data_8PS7
# 
_entry.id   8PS7 
# 
_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   8PS7         pdb_00008ps7 10.2210/pdb8ps7/pdb 
WWPDB D_1292131388 ?            ?                   
# 
_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                        8PS7 
_pdbx_database_status.recvd_initial_deposition_date   2023-07-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              kra@mbg.au.dk 
_pdbx_contact_author.name_first         Kasper 
_pdbx_contact_author.name_last          Andersen 
_pdbx_contact_author.name_mi            R 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4415-8067 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Simonsen, B.'   1 0000-0002-9197-9992 
'Gysel, K.'      2 0000-0003-4245-9998 
'Laursen, M.'    3 0000-0002-6265-2069 
'Andersen, K.R.' 4 0000-0002-4415-8067 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;The Medicago truncatula LYR4 intracellular domain serves as a scaffold in immunity signaling independent of its phosphorylation activity
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2024.10.23.619817 
_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 'Simonsen, B.'    1  ? 
primary 'Rubsam, H.'      2  ? 
primary 'Kolte, M.V.'     3  ? 
primary 'Larsen, M.M.'    4  ? 
primary 'Kronauer, C.'    5  ? 
primary 'Gysel, K.'       6  ? 
primary 'Laursen, M.'     7  ? 
primary 'Feng, F.'        8  ? 
primary 'Kaya, G.'        9  ? 
primary 'Oldroyd, G.E.D.' 10 ? 
primary 'Stougaard, J.'   11 ? 
primary 'Fort, S.'        12 ? 
primary 'Radutoiu, S.'    13 ? 
primary 'Andersen, K.R.'  14 ? 
# 
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 'LysM-domain receptor-like kinase'            33429.762 2   ? ? ? ? 
2 non-polymer syn GLYCEROL                                      92.094    3   ? ? ? ? 
3 non-polymer syn 'SULFATE ION'                                 96.063    2   ? ? ? ? 
4 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' 506.196   2   ? ? ? ? 
5 water       nat water                                         18.015    173 ? ? ? ? 
# 
_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       
;SLTVYKYEDLQNATNFFSEENKIKGSVYRASFKGDDAAVKILKGDVSSEINILKRINHANIIRLSGFCVYKGNTYLVYEF
AENNSLDDWLHSEKNKDKNYSNSMCLSWFQRVQIAHDVADALNYLHNYANPPHVHKNLKSGNILLDGKFRGKVSNFGLAR
VMENEGGDEGFQLTRHVIGTQGYMAPEYIENGLITPKMDVFAFGVVILELLSGREVVGSDKSNGLGDQLLASTVNQVLEG
DNVREKLRGFMDPNLRDEYPLDLAFSMAEIAKRCVARDLNSRPNVSEVFMILSKIQS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SLTVYKYEDLQNATNFFSEENKIKGSVYRASFKGDDAAVKILKGDVSSEINILKRINHANIIRLSGFCVYKGNTYLVYEF
AENNSLDDWLHSEKNKDKNYSNSMCLSWFQRVQIAHDVADALNYLHNYANPPHVHKNLKSGNILLDGKFRGKVSNFGLAR
VMENEGGDEGFQLTRHVIGTQGYMAPEYIENGLITPKMDVFAFGVVILELLSGREVVGSDKSNGLGDQLLASTVNQVLEG
DNVREKLRGFMDPNLRDEYPLDLAFSMAEIAKRCVARDLNSRPNVSEVFMILSKIQS
;
_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 GLYCEROL                                      GOL 
3 'SULFATE ION'                                 SO4 
4 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ANP 
5 water                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   LEU n 
1 3   THR n 
1 4   VAL n 
1 5   TYR n 
1 6   LYS n 
1 7   TYR n 
1 8   GLU n 
1 9   ASP n 
1 10  LEU n 
1 11  GLN n 
1 12  ASN n 
1 13  ALA n 
1 14  THR n 
1 15  ASN n 
1 16  PHE n 
1 17  PHE n 
1 18  SER n 
1 19  GLU n 
1 20  GLU n 
1 21  ASN n 
1 22  LYS n 
1 23  ILE n 
1 24  LYS n 
1 25  GLY n 
1 26  SER n 
1 27  VAL n 
1 28  TYR n 
1 29  ARG n 
1 30  ALA n 
1 31  SER n 
1 32  PHE n 
1 33  LYS n 
1 34  GLY n 
1 35  ASP n 
1 36  ASP n 
1 37  ALA n 
1 38  ALA n 
1 39  VAL n 
1 40  LYS n 
1 41  ILE n 
1 42  LEU n 
1 43  LYS n 
1 44  GLY n 
1 45  ASP n 
1 46  VAL n 
1 47  SER n 
1 48  SER n 
1 49  GLU n 
1 50  ILE n 
1 51  ASN n 
1 52  ILE n 
1 53  LEU n 
1 54  LYS n 
1 55  ARG n 
1 56  ILE n 
1 57  ASN n 
1 58  HIS n 
1 59  ALA n 
1 60  ASN n 
1 61  ILE n 
1 62  ILE n 
1 63  ARG n 
1 64  LEU n 
1 65  SER n 
1 66  GLY n 
1 67  PHE n 
1 68  CYS n 
1 69  VAL n 
1 70  TYR n 
1 71  LYS n 
1 72  GLY n 
1 73  ASN n 
1 74  THR n 
1 75  TYR n 
1 76  LEU n 
1 77  VAL n 
1 78  TYR n 
1 79  GLU n 
1 80  PHE n 
1 81  ALA n 
1 82  GLU n 
1 83  ASN n 
1 84  ASN n 
1 85  SER n 
1 86  LEU n 
1 87  ASP n 
1 88  ASP n 
1 89  TRP n 
1 90  LEU n 
1 91  HIS n 
1 92  SER n 
1 93  GLU n 
1 94  LYS n 
1 95  ASN n 
1 96  LYS n 
1 97  ASP n 
1 98  LYS n 
1 99  ASN n 
1 100 TYR n 
1 101 SER n 
1 102 ASN n 
1 103 SER n 
1 104 MET n 
1 105 CYS n 
1 106 LEU n 
1 107 SER n 
1 108 TRP n 
1 109 PHE n 
1 110 GLN n 
1 111 ARG n 
1 112 VAL n 
1 113 GLN n 
1 114 ILE n 
1 115 ALA n 
1 116 HIS n 
1 117 ASP n 
1 118 VAL n 
1 119 ALA n 
1 120 ASP n 
1 121 ALA n 
1 122 LEU n 
1 123 ASN n 
1 124 TYR n 
1 125 LEU n 
1 126 HIS n 
1 127 ASN n 
1 128 TYR n 
1 129 ALA n 
1 130 ASN n 
1 131 PRO n 
1 132 PRO n 
1 133 HIS n 
1 134 VAL n 
1 135 HIS n 
1 136 LYS n 
1 137 ASN n 
1 138 LEU n 
1 139 LYS n 
1 140 SER n 
1 141 GLY n 
1 142 ASN n 
1 143 ILE n 
1 144 LEU n 
1 145 LEU n 
1 146 ASP n 
1 147 GLY n 
1 148 LYS n 
1 149 PHE n 
1 150 ARG n 
1 151 GLY n 
1 152 LYS n 
1 153 VAL n 
1 154 SER n 
1 155 ASN n 
1 156 PHE n 
1 157 GLY n 
1 158 LEU n 
1 159 ALA n 
1 160 ARG n 
1 161 VAL n 
1 162 MET n 
1 163 GLU n 
1 164 ASN n 
1 165 GLU n 
1 166 GLY n 
1 167 GLY n 
1 168 ASP n 
1 169 GLU n 
1 170 GLY n 
1 171 PHE n 
1 172 GLN n 
1 173 LEU n 
1 174 THR n 
1 175 ARG n 
1 176 HIS n 
1 177 VAL n 
1 178 ILE n 
1 179 GLY n 
1 180 THR n 
1 181 GLN n 
1 182 GLY n 
1 183 TYR n 
1 184 MET n 
1 185 ALA n 
1 186 PRO n 
1 187 GLU n 
1 188 TYR n 
1 189 ILE n 
1 190 GLU n 
1 191 ASN n 
1 192 GLY n 
1 193 LEU n 
1 194 ILE n 
1 195 THR n 
1 196 PRO n 
1 197 LYS n 
1 198 MET n 
1 199 ASP n 
1 200 VAL n 
1 201 PHE n 
1 202 ALA n 
1 203 PHE n 
1 204 GLY n 
1 205 VAL n 
1 206 VAL n 
1 207 ILE n 
1 208 LEU n 
1 209 GLU n 
1 210 LEU n 
1 211 LEU n 
1 212 SER n 
1 213 GLY n 
1 214 ARG n 
1 215 GLU n 
1 216 VAL n 
1 217 VAL n 
1 218 GLY n 
1 219 SER n 
1 220 ASP n 
1 221 LYS n 
1 222 SER n 
1 223 ASN n 
1 224 GLY n 
1 225 LEU n 
1 226 GLY n 
1 227 ASP n 
1 228 GLN n 
1 229 LEU n 
1 230 LEU n 
1 231 ALA n 
1 232 SER n 
1 233 THR n 
1 234 VAL n 
1 235 ASN n 
1 236 GLN n 
1 237 VAL n 
1 238 LEU n 
1 239 GLU n 
1 240 GLY n 
1 241 ASP n 
1 242 ASN n 
1 243 VAL n 
1 244 ARG n 
1 245 GLU n 
1 246 LYS n 
1 247 LEU n 
1 248 ARG n 
1 249 GLY n 
1 250 PHE n 
1 251 MET n 
1 252 ASP n 
1 253 PRO n 
1 254 ASN n 
1 255 LEU n 
1 256 ARG n 
1 257 ASP n 
1 258 GLU n 
1 259 TYR n 
1 260 PRO n 
1 261 LEU n 
1 262 ASP n 
1 263 LEU n 
1 264 ALA n 
1 265 PHE n 
1 266 SER n 
1 267 MET n 
1 268 ALA n 
1 269 GLU n 
1 270 ILE n 
1 271 ALA n 
1 272 LYS n 
1 273 ARG n 
1 274 CYS n 
1 275 VAL n 
1 276 ALA n 
1 277 ARG n 
1 278 ASP n 
1 279 LEU n 
1 280 ASN n 
1 281 SER n 
1 282 ARG n 
1 283 PRO n 
1 284 ASN n 
1 285 VAL n 
1 286 SER n 
1 287 GLU n 
1 288 VAL n 
1 289 PHE n 
1 290 MET n 
1 291 ILE n 
1 292 LEU n 
1 293 SER n 
1 294 LYS n 
1 295 ILE n 
1 296 GLN n 
1 297 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   297 
_entity_src_gen.gene_src_common_name               'barrel medic' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 '11433363, MTR_5g085790, MtrunA17_Chr5g0439331' 
_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      'Medicago truncatula' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3880 
_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               Rosetta2 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                       ?                               'C3 H7 N O2'        89.093 
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ?                               'C10 H17 N6 O12 P3' 
506.196 
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 
GOL non-polymer         . GLYCEROL                                      'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094 
HIS 'L-peptide linking' y HISTIDINE                                     ?                               'C6 H10 N3 O2 1'    
156.162 
HOH non-polymer         . WATER                                         ?                               'H2 O'              18.015 
ILE 'L-peptide linking' y ISOLEUCINE                                    ?                               'C6 H13 N O2'       
131.173 
LEU 'L-peptide linking' y LEUCINE                                       ?                               'C6 H13 N O2'       
131.173 
LYS 'L-peptide linking' y LYSINE                                        ?                               'C6 H15 N2 O2 1'    
147.195 
MET 'L-peptide linking' y METHIONINE                                    ?                               'C5 H11 N O2 S'     
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                 ?                               'C9 H11 N O2'       
165.189 
PRO 'L-peptide linking' y PROLINE                                       ?                               'C5 H9 N O2'        
115.130 
SER 'L-peptide linking' y SERINE                                        ?                               'C3 H7 N O3'        
105.093 
SO4 non-polymer         . 'SULFATE ION'                                 ?                               'O4 S -2'           96.063 
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   SER 1   340 340 SER SER A . n 
A 1 2   LEU 2   341 341 LEU LEU A . n 
A 1 3   THR 3   342 342 THR THR A . n 
A 1 4   VAL 4   343 343 VAL VAL A . n 
A 1 5   TYR 5   344 344 TYR TYR A . n 
A 1 6   LYS 6   345 345 LYS LYS A . n 
A 1 7   TYR 7   346 346 TYR TYR A . n 
A 1 8   GLU 8   347 347 GLU GLU A . n 
A 1 9   ASP 9   348 348 ASP ASP A . n 
A 1 10  LEU 10  349 349 LEU LEU A . n 
A 1 11  GLN 11  350 350 GLN GLN A . n 
A 1 12  ASN 12  351 351 ASN ASN A . n 
A 1 13  ALA 13  352 352 ALA ALA A . n 
A 1 14  THR 14  353 353 THR THR A . n 
A 1 15  ASN 15  354 354 ASN ASN A . n 
A 1 16  PHE 16  355 355 PHE PHE A . n 
A 1 17  PHE 17  356 356 PHE PHE A . n 
A 1 18  SER 18  357 357 SER SER A . n 
A 1 19  GLU 19  358 358 GLU GLU A . n 
A 1 20  GLU 20  359 359 GLU GLU A . n 
A 1 21  ASN 21  360 360 ASN ASN A . n 
A 1 22  LYS 22  361 361 LYS LYS A . n 
A 1 23  ILE 23  362 362 ILE ILE A . n 
A 1 24  LYS 24  363 363 LYS LYS A . n 
A 1 25  GLY 25  364 364 GLY GLY A . n 
A 1 26  SER 26  365 365 SER SER A . n 
A 1 27  VAL 27  366 366 VAL VAL A . n 
A 1 28  TYR 28  367 367 TYR TYR A . n 
A 1 29  ARG 29  368 368 ARG ARG A . n 
A 1 30  ALA 30  369 369 ALA ALA A . n 
A 1 31  SER 31  370 370 SER SER A . n 
A 1 32  PHE 32  371 371 PHE PHE A . n 
A 1 33  LYS 33  372 372 LYS LYS A . n 
A 1 34  GLY 34  373 373 GLY GLY A . n 
A 1 35  ASP 35  374 374 ASP ASP A . n 
A 1 36  ASP 36  375 375 ASP ASP A . n 
A 1 37  ALA 37  376 376 ALA ALA A . n 
A 1 38  ALA 38  377 377 ALA ALA A . n 
A 1 39  VAL 39  378 378 VAL VAL A . n 
A 1 40  LYS 40  379 379 LYS LYS A . n 
A 1 41  ILE 41  380 380 ILE ILE A . n 
A 1 42  LEU 42  381 381 LEU LEU A . n 
A 1 43  LYS 43  382 382 LYS LYS A . n 
A 1 44  GLY 44  383 383 GLY GLY A . n 
A 1 45  ASP 45  384 384 ASP ASP A . n 
A 1 46  VAL 46  385 385 VAL VAL A . n 
A 1 47  SER 47  386 386 SER SER A . n 
A 1 48  SER 48  387 387 SER SER A . n 
A 1 49  GLU 49  388 388 GLU GLU A . n 
A 1 50  ILE 50  389 389 ILE ILE A . n 
A 1 51  ASN 51  390 390 ASN ASN A . n 
A 1 52  ILE 52  391 391 ILE ILE A . n 
A 1 53  LEU 53  392 392 LEU LEU A . n 
A 1 54  LYS 54  393 393 LYS LYS A . n 
A 1 55  ARG 55  394 394 ARG ARG A . n 
A 1 56  ILE 56  395 395 ILE ILE A . n 
A 1 57  ASN 57  396 396 ASN ASN A . n 
A 1 58  HIS 58  397 397 HIS HIS A . n 
A 1 59  ALA 59  398 398 ALA ALA A . n 
A 1 60  ASN 60  399 399 ASN ASN A . n 
A 1 61  ILE 61  400 400 ILE ILE A . n 
A 1 62  ILE 62  401 401 ILE ILE A . n 
A 1 63  ARG 63  402 402 ARG ARG A . n 
A 1 64  LEU 64  403 403 LEU LEU A . n 
A 1 65  SER 65  404 404 SER SER A . n 
A 1 66  GLY 66  405 405 GLY GLY A . n 
A 1 67  PHE 67  406 406 PHE PHE A . n 
A 1 68  CYS 68  407 407 CYS CYS A . n 
A 1 69  VAL 69  408 408 VAL VAL A . n 
A 1 70  TYR 70  409 409 TYR TYR A . n 
A 1 71  LYS 71  410 410 LYS LYS A . n 
A 1 72  GLY 72  411 411 GLY GLY A . n 
A 1 73  ASN 73  412 412 ASN ASN A . n 
A 1 74  THR 74  413 413 THR THR A . n 
A 1 75  TYR 75  414 414 TYR TYR A . n 
A 1 76  LEU 76  415 415 LEU LEU A . n 
A 1 77  VAL 77  416 416 VAL VAL A . n 
A 1 78  TYR 78  417 417 TYR TYR A . n 
A 1 79  GLU 79  418 418 GLU GLU A . n 
A 1 80  PHE 80  419 419 PHE PHE A . n 
A 1 81  ALA 81  420 420 ALA ALA A . n 
A 1 82  GLU 82  421 421 GLU GLU A . n 
A 1 83  ASN 83  422 422 ASN ASN A . n 
A 1 84  ASN 84  423 423 ASN ASN A . n 
A 1 85  SER 85  424 424 SER SER A . n 
A 1 86  LEU 86  425 425 LEU LEU A . n 
A 1 87  ASP 87  426 426 ASP ASP A . n 
A 1 88  ASP 88  427 427 ASP ASP A . n 
A 1 89  TRP 89  428 428 TRP TRP A . n 
A 1 90  LEU 90  429 429 LEU LEU A . n 
A 1 91  HIS 91  430 430 HIS HIS A . n 
A 1 92  SER 92  431 431 SER SER A . n 
A 1 93  GLU 93  432 ?   ?   ?   A . n 
A 1 94  LYS 94  433 ?   ?   ?   A . n 
A 1 95  ASN 95  434 ?   ?   ?   A . n 
A 1 96  LYS 96  435 ?   ?   ?   A . n 
A 1 97  ASP 97  436 ?   ?   ?   A . n 
A 1 98  LYS 98  437 ?   ?   ?   A . n 
A 1 99  ASN 99  438 ?   ?   ?   A . n 
A 1 100 TYR 100 439 ?   ?   ?   A . n 
A 1 101 SER 101 440 ?   ?   ?   A . n 
A 1 102 ASN 102 441 ?   ?   ?   A . n 
A 1 103 SER 103 442 ?   ?   ?   A . n 
A 1 104 MET 104 443 443 MET MET A . n 
A 1 105 CYS 105 444 444 CYS CYS A . n 
A 1 106 LEU 106 445 445 LEU LEU A . n 
A 1 107 SER 107 446 446 SER SER A . n 
A 1 108 TRP 108 447 447 TRP TRP A . n 
A 1 109 PHE 109 448 448 PHE PHE A . n 
A 1 110 GLN 110 449 449 GLN GLN A . n 
A 1 111 ARG 111 450 450 ARG ARG A . n 
A 1 112 VAL 112 451 451 VAL VAL A . n 
A 1 113 GLN 113 452 452 GLN GLN A . n 
A 1 114 ILE 114 453 453 ILE ILE A . n 
A 1 115 ALA 115 454 454 ALA ALA A . n 
A 1 116 HIS 116 455 455 HIS HIS A . n 
A 1 117 ASP 117 456 456 ASP ASP A . n 
A 1 118 VAL 118 457 457 VAL VAL A . n 
A 1 119 ALA 119 458 458 ALA ALA A . n 
A 1 120 ASP 120 459 459 ASP ASP A . n 
A 1 121 ALA 121 460 460 ALA ALA A . n 
A 1 122 LEU 122 461 461 LEU LEU A . n 
A 1 123 ASN 123 462 462 ASN ASN A . n 
A 1 124 TYR 124 463 463 TYR TYR A . n 
A 1 125 LEU 125 464 464 LEU LEU A . n 
A 1 126 HIS 126 465 465 HIS HIS A . n 
A 1 127 ASN 127 466 466 ASN ASN A . n 
A 1 128 TYR 128 467 467 TYR TYR A . n 
A 1 129 ALA 129 468 468 ALA ALA A . n 
A 1 130 ASN 130 469 469 ASN ASN A . n 
A 1 131 PRO 131 470 470 PRO PRO A . n 
A 1 132 PRO 132 471 471 PRO PRO A . n 
A 1 133 HIS 133 472 472 HIS HIS A . n 
A 1 134 VAL 134 473 473 VAL VAL A . n 
A 1 135 HIS 135 474 474 HIS HIS A . n 
A 1 136 LYS 136 475 475 LYS LYS A . n 
A 1 137 ASN 137 476 476 ASN ASN A . n 
A 1 138 LEU 138 477 477 LEU LEU A . n 
A 1 139 LYS 139 478 478 LYS LYS A . n 
A 1 140 SER 140 479 479 SER SER A . n 
A 1 141 GLY 141 480 480 GLY GLY A . n 
A 1 142 ASN 142 481 481 ASN ASN A . n 
A 1 143 ILE 143 482 482 ILE ILE A . n 
A 1 144 LEU 144 483 483 LEU LEU A . n 
A 1 145 LEU 145 484 484 LEU LEU A . n 
A 1 146 ASP 146 485 485 ASP ASP A . n 
A 1 147 GLY 147 486 486 GLY GLY A . n 
A 1 148 LYS 148 487 487 LYS LYS A . n 
A 1 149 PHE 149 488 488 PHE PHE A . n 
A 1 150 ARG 150 489 489 ARG ARG A . n 
A 1 151 GLY 151 490 490 GLY GLY A . n 
A 1 152 LYS 152 491 491 LYS LYS A . n 
A 1 153 VAL 153 492 492 VAL VAL A . n 
A 1 154 SER 154 493 493 SER SER A . n 
A 1 155 ASN 155 494 494 ASN ASN A . n 
A 1 156 PHE 156 495 495 PHE PHE A . n 
A 1 157 GLY 157 496 496 GLY GLY A . n 
A 1 158 LEU 158 497 497 LEU LEU A . n 
A 1 159 ALA 159 498 498 ALA ALA A . n 
A 1 160 ARG 160 499 499 ARG ARG A . n 
A 1 161 VAL 161 500 500 VAL VAL A . n 
A 1 162 MET 162 501 501 MET MET A . n 
A 1 163 GLU 163 502 502 GLU GLU A . n 
A 1 164 ASN 164 503 503 ASN ASN A . n 
A 1 165 GLU 165 504 504 GLU GLU A . n 
A 1 166 GLY 166 505 505 GLY GLY A . n 
A 1 167 GLY 167 506 506 GLY GLY A . n 
A 1 168 ASP 168 507 507 ASP ASP A . n 
A 1 169 GLU 169 508 508 GLU GLU A . n 
A 1 170 GLY 170 509 509 GLY GLY A . n 
A 1 171 PHE 171 510 510 PHE PHE A . n 
A 1 172 GLN 172 511 511 GLN GLN A . n 
A 1 173 LEU 173 512 512 LEU LEU A . n 
A 1 174 THR 174 513 513 THR THR A . n 
A 1 175 ARG 175 514 514 ARG ARG A . n 
A 1 176 HIS 176 515 515 HIS HIS A . n 
A 1 177 VAL 177 516 516 VAL VAL A . n 
A 1 178 ILE 178 517 517 ILE ILE A . n 
A 1 179 GLY 179 518 518 GLY GLY A . n 
A 1 180 THR 180 519 519 THR THR A . n 
A 1 181 GLN 181 520 520 GLN GLN A . n 
A 1 182 GLY 182 521 521 GLY GLY A . n 
A 1 183 TYR 183 522 522 TYR TYR A . n 
A 1 184 MET 184 523 523 MET MET A . n 
A 1 185 ALA 185 524 524 ALA ALA A . n 
A 1 186 PRO 186 525 525 PRO PRO A . n 
A 1 187 GLU 187 526 526 GLU GLU A . n 
A 1 188 TYR 188 527 527 TYR TYR A . n 
A 1 189 ILE 189 528 528 ILE ILE A . n 
A 1 190 GLU 190 529 529 GLU GLU A . n 
A 1 191 ASN 191 530 530 ASN ASN A . n 
A 1 192 GLY 192 531 531 GLY GLY A . n 
A 1 193 LEU 193 532 532 LEU LEU A . n 
A 1 194 ILE 194 533 533 ILE ILE A . n 
A 1 195 THR 195 534 534 THR THR A . n 
A 1 196 PRO 196 535 535 PRO PRO A . n 
A 1 197 LYS 197 536 536 LYS LYS A . n 
A 1 198 MET 198 537 537 MET MET A . n 
A 1 199 ASP 199 538 538 ASP ASP A . n 
A 1 200 VAL 200 539 539 VAL VAL A . n 
A 1 201 PHE 201 540 540 PHE PHE A . n 
A 1 202 ALA 202 541 541 ALA ALA A . n 
A 1 203 PHE 203 542 542 PHE PHE A . n 
A 1 204 GLY 204 543 543 GLY GLY A . n 
A 1 205 VAL 205 544 544 VAL VAL A . n 
A 1 206 VAL 206 545 545 VAL VAL A . n 
A 1 207 ILE 207 546 546 ILE ILE A . n 
A 1 208 LEU 208 547 547 LEU LEU A . n 
A 1 209 GLU 209 548 548 GLU GLU A . n 
A 1 210 LEU 210 549 549 LEU LEU A . n 
A 1 211 LEU 211 550 550 LEU LEU A . n 
A 1 212 SER 212 551 551 SER SER A . n 
A 1 213 GLY 213 552 552 GLY GLY A . n 
A 1 214 ARG 214 553 553 ARG ARG A . n 
A 1 215 GLU 215 554 554 GLU GLU A . n 
A 1 216 VAL 216 555 555 VAL VAL A . n 
A 1 217 VAL 217 556 556 VAL VAL A . n 
A 1 218 GLY 218 557 557 GLY GLY A . n 
A 1 219 SER 219 558 558 SER SER A . n 
A 1 220 ASP 220 559 ?   ?   ?   A . n 
A 1 221 LYS 221 560 ?   ?   ?   A . n 
A 1 222 SER 222 561 ?   ?   ?   A . n 
A 1 223 ASN 223 562 ?   ?   ?   A . n 
A 1 224 GLY 224 563 ?   ?   ?   A . n 
A 1 225 LEU 225 564 ?   ?   ?   A . n 
A 1 226 GLY 226 565 ?   ?   ?   A . n 
A 1 227 ASP 227 566 566 ASP ASP A . n 
A 1 228 GLN 228 567 567 GLN GLN A . n 
A 1 229 LEU 229 568 568 LEU LEU A . n 
A 1 230 LEU 230 569 569 LEU LEU A . n 
A 1 231 ALA 231 570 570 ALA ALA A . n 
A 1 232 SER 232 571 571 SER SER A . n 
A 1 233 THR 233 572 572 THR THR A . n 
A 1 234 VAL 234 573 573 VAL VAL A . n 
A 1 235 ASN 235 574 574 ASN ASN A . n 
A 1 236 GLN 236 575 575 GLN GLN A . n 
A 1 237 VAL 237 576 576 VAL VAL A . n 
A 1 238 LEU 238 577 577 LEU LEU A . n 
A 1 239 GLU 239 578 578 GLU GLU A . n 
A 1 240 GLY 240 579 579 GLY GLY A . n 
A 1 241 ASP 241 580 580 ASP ASP A . n 
A 1 242 ASN 242 581 581 ASN ASN A . n 
A 1 243 VAL 243 582 582 VAL VAL A . n 
A 1 244 ARG 244 583 583 ARG ARG A . n 
A 1 245 GLU 245 584 584 GLU GLU A . n 
A 1 246 LYS 246 585 585 LYS LYS A . n 
A 1 247 LEU 247 586 586 LEU LEU A . n 
A 1 248 ARG 248 587 587 ARG ARG A . n 
A 1 249 GLY 249 588 588 GLY GLY A . n 
A 1 250 PHE 250 589 589 PHE PHE A . n 
A 1 251 MET 251 590 590 MET MET A . n 
A 1 252 ASP 252 591 591 ASP ASP A . n 
A 1 253 PRO 253 592 592 PRO PRO A . n 
A 1 254 ASN 254 593 593 ASN ASN A . n 
A 1 255 LEU 255 594 594 LEU LEU A . n 
A 1 256 ARG 256 595 595 ARG ARG A . n 
A 1 257 ASP 257 596 596 ASP ASP A . n 
A 1 258 GLU 258 597 597 GLU GLU A . n 
A 1 259 TYR 259 598 598 TYR TYR A . n 
A 1 260 PRO 260 599 599 PRO PRO A . n 
A 1 261 LEU 261 600 600 LEU LEU A . n 
A 1 262 ASP 262 601 601 ASP ASP A . n 
A 1 263 LEU 263 602 602 LEU LEU A . n 
A 1 264 ALA 264 603 603 ALA ALA A . n 
A 1 265 PHE 265 604 604 PHE PHE A . n 
A 1 266 SER 266 605 605 SER SER A . n 
A 1 267 MET 267 606 606 MET MET A . n 
A 1 268 ALA 268 607 607 ALA ALA A . n 
A 1 269 GLU 269 608 608 GLU GLU A . n 
A 1 270 ILE 270 609 609 ILE ILE A . n 
A 1 271 ALA 271 610 610 ALA ALA A . n 
A 1 272 LYS 272 611 611 LYS LYS A . n 
A 1 273 ARG 273 612 612 ARG ARG A . n 
A 1 274 CYS 274 613 613 CYS CYS A . n 
A 1 275 VAL 275 614 614 VAL VAL A . n 
A 1 276 ALA 276 615 615 ALA ALA A . n 
A 1 277 ARG 277 616 616 ARG ARG A . n 
A 1 278 ASP 278 617 617 ASP ASP A . n 
A 1 279 LEU 279 618 618 LEU LEU A . n 
A 1 280 ASN 280 619 619 ASN ASN A . n 
A 1 281 SER 281 620 620 SER SER A . n 
A 1 282 ARG 282 621 621 ARG ARG A . n 
A 1 283 PRO 283 622 622 PRO PRO A . n 
A 1 284 ASN 284 623 623 ASN ASN A . n 
A 1 285 VAL 285 624 624 VAL VAL A . n 
A 1 286 SER 286 625 625 SER SER A . n 
A 1 287 GLU 287 626 626 GLU GLU A . n 
A 1 288 VAL 288 627 627 VAL VAL A . n 
A 1 289 PHE 289 628 628 PHE PHE A . n 
A 1 290 MET 290 629 629 MET MET A . n 
A 1 291 ILE 291 630 630 ILE ILE A . n 
A 1 292 LEU 292 631 631 LEU LEU A . n 
A 1 293 SER 293 632 632 SER SER A . n 
A 1 294 LYS 294 633 633 LYS LYS A . n 
A 1 295 ILE 295 634 634 ILE ILE A . n 
A 1 296 GLN 296 635 635 GLN GLN A . n 
A 1 297 SER 297 636 636 SER SER A . n 
B 1 1   SER 1   340 340 SER SER B . n 
B 1 2   LEU 2   341 341 LEU LEU B . n 
B 1 3   THR 3   342 342 THR THR B . n 
B 1 4   VAL 4   343 343 VAL VAL B . n 
B 1 5   TYR 5   344 344 TYR TYR B . n 
B 1 6   LYS 6   345 345 LYS LYS B . n 
B 1 7   TYR 7   346 346 TYR TYR B . n 
B 1 8   GLU 8   347 347 GLU GLU B . n 
B 1 9   ASP 9   348 348 ASP ASP B . n 
B 1 10  LEU 10  349 349 LEU LEU B . n 
B 1 11  GLN 11  350 350 GLN GLN B . n 
B 1 12  ASN 12  351 351 ASN ASN B . n 
B 1 13  ALA 13  352 352 ALA ALA B . n 
B 1 14  THR 14  353 353 THR THR B . n 
B 1 15  ASN 15  354 354 ASN ASN B . n 
B 1 16  PHE 16  355 355 PHE PHE B . n 
B 1 17  PHE 17  356 356 PHE PHE B . n 
B 1 18  SER 18  357 357 SER SER B . n 
B 1 19  GLU 19  358 358 GLU GLU B . n 
B 1 20  GLU 20  359 359 GLU GLU B . n 
B 1 21  ASN 21  360 360 ASN ASN B . n 
B 1 22  LYS 22  361 361 LYS LYS B . n 
B 1 23  ILE 23  362 362 ILE ILE B . n 
B 1 24  LYS 24  363 363 LYS LYS B . n 
B 1 25  GLY 25  364 364 GLY GLY B . n 
B 1 26  SER 26  365 365 SER SER B . n 
B 1 27  VAL 27  366 366 VAL VAL B . n 
B 1 28  TYR 28  367 367 TYR TYR B . n 
B 1 29  ARG 29  368 368 ARG ARG B . n 
B 1 30  ALA 30  369 369 ALA ALA B . n 
B 1 31  SER 31  370 370 SER SER B . n 
B 1 32  PHE 32  371 371 PHE PHE B . n 
B 1 33  LYS 33  372 372 LYS LYS B . n 
B 1 34  GLY 34  373 373 GLY GLY B . n 
B 1 35  ASP 35  374 374 ASP ASP B . n 
B 1 36  ASP 36  375 375 ASP ASP B . n 
B 1 37  ALA 37  376 376 ALA ALA B . n 
B 1 38  ALA 38  377 377 ALA ALA B . n 
B 1 39  VAL 39  378 378 VAL VAL B . n 
B 1 40  LYS 40  379 379 LYS LYS B . n 
B 1 41  ILE 41  380 380 ILE ILE B . n 
B 1 42  LEU 42  381 381 LEU LEU B . n 
B 1 43  LYS 43  382 382 LYS LYS B . n 
B 1 44  GLY 44  383 383 GLY GLY B . n 
B 1 45  ASP 45  384 384 ASP ASP B . n 
B 1 46  VAL 46  385 385 VAL VAL B . n 
B 1 47  SER 47  386 386 SER SER B . n 
B 1 48  SER 48  387 387 SER SER B . n 
B 1 49  GLU 49  388 388 GLU GLU B . n 
B 1 50  ILE 50  389 389 ILE ILE B . n 
B 1 51  ASN 51  390 390 ASN ASN B . n 
B 1 52  ILE 52  391 391 ILE ILE B . n 
B 1 53  LEU 53  392 392 LEU LEU B . n 
B 1 54  LYS 54  393 393 LYS LYS B . n 
B 1 55  ARG 55  394 394 ARG ARG B . n 
B 1 56  ILE 56  395 395 ILE ILE B . n 
B 1 57  ASN 57  396 396 ASN ASN B . n 
B 1 58  HIS 58  397 397 HIS HIS B . n 
B 1 59  ALA 59  398 398 ALA ALA B . n 
B 1 60  ASN 60  399 399 ASN ASN B . n 
B 1 61  ILE 61  400 400 ILE ILE B . n 
B 1 62  ILE 62  401 401 ILE ILE B . n 
B 1 63  ARG 63  402 402 ARG ARG B . n 
B 1 64  LEU 64  403 403 LEU LEU B . n 
B 1 65  SER 65  404 404 SER SER B . n 
B 1 66  GLY 66  405 405 GLY GLY B . n 
B 1 67  PHE 67  406 406 PHE PHE B . n 
B 1 68  CYS 68  407 407 CYS CYS B . n 
B 1 69  VAL 69  408 408 VAL VAL B . n 
B 1 70  TYR 70  409 409 TYR TYR B . n 
B 1 71  LYS 71  410 410 LYS LYS B . n 
B 1 72  GLY 72  411 411 GLY GLY B . n 
B 1 73  ASN 73  412 412 ASN ASN B . n 
B 1 74  THR 74  413 413 THR THR B . n 
B 1 75  TYR 75  414 414 TYR TYR B . n 
B 1 76  LEU 76  415 415 LEU LEU B . n 
B 1 77  VAL 77  416 416 VAL VAL B . n 
B 1 78  TYR 78  417 417 TYR TYR B . n 
B 1 79  GLU 79  418 418 GLU GLU B . n 
B 1 80  PHE 80  419 419 PHE PHE B . n 
B 1 81  ALA 81  420 420 ALA ALA B . n 
B 1 82  GLU 82  421 421 GLU GLU B . n 
B 1 83  ASN 83  422 422 ASN ASN B . n 
B 1 84  ASN 84  423 423 ASN ASN B . n 
B 1 85  SER 85  424 424 SER SER B . n 
B 1 86  LEU 86  425 425 LEU LEU B . n 
B 1 87  ASP 87  426 426 ASP ASP B . n 
B 1 88  ASP 88  427 427 ASP ASP B . n 
B 1 89  TRP 89  428 428 TRP TRP B . n 
B 1 90  LEU 90  429 429 LEU LEU B . n 
B 1 91  HIS 91  430 430 HIS HIS B . n 
B 1 92  SER 92  431 431 SER SER B . n 
B 1 93  GLU 93  432 ?   ?   ?   B . n 
B 1 94  LYS 94  433 ?   ?   ?   B . n 
B 1 95  ASN 95  434 ?   ?   ?   B . n 
B 1 96  LYS 96  435 ?   ?   ?   B . n 
B 1 97  ASP 97  436 ?   ?   ?   B . n 
B 1 98  LYS 98  437 ?   ?   ?   B . n 
B 1 99  ASN 99  438 ?   ?   ?   B . n 
B 1 100 TYR 100 439 ?   ?   ?   B . n 
B 1 101 SER 101 440 ?   ?   ?   B . n 
B 1 102 ASN 102 441 ?   ?   ?   B . n 
B 1 103 SER 103 442 ?   ?   ?   B . n 
B 1 104 MET 104 443 443 MET MET B . n 
B 1 105 CYS 105 444 444 CYS CYS B . n 
B 1 106 LEU 106 445 445 LEU LEU B . n 
B 1 107 SER 107 446 446 SER SER B . n 
B 1 108 TRP 108 447 447 TRP TRP B . n 
B 1 109 PHE 109 448 448 PHE PHE B . n 
B 1 110 GLN 110 449 449 GLN GLN B . n 
B 1 111 ARG 111 450 450 ARG ARG B . n 
B 1 112 VAL 112 451 451 VAL VAL B . n 
B 1 113 GLN 113 452 452 GLN GLN B . n 
B 1 114 ILE 114 453 453 ILE ILE B . n 
B 1 115 ALA 115 454 454 ALA ALA B . n 
B 1 116 HIS 116 455 455 HIS HIS B . n 
B 1 117 ASP 117 456 456 ASP ASP B . n 
B 1 118 VAL 118 457 457 VAL VAL B . n 
B 1 119 ALA 119 458 458 ALA ALA B . n 
B 1 120 ASP 120 459 459 ASP ASP B . n 
B 1 121 ALA 121 460 460 ALA ALA B . n 
B 1 122 LEU 122 461 461 LEU LEU B . n 
B 1 123 ASN 123 462 462 ASN ASN B . n 
B 1 124 TYR 124 463 463 TYR TYR B . n 
B 1 125 LEU 125 464 464 LEU LEU B . n 
B 1 126 HIS 126 465 465 HIS HIS B . n 
B 1 127 ASN 127 466 466 ASN ASN B . n 
B 1 128 TYR 128 467 467 TYR TYR B . n 
B 1 129 ALA 129 468 468 ALA ALA B . n 
B 1 130 ASN 130 469 469 ASN ASN B . n 
B 1 131 PRO 131 470 470 PRO PRO B . n 
B 1 132 PRO 132 471 471 PRO PRO B . n 
B 1 133 HIS 133 472 472 HIS HIS B . n 
B 1 134 VAL 134 473 473 VAL VAL B . n 
B 1 135 HIS 135 474 474 HIS HIS B . n 
B 1 136 LYS 136 475 475 LYS LYS B . n 
B 1 137 ASN 137 476 476 ASN ASN B . n 
B 1 138 LEU 138 477 477 LEU LEU B . n 
B 1 139 LYS 139 478 478 LYS LYS B . n 
B 1 140 SER 140 479 479 SER SER B . n 
B 1 141 GLY 141 480 480 GLY GLY B . n 
B 1 142 ASN 142 481 481 ASN ASN B . n 
B 1 143 ILE 143 482 482 ILE ILE B . n 
B 1 144 LEU 144 483 483 LEU LEU B . n 
B 1 145 LEU 145 484 484 LEU LEU B . n 
B 1 146 ASP 146 485 485 ASP ASP B . n 
B 1 147 GLY 147 486 486 GLY GLY B . n 
B 1 148 LYS 148 487 487 LYS LYS B . n 
B 1 149 PHE 149 488 488 PHE PHE B . n 
B 1 150 ARG 150 489 489 ARG ARG B . n 
B 1 151 GLY 151 490 490 GLY GLY B . n 
B 1 152 LYS 152 491 491 LYS LYS B . n 
B 1 153 VAL 153 492 492 VAL VAL B . n 
B 1 154 SER 154 493 493 SER SER B . n 
B 1 155 ASN 155 494 494 ASN ASN B . n 
B 1 156 PHE 156 495 495 PHE PHE B . n 
B 1 157 GLY 157 496 496 GLY GLY B . n 
B 1 158 LEU 158 497 497 LEU LEU B . n 
B 1 159 ALA 159 498 ?   ?   ?   B . n 
B 1 160 ARG 160 499 ?   ?   ?   B . n 
B 1 161 VAL 161 500 ?   ?   ?   B . n 
B 1 162 MET 162 501 ?   ?   ?   B . n 
B 1 163 GLU 163 502 ?   ?   ?   B . n 
B 1 164 ASN 164 503 ?   ?   ?   B . n 
B 1 165 GLU 165 504 ?   ?   ?   B . n 
B 1 166 GLY 166 505 ?   ?   ?   B . n 
B 1 167 GLY 167 506 ?   ?   ?   B . n 
B 1 168 ASP 168 507 ?   ?   ?   B . n 
B 1 169 GLU 169 508 ?   ?   ?   B . n 
B 1 170 GLY 170 509 ?   ?   ?   B . n 
B 1 171 PHE 171 510 510 PHE PHE B . n 
B 1 172 GLN 172 511 511 GLN GLN B . n 
B 1 173 LEU 173 512 512 LEU LEU B . n 
B 1 174 THR 174 513 513 THR THR B . n 
B 1 175 ARG 175 514 514 ARG ARG B . n 
B 1 176 HIS 176 515 515 HIS HIS B . n 
B 1 177 VAL 177 516 516 VAL VAL B . n 
B 1 178 ILE 178 517 517 ILE ILE B . n 
B 1 179 GLY 179 518 518 GLY GLY B . n 
B 1 180 THR 180 519 519 THR THR B . n 
B 1 181 GLN 181 520 520 GLN GLN B . n 
B 1 182 GLY 182 521 521 GLY GLY B . n 
B 1 183 TYR 183 522 522 TYR TYR B . n 
B 1 184 MET 184 523 523 MET MET B . n 
B 1 185 ALA 185 524 524 ALA ALA B . n 
B 1 186 PRO 186 525 525 PRO PRO B . n 
B 1 187 GLU 187 526 526 GLU GLU B . n 
B 1 188 TYR 188 527 527 TYR TYR B . n 
B 1 189 ILE 189 528 528 ILE ILE B . n 
B 1 190 GLU 190 529 529 GLU GLU B . n 
B 1 191 ASN 191 530 530 ASN ASN B . n 
B 1 192 GLY 192 531 531 GLY GLY B . n 
B 1 193 LEU 193 532 532 LEU LEU B . n 
B 1 194 ILE 194 533 533 ILE ILE B . n 
B 1 195 THR 195 534 534 THR THR B . n 
B 1 196 PRO 196 535 535 PRO PRO B . n 
B 1 197 LYS 197 536 536 LYS LYS B . n 
B 1 198 MET 198 537 537 MET MET B . n 
B 1 199 ASP 199 538 538 ASP ASP B . n 
B 1 200 VAL 200 539 539 VAL VAL B . n 
B 1 201 PHE 201 540 540 PHE PHE B . n 
B 1 202 ALA 202 541 541 ALA ALA B . n 
B 1 203 PHE 203 542 542 PHE PHE B . n 
B 1 204 GLY 204 543 543 GLY GLY B . n 
B 1 205 VAL 205 544 544 VAL VAL B . n 
B 1 206 VAL 206 545 545 VAL VAL B . n 
B 1 207 ILE 207 546 546 ILE ILE B . n 
B 1 208 LEU 208 547 547 LEU LEU B . n 
B 1 209 GLU 209 548 548 GLU GLU B . n 
B 1 210 LEU 210 549 549 LEU LEU B . n 
B 1 211 LEU 211 550 550 LEU LEU B . n 
B 1 212 SER 212 551 551 SER SER B . n 
B 1 213 GLY 213 552 552 GLY GLY B . n 
B 1 214 ARG 214 553 553 ARG ARG B . n 
B 1 215 GLU 215 554 554 GLU GLU B . n 
B 1 216 VAL 216 555 555 VAL VAL B . n 
B 1 217 VAL 217 556 556 VAL VAL B . n 
B 1 218 GLY 218 557 557 GLY GLY B . n 
B 1 219 SER 219 558 558 SER SER B . n 
B 1 220 ASP 220 559 559 ASP ASP B . n 
B 1 221 LYS 221 560 560 LYS LYS B . n 
B 1 222 SER 222 561 561 SER SER B . n 
B 1 223 ASN 223 562 562 ASN ASN B . n 
B 1 224 GLY 224 563 563 GLY GLY B . n 
B 1 225 LEU 225 564 564 LEU LEU B . n 
B 1 226 GLY 226 565 565 GLY GLY B . n 
B 1 227 ASP 227 566 566 ASP ASP B . n 
B 1 228 GLN 228 567 567 GLN GLN B . n 
B 1 229 LEU 229 568 568 LEU LEU B . n 
B 1 230 LEU 230 569 569 LEU LEU B . n 
B 1 231 ALA 231 570 570 ALA ALA B . n 
B 1 232 SER 232 571 571 SER SER B . n 
B 1 233 THR 233 572 572 THR THR B . n 
B 1 234 VAL 234 573 573 VAL VAL B . n 
B 1 235 ASN 235 574 574 ASN ASN B . n 
B 1 236 GLN 236 575 575 GLN GLN B . n 
B 1 237 VAL 237 576 576 VAL VAL B . n 
B 1 238 LEU 238 577 577 LEU LEU B . n 
B 1 239 GLU 239 578 578 GLU GLU B . n 
B 1 240 GLY 240 579 579 GLY GLY B . n 
B 1 241 ASP 241 580 580 ASP ASP B . n 
B 1 242 ASN 242 581 581 ASN ASN B . n 
B 1 243 VAL 243 582 582 VAL VAL B . n 
B 1 244 ARG 244 583 583 ARG ARG B . n 
B 1 245 GLU 245 584 584 GLU GLU B . n 
B 1 246 LYS 246 585 585 LYS LYS B . n 
B 1 247 LEU 247 586 586 LEU LEU B . n 
B 1 248 ARG 248 587 587 ARG ARG B . n 
B 1 249 GLY 249 588 588 GLY GLY B . n 
B 1 250 PHE 250 589 589 PHE PHE B . n 
B 1 251 MET 251 590 590 MET MET B . n 
B 1 252 ASP 252 591 591 ASP ASP B . n 
B 1 253 PRO 253 592 592 PRO PRO B . n 
B 1 254 ASN 254 593 593 ASN ASN B . n 
B 1 255 LEU 255 594 594 LEU LEU B . n 
B 1 256 ARG 256 595 595 ARG ARG B . n 
B 1 257 ASP 257 596 596 ASP ASP B . n 
B 1 258 GLU 258 597 597 GLU GLU B . n 
B 1 259 TYR 259 598 598 TYR TYR B . n 
B 1 260 PRO 260 599 599 PRO PRO B . n 
B 1 261 LEU 261 600 600 LEU LEU B . n 
B 1 262 ASP 262 601 601 ASP ASP B . n 
B 1 263 LEU 263 602 602 LEU LEU B . n 
B 1 264 ALA 264 603 603 ALA ALA B . n 
B 1 265 PHE 265 604 604 PHE PHE B . n 
B 1 266 SER 266 605 605 SER SER B . n 
B 1 267 MET 267 606 606 MET MET B . n 
B 1 268 ALA 268 607 607 ALA ALA B . n 
B 1 269 GLU 269 608 608 GLU GLU B . n 
B 1 270 ILE 270 609 609 ILE ILE B . n 
B 1 271 ALA 271 610 610 ALA ALA B . n 
B 1 272 LYS 272 611 611 LYS LYS B . n 
B 1 273 ARG 273 612 612 ARG ARG B . n 
B 1 274 CYS 274 613 613 CYS CYS B . n 
B 1 275 VAL 275 614 614 VAL VAL B . n 
B 1 276 ALA 276 615 615 ALA ALA B . n 
B 1 277 ARG 277 616 616 ARG ARG B . n 
B 1 278 ASP 278 617 617 ASP ASP B . n 
B 1 279 LEU 279 618 618 LEU LEU B . n 
B 1 280 ASN 280 619 619 ASN ASN B . n 
B 1 281 SER 281 620 620 SER SER B . n 
B 1 282 ARG 282 621 621 ARG ARG B . n 
B 1 283 PRO 283 622 622 PRO PRO B . n 
B 1 284 ASN 284 623 623 ASN ASN B . n 
B 1 285 VAL 285 624 624 VAL VAL B . n 
B 1 286 SER 286 625 625 SER SER B . n 
B 1 287 GLU 287 626 626 GLU GLU B . n 
B 1 288 VAL 288 627 627 VAL VAL B . n 
B 1 289 PHE 289 628 628 PHE PHE B . n 
B 1 290 MET 290 629 629 MET MET B . n 
B 1 291 ILE 291 630 630 ILE ILE B . n 
B 1 292 LEU 292 631 631 LEU LEU B . n 
B 1 293 SER 293 632 632 SER SER B . n 
B 1 294 LYS 294 633 633 LYS LYS B . n 
B 1 295 ILE 295 634 634 ILE ILE B . n 
B 1 296 GLN 296 635 635 GLN GLN B . n 
B 1 297 SER 297 636 636 SER SER B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ANP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ANP 
_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 GOL 1  701 701 GOL GOL A . 
D 3 SO4 1  702 702 SO4 SO4 A . 
E 2 GOL 1  703 703 GOL GOL A . 
F 4 ANP 1  704 704 ANP ANP A . 
G 2 GOL 1  701 701 GOL GOL B . 
H 3 SO4 1  702 702 SO4 SO4 B . 
I 4 ANP 1  703 703 ANP ANP B . 
J 5 HOH 1  801 801 HOH HOH A . 
J 5 HOH 2  802 802 HOH HOH A . 
J 5 HOH 3  803 803 HOH HOH A . 
J 5 HOH 4  804 804 HOH HOH A . 
J 5 HOH 5  805 805 HOH HOH A . 
J 5 HOH 6  806 806 HOH HOH A . 
J 5 HOH 7  807 807 HOH HOH A . 
J 5 HOH 8  808 808 HOH HOH A . 
J 5 HOH 9  809 809 HOH HOH A . 
J 5 HOH 10 810 810 HOH HOH A . 
J 5 HOH 11 811 811 HOH HOH A . 
J 5 HOH 12 812 812 HOH HOH A . 
J 5 HOH 13 813 813 HOH HOH A . 
J 5 HOH 14 814 814 HOH HOH A . 
J 5 HOH 15 815 815 HOH HOH A . 
J 5 HOH 16 816 816 HOH HOH A . 
J 5 HOH 17 817 817 HOH HOH A . 
J 5 HOH 18 818 818 HOH HOH A . 
J 5 HOH 19 819 819 HOH HOH A . 
J 5 HOH 20 820 820 HOH HOH A . 
J 5 HOH 21 821 821 HOH HOH A . 
J 5 HOH 22 822 823 HOH HOH A . 
J 5 HOH 23 823 822 HOH HOH A . 
J 5 HOH 24 824 824 HOH HOH A . 
J 5 HOH 25 825 825 HOH HOH A . 
J 5 HOH 26 826 827 HOH HOH A . 
J 5 HOH 27 827 826 HOH HOH A . 
J 5 HOH 28 828 828 HOH HOH A . 
J 5 HOH 29 829 829 HOH HOH A . 
J 5 HOH 30 830 830 HOH HOH A . 
J 5 HOH 31 831 831 HOH HOH A . 
J 5 HOH 32 832 832 HOH HOH A . 
J 5 HOH 33 833 833 HOH HOH A . 
J 5 HOH 34 834 834 HOH HOH A . 
J 5 HOH 35 835 835 HOH HOH A . 
J 5 HOH 36 836 836 HOH HOH A . 
J 5 HOH 37 837 837 HOH HOH A . 
J 5 HOH 38 838 838 HOH HOH A . 
J 5 HOH 39 839 839 HOH HOH A . 
J 5 HOH 40 840 840 HOH HOH A . 
J 5 HOH 41 841 841 HOH HOH A . 
J 5 HOH 42 842 842 HOH HOH A . 
J 5 HOH 43 843 843 HOH HOH A . 
J 5 HOH 44 844 844 HOH HOH A . 
J 5 HOH 45 845 845 HOH HOH A . 
J 5 HOH 46 846 846 HOH HOH A . 
J 5 HOH 47 847 847 HOH HOH A . 
J 5 HOH 48 848 848 HOH HOH A . 
J 5 HOH 49 849 849 HOH HOH A . 
J 5 HOH 50 850 850 HOH HOH A . 
J 5 HOH 51 851 851 HOH HOH A . 
J 5 HOH 52 852 852 HOH HOH A . 
J 5 HOH 53 853 853 HOH HOH A . 
J 5 HOH 54 854 854 HOH HOH A . 
J 5 HOH 55 855 855 HOH HOH A . 
J 5 HOH 56 856 856 HOH HOH A . 
J 5 HOH 57 857 857 HOH HOH A . 
J 5 HOH 58 858 858 HOH HOH A . 
J 5 HOH 59 859 859 HOH HOH A . 
J 5 HOH 60 860 860 HOH HOH A . 
J 5 HOH 61 861 861 HOH HOH A . 
J 5 HOH 62 862 862 HOH HOH A . 
J 5 HOH 63 863 863 HOH HOH A . 
J 5 HOH 64 864 864 HOH HOH A . 
J 5 HOH 65 865 865 HOH HOH A . 
J 5 HOH 66 866 866 HOH HOH A . 
J 5 HOH 67 867 867 HOH HOH A . 
J 5 HOH 68 868 868 HOH HOH A . 
J 5 HOH 69 869 869 HOH HOH A . 
J 5 HOH 70 870 870 HOH HOH A . 
J 5 HOH 71 871 871 HOH HOH A . 
J 5 HOH 72 872 872 HOH HOH A . 
J 5 HOH 73 873 873 HOH HOH A . 
J 5 HOH 74 874 874 HOH HOH A . 
J 5 HOH 75 875 875 HOH HOH A . 
J 5 HOH 76 876 876 HOH HOH A . 
J 5 HOH 77 877 877 HOH HOH A . 
J 5 HOH 78 878 878 HOH HOH A . 
J 5 HOH 79 879 879 HOH HOH A . 
J 5 HOH 80 880 880 HOH HOH A . 
J 5 HOH 81 881 881 HOH HOH A . 
J 5 HOH 82 882 882 HOH HOH A . 
J 5 HOH 83 883 883 HOH HOH A . 
J 5 HOH 84 884 884 HOH HOH A . 
J 5 HOH 85 885 885 HOH HOH A . 
J 5 HOH 86 886 886 HOH HOH A . 
J 5 HOH 87 887 887 HOH HOH A . 
J 5 HOH 88 888 888 HOH HOH A . 
J 5 HOH 89 889 889 HOH HOH A . 
J 5 HOH 90 890 890 HOH HOH A . 
J 5 HOH 91 891 891 HOH HOH A . 
J 5 HOH 92 892 892 HOH HOH A . 
J 5 HOH 93 893 893 HOH HOH A . 
J 5 HOH 94 894 894 HOH HOH A . 
J 5 HOH 95 895 895 HOH HOH A . 
J 5 HOH 96 896 896 HOH HOH A . 
J 5 HOH 97 897 897 HOH HOH A . 
J 5 HOH 98 898 898 HOH HOH A . 
K 5 HOH 1  801 801 HOH HOH B . 
K 5 HOH 2  802 802 HOH HOH B . 
K 5 HOH 3  803 803 HOH HOH B . 
K 5 HOH 4  804 804 HOH HOH B . 
K 5 HOH 5  805 805 HOH HOH B . 
K 5 HOH 6  806 806 HOH HOH B . 
K 5 HOH 7  807 807 HOH HOH B . 
K 5 HOH 8  808 808 HOH HOH B . 
K 5 HOH 9  809 809 HOH HOH B . 
K 5 HOH 10 810 810 HOH HOH B . 
K 5 HOH 11 811 811 HOH HOH B . 
K 5 HOH 12 812 812 HOH HOH B . 
K 5 HOH 13 813 813 HOH HOH B . 
K 5 HOH 14 814 814 HOH HOH B . 
K 5 HOH 15 815 815 HOH HOH B . 
K 5 HOH 16 816 816 HOH HOH B . 
K 5 HOH 17 817 817 HOH HOH B . 
K 5 HOH 18 818 818 HOH HOH B . 
K 5 HOH 19 819 819 HOH HOH B . 
K 5 HOH 20 820 820 HOH HOH B . 
K 5 HOH 21 821 821 HOH HOH B . 
K 5 HOH 22 822 822 HOH HOH B . 
K 5 HOH 23 823 823 HOH HOH B . 
K 5 HOH 24 824 824 HOH HOH B . 
K 5 HOH 25 825 825 HOH HOH B . 
K 5 HOH 26 826 826 HOH HOH B . 
K 5 HOH 27 827 827 HOH HOH B . 
K 5 HOH 28 828 828 HOH HOH B . 
K 5 HOH 29 829 829 HOH HOH B . 
K 5 HOH 30 830 830 HOH HOH B . 
K 5 HOH 31 831 831 HOH HOH B . 
K 5 HOH 32 832 832 HOH HOH B . 
K 5 HOH 33 833 833 HOH HOH B . 
K 5 HOH 34 834 834 HOH HOH B . 
K 5 HOH 35 835 835 HOH HOH B . 
K 5 HOH 36 836 836 HOH HOH B . 
K 5 HOH 37 837 837 HOH HOH B . 
K 5 HOH 38 838 838 HOH HOH B . 
K 5 HOH 39 839 839 HOH HOH B . 
K 5 HOH 40 840 840 HOH HOH B . 
K 5 HOH 41 841 841 HOH HOH B . 
K 5 HOH 42 842 842 HOH HOH B . 
K 5 HOH 43 843 843 HOH HOH B . 
K 5 HOH 44 844 844 HOH HOH B . 
K 5 HOH 45 845 845 HOH HOH B . 
K 5 HOH 46 846 846 HOH HOH B . 
K 5 HOH 47 847 847 HOH HOH B . 
K 5 HOH 48 848 848 HOH HOH B . 
K 5 HOH 49 849 849 HOH HOH B . 
K 5 HOH 50 850 850 HOH HOH B . 
K 5 HOH 51 851 851 HOH HOH B . 
K 5 HOH 52 852 852 HOH HOH B . 
K 5 HOH 53 853 853 HOH HOH B . 
K 5 HOH 54 854 854 HOH HOH B . 
K 5 HOH 55 855 855 HOH HOH B . 
K 5 HOH 56 856 856 HOH HOH B . 
K 5 HOH 57 857 857 HOH HOH B . 
K 5 HOH 58 858 858 HOH HOH B . 
K 5 HOH 59 859 859 HOH HOH B . 
K 5 HOH 60 860 860 HOH HOH B . 
K 5 HOH 61 861 861 HOH HOH B . 
K 5 HOH 62 862 862 HOH HOH B . 
K 5 HOH 63 863 863 HOH HOH B . 
K 5 HOH 64 864 864 HOH HOH B . 
K 5 HOH 65 865 865 HOH HOH B . 
K 5 HOH 66 866 866 HOH HOH B . 
K 5 HOH 67 867 867 HOH HOH B . 
K 5 HOH 68 868 868 HOH HOH B . 
K 5 HOH 69 869 869 HOH HOH B . 
K 5 HOH 70 870 870 HOH HOH B . 
K 5 HOH 71 871 871 HOH HOH B . 
K 5 HOH 72 872 872 HOH HOH B . 
K 5 HOH 73 873 873 HOH HOH B . 
K 5 HOH 74 874 874 HOH HOH B . 
K 5 HOH 75 875 875 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.40 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8PS7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.684 
_cell.length_a_esd                 ? 
_cell.length_b                     78.242 
_cell.length_b_esd                 ? 
_cell.length_c                     70.365 
_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                         8PS7 
_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                   8PS7 
_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          42.19 
_exptl_crystal.description                  Needles 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    'ammonium sulfate, sodium cacodylate trihydrate, PEG8000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_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 EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-01-26 
_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   0.979491 
_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                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979491 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          21.79 
_reflns.entry_id                                       8PS7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.100 
_reflns.d_resolution_low                               43.124 
_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                                     18580 
_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                           91.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.500 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.2000 
_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                                0.24 
_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                                   0.98 
_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                                    2.10 
_reflns_shell.d_res_low                                     2.34 
_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                             929 
_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                                  0.62 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          70.2 
_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                               35.61 
_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                                 8PS7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             43.12 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     18578 
_refine.ls_number_reflns_R_free                  1465 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    56.7 
_refine.ls_percent_reflns_R_free                 7.890 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.225 
_refine.ls_R_factor_R_free                       0.269 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.221 
_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                          1.360 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GEOSTD + MONOMER LIBRARY + CDL V1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_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                 29.557 
_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                            0.280 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        43.12 
_refine_hist.number_atoms_solvent             173 
_refine_hist.number_atoms_total               4646 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4383 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         90 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  ? 4552 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.479  ? 6151 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.516 ? 1670 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.038  ? 676  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.002  ? 785  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.1000 2.1800  . . 13  91   3.00   . . . . 0.3151 . . . . . . . . . . . 0.3576 
'X-RAY DIFFRACTION' 2.1800 2.2600  . . 42  356  12.00  . . . . 0.2941 . . . . . . . . . . . 0.3212 
'X-RAY DIFFRACTION' 2.2600 2.3700  . . 56  568  19.00  . . . . 0.3142 . . . . . . . . . . . 0.3218 
'X-RAY DIFFRACTION' 2.3700 2.4900  . . 65  854  28.00  . . . . 0.2882 . . . . . . . . . . . 0.3570 
'X-RAY DIFFRACTION' 2.4900 2.6500  . . 102 1318 44.00  . . . . 0.2812 . . . . . . . . . . . 0.3228 
'X-RAY DIFFRACTION' 2.6500 2.8500  . . 183 2101 70.00  . . . . 0.2739 . . . . . . . . . . . 0.2721 
'X-RAY DIFFRACTION' 2.8500 3.1400  . . 264 2672 90.00  . . . . 0.2509 . . . . . . . . . . . 0.3058 
'X-RAY DIFFRACTION' 3.1400 3.5900  . . 250 3012 100.00 . . . . 0.2115 . . . . . . . . . . . 0.2774 
'X-RAY DIFFRACTION' 3.5900 4.5300  . . 244 3030 100.00 . . . . 0.1797 . . . . . . . . . . . 0.2211 
'X-RAY DIFFRACTION' 4.5300 43.1200 . . 246 3111 100.00 . . . . 0.2099 . . . . . . . . . . . 0.2622 
# 
_struct.entry_id                     8PS7 
_struct.title                        'Crystal structure of Medicago truncatula LYR4 kinase domain' 
_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        8PS7 
_struct_keywords.text            'Kinase, Immunity, LysM, PLANT PROTEIN' 
_struct_keywords.pdbx_keywords   'PLANT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    G7K7K0_MEDTR 
_struct_ref.pdbx_db_accession          G7K7K0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SLTVYKYEDLQNATNFFSEENKIKGSVYRASFKGDDAAVKILKGDVSSEINILKRINHANIIRLSGFCVYKGNTYLVYEF
AENNSLDDWLHSEKNKDKNYSNSMCLSWFQRVQIAHDVADALNYLHNYANPPHVHKNLKSGNILLDGKFRGKVSNFGLAR
VMENEGGDEGFQLTRHVIGTQGYMAPEYIENGLITPKMDVFAFGVVILELLSGREVVGSDKSNGLGDQLLASTVNQVLEG
DNVREKLRGFMDPNLRDEYPLDLAFSMAEIAKRCVARDLNSRPNVSEVFMILSKIQS
;
_struct_ref.pdbx_align_begin           340 
# 
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 8PS7 A 1 ? 297 ? G7K7K0 340 ? 636 ? 340 636 
2 1 8PS7 B 1 ? 297 ? G7K7K0 340 ? 636 ? 340 636 
# 
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,E,F,J 
2 1 B,G,H,I,K   
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'gel filtration' ? 
2 2 'gel filtration' ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 6   ? THR A 14  ? LYS A 345 THR A 353 1 ? 9  
HELX_P HELX_P2  AA2 VAL A 46  ? LYS A 54  ? VAL A 385 LYS A 393 1 ? 9  
HELX_P HELX_P3  AA3 SER A 85  ? HIS A 91  ? SER A 424 HIS A 430 1 ? 7  
HELX_P HELX_P4  AA4 SER A 107 ? TYR A 128 ? SER A 446 TYR A 467 1 ? 22 
HELX_P HELX_P5  AA5 GLN A 172 ? MET A 184 ? GLN A 511 MET A 523 1 ? 13 
HELX_P HELX_P6  AA6 ALA A 185 ? GLY A 192 ? ALA A 524 GLY A 531 1 ? 8  
HELX_P HELX_P7  AA7 THR A 195 ? GLY A 213 ? THR A 534 GLY A 552 1 ? 19 
HELX_P HELX_P8  AA8 LEU A 229 ? GLU A 239 ? LEU A 568 GLU A 578 1 ? 11 
HELX_P HELX_P9  AA9 ASN A 242 ? MET A 251 ? ASN A 581 MET A 590 1 ? 10 
HELX_P HELX_P10 AB1 ASP A 252 ? ARG A 256 ? ASP A 591 ARG A 595 5 ? 5  
HELX_P HELX_P11 AB2 PRO A 260 ? VAL A 275 ? PRO A 599 VAL A 614 1 ? 16 
HELX_P HELX_P12 AB3 ASP A 278 ? ARG A 282 ? ASP A 617 ARG A 621 5 ? 5  
HELX_P HELX_P13 AB4 ASN A 284 ? ILE A 295 ? ASN A 623 ILE A 634 1 ? 12 
HELX_P HELX_P14 AB5 LYS B 6   ? THR B 14  ? LYS B 345 THR B 353 1 ? 9  
HELX_P HELX_P15 AB6 ILE B 52  ? ILE B 56  ? ILE B 391 ILE B 395 5 ? 5  
HELX_P HELX_P16 AB7 SER B 85  ? SER B 92  ? SER B 424 SER B 431 1 ? 8  
HELX_P HELX_P17 AB8 SER B 107 ? TYR B 128 ? SER B 446 TYR B 467 1 ? 22 
HELX_P HELX_P18 AB9 LYS B 139 ? GLY B 141 ? LYS B 478 GLY B 480 5 ? 3  
HELX_P HELX_P19 AC1 GLN B 172 ? MET B 184 ? GLN B 511 MET B 523 1 ? 13 
HELX_P HELX_P20 AC2 ALA B 185 ? GLY B 192 ? ALA B 524 GLY B 531 1 ? 8  
HELX_P HELX_P21 AC3 THR B 195 ? GLY B 213 ? THR B 534 GLY B 552 1 ? 19 
HELX_P HELX_P22 AC4 LEU B 230 ? GLU B 239 ? LEU B 569 GLU B 578 1 ? 10 
HELX_P HELX_P23 AC5 ASN B 242 ? MET B 251 ? ASN B 581 MET B 590 1 ? 10 
HELX_P HELX_P24 AC6 ASP B 252 ? ARG B 256 ? ASP B 591 ARG B 595 5 ? 5  
HELX_P HELX_P25 AC7 PRO B 260 ? VAL B 275 ? PRO B 599 VAL B 614 1 ? 16 
HELX_P HELX_P26 AC8 ASN B 284 ? SER B 297 ? ASN B 623 SER B 636 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASN 130 A . ? ASN 469 A PRO 131 A ? PRO 470 A 1 0.24  
2 ASN 130 B . ? ASN 469 B PRO 131 B ? PRO 470 B 1 -1.64 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 2 ? 
AA3 ? 5 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 27  ? ALA A 30  ? VAL A 366 ALA A 369 
AA1 2 ALA A 37  ? LYS A 43  ? ALA A 376 LYS A 382 
AA1 3 ASN A 73  ? GLU A 79  ? ASN A 412 GLU A 418 
AA1 4 LEU A 64  ? TYR A 70  ? LEU A 403 TYR A 409 
AA2 1 LEU A 144 ? LEU A 145 ? LEU A 483 LEU A 484 
AA2 2 GLY A 151 ? LYS A 152 ? GLY A 490 LYS A 491 
AA3 1 THR B 3   ? VAL B 4   ? THR B 342 VAL B 343 
AA3 2 LEU B 64  ? TYR B 70  ? LEU B 403 TYR B 409 
AA3 3 ASN B 73  ? GLU B 79  ? ASN B 412 GLU B 418 
AA3 4 ALA B 37  ? LYS B 43  ? ALA B 376 LYS B 382 
AA3 5 VAL B 27  ? ALA B 30  ? VAL B 366 ALA B 369 
AA4 1 ILE B 143 ? LEU B 145 ? ILE B 482 LEU B 484 
AA4 2 GLY B 151 ? VAL B 153 ? GLY B 490 VAL B 492 
AA5 1 VAL B 217 ? SER B 219 ? VAL B 556 SER B 558 
AA5 2 ASP B 227 ? LEU B 229 ? ASP B 566 LEU B 568 
# 
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 TYR A 28  ? N TYR A 367 O VAL A 39  ? O VAL A 378 
AA1 2 3 N LEU A 42  ? N LEU A 381 O THR A 74  ? O THR A 413 
AA1 3 4 O TYR A 75  ? O TYR A 414 N CYS A 68  ? N CYS A 407 
AA2 1 2 N LEU A 144 ? N LEU A 483 O LYS A 152 ? O LYS A 491 
AA3 1 2 N THR B 3   ? N THR B 342 O PHE B 67  ? O PHE B 406 
AA3 2 3 N CYS B 68  ? N CYS B 407 O TYR B 75  ? O TYR B 414 
AA3 3 4 O THR B 74  ? O THR B 413 N LEU B 42  ? N LEU B 381 
AA3 4 5 O ALA B 37  ? O ALA B 376 N ALA B 30  ? N ALA B 369 
AA4 1 2 N LEU B 144 ? N LEU B 483 O LYS B 152 ? O LYS B 491 
AA5 1 2 N GLY B 218 ? N GLY B 557 O GLN B 228 ? O GLN B 567 
# 
_pdbx_entry_details.entry_id                   8PS7 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 LEU A 341 ? ? 54.74   -130.48 
2  1 SER A 357 ? ? -97.44  54.46   
3  1 GLU A 358 ? ? 49.62   26.83   
4  1 LYS A 361 ? ? -66.04  -179.55 
5  1 ASN A 422 ? ? 86.87   6.57    
6  1 ASN A 423 ? ? 65.85   -135.57 
7  1 LYS A 475 ? ? 83.85   -10.66  
8  1 SER A 493 ? ? -132.70 -71.23  
9  1 LEU A 497 ? ? 69.48   -26.02  
10 1 ASP A 596 ? ? 70.27   -10.20  
11 1 GLU B 358 ? ? 74.16   -27.59  
12 1 ASN B 390 ? ? -76.92  43.82   
13 1 ASN B 423 ? ? 57.86   -150.29 
14 1 LYS B 475 ? ? 79.60   -10.79  
15 1 ARG B 595 ? ? 50.41   -123.64 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
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 -32.6384 9.2838   -2.0069  0.3740 ? -0.0071 ? -0.0048 ? 0.4636 ? 0.0163  ? 0.4212 ? 2.8066 ? 
2.4763  ? -1.9758 ? 4.7848 ? -0.0966 ? 2.4826 ? -0.1415 ? 0.4409  ? 0.3165  ? -0.4185 ? -0.1611 ? -0.3957 ? 0.0967  ? -0.0907 ? 
0.2678  ? 
2  'X-RAY DIFFRACTION' ? refined -20.9474 16.3188  3.0988   0.4998 ? -0.2810 ? 0.1021  ? 0.7107 ? -0.0176 ? 0.3401 ? 9.4665 ? 
0.1268  ? -3.0836 ? 6.0648 ? -4.6822 ? 4.5563 ? 0.5339  ? -1.6687 ? 1.0699  ? 1.0767  ? -0.6050 ? -0.7704 ? -1.2156 ? 1.1638  ? 
-0.0621 ? 
3  'X-RAY DIFFRACTION' ? refined -21.0263 7.4500   -7.1383  0.2774 ? -0.0078 ? -0.0239 ? 0.4238 ? -0.0198 ? 0.0943 ? 2.9430 ? 
-0.6987 ? -2.0518 ? 2.2050 ? 0.7749  ? 2.8679 ? 0.3861  ? 0.0669  ? 0.1927  ? -0.0479 ? -0.5541 ? 0.1993  ? -0.0392 ? -0.6791 ? 
0.0993  ? 
4  'X-RAY DIFFRACTION' ? refined -10.6871 6.1534   -13.6389 0.1444 ? 0.0032  ? 0.0009  ? 0.2001 ? 0.0217  ? 0.0678 ? 1.5423 ? 
-0.0703 ? -0.1928 ? 3.9684 ? 0.0119  ? 1.6262 ? 0.0156  ? 0.0574  ? -0.0099 ? -0.1959 ? 0.0468  ? 0.1464  ? -0.3521 ? 0.1026  ? 
-0.0518 ? 
5  'X-RAY DIFFRACTION' ? refined -9.5200  -0.4570  3.4941   0.3892 ? -0.1279 ? 0.0139  ? 0.2686 ? 0.0275  ? 0.2545 ? 2.9680 ? 
-2.3664 ? 1.8864  ? 1.9025 ? -1.2584 ? 3.6383 ? 0.5954  ? -0.2151 ? -0.3897 ? -0.3588 ? -0.2564 ? 0.2343  ? 0.2108  ? -0.5081 ? 
-0.3169 ? 
6  'X-RAY DIFFRACTION' ? refined 0.0905   -5.3119  -4.8706  0.2084 ? 0.0344  ? 0.0457  ? 0.2867 ? 0.0471  ? 0.0407 ? 0.8848 ? 
-0.1603 ? 0.5402  ? 0.1099 ? -0.2421 ? 2.8216 ? -0.0050 ? -0.0053 ? -0.2258 ? -0.0854 ? 0.0014  ? 0.0401  ? 0.3446  ? 0.3698  ? 
-0.0088 ? 
7  'X-RAY DIFFRACTION' ? refined -1.2275  -15.8376 -19.9276 0.3744 ? 0.0860  ? 0.0123  ? 0.2594 ? -0.0709 ? 0.1690 ? 5.3434 ? 
-0.5629 ? -1.0708 ? 1.1021 ? -0.6423 ? 4.2878 ? -0.3108 ? 0.6300  ? -0.8789 ? -0.0820 ? 0.1344  ? 0.1462  ? 0.3486  ? -0.1117 ? 
0.1318  ? 
8  'X-RAY DIFFRACTION' ? refined 2.5281   0.8646   -17.5508 0.1073 ? 0.0148  ? 0.0677  ? 0.4143 ? 0.0496  ? 0.0932 ? 1.0023 ? 
-0.0062 ? -1.1856 ? 3.6126 ? 1.0443  ? 4.0416 ? 0.0517  ? 0.2666  ? 0.0540  ? -0.0102 ? 0.0335  ? -0.4571 ? -0.1656 ? 0.5810  ? 
-0.1159 ? 
