS A 97  ? 0.2338 0.2456 0.2205 -0.0237 0.0135  0.0029  109 HIS A C   
599  O O   . HIS A 97  ? 0.2177 0.2268 0.2040 -0.0250 0.0154  -0.0029 109 HIS A O   
600  C CB  . HIS A 97  ? 0.1801 0.1713 0.1697 -0.0206 0.0120  0.0082  109 HIS A CB  
601  C CG  . HIS A 97  ? 0.1959 0.1914 0.1857 -0.0212 0.0116  0.0124  109 HIS A CG  
602  N ND1 . HIS A 97  ? 0.2075 0.2090 0.1963 -0.0231 0.0134  0.0096  109 HIS A ND1 
603  C CD2 . HIS A 97  ? 0.2347 0.2297 0.2260 -0.0201 0.0097  0.0193  109 HIS A CD2 
604  C CE1 . HIS A 97  ? 0.1896 0.1945 0.1790 -0.0233 0.0129  0.0146  109 HIS A CE1 
605  N NE2 . HIS A 97  ? 0.2647 0.2655 0.2555 -0.0216 0.0105  0.0207  109 HIS A NE2 
606  N N   . HIS A 98  ? 0.1812 0.2048 0.1668 -0.0243 0.0127  0.0057  110 HIS A N   
607  C CA  . HIS A 98  ? 0.1633 0.1977 0.1469 -0.0264 0.0142  0.0022  110 HIS A CA  
608  C C   . HIS A 98  ? 0.2185 0.2571 0.2016 -0.0268 0.0142  0.0067  110 HIS A C   
609  O O   . HIS A 98  ? 0.2225 0.2541 0.2071 -0.0257 0.0133  0.0116  110 HIS A O   
610  C CB  . HIS A 98  ? 0.1798 0.2256 0.1621 -0.0269 0.0136  0.0011  110 HIS A CB  
611  C CG  . HIS A 98  ? 0.2202 0.2699 0.2027 -0.0254 0.0110  0.0080  110 HIS A CG  
612  N ND1 . HIS A 98  ? 0.2291 0.2848 0.2106 -0.0253 0.0099  0.0141  110 HIS A ND1 
613  C CD2 . HIS A 98  ? 0.2192 0.2677 0.2030 -0.0238 0.0092  0.0097  110 HIS A CD2 
614  C CE1 . HIS A 98  ? 0.2465 0.3040 0.2285 -0.0238 0.0073  0.0194  110 HIS A CE1 
615  N NE2 . HIS A 98  ? 0.1999 0.2531 0.1834 -0.0227 0.0068  0.0167  110 HIS A NE2 
616  N N   . SER A 99  ? 0.2802 0.3303 0.2612 -0.0284 0.0154  0.0045  111 SER A N   
617  C CA  . SER A 99  ? 0.2539 0.3089 0.2343 -0.0292 0.0160  0.0079  111 SER A CA  
618  C C   . SER A 99  ? 0.2803 0.3368 0.2610 -0.0283 0.0138  0.0170  111 SER A C   
619  O O   . SER A 99  ? 0.2862 0.3405 0.2679 -0.0285 0.0139  0.0212  111 SER A O   
620  C CB  . SER A 99  ? 0.2823 0.3510 0.2601 -0.0310 0.0175  0.0039  111 SER A CB  
621  O OG  . SER A 99  ? 0.3212 0.4000 0.2970 -0.0311 0.0163  0.0045  111 SER A OG  
622  N N   . ARG A 100 ? 0.2074 0.2674 0.1875 -0.0274 0.0118  0.0202  112 ARG A N   
623  C CA  . ARG A 100 ? 0.2044 0.2658 0.1848 -0.0265 0.0093  0.0289  112 ARG A CA  
624  C C   . ARG A 100 ? 0.2299 0.2792 0.2133 -0.0241 0.0071  0.0323  112 ARG A C   
625  O O   . ARG A 100 ? 0.2982 0.3482 0.2822 -0.0230 0.0045  0.0390  112 ARG A O   
626  C CB  . ARG A 100 ? 0.2681 0.3425 0.2459 -0.0267 0.0080  0.0308  112 ARG A CB  
627  N N   . GLY A 101 ? 0.2463 0.2849 0.2315 -0.0234 0.0079  0.0277  113 GLY A N   
628  C CA  . GLY A 101 ? 0.1906 0.2175 0.1785 -0.0211 0.0060  0.0308  113 GLY A CA  
629  C C   . GLY A 101 ? 0.1968 0.2188 0.1854 -0.0199 0.0060  0.0261  113 GLY A C   
630  O O   . GLY A 101 ? 0.1984 0.2234 0.1857 -0.0212 0.0079  0.0197  113 GLY A O   
631  N N   . ASN A 102 ? 0.2079 0.2220 0.1988 -0.0176 0.0039  0.0292  114 ASN A N   
632  C CA  . ASN A 102 ? 0.2240 0.2335 0.2157 -0.0163 0.0039  0.0254  114 ASN A CA  
633  C C   . ASN A 102 ? 0.2401 0.2592 0.2314 -0.0160 0.0026  0.0257  114 ASN A C   
634  O O   . ASN A 102 ? 0.2824 0.3103 0.2728 -0.0161 0.0010  0.0299  114 ASN A O   
635  C CB  . ASN A 102 ? 0.1987 0.1964 0.1930 -0.0137 0.0021  0.0282  114 ASN A CB  
636  C CG  . ASN A 102 ? 0.2486 0.2358 0.2435 -0.0138 0.0033  0.0269  114 ASN A CG  
637  O OD1 . ASN A 102 ? 0.2596 0.2422 0.2561 -0.0130 0.0019  0.0315  114 ASN A OD1 
638  N ND2 . ASN A 102 ? 0.2148 0.1982 0.2086 -0.0148 0.0057  0.0206  114 ASN A ND2 
639  N N   . THR A 103 ? 0.2006 0.2179 0.1925 -0.0155 0.0031  0.0211  115 THR A N   
640  C CA  . THR A 103 ? 0.1932 0.2192 0.1852 -0.0150 0.0019  0.0206  115 THR A CA  
641  C C   . THR A 103 ? 0.1786 0.1982 0.1731 -0.0129 0.0012  0.0193  115 THR A C   
642  O O   . THR A 103 ? 0.1814 0.1906 0.1767 -0.0124 0.0023  0.0174  115 THR A O   
643  C CB  . THR A 103 ? 0.2229 0.2583 0.2129 -0.0176 0.0040  0.0148  115 THR A CB  
644  O OG1 . THR A 103 ? 0.2484 0.2929 0.2389 -0.0171 0.0025  0.0146  115 THR A OG1 
645  C CG2 . THR A 103 ? 0.1913 0.2203 0.1815 -0.0189 0.0067  0.0081  115 THR A CG2 
646  N N   . ASN A 104 ? 0.2062 0.2325 0.2018 -0.0116 -0.0008 0.0206  116 ASN A N   
647  C CA  . ASN A 104 ? 0.2307 0.2542 0.2287 -0.0099 -0.0012 0.0183  116 ASN A CA  
648  C C   . ASN A 104 ? 0.1848 0.2188 0.1828 -0.0111 -0.0006 0.0141  116 ASN A C   
649  O O   . ASN A 104 ? 0.2311 0.2666 0.2313 -0.0094 -0.0018 0.0135  116 ASN A O   
650  C CB  . ASN A 104 ? 0.2311 0.2511 0.2318 -0.0064 -0.0046 0.0237  116 ASN A CB  
651  C CG  . ASN A 104 ? 0.2486 0.2778 0.2493 -0.0055 -0.0077 0.0290  116 ASN A CG  
652  O OD1 . ASN A 104 ? 0.2685 0.3081 0.2672 -0.0074 -0.0073 0.0281  116 ASN A OD1 
653  N ND2 . ASN A 104 ? 0.2313 0.2565 0.2343 -0.0026 -0.0109 0.0345  116 ASN A ND2 
654  N N   . LYS A 105 ? 0.2408 0.2822 0.2363 -0.0139 0.0010  0.0109  117 LYS A N   
655  C CA  . LYS A 105 ? 0.2831 0.3341 0.2788 -0.0154 0.0017  0.0062  117 LYS A CA  
656  C C   . LYS A 105 ? 0.2441 0.2899 0.2409 -0.0167 0.0043  0.0000  117 LYS A C   
657  O O   . LYS A 105 ? 0.1873 0.2232 0.1836 -0.0173 0.0062  -0.0016 117 LYS A O   
658  C CB  . LYS A 105 ? 0.2402 0.3009 0.2331 -0.0179 0.0025  0.0045  117 LYS A CB  
659  C CG  . LYS A 105 ? 0.2420 0.3102 0.2333 -0.0171 0.0000  0.0106  117 LYS A CG  
660  C CD  . LYS A 105 ? 0.2700 0.3443 0.2630 -0.0147 -0.0032 0.0140  117 LYS A CD  
661  C CE  . LYS A 105 ? 0.3463 0.4266 0.3374 -0.0139 -0.0059 0.0209  117 LYS A CE  
662  N NZ  . LYS A 105 ? 0.3465 0.4290 0.3398 -0.0109 -0.0097 0.0259  117 LYS A NZ  
663  N N   . PHE A 106 ? 0.1908 0.2437 0.1893 -0.0172 0.0043  -0.0035 118 PHE A N   
664  C CA  . PHE A 106 ? 0.2320 0.2814 0.2321 -0.0185 0.0066  -0.0090 118 PHE A CA  
665  C C   . PHE A 106 ? 0.2205 0.2791 0.2203 -0.0216 0.0080  -0.0146 118 PHE A C   
666  O O   . PHE A 106 ? 0.2264 0.2961 0.2266 -0.0215 0.0063  -0.0144 118 PHE A O   
667  C CB  . PHE A 106 ? 0.2001 0.2492 0.2035 -0.0160 0.0053  -0.0079 118 PHE A CB  
668  C CG  . PHE A 106 ? 0.2204 0.2656 0.2254 -0.0173 0.0078  -0.0129 118 PHE A CG  
669  C CD1 . PHE A 106 ? 0.2137 0.2670 0.2202 -0.0196 0.0089  -0.0179 118 PHE A CD1 
670  C CD2 . PHE A 106 ? 0.2111 0.2446 0.2162 -0.0162 0.0090  -0.0126 118 PHE A CD2 
671  C CE1 . PHE A 106 ? 0.2426 0.2926 0.2507 -0.0211 0.0113  -0.0221 118 PHE A CE1 
672  C CE2 . PHE A 106 ? 0.2575 0.2878 0.2638 -0.0176 0.0114  -0.0168 118 PHE A CE2 
673  C CZ  . PHE A 106 ? 0.2480 0.2864 0.2559 -0.0201 0.0126  -0.0215 118 PHE A CZ  
674  N N   . TYR A 107 ? 0.1851 0.2389 0.1841 -0.0243 0.0108  -0.0195 119 TYR A N   
675  C CA  . TYR A 107 ? 0.2228 0.2844 0.2220 -0.0274 0.0121  -0.0254 119 TYR A CA  
676  C C   . TYR A 107 ? 0.2256 0.2831 0.2270 -0.0293 0.0143  -0.0303 119 TYR A C   
677  O O   . TYR A 107 ? 0.1972 0.2442 0.1989 -0.0287 0.0155  -0.0297 119 TYR A O   
678  C CB  . TYR A 107 ? 0.2142 0.2755 0.2106 -0.0295 0.0133  -0.0276 119 TYR A CB  
679  C CG  . TYR A 107 ? 0.1911 0.2568 0.1851 -0.0282 0.0117  -0.0231 119 TYR A CG  
680  C CD1 . TYR A 107 ? 0.2213 0.2789 0.2142 -0.0263 0.0111  -0.0179 119 TYR A CD1 
681  C CD2 . TYR A 107 ? 0.1788 0.2567 0.1715 -0.0292 0.0107  -0.0241 119 TYR A CD2 
682  C CE1 . TYR A 107 ? 0.2118 0.2733 0.2027 -0.0255 0.0098  -0.0135 119 TYR A CE1 
683  C CE2 . TYR A 107 ? 0.2464 0.3284 0.2365 -0.0282 0.0095  -0.0197 119 TYR A CE2 
684  C CZ  . TYR A 107 ? 0.2148 0.2885 0.2042 -0.0265 0.0091  -0.0142 119 TYR A CZ  
685  O OH  . TYR A 107 ? 0.2295 0.3072 0.2165 -0.0258 0.0079  -0.0094 119 TYR A OH  
686  N N   . MET A 108 ? 0.2520 0.3180 0.2548 -0.0317 0.0147  -0.0351 120 MET A N   
687  C CA  . MET A 108 ? 0.2027 0.2665 0.2079 -0.0342 0.0169  -0.0402 120 MET A CA  
688  C C   . MET A 108 ? 0.2303 0.2976 0.2349 -0.0377 0.0182  -0.0460 120 MET A C   
689  O O   . MET A 108 ? 0.2018 0.2788 0.2056 -0.0381 0.0168  -0.0468 120 MET A O   
690  C CB  . MET A 108 ? 0.2405 0.3122 0.2493 -0.0337 0.0160  -0.0409 120 MET A CB  
691  C CG  . MET A 108 ? 0.2595 0.3314 0.2712 -0.0370 0.0183  -0.0466 120 MET A CG  
692  S SD  . MET A 108 ? 0.3460 0.4276 0.3626 -0.0366 0.0176  -0.0478 120 MET A SD  
693  C CE  . MET A 108 ? 0.2966 0.3792 0.3128 -0.0313 0.0145  -0.0408 120 MET A CE  
694  N N   . LEU A 109 ? 0.2390 0.2983 0.2441 -0.0403 0.0206  -0.0498 121 LEU A N   
695  C CA  . LEU A 109 ? 0.2608 0.3233 0.2664 -0.0438 0.0216  -0.0559 121 LEU A CA  
696  C C   . LEU A 109 ? 0.3167 0.3762 0.3254 -0.0466 0.0236  -0.0598 121 LEU A C   
697  O O   . LEU A 109 ? 0.2923 0.3406 0.3006 -0.0471 0.0254  -0.0593 121 LEU A O   
698  C CB  . LEU A 109 ? 0.2674 0.3226 0.2702 -0.0446 0.0225  -0.0571 121 LEU A CB  
699  C CG  . LEU A 109 ? 0.3284 0.3901 0.3319 -0.0476 0.0228  -0.0635 121 LEU A CG  
700  C CD1 . LEU A 109 ? 0.3128 0.3787 0.3136 -0.0468 0.0219  -0.0634 121 LEU A CD1 
701  C CD2 . LEU A 109 ? 0.3772 0.4299 0.3820 -0.0507 0.0249  -0.0681 121 LEU A CD2 
702  N N   . ASP A 110 ? 0.3266 0.3963 0.3383 -0.0485 0.0232  -0.0636 122 ASP A N   
703  C CA  . ASP A 110 ? 0.3460 0.4143 0.3613 -0.0516 0.0250  -0.0675 122 ASP A CA  
704  C C   . ASP A 110 ? 0.3147 0.3779 0.3298 -0.0552 0.0265  -0.0726 122 ASP A C   
705  O O   . ASP A 110 ? 0.3356 0.4057 0.3510 -0.0566 0.0256  -0.0765 122 ASP A O   
706  C CB  . ASP A 110 ? 0.3614 0.4429 0.3805 -0.0522 0.0238  -0.0695 122 ASP A CB  
707  C CG  . ASP A 110 ? 0.4041 0.4847 0.4273 -0.0552 0.0258  -0.0727 122 ASP A CG  
708  O OD1 . ASP A 110 ? 0.4319 0.5016 0.4546 -0.0571 0.0282  -0.0733 122 ASP A OD1 
709  O OD2 . ASP A 110 ? 0.4527 0.5438 0.4797 -0.0558 0.0250  -0.0745 122 ASP A OD2 
710  N N   . SER A 111 ? 0.4062 0.4569 0.4206 -0.0565 0.0286  -0.0726 123 SER A N   
711  C CA  . SER A 111 ? 0.3917 0.4361 0.4061 -0.0598 0.0298  -0.0772 123 SER A CA  
712  C C   . SER A 111 ? 0.4392 0.4842 0.4576 -0.0639 0.0313  -0.0814 123 SER A C   
713  O O   . SER A 111 ? 0.4748 0.5111 0.4934 -0.0668 0.0328  -0.0841 123 SER A O   
714  C CB  . SER A 111 ? 0.4177 0.4476 0.4286 -0.0589 0.0309  -0.0747 123 SER A CB  
715  O OG  . SER A 111 ? 0.4111 0.4329 0.4224 -0.0593 0.0327  -0.0727 123 SER A OG  
716  N N   . ARG A 112 ? 0.4166 0.4719 0.4385 -0.0644 0.0309  -0.0821 124 ARG A N   
717  C CA  . ARG A 112 ? 0.4884 0.5450 0.5147 -0.0684 0.0325  -0.0859 124 ARG A CA  
718  C C   . ARG A 112 ? 0.5536 0.6183 0.5829 -0.0716 0.0315  -0.0922 124 ARG A C   
719  O O   . ARG A 112 ? 0.6253 0.6840 0.6556 -0.0739 0.0327  -0.0946 124 ARG A O   
720  C CB  . ARG A 112 ? 0.4541 0.5176 0.4833 -0.0674 0.0327  -0.0837 124 ARG A CB  
721  C CG  . ARG A 112 ? 0.4430 0.4972 0.4705 -0.0659 0.0345  -0.0791 124 ARG A CG  
722  C CD  . ARG A 112 ? 0.4331 0.4952 0.4637 -0.0645 0.0345  -0.0774 124 ARG A CD  
723  N NE  . ARG A 112 ? 0.3990 0.4697 0.4290 -0.0603 0.0317  -0.0747 124 ARG A NE  
724  C CZ  . ARG A 112 ? 0.3608 0.4394 0.3934 -0.0580 0.0308  -0.0729 124 ARG A CZ  
725  N NH1 . ARG A 112 ? 0.3551 0.4347 0.3911 -0.0593 0.0326  -0.0736 124 ARG A NH1 
726  N NH2 . ARG A 112 ? 0.3617 0.4476 0.3934 -0.0543 0.0279  -0.0704 124 ARG A NH2 
727  N N   . SER A 113 ? 0.5884 0.6661 0.6186 -0.0701 0.0293  -0.0932 125 SER A N   
728  C CA  . SER A 113 ? 0.6385 0.7252 0.6718 -0.0728 0.0282  -0.0994 125 SER A CA  
729  C C   . SER A 113 ? 0.6644 0.7509 0.6944 -0.0718 0.0269  -0.1013 125 SER A C   
730  O O   . SER A 113 ? 0.6945 0.7748 0.7249 -0.0720 0.0277  -0.1025 125 SER A O   
731  C CB  . SER A 113 ? 0.6711 0.7729 0.7073 -0.0719 0.0263  -0.0999 125 SER A CB  
732  O OG  . SER A 113 ? 0.6680 0.7738 0.7010 -0.0673 0.0247  -0.0946 125 SER A OG  
733  N N   . VAL A 117 ? 0.5109 0.6255 0.5294 -0.0641 0.0200  -0.1077 129 VAL A N   
734  C CA  . VAL A 117 ? 0.4571 0.5657 0.4708 -0.0623 0.0203  -0.1045 129 VAL A CA  
735  C C   . VAL A 117 ? 0.4545 0.5611 0.4662 -0.0605 0.0202  -0.0979 129 VAL A C   
736  O O   . VAL A 117 ? 0.4391 0.5547 0.4517 -0.0595 0.0190  -0.0957 129 VAL A O   
737  C CB  . VAL A 117 ? 0.5412 0.6591 0.5518 -0.0605 0.0190  -0.1055 129 VAL A CB  
738  C CG1 . VAL A 117 ? 0.5193 0.6532 0.5287 -0.0601 0.0167  -0.1059 129 VAL A CG1 
739  C CG2 . VAL A 117 ? 0.3934 0.5055 0.3991 -0.0588 0.0194  -0.1021 129 VAL A CG2 
740  N N   . LEU A 118 ? 0.3728 0.4670 0.3825 -0.0593 0.0216  -0.0938 130 LEU A N   
741  C CA  . LEU A 118 ? 0.3642 0.4541 0.3729 -0.0569 0.0218  -0.0867 130 LEU A CA  
742  C C   . LEU A 118 ? 0.3531 0.4513 0.3587 -0.0536 0.0200  -0.0816 130 LEU A C   
743  O O   . LEU A 118 ? 0.3290 0.4291 0.3316 -0.0526 0.0196  -0.0815 130 LEU A O   
744  C CB  . LEU A 118 ? 0.3750 0.4496 0.3823 -0.0565 0.0235  -0.0840 130 LEU A CB  
745  C CG  . LEU A 118 ? 0.4029 0.4668 0.4124 -0.0595 0.0253  -0.0877 130 LEU A CG  
746  C CD1 . LEU A 118 ? 0.4159 0.4655 0.4232 -0.0582 0.0266  -0.0836 130 LEU A CD1 
747  C CD2 . LEU A 118 ? 0.3707 0.4373 0.3842 -0.0617 0.0258  -0.0891 130 LEU A CD2 
748  N N   . GLN A 119 ? 0.3499 0.4525 0.3562 -0.0519 0.0189  -0.0773 131 GLN A N   
749  C CA  . GLN A 119 ? 0.3119 0.4222 0.3155 -0.0488 0.0170  -0.0720 131 GLN A CA  
750  C C   . GLN A 119 ? 0.2993 0.4023 0.3024 -0.0461 0.0169  -0.0649 131 GLN A C   
751  O O   . GLN A 119 ? 0.2800 0.3791 0.2857 -0.0461 0.0174  -0.0641 131 GLN A O   
752  C CB  . GLN A 119 ? 0.3451 0.4700 0.3503 -0.0488 0.0149  -0.0735 131 GLN A CB  
753  C CG  . GLN A 119 ? 0.3766 0.5103 0.3820 -0.0510 0.0145  -0.0804 131 GLN A CG  
754  C CD  . GLN A 119 ? 0.4093 0.5583 0.4141 -0.0499 0.0119  -0.0802 131 GLN A CD  
755  O OE1 . GLN A 119 ? 0.4586 0.6112 0.4629 -0.0474 0.0103  -0.0747 131 GLN A OE1 
756  N NE2 . GLN A 119 ? 0.4568 0.6148 0.4616 -0.0516 0.0113  -0.0863 131 GLN A NE2 
757  N N   . TRP A 120 ? 0.2761 0.3770 0.2757 -0.0437 0.0163  -0.0599 132 TRP A N   
758  C CA  . TRP A 120 ? 0.2433 0.3384 0.2422 -0.0408 0.0156  -0.0528 132 TRP A CA  
759  C C   . TRP A 120 ? 0.2367 0.3421 0.2364 -0.0387 0.0131  -0.0492 132 TRP A C   
760  O O   . TRP A 120 ? 0.2253 0.3423 0.2238 -0.0387 0.0115  -0.0500 132 TRP A O   
761  C CB  . TRP A 120 ? 0.2460 0.3359 0.2415 -0.0393 0.0157  -0.0488 132 TRP A CB  
762  C CG  . TRP A 120 ? 0.2490 0.3269 0.2439 -0.0404 0.0179  -0.0509 132 TRP A CG  
763  C CD1 . TRP A 120 ? 0.2646 0.3424 0.2584 -0.0423 0.0190  -0.0556 132 TRP A CD1 
764  C CD2 . TRP A 120 ? 0.2512 0.3156 0.2462 -0.0395 0.0190  -0.0483 132 TRP A CD2 
765  N NE1 . TRP A 120 ? 0.2511 0.3160 0.2446 -0.0426 0.0206  -0.0560 132 TRP A NE1 
766  C CE2 . TRP A 120 ? 0.2409 0.2974 0.2349 -0.0409 0.0206  -0.0514 132 TRP A CE2 
767  C CE3 . TRP A 120 ? 0.2413 0.2997 0.2373 -0.0375 0.0186  -0.0437 132 TRP A CE3 
768  C CZ2 . TRP A 120 ? 0.2465 0.2894 0.2403 -0.0405 0.0218  -0.0500 132 TRP A CZ2 
769  C CZ3 . TRP A 120 ? 0.1981 0.2432 0.1938 -0.0370 0.0199  -0.0426 132 TRP A CZ3 
770  C CH2 . TRP A 120 ? 0.2664 0.3039 0.2608 -0.0386 0.0215  -0.0456 132 TRP A CH2 
771  N N   . GLU A 121 ? 0.2331 0.3339 0.2344 -0.0367 0.0126  -0.0452 133 GLU A N   
772  C CA  . GLU A 121 ? 0.1918 0.3005 0.1939 -0.0341 0.0099  -0.0410 133 GLU A CA  
773  C C   . GLU A 121 ? 0.2607 0.3620 0.2614 -0.0310 0.0089  -0.0338 133 GLU A C   
774  O O   . GLU A 121 ? 0.2269 0.3173 0.2286 -0.0303 0.0101  -0.0326 133 GLU A O   
775  C CB  . GLU A 121 ? 0.2730 0.3845 0.2795 -0.0344 0.0098  -0.0434 133 GLU A CB  
776  C CG  . GLU A 121 ? 0.3168 0.4387 0.3253 -0.0372 0.0099  -0.0498 133 GLU A CG  
777  C CD  . GLU A 121 ? 0.3749 0.5105 0.3836 -0.0356 0.0067  -0.0485 133 GLU A CD  
778  O OE1 . GLU A 121 ? 0.4355 0.5728 0.4417 -0.0328 0.0046  -0.0426 133 GLU A OE1 
779  O OE2 . GLU A 121 ? 0.4072 0.5517 0.4187 -0.0372 0.0063  -0.0532 133 GLU A OE2 
780  N N   . ARG A 122 ? 0.2378 0.3453 0.2364 -0.0290 0.0065  -0.0289 134 ARG A N   
781  C CA  . ARG A 122 ? 0.2549 0.3566 0.2527 -0.0259 0.0049  -0.0217 134 ARG A CA  
782  C C   . ARG A 122 ? 0.2683 0.3736 0.2692 -0.0234 0.0025  -0.0191 134 ARG A C   
783  O O   . ARG A 122 ? 0.2648 0.3813 0.2662 -0.0231 0.0005  -0.0196 134 ARG A O   
784  C CB  . ARG A 122 ? 0.2502 0.3565 0.2444 -0.0252 0.0035  -0.0172 134 ARG A CB  
785  C CG  . ARG A 122 ? 0.2483 0.3461 0.2418 -0.0227 0.0024  -0.0101 134 ARG A CG  
786  C CD  . ARG A 122 ? 0.3035 0.4071 0.2937 -0.0220 0.0007  -0.0048 134 ARG A CD  
787  N NE  . ARG A 122 ? 0.3067 0.4226 0.2966 -0.0211 -0.0021 -0.0030 134 ARG A NE  
788  C CZ  . ARG A 122 ? 0.3235 0.4512 0.3115 -0.0227 -0.0023 -0.0061 134 ARG A CZ  
789  N NH1 . ARG A 122 ? 0.3159 0.4449 0.3020 -0.0254 0.0002  -0.0113 134 ARG A NH1 
790  N NH2 . ARG A 122 ? 0.2728 0.4110 0.2606 -0.0215 -0.0051 -0.0042 134 ARG A NH2 
791  N N   . ILE A 123 ? 0.2447 0.3405 0.2475 -0.0214 0.0026  -0.0166 135 ILE A N   
792  C CA  . ILE A 123 ? 0.2217 0.3200 0.2281 -0.0191 0.0008  -0.0155 135 ILE A CA  
793  C C   . ILE A 123 ? 0.2664 0.3651 0.2725 -0.0155 -0.0027 -0.0082 135 ILE A C   
794  O O   . ILE A 123 ? 0.2933 0.3829 0.2982 -0.0141 -0.0029 -0.0039 135 ILE A O   
795  C CB  . ILE A 123 ? 0.2226 0.3111 0.2316 -0.0190 0.0029  -0.0176 135 ILE A CB  
796  C CG1 . ILE A 123 ? 0.2282 0.3155 0.2373 -0.0228 0.0063  -0.0244 135 ILE A CG1 
797  C CG2 . ILE A 123 ? 0.2400 0.3321 0.2531 -0.0164 0.0011  -0.0169 135 ILE A CG2 
798  C CD1 . ILE A 123 ? 0.2505 0.3499 0.2619 -0.0248 0.0061  -0.0292 135 ILE A CD1 
799  N N   . ASP A 124 ? 0.2797 0.3887 0.2872 -0.0139 -0.0057 -0.0069 136 ASP A N   
800  C CA  . ASP A 124 ? 0.3251 0.4348 0.3331 -0.0102 -0.0095 -0.0001 136 ASP A CA  
801  C C   . ASP A 124 ? 0.2502 0.3528 0.2623 -0.0075 -0.0099 0.0005  136 ASP A C   
802  O O   . ASP A 124 ? 0.3037 0.4119 0.3194 -0.0059 -0.0115 -0.0009 136 ASP A O   
803  C CB  . ASP A 124 ? 0.2671 0.3904 0.2752 -0.0095 -0.0126 0.0008  136 ASP A CB  
804  C CG  . ASP A 124 ? 0.3793 0.5106 0.3831 -0.0122 -0.0120 -0.0004 136 ASP A CG  
805  O OD1 . ASP A 124 ? 0.3780 0.5049 0.3782 -0.0131 -0.0109 0.0022  136 ASP A OD1 
806  O OD2 . ASP A 124 ? 0.5091 0.6516 0.5133 -0.0132 -0.0127 -0.0040 136 ASP A OD2 
807  N N   . CYS A 125 ? 0.2791 0.3695 0.2908 -0.0070 -0.0086 0.0021  137 CYS A N   
808  C CA  . CYS A 125 ? 0.2985 0.3818 0.3136 -0.0046 -0.0085 0.0018  137 CYS A CA  
809  C C   . CYS A 125 ? 0.2666 0.3517 0.2844 -0.0003 -0.0128 0.0069  137 CYS A C   
810  O O   . CYS A 125 ? 0.2634 0.3497 0.2796 0.0010  -0.0157 0.0125  137 CYS A O   
811  C CB  . CYS A 125 ? 0.2294 0.2992 0.2431 -0.0048 -0.0063 0.0025  137 CYS A CB  
812  S SG  . CYS A 125 ? 0.2559 0.3219 0.2676 -0.0094 -0.0014 -0.0042 137 CYS A SG  
813  N N   . GLN A 126 ? 0.2624 0.3477 0.2844 0.0018  -0.0133 0.0049  138 GLN A N   
814  C CA  . GLN A 126 ? 0.2974 0.3825 0.3225 0.0063  -0.0174 0.0092  138 GLN A CA  
815  C C   . GLN A 126 ? 0.2858 0.3577 0.3113 0.0086  -0.0176 0.0121  138 GLN A C   
816  O O   . GLN A 126 ? 0.2541 0.3178 0.2783 0.0070  -0.0142 0.0096  138 GLN A O   
817  C CB  . GLN A 126 ? 0.3385 0.4308 0.3685 0.0080  -0.0182 0.0055  138 GLN A CB  
818  C CG  . GLN A 126 ? 0.3512 0.4572 0.3815 0.0062  -0.0188 0.0028  138 GLN A CG  
819  C CD  . GLN A 126 ? 0.4894 0.6037 0.5250 0.0092  -0.0216 0.0016  138 GLN A CD  
820  O OE1 . GLN A 126 ? 0.4739 0.5902 0.5130 0.0087  -0.0195 -0.0036 138 GLN A OE1 
821  N NE2 . GLN A 126 ? 0.4978 0.6170 0.5340 0.0122  -0.0263 0.0063  138 GLN A NE2 
822  N N   . GLY A 127 ? 0.3073 0.3773 0.3345 0.0124  -0.0217 0.0176  139 GLY A N   
823  C CA  . GLY A 127 ? 0.2976 0.3557 0.3260 0.0150  -0.0226 0.0204  139 GLY A CA  
824  C C   . GLY A 127 ? 0.2562 0.3068 0.2810 0.0139  -0.0226 0.0250  139 GLY A C   
825  O O   . GLY A 127 ? 0.2649 0.3198 0.2862 0.0111  -0.0220 0.0265  139 GLY A O   
826  N N   . ILE A 128 ? 0.2497 0.2893 0.2756 0.0160  -0.0233 0.0272  140 ILE A N   
827  C CA  . ILE A 128 ? 0.3302 0.3617 0.3537 0.0154  -0.0237 0.0318  140 ILE A CA  
828  C C   . ILE A 128 ? 0.3055 0.3318 0.3258 0.0119  -0.0190 0.0279  140 ILE A C   
829  O O   . ILE A 128 ? 0.3018 0.3211 0.3228 0.0124  -0.0170 0.0243  140 ILE A O   
830  C CB  . ILE A 128 ? 0.3452 0.3669 0.3719 0.0194  -0.0268 0.0355  140 ILE A CB  
831  C CG1 . ILE A 128 ? 0.3126 0.3392 0.3431 0.0232  -0.0317 0.0389  140 ILE A CG1 
832  C CG2 . ILE A 128 ? 0.3260 0.3396 0.3507 0.0185  -0.0273 0.0404  140 ILE A CG2 
833  C CD1 . ILE A 128 ? 0.3439 0.3610 0.3780 0.0273  -0.0351 0.0422  140 ILE A CD1 
834  N N   . PRO A 129 ? 0.2768 0.3062 0.2933 0.0085  -0.0173 0.0284  141 PRO A N   
835  C CA  . PRO A 129 ? 0.2474 0.2717 0.2610 0.0053  -0.0131 0.0245  141 PRO A CA  
836  C C   . PRO A 129 ? 0.2617 0.2736 0.2751 0.0063  -0.0132 0.0270  141 PRO A C   
837  O O   . PRO A 129 ? 0.2922 0.3000 0.3073 0.0089  -0.0165 0.0323  141 PRO A O   
838  C CB  . PRO A 129 ? 0.2771 0.3093 0.2872 0.0020  -0.0122 0.0250  141 PRO A CB  
839  C CG  . PRO A 129 ? 0.2338 0.2709 0.2444 0.0038  -0.0162 0.0315  141 PRO A CG  
840  C CD  . PRO A 129 ? 0.2445 0.2830 0.2592 0.0074  -0.0192 0.0322  141 PRO A CD  
841  N N   . PRO A 130 ? 0.2364 0.2417 0.2478 0.0043  -0.0098 0.0234  142 PRO A N   
842  C CA  . PRO A 130 ? 0.2147 0.2089 0.2255 0.0048  -0.0099 0.0258  142 PRO A CA  
843  C C   . PRO A 130 ? 0.2070 0.2031 0.2162 0.0034  -0.0109 0.0306  142 PRO A C   
844  O O   . PRO A 130 ? 0.2483 0.2539 0.2558 0.0014  -0.0107 0.0311  142 PRO A O   
845  C CB  . PRO A 130 ? 0.2211 0.2096 0.2297 0.0025  -0.0059 0.0203  142 PRO A CB  
846  C CG  . PRO A 130 ? 0.2005 0.1955 0.2095 0.0015  -0.0040 0.0151  142 PRO A CG  
847  C CD  . PRO A 130 ? 0.1624 0.1696 0.1722 0.0014  -0.0059 0.0170  142 PRO A CD  
848  N N   . SER A 131 ? 0.2618 0.2488 0.2715 0.0044  -0.0119 0.0340  143 SER A N   
849  C CA  . SER A 131 ? 0.2613 0.2491 0.2694 0.0027  -0.0122 0.0382  143 SER A CA  
850  C C   . SER A 131 ? 0.2318 0.2219 0.2365 -0.0010 -0.0084 0.0340  143 SER A C   
851  O O   . SER A 131 ? 0.2382 0.2252 0.2420 -0.0019 -0.0057 0.0284  143 SER A O   
852  C CB  . SER A 131 ? 0.2458 0.2227 0.2558 0.0044  -0.0140 0.0421  143 SER A CB  
853  O OG  . SER A 131 ? 0.2268 0.1944 0.2363 0.0043  -0.0118 0.0379  143 SER A OG  
854  N N   . SER A 132 ? 0.2242 0.2202 0.2271 -0.0031 -0.0082 0.0367  144 SER A N   
855  C CA  . SER A 132 ? 0.2030 0.2021 0.2029 -0.0064 -0.0049 0.0326  144 SER A CA  
856  C C   . SER A 132 ? 0.1787 0.1668 0.1785 -0.0068 -0.0032 0.0309  144 SER A C   
857  O O   . SER A 132 ? 0.2021 0.1842 0.2031 -0.0059 -0.0046 0.0352  144 SER A O   
858  C CB  . SER A 132 ? 0.2323 0.2405 0.2303 -0.0083 -0.0052 0.0362  144 SER A CB  
859  O OG  . SER A 132 ? 0.2039 0.2200 0.2026 -0.0070 -0.0079 0.0398  144 SER A OG  
860  N N   . LYS A 133 ? 0.1641 0.1495 0.1626 -0.0082 -0.0003 0.0248  145 LYS A N   
861  C CA  . LYS A 133 ? 0.1705 0.1443 0.1690 -0.0079 0.0009  0.0229  145 LYS A CA  
862  C C   . LYS A 133 ? 0.1474 0.1205 0.1437 -0.0103 0.0043  0.0164  145 LYS A C   
863  O O   . LYS A 133 ? 0.1943 0.1751 0.1895 -0.0119 0.0056  0.0129  145 LYS A O   
864  C CB  . LYS A 133 ? 0.1789 0.1438 0.1794 -0.0049 -0.0006 0.0236  145 LYS A CB  
865  C CG  . LYS A 133 ? 0.1878 0.1552 0.1886 -0.0043 0.0001  0.0197  145 LYS A CG  
866  C CD  . LYS A 133 ? 0.1886 0.1480 0.1915 -0.0010 -0.0016 0.0207  145 LYS A CD  
867  C CE  . LYS A 133 ? 0.2039 0.1655 0.2072 -0.0005 -0.0005 0.0166  145 LYS A CE  
868  N NZ  . LYS A 133 ? 0.2012 0.1564 0.2068 0.0031  -0.0024 0.0178  145 LYS A NZ  
869  N N   . ASP A 134 ? 0.1658 0.1291 0.1616 -0.0104 0.0054  0.0147  146 ASP A N   
870  C CA  . ASP A 134 ? 0.1480 0.1088 0.1420 -0.0124 0.0082  0.0088  146 ASP A CA  
871  C C   . ASP A 134 ? 0.1484 0.0965 0.1424 -0.0110 0.0086  0.0074  146 ASP A C   
872  O O   . ASP A 134 ? 0.1816 0.1235 0.1771 -0.0085 0.0066  0.0108  146 ASP A O   
873  C CB  . ASP A 134 ? 0.1499 0.1146 0.1426 -0.0148 0.0096  0.0076  146 ASP A CB  
874  C CG  . ASP A 134 ? 0.1908 0.1498 0.1844 -0.0140 0.0087  0.0112  146 ASP A CG  
875  O OD1 . ASP A 134 ? 0.2230 0.1719 0.2178 -0.0120 0.0076  0.0127  146 ASP A OD1 
876  O OD2 . ASP A 134 ? 0.2020 0.1669 0.1952 -0.0155 0.0091  0.0122  146 ASP A OD2 
877  N N   . LYS A 135 ? 0.1663 0.1103 0.1586 -0.0126 0.0109  0.0024  147 LYS A N   
878  C CA  . LYS A 135 ? 0.1876 0.1194 0.1792 -0.0116 0.0113  0.0009  147 LYS A CA  
879  C C   . LYS A 135 ? 0.1871 0.1141 0.1795 -0.0090 0.0102  0.0021  147 LYS A C   
880  O O   . LYS A 135 ? 0.1617 0.0808 0.1550 -0.0066 0.0086  0.0046  147 LYS A O   
881  C CB  . LYS A 135 ? 0.1742 0.0999 0.1663 -0.0109 0.0104  0.0031  147 LYS A CB  
882  C CG  . LYS A 135 ? 0.2360 0.1656 0.2273 -0.0133 0.0118  0.0010  147 LYS A CG  
883  C CD  . LYS A 135 ? 0.1945 0.1173 0.1867 -0.0126 0.0111  0.0027  147 LYS A CD  
884  C CE  . LYS A 135 ? 0.2239 0.1497 0.2184 -0.0114 0.0089  0.0087  147 LYS A CE  
885  N NZ  . LYS A 135 ? 0.2069 0.1451 0.2013 -0.0133 0.0094  0.0099  147 LYS A NZ  
886  N N   . LEU A 136 ? 0.1889 0.1211 0.1813 -0.0096 0.0111  0.0000  148 LEU A N   
887  C CA  . LEU A 136 ? 0.1827 0.1124 0.1760 -0.0073 0.0103  0.0005  148 LEU A CA  
888  C C   . LEU A 136 ? 0.1579 0.0851 0.1495 -0.0088 0.0129  -0.0042 148 LEU A C   
889  O O   . LEU A 136 ? 0.2227 0.1467 0.2123 -0.0111 0.0148  -0.0073 148 LEU A O   
890  C CB  . LEU A 136 ? 0.1844 0.1237 0.1800 -0.0062 0.0086  0.0031  148 LEU A CB  
891  C CG  . LEU A 136 ? 0.1516 0.1023 0.1471 -0.0087 0.0098  0.0007  148 LEU A CG  
892  C CD1 . LEU A 136 ? 0.2143 0.1716 0.2120 -0.0071 0.0085  0.0017  148 LEU A CD1 
893  C CD2 . LEU A 136 ? 0.1981 0.1559 0.1933 -0.0102 0.0093  0.0026  148 LEU A CD2 
894  N N   . GLY A 137 ? 0.1252 0.1443 0.1726 0.0033  0.0156  0.0408  149 GLY A N   
895  C CA  . GLY A 137 ? 0.1235 0.1488 0.1712 0.0048  0.0176  0.0422  149 GLY A CA  
896  C C   . GLY A 137 ? 0.1202 0.1490 0.1682 0.0074  0.0183  0.0443  149 GLY A C   
897  O O   . GLY A 137 ? 0.1212 0.1472 0.1689 0.0084  0.0172  0.0442  149 GLY A O   
898  N N   . VAL A 138 ? 0.1034 0.1384 0.1518 0.0084  0.0201  0.0462  150 VAL A N   
899  C CA  . VAL A 138 ? 0.1315 0.1709 0.1803 0.0106  0.0211  0.0484  150 VAL A CA  
900  C C   . VAL A 138 ? 0.1313 0.1771 0.1792 0.0137  0.0224  0.0492  150 VAL A C   
901  O O   . VAL A 138 ? 0.1550 0.2031 0.2031 0.0124  0.0232  0.0495  150 VAL A O   
902  C CB  . VAL A 138 ? 0.1770 0.2185 0.2285 0.0067  0.0219  0.0515  150 VAL A CB  
903  C CG1 . VAL A 138 ? 0.1513 0.1961 0.2043 0.0035  0.0231  0.0528  150 VAL A CG1 
904  C CG2 . VAL A 138 ? 0.1068 0.1525 0.1587 0.0090  0.0227  0.0538  150 VAL A CG2 
905  N N   . TRP A 139 ? 0.1432 0.1920 0.1902 0.0179  0.0226  0.0496  151 TRP A N   
906  C CA  . TRP A 139 ? 0.1509 0.2072 0.1973 0.0206  0.0241  0.0511  151 TRP A CA  
907  C C   . TRP A 139 ? 0.1562 0.2177 0.2044 0.0200  0.0253  0.0547  151 TRP A C   
908  O O   . TRP A 139 ? 0.1723 0.2315 0.2211 0.0199  0.0247  0.0551  151 TRP A O   
909  C CB  . TRP A 139 ? 0.1516 0.2084 0.1954 0.0264  0.0234  0.0486  151 TRP A CB  
910  C CG  . TRP A 139 ? 0.1504 0.2013 0.1922 0.0275  0.0220  0.0448  151 TRP A CG  
911  C CD1 . TRP A 139 ? 0.1743 0.2252 0.2155 0.0264  0.0222  0.0438  151 TRP A CD1 
912  C CD2 . TRP A 139 ? 0.1618 0.2060 0.2019 0.0299  0.0199  0.0417  151 TRP A CD2 
913  N NE1 . TRP A 139 ? 0.1851 0.2300 0.2244 0.0280  0.0206  0.0403  151 TRP A NE1 
914  C CE2 . TRP A 139 ? 0.1790 0.2194 0.2175 0.0299  0.0190  0.0389  151 TRP A CE2 
915  C CE3 . TRP A 139 ? 0.2018 0.2425 0.2415 0.0318  0.0184  0.0410  151 TRP A CE3 
916  C CZ2 . TRP A 139 ? 0.1663 0.1999 0.2029 0.0319  0.0167  0.0356  151 TRP A CZ2 
917  C CZ3 . TRP A 139 ? 0.1822 0.2157 0.2200 0.0337  0.0159  0.0377  151 TRP A CZ3 
918  C CH2 . TRP A 139 ? 0.1752 0.2053 0.2115 0.0337  0.0151  0.0350  151 TRP A CH2 
919  N N   . VAL A 140 ? 0.1659 0.2345 0.2148 0.0196  0.0268  0.0574  152 VAL A N   
920  C CA  . VAL A 140 ? 0.1795 0.2541 0.2299 0.0193  0.0279  0.0610  152 VAL A CA  
921  C C   . VAL A 140 ? 0.1834 0.2651 0.2323 0.0242  0.0287  0.0614  152 VAL A C   
922  O O   . VAL A 140 ? 0.1788 0.2643 0.2267 0.0253  0.0292  0.0613  152 VAL A O   
923  C CB  . VAL A 140 ? 0.2309 0.3084 0.2834 0.0146  0.0288  0.0642  152 VAL A CB  
924  C CG1 . VAL A 140 ? 0.2155 0.2997 0.2694 0.0145  0.0300  0.0681  152 VAL A CG1 
925  C CG2 . VAL A 140 ? 0.2015 0.2726 0.2555 0.0101  0.0281  0.0635  152 VAL A CG2 
926  N N   . TYR A 141 ? 0.1854 0.2692 0.2342 0.0271  0.0287  0.0620  153 TYR A N   
927  C CA  . TYR A 141 ? 0.2367 0.3282 0.2842 0.0319  0.0295  0.0625  153 TYR A CA  
928  C C   . TYR A 141 ? 0.2176 0.3135 0.2664 0.0322  0.0302  0.0654  153 TYR A C   
929  O O   . TYR A 141 ? 0.2028 0.2948 0.2518 0.0335  0.0293  0.0644  153 TYR A O   
930  C CB  . TYR A 141 ? 0.2184 0.3070 0.2633 0.0372  0.0283  0.0583  153 TYR A CB  
931  C CG  . TYR A 141 ? 0.1942 0.2914 0.2375 0.0424  0.0290  0.0584  153 TYR A CG  
932  C CD1 . TYR A 141 ? 0.2389 0.3438 0.2821 0.0420  0.0304  0.0604  153 TYR A CD1 
933  C CD2 . TYR A 141 ? 0.2226 0.3204 0.2646 0.0477  0.0283  0.0565  153 TYR A CD2 
934  C CE1 . TYR A 141 ? 0.2592 0.3730 0.3010 0.0467  0.0312  0.0607  153 TYR A CE1 
935  C CE2 . TYR A 141 ? 0.2693 0.3757 0.3099 0.0526  0.0290  0.0564  153 TYR A CE2 
936  C CZ  . TYR A 141 ? 0.2718 0.3865 0.3123 0.0521  0.0305  0.0585  153 TYR A CZ  
937  O OH  . TYR A 141 ? 0.3162 0.4403 0.3553 0.0570  0.0313  0.0585  153 TYR A OH  
938  N N   . LYS A 142 ? 0.2441 0.3482 0.2941 0.0308  0.0317  0.0693  154 LYS A N   
939  C CA  . LYS A 142 ? 0.2029 0.3126 0.2543 0.0307  0.0326  0.0727  154 LYS A CA  
940  C C   . LYS A 142 ? 0.1747 0.2779 0.2280 0.0270  0.0320  0.0733  154 LYS A C   
941  O O   . LYS A 142 ? 0.2605 0.3595 0.3150 0.0223  0.0318  0.0737  154 LYS A O   
942  C CB  . LYS A 142 ? 0.1780 0.2927 0.2279 0.0369  0.0327  0.0716  154 LYS A CB  
943  C CG  . LYS A 142 ? 0.2032 0.3262 0.2514 0.0401  0.0335  0.0717  154 LYS A CG  
944  C CD  . LYS A 142 ? 0.2513 0.3784 0.2976 0.0468  0.0333  0.0694  154 LYS A CD  
945  C CE  . LYS A 142 ? 0.2829 0.4174 0.3272 0.0501  0.0339  0.0687  154 LYS A CE  
946  N NZ  . LYS A 142 ? 0.2605 0.4040 0.3058 0.0471  0.0353  0.0732  154 LYS A NZ  
947  N N   . ASN A 143 ? 0.1741 0.2765 0.2277 0.0289  0.0317  0.0733  155 ASN A N   
948  C CA  . ASN A 143 ? 0.1674 0.2645 0.2229 0.0254  0.0312  0.0742  155 ASN A CA  
949  C C   . ASN A 143 ? 0.1933 0.2804 0.2482 0.0245  0.0294  0.0707  155 ASN A C   
950  O O   . ASN A 143 ? 0.1706 0.2531 0.2271 0.0213  0.0288  0.0713  155 ASN A O   
951  C CB  . ASN A 143 ? 0.1946 0.2951 0.2506 0.0278  0.0313  0.0758  155 ASN A CB  
952  C CG  . ASN A 143 ? 0.2278 0.3281 0.2818 0.0341  0.0304  0.0727  155 ASN A CG  
953  O OD1 . ASN A 143 ? 0.2598 0.3657 0.3122 0.0380  0.0309  0.0719  155 ASN A OD1 
954  N ND2 . ASN A 143 ? 0.2095 0.3036 0.2635 0.0352  0.0288  0.0710  155 ASN A ND2 
955  N N   . LYS A 144 ? 0.1912 0.2751 0.2441 0.0270  0.0285  0.0672  156 LYS A N   
956  C CA  . LYS A 144 ? 0.1860 0.2606 0.2381 0.0267  0.0265  0.0639  156 LYS A CA  
957  C C   . LYS A 144 ? 0.1615 0.2320 0.2139 0.0226  0.0264  0.0630  156 LYS A C   
958  O O   . LYS A 144 ? 0.1668 0.2407 0.2187 0.0224  0.0273  0.0631  156 LYS A O   
959  C CB  . LYS A 144 ? 0.1876 0.2606 0.2371 0.0326  0.0252  0.0603  156 LYS A CB  
960  C CG  . LYS A 144 ? 0.2064 0.2826 0.2556 0.0371  0.0249  0.0605  156 LYS A CG  
961  C CD  . LYS A 144 ? 0.2866 0.3601 0.3331 0.0430  0.0232  0.0565  156 LYS A CD  
962  C CE  . LYS A 144 ? 0.3447 0.4251 0.3905 0.0485  0.0236  0.0569  156 LYS A CE  
963  N NZ  . LYS A 144 ? 0.3916 0.4682 0.4351 0.0543  0.0213  0.0527  156 LYS A NZ  
964  N N   . LEU A 145 ? 0.1144 0.1782 0.1677 0.0191  0.0253  0.0623  157 LEU A N   
965  C CA  . LEU A 145 ? 0.1433 0.2016 0.1963 0.0162  0.0245  0.0602  157 LEU A CA  
966  C C   . LEU A 145 ? 0.1568 0.2083 0.2079 0.0188  0.0224  0.0566  157 LEU A C   
967  O O   . LEU A 145 ? 0.1663 0.2140 0.2177 0.0191  0.0210  0.0563  157 LEU A O   
968  C CB  . LEU A 145 ? 0.1412 0.1972 0.1965 0.0104  0.0246  0.0618  157 LEU A CB  
969  C CG  . LEU A 145 ? 0.1488 0.2109 0.2063 0.0078  0.0263  0.0656  157 LEU A CG  
970  C CD1 . LEU A 145 ? 0.1915 0.2510 0.2511 0.0023  0.0262  0.0668  157 LEU A CD1 
971  C CD2 . LEU A 145 ? 0.2078 0.2753 0.2649 0.0081  0.0276  0.0666  157 LEU A CD2 
972  N N   . ILE A 146 ? 0.1389 0.1887 0.1882 0.0205  0.0219  0.0539  158 ILE A N   
973  C CA  . ILE A 146 ? 0.1404 0.1840 0.1875 0.0235  0.0197  0.0504  158 ILE A CA  
974  C C   . ILE A 146 ? 0.1591 0.1967 0.2061 0.0200  0.0187  0.0485  158 ILE A C   
975  O O   . ILE A 146 ? 0.1769 0.2161 0.2236 0.0192  0.0195  0.0479  158 ILE A O   
976  C CB  . ILE A 146 ? 0.1471 0.1941 0.1919 0.0292  0.0199  0.0485  158 ILE A CB  
977  C CG1 . ILE A 146 ? 0.1442 0.1991 0.1895 0.0321  0.0213  0.0509  158 ILE A CG1 
978  C CG2 . ILE A 146 ? 0.1631 0.2034 0.2056 0.0327  0.0173  0.0448  158 ILE A CG2 
979  C CD1 . ILE A 146 ? 0.2003 0.2620 0.2439 0.0361  0.0225  0.0505  158 ILE A CD1 
980  N N   . PHE A 147 ? 0.1340 0.1651 0.1813 0.0179  0.0168  0.0477  159 PHE A N   
981  C CA  . PHE A 147 ? 0.1583 0.1841 0.2057 0.0141  0.0157  0.0463  159 PHE A CA  
982  C C   . PHE A 147 ? 0.1531 0.1727 0.1981 0.0168  0.0133  0.0429  159 PHE A C   
983  O O   . PHE A 147 ? 0.1652 0.1821 0.2090 0.0201  0.0116  0.0419  159 PHE A O   
984  C CB  . PHE A 147 ? 0.1433 0.1666 0.1928 0.0094  0.0151  0.0480  159 PHE A CB  
985  C CG  . PHE A 147 ? 0.1506 0.1794 0.2026 0.0064  0.0173  0.0512  159 PHE A CG  
986  C CD1 . PHE A 147 ? 0.1444 0.1753 0.1976 0.0028  0.0185  0.0518  159 PHE A CD1 
987  C CD2 . PHE A 147 ? 0.1708 0.2030 0.2238 0.0074  0.0179  0.0536  159 PHE A CD2 
988  C CE1 . PHE A 147 ? 0.1684 0.2041 0.2238 0.0001  0.0202  0.0547  159 PHE A CE1 
989  C CE2 . PHE A 147 ? 0.1644 0.2017 0.2196 0.0046  0.0198  0.0567  159 PHE A CE2 
990  C CZ  . PHE A 147 ? 0.1351 0.1739 0.1915 0.0009  0.0209  0.0572  159 PHE A CZ  
991  N N   . PHE A 148 ? 0.1450 0.1624 0.1892 0.0155  0.0130  0.0410  160 PHE A N   
992  C CA  . PHE A 148 ? 0.1728 0.1842 0.2145 0.0178  0.0107  0.0377  160 PHE A CA  
993  C C   . PHE A 148 ? 0.1774 0.1838 0.2194 0.0134  0.0094  0.0368  160 PHE A C   
994  O O   . PHE A 148 ? 0.1591 0.1679 0.2024 0.0101  0.0109  0.0374  160 PHE A O   
995  C CB  . PHE A 148 ? 0.1444 0.1584 0.1840 0.0221  0.0114  0.0358  160 PHE A CB  
996  C CG  . PHE A 148 ? 0.1543 0.1623 0.1915 0.0237  0.0091  0.0324  160 PHE A CG  
997  C CD1 . PHE A 148 ? 0.1798 0.1826 0.2152 0.0271  0.0064  0.0305  160 PHE A CD1 
998  C CD2 . PHE A 148 ? 0.1690 0.1760 0.2057 0.0218  0.0094  0.0312  160 PHE A CD2 
999  C CE1 . PHE A 148 ? 0.1985 0.1953 0.2316 0.0285  0.0041  0.0274  160 PHE A CE1 
1000 C CE2 . PHE A 148 ? 0.1976 0.1990 0.2322 0.0231  0.0073  0.0281  160 PHE A CE2 
1001 C CZ  . PHE A 148 ? 0.1889 0.1850 0.2215 0.0264  0.0046  0.0262  160 PHE A CZ  
1002 N N   . GLY A 149 ? 0.1379 0.1375 0.1789 0.0132  0.0065  0.0353  161 GLY A N   
1003 C CA  . GLY A 149 ? 0.1513 0.1456 0.1918 0.0100  0.0048  0.0338  161 GLY A CA  
1004 C C   . GLY A 149 ? 0.1516 0.1464 0.1947 0.0039  0.0052  0.0357  161 GLY A C   
1005 O O   . GLY A 149 ? 0.1214 0.1187 0.1665 0.0020  0.0060  0.0382  161 GLY A O   
1006 N N   . GLY A 150 ? 0.1654 0.1579 0.2083 0.0009  0.0045  0.0345  162 GLY A N   
1007 C CA  . GLY A 150 ? 0.1436 0.1374 0.1888 -0.0047 0.0051  0.0359  162 GLY A CA  
1008 C C   . GLY A 150 ? 0.1636 0.1519 0.2085 -0.0079 0.0022  0.0353  162 GLY A C   
1009 O O   . GLY A 150 ? 0.1676 0.1505 0.2105 -0.0059 -0.0004 0.0337  162 GLY A O   
1010 N N   . TYR A 151 ? 0.1841 0.1742 0.2312 -0.0129 0.0026  0.0367  163 TYR A N   
1011 C CA  . TYR A 151 ? 0.1803 0.1667 0.2275 -0.0170 0.0002  0.0365  163 TYR A CA  
1012 C C   . TYR A 151 ? 0.1767 0.1644 0.2260 -0.0207 -0.0001 0.0392  163 TYR A C   
1013 O O   . TYR A 151 ? 0.1423 0.1353 0.1938 -0.0224 0.0023  0.0407  163 TYR A O   
1014 C CB  . TYR A 151 ? 0.1390 0.1275 0.1868 -0.0199 0.0011  0.0354  163 TYR A CB  
1015 C CG  . TYR A 151 ? 0.1593 0.1443 0.2067 -0.0236 -0.0015 0.0347  163 TYR A CG  
1016 C CD1 . TYR A 151 ? 0.2075 0.1865 0.2524 -0.0219 -0.0042 0.0330  163 TYR A CD1 
1017 C CD2 . TYR A 151 ? 0.2459 0.2339 0.2953 -0.0287 -0.0012 0.0358  163 TYR A CD2 
1018 C CE1 . TYR A 151 ? 0.2232 0.1992 0.2678 -0.0254 -0.0066 0.0326  163 TYR A CE1 
1019 C CE2 . TYR A 151 ? 0.1943 0.1799 0.2433 -0.0321 -0.0035 0.0353  163 TYR A CE2 
1020 C CZ  . TYR A 151 ? 0.2411 0.2207 0.2878 -0.0306 -0.0062 0.0338  163 TYR A CZ  
1021 O OH  . TYR A 151 ? 0.2325 0.2097 0.2787 -0.0342 -0.0087 0.0336  163 TYR A OH  
1022 N N   . GLY A 152 ? 0.1784 0.1614 0.2272 -0.0220 -0.0031 0.0397  164 GLY A N   
1023 C CA  . GLY A 152 ? 0.2407 0.2249 0.2916 -0.0258 -0.0036 0.0423  164 GLY A CA  
1024 C C   . GLY A 152 ? 0.2497 0.2278 0.2997 -0.0270 -0.0075 0.0428  164 GLY A C   
1025 O O   . GLY A 152 ? 0.2210 0.1940 0.2691 -0.0261 -0.0100 0.0411  164 GLY A O   
1026 N N   . TYR A 153 ? 0.2185 0.1972 0.2701 -0.0292 -0.0081 0.0454  165 TYR A N   
1027 C CA  . TYR A 153 ? 0.2797 0.2530 0.3309 -0.0311 -0.0120 0.0464  165 TYR A CA  
1028 C C   . TYR A 153 ? 0.2611 0.2282 0.3100 -0.0260 -0.0144 0.0453  165 TYR A C   
1029 O O   . TYR A 153 ? 0.2377 0.2059 0.2858 -0.0210 -0.0127 0.0442  165 TYR A O   
1030 C CB  . TYR A 153 ? 0.2211 0.1971 0.2747 -0.0350 -0.0119 0.0495  165 TYR A CB  
1031 C CG  . TYR A 153 ? 0.2586 0.2413 0.3145 -0.0395 -0.0093 0.0504  165 TYR A CG  
1032 C CD1 . TYR A 153 ? 0.3547 0.3381 0.4103 -0.0426 -0.0098 0.0493  165 TYR A CD1 
1033 C CD2 . TYR A 153 ? 0.2660 0.2545 0.3240 -0.0403 -0.0065 0.0522  165 TYR A CD2 
1034 C CE1 . TYR A 153 ? 0.3334 0.3231 0.3911 -0.0463 -0.0076 0.0498  165 TYR A CE1 
1035 C CE2 . TYR A 153 ? 0.3080 0.3025 0.3679 -0.0441 -0.0043 0.0526  165 TYR A CE2 
1036 C CZ  . TYR A 153 ? 0.3173 0.3124 0.3760 -0.0462 -0.0048 0.0505  165 TYR A CZ  
1037 O OH  . TYR A 153 ? 0.3089 0.3098 0.3662 -0.0472 -0.0027 0.0480  165 TYR A OH  
1038 N N   . LEU A 154 ? 0.2960 0.2569 0.3440 -0.0273 -0.0185 0.0456  166 LEU A N   
1039 C CA  . LEU A 154 ? 0.2958 0.2507 0.3420 -0.0226 -0.0213 0.0447  166 LEU A CA  
1040 C C   . LEU A 154 ? 0.3179 0.2755 0.3653 -0.0203 -0.0198 0.0464  166 LEU A C   
1041 O O   . LEU A 154 ? 0.3719 0.3333 0.4217 -0.0241 -0.0186 0.0491  166 LEU A O   
1042 C CB  . LEU A 154 ? 0.3510 0.2987 0.3964 -0.0253 -0.0264 0.0455  166 LEU A CB  
1043 C CG  . LEU A 154 ? 0.3349 0.2753 0.3783 -0.0209 -0.0302 0.0445  166 LEU A CG  
1044 C CD1 . LEU A 154 ? 0.3596 0.2958 0.4000 -0.0161 -0.0313 0.0409  166 LEU A CD1 
1045 C CD2 . LEU A 154 ? 0.4037 0.3384 0.4472 -0.0250 -0.0350 0.0464  166 LEU A CD2 
1046 N N   . PRO A 155 ? 0.3518 0.3084 0.3978 -0.0142 -0.0195 0.0448  167 PRO A N   
1047 C CA  . PRO A 155 ? 0.4169 0.3766 0.4641 -0.0118 -0.0180 0.0464  167 PRO A CA  
1048 C C   . PRO A 155 ? 0.5101 0.4659 0.5582 -0.0138 -0.0212 0.0486  167 PRO A C   
1049 O O   . PRO A 155 ? 0.5156 0.4645 0.5625 -0.0148 -0.0255 0.0482  167 PRO A O   
1050 C CB  . PRO A 155 ? 0.4015 0.3600 0.4465 -0.0046 -0.0178 0.0438  167 PRO A CB  
1051 C CG  . PRO A 155 ? 0.3538 0.3110 0.3969 -0.0036 -0.0177 0.0410  167 PRO A CG  
1052 C CD  . PRO A 155 ? 0.3228 0.2765 0.3661 -0.0092 -0.0200 0.0415  167 PRO A CD  
1053 N N   . GLU A 156 ? 0.5449 0.5051 0.5951 -0.0145 -0.0193 0.0510  168 GLU A N   
1054 C CA  . GLU A 156 ? 0.6350 0.5923 0.6863 -0.0163 -0.0221 0.0534  168 GLU A CA  
1055 C C   . GLU A 156 ? 0.6953 0.6474 0.7449 -0.0105 -0.0249 0.0521  168 GLU A C   
1056 O O   . GLU A 156 ? 0.7507 0.6991 0.8009 -0.0115 -0.0279 0.0537  168 GLU A O   
1057 C CB  . GLU A 156 ? 0.6483 0.6122 0.7024 -0.0189 -0.0190 0.0564  168 GLU A CB  
1058 C CG  . GLU A 156 ? 0.6521 0.6214 0.7080 -0.0246 -0.0164 0.0577  168 GLU A CG  
1059 C CD  . GLU A 156 ? 0.5663 0.5319 0.6219 -0.0295 -0.0193 0.0578  168 GLU A CD  
1060 O OE1 . GLU A 156 ? 0.5881 0.5564 0.6438 -0.0318 -0.0177 0.0568  168 GLU A OE1 
1061 O OE2 . GLU A 156 ? 0.6100 0.5704 0.6655 -0.0312 -0.0233 0.0589  168 GLU A OE2 
1062 N N   . ASP A 157 ? 0.7772 0.7292 0.8248 -0.0045 -0.0241 0.0492  169 ASP A N   
1063 C CA  . ASP A 157 ? 0.8425 0.7903 0.8884 0.0017  -0.0266 0.0475  169 ASP A CA  
1064 C C   . ASP A 157 ? 0.8131 0.7576 0.8560 0.0062  -0.0276 0.0437  169 ASP A C   
1065 O O   . ASP A 157 ? 0.7172 0.6645 0.7596 0.0052  -0.0252 0.0426  169 ASP A O   
1066 C CB  . ASP A 157 ? 0.8484 0.8025 0.8953 0.0054  -0.0234 0.0484  169 ASP A CB  
1067 C CG  . ASP A 157 ? 0.8962 0.8473 0.9412 0.0127  -0.0255 0.0461  169 ASP A CG  
1068 O OD1 . ASP A 157 ? 0.9652 0.9112 1.0103 0.0134  -0.0292 0.0467  169 ASP A OD1 
1069 O OD2 . ASP A 157 ? 0.8536 0.8075 0.8970 0.0177  -0.0237 0.0437  169 ASP A OD2 
1070 N N   . LYS A 158 ? 0.9030 0.8414 0.9439 0.0111  -0.0313 0.0415  170 LYS A N   
1071 C CA  . LYS A 158 ? 0.8662 0.8021 0.9041 0.0167  -0.0321 0.0377  170 LYS A CA  
1072 C C   . LYS A 158 ? 0.7889 0.7323 0.8266 0.0222  -0.0281 0.0366  170 LYS A C   
1073 O O   . LYS A 158 ? 0.8451 0.7877 0.8813 0.0285  -0.0293 0.0345  170 LYS A O   
1074 C CB  . LYS A 158 ? 0.9123 0.8388 0.9480 0.0200  -0.0379 0.0357  170 LYS A CB  
1075 C CG  . LYS A 158 ? 0.9900 0.9088 1.0254 0.0148  -0.0424 0.0364  170 LYS A CG  
1076 C CD  . LYS A 158 ? 1.0448 0.9547 1.0790 0.0170  -0.0483 0.0357  170 LYS A CD  
1077 C CE  . LYS A 158 ? 1.1015 1.0133 1.1378 0.0170  -0.0483 0.0383  170 LYS A CE  
1078 N NZ  . LYS A 158 ? 1.1183 1.0345 1.1576 0.0097  -0.0460 0.0425  170 LYS A NZ  
1079 N N   . VAL A 159 ? 0.7006 0.6518 0.7400 0.0196  -0.0233 0.0381  171 VAL A N   
1080 C CA  . VAL A 159 ? 0.5672 0.5265 0.6067 0.0236  -0.0192 0.0378  171 VAL A CA  
1081 C C   . VAL A 159 ? 0.4939 0.4524 0.5305 0.0288  -0.0194 0.0340  171 VAL A C   
1082 O O   . VAL A 159 ? 0.5291 0.4812 0.5639 0.0284  -0.0222 0.0319  171 VAL A O   
1083 C CB  . VAL A 159 ? 0.5653 0.5322 0.6072 0.0190  -0.0146 0.0404  171 VAL A CB  
1084 C CG1 . VAL A 159 ? 0.6366 0.6020 0.6808 0.0122  -0.0153 0.0434  171 VAL A CG1 
1085 C CG2 . VAL A 159 ? 0.4071 0.3758 0.4480 0.0183  -0.0127 0.0387  171 VAL A CG2 
1086 N N   . LEU A 160 ? 0.4320 0.3971 0.4682 0.0336  -0.0165 0.0332  172 LEU A N   
1087 C CA  . LEU A 160 ? 0.3510 0.3162 0.3844 0.0388  -0.0166 0.0297  172 LEU A CA  
1088 C C   . LEU A 160 ? 0.3418 0.3081 0.3750 0.0355  -0.0147 0.0292  172 LEU A C   
1089 O O   . LEU A 160 ? 0.3524 0.3246 0.3876 0.0318  -0.0111 0.0314  172 LEU A O   
1090 C CB  . LEU A 160 ? 0.3814 0.3545 0.4146 0.0444  -0.0138 0.0293  172 LEU A CB  
1091 C CG  . LEU A 160 ? 0.3943 0.3676 0.4277 0.0484  -0.0153 0.0296  172 LEU A CG  
1092 C CD1 . LEU A 160 ? 0.3660 0.3486 0.3992 0.0536  -0.0121 0.0294  172 LEU A CD1 
1093 C CD2 . LEU A 160 ? 0.3905 0.3546 0.4217 0.0519  -0.0206 0.0266  172 LEU A CD2 
1094 N N   . GLY A 161 ? 0.3547 0.3153 0.3855 0.0371  -0.0172 0.0261  173 GLY A N   
1095 C CA  . GLY A 161 ? 0.2947 0.2553 0.3249 0.0343  -0.0161 0.0253  173 GLY A CA  
1096 C C   . GLY A 161 ? 0.3109 0.2626 0.3402 0.0310  -0.0201 0.0244  173 GLY A C   
1097 O O   . GLY A 161 ? 0.3501 0.2951 0.3788 0.0315  -0.0241 0.0241  173 GLY A O   
1098 N N   . THR A 162 ? 0.3326 0.2843 0.3618 0.0274  -0.0191 0.0241  174 THR A N   
1099 C CA  . THR A 162 ? 0.2954 0.2399 0.3240 0.0233  -0.0224 0.0238  174 THR A CA  
1100 C C   . THR A 162 ? 0.2734 0.2213 0.3043 0.0167  -0.0200 0.0261  174 THR A C   
1101 O O   . THR A 162 ? 0.2609 0.2160 0.2931 0.0159  -0.0159 0.0270  174 THR A O   
1102 C CB  . THR A 162 ? 0.2850 0.2246 0.3105 0.0263  -0.0245 0.0202  174 THR A CB  
1103 O OG1 . THR A 162 ? 0.3415 0.2864 0.3669 0.0261  -0.0210 0.0194  174 THR A OG1 
1104 C CG2 . THR A 162 ? 0.3289 0.2660 0.3519 0.0336  -0.0267 0.0174  174 THR A CG2 
1105 N N   . PHE A 163 ? 0.2348 0.1775 0.2660 0.0118  -0.0228 0.0269  175 PHE A N   
1106 C CA  . PHE A 163 ? 0.2294 0.1747 0.2627 0.0053  -0.0213 0.0289  175 PHE A CA  
1107 C C   . PHE A 163 ? 0.3060 0.2454 0.3378 0.0027  -0.0244 0.0276  175 PHE A C   
1108 O O   . PHE A 163 ? 0.3288 0.2608 0.3590 0.0033  -0.0288 0.0269  175 PHE A O   
1109 C CB  . PHE A 163 ? 0.2825 0.2289 0.3184 0.0011  -0.0216 0.0323  175 PHE A CB  
1110 C CG  . PHE A 163 ? 0.2622 0.2107 0.3001 -0.0058 -0.0208 0.0342  175 PHE A CG  
1111 C CD1 . PHE A 163 ? 0.2930 0.2490 0.3330 -0.0081 -0.0166 0.0355  175 PHE A CD1 
1112 C CD2 . PHE A 163 ? 0.2821 0.2252 0.3197 -0.0099 -0.0245 0.0348  175 PHE A CD2 
1113 C CE1 . PHE A 163 ? 0.2336 0.1919 0.2755 -0.0142 -0.0161 0.0371  175 PHE A CE1 
1114 C CE2 . PHE A 163 ? 0.2969 0.2427 0.3363 -0.0162 -0.0239 0.0366  175 PHE A CE2 
1115 C CZ  . PHE A 163 ? 0.2890 0.2425 0.3305 -0.0181 -0.0196 0.0376  175 PHE A CZ  
1116 N N   . GLU A 164 ? 0.2811 0.2236 0.3133 -0.0002 -0.0223 0.0273  176 GLU A N   
1117 C CA  . GLU A 164 ? 0.3170 0.2549 0.3478 -0.0028 -0.0248 0.0260  176 GLU A CA  
1118 C C   . GLU A 164 ? 0.2632 0.2046 0.2964 -0.0095 -0.0237 0.0282  176 GLU A C   
1119 O O   . GLU A 164 ? 0.2645 0.2125 0.2993 -0.0107 -0.0198 0.0286  176 GLU A O   
1120 C CB  . GLU A 164 ? 0.3504 0.2887 0.3791 0.0008  -0.0236 0.0230  176 GLU A CB  
1121 C CG  . GLU A 164 ? 0.3635 0.2999 0.3899 0.0078  -0.0242 0.0206  176 GLU A CG  
1122 C CD  . GLU A 164 ? 0.4312 0.3588 0.4547 0.0099  -0.0291 0.0184  176 GLU A CD  
1123 O OE1 . GLU A 164 ? 0.4619 0.3868 0.4839 0.0089  -0.0302 0.0168  176 GLU A OE1 
1124 O OE2 . GLU A 164 ? 0.4883 0.4115 0.5111 0.0124  -0.0320 0.0183  176 GLU A OE2 
1125 N N   . PHE A 165 ? 0.2730 0.2100 0.3062 -0.0138 -0.0271 0.0294  177 PHE A N   
1126 C CA  . PHE A 165 ? 0.2573 0.1980 0.2927 -0.0203 -0.0263 0.0313  177 PHE A CA  
1127 C C   . PHE A 165 ? 0.2771 0.2201 0.3120 -0.0213 -0.0247 0.0296  177 PHE A C   
1128 O O   . PHE A 165 ? 0.2509 0.1897 0.2834 -0.0189 -0.0263 0.0272  177 PHE A O   
1129 C CB  . PHE A 165 ? 0.3000 0.2358 0.3355 -0.0247 -0.0307 0.0332  177 PHE A CB  
1130 C CG  . PHE A 165 ? 0.2809 0.2178 0.3184 -0.0268 -0.0311 0.0361  177 PHE A CG  
1131 C CD1 . PHE A 165 ? 0.3116 0.2556 0.3520 -0.0309 -0.0281 0.0383  177 PHE A CD1 
1132 C CD2 . PHE A 165 ? 0.3072 0.2379 0.3437 -0.0247 -0.0347 0.0365  177 PHE A CD2 
1133 C CE1 . PHE A 165 ? 0.3239 0.2690 0.3662 -0.0329 -0.0286 0.0411  177 PHE A CE1 
1134 C CE2 . PHE A 165 ? 0.2863 0.2179 0.3247 -0.0268 -0.0353 0.0393  177 PHE A CE2 
1135 C CZ  . PHE A 165 ? 0.3285 0.2674 0.3698 -0.0310 -0.0321 0.0417  177 PHE A CZ  
1136 N N   . ASP A 166 ? 0.2553 0.2051 0.2925 -0.0249 -0.0216 0.0307  178 ASP A N   
1137 C CA  . ASP A 166 ? 0.3035 0.2559 0.3408 -0.0270 -0.0204 0.0295  178 ASP A CA  
1138 C C   . ASP A 166 ? 0.2862 0.2369 0.3238 -0.0328 -0.0233 0.0308  178 ASP A C   
1139 O O   . ASP A 166 ? 0.3082 0.2627 0.3481 -0.0372 -0.0229 0.0331  178 ASP A O   
1140 C CB  . ASP A 166 ? 0.2998 0.2602 0.3393 -0.0278 -0.0159 0.0299  178 ASP A CB  
1141 C CG  . ASP A 166 ? 0.3017 0.2651 0.3415 -0.0302 -0.0147 0.0286  178 ASP A CG  
1142 O OD1 . ASP A 166 ? 0.3175 0.2771 0.3557 -0.0314 -0.0172 0.0275  178 ASP A OD1 
1143 O OD2 . ASP A 166 ? 0.3241 0.2938 0.3658 -0.0310 -0.0115 0.0288  178 ASP A OD2 
1144 N N   . GLU A 167 ? 0.3065 0.2518 0.3419 -0.0327 -0.0263 0.0293  179 GLU A N   
1145 C CA  . GLU A 167 ? 0.3125 0.2556 0.3479 -0.0381 -0.0297 0.0307  179 GLU A CA  
1146 C C   . GLU A 167 ? 0.3495 0.2999 0.3873 -0.0433 -0.0276 0.0317  179 GLU A C   
1147 O O   . GLU A 167 ? 0.3574 0.3083 0.3961 -0.0484 -0.0298 0.0338  179 GLU A O   
1148 C CB  . GLU A 167 ? 0.3684 0.3047 0.4008 -0.0368 -0.0330 0.0286  179 GLU A CB  
1149 C CG  . GLU A 167 ? 0.3781 0.3168 0.4096 -0.0344 -0.0305 0.0259  179 GLU A CG  
1150 C CD  . GLU A 167 ? 0.4545 0.3881 0.4837 -0.0352 -0.0336 0.0245  179 GLU A CD  
1151 O OE1 . GLU A 167 ? 0.4791 0.4054 0.5064 -0.0352 -0.0380 0.0247  179 GLU A OE1 
1152 O OE2 . GLU A 167 ? 0.4430 0.3797 0.4721 -0.0358 -0.0319 0.0230  179 GLU A OE2 
1153 N N   . THR A 168 ? 0.3230 0.2791 0.3617 -0.0420 -0.0237 0.0303  180 THR A N   
1154 C CA  . THR A 168 ? 0.3460 0.3092 0.3868 -0.0463 -0.0216 0.0309  180 THR A CA  
1155 C C   . THR A 168 ? 0.4025 0.3709 0.4461 -0.0495 -0.0203 0.0335  180 THR A C   
1156 O O   . THR A 168 ? 0.4175 0.3918 0.4630 -0.0537 -0.0193 0.0342  180 THR A O   
1157 C CB  . THR A 168 ? 0.3271 0.2946 0.3683 -0.0438 -0.0179 0.0287  180 THR A CB  
1158 O OG1 . THR A 168 ? 0.3486 0.3182 0.3905 -0.0401 -0.0151 0.0287  180 THR A OG1 
1159 C CG2 . THR A 168 ? 0.3904 0.3535 0.4289 -0.0409 -0.0190 0.0261  180 THR A CG2 
1160 N N   . SER A 169 ? 0.3444 0.3111 0.3883 -0.0476 -0.0203 0.0348  181 SER A N   
1161 C CA  . SER A 169 ? 0.3936 0.3650 0.4401 -0.0505 -0.0192 0.0373  181 SER A CA  
1162 C C   . SER A 169 ? 0.4243 0.3929 0.4710 -0.0546 -0.0230 0.0399  181 SER A C   
1163 O O   . SER A 169 ? 0.4214 0.3935 0.4701 -0.0574 -0.0225 0.0422  181 SER A O   
1164 C CB  . SER A 169 ? 0.3655 0.3373 0.4125 -0.0464 -0.0170 0.0376  181 SER A CB  
1165 O OG  . SER A 169 ? 0.3115 0.2766 0.3568 -0.0437 -0.0197 0.0381  181 SER A OG  
1166 N N   . PHE A 170 ? 0.4096 0.3718 0.4542 -0.0552 -0.0269 0.0395  182 PHE A N   
1167 C CA  . PHE A 170 ? 0.4446 0.4035 0.4893 -0.0591 -0.0310 0.0421  182 PHE A CA  
1168 C C   . PHE A 170 ? 0.5146 0.4813 0.5593 -0.0630 -0.0300 0.0423  182 PHE A C   
1169 O O   . PHE A 170 ? 0.5284 0.4977 0.5729 -0.0643 -0.0304 0.0437  182 PHE A O   
1170 C CB  . PHE A 170 ? 0.4306 0.3806 0.4723 -0.0579 -0.0354 0.0412  182 PHE A CB  
1171 C CG  . PHE A 170 ? 0.3803 0.3238 0.4200 -0.0515 -0.0361 0.0395  182 PHE A CG  
1172 C CD1 . PHE A 170 ? 0.3861 0.3313 0.4268 -0.0480 -0.0335 0.0397  182 PHE A CD1 
1173 C CD2 . PHE A 170 ? 0.3800 0.3157 0.4168 -0.0489 -0.0394 0.0377  182 PHE A CD2 
1174 C CE1 . PHE A 170 ? 0.4075 0.3474 0.4463 -0.0420 -0.0341 0.0380  182 PHE A CE1 
1175 C CE2 . PHE A 170 ? 0.3729 0.3029 0.4077 -0.0428 -0.0401 0.0359  182 PHE A CE2 