9  'X-RAY DIFFRACTION' ? refined -21.4666 25.8865  -31.4627 0.3245 ? 0.0002  ? -0.0364 ? 0.4571 ? -0.0277 ? 0.2465 ? 3.3891 ? 
0.4653  ? 1.5233  ? 2.1998 ? 0.8930  ? 1.9027 ? 0.1427  ? 0.0999  ? -0.2548 ? -0.5028 ? -0.2599 ? 0.4782  ? 0.0643  ? -0.4223 ? 
0.1243  ? 
10 'X-RAY DIFFRACTION' ? refined -4.9350  30.1500  -30.0186 0.1982 ? -0.0265 ? -0.0106 ? 0.2823 ? 0.0164  ? 0.1173 ? 0.7227 ? 
-0.8208 ? -0.4946 ? 1.6558 ? -0.0665 ? 0.7973 ? -0.0163 ? 0.0749  ? -0.0914 ? -0.1248 ? 0.0273  ? 0.2268  ? 0.1520  ? 0.1445  ? 
-0.0194 ? 
11 'X-RAY DIFFRACTION' ? refined 3.9119   41.2277  -20.2973 0.1428 ? 0.0005  ? -0.0094 ? 0.2005 ? -0.0072 ? 0.0531 ? 1.7675 ? 
-0.0103 ? 0.3723  ? 2.8676 ? 0.1972  ? 3.7137 ? -0.1132 ? 0.0096  ? 0.2825  ? -0.1854 ? 0.1118  ? -0.1165 ? -0.3198 ? 0.0780  ? 
-0.0096 ? 
# 
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 'B' AND (RESID 340 THROUGH 375 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'B' AND (RESID 376 THROUGH 391 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'B' AND (RESID 392 THROUGH 446 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'B' AND (RESID 447 THROUGH 492 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'B' AND (RESID 493 THROUGH 522 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'B' AND (RESID 523 THROUGH 577 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'B' AND (RESID 578 THROUGH 599 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'B' AND (RESID 600 THROUGH 636 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 340 THROUGH 446 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 447 THROUGH 534 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 535 THROUGH 636 )
;
# 
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 896 ? 6.02 . 
2 1 O ? A HOH 897 ? 7.27 . 
3 1 O ? A HOH 898 ? 7.50 . 
4 1 O ? B HOH 874 ? 6.83 . 
5 1 O ? B HOH 875 ? 7.13 . 
# 
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 GLU 432 ? A GLU 93  
2  1 Y 1 A LYS 433 ? A LYS 94  
3  1 Y 1 A ASN 434 ? A ASN 95  
4  1 Y 1 A LYS 435 ? A LYS 96  
5  1 Y 1 A ASP 436 ? A ASP 97  
6  1 Y 1 A LYS 437 ? A LYS 98  
7  1 Y 1 A ASN 438 ? A ASN 99  
8  1 Y 1 A TYR 439 ? A TYR 100 
9  1 Y 1 A SER 440 ? A SER 101 
10 1 Y 1 A ASN 441 ? A ASN 102 
11 1 Y 1 A SER 442 ? A SER 103 
12 1 Y 1 A ASP 559 ? A ASP 220 
13 1 Y 1 A LYS 560 ? A LYS 221 
14 1 Y 1 A SER 561 ? A SER 222 
15 1 Y 1 A ASN 562 ? A ASN 223 
16 1 Y 1 A GLY 563 ? A GLY 224 
17 1 Y 1 A LEU 564 ? A LEU 225 
18 1 Y 1 A GLY 565 ? A GLY 226 
19 1 Y 1 B GLU 432 ? B GLU 93  
20 1 Y 1 B LYS 433 ? B LYS 94  
21 1 Y 1 B ASN 434 ? B ASN 95  
22 1 Y 1 B LYS 435 ? B LYS 96  
23 1 Y 1 B ASP 436 ? B ASP 97  
24 1 Y 1 B LYS 437 ? B LYS 98  
25 1 Y 1 B ASN 438 ? B ASN 99  
26 1 Y 1 B TYR 439 ? B TYR 100 
27 1 Y 1 B SER 440 ? B SER 101 
28 1 Y 1 B ASN 441 ? B ASN 102 
29 1 Y 1 B SER 442 ? B SER 103 
30 1 Y 1 B ALA 498 ? B ALA 159 
31 1 Y 1 B ARG 499 ? B ARG 160 
32 1 Y 1 B VAL 500 ? B VAL 161 
33 1 Y 1 B MET 501 ? B MET 162 
34 1 Y 1 B GLU 502 ? B GLU 163 
35 1 Y 1 B ASN 503 ? B ASN 164 
36 1 Y 1 B GLU 504 ? B GLU 165 
37 1 Y 1 B GLY 505 ? B GLY 166 
38 1 Y 1 B GLY 506 ? B GLY 167 
39 1 Y 1 B ASP 507 ? B ASP 168 
40 1 Y 1 B GLU 508 ? B GLU 169 
41 1 Y 1 B GLY 509 ? B GLY 170 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ANP PG     P N N 14  
ANP O1G    O N N 15  
ANP O2G    O N N 16  
ANP O3G    O N N 17  
ANP PB     P N N 18  
ANP O1B    O N N 19  
ANP O2B    O N N 20  
ANP N3B    N N N 21  
ANP PA     P N N 22  
ANP O1A    O N N 23  
ANP O2A    O N N 24  
ANP O3A    O N N 25  
ANP "O5'"  O N N 26  
ANP "C5'"  C N N 27  
ANP "C4'"  C N R 28  
ANP "O4'"  O N N 29  
ANP "C3'"  C N S 30  
ANP "O3'"  O N N 31  
ANP "C2'"  C N R 32  
ANP "O2'"  O N N 33  
ANP "C1'"  C N R 34  
ANP N9     N Y N 35  
ANP C8     C Y N 36  
ANP N7     N Y N 37  
ANP C5     C Y N 38  
ANP C6     C Y N 39  
ANP N6     N N N 40  
ANP N1     N Y N 41  
ANP C2     C Y N 42  
ANP N3     N Y N 43  
ANP C4     C Y N 44  
ANP HOG2   H N N 45  
ANP HOG3   H N N 46  
ANP HOB2   H N N 47  
ANP HNB1   H N N 48  
ANP HOA2   H N N 49  
ANP "H5'1" H N N 50  
ANP "H5'2" H N N 51  
ANP "H4'"  H N N 52  
ANP "H3'"  H N N 53  
ANP "HO3'" H N N 54  
ANP "H2'"  H N N 55  
ANP "HO2'" H N N 56  
ANP "H1'"  H N N 57  
ANP H8     H N N 58  
ANP HN61   H N N 59  
ANP HN62   H N N 60  
ANP H2     H N N 61  
ARG N      N N N 62  
ARG CA     C N S 63  
ARG C      C N N 64  
ARG O      O N N 65  
ARG CB     C N N 66  
ARG CG     C N N 67  
ARG CD     C N N 68  
ARG NE     N N N 69  
ARG CZ     C N N 70  
ARG NH1    N N N 71  
ARG NH2    N N N 72  
ARG OXT    O N N 73  
ARG H      H N N 74  
ARG H2     H N N 75  
ARG HA     H N N 76  
ARG HB2    H N N 77  
ARG HB3    H N N 78  
ARG HG2    H N N 79  
ARG HG3    H N N 80  
ARG HD2    H N N 81  
ARG HD3    H N N 82  
ARG HE     H N N 83  
ARG HH11   H N N 84  
ARG HH12   H N N 85  
ARG HH21   H N N 86  
ARG HH22   H N N 87  
ARG HXT    H N N 88  
ASN N      N N N 89  
ASN CA     C N S 90  
ASN C      C N N 91  
ASN O      O N N 92  
ASN CB     C N N 93  
ASN CG     C N N 94  
ASN OD1    O N N 95  
ASN ND2    N N N 96  
ASN OXT    O N N 97  
ASN H      H N N 98  
ASN H2     H N N 99  
ASN HA     H N N 100 
ASN HB2    H N N 101 
ASN HB3    H N N 102 
ASN HD21   H N N 103 
ASN HD22   H N N 104 
ASN HXT    H N N 105 
ASP N      N N N 106 
ASP CA     C N S 107 
ASP C      C N N 108 
ASP O      O N N 109 
ASP CB     C N N 110 
ASP CG     C N N 111 
ASP OD1    O N N 112 
ASP OD2    O N N 113 
ASP OXT    O N N 114 
ASP H      H N N 115 
ASP H2     H N N 116 
ASP HA     H N N 117 
ASP HB2    H N N 118 
ASP HB3    H N N 119 
ASP HD2    H N N 120 
ASP HXT    H N N 121 
CYS N      N N N 122 
CYS CA     C N R 123 
CYS C      C N N 124 
CYS O      O N N 125 
CYS CB     C N N 126 
CYS SG     S N N 127 
CYS OXT    O N N 128 
CYS H      H N N 129 
CYS H2     H N N 130 
CYS HA     H N N 131 
CYS HB2    H N N 132 
CYS HB3    H N N 133 
CYS HG     H N N 134 
CYS HXT    H N N 135 
GLN N      N N N 136 
GLN CA     C N S 137 
GLN C      C N N 138 
GLN O      O N N 139 
GLN CB     C N N 140 
GLN CG     C N N 141 
GLN CD     C N N 142 
GLN OE1    O N N 143 
GLN NE2    N N N 144 
GLN OXT    O N N 145 
GLN H      H N N 146 
GLN H2     H N N 147 
GLN HA     H N N 148 
GLN HB2    H N N 149 
GLN HB3    H N N 150 
GLN HG2    H N N 151 
GLN HG3    H N N 152 
GLN HE21   H N N 153 
GLN HE22   H N N 154 
GLN HXT    H N N 155 
GLU N      N N N 156 
GLU CA     C N S 157 
GLU C      C N N 158 
GLU O      O N N 159 
GLU CB     C N N 160 
GLU CG     C N N 161 
GLU CD     C N N 162 
GLU OE1    O N N 163 
GLU OE2    O N N 164 
GLU OXT    O N N 165 
GLU H      H N N 166 
GLU H2     H N N 167 
GLU HA     H N N 168 
GLU HB2    H N N 169 
GLU HB3    H N N 170 
GLU HG2    H N N 171 
GLU HG3    H N N 172 
GLU HE2    H N N 173 
GLU HXT    H N N 174 
GLY N      N N N 175 
GLY CA     C N N 176 
GLY C      C N N 177 
GLY O      O N N 178 
GLY OXT    O N N 179 
GLY H      H N N 180 
GLY H2     H N N 181 
GLY HA2    H N N 182 
GLY HA3    H N N 183 
GLY HXT    H N N 184 
GOL C1     C N N 185 
GOL O1     O N N 186 
GOL C2     C N N 187 
GOL O2     O N N 188 
GOL C3     C N N 189 
GOL O3     O N N 190 
GOL H11    H N N 191 
GOL H12    H N N 192 
GOL HO1    H N N 193 
GOL H2     H N N 194 
GOL HO2    H N N 195 
GOL H31    H N N 196 
GOL H32    H N N 197 
GOL HO3    H N N 198 
HIS N      N N N 199 
HIS CA     C N S 200 
HIS C      C N N 201 
HIS O      O N N 202 
HIS CB     C N N 203 
HIS CG     C Y N 204 
HIS ND1    N Y N 205 
HIS CD2    C Y N 206 
HIS CE1    C Y N 207 
HIS NE2    N Y N 208 
HIS OXT    O N N 209 
HIS H      H N N 210 
HIS H2     H N N 211 
HIS HA     H N N 212 
HIS HB2    H N N 213 
HIS HB3    H N N 214 
HIS HD1    H N N 215 
HIS HD2    H N N 216 
HIS HE1    H N N 217 
HIS HE2    H N N 218 
HIS HXT    H N N 219 
HOH O      O N N 220 
HOH H1     H N N 221 
HOH H2     H N N 222 
ILE N      N N N 223 
ILE CA     C N S 224 
ILE C      C N N 225 
ILE O      O N N 226 
ILE CB     C N S 227 
ILE CG1    C N N 228 
ILE CG2    C N N 229 
ILE CD1    C N N 230 
ILE OXT    O N N 231 
ILE H      H N N 232 
ILE H2     H N N 233 
ILE HA     H N N 234 
ILE HB     H N N 235 
ILE HG12   H N N 236 
ILE HG13   H N N 237 
ILE HG21   H N N 238 
ILE HG22   H N N 239 
ILE HG23   H N N 240 
ILE HD11   H N N 241 
ILE HD12   H N N 242 
ILE HD13   H N N 243 
ILE HXT    H N N 244 
LEU N      N N N 245 
LEU CA     C N S 246 
LEU C      C N N 247 
LEU O      O N N 248 
LEU CB     C N N 249 
LEU CG     C N N 250 
LEU CD1    C N N 251 
LEU CD2    C N N 252 
LEU OXT    O N N 253 
LEU H      H N N 254 
LEU H2     H N N 255 
LEU HA     H N N 256 
LEU HB2    H N N 257 
LEU HB3    H N N 258 
LEU HG     H N N 259 
LEU HD11   H N N 260 
LEU HD12   H N N 261 
LEU HD13   H N N 262 
LEU HD21   H N N 263 
LEU HD22   H N N 264 
LEU HD23   H N N 265 
LEU HXT    H N N 266 
LYS N      N N N 267 
LYS CA     C N S 268 
LYS C      C N N 269 
LYS O      O N N 270 
LYS CB     C N N 271 
LYS CG     C N N 272 
LYS CD     C N N 273 
LYS CE     C N N 274 
LYS NZ     N N N 275 
LYS OXT    O N N 276 
LYS H      H N N 277 
LYS H2     H N N 278 
LYS HA     H N N 279 
LYS HB2    H N N 280 
LYS HB3    H N N 281 
LYS HG2    H N N 282 
LYS HG3    H N N 283 
LYS HD2    H N N 284 
LYS HD3    H N N 285 
LYS HE2    H N N 286 
LYS HE3    H N N 287 
LYS HZ1    H N N 288 
LYS HZ2    H N N 289 
LYS HZ3    H N N 290 
LYS HXT    H N N 291 
MET N      N N N 292 
MET CA     C N S 293 
MET C      C N N 294 
MET O      O N N 295 
MET CB     C N N 296 
MET CG     C N N 297 
MET SD     S N N 298 
MET CE     C N N 299 
MET OXT    O N N 300 
MET H      H N N 301 
MET H2     H N N 302 
MET HA     H N N 303 
MET HB2    H N N 304 
MET HB3    H N N 305 
MET HG2    H N N 306 
MET HG3    H N N 307 
MET HE1    H N N 308 
MET HE2    H N N 309 
MET HE3    H N N 310 
MET HXT    H N N 311 
PHE N      N N N 312 
PHE CA     C N S 313 
PHE C      C N N 314 
PHE O      O N N 315 
PHE CB     C N N 316 
PHE CG     C Y N 317 
PHE CD1    C Y N 318 
PHE CD2    C Y N 319 
PHE CE1    C Y N 320 
PHE CE2    C Y N 321 
PHE CZ     C Y N 322 
PHE OXT    O N N 323 
PHE H      H N N 324 
PHE H2     H N N 325 
PHE HA     H N N 326 
PHE HB2    H N N 327 
PHE HB3    H N N 328 
PHE HD1    H N N 329 
PHE HD2    H N N 330 
PHE HE1    H N N 331 
PHE HE2    H N N 332 
PHE HZ     H N N 333 
PHE HXT    H N N 334 
PRO N      N N N 335 
PRO CA     C N S 336 
PRO C      C N N 337 
PRO O      O N N 338 
PRO CB     C N N 339 
PRO CG     C N N 340 
PRO CD     C N N 341 
PRO OXT    O N N 342 
PRO H      H N N 343 
PRO HA     H N N 344 
PRO HB2    H N N 345 
PRO HB3    H N N 346 
PRO HG2    H N N 347 
PRO HG3    H N N 348 
PRO HD2    H N N 349 
PRO HD3    H N N 350 
PRO HXT    H N N 351 
SER N      N N N 352 
SER CA     C N S 353 
SER C      C N N 354 
SER O      O N N 355 
SER CB     C N N 356 
SER OG     O N N 357 
SER OXT    O N N 358 
SER H      H N N 359 
SER H2     H N N 360 
SER HA     H N N 361 
SER HB2    H N N 362 
SER HB3    H N N 363 
SER HG     H N N 364 
SER HXT    H N N 365 
SO4 S      S N N 366 
SO4 O1     O N N 367 
SO4 O2     O N N 368 
SO4 O3     O N N 369 
SO4 O4     O N N 370 
THR N      N N N 371 
THR CA     C N S 372 
THR C      C N N 373 
THR O      O N N 374 
THR CB     C N R 375 
THR OG1    O N N 376 
THR CG2    C N N 377 
THR OXT    O N N 378 
THR H      H N N 379 
THR H2     H N N 380 
THR HA     H N N 381 
THR HB     H N N 382 
THR HG1    H N N 383 
THR HG21   H N N 384 
THR HG22   H N N 385 
THR HG23   H N N 386 
THR HXT    H N N 387 
TRP N      N N N 388 
TRP CA     C N S 389 
TRP C      C N N 390 
TRP O      O N N 391 
TRP CB     C N N 392 
TRP CG     C Y N 393 
TRP CD1    C Y N 394 
TRP CD2    C Y N 395 
TRP NE1    N Y N 396 
TRP CE2    C Y N 397 
TRP CE3    C Y N 398 
TRP CZ2    C Y N 399 
TRP CZ3    C Y N 400 
TRP CH2    C Y N 401 
TRP OXT    O N N 402 
TRP H      H N N 403 
TRP H2     H N N 404 
TRP HA     H N N 405 
TRP HB2    H N N 406 
TRP HB3    H N N 407 
TRP HD1    H N N 408 
TRP HE1    H N N 409 
TRP HE3    H N N 410 
TRP HZ2    H N N 411 
TRP HZ3    H N N 412 
TRP HH2    H N N 413 
TRP HXT    H N N 414 
TYR N      N N N 415 
TYR CA     C N S 416 
TYR C      C N N 417 
TYR O      O N N 418 
TYR CB     C N N 419 
TYR CG     C Y N 420 
TYR CD1    C Y N 421 
TYR CD2    C Y N 422 
TYR CE1    C Y N 423 
TYR CE2    C Y N 424 
TYR CZ     C Y N 425 
TYR OH     O N N 426 
TYR OXT    O N N 427 
TYR H      H N N 428 
TYR H2     H N N 429 
TYR HA     H N N 430 
TYR HB2    H N N 431 
TYR HB3    H N N 432 
TYR HD1    H N N 433 
TYR HD2    H N N 434 
TYR HE1    H N N 435 
TYR HE2    H N N 436 
TYR HH     H N N 437 
TYR HXT    H N N 438 
VAL N      N N N 439 
VAL CA     C N S 440 
VAL C      C N N 441 
VAL O      O N N 442 
VAL CB     C N N 443 
VAL CG1    C N N 444 
VAL CG2    C N N 445 
VAL OXT    O N N 446 
VAL H      H N N 447 
VAL H2     H N N 448 
VAL HA     H N N 449 
VAL HB     H N N 450 
VAL HG11   H N N 451 
VAL HG12   H N N 452 
VAL HG13   H N N 453 
VAL HG21   H N N 454 
VAL HG22   H N N 455 
VAL HG23   H N N 456 
VAL HXT    H N N 457 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ANP PG    O1G    doub N N 13  
ANP PG    O2G    sing N N 14  
ANP PG    O3G    sing N N 15  
ANP PG    N3B    sing N N 16  
ANP O2G   HOG2   sing N N 17  
ANP O3G   HOG3   sing N N 18  
ANP PB    O1B    doub N N 19  
ANP PB    O2B    sing N N 20  
ANP PB    N3B    sing N N 21  
ANP PB    O3A    sing N N 22  
ANP O2B   HOB2   sing N N 23  
ANP N3B   HNB1   sing N N 24  
ANP PA    O1A    doub N N 25  
ANP PA    O2A    sing N N 26  
ANP PA    O3A    sing N N 27  
ANP PA    "O5'"  sing N N 28  
ANP O2A   HOA2   sing N N 29  
ANP "O5'" "C5'"  sing N N 30  
ANP "C5'" "C4'"  sing N N 31  
ANP "C5'" "H5'1" sing N N 32  
ANP "C5'" "H5'2" sing N N 33  
ANP "C4'" "O4'"  sing N N 34  
ANP "C4'" "C3'"  sing N N 35  
ANP "C4'" "H4'"  sing N N 36  
ANP "O4'" "C1'"  sing N N 37  
ANP "C3'" "O3'"  sing N N 38  
ANP "C3'" "C2'"  sing N N 39  
ANP "C3'" "H3'"  sing N N 40  
ANP "O3'" "HO3'" sing N N 41  
ANP "C2'" "O2'"  sing N N 42  
ANP "C2'" "C1'"  sing N N 43  
ANP "C2'" "H2'"  sing N N 44  
ANP "O2'" "HO2'" sing N N 45  
ANP "C1'" N9     sing N N 46  
ANP "C1'" "H1'"  sing N N 47  
ANP N9    C8     sing Y N 48  
ANP N9    C4     sing Y N 49  
ANP C8    N7     doub Y N 50  
ANP C8    H8     sing N N 51  
ANP N7    C5     sing Y N 52  
ANP C5    C6     sing Y N 53  
ANP C5    C4     doub Y N 54  
ANP C6    N6     sing N N 55  
ANP C6    N1     doub Y N 56  
ANP N6    HN61   sing N N 57  
ANP N6    HN62   sing N N 58  
ANP N1    C2     sing Y N 59  
ANP C2    N3     doub Y N 60  
ANP C2    H2     sing N N 61  
ANP N3    C4     sing Y N 62  
ARG N     CA     sing N N 63  
ARG N     H      sing N N 64  
ARG N     H2     sing N N 65  
ARG CA    C      sing N N 66  
ARG CA    CB     sing N N 67  
ARG CA    HA     sing N N 68  
ARG C     O      doub N N 69  
ARG C     OXT    sing N N 70  
ARG CB    CG     sing N N 71  
ARG CB    HB2    sing N N 72  
ARG CB    HB3    sing N N 73  
ARG CG    CD     sing N N 74  
ARG CG    HG2    sing N N 75  
ARG CG    HG3    sing N N 76  
ARG CD    NE     sing N N 77  
ARG CD    HD2    sing N N 78  
ARG CD    HD3    sing N N 79  
ARG NE    CZ     sing N N 80  
ARG NE    HE     sing N N 81  
ARG CZ    NH1    sing N N 82  
ARG CZ    NH2    doub N N 83  
ARG NH1   HH11   sing N N 84  
ARG NH1   HH12   sing N N 85  
ARG NH2   HH21   sing N N 86  
ARG NH2   HH22   sing N N 87  
ARG OXT   HXT    sing N N 88  
ASN N     CA     sing N N 89  
ASN N     H      sing N N 90  
ASN N     H2     sing N N 91  
ASN CA    C      sing N N 92  
ASN CA    CB     sing N N 93  
ASN CA    HA     sing N N 94  
ASN C     O      doub N N 95  
ASN C     OXT    sing N N 96  
ASN CB    CG     sing N N 97  
ASN CB    HB2    sing N N 98  
ASN CB    HB3    sing N N 99  
ASN CG    OD1    doub N N 100 
ASN CG    ND2    sing N N 101 
ASN ND2   HD21   sing N N 102 
ASN ND2   HD22   sing N N 103 
ASN OXT   HXT    sing N N 104 
ASP N     CA     sing N N 105 
ASP N     H      sing N N 106 
ASP N     H2     sing N N 107 
ASP CA    C      sing N N 108 
ASP CA    CB     sing N N 109 
ASP CA    HA     sing N N 110 
ASP C     O      doub N N 111 
ASP C     OXT    sing N N 112 
ASP CB    CG     sing N N 113 
ASP CB    HB2    sing N N 114 
ASP CB    HB3    sing N N 115 
ASP CG    OD1    doub N N 116 
ASP CG    OD2    sing N N 117 
ASP OD2   HD2    sing N N 118 
ASP OXT   HXT    sing N N 119 
CYS N     CA     sing N N 120 
CYS N     H      sing N N 121 
CYS N     H2     sing N N 122 
CYS CA    C      sing N N 123 
CYS CA    CB     sing N N 124 
CYS CA    HA     sing N N 125 
CYS C     O      doub N N 126 
CYS C     OXT    sing N N 127 
CYS CB    SG     sing N N 128 
CYS CB    HB2    sing N N 129 
CYS CB    HB3    sing N N 130 
CYS SG    HG     sing N N 131 
CYS OXT   HXT    sing N N 132 
GLN N     CA     sing N N 133 
GLN N     H      sing N N 134 
GLN N     H2     sing N N 135 
GLN CA    C      sing N N 136 
GLN CA    CB     sing N N 137 
GLN CA    HA     sing N N 138 
GLN C     O      doub N N 139 
GLN C     OXT    sing N N 140 
GLN CB    CG     sing N N 141 
GLN CB    HB2    sing N N 142 
GLN CB    HB3    sing N N 143 
GLN CG    CD     sing N N 144 
GLN CG    HG2    sing N N 145 
GLN CG    HG3    sing N N 146 
GLN CD    OE1    doub N N 147 
GLN CD    NE2    sing N N 148 
GLN NE2   HE21   sing N N 149 
GLN NE2   HE22   sing N N 150 
GLN OXT   HXT    sing N N 151 
GLU N     CA     sing N N 152 
GLU N     H      sing N N 153 
GLU N     H2     sing N N 154 
GLU CA    C      sing N N 155 
GLU CA    CB     sing N N 156 
GLU CA    HA     sing N N 157 
GLU C     O      doub N N 158 
GLU C     OXT    sing N N 159 
GLU CB    CG     sing N N 160 
GLU CB    HB2    sing N N 161 
GLU CB    HB3    sing N N 162 
GLU CG    CD     sing N N 163 
GLU CG    HG2    sing N N 164 
GLU CG    HG3    sing N N 165 
GLU CD    OE1    doub N N 166 
GLU CD    OE2    sing N N 167 
GLU OE2   HE2    sing N N 168 
GLU OXT   HXT    sing N N 169 
GLY N     CA     sing N N 170 
GLY N     H      sing N N 171 
GLY N     H2     sing N N 172 
GLY CA    C      sing N N 173 
GLY CA    HA2    sing N N 174 
GLY CA    HA3    sing N N 175 
GLY C     O      doub N N 176 
GLY C     OXT    sing N N 177 
GLY OXT   HXT    sing N N 178 
GOL C1    O1     sing N N 179 
GOL C1    C2     sing N N 180 
GOL C1    H11    sing N N 181 
GOL C1    H12    sing N N 182 
GOL O1    HO1    sing N N 183 
GOL C2    O2     sing N N 184 
GOL C2    C3     sing N N 185 
GOL C2    H2     sing N N 186 
GOL O2    HO2    sing N N 187 
GOL C3    O3     sing N N 188 
GOL C3    H31    sing N N 189 
GOL C3    H32    sing N N 190 
GOL O3    HO3    sing N N 191 
HIS N     CA     sing N N 192 
HIS N     H      sing N N 193 
HIS N     H2     sing N N 194 
HIS CA    C      sing N N 195 
HIS CA    CB     sing N N 196 
HIS CA    HA     sing N N 197 
HIS C     O      doub N N 198 
HIS C     OXT    sing N N 199 
HIS CB    CG     sing N N 200 
HIS CB    HB2    sing N N 201 
HIS CB    HB3    sing N N 202 
HIS CG    ND1    sing Y N 203 
HIS CG    CD2    doub Y N 204 
HIS ND1   CE1    doub Y N 205 
HIS ND1   HD1    sing N N 206 
HIS CD2   NE2    sing Y N 207 
HIS CD2   HD2    sing N N 208 
HIS CE1   NE2    sing Y N 209 
HIS CE1   HE1    sing N N 210 
HIS NE2   HE2    sing N N 211 
HIS OXT   HXT    sing N N 212 
HOH O     H1     sing N N 213 
HOH O     H2     sing N N 214 
ILE N     CA     sing N N 215 
ILE N     H      sing N N 216 
ILE N     H2     sing N N 217 
ILE CA    C      sing N N 218 
ILE CA    CB     sing N N 219 
ILE CA    HA     sing N N 220 
ILE C     O      doub N N 221 
ILE C     OXT    sing N N 222 
ILE CB    CG1    sing N N 223 
ILE CB    CG2    sing N N 224 
ILE CB    HB     sing N N 225 
ILE CG1   CD1    sing N N 226 
ILE CG1   HG12   sing N N 227 
ILE CG1   HG13   sing N N 228 
ILE CG2   HG21   sing N N 229 
ILE CG2   HG22   sing N N 230 
ILE CG2   HG23   sing N N 231 
ILE CD1   HD11   sing N N 232 
ILE CD1   HD12   sing N N 233 
ILE CD1   HD13   sing N N 234 
ILE OXT   HXT    sing N N 235 
LEU N     CA     sing N N 236 
LEU N     H      sing N N 237 
LEU N     H2     sing N N 238 
LEU CA    C      sing N N 239 
LEU CA    CB     sing N N 240 
LEU CA    HA     sing N N 241 
LEU C     O      doub N N 242 
LEU C     OXT    sing N N 243 
LEU CB    CG     sing N N 244 
LEU CB    HB2    sing N N 245 
LEU CB    HB3    sing N N 246 
LEU CG    CD1    sing N N 247 
LEU CG    CD2    sing N N 248 
LEU CG    HG     sing N N 249 
LEU CD1   HD11   sing N N 250 
LEU CD1   HD12   sing N N 251 
LEU CD1   HD13   sing N N 252 
LEU CD2   HD21   sing N N 253 
LEU CD2   HD22   sing N N 254 
LEU CD2   HD23   sing N N 255 
LEU OXT   HXT    sing N N 256 
LYS N     CA     sing N N 257 
LYS N     H      sing N N 258 
LYS N     H2     sing N N 259 
LYS CA    C      sing N N 260 
LYS CA    CB     sing N N 261 
LYS CA    HA     sing N N 262 
LYS C     O      doub N N 263 
LYS C     OXT    sing N N 264 
LYS CB    CG     sing N N 265 
LYS CB    HB2    sing N N 266 
LYS CB    HB3    sing N N 267 
LYS CG    CD     sing N N 268 
LYS CG    HG2    sing N N 269 
LYS CG    HG3    sing N N 270 
LYS CD    CE     sing N N 271 
LYS CD    HD2    sing N N 272 
LYS CD    HD3    sing N N 273 
LYS CE    NZ     sing N N 274 
LYS CE    HE2    sing N N 275 
LYS CE    HE3    sing N N 276 
LYS NZ    HZ1    sing N N 277 
LYS NZ    HZ2    sing N N 278 
LYS NZ    HZ3    sing N N 279 
LYS OXT   HXT    sing N N 280 
MET N     CA     sing N N 281 
MET N     H      sing N N 282 
MET N     H2     sing N N 283 
MET CA    C      sing N N 284 
MET CA    CB     sing N N 285 
MET CA    HA     sing N N 286 
MET C     O      doub N N 287 
MET C     OXT    sing N N 288 
MET CB    CG     sing N N 289 
MET CB    HB2    sing N N 290 
MET CB    HB3    sing N N 291 
MET CG    SD     sing N N 292 
MET CG    HG2    sing N N 293 
MET CG    HG3    sing N N 294 
MET SD    CE     sing N N 295 
MET CE    HE1    sing N N 296 
MET CE    HE2    sing N N 297 
MET CE    HE3    sing N N 298 
MET OXT   HXT    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 
SO4 S     O1     doub N N 353 
SO4 S     O2     doub N N 354 
SO4 S     O3     sing N N 355 
SO4 S     O4     sing N N 356 
THR N     CA     sing N N 357 
THR N     H      sing N N 358 
THR N     H2     sing N N 359 
THR CA    C      sing N N 360 
THR CA    CB     sing N N 361 
THR CA    HA     sing N N 362 
THR C     O      doub N N 363 
THR C     OXT    sing N N 364 
THR CB    OG1    sing N N 365 
THR CB    CG2    sing N N 366 
THR CB    HB     sing N N 367 
THR OG1   HG1    sing N N 368 
THR CG2   HG21   sing N N 369 
THR CG2   HG22   sing N N 370 
THR CG2   HG23   sing N N 371 
THR OXT   HXT    sing N N 372 
TRP N     CA     sing N N 373 
TRP N     H      sing N N 374 
TRP N     H2     sing N N 375 
TRP CA    C      sing N N 376 
TRP CA    CB     sing N N 377 
TRP CA    HA     sing N N 378 
TRP C     O      doub N N 379 
TRP C     OXT    sing N N 380 
TRP CB    CG     sing N N 381 
TRP CB    HB2    sing N N 382 
TRP CB    HB3    sing N N 383 
TRP CG    CD1    doub Y N 384 
TRP CG    CD2    sing Y N 385 
TRP CD1   NE1    sing Y N 386 
TRP CD1   HD1    sing N N 387 
TRP CD2   CE2    doub Y N 388 
TRP CD2   CE3    sing Y N 389 
TRP NE1   CE2    sing Y N 390 
TRP NE1   HE1    sing N N 391 
TRP CE2   CZ2    sing Y N 392 
TRP CE3   CZ3    doub Y N 393 
TRP CE3   HE3    sing N N 394 
TRP CZ2   CH2    doub Y N 395 
TRP CZ2   HZ2    sing N N 396 
TRP CZ3   CH2    sing Y N 397 
TRP CZ3   HZ3    sing N N 398 
TRP CH2   HH2    sing N N 399 
TRP OXT   HXT    sing N N 400 
TYR N     CA     sing N N 401 
TYR N     H      sing N N 402 
TYR N     H2     sing N N 403 
TYR CA    C      sing N N 404 
TYR CA    CB     sing N N 405 
TYR CA    HA     sing N N 406 
TYR C     O      doub N N 407 
TYR C     OXT    sing N N 408 
TYR CB    CG     sing N N 409 
TYR CB    HB2    sing N N 410 
TYR CB    HB3    sing N N 411 
TYR CG    CD1    doub Y N 412 
TYR CG    CD2    sing Y N 413 
TYR CD1   CE1    sing Y N 414 
TYR CD1   HD1    sing N N 415 
TYR CD2   CE2    doub Y N 416 
TYR CD2   HD2    sing N N 417 
TYR CE1   CZ     doub Y N 418 
TYR CE1   HE1    sing N N 419 
TYR CE2   CZ     sing Y N 420 
TYR CE2   HE2    sing N N 421 
TYR CZ    OH     sing N N 422 
TYR OH    HH     sing N N 423 
TYR OXT   HXT    sing N N 424 
VAL N     CA     sing N N 425 
VAL N     H      sing N N 426 
VAL N     H2     sing N N 427 
VAL CA    C      sing N N 428 
VAL CA    CB     sing N N 429 
VAL CA    HA     sing N N 430 
VAL C     O      doub N N 431 
VAL C     OXT    sing N N 432 
VAL CB    CG1    sing N N 433 
VAL CB    CG2    sing N N 434 
VAL CB    HB     sing N N 435 
VAL CG1   HG11   sing N N 436 
VAL CG1   HG12   sing N N 437 
VAL CG1   HG13   sing N N 438 
VAL CG2   HG21   sing N N 439 
VAL CG2   HG22   sing N N 440 
VAL CG2   HG23   sing N N 441 
VAL OXT   HXT    sing N N 442 
# 
_pdbx_audit_support.funding_organization   'Novo Nordisk Foundation' 
_pdbx_audit_support.country                Denmark 
_pdbx_audit_support.grant_number           NNF18OC0052855 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Unpublished structure' 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8PS7 
_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]   0.019348 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000135 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012781 
_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]   0.014212 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N      . SER A 1 1   ? -18.497 9.660   -27.562 1.00 77.85  ? 340 SER A N      1 
ATOM   2    C CA     . SER A 1 1   ? -19.558 9.734   -28.559 1.00 79.96  ? 340 SER A CA     1 
ATOM   3    C C      . SER A 1 1   ? -20.279 11.078  -28.488 1.00 94.82  ? 340 SER A C      1 
ATOM   4    O O      . SER A 1 1   ? -21.163 11.362  -29.298 1.00 92.97  ? 340 SER A O      1 
ATOM   5    C CB     . SER A 1 1   ? -20.551 8.586   -28.372 1.00 83.23  ? 340 SER A CB     1 
ATOM   6    O OG     . SER A 1 1   ? -21.517 8.567   -29.408 1.00 89.05  ? 340 SER A OG     1 
ATOM   7    N N      . LEU A 1 2   ? -19.892 11.903  -27.516 1.00 87.08  ? 341 LEU A N      1 
ATOM   8    C CA     . LEU A 1 2   ? -20.439 13.255  -27.349 1.00 73.35  ? 341 LEU A CA     1 
ATOM   9    C C      . LEU A 1 2   ? -21.961 13.140  -27.258 1.00 79.69  ? 341 LEU A C      1 
ATOM   10   O O      . LEU A 1 2   ? -22.462 12.326  -26.469 1.00 106.62 ? 341 LEU A O      1 
ATOM   11   C CB     . LEU A 1 2   ? -19.917 14.146  -28.467 1.00 69.99  ? 341 LEU A CB     1 
ATOM   12   C CG     . LEU A 1 2   ? -18.428 14.489  -28.440 1.00 69.26  ? 341 LEU A CG     1 
ATOM   13   C CD1    . LEU A 1 2   ? -18.039 15.297  -29.668 1.00 70.59  ? 341 LEU A CD1    1 
ATOM   14   C CD2    . LEU A 1 2   ? -18.085 15.248  -27.169 1.00 87.77  ? 341 LEU A CD2    1 
ATOM   15   N N      . THR A 1 3   ? -22.721 13.924  -28.021 1.00 64.12  ? 342 THR A N      1 
ATOM   16   C CA     . THR A 1 3   ? -24.180 13.859  -28.025 1.00 62.06  ? 342 THR A CA     1 
ATOM   17   C C      . THR A 1 3   ? -24.649 14.057  -29.459 1.00 66.54  ? 342 THR A C      1 
ATOM   18   O O      . THR A 1 3   ? -24.509 15.153  -30.012 1.00 62.31  ? 342 THR A O      1 
ATOM   19   C CB     . THR A 1 3   ? -24.785 14.919  -27.103 1.00 54.94  ? 342 THR A CB     1 
ATOM   20   O OG1    . THR A 1 3   ? -24.321 14.711  -25.762 1.00 53.11  ? 342 THR A OG1    1 
ATOM   21   C CG2    . THR A 1 3   ? -26.304 14.849  -27.127 1.00 57.57  ? 342 THR A CG2    1 
ATOM   22   N N      . VAL A 1 4   ? -25.198 13.004  -30.056 1.00 65.86  ? 343 VAL A N      1 
ATOM   23   C CA     . VAL A 1 4   ? -25.656 13.057  -31.440 1.00 65.56  ? 343 VAL A CA     1 
ATOM   24   C C      . VAL A 1 4   ? -26.936 13.878  -31.509 1.00 67.54  ? 343 VAL A C      1 
ATOM   25   O O      . VAL A 1 4   ? -27.887 13.637  -30.755 1.00 69.27  ? 343 VAL A O      1 
ATOM   26   C CB     . VAL A 1 4   ? -25.867 11.643  -31.999 1.00 60.74  ? 343 VAL A CB     1 
ATOM   27   C CG1    . VAL A 1 4   ? -26.554 11.710  -33.350 1.00 60.35  ? 343 VAL A CG1    1 
ATOM   28   C CG2    . VAL A 1 4   ? -24.534 10.919  -32.111 1.00 64.41  ? 343 VAL A CG2    1 
ATOM   29   N N      . TYR A 1 5   ? -26.960 14.851  -32.418 1.00 59.04  ? 344 TYR A N      1 
ATOM   30   C CA     . TYR A 1 5   ? -28.049 15.807  -32.540 1.00 54.89  ? 344 TYR A CA     1 
ATOM   31   C C      . TYR A 1 5   ? -28.852 15.558  -33.810 1.00 57.50  ? 344 TYR A C      1 
ATOM   32   O O      . TYR A 1 5   ? -28.298 15.179  -34.848 1.00 58.25  ? 344 TYR A O      1 
ATOM   33   C CB     . TYR A 1 5   ? -27.518 17.245  -32.552 1.00 53.77  ? 344 TYR A CB     1 
ATOM   34   C CG     . TYR A 1 5   ? -27.199 17.806  -31.184 1.00 53.79  ? 344 TYR A CG     1 
ATOM   35   C CD1    . TYR A 1 5   ? -28.209 18.265  -30.349 1.00 51.02  ? 344 TYR A CD1    1 
ATOM   36   C CD2    . TYR A 1 5   ? -25.888 17.894  -30.735 1.00 51.54  ? 344 TYR A CD2    1 
ATOM   37   C CE1    . TYR A 1 5   ? -27.925 18.784  -29.100 1.00 47.83  ? 344 TYR A CE1    1 
ATOM   38   C CE2    . TYR A 1 5   ? -25.593 18.411  -29.488 1.00 50.20  ? 344 TYR A CE2    1 
ATOM   39   C CZ     . TYR A 1 5   ? -26.614 18.855  -28.674 1.00 53.49  ? 344 TYR A CZ     1 
ATOM   40   O OH     . TYR A 1 5   ? -26.320 19.371  -27.431 1.00 47.78  ? 344 TYR A OH     1 
ATOM   41   N N      . LYS A 1 6   ? -30.160 15.781  -33.716 1.00 57.64  ? 345 LYS A N      1 
ATOM   42   C CA     . LYS A 1 6   ? -31.038 15.782  -34.876 1.00 48.74  ? 345 LYS A CA     1 
ATOM   43   C C      . LYS A 1 6   ? -31.063 17.184  -35.470 1.00 46.27  ? 345 LYS A C      1 
ATOM   44   O O      . LYS A 1 6   ? -31.273 18.164  -34.747 1.00 43.71  ? 345 LYS A O      1 
ATOM   45   C CB     . LYS A 1 6   ? -32.452 15.348  -34.488 1.00 47.87  ? 345 LYS A CB     1 
ATOM   46   C CG     . LYS A 1 6   ? -32.518 14.271  -33.415 1.00 54.34  ? 345 LYS A CG     1 
ATOM   47   C CD     . LYS A 1 6   ? -33.955 14.075  -32.949 1.00 63.68  ? 345 LYS A CD     1 
ATOM   48   C CE     . LYS A 1 6   ? -34.026 13.450  -31.562 1.00 63.57  ? 345 LYS A CE     1 
ATOM   49   N NZ     . LYS A 1 6   ? -33.519 12.052  -31.541 1.00 64.10  ? 345 LYS A NZ     1 
ATOM   50   N N      . TYR A 1 7   ? -30.844 17.277  -36.784 1.00 45.11  ? 346 TYR A N      1 
ATOM   51   C CA     . TYR A 1 7   ? -30.825 18.581  -37.441 1.00 44.64  ? 346 TYR A CA     1 
ATOM   52   C C      . TYR A 1 7   ? -32.069 19.397  -37.114 1.00 45.27  ? 346 TYR A C      1 
ATOM   53   O O      . TYR A 1 7   ? -31.994 20.627  -37.002 1.00 44.59  ? 346 TYR A O      1 
ATOM   54   C CB     . TYR A 1 7   ? -30.686 18.401  -38.954 1.00 48.46  ? 346 TYR A CB     1 
ATOM   55   C CG     . TYR A 1 7   ? -30.762 19.687  -39.747 1.00 45.65  ? 346 TYR A CG     1 
ATOM   56   C CD1    . TYR A 1 7   ? -29.707 20.590  -39.746 1.00 43.89  ? 346 TYR A CD1    1 
ATOM   57   C CD2    . TYR A 1 7   ? -31.883 19.991  -40.508 1.00 48.17  ? 346 TYR A CD2    1 
ATOM   58   C CE1    . TYR A 1 7   ? -29.773 21.764  -40.473 1.00 46.09  ? 346 TYR A CE1    1 
ATOM   59   C CE2    . TYR A 1 7   ? -31.957 21.161  -41.239 1.00 47.85  ? 346 TYR A CE2    1 
ATOM   60   C CZ     . TYR A 1 7   ? -30.900 22.044  -41.218 1.00 46.15  ? 346 TYR A CZ     1 
ATOM   61   O OH     . TYR A 1 7   ? -30.972 23.211  -41.945 1.00 46.68  ? 346 TYR A OH     1 
ATOM   62   N N      . GLU A 1 8   ? -33.216 18.734  -36.952 1.00 47.21  ? 347 GLU A N      1 
ATOM   63   C CA     . GLU A 1 8   ? -34.447 19.436  -36.600 1.00 48.29  ? 347 GLU A CA     1 
ATOM   64   C C      . GLU A 1 8   ? -34.257 20.278  -35.345 1.00 46.76  ? 347 GLU A C      1 
ATOM   65   O O      . GLU A 1 8   ? -34.538 21.481  -35.337 1.00 46.51  ? 347 GLU A O      1 
ATOM   66   C CB     . GLU A 1 8   ? -35.578 18.428  -36.398 1.00 50.64  ? 347 GLU A CB     1 
ATOM   67   C CG     . GLU A 1 8   ? -35.442 17.172  -37.237 1.00 52.41  ? 347 GLU A CG     1 
ATOM   68   C CD     . GLU A 1 8   ? -36.311 16.039  -36.728 1.00 62.11  ? 347 GLU A CD     1 
ATOM   69   O OE1    . GLU A 1 8   ? -37.394 16.322  -36.171 1.00 55.25  ? 347 GLU A OE1    1 
ATOM   70   O OE2    . GLU A 1 8   ? -35.904 14.866  -36.874 1.00 63.74  ? 347 GLU A OE2    1 
ATOM   71   N N      . ASP A 1 9   ? -33.776 19.651  -34.268 1.00 45.94  ? 348 ASP A N      1 
ATOM   72   C CA     . ASP A 1 9   ? -33.568 20.369  -33.016 1.00 44.68  ? 348 ASP A CA     1 
ATOM   73   C C      . ASP A 1 9   ? -32.655 21.572  -33.203 1.00 42.64  ? 348 ASP A C      1 
ATOM   74   O O      . ASP A 1 9   ? -32.741 22.540  -32.439 1.00 42.01  ? 348 ASP A O      1 
ATOM   75   C CB     . ASP A 1 9   ? -32.990 19.423  -31.964 1.00 45.77  ? 348 ASP A CB     1 
ATOM   76   C CG     . ASP A 1 9   ? -33.793 18.143  -31.828 1.00 51.33  ? 348 ASP A CG     1 
ATOM   77   O OD1    . ASP A 1 9   ? -35.038 18.223  -31.755 1.00 48.34  ? 348 ASP A OD1    1 
ATOM   78   O OD2    . ASP A 1 9   ? -33.177 17.056  -31.801 1.00 54.65  ? 348 ASP A OD2    1 
ATOM   79   N N      . LEU A 1 10  ? -31.776 21.532  -34.206 1.00 41.82  ? 349 LEU A N      1 
ATOM   80   C CA     . LEU A 1 10  ? -30.890 22.662  -34.458 1.00 40.96  ? 349 LEU A CA     1 
ATOM   81   C C      . LEU A 1 10  ? -31.621 23.797  -35.167 1.00 41.13  ? 349 LEU A C      1 
ATOM   82   O O      . LEU A 1 10  ? -31.461 24.966  -34.798 1.00 41.46  ? 349 LEU A O      1 
ATOM   83   C CB     . LEU A 1 10  ? -29.678 22.207  -35.272 1.00 40.98  ? 349 LEU A CB     1 
ATOM   84   C CG     . LEU A 1 10  ? -28.917 21.007  -34.699 1.00 38.66  ? 349 LEU A CG     1 
ATOM   85   C CD1    . LEU A 1 10  ? -27.650 20.740  -35.496 1.00 39.74  ? 349 LEU A CD1    1 
ATOM   86   C CD2    . LEU A 1 10  ? -28.602 21.217  -33.226 1.00 37.37  ? 349 LEU A CD2    1 
ATOM   87   N N      . GLN A 1 11  ? -32.425 23.472  -36.183 1.00 43.02  ? 350 GLN A N      1 
ATOM   88   C CA     . GLN A 1 11  ? -33.240 24.488  -36.842 1.00 44.35  ? 350 GLN A CA     1 
ATOM   89   C C      . GLN A 1 11  ? -34.078 25.260  -35.832 1.00 44.75  ? 350 GLN A C      1 
ATOM   90   O O      . GLN A 1 11  ? -34.077 26.496  -35.817 1.00 44.57  ? 350 GLN A O      1 
ATOM   91   C CB     . GLN A 1 11  ? -34.146 23.839  -37.890 1.00 46.65  ? 350 GLN A CB     1 
ATOM   92   C CG     . GLN A 1 11  ? -33.497 23.586  -39.236 1.00 46.93  ? 350 GLN A CG     1 
ATOM   93   C CD     . GLN A 1 11  ? -34.455 22.943  -40.218 1.00 49.43  ? 350 GLN A CD     1 
ATOM   94   O OE1    . GLN A 1 11  ? -35.265 22.095  -39.846 1.00 50.58  ? 350 GLN A OE1    1 
ATOM   95   N NE2    . GLN A 1 11  ? -34.373 23.350  -41.480 1.00 51.10  ? 350 GLN A NE2    1 
ATOM   96   N N      . ASN A 1 12  ? -34.802 24.539  -34.975 1.00 45.56  ? 351 ASN A N      1 
ATOM   97   C CA     . ASN A 1 12  ? -35.713 25.191  -34.040 1.00 46.47  ? 351 ASN A CA     1 
ATOM   98   C C      . ASN A 1 12  ? -34.957 26.039  -33.023 1.00 44.64  ? 351 ASN A C      1 
ATOM   99   O O      . ASN A 1 12  ? -35.421 27.121  -32.644 1.00 45.17  ? 351 ASN A O      1 
ATOM   100  C CB     . ASN A 1 12  ? -36.575 24.141  -33.338 1.00 47.97  ? 351 ASN A CB     1 
ATOM   101  C CG     . ASN A 1 12  ? -37.316 23.245  -34.316 1.00 49.92  ? 351 ASN A CG     1 
ATOM   102  O OD1    . ASN A 1 12  ? -37.582 23.633  -35.455 1.00 50.76  ? 351 ASN A OD1    1 
ATOM   103  N ND2    . ASN A 1 12  ? -37.648 22.038  -33.876 1.00 50.86  ? 351 ASN A ND2    1 
ATOM   104  N N      . ALA A 1 13  ? -33.795 25.567  -32.568 1.00 44.62  ? 352 ALA A N      1 
ATOM   105  C CA     . ALA A 1 13  ? -33.018 26.337  -31.603 1.00 47.87  ? 352 ALA A CA     1 
ATOM   106  C C      . ALA A 1 13  ? -32.478 27.619  -32.223 1.00 50.28  ? 352 ALA A C      1 
ATOM   107  O O      . ALA A 1 13  ? -32.378 28.649  -31.545 1.00 55.53  ? 352 ALA A O      1 
ATOM   108  C CB     . ALA A 1 13  ? -31.874 25.487  -31.050 1.00 42.75  ? 352 ALA A CB     1 
ATOM   109  N N      . THR A 1 14  ? -32.130 27.578  -33.507 1.00 45.09  ? 353 THR A N      1 
ATOM   110  C CA     . THR A 1 14  ? -31.556 28.718  -34.208 1.00 45.49  ? 353 THR A CA     1 
ATOM   111  C C      . THR A 1 14  ? -32.589 29.494  -35.015 1.00 49.26  ? 353 THR A C      1 
ATOM   112  O O      . THR A 1 14  ? -32.211 30.325  -35.849 1.00 54.06  ? 353 THR A O      1 
ATOM   113  C CB     . THR A 1 14  ? -30.422 28.255  -35.126 1.00 44.67  ? 353 THR A CB     1 
ATOM   114  O OG1    . THR A 1 14  ? -30.951 27.399  -36.146 1.00 49.48  ? 353 THR A OG1    1 
ATOM   115  C CG2    . THR A 1 14  ? -29.370 27.493  -34.335 1.00 42.38  ? 353 THR A CG2    1 
ATOM   116  N N      . ASN A 1 15  ? -33.877 29.252  -34.783 1.00 47.22  ? 354 ASN A N      1 
ATOM   117  C CA     . ASN A 1 15  ? -34.944 29.863  -35.573 1.00 49.35  ? 354 ASN A CA     1 
ATOM   118  C C      . ASN A 1 15  ? -34.691 29.665  -37.063 1.00 49.86  ? 354 ASN A C      1 
ATOM   119  O O      . ASN A 1 15  ? -34.799 30.590  -37.869 1.00 52.72  ? 354 ASN A O      1 
ATOM   120  C CB     . ASN A 1 15  ? -35.099 31.346  -35.239 1.00 53.42  ? 354 ASN A CB     1 
ATOM   121  C CG     . ASN A 1 15  ? -35.927 31.579  -33.993 1.00 56.77  ? 354 ASN A CG     1 
ATOM   122  O OD1    . ASN A 1 15  ? -35.956 30.745  -33.089 1.00 53.50  ? 354 ASN A OD1    1 
ATOM   123  N ND2    . ASN A 1 15  ? -36.613 32.716  -33.943 1.00 55.53  ? 354 ASN A ND2    1 
ATOM   124  N N      . PHE A 1 16  ? -34.350 28.430  -37.427 1.00 46.48  ? 355 PHE A N      1 
ATOM   125  C CA     . PHE A 1 16  ? -34.001 28.096  -38.804 1.00 46.83  ? 355 PHE A CA     1 
ATOM   126  C C      . PHE A 1 16  ? -32.871 28.994  -39.297 1.00 55.62  ? 355 PHE A C      1 
ATOM   127  O O      . PHE A 1 16  ? -32.863 29.459  -40.440 1.00 55.12  ? 355 PHE A O      1 
ATOM   128  C CB     . PHE A 1 16  ? -35.229 28.178  -39.713 1.00 49.58  ? 355 PHE A CB     1 
ATOM   129  C CG     . PHE A 1 16  ? -36.298 27.180  -39.361 1.00 50.85  ? 355 PHE A CG     1 
ATOM   130  C CD1    . PHE A 1 16  ? -37.094 27.366  -38.242 1.00 51.22  ? 355 PHE A CD1    1 
ATOM   131  C CD2    . PHE A 1 16  ? -36.492 26.047  -40.131 1.00 51.89  ? 355 PHE A CD2    1 
ATOM   132  C CE1    . PHE A 1 16  ? -38.067 26.445  -37.904 1.00 52.64  ? 355 PHE A CE1    1 
ATOM   133  C CE2    . PHE A 1 16  ? -37.463 25.124  -39.799 1.00 53.25  ? 355 PHE A CE2    1 
ATOM   134  C CZ     . PHE A 1 16  ? -38.252 25.323  -38.685 1.00 53.64  ? 355 PHE A CZ     1 
ATOM   135  N N      . PHE A 1 17  ? -31.901 29.232  -38.413 1.00 55.55  ? 356 PHE A N      1 
ATOM   136  C CA     . PHE A 1 17  ? -30.733 30.054  -38.716 1.00 49.62  ? 356 PHE A CA     1 
ATOM   137  C C      . PHE A 1 17  ? -31.168 31.437  -39.206 1.00 55.47  ? 356 PHE A C      1 
ATOM   138  O O      . PHE A 1 17  ? -30.815 31.888  -40.297 1.00 61.98  ? 356 PHE A O      1 
ATOM   139  C CB     . PHE A 1 17  ? -29.829 29.343  -39.728 1.00 44.13  ? 356 PHE A CB     1 
ATOM   140  C CG     . PHE A 1 17  ? -29.392 27.976  -39.278 1.00 44.51  ? 356 PHE A CG     1 
ATOM   141  C CD1    . PHE A 1 17  ? -28.257 27.820  -38.501 1.00 42.74  ? 356 PHE A CD1    1 
ATOM   142  C CD2    . PHE A 1 17  ? -30.126 26.849  -39.614 1.00 45.06  ? 356 PHE A CD2    1 
ATOM   143  C CE1    . PHE A 1 17  ? -27.854 26.566  -38.077 1.00 39.05  ? 356 PHE A CE1    1 
ATOM   144  C CE2    . PHE A 1 17  ? -29.728 25.592  -39.193 1.00 44.64  ? 356 PHE A CE2    1 
ATOM   145  C CZ     . PHE A 1 17  ? -28.590 25.452  -38.423 1.00 39.56  ? 356 PHE A CZ     1 
ATOM   146  N N      . SER A 1 18  ? -31.934 32.110  -38.354 1.00 78.69  ? 357 SER A N      1 
ATOM   147  C CA     . SER A 1 18  ? -32.667 33.332  -38.693 1.00 85.17  ? 357 SER A CA     1 
ATOM   148  C C      . SER A 1 18  ? -31.917 34.589  -38.271 1.00 87.06  ? 357 SER A C      1 
ATOM   149  O O      . SER A 1 18  ? -32.464 35.418  -37.552 1.00 87.30  ? 357 SER A O      1 
ATOM   150  C CB     . SER A 1 18  ? -34.038 33.300  -38.036 1.00 84.61  ? 357 SER A CB     1 
ATOM   151  O OG     . SER A 1 18  ? -33.908 33.469  -36.634 1.00 84.43  ? 357 SER A OG     1 
ATOM   152  N N      . GLU A 1 19  ? -30.664 34.765  -38.690 1.00 64.57  ? 358 GLU A N      1 
ATOM   153  C CA     . GLU A 1 19  ? -29.849 35.896  -38.231 1.00 55.72  ? 358 GLU A CA     1 
ATOM   154  C C      . GLU A 1 19  ? -29.881 36.024  -36.706 1.00 60.80  ? 358 GLU A C      1 
ATOM   155  O O      . GLU A 1 19  ? -29.729 37.118  -36.148 1.00 61.89  ? 358 GLU A O      1 
ATOM   156  C CB     . GLU A 1 19  ? -30.286 37.197  -38.903 1.00 59.59  ? 358 GLU A CB     1 
ATOM   157  C CG     . GLU A 1 19  ? -30.294 37.120  -40.417 1.00 62.28  ? 358 GLU A CG     1 
ATOM   158  C CD     . GLU A 1 19  ? -28.904 37.180  -41.014 1.00 57.20  ? 358 GLU A CD     1 
ATOM   159  O OE1    . GLU A 1 19  ? -28.205 38.184  -40.775 1.00 59.40  ? 358 GLU A OE1    1 
ATOM   160  O OE2    . GLU A 1 19  ? -28.505 36.233  -41.724 1.00 53.65  ? 358 GLU A OE2    1 
ATOM   161  N N      . GLU A 1 20  ? -30.110 34.891  -36.031 1.00 64.80  ? 359 GLU A N      1 
ATOM   162  C CA     . GLU A 1 20  ? -29.657 34.660  -34.665 1.00 55.71  ? 359 GLU A CA     1 
ATOM   163  C C      . GLU A 1 20  ? -28.164 34.398  -34.618 1.00 53.33  ? 359 GLU A C      1 
ATOM   164  O O      . GLU A 1 20  ? -27.631 34.051  -33.558 1.00 55.55  ? 359 GLU A O      1 
ATOM   165  C CB     . GLU A 1 20  ? -30.390 33.471  -34.037 1.00 53.83  ? 359 GLU A CB     1 
ATOM   166  C CG     . GLU A 1 20  ? -31.843 33.708  -33.702 1.00 62.49  ? 359 GLU A CG     1 
ATOM   167  C CD     . GLU A 1 20  ? -32.425 32.546  -32.932 1.00 71.94  ? 359 GLU A CD     1 
ATOM   168  O OE1    . GLU A 1 20  ? -31.659 31.617  -32.600 1.00 62.08  ? 359 GLU A OE1    1 
ATOM   169  O OE2    . GLU A 1 20  ? -33.639 32.557  -32.656 1.00 72.43  ? 359 GLU A OE2    1 
ATOM   170  N N      . ASN A 1 21  ? -27.487 34.580  -35.749 1.00 51.74  ? 360 ASN A N      1 
ATOM   171  C CA     . ASN A 1 21  ? -26.082 34.238  -35.865 1.00 50.27  ? 360 ASN A CA     1 
ATOM   172  C C      . ASN A 1 21  ? -25.223 35.222  -35.090 1.00 51.49  ? 360 ASN A C      1 
ATOM   173  O O      . ASN A 1 21  ? -25.478 36.429  -35.090 1.00 49.52  ? 360 ASN A O      1 
ATOM   174  C CB     . ASN A 1 21  ? -25.664 34.245  -37.333 1.00 46.12  ? 360 ASN A CB     1 
ATOM   175  C CG     . ASN A 1 21  ? -25.592 35.655  -37.913 1.00 58.34  ? 360 ASN A CG     1 
ATOM   176  O OD1    . ASN A 1 21  ? -26.400 36.525  -37.574 1.00 65.60  ? 360 ASN A OD1    1 
ATOM   177  N ND2    . ASN A 1 21  ? -24.615 35.888  -38.783 1.00 60.67  ? 360 ASN A ND2    1 
ATOM   178  N N      . LYS A 1 22  ? -24.207 34.696  -34.416 1.00 49.87  ? 361 LYS A N      1 
ATOM   179  C CA     . LYS A 1 22  ? -23.090 35.528  -34.011 1.00 55.66  ? 361 LYS A CA     1 
ATOM   180  C C      . LYS A 1 22  ? -22.350 36.007  -35.261 1.00 59.72  ? 361 LYS A C      1 
ATOM   181  O O      . LYS A 1 22  ? -22.720 35.689  -36.397 1.00 65.00  ? 361 LYS A O      1 
ATOM   182  C CB     . LYS A 1 22  ? -22.177 34.761  -33.056 1.00 50.77  ? 361 LYS A CB     1 
ATOM   183  C CG     . LYS A 1 22  ? -22.548 34.908  -31.583 1.00 52.89  ? 361 LYS A CG     1 
ATOM   184  C CD     . LYS A 1 22  ? -22.052 36.237  -31.037 1.00 55.43  ? 361 LYS A CD     1 
ATOM   185  C CE     . LYS A 1 22  ? -21.538 36.100  -29.609 1.00 50.69  ? 361 LYS A CE     1 
ATOM   186  N NZ     . LYS A 1 22  ? -22.627 35.941  -28.603 1.00 62.44  ? 361 LYS A NZ     1 
ATOM   187  N N      . ILE A 1 23  ? -21.284 36.781  -35.048 1.00 63.57  ? 362 ILE A N      1 
ATOM   188  C CA     . ILE A 1 23  ? -20.610 37.453  -36.161 1.00 66.29  ? 362 ILE A CA     1 
ATOM   189  C C      . ILE A 1 23  ? -20.257 36.458  -37.261 1.00 68.45  ? 362 ILE A C      1 
ATOM   190  O O      . ILE A 1 23  ? -20.648 36.624  -38.422 1.00 75.56  ? 362 ILE A O      1 
ATOM   191  C CB     . ILE A 1 23  ? -19.367 38.210  -35.664 1.00 69.45  ? 362 ILE A CB     1 
ATOM   192  C CG1    . ILE A 1 23  ? -19.771 39.215  -34.583 1.00 70.64  ? 362 ILE A CG1    1 
ATOM   193  C CG2    . ILE A 1 23  ? -18.677 38.914  -36.830 1.00 80.80  ? 362 ILE A CG2    1 
ATOM   194  C CD1    . ILE A 1 23  ? -18.939 40.475  -34.590 1.00 66.18  ? 362 ILE A CD1    1 
ATOM   195  N N      . LYS A 1 24  ? -19.509 35.414  -36.912 1.00 68.84  ? 363 LYS A N      1 
ATOM   196  C CA     . LYS A 1 24  ? -19.088 34.434  -37.905 1.00 77.69  ? 363 LYS A CA     1 
ATOM   197  C C      . LYS A 1 24  ? -20.293 33.874  -38.650 1.00 70.56  ? 363 LYS A C      1 
ATOM   198  O O      . LYS A 1 24  ? -21.314 33.535  -38.047 1.00 74.97  ? 363 LYS A O      1 
ATOM   199  C CB     . LYS A 1 24  ? -18.313 33.299  -37.235 1.00 86.68  ? 363 LYS A CB     1 
ATOM   200  C CG     . LYS A 1 24  ? -17.794 32.240  -38.194 1.00 77.76  ? 363 LYS A CG     1 
ATOM   201  C CD     . LYS A 1 24  ? -16.371 32.530  -38.654 1.00 75.54  ? 363 LYS A CD     1 
ATOM   202  C CE     . LYS A 1 24  ? -15.751 31.314  -39.340 1.00 70.33  ? 363 LYS A CE     1 
ATOM   203  N NZ     . LYS A 1 24  ? -16.382 31.000  -40.652 1.00 67.19  ? 363 LYS A NZ     1 
ATOM   204  N N      . GLY A 1 25  ? -20.171 33.793  -39.977 1.00 58.42  ? 364 GLY A N      1 
ATOM   205  C CA     . GLY A 1 25  ? -21.237 33.221  -40.781 1.00 60.88  ? 364 GLY A CA     1 
ATOM   206  C C      . GLY A 1 25  ? -21.622 31.816  -40.360 1.00 58.49  ? 364 GLY A C      1 
ATOM   207  O O      . GLY A 1 25  ? -22.795 31.442  -40.440 1.00 64.90  ? 364 GLY A O      1 
ATOM   208  N N      . SER A 1 26  ? -20.649 31.017  -39.916 1.00 54.60  ? 365 SER A N      1 
ATOM   209  C CA     . SER A 1 26  ? -20.892 29.645  -39.485 1.00 50.37  ? 365 SER A CA     1 
ATOM   210  C C      . SER A 1 26  ? -21.311 29.532  -38.024 1.00 45.24  ? 365 SER A C      1 
ATOM   211  O O      . SER A 1 26  ? -21.677 28.436  -37.585 1.00 43.07  ? 365 SER A O      1 
ATOM   212  C CB     . SER A 1 26  ? -19.638 28.790  -39.720 1.00 52.25  ? 365 SER A CB     1 
ATOM   213  O OG     . SER A 1 26  ? -18.469 29.444  -39.252 1.00 58.63  ? 365 SER A OG     1 
ATOM   214  N N      . VAL A 1 27  ? -21.272 30.625  -37.267 1.00 48.11  ? 366 VAL A N      1 
ATOM   215  C CA     . VAL A 1 27  ? -21.511 30.602  -35.828 1.00 47.73  ? 366 VAL A CA     1 
ATOM   216  C C      . VAL A 1 27  ? -22.904 31.148  -35.552 1.00 43.48  ? 366 VAL A C      1 
ATOM   217  O O      . VAL A 1 27  ? -23.194 32.315  -35.843 1.00 45.84  ? 366 VAL A O      1 
ATOM   218  C CB     . VAL A 1 27  ? -20.444 31.406  -35.070 1.00 45.93  ? 366 VAL A CB     1 
ATOM   219  C CG1    . VAL A 1 27  ? -20.782 31.463  -33.586 1.00 48.22  ? 366 VAL A CG1    1 
ATOM   220  C CG2    . VAL A 1 27  ? -19.070 30.791  -35.287 1.00 47.70  ? 366 VAL A CG2    1 
ATOM   221  N N      . TYR A 1 28  ? -23.761 30.305  -34.982 1.00 35.15  ? 367 TYR A N      1 
ATOM   222  C CA     . TYR A 1 28  ? -25.107 30.680  -34.580 1.00 39.03  ? 367 TYR A CA     1 
ATOM   223  C C      . TYR A 1 28  ? -25.307 30.384  -33.100 1.00 40.57  ? 367 TYR A C      1 
ATOM   224  O O      . TYR A 1 28  ? -24.641 29.517  -32.527 1.00 40.12  ? 367 TYR A O      1 
ATOM   225  C CB     . TYR A 1 28  ? -26.165 29.929  -35.401 1.00 40.58  ? 367 TYR A CB     1 
ATOM   226  C CG     . TYR A 1 28  ? -26.183 30.302  -36.863 1.00 39.93  ? 367 TYR A CG     1 
ATOM   227  C CD1    . TYR A 1 28  ? -25.270 29.752  -37.752 1.00 38.98  ? 367 TYR A CD1    1 
ATOM   228  C CD2    . TYR A 1 28  ? -27.115 31.203  -37.356 1.00 43.00  ? 367 TYR A CD2    1 
ATOM   229  C CE1    . TYR A 1 28  ? -25.282 30.093  -39.090 1.00 39.51  ? 367 TYR A CE1    1 
ATOM   230  C CE2    . TYR A 1 28  ? -27.135 31.549  -38.691 1.00 47.10  ? 367 TYR A CE2    1 
ATOM   231  C CZ     . TYR A 1 28  ? -26.218 30.992  -39.554 1.00 43.98  ? 367 TYR A CZ     1 
ATOM   232  O OH     . TYR A 1 28  ? -26.240 31.340  -40.886 1.00 44.67  ? 367 TYR A OH     1 
ATOM   233  N N      . ARG A 1 29  ? -26.233 31.118  -32.488 1.00 40.39  ? 368 ARG A N      1 
ATOM   234  C CA     . ARG A 1 29  ? -26.643 30.881  -31.110 1.00 41.67  ? 368 ARG A CA     1 
ATOM   235  C C      . ARG A 1 29  ? -27.879 29.992  -31.112 1.00 43.93  ? 368 ARG A C      1 
ATOM   236  O O      . ARG A 1 29  ? -28.887 30.323  -31.746 1.00 43.96  ? 368 ARG A O      1 
ATOM   237  C CB     . ARG A 1 29  ? -26.932 32.192  -30.378 1.00 34.01  ? 368 ARG A CB     1 
ATOM   238  C CG     . ARG A 1 29  ? -27.365 31.982  -28.939 1.00 39.84  ? 368 ARG A CG     1 
ATOM   239  C CD     . ARG A 1 29  ? -27.410 33.283  -28.165 1.00 39.95  ? 368 ARG A CD     1 
ATOM   240  N NE     . ARG A 1 29  ? -27.646 33.052  -26.745 1.00 47.92  ? 368 ARG A NE     1 
ATOM   241  C CZ     . ARG A 1 29  ? -27.594 33.997  -25.816 1.00 62.87  ? 368 ARG A CZ     1 
ATOM   242  N NH1    . ARG A 1 29  ? -27.317 35.254  -26.123 1.00 64.79  ? 368 ARG A NH1    1 
ATOM   243  N NH2    . ARG A 1 29  ? -27.821 33.672  -24.546 1.00 55.22  ? 368 ARG A NH2    1 
ATOM   244  N N      . ALA A 1 30  ? -27.794 28.866  -30.411 1.00 42.54  ? 369 ALA A N      1 
ATOM   245  C CA     . ALA A 1 30  ? -28.905 27.938  -30.258 1.00 48.42  ? 369 ALA A CA     1 
ATOM   246  C C      . ALA A 1 30  ? -29.446 28.064  -28.841 1.00 53.40  ? 369 ALA A C      1 
ATOM   247  O O      . ALA A 1 30  ? -28.718 27.825  -27.872 1.00 49.13  ? 369 ALA A O      1 
ATOM   248  C CB     . ALA A 1 30  ? -28.467 26.502  -30.544 1.00 44.04  ? 369 ALA A CB     1 
ATOM   249  N N      . SER A 1 31  ? -30.712 28.450  -28.726 1.00 70.21  ? 370 SER A N      1 
ATOM   250  C CA     . SER A 1 31  ? -31.391 28.558  -27.440 1.00 68.97  ? 370 SER A CA     1 
ATOM   251  C C      . SER A 1 31  ? -32.340 27.373  -27.316 1.00 71.38  ? 370 SER A C      1 
ATOM   252  O O      . SER A 1 31  ? -33.342 27.295  -28.034 1.00 83.79  ? 370 SER A O      1 
ATOM   253  C CB     . SER A 1 31  ? -32.140 29.884  -27.329 1.00 71.61  ? 370 SER A CB     1 
ATOM   254  O OG     . SER A 1 31  ? -33.117 30.000  -28.349 1.00 73.08  ? 370 SER A OG     1 
ATOM   255  N N      . PHE A 1 32  ? -32.021 26.450  -26.414 1.00 61.05  ? 371 PHE A N      1 
ATOM   256  C CA     . PHE A 1 32  ? -32.794 25.222  -26.292 1.00 61.33  ? 371 PHE A CA     1 
ATOM   257  C C      . PHE A 1 32  ? -32.302 24.451  -25.079 1.00 67.15  ? 371 PHE A C      1 
ATOM   258  O O      . PHE A 1 32  ? -31.176 24.646  -24.612 1.00 73.73  ? 371 PHE A O      1 
ATOM   259  C CB     . PHE A 1 32  ? -32.674 24.361  -27.552 1.00 57.12  ? 371 PHE A CB     1 
ATOM   260  C CG     . PHE A 1 32  ? -31.300 23.795  -27.765 1.00 57.32  ? 371 PHE A CG     1 
ATOM   261  C CD1    . PHE A 1 32  ? -30.285 24.583  -28.277 1.00 56.38  ? 371 PHE A CD1    1 
ATOM   262  C CD2    . PHE A 1 32  ? -31.024 22.476  -27.452 1.00 67.28  ? 371 PHE A CD2    1 
ATOM   263  C CE1    . PHE A 1 32  ? -29.020 24.066  -28.473 1.00 53.78  ? 371 PHE A CE1    1 
ATOM   264  C CE2    . PHE A 1 32  ? -29.761 21.953  -27.646 1.00 65.47  ? 371 PHE A CE2    1 
ATOM   265  C CZ     . PHE A 1 32  ? -28.758 22.749  -28.158 1.00 55.60  ? 371 PHE A CZ     1 
ATOM   266  N N      . LYS A 1 33  ? -33.162 23.562  -24.580 1.00 65.00  ? 372 LYS A N      1 
ATOM   267  C CA     . LYS A 1 33  ? -32.813 22.670  -23.476 1.00 68.31  ? 372 LYS A CA     1 
ATOM   268  C C      . LYS A 1 33  ? -32.323 23.450  -22.259 1.00 72.03  ? 372 LYS A C      1 
ATOM   269  O O      . LYS A 1 33  ? -31.442 22.994  -21.526 1.00 75.79  ? 372 LYS A O      1 
ATOM   270  C CB     . LYS A 1 33  ? -31.766 21.643  -23.919 1.00 70.62  ? 372 LYS A CB     1 
ATOM   271  C CG     . LYS A 1 33  ? -31.491 20.535  -22.920 1.00 88.78  ? 372 LYS A CG     1 
ATOM   272  C CD     . LYS A 1 33  ? -30.400 19.610  -23.435 1.00 95.26  ? 372 LYS A CD     1 
ATOM   273  C CE     . LYS A 1 33  ? -30.073 18.525  -22.426 1.00 92.71  ? 372 LYS A CE     1 
ATOM   274  N NZ     . LYS A 1 33  ? -28.969 17.643  -22.894 1.00 90.73  ? 372 LYS A NZ     1 
ATOM   275  N N      . GLY A 1 34  ? -32.890 24.633  -22.038 1.00 70.20  ? 373 GLY A N      1 
ATOM   276  C CA     . GLY A 1 34  ? -32.462 25.482  -20.945 1.00 58.23  ? 373 GLY A CA     1 
ATOM   277  C C      . GLY A 1 34  ? -31.105 26.109  -21.186 1.00 61.53  ? 373 GLY A C      1 
ATOM   278  O O      . GLY A 1 34  ? -30.995 27.328  -21.348 1.00 61.12  ? 373 GLY A O      1 
ATOM   279  N N      . ASP A 1 35  ? -30.064 25.281  -21.220 1.00 66.48  ? 374 ASP A N      1 
ATOM   280  C CA     . ASP A 1 35  ? -28.702 25.764  -21.410 1.00 63.45  ? 374 ASP A CA     1 
ATOM   281  C C      . ASP A 1 35  ? -28.479 26.094  -22.882 1.00 54.45  ? 374 ASP A C      1 
ATOM   282  O O      . ASP A 1 35  ? -28.663 25.235  -23.751 1.00 52.64  ? 374 ASP A O      1 
ATOM   283  C CB     . ASP A 1 35  ? -27.699 24.719  -20.929 1.00 60.43  ? 374 ASP A CB     1 
ATOM   284  C CG     . ASP A 1 35  ? -26.288 25.263  -20.836 1.00 65.56  ? 374 ASP A CG     1 
ATOM   285  O OD1    . ASP A 1 35  ? -26.100 26.475  -21.072 1.00 81.57  ? 374 ASP A OD1    1 
ATOM   286  O OD2    . ASP A 1 35  ? -25.367 24.477  -20.526 1.00 68.08  ? 374 ASP A OD2    1 
ATOM   287  N N      . ASP A 1 36  ? -28.083 27.334  -23.161 1.00 48.17  ? 375 ASP A N      1 
ATOM   288  C CA     . ASP A 1 36  ? -27.845 27.752  -24.533 1.00 46.30  ? 375 ASP A CA     1 
ATOM   289  C C      . ASP A 1 36  ? -26.553 27.136  -25.067 1.00 43.06  ? 375 ASP A C      1 
ATOM   290  O O      . ASP A 1 36  ? -25.727 26.596  -24.325 1.00 45.76  ? 375 ASP A O      1 
ATOM   291  C CB     . ASP A 1 36  ? -27.784 29.276  -24.631 1.00 47.50  ? 375 ASP A CB     1 
ATOM   292  C CG     . ASP A 1 36  ? -29.159 29.915  -24.647 1.00 56.09  ? 375 ASP A CG     1 
ATOM   293  O OD1    . ASP A 1 36  ? -30.154 29.198  -24.406 1.00 58.42  ? 375 ASP A OD1    1 
ATOM   294  O OD2    . ASP A 1 36  ? -29.247 31.134  -24.908 1.00 51.02  ? 375 ASP A OD2    1 
ATOM   295  N N      . ALA A 1 37  ? -26.382 27.229  -26.383 1.00 37.16  ? 376 ALA A N      1 
ATOM   296  C CA     . ALA A 1 37  ? -25.215 26.670  -27.046 1.00 37.77  ? 376 ALA A CA     1 
ATOM   297  C C      . ALA A 1 37  ? -24.903 27.498  -28.284 1.00 35.97  ? 376 ALA A C      1 
ATOM   298  O O      . ALA A 1 37  ? -25.651 28.404  -28.659 1.00 38.36  ? 376 ALA A O      1 
ATOM   299  C CB     . ALA A 1 37  ? -25.433 25.199  -27.419 1.00 35.34  ? 376 ALA A CB     1 
ATOM   300  N N      . ALA A 1 38  ? -23.778 27.174  -28.914 1.00 32.31  ? 377 ALA A N      1 
ATOM   301  C CA     . ALA A 1 38  ? -23.359 27.792  -30.164 1.00 30.05  ? 377 ALA A CA     1 
ATOM   302  C C      . ALA A 1 38  ? -23.208 26.708  -31.219 1.00 34.74  ? 377 ALA A C      1 
ATOM   303  O O      . ALA A 1 38  ? -22.573 25.678  -30.968 1.00 35.40  ? 377 ALA A O      1 
ATOM   304  C CB     . ALA A 1 38  ? -22.046 28.558  -29.994 1.00 26.47  ? 377 ALA A CB     1 
ATOM   305  N N      . VAL A 1 39  ? -23.797 26.936  -32.389 1.00 35.71  ? 378 VAL A N      1 
ATOM   306  C CA     . VAL A 1 39  ? -23.764 25.987  -33.495 1.00 33.77  ? 378 VAL A CA     1 
ATOM   307  C C      . VAL A 1 39  ? -22.841 26.536  -34.573 1.00 34.33  ? 378 VAL A C      1 
ATOM   308  O O      . VAL A 1 39  ? -22.991 27.687  -35.001 1.00 32.86  ? 378 VAL A O      1 
ATOM   309  C CB     . VAL A 1 39  ? -25.171 25.725  -34.059 1.00 36.84  ? 378 VAL A CB     1 
ATOM   310  C CG1    . VAL A 1 39  ? -25.115 24.670  -35.154 1.00 42.42  ? 378 VAL A CG1    1 
ATOM   311  C CG2    . VAL A 1 39  ? -26.119 25.303  -32.949 1.00 38.65  ? 378 VAL A CG2    1 
ATOM   312  N N      . LYS A 1 40  ? -21.888 25.716  -35.004 1.00 35.90  ? 379 LYS A N      1 
ATOM   313  C CA     . LYS A 1 40  ? -20.959 26.061  -36.072 1.00 38.83  ? 379 LYS A CA     1 
ATOM   314  C C      . LYS A 1 40  ? -21.218 25.145  -37.259 1.00 42.89  ? 379 LYS A C      1 
ATOM   315  O O      . LYS A 1 40  ? -21.126 23.919  -37.131 1.00 41.09  ? 379 LYS A O      1 
ATOM   316  C CB     . LYS A 1 40  ? -19.510 25.934  -35.604 1.00 37.33  ? 379 LYS A CB     1 
ATOM   317  C CG     . LYS A 1 40  ? -18.506 25.868  -36.744 1.00 45.44  ? 379 LYS A CG     1 
ATOM   318  C CD     . LYS A 1 40  ? -17.103 25.585  -36.231 1.00 46.89  ? 379 LYS A CD     1 
ATOM   319  C CE     . LYS A 1 40  ? -16.509 26.802  -35.548 1.00 44.93  ? 379 LYS A CE     1 
ATOM   320  N NZ     . LYS A 1 40  ? -16.361 27.942  -36.498 1.00 52.84  ? 379 LYS A NZ     1 
ATOM   321  N N      . ILE A 1 41  ? -21.542 25.737  -38.405 1.00 45.26  ? 380 ILE A N      1 
ATOM   322  C CA     . ILE A 1 41  ? -21.785 24.986  -39.631 1.00 45.31  ? 380 ILE A CA     1 
ATOM   323  C C      . ILE A 1 41  ? -20.469 24.843  -40.383 1.00 43.18  ? 380 ILE A C      1 
ATOM   324  O O      . ILE A 1 41  ? -19.743 25.826  -40.575 1.00 44.55  ? 380 ILE A O      1 
ATOM   325  C CB     . ILE A 1 41  ? -22.844 25.681  -40.503 1.00 40.16  ? 380 ILE A CB     1 
ATOM   326  C CG1    . ILE A 1 41  ? -24.098 25.984  -39.682 1.00 42.97  ? 380 ILE A CG1    1 
ATOM   327  C CG2    . ILE A 1 41  ? -23.190 24.820  -41.706 1.00 45.99  ? 380 ILE A CG2    1 
ATOM   328  C CD1    . ILE A 1 41  ? -25.170 26.720  -40.460 1.00 43.42  ? 380 ILE A CD1    1 
ATOM   329  N N      . LEU A 1 42  ? -20.158 23.621  -40.809 1.00 44.69  ? 381 LEU A N      1 
ATOM   330  C CA     . LEU A 1 42  ? -18.931 23.339  -41.539 1.00 44.34  ? 381 LEU A CA     1 
ATOM   331  C C      . LEU A 1 42  ? -19.244 22.500  -42.768 1.00 52.10  ? 381 LEU A C      1 
ATOM   332  O O      . LEU A 1 42  ? -20.079 21.591  -42.717 1.00 52.04  ? 381 LEU A O      1 
ATOM   333  C CB     . LEU A 1 42  ? -17.906 22.618  -40.652 1.00 45.52  ? 381 LEU A CB     1 
ATOM   334  C CG     . LEU A 1 42  ? -17.377 23.423  -39.462 1.00 43.38  ? 381 LEU A CG     1 
ATOM   335  C CD1    . LEU A 1 42  ? -16.354 22.621  -38.674 1.00 43.23  ? 381 LEU A CD1    1 
ATOM   336  C CD2    . LEU A 1 42  ? -16.783 24.745  -39.927 1.00 38.08  ? 381 LEU A CD2    1 
ATOM   337  N N      . LYS A 1 43  ? -18.566 22.810  -43.871 1.00 51.87  ? 382 LYS A N      1 
ATOM   338  C CA     . LYS A 1 43  ? -18.806 22.117  -45.129 1.00 50.30  ? 382 LYS A CA     1 
ATOM   339  C C      . LYS A 1 43  ? -18.239 20.702  -45.086 1.00 51.79  ? 382 LYS A C      1 
ATOM   340  O O      . LYS A 1 43  ? -17.153 20.465  -44.548 1.00 48.31  ? 382 LYS A O      1 
ATOM   341  C CB     . LYS A 1 43  ? -18.182 22.900  -46.284 1.00 52.14  ? 382 LYS A CB     1 
ATOM   342  C CG     . LYS A 1 43  ? -18.187 22.179  -47.626 1.00 53.22  ? 382 LYS A CG     1 
ATOM   343  C CD     . LYS A 1 43  ? -19.580 22.119  -48.232 1.00 58.45  ? 382 LYS A CD     1 
ATOM   344  C CE     . LYS A 1 43  ? -19.536 21.574  -49.652 1.00 52.33  ? 382 LYS A CE     1 
ATOM   345  N NZ     . LYS A 1 43  ? -18.728 22.436  -50.561 1.00 53.88  ? 382 LYS A NZ     1 
ATOM   346  N N      . GLY A 1 44  ? -18.985 19.759  -45.658 1.00 49.35  ? 383 GLY A N      1 
ATOM   347  C CA     . GLY A 1 44  ? -18.540 18.382  -45.736 1.00 46.19  ? 383 GLY A CA     1 
ATOM   348  C C      . GLY A 1 44  ? -18.533 17.669  -44.400 1.00 48.60  ? 383 GLY A C      1 
ATOM   349  O O      . GLY A 1 44  ? -18.642 18.305  -43.348 1.00 48.82  ? 383 GLY A O      1 
ATOM   350  N N      . ASP A 1 45  ? -18.406 16.345  -44.427 1.00 47.16  ? 384 ASP A N      1 
ATOM   351  C CA     . ASP A 1 45  ? -18.348 15.554  -43.203 1.00 47.69  ? 384 ASP A CA     1 
ATOM   352  C C      . ASP A 1 45  ? -16.953 15.677  -42.605 1.00 46.27  ? 384 ASP A C      1 
ATOM   353  O O      . ASP A 1 45  ? -15.987 15.130  -43.144 1.00 44.36  ? 384 ASP A O      1 
ATOM   354  C CB     . ASP A 1 45  ? -18.697 14.095  -43.487 1.00 49.73  ? 384 ASP A CB     1 
ATOM   355  C CG     . ASP A 1 45  ? -18.847 13.273  -42.220 1.00 52.51  ? 384 ASP A CG     1 
ATOM   356  O OD1    . ASP A 1 45  ? -18.953 13.875  -41.131 1.00 52.07  ? 384 ASP A OD1    1 
ATOM   357  O OD2    . ASP A 1 45  ? -18.858 12.027  -42.311 1.00 48.05  ? 384 ASP A OD2    1 
ATOM   358  N N      . VAL A 1 46  ? -16.845 16.401  -41.494 1.00 47.84  ? 385 VAL A N      1 
ATOM   359  C CA     . VAL A 1 46  ? -15.577 16.547  -40.790 1.00 52.37  ? 385 VAL A CA     1 
ATOM   360  C C      . VAL A 1 46  ? -15.600 15.652  -39.559 1.00 51.03  ? 385 VAL A C      1 
ATOM   361  O O      . VAL A 1 46  ? -14.945 15.943  -38.551 1.00 49.72  ? 385 VAL A O      1 
ATOM   362  C CB     . VAL A 1 46  ? -15.312 18.015  -40.411 1.00 54.54  ? 385 VAL A CB     1 
ATOM   363  C CG1    . VAL A 1 46  ? -15.127 18.860  -41.661 1.00 47.29  ? 385 VAL A CG1    1 
ATOM   364  C CG2    . VAL A 1 46  ? -16.454 18.555  -39.569 1.00 55.77  ? 385 VAL A CG2    1 
ATOM   365  N N      . SER A 1 47  ? -16.354 14.553  -39.639 1.00 49.39  ? 386 SER A N      1 
ATOM   366  C CA     . SER A 1 47  ? -16.474 13.646  -38.502 1.00 53.07  ? 386 SER A CA     1 
ATOM   367  C C      . SER A 1 47  ? -15.120 13.064  -38.112 1.00 53.66  ? 386 SER A C      1 
ATOM   368  O O      . SER A 1 47  ? -14.832 12.881  -36.924 1.00 49.35  ? 386 SER A O      1 
ATOM   369  C CB     . SER A 1 47  ? -17.466 12.529  -38.831 1.00 54.45  ? 386 SER A CB     1 
ATOM   370  O OG     . SER A 1 47  ? -17.735 11.722  -37.697 1.00 74.35  ? 386 SER A OG     1 
ATOM   371  N N      . SER A 1 48  ? -14.273 12.771  -39.101 1.00 52.49  ? 387 SER A N      1 
ATOM   372  C CA     . SER A 1 48  ? -12.983 12.155  -38.813 1.00 50.23  ? 387 SER A CA     1 
ATOM   373  C C      . SER A 1 48  ? -12.120 13.053  -37.935 1.00 50.47  ? 387 SER A C      1 
ATOM   374  O O      . SER A 1 48  ? -11.466 12.576  -37.000 1.00 54.84  ? 387 SER A O      1 
ATOM   375  C CB     . SER A 1 48  ? -12.264 11.822  -40.119 1.00 52.34  ? 387 SER A CB     1 
ATOM   376  O OG     . SER A 1 48  ? -12.326 12.914  -41.019 1.00 57.72  ? 387 SER A OG     1 
ATOM   377  N N      . GLU A 1 49  ? -12.109 14.358  -38.214 1.00 52.10  ? 388 GLU A N      1 
ATOM   378  C CA     . GLU A 1 49  ? -11.297 15.273  -37.417 1.00 52.82  ? 388 GLU A CA     1 
ATOM   379  C C      . GLU A 1 49  ? -11.814 15.384  -35.988 1.00 47.58  ? 388 GLU A C      1 
ATOM   380  O O      . GLU A 1 49  ? -11.025 15.567  -35.054 1.00 48.73  ? 388 GLU A O      1 
ATOM   381  C CB     . GLU A 1 49  ? -11.257 16.653  -38.077 1.00 58.17  ? 388 GLU A CB     1 
ATOM   382  C CG     . GLU A 1 49  ? -10.456 16.712  -39.373 1.00 51.98  ? 388 GLU A CG     1 
ATOM   383  C CD     . GLU A 1 49  ? -11.141 15.999  -40.523 1.00 54.29  ? 388 GLU A CD     1 
ATOM   384  O OE1    . GLU A 1 49  ? -12.380 16.100  -40.637 1.00 48.45  ? 388 GLU A OE1    1 
ATOM   385  O OE2    . GLU A 1 49  ? -10.441 15.328  -41.308 1.00 60.54  ? 388 GLU A OE2    1 
ATOM   386  N N      . ILE A 1 50  ? -13.129 15.274  -35.799 1.00 51.12  ? 389 ILE A N      1 
ATOM   387  C CA     . ILE A 1 50  ? -13.699 15.395  -34.462 1.00 47.27  ? 389 ILE A CA     1 
ATOM   388  C C      . ILE A 1 50  ? -13.309 14.201  -33.600 1.00 46.47  ? 389 ILE A C      1 
ATOM   389  O O      . ILE A 1 50  ? -12.977 14.353  -32.418 1.00 44.76  ? 389 ILE A O      1 
ATOM   390  C CB     . ILE A 1 50  ? -15.226 15.555  -34.551 1.00 45.75  ? 389 ILE A CB     1 
ATOM   391  C CG1    . ILE A 1 50  ? -15.581 16.791  -35.379 1.00 44.93  ? 389 ILE A CG1    1 
ATOM   392  C CG2    . ILE A 1 50  ? -15.835 15.638  -33.160 1.00 45.00  ? 389 ILE A CG2    1 
ATOM   393  C CD1    . ILE A 1 50  ? -17.022 16.821  -35.841 1.00 45.46  ? 389 ILE A CD1    1 
ATOM   394  N N      . ASN A 1 51  ? -13.348 12.994  -34.171 1.00 43.36  ? 390 ASN A N      1 
ATOM   395  C CA     . ASN A 1 51  ? -13.004 11.798  -33.409 1.00 44.96  ? 390 ASN A CA     1 
ATOM   396  C C      . ASN A 1 51  ? -11.583 11.849  -32.866 1.00 43.90  ? 390 ASN A C      1 
ATOM   397  O O      . ASN A 1 51  ? -11.263 11.107  -31.930 1.00 44.57  ? 390 ASN A O      1 
ATOM   398  C CB     . ASN A 1 51  ? -13.193 10.552  -34.275 1.00 45.96  ? 390 ASN A CB     1 
ATOM   399  C CG     . ASN A 1 51  ? -14.627 10.375  -34.729 1.00 56.10  ? 390 ASN A CG     1 
ATOM   400  O OD1    . ASN A 1 51  ? -15.563 10.801  -34.049 1.00 55.27  ? 390 ASN A OD1    1 
ATOM   401  N ND2    . ASN A 1 51  ? -14.809 9.746   -35.886 1.00 54.98  ? 390 ASN A ND2    1 
ATOM   402  N N      . ILE A 1 52  ? -10.730 12.700  -33.429 1.00 39.94  ? 391 ILE A N      1 
ATOM   403  C CA     . ILE A 1 52  ? -9.378  12.899  -32.912 1.00 46.58  ? 391 ILE A CA     1 
ATOM   404  C C      . ILE A 1 52  ? -9.324  14.079  -31.952 1.00 42.49  ? 391 ILE A C      1 
ATOM   405  O O      . ILE A 1 52  ? -8.808  13.964  -30.837 1.00 40.96  ? 391 ILE A O      1 
ATOM   406  C CB     . ILE A 1 52  ? -8.381  13.084  -34.077 1.00 51.46  ? 391 ILE A CB     1 
ATOM   407  C CG1    . ILE A 1 52  ? -8.514  11.947  -35.090 1.00 47.42  ? 391 ILE A CG1    1 
ATOM   408  C CG2    . ILE A 1 52  ? -6.956  13.153  -33.545 1.00 46.94  ? 391 ILE A CG2    1 
ATOM   409  C CD1    . ILE A 1 52  ? -8.067  10.606  -34.564 1.00 48.34  ? 391 ILE A CD1    1 
ATOM   410  N N      . LEU A 1 53  ? -9.861  15.228  -32.368 1.00 40.29  ? 392 LEU A N      1 
ATOM   411  C CA     . LEU A 1 53  ? -9.808  16.426  -31.538 1.00 44.27  ? 392 LEU A CA     1 
ATOM   412  C C      . LEU A 1 53  ? -10.760 16.364  -30.350 1.00 39.46  ? 392 LEU A C      1 
ATOM   413  O O      . LEU A 1 53  ? -10.576 17.119  -29.389 1.00 40.31  ? 392 LEU A O      1 
ATOM   414  C CB     . LEU A 1 53  ? -10.113 17.663  -32.386 1.00 44.62  ? 392 LEU A CB     1 
ATOM   415  C CG     . LEU A 1 53  ? -9.050  18.033  -33.423 1.00 42.02  ? 392 LEU A CG     1 
ATOM   416  C CD1    . LEU A 1 53  ? -9.575  19.074  -34.400 1.00 40.44  ? 392 LEU A CD1    1 
ATOM   417  C CD2    . LEU A 1 53  ? -7.791  18.531  -32.732 1.00 38.08  ? 392 LEU A CD2    1 
ATOM   418  N N      . LYS A 1 54  ? -11.768 15.490  -30.388 1.00 38.33  ? 393 LYS A N      1 
ATOM   419  C CA     . LYS A 1 54  ? -12.679 15.369  -29.255 1.00 37.01  ? 393 LYS A CA     1 
ATOM   420  C C      . LYS A 1 54  ? -11.982 14.879  -27.994 1.00 38.74  ? 393 LYS A C      1 
ATOM   421  O O      . LYS A 1 54  ? -12.588 14.915  -26.917 1.00 39.63  ? 393 LYS A O      1 
ATOM   422  C CB     . LYS A 1 54  ? -13.840 14.434  -29.605 1.00 39.73  ? 393 LYS A CB     1 
ATOM   423  C CG     . LYS A 1 54  ? -13.453 12.972  -29.735 1.00 40.04  ? 393 LYS A CG     1 
ATOM   424  C CD     . LYS A 1 54  ? -14.658 12.128  -30.116 1.00 38.93  ? 393 LYS A CD     1 
ATOM   425  C CE     . LYS A 1 54  ? -14.382 10.645  -29.940 1.00 44.04  ? 393 LYS A CE     1 
ATOM   426  N NZ     . LYS A 1 54  ? -15.609 9.832   -30.182 1.00 50.52  ? 393 LYS A NZ     1 
ATOM   427  N N      . ARG A 1 55  ? -10.732 14.419  -28.098 1.00 35.69  ? 394 ARG A N      1 
ATOM   428  C CA     . ARG A 1 55  ? -9.976  14.055  -26.905 1.00 37.20  ? 394 ARG A CA     1 
ATOM   429  C C      . ARG A 1 55  ? -9.704  15.269  -26.026 1.00 35.68  ? 394 ARG A C      1 
ATOM   430  O O      . ARG A 1 55  ? -9.520  15.127  -24.812 1.00 32.57  ? 394 ARG A O      1 
ATOM   431  C CB     . ARG A 1 55  ? -8.656  13.394  -27.307 1.00 35.70  ? 394 ARG A CB     1 
ATOM   432  C CG     . ARG A 1 55  ? -7.597  14.378  -27.795 1.00 36.29  ? 394 ARG A CG     1 
ATOM   433  C CD     . ARG A 1 55  ? -6.506  13.681  -28.595 1.00 34.28  ? 394 ARG A CD     1 
ATOM   434  N NE     . ARG A 1 55  ? -5.304  14.498  -28.717 1.00 34.84  ? 394 ARG A NE     1 
ATOM   435  C CZ     . ARG A 1 55  ? -5.091  15.394  -29.672 1.00 38.47  ? 394 ARG A CZ     1 
ATOM   436  N NH1    . ARG A 1 55  ? -5.989  15.627  -30.617 1.00 41.65  ? 394 ARG A NH1    1 
ATOM   437  N NH2    . ARG A 1 55  ? -3.948  16.076  -29.679 1.00 33.74  ? 394 ARG A NH2    1 
ATOM   438  N N      . ILE A 1 56  ? -9.679  16.462  -26.619 1.00 36.64  ? 395 ILE A N      1 
ATOM   439  C CA     . ILE A 1 56  ? -9.315  17.691  -25.918 1.00 32.83  ? 395 ILE A CA     1 
ATOM   440  C C      . ILE A 1 56  ? -10.564 18.217  -25.216 1.00 31.66  ? 395 ILE A C      1 
ATOM   441  O O      . ILE A 1 56  ? -11.447 18.797  -25.849 1.00 35.60  ? 395 ILE A O      1 
ATOM   442  C CB     . ILE A 1 56  ? -8.726  18.733  -26.870 1.00 26.67  ? 395 ILE A CB     1 
ATOM   443  C CG1    . ILE A 1 56  ? -7.503  18.166  -27.594 1.00 34.91  ? 395 ILE A CG1    1 
ATOM   444  C CG2    . ILE A 1 56  ? -8.366  20.000  -26.109 1.00 31.55  ? 395 ILE A CG2    1 
ATOM   445  C CD1    . ILE A 1 56  ? -6.993  19.050  -28.708 1.00 34.55  ? 395 ILE A CD1    1 
ATOM   446  N N      . ASN A 1 57  ? -10.639 18.023  -23.902 1.00 32.06  ? 396 ASN A N      1 
ATOM   447  C CA     . ASN A 1 57  ? -11.695 18.604  -23.085 1.00 32.82  ? 396 ASN A CA     1 
ATOM   448  C C      . ASN A 1 57  ? -11.086 19.140  -21.799 1.00 31.07  ? 396 ASN A C      1 
ATOM   449  O O      . ASN A 1 57  ? -10.264 18.472  -21.167 1.00 33.50  ? 396 ASN A O      1 
ATOM   450  C CB     . ASN A 1 57  ? -12.803 17.588  -22.772 1.00 32.63  ? 396 ASN A CB     1 
ATOM   451  C CG     . ASN A 1 57  ? -12.270 16.186  -22.570 1.00 40.68  ? 396 ASN A CG     1 
ATOM   452  O OD1    . ASN A 1 57  ? -11.801 15.836  -21.487 1.00 64.98  ? 396 ASN A OD1    1 
ATOM   453  N ND2    . ASN A 1 57  ? -12.350 15.368  -23.615 1.00 40.30  ? 396 ASN A ND2    1 
ATOM   454  N N      . HIS A 1 58  ? -11.491 20.351  -21.421 1.00 25.00  ? 397 HIS A N      1 
ATOM   455  C CA     . HIS A 1 58  ? -10.890 21.041  -20.291 1.00 22.08  ? 397 HIS A CA     1 
ATOM   456  C C      . HIS A 1 58  ? -11.821 22.160  -19.847 1.00 21.58  ? 397 HIS A C      1 
ATOM   457  O O      . HIS A 1 58  ? -12.552 22.732  -20.659 1.00 21.38  ? 397 HIS A O      1 
ATOM   458  C CB     . HIS A 1 58  ? -9.510  21.593  -20.659 1.00 25.30  ? 397 HIS A CB     1 
ATOM   459  C CG     . HIS A 1 58  ? -8.748  22.146  -19.497 1.00 20.69  ? 397 HIS A CG     1 
ATOM   460  N ND1    . HIS A 1 58  ? -8.913  23.438  -19.047 1.00 19.72  ? 397 HIS A ND1    1 
ATOM   461  C CD2    . HIS A 1 58  ? -7.810  21.585  -18.698 1.00 21.39  ? 397 HIS A CD2    1 
ATOM   462  C CE1    . HIS A 1 58  ? -8.113  23.648  -18.018 1.00 24.93  ? 397 HIS A CE1    1 
ATOM   463  N NE2    . HIS A 1 58  ? -7.433  22.539  -17.785 1.00 25.70  ? 397 HIS A NE2    1 
ATOM   464  N N      . ALA A 1 59  ? -11.781 22.466  -18.548 1.00 21.78  ? 398 ALA A N      1 
ATOM   465  C CA     . ALA A 1 59  ? -12.696 23.456  -17.991 1.00 21.71  ? 398 ALA A CA     1 
ATOM   466  C C      . ALA A 1 59  ? -12.517 24.825  -18.634 1.00 20.38  ? 398 ALA A C      1 
ATOM   467  O O      . ALA A 1 59  ? -13.466 25.616  -18.681 1.00 20.44  ? 398 ALA A O      1 
ATOM   468  C CB     . ALA A 1 59  ? -12.505 23.554  -16.477 1.00 22.80  ? 398 ALA A CB     1 
ATOM   469  N N      . ASN A 1 60  ? -11.317 25.127  -19.132 1.00 20.12  ? 399 ASN A N      1 
ATOM   470  C CA     . ASN A 1 60  ? -11.031 26.417  -19.746 1.00 19.95  ? 399 ASN A CA     1 
ATOM   471  C C      . ASN A 1 60  ? -10.864 26.311  -21.259 1.00 21.83  ? 399 ASN A C      1 
ATOM   472  O O      . ASN A 1 60  ? -10.260 27.192  -21.881 1.00 19.72  ? 399 ASN A O      1 
ATOM   473  C CB     . ASN A 1 60  ? -9.791  27.041  -19.105 1.00 20.44  ? 399 ASN A CB     1 
ATOM   474  C CG     . ASN A 1 60  ? -9.935  27.206  -17.602 1.00 21.03  ? 399 ASN A CG     1 
ATOM   475  O OD1    . ASN A 1 60  ? -9.158  26.648  -16.828 1.00 21.74  ? 399 ASN A OD1    1 
ATOM   476  N ND2    . ASN A 1 60  ? -10.936 27.973  -17.182 1.00 20.04  ? 399 ASN A ND2    1 
ATOM   477  N N      . ILE A 1 61  ? -11.384 25.245  -21.861 1.00 23.90  ? 400 ILE A N      1 
ATOM   478  C CA     . ILE A 1 61  ? -11.426 25.078  -23.308 1.00 23.22  ? 400 ILE A CA     1 
ATOM   479  C C      . ILE A 1 61  ? -12.884 24.950  -23.720 1.00 23.21  ? 400 ILE A C      1 
ATOM   480  O O      . ILE A 1 61  ? -13.668 24.273  -23.045 1.00 22.24  ? 400 ILE A O      1 
ATOM   481  C CB     . ILE A 1 61  ? -10.616 23.848  -23.768 1.00 21.87  ? 400 ILE A CB     1 
ATOM   482  C CG1    . ILE A 1 61  ? -9.124  24.068  -23.510 1.00 22.51  ? 400 ILE A CG1    1 
ATOM   483  C CG2    . ILE A 1 61  ? -10.876 23.553  -25.237 1.00 24.13  ? 400 ILE A CG2    1 
ATOM   484  C CD1    . ILE A 1 61  ? -8.261  22.887  -23.891 1.00 20.73  ? 400 ILE A CD1    1 
ATOM   485  N N      . ILE A 1 62  ? -13.249 25.607  -24.821 1.00 22.25  ? 401 ILE A N      1 
ATOM   486  C CA     . ILE A 1 62  ? -14.643 25.605  -25.252 1.00 28.23  ? 401 ILE A CA     1 
ATOM   487  C C      . ILE A 1 62  ? -15.087 24.164  -25.475 1.00 31.23  ? 401 ILE A C      1 
ATOM   488  O O      . ILE A 1 62  ? -14.529 23.444  -26.313 1.00 32.89  ? 401 ILE A O      1 
ATOM   489  C CB     . ILE A 1 62  ? -14.825 26.473  -26.504 1.00 27.36  ? 401 ILE A CB     1 
ATOM   490  C CG1    . ILE A 1 62  ? -16.298 26.846  -26.678 1.00 26.01  ? 401 ILE A CG1    1 
ATOM   491  C CG2    . ILE A 1 62  ? -14.289 25.771  -27.742 1.00 25.28  ? 401 ILE A CG2    1 
ATOM   492  C CD1    . ILE A 1 62  ? -16.855 27.656  -25.526 1.00 23.27  ? 401 ILE A CD1    1 
ATOM   493  N N      . ARG A 1 63  ? -16.088 23.732  -24.711 1.00 28.49  ? 402 ARG A N      1 
ATOM   494  C CA     . ARG A 1 63  ? -16.492 22.333  -24.694 1.00 29.67  ? 402 ARG A CA     1 
ATOM   495  C C      . ARG A 1 63  ? -17.405 22.013  -25.869 1.00 31.56  ? 402 ARG A C      1 
ATOM   496  O O      . ARG A 1 63  ? -18.275 22.808  -26.232 1.00 32.36  ? 402 ARG A O      1 
ATOM   497  C CB     . ARG A 1 63  ? -17.199 22.003  -23.378 1.00 30.37  ? 402 ARG A CB     1 
ATOM   498  C CG     . ARG A 1 63  ? -17.448 20.520  -23.153 1.00 44.97  ? 402 ARG A CG     1 
ATOM   499  C CD     . ARG A 1 63  ? -18.154 20.276  -21.827 1.00 41.29  ? 402 ARG A CD     1 
ATOM   500  N NE     . ARG A 1 63  ? -19.530 19.835  -22.013 1.00 49.63  ? 402 ARG A NE     1 
ATOM   501  C CZ     . ARG A 1 63  ? -19.893 18.570  -22.180 1.00 62.04  ? 402 ARG A CZ     1 
ATOM   502  N NH1    . ARG A 1 63  ? -19.003 17.591  -22.190 1.00 67.70  ? 402 ARG A NH1    1 
ATOM   503  N NH2    . ARG A 1 63  ? -21.181 18.280  -22.345 1.00 54.57  ? 402 ARG A NH2    1 
ATOM   504  N N      . LEU A 1 64  ? -17.208 20.832  -26.454 1.00 33.47  ? 403 LEU A N      1 
ATOM   505  C CA     . LEU A 1 64  ? -17.999 20.365  -27.588 1.00 31.60  ? 403 LEU A CA     1 
ATOM   506  C C      . LEU A 1 64  ? -19.078 19.420  -27.074 1.00 36.48  ? 403 LEU A C      1 
ATOM   507  O O      . LEU A 1 64  ? -18.772 18.336  -26.565 1.00 45.05  ? 403 LEU A O      1 
ATOM   508  C CB     . LEU A 1 64  ? -17.112 19.676  -28.624 1.00 32.93  ? 403 LEU A CB     1 
ATOM   509  C CG     . LEU A 1 64  ? -17.834 19.039  -29.814 1.00 36.41  ? 403 LEU A CG     1 
ATOM   510  C CD1    . LEU A 1 64  ? -18.561 20.090  -30.641 1.00 38.79  ? 403 LEU A CD1    1 
ATOM   511  C CD2    . LEU A 1 64  ? -16.866 18.239  -30.678 1.00 41.37  ? 403 LEU A CD2    1 
ATOM   512  N N      . SER A 1 65  ? -20.340 19.835  -27.200 1.00 35.69  ? 404 SER A N      1 
ATOM   513  C CA     . SER A 1 65  ? -21.444 18.975  -26.785 1.00 35.19  ? 404 SER A CA     1 
ATOM   514  C C      . SER A 1 65  ? -21.600 17.793  -27.733 1.00 41.55  ? 404 SER A C      1 
ATOM   515  O O      . SER A 1 65  ? -21.705 16.642  -27.295 1.00 49.82  ? 404 SER A O      1 
ATOM   516  C CB     . SER A 1 65  ? -22.743 19.779  -26.711 1.00 36.46  ? 404 SER A CB     1 
ATOM   517  O OG     . SER A 1 65  ? -22.667 20.786  -25.718 1.00 42.55  ? 404 SER A OG     1 
ATOM   518  N N      . GLY A 1 66  ? -21.618 18.061  -29.032 1.00 40.25  ? 405 GLY A N      1 
ATOM   519  C CA     . GLY A 1 66  ? -21.777 17.005  -30.012 1.00 46.88  ? 405 GLY A CA     1 
ATOM   520  C C      . GLY A 1 66  ? -21.738 17.585  -31.407 1.00 44.32  ? 405 GLY A C      1 
ATOM   521  O O      . GLY A 1 66  ? -21.398 18.753  -31.604 1.00 42.43  ? 405 GLY A O      1 
ATOM   522  N N      . PHE A 1 67  ? -22.097 16.751  -32.381 1.00 43.59  ? 406 PHE A N      1 
ATOM   523  C CA     . PHE A 1 67  ? -22.104 17.167  -33.774 1.00 47.52  ? 406 PHE A CA     1 
ATOM   524  C C      . PHE A 1 67  ? -23.259 16.497  -34.502 1.00 49.40  ? 406 PHE A C      1 
ATOM   525  O O      . PHE A 1 67  ? -23.889 15.560  -34.002 1.00 51.46  ? 406 PHE A O      1 
ATOM   526  C CB     . PHE A 1 67  ? -20.772 16.850  -34.470 1.00 49.54  ? 406 PHE A CB     1 
ATOM   527  C CG     . PHE A 1 67  ? -20.512 15.381  -34.654 1.00 52.34  ? 406 PHE A CG     1 
ATOM   528  C CD1    . PHE A 1 67  ? -19.991 14.621  -33.620 1.00 56.45  ? 406 PHE A CD1    1 
ATOM   529  C CD2    . PHE A 1 67  ? -20.772 14.764  -35.866 1.00 50.20  ? 406 PHE A CD2    1 
ATOM   530  C CE1    . PHE A 1 67  ? -19.745 13.269  -33.789 1.00 65.79  ? 406 PHE A CE1    1 
ATOM   531  C CE2    . PHE A 1 67  ? -20.528 13.414  -36.041 1.00 54.49  ? 406 PHE A CE2    1 
ATOM   532  C CZ     . PHE A 1 67  ? -20.013 12.666  -35.001 1.00 59.76  ? 406 PHE A CZ     1 
ATOM   533  N N      . CYS A 1 68  ? -23.533 17.007  -35.700 1.00 47.81  ? 407 CYS A N      1 
ATOM   534  C CA     . CYS A 1 68  ? -24.603 16.504  -36.549 1.00 46.89  ? 407 CYS A CA     1 
ATOM   535  C C      . CYS A 1 68  ? -24.180 16.679  -37.998 1.00 49.74  ? 407 CYS A C      1 
ATOM   536  O O      . CYS A 1 68  ? -23.776 17.775  -38.398 1.00 46.11  ? 407 CYS A O      1 
ATOM   537  C CB     . CYS A 1 68  ? -25.920 17.243  -36.282 1.00 47.55  ? 407 CYS A CB     1 
ATOM   538  S SG     . CYS A 1 68  ? -27.245 16.873  -37.460 1.00 54.21  ? 407 CYS A SG     1 
ATOM   539  N N      . VAL A 1 69  ? -24.262 15.602  -38.771 1.00 52.80  ? 408 VAL A N      1 
ATOM   540  C CA     . VAL A 1 69  ? -23.972 15.628  -40.200 1.00 49.04  ? 408 VAL A CA     1 
ATOM   541  C C      . VAL A 1 69  ? -25.300 15.523  -40.935 1.00 50.47  ? 408 VAL A C      1 
ATOM   542  O O      . VAL A 1 69  ? -26.017 14.524  -40.795 1.00 46.47  ? 408 VAL A O      1 
ATOM   543  C CB     . VAL A 1 69  ? -23.018 14.497  -40.611 1.00 44.11  ? 408 VAL A CB     1 
ATOM   544  C CG1    . VAL A 1 69  ? -22.487 14.739  -42.017 1.00 45.28  ? 408 VAL A CG1    1 
ATOM   545  C CG2    . VAL A 1 69  ? -21.877 14.376  -39.614 1.00 50.52  ? 408 VAL A CG2    1 
ATOM   546  N N      . TYR A 1 70  ? -25.636 16.554  -41.707 1.00 51.01  ? 409 TYR A N      1 
ATOM   547  C CA     . TYR A 1 70  ? -26.908 16.599  -42.418 1.00 49.83  ? 409 TYR A CA     1 
ATOM   548  C C      . TYR A 1 70  ? -26.680 17.159  -43.812 1.00 54.07  ? 409 TYR A C      1 
ATOM   549  O O      . TYR A 1 70  ? -26.277 18.317  -43.960 1.00 51.14  ? 409 TYR A O      1 
ATOM   550  C CB     . TYR A 1 70  ? -27.937 17.443  -41.659 1.00 53.61  ? 409 TYR A CB     1 
ATOM   551  C CG     . TYR A 1 70  ? -29.331 17.361  -42.233 1.00 51.28  ? 409 TYR A CG     1 
ATOM   552  C CD1    . TYR A 1 70  ? -30.139 16.259  -41.989 1.00 53.95  ? 409 TYR A CD1    1 
ATOM   553  C CD2    . TYR A 1 70  ? -29.842 18.387  -43.017 1.00 53.81  ? 409 TYR A CD2    1 
ATOM   554  C CE1    . TYR A 1 70  ? -31.416 16.178  -42.512 1.00 56.81  ? 409 TYR A CE1    1 
ATOM   555  C CE2    . TYR A 1 70  ? -31.118 18.317  -43.543 1.00 54.64  ? 409 TYR A CE2    1 
ATOM   556  C CZ     . TYR A 1 70  ? -31.900 17.210  -43.287 1.00 57.51  ? 409 TYR A CZ     1 
ATOM   557  O OH     . TYR A 1 70  ? -33.170 17.137  -43.810 1.00 58.59  ? 409 TYR A OH     1 
ATOM   558  N N      . LYS A 1 71  ? -26.933 16.334  -44.825 1.00 59.67  ? 410 LYS A N      1 
ATOM   559  C CA     . LYS A 1 71  ? -26.874 16.751  -46.224 1.00 59.00  ? 410 LYS A CA     1 
ATOM   560  C C      . LYS A 1 71  ? -25.522 17.378  -46.562 1.00 52.82  ? 410 LYS A C      1 
ATOM   561  O O      . LYS A 1 71  ? -25.431 18.501  -47.065 1.00 51.50  ? 410 LYS A O      1 
ATOM   562  C CB     . LYS A 1 71  ? -28.028 17.699  -46.554 1.00 53.12  ? 410 LYS A CB     1 
ATOM   563  C CG     . LYS A 1 71  ? -29.393 17.043  -46.402 1.00 54.56  ? 410 LYS A CG     1 
ATOM   564  C CD     . LYS A 1 71  ? -30.531 17.978  -46.771 1.00 56.88  ? 410 LYS A CD     1 
ATOM   565  C CE     . LYS A 1 71  ? -31.870 17.269  -46.638 1.00 57.22  ? 410 LYS A CE     1 
ATOM   566  N NZ     . LYS A 1 71  ? -33.020 18.169  -46.930 1.00 66.08  ? 410 LYS A NZ     1 
ATOM   567  N N      . GLY A 1 72  ? -24.458 16.630  -46.279 1.00 50.96  ? 411 GLY A N      1 
ATOM   568  C CA     . GLY A 1 72  ? -23.121 17.018  -46.676 1.00 57.06  ? 411 GLY A CA     1 
ATOM   569  C C      . GLY A 1 72  ? -22.474 18.102  -45.846 1.00 57.69  ? 411 GLY A C      1 
ATOM   570  O O      . GLY A 1 72  ? -21.416 18.608  -46.239 1.00 57.23  ? 411 GLY A O      1 
ATOM   571  N N      . ASN A 1 73  ? -23.064 18.478  -44.715 1.00 62.57  ? 412 ASN A N      1 
ATOM   572  C CA     . ASN A 1 73  ? -22.491 19.493  -43.846 1.00 53.57  ? 412 ASN A CA     1 
ATOM   573  C C      . ASN A 1 73  ? -22.485 18.999  -42.407 1.00 52.11  ? 412 ASN A C      1 
ATOM   574  O O      . ASN A 1 73  ? -23.340 18.208  -41.998 1.00 52.55  ? 412 ASN A O      1 
ATOM   575  C CB     . ASN A 1 73  ? -23.256 20.820  -43.942 1.00 59.16  ? 412 ASN A CB     1 
ATOM   576  C CG     . ASN A 1 73  ? -22.906 21.603  -45.193 1.00 62.94  ? 412 ASN A CG     1 
ATOM   577  O OD1    . ASN A 1 73  ? -21.986 22.421  -45.189 1.00 58.09  ? 412 ASN A OD1    1 
ATOM   578  N ND2    . ASN A 1 73  ? -23.638 21.353  -46.272 1.00 61.15  ? 412 ASN A ND2    1 
ATOM   579  N N      . THR A 1 74  ? -21.504 19.472  -41.646 1.00 53.98  ? 413 THR A N      1 
ATOM   580  C CA     . THR A 1 74  ? -21.346 19.120  -40.243 1.00 57.16  ? 413 THR A CA     1 
ATOM   581  C C      . THR A 1 74  ? -21.702 20.322  -39.380 1.00 54.89  ? 413 THR A C      1 
ATOM   582  O O      . THR A 1 74  ? -21.165 21.416  -39.580 1.00 53.52  ? 413 THR A O      1 
ATOM   583  C CB     . THR A 1 74  ? -19.915 18.664  -39.946 1.00 57.46  ? 413 THR A CB     1 
ATOM   584  O OG1    . THR A 1 74  ? -19.636 17.454  -40.663 1.00 62.61  ? 413 THR A OG1    1 
ATOM   585  C CG2    . THR A 1 74  ? -19.731 18.419  -38.456 1.00 63.75  ? 413 THR A CG2    1 
ATOM   586  N N      . TYR A 1 75  ? -22.609 20.115  -38.431 1.00 48.25  ? 414 TYR A N      1 
ATOM   587  C CA     . TYR A 1 75  ? -23.014 21.144  -37.481 1.00 46.39  ? 414 TYR A CA     1 
ATOM   588  C C      . TYR A 1 75  ? -22.497 20.754  -36.103 1.00 42.39  ? 414 TYR A C      1 
ATOM   589  O O      . TYR A 1 75  ? -22.918 19.734  -35.548 1.00 46.73  ? 414 TYR A O      1 
ATOM   590  C CB     . TYR A 1 75  ? -24.534 21.309  -37.460 1.00 46.21  ? 414 TYR A CB     1 
ATOM   591  C CG     . TYR A 1 75  ? -25.157 21.552  -38.818 1.00 43.38  ? 414 TYR A CG     1 
ATOM   592  C CD1    . TYR A 1 75  ? -25.302 22.839  -39.320 1.00 43.64  ? 414 TYR A CD1    1 
ATOM   593  C CD2    . TYR A 1 75  ? -25.609 20.493  -39.595 1.00 46.23  ? 414 TYR A CD2    1 
ATOM   594  C CE1    . TYR A 1 75  ? -25.875 23.065  -40.560 1.00 43.16  ? 414 TYR A CE1    1 
ATOM   595  C CE2    . TYR A 1 75  ? -26.184 20.708  -40.835 1.00 46.75  ? 414 TYR A CE2    1 
ATOM   596  C CZ     . TYR A 1 75  ? -26.315 21.996  -41.313 1.00 43.23  ? 414 TYR A CZ     1 
ATOM   597  O OH     . TYR A 1 75  ? -26.886 22.214  -42.547 1.00 43.60  ? 414 TYR A OH     1 
ATOM   598  N N      . LEU A 1 76  ? -21.585 21.556  -35.561 1.00 41.54  ? 415 LEU A N      1 
ATOM   599  C CA     . LEU A 1 76  ? -21.014 21.304  -34.246 1.00 36.70  ? 415 LEU A CA     1 
ATOM   600  C C      . LEU A 1 76  ? -21.646 22.229  -33.215 1.00 36.81  ? 415 LEU A C      1 
ATOM   601  O O      . LEU A 1 76  ? -21.858 23.417  -33.476 1.00 40.15  ? 415 LEU A O      1 
ATOM   602  C CB     . LEU A 1 76  ? -19.496 21.490  -34.256 1.00 34.00  ? 415 LEU A CB     1 
ATOM   603  C CG     . LEU A 1 76  ? -18.699 20.468  -35.070 1.00 37.43  ? 415 LEU A CG     1 
ATOM   604  C CD1    . LEU A 1 76  ? -18.486 20.950  -36.498 1.00 35.41  ? 415 LEU A CD1    1 
ATOM   605  C CD2    . LEU A 1 76  ? -17.374 20.151  -34.394 1.00 37.30  ? 415 LEU A CD2    1 
ATOM   606  N N      . VAL A 1 77  ? -21.942 21.675  -32.043 1.00 33.90  ? 416 VAL A N      1 
ATOM   607  C CA     . VAL A 1 77  ? -22.603 22.398  -30.963 1.00 35.56  ? 416 VAL A CA     1 
ATOM   608  C C      . VAL A 1 77  ? -21.636 22.490  -29.790 1.00 30.94  ? 416 VAL A C      1 
ATOM   609  O O      . VAL A 1 77  ? -21.270 21.469  -29.195 1.00 34.05  ? 416 VAL A O      1 
ATOM   610  C CB     . VAL A 1 77  ? -23.914 21.715  -30.545 1.00 37.89  ? 416 VAL A CB     1 
ATOM   611  C CG1    . VAL A 1 77  ? -24.705 22.612  -29.605 1.00 38.15  ? 416 VAL A CG1    1 
ATOM   612  C CG2    . VAL A 1 77  ? -24.738 21.348  -31.773 1.00 36.75  ? 416 VAL A CG2    1 
ATOM   613  N N      . TYR A 1 78  ? -21.221 23.708  -29.463 1.00 31.74  ? 417 TYR A N      1 
ATOM   614  C CA     . TYR A 1 78  ? -20.338 23.980  -28.338 1.00 29.26  ? 417 TYR A CA     1 
ATOM   615  C C      . TYR A 1 78  ? -21.122 24.631  -27.207 1.00 31.06  ? 417 TYR A C      1 
ATOM   616  O O      . TYR A 1 78  ? -22.247 25.104  -27.385 1.00 34.92  ? 417 TYR A O      1 
ATOM   617  C CB     . TYR A 1 78  ? -19.178 24.891  -28.757 1.00 28.25  ? 417 TYR A CB     1 
ATOM   618  C CG     . TYR A 1 78  ? -18.294 24.335  -29.849 1.00 30.05  ? 417 TYR A CG     1 
ATOM   619  C CD1    . TYR A 1 78  ? -18.680 24.396  -31.181 1.00 30.40  ? 417 TYR A CD1    1 
ATOM   620  C CD2    . TYR A 1 78  ? -17.062 23.769  -29.552 1.00 32.12  ? 417 TYR A CD2    1 
ATOM   621  C CE1    . TYR A 1 78  ? -17.872 23.897  -32.184 1.00 28.88  ? 417 TYR A CE1    1 
ATOM   622  C CE2    . TYR A 1 78  ? -16.247 23.268  -30.550 1.00 32.05  ? 417 TYR A CE2    1 
ATOM   623  C CZ     . TYR A 1 78  ? -16.658 23.334  -31.863 1.00 29.00  ? 417 TYR A CZ     1 
ATOM   624  O OH     . TYR A 1 78  ? -15.851 22.837  -32.859 1.00 41.97  ? 417 TYR A OH     1 
ATOM   625  N N      . GLU A 1 79  ? -20.509 24.658  -26.027 1.00 27.13  ? 418 GLU A N      1 
ATOM   626  C CA     . GLU A 1 79  ? -21.087 25.404  -24.920 1.00 26.17  ? 418 GLU A CA     1 
ATOM   627  C C      . GLU A 1 79  ? -21.077 26.889  -25.251 1.00 29.16  ? 418 GLU A C      1 
ATOM   628  O O      . GLU A 1 79  ? -20.072 27.423  -25.730 1.00 32.82  ? 418 GLU A O      1 
ATOM   629  C CB     . GLU A 1 79  ? -20.317 25.140  -23.626 1.00 24.71  ? 418 GLU A CB     1 
ATOM   630  C CG     . GLU A 1 79  ? -18.851 25.534  -23.664 1.00 28.44  ? 418 GLU A CG     1 
ATOM   631  C CD     . GLU A 1 79  ? -18.233 25.583  -22.277 1.00 32.63  ? 418 GLU A CD     1 
ATOM   632  O OE1    . GLU A 1 79  ? -18.921 26.037  -21.338 1.00 26.74  ? 418 GLU A OE1    1 
ATOM   633  O OE2    . GLU A 1 79  ? -17.065 25.162  -22.124 1.00 30.43  ? 418 GLU A OE2    1 
ATOM   634  N N      . PHE A 1 80  ? -22.204 27.554  -25.012 1.00 33.59  ? 419 PHE A N      1 
ATOM   635  C CA     . PHE A 1 80  ? -22.301 28.978  -25.297 1.00 32.97  ? 419 PHE A CA     1 
ATOM   636  C C      . PHE A 1 80  ? -21.506 29.770  -24.270 1.00 30.16  ? 419 PHE A C      1 
ATOM   637  O O      . PHE A 1 80  ? -21.616 29.531  -23.064 1.00 29.06  ? 419 PHE A O      1 
ATOM   638  C CB     . PHE A 1 80  ? -23.762 29.424  -25.301 1.00 32.37  ? 419 PHE A CB     1 
ATOM   639  C CG     . PHE A 1 80  ? -23.944 30.890  -25.564 1.00 33.17  ? 419 PHE A CG     1 
ATOM   640  C CD1    . PHE A 1 80  ? -23.740 31.408  -26.832 1.00 32.37  ? 419 PHE A CD1    1 
ATOM   641  C CD2    . PHE A 1 80  ? -24.317 31.750  -24.546 1.00 30.07  ? 419 PHE A CD2    1 
ATOM   642  C CE1    . PHE A 1 80  ? -23.904 32.757  -27.080 1.00 33.05  ? 419 PHE A CE1    1 
ATOM   643  C CE2    . PHE A 1 80  ? -24.483 33.101  -24.788 1.00 34.66  ? 419 PHE A CE2    1 
ATOM   644  C CZ     . PHE A 1 80  ? -24.276 33.605  -26.057 1.00 36.74  ? 419 PHE A CZ     1 
ATOM   645  N N      . ALA A 1 81  ? -20.699 30.708  -24.751 1.00 27.16  ? 420 ALA A N      1 
ATOM   646  C CA     . ALA A 1 81  ? -19.882 31.566  -23.901 1.00 25.08  ? 420 ALA A CA     1 
ATOM   647  C C      . ALA A 1 81  ? -20.457 32.974  -23.975 1.00 30.38  ? 420 ALA A C      1 
ATOM   648  O O      . ALA A 1 81  ? -20.180 33.721  -24.919 1.00 29.94  ? 420 ALA A O      1 
ATOM   649  C CB     . ALA A 1 81  ? -18.417 31.534  -24.329 1.00 27.84  ? 420 ALA A CB     1 
ATOM   650  N N      . GLU A 1 82  ? -21.279 33.326  -22.991 1.00 34.50  ? 421 GLU A N      1 
ATOM   651  C CA     . GLU A 1 82  ? -21.725 34.704  -22.869 1.00 29.28  ? 421 GLU A CA     1 
ATOM   652  C C      . GLU A 1 82  ? -20.560 35.581  -22.422 1.00 29.37  ? 421 GLU A C      1 
ATOM   653  O O      . GLU A 1 82  ? -19.663 35.134  -21.704 1.00 33.73  ? 421 GLU A O      1 
ATOM   654  C CB     . GLU A 1 82  ? -22.885 34.810  -21.878 1.00 31.95  ? 421 GLU A CB     1 
ATOM   655  C CG     . GLU A 1 82  ? -22.495 34.554  -20.438 1.00 39.79  ? 421 GLU A CG     1 
ATOM   656  C CD     . GLU A 1 82  ? -23.600 34.912  -19.464 1.00 48.60  ? 421 GLU A CD     1 
ATOM   657  O OE1    . GLU A 1 82  ? -24.747 34.472  -19.680 1.00 47.71  ? 421 GLU A OE1    1 
ATOM   658  O OE2    . GLU A 1 82  ? -23.322 35.632  -18.480 1.00 52.89  ? 421 GLU A OE2    1 
ATOM   659  N N      . ASN A 1 83  ? -20.579 36.841  -22.858 1.00 29.76  ? 422 ASN A N      1 
ATOM   660  C CA     . ASN A 1 83  ? -19.544 37.850  -22.627 1.00 34.05  ? 422 ASN A CA     1 
ATOM   661  C C      . ASN A 1 83  ? -18.465 37.760  -23.700 1.00 29.84  ? 422 ASN A C      1 
ATOM   662  O O      . ASN A 1 83  ? -17.422 38.423  -23.584 1.00 31.41  ? 422 ASN A O      1 
ATOM   663  C CB     . ASN A 1 83  ? -18.910 37.754  -21.227 1.00 27.98  ? 422 ASN A CB     1 
ATOM   664  C CG     . ASN A 1 83  ? -19.862 38.168  -20.123 1.00 28.83  ? 422 ASN A CG     1 
ATOM   665  O OD1    . ASN A 1 83  ? -20.431 39.258  -20.160 1.00 32.81  ? 422 ASN A OD1    1 
ATOM   666  N ND2    . ASN A 1 83  ? -20.039 37.299  -19.134 1.00 34.21  ? 422 ASN A ND2    1 
ATOM   667  N N      . ASN A 1 84  ? -18.666 36.928  -24.714 1.00 26.32  ? 423 ASN A N      1 
ATOM   668  C CA     . ASN A 1 84  ? -17.995 37.012  -26.013 1.00 28.30  ? 423 ASN A CA     1 
ATOM   669  C C      . ASN A 1 84  ? -16.502 36.738  -25.829 1.00 28.09  ? 423 ASN A C      1 
ATOM   670  O O      . ASN A 1 84  ? -16.141 35.789  -25.124 1.00 27.92  ? 423 ASN A O      1 
ATOM   671  C CB     . ASN A 1 84  ? -18.332 38.358  -26.655 1.00 31.36  ? 423 ASN A CB     1 
ATOM   672  C CG     . ASN A 1 84  ? -19.792 38.773  -26.408 1.00 34.95  ? 423 ASN A CG     1 
ATOM   673  O OD1    . ASN A 1 84  ? -20.720 38.214  -26.999 1.00 43.35  ? 423 ASN A OD1    1 
ATOM   674  N ND2    . ASN A 1 84  ? -19.996 39.738  -25.514 1.00 30.27  ? 423 ASN A ND2    1 
ATOM   675  N N      . SER A 1 85  ? -15.633 37.528  -26.454 1.00 25.08  ? 424 SER A N      1 
ATOM   676  C CA     . SER A 1 85  ? -14.197 37.303  -26.536 1.00 24.39  ? 424 SER A CA     1 
ATOM   677  C C      . SER A 1 85  ? -13.453 38.374  -25.749 1.00 25.22  ? 424 SER A C      1 
ATOM   678  O O      . SER A 1 85  ? -13.948 39.489  -25.556 1.00 27.62  ? 424 SER A O      1 
ATOM   679  C CB     . SER A 1 85  ? -13.716 37.327  -27.996 1.00 23.91  ? 424 SER A CB     1 
ATOM   680  O OG     . SER A 1 85  ? -13.467 38.655  -28.432 1.00 25.71  ? 424 SER A OG     1 
ATOM   681  N N      . LEU A 1 86  ? -12.254 38.020  -25.291 1.00 23.17  ? 425 LEU A N      1 
ATOM   682  C CA     . LEU A 1 86  ? -11.430 38.972  -24.555 1.00 23.72  ? 425 LEU A CA     1 
ATOM   683  C C      . LEU A 1 86  ? -11.169 40.235  -25.373 1.00 23.34  ? 425 LEU A C      1 
ATOM   684  O O      . LEU A 1 86  ? -11.197 41.350  -24.837 1.00 25.95  ? 425 LEU A O      1 
ATOM   685  C CB     . LEU A 1 86  ? -10.119 38.300  -24.161 1.00 22.87  ? 425 LEU A CB     1 
ATOM   686  C CG     . LEU A 1 86  ? -9.136  39.144  -23.372 1.00 22.82  ? 425 LEU A CG     1 
ATOM   687  C CD1    . LEU A 1 86  ? -9.770  39.503  -22.046 1.00 19.08  ? 425 LEU A CD1    1 
ATOM   688  C CD2    . LEU A 1 86  ? -7.848  38.362  -23.190 1.00 17.82  ? 425 LEU A CD2    1 
ATOM   689  N N      . ASP A 1 87  ? -10.926 40.080  -26.676 1.00 22.61  ? 426 ASP A N      1 
ATOM   690  C CA     . ASP A 1 87  ? -10.714 41.237  -27.538 1.00 23.51  ? 426 ASP A CA     1 
ATOM   691  C C      . ASP A 1 87  ? -11.849 42.247  -27.406 1.00 29.05  ? 426 ASP A C      1 
ATOM   692  O O      . ASP A 1 87  ? -11.606 43.453  -27.287 1.00 33.78  ? 426 ASP A O      1 
ATOM   693  C CB     . ASP A 1 87  ? -10.558 40.780  -28.991 1.00 23.50  ? 426 ASP A CB     1 
ATOM   694  C CG     . ASP A 1 87  ? -10.159 41.907  -29.916 1.00 27.61  ? 426 ASP A CG     1 
ATOM   695  O OD1    . ASP A 1 87  ? -11.038 42.704  -30.300 1.00 38.04  ? 426 ASP A OD1    1 
ATOM   696  O OD2    . ASP A 1 87  ? -8.960  42.003  -30.248 1.00 31.99  ? 426 ASP A OD2    1 
ATOM   697  N N      . ASP A 1 88  ? -13.098 41.772  -27.417 1.00 26.25  ? 427 ASP A N      1 
ATOM   698  C CA     . ASP A 1 88  ? -14.240 42.673  -27.277 1.00 29.35  ? 427 ASP A CA     1 
ATOM   699  C C      . ASP A 1 88  ? -14.142 43.506  -26.006 1.00 31.47  ? 427 ASP A C      1 
ATOM   700  O O      . ASP A 1 88  ? -14.462 44.700  -26.009 1.00 38.00  ? 427 ASP A O      1 
ATOM   701  C CB     . ASP A 1 88  ? -15.540 41.868  -27.286 1.00 26.87  ? 427 ASP A CB     1 
ATOM   702  C CG     . ASP A 1 88  ? -15.703 41.045  -28.544 1.00 30.48  ? 427 ASP A CG     1 
ATOM   703  O OD1    . ASP A 1 88  ? -15.443 41.585  -29.640 1.00 32.77  ? 427 ASP A OD1    1 
ATOM   704  O OD2    . ASP A 1 88  ? -16.077 39.857  -28.438 1.00 31.30  ? 427 ASP A OD2    1 
ATOM   705  N N      . TRP A 1 89  ? -13.705 42.894  -24.905 1.00 29.66  ? 428 TRP A N      1 
ATOM   706  C CA     . TRP A 1 89  ? -13.659 43.612  -23.637 1.00 27.59  ? 428 TRP A CA     1 
ATOM   707  C C      . TRP A 1 89  ? -12.438 44.520  -23.543 1.00 31.23  ? 428 TRP A C      1 
ATOM   708  O O      . TRP A 1 89  ? -12.541 45.649  -23.050 1.00 38.39  ? 428 TRP A O      1 
ATOM   709  C CB     . TRP A 1 89  ? -13.695 42.619  -22.473 1.00 25.96  ? 428 TRP A CB     1 
ATOM   710  C CG     . TRP A 1 89  ? -15.071 42.084  -22.224 1.00 29.26  ? 428 TRP A CG     1 
ATOM   711  C CD1    . TRP A 1 89  ? -15.655 41.008  -22.825 1.00 31.85  ? 428 TRP A CD1    1 
ATOM   712  C CD2    . TRP A 1 89  ? -16.046 42.615  -21.319 1.00 28.17  ? 428 TRP A CD2    1 
ATOM   713  N NE1    . TRP A 1 89  ? -16.932 40.833  -22.347 1.00 29.56  ? 428 TRP A NE1    1 
ATOM   714  C CE2    . TRP A 1 89  ? -17.196 41.808  -21.421 1.00 30.11  ? 428 TRP A CE2    1 
ATOM   715  C CE3    . TRP A 1 89  ? -16.057 43.694  -20.431 1.00 34.90  ? 428 TRP A CE3    1 
ATOM   716  C CZ2    . TRP A 1 89  ? -18.343 42.046  -20.668 1.00 31.30  ? 428 TRP A CZ2    1 
ATOM   717  C CZ3    . TRP A 1 89  ? -17.194 43.928  -19.685 1.00 38.70  ? 428 TRP A CZ3    1 
ATOM   718  C CH2    . TRP A 1 89  ? -18.321 43.108  -19.807 1.00 38.32  ? 428 TRP A CH2    1 
ATOM   719  N N      . LEU A 1 90  ? -11.282 44.054  -24.018 1.00 32.07  ? 429 LEU A N      1 
ATOM   720  C CA     . LEU A 1 90  ? -10.065 44.853  -23.923 1.00 30.50  ? 429 LEU A CA     1 
ATOM   721  C C      . LEU A 1 90  ? -10.038 46.013  -24.910 1.00 32.25  ? 429 LEU A C      1 
ATOM   722  O O      . LEU A 1 90  ? -9.249  46.946  -24.725 1.00 33.65  ? 429 LEU A O      1 
ATOM   723  C CB     . LEU A 1 90  ? -8.835  43.972  -24.144 1.00 22.92  ? 429 LEU A CB     1 
ATOM   724  C CG     . LEU A 1 90  ? -8.542  42.910  -23.088 1.00 21.53  ? 429 LEU A CG     1 
ATOM   725  C CD1    . LEU A 1 90  ? -7.323  42.094  -23.486 1.00 20.45  ? 429 LEU A CD1    1 
ATOM   726  C CD2    . LEU A 1 90  ? -8.345  43.551  -21.723 1.00 24.68  ? 429 LEU A CD2    1 
ATOM   727  N N      . HIS A 1 91  ? -10.874 45.984  -25.943 1.00 33.73  ? 430 HIS A N      1 
ATOM   728  C CA     . HIS A 1 91  ? -10.851 46.988  -27.003 1.00 38.86  ? 430 HIS A CA     1 
ATOM   729  C C      . HIS A 1 91  ? -12.246 47.556  -27.226 1.00 46.51  ? 430 HIS A C      1 
ATOM   730  O O      . HIS A 1 91  ? -12.764 47.595  -28.344 1.00 52.03  ? 430 HIS A O      1 
ATOM   731  C CB     . HIS A 1 91  ? -10.281 46.389  -28.286 1.00 34.84  ? 430 HIS A CB     1 
ATOM   732  C CG     . HIS A 1 91  ? -8.954  45.721  -28.098 1.00 33.27  ? 430 HIS A CG     1 
ATOM   733  N ND1    . HIS A 1 91  ? -8.733  44.400  -28.424 1.00 31.96  ? 430 HIS A ND1    1 
ATOM   734  C CD2    . HIS A 1 91  ? -7.780  46.190  -27.613 1.00 31.06  ? 430 HIS A CD2    1 
ATOM   735  C CE1    . HIS A 1 91  ? -7.480  44.083  -28.146 1.00 26.71  ? 430 HIS A CE1    1 
ATOM   736  N NE2    . HIS A 1 91  ? -6.880  45.152  -27.654 1.00 29.24  ? 430 HIS A NE2    1 
ATOM   737  N N      . SER A 1 92  ? -12.873 48.009  -26.145 1.00 71.30  ? 431 SER A N      1 
ATOM   738  C CA     . SER A 1 92  ? -14.217 48.569  -26.212 1.00 73.33  ? 431 SER A CA     1 
ATOM   739  C C      . SER A 1 92  ? -14.405 49.670  -25.174 1.00 83.71  ? 431 SER A C      1 
ATOM   740  O O      . SER A 1 92  ? -13.900 49.577  -24.055 1.00 90.49  ? 431 SER A O      1 
ATOM   741  C CB     . SER A 1 92  ? -15.264 47.472  -26.010 1.00 71.35  ? 431 SER A CB     1 
ATOM   742  O OG     . SER A 1 92  ? -16.576 48.007  -26.047 1.00 77.20  ? 431 SER A OG     1 
ATOM   743  N N      . MET A 1 104 ? -18.535 48.101  -18.819 1.00 49.98  ? 443 MET A N      1 
ATOM   744  C CA     . MET A 1 104 ? -17.639 47.522  -17.827 1.00 47.59  ? 443 MET A CA     1 
ATOM   745  C C      . MET A 1 104 ? -16.255 47.260  -18.410 1.00 50.70  ? 443 MET A C      1 
ATOM   746  O O      . MET A 1 104 ? -16.113 46.982  -19.601 1.00 50.33  ? 443 MET A O      1 
ATOM   747  C CB     . MET A 1 104 ? -18.218 46.220  -17.273 1.00 50.40  ? 443 MET A CB     1 
ATOM   748  C CG     . MET A 1 104 ? -17.248 45.444  -16.390 1.00 66.55  ? 443 MET A CG     1 
ATOM   749  S SD     . MET A 1 104 ? -17.835 43.793  -15.963 1.00 50.61  ? 443 MET A SD     1 
ATOM   750  C CE     . MET A 1 104 ? -16.434 43.163  -15.044 1.00 42.68  ? 443 MET A CE     1 
ATOM   751  N N      . CYS A 1 105 ? -15.238 47.353  -17.559 1.00 43.09  ? 444 CYS A N      1 
ATOM   752  C CA     . CYS A 1 105 ? -13.872 47.011  -17.919 1.00 39.02  ? 444 CYS A CA     1 
ATOM   753  C C      . CYS A 1 105 ? -13.369 45.907  -17.000 1.00 36.79  ? 444 CYS A C      1 
ATOM   754  O O      . CYS A 1 105 ? -13.742 45.839  -15.824 1.00 46.71  ? 444 CYS A O      1 
ATOM   755  C CB     . CYS A 1 105 ? -12.945 48.228  -17.830 1.00 47.01  ? 444 CYS A CB     1 
ATOM   756  S SG     . CYS A 1 105 ? -13.305 49.525  -19.038 1.00 56.89  ? 444 CYS A SG     1 
ATOM   757  N N      . LEU A 1 106 ? -12.521 45.039  -17.545 1.00 31.60  ? 445 LEU A N      1 
ATOM   758  C CA     . LEU A 1 106 ? -11.984 43.927  -16.773 1.00 25.28  ? 445 LEU A CA     1 
ATOM   759  C C      . LEU A 1 106 ? -11.036 44.446  -15.697 1.00 27.14  ? 445 LEU A C      1 
ATOM   760  O O      . LEU A 1 106 ? -10.048 45.123  -16.002 1.00 27.03  ? 445 LEU A O      1 
ATOM   761  C CB     . LEU A 1 106 ? -11.265 42.942  -17.691 1.00 23.92  ? 445 LEU A CB     1 
ATOM   762  C CG     . LEU A 1 106 ? -12.128 42.178  -18.697 1.00 26.64  ? 445 LEU A CG     1 
ATOM   763  C CD1    . LEU A 1 106 ? -11.255 41.320  -19.600 1.00 26.18  ? 445 LEU A CD1    1 
ATOM   764  C CD2    . LEU A 1 106 ? -13.166 41.326  -17.983 1.00 23.98  ? 445 LEU A CD2    1 
ATOM   765  N N      . SER A 1 107 ? -11.338 44.129  -14.442 1.00 24.34  ? 446 SER A N      1 
ATOM   766  C CA     . SER A 1 107 ? -10.480 44.523  -13.338 1.00 24.67  ? 446 SER A CA     1 
ATOM   767  C C      . SER A 1 107 ? -9.171  43.733  -13.368 1.00 23.76  ? 446 SER A C      1 
ATOM   768  O O      . SER A 1 107 ? -8.974  42.822  -14.179 1.00 24.60  ? 446 SER A O      1 
ATOM   769  C CB     . SER A 1 107 ? -11.200 44.316  -12.006 1.00 25.80  ? 446 SER A CB     1 
ATOM   770  O OG     . SER A 1 107 ? -11.665 42.982  -11.880 1.00 25.10  ? 446 SER A OG     1 
ATOM   771  N N      . TRP A 1 108 ? -8.262  44.100  -12.462 1.00 20.69  ? 447 TRP A N      1 
ATOM   772  C CA     . TRP A 1 108 ? -6.990  43.391  -12.360 1.00 19.56  ? 447 TRP A CA     1 
ATOM   773  C C      . TRP A 1 108 ? -7.209  41.925  -12.008 1.00 18.57  ? 447 TRP A C      1 
ATOM   774  O O      . TRP A 1 108 ? -6.649  41.029  -12.649 1.00 23.43  ? 447 TRP A O      1 
ATOM   775  C CB     . TRP A 1 108 ? -6.095  44.069  -11.321 1.00 19.93  ? 447 TRP A CB     1 
ATOM   776  C CG     . TRP A 1 108 ? -4.861  43.288  -10.992 1.00 18.70  ? 447 TRP A CG     1 
ATOM   777  C CD1    . TRP A 1 108 ? -4.641  42.533  -9.877  1.00 19.47  ? 447 TRP A CD1    1 
ATOM   778  C CD2    . TRP A 1 108 ? -3.677  43.176  -11.791 1.00 20.87  ? 447 TRP A CD2    1 
ATOM   779  N NE1    . TRP A 1 108 ? -3.392  41.962  -9.930  1.00 20.73  ? 447 TRP A NE1    1 
ATOM   780  C CE2    . TRP A 1 108 ? -2.781  42.341  -11.096 1.00 21.96  ? 447 TRP A CE2    1 
ATOM   781  C CE3    . TRP A 1 108 ? -3.288  43.703  -13.026 1.00 20.09  ? 447 TRP A CE3    1 
ATOM   782  C CZ2    . TRP A 1 108 ? -1.521  42.021  -11.594 1.00 22.99  ? 447 TRP A CZ2    1 
ATOM   783  C CZ3    . TRP A 1 108 ? -2.038  43.384  -13.519 1.00 18.48  ? 447 TRP A CZ3    1 
ATOM   784  C CH2    . TRP A 1 108 ? -1.169  42.552  -12.805 1.00 22.00  ? 447 TRP A CH2    1 
ATOM   785  N N      . PHE A 1 109 ? -8.024  41.666  -10.985 1.00 17.91  ? 448 PHE A N      1 
ATOM   786  C CA     . PHE A 1 109 ? -8.320  40.294  -10.585 1.00 20.83  ? 448 PHE A CA     1 
ATOM   787  C C      . PHE A 1 109 ? -8.832  39.476  -11.765 1.00 23.04  ? 448 PHE A C      1 