1176 C CZ  . PHE A 170 ? 0.3631 0.2955 0.3989 -0.0393 -0.0374 0.0360  182 PHE A CZ  
1177 N N   . TRP A 171 ? 0.5061 0.4765 0.5504 -0.0639 -0.0287 0.0406  183 TRP A N   
1178 C CA  . TRP A 171 ? 0.5713 0.5480 0.6147 -0.0666 -0.0284 0.0402  183 TRP A CA  
1179 C C   . TRP A 171 ? 0.6326 0.6185 0.6773 -0.0665 -0.0239 0.0388  183 TRP A C   
1180 O O   . TRP A 171 ? 0.6949 0.6862 0.7391 -0.0683 -0.0234 0.0381  183 TRP A O   
1181 C CB  . TRP A 171 ? 0.6010 0.5750 0.6428 -0.0679 -0.0308 0.0393  183 TRP A CB  
1182 C CG  . TRP A 171 ? 0.5549 0.5185 0.5952 -0.0670 -0.0351 0.0398  183 TRP A CG  
1183 C CD1 . TRP A 171 ? 0.5602 0.5183 0.5990 -0.0679 -0.0393 0.0414  183 TRP A CD1 
1184 C CD2 . TRP A 171 ? 0.5357 0.4928 0.5757 -0.0648 -0.0359 0.0384  183 TRP A CD2 
1185 N NE1 . TRP A 171 ? 0.5377 0.4860 0.5752 -0.0661 -0.0427 0.0408  183 TRP A NE1 
1186 C CE2 . TRP A 171 ? 0.5448 0.4921 0.5829 -0.0641 -0.0406 0.0389  183 TRP A CE2 
1187 C CE3 . TRP A 171 ? 0.5094 0.4683 0.5499 -0.0622 -0.0327 0.0362  183 TRP A CE3 
1188 C CZ2 . TRP A 171 ? 0.5501 0.4906 0.5858 -0.0593 -0.0416 0.0364  183 TRP A CZ2 
1189 C CZ3 . TRP A 171 ? 0.5323 0.4850 0.5702 -0.0572 -0.0334 0.0336  183 TRP A CZ3 
1190 C CH2 . TRP A 171 ? 0.4824 0.4262 0.5179 -0.0557 -0.0377 0.0337  183 TRP A CH2 
1191 N N   . ASN A 172 ? 0.6952 0.6830 0.7416 -0.0644 -0.0208 0.0384  184 ASN A N   
1192 C CA  . ASN A 172 ? 0.6934 0.6891 0.7407 -0.0639 -0.0169 0.0368  184 ASN A CA  
1193 C C   . ASN A 172 ? 0.7705 0.7697 0.8186 -0.0632 -0.0149 0.0375  184 ASN A C   
1194 O O   . ASN A 172 ? 0.7646 0.7701 0.8129 -0.0634 -0.0126 0.0363  184 ASN A O   
1195 C CB  . ASN A 172 ? 0.6944 0.6903 0.7429 -0.0620 -0.0147 0.0353  184 ASN A CB  
1196 C CG  . ASN A 172 ? 0.6138 0.6040 0.6634 -0.0599 -0.0151 0.0366  184 ASN A CG  
1197 O OD1 . ASN A 172 ? 0.6073 0.5947 0.6570 -0.0594 -0.0162 0.0385  184 ASN A OD1 
1198 N ND2 . ASN A 172 ? 0.5982 0.5869 0.6487 -0.0582 -0.0142 0.0357  184 ASN A ND2 
1199 N N   . SER A 173 ? 0.6878 0.6828 0.7363 -0.0622 -0.0159 0.0394  185 SER A N   
1200 C CA  . SER A 173 ? 0.6890 0.6868 0.7382 -0.0614 -0.0141 0.0402  185 SER A CA  
1201 C C   . SER A 173 ? 0.7094 0.7044 0.7579 -0.0627 -0.0171 0.0423  185 SER A C   
1202 O O   . SER A 173 ? 0.6845 0.6761 0.7318 -0.0645 -0.0203 0.0430  185 SER A O   
1203 C CB  . SER A 173 ? 0.7235 0.7197 0.7742 -0.0587 -0.0123 0.0407  185 SER A CB  
1204 O OG  . SER A 173 ? 0.6460 0.6347 0.6971 -0.0579 -0.0149 0.0422  185 SER A OG  
1205 N N   . SER A 174 ? 0.7246 0.7210 0.7737 -0.0619 -0.0160 0.0434  186 SER A N   
1206 C CA  . SER A 174 ? 0.7446 0.7380 0.7932 -0.0629 -0.0187 0.0455  186 SER A CA  
1207 C C   . SER A 174 ? 0.7080 0.6952 0.7576 -0.0611 -0.0201 0.0473  186 SER A C   
1208 O O   . SER A 174 ? 0.7136 0.6963 0.7628 -0.0618 -0.0234 0.0491  186 SER A O   
1209 C CB  . SER A 174 ? 0.7724 0.7714 0.8210 -0.0634 -0.0170 0.0456  186 SER A CB  
1210 O OG  . SER A 174 ? 0.8254 0.8266 0.8751 -0.0612 -0.0139 0.0452  186 SER A OG  
1211 N N   . HIS A 175 ? 0.6907 0.6776 0.7416 -0.0587 -0.0178 0.0469  187 HIS A N   
1212 C CA  . HIS A 175 ? 0.6532 0.6344 0.7054 -0.0565 -0.0188 0.0487  187 HIS A CA  
1213 C C   . HIS A 175 ? 0.6079 0.5846 0.6606 -0.0549 -0.0192 0.0481  187 HIS A C   
1214 O O   . HIS A 175 ? 0.6088 0.5894 0.6623 -0.0539 -0.0161 0.0468  187 HIS A O   
1215 C CB  . HIS A 175 ? 0.6600 0.6456 0.7136 -0.0547 -0.0155 0.0492  187 HIS A CB  
1216 C CG  . HIS A 175 ? 0.6602 0.6412 0.7148 -0.0531 -0.0170 0.0516  187 HIS A CG  
1217 N ND1 . HIS A 175 ? 0.6143 0.5987 0.6701 -0.0516 -0.0145 0.0526  187 HIS A ND1 
1218 C CD2 . HIS A 175 ? 0.6633 0.6361 0.7178 -0.0525 -0.0208 0.0532  187 HIS A CD2 
1219 C CE1 . HIS A 175 ? 0.5903 0.5694 0.6470 -0.0502 -0.0166 0.0548  187 HIS A CE1 
1220 N NE2 . HIS A 175 ? 0.6572 0.6289 0.7131 -0.0506 -0.0205 0.0551  187 HIS A NE2 
1221 N N   . PRO A 176 ? 0.4953 0.4639 0.5466 -0.0535 -0.0228 0.0481  188 PRO A N   
1222 C CA  . PRO A 176 ? 0.4343 0.3998 0.4833 -0.0490 -0.0224 0.0449  188 PRO A CA  
1223 C C   . PRO A 176 ? 0.4061 0.3726 0.4549 -0.0434 -0.0193 0.0438  188 PRO A C   
1224 O O   . PRO A 176 ? 0.3167 0.2846 0.3666 -0.0424 -0.0183 0.0454  188 PRO A O   
1225 C CB  . PRO A 176 ? 0.4274 0.3841 0.4739 -0.0482 -0.0272 0.0446  188 PRO A CB  
1226 C CG  . PRO A 176 ? 0.4894 0.4440 0.5369 -0.0496 -0.0294 0.0474  188 PRO A CG  
1227 C CD  . PRO A 176 ? 0.5099 0.4721 0.5604 -0.0546 -0.0272 0.0498  188 PRO A CD  
1228 N N   . ARG A 177 ? 0.3134 0.2797 0.3607 -0.0398 -0.0178 0.0411  189 ARG A N   
1229 C CA  . ARG A 177 ? 0.2989 0.2674 0.3461 -0.0349 -0.0147 0.0401  189 ARG A CA  
1230 C C   . ARG A 177 ? 0.2886 0.2528 0.3330 -0.0300 -0.0154 0.0373  189 ARG A C   
1231 O O   . ARG A 177 ? 0.3054 0.2659 0.3482 -0.0308 -0.0176 0.0358  189 ARG A O   
1232 C CB  . ARG A 177 ? 0.2917 0.2680 0.3410 -0.0363 -0.0106 0.0403  189 ARG A CB  
1233 C CG  . ARG A 177 ? 0.3215 0.3026 0.3736 -0.0410 -0.0098 0.0430  189 ARG A CG  
1234 C CD  . ARG A 177 ? 0.2980 0.2863 0.3520 -0.0417 -0.0060 0.0430  189 ARG A CD  
1235 N NE  . ARG A 177 ? 0.3502 0.3407 0.4040 -0.0428 -0.0051 0.0411  189 ARG A NE  
1236 C CZ  . ARG A 177 ? 0.3630 0.3591 0.4182 -0.0428 -0.0021 0.0405  189 ARG A CZ  
1237 N NH1 . ARG A 177 ? 0.3320 0.3320 0.3888 -0.0423 0.0002  0.0418  189 ARG A NH1 
1238 N NH2 . ARG A 177 ? 0.3165 0.3139 0.3713 -0.0434 -0.0016 0.0385  189 ARG A NH2 
1239 N N   . GLY A 178 ? 0.3227 0.2506 0.2980 -0.0498 -0.0429 0.0016  190 GLY A N   
1240 C CA  . GLY A 178 ? 0.2722 0.2011 0.2469 -0.0428 -0.0453 -0.0005 190 GLY A CA  
1241 C C   . GLY A 178 ? 0.2582 0.1915 0.2345 -0.0352 -0.0411 -0.0013 190 GLY A C   
1242 O O   . GLY A 178 ? 0.2124 0.1484 0.1913 -0.0355 -0.0363 0.0000  190 GLY A O   
1243 N N   . TRP A 179 ? 0.2325 0.1667 0.2072 -0.0286 -0.0432 -0.0034 191 TRP A N   
1244 C CA  . TRP A 179 ? 0.2179 0.1574 0.1935 -0.0211 -0.0394 -0.0041 191 TRP A CA  
1245 C C   . TRP A 179 ? 0.2559 0.1903 0.2279 -0.0163 -0.0434 -0.0068 191 TRP A C   
1246 O O   . TRP A 179 ? 0.2424 0.1687 0.2101 -0.0165 -0.0505 -0.0090 191 TRP A O   
1247 C CB  . TRP A 179 ? 0.2546 0.1994 0.2300 -0.0168 -0.0387 -0.0047 191 TRP A CB  
1248 C CG  . TRP A 179 ? 0.2693 0.2195 0.2492 -0.0207 -0.0356 -0.0024 191 TRP A CG  
1249 C CD1 . TRP A 179 ? 0.2559 0.2133 0.2411 -0.0207 -0.0288 0.0001  191 TRP A CD1 
1250 C CD2 . TRP A 179 ? 0.2636 0.2126 0.2435 -0.0249 -0.0394 -0.0023 191 TRP A CD2 
1251 N NE1 . TRP A 179 ? 0.2421 0.2031 0.2309 -0.0241 -0.0280 0.0014  191 TRP A NE1 
1252 C CE2 . TRP A 179 ? 0.2401 0.1966 0.2260 -0.0269 -0.0343 0.0001  191 TRP A CE2 
1253 C CE3 . TRP A 179 ? 0.2668 0.2089 0.2425 -0.0273 -0.0470 -0.0040 191 TRP A CE3 
1254 C CZ2 . TRP A 179 ? 0.2572 0.2161 0.2459 -0.0310 -0.0361 0.0008  191 TRP A CZ2 
1255 C CZ3 . TRP A 179 ? 0.2523 0.1963 0.2303 -0.0321 -0.0489 -0.0029 191 TRP A CZ3 
1256 C CH2 . TRP A 179 ? 0.2393 0.1922 0.2240 -0.0338 -0.0433 -0.0005 191 TRP A CH2 
1257 N N   . ASN A 180 ? 0.2532 0.1925 0.2274 -0.0117 -0.0391 -0.0065 192 ASN A N   
1258 C CA  . ASN A 180 ? 0.2383 0.1754 0.2105 -0.0058 -0.0419 -0.0092 192 ASN A CA  
1259 C C   . ASN A 180 ? 0.2452 0.1909 0.2181 0.0016  -0.0374 -0.0099 192 ASN A C   
1260 O O   . ASN A 180 ? 0.2087 0.1619 0.1844 0.0016  -0.0317 -0.0074 192 ASN A O   
1261 C CB  . ASN A 180 ? 0.2024 0.1371 0.1770 -0.0080 -0.0417 -0.0081 192 ASN A CB  
1262 C CG  . ASN A 180 ? 0.2165 0.1595 0.1964 -0.0082 -0.0342 -0.0051 192 ASN A CG  
1263 O OD1 . ASN A 180 ? 0.2030 0.1519 0.1849 -0.0026 -0.0313 -0.0054 192 ASN A OD1 
1264 N ND2 . ASN A 180 ? 0.2493 0.1928 0.2315 -0.0147 -0.0309 -0.0022 192 ASN A ND2 
1265 N N   . ASP A 181 ? 0.2315 0.1759 0.2016 0.0081  -0.0403 -0.0134 193 ASP A N   
1266 C CA  . ASP A 181 ? 0.2380 0.1912 0.2085 0.0153  -0.0359 -0.0142 193 ASP A CA  
1267 C C   . ASP A 181 ? 0.2091 0.1654 0.1835 0.0182  -0.0341 -0.0143 193 ASP A C   
1268 O O   . ASP A 181 ? 0.2312 0.1935 0.2052 0.0251  -0.0323 -0.0163 193 ASP A O   
1269 C CB  . ASP A 181 ? 0.3028 0.2543 0.2668 0.0216  -0.0397 -0.0188 193 ASP A CB  
1270 C CG  . ASP A 181 ? 0.3316 0.2738 0.2922 0.0243  -0.0471 -0.0234 193 ASP A CG  
1271 O OD1 . ASP A 181 ? 0.2772 0.2138 0.2404 0.0209  -0.0498 -0.0227 193 ASP A OD1 
1272 O OD2 . ASP A 181 ? 0.3885 0.3281 0.3433 0.0298  -0.0508 -0.0279 193 ASP A OD2 
1273 N N   . HIS A 182 ? 0.2015 0.1541 0.1794 0.0129  -0.0348 -0.0122 194 HIS A N   
1274 C CA  . HIS A 182 ? 0.2252 0.1796 0.2070 0.0151  -0.0346 -0.0124 194 HIS A CA  
1275 C C   . HIS A 182 ? 0.2139 0.1804 0.2008 0.0177  -0.0271 -0.0097 194 HIS A C   
1276 O O   . HIS A 182 ? 0.1992 0.1703 0.1879 0.0145  -0.0220 -0.0062 194 HIS A O   
1277 C CB  . HIS A 182 ? 0.2412 0.1887 0.2251 0.0080  -0.0373 -0.0102 194 HIS A CB  
1278 C CG  . HIS A 182 ? 0.2909 0.2264 0.2699 0.0046  -0.0450 -0.0120 194 HIS A CG  
1279 N ND1 . HIS A 182 ? 0.3224 0.2506 0.3012 -0.0027 -0.0480 -0.0099 194 HIS A ND1 
1280 C CD2 . HIS A 182 ? 0.3015 0.2307 0.2751 0.0071  -0.0505 -0.0155 194 HIS A CD2 
1281 C CE1 . HIS A 182 ? 0.2750 0.1933 0.2489 -0.0047 -0.0550 -0.0117 194 HIS A CE1 
1282 N NE2 . HIS A 182 ? 0.2925 0.2110 0.2634 0.0011  -0.0568 -0.0151 194 HIS A NE2 
1283 N N   . VAL A 183 ? 0.2077 0.1793 0.1972 0.0236  -0.0267 -0.0115 195 VAL A N   
1284 C CA  . VAL A 183 ? 0.1817 0.1646 0.1773 0.0250  -0.0203 -0.0084 195 VAL A CA  
1285 C C   . VAL A 183 ? 0.1705 0.1518 0.1716 0.0227  -0.0222 -0.0073 195 VAL A C   
1286 O O   . VAL A 183 ? 0.2062 0.1826 0.2071 0.0257  -0.0276 -0.0106 195 VAL A O   
1287 C CB  . VAL A 183 ? 0.1688 0.1613 0.1637 0.0335  -0.0175 -0.0109 195 VAL A CB  
1288 C CG1 . VAL A 183 ? 0.1649 0.1697 0.1667 0.0343  -0.0111 -0.0073 195 VAL A CG1 
1289 C CG2 . VAL A 183 ? 0.1646 0.1584 0.1530 0.0354  -0.0160 -0.0118 195 VAL A CG2 
1290 N N   . HIS A 184 ? 0.1720 0.1566 0.1779 0.0174  -0.0183 -0.0027 196 HIS A N   
1291 C CA  . HIS A 184 ? 0.1818 0.1655 0.1930 0.0149  -0.0200 -0.0013 196 HIS A CA  
1292 C C   . HIS A 184 ? 0.1741 0.1695 0.1922 0.0152  -0.0140 0.0024  196 HIS A C   
1293 O O   . HIS A 184 ? 0.1807 0.1811 0.1992 0.0133  -0.0086 0.0055  196 HIS A O   
1294 C CB  . HIS A 184 ? 0.2314 0.2052 0.2410 0.0063  -0.0227 0.0008  196 HIS A CB  
1295 C CG  . HIS A 184 ? 0.2305 0.1926 0.2347 0.0050  -0.0300 -0.0022 196 HIS A CG  
1296 N ND1 . HIS A 184 ? 0.2518 0.2087 0.2501 0.0044  -0.0316 -0.0039 196 HIS A ND1 
1297 C CD2 . HIS A 184 ? 0.2440 0.1984 0.2480 0.0038  -0.0365 -0.0032 196 HIS A CD2 
1298 C CE1 . HIS A 184 ? 0.2392 0.1855 0.2336 0.0026  -0.0387 -0.0058 196 HIS A CE1 
1299 N NE2 . HIS A 184 ? 0.2377 0.1820 0.2353 0.0023  -0.0419 -0.0054 196 HIS A NE2 
1300 N N   . ILE A 185 ? 0.1853 0.1850 0.2094 0.0175  -0.0153 0.0023  197 ILE A N   
1301 C CA  . ILE A 185 ? 0.1640 0.1748 0.1958 0.0170  -0.0104 0.0061  197 ILE A CA  
1302 C C   . ILE A 185 ? 0.1735 0.1792 0.2088 0.0099  -0.0127 0.0091  197 ILE A C   
1303 O O   . ILE A 185 ? 0.1670 0.1661 0.2027 0.0095  -0.0187 0.0073  197 ILE A O   
1304 C CB  . ILE A 185 ? 0.1997 0.2212 0.2368 0.0248  -0.0097 0.0040  197 ILE A CB  
1305 C CG1 . ILE A 185 ? 0.2287 0.2564 0.2614 0.0317  -0.0065 0.0011  197 ILE A CG1 
1306 C CG2 . ILE A 185 ? 0.2129 0.2455 0.2591 0.0227  -0.0056 0.0086  197 ILE A CG2 
1307 C CD1 . ILE A 185 ? 0.2313 0.2676 0.2673 0.0406  -0.0068 -0.0029 197 ILE A CD1 
1308 N N   . LEU A 186 ? 0.1582 0.1664 0.1958 0.0044  -0.0084 0.0135  198 LEU A N   
1309 C CA  . LEU A 186 ? 0.1948 0.2016 0.2370 -0.0014 -0.0096 0.0166  198 LEU A CA  
1310 C C   . LEU A 186 ? 0.1840 0.2043 0.2349 0.0006  -0.0055 0.0197  198 LEU A C   
1311 O O   . LEU A 186 ? 0.1870 0.2143 0.2389 0.0004  0.0002  0.0225  198 LEU A O   
1312 C CB  . LEU A 186 ? 0.1720 0.1714 0.2106 -0.0092 -0.0080 0.0191  198 LEU A CB  
1313 C CG  . LEU A 186 ? 0.2091 0.2030 0.2494 -0.0164 -0.0103 0.0215  198 LEU A CG  
1314 C CD1 . LEU A 186 ? 0.2592 0.2620 0.3071 -0.0181 -0.0068 0.0256  198 LEU A CD1 
1315 C CD2 . LEU A 186 ? 0.2006 0.1883 0.2406 -0.0167 -0.0174 0.0195  198 LEU A CD2 
1316 N N   . ASP A 187 ? 0.2331 0.2572 0.2903 0.0024  -0.0087 0.0194  199 ASP A N   
1317 C CA  . ASP A 187 ? 0.2090 0.2472 0.2759 0.0043  -0.0055 0.0222  199 ASP A CA  
1318 C C   . ASP A 187 ? 0.1982 0.2346 0.2690 -0.0039 -0.0057 0.0269  199 ASP A C   
1319 O O   . ASP A 187 ? 0.2223 0.2514 0.2937 -0.0074 -0.0111 0.0267  199 ASP A O   
1320 C CB  . ASP A 187 ? 0.2273 0.2708 0.2999 0.0109  -0.0093 0.0191  199 ASP A CB  
1321 C CG  . ASP A 187 ? 0.2377 0.2979 0.3212 0.0136  -0.0056 0.0217  199 ASP A CG  
1322 O OD1 . ASP A 187 ? 0.2183 0.2840 0.3060 0.0083  -0.0019 0.0269  199 ASP A OD1 
1323 O OD2 . ASP A 187 ? 0.2642 0.3321 0.3524 0.0211  -0.0066 0.0185  199 ASP A OD2 
1324 N N   . THR A 188 ? 0.2012 0.2437 0.2744 -0.0070 -0.0003 0.0312  200 THR A N   
1325 C CA  . THR A 188 ? 0.2133 0.2531 0.2897 -0.0149 -0.0007 0.0355  200 THR A CA  
1326 C C   . THR A 188 ? 0.2044 0.2537 0.2914 -0.0153 -0.0023 0.0380  200 THR A C   
1327 O O   . THR A 188 ? 0.1814 0.2282 0.2712 -0.0221 -0.0034 0.0415  200 THR A O   
1328 C CB  . THR A 188 ? 0.2241 0.2657 0.2994 -0.0185 0.0049  0.0394  200 THR A CB  
1329 O OG1 . THR A 188 ? 0.2363 0.2924 0.3167 -0.0141 0.0099  0.0416  200 THR A OG1 
1330 C CG2 . THR A 188 ? 0.2401 0.2716 0.3057 -0.0190 0.0060  0.0372  200 THR A CG2 
1331 N N   . GLU A 189 ? 0.1897 0.2500 0.2829 -0.0083 -0.0025 0.0363  201 GLU A N   
1332 C CA  . GLU A 189 ? 0.1604 0.2288 0.2643 -0.0087 -0.0052 0.0383  201 GLU A CA  
1333 C C   . GLU A 189 ? 0.1775 0.2340 0.2799 -0.0117 -0.0132 0.0365  201 GLU A C   
1334 O O   . GLU A 189 ? 0.2329 0.2910 0.3418 -0.0160 -0.0163 0.0394  201 GLU A O   
1335 C CB  . GLU A 189 ? 0.2448 0.3287 0.3564 0.0001  -0.0033 0.0363  201 GLU A CB  
1336 C CG  . GLU A 189 ? 0.1699 0.2697 0.2864 0.0015  0.0045  0.0400  201 GLU A CG  
1337 C CD  . GLU A 189 ? 0.2000 0.3136 0.3198 0.0115  0.0077  0.0365  201 GLU A CD  
1338 O OE1 . GLU A 189 ? 0.2344 0.3481 0.3565 0.0177  0.0036  0.0318  201 GLU A OE1 
1339 O OE2 . GLU A 189 ? 0.2403 0.3647 0.3600 0.0130  0.0144  0.0386  201 GLU A OE2 
1340 N N   . THR A 190 ? 0.2388 0.2833 0.3324 -0.0099 -0.0168 0.0321  202 THR A N   
1341 C CA  . THR A 190 ? 0.2064 0.2392 0.2975 -0.0126 -0.0247 0.0307  202 THR A CA  
1342 C C   . THR A 190 ? 0.2626 0.2791 0.3415 -0.0176 -0.0267 0.0291  202 THR A C   
1343 O O   . THR A 190 ? 0.2458 0.2519 0.3212 -0.0205 -0.0333 0.0281  202 THR A O   
1344 C CB  . THR A 190 ? 0.2223 0.2572 0.3166 -0.0045 -0.0293 0.0266  202 THR A CB  
1345 O OG1 . THR A 190 ? 0.2565 0.2902 0.3445 0.0016  -0.0269 0.0224  202 THR A OG1 
1346 C CG2 . THR A 190 ? 0.2219 0.2736 0.3298 0.0003  -0.0282 0.0278  202 THR A CG2 
1347 N N   . PHE A 191 ? 0.2019 0.2162 0.2744 -0.0187 -0.0214 0.0291  203 PHE A N   
1348 C CA  . PHE A 191 ? 0.2335 0.2343 0.2950 -0.0221 -0.0226 0.0270  203 PHE A CA  
1349 C C   . PHE A 191 ? 0.2871 0.2808 0.3446 -0.0184 -0.0286 0.0230  203 PHE A C   
1350 O O   . PHE A 191 ? 0.2751 0.2575 0.3272 -0.0229 -0.0341 0.0224  203 PHE A O   
1351 C CB  . PHE A 191 ? 0.2633 0.2548 0.3209 -0.0313 -0.0241 0.0293  203 PHE A CB  
1352 C CG  . PHE A 191 ? 0.2630 0.2594 0.3237 -0.0351 -0.0187 0.0329  203 PHE A CG  
1353 C CD1 . PHE A 191 ? 0.2614 0.2565 0.3176 -0.0356 -0.0133 0.0329  203 PHE A CD1 
1354 C CD2 . PHE A 191 ? 0.3222 0.3247 0.3909 -0.0378 -0.0194 0.0364  203 PHE A CD2 
1355 C CE1 . PHE A 191 ? 0.2896 0.2883 0.3487 -0.0388 -0.0089 0.0364  203 PHE A CE1 
1356 C CE2 . PHE A 191 ? 0.3091 0.3153 0.3805 -0.0414 -0.0149 0.0399  203 PHE A CE2 
1357 C CZ  . PHE A 191 ? 0.2795 0.2835 0.3460 -0.0418 -0.0097 0.0399  203 PHE A CZ  
1358 N N   . THR A 192 ? 0.2236 0.2242 0.2835 -0.0100 -0.0277 0.0202  204 THR A N   
1359 C CA  . THR A 192 ? 0.2401 0.2343 0.2965 -0.0052 -0.0333 0.0159  204 THR A CA  
1360 C C   . THR A 192 ? 0.1964 0.1895 0.2463 -0.0011 -0.0304 0.0128  204 THR A C   
1361 O O   . THR A 192 ? 0.1892 0.1926 0.2415 0.0036  -0.0247 0.0127  204 THR A O   
1362 C CB  . THR A 192 ? 0.2523 0.2553 0.3178 0.0022  -0.0360 0.0144  204 THR A CB  
1363 O OG1 . THR A 192 ? 0.2449 0.2490 0.3170 -0.0018 -0.0396 0.0174  204 THR A OG1 
1364 C CG2 . THR A 192 ? 0.2418 0.2371 0.3034 0.0078  -0.0423 0.0095  204 THR A CG2 
1365 N N   . TRP A 193 ? 0.1849 0.1655 0.2264 -0.0033 -0.0346 0.0107  205 TRP A N   
1366 C CA  . TRP A 193 ? 0.2369 0.2148 0.2719 0.0004  -0.0336 0.0074  205 TRP A CA  
1367 C C   . TRP A 193 ? 0.2371 0.2171 0.2737 0.0095  -0.0371 0.0030  205 TRP A C   
1368 O O   . TRP A 193 ? 0.2783 0.2540 0.3172 0.0111  -0.0436 0.0016  205 TRP A O   
1369 C CB  . TRP A 193 ? 0.2396 0.2038 0.2658 -0.0057 -0.0374 0.0069  205 TRP A CB  
1370 C CG  . TRP A 193 ? 0.2602 0.2220 0.2833 -0.0136 -0.0332 0.0100  205 TRP A CG  
1371 C CD1 . TRP A 193 ? 0.2669 0.2221 0.2882 -0.0216 -0.0350 0.0124  205 TRP A CD1 
1372 C CD2 . TRP A 193 ? 0.2344 0.2002 0.2557 -0.0141 -0.0267 0.0108  205 TRP A CD2 
1373 N NE1 . TRP A 193 ? 0.2279 0.1829 0.2465 -0.0265 -0.0297 0.0141  205 TRP A NE1 
1374 C CE2 . TRP A 193 ? 0.2172 0.1785 0.2362 -0.0219 -0.0248 0.0133  205 TRP A CE2 
1375 C CE3 . TRP A 193 ? 0.2396 0.2121 0.2609 -0.0085 -0.0225 0.0095  205 TRP A CE3 
1376 C CZ2 . TRP A 193 ? 0.2324 0.1958 0.2501 -0.0239 -0.0190 0.0144  205 TRP A CZ2 
1377 C CZ3 . TRP A 193 ? 0.2217 0.1962 0.2413 -0.0109 -0.0170 0.0112  205 TRP A CZ3 
1378 C CH2 . TRP A 193 ? 0.1968 0.1667 0.2151 -0.0183 -0.0154 0.0136  205 TRP A CH2 
1379 N N   . SER A 194 ? 0.2029 0.1889 0.2379 0.0155  -0.0332 0.0006  206 SER A N   
1380 C CA  . SER A 194 ? 0.2109 0.1971 0.2450 0.0241  -0.0364 -0.0046 206 SER A CA  
1381 C C   . SER A 194 ? 0.1918 0.1768 0.2184 0.0263  -0.0337 -0.0069 206 SER A C   
1382 O O   . SER A 194 ? 0.2199 0.2056 0.2436 0.0216  -0.0291 -0.0041 206 SER A O   
1383 C CB  . SER A 194 ? 0.2251 0.2253 0.2682 0.0317  -0.0337 -0.0056 206 SER A CB  
1384 O OG  . SER A 194 ? 0.2416 0.2546 0.2866 0.0328  -0.0252 -0.0034 206 SER A OG  
1385 N N   . GLN A 195 ? 0.2180 0.2009 0.2415 0.0337  -0.0371 -0.0121 207 GLN A N   
1386 C CA  . GLN A 195 ? 0.2484 0.2315 0.2650 0.0368  -0.0347 -0.0147 207 GLN A CA  
1387 C C   . GLN A 195 ? 0.2449 0.2377 0.2633 0.0471  -0.0327 -0.0190 207 GLN A C   
1388 O O   . GLN A 195 ? 0.2655 0.2566 0.2866 0.0528  -0.0375 -0.0229 207 GLN A O   
1389 C CB  . GLN A 195 ? 0.2722 0.2405 0.2804 0.0347  -0.0415 -0.0174 207 GLN A CB  
1390 C CG  . GLN A 195 ? 0.2513 0.2105 0.2567 0.0247  -0.0431 -0.0136 207 GLN A CG  
1391 C CD  . GLN A 195 ? 0.3464 0.2934 0.3436 0.0226  -0.0486 -0.0159 207 GLN A CD  
1392 O OE1 . GLN A 195 ? 0.3408 0.2770 0.3358 0.0217  -0.0563 -0.0176 207 GLN A OE1 
1393 N NE2 . GLN A 195 ? 0.3054 0.2542 0.2984 0.0217  -0.0451 -0.0157 207 GLN A NE2 
1394 N N   . PRO A 196 ? 0.2660 0.2693 0.2832 0.0498  -0.0258 -0.0185 208 PRO A N   
1395 C CA  . PRO A 196 ? 0.2397 0.2526 0.2572 0.0596  -0.0235 -0.0230 208 PRO A CA  
1396 C C   . PRO A 196 ? 0.2934 0.2968 0.3020 0.0648  -0.0287 -0.0294 208 PRO A C   
1397 O O   . PRO A 196 ? 0.3025 0.2956 0.3039 0.0605  -0.0316 -0.0293 208 PRO A O   
1398 C CB  . PRO A 196 ? 0.2537 0.2794 0.2712 0.0589  -0.0146 -0.0193 208 PRO A CB  
1399 C CG  . PRO A 196 ? 0.2307 0.2478 0.2428 0.0509  -0.0147 -0.0158 208 PRO A CG  
1400 C CD  . PRO A 196 ? 0.2642 0.2698 0.2783 0.0443  -0.0203 -0.0142 208 PRO A CD  
1401 N N   . ILE A 197 ? 0.2796 0.2868 0.2892 0.0741  -0.0301 -0.0351 209 ILE A N   
1402 C CA  . ILE A 197 ? 0.3259 0.3259 0.3267 0.0805  -0.0343 -0.0420 209 ILE A CA  
1403 C C   . ILE A 197 ? 0.3185 0.3288 0.3140 0.0834  -0.0271 -0.0423 209 ILE A C   
1404 O O   . ILE A 197 ? 0.3665 0.3919 0.3658 0.0888  -0.0208 -0.0427 209 ILE A O   
1405 C CB  . ILE A 197 ? 0.3573 0.3569 0.3612 0.0900  -0.0387 -0.0486 209 ILE A CB  
1406 C CG1 . ILE A 197 ? 0.3344 0.3256 0.3449 0.0869  -0.0455 -0.0472 209 ILE A CG1 
1407 C CG2 . ILE A 197 ? 0.3417 0.3316 0.3355 0.0963  -0.0439 -0.0561 209 ILE A CG2 
1408 C CD1 . ILE A 197 ? 0.3988 0.3705 0.4027 0.0816  -0.0546 -0.0478 209 ILE A CD1 
1409 N N   . THR A 198 ? 0.3549 0.3579 0.3418 0.0797  -0.0282 -0.0418 210 THR A N   
1410 C CA  . THR A 198 ? 0.3400 0.3518 0.3211 0.0816  -0.0221 -0.0413 210 THR A CA  
1411 C C   . THR A 198 ? 0.3832 0.3908 0.3548 0.0894  -0.0255 -0.0490 210 THR A C   
1412 O O   . THR A 198 ? 0.3727 0.3669 0.3407 0.0912  -0.0336 -0.0539 210 THR A O   
1413 C CB  . THR A 198 ? 0.3372 0.3453 0.3153 0.0729  -0.0207 -0.0356 210 THR A CB  
1414 O OG1 . THR A 198 ? 0.3259 0.3190 0.2971 0.0704  -0.0280 -0.0382 210 THR A OG1 
1415 C CG2 . THR A 198 ? 0.3143 0.3241 0.3009 0.0650  -0.0183 -0.0288 210 THR A CG2 
1416 N N   . THR A 199 ? 0.3656 0.3844 0.3328 0.0939  -0.0194 -0.0499 211 THR A N   
1417 C CA  . THR A 199 ? 0.3676 0.3827 0.3237 0.1001  -0.0218 -0.0564 211 THR A CA  
1418 C C   . THR A 199 ? 0.3643 0.3791 0.3130 0.0951  -0.0197 -0.0526 211 THR A C   
1419 O O   . THR A 199 ? 0.3525 0.3730 0.3053 0.0885  -0.0149 -0.0453 211 THR A O   
1420 C CB  . THR A 199 ? 0.3942 0.4226 0.3495 0.1102  -0.0168 -0.0615 211 THR A CB  
1421 O OG1 . THR A 199 ? 0.3810 0.4262 0.3388 0.1087  -0.0072 -0.0558 211 THR A OG1 
1422 C CG2 . THR A 199 ? 0.3862 0.4160 0.3503 0.1156  -0.0188 -0.0651 211 THR A CG2 
1423 N N   . GLY A 200 ? 0.4206 0.4280 0.3585 0.0984  -0.0240 -0.0578 212 GLY A N   
1424 C CA  . GLY A 200 ? 0.4030 0.4097 0.3335 0.0945  -0.0231 -0.0550 212 GLY A CA  
1425 C C   . GLY A 200 ? 0.4592 0.4523 0.3894 0.0864  -0.0294 -0.0523 212 GLY A C   
1426 O O   . GLY A 200 ? 0.4303 0.4153 0.3664 0.0823  -0.0335 -0.0513 212 GLY A O   
1427 N N   . LYS A 201 ? 0.6340 0.6251 0.5570 0.0838  -0.0302 -0.0510 213 LYS A N   
1428 C CA  . LYS A 201 ? 0.5618 0.5424 0.4849 0.0759  -0.0353 -0.0479 213 LYS A CA  
1429 C C   . LYS A 201 ? 0.5064 0.4919 0.4389 0.0683  -0.0304 -0.0399 213 LYS A C   
1430 O O   . LYS A 201 ? 0.4944 0.4900 0.4282 0.0670  -0.0240 -0.0350 213 LYS A O   
1431 C CB  . LYS A 201 ? 0.6234 0.6022 0.5370 0.0758  -0.0372 -0.0486 213 LYS A CB  
1432 C CG  . LYS A 201 ? 0.5874 0.5588 0.5023 0.0674  -0.0411 -0.0445 213 LYS A CG  
1433 C CD  . LYS A 201 ? 0.5767 0.5574 0.4957 0.0627  -0.0347 -0.0369 213 LYS A CD  
1434 C CE  . LYS A 201 ? 0.5622 0.5368 0.4826 0.0553  -0.0385 -0.0335 213 LYS A CE  
1435 N NZ  . LYS A 201 ? 0.5550 0.5192 0.4799 0.0501  -0.0439 -0.0340 213 LYS A NZ  
1436 N N   . ALA A 202 ? 0.4524 0.4308 0.3913 0.0634  -0.0336 -0.0385 214 ALA A N   
1437 C CA  . ALA A 202 ? 0.3624 0.3431 0.3090 0.0557  -0.0300 -0.0315 214 ALA A CA  
1438 C C   . ALA A 202 ? 0.3913 0.3684 0.3353 0.0502  -0.0315 -0.0287 214 ALA A C   
1439 O O   . ALA A 202 ? 0.3643 0.3337 0.3019 0.0506  -0.0375 -0.0321 214 ALA A O   
1440 C CB  . ALA A 202 ? 0.3570 0.3303 0.3096 0.0517  -0.0335 -0.0311 214 ALA A CB  
1441 N N   . PRO A 203 ? 0.3031 0.2858 0.2523 0.0451  -0.0265 -0.0225 215 PRO A N   
1442 C CA  . PRO A 203 ? 0.2813 0.2607 0.2301 0.0397  -0.0282 -0.0198 215 PRO A CA  
1443 C C   . PRO A 203 ? 0.2801 0.2482 0.2296 0.0347  -0.0347 -0.0212 215 PRO A C   
1444 O O   . PRO A 203 ? 0.3195 0.2829 0.2718 0.0336  -0.0366 -0.0224 215 PRO A O   
1445 C CB  . PRO A 203 ? 0.2510 0.2376 0.2070 0.0354  -0.0215 -0.0133 215 PRO A CB  
1446 C CG  . PRO A 203 ? 0.2738 0.2691 0.2320 0.0394  -0.0160 -0.0124 215 PRO A CG  
1447 C CD  . PRO A 203 ? 0.3114 0.3033 0.2677 0.0440  -0.0194 -0.0178 215 PRO A CD  
1448 N N   . SER A 204 ? 0.2649 0.2292 0.2120 0.0315  -0.0382 -0.0209 216 SER A N   
1449 C CA  . SER A 204 ? 0.2856 0.2408 0.2342 0.0252  -0.0436 -0.0209 216 SER A CA  
1450 C C   . SER A 204 ? 0.2331 0.1897 0.1896 0.0195  -0.0397 -0.0167 216 SER A C   
1451 O O   . SER A 204 ? 0.2322 0.1967 0.1932 0.0193  -0.0331 -0.0130 216 SER A O   
1452 C CB  . SER A 204 ? 0.2925 0.2465 0.2393 0.0220  -0.0465 -0.0199 216 SER A CB  
1453 O OG  . SER A 204 ? 0.2976 0.2589 0.2504 0.0186  -0.0410 -0.0147 216 SER A OG  
1454 N N   . PRO A 205 ? 0.2693 0.2179 0.2271 0.0145  -0.0439 -0.0171 217 PRO A N   
1455 C CA  . PRO A 205 ? 0.2376 0.1872 0.2018 0.0081  -0.0404 -0.0131 217 PRO A CA  
1456 C C   . PRO A 205 ? 0.2562 0.2117 0.2242 0.0046  -0.0362 -0.0094 217 PRO A C   
1457 O O   . PRO A 205 ? 0.2254 0.1813 0.1913 0.0047  -0.0384 -0.0097 217 PRO A O   
1458 C CB  . PRO A 205 ? 0.2598 0.1991 0.2226 0.0027  -0.0469 -0.0142 217 PRO A CB  
1459 C CG  . PRO A 205 ? 0.3089 0.2412 0.2654 0.0076  -0.0538 -0.0190 217 PRO A CG  
1460 C CD  . PRO A 205 ? 0.2629 0.2007 0.2157 0.0142  -0.0523 -0.0210 217 PRO A CD  
1461 N N   . ARG A 206 ? 0.2279 0.1880 0.2017 0.0019  -0.0303 -0.0059 218 ARG A N   
1462 C CA  . ARG A 206 ? 0.2304 0.1963 0.2085 -0.0005 -0.0259 -0.0025 218 ARG A CA  
1463 C C   . ARG A 206 ? 0.1830 0.1509 0.1668 -0.0043 -0.0206 0.0004  218 ARG A C   
1464 O O   . ARG A 206 ? 0.1828 0.1498 0.1673 -0.0039 -0.0194 0.0004  218 ARG A O   
1465 C CB  . ARG A 206 ? 0.2191 0.1919 0.1960 0.0051  -0.0230 -0.0017 218 ARG A CB  
1466 C CG  . ARG A 206 ? 0.1820 0.1592 0.1584 0.0099  -0.0194 -0.0015 218 ARG A CG  
1467 C CD  . ARG A 206 ? 0.1819 0.1652 0.1546 0.0155  -0.0179 -0.0012 218 ARG A CD  
1468 N NE  . ARG A 206 ? 0.2613 0.2412 0.2267 0.0191  -0.0233 -0.0054 218 ARG A NE  
1469 C CZ  . ARG A 206 ? 0.2630 0.2461 0.2236 0.0227  -0.0238 -0.0056 218 ARG A CZ  
1470 N NH1 . ARG A 206 ? 0.2790 0.2690 0.2416 0.0231  -0.0194 -0.0015 218 ARG A NH1 
1471 N NH2 . ARG A 206 ? 0.2883 0.2670 0.2417 0.0257  -0.0294 -0.0100 218 ARG A NH2 
1472 N N   . ALA A 207 ? 0.1589 0.1300 0.1471 -0.0075 -0.0175 0.0029  219 ALA A N   
1473 C CA  . ALA A 207 ? 0.1515 0.1249 0.1451 -0.0106 -0.0121 0.0055  219 ALA A CA  
1474 C C   . ALA A 207 ? 0.1842 0.1637 0.1817 -0.0091 -0.0081 0.0081  219 ALA A C   
1475 O O   . ALA A 207 ? 0.2016 0.1833 0.1983 -0.0072 -0.0099 0.0081  219 ALA A O   
1476 C CB  . ALA A 207 ? 0.1877 0.1569 0.1828 -0.0175 -0.0129 0.0053  219 ALA A CB  
1477 N N   . ALA A 208 ? 0.1519 0.1336 0.1535 -0.0100 -0.0031 0.0105  220 ALA A N   
1478 C CA  . ALA A 208 ? 0.1286 0.1150 0.1346 -0.0088 0.0006  0.0133  220 ALA A CA  
1479 C C   . ALA A 208 ? 0.1600 0.1507 0.1634 -0.0032 0.0005  0.0147  220 ALA A C   
1480 O O   . ALA A 208 ? 0.1729 0.1671 0.1784 -0.0016 0.0016  0.0168  220 ALA A O   
1481 C CB  . ALA A 208 ? 0.1386 0.1258 0.1482 -0.0113 0.0001  0.0131  220 ALA A CB  
1482 N N   . HIS A 209 ? 0.1746 0.1652 0.1733 -0.0002 -0.0010 0.0133  221 HIS A N   
1483 C CA  . HIS A 209 ? 0.1885 0.1840 0.1842 0.0049  0.0003  0.0146  221 HIS A CA  
1484 C C   . HIS A 209 ? 0.2029 0.2019 0.2026 0.0046  0.0054  0.0185  221 HIS A C   
1485 O O   . HIS A 209 ? 0.1967 0.1935 0.2008 0.0008  0.0075  0.0194  221 HIS A O   
1486 C CB  . HIS A 209 ? 0.1631 0.1578 0.1533 0.0082  -0.0024 0.0114  221 HIS A CB  
1487 C CG  . HIS A 209 ? 0.1968 0.1878 0.1885 0.0059  -0.0028 0.0098  221 HIS A CG  
1488 N ND1 . HIS A 209 ? 0.1725 0.1571 0.1649 0.0014  -0.0057 0.0080  221 HIS A ND1 
1489 C CD2 . HIS A 209 ? 0.1923 0.1851 0.1849 0.0072  -0.0010 0.0101  221 HIS A CD2 
1490 C CE1 . HIS A 209 ? 0.1979 0.1799 0.1910 0.0000  -0.0059 0.0073  221 HIS A CE1 
1491 N NE2 . HIS A 209 ? 0.1895 0.1766 0.1831 0.0037  -0.0032 0.0083  221 HIS A NE2 
1492 N N   . ALA A 210 ? 0.1551 0.1596 0.1528 0.0083  0.0072  0.0208  222 ALA A N   
1493 C CA  . ALA A 210 ? 0.1575 0.1656 0.1588 0.0077  0.0117  0.0248  222 ALA A CA  
1494 C C   . ALA A 210 ? 0.2088 0.2222 0.2068 0.0114  0.0128  0.0247  222 ALA A C   
1495 O O   . ALA A 210 ? 0.1532 0.1696 0.1456 0.0155  0.0114  0.0231  222 ALA A O   
1496 C CB  . ALA A 210 ? 0.1714 0.1817 0.1748 0.0078  0.0136  0.0292  222 ALA A CB  
1497 N N   . CYS A 211 ? 0.1623 0.1772 0.1639 0.0098  0.0154  0.0262  223 CYS A N   
1498 C CA  . CYS A 211 ? 0.1729 0.1944 0.1735 0.0128  0.0172  0.0265  223 CYS A CA  
1499 C C   . CYS A 211 ? 0.1731 0.2006 0.1770 0.0118  0.0216  0.0323  223 CYS A C   
1500 O O   . CYS A 211 ? 0.2065 0.2312 0.2150 0.0078  0.0231  0.0355  223 CYS A O   
1501 C CB  . CYS A 211 ? 0.1786 0.1976 0.1816 0.0116  0.0159  0.0236  223 CYS A CB  
1502 S SG  . CYS A 211 ? 0.1923 0.2039 0.1910 0.0128  0.0100  0.0171  223 CYS A SG  
1503 N N   . ALA A 212 ? 0.1279 0.1639 0.1292 0.0154  0.0238  0.0336  224 ALA A N   
1504 C CA  . ALA A 212 ? 0.1830 0.2259 0.1872 0.0141  0.0280  0.0395  224 ALA A CA  
1505 C C   . ALA A 212 ? 0.1794 0.2318 0.1828 0.0176  0.0302  0.0388  224 ALA A C   
1506 O O   . ALA A 212 ? 0.1657 0.2205 0.1637 0.0225  0.0289  0.0344  224 ALA A O   
1507 C CB  . ALA A 212 ? 0.2063 0.2512 0.2073 0.0146  0.0290  0.0438  224 ALA A CB  
1508 N N   . THR A 213 ? 0.1894 0.2475 0.1984 0.0151  0.0334  0.0429  225 THR A N   
1509 C CA  . THR A 213 ? 0.2018 0.2704 0.2120 0.0181  0.0359  0.0425  225 THR A CA  
1510 C C   . THR A 213 ? 0.1508 0.2299 0.1610 0.0176  0.0405  0.0489  225 THR A C   
1511 O O   . THR A 213 ? 0.1730 0.2510 0.1874 0.0126  0.0419  0.0548  225 THR A O   
1512 C CB  . THR A 213 ? 0.1929 0.2611 0.2109 0.0154  0.0356  0.0420  225 THR A CB  
1513 O OG1 . THR A 213 ? 0.1855 0.2429 0.2034 0.0145  0.0311  0.0371  225 THR A OG1 
1514 C CG2 . THR A 213 ? 0.1812 0.2608 0.2013 0.0195  0.0376  0.0405  225 THR A CG2 
1515 N N   . VAL A 214 ? 0.1525 0.2414 0.1578 0.0225  0.0427  0.0478  226 VAL A N   
1516 C CA  . VAL A 214 ? 0.1408 0.2422 0.1462 0.0221  0.0477  0.0536  226 VAL A CA  
1517 C C   . VAL A 214 ? 0.2487 0.3617 0.2557 0.0267  0.0503  0.0503  226 VAL A C   
1518 O O   . VAL A 214 ? 0.2558 0.3697 0.2570 0.0328  0.0491  0.0439  226 VAL A O   
1519 C CB  . VAL A 214 ? 0.1949 0.2985 0.1914 0.0237  0.0486  0.0562  226 VAL A CB  
1520 C CG1 . VAL A 214 ? 0.2598 0.3757 0.2567 0.0216  0.0537  0.0638  226 VAL A CG1 
1521 C CG2 . VAL A 214 ? 0.1485 0.2401 0.1434 0.0208  0.0451  0.0578  226 VAL A CG2 
1522 N N   . GLY A 215 ? 0.2582 0.3802 0.2732 0.0239  0.0535  0.0545  227 GLY A N   
1523 C CA  . GLY A 215 ? 0.2976 0.4319 0.3159 0.0283  0.0562  0.0515  227 GLY A CA  
1524 C C   . GLY A 215 ? 0.2356 0.3631 0.2555 0.0321  0.0519  0.0435  227 GLY A C   
1525 O O   . GLY A 215 ? 0.2379 0.3547 0.2623 0.0285  0.0481  0.0427  227 GLY A O   
1526 N N   . ASN A 216 ? 0.2403 0.3738 0.2562 0.0396  0.0523  0.0373  228 ASN A N   
1527 C CA  . ASN A 216 ? 0.2723 0.3991 0.2885 0.0442  0.0477  0.0293  228 ASN A CA  
1528 C C   . ASN A 216 ? 0.1961 0.3109 0.2021 0.0471  0.0433  0.0239  228 ASN A C   
1529 O O   . ASN A 216 ? 0.2064 0.3180 0.2096 0.0528  0.0400  0.0166  228 ASN A O   
1530 C CB  . ASN A 216 ? 0.2661 0.4063 0.2850 0.0511  0.0505  0.0252  228 ASN A CB  
1531 C CG  . ASN A 216 ? 0.2803 0.4284 0.2894 0.0574  0.0536  0.0223  228 ASN A CG  
1532 O OD1 . ASN A 216 ? 0.2201 0.3646 0.2205 0.0560  0.0539  0.0244  228 ASN A OD1 
1533 N ND2 . ASN A 216 ? 0.2944 0.4535 0.3047 0.0646  0.0558  0.0173  228 ASN A ND2 
1534 N N   . ARG A 217 ? 0.1834 0.2917 0.1841 0.0435  0.0427  0.0272  229 ARG A N   
1535 C CA  . ARG A 217 ? 0.1570 0.2545 0.1489 0.0456  0.0382  0.0228  229 ARG A CA  
1536 C C   . ARG A 217 ? 0.1438 0.2281 0.1383 0.0395  0.0344  0.0246  229 ARG A C   
1537 O O   . ARG A 217 ? 0.1798 0.2635 0.1772 0.0341  0.0362  0.0308  229 ARG A O   
1538 C CB  . ARG A 217 ? 0.2208 0.3230 0.2033 0.0476  0.0404  0.0245  229 ARG A CB  
1539 C CG  . ARG A 217 ? 0.2209 0.3350 0.1984 0.0546  0.0437  0.0209  229 ARG A CG  
1540 C CD  . ARG A 217 ? 0.2180 0.3347 0.1841 0.0567  0.0449  0.0216  229 ARG A CD  
1541 N NE  . ARG A 217 ? 0.2608 0.3920 0.2227 0.0621  0.0500  0.0202  229 ARG A NE  
1542 C CZ  . ARG A 217 ? 0.2821 0.4173 0.2327 0.0655  0.0513  0.0191  229 ARG A CZ  
1543 N NH1 . ARG A 217 ? 0.3246 0.4502 0.2670 0.0643  0.0472  0.0193  229 ARG A NH1 
1544 N NH2 . ARG A 217 ? 0.2774 0.4272 0.2247 0.0702  0.0567  0.0179  229 ARG A NH2 
1545 N N   . GLY A 218 ? 0.1561 0.2299 0.1496 0.0403  0.0291  0.0191  230 GLY A N   
1546 C CA  . GLY A 218 ? 0.1644 0.2263 0.1596 0.0348  0.0257  0.0201  230 GLY A CA  
1547 C C   . GLY A 218 ? 0.1607 0.2156 0.1482 0.0357  0.0224  0.0179  230 GLY A C   
1548 O O   . GLY A 218 ? 0.2197 0.2693 0.2025 0.0392  0.0182  0.0120  230 GLY A O   
1549 N N   . PHE A 219 ? 0.1503 0.2049 0.1366 0.0328  0.0239  0.0226  231 PHE A N   
1550 C CA  . PHE A 219 ? 0.1853 0.2345 0.1650 0.0336  0.0208  0.0212  231 PHE A CA  
1551 C C   . PHE A 219 ? 0.2013 0.2394 0.1835 0.0296  0.0166  0.0196  231 PHE A C   
1552 O O   . PHE A 219 ? 0.1764 0.2112 0.1652 0.0251  0.0172  0.0216  231 PHE A O   
1553 C CB  . PHE A 219 ? 0.1937 0.2472 0.1716 0.0322  0.0236  0.0272  231 PHE A CB  
1554 C CG  . PHE A 219 ? 0.1991 0.2639 0.1727 0.0358  0.0276  0.0291  231 PHE A CG  
1555 C CD1 . PHE A 219 ? 0.1792 0.2464 0.1431 0.0407  0.0265  0.0260  231 PHE A CD1 
1556 C CD2 . PHE A 219 ? 0.2076 0.2809 0.1865 0.0341  0.0325  0.0339  231 PHE A CD2 
1557 C CE1 . PHE A 219 ? 0.2135 0.2917 0.1727 0.0440  0.0307  0.0275  231 PHE A CE1 
1558 C CE2 . PHE A 219 ? 0.1952 0.2802 0.1700 0.0371  0.0367  0.0359  231 PHE A CE2 
1559 C CZ  . PHE A 219 ? 0.2519 0.3395 0.2167 0.0421  0.0360  0.0327  231 PHE A CZ  
1560 N N   . VAL A 220 ? 0.1589 0.1914 0.1355 0.0311  0.0123  0.0161  232 VAL A N   
1561 C CA  . VAL A 220 ? 0.2246 0.2480 0.2035 0.0269  0.0087  0.0153  232 VAL A CA  
1562 C C   . VAL A 220 ? 0.1997 0.2214 0.1732 0.0280  0.0059  0.0149  232 VAL A C   
1563 O O   . VAL A 220 ? 0.1776 0.2010 0.1438 0.0325  0.0041  0.0120  232 VAL A O   
1564 C CB  . VAL A 220 ? 0.1880 0.2044 0.1674 0.0263  0.0045  0.0103  232 VAL A CB  
1565 C CG1 . VAL A 220 ? 0.2036 0.2191 0.1758 0.0318  0.0009  0.0047  232 VAL A CG1 
1566 C CG2 . VAL A 220 ? 0.2156 0.2240 0.1970 0.0216  0.0014  0.0099  232 VAL A CG2 
1567 N N   . PHE A 221 ? 0.1537 0.1719 0.1310 0.0241  0.0053  0.0175  233 PHE A N   
1568 C CA  . PHE A 221 ? 0.1580 0.1752 0.1318 0.0246  0.0025  0.0180  233 PHE A CA  
1569 C C   . PHE A 221 ? 0.1688 0.1794 0.1465 0.0207  -0.0009 0.0165  233 PHE A C   
1570 O O   . PHE A 221 ? 0.1739 0.1826 0.1584 0.0167  0.0010  0.0182  233 PHE A O   
1571 C CB  . PHE A 221 ? 0.1846 0.2069 0.1599 0.0243  0.0058  0.0240  233 PHE A CB  
1572 C CG  . PHE A 221 ? 0.1989 0.2203 0.1717 0.0247  0.0027  0.0251  233 PHE A CG  
1573 C CD1 . PHE A 221 ? 0.1957 0.2184 0.1599 0.0284  -0.0004 0.0228  233 PHE A CD1 
1574 C CD2 . PHE A 221 ? 0.1985 0.2181 0.1779 0.0216  0.0027  0.0284  233 PHE A CD2 
1575 C CE1 . PHE A 221 ? 0.2183 0.2402 0.1804 0.0286  -0.0039 0.0241  233 PHE A CE1 
1576 C CE2 . PHE A 221 ? 0.2111 0.2306 0.1894 0.0222  -0.0005 0.0296  233 PHE A CE2 
1577 C CZ  . PHE A 221 ? 0.2090 0.2297 0.1785 0.0255  -0.0040 0.0276  233 PHE A CZ  
1578 N N   . GLY A 222 ? 0.1764 0.1839 0.1496 0.0216  -0.0059 0.0135  234 GLY A N   
1579 C CA  . GLY A 222 ? 0.2004 0.2037 0.1778 0.0177  -0.0088 0.0132  234 GLY A CA  
1580 C C   . GLY A 222 ? 0.1839 0.1817 0.1645 0.0139  -0.0099 0.0105  234 GLY A C   
1581 O O   . GLY A 222 ? 0.1735 0.1691 0.1515 0.0151  -0.0106 0.0078  234 GLY A O   
1582 N N   . GLY A 223 ? 0.1738 0.1698 0.1604 0.0095  -0.0101 0.0115  235 GLY A N   
1583 C CA  . GLY A 223 ? 0.2134 0.2043 0.2026 0.0049  -0.0112 0.0096  235 GLY A CA  
1584 C C   . GLY A 223 ? 0.2416 0.2295 0.2305 0.0022  -0.0163 0.0076  235 GLY A C   
1585 O O   . GLY A 223 ? 0.2175 0.2064 0.2036 0.0042  -0.0196 0.0072  235 GLY A O   
1586 N N   . ARG A 224 ? 0.1766 0.1607 0.1684 -0.0028 -0.0169 0.0067  236 ARG A N   
1587 C CA  . ARG A 224 ? 0.2130 0.1942 0.2049 -0.0066 -0.0217 0.0051  236 ARG A CA  
1588 C C   . ARG A 224 ? 0.2145 0.1885 0.2000 -0.0069 -0.0270 0.0017  236 ARG A C   
1589 O O   . ARG A 224 ? 0.2087 0.1794 0.1931 -0.0074 -0.0261 0.0009  236 ARG A O   
1590 C CB  . ARG A 224 ? 0.2350 0.2169 0.2336 -0.0124 -0.0190 0.0064  236 ARG A CB  
1591 C CG  . ARG A 224 ? 0.2529 0.2313 0.2511 -0.0176 -0.0237 0.0048  236 ARG A CG  
1592 C CD  . ARG A 224 ? 0.2237 0.2065 0.2258 -0.0187 -0.0256 0.0057  236 ARG A CD  
1593 N NE  . ARG A 224 ? 0.2263 0.2057 0.2274 -0.0238 -0.0309 0.0044  236 ARG A NE  
1594 C CZ  . ARG A 224 ? 0.2763 0.2557 0.2809 -0.0302 -0.0298 0.0048  236 ARG A CZ  
1595 N NH1 . ARG A 224 ? 0.2667 0.2494 0.2763 -0.0320 -0.0235 0.0061  236 ARG A NH1 
1596 N NH2 . ARG A 224 ? 0.2696 0.2450 0.2720 -0.0351 -0.0353 0.0040  236 ARG A NH2 
1597 N N   . TYR A 225 ? 0.2347 0.2060 0.2165 -0.0068 -0.0330 -0.0002 237 TYR A N   
1598 C CA  . TYR A 225 ? 0.2697 0.2328 0.2459 -0.0080 -0.0392 -0.0035 237 TYR A CA  
1599 C C   . TYR A 225 ? 0.2658 0.2266 0.2413 -0.0114 -0.0452 -0.0042 237 TYR A C   
1600 O O   . TYR A 225 ? 0.2419 0.2052 0.2156 -0.0086 -0.0473 -0.0044 237 TYR A O   
1601 C CB  . TYR A 225 ? 0.2630 0.2237 0.2321 -0.0012 -0.0410 -0.0065 237 TYR A CB  
1602 C CG  . TYR A 225 ? 0.2693 0.2205 0.2323 -0.0012 -0.0482 -0.0104 237 TYR A CG  
1603 C CD1 . TYR A 225 ? 0.3108 0.2558 0.2749 -0.0063 -0.0504 -0.0105 237 TYR A CD1 
1604 C CD2 . TYR A 225 ? 0.3563 0.3043 0.3119 0.0039  -0.0531 -0.0141 237 TYR A CD2 
1605 C CE1 . TYR A 225 ? 0.3329 0.2682 0.2916 -0.0063 -0.0576 -0.0138 237 TYR A CE1 
1606 C CE2 . TYR A 225 ? 0.3906 0.3288 0.3406 0.0043  -0.0602 -0.0180 237 TYR A CE2 
1607 C CZ  . TYR A 225 ? 0.3976 0.3292 0.3495 -0.0009 -0.0625 -0.0177 237 TYR A CZ  
1608 O OH  . TYR A 225 ? 0.4880 0.4089 0.4345 -0.0006 -0.0702 -0.0213 237 TYR A OH  
1609 N N   . ARG A 226 ? 0.2700 0.2258 0.2464 -0.0177 -0.0483 -0.0043 238 ARG A N   
1610 C CA  . ARG A 226 ? 0.3000 0.2535 0.2765 -0.0224 -0.0544 -0.0045 238 ARG A CA  
1611 C C   . ARG A 226 ? 0.2801 0.2427 0.2633 -0.0233 -0.0515 -0.0019 238 ARG A C   
1612 O O   . ARG A 226 ? 0.2800 0.2487 0.2703 -0.0254 -0.0454 0.0006  238 ARG A O   
1613 C CB  . ARG A 226 ? 0.3392 0.2848 0.3072 -0.0193 -0.0623 -0.0081 238 ARG A CB  
1614 C CG  . ARG A 226 ? 0.3643 0.3002 0.3268 -0.0187 -0.0657 -0.0107 238 ARG A CG  
1615 C CD  . ARG A 226 ? 0.3810 0.3087 0.3349 -0.0144 -0.0735 -0.0151 238 ARG A CD  
1616 N NE  . ARG A 226 ? 0.4561 0.3808 0.4090 -0.0188 -0.0803 -0.0151 238 ARG A NE  
1617 C CZ  . ARG A 226 ? 0.4803 0.3987 0.4338 -0.0262 -0.0856 -0.0142 238 ARG A CZ  
1618 N NH1 . ARG A 226 ? 0.4705 0.3846 0.4250 -0.0300 -0.0849 -0.0133 238 ARG A NH1 
1619 N NH2 . ARG A 226 ? 0.5495 0.4661 0.5026 -0.0302 -0.0918 -0.0140 238 ARG A NH2 
1620 N N   . ASP A 227 ? 0.3157 0.2797 0.2973 -0.0213 -0.0558 -0.0024 239 ASP A N   
1621 C CA  . ASP A 227 ? 0.2824 0.2552 0.2715 -0.0225 -0.0540 0.0003  239 ASP A CA  
1622 C C   . ASP A 227 ? 0.2877 0.2658 0.2764 -0.0158 -0.0511 0.0012  239 ASP A C   
1623 O O   . ASP A 227 ? 0.3176 0.3013 0.3101 -0.0154 -0.0523 0.0029  239 ASP A O   
1624 C CB  . ASP A 227 ? 0.3844 0.3560 0.3738 -0.0267 -0.0614 0.0000  239 ASP A CB  
1625 C CG  . ASP A 227 ? 0.4002 0.3700 0.3933 -0.0350 -0.0627 0.0009  239 ASP A CG  
1626 O OD1 . ASP A 227 ? 0.3714 0.3443 0.3695 -0.0377 -0.0565 0.0023  239 ASP A OD1 
1627 O OD2 . ASP A 227 ? 0.5568 0.5221 0.5476 -0.0391 -0.0699 0.0002  239 ASP A OD2 
1628 N N   . ALA A 228 ? 0.2811 0.2583 0.2658 -0.0109 -0.0472 0.0007  240 ALA A N   
1629 C CA  . ALA A 228 ? 0.2344 0.2171 0.2188 -0.0053 -0.0438 0.0024  240 ALA A CA  
1630 C C   . ALA A 228 ? 0.2290 0.2145 0.2164 -0.0037 -0.0363 0.0042  240 ALA A C   
1631 O O   . ALA A 228 ? 0.2208 0.2027 0.2078 -0.0053 -0.0343 0.0032  240 ALA A O   
1632 C CB  . ALA A 228 ? 0.2514 0.2310 0.2254 0.0003  -0.0478 -0.0002 240 ALA A CB  
1633 N N   . ARG A 229 ? 0.1987 0.1903 0.1896 -0.0010 -0.0325 0.0072  241 ARG A N   
1634 C CA  . ARG A 229 ? 0.1938 0.1878 0.1856 0.0018  -0.0263 0.0092  241 ARG A CA  
1635 C C   . ARG A 229 ? 0.2303 0.2258 0.2147 0.0075  -0.0270 0.0095  241 ARG A C   
1636 O O   . ARG A 229 ? 0.2293 0.2276 0.2128 0.0092  -0.0296 0.0108  241 ARG A O   
1637 C CB  . ARG A 229 ? 0.2184 0.2173 0.2197 0.0001  -0.0217 0.0126  241 ARG A CB  
1638 C CG  . ARG A 229 ? 0.2083 0.2058 0.2154 -0.0055 -0.0202 0.0117  241 ARG A CG  
1639 C CD  . ARG A 229 ? 0.1896 0.1915 0.2064 -0.0073 -0.0156 0.0140  241 ARG A CD  
1640 N NE  . ARG A 229 ? 0.2032 0.2037 0.2235 -0.0129 -0.0146 0.0124  241 ARG A NE  
1641 C CZ  . ARG A 229 ? 0.2294 0.2327 0.2548 -0.0166 -0.0163 0.0120  241 ARG A CZ  
1642 N NH1 . ARG A 229 ? 0.2022 0.2105 0.2316 -0.0152 -0.0189 0.0132  241 ARG A NH1 
1643 N NH2 . ARG A 229 ? 0.2816 0.2834 0.3083 -0.0221 -0.0154 0.0107  241 ARG A NH2 
1644 N N   . MET A 230 ? 0.2469 0.2412 0.2263 0.0103  -0.0249 0.0083  242 MET A N   
1645 C CA  . MET A 230 ? 0.2272 0.2215 0.1972 0.0154  -0.0268 0.0065  242 MET A CA  
1646 C C   . MET A 230 ? 0.2390 0.2394 0.2077 0.0190  -0.0223 0.0101  242 MET A C   
1647 O O   . MET A 230 ? 0.2153 0.2189 0.1905 0.0177  -0.0174 0.0140  242 MET A O   
1648 C CB  . MET A 230 ? 0.2469 0.2366 0.2121 0.0167  -0.0277 0.0024  242 MET A CB  
1649 C CG  . MET A 230 ? 0.2840 0.2664 0.2469 0.0141  -0.0343 -0.0015 242 MET A CG  
1650 S SD  . MET A 230 ? 0.3621 0.3378 0.3215 0.0149  -0.0357 -0.0057 242 MET A SD  
1651 C CE  . MET A 230 ? 0.3135 0.2920 0.2820 0.0111  -0.0289 -0.0021 242 MET A CE  
1652 N N   . ASN A 231 ? 0.3017 0.3034 0.2616 0.0234  -0.0243 0.0090  243 ASN A N   
1653 C CA  . ASN A 231 ? 0.2463 0.2541 0.2033 0.0266  -0.0206 0.0127  243 ASN A CA  
1654 C C   . ASN A 231 ? 0.2795 0.2893 0.2289 0.0309  -0.0183 0.0105  243 ASN A C   
1655 O O   . ASN A 231 ? 0.2663 0.2815 0.2109 0.0339  -0.0159 0.0130  243 ASN A O   
1656 C CB  . ASN A 231 ? 0.3118 0.3213 0.2648 0.0278  -0.0244 0.0143  243 ASN A CB  
1657 C CG  . ASN A 231 ? 0.2558 0.2628 0.1974 0.0312  -0.0294 0.0097  243 ASN A CG  
1658 O OD1 . ASN A 231 ? 0.3387 0.3407 0.2774 0.0316  -0.0321 0.0045  243 ASN A OD1 
1659 N ND2 . ASN A 231 ? 0.3490 0.3590 0.2836 0.0338  -0.0311 0.0113  243 ASN A ND2 
1660 N N   . ASP A 232 ? 0.2344 0.2404 0.1827 0.0314  -0.0191 0.0059  244 ASP A N   
1661 C CA  . ASP A 232 ? 0.2236 0.2317 0.1648 0.0364  -0.0176 0.0029  244 ASP A CA  
1662 C C   . ASP A 232 ? 0.2443 0.2581 0.1904 0.0364  -0.0108 0.0060  244 ASP A C   
1663 O O   . ASP A 232 ? 0.2240 0.2377 0.1787 0.0324  -0.0081 0.0094  244 ASP A O   
1664 C CB  . ASP A 232 ? 0.2319 0.2330 0.1692 0.0378  -0.0225 -0.0038 244 ASP A CB  
1665 C CG  . ASP A 232 ? 0.2694 0.2651 0.2143 0.0335  -0.0231 -0.0044 244 ASP A CG  
1666 O OD1 . ASP A 232 ? 0.2382 0.2346 0.1909 0.0288  -0.0210 -0.0004 244 ASP A OD1 
1667 O OD2 . ASP A 232 ? 0.3020 0.2926 0.2445 0.0349  -0.0260 -0.0091 244 ASP A OD2 
1668 N N   . LEU A 233 ? 0.2368 0.2560 0.1771 0.0411  -0.0081 0.0047  245 LEU A N   
1669 C CA  . LEU A 233 ? 0.2282 0.2546 0.1725 0.0414  -0.0017 0.0081  245 LEU A CA  
1670 C C   . LEU A 233 ? 0.2440 0.2725 0.1847 0.0462  -0.0010 0.0030  245 LEU A C   
1671 O O   . LEU A 233 ? 0.2312 0.2599 0.1628 0.0510  -0.0032 -0.0014 245 LEU A O   
1672 C CB  . LEU A 233 ? 0.2248 0.2589 0.1664 0.0421  0.0021  0.0137  245 LEU A CB  
1673 C CG  . LEU A 233 ? 0.2104 0.2529 0.1558 0.0417  0.0088  0.0186  245 LEU A CG  
1674 C CD1 . LEU A 233 ? 0.2200 0.2602 0.1764 0.0364  0.0108  0.0225  245 LEU A CD1 
1675 C CD2 . LEU A 233 ? 0.2118 0.2608 0.1519 0.0424  0.0110  0.0238  245 LEU A CD2 
1676 N N   . HIS A 234 ? 0.1900 0.2193 0.1377 0.0451  0.0016  0.0031  246 HIS A N   
1677 C CA  . HIS A 234 ? 0.2316 0.2637 0.1782 0.0496  0.0024  -0.0013 246 HIS A CA  
1678 C C   . HIS A 234 ? 0.2236 0.2637 0.1777 0.0483  0.0086  0.0030  246 HIS A C   
1679 O O   . HIS A 234 ? 0.2145 0.2551 0.1750 0.0432  0.0110  0.0086  246 HIS A O   
1680 C CB  . HIS A 234 ? 0.2387 0.2611 0.1868 0.0494  -0.0030 -0.0067 246 HIS A CB  
1681 C CG  . HIS A 234 ? 0.2784 0.2912 0.2212 0.0486  -0.0097 -0.0100 246 HIS A CG  
1682 N ND1 . HIS A 234 ? 0.3295 0.3375 0.2646 0.0533  -0.0147 -0.0166 246 HIS A ND1 
1683 C CD2 . HIS A 234 ? 0.2246 0.2321 0.1693 0.0435  -0.0125 -0.0077 246 HIS A CD2 
1684 C CE1 . HIS A 234 ? 0.3304 0.3301 0.2626 0.0506  -0.0205 -0.0178 246 HIS A CE1 
1685 N NE2 . HIS A 234 ? 0.2617 0.2617 0.2001 0.0446  -0.0191 -0.0124 246 HIS A NE2 
1686 N N   . TYR A 235 ? 0.2590 0.3054 0.2128 0.0530  0.0108  0.0001  247 TYR A N   
1687 C CA  . TYR A 235 ? 0.2500 0.3030 0.2125 0.0515  0.0154  0.0033  247 TYR A CA  
1688 C C   . TYR A 235 ? 0.1979 0.2510 0.1623 0.0558  0.0138  -0.0025 247 TYR A C   
1689 O O   . TYR A 235 ? 0.2599 0.3138 0.2179 0.0622  0.0122  -0.0083 247 TYR A O   
1690 C CB  . TYR A 235 ? 0.2278 0.2938 0.1904 0.0520  0.0221  0.0086  247 TYR A CB  
1691 C CG  . TYR A 235 ? 0.2424 0.3186 0.1996 0.0589  0.0251  0.0052  247 TYR A CG  
1692 C CD1 . TYR A 235 ? 0.1951 0.2787 0.1579 0.0619  0.0277  0.0033  247 TYR A CD1 
1693 C CD2 . TYR A 235 ? 0.2555 0.3347 0.2022 0.0625  0.0254  0.0039  247 TYR A CD2 
1694 C CE1 . TYR A 235 ? 0.2570 0.3512 0.2155 0.0686  0.0310  -0.0002 247 TYR A CE1 
1695 C CE2 . TYR A 235 ? 0.2908 0.3797 0.2319 0.0688  0.0285  0.0005  247 TYR A CE2 
1696 C CZ  . TYR A 235 ? 0.3182 0.4149 0.2654 0.0720  0.0316  -0.0017 247 TYR A CZ  
1697 O OH  . TYR A 235 ? 0.3252 0.4327 0.2670 0.0789  0.0353  -0.0055 247 TYR A OH  
1698 N N   . LEU A 236 ? 0.2501 0.3017 0.2234 0.0526  0.0139  -0.0010 248 LEU A N   
1699 C CA  . LEU A 236 ? 0.1927 0.2457 0.1697 0.0564  0.0127  -0.0053 248 LEU A CA  
1700 C C   . LEU A 236 ? 0.1636 0.2309 0.1466 0.0576  0.0193  -0.0018 248 LEU A C   
1701 O O   . LEU A 236 ? 0.1994 0.2702 0.1885 0.0521  0.0227  0.0047  248 LEU A O   
1702 C CB  . LEU A 236 ? 0.2190 0.2616 0.2018 0.0517  0.0082  -0.0056 248 LEU A CB  
1703 C CG  . LEU A 236 ? 0.2396 0.2824 0.2279 0.0544  0.0063  -0.0088 248 LEU A CG  
1704 C CD1 . LEU A 236 ? 0.2335 0.2729 0.2162 0.0620  0.0018  -0.0166 248 LEU A CD1 
1705 C CD2 . LEU A 236 ? 0.2235 0.2565 0.2172 0.0478  0.0025  -0.0071 248 LEU A CD2 
1706 N N   . ASN A 237 ? 0.2157 0.2915 0.1967 0.0648  0.0211  -0.0060 249 ASN A N   
1707 C CA  . ASN A 237 ? 0.2151 0.3061 0.2027 0.0664  0.0273  -0.0032 249 ASN A CA  
1708 C C   . ASN A 237 ? 0.2027 0.2925 0.2012 0.0642  0.0257  -0.0027 249 ASN A C   
1709 O O   . ASN A 237 ? 0.2289 0.3128 0.2284 0.0679  0.0209  -0.0084 249 ASN A O   
1710 C CB  . ASN A 237 ? 0.2663 0.3669 0.2488 0.0754  0.0296  -0.0088 249 ASN A CB  
1711 C CG  . ASN A 237 ? 0.2462 0.3645 0.2359 0.0772  0.0366  -0.0058 249 ASN A CG  
1712 O OD1 . ASN A 237 ? 0.2351 0.3569 0.2355 0.0753  0.0371  -0.0039 249 ASN A OD1 
1713 N ND2 . ASN A 237 ? 0.2558 0.3860 0.2395 0.0804  0.0421  -0.0051 249 ASN A ND2 
1714 N N   . LEU A 238 ? 0.2216 0.3164 0.2281 0.0581  0.0291  0.0043  250 LEU A N   
1715 C CA  . LEU A 238 ? 0.2168 0.3083 0.2328 0.0545  0.0267  0.0054  250 LEU A CA  
1716 C C   . LEU A 238 ? 0.2412 0.3449 0.2652 0.0590  0.0288  0.0040  250 LEU A C   
1717 O O   . LEU A 238 ? 0.2348 0.3372 0.2674 0.0561  0.0269  0.0054  250 LEU A O   
1718 C CB  . LEU A 238 ? 0.2380 0.3279 0.2587 0.0458  0.0287  0.0130  250 LEU A CB  
1719 C CG  . LEU A 238 ? 0.1988 0.2782 0.2125 0.0419  0.0270  0.0144  250 LEU A CG  
1720 C CD1 . LEU A 238 ? 0.1321 0.2112 0.1498 0.0343  0.0298  0.0218  250 LEU A CD1 
1721 C CD2 . LEU A 238 ? 0.1896 0.2541 0.2001 0.0413  0.0203  0.0096  250 LEU A CD2 
1722 N N   . ASP A 239 ? 0.2695 0.3855 0.2911 0.0660  0.0329  0.0014  251 ASP A N   
1723 C CA  . ASP A 239 ? 0.2194 0.3486 0.2483 0.0721  0.0352  -0.0014 251 ASP A CA  
1724 C C   . ASP A 239 ? 0.2568 0.3813 0.2814 0.0810  0.0308  -0.0108 251 ASP A C   
1725 O O   . ASP A 239 ? 0.2756 0.4005 0.3075 0.0845  0.0278  -0.0141 251 ASP A O   
1726 C CB  . ASP A 239 ? 0.2777 0.4255 0.3067 0.0740  0.0436  0.0020  251 ASP A CB  
1727 C CG  . ASP A 239 ? 0.3023 0.4583 0.3396 0.0663  0.0478  0.0111  251 ASP A CG  
1728 O OD1 . ASP A 239 ? 0.2739 0.4256 0.3201 0.0617  0.0449  0.0133  251 ASP A OD1 
1729 O OD2 . ASP A 239 ? 0.3397 0.5060 0.3744 0.0646  0.0538  0.0160  251 ASP A OD2 
1730 N N   . THR A 240 ? 0.2646 0.3845 0.2775 0.0850  0.0300  -0.0151 252 THR A N   
1731 C CA  . THR A 240 ? 0.2873 0.4007 0.2949 0.0934  0.0251  -0.0244 252 THR A CA  
1732 C C   . THR A 240 ? 0.2792 0.3723 0.2830 0.0906  0.0163  -0.0271 252 THR A C   
1733 O O   . THR A 240 ? 0.3252 0.4111 0.3286 0.0961  0.0106  -0.0338 252 THR A O   
1734 C CB  . THR A 240 ? 0.2941 0.4125 0.2901 0.0995  0.0282  -0.0284 252 THR A CB  
1735 O OG1 . THR A 240 ? 0.2751 0.3826 0.2611 0.0949  0.0260  -0.0265 252 THR A OG1 
1736 C CG2 . THR A 240 ? 0.3323 0.4713 0.3308 0.1008  0.0376  -0.0245 252 THR A CG2 
1737 N N   . TRP A 241 ? 0.2585 0.3425 0.2599 0.0822  0.0150  -0.0219 253 TRP A N   
1738 C CA  . TRP A 241 ? 0.2665 0.3322 0.2635 0.0787  0.0073  -0.0238 253 TRP A CA  
1739 C C   . TRP A 241 ? 0.3245 0.3828 0.3098 0.0836  0.0038  -0.0300 253 TRP A C   
1740 O O   . TRP A 241 ? 0.3668 0.4123 0.3488 0.0854  -0.0035 -0.0352 253 TRP A O   
1741 C CB  . TRP A 241 ? 0.2937 0.3518 0.2976 0.0784  0.0014  -0.0260 253 TRP A CB  
1742 C CG  . TRP A 241 ? 0.2672 0.3327 0.2821 0.0735  0.0045  -0.0199 253 TRP A CG  
1743 C CD1 . TRP A 241 ? 0.3050 0.3817 0.3294 0.0770  0.0067  -0.0201 253 TRP A CD1 
1744 C CD2 . TRP A 241 ? 0.2520 0.3148 0.2698 0.0640  0.0060  -0.0129 253 TRP A CD2 
1745 N NE1 . TRP A 241 ? 0.2866 0.3672 0.3194 0.0699  0.0090  -0.0133 253 TRP A NE1 
1746 C CE2 . TRP A 241 ? 0.2537 0.3253 0.2822 0.0620  0.0085  -0.0090 253 TRP A CE2 
1747 C CE3 . TRP A 241 ? 0.2253 0.2790 0.2380 0.0573  0.0053  -0.0097 253 TRP A CE3 
1748 C CZ2 . TRP A 241 ? 0.2235 0.2943 0.2567 0.0534  0.0102  -0.0023 253 TRP A CZ2 
1749 C CZ3 . TRP A 241 ? 0.2547 0.3079 0.2725 0.0493  0.0072  -0.0034 253 TRP A CZ3 
1750 C CH2 . TRP A 241 ? 0.2321 0.2932 0.2596 0.0474  0.0096  0.0001  253 TRP A CH2 
1751 N N   . GLU A 242 ? 0.3209 0.3866 0.2993 0.0853  0.0085  -0.0292 254 GLU A N   
1752 C CA  . GLU A 242 ? 0.2729 0.3324 0.2393 0.0893  0.0055  -0.0344 254 GLU A CA  
1753 C C   . GLU A 242 ? 0.3069 0.3615 0.2683 0.0825  0.0056  -0.0293 254 GLU A C   
1754 O O   . GLU A 242 ? 0.2940 0.3576 0.2571 0.0789  0.0115  -0.0229 254 GLU A O   
1755 C CB  . GLU A 242 ? 0.3559 0.4284 0.3173 0.0977  0.0106  -0.0383 254 GLU A CB  
1756 C CG  . GLU A 242 ? 0.3626 0.4335 0.3109 0.0995  0.0106  -0.0401 254 GLU A CG  
1757 C CD  . GLU A 242 ? 0.4313 0.5151 0.3739 0.1081  0.0156  -0.0447 254 GLU A CD  
1758 O OE1 . GLU A 242 ? 0.4573 0.5394 0.3983 0.1161  0.0129  -0.0529 254 GLU A OE1 
1759 O OE2 . GLU A 242 ? 0.4734 0.5689 0.4128 0.1070  0.0223  -0.0401 254 GLU A OE2 
1760 N N   . TRP A 243 ? 0.2890 0.3294 0.2446 0.0807  -0.0013 -0.0320 255 TRP A N   
1761 C CA  . TRP A 243 ? 0.3074 0.3432 0.2585 0.0750  -0.0018 -0.0280 255 TRP A CA  
1762 C C   . TRP A 243 ? 0.3224 0.3637 0.2633 0.0792  0.0003  -0.0295 255 TRP A C   
1763 O O   . TRP A 243 ? 0.3186 0.3608 0.2527 0.0866  -0.0009 -0.0361 255 TRP A O   
1764 C CB  . TRP A 243 ? 0.3052 0.3251 0.2541 0.0713  -0.0099 -0.0302 255 TRP A CB  
1765 C CG  . TRP A 243 ? 0.3155 0.3293 0.2729 0.0643  -0.0117 -0.0266 255 TRP A CG  
1766 C CD1 . TRP A 243 ? 0.3144 0.3207 0.2757 0.0642  -0.0165 -0.0293 255 TRP A CD1 
1767 C CD2 . TRP A 243 ? 0.2640 0.2781 0.2263 0.0565  -0.0091 -0.0197 255 TRP A CD2 
1768 N NE1 . TRP A 243 ? 0.2901 0.2924 0.2578 0.0564  -0.0167 -0.0245 255 TRP A NE1 
1769 C CE2 . TRP A 243 ? 0.3074 0.3144 0.2759 0.0518  -0.0120 -0.0189 255 TRP A CE2 
1770 C CE3 . TRP A 243 ? 0.2872 0.3065 0.2491 0.0532  -0.0047 -0.0143 255 TRP A CE3 
1771 C CZ2 . TRP A 243 ? 0.2506 0.2559 0.2244 0.0442  -0.0104 -0.0134 255 TRP A CZ2 
1772 C CZ3 . TRP A 243 ? 0.2454 0.2627 0.2135 0.0459  -0.0033 -0.0089 255 TRP A CZ3 
1773 C CH2 . TRP A 243 ? 0.2030 0.2135 0.1767 0.0416  -0.0060 -0.0088 255 TRP A CH2 
1774 N N   . ASN A 244 ? 0.2992 0.3438 0.2386 0.0746  0.0034  -0.0234 256 ASN A N   
1775 C CA  . ASN A 244 ? 0.2852 0.3337 0.2144 0.0771  0.0047  -0.0236 256 ASN A CA  
1776 C C   . ASN A 244 ? 0.3318 0.3730 0.2593 0.0709  0.0017  -0.0194 256 ASN A C   
1777 O O   . ASN A 244 ? 0.2866 0.3281 0.2218 0.0647  0.0037  -0.0131 256 ASN A O   
1778 C CB  . ASN A 244 ? 0.3014 0.3655 0.2310 0.0784  0.0130  -0.0190 256 ASN A CB  
1779 C CG  . ASN A 244 ? 0.3790 0.4528 0.3110 0.0848  0.0168  -0.0230 256 ASN A CG  
1780 O OD1 . ASN A 244 ? 0.3645 0.4434 0.3069 0.0832  0.0196  -0.0204 256 ASN A OD1 
1781 N ND2 . ASN A 244 ? 0.3413 0.4179 0.2638 0.0922  0.0166  -0.0295 256 ASN A ND2 
1782 N N   . GLU A 245 ? 0.3411 0.3762 0.2589 0.0726  -0.0030 -0.0229 257 GLU A N   
1783 C CA  . GLU A 245 ? 0.3370 0.3676 0.2532 0.0675  -0.0055 -0.0188 257 GLU A CA  
1784 C C   . GLU A 245 ? 0.3162 0.3558 0.2257 0.0687  -0.0014 -0.0150 257 GLU A C   
1785 O O   . GLU A 245 ? 0.3420 0.3859 0.2419 0.0745  -0.0007 -0.0190 257 GLU A O   
1786 C CB  . GLU A 245 ? 0.3360 0.3543 0.2463 0.0674  -0.0139 -0.0238 257 GLU A CB  
1787 C CG  . GLU A 245 ? 0.3162 0.3316 0.2264 0.0620  -0.0162 -0.0191 257 GLU A CG  
1788 C CD  . GLU A 245 ? 0.3919 0.3957 0.2987 0.0603  -0.0246 -0.0230 257 GLU A CD  
1789 O OE1 . GLU A 245 ? 0.4933 0.4902 0.3959 0.0637  -0.0292 -0.0296 257 GLU A OE1 
1790 O OE2 . GLU A 245 ? 0.3943 0.3958 0.3028 0.0557  -0.0268 -0.0192 257 GLU A OE2 
1791 N N   . LEU A 246 ? 0.2579 0.3000 0.1721 0.0634  0.0011  -0.0075 258 LEU A N   
1792 C CA  . LEU A 246 ? 0.2831 0.3334 0.1922 0.0634  0.0048  -0.0024 258 LEU A CA  
1793 C C   . LEU A 246 ? 0.3044 0.3486 0.2072 0.0618  -0.0007 -0.0019 258 LEU A C   
1794 O O   . LEU A 246 ? 0.3217 0.3579 0.2298 0.0576  -0.0049 -0.0010 258 LEU A O   
1795 C CB  . LEU A 246 ? 0.3324 0.3887 0.2508 0.0585  0.0103  0.0059  258 LEU A CB  
1796 C CG  . LEU A 246 ? 0.2882 0.3528 0.2130 0.0595  0.0161  0.0067  258 LEU A CG  
1797 C CD1 . LEU A 246 ? 0.2631 0.3305 0.1975 0.0537  0.0200  0.0147  258 LEU A CD1 
1798 C CD2 . LEU A 246 ? 0.3017 0.3775 0.2183 0.0649  0.0206  0.0054  258 LEU A CD2 
1799 N N   . ILE A 247 ? 0.3615 0.4099 0.2530 0.0651  -0.0006 -0.0024 259 ILE A N   
1800 C CA  . ILE A 247 ? 0.4203 0.4632 0.3046 0.0643  -0.0064 -0.0024 259 ILE A CA  
1801 C C   . ILE A 247 ? 0.3650 0.4154 0.2455 0.0628  -0.0032 0.0050  259 ILE A C   
1802 O O   . ILE A 247 ? 0.3815 0.4368 0.2503 0.0665  -0.0023 0.0038  259 ILE A O   
1803 C CB  . ILE A 247 ? 0.4350 0.4735 0.3069 0.0697  -0.0112 -0.0108 259 ILE A CB  
1804 C CG1 . ILE A 247 ? 0.4728 0.5064 0.3476 0.0727  -0.0126 -0.0181 259 ILE A CG1 
1805 C CG2 . ILE A 247 ? 0.4791 0.5089 0.3466 0.0676  -0.0193 -0.0118 259 ILE A CG2 
1806 C CD1 . ILE A 247 ? 0.4173 0.4400 0.3002 0.0683  -0.0183 -0.0191 259 ILE A CD1 
1807 N N   . PRO A 248 ? 0.3998 0.4509 0.2894 0.0577  -0.0016 0.0125  260 PRO A N   
1808 C CA  . PRO A 248 ? 0.3568 0.4142 0.2429 0.0562  0.0009  0.0201  260 PRO A CA  
1809 C C   . PRO A 248 ? 0.3952 0.4493 0.2714 0.0569  -0.0050 0.0198  260 PRO A C   
1810 O O   . PRO A 248 ? 0.4462 0.4920 0.3232 0.0561  -0.0115 0.0165  260 PRO A O   
1811 C CB  . PRO A 248 ? 0.3236 0.3795 0.2230 0.0507  0.0023  0.0269  260 PRO A CB  
1812 C CG  . PRO A 248 ? 0.3155 0.3669 0.2246 0.0496  0.0025  0.0231  260 PRO A CG  
1813 C CD  . PRO A 248 ? 0.3289 0.3749 0.2319 0.0531  -0.0021 0.0145  260 PRO A CD  
1814 N N   . GLN A 249 ? 0.3665 0.4273 0.2331 0.0580  -0.0029 0.0237  261 GLN A N   
1815 C CA  . GLN A 249 ? 0.4396 0.4981 0.2953 0.0586  -0.0083 0.0242  261 GLN A CA  
1816 C C   . GLN A 249 ? 0.3632 0.4193 0.2259 0.0540  -0.0112 0.0321  261 GLN A C   
1817 O O   . GLN A 249 ? 0.3492 0.4078 0.2215 0.0507  -0.0073 0.0386  261 GLN A O   
1818 C CB  . GLN A 249 ? 0.5048 0.5718 0.3459 0.0618  -0.0048 0.0250  261 GLN A CB  
1819 C CG  . GLN A 249 ? 0.5978 0.6678 0.4310 0.0675  -0.0022 0.0164  261 GLN A CG  
1820 C CD  . GLN A 249 ? 0.6532 0.7148 0.4771 0.0709  -0.0096 0.0077  261 GLN A CD  
1821 O OE1 . GLN A 249 ? 0.6584 0.7166 0.4822 0.0744  -0.0103 -0.0005 261 GLN A OE1 
1822 N NE2 . GLN A 249 ? 0.6631 0.7208 0.4791 0.0696  -0.0156 0.0094  261 GLN A NE2 
1823 N N   . GLY A 250 ? 0.4254 0.4763 0.2831 0.0538  -0.0184 0.0313  262 GLY A N   
1824 C CA  . GLY A 250 ? 0.3251 0.3741 0.1892 0.0501  -0.0218 0.0384  262 GLY A CA  
1825 C C   . GLY A 250 ? 0.3178 0.3613 0.1978 0.0470  -0.0234 0.0381  262 GLY A C   
1826 O O   . GLY A 250 ? 0.3322 0.3711 0.2155 0.0475  -0.0251 0.0316  262 GLY A O   
1827 N N   . ILE A 251 ? 0.2815 0.3253 0.1712 0.0439  -0.0230 0.0453  263 ILE A N   
1828 C CA  . ILE A 251 ? 0.2921 0.3311 0.1963 0.0410  -0.0251 0.0455  263 ILE A CA  
1829 C C   . ILE A 251 ? 0.3065 0.3455 0.2199 0.0398  -0.0192 0.0438  263 ILE A C   
1830 O O   . ILE A 251 ? 0.3241 0.3675 0.2381 0.0396  -0.0133 0.0473  263 ILE A O   
1831 C CB  . ILE A 251 ? 0.2681 0.3073 0.1790 0.0388  -0.0269 0.0533  263 ILE A CB  
1832 C CG1 . ILE A 251 ? 0.3109 0.3507 0.2114 0.0400  -0.0328 0.0556  263 ILE A CG1 
1833 C CG2 . ILE A 251 ? 0.3020 0.3371 0.2278 0.0364  -0.0291 0.0527  263 ILE A CG2 
1834 C CD1 . ILE A 251 ? 0.3112 0.3468 0.2134 0.0399  -0.0405 0.0517  263 ILE A CD1 
1835 N N   . CYS A 252 ? 0.2721 0.3064 0.1928 0.0387  -0.0212 0.0389  264 CYS A N   
1836 C CA  . CYS A 252 ? 0.2342 0.2673 0.1638 0.0371  -0.0167 0.0372  264 CYS A CA  
1837 C C   . CYS A 252 ? 0.2291 0.2588 0.1718 0.0337  -0.0181 0.0388  264 CYS A C   
1838 O O   . CYS A 252 ? 0.2167 0.2445 0.1614 0.0330  -0.0233 0.0388  264 CYS A O   
1839 C CB  . CYS A 252 ? 0.2924 0.3227 0.2180 0.0388  -0.0177 0.0293  264 CYS A CB  
1840 S SG  . CYS A 252 ? 0.3496 0.3843 0.2604 0.0438  -0.0155 0.0257  264 CYS A SG  
1841 N N   . PRO A 253 ? 0.2343 0.2636 0.1862 0.0315  -0.0135 0.0399  265 PRO A N   
1842 C CA  . PRO A 253 ? 0.2429 0.2692 0.2069 0.0284  -0.0143 0.0406  265 PRO A CA  
1843 C C   . PRO A 253 ? 0.2179 0.2404 0.1838 0.0273  -0.0184 0.0349  265 PRO A C   
1844 O O   . PRO A 253 ? 0.2001 0.2207 0.1599 0.0283  -0.0196 0.0298  265 PRO A O   
1845 C CB  . PRO A 253 ? 0.1904 0.2166 0.1610 0.0266  -0.0083 0.0419  265 PRO A CB  
1846 C CG  . PRO A 253 ? 0.2219 0.2524 0.1853 0.0284  -0.0045 0.0443  265 PRO A CG  
1847 C CD  . PRO A 253 ? 0.2009 0.2329 0.1526 0.0316  -0.0074 0.0406  265 PRO A CD  
1848 N N   . VAL A 254 ? 0.2263 0.2477 0.2012 0.0251  -0.0207 0.0358  266 VAL A N   
1849 C CA  . VAL A 254 ? 0.2449 0.2635 0.2233 0.0230  -0.0244 0.0312  266 VAL A CA  
1850 C C   . VAL A 254 ? 0.2020 0.2178 0.1826 0.0210  -0.0211 0.0277  266 VAL A C   
1851 O O   . VAL A 254 ? 0.1932 0.2094 0.1772 0.0204  -0.0158 0.0294  266 VAL A O   
1852 C CB  . VAL A 254 ? 0.2403 0.2601 0.2297 0.0210  -0.0262 0.0334  266 VAL A CB  
1853 C CG1 . VAL A 254 ? 0.1860 0.2061 0.1855 0.0193  -0.0207 0.0358  266 VAL A CG1 
1854 C CG2 . VAL A 254 ? 0.2140 0.2321 0.2062 0.0184  -0.0306 0.0292  266 VAL A CG2 
1855 N N   . GLY A 255 ? 0.1668 0.1791 0.1451 0.0197  -0.0247 0.0228  267 GLY A N   
1856 C CA  . GLY A 255 ? 0.2054 0.2142 0.1855 0.0175  -0.0227 0.0195  267 GLY A CA  
1857 C C   . GLY A 255 ? 0.1679 0.1769 0.1590 0.0137  -0.0194 0.0210  267 GLY A C   
1858 O O   . GLY A 255 ? 0.1645 0.1756 0.1628 0.0122  -0.0203 0.0228  267 GLY A O   
1859 N N   . ARG A 256 ? 0.1565 0.1636 0.1491 0.0122  -0.0155 0.0200  268 ARG A N   
1860 C CA  . ARG A 256 ? 0.1511 0.1583 0.1530 0.0089  -0.0116 0.0215  268 ARG A CA  
1861 C C   . ARG A 256 ? 0.1524 0.1562 0.1541 0.0067  -0.0091 0.0193  268 ARG A C   
1862 O O   . ARG A 256 ? 0.1698 0.1722 0.1652 0.0085  -0.0092 0.0177  268 ARG A O   
1863 C CB  . ARG A 256 ? 0.1427 0.1530 0.1486 0.0105  -0.0077 0.0262  268 ARG A CB  
1864 C CG  . ARG A 256 ? 0.1869 0.1978 0.1877 0.0126  -0.0044 0.0278  268 ARG A CG  
1865 C CD  . ARG A 256 ? 0.1825 0.1962 0.1854 0.0142  -0.0017 0.0331  268 ARG A CD  
1866 N NE  . ARG A 256 ? 0.1634 0.1797 0.1624 0.0169  -0.0049 0.0354  268 ARG A NE  
1867 C CZ  . ARG A 256 ? 0.1788 0.1969 0.1805 0.0180  -0.0044 0.0403  268 ARG A CZ  
1868 N NH1 . ARG A 256 ? 0.1600 0.1773 0.1680 0.0167  -0.0007 0.0434  268 ARG A NH1 
1869 N NH2 . ARG A 256 ? 0.1601 0.1803 0.1576 0.0202  -0.0082 0.0422  268 ARG A NH2 
1870 N N   . SER A 257 ? 0.1496 0.1523 0.1582 0.0028  -0.0067 0.0192  269 SER A N   
1871 C CA  . SER A 257 ? 0.1803 0.1801 0.1898 0.0003  -0.0034 0.0183  269 SER A CA  
1872 C C   . SER A 257 ? 0.1541 0.1550 0.1705 -0.0008 0.0014  0.0210  269 SER A C   
1873 O O   . SER A 257 ? 0.1497 0.1534 0.1709 0.0002  0.0020  0.0231  269 SER A O   
1874 C CB  . SER A 257 ? 0.1951 0.1912 0.2049 -0.0040 -0.0056 0.0151  269 SER A CB  
1875 O OG  . SER A 257 ? 0.1917 0.1897 0.2084 -0.0070 -0.0048 0.0154  269 SER A OG  
1876 N N   . TRP A 258 ? 0.1577 0.1561 0.1748 -0.0030 0.0045  0.0207  270 TRP A N   
1877 C CA  . TRP A 258 ? 0.1669 0.1648 0.1899 -0.0047 0.0088  0.0224  270 TRP A CA  
1878 C C   . TRP A 258 ? 0.1579 0.1581 0.1825 -0.0016 0.0108  0.0265  270 TRP A C   
1879 O O   . TRP A 258 ? 0.1317 0.1315 0.1620 -0.0021 0.0132  0.0282  270 TRP A O   
1880 C CB  . TRP A 258 ? 0.1726 0.1706 0.2014 -0.0075 0.0093  0.0209  270 TRP A CB  
1881 C CG  . TRP A 258 ? 0.1884 0.1832 0.2164 -0.0122 0.0095  0.0179  270 TRP A CG  
1882 C CD1 . TRP A 258 ? 0.1757 0.1667 0.2009 -0.0144 0.0109  0.0172  270 TRP A CD1 
1883 C CD2 . TRP A 258 ? 0.2013 0.1966 0.2311 -0.0157 0.0081  0.0155  270 TRP A CD2 
1884 N NE1 . TRP A 258 ? 0.1971 0.1856 0.2217 -0.0191 0.0103  0.0147  270 TRP A NE1 
1885 C CE2 . TRP A 258 ? 0.2196 0.2108 0.2468 -0.0201 0.0088  0.0137  270 TRP A CE2 
1886 C CE3 . TRP A 258 ? 0.2154 0.2147 0.2491 -0.0158 0.0062  0.0151  270 TRP A CE3 
1887 C CZ2 . TRP A 258 ? 0.2198 0.2108 0.2475 -0.0248 0.0079  0.0116  270 TRP A CZ2 
1888 C CZ3 . TRP A 258 ? 0.2246 0.2242 0.2595 -0.0205 0.0054  0.0130  270 TRP A CZ3 
1889 C CH2 . TRP A 258 ? 0.2111 0.2065 0.2427 -0.0251 0.0064  0.0114  270 TRP A CH2 
1890 N N   . HIS A 259 ? 0.1500 0.1526 0.1694 0.0017  0.0095  0.0281  271 HIS A N   
1891 C CA  . HIS A 259 ? 0.1516 0.1566 0.1708 0.0042  0.0112  0.0326  271 HIS A CA  
1892 C C   . HIS A 259 ? 0.1762 0.1808 0.1945 0.0033  0.0143  0.0341  271 HIS A C   
1893 O O   . HIS A 259 ? 0.1736 0.1765 0.1905 0.0016  0.0146  0.0315  271 HIS A O   
1894 C CB  . HIS A 259 ? 0.1560 0.1645 0.1689 0.0079  0.0083  0.0333  271 HIS A CB  
1895 C CG  . HIS A 259 ? 0.1641 0.1727 0.1703 0.0089  0.0067  0.0300  271 HIS A CG  
1896 N ND1 . HIS A 259 ? 0.1448 0.1506 0.1496 0.0075  0.0037  0.0255  271 HIS A ND1 
1897 C CD2 . HIS A 259 ? 0.1819 0.1932 0.1827 0.0112  0.0077  0.0304  271 HIS A CD2 
1898 C CE1 . HIS A 259 ? 0.1472 0.1528 0.1458 0.0093  0.0024  0.0231  271 HIS A CE1 
1899 N NE2 . HIS A 259 ? 0.1257 0.1352 0.1220 0.0119  0.0050  0.0258  271 HIS A NE2 
1900 N N   . SER A 260 ? 0.1495 0.1559 0.1687 0.0043  0.0163  0.0388  272 SER A N   
1901 C CA  . SER A 260 ? 0.1874 0.1948 0.2059 0.0034  0.0190  0.0411  272 SER A CA  
1902 C C   . SER A 260 ? 0.1852 0.1984 0.1981 0.0066  0.0191  0.0437  272 SER A C   
1903 O O   . SER A 260 ? 0.1508 0.1663 0.1612 0.0090  0.0176  0.0458  272 SER A O   
1904 C CB  . SER A 260 ? 0.1996 0.2042 0.2238 0.0012  0.0215  0.0447  272 SER A CB  
1905 O OG  . SER A 260 ? 0.1674 0.1725 0.1932 0.0029  0.0209  0.0486  272 SER A OG  
1906 N N   . LEU A 261 ? 0.1524 0.1685 0.1631 0.0066  0.0207  0.0434  273 LEU A N   
1907 C CA  . LEU A 261 ? 0.1587 0.1816 0.1643 0.0095  0.0218  0.0457  273 LEU A CA  
1908 C C   . LEU A 261 ? 0.1702 0.1960 0.1789 0.0074  0.0253  0.0489  273 LEU A C   
1909 O O   . LEU A 261 ? 0.1856 0.2098 0.1966 0.0057  0.0257  0.0463  273 LEU A O   
1910 C CB  . LEU A 261 ? 0.1481 0.1731 0.1478 0.0126  0.0198  0.0406  273 LEU A CB  
1911 C CG  . LEU A 261 ? 0.1715 0.2039 0.1645 0.0165  0.0208  0.0418  273 LEU A CG  
1912 C CD1 . LEU A 261 ? 0.1898 0.2228 0.1787 0.0183  0.0188  0.0438  273 LEU A CD1 
1913 C CD2 . LEU A 261 ? 0.1600 0.1935 0.1484 0.0196  0.0192  0.0360  273 LEU A CD2 
1914 N N   . THR A 262 ? 0.1731 0.2029 0.1816 0.0071  0.0273  0.0548  274 THR A N   
1915 C CA  . THR A 262 ? 0.1514 0.1835 0.1640 0.0041  0.0304  0.0591  274 THR A CA  
1916 C C   . THR A 262 ? 0.1888 0.2303 0.1978 0.0055  0.0328  0.0637  274 THR A C   
1917 O O   . THR A 262 ? 0.2138 0.2572 0.2193 0.0066  0.0325  0.0676  274 THR A O   
1918 C CB  . THR A 262 ? 0.2113 0.2369 0.2293 0.0006  0.0303  0.0629  274 THR A CB  
1919 O OG1 . THR A 262 ? 0.2116 0.2297 0.2322 0.0000  0.0283  0.0585  274 THR A OG1 
1920 C CG2 . THR A 262 ? 0.2139 0.2397 0.2367 -0.0033 0.0326  0.0659  274 THR A CG2 
1921 N N   . PRO A 263 ? 0.1991 0.2470 0.2094 0.0051  0.0353  0.0641  275 PRO A N   
1922 C CA  . PRO A 263 ? 0.1869 0.2450 0.1947 0.0056  0.0385  0.0692  275 PRO A CA  
1923 C C   . PRO A 263 ? 0.2174 0.2740 0.2279 0.0016  0.0393  0.0771  275 PRO A C   
1924 O O   . PRO A 263 ? 0.2141 0.2644 0.2309 -0.0025 0.0390  0.0788  275 PRO A O   
1925 C CB  . PRO A 263 ? 0.2344 0.2988 0.2458 0.0052  0.0408  0.0678  275 PRO A CB  
1926 C CG  . PRO A 263 ? 0.2281 0.2856 0.2416 0.0057  0.0382  0.0610  275 PRO A CG  
1927 C CD  . PRO A 263 ? 0.2486 0.2952 0.2631 0.0037  0.0354  0.0602  275 PRO A CD  
1928 N N   . VAL A 264 ? 0.2312 0.2927 0.2365 0.0026  0.0401  0.0819  276 VAL A N   
1929 C CA  . VAL A 264 ? 0.2269 0.2872 0.2342 -0.0014 0.0405  0.0901  276 VAL A CA  
1930 C C   . VAL A 264 ? 0.2522 0.3242 0.2572 -0.0026 0.0442  0.0963  276 VAL A C   
1931 O O   . VAL A 264 ? 0.3001 0.3703 0.3081 -0.0069 0.0438  0.1014  276 VAL A O   
1932 C CB  . VAL A 264 ? 0.2461 0.2997 0.2505 -0.0004 0.0372  0.0923  276 VAL A CB  
1933 C CG1 . VAL A 264 ? 0.2866 0.3289 0.2965 -0.0010 0.0344  0.0885  276 VAL A CG1 
1934 C CG2 . VAL A 264 ? 0.2531 0.3111 0.2487 0.0045  0.0362  0.0894  276 VAL A CG2 
1935 N N   . SER A 265 ? 0.2706 0.3530 0.2705 0.0011  0.0467  0.0934  277 SER A N   
1936 C CA  . SER A 265 ? 0.2294 0.3240 0.2278 0.0002  0.0504  0.0971  277 SER A CA  
1937 C C   . SER A 265 ? 0.2777 0.3819 0.2745 0.0049  0.0533  0.0912  277 SER A C   
1938 O O   . SER A 265 ? 0.2840 0.3827 0.2802 0.0084  0.0508  0.0835  277 SER A O   
1939 C CB  . SER A 265 ? 0.2901 0.3879 0.2804 0.0007  0.0501  0.1013  277 SER A CB  
1940 O OG  . SER A 265 ? 0.2897 0.3909 0.2707 0.0064  0.0503  0.0982  277 SER A OG  
1941 N N   . SER A 266 ? 0.2530 0.3692 0.2493 0.0051  0.0566  0.0923  278 SER A N   
1942 C CA  . SER A 266 ? 0.2752 0.4017 0.2689 0.0107  0.0596  0.0866  278 SER A CA  
1943 C C   . SER A 266 ? 0.2781 0.4047 0.2604 0.0167  0.0586  0.0821  278 SER A C   
1944 O O   . SER A 266 ? 0.2868 0.4200 0.2658 0.0221  0.0599  0.0757  278 SER A O   
1945 C CB  . SER A 266 ? 0.2743 0.4130 0.2708 0.0097  0.0629  0.0880  278 SER A CB  
1946 O OG  . SER A 266 ? 0.3510 0.4935 0.3412 0.0084  0.0636  0.0924  278 SER A OG  
1947 N N   . ASP A 267 ? 0.2388 0.3577 0.2156 0.0159  0.0555  0.0846  279 ASP A N   
1948 C CA  . ASP A 267 ? 0.2514 0.3697 0.2170 0.0209  0.0536  0.0805  279 ASP A CA  
1949 C C   . ASP A 267 ? 0.2536 0.3584 0.2177 0.0209  0.0479  0.0789  279 ASP A C   
1950 O O   . ASP A 267 ? 0.2687 0.3724 0.2237 0.0242  0.0456  0.0767  279 ASP A O   
1951 C CB  . ASP A 267 ? 0.2406 0.3691 0.1977 0.0206  0.0568  0.0868  279 ASP A CB  
1952 C CG  . ASP A 267 ? 0.2320 0.3634 0.1765 0.0266  0.0560  0.0814  279 ASP A CG  
1953 O OD1 . ASP A 267 ? 0.2783 0.4117 0.2216 0.0318  0.0562  0.0730  279 ASP A OD1 
1954 O OD2 . ASP A 267 ? 0.3157 0.4471 0.2515 0.0262  0.0549  0.0856  279 ASP A OD2 
1955 N N   . HIS A 268 ? 0.2112 0.3059 0.1839 0.0173  0.0454  0.0798  280 HIS A N   
1956 C CA  . HIS A 268 ? 0.1803 0.2637 0.1521 0.0173  0.0404  0.0788  280 HIS A CA  
1957 C C   . HIS A 268 ? 0.1847 0.2589 0.1647 0.0161  0.0381  0.0740  280 HIS A C   
1958 O O   . HIS A 268 ? 0.2085 0.2819 0.1962 0.0127  0.0399  0.0756  280 HIS A O   
1959 C CB  . HIS A 268 ? 0.2158 0.2959 0.1885 0.0134  0.0394  0.0872  280 HIS A CB  
1960 C CG  . HIS A 268 ? 0.2724 0.3604 0.2360 0.0139  0.0409  0.0928  280 HIS A CG  
1961 N ND1 . HIS A 268 ? 0.2796 0.3783 0.2422 0.0119  0.0457  0.0981  280 HIS A ND1 
1962 C CD2 . HIS A 268 ? 0.3198 0.4069 0.2746 0.0159  0.0381  0.0940  280 HIS A CD2 
1963 C CE1 . HIS A 268 ? 0.3436 0.4477 0.2966 0.0125  0.0461  0.1024  280 HIS A CE1 
1964 N NE2 . HIS A 268 ? 0.2653 0.3621 0.2132 0.0150  0.0413  0.1000  280 HIS A NE2 
1965 N N   . LEU A 269 ? 0.1864 0.2536 0.1642 0.0185  0.0341  0.0684  281 LEU A N   
1966 C CA  . LEU A 269 ? 0.1984 0.2563 0.1830 0.0170  0.0316  0.0643  281 LEU A CA  
1967 C C   . LEU A 269 ? 0.2499 0.3002 0.2360 0.0157  0.0282  0.0664  281 LEU A C   
1968 O O   . LEU A 269 ? 0.2918 0.3426 0.2719 0.0181  0.0259  0.0668  281 LEU A O   
1969 C CB  . LEU A 269 ? 0.1979 0.2542 0.1798 0.0204  0.0294  0.0560  281 LEU A CB  
1970 C CG  . LEU A 269 ? 0.1996 0.2638 0.1781 0.0236  0.0318  0.0525  281 LEU A CG  
1971 C CD1 . LEU A 269 ? 0.2263 0.2863 0.2017 0.0270  0.0283  0.0444  281 LEU A CD1 
1972 C CD2 . LEU A 269 ? 0.2206 0.2877 0.2067 0.0208  0.0351  0.0545  281 LEU A CD2 
1973 N N   . PHE A 270 ? 0.1890 0.2325 0.1832 0.0123  0.0279  0.0674  282 PHE A N   
1974 C CA  . PHE A 270 ? 0.1908 0.2275 0.1880 0.0115  0.0250  0.0692  282 PHE A CA  
1975 C C   . PHE A 270 ? 0.1652 0.1960 0.1654 0.0120  0.0224  0.0627  282 PHE A C   
1976 O O   . PHE A 270 ? 0.1759 0.2040 0.1802 0.0102  0.0234  0.0593  282 PHE A O   
1977 C CB  . PHE A 270 ? 0.2199 0.2528 0.2240 0.0076  0.0263  0.0747  282 PHE A CB  
1978 C CG  . PHE A 270 ? 0.1782 0.2042 0.1860 0.0075  0.0233  0.0765  282 PHE A CG  
1979 C CD1 . PHE A 270 ? 0.2276 0.2547 0.2318 0.0089  0.0212  0.0814  282 PHE A CD1 
1980 C CD2 . PHE A 270 ? 0.2151 0.2339 0.2301 0.0061  0.0226  0.0732  282 PHE A CD2 
1981 C CE1 . PHE A 270 ? 0.2623 0.2833 0.2709 0.0092  0.0181  0.0830  282 PHE A CE1 
1982 C CE2 . PHE A 270 ? 0.2469 0.2602 0.2663 0.0066  0.0200  0.0744  282 PHE A CE2 
1983 C CZ  . PHE A 270 ? 0.2698 0.2842 0.2865 0.0083  0.0177  0.0793  282 PHE A CZ  
1984 N N   . LEU A 271 ? 0.1907 0.2198 0.1886 0.0141  0.0189  0.0613  283 LEU A N   
1985 C CA  . LEU A 271 ? 0.1746 0.1991 0.1750 0.0144  0.0160  0.0558  283 LEU A CA  
1986 C C   . LEU A 271 ? 0.1799 0.1997 0.1871 0.0133  0.0145  0.0578  283 LEU A C   
1987 O O   . LEU A 271 ? 0.1937 0.2141 0.2004 0.0142  0.0132  0.0626  283 LEU A O   
1988 C CB  . LEU A 271 ? 0.2059 0.2327 0.1989 0.0176  0.0127  0.0522  283 LEU A CB  
1989 C CG  . LEU A 271 ? 0.1837 0.2066 0.1786 0.0177  0.0087  0.0475  283 LEU A CG  
1990 C CD1 . LEU A 271 ? 0.1853 0.2051 0.1827 0.0159  0.0092  0.0421  283 LEU A CD1 
1991 C CD2 . LEU A 271 ? 0.1922 0.2172 0.1792 0.0208  0.0047  0.0459  283 LEU A CD2 
1992 N N   . PHE A 272 ? 0.1333 0.1486 0.1469 0.0114  0.0145  0.0542  284 PHE A N   
1993 C CA  . PHE A 272 ? 0.1999 0.2116 0.2205 0.0111  0.0131  0.0549  284 PHE A CA  
1994 C C   . PHE A 272 ? 0.1939 0.2034 0.2182 0.0102  0.0120  0.0492  284 PHE A C   
1995 O O   . PHE A 272 ? 0.1806 0.1886 0.2051 0.0081  0.0137  0.0455  284 PHE A O   
1996 C CB  . PHE A 272 ? 0.2124 0.2201 0.2392 0.0090  0.0155  0.0583  284 PHE A CB  
1997 C CG  . PHE A 272 ? 0.1907 0.1945 0.2252 0.0094  0.0143  0.0579  284 PHE A CG  
1998 C CD1 . PHE A 272 ? 0.2218 0.2266 0.2574 0.0120  0.0111  0.0608  284 PHE A CD1 
1999 C CD2 . PHE A 272 ? 0.1907 0.1903 0.2314 0.0073  0.0162  0.0544  284 PHE A CD2 
2000 C CE1 . PHE A 272 ? 0.2301 0.2321 0.2740 0.0130  0.0098  0.0603  284 PHE A CE1 
2001 C CE2 . PHE A 272 ? 0.2227 0.2196 0.2709 0.0083  0.0154  0.0535  284 PHE A CE2 
2002 C CZ  . PHE A 272 ? 0.2034 0.2017 0.2537 0.0113  0.0123  0.0564  284 PHE A CZ  
2003 N N   . GLY A 273 ? 0.1772 0.1871 0.2048 0.0116  0.0091  0.0487  285 GLY A N   
2004 C CA  . GLY A 273 ? 0.1561 0.1648 0.1892 0.0103  0.0083  0.0443  285 GLY A CA  
2005 C C   . GLY A 273 ? 0.1570 0.1668 0.1859 0.0094  0.0065  0.0395  285 GLY A C   
2006 O O   . GLY A 273 ? 0.1652 0.1768 0.1866 0.0109  0.0045  0.0390  285 GLY A O   
2007 N N   . GLY A 274 ? 0.1935 0.2017 0.2271 0.0068  0.0073  0.0358  286 GLY A N   
2008 C CA  . GLY A 274 ? 0.1800 0.1881 0.2105 0.0051  0.0053  0.0315  286 GLY A CA  
2009 C C   . GLY A 274 ? 0.1617 0.1721 0.1969 0.0045  0.0025  0.0297  286 GLY A C   
2010 O O   . GLY A 274 ? 0.1464 0.1584 0.1892 0.0051  0.0031  0.0309  286 GLY A O   
2011 N N   . PHE A 275 ? 0.1573 0.1677 0.1881 0.0034  -0.0010 0.0268  287 PHE A N   
2012 C CA  . PHE A 275 ? 0.1520 0.1644 0.1872 0.0013  -0.0035 0.0246  287 PHE A CA  
2013 C C   . PHE A 275 ? 0.1583 0.1709 0.1870 0.0019  -0.0091 0.0233  287 PHE A C   
2014 O O   . PHE A 275 ? 0.1642 0.1734 0.1856 0.0013  -0.0102 0.0211  287 PHE A O   
2015 C CB  . PHE A 275 ? 0.1558 0.1660 0.1932 -0.0033 -0.0010 0.0216  287 PHE A CB  
2016 C CG  . PHE A 275 ? 0.1680 0.1814 0.2120 -0.0063 -0.0018 0.0199  287 PHE A CG  
2017 C CD1 . PHE A 275 ? 0.2204 0.2387 0.2730 -0.0047 -0.0015 0.0212  287 PHE A CD1 
2018 C CD2 . PHE A 275 ? 0.1837 0.1954 0.2257 -0.0108 -0.0029 0.0171  287 PHE A CD2 
2019 C CE1 . PHE A 275 ? 0.2015 0.2244 0.2613 -0.0075 -0.0017 0.0196  287 PHE A CE1 
2020 C CE2 . PHE A 275 ? 0.2228 0.2386 0.2711 -0.0143 -0.0032 0.0159  287 PHE A CE2 
2021 C CZ  . PHE A 275 ? 0.2392 0.2612 0.2967 -0.0125 -0.0024 0.0170  287 PHE A CZ  
2022 N N   . THR A 276 ? 0.1633 0.1793 0.1943 0.0032  -0.0130 0.0243  288 THR A N   
2023 C CA  . THR A 276 ? 0.1756 0.1910 0.1993 0.0040  -0.0187 0.0230  288 THR A CA  
2024 C C   . THR A 276 ? 0.2032 0.2169 0.2270 -0.0003 -0.0217 0.0194  288 THR A C   
2025 O O   . THR A 276 ? 0.1935 0.2079 0.2235 -0.0041 -0.0193 0.0184  288 THR A O   
2026 C CB  . THR A 276 ? 0.2336 0.2529 0.2591 0.0066  -0.0227 0.0255  288 THR A CB  
2027 O OG1 . THR A 276 ? 0.2441 0.2675 0.2797 0.0042  -0.0239 0.0254  288 THR A OG1 
2028 C CG2 . THR A 276 ? 0.2161 0.2368 0.2421 0.0103  -0.0201 0.0297  288 THR A CG2 
2029 N N   . THR A 277 ? 0.1818 0.1930 0.1977 0.0002  -0.0273 0.0176  289 THR A N   
2030 C CA  . THR A 277 ? 0.2290 0.2379 0.2442 -0.0040 -0.0317 0.0148  289 THR A CA  
2031 C C   . THR A 277 ? 0.2387 0.2533 0.2646 -0.0075 -0.0325 0.0158  289 THR A C   
2032 O O   . THR A 277 ? 0.2577 0.2722 0.2875 -0.0124 -0.0319 0.0144  289 THR A O   
2033 C CB  . THR A 277 ? 0.2770 0.2826 0.2826 -0.0020 -0.0384 0.0130  289 THR A CB  
2034 O OG1 . THR A 277 ? 0.2456 0.2465 0.2418 0.0011  -0.0373 0.0112  289 THR A OG1 
2035 C CG2 . THR A 277 ? 0.2661 0.2689 0.2715 -0.0067 -0.0442 0.0106  289 THR A CG2 
2036 N N   . ASP A 278 ? 0.2543 0.2743 0.2852 -0.0050 -0.0338 0.0182  290 ASP A N   
2037 C CA  A ASP A 278 ? 0.2480 0.2747 0.2902 -0.0076 -0.0346 0.0192  290 ASP A CA  
2038 C CA  B ASP A 278 ? 0.2588 0.2855 0.3010 -0.0077 -0.0346 0.0192  290 ASP A CA  
2039 C C   . ASP A 278 ? 0.2443 0.2753 0.2967 -0.0075 -0.0278 0.0204  290 ASP A C   
2040 O O   . ASP A 278 ? 0.2928 0.3307 0.3557 -0.0075 -0.0277 0.0217  290 ASP A O   
2041 C CB  A ASP A 278 ? 0.2712 0.3016 0.3144 -0.0050 -0.0402 0.0212  290 ASP A CB  
2042 C CB  B ASP A 278 ? 0.2790 0.3095 0.3225 -0.0053 -0.0403 0.0211  290 ASP A CB  
2043 C CG  A ASP A 278 ? 0.3008 0.3261 0.3326 -0.0047 -0.0471 0.0195  290 ASP A CG  
2044 C CG  B ASP A 278 ? 0.2763 0.3094 0.3222 -0.0001 -0.0382 0.0244  290 ASP A CG  
2045 O OD1 A ASP A 278 ? 0.3159 0.3381 0.3452 -0.0089 -0.0505 0.0169  290 ASP A OD1 
2046 O OD1 B ASP A 278 ? 0.2941 0.3240 0.3359 0.0023  -0.0336 0.0251  290 ASP A OD1 
2047 O OD2 A ASP A 278 ? 0.3276 0.3516 0.3523 -0.0004 -0.0494 0.0206  290 ASP A OD2 
2048 O OD2 B ASP A 278 ? 0.3076 0.3459 0.3594 0.0013  -0.0416 0.0267  290 ASP A OD2 
2049 N N   . LYS A 279 ? 0.2532 0.2803 0.3029 -0.0071 -0.0224 0.0199  291 LYS A N   
2050 C CA  . LYS A 279 ? 0.2399 0.2691 0.2975 -0.0078 -0.0159 0.0200  291 LYS A CA  
2051 C C   . LYS A 279 ? 0.2478 0.2807 0.3126 -0.0033 -0.0140 0.0228  291 LYS A C   
2052 O O   . LYS A 279 ? 0.2584 0.2960 0.3335 -0.0036 -0.0109 0.0227  291 LYS A O   
2053 C CB  . LYS A 279 ? 0.2516 0.2851 0.3165 -0.0131 -0.0149 0.0181  291 LYS A CB  
2054 C CG  . LYS A 279 ? 0.2190 0.2480 0.2766 -0.0180 -0.0176 0.0160  291 LYS A CG  
2055 C CD  . LYS A 279 ? 0.2494 0.2813 0.3124 -0.0239 -0.0144 0.0144  291 LYS A CD  
2056 C CE  . LYS A 279 ? 0.3299 0.3572 0.3862 -0.0294 -0.0185 0.0130  291 LYS A CE  
2057 N NZ  . LYS A 279 ? 0.2988 0.3263 0.3566 -0.0352 -0.0144 0.0117  291 LYS A NZ  
2058 N N   . GLN A 280 ? 0.2137 0.2444 0.2730 0.0008  -0.0157 0.0253  292 GLN A N   
2059 C CA  . GLN A 280 ? 0.2230 0.2552 0.2875 0.0049  -0.0139 0.0285  292 GLN A CA  
2060 C C   . GLN A 280 ? 0.2441 0.2713 0.3054 0.0057  -0.0087 0.0292  292 GLN A C   
2061 O O   . GLN A 280 ? 0.2012 0.2243 0.2528 0.0059  -0.0087 0.0293  292 GLN A O   
2062 C CB  . GLN A 280 ? 0.2579 0.2909 0.3181 0.0085  -0.0191 0.0317  292 GLN A CB  
2063 C CG  . GLN A 280 ? 0.3412 0.3804 0.4098 0.0093  -0.0236 0.0328  292 GLN A CG  
2064 C CD  . GLN A 280 ? 0.3863 0.4287 0.4663 0.0122  -0.0213 0.0352  292 GLN A CD  
2065 O OE1 . GLN A 280 ? 0.3965 0.4355 0.4772 0.0136  -0.0167 0.0361  292 GLN A OE1 
2066 N NE2 . GLN A 280 ? 0.4410 0.4896 0.5303 0.0132  -0.0249 0.0361  292 GLN A NE2 
2067 N N   . PRO A 281 ? 0.1656 0.1930 0.2347 0.0061  -0.0042 0.0294  293 PRO A N   
2068 C CA  . PRO A 281 ? 0.1928 0.2153 0.2593 0.0074  -0.0003 0.0311  293 PRO A CA  
2069 C C   . PRO A 281 ? 0.1870 0.2085 0.2493 0.0111  -0.0027 0.0357  293 PRO A C   
2070 O O   . PRO A 281 ? 0.2080 0.2326 0.2743 0.0138  -0.0061 0.0382  293 PRO A O   
2071 C CB  . PRO A 281 ? 0.2007 0.2240 0.2776 0.0077  0.0035  0.0303  293 PRO A CB  
2072 C CG  . PRO A 281 ? 0.1712 0.2001 0.2548 0.0051  0.0034  0.0269  293 PRO A CG  
2073 C CD  . PRO A 281 ? 0.2170 0.2494 0.2978 0.0052  -0.0024 0.0277  293 PRO A CD  
2074 N N   . LEU A 282 ? 0.1940 0.2116 0.2487 0.0112  -0.0009 0.0372  294 LEU A N   
2075 C CA  . LEU A 282 ? 0.1701 0.1873 0.2188 0.0140  -0.0027 0.0417  294 LEU A CA  
2076 C C   . LEU A 282 ? 0.1865 0.2004 0.2375 0.0149  0.0005  0.0453  294 LEU A C   
2077 O O   . LEU A 282 ? 0.1655 0.1762 0.2177 0.0129  0.0046  0.0440  294 LEU A O   
2078 C CB  . LEU A 282 ? 0.1664 0.1829 0.2038 0.0136  -0.0033 0.0409  294 LEU A CB  
2079 C CG  . LEU A 282 ? 0.1357 0.1538 0.1686 0.0130  -0.0073 0.0375  294 LEU A CG  
2080 C CD1 . LEU A 282 ? 0.1419 0.1584 0.1643 0.0131  -0.0072 0.0359  294 LEU A CD1 
2081 C CD2 . LEU A 282 ? 0.1823 0.2035 0.2151 0.0155  -0.0123 0.0398  294 LEU A CD2 
2082 N N   . SER A 283 ? 0.1861 0.2005 0.2372 0.0176  -0.0019 0.0502  295 SER A N   
2083 C CA  . SER A 283 ? 0.2112 0.2220 0.2628 0.0183  0.0000  0.0549  295 SER A CA  
2084 C C   . SER A 283 ? 0.2168 0.2284 0.2588 0.0193  -0.0014 0.0597  295 SER A C   
2085 O O   . SER A 283 ? 0.2316 0.2409 0.2737 0.0197  -0.0010 0.0649  295 SER A O   
2086 C CB  . SER A 283 ? 0.2355 0.2452 0.2971 0.0206  -0.0017 0.0571  295 SER A CB  
2087 O OG  . SER A 283 ? 0.2139 0.2269 0.2746 0.0231  -0.0068 0.0600  295 SER A OG  
2088 N N   . ASP A 284 ? 0.2332 0.2480 0.2667 0.0194  -0.0031 0.0582  296 ASP A N   
2089 C CA  . ASP A 284 ? 0.2252 0.2417 0.2490 0.0205  -0.0039 0.0624  296 ASP A CA  
2090 C C   . ASP A 284 ? 0.2375 0.2535 0.2567 0.0188  0.0007  0.0629  296 ASP A C   
2091 O O   . ASP A 284 ? 0.2071 0.2215 0.2286 0.0168  0.0037  0.0591  296 ASP A O   
2092 C CB  . ASP A 284 ? 0.2310 0.2509 0.2467 0.0220  -0.0078 0.0603  296 ASP A CB  
2093 C CG  . ASP A 284 ? 0.2061 0.2263 0.2191 0.0208  -0.0070 0.0539  296 ASP A CG  
2094 O OD1 . ASP A 284 ? 0.2599 0.2782 0.2794 0.0187  -0.0047 0.0505  296 ASP A OD1 
2095 O OD2 . ASP A 284 ? 0.2477 0.2697 0.2515 0.0219  -0.0091 0.0522  296 ASP A OD2 
2096 N N   . ALA A 285 ? 0.2366 0.2543 0.2494 0.0193  0.0011  0.0681  297 ALA A N   
2097 C CA  . ALA A 285 ? 0.2370 0.2558 0.2458 0.0177  0.0053  0.0696  297 ALA A CA  
2098 C C   . ALA A 285 ? 0.2250 0.2491 0.2228 0.0192  0.0049  0.0721  297 ALA A C   
2099 O O   . ALA A 285 ? 0.2899 0.3152 0.2840 0.0207  0.0017  0.0760  297 ALA A O   
2100 C CB  . ALA A 285 ? 0.2570 0.2722 0.2716 0.0157  0.0075  0.0748  297 ALA A CB  
2101 N N   . TRP A 286 ? 0.1891 0.2166 0.1816 0.0190  0.0080  0.0697  298 TRP A N   
2102 C CA  . TRP A 286 ? 0.2519 0.2854 0.2336 0.0208  0.0085  0.0710  298 TRP A CA  
2103 C C   . TRP A 286 ? 0.2272 0.2645 0.2077 0.0193  0.0136  0.0726  298 TRP A C   
2104 O O   . TRP A 286 ? 0.2351 0.2704 0.2220 0.0173  0.0161  0.0706  298 TRP A O   
2105 C CB  . TRP A 286 ? 0.2119 0.2469 0.1869 0.0235  0.0061  0.0645  298 TRP A CB  
2106 C CG  . TRP A 286 ? 0.2645 0.2965 0.2411 0.0245  0.0009  0.0620  298 TRP A CG  
2107 C CD1 . TRP A 286 ? 0.2186 0.2462 0.2043 0.0232  -0.0006 0.0593  298 TRP A CD1 
2108 C CD2 . TRP A 286 ? 0.2304 0.2640 0.1991 0.0268  -0.0036 0.0621  298 TRP A CD2 
2109 N NE1 . TRP A 286 ? 0.2306 0.2577 0.2156 0.0245  -0.0058 0.0579  298 TRP A NE1 
2110 C CE2 . TRP A 286 ? 0.2307 0.2608 0.2051 0.0267  -0.0080 0.0595  298 TRP A CE2 
2111 C CE3 . TRP A 286 ? 0.2250 0.2628 0.1819 0.0289  -0.0043 0.0640  298 TRP A CE3 
2112 C CZ2 . TRP A 286 ? 0.2521 0.2827 0.2217 0.0284  -0.0136 0.0590  298 TRP A CZ2 
2113 C CZ3 . TRP A 286 ? 0.2731 0.3106 0.2240 0.0307  -0.0098 0.0632  298 TRP A CZ3 
2114 C CH2 . TRP A 286 ? 0.2395 0.2733 0.1970 0.0303  -0.0147 0.0608  298 TRP A CH2 
2115 N N   . THR A 287 ? 0.2266 0.2704 0.1988 0.0203  0.0151  0.0760  299 THR A N   
2116 C CA  . THR A 287 ? 0.2478 0.2976 0.2180 0.0197  0.0200  0.0763  299 THR A CA  
2117 C C   . THR A 287 ? 0.2680 0.3236 0.2284 0.0235  0.0202  0.0714  299 THR A C   
2118 O O   . THR A 287 ? 0.3181 0.3757 0.2700 0.0257  0.0178  0.0722  299 THR A O   
2119 C CB  . THR A 287 ? 0.3031 0.3567 0.2727 0.0170  0.0227  0.0850  299 THR A CB  
2120 O OG1 . THR A 287 ? 0.3623 0.4092 0.3412 0.0137  0.0221  0.0890  299 THR A OG1 
2121 C CG2 . THR A 287 ? 0.2837 0.3451 0.2522 0.0163  0.0278  0.0852  299 THR A CG2 
2122 N N   . TYR A 288 ? 0.2504 0.3082 0.2118 0.0244  0.0226  0.0662  300 TYR A N   
2123 C CA  . TYR A 288 ? 0.2300 0.2934 0.1824 0.0285  0.0231  0.0612  300 TYR A CA  
2124 C C   . TYR A 288 ? 0.2191 0.2927 0.1686 0.0286  0.0286  0.0648  300 TYR A C   
2125 O O   . TYR A 288 ? 0.2394 0.3154 0.1957 0.0265  0.0321  0.0659  300 TYR A O   
2126 C CB  . TYR A 288 ? 0.2422 0.3020 0.1971 0.0301  0.0219  0.0530  300 TYR A CB  
2127 C CG  . TYR A 288 ? 0.2111 0.2760 0.1574 0.0348  0.0225  0.0475  300 TYR A CG  
2128 C CD1 . TYR A 288 ? 0.2188 0.2832 0.1552 0.0382  0.0189  0.0444  300 TYR A CD1 
2129 C CD2 . TYR A 288 ? 0.1967 0.2671 0.1450 0.0361  0.0263  0.0450  300 TYR A CD2 
2130 C CE1 . TYR A 288 ? 0.3168 0.3852 0.2445 0.0430  0.0193  0.0386  300 TYR A CE1 
2131 C CE2 . TYR A 288 ? 0.2421 0.3173 0.1829 0.0412  0.0267  0.0394  300 TYR A CE2 
2132 C CZ  . TYR A 288 ? 0.2132 0.2871 0.1433 0.0448  0.0233  0.0360  300 TYR A CZ  
2133 O OH  . TYR A 288 ? 0.2863 0.3642 0.2084 0.0502  0.0237  0.0297  300 TYR A OH  
2134 N N   . CYS A 289 ? 0.2193 0.2991 0.1585 0.0306  0.0292  0.0670  301 CYS A N   
2135 C CA  . CYS A 289 ? 0.2235 0.3147 0.1586 0.0310  0.0347  0.0702  301 CYS A CA  
2136 C C   . CYS A 289 ? 0.2449 0.3412 0.1757 0.0359  0.0364  0.0621  301 CYS A C   
2137 O O   . CYS A 289 ? 0.2503 0.3452 0.1721 0.0401  0.0335  0.0566  301 CYS A O   
2138 C CB  . CYS A 289 ? 0.2587 0.3545 0.1837 0.0308  0.0347  0.0763  301 CYS A CB  
2139 S SG  . CYS A 289 ? 0.3236 0.4348 0.2436 0.0306  0.0421  0.0807  301 CYS A SG  
2140 N N   . ILE A 290 ? 0.2303 0.3320 0.1680 0.0355  0.0405  0.0612  302 ILE A N   
2141 C CA  . ILE A 290 ? 0.2252 0.3308 0.1611 0.0404  0.0417  0.0532  302 ILE A CA  
2142 C C   . ILE A 290 ? 0.2530 0.3695 0.1775 0.0449  0.0449  0.0519  302 ILE A C   
2143 O O   . ILE A 290 ? 0.2841 0.3998 0.2011 0.0503  0.0430  0.0443  302 ILE A O   
2144 C CB  . ILE A 290 ? 0.2473 0.3568 0.1943 0.0386  0.0452  0.0535  302 ILE A CB  
2145 C CG1 . ILE A 290 ? 0.2021 0.3001 0.1588 0.0349  0.0418  0.0529  302 ILE A CG1 
2146 C CG2 . ILE A 290 ? 0.2345 0.3504 0.1799 0.0442  0.0470  0.0460  302 ILE A CG2 
2147 C CD1 . ILE A 290 ? 0.2220 0.3230 0.1893 0.0312  0.0449  0.0561  302 ILE A CD1 
2148 N N   . SER A 291 ? 0.2655 0.3920 0.1882 0.0424  0.0497  0.0594  303 SER A N   
2149 C CA  . SER A 291 ? 0.2901 0.4289 0.2020 0.0462  0.0539  0.0588  303 SER A CA  
2150 C C   . SER A 291 ? 0.2758 0.4105 0.1739 0.0491  0.0499  0.0563  303 SER A C   
2151 O O   . SER A 291 ? 0.2922 0.4327 0.1800 0.0546  0.0512  0.0506  303 SER A O   
2152 C CB  . SER A 291 ? 0.2743 0.4235 0.1880 0.0413  0.0591  0.0684  303 SER A CB  
2153 O OG  . SER A 291 ? 0.2696 0.4118 0.1824 0.0363  0.0560  0.0761  303 SER A OG  
2154 N N   . LYS A 292 ? 0.2918 0.4169 0.1895 0.0458  0.0449  0.0605  304 LYS A N   
2155 C CA  . LYS A 292 ? 0.3152 0.4357 0.2006 0.0481  0.0402  0.0586  304 LYS A CA  
2156 C C   . LYS A 292 ? 0.2809 0.3903 0.1660 0.0513  0.0339  0.0499  304 LYS A C   
2157 O O   . LYS A 292 ? 0.3423 0.4483 0.2164 0.0539  0.0297  0.0468  304 LYS A O   
2158 C CB  . LYS A 292 ? 0.3475 0.4638 0.2323 0.0431  0.0376  0.0679  304 LYS A CB  
2159 C CG  . LYS A 292 ? 0.3727 0.4998 0.2528 0.0401  0.0427  0.0769  304 LYS A CG  
2160 C CD  . LYS A 292 ? 0.3819 0.5031 0.2653 0.0344  0.0396  0.0865  304 LYS A CD  
2161 C CE  . LYS A 292 ? 0.4782 0.5902 0.3551 0.0356  0.0323  0.0859  304 LYS A CE  
2162 N NZ  . LYS A 292 ? 0.4430 0.5429 0.3313 0.0348  0.0273  0.0830  304 LYS A NZ  
2163 N N   . ASN A 293 ? 0.3055 0.4091 0.2017 0.0508  0.0329  0.0461  305 ASN A N   
2164 C CA  . ASN A 293 ? 0.2748 0.3672 0.1720 0.0525  0.0266  0.0389  305 ASN A CA  
2165 C C   . ASN A 293 ? 0.2997 0.3842 0.1939 0.0504  0.0207  0.0416  305 ASN A C   
2166 O O   . ASN A 293 ? 0.3142 0.3945 0.1995 0.0532  0.0159  0.0370  305 ASN A O   
2167 C CB  . ASN A 293 ? 0.3127 0.4063 0.2012 0.0590  0.0257  0.0294  305 ASN A CB  
2168 C CG  . ASN A 293 ? 0.3225 0.4041 0.2124 0.0603  0.0190  0.0221  305 ASN A CG  
2169 O OD1 . ASN A 293 ? 0.3065 0.3811 0.2069 0.0569  0.0169  0.0226  305 ASN A OD1 
2170 N ND2 . ASN A 293 ? 0.3506 0.4297 0.2292 0.0650  0.0154  0.0151  305 ASN A ND2 
2171 N N   . GLU A 294 ? 0.2724 0.3551 0.1741 0.0455  0.0210  0.0494  306 GLU A N   
2172 C CA  . GLU A 294 ? 0.3135 0.3900 0.2141 0.0434  0.0157  0.0532  306 GLU A CA  
2173 C C   . GLU A 294 ? 0.3064 0.3769 0.2206 0.0389  0.0149  0.0575  306 GLU A C   
2174 O O   . GLU A 294 ? 0.2639 0.3372 0.1854 0.0361  0.0193  0.0618  306 GLU A O   
2175 C CB  . GLU A 294 ? 0.3328 0.4153 0.2238 0.0429  0.0167  0.0602  306 GLU A CB  
2176 C CG  . GLU A 294 ? 0.3870 0.4637 0.2797 0.0400  0.0117  0.0663  306 GLU A CG  
2177 C CD  . GLU A 294 ? 0.4519 0.5339 0.3350 0.0388  0.0125  0.0740  306 GLU A CD  
2178 O OE1 . GLU A 294 ? 0.4494 0.5338 0.3192 0.0416  0.0105  0.0719  306 GLU A OE1 
2179 O OE2 . GLU A 294 ? 0.4466 0.5302 0.3351 0.0350  0.0148  0.0823  306 GLU A OE2 
2180 N N   . TRP A 295 ? 0.2500 0.3125 0.1674 0.0381  0.0092  0.0562  307 TRP A N   
2181 C CA  . TRP A 295 ? 0.2530 0.3099 0.1823 0.0344  0.0080  0.0602  307 TRP A CA  
2182 C C   . TRP A 295 ? 0.2997 0.3567 0.2279 0.0326  0.0063  0.0683  307 TRP A C   
2183 O O   . TRP A 295 ? 0.2438 0.3016 0.1628 0.0342  0.0028  0.0693  307 TRP A O   
2184 C CB  . TRP A 295 ? 0.2235 0.2728 0.1580 0.0343  0.0030  0.0549  307 TRP A CB  
2185 C CG  . TRP A 295 ? 0.2566 0.3036 0.1944 0.0350  0.0037  0.0478  307 TRP A CG  
2186 C CD1 . TRP A 295 ? 0.2525 0.2987 0.1834 0.0381  0.0016  0.0407  307 TRP A CD1 
2187 C CD2 . TRP A 295 ? 0.1916 0.2358 0.1401 0.0323  0.0062  0.0471  307 TRP A CD2 
2188 N NE1 . TRP A 295 ? 0.2488 0.2918 0.1858 0.0374  0.0024  0.0360  307 TRP A NE1 
2189 C CE2 . TRP A 295 ? 0.1936 0.2356 0.1412 0.0337  0.0053  0.0399  307 TRP A CE2 
2190 C CE3 . TRP A 295 ? 0.2022 0.2449 0.1604 0.0287  0.0087  0.0518  307 TRP A CE3 
2191 C CZ2 . TRP A 295 ? 0.2283 0.2671 0.1842 0.0315  0.0069  0.0377  307 TRP A CZ2 
2192 C CZ3 . TRP A 295 ? 0.1641 0.2037 0.1304 0.0267  0.0105  0.0490  307 TRP A CZ3 
2193 C CH2 . TRP A 295 ? 0.1728 0.2107 0.1376 0.0279  0.0096  0.0423  307 TRP A CH2 
2194 N N   . ILE A 296 ? 0.2654 0.3209 0.2026 0.0292  0.0084  0.0741  308 ILE A N   
2195 C CA  . ILE A 296 ? 0.2778 0.3315 0.2165 0.0273  0.0063  0.0821  308 ILE A CA  
2196 C C   . ILE A 296 ? 0.2817 0.3278 0.2333 0.0256  0.0039  0.0821  308 ILE A C   
2197 O O   . ILE A 296 ? 0.3130 0.3569 0.2733 0.0237  0.0069  0.0807  308 ILE A O   
2198 C CB  . ILE A 296 ? 0.3239 0.3827 0.2609 0.0248  0.0108  0.0899  308 ILE A CB  
2199 C CG1 . ILE A 296 ? 0.3613 0.4191 0.3090 0.0218  0.0151  0.0907  308 ILE A CG1 
2200 C CG2 . ILE A 296 ? 0.3415 0.4094 0.2666 0.0267  0.0143  0.0888  308 ILE A CG2 
2201 C CD1 . ILE A 296 ? 0.3758 0.4268 0.3333 0.0185  0.0137  0.0969  308 ILE A CD1 
2202 N N   . GLN A 297 ? 0.2807 0.3231 0.2336 0.0263  -0.0015 0.0833  309 GLN A N   
2203 C CA  . GLN A 297 ? 0.2663 0.3026 0.2319 0.0250  -0.0033 0.0837  309 GLN A CA  
2204 C C   . GLN A 297 ? 0.2654 0.2997 0.2364 0.0224  -0.0013 0.0911  309 GLN A C   
2205 O O   . GLN A 297 ? 0.3657 0.4023 0.3305 0.0217  -0.0015 0.0979  309 GLN A O   
2206 C CB  . GLN A 297 ? 0.2853 0.3190 0.2520 0.0266  -0.0098 0.0832  309 GLN A CB  
2207 C CG  . GLN A 297 ? 0.2986 0.3273 0.2792 0.0259  -0.0113 0.0826  309 GLN A CG  
2208 C CD  . GLN A 297 ? 0.3476 0.3755 0.3312 0.0273  -0.0162 0.0777  309 GLN A CD  
2209 O OE1 . GLN A 297 ? 0.3139 0.3441 0.2888 0.0288  -0.0194 0.0755  309 GLN A OE1 
2210 N NE2 . GLN A 297 ? 0.3234 0.3484 0.3193 0.0268  -0.0168 0.0759  309 GLN A NE2 
2211 N N   . PHE A 298 ? 0.2756 0.3053 0.2575 0.0208  0.0004  0.0900  310 PHE A N   
2212 C CA  . PHE A 298 ? 0.3183 0.3450 0.3058 0.0180  0.0026  0.0959  310 PHE A CA  
2213 C C   . PHE A 298 ? 0.3291 0.3490 0.3264 0.0184  -0.0011 0.0976  310 PHE A C   
2214 O O   . PHE A 298 ? 0.3291 0.3465 0.3334 0.0195  -0.0023 0.0920  310 PHE A O   
2215 C CB  . PHE A 298 ? 0.3106 0.3373 0.3024 0.0158  0.0077  0.0929  310 PHE A CB  
2216 C CG  . PHE A 298 ? 0.2986 0.3213 0.2966 0.0126  0.0096  0.0984  310 PHE A CG  
2217 C CD1 . PHE A 298 ? 0.3109 0.3261 0.3193 0.0119  0.0088  0.0970  310 PHE A CD1 
2218 C CD2 . PHE A 298 ? 0.3370 0.3634 0.3304 0.0102  0.0122  0.1047  310 PHE A CD2 
2219 C CE1 . PHE A 298 ? 0.3196 0.3298 0.3332 0.0090  0.0100  0.1016  310 PHE A CE1 
2220 C CE2 . PHE A 298 ? 0.4004 0.4225 0.3997 0.0067  0.0133  0.1099  310 PHE A CE2 
2221 C CZ  . PHE A 298 ? 0.3880 0.4013 0.3971 0.0062  0.0120  0.1082  310 PHE A CZ  
2222 N N   . ASN A 299 ? 0.3641 0.3813 0.3620 0.0175  -0.0030 0.1054  311 ASN A N   
2223 C CA  . ASN A 299 ? 0.3707 0.3814 0.3777 0.0186  -0.0072 0.1073  311 ASN A CA  
2224 C C   . ASN A 299 ? 0.3653 0.3695 0.3820 0.0166  -0.0048 0.1078  311 ASN A C   
2225 O O   . ASN A 299 ? 0.4000 0.4033 0.4149 0.0135  -0.0021 0.1124  311 ASN A O   
2226 C CB  . ASN A 299 ? 0.4338 0.4439 0.4360 0.0191  -0.0119 0.1155  311 ASN A CB  
2227 C CG  . ASN A 299 ? 0.4788 0.4940 0.4728 0.0215  -0.0156 0.1141  311 ASN A CG  
2228 O OD1 . ASN A 299 ? 0.4547 0.4724 0.4490 0.0232  -0.0156 0.1068  311 ASN A OD1 
2229 N ND2 . ASN A 299 ? 0.5644 0.5806 0.5504 0.0214  -0.0191 0.1212  311 ASN A ND2 
2230 N N   . HIS A 300 ? 0.3833 0.3834 0.4101 0.0182  -0.0057 0.1029  312 HIS A N   
2231 C CA  . HIS A 300 ? 0.3652 0.3589 0.4007 0.0166  -0.0032 0.1014  312 HIS A CA  
2232 C C   . HIS A 300 ? 0.3572 0.3459 0.4032 0.0195  -0.0066 0.0997  312 HIS A C   
2233 O O   . HIS A 300 ? 0.3595 0.3511 0.4067 0.0225  -0.0101 0.0983  312 HIS A O   
2234 C CB  . HIS A 300 ? 0.3594 0.3551 0.3952 0.0150  0.0016  0.0944  312 HIS A CB  
2235 C CG  . HIS A 300 ? 0.3464 0.3453 0.3840 0.0171  0.0011  0.0870  312 HIS A CG  
2236 N ND1 . HIS A 300 ? 0.3464 0.3423 0.3936 0.0185  0.0004  0.0825  312 HIS A ND1 
2237 C CD2 . HIS A 300 ? 0.3483 0.3532 0.3794 0.0178  0.0010  0.0834  312 HIS A CD2 
2238 C CE1 . HIS A 300 ? 0.3485 0.3488 0.3951 0.0194  0.0000  0.0770  312 HIS A CE1 
2239 N NE2 . HIS A 300 ? 0.2819 0.2870 0.3188 0.0190  0.0000  0.0774  312 HIS A NE2 
2240 N N   . PRO A 301 ? 0.3868 0.3680 0.4407 0.0190  -0.0057 0.0997  313 PRO A N   
2241 C CA  . PRO A 301 ? 0.4113 0.3879 0.4761 0.0224  -0.0086 0.0978  313 PRO A CA  
2242 C C   . PRO A 301 ? 0.3616 0.3393 0.4336 0.0234  -0.0058 0.0888  313 PRO A C   
2243 O O   . PRO A 301 ? 0.4127 0.3866 0.4945 0.0261  -0.0070 0.0865  313 PRO A O   
2244 C CB  . PRO A 301 ? 0.3942 0.3613 0.4625 0.0211  -0.0093 0.1026  313 PRO A CB  
2245 C CG  . PRO A 301 ? 0.4076 0.3745 0.4708 0.0165  -0.0045 0.1025  313 PRO A CG  
2246 C CD  . PRO A 301 ? 0.4157 0.3921 0.4689 0.0152  -0.0027 0.1025  313 PRO A CD  
2247 N N   . TYR A 302 ? 0.3474 0.3301 0.4149 0.0214  -0.0021 0.0838  314 TYR A N   
2248 C CA  . TYR A 302 ? 0.3247 0.3088 0.3977 0.0216  0.0007  0.0757  314 TYR A CA  
2249 C C   . TYR A 302 ? 0.3298 0.3214 0.4024 0.0232  -0.0011 0.0722  314 TYR A C   
2250 O O   . TYR A 302 ? 0.3040 0.2985 0.3769 0.0219  0.0014  0.0662  314 TYR A O   
2251 C CB  . TYR A 302 ? 0.3410 0.3242 0.4099 0.0177  0.0055  0.0726  314 TYR A CB  
2252 C CG  . TYR A 302 ? 0.3439 0.3199 0.4129 0.0153  0.0070  0.0763  314 TYR A CG  
2253 C CD1 . TYR A 302 ? 0.3738 0.3424 0.4506 0.0160  0.0074  0.0747  314 TYR A CD1 
2254 C CD2 . TYR A 302 ? 0.3741 0.3511 0.4354 0.0124  0.0081  0.0810  314 TYR A CD2 
2255 C CE1 . TYR A 302 ? 0.3800 0.3411 0.4566 0.0135  0.0081  0.0780  314 TYR A CE1 
2256 C CE2 . TYR A 302 ? 0.3613 0.3321 0.4231 0.0096  0.0091  0.0847  314 TYR A CE2 
2257 C CZ  . TYR A 302 ? 0.4022 0.3644 0.4715 0.0100  0.0089  0.0832  314 TYR A CZ  
2258 O OH  . TYR A 302 ? 0.4544 0.4095 0.5240 0.0069  0.0093  0.0868  314 TYR A OH  
2259 N N   . THR A 303 ? 0.3216 0.3160 0.3932 0.0257  -0.0059 0.0759  315 THR A N   
2260 C CA  . THR A 303 ? 0.3316 0.3329 0.4022 0.0268  -0.0083 0.0729  315 THR A CA  
2261 C C   . THR A 303 ? 0.2962 0.2997 0.3776 0.0281  -0.0078 0.0670  315 THR A C   
2262 O O   . THR A 303 ? 0.2394 0.2484 0.3202 0.0276  -0.0085 0.0631  315 THR A O   
2263 C CB  . THR A 303 ? 0.3026 0.3059 0.3699 0.0291  -0.0140 0.0784  315 THR A CB  
2264 O OG1 . THR A 303 ? 0.3985 0.3968 0.4720 0.0312  -0.0166 0.0835  315 THR A OG1 
2265 C CG2 . THR A 303 ? 0.3400 0.3450 0.3939 0.0274  -0.0140 0.0821  315 THR A CG2 
2266 N N   . GLU A 304 ? 0.2814 0.2808 0.3725 0.0295  -0.0064 0.0659  316 GLU A N   
2267 C CA  . GLU A 304 ? 0.3331 0.3355 0.4346 0.0307  -0.0048 0.0599  316 GLU A CA  
2268 C C   . GLU A 304 ? 0.2609 0.2614 0.3619 0.0275  0.0011  0.0543  316 GLU A C   
2269 O O   . GLU A 304 ? 0.2631 0.2649 0.3725 0.0281  0.0035  0.0494  316 GLU A O   
2270 C CB  . GLU A 304 ? 0.3371 0.3368 0.4500 0.0349  -0.0070 0.0612  316 GLU A CB  
2271 C CG  . GLU A 304 ? 0.3758 0.3824 0.5004 0.0375  -0.0076 0.0566  316 GLU A CG  
2272 C CD  . GLU A 304 ? 0.4239 0.4279 0.5603 0.0426  -0.0100 0.0579  316 GLU A CD  
2273 O OE1 . GLU A 304 ? 0.4490 0.4461 0.5836 0.0441  -0.0131 0.0636  316 GLU A OE1 
2274 O OE2 . GLU A 304 ? 0.4886 0.4978 0.6365 0.0450  -0.0089 0.0532  316 GLU A OE2 
2275 N N   . LYS A 305 ? 0.2592 0.2571 0.3506 0.0241  0.0035  0.0550  317 LYS A N   
2276 C CA  . LYS A 305 ? 0.2621 0.2576 0.3522 0.0207  0.0084  0.0503  317 LYS A CA  
2277 C C   . LYS A 305 ? 0.2078 0.2068 0.2889 0.0175  0.0093  0.0486  317 LYS A C   
2278 O O   . LYS A 305 ? 0.2215 0.2178 0.2956 0.0151  0.0111  0.0498  317 LYS A O   
2279 C CB  . LYS A 305 ? 0.3102 0.2976 0.3993 0.0197  0.0105  0.0527  317 LYS A CB  
2280 C CG  . LYS A 305 ? 0.3088 0.2912 0.4076 0.0228  0.0101  0.0525  317 LYS A CG  
2281 C CD  . LYS A 305 ? 0.3390 0.3126 0.4375 0.0209  0.0128  0.0523  317 LYS A CD  
2282 C CE  . LYS A 305 ? 0.3860 0.3537 0.4938 0.0246  0.0118  0.0518  317 LYS A CE  
2283 N NZ  . LYS A 305 ? 0.4137 0.3712 0.5200 0.0229  0.0125  0.0539  317 LYS A NZ  
2284 N N   . PRO A 306 ? 0.2315 0.2365 0.3131 0.0174  0.0078  0.0456  318 PRO A N   
2285 C CA  . PRO A 306 ? 0.2062 0.2133 0.2793 0.0145  0.0081  0.0435  318 PRO A CA  
2286 C C   . PRO A 306 ? 0.2222 0.2261 0.2941 0.0109  0.0125  0.0396  318 PRO A C   
2287 O O   . PRO A 306 ? 0.2375 0.2396 0.3158 0.0104  0.0153  0.0368  318 PRO A O   
2288 C CB  . PRO A 306 ? 0.1856 0.1988 0.2615 0.0148  0.0052  0.0409  318 PRO A CB  
2289 C CG  . PRO A 306 ? 0.1873 0.2024 0.2748 0.0168  0.0055  0.0398  318 PRO A CG  
2290 C CD  . PRO A 306 ? 0.2204 0.2306 0.3106 0.0197  0.0055  0.0439  318 PRO A CD  
2291 N N   . ARG A 307 ? 0.2030 0.2061 0.2664 0.0087  0.0131  0.0394  319 ARG A N   
2292 C CA  . ARG A 307 ? 0.2126 0.2126 0.2742 0.0051  0.0166  0.0361  319 ARG A CA  
2293 C C   . ARG A 307 ? 0.2164 0.2182 0.2709 0.0030  0.0156  0.0338  319 ARG A C   
2294 O O   . ARG A 307 ? 0.1856 0.1891 0.2339 0.0043  0.0132  0.0357  319 ARG A O   
2295 C CB  . ARG A 307 ? 0.2218 0.2168 0.2812 0.0042  0.0189  0.0389  319 ARG A CB  
2296 C CG  . ARG A 307 ? 0.2289 0.2198 0.2948 0.0056  0.0199  0.0407  319 ARG A CG  
2297 C CD  . ARG A 307 ? 0.1999 0.1891 0.2721 0.0047  0.0225  0.0358  319 ARG A CD  
2298 N NE  . ARG A 307 ? 0.2548 0.2387 0.3328 0.0064  0.0234  0.0370  319 ARG A NE  
2299 C CZ  . ARG A 307 ? 0.2315 0.2164 0.3174 0.0099  0.0223  0.0367  319 ARG A CZ  
2300 N NH1 . ARG A 307 ? 0.2143 0.2058 0.3037 0.0119  0.0204  0.0357  319 ARG A NH1 
2301 N NH2 . ARG A 307 ? 0.3063 0.2850 0.3971 0.0116  0.0229  0.0374  319 ARG A NH2 
2302 N N   . LEU A 308 ? 0.1770 0.1779 0.2318 -0.0004 0.0172  0.0296  320 LEU A N   
2303 C CA  . LEU A 308 ? 0.1953 0.1962 0.2435 -0.0028 0.0161  0.0274  320 LEU A CA  
2304 C C   . LEU A 308 ? 0.2028 0.1995 0.2501 -0.0066 0.0192  0.0250  320 LEU A C   
2305 O O   . LEU A 308 ? 0.1921 0.1876 0.2444 -0.0081 0.0218  0.0232  320 LEU A O   
2306 C CB  . LEU A 308 ? 0.1842 0.1885 0.2326 -0.0036 0.0131  0.0248  320 LEU A CB  
2307 C CG  . LEU A 308 ? 0.2068 0.2141 0.2630 -0.0049 0.0139  0.0226  320 LEU A CG  
2308 C CD1 . LEU A 308 ? 0.2670 0.2755 0.3210 -0.0087 0.0122  0.0195  320 LEU A CD1 
2309 C CD2 . LEU A 308 ? 0.1841 0.1959 0.2458 -0.0011 0.0115  0.0248  320 LEU A CD2 
2310 N N   . TRP A 309 ? 0.1526 0.1475 0.1937 -0.0080 0.0187  0.0247  321 TRP A N   
2311 C CA  . TRP A 309 ? 0.1800 0.1708 0.2191 -0.0118 0.0208  0.0230  321 TRP A CA  
2312 C C   . TRP A 309 ? 0.2242 0.2117 0.2660 -0.0119 0.0239  0.0250  321 TRP A C   
2313 O O   . TRP A 309 ? 0.2040 0.1877 0.2460 -0.0151 0.0260  0.0232  321 TRP A O   
2314 C CB  . TRP A 309 ? 0.1947 0.1847 0.2349 -0.0157 0.0214  0.0191  321 TRP A CB  
2315 C CG  . TRP A 309 ? 0.1700 0.1568 0.2046 -0.0193 0.0205  0.0174  321 TRP A CG  
2316 C CD1 . TRP A 309 ? 0.1662 0.1511 0.1964 -0.0188 0.0196  0.0186  321 TRP A CD1 
2317 C CD2 . TRP A 309 ? 0.1892 0.1743 0.2221 -0.0239 0.0203  0.0144  321 TRP A CD2 
2318 N NE1 . TRP A 309 ? 0.1586 0.1404 0.1848 -0.0225 0.0184  0.0165  321 TRP A NE1 
2319 C CE2 . TRP A 309 ? 0.1401 0.1215 0.1674 -0.0259 0.0187  0.0141  321 TRP A CE2 
2320 C CE3 . TRP A 309 ? 0.1931 0.1800 0.2289 -0.0266 0.0213  0.0121  321 TRP A CE3 
2321 C CZ2 . TRP A 309 ? 0.1615 0.1399 0.1853 -0.0308 0.0176  0.0119  321 TRP A CZ2 
2322 C CZ3 . TRP A 309 ? 0.2137 0.1984 0.2458 -0.0318 0.0208  0.0100  321 TRP A CZ3 
2323 C CH2 . TRP A 309 ? 0.1714 0.1513 0.1972 -0.0339 0.0186  0.0100  321 TRP A CH2 
2324 N N   . HIS A 310 ? 0.2145 0.2032 0.2581 -0.0086 0.0237  0.0287  322 HIS A N   
2325 C CA  . HIS A 310 ? 0.2151 0.2007 0.2603 -0.0087 0.0256  0.0318  322 HIS A CA  
2326 C C   . HIS A 310 ? 0.2020 0.1875 0.2423 -0.0099 0.0256  0.0335  322 HIS A C   
2327 O O   . HIS A 310 ? 0.2276 0.2155 0.2636 -0.0099 0.0241  0.0321  322 HIS A O   
2328 C CB  . HIS A 310 ? 0.2058 0.1929 0.2539 -0.0050 0.0247  0.0358  322 HIS A CB  
2329 C CG  . HIS A 310 ? 0.2368 0.2288 0.2806 -0.0024 0.0222  0.0383  322 HIS A CG  
2330 N ND1 . HIS A 310 ? 0.1864 0.1820 0.2286 -0.0011 0.0198  0.0361  322 HIS A ND1 