ATOM   788  O O      . PHE A 1 109 ? -8.359  38.362  -12.019 1.00 24.53  ? 448 PHE A O      1 
ATOM   789  C CB     . PHE A 1 109 ? -9.338  40.304  -9.442  1.00 23.38  ? 448 PHE A CB     1 
ATOM   790  C CG     . PHE A 1 109 ? -9.782  38.937  -9.006  1.00 28.79  ? 448 PHE A CG     1 
ATOM   791  C CD1    . PHE A 1 109 ? -9.018  38.198  -8.118  1.00 33.41  ? 448 PHE A CD1    1 
ATOM   792  C CD2    . PHE A 1 109 ? -10.969 38.397  -9.474  1.00 25.05  ? 448 PHE A CD2    1 
ATOM   793  C CE1    . PHE A 1 109 ? -9.425  36.939  -7.713  1.00 41.17  ? 448 PHE A CE1    1 
ATOM   794  C CE2    . PHE A 1 109 ? -11.382 37.142  -9.074  1.00 27.25  ? 448 PHE A CE2    1 
ATOM   795  C CZ     . PHE A 1 109 ? -10.610 36.411  -8.192  1.00 42.36  ? 448 PHE A CZ     1 
ATOM   796  N N      . GLN A 1 110 ? -9.798  40.023  -12.507 1.00 22.71  ? 449 GLN A N      1 
ATOM   797  C CA     . GLN A 1 110 ? -10.346 39.306  -13.654 1.00 23.52  ? 449 GLN A CA     1 
ATOM   798  C C      . GLN A 1 110 ? -9.276  39.038  -14.705 1.00 23.41  ? 449 GLN A C      1 
ATOM   799  O O      . GLN A 1 110 ? -9.180  37.925  -15.235 1.00 24.07  ? 449 GLN A O      1 
ATOM   800  C CB     . GLN A 1 110 ? -11.507 40.095  -14.259 1.00 22.27  ? 449 GLN A CB     1 
ATOM   801  C CG     . GLN A 1 110 ? -12.719 40.197  -13.354 1.00 18.65  ? 449 GLN A CG     1 
ATOM   802  C CD     . GLN A 1 110 ? -13.853 40.983  -13.983 1.00 24.32  ? 449 GLN A CD     1 
ATOM   803  O OE1    . GLN A 1 110 ? -13.667 42.117  -14.425 1.00 27.46  ? 449 GLN A OE1    1 
ATOM   804  N NE2    . GLN A 1 110 ? -15.038 40.381  -14.028 1.00 23.12  ? 449 GLN A NE2    1 
ATOM   805  N N      . ARG A 1 111 ? -8.462  40.047  -15.023 1.00 21.74  ? 450 ARG A N      1 
ATOM   806  C CA     . ARG A 1 111 ? -7.416  39.860  -16.023 1.00 20.99  ? 450 ARG A CA     1 
ATOM   807  C C      . ARG A 1 111 ? -6.445  38.762  -15.606 1.00 22.60  ? 450 ARG A C      1 
ATOM   808  O O      . ARG A 1 111 ? -5.999  37.967  -16.442 1.00 25.27  ? 450 ARG A O      1 
ATOM   809  C CB     . ARG A 1 111 ? -6.678  41.179  -16.260 1.00 21.39  ? 450 ARG A CB     1 
ATOM   810  C CG     . ARG A 1 111 ? -7.569  42.296  -16.791 1.00 20.34  ? 450 ARG A CG     1 
ATOM   811  C CD     . ARG A 1 111 ? -6.914  43.660  -16.638 1.00 22.00  ? 450 ARG A CD     1 
ATOM   812  N NE     . ARG A 1 111 ? -7.835  44.747  -16.952 1.00 24.59  ? 450 ARG A NE     1 
ATOM   813  C CZ     . ARG A 1 111 ? -7.751  45.519  -18.027 1.00 24.46  ? 450 ARG A CZ     1 
ATOM   814  N NH1    . ARG A 1 111 ? -6.777  45.371  -18.911 1.00 23.17  ? 450 ARG A NH1    1 
ATOM   815  N NH2    . ARG A 1 111 ? -8.664  46.469  -18.218 1.00 18.62  ? 450 ARG A NH2    1 
ATOM   816  N N      . VAL A 1 112 ? -6.109  38.696  -14.316 1.00 23.26  ? 451 VAL A N      1 
ATOM   817  C CA     . VAL A 1 112 ? -5.227  37.634  -13.841 1.00 21.72  ? 451 VAL A CA     1 
ATOM   818  C C      . VAL A 1 112 ? -5.929  36.285  -13.917 1.00 21.82  ? 451 VAL A C      1 
ATOM   819  O O      . VAL A 1 112 ? -5.323  35.276  -14.299 1.00 22.13  ? 451 VAL A O      1 
ATOM   820  C CB     . VAL A 1 112 ? -4.736  37.937  -12.413 1.00 23.66  ? 451 VAL A CB     1 
ATOM   821  C CG1    . VAL A 1 112 ? -3.920  36.771  -11.878 1.00 24.24  ? 451 VAL A CG1    1 
ATOM   822  C CG2    . VAL A 1 112 ? -3.916  39.216  -12.395 1.00 20.13  ? 451 VAL A CG2    1 
ATOM   823  N N      . GLN A 1 113 ? -7.214  36.240  -13.559 1.00 23.33  ? 452 GLN A N      1 
ATOM   824  C CA     . GLN A 1 113 ? -7.960  34.991  -13.664 1.00 25.46  ? 452 GLN A CA     1 
ATOM   825  C C      . GLN A 1 113 ? -7.968  34.476  -15.098 1.00 23.91  ? 452 GLN A C      1 
ATOM   826  O O      . GLN A 1 113 ? -7.759  33.281  -15.338 1.00 25.86  ? 452 GLN A O      1 
ATOM   827  C CB     . GLN A 1 113 ? -9.389  35.187  -13.157 1.00 30.65  ? 452 GLN A CB     1 
ATOM   828  C CG     . GLN A 1 113 ? -10.252 33.929  -13.203 1.00 35.34  ? 452 GLN A CG     1 
ATOM   829  C CD     . GLN A 1 113 ? -9.839  32.894  -12.172 1.00 43.91  ? 452 GLN A CD     1 
ATOM   830  O OE1    . GLN A 1 113 ? -9.140  31.929  -12.486 1.00 43.53  ? 452 GLN A OE1    1 
ATOM   831  N NE2    . GLN A 1 113 ? -10.274 33.089  -10.932 1.00 50.96  ? 452 GLN A NE2    1 
ATOM   832  N N      . ILE A 1 114 ? -8.200  35.365  -16.066 1.00 20.42  ? 453 ILE A N      1 
ATOM   833  C CA     . ILE A 1 114 ? -8.272  34.939  -17.460 1.00 20.89  ? 453 ILE A CA     1 
ATOM   834  C C      . ILE A 1 114 ? -6.920  34.423  -17.939 1.00 23.74  ? 453 ILE A C      1 
ATOM   835  O O      . ILE A 1 114 ? -6.840  33.395  -18.621 1.00 25.14  ? 453 ILE A O      1 
ATOM   836  C CB     . ILE A 1 114 ? -8.790  36.089  -18.342 1.00 20.88  ? 453 ILE A CB     1 
ATOM   837  C CG1    . ILE A 1 114 ? -10.274 36.344  -18.056 1.00 18.97  ? 453 ILE A CG1    1 
ATOM   838  C CG2    . ILE A 1 114 ? -8.569  35.770  -19.810 1.00 17.13  ? 453 ILE A CG2    1 
ATOM   839  C CD1    . ILE A 1 114 ? -10.823 37.579  -18.728 1.00 20.61  ? 453 ILE A CD1    1 
ATOM   840  N N      . ALA A 1 115 ? -5.837  35.124  -17.598 1.00 22.60  ? 454 ALA A N      1 
ATOM   841  C CA     . ALA A 1 115 ? -4.513  34.626  -17.949 1.00 21.80  ? 454 ALA A CA     1 
ATOM   842  C C      . ALA A 1 115 ? -4.259  33.257  -17.334 1.00 22.60  ? 454 ALA A C      1 
ATOM   843  O O      . ALA A 1 115 ? -3.597  32.410  -17.948 1.00 22.48  ? 454 ALA A O      1 
ATOM   844  C CB     . ALA A 1 115 ? -3.443  35.622  -17.501 1.00 18.24  ? 454 ALA A CB     1 
ATOM   845  N N      . HIS A 1 116 ? -4.790  33.018  -16.133 1.00 19.13  ? 455 HIS A N      1 
ATOM   846  C CA     . HIS A 1 116 ? -4.572  31.744  -15.457 1.00 21.53  ? 455 HIS A CA     1 
ATOM   847  C C      . HIS A 1 116 ? -5.335  30.615  -16.140 1.00 19.58  ? 455 HIS A C      1 
ATOM   848  O O      . HIS A 1 116 ? -4.798  29.516  -16.322 1.00 19.51  ? 455 HIS A O      1 
ATOM   849  C CB     . HIS A 1 116 ? -4.976  31.865  -13.987 1.00 23.76  ? 455 HIS A CB     1 
ATOM   850  C CG     . HIS A 1 116 ? -4.713  30.632  -13.181 1.00 21.96  ? 455 HIS A CG     1 
ATOM   851  N ND1    . HIS A 1 116 ? -5.687  29.693  -12.918 1.00 26.95  ? 455 HIS A ND1    1 
ATOM   852  C CD2    . HIS A 1 116 ? -3.587  30.185  -12.576 1.00 20.94  ? 455 HIS A CD2    1 
ATOM   853  C CE1    . HIS A 1 116 ? -5.172  28.719  -12.190 1.00 30.01  ? 455 HIS A CE1    1 
ATOM   854  N NE2    . HIS A 1 116 ? -3.899  28.993  -11.968 1.00 22.44  ? 455 HIS A NE2    1 
ATOM   855  N N      . ASP A 1 117 ? -6.590  30.862  -16.519 1.00 21.95  ? 456 ASP A N      1 
ATOM   856  C CA     . ASP A 1 117 ? -7.363  29.837  -17.214 1.00 20.58  ? 456 ASP A CA     1 
ATOM   857  C C      . ASP A 1 117 ? -6.703  29.450  -18.531 1.00 19.93  ? 456 ASP A C      1 
ATOM   858  O O      . ASP A 1 117 ? -6.680  28.269  -18.900 1.00 21.49  ? 456 ASP A O      1 
ATOM   859  C CB     . ASP A 1 117 ? -8.792  30.328  -17.451 1.00 21.26  ? 456 ASP A CB     1 
ATOM   860  C CG     . ASP A 1 117 ? -9.513  30.678  -16.163 1.00 22.66  ? 456 ASP A CG     1 
ATOM   861  O OD1    . ASP A 1 117 ? -9.201  30.071  -15.117 1.00 22.40  ? 456 ASP A OD1    1 
ATOM   862  O OD2    . ASP A 1 117 ? -10.396 31.561  -16.197 1.00 25.78  ? 456 ASP A OD2    1 
ATOM   863  N N      . VAL A 1 118 ? -6.158  30.431  -19.255 1.00 18.23  ? 457 VAL A N      1 
ATOM   864  C CA     . VAL A 1 118 ? -5.510  30.136  -20.529 1.00 15.72  ? 457 VAL A CA     1 
ATOM   865  C C      . VAL A 1 118 ? -4.226  29.346  -20.306 1.00 18.25  ? 457 VAL A C      1 
ATOM   866  O O      . VAL A 1 118 ? -3.946  28.377  -21.021 1.00 16.03  ? 457 VAL A O      1 
ATOM   867  C CB     . VAL A 1 118 ? -5.250  31.434  -21.314 1.00 17.58  ? 457 VAL A CB     1 
ATOM   868  C CG1    . VAL A 1 118 ? -4.554  31.124  -22.630 1.00 19.91  ? 457 VAL A CG1    1 
ATOM   869  C CG2    . VAL A 1 118 ? -6.555  32.177  -21.564 1.00 19.87  ? 457 VAL A CG2    1 
ATOM   870  N N      . ALA A 1 119 ? -3.420  29.747  -19.319 1.00 16.94  ? 458 ALA A N      1 
ATOM   871  C CA     . ALA A 1 119 ? -2.240  28.961  -18.978 1.00 16.43  ? 458 ALA A CA     1 
ATOM   872  C C      . ALA A 1 119 ? -2.635  27.558  -18.540 1.00 19.98  ? 458 ALA A C      1 
ATOM   873  O O      . ALA A 1 119 ? -1.938  26.582  -18.843 1.00 19.21  ? 458 ALA A O      1 
ATOM   874  C CB     . ALA A 1 119 ? -1.436  29.661  -17.883 1.00 16.71  ? 458 ALA A CB     1 
ATOM   875  N N      . ASP A 1 120 ? -3.760  27.440  -17.832 1.00 20.40  ? 459 ASP A N      1 
ATOM   876  C CA     . ASP A 1 120 ? -4.254  26.131  -17.420 1.00 19.94  ? 459 ASP A CA     1 
ATOM   877  C C      . ASP A 1 120 ? -4.600  25.271  -18.629 1.00 17.45  ? 459 ASP A C      1 
ATOM   878  O O      . ASP A 1 120 ? -4.326  24.065  -18.643 1.00 17.82  ? 459 ASP A O      1 
ATOM   879  C CB     . ASP A 1 120 ? -5.472  26.307  -16.511 1.00 18.08  ? 459 ASP A CB     1 
ATOM   880  C CG     . ASP A 1 120 ? -5.837  25.042  -15.763 1.00 20.95  ? 459 ASP A CG     1 
ATOM   881  O OD1    . ASP A 1 120 ? -5.083  24.051  -15.854 1.00 28.72  ? 459 ASP A OD1    1 
ATOM   882  O OD2    . ASP A 1 120 ? -6.882  25.041  -15.079 1.00 23.73  ? 459 ASP A OD2    1 
ATOM   883  N N      . ALA A 1 121 ? -5.203  25.876  -19.656 1.00 18.96  ? 460 ALA A N      1 
ATOM   884  C CA     . ALA A 1 121 ? -5.553  25.125  -20.858 1.00 17.08  ? 460 ALA A CA     1 
ATOM   885  C C      . ALA A 1 121 ? -4.321  24.827  -21.701 1.00 18.70  ? 460 ALA A C      1 
ATOM   886  O O      . ALA A 1 121 ? -4.170  23.714  -22.219 1.00 19.62  ? 460 ALA A O      1 
ATOM   887  C CB     . ALA A 1 121 ? -6.590  25.894  -21.676 1.00 16.82  ? 460 ALA A CB     1 
ATOM   888  N N      . LEU A 1 122 ? -3.429  25.808  -21.856 1.00 18.73  ? 461 LEU A N      1 
ATOM   889  C CA     . LEU A 1 122 ? -2.197  25.565  -22.598 1.00 16.60  ? 461 LEU A CA     1 
ATOM   890  C C      . LEU A 1 122 ? -1.343  24.504  -21.922 1.00 20.32  ? 461 LEU A C      1 
ATOM   891  O O      . LEU A 1 122 ? -0.654  23.735  -22.603 1.00 22.09  ? 461 LEU A O      1 
ATOM   892  C CB     . LEU A 1 122 ? -1.410  26.865  -22.754 1.00 16.27  ? 461 LEU A CB     1 
ATOM   893  C CG     . LEU A 1 122 ? -2.079  27.896  -23.663 1.00 15.89  ? 461 LEU A CG     1 
ATOM   894  C CD1    . LEU A 1 122 ? -1.174  29.099  -23.888 1.00 16.75  ? 461 LEU A CD1    1 
ATOM   895  C CD2    . LEU A 1 122 ? -2.460  27.250  -24.988 1.00 20.12  ? 461 LEU A CD2    1 
ATOM   896  N N      . ASN A 1 123 ? -1.374  24.446  -20.588 1.00 19.53  ? 462 ASN A N      1 
ATOM   897  C CA     . ASN A 1 123 ? -0.648  23.401  -19.874 1.00 20.04  ? 462 ASN A CA     1 
ATOM   898  C C      . ASN A 1 123 ? -1.223  22.024  -20.185 1.00 20.08  ? 462 ASN A C      1 
ATOM   899  O O      . ASN A 1 123 ? -0.473  21.061  -20.384 1.00 19.44  ? 462 ASN A O      1 
ATOM   900  C CB     . ASN A 1 123 ? -0.684  23.683  -18.371 1.00 18.12  ? 462 ASN A CB     1 
ATOM   901  C CG     . ASN A 1 123 ? 0.082   22.656  -17.564 1.00 19.70  ? 462 ASN A CG     1 
ATOM   902  O OD1    . ASN A 1 123 ? -0.484  21.970  -16.709 1.00 19.24  ? 462 ASN A OD1    1 
ATOM   903  N ND2    . ASN A 1 123 ? 1.378   22.539  -17.835 1.00 22.46  ? 462 ASN A ND2    1 
ATOM   904  N N      . TYR A 1 124 ? -2.552  21.915  -20.239 1.00 20.29  ? 463 TYR A N      1 
ATOM   905  C CA     . TYR A 1 124 ? -3.183  20.645  -20.584 1.00 19.35  ? 463 TYR A CA     1 
ATOM   906  C C      . TYR A 1 124 ? -2.888  20.254  -22.027 1.00 22.21  ? 463 TYR A C      1 
ATOM   907  O O      . TYR A 1 124 ? -2.574  19.091  -22.309 1.00 23.17  ? 463 TYR A O      1 
ATOM   908  C CB     . TYR A 1 124 ? -4.690  20.738  -20.339 1.00 18.80  ? 463 TYR A CB     1 
ATOM   909  C CG     . TYR A 1 124 ? -5.522  19.721  -21.089 1.00 22.86  ? 463 TYR A CG     1 
ATOM   910  C CD1    . TYR A 1 124 ? -5.663  18.423  -20.617 1.00 23.45  ? 463 TYR A CD1    1 
ATOM   911  C CD2    . TYR A 1 124 ? -6.185  20.067  -22.262 1.00 24.02  ? 463 TYR A CD2    1 
ATOM   912  C CE1    . TYR A 1 124 ? -6.427  17.495  -21.298 1.00 27.79  ? 463 TYR A CE1    1 
ATOM   913  C CE2    . TYR A 1 124 ? -6.953  19.146  -22.949 1.00 21.39  ? 463 TYR A CE2    1 
ATOM   914  C CZ     . TYR A 1 124 ? -7.070  17.862  -22.462 1.00 26.71  ? 463 TYR A CZ     1 
ATOM   915  O OH     . TYR A 1 124 ? -7.832  16.936  -23.138 1.00 30.17  ? 463 TYR A OH     1 
ATOM   916  N N      . LEU A 1 125 ? -2.973  21.213  -22.952 1.00 21.80  ? 464 LEU A N      1 
ATOM   917  C CA     . LEU A 1 125 ? -2.764  20.903  -24.362 1.00 19.36  ? 464 LEU A CA     1 
ATOM   918  C C      . LEU A 1 125 ? -1.348  20.409  -24.624 1.00 19.42  ? 464 LEU A C      1 
ATOM   919  O O      . LEU A 1 125 ? -1.142  19.483  -25.418 1.00 21.69  ? 464 LEU A O      1 
ATOM   920  C CB     . LEU A 1 125 ? -3.062  22.135  -25.217 1.00 20.67  ? 464 LEU A CB     1 
ATOM   921  C CG     . LEU A 1 125 ? -4.519  22.595  -25.256 1.00 24.78  ? 464 LEU A CG     1 
ATOM   922  C CD1    . LEU A 1 125 ? -4.662  23.850  -26.100 1.00 19.27  ? 464 LEU A CD1    1 
ATOM   923  C CD2    . LEU A 1 125 ? -5.405  21.482  -25.791 1.00 26.13  ? 464 LEU A CD2    1 
ATOM   924  N N      . HIS A 1 126 ? -0.357  21.013  -23.967 1.00 19.73  ? 465 HIS A N      1 
ATOM   925  C CA     . HIS A 1 126 ? 1.037   20.727  -24.283 1.00 22.52  ? 465 HIS A CA     1 
ATOM   926  C C      . HIS A 1 126 ? 1.574   19.487  -23.585 1.00 18.80  ? 465 HIS A C      1 
ATOM   927  O O      . HIS A 1 126 ? 2.569   18.921  -24.047 1.00 25.15  ? 465 HIS A O      1 
ATOM   928  C CB     . HIS A 1 126 ? 1.918   21.927  -23.920 1.00 22.45  ? 465 HIS A CB     1 
ATOM   929  C CG     . HIS A 1 126 ? 1.688   23.128  -24.783 1.00 18.86  ? 465 HIS A CG     1 
ATOM   930  N ND1    . HIS A 1 126 ? 2.346   24.323  -24.586 1.00 17.45  ? 465 HIS A ND1    1 
ATOM   931  C CD2    . HIS A 1 126 ? 0.876   23.317  -25.850 1.00 17.26  ? 465 HIS A CD2    1 
ATOM   932  C CE1    . HIS A 1 126 ? 1.947   25.198  -25.492 1.00 17.44  ? 465 HIS A CE1    1 
ATOM   933  N NE2    . HIS A 1 126 ? 1.055   24.612  -26.271 1.00 18.21  ? 465 HIS A NE2    1 
ATOM   934  N N      . ASN A 1 127 ? 0.946   19.046  -22.497 1.00 21.93  ? 466 ASN A N      1 
ATOM   935  C CA     . ASN A 1 127 ? 1.551   18.005  -21.678 1.00 19.66  ? 466 ASN A CA     1 
ATOM   936  C C      . ASN A 1 127 ? 0.622   16.820  -21.449 1.00 20.38  ? 466 ASN A C      1 
ATOM   937  O O      . ASN A 1 127 ? 1.043   15.665  -21.569 1.00 23.60  ? 466 ASN A O      1 
ATOM   938  C CB     . ASN A 1 127 ? 1.990   18.592  -20.336 1.00 21.09  ? 466 ASN A CB     1 
ATOM   939  C CG     . ASN A 1 127 ? 2.992   19.718  -20.494 1.00 20.13  ? 466 ASN A CG     1 
ATOM   940  O OD1    . ASN A 1 127 ? 2.738   20.854  -20.093 1.00 24.26  ? 466 ASN A OD1    1 
ATOM   941  N ND2    . ASN A 1 127 ? 4.139   19.409  -21.085 1.00 21.92  ? 466 ASN A ND2    1 
ATOM   942  N N      . TYR A 1 128 ? -0.640  17.089  -21.121 1.00 22.02  ? 467 TYR A N      1 
ATOM   943  C CA     . TYR A 1 128 ? -1.533  16.046  -20.638 1.00 26.16  ? 467 TYR A CA     1 
ATOM   944  C C      . TYR A 1 128 ? -2.676  15.724  -21.587 1.00 25.88  ? 467 TYR A C      1 
ATOM   945  O O      . TYR A 1 128 ? -3.407  14.757  -21.340 1.00 21.49  ? 467 TYR A O      1 
ATOM   946  C CB     . TYR A 1 128 ? -2.077  16.436  -19.258 1.00 20.84  ? 467 TYR A CB     1 
ATOM   947  C CG     . TYR A 1 128 ? -0.951  16.839  -18.342 1.00 20.84  ? 467 TYR A CG     1 
ATOM   948  C CD1    . TYR A 1 128 ? 0.019   15.919  -17.968 1.00 21.41  ? 467 TYR A CD1    1 
ATOM   949  C CD2    . TYR A 1 128 ? -0.830  18.143  -17.885 1.00 20.37  ? 467 TYR A CD2    1 
ATOM   950  C CE1    . TYR A 1 128 ? 1.065   16.279  -17.151 1.00 21.56  ? 467 TYR A CE1    1 
ATOM   951  C CE2    . TYR A 1 128 ? 0.213   18.513  -17.062 1.00 21.75  ? 467 TYR A CE2    1 
ATOM   952  C CZ     . TYR A 1 128 ? 1.159   17.576  -16.698 1.00 23.51  ? 467 TYR A CZ     1 
ATOM   953  O OH     . TYR A 1 128 ? 2.203   17.936  -15.878 1.00 27.46  ? 467 TYR A OH     1 
ATOM   954  N N      . ALA A 1 129 ? -2.853  16.493  -22.656 1.00 23.11  ? 468 ALA A N      1 
ATOM   955  C CA     . ALA A 1 129 ? -3.677  16.016  -23.755 1.00 24.42  ? 468 ALA A CA     1 
ATOM   956  C C      . ALA A 1 129 ? -3.071  14.729  -24.297 1.00 27.99  ? 468 ALA A C      1 
ATOM   957  O O      . ALA A 1 129 ? -1.848  14.596  -24.397 1.00 36.49  ? 468 ALA A O      1 
ATOM   958  C CB     . ALA A 1 129 ? -3.772  17.073  -24.854 1.00 24.38  ? 468 ALA A CB     1 
ATOM   959  N N      . ASN A 1 130 ? -3.929  13.764  -24.624 1.00 24.83  ? 469 ASN A N      1 
ATOM   960  C CA     . ASN A 1 130 ? -3.488  12.438  -25.048 1.00 28.98  ? 469 ASN A CA     1 
ATOM   961  C C      . ASN A 1 130 ? -3.815  12.243  -26.523 1.00 31.38  ? 469 ASN A C      1 
ATOM   962  O O      . ASN A 1 130 ? -4.914  11.782  -26.865 1.00 38.80  ? 469 ASN A O      1 
ATOM   963  C CB     . ASN A 1 130 ? -4.152  11.354  -24.192 1.00 27.17  ? 469 ASN A CB     1 
ATOM   964  C CG     . ASN A 1 130 ? -3.499  9.995   -24.356 1.00 28.46  ? 469 ASN A CG     1 
ATOM   965  O OD1    . ASN A 1 130 ? -2.590  9.640   -23.609 1.00 31.77  ? 469 ASN A OD1    1 
ATOM   966  N ND2    . ASN A 1 130 ? -3.964  9.226   -25.333 1.00 36.10  ? 469 ASN A ND2    1 
ATOM   967  N N      . PRO A 1 131 ? -2.897  12.574  -27.443 1.00 31.22  ? 470 PRO A N      1 
ATOM   968  C CA     . PRO A 1 131 ? -1.551  13.121  -27.230 1.00 28.95  ? 470 PRO A CA     1 
ATOM   969  C C      . PRO A 1 131 ? -1.534  14.645  -27.166 1.00 30.07  ? 470 PRO A C      1 
ATOM   970  O O      . PRO A 1 131 ? -2.555  15.292  -27.383 1.00 33.26  ? 470 PRO A O      1 
ATOM   971  C CB     . PRO A 1 131 ? -0.793  12.605  -28.454 1.00 30.16  ? 470 PRO A CB     1 
ATOM   972  C CG     . PRO A 1 131 ? -1.830  12.675  -29.543 1.00 32.75  ? 470 PRO A CG     1 
ATOM   973  C CD     . PRO A 1 131 ? -3.141  12.302  -28.873 1.00 34.50  ? 470 PRO A CD     1 
ATOM   974  N N      . PRO A 1 132 ? -0.380  15.242  -26.868 1.00 29.90  ? 471 PRO A N      1 
ATOM   975  C CA     . PRO A 1 132 ? -0.304  16.707  -26.813 1.00 25.04  ? 471 PRO A CA     1 
ATOM   976  C C      . PRO A 1 132 ? -0.656  17.334  -28.153 1.00 26.12  ? 471 PRO A C      1 
ATOM   977  O O      . PRO A 1 132 ? -0.499  16.726  -29.214 1.00 28.58  ? 471 PRO A O      1 
ATOM   978  C CB     . PRO A 1 132 ? 1.158   16.974  -26.436 1.00 22.06  ? 471 PRO A CB     1 
ATOM   979  C CG     . PRO A 1 132 ? 1.609   15.715  -25.765 1.00 26.55  ? 471 PRO A CG     1 
ATOM   980  C CD     . PRO A 1 132 ? 0.886   14.606  -26.471 1.00 28.96  ? 471 PRO A CD     1 
ATOM   981  N N      . HIS A 1 133 ? -1.133  18.575  -28.090 1.00 24.74  ? 472 HIS A N      1 
ATOM   982  C CA     . HIS A 1 133 ? -1.620  19.291  -29.261 1.00 24.17  ? 472 HIS A CA     1 
ATOM   983  C C      . HIS A 1 133 ? -1.171  20.741  -29.179 1.00 23.81  ? 472 HIS A C      1 
ATOM   984  O O      . HIS A 1 133 ? -1.282  21.366  -28.121 1.00 20.85  ? 472 HIS A O      1 
ATOM   985  C CB     . HIS A 1 133 ? -3.151  19.204  -29.351 1.00 26.13  ? 472 HIS A CB     1 
ATOM   986  C CG     . HIS A 1 133 ? -3.737  19.944  -30.514 1.00 28.70  ? 472 HIS A CG     1 
ATOM   987  N ND1    . HIS A 1 133 ? -4.386  21.153  -30.377 1.00 27.95  ? 472 HIS A ND1    1 
ATOM   988  C CD2    . HIS A 1 133 ? -3.782  19.642  -31.833 1.00 29.28  ? 472 HIS A CD2    1 
ATOM   989  C CE1    . HIS A 1 133 ? -4.802  21.565  -31.561 1.00 25.17  ? 472 HIS A CE1    1 
ATOM   990  N NE2    . HIS A 1 133 ? -4.448  20.666  -32.462 1.00 31.15  ? 472 HIS A NE2    1 
ATOM   991  N N      . VAL A 1 134 ? -0.659  21.268  -30.287 1.00 22.80  ? 473 VAL A N      1 
ATOM   992  C CA     . VAL A 1 134 ? -0.254  22.666  -30.369 1.00 20.46  ? 473 VAL A CA     1 
ATOM   993  C C      . VAL A 1 134 ? -1.416  23.478  -30.926 1.00 23.16  ? 473 VAL A C      1 
ATOM   994  O O      . VAL A 1 134 ? -2.006  23.115  -31.950 1.00 24.84  ? 473 VAL A O      1 
ATOM   995  C CB     . VAL A 1 134 ? 1.003   22.828  -31.238 1.00 21.09  ? 473 VAL A CB     1 
ATOM   996  C CG1    . VAL A 1 134 ? 1.302   24.299  -31.468 1.00 24.96  ? 473 VAL A CG1    1 
ATOM   997  C CG2    . VAL A 1 134 ? 2.190   22.137  -30.582 1.00 25.76  ? 473 VAL A CG2    1 
ATOM   998  N N      . HIS A 1 135 ? -1.745  24.580  -30.250 1.00 23.47  ? 474 HIS A N      1 
ATOM   999  C CA     . HIS A 1 135 ? -2.899  25.382  -30.646 1.00 26.96  ? 474 HIS A CA     1 
ATOM   1000 C C      . HIS A 1 135 ? -2.665  26.054  -31.994 1.00 24.31  ? 474 HIS A C      1 
ATOM   1001 O O      . HIS A 1 135 ? -3.381  25.791  -32.968 1.00 27.41  ? 474 HIS A O      1 
ATOM   1002 C CB     . HIS A 1 135 ? -3.201  26.419  -29.563 1.00 25.83  ? 474 HIS A CB     1 
ATOM   1003 C CG     . HIS A 1 135 ? -4.532  27.084  -29.717 1.00 20.54  ? 474 HIS A CG     1 
ATOM   1004 N ND1    . HIS A 1 135 ? -4.875  27.813  -30.834 1.00 21.83  ? 474 HIS A ND1    1 
ATOM   1005 C CD2    . HIS A 1 135 ? -5.603  27.134  -28.891 1.00 23.91  ? 474 HIS A CD2    1 
ATOM   1006 C CE1    . HIS A 1 135 ? -6.101  28.283  -30.691 1.00 26.45  ? 474 HIS A CE1    1 
ATOM   1007 N NE2    . HIS A 1 135 ? -6.566  27.884  -29.520 1.00 29.42  ? 474 HIS A NE2    1 
ATOM   1008 N N      . LYS A 1 136 ? -1.671  26.937  -32.065 1.00 23.28  ? 475 LYS A N      1 
ATOM   1009 C CA     . LYS A 1 136 ? -1.219  27.657  -33.250 1.00 26.55  ? 475 LYS A CA     1 
ATOM   1010 C C      . LYS A 1 136 ? -2.040  28.914  -33.527 1.00 23.00  ? 475 LYS A C      1 
ATOM   1011 O O      . LYS A 1 136 ? -1.635  29.714  -34.371 1.00 22.97  ? 475 LYS A O      1 
ATOM   1012 C CB     . LYS A 1 136 ? -1.210  26.790  -34.525 1.00 22.13  ? 475 LYS A CB     1 
ATOM   1013 C CG     . LYS A 1 136 ? -0.130  25.720  -34.548 1.00 26.52  ? 475 LYS A CG     1 
ATOM   1014 C CD     . LYS A 1 136 ? 0.363   25.461  -35.966 1.00 27.38  ? 475 LYS A CD     1 
ATOM   1015 C CE     . LYS A 1 136 ? -0.605  24.596  -36.756 1.00 35.20  ? 475 LYS A CE     1 
ATOM   1016 N NZ     . LYS A 1 136 ? -0.607  23.191  -36.262 1.00 42.09  ? 475 LYS A NZ     1 
ATOM   1017 N N      . ASN A 1 137 ? -3.167  29.127  -32.853 1.00 23.90  ? 476 ASN A N      1 
ATOM   1018 C CA     . ASN A 1 137 ? -4.068  30.222  -33.198 1.00 26.38  ? 476 ASN A CA     1 
ATOM   1019 C C      . ASN A 1 137 ? -4.619  30.885  -31.943 1.00 25.06  ? 476 ASN A C      1 
ATOM   1020 O O      . ASN A 1 137 ? -5.798  31.249  -31.880 1.00 27.18  ? 476 ASN A O      1 
ATOM   1021 C CB     . ASN A 1 137 ? -5.205  29.726  -34.093 1.00 27.01  ? 476 ASN A CB     1 
ATOM   1022 C CG     . ASN A 1 137 ? -6.052  30.853  -34.643 1.00 30.06  ? 476 ASN A CG     1 
ATOM   1023 O OD1    . ASN A 1 137 ? -5.586  31.983  -34.787 1.00 36.68  ? 476 ASN A OD1    1 
ATOM   1024 N ND2    . ASN A 1 137 ? -7.307  30.552  -34.951 1.00 35.38  ? 476 ASN A ND2    1 
ATOM   1025 N N      . LEU A 1 138 ? -3.775  31.060  -30.929 1.00 23.30  ? 477 LEU A N      1 
ATOM   1026 C CA     . LEU A 1 138 ? -4.209  31.671  -29.678 1.00 21.22  ? 477 LEU A CA     1 
ATOM   1027 C C      . LEU A 1 138 ? -4.229  33.188  -29.829 1.00 24.26  ? 477 LEU A C      1 
ATOM   1028 O O      . LEU A 1 138 ? -3.181  33.813  -30.028 1.00 24.34  ? 477 LEU A O      1 
ATOM   1029 C CB     . LEU A 1 138 ? -3.294  31.259  -28.529 1.00 19.59  ? 477 LEU A CB     1 
ATOM   1030 C CG     . LEU A 1 138 ? -3.712  31.790  -27.155 1.00 21.39  ? 477 LEU A CG     1 
ATOM   1031 C CD1    . LEU A 1 138 ? -5.034  31.175  -26.716 1.00 15.12  ? 477 LEU A CD1    1 
ATOM   1032 C CD2    . LEU A 1 138 ? -2.626  31.542  -26.120 1.00 19.00  ? 477 LEU A CD2    1 
ATOM   1033 N N      . LYS A 1 139 ? -5.419  33.776  -29.727 1.00 21.83  ? 478 LYS A N      1 
ATOM   1034 C CA     . LYS A 1 139 ? -5.596  35.214  -29.864 1.00 24.01  ? 478 LYS A CA     1 
ATOM   1035 C C      . LYS A 1 139 ? -6.652  35.682  -28.873 1.00 22.39  ? 478 LYS A C      1 
ATOM   1036 O O      . LYS A 1 139 ? -7.466  34.896  -28.384 1.00 23.65  ? 478 LYS A O      1 
ATOM   1037 C CB     . LYS A 1 139 ? -6.008  35.599  -31.291 1.00 24.43  ? 478 LYS A CB     1 
ATOM   1038 C CG     . LYS A 1 139 ? -5.036  35.152  -32.371 1.00 27.99  ? 478 LYS A CG     1 
ATOM   1039 C CD     . LYS A 1 139 ? -5.676  35.251  -33.747 1.00 26.77  ? 478 LYS A CD     1 
ATOM   1040 C CE     . LYS A 1 139 ? -4.632  35.241  -34.854 1.00 26.30  ? 478 LYS A CE     1 
ATOM   1041 N NZ     . LYS A 1 139 ? -3.734  34.060  -34.772 1.00 22.24  ? 478 LYS A NZ     1 
ATOM   1042 N N      . SER A 1 140 ? -6.630  36.984  -28.581 1.00 21.11  ? 479 SER A N      1 
ATOM   1043 C CA     . SER A 1 140 ? -7.642  37.552  -27.696 1.00 23.08  ? 479 SER A CA     1 
ATOM   1044 C C      . SER A 1 140 ? -9.043  37.321  -28.249 1.00 23.49  ? 479 SER A C      1 
ATOM   1045 O O      . SER A 1 140 ? -9.987  37.076  -27.489 1.00 20.61  ? 479 SER A O      1 
ATOM   1046 C CB     . SER A 1 140 ? -7.380  39.044  -27.486 1.00 20.64  ? 479 SER A CB     1 
ATOM   1047 O OG     . SER A 1 140 ? -7.355  39.740  -28.719 1.00 26.79  ? 479 SER A OG     1 
ATOM   1048 N N      . GLY A 1 141 ? -9.196  37.390  -29.574 1.00 24.54  ? 480 GLY A N      1 
ATOM   1049 C CA     . GLY A 1 141 ? -10.492 37.153  -30.184 1.00 27.93  ? 480 GLY A CA     1 
ATOM   1050 C C      . GLY A 1 141 ? -10.957 35.715  -30.106 1.00 25.47  ? 480 GLY A C      1 
ATOM   1051 O O      . GLY A 1 141 ? -12.158 35.456  -30.229 1.00 25.39  ? 480 GLY A O      1 
ATOM   1052 N N      . ASN A 1 142 ? -10.034 34.775  -29.904 1.00 27.51  ? 481 ASN A N      1 
ATOM   1053 C CA     . ASN A 1 142 ? -10.383 33.367  -29.764 1.00 24.12  ? 481 ASN A CA     1 
ATOM   1054 C C      . ASN A 1 142 ? -10.614 32.954  -28.319 1.00 22.12  ? 481 ASN A C      1 
ATOM   1055 O O      . ASN A 1 142 ? -11.226 31.907  -28.078 1.00 25.83  ? 481 ASN A O      1 
ATOM   1056 C CB     . ASN A 1 142 ? -9.282  32.485  -30.364 1.00 22.72  ? 481 ASN A CB     1 
ATOM   1057 C CG     . ASN A 1 142 ? -9.123  32.686  -31.857 1.00 33.31  ? 481 ASN A CG     1 
ATOM   1058 O OD1    . ASN A 1 142 ? -10.107 32.778  -32.593 1.00 44.01  ? 481 ASN A OD1    1 
ATOM   1059 N ND2    . ASN A 1 142 ? -7.876  32.762  -32.313 1.00 29.33  ? 481 ASN A ND2    1 
ATOM   1060 N N      . ILE A 1 143 ? -10.137 33.744  -27.359 1.00 21.69  ? 482 ILE A N      1 
ATOM   1061 C CA     . ILE A 1 143 ? -10.285 33.433  -25.939 1.00 22.74  ? 482 ILE A CA     1 
ATOM   1062 C C      . ILE A 1 143 ? -11.659 33.933  -25.503 1.00 20.29  ? 482 ILE A C      1 
ATOM   1063 O O      . ILE A 1 143 ? -11.874 35.135  -25.334 1.00 21.55  ? 482 ILE A O      1 
ATOM   1064 C CB     . ILE A 1 143 ? -9.162  34.049  -25.102 1.00 19.31  ? 482 ILE A CB     1 
ATOM   1065 C CG1    . ILE A 1 143 ? -7.824  33.404  -25.471 1.00 20.46  ? 482 ILE A CG1    1 
ATOM   1066 C CG2    . ILE A 1 143 ? -9.452  33.889  -23.616 1.00 17.21  ? 482 ILE A CG2    1 
ATOM   1067 C CD1    . ILE A 1 143 ? -6.617  34.214  -25.069 1.00 19.05  ? 482 ILE A CD1    1 
ATOM   1068 N N      . LEU A 1 144 ? -12.597 33.009  -25.324 1.00 20.94  ? 483 LEU A N      1 
ATOM   1069 C CA     . LEU A 1 144 ? -13.940 33.371  -24.909 1.00 25.20  ? 483 LEU A CA     1 
ATOM   1070 C C      . LEU A 1 144 ? -14.018 33.482  -23.389 1.00 22.66  ? 483 LEU A C      1 
ATOM   1071 O O      . LEU A 1 144 ? -13.127 33.047  -22.655 1.00 21.04  ? 483 LEU A O      1 
ATOM   1072 C CB     . LEU A 1 144 ? -14.957 32.354  -25.424 1.00 19.80  ? 483 LEU A CB     1 
ATOM   1073 C CG     . LEU A 1 144 ? -14.975 32.148  -26.939 1.00 25.03  ? 483 LEU A CG     1 
ATOM   1074 C CD1    . LEU A 1 144 ? -16.093 31.201  -27.348 1.00 25.02  ? 483 LEU A CD1    1 
ATOM   1075 C CD2    . LEU A 1 144 ? -15.102 33.480  -27.659 1.00 26.60  ? 483 LEU A CD2    1 
ATOM   1076 N N      . LEU A 1 145 ? -15.103 34.090  -22.925 1.00 22.48  ? 484 LEU A N      1 
ATOM   1077 C CA     . LEU A 1 145 ? -15.375 34.256  -21.508 1.00 24.48  ? 484 LEU A CA     1 
ATOM   1078 C C      . LEU A 1 145 ? -16.772 33.731  -21.221 1.00 25.77  ? 484 LEU A C      1 
ATOM   1079 O O      . LEU A 1 145 ? -17.664 33.815  -22.069 1.00 28.52  ? 484 LEU A O      1 
ATOM   1080 C CB     . LEU A 1 145 ? -15.260 35.726  -21.084 1.00 24.84  ? 484 LEU A CB     1 
ATOM   1081 C CG     . LEU A 1 145 ? -14.025 36.476  -21.592 1.00 21.71  ? 484 LEU A CG     1 
ATOM   1082 C CD1    . LEU A 1 145 ? -14.152 37.964  -21.322 1.00 20.39  ? 484 LEU A CD1    1 
ATOM   1083 C CD2    . LEU A 1 145 ? -12.751 35.922  -20.971 1.00 20.70  ? 484 LEU A CD2    1 
ATOM   1084 N N      . ASP A 1 146 ? -16.953 33.163  -20.034 1.00 22.96  ? 485 ASP A N      1 
ATOM   1085 C CA     . ASP A 1 146 ? -18.258 32.659  -19.644 1.00 25.39  ? 485 ASP A CA     1 
ATOM   1086 C C      . ASP A 1 146 ? -18.959 33.687  -18.750 1.00 29.69  ? 485 ASP A C      1 
ATOM   1087 O O      . ASP A 1 146 ? -18.557 34.855  -18.689 1.00 31.78  ? 485 ASP A O      1 
ATOM   1088 C CB     . ASP A 1 146 ? -18.111 31.284  -18.976 1.00 22.25  ? 485 ASP A CB     1 
ATOM   1089 C CG     . ASP A 1 146 ? -17.419 31.353  -17.630 1.00 26.87  ? 485 ASP A CG     1 
ATOM   1090 O OD1    . ASP A 1 146 ? -16.899 32.429  -17.268 1.00 29.00  ? 485 ASP A OD1    1 
ATOM   1091 O OD2    . ASP A 1 146 ? -17.398 30.324  -16.926 1.00 30.34  ? 485 ASP A OD2    1 
ATOM   1092 N N      . GLY A 1 147 ? -20.019 33.263  -18.060 1.00 26.08  ? 486 GLY A N      1 
ATOM   1093 C CA     . GLY A 1 147 ? -20.770 34.187  -17.228 1.00 28.19  ? 486 GLY A CA     1 
ATOM   1094 C C      . GLY A 1 147 ? -19.965 34.746  -16.072 1.00 30.18  ? 486 GLY A C      1 
ATOM   1095 O O      . GLY A 1 147 ? -20.228 35.860  -15.610 1.00 28.00  ? 486 GLY A O      1 
ATOM   1096 N N      . LYS A 1 148 ? -18.990 33.983  -15.580 1.00 29.73  ? 487 LYS A N      1 
ATOM   1097 C CA     . LYS A 1 148 ? -18.080 34.445  -14.542 1.00 25.97  ? 487 LYS A CA     1 
ATOM   1098 C C      . LYS A 1 148 ? -16.756 34.938  -15.118 1.00 26.54  ? 487 LYS A C      1 
ATOM   1099 O O      . LYS A 1 148 ? -15.751 34.985  -14.401 1.00 29.82  ? 487 LYS A O      1 
ATOM   1100 C CB     . LYS A 1 148 ? -17.856 33.336  -13.512 1.00 26.16  ? 487 LYS A CB     1 
ATOM   1101 C CG     . LYS A 1 148 ? -19.051 33.144  -12.589 1.00 27.90  ? 487 LYS A CG     1 
ATOM   1102 C CD     . LYS A 1 148 ? -18.952 31.882  -11.751 1.00 31.76  ? 487 LYS A CD     1 
ATOM   1103 C CE     . LYS A 1 148 ? -19.987 31.909  -10.635 1.00 35.72  ? 487 LYS A CE     1 
ATOM   1104 N NZ     . LYS A 1 148 ? -20.667 30.598  -10.459 1.00 39.77  ? 487 LYS A NZ     1 
ATOM   1105 N N      . PHE A 1 149 ? -16.746 35.311  -16.399 1.00 24.65  ? 488 PHE A N      1 
ATOM   1106 C CA     . PHE A 1 149 ? -15.580 35.916  -17.044 1.00 24.71  ? 488 PHE A CA     1 
ATOM   1107 C C      . PHE A 1 149 ? -14.348 35.027  -16.916 1.00 27.23  ? 488 PHE A C      1 
ATOM   1108 O O      . PHE A 1 149 ? -13.241 35.495  -16.636 1.00 32.10  ? 488 PHE A O      1 
ATOM   1109 C CB     . PHE A 1 149 ? -15.316 37.318  -16.494 1.00 25.49  ? 488 PHE A CB     1 
ATOM   1110 C CG     . PHE A 1 149 ? -16.330 38.330  -16.935 1.00 27.42  ? 488 PHE A CG     1 
ATOM   1111 C CD1    . PHE A 1 149 ? -17.560 38.414  -16.306 1.00 29.59  ? 488 PHE A CD1    1 
ATOM   1112 C CD2    . PHE A 1 149 ? -16.062 39.182  -17.992 1.00 27.96  ? 488 PHE A CD2    1 
ATOM   1113 C CE1    . PHE A 1 149 ? -18.503 39.337  -16.718 1.00 32.38  ? 488 PHE A CE1    1 
ATOM   1114 C CE2    . PHE A 1 149 ? -16.999 40.107  -18.409 1.00 27.22  ? 488 PHE A CE2    1 
ATOM   1115 C CZ     . PHE A 1 149 ? -18.221 40.185  -17.772 1.00 30.08  ? 488 PHE A CZ     1 
ATOM   1116 N N      . ARG A 1 150 ? -14.546 33.732  -17.126 1.00 23.16  ? 489 ARG A N      1 
ATOM   1117 C CA     . ARG A 1 150 ? -13.471 32.756  -17.140 1.00 21.26  ? 489 ARG A CA     1 
ATOM   1118 C C      . ARG A 1 150 ? -13.142 32.377  -18.579 1.00 22.17  ? 489 ARG A C      1 
ATOM   1119 O O      . ARG A 1 150 ? -14.013 32.370  -19.453 1.00 23.10  ? 489 ARG A O      1 
ATOM   1120 C CB     . ARG A 1 150 ? -13.864 31.520  -16.331 1.00 24.21  ? 489 ARG A CB     1 
ATOM   1121 C CG     . ARG A 1 150 ? -14.424 31.868  -14.961 1.00 28.15  ? 489 ARG A CG     1 
ATOM   1122 C CD     . ARG A 1 150 ? -14.756 30.631  -14.149 1.00 32.90  ? 489 ARG A CD     1 
ATOM   1123 N NE     . ARG A 1 150 ? -13.681 29.647  -14.187 1.00 38.57  ? 489 ARG A NE     1 
ATOM   1124 C CZ     . ARG A 1 150 ? -12.446 29.864  -13.754 1.00 40.03  ? 489 ARG A CZ     1 
ATOM   1125 N NH1    . ARG A 1 150 ? -12.076 31.042  -13.277 1.00 38.17  ? 489 ARG A NH1    1 
ATOM   1126 N NH2    . ARG A 1 150 ? -11.556 28.877  -13.811 1.00 36.70  ? 489 ARG A NH2    1 
ATOM   1127 N N      . GLY A 1 151 ? -11.870 32.066  -18.817 1.00 20.60  ? 490 GLY A N      1 
ATOM   1128 C CA     . GLY A 1 151 ? -11.390 31.875  -20.176 1.00 16.10  ? 490 GLY A CA     1 
ATOM   1129 C C      . GLY A 1 151 ? -11.826 30.543  -20.765 1.00 17.04  ? 490 GLY A C      1 
ATOM   1130 O O      . GLY A 1 151 ? -11.897 29.524  -20.078 1.00 22.39  ? 490 GLY A O      1 
ATOM   1131 N N      . LYS A 1 152 ? -12.110 30.563  -22.067 1.00 22.40  ? 491 LYS A N      1 
ATOM   1132 C CA     . LYS A 1 152 ? -12.532 29.374  -22.809 1.00 22.84  ? 491 LYS A CA     1 
ATOM   1133 C C      . LYS A 1 152 ? -11.891 29.438  -24.194 1.00 23.36  ? 491 LYS A C      1 
ATOM   1134 O O      . LYS A 1 152 ? -12.410 30.111  -25.090 1.00 25.00  ? 491 LYS A O      1 
ATOM   1135 C CB     . LYS A 1 152 ? -14.051 29.298  -22.906 1.00 20.22  ? 491 LYS A CB     1 
ATOM   1136 C CG     . LYS A 1 152 ? -14.773 29.281  -21.568 1.00 19.64  ? 491 LYS A CG     1 
ATOM   1137 C CD     . LYS A 1 152 ? -15.009 27.864  -21.068 1.00 18.93  ? 491 LYS A CD     1 
ATOM   1138 C CE     . LYS A 1 152 ? -15.720 27.872  -19.724 1.00 20.39  ? 491 LYS A CE     1 
ATOM   1139 N NZ     . LYS A 1 152 ? -16.117 26.506  -19.286 1.00 23.34  ? 491 LYS A NZ     1 
ATOM   1140 N N      . VAL A 1 153 ? -10.767 28.736  -24.368 1.00 23.29  ? 492 VAL A N      1 
ATOM   1141 C CA     . VAL A 1 153 ? -10.102 28.716  -25.664 1.00 25.30  ? 492 VAL A CA     1 
ATOM   1142 C C      . VAL A 1 153 ? -11.024 28.075  -26.701 1.00 24.83  ? 492 VAL A C      1 
ATOM   1143 O O      . VAL A 1 153 ? -11.843 27.205  -26.382 1.00 28.44  ? 492 VAL A O      1 
ATOM   1144 C CB     . VAL A 1 153 ? -8.760  27.968  -25.576 1.00 22.35  ? 492 VAL A CB     1 
ATOM   1145 C CG1    . VAL A 1 153 ? -7.871  28.330  -26.756 1.00 32.98  ? 492 VAL A CG1    1 
ATOM   1146 C CG2    . VAL A 1 153 ? -8.063  28.275  -24.256 1.00 20.68  ? 492 VAL A CG2    1 
ATOM   1147 N N      . SER A 1 154 ? -10.889 28.501  -27.960 1.00 28.19  ? 493 SER A N      1 
ATOM   1148 C CA     . SER A 1 154 ? -11.851 28.079  -28.974 1.00 32.25  ? 493 SER A CA     1 
ATOM   1149 C C      . SER A 1 154 ? -11.216 27.586  -30.273 1.00 37.41  ? 493 SER A C      1 
ATOM   1150 O O      . SER A 1 154 ? -11.265 26.389  -30.576 1.00 42.15  ? 493 SER A O      1 
ATOM   1151 C CB     . SER A 1 154 ? -12.822 29.224  -29.284 1.00 27.69  ? 493 SER A CB     1 
ATOM   1152 O OG     . SER A 1 154 ? -12.174 30.283  -29.967 1.00 41.73  ? 493 SER A OG     1 
ATOM   1153 N N      . ASN A 1 155 ? -10.640 28.495  -31.062 1.00 32.51  ? 494 ASN A N      1 
ATOM   1154 C CA     . ASN A 1 155 ? -10.242 28.190  -32.441 1.00 37.57  ? 494 ASN A CA     1 
ATOM   1155 C C      . ASN A 1 155 ? -8.898  27.459  -32.462 1.00 35.96  ? 494 ASN A C      1 
ATOM   1156 O O      . ASN A 1 155 ? -7.888  27.946  -32.974 1.00 33.89  ? 494 ASN A O      1 
ATOM   1157 C CB     . ASN A 1 155 ? -10.183 29.465  -33.273 1.00 34.85  ? 494 ASN A CB     1 
ATOM   1158 C CG     . ASN A 1 155 ? -11.559 30.001  -33.627 1.00 37.57  ? 494 ASN A CG     1 
ATOM   1159 O OD1    . ASN A 1 155 ? -12.547 29.705  -32.958 1.00 35.67  ? 494 ASN A OD1    1 
ATOM   1160 N ND2    . ASN A 1 155 ? -11.627 30.795  -34.691 1.00 46.57  ? 494 ASN A ND2    1 
ATOM   1161 N N      . PHE A 1 156 ? -8.907  26.245  -31.913 1.00 36.61  ? 495 PHE A N      1 
ATOM   1162 C CA     . PHE A 1 156 ? -7.695  25.443  -31.841 1.00 34.89  ? 495 PHE A CA     1 
ATOM   1163 C C      . PHE A 1 156 ? -7.611  24.353  -32.906 1.00 36.63  ? 495 PHE A C      1 
ATOM   1164 O O      . PHE A 1 156 ? -6.579  23.681  -32.990 1.00 37.22  ? 495 PHE A O      1 
ATOM   1165 C CB     . PHE A 1 156 ? -7.551  24.808  -30.447 1.00 31.93  ? 495 PHE A CB     1 
ATOM   1166 C CG     . PHE A 1 156 ? -8.821  24.223  -29.905 1.00 31.98  ? 495 PHE A CG     1 
ATOM   1167 C CD1    . PHE A 1 156 ? -9.305  23.016  -30.381 1.00 43.89  ? 495 PHE A CD1    1 
ATOM   1168 C CD2    . PHE A 1 156 ? -9.522  24.871  -28.904 1.00 30.15  ? 495 PHE A CD2    1 
ATOM   1169 C CE1    . PHE A 1 156 ? -10.475 22.474  -29.879 1.00 47.24  ? 495 PHE A CE1    1 
ATOM   1170 C CE2    . PHE A 1 156 ? -10.692 24.338  -28.398 1.00 41.28  ? 495 PHE A CE2    1 
ATOM   1171 C CZ     . PHE A 1 156 ? -11.170 23.137  -28.885 1.00 50.50  ? 495 PHE A CZ     1 
ATOM   1172 N N      . GLY A 1 157 ? -8.645  24.163  -33.723 1.00 44.13  ? 496 GLY A N      1 
ATOM   1173 C CA     . GLY A 1 157 ? -8.589  23.116  -34.729 1.00 51.36  ? 496 GLY A CA     1 
ATOM   1174 C C      . GLY A 1 157 ? -9.658  23.199  -35.800 1.00 54.89  ? 496 GLY A C      1 
ATOM   1175 O O      . GLY A 1 157 ? -10.805 23.557  -35.517 1.00 60.45  ? 496 GLY A O      1 
ATOM   1176 N N      . LEU A 1 158 ? -9.289  22.885  -37.043 1.00 47.44  ? 497 LEU A N      1 
ATOM   1177 C CA     . LEU A 1 158 ? -10.228 22.872  -38.162 1.00 49.55  ? 497 LEU A CA     1 
ATOM   1178 C C      . LEU A 1 158 ? -10.696 24.273  -38.542 1.00 54.13  ? 497 LEU A C      1 
ATOM   1179 O O      . LEU A 1 158 ? -11.081 24.510  -39.693 1.00 49.08  ? 497 LEU A O      1 
ATOM   1180 C CB     . LEU A 1 158 ? -11.428 21.978  -37.842 1.00 45.17  ? 497 LEU A CB     1 
ATOM   1181 C CG     . LEU A 1 158 ? -11.439 20.620  -38.547 1.00 46.41  ? 497 LEU A CG     1 
ATOM   1182 C CD1    . LEU A 1 158 ? -12.592 19.770  -38.040 1.00 46.84  ? 497 LEU A CD1    1 
ATOM   1183 C CD2    . LEU A 1 158 ? -11.529 20.801  -40.055 1.00 44.02  ? 497 LEU A CD2    1 
ATOM   1184 N N      . ALA A 1 159 ? -10.674 25.204  -37.587 1.00 57.82  ? 498 ALA A N      1 
ATOM   1185 C CA     . ALA A 1 159 ? -10.933 26.610  -37.859 1.00 55.17  ? 498 ALA A CA     1 
ATOM   1186 C C      . ALA A 1 159 ? -9.665  27.381  -38.198 1.00 62.56  ? 498 ALA A C      1 
ATOM   1187 O O      . ALA A 1 159 ? -9.754  28.556  -38.573 1.00 61.78  ? 498 ALA A O      1 
ATOM   1188 C CB     . ALA A 1 159 ? -11.630 27.265  -36.660 1.00 45.87  ? 498 ALA A CB     1 
ATOM   1189 N N      . ARG A 1 160 ? -8.494  26.757  -38.067 1.00 50.26  ? 499 ARG A N      1 
ATOM   1190 C CA     . ARG A 1 160 ? -7.247  27.384  -38.489 1.00 51.87  ? 499 ARG A CA     1 
ATOM   1191 C C      . ARG A 1 160 ? -7.146  27.393  -40.013 1.00 52.05  ? 499 ARG A C      1 
ATOM   1192 O O      . ARG A 1 160 ? -7.737  26.557  -40.702 1.00 54.97  ? 499 ARG A O      1 
ATOM   1193 C CB     . ARG A 1 160 ? -6.055  26.666  -37.858 1.00 49.34  ? 499 ARG A CB     1 
ATOM   1194 C CG     . ARG A 1 160 ? -6.096  26.690  -36.339 1.00 43.20  ? 499 ARG A CG     1 
ATOM   1195 C CD     . ARG A 1 160 ? -5.206  25.626  -35.722 1.00 41.42  ? 499 ARG A CD     1 
ATOM   1196 N NE     . ARG A 1 160 ? -5.731  24.284  -35.940 1.00 41.72  ? 499 ARG A NE     1 
ATOM   1197 C CZ     . ARG A 1 160 ? -5.095  23.166  -35.615 1.00 39.97  ? 499 ARG A CZ     1 
ATOM   1198 N NH1    . ARG A 1 160 ? -3.900  23.189  -35.048 1.00 38.91  ? 499 ARG A NH1    1 
ATOM   1199 N NH2    . ARG A 1 160 ? -5.673  21.995  -35.868 1.00 36.90  ? 499 ARG A NH2    1 
ATOM   1200 N N      . VAL A 1 161 ? -6.375  28.351  -40.538 1.00 51.50  ? 500 VAL A N      1 
ATOM   1201 C CA     . VAL A 1 161 ? -6.575  28.799  -41.918 1.00 53.74  ? 500 VAL A CA     1 
ATOM   1202 C C      . VAL A 1 161 ? -6.349  27.660  -42.908 1.00 67.47  ? 500 VAL A C      1 
ATOM   1203 O O      . VAL A 1 161 ? -7.148  27.446  -43.829 1.00 64.39  ? 500 VAL A O      1 
ATOM   1204 C CB     . VAL A 1 161 ? -5.677  30.010  -42.228 1.00 47.08  ? 500 VAL A CB     1 
ATOM   1205 C CG1    . VAL A 1 161 ? -5.219  29.967  -43.672 1.00 40.43  ? 500 VAL A CG1    1 
ATOM   1206 C CG2    . VAL A 1 161 ? -6.443  31.304  -41.960 1.00 44.00  ? 500 VAL A CG2    1 
ATOM   1207 N N      . MET A 1 162 ? -5.252  26.926  -42.749 1.00 60.36  ? 501 MET A N      1 
ATOM   1208 C CA     . MET A 1 162 ? -4.949  25.807  -43.631 1.00 52.63  ? 501 MET A CA     1 
ATOM   1209 C C      . MET A 1 162 ? -5.177  24.452  -42.968 1.00 54.32  ? 501 MET A C      1 
ATOM   1210 O O      . MET A 1 162 ? -4.875  23.421  -43.577 1.00 54.47  ? 501 MET A O      1 
ATOM   1211 C CB     . MET A 1 162 ? -3.515  25.918  -44.159 1.00 48.32  ? 501 MET A CB     1 
ATOM   1212 C CG     . MET A 1 162 ? -3.396  26.712  -45.465 1.00 41.91  ? 501 MET A CG     1 
ATOM   1213 S SD     . MET A 1 162 ? -4.548  26.167  -46.753 1.00 50.04  ? 501 MET A SD     1 
ATOM   1214 C CE     . MET A 1 162 ? -5.630  27.590  -46.876 1.00 41.68  ? 501 MET A CE     1 
ATOM   1215 N N      . GLU A 1 163 ? -5.715  24.420  -41.746 1.00 52.90  ? 502 GLU A N      1 
ATOM   1216 C CA     . GLU A 1 163 ? -6.117  23.138  -41.171 1.00 55.20  ? 502 GLU A CA     1 
ATOM   1217 C C      . GLU A 1 163 ? -7.392  22.608  -41.819 1.00 61.75  ? 502 GLU A C      1 
ATOM   1218 O O      . GLU A 1 163 ? -7.565  21.389  -41.939 1.00 66.16  ? 502 GLU A O      1 
ATOM   1219 C CB     . GLU A 1 163 ? -6.298  23.265  -39.658 1.00 54.01  ? 502 GLU A CB     1 
ATOM   1220 C CG     . GLU A 1 163 ? -5.096  23.868  -38.963 1.00 53.38  ? 502 GLU A CG     1 
ATOM   1221 C CD     . GLU A 1 163 ? -3.794  23.320  -39.503 1.00 47.61  ? 502 GLU A CD     1 
ATOM   1222 O OE1    . GLU A 1 163 ? -3.626  22.082  -39.517 1.00 49.52  ? 502 GLU A OE1    1 
ATOM   1223 O OE2    . GLU A 1 163 ? -2.946  24.130  -39.930 1.00 41.13  ? 502 GLU A OE2    1 
ATOM   1224 N N      . ASN A 1 164 ? -8.289  23.497  -42.245 1.00 60.18  ? 503 ASN A N      1 
ATOM   1225 C CA     . ASN A 1 164 ? -9.504  23.061  -42.922 1.00 56.11  ? 503 ASN A CA     1 
ATOM   1226 C C      . ASN A 1 164 ? -9.168  22.250  -44.169 1.00 62.34  ? 503 ASN A C      1 
ATOM   1227 O O      . ASN A 1 164 ? -8.440  22.713  -45.054 1.00 56.06  ? 503 ASN A O      1 
ATOM   1228 C CB     . ASN A 1 164 ? -10.372 24.268  -43.291 1.00 59.27  ? 503 ASN A CB     1 
ATOM   1229 C CG     . ASN A 1 164 ? -9.551  25.514  -43.584 1.00 65.15  ? 503 ASN A CG     1 
ATOM   1230 O OD1    . ASN A 1 164 ? -9.505  26.445  -42.778 1.00 61.40  ? 503 ASN A OD1    1 
ATOM   1231 N ND2    . ASN A 1 164 ? -8.883  25.528  -44.734 1.00 66.46  ? 503 ASN A ND2    1 
ATOM   1232 N N      . GLU A 1 165 ? -9.710  21.031  -44.236 1.00 78.56  ? 504 GLU A N      1 
ATOM   1233 C CA     . GLU A 1 165 ? -9.530  20.200  -45.424 1.00 71.77  ? 504 GLU A CA     1 
ATOM   1234 C C      . GLU A 1 165 ? -10.204 20.829  -46.635 1.00 72.94  ? 504 GLU A C      1 
ATOM   1235 O O      . GLU A 1 165 ? -9.576  21.006  -47.685 1.00 74.76  ? 504 GLU A O      1 
ATOM   1236 C CB     . GLU A 1 165 ? -10.074 18.793  -45.173 1.00 65.10  ? 504 GLU A CB     1 
ATOM   1237 C CG     . GLU A 1 165 ? -9.932  17.844  -46.354 1.00 80.15  ? 504 GLU A CG     1 
ATOM   1238 C CD     . GLU A 1 165 ? -8.497  17.428  -46.604 1.00 78.49  ? 504 GLU A CD     1 
ATOM   1239 O OE1    . GLU A 1 165 ? -7.584  18.009  -45.982 1.00 68.20  ? 504 GLU A OE1    1 
ATOM   1240 O OE2    . GLU A 1 165 ? -8.283  16.515  -47.427 1.00 64.28  ? 504 GLU A OE2    1 
ATOM   1241 N N      . GLY A 1 166 ? -11.488 21.154  -46.517 1.00 64.17  ? 505 GLY A N      1 
ATOM   1242 C CA     . GLY A 1 166 ? -12.122 21.995  -47.507 1.00 57.67  ? 505 GLY A CA     1 
ATOM   1243 C C      . GLY A 1 166 ? -11.566 23.402  -47.446 1.00 71.58  ? 505 GLY A C      1 
ATOM   1244 O O      . GLY A 1 166 ? -11.899 24.169  -46.537 1.00 74.53  ? 505 GLY A O      1 
ATOM   1245 N N      . GLY A 1 167 ? -10.698 23.746  -48.392 1.00 86.44  ? 506 GLY A N      1 
ATOM   1246 C CA     . GLY A 1 167 ? -10.184 25.094  -48.488 1.00 88.04  ? 506 GLY A CA     1 
ATOM   1247 C C      . GLY A 1 167 ? -11.293 26.086  -48.785 1.00 95.99  ? 506 GLY A C      1 
ATOM   1248 O O      . GLY A 1 167 ? -12.446 25.733  -49.038 1.00 99.75  ? 506 GLY A O      1 
ATOM   1249 N N      . ASP A 1 168 ? -10.928 27.366  -48.758 1.00 80.60  ? 507 ASP A N      1 
ATOM   1250 C CA     . ASP A 1 168 ? -11.923 28.418  -48.888 1.00 86.10  ? 507 ASP A CA     1 
ATOM   1251 C C      . ASP A 1 168 ? -11.379 29.590  -49.690 1.00 81.33  ? 507 ASP A C      1 
ATOM   1252 O O      . ASP A 1 168 ? -10.172 29.848  -49.719 1.00 82.86  ? 507 ASP A O      1 
ATOM   1253 C CB     . ASP A 1 168 ? -12.399 28.912  -47.511 1.00 101.79 ? 507 ASP A CB     1 
ATOM   1254 C CG     . ASP A 1 168 ? -13.286 27.904  -46.799 1.00 111.74 ? 507 ASP A CG     1 
ATOM   1255 O OD1    . ASP A 1 168 ? -13.955 27.104  -47.494 1.00 109.53 ? 507 ASP A OD1    1 
ATOM   1256 O OD2    . ASP A 1 168 ? -13.311 27.919  -45.547 1.00 113.08 ? 507 ASP A OD2    1 
ATOM   1257 N N      . GLU A 1 169 ? -12.302 30.298  -50.342 1.00 75.14  ? 508 GLU A N      1 
ATOM   1258 C CA     . GLU A 1 169 ? -12.028 31.572  -50.987 1.00 66.52  ? 508 GLU A CA     1 
ATOM   1259 C C      . GLU A 1 169 ? -12.873 32.706  -50.421 1.00 70.64  ? 508 GLU A C      1 
ATOM   1260 O O      . GLU A 1 169 ? -12.717 33.853  -50.855 1.00 64.83  ? 508 GLU A O      1 
ATOM   1261 C CB     . GLU A 1 169 ? -12.246 31.463  -52.503 1.00 61.70  ? 508 GLU A CB     1 
ATOM   1262 C CG     . GLU A 1 169 ? -11.076 30.830  -53.238 1.00 56.42  ? 508 GLU A CG     1 
ATOM   1263 C CD     . GLU A 1 169 ? -9.818  31.673  -53.152 1.00 50.16  ? 508 GLU A CD     1 
ATOM   1264 O OE1    . GLU A 1 169 ? -9.842  32.827  -53.630 1.00 57.65  ? 508 GLU A OE1    1 
ATOM   1265 O OE2    . GLU A 1 169 ? -8.809  31.189  -52.598 1.00 44.90  ? 508 GLU A OE2    1 
ATOM   1266 N N      . GLY A 1 170 ? -13.768 32.419  -49.476 1.00 65.46  ? 509 GLY A N      1 
ATOM   1267 C CA     . GLY A 1 170 ? -14.438 33.461  -48.721 1.00 53.77  ? 509 GLY A CA     1 
ATOM   1268 C C      . GLY A 1 170 ? -13.582 33.865  -47.540 1.00 56.04  ? 509 GLY A C      1 
ATOM   1269 O O      . GLY A 1 170 ? -14.006 33.775  -46.383 1.00 59.93  ? 509 GLY A O      1 
ATOM   1270 N N      . PHE A 1 171 ? -12.368 34.319  -47.834 1.00 55.73  ? 510 PHE A N      1 
ATOM   1271 C CA     . PHE A 1 171 ? -11.304 34.470  -46.854 1.00 46.57  ? 510 PHE A CA     1 
ATOM   1272 C C      . PHE A 1 171 ? -10.868 35.926  -46.767 1.00 45.98  ? 510 PHE A C      1 
ATOM   1273 O O      . PHE A 1 171 ? -10.702 36.597  -47.791 1.00 45.40  ? 510 PHE A O      1 
ATOM   1274 C CB     . PHE A 1 171 ? -10.122 33.565  -47.232 1.00 45.64  ? 510 PHE A CB     1 
ATOM   1275 C CG     . PHE A 1 171 ? -8.852  33.873  -46.499 1.00 38.68  ? 510 PHE A CG     1 
ATOM   1276 C CD1    . PHE A 1 171 ? -8.713  33.555  -45.161 1.00 36.23  ? 510 PHE A CD1    1 
ATOM   1277 C CD2    . PHE A 1 171 ? -7.783  34.454  -47.161 1.00 37.22  ? 510 PHE A CD2    1 
ATOM   1278 C CE1    . PHE A 1 171 ? -7.538  33.829  -44.489 1.00 39.38  ? 510 PHE A CE1    1 
ATOM   1279 C CE2    . PHE A 1 171 ? -6.606  34.730  -46.496 1.00 38.57  ? 510 PHE A CE2    1 
ATOM   1280 C CZ     . PHE A 1 171 ? -6.483  34.416  -45.157 1.00 39.36  ? 510 PHE A CZ     1 
ATOM   1281 N N      . GLN A 1 172 ? -10.691 36.411  -45.539 1.00 45.39  ? 511 GLN A N      1 
ATOM   1282 C CA     . GLN A 1 172 ? -10.262 37.788  -45.290 1.00 42.42  ? 511 GLN A CA     1 
ATOM   1283 C C      . GLN A 1 172 ? -8.744  37.797  -45.162 1.00 40.72  ? 511 GLN A C      1 
ATOM   1284 O O      . GLN A 1 172 ? -8.196  37.505  -44.096 1.00 40.55  ? 511 GLN A O      1 
ATOM   1285 C CB     . GLN A 1 172 ? -10.931 38.346  -44.039 1.00 46.48  ? 511 GLN A CB     1 
ATOM   1286 C CG     . GLN A 1 172 ? -12.446 38.434  -44.125 1.00 49.00  ? 511 GLN A CG     1 
ATOM   1287 C CD     . GLN A 1 172 ? -13.069 38.965  -42.848 1.00 59.83  ? 511 GLN A CD     1 
ATOM   1288 O OE1    . GLN A 1 172 ? -12.938 40.146  -42.522 1.00 66.33  ? 511 GLN A OE1    1 
ATOM   1289 N NE2    . GLN A 1 172 ? -13.745 38.090  -42.113 1.00 60.03  ? 511 GLN A NE2    1 
ATOM   1290 N N      . LEU A 1 173 ? -8.061  38.142  -46.254 1.00 40.06  ? 512 LEU A N      1 
ATOM   1291 C CA     . LEU A 1 173 ? -6.603  38.082  -46.269 1.00 37.55  ? 512 LEU A CA     1 
ATOM   1292 C C      . LEU A 1 173 ? -5.993  39.124  -45.338 1.00 34.37  ? 512 LEU A C      1 
ATOM   1293 O O      . LEU A 1 173 ? -5.160  38.796  -44.485 1.00 34.20  ? 512 LEU A O      1 
ATOM   1294 C CB     . LEU A 1 173 ? -6.091  38.264  -47.698 1.00 33.31  ? 512 LEU A CB     1 
ATOM   1295 C CG     . LEU A 1 173 ? -4.575  38.230  -47.874 0.47 30.61  ? 512 LEU A CG     1 
ATOM   1296 C CD1    . LEU A 1 173 ? -4.001  37.037  -47.143 1.00 31.79  ? 512 LEU A CD1    1 
ATOM   1297 C CD2    . LEU A 1 173 ? -4.210  38.181  -49.348 1.00 32.31  ? 512 LEU A CD2    1 
ATOM   1298 N N      . THR A 1 174 ? -6.395  40.390  -45.487 1.00 34.42  ? 513 THR A N      1 
ATOM   1299 C CA     . THR A 1 174 ? -5.816  41.454  -44.673 1.00 30.60  ? 513 THR A CA     1 
ATOM   1300 C C      . THR A 1 174 ? -5.962  41.169  -43.185 1.00 34.95  ? 513 THR A C      1 
ATOM   1301 O O      . THR A 1 174 ? -5.118  41.588  -42.385 1.00 32.74  ? 513 THR A O      1 
ATOM   1302 C CB     . THR A 1 174 ? -6.470  42.794  -45.014 1.00 32.63  ? 513 THR A CB     1 
ATOM   1303 O OG1    . THR A 1 174 ? -6.284  43.080  -46.406 1.00 38.04  ? 513 THR A OG1    1 
ATOM   1304 C CG2    . THR A 1 174 ? -5.856  43.911  -44.183 1.00 29.16  ? 513 THR A CG2    1 
ATOM   1305 N N      . ARG A 1 175 ? -7.020  40.457  -42.797 1.00 36.38  ? 514 ARG A N      1 
ATOM   1306 C CA     . ARG A 1 175 ? -7.279  40.195  -41.387 1.00 35.07  ? 514 ARG A CA     1 
ATOM   1307 C C      . ARG A 1 175 ? -6.400  39.065  -40.862 1.00 34.70  ? 514 ARG A C      1 
ATOM   1308 O O      . ARG A 1 175 ? -5.791  39.186  -39.792 1.00 33.94  ? 514 ARG A O      1 
ATOM   1309 C CB     . ARG A 1 175 ? -8.761  39.876  -41.196 1.00 41.16  ? 514 ARG A CB     1 
ATOM   1310 C CG     . ARG A 1 175 ? -9.211  39.723  -39.761 1.00 40.78  ? 514 ARG A CG     1 
ATOM   1311 C CD     . ARG A 1 175 ? -10.727 39.692  -39.702 1.00 54.12  ? 514 ARG A CD     1 
ATOM   1312 N NE     . ARG A 1 175 ? -11.221 39.000  -38.519 1.00 69.80  ? 514 ARG A NE     1 
ATOM   1313 C CZ     . ARG A 1 175 ? -11.428 37.692  -38.454 1.00 67.82  ? 514 ARG A CZ     1 
ATOM   1314 N NH1    . ARG A 1 175 ? -11.179 36.901  -39.485 1.00 61.62  ? 514 ARG A NH1    1 
ATOM   1315 N NH2    . ARG A 1 175 ? -11.895 37.165  -37.327 1.00 70.24  ? 514 ARG A NH2    1 