2331 C CD2 . HIS A 310 ? 0.2246 0.2186 0.2647 -0.0011 0.0219  0.0425  322 HIS A CD2 
2332 C CE1 . HIS A 310 ? 0.2005 0.1994 0.2378 0.0013  0.0179  0.0385  322 HIS A CE1 
2333 N NE2 . HIS A 310 ? 0.1757 0.1742 0.2115 0.0014  0.0194  0.0423  322 HIS A NE2 
2334 N N   . THR A 311 ? 0.1839 0.1670 0.2255 -0.0107 0.0271  0.0367  323 THR A N   
2335 C CA  . THR A 311 ? 0.2309 0.2158 0.2693 -0.0114 0.0273  0.0394  323 THR A CA  
2336 C C   . THR A 311 ? 0.2540 0.2408 0.2934 -0.0095 0.0275  0.0451  323 THR A C   
2337 O O   . THR A 311 ? 0.2122 0.1962 0.2552 -0.0086 0.0275  0.0471  323 THR A O   
2338 C CB  . THR A 311 ? 0.2027 0.1833 0.2414 -0.0155 0.0286  0.0384  323 THR A CB  
2339 O OG1 . THR A 311 ? 0.1987 0.1739 0.2414 -0.0168 0.0299  0.0396  323 THR A OG1 
2340 C CG2 . THR A 311 ? 0.1867 0.1654 0.2235 -0.0179 0.0281  0.0333  323 THR A CG2 
2341 N N   . ALA A 312 ? 0.2396 0.2313 0.2757 -0.0089 0.0276  0.0479  324 ALA A N   
2342 C CA  . ALA A 312 ? 0.2255 0.2200 0.2616 -0.0081 0.0281  0.0539  324 ALA A CA  
2343 C C   . ALA A 312 ? 0.2397 0.2369 0.2752 -0.0104 0.0296  0.0564  324 ALA A C   
2344 O O   . ALA A 312 ? 0.2229 0.2235 0.2560 -0.0103 0.0297  0.0538  324 ALA A O   
2345 C CB  . ALA A 312 ? 0.2362 0.2367 0.2682 -0.0041 0.0268  0.0556  324 ALA A CB  
2346 N N   . CYS A 313 ? 0.2286 0.2242 0.2667 -0.0124 0.0305  0.0615  325 CYS A N   
2347 C CA  . CYS A 313 ? 0.2251 0.2245 0.2638 -0.0150 0.0319  0.0652  325 CYS A CA  
2348 C C   . CYS A 313 ? 0.2643 0.2671 0.3028 -0.0150 0.0324  0.0724  325 CYS A C   
2349 O O   . CYS A 313 ? 0.2524 0.2500 0.2926 -0.0150 0.0313  0.0752  325 CYS A O   
2350 C CB  . CYS A 313 ? 0.2533 0.2459 0.2958 -0.0196 0.0321  0.0645  325 CYS A CB  
2351 S SG  . CYS A 313 ? 0.2701 0.2582 0.3121 -0.0211 0.0315  0.0569  325 CYS A SG  
2352 N N   . ALA A 314 ? 0.2626 0.2743 0.2993 -0.0150 0.0339  0.0756  326 ALA A N   
2353 C CA  . ALA A 314 ? 0.2749 0.2909 0.3110 -0.0159 0.0348  0.0831  326 ALA A CA  
2354 C C   . ALA A 314 ? 0.3117 0.3243 0.3508 -0.0203 0.0337  0.0835  326 ALA A C   
2355 O O   . ALA A 314 ? 0.3403 0.3532 0.3813 -0.0223 0.0339  0.0805  326 ALA A O   
2356 C CB  . ALA A 314 ? 0.2747 0.3029 0.3063 -0.0134 0.0367  0.0844  326 ALA A CB  
2357 N N   . SER A 315 ? 0.3252 0.3343 0.3646 -0.0217 0.0322  0.0875  327 SER A N   
2358 C CA  . SER A 315 ? 0.3589 0.3645 0.4004 -0.0259 0.0309  0.0886  327 SER A CA  
2359 C C   . SER A 315 ? 0.4158 0.4310 0.4558 -0.0272 0.0322  0.0936  327 SER A C   
2360 O O   . SER A 315 ? 0.3429 0.3660 0.3796 -0.0248 0.0336  0.0967  327 SER A O   
2361 C CB  . SER A 315 ? 0.3678 0.3624 0.4107 -0.0270 0.0283  0.0899  327 SER A CB  
2362 O OG  . SER A 315 ? 0.4311 0.4273 0.4721 -0.0261 0.0275  0.0957  327 SER A OG  
2363 N N   . ASP A 316 ? 0.3712 0.3858 0.4135 -0.0311 0.0316  0.0943  328 ASP A N   
2364 C CA  . ASP A 316 ? 0.4278 0.4508 0.4698 -0.0332 0.0326  0.0994  328 ASP A CA  
2365 C C   . ASP A 316 ? 0.4592 0.4804 0.4985 -0.0333 0.0315  0.1050  328 ASP A C   
2366 O O   . ASP A 316 ? 0.4523 0.4822 0.4898 -0.0342 0.0328  0.1096  328 ASP A O   
2367 C CB  . ASP A 316 ? 0.4223 0.4429 0.4677 -0.0378 0.0315  0.0994  328 ASP A CB  
2368 C CG  . ASP A 316 ? 0.4381 0.4657 0.4861 -0.0381 0.0331  0.0964  328 ASP A CG  
2369 O OD1 . ASP A 316 ? 0.4186 0.4520 0.4659 -0.0347 0.0349  0.0937  328 ASP A OD1 
2370 O OD2 . ASP A 316 ? 0.4533 0.4807 0.5043 -0.0419 0.0322  0.0969  328 ASP A OD2 
2371 N N   . GLU A 317 ? 0.4250 0.4355 0.4643 -0.0326 0.0290  0.1047  329 GLU A N   
2372 C CA  . GLU A 317 ? 0.4756 0.4823 0.5130 -0.0330 0.0269  0.1101  329 GLU A CA  
2373 C C   . GLU A 317 ? 0.4409 0.4503 0.4748 -0.0287 0.0271  0.1116  329 GLU A C   
2374 O O   . GLU A 317 ? 0.4338 0.4367 0.4671 -0.0280 0.0245  0.1146  329 GLU A O   
2375 C CB  . GLU A 317 ? 0.4804 0.4733 0.5207 -0.0347 0.0236  0.1093  329 GLU A CB  
2376 C CG  . GLU A 317 ? 0.5470 0.5366 0.5897 -0.0391 0.0230  0.1083  329 GLU A CG  
2377 C CD  . GLU A 317 ? 0.6090 0.5876 0.6525 -0.0418 0.0196  0.1111  329 GLU A CD  
2378 O OE1 . GLU A 317 ? 0.5494 0.5168 0.5943 -0.0407 0.0175  0.1080  329 GLU A OE1 
2379 O OE2 . GLU A 317 ? 0.6227 0.6042 0.6656 -0.0450 0.0190  0.1166  329 GLU A OE2 
2380 N N   . GLY A 318 ? 0.4058 0.4245 0.4372 -0.0257 0.0299  0.1096  330 GLY A N   
2381 C CA  . GLY A 318 ? 0.4649 0.4879 0.4913 -0.0218 0.0302  0.1116  330 GLY A CA  
2382 C C   . GLY A 318 ? 0.4806 0.4969 0.5079 -0.0182 0.0287  0.1088  330 GLY A C   
2383 O O   . GLY A 318 ? 0.4743 0.4940 0.4972 -0.0148 0.0286  0.1102  330 GLY A O   
2384 N N   . GLU A 319 ? 0.3660 0.3731 0.3985 -0.0189 0.0276  0.1047  331 GLU A N   
2385 C CA  . GLU A 319 ? 0.4002 0.4004 0.4349 -0.0159 0.0262  0.1020  331 GLU A CA  
2386 C C   . GLU A 319 ? 0.3700 0.3733 0.4050 -0.0141 0.0285  0.0965  331 GLU A C   
2387 O O   . GLU A 319 ? 0.2782 0.2862 0.3131 -0.0156 0.0306  0.0939  331 GLU A O   
2388 C CB  . GLU A 319 ? 0.3964 0.3845 0.4365 -0.0176 0.0238  0.1005  331 GLU A CB  
2389 C CG  . GLU A 319 ? 0.4563 0.4401 0.4962 -0.0196 0.0210  0.1060  331 GLU A CG  
2390 C CD  . GLU A 319 ? 0.4646 0.4363 0.5091 -0.0214 0.0187  0.1041  331 GLU A CD  
2391 O OE1 . GLU A 319 ? 0.4633 0.4305 0.5108 -0.0215 0.0195  0.0984  331 GLU A OE1 
2392 O OE2 . GLU A 319 ? 0.5192 0.4858 0.5637 -0.0229 0.0160  0.1084  331 GLU A OE2 
2393 N N   . VAL A 320 ? 0.3260 0.3266 0.3610 -0.0105 0.0274  0.0930  332 VAL A N   
2394 C CA  . VAL A 320 ? 0.3119 0.3126 0.3473 -0.0089 0.0280  0.0848  332 VAL A CA  
2395 C C   . VAL A 320 ? 0.3025 0.2935 0.3433 -0.0090 0.0266  0.0810  332 VAL A C   
2396 O O   . VAL A 320 ? 0.2390 0.2262 0.2816 -0.0067 0.0244  0.0818  332 VAL A O   
2397 C CB  . VAL A 320 ? 0.2972 0.3043 0.3272 -0.0047 0.0273  0.0816  332 VAL A CB  
2398 C CG1 . VAL A 320 ? 0.2375 0.2427 0.2683 -0.0036 0.0272  0.0735  332 VAL A CG1 
2399 C CG2 . VAL A 320 ? 0.2615 0.2785 0.2857 -0.0043 0.0293  0.0841  332 VAL A CG2 
2400 N N   . ILE A 321 ? 0.2569 0.2442 0.3003 -0.0114 0.0278  0.0768  333 ILE A N   
2401 C CA  . ILE A 321 ? 0.2897 0.2679 0.3378 -0.0120 0.0273  0.0729  333 ILE A CA  
2402 C C   . ILE A 321 ? 0.2762 0.2556 0.3236 -0.0102 0.0275  0.0656  333 ILE A C   
2403 O O   . ILE A 321 ? 0.3059 0.2880 0.3511 -0.0116 0.0287  0.0623  333 ILE A O   
2404 C CB  . ILE A 321 ? 0.2776 0.2502 0.3282 -0.0166 0.0282  0.0733  333 ILE A CB  
2405 C CG1 . ILE A 321 ? 0.3113 0.2838 0.3610 -0.0187 0.0268  0.0788  333 ILE A CG1 
2406 C CG2 . ILE A 321 ? 0.2999 0.2631 0.3542 -0.0170 0.0279  0.0683  333 ILE A CG2 
2407 C CD1 . ILE A 321 ? 0.3188 0.2863 0.3706 -0.0170 0.0246  0.0830  333 ILE A CD1 
2408 N N   . VAL A 322 ? 0.2359 0.2132 0.2857 -0.0073 0.0262  0.0633  334 VAL A N   
2409 C CA  . VAL A 322 ? 0.2536 0.2322 0.3035 -0.0060 0.0263  0.0569  334 VAL A CA  
2410 C C   . VAL A 322 ? 0.2847 0.2562 0.3394 -0.0072 0.0272  0.0528  334 VAL A C   
2411 O O   . VAL A 322 ? 0.3076 0.2737 0.3665 -0.0064 0.0266  0.0546  334 VAL A O   
2412 C CB  . VAL A 322 ? 0.2401 0.2231 0.2895 -0.0020 0.0241  0.0571  334 VAL A CB  
2413 C CG1 . VAL A 322 ? 0.2354 0.2184 0.2874 -0.0011 0.0239  0.0510  334 VAL A CG1 
2414 C CG2 . VAL A 322 ? 0.2492 0.2393 0.2920 -0.0009 0.0236  0.0589  334 VAL A CG2 
2415 N N   . PHE A 323 ? 0.2471 0.2182 0.3007 -0.0092 0.0285  0.0474  335 PHE A N   
2416 C CA  . PHE A 323 ? 0.2525 0.2177 0.3093 -0.0105 0.0299  0.0428  335 PHE A CA  
2417 C C   . PHE A 323 ? 0.2698 0.2381 0.3261 -0.0105 0.0305  0.0371  335 PHE A C   
2418 O O   . PHE A 323 ? 0.2501 0.2231 0.3023 -0.0110 0.0298  0.0363  335 PHE A O   
2419 C CB  . PHE A 323 ? 0.2403 0.2001 0.2958 -0.0148 0.0312  0.0424  335 PHE A CB  
2420 C CG  . PHE A 323 ? 0.2727 0.2265 0.3300 -0.0164 0.0328  0.0370  335 PHE A CG  
2421 C CD1 . PHE A 323 ? 0.2689 0.2164 0.3306 -0.0150 0.0330  0.0365  335 PHE A CD1 
2422 C CD2 . PHE A 323 ? 0.2323 0.1866 0.2863 -0.0193 0.0339  0.0322  335 PHE A CD2 
2423 C CE1 . PHE A 323 ? 0.2970 0.2394 0.3598 -0.0160 0.0349  0.0308  335 PHE A CE1 
2424 C CE2 . PHE A 323 ? 0.3031 0.2524 0.3578 -0.0209 0.0357  0.0272  335 PHE A CE2 
2425 C CZ  . PHE A 323 ? 0.3028 0.2465 0.3618 -0.0192 0.0365  0.0263  335 PHE A CZ  
2426 N N   . GLY A 324 ? 0.2588 0.2246 0.3194 -0.0098 0.0317  0.0332  336 GLY A N   
2427 C CA  . GLY A 324 ? 0.2836 0.2521 0.3439 -0.0109 0.0327  0.0280  336 GLY A CA  
2428 C C   . GLY A 324 ? 0.2307 0.2064 0.2913 -0.0085 0.0308  0.0281  336 GLY A C   
2429 O O   . GLY A 324 ? 0.2119 0.1902 0.2741 -0.0051 0.0288  0.0317  336 GLY A O   
2430 N N   . GLY A 325 ? 0.2154 0.1939 0.2739 -0.0106 0.0311  0.0244  337 GLY A N   
2431 C CA  . GLY A 325 ? 0.2169 0.2016 0.2755 -0.0090 0.0288  0.0240  337 GLY A CA  
2432 C C   . GLY A 325 ? 0.2106 0.1984 0.2763 -0.0073 0.0295  0.0217  337 GLY A C   
2433 O O   . GLY A 325 ? 0.2333 0.2185 0.3038 -0.0067 0.0319  0.0200  337 GLY A O   
2434 N N   . CYS A 326 ? 0.1793 0.1730 0.2458 -0.0063 0.0272  0.0214  338 CYS A N   
2435 C CA  . CYS A 326 ? 0.2005 0.1993 0.2744 -0.0051 0.0275  0.0191  338 CYS A CA  
2436 C C   . CYS A 326 ? 0.2503 0.2531 0.3280 -0.0007 0.0240  0.0223  338 CYS A C   
2437 O O   . CYS A 326 ? 0.1964 0.2001 0.2690 0.0002  0.0208  0.0251  338 CYS A O   
2438 C CB  . CYS A 326 ? 0.2047 0.2072 0.2767 -0.0089 0.0274  0.0158  338 CYS A CB  
2439 S SG  . CYS A 326 ? 0.1908 0.2007 0.2725 -0.0088 0.0292  0.0125  338 CYS A SG  
2440 N N   . ALA A 327 ? 0.1700 0.1754 0.2568 0.0023  0.0246  0.0218  339 ALA A N   
2441 C CA  . ALA A 327 ? 0.1921 0.2008 0.2834 0.0067  0.0209  0.0252  339 ALA A CA  
2442 C C   . ALA A 327 ? 0.2043 0.2209 0.2986 0.0066  0.0181  0.0241  339 ALA A C   
2443 O O   . ALA A 327 ? 0.2339 0.2535 0.3305 0.0098  0.0142  0.0271  339 ALA A O   
2444 C CB  . ALA A 327 ? 0.2095 0.2165 0.3098 0.0106  0.0220  0.0255  339 ALA A CB  
2445 N N   . ASN A 328 ? 0.1723 0.1920 0.2661 0.0027  0.0197  0.0204  340 ASN A N   
2446 C CA  . ASN A 328 ? 0.1842 0.2112 0.2805 0.0016  0.0167  0.0196  340 ASN A CA  
2447 C C   . ASN A 328 ? 0.1890 0.2150 0.2772 -0.0037 0.0164  0.0177  340 ASN A C   
2448 O O   . ASN A 328 ? 0.1778 0.1977 0.2578 -0.0054 0.0173  0.0178  340 ASN A O   
2449 C CB  . ASN A 328 ? 0.1548 0.1891 0.2631 0.0025  0.0188  0.0171  340 ASN A CB  
2450 C CG  . ASN A 328 ? 0.1948 0.2285 0.3042 -0.0007 0.0245  0.0128  340 ASN A CG  
2451 O OD1 . ASN A 328 ? 0.2077 0.2353 0.3089 -0.0041 0.0265  0.0118  340 ASN A OD1 
2452 N ND2 . ASN A 328 ? 0.1961 0.2364 0.3158 0.0005  0.0273  0.0101  340 ASN A ND2 
2453 N N   . ASN A 329 ? 0.1700 0.2020 0.2608 -0.0062 0.0145  0.0163  341 ASN A N   
2454 C CA  . ASN A 329 ? 0.1883 0.2191 0.2720 -0.0115 0.0132  0.0147  341 ASN A CA  
2455 C C   . ASN A 329 ? 0.1837 0.2125 0.2665 -0.0156 0.0183  0.0117  341 ASN A C   
2456 O O   . ASN A 329 ? 0.1456 0.1800 0.2348 -0.0177 0.0211  0.0095  341 ASN A O   
2457 C CB  . ASN A 329 ? 0.1634 0.2013 0.2510 -0.0135 0.0094  0.0144  341 ASN A CB  
2458 C CG  . ASN A 329 ? 0.1571 0.1926 0.2371 -0.0190 0.0070  0.0132  341 ASN A CG  
2459 O OD1 . ASN A 329 ? 0.1785 0.2077 0.2511 -0.0216 0.0087  0.0122  341 ASN A OD1 
2460 N ND2 . ASN A 329 ? 0.1686 0.2086 0.2504 -0.0210 0.0025  0.0135  341 ASN A ND2 
2461 N N   . LEU A 330 ? 0.1416 0.1628 0.2162 -0.0169 0.0195  0.0117  342 LEU A N   
2462 C CA  . LEU A 330 ? 0.1662 0.1846 0.2387 -0.0209 0.0239  0.0090  342 LEU A CA  
2463 C C   . LEU A 330 ? 0.1481 0.1689 0.2183 -0.0270 0.0233  0.0072  342 LEU A C   
2464 O O   . LEU A 330 ? 0.1946 0.2150 0.2641 -0.0309 0.0271  0.0048  342 LEU A O   
2465 C CB  . LEU A 330 ? 0.1989 0.2089 0.2634 -0.0210 0.0244  0.0099  342 LEU A CB  
2466 C CG  . LEU A 330 ? 0.2448 0.2512 0.3010 -0.0215 0.0200  0.0115  342 LEU A CG  
2467 C CD1 . LEU A 330 ? 0.2680 0.2722 0.3184 -0.0272 0.0189  0.0096  342 LEU A CD1 
2468 C CD2 . LEU A 330 ? 0.1914 0.1924 0.2434 -0.0190 0.0206  0.0135  342 LEU A CD2 
2469 N N   . LEU A 331 ? 0.1710 0.1939 0.2394 -0.0281 0.0183  0.0082  343 LEU A N   
2470 C CA  . LEU A 331 ? 0.1727 0.1972 0.2388 -0.0344 0.0168  0.0071  343 LEU A CA  
2471 C C   . LEU A 331 ? 0.1811 0.2150 0.2564 -0.0366 0.0201  0.0056  343 LEU A C   
2472 O O   . LEU A 331 ? 0.1915 0.2273 0.2652 -0.0427 0.0206  0.0046  343 LEU A O   
2473 C CB  . LEU A 331 ? 0.1854 0.2091 0.2476 -0.0347 0.0100  0.0085  343 LEU A CB  
2474 C CG  . LEU A 331 ? 0.1775 0.1932 0.2308 -0.0319 0.0067  0.0096  343 LEU A CG  
2475 C CD1 . LEU A 331 ? 0.2268 0.2422 0.2768 -0.0310 0.0001  0.0105  343 LEU A CD1 
2476 C CD2 . LEU A 331 ? 0.2237 0.2326 0.2695 -0.0360 0.0075  0.0085  343 LEU A CD2 
2477 N N   . VAL A 332 ? 0.1732 0.2130 0.2580 -0.0319 0.0222  0.0056  344 VAL A N   
2478 C CA  . VAL A 332 ? 0.1816 0.2308 0.2762 -0.0330 0.0266  0.0035  344 VAL A CA  
2479 C C   . VAL A 332 ? 0.1777 0.2235 0.2719 -0.0319 0.0329  0.0010  344 VAL A C   
2480 O O   . VAL A 332 ? 0.1608 0.2068 0.2609 -0.0264 0.0353  0.0005  344 VAL A O   
2481 C CB  . VAL A 332 ? 0.1953 0.2530 0.3012 -0.0281 0.0250  0.0046  344 VAL A CB  
2482 C CG1 . VAL A 332 ? 0.1943 0.2631 0.3111 -0.0293 0.0298  0.0021  344 VAL A CG1 
2483 C CG2 . VAL A 332 ? 0.2053 0.2648 0.3099 -0.0292 0.0179  0.0071  344 VAL A CG2 
2484 N N   . HIS A 333 ? 0.1763 0.2182 0.2631 -0.0376 0.0353  -0.0006 345 HIS A N   
2485 C CA  . HIS A 333 ? 0.2385 0.2737 0.3213 -0.0370 0.0398  -0.0026 345 HIS A CA  
2486 C C   . HIS A 333 ? 0.2484 0.2893 0.3402 -0.0340 0.0457  -0.0058 345 HIS A C   
2487 O O   . HIS A 333 ? 0.2498 0.2853 0.3418 -0.0301 0.0481  -0.0068 345 HIS A O   
2488 C CB  . HIS A 333 ? 0.2593 0.2895 0.3319 -0.0441 0.0404  -0.0034 345 HIS A CB  
2489 C CG  . HIS A 333 ? 0.2494 0.2723 0.3169 -0.0444 0.0443  -0.0054 345 HIS A CG  
2490 N ND1 . HIS A 333 ? 0.2038 0.2179 0.2667 -0.0415 0.0427  -0.0040 345 HIS A ND1 
2491 C CD2 . HIS A 333 ? 0.2796 0.3031 0.3457 -0.0475 0.0497  -0.0088 345 HIS A CD2 
2492 C CE1 . HIS A 333 ? 0.3226 0.3316 0.3817 -0.0430 0.0465  -0.0063 345 HIS A CE1 
2493 N NE2 . HIS A 333 ? 0.3300 0.3442 0.3905 -0.0465 0.0508  -0.0094 345 HIS A NE2 
2494 N N   . HIS A 334 ? 0.1933 0.2453 0.2930 -0.0354 0.0479  -0.0073 346 HIS A N   
2495 C CA  . HIS A 334 ? 0.2003 0.2584 0.3089 -0.0321 0.0539  -0.0110 346 HIS A CA  
2496 C C   . HIS A 334 ? 0.2363 0.2958 0.3548 -0.0238 0.0527  -0.0103 346 HIS A C   
2497 O O   . HIS A 334 ? 0.2921 0.3536 0.4174 -0.0197 0.0572  -0.0136 346 HIS A O   
2498 C CB  . HIS A 334 ? 0.2449 0.3161 0.3599 -0.0363 0.0571  -0.0129 346 HIS A CB  
2499 C CG  . HIS A 334 ? 0.1868 0.2674 0.3101 -0.0360 0.0528  -0.0102 346 HIS A CG  
2500 N ND1 . HIS A 334 ? 0.2515 0.3306 0.3692 -0.0407 0.0469  -0.0067 346 HIS A ND1 
2501 C CD2 . HIS A 334 ? 0.2051 0.2969 0.3421 -0.0317 0.0532  -0.0105 346 HIS A CD2 
2502 C CE1 . HIS A 334 ? 0.2075 0.2961 0.3346 -0.0396 0.0437  -0.0050 346 HIS A CE1 
2503 N NE2 . HIS A 334 ? 0.1992 0.2961 0.3384 -0.0342 0.0475  -0.0071 346 HIS A NE2 
2504 N N   . ARG A 335 ? 0.1981 0.2561 0.3173 -0.0210 0.0466  -0.0062 347 ARG A N   
2505 C CA  . ARG A 335 ? 0.2247 0.2824 0.3517 -0.0134 0.0447  -0.0047 347 ARG A CA  
2506 C C   . ARG A 335 ? 0.2276 0.2735 0.3470 -0.0107 0.0419  -0.0019 347 ARG A C   
2507 O O   . ARG A 335 ? 0.1979 0.2423 0.3223 -0.0049 0.0398  0.0002  347 ARG A O   
2508 C CB  . ARG A 335 ? 0.1865 0.2531 0.3212 -0.0119 0.0398  -0.0019 347 ARG A CB  
2509 C CG  . ARG A 335 ? 0.2166 0.2962 0.3589 -0.0157 0.0418  -0.0038 347 ARG A CG  
2510 C CD  . ARG A 335 ? 0.2453 0.3353 0.4000 -0.0121 0.0380  -0.0019 347 ARG A CD  
2511 N NE  . ARG A 335 ? 0.2459 0.3326 0.3959 -0.0122 0.0305  0.0024  347 ARG A NE  
2512 C CZ  . ARG A 335 ? 0.2411 0.3322 0.3894 -0.0171 0.0264  0.0041  347 ARG A CZ  
2513 N NH1 . ARG A 335 ? 0.2130 0.3123 0.3641 -0.0230 0.0289  0.0024  347 ARG A NH1 
2514 N NH2 . ARG A 335 ? 0.2266 0.3134 0.3697 -0.0163 0.0195  0.0075  347 ARG A NH2 
2515 N N   . ALA A 336 ? 0.2152 0.2530 0.3231 -0.0149 0.0417  -0.0015 348 ALA A N   
2516 C CA  . ALA A 336 ? 0.2296 0.2580 0.3305 -0.0130 0.0387  0.0018  348 ALA A CA  
2517 C C   . ALA A 336 ? 0.2234 0.2461 0.3272 -0.0084 0.0408  0.0015  348 ALA A C   
2518 O O   . ALA A 336 ? 0.2652 0.2866 0.3710 -0.0085 0.0454  -0.0022 348 ALA A O   
2519 C CB  . ALA A 336 ? 0.2266 0.2484 0.3158 -0.0185 0.0383  0.0018  348 ALA A CB  
2520 N N   . ALA A 337 ? 0.2157 0.2346 0.3194 -0.0043 0.0372  0.0055  349 ALA A N   
2521 C CA  . ALA A 337 ? 0.2153 0.2279 0.3218 0.0001  0.0380  0.0064  349 ALA A CA  
2522 C C   . ALA A 337 ? 0.2216 0.2252 0.3183 -0.0018 0.0369  0.0091  349 ALA A C   
2523 O O   . ALA A 337 ? 0.2411 0.2428 0.3351 0.0000  0.0333  0.0136  349 ALA A O   
2524 C CB  . ALA A 337 ? 0.2195 0.2352 0.3338 0.0058  0.0345  0.0096  349 ALA A CB  
2525 N N   . HIS A 338 ? 0.2088 0.2073 0.3002 -0.0056 0.0401  0.0064  350 HIS A N   
2526 C CA  . HIS A 338 ? 0.2667 0.2572 0.3501 -0.0075 0.0394  0.0087  350 HIS A CA  
2527 C C   . HIS A 338 ? 0.2801 0.2638 0.3665 -0.0041 0.0397  0.0102  350 HIS A C   
2528 O O   . HIS A 338 ? 0.2641 0.2472 0.3571 -0.0015 0.0419  0.0073  350 HIS A O   
2529 C CB  . HIS A 338 ? 0.2487 0.2362 0.3252 -0.0131 0.0419  0.0055  350 HIS A CB  
2530 C CG  . HIS A 338 ? 0.2415 0.2344 0.3147 -0.0170 0.0411  0.0044  350 HIS A CG  
2531 N ND1 . HIS A 338 ? 0.2230 0.2156 0.2900 -0.0188 0.0376  0.0070  350 HIS A ND1 
2532 C CD2 . HIS A 338 ? 0.2646 0.2633 0.3399 -0.0196 0.0432  0.0010  350 HIS A CD2 
2533 C CE1 . HIS A 338 ? 0.2225 0.2193 0.2877 -0.0223 0.0370  0.0054  350 HIS A CE1 
2534 N NE2 . HIS A 338 ? 0.2371 0.2380 0.3073 -0.0232 0.0404  0.0020  350 HIS A NE2 
2535 N N   . SER A 339 ? 0.2423 0.2213 0.3242 -0.0042 0.0374  0.0146  351 SER A N   
2536 C CA  . SER A 339 ? 0.2445 0.2174 0.3290 -0.0012 0.0364  0.0178  351 SER A CA  
2537 C C   . SER A 339 ? 0.2419 0.2065 0.3208 -0.0045 0.0375  0.0183  351 SER A C   
2538 O O   . SER A 339 ? 0.2160 0.1804 0.2883 -0.0086 0.0377  0.0183  351 SER A O   
2539 C CB  . SER A 339 ? 0.2324 0.2076 0.3164 0.0015  0.0324  0.0239  351 SER A CB  
2540 O OG  . SER A 339 ? 0.2511 0.2203 0.3377 0.0039  0.0311  0.0276  351 SER A OG  
2541 N N   . ASN A 340 ? 0.2757 0.2332 0.3579 -0.0027 0.0376  0.0188  352 ASN A N   
2542 C CA  . ASN A 340 ? 0.3068 0.2560 0.3844 -0.0057 0.0375  0.0208  352 ASN A CA  
2543 C C   . ASN A 340 ? 0.3275 0.2736 0.4065 -0.0037 0.0344  0.0275  352 ASN A C   
2544 O O   . ASN A 340 ? 0.3442 0.2828 0.4215 -0.0057 0.0339  0.0296  352 ASN A O   
2545 C CB  . ASN A 340 ? 0.3420 0.2839 0.4207 -0.0065 0.0400  0.0157  352 ASN A CB  
2546 C CG  . ASN A 340 ? 0.3554 0.2928 0.4416 -0.0015 0.0395  0.0151  352 ASN A CG  
2547 O OD1 . ASN A 340 ? 0.3595 0.3006 0.4512 0.0028  0.0374  0.0179  352 ASN A OD1 
2548 N ND2 . ASN A 340 ? 0.4571 0.3861 0.5435 -0.0019 0.0411  0.0111  352 ASN A ND2 
2549 N N   . GLU A 341 ? 0.3145 0.2660 0.3962 -0.0002 0.0320  0.0310  353 GLU A N   
2550 C CA  . GLU A 341 ? 0.3038 0.2525 0.3866 0.0017  0.0290  0.0377  353 GLU A CA  
2551 C C   . GLU A 341 ? 0.3016 0.2515 0.3777 -0.0016 0.0281  0.0428  353 GLU A C   
2552 O O   . GLU A 341 ? 0.2911 0.2466 0.3624 -0.0037 0.0290  0.0418  353 GLU A O   
2553 C CB  . GLU A 341 ? 0.2998 0.2542 0.3869 0.0063  0.0264  0.0399  353 GLU A CB  
2554 C CG  . GLU A 341 ? 0.3281 0.2831 0.4237 0.0104  0.0269  0.0355  353 GLU A CG  
2555 C CD  . GLU A 341 ? 0.3636 0.3215 0.4643 0.0151  0.0231  0.0397  353 GLU A CD  
2556 O OE1 . GLU A 341 ? 0.4022 0.3547 0.5026 0.0160  0.0202  0.0454  353 GLU A OE1 
2557 O OE2 . GLU A 341 ? 0.4068 0.3723 0.5115 0.0175  0.0226  0.0375  353 GLU A OE2 
2558 N N   . ILE A 342 ? 0.3418 0.2866 0.4180 -0.0020 0.0263  0.0485  354 ILE A N   
2559 C CA  . ILE A 342 ? 0.3012 0.2487 0.3724 -0.0043 0.0253  0.0548  354 ILE A CA  
2560 C C   . ILE A 342 ? 0.3437 0.2949 0.4156 -0.0009 0.0224  0.0602  354 ILE A C   
2561 O O   . ILE A 342 ? 0.3345 0.2805 0.4108 0.0015  0.0202  0.0629  354 ILE A O   
2562 C CB  . ILE A 342 ? 0.3273 0.2671 0.3979 -0.0079 0.0250  0.0581  354 ILE A CB  
2563 C CG1 . ILE A 342 ? 0.3096 0.2469 0.3778 -0.0120 0.0274  0.0533  354 ILE A CG1 
2564 C CG2 . ILE A 342 ? 0.3700 0.3134 0.4372 -0.0097 0.0237  0.0659  354 ILE A CG2 
2565 C CD1 . ILE A 342 ? 0.3306 0.2761 0.3937 -0.0141 0.0287  0.0529  354 ILE A CD1 
2566 N N   . LEU A 343 ? 0.3001 0.2597 0.3674 -0.0006 0.0222  0.0618  355 LEU A N   
2567 C CA  . LEU A 343 ? 0.2943 0.2580 0.3600 0.0019  0.0195  0.0674  355 LEU A CA  
2568 C C   . LEU A 343 ? 0.3007 0.2668 0.3607 -0.0010 0.0199  0.0734  355 LEU A C   
2569 O O   . LEU A 343 ? 0.2865 0.2572 0.3422 -0.0032 0.0219  0.0719  355 LEU A O   
2570 C CB  . LEU A 343 ? 0.3000 0.2716 0.3640 0.0045  0.0188  0.0645  355 LEU A CB  
2571 C CG  . LEU A 343 ? 0.3169 0.2891 0.3868 0.0074  0.0183  0.0591  355 LEU A CG  
2572 C CD1 . LEU A 343 ? 0.3305 0.2997 0.4032 0.0055  0.0215  0.0525  355 LEU A CD1 
2573 C CD2 . LEU A 343 ? 0.3001 0.2803 0.3671 0.0091  0.0169  0.0578  355 LEU A CD2 
2574 N N   . ILE A 344 ? 0.3427 0.3058 0.4030 -0.0012 0.0178  0.0804  356 ILE A N   
2575 C CA  . ILE A 344 ? 0.3025 0.2687 0.3579 -0.0043 0.0183  0.0869  356 ILE A CA  
2576 C C   . ILE A 344 ? 0.3145 0.2875 0.3650 -0.0021 0.0166  0.0916  356 ILE A C   
2577 O O   . ILE A 344 ? 0.3533 0.3235 0.4055 0.0001  0.0133  0.0954  356 ILE A O   
2578 C CB  . ILE A 344 ? 0.3204 0.2780 0.3786 -0.0074 0.0172  0.0921  356 ILE A CB  
2579 C CG1 . ILE A 344 ? 0.2896 0.2396 0.3519 -0.0095 0.0186  0.0869  356 ILE A CG1 
2580 C CG2 . ILE A 344 ? 0.3433 0.3066 0.3960 -0.0111 0.0178  0.0972  356 ILE A CG2 
2581 C CD1 . ILE A 344 ? 0.3028 0.2450 0.3655 -0.0123 0.0163  0.0884  356 ILE A CD1 
2582 N N   . PHE A 345 ? 0.2931 0.2750 0.3374 -0.0026 0.0185  0.0914  357 PHE A N   
2583 C CA  . PHE A 345 ? 0.3109 0.3000 0.3489 -0.0008 0.0173  0.0956  357 PHE A CA  
2584 C C   . PHE A 345 ? 0.3712 0.3636 0.4054 -0.0043 0.0187  0.1030  357 PHE A C   
2585 O O   . PHE A 345 ? 0.3725 0.3680 0.4061 -0.0071 0.0217  0.1024  357 PHE A O   
2586 C CB  . PHE A 345 ? 0.2859 0.2827 0.3191 0.0014  0.0185  0.0900  357 PHE A CB  
2587 C CG  . PHE A 345 ? 0.3383 0.3331 0.3749 0.0043  0.0168  0.0836  357 PHE A CG  
2588 C CD1 . PHE A 345 ? 0.2873 0.2789 0.3282 0.0033  0.0185  0.0773  357 PHE A CD1 
2589 C CD2 . PHE A 345 ? 0.3299 0.3263 0.3655 0.0076  0.0135  0.0843  357 PHE A CD2 
2590 C CE1 . PHE A 345 ? 0.2807 0.2714 0.3250 0.0054  0.0173  0.0717  357 PHE A CE1 
2591 C CE2 . PHE A 345 ? 0.2880 0.2836 0.3277 0.0099  0.0120  0.0786  357 PHE A CE2 
2592 C CZ  . PHE A 345 ? 0.2696 0.2627 0.3138 0.0087  0.0141  0.0724  357 PHE A CZ  
2593 N N   . SER A 346 ? 0.3899 0.3821 0.4216 -0.0042 0.0162  0.1103  358 SER A N   
2594 C CA  . SER A 346 ? 0.4223 0.4182 0.4499 -0.0078 0.0171  0.1163  358 SER A CA  
2595 C C   . SER A 346 ? 0.4623 0.4693 0.4810 -0.0063 0.0185  0.1186  358 SER A C   
2596 O O   . SER A 346 ? 0.4931 0.5016 0.5071 -0.0049 0.0159  0.1228  358 SER A O   
2597 C CB  . SER A 346 ? 0.4859 0.4742 0.5153 -0.0091 0.0131  0.1209  358 SER A CB  
2598 O OG  . SER A 346 ? 0.4368 0.4143 0.4741 -0.0087 0.0113  0.1179  358 SER A OG  
2599 N N   . VAL A 347 ? 0.4980 0.5129 0.5143 -0.0065 0.0225  0.1154  359 VAL A N   
2600 C CA  . VAL A 347 ? 0.5430 0.5685 0.5505 -0.0042 0.0241  0.1152  359 VAL A CA  
2601 C C   . VAL A 347 ? 0.6045 0.6376 0.6073 -0.0071 0.0261  0.1196  359 VAL A C   
2602 O O   . VAL A 347 ? 0.6726 0.7142 0.6672 -0.0053 0.0271  0.1210  359 VAL A O   
2603 C CB  . VAL A 347 ? 0.5569 0.5866 0.5639 -0.0020 0.0264  0.1064  359 VAL A CB  
2604 C CG1 . VAL A 347 ? 0.4421 0.4800 0.4401 0.0019  0.0264  0.1039  359 VAL A CG1 
2605 C CG2 . VAL A 347 ? 0.4032 0.4245 0.4168 -0.0007 0.0244  0.0996  359 VAL A CG2 
2606 N N   . GLN A 348 ? 0.5762 0.6066 0.5838 -0.0115 0.0264  0.1210  360 GLN A N   
2607 C CA  . GLN A 348 ? 0.5973 0.6349 0.6014 -0.0146 0.0281  0.1249  360 GLN A CA  
2608 C C   . GLN A 348 ? 0.6011 0.6311 0.6075 -0.0184 0.0250  0.1301  360 GLN A C   
2609 O O   . GLN A 348 ? 0.6293 0.6573 0.6316 -0.0181 0.0222  0.1346  360 GLN A O   
2610 C CB  . GLN A 348 ? 0.5935 0.6375 0.6006 -0.0164 0.0320  0.1216  360 GLN A CB  
2611 C CG  . GLN A 348 ? 0.5761 0.6289 0.5801 -0.0126 0.0352  0.1169  360 GLN A CG  
2612 C CD  . GLN A 348 ? 0.6653 0.7301 0.6608 -0.0107 0.0377  0.1186  360 GLN A CD  
2613 O OE1 . GLN A 348 ? 0.6625 0.7321 0.6563 -0.0136 0.0386  0.1227  360 GLN A OE1 
2614 N NE2 . GLN A 348 ? 0.6056 0.6751 0.5953 -0.0059 0.0387  0.1152  360 GLN A NE2 
2615 N N   . LEU B 14  ? 0.7202 0.5154 0.5544 -0.0117 -0.0567 -0.0573 26  LEU B N   
2616 C CA  . LEU B 14  ? 0.8337 0.6270 0.6657 -0.0064 -0.0546 -0.0586 26  LEU B CA  
2617 C C   . LEU B 14  ? 0.8546 0.6643 0.7007 -0.0060 -0.0546 -0.0558 26  LEU B C   
2618 O O   . LEU B 14  ? 0.8289 0.6494 0.6843 -0.0108 -0.0567 -0.0530 26  LEU B O   
2619 C CB  . LEU B 14  ? 0.8641 0.6562 0.7002 0.0022  -0.0501 -0.0595 26  LEU B CB  
2620 C CG  . LEU B 14  ? 0.8894 0.6715 0.7152 0.0035  -0.0474 -0.0598 26  LEU B CG  
2621 C CD1 . LEU B 14  ? 0.9420 0.7245 0.7736 0.0110  -0.0436 -0.0599 26  LEU B CD1 
2622 C CD2 . LEU B 14  ? 0.9664 0.7416 0.7811 0.0029  -0.0467 -0.0605 26  LEU B CD2 
2623 N N   . ALA B 15  ? 0.9076 0.7193 0.7557 -0.0003 -0.0519 -0.0562 27  ALA B N   
2624 C CA  . ALA B 15  ? 0.8126 0.6392 0.6731 0.0003  -0.0515 -0.0535 27  ALA B CA  
2625 C C   . ALA B 15  ? 0.7226 0.5638 0.6013 0.0017  -0.0509 -0.0513 27  ALA B C   
2626 O O   . ALA B 15  ? 0.6905 0.5314 0.5744 0.0067  -0.0487 -0.0525 27  ALA B O   
2627 C CB  . ALA B 15  ? 0.8066 0.6319 0.6662 0.0072  -0.0483 -0.0547 27  ALA B CB  
2628 N N   . CYS B 16  ? 0.6401 0.4939 0.5285 -0.0029 -0.0525 -0.0479 28  CYS B N   
2629 C CA  . CYS B 16  ? 0.6033 0.4703 0.5082 -0.0029 -0.0519 -0.0456 28  CYS B CA  
2630 C C   . CYS B 16  ? 0.5401 0.4221 0.4584 -0.0017 -0.0508 -0.0426 28  CYS B C   
2631 O O   . CYS B 16  ? 0.4871 0.3719 0.4027 -0.0056 -0.0527 -0.0406 28  CYS B O   
2632 C CB  . CYS B 16  ? 0.6081 0.4755 0.5123 -0.0107 -0.0551 -0.0439 28  CYS B CB  
2633 S SG  . CYS B 16  ? 0.6853 0.5622 0.6049 -0.0104 -0.0537 -0.0426 28  CYS B SG  
2634 N N   . PRO B 17  ? 0.4836 0.3754 0.4159 0.0036  -0.0478 -0.0420 29  PRO B N   
2635 C CA  . PRO B 17  ? 0.4475 0.3537 0.3931 0.0049  -0.0465 -0.0391 29  PRO B CA  
2636 C C   . PRO B 17  ? 0.4244 0.3411 0.3786 -0.0018 -0.0484 -0.0350 29  PRO B C   
2637 O O   . PRO B 17  ? 0.3976 0.3130 0.3518 -0.0062 -0.0499 -0.0343 29  PRO B O   
2638 C CB  . PRO B 17  ? 0.4347 0.3470 0.3920 0.0116  -0.0428 -0.0398 29  PRO B CB  
2639 C CG  . PRO B 17  ? 0.4448 0.3503 0.3992 0.0107  -0.0430 -0.0415 29  PRO B CG  
2640 C CD  . PRO B 17  ? 0.5109 0.4012 0.4477 0.0080  -0.0455 -0.0438 29  PRO B CD  
2641 N N   . ALA B 18  ? 0.3624 0.2896 0.3240 -0.0025 -0.0484 -0.0319 30  ALA B N   
2642 C CA  . ALA B 18  ? 0.3723 0.3111 0.3441 -0.0083 -0.0499 -0.0272 30  ALA B CA  
2643 C C   . ALA B 18  ? 0.3347 0.2839 0.3229 -0.0064 -0.0469 -0.0257 30  ALA B C   
2644 O O   . ALA B 18  ? 0.3737 0.3247 0.3678 -0.0001 -0.0435 -0.0276 30  ALA B O   
2645 C CB  . ALA B 18  ? 0.3691 0.3168 0.3451 -0.0092 -0.0505 -0.0241 30  ALA B CB  
2646 N N   . GLU B 19  ? 0.3373 0.2931 0.3325 -0.0121 -0.0481 -0.0222 31  GLU B N   
2647 C CA  . GLU B 19  ? 0.3050 0.2707 0.3158 -0.0111 -0.0450 -0.0204 31  GLU B CA  
2648 C C   . GLU B 19  ? 0.2615 0.2399 0.2864 -0.0066 -0.0416 -0.0184 31  GLU B C   
2649 O O   . GLU B 19  ? 0.3007 0.2833 0.3257 -0.0063 -0.0425 -0.0168 31  GLU B O   
2650 C CB  . GLU B 19  ? 0.3466 0.3173 0.3624 -0.0183 -0.0468 -0.0164 31  GLU B CB  
2651 C CG  . GLU B 19  ? 0.3798 0.3622 0.4036 -0.0223 -0.0481 -0.0109 31  GLU B CG  
2652 C CD  . GLU B 19  ? 0.4466 0.4228 0.4569 -0.0277 -0.0531 -0.0101 31  GLU B CD  
2653 O OE1 . GLU B 19  ? 0.4679 0.4302 0.4621 -0.0276 -0.0550 -0.0143 31  GLU B OE1 
2654 O OE2 . GLU B 19  ? 0.4589 0.4440 0.4746 -0.0322 -0.0549 -0.0052 31  GLU B OE2 
2655 N N   . ARG B 20  ? 0.2557 0.2398 0.2922 -0.0031 -0.0377 -0.0186 32  ARG B N   
2656 C CA  . ARG B 20  ? 0.2243 0.2199 0.2741 0.0014  -0.0341 -0.0169 32  ARG B CA  
2657 C C   . ARG B 20  ? 0.2132 0.2143 0.2751 0.0034  -0.0299 -0.0168 32  ARG B C   
2658 O O   . ARG B 20  ? 0.2428 0.2367 0.3006 0.0032  -0.0295 -0.0194 32  ARG B O   
2659 C CB  . ARG B 20  ? 0.2316 0.2230 0.2756 0.0078  -0.0333 -0.0201 32  ARG B CB  
2660 C CG  . ARG B 20  ? 0.2252 0.2069 0.2627 0.0122  -0.0320 -0.0247 32  ARG B CG  
2661 C CD  . ARG B 20  ? 0.2895 0.2641 0.3174 0.0173  -0.0323 -0.0277 32  ARG B CD  
2662 N NE  . ARG B 20  ? 0.2789 0.2434 0.2917 0.0139  -0.0361 -0.0287 32  ARG B NE  
2663 C CZ  . ARG B 20  ? 0.3012 0.2608 0.3054 0.0164  -0.0369 -0.0301 32  ARG B CZ  
2664 N NH1 . ARG B 20  ? 0.2394 0.2036 0.2488 0.0224  -0.0343 -0.0305 32  ARG B NH1 
2665 N NH2 . ARG B 20  ? 0.3502 0.2998 0.3401 0.0126  -0.0401 -0.0310 32  ARG B NH2 
2666 N N   . SER B 21  ? 0.2071 0.2208 0.2838 0.0052  -0.0266 -0.0138 33  SER B N   
2667 C CA  . SER B 21  ? 0.1816 0.2004 0.2695 0.0085  -0.0217 -0.0143 33  SER B CA  
2668 C C   . SER B 21  ? 0.1839 0.2092 0.2784 0.0146  -0.0190 -0.0145 33  SER B C   
2669 O O   . SER B 21  ? 0.1463 0.1743 0.2393 0.0155  -0.0206 -0.0134 33  SER B O   
2670 C CB  . SER B 21  ? 0.1538 0.1820 0.2551 0.0046  -0.0193 -0.0101 33  SER B CB  
2671 O OG  . SER B 21  ? 0.1698 0.1924 0.2654 -0.0010 -0.0218 -0.0097 33  SER B OG  
2672 N N   . GLY B 22  ? 0.1550 0.1827 0.2566 0.0184  -0.0148 -0.0159 34  GLY B N   
2673 C CA  . GLY B 22  ? 0.1226 0.1568 0.2314 0.0240  -0.0119 -0.0160 34  GLY B CA  
2674 C C   . GLY B 22  ? 0.1216 0.1493 0.2202 0.0287  -0.0137 -0.0192 34  GLY B C   
2675 O O   . GLY B 22  ? 0.1147 0.1483 0.2185 0.0331  -0.0120 -0.0188 34  GLY B O   
2676 N N   . HIS B 23  ? 0.1458 0.1612 0.2302 0.0281  -0.0168 -0.0223 35  HIS B N   
2677 C CA  . HIS B 23  ? 0.1461 0.1532 0.2197 0.0326  -0.0181 -0.0256 35  HIS B CA  
2678 C C   . HIS B 23  ? 0.1734 0.1790 0.2494 0.0378  -0.0151 -0.0281 35  HIS B C   
2679 O O   . HIS B 23  ? 0.1549 0.1648 0.2394 0.0374  -0.0123 -0.0276 35  HIS B O   
2680 C CB  . HIS B 23  ? 0.1838 0.1780 0.2420 0.0297  -0.0220 -0.0277 35  HIS B CB  
2681 C CG  . HIS B 23  ? 0.1672 0.1559 0.2232 0.0267  -0.0221 -0.0289 35  HIS B CG  
2682 N ND1 . HIS B 23  ? 0.2404 0.2340 0.3032 0.0214  -0.0218 -0.0264 35  HIS B ND1 
2683 C CD2 . HIS B 23  ? 0.2267 0.2052 0.2744 0.0280  -0.0225 -0.0321 35  HIS B CD2 
2684 C CE1 . HIS B 23  ? 0.2223 0.2090 0.2810 0.0197  -0.0219 -0.0282 35  HIS B CE1 
2685 N NE2 . HIS B 23  ? 0.2312 0.2088 0.2808 0.0236  -0.0225 -0.0316 35  HIS B NE2 
2686 N N   . VAL B 24  ? 0.1895 0.1886 0.2575 0.0426  -0.0157 -0.0307 36  VAL B N   
2687 C CA  . VAL B 24  ? 0.1597 0.1551 0.2272 0.0469  -0.0138 -0.0331 36  VAL B CA  
2688 C C   . VAL B 24  ? 0.1761 0.1579 0.2296 0.0467  -0.0164 -0.0359 36  VAL B C   
2689 O O   . VAL B 24  ? 0.1948 0.1693 0.2378 0.0452  -0.0193 -0.0365 36  VAL B O   
2690 C CB  . VAL B 24  ? 0.1557 0.1556 0.2276 0.0535  -0.0116 -0.0334 36  VAL B CB  
2691 C CG1 . VAL B 24  ? 0.1740 0.1874 0.2604 0.0538  -0.0086 -0.0306 36  VAL B CG1 
2692 C CG2 . VAL B 24  ? 0.1836 0.1782 0.2461 0.0561  -0.0137 -0.0343 36  VAL B CG2 
2693 N N   . ALA B 25  ? 0.1767 0.1548 0.2300 0.0479  -0.0152 -0.0374 37  ALA B N   
2694 C CA  . ALA B 25  ? 0.2353 0.2012 0.2768 0.0490  -0.0171 -0.0399 37  ALA B CA  
2695 C C   . ALA B 25  ? 0.2457 0.2118 0.2904 0.0536  -0.0149 -0.0409 37  ALA B C   
2696 O O   . ALA B 25  ? 0.2438 0.2158 0.2971 0.0526  -0.0127 -0.0402 37  ALA B O   
2697 C CB  . ALA B 25  ? 0.2227 0.1821 0.2585 0.0431  -0.0192 -0.0403 37  ALA B CB  
2698 N N   . VAL B 26  ? 0.2844 0.2448 0.3213 0.0573  -0.0149 -0.0413 38  VAL B N   
2699 C CA  . VAL B 26  ? 0.2654 0.2273 0.3015 0.0575  -0.0120 -0.0388 38  VAL B CA  
2700 C C   . VAL B 26  ? 0.3034 0.2542 0.3284 0.0586  -0.0136 -0.0401 38  VAL B C   
2701 O O   . VAL B 26  ? 0.3127 0.2555 0.3295 0.0596  -0.0160 -0.0421 38  VAL B O   
2702 C CB  . VAL B 26  ? 0.2781 0.2486 0.3184 0.0588  -0.0083 -0.0351 38  VAL B CB  
2703 C CG1 . VAL B 26  ? 0.2534 0.2346 0.3037 0.0571  -0.0062 -0.0331 38  VAL B CG1 
2704 C CG2 . VAL B 26  ? 0.2918 0.2596 0.3269 0.0614  -0.0089 -0.0352 38  VAL B CG2 
2705 N N   . SER B 27  ? 0.3078 0.2579 0.3321 0.0583  -0.0121 -0.0387 39  SER B N   
2706 C CA  . SER B 27  ? 0.3133 0.2536 0.3283 0.0591  -0.0135 -0.0395 39  SER B CA  
2707 C C   . SER B 27  ? 0.3266 0.2697 0.3433 0.0601  -0.0109 -0.0367 39  SER B C   
2708 O O   . SER B 27  ? 0.2877 0.2388 0.3116 0.0595  -0.0086 -0.0346 39  SER B O   
2709 C CB  . SER B 27  ? 0.3867 0.3187 0.3969 0.0564  -0.0164 -0.0422 39  SER B CB  
2710 O OG  . SER B 27  ? 0.3667 0.3006 0.3804 0.0549  -0.0155 -0.0414 39  SER B OG  
2711 N N   . ASP B 28  ? 0.3434 0.2795 0.3532 0.0617  -0.0114 -0.0367 40  ASP B N   
2712 C CA  . ASP B 28  ? 0.3829 0.3195 0.3935 0.0628  -0.0098 -0.0345 40  ASP B CA  
2713 C C   . ASP B 28  ? 0.3922 0.3227 0.3994 0.0614  -0.0117 -0.0355 40  ASP B C   
2714 O O   . ASP B 28  ? 0.4082 0.3373 0.4147 0.0625  -0.0111 -0.0340 40  ASP B O   
2715 C CB  . ASP B 28  ? 0.3697 0.3027 0.3760 0.0655  -0.0089 -0.0336 40  ASP B CB  
2716 C CG  . ASP B 28  ? 0.4079 0.3296 0.4039 0.0659  -0.0113 -0.0361 40  ASP B CG  
2717 O OD1 . ASP B 28  ? 0.4064 0.3224 0.3982 0.0638  -0.0138 -0.0383 40  ASP B OD1 
2718 O OD2 . ASP B 28  ? 0.4411 0.3592 0.4329 0.0680  -0.0105 -0.0359 40  ASP B OD2 
2719 N N   . GLY B 29  ? 0.3798 0.3062 0.3846 0.0589  -0.0140 -0.0381 41  GLY B N   
2720 C CA  . GLY B 29  ? 0.4362 0.3555 0.4366 0.0569  -0.0161 -0.0393 41  GLY B CA  
2721 C C   . GLY B 29  ? 0.4386 0.3469 0.4287 0.0566  -0.0183 -0.0410 41  GLY B C   
2722 O O   . GLY B 29  ? 0.4429 0.3447 0.4286 0.0543  -0.0202 -0.0421 41  GLY B O   
2723 N N   . ARG B 30  ? 0.4047 0.3102 0.3903 0.0587  -0.0180 -0.0411 42  ARG B N   
2724 C CA  . ARG B 30  ? 0.4075 0.3020 0.3824 0.0584  -0.0197 -0.0427 42  ARG B CA  
2725 C C   . ARG B 30  ? 0.4696 0.3609 0.4398 0.0578  -0.0209 -0.0446 42  ARG B C   
2726 O O   . ARG B 30  ? 0.4813 0.3638 0.4431 0.0551  -0.0232 -0.0466 42  ARG B O   
2727 C CB  . ARG B 30  ? 0.4566 0.3483 0.4286 0.0616  -0.0180 -0.0409 42  ARG B CB  
2728 C CG  . ARG B 30  ? 0.5029 0.3829 0.4640 0.0613  -0.0193 -0.0421 42  ARG B CG  
2729 C CD  . ARG B 30  ? 0.5412 0.4185 0.5017 0.0627  -0.0187 -0.0404 42  ARG B CD  
2730 N NE  . ARG B 30  ? 0.5423 0.4252 0.5084 0.0664  -0.0159 -0.0377 42  ARG B NE  
2731 C CZ  . ARG B 30  ? 0.5704 0.4544 0.5395 0.0680  -0.0152 -0.0355 42  ARG B CZ  
2732 N NH1 . ARG B 30  ? 0.5751 0.4554 0.5425 0.0663  -0.0170 -0.0356 42  ARG B NH1 
2733 N NH2 . ARG B 30  ? 0.5795 0.4683 0.5535 0.0710  -0.0127 -0.0331 42  ARG B NH2 
2734 N N   . HIS B 31  ? 0.4353 0.3332 0.4102 0.0600  -0.0193 -0.0439 43  HIS B N   
2735 C CA  . HIS B 31  ? 0.4082 0.3036 0.3791 0.0598  -0.0206 -0.0457 43  HIS B CA  
2736 C C   . HIS B 31  ? 0.3948 0.2999 0.3754 0.0591  -0.0206 -0.0457 43  HIS B C   
2737 O O   . HIS B 31  ? 0.3930 0.3083 0.3831 0.0606  -0.0180 -0.0435 43  HIS B O   
2738 C CB  . HIS B 31  ? 0.4392 0.3335 0.4068 0.0632  -0.0187 -0.0449 43  HIS B CB  
2739 C CG  . HIS B 31  ? 0.4497 0.3368 0.4107 0.0646  -0.0177 -0.0442 43  HIS B CG  
2740 N ND1 . HIS B 31  ? 0.4879 0.3794 0.4543 0.0666  -0.0154 -0.0416 43  HIS B ND1 
2741 C CD2 . HIS B 31  ? 0.4778 0.3535 0.4275 0.0642  -0.0185 -0.0455 43  HIS B CD2 
2742 C CE1 . HIS B 31  ? 0.4796 0.3630 0.4390 0.0677  -0.0150 -0.0415 43  HIS B CE1 
2743 N NE2 . HIS B 31  ? 0.4809 0.3547 0.4301 0.0663  -0.0166 -0.0438 43  HIS B NE2 
2744 N N   . MET B 32  ? 0.3928 0.2948 0.3712 0.0566  -0.0233 -0.0480 44  MET B N   
2745 C CA  . MET B 32  ? 0.3452 0.2563 0.3338 0.0559  -0.0235 -0.0482 44  MET B CA  
2746 C C   . MET B 32  ? 0.3597 0.2730 0.3474 0.0568  -0.0238 -0.0482 44  MET B C   
2747 O O   . MET B 32  ? 0.3088 0.2146 0.2865 0.0541  -0.0258 -0.0490 44  MET B O   
2748 C CB  . MET B 32  ? 0.3734 0.2847 0.3630 0.0495  -0.0253 -0.0484 44  MET B CB  
2749 C CG  . MET B 32  ? 0.3295 0.2538 0.3321 0.0471  -0.0238 -0.0465 44  MET B CG  
2750 S SD  . MET B 32  ? 0.3324 0.2568 0.3357 0.0390  -0.0254 -0.0460 44  MET B SD  
2751 C CE  . MET B 32  ? 0.2906 0.2104 0.2848 0.0348  -0.0284 -0.0458 44  MET B CE  
2752 N N   . PHE B 33  ? 0.3073 0.2311 0.3050 0.0600  -0.0217 -0.0469 45  PHE B N   
2753 C CA  . PHE B 33  ? 0.3308 0.2582 0.3285 0.0608  -0.0217 -0.0463 45  PHE B CA  
2754 C C   . PHE B 33  ? 0.3102 0.2486 0.3173 0.0562  -0.0218 -0.0443 45  PHE B C   
2755 O O   . PHE B 33  ? 0.3243 0.2722 0.3430 0.0562  -0.0200 -0.0430 45  PHE B O   
2756 C CB  . PHE B 33  ? 0.3410 0.2750 0.3432 0.0651  -0.0183 -0.0442 45  PHE B CB  
2757 C CG  . PHE B 33  ? 0.3986 0.3274 0.3946 0.0663  -0.0164 -0.0430 45  PHE B CG  
2758 C CD1 . PHE B 33  ? 0.3966 0.3289 0.3971 0.0656  -0.0144 -0.0410 45  PHE B CD1 
2759 C CD2 . PHE B 33  ? 0.4185 0.3387 0.4044 0.0680  -0.0166 -0.0440 45  PHE B CD2 
2760 C CE1 . PHE B 33  ? 0.4152 0.3432 0.4114 0.0669  -0.0129 -0.0398 45  PHE B CE1 
2761 C CE2 . PHE B 33  ? 0.4676 0.3838 0.4495 0.0692  -0.0147 -0.0427 45  PHE B CE2 
2762 C CZ  . PHE B 33  ? 0.4157 0.3361 0.4032 0.0687  -0.0130 -0.0406 45  PHE B CZ  
2763 N N   . VAL B 34  ? 0.2792 0.2163 0.2813 0.0520  -0.0238 -0.0437 46  VAL B N   
2764 C CA  . VAL B 34  ? 0.2605 0.2073 0.2706 0.0469  -0.0244 -0.0413 46  VAL B CA  
2765 C C   . VAL B 34  ? 0.2614 0.2138 0.2731 0.0477  -0.0244 -0.0399 46  VAL B C   
2766 O O   . VAL B 34  ? 0.2899 0.2345 0.2908 0.0485  -0.0257 -0.0411 46  VAL B O   
2767 C CB  . VAL B 34  ? 0.3039 0.2449 0.3071 0.0400  -0.0273 -0.0412 46  VAL B CB  
2768 C CG1 . VAL B 34  ? 0.2825 0.2339 0.2943 0.0347  -0.0279 -0.0381 46  VAL B CG1 
2769 C CG2 . VAL B 34  ? 0.2626 0.1985 0.2647 0.0390  -0.0272 -0.0426 46  VAL B CG2 
2770 N N   . TRP B 35  ? 0.2601 0.2256 0.2851 0.0476  -0.0228 -0.0374 47  TRP B N   
2771 C CA  . TRP B 35  ? 0.2331 0.2055 0.2612 0.0480  -0.0229 -0.0356 47  TRP B CA  
2772 C C   . TRP B 35  ? 0.2114 0.1961 0.2514 0.0435  -0.0228 -0.0320 47  TRP B C   
2773 O O   . TRP B 35  ? 0.1601 0.1517 0.2107 0.0430  -0.0207 -0.0309 47  TRP B O   
2774 C CB  . TRP B 35  ? 0.2566 0.2334 0.2901 0.0551  -0.0201 -0.0361 47  TRP B CB  
2775 C CG  . TRP B 35  ? 0.2513 0.2356 0.2886 0.0557  -0.0200 -0.0342 47  TRP B CG  
2776 C CD1 . TRP B 35  ? 0.2933 0.2720 0.3209 0.0566  -0.0212 -0.0350 47  TRP B CD1 
2777 C CD2 . TRP B 35  ? 0.2097 0.2081 0.2612 0.0554  -0.0184 -0.0312 47  TRP B CD2 
2778 N NE1 . TRP B 35  ? 0.2292 0.2179 0.2640 0.0565  -0.0209 -0.0326 47  TRP B NE1 
2779 C CE2 . TRP B 35  ? 0.2141 0.2153 0.2640 0.0559  -0.0191 -0.0301 47  TRP B CE2 
2780 C CE3 . TRP B 35  ? 0.1752 0.1840 0.2406 0.0544  -0.0162 -0.0292 47  TRP B CE3 
2781 C CZ2 . TRP B 35  ? 0.1740 0.1883 0.2360 0.0558  -0.0180 -0.0270 47  TRP B CZ2 
2782 C CZ3 . TRP B 35  ? 0.1558 0.1773 0.2332 0.0544  -0.0147 -0.0261 47  TRP B CZ3 
2783 C CH2 . TRP B 35  ? 0.1762 0.2006 0.2521 0.0552  -0.0157 -0.0249 47  TRP B CH2 
2784 N N   . GLY B 36  ? 0.2182 0.2057 0.2564 0.0402  -0.0248 -0.0300 48  GLY B N   
2785 C CA  . GLY B 36  ? 0.2311 0.2321 0.2824 0.0373  -0.0242 -0.0260 48  GLY B CA  
2786 C C   . GLY B 36  ? 0.1640 0.1679 0.2196 0.0309  -0.0252 -0.0237 48  GLY B C   
2787 O O   . GLY B 36  ? 0.2024 0.1973 0.2483 0.0270  -0.0277 -0.0248 48  GLY B O   
2788 N N   . GLY B 37  ? 0.1419 0.1586 0.2126 0.0300  -0.0230 -0.0203 49  GLY B N   
2789 C CA  . GLY B 37  ? 0.1694 0.1906 0.2464 0.0243  -0.0233 -0.0174 49  GLY B CA  
2790 C C   . GLY B 37  ? 0.1978 0.2242 0.2755 0.0189  -0.0262 -0.0134 49  GLY B C   
2791 O O   . GLY B 37  ? 0.1804 0.2078 0.2545 0.0197  -0.0277 -0.0128 49  GLY B O   
2792 N N   . TYR B 38  ? 0.1502 0.1797 0.2322 0.0132  -0.0271 -0.0104 50  TYR B N   
2793 C CA  . TYR B 38  ? 0.1936 0.2296 0.2783 0.0074  -0.0298 -0.0057 50  TYR B CA  
2794 C C   . TYR B 38  ? 0.2353 0.2671 0.3162 0.0009  -0.0322 -0.0045 50  TYR B C   
2795 O O   . TYR B 38  ? 0.1991 0.2251 0.2782 0.0012  -0.0310 -0.0070 50  TYR B O   
2796 C CB  . TYR B 38  ? 0.2168 0.2686 0.3196 0.0080  -0.0268 -0.0008 50  TYR B CB  
2797 C CG  . TYR B 38  ? 0.1434 0.2009 0.2578 0.0055  -0.0241 0.0017  50  TYR B CG  
2798 C CD1 . TYR B 38  ? 0.1415 0.1970 0.2599 0.0091  -0.0201 -0.0012 50  TYR B CD1 
2799 C CD2 . TYR B 38  ? 0.1617 0.2262 0.2827 -0.0006 -0.0255 0.0070  50  TYR B CD2 
2800 C CE1 . TYR B 38  ? 0.1551 0.2149 0.2834 0.0067  -0.0173 0.0009  50  TYR B CE1 
2801 C CE2 . TYR B 38  ? 0.1649 0.2341 0.2964 -0.0027 -0.0226 0.0094  50  TYR B CE2 
2802 C CZ  . TYR B 38  ? 0.1446 0.2111 0.2795 0.0009  -0.0183 0.0061  50  TYR B CZ  
2803 O OH  . TYR B 38  ? 0.1510 0.2217 0.2960 -0.0014 -0.0152 0.0085  50  TYR B OH  
2804 N N   . LYS B 39  ? 0.2051 0.2401 0.2847 -0.0051 -0.0357 -0.0006 51  LYS B N   
2805 C CA  . LYS B 39  ? 0.2672 0.3000 0.3447 -0.0118 -0.0381 0.0015  51  LYS B CA  
2806 C C   . LYS B 39  ? 0.3084 0.3528 0.3949 -0.0171 -0.0398 0.0082  51  LYS B C   
2807 O O   . LYS B 39  ? 0.2540 0.3091 0.3509 -0.0151 -0.0382 0.0112  51  LYS B O   
2808 C CB  . LYS B 39  ? 0.2422 0.2596 0.3003 -0.0144 -0.0422 -0.0024 51  LYS B CB  
2809 C CG  . LYS B 39  ? 0.3834 0.3961 0.4293 -0.0162 -0.0460 -0.0026 51  LYS B CG  
2810 C CD  . LYS B 39  ? 0.3951 0.3910 0.4216 -0.0173 -0.0488 -0.0075 51  LYS B CD  
2811 C CE  . LYS B 39  ? 0.4740 0.4636 0.4871 -0.0187 -0.0518 -0.0083 51  LYS B CE  
2812 N NZ  . LYS B 39  ? 0.5066 0.5005 0.5184 -0.0267 -0.0560 -0.0035 51  LYS B NZ  
2813 N N   . SER B 40  ? 0.3493 0.3921 0.4324 -0.0240 -0.0431 0.0108  52  SER B N   
2814 C CA  . SER B 40  ? 0.3940 0.4479 0.4857 -0.0299 -0.0451 0.0179  52  SER B CA  
2815 C C   . SER B 40  ? 0.4571 0.5031 0.5334 -0.0367 -0.0512 0.0184  52  SER B C   
2816 O O   . SER B 40  ? 0.5050 0.5462 0.5769 -0.0415 -0.0533 0.0189  52  SER B O   
2817 C CB  . SER B 40  ? 0.3686 0.4310 0.4752 -0.0319 -0.0423 0.0220  52  SER B CB  
2818 O OG  . SER B 40  ? 0.3823 0.4353 0.4809 -0.0351 -0.0436 0.0198  52  SER B OG  
2819 N N   . ASN B 41  ? 0.5773 0.6219 0.6455 -0.0373 -0.0541 0.0184  53  ASN B N   
2820 C CA  . ASN B 41  ? 0.6322 0.6700 0.6858 -0.0444 -0.0598 0.0194  53  ASN B CA  
2821 C C   . ASN B 41  ? 0.6672 0.7066 0.7157 -0.0446 -0.0619 0.0203  53  ASN B C   
2822 O O   . ASN B 41  ? 0.6882 0.7154 0.7201 -0.0439 -0.0637 0.0157  53  ASN B O   
2823 C CB  . ASN B 41  ? 0.7199 0.7402 0.7551 -0.0450 -0.0616 0.0133  53  ASN B CB  
2824 C CG  . ASN B 41  ? 0.7778 0.7921 0.8009 -0.0537 -0.0672 0.0153  53  ASN B CG  
2825 O OD1 . ASN B 41  ? 0.7647 0.7886 0.7952 -0.0598 -0.0695 0.0216  53  ASN B OD1 
2826 N ND2 . ASN B 41  ? 0.8070 0.8053 0.8113 -0.0545 -0.0693 0.0100  53  ASN B ND2 
2827 N N   . PHE B 49  ? 0.4000 0.4619 0.4909 -0.0147 -0.0425 0.0142  61  PHE B N   
2828 C CA  . PHE B 49  ? 0.2759 0.3367 0.3635 -0.0091 -0.0414 0.0114  61  PHE B CA  
2829 C C   . PHE B 49  ? 0.2802 0.3316 0.3626 -0.0021 -0.0383 0.0049  61  PHE B C   
2830 O O   . PHE B 49  ? 0.2974 0.3426 0.3776 -0.0020 -0.0374 0.0025  61  PHE B O   
2831 C CB  . PHE B 49  ? 0.3999 0.4539 0.4722 -0.0126 -0.0461 0.0110  61  PHE B CB  
2832 C CG  . PHE B 49  ? 0.4623 0.5002 0.5157 -0.0158 -0.0493 0.0069  61  PHE B CG  
2833 C CD1 . PHE B 49  ? 0.4852 0.5107 0.5288 -0.0107 -0.0477 0.0006  61  PHE B CD1 
2834 C CD2 . PHE B 49  ? 0.5129 0.5481 0.5583 -0.0240 -0.0541 0.0097  61  PHE B CD2 
2835 C CE1 . PHE B 49  ? 0.5794 0.5902 0.6061 -0.0135 -0.0503 -0.0030 61  PHE B CE1 
2836 C CE2 . PHE B 49  ? 0.6019 0.6219 0.6297 -0.0271 -0.0569 0.0059  61  PHE B CE2 
2837 C CZ  . PHE B 49  ? 0.5724 0.5802 0.5909 -0.0216 -0.0549 -0.0005 61  PHE B CZ  
2838 N N   . TYR B 50  ? 0.2445 0.2946 0.3242 0.0034  -0.0370 0.0023  62  TYR B N   
2839 C CA  . TYR B 50  ? 0.2584 0.2996 0.3324 0.0099  -0.0345 -0.0034 62  TYR B CA  
2840 C C   . TYR B 50  ? 0.2908 0.3160 0.3449 0.0090  -0.0375 -0.0078 62  TYR B C   
2841 O O   . TYR B 50  ? 0.3101 0.3315 0.3543 0.0055  -0.0408 -0.0072 62  TYR B O   
2842 C CB  . TYR B 50  ? 0.2174 0.2648 0.2986 0.0167  -0.0313 -0.0041 62  TYR B CB  
2843 C CG  . TYR B 50  ? 0.2200 0.2816 0.3204 0.0188  -0.0274 -0.0007 62  TYR B CG  
2844 C CD1 . TYR B 50  ? 0.2147 0.2770 0.3224 0.0224  -0.0235 -0.0026 62  TYR B CD1 
2845 C CD2 . TYR B 50  ? 0.2320 0.3064 0.3433 0.0168  -0.0274 0.0045  62  TYR B CD2 
2846 C CE1 . TYR B 50  ? 0.1996 0.2741 0.3243 0.0240  -0.0194 0.0004  62  TYR B CE1 
2847 C CE2 . TYR B 50  ? 0.2271 0.3141 0.3561 0.0187  -0.0235 0.0077  62  TYR B CE2 
2848 C CZ  . TYR B 50  ? 0.1976 0.2843 0.3330 0.0223  -0.0193 0.0055  62  TYR B CZ  
2849 O OH  . TYR B 50  ? 0.2358 0.3347 0.3885 0.0240  -0.0150 0.0088  62  TYR B OH  
2850 N N   . LEU B 51  ? 0.2735 0.2891 0.3218 0.0121  -0.0362 -0.0122 63  LEU B N   
2851 C CA  . LEU B 51  ? 0.2856 0.2856 0.3158 0.0125  -0.0382 -0.0166 63  LEU B CA  
2852 C C   . LEU B 51  ? 0.2469 0.2440 0.2718 0.0179  -0.0371 -0.0188 63  LEU B C   
2853 O O   . LEU B 51  ? 0.2848 0.2909 0.3207 0.0228  -0.0342 -0.0180 63  LEU B O   
2854 C CB  . LEU B 51  ? 0.2366 0.2281 0.2634 0.0147  -0.0368 -0.0202 63  LEU B CB  
2855 C CG  . LEU B 51  ? 0.2603 0.2480 0.2843 0.0086  -0.0390 -0.0195 63  LEU B CG  
2856 C CD1 . LEU B 51  ? 0.3217 0.3008 0.3311 0.0023  -0.0435 -0.0192 63  LEU B CD1 
2857 C CD2 . LEU B 51  ? 0.2232 0.2241 0.2634 0.0058  -0.0377 -0.0150 63  LEU B CD2 
2858 N N   . PRO B 52  ? 0.2647 0.2491 0.2729 0.0171  -0.0392 -0.0216 64  PRO B N   
2859 C CA  . PRO B 52  ? 0.2814 0.2631 0.2840 0.0214  -0.0383 -0.0232 64  PRO B CA  
2860 C C   . PRO B 52  ? 0.3003 0.2821 0.3080 0.0301  -0.0343 -0.0260 64  PRO B C   
2861 O O   . PRO B 52  ? 0.2719 0.2466 0.2769 0.0328  -0.0330 -0.0288 64  PRO B O   
2862 C CB  . PRO B 52  ? 0.3330 0.2987 0.3155 0.0184  -0.0409 -0.0260 64  PRO B CB  
2863 C CG  . PRO B 52  ? 0.3535 0.3173 0.3327 0.0106  -0.0442 -0.0243 64  PRO B CG  
2864 C CD  . PRO B 52  ? 0.3164 0.2884 0.3097 0.0115  -0.0425 -0.0230 64  PRO B CD  
2865 N N   . ARG B 53  ? 0.2807 0.2706 0.2957 0.0343  -0.0323 -0.0250 65  ARG B N   
2866 C CA  . ARG B 53  ? 0.2446 0.2372 0.2669 0.0424  -0.0285 -0.0268 65  ARG B CA  
2867 C C   . ARG B 53  ? 0.3208 0.2996 0.3302 0.0472  -0.0275 -0.0311 65  ARG B C   
2868 O O   . ARG B 53  ? 0.2519 0.2300 0.2652 0.0530  -0.0248 -0.0329 65  ARG B O   
2869 C CB  . ARG B 53  ? 0.2314 0.2362 0.2645 0.0453  -0.0268 -0.0244 65  ARG B CB  
2870 C CG  . ARG B 53  ? 0.2752 0.2766 0.2986 0.0438  -0.0287 -0.0242 65  ARG B CG  
2871 C CD  . ARG B 53  ? 0.2420 0.2576 0.2773 0.0439  -0.0281 -0.0205 65  ARG B CD  
2872 N NE  . ARG B 53  ? 0.2527 0.2740 0.2968 0.0516  -0.0245 -0.0214 65  ARG B NE  
2873 C CZ  . ARG B 53  ? 0.2428 0.2732 0.2937 0.0536  -0.0235 -0.0194 65  ARG B CZ  
2874 N NH1 . ARG B 53  ? 0.2374 0.2720 0.2870 0.0486  -0.0261 -0.0164 65  ARG B NH1 
2875 N NH2 . ARG B 53  ? 0.2085 0.2439 0.2676 0.0607  -0.0201 -0.0203 65  ARG B NH2 
2876 N N   . GLU B 54  ? 0.3021 0.2701 0.2964 0.0450  -0.0295 -0.0326 66  GLU B N   
2877 C CA  . GLU B 54  ? 0.2914 0.2467 0.2740 0.0501  -0.0279 -0.0363 66  GLU B CA  
2878 C C   . GLU B 54  ? 0.3891 0.3318 0.3622 0.0496  -0.0284 -0.0390 66  GLU B C   
2879 O O   . GLU B 54  ? 0.3695 0.3012 0.3336 0.0541  -0.0268 -0.0419 66  GLU B O   
2880 C CB  . GLU B 54  ? 0.3731 0.3214 0.3429 0.0484  -0.0291 -0.0369 66  GLU B CB  
2881 C CG  . GLU B 54  ? 0.3800 0.3196 0.3366 0.0403  -0.0327 -0.0369 66  GLU B CG  
2882 C CD  . GLU B 54  ? 0.3993 0.3503 0.3633 0.0332  -0.0357 -0.0326 66  GLU B CD  
2883 O OE1 . GLU B 54  ? 0.2968 0.2624 0.2763 0.0347  -0.0347 -0.0297 66  GLU B OE1 
2884 O OE2 . GLU B 54  ? 0.4292 0.3744 0.3833 0.0259  -0.0390 -0.0320 66  GLU B OE2 
2885 N N   . GLU B 55  ? 0.3719 0.3158 0.3470 0.0441  -0.0304 -0.0379 67  GLU B N   
2886 C CA  . GLU B 55  ? 0.3762 0.3084 0.3423 0.0429  -0.0312 -0.0403 67  GLU B CA  
2887 C C   . GLU B 55  ? 0.3639 0.2992 0.3393 0.0475  -0.0289 -0.0410 67  GLU B C   
2888 O O   . GLU B 55  ? 0.3212 0.2690 0.3111 0.0480  -0.0278 -0.0389 67  GLU B O   
2889 C CB  . GLU B 55  ? 0.3808 0.3125 0.3438 0.0344  -0.0347 -0.0387 67  GLU B CB  
2890 C CG  . GLU B 55  ? 0.4165 0.3442 0.3690 0.0288  -0.0376 -0.0378 67  GLU B CG  
2891 C CD  . GLU B 55  ? 0.4676 0.3937 0.4160 0.0203  -0.0412 -0.0362 67  GLU B CD  
2892 O OE1 . GLU B 55  ? 0.4123 0.3451 0.3706 0.0186  -0.0414 -0.0347 67  GLU B OE1 
2893 O OE2 . GLU B 55  ? 0.4493 0.3670 0.3842 0.0153  -0.0438 -0.0365 67  GLU B OE2 
2894 N N   . LEU B 56  ? 0.3751 0.2988 0.3419 0.0508  -0.0280 -0.0438 68  LEU B N   
2895 C CA  . LEU B 56  ? 0.3691 0.2933 0.3421 0.0546  -0.0262 -0.0447 68  LEU B CA  
2896 C C   . LEU B 56  ? 0.4516 0.3635 0.4136 0.0514  -0.0280 -0.0465 68  LEU B C   
2897 O O   . LEU B 56  ? 0.4216 0.3205 0.3701 0.0525  -0.0282 -0.0486 68  LEU B O   
2898 C CB  . LEU B 56  ? 0.3899 0.3126 0.3640 0.0628  -0.0232 -0.0459 68  LEU B CB  
2899 C CG  . LEU B 56  ? 0.3701 0.2950 0.3518 0.0670  -0.0213 -0.0462 68  LEU B CG  
2900 C CD1 . LEU B 56  ? 0.3303 0.2694 0.3274 0.0654  -0.0207 -0.0440 68  LEU B CD1 
2901 C CD2 . LEU B 56  ? 0.4575 0.3820 0.4397 0.0733  -0.0181 -0.0461 68  LEU B CD2 
2902 N N   . TRP B 57  ? 0.3427 0.2582 0.3101 0.0473  -0.0292 -0.0456 69  TRP B N   
2903 C CA  . TRP B 57  ? 0.3872 0.2921 0.3452 0.0438  -0.0310 -0.0470 69  TRP B CA  
2904 C C   . TRP B 57  ? 0.4002 0.3025 0.3611 0.0484  -0.0292 -0.0483 69  TRP B C   
2905 O O   . TRP B 57  ? 0.3489 0.2611 0.3224 0.0506  -0.0274 -0.0472 69  TRP B O   
2906 C CB  . TRP B 57  ? 0.3943 0.3042 0.3560 0.0363  -0.0334 -0.0452 69  TRP B CB  
2907 C CG  . TRP B 57  ? 0.4523 0.3615 0.4076 0.0306  -0.0361 -0.0439 69  TRP B CG  
2908 C CD1 . TRP B 57  ? 0.4190 0.3394 0.3821 0.0285  -0.0365 -0.0411 69  TRP B CD1 
2909 C CD2 . TRP B 57  ? 0.4853 0.3820 0.4250 0.0260  -0.0388 -0.0452 69  TRP B CD2 
2910 N NE1 . TRP B 57  ? 0.4565 0.3723 0.4098 0.0226  -0.0395 -0.0404 69  TRP B NE1 
2911 C CE2 . TRP B 57  ? 0.4962 0.3973 0.4347 0.0209  -0.0410 -0.0430 69  TRP B CE2 
2912 C CE3 . TRP B 57  ? 0.5053 0.3875 0.4319 0.0254  -0.0396 -0.0479 69  TRP B CE3 
2913 C CZ2 . TRP B 57  ? 0.5216 0.4128 0.4457 0.0151  -0.0440 -0.0435 69  TRP B CZ2 
2914 C CZ3 . TRP B 57  ? 0.5530 0.4251 0.4653 0.0199  -0.0424 -0.0486 69  TRP B CZ3 
2915 C CH2 . TRP B 57  ? 0.5166 0.3932 0.4276 0.0147  -0.0445 -0.0465 69  TRP B CH2 
2916 N N   . ILE B 58  ? 0.4472 0.3361 0.3962 0.0497  -0.0295 -0.0505 70  ILE B N   
2917 C CA  . ILE B 58  ? 0.4242 0.3093 0.3744 0.0540  -0.0280 -0.0515 70  ILE B CA  
2918 C C   . ILE B 58  ? 0.4287 0.3056 0.3720 0.0493  -0.0302 -0.0524 70  ILE B C   
2919 O O   . ILE B 58  ? 0.4616 0.3276 0.3921 0.0461  -0.0319 -0.0537 70  ILE B O   
2920 C CB  . ILE B 58  ? 0.4116 0.2883 0.3548 0.0605  -0.0260 -0.0528 70  ILE B CB  
2921 C CG1 . ILE B 58  ? 0.4008 0.2870 0.3516 0.0646  -0.0237 -0.0514 70  ILE B CG1 
2922 C CG2 . ILE B 58  ? 0.4140 0.2924 0.3606 0.0615  -0.0237 -0.0508 70  ILE B CG2 
2923 C CD1 . ILE B 58  ? 0.4638 0.3471 0.4098 0.0677  -0.0206 -0.0502 70  ILE B CD1 
2924 N N   . TYR B 59  ? 0.4390 0.3207 0.3902 0.0485  -0.0300 -0.0518 71  TYR B N   
2925 C CA  . TYR B 59  ? 0.4395 0.3143 0.3854 0.0442  -0.0319 -0.0526 71  TYR B CA  
2926 C C   . TYR B 59  ? 0.4459 0.3150 0.3902 0.0484  -0.0306 -0.0533 71  TYR B C   
2927 O O   . TYR B 59  ? 0.4494 0.3278 0.4040 0.0514  -0.0281 -0.0516 71  TYR B O   
2928 C CB  . TYR B 59  ? 0.4170 0.3016 0.3729 0.0391  -0.0325 -0.0511 71  TYR B CB  
2929 C CG  . TYR B 59  ? 0.4208 0.2997 0.3731 0.0349  -0.0341 -0.0517 71  TYR B CG  
2930 C CD1 . TYR B 59  ? 0.4368 0.3083 0.3797 0.0291  -0.0369 -0.0523 71  TYR B CD1 
2931 C CD2 . TYR B 59  ? 0.3870 0.2680 0.3454 0.0364  -0.0329 -0.0517 71  TYR B CD2 
2932 C CE1 . TYR B 59  ? 0.4622 0.3287 0.4020 0.0253  -0.0384 -0.0528 71  TYR B CE1 
2933 C CE2 . TYR B 59  ? 0.4234 0.2993 0.3785 0.0323  -0.0344 -0.0523 71  TYR B CE2 
2934 C CZ  . TYR B 59  ? 0.4252 0.2939 0.3711 0.0270  -0.0370 -0.0529 71  TYR B CZ  
2935 O OH  . TYR B 59  ? 0.4781 0.3416 0.4207 0.0230  -0.0385 -0.0535 71  TYR B OH  
2936 N N   . ASN B 60  ? 0.4638 0.3230 0.3974 0.0467  -0.0310 -0.0536 72  ASN B N   
2937 C CA  . ASN B 60  ? 0.4866 0.3448 0.4205 0.0484  -0.0291 -0.0521 72  ASN B CA  
2938 C C   . ASN B 60  ? 0.4746 0.3336 0.4115 0.0446  -0.0306 -0.0522 72  ASN B C   
2939 O O   . ASN B 60  ? 0.4608 0.3136 0.3912 0.0397  -0.0331 -0.0534 72  ASN B O   
2940 C CB  . ASN B 60  ? 0.5229 0.3702 0.4446 0.0484  -0.0288 -0.0525 72  ASN B CB  
2941 C CG  . ASN B 60  ? 0.5397 0.3865 0.4626 0.0515  -0.0265 -0.0507 72  ASN B CG  
2942 O OD1 . ASN B 60  ? 0.5563 0.4065 0.4847 0.0509  -0.0266 -0.0498 72  ASN B OD1 
2943 N ND2 . ASN B 60  ? 0.5333 0.3754 0.4510 0.0545  -0.0245 -0.0502 72  ASN B ND2 
2944 N N   . MET B 61  ? 0.4584 0.3252 0.4049 0.0464  -0.0290 -0.0507 73  MET B N   
2945 C CA  . MET B 61  ? 0.4718 0.3402 0.4222 0.0428  -0.0300 -0.0509 73  MET B CA  
2946 C C   . MET B 61  ? 0.5559 0.4170 0.4995 0.0409  -0.0307 -0.0506 73  MET B C   
2947 O O   . MET B 61  ? 0.4798 0.3401 0.4240 0.0368  -0.0320 -0.0510 73  MET B O   
2948 C CB  . MET B 61  ? 0.4893 0.3683 0.4518 0.0450  -0.0279 -0.0494 73  MET B CB  
2949 C CG  . MET B 61  ? 0.4704 0.3581 0.4415 0.0461  -0.0272 -0.0496 73  MET B CG  
2950 S SD  . MET B 61  ? 0.5207 0.4210 0.5047 0.0493  -0.0238 -0.0471 73  MET B SD  
2951 C CE  . MET B 61  ? 0.3879 0.2964 0.3822 0.0469  -0.0240 -0.0482 73  MET B CE  
2952 N N   . GLU B 62  ? 0.5285 0.3843 0.4662 0.0439  -0.0296 -0.0499 74  GLU B N   
2953 C CA  . GLU B 62  ? 0.5489 0.3974 0.4803 0.0427  -0.0301 -0.0495 74  GLU B CA  
2954 C C   . GLU B 62  ? 0.5888 0.4280 0.5092 0.0389  -0.0320 -0.0510 74  GLU B C   
2955 O O   . GLU B 62  ? 0.6110 0.4461 0.5278 0.0352  -0.0334 -0.0512 74  GLU B O   
2956 C CB  . GLU B 62  ? 0.5901 0.4377 0.5212 0.0478  -0.0278 -0.0478 74  GLU B CB  
2957 C CG  . GLU B 62  ? 0.5929 0.4496 0.5344 0.0511  -0.0260 -0.0459 74  GLU B CG  
2958 C CD  . GLU B 62  ? 0.6477 0.5036 0.5892 0.0557  -0.0238 -0.0439 74  GLU B CD  
2959 O OE1 . GLU B 62  ? 0.6608 0.5129 0.5975 0.0579  -0.0226 -0.0440 74  GLU B OE1 
2960 O OE2 . GLU B 62  ? 0.6114 0.4704 0.5578 0.0571  -0.0232 -0.0421 74  GLU B OE2 
2961 N N   . THR B 63  ? 0.5648 0.4007 0.4798 0.0395  -0.0319 -0.0519 75  THR B N   
2962 C CA  . THR B 63  ? 0.6092 0.4359 0.5129 0.0358  -0.0336 -0.0531 75  THR B CA  
2963 C C   . THR B 63  ? 0.5581 0.3858 0.4610 0.0305  -0.0363 -0.0543 75  THR B C   
2964 O O   . THR B 63  ? 0.5349 0.3569 0.4304 0.0255  -0.0382 -0.0549 75  THR B O   
2965 C CB  . THR B 63  ? 0.5992 0.4205 0.4959 0.0389  -0.0320 -0.0534 75  THR B CB  
2966 O OG1 . THR B 63  ? 0.5908 0.4163 0.4900 0.0397  -0.0322 -0.0540 75  THR B OG1 
2967 C CG2 . THR B 63  ? 0.5969 0.4194 0.4969 0.0447  -0.0290 -0.0518 75  THR B CG2 
2968 N N   . GLY B 64  ? 0.5565 0.3918 0.4673 0.0312  -0.0365 -0.0545 76  GLY B N   
2969 C CA  . GLY B 64  ? 0.5253 0.3620 0.4364 0.0262  -0.0392 -0.0555 76  GLY B CA  
2970 C C   . GLY B 64  ? 0.5650 0.3975 0.4687 0.0250  -0.0406 -0.0565 76  GLY B C   
2971 O O   . GLY B 64  ? 0.5642 0.3957 0.4653 0.0195  -0.0435 -0.0570 76  GLY B O   
2972 N N   . ARG B 65  ? 0.5753 0.4053 0.4754 0.0296  -0.0386 -0.0566 77  ARG B N   
2973 C CA  . ARG B 65  ? 0.5610 0.3860 0.4526 0.0284  -0.0397 -0.0576 77  ARG B CA  
2974 C C   . ARG B 65  ? 0.5493 0.3816 0.4482 0.0328  -0.0386 -0.0576 77  ARG B C   
2975 O O   . ARG B 65  ? 0.5353 0.3745 0.4437 0.0382  -0.0360 -0.0568 77  ARG B O   
2976 C CB  . ARG B 65  ? 0.6161 0.4315 0.4963 0.0294  -0.0381 -0.0577 77  ARG B CB  
2977 C CG  . ARG B 65  ? 0.6560 0.4650 0.5298 0.0253  -0.0390 -0.0575 77  ARG B CG  
2978 C CD  . ARG B 65  ? 0.7196 0.5180 0.5809 0.0252  -0.0378 -0.0578 77  ARG B CD  
2979 N NE  . ARG B 65  ? 0.7146 0.5113 0.5770 0.0309  -0.0345 -0.0570 77  ARG B NE  
2980 C CZ  . ARG B 65  ? 0.7207 0.5094 0.5757 0.0306  -0.0336 -0.0568 77  ARG B CZ  
2981 N NH1 . ARG B 65  ? 0.7008 0.4828 0.5469 0.0252  -0.0355 -0.0574 77  ARG B NH1 
2982 N NH2 . ARG B 65  ? 0.6961 0.4838 0.5531 0.0359  -0.0306 -0.0559 77  ARG B NH2 
2983 N N   . TRP B 66  ? 0.5334 0.3685 0.4302 0.0294  -0.0397 -0.0569 78  TRP B N   
2984 C CA  . TRP B 66  ? 0.5046 0.3507 0.4103 0.0318  -0.0383 -0.0554 78  TRP B CA  
2985 C C   . TRP B 66  ? 0.5709 0.4095 0.4674 0.0357  -0.0368 -0.0567 78  TRP B C   
2986 O O   . TRP B 66  ? 0.6112 0.4359 0.4935 0.0351  -0.0372 -0.0586 78  TRP B O   
2987 C CB  . TRP B 66  ? 0.5013 0.3565 0.4117 0.0252  -0.0406 -0.0532 78  TRP B CB  
2988 C CG  . TRP B 66  ? 0.4699 0.3355 0.3925 0.0221  -0.0411 -0.0514 78  TRP B CG  
2989 C CD1 . TRP B 66  ? 0.4989 0.3618 0.4192 0.0164  -0.0433 -0.0512 78  TRP B CD1 
2990 C CD2 . TRP B 66  ? 0.4543 0.3343 0.3930 0.0243  -0.0391 -0.0494 78  TRP B CD2 
2991 N NE1 . TRP B 66  ? 0.4224 0.2970 0.3564 0.0150  -0.0426 -0.0493 78  TRP B NE1 
2992 C CE2 . TRP B 66  ? 0.4576 0.3427 0.4030 0.0197  -0.0400 -0.0482 78  TRP B CE2 
2993 C CE3 . TRP B 66  ? 0.4345 0.3234 0.3825 0.0296  -0.0366 -0.0486 78  TRP B CE3 
2994 C CZ2 . TRP B 66  ? 0.3951 0.2932 0.3557 0.0203  -0.0381 -0.0462 78  TRP B CZ2 
2995 C CZ3 . TRP B 66  ? 0.4122 0.3142 0.3753 0.0302  -0.0349 -0.0467 78  TRP B CZ3 
2996 C CH2 . TRP B 66  ? 0.3917 0.2981 0.3610 0.0255  -0.0355 -0.0455 78  TRP B CH2 
2997 N N   . LYS B 67  ? 0.5899 0.4378 0.4948 0.0396  -0.0349 -0.0556 79  LYS B N   
2998 C CA  . LYS B 67  ? 0.6152 0.4580 0.5130 0.0431  -0.0334 -0.0565 79  LYS B CA  
2999 C C   . LYS B 67  ? 0.5558 0.4122 0.4637 0.0430  -0.0331 -0.0544 79  LYS B C   
3000 O O   . LYS B 67  ? 0.5163 0.3856 0.4387 0.0444  -0.0324 -0.0527 79  LYS B O   
3001 C CB  . LYS B 67  ? 0.5688 0.4058 0.4655 0.0512  -0.0301 -0.0577 79  LYS B CB  
3002 C CG  . LYS B 67  ? 0.6702 0.5041 0.5617 0.0549  -0.0275 -0.0578 79  LYS B CG  
3003 C CD  . LYS B 67  ? 0.6972 0.5184 0.5720 0.0505  -0.0291 -0.0597 79  LYS B CD  
3004 C CE  . LYS B 67  ? 0.7439 0.5588 0.6117 0.0536  -0.0253 -0.0593 79  LYS B CE  
3005 N NZ  . LYS B 67  ? 0.7637 0.5874 0.6408 0.0598  -0.0221 -0.0580 79  LYS B NZ  
3006 N N   . LYS B 68  ? 0.5727 0.4259 0.4727 0.0412  -0.0336 -0.0546 80  LYS B N   
3007 C CA  . LYS B 68  ? 0.5445 0.4099 0.4530 0.0409  -0.0336 -0.0524 80  LYS B CA  
3008 C C   . LYS B 68  ? 0.5833 0.4448 0.4872 0.0465  -0.0309 -0.0535 80  LYS B C   
3009 O O   . LYS B 68  ? 0.5866 0.4360 0.4758 0.0452  -0.0311 -0.0552 80  LYS B O   
3010 C CB  . LYS B 68  ? 0.5575 0.4251 0.4623 0.0325  -0.0370 -0.0508 80  LYS B CB  
3011 C CG  . LYS B 68  ? 0.5776 0.4589 0.4925 0.0319  -0.0371 -0.0481 80  LYS B CG  
3012 C CD  . LYS B 68  ? 0.5735 0.4552 0.4822 0.0239  -0.0405 -0.0464 80  LYS B CD  
3013 C CE  . LYS B 68  ? 0.6429 0.5106 0.5338 0.0229  -0.0407 -0.0485 80  LYS B CE  
3014 N NZ  . LYS B 68  ? 0.6492 0.5161 0.5326 0.0140  -0.0445 -0.0468 80  LYS B NZ  
3015 N N   . ILE B 69  ? 0.5183 0.3899 0.4344 0.0524  -0.0285 -0.0526 81  ILE B N   
3016 C CA  . ILE B 69  ? 0.5206 0.3908 0.4345 0.0579  -0.0259 -0.0532 81  ILE B CA  
3017 C C   . ILE B 69  ? 0.5102 0.3944 0.4341 0.0566  -0.0263 -0.0508 81  ILE B C   
3018 O O   . ILE B 69  ? 0.4950 0.3921 0.4319 0.0545  -0.0273 -0.0485 81  ILE B O   
3019 C CB  . ILE B 69  ? 0.5397 0.4096 0.4589 0.0665  -0.0225 -0.0539 81  ILE B CB  
3020 C CG1 . ILE B 69  ? 0.5313 0.4147 0.4672 0.0679  -0.0222 -0.0521 81  ILE B CG1 
3021 C CG2 . ILE B 69  ? 0.5503 0.4057 0.4585 0.0679  -0.0216 -0.0557 81  ILE B CG2 
3022 C CD1 . ILE B 69  ? 0.5214 0.4103 0.4656 0.0736  -0.0185 -0.0505 81  ILE B CD1 
3023 N N   . ASN B 70  ? 0.4899 0.3715 0.4077 0.0577  -0.0255 -0.0511 82  ASN B N   
3024 C CA  . ASN B 70  ? 0.4598 0.3543 0.3869 0.0573  -0.0256 -0.0488 82  ASN B CA  
3025 C C   . ASN B 70  ? 0.5149 0.4144 0.4498 0.0658  -0.0220 -0.0490 82  ASN B C   
3026 O O   . ASN B 70  ? 0.5473 0.4366 0.4738 0.0707  -0.0196 -0.0510 82  ASN B O   
3027 C CB  . ASN B 70  ? 0.5600 0.4496 0.4755 0.0520  -0.0275 -0.0487 82  ASN B CB  
3028 C CG  . ASN B 70  ? 0.5481 0.4375 0.4596 0.0429  -0.0315 -0.0474 82  ASN B CG  
3029 O OD1 . ASN B 70  ? 0.5196 0.4216 0.4410 0.0387  -0.0335 -0.0442 82  ASN B OD1 
3030 N ND2 . ASN B 70  ? 0.6353 0.5106 0.5328 0.0397  -0.0327 -0.0495 82  ASN B ND2 
3031 N N   . THR B 71  ? 0.3798 0.4824 0.3742 0.0938  -0.0379 -0.0813 83  THR B N   
3032 C CA  . THR B 71  ? 0.4009 0.5121 0.3971 0.0947  -0.0351 -0.0763 83  THR B CA  
3033 C C   . THR B 71  ? 0.3382 0.4632 0.3295 0.0950  -0.0330 -0.0758 83  THR B C   
3034 O O   . THR B 71  ? 0.3735 0.5015 0.3602 0.0939  -0.0340 -0.0775 83  THR B O   
3035 C CB  . THR B 71  ? 0.3169 0.4238 0.3159 0.0911  -0.0352 -0.0680 83  THR B CB  
3036 O OG1 . THR B 71  ? 0.3221 0.4298 0.3177 0.0880  -0.0359 -0.0640 83  THR B OG1 
3037 C CG2 . THR B 71  ? 0.3634 0.4570 0.3671 0.0904  -0.0374 -0.0681 83  THR B CG2 
3038 N N   . GLU B 72  ? 0.3152 0.4493 0.3077 0.0964  -0.0302 -0.0728 84  GLU B N   
3039 C CA  . GLU B 72  ? 0.3981 0.5459 0.3863 0.0965  -0.0279 -0.0711 84  GLU B CA  
3040 C C   . GLU B 72  ? 0.3482 0.5009 0.3386 0.0950  -0.0255 -0.0630 84  GLU B C   
3041 O O   . GLU B 72  ? 0.3027 0.4476 0.2969 0.0928  -0.0259 -0.0584 84  GLU B O   
3042 C CB  . GLU B 72  ? 0.4205 0.5765 0.4064 0.1005  -0.0263 -0.0785 84  GLU B CB  
3043 C CG  . GLU B 72  ? 0.3954 0.5484 0.3773 0.1011  -0.0282 -0.0865 84  GLU B CG  
3044 C CD  . GLU B 72  ? 0.4353 0.5961 0.4147 0.1049  -0.0261 -0.0941 84  GLU B CD  
3045 O OE1 . GLU B 72  ? 0.4475 0.6188 0.4270 0.1067  -0.0232 -0.0924 84  GLU B OE1 
3046 O OE2 . GLU B 72  ? 0.4835 0.6396 0.4606 0.1058  -0.0272 -0.1020 84  GLU B OE2 
3047 N N   . GLY B 73  ? 0.3573 0.5229 0.3449 0.0956  -0.0228 -0.0611 85  GLY B N   
3048 C CA  . GLY B 73  ? 0.3026 0.4733 0.2916 0.0937  -0.0201 -0.0534 85  GLY B CA  
3049 C C   . GLY B 73  ? 0.2745 0.4431 0.2616 0.0898  -0.0201 -0.0461 85  GLY B C   
3050 O O   . GLY B 73  ? 0.2627 0.4335 0.2456 0.0894  -0.0212 -0.0465 85  GLY B O   
3051 N N   . ASP B 74  ? 0.2201 0.3846 0.2100 0.0869  -0.0188 -0.0395 86  ASP B N   
3052 C CA  . ASP B 74  ? 0.2266 0.3883 0.2151 0.0834  -0.0180 -0.0320 86  ASP B CA  
3053 C C   . ASP B 74  ? 0.2472 0.3956 0.2370 0.0816  -0.0211 -0.0323 86  ASP B C   
3054 O O   . ASP B 74  ? 0.2478 0.3871 0.2404 0.0788  -0.0209 -0.0282 86  ASP B O   
3055 C CB  . ASP B 74  ? 0.2111 0.3734 0.2018 0.0806  -0.0149 -0.0252 86  ASP B CB  
3056 C CG  . ASP B 74  ? 0.2725 0.4475 0.2627 0.0821  -0.0119 -0.0250 86  ASP B CG  
3057 O OD1 . ASP B 74  ? 0.2194 0.4047 0.2061 0.0848  -0.0114 -0.0278 86  ASP B OD1 
3058 O OD2 . ASP B 74  ? 0.2256 0.4006 0.2188 0.0803  -0.0100 -0.0220 86  ASP B OD2 
3059 N N   . VAL B 75  ? 0.2503 0.3977 0.2377 0.0831  -0.0238 -0.0374 87  VAL B N   
3060 C CA  . VAL B 75  ? 0.2425 0.3777 0.2311 0.0815  -0.0268 -0.0382 87  VAL B CA  
3061 C C   . VAL B 75  ? 0.2267 0.3579 0.2151 0.0782  -0.0258 -0.0301 87  VAL B C   
3062 O O   . VAL B 75  ? 0.2626 0.4017 0.2478 0.0780  -0.0241 -0.0258 87  VAL B O   
3063 C CB  . VAL B 75  ? 0.2376 0.3740 0.2230 0.0831  -0.0296 -0.0446 87  VAL B CB  
3064 C CG1 . VAL B 75  ? 0.2042 0.3277 0.1913 0.0814  -0.0328 -0.0461 87  VAL B CG1 
3065 C CG2 . VAL B 75  ? 0.2410 0.3825 0.2258 0.0866  -0.0297 -0.0527 87  VAL B CG2 
3066 N N   . PRO B 76  ? 0.2113 0.3308 0.2029 0.0757  -0.0263 -0.0274 88  PRO B N   
3067 C CA  . PRO B 76  ? 0.1658 0.2808 0.1571 0.0727  -0.0250 -0.0200 88  PRO B CA  
3068 C C   . PRO B 76  ? 0.2098 0.3251 0.1984 0.0730  -0.0270 -0.0201 88  PRO B C   
3069 O O   . PRO B 76  ? 0.1893 0.3050 0.1769 0.0746  -0.0301 -0.0266 88  PRO B O   
3070 C CB  . PRO B 76  ? 0.1965 0.2983 0.1918 0.0700  -0.0257 -0.0189 88  PRO B CB  
3071 C CG  . PRO B 76  ? 0.1965 0.2956 0.1941 0.0720  -0.0284 -0.0262 88  PRO B CG  
3072 C CD  . PRO B 76  ? 0.1888 0.2995 0.1845 0.0755  -0.0278 -0.0306 88  PRO B CD  
3073 N N   . PRO B 77  ? 0.1719 0.2877 0.1593 0.0716  -0.0252 -0.0131 89  PRO B N   
3074 C CA  . PRO B 77  ? 0.1825 0.2982 0.1681 0.0716  -0.0272 -0.0124 89  PRO B CA  
3075 C C   . PRO B 77  ? 0.1657 0.2685 0.1540 0.0701  -0.0303 -0.0150 89  PRO B C   
3076 O O   . PRO B 77  ? 0.1876 0.2807 0.1791 0.0684  -0.0299 -0.0143 89  PRO B O   
3077 C CB  . PRO B 77  ? 0.1865 0.3044 0.1712 0.0705  -0.0237 -0.0030 89  PRO B CB  
3078 C CG  . PRO B 77  ? 0.1863 0.2980 0.1736 0.0684  -0.0204 0.0008  89  PRO B CG  
3079 C CD  . PRO B 77  ? 0.1622 0.2779 0.1501 0.0696  -0.0209 -0.0051 89  PRO B CD  
3080 N N   . SER B 78  ? 0.2011 0.3046 0.1879 0.0706  -0.0335 -0.0183 90  SER B N   
3081 C CA  . SER B 78  ? 0.2075 0.2996 0.1965 0.0690  -0.0363 -0.0200 90  SER B CA  
3082 C C   . SER B 78  ? 0.1989 0.2831 0.1900 0.0666  -0.0342 -0.0122 90  SER B C   
3083 O O   . SER B 78  ? 0.1837 0.2726 0.1734 0.0666  -0.0323 -0.0059 90  SER B O   
3084 C CB  . SER B 78  ? 0.2579 0.3544 0.2444 0.0695  -0.0395 -0.0236 90  SER B CB  
3085 O OG  . SER B 78  ? 0.2828 0.3832 0.2674 0.0711  -0.0417 -0.0322 90  SER B OG  
3086 N N   . MET B 79  ? 0.2032 0.2753 0.1975 0.0647  -0.0345 -0.0125 91  MET B N   
3087 C CA  . MET B 79  ? 0.1799 0.2436 0.1760 0.0621  -0.0319 -0.0057 91  MET B CA  
3088 C C   . MET B 79  ? 0.2056 0.2565 0.2046 0.0600  -0.0343 -0.0076 91  MET B C   
3089 O O   . MET B 79  ? 0.2279 0.2746 0.2282 0.0602  -0.0371 -0.0137 91  MET B O   
3090 C CB  . MET B 79  ? 0.1732 0.2363 0.1703 0.0608  -0.0281 -0.0023 91  MET B CB  
3091 C CG  . MET B 79  ? 0.1908 0.2652 0.1854 0.0622  -0.0245 0.0020  91  MET B CG  
3092 S SD  . MET B 79  ? 0.2064 0.2801 0.2021 0.0601  -0.0203 0.0050  91  MET B SD  
3093 C CE  . MET B 79  ? 0.1844 0.2614 0.1813 0.0619  -0.0234 -0.0037 91  MET B CE  
3094 N N   . SER B 80  ? 0.1878 0.2321 0.1876 0.0581  -0.0329 -0.0021 92  SER B N   
3095 C CA  . SER B 80  ? 0.2082 0.2394 0.2108 0.0553  -0.0335 -0.0019 92  SER B CA  
3096 C C   . SER B 80  ? 0.1418 0.1676 0.1455 0.0528  -0.0294 0.0027  92  SER B C   
3097 O O   . SER B 80  ? 0.1751 0.2060 0.1775 0.0529  -0.0256 0.0074  92  SER B O   
3098 C CB  . SER B 80  ? 0.1777 0.2049 0.1806 0.0547  -0.0342 0.0013  92  SER B CB  
3099 O OG  . SER B 80  ? 0.1704 0.1995 0.1726 0.0546  -0.0299 0.0091  92  SER B OG  
3100 N N   . GLY B 81  ? 0.1775 0.1928 0.1835 0.0501  -0.0302 0.0014  93  GLY B N   
3101 C CA  . GLY B 81  ? 0.1257 0.1350 0.1325 0.0468  -0.0261 0.0060  93  GLY B CA  
3102 C C   . GLY B 81  ? 0.1542 0.1680 0.1609 0.0461  -0.0241 0.0056  93  GLY B C   
3103 O O   . GLY B 81  ? 0.1718 0.1819 0.1784 0.0430  -0.0202 0.0099  93  GLY B O   
3104 N N   . SER B 82  ? 0.1478 0.1696 0.1544 0.0488  -0.0264 0.0007  94  SER B N   
3105 C CA  . SER B 82  ? 0.1391 0.1662 0.1460 0.0484  -0.0246 0.0004  94  SER B CA  
3106 C C   . SER B 82  ? 0.1487 0.1682 0.1582 0.0453  -0.0255 -0.0012 94  SER B C   
3107 O O   . SER B 82  ? 0.1598 0.1711 0.1710 0.0444  -0.0282 -0.0033 94  SER B O   
3108 C CB  . SER B 82  ? 0.1724 0.2102 0.1785 0.0525  -0.0267 -0.0046 94  SER B CB  
3109 O OG  . SER B 82  ? 0.1386 0.1851 0.1418 0.0548  -0.0255 -0.0028 94  SER B OG  
3110 N N   . CYS B 83  ? 0.1429 0.1661 0.1529 0.0437  -0.0231 0.0000  95  CYS B N   
3111 C CA  . CYS B 83  ? 0.1542 0.1719 0.1666 0.0402  -0.0234 -0.0005 95  CYS B CA  
3112 C C   . CYS B 83  ? 0.1628 0.1892 0.1768 0.0423  -0.0247 -0.0040 95  CYS B C   
3113 O O   . CYS B 83  ? 0.1859 0.2214 0.1989 0.0430  -0.0222 -0.0027 95  CYS B O   
3114 C CB  . CYS B 83  ? 0.1518 0.1654 0.1632 0.0351  -0.0187 0.0051  95  CYS B CB  
3115 S SG  . CYS B 83  ? 0.1936 0.2014 0.2073 0.0297  -0.0187 0.0049  95  CYS B SG  
3116 N N   . ALA B 84  ? 0.1573 0.1812 0.1739 0.0437  -0.0285 -0.0084 96  ALA B N   
3117 C CA  . ALA B 84  ? 0.1860 0.2182 0.2044 0.0470  -0.0300 -0.0123 96  ALA B CA  
3118 C C   . ALA B 84  ? 0.2213 0.2504 0.2433 0.0453  -0.0317 -0.0133 96  ALA B C   
3119 O O   . ALA B 84  ? 0.1790 0.1984 0.2020 0.0425  -0.0331 -0.0128 96  ALA B O   
3120 C CB  . ALA B 84  ? 0.1866 0.2212 0.2047 0.0523  -0.0331 -0.0176 96  ALA B CB  
3121 N N   . VAL B 85  ? 0.1995 0.2375 0.2234 0.0470  -0.0314 -0.0145 97  VAL B N   
3122 C CA  . VAL B 85  ? 0.1978 0.2358 0.2255 0.0460  -0.0329 -0.0151 97  VAL B CA  
3123 C C   . VAL B 85  ? 0.2326 0.2784 0.2628 0.0518  -0.0346 -0.0194 97  VAL B C   
3124 O O   . VAL B 85  ? 0.2248 0.2779 0.2534 0.0555  -0.0337 -0.0213 97  VAL B O   
3125 C CB  . VAL B 85  ? 0.2212 0.2632 0.2493 0.0409  -0.0299 -0.0108 97  VAL B CB  
3126 C CG1 . VAL B 85  ? 0.2190 0.2542 0.2440 0.0355  -0.0270 -0.0066 97  VAL B CG1 
3127 C CG2 . VAL B 85  ? 0.2240 0.2791 0.2520 0.0429  -0.0276 -0.0106 97  VAL B CG2 
3128 N N   . CYS B 86  ? 0.2231 0.2672 0.2570 0.0525  -0.0369 -0.0207 98  CYS B N   
3129 C CA  . CYS B 86  ? 0.2096 0.2614 0.2467 0.0577  -0.0379 -0.0239 98  CYS B CA  
3130 C C   . CYS B 86  ? 0.2124 0.2700 0.2530 0.0552  -0.0374 -0.0210 98  CYS B C   
3131 O O   . CYS B 86  ? 0.2265 0.2779 0.2688 0.0517  -0.0388 -0.0191 98  CYS B O   
3132 C CB  . CYS B 86  ? 0.2496 0.2945 0.2886 0.0620  -0.0414 -0.0286 98  CYS B CB  
3133 S SG  . CYS B 86  ? 0.3187 0.3718 0.3621 0.0689  -0.0421 -0.0324 98  CYS B SG  
3134 N N   . VAL B 87  ? 0.2109 0.2806 0.2524 0.0568  -0.0353 -0.0204 99  VAL B N   
3135 C CA  . VAL B 87  ? 0.2974 0.3749 0.3425 0.0548  -0.0347 -0.0177 99  VAL B CA  
3136 C C   . VAL B 87  ? 0.2739 0.3618 0.3222 0.0614  -0.0348 -0.0204 99  VAL B C   
3137 O O   . VAL B 87  ? 0.2572 0.3524 0.3037 0.0642  -0.0328 -0.0219 99  VAL B O   
3138 C CB  . VAL B 87  ? 0.2843 0.3672 0.3271 0.0487  -0.0312 -0.0132 99  VAL B CB  
3139 C CG1 . VAL B 87  ? 0.3046 0.3973 0.3513 0.0465  -0.0308 -0.0106 99  VAL B CG1 
3140 C CG2 . VAL B 87  ? 0.2807 0.3524 0.3202 0.0424  -0.0305 -0.0105 99  VAL B CG2 
3141 N N   . ASP B 88  ? 0.3262 0.4151 0.3795 0.0639  -0.0369 -0.0209 100 ASP B N   
3142 C CA  . ASP B 88  ? 0.3065 0.4047 0.3636 0.0706  -0.0368 -0.0234 100 ASP B CA  
3143 C C   . ASP B 88  ? 0.3265 0.4221 0.3816 0.0768  -0.0369 -0.0289 100 ASP B C   
3144 O O   . ASP B 88  ? 0.3439 0.4488 0.3995 0.0814  -0.0352 -0.0311 100 ASP B O   
3145 C CB  . ASP B 88  ? 0.3848 0.4981 0.4430 0.0696  -0.0340 -0.0206 100 ASP B CB  
3146 C CG  . ASP B 88  ? 0.4130 0.5307 0.4738 0.0639  -0.0340 -0.0157 100 ASP B CG  
3147 O OD1 . ASP B 88  ? 0.4264 0.5418 0.4913 0.0647  -0.0365 -0.0150 100 ASP B OD1 
3148 O OD2 . ASP B 88  ? 0.4330 0.5565 0.4917 0.0583  -0.0316 -0.0124 100 ASP B OD2 
3149 N N   . ARG B 89  ? 0.3241 0.4073 0.3767 0.0766  -0.0388 -0.0313 101 ARG B N   
3150 C CA  . ARG B 89  ? 0.3385 0.4182 0.3883 0.0812  -0.0391 -0.0367 101 ARG B CA  
3151 C C   . ARG B 89  ? 0.3140 0.4014 0.3595 0.0811  -0.0363 -0.0371 101 ARG B C   
3152 O O   . ARG B 89  ? 0.2997 0.3899 0.3435 0.0857  -0.0357 -0.0416 101 ARG B O   
3153 C CB  . ARG B 89  ? 0.3661 0.4472 0.4198 0.0884  -0.0397 -0.0411 101 ARG B CB  
3154 C CG  . ARG B 89  ? 0.3672 0.4368 0.4237 0.0895  -0.0427 -0.0423 101 ARG B CG  
3155 C CD  . ARG B 89  ? 0.4064 0.4638 0.4586 0.0884  -0.0443 -0.0457 101 ARG B CD  
3156 N NE  . ARG B 89  ? 0.4239 0.4811 0.4731 0.0924  -0.0432 -0.0514 101 ARG B NE  
3157 C CZ  . ARG B 89  ? 0.4474 0.5003 0.4973 0.0955  -0.0429 -0.0548 101 ARG B CZ  
3158 N NH1 . ARG B 89  ? 0.4393 0.4881 0.4930 0.0954  -0.0434 -0.0526 101 ARG B NH1 
3159 N NH2 . ARG B 89  ? 0.5195 0.5725 0.5662 0.0987  -0.0419 -0.0603 101 ARG B NH2 
3160 N N   . VAL B 90  ? 0.2593 0.3499 0.3027 0.0756  -0.0345 -0.0323 102 VAL B N   
3161 C CA  . VAL B 90  ? 0.2394 0.3352 0.2782 0.0745  -0.0320 -0.0316 102 VAL B CA  
3162 C C   . VAL B 90  ? 0.2604 0.3462 0.2955 0.0698  -0.0324 -0.0294 102 VAL B C   
3163 O O   . VAL B 90  ? 0.2188 0.2985 0.2547 0.0649  -0.0328 -0.0258 102 VAL B O   
3164 C CB  . VAL B 90  ? 0.3019 0.4098 0.3412 0.0723  -0.0289 -0.0276 102 VAL B CB  
3165 C CG1 . VAL B 90  ? 0.2660 0.3778 0.3003 0.0705  -0.0262 -0.0260 102 VAL B CG1 
3166 C CG2 . VAL B 90  ? 0.2802 0.3989 0.3231 0.0777  -0.0283 -0.0301 102 VAL B CG2 
3167 N N   . LEU B 91  ? 0.2119 0.2963 0.2430 0.0713  -0.0323 -0.0316 103 LEU B N   
3168 C CA  . LEU B 91  ? 0.2346 0.3104 0.2623 0.0676  -0.0325 -0.0294 103 LEU B CA  
3169 C C   . LEU B 91  ? 0.2181 0.2998 0.2427 0.0644  -0.0290 -0.0248 103 LEU B C   
3170 O O   . LEU B 91  ? 0.2323 0.3242 0.2553 0.0668  -0.0270 -0.0253 103 LEU B O   
3171 C CB  . LEU B 91  ? 0.2272 0.2984 0.2525 0.0707  -0.0345 -0.0340 103 LEU B CB  
3172 C CG  . LEU B 91  ? 0.2790 0.3455 0.3068 0.0749  -0.0374 -0.0397 103 LEU B CG  
3173 C CD1 . LEU B 91  ? 0.3033 0.3647 0.3278 0.0763  -0.0391 -0.0437 103 LEU B CD1 
3174 C CD2 . LEU B 91  ? 0.2752 0.3329 0.3068 0.0728  -0.0395 -0.0383 103 LEU B CD2 
3175 N N   . TYR B 92  ? 0.1689 0.2438 0.1924 0.0591  -0.0280 -0.0202 104 TYR B N   
3176 C CA  . TYR B 92  ? 0.1931 0.2706 0.2134 0.0557  -0.0244 -0.0153 104 TYR B CA  
3177 C C   . TYR B 92  ? 0.1948 0.2625 0.2125 0.0538  -0.0248 -0.0136 104 TYR B C   
3178 O O   . TYR B 92  ? 0.2363 0.2939 0.2553 0.0519  -0.0268 -0.0139 104 TYR B O   
3179 C CB  . TYR B 92  ? 0.1814 0.2599 0.2030 0.0504  -0.0219 -0.0108 104 TYR B CB  
3180 C CG  . TYR B 92  ? 0.1985 0.2874 0.2231 0.0515  -0.0215 -0.0116 104 TYR B CG  
3181 C CD1 . TYR B 92  ? 0.2187 0.3196 0.2423 0.0529  -0.0187 -0.0108 104 TYR B CD1 
3182 C CD2 . TYR B 92  ? 0.2310 0.3184 0.2598 0.0512  -0.0237 -0.0128 104 TYR B CD2 
3183 C CE1 . TYR B 92  ? 0.2241 0.3352 0.2508 0.0540  -0.0182 -0.0113 104 TYR B CE1 
3184 C CE2 . TYR B 92  ? 0.2572 0.3549 0.2892 0.0525  -0.0233 -0.0131 104 TYR B CE2 
3185 C CZ  . TYR B 92  ? 0.2626 0.3723 0.2937 0.0538  -0.0205 -0.0124 104 TYR B CZ  
3186 O OH  . TYR B 92  ? 0.2716 0.3922 0.3063 0.0551  -0.0201 -0.0125 104 TYR B OH  
3187 N N   . LEU B 93  ? 0.1747 0.2461 0.1890 0.0542  -0.0226 -0.0114 105 LEU B N   
3188 C CA  . LEU B 93  ? 0.1501 0.2144 0.1619 0.0535  -0.0229 -0.0098 105 LEU B CA  
3189 C C   . LEU B 93  ? 0.1478 0.2139 0.1570 0.0507  -0.0185 -0.0036 105 LEU B C   
3190 O O   . LEU B 93  ? 0.1852 0.2613 0.1930 0.0517  -0.0160 -0.0023 105 LEU B O   
3191 C CB  . LEU B 93  ? 0.1650 0.2331 0.1751 0.0583  -0.0253 -0.0143 105 LEU B CB  
3192 C CG  . LEU B 93  ? 0.1835 0.2470 0.1912 0.0587  -0.0264 -0.0137 105 LEU B CG  
3193 C CD1 . LEU B 93  ? 0.2260 0.2781 0.2356 0.0576  -0.0296 -0.0157 105 LEU B CD1 
3194 C CD2 . LEU B 93  ? 0.1833 0.2556 0.1888 0.0631  -0.0278 -0.0180 105 LEU B CD2 
3195 N N   . PHE B 94  ? 0.1721 0.2284 0.1807 0.0470  -0.0172 0.0003  106 PHE B N   
3196 C CA  . PHE B 94  ? 0.1463 0.2024 0.1525 0.0442  -0.0125 0.0065  106 PHE B CA  
3197 C C   . PHE B 94  ? 0.1863 0.2354 0.1910 0.0444  -0.0124 0.0090  106 PHE B C   
3198 O O   . PHE B 94  ? 0.1651 0.2053 0.1711 0.0437  -0.0150 0.0074  106 PHE B O   
3199 C CB  . PHE B 94  ? 0.1568 0.2077 0.1639 0.0384  -0.0093 0.0100  106 PHE B CB  
3200 C CG  . PHE B 94  ? 0.1531 0.2001 0.1577 0.0353  -0.0043 0.0163  106 PHE B CG  
3201 C CD1 . PHE B 94  ? 0.2152 0.2705 0.2179 0.0354  -0.0005 0.0196  106 PHE B CD1 
3202 C CD2 . PHE B 94  ? 0.1700 0.2052 0.1742 0.0328  -0.0033 0.0189  106 PHE B CD2 
3203 C CE1 . PHE B 94  ? 0.2242 0.2754 0.2246 0.0328  0.0045  0.0257  106 PHE B CE1 
3204 C CE2 . PHE B 94  ? 0.2078 0.2389 0.2099 0.0305  0.0018  0.0249  106 PHE B CE2 
3205 C CZ  . PHE B 94  ? 0.2021 0.2410 0.2023 0.0305  0.0057  0.0284  106 PHE B CZ  
3206 N N   . GLY B 95  ? 0.1757 0.2291 0.1778 0.0452  -0.0093 0.0134  107 GLY B N   
3207 C CA  . GLY B 95  ? 0.2024 0.2495 0.2033 0.0451  -0.0082 0.0173  107 GLY B CA  
3208 C C   . GLY B 95  ? 0.1621 0.2095 0.1631 0.0486  -0.0128 0.0136  107 GLY B C   
3209 O O   . GLY B 95  ? 0.1561 0.2093 0.1574 0.0516  -0.0164 0.0079  107 GLY B O   
3210 N N   . GLY B 96  ? 0.1541 0.1945 0.1548 0.0481  -0.0123 0.0168  108 GLY B N   
3211 C CA  . GLY B 96  ? 0.1898 0.2306 0.1903 0.0508  -0.0161 0.0144  108 GLY B CA  
3212 C C   . GLY B 96  ? 0.1898 0.2351 0.1884 0.0526  -0.0140 0.0199  108 GLY B C   
3213 O O   . GLY B 96  ? 0.1564 0.2035 0.1539 0.0519  -0.0093 0.0259  108 GLY B O   
3214 N N   . HIS B 97  ? 0.1785 0.2260 0.1767 0.0549  -0.0175 0.0177  109 HIS B N   
3215 C CA  . HIS B 97  ? 0.1826 0.2357 0.1792 0.0569  -0.0164 0.0225  109 HIS B CA  
3216 C C   . HIS B 97  ? 0.1694 0.2330 0.1644 0.0600  -0.0206 0.0175  109 HIS B C   
3217 O O   . HIS B 97  ? 0.1813 0.2419 0.1771 0.0601  -0.0249 0.0115  109 HIS B O   
3218 C CB  . HIS B 97  ? 0.2038 0.2471 0.2021 0.0556  -0.0160 0.0261  109 HIS B CB  
3219 C CG  . HIS B 97  ? 0.2493 0.2982 0.2465 0.0578  -0.0143 0.0324  109 HIS B CG  
3220 N ND1 . HIS B 97  ? 0.2363 0.2920 0.2329 0.0600  -0.0180 0.0307  109 HIS B ND1 
3221 C CD2 . HIS B 97  ? 0.2333 0.2820 0.2302 0.0580  -0.0091 0.0406  109 HIS B CD2 
3222 C CE1 . HIS B 97  ? 0.2443 0.3047 0.2405 0.0617  -0.0154 0.0379  109 HIS B CE1 
3223 N NE2 . HIS B 97  ? 0.2407 0.2966 0.2371 0.0607  -0.0099 0.0441  109 HIS B NE2 
3224 N N   . HIS B 98  ? 0.2463 0.3221 0.2387 0.0623  -0.0193 0.0200  110 HIS B N   
3225 C CA  . HIS B 98  ? 0.2283 0.3154 0.2184 0.0649  -0.0228 0.0155  110 HIS B CA  
3226 C C   . HIS B 98  ? 0.2379 0.3321 0.2267 0.0664  -0.0221 0.0213  110 HIS B C   
3227 O O   . HIS B 98  ? 0.1979 0.2866 0.1880 0.0657  -0.0193 0.0283  110 HIS B O   
3228 C CB  . HIS B 98  ? 0.2104 0.3075 0.1986 0.0663  -0.0221 0.0123  110 HIS B CB  
3229 C CG  . HIS B 98  ? 0.2409 0.3420 0.2283 0.0661  -0.0171 0.0191  110 HIS B CG  
3230 N ND1 . HIS B 98  ? 0.2241 0.3346 0.2091 0.0678  -0.0148 0.0252  110 HIS B ND1 
3231 C CD2 . HIS B 98  ? 0.2161 0.3132 0.2045 0.0643  -0.0138 0.0208  110 HIS B CD2 
3232 C CE1 . HIS B 98  ? 0.2268 0.3383 0.2116 0.0670  -0.0101 0.0305  110 HIS B CE1 
3233 N NE2 . HIS B 98  ? 0.2105 0.3138 0.1972 0.0647  -0.0094 0.0278  110 HIS B NE2 
3234 N N   . SER B 99  ? 0.2309 0.3376 0.2169 0.0685  -0.0247 0.0185  111 SER B N   
3235 C CA  . SER B 99  ? 0.2658 0.3807 0.2504 0.0698  -0.0250 0.0233  111 SER B CA  
3236 C C   . SER B 99  ? 0.2548 0.3738 0.2391 0.0709  -0.0199 0.0334  111 SER B C   
3237 O O   . SER B 99  ? 0.2909 0.4138 0.2753 0.0720  -0.0193 0.0395  111 SER B O   
3238 C CB  . SER B 99  ? 0.2339 0.3627 0.2150 0.0714  -0.0284 0.0179  111 SER B CB  
3239 O OG  . SER B 99  ? 0.2973 0.4347 0.2760 0.0725  -0.0267 0.0164  111 SER B OG  
3240 N N   . ARG B 100 ? 0.2231 0.3414 0.2071 0.0705  -0.0161 0.0356  112 ARG B N   
3241 C CA  . ARG B 100 ? 0.2068 0.3276 0.1904 0.0712  -0.0107 0.0451  112 ARG B CA  
3242 C C   . ARG B 100 ? 0.2730 0.3797 0.2590 0.0687  -0.0064 0.0487  112 ARG B C   
3243 O O   . ARG B 100 ? 0.2869 0.3944 0.2724 0.0685  -0.0015 0.0544  112 ARG B O   
3244 C CB  . ARG B 100 ? 0.2767 0.4112 0.2572 0.0728  -0.0094 0.0453  112 ARG B CB  
3245 C CG  . ARG B 100 ? 0.2957 0.4441 0.2732 0.0747  -0.0138 0.0402  112 ARG B CG  
3246 C CD  . ARG B 100 ? 0.3319 0.4944 0.3068 0.0770  -0.0119 0.0473  112 ARG B CD  
3247 N NE  . ARG B 100 ? 0.4061 0.5710 0.3804 0.0772  -0.0068 0.0532  112 ARG B NE  
3248 C CZ  . ARG B 100 ? 0.3233 0.4958 0.2952 0.0775  -0.0062 0.0499  112 ARG B CZ  
3249 N NH1 . ARG B 100 ? 0.3404 0.5191 0.3104 0.0778  -0.0101 0.0408  112 ARG B NH1 
3250 N NH2 . ARG B 100 ? 0.3119 0.4855 0.2834 0.0773  -0.0012 0.0559  112 ARG B NH2 
3251 N N   . GLY B 101 ? 0.2256 0.3196 0.2142 0.0665  -0.0080 0.0451  113 GLY B N   
3252 C CA  . GLY B 101 ? 0.2280 0.3084 0.2187 0.0637  -0.0039 0.0489  113 GLY B CA  
3253 C C   . GLY B 101 ? 0.2247 0.2983 0.2162 0.0609  -0.0043 0.0432  113 GLY B C   
3254 O O   . GLY B 101 ? 0.1881 0.2649 0.1794 0.0612  -0.0085 0.0356  113 GLY B O   
3255 N N   . ASN B 102 ? 0.2319 0.2961 0.2243 0.0580  0.0003  0.0472  114 ASN B N   
3256 C CA  . ASN B 102 ? 0.2043 0.2615 0.1979 0.0547  0.0003  0.0428  114 ASN B CA  
3257 C C   . ASN B 102 ? 0.2250 0.2909 0.2170 0.0547  0.0019  0.0419  114 ASN B C   
3258 O O   . ASN B 102 ? 0.2077 0.2831 0.1977 0.0566  0.0044  0.0460  114 ASN B O   
3259 C CB  . ASN B 102 ? 0.2254 0.2686 0.2203 0.0508  0.0047  0.0471  114 ASN B CB  
3260 C CG  . ASN B 102 ? 0.2398 0.2728 0.2367 0.0502  0.0028  0.0465  114 ASN B CG  
3261 O OD1 . ASN B 102 ? 0.2484 0.2753 0.2456 0.0500  0.0063  0.0525  114 ASN B OD1 
3262 N ND2 . ASN B 102 ? 0.1985 0.2292 0.1967 0.0498  -0.0024 0.0395  114 ASN B ND2 
3263 N N   . THR B 103 ? 0.2007 0.2637 0.1939 0.0524  0.0006  0.0367  115 THR B N   
3264 C CA  . THR B 103 ? 0.1942 0.2654 0.1865 0.0522  0.0018  0.0352  115 THR B CA  
3265 C C   . THR B 103 ? 0.1936 0.2567 0.1876 0.0477  0.0035  0.0343  115 THR B C   
3266 O O   . THR B 103 ? 0.2044 0.2566 0.2002 0.0452  0.0024  0.0329  115 THR B O   
3267 C CB  . THR B 103 ? 0.2216 0.3030 0.2135 0.0555  -0.0030 0.0280  115 THR B CB  
3268 O OG1 . THR B 103 ? 0.2186 0.3094 0.2096 0.0558  -0.0013 0.0273  115 THR B OG1 
3269 C CG2 . THR B 103 ? 0.2451 0.3195 0.2395 0.0548  -0.0074 0.0212  115 THR B CG2 
3270 N N   . ASN B 104 ? 0.1801 0.2494 0.1733 0.0465  0.0063  0.0353  116 ASN B N   
3271 C CA  . ASN B 104 ? 0.2286 0.2943 0.2233 0.0423  0.0075  0.0337  116 ASN B CA  
3272 C C   . ASN B 104 ? 0.2074 0.2848 0.2024 0.0441  0.0056  0.0291  116 ASN B C   
3273 O O   . ASN B 104 ? 0.2459 0.3247 0.2416 0.0410  0.0076  0.0292  116 ASN B O   
3274 C CB  . ASN B 104 ? 0.2042 0.2645 0.1977 0.0379  0.0139  0.0402  116 ASN B CB  
3275 C CG  . ASN B 104 ? 0.2323 0.3022 0.2234 0.0395  0.0177  0.0449  116 ASN B CG  
3276 O OD1 . ASN B 104 ? 0.2539 0.3357 0.2441 0.0434  0.0155  0.0429  116 ASN B OD1 
3277 N ND2 . ASN B 104 ? 0.2622 0.3266 0.2520 0.0361  0.0236  0.0512  116 ASN B ND2 
3278 N N   . LYS B 105 ? 0.2061 0.2923 0.2005 0.0488  0.0021  0.0252  117 LYS B N   
3279 C CA  . LYS B 105 ? 0.2268 0.3236 0.2217 0.0511  0.0001  0.0201  117 LYS B CA  
3280 C C   . LYS B 105 ? 0.1745 0.2666 0.1725 0.0505  -0.0035 0.0143  117 LYS B C   
3281 O O   . LYS B 105 ? 0.1838 0.2662 0.1832 0.0499  -0.0061 0.0125  117 LYS B O   
3282 C CB  . LYS B 105 ? 0.1842 0.2908 0.1769 0.0561  -0.0023 0.0173  117 LYS B CB  
3283 N N   . PHE B 106 ? 0.1788 0.2783 0.1782 0.0507  -0.0036 0.0116  118 PHE B N   
3284 C CA  . PHE B 106 ? 0.2234 0.3203 0.2262 0.0502  -0.0064 0.0069  118 PHE B CA  
3285 C C   . PHE B 106 ? 0.1726 0.2791 0.1762 0.0553  -0.0092 0.0008  118 PHE B C   
3286 O O   . PHE B 106 ? 0.2057 0.3234 0.2080 0.0571  -0.0074 0.0009  118 PHE B O   
3287 C CB  . PHE B 106 ? 0.1654 0.2628 0.1696 0.0456  -0.0034 0.0097  118 PHE B CB  
3288 C CG  . PHE B 106 ? 0.2211 0.3161 0.2291 0.0445  -0.0061 0.0061  118 PHE B CG  
3289 C CD1 . PHE B 106 ? 0.2058 0.2890 0.2153 0.0411  -0.0073 0.0064  118 PHE B CD1 
3290 C CD2 . PHE B 106 ? 0.2276 0.3326 0.2378 0.0470  -0.0072 0.0027  118 PHE B CD2 
3291 C CE1 . PHE B 106 ? 0.2229 0.3045 0.2358 0.0401  -0.0098 0.0036  118 PHE B CE1 
3292 C CE2 . PHE B 106 ? 0.2209 0.3243 0.2349 0.0463  -0.0095 0.0000  118 PHE B CE2 
3293 C CZ  . PHE B 106 ? 0.1991 0.2910 0.2145 0.0428  -0.0109 0.0006  118 PHE B CZ  
3294 N N   . TYR B 107 ? 0.1761 0.2779 0.1817 0.0574  -0.0133 -0.0044 119 TYR B N   
3295 C CA  . TYR B 107 ? 0.1694 0.2785 0.1757 0.0624  -0.0158 -0.0107 119 TYR B CA  
3296 C C   . TYR B 107 ? 0.2016 0.3084 0.2122 0.0627  -0.0179 -0.0141 119 TYR B C   
3297 O O   . TYR B 107 ? 0.2085 0.3064 0.2213 0.0594  -0.0186 -0.0127 119 TYR B O   
3298 C CB  . TYR B 107 ? 0.1835 0.2899 0.1880 0.0656  -0.0188 -0.0146 119 TYR B CB  
3299 C CG  . TYR B 107 ? 0.2260 0.3362 0.2264 0.0658  -0.0173 -0.0113 119 TYR B CG  
3300 C CD1 . TYR B 107 ? 0.2241 0.3267 0.2236 0.0628  -0.0162 -0.0060 119 TYR B CD1 
3301 C CD2 . TYR B 107 ? 0.2199 0.3418 0.2176 0.0691  -0.0167 -0.0132 119 TYR B CD2 
3302 C CE1 . TYR B 107 ? 0.1977 0.3041 0.1939 0.0633  -0.0146 -0.0023 119 TYR B CE1 
3303 C CE2 . TYR B 107 ? 0.1949 0.3211 0.1888 0.0693  -0.0154 -0.0096 119 TYR B CE2 
3304 C CZ  . TYR B 107 ? 0.2059 0.3245 0.1993 0.0665  -0.0143 -0.0039 119 TYR B CZ  
3305 O OH  . TYR B 107 ? 0.1947 0.3181 0.1849 0.0671  -0.0129 0.0003  119 TYR B OH  
3306 N N   . MET B 108 ? 0.2159 0.3311 0.2277 0.0669  -0.0186 -0.0187 120 MET B N   
3307 C CA  . MET B 108 ? 0.1943 0.3087 0.2104 0.0685  -0.0206 -0.0221 120 MET B CA  
3308 C C   . MET B 108 ? 0.2336 0.3494 0.2498 0.0741  -0.0231 -0.0290 120 MET B C   
3309 O O   . MET B 108 ? 0.2678 0.3910 0.2809 0.0770  -0.0222 -0.0312 120 MET B O   
3310 C CB  . MET B 108 ? 0.2631 0.3875 0.2814 0.0677  -0.0181 -0.0200 120 MET B CB  
3311 C CG  . MET B 108 ? 0.2761 0.4030 0.2991 0.0707  -0.0198 -0.0236 120 MET B CG  
3312 S SD  . MET B 108 ? 0.4016 0.5423 0.4272 0.0697  -0.0167 -0.0208 120 MET B SD  
3313 C CE  . MET B 108 ? 0.3500 0.5032 0.3718 0.0735  -0.0141 -0.0223 120 MET B CE  
3314 N N   . LEU B 109 ? 0.2133 0.3218 0.2327 0.0755  -0.0259 -0.0324 121 LEU B N   
3315 C CA  . LEU B 109 ? 0.2596 0.3680 0.2794 0.0808  -0.0279 -0.0393 121 LEU B CA  
3316 C C   . LEU B 109 ? 0.2763 0.3843 0.3014 0.0830  -0.0289 -0.0411 121 LEU B C   
3317 O O   . LEU B 109 ? 0.2722 0.3708 0.3001 0.0815  -0.0311 -0.0406 121 LEU B O   
3318 C CB  . LEU B 109 ? 0.2471 0.3450 0.2651 0.0808  -0.0308 -0.0421 121 LEU B CB  
3319 C CG  . LEU B 109 ? 0.3231 0.4220 0.3407 0.0859  -0.0321 -0.0496 121 LEU B CG  
3320 C CD1 . LEU B 109 ? 0.3042 0.4093 0.3165 0.0871  -0.0314 -0.0518 121 LEU B CD1 
3321 C CD2 . LEU B 109 ? 0.3682 0.4548 0.3877 0.0864  -0.0354 -0.0530 121 LEU B CD2 
3322 N N   . ASP B 110 ? 0.3019 0.4203 0.3284 0.0868  -0.0272 -0.0432 122 ASP B N   
3323 C CA  . ASP B 110 ? 0.3149 0.4347 0.3469 0.0898  -0.0278 -0.0448 122 ASP B CA  
3324 C C   . ASP B 110 ? 0.3374 0.4497 0.3702 0.0944  -0.0301 -0.0512 122 ASP B C   
3325 O O   . ASP B 110 ? 0.4088 0.5244 0.4392 0.0984  -0.0294 -0.0563 122 ASP B O   
3326 C CB  . ASP B 110 ? 0.3133 0.4474 0.3465 0.0925  -0.0250 -0.0446 122 ASP B CB  
3327 C CG  . ASP B 110 ? 0.3966 0.5341 0.4360 0.0941  -0.0251 -0.0435 122 ASP B CG  
3328 O OD1 . ASP B 110 ? 0.3622 0.4910 0.4048 0.0955  -0.0275 -0.0451 122 ASP B OD1 
3329 O OD2 . ASP B 110 ? 0.3887 0.5378 0.4298 0.0938  -0.0227 -0.0407 122 ASP B OD2 
3330 N N   . SER B 111 ? 0.3454 0.4473 0.3813 0.0936  -0.0326 -0.0509 123 SER B N   
3331 C CA  . SER B 111 ? 0.4295 0.5222 0.4663 0.0972  -0.0348 -0.0565 123 SER B CA  
3332 C C   . SER B 111 ? 0.4386 0.5321 0.4812 0.1017  -0.0349 -0.0581 123 SER B C   
3333 O O   . SER B 111 ? 0.4666 0.5504 0.5104 0.1038  -0.0366 -0.0614 123 SER B O   
3334 C CB  . SER B 111 ? 0.4312 0.5106 0.4671 0.0932  -0.0376 -0.0554 123 SER B CB  
3335 O OG  . SER B 111 ? 0.4294 0.5051 0.4692 0.0902  -0.0387 -0.0507 123 SER B OG  
3336 N N   . ARG B 112 ? 0.4283 0.5330 0.4740 0.1028  -0.0329 -0.0552 124 ARG B N   
3337 C CA  . ARG B 112 ? 0.4718 0.5771 0.5230 0.1059  -0.0329 -0.0548 124 ARG B CA  
3338 C C   . ARG B 112 ? 0.5380 0.6427 0.5884 0.1109  -0.0313 -0.0603 124 ARG B C   
3339 O O   . ARG B 112 ? 0.5823 0.6802 0.6355 0.1126  -0.0316 -0.0609 124 ARG B O   
3340 C CB  . ARG B 112 ? 0.4187 0.5370 0.4737 0.1049  -0.0313 -0.0496 124 ARG B CB  
3341 C CG  . ARG B 112 ? 0.4377 0.5531 0.4932 0.0980  -0.0327 -0.0435 124 ARG B CG  
3342 C CD  . ARG B 112 ? 0.3959 0.5237 0.4549 0.0961  -0.0311 -0.0385 124 ARG B CD  
3343 N NE  . ARG B 112 ? 0.4056 0.5452 0.4620 0.0964  -0.0280 -0.0384 124 ARG B NE  
3344 C CZ  . ARG B 112 ? 0.3981 0.5434 0.4522 0.0908  -0.0263 -0.0339 124 ARG B CZ  
3345 N NH1 . ARG B 112 ? 0.4400 0.5807 0.4941 0.0842  -0.0271 -0.0293 124 ARG B NH1 
3346 N NH2 . ARG B 112 ? 0.3846 0.5401 0.4361 0.0916  -0.0234 -0.0342 124 ARG B NH2 
3347 N N   . SER B 113 ? 0.5764 0.6879 0.6230 0.1133  -0.0293 -0.0641 125 SER B N   
3348 C CA  . SER B 113 ? 0.5822 0.6927 0.6274 0.1177  -0.0277 -0.0699 125 SER B CA  
3349 C C   . SER B 113 ? 0.5920 0.6978 0.6313 0.1178  -0.0283 -0.0757 125 SER B C   
3350 O O   . SER B 113 ? 0.5882 0.6971 0.6244 0.1156  -0.0289 -0.0749 125 SER B O   
3351 C CB  . SER B 113 ? 0.6086 0.7333 0.6548 0.1208  -0.0243 -0.0696 125 SER B CB  
3352 O OG  . SER B 113 ? 0.6597 0.7948 0.7023 0.1198  -0.0231 -0.0693 125 SER B OG  
3353 N N   . VAL B 117 ? 0.5527 0.6708 0.5635 0.1199  -0.0261 -0.1014 129 VAL B N   
3354 C CA  . VAL B 117 ? 0.5181 0.6351 0.5253 0.1148  -0.0282 -0.0976 129 VAL B CA  
3355 C C   . VAL B 117 ? 0.4985 0.6205 0.5083 0.1118  -0.0280 -0.0885 129 VAL B C   
3356 O O   . VAL B 117 ? 0.4808 0.6139 0.4915 0.1130  -0.0254 -0.0858 129 VAL B O   
3357 C CB  . VAL B 117 ? 0.5529 0.6779 0.5529 0.1138  -0.0275 -0.1011 129 VAL B CB  
3358 C CG1 . VAL B 117 ? 0.4456 0.5757 0.4428 0.1090  -0.0282 -0.0941 129 VAL B CG1 
3359 C CG2 . VAL B 117 ? 0.5815 0.6975 0.5781 0.1136  -0.0292 -0.1086 129 VAL B CG2 
3360 N N   . LEU B 118 ? 0.4862 0.5996 0.4970 0.1076  -0.0304 -0.0839 130 LEU B N   
3361 C CA  . LEU B 118 ? 0.4471 0.5625 0.4605 0.1043  -0.0302 -0.0756 130 LEU B CA  
3362 C C   . LEU B 118 ? 0.4220 0.5463 0.4309 0.1013  -0.0288 -0.0713 130 LEU B C   
3363 O O   . LEU B 118 ? 0.3916 0.5164 0.3956 0.1002  -0.0295 -0.0733 130 LEU B O   
3364 C CB  . LEU B 118 ? 0.4481 0.5506 0.4641 0.1011  -0.0330 -0.0727 130 LEU B CB  
3365 C CG  . LEU B 118 ? 0.4967 0.5922 0.5186 0.1034  -0.0339 -0.0735 130 LEU B CG  
3366 C CD1 . LEU B 118 ? 0.5312 0.6223 0.5536 0.1082  -0.0342 -0.0815 130 LEU B CD1 
3367 C CD2 . LEU B 118 ? 0.4729 0.5571 0.4971 0.0993  -0.0366 -0.0695 130 LEU B CD2 
3368 N N   . GLN B 119 ? 0.3973 0.5291 0.4079 0.0999  -0.0267 -0.0654 131 GLN B N   
3369 C CA  . GLN B 119 ? 0.3846 0.5266 0.3914 0.0979  -0.0245 -0.0612 131 GLN B CA  
3370 C C   . GLN B 119 ? 0.2797 0.4183 0.2874 0.0928  -0.0244 -0.0532 131 GLN B C   
3371 O O   . GLN B 119 ? 0.2818 0.4194 0.2936 0.0915  -0.0238 -0.0497 131 GLN B O   
3372 C CB  . GLN B 119 ? 0.3727 0.5278 0.3802 0.1007  -0.0214 -0.0616 131 GLN B CB  
3373 C CG  . GLN B 119 ? 0.3886 0.5487 0.3942 0.1056  -0.0207 -0.0694 131 GLN B CG  
3374 C CD  . GLN B 119 ? 0.4344 0.6008 0.4334 0.1050  -0.0202 -0.0710 131 GLN B CD  
3375 O OE1 . GLN B 119 ? 0.4653 0.6277 0.4612 0.1059  -0.0218 -0.0767 131 GLN B OE1 
3376 N NE2 . GLN B 119 ? 0.4525 0.6292 0.4492 0.1032  -0.0180 -0.0658 131 GLN B NE2 
3377 N N   . TRP B 120 ? 0.2761 0.4137 0.2798 0.0899  -0.0246 -0.0501 132 TRP B N   
3378 C CA  . TRP B 120 ? 0.2425 0.3773 0.2465 0.0853  -0.0236 -0.0424 132 TRP B CA  
3379 C C   . TRP B 120 ? 0.2200 0.3661 0.2230 0.0844  -0.0199 -0.0377 132 TRP B C   
3380 O O   . TRP B 120 ? 0.2761 0.4330 0.2762 0.0867  -0.0183 -0.0393 132 TRP B O   
3381 C CB  . TRP B 120 ? 0.2594 0.3891 0.2599 0.0830  -0.0248 -0.0403 132 TRP B CB  
3382 C CG  . TRP B 120 ? 0.2687 0.3856 0.2705 0.0822  -0.0282 -0.0428 132 TRP B CG  
3383 C CD1 . TRP B 120 ? 0.2843 0.3980 0.2845 0.0842  -0.0308 -0.0489 132 TRP B CD1 
3384 C CD2 . TRP B 120 ? 0.2592 0.3650 0.2638 0.0788  -0.0292 -0.0390 132 TRP B CD2 
3385 N NE1 . TRP B 120 ? 0.2571 0.3585 0.2592 0.0823  -0.0334 -0.0491 132 TRP B NE1 
3386 C CE2 . TRP B 120 ? 0.2475 0.3439 0.2523 0.0791  -0.0325 -0.0431 132 TRP B CE2 
3387 C CE3 . TRP B 120 ? 0.2346 0.3374 0.2414 0.0752  -0.0275 -0.0329 132 TRP B CE3 
3388 C CZ2 . TRP B 120 ? 0.2333 0.3178 0.2405 0.0762  -0.0342 -0.0410 132 TRP B CZ2 
3389 C CZ3 . TRP B 120 ? 0.2095 0.3005 0.2185 0.0722  -0.0291 -0.0311 132 TRP B CZ3 
3390 C CH2 . TRP B 120 ? 0.2595 0.3416 0.2688 0.0729  -0.0325 -0.0350 132 TRP B CH2 
3391 N N   . GLU B 121 ? 0.2000 0.3438 0.2053 0.0807  -0.0184 -0.0319 133 GLU B N   
3392 C CA  . GLU B 121 ? 0.2041 0.3571 0.2088 0.0788  -0.0147 -0.0266 133 GLU B CA  
3393 C C   . GLU B 121 ? 0.2305 0.3774 0.2339 0.0737  -0.0133 -0.0196 133 GLU B C   
3394 O O   . GLU B 121 ? 0.2289 0.3665 0.2349 0.0704  -0.0139 -0.0173 133 GLU B O   
3395 C CB  . GLU B 121 ? 0.2483 0.4056 0.2575 0.0789  -0.0137 -0.0267 133 GLU B CB  
3396 C CG  . GLU B 121 ? 0.2813 0.4444 0.2924 0.0843  -0.0146 -0.0332 133 GLU B CG  
3397 C CD  . GLU B 121 ? 0.3630 0.5407 0.3722 0.0867  -0.0117 -0.0338 133 GLU B CD  
3398 O OE1 . GLU B 121 ? 0.3931 0.5772 0.4013 0.0837  -0.0088 -0.0283 133 GLU B OE1 
3399 O OE2 . GLU B 121 ? 0.3705 0.5529 0.3792 0.0915  -0.0122 -0.0398 133 GLU B OE2 
3400 N N   . ARG B 122 ? 0.2496 0.4018 0.2490 0.0731  -0.0111 -0.0159 134 ARG B N   
3401 C CA  . ARG B 122 ? 0.2323 0.3798 0.2306 0.0686  -0.0085 -0.0085 134 ARG B CA  
3402 C C   . ARG B 122 ? 0.2475 0.4007 0.2472 0.0658  -0.0050 -0.0046 134 ARG B C   
3403 O O   . ARG B 122 ? 0.2687 0.4339 0.2675 0.0677  -0.0031 -0.0051 134 ARG B O   
3404 C CB  . ARG B 122 ? 0.2115 0.3628 0.2054 0.0692  -0.0074 -0.0055 134 ARG B CB  
3405 C CG  . ARG B 122 ? 0.2075 0.3518 0.2005 0.0652  -0.0048 0.0021  134 ARG B CG  
3406 C CD  . ARG B 122 ? 0.2069 0.3572 0.1957 0.0665  -0.0034 0.0058  134 ARG B CD  
3407 N NE  . ARG B 122 ? 0.2862 0.4492 0.2729 0.0674  -0.0002 0.0079  134 ARG B NE  
3408 C CZ  . ARG B 122 ? 0.2634 0.4381 0.2482 0.0710  -0.0011 0.0036  134 ARG B CZ  
3409 N NH1 . ARG B 122 ? 0.2995 0.4748 0.2840 0.0742  -0.0048 -0.0032 134 ARG B NH1 
3410 N NH2 . ARG B 122 ? 0.2495 0.4355 0.2327 0.0713  0.0021  0.0061  134 ARG B NH2 
3411 N N   . ILE B 123 ? 0.1635 0.3086 0.1653 0.0612  -0.0039 -0.0010 135 ILE B N   
3412 C CA  . ILE B 123 ? 0.2507 0.4005 0.2540 0.0577  -0.0008 0.0023  135 ILE B CA  
3413 C C   . ILE B 123 ? 0.2300 0.3794 0.2303 0.0539  0.0036  0.0093  135 ILE B C   
3414 O O   . ILE B 123 ? 0.2636 0.4026 0.2627 0.0513  0.0043  0.0127  135 ILE B O   
3415 C CB  . ILE B 123 ? 0.2135 0.3556 0.2208 0.0544  -0.0021 0.0017  135 ILE B CB  
3416 C CG1 . ILE B 123 ? 0.2664 0.4074 0.2766 0.0587  -0.0065 -0.0048 135 ILE B CG1 
3417 C CG2 . ILE B 123 ? 0.2596 0.4089 0.2685 0.0510  0.0008  0.0044  135 ILE B CG2 
3418 C CD1 . ILE B 123 ? 0.2767 0.4306 0.2881 0.0634  -0.0066 -0.0088 135 ILE B CD1 
3419 N N   . ASP B 124 ? 0.3266 0.4872 0.3258 0.0536  0.0069  0.0115  136 ASP B N   
3420 C CA  . ASP B 124 ? 0.3201 0.4810 0.3167 0.0496  0.0117  0.0184  136 ASP B CA  
3421 C C   . ASP B 124 ? 0.2839 0.4383 0.2826 0.0433  0.0138  0.0212  136 ASP B C   
3422 O O   . ASP B 124 ? 0.3285 0.4902 0.3283 0.0407  0.0160  0.0223  136 ASP B O   
3423 C CB  . ASP B 124 ? 0.3938 0.5695 0.3887 0.0513  0.0143  0.0195  136 ASP B CB  
3424 C CG  . ASP B 124 ? 0.4826 0.6644 0.4740 0.0561  0.0136  0.0188  136 ASP B CG  
3425 O OD1 . ASP B 124 ? 0.4019 0.5768 0.3922 0.0578  0.0113  0.0180  136 ASP B OD1 
3426 O OD2 . ASP B 124 ? 0.5671 0.7615 0.5568 0.0579  0.0155  0.0192  136 ASP B OD2 
3427 N N   . CYS B 125 ? 0.2369 0.3777 0.2361 0.0405  0.0130  0.0222  137 CYS B N   
3428 C CA  . CYS B 125 ? 0.2826 0.4166 0.2834 0.0342  0.0146  0.0241  137 CYS B CA  
3429 C C   . CYS B 125 ? 0.2434 0.3779 0.2418 0.0291  0.0205  0.0303  137 CYS B C   
3430 O O   . CYS B 125 ? 0.2707 0.4043 0.2660 0.0298  0.0233  0.0344  137 CYS B O   
3431 C CB  . CYS B 125 ? 0.2081 0.3272 0.2095 0.0323  0.0129  0.0239  137 CYS B CB  
3432 S SG  . CYS B 125 ? 0.2634 0.3805 0.2677 0.0375  0.0063  0.0169  137 CYS B SG  
3433 N N   . GLN B 126 ? 0.2379 0.3741 0.2378 0.0237  0.0224  0.0311  138 GLN B N   
3434 C CA  . GLN B 126 ? 0.2657 0.4008 0.2634 0.0176  0.0281  0.0366  138 GLN B CA  
3435 C C   . GLN B 126 ? 0.2864 0.4053 0.2828 0.0124  0.0304  0.0395  138 GLN B C   
3436 O O   . GLN B 126 ? 0.2598 0.3696 0.2577 0.0125  0.0272  0.0370  138 GLN B O   
3437 C CB  . GLN B 126 ? 0.2930 0.4375 0.2928 0.0135  0.0292  0.0359  138 GLN B CB  
3438 C CG  . GLN B 126 ? 0.2950 0.4549 0.2972 0.0190  0.0263  0.0319  138 GLN B CG  
3439 C CD  . GLN B 126 ? 0.3740 0.5443 0.3786 0.0151  0.0274  0.0318  138 GLN B CD  
3440 O OE1 . GLN B 126 ? 0.3625 0.5385 0.3709 0.0169  0.0239  0.0279  138 GLN B OE1 
3441 N NE2 . GLN B 126 ? 0.3888 0.5620 0.3913 0.0097  0.0325  0.0363  138 GLN B NE2 
3442 N N   . GLY B 127 ? 0.2867 0.4017 0.2803 0.0076  0.0362  0.0449  139 GLY B N   
3443 C CA  . GLY B 127 ? 0.2567 0.3563 0.2489 0.0021  0.0394  0.0478  139 GLY B CA  
3444 C C   . GLY B 127 ? 0.2690 0.3589 0.2595 0.0059  0.0396  0.0501  139 GLY B C   
3445 O O   . GLY B 127 ? 0.2958 0.3914 0.2860 0.0124  0.0373  0.0497  139 GLY B O   
3446 N N   . ILE B 128 ? 0.2605 0.3359 0.2501 0.0015  0.0423  0.0523  140 ILE B N   
3447 C CA  . ILE B 128 ? 0.3050 0.3702 0.2931 0.0043  0.0435  0.0554  140 ILE B CA  
3448 C C   . ILE B 128 ? 0.2382 0.2985 0.2286 0.0074  0.0376  0.0508  140 ILE B C   
3449 O O   . ILE B 128 ? 0.3132 0.3652 0.3048 0.0030  0.0367  0.0486  140 ILE B O   
3450 C CB  . ILE B 128 ? 0.2874 0.3389 0.2732 -0.0017 0.0502  0.0605  140 ILE B CB  
3451 C CG1 . ILE B 128 ? 0.3286 0.3847 0.3121 -0.0053 0.0562  0.0649  140 ILE B CG1 
3452 C CG2 . ILE B 128 ? 0.3323 0.3741 0.3173 0.0019  0.0514  0.0640  140 ILE B CG2 
3453 C CD1 . ILE B 128 ? 0.3253 0.3675 0.3061 -0.0104 0.0637  0.0705  140 ILE B CD1 
3454 N N   . PRO B 129 ? 0.2719 0.3369 0.2629 0.0143  0.0336  0.0493  141 PRO B N   
3455 C CA  . PRO B 129 ? 0.2463 0.3069 0.2394 0.0170  0.0280  0.0447  141 PRO B CA  
3456 C C   . PRO B 129 ? 0.2305 0.2760 0.2230 0.0150  0.0299  0.0474  141 PRO B C   
3457 O O   . PRO B 129 ? 0.2335 0.2725 0.2239 0.0124  0.0357  0.0530  141 PRO B O   
3458 C CB  . PRO B 129 ? 0.2525 0.3229 0.2455 0.0244  0.0244  0.0431  141 PRO B CB  
3459 C CG  . PRO B 129 ? 0.2453 0.3199 0.2356 0.0254  0.0290  0.0489  141 PRO B CG  
3460 C CD  . PRO B 129 ? 0.2641 0.3386 0.2534 0.0195  0.0343  0.0519  141 PRO B CD  
3461 N N   . PRO B 130 ? 0.2209 0.2602 0.2152 0.0161  0.0256  0.0438  142 PRO B N   
3462 C CA  . PRO B 130 ? 0.2449 0.2709 0.2388 0.0153  0.0270  0.0463  142 PRO B CA  
3463 C C   . PRO B 130 ? 0.2378 0.2655 0.2305 0.0205  0.0279  0.0501  142 PRO B C   
3464 O O   . PRO B 130 ? 0.1977 0.2369 0.1899 0.0252  0.0262  0.0499  142 PRO B O   
3465 C CB  . PRO B 130 ? 0.1927 0.2147 0.1891 0.0160  0.0212  0.0407  142 PRO B CB  
3466 C CG  . PRO B 130 ? 0.1906 0.2223 0.1888 0.0160  0.0175  0.0358  142 PRO B CG  
3467 C CD  . PRO B 130 ? 0.2170 0.2612 0.2140 0.0183  0.0193  0.0373  142 PRO B CD  
3468 N N   . SER B 131 ? 0.2351 0.2515 0.2274 0.0198  0.0306  0.0538  143 SER B N   
3469 C CA  . SER B 131 ? 0.2364 0.2545 0.2280 0.0250  0.0309  0.0576  143 SER B CA  
3470 C C   . SER B 131 ? 0.2348 0.2588 0.2280 0.0301  0.0239  0.0527  143 SER B C   
3471 O O   . SER B 131 ? 0.2604 0.2822 0.2554 0.0293  0.0194  0.0471  143 SER B O   
3472 C CB  . SER B 131 ? 0.2460 0.2503 0.2372 0.0233  0.0355  0.0627  143 SER B CB  
3473 O OG  . SER B 131 ? 0.2901 0.2843 0.2829 0.0209  0.0331  0.0591  143 SER B OG  
3474 N N   . SER B 132 ? 0.1764 0.2082 0.1687 0.0352  0.0230  0.0550  144 SER B N   
3475 C CA  . SER B 132 ? 0.1659 0.2033 0.1592 0.0396  0.0167  0.0503  144 SER B CA  
3476 C C   . SER B 132 ? 0.2162 0.2424 0.2113 0.0389  0.0146  0.0491  144 SER B C   
3477 O O   . SER B 132 ? 0.2461 0.2645 0.2410 0.0385  0.0181  0.0543  144 SER B O   
3478 C CB  . SER B 132 ? 0.2202 0.2684 0.2119 0.0446  0.0167  0.0537  144 SER B CB  
3479 O OG  . SER B 132 ? 0.2671 0.3261 0.2572 0.0452  0.0185  0.0545  144 SER B OG  
3480 N N   . LYS B 133 ? 0.1908 0.2159 0.1875 0.0389  0.0092  0.0425  145 LYS B N   
3481 C CA  . LYS B 133 ? 0.2161 0.2298 0.2146 0.0374  0.0075  0.0412  145 LYS B CA  
3482 C C   . LYS B 133 ? 0.1784 0.1939 0.1785 0.0391  0.0008  0.0340  145 LYS B C   
3483 O O   . LYS B 133 ? 0.1659 0.1903 0.1660 0.0410  -0.0021 0.0295  145 LYS B O   
3484 C CB  . LYS B 133 ? 0.1866 0.1888 0.1854 0.0316  0.0113  0.0425  145 LYS B CB  
3485 C CG  . LYS B 133 ? 0.1553 0.1605 0.1545 0.0286  0.0104  0.0386  145 LYS B CG  