ATOM   1316 N N      . HIS A 1 176 ? -6.319  37.959  -41.606 1.00 35.86  ? 515 HIS A N      1 
ATOM   1317 C CA     . HIS A 1 176 ? -5.435  36.865  -41.215 1.00 35.92  ? 515 HIS A CA     1 
ATOM   1318 C C      . HIS A 1 176 ? -3.986  37.322  -41.118 1.00 30.96  ? 515 HIS A C      1 
ATOM   1319 O O      . HIS A 1 176 ? -3.224  36.803  -40.294 1.00 31.37  ? 515 HIS A O      1 
ATOM   1320 C CB     . HIS A 1 176 ? -5.560  35.709  -42.210 1.00 32.84  ? 515 HIS A CB     1 
ATOM   1321 C CG     . HIS A 1 176 ? -4.554  34.621  -42.003 1.00 31.05  ? 515 HIS A CG     1 
ATOM   1322 N ND1    . HIS A 1 176 ? -4.685  33.661  -41.023 1.00 33.41  ? 515 HIS A ND1    1 
ATOM   1323 C CD2    . HIS A 1 176 ? -3.398  34.341  -42.650 1.00 35.74  ? 515 HIS A CD2    1 
ATOM   1324 C CE1    . HIS A 1 176 ? -3.655  32.836  -41.076 1.00 38.89  ? 515 HIS A CE1    1 
ATOM   1325 N NE2    . HIS A 1 176 ? -2.859  33.227  -42.055 1.00 37.18  ? 515 HIS A NE2    1 
ATOM   1326 N N      . VAL A 1 177 ? -3.589  38.293  -41.942 1.00 30.07  ? 516 VAL A N      1 
ATOM   1327 C CA     . VAL A 1 177 ? -2.204  38.747  -41.935 1.00 30.64  ? 516 VAL A CA     1 
ATOM   1328 C C      . VAL A 1 177 ? -1.935  39.685  -40.762 1.00 34.46  ? 516 VAL A C      1 
ATOM   1329 O O      . VAL A 1 177 ? -0.818  39.712  -40.231 1.00 36.95  ? 516 VAL A O      1 
ATOM   1330 C CB     . VAL A 1 177 ? -1.858  39.413  -43.278 1.00 27.90  ? 516 VAL A CB     1 
ATOM   1331 C CG1    . VAL A 1 177 ? -0.385  39.767  -43.329 1.00 30.15  ? 516 VAL A CG1    1 
ATOM   1332 C CG2    . VAL A 1 177 ? -2.226  38.495  -44.433 1.00 28.99  ? 516 VAL A CG2    1 
ATOM   1333 N N      . ILE A 1 178 ? -2.934  40.461  -40.336 1.00 32.92  ? 517 ILE A N      1 
ATOM   1334 C CA     . ILE A 1 178 ? -2.750  41.341  -39.183 1.00 33.34  ? 517 ILE A CA     1 
ATOM   1335 C C      . ILE A 1 178 ? -2.493  40.518  -37.927 1.00 31.36  ? 517 ILE A C      1 
ATOM   1336 O O      . ILE A 1 178 ? -1.547  40.778  -37.174 1.00 30.62  ? 517 ILE A O      1 
ATOM   1337 C CB     . ILE A 1 178 ? -3.966  42.269  -39.010 1.00 32.79  ? 517 ILE A CB     1 
ATOM   1338 C CG1    . ILE A 1 178 ? -4.098  43.207  -40.210 1.00 29.70  ? 517 ILE A CG1    1 
ATOM   1339 C CG2    . ILE A 1 178 ? -3.847  43.066  -37.717 1.00 31.95  ? 517 ILE A CG2    1 
ATOM   1340 C CD1    . ILE A 1 178 ? -5.281  44.144  -40.122 1.00 26.64  ? 517 ILE A CD1    1 
ATOM   1341 N N      . GLY A 1 179 ? -3.338  39.515  -37.679 1.00 34.05  ? 518 GLY A N      1 
ATOM   1342 C CA     . GLY A 1 179 ? -3.105  38.630  -36.552 1.00 28.40  ? 518 GLY A CA     1 
ATOM   1343 C C      . GLY A 1 179 ? -1.809  37.856  -36.672 1.00 28.68  ? 518 GLY A C      1 
ATOM   1344 O O      . GLY A 1 179 ? -1.141  37.594  -35.668 1.00 33.58  ? 518 GLY A O      1 
ATOM   1345 N N      . THR A 1 180 ? -1.431  37.486  -37.897 1.00 31.78  ? 519 THR A N      1 
ATOM   1346 C CA     . THR A 1 180 ? -0.187  36.751  -38.106 1.00 32.62  ? 519 THR A CA     1 
ATOM   1347 C C      . THR A 1 180 ? 1.011   37.533  -37.580 1.00 34.92  ? 519 THR A C      1 
ATOM   1348 O O      . THR A 1 180 ? 1.828   37.002  -36.817 1.00 31.94  ? 519 THR A O      1 
ATOM   1349 C CB     . THR A 1 180 ? -0.010  36.433  -39.591 1.00 33.28  ? 519 THR A CB     1 
ATOM   1350 O OG1    . THR A 1 180 ? -0.748  35.248  -39.920 1.00 43.37  ? 519 THR A OG1    1 
ATOM   1351 C CG2    . THR A 1 180 ? 1.459   36.225  -39.923 1.00 33.82  ? 519 THR A CG2    1 
ATOM   1352 N N      . GLN A 1 181 ? 1.133   38.802  -37.975 1.00 34.18  ? 520 GLN A N      1 
ATOM   1353 C CA     . GLN A 1 181 ? 2.288   39.588  -37.554 1.00 33.97  ? 520 GLN A CA     1 
ATOM   1354 C C      . GLN A 1 181 ? 2.267   39.871  -36.057 1.00 32.25  ? 520 GLN A C      1 
ATOM   1355 O O      . GLN A 1 181 ? 3.330   39.943  -35.428 1.00 34.31  ? 520 GLN A O      1 
ATOM   1356 C CB     . GLN A 1 181 ? 2.354   40.899  -38.336 1.00 33.51  ? 520 GLN A CB     1 
ATOM   1357 C CG     . GLN A 1 181 ? 1.170   41.828  -38.115 1.00 33.17  ? 520 GLN A CG     1 
ATOM   1358 C CD     . GLN A 1 181 ? 1.405   43.216  -38.685 1.00 28.78  ? 520 GLN A CD     1 
ATOM   1359 O OE1    . GLN A 1 181 ? 2.546   43.638  -38.874 1.00 26.75  ? 520 GLN A OE1    1 
ATOM   1360 N NE2    . GLN A 1 181 ? 0.323   43.931  -38.965 1.00 30.09  ? 520 GLN A NE2    1 
ATOM   1361 N N      . GLY A 1 182 ? 1.079   40.024  -35.468 1.00 31.42  ? 521 GLY A N      1 
ATOM   1362 C CA     . GLY A 1 182 ? 1.000   40.406  -34.069 1.00 26.30  ? 521 GLY A CA     1 
ATOM   1363 C C      . GLY A 1 182 ? 1.163   39.261  -33.092 1.00 32.12  ? 521 GLY A C      1 
ATOM   1364 O O      . GLY A 1 182 ? 1.639   39.469  -31.971 1.00 25.09  ? 521 GLY A O      1 
ATOM   1365 N N      . TYR A 1 183 ? 0.780   38.047  -33.489 1.00 30.79  ? 522 TYR A N      1 
ATOM   1366 C CA     . TYR A 1 183 ? 0.791   36.901  -32.588 1.00 22.22  ? 522 TYR A CA     1 
ATOM   1367 C C      . TYR A 1 183 ? 1.823   35.842  -32.938 1.00 21.36  ? 522 TYR A C      1 
ATOM   1368 O O      . TYR A 1 183 ? 2.282   35.134  -32.041 1.00 23.37  ? 522 TYR A O      1 
ATOM   1369 C CB     . TYR A 1 183 ? -0.591  36.235  -32.555 1.00 23.26  ? 522 TYR A CB     1 
ATOM   1370 C CG     . TYR A 1 183 ? -1.678  37.056  -31.894 1.00 24.60  ? 522 TYR A CG     1 
ATOM   1371 C CD1    . TYR A 1 183 ? -2.437  37.959  -32.626 1.00 26.21  ? 522 TYR A CD1    1 
ATOM   1372 C CD2    . TYR A 1 183 ? -1.954  36.914  -30.539 1.00 24.85  ? 522 TYR A CD2    1 
ATOM   1373 C CE1    . TYR A 1 183 ? -3.435  38.705  -32.026 1.00 26.53  ? 522 TYR A CE1    1 
ATOM   1374 C CE2    . TYR A 1 183 ? -2.951  37.657  -29.930 1.00 24.05  ? 522 TYR A CE2    1 
ATOM   1375 C CZ     . TYR A 1 183 ? -3.688  38.549  -30.679 1.00 29.22  ? 522 TYR A CZ     1 
ATOM   1376 O OH     . TYR A 1 183 ? -4.680  39.291  -30.079 1.00 27.29  ? 522 TYR A OH     1 
ATOM   1377 N N      . MET A 1 184 ? 2.199   35.709  -34.206 1.00 24.92  ? 523 MET A N      1 
ATOM   1378 C CA     . MET A 1 184 ? 3.024   34.585  -34.629 1.00 23.71  ? 523 MET A CA     1 
ATOM   1379 C C      . MET A 1 184 ? 4.477   34.777  -34.218 1.00 24.94  ? 523 MET A C      1 
ATOM   1380 O O      . MET A 1 184 ? 5.010   35.890  -34.252 1.00 25.81  ? 523 MET A O      1 
ATOM   1381 C CB     . MET A 1 184 ? 2.935   34.396  -36.141 1.00 22.55  ? 523 MET A CB     1 
ATOM   1382 C CG     . MET A 1 184 ? 1.653   33.729  -36.597 1.00 29.08  ? 523 MET A CG     1 
ATOM   1383 S SD     . MET A 1 184 ? 1.399   32.128  -35.806 1.00 37.41  ? 523 MET A SD     1 
ATOM   1384 C CE     . MET A 1 184 ? -0.123  31.592  -36.584 1.00 38.62  ? 523 MET A CE     1 
ATOM   1385 N N      . ALA A 1 185 ? 5.118   33.674  -33.839 1.00 24.11  ? 524 ALA A N      1 
ATOM   1386 C CA     . ALA A 1 185 ? 6.514   33.727  -33.445 1.00 22.06  ? 524 ALA A CA     1 
ATOM   1387 C C      . ALA A 1 185 ? 7.404   33.829  -34.682 1.00 23.86  ? 524 ALA A C      1 
ATOM   1388 O O      . ALA A 1 185 ? 7.025   33.385  -35.768 1.00 26.92  ? 524 ALA A O      1 
ATOM   1389 C CB     . ALA A 1 185 ? 6.891   32.495  -32.628 1.00 21.22  ? 524 ALA A CB     1 
ATOM   1390 N N      . PRO A 1 186 ? 8.596   34.415  -34.542 1.00 26.60  ? 525 PRO A N      1 
ATOM   1391 C CA     . PRO A 1 186 ? 9.450   34.604  -35.725 1.00 26.45  ? 525 PRO A CA     1 
ATOM   1392 C C      . PRO A 1 186 ? 9.866   33.304  -36.392 1.00 27.18  ? 525 PRO A C      1 
ATOM   1393 O O      . PRO A 1 186 ? 9.940   33.249  -37.626 1.00 24.44  ? 525 PRO A O      1 
ATOM   1394 C CB     . PRO A 1 186 ? 10.657  35.370  -35.162 1.00 30.39  ? 525 PRO A CB     1 
ATOM   1395 C CG     . PRO A 1 186 ? 10.676  35.033  -33.711 1.00 29.41  ? 525 PRO A CG     1 
ATOM   1396 C CD     . PRO A 1 186 ? 9.237   34.900  -33.310 1.00 28.36  ? 525 PRO A CD     1 
ATOM   1397 N N      . GLU A 1 187 ? 10.149  32.254  -35.616 1.00 25.27  ? 526 GLU A N      1 
ATOM   1398 C CA     . GLU A 1 187 ? 10.555  30.991  -36.225 1.00 26.42  ? 526 GLU A CA     1 
ATOM   1399 C C      . GLU A 1 187 ? 9.441   30.377  -37.063 1.00 22.79  ? 526 GLU A C      1 
ATOM   1400 O O      . GLU A 1 187 ? 9.720   29.529  -37.917 1.00 20.60  ? 526 GLU A O      1 
ATOM   1401 C CB     . GLU A 1 187 ? 11.014  29.996  -35.157 1.00 21.72  ? 526 GLU A CB     1 
ATOM   1402 C CG     . GLU A 1 187 ? 9.889   29.381  -34.342 1.00 20.87  ? 526 GLU A CG     1 
ATOM   1403 C CD     . GLU A 1 187 ? 9.561   30.186  -33.105 1.00 20.93  ? 526 GLU A CD     1 
ATOM   1404 O OE1    . GLU A 1 187 ? 10.249  31.195  -32.854 1.00 26.42  ? 526 GLU A OE1    1 
ATOM   1405 O OE2    . GLU A 1 187 ? 8.618   29.808  -32.380 1.00 19.44  ? 526 GLU A OE2    1 
ATOM   1406 N N      . TYR A 1 188 ? 8.188   30.776  -36.835 1.00 23.08  ? 527 TYR A N      1 
ATOM   1407 C CA     . TYR A 1 188 ? 7.107   30.336  -37.710 1.00 24.29  ? 527 TYR A CA     1 
ATOM   1408 C C      . TYR A 1 188 ? 7.016   31.219  -38.949 1.00 22.27  ? 527 TYR A C      1 
ATOM   1409 O O      . TYR A 1 188 ? 6.942   30.716  -40.076 1.00 23.35  ? 527 TYR A O      1 
ATOM   1410 C CB     . TYR A 1 188 ? 5.777   30.334  -36.952 1.00 21.50  ? 527 TYR A CB     1 
ATOM   1411 C CG     . TYR A 1 188 ? 4.612   29.824  -37.774 1.00 21.73  ? 527 TYR A CG     1 
ATOM   1412 C CD1    . TYR A 1 188 ? 4.436   28.464  -37.993 1.00 24.56  ? 527 TYR A CD1    1 
ATOM   1413 C CD2    . TYR A 1 188 ? 3.689   30.701  -38.330 1.00 20.82  ? 527 TYR A CD2    1 
ATOM   1414 C CE1    . TYR A 1 188 ? 3.374   27.992  -38.744 1.00 25.27  ? 527 TYR A CE1    1 
ATOM   1415 C CE2    . TYR A 1 188 ? 2.624   30.238  -39.081 1.00 20.63  ? 527 TYR A CE2    1 
ATOM   1416 C CZ     . TYR A 1 188 ? 2.472   28.883  -39.285 1.00 23.67  ? 527 TYR A CZ     1 
ATOM   1417 O OH     . TYR A 1 188 ? 1.415   28.417  -40.032 1.00 23.75  ? 527 TYR A OH     1 
ATOM   1418 N N      . ILE A 1 189 ? 7.032   32.540  -38.757 1.00 22.44  ? 528 ILE A N      1 
ATOM   1419 C CA     . ILE A 1 189 ? 6.962   33.459  -39.889 1.00 25.31  ? 528 ILE A CA     1 
ATOM   1420 C C      . ILE A 1 189 ? 8.104   33.207  -40.862 1.00 25.86  ? 528 ILE A C      1 
ATOM   1421 O O      . ILE A 1 189 ? 7.953   33.407  -42.074 1.00 26.45  ? 528 ILE A O      1 
ATOM   1422 C CB     . ILE A 1 189 ? 6.966   34.920  -39.395 1.00 23.64  ? 528 ILE A CB     1 
ATOM   1423 C CG1    . ILE A 1 189 ? 5.865   35.139  -38.355 1.00 25.56  ? 528 ILE A CG1    1 
ATOM   1424 C CG2    . ILE A 1 189 ? 6.797   35.878  -40.564 1.00 27.20  ? 528 ILE A CG2    1 
ATOM   1425 C CD1    . ILE A 1 189 ? 4.474   34.897  -38.882 1.00 26.79  ? 528 ILE A CD1    1 
ATOM   1426 N N      . GLU A 1 190 ? 9.254   32.761  -40.361 1.00 24.65  ? 529 GLU A N      1 
ATOM   1427 C CA     . GLU A 1 190 ? 10.450  32.628  -41.183 1.00 25.54  ? 529 GLU A CA     1 
ATOM   1428 C C      . GLU A 1 190 ? 10.699  31.212  -41.680 1.00 26.30  ? 529 GLU A C      1 
ATOM   1429 O O      . GLU A 1 190 ? 11.218  31.043  -42.789 1.00 23.45  ? 529 GLU A O      1 
ATOM   1430 C CB     . GLU A 1 190 ? 11.681  33.107  -40.405 1.00 26.41  ? 529 GLU A CB     1 
ATOM   1431 C CG     . GLU A 1 190 ? 11.596  34.553  -39.954 1.00 29.78  ? 529 GLU A CG     1 
ATOM   1432 C CD     . GLU A 1 190 ? 12.840  35.014  -39.224 1.00 38.22  ? 529 GLU A CD     1 
ATOM   1433 O OE1    . GLU A 1 190 ? 13.838  34.262  -39.210 1.00 36.52  ? 529 GLU A OE1    1 
ATOM   1434 O OE2    . GLU A 1 190 ? 12.817  36.131  -38.663 1.00 43.07  ? 529 GLU A OE2    1 
ATOM   1435 N N      . ASN A 1 191 ? 10.346  30.191  -40.898 1.00 22.10  ? 530 ASN A N      1 
ATOM   1436 C CA     . ASN A 1 191 ? 10.643  28.815  -41.267 1.00 22.48  ? 530 ASN A CA     1 
ATOM   1437 C C      . ASN A 1 191 ? 9.465   27.866  -41.097 1.00 22.00  ? 530 ASN A C      1 
ATOM   1438 O O      . ASN A 1 191 ? 9.613   26.671  -41.375 1.00 22.33  ? 530 ASN A O      1 
ATOM   1439 C CB     . ASN A 1 191 ? 11.831  28.289  -40.446 1.00 25.98  ? 530 ASN A CB     1 
ATOM   1440 C CG     . ASN A 1 191 ? 13.003  29.252  -40.432 1.00 32.61  ? 530 ASN A CG     1 
ATOM   1441 O OD1    . ASN A 1 191 ? 13.162  30.040  -39.499 1.00 33.13  ? 530 ASN A OD1    1 
ATOM   1442 N ND2    . ASN A 1 191 ? 13.831  29.193  -41.469 1.00 30.74  ? 530 ASN A ND2    1 
ATOM   1443 N N      . GLY A 1 192 ? 8.308   28.353  -40.657 1.00 22.97  ? 531 GLY A N      1 
ATOM   1444 C CA     . GLY A 1 192 ? 7.190   27.465  -40.404 1.00 21.93  ? 531 GLY A CA     1 
ATOM   1445 C C      . GLY A 1 192 ? 7.439   26.461  -39.306 1.00 22.26  ? 531 GLY A C      1 
ATOM   1446 O O      . GLY A 1 192 ? 6.773   25.423  -39.263 1.00 24.67  ? 531 GLY A O      1 
ATOM   1447 N N      . LEU A 1 193 ? 8.387   26.738  -38.412 1.00 22.80  ? 532 LEU A N      1 
ATOM   1448 C CA     . LEU A 1 193 ? 8.717   25.816  -37.330 1.00 20.39  ? 532 LEU A CA     1 
ATOM   1449 C C      . LEU A 1 193 ? 7.598   25.827  -36.299 1.00 20.89  ? 532 LEU A C      1 
ATOM   1450 O O      . LEU A 1 193 ? 7.381   26.833  -35.616 1.00 20.72  ? 532 LEU A O      1 
ATOM   1451 C CB     . LEU A 1 193 ? 10.046  26.200  -36.691 1.00 22.88  ? 532 LEU A CB     1 
ATOM   1452 C CG     . LEU A 1 193 ? 10.398  25.367  -35.457 1.00 23.86  ? 532 LEU A CG     1 
ATOM   1453 C CD1    . LEU A 1 193 ? 10.491  23.891  -35.816 1.00 24.01  ? 532 LEU A CD1    1 
ATOM   1454 C CD2    . LEU A 1 193 ? 11.686  25.854  -34.815 1.00 26.73  ? 532 LEU A CD2    1 
ATOM   1455 N N      . ILE A 1 194 ? 6.895   24.706  -36.175 1.00 20.30  ? 533 ILE A N      1 
ATOM   1456 C CA     . ILE A 1 194 ? 5.723   24.593  -35.316 1.00 19.09  ? 533 ILE A CA     1 
ATOM   1457 C C      . ILE A 1 194 ? 6.121   23.816  -34.069 1.00 19.28  ? 533 ILE A C      1 
ATOM   1458 O O      . ILE A 1 194 ? 6.330   22.599  -34.123 1.00 23.44  ? 533 ILE A O      1 
ATOM   1459 C CB     . ILE A 1 194 ? 4.557   23.914  -36.045 1.00 19.85  ? 533 ILE A CB     1 
ATOM   1460 C CG1    . ILE A 1 194 ? 4.086   24.779  -37.217 1.00 19.40  ? 533 ILE A CG1    1 
ATOM   1461 C CG2    . ILE A 1 194 ? 3.416   23.639  -35.080 1.00 20.77  ? 533 ILE A CG2    1 
ATOM   1462 C CD1    . ILE A 1 194 ? 3.024   24.122  -38.069 1.00 22.17  ? 533 ILE A CD1    1 
ATOM   1463 N N      . THR A 1 195 ? 6.225   24.513  -32.948 1.00 18.62  ? 534 THR A N      1 
ATOM   1464 C CA     . THR A 1 195 ? 6.461   23.915  -31.645 1.00 18.96  ? 534 THR A CA     1 
ATOM   1465 C C      . THR A 1 195 ? 5.466   24.491  -30.652 1.00 20.40  ? 534 THR A C      1 
ATOM   1466 O O      . THR A 1 195 ? 4.833   25.518  -30.920 1.00 23.75  ? 534 THR A O      1 
ATOM   1467 C CB     . THR A 1 195 ? 7.889   24.179  -31.144 1.00 19.88  ? 534 THR A CB     1 
ATOM   1468 O OG1    . THR A 1 195 ? 7.956   25.482  -30.549 1.00 25.51  ? 534 THR A OG1    1 
ATOM   1469 C CG2    . THR A 1 195 ? 8.883   24.097  -32.292 1.00 19.42  ? 534 THR A CG2    1 
ATOM   1470 N N      . PRO A 1 196 ? 5.299   23.850  -29.494 1.00 20.26  ? 535 PRO A N      1 
ATOM   1471 C CA     . PRO A 1 196 ? 4.480   24.463  -28.437 1.00 20.31  ? 535 PRO A CA     1 
ATOM   1472 C C      . PRO A 1 196 ? 4.983   25.832  -28.005 1.00 21.19  ? 535 PRO A C      1 
ATOM   1473 O O      . PRO A 1 196 ? 4.235   26.572  -27.354 1.00 22.90  ? 535 PRO A O      1 
ATOM   1474 C CB     . PRO A 1 196 ? 4.553   23.441  -27.291 1.00 19.53  ? 535 PRO A CB     1 
ATOM   1475 C CG     . PRO A 1 196 ? 5.685   22.512  -27.648 1.00 22.28  ? 535 PRO A CG     1 
ATOM   1476 C CD     . PRO A 1 196 ? 5.742   22.493  -29.137 1.00 22.16  ? 535 PRO A CD     1 
ATOM   1477 N N      . LYS A 1 197 ? 6.223   26.194  -28.355 1.00 22.18  ? 536 LYS A N      1 
ATOM   1478 C CA     . LYS A 1 197 ? 6.734   27.520  -28.019 1.00 18.35  ? 536 LYS A CA     1 
ATOM   1479 C C      . LYS A 1 197 ? 6.009   28.618  -28.785 1.00 19.65  ? 536 LYS A C      1 
ATOM   1480 O O      . LYS A 1 197 ? 5.960   29.761  -28.319 1.00 21.82  ? 536 LYS A O      1 
ATOM   1481 C CB     . LYS A 1 197 ? 8.237   27.595  -28.288 1.00 20.73  ? 536 LYS A CB     1 
ATOM   1482 C CG     . LYS A 1 197 ? 9.070   26.630  -27.464 1.00 21.07  ? 536 LYS A CG     1 
ATOM   1483 C CD     . LYS A 1 197 ? 8.991   26.949  -25.978 1.00 23.67  ? 536 LYS A CD     1 
ATOM   1484 C CE     . LYS A 1 197 ? 9.919   26.046  -25.178 1.00 25.16  ? 536 LYS A CE     1 
ATOM   1485 N NZ     . LYS A 1 197 ? 9.883   26.339  -23.722 1.00 24.52  ? 536 LYS A NZ     1 
ATOM   1486 N N      . MET A 1 198 ? 5.448   28.305  -29.957 1.00 20.46  ? 537 MET A N      1 
ATOM   1487 C CA     . MET A 1 198 ? 4.671   29.311  -30.675 1.00 19.29  ? 537 MET A CA     1 
ATOM   1488 C C      . MET A 1 198 ? 3.396   29.665  -29.920 1.00 16.97  ? 537 MET A C      1 
ATOM   1489 O O      . MET A 1 198 ? 2.954   30.819  -29.956 1.00 18.73  ? 537 MET A O      1 
ATOM   1490 C CB     . MET A 1 198 ? 4.347   28.828  -32.092 1.00 18.26  ? 537 MET A CB     1 
ATOM   1491 C CG     . MET A 1 198 ? 3.277   27.757  -32.178 1.00 17.68  ? 537 MET A CG     1 
ATOM   1492 S SD     . MET A 1 198 ? 3.014   27.211  -33.876 1.00 30.29  ? 537 MET A SD     1 
ATOM   1493 C CE     . MET A 1 198 ? 2.713   28.774  -34.698 1.00 19.84  ? 537 MET A CE     1 
ATOM   1494 N N      . ASP A 1 199 ? 2.795   28.693  -29.230 1.00 20.44  ? 538 ASP A N      1 
ATOM   1495 C CA     . ASP A 1 199 ? 1.691   29.009  -28.331 1.00 18.24  ? 538 ASP A CA     1 
ATOM   1496 C C      . ASP A 1 199 ? 2.164   29.879  -27.173 1.00 17.56  ? 538 ASP A C      1 
ATOM   1497 O O      . ASP A 1 199 ? 1.457   30.800  -26.751 1.00 17.69  ? 538 ASP A O      1 
ATOM   1498 C CB     . ASP A 1 199 ? 1.050   27.723  -27.809 1.00 18.98  ? 538 ASP A CB     1 
ATOM   1499 C CG     . ASP A 1 199 ? 0.336   26.944  -28.897 1.00 21.16  ? 538 ASP A CG     1 
ATOM   1500 O OD1    . ASP A 1 199 ? 0.245   27.453  -30.033 1.00 19.71  ? 538 ASP A OD1    1 
ATOM   1501 O OD2    . ASP A 1 199 ? -0.135  25.823  -28.614 1.00 20.17  ? 538 ASP A OD2    1 
ATOM   1502 N N      . VAL A 1 200 ? 3.362   29.603  -26.650 1.00 15.57  ? 539 VAL A N      1 
ATOM   1503 C CA     . VAL A 1 200 ? 3.903   30.413  -25.562 1.00 16.18  ? 539 VAL A CA     1 
ATOM   1504 C C      . VAL A 1 200 ? 4.110   31.850  -26.021 1.00 19.93  ? 539 VAL A C      1 
ATOM   1505 O O      . VAL A 1 200 ? 3.830   32.802  -25.281 1.00 21.66  ? 539 VAL A O      1 
ATOM   1506 C CB     . VAL A 1 200 ? 5.210   29.793  -25.033 1.00 18.59  ? 539 VAL A CB     1 
ATOM   1507 C CG1    . VAL A 1 200 ? 5.961   30.799  -24.174 1.00 22.73  ? 539 VAL A CG1    1 
ATOM   1508 C CG2    . VAL A 1 200 ? 4.918   28.530  -24.240 1.00 16.31  ? 539 VAL A CG2    1 
ATOM   1509 N N      . PHE A 1 201 ? 4.610   32.031  -27.246 1.00 16.55  ? 540 PHE A N      1 
ATOM   1510 C CA     . PHE A 1 201 ? 4.776   33.375  -27.791 1.00 19.30  ? 540 PHE A CA     1 
ATOM   1511 C C      . PHE A 1 201 ? 3.434   34.088  -27.892 1.00 19.49  ? 540 PHE A C      1 
ATOM   1512 O O      . PHE A 1 201 ? 3.275   35.211  -27.397 1.00 18.63  ? 540 PHE A O      1 
ATOM   1513 C CB     . PHE A 1 201 ? 5.457   33.301  -29.157 1.00 20.23  ? 540 PHE A CB     1 
ATOM   1514 C CG     . PHE A 1 201 ? 5.812   34.643  -29.738 1.00 21.03  ? 540 PHE A CG     1 
ATOM   1515 C CD1    . PHE A 1 201 ? 7.043   35.223  -29.476 1.00 21.15  ? 540 PHE A CD1    1 
ATOM   1516 C CD2    . PHE A 1 201 ? 4.923   35.318  -30.558 1.00 18.25  ? 540 PHE A CD2    1 
ATOM   1517 C CE1    . PHE A 1 201 ? 7.374   36.454  -30.014 1.00 21.48  ? 540 PHE A CE1    1 
ATOM   1518 C CE2    . PHE A 1 201 ? 5.249   36.549  -31.098 1.00 15.76  ? 540 PHE A CE2    1 
ATOM   1519 C CZ     . PHE A 1 201 ? 6.476   37.116  -30.826 1.00 17.19  ? 540 PHE A CZ     1 
ATOM   1520 N N      . ALA A 1 202 ? 2.452   33.446  -28.530 1.00 16.21  ? 541 ALA A N      1 
ATOM   1521 C CA     . ALA A 1 202 ? 1.115   34.026  -28.608 1.00 15.74  ? 541 ALA A CA     1 
ATOM   1522 C C      . ALA A 1 202 ? 0.578   34.347  -27.219 1.00 19.63  ? 541 ALA A C      1 
ATOM   1523 O O      . ALA A 1 202 ? 0.114   35.464  -26.962 1.00 20.27  ? 541 ALA A O      1 
ATOM   1524 C CB     . ALA A 1 202 ? 0.173   33.073  -29.343 1.00 16.63  ? 541 ALA A CB     1 
ATOM   1525 N N      . PHE A 1 203 ? 0.636   33.373  -26.306 1.00 18.78  ? 542 PHE A N      1 
ATOM   1526 C CA     . PHE A 1 203 ? 0.185   33.610  -24.941 1.00 16.38  ? 542 PHE A CA     1 
ATOM   1527 C C      . PHE A 1 203 ? 0.889   34.809  -24.321 1.00 20.86  ? 542 PHE A C      1 
ATOM   1528 O O      . PHE A 1 203 ? 0.287   35.541  -23.525 1.00 21.03  ? 542 PHE A O      1 
ATOM   1529 C CB     . PHE A 1 203 ? 0.409   32.356  -24.092 1.00 18.04  ? 542 PHE A CB     1 
ATOM   1530 C CG     . PHE A 1 203 ? -0.155  32.454  -22.699 1.00 17.09  ? 542 PHE A CG     1 
ATOM   1531 C CD1    . PHE A 1 203 ? -1.422  32.968  -22.486 1.00 14.85  ? 542 PHE A CD1    1 
ATOM   1532 C CD2    . PHE A 1 203 ? 0.576   32.015  -21.608 1.00 17.27  ? 542 PHE A CD2    1 
ATOM   1533 C CE1    . PHE A 1 203 ? -1.945  33.054  -21.211 1.00 18.86  ? 542 PHE A CE1    1 
ATOM   1534 C CE2    . PHE A 1 203 ? 0.057   32.097  -20.329 1.00 18.18  ? 542 PHE A CE2    1 
ATOM   1535 C CZ     . PHE A 1 203 ? -1.205  32.618  -20.131 1.00 18.95  ? 542 PHE A CZ     1 
ATOM   1536 N N      . GLY A 1 204 ? 2.157   35.031  -24.670 1.00 17.58  ? 543 GLY A N      1 
ATOM   1537 C CA     . GLY A 1 204 ? 2.839   36.222  -24.194 1.00 19.29  ? 543 GLY A CA     1 
ATOM   1538 C C      . GLY A 1 204 ? 2.160   37.499  -24.652 1.00 20.69  ? 543 GLY A C      1 
ATOM   1539 O O      . GLY A 1 204 ? 1.988   38.439  -23.870 1.00 22.35  ? 543 GLY A O      1 
ATOM   1540 N N      . VAL A 1 205 ? 1.762   37.550  -25.925 1.00 18.11  ? 544 VAL A N      1 
ATOM   1541 C CA     . VAL A 1 205 ? 1.104   38.744  -26.448 1.00 16.27  ? 544 VAL A CA     1 
ATOM   1542 C C      . VAL A 1 205 ? -0.233  38.964  -25.751 1.00 18.10  ? 544 VAL A C      1 
ATOM   1543 O O      . VAL A 1 205 ? -0.605  40.101  -25.435 1.00 20.03  ? 544 VAL A O      1 
ATOM   1544 C CB     . VAL A 1 205 ? 0.937   38.639  -27.975 1.00 18.43  ? 544 VAL A CB     1 
ATOM   1545 C CG1    . VAL A 1 205 ? 0.391   39.942  -28.541 1.00 18.66  ? 544 VAL A CG1    1 
ATOM   1546 C CG2    . VAL A 1 205 ? 2.256   38.274  -28.635 1.00 19.94  ? 544 VAL A CG2    1 
ATOM   1547 N N      . VAL A 1 206 ? -0.981  37.884  -25.509 1.00 17.14  ? 545 VAL A N      1 
ATOM   1548 C CA     . VAL A 1 206 ? -2.259  38.004  -24.809 1.00 16.57  ? 545 VAL A CA     1 
ATOM   1549 C C      . VAL A 1 206 ? -2.062  38.697  -23.468 1.00 19.84  ? 545 VAL A C      1 
ATOM   1550 O O      . VAL A 1 206 ? -2.773  39.651  -23.129 1.00 23.87  ? 545 VAL A O      1 
ATOM   1551 C CB     . VAL A 1 206 ? -2.912  36.621  -24.637 1.00 17.88  ? 545 VAL A CB     1 
ATOM   1552 C CG1    . VAL A 1 206 ? -4.081  36.707  -23.671 1.00 11.60  ? 545 VAL A CG1    1 
ATOM   1553 C CG2    . VAL A 1 206 ? -3.366  36.077  -25.984 1.00 19.84  ? 545 VAL A CG2    1 
ATOM   1554 N N      . ILE A 1 207 ? -1.089  38.226  -22.685 1.00 19.20  ? 546 ILE A N      1 
ATOM   1555 C CA     . ILE A 1 207 ? -0.792  38.851  -21.398 1.00 20.61  ? 546 ILE A CA     1 
ATOM   1556 C C      . ILE A 1 207 ? -0.537  40.342  -21.583 1.00 20.93  ? 546 ILE A C      1 
ATOM   1557 O O      . ILE A 1 207 ? -1.057  41.180  -20.836 1.00 18.20  ? 546 ILE A O      1 
ATOM   1558 C CB     . ILE A 1 207 ? 0.403   38.149  -20.728 1.00 17.69  ? 546 ILE A CB     1 
ATOM   1559 C CG1    . ILE A 1 207 ? 0.089   36.667  -20.508 1.00 16.60  ? 546 ILE A CG1    1 
ATOM   1560 C CG2    . ILE A 1 207 ? 0.757   38.830  -19.417 1.00 17.71  ? 546 ILE A CG2    1 
ATOM   1561 C CD1    . ILE A 1 207 ? 1.196   35.901  -19.820 1.00 16.68  ? 546 ILE A CD1    1 
ATOM   1562 N N      . LEU A 1 208 ? 0.265   40.694  -22.592 1.00 19.79  ? 547 LEU A N      1 
ATOM   1563 C CA     . LEU A 1 208 ? 0.517   42.103  -22.873 1.00 18.88  ? 547 LEU A CA     1 
ATOM   1564 C C      . LEU A 1 208 ? -0.783  42.843  -23.168 1.00 19.80  ? 547 LEU A C      1 
ATOM   1565 O O      . LEU A 1 208 ? -0.973  43.980  -22.722 1.00 20.26  ? 547 LEU A O      1 
ATOM   1566 C CB     . LEU A 1 208 ? 1.500   42.240  -24.036 1.00 18.63  ? 547 LEU A CB     1 
ATOM   1567 C CG     . LEU A 1 208 ? 2.888   41.642  -23.796 1.00 17.87  ? 547 LEU A CG     1 
ATOM   1568 C CD1    . LEU A 1 208 ? 3.827   41.971  -24.946 1.00 20.58  ? 547 LEU A CD1    1 
ATOM   1569 C CD2    . LEU A 1 208 ? 3.464   42.126  -22.471 1.00 19.77  ? 547 LEU A CD2    1 
ATOM   1570 N N      . GLU A 1 209 ? -1.692  42.213  -23.918 1.00 18.64  ? 548 GLU A N      1 
ATOM   1571 C CA     . GLU A 1 209 ? -3.014  42.799  -24.113 1.00 15.90  ? 548 GLU A CA     1 
ATOM   1572 C C      . GLU A 1 209 ? -3.726  42.983  -22.782 1.00 19.34  ? 548 GLU A C      1 
ATOM   1573 O O      . GLU A 1 209 ? -4.359  44.019  -22.543 1.00 20.78  ? 548 GLU A O      1 
ATOM   1574 C CB     . GLU A 1 209 ? -3.857  41.923  -25.036 1.00 17.55  ? 548 GLU A CB     1 
ATOM   1575 C CG     . GLU A 1 209 ? -3.301  41.725  -26.429 1.00 16.88  ? 548 GLU A CG     1 
ATOM   1576 C CD     . GLU A 1 209 ? -4.289  41.014  -27.333 1.00 19.03  ? 548 GLU A CD     1 
ATOM   1577 O OE1    . GLU A 1 209 ? -5.453  41.465  -27.410 1.00 21.12  ? 548 GLU A OE1    1 
ATOM   1578 O OE2    . GLU A 1 209 ? -3.911  39.997  -27.950 1.00 24.93  ? 548 GLU A OE2    1 
ATOM   1579 N N      . LEU A 1 210 ? -3.636  41.983  -21.902 1.00 19.87  ? 549 LEU A N      1 
ATOM   1580 C CA     . LEU A 1 210 ? -4.306  42.069  -20.610 1.00 17.03  ? 549 LEU A CA     1 
ATOM   1581 C C      . LEU A 1 210 ? -3.727  43.180  -19.744 1.00 17.98  ? 549 LEU A C      1 
ATOM   1582 O O      . LEU A 1 210 ? -4.466  43.821  -18.987 1.00 22.09  ? 549 LEU A O      1 
ATOM   1583 C CB     . LEU A 1 210 ? -4.217  40.724  -19.887 1.00 17.29  ? 549 LEU A CB     1 
ATOM   1584 C CG     . LEU A 1 210 ? -5.087  39.607  -20.469 1.00 18.30  ? 549 LEU A CG     1 
ATOM   1585 C CD1    . LEU A 1 210 ? -4.729  38.265  -19.851 1.00 17.71  ? 549 LEU A CD1    1 
ATOM   1586 C CD2    . LEU A 1 210 ? -6.556  39.922  -20.249 1.00 15.61  ? 549 LEU A CD2    1 
ATOM   1587 N N      . LEU A 1 211 ? -2.420  43.428  -19.840 1.00 19.64  ? 550 LEU A N      1 
ATOM   1588 C CA     . LEU A 1 211 ? -1.793  44.444  -19.001 1.00 20.56  ? 550 LEU A CA     1 
ATOM   1589 C C      . LEU A 1 211 ? -1.996  45.847  -19.557 1.00 21.58  ? 550 LEU A C      1 
ATOM   1590 O O      . LEU A 1 211 ? -2.255  46.785  -18.795 1.00 21.34  ? 550 LEU A O      1 
ATOM   1591 C CB     . LEU A 1 211 ? -0.301  44.152  -18.848 1.00 15.15  ? 550 LEU A CB     1 
ATOM   1592 C CG     . LEU A 1 211 ? 0.051   42.895  -18.059 1.00 15.91  ? 550 LEU A CG     1 
ATOM   1593 C CD1    . LEU A 1 211 ? 1.553   42.670  -18.057 1.00 12.85  ? 550 LEU A CD1    1 
ATOM   1594 C CD2    . LEU A 1 211 ? -0.482  43.008  -16.639 1.00 14.84  ? 550 LEU A CD2    1 
ATOM   1595 N N      . SER A 1 212 ? -1.878  46.014  -20.876 1.00 17.01  ? 551 SER A N      1 
ATOM   1596 C CA     . SER A 1 212 ? -1.984  47.327  -21.496 1.00 20.79  ? 551 SER A CA     1 
ATOM   1597 C C      . SER A 1 212 ? -3.326  47.606  -22.157 1.00 23.23  ? 551 SER A C      1 
ATOM   1598 O O      . SER A 1 212 ? -3.634  48.776  -22.399 1.00 22.39  ? 551 SER A O      1 
ATOM   1599 C CB     . SER A 1 212 ? -0.882  47.511  -22.553 1.00 23.72  ? 551 SER A CB     1 
ATOM   1600 O OG     . SER A 1 212 ? -1.089  46.667  -23.678 1.00 22.85  ? 551 SER A OG     1 
ATOM   1601 N N      . GLY A 1 213 ? -4.116  46.581  -22.472 1.00 23.07  ? 552 GLY A N      1 
ATOM   1602 C CA     . GLY A 1 213 ? -5.286  46.791  -23.301 1.00 21.35  ? 552 GLY A CA     1 
ATOM   1603 C C      . GLY A 1 213 ? -4.993  47.261  -24.711 1.00 23.31  ? 552 GLY A C      1 
ATOM   1604 O O      . GLY A 1 213 ? -5.934  47.565  -25.451 1.00 21.86  ? 552 GLY A O      1 
ATOM   1605 N N      . ARG A 1 214 ? -3.720  47.313  -25.113 1.00 21.58  ? 553 ARG A N      1 
ATOM   1606 C CA     . ARG A 1 214 ? -3.334  47.827  -26.422 1.00 22.13  ? 553 ARG A CA     1 
ATOM   1607 C C      . ARG A 1 214 ? -3.589  46.805  -27.533 1.00 24.05  ? 553 ARG A C      1 
ATOM   1608 O O      . ARG A 1 214 ? -3.687  45.598  -27.299 1.00 22.08  ? 553 ARG A O      1 
ATOM   1609 C CB     . ARG A 1 214 ? -1.857  48.228  -26.430 1.00 21.58  ? 553 ARG A CB     1 
ATOM   1610 C CG     . ARG A 1 214 ? -1.509  49.291  -25.403 1.00 24.47  ? 553 ARG A CG     1 
ATOM   1611 C CD     . ARG A 1 214 ? -0.065  49.736  -25.522 1.00 23.28  ? 553 ARG A CD     1 
ATOM   1612 N NE     . ARG A 1 214 ? 0.237   50.874  -24.661 1.00 30.03  ? 553 ARG A NE     1 
ATOM   1613 C CZ     . ARG A 1 214 ? 1.415   51.482  -24.619 1.00 28.49  ? 553 ARG A CZ     1 
ATOM   1614 N NH1    . ARG A 1 214 ? 2.424   51.085  -25.378 1.00 23.44  ? 553 ARG A NH1    1 
ATOM   1615 N NH2    . ARG A 1 214 ? 1.584   52.513  -23.797 1.00 28.97  ? 553 ARG A NH2    1 
ATOM   1616 N N      . GLU A 1 215 ? -3.695  47.310  -28.760 1.00 23.55  ? 554 GLU A N      1 
ATOM   1617 C CA     . GLU A 1 215 ? -3.791  46.441  -29.924 1.00 23.50  ? 554 GLU A CA     1 
ATOM   1618 C C      . GLU A 1 215 ? -2.478  45.692  -30.131 1.00 24.21  ? 554 GLU A C      1 
ATOM   1619 O O      . GLU A 1 215 ? -1.392  46.211  -29.862 1.00 24.07  ? 554 GLU A O      1 
ATOM   1620 C CB     . GLU A 1 215 ? -4.140  47.256  -31.169 1.00 24.67  ? 554 GLU A CB     1 
ATOM   1621 C CG     . GLU A 1 215 ? -5.486  47.961  -31.080 1.00 28.06  ? 554 GLU A CG     1 
ATOM   1622 C CD     . GLU A 1 215 ? -6.650  47.001  -31.218 1.00 30.53  ? 554 GLU A CD     1 
ATOM   1623 O OE1    . GLU A 1 215 ? -6.479  45.807  -30.890 1.00 28.75  ? 554 GLU A OE1    1 
ATOM   1624 O OE2    . GLU A 1 215 ? -7.731  47.436  -31.667 1.00 29.65  ? 554 GLU A OE2    1 
ATOM   1625 N N      . VAL A 1 216 ? -2.587  44.444  -30.595 1.00 24.19  ? 555 VAL A N      1 
ATOM   1626 C CA     . VAL A 1 216 ? -1.392  43.646  -30.846 1.00 25.02  ? 555 VAL A CA     1 
ATOM   1627 C C      . VAL A 1 216 ? -0.491  44.335  -31.861 1.00 27.50  ? 555 VAL A C      1 
ATOM   1628 O O      . VAL A 1 216 ? 0.740   44.229  -31.785 1.00 30.91  ? 555 VAL A O      1 
ATOM   1629 C CB     . VAL A 1 216 ? -1.790  42.230  -31.303 1.00 27.71  ? 555 VAL A CB     1 
ATOM   1630 C CG1    . VAL A 1 216 ? -2.641  41.556  -30.236 1.00 22.03  ? 555 VAL A CG1    1 
ATOM   1631 C CG2    . VAL A 1 216 ? -2.535  42.293  -32.625 1.00 32.80  ? 555 VAL A CG2    1 
ATOM   1632 N N      . VAL A 1 217 ? -1.077  45.049  -32.818 1.00 22.76  ? 556 VAL A N      1 
ATOM   1633 C CA     . VAL A 1 217 ? -0.338  45.868  -33.775 1.00 25.64  ? 556 VAL A CA     1 
ATOM   1634 C C      . VAL A 1 217 ? -0.964  47.255  -33.711 1.00 30.12  ? 556 VAL A C      1 
ATOM   1635 O O      . VAL A 1 217 ? -2.055  47.477  -34.248 1.00 33.70  ? 556 VAL A O      1 
ATOM   1636 C CB     . VAL A 1 217 ? -0.381  45.301  -35.198 1.00 27.34  ? 556 VAL A CB     1 
ATOM   1637 C CG1    . VAL A 1 217 ? 0.381   46.206  -36.155 1.00 32.83  ? 556 VAL A CG1    1 
ATOM   1638 C CG2    . VAL A 1 217 ? 0.192   43.893  -35.222 1.00 29.50  ? 556 VAL A CG2    1 
ATOM   1639 N N      . GLY A 1 218 ? -0.281  48.191  -33.050 1.00 30.46  ? 557 GLY A N      1 
ATOM   1640 C CA     . GLY A 1 218 ? -0.847  49.499  -32.800 1.00 33.24  ? 557 GLY A CA     1 
ATOM   1641 C C      . GLY A 1 218 ? -0.688  50.462  -33.961 1.00 34.89  ? 557 GLY A C      1 
ATOM   1642 O O      . GLY A 1 218 ? -0.015  50.192  -34.955 1.00 40.17  ? 557 GLY A O      1 
ATOM   1643 N N      . SER A 1 219 ? -1.333  51.615  -33.815 1.00 37.69  ? 558 SER A N      1 
ATOM   1644 C CA     . SER A 1 219 ? -1.288  52.660  -34.829 1.00 40.73  ? 558 SER A CA     1 
ATOM   1645 C C      . SER A 1 219 ? -0.161  53.646  -34.543 1.00 51.57  ? 558 SER A C      1 
ATOM   1646 O O      . SER A 1 219 ? -0.394  54.732  -34.010 1.00 59.27  ? 558 SER A O      1 
ATOM   1647 C CB     . SER A 1 219 ? -2.627  53.396  -34.897 1.00 48.62  ? 558 SER A CB     1 
ATOM   1648 O OG     . SER A 1 219 ? -3.694  52.493  -35.131 1.00 50.78  ? 558 SER A OG     1 
ATOM   1649 N N      . ASP A 1 227 ? 3.112   51.267  -37.134 1.00 34.31  ? 566 ASP A N      1 
ATOM   1650 C CA     . ASP A 1 227 ? 2.793   49.857  -36.931 1.00 34.14  ? 566 ASP A CA     1 
ATOM   1651 C C      . ASP A 1 227 ? 3.796   49.183  -36.003 1.00 33.95  ? 566 ASP A C      1 
ATOM   1652 O O      . ASP A 1 227 ? 4.694   48.474  -36.458 1.00 36.89  ? 566 ASP A O      1 
ATOM   1653 C CB     . ASP A 1 227 ? 2.750   49.116  -38.269 1.00 32.94  ? 566 ASP A CB     1 
ATOM   1654 C CG     . ASP A 1 227 ? 1.379   49.150  -38.913 1.00 35.45  ? 566 ASP A CG     1 
ATOM   1655 O OD1    . ASP A 1 227 ? 0.455   49.744  -38.318 1.00 42.71  ? 566 ASP A OD1    1 
ATOM   1656 O OD2    . ASP A 1 227 ? 1.226   48.579  -40.013 1.00 34.89  ? 566 ASP A OD2    1 
ATOM   1657 N N      . GLN A 1 228 ? 3.640   49.401  -34.702 1.00 30.58  ? 567 GLN A N      1 
ATOM   1658 C CA     . GLN A 1 228 ? 4.521   48.810  -33.705 1.00 35.82  ? 567 GLN A CA     1 
ATOM   1659 C C      . GLN A 1 228 ? 3.832   47.613  -33.066 1.00 31.53  ? 567 GLN A C      1 
ATOM   1660 O O      . GLN A 1 228 ? 2.686   47.716  -32.617 1.00 30.03  ? 567 GLN A O      1 
ATOM   1661 C CB     . GLN A 1 228 ? 4.910   49.830  -32.634 1.00 37.52  ? 567 GLN A CB     1 
ATOM   1662 C CG     . GLN A 1 228 ? 6.084   49.384  -31.777 1.00 43.69  ? 567 GLN A CG     1 
ATOM   1663 C CD     . GLN A 1 228 ? 6.431   50.381  -30.691 1.00 51.51  ? 567 GLN A CD     1 
ATOM   1664 O OE1    . GLN A 1 228 ? 5.586   51.165  -30.256 1.00 51.21  ? 567 GLN A OE1    1 
ATOM   1665 N NE2    . GLN A 1 228 ? 7.684   50.358  -30.247 1.00 53.44  ? 567 GLN A NE2    1 
ATOM   1666 N N      . LEU A 1 229 ? 4.536   46.484  -33.027 1.00 32.14  ? 568 LEU A N      1 
ATOM   1667 C CA     . LEU A 1 229 ? 3.985   45.255  -32.476 1.00 31.14  ? 568 LEU A CA     1 
ATOM   1668 C C      . LEU A 1 229 ? 4.028   45.287  -30.954 1.00 29.31  ? 568 LEU A C      1 
ATOM   1669 O O      . LEU A 1 229 ? 5.016   45.718  -30.353 1.00 28.73  ? 568 LEU A O      1 
ATOM   1670 C CB     . LEU A 1 229 ? 4.763   44.047  -32.997 1.00 32.24  ? 568 LEU A CB     1 
ATOM   1671 C CG     . LEU A 1 229 ? 5.051   44.016  -34.501 1.00 31.81  ? 568 LEU A CG     1 
ATOM   1672 C CD1    . LEU A 1 229 ? 5.956   42.844  -34.850 1.00 31.53  ? 568 LEU A CD1    1 
ATOM   1673 C CD2    . LEU A 1 229 ? 3.760   43.960  -35.304 1.00 29.87  ? 568 LEU A CD2    1 
ATOM   1674 N N      . LEU A 1 230 ? 2.946   44.818  -30.329 1.00 28.28  ? 569 LEU A N      1 
ATOM   1675 C CA     . LEU A 1 230 ? 2.874   44.820  -28.873 1.00 28.22  ? 569 LEU A CA     1 
ATOM   1676 C C      . LEU A 1 230 ? 3.918   43.907  -28.244 1.00 26.73  ? 569 LEU A C      1 
ATOM   1677 O O      . LEU A 1 230 ? 4.214   44.051  -27.053 1.00 26.35  ? 569 LEU A O      1 
ATOM   1678 C CB     . LEU A 1 230 ? 1.472   44.410  -28.416 1.00 25.40  ? 569 LEU A CB     1 
ATOM   1679 C CG     . LEU A 1 230 ? 1.168   44.540  -26.922 1.00 24.37  ? 569 LEU A CG     1 
ATOM   1680 C CD1    . LEU A 1 230 ? 1.439   45.958  -26.444 1.00 26.35  ? 569 LEU A CD1    1 
ATOM   1681 C CD2    . LEU A 1 230 ? -0.269  44.144  -26.633 1.00 24.21  ? 569 LEU A CD2    1 
ATOM   1682 N N      . ALA A 1 231 ? 4.483   42.975  -29.014 1.00 27.07  ? 570 ALA A N      1 
ATOM   1683 C CA     . ALA A 1 231 ? 5.488   42.057  -28.496 1.00 25.09  ? 570 ALA A CA     1 
ATOM   1684 C C      . ALA A 1 231 ? 6.889   42.654  -28.468 1.00 29.53  ? 570 ALA A C      1 
ATOM   1685 O O      . ALA A 1 231 ? 7.779   42.066  -27.845 1.00 30.34  ? 570 ALA A O      1 
ATOM   1686 C CB     . ALA A 1 231 ? 5.498   40.768  -29.323 1.00 22.64  ? 570 ALA A CB     1 
ATOM   1687 N N      . SER A 1 232 ? 7.113   43.791  -29.126 1.00 28.87  ? 571 SER A N      1 
ATOM   1688 C CA     . SER A 1 232 ? 8.409   44.455  -29.076 1.00 32.43  ? 571 SER A CA     1 
ATOM   1689 C C      . SER A 1 232 ? 8.440   45.632  -28.113 1.00 32.97  ? 571 SER A C      1 
ATOM   1690 O O      . SER A 1 232 ? 9.530   46.097  -27.761 1.00 39.02  ? 571 SER A O      1 
ATOM   1691 C CB     . SER A 1 232 ? 8.820   44.940  -30.473 1.00 29.67  ? 571 SER A CB     1 
ATOM   1692 O OG     . SER A 1 232 ? 7.976   45.986  -30.921 1.00 44.87  ? 571 SER A OG     1 
ATOM   1693 N N      . THR A 1 233 ? 7.276   46.119  -27.678 1.00 29.66  ? 572 THR A N      1 
ATOM   1694 C CA     . THR A 1 233 ? 7.249   47.259  -26.770 1.00 33.83  ? 572 THR A CA     1 
ATOM   1695 C C      . THR A 1 233 ? 7.628   46.855  -25.351 1.00 33.44  ? 572 THR A C      1 
ATOM   1696 O O      . THR A 1 233 ? 8.252   47.642  -24.630 1.00 33.62  ? 572 THR A O      1 
ATOM   1697 C CB     . THR A 1 233 ? 5.865   47.910  -26.786 1.00 34.99  ? 572 THR A CB     1 
ATOM   1698 O OG1    . THR A 1 233 ? 4.893   46.977  -26.296 1.00 38.46  ? 572 THR A OG1    1 
ATOM   1699 C CG2    . THR A 1 233 ? 5.490   48.326  -28.202 1.00 28.16  ? 572 THR A CG2    1 
ATOM   1700 N N      . VAL A 1 234 ? 7.269   45.637  -24.938 1.00 31.98  ? 573 VAL A N      1 
ATOM   1701 C CA     . VAL A 1 234 ? 7.554   45.197  -23.576 1.00 32.89  ? 573 VAL A CA     1 
ATOM   1702 C C      . VAL A 1 234 ? 9.050   45.200  -23.302 1.00 31.84  ? 573 VAL A C      1 
ATOM   1703 O O      . VAL A 1 234 ? 9.479   45.370  -22.155 1.00 30.29  ? 573 VAL A O      1 
ATOM   1704 C CB     . VAL A 1 234 ? 6.944   43.805  -23.326 1.00 30.41  ? 573 VAL A CB     1 
ATOM   1705 C CG1    . VAL A 1 234 ? 7.562   42.780  -24.264 1.00 29.75  ? 573 VAL A CG1    1 
ATOM   1706 C CG2    . VAL A 1 234 ? 7.141   43.398  -21.877 1.00 28.56  ? 573 VAL A CG2    1 
ATOM   1707 N N      . ASN A 1 235 ? 9.869   45.008  -24.339 1.00 35.70  ? 574 ASN A N      1 
ATOM   1708 C CA     . ASN A 1 235 ? 11.315  45.038  -24.148 1.00 37.51  ? 574 ASN A CA     1 
ATOM   1709 C C      . ASN A 1 235 ? 11.797  46.449  -23.831 1.00 43.61  ? 574 ASN A C      1 
ATOM   1710 O O      . ASN A 1 235 ? 12.638  46.641  -22.945 1.00 39.07  ? 574 ASN A O      1 
ATOM   1711 C CB     . ASN A 1 235 ? 12.015  44.496  -25.394 1.00 40.40  ? 574 ASN A CB     1 
ATOM   1712 C CG     . ASN A 1 235 ? 11.413  43.191  -25.877 1.00 39.39  ? 574 ASN A CG     1 
ATOM   1713 O OD1    . ASN A 1 235 ? 11.126  42.295  -25.082 1.00 41.76  ? 574 ASN A OD1    1 
ATOM   1714 N ND2    . ASN A 1 235 ? 11.209  43.081  -27.185 1.00 37.52  ? 574 ASN A ND2    1 
ATOM   1715 N N      . GLN A 1 236 ? 11.273  47.447  -24.545 1.00 34.15  ? 575 GLN A N      1 
ATOM   1716 C CA     . GLN A 1 236 ? 11.640  48.829  -24.265 1.00 37.21  ? 575 GLN A CA     1 
ATOM   1717 C C      . GLN A 1 236 ? 11.097  49.292  -22.919 1.00 37.52  ? 575 GLN A C      1 
ATOM   1718 O O      . GLN A 1 236 ? 11.721  50.126  -22.254 1.00 40.75  ? 575 GLN A O      1 
ATOM   1719 C CB     . GLN A 1 236 ? 11.133  49.737  -25.384 1.00 40.13  ? 575 GLN A CB     1 
ATOM   1720 C CG     . GLN A 1 236 ? 11.533  49.275  -26.776 1.00 46.36  ? 575 GLN A CG     1 
ATOM   1721 C CD     . GLN A 1 236 ? 10.686  49.903  -27.865 1.00 49.87  ? 575 GLN A CD     1 
ATOM   1722 O OE1    . GLN A 1 236 ? 10.059  50.943  -27.658 1.00 50.10  ? 575 GLN A OE1    1 
ATOM   1723 N NE2    . GLN A 1 236 ? 10.652  49.265  -29.031 1.00 46.49  ? 575 GLN A NE2    1 
ATOM   1724 N N      . VAL A 1 237 ? 9.944   48.762  -22.501 1.00 34.06  ? 576 VAL A N      1 
ATOM   1725 C CA     . VAL A 1 237 ? 9.352   49.176  -21.233 1.00 31.20  ? 576 VAL A CA     1 
ATOM   1726 C C      . VAL A 1 237 ? 10.159  48.651  -20.053 1.00 35.18  ? 576 VAL A C      1 
ATOM   1727 O O      . VAL A 1 237 ? 10.255  49.317  -19.015 1.00 38.31  ? 576 VAL A O      1 
ATOM   1728 C CB     . VAL A 1 237 ? 7.884   48.715  -21.154 1.00 26.30  ? 576 VAL A CB     1 
ATOM   1729 C CG1    . VAL A 1 237 ? 7.355   48.871  -19.735 1.00 24.91  ? 576 VAL A CG1    1 
ATOM   1730 C CG2    . VAL A 1 237 ? 7.028   49.500  -22.133 1.00 26.25  ? 576 VAL A CG2    1 
ATOM   1731 N N      . LEU A 1 238 ? 10.750  47.463  -20.183 1.00 31.17  ? 577 LEU A N      1 
ATOM   1732 C CA     . LEU A 1 238 ? 11.472  46.835  -19.085 1.00 32.73  ? 577 LEU A CA     1 
ATOM   1733 C C      . LEU A 1 238 ? 12.980  47.032  -19.161 1.00 36.94  ? 577 LEU A C      1 
ATOM   1734 O O      . LEU A 1 238 ? 13.686  46.642  -18.225 1.00 37.19  ? 577 LEU A O      1 
ATOM   1735 C CB     . LEU A 1 238 ? 11.155  45.336  -19.037 1.00 30.55  ? 577 LEU A CB     1 
ATOM   1736 C CG     . LEU A 1 238 ? 9.676   45.012  -18.817 1.00 28.32  ? 577 LEU A CG     1 
ATOM   1737 C CD1    . LEU A 1 238 ? 9.464   43.516  -18.648 1.00 32.45  ? 577 LEU A CD1    1 
ATOM   1738 C CD2    . LEU A 1 238 ? 9.135   45.776  -17.618 1.00 23.07  ? 577 LEU A CD2    1 
ATOM   1739 N N      . GLU A 1 239 ? 13.486  47.623  -20.238 1.00 38.29  ? 578 GLU A N      1 
ATOM   1740 C CA     . GLU A 1 239 ? 14.908  47.884  -20.381 1.00 36.36  ? 578 GLU A CA     1 
ATOM   1741 C C      . GLU A 1 239 ? 15.265  49.241  -19.778 1.00 38.05  ? 578 GLU A C      1 
ATOM   1742 O O      . GLU A 1 239 ? 14.401  50.021  -19.370 1.00 41.74  ? 578 GLU A O      1 
ATOM   1743 C CB     . GLU A 1 239 ? 15.314  47.843  -21.853 1.00 40.88  ? 578 GLU A CB     1 
ATOM   1744 C CG     . GLU A 1 239 ? 14.827  49.045  -22.647 1.00 49.25  ? 578 GLU A CG     1 
ATOM   1745 C CD     . GLU A 1 239 ? 15.318  49.043  -24.080 1.00 63.78  ? 578 GLU A CD     1 
ATOM   1746 O OE1    . GLU A 1 239 ? 15.503  47.945  -24.644 1.00 75.38  ? 578 GLU A OE1    1 
ATOM   1747 O OE2    . GLU A 1 239 ? 15.524  50.142  -24.640 1.00 56.18  ? 578 GLU A OE2    1 
ATOM   1748 N N      . GLY A 1 240 ? 16.563  49.515  -19.724 1.00 42.58  ? 579 GLY A N      1 
ATOM   1749 C CA     . GLY A 1 240 ? 17.036  50.804  -19.271 1.00 47.63  ? 579 GLY A CA     1 
ATOM   1750 C C      . GLY A 1 240 ? 16.570  51.176  -17.869 1.00 46.02  ? 579 GLY A C      1 
ATOM   1751 O O      . GLY A 1 240 ? 16.266  50.332  -17.023 1.00 42.75  ? 579 GLY A O      1 
ATOM   1752 N N      . ASP A 1 241 ? 16.526  52.484  -17.639 1.00 51.69  ? 580 ASP A N      1 
ATOM   1753 C CA     . ASP A 1 241 ? 16.199  53.050  -16.341 1.00 56.21  ? 580 ASP A CA     1 
ATOM   1754 C C      . ASP A 1 241 ? 14.759  53.551  -16.322 1.00 60.82  ? 580 ASP A C      1 
ATOM   1755 O O      . ASP A 1 241 ? 14.097  53.671  -17.356 1.00 54.58  ? 580 ASP A O      1 
ATOM   1756 C CB     . ASP A 1 241 ? 17.163  54.190  -16.000 1.00 63.49  ? 580 ASP A CB     1 
ATOM   1757 C CG     . ASP A 1 241 ? 18.617  53.788  -16.159 1.00 73.65  ? 580 ASP A CG     1 
ATOM   1758 O OD1    . ASP A 1 241 ? 18.970  52.650  -15.781 1.00 69.55  ? 580 ASP A OD1    1 
ATOM   1759 O OD2    . ASP A 1 241 ? 19.407  54.612  -16.666 1.00 70.55  ? 580 ASP A OD2    1 
ATOM   1760 N N      . ASN A 1 242 ? 14.281  53.852  -15.114 1.00 70.34  ? 581 ASN A N      1 
ATOM   1761 C CA     . ASN A 1 242 ? 12.922  54.350  -14.912 1.00 60.57  ? 581 ASN A CA     1 
ATOM   1762 C C      . ASN A 1 242 ? 11.888  53.320  -15.358 1.00 50.06  ? 581 ASN A C      1 
ATOM   1763 O O      . ASN A 1 242 ? 10.856  53.660  -15.939 1.00 52.52  ? 581 ASN A O      1 
ATOM   1764 C CB     . ASN A 1 242 ? 12.709  55.682  -15.633 1.00 56.87  ? 581 ASN A CB     1 
ATOM   1765 C CG     . ASN A 1 242 ? 13.665  56.761  -15.163 1.00 75.19  ? 581 ASN A CG     1 
ATOM   1766 O OD1    . ASN A 1 242 ? 14.436  57.310  -15.952 1.00 93.13  ? 581 ASN A OD1    1 
ATOM   1767 N ND2    . ASN A 1 242 ? 13.618  57.075  -13.874 1.00 87.34  ? 581 ASN A ND2    1 
ATOM   1768 N N      . VAL A 1 243 ? 12.168  52.044  -15.081 1.00 43.60  ? 582 VAL A N      1 
ATOM   1769 C CA     . VAL A 1 243 ? 11.257  50.980  -15.492 1.00 40.67  ? 582 VAL A CA     1 
ATOM   1770 C C      . VAL A 1 243 ? 9.898   51.137  -14.824 1.00 37.33  ? 582 VAL A C      1 
ATOM   1771 O O      . VAL A 1 243 ? 8.863   50.824  -15.426 1.00 35.18  ? 582 VAL A O      1 
ATOM   1772 C CB     . VAL A 1 243 ? 11.876  49.601  -15.194 1.00 35.91  ? 582 VAL A CB     1 
ATOM   1773 C CG1    . VAL A 1 243 ? 10.896  48.495  -15.544 1.00 29.50  ? 582 VAL A CG1    1 
ATOM   1774 C CG2    . VAL A 1 243 ? 13.178  49.429  -15.962 1.00 38.29  ? 582 VAL A CG2    1 
ATOM   1775 N N      . ARG A 1 244 ? 9.871   51.621  -13.580 1.00 34.75  ? 583 ARG A N      1 
ATOM   1776 C CA     . ARG A 1 244 ? 8.599   51.783  -12.882 1.00 32.61  ? 583 ARG A CA     1 
ATOM   1777 C C      . ARG A 1 244 ? 7.690   52.760  -13.619 1.00 29.94  ? 583 ARG A C      1 
ATOM   1778 O O      . ARG A 1 244 ? 6.507   52.476  -13.841 1.00 32.59  ? 583 ARG A O      1 
ATOM   1779 C CB     . ARG A 1 244 ? 8.841   52.238  -11.441 1.00 34.69  ? 583 ARG A CB     1 
ATOM   1780 C CG     . ARG A 1 244 ? 9.222   51.106  -10.492 1.00 38.92  ? 583 ARG A CG     1 
ATOM   1781 C CD     . ARG A 1 244 ? 9.364   51.583  -9.051  1.00 39.73  ? 583 ARG A CD     1 
ATOM   1782 N NE     . ARG A 1 244 ? 10.591  52.341  -8.833  1.00 45.45  ? 583 ARG A NE     1 
ATOM   1783 C CZ     . ARG A 1 244 ? 10.988  52.802  -7.654  1.00 48.52  ? 583 ARG A CZ     1 
ATOM   1784 N NH1    . ARG A 1 244 ? 10.275  52.601  -6.557  1.00 47.90  ? 583 ARG A NH1    1 
ATOM   1785 N NH2    . ARG A 1 244 ? 12.129  53.479  -7.573  1.00 46.44  ? 583 ARG A NH2    1 
ATOM   1786 N N      . GLU A 1 245 ? 8.228   53.915  -14.017 1.00 31.97  ? 584 GLU A N      1 
ATOM   1787 C CA     . GLU A 1 245 ? 7.409   54.901  -14.716 1.00 31.99  ? 584 GLU A CA     1 
ATOM   1788 C C      . GLU A 1 245 ? 6.984   54.400  -16.091 1.00 30.71  ? 584 GLU A C      1 
ATOM   1789 O O      . GLU A 1 245 ? 5.822   54.562  -16.484 1.00 27.67  ? 584 GLU A O      1 
ATOM   1790 C CB     . GLU A 1 245 ? 8.160   56.227  -14.837 1.00 30.07  ? 584 GLU A CB     1 
ATOM   1791 C CG     . GLU A 1 245 ? 8.055   57.106  -13.603 1.00 32.01  ? 584 GLU A CG     1 
ATOM   1792 C CD     . GLU A 1 245 ? 6.614   57.406  -13.225 1.00 41.60  ? 584 GLU A CD     1 
ATOM   1793 O OE1    . GLU A 1 245 ? 5.705   57.056  -14.009 1.00 36.66  ? 584 GLU A OE1    1 
ATOM   1794 O OE2    . GLU A 1 245 ? 6.390   57.991  -12.144 1.00 51.90  ? 584 GLU A OE2    1 
ATOM   1795 N N      . LYS A 1 246 ? 7.907   53.793  -16.839 1.00 29.15  ? 585 LYS A N      1 
ATOM   1796 C CA     . LYS A 1 246 ? 7.554   53.291  -18.161 1.00 26.75  ? 585 LYS A CA     1 
ATOM   1797 C C      . LYS A 1 246 ? 6.519   52.177  -18.077 1.00 30.00  ? 585 LYS A C      1 
ATOM   1798 O O      . LYS A 1 246 ? 5.725   52.001  -19.009 1.00 29.91  ? 585 LYS A O      1 
ATOM   1799 C CB     . LYS A 1 246 ? 8.807   52.815  -18.895 1.00 27.34  ? 585 LYS A CB     1 
ATOM   1800 C CG     . LYS A 1 246 ? 9.759   53.946  -19.252 1.00 31.54  ? 585 LYS A CG     1 
ATOM   1801 C CD     . LYS A 1 246 ? 10.859  53.495  -20.198 1.00 41.83  ? 585 LYS A CD     1 
ATOM   1802 C CE     . LYS A 1 246 ? 11.854  52.581  -19.506 1.00 44.95  ? 585 LYS A CE     1 
ATOM   1803 N NZ     . LYS A 1 246 ? 13.022  52.292  -20.384 1.00 43.27  ? 585 LYS A NZ     1 
ATOM   1804 N N      . LEU A 1 247 ? 6.500   51.430  -16.970 1.00 29.23  ? 586 LEU A N      1 
ATOM   1805 C CA     . LEU A 1 247 ? 5.514   50.367  -16.808 1.00 26.22  ? 586 LEU A CA     1 
ATOM   1806 C C      . LEU A 1 247 ? 4.148   50.920  -16.416 1.00 26.27  ? 586 LEU A C      1 
ATOM   1807 O O      . LEU A 1 247 ? 3.122   50.456  -16.926 1.00 23.60  ? 586 LEU A O      1 
ATOM   1808 C CB     . LEU A 1 247 ? 5.999   49.351  -15.774 1.00 27.52  ? 586 LEU A CB     1 
ATOM   1809 C CG     . LEU A 1 247 ? 4.987   48.297  -15.323 1.00 26.75  ? 586 LEU A CG     1 
ATOM   1810 C CD1    . LEU A 1 247 ? 4.222   47.728  -16.508 1.00 26.49  ? 586 LEU A CD1    1 
ATOM   1811 C CD2    . LEU A 1 247 ? 5.702   47.192  -14.568 1.00 28.20  ? 586 LEU A CD2    1 
ATOM   1812 N N      . ARG A 1 248 ? 4.111   51.900  -15.509 1.00 23.98  ? 587 ARG A N      1 
ATOM   1813 C CA     . ARG A 1 248 ? 2.847   52.558  -15.192 1.00 24.89  ? 587 ARG A CA     1 
ATOM   1814 C C      . ARG A 1 248 ? 2.185   53.087  -16.457 1.00 22.95  ? 587 ARG A C      1 
ATOM   1815 O O      . ARG A 1 248 ? 1.001   52.835  -16.708 1.00 26.17  ? 587 ARG A O      1 
ATOM   1816 C CB     . ARG A 1 248 ? 3.068   53.692  -14.188 1.00 26.34  ? 587 ARG A CB     1 
ATOM   1817 C CG     . ARG A 1 248 ? 3.142   53.262  -12.729 1.00 29.64  ? 587 ARG A CG     1 
ATOM   1818 C CD     . ARG A 1 248 ? 2.795   54.430  -11.810 1.00 39.75  ? 587 ARG A CD     1 
ATOM   1819 N NE     . ARG A 1 248 ? 3.368   54.293  -10.476 1.00 42.41  ? 587 ARG A NE     1 
ATOM   1820 C CZ     . ARG A 1 248 ? 2.729   53.792  -9.428  1.00 47.98  ? 587 ARG A CZ     1 
ATOM   1821 N NH1    . ARG A 1 248 ? 1.482   53.357  -9.520  1.00 47.96  ? 587 ARG A NH1    1 
ATOM   1822 N NH2    . ARG A 1 248 ? 3.356   53.726  -8.256  1.00 50.65  ? 587 ARG A NH2    1 
ATOM   1823 N N      . GLY A 1 249 ? 2.944   53.823  -17.272 1.00 23.94  ? 588 GLY A N      1 
ATOM   1824 C CA     . GLY A 1 249 ? 2.403   54.317  -18.526 1.00 25.53  ? 588 GLY A CA     1 
ATOM   1825 C C      . GLY A 1 249 ? 1.993   53.207  -19.472 1.00 25.27  ? 588 GLY A C      1 
ATOM   1826 O O      . GLY A 1 249 ? 1.091   53.388  -20.294 1.00 29.31  ? 588 GLY A O      1 
ATOM   1827 N N      . PHE A 1 250 ? 2.647   52.048  -19.376 1.00 23.88  ? 589 PHE A N      1 
ATOM   1828 C CA     . PHE A 1 250 ? 2.275   50.921  -20.223 1.00 24.39  ? 589 PHE A CA     1 
ATOM   1829 C C      . PHE A 1 250 ? 0.978   50.275  -19.756 1.00 26.33  ? 589 PHE A C      1 
ATOM   1830 O O      . PHE A 1 250 ? 0.259   49.677  -20.564 1.00 29.21  ? 589 PHE A O      1 
ATOM   1831 C CB     . PHE A 1 250 ? 3.404   49.891  -20.247 1.00 24.10  ? 589 PHE A CB     1 
ATOM   1832 C CG     . PHE A 1 250 ? 3.141   48.721  -21.151 1.00 23.45  ? 589 PHE A CG     1 
ATOM   1833 C CD1    . PHE A 1 250 ? 3.147   48.878  -22.527 1.00 24.77  ? 589 PHE A CD1    1 
ATOM   1834 C CD2    . PHE A 1 250 ? 2.901   47.462  -20.626 1.00 21.97  ? 589 PHE A CD2    1 
ATOM   1835 C CE1    . PHE A 1 250 ? 2.909   47.801  -23.364 1.00 25.65  ? 589 PHE A CE1    1 
ATOM   1836 C CE2    . PHE A 1 250 ? 2.664   46.382  -21.456 1.00 21.29  ? 589 PHE A CE2    1 
ATOM   1837 C CZ     . PHE A 1 250 ? 2.668   46.551  -22.827 1.00 22.58  ? 589 PHE A CZ     1 
ATOM   1838 N N      . MET A 1 251 ? 0.659   50.395  -18.470 1.00 25.02  ? 590 MET A N      1 
ATOM   1839 C CA     . MET A 1 251 ? -0.521  49.739  -17.927 1.00 26.09  ? 590 MET A CA     1 
ATOM   1840 C C      . MET A 1 251 ? -1.799  50.339  -18.503 1.00 25.28  ? 590 MET A C      1 
ATOM   1841 O O      . MET A 1 251 ? -1.878  51.541  -18.779 1.00 24.40  ? 590 MET A O      1 
ATOM   1842 C CB     . MET A 1 251 ? -0.533  49.843  -16.402 1.00 23.20  ? 590 MET A CB     1 