3486 C CD  . LYS B 133 ? 0.1783 0.1724 0.1774 0.0222  0.0141  0.0400  145 LYS B CD  
3487 C CE  . LYS B 133 ? 0.1792 0.1772 0.1788 0.0187  0.0136  0.0368  145 LYS B CE  
3488 N NZ  . LYS B 133 ? 0.2208 0.2079 0.2197 0.0119  0.0176  0.0385  145 LYS B NZ  
3489 N N   . ASP B 134 ? 0.1617 0.1681 0.1633 0.0383  -0.0012 0.0329  146 ASP B N   
3490 C CA  . ASP B 134 ? 0.1451 0.1507 0.1483 0.0393  -0.0072 0.0264  146 ASP B CA  
3491 C C   . ASP B 134 ? 0.1369 0.1296 0.1418 0.0354  -0.0074 0.0257  146 ASP B C   
3492 O O   . ASP B 134 ? 0.1573 0.1421 0.1618 0.0319  -0.0028 0.0299  146 ASP B O   
3493 C CB  . ASP B 134 ? 0.1549 0.1662 0.1579 0.0437  -0.0108 0.0250  146 ASP B CB  
3494 C CG  . ASP B 134 ? 0.2381 0.2432 0.2414 0.0439  -0.0094 0.0296  146 ASP B CG  
3495 O OD1 . ASP B 134 ? 0.1768 0.1709 0.1810 0.0407  -0.0069 0.0321  146 ASP B OD1 
3496 O OD2 . ASP B 134 ? 0.2095 0.2217 0.2121 0.0473  -0.0109 0.0305  146 ASP B OD2 
3497 N N   . LYS B 135 ? 0.1265 0.1171 0.1331 0.0360  -0.0125 0.0204  147 LYS B N   
3498 C CA  . LYS B 135 ? 0.1403 0.1193 0.1485 0.0328  -0.0137 0.0192  147 LYS B CA  
3499 C C   . LYS B 135 ? 0.1571 0.1294 0.1653 0.0276  -0.0102 0.0208  147 LYS B C   
3500 O O   . LYS B 135 ? 0.1738 0.1366 0.1817 0.0243  -0.0070 0.0240  147 LYS B O   
3501 C CB  . LYS B 135 ? 0.1545 0.1277 0.1628 0.0335  -0.0128 0.0226  147 LYS B CB  
3502 C CG  . LYS B 135 ? 0.1820 0.1612 0.1906 0.0378  -0.0172 0.0202  147 LYS B CG  
3503 C CD  . LYS B 135 ? 0.1832 0.1565 0.1923 0.0379  -0.0166 0.0235  147 LYS B CD  
3504 C CE  . LYS B 135 ? 0.2045 0.1779 0.2125 0.0383  -0.0108 0.0309  147 LYS B CE  
3505 N NZ  . LYS B 135 ? 0.2006 0.1863 0.2070 0.0420  -0.0103 0.0327  147 LYS B NZ  
3506 N N   . LEU B 136 ? 0.1263 0.1043 0.1347 0.0268  -0.0108 0.0184  148 LEU B N   
3507 C CA  . LEU B 136 ? 0.1787 0.1532 0.1871 0.0215  -0.0080 0.0193  148 LEU B CA  
3508 C C   . LEU B 136 ? 0.1510 0.1255 0.1616 0.0205  -0.0124 0.0144  148 LEU B C   
3509 O O   . LEU B 136 ? 0.1959 0.1692 0.2082 0.0230  -0.0170 0.0108  148 LEU B O   
3510 C CB  . LEU B 136 ? 0.1510 0.1334 0.1578 0.0210  -0.0041 0.0218  148 LEU B CB  
3511 C CG  . LEU B 136 ? 0.1583 0.1534 0.1657 0.0251  -0.0070 0.0185  148 LEU B CG  
3512 C CD1 . LEU B 136 ? 0.2075 0.2086 0.2146 0.0224  -0.0045 0.0191  148 LEU B CD1 
3513 C CD2 . LEU B 136 ? 0.1511 0.1531 0.1569 0.0299  -0.0065 0.0203  148 LEU B CD2 
3514 N N   . GLY B 137 ? 0.1400 0.1156 0.1508 0.0165  -0.0108 0.0145  149 GLY B N   
3515 C CA  . GLY B 137 ? 0.1628 0.1400 0.1760 0.0157  -0.0147 0.0106  149 GLY B CA  
3516 C C   . GLY B 137 ? 0.1707 0.1563 0.1841 0.0137  -0.0129 0.0109  149 GLY B C   
3517 O O   . GLY B 137 ? 0.1619 0.1501 0.1732 0.0118  -0.0084 0.0142  149 GLY B O   
3518 N N   . VAL B 138 ? 0.1427 0.1326 0.1586 0.0142  -0.0165 0.0077  150 VAL B N   
3519 C CA  . VAL B 138 ? 0.1293 0.1291 0.1459 0.0130  -0.0154 0.0078  150 VAL B CA  
3520 C C   . VAL B 138 ? 0.1407 0.1409 0.1601 0.0105  -0.0182 0.0059  150 VAL B C   
3521 O O   . VAL B 138 ? 0.1614 0.1579 0.1830 0.0126  -0.0224 0.0032  150 VAL B O   
3522 C CB  . VAL B 138 ? 0.1390 0.1502 0.1562 0.0192  -0.0166 0.0058  150 VAL B CB  
3523 C CG1 . VAL B 138 ? 0.1992 0.2109 0.2189 0.0244  -0.0220 0.0012  150 VAL B CG1 
3524 C CG2 . VAL B 138 ? 0.1694 0.1910 0.1874 0.0177  -0.0151 0.0063  150 VAL B CG2 
3525 N N   . TRP B 139 ? 0.1661 0.1713 0.1855 0.0059  -0.0159 0.0075  151 TRP B N   
3526 C CA  . TRP B 139 ? 0.1585 0.1672 0.1806 0.0035  -0.0183 0.0064  151 TRP B CA  
3527 C C   . TRP B 139 ? 0.1831 0.2058 0.2074 0.0062  -0.0187 0.0057  151 TRP B C   
3528 O O   . TRP B 139 ? 0.1729 0.2017 0.1954 0.0056  -0.0152 0.0074  151 TRP B O   
3529 C CB  . TRP B 139 ? 0.1573 0.1610 0.1777 -0.0050 -0.0153 0.0089  151 TRP B CB  
3530 C CG  . TRP B 139 ? 0.1744 0.1643 0.1923 -0.0086 -0.0135 0.0102  151 TRP B CG  
3531 C CD1 . TRP B 139 ? 0.1719 0.1531 0.1907 -0.0082 -0.0165 0.0087  151 TRP B CD1 
3532 C CD2 . TRP B 139 ? 0.1907 0.1738 0.2047 -0.0133 -0.0078 0.0133  151 TRP B CD2 
3533 N NE1 . TRP B 139 ? 0.1445 0.1144 0.1603 -0.0123 -0.0132 0.0107  151 TRP B NE1 
3534 C CE2 . TRP B 139 ? 0.1587 0.1292 0.1717 -0.0153 -0.0077 0.0135  151 TRP B CE2 
3535 C CE3 . TRP B 139 ? 0.1611 0.1473 0.1726 -0.0159 -0.0026 0.0160  151 TRP B CE3 
3536 C CZ2 . TRP B 139 ? 0.2210 0.1819 0.2306 -0.0196 -0.0024 0.0162  151 TRP B CZ2 
3537 C CZ3 . TRP B 139 ? 0.1883 0.1645 0.1963 -0.0203 0.0027  0.0188  151 TRP B CZ3 
3538 C CH2 . TRP B 139 ? 0.2008 0.1644 0.2080 -0.0218 0.0028  0.0189  151 TRP B CH2 
3539 N N   . VAL B 140 ? 0.1811 0.2089 0.2091 0.0092  -0.0228 0.0033  152 VAL B N   
3540 C CA  . VAL B 140 ? 0.2144 0.2558 0.2450 0.0118  -0.0232 0.0027  152 VAL B CA  
3541 C C   . VAL B 140 ? 0.1836 0.2296 0.2158 0.0058  -0.0229 0.0045  152 VAL B C   
3542 O O   . VAL B 140 ? 0.1641 0.2049 0.1978 0.0035  -0.0253 0.0044  152 VAL B O   
3543 C CB  . VAL B 140 ? 0.2288 0.2740 0.2630 0.0198  -0.0274 -0.0010 152 VAL B CB  
3544 C CG1 . VAL B 140 ? 0.2025 0.2622 0.2398 0.0224  -0.0275 -0.0014 152 VAL B CG1 
3545 C CG2 . VAL B 140 ? 0.2048 0.2465 0.2370 0.0252  -0.0277 -0.0032 152 VAL B CG2 
3546 N N   . TYR B 141 ? 0.1951 0.2512 0.2271 0.0031  -0.0200 0.0064  153 TYR B N   
3547 C CA  . TYR B 141 ? 0.1895 0.2519 0.2231 -0.0029 -0.0199 0.0081  153 TYR B CA  
3548 C C   . TYR B 141 ? 0.2111 0.2888 0.2463 -0.0020 -0.0184 0.0089  153 TYR B C   
3549 O O   . TYR B 141 ? 0.1817 0.2622 0.2140 -0.0044 -0.0144 0.0105  153 TYR B O   
3550 C CB  . TYR B 141 ? 0.1948 0.2486 0.2244 -0.0121 -0.0165 0.0105  153 TYR B CB  
3551 C CG  . TYR B 141 ? 0.2098 0.2688 0.2407 -0.0191 -0.0169 0.0119  153 TYR B CG  
3552 C CD1 . TYR B 141 ? 0.2417 0.3028 0.2764 -0.0177 -0.0214 0.0111  153 TYR B CD1 
3553 C CD2 . TYR B 141 ? 0.2380 0.3002 0.2661 -0.0272 -0.0126 0.0141  153 TYR B CD2 
3554 C CE1 . TYR B 141 ? 0.2249 0.2922 0.2608 -0.0244 -0.0219 0.0127  153 TYR B CE1 
3555 C CE2 . TYR B 141 ? 0.2879 0.3558 0.3168 -0.0342 -0.0129 0.0153  153 TYR B CE2 
3556 C CZ  . TYR B 141 ? 0.2641 0.3350 0.2969 -0.0327 -0.0176 0.0147  153 TYR B CZ  
3557 O OH  . TYR B 141 ? 0.2904 0.3683 0.3239 -0.0401 -0.0179 0.0162  153 TYR B OH  
3558 N N   . LYS B 142 ? 0.2007 0.2884 0.2407 0.0018  -0.0216 0.0080  154 LYS B N   
3559 C CA  . LYS B 142 ? 0.1962 0.2997 0.2389 0.0035  -0.0207 0.0087  154 LYS B CA  
3560 C C   . LYS B 142 ? 0.1779 0.2837 0.2186 0.0088  -0.0187 0.0075  154 LYS B C   
3561 O O   . LYS B 142 ? 0.2623 0.3621 0.3029 0.0152  -0.0204 0.0048  154 LYS B O   
3562 C CB  . LYS B 142 ? 0.1814 0.2910 0.2229 -0.0057 -0.0179 0.0118  154 LYS B CB  
3563 C CG  . LYS B 142 ? 0.2784 0.3897 0.3226 -0.0100 -0.0207 0.0128  154 LYS B CG  
3564 C CD  . LYS B 142 ? 0.2553 0.3633 0.2957 -0.0211 -0.0176 0.0152  154 LYS B CD  
3565 C CE  . LYS B 142 ? 0.3385 0.4508 0.3816 -0.0256 -0.0204 0.0163  154 LYS B CE  
3566 N NZ  . LYS B 142 ? 0.3001 0.4064 0.3464 -0.0197 -0.0252 0.0148  154 LYS B NZ  
3567 N N   . ASN B 143 ? 0.2243 0.3383 0.2633 0.0061  -0.0149 0.0093  155 ASN B N   
3568 C CA  . ASN B 143 ? 0.2006 0.3183 0.2379 0.0111  -0.0129 0.0085  155 ASN B CA  
3569 C C   . ASN B 143 ? 0.2136 0.3194 0.2458 0.0096  -0.0104 0.0092  155 ASN B C   
3570 O O   . ASN B 143 ? 0.2138 0.3221 0.2440 0.0135  -0.0087 0.0089  155 ASN B O   
3571 C CB  . ASN B 143 ? 0.2019 0.3338 0.2394 0.0086  -0.0098 0.0106  155 ASN B CB  
3572 C CG  . ASN B 143 ? 0.2015 0.3316 0.2362 -0.0015 -0.0062 0.0140  155 ASN B CG  
3573 O OD1 . ASN B 143 ? 0.2700 0.3997 0.3061 -0.0068 -0.0074 0.0149  155 ASN B OD1 
3574 N ND2 . ASN B 143 ? 0.1820 0.3105 0.2124 -0.0045 -0.0017 0.0159  155 ASN B ND2 
3575 N N   . LYS B 144 ? 0.1924 0.2858 0.2223 0.0043  -0.0100 0.0104  156 LYS B N   
3576 C CA  . LYS B 144 ? 0.1729 0.2550 0.1982 0.0020  -0.0069 0.0119  156 LYS B CA  
3577 C C   . LYS B 144 ? 0.1851 0.2564 0.2101 0.0068  -0.0099 0.0096  156 LYS B C   
3578 O O   . LYS B 144 ? 0.1745 0.2411 0.2018 0.0076  -0.0135 0.0078  156 LYS B O   
3579 C CB  . LYS B 144 ? 0.1765 0.2510 0.1990 -0.0074 -0.0036 0.0147  156 LYS B CB  
3580 C CG  . LYS B 144 ? 0.1766 0.2603 0.1987 -0.0141 -0.0003 0.0170  156 LYS B CG  
3581 C CD  . LYS B 144 ? 0.2422 0.3154 0.2601 -0.0231 0.0041  0.0195  156 LYS B CD  
3582 C CE  . LYS B 144 ? 0.2553 0.3364 0.2720 -0.0307 0.0081  0.0218  156 LYS B CE  
3583 N NZ  . LYS B 144 ? 0.2679 0.3603 0.2884 -0.0329 0.0050  0.0210  156 LYS B NZ  
3584 N N   . LEU B 145 ? 0.1658 0.2335 0.1879 0.0099  -0.0082 0.0100  157 LEU B N   
3585 C CA  . LEU B 145 ? 0.1542 0.2103 0.1749 0.0123  -0.0096 0.0090  157 LEU B CA  
3586 C C   . LEU B 145 ? 0.1754 0.2216 0.1923 0.0065  -0.0052 0.0128  157 LEU B C   
3587 O O   . LEU B 145 ? 0.1847 0.2337 0.1990 0.0049  -0.0009 0.0156  157 LEU B O   
3588 C CB  . LEU B 145 ? 0.1789 0.2388 0.1990 0.0197  -0.0107 0.0071  157 LEU B CB  
3589 C CG  . LEU B 145 ? 0.1693 0.2395 0.1926 0.0262  -0.0140 0.0032  157 LEU B CG  
3590 C CD1 . LEU B 145 ? 0.2435 0.3163 0.2651 0.0325  -0.0146 0.0012  157 LEU B CD1 
3591 C CD2 . LEU B 145 ? 0.1577 0.2239 0.1845 0.0276  -0.0185 0.0002  157 LEU B CD2 
3592 N N   . ILE B 146 ? 0.1458 0.1803 0.1623 0.0034  -0.0060 0.0128  158 ILE B N   
3593 C CA  . ILE B 146 ? 0.1361 0.1601 0.1493 -0.0028 -0.0015 0.0162  158 ILE B CA  
3594 C C   . ILE B 146 ? 0.1729 0.1864 0.1848 0.0003  -0.0021 0.0162  158 ILE B C   
3595 O O   . ILE B 146 ? 0.1710 0.1782 0.1845 0.0014  -0.0058 0.0140  158 ILE B O   
3596 C CB  . ILE B 146 ? 0.1299 0.1494 0.1434 -0.0102 -0.0013 0.0164  158 ILE B CB  
3597 C CG1 . ILE B 146 ? 0.1516 0.1837 0.1670 -0.0127 -0.0015 0.0161  158 ILE B CG1 
3598 C CG2 . ILE B 146 ? 0.2051 0.2146 0.2147 -0.0170 0.0044  0.0196  158 ILE B CG2 
3599 C CD1 . ILE B 146 ? 0.1917 0.2249 0.2099 -0.0156 -0.0050 0.0146  158 ILE B CD1 
3600 N N   . PHE B 147 ? 0.1476 0.1599 0.1570 0.0018  0.0014  0.0190  159 PHE B N   
3601 C CA  . PHE B 147 ? 0.1672 0.1715 0.1754 0.0052  0.0011  0.0197  159 PHE B CA  
3602 C C   . PHE B 147 ? 0.1643 0.1561 0.1701 0.0000  0.0057  0.0232  159 PHE B C   
3603 O O   . PHE B 147 ? 0.1681 0.1586 0.1718 -0.0050 0.0108  0.0263  159 PHE B O   
3604 C CB  . PHE B 147 ? 0.1445 0.1563 0.1516 0.0108  0.0020  0.0209  159 PHE B CB  
3605 C CG  . PHE B 147 ? 0.1390 0.1624 0.1481 0.0163  -0.0022 0.0170  159 PHE B CG  
3606 C CD1 . PHE B 147 ? 0.1725 0.1954 0.1831 0.0215  -0.0071 0.0133  159 PHE B CD1 
3607 C CD2 . PHE B 147 ? 0.1742 0.2089 0.1837 0.0163  -0.0011 0.0169  159 PHE B CD2 
3608 C CE1 . PHE B 147 ? 0.1626 0.1954 0.1749 0.0266  -0.0104 0.0093  159 PHE B CE1 
3609 C CE2 . PHE B 147 ? 0.1630 0.2081 0.1744 0.0216  -0.0046 0.0132  159 PHE B CE2 
3610 C CZ  . PHE B 147 ? 0.1872 0.2310 0.1999 0.0268  -0.0091 0.0093  159 PHE B CZ  
3611 N N   . PHE B 148 ? 0.1711 0.1535 0.1772 0.0012  0.0041  0.0229  160 PHE B N   
3612 C CA  . PHE B 148 ? 0.1769 0.1468 0.1809 -0.0033 0.0085  0.0260  160 PHE B CA  
3613 C C   . PHE B 148 ? 0.1874 0.1517 0.1912 0.0011  0.0084  0.0276  160 PHE B C   
3614 O O   . PHE B 148 ? 0.1803 0.1459 0.1859 0.0056  0.0033  0.0247  160 PHE B O   
3615 C CB  . PHE B 148 ? 0.2059 0.1683 0.2106 -0.0088 0.0073  0.0241  160 PHE B CB  
3616 C CG  . PHE B 148 ? 0.2021 0.1507 0.2048 -0.0125 0.0113  0.0265  160 PHE B CG  
3617 C CD1 . PHE B 148 ? 0.2173 0.1605 0.2170 -0.0174 0.0182  0.0302  160 PHE B CD1 
3618 C CD2 . PHE B 148 ? 0.2528 0.1939 0.2567 -0.0110 0.0084  0.0252  160 PHE B CD2 
3619 C CE1 . PHE B 148 ? 0.2648 0.1949 0.2628 -0.0206 0.0224  0.0324  160 PHE B CE1 
3620 C CE2 . PHE B 148 ? 0.2195 0.1481 0.2217 -0.0142 0.0123  0.0275  160 PHE B CE2 
3621 C CZ  . PHE B 148 ? 0.2100 0.1330 0.2093 -0.0188 0.0194  0.0310  160 PHE B CZ  
3622 N N   . GLY B 149 ? 0.1639 0.1222 0.1654 -0.0002 0.0141  0.0322  161 GLY B N   
3623 C CA  . GLY B 149 ? 0.1793 0.1308 0.1806 0.0028  0.0149  0.0346  161 GLY B CA  
3624 C C   . GLY B 149 ? 0.1521 0.1124 0.1539 0.0099  0.0126  0.0352  161 GLY B C   
3625 O O   . GLY B 149 ? 0.1722 0.1433 0.1738 0.0123  0.0118  0.0347  161 GLY B O   
3626 N N   . GLY B 150 ? 0.1977 0.1537 0.2001 0.0131  0.0116  0.0364  162 GLY B N   
3627 C CA  . GLY B 150 ? 0.1884 0.1528 0.1912 0.0195  0.0087  0.0365  162 GLY B CA  
3628 C C   . GLY B 150 ? 0.2122 0.1737 0.2142 0.0217  0.0127  0.0424  162 GLY B C   
3629 O O   . GLY B 150 ? 0.1709 0.1227 0.1721 0.0187  0.0181  0.0464  162 GLY B O   
3630 N N   . TYR B 151 ? 0.1464 0.1168 0.1486 0.0272  0.0101  0.0428  163 TYR B N   
3631 C CA  . TYR B 151 ? 0.2143 0.1844 0.2161 0.0305  0.0127  0.0483  163 TYR B CA  
3632 C C   . TYR B 151 ? 0.1874 0.1707 0.1880 0.0346  0.0129  0.0504  163 TYR B C   
3633 O O   . TYR B 151 ? 0.2267 0.2197 0.2274 0.0371  0.0081  0.0458  163 TYR B O   
3634 C CB  . TYR B 151 ? 0.1813 0.1497 0.1850 0.0329  0.0083  0.0464  163 TYR B CB  
3635 C CG  . TYR B 151 ? 0.2170 0.1849 0.2209 0.0361  0.0108  0.0524  163 TYR B CG  
3636 C CD1 . TYR B 151 ? 0.2215 0.1783 0.2256 0.0341  0.0164  0.0574  163 TYR B CD1 
3637 C CD2 . TYR B 151 ? 0.2177 0.1965 0.2217 0.0410  0.0076  0.0529  163 TYR B CD2 
3638 C CE1 . TYR B 151 ? 0.2730 0.2297 0.2779 0.0375  0.0188  0.0633  163 TYR B CE1 
3639 C CE2 . TYR B 151 ? 0.2166 0.1962 0.2212 0.0440  0.0097  0.0588  163 TYR B CE2 
3640 C CZ  . TYR B 151 ? 0.2512 0.2198 0.2565 0.0425  0.0154  0.0642  163 TYR B CZ  
3641 O OH  . TYR B 151 ? 0.3066 0.2770 0.3129 0.0450  0.0175  0.0692  163 TYR B OH  
3642 N N   . GLY B 152 ? 0.2099 0.1932 0.2092 0.0354  0.0186  0.0572  164 GLY B N   
3643 C CA  . GLY B 152 ? 0.1588 0.1549 0.1567 0.0391  0.0190  0.0597  164 GLY B CA  
3644 C C   . GLY B 152 ? 0.2156 0.2095 0.2122 0.0390  0.0263  0.0678  164 GLY B C   
3645 O O   . GLY B 152 ? 0.2330 0.2152 0.2299 0.0369  0.0310  0.0718  164 GLY B O   
3646 N N   . TYR B 153 ? 0.2145 0.2194 0.2094 0.0412  0.0276  0.0702  165 TYR B N   
3647 C CA  . TYR B 153 ? 0.2884 0.2928 0.2821 0.0421  0.0343  0.0785  165 TYR B CA  
3648 C C   . TYR B 153 ? 0.3183 0.3115 0.3111 0.0366  0.0407  0.0807  165 TYR B C   
3649 O O   . TYR B 153 ? 0.2751 0.2652 0.2676 0.0321  0.0398  0.0757  165 TYR B O   
3650 C CB  . TYR B 153 ? 0.2898 0.3095 0.2818 0.0455  0.0339  0.0804  165 TYR B CB  
3651 C CG  . TYR B 153 ? 0.2412 0.2729 0.2335 0.0501  0.0273  0.0770  165 TYR B CG  
3652 C CD1 . TYR B 153 ? 0.2975 0.3286 0.2913 0.0531  0.0254  0.0789  165 TYR B CD1 
3653 C CD2 . TYR B 153 ? 0.2785 0.3221 0.2698 0.0512  0.0230  0.0714  165 TYR B CD2 
3654 C CE1 . TYR B 153 ? 0.3569 0.3989 0.3507 0.0566  0.0194  0.0753  165 TYR B CE1 
3655 C CE2 . TYR B 153 ? 0.2456 0.2995 0.2368 0.0550  0.0173  0.0677  165 TYR B CE2 
3656 C CZ  . TYR B 153 ? 0.2712 0.3242 0.2635 0.0574  0.0154  0.0695  165 TYR B CZ  
3657 O OH  . TYR B 153 ? 0.3185 0.3816 0.3104 0.0604  0.0098  0.0655  165 TYR B OH  
3658 N N   . LEU B 154 ? 0.3354 0.3226 0.3275 0.0370  0.0475  0.0884  166 LEU B N   
3659 C CA  . LEU B 154 ? 0.3531 0.3314 0.3438 0.0320  0.0545  0.0910  166 LEU B CA  
3660 C C   . LEU B 154 ? 0.3781 0.3650 0.3670 0.0296  0.0540  0.0885  166 LEU B C   
3661 O O   . LEU B 154 ? 0.3444 0.3450 0.3327 0.0335  0.0515  0.0888  166 LEU B O   
3662 C CB  . LEU B 154 ? 0.3824 0.3605 0.3746 0.0333  0.0583  0.0942  166 LEU B CB  
3663 C CG  . LEU B 154 ? 0.3845 0.3553 0.3758 0.0278  0.0633  0.0932  166 LEU B CG  
3664 C CD1 . LEU B 154 ? 0.3496 0.3067 0.3416 0.0226  0.0639  0.0881  166 LEU B CD1 
3665 C CD2 . LEU B 154 ? 0.3736 0.3474 0.3656 0.0303  0.0669  0.0978  166 LEU B CD2 
3666 N N   . PRO B 155 ? 0.3330 0.3131 0.3211 0.0233  0.0558  0.0852  167 PRO B N   
3667 C CA  . PRO B 155 ? 0.4017 0.3907 0.3885 0.0209  0.0556  0.0829  167 PRO B CA  
3668 C C   . PRO B 155 ? 0.4841 0.4788 0.4690 0.0226  0.0608  0.0897  167 PRO B C   
3669 O O   . PRO B 155 ? 0.4606 0.4471 0.4455 0.0215  0.0657  0.0932  167 PRO B O   
3670 C CB  . PRO B 155 ? 0.4036 0.3817 0.3897 0.0132  0.0585  0.0802  167 PRO B CB  
3671 C CG  . PRO B 155 ? 0.4295 0.3964 0.4171 0.0122  0.0568  0.0780  167 PRO B CG  
3672 C CD  . PRO B 155 ? 0.3274 0.2926 0.3159 0.0180  0.0577  0.0830  167 PRO B CD  
3673 N N   . GLU B 156 ? 0.4718 0.4814 0.4561 0.0252  0.0578  0.0882  168 GLU B N   
3674 C CA  . GLU B 156 ? 0.5149 0.5314 0.4973 0.0265  0.0625  0.0943  168 GLU B CA  
3675 C C   . GLU B 156 ? 0.5597 0.5681 0.5405 0.0199  0.0691  0.0962  168 GLU B C   
3676 O O   . GLU B 156 ? 0.5923 0.6001 0.5728 0.0196  0.0721  0.0988  168 GLU B O   
3677 C CB  . GLU B 156 ? 0.5547 0.5889 0.5367 0.0298  0.0576  0.0911  168 GLU B CB  
3678 C CG  . GLU B 156 ? 0.5437 0.5864 0.5271 0.0356  0.0504  0.0874  168 GLU B CG  
3679 C CD  . GLU B 156 ? 0.6355 0.6817 0.6186 0.0411  0.0515  0.0939  168 GLU B CD  
3680 O OE1 . GLU B 156 ? 0.6074 0.6614 0.5887 0.0430  0.0548  0.0995  168 GLU B OE1 
3681 O OE2 . GLU B 156 ? 0.5778 0.6194 0.5624 0.0434  0.0490  0.0937  168 GLU B OE2 
3682 N N   . ASP B 157 ? 0.5686 0.5708 0.5495 0.0139  0.0688  0.0915  169 ASP B N   
3683 C CA  . ASP B 157 ? 0.5989 0.5938 0.5786 0.0064  0.0727  0.0898  169 ASP B CA  
3684 C C   . ASP B 157 ? 0.6044 0.5849 0.5846 0.0009  0.0723  0.0852  169 ASP B C   
3685 O O   . ASP B 157 ? 0.5637 0.5433 0.5451 0.0016  0.0694  0.0831  169 ASP B O   
3686 C CB  . ASP B 157 ? 0.5894 0.5961 0.5681 0.0039  0.0728  0.0886  169 ASP B CB  
3687 C CG  . ASP B 157 ? 0.6588 0.6584 0.6361 -0.0048 0.0758  0.0859  169 ASP B CG  
3688 O OD1 . ASP B 157 ? 0.6545 0.6506 0.6302 -0.0070 0.0789  0.0874  169 ASP B OD1 
3689 O OD2 . ASP B 157 ? 0.6383 0.6361 0.6160 -0.0095 0.0749  0.0822  169 ASP B OD2 
3690 N N   . LYS B 158 ? 0.6611 0.6312 0.6402 -0.0043 0.0749  0.0837  170 LYS B N   
3691 C CA  . LYS B 158 ? 0.6219 0.5805 0.6009 -0.0103 0.0742  0.0789  170 LYS B CA  
3692 C C   . LYS B 158 ? 0.5901 0.5520 0.5682 -0.0163 0.0734  0.0754  170 LYS B C   
3693 O O   . LYS B 158 ? 0.6157 0.5833 0.5923 -0.0199 0.0754  0.0758  170 LYS B O   
3694 C CB  . LYS B 158 ? 0.6418 0.5914 0.6195 -0.0138 0.0771  0.0786  170 LYS B CB  
3695 C CG  . LYS B 158 ? 0.6116 0.5538 0.5882 -0.0216 0.0768  0.0738  170 LYS B CG  
3696 C CD  . LYS B 158 ? 0.6096 0.5439 0.5878 -0.0212 0.0742  0.0705  170 LYS B CD  
3697 C CE  . LYS B 158 ? 0.5843 0.5119 0.5616 -0.0279 0.0741  0.0665  170 LYS B CE  
3698 N NZ  . LYS B 158 ? 0.4397 0.3618 0.4186 -0.0277 0.0709  0.0628  170 LYS B NZ  
3699 N N   . VAL B 159 ? 0.5954 0.5543 0.5749 -0.0173 0.0705  0.0721  171 VAL B N   
3700 C CA  . VAL B 159 ? 0.5501 0.5128 0.5297 -0.0223 0.0694  0.0689  171 VAL B CA  
3701 C C   . VAL B 159 ? 0.4951 0.4475 0.4748 -0.0278 0.0672  0.0640  171 VAL B C   
3702 O O   . VAL B 159 ? 0.4985 0.4421 0.4782 -0.0274 0.0667  0.0631  171 VAL B O   
3703 C CB  . VAL B 159 ? 0.5503 0.5249 0.5325 -0.0168 0.0642  0.0676  171 VAL B CB  
3704 C CG1 . VAL B 159 ? 0.6218 0.6103 0.6040 -0.0115 0.0635  0.0699  171 VAL B CG1 
3705 C CG2 . VAL B 159 ? 0.4642 0.4342 0.4484 -0.0116 0.0598  0.0663  171 VAL B CG2 
3706 N N   . LEU B 160 ? 0.3898 0.3450 0.3699 -0.0325 0.0657  0.0608  172 LEU B N   
3707 C CA  . LEU B 160 ? 0.4148 0.3627 0.3952 -0.0377 0.0629  0.0562  172 LEU B CA  
3708 C C   . LEU B 160 ? 0.3752 0.3170 0.3575 -0.0336 0.0597  0.0549  172 LEU B C   
3709 O O   . LEU B 160 ? 0.3401 0.2852 0.3240 -0.0298 0.0584  0.0557  172 LEU B O   
3710 C CB  . LEU B 160 ? 0.4067 0.3607 0.3875 -0.0437 0.0620  0.0534  172 LEU B CB  
3711 C CG  . LEU B 160 ? 0.4177 0.3791 0.3974 -0.0488 0.0645  0.0541  172 LEU B CG  
3712 C CD1 . LEU B 160 ? 0.4212 0.3903 0.4017 -0.0538 0.0632  0.0512  172 LEU B CD1 
3713 C CD2 . LEU B 160 ? 0.4603 0.4157 0.4397 -0.0523 0.0652  0.0537  172 LEU B CD2 
3714 N N   . GLY B 161 ? 0.3670 0.3008 0.3493 -0.0339 0.0584  0.0530  173 GLY B N   
3715 C CA  . GLY B 161 ? 0.3411 0.2696 0.3251 -0.0305 0.0550  0.0513  173 GLY B CA  
3716 C C   . GLY B 161 ? 0.3503 0.2746 0.3344 -0.0255 0.0562  0.0534  173 GLY B C   
3717 O O   . GLY B 161 ? 0.3804 0.3043 0.3633 -0.0253 0.0596  0.0557  173 GLY B O   
3718 N N   . THR B 162 ? 0.3350 0.2565 0.3209 -0.0215 0.0533  0.0526  174 THR B N   
3719 C CA  . THR B 162 ? 0.3215 0.2399 0.3081 -0.0170 0.0540  0.0541  174 THR B CA  
3720 C C   . THR B 162 ? 0.3257 0.2467 0.3144 -0.0102 0.0522  0.0565  174 THR B C   
3721 O O   . THR B 162 ? 0.3166 0.2391 0.3065 -0.0092 0.0489  0.0555  174 THR B O   
3722 C CB  . THR B 162 ? 0.3753 0.2880 0.3622 -0.0194 0.0523  0.0502  174 THR B CB  
3723 O OG1 . THR B 162 ? 0.3279 0.2403 0.3161 -0.0199 0.0476  0.0470  174 THR B OG1 
3724 C CG2 . THR B 162 ? 0.3545 0.2653 0.3397 -0.0254 0.0540  0.0483  174 THR B CG2 
3725 N N   . PHE B 163 ? 0.2920 0.2170 0.3404 0.0316  0.0262  0.0150  175 PHE B N   
3726 C CA  . PHE B 163 ? 0.2966 0.2254 0.3490 0.0358  0.0227  0.0149  175 PHE B CA  
3727 C C   . PHE B 163 ? 0.2955 0.2235 0.3542 0.0382  0.0239  0.0125  175 PHE B C   
3728 O O   . PHE B 163 ? 0.3014 0.2248 0.3607 0.0388  0.0264  0.0124  175 PHE B O   
3729 C CB  . PHE B 163 ? 0.2924 0.2203 0.3420 0.0400  0.0195  0.0183  175 PHE B CB  
3730 C CG  . PHE B 163 ? 0.2829 0.2142 0.3368 0.0448  0.0160  0.0182  175 PHE B CG  
3731 C CD1 . PHE B 163 ? 0.3199 0.2494 0.3779 0.0490  0.0160  0.0180  175 PHE B CD1 
3732 C CD2 . PHE B 163 ? 0.2663 0.2027 0.3200 0.0452  0.0128  0.0186  175 PHE B CD2 
3733 C CE1 . PHE B 163 ? 0.2730 0.2059 0.3349 0.0533  0.0128  0.0180  175 PHE B CE1 
3734 C CE2 . PHE B 163 ? 0.2447 0.1844 0.3022 0.0495  0.0097  0.0185  175 PHE B CE2 
3735 C CZ  . PHE B 163 ? 0.2990 0.2369 0.3605 0.0536  0.0096  0.0183  175 PHE B CZ  
3736 N N   . GLU B 164 ? 0.2919 0.2246 0.3556 0.0392  0.0222  0.0105  176 GLU B N   
3737 C CA  . GLU B 164 ? 0.3110 0.2438 0.3812 0.0411  0.0233  0.0079  176 GLU B CA  
3738 C C   . GLU B 164 ? 0.2851 0.2216 0.3591 0.0459  0.0195  0.0082  176 GLU B C   
3739 O O   . GLU B 164 ? 0.2279 0.1693 0.3024 0.0455  0.0171  0.0079  176 GLU B O   
3740 C CB  . GLU B 164 ? 0.3186 0.2536 0.3913 0.0367  0.0258  0.0045  176 GLU B CB  
3741 C CG  . GLU B 164 ? 0.3625 0.2981 0.4421 0.0386  0.0267  0.0018  176 GLU B CG  
3742 C CD  . GLU B 164 ? 0.4062 0.3363 0.4872 0.0403  0.0294  0.0018  176 GLU B CD  
3743 O OE1 . GLU B 164 ? 0.4060 0.3320 0.4834 0.0372  0.0324  0.0021  176 GLU B OE1 
3744 O OE2 . GLU B 164 ? 0.4653 0.3952 0.5510 0.0446  0.0284  0.0015  176 GLU B OE2 
3745 N N   . PHE B 165 ? 0.3192 0.2535 0.3961 0.0503  0.0191  0.0088  177 PHE B N   
3746 C CA  . PHE B 165 ? 0.2998 0.2376 0.3804 0.0550  0.0154  0.0093  177 PHE B CA  
3747 C C   . PHE B 165 ? 0.3059 0.2481 0.3924 0.0547  0.0152  0.0061  177 PHE B C   
3748 O O   . PHE B 165 ? 0.2877 0.2288 0.3773 0.0526  0.0182  0.0035  177 PHE B O   
3749 C CB  . PHE B 165 ? 0.3180 0.2524 0.4005 0.0597  0.0152  0.0108  177 PHE B CB  
3750 C CG  . PHE B 165 ? 0.2857 0.2186 0.3635 0.0623  0.0129  0.0145  177 PHE B CG  
3751 C CD1 . PHE B 165 ? 0.3181 0.2551 0.3948 0.0644  0.0089  0.0160  177 PHE B CD1 
3752 C CD2 . PHE B 165 ? 0.3205 0.2479 0.3953 0.0627  0.0148  0.0165  177 PHE B CD2 
3753 C CE1 . PHE B 165 ? 0.3017 0.2374 0.3741 0.0668  0.0067  0.0194  177 PHE B CE1 
3754 C CE2 . PHE B 165 ? 0.3440 0.2701 0.4145 0.0651  0.0126  0.0199  177 PHE B CE2 
3755 C CZ  . PHE B 165 ? 0.3404 0.2706 0.4097 0.0672  0.0086  0.0214  177 PHE B CZ  
3756 N N   . ASP B 166 ? 0.2819 0.2290 0.3698 0.0568  0.0116  0.0063  178 ASP B N   
3757 C CA  . ASP B 166 ? 0.3490 0.3005 0.4429 0.0578  0.0106  0.0037  178 ASP B CA  
3758 C C   . ASP B 166 ? 0.3498 0.3007 0.4481 0.0631  0.0092  0.0042  178 ASP B C   
3759 O O   . ASP B 166 ? 0.3375 0.2896 0.4348 0.0668  0.0060  0.0065  178 ASP B O   
3760 C CB  . ASP B 166 ? 0.2656 0.2227 0.3587 0.0572  0.0074  0.0037  178 ASP B CB  
3761 C CG  . ASP B 166 ? 0.3145 0.2764 0.4138 0.0582  0.0062  0.0010  178 ASP B CG  
3762 O OD1 . ASP B 166 ? 0.3499 0.3110 0.4541 0.0592  0.0078  -0.0010 178 ASP B OD1 
3763 O OD2 . ASP B 166 ? 0.2955 0.2621 0.3947 0.0580  0.0036  0.0009  178 ASP B OD2 
3764 N N   . GLU B 167 ? 0.3692 0.3184 0.4723 0.0636  0.0117  0.0022  179 GLU B N   
3765 C CA  . GLU B 167 ? 0.3566 0.3046 0.4637 0.0685  0.0108  0.0030  179 GLU B CA  
3766 C C   . GLU B 167 ? 0.3687 0.3220 0.4792 0.0721  0.0069  0.0029  179 GLU B C   
3767 O O   . GLU B 167 ? 0.4041 0.3579 0.5129 0.0754  0.0047  0.0045  179 GLU B O   
3768 C CB  . GLU B 167 ? 0.3930 0.3381 0.5048 0.0680  0.0145  0.0006  179 GLU B CB  
3769 C CG  . GLU B 167 ? 0.4227 0.3712 0.5388 0.0655  0.0156  -0.0030 179 GLU B CG  
3770 C CD  . GLU B 167 ? 0.5118 0.4573 0.6327 0.0653  0.0191  -0.0053 179 GLU B CD  
3771 O OE1 . GLU B 167 ? 0.4661 0.4068 0.5870 0.0669  0.0209  -0.0041 179 GLU B OE1 
3772 O OE2 . GLU B 167 ? 0.5219 0.4700 0.6469 0.0636  0.0201  -0.0084 179 GLU B OE2 
3773 N N   . THR B 168 ? 0.3474 0.3054 0.4595 0.0703  0.0057  0.0009  180 THR B N   
3774 C CA  . THR B 168 ? 0.3963 0.3600 0.5096 0.0727  0.0020  0.0006  180 THR B CA  
3775 C C   . THR B 168 ? 0.4378 0.4028 0.5458 0.0749  -0.0015 0.0037  180 THR B C   
3776 O O   . THR B 168 ? 0.4541 0.4227 0.5613 0.0776  -0.0044 0.0042  180 THR B O   
3777 C CB  . THR B 168 ? 0.3471 0.3154 0.4637 0.0703  0.0015  -0.0020 180 THR B CB  
3778 O OG1 . THR B 168 ? 0.3451 0.3142 0.4571 0.0672  0.0011  -0.0012 180 THR B OG1 
3779 C CG2 . THR B 168 ? 0.4081 0.3752 0.5292 0.0678  0.0051  -0.0052 180 THR B CG2 
3780 N N   . SER B 169 ? 0.3616 0.3237 0.4658 0.0738  -0.0012 0.0059  181 SER B N   
3781 C CA  . SER B 169 ? 0.4220 0.3851 0.5208 0.0756  -0.0043 0.0088  181 SER B CA  
3782 C C   . SER B 169 ? 0.4651 0.4260 0.5608 0.0789  -0.0052 0.0109  181 SER B C   
3783 O O   . SER B 169 ? 0.4839 0.4462 0.5751 0.0808  -0.0080 0.0131  181 SER B O   
3784 C CB  . SER B 169 ? 0.3738 0.3347 0.4683 0.0727  -0.0035 0.0104  181 SER B CB  
3785 O OG  . SER B 169 ? 0.2802 0.2354 0.3722 0.0713  -0.0003 0.0112  181 SER B OG  
3786 N N   . PHE B 170 ? 0.4501 0.4074 0.5480 0.0797  -0.0028 0.0104  182 PHE B N   
3787 C CA  . PHE B 170 ? 0.4665 0.4220 0.5619 0.0829  -0.0038 0.0124  182 PHE B CA  
3788 C C   . PHE B 170 ? 0.5281 0.4881 0.6248 0.0859  -0.0063 0.0119  182 PHE B C   
3789 O O   . PHE B 170 ? 0.5535 0.5143 0.6467 0.0887  -0.0086 0.0138  182 PHE B O   
3790 C CB  . PHE B 170 ? 0.4042 0.3542 0.5014 0.0826  -0.0003 0.0121  182 PHE B CB  
3791 C CG  . PHE B 170 ? 0.3964 0.3412 0.4906 0.0804  0.0022  0.0137  182 PHE B CG  
3792 C CD1 . PHE B 170 ? 0.4036 0.3472 0.4993 0.0767  0.0049  0.0123  182 PHE B CD1 
3793 C CD2 . PHE B 170 ? 0.3571 0.2985 0.4469 0.0819  0.0017  0.0164  182 PHE B CD2 
3794 C CE1 . PHE B 170 ? 0.3706 0.3093 0.4630 0.0745  0.0074  0.0139  182 PHE B CE1 
3795 C CE2 . PHE B 170 ? 0.3894 0.3260 0.4760 0.0797  0.0041  0.0179  182 PHE B CE2 
3796 C CZ  . PHE B 170 ? 0.3530 0.2882 0.4408 0.0761  0.0071  0.0167  182 PHE B CZ  
3797 N N   . TRP B 171 ? 0.5543 0.5175 0.6558 0.0852  -0.0058 0.0092  183 TRP B N   
3798 C CA  . TRP B 171 ? 0.6256 0.5930 0.7284 0.0879  -0.0078 0.0089  183 TRP B CA  
3799 C C   . TRP B 171 ? 0.6582 0.6307 0.7580 0.0885  -0.0109 0.0099  183 TRP B C   
3800 O O   . TRP B 171 ? 0.6294 0.6034 0.7260 0.0912  -0.0129 0.0120  183 TRP B O   
3801 C CB  . TRP B 171 ? 0.5719 0.5411 0.6806 0.0867  -0.0062 0.0058  183 TRP B CB  
3802 N N   . ASN B 172 ? 0.6777 0.6529 0.7784 0.0858  -0.0112 0.0085  184 ASN B N   
3803 C CA  . ASN B 172 ? 0.7488 0.7292 0.8475 0.0860  -0.0139 0.0091  184 ASN B CA  
3804 C C   . ASN B 172 ? 0.7880 0.7677 0.8810 0.0863  -0.0153 0.0119  184 ASN B C   
3805 O O   . ASN B 172 ? 0.8331 0.8152 0.9231 0.0884  -0.0171 0.0140  184 ASN B O   
3806 C CB  . ASN B 172 ? 0.8159 0.7995 0.9178 0.0829  -0.0137 0.0065  184 ASN B CB  
3807 N N   . SER B 173 ? 0.7776 0.7539 0.8690 0.0840  -0.0143 0.0121  185 SER B N   
3808 C CA  . SER B 173 ? 0.7671 0.7424 0.8529 0.0840  -0.0156 0.0147  185 SER B CA  
3809 C C   . SER B 173 ? 0.7303 0.7025 0.8124 0.0869  -0.0159 0.0170  185 SER B C   
3810 O O   . SER B 173 ? 0.6926 0.6612 0.7764 0.0879  -0.0144 0.0167  185 SER B O   
3811 C CB  . SER B 173 ? 0.6838 0.6558 0.7691 0.0808  -0.0142 0.0146  185 SER B CB  
3812 O OG  . SER B 173 ? 0.6156 0.5896 0.7054 0.0781  -0.0132 0.0119  185 SER B OG  
3813 N N   . SER B 174 ? 0.7720 0.7457 0.8490 0.0881  -0.0178 0.0195  186 SER B N   
3814 C CA  . SER B 174 ? 0.7573 0.7276 0.8300 0.0906  -0.0184 0.0216  186 SER B CA  
3815 C C   . SER B 174 ? 0.7112 0.6753 0.7815 0.0887  -0.0177 0.0220  186 SER B C   
3816 O O   . SER B 174 ? 0.6904 0.6504 0.7596 0.0898  -0.0177 0.0228  186 SER B O   
3817 C CB  . SER B 174 ? 0.7976 0.7723 0.8666 0.0909  -0.0197 0.0244  186 SER B CB  
3818 O OG  . SER B 174 ? 0.8069 0.7821 0.8729 0.0884  -0.0200 0.0256  186 SER B OG  
3819 N N   . HIS B 175 ? 0.6585 0.6224 0.7288 0.0856  -0.0169 0.0217  187 HIS B N   
3820 C CA  . HIS B 175 ? 0.5935 0.5522 0.6624 0.0832  -0.0151 0.0228  187 HIS B CA  
3821 C C   . HIS B 175 ? 0.5117 0.4693 0.5858 0.0804  -0.0117 0.0211  187 HIS B C   
3822 O O   . HIS B 175 ? 0.4879 0.4492 0.5645 0.0788  -0.0121 0.0195  187 HIS B O   
3823 C CB  . HIS B 175 ? 0.5599 0.5191 0.6236 0.0817  -0.0168 0.0245  187 HIS B CB  
3824 C CG  . HIS B 175 ? 0.5847 0.5391 0.6441 0.0812  -0.0167 0.0269  187 HIS B CG  
3825 N ND1 . HIS B 175 ? 0.5640 0.5132 0.6237 0.0799  -0.0131 0.0278  187 HIS B ND1 
3826 C CD2 . HIS B 175 ? 0.6364 0.5906 0.6919 0.0815  -0.0197 0.0286  187 HIS B CD2 
3827 C CE1 . HIS B 175 ? 0.6551 0.6012 0.7101 0.0797  -0.0136 0.0301  187 HIS B CE1 
3828 N NE2 . HIS B 175 ? 0.6785 0.6277 0.7312 0.0805  -0.0176 0.0306  187 HIS B NE2 
3829 N N   . PRO B 176 ? 0.4211 0.3739 0.4969 0.0796  -0.0085 0.0210  188 PRO B N   
3830 C CA  . PRO B 176 ? 0.3999 0.3515 0.4806 0.0768  -0.0050 0.0190  188 PRO B CA  
3831 C C   . PRO B 176 ? 0.3615 0.3126 0.4383 0.0726  -0.0039 0.0193  188 PRO B C   
3832 O O   . PRO B 176 ? 0.3226 0.2723 0.3939 0.0722  -0.0047 0.0218  188 PRO B O   
3833 C CB  . PRO B 176 ? 0.4171 0.3633 0.4989 0.0771  -0.0018 0.0190  188 PRO B CB  
3834 C CG  . PRO B 176 ? 0.4236 0.3670 0.4997 0.0788  -0.0030 0.0219  188 PRO B CG  
3835 C CD  . PRO B 176 ? 0.4992 0.4472 0.5724 0.0810  -0.0076 0.0227  188 PRO B CD  
3836 N N   . ARG B 177 ? 0.3347 0.2876 0.4135 0.0690  -0.0021 0.0165  189 ARG B N   
3837 C CA  . ARG B 177 ? 0.2329 0.1862 0.3076 0.0642  -0.0010 0.0162  189 ARG B CA  
3838 C C   . ARG B 177 ? 0.2869 0.2384 0.3633 0.0602  0.0029  0.0136  189 ARG B C   
3839 O O   . ARG B 177 ? 0.2223 0.1733 0.3037 0.0612  0.0044  0.0116  189 ARG B O   
3840 C CB  . ARG B 177 ? 0.2955 0.2545 0.3704 0.0636  -0.0038 0.0156  189 ARG B CB  
3841 C CG  . ARG B 177 ? 0.3205 0.2813 0.3933 0.0671  -0.0076 0.0181  189 ARG B CG  
3842 C CD  . ARG B 177 ? 0.3025 0.2688 0.3754 0.0663  -0.0102 0.0176  189 ARG B CD  
3843 N NE  . ARG B 177 ? 0.3790 0.3497 0.4579 0.0683  -0.0117 0.0153  189 ARG B NE  
3844 C CZ  . ARG B 177 ? 0.3976 0.3733 0.4777 0.0678  -0.0138 0.0142  189 ARG B CZ  
3845 N NH1 . ARG B 177 ? 0.3047 0.2819 0.3808 0.0655  -0.0146 0.0153  189 ARG B NH1 
3846 N NH2 . ARG B 177 ? 0.4094 0.3889 0.4953 0.0697  -0.0151 0.0121  189 ARG B NH2 
3847 N N   . GLY B 178 ? 0.2651 0.2157 0.3373 0.0557  0.0047  0.0137  190 GLY B N   
3848 C CA  . GLY B 178 ? 0.2502 0.1994 0.3233 0.0515  0.0084  0.0114  190 GLY B CA  
3849 C C   . GLY B 178 ? 0.2208 0.1718 0.2901 0.0466  0.0090  0.0113  190 GLY B C   
3850 O O   . GLY B 178 ? 0.2236 0.1770 0.2898 0.0467  0.0065  0.0130  190 GLY B O   
3851 N N   . TRP B 179 ? 0.2331 0.1831 0.3028 0.0424  0.0124  0.0093  191 TRP B N   
3852 C CA  . TRP B 179 ? 0.1532 0.1048 0.2197 0.0372  0.0136  0.0090  191 TRP B CA  
3853 C C   . TRP B 179 ? 0.1851 0.1320 0.2458 0.0345  0.0160  0.0108  191 TRP B C   
3854 O O   . TRP B 179 ? 0.2017 0.1438 0.2620 0.0355  0.0180  0.0111  191 TRP B O   
3855 C CB  . TRP B 179 ? 0.1879 0.1415 0.2585 0.0339  0.0160  0.0055  191 TRP B CB  
3856 C CG  . TRP B 179 ? 0.1914 0.1496 0.2681 0.0363  0.0140  0.0034  191 TRP B CG  
3857 C CD1 . TRP B 179 ? 0.1693 0.1329 0.2472 0.0360  0.0115  0.0030  191 TRP B CD1 
3858 C CD2 . TRP B 179 ? 0.2208 0.1785 0.3032 0.0393  0.0143  0.0015  191 TRP B CD2 
3859 N NE1 . TRP B 179 ? 0.2077 0.1741 0.2916 0.0386  0.0103  0.0009  191 TRP B NE1 
3860 C CE2 . TRP B 179 ? 0.2319 0.1950 0.3186 0.0407  0.0119  -0.0001 191 TRP B CE2 
3861 C CE3 . TRP B 179 ? 0.2741 0.2275 0.3584 0.0411  0.0164  0.0010  191 TRP B CE3 
3862 C CZ2 . TRP B 179 ? 0.2269 0.1911 0.3198 0.0437  0.0115  -0.0021 191 TRP B CZ2 
3863 C CZ3 . TRP B 179 ? 0.2343 0.1888 0.3249 0.0441  0.0161  -0.0010 191 TRP B CZ3 
3864 C CH2 . TRP B 179 ? 0.2065 0.1665 0.3013 0.0454  0.0136  -0.0025 191 TRP B CH2 
3865 N N   . ASN B 180 ? 0.1903 0.1386 0.2466 0.0310  0.0159  0.0120  192 ASN B N   
3866 C CA  . ASN B 180 ? 0.1610 0.1053 0.2116 0.0279  0.0182  0.0136  192 ASN B CA  
3867 C C   . ASN B 180 ? 0.1982 0.1447 0.2471 0.0222  0.0200  0.0126  192 ASN B C   
3868 O O   . ASN B 180 ? 0.1750 0.1265 0.2261 0.0210  0.0188  0.0115  192 ASN B O   
3869 C CB  . ASN B 180 ? 0.2059 0.1489 0.2515 0.0299  0.0159  0.0172  192 ASN B CB  
3870 C CG  . ASN B 180 ? 0.1893 0.1367 0.2328 0.0285  0.0135  0.0183  192 ASN B CG  
3871 O OD1 . ASN B 180 ? 0.1928 0.1406 0.2327 0.0243  0.0148  0.0189  192 ASN B OD1 
3872 N ND2 . ASN B 180 ? 0.1675 0.1184 0.2132 0.0321  0.0100  0.0186  192 ASN B ND2 
3873 N N   . ASP B 181 ? 0.1914 0.1343 0.2365 0.0187  0.0231  0.0131  193 ASP B N   
3874 C CA  . ASP B 181 ? 0.2082 0.1527 0.2507 0.0130  0.0250  0.0127  193 ASP B CA  
3875 C C   . ASP B 181 ? 0.2146 0.1578 0.2505 0.0113  0.0245  0.0159  193 ASP B C   
3876 O O   . ASP B 181 ? 0.2182 0.1611 0.2510 0.0065  0.0268  0.0160  193 ASP B O   
3877 C CB  . ASP B 181 ? 0.2371 0.1790 0.2806 0.0095  0.0292  0.0103  193 ASP B CB  
3878 C CG  . ASP B 181 ? 0.2956 0.2311 0.3356 0.0098  0.0314  0.0116  193 ASP B CG  
3879 O OD1 . ASP B 181 ? 0.2582 0.1915 0.2947 0.0124  0.0298  0.0144  193 ASP B OD1 
3880 O OD2 . ASP B 181 ? 0.3126 0.2454 0.3535 0.0075  0.0349  0.0097  193 ASP B OD2 
3881 N N   . HIS B 182 ? 0.2290 0.1716 0.2628 0.0151  0.0217  0.0185  194 HIS B N   
3882 C CA  . HIS B 182 ? 0.2403 0.1808 0.2677 0.0139  0.0214  0.0216  194 HIS B CA  
3883 C C   . HIS B 182 ? 0.2232 0.1678 0.2482 0.0102  0.0207  0.0225  194 HIS B C   
3884 O O   . HIS B 182 ? 0.1887 0.1381 0.2167 0.0104  0.0188  0.0216  194 HIS B O   
3885 C CB  . HIS B 182 ? 0.2593 0.1985 0.2853 0.0189  0.0183  0.0241  194 HIS B CB  
3886 C CG  . HIS B 182 ? 0.3031 0.2383 0.3312 0.0229  0.0188  0.0238  194 HIS B CG  
3887 N ND1 . HIS B 182 ? 0.2965 0.2312 0.3249 0.0280  0.0159  0.0255  194 HIS B ND1 
3888 C CD2 . HIS B 182 ? 0.2715 0.2031 0.3015 0.0224  0.0218  0.0221  194 HIS B CD2 
3889 C CE1 . HIS B 182 ? 0.3156 0.2466 0.3462 0.0306  0.0171  0.0249  194 HIS B CE1 
3890 N NE2 . HIS B 182 ? 0.2928 0.2219 0.3245 0.0274  0.0207  0.0229  194 HIS B NE2 
3891 N N   . VAL B 183 ? 0.2195 0.1926 0.2101 -0.0158 0.0169  -0.0114 195 VAL B N   
3892 C CA  . VAL B 183 ? 0.2012 0.1806 0.1934 -0.0162 0.0133  -0.0093 195 VAL B CA  
3893 C C   . VAL B 183 ? 0.2530 0.2310 0.2473 -0.0139 0.0144  -0.0081 195 VAL B C   
3894 O O   . VAL B 183 ? 0.2330 0.2088 0.2278 -0.0155 0.0178  -0.0098 195 VAL B O   
3895 C CB  . VAL B 183 ? 0.1819 0.1684 0.1740 -0.0218 0.0124  -0.0108 195 VAL B CB  
3896 C CG1 . VAL B 183 ? 0.1760 0.1695 0.1703 -0.0217 0.0087  -0.0080 195 VAL B CG1 
3897 C CG2 . VAL B 183 ? 0.1984 0.1861 0.1878 -0.0240 0.0118  -0.0120 195 VAL B CG2 
3898 N N   . HIS B 184 ? 0.1994 0.1782 0.1947 -0.0101 0.0117  -0.0051 196 HIS B N   
3899 C CA  . HIS B 184 ? 0.2267 0.2051 0.2239 -0.0077 0.0125  -0.0036 196 HIS B CA  
3900 C C   . HIS B 184 ? 0.1900 0.1750 0.1896 -0.0072 0.0091  -0.0011 196 HIS B C   
3901 O O   . HIS B 184 ? 0.1862 0.1728 0.1852 -0.0061 0.0059  0.0005  196 HIS B O   
3902 C CB  . HIS B 184 ? 0.1894 0.1608 0.1852 -0.0023 0.0134  -0.0024 196 HIS B CB  
3903 C CG  . HIS B 184 ? 0.2277 0.1926 0.2218 -0.0018 0.0173  -0.0041 196 HIS B CG  
3904 N ND1 . HIS B 184 ? 0.2254 0.1872 0.2177 -0.0021 0.0180  -0.0054 196 HIS B ND1 
3905 C CD2 . HIS B 184 ? 0.2732 0.2342 0.2675 -0.0008 0.0209  -0.0043 196 HIS B CD2 
3906 C CE1 . HIS B 184 ? 0.2993 0.2554 0.2908 -0.0010 0.0218  -0.0064 196 HIS B CE1 
3907 N NE2 . HIS B 184 ? 0.2551 0.2103 0.2475 -0.0004 0.0237  -0.0057 196 HIS B NE2 
3908 N N   . ILE B 185 ? 0.2340 0.2226 0.2365 -0.0078 0.0101  -0.0006 197 ILE B N   
3909 C CA  . ILE B 185 ? 0.1783 0.1732 0.1839 -0.0067 0.0074  0.0021  197 ILE B CA  
3910 C C   . ILE B 185 ? 0.1838 0.1749 0.1900 -0.0015 0.0085  0.0039  197 ILE B C   
3911 O O   . ILE B 185 ? 0.2146 0.2020 0.2208 -0.0009 0.0120  0.0030  197 ILE B O   
3912 C CB  . ILE B 185 ? 0.1826 0.1857 0.1916 -0.0113 0.0076  0.0014  197 ILE B CB  
3913 C CG1 . ILE B 185 ? 0.2031 0.2106 0.2107 -0.0165 0.0062  -0.0004 197 ILE B CG1 
3914 C CG2 . ILE B 185 ? 0.2293 0.2392 0.2424 -0.0092 0.0055  0.0046  197 ILE B CG2 
3915 C CD1 . ILE B 185 ? 0.2015 0.2153 0.2113 -0.0219 0.0072  -0.0024 197 ILE B CD1 
3916 N N   . LEU B 186 ? 0.1728 0.1642 0.1791 0.0022  0.0058  0.0064  198 LEU B N   
3917 C CA  . LEU B 186 ? 0.2004 0.1902 0.2079 0.0068  0.0066  0.0083  198 LEU B CA  
3918 C C   . LEU B 186 ? 0.1726 0.1709 0.1847 0.0066  0.0049  0.0106  198 LEU B C   
3919 O O   . LEU B 186 ? 0.1968 0.1981 0.2092 0.0071  0.0016  0.0124  198 LEU B O   
3920 C CB  . LEU B 186 ? 0.2046 0.1876 0.2087 0.0116  0.0052  0.0093  198 LEU B CB  
3921 C CG  . LEU B 186 ? 0.2744 0.2535 0.2779 0.0167  0.0066  0.0105  198 LEU B CG  
3922 C CD1 . LEU B 186 ? 0.2830 0.2658 0.2892 0.0193  0.0047  0.0131  198 LEU B CD1 
3923 C CD2 . LEU B 186 ? 0.2226 0.2011 0.2271 0.0165  0.0108  0.0098  198 LEU B CD2 
3924 N N   . ASP B 187 ? 0.2054 0.2075 0.2210 0.0061  0.0072  0.0109  199 ASP B N   
3925 C CA  . ASP B 187 ? 0.2165 0.2277 0.2374 0.0061  0.0058  0.0132  199 ASP B CA  
3926 C C   . ASP B 187 ? 0.2437 0.2524 0.2651 0.0122  0.0059  0.0157  199 ASP B C   
3927 O O   . ASP B 187 ? 0.2203 0.2250 0.2413 0.0149  0.0091  0.0155  199 ASP B O   
3928 C CB  . ASP B 187 ? 0.2380 0.2552 0.2630 0.0022  0.0083  0.0121  199 ASP B CB  
3929 C CG  . ASP B 187 ? 0.2699 0.2982 0.3010 0.0014  0.0066  0.0145  199 ASP B CG  
3930 O OD1 . ASP B 187 ? 0.2873 0.3177 0.3200 0.0056  0.0045  0.0175  199 ASP B OD1 
3931 O OD2 . ASP B 187 ? 0.2959 0.3311 0.3305 -0.0034 0.0073  0.0134  199 ASP B OD2 
3932 N N   . THR B 188 ? 0.2383 0.2490 0.2604 0.0145  0.0027  0.0181  200 THR B N   
3933 C CA  . THR B 188 ? 0.2227 0.2300 0.2448 0.0204  0.0029  0.0203  200 THR B CA  
3934 C C   . THR B 188 ? 0.2250 0.2390 0.2529 0.0223  0.0047  0.0222  200 THR B C   
3935 O O   . THR B 188 ? 0.2223 0.2332 0.2502 0.0275  0.0057  0.0238  200 THR B O   
3936 C CB  . THR B 188 ? 0.2097 0.2162 0.2307 0.0224  -0.0008 0.0223  200 THR B CB  
3937 O OG1 . THR B 188 ? 0.2507 0.2669 0.2758 0.0196  -0.0034 0.0243  200 THR B OG1 
3938 C CG2 . THR B 188 ? 0.2499 0.2489 0.2654 0.0213  -0.0021 0.0205  200 THR B CG2 
3939 N N   . GLU B 189 ? 0.2439 0.2668 0.2765 0.0181  0.0052  0.0221  201 GLU B N   
3940 C CA  . GLU B 189 ? 0.1996 0.2291 0.2381 0.0196  0.0074  0.0238  201 GLU B CA  
3941 C C   . GLU B 189 ? 0.2301 0.2534 0.2670 0.0214  0.0121  0.0224  201 GLU B C   
3942 O O   . GLU B 189 ? 0.2106 0.2355 0.2505 0.0251  0.0144  0.0241  201 GLU B O   
3943 C CB  . GLU B 189 ? 0.2265 0.2678 0.2707 0.0140  0.0066  0.0238  201 GLU B CB  
3944 C CG  . GLU B 189 ? 0.1961 0.2460 0.2431 0.0128  0.0021  0.0262  201 GLU B CG  
3945 C CD  . GLU B 189 ? 0.2812 0.3423 0.3324 0.0062  0.0008  0.0253  201 GLU B CD  
3946 O OE1 . GLU B 189 ? 0.3202 0.3836 0.3738 0.0029  0.0037  0.0234  201 GLU B OE1 
3947 O OE2 . GLU B 189 ? 0.2176 0.2852 0.2693 0.0041  -0.0031 0.0266  201 GLU B OE2 
3948 N N   . THR B 190 ? 0.2688 0.2856 0.3012 0.0189  0.0137  0.0195  202 THR B N   
3949 C CA  . THR B 190 ? 0.2681 0.2788 0.2984 0.0204  0.0181  0.0185  202 THR B CA  
3950 C C   . THR B 190 ? 0.3071 0.3063 0.3298 0.0225  0.0186  0.0167  202 THR B C   
3951 O O   . THR B 190 ? 0.2778 0.2713 0.2979 0.0244  0.0222  0.0162  202 THR B O   
3952 C CB  . THR B 190 ? 0.2561 0.2711 0.2897 0.0150  0.0208  0.0169  202 THR B CB  
3953 O OG1 . THR B 190 ? 0.3022 0.3155 0.3331 0.0102  0.0195  0.0144  202 THR B OG1 
3954 C CG2 . THR B 190 ? 0.2562 0.2838 0.2980 0.0127  0.0202  0.0186  202 THR B CG2 
3955 N N   . PHE B 191 ? 0.2599 0.2560 0.2792 0.0223  0.0152  0.0162  203 PHE B N   
3956 C CA  . PHE B 191 ? 0.2468 0.2333 0.2595 0.0234  0.0151  0.0144  203 PHE B CA  
3957 C C   . PHE B 191 ? 0.3165 0.3000 0.3277 0.0205  0.0182  0.0124  203 PHE B C   
3958 O O   . PHE B 191 ? 0.3148 0.2916 0.3223 0.0229  0.0209  0.0119  203 PHE B O   
3959 C CB  . PHE B 191 ? 0.2639 0.2434 0.2726 0.0294  0.0156  0.0152  203 PHE B CB  
3960 C CG  . PHE B 191 ? 0.2902 0.2706 0.2996 0.0323  0.0126  0.0168  203 PHE B CG  
3961 C CD1 . PHE B 191 ? 0.2752 0.2526 0.2818 0.0320  0.0090  0.0165  203 PHE B CD1 
3962 C CD2 . PHE B 191 ? 0.3234 0.3079 0.3366 0.0353  0.0135  0.0190  203 PHE B CD2 
3963 C CE1 . PHE B 191 ? 0.3134 0.2909 0.3206 0.0345  0.0065  0.0182  203 PHE B CE1 
3964 C CE2 . PHE B 191 ? 0.3164 0.3010 0.3303 0.0383  0.0110  0.0207  203 PHE B CE2 
3965 C CZ  . PHE B 191 ? 0.3201 0.3010 0.3310 0.0378  0.0075  0.0203  203 PHE B CZ  
3966 N N   . THR B 192 ? 0.2169 0.2054 0.2307 0.0151  0.0179  0.0112  204 THR B N   
3967 C CA  . THR B 192 ? 0.2679 0.2541 0.2811 0.0115  0.0211  0.0091  204 THR B CA  
3968 C C   . THR B 192 ? 0.2629 0.2480 0.2740 0.0078  0.0193  0.0070  204 THR B C   
3969 O O   . THR B 192 ? 0.2744 0.2657 0.2875 0.0048  0.0164  0.0069  204 THR B O   
3970 C CB  . THR B 192 ? 0.2844 0.2778 0.3032 0.0078  0.0233  0.0091  204 THR B CB  
3971 O OG1 . THR B 192 ? 0.2912 0.2850 0.3120 0.0113  0.0259  0.0110  204 THR B OG1 
3972 C CG2 . THR B 192 ? 0.3027 0.2933 0.3209 0.0032  0.0265  0.0066  204 THR B CG2 
3973 N N   . TRP B 193 ? 0.2592 0.2366 0.2662 0.0082  0.0212  0.0055  205 TRP B N   
3974 C CA  . TRP B 193 ? 0.2660 0.2418 0.2710 0.0050  0.0203  0.0034  205 TRP B CA  
3975 C C   . TRP B 193 ? 0.2719 0.2506 0.2792 -0.0007 0.0228  0.0012  205 TRP B C   
3976 O O   . TRP B 193 ? 0.2762 0.2543 0.2853 -0.0017 0.0264  0.0011  205 TRP B O   
3977 C CB  . TRP B 193 ? 0.2713 0.2383 0.2717 0.0080  0.0216  0.0029  205 TRP B CB  
3978 C CG  . TRP B 193 ? 0.3009 0.2648 0.2983 0.0126  0.0187  0.0042  205 TRP B CG  
3979 C CD1 . TRP B 193 ? 0.2716 0.2308 0.2664 0.0175  0.0194  0.0056  205 TRP B CD1 
3980 C CD2 . TRP B 193 ? 0.2889 0.2538 0.2853 0.0125  0.0148  0.0043  205 TRP B CD2 
3981 N NE1 . TRP B 193 ? 0.2785 0.2358 0.2709 0.0203  0.0159  0.0061  205 TRP B NE1 
3982 C CE2 . TRP B 193 ? 0.2877 0.2484 0.2813 0.0173  0.0132  0.0055  205 TRP B CE2 
3983 C CE3 . TRP B 193 ? 0.2535 0.2225 0.2509 0.0088  0.0126  0.0034  205 TRP B CE3 
3984 C CZ2 . TRP B 193 ? 0.2948 0.2550 0.2871 0.0181  0.0095  0.0058  205 TRP B CZ2 
3985 C CZ3 . TRP B 193 ? 0.2378 0.2064 0.2337 0.0099  0.0091  0.0040  205 TRP B CZ3 
3986 C CH2 . TRP B 193 ? 0.2367 0.2010 0.2305 0.0144  0.0076  0.0052  205 TRP B CH2 
3987 N N   . SER B 194 ? 0.2449 0.2263 0.2519 -0.0047 0.0210  -0.0005 206 SER B N   
3988 C CA  . SER B 194 ? 0.2692 0.2528 0.2775 -0.0106 0.0230  -0.0033 206 SER B CA  
3989 C C   . SER B 194 ? 0.2705 0.2534 0.2760 -0.0131 0.0213  -0.0052 206 SER B C   
3990 O O   . SER B 194 ? 0.2367 0.2198 0.2405 -0.0107 0.0181  -0.0040 206 SER B O   
3991 C CB  . SER B 194 ? 0.2620 0.2553 0.2751 -0.0143 0.0219  -0.0029 206 SER B CB  
3992 O OG  . SER B 194 ? 0.3210 0.3213 0.3346 -0.0156 0.0174  -0.0022 206 SER B OG  
3993 N N   . GLN B 195 ? 0.2737 0.2556 0.2786 -0.0179 0.0238  -0.0084 207 GLN B N   
3994 C CA  . GLN B 195 ? 0.2854 0.2680 0.2878 -0.0209 0.0224  -0.0105 207 GLN B CA  
3995 C C   . GLN B 195 ? 0.2500 0.2398 0.2539 -0.0275 0.0219  -0.0128 207 GLN B C   
3996 O O   . GLN B 195 ? 0.3017 0.2919 0.3076 -0.0309 0.0248  -0.0145 207 GLN B O   
3997 C CB  . GLN B 195 ? 0.3199 0.2936 0.3191 -0.0203 0.0260  -0.0126 207 GLN B CB  
3998 C CG  . GLN B 195 ? 0.3087 0.2758 0.3061 -0.0141 0.0262  -0.0105 207 GLN B CG  
3999 C CD  . GLN B 195 ? 0.3189 0.2786 0.3135 -0.0134 0.0290  -0.0122 207 GLN B CD  
4000 O OE1 . GLN B 195 ? 0.3445 0.2979 0.3387 -0.0124 0.0331  -0.0127 207 GLN B OE1 
4001 N NE2 . GLN B 195 ? 0.3285 0.2892 0.3216 -0.0139 0.0272  -0.0130 207 GLN B NE2 
4002 N N   . PRO B 196 ? 0.2439 0.2393 0.2467 -0.0297 0.0185  -0.0131 208 PRO B N   
4003 C CA  . PRO B 196 ? 0.2692 0.2720 0.2726 -0.0362 0.0177  -0.0155 208 PRO B CA  
4004 C C   . PRO B 196 ? 0.2853 0.2833 0.2852 -0.0406 0.0209  -0.0200 208 PRO B C   
4005 O O   . PRO B 196 ? 0.2852 0.2766 0.2819 -0.0387 0.0224  -0.0209 208 PRO B O   
4006 C CB  . PRO B 196 ? 0.2304 0.2406 0.2333 -0.0360 0.0126  -0.0133 208 PRO B CB  
4007 C CG  . PRO B 196 ? 0.2650 0.2688 0.2650 -0.0312 0.0121  -0.0118 208 PRO B CG  
4008 C CD  . PRO B 196 ? 0.2288 0.2250 0.2298 -0.0264 0.0149  -0.0108 208 PRO B CD  
4009 N N   . ILE B 197 ? 0.3091 0.3110 0.3100 -0.0467 0.0220  -0.0230 209 ILE B N   
4010 C CA  . ILE B 197 ? 0.3266 0.3250 0.3239 -0.0517 0.0248  -0.0278 209 ILE B CA  
4011 C C   . ILE B 197 ? 0.3068 0.3114 0.3009 -0.0542 0.0212  -0.0284 209 ILE B C   
4012 O O   . ILE B 197 ? 0.2641 0.2785 0.2593 -0.0579 0.0178  -0.0282 209 ILE B O   
4013 C CB  . ILE B 197 ? 0.3088 0.3089 0.3081 -0.0579 0.0273  -0.0311 209 ILE B CB  
4014 C CG1 . ILE B 197 ? 0.3563 0.3506 0.3589 -0.0553 0.0309  -0.0298 209 ILE B CG1 
4015 C CG2 . ILE B 197 ? 0.3293 0.3240 0.3243 -0.0629 0.0308  -0.0365 209 ILE B CG2 
4016 C CD1 . ILE B 197 ? 0.3660 0.3479 0.3659 -0.0510 0.0353  -0.0301 209 ILE B CD1 
4017 N N   . THR B 198 ? 0.3547 0.3540 0.3450 -0.0521 0.0219  -0.0289 210 THR B N   
4018 C CA  . THR B 198 ? 0.3129 0.3172 0.2997 -0.0539 0.0190  -0.0292 210 THR B CA  
4019 C C   . THR B 198 ? 0.3487 0.3510 0.3312 -0.0596 0.0219  -0.0346 210 THR B C   
4020 O O   . THR B 198 ? 0.3972 0.3911 0.3787 -0.0604 0.0268  -0.0379 210 THR B O   
4021 C CB  . THR B 198 ? 0.3224 0.3231 0.3078 -0.0485 0.0179  -0.0265 210 THR B CB  
4022 O OG1 . THR B 198 ? 0.3507 0.3416 0.3343 -0.0466 0.0225  -0.0286 210 THR B OG1 
4023 C CG2 . THR B 198 ? 0.2722 0.2741 0.2612 -0.0429 0.0151  -0.0215 210 THR B CG2 
4024 N N   . THR B 199 ? 0.3083 0.3178 0.2877 -0.0633 0.0190  -0.0354 211 THR B N   
4025 C CA  . THR B 199 ? 0.3292 0.3370 0.3032 -0.0682 0.0213  -0.0404 211 THR B CA  
4026 C C   . THR B 199 ? 0.3270 0.3356 0.2973 -0.0663 0.0198  -0.0390 211 THR B C   
4027 O O   . THR B 199 ? 0.3254 0.3369 0.2973 -0.0620 0.0164  -0.0342 211 THR B O   
4028 C CB  . THR B 199 ? 0.3424 0.3587 0.3152 -0.0755 0.0195  -0.0433 211 THR B CB  
4029 O OG1 . THR B 199 ? 0.3356 0.3630 0.3094 -0.0753 0.0136  -0.0392 211 THR B OG1 
4030 C CG2 . THR B 199 ? 0.4030 0.4183 0.3798 -0.0781 0.0214  -0.0450 211 THR B CG2 
4031 N N   . GLY B 200 ? 0.3612 0.3670 0.3263 -0.0698 0.0227  -0.0434 212 GLY B N   
4032 C CA  . GLY B 200 ? 0.3097 0.3151 0.2712 -0.0681 0.0225  -0.0426 212 GLY B CA  
4033 C C   . GLY B 200 ? 0.3514 0.3472 0.3141 -0.0627 0.0263  -0.0421 212 GLY B C   
4034 O O   . GLY B 200 ? 0.3555 0.3450 0.3216 -0.0597 0.0286  -0.0417 212 GLY B O   
4035 N N   . LYS B 201 ? 0.3665 0.3613 0.3263 -0.0614 0.0271  -0.0420 213 LYS B N   
4036 C CA  . LYS B 201 ? 0.3583 0.3456 0.3198 -0.0560 0.0300  -0.0409 213 LYS B CA  
4037 C C   . LYS B 201 ? 0.3227 0.3126 0.2880 -0.0508 0.0258  -0.0350 213 LYS B C   
4038 O O   . LYS B 201 ? 0.3248 0.3210 0.2891 -0.0511 0.0220  -0.0323 213 LYS B O   
4039 C CB  . LYS B 201 ? 0.3971 0.3822 0.3544 -0.0568 0.0331  -0.0434 213 LYS B CB  
4040 C CG  . LYS B 201 ? 0.4353 0.4126 0.3950 -0.0515 0.0369  -0.0429 213 LYS B CG  
4041 C CD  . LYS B 201 ? 0.4721 0.4453 0.4280 -0.0530 0.0421  -0.0472 213 LYS B CD  
4042 C CE  . LYS B 201 ? 0.4888 0.4632 0.4451 -0.0496 0.0420  -0.0446 213 LYS B CE  
4043 N NZ  . LYS B 201 ? 0.5073 0.4774 0.4605 -0.0504 0.0476  -0.0487 213 LYS B NZ  
4044 N N   . ALA B 202 ? 0.3551 0.3399 0.3244 -0.0463 0.0265  -0.0331 214 ALA B N   
4045 C CA  . ALA B 202 ? 0.2975 0.2835 0.2700 -0.0413 0.0230  -0.0282 214 ALA B CA  
4046 C C   . ALA B 202 ? 0.2878 0.2722 0.2598 -0.0386 0.0236  -0.0271 214 ALA B C   
4047 O O   . ALA B 202 ? 0.3473 0.3282 0.3173 -0.0395 0.0275  -0.0301 214 ALA B O   
4048 C CB  . ALA B 202 ? 0.3038 0.2846 0.2800 -0.0374 0.0239  -0.0268 214 ALA B CB  
4049 N N   . PRO B 203 ? 0.2656 0.2525 0.2395 -0.0355 0.0199  -0.0229 215 PRO B N   
4050 C CA  . PRO B 203 ? 0.2706 0.2556 0.2450 -0.0326 0.0206  -0.0217 215 PRO B CA  
4051 C C   . PRO B 203 ? 0.2538 0.2316 0.2305 -0.0287 0.0240  -0.0225 215 PRO B C   
4052 O O   . PRO B 203 ? 0.2747 0.2489 0.2528 -0.0274 0.0249  -0.0228 215 PRO B O   
4053 C CB  . PRO B 203 ? 0.2479 0.2364 0.2244 -0.0302 0.0158  -0.0171 215 PRO B CB  
4054 C CG  . PRO B 203 ? 0.2295 0.2225 0.2059 -0.0321 0.0126  -0.0159 215 PRO B CG  
4055 C CD  . PRO B 203 ? 0.2526 0.2434 0.2287 -0.0339 0.0152  -0.0190 215 PRO B CD  
4056 N N   . SER B 204 ? 0.2261 0.2022 0.2034 -0.0267 0.0258  -0.0224 216 SER B N   
4057 C CA  . SER B 204 ? 0.1679 0.1379 0.1477 -0.0224 0.0286  -0.0225 216 SER B CA  
4058 C C   . SER B 204 ? 0.2135 0.1826 0.1963 -0.0182 0.0253  -0.0190 216 SER B C   
4059 O O   . SER B 204 ? 0.2178 0.1908 0.2012 -0.0182 0.0210  -0.0163 216 SER B O   
4060 C CB  . SER B 204 ? 0.2161 0.1861 0.1968 -0.0208 0.0306  -0.0225 216 SER B CB  
4061 O OG  . SER B 204 ? 0.2254 0.1992 0.2082 -0.0190 0.0266  -0.0189 216 SER B OG  
4062 N N   . PRO B 205 ? 0.2557 0.2193 0.2402 -0.0145 0.0274  -0.0188 217 PRO B N   
4063 C CA  . PRO B 205 ? 0.2231 0.1857 0.2099 -0.0101 0.0244  -0.0156 217 PRO B CA  
4064 C C   . PRO B 205 ? 0.2421 0.2083 0.2304 -0.0088 0.0211  -0.0132 217 PRO B C   
4065 O O   . PRO B 205 ? 0.2241 0.1916 0.2129 -0.0093 0.0226  -0.0138 217 PRO B O   
4066 C CB  . PRO B 205 ? 0.2605 0.2170 0.2485 -0.0064 0.0280  -0.0160 217 PRO B CB  
4067 C CG  . PRO B 205 ? 0.2510 0.2044 0.2371 -0.0094 0.0327  -0.0195 217 PRO B CG  
4068 C CD  . PRO B 205 ? 0.2776 0.2354 0.2617 -0.0140 0.0327  -0.0215 217 PRO B CD  
4069 N N   . ARG B 206 ? 0.2235 0.1912 0.2126 -0.0074 0.0169  -0.0106 218 ARG B N   
4070 C CA  . ARG B 206 ? 0.2378 0.2084 0.2284 -0.0066 0.0137  -0.0083 218 ARG B CA  
4071 C C   . ARG B 206 ? 0.1828 0.1523 0.1744 -0.0037 0.0099  -0.0059 218 ARG B C   
4072 O O   . ARG B 206 ? 0.2135 0.1812 0.2043 -0.0029 0.0095  -0.0056 218 ARG B O   
4073 C CB  . ARG B 206 ? 0.2121 0.1877 0.2014 -0.0106 0.0122  -0.0081 218 ARG B CB  
4074 C CG  . ARG B 206 ? 0.1911 0.1688 0.1786 -0.0129 0.0102  -0.0077 218 ARG B CG  
4075 C CD  . ARG B 206 ? 0.2144 0.1972 0.1999 -0.0171 0.0096  -0.0078 218 ARG B CD  
4076 N NE  . ARG B 206 ? 0.2189 0.2017 0.2023 -0.0198 0.0136  -0.0111 218 ARG B NE  
4077 C CZ  . ARG B 206 ? 0.2388 0.2254 0.2199 -0.0233 0.0143  -0.0119 218 ARG B CZ  
4078 N NH1 . ARG B 206 ? 0.1882 0.1789 0.1689 -0.0244 0.0113  -0.0093 218 ARG B NH1 
4079 N NH2 . ARG B 206 ? 0.2370 0.2228 0.2159 -0.0256 0.0183  -0.0155 218 ARG B NH2 
4080 N N   . ALA B 207 ? 0.1427 0.1133 0.1360 -0.0023 0.0074  -0.0041 219 ALA B N   
4081 C CA  . ALA B 207 ? 0.1591 0.1291 0.1528 -0.0004 0.0034  -0.0020 219 ALA B CA  
4082 C C   . ALA B 207 ? 0.1843 0.1575 0.1789 -0.0022 0.0007  -0.0004 219 ALA B C   
4083 O O   . ALA B 207 ? 0.1844 0.1604 0.1799 -0.0042 0.0019  -0.0008 219 ALA B O   
4084 C CB  . ALA B 207 ? 0.1786 0.1452 0.1732 0.0038  0.0031  -0.0015 219 ALA B CB  
4085 N N   . ALA B 208 ? 0.1500 0.1225 0.1445 -0.0014 -0.0029 0.0014  220 ALA B N   
4086 C CA  . ALA B 208 ? 0.1506 0.1252 0.1460 -0.0030 -0.0056 0.0033  220 ALA B CA  
4087 C C   . ALA B 208 ? 0.1630 0.1415 0.1573 -0.0068 -0.0050 0.0036  220 ALA B C   
4088 O O   . ALA B 208 ? 0.1421 0.1230 0.1372 -0.0088 -0.0059 0.0049  220 ALA B O   
4089 C CB  . ALA B 208 ? 0.1920 0.1673 0.1900 -0.0024 -0.0061 0.0035  220 ALA B CB  
4090 N N   . HIS B 209 ? 0.1527 0.1320 0.1451 -0.0080 -0.0034 0.0025  221 HIS B N   
4091 C CA  . HIS B 209 ? 0.1765 0.1597 0.1671 -0.0114 -0.0036 0.0031  221 HIS B CA  
4092 C C   . HIS B 209 ? 0.1795 0.1629 0.1699 -0.0109 -0.0071 0.0059  221 HIS B C   
4093 O O   . HIS B 209 ? 0.1851 0.1650 0.1764 -0.0080 -0.0089 0.0069  221 HIS B O   
4094 C CB  . HIS B 209 ? 0.1461 0.1302 0.1350 -0.0128 -0.0010 0.0008  221 HIS B CB  
4095 C CG  . HIS B 209 ? 0.1724 0.1532 0.1616 -0.0103 -0.0006 0.0001  221 HIS B CG  
4096 N ND1 . HIS B 209 ? 0.1663 0.1429 0.1565 -0.0073 0.0009  -0.0010 221 HIS B ND1 
4097 C CD2 . HIS B 209 ? 0.1792 0.1607 0.1680 -0.0103 -0.0015 0.0005  221 HIS B CD2 
4098 C CE1 . HIS B 209 ? 0.1716 0.1460 0.1616 -0.0056 0.0012  -0.0012 221 HIS B CE1 
4099 N NE2 . HIS B 209 ? 0.1556 0.1330 0.1450 -0.0074 -0.0002 -0.0004 221 HIS B NE2 
4100 N N   . ALA B 210 ? 0.1724 0.1598 0.1614 -0.0136 -0.0080 0.0073  222 ALA B N   
4101 C CA  . ALA B 210 ? 0.1736 0.1616 0.1625 -0.0130 -0.0109 0.0102  222 ALA B CA  
4102 C C   . ALA B 210 ? 0.1787 0.1707 0.1662 -0.0146 -0.0107 0.0100  222 ALA B C   
4103 O O   . ALA B 210 ? 0.1787 0.1746 0.1644 -0.0178 -0.0092 0.0087  222 ALA B O   
4104 C CB  . ALA B 210 ? 0.1979 0.1870 0.1867 -0.0143 -0.0128 0.0132  222 ALA B CB  
4105 N N   . CYS B 211 ? 0.2122 0.2035 0.2006 -0.0124 -0.0122 0.0113  223 CYS B N   
4106 C CA  . CYS B 211 ? 0.1970 0.1929 0.1851 -0.0137 -0.0125 0.0115  223 CYS B CA  
4107 C C   . CYS B 211 ? 0.1892 0.1877 0.1776 -0.0131 -0.0155 0.0155  223 CYS B C   
4108 O O   . CYS B 211 ? 0.1962 0.1909 0.1858 -0.0104 -0.0171 0.0177  223 CYS B O   
4109 C CB  . CYS B 211 ? 0.1816 0.1752 0.1709 -0.0115 -0.0112 0.0098  223 CYS B CB  
4110 S SG  . CYS B 211 ? 0.1986 0.1900 0.1872 -0.0126 -0.0072 0.0054  223 CYS B SG  
4111 N N   . ALA B 212 ? 0.1735 0.1787 0.1610 -0.0157 -0.0163 0.0165  224 ALA B N   
4112 C CA  . ALA B 212 ? 0.1997 0.2082 0.1879 -0.0148 -0.0191 0.0207  224 ALA B CA  
4113 C C   . ALA B 212 ? 0.1769 0.1926 0.1653 -0.0165 -0.0197 0.0207  224 ALA B C   
4114 O O   . ALA B 212 ? 0.1836 0.2030 0.1703 -0.0202 -0.0183 0.0179  224 ALA B O   
4115 C CB  . ALA B 212 ? 0.2411 0.2510 0.2274 -0.0166 -0.0204 0.0234  224 ALA B CB  
4116 N N   . THR B 213 ? 0.2099 0.2278 0.2007 -0.0141 -0.0216 0.0238  225 THR B N   
4117 C CA  . THR B 213 ? 0.1832 0.2088 0.1754 -0.0153 -0.0224 0.0241  225 THR B CA  
4118 C C   . THR B 213 ? 0.1667 0.1989 0.1588 -0.0157 -0.0254 0.0287  225 THR B C   
4119 O O   . THR B 213 ? 0.1813 0.2109 0.1745 -0.0124 -0.0270 0.0326  225 THR B O   
4120 C CB  . THR B 213 ? 0.1687 0.1926 0.1647 -0.0118 -0.0218 0.0239  225 THR B CB  
4121 O OG1 . THR B 213 ? 0.2034 0.2206 0.1991 -0.0111 -0.0190 0.0201  225 THR B OG1 
4122 C CG2 . THR B 213 ? 0.2418 0.2743 0.2400 -0.0136 -0.0223 0.0238  225 THR B CG2 
4123 N N   . VAL B 214 ? 0.2244 0.2650 0.2149 -0.0196 -0.0263 0.0283  226 VAL B N   
4124 C CA  . VAL B 214 ? 0.2505 0.2991 0.2410 -0.0199 -0.0294 0.0329  226 VAL B CA  
4125 C C   . VAL B 214 ? 0.2428 0.3008 0.2347 -0.0225 -0.0303 0.0317  226 VAL B C   
4126 O O   . VAL B 214 ? 0.2139 0.2750 0.2032 -0.0272 -0.0291 0.0277  226 VAL B O   
4127 C CB  . VAL B 214 ? 0.2295 0.2798 0.2153 -0.0228 -0.0303 0.0344  226 VAL B CB  
4128 C CG1 . VAL B 214 ? 0.2632 0.3218 0.2489 -0.0226 -0.0337 0.0397  226 VAL B CG1 
4129 C CG2 . VAL B 214 ? 0.1776 0.2188 0.1627 -0.0204 -0.0294 0.0356  226 VAL B CG2 
4130 N N   . GLY B 215 ? 0.3053 0.3679 0.3017 -0.0196 -0.0321 0.0351  227 GLY B N   
4131 C CA  . GLY B 215 ? 0.2944 0.3663 0.2934 -0.0218 -0.0329 0.0341  227 GLY B CA  
4132 C C   . GLY B 215 ? 0.2391 0.3071 0.2388 -0.0236 -0.0296 0.0284  227 GLY B C   
4133 O O   . GLY B 215 ? 0.3396 0.3991 0.3409 -0.0204 -0.0273 0.0271  227 GLY B O   
4134 N N   . ASN B 216 ? 0.2389 0.3127 0.2370 -0.0290 -0.0292 0.0247  228 ASN B N   
4135 C CA  . ASN B 216 ? 0.2242 0.2943 0.2226 -0.0314 -0.0258 0.0192  228 ASN B CA  
4136 C C   . ASN B 216 ? 0.2069 0.2701 0.2000 -0.0342 -0.0230 0.0149  228 ASN B C   
4137 O O   . ASN B 216 ? 0.1916 0.2539 0.1836 -0.0379 -0.0205 0.0101  228 ASN B O   
4138 C CB  . ASN B 216 ? 0.2808 0.3608 0.2812 -0.0359 -0.0266 0.0174  228 ASN B CB  
4139 C CG  . ASN B 216 ? 0.2468 0.3343 0.2423 -0.0415 -0.0285 0.0163  228 ASN B CG  
4140 O OD1 . ASN B 216 ? 0.2364 0.3218 0.2271 -0.0419 -0.0290 0.0172  228 ASN B OD1 
4141 N ND2 . ASN B 216 ? 0.2916 0.3880 0.2883 -0.0461 -0.0294 0.0142  228 ASN B ND2 
4142 N N   . ARG B 217 ? 0.2021 0.2608 0.1921 -0.0327 -0.0234 0.0166  229 ARG B N   
4143 C CA  . ARG B 217 ? 0.1972 0.2497 0.1829 -0.0348 -0.0206 0.0129  229 ARG B CA  
4144 C C   . ARG B 217 ? 0.1832 0.2258 0.1701 -0.0302 -0.0190 0.0135  229 ARG B C   
4145 O O   . ARG B 217 ? 0.2179 0.2587 0.2054 -0.0270 -0.0209 0.0175  229 ARG B O   
4146 C CB  . ARG B 217 ? 0.2009 0.2572 0.1816 -0.0378 -0.0220 0.0140  229 ARG B CB  
4147 C CG  . ARG B 217 ? 0.2074 0.2737 0.1859 -0.0428 -0.0237 0.0129  229 ARG B CG  
4148 C CD  . ARG B 217 ? 0.2591 0.3285 0.2316 -0.0461 -0.0243 0.0131  229 ARG B CD  
4149 N NE  . ARG B 217 ? 0.2410 0.3209 0.2110 -0.0508 -0.0266 0.0127  229 ARG B NE  
4150 C CZ  . ARG B 217 ? 0.2611 0.3448 0.2248 -0.0551 -0.0267 0.0112  229 ARG B CZ  
4151 N NH1 . ARG B 217 ? 0.2647 0.3426 0.2241 -0.0555 -0.0243 0.0100  229 ARG B NH1 
4152 N NH2 . ARG B 217 ? 0.3055 0.3994 0.2671 -0.0593 -0.0293 0.0108  229 ARG B NH2 
4153 N N   . GLY B 218 ? 0.1813 0.2174 0.1683 -0.0301 -0.0157 0.0096  230 GLY B N   
4154 C CA  . GLY B 218 ? 0.2149 0.2421 0.2024 -0.0264 -0.0142 0.0095  230 GLY B CA  
4155 C C   . GLY B 218 ? 0.1813 0.2051 0.1652 -0.0283 -0.0123 0.0073  230 GLY B C   
4156 O O   . GLY B 218 ? 0.1903 0.2120 0.1727 -0.0306 -0.0092 0.0032  230 GLY B O   
4157 N N   . PHE B 219 ? 0.1933 0.2165 0.1760 -0.0274 -0.0138 0.0101  231 PHE B N   
4158 C CA  . PHE B 219 ? 0.1807 0.2016 0.1604 -0.0292 -0.0120 0.0085  231 PHE B CA  
4159 C C   . PHE B 219 ? 0.2082 0.2212 0.1895 -0.0262 -0.0099 0.0071  231 PHE B C   
4160 O O   . PHE B 219 ? 0.2339 0.2430 0.2179 -0.0224 -0.0109 0.0086  231 PHE B O   
4161 C CB  . PHE B 219 ? 0.1458 0.1694 0.1238 -0.0296 -0.0143 0.0123  231 PHE B CB  
4162 C CG  . PHE B 219 ? 0.2119 0.2438 0.1876 -0.0327 -0.0165 0.0140  231 PHE B CG  
4163 C CD1 . PHE B 219 ? 0.2169 0.2531 0.1947 -0.0311 -0.0196 0.0178  231 PHE B CD1 
4164 C CD2 . PHE B 219 ? 0.2075 0.2432 0.1787 -0.0371 -0.0152 0.0118  231 PHE B CD2 
4165 C CE1 . PHE B 219 ? 0.2297 0.2743 0.2054 -0.0337 -0.0219 0.0197  231 PHE B CE1 
4166 C CE2 . PHE B 219 ? 0.2161 0.2600 0.1846 -0.0401 -0.0175 0.0133  231 PHE B CE2 
4167 C CZ  . PHE B 219 ? 0.2138 0.2624 0.1846 -0.0384 -0.0210 0.0174  231 PHE B CZ  
4168 N N   . VAL B 220 ? 0.1998 0.2106 0.1793 -0.0278 -0.0070 0.0040  232 VAL B N   
4169 C CA  . VAL B 220 ? 0.2015 0.2059 0.1825 -0.0251 -0.0052 0.0030  232 VAL B CA  
4170 C C   . VAL B 220 ? 0.2009 0.2058 0.1799 -0.0271 -0.0036 0.0023  232 VAL B C   
4171 O O   . VAL B 220 ? 0.1956 0.2037 0.1716 -0.0307 -0.0019 0.0001  232 VAL B O   
4172 C CB  . VAL B 220 ? 0.1926 0.1929 0.1747 -0.0240 -0.0023 -0.0003 232 VAL B CB  
4173 C CG1 . VAL B 220 ? 0.1959 0.1977 0.1755 -0.0279 0.0009  -0.0043 232 VAL B CG1 
4174 C CG2 . VAL B 220 ? 0.1964 0.1908 0.1801 -0.0207 -0.0010 -0.0007 232 VAL B CG2 
4175 N N   . PHE B 221 ? 0.1775 0.1798 0.1582 -0.0251 -0.0043 0.0042  233 PHE B N   
4176 C CA  . PHE B 221 ? 0.1822 0.1854 0.1617 -0.0268 -0.0029 0.0040  233 PHE B CA  
4177 C C   . PHE B 221 ? 0.1674 0.1661 0.1498 -0.0242 -0.0013 0.0031  233 PHE B C   
4178 O O   . PHE B 221 ? 0.2075 0.2029 0.1925 -0.0211 -0.0032 0.0046  233 PHE B O   
4179 C CB  . PHE B 221 ? 0.1701 0.1763 0.1490 -0.0277 -0.0056 0.0081  233 PHE B CB  
4180 C CG  . PHE B 221 ? 0.1969 0.2042 0.1750 -0.0295 -0.0038 0.0082  233 PHE B CG  
4181 C CD1 . PHE B 221 ? 0.2211 0.2316 0.1957 -0.0327 -0.0010 0.0058  233 PHE B CD1 
4182 C CD2 . PHE B 221 ? 0.1919 0.1971 0.1728 -0.0280 -0.0048 0.0105  233 PHE B CD2 
4183 C CE1 . PHE B 221 ? 0.2142 0.2260 0.1882 -0.0342 0.0010  0.0060  233 PHE B CE1 
4184 C CE2 . PHE B 221 ? 0.2118 0.2186 0.1926 -0.0298 -0.0029 0.0108  233 PHE B CE2 
4185 C CZ  . PHE B 221 ? 0.1936 0.2038 0.1709 -0.0327 0.0000  0.0086  233 PHE B CZ  
4186 N N   . GLY B 222 ? 0.1464 0.1453 0.1282 -0.0254 0.0021  0.0006  234 GLY B N   
4187 C CA  . GLY B 222 ? 0.1903 0.1865 0.1753 -0.0230 0.0033  0.0005  234 GLY B CA  
4188 C C   . GLY B 222 ? 0.1721 0.1637 0.1594 -0.0195 0.0039  -0.0009 234 GLY B C   
4189 O O   . GLY B 222 ? 0.1769 0.1668 0.1631 -0.0192 0.0049  -0.0027 234 GLY B O   
4190 N N   . GLY B 223 ? 0.1953 0.1850 0.1858 -0.0169 0.0034  -0.0001 235 GLY B N   
4191 C CA  . GLY B 223 ? 0.1945 0.1801 0.1870 -0.0132 0.0037  -0.0009 235 GLY B CA  
4192 C C   . GLY B 223 ? 0.2339 0.2189 0.2284 -0.0119 0.0071  -0.0026 235 GLY B C   
4193 O O   . GLY B 223 ? 0.2234 0.2110 0.2177 -0.0139 0.0096  -0.0035 235 GLY B O   
4194 N N   . ARG B 224 ? 0.1692 0.1507 0.1655 -0.0083 0.0071  -0.0028 236 ARG B N   
4195 C CA  . ARG B 224 ? 0.2138 0.1947 0.2128 -0.0060 0.0098  -0.0037 236 ARG B CA  
4196 C C   . ARG B 224 ? 0.2269 0.2043 0.2245 -0.0049 0.0137  -0.0061 236 ARG B C   
4197 O O   . ARG B 224 ? 0.2353 0.2095 0.2315 -0.0037 0.0131  -0.0063 236 ARG B O   
4198 C CB  . ARG B 224 ? 0.2070 0.1869 0.2089 -0.0026 0.0070  -0.0020 236 ARG B CB  
4199 C CG  . ARG B 224 ? 0.2409 0.2196 0.2454 0.0009  0.0095  -0.0026 236 ARG B CG  
4200 C CD  . ARG B 224 ? 0.2744 0.2575 0.2828 0.0007  0.0104  -0.0021 236 ARG B CD  
4201 N NE  . ARG B 224 ? 0.2405 0.2230 0.2515 0.0040  0.0136  -0.0028 236 ARG B NE  
4202 C CZ  . ARG B 224 ? 0.2668 0.2487 0.2803 0.0079  0.0121  -0.0016 236 ARG B CZ  
4203 N NH1 . ARG B 224 ? 0.2806 0.2627 0.2945 0.0086  0.0074  0.0000  236 ARG B NH1 
4204 N NH2 . ARG B 224 ? 0.2696 0.2508 0.2852 0.0111  0.0155  -0.0019 236 ARG B NH2 
4205 N N   . TYR B 225 ? 0.2383 0.2160 0.2364 -0.0052 0.0179  -0.0079 237 TYR B N   
4206 C CA  . TYR B 225 ? 0.2384 0.2118 0.2354 -0.0040 0.0222  -0.0103 237 TYR B CA  
4207 C C   . TYR B 225 ? 0.2620 0.2357 0.2618 -0.0020 0.0259  -0.0110 237 TYR B C   
4208 O O   . TYR B 225 ? 0.2842 0.2610 0.2840 -0.0042 0.0277  -0.0118 237 TYR B O   
4209 C CB  . TYR B 225 ? 0.3048 0.2776 0.2977 -0.0080 0.0243  -0.0129 237 TYR B CB  
4210 C CG  . TYR B 225 ? 0.2956 0.2635 0.2874 -0.0074 0.0291  -0.0157 237 TYR B CG  
4211 C CD1 . TYR B 225 ? 0.2925 0.2555 0.2852 -0.0039 0.0297  -0.0151 237 TYR B CD1 
4212 C CD2 . TYR B 225 ? 0.2859 0.2533 0.2753 -0.0103 0.0333  -0.0188 237 TYR B CD2 
4213 C CE1 . TYR B 225 ? 0.3217 0.2794 0.3135 -0.0033 0.0344  -0.0174 237 TYR B CE1 
4214 C CE2 . TYR B 225 ? 0.3157 0.2775 0.3039 -0.0099 0.0380  -0.0216 237 TYR B CE2 
4215 C CZ  . TYR B 225 ? 0.3417 0.2986 0.3314 -0.0064 0.0386  -0.0207 237 TYR B CZ  
4216 O OH  . TYR B 225 ? 0.3908 0.3415 0.3794 -0.0060 0.0436  -0.0232 237 TYR B OH  
4217 N N   . ARG B 226 ? 0.2986 0.2691 0.3007 0.0024  0.0270  -0.0104 238 ARG B N   
4218 C CA  . ARG B 226 ? 0.3202 0.2910 0.3257 0.0053  0.0306  -0.0105 238 ARG B CA  
4219 C C   . ARG B 226 ? 0.2630 0.2401 0.2722 0.0050  0.0284  -0.0087 238 ARG B C   
4220 O O   . ARG B 226 ? 0.2826 0.2621 0.2935 0.0056  0.0237  -0.0064 238 ARG B O   
4221 C CB  . ARG B 226 ? 0.3075 0.2752 0.3107 0.0036  0.0365  -0.0138 238 ARG B CB  
4222 C CG  . ARG B 226 ? 0.3703 0.3311 0.3706 0.0042  0.0390  -0.0155 238 ARG B CG  
4223 C CD  . ARG B 226 ? 0.3987 0.3565 0.3964 0.0018  0.0447  -0.0192 238 ARG B CD  
4224 N NE  . ARG B 226 ? 0.4803 0.4307 0.4764 0.0030  0.0484  -0.0208 238 ARG B NE  
4225 C CZ  . ARG B 226 ? 0.4992 0.4450 0.4972 0.0070  0.0528  -0.0209 238 ARG B CZ  
4226 N NH1 . ARG B 226 ? 0.5441 0.4925 0.5462 0.0105  0.0538  -0.0194 238 ARG B NH1 
4227 N NH2 . ARG B 226 ? 0.5216 0.4601 0.5178 0.0075  0.0564  -0.0225 238 ARG B NH2 
4228 N N   . ASP B 227 ? 0.3520 0.3320 0.3625 0.0037  0.0318  -0.0098 239 ASP B N   
4229 C CA  . ASP B 227 ? 0.3297 0.3162 0.3443 0.0032  0.0303  -0.0080 239 ASP B CA  
4230 C C   . ASP B 227 ? 0.3307 0.3207 0.3428 -0.0018 0.0285  -0.0079 239 ASP B C   
4231 O O   . ASP B 227 ? 0.3129 0.3080 0.3276 -0.0031 0.0290  -0.0071 239 ASP B O   
4232 C CB  . ASP B 227 ? 0.3880 0.3763 0.4061 0.0051  0.0353  -0.0087 239 ASP B CB  
4233 C CG  . ASP B 227 ? 0.4178 0.4037 0.4394 0.0106  0.0370  -0.0080 239 ASP B CG  
4234 O OD1 . ASP B 227 ? 0.4452 0.4284 0.4670 0.0124  0.0425  -0.0097 239 ASP B OD1 
4235 O OD2 . ASP B 227 ? 0.4549 0.4412 0.4785 0.0132  0.0329  -0.0057 239 ASP B OD2 
4236 N N   . ALA B 228 ? 0.2743 0.2621 0.2817 -0.0044 0.0266  -0.0085 240 ALA B N   
4237 C CA  . ALA B 228 ? 0.2832 0.2743 0.2878 -0.0089 0.0251  -0.0082 240 ALA B CA  
4238 C C   . ALA B 228 ? 0.2846 0.2753 0.2877 -0.0099 0.0198  -0.0062 240 ALA B C   
4239 O O   . ALA B 228 ? 0.2471 0.2341 0.2492 -0.0082 0.0183  -0.0063 240 ALA B O   
4240 C CB  . ALA B 228 ? 0.2911 0.2809 0.2904 -0.0121 0.0289  -0.0113 240 ALA B CB  
4241 N N   . ARG B 229 ? 0.2189 0.2134 0.2222 -0.0125 0.0173  -0.0043 241 ARG B N   
4242 C CA  . ARG B 229 ? 0.2227 0.2170 0.2234 -0.0144 0.0131  -0.0026 241 ARG B CA  
4243 C C   . ARG B 229 ? 0.2220 0.2187 0.2183 -0.0185 0.0145  -0.0033 241 ARG B C   
4244 O O   . ARG B 229 ? 0.2059 0.2062 0.2023 -0.0205 0.0160  -0.0029 241 ARG B O   
4245 C CB  . ARG B 229 ? 0.1955 0.1917 0.1996 -0.0142 0.0092  0.0004  241 ARG B CB  
4246 C CG  . ARG B 229 ? 0.1897 0.1835 0.1973 -0.0102 0.0075  0.0007  241 ARG B CG  
4247 C CD  . ARG B 229 ? 0.1786 0.1737 0.1897 -0.0099 0.0037  0.0031  241 ARG B CD  
4248 N NE  . ARG B 229 ? 0.2236 0.2167 0.2371 -0.0061 0.0024  0.0029  241 ARG B NE  
4249 C CZ  . ARG B 229 ? 0.2564 0.2520 0.2744 -0.0041 0.0030  0.0030  241 ARG B CZ  
4250 N NH1 . ARG B 229 ? 0.1943 0.1948 0.2158 -0.0057 0.0046  0.0036  241 ARG B NH1 
4251 N NH2 . ARG B 229 ? 0.2371 0.2307 0.2562 -0.0004 0.0021  0.0028  241 ARG B NH2 
4252 N N   . MET B 230 ? 0.2120 0.2070 0.2044 -0.0197 0.0140  -0.0044 242 MET B N   
4253 C CA  . MET B 230 ? 0.2487 0.2456 0.2364 -0.0233 0.0162  -0.0063 242 MET B CA  
4254 C C   . MET B 230 ? 0.1986 0.1990 0.1835 -0.0262 0.0130  -0.0038 242 MET B C   
4255 O O   . MET B 230 ? 0.1969 0.1971 0.1833 -0.0253 0.0090  -0.0009 242 MET B O   
4256 C CB  . MET B 230 ? 0.2836 0.2770 0.2689 -0.0231 0.0180  -0.0093 242 MET B CB  
4257 C CG  . MET B 230 ? 0.3084 0.2980 0.2960 -0.0202 0.0219  -0.0116 242 MET B CG  
4258 S SD  . MET B 230 ? 0.3416 0.3259 0.3274 -0.0194 0.0232  -0.0141 242 MET B SD  
4259 C CE  . MET B 230 ? 0.3419 0.3290 0.3221 -0.0248 0.0234  -0.0162 242 MET B CE  
4260 N N   . ASN B 231 ? 0.2458 0.2492 0.2263 -0.0298 0.0149  -0.0051 243 ASN B N   
4261 C CA  . ASN B 231 ? 0.2340 0.2414 0.2114 -0.0328 0.0123  -0.0026 243 ASN B CA  
4262 C C   . ASN B 231 ? 0.2497 0.2585 0.2224 -0.0352 0.0116  -0.0040 243 ASN B C   
4263 O O   . ASN B 231 ? 0.2603 0.2733 0.2293 -0.0381 0.0101  -0.0023 243 ASN B O   
4264 C CB  . ASN B 231 ? 0.2436 0.2548 0.2192 -0.0352 0.0148  -0.0022 243 ASN B CB  
4265 C CG  . ASN B 231 ? 0.2316 0.2434 0.2031 -0.0374 0.0194  -0.0064 243 ASN B CG  
4266 O OD1 . ASN B 231 ? 0.3550 0.3634 0.3263 -0.0365 0.0215  -0.0099 243 ASN B OD1 
4267 N ND2 . ASN B 231 ? 0.3228 0.3385 0.2904 -0.0405 0.0211  -0.0062 243 ASN B ND2 
4268 N N   . ASP B 232 ? 0.2151 0.2209 0.1877 -0.0344 0.0127  -0.0069 244 ASP B N   
4269 C CA  . ASP B 232 ? 0.1984 0.2060 0.1667 -0.0374 0.0127  -0.0090 244 ASP B CA  
4270 C C   . ASP B 232 ? 0.2354 0.2444 0.2045 -0.0368 0.0082  -0.0062 244 ASP B C   
4271 O O   . ASP B 232 ? 0.2398 0.2464 0.2128 -0.0335 0.0058  -0.0038 244 ASP B O   
4272 C CB  . ASP B 232 ? 0.2135 0.2173 0.1812 -0.0376 0.0167  -0.0137 244 ASP B CB  
4273 C CG  . ASP B 232 ? 0.2723 0.2706 0.2446 -0.0334 0.0169  -0.0138 244 ASP B CG  
4274 O OD1 . ASP B 232 ? 0.2465 0.2437 0.2226 -0.0301 0.0146  -0.0108 244 ASP B OD1 
4275 O OD2 . ASP B 232 ? 0.2731 0.2680 0.2448 -0.0335 0.0195  -0.0171 244 ASP B OD2 
4276 N N   . LEU B 233 ? 0.2491 0.2624 0.2145 -0.0401 0.0069  -0.0066 245 LEU B N   
4277 C CA  . LEU B 233 ? 0.2277 0.2439 0.1936 -0.0399 0.0027  -0.0037 245 LEU B CA  
4278 C C   . LEU B 233 ? 0.2332 0.2509 0.1974 -0.0422 0.0032  -0.0068 245 LEU B C   
4279 O O   . LEU B 233 ? 0.2466 0.2669 0.2066 -0.0461 0.0050  -0.0099 245 LEU B O   
4280 C CB  . LEU B 233 ? 0.2145 0.2364 0.1777 -0.0418 -0.0001 0.0001  245 LEU B CB  
4281 C CG  . LEU B 233 ? 0.1945 0.2202 0.1584 -0.0413 -0.0046 0.0041  245 LEU B CG  
4282 C CD1 . LEU B 233 ? 0.2027 0.2241 0.1717 -0.0367 -0.0067 0.0070  245 LEU B CD1 
4283 C CD2 . LEU B 233 ? 0.1591 0.1899 0.1196 -0.0432 -0.0065 0.0078  245 LEU B CD2 
4284 N N   . HIS B 234 ? 0.1927 0.2089 0.1603 -0.0399 0.0014  -0.0059 246 HIS B N   
4285 C CA  . HIS B 234 ? 0.2225 0.2405 0.1896 -0.0421 0.0017  -0.0084 246 HIS B CA  
4286 C C   . HIS B 234 ? 0.2263 0.2478 0.1961 -0.0405 -0.0024 -0.0048 246 HIS B C   
4287 O O   . HIS B 234 ? 0.1875 0.2077 0.1599 -0.0370 -0.0047 -0.0009 246 HIS B O   
4288 C CB  . HIS B 234 ? 0.2304 0.2421 0.1994 -0.0408 0.0053  -0.0121 246 HIS B CB  
4289 C CG  . HIS B 234 ? 0.2621 0.2694 0.2295 -0.0412 0.0097  -0.0154 246 HIS B CG  
4290 N ND1 . HIS B 234 ? 0.2812 0.2870 0.2457 -0.0445 0.0134  -0.0202 246 HIS B ND1 
4291 C CD2 . HIS B 234 ? 0.2631 0.2671 0.2317 -0.0386 0.0111  -0.0146 246 HIS B CD2 
4292 C CE1 . HIS B 234 ? 0.2702 0.2718 0.2342 -0.0435 0.0172  -0.0222 246 HIS B CE1 
4293 N NE2 . HIS B 234 ? 0.2825 0.2834 0.2491 -0.0400 0.0158  -0.0187 246 HIS B NE2 
4294 N N   . TYR B 235 ? 0.2271 0.2530 0.1964 -0.0432 -0.0032 -0.0061 247 TYR B N   
4295 C CA  . TYR B 235 ? 0.2246 0.2530 0.1977 -0.0412 -0.0061 -0.0033 247 TYR B CA  
4296 C C   . TYR B 235 ? 0.2448 0.2738 0.2191 -0.0433 -0.0045 -0.0067 247 TYR B C   
4297 O O   . TYR B 235 ? 0.2255 0.2560 0.1966 -0.0478 -0.0025 -0.0108 247 TYR B O   
4298 C CB  . TYR B 235 ? 0.2425 0.2788 0.2148 -0.0419 -0.0104 0.0009  247 TYR B CB  
4299 C CG  . TYR B 235 ? 0.2535 0.2979 0.2230 -0.0470 -0.0115 -0.0006 247 TYR B CG  
4300 C CD1 . TYR B 235 ? 0.2312 0.2786 0.1951 -0.0511 -0.0108 -0.0025 247 TYR B CD1 
4301 C CD2 . TYR B 235 ? 0.2442 0.2938 0.2166 -0.0476 -0.0134 -0.0001 247 TYR B CD2 
4302 C CE1 . TYR B 235 ? 0.2797 0.3350 0.2405 -0.0560 -0.0121 -0.0041 247 TYR B CE1 
4303 C CE2 . TYR B 235 ? 0.2442 0.3022 0.2144 -0.0525 -0.0148 -0.0016 247 TYR B CE2 
4304 C CZ  . TYR B 235 ? 0.2833 0.3440 0.2474 -0.0567 -0.0143 -0.0036 247 TYR B CZ  
4305 O OH  . TYR B 235 ? 0.3559 0.4252 0.3173 -0.0618 -0.0161 -0.0052 247 TYR B OH  
4306 N N   . LEU B 236 ? 0.2218 0.2492 0.2005 -0.0401 -0.0051 -0.0053 248 LEU B N   
4307 C CA  . LEU B 236 ? 0.1816 0.2103 0.1625 -0.0417 -0.0040 -0.0075 248 LEU B CA  
4308 C C   . LEU B 236 ? 0.1769 0.2146 0.1600 -0.0423 -0.0079 -0.0043 248 LEU B C   
4309 O O   . LEU B 236 ? 0.1887 0.2277 0.1740 -0.0386 -0.0107 0.0002  248 LEU B O   
4310 C CB  . LEU B 236 ? 0.1683 0.1895 0.1525 -0.0374 -0.0018 -0.0075 248 LEU B CB  
4311 C CG  . LEU B 236 ? 0.2230 0.2440 0.2100 -0.0384 0.0001  -0.0095 248 LEU B CG  
4312 C CD1 . LEU B 236 ? 0.2080 0.2269 0.1923 -0.0432 0.0037  -0.0147 248 LEU B CD1 
4313 C CD2 . LEU B 236 ? 0.2122 0.2258 0.2019 -0.0331 0.0018  -0.0084 248 LEU B CD2 
4314 N N   . ASN B 237 ? 0.1922 0.2361 0.1748 -0.0471 -0.0081 -0.0067 249 ASN B N   
4315 C CA  . ASN B 237 ? 0.2139 0.2673 0.1996 -0.0478 -0.0118 -0.0038 249 ASN B CA  
4316 C C   . ASN B 237 ? 0.2118 0.2634 0.2033 -0.0446 -0.0109 -0.0029 249 ASN B C   
4317 O O   . ASN B 237 ? 0.2401 0.2880 0.2325 -0.0462 -0.0076 -0.0064 249 ASN B O   
4318 C CB  . ASN B 237 ? 0.1665 0.2280 0.1498 -0.0544 -0.0125 -0.0068 249 ASN B CB  
4319 C CG  . ASN B 237 ? 0.2155 0.2884 0.2023 -0.0553 -0.0167 -0.0036 249 ASN B CG  
4320 O OD1 . ASN B 237 ? 0.2848 0.3590 0.2773 -0.0520 -0.0174 -0.0010 249 ASN B OD1 
4321 N ND2 . ASN B 237 ? 0.2340 0.3158 0.2173 -0.0597 -0.0195 -0.0037 249 ASN B ND2 
4322 N N   . LEU B 238 ? 0.1676 0.2212 0.1626 -0.0400 -0.0135 0.0020  250 LEU B N   
4323 C CA  . LEU B 238 ? 0.2329 0.2834 0.2327 -0.0361 -0.0122 0.0030  250 LEU B CA  
4324 C C   . LEU B 238 ? 0.2145 0.2737 0.2189 -0.0382 -0.0131 0.0032  250 LEU B C   
4325 O O   . LEU B 238 ? 0.2840 0.3416 0.2926 -0.0351 -0.0119 0.0043  250 LEU B O   
4326 C CB  . LEU B 238 ? 0.2151 0.2624 0.2163 -0.0299 -0.0140 0.0076  250 LEU B CB  
4327 C CG  . LEU B 238 ? 0.2218 0.2615 0.2191 -0.0282 -0.0134 0.0075  250 LEU B CG  
4328 C CD1 . LEU B 238 ? 0.1990 0.2363 0.1973 -0.0231 -0.0157 0.0120  250 LEU B CD1 
4329 C CD2 . LEU B 238 ? 0.2345 0.2650 0.2306 -0.0276 -0.0094 0.0038  250 LEU B CD2 
4330 N N   . ASP B 239 ? 0.2736 0.3422 0.2771 -0.0434 -0.0152 0.0024  251 ASP B N   
4331 C CA  . ASP B 239 ? 0.2599 0.3374 0.2672 -0.0473 -0.0158 0.0013  251 ASP B CA  
4332 C C   . ASP B 239 ? 0.2867 0.3611 0.2919 -0.0530 -0.0122 -0.0048 251 ASP B C   
4333 O O   . ASP B 239 ? 0.2782 0.3519 0.2873 -0.0540 -0.0098 -0.0065 251 ASP B O   
4334 C CB  . ASP B 239 ? 0.2637 0.3538 0.2707 -0.0503 -0.0205 0.0036  251 ASP B CB  
4335 C CG  . ASP B 239 ? 0.2884 0.3839 0.2994 -0.0449 -0.0240 0.0100  251 ASP B CG  
4336 O OD1 . ASP B 239 ? 0.3286 0.4213 0.3444 -0.0401 -0.0229 0.0122  251 ASP B OD1 
4337 O OD2 . ASP B 239 ? 0.3237 0.4261 0.3327 -0.0456 -0.0277 0.0129  251 ASP B OD2 
4338 N N   . THR B 240 ? 0.2897 0.3622 0.2889 -0.0570 -0.0116 -0.0081 252 THR B N   
4339 C CA  . THR B 240 ? 0.2888 0.3589 0.2852 -0.0630 -0.0084 -0.0142 252 THR B CA  
4340 C C   . THR B 240 ? 0.2618 0.3186 0.2562 -0.0613 -0.0033 -0.0172 252 THR B C   
4341 O O   . THR B 240 ? 0.3178 0.3709 0.3112 -0.0654 0.0002  -0.0220 252 THR B O   
4342 C CB  . THR B 240 ? 0.2624 0.3371 0.2526 -0.0683 -0.0101 -0.0165 252 THR B CB  
4343 O OG1 . THR B 240 ? 0.2956 0.3621 0.2808 -0.0660 -0.0085 -0.0169 252 THR B OG1 
4344 C CG2 . THR B 240 ? 0.3087 0.3959 0.2999 -0.0685 -0.0157 -0.0121 252 THR B CG2 
4345 N N   . TRP B 241 ? 0.2564 0.3061 0.2503 -0.0553 -0.0029 -0.0146 253 TRP B N   
4346 C CA  . TRP B 241 ? 0.2532 0.2910 0.2453 -0.0530 0.0015  -0.0168 253 TRP B CA  
4347 C C   . TRP B 241 ? 0.2754 0.3094 0.2617 -0.0570 0.0040  -0.0214 253 TRP B C   
4348 O O   . TRP B 241 ? 0.3249 0.3506 0.3100 -0.0576 0.0085  -0.0249 253 TRP B O   
4349 C CB  . TRP B 241 ? 0.2762 0.3093 0.2720 -0.0522 0.0050  -0.0181 253 TRP B CB  
4350 C CG  . TRP B 241 ? 0.2957 0.3324 0.2967 -0.0480 0.0029  -0.0137 253 TRP B CG  
4351 C CD1 . TRP B 241 ? 0.2719 0.3160 0.2777 -0.0498 0.0020  -0.0129 253 TRP B CD1 
4352 C CD2 . TRP B 241 ? 0.2221 0.2559 0.2243 -0.0414 0.0015  -0.0095 253 TRP B CD2 
4353 N NE1 . TRP B 241 ? 0.2555 0.3010 0.2653 -0.0442 0.0004  -0.0084 253 TRP B NE1 
4354 C CE2 . TRP B 241 ? 0.2577 0.2966 0.2651 -0.0391 0.0000  -0.0064 253 TRP B CE2 
4355 C CE3 . TRP B 241 ? 0.2696 0.2967 0.2689 -0.0373 0.0013  -0.0082 253 TRP B CE3 
4356 C CZ2 . TRP B 241 ? 0.2940 0.3308 0.3032 -0.0329 -0.0013 -0.0024 253 TRP B CZ2 
4357 C CZ3 . TRP B 241 ? 0.2559 0.2813 0.2572 -0.0315 -0.0003 -0.0043 253 TRP B CZ3 
4358 C CH2 . TRP B 241 ? 0.2925 0.3223 0.2984 -0.0293 -0.0015 -0.0015 253 TRP B CH2 
4359 N N   . GLU B 242 ? 0.3036 0.3433 0.2862 -0.0594 0.0013  -0.0210 254 GLU B N   
4360 C CA  . GLU B 242 ? 0.2895 0.3263 0.2661 -0.0630 0.0035  -0.0251 254 GLU B CA  
4361 C C   . GLU B 242 ? 0.2433 0.2763 0.2176 -0.0590 0.0031  -0.0227 254 GLU B C   
4362 O O   . GLU B 242 ? 0.2278 0.2657 0.2028 -0.0566 -0.0007 -0.0182 254 GLU B O   
4363 C CB  . GLU B 242 ? 0.3168 0.3634 0.2902 -0.0692 0.0008  -0.0267 254 GLU B CB  
4364 C CG  . GLU B 242 ? 0.3479 0.3920 0.3145 -0.0733 0.0032  -0.0312 254 GLU B CG  
4365 C CD  . GLU B 242 ? 0.3717 0.4262 0.3343 -0.0792 -0.0001 -0.0324 254 GLU B CD  
4366 O OE1 . GLU B 242 ? 0.3349 0.3961 0.2961 -0.0780 -0.0041 -0.0282 254 GLU B OE1 
4367 O OE2 . GLU B 242 ? 0.4523 0.5086 0.4133 -0.0851 0.0013  -0.0373 254 GLU B OE2 
4368 N N   . TRP B 243 ? 0.2747 0.2993 0.2466 -0.0583 0.0073  -0.0256 255 TRP B N   
4369 C CA  . TRP B 243 ? 0.2685 0.2896 0.2383 -0.0552 0.0075  -0.0239 255 TRP B CA  
4370 C C   . TRP B 243 ? 0.2848 0.3101 0.2489 -0.0593 0.0071  -0.0256 255 TRP B C   
4371 O O   . TRP B 243 ? 0.3196 0.3449 0.2801 -0.0642 0.0095  -0.0304 255 TRP B O   
4372 C CB  . TRP B 243 ? 0.2807 0.2915 0.2508 -0.0525 0.0123  -0.0262 255 TRP B CB  
4373 C CG  . TRP B 243 ? 0.2636 0.2692 0.2382 -0.0466 0.0124  -0.0233 255 TRP B CG  
4374 C CD1 . TRP B 243 ? 0.2697 0.2697 0.2468 -0.0451 0.0152  -0.0245 255 TRP B CD1 
4375 C CD2 . TRP B 243 ? 0.2002 0.2054 0.1767 -0.0417 0.0098  -0.0188 255 TRP B CD2 
4376 N NE1 . TRP B 243 ? 0.2509 0.2475 0.2311 -0.0394 0.0143  -0.0210 255 TRP B NE1 
4377 C CE2 . TRP B 243 ? 0.2482 0.2477 0.2280 -0.0374 0.0109  -0.0178 255 TRP B CE2 
4378 C CE3 . TRP B 243 ? 0.2135 0.2223 0.1890 -0.0407 0.0067  -0.0157 255 TRP B CE3 
4379 C CZ2 . TRP B 243 ? 0.2205 0.2180 0.2025 -0.0323 0.0089  -0.0141 255 TRP B CZ2 
4380 C CZ3 . TRP B 243 ? 0.2225 0.2290 0.2006 -0.0358 0.0048  -0.0120 255 TRP B CZ3 
4381 C CH2 . TRP B 243 ? 0.2064 0.2072 0.1875 -0.0317 0.0059  -0.0114 255 TRP B CH2 
4382 N N   . ASN B 244 ? 0.2709 0.2990 0.2339 -0.0573 0.0045  -0.0218 256 ASN B N   
4383 C CA  . ASN B 244 ? 0.2950 0.3270 0.2524 -0.0606 0.0042  -0.0226 256 ASN B CA  
4384 C C   . ASN B 244 ? 0.2435 0.2711 0.2005 -0.0571 0.0054  -0.0207 256 ASN B C   
4385 O O   . ASN B 244 ? 0.2497 0.2759 0.2104 -0.0525 0.0034  -0.0164 256 ASN B O   
4386 C CB  . ASN B 244 ? 0.3019 0.3442 0.2581 -0.0626 -0.0009 -0.0192 256 ASN B CB  
4387 C CG  . ASN B 244 ? 0.3471 0.3952 0.3046 -0.0661 -0.0026 -0.0207 256 ASN B CG  
4388 O OD1 . ASN B 244 ? 0.3620 0.4134 0.3154 -0.0717 -0.0018 -0.0249 256 ASN B OD1 
4389 N ND2 . ASN B 244 ? 0.3198 0.3696 0.2831 -0.0630 -0.0050 -0.0173 256 ASN B ND2 
4390 N N   . GLU B 245 ? 0.2972 0.3228 0.2497 -0.0593 0.0087  -0.0239 257 GLU B N   
4391 C CA  . GLU B 245 ? 0.2938 0.3172 0.2457 -0.0568 0.0096  -0.0219 257 GLU B CA  
4392 C C   . GLU B 245 ? 0.3172 0.3479 0.2648 -0.0591 0.0068  -0.0192 257 GLU B C   
4393 O O   . GLU B 245 ? 0.3432 0.3787 0.2856 -0.0639 0.0067  -0.0217 257 GLU B O   
4394 C CB  . GLU B 245 ? 0.3253 0.3425 0.2753 -0.0571 0.0152  -0.0263 257 GLU B CB  
4395 C CG  . GLU B 245 ? 0.3447 0.3599 0.2960 -0.0537 0.0161  -0.0237 257 GLU B CG  
4396 C CD  . GLU B 245 ? 0.4163 0.4263 0.3662 -0.0536 0.0217  -0.0276 257 GLU B CD  
4397 O OE1 . GLU B 245 ? 0.5197 0.5284 0.4654 -0.0571 0.0251  -0.0325 257 GLU B OE1 
4398 O OE2 . GLU B 245 ? 0.4116 0.4188 0.3646 -0.0499 0.0228  -0.0257 257 GLU B OE2 
4399 N N   . LEU B 246 ? 0.2695 0.3008 0.2192 -0.0559 0.0046  -0.0142 258 LEU B N   
4400 C CA  . LEU B 246 ? 0.2660 0.3034 0.2120 -0.0575 0.0021  -0.0108 258 LEU B CA  
4401 C C   . LEU B 246 ? 0.3305 0.3654 0.2740 -0.0576 0.0056  -0.0117 258 LEU B C   
4402 O O   . LEU B 246 ? 0.3028 0.3323 0.2503 -0.0541 0.0074  -0.0111 258 LEU B O   
4403 C CB  . LEU B 246 ? 0.3105 0.3499 0.2604 -0.0541 -0.0024 -0.0045 258 LEU B CB  
4404 C CG  . LEU B 246 ? 0.2743 0.3176 0.2267 -0.0539 -0.0059 -0.0031 258 LEU B CG  
4405 C CD1 . LEU B 246 ? 0.3007 0.3435 0.2577 -0.0494 -0.0093 0.0026  258 LEU B CD1 
4406 C CD2 . LEU B 246 ? 0.2974 0.3493 0.2448 -0.0584 -0.0082 -0.0031 258 LEU B CD2 
4407 N N   . ILE B 247 ? 0.3510 0.3904 0.2881 -0.0616 0.0064  -0.0129 259 ILE B N   
4408 C CA  . ILE B 247 ? 0.3484 0.3866 0.2824 -0.0622 0.0100  -0.0138 259 ILE B CA  
4409 C C   . ILE B 247 ? 0.3475 0.3920 0.2780 -0.0634 0.0071  -0.0089 259 ILE B C   
4410 O O   . ILE B 247 ? 0.3612 0.4112 0.2849 -0.0675 0.0067  -0.0099 259 ILE B O   
4411 C CB  . ILE B 247 ? 0.3802 0.4171 0.3089 -0.0659 0.0146  -0.0204 259 ILE B CB  
4412 C CG1 . ILE B 247 ? 0.3986 0.4280 0.3312 -0.0641 0.0180  -0.0247 259 ILE B CG1 
4413 C CG2 . ILE B 247 ? 0.4450 0.4820 0.3696 -0.0670 0.0184  -0.0212 259 ILE B CG2 
4414 C CD1 . ILE B 247 ? 0.4003 0.4239 0.3376 -0.0599 0.0212  -0.0241 259 ILE B CD1 
4415 N N   . PRO B 248 ? 0.3590 0.4028 0.2937 -0.0601 0.0049  -0.0035 260 PRO B N   
4416 C CA  . PRO B 248 ? 0.3472 0.3963 0.2788 -0.0611 0.0024  0.0017  260 PRO B CA  
4417 C C   . PRO B 248 ? 0.3607 0.4111 0.2869 -0.0636 0.0060  0.0006  260 PRO B C   
4418 O O   . PRO B 248 ? 0.4116 0.4578 0.3393 -0.0628 0.0104  -0.0023 260 PRO B O   
4419 C CB  . PRO B 248 ? 0.3488 0.3946 0.2869 -0.0568 0.0001  0.0069  260 PRO B CB  
4420 C CG  . PRO B 248 ? 0.2683 0.3086 0.2124 -0.0538 0.0005  0.0045  260 PRO B CG  
4421 C CD  . PRO B 248 ? 0.3295 0.3675 0.2717 -0.0555 0.0048  -0.0019 260 PRO B CD  
4422 N N   . GLN B 249 ? 0.3890 0.4458 0.3090 -0.0664 0.0044  0.0031  261 GLN B N   
4423 C CA  . GLN B 249 ? 0.4084 0.4669 0.3228 -0.0687 0.0077  0.0029  261 GLN B CA  
4424 C C   . GLN B 249 ? 0.3471 0.4041 0.2654 -0.0662 0.0076  0.0085  261 GLN B C   
4425 O O   . GLN B 249 ? 0.3345 0.3916 0.2565 -0.0640 0.0037  0.0138  261 GLN B O   
4426 C CB  . GLN B 249 ? 0.4217 0.4878 0.3271 -0.0729 0.0060  0.0035  261 GLN B CB  
4427 C CG  . GLN B 249 ? 0.5311 0.5994 0.4319 -0.0763 0.0060  -0.0024 261 GLN B CG  
4428 C CD  . GLN B 249 ? 0.4927 0.5575 0.3898 -0.0786 0.0119  -0.0097 261 GLN B CD  
4429 O OE1 . GLN B 249 ? 0.4931 0.5517 0.3947 -0.0761 0.0159  -0.0115 261 GLN B OE1 
4430 N NE2 . GLN B 249 ? 0.5249 0.5936 0.4137 -0.0833 0.0125  -0.0139 261 GLN B NE2 
4431 N N   . GLY B 250 ? 0.3177 0.3733 0.2352 -0.0667 0.0122  0.0071  262 GLY B N   
4432 C CA  . GLY B 250 ? 0.2758 0.3307 0.1966 -0.0652 0.0127  0.0121  262 GLY B CA  
4433 C C   . GLY B 250 ? 0.2804 0.3294 0.2104 -0.0615 0.0135  0.0119  262 GLY B C   
4434 O O   . GLY B 250 ? 0.3430 0.3883 0.2762 -0.0600 0.0150  0.0074  262 GLY B O   
4435 N N   . ILE B 251 ? 0.2596 0.3077 0.1937 -0.0600 0.0123  0.0170  263 ILE B N   
4436 C CA  . ILE B 251 ? 0.2209 0.2642 0.1634 -0.0569 0.0130  0.0170  263 ILE B CA  
4437 C C   . ILE B 251 ? 0.2368 0.2764 0.1840 -0.0540 0.0092  0.0168  263 ILE B C   
4438 O O   . ILE B 251 ? 0.2165 0.2573 0.1622 -0.0538 0.0052  0.0195  263 ILE B O   
4439 C CB  . ILE B 251 ? 0.2425 0.2860 0.1882 -0.0567 0.0127  0.0224  263 ILE B CB  
4440 C CG1 . ILE B 251 ? 0.3081 0.3562 0.2478 -0.0600 0.0159  0.0236  263 ILE B CG1 
4441 C CG2 . ILE B 251 ? 0.2995 0.3390 0.2535 -0.0542 0.0140  0.0215  263 ILE B CG2 
4442 C CD1 . ILE B 251 ? 0.2771 0.3252 0.2188 -0.0603 0.0214  0.0203  263 ILE B CD1 
4443 N N   . CYS B 252 ? 0.2256 0.2609 0.1784 -0.0514 0.0107  0.0139  264 CYS B N   
4444 C CA  . CYS B 252 ? 0.2626 0.2939 0.2199 -0.0484 0.0079  0.0132  264 CYS B CA  
4445 C C   . CYS B 252 ? 0.2325 0.2599 0.1971 -0.0456 0.0075  0.0147  264 CYS B C   
4446 O O   . CYS B 252 ? 0.2242 0.2520 0.1912 -0.0457 0.0105  0.0142  264 CYS B O   
4447 C CB  . CYS B 252 ? 0.2660 0.2956 0.2224 -0.0481 0.0100  0.0076  264 CYS B CB  
4448 S SG  . CYS B 252 ? 0.3039 0.3379 0.2520 -0.0520 0.0099  0.0049  264 CYS B SG  
4449 N N   . PRO B 253 ? 0.2132 0.2372 0.1816 -0.0429 0.0040  0.0162  265 PRO B N   
4450 C CA  . PRO B 253 ? 0.2332 0.2534 0.2081 -0.0403 0.0034  0.0170  265 PRO B CA  
4451 C C   . PRO B 253 ? 0.2039 0.2226 0.1818 -0.0388 0.0067  0.0128  265 PRO B C   
4452 O O   . PRO B 253 ? 0.1875 0.2059 0.1632 -0.0388 0.0088  0.0089  265 PRO B O   
4453 C CB  . PRO B 253 ? 0.1991 0.2158 0.1758 -0.0378 -0.0007 0.0184  265 PRO B CB  
4454 C CG  . PRO B 253 ? 0.1906 0.2101 0.1624 -0.0393 -0.0027 0.0203  265 PRO B CG  
4455 C CD  . PRO B 253 ? 0.2483 0.2722 0.2150 -0.0423 0.0003  0.0176  265 PRO B CD  
4456 N N   . VAL B 254 ? 0.2030 0.2208 0.1861 -0.0377 0.0073  0.0136  266 VAL B N   
4457 C CA  . VAL B 254 ? 0.1994 0.2162 0.1862 -0.0357 0.0102  0.0103  266 VAL B CA  
4458 C C   . VAL B 254 ? 0.1572 0.1697 0.1455 -0.0326 0.0086  0.0084  266 VAL B C   
4459 O O   . VAL B 254 ? 0.1866 0.1967 0.1753 -0.0315 0.0048  0.0102  266 VAL B O   
4460 C CB  . VAL B 254 ? 0.1932 0.2111 0.1859 -0.0353 0.0106  0.0121  266 VAL B CB  
4461 C CG1 . VAL B 254 ? 0.1976 0.2124 0.1941 -0.0338 0.0060  0.0147  266 VAL B CG1 
4462 C CG2 . VAL B 254 ? 0.1954 0.2138 0.1917 -0.0334 0.0142  0.0090  266 VAL B CG2 
4463 N N   . GLY B 255 ? 0.1418 0.1531 0.1306 -0.0311 0.0117  0.0047  267 GLY B N   
4464 C CA  . GLY B 255 ? 0.1442 0.1514 0.1341 -0.0282 0.0107  0.0029  267 GLY B CA  
4465 C C   . GLY B 255 ? 0.1882 0.1929 0.1830 -0.0253 0.0076  0.0048  267 GLY B C   
4466 O O   . GLY B 255 ? 0.1706 0.1770 0.1693 -0.0253 0.0074  0.0063  267 GLY B O   
4467 N N   . ARG B 256 ? 0.1665 0.1676 0.1611 -0.0232 0.0051  0.0046  268 ARG B N   
4468 C CA  . ARG B 256 ? 0.1371 0.1357 0.1352 -0.0209 0.0017  0.0064  268 ARG B CA  
4469 C C   . ARG B 256 ? 0.1757 0.1702 0.1732 -0.0181 0.0003  0.0053  268 ARG B C   
4470 O O   . ARG B 256 ? 0.1497 0.1435 0.1440 -0.0185 0.0012  0.0040  268 ARG B O   
4471 C CB  . ARG B 256 ? 0.1309 0.1301 0.1286 -0.0227 -0.0016 0.0099  268 ARG B CB  
4472 C CG  . ARG B 256 ? 0.1564 0.1552 0.1500 -0.0236 -0.0032 0.0108  268 ARG B CG  
4473 C CD  . ARG B 256 ? 0.2063 0.2059 0.1991 -0.0253 -0.0057 0.0146  268 ARG B CD  
4474 N NE  . ARG B 256 ? 0.1377 0.1415 0.1292 -0.0286 -0.0038 0.0157  268 ARG B NE  
4475 C CZ  . ARG B 256 ? 0.1886 0.1932 0.1803 -0.0303 -0.0052 0.0192  268 ARG B CZ  
4476 N NH1 . ARG B 256 ? 0.1779 0.1790 0.1711 -0.0293 -0.0085 0.0218  268 ARG B NH1 
4477 N NH2 . ARG B 256 ? 0.2075 0.2162 0.1976 -0.0333 -0.0030 0.0202  268 ARG B NH2 
4478 N N   . SER B 257 ? 0.1611 0.1530 0.1616 -0.0153 -0.0017 0.0058  269 SER B N   
4479 C CA  . SER B 257 ? 0.1837 0.1714 0.1835 -0.0126 -0.0038 0.0057  269 SER B CA  
4480 C C   . SER B 257 ? 0.1763 0.1621 0.1772 -0.0122 -0.0078 0.0080  269 SER B C   
4481 O O   . SER B 257 ? 0.1662 0.1536 0.1689 -0.0139 -0.0089 0.0096  269 SER B O   
4482 C CB  . SER B 257 ? 0.1528 0.1383 0.1542 -0.0093 -0.0024 0.0038  269 SER B CB  
4483 O OG  . SER B 257 ? 0.2004 0.1868 0.2057 -0.0082 -0.0037 0.0046  269 SER B OG  
4484 N N   . TRP B 258 ? 0.1614 0.1434 0.1611 -0.0099 -0.0098 0.0081  270 TRP B N   
4485 C CA  . TRP B 258 ? 0.1501 0.1290 0.1504 -0.0089 -0.0133 0.0097  270 TRP B CA  
4486 C C   . TRP B 258 ? 0.1515 0.1310 0.1511 -0.0114 -0.0149 0.0123  270 TRP B C   
4487 O O   . TRP B 258 ? 0.1674 0.1444 0.1679 -0.0115 -0.0174 0.0138  270 TRP B O   
4488 C CB  . TRP B 258 ? 0.1814 0.1598 0.1848 -0.0079 -0.0144 0.0093  270 TRP B CB  
4489 C CG  . TRP B 258 ? 0.1800 0.1557 0.1831 -0.0043 -0.0145 0.0076  270 TRP B CG  
4490 C CD1 . TRP B 258 ? 0.1578 0.1297 0.1584 -0.0019 -0.0150 0.0072  270 TRP B CD1 
4491 C CD2 . TRP B 258 ? 0.1521 0.1290 0.1578 -0.0026 -0.0139 0.0065  270 TRP B CD2 
4492 N NE1 . TRP B 258 ? 0.1826 0.1529 0.1834 0.0011  -0.0147 0.0058  270 TRP B NE1 
4493 C CE2 . TRP B 258 ? 0.1901 0.1635 0.1940 0.0009  -0.0142 0.0055  270 TRP B CE2 
4494 C CE3 . TRP B 258 ? 0.2199 0.2008 0.2293 -0.0035 -0.0131 0.0065  270 TRP B CE3 
4495 C CZ2 . TRP B 258 ? 0.1869 0.1605 0.1923 0.0035  -0.0139 0.0047  270 TRP B CZ2 
4496 C CZ3 . TRP B 258 ? 0.1810 0.1627 0.1926 -0.0007 -0.0129 0.0057  270 TRP B CZ3 
4497 C CH2 . TRP B 258 ? 0.2029 0.1808 0.2122 0.0028  -0.0134 0.0049  270 TRP B CH2 
4498 N N   . HIS B 259 ? 0.1897 0.1723 0.1873 -0.0134 -0.0136 0.0130  271 HIS B N   
4499 C CA  . HIS B 259 ? 0.1763 0.1600 0.1724 -0.0155 -0.0149 0.0159  271 HIS B CA  
4500 C C   . HIS B 259 ? 0.1833 0.1649 0.1776 -0.0138 -0.0165 0.0169  271 HIS B C   
4501 O O   . HIS B 259 ? 0.1617 0.1417 0.1555 -0.0115 -0.0161 0.0151  271 HIS B O   
4502 C CB  . HIS B 259 ? 0.1486 0.1374 0.1430 -0.0185 -0.0125 0.0158  271 HIS B CB  
4503 C CG  . HIS B 259 ? 0.1822 0.1727 0.1747 -0.0183 -0.0103 0.0132  271 HIS B CG  
4504 N ND1 . HIS B 259 ? 0.1719 0.1612 0.1655 -0.0167 -0.0081 0.0102  271 HIS B ND1 
4505 C CD2 . HIS B 259 ? 0.1607 0.1536 0.1503 -0.0194 -0.0099 0.0131  271 HIS B CD2 
4506 C CE1 . HIS B 259 ? 0.1956 0.1860 0.1870 -0.0171 -0.0062 0.0082  271 HIS B CE1 
4507 N NE2 . HIS B 259 ? 0.1413 0.1342 0.1303 -0.0190 -0.0074 0.0098  271 HIS B NE2 
4508 N N   . SER B 260 ? 0.1821 0.1639 0.1755 -0.0147 -0.0181 0.0201  272 SER B N   
4509 C CA  . SER B 260 ? 0.2098 0.1907 0.2020 -0.0130 -0.0195 0.0215  272 SER B CA  
4510 C C   . SER B 260 ? 0.1937 0.1801 0.1837 -0.0152 -0.0191 0.0231  272 SER B C   
4511 O O   . SER B 260 ? 0.1874 0.1768 0.1766 -0.0181 -0.0185 0.0244  272 SER B O   
4512 C CB  . SER B 260 ? 0.2253 0.2011 0.2182 -0.0114 -0.0220 0.0241  272 SER B CB  
4513 O OG  . SER B 260 ? 0.1836 0.1601 0.1766 -0.0138 -0.0226 0.0271  272 SER B OG  
4514 N N   . LEU B 261 ? 0.1911 0.1793 0.1803 -0.0141 -0.0193 0.0230  273 LEU B N   
4515 C CA  . LEU B 261 ? 0.2162 0.2104 0.2032 -0.0163 -0.0194 0.0244  273 LEU B CA  
4516 C C   . LEU B 261 ? 0.2180 0.2125 0.2055 -0.0140 -0.0213 0.0268  273 LEU B C   
4517 O O   . LEU B 261 ? 0.2095 0.2026 0.1981 -0.0117 -0.0211 0.0251  273 LEU B O   
4518 C CB  . LEU B 261 ? 0.1758 0.1739 0.1614 -0.0183 -0.0170 0.0208  273 LEU B CB  
4519 C CG  . LEU B 261 ? 0.1526 0.1576 0.1355 -0.0212 -0.0172 0.0218  273 LEU B CG  
4520 C CD1 . LEU B 261 ? 0.2167 0.2240 0.1975 -0.0241 -0.0169 0.0236  273 LEU B CD1 
4521 C CD2 . LEU B 261 ? 0.1919 0.1998 0.1735 -0.0229 -0.0151 0.0179  273 LEU B CD2 
4522 N N   . THR B 262 ? 0.1975 0.1939 0.1843 -0.0144 -0.0231 0.0310  274 THR B N   
4523 C CA  . THR B 262 ? 0.2124 0.2079 0.2005 -0.0113 -0.0251 0.0341  274 THR B CA  
4524 C C   . THR B 262 ? 0.2162 0.2188 0.2029 -0.0127 -0.0264 0.0374  274 THR B C   
4525 O O   . THR B 262 ? 0.2065 0.2112 0.1914 -0.0149 -0.0268 0.0401  274 THR B O   
4526 C CB  . THR B 262 ? 0.2247 0.2132 0.2140 -0.0094 -0.0262 0.0365  274 THR B CB  
4527 O OG1 . THR B 262 ? 0.2565 0.2393 0.2468 -0.0086 -0.0253 0.0331  274 THR B OG1 
4528 C CG2 . THR B 262 ? 0.2804 0.2666 0.2710 -0.0056 -0.0277 0.0394  274 THR B CG2 
4529 N N   . PRO B 263 ? 0.2110 0.2181 0.1987 -0.0115 -0.0271 0.0378  275 PRO B N   
4530 C CA  . PRO B 263 ? 0.1900 0.2045 0.1767 -0.0125 -0.0289 0.0416  275 PRO B CA  
4531 C C   . PRO B 263 ? 0.2437 0.2553 0.2312 -0.0099 -0.0307 0.0470  275 PRO B C   
4532 O O   . PRO B 263 ? 0.2579 0.2631 0.2478 -0.0062 -0.0309 0.0478  275 PRO B O   
4533 C CB  . PRO B 263 ? 0.2100 0.2293 0.1986 -0.0114 -0.0292 0.0404  275 PRO B CB  
4534 C CG  . PRO B 263 ? 0.2142 0.2294 0.2036 -0.0113 -0.0269 0.0351  275 PRO B CG  
4535 C CD  . PRO B 263 ? 0.1983 0.2045 0.1880 -0.0094 -0.0263 0.0349  275 PRO B CD  
4536 N N   . VAL B 264 ? 0.2052 0.2212 0.1903 -0.0119 -0.0318 0.0508  276 VAL B N   
4537 C CA  . VAL B 264 ? 0.2375 0.2505 0.2229 -0.0098 -0.0333 0.0565  276 VAL B CA  
4538 C C   . VAL B 264 ? 0.2930 0.3143 0.2776 -0.0096 -0.0354 0.0613  276 VAL B C   
4539 O O   . VAL B 264 ? 0.3309 0.3507 0.3156 -0.0077 -0.0366 0.0668  276 VAL B O   
4540 C CB  . VAL B 264 ? 0.2565 0.2649 0.2400 -0.0121 -0.0324 0.0574  276 VAL B CB  
4541 C CG1 . VAL B 264 ? 0.2651 0.2648 0.2503 -0.0114 -0.0309 0.0537  276 VAL B CG1 
4542 C CG2 . VAL B 264 ? 0.2975 0.3123 0.2772 -0.0168 -0.0315 0.0562  276 VAL B CG2 
4543 N N   . SER B 265 ? 0.2638 0.2940 0.2478 -0.0115 -0.0360 0.0595  277 SER B N   
4544 C CA  . SER B 265 ? 0.2711 0.3109 0.2547 -0.0114 -0.0384 0.0635  277 SER B CA  
4545 C C   . SER B 265 ? 0.2746 0.3220 0.2583 -0.0140 -0.0383 0.0590  277 SER B C   
4546 O O   . SER B 265 ? 0.2955 0.3396 0.2793 -0.0154 -0.0361 0.0534  277 SER B O   
4547 C CB  . SER B 265 ? 0.2775 0.3215 0.2566 -0.0141 -0.0394 0.0676  277 SER B CB  
4548 O OG  . SER B 265 ? 0.2814 0.3305 0.2564 -0.0192 -0.0384 0.0635  277 SER B OG  
4549 N N   . SER B 266 ? 0.2662 0.3238 0.2498 -0.0147 -0.0406 0.0616  278 SER B N   
4550 C CA  . SER B 266 ? 0.2878 0.3534 0.2710 -0.0181 -0.0407 0.0573  278 SER B CA  
4551 C C   . SER B 266 ? 0.2393 0.3069 0.2168 -0.0237 -0.0393 0.0535  278 SER B C   
4552 O O   . SER B 266 ? 0.2790 0.3520 0.2553 -0.0272 -0.0389 0.0492  278 SER B O   
4553 C CB  . SER B 266 ? 0.2915 0.3685 0.2763 -0.0176 -0.0439 0.0613  278 SER B CB  
4554 O OG  . SER B 266 ? 0.3402 0.4224 0.3209 -0.0189 -0.0460 0.0662  278 SER B OG  
4555 N N   . ASP B 267 ? 0.2336 0.2969 0.2075 -0.0247 -0.0384 0.0549  279 ASP B N   
4556 C CA  . ASP B 267 ? 0.2219 0.2879 0.1901 -0.0298 -0.0371 0.0517  279 ASP B CA  
4557 C C   . ASP B 267 ? 0.2351 0.2924 0.2019 -0.0304 -0.0341 0.0498  279 ASP B C   
4558 O O   . ASP B 267 ? 0.2237 0.2827 0.1857 -0.0342 -0.0326 0.0479  279 ASP B O   
4559 C CB  . ASP B 267 ? 0.2560 0.3308 0.2197 -0.0317 -0.0396 0.0565  279 ASP B CB  
4560 C CG  . ASP B 267 ? 0.2816 0.3608 0.2388 -0.0373 -0.0383 0.0530  279 ASP B CG  
4561 O OD1 . ASP B 267 ? 0.2495 0.3294 0.2061 -0.0401 -0.0366 0.0467  279 ASP B OD1 
4562 O OD2 . ASP B 267 ? 0.3079 0.3892 0.2604 -0.0387 -0.0388 0.0565  279 ASP B OD2 
4563 N N   . HIS B 268 ? 0.2417 0.2901 0.2125 -0.0268 -0.0332 0.0501  280 HIS B N   
4564 C CA  . HIS B 268 ? 0.2250 0.2659 0.1950 -0.0274 -0.0308 0.0487  280 HIS B CA  
4565 C C   . HIS B 268 ? 0.2277 0.2604 0.2018 -0.0248 -0.0292 0.0452  280 HIS B C   
4566 O O   . HIS B 268 ? 0.2904 0.3200 0.2682 -0.0210 -0.0303 0.0464  280 HIS B O   
4567 C CB  . HIS B 268 ? 0.2658 0.3036 0.2353 -0.0261 -0.0318 0.0546  280 HIS B CB  
4568 C CG  . HIS B 268 ? 0.2937 0.3387 0.2584 -0.0287 -0.0329 0.0584  280 HIS B CG  
4569 N ND1 . HIS B 268 ? 0.3149 0.3658 0.2793 -0.0272 -0.0359 0.0636  280 HIS B ND1 
4570 C CD2 . HIS B 268 ? 0.2788 0.3265 0.2386 -0.0325 -0.0315 0.0580  280 HIS B CD2 
4571 C CE1 . HIS B 268 ? 0.2761 0.3330 0.2353 -0.0301 -0.0365 0.0663  280 HIS B CE1 
4572 N NE2 . HIS B 268 ? 0.2848 0.3397 0.2409 -0.0334 -0.0337 0.0628  280 HIS B NE2 
4573 N N   . LEU B 269 ? 0.2307 0.2600 0.2040 -0.0267 -0.0265 0.0410  281 LEU B N   
4574 C CA  . LEU B 269 ? 0.2091 0.2308 0.1857 -0.0245 -0.0250 0.0379  281 LEU B CA  
4575 C C   . LEU B 269 ? 0.2554 0.2719 0.2321 -0.0248 -0.0242 0.0392  281 LEU B C   
4576 O O   . LEU B 269 ? 0.2400 0.2591 0.2139 -0.0278 -0.0232 0.0399  281 LEU B O   
4577 C CB  . LEU B 269 ? 0.2075 0.2297 0.1838 -0.0261 -0.0226 0.0320  281 LEU B CB  
4578 C CG  . LEU B 269 ? 0.1766 0.2049 0.1519 -0.0275 -0.0228 0.0300  281 LEU B CG  
4579 C CD1 . LEU B 269 ? 0.1845 0.2120 0.1590 -0.0296 -0.0198 0.0241  281 LEU B CD1 
4580 C CD2 . LEU B 269 ? 0.2156 0.2444 0.1944 -0.0242 -0.0249 0.0318  281 LEU B CD2 
4581 N N   . PHE B 270 ? 0.2372 0.2465 0.2172 -0.0218 -0.0245 0.0395  282 PHE B N   
4582 C CA  . PHE B 270 ? 0.2024 0.2068 0.1832 -0.0223 -0.0239 0.0406  282 PHE B CA  
4583 C C   . PHE B 270 ? 0.2258 0.2264 0.2086 -0.0221 -0.0220 0.0359  282 PHE B C   
4584 O O   . PHE B 270 ? 0.1927 0.1898 0.1776 -0.0195 -0.0222 0.0337  282 PHE B O   
4585 C CB  . PHE B 270 ? 0.1920 0.1908 0.1748 -0.0195 -0.0259 0.0447  282 PHE B CB  
4586 C CG  . PHE B 270 ? 0.2159 0.2096 0.1997 -0.0205 -0.0254 0.0460  282 PHE B CG  
4587 C CD1 . PHE B 270 ? 0.2541 0.2497 0.2361 -0.0230 -0.0252 0.0497  282 PHE B CD1 
4588 C CD2 . PHE B 270 ? 0.2231 0.2103 0.2097 -0.0191 -0.0251 0.0434  282 PHE B CD2 
4589 C CE1 . PHE B 270 ? 0.2314 0.2224 0.2149 -0.0243 -0.0245 0.0508  282 PHE B CE1 
4590 C CE2 . PHE B 270 ? 0.2554 0.2384 0.2434 -0.0206 -0.0249 0.0443  282 PHE B CE2 
4591 C CZ  . PHE B 270 ? 0.2597 0.2446 0.2464 -0.0232 -0.0245 0.0480  282 PHE B CZ  
4592 N N   . LEU B 271 ? 0.1827 0.1842 0.1649 -0.0248 -0.0201 0.0348  283 LEU B N   
4593 C CA  . LEU B 271 ? 0.1983 0.1976 0.1823 -0.0249 -0.0181 0.0307  283 LEU B CA  
4594 C C   . LEU B 271 ? 0.2071 0.2023 0.1937 -0.0251 -0.0183 0.0320  283 LEU B C   
4595 O O   . LEU B 271 ? 0.2121 0.2084 0.1979 -0.0272 -0.0183 0.0352  283 LEU B O   
4596 C CB  . LEU B 271 ? 0.2116 0.2161 0.1933 -0.0278 -0.0153 0.0280  283 LEU B CB  
4597 C CG  . LEU B 271 ? 0.2280 0.2309 0.2118 -0.0280 -0.0129 0.0247  283 LEU B CG  
4598 C CD1 . LEU B 271 ? 0.1842 0.1841 0.1699 -0.0253 -0.0125 0.0212  283 LEU B CD1 
4599 C CD2 . LEU B 271 ? 0.1989 0.2065 0.1804 -0.0311 -0.0098 0.0230  283 LEU B CD2 
4600 N N   . PHE B 272 ? 0.1644 0.1551 0.1540 -0.0231 -0.0186 0.0298  284 PHE B N   
4601 C CA  . PHE B 272 ? 0.1893 0.1766 0.1816 -0.0237 -0.0190 0.0306  284 PHE B CA  
4602 C C   . PHE B 272 ? 0.2308 0.2166 0.2260 -0.0227 -0.0181 0.0269  284 PHE B C   
4603 O O   . PHE B 272 ? 0.2226 0.2059 0.2181 -0.0200 -0.0186 0.0246  284 PHE B O   
4604 C CB  . PHE B 272 ? 0.1878 0.1693 0.1811 -0.0221 -0.0215 0.0334  284 PHE B CB  
4605 C CG  . PHE B 272 ? 0.2005 0.1780 0.1967 -0.0231 -0.0221 0.0337  284 PHE B CG  
4606 C CD1 . PHE B 272 ? 0.2294 0.2088 0.2263 -0.0264 -0.0211 0.0360  284 PHE B CD1 
4607 C CD2 . PHE B 272 ? 0.2344 0.2067 0.2327 -0.0210 -0.0234 0.0315  284 PHE B CD2 
4608 C CE1 . PHE B 272 ? 0.2240 0.2004 0.2243 -0.0279 -0.0216 0.0362  284 PHE B CE1 
4609 C CE2 . PHE B 272 ? 0.2609 0.2300 0.2619 -0.0225 -0.0242 0.0315  284 PHE B CE2 
4610 C CZ  . PHE B 272 ? 0.2719 0.2432 0.2742 -0.0260 -0.0233 0.0338  284 PHE B CZ  
4611 N N   . GLY B 273 ? 0.1835 0.1710 0.1809 -0.0249 -0.0169 0.0268  285 GLY B N   
4612 C CA  . GLY B 273 ? 0.2272 0.2135 0.2282 -0.0241 -0.0168 0.0243  285 GLY B CA  
4613 C C   . GLY B 273 ? 0.1935 0.1824 0.1946 -0.0228 -0.0145 0.0207  285 GLY B C   
4614 O O   . GLY B 273 ? 0.2049 0.1974 0.2037 -0.0238 -0.0122 0.0198  285 GLY B O   
4615 N N   . GLY B 274 ? 0.1637 0.1506 0.1675 -0.0208 -0.0151 0.0186  286 GLY B N   
4616 C CA  . GLY B 274 ? 0.1667 0.1551 0.1710 -0.0190 -0.0130 0.0156  286 GLY B CA  
4617 C C   . GLY B 274 ? 0.1519 0.1436 0.1602 -0.0197 -0.0114 0.0147  286 GLY B C   
4618 O O   . GLY B 274 ? 0.1916 0.1840 0.2030 -0.0212 -0.0126 0.0160  286 GLY B O   
4619 N N   . PHE B 275 ? 0.1711 0.1649 0.1795 -0.0186 -0.0085 0.0123  287 PHE B N   
4620 C CA  . PHE B 275 ? 0.1948 0.1912 0.2074 -0.0176 -0.0070 0.0111  287 PHE B CA  
4621 C C   . PHE B 275 ? 0.1436 0.1431 0.1553 -0.0179 -0.0026 0.0094  287 PHE B C   
4622 O O   . PHE B 275 ? 0.1816 0.1794 0.1901 -0.0168 -0.0011 0.0077  287 PHE B O   
4623 C CB  . PHE B 275 ? 0.1995 0.1926 0.2132 -0.0139 -0.0088 0.0097  287 PHE B CB  
4624 C CG  . PHE B 275 ? 0.1993 0.1951 0.2179 -0.0125 -0.0087 0.0092  287 PHE B CG  
4625 C CD1 . PHE B 275 ? 0.2289 0.2284 0.2518 -0.0147 -0.0096 0.0105  287 PHE B CD1 
4626 C CD2 . PHE B 275 ? 0.2228 0.2178 0.2419 -0.0089 -0.0077 0.0075  287 PHE B CD2 
4627 C CE1 . PHE B 275 ? 0.2671 0.2700 0.2951 -0.0134 -0.0097 0.0101  287 PHE B CE1 
4628 C CE2 . PHE B 275 ? 0.2274 0.2255 0.2512 -0.0073 -0.0078 0.0073  287 PHE B CE2 
4629 C CZ  . PHE B 275 ? 0.2104 0.2129 0.2388 -0.0095 -0.0089 0.0086  287 PHE B CZ  
4630 N N   . THR B 276 ? 0.1783 0.1824 0.1930 -0.0195 -0.0004 0.0097  288 THR B N   
4631 C CA  . THR B 276 ? 0.1798 0.1866 0.1931 -0.0202 0.0043  0.0080  288 THR B CA  
4632 C C   . THR B 276 ? 0.2008 0.2076 0.2169 -0.0168 0.0068  0.0058  288 THR B C   
4633 O O   . THR B 276 ? 0.2010 0.2071 0.2207 -0.0142 0.0048  0.0060  288 THR B O   
4634 C CB  . THR B 276 ? 0.2323 0.2440 0.2472 -0.0233 0.0062  0.0095  288 THR B CB  
4635 O OG1 . THR B 276 ? 0.2109 0.2257 0.2322 -0.0225 0.0061  0.0101  288 THR B OG1 
4636 C CG2 . THR B 276 ? 0.2099 0.2213 0.2226 -0.0263 0.0035  0.0124  288 THR B CG2 
4637 N N   . THR B 277 ? 0.1789 0.1866 0.1931 -0.0170 0.0112  0.0037  289 THR B N   
4638 C CA  . THR B 277 ? 0.2359 0.2434 0.2527 -0.0137 0.0145  0.0018  289 THR B CA  
4639 C C   . THR B 277 ? 0.2401 0.2520 0.2639 -0.0123 0.0142  0.0031  289 THR B C   
4640 O O   . THR B 277 ? 0.2410 0.2523 0.2682 -0.0087 0.0138  0.0029  289 THR B O   