ATOM   1843 C CG     . MET A 1 251 ? 0.551   49.018  -15.730 1.00 23.00  ? 590 MET A CG     1 
ATOM   1844 S SD     . MET A 1 251 ? 0.490   47.298  -16.261 1.00 22.30  ? 590 MET A SD     1 
ATOM   1845 C CE     . MET A 1 251 ? -1.130  46.816  -15.664 1.00 19.67  ? 590 MET A CE     1 
ATOM   1846 N N      . ASP A 1 252 ? -2.802  49.487  -18.681 1.00 22.58  ? 591 ASP A N      1 
ATOM   1847 C CA     . ASP A 1 252 ? -4.092  49.895  -19.209 1.00 23.80  ? 591 ASP A CA     1 
ATOM   1848 C C      . ASP A 1 252 ? -4.660  51.051  -18.386 1.00 29.04  ? 591 ASP A C      1 
ATOM   1849 O O      . ASP A 1 252 ? -4.843  50.905  -17.167 1.00 28.50  ? 591 ASP A O      1 
ATOM   1850 C CB     . ASP A 1 252 ? -5.055  48.709  -19.193 1.00 24.15  ? 591 ASP A CB     1 
ATOM   1851 C CG     . ASP A 1 252 ? -6.335  48.978  -19.963 1.00 24.21  ? 591 ASP A CG     1 
ATOM   1852 O OD1    . ASP A 1 252 ? -6.802  50.138  -19.978 1.00 22.94  ? 591 ASP A OD1    1 
ATOM   1853 O OD2    . ASP A 1 252 ? -6.879  48.021  -20.554 1.00 28.44  ? 591 ASP A OD2    1 
ATOM   1854 N N      . PRO A 1 253 ? -4.947  52.201  -19.001 1.00 26.38  ? 592 PRO A N      1 
ATOM   1855 C CA     . PRO A 1 253 ? -5.527  53.315  -18.233 1.00 26.36  ? 592 PRO A CA     1 
ATOM   1856 C C      . PRO A 1 253 ? -6.811  52.945  -17.512 1.00 28.76  ? 592 PRO A C      1 
ATOM   1857 O O      . PRO A 1 253 ? -7.069  53.460  -16.416 1.00 36.46  ? 592 PRO A O      1 
ATOM   1858 C CB     . PRO A 1 253 ? -5.770  54.387  -19.305 1.00 28.39  ? 592 PRO A CB     1 
ATOM   1859 C CG     . PRO A 1 253 ? -4.816  54.052  -20.403 1.00 27.22  ? 592 PRO A CG     1 
ATOM   1860 C CD     . PRO A 1 253 ? -4.716  52.556  -20.412 1.00 24.73  ? 592 PRO A CD     1 
ATOM   1861 N N      . ASN A 1 254 ? -7.623  52.057  -18.092 1.00 30.12  ? 593 ASN A N      1 
ATOM   1862 C CA     . ASN A 1 254 ? -8.916  51.726  -17.503 1.00 27.91  ? 593 ASN A CA     1 
ATOM   1863 C C      . ASN A 1 254 ? -8.788  51.015  -16.162 1.00 29.00  ? 593 ASN A C      1 
ATOM   1864 O O      . ASN A 1 254 ? -9.778  50.928  -15.428 1.00 31.54  ? 593 ASN A O      1 
ATOM   1865 C CB     . ASN A 1 254 ? -9.729  50.872  -18.476 1.00 27.67  ? 593 ASN A CB     1 
ATOM   1866 C CG     . ASN A 1 254 ? -10.092 51.622  -19.743 1.00 32.48  ? 593 ASN A CG     1 
ATOM   1867 O OD1    . ASN A 1 254 ? -10.280 52.839  -19.724 1.00 30.78  ? 593 ASN A OD1    1 
ATOM   1868 N ND2    . ASN A 1 254 ? -10.191 50.898  -20.853 1.00 34.81  ? 593 ASN A ND2    1 
ATOM   1869 N N      . LEU A 1 255 ? -7.602  50.502  -15.827 1.00 29.17  ? 594 LEU A N      1 
ATOM   1870 C CA     . LEU A 1 255 ? -7.406  49.915  -14.505 1.00 28.57  ? 594 LEU A CA     1 
ATOM   1871 C C      . LEU A 1 255 ? -7.426  50.980  -13.416 1.00 31.93  ? 594 LEU A C      1 
ATOM   1872 O O      . LEU A 1 255 ? -7.868  50.709  -12.293 1.00 33.78  ? 594 LEU A O      1 
ATOM   1873 C CB     . LEU A 1 255 ? -6.097  49.127  -14.468 1.00 27.78  ? 594 LEU A CB     1 
ATOM   1874 C CG     . LEU A 1 255 ? -6.078  47.834  -15.288 1.00 23.51  ? 594 LEU A CG     1 
ATOM   1875 C CD1    . LEU A 1 255 ? -4.658  47.311  -15.435 1.00 23.41  ? 594 LEU A CD1    1 
ATOM   1876 C CD2    . LEU A 1 255 ? -6.974  46.780  -14.651 1.00 23.16  ? 594 LEU A CD2    1 
ATOM   1877 N N      . ARG A 1 256 ? -6.953  52.188  -13.724 1.00 31.94  ? 595 ARG A N      1 
ATOM   1878 C CA     . ARG A 1 256 ? -7.070  53.333  -12.823 1.00 34.96  ? 595 ARG A CA     1 
ATOM   1879 C C      . ARG A 1 256 ? -6.386  53.071  -11.481 1.00 35.05  ? 595 ARG A C      1 
ATOM   1880 O O      . ARG A 1 256 ? -6.987  53.210  -10.414 1.00 40.33  ? 595 ARG A O      1 
ATOM   1881 C CB     . ARG A 1 256 ? -8.539  53.714  -12.620 1.00 39.68  ? 595 ARG A CB     1 
ATOM   1882 C CG     . ARG A 1 256 ? -9.159  54.452  -13.793 1.00 40.85  ? 595 ARG A CG     1 
ATOM   1883 C CD     . ARG A 1 256 ? -10.578 54.907  -13.476 1.00 60.60  ? 595 ARG A CD     1 
ATOM   1884 N NE     . ARG A 1 256 ? -10.788 55.101  -12.045 1.00 70.23  ? 595 ARG A NE     1 
ATOM   1885 C CZ     . ARG A 1 256 ? -11.698 54.455  -11.327 1.00 71.53  ? 595 ARG A CZ     1 
ATOM   1886 N NH1    . ARG A 1 256 ? -12.533 53.592  -11.883 1.00 79.12  ? 595 ARG A NH1    1 
ATOM   1887 N NH2    . ARG A 1 256 ? -11.778 54.689  -10.020 1.00 63.38  ? 595 ARG A NH2    1 
ATOM   1888 N N      . ASP A 1 257 ? -5.110  52.690  -11.542 1.00 32.27  ? 596 ASP A N      1 
ATOM   1889 C CA     . ASP A 1 257 ? -4.303  52.520  -10.337 1.00 32.32  ? 596 ASP A CA     1 
ATOM   1890 C C      . ASP A 1 257 ? -4.726  51.309  -9.513  1.00 27.91  ? 596 ASP A C      1 
ATOM   1891 O O      . ASP A 1 257 ? -4.026  50.925  -8.571  1.00 30.09  ? 596 ASP A O      1 
ATOM   1892 C CB     . ASP A 1 257 ? -4.366  53.778  -9.465  1.00 32.69  ? 596 ASP A CB     1 
ATOM   1893 C CG     . ASP A 1 257 ? -3.575  54.935  -10.044 1.00 49.09  ? 596 ASP A CG     1 
ATOM   1894 O OD1    . ASP A 1 257 ? -3.299  54.922  -11.263 1.00 52.16  ? 596 ASP A OD1    1 
ATOM   1895 O OD2    . ASP A 1 257 ? -3.218  55.852  -9.273  1.00 61.60  ? 596 ASP A OD2    1 
ATOM   1896 N N      . GLU A 1 258 ? -5.863  50.699  -9.850  1.00 26.03  ? 597 GLU A N      1 
ATOM   1897 C CA     . GLU A 1 258 ? -6.380  49.561  -9.089  1.00 27.29  ? 597 GLU A CA     1 
ATOM   1898 C C      . GLU A 1 258 ? -5.694  48.262  -9.523  1.00 26.21  ? 597 GLU A C      1 
ATOM   1899 O O      . GLU A 1 258 ? -6.309  47.332  -10.045 1.00 25.60  ? 597 GLU A O      1 
ATOM   1900 C CB     . GLU A 1 258 ? -7.893  49.463  -9.237  1.00 28.02  ? 597 GLU A CB     1 
ATOM   1901 C CG     . GLU A 1 258 ? -8.670  50.454  -8.386  1.00 33.11  ? 597 GLU A CG     1 
ATOM   1902 C CD     . GLU A 1 258 ? -10.164 50.173  -8.386  1.00 30.62  ? 597 GLU A CD     1 
ATOM   1903 O OE1    . GLU A 1 258 ? -10.549 48.988  -8.480  1.00 29.61  ? 597 GLU A OE1    1 
ATOM   1904 O OE2    . GLU A 1 258 ? -10.951 51.139  -8.299  1.00 33.10  ? 597 GLU A OE2    1 
ATOM   1905 N N      . TYR A 1 259 ? -4.384  48.215  -9.289  1.00 21.72  ? 598 TYR A N      1 
ATOM   1906 C CA     . TYR A 1 259 ? -3.596  47.028  -9.583  1.00 22.48  ? 598 TYR A CA     1 
ATOM   1907 C C      . TYR A 1 259 ? -2.280  47.125  -8.831  1.00 21.21  ? 598 TYR A C      1 
ATOM   1908 O O      . TYR A 1 259 ? -1.762  48.231  -8.635  1.00 20.24  ? 598 TYR A O      1 
ATOM   1909 C CB     . TYR A 1 259 ? -3.344  46.882  -11.091 1.00 23.32  ? 598 TYR A CB     1 
ATOM   1910 C CG     . TYR A 1 259 ? -2.445  47.947  -11.675 1.00 20.80  ? 598 TYR A CG     1 
ATOM   1911 C CD1    . TYR A 1 259 ? -1.064  47.788  -11.689 1.00 20.99  ? 598 TYR A CD1    1 
ATOM   1912 C CD2    . TYR A 1 259 ? -2.976  49.111  -12.211 1.00 21.54  ? 598 TYR A CD2    1 
ATOM   1913 C CE1    . TYR A 1 259 ? -0.238  48.759  -12.220 1.00 21.92  ? 598 TYR A CE1    1 
ATOM   1914 C CE2    . TYR A 1 259 ? -2.158  50.089  -12.745 1.00 22.38  ? 598 TYR A CE2    1 
ATOM   1915 C CZ     . TYR A 1 259 ? -0.789  49.908  -12.747 1.00 19.64  ? 598 TYR A CZ     1 
ATOM   1916 O OH     . TYR A 1 259 ? 0.034   50.876  -13.277 1.00 23.02  ? 598 TYR A OH     1 
ATOM   1917 N N      . PRO A 1 260 ? -1.723  46.001  -8.388  1.00 21.55  ? 599 PRO A N      1 
ATOM   1918 C CA     . PRO A 1 260 ? -0.406  46.010  -7.737  1.00 22.79  ? 599 PRO A CA     1 
ATOM   1919 C C      . PRO A 1 260 ? 0.693   46.143  -8.778  1.00 24.65  ? 599 PRO A C      1 
ATOM   1920 O O      . PRO A 1 260 ? 0.977   45.204  -9.530  1.00 21.23  ? 599 PRO A O      1 
ATOM   1921 C CB     . PRO A 1 260 ? -0.363  44.651  -7.024  1.00 19.72  ? 599 PRO A CB     1 
ATOM   1922 C CG     . PRO A 1 260 ? -1.238  43.776  -7.864  1.00 21.33  ? 599 PRO A CG     1 
ATOM   1923 C CD     . PRO A 1 260 ? -2.331  44.661  -8.398  1.00 21.16  ? 599 PRO A CD     1 
ATOM   1924 N N      . LEU A 1 261 ? 1.325   47.320  -8.820  1.00 25.10  ? 600 LEU A N      1 
ATOM   1925 C CA     . LEU A 1 261 ? 2.397   47.548  -9.784  1.00 25.18  ? 600 LEU A CA     1 
ATOM   1926 C C      . LEU A 1 261 ? 3.476   46.482  -9.680  1.00 23.53  ? 600 LEU A C      1 
ATOM   1927 O O      . LEU A 1 261 ? 4.102   46.128  -10.686 1.00 28.74  ? 600 LEU A O      1 
ATOM   1928 C CB     . LEU A 1 261 ? 3.003   48.936  -9.581  1.00 27.41  ? 600 LEU A CB     1 
ATOM   1929 C CG     . LEU A 1 261 ? 4.177   49.268  -10.504 1.00 26.30  ? 600 LEU A CG     1 
ATOM   1930 C CD1    . LEU A 1 261 ? 3.749   49.180  -11.960 1.00 21.29  ? 600 LEU A CD1    1 
ATOM   1931 C CD2    . LEU A 1 261 ? 4.756   50.639  -10.192 1.00 28.10  ? 600 LEU A CD2    1 
ATOM   1932 N N      . ASP A 1 262 ? 3.701   45.954  -8.479  1.00 24.81  ? 601 ASP A N      1 
ATOM   1933 C CA     . ASP A 1 262 ? 4.693   44.900  -8.305  1.00 25.79  ? 601 ASP A CA     1 
ATOM   1934 C C      . ASP A 1 262 ? 4.354   43.687  -9.164  1.00 28.30  ? 601 ASP A C      1 
ATOM   1935 O O      . ASP A 1 262 ? 5.154   43.254  -10.000 1.00 34.20  ? 601 ASP A O      1 
ATOM   1936 C CB     . ASP A 1 262 ? 4.783   44.512  -6.829  1.00 29.15  ? 601 ASP A CB     1 
ATOM   1937 C CG     . ASP A 1 262 ? 5.891   43.518  -6.557  1.00 36.39  ? 601 ASP A CG     1 
ATOM   1938 O OD1    . ASP A 1 262 ? 7.074   43.918  -6.602  1.00 45.59  ? 601 ASP A OD1    1 
ATOM   1939 O OD2    . ASP A 1 262 ? 5.582   42.334  -6.302  1.00 36.97  ? 601 ASP A OD2    1 
ATOM   1940 N N      . LEU A 1 263 ? 3.159   43.125  -8.968  1.00 29.38  ? 602 LEU A N      1 
ATOM   1941 C CA     . LEU A 1 263 ? 2.768   41.932  -9.710  1.00 22.97  ? 602 LEU A CA     1 
ATOM   1942 C C      . LEU A 1 263 ? 2.583   42.221  -11.194 1.00 24.79  ? 602 LEU A C      1 
ATOM   1943 O O      . LEU A 1 263 ? 2.724   41.313  -12.020 1.00 23.76  ? 602 LEU A O      1 
ATOM   1944 C CB     . LEU A 1 263 ? 1.492   41.343  -9.109  1.00 18.06  ? 602 LEU A CB     1 
ATOM   1945 C CG     . LEU A 1 263 ? 1.564   41.085  -7.602  1.00 24.15  ? 602 LEU A CG     1 
ATOM   1946 C CD1    . LEU A 1 263 ? 0.249   40.525  -7.081  1.00 24.39  ? 602 LEU A CD1    1 
ATOM   1947 C CD2    . LEU A 1 263 ? 2.722   40.156  -7.264  1.00 29.88  ? 602 LEU A CD2    1 
ATOM   1948 N N      . ALA A 1 264 ? 2.264   43.466  -11.554 1.00 25.20  ? 603 ALA A N      1 
ATOM   1949 C CA     . ALA A 1 264 ? 2.177   43.823  -12.967 1.00 19.75  ? 603 ALA A CA     1 
ATOM   1950 C C      . ALA A 1 264 ? 3.541   43.720  -13.637 1.00 25.63  ? 603 ALA A C      1 
ATOM   1951 O O      . ALA A 1 264 ? 3.679   43.109  -14.703 1.00 23.26  ? 603 ALA A O      1 
ATOM   1952 C CB     . ALA A 1 264 ? 1.601   45.231  -13.118 1.00 19.26  ? 603 ALA A CB     1 
ATOM   1953 N N      . PHE A 1 265 ? 4.567   44.313  -13.019 1.00 27.20  ? 604 PHE A N      1 
ATOM   1954 C CA     . PHE A 1 265 ? 5.925   44.173  -13.535 1.00 26.40  ? 604 PHE A CA     1 
ATOM   1955 C C      . PHE A 1 265 ? 6.311   42.706  -13.661 1.00 24.74  ? 604 PHE A C      1 
ATOM   1956 O O      . PHE A 1 265 ? 6.843   42.276  -14.691 1.00 24.80  ? 604 PHE A O      1 
ATOM   1957 C CB     . PHE A 1 265 ? 6.911   44.912  -12.630 1.00 21.51  ? 604 PHE A CB     1 
ATOM   1958 C CG     . PHE A 1 265 ? 8.346   44.524  -12.858 1.00 29.50  ? 604 PHE A CG     1 
ATOM   1959 C CD1    . PHE A 1 265 ? 9.091   45.127  -13.858 1.00 33.10  ? 604 PHE A CD1    1 
ATOM   1960 C CD2    . PHE A 1 265 ? 8.948   43.552  -12.075 1.00 29.57  ? 604 PHE A CD2    1 
ATOM   1961 C CE1    . PHE A 1 265 ? 10.409  44.770  -14.071 1.00 27.05  ? 604 PHE A CE1    1 
ATOM   1962 C CE2    . PHE A 1 265 ? 10.266  43.190  -12.285 1.00 32.59  ? 604 PHE A CE2    1 
ATOM   1963 C CZ     . PHE A 1 265 ? 10.997  43.801  -13.284 1.00 31.82  ? 604 PHE A CZ     1 
ATOM   1964 N N      . SER A 1 266 ? 6.054   41.922  -12.612 1.00 25.22  ? 605 SER A N      1 
ATOM   1965 C CA     . SER A 1 266 ? 6.347   40.493  -12.659 1.00 22.90  ? 605 SER A CA     1 
ATOM   1966 C C      . SER A 1 266 ? 5.649   39.833  -13.840 1.00 23.00  ? 605 SER A C      1 
ATOM   1967 O O      . SER A 1 266 ? 6.273   39.106  -14.621 1.00 22.73  ? 605 SER A O      1 
ATOM   1968 C CB     . SER A 1 266 ? 5.928   39.838  -11.341 1.00 27.76  ? 605 SER A CB     1 
ATOM   1969 O OG     . SER A 1 266 ? 6.240   38.456  -11.325 1.00 39.62  ? 605 SER A OG     1 
ATOM   1970 N N      . MET A 1 267 ? 4.347   40.083  -13.990 1.00 24.11  ? 606 MET A N      1 
ATOM   1971 C CA     . MET A 1 267 ? 3.602   39.496  -15.099 1.00 22.72  ? 606 MET A CA     1 
ATOM   1972 C C      . MET A 1 267 ? 4.137   39.985  -16.439 1.00 25.32  ? 606 MET A C      1 
ATOM   1973 O O      . MET A 1 267 ? 4.236   39.210  -17.399 1.00 23.79  ? 606 MET A O      1 
ATOM   1974 C CB     . MET A 1 267 ? 2.117   39.823  -14.953 1.00 20.46  ? 606 MET A CB     1 
ATOM   1975 C CG     . MET A 1 267 ? 1.190   38.877  -15.685 1.00 31.44  ? 606 MET A CG     1 
ATOM   1976 S SD     . MET A 1 267 ? -0.510  39.108  -15.144 1.00 31.26  ? 606 MET A SD     1 
ATOM   1977 C CE     . MET A 1 267 ? -0.273  39.138  -13.373 1.00 25.28  ? 606 MET A CE     1 
ATOM   1978 N N      . ALA A 1 268 ? 4.483   41.271  -16.526 1.00 23.67  ? 607 ALA A N      1 
ATOM   1979 C CA     . ALA A 1 268 ? 5.100   41.784  -17.744 1.00 21.77  ? 607 ALA A CA     1 
ATOM   1980 C C      . ALA A 1 268 ? 6.424   41.089  -18.028 1.00 21.36  ? 607 ALA A C      1 
ATOM   1981 O O      . ALA A 1 268 ? 6.787   40.896  -19.194 1.00 22.24  ? 607 ALA A O      1 
ATOM   1982 C CB     . ALA A 1 268 ? 5.299   43.296  -17.635 1.00 19.90  ? 607 ALA A CB     1 
ATOM   1983 N N      . GLU A 1 269 ? 7.154   40.702  -16.978 1.00 24.14  ? 608 GLU A N      1 
ATOM   1984 C CA     . GLU A 1 269 ? 8.424   40.008  -17.166 1.00 22.42  ? 608 GLU A CA     1 
ATOM   1985 C C      . GLU A 1 269 ? 8.218   38.629  -17.778 1.00 20.16  ? 608 GLU A C      1 
ATOM   1986 O O      . GLU A 1 269 ? 8.934   38.245  -18.710 1.00 25.35  ? 608 GLU A O      1 
ATOM   1987 C CB     . GLU A 1 269 ? 9.165   39.898  -15.833 1.00 21.77  ? 608 GLU A CB     1 
ATOM   1988 C CG     . GLU A 1 269 ? 10.363  38.960  -15.860 1.00 26.56  ? 608 GLU A CG     1 
ATOM   1989 C CD     . GLU A 1 269 ? 11.492  39.473  -16.734 1.00 29.46  ? 608 GLU A CD     1 
ATOM   1990 O OE1    . GLU A 1 269 ? 11.496  40.681  -17.052 1.00 33.64  ? 608 GLU A OE1    1 
ATOM   1991 O OE2    . GLU A 1 269 ? 12.376  38.670  -17.102 1.00 30.95  ? 608 GLU A OE2    1 
ATOM   1992 N N      . ILE A 1 270 ? 7.246   37.865  -17.271 1.00 19.70  ? 609 ILE A N      1 
ATOM   1993 C CA     . ILE A 1 270 ? 6.983   36.548  -17.839 1.00 22.21  ? 609 ILE A CA     1 
ATOM   1994 C C      . ILE A 1 270 ? 6.465   36.651  -19.267 1.00 21.80  ? 609 ILE A C      1 
ATOM   1995 O O      . ILE A 1 270 ? 6.602   35.697  -20.041 1.00 22.45  ? 609 ILE A O      1 
ATOM   1996 C CB     . ILE A 1 270 ? 5.995   35.758  -16.959 1.00 22.17  ? 609 ILE A CB     1 
ATOM   1997 C CG1    . ILE A 1 270 ? 6.075   34.263  -17.282 1.00 23.93  ? 609 ILE A CG1    1 
ATOM   1998 C CG2    . ILE A 1 270 ? 4.577   36.266  -17.158 1.00 21.88  ? 609 ILE A CG2    1 
ATOM   1999 C CD1    . ILE A 1 270 ? 7.450   33.660  -17.063 1.00 19.86  ? 609 ILE A CD1    1 
ATOM   2000 N N      . ALA A 1 271 ? 5.870   37.785  -19.640 1.00 23.16  ? 610 ALA A N      1 
ATOM   2001 C CA     . ALA A 1 271 ? 5.444   37.981  -21.020 1.00 20.53  ? 610 ALA A CA     1 
ATOM   2002 C C      . ALA A 1 271 ? 6.629   38.280  -21.930 1.00 22.79  ? 610 ALA A C      1 
ATOM   2003 O O      . ALA A 1 271 ? 6.679   37.794  -23.065 1.00 24.12  ? 610 ALA A O      1 
ATOM   2004 C CB     . ALA A 1 271 ? 4.410   39.104  -21.099 1.00 18.96  ? 610 ALA A CB     1 
ATOM   2005 N N      . LYS A 1 272 ? 7.590   39.078  -21.454 1.00 22.27  ? 611 LYS A N      1 
ATOM   2006 C CA     . LYS A 1 272 ? 8.785   39.340  -22.250 1.00 25.92  ? 611 LYS A CA     1 
ATOM   2007 C C      . LYS A 1 272 ? 9.513   38.045  -22.586 1.00 22.80  ? 611 LYS A C      1 
ATOM   2008 O O      . LYS A 1 272 ? 9.932   37.837  -23.730 1.00 23.30  ? 611 LYS A O      1 
ATOM   2009 C CB     . LYS A 1 272 ? 9.721   40.298  -21.512 1.00 20.72  ? 611 LYS A CB     1 
ATOM   2010 C CG     . LYS A 1 272 ? 11.029  40.551  -22.250 1.00 17.39  ? 611 LYS A CG     1 
ATOM   2011 C CD     . LYS A 1 272 ? 12.155  40.911  -21.293 1.00 27.66  ? 611 LYS A CD     1 
ATOM   2012 C CE     . LYS A 1 272 ? 12.411  42.409  -21.250 1.00 34.94  ? 611 LYS A CE     1 
ATOM   2013 N NZ     . LYS A 1 272 ? 13.110  42.888  -22.477 1.00 34.23  ? 611 LYS A NZ     1 
ATOM   2014 N N      . ARG A 1 273 ? 9.677   37.162  -21.598 1.00 23.72  ? 612 ARG A N      1 
ATOM   2015 C CA     . ARG A 1 273 ? 10.316  35.878  -21.862 1.00 20.80  ? 612 ARG A CA     1 
ATOM   2016 C C      . ARG A 1 273 ? 9.510   35.063  -22.863 1.00 21.30  ? 612 ARG A C      1 
ATOM   2017 O O      . ARG A 1 273 ? 10.079  34.351  -23.698 1.00 21.55  ? 612 ARG A O      1 
ATOM   2018 C CB     . ARG A 1 273 ? 10.492  35.102  -20.558 1.00 22.62  ? 612 ARG A CB     1 
ATOM   2019 C CG     . ARG A 1 273 ? 11.210  35.878  -19.469 1.00 27.03  ? 612 ARG A CG     1 
ATOM   2020 C CD     . ARG A 1 273 ? 11.479  35.006  -18.253 1.00 28.27  ? 612 ARG A CD     1 
ATOM   2021 N NE     . ARG A 1 273 ? 12.218  35.721  -17.219 1.00 25.07  ? 612 ARG A NE     1 
ATOM   2022 C CZ     . ARG A 1 273 ? 12.665  35.165  -16.102 1.00 32.72  ? 612 ARG A CZ     1 
ATOM   2023 N NH1    . ARG A 1 273 ? 12.473  33.881  -15.845 1.00 37.75  ? 612 ARG A NH1    1 
ATOM   2024 N NH2    . ARG A 1 273 ? 13.323  35.914  -15.221 1.00 38.78  ? 612 ARG A NH2    1 
ATOM   2025 N N      . CYS A 1 274 ? 8.180   35.157  -22.797 1.00 22.62  ? 613 CYS A N      1 
ATOM   2026 C CA     . CYS A 1 274 ? 7.347   34.411  -23.732 1.00 21.27  ? 613 CYS A CA     1 
ATOM   2027 C C      . CYS A 1 274 ? 7.496   34.930  -25.157 1.00 25.54  ? 613 CYS A C      1 
ATOM   2028 O O      . CYS A 1 274 ? 7.391   34.149  -26.110 1.00 28.46  ? 613 CYS A O      1 
ATOM   2029 C CB     . CYS A 1 274 ? 5.883   34.468  -23.295 1.00 20.95  ? 613 CYS A CB     1 
ATOM   2030 S SG     . CYS A 1 274 ? 5.507   33.515  -21.803 1.00 16.97  ? 613 CYS A SG     1 
ATOM   2031 N N      . VAL A 1 275 ? 7.747   36.226  -25.324 1.00 22.51  ? 614 VAL A N      1 
ATOM   2032 C CA     . VAL A 1 275 ? 7.852   36.832  -26.645 1.00 17.33  ? 614 VAL A CA     1 
ATOM   2033 C C      . VAL A 1 275 ? 9.307   36.927  -27.110 1.00 22.15  ? 614 VAL A C      1 
ATOM   2034 O O      . VAL A 1 275 ? 9.607   37.655  -28.055 1.00 19.53  ? 614 VAL A O      1 
ATOM   2035 C CB     . VAL A 1 275 ? 7.163   38.205  -26.692 1.00 18.36  ? 614 VAL A CB     1 
ATOM   2036 C CG1    . VAL A 1 275 ? 5.673   38.063  -26.405 1.00 20.18  ? 614 VAL A CG1    1 
ATOM   2037 C CG2    . VAL A 1 275 ? 7.815   39.166  -25.709 1.00 24.41  ? 614 VAL A CG2    1 
ATOM   2038 N N      . ALA A 1 276 ? 10.217  36.202  -26.464 1.00 22.92  ? 615 ALA A N      1 
ATOM   2039 C CA     . ALA A 1 276 ? 11.595  36.162  -26.933 1.00 22.60  ? 615 ALA A CA     1 
ATOM   2040 C C      . ALA A 1 276 ? 11.661  35.547  -28.327 1.00 27.10  ? 615 ALA A C      1 
ATOM   2041 O O      . ALA A 1 276 ? 10.842  34.701  -28.696 1.00 28.74  ? 615 ALA A O      1 
ATOM   2042 C CB     . ALA A 1 276 ? 12.467  35.365  -25.963 1.00 22.36  ? 615 ALA A CB     1 
ATOM   2043 N N      . ARG A 1 277 ? 12.653  35.982  -29.110 1.00 30.59  ? 616 ARG A N      1 
ATOM   2044 C CA     . ARG A 1 277 ? 12.786  35.471  -30.473 1.00 34.56  ? 616 ARG A CA     1 
ATOM   2045 C C      . ARG A 1 277 ? 13.262  34.023  -30.482 1.00 41.28  ? 616 ARG A C      1 
ATOM   2046 O O      . ARG A 1 277 ? 12.797  33.218  -31.299 1.00 39.83  ? 616 ARG A O      1 
ATOM   2047 C CB     . ARG A 1 277 ? 13.736  36.355  -31.283 1.00 42.13  ? 616 ARG A CB     1 
ATOM   2048 C CG     . ARG A 1 277 ? 13.124  37.673  -31.739 1.00 51.92  ? 616 ARG A CG     1 
ATOM   2049 C CD     . ARG A 1 277 ? 14.072  38.454  -32.645 1.00 50.56  ? 616 ARG A CD     1 
ATOM   2050 N NE     . ARG A 1 277 ? 14.175  37.878  -33.981 1.00 53.14  ? 616 ARG A NE     1 
ATOM   2051 C CZ     . ARG A 1 277 ? 13.409  38.224  -35.007 1.00 49.74  ? 616 ARG A CZ     1 
ATOM   2052 N NH1    . ARG A 1 277 ? 12.456  39.133  -34.883 1.00 43.99  ? 616 ARG A NH1    1 
ATOM   2053 N NH2    . ARG A 1 277 ? 13.603  37.643  -36.188 1.00 44.39  ? 616 ARG A NH2    1 
ATOM   2054 N N      . ASP A 1 278 ? 14.187  33.671  -29.592 1.00 38.46  ? 617 ASP A N      1 
ATOM   2055 C CA     . ASP A 1 278 ? 14.676  32.301  -29.493 1.00 37.10  ? 617 ASP A CA     1 
ATOM   2056 C C      . ASP A 1 278 ? 13.648  31.446  -28.763 1.00 33.39  ? 617 ASP A C      1 
ATOM   2057 O O      . ASP A 1 278 ? 13.337  31.701  -27.594 1.00 33.57  ? 617 ASP A O      1 
ATOM   2058 C CB     . ASP A 1 278 ? 16.021  32.265  -28.772 1.00 37.36  ? 617 ASP A CB     1 
ATOM   2059 C CG     . ASP A 1 278 ? 17.117  32.962  -29.552 1.00 58.09  ? 617 ASP A CG     1 
ATOM   2060 O OD1    . ASP A 1 278 ? 16.822  33.500  -30.641 1.00 65.55  ? 617 ASP A OD1    1 
ATOM   2061 O OD2    . ASP A 1 278 ? 18.274  32.970  -29.080 1.00 62.28  ? 617 ASP A OD2    1 
ATOM   2062 N N      . LEU A 1 279 ? 13.124  30.428  -29.448 1.00 31.23  ? 618 LEU A N      1 
ATOM   2063 C CA     . LEU A 1 279 ? 12.070  29.610  -28.856 1.00 28.42  ? 618 LEU A CA     1 
ATOM   2064 C C      . LEU A 1 279 ? 12.564  28.880  -27.613 1.00 30.17  ? 618 LEU A C      1 
ATOM   2065 O O      . LEU A 1 279 ? 11.843  28.788  -26.613 1.00 31.28  ? 618 LEU A O      1 
ATOM   2066 C CB     . LEU A 1 279 ? 11.526  28.623  -29.892 1.00 23.05  ? 618 LEU A CB     1 
ATOM   2067 C CG     . LEU A 1 279 ? 12.487  27.631  -30.548 1.00 29.52  ? 618 LEU A CG     1 
ATOM   2068 C CD1    . LEU A 1 279 ? 12.764  26.444  -29.636 1.00 40.67  ? 618 LEU A CD1    1 
ATOM   2069 C CD2    . LEU A 1 279 ? 11.933  27.163  -31.881 1.00 31.06  ? 618 LEU A CD2    1 
ATOM   2070 N N      . ASN A 1 280 ? 13.795  28.362  -27.648 1.00 34.84  ? 619 ASN A N      1 
ATOM   2071 C CA     . ASN A 1 280 ? 14.325  27.648  -26.492 1.00 36.73  ? 619 ASN A CA     1 
ATOM   2072 C C      . ASN A 1 280 ? 14.515  28.558  -25.287 1.00 31.69  ? 619 ASN A C      1 
ATOM   2073 O O      . ASN A 1 280 ? 14.528  28.069  -24.152 1.00 30.14  ? 619 ASN A O      1 
ATOM   2074 C CB     . ASN A 1 280 ? 15.645  26.966  -26.850 1.00 41.12  ? 619 ASN A CB     1 
ATOM   2075 C CG     . ASN A 1 280 ? 15.447  25.737  -27.713 1.00 42.38  ? 619 ASN A CG     1 
ATOM   2076 O OD1    . ASN A 1 280 ? 14.441  25.038  -27.596 1.00 44.95  ? 619 ASN A OD1    1 
ATOM   2077 N ND2    . ASN A 1 280 ? 16.409  25.465  -28.586 1.00 46.62  ? 619 ASN A ND2    1 
ATOM   2078 N N      . SER A 1 281 ? 14.665  29.866  -25.504 1.00 31.35  ? 620 SER A N      1 
ATOM   2079 C CA     . SER A 1 281 ? 14.741  30.793  -24.381 1.00 30.64  ? 620 SER A CA     1 
ATOM   2080 C C      . SER A 1 281 ? 13.381  30.984  -23.726 1.00 30.05  ? 620 SER A C      1 
ATOM   2081 O O      . SER A 1 281 ? 13.305  31.234  -22.517 1.00 30.80  ? 620 SER A O      1 
ATOM   2082 C CB     . SER A 1 281 ? 15.299  32.138  -24.843 1.00 37.13  ? 620 SER A CB     1 
ATOM   2083 O OG     . SER A 1 281 ? 16.546  31.976  -25.497 1.00 68.47  ? 620 SER A OG     1 
ATOM   2084 N N      . ARG A 1 282 ? 12.304  30.872  -24.500 1.00 28.33  ? 621 ARG A N      1 
ATOM   2085 C CA     . ARG A 1 282 ? 10.971  31.008  -23.942 1.00 24.00  ? 621 ARG A CA     1 
ATOM   2086 C C      . ARG A 1 282 ? 10.730  29.930  -22.887 1.00 25.21  ? 621 ARG A C      1 
ATOM   2087 O O      . ARG A 1 282 ? 11.262  28.820  -22.984 1.00 28.60  ? 621 ARG A O      1 
ATOM   2088 C CB     . ARG A 1 282 ? 9.915   30.902  -25.041 1.00 22.71  ? 621 ARG A CB     1 
ATOM   2089 C CG     . ARG A 1 282 ? 9.999   31.994  -26.087 1.00 23.87  ? 621 ARG A CG     1 
ATOM   2090 C CD     . ARG A 1 282 ? 9.116   31.678  -27.280 1.00 21.80  ? 621 ARG A CD     1 
ATOM   2091 N NE     . ARG A 1 282 ? 9.486   32.473  -28.444 1.00 25.86  ? 621 ARG A NE     1 
ATOM   2092 C CZ     . ARG A 1 282 ? 9.301   32.093  -29.701 1.00 25.80  ? 621 ARG A CZ     1 
ATOM   2093 N NH1    . ARG A 1 282 ? 8.752   30.926  -29.997 1.00 21.52  ? 621 ARG A NH1    1 
ATOM   2094 N NH2    . ARG A 1 282 ? 9.690   32.898  -30.685 1.00 29.41  ? 621 ARG A NH2    1 
ATOM   2095 N N      . PRO A 1 283 ? 9.941   30.232  -21.866 1.00 21.34  ? 622 PRO A N      1 
ATOM   2096 C CA     . PRO A 1 283 ? 9.587   29.213  -20.882 1.00 20.58  ? 622 PRO A CA     1 
ATOM   2097 C C      . PRO A 1 283 ? 8.497   28.296  -21.412 1.00 23.44  ? 622 PRO A C      1 
ATOM   2098 O O      . PRO A 1 283 ? 7.747   28.633  -22.330 1.00 23.59  ? 622 PRO A O      1 
ATOM   2099 C CB     . PRO A 1 283 ? 9.079   30.038  -19.697 1.00 23.66  ? 622 PRO A CB     1 
ATOM   2100 C CG     . PRO A 1 283 ? 8.468   31.237  -20.345 1.00 23.99  ? 622 PRO A CG     1 
ATOM   2101 C CD     . PRO A 1 283 ? 9.326   31.535  -21.557 1.00 25.02  ? 622 PRO A CD     1 
ATOM   2102 N N      . ASN A 1 284 ? 8.428   27.111  -20.816 1.00 22.56  ? 623 ASN A N      1 
ATOM   2103 C CA     . ASN A 1 284 ? 7.292   26.240  -21.060 1.00 22.35  ? 623 ASN A CA     1 
ATOM   2104 C C      . ASN A 1 284 ? 6.051   26.828  -20.401 1.00 24.19  ? 623 ASN A C      1 
ATOM   2105 O O      . ASN A 1 284 ? 6.127   27.483  -19.358 1.00 21.40  ? 623 ASN A O      1 
ATOM   2106 C CB     . ASN A 1 284 ? 7.569   24.838  -20.521 1.00 19.50  ? 623 ASN A CB     1 
ATOM   2107 C CG     . ASN A 1 284 ? 8.736   24.170  -21.216 1.00 25.03  ? 623 ASN A CG     1 
ATOM   2108 O OD1    . ASN A 1 284 ? 8.792   24.116  -22.446 1.00 30.06  ? 623 ASN A OD1    1 
ATOM   2109 N ND2    . ASN A 1 284 ? 9.684   23.668  -20.433 1.00 28.04  ? 623 ASN A ND2    1 
ATOM   2110 N N      . VAL A 1 285 ? 4.895   26.608  -21.031 1.00 23.85  ? 624 VAL A N      1 
ATOM   2111 C CA     . VAL A 1 285 ? 3.660   27.142  -20.467 1.00 18.53  ? 624 VAL A CA     1 
ATOM   2112 C C      . VAL A 1 285 ? 3.466   26.638  -19.044 1.00 20.87  ? 624 VAL A C      1 
ATOM   2113 O O      . VAL A 1 285 ? 2.866   27.325  -18.208 1.00 20.22  ? 624 VAL A O      1 
ATOM   2114 C CB     . VAL A 1 285 ? 2.459   26.790  -21.367 1.00 17.47  ? 624 VAL A CB     1 
ATOM   2115 C CG1    . VAL A 1 285 ? 2.156   25.302  -21.296 1.00 21.12  ? 624 VAL A CG1    1 
ATOM   2116 C CG2    . VAL A 1 285 ? 1.245   27.613  -20.978 1.00 14.47  ? 624 VAL A CG2    1 
ATOM   2117 N N      . SER A 1 286 ? 3.981   25.442  -18.739 1.00 22.68  ? 625 SER A N      1 
ATOM   2118 C CA     . SER A 1 286 ? 3.886   24.914  -17.382 1.00 20.96  ? 625 SER A CA     1 
ATOM   2119 C C      . SER A 1 286 ? 4.544   25.854  -16.379 1.00 23.25  ? 625 SER A C      1 
ATOM   2120 O O      . SER A 1 286 ? 4.060   26.010  -15.251 1.00 22.12  ? 625 SER A O      1 
ATOM   2121 C CB     . SER A 1 286 ? 4.524   23.527  -17.312 1.00 21.47  ? 625 SER A CB     1 
ATOM   2122 O OG     . SER A 1 286 ? 5.927   23.603  -17.499 1.00 24.65  ? 625 SER A OG     1 
ATOM   2123 N N      . GLU A 1 287 ? 5.653   26.486  -16.768 1.00 23.64  ? 626 GLU A N      1 
ATOM   2124 C CA     . GLU A 1 287 ? 6.304   27.442  -15.880 1.00 18.96  ? 626 GLU A CA     1 
ATOM   2125 C C      . GLU A 1 287 ? 5.461   28.700  -15.714 1.00 19.26  ? 626 GLU A C      1 
ATOM   2126 O O      . GLU A 1 287 ? 5.292   29.198  -14.595 1.00 25.49  ? 626 GLU A O      1 
ATOM   2127 C CB     . GLU A 1 287 ? 7.693   27.790  -16.412 1.00 21.76  ? 626 GLU A CB     1 
ATOM   2128 C CG     . GLU A 1 287 ? 8.446   28.809  -15.573 1.00 26.95  ? 626 GLU A CG     1 
ATOM   2129 C CD     . GLU A 1 287 ? 9.854   29.051  -16.081 1.00 31.99  ? 626 GLU A CD     1 
ATOM   2130 O OE1    . GLU A 1 287 ? 10.287  28.321  -17.000 1.00 29.52  ? 626 GLU A OE1    1 
ATOM   2131 O OE2    . GLU A 1 287 ? 10.526  29.969  -15.564 1.00 35.27  ? 626 GLU A OE2    1 
ATOM   2132 N N      . VAL A 1 288 ? 4.923   29.227  -16.816 1.00 18.78  ? 627 VAL A N      1 
ATOM   2133 C CA     . VAL A 1 288 ? 4.050   30.395  -16.733 1.00 21.90  ? 627 VAL A CA     1 
ATOM   2134 C C      . VAL A 1 288 ? 2.831   30.087  -15.872 1.00 20.59  ? 627 VAL A C      1 
ATOM   2135 O O      . VAL A 1 288 ? 2.336   30.950  -15.137 1.00 22.99  ? 627 VAL A O      1 
ATOM   2136 C CB     . VAL A 1 288 ? 3.643   30.861  -18.143 1.00 22.40  ? 627 VAL A CB     1 
ATOM   2137 C CG1    . VAL A 1 288 ? 2.738   32.084  -18.060 1.00 22.52  ? 627 VAL A CG1    1 
ATOM   2138 C CG2    . VAL A 1 288 ? 4.876   31.154  -18.984 1.00 16.98  ? 627 VAL A CG2    1 
ATOM   2139 N N      . PHE A 1 289 ? 2.328   28.852  -15.948 1.00 19.65  ? 628 PHE A N      1 
ATOM   2140 C CA     . PHE A 1 289 ? 1.171   28.476  -15.142 1.00 22.73  ? 628 PHE A CA     1 
ATOM   2141 C C      . PHE A 1 289 ? 1.505   28.490  -13.656 1.00 23.64  ? 628 PHE A C      1 
ATOM   2142 O O      . PHE A 1 289 ? 0.664   28.864  -12.829 1.00 23.38  ? 628 PHE A O      1 
ATOM   2143 C CB     . PHE A 1 289 ? 0.661   27.099  -15.570 1.00 21.79  ? 628 PHE A CB     1 
ATOM   2144 C CG     . PHE A 1 289 ? -0.607  26.678  -14.881 1.00 18.78  ? 628 PHE A CG     1 
ATOM   2145 C CD1    . PHE A 1 289 ? -1.750  27.454  -14.971 1.00 18.93  ? 628 PHE A CD1    1 
ATOM   2146 C CD2    . PHE A 1 289 ? -0.660  25.499  -14.162 1.00 21.47  ? 628 PHE A CD2    1 
ATOM   2147 C CE1    . PHE A 1 289 ? -2.920  27.066  -14.343 1.00 19.24  ? 628 PHE A CE1    1 
ATOM   2148 C CE2    . PHE A 1 289 ? -1.827  25.104  -13.534 1.00 24.33  ? 628 PHE A CE2    1 
ATOM   2149 C CZ     . PHE A 1 289 ? -2.958  25.890  -13.625 1.00 23.22  ? 628 PHE A CZ     1 
ATOM   2150 N N      . MET A 1 290 ? 2.727   28.087  -13.294 1.00 21.77  ? 629 MET A N      1 
ATOM   2151 C CA     . MET A 1 290 ? 3.135   28.147  -11.895 1.00 19.19  ? 629 MET A CA     1 
ATOM   2152 C C      . MET A 1 290 ? 3.345   29.584  -11.439 1.00 21.25  ? 629 MET A C      1 
ATOM   2153 O O      . MET A 1 290 ? 3.079   29.912  -10.278 1.00 22.31  ? 629 MET A O      1 
ATOM   2154 C CB     . MET A 1 290 ? 4.408   27.327  -11.683 1.00 22.16  ? 629 MET A CB     1 
ATOM   2155 C CG     . MET A 1 290 ? 5.007   27.438  -10.283 1.00 22.35  ? 629 MET A CG     1 
ATOM   2156 S SD     . MET A 1 290 ? 6.119   28.847  -10.081 1.00 27.67  ? 629 MET A SD     1 
ATOM   2157 C CE     . MET A 1 290 ? 7.362   28.481  -11.319 1.00 25.18  ? 629 MET A CE     1 
ATOM   2158 N N      . ILE A 1 291 ? 3.814   30.453  -12.334 1.00 24.60  ? 630 ILE A N      1 
ATOM   2159 C CA     . ILE A 1 291 ? 4.008   31.853  -11.972 1.00 23.83  ? 630 ILE A CA     1 
ATOM   2160 C C      . ILE A 1 291 ? 2.665   32.527  -11.717 1.00 25.24  ? 630 ILE A C      1 
ATOM   2161 O O      . ILE A 1 291 ? 2.461   33.172  -10.683 1.00 26.22  ? 630 ILE A O      1 
ATOM   2162 C CB     . ILE A 1 291 ? 4.806   32.586  -13.065 1.00 22.28  ? 630 ILE A CB     1 
ATOM   2163 C CG1    . ILE A 1 291 ? 6.205   31.982  -13.198 1.00 22.63  ? 630 ILE A CG1    1 
ATOM   2164 C CG2    . ILE A 1 291 ? 4.884   34.073  -12.762 1.00 21.68  ? 630 ILE A CG2    1 
ATOM   2165 C CD1    . ILE A 1 291 ? 6.975   31.936  -11.898 1.00 23.48  ? 630 ILE A CD1    1 
ATOM   2166 N N      . LEU A 1 292 ? 1.728   32.385  -12.658 1.00 23.41  ? 631 LEU A N      1 
ATOM   2167 C CA     . LEU A 1 292 ? 0.436   33.048  -12.516 1.00 22.73  ? 631 LEU A CA     1 
ATOM   2168 C C      . LEU A 1 292 ? -0.334  32.539  -11.304 1.00 24.19  ? 631 LEU A C      1 
ATOM   2169 O O      . LEU A 1 292 ? -1.126  33.285  -10.717 1.00 24.30  ? 631 LEU A O      1 
ATOM   2170 C CB     . LEU A 1 292 ? -0.390  32.863  -13.790 1.00 20.07  ? 631 LEU A CB     1 
ATOM   2171 C CG     . LEU A 1 292 ? 0.130   33.594  -15.028 1.00 19.46  ? 631 LEU A CG     1 
ATOM   2172 C CD1    . LEU A 1 292 ? -0.738  33.293  -16.239 1.00 20.73  ? 631 LEU A CD1    1 
ATOM   2173 C CD2    . LEU A 1 292 ? 0.188   35.090  -14.769 1.00 18.05  ? 631 LEU A CD2    1 
ATOM   2174 N N      . SER A 1 293 ? -0.116  31.282  -10.911 1.00 26.00  ? 632 SER A N      1 
ATOM   2175 C CA     . SER A 1 293 ? -0.857  30.726  -9.783  1.00 23.56  ? 632 SER A CA     1 
ATOM   2176 C C      . SER A 1 293 ? -0.366  31.277  -8.450  1.00 25.90  ? 632 SER A C      1 
ATOM   2177 O O      . SER A 1 293 ? -1.149  31.377  -7.498  1.00 28.32  ? 632 SER A O      1 
ATOM   2178 C CB     . SER A 1 293 ? -0.763  29.200  -9.788  1.00 20.04  ? 632 SER A CB     1 
ATOM   2179 O OG     . SER A 1 293 ? -1.564  28.641  -10.814 1.00 23.76  ? 632 SER A OG     1 
ATOM   2180 N N      . LYS A 1 294 ? 0.914   31.637  -8.357  1.00 26.11  ? 633 LYS A N      1 
ATOM   2181 C CA     . LYS A 1 294 ? 1.451   32.104  -7.084  1.00 28.12  ? 633 LYS A CA     1 
ATOM   2182 C C      . LYS A 1 294 ? 1.128   33.574  -6.840  1.00 29.87  ? 633 LYS A C      1 
ATOM   2183 O O      . LYS A 1 294 ? 0.890   33.974  -5.696  1.00 35.06  ? 633 LYS A O      1 
ATOM   2184 C CB     . LYS A 1 294 ? 2.960   31.866  -7.029  1.00 29.82  ? 633 LYS A CB     1 
ATOM   2185 C CG     . LYS A 1 294 ? 3.343   30.397  -7.042  1.00 25.70  ? 633 LYS A CG     1 
ATOM   2186 C CD     . LYS A 1 294 ? 4.806   30.202  -6.696  1.00 30.08  ? 633 LYS A CD     1 
ATOM   2187 C CE     . LYS A 1 294 ? 5.127   28.729  -6.517  1.00 31.26  ? 633 LYS A CE     1 
ATOM   2188 N NZ     . LYS A 1 294 ? 4.260   28.099  -5.484  1.00 32.62  ? 633 LYS A NZ     1 
ATOM   2189 N N      . ILE A 1 295 ? 1.117   34.394  -7.897  1.00 27.41  ? 634 ILE A N      1 
ATOM   2190 C CA     . ILE A 1 295 ? 0.715   35.792  -7.750  1.00 30.93  ? 634 ILE A CA     1 
ATOM   2191 C C      . ILE A 1 295 ? -0.793  35.962  -7.739  1.00 34.39  ? 634 ILE A C      1 
ATOM   2192 O O      . ILE A 1 295 ? -1.278  37.095  -7.617  1.00 39.08  ? 634 ILE A O      1 
ATOM   2193 C CB     . ILE A 1 295 ? 1.311   36.678  -8.864  1.00 27.77  ? 634 ILE A CB     1 
ATOM   2194 C CG1    . ILE A 1 295 ? 0.697   36.333  -10.222 1.00 23.60  ? 634 ILE A CG1    1 
ATOM   2195 C CG2    . ILE A 1 295 ? 2.824   36.533  -8.907  1.00 36.96  ? 634 ILE A CG2    1 
ATOM   2196 C CD1    . ILE A 1 295 ? 1.315   37.096  -11.378 1.00 24.47  ? 634 ILE A CD1    1 
ATOM   2197 N N      . GLN A 1 296 ? -1.550  34.876  -7.859  1.00 34.42  ? 635 GLN A N      1 
ATOM   2198 C CA     . GLN A 1 296 ? -2.999  34.958  -7.823  1.00 37.56  ? 635 GLN A CA     1 
ATOM   2199 C C      . GLN A 1 296 ? -3.493  35.013  -6.379  1.00 54.38  ? 635 GLN A C      1 
ATOM   2200 O O      . GLN A 1 296 ? -2.791  34.636  -5.436  1.00 54.42  ? 635 GLN A O      1 
ATOM   2201 C CB     . GLN A 1 296 ? -3.626  33.770  -8.555  1.00 34.68  ? 635 GLN A CB     1 
ATOM   2202 C CG     . GLN A 1 296 ? -5.117  33.918  -8.814  1.00 39.50  ? 635 GLN A CG     1 
ATOM   2203 C CD     . GLN A 1 296 ? -5.671  32.810  -9.688  1.00 40.46  ? 635 GLN A CD     1 
ATOM   2204 O OE1    . GLN A 1 296 ? -5.145  31.697  -9.710  1.00 34.95  ? 635 GLN A OE1    1 
ATOM   2205 N NE2    . GLN A 1 296 ? -6.738  33.114  -10.422 1.00 37.91  ? 635 GLN A NE2    1 
ATOM   2206 N N      . SER A 1 297 ? -4.721  35.498  -6.219  1.00 81.28  ? 636 SER A N      1 
ATOM   2207 C CA     . SER A 1 297 ? -5.318  35.699  -4.902  1.00 73.31  ? 636 SER A CA     1 
ATOM   2208 C C      . SER A 1 297 ? -5.195  34.463  -4.017  1.00 79.56  ? 636 SER A C      1 
ATOM   2209 O O      . SER A 1 297 ? -5.391  34.537  -2.804  1.00 68.31  ? 636 SER A O      1 
ATOM   2210 C CB     . SER A 1 297 ? -6.791  36.089  -5.045  1.00 74.21  ? 636 SER A CB     1 
ATOM   2211 O OG     . SER A 1 297 ? -7.516  35.090  -5.740  1.00 94.04  ? 636 SER A OG     1 
ATOM   2212 N N      . SER B 1 1   ? -23.509 26.373  -7.177  1.00 64.26  ? 340 SER B N      1 
ATOM   2213 C CA     . SER B 1 1   ? -23.141 25.621  -8.369  1.00 68.61  ? 340 SER B CA     1 
ATOM   2214 C C      . SER B 1 1   ? -23.939 24.327  -8.473  1.00 74.33  ? 340 SER B C      1 
ATOM   2215 O O      . SER B 1 1   ? -24.450 23.981  -9.540  1.00 77.35  ? 340 SER B O      1 
ATOM   2216 C CB     . SER B 1 1   ? -21.643 25.315  -8.363  1.00 64.66  ? 340 SER B CB     1 
ATOM   2217 O OG     . SER B 1 1   ? -21.290 24.503  -7.256  1.00 78.41  ? 340 SER B OG     1 
ATOM   2218 N N      . LEU B 1 2   ? -24.039 23.614  -7.355  1.00 62.67  ? 341 LEU B N      1 
ATOM   2219 C CA     . LEU B 1 2   ? -24.739 22.341  -7.309  1.00 53.88  ? 341 LEU B CA     1 
ATOM   2220 C C      . LEU B 1 2   ? -26.241 22.567  -7.145  1.00 56.86  ? 341 LEU B C      1 
ATOM   2221 O O      . LEU B 1 2   ? -26.727 23.699  -7.077  1.00 60.33  ? 341 LEU B O      1 
ATOM   2222 C CB     . LEU B 1 2   ? -24.186 21.480  -6.177  1.00 47.49  ? 341 LEU B CB     1 
ATOM   2223 C CG     . LEU B 1 2   ? -22.662 21.369  -6.127  1.00 48.51  ? 341 LEU B CG     1 
ATOM   2224 C CD1    . LEU B 1 2   ? -22.189 21.147  -4.700  1.00 48.18  ? 341 LEU B CD1    1 
ATOM   2225 C CD2    . LEU B 1 2   ? -22.169 20.255  -7.038  1.00 48.97  ? 341 LEU B CD2    1 
ATOM   2226 N N      . THR B 1 3   ? -26.989 21.468  -7.085  1.00 48.85  ? 342 THR B N      1 
ATOM   2227 C CA     . THR B 1 3   ? -28.429 21.507  -6.875  1.00 46.65  ? 342 THR B CA     1 
ATOM   2228 C C      . THR B 1 3   ? -28.717 21.297  -5.395  1.00 44.69  ? 342 THR B C      1 
ATOM   2229 O O      . THR B 1 3   ? -28.384 20.245  -4.837  1.00 43.54  ? 342 THR B O      1 
ATOM   2230 C CB     . THR B 1 3   ? -29.142 20.442  -7.708  1.00 46.56  ? 342 THR B CB     1 
ATOM   2231 O OG1    . THR B 1 3   ? -28.661 20.479  -9.058  1.00 51.68  ? 342 THR B OG1    1 
ATOM   2232 C CG2    . THR B 1 3   ? -30.643 20.686  -7.705  1.00 46.85  ? 342 THR B CG2    1 
ATOM   2233 N N      . VAL B 1 4   ? -29.326 22.295  -4.763  1.00 45.09  ? 343 VAL B N      1 
ATOM   2234 C CA     . VAL B 1 4   ? -29.738 22.185  -3.367  1.00 43.86  ? 343 VAL B CA     1 
ATOM   2235 C C      . VAL B 1 4   ? -31.047 21.403  -3.328  1.00 42.69  ? 343 VAL B C      1 
ATOM   2236 O O      . VAL B 1 4   ? -32.083 21.884  -3.793  1.00 43.90  ? 343 VAL B O      1 
ATOM   2237 C CB     . VAL B 1 4   ? -29.888 23.562  -2.711  1.00 47.73  ? 343 VAL B CB     1 
ATOM   2238 C CG1    . VAL B 1 4   ? -28.533 24.243  -2.593  1.00 49.30  ? 343 VAL B CG1    1 
ATOM   2239 C CG2    . VAL B 1 4   ? -30.855 24.432  -3.506  1.00 49.28  ? 343 VAL B CG2    1 
ATOM   2240 N N      . TYR B 1 5   ? -30.999 20.191  -2.786  1.00 40.88  ? 344 TYR B N      1 
ATOM   2241 C CA     . TYR B 1 5   ? -32.177 19.346  -2.678  1.00 39.95  ? 344 TYR B CA     1 
ATOM   2242 C C      . TYR B 1 5   ? -32.878 19.579  -1.347  1.00 39.25  ? 344 TYR B C      1 
ATOM   2243 O O      . TYR B 1 5   ? -32.244 19.873  -0.331  1.00 38.87  ? 344 TYR B O      1 
ATOM   2244 C CB     . TYR B 1 5   ? -31.806 17.868  -2.810  1.00 38.62  ? 344 TYR B CB     1 
ATOM   2245 C CG     . TYR B 1 5   ? -31.416 17.438  -4.207  1.00 39.55  ? 344 TYR B CG     1 
ATOM   2246 C CD1    . TYR B 1 5   ? -30.101 17.536  -4.644  1.00 40.66  ? 344 TYR B CD1    1 
ATOM   2247 C CD2    . TYR B 1 5   ? -32.361 16.924  -5.085  1.00 40.09  ? 344 TYR B CD2    1 
ATOM   2248 C CE1    . TYR B 1 5   ? -29.741 17.140  -5.919  1.00 41.66  ? 344 TYR B CE1    1 
ATOM   2249 C CE2    . TYR B 1 5   ? -32.010 16.525  -6.361  1.00 41.29  ? 344 TYR B CE2    1 
ATOM   2250 C CZ     . TYR B 1 5   ? -30.700 16.635  -6.773  1.00 41.90  ? 344 TYR B CZ     1 
ATOM   2251 O OH     . TYR B 1 5   ? -30.346 16.239  -8.043  1.00 43.38  ? 344 TYR B OH     1 
ATOM   2252 N N      . LYS B 1 6   ? -34.201 19.440  -1.363  1.00 42.95  ? 345 LYS B N      1 
ATOM   2253 C CA     . LYS B 1 6   ? -34.995 19.526  -0.148  1.00 45.43  ? 345 LYS B CA     1 
ATOM   2254 C C      . LYS B 1 6   ? -35.196 18.135  0.438   1.00 43.13  ? 345 LYS B C      1 
ATOM   2255 O O      . LYS B 1 6   ? -35.454 17.171  -0.290  1.00 41.97  ? 345 LYS B O      1 
ATOM   2256 C CB     . LYS B 1 6   ? -36.344 20.194  -0.423  1.00 46.87  ? 345 LYS B CB     1 
ATOM   2257 C CG     . LYS B 1 6   ? -36.227 21.678  -0.742  1.00 49.62  ? 345 LYS B CG     1 
ATOM   2258 C CD     . LYS B 1 6   ? -37.564 22.395  -0.650  1.00 56.74  ? 345 LYS B CD     1 
ATOM   2259 C CE     . LYS B 1 6   ? -38.479 22.033  -1.807  1.00 55.14  ? 345 LYS B CE     1 
ATOM   2260 N NZ     . LYS B 1 6   ? -39.705 22.880  -1.819  1.00 55.73  ? 345 LYS B NZ     1 
ATOM   2261 N N      . TYR B 1 7   ? -35.070 18.040  1.764   1.00 41.31  ? 346 TYR B N      1 
ATOM   2262 C CA     . TYR B 1 7   ? -35.079 16.743  2.433   1.00 42.22  ? 346 TYR B CA     1 
ATOM   2263 C C      . TYR B 1 7   ? -36.337 15.936  2.138   1.00 43.25  ? 346 TYR B C      1 
ATOM   2264 O O      . TYR B 1 7   ? -36.311 14.706  2.258   1.00 45.34  ? 346 TYR B O      1 
ATOM   2265 C CB     . TYR B 1 7   ? -34.918 16.938  3.942   1.00 41.33  ? 346 TYR B CB     1 
ATOM   2266 C CG     . TYR B 1 7   ? -34.903 15.651  4.731   1.00 41.09  ? 346 TYR B CG     1 
ATOM   2267 C CD1    . TYR B 1 7   ? -33.818 14.785  4.664   1.00 40.30  ? 346 TYR B CD1    1 
ATOM   2268 C CD2    . TYR B 1 7   ? -35.970 15.303  5.548   1.00 42.47  ? 346 TYR B CD2    1 
ATOM   2269 C CE1    . TYR B 1 7   ? -33.798 13.607  5.387   1.00 39.61  ? 346 TYR B CE1    1 
ATOM   2270 C CE2    . TYR B 1 7   ? -35.959 14.128  6.275   1.00 44.68  ? 346 TYR B CE2    1 
ATOM   2271 C CZ     . TYR B 1 7   ? -34.872 13.283  6.191   1.00 44.20  ? 346 TYR B CZ     1 
ATOM   2272 O OH     . TYR B 1 7   ? -34.861 12.111  6.914   1.00 37.46  ? 346 TYR B OH     1 
ATOM   2273 N N      . GLU B 1 8   ? -37.436 16.591  1.758   1.00 40.34  ? 347 GLU B N      1 
ATOM   2274 C CA     . GLU B 1 8   ? -38.643 15.850  1.407   1.00 37.85  ? 347 GLU B CA     1 
ATOM   2275 C C      . GLU B 1 8   ? -38.417 14.987  0.172   1.00 40.33  ? 347 GLU B C      1 
ATOM   2276 O O      . GLU B 1 8   ? -38.938 13.868  0.081   1.00 41.79  ? 347 GLU B O      1 
ATOM   2277 C CB     . GLU B 1 8   ? -39.805 16.815  1.176   1.00 44.45  ? 347 GLU B CB     1 
ATOM   2278 C CG     . GLU B 1 8   ? -40.210 17.612  2.403   1.00 51.23  ? 347 GLU B CG     1 
ATOM   2279 C CD     . GLU B 1 8   ? -41.371 18.545  2.125   1.00 56.84  ? 347 GLU B CD     1 
ATOM   2280 O OE1    . GLU B 1 8   ? -41.880 18.537  0.984   1.00 55.71  ? 347 GLU B OE1    1 
ATOM   2281 O OE2    . GLU B 1 8   ? -41.774 19.287  3.045   1.00 67.07  ? 347 GLU B OE2    1 
ATOM   2282 N N      . ASP B 1 9   ? -37.641 15.490  -0.789  1.00 42.04  ? 348 ASP B N      1 
ATOM   2283 C CA     . ASP B 1 9   ? -37.402 14.740  -2.017  1.00 37.43  ? 348 ASP B CA     1 
ATOM   2284 C C      . ASP B 1 9   ? -36.463 13.565  -1.774  1.00 36.46  ? 348 ASP B C      1 
ATOM   2285 O O      . ASP B 1 9   ? -36.634 12.494  -2.369  1.00 40.49  ? 348 ASP B O      1 
ATOM   2286 C CB     . ASP B 1 9   ? -36.843 15.671  -3.091  1.00 41.69  ? 348 ASP B CB     1 
ATOM   2287 C CG     . ASP B 1 9   ? -37.725 16.884  -3.324  1.00 48.42  ? 348 ASP B CG     1 
ATOM   2288 O OD1    . ASP B 1 9   ? -38.958 16.711  -3.443  1.00 46.23  ? 348 ASP B OD1    1 
ATOM   2289 O OD2    . ASP B 1 9   ? -37.188 18.012  -3.375  1.00 53.19  ? 348 ASP B OD2    1 
ATOM   2290 N N      . LEU B 1 10  ? -35.464 13.744  -0.906  1.00 36.79  ? 349 LEU B N      1 
ATOM   2291 C CA     . LEU B 1 10  ? -34.587 12.631  -0.557  1.00 35.16  ? 349 LEU B CA     1 
ATOM   2292 C C      . LEU B 1 10  ? -35.361 11.534  0.161   1.00 38.27  ? 349 LEU B C      1 
ATOM   2293 O O      . LEU B 1 10  ? -35.178 10.344  -0.124  1.00 35.22  ? 349 LEU B O      1 
ATOM   2294 C CB     . LEU B 1 10  ? -33.428 13.126  0.308   1.00 36.06  ? 349 LEU B CB     1 
ATOM   2295 C CG     . LEU B 1 10  ? -32.637 14.323  -0.227  1.00 43.79  ? 349 LEU B CG     1 
ATOM   2296 C CD1    . LEU B 1 10  ? -31.526 14.708  0.739   1.00 40.64  ? 349 LEU B CD1    1 
ATOM   2297 C CD2    . LEU B 1 10  ? -32.074 14.031  -1.610  1.00 34.82  ? 349 LEU B CD2    1 
ATOM   2298 N N      . GLN B 1 11  ? -36.235 11.916  1.096   1.00 38.81  ? 350 GLN B N      1 
ATOM   2299 C CA     . GLN B 1 11  ? -37.083 10.937  1.769   1.00 35.85  ? 350 GLN B CA     1 
ATOM   2300 C C      . GLN B 1 11  ? -37.906 10.141  0.763   1.00 34.00  ? 350 GLN B C      1 
ATOM   2301 O O      . GLN B 1 11  ? -37.953 8.907   0.818   1.00 33.87  ? 350 GLN B O      1 
ATOM   2302 C CB     . GLN B 1 11  ? -38.001 11.639  2.771   1.00 35.36  ? 350 GLN B CB     1 
ATOM   2303 C CG     . GLN B 1 11  ? -37.423 11.796  4.166   1.00 38.46  ? 350 GLN B CG     1 
ATOM   2304 C CD     . GLN B 1 11  ? -38.416 12.416  5.132   1.00 41.12  ? 350 GLN B CD     1 
ATOM   2305 O OE1    . GLN B 1 11  ? -39.179 13.311  4.766   1.00 37.11  ? 350 GLN B OE1    1 
ATOM   2306 N NE2    . GLN B 1 11  ? -38.416 11.937  6.371   1.00 41.81  ? 350 GLN B NE2    1 
ATOM   2307 N N      . ASN B 1 12  ? -38.565 10.836  -0.167  1.00 32.71  ? 351 ASN B N      1 
ATOM   2308 C CA     . ASN B 1 12  ? -39.470 10.161  -1.091  1.00 34.09  ? 351 ASN B CA     1 
ATOM   2309 C C      . ASN B 1 12  ? -38.719 9.351   -2.139  1.00 35.52  ? 351 ASN B C      1 
ATOM   2310 O O      . ASN B 1 12  ? -39.239 8.341   -2.626  1.00 40.09  ? 351 ASN B O      1 
ATOM   2311 C CB     . ASN B 1 12  ? -40.387 11.182  -1.763  1.00 37.07  ? 351 ASN B CB     1 
ATOM   2312 C CG     . ASN B 1 12  ? -41.241 11.946  -0.765  1.00 36.83  ? 351 ASN B CG     1 
ATOM   2313 O OD1    . ASN B 1 12  ? -41.465 11.488  0.356   1.00 34.44  ? 351 ASN B OD1    1 
ATOM   2314 N ND2    . ASN B 1 12  ? -41.726 13.113  -1.172  1.00 37.32  ? 351 ASN B ND2    1 
ATOM   2315 N N      . ALA B 1 13  ? -37.501 9.766   -2.495  1.00 36.69  ? 352 ALA B N      1 
ATOM   2316 C CA     . ALA B 1 13  ? -36.746 9.057   -3.522  1.00 39.00  ? 352 ALA B CA     1 
ATOM   2317 C C      . ALA B 1 13  ? -36.065 7.807   -2.981  1.00 40.20  ? 352 ALA B C      1 
ATOM   2318 O O      . ALA B 1 13  ? -35.807 6.870   -3.745  1.00 45.75  ? 352 ALA B O      1 
ATOM   2319 C CB     . ALA B 1 13  ? -35.709 9.989   -4.150  1.00 42.95  ? 352 ALA B CB     1 
ATOM   2320 N N      . THR B 1 14  ? -35.766 7.768   -1.682  1.00 36.66  ? 353 THR B N      1 
ATOM   2321 C CA     . THR B 1 14  ? -35.144 6.606   -1.059  1.00 40.55  ? 353 THR B CA     1 
ATOM   2322 C C      . THR B 1 14  ? -36.126 5.822   -0.195  1.00 41.69  ? 353 THR B C      1 
ATOM   2323 O O      . THR B 1 14  ? -35.701 5.030   0.653   1.00 47.04  ? 353 THR B O      1 
ATOM   2324 C CB     . THR B 1 14  ? -33.932 7.028   -0.226  1.00 37.79  ? 353 THR B CB     1 
ATOM   2325 O OG1    . THR B 1 14  ? -34.366 7.812   0.893   1.00 37.29  ? 353 THR B OG1    1 
ATOM   2326 C CG2    . THR B 1 14  ? -32.967 7.849   -1.065  1.00 32.12  ? 353 THR B CG2    1 
ATOM   2327 N N      . ASN B 1 15  ? -37.428 6.021   -0.395  1.00 38.33  ? 354 ASN B N      1 
ATOM   2328 C CA     . ASN B 1 15  ? -38.451 5.369   0.419   1.00 39.24  ? 354 ASN B CA     1 
ATOM   2329 C C      . ASN B 1 15  ? -38.172 5.582   1.905   1.00 39.84  ? 354 ASN B C      1 
ATOM   2330 O O      . ASN B 1 15  ? -38.150 4.645   2.705   1.00 45.89  ? 354 ASN B O      1 
ATOM   2331 C CB     . ASN B 1 15  ? -38.551 3.880   0.084   1.00 45.34  ? 354 ASN B CB     1 
ATOM   2332 C CG     . ASN B 1 15  ? -39.317 3.622   -1.197  1.00 51.81  ? 354 ASN B CG     1 
ATOM   2333 O OD1    . ASN B 1 15  ? -38.868 3.982   -2.285  1.00 47.17  ? 354 ASN B OD1    1 
ATOM   2334 N ND2    . ASN B 1 15  ? -40.478 2.987   -1.074  1.00 52.35  ? 354 ASN B ND2    1 
ATOM   2335 N N      . PHE B 1 16  ? -37.940 6.843   2.268   1.00 36.06  ? 355 PHE B N      1 
ATOM   2336 C CA     . PHE B 1 16  ? -37.641 7.216   3.651   1.00 34.70  ? 355 PHE B CA     1 
ATOM   2337 C C      . PHE B 1 16  ? -36.438 6.445   4.186   1.00 36.51  ? 355 PHE B C      1 
ATOM   2338 O O      . PHE B 1 16  ? -36.342 6.154   5.382   1.00 46.22  ? 355 PHE B O      1 
ATOM   2339 C CB     . PHE B 1 16  ? -38.866 7.025   4.547   1.00 35.57  ? 355 PHE B CB     1 
ATOM   2340 C CG     . PHE B 1 16  ? -39.992 7.973   4.239   1.00 35.74  ? 355 PHE B CG     1 
ATOM   2341 C CD1    . PHE B 1 16  ? -40.839 7.739   3.167   1.00 31.56  ? 355 PHE B CD1    1 
ATOM   2342 C CD2    . PHE B 1 16  ? -40.202 9.100   5.020   1.00 34.65  ? 355 PHE B CD2    1 
ATOM   2343 C CE1    . PHE B 1 16  ? -41.872 8.611   2.878   1.00 31.31  ? 355 PHE B CE1    1 
ATOM   2344 C CE2    . PHE B 1 16  ? -41.235 9.975   4.736   1.00 31.04  ? 355 PHE B CE2    1 
ATOM   2345 C CZ     . PHE B 1 16  ? -42.071 9.730   3.663   1.00 31.73  ? 355 PHE B CZ     1 
ATOM   2346 N N      . PHE B 1 17  ? -35.510 6.109   3.290   1.00 36.36  ? 356 PHE B N      1 
ATOM   2347 C CA     . PHE B 1 17  ? -34.201 5.578   3.668   1.00 41.38  ? 356 PHE B CA     1 
ATOM   2348 C C      . PHE B 1 17  ? -34.305 4.173   4.267   1.00 44.60  ? 356 PHE B C      1 
ATOM   2349 O O      . PHE B 1 17  ? -33.769 3.897   5.340   1.00 48.27  ? 356 PHE B O      1 
ATOM   2350 C CB     . PHE B 1 17  ? -33.489 6.525   4.640   1.00 41.02  ? 356 PHE B CB     1 
ATOM   2351 C CG     . PHE B 1 17  ? -33.177 7.873   4.060   1.00 34.21  ? 356 PHE B CG     1 
ATOM   2352 C CD1    . PHE B 1 17  ? -32.156 8.025   3.138   1.00 35.43  ? 356 PHE B CD1    1 
ATOM   2353 C CD2    . PHE B 1 17  ? -33.893 8.991   4.449   1.00 32.32  ? 356 PHE B CD2    1 
ATOM   2354 C CE1    . PHE B 1 17  ? -31.864 9.265   2.605   1.00 34.49  ? 356 PHE B CE1    1 
ATOM   2355 C CE2    . PHE B 1 17  ? -33.606 10.233  3.921   1.00 32.32  ? 356 PHE B CE2    1 
ATOM   2356 C CZ     . PHE B 1 17  ? -32.590 10.371  2.998   1.00 31.31  ? 356 PHE B CZ     1 
ATOM   2357 N N      . SER B 1 18  ? -34.984 3.276   3.554   1.00 47.62  ? 357 SER B N      1 
ATOM   2358 C CA     . SER B 1 18  ? -35.126 1.896   4.006   1.00 46.43  ? 357 SER B CA     1 
ATOM   2359 C C      . SER B 1 18  ? -35.257 0.988   2.794   1.00 50.87  ? 357 SER B C      1 
ATOM   2360 O O      . SER B 1 18  ? -36.110 1.219   1.934   1.00 57.75  ? 357 SER B O      1 
ATOM   2361 C CB     . SER B 1 18  ? -36.348 1.724   4.919   1.00 65.49  ? 357 SER B CB     1 
ATOM   2362 O OG     . SER B 1 18  ? -36.663 2.924   5.603   1.00 65.09  ? 357 SER B OG     1 
ATOM   2363 N N      . GLU B 1 19  ? -34.419 -0.044  2.738   1.00 50.48  ? 358 GLU B N      1 
ATOM   2364 C CA     . GLU B 1 19  ? -34.465 -1.041  1.673   1.00 43.82  ? 358 GLU B CA     1 
ATOM   2365 C C      . GLU B 1 19  ? -33.911 -0.494  0.366   1.00 46.76  ? 358 GLU B C      1 
ATOM   2366 O O      . GLU B 1 19  ? -33.415 -1.269  -0.454  1.00 51.13  ? 358 GLU B O      1 
ATOM   2367 C CB     . GLU B 1 19  ? -35.882 -1.575  1.455   1.00 51.17  ? 358 GLU B CB     1 
ATOM   2368 C CG     . GLU B 1 19  ? -36.386 -2.430  2.606   1.00 59.40  ? 358 GLU B CG     1 
ATOM   2369 C CD     . GLU B 1 19  ? -37.808 -2.889  2.408   1.00 62.40  ? 358 GLU B CD     1 
ATOM   2370 O OE1    . GLU B 1 19  ? -38.259 -2.939  1.247   1.00 60.32  ? 358 GLU B OE1    1 