4641 C CB  . THR B 277 ? 0.2283 0.2363 0.2420 -0.0149 0.0199  -0.0007 289 THR B CB  
4642 O OG1 . THR B 277 ? 0.2164 0.2206 0.2241 -0.0161 0.0199  -0.0023 289 THR B OG1 
4643 C CG2 . THR B 277 ? 0.2105 0.2182 0.2275 -0.0113 0.0238  -0.0024 289 THR B CG2 
4644 N N   . ASP B 278 ? 0.2470 0.2635 0.2730 -0.0152 0.0143  0.0048  290 ASP B N   
4645 C CA  . ASP B 278 ? 0.2542 0.2761 0.2874 -0.0149 0.0140  0.0063  290 ASP B CA  
4646 C C   . ASP B 278 ? 0.2406 0.2622 0.2766 -0.0153 0.0085  0.0083  290 ASP B C   
4647 O O   . ASP B 278 ? 0.3060 0.3324 0.3473 -0.0168 0.0075  0.0100  290 ASP B O   
4648 C CB  . ASP B 278 ? 0.3090 0.3359 0.3431 -0.0183 0.0171  0.0073  290 ASP B CB  
4649 C CG  . ASP B 278 ? 0.3744 0.4018 0.4057 -0.0179 0.0230  0.0049  290 ASP B CG  
4650 O OD1 . ASP B 278 ? 0.3850 0.4110 0.4176 -0.0143 0.0255  0.0030  290 ASP B OD1 
4651 O OD2 . ASP B 278 ? 0.4265 0.4552 0.4539 -0.0212 0.0251  0.0050  290 ASP B OD2 
4652 N N   . LYS B 279 ? 0.2466 0.2627 0.2790 -0.0141 0.0051  0.0080  291 LYS B N   
4653 C CA  . LYS B 279 ? 0.2393 0.2541 0.2737 -0.0139 0.0000  0.0092  291 LYS B CA  
4654 C C   . LYS B 279 ? 0.2418 0.2581 0.2774 -0.0180 -0.0021 0.0114  291 LYS B C   
4655 O O   . LYS B 279 ? 0.3106 0.3286 0.3506 -0.0187 -0.0052 0.0124  291 LYS B O   
4656 C CB  . LYS B 279 ? 0.2278 0.2455 0.2678 -0.0107 -0.0008 0.0090  291 LYS B CB  
4657 C CG  . LYS B 279 ? 0.2559 0.2719 0.2948 -0.0065 0.0021  0.0073  291 LYS B CG  
4658 C CD  . LYS B 279 ? 0.2554 0.2723 0.2979 -0.0025 0.0001  0.0074  291 LYS B CD  
4659 C CE  . LYS B 279 ? 0.3517 0.3628 0.3898 0.0012  0.0012  0.0060  291 LYS B CE  
4660 N NZ  . LYS B 279 ? 0.2857 0.2969 0.3259 0.0054  -0.0010 0.0064  291 LYS B NZ  
4661 N N   . GLN B 280 ? 0.2118 0.2275 0.2434 -0.0209 -0.0007 0.0122  292 GLN B N   
4662 C CA  . GLN B 280 ? 0.2221 0.2379 0.2539 -0.0246 -0.0026 0.0147  292 GLN B CA  
4663 C C   . GLN B 280 ? 0.2513 0.2608 0.2783 -0.0247 -0.0061 0.0154  292 GLN B C   
4664 O O   . GLN B 280 ? 0.1969 0.2038 0.2187 -0.0240 -0.0052 0.0147  292 GLN B O   
4665 C CB  . GLN B 280 ? 0.2316 0.2509 0.2617 -0.0277 0.0010  0.0158  292 GLN B CB  
4666 C CG  . GLN B 280 ? 0.2976 0.3199 0.3311 -0.0314 0.0004  0.0186  292 GLN B CG  
4667 C CD  . GLN B 280 ? 0.2774 0.3058 0.3186 -0.0315 0.0016  0.0186  292 GLN B CD  
4668 O OE1 . GLN B 280 ? 0.3445 0.3758 0.3899 -0.0346 0.0010  0.0207  292 GLN B OE1 
4669 N NE2 . GLN B 280 ? 0.3774 0.4080 0.4210 -0.0281 0.0035  0.0164  292 GLN B NE2 
4670 N N   . PRO B 281 ? 0.2337 0.2407 0.2625 -0.0255 -0.0099 0.0165  293 PRO B N   
4671 C CA  . PRO B 281 ? 0.2301 0.2309 0.2546 -0.0256 -0.0128 0.0176  293 PRO B CA  
4672 C C   . PRO B 281 ? 0.2253 0.2263 0.2467 -0.0286 -0.0116 0.0201  293 PRO B C   
4673 O O   . PRO B 281 ? 0.2187 0.2233 0.2425 -0.0317 -0.0103 0.0218  293 PRO B O   
4674 C CB  . PRO B 281 ? 0.2393 0.2380 0.2672 -0.0264 -0.0165 0.0181  293 PRO B CB  
4675 C CG  . PRO B 281 ? 0.2096 0.2133 0.2431 -0.0256 -0.0162 0.0168  293 PRO B CG  
4676 C CD  . PRO B 281 ? 0.2727 0.2823 0.3076 -0.0262 -0.0118 0.0168  293 PRO B CD  
4677 N N   . LEU B 282 ? 0.1928 0.1901 0.2091 -0.0278 -0.0123 0.0205  294 LEU B N   
4678 C CA  . LEU B 282 ? 0.2224 0.2204 0.2349 -0.0301 -0.0113 0.0229  294 LEU B CA  
4679 C C   . LEU B 282 ? 0.1988 0.1918 0.2098 -0.0307 -0.0143 0.0258  294 LEU B C   
4680 O O   . LEU B 282 ? 0.1844 0.1724 0.1947 -0.0284 -0.0168 0.0251  294 LEU B O   
4681 C CB  . LEU B 282 ? 0.1993 0.1981 0.2071 -0.0288 -0.0096 0.0215  294 LEU B CB  
4682 C CG  . LEU B 282 ? 0.2273 0.2307 0.2356 -0.0287 -0.0058 0.0190  294 LEU B CG  
4683 C CD1 . LEU B 282 ? 0.2004 0.2036 0.2042 -0.0276 -0.0042 0.0168  294 LEU B CD1 
4684 C CD2 . LEU B 282 ? 0.2437 0.2518 0.2529 -0.0320 -0.0032 0.0206  294 LEU B CD2 
4685 N N   . SER B 283 ? 0.1923 0.1865 0.2026 -0.0338 -0.0137 0.0290  295 SER B N   
4686 C CA  . SER B 283 ? 0.2000 0.1895 0.2084 -0.0344 -0.0158 0.0324  295 SER B CA  
4687 C C   . SER B 283 ? 0.2025 0.1945 0.2064 -0.0357 -0.0146 0.0353  295 SER B C   
4688 O O   . SER B 283 ? 0.2387 0.2277 0.2412 -0.0366 -0.0158 0.0390  295 SER B O   
4689 C CB  . SER B 283 ? 0.2537 0.2411 0.2660 -0.0370 -0.0168 0.0344  295 SER B CB  
4690 O OG  . SER B 283 ? 0.2938 0.2868 0.3084 -0.0402 -0.0142 0.0355  295 SER B OG  
4691 N N   . ASP B 284 ? 0.2223 0.2194 0.2236 -0.0359 -0.0121 0.0337  296 ASP B N   
4692 C CA  . ASP B 284 ? 0.2273 0.2271 0.2235 -0.0371 -0.0113 0.0361  296 ASP B CA  
4693 C C   . ASP B 284 ? 0.2269 0.2244 0.2200 -0.0346 -0.0135 0.0363  296 ASP B C   
4694 O O   . ASP B 284 ? 0.2390 0.2340 0.2331 -0.0319 -0.0145 0.0335  296 ASP B O   
4695 C CB  . ASP B 284 ? 0.1992 0.2052 0.1933 -0.0386 -0.0078 0.0340  296 ASP B CB  
4696 C CG  . ASP B 284 ? 0.2125 0.2190 0.2067 -0.0364 -0.0067 0.0293  296 ASP B CG  
4697 O OD1 . ASP B 284 ? 0.2387 0.2421 0.2364 -0.0341 -0.0079 0.0272  296 ASP B OD1 
4698 O OD2 . ASP B 284 ? 0.2448 0.2549 0.2354 -0.0371 -0.0046 0.0276  296 ASP B OD2 
4699 N N   . ALA B 285 ? 0.2162 0.2149 0.2056 -0.0354 -0.0142 0.0399  297 ALA B N   
4700 C CA  . ALA B 285 ? 0.2242 0.2219 0.2109 -0.0332 -0.0162 0.0408  297 ALA B CA  
4701 C C   . ALA B 285 ? 0.2098 0.2137 0.1915 -0.0350 -0.0153 0.0421  297 ALA B C   
4702 O O   . ALA B 285 ? 0.2332 0.2401 0.2129 -0.0377 -0.0139 0.0445  297 ALA B O   
4703 C CB  . ALA B 285 ? 0.2401 0.2323 0.2276 -0.0318 -0.0188 0.0449  297 ALA B CB  
4704 N N   . TRP B 286 ? 0.1732 0.1791 0.1528 -0.0336 -0.0161 0.0404  298 TRP B N   
4705 C CA  . TRP B 286 ? 0.2029 0.2152 0.1775 -0.0354 -0.0156 0.0410  298 TRP B CA  
4706 C C   . TRP B 286 ? 0.2154 0.2285 0.1889 -0.0333 -0.0183 0.0423  298 TRP B C   
4707 O O   . TRP B 286 ? 0.1757 0.1849 0.1522 -0.0303 -0.0197 0.0413  298 TRP B O   
4708 C CB  . TRP B 286 ? 0.1973 0.2134 0.1702 -0.0371 -0.0127 0.0359  298 TRP B CB  
4709 C CG  . TRP B 286 ? 0.2315 0.2477 0.2059 -0.0387 -0.0096 0.0340  298 TRP B CG  
4710 C CD1 . TRP B 286 ? 0.2171 0.2294 0.1965 -0.0375 -0.0090 0.0326  298 TRP B CD1 
4711 C CD2 . TRP B 286 ? 0.2190 0.2399 0.1899 -0.0419 -0.0065 0.0331  298 TRP B CD2 
4712 N NE1 . TRP B 286 ? 0.1946 0.2093 0.1746 -0.0395 -0.0058 0.0312  298 TRP B NE1 
4713 C CE2 . TRP B 286 ? 0.1976 0.2173 0.1723 -0.0421 -0.0040 0.0314  298 TRP B CE2 
4714 C CE3 . TRP B 286 ? 0.2239 0.2502 0.1887 -0.0445 -0.0055 0.0335  298 TRP B CE3 
4715 C CZ2 . TRP B 286 ? 0.2054 0.2290 0.1784 -0.0446 -0.0002 0.0302  298 TRP B CZ2 
4716 C CZ3 . TRP B 286 ? 0.2095 0.2392 0.1718 -0.0471 -0.0019 0.0320  298 TRP B CZ3 
4717 C CH2 . TRP B 286 ? 0.2255 0.2537 0.1920 -0.0471 0.0009  0.0304  298 TRP B CH2 
4718 N N   . THR B 287 ? 0.1992 0.2183 0.1684 -0.0350 -0.0188 0.0445  299 THR B N   
4719 C CA  . THR B 287 ? 0.2500 0.2726 0.2178 -0.0338 -0.0208 0.0444  299 THR B CA  
4720 C C   . THR B 287 ? 0.2673 0.2960 0.2314 -0.0367 -0.0192 0.0403  299 THR B C   
4721 O O   . THR B 287 ? 0.2357 0.2679 0.1959 -0.0399 -0.0173 0.0400  299 THR B O   
4722 C CB  . THR B 287 ? 0.2643 0.2896 0.2304 -0.0331 -0.0235 0.0505  299 THR B CB  
4723 O OG1 . THR B 287 ? 0.3008 0.3309 0.2622 -0.0363 -0.0227 0.0530  299 THR B OG1 
4724 C CG2 . THR B 287 ? 0.2858 0.3040 0.2556 -0.0301 -0.0249 0.0544  299 THR B CG2 
4725 N N   . TYR B 288 ? 0.2442 0.2738 0.2092 -0.0357 -0.0196 0.0370  300 TYR B N   
4726 C CA  . TYR B 288 ? 0.2080 0.2436 0.1693 -0.0386 -0.0186 0.0335  300 TYR B CA  
4727 C C   . TYR B 288 ? 0.2330 0.2749 0.1923 -0.0387 -0.0218 0.0368  300 TYR B C   
4728 O O   . TYR B 288 ? 0.2513 0.2924 0.2141 -0.0357 -0.0242 0.0389  300 TYR B O   
4729 C CB  . TYR B 288 ? 0.2192 0.2524 0.1827 -0.0380 -0.0169 0.0278  300 TYR B CB  
4730 C CG  . TYR B 288 ? 0.1972 0.2358 0.1569 -0.0412 -0.0159 0.0240  300 TYR B CG  
4731 C CD1 . TYR B 288 ? 0.2395 0.2804 0.1945 -0.0448 -0.0131 0.0213  300 TYR B CD1 
4732 C CD2 . TYR B 288 ? 0.1991 0.2404 0.1597 -0.0408 -0.0176 0.0230  300 TYR B CD2 
4733 C CE1 . TYR B 288 ? 0.2578 0.3031 0.2089 -0.0481 -0.0121 0.0173  300 TYR B CE1 
4734 C CE2 . TYR B 288 ? 0.2321 0.2782 0.1895 -0.0442 -0.0167 0.0192  300 TYR B CE2 
4735 C CZ  . TYR B 288 ? 0.2175 0.2653 0.1698 -0.0480 -0.0140 0.0163  300 TYR B CZ  
4736 O OH  . TYR B 288 ? 0.2391 0.2912 0.1878 -0.0517 -0.0132 0.0121  300 TYR B OH  
4737 N N   . CYS B 289 ? 0.2145 0.2629 0.1683 -0.0421 -0.0220 0.0377  301 CYS B N   
4738 C CA  . CYS B 289 ? 0.2175 0.2733 0.1690 -0.0426 -0.0252 0.0410  301 CYS B CA  
4739 C C   . CYS B 289 ? 0.2434 0.3042 0.1936 -0.0450 -0.0251 0.0360  301 CYS B C   
4740 O O   . CYS B 289 ? 0.2697 0.3327 0.2153 -0.0488 -0.0228 0.0318  301 CYS B O   
4741 C CB  . CYS B 289 ? 0.2040 0.2647 0.1499 -0.0450 -0.0258 0.0452  301 CYS B CB  
4742 S SG  . CYS B 289 ? 0.3326 0.4036 0.2755 -0.0455 -0.0302 0.0496  301 CYS B SG  
4743 N N   . ILE B 290 ? 0.2327 0.2947 0.1868 -0.0428 -0.0272 0.0363  302 ILE B N   
4744 C CA  . ILE B 290 ? 0.2179 0.2834 0.1719 -0.0451 -0.0268 0.0312  302 ILE B CA  
4745 C C   . ILE B 290 ? 0.2384 0.3136 0.1865 -0.0496 -0.0282 0.0309  302 ILE B C   
4746 O O   . ILE B 290 ? 0.2762 0.3531 0.2208 -0.0535 -0.0261 0.0254  302 ILE B O   
4747 C CB  . ILE B 290 ? 0.2083 0.2737 0.1683 -0.0416 -0.0287 0.0322  302 ILE B CB  
4748 C CG1 . ILE B 290 ? 0.2438 0.2993 0.2087 -0.0378 -0.0267 0.0308  302 ILE B CG1 
4749 C CG2 . ILE B 290 ? 0.2091 0.2806 0.1689 -0.0446 -0.0290 0.0281  302 ILE B CG2 
4750 C CD1 . ILE B 290 ? 0.2845 0.3387 0.2550 -0.0335 -0.0286 0.0332  302 ILE B CD1 
4751 N N   . SER B 291 ? 0.2690 0.3503 0.2155 -0.0490 -0.0316 0.0368  303 SER B N   
4752 C CA  . SER B 291 ? 0.2515 0.3429 0.1922 -0.0531 -0.0336 0.0369  303 SER B CA  
4753 C C   . SER B 291 ? 0.2603 0.3522 0.1934 -0.0572 -0.0311 0.0347  303 SER B C   
4754 O O   . SER B 291 ? 0.2770 0.3755 0.2045 -0.0618 -0.0313 0.0316  303 SER B O   
4755 C CB  . SER B 291 ? 0.2461 0.3443 0.1874 -0.0509 -0.0381 0.0445  303 SER B CB  
4756 O OG  . SER B 291 ? 0.2732 0.3675 0.2130 -0.0490 -0.0378 0.0497  303 SER B OG  
4757 N N   . LYS B 292 ? 0.2102 0.2954 0.1429 -0.0559 -0.0286 0.0361  304 LYS B N   
4758 C CA  . LYS B 292 ? 0.2981 0.3835 0.2241 -0.0595 -0.0256 0.0340  304 LYS B CA  
4759 C C   . LYS B 292 ? 0.2874 0.3664 0.2138 -0.0608 -0.0209 0.0269  304 LYS B C   
4760 O O   . LYS B 292 ? 0.3062 0.3856 0.2269 -0.0640 -0.0179 0.0240  304 LYS B O   
4761 C CB  . LYS B 292 ? 0.2878 0.3707 0.2129 -0.0578 -0.0254 0.0400  304 LYS B CB  
4762 C CG  . LYS B 292 ? 0.3520 0.4408 0.2758 -0.0564 -0.0297 0.0476  304 LYS B CG  
4763 C CD  . LYS B 292 ? 0.3658 0.4532 0.2861 -0.0565 -0.0286 0.0527  304 LYS B CD  
4764 C CE  . LYS B 292 ? 0.3999 0.4890 0.3218 -0.0532 -0.0323 0.0612  304 LYS B CE  
4765 N NZ  . LYS B 292 ? 0.4240 0.5053 0.3544 -0.0484 -0.0329 0.0629  304 LYS B NZ  
4766 N N   . ASN B 293 ? 0.2659 0.3390 0.1988 -0.0582 -0.0200 0.0243  305 ASN B N   
4767 C CA  . ASN B 293 ? 0.2688 0.3354 0.2028 -0.0586 -0.0155 0.0183  305 ASN B CA  
4768 C C   . ASN B 293 ? 0.2976 0.3601 0.2304 -0.0583 -0.0124 0.0191  305 ASN B C   
4769 O O   . ASN B 293 ? 0.2810 0.3426 0.2101 -0.0609 -0.0086 0.0149  305 ASN B O   
4770 C CB  . ASN B 293 ? 0.2829 0.3527 0.2123 -0.0631 -0.0137 0.0119  305 ASN B CB  
4771 C CG  . ASN B 293 ? 0.3581 0.4206 0.2891 -0.0631 -0.0090 0.0057  305 ASN B CG  
4772 O OD1 . ASN B 293 ? 0.2926 0.3486 0.2296 -0.0593 -0.0079 0.0059  305 ASN B OD1 
4773 N ND2 . ASN B 293 ? 0.3306 0.3942 0.2561 -0.0672 -0.0060 0.0002  305 ASN B ND2 
4774 N N   . GLU B 294 ? 0.2513 0.3114 0.1874 -0.0553 -0.0140 0.0248  306 GLU B N   
4775 C CA  . GLU B 294 ? 0.2429 0.3003 0.1782 -0.0552 -0.0118 0.0269  306 GLU B CA  
4776 C C   . GLU B 294 ? 0.2465 0.2973 0.1889 -0.0511 -0.0125 0.0300  306 GLU B C   
4777 O O   . GLU B 294 ? 0.2564 0.3066 0.2020 -0.0484 -0.0159 0.0337  306 GLU B O   
4778 C CB  . GLU B 294 ? 0.2618 0.3251 0.1913 -0.0572 -0.0134 0.0319  306 GLU B CB  
4779 C CG  . GLU B 294 ? 0.3478 0.4082 0.2784 -0.0562 -0.0125 0.0368  306 GLU B CG  
4780 C CD  . GLU B 294 ? 0.3708 0.4372 0.2945 -0.0586 -0.0133 0.0414  306 GLU B CD  
4781 O OE1 . GLU B 294 ? 0.4356 0.5063 0.3526 -0.0622 -0.0112 0.0384  306 GLU B OE1 
4782 O OE2 . GLU B 294 ? 0.3726 0.4391 0.2972 -0.0569 -0.0159 0.0481  306 GLU B OE2 
4783 N N   . TRP B 295 ? 0.2723 0.3184 0.2168 -0.0508 -0.0093 0.0283  307 TRP B N   
4784 C CA  . TRP B 295 ? 0.2348 0.2751 0.1853 -0.0477 -0.0098 0.0311  307 TRP B CA  
4785 C C   . TRP B 295 ? 0.2478 0.2889 0.1969 -0.0485 -0.0101 0.0366  307 TRP B C   
4786 O O   . TRP B 295 ? 0.2714 0.3159 0.2159 -0.0514 -0.0078 0.0367  307 TRP B O   
4787 C CB  . TRP B 295 ? 0.2413 0.2770 0.1953 -0.0470 -0.0063 0.0268  307 TRP B CB  
4788 C CG  . TRP B 295 ? 0.2286 0.2619 0.1850 -0.0455 -0.0058 0.0222  307 TRP B CG  
4789 C CD1 . TRP B 295 ? 0.2182 0.2528 0.1720 -0.0473 -0.0033 0.0169  307 TRP B CD1 
4790 C CD2 . TRP B 295 ? 0.2047 0.2331 0.1664 -0.0420 -0.0077 0.0223  307 TRP B CD2 
4791 N NE1 . TRP B 295 ? 0.2475 0.2783 0.2051 -0.0449 -0.0034 0.0141  307 TRP B NE1 
4792 C CE2 . TRP B 295 ? 0.2326 0.2599 0.1949 -0.0416 -0.0061 0.0173  307 TRP B CE2 
4793 C CE3 . TRP B 295 ? 0.2319 0.2566 0.1979 -0.0391 -0.0103 0.0260  307 TRP B CE3 
4794 C CZ2 . TRP B 295 ? 0.2332 0.2560 0.1999 -0.0384 -0.0071 0.0162  307 TRP B CZ2 
4795 C CZ3 . TRP B 295 ? 0.1620 0.1822 0.1321 -0.0359 -0.0113 0.0245  307 TRP B CZ3 
4796 C CH2 . TRP B 295 ? 0.1857 0.2053 0.1560 -0.0355 -0.0097 0.0198  307 TRP B CH2 
4797 N N   . ILE B 296 ? 0.2392 0.2765 0.1921 -0.0459 -0.0127 0.0412  308 ILE B N   
4798 C CA  . ILE B 296 ? 0.2609 0.2978 0.2131 -0.0464 -0.0131 0.0470  308 ILE B CA  
4799 C C   . ILE B 296 ? 0.2588 0.2885 0.2173 -0.0444 -0.0129 0.0478  308 ILE B C   
4800 O O   . ILE B 296 ? 0.2571 0.2824 0.2197 -0.0414 -0.0150 0.0479  308 ILE B O   
4801 C CB  . ILE B 296 ? 0.2451 0.2846 0.1952 -0.0454 -0.0168 0.0526  308 ILE B CB  
4802 C CG1 . ILE B 296 ? 0.2991 0.3468 0.2424 -0.0480 -0.0173 0.0519  308 ILE B CG1 
4803 C CG2 . ILE B 296 ? 0.2744 0.3112 0.2250 -0.0451 -0.0173 0.0589  308 ILE B CG2 
4804 C CD1 . ILE B 296 ? 0.4278 0.4797 0.3680 -0.0474 -0.0207 0.0583  308 ILE B CD1 
4805 N N   . GLN B 297 ? 0.2595 0.2884 0.2188 -0.0462 -0.0102 0.0482  309 GLN B N   
4806 C CA  . GLN B 297 ? 0.2460 0.2689 0.2115 -0.0449 -0.0101 0.0486  309 GLN B CA  
4807 C C   . GLN B 297 ? 0.2831 0.3019 0.2500 -0.0436 -0.0128 0.0544  309 GLN B C   
4808 O O   . GLN B 297 ? 0.3414 0.3624 0.3047 -0.0448 -0.0133 0.0593  309 GLN B O   
4809 C CB  . GLN B 297 ? 0.2412 0.2653 0.2078 -0.0474 -0.0064 0.0477  309 GLN B CB  
4810 C CG  . GLN B 297 ? 0.2732 0.2919 0.2466 -0.0465 -0.0064 0.0477  309 GLN B CG  
4811 C CD  . GLN B 297 ? 0.2897 0.3102 0.2661 -0.0478 -0.0029 0.0440  309 GLN B CD  
4812 O OE1 . GLN B 297 ? 0.3368 0.3621 0.3100 -0.0496 0.0002  0.0420  309 GLN B OE1 
4813 N NE2 . GLN B 297 ? 0.3467 0.3635 0.3295 -0.0468 -0.0033 0.0431  309 GLN B NE2 
4814 N N   . PHE B 298 ? 0.3068 0.3192 0.2788 -0.0410 -0.0144 0.0539  310 PHE B N   
4815 C CA  . PHE B 298 ? 0.3215 0.3286 0.2951 -0.0391 -0.0170 0.0585  310 PHE B CA  
4816 C C   . PHE B 298 ? 0.3530 0.3550 0.3307 -0.0402 -0.0161 0.0599  310 PHE B C   
4817 O O   . PHE B 298 ? 0.3222 0.3217 0.3041 -0.0400 -0.0155 0.0560  310 PHE B O   
4818 C CB  . PHE B 298 ? 0.3395 0.3432 0.3154 -0.0353 -0.0194 0.0568  310 PHE B CB  
4819 C CG  . PHE B 298 ? 0.3457 0.3437 0.3228 -0.0328 -0.0218 0.0614  310 PHE B CG  
4820 C CD1 . PHE B 298 ? 0.3993 0.3999 0.3735 -0.0317 -0.0235 0.0660  310 PHE B CD1 
4821 C CD2 . PHE B 298 ? 0.2935 0.2836 0.2748 -0.0315 -0.0224 0.0610  310 PHE B CD2 
4822 C CE1 . PHE B 298 ? 0.3976 0.3925 0.3732 -0.0290 -0.0253 0.0705  310 PHE B CE1 
4823 C CE2 . PHE B 298 ? 0.2893 0.2733 0.2717 -0.0292 -0.0242 0.0649  310 PHE B CE2 
4824 C CZ  . PHE B 298 ? 0.4054 0.3916 0.3850 -0.0277 -0.0255 0.0698  310 PHE B CZ  
4825 N N   . ASN B 299 ? 0.3789 0.3794 0.3554 -0.0416 -0.0161 0.0654  311 ASN B N   
4826 C CA  . ASN B 299 ? 0.3653 0.3609 0.3457 -0.0433 -0.0152 0.0671  311 ASN B CA  
4827 C C   . ASN B 299 ? 0.3699 0.3569 0.3536 -0.0408 -0.0177 0.0683  311 ASN B C   
4828 O O   . ASN B 299 ? 0.4157 0.4005 0.3976 -0.0382 -0.0196 0.0715  311 ASN B O   
4829 C CB  . ASN B 299 ? 0.4128 0.4106 0.3903 -0.0463 -0.0135 0.0725  311 ASN B CB  
4830 C CG  . ASN B 299 ? 0.5096 0.5159 0.4829 -0.0488 -0.0108 0.0711  311 ASN B CG  
4831 O OD1 . ASN B 299 ? 0.5955 0.6041 0.5709 -0.0511 -0.0081 0.0685  311 ASN B OD1 
4832 N ND2 . ASN B 299 ? 0.5021 0.5133 0.4696 -0.0483 -0.0116 0.0727  311 ASN B ND2 
4833 N N   . HIS B 300 ? 0.3987 0.3811 0.3872 -0.0413 -0.0176 0.0656  312 HIS B N   
4834 C CA  . HIS B 300 ? 0.3423 0.3164 0.3338 -0.0389 -0.0198 0.0652  312 HIS B CA  
4835 C C   . HIS B 300 ? 0.3502 0.3199 0.3462 -0.0416 -0.0192 0.0645  312 HIS B C   
4836 O O   . HIS B 300 ? 0.3283 0.3027 0.3261 -0.0447 -0.0171 0.0632  312 HIS B O   
4837 C CB  . HIS B 300 ? 0.3356 0.3095 0.3277 -0.0355 -0.0212 0.0602  312 HIS B CB  
4838 C CG  . HIS B 300 ? 0.3350 0.3127 0.3293 -0.0365 -0.0199 0.0549  312 HIS B CG  
4839 N ND1 . HIS B 300 ? 0.3434 0.3175 0.3420 -0.0368 -0.0204 0.0518  312 HIS B ND1 
4840 C CD2 . HIS B 300 ? 0.3294 0.3143 0.3222 -0.0373 -0.0182 0.0522  312 HIS B CD2 
4841 C CE1 . HIS B 300 ? 0.2708 0.2500 0.2708 -0.0373 -0.0190 0.0479  312 HIS B CE1 
4842 N NE2 . HIS B 300 ? 0.2905 0.2758 0.2870 -0.0376 -0.0174 0.0479  312 HIS B NE2 
4843 N N   . PRO B 301 ? 0.3419 0.3030 0.3401 -0.0406 -0.0208 0.0651  313 PRO B N   
4844 C CA  . PRO B 301 ? 0.3790 0.3359 0.3817 -0.0437 -0.0205 0.0643  313 PRO B CA  
4845 C C   . PRO B 301 ? 0.3442 0.3005 0.3505 -0.0431 -0.0216 0.0584  313 PRO B C   
4846 O O   . PRO B 301 ? 0.3631 0.3155 0.3733 -0.0455 -0.0220 0.0574  313 PRO B O   
4847 C CB  . PRO B 301 ? 0.3567 0.3036 0.3591 -0.0429 -0.0217 0.0681  313 PRO B CB  
4848 C CG  . PRO B 301 ? 0.3801 0.3251 0.3795 -0.0379 -0.0233 0.0680  313 PRO B CG  
4849 C CD  . PRO B 301 ? 0.3801 0.3347 0.3766 -0.0369 -0.0227 0.0672  313 PRO B CD  
4850 N N   . TYR B 302 ? 0.3000 0.2603 0.3052 -0.0403 -0.0221 0.0545  314 TYR B N   
4851 C CA  . TYR B 302 ? 0.3647 0.3247 0.3729 -0.0394 -0.0231 0.0492  314 TYR B CA  
4852 C C   . TYR B 302 ? 0.3165 0.2850 0.3267 -0.0409 -0.0212 0.0465  314 TYR B C   
4853 O O   . TYR B 302 ? 0.2991 0.2696 0.3101 -0.0389 -0.0217 0.0424  314 TYR B O   
4854 C CB  . TYR B 302 ? 0.3510 0.3083 0.3568 -0.0348 -0.0248 0.0468  314 TYR B CB  
4855 C CG  . TYR B 302 ? 0.3717 0.3211 0.3755 -0.0325 -0.0263 0.0494  314 TYR B CG  
4856 C CD1 . TYR B 302 ? 0.3923 0.3331 0.3977 -0.0323 -0.0278 0.0485  314 TYR B CD1 
4857 C CD2 . TYR B 302 ? 0.3750 0.3257 0.3753 -0.0302 -0.0262 0.0525  314 TYR B CD2 
4858 C CE1 . TYR B 302 ? 0.4272 0.3601 0.4307 -0.0298 -0.0288 0.0507  314 TYR B CE1 
4859 C CE2 . TYR B 302 ? 0.3760 0.3197 0.3749 -0.0275 -0.0274 0.0551  314 TYR B CE2 
4860 C CZ  . TYR B 302 ? 0.4045 0.3391 0.4051 -0.0271 -0.0285 0.0542  314 TYR B CZ  
4861 O OH  . TYR B 302 ? 0.3864 0.3136 0.3855 -0.0241 -0.0292 0.0568  314 TYR B OH  
4862 N N   . THR B 303 ? 0.2946 0.2679 0.3056 -0.0444 -0.0189 0.0489  315 THR B N   
4863 C CA  . THR B 303 ? 0.3101 0.2914 0.3232 -0.0456 -0.0166 0.0464  315 THR B CA  
4864 C C   . THR B 303 ? 0.3274 0.3092 0.3461 -0.0461 -0.0175 0.0428  315 THR B C   
4865 O O   . THR B 303 ? 0.2800 0.2674 0.3004 -0.0452 -0.0162 0.0397  315 THR B O   
4866 C CB  . THR B 303 ? 0.3471 0.3331 0.3602 -0.0494 -0.0137 0.0499  315 THR B CB  
4867 O OG1 . THR B 303 ? 0.4040 0.3876 0.4219 -0.0527 -0.0139 0.0514  315 THR B OG1 
4868 C CG2 . THR B 303 ? 0.3709 0.3554 0.3784 -0.0492 -0.0135 0.0544  315 THR B CG2 
4869 N N   . GLU B 304 ? 0.3022 0.2784 0.3239 -0.0475 -0.0195 0.0432  316 GLU B N   
4870 C CA  . GLU B 304 ? 0.3324 0.3094 0.3594 -0.0483 -0.0209 0.0399  316 GLU B CA  
4871 C C   . GLU B 304 ? 0.3420 0.3144 0.3678 -0.0446 -0.0237 0.0363  316 GLU B C   
4872 O O   . GLU B 304 ? 0.3251 0.2964 0.3543 -0.0451 -0.0257 0.0338  316 GLU B O   
4873 C CB  . GLU B 304 ? 0.3974 0.3713 0.4285 -0.0526 -0.0215 0.0418  316 GLU B CB  
4874 C CG  . GLU B 304 ? 0.4298 0.4094 0.4634 -0.0567 -0.0184 0.0449  316 GLU B CG  
4875 C CD  . GLU B 304 ? 0.5184 0.4968 0.5578 -0.0613 -0.0190 0.0457  316 GLU B CD  
4876 O OE1 . GLU B 304 ? 0.5592 0.5299 0.5992 -0.0618 -0.0217 0.0450  316 GLU B OE1 
4877 O OE2 . GLU B 304 ? 0.6185 0.6038 0.6622 -0.0646 -0.0165 0.0469  316 GLU B OE2 
4878 N N   . LYS B 305 ? 0.3251 0.2953 0.3460 -0.0410 -0.0240 0.0361  317 LYS B N   
4879 C CA  . LYS B 305 ? 0.2715 0.2374 0.2906 -0.0372 -0.0262 0.0330  317 LYS B CA  
4880 C C   . LYS B 305 ? 0.2595 0.2299 0.2761 -0.0340 -0.0249 0.0311  317 LYS B C   
4881 O O   . LYS B 305 ? 0.2908 0.2588 0.3035 -0.0312 -0.0251 0.0314  317 LYS B O   
4882 C CB  . LYS B 305 ? 0.3215 0.2786 0.3373 -0.0357 -0.0278 0.0347  317 LYS B CB  
4883 C CG  . LYS B 305 ? 0.3387 0.2901 0.3565 -0.0391 -0.0288 0.0367  317 LYS B CG  
4884 C CD  . LYS B 305 ? 0.4305 0.3719 0.4458 -0.0369 -0.0308 0.0366  317 LYS B CD  
4885 C CE  . LYS B 305 ? 0.4329 0.3678 0.4506 -0.0406 -0.0317 0.0376  317 LYS B CE  
4886 N NZ  . LYS B 305 ? 0.5074 0.4317 0.5219 -0.0388 -0.0326 0.0391  317 LYS B NZ  
4887 N N   . PRO B 306 ? 0.2379 0.2150 0.2571 -0.0342 -0.0233 0.0291  318 PRO B N   
4888 C CA  . PRO B 306 ? 0.2206 0.2007 0.2377 -0.0311 -0.0220 0.0268  318 PRO B CA  
4889 C C   . PRO B 306 ? 0.2098 0.1851 0.2254 -0.0275 -0.0243 0.0243  318 PRO B C   
4890 O O   . PRO B 306 ? 0.2106 0.1819 0.2278 -0.0275 -0.0267 0.0233  318 PRO B O   
4891 C CB  . PRO B 306 ? 0.2447 0.2318 0.2659 -0.0320 -0.0200 0.0252  318 PRO B CB  
4892 C CG  . PRO B 306 ? 0.2253 0.2126 0.2515 -0.0349 -0.0214 0.0258  318 PRO B CG  
4893 C CD  . PRO B 306 ? 0.2154 0.1975 0.2401 -0.0372 -0.0225 0.0288  318 PRO B CD  
4894 N N   . ARG B 307 ? 0.1931 0.1684 0.2053 -0.0246 -0.0235 0.0232  319 ARG B N   
4895 C CA  . ARG B 307 ? 0.2153 0.1866 0.2257 -0.0210 -0.0250 0.0210  319 ARG B CA  
4896 C C   . ARG B 307 ? 0.1961 0.1708 0.2051 -0.0187 -0.0230 0.0189  319 ARG B C   
4897 O O   . ARG B 307 ? 0.1895 0.1675 0.1968 -0.0194 -0.0208 0.0197  319 ARG B O   
4898 C CB  . ARG B 307 ? 0.1877 0.1529 0.1947 -0.0195 -0.0265 0.0225  319 ARG B CB  
4899 C CG  . ARG B 307 ? 0.2123 0.1722 0.2200 -0.0212 -0.0283 0.0244  319 ARG B CG  
4900 C CD  . ARG B 307 ? 0.2422 0.1984 0.2515 -0.0208 -0.0306 0.0219  319 ARG B CD  
4901 N NE  . ARG B 307 ? 0.2665 0.2164 0.2763 -0.0226 -0.0323 0.0231  319 ARG B NE  
4902 C CZ  . ARG B 307 ? 0.2856 0.2363 0.2989 -0.0264 -0.0328 0.0238  319 ARG B CZ  
4903 N NH1 . ARG B 307 ? 0.2577 0.2157 0.2745 -0.0287 -0.0315 0.0238  319 ARG B NH1 
4904 N NH2 . ARG B 307 ? 0.3743 0.3180 0.3876 -0.0280 -0.0344 0.0245  319 ARG B NH2 
4905 N N   . LEU B 308 ? 0.1870 0.1604 0.1964 -0.0160 -0.0236 0.0164  320 LEU B N   
4906 C CA  . LEU B 308 ? 0.1660 0.1409 0.1738 -0.0133 -0.0218 0.0145  320 LEU B CA  
4907 C C   . LEU B 308 ? 0.2210 0.1908 0.2266 -0.0099 -0.0235 0.0131  320 LEU B C   
4908 O O   . LEU B 308 ? 0.2193 0.1860 0.2256 -0.0093 -0.0259 0.0125  320 LEU B O   
4909 C CB  . LEU B 308 ? 0.1863 0.1661 0.1972 -0.0132 -0.0198 0.0129  320 LEU B CB  
4910 C CG  . LEU B 308 ? 0.2202 0.2017 0.2354 -0.0137 -0.0213 0.0124  320 LEU B CG  
4911 C CD1 . LEU B 308 ? 0.2145 0.1997 0.2318 -0.0116 -0.0195 0.0107  320 LEU B CD1 
4912 C CD2 . LEU B 308 ? 0.2126 0.1974 0.2308 -0.0176 -0.0210 0.0143  320 LEU B CD2 
4913 N N   . TRP B 309 ? 0.1713 0.1406 0.1743 -0.0078 -0.0221 0.0125  321 TRP B N   
4914 C CA  . TRP B 309 ? 0.1834 0.1481 0.1839 -0.0044 -0.0231 0.0114  321 TRP B CA  
4915 C C   . TRP B 309 ? 0.2249 0.1845 0.2240 -0.0042 -0.0255 0.0127  321 TRP B C   
4916 O O   . TRP B 309 ? 0.2223 0.1773 0.2197 -0.0016 -0.0269 0.0117  321 TRP B O   
4917 C CB  . TRP B 309 ? 0.2018 0.1657 0.2030 -0.0022 -0.0237 0.0093  321 TRP B CB  
4918 C CG  . TRP B 309 ? 0.2052 0.1674 0.2040 0.0012  -0.0224 0.0079  321 TRP B CG  
4919 C CD1 . TRP B 309 ? 0.1687 0.1301 0.1653 0.0021  -0.0209 0.0082  321 TRP B CD1 
4920 C CD2 . TRP B 309 ? 0.2013 0.1626 0.1999 0.0040  -0.0225 0.0064  321 TRP B CD2 
4921 N NE1 . TRP B 309 ? 0.1884 0.1481 0.1834 0.0052  -0.0198 0.0068  321 TRP B NE1 
4922 C CE2 . TRP B 309 ? 0.1664 0.1258 0.1623 0.0065  -0.0207 0.0058  321 TRP B CE2 
4923 C CE3 . TRP B 309 ? 0.1773 0.1397 0.1776 0.0046  -0.0240 0.0056  321 TRP B CE3 
4924 C CZ2 . TRP B 309 ? 0.1924 0.1504 0.1870 0.0097  -0.0201 0.0046  321 TRP B CZ2 
4925 C CZ3 . TRP B 309 ? 0.2009 0.1624 0.2000 0.0080  -0.0236 0.0045  321 TRP B CZ3 
4926 C CH2 . TRP B 309 ? 0.1972 0.1562 0.1933 0.0105  -0.0216 0.0041  321 TRP B CH2 
4927 N N   . HIS B 310 ? 0.2034 0.1635 0.2028 -0.0066 -0.0257 0.0151  322 HIS B N   
4928 C CA  . HIS B 310 ? 0.2103 0.1657 0.2084 -0.0061 -0.0273 0.0170  322 HIS B CA  
4929 C C   . HIS B 310 ? 0.2144 0.1700 0.2102 -0.0040 -0.0264 0.0177  322 HIS B C   
4930 O O   . HIS B 310 ? 0.2259 0.1852 0.2213 -0.0034 -0.0246 0.0166  322 HIS B O   
4931 C CB  . HIS B 310 ? 0.2375 0.1937 0.2369 -0.0095 -0.0277 0.0197  322 HIS B CB  
4932 C CG  . HIS B 310 ? 0.2037 0.1661 0.2031 -0.0115 -0.0257 0.0211  322 HIS B CG  
4933 N ND1 . HIS B 310 ? 0.2005 0.1681 0.2012 -0.0129 -0.0238 0.0196  322 HIS B ND1 
4934 C CD2 . HIS B 310 ? 0.2229 0.1872 0.2208 -0.0123 -0.0252 0.0238  322 HIS B CD2 
4935 C CE1 . HIS B 310 ? 0.2261 0.1982 0.2258 -0.0147 -0.0221 0.0210  322 HIS B CE1 
4936 N NE2 . HIS B 310 ? 0.2325 0.2030 0.2304 -0.0144 -0.0231 0.0235  322 HIS B NE2 
4937 N N   . THR B 311 ? 0.2151 0.1669 0.2099 -0.0030 -0.0275 0.0197  323 THR B N   
4938 C CA  . THR B 311 ? 0.2386 0.1916 0.2322 -0.0011 -0.0268 0.0211  323 THR B CA  
4939 C C   . THR B 311 ? 0.2374 0.1910 0.2312 -0.0025 -0.0274 0.0249  323 THR B C   
4940 O O   . THR B 311 ? 0.2336 0.1841 0.2280 -0.0041 -0.0284 0.0264  323 THR B O   
4941 C CB  . THR B 311 ? 0.2184 0.1660 0.2105 0.0028  -0.0273 0.0200  323 THR B CB  
4942 O OG1 . THR B 311 ? 0.2044 0.1454 0.1962 0.0034  -0.0289 0.0207  323 THR B OG1 
4943 C CG2 . THR B 311 ? 0.2306 0.1780 0.2221 0.0044  -0.0265 0.0167  323 THR B CG2 
4944 N N   . ALA B 312 ? 0.2515 0.2094 0.2447 -0.0021 -0.0267 0.0265  324 ALA B N   
4945 C CA  . ALA B 312 ? 0.2463 0.2059 0.2394 -0.0030 -0.0273 0.0306  324 ALA B CA  
4946 C C   . ALA B 312 ? 0.2138 0.1744 0.2067 0.0000  -0.0275 0.0321  324 ALA B C   
4947 O O   . ALA B 312 ? 0.2245 0.1887 0.2173 0.0008  -0.0266 0.0303  324 ALA B O   
4948 C CB  . ALA B 312 ? 0.1930 0.1596 0.1857 -0.0066 -0.0264 0.0315  324 ALA B CB  
4949 N N   . CYS B 313 ? 0.2135 0.1708 0.2065 0.0016  -0.0286 0.0356  325 CYS B N   
4950 C CA  . CYS B 313 ? 0.2633 0.2225 0.2568 0.0046  -0.0288 0.0379  325 CYS B CA  
4951 C C   . CYS B 313 ? 0.2872 0.2487 0.2809 0.0039  -0.0298 0.0429  325 CYS B C   
4952 O O   . CYS B 313 ? 0.2809 0.2376 0.2744 0.0031  -0.0303 0.0451  325 CYS B O   
4953 C CB  . CYS B 313 ? 0.2546 0.2065 0.2484 0.0088  -0.0289 0.0372  325 CYS B CB  
4954 S SG  . CYS B 313 ? 0.2946 0.2439 0.2876 0.0103  -0.0278 0.0317  325 CYS B SG  
4955 N N   . ALA B 314 ? 0.2848 0.2537 0.2788 0.0042  -0.0300 0.0450  326 ALA B N   
4956 C CA  . ALA B 314 ? 0.3332 0.3049 0.3272 0.0043  -0.0311 0.0504  326 ALA B CA  
4957 C C   . ALA B 314 ? 0.3394 0.3063 0.3350 0.0091  -0.0316 0.0533  326 ALA B C   
4958 O O   . ALA B 314 ? 0.3120 0.2784 0.3090 0.0123  -0.0311 0.0517  326 ALA B O   
4959 C CB  . ALA B 314 ? 0.2959 0.2783 0.2895 0.0026  -0.0315 0.0514  326 ALA B CB  
4960 N N   . SER B 315 ? 0.3659 0.3291 0.3615 0.0096  -0.0323 0.0578  327 SER B N   
4961 C CA  . SER B 315 ? 0.3915 0.3499 0.3886 0.0143  -0.0326 0.0613  327 SER B CA  
4962 C C   . SER B 315 ? 0.4339 0.4006 0.4321 0.0156  -0.0337 0.0666  327 SER B C   
4963 O O   . SER B 315 ? 0.4116 0.3868 0.4086 0.0124  -0.0344 0.0679  327 SER B O   
4964 C CB  . SER B 315 ? 0.4221 0.3701 0.4185 0.0143  -0.0324 0.0632  327 SER B CB  
4965 O OG  . SER B 315 ? 0.4483 0.3987 0.4440 0.0127  -0.0331 0.0685  327 SER B OG  
4966 N N   . ASP B 316 ? 0.4146 0.3790 0.4150 0.0206  -0.0337 0.0697  328 ASP B N   
4967 C CA  . ASP B 316 ? 0.4837 0.4562 0.4859 0.0228  -0.0349 0.0752  328 ASP B CA  
4968 C C   . ASP B 316 ? 0.4964 0.4682 0.4972 0.0218  -0.0359 0.0811  328 ASP B C   
4969 O O   . ASP B 316 ? 0.5365 0.5162 0.5382 0.0231  -0.0372 0.0862  328 ASP B O   
4970 C CB  . ASP B 316 ? 0.4946 0.4647 0.5002 0.0289  -0.0343 0.0769  328 ASP B CB  
4971 C CG  . ASP B 316 ? 0.4860 0.4620 0.4936 0.0300  -0.0337 0.0730  328 ASP B CG  
4972 O OD1 . ASP B 316 ? 0.5053 0.4914 0.5128 0.0267  -0.0345 0.0715  328 ASP B OD1 
4973 O OD2 . ASP B 316 ? 0.5103 0.4807 0.5196 0.0342  -0.0323 0.0715  328 ASP B OD2 
4974 N N   . GLU B 317 ? 0.5179 0.4809 0.5167 0.0197  -0.0352 0.0808  329 GLU B N   
4975 C CA  . GLU B 317 ? 0.6072 0.5684 0.6047 0.0187  -0.0357 0.0865  329 GLU B CA  
4976 C C   . GLU B 317 ? 0.6187 0.5826 0.6131 0.0127  -0.0357 0.0852  329 GLU B C   
4977 O O   . GLU B 317 ? 0.6214 0.5788 0.6145 0.0107  -0.0351 0.0871  329 GLU B O   
4978 C CB  . GLU B 317 ? 0.6092 0.5568 0.6072 0.0216  -0.0345 0.0884  329 GLU B CB  
4979 C CG  . GLU B 317 ? 0.6891 0.6348 0.6899 0.0279  -0.0345 0.0930  329 GLU B CG  
4980 C CD  . GLU B 317 ? 0.7753 0.7239 0.7760 0.0291  -0.0354 0.1011  329 GLU B CD  
4981 O OE1 . GLU B 317 ? 0.7833 0.7360 0.7860 0.0338  -0.0356 0.1043  329 GLU B OE1 
4982 O OE2 . GLU B 317 ? 0.7955 0.7426 0.7936 0.0253  -0.0355 0.1033  329 GLU B OE2 
4983 N N   . GLY B 318 ? 0.5395 0.5127 0.5329 0.0096  -0.0360 0.0817  330 GLY B N   
4984 C CA  . GLY B 318 ? 0.5265 0.5041 0.5169 0.0042  -0.0358 0.0808  330 GLY B CA  
4985 C C   . GLY B 318 ? 0.5124 0.4826 0.5021 0.0011  -0.0344 0.0770  330 GLY B C   
4986 O O   . GLY B 318 ? 0.5054 0.4751 0.4933 -0.0022 -0.0340 0.0791  330 GLY B O   
4987 N N   . GLU B 319 ? 0.4396 0.4045 0.4308 0.0019  -0.0337 0.0717  331 GLU B N   
4988 C CA  . GLU B 319 ? 0.4117 0.3710 0.4026 -0.0011 -0.0326 0.0678  331 GLU B CA  
4989 C C   . GLU B 319 ? 0.3779 0.3400 0.3692 -0.0018 -0.0321 0.0614  331 GLU B C   
4990 O O   . GLU B 319 ? 0.3701 0.3361 0.3621 0.0005  -0.0323 0.0599  331 GLU B O   
4991 C CB  . GLU B 319 ? 0.4177 0.3650 0.4099 0.0007  -0.0324 0.0681  331 GLU B CB  
4992 C CG  . GLU B 319 ? 0.4630 0.4054 0.4547 0.0001  -0.0323 0.0739  331 GLU B CG  
4993 C CD  . GLU B 319 ? 0.4672 0.3968 0.4600 0.0018  -0.0319 0.0738  331 GLU B CD  
4994 O OE1 . GLU B 319 ? 0.4779 0.4028 0.4717 0.0048  -0.0319 0.0703  331 GLU B OE1 
4995 O OE2 . GLU B 319 ? 0.4403 0.3643 0.4329 0.0000  -0.0314 0.0771  331 GLU B OE2 
4996 N N   . VAL B 320 ? 0.3647 0.3252 0.3557 -0.0051 -0.0313 0.0580  332 VAL B N   
4997 C CA  . VAL B 320 ? 0.3152 0.2765 0.3068 -0.0055 -0.0306 0.0521  332 VAL B CA  
4998 C C   . VAL B 320 ? 0.3048 0.2572 0.2975 -0.0053 -0.0305 0.0496  332 VAL B C   
4999 O O   . VAL B 320 ? 0.3062 0.2557 0.2992 -0.0081 -0.0304 0.0504  332 VAL B O   
5000 C CB  . VAL B 320 ? 0.2756 0.2443 0.2660 -0.0094 -0.0295 0.0500  332 VAL B CB  
5001 C CG1 . VAL B 320 ? 0.2736 0.2423 0.2647 -0.0093 -0.0286 0.0443  332 VAL B CG1 
5002 C CG2 . VAL B 320 ? 0.3118 0.2894 0.3005 -0.0100 -0.0298 0.0521  332 VAL B CG2 
5003 N N   . ILE B 321 ? 0.2898 0.2381 0.2830 -0.0022 -0.0307 0.0466  333 ILE B N   
5004 C CA  . ILE B 321 ? 0.3068 0.2466 0.3005 -0.0018 -0.0309 0.0439  333 ILE B CA  
5005 C C   . ILE B 321 ? 0.2605 0.2029 0.2543 -0.0034 -0.0305 0.0390  333 ILE B C   
5006 O O   . ILE B 321 ? 0.2868 0.2321 0.2803 -0.0015 -0.0300 0.0364  333 ILE B O   
5007 C CB  . ILE B 321 ? 0.3135 0.2467 0.3069 0.0028  -0.0312 0.0436  333 ILE B CB  
5008 C CG1 . ILE B 321 ? 0.3585 0.2898 0.3522 0.0049  -0.0315 0.0490  333 ILE B CG1 
5009 C CG2 . ILE B 321 ? 0.3081 0.2324 0.3012 0.0029  -0.0316 0.0403  333 ILE B CG2 
5010 C CD1 . ILE B 321 ? 0.3606 0.2887 0.3543 0.0021  -0.0316 0.0526  333 ILE B CD1 
5011 N N   . VAL B 322 ? 0.2410 0.1829 0.2358 -0.0068 -0.0305 0.0379  334 VAL B N   
5012 C CA  . VAL B 322 ? 0.2680 0.2121 0.2635 -0.0080 -0.0301 0.0336  334 VAL B CA  
5013 C C   . VAL B 322 ? 0.2454 0.1821 0.2412 -0.0072 -0.0313 0.0310  334 VAL B C   
5014 O O   . VAL B 322 ? 0.2660 0.1970 0.2623 -0.0085 -0.0321 0.0323  334 VAL B O   
5015 C CB  . VAL B 322 ? 0.2690 0.2186 0.2656 -0.0122 -0.0293 0.0340  334 VAL B CB  
5016 C CG1 . VAL B 322 ? 0.2616 0.2119 0.2598 -0.0132 -0.0292 0.0301  334 VAL B CG1 
5017 C CG2 . VAL B 322 ? 0.2852 0.2428 0.2807 -0.0129 -0.0279 0.0351  334 VAL B CG2 
5018 N N   . PHE B 323 ? 0.2160 0.1526 0.2112 -0.0052 -0.0313 0.0273  335 PHE B N   
5019 C CA  . PHE B 323 ? 0.3049 0.2351 0.2997 -0.0045 -0.0326 0.0243  335 PHE B CA  
5020 C C   . PHE B 323 ? 0.2758 0.2095 0.2713 -0.0050 -0.0327 0.0208  335 PHE B C   
5021 O O   . PHE B 323 ? 0.2607 0.1994 0.2559 -0.0037 -0.0315 0.0197  335 PHE B O   
5022 C CB  . PHE B 323 ? 0.2745 0.1987 0.2669 -0.0003 -0.0329 0.0235  335 PHE B CB  
5023 C CG  . PHE B 323 ? 0.2533 0.1712 0.2444 0.0004  -0.0342 0.0201  335 PHE B CG  
5024 C CD1 . PHE B 323 ? 0.2892 0.2009 0.2806 -0.0018 -0.0355 0.0201  335 PHE B CD1 
5025 C CD2 . PHE B 323 ? 0.2852 0.2035 0.2746 0.0028  -0.0342 0.0169  335 PHE B CD2 
5026 C CE1 . PHE B 323 ? 0.3305 0.2367 0.3204 -0.0016 -0.0370 0.0166  335 PHE B CE1 
5027 C CE2 . PHE B 323 ? 0.2955 0.2084 0.2831 0.0033  -0.0356 0.0137  335 PHE B CE2 
5028 C CZ  . PHE B 323 ? 0.2947 0.2017 0.2824 0.0010  -0.0371 0.0134  335 PHE B CZ  
5029 N N   . GLY B 324 ? 0.2802 0.2110 0.2766 -0.0067 -0.0342 0.0190  336 GLY B N   
5030 C CA  . GLY B 324 ? 0.2694 0.2030 0.2665 -0.0066 -0.0347 0.0157  336 GLY B CA  
5031 C C   . GLY B 324 ? 0.2878 0.2296 0.2877 -0.0087 -0.0334 0.0160  336 GLY B C   
5032 O O   . GLY B 324 ? 0.2326 0.1776 0.2343 -0.0115 -0.0325 0.0184  336 GLY B O   
5033 N N   . GLY B 325 ? 0.2484 0.1935 0.2484 -0.0072 -0.0330 0.0137  337 GLY B N   
5034 C CA  . GLY B 325 ? 0.2213 0.1736 0.2241 -0.0087 -0.0315 0.0135  337 GLY B CA  
5035 C C   . GLY B 325 ? 0.2528 0.2070 0.2591 -0.0114 -0.0329 0.0128  337 GLY B C   
5036 O O   . GLY B 325 ? 0.2705 0.2204 0.2770 -0.0127 -0.0352 0.0124  337 GLY B O   
5037 N N   . CYS B 326 ? 0.2167 0.1776 0.2260 -0.0125 -0.0314 0.0127  338 CYS B N   
5038 C CA  . CYS B 326 ? 0.2489 0.2134 0.2624 -0.0146 -0.0325 0.0120  338 CYS B CA  
5039 C C   . CYS B 326 ? 0.2401 0.2092 0.2570 -0.0184 -0.0308 0.0141  338 CYS B C   
5040 O O   . CYS B 326 ? 0.2315 0.2035 0.2476 -0.0186 -0.0282 0.0154  338 CYS B O   
5041 C CB  . CYS B 326 ? 0.1623 0.1310 0.1769 -0.0120 -0.0318 0.0101  338 CYS B CB  
5042 S SG  . CYS B 326 ? 0.2237 0.1980 0.2441 -0.0139 -0.0337 0.0092  338 CYS B SG  
5043 N N   . ALA B 327 ? 0.2295 0.1996 0.2501 -0.0217 -0.0323 0.0146  339 ALA B N   
5044 C CA  . ALA B 327 ? 0.2200 0.1943 0.2439 -0.0255 -0.0306 0.0168  339 ALA B CA  
5045 C C   . ALA B 327 ? 0.2328 0.2156 0.2612 -0.0260 -0.0286 0.0164  339 ALA B C   
5046 O O   . ALA B 327 ? 0.2508 0.2379 0.2816 -0.0288 -0.0264 0.0183  339 ALA B O   
5047 C CB  . ALA B 327 ? 0.2545 0.2257 0.2808 -0.0292 -0.0328 0.0178  339 ALA B CB  
5048 N N   . ASN B 328 ? 0.2142 0.1997 0.2439 -0.0233 -0.0291 0.0142  340 ASN B N   
5049 C CA  . ASN B 328 ? 0.1942 0.1877 0.2287 -0.0232 -0.0271 0.0140  340 ASN B CA  
5050 C C   . ASN B 328 ? 0.2137 0.2080 0.2462 -0.0187 -0.0256 0.0123  340 ASN B C   
5051 O O   . ASN B 328 ? 0.2126 0.2020 0.2399 -0.0164 -0.0253 0.0117  340 ASN B O   
5052 C CB  . ASN B 328 ? 0.2102 0.2077 0.2507 -0.0255 -0.0295 0.0137  340 ASN B CB  
5053 C CG  . ASN B 328 ? 0.2352 0.2296 0.2747 -0.0235 -0.0334 0.0116  340 ASN B CG  
5054 O OD1 . ASN B 328 ? 0.2179 0.2072 0.2522 -0.0202 -0.0340 0.0104  340 ASN B OD1 
5055 N ND2 . ASN B 328 ? 0.2275 0.2254 0.2718 -0.0258 -0.0361 0.0111  340 ASN B ND2 
5056 N N   . ASN B 329 ? 0.1607 0.1612 0.1975 -0.0175 -0.0243 0.0117  341 ASN B N   
5057 C CA  . ASN B 329 ? 0.1692 0.1703 0.2045 -0.0133 -0.0224 0.0104  341 ASN B CA  
5058 C C   . ASN B 329 ? 0.1962 0.1934 0.2293 -0.0103 -0.0258 0.0091  341 ASN B C   
5059 O O   . ASN B 329 ? 0.2409 0.2413 0.2774 -0.0097 -0.0281 0.0086  341 ASN B O   
5060 C CB  . ASN B 329 ? 0.1872 0.1958 0.2281 -0.0125 -0.0199 0.0105  341 ASN B CB  
5061 C CG  . ASN B 329 ? 0.2101 0.2188 0.2498 -0.0079 -0.0176 0.0093  341 ASN B CG  
5062 O OD1 . ASN B 329 ? 0.2642 0.2673 0.2987 -0.0055 -0.0178 0.0084  341 ASN B OD1 
5063 N ND2 . ASN B 329 ? 0.1744 0.1893 0.2191 -0.0066 -0.0152 0.0095  341 ASN B ND2 
5064 N N   . LEU B 330 ? 0.1650 0.1557 0.1922 -0.0085 -0.0260 0.0085  342 LEU B N   
5065 C CA  . LEU B 330 ? 0.1875 0.1740 0.2117 -0.0058 -0.0289 0.0072  342 LEU B CA  
5066 C C   . LEU B 330 ? 0.1990 0.1881 0.2239 -0.0018 -0.0282 0.0064  342 LEU B C   
5067 O O   . LEU B 330 ? 0.1847 0.1714 0.2074 0.0006  -0.0308 0.0055  342 LEU B O   
5068 C CB  . LEU B 330 ? 0.1772 0.1567 0.1953 -0.0046 -0.0287 0.0069  342 LEU B CB  
5069 C CG  . LEU B 330 ? 0.1995 0.1785 0.2151 -0.0033 -0.0249 0.0071  342 LEU B CG  
5070 C CD1 . LEU B 330 ? 0.2380 0.2166 0.2521 0.0007  -0.0234 0.0060  342 LEU B CD1 
5071 C CD2 . LEU B 330 ? 0.2663 0.2402 0.2778 -0.0040 -0.0252 0.0077  342 LEU B CD2 
5072 N N   . LEU B 331 ? 0.1938 0.1873 0.2214 -0.0007 -0.0246 0.0068  343 LEU B N   
5073 C CA  . LEU B 331 ? 0.2243 0.2203 0.2532 0.0033  -0.0237 0.0065  343 LEU B CA  
5074 C C   . LEU B 331 ? 0.2214 0.2232 0.2555 0.0033  -0.0268 0.0068  343 LEU B C   
5075 O O   . LEU B 331 ? 0.2369 0.2405 0.2717 0.0069  -0.0274 0.0068  343 LEU B O   
5076 C CB  . LEU B 331 ? 0.2210 0.2197 0.2517 0.0043  -0.0187 0.0067  343 LEU B CB  
5077 C CG  . LEU B 331 ? 0.2305 0.2247 0.2565 0.0035  -0.0157 0.0062  343 LEU B CG  
5078 C CD1 . LEU B 331 ? 0.2689 0.2665 0.2970 0.0030  -0.0109 0.0061  343 LEU B CD1 
5079 C CD2 . LEU B 331 ? 0.2332 0.2218 0.2543 0.0068  -0.0154 0.0054  343 LEU B CD2 
5080 N N   . VAL B 332 ? 0.2159 0.2211 0.2540 -0.0008 -0.0288 0.0073  344 VAL B N   
5081 C CA  . VAL B 332 ? 0.2386 0.2492 0.2815 -0.0016 -0.0325 0.0074  344 VAL B CA  
5082 C C   . VAL B 332 ? 0.2513 0.2561 0.2896 -0.0025 -0.0370 0.0061  344 VAL B C   
5083 O O   . VAL B 332 ? 0.2469 0.2500 0.2857 -0.0066 -0.0391 0.0059  344 VAL B O   
5084 C CB  . VAL B 332 ? 0.2227 0.2400 0.2725 -0.0057 -0.0320 0.0084  344 VAL B CB  
5085 C CG1 . VAL B 332 ? 0.2499 0.2751 0.3061 -0.0060 -0.0353 0.0087  344 VAL B CG1 
5086 C CG2 . VAL B 332 ? 0.2530 0.2736 0.3051 -0.0051 -0.0267 0.0094  344 VAL B CG2 
5087 N N   . HIS B 333 ? 0.2098 0.2811 0.3044 0.0584  0.0047  0.0067  345 HIS B N   
5088 C CA  . HIS B 333 ? 0.2072 0.2721 0.2965 0.0506  0.0003  0.0037  345 HIS B CA  
5089 C C   . HIS B 333 ? 0.2023 0.2943 0.3004 0.0420  -0.0061 -0.0041 345 HIS B C   
5090 O O   . HIS B 333 ? 0.2505 0.3359 0.3477 0.0295  -0.0082 -0.0094 345 HIS B O   
5091 C CB  . HIS B 333 ? 0.2285 0.2851 0.3067 0.0623  -0.0004 0.0102  345 HIS B CB  
5092 C CG  . HIS B 333 ? 0.2825 0.3324 0.3546 0.0555  -0.0050 0.0077  345 HIS B CG  
5093 N ND1 . HIS B 333 ? 0.2542 0.2774 0.3195 0.0462  -0.0032 0.0067  345 HIS B ND1 
5094 C CD2 . HIS B 333 ? 0.2718 0.3387 0.3432 0.0573  -0.0113 0.0061  345 HIS B CD2 
5095 C CE1 . HIS B 333 ? 0.2897 0.3132 0.3505 0.0424  -0.0081 0.0047  345 HIS B CE1 
5096 N NE2 . HIS B 333 ? 0.2857 0.3351 0.3501 0.0488  -0.0130 0.0042  345 HIS B NE2 
5097 N N   . HIS B 334 ? 0.2039 0.3265 0.3103 0.0483  -0.0086 -0.0052 346 HIS B N   
5098 C CA  . HIS B 334 ? 0.2304 0.3814 0.3453 0.0401  -0.0143 -0.0134 346 HIS B CA  
5099 C C   . HIS B 334 ? 0.2259 0.3801 0.3501 0.0249  -0.0128 -0.0214 346 HIS B C   
5100 O O   . HIS B 334 ? 0.2283 0.4020 0.3588 0.0152  -0.0165 -0.0294 346 HIS B O   
5101 C CB  . HIS B 334 ? 0.2046 0.3899 0.3250 0.0524  -0.0176 -0.0121 346 HIS B CB  
5102 C CG  . HIS B 334 ? 0.2378 0.4356 0.3663 0.0580  -0.0141 -0.0108 346 HIS B CG  
5103 N ND1 . HIS B 334 ? 0.2433 0.4219 0.3675 0.0677  -0.0081 -0.0030 346 HIS B ND1 
5104 C CD2 . HIS B 334 ? 0.2024 0.4300 0.3429 0.0551  -0.0157 -0.0164 346 HIS B CD2 
5105 C CE1 . HIS B 334 ? 0.2504 0.4462 0.3835 0.0709  -0.0062 -0.0036 346 HIS B CE1 
5106 N NE2 . HIS B 334 ? 0.2047 0.4308 0.3478 0.0636  -0.0109 -0.0116 346 HIS B NE2 
5107 N N   . ARG B 335 ? 0.1930 0.3290 0.3180 0.0225  -0.0072 -0.0197 347 ARG B N   
5108 C CA  . ARG B 335 ? 0.2150 0.3496 0.3474 0.0082  -0.0049 -0.0265 347 ARG B CA  
5109 C C   . ARG B 335 ? 0.1976 0.2996 0.3228 -0.0011 -0.0014 -0.0264 347 ARG B C   
5110 O O   . ARG B 335 ? 0.2201 0.3171 0.3498 -0.0127 0.0014  -0.0313 347 ARG B O   
5111 C CB  . ARG B 335 ? 0.2288 0.3721 0.3695 0.0121  -0.0011 -0.0255 347 ARG B CB  
5112 C CG  . ARG B 335 ? 0.2721 0.4466 0.4191 0.0244  -0.0036 -0.0239 347 ARG B CG  
5113 C CD  . ARG B 335 ? 0.2621 0.4534 0.4207 0.0225  -0.0012 -0.0270 347 ARG B CD  
5114 N NE  . ARG B 335 ? 0.2970 0.4661 0.4543 0.0246  0.0051  -0.0224 347 ARG B NE  
5115 C CZ  . ARG B 335 ? 0.3226 0.4929 0.4798 0.0378  0.0083  -0.0158 347 ARG B CZ  
5116 N NH1 . ARG B 335 ? 0.2781 0.4710 0.4364 0.0512  0.0059  -0.0123 347 ARG B NH1 
5117 N NH2 . ARG B 335 ? 0.3219 0.4705 0.4777 0.0377  0.0144  -0.0126 347 ARG B NH2 
5118 N N   . ALA B 336 ? 0.1970 0.2774 0.3109 0.0036  -0.0011 -0.0210 348 ALA B N   
5119 C CA  . ALA B 336 ? 0.2063 0.2564 0.3131 -0.0032 0.0029  -0.0199 348 ALA B CA  
5120 C C   . ALA B 336 ? 0.2245 0.2717 0.3325 -0.0184 0.0020  -0.0270 348 ALA B C   
5121 O O   . ALA B 336 ? 0.2307 0.2918 0.3400 -0.0228 -0.0024 -0.0316 348 ALA B O   
5122 C CB  . ALA B 336 ? 0.1995 0.2297 0.2938 0.0042  0.0028  -0.0137 348 ALA B CB  
5123 N N   . ALA B 337 ? 0.1750 0.2042 0.2822 -0.0263 0.0068  -0.0281 349 ALA B N   
5124 C CA  . ALA B 337 ? 0.2045 0.2271 0.3116 -0.0400 0.0077  -0.0339 349 ALA B CA  
5125 C C   . ALA B 337 ? 0.2356 0.2300 0.3310 -0.0420 0.0097  -0.0307 349 ALA B C   
5126 O O   . ALA B 337 ? 0.2511 0.2289 0.3445 -0.0457 0.0145  -0.0297 349 ALA B O   
5127 C CB  . ALA B 337 ? 0.2250 0.2515 0.3407 -0.0476 0.0119  -0.0380 349 ALA B CB  
5128 N N   . HIS B 338 ? 0.2824 0.2730 0.3702 -0.0399 0.0058  -0.0293 350 HIS B N   
5129 C CA  . HIS B 338 ? 0.2574 0.2234 0.3341 -0.0419 0.0072  -0.0266 350 HIS B CA  
5130 C C   . HIS B 338 ? 0.2905 0.2495 0.3661 -0.0547 0.0088  -0.0318 350 HIS B C   
5131 O O   . HIS B 338 ? 0.2985 0.2722 0.3802 -0.0618 0.0074  -0.0378 350 HIS B O   
5132 C CB  . HIS B 338 ? 0.2398 0.2041 0.3087 -0.0348 0.0027  -0.0233 350 HIS B CB  
5133 C CG  . HIS B 338 ? 0.2449 0.2135 0.3133 -0.0215 0.0024  -0.0176 350 HIS B CG  
5134 N ND1 . HIS B 338 ? 0.2734 0.2241 0.3362 -0.0156 0.0068  -0.0122 350 HIS B ND1 
5135 C CD2 . HIS B 338 ? 0.2199 0.2088 0.2926 -0.0128 -0.0010 -0.0164 350 HIS B CD2 
5136 C CE1 . HIS B 338 ? 0.2466 0.2044 0.3096 -0.0038 0.0066  -0.0078 350 HIS B CE1 
5137 N NE2 . HIS B 338 ? 0.2625 0.2438 0.3314 -0.0014 0.0017  -0.0099 350 HIS B NE2 
5138 N N   . SER B 339 ? 0.2985 0.2349 0.3658 -0.0575 0.0122  -0.0296 351 SER B N   
5139 C CA  . SER B 339 ? 0.3052 0.2368 0.3648 -0.0638 0.0131  -0.0301 351 SER B CA  
5140 C C   . SER B 339 ? 0.2721 0.1935 0.3160 -0.0609 0.0091  -0.0254 351 SER B C   
5141 O O   . SER B 339 ? 0.2609 0.1734 0.2984 -0.0556 0.0076  -0.0218 351 SER B O   
5142 C CB  . SER B 339 ? 0.2244 0.1520 0.2792 -0.0605 0.0160  -0.0260 351 SER B CB  
5143 O OG  . SER B 339 ? 0.3092 0.2368 0.3565 -0.0622 0.0150  -0.0246 351 SER B OG  
5144 N N   . ASN B 340 ? 0.3211 0.2446 0.3605 -0.0638 0.0074  -0.0255 352 ASN B N   
5145 C CA  . ASN B 340 ? 0.3044 0.2210 0.3333 -0.0595 0.0037  -0.0205 352 ASN B CA  
5146 C C   . ASN B 340 ? 0.3472 0.2640 0.3734 -0.0578 0.0049  -0.0179 352 ASN B C   
5147 O O   . ASN B 340 ? 0.3498 0.2643 0.3716 -0.0570 0.0067  -0.0177 352 ASN B O   
5148 C CB  . ASN B 340 ? 0.4112 0.3297 0.4400 -0.0628 0.0010  -0.0232 352 ASN B CB  
5149 C CG  . ASN B 340 ? 0.3784 0.3046 0.4114 -0.0691 0.0028  -0.0278 352 ASN B CG  
5150 O OD1 . ASN B 340 ? 0.4046 0.3362 0.4427 -0.0722 0.0062  -0.0302 352 ASN B OD1 
5151 N ND2 . ASN B 340 ? 0.4420 0.3691 0.4731 -0.0711 0.0008  -0.0295 352 ASN B ND2 
5152 N N   . GLU B 341 ? 0.3223 0.2416 0.3517 -0.0585 0.0085  -0.0186 353 GLU B N   
5153 C CA  . GLU B 341 ? 0.3208 0.2394 0.3478 -0.0580 0.0138  -0.0186 353 GLU B CA  
5154 C C   . GLU B 341 ? 0.3613 0.2750 0.3816 -0.0525 0.0160  -0.0156 353 GLU B C   
5155 O O   . GLU B 341 ? 0.3374 0.2494 0.3567 -0.0488 0.0142  -0.0133 353 GLU B O   
5156 C CB  . GLU B 341 ? 0.3747 0.2978 0.4076 -0.0602 0.0165  -0.0202 353 GLU B CB  
5157 C CG  . GLU B 341 ? 0.4006 0.3314 0.4418 -0.0670 0.0169  -0.0253 353 GLU B CG  
5158 C CD  . GLU B 341 ? 0.4823 0.4181 0.5294 -0.0695 0.0212  -0.0276 353 GLU B CD  
5159 O OE1 . GLU B 341 ? 0.5357 0.4681 0.5785 -0.0675 0.0241  -0.0260 353 GLU B OE1 
5160 O OE2 . GLU B 341 ? 0.5291 0.4734 0.5866 -0.0735 0.0230  -0.0322 353 GLU B OE2 
5161 N N   . ILE B 342 ? 0.3549 0.2667 0.3701 -0.0521 0.0203  -0.0158 354 ILE B N   
5162 C CA  . ILE B 342 ? 0.3745 0.2840 0.3838 -0.0479 0.0236  -0.0139 354 ILE B CA  
5163 C C   . ILE B 342 ? 0.3566 0.2678 0.3680 -0.0482 0.0284  -0.0148 354 ILE B C   
5164 O O   . ILE B 342 ? 0.3310 0.2431 0.3443 -0.0517 0.0312  -0.0171 354 ILE B O   
5165 C CB  . ILE B 342 ? 0.3493 0.2558 0.3510 -0.0473 0.0258  -0.0136 354 ILE B CB  
5166 C CG1 . ILE B 342 ? 0.3292 0.2344 0.3287 -0.0458 0.0213  -0.0123 354 ILE B CG1 
5167 C CG2 . ILE B 342 ? 0.3382 0.2437 0.3341 -0.0442 0.0304  -0.0126 354 ILE B CG2 
5168 C CD1 . ILE B 342 ? 0.3533 0.2582 0.3505 -0.0414 0.0200  -0.0099 354 ILE B CD1 
5169 N N   . LEU B 343 ? 0.3435 0.2552 0.3546 -0.0449 0.0295  -0.0134 355 LEU B N   
5170 C CA  . LEU B 343 ? 0.3017 0.2150 0.3143 -0.0445 0.0342  -0.0141 355 LEU B CA  
5171 C C   . LEU B 343 ? 0.3331 0.2451 0.3388 -0.0410 0.0377  -0.0130 355 LEU B C   
5172 O O   . LEU B 343 ? 0.3455 0.2571 0.3481 -0.0382 0.0361  -0.0115 355 LEU B O   
5173 C CB  . LEU B 343 ? 0.3497 0.2656 0.3686 -0.0438 0.0330  -0.0138 355 LEU B CB  
5174 C CG  . LEU B 343 ? 0.3405 0.2594 0.3671 -0.0477 0.0317  -0.0156 355 LEU B CG  
5175 C CD1 . LEU B 343 ? 0.3906 0.3099 0.4187 -0.0514 0.0278  -0.0168 355 LEU B CD1 
5176 C CD2 . LEU B 343 ? 0.3468 0.2676 0.3785 -0.0462 0.0303  -0.0148 355 LEU B CD2 
5177 N N   . ILE B 344 ? 0.3446 0.2558 0.3475 -0.0414 0.0426  -0.0140 356 ILE B N   
5178 C CA  . ILE B 344 ? 0.3703 0.2802 0.3659 -0.0386 0.0461  -0.0134 356 ILE B CA  
5179 C C   . ILE B 344 ? 0.3509 0.2627 0.3482 -0.0372 0.0503  -0.0140 356 ILE B C   
5180 O O   . ILE B 344 ? 0.3930 0.3048 0.3930 -0.0389 0.0534  -0.0154 356 ILE B O   
5181 C CB  . ILE B 344 ? 0.3946 0.3009 0.3837 -0.0397 0.0488  -0.0140 356 ILE B CB  
5182 C CG1 . ILE B 344 ? 0.3786 0.2833 0.3657 -0.0407 0.0447  -0.0133 356 ILE B CG1 
5183 C CG2 . ILE B 344 ? 0.3562 0.2612 0.3377 -0.0367 0.0529  -0.0135 356 ILE B CG2 
5184 C CD1 . ILE B 344 ? 0.4066 0.3074 0.3882 -0.0424 0.0474  -0.0142 356 ILE B CD1 
5185 N N   . PHE B 345 ? 0.3397 0.2531 0.3353 -0.0344 0.0506  -0.0132 357 PHE B N   
5186 C CA  . PHE B 345 ? 0.3087 0.2241 0.3053 -0.0328 0.0546  -0.0138 357 PHE B CA  
5187 C C   . PHE B 345 ? 0.3988 0.3128 0.3873 -0.0308 0.0582  -0.0139 357 PHE B C   
5188 O O   . PHE B 345 ? 0.3609 0.2744 0.3438 -0.0294 0.0569  -0.0131 357 PHE B O   
5189 C CB  . PHE B 345 ? 0.3061 0.2242 0.3065 -0.0313 0.0531  -0.0134 357 PHE B CB  
5190 C CG  . PHE B 345 ? 0.3301 0.2491 0.3381 -0.0329 0.0497  -0.0132 357 PHE B CG  
5191 C CD1 . PHE B 345 ? 0.3298 0.2475 0.3382 -0.0335 0.0449  -0.0122 357 PHE B CD1 
5192 C CD2 . PHE B 345 ? 0.3371 0.2582 0.3517 -0.0338 0.0512  -0.0142 357 PHE B CD2 
5193 C CE1 . PHE B 345 ? 0.3167 0.2351 0.3318 -0.0349 0.0418  -0.0121 357 PHE B CE1 
5194 C CE2 . PHE B 345 ? 0.3268 0.2489 0.3482 -0.0353 0.0482  -0.0142 357 PHE B CE2 
5195 C CZ  . PHE B 345 ? 0.2825 0.2032 0.3040 -0.0359 0.0435  -0.0131 357 PHE B CZ  
5196 N N   . SER B 346 ? 0.4504 0.3636 0.4378 -0.0305 0.0628  -0.0149 358 SER B N   
5197 C CA  . SER B 346 ? 0.4614 0.3730 0.4412 -0.0282 0.0666  -0.0152 358 SER B CA  
5198 C C   . SER B 346 ? 0.5134 0.4281 0.4946 -0.0262 0.0688  -0.0159 358 SER B C   
5199 O O   . SER B 346 ? 0.5425 0.4578 0.5270 -0.0261 0.0719  -0.0169 358 SER B O   
5200 C CB  . SER B 346 ? 0.5209 0.4286 0.4978 -0.0287 0.0709  -0.0160 358 SER B CB  
5201 O OG  . SER B 346 ? 0.5325 0.4375 0.5008 -0.0263 0.0738  -0.0160 358 SER B OG  
5202 N N   . VAL B 347 ? 0.5192 0.4356 0.4977 -0.0249 0.0674  -0.0157 359 VAL B N   
5203 C CA  . VAL B 347 ? 0.5424 0.4616 0.5222 -0.0235 0.0694  -0.0168 359 VAL B CA  
5204 C C   . VAL B 347 ? 0.6412 0.5597 0.6145 -0.0214 0.0723  -0.0179 359 VAL B C   
5205 O O   . VAL B 347 ? 0.6746 0.5962 0.6506 -0.0205 0.0713  -0.0179 359 VAL B O   
5206 C CB  . VAL B 347 ? 0.4566 0.3779 0.4376 -0.0235 0.0665  -0.0164 359 VAL B CB  
5207 C CG1 . VAL B 347 ? 0.4613 0.3853 0.4453 -0.0226 0.0689  -0.0178 359 VAL B CG1 
5208 C CG2 . VAL B 347 ? 0.4137 0.3348 0.4006 -0.0252 0.0623  -0.0150 359 VAL B CG2 
5209 N N   . GLN B 348 ? 0.6677 0.5838 0.6349 -0.0207 0.0711  -0.0168 360 GLN B N   
5210 C CA  . GLN B 348 ? 0.7232 0.6401 0.6877 -0.0187 0.0689  -0.0156 360 GLN B CA  
5211 C C   . GLN B 348 ? 0.7483 0.6612 0.7115 -0.0183 0.0719  -0.0153 360 GLN B C   
5212 O O   . GLN B 348 ? 0.7608 0.6697 0.7204 -0.0188 0.0733  -0.0152 360 GLN B O   
5213 C CB  . GLN B 348 ? 0.7771 0.6948 0.7365 -0.0178 0.0649  -0.0145 360 GLN B CB  
5214 C CG  . GLN B 348 ? 0.7749 0.6966 0.7353 -0.0181 0.0620  -0.0147 360 GLN B CG  
5215 C CD  . GLN B 348 ? 0.8271 0.7526 0.7906 -0.0174 0.0607  -0.0152 360 GLN B CD  
5216 O OE1 . GLN B 348 ? 0.8062 0.7318 0.7691 -0.0161 0.0600  -0.0148 360 GLN B OE1 
5217 N NE2 . GLN B 348 ? 0.7522 0.6801 0.7188 -0.0182 0.0608  -0.0160 360 GLN B NE2 
# 