ATOM   2371 O OE2    . GLU B 1 19  ? -38.480 -3.187  3.414   1.00 73.92  ? 358 GLU B OE2    1 
ATOM   2372 N N      . GLU B 1 20  ? -33.995 0.820   0.152   1.00 51.06  ? 359 GLU B N      1 
ATOM   2373 C CA     . GLU B 1 20  ? -33.215 1.483   -0.883  1.00 43.07  ? 359 GLU B CA     1 
ATOM   2374 C C      . GLU B 1 20  ? -31.749 1.597   -0.494  1.00 43.28  ? 359 GLU B C      1 
ATOM   2375 O O      . GLU B 1 20  ? -30.974 2.242   -1.206  1.00 42.88  ? 359 GLU B O      1 
ATOM   2376 C CB     . GLU B 1 20  ? -33.788 2.874   -1.164  1.00 43.29  ? 359 GLU B CB     1 
ATOM   2377 C CG     . GLU B 1 20  ? -35.250 2.862   -1.570  1.00 42.42  ? 359 GLU B CG     1 
ATOM   2378 C CD     . GLU B 1 20  ? -35.455 3.223   -3.026  1.00 52.87  ? 359 GLU B CD     1 
ATOM   2379 O OE1    . GLU B 1 20  ? -34.720 2.695   -3.888  1.00 58.38  ? 359 GLU B OE1    1 
ATOM   2380 O OE2    . GLU B 1 20  ? -36.352 4.041   -3.309  1.00 55.32  ? 359 GLU B OE2    1 
ATOM   2381 N N      . ASN B 1 21  ? -31.367 0.995   0.631   1.00 50.42  ? 360 ASN B N      1 
ATOM   2382 C CA     . ASN B 1 21  ? -30.003 1.085   1.130   1.00 48.75  ? 360 ASN B CA     1 
ATOM   2383 C C      . ASN B 1 21  ? -29.052 0.280   0.251   1.00 50.18  ? 360 ASN B C      1 
ATOM   2384 O O      . ASN B 1 21  ? -29.331 -0.874  -0.090  1.00 51.44  ? 360 ASN B O      1 
ATOM   2385 C CB     . ASN B 1 21  ? -29.951 0.575   2.571   1.00 50.25  ? 360 ASN B CB     1 
ATOM   2386 C CG     . ASN B 1 21  ? -28.664 0.943   3.279   1.00 62.53  ? 360 ASN B CG     1 
ATOM   2387 O OD1    . ASN B 1 21  ? -28.029 1.945   2.956   1.00 68.57  ? 360 ASN B OD1    1 
ATOM   2388 N ND2    . ASN B 1 21  ? -28.281 0.140   4.267   1.00 63.05  ? 360 ASN B ND2    1 
ATOM   2389 N N      . LYS B 1 22  ? -27.932 0.892   -0.118  1.00 50.13  ? 361 LYS B N      1 
ATOM   2390 C CA     . LYS B 1 22  ? -26.836 0.176   -0.747  1.00 51.69  ? 361 LYS B CA     1 
ATOM   2391 C C      . LYS B 1 22  ? -25.925 -0.406  0.331   1.00 56.95  ? 361 LYS B C      1 
ATOM   2392 O O      . LYS B 1 22  ? -26.040 -0.087  1.516   1.00 58.45  ? 361 LYS B O      1 
ATOM   2393 C CB     . LYS B 1 22  ? -26.053 1.101   -1.682  1.00 53.83  ? 361 LYS B CB     1 
ATOM   2394 C CG     . LYS B 1 22  ? -26.918 1.871   -2.682  1.00 47.95  ? 361 LYS B CG     1 
ATOM   2395 C CD     . LYS B 1 22  ? -27.070 1.135   -4.013  1.00 51.79  ? 361 LYS B CD     1 
ATOM   2396 C CE     . LYS B 1 22  ? -28.131 0.044   -3.958  1.00 52.57  ? 361 LYS B CE     1 
ATOM   2397 N NZ     . LYS B 1 22  ? -28.602 -0.323  -5.328  1.00 50.61  ? 361 LYS B NZ     1 
ATOM   2398 N N      . ILE B 1 23  ? -25.002 -1.269  -0.098  1.00 61.51  ? 362 ILE B N      1 
ATOM   2399 C CA     . ILE B 1 23  ? -24.127 -1.964  0.844   1.00 73.87  ? 362 ILE B CA     1 
ATOM   2400 C C      . ILE B 1 23  ? -23.505 -0.998  1.839   1.00 74.39  ? 362 ILE B C      1 
ATOM   2401 O O      . ILE B 1 23  ? -23.215 -1.373  2.983   1.00 89.78  ? 362 ILE B O      1 
ATOM   2402 C CB     . ILE B 1 23  ? -23.048 -2.760  0.085   1.00 82.63  ? 362 ILE B CB     1 
ATOM   2403 C CG1    . ILE B 1 23  ? -23.685 -3.932  -0.661  1.00 77.64  ? 362 ILE B CG1    1 
ATOM   2404 C CG2    . ILE B 1 23  ? -21.975 -3.250  1.045   1.00 78.07  ? 362 ILE B CG2    1 
ATOM   2405 C CD1    . ILE B 1 23  ? -22.700 -4.756  -1.451  1.00 82.01  ? 362 ILE B CD1    1 
ATOM   2406 N N      . LYS B 1 24  ? -23.286 0.249   1.432   1.00 65.25  ? 363 LYS B N      1 
ATOM   2407 C CA     . LYS B 1 24  ? -22.794 1.259   2.355   1.00 65.56  ? 363 LYS B CA     1 
ATOM   2408 C C      . LYS B 1 24  ? -23.905 1.697   3.299   1.00 60.11  ? 363 LYS B C      1 
ATOM   2409 O O      . LYS B 1 24  ? -25.036 1.957   2.876   1.00 57.56  ? 363 LYS B O      1 
ATOM   2410 C CB     . LYS B 1 24  ? -22.254 2.474   1.601   1.00 65.24  ? 363 LYS B CB     1 
ATOM   2411 C CG     . LYS B 1 24  ? -21.471 3.428   2.489   1.00 64.44  ? 363 LYS B CG     1 
ATOM   2412 C CD     . LYS B 1 24  ? -20.380 2.679   3.238   1.00 68.46  ? 363 LYS B CD     1 
ATOM   2413 C CE     . LYS B 1 24  ? -19.972 3.408   4.506   1.00 71.52  ? 363 LYS B CE     1 
ATOM   2414 N NZ     . LYS B 1 24  ? -19.047 2.586   5.336   1.00 70.61  ? 363 LYS B NZ     1 
ATOM   2415 N N      . GLY B 1 25  ? -23.575 1.779   4.587   1.00 57.38  ? 364 GLY B N      1 
ATOM   2416 C CA     . GLY B 1 25  ? -24.514 2.263   5.580   1.00 57.56  ? 364 GLY B CA     1 
ATOM   2417 C C      . GLY B 1 25  ? -24.972 3.691   5.368   1.00 63.11  ? 364 GLY B C      1 
ATOM   2418 O O      . GLY B 1 25  ? -25.983 4.088   5.959   1.00 66.01  ? 364 GLY B O      1 
ATOM   2419 N N      . SER B 1 26  ? -24.260 4.467   4.543   1.00 59.95  ? 365 SER B N      1 
ATOM   2420 C CA     . SER B 1 26  ? -24.625 5.847   4.257   1.00 56.62  ? 365 SER B CA     1 
ATOM   2421 C C      . SER B 1 26  ? -25.196 6.058   2.863   1.00 47.21  ? 365 SER B C      1 
ATOM   2422 O O      . SER B 1 26  ? -25.861 7.074   2.638   1.00 50.01  ? 365 SER B O      1 
ATOM   2423 C CB     . SER B 1 26  ? -23.410 6.772   4.429   1.00 60.40  ? 365 SER B CB     1 
ATOM   2424 O OG     . SER B 1 26  ? -22.970 6.810   5.775   1.00 70.00  ? 365 SER B OG     1 
ATOM   2425 N N      . VAL B 1 27  ? -24.960 5.137   1.934   1.00 49.81  ? 366 VAL B N      1 
ATOM   2426 C CA     . VAL B 1 27  ? -25.355 5.295   0.540   1.00 48.46  ? 366 VAL B CA     1 
ATOM   2427 C C      . VAL B 1 27  ? -26.686 4.592   0.314   1.00 46.15  ? 366 VAL B C      1 
ATOM   2428 O O      . VAL B 1 27  ? -26.844 3.411   0.652   1.00 47.23  ? 366 VAL B O      1 
ATOM   2429 C CB     . VAL B 1 27  ? -24.275 4.745   -0.406  1.00 44.05  ? 366 VAL B CB     1 
ATOM   2430 C CG1    . VAL B 1 27  ? -24.787 4.728   -1.838  1.00 40.21  ? 366 VAL B CG1    1 
ATOM   2431 C CG2    . VAL B 1 27  ? -23.011 5.581   -0.300  1.00 46.99  ? 366 VAL B CG2    1 
ATOM   2432 N N      . TYR B 1 28  ? -27.640 5.317   -0.267  1.00 39.12  ? 367 TYR B N      1 
ATOM   2433 C CA     . TYR B 1 28  ? -28.955 4.790   -0.599  1.00 41.11  ? 367 TYR B CA     1 
ATOM   2434 C C      . TYR B 1 28  ? -29.255 5.066   -2.064  1.00 39.87  ? 367 TYR B C      1 
ATOM   2435 O O      . TYR B 1 28  ? -28.992 6.165   -2.562  1.00 36.99  ? 367 TYR B O      1 
ATOM   2436 C CB     . TYR B 1 28  ? -30.053 5.419   0.269   1.00 41.67  ? 367 TYR B CB     1 
ATOM   2437 C CG     . TYR B 1 28  ? -30.054 4.966   1.711   1.00 46.72  ? 367 TYR B CG     1 
ATOM   2438 C CD1    . TYR B 1 28  ? -29.149 5.489   2.624   1.00 46.31  ? 367 TYR B CD1    1 
ATOM   2439 C CD2    . TYR B 1 28  ? -30.971 4.026   2.161   1.00 44.47  ? 367 TYR B CD2    1 
ATOM   2440 C CE1    . TYR B 1 28  ? -29.150 5.082   3.944   1.00 41.94  ? 367 TYR B CE1    1 
ATOM   2441 C CE2    . TYR B 1 28  ? -30.979 3.612   3.478   1.00 45.89  ? 367 TYR B CE2    1 
ATOM   2442 C CZ     . TYR B 1 28  ? -30.066 4.144   4.366   1.00 43.09  ? 367 TYR B CZ     1 
ATOM   2443 O OH     . TYR B 1 28  ? -30.070 3.735   5.680   1.00 46.57  ? 367 TYR B OH     1 
ATOM   2444 N N      . ARG B 1 29  ? -29.809 4.069   -2.749  1.00 41.34  ? 368 ARG B N      1 
ATOM   2445 C CA     . ARG B 1 29  ? -30.269 4.258   -4.120  1.00 37.19  ? 368 ARG B CA     1 
ATOM   2446 C C      . ARG B 1 29  ? -31.523 5.122   -4.105  1.00 42.71  ? 368 ARG B C      1 
ATOM   2447 O O      . ARG B 1 29  ? -32.574 4.696   -3.615  1.00 39.20  ? 368 ARG B O      1 
ATOM   2448 C CB     . ARG B 1 29  ? -30.543 2.912   -4.783  1.00 39.22  ? 368 ARG B CB     1 
ATOM   2449 C CG     . ARG B 1 29  ? -30.750 2.995   -6.286  1.00 44.49  ? 368 ARG B CG     1 
ATOM   2450 C CD     . ARG B 1 29  ? -31.660 1.884   -6.782  1.00 49.33  ? 368 ARG B CD     1 
ATOM   2451 N NE     . ARG B 1 29  ? -31.603 1.733   -8.231  1.00 53.44  ? 368 ARG B NE     1 
ATOM   2452 C CZ     . ARG B 1 29  ? -30.992 0.735   -8.855  1.00 59.13  ? 368 ARG B CZ     1 
ATOM   2453 N NH1    . ARG B 1 29  ? -30.392 -0.235  -8.185  1.00 59.78  ? 368 ARG B NH1    1 
ATOM   2454 N NH2    . ARG B 1 29  ? -30.987 0.707   -10.185 1.00 62.23  ? 368 ARG B NH2    1 
ATOM   2455 N N      . ALA B 1 30  ? -31.415 6.341   -4.626  1.00 43.27  ? 369 ALA B N      1 
ATOM   2456 C CA     . ALA B 1 30  ? -32.540 7.262   -4.706  1.00 40.42  ? 369 ALA B CA     1 
ATOM   2457 C C      . ALA B 1 30  ? -33.156 7.184   -6.095  1.00 44.43  ? 369 ALA B C      1 
ATOM   2458 O O      . ALA B 1 30  ? -32.448 7.299   -7.101  1.00 40.45  ? 369 ALA B O      1 
ATOM   2459 C CB     . ALA B 1 30  ? -32.100 8.694   -4.399  1.00 36.65  ? 369 ALA B CB     1 
ATOM   2460 N N      . SER B 1 31  ? -34.469 6.989   -6.146  1.00 52.92  ? 370 SER B N      1 
ATOM   2461 C CA     . SER B 1 31  ? -35.198 6.823   -7.401  1.00 50.63  ? 370 SER B CA     1 
ATOM   2462 C C      . SER B 1 31  ? -35.972 8.109   -7.683  1.00 51.56  ? 370 SER B C      1 
ATOM   2463 O O      . SER B 1 31  ? -37.115 8.269   -7.253  1.00 59.24  ? 370 SER B O      1 
ATOM   2464 C CB     . SER B 1 31  ? -36.127 5.612   -7.337  1.00 49.85  ? 370 SER B CB     1 
ATOM   2465 O OG     . SER B 1 31  ? -37.106 5.774   -6.325  1.00 65.02  ? 370 SER B OG     1 
ATOM   2466 N N      . PHE B 1 32  ? -35.337 9.029   -8.401  1.00 52.05  ? 371 PHE B N      1 
ATOM   2467 C CA     . PHE B 1 32  ? -36.023 10.208  -8.902  1.00 55.17  ? 371 PHE B CA     1 
ATOM   2468 C C      . PHE B 1 32  ? -36.695 9.892   -10.236 1.00 60.27  ? 371 PHE B C      1 
ATOM   2469 O O      . PHE B 1 32  ? -36.435 8.865   -10.866 1.00 59.31  ? 371 PHE B O      1 
ATOM   2470 C CB     . PHE B 1 32  ? -35.051 11.379  -9.064  1.00 54.88  ? 371 PHE B CB     1 
ATOM   2471 C CG     . PHE B 1 32  ? -34.459 11.867  -7.773  1.00 54.05  ? 371 PHE B CG     1 
ATOM   2472 C CD1    . PHE B 1 32  ? -35.261 12.432  -6.795  1.00 53.67  ? 371 PHE B CD1    1 
ATOM   2473 C CD2    . PHE B 1 32  ? -33.095 11.782  -7.545  1.00 48.42  ? 371 PHE B CD2    1 
ATOM   2474 C CE1    . PHE B 1 32  ? -34.715 12.888  -5.608  1.00 49.78  ? 371 PHE B CE1    1 
ATOM   2475 C CE2    . PHE B 1 32  ? -32.543 12.237  -6.361  1.00 38.67  ? 371 PHE B CE2    1 
ATOM   2476 C CZ     . PHE B 1 32  ? -33.353 12.791  -5.392  1.00 42.17  ? 371 PHE B CZ     1 
ATOM   2477 N N      . LYS B 1 33  ? -37.575 10.795  -10.667 1.00 61.94  ? 372 LYS B N      1 
ATOM   2478 C CA     . LYS B 1 33  ? -38.216 10.644  -11.966 1.00 67.33  ? 372 LYS B CA     1 
ATOM   2479 C C      . LYS B 1 33  ? -37.161 10.639  -13.065 1.00 68.40  ? 372 LYS B C      1 
ATOM   2480 O O      . LYS B 1 33  ? -36.583 11.683  -13.385 1.00 78.34  ? 372 LYS B O      1 
ATOM   2481 C CB     . LYS B 1 33  ? -39.237 11.758  -12.205 1.00 66.13  ? 372 LYS B CB     1 
ATOM   2482 C CG     . LYS B 1 33  ? -40.009 11.618  -13.508 1.00 67.08  ? 372 LYS B CG     1 
ATOM   2483 C CD     . LYS B 1 33  ? -40.790 10.314  -13.546 1.00 75.18  ? 372 LYS B CD     1 
ATOM   2484 C CE     . LYS B 1 33  ? -41.615 10.195  -14.817 1.00 74.72  ? 372 LYS B CE     1 
ATOM   2485 N NZ     . LYS B 1 33  ? -42.418 8.939   -14.839 1.00 59.90  ? 372 LYS B NZ     1 
ATOM   2486 N N      . GLY B 1 34  ? -36.895 9.469   -13.638 1.00 66.39  ? 373 GLY B N      1 
ATOM   2487 C CA     . GLY B 1 34  ? -35.868 9.345   -14.652 1.00 65.60  ? 373 GLY B CA     1 
ATOM   2488 C C      . GLY B 1 34  ? -34.563 8.809   -14.100 1.00 70.54  ? 373 GLY B C      1 
ATOM   2489 O O      . GLY B 1 34  ? -34.523 7.705   -13.549 1.00 68.10  ? 373 GLY B O      1 
ATOM   2490 N N      . ASP B 1 35  ? -33.490 9.583   -14.238 1.00 84.52  ? 374 ASP B N      1 
ATOM   2491 C CA     . ASP B 1 35  ? -32.190 9.149   -13.746 1.00 67.61  ? 374 ASP B CA     1 
ATOM   2492 C C      . ASP B 1 35  ? -32.217 8.975   -12.233 1.00 61.89  ? 374 ASP B C      1 
ATOM   2493 O O      . ASP B 1 35  ? -32.795 9.787   -11.505 1.00 66.26  ? 374 ASP B O      1 
ATOM   2494 C CB     . ASP B 1 35  ? -31.110 10.157  -14.137 1.00 67.48  ? 374 ASP B CB     1 
ATOM   2495 C CG     . ASP B 1 35  ? -30.907 10.242  -15.634 1.00 79.13  ? 374 ASP B CG     1 
ATOM   2496 O OD1    . ASP B 1 35  ? -31.563 9.475   -16.369 1.00 86.02  ? 374 ASP B OD1    1 
ATOM   2497 O OD2    . ASP B 1 35  ? -30.090 11.076  -16.077 1.00 88.57  ? 374 ASP B OD2    1 
ATOM   2498 N N      . ASP B 1 36  ? -31.586 7.904   -11.760 1.00 52.14  ? 375 ASP B N      1 
ATOM   2499 C CA     . ASP B 1 36  ? -31.474 7.644   -10.335 1.00 45.31  ? 375 ASP B CA     1 
ATOM   2500 C C      . ASP B 1 36  ? -30.248 8.367   -9.778  1.00 43.30  ? 375 ASP B C      1 
ATOM   2501 O O      . ASP B 1 36  ? -29.572 9.128   -10.476 1.00 44.76  ? 375 ASP B O      1 
ATOM   2502 C CB     . ASP B 1 36  ? -31.415 6.140   -10.070 1.00 46.10  ? 375 ASP B CB     1 
ATOM   2503 C CG     . ASP B 1 36  ? -32.767 5.470   -10.206 1.00 54.71  ? 375 ASP B CG     1 
ATOM   2504 O OD1    . ASP B 1 36  ? -33.738 6.160   -10.586 1.00 60.03  ? 375 ASP B OD1    1 
ATOM   2505 O OD2    . ASP B 1 36  ? -32.860 4.256   -9.928  1.00 55.65  ? 375 ASP B OD2    1 
ATOM   2506 N N      . ALA B 1 37  ? -29.951 8.131   -8.503  1.00 40.30  ? 376 ALA B N      1 
ATOM   2507 C CA     . ALA B 1 37  ? -28.812 8.754   -7.846  1.00 37.17  ? 376 ALA B CA     1 
ATOM   2508 C C      . ALA B 1 37  ? -28.512 7.980   -6.572  1.00 30.82  ? 376 ALA B C      1 
ATOM   2509 O O      . ALA B 1 37  ? -29.295 7.132   -6.137  1.00 35.35  ? 376 ALA B O      1 
ATOM   2510 C CB     . ALA B 1 37  ? -29.077 10.233  -7.545  1.00 31.84  ? 376 ALA B CB     1 
ATOM   2511 N N      . ALA B 1 38  ? -27.361 8.282   -5.979  1.00 29.92  ? 377 ALA B N      1 
ATOM   2512 C CA     . ALA B 1 38  ? -26.924 7.662   -4.732  1.00 30.49  ? 377 ALA B CA     1 
ATOM   2513 C C      . ALA B 1 38  ? -26.727 8.761   -3.697  1.00 32.86  ? 377 ALA B C      1 
ATOM   2514 O O      . ALA B 1 38  ? -25.832 9.601   -3.839  1.00 32.50  ? 377 ALA B O      1 
ATOM   2515 C CB     . ALA B 1 38  ? -25.640 6.860   -4.936  1.00 31.67  ? 377 ALA B CB     1 
ATOM   2516 N N      . VAL B 1 39  ? -27.564 8.759   -2.664  1.00 33.72  ? 378 VAL B N      1 
ATOM   2517 C CA     . VAL B 1 39  ? -27.463 9.724   -1.577  1.00 31.99  ? 378 VAL B CA     1 
ATOM   2518 C C      . VAL B 1 39  ? -26.523 9.164   -0.520  1.00 32.62  ? 378 VAL B C      1 
ATOM   2519 O O      . VAL B 1 39  ? -26.627 7.991   -0.141  1.00 35.22  ? 378 VAL B O      1 
ATOM   2520 C CB     . VAL B 1 39  ? -28.847 10.029  -0.980  1.00 32.43  ? 378 VAL B CB     1 
ATOM   2521 C CG1    . VAL B 1 39  ? -28.752 11.155  0.041   1.00 34.79  ? 378 VAL B CG1    1 
ATOM   2522 C CG2    . VAL B 1 39  ? -29.837 10.380  -2.084  1.00 31.12  ? 378 VAL B CG2    1 
ATOM   2523 N N      . LYS B 1 40  ? -25.599 9.997   -0.048  1.00 33.40  ? 379 LYS B N      1 
ATOM   2524 C CA     . LYS B 1 40  ? -24.611 9.599   0.949   1.00 38.68  ? 379 LYS B CA     1 
ATOM   2525 C C      . LYS B 1 40  ? -24.764 10.496  2.170   1.00 40.67  ? 379 LYS B C      1 
ATOM   2526 O O      . LYS B 1 40  ? -24.431 11.686  2.118   1.00 41.03  ? 379 LYS B O      1 
ATOM   2527 C CB     . LYS B 1 40  ? -23.192 9.674   0.384   1.00 34.48  ? 379 LYS B CB     1 
ATOM   2528 C CG     . LYS B 1 40  ? -22.126 9.233   1.372   1.00 42.42  ? 379 LYS B CG     1 
ATOM   2529 C CD     . LYS B 1 40  ? -20.844 8.824   0.672   1.00 41.21  ? 379 LYS B CD     1 
ATOM   2530 C CE     . LYS B 1 40  ? -19.903 8.126   1.643   1.00 46.62  ? 379 LYS B CE     1 
ATOM   2531 N NZ     . LYS B 1 40  ? -18.709 7.558   0.961   1.00 58.21  ? 379 LYS B NZ     1 
ATOM   2532 N N      . ILE B 1 41  ? -25.266 9.926   3.261   1.00 47.38  ? 380 ILE B N      1 
ATOM   2533 C CA     . ILE B 1 41  ? -25.446 10.666  4.505   1.00 43.89  ? 380 ILE B CA     1 
ATOM   2534 C C      . ILE B 1 41  ? -24.085 10.843  5.167   1.00 47.47  ? 380 ILE B C      1 
ATOM   2535 O O      . ILE B 1 41  ? -23.399 9.862   5.474   1.00 48.12  ? 380 ILE B O      1 
ATOM   2536 C CB     . ILE B 1 41  ? -26.423 9.942   5.441   1.00 41.05  ? 380 ILE B CB     1 
ATOM   2537 C CG1    . ILE B 1 41  ? -27.594 9.352   4.652   1.00 41.26  ? 380 ILE B CG1    1 
ATOM   2538 C CG2    . ILE B 1 41  ? -26.935 10.891  6.514   1.00 36.52  ? 380 ILE B CG2    1 
ATOM   2539 C CD1    . ILE B 1 41  ? -28.567 8.569   5.510   1.00 31.94  ? 380 ILE B CD1    1 
ATOM   2540 N N      . LEU B 1 42  ? -23.692 12.094  5.388   1.00 45.78  ? 381 LEU B N      1 
ATOM   2541 C CA     . LEU B 1 42  ? -22.441 12.419  6.056   1.00 48.69  ? 381 LEU B CA     1 
ATOM   2542 C C      . LEU B 1 42  ? -22.721 13.265  7.289   1.00 56.89  ? 381 LEU B C      1 
ATOM   2543 O O      . LEU B 1 42  ? -23.556 14.176  7.254   1.00 57.44  ? 381 LEU B O      1 
ATOM   2544 C CB     . LEU B 1 42  ? -21.481 13.159  5.119   1.00 56.79  ? 381 LEU B CB     1 
ATOM   2545 C CG     . LEU B 1 42  ? -20.757 12.304  4.077   1.00 51.39  ? 381 LEU B CG     1 
ATOM   2546 C CD1    . LEU B 1 42  ? -19.826 13.157  3.230   1.00 42.87  ? 381 LEU B CD1    1 
ATOM   2547 C CD2    . LEU B 1 42  ? -19.989 11.179  4.756   1.00 49.26  ? 381 LEU B CD2    1 
ATOM   2548 N N      . LYS B 1 43  ? -22.018 12.959  8.375   1.00 62.08  ? 382 LYS B N      1 
ATOM   2549 C CA     . LYS B 1 43  ? -22.206 13.684  9.622   1.00 69.89  ? 382 LYS B CA     1 
ATOM   2550 C C      . LYS B 1 43  ? -21.760 15.135  9.483   1.00 70.82  ? 382 LYS B C      1 
ATOM   2551 O O      . LYS B 1 43  ? -20.840 15.461  8.727   1.00 81.38  ? 382 LYS B O      1 
ATOM   2552 C CB     . LYS B 1 43  ? -21.427 13.013  10.753  1.00 73.33  ? 382 LYS B CB     1 
ATOM   2553 C CG     . LYS B 1 43  ? -21.453 13.781  12.069  1.00 79.08  ? 382 LYS B CG     1 
ATOM   2554 C CD     . LYS B 1 43  ? -22.824 13.711  12.723  1.00 77.12  ? 382 LYS B CD     1 
ATOM   2555 C CE     . LYS B 1 43  ? -22.873 14.516  14.015  1.00 78.11  ? 382 LYS B CE     1 
ATOM   2556 N NZ     . LYS B 1 43  ? -23.109 15.967  13.767  1.00 77.61  ? 382 LYS B NZ     1 
ATOM   2557 N N      . GLY B 1 44  ? -22.427 16.009  10.230  1.00 69.47  ? 383 GLY B N      1 
ATOM   2558 C CA     . GLY B 1 44  ? -22.034 17.400  10.292  1.00 75.45  ? 383 GLY B CA     1 
ATOM   2559 C C      . GLY B 1 44  ? -22.763 18.304  9.322   1.00 86.84  ? 383 GLY B C      1 
ATOM   2560 O O      . GLY B 1 44  ? -22.650 18.146  8.102   1.00 79.58  ? 383 GLY B O      1 
ATOM   2561 N N      . ASP B 1 45  ? -23.524 19.259  9.865   1.00 123.78 ? 384 ASP B N      1 
ATOM   2562 C CA     . ASP B 1 45  ? -24.059 20.345  9.053   1.00 123.33 ? 384 ASP B CA     1 
ATOM   2563 C C      . ASP B 1 45  ? -22.971 21.012  8.225   1.00 124.23 ? 384 ASP B C      1 
ATOM   2564 O O      . ASP B 1 45  ? -23.274 21.610  7.184   1.00 124.61 ? 384 ASP B O      1 
ATOM   2565 C CB     . ASP B 1 45  ? -24.744 21.376  9.958   1.00 129.59 ? 384 ASP B CB     1 
ATOM   2566 C CG     . ASP B 1 45  ? -25.373 22.520  9.181   1.00 131.24 ? 384 ASP B CG     1 
ATOM   2567 O OD1    . ASP B 1 45  ? -24.650 23.233  8.455   1.00 132.79 ? 384 ASP B OD1    1 
ATOM   2568 O OD2    . ASP B 1 45  ? -26.599 22.713  9.306   1.00 130.30 ? 384 ASP B OD2    1 
ATOM   2569 N N      . VAL B 1 46  ? -21.715 20.913  8.660   1.00 95.16  ? 385 VAL B N      1 
ATOM   2570 C CA     . VAL B 1 46  ? -20.591 21.503  7.945   1.00 90.19  ? 385 VAL B CA     1 
ATOM   2571 C C      . VAL B 1 46  ? -19.809 20.434  7.189   1.00 80.94  ? 385 VAL B C      1 
ATOM   2572 O O      . VAL B 1 46  ? -18.825 19.886  7.702   1.00 83.37  ? 385 VAL B O      1 
ATOM   2573 C CB     . VAL B 1 46  ? -19.662 22.268  8.906   1.00 94.65  ? 385 VAL B CB     1 
ATOM   2574 C CG1    . VAL B 1 46  ? -18.820 23.268  8.129   1.00 88.89  ? 385 VAL B CG1    1 
ATOM   2575 C CG2    . VAL B 1 46  ? -20.472 22.946  9.992   1.00 94.35  ? 385 VAL B CG2    1 
ATOM   2576 N N      . SER B 1 47  ? -20.256 20.124  5.970   1.00 71.93  ? 386 SER B N      1 
ATOM   2577 C CA     . SER B 1 47  ? -19.428 19.486  4.952   1.00 61.44  ? 386 SER B CA     1 
ATOM   2578 C C      . SER B 1 47  ? -19.074 20.468  3.841   1.00 59.96  ? 386 SER B C      1 
ATOM   2579 O O      . SER B 1 47  ? -18.659 20.055  2.753   1.00 62.35  ? 386 SER B O      1 
ATOM   2580 C CB     . SER B 1 47  ? -20.119 18.246  4.375   1.00 64.01  ? 386 SER B CB     1 
ATOM   2581 O OG     . SER B 1 47  ? -20.313 17.267  5.381   1.00 72.88  ? 386 SER B OG     1 
ATOM   2582 N N      . SER B 1 48  ? -19.246 21.766  4.105   1.00 65.80  ? 387 SER B N      1 
ATOM   2583 C CA     . SER B 1 48  ? -18.947 22.790  3.110   1.00 68.95  ? 387 SER B CA     1 
ATOM   2584 C C      . SER B 1 48  ? -17.487 22.735  2.678   1.00 66.79  ? 387 SER B C      1 
ATOM   2585 O O      . SER B 1 48  ? -17.182 22.837  1.484   1.00 67.61  ? 387 SER B O      1 
ATOM   2586 C CB     . SER B 1 48  ? -19.290 24.174  3.666   1.00 70.58  ? 387 SER B CB     1 
ATOM   2587 O OG     . SER B 1 48  ? -18.303 24.613  4.583   1.00 76.34  ? 387 SER B OG     1 
ATOM   2588 N N      . GLU B 1 49  ? -16.567 22.581  3.634   1.00 69.48  ? 388 GLU B N      1 
ATOM   2589 C CA     . GLU B 1 49  ? -15.160 22.443  3.277   1.00 71.54  ? 388 GLU B CA     1 
ATOM   2590 C C      . GLU B 1 49  ? -14.951 21.276  2.322   1.00 66.09  ? 388 GLU B C      1 
ATOM   2591 O O      . GLU B 1 49  ? -14.192 21.387  1.352   1.00 68.71  ? 388 GLU B O      1 
ATOM   2592 C CB     . GLU B 1 49  ? -14.312 22.270  4.538   1.00 77.75  ? 388 GLU B CB     1 
ATOM   2593 C CG     . GLU B 1 49  ? -12.811 22.272  4.294   1.00 81.71  ? 388 GLU B CG     1 
ATOM   2594 C CD     . GLU B 1 49  ? -12.233 20.878  4.146   1.00 79.86  ? 388 GLU B CD     1 
ATOM   2595 O OE1    . GLU B 1 49  ? -12.963 19.895  4.395   1.00 85.04  ? 388 GLU B OE1    1 
ATOM   2596 O OE2    . GLU B 1 49  ? -11.043 20.766  3.782   1.00 80.58  ? 388 GLU B OE2    1 
ATOM   2597 N N      . ILE B 1 50  ? -15.630 20.152  2.568   1.00 62.11  ? 389 ILE B N      1 
ATOM   2598 C CA     . ILE B 1 50  ? -15.526 18.988  1.699   1.00 63.03  ? 389 ILE B CA     1 
ATOM   2599 C C      . ILE B 1 50  ? -16.042 19.269  0.292   1.00 62.42  ? 389 ILE B C      1 
ATOM   2600 O O      . ILE B 1 50  ? -15.794 18.476  -0.623  1.00 61.83  ? 389 ILE B O      1 
ATOM   2601 C CB     . ILE B 1 50  ? -16.270 17.780  2.315   1.00 60.13  ? 389 ILE B CB     1 
ATOM   2602 C CG1    . ILE B 1 50  ? -15.591 17.325  3.611   1.00 70.23  ? 389 ILE B CG1    1 
ATOM   2603 C CG2    . ILE B 1 50  ? -16.332 16.623  1.328   1.00 51.73  ? 389 ILE B CG2    1 
ATOM   2604 C CD1    . ILE B 1 50  ? -15.943 18.159  4.828   1.00 67.36  ? 389 ILE B CD1    1 
ATOM   2605 N N      . ASN B 1 51  ? -16.740 20.389  0.088   1.00 60.13  ? 390 ASN B N      1 
ATOM   2606 C CA     . ASN B 1 51  ? -17.140 20.789  -1.258  1.00 53.19  ? 390 ASN B CA     1 
ATOM   2607 C C      . ASN B 1 51  ? -15.965 21.389  -2.026  1.00 59.43  ? 390 ASN B C      1 
ATOM   2608 O O      . ASN B 1 51  ? -16.087 22.433  -2.679  1.00 63.81  ? 390 ASN B O      1 
ATOM   2609 C CB     . ASN B 1 51  ? -18.327 21.752  -1.211  1.00 58.02  ? 390 ASN B CB     1 
ATOM   2610 C CG     . ASN B 1 51  ? -19.633 21.043  -0.841  1.00 57.11  ? 390 ASN B CG     1 
ATOM   2611 O OD1    . ASN B 1 51  ? -19.610 19.945  -0.285  1.00 48.96  ? 390 ASN B OD1    1 
ATOM   2612 N ND2    . ASN B 1 51  ? -20.772 21.670  -1.145  1.00 53.72  ? 390 ASN B ND2    1 
ATOM   2613 N N      . ILE B 1 52  ? -14.808 20.731  -1.908  1.00 61.66  ? 391 ILE B N      1 
ATOM   2614 C CA     . ILE B 1 52  ? -13.803 20.730  -2.962  1.00 54.38  ? 391 ILE B CA     1 
ATOM   2615 C C      . ILE B 1 52  ? -14.142 19.719  -4.047  1.00 49.35  ? 391 ILE B C      1 
ATOM   2616 O O      . ILE B 1 52  ? -13.536 19.765  -5.125  1.00 49.71  ? 391 ILE B O      1 
ATOM   2617 C CB     . ILE B 1 52  ? -12.400 20.432  -2.393  1.00 58.57  ? 391 ILE B CB     1 
ATOM   2618 C CG1    . ILE B 1 52  ? -12.128 21.352  -1.206  1.00 64.38  ? 391 ILE B CG1    1 
ATOM   2619 C CG2    . ILE B 1 52  ? -11.332 20.591  -3.482  1.00 60.26  ? 391 ILE B CG2    1 
ATOM   2620 C CD1    . ILE B 1 52  ? -11.168 20.834  -0.198  1.00 68.34  ? 391 ILE B CD1    1 
ATOM   2621 N N      . LEU B 1 53  ? -15.090 18.808  -3.791  1.00 41.35  ? 392 LEU B N      1 
ATOM   2622 C CA     . LEU B 1 53  ? -15.488 17.791  -4.768  1.00 43.71  ? 392 LEU B CA     1 
ATOM   2623 C C      . LEU B 1 53  ? -16.210 18.380  -5.983  1.00 38.36  ? 392 LEU B C      1 
ATOM   2624 O O      . LEU B 1 53  ? -16.078 17.858  -7.099  1.00 40.39  ? 392 LEU B O      1 
ATOM   2625 C CB     . LEU B 1 53  ? -16.390 16.756  -4.086  1.00 42.15  ? 392 LEU B CB     1 
ATOM   2626 C CG     . LEU B 1 53  ? -15.847 16.119  -2.802  1.00 37.80  ? 392 LEU B CG     1 
ATOM   2627 C CD1    . LEU B 1 53  ? -16.961 15.639  -1.872  1.00 39.61  ? 392 LEU B CD1    1 
ATOM   2628 C CD2    . LEU B 1 53  ? -14.932 14.970  -3.163  1.00 35.59  ? 392 LEU B CD2    1 
ATOM   2629 N N      . LYS B 1 54  ? -17.020 19.423  -5.780  1.00 40.08  ? 393 LYS B N      1 
ATOM   2630 C CA     . LYS B 1 54  ? -17.723 20.051  -6.894  1.00 38.50  ? 393 LYS B CA     1 
ATOM   2631 C C      . LYS B 1 54  ? -16.773 20.432  -8.019  1.00 38.72  ? 393 LYS B C      1 
ATOM   2632 O O      . LYS B 1 54  ? -17.158 20.387  -9.192  1.00 40.22  ? 393 LYS B O      1 
ATOM   2633 C CB     . LYS B 1 54  ? -18.478 21.288  -6.406  1.00 44.43  ? 393 LYS B CB     1 
ATOM   2634 C CG     . LYS B 1 54  ? -17.858 21.925  -5.173  1.00 48.22  ? 393 LYS B CG     1 
ATOM   2635 C CD     . LYS B 1 54  ? -18.531 23.233  -4.783  1.00 47.66  ? 393 LYS B CD     1 
ATOM   2636 C CE     . LYS B 1 54  ? -17.837 24.420  -5.427  1.00 47.62  ? 393 LYS B CE     1 
ATOM   2637 N NZ     . LYS B 1 54  ? -18.278 25.700  -4.811  1.00 46.57  ? 393 LYS B NZ     1 
ATOM   2638 N N      . ARG B 1 55  ? -15.540 20.814  -7.689  1.00 38.79  ? 394 ARG B N      1 
ATOM   2639 C CA     . ARG B 1 55  ? -14.551 21.185  -8.695  1.00 39.58  ? 394 ARG B CA     1 
ATOM   2640 C C      . ARG B 1 55  ? -13.834 19.981  -9.292  1.00 36.47  ? 394 ARG B C      1 
ATOM   2641 O O      . ARG B 1 55  ? -12.957 20.159  -10.147 1.00 33.67  ? 394 ARG B O      1 
ATOM   2642 C CB     . ARG B 1 55  ? -13.531 22.149  -8.089  1.00 39.71  ? 394 ARG B CB     1 
ATOM   2643 C CG     . ARG B 1 55  ? -14.143 23.143  -7.123  1.00 44.11  ? 394 ARG B CG     1 
ATOM   2644 C CD     . ARG B 1 55  ? -13.764 24.567  -7.473  1.00 49.39  ? 394 ARG B CD     1 
ATOM   2645 N NE     . ARG B 1 55  ? -13.920 25.456  -6.329  1.00 53.73  ? 394 ARG B NE     1 
ATOM   2646 C CZ     . ARG B 1 55  ? -13.034 25.567  -5.349  1.00 58.23  ? 394 ARG B CZ     1 
ATOM   2647 N NH1    . ARG B 1 55  ? -11.926 24.844  -5.336  1.00 56.07  ? 394 ARG B NH1    1 
ATOM   2648 N NH2    . ARG B 1 55  ? -13.266 26.422  -4.358  1.00 60.86  ? 394 ARG B NH2    1 
ATOM   2649 N N      . ILE B 1 56  ? -14.176 18.772  -8.862  1.00 33.44  ? 395 ILE B N      1 
ATOM   2650 C CA     . ILE B 1 56  ? -13.616 17.545  -9.420  1.00 33.27  ? 395 ILE B CA     1 
ATOM   2651 C C      . ILE B 1 56  ? -14.649 17.032  -10.417 1.00 34.38  ? 395 ILE B C      1 
ATOM   2652 O O      . ILE B 1 56  ? -15.581 16.306  -10.066 1.00 35.95  ? 395 ILE B O      1 
ATOM   2653 C CB     . ILE B 1 56  ? -13.298 16.517  -8.338  1.00 33.43  ? 395 ILE B CB     1 
ATOM   2654 C CG1    . ILE B 1 56  ? -12.307 17.095  -7.324  1.00 36.00  ? 395 ILE B CG1    1 
ATOM   2655 C CG2    . ILE B 1 56  ? -12.751 15.243  -8.963  1.00 31.67  ? 395 ILE B CG2    1 
ATOM   2656 C CD1    . ILE B 1 56  ? -12.012 16.166  -6.167  1.00 33.14  ? 395 ILE B CD1    1 
ATOM   2657 N N      . ASN B 1 57  ? -14.482 17.413  -11.681 1.00 28.69  ? 396 ASN B N      1 
ATOM   2658 C CA     . ASN B 1 57  ? -15.435 17.086  -12.734 1.00 28.64  ? 396 ASN B CA     1 
ATOM   2659 C C      . ASN B 1 57  ? -14.719 16.335  -13.846 1.00 25.70  ? 396 ASN B C      1 
ATOM   2660 O O      . ASN B 1 57  ? -13.781 16.862  -14.454 1.00 26.21  ? 396 ASN B O      1 
ATOM   2661 C CB     . ASN B 1 57  ? -16.102 18.353  -13.270 1.00 34.82  ? 396 ASN B CB     1 
ATOM   2662 C CG     . ASN B 1 57  ? -16.961 19.040  -12.225 1.00 44.91  ? 396 ASN B CG     1 
ATOM   2663 O OD1    . ASN B 1 57  ? -17.712 18.388  -11.498 1.00 45.83  ? 396 ASN B OD1    1 
ATOM   2664 N ND2    . ASN B 1 57  ? -16.847 20.361  -12.138 1.00 51.05  ? 396 ASN B ND2    1 
ATOM   2665 N N      . HIS B 1 58  ? -15.164 15.108  -14.107 1.00 24.53  ? 397 HIS B N      1 
ATOM   2666 C CA     . HIS B 1 58  ? -14.570 14.269  -15.135 1.00 24.92  ? 397 HIS B CA     1 
ATOM   2667 C C      . HIS B 1 58  ? -15.546 13.148  -15.462 1.00 23.71  ? 397 HIS B C      1 
ATOM   2668 O O      . HIS B 1 58  ? -16.178 12.589  -14.562 1.00 24.05  ? 397 HIS B O      1 
ATOM   2669 C CB     . HIS B 1 58  ? -13.222 13.699  -14.677 1.00 23.09  ? 397 HIS B CB     1 
ATOM   2670 C CG     . HIS B 1 58  ? -12.412 13.099  -15.783 1.00 22.39  ? 397 HIS B CG     1 
ATOM   2671 N ND1    . HIS B 1 58  ? -12.608 11.813  -16.238 1.00 21.60  ? 397 HIS B ND1    1 
ATOM   2672 C CD2    . HIS B 1 58  ? -11.399 13.608  -16.523 1.00 23.05  ? 397 HIS B CD2    1 
ATOM   2673 C CE1    . HIS B 1 58  ? -11.752 11.556  -17.212 1.00 21.73  ? 397 HIS B CE1    1 
ATOM   2674 N NE2    . HIS B 1 58  ? -11.007 12.629  -17.404 1.00 22.58  ? 397 HIS B NE2    1 
ATOM   2675 N N      . ALA B 1 59  ? -15.663 12.828  -16.752 1.00 24.37  ? 398 ALA B N      1 
ATOM   2676 C CA     . ALA B 1 59  ? -16.618 11.813  -17.182 1.00 24.91  ? 398 ALA B CA     1 
ATOM   2677 C C      . ALA B 1 59  ? -16.368 10.460  -16.531 1.00 23.64  ? 398 ALA B C      1 
ATOM   2678 O O      . ALA B 1 59  ? -17.291 9.642   -16.457 1.00 25.05  ? 398 ALA B O      1 
ATOM   2679 C CB     . ALA B 1 59  ? -16.584 11.671  -18.705 1.00 26.16  ? 398 ALA B CB     1 
ATOM   2680 N N      . ASN B 1 60  ? -15.147 10.203  -16.061 1.00 25.57  ? 399 ASN B N      1 
ATOM   2681 C CA     . ASN B 1 60  ? -14.800 8.940   -15.421 1.00 23.41  ? 399 ASN B CA     1 
ATOM   2682 C C      . ASN B 1 60  ? -14.628 9.097   -13.912 1.00 25.01  ? 399 ASN B C      1 
ATOM   2683 O O      . ASN B 1 60  ? -13.905 8.325   -13.277 1.00 25.66  ? 399 ASN B O      1 
ATOM   2684 C CB     . ASN B 1 60  ? -13.539 8.351   -16.050 1.00 22.63  ? 399 ASN B CB     1 
ATOM   2685 C CG     . ASN B 1 60  ? -13.679 8.137   -17.547 1.00 22.40  ? 399 ASN B CG     1 
ATOM   2686 O OD1    . ASN B 1 60  ? -12.838 8.577   -18.332 1.00 21.97  ? 399 ASN B OD1    1 
ATOM   2687 N ND2    . ASN B 1 60  ? -14.750 7.461   -17.949 1.00 21.72  ? 399 ASN B ND2    1 
ATOM   2688 N N      . ILE B 1 61  ? -15.285 10.099  -13.329 1.00 26.02  ? 400 ILE B N      1 
ATOM   2689 C CA     . ILE B 1 61  ? -15.295 10.322  -11.888 1.00 27.07  ? 400 ILE B CA     1 
ATOM   2690 C C      . ILE B 1 61  ? -16.737 10.545  -11.462 1.00 23.91  ? 400 ILE B C      1 
ATOM   2691 O O      . ILE B 1 61  ? -17.426 11.405  -12.023 1.00 23.10  ? 400 ILE B O      1 
ATOM   2692 C CB     . ILE B 1 61  ? -14.419 11.524  -11.482 1.00 27.61  ? 400 ILE B CB     1 
ATOM   2693 C CG1    . ILE B 1 61  ? -12.952 11.270  -11.837 1.00 25.40  ? 400 ILE B CG1    1 
ATOM   2694 C CG2    . ILE B 1 61  ? -14.571 11.816  -9.996  1.00 27.42  ? 400 ILE B CG2    1 
ATOM   2695 C CD1    . ILE B 1 61  ? -12.044 12.455  -11.572 1.00 22.93  ? 400 ILE B CD1    1 
ATOM   2696 N N      . ILE B 1 62  ? -17.195 9.766   -10.477 1.00 27.06  ? 401 ILE B N      1 
ATOM   2697 C CA     . ILE B 1 62  ? -18.574 9.878   -10.017 1.00 27.79  ? 401 ILE B CA     1 
ATOM   2698 C C      . ILE B 1 62  ? -18.875 11.335  -9.703  1.00 29.95  ? 401 ILE B C      1 
ATOM   2699 O O      . ILE B 1 62  ? -18.140 11.995  -8.961  1.00 29.52  ? 401 ILE B O      1 
ATOM   2700 C CB     . ILE B 1 62  ? -18.814 8.959   -8.805  1.00 26.08  ? 401 ILE B CB     1 
ATOM   2701 C CG1    . ILE B 1 62  ? -20.246 8.418   -8.824  1.00 26.41  ? 401 ILE B CG1    1 
ATOM   2702 C CG2    . ILE B 1 62  ? -18.535 9.692   -7.501  1.00 29.87  ? 401 ILE B CG2    1 
ATOM   2703 C CD1    . ILE B 1 62  ? -20.575 7.630   -10.071 1.00 27.26  ? 401 ILE B CD1    1 
ATOM   2704 N N      . ARG B 1 63  ? -19.949 11.850  -10.294 1.00 31.23  ? 402 ARG B N      1 
ATOM   2705 C CA     . ARG B 1 63  ? -20.246 13.274  -10.250 1.00 32.28  ? 402 ARG B CA     1 
ATOM   2706 C C      . ARG B 1 63  ? -21.180 13.594  -9.091  1.00 33.40  ? 402 ARG B C      1 
ATOM   2707 O O      . ARG B 1 63  ? -22.175 12.896  -8.873  1.00 34.41  ? 402 ARG B O      1 
ATOM   2708 C CB     . ARG B 1 63  ? -20.870 13.731  -11.568 1.00 37.11  ? 402 ARG B CB     1 
ATOM   2709 C CG     . ARG B 1 63  ? -21.391 15.159  -11.542 1.00 41.11  ? 402 ARG B CG     1 
ATOM   2710 C CD     . ARG B 1 63  ? -22.021 15.543  -12.871 1.00 49.83  ? 402 ARG B CD     1 
ATOM   2711 N NE     . ARG B 1 63  ? -23.116 14.651  -13.233 1.00 55.52  ? 402 ARG B NE     1 
ATOM   2712 C CZ     . ARG B 1 63  ? -24.388 14.859  -12.919 1.00 69.46  ? 402 ARG B CZ     1 
ATOM   2713 N NH1    . ARG B 1 63  ? -24.766 15.926  -12.233 1.00 57.68  ? 402 ARG B NH1    1 
ATOM   2714 N NH2    . ARG B 1 63  ? -25.304 13.974  -13.302 1.00 71.02  ? 402 ARG B NH2    1 
ATOM   2715 N N      . LEU B 1 64  ? -20.856 14.655  -8.356  1.00 36.30  ? 403 LEU B N      1 
ATOM   2716 C CA     . LEU B 1 64  ? -21.728 15.160  -7.301  1.00 35.20  ? 403 LEU B CA     1 
ATOM   2717 C C      . LEU B 1 64  ? -22.824 16.005  -7.938  1.00 38.13  ? 403 LEU B C      1 
ATOM   2718 O O      . LEU B 1 64  ? -22.554 17.088  -8.468  1.00 42.25  ? 403 LEU B O      1 
ATOM   2719 C CB     . LEU B 1 64  ? -20.927 15.972  -6.286  1.00 34.86  ? 403 LEU B CB     1 
ATOM   2720 C CG     . LEU B 1 64  ? -21.714 16.576  -5.122  1.00 37.21  ? 403 LEU B CG     1 
ATOM   2721 C CD1    . LEU B 1 64  ? -22.384 15.480  -4.307  1.00 33.16  ? 403 LEU B CD1    1 
ATOM   2722 C CD2    . LEU B 1 64  ? -20.806 17.424  -4.244  1.00 35.88  ? 403 LEU B CD2    1 
ATOM   2723 N N      . SER B 1 65  ? -24.065 15.515  -7.885  1.00 39.95  ? 404 SER B N      1 
ATOM   2724 C CA     . SER B 1 65  ? -25.182 16.231  -8.493  1.00 38.58  ? 404 SER B CA     1 
ATOM   2725 C C      . SER B 1 65  ? -25.620 17.415  -7.638  1.00 40.48  ? 404 SER B C      1 
ATOM   2726 O O      . SER B 1 65  ? -25.780 18.531  -8.143  1.00 50.62  ? 404 SER B O      1 
ATOM   2727 C CB     . SER B 1 65  ? -26.354 15.275  -8.722  1.00 41.27  ? 404 SER B CB     1 
ATOM   2728 O OG     . SER B 1 65  ? -25.963 14.173  -9.525  1.00 44.51  ? 404 SER B OG     1 
ATOM   2729 N N      . GLY B 1 66  ? -25.824 17.190  -6.351  1.00 40.37  ? 405 GLY B N      1 
ATOM   2730 C CA     . GLY B 1 66  ? -26.254 18.243  -5.464  1.00 42.73  ? 405 GLY B CA     1 
ATOM   2731 C C      . GLY B 1 66  ? -25.972 17.883  -4.026  1.00 35.72  ? 405 GLY B C      1 
ATOM   2732 O O      . GLY B 1 66  ? -25.178 16.988  -3.735  1.00 34.95  ? 405 GLY B O      1 
ATOM   2733 N N      . PHE B 1 67  ? -26.636 18.590  -3.115  1.00 35.66  ? 406 PHE B N      1 
ATOM   2734 C CA     . PHE B 1 67  ? -26.436 18.337  -1.695  1.00 38.64  ? 406 PHE B CA     1 
ATOM   2735 C C      . PHE B 1 67  ? -27.642 18.845  -0.922  1.00 39.64  ? 406 PHE B C      1 
ATOM   2736 O O      . PHE B 1 67  ? -28.451 19.624  -1.434  1.00 40.47  ? 406 PHE B O      1 
ATOM   2737 C CB     . PHE B 1 67  ? -25.150 18.993  -1.179  1.00 41.13  ? 406 PHE B CB     1 
ATOM   2738 C CG     . PHE B 1 67  ? -25.254 20.479  -1.004  1.00 39.69  ? 406 PHE B CG     1 
ATOM   2739 C CD1    . PHE B 1 67  ? -25.106 21.332  -2.085  1.00 46.37  ? 406 PHE B CD1    1 
ATOM   2740 C CD2    . PHE B 1 67  ? -25.490 21.024  0.245   1.00 38.03  ? 406 PHE B CD2    1 
ATOM   2741 C CE1    . PHE B 1 67  ? -25.199 22.702  -1.923  1.00 44.67  ? 406 PHE B CE1    1 
ATOM   2742 C CE2    . PHE B 1 67  ? -25.583 22.392  0.415   1.00 40.67  ? 406 PHE B CE2    1 
ATOM   2743 C CZ     . PHE B 1 67  ? -25.437 23.233  -0.670  1.00 43.67  ? 406 PHE B CZ     1 
ATOM   2744 N N      . CYS B 1 68  ? -27.749 18.387  0.323   1.00 38.36  ? 407 CYS B N      1 
ATOM   2745 C CA     . CYS B 1 68  ? -28.843 18.765  1.204   1.00 39.53  ? 407 CYS B CA     1 
ATOM   2746 C C      . CYS B 1 68  ? -28.370 18.669  2.645   1.00 38.87  ? 407 CYS B C      1 
ATOM   2747 O O      . CYS B 1 68  ? -27.642 17.740  3.006   1.00 38.77  ? 407 CYS B O      1 
ATOM   2748 C CB     . CYS B 1 68  ? -30.072 17.873  0.989   1.00 39.36  ? 407 CYS B CB     1 
ATOM   2749 S SG     . CYS B 1 68  ? -31.431 18.196  2.135   1.00 48.61  ? 407 CYS B SG     1 
ATOM   2750 N N      . VAL B 1 69  ? -28.783 19.636  3.461   1.00 40.74  ? 408 VAL B N      1 
ATOM   2751 C CA     . VAL B 1 69  ? -28.467 19.665  4.883   1.00 46.22  ? 408 VAL B CA     1 
ATOM   2752 C C      . VAL B 1 69  ? -29.773 19.779  5.653   1.00 46.20  ? 408 VAL B C      1 
ATOM   2753 O O      . VAL B 1 69  ? -30.580 20.675  5.383   1.00 49.14  ? 408 VAL B O      1 
ATOM   2754 C CB     . VAL B 1 69  ? -27.523 20.829  5.241   1.00 53.85  ? 408 VAL B CB     1 
ATOM   2755 C CG1    . VAL B 1 69  ? -27.158 20.785  6.719   1.00 60.57  ? 408 VAL B CG1    1 
ATOM   2756 C CG2    . VAL B 1 69  ? -26.273 20.783  4.377   1.00 50.52  ? 408 VAL B CG2    1 
ATOM   2757 N N      . TYR B 1 70  ? -29.983 18.872  6.605   1.00 45.52  ? 409 TYR B N      1 
ATOM   2758 C CA     . TYR B 1 70  ? -31.218 18.848  7.380   1.00 46.54  ? 409 TYR B CA     1 
ATOM   2759 C C      . TYR B 1 70  ? -30.939 18.232  8.741   1.00 49.71  ? 409 TYR B C      1 
ATOM   2760 O O      . TYR B 1 70  ? -30.451 17.100  8.821   1.00 49.95  ? 409 TYR B O      1 
ATOM   2761 C CB     . TYR B 1 70  ? -32.311 18.066  6.646   1.00 46.78  ? 409 TYR B CB     1 
ATOM   2762 C CG     . TYR B 1 70  ? -33.527 17.763  7.492   1.00 48.63  ? 409 TYR B CG     1 
ATOM   2763 C CD1    . TYR B 1 70  ? -34.509 18.724  7.703   1.00 51.82  ? 409 TYR B CD1    1 
ATOM   2764 C CD2    . TYR B 1 70  ? -33.697 16.514  8.075   1.00 49.19  ? 409 TYR B CD2    1 
ATOM   2765 C CE1    . TYR B 1 70  ? -35.623 18.450  8.475   1.00 50.49  ? 409 TYR B CE1    1 
ATOM   2766 C CE2    . TYR B 1 70  ? -34.807 16.230  8.846   1.00 51.44  ? 409 TYR B CE2    1 
ATOM   2767 C CZ     . TYR B 1 70  ? -35.767 17.201  9.043   1.00 53.30  ? 409 TYR B CZ     1 
ATOM   2768 O OH     . TYR B 1 70  ? -36.872 16.920  9.813   1.00 56.31  ? 409 TYR B OH     1 
ATOM   2769 N N      . LYS B 1 71  ? -31.244 18.981  9.801   1.00 47.58  ? 410 LYS B N      1 
ATOM   2770 C CA     . LYS B 1 71  ? -31.129 18.495  11.176  1.00 47.08  ? 410 LYS B CA     1 
ATOM   2771 C C      . LYS B 1 71  ? -29.710 18.017  11.488  1.00 50.53  ? 410 LYS B C      1 
ATOM   2772 O O      . LYS B 1 71  ? -29.500 16.948  12.064  1.00 49.61  ? 410 LYS B O      1 
ATOM   2773 C CB     . LYS B 1 71  ? -32.153 17.391  11.452  1.00 49.53  ? 410 LYS B CB     1 
ATOM   2774 C CG     . LYS B 1 71  ? -33.241 17.794  12.435  1.00 58.44  ? 410 LYS B CG     1 
ATOM   2775 C CD     . LYS B 1 71  ? -33.936 19.077  11.999  1.00 59.50  ? 410 LYS B CD     1 
ATOM   2776 C CE     . LYS B 1 71  ? -35.031 19.477  12.978  1.00 57.63  ? 410 LYS B CE     1 
ATOM   2777 N NZ     . LYS B 1 71  ? -34.497 19.750  14.342  1.00 53.06  ? 410 LYS B NZ     1 
ATOM   2778 N N      . GLY B 1 72  ? -28.728 18.829  11.103  1.00 51.41  ? 411 GLY B N      1 
ATOM   2779 C CA     . GLY B 1 72  ? -27.348 18.576  11.456  1.00 60.86  ? 411 GLY B CA     1 
ATOM   2780 C C      . GLY B 1 72  ? -26.648 17.496  10.660  1.00 65.54  ? 411 GLY B C      1 
ATOM   2781 O O      . GLY B 1 72  ? -25.468 17.228  10.923  1.00 74.01  ? 411 GLY B O      1 
ATOM   2782 N N      . ASN B 1 73  ? -27.325 16.862  9.707   1.00 59.47  ? 412 ASN B N      1 
ATOM   2783 C CA     . ASN B 1 73  ? -26.711 15.869  8.837   1.00 56.90  ? 412 ASN B CA     1 
ATOM   2784 C C      . ASN B 1 73  ? -26.807 16.332  7.391   1.00 53.19  ? 412 ASN B C      1 
ATOM   2785 O O      . ASN B 1 73  ? -27.812 16.921  6.981   1.00 52.01  ? 412 ASN B O      1 
ATOM   2786 C CB     . ASN B 1 73  ? -27.370 14.495  9.002   1.00 54.62  ? 412 ASN B CB     1 
ATOM   2787 C CG     . ASN B 1 73  ? -26.663 13.627  10.027  1.00 60.33  ? 412 ASN B CG     1 
ATOM   2788 O OD1    . ASN B 1 73  ? -25.789 14.095  10.757  1.00 62.30  ? 412 ASN B OD1    1 
ATOM   2789 N ND2    . ASN B 1 73  ? -27.038 12.353  10.085  1.00 62.25  ? 412 ASN B ND2    1 
ATOM   2790 N N      . THR B 1 74  ? -25.753 16.067  6.624   1.00 54.45  ? 413 THR B N      1 
ATOM   2791 C CA     . THR B 1 74  ? -25.659 16.486  5.233   1.00 49.51  ? 413 THR B CA     1 
ATOM   2792 C C      . THR B 1 74  ? -25.740 15.273  4.316   1.00 41.85  ? 413 THR B C      1 
ATOM   2793 O O      . THR B 1 74  ? -25.138 14.231  4.592   1.00 42.41  ? 413 THR B O      1 
ATOM   2794 C CB     . THR B 1 74  ? -24.357 17.249  4.976   1.00 50.18  ? 413 THR B CB     1 
ATOM   2795 O OG1    . THR B 1 74  ? -24.372 18.481  5.709   1.00 60.28  ? 413 THR B OG1    1 
ATOM   2796 C CG2    . THR B 1 74  ? -24.198 17.547  3.493   1.00 41.72  ? 413 THR B CG2    1 
ATOM   2797 N N      . TYR B 1 75  ? -26.482 15.419  3.222   1.00 39.12  ? 414 TYR B N      1 
ATOM   2798 C CA     . TYR B 1 75  ? -26.717 14.340  2.272   1.00 36.67  ? 414 TYR B CA     1 
ATOM   2799 C C      . TYR B 1 75  ? -26.145 14.741  0.920   1.00 37.07  ? 414 TYR B C      1 
ATOM   2800 O O      . TYR B 1 75  ? -26.516 15.784  0.371   1.00 38.61  ? 414 TYR B O      1 
ATOM   2801 C CB     . TYR B 1 75  ? -28.211 14.031  2.156   1.00 31.35  ? 414 TYR B CB     1 
ATOM   2802 C CG     . TYR B 1 75  ? -28.921 13.929  3.487   1.00 38.23  ? 414 TYR B CG     1 
ATOM   2803 C CD1    . TYR B 1 75  ? -29.419 15.062  4.117   1.00 41.13  ? 414 TYR B CD1    1 
ATOM   2804 C CD2    . TYR B 1 75  ? -29.093 12.702  4.114   1.00 33.02  ? 414 TYR B CD2    1 
ATOM   2805 C CE1    . TYR B 1 75  ? -30.068 14.978  5.331   1.00 40.25  ? 414 TYR B CE1    1 
ATOM   2806 C CE2    . TYR B 1 75  ? -29.741 12.607  5.330   1.00 36.56  ? 414 TYR B CE2    1 
ATOM   2807 C CZ     . TYR B 1 75  ? -30.228 13.748  5.935   1.00 43.38  ? 414 TYR B CZ     1 
ATOM   2808 O OH     . TYR B 1 75  ? -30.876 13.661  7.148   1.00 42.25  ? 414 TYR B OH     1 
ATOM   2809 N N      . LEU B 1 76  ? -25.248 13.915  0.388   1.00 33.00  ? 415 LEU B N      1 
ATOM   2810 C CA     . LEU B 1 76  ? -24.636 14.149  -0.912  1.00 33.22  ? 415 LEU B CA     1 
ATOM   2811 C C      . LEU B 1 76  ? -25.332 13.295  -1.963  1.00 31.92  ? 415 LEU B C      1 
ATOM   2812 O O      . LEU B 1 76  ? -25.432 12.073  -1.810  1.00 35.12  ? 415 LEU B O      1 
ATOM   2813 C CB     . LEU B 1 76  ? -23.140 13.831  -0.875  1.00 30.11  ? 415 LEU B CB     1 
ATOM   2814 C CG     . LEU B 1 76  ? -22.310 14.693  0.079   1.00 33.33  ? 415 LEU B CG     1 
ATOM   2815 C CD1    . LEU B 1 76  ? -20.854 14.255  0.072   1.00 29.10  ? 415 LEU B CD1    1 
ATOM   2816 C CD2    . LEU B 1 76  ? -22.436 16.164  -0.285  1.00 31.58  ? 415 LEU B CD2    1 
ATOM   2817 N N      . VAL B 1 77  ? -25.810 13.939  -3.021  1.00 28.65  ? 416 VAL B N      1 
ATOM   2818 C CA     . VAL B 1 77  ? -26.517 13.266  -4.105  1.00 31.01  ? 416 VAL B CA     1 
ATOM   2819 C C      . VAL B 1 77  ? -25.535 13.090  -5.256  1.00 31.48  ? 416 VAL B C      1 
ATOM   2820 O O      . VAL B 1 77  ? -25.173 14.059  -5.933  1.00 29.27  ? 416 VAL B O      1 
ATOM   2821 C CB     . VAL B 1 77  ? -27.762 14.051  -4.539  1.00 33.81  ? 416 VAL B CB     1 
ATOM   2822 C CG1    . VAL B 1 77  ? -28.590 13.233  -5.514  1.00 33.05  ? 416 VAL B CG1    1 
ATOM   2823 C CG2    . VAL B 1 77  ? -28.590 14.447  -3.325  1.00 31.47  ? 416 VAL B CG2    1 
ATOM   2824 N N      . TYR B 1 78  ? -25.105 11.853  -5.482  1.00 31.53  ? 417 TYR B N      1 
ATOM   2825 C CA     . TYR B 1 78  ? -24.117 11.523  -6.497  1.00 30.71  ? 417 TYR B CA     1 
ATOM   2826 C C      . TYR B 1 78  ? -24.774 10.864  -7.703  1.00 30.10  ? 417 TYR B C      1 
ATOM   2827 O O      . TYR B 1 78  ? -25.869 10.301  -7.619  1.00 29.31  ? 417 TYR B O      1 
ATOM   2828 C CB     . TYR B 1 78  ? -23.041 10.584  -5.936  1.00 32.37  ? 417 TYR B CB     1 
ATOM   2829 C CG     . TYR B 1 78  ? -22.036 11.243  -5.019  1.00 32.99  ? 417 TYR B CG     1 
ATOM   2830 C CD1    . TYR B 1 78  ? -20.975 11.977  -5.535  1.00 32.04  ? 417 TYR B CD1    1 
ATOM   2831 C CD2    . TYR B 1 78  ? -22.134 11.113  -3.640  1.00 27.74  ? 417 TYR B CD2    1 
ATOM   2832 C CE1    . TYR B 1 78  ? -20.050 12.576  -4.702  1.00 32.76  ? 417 TYR B CE1    1 
ATOM   2833 C CE2    . TYR B 1 78  ? -21.213 11.706  -2.799  1.00 28.30  ? 417 TYR B CE2    1 
ATOM   2834 C CZ     . TYR B 1 78  ? -20.173 12.436  -3.335  1.00 29.92  ? 417 TYR B CZ     1 
ATOM   2835 O OH     . TYR B 1 78  ? -19.254 13.030  -2.501  1.00 33.30  ? 417 TYR B OH     1 
ATOM   2836 N N      . GLU B 1 79  ? -24.078 10.944  -8.835  1.00 30.96  ? 418 GLU B N      1 
ATOM   2837 C CA     . GLU B 1 79  ? -24.458 10.165  -10.004 1.00 30.27  ? 418 GLU B CA     1 
ATOM   2838 C C      . GLU B 1 79  ? -24.477 8.682   -9.655  1.00 33.54  ? 418 GLU B C      1 
ATOM   2839 O O      . GLU B 1 79  ? -23.582 8.176   -8.971  1.00 35.08  ? 418 GLU B O      1 
ATOM   2840 C CB     . GLU B 1 79  ? -23.479 10.428  -11.148 1.00 31.33  ? 418 GLU B CB     1 
ATOM   2841 C CG     . GLU B 1 79  ? -23.509 9.389   -12.254 1.00 29.74  ? 418 GLU B CG     1 
ATOM   2842 C CD     . GLU B 1 79  ? -22.295 9.475   -13.161 1.00 36.08  ? 418 GLU B CD     1 
ATOM   2843 O OE1    . GLU B 1 79  ? -21.362 10.242  -12.835 1.00 34.72  ? 418 GLU B OE1    1 
ATOM   2844 O OE2    . GLU B 1 79  ? -22.270 8.776   -14.197 1.00 27.44  ? 418 GLU B OE2    1 
ATOM   2845 N N      . PHE B 1 80  ? -25.507 7.983   -10.124 1.00 32.46  ? 419 PHE B N      1 
ATOM   2846 C CA     . PHE B 1 80  ? -25.683 6.572   -9.809  1.00 34.14  ? 419 PHE B CA     1 
ATOM   2847 C C      . PHE B 1 80  ? -24.999 5.709   -10.862 1.00 33.94  ? 419 PHE B C      1 
ATOM   2848 O O      . PHE B 1 80  ? -25.255 5.861   -12.060 1.00 32.83  ? 419 PHE B O      1 
ATOM   2849 C CB     . PHE B 1 80  ? -27.168 6.215   -9.716  1.00 35.75  ? 419 PHE B CB     1 
ATOM   2850 C CG     . PHE B 1 80  ? -27.421 4.768   -9.391  1.00 34.27  ? 419 PHE B CG     1 
ATOM   2851 C CD1    . PHE B 1 80  ? -27.243 4.292   -8.102  1.00 36.54  ? 419 PHE B CD1    1 
ATOM   2852 C CD2    . PHE B 1 80  ? -27.831 3.884   -10.374 1.00 35.47  ? 419 PHE B CD2    1 
ATOM   2853 C CE1    . PHE B 1 80  ? -27.468 2.963   -7.800  1.00 38.47  ? 419 PHE B CE1    1 
ATOM   2854 C CE2    . PHE B 1 80  ? -28.059 2.553   -10.077 1.00 39.11  ? 419 PHE B CE2    1 
ATOM   2855 C CZ     . PHE B 1 80  ? -27.876 2.093   -8.789  1.00 38.53  ? 419 PHE B CZ     1 
ATOM   2856 N N      . ALA B 1 81  ? -24.128 4.810   -10.407 1.00 34.19  ? 420 ALA B N      1 
ATOM   2857 C CA     . ALA B 1 81  ? -23.488 3.819   -11.264 1.00 31.03  ? 420 ALA B CA     1 
ATOM   2858 C C      . ALA B 1 81  ? -24.243 2.502   -11.125 1.00 31.93  ? 420 ALA B C      1 
ATOM   2859 O O      . ALA B 1 81  ? -24.317 1.939   -10.027 1.00 32.09  ? 420 ALA B O      1 
ATOM   2860 C CB     . ALA B 1 81  ? -22.016 3.643   -10.895 1.00 31.09  ? 420 ALA B CB     1 
ATOM   2861 N N      . GLU B 1 82  ? -24.795 2.011   -12.232 1.00 29.41  ? 421 GLU B N      1 
ATOM   2862 C CA     . GLU B 1 82  ? -25.737 0.901   -12.179 1.00 35.66  ? 421 GLU B CA     1 
ATOM   2863 C C      . GLU B 1 82  ? -25.093 -0.475  -12.307 1.00 34.90  ? 421 GLU B C      1 
ATOM   2864 O O      . GLU B 1 82  ? -25.778 -1.478  -12.080 1.00 36.12  ? 421 GLU B O      1 
ATOM   2865 C CB     . GLU B 1 82  ? -26.805 1.066   -13.268 1.00 40.75  ? 421 GLU B CB     1 
ATOM   2866 C CG     . GLU B 1 82  ? -26.264 1.248   -14.679 1.00 40.04  ? 421 GLU B CG     1 
ATOM   2867 C CD     . GLU B 1 82  ? -27.373 1.429   -15.698 1.00 42.22  ? 421 GLU B CD     1 
ATOM   2868 O OE1    . GLU B 1 82  ? -28.538 1.125   -15.364 1.00 54.74  ? 421 GLU B OE1    1 
ATOM   2869 O OE2    . GLU B 1 82  ? -27.085 1.877   -16.826 1.00 50.32  ? 421 GLU B OE2    1 
ATOM   2870 N N      . ASN B 1 83  ? -23.812 -0.564  -12.660 1.00 28.44  ? 422 ASN B N      1 
ATOM   2871 C CA     . ASN B 1 83  ? -23.132 -1.847  -12.810 1.00 30.39  ? 422 ASN B CA     1 
ATOM   2872 C C      . ASN B 1 83  ? -22.124 -2.091  -11.689 1.00 29.55  ? 422 ASN B C      1 
ATOM   2873 O O      . ASN B 1 83  ? -21.048 -2.647  -11.912 1.00 31.54  ? 422 ASN B O      1 
ATOM   2874 C CB     . ASN B 1 83  ? -22.461 -1.950  -14.176 1.00 27.50  ? 422 ASN B CB     1 
ATOM   2875 C CG     . ASN B 1 83  ? -23.444 -2.300  -15.278 1.00 29.00  ? 422 ASN B CG     1 
ATOM   2876 O OD1    . ASN B 1 83  ? -24.482 -2.912  -15.026 1.00 30.69  ? 422 ASN B OD1    1 
ATOM   2877 N ND2    . ASN B 1 83  ? -23.128 -1.902  -16.503 1.00 30.87  ? 422 ASN B ND2    1 
ATOM   2878 N N      . ASN B 1 84  ? -22.462 -1.653  -10.482 1.00 26.17  ? 423 ASN B N      1 
ATOM   2879 C CA     . ASN B 1 84  ? -21.732 -2.004  -9.259  1.00 28.42  ? 423 ASN B CA     1 
ATOM   2880 C C      . ASN B 1 84  ? -20.270 -1.576  -9.402  1.00 25.68  ? 423 ASN B C      1 
ATOM   2881 O O      . ASN B 1 84  ? -19.960 -0.607  -10.108 1.00 25.59  ? 423 ASN B O      1 
ATOM   2882 C CB     . ASN B 1 84  ? -21.938 -3.475  -8.974  1.00 29.98  ? 423 ASN B CB     1 
ATOM   2883 C CG     . ASN B 1 84  ? -23.403 -3.876  -9.005  1.00 32.61  ? 423 ASN B CG     1 
ATOM   2884 O OD1    . ASN B 1 84  ? -24.145 -3.635  -8.052  1.00 32.14  ? 423 ASN B OD1    1 
ATOM   2885 N ND2    . ASN B 1 84  ? -23.820 -4.515  -10.094 1.00 31.16  ? 423 ASN B ND2    1 
ATOM   2886 N N      . SER B 1 85  ? -19.365 -2.293  -8.745  1.00 22.12  ? 424 SER B N      1 
ATOM   2887 C CA     . SER B 1 85  ? -17.949 -1.969  -8.731  1.00 25.69  ? 424 SER B CA     1 
ATOM   2888 C C      . SER B 1 85  ? -17.188 -2.929  -9.633  1.00 26.62  ? 424 SER B C      1 
ATOM   2889 O O      . SER B 1 85  ? -17.669 -4.014  -9.975  1.00 27.71  ? 424 SER B O      1 
ATOM   2890 C CB     . SER B 1 85  ? -17.385 -2.034  -7.306  1.00 23.65  ? 424 SER B CB     1 
ATOM   2891 O OG     . SER B 1 85  ? -17.084 -3.369  -6.929  1.00 24.71  ? 424 SER B OG     1 
ATOM   2892 N N      . LEU B 1 86  ? -15.984 -2.505  -10.022 1.00 22.31  ? 425 LEU B N      1 
ATOM   2893 C CA     . LEU B 1 86  ? -15.103 -3.385  -10.778 1.00 21.97  ? 425 LEU B CA     1 
ATOM   2894 C C      . LEU B 1 86  ? -14.803 -4.654  -9.993  1.00 24.65  ? 425 LEU B C      1 
ATOM   2895 O O      . LEU B 1 86  ? -14.695 -5.741  -10.572 1.00 24.68  ? 425 LEU B O      1 
ATOM   2896 C CB     . LEU B 1 86  ? -13.811 -2.650  -11.134 1.00 24.47  ? 425 LEU B CB     1 
ATOM   2897 C CG     . LEU B 1 86  ? -12.776 -3.451  -11.923 1.00 25.23  ? 425 LEU B CG     1 
ATOM   2898 C CD1    . LEU B 1 86  ? -13.363 -3.920  -13.243 1.00 21.85  ? 425 LEU B CD1    1 
ATOM   2899 C CD2    . LEU B 1 86  ? -11.512 -2.635  -12.157 1.00 17.82  ? 425 LEU B CD2    1 
ATOM   2900 N N      . ASP B 1 87  ? -14.676 -4.536  -8.669  1.00 24.96  ? 426 ASP B N      1 
ATOM   2901 C CA     . ASP B 1 87  ? -14.432 -5.710  -7.838  1.00 24.81  ? 426 ASP B CA     1 
ATOM   2902 C C      . ASP B 1 87  ? -15.552 -6.733  -7.987  1.00 28.78  ? 426 ASP B C      1 
ATOM   2903 O O      . ASP B 1 87  ? -15.296 -7.940  -8.054  1.00 36.78  ? 426 ASP B O      1 
ATOM   2904 C CB     . ASP B 1 87  ? -14.275 -5.286  -6.377  1.00 23.89  ? 426 ASP B CB     1 
ATOM   2905 C CG     . ASP B 1 87  ? -13.698 -6.383  -5.509  1.00 26.50  ? 426 ASP B CG     1 
ATOM   2906 O OD1    . ASP B 1 87  ? -14.351 -7.436  -5.359  1.00 34.21  ? 426 ASP B OD1    1 
ATOM   2907 O OD2    . ASP B 1 87  ? -12.584 -6.191  -4.980  1.00 31.95  ? 426 ASP B OD2    1 
ATOM   2908 N N      . ASP B 1 88  ? -16.803 -6.268  -8.049  1.00 28.85  ? 427 ASP B N      1 
ATOM   2909 C CA     . ASP B 1 88  ? -17.936 -7.185  -8.150  1.00 31.51  ? 427 ASP B CA     1 
ATOM   2910 C C      . ASP B 1 88  ? -17.929 -7.957  -9.463  1.00 29.26  ? 427 ASP B C      1 
ATOM   2911 O O      . ASP B 1 88  ? -18.422 -9.090  -9.516  1.00 30.15  ? 427 ASP B O      1 
ATOM   2912 C CB     . ASP B 1 88  ? -19.246 -6.411  -8.001  1.00 28.78  ? 427 ASP B CB     1 
ATOM   2913 C CG     . ASP B 1 88  ? -19.334 -5.669  -6.686  1.00 31.05  ? 427 ASP B CG     1 
ATOM   2914 O OD1    . ASP B 1 88  ? -19.014 -6.277  -5.642  1.00 32.32  ? 427 ASP B OD1    1 
ATOM   2915 O OD2    . ASP B 1 88  ? -19.713 -4.478  -6.697  1.00 32.11  ? 427 ASP B OD2    1 
ATOM   2916 N N      . TRP B 1 89  ? -17.384 -7.370  -10.527 1.00 28.62  ? 428 TRP B N      1 
ATOM   2917 C CA     . TRP B 1 89  ? -17.382 -8.019  -11.831 1.00 25.70  ? 428 TRP B CA     1 
ATOM   2918 C C      . TRP B 1 89  ? -16.153 -8.880  -12.070 1.00 25.76  ? 428 TRP B C      1 
ATOM   2919 O O      . TRP B 1 89  ? -16.166 -9.707  -12.989 1.00 33.08  ? 428 TRP B O      1 
ATOM   2920 C CB     . TRP B 1 89  ? -17.497 -6.971  -12.943 1.00 26.76  ? 428 TRP B CB     1 
ATOM   2921 C CG     . TRP B 1 89  ? -18.901 -6.505  -13.148 1.00 25.83  ? 428 TRP B CG     1 
ATOM   2922 C CD1    . TRP B 1 89  ? -19.550 -5.529  -12.453 1.00 28.04  ? 428 TRP B CD1    1 
ATOM   2923 C CD2    . TRP B 1 89  ? -19.840 -7.009  -14.104 1.00 29.62  ? 428 TRP B CD2    1 
ATOM   2924 N NE1    . TRP B 1 89  ? -20.836 -5.391  -12.920 1.00 27.59  ? 428 TRP B NE1    1 
ATOM   2925 C CE2    . TRP B 1 89  ? -21.038 -6.289  -13.934 1.00 28.28  ? 428 TRP B CE2    1 
ATOM   2926 C CE3    . TRP B 1 89  ? -19.782 -7.999  -15.089 1.00 32.11  ? 428 TRP B CE3    1 
ATOM   2927 C CZ2    . TRP B 1 89  ? -22.168 -6.529  -14.711 1.00 30.67  ? 428 TRP B CZ2    1 
ATOM   2928 C CZ3    . TRP B 1 89  ? -20.902 -8.232  -15.861 1.00 34.13  ? 428 TRP B CZ3    1 
ATOM   2929 C CH2    . TRP B 1 89  ? -22.079 -7.501  -15.669 1.00 31.85  ? 428 TRP B CH2    1 
ATOM   2930 N N      . LEU B 1 90  ? -15.103 -8.713  -11.270 1.00 25.48  ? 429 LEU B N      1 
ATOM   2931 C CA     . LEU B 1 90  ? -13.877 -9.482  -11.430 1.00 24.94  ? 429 LEU B CA     1 
ATOM   2932 C C      . LEU B 1 90  ? -13.788 -10.680 -10.498 1.00 26.47  ? 429 LEU B C      1 
ATOM   2933 O O      . LEU B 1 90  ? -13.259 -11.721 -10.900 1.00 28.15  ? 429 LEU B O      1 
ATOM   2934 C CB     . LEU B 1 90  ? -12.655 -8.586  -11.200 1.00 23.66  ? 429 LEU B CB     1 
ATOM   2935 C CG     . LEU B 1 90  ? -12.387 -7.510  -12.252 1.00 22.23  ? 429 LEU B CG     1 
ATOM   2936 C CD1    . LEU B 1 90  ? -11.315 -6.551  -11.766 1.00 22.99  ? 429 LEU B CD1    1 
ATOM   2937 C CD2    . LEU B 1 90  ? -11.982 -8.143  -13.575 1.00 24.39  ? 429 LEU B CD2    1 
ATOM   2938 N N      . HIS B 1 91  ? -14.296 -10.566 -9.271  1.00 27.91  ? 430 HIS B N      1 
ATOM   2939 C CA     . HIS B 1 91  ? -14.121 -11.604 -8.267  1.00 29.18  ? 430 HIS B CA     1 
ATOM   2940 C C      . HIS B 1 91  ? -15.417 -12.274 -7.832  1.00 45.89  ? 430 HIS B C      1 
ATOM   2941 O O      . HIS B 1 91  ? -15.358 -13.319 -7.173  1.00 53.53  ? 430 HIS B O      1 
ATOM   2942 C CB     . HIS B 1 91  ? -13.412 -11.027 -7.033  1.00 27.59  ? 430 HIS B CB     1 
ATOM   2943 C CG     . HIS B 1 91  ? -12.212 -10.196 -7.365  1.00 30.19  ? 430 HIS B CG     1 
ATOM   2944 N ND1    . HIS B 1 91  ? -12.196 -8.824  -7.232  1.00 34.89  ? 430 HIS B ND1    1 
ATOM   2945 C CD2    . HIS B 1 91  ? -10.992 -10.542 -7.839  1.00 25.97  ? 430 HIS B CD2    1 
ATOM   2946 C CE1    . HIS B 1 91  ? -11.015 -8.362  -7.602  1.00 28.68  ? 430 HIS B CE1    1 
ATOM   2947 N NE2    . HIS B 1 91  ? -10.265 -9.384  -7.974  1.00 24.19  ? 430 HIS B NE2    1 
ATOM   2948 N N      . SER B 1 92  ? -16.574 -11.715 -8.171  1.00 46.72  ? 431 SER B N      1 
ATOM   2949 C CA     . SER B 1 92  ? -17.846 -12.344 -7.836  1.00 60.95  ? 431 SER B CA     1 
ATOM   2950 C C      . SER B 1 92  ? -18.472 -12.983 -9.072  1.00 52.19  ? 431 SER B C      1 
ATOM   2951 O O      . SER B 1 92  ? -17.791 -13.663 -9.839  1.00 51.77  ? 431 SER B O      1 
ATOM   2952 C CB     . SER B 1 92  ? -18.810 -11.327 -7.220  1.00 63.08  ? 431 SER B CB     1 
ATOM   2953 O OG     . SER B 1 92  ? -18.320 -10.848 -5.980  1.00 64.76  ? 431 SER B OG     1 
ATOM   2954 N N      . MET B 1 104 ? -20.337 -13.584 -19.987 1.00 55.96  ? 443 MET B N      1 
ATOM   2955 C CA     . MET B 1 104 ? -20.943 -12.747 -18.958 1.00 65.97  ? 443 MET B CA     1 
ATOM   2956 C C      . MET B 1 104 ? -19.885 -11.919 -18.235 1.00 65.32  ? 443 MET B C      1 
ATOM   2957 O O      . MET B 1 104 ? -20.150 -10.797 -17.802 1.00 58.58  ? 443 MET B O      1 
ATOM   2958 C CB     . MET B 1 104 ? -21.717 -13.605 -17.956 1.00 66.76  ? 443 MET B CB     1 
ATOM   2959 C CG     . MET B 1 104 ? -22.546 -12.807 -16.967 1.00 71.52  ? 443 MET B CG     1 
ATOM   2960 S SD     . MET B 1 104 ? -23.454 -13.864 -15.823 1.00 111.84 ? 443 MET B SD     1 
ATOM   2961 C CE     . MET B 1 104 ? -24.604 -12.686 -15.114 1.00 81.88  ? 443 MET B CE     1 
ATOM   2962 N N      . CYS B 1 105 ? -18.685 -12.481 -18.107 1.00 62.11  ? 444 CYS B N      1 
ATOM   2963 C CA     . CYS B 1 105 ? -17.585 -11.771 -17.474 1.00 53.99  ? 444 CYS B CA     1 
ATOM   2964 C C      . CYS B 1 105 ? -17.184 -10.564 -18.320 1.00 51.21  ? 444 CYS B C      1 
ATOM   2965 O O      . CYS B 1 105 ? -17.741 -10.300 -19.390 1.00 51.36  ? 444 CYS B O      1 
ATOM   2966 C CB     . CYS B 1 105 ? -16.396 -12.706 -17.266 1.00 53.96  ? 444 CYS B CB     1 
ATOM   2967 S SG     . CYS B 1 105 ? -16.708 -14.079 -16.134 1.00 54.00  ? 444 CYS B SG     1 
ATOM   2968 N N      . LEU B 1 106 ? -16.199 -9.819  -17.828 1.00 39.20  ? 445 LEU B N      1 
ATOM   2969 C CA     . LEU B 1 106 ? -15.679 -8.674  -18.561 1.00 36.48  ? 445 LEU B CA     1 
ATOM   2970 C C      . LEU B 1 106 ? -14.762 -9.148  -19.681 1.00 31.38  ? 445 LEU B C      1 
ATOM   2971 O O      . LEU B 1 106 ? -13.916 -10.023 -19.476 1.00 30.09  ? 445 LEU B O      1 
ATOM   2972 C CB     . LEU B 1 106 ? -14.932 -7.730  -17.619 1.00 30.30  ? 445 LEU B CB     1 
ATOM   2973 C CG     . LEU B 1 106 ? -15.812 -6.915  -16.669 1.00 29.75  ? 445 LEU B CG     1 
ATOM   2974 C CD1    . LEU B 1 106 ? -14.968 -6.141  -15.671 1.00 25.40  ? 445 LEU B CD1    1 
ATOM   2975 C CD2    . LEU B 1 106 ? -16.711 -5.973  -17.459 1.00 29.45  ? 445 LEU B CD2    1 
ATOM   2976 N N      . SER B 1 107 ? -14.941 -8.574  -20.867 1.00 30.12  ? 446 SER B N      1 
ATOM   2977 C CA     . SER B 1 107 ? -14.111 -8.914  -22.009 1.00 29.31  ? 446 SER B CA     1 
ATOM   2978 C C      . SER B 1 107 ? -12.749 -8.233  -21.897 1.00 27.36  ? 446 SER B C      1 
ATOM   2979 O O      . SER B 1 107 ? -12.529 -7.350  -21.064 1.00 25.68  ? 446 SER B O      1 
ATOM   2980 C CB     . SER B 1 107 ? -14.798 -8.507  -23.311 1.00 30.82  ? 446 SER B CB     1 
ATOM   2981 O OG     . SER B 1 107 ? -14.918 -7.096  -23.401 1.00 29.71  ? 446 SER B OG     1 
ATOM   2982 N N      . TRP B 1 108 ? -11.822 -8.655  -22.759 1.00 23.76  ? 447 TRP B N      1 
ATOM   2983 C CA     . TRP B 1 108 ? -10.519 -8.000  -22.804 1.00 22.59  ? 447 TRP B CA     1 
ATOM   2984 C C      . TRP B 1 108 ? -10.661 -6.520  -23.136 1.00 21.48  ? 447 TRP B C      1 
ATOM   2985 O O      . TRP B 1 108 ? -10.004 -5.671  -22.522 1.00 20.87  ? 447 TRP B O      1 
ATOM   2986 C CB     . TRP B 1 108 ? -9.612  -8.689  -23.822 1.00 23.62  ? 447 TRP B CB     1 
ATOM   2987 C CG     . TRP B 1 108 ? -8.389  -7.886  -24.131 1.00 22.06  ? 447 TRP B CG     1 
ATOM   2988 C CD1    . TRP B 1 108 ? -8.177  -7.105  -25.228 1.00 24.18  ? 447 TRP B CD1    1 
ATOM   2989 C CD2    . TRP B 1 108 ? -7.217  -7.765  -23.319 1.00 19.68  ? 447 TRP B CD2    1 
ATOM   2990 N NE1    . TRP B 1 108 ? -6.940  -6.512  -25.154 1.00 27.69  ? 447 TRP B NE1    1 
ATOM   2991 C CE2    . TRP B 1 108 ? -6.331  -6.901  -23.990 1.00 24.77  ? 447 TRP B CE2    1 
ATOM   2992 C CE3    . TRP B 1 108 ? -6.830  -8.307  -22.091 1.00 20.07  ? 447 TRP B CE3    1 
ATOM   2993 C CZ2    . TRP B 1 108 ? -5.080  -6.567  -23.476 1.00 23.98  ? 447 TRP B CZ2    1 
ATOM   2994 C CZ3    . TRP B 1 108 ? -5.589  -7.974  -21.581 1.00 23.94  ? 447 TRP B CZ3    1 
ATOM   2995 C CH2    . TRP B 1 108 ? -4.729  -7.112  -22.273 1.00 24.38  ? 447 TRP B CH2    1 
ATOM   2996 N N      . PHE B 1 109 ? -11.520 -6.192  -24.104 1.00 22.38  ? 448 PHE B N      1 
ATOM   2997 C CA     . PHE B 1 109 ? -11.668 -4.805  -24.530 1.00 23.36  ? 448 PHE B CA     1 
ATOM   2998 C C      . PHE B 1 109 ? -12.265 -3.945  -23.424 1.00 21.80  ? 448 PHE B C      1 
ATOM   2999 O O      . PHE B 1 109 ? -11.825 -2.810  -23.208 1.00 23.96  ? 448 PHE B O      1 
ATOM   3000 C CB     . PHE B 1 109 ? -12.527 -4.739  -25.793 1.00 26.44  ? 448 PHE B CB     1 
ATOM   3001 C CG     . PHE B 1 109 ? -12.492 -3.405  -26.484 1.00 33.13  ? 448 PHE B CG     1 
ATOM   3002 C CD1    . PHE B 1 109 ? -11.344 -2.977  -27.134 1.00 33.22  ? 448 PHE B CD1    1 
ATOM   3003 C CD2    . PHE B 1 109 ? -13.610 -2.586  -26.497 1.00 37.47  ? 448 PHE B CD2    1 
ATOM   3004 C CE1    . PHE B 1 109 ? -11.310 -1.753  -27.776 1.00 35.03  ? 448 PHE B CE1    1 
ATOM   3005 C CE2    . PHE B 1 109 ? -13.583 -1.361  -27.138 1.00 35.82  ? 448 PHE B CE2    1 
ATOM   3006 C CZ     . PHE B 1 109 ? -12.431 -0.943  -27.778 1.00 37.45  ? 448 PHE B CZ     1 
ATOM   3007 N N      . GLN B 1 110 ? -13.268 -4.467  -22.711 1.00 22.00  ? 449 GLN B N      1 
ATOM   3008 C CA     . GLN B 1 110 ? -13.866 -3.706  -21.618 1.00 22.32  ? 449 GLN B CA     1 
ATOM   3009 C C      . GLN B 1 110 ? -12.847 -3.417  -20.525 1.00 20.83  ? 449 GLN B C      1 
ATOM   3010 O O      . GLN B 1 110 ? -12.834 -2.322  -19.950 1.00 24.03  ? 449 GLN B O      1 
ATOM   3011 C CB     . GLN B 1 110 ? -15.063 -4.460  -21.044 1.00 22.90  ? 449 GLN B CB     1 
ATOM   3012 C CG     . GLN B 1 110 ? -16.223 -4.605  -22.008 1.00 24.23  ? 449 GLN B CG     1 
ATOM   3013 C CD     . GLN B 1 110 ? -17.345 -5.447  -21.441 1.00 25.12  ? 449 GLN B CD     1 
ATOM   3014 O OE1    . GLN B 1 110 ? -17.104 -6.471  -20.801 1.00 25.05  ? 449 GLN B OE1    1 
ATOM   3015 N NE2    . GLN B 1 110 ? -18.581 -5.016  -21.667 1.00 28.83  ? 449 GLN B NE2    1 
ATOM   3016 N N      . ARG B 1 111 ? -11.983 -4.388  -20.224 1.00 20.53  ? 450 ARG B N      1 
ATOM   3017 C CA     . ARG B 1 111 ? -10.987 -4.194  -19.177 1.00 18.31  ? 450 ARG B CA     1 
ATOM   3018 C C      . ARG B 1 111 ? -9.968  -3.135  -19.580 1.00 18.53  ? 450 ARG B C      1 
ATOM   3019 O O      . ARG B 1 111 ? -9.636  -2.246  -18.788 1.00 22.84  ? 450 ARG B O      1 
ATOM   3020 C CB     . ARG B 1 111 ? -10.305 -5.524  -18.863 1.00 19.07  ? 450 ARG B CB     1 
ATOM   3021 C CG     . ARG B 1 111 ? -11.294 -6.640  -18.606 1.00 19.31  ? 450 ARG B CG     1 
ATOM   3022 C CD     . ARG B 1 111 ? -10.611 -7.936  -18.241 1.00 20.38  ? 450 ARG B CD     1 
ATOM   3023 N NE     . ARG B 1 111 ? -11.584 -8.980  -17.943 1.00 24.66  ? 450 ARG B NE     1 
ATOM   3024 C CZ     . ARG B 1 111 ? -11.316 -10.077 -17.249 1.00 25.42  ? 450 ARG B CZ     1 
ATOM   3025 N NH1    . ARG B 1 111 ? -10.111 -10.302 -16.752 1.00 24.98  ? 450 ARG B NH1    1 
ATOM   3026 N NH2    . ARG B 1 111 ? -12.283 -10.965 -17.040 1.00 26.46  ? 450 ARG B NH2    1 
ATOM   3027 N N      . VAL B 1 112 ? -9.461  -3.213  -20.812 1.00 19.09  ? 451 VAL B N      1 
ATOM   3028 C CA     . VAL B 1 112 ? -8.585  -2.158  -21.318 1.00 19.50  ? 451 VAL B CA     1 
ATOM   3029 C C      . VAL B 1 112 ? -9.268  -0.804  -21.179 1.00 21.47  ? 451 VAL B C      1 
ATOM   3030 O O      . VAL B 1 112 ? -8.687  0.161   -20.670 1.00 20.74  ? 451 VAL B O      1 
ATOM   3031 C CB     . VAL B 1 112 ? -8.187  -2.440  -22.778 1.00 18.76  ? 451 VAL B CB     1 
ATOM   3032 C CG1    . VAL B 1 112 ? -7.239  -1.364  -23.285 1.00 20.98  ? 451 VAL B CG1    1 
ATOM   3033 C CG2    . VAL B 1 112 ? -7.560  -3.819  -22.908 1.00 18.19  ? 451 VAL B CG2    1 
ATOM   3034 N N      . GLN B 1 113 ? -10.526 -0.721  -21.619 1.00 22.65  ? 452 GLN B N      1 
ATOM   3035 C CA     . GLN B 1 113 ? -11.251 0.543   -21.545 1.00 21.22  ? 452 GLN B CA     1 
ATOM   3036 C C      . GLN B 1 113 ? -11.393 1.018   -20.104 1.00 22.06  ? 452 GLN B C      1 
ATOM   3037 O O      . GLN B 1 113 ? -11.202 2.205   -19.814 1.00 26.68  ? 452 GLN B O      1 
ATOM   3038 C CB     . GLN B 1 113 ? -12.623 0.403   -22.202 1.00 25.07  ? 452 GLN B CB     1 
ATOM   3039 C CG     . GLN B 1 113 ? -13.429 1.692   -22.210 1.00 31.00  ? 452 GLN B CG     1 
ATOM   3040 C CD     . GLN B 1 113 ? -14.723 1.568   -22.989 1.00 48.93  ? 452 GLN B CD     1 
ATOM   3041 O OE1    . GLN B 1 113 ? -15.562 0.717   -22.691 1.00 56.44  ? 452 GLN B OE1    1 
ATOM   3042 N NE2    . GLN B 1 113 ? -14.889 2.416   -23.999 1.00 45.79  ? 452 GLN B NE2    1 
ATOM   3043 N N      . ILE B 1 114 ? -11.727 0.109   -19.186 1.00 19.24  ? 453 ILE B N      1 
ATOM   3044 C CA     . ILE B 1 114 ? -11.864 0.494   -17.783 1.00 18.54  ? 453 ILE B CA     1 
ATOM   3045 C C      . ILE B 1 114 ? -10.555 1.077   -17.266 1.00 21.51  ? 453 ILE B C      1 
ATOM   3046 O O      . ILE B 1 114 ? -10.532 2.145   -16.642 1.00 25.50  ? 453 ILE B O      1 
ATOM   3047 C CB     . ILE B 1 114 ? -12.326 -0.705  -16.937 1.00 16.41  ? 453 ILE B CB     1 
ATOM   3048 C CG1    . ILE B 1 114 ? -13.777 -1.059  -17.272 1.00 18.98  ? 453 ILE B CG1    1 
ATOM   3049 C CG2    . ILE B 1 114 ? -12.171 -0.404  -15.456 1.00 18.07  ? 453 ILE B CG2    1 
ATOM   3050 C CD1    . ILE B 1 114 ? -14.278 -2.313  -16.589 1.00 20.98  ? 453 ILE B CD1    1 
ATOM   3051 N N      . ALA B 1 115 ? -9.442  0.385   -17.522 1.00 18.32  ? 454 ALA B N      1 
ATOM   3052 C CA     . ALA B 1 115 ? -8.138  0.923   -17.147 1.00 20.04  ? 454 ALA B CA     1 
ATOM   3053 C C      . ALA B 1 115 ? -7.878  2.255   -17.838 1.00 20.82  ? 454 ALA B C      1 
ATOM   3054 O O      . ALA B 1 115 ? -7.334  3.185   -17.230 1.00 23.55  ? 454 ALA B O      1 
ATOM   3055 C CB     . ALA B 1 115 ? -7.037  -0.083  -17.482 1.00 19.48  ? 454 ALA B CB     1 
ATOM   3056 N N      . HIS B 1 116 ? -8.257  2.363   -19.114 1.00 19.90  ? 455 HIS B N      1 
ATOM   3057 C CA     . HIS B 1 116 ? -8.146  3.635   -19.820 1.00 20.44  ? 455 HIS B CA     1 
ATOM   3058 C C      . HIS B 1 116 ? -8.943  4.724   -19.114 1.00 18.06  ? 455 HIS B C      1 
ATOM   3059 O O      . HIS B 1 116 ? -8.465  5.855   -18.962 1.00 19.50  ? 455 HIS B O      1 
ATOM   3060 C CB     . HIS B 1 116 ? -8.617  3.464   -21.265 1.00 21.64  ? 455 HIS B CB     1 
ATOM   3061 C CG     . HIS B 1 116 ? -8.571  4.722   -22.077 1.00 23.72  ? 455 HIS B CG     1 
ATOM   3062 N ND1    . HIS B 1 116 ? -7.486  5.068   -22.854 1.00 24.67  ? 455 HIS B ND1    1 
ATOM   3063 C CD2    . HIS B 1 116 ? -9.485  5.707   -22.248 1.00 27.39  ? 455 HIS B CD2    1 
ATOM   3064 C CE1    . HIS B 1 116 ? -7.731  6.215   -23.462 1.00 21.24  ? 455 HIS B CE1    1 
ATOM   3065 N NE2    . HIS B 1 116 ? -8.936  6.625   -23.110 1.00 26.01  ? 455 HIS B NE2    1 
ATOM   3066 N N      . ASP B 1 117 ? -10.157 4.400   -18.665 1.00 20.30  ? 456 ASP B N      1 
ATOM   3067 C CA     . ASP B 1 117 ? -10.988 5.390   -17.986 1.00 22.37  ? 456 ASP B CA     1 
ATOM   3068 C C      . ASP B 1 117 ? -10.366 5.819   -16.664 1.00 17.69  ? 456 ASP B C      1 
ATOM   3069 O O      . ASP B 1 117 ? -10.311 7.014   -16.350 1.00 18.32  ? 456 ASP B O      1 
ATOM   3070 C CB     . ASP B 1 117 ? -12.395 4.834   -17.760 1.00 22.80  ? 456 ASP B CB     1 
ATOM   3071 C CG     . ASP B 1 117 ? -13.136 4.577   -19.057 1.00 23.68  ? 456 ASP B CG     1 
ATOM   3072 O OD1    . ASP B 1 117 ? -12.806 5.227   -20.071 1.00 21.86  ? 456 ASP B OD1    1 
ATOM   3073 O OD2    . ASP B 1 117 ? -14.053 3.728   -19.058 1.00 28.03  ? 456 ASP B OD2    1 
ATOM   3074 N N      . VAL B 1 118 ? -9.900  4.855   -15.868 1.00 14.20  ? 457 VAL B N      1 
ATOM   3075 C CA     . VAL B 1 118 ? -9.294  5.190   -14.584 1.00 20.71  ? 457 VAL B CA     1 
ATOM   3076 C C      . VAL B 1 118 ? -7.978  5.935   -14.779 1.00 22.61  ? 457 VAL B C      1 
ATOM   3077 O O      . VAL B 1 118 ? -7.640  6.828   -13.992 1.00 17.42  ? 457 VAL B O      1 
ATOM   3078 C CB     . VAL B 1 118 ? -9.106  3.919   -13.736 1.00 21.89  ? 457 VAL B CB     1 
ATOM   3079 C CG1    . VAL B 1 118 ? -8.360  4.245   -12.453 1.00 21.62  ? 457 VAL B CG1    1 
ATOM   3080 C CG2    . VAL B 1 118 ? -10.455 3.284   -13.424 1.00 21.18  ? 457 VAL B CG2    1 
ATOM   3081 N N      . ALA B 1 119 ? -7.212  5.589   -15.818 1.00 15.60  ? 458 ALA B N      1 
ATOM   3082 C CA     . ALA B 1 119 ? -6.000  6.342   -16.119 1.00 16.98  ? 458 ALA B CA     1 
ATOM   3083 C C      . ALA B 1 119 ? -6.332  7.770   -16.530 1.00 20.35  ? 458 ALA B C      1 
ATOM   3084 O O      . ALA B 1 119 ? -5.629  8.713   -16.148 1.00 20.55  ? 458 ALA B O      1 
ATOM   3085 C CB     . ALA B 1 119 ? -5.200  5.639   -17.215 1.00 19.73  ? 458 ALA B CB     1 
ATOM   3086 N N      . ASP B 1 120 ? -7.396  7.944   -17.316 1.00 19.73  ? 459 ASP B N      1 
ATOM   3087 C CA     . ASP B 1 120 ? -7.842  9.283   -17.685 1.00 19.41  ? 459 ASP B CA     1 
ATOM   3088 C C      . ASP B 1 120 ? -8.150  10.112  -16.444 1.00 21.63  ? 459 ASP B C      1 
ATOM   3089 O O      . ASP B 1 120 ? -7.656  11.236  -16.293 1.00 21.09  ? 459 ASP B O      1 
ATOM   3090 C CB     . ASP B 1 120 ? -9.070  9.183   -18.592 1.00 23.20  ? 459 ASP B CB     1 
ATOM   3091 C CG     . ASP B 1 120 ? -9.361  10.474  -19.335 1.00 22.87  ? 459 ASP B CG     1 
ATOM   3092 O OD1    . ASP B 1 120 ? -8.615  11.458  -19.153 1.00 24.89  ? 459 ASP B OD1    1 
ATOM   3093 O OD2    . ASP B 1 120 ? -10.339 10.500  -20.110 1.00 25.55  ? 459 ASP B OD2    1 
ATOM   3094 N N      . ALA B 1 121 ? -8.955  9.560   -15.532 1.00 20.95  ? 460 ALA B N      1 
ATOM   3095 C CA     . ALA B 1 121 ? -9.341  10.298  -14.333 1.00 19.13  ? 460 ALA B CA     1 
ATOM   3096 C C      . ALA B 1 121 ? -8.130  10.638  -13.474 1.00 19.09  ? 460 ALA B C      1 
ATOM   3097 O O      . ALA B 1 121 ? -8.067  11.719  -12.878 1.00 20.89  ? 460 ALA B O      1 
ATOM   3098 C CB     . ALA B 1 121 ? -10.360 9.493   -13.528 1.00 21.28  ? 460 ALA B CB     1 
ATOM   3099 N N      . LEU B 1 122 ? -7.160  9.724   -13.390 1.00 23.49  ? 461 LEU B N      1 
ATOM   3100 C CA     . LEU B 1 122 ? -5.958  10.000  -12.609 1.00 21.71  ? 461 LEU B CA     1 
ATOM   3101 C C      . LEU B 1 122 ? -5.103  11.069  -13.276 1.00 21.97  ? 461 LEU B C      1 
ATOM   3102 O O      . LEU B 1 122 ? -4.514  11.917  -12.594 1.00 21.47  ? 461 LEU B O      1 
ATOM   3103 C CB     . LEU B 1 122 ? -5.157  8.714   -12.407 1.00 15.43  ? 461 LEU B CB     1 
ATOM   3104 C CG     . LEU B 1 122 ? -5.879  7.616   -11.624 1.00 15.80  ? 461 LEU B CG     1 
ATOM   3105 C CD1    . LEU B 1 122 ? -4.992  6.391   -11.472 1.00 15.65  ? 461 LEU B CD1    1 
ATOM   3106 C CD2    . LEU B 1 122 ? -6.322  8.131   -10.265 1.00 19.38  ? 461 LEU B CD2    1 
ATOM   3107 N N      . ASN B 1 123 ? -5.021  11.044  -14.609 1.00 22.26  ? 462 ASN B N      1 
ATOM   3108 C CA     . ASN B 1 123 ? -4.322  12.105  -15.325 1.00 22.37  ? 462 ASN B CA     1 
ATOM   3109 C C      . ASN B 1 123 ? -4.927  13.465  -15.001 1.00 22.21  ? 462 ASN B C      1 
ATOM   3110 O O      . ASN B 1 123 ? -4.202  14.437  -14.759 1.00 22.10  ? 462 ASN B O      1 
ATOM   3111 C CB     . ASN B 1 123 ? -4.371  11.836  -16.830 1.00 22.85  ? 462 ASN B CB     1 
ATOM   3112 C CG     . ASN B 1 123 ? -3.332  12.626  -17.601 1.00 22.81  ? 462 ASN B CG     1 
ATOM   3113 O OD1    . ASN B 1 123 ? -2.177  12.723  -17.190 1.00 27.76  ? 462 ASN B OD1    1 
ATOM   3114 N ND2    . ASN B 1 123 ? -3.741  13.198  -18.727 1.00 21.69  ? 462 ASN B ND2    1 
ATOM   3115 N N      . TYR B 1 124 ? -6.258  13.547  -14.986 1.00 23.10  ? 463 TYR B N      1 
ATOM   3116 C CA     . TYR B 1 124 ? -6.931  14.788  -14.617 1.00 24.08  ? 463 TYR B CA     1 
ATOM   3117 C C      . TYR B 1 124 ? -6.628  15.167  -13.173 1.00 19.27  ? 463 TYR B C      1 
ATOM   3118 O O      . TYR B 1 124 ? -6.244  16.307  -12.884 1.00 21.03  ? 463 TYR B O      1 
ATOM   3119 C CB     . TYR B 1 124 ? -8.438  14.639  -14.841 1.00 22.38  ? 463 TYR B CB     1 
ATOM   3120 C CG     . TYR B 1 124 ? -9.294  15.681  -14.157 1.00 24.53  ? 463 TYR B CG     1 
ATOM   3121 C CD1    . TYR B 1 124 ? -9.489  16.933  -14.726 1.00 22.38  ? 463 TYR B CD1    1 
ATOM   3122 C CD2    . TYR B 1 124 ? -9.927  15.402  -12.950 1.00 23.16  ? 463 TYR B CD2    1 
ATOM   3123 C CE1    . TYR B 1 124 ? -10.280 17.884  -14.106 1.00 21.24  ? 463 TYR B CE1    1 
ATOM   3124 C CE2    . TYR B 1 124 ? -10.718 16.346  -12.324 1.00 22.97  ? 463 TYR B CE2    1 
ATOM   3125 C CZ     . TYR B 1 124 ? -10.892 17.584  -12.906 1.00 23.67  ? 463 TYR B CZ     1 
ATOM   3126 O OH     . TYR B 1 124 ? -11.677 18.528  -12.287 1.00 27.70  ? 463 TYR B OH     1 
ATOM   3127 N N      . LEU B 1 125 ? -6.783  14.214  -12.251 1.00 22.11  ? 464 LEU B N      1 
ATOM   3128 C CA     . LEU B 1 125 ? -6.575  14.506  -10.836 1.00 23.46  ? 464 LEU B CA     1 
ATOM   3129 C C      . LEU B 1 125 ? -5.151  14.974  -10.560 1.00 23.82  ? 464 LEU B C      1 
ATOM   3130 O O      . LEU B 1 125 ? -4.936  15.892  -9.760  1.00 22.61  ? 464 LEU B O      1 
ATOM   3131 C CB     . LEU B 1 125 ? -6.898  13.270  -9.994  1.00 22.34  ? 464 LEU B CB     1 
ATOM   3132 C CG     . LEU B 1 125 ? -8.367  12.970  -9.693  1.00 25.79  ? 464 LEU B CG     1 
ATOM   3133 C CD1    . LEU B 1 125 ? -8.498  11.617  -9.019  1.00 24.06  ? 464 LEU B CD1    1 
ATOM   3134 C CD2    . LEU B 1 125 ? -8.964  14.060  -8.820  1.00 23.44  ? 464 LEU B CD2    1 
ATOM   3135 N N      . HIS B 1 126 ? -4.165  14.357  -11.211 1.00 21.86  ? 465 HIS B N      1 
ATOM   3136 C CA     . HIS B 1 126 ? -2.768  14.595  -10.873 1.00 21.16  ? 465 HIS B CA     1 
ATOM   3137 C C      . HIS B 1 126 ? -2.144  15.767  -11.618 1.00 23.61  ? 465 HIS B C      1 
ATOM   3138 O O      . HIS B 1 126 ? -1.133  16.303  -11.151 1.00 27.18  ? 465 HIS B O      1 
ATOM   3139 C CB     . HIS B 1 126 ? -1.933  13.338  -11.150 1.00 21.10  ? 465 HIS B CB     1 
ATOM   3140 C CG     . HIS B 1 126 ? -2.292  12.168  -10.288 1.00 22.17  ? 465 HIS B CG     1 
ATOM   3141 N ND1    . HIS B 1 126 ? -1.669  10.943  -10.400 1.00 21.29  ? 465 HIS B ND1    1 
ATOM   3142 C CD2    . HIS B 1 126 ? -3.205  12.036  -9.296  1.00 18.89  ? 465 HIS B CD2    1 
ATOM   3143 C CE1    . HIS B 1 126 ? -2.186  10.106  -9.518  1.00 19.68  ? 465 HIS B CE1    1 
ATOM   3144 N NE2    . HIS B 1 126 ? -3.119  10.745  -8.835  1.00 18.41  ? 465 HIS B NE2    1 
ATOM   3145 N N      . ASN B 1 127 ? -2.712  16.184  -12.750 1.00 22.84  ? 466 ASN B N      1 
ATOM   3146 C CA     . ASN B 1 127 ? -1.996  17.100  -13.630 1.00 20.48  ? 466 ASN B CA     1 
ATOM   3147 C C      . ASN B 1 127 ? -2.796  18.342  -14.003 1.00 24.43  ? 466 ASN B C      1 
ATOM   3148 O O      . ASN B 1 127 ? -2.267  19.458  -13.941 1.00 28.48  ? 466 ASN B O      1 
ATOM   3149 C CB     . ASN B 1 127 ? -1.562  16.362  -14.898 1.00 24.60  ? 466 ASN B CB     1 
ATOM   3150 C CG     . ASN B 1 127 ? -0.638  15.196  -14.602 1.00 21.92  ? 466 ASN B CG     1 
ATOM   3151 O OD1    . ASN B 1 127 ? 0.315   15.324  -13.835 1.00 21.01  ? 466 ASN B OD1    1 
ATOM   3152 N ND2    . ASN B 1 127 ? -0.925  14.048  -15.203 1.00 20.10  ? 466 ASN B ND2    1 
ATOM   3153 N N      . TYR B 1 128 ? -4.058  18.177  -14.408 1.00 23.49  ? 467 TYR B N      1 
ATOM   3154 C CA     . TYR B 1 128 ? -4.825  19.315  -14.904 1.00 25.24  ? 467 TYR B CA     1 
ATOM   3155 C C      . TYR B 1 128 ? -6.173  19.453  -14.203 1.00 25.76  ? 467 TYR B C      1 
ATOM   3156 O O      . TYR B 1 128 ? -7.145  19.920  -14.802 1.00 32.41  ? 467 TYR B O      1 
ATOM   3157 C CB     . TYR B 1 128 ? -5.005  19.240  -16.421 1.00 23.16  ? 467 TYR B CB     1 
ATOM   3158 C CG     . TYR B 1 128 ? -5.863  18.106  -16.933 1.00 20.36  ? 467 TYR B CG     1 
ATOM   3159 C CD1    . TYR B 1 128 ? -5.342  16.830  -17.096 1.00 24.12  ? 467 TYR B CD1    1 
ATOM   3160 C CD2    . TYR B 1 128 ? -7.186  18.323  -17.296 1.00 23.17  ? 467 TYR B CD2    1 
ATOM   3161 C CE1    . TYR B 1 128 ? -6.123  15.793  -17.585 1.00 24.35  ? 467 TYR B CE1    1 
ATOM   3162 C CE2    . TYR B 1 128 ? -7.974  17.296  -17.783 1.00 24.25  ? 467 TYR B CE2    1 
ATOM   3163 C CZ     . TYR B 1 128 ? -7.438  16.033  -17.925 1.00 23.93  ? 467 TYR B CZ     1 
ATOM   3164 O OH     . TYR B 1 128 ? -8.220  15.008  -18.409 1.00 31.55  ? 467 TYR B OH     1 
ATOM   3165 N N      . ALA B 1 129 ? -6.244  19.073  -12.932 1.00 22.35  ? 468 ALA B N      1 
ATOM   3166 C CA     . ALA B 1 129 ? -7.373  19.443  -12.092 1.00 23.69  ? 468 ALA B CA     1 
ATOM   3167 C C      . ALA B 1 129 ? -7.025  20.716  -11.335 1.00 27.01  ? 468 ALA B C      1 
ATOM   3168 O O      . ALA B 1 129 ? -5.873  20.918  -10.939 1.00 29.09  ? 468 ALA B O      1 
ATOM   3169 C CB     . ALA B 1 129 ? -7.727  18.325  -11.110 1.00 24.44  ? 468 ALA B CB     1 
ATOM   3170 N N      . ASN B 1 130 ? -8.019  21.579  -11.151 1.00 27.50  ? 469 ASN B N      1 
ATOM   3171 C CA     . ASN B 1 130 ? -7.836  22.831  -10.416 1.00 33.01  ? 469 ASN B CA     1 
ATOM   3172 C C      . ASN B 1 130 ? -8.814  22.876  -9.252  1.00 35.07  ? 469 ASN B C      1 
ATOM   3173 O O      . ASN B 1 130 ? -10.010 23.156  -9.453  1.00 52.52  ? 469 ASN B O      1 
ATOM   3174 C CB     . ASN B 1 130 ? -8.029  24.040  -11.329 1.00 32.53  ? 469 ASN B CB     1 
ATOM   3175 C CG     . ASN B 1 130 ? -7.606  25.340  -10.670 1.00 41.03  ? 469 ASN B CG     1 
ATOM   3176 O OD1    . ASN B 1 130 ? -6.559  25.412  -10.025 1.00 47.77  ? 469 ASN B OD1    1 
ATOM   3177 N ND2    . ASN B 1 130 ? -8.425  26.375  -10.822 1.00 36.38  ? 469 ASN B ND2    1 
ATOM   3178 N N      . PRO B 1 131 ? -8.368  22.601  -8.023  1.00 27.83  ? 470 PRO B N      1 
ATOM   3179 C CA     . PRO B 1 131 ? -7.005  22.213  -7.635  1.00 26.97  ? 470 PRO B CA     1 
ATOM   3180 C C      . PRO B 1 131 ? -6.715  20.741  -7.916  1.00 30.28  ? 470 PRO B C      1 
ATOM   3181 O O      . PRO B 1 131 ? -7.632  19.937  -8.060  1.00 31.86  ? 470 PRO B O      1 
ATOM   3182 C CB     . PRO B 1 131 ? -6.984  22.520  -6.133  1.00 30.68  ? 470 PRO B CB     1 
ATOM   3183 C CG     . PRO B 1 131 ? -8.397  22.263  -5.698  1.00 36.76  ? 470 PRO B CG     1 
ATOM   3184 C CD     . PRO B 1 131 ? -9.253  22.734  -6.852  1.00 39.62  ? 470 PRO B CD     1 
ATOM   3185 N N      . PRO B 1 132 ? -5.442  20.365  -8.000  1.00 30.49  ? 471 PRO B N      1 
ATOM   3186 C CA     . PRO B 1 132 ? -5.085  18.959  -8.198  1.00 27.21  ? 471 PRO B CA     1 
ATOM   3187 C C      . PRO B 1 132 ? -5.014  18.211  -6.874  1.00 29.61  ? 471 PRO B C      1 
ATOM   3188 O O      . PRO B 1 132 ? -4.786  18.788  -5.809  1.00 32.83  ? 471 PRO B O      1 
ATOM   3189 C CB     . PRO B 1 132 ? -3.697  19.037  -8.861  1.00 22.58  ? 471 PRO B CB     1 
ATOM   3190 C CG     . PRO B 1 132 ? -3.310  20.518  -8.863  1.00 29.27  ? 471 PRO B CG     1 
ATOM   3191 C CD     . PRO B 1 132 ? -4.249  21.219  -7.936  1.00 33.75  ? 471 PRO B CD     1 
ATOM   3192 N N      . HIS B 1 133 ? -5.213  16.896  -6.960  1.00 28.26  ? 472 HIS B N      1 
ATOM   3193 C CA     . HIS B 1 133 ? -5.325  16.067  -5.769  1.00 27.72  ? 472 HIS B CA     1 
ATOM   3194 C C      . HIS B 1 133 ? -4.669  14.714  -5.999  1.00 28.41  ? 472 HIS B C      1 
ATOM   3195 O O      . HIS B 1 133 ? -4.309  14.347  -7.121  1.00 26.49  ? 472 HIS B O      1 
ATOM   3196 C CB     . HIS B 1 133 ? -6.790  15.862  -5.364  1.00 33.31  ? 472 HIS B CB     1 
ATOM   3197 C CG     . HIS B 1 133 ? -7.512  17.130  -5.037  1.00 31.66  ? 472 HIS B CG     1 
ATOM   3198 N ND1    . HIS B 1 133 ? -7.298  17.826  -3.867  1.00 31.17  ? 472 HIS B ND1    1 
ATOM   3199 C CD2    . HIS B 1 133 ? -8.453  17.823  -5.721  1.00 29.36  ? 472 HIS B CD2    1 
ATOM   3200 C CE1    . HIS B 1 133 ? -8.071  18.897  -3.847  1.00 36.16  ? 472 HIS B CE1    1 
ATOM   3201 N NE2    . HIS B 1 133 ? -8.782  18.919  -4.960  1.00 34.19  ? 472 HIS B NE2    1 
ATOM   3202 N N      . VAL B 1 134 ? -4.524  13.973  -4.903  1.00 27.49  ? 473 VAL B N      1 
ATOM   3203 C CA     . VAL B 1 134 ? -4.144  12.566  -4.920  1.00 25.51  ? 473 VAL B CA     1 
ATOM   3204 C C      . VAL B 1 134 ? -5.304  11.782  -4.321  1.00 26.69  ? 473 VAL B C      1 
ATOM   3205 O O      . VAL B 1 134 ? -5.729  12.058  -3.191  1.00 26.16  ? 473 VAL B O      1 
ATOM   3206 C CB     . VAL B 1 134 ? -2.843  12.312  -4.142  1.00 24.94  ? 473 VAL B CB     1 
ATOM   3207 C CG1    . VAL B 1 134 ? -2.595  10.821  -3.994  1.00 24.93  ? 473 VAL B CG1    1 
ATOM   3208 C CG2    . VAL B 1 134 ? -1.669  12.985  -4.837  1.00 24.74  ? 473 VAL B CG2    1 
ATOM   3209 N N      . HIS B 1 135 ? -5.823  10.816  -5.081  1.00 24.58  ? 474 HIS B N      1 
ATOM   3210 C CA     . HIS B 1 135 ? -7.003  10.078  -4.640  1.00 25.16  ? 474 HIS B CA     1 
ATOM   3211 C C      . HIS B 1 135 ? -6.759  9.408   -3.292  1.00 27.64  ? 474 HIS B C      1 
ATOM   3212 O O      . HIS B 1 135 ? -7.515  9.610   -2.335  1.00 29.36  ? 474 HIS B O      1 
ATOM   3213 C CB     . HIS B 1 135 ? -7.400  9.048   -5.698  1.00 28.43  ? 474 HIS B CB     1 
ATOM   3214 C CG     . HIS B 1 135 ? -8.750  8.443   -5.473  1.00 26.07  ? 474 HIS B CG     1 
ATOM   3215 N ND1    . HIS B 1 135 ? -8.981  7.470   -4.526  1.00 22.81  ? 474 HIS B ND1    1 
ATOM   3216 C CD2    . HIS B 1 135 ? -9.941  8.673   -6.075  1.00 28.44  ? 474 HIS B CD2    1 
ATOM   3217 C CE1    . HIS B 1 135 ? -10.256 7.127   -4.553  1.00 25.44  ? 474 HIS B CE1    1 
ATOM   3218 N NE2    . HIS B 1 135 ? -10.861 7.842   -5.485  1.00 25.73  ? 474 HIS B NE2    1 
ATOM   3219 N N      . LYS B 1 136 ? -5.704  8.601   -3.202  1.00 27.94  ? 475 LYS B N      1 
ATOM   3220 C CA     . LYS B 1 136 ? -5.226  7.927   -2.002  1.00 29.33  ? 475 LYS B CA     1 
ATOM   3221 C C      . LYS B 1 136 ? -6.033  6.672   -1.677  1.00 28.05  ? 475 LYS B C      1 
ATOM   3222 O O      . LYS B 1 136 ? -5.611  5.899   -0.816  1.00 28.89  ? 475 LYS B O      1 
ATOM   3223 C CB     . LYS B 1 136 ? -5.212  8.840   -0.759  1.00 30.13  ? 475 LYS B CB     1 
ATOM   3224 C CG     . LYS B 1 136 ? -4.414  10.124  -0.941  1.00 27.85  ? 475 LYS B CG     1 
ATOM   3225 C CD     . LYS B 1 136 ? -4.148  10.805  0.393   1.00 30.14  ? 475 LYS B CD     1 
ATOM   3226 C CE     . LYS B 1 136 ? -5.428  11.334  1.014   1.00 44.58  ? 475 LYS B CE     1 
ATOM   3227 N NZ     . LYS B 1 136 ? -5.280  11.538  2.486   1.00 48.59  ? 475 LYS B NZ     1 
ATOM   3228 N N      . ASN B 1 137 ? -7.167  6.433   -2.329  1.00 24.60  ? 476 ASN B N      1 
ATOM   3229 C CA     . ASN B 1 137 ? -8.022  5.295   -2.008  1.00 21.17  ? 476 ASN B CA     1 
ATOM   3230 C C      . ASN B 1 137 ? -8.547  4.656   -3.290  1.00 25.87  ? 476 ASN B C      1 
ATOM   3231 O O      . ASN B 1 137 ? -9.747  4.437   -3.459  1.00 27.58  ? 476 ASN B O      1 
ATOM   3232 C CB     . ASN B 1 137 ? -9.171  5.727   -1.098  1.00 27.17  ? 476 ASN B CB     1 
ATOM   3233 C CG     . ASN B 1 137 ? -9.855  4.555   -0.422  1.00 28.25  ? 476 ASN B CG     1 
ATOM   3234 O OD1    . ASN B 1 137 ? -9.208  3.583   -0.034  1.00 29.39  ? 476 ASN B OD1    1 
ATOM   3235 N ND2    . ASN B 1 137 ? -11.173 4.644   -0.276  1.00 24.88  ? 476 ASN B ND2    1 
ATOM   3236 N N      . LEU B 1 138 ? -7.641  4.348   -4.215  1.00 21.64  ? 477 LEU B N      1 
ATOM   3237 C CA     . LEU B 1 138 ? -8.011  3.723   -5.478  1.00 21.63  ? 477 LEU B CA     1 
ATOM   3238 C C      . LEU B 1 138 ? -8.030  2.210   -5.305  1.00 20.03  ? 477 LEU B C      1 
ATOM   3239 O O      . LEU B 1 138 ? -7.006  1.603   -4.973  1.00 21.94  ? 477 LEU B O      1 
ATOM   3240 C CB     . LEU B 1 138 ? -7.049  4.123   -6.595  1.00 12.86  ? 477 LEU B CB     1 
ATOM   3241 C CG     . LEU B 1 138 ? -7.432  3.590   -7.978  1.00 18.76  ? 477 LEU B CG     1 
ATOM   3242 C CD1    . LEU B 1 138 ? -8.798  4.116   -8.396  1.00 13.86  ? 477 LEU B CD1    1 
ATOM   3243 C CD2    . LEU B 1 138 ? -6.378  3.942   -9.015  1.00 20.26  ? 477 LEU B CD2    1 
ATOM   3244 N N      . LYS B 1 139 ? -9.194  1.607   -5.530  1.00 19.32  ? 478 LYS B N      1 
ATOM   3245 C CA     . LYS B 1 139 ? -9.369  0.170   -5.397  1.00 21.79  ? 478 LYS B CA     1 
ATOM   3246 C C      . LYS B 1 139 ? -10.501 -0.264  -6.316  1.00 22.43  ? 478 LYS B C      1 
ATOM   3247 O O      . LYS B 1 139 ? -11.417 0.512   -6.600  1.00 23.28  ? 478 LYS B O      1 
ATOM   3248 C CB     . LYS B 1 139 ? -9.672  -0.226  -3.945  1.00 26.51  ? 478 LYS B CB     1 
ATOM   3249 C CG     . LYS B 1 139 ? -8.607  0.205   -2.943  1.00 30.38  ? 478 LYS B CG     1 
ATOM   3250 C CD     . LYS B 1 139 ? -9.020  -0.119  -1.517  1.00 33.77  ? 478 LYS B CD     1 
ATOM   3251 C CE     . LYS B 1 139 ? -7.891  0.158   -0.537  1.00 33.21  ? 478 LYS B CE     1 
ATOM   3252 N NZ     . LYS B 1 139 ? -7.468  1.585   -0.555  1.00 30.95  ? 478 LYS B NZ     1 
ATOM   3253 N N      . SER B 1 140 ? -10.429 -1.514  -6.784  1.00 20.22  ? 479 SER B N      1 
ATOM   3254 C CA     . SER B 1 140 ? -11.473 -2.029  -7.664  1.00 20.05  ? 479 SER B CA     1 
ATOM   3255 C C      . SER B 1 140 ? -12.857 -1.862  -7.048  1.00 23.59  ? 479 SER B C      1 
ATOM   3256 O O      . SER B 1 140 ? -13.831 -1.617  -7.767  1.00 25.05  ? 479 SER B O      1 
ATOM   3257 C CB     . SER B 1 140 ? -11.203 -3.499  -7.997  1.00 18.90  ? 479 SER B CB     1 
ATOM   3258 O OG     . SER B 1 140 ? -11.021 -4.265  -6.819  1.00 24.77  ? 479 SER B OG     1 
ATOM   3259 N N      . GLY B 1 141 ? -12.967 -1.987  -5.723  1.00 22.06  ? 480 GLY B N      1 
ATOM   3260 C CA     . GLY B 1 141 ? -14.239 -1.742  -5.065  1.00 21.72  ? 480 GLY B CA     1 
ATOM   3261 C C      . GLY B 1 141 ? -14.739 -0.319  -5.196  1.00 23.49  ? 480 GLY B C      1 
ATOM   3262 O O      . GLY B 1 141 ? -15.945 -0.084  -5.068  1.00 24.96  ? 480 GLY B O      1 
ATOM   3263 N N      . ASN B 1 142 ? -13.843 0.635   -5.451  1.00 23.86  ? 481 ASN B N      1 
ATOM   3264 C CA     . ASN B 1 142 ? -14.201 2.042   -5.569  1.00 21.56  ? 481 ASN B CA     1 
ATOM   3265 C C      . ASN B 1 142 ? -14.228 2.530   -7.014  1.00 21.23  ? 481 ASN B C      1 
ATOM   3266 O O      . ASN B 1 142 ? -14.409 3.728   -7.248  1.00 22.28  ? 481 ASN B O      1 
ATOM   3267 C CB     . ASN B 1 142 ? -13.236 2.899   -4.744  1.00 22.03  ? 481 ASN B CB     1 
ATOM   3268 C CG     . ASN B 1 142 ? -13.324 2.607   -3.256  1.00 28.35  ? 481 ASN B CG     1 
ATOM   3269 O OD1    . ASN B 1 142 ? -14.328 2.082   -2.774  1.00 37.02  ? 481 ASN B OD1    1 
ATOM   3270 N ND2    . ASN B 1 142 ? -12.272 2.948   -2.520  1.00 26.17  ? 481 ASN B ND2    1 
ATOM   3271 N N      . ILE B 1 143 ? -14.042 1.636   -7.979  1.00 21.06  ? 482 ILE B N      1 
ATOM   3272 C CA     . ILE B 1 143 ? -14.169 1.967   -9.398  1.00 23.74  ? 482 ILE B CA     1 
ATOM   3273 C C      . ILE B 1 143 ? -15.554 1.487   -9.818  1.00 22.95  ? 482 ILE B C      1 
ATOM   3274 O O      . ILE B 1 143 ? -15.755 0.328   -10.188 1.00 22.60  ? 482 ILE B O      1 
ATOM   3275 C CB     . ILE B 1 143 ? -13.057 1.339   -10.235 1.00 18.89  ? 482 ILE B CB     1 
ATOM   3276 C CG1    . ILE B 1 143 ? -11.692 1.844   -9.769  1.00 20.20  ? 482 ILE B CG1    1 
ATOM   3277 C CG2    . ILE B 1 143 ? -13.264 1.646   -11.708 1.00 17.17  ? 482 ILE B CG2    1 
ATOM   3278 C CD1    . ILE B 1 143 ? -10.529 1.123   -10.409 1.00 15.51  ? 482 ILE B CD1    1 
ATOM   3279 N N      . LEU B 1 144 ? -16.524 2.391   -9.743  1.00 23.24  ? 483 LEU B N      1 
ATOM   3280 C CA     . LEU B 1 144 ? -17.894 2.080   -10.114 1.00 21.96  ? 483 LEU B CA     1 
ATOM   3281 C C      . LEU B 1 144 ? -18.029 2.028   -11.629 1.00 22.57  ? 483 LEU B C      1 
ATOM   3282 O O      . LEU B 1 144 ? -17.267 2.662   -12.363 1.00 26.51  ? 483 LEU B O      1 
ATOM   3283 C CB     . LEU B 1 144 ? -18.847 3.117   -9.521  1.00 19.79  ? 483 LEU B CB     1 
ATOM   3284 C CG     . LEU B 1 144 ? -18.638 3.355   -8.023  1.00 23.23  ? 483 LEU B CG     1 
ATOM   3285 C CD1    . LEU B 1 144 ? -19.376 4.600   -7.568  1.00 28.22  ? 483 LEU B CD1    1 
ATOM   3286 C CD2    . LEU B 1 144 ? -19.074 2.143   -7.212  1.00 25.55  ? 483 LEU B CD2    1 
ATOM   3287 N N      . LEU B 1 145 ? -19.006 1.259   -12.096 1.00 25.18  ? 484 LEU B N      1 
ATOM   3288 C CA     . LEU B 1 145 ? -19.169 0.988   -13.516 1.00 24.25  ? 484 LEU B CA     1 
ATOM   3289 C C      . LEU B 1 145 ? -20.419 1.660   -14.064 1.00 25.19  ? 484 LEU B C      1 
ATOM   3290 O O      . LEU B 1 145 ? -21.462 1.699   -13.403 1.00 26.19  ? 484 LEU B O      1 
ATOM   3291 C CB     . LEU B 1 145 ? -19.223 -0.518  -13.784 1.00 24.82  ? 484 LEU B CB     1 
ATOM   3292 C CG     . LEU B 1 145 ? -17.852 -1.153  -14.027 1.00 24.13  ? 484 LEU B CG     1 
ATOM   3293 C CD1    . LEU B 1 145 ? -16.923 -0.887  -12.853 1.00 26.21  ? 484 LEU B CD1    1 
ATOM   3294 C CD2    . LEU B 1 145 ? -17.983 -2.640  -14.290 1.00 23.64  ? 484 LEU B CD2    1 
ATOM   3295 N N      . ASP B 1 146 ? -20.296 2.182   -15.281 1.00 26.82  ? 485 ASP B N      1 
ATOM   3296 C CA     . ASP B 1 146 ? -21.384 2.839   -15.982 1.00 22.72  ? 485 ASP B CA     1 
ATOM   3297 C C      . ASP B 1 146 ? -22.401 1.806   -16.467 1.00 28.01  ? 485 ASP B C      1 
ATOM   3298 O O      . ASP B 1 146 ? -22.178 0.592   -16.409 1.00 25.65  ? 485 ASP B O      1 
ATOM   3299 C CB     . ASP B 1 146 ? -20.830 3.638   -17.165 1.00 24.50  ? 485 ASP B CB     1 
ATOM   3300 C CG     . ASP B 1 146 ? -21.561 4.944   -17.386 1.00 27.96  ? 485 ASP B CG     1 
ATOM   3301 O OD1    . ASP B 1 146 ? -22.424 5.289   -16.556 1.00 36.00  ? 485 ASP B OD1    1 
ATOM   3302 O OD2    . ASP B 1 146 ? -21.269 5.630   -18.388 1.00 28.46  ? 485 ASP B OD2    1 
ATOM   3303 N N      . GLY B 1 147 ? -23.542 2.303   -16.945 1.00 30.18  ? 486 GLY B N      1 
ATOM   3304 C CA     . GLY B 1 147 ? -24.482 1.433   -17.626 1.00 27.92  ? 486 GLY B CA     1 
ATOM   3305 C C      . GLY B 1 147 ? -23.891 0.762   -18.846 1.00 29.55  ? 486 GLY B C      1 
ATOM   3306 O O      . GLY B 1 147 ? -24.392 -0.282  -19.278 1.00 27.55  ? 486 GLY B O      1 
ATOM   3307 N N      . LYS B 1 148 ? -22.834 1.343   -19.415 1.00 27.45  ? 487 LYS B N      1 
ATOM   3308 C CA     . LYS B 1 148 ? -22.084 0.735   -20.505 1.00 27.20  ? 487 LYS B CA     1 
ATOM   3309 C C      . LYS B 1 148 ? -20.709 0.259   -20.048 1.00 28.63  ? 487 LYS B C      1 
ATOM   3310 O O      . LYS B 1 148 ? -19.802 0.094   -20.871 1.00 33.15  ? 487 LYS B O      1 
ATOM   3311 C CB     . LYS B 1 148 ? -21.964 1.715   -21.672 1.00 26.98  ? 487 LYS B CB     1 
ATOM   3312 C CG     . LYS B 1 148 ? -23.306 2.069   -22.303 1.00 33.56  ? 487 LYS B CG     1 
ATOM   3313 C CD     . LYS B 1 148 ? -23.156 3.048   -23.460 1.00 45.63  ? 487 LYS B CD     1 
ATOM   3314 C CE     . LYS B 1 148 ? -22.975 4.479   -22.974 1.00 43.74  ? 487 LYS B CE     1 
ATOM   3315 N NZ     . LYS B 1 148 ? -24.201 5.005   -22.311 1.00 44.08  ? 487 LYS B NZ     1 
ATOM   3316 N N      . PHE B 1 149 ? -20.539 0.044   -18.742 1.00 26.06  ? 488 PHE B N      1 
ATOM   3317 C CA     . PHE B 1 149 ? -19.317 -0.531  -18.180 1.00 23.33  ? 488 PHE B CA     1 
ATOM   3318 C C      . PHE B 1 149 ? -18.120 0.395   -18.382 1.00 26.85  ? 488 PHE B C      1 
ATOM   3319 O O      . PHE B 1 149 ? -17.036 -0.023  -18.796 1.00 26.05  ? 488 PHE B O      1 
ATOM   3320 C CB     . PHE B 1 149 ? -19.058 -1.918  -18.763 1.00 26.92  ? 488 PHE B CB     1 
ATOM   3321 C CG     . PHE B 1 149 ? -20.145 -2.901  -18.455 1.00 29.78  ? 488 PHE B CG     1 
ATOM   3322 C CD1    . PHE B 1 149 ? -20.168 -3.565  -17.241 1.00 25.75  ? 488 PHE B CD1    1 
ATOM   3323 C CD2    . PHE B 1 149 ? -21.159 -3.144  -19.365 1.00 28.25  ? 488 PHE B CD2    1 
ATOM   3324 C CE1    . PHE B 1 149 ? -21.171 -4.462  -16.947 1.00 26.43  ? 488 PHE B CE1    1 
ATOM   3325 C CE2    . PHE B 1 149 ? -22.166 -4.043  -19.075 1.00 29.16  ? 488 PHE B CE2    1 
ATOM   3326 C CZ     . PHE B 1 149 ? -22.171 -4.702  -17.863 1.00 28.17  ? 488 PHE B CZ     1 
ATOM   3327 N N      . ARG B 1 150 ? -18.326 1.670   -18.071 1.00 28.86  ? 489 ARG B N      1 
ATOM   3328 C CA     . ARG B 1 150 ? -17.273 2.671   -18.092 1.00 24.52  ? 489 ARG B CA     1 
ATOM   3329 C C      . ARG B 1 150 ? -16.817 2.965   -16.668 1.00 22.49  ? 489 ARG B C      1 
ATOM   3330 O O      . ARG B 1 150 ? -17.593 2.863   -15.714 1.00 25.38  ? 489 ARG B O      1 
ATOM   3331 C CB     . ARG B 1 150 ? -17.758 3.953   -18.769 1.00 24.79  ? 489 ARG B CB     1 
ATOM   3332 C CG     . ARG B 1 150 ? -18.271 3.733   -20.183 1.00 27.48  ? 489 ARG B CG     1 
ATOM   3333 C CD     . ARG B 1 150 ? -17.162 3.228   -21.091 1.00 27.51  ? 489 ARG B CD     1 
ATOM   3334 N NE     . ARG B 1 150 ? -16.046 4.164   -21.133 1.00 27.87  ? 489 ARG B NE     1 
ATOM   3335 C CZ     . ARG B 1 150 ? -15.977 5.208   -21.946 1.00 30.46  ? 489 ARG B CZ     1 
ATOM   3336 N NH1    . ARG B 1 150 ? -16.939 5.470   -22.816 1.00 28.40  ? 489 ARG B NH1    1 
ATOM   3337 N NH2    . ARG B 1 150 ? -14.919 6.012   -21.883 1.00 32.69  ? 489 ARG B NH2    1 
ATOM   3338 N N      . GLY B 1 151 ? -15.544 3.323   -16.534 1.00 22.37  ? 490 GLY B N      1 
ATOM   3339 C CA     . GLY B 1 151 ? -14.980 3.549   -15.214 1.00 19.18  ? 490 GLY B CA     1 
ATOM   3340 C C      . GLY B 1 151 ? -15.495 4.839   -14.602 1.00 22.88  ? 490 GLY B C      1 
ATOM   3341 O O      . GLY B 1 151 ? -15.447 5.906   -15.228 1.00 24.45  ? 490 GLY B O      1 
ATOM   3342 N N      . LYS B 1 152 ? -15.990 4.748   -13.369 1.00 24.19  ? 491 LYS B N      1 
ATOM   3343 C CA     . LYS B 1 152 ? -16.436 5.906   -12.596 1.00 24.02  ? 491 LYS B CA     1 
ATOM   3344 C C      . LYS B 1 152 ? -15.750 5.834   -11.234 1.00 22.82  ? 491 LYS B C      1 
ATOM   3345 O O      . LYS B 1 152 ? -16.229 5.145   -10.327 1.00 19.54  ? 491 LYS B O      1 
ATOM   3346 C CB     . LYS B 1 152 ? -17.955 5.930   -12.451 1.00 22.34  ? 491 LYS B CB     1 
ATOM   3347 C CG     . LYS B 1 152 ? -18.717 6.013   -13.762 1.00 25.19  ? 491 LYS B CG     1 
ATOM   3348 C CD     . LYS B 1 152 ? -18.834 7.444   -14.261 1.00 24.76  ? 491 LYS B CD     1 
ATOM   3349 C CE     . LYS B 1 152 ? -19.627 7.506   -15.558 1.00 22.55  ? 491 LYS B CE     1 
ATOM   3350 N NZ     . LYS B 1 152 ? -19.915 8.909   -15.962 1.00 29.79  ? 491 LYS B NZ     1 
ATOM   3351 N N      . VAL B 1 153 ? -14.628 6.542   -11.090 1.00 23.39  ? 492 VAL B N      1 
ATOM   3352 C CA     . VAL B 1 153 ? -13.888 6.517   -9.835  1.00 24.18  ? 492 VAL B CA     1 
ATOM   3353 C C      . VAL B 1 153 ? -14.716 7.173   -8.735  1.00 23.42  ? 492 VAL B C      1 
ATOM   3354 O O      . VAL B 1 153 ? -15.539 8.064   -8.989  1.00 26.34  ? 492 VAL B O      1 
ATOM   3355 C CB     . VAL B 1 153 ? -12.523 7.209   -9.994  1.00 26.51  ? 492 VAL B CB     1 
ATOM   3356 C CG1    . VAL B 1 153 ? -11.729 7.121   -8.699  1.00 23.96  ? 492 VAL B CG1    1 
ATOM   3357 C CG2    . VAL B 1 153 ? -11.746 6.587   -11.145 1.00 22.23  ? 492 VAL B CG2    1 
ATOM   3358 N N      . SER B 1 154 ? -14.503 6.727   -7.500  1.00 28.84  ? 493 SER B N      1 
ATOM   3359 C CA     . SER B 1 154 ? -15.274 7.214   -6.364  1.00 28.47  ? 493 SER B CA     1 
ATOM   3360 C C      . SER B 1 154 ? -14.461 7.024   -5.091  1.00 27.33  ? 493 SER B C      1 
ATOM   3361 O O      . SER B 1 154 ? -13.294 6.622   -5.123  1.00 26.78  ? 493 SER B O      1 
ATOM   3362 C CB     . SER B 1 154 ? -16.618 6.491   -6.253  1.00 29.48  ? 493 SER B CB     1 
ATOM   3363 O OG     . SER B 1 154 ? -16.431 5.140   -5.865  1.00 29.59  ? 493 SER B OG     1 
ATOM   3364 N N      . ASN B 1 155 ? -15.101 7.324   -3.962  1.00 29.67  ? 494 ASN B N      1 
ATOM   3365 C CA     . ASN B 1 155 ? -14.554 7.078   -2.630  1.00 27.92  ? 494 ASN B CA     1 
ATOM   3366 C C      . ASN B 1 155 ? -13.184 7.740   -2.462  1.00 26.38  ? 494 ASN B C      1 
ATOM   3367 O O      . ASN B 1 155 ? -12.185 7.100   -2.130  1.00 27.18  ? 494 ASN B O      1 
ATOM   3368 C CB     . ASN B 1 155 ? -14.487 5.574   -2.346  1.00 28.48  ? 494 ASN B CB     1 
ATOM   3369 C CG     . ASN B 1 155 ? -14.859 5.235   -0.916  1.00 31.05  ? 494 ASN B CG     1 
ATOM   3370 O OD1    . ASN B 1 155 ? -15.144 6.122   -0.110  1.00 33.42  ? 494 ASN B OD1    1 
ATOM   3371 N ND2    . ASN B 1 155 ? -14.872 3.945   -0.596  1.00 33.45  ? 494 ASN B ND2    1 
ATOM   3372 N N      . PHE B 1 156 ? -13.161 9.052   -2.690  1.00 31.22  ? 495 PHE B N      1 
ATOM   3373 C CA     . PHE B 1 156 ? -11.950 9.833   -2.488  1.00 31.07  ? 495 PHE B CA     1 
ATOM   3374 C C      . PHE B 1 156 ? -11.636 9.962   -1.002  1.00 36.66  ? 495 PHE B C      1 
ATOM   3375 O O      . PHE B 1 156 ? -12.528 9.929   -0.149  1.00 34.99  ? 495 PHE B O      1 
ATOM   3376 C CB     . PHE B 1 156 ? -12.099 11.227  -3.101  1.00 31.38  ? 495 PHE B CB     1 
ATOM   3377 C CG     . PHE B 1 156 ? -12.122 11.236  -4.602  1.00 28.66  ? 495 PHE B CG     1 
ATOM   3378 C CD1    . PHE B 1 156 ? -13.175 10.664  -5.297  1.00 29.34  ? 495 PHE B CD1    1 
ATOM   3379 C CD2    . PHE B 1 156 ? -11.099 11.835  -5.317  1.00 28.85  ? 495 PHE B CD2    1 
ATOM   3380 C CE1    . PHE B 1 156 ? -13.198 10.676  -6.678  1.00 32.90  ? 495 PHE B CE1    1 
ATOM   3381 C CE2    . PHE B 1 156 ? -11.117 11.852  -6.698  1.00 31.47  ? 495 PHE B CE2    1 
ATOM   3382 C CZ     . PHE B 1 156 ? -12.169 11.272  -7.380  1.00 32.95  ? 495 PHE B CZ     1 
ATOM   3383 N N      . GLY B 1 157 ? -10.353 10.118  -0.698  1.00 37.23  ? 496 GLY B N      1 
ATOM   3384 C CA     . GLY B 1 157 ? -9.909  10.334  0.662   1.00 40.25  ? 496 GLY B CA     1 
ATOM   3385 C C      . GLY B 1 157 ? -9.517  9.039   1.352   1.00 45.91  ? 496 GLY B C      1 
ATOM   3386 O O      . GLY B 1 157 ? -9.959  7.945   0.995   1.00 47.94  ? 496 GLY B O      1 
ATOM   3387 N N      . LEU B 1 158 ? -8.675  9.173   2.372   1.00 58.66  ? 497 LEU B N      1 
ATOM   3388 C CA     . LEU B 1 158 ? -8.147  8.016   3.083   1.00 65.26  ? 497 LEU B CA     1 
ATOM   3389 C C      . LEU B 1 158 ? -8.409  8.123   4.583   1.00 62.19  ? 497 LEU B C      1 
ATOM   3390 O O      . LEU B 1 158 ? -8.743  7.137   5.239   1.00 71.55  ? 497 LEU B O      1 
ATOM   3391 C CB     . LEU B 1 158 ? -6.647  7.871   2.818   1.00 57.76  ? 497 LEU B CB     1 
ATOM   3392 C CG     . LEU B 1 158 ? -6.065  6.465   2.956   1.00 60.83  ? 497 LEU B CG     1 
ATOM   3393 C CD1    . LEU B 1 158 ? -6.808  5.499   2.048   1.00 51.75  ? 497 LEU B CD1    1 
ATOM   3394 C CD2    . LEU B 1 158 ? -4.582  6.477   2.630   1.00 54.28  ? 497 LEU B CD2    1 
ATOM   3395 N N      . PHE B 1 171 ? -16.927 0.314   12.999  1.00 46.75  ? 510 PHE B N      1 
ATOM   3396 C CA     . PHE B 1 171 ? -15.861 0.312   12.003  1.00 43.34  ? 510 PHE B CA     1 
ATOM   3397 C C      . PHE B 1 171 ? -15.353 -1.106  11.762  1.00 42.37  ? 510 PHE B C      1 
ATOM   3398 O O      . PHE B 1 171 ? -15.208 -1.895  12.696  1.00 48.58  ? 510 PHE B O      1 
ATOM   3399 C CB     . PHE B 1 171 ? -14.714 1.226   12.443  1.00 40.29  ? 510 PHE B CB     1 
ATOM   3400 C CG     . PHE B 1 171 ? -13.512 1.175   11.541  1.00 38.37  ? 510 PHE B CG     1 
ATOM   3401 C CD1    . PHE B 1 171 ? -13.513 1.838   10.325  1.00 38.06  ? 510 PHE B CD1    1 
ATOM   3402 C CD2    . PHE B 1 171 ? -12.377 0.474   11.915  1.00 37.02  ? 510 PHE B CD2    1 
ATOM   3403 C CE1    . PHE B 1 171 ? -12.407 1.795   9.496   1.00 33.17  ? 510 PHE B CE1    1 
ATOM   3404 C CE2    . PHE B 1 171 ? -11.270 0.428   11.090  1.00 35.09  ? 510 PHE B CE2    1 
ATOM   3405 C CZ     . PHE B 1 171 ? -11.285 1.090   9.879   1.00 32.77  ? 510 PHE B CZ     1 
ATOM   3406 N N      . GLN B 1 172 ? -15.083 -1.420  10.498  1.00 41.46  ? 511 GLN B N      1 
ATOM   3407 C CA     . GLN B 1 172 ? -14.634 -2.749  10.088  1.00 44.47  ? 511 GLN B CA     1 
ATOM   3408 C C      . GLN B 1 172 ? -13.124 -2.690  9.880   1.00 44.96  ? 511 GLN B C      1 
ATOM   3409 O O      . GLN B 1 172 ? -12.636 -2.346  8.803   1.00 44.55  ? 511 GLN B O      1 
ATOM   3410 C CB     . GLN B 1 172 ? -15.368 -3.195  8.830   1.00 48.25  ? 511 GLN B CB     1 
ATOM   3411 C CG     . GLN B 1 172 ? -16.880 -3.234  8.986   1.00 52.18  ? 511 GLN B CG     1 
ATOM   3412 C CD     . GLN B 1 172 ? -17.606 -2.805  7.727   1.00 55.98  ? 511 GLN B CD     1 
ATOM   3413 O OE1    . GLN B 1 172 ? -17.175 -1.885  7.032   1.00 65.02  ? 511 GLN B OE1    1 
ATOM   3414 N NE2    . GLN B 1 172 ? -18.714 -3.472  7.425   1.00 46.32  ? 511 GLN B NE2    1 
ATOM   3415 N N      . LEU B 1 173 ? -12.379 -3.034  10.932  1.00 41.67  ? 512 LEU B N      1 
ATOM   3416 C CA     . LEU B 1 173 ? -10.922 -2.965  10.873  1.00 37.58  ? 512 LEU B CA     1 
ATOM   3417 C C      . LEU B 1 173 ? -10.361 -3.973  9.878   1.00 38.88  ? 512 LEU B C      1 
ATOM   3418 O O      . LEU B 1 173 ? -9.625  -3.608  8.953   1.00 38.84  ? 512 LEU B O      1 
ATOM   3419 C CB     . LEU B 1 173 ? -10.334 -3.202  12.265  1.00 34.94  ? 512 LEU B CB     1 
ATOM   3420 C CG     . LEU B 1 173 ? -8.815  -3.082  12.388  1.00 30.31  ? 512 LEU B CG     1 
ATOM   3421 C CD1    . LEU B 1 173 ? -8.425  -1.675  12.808  1.00 29.57  ? 512 LEU B CD1    1 
ATOM   3422 C CD2    . LEU B 1 173 ? -8.264  -4.116  13.360  1.00 34.33  ? 512 LEU B CD2    1 
ATOM   3423 N N      . THR B 1 174 ? -10.697 -5.253  10.057  1.00 37.85  ? 513 THR B N      1 
ATOM   3424 C CA     . THR B 1 174 ? -10.111 -6.305  9.230   1.00 37.70  ? 513 THR B CA     1 
ATOM   3425 C C      . THR B 1 174 ? -10.295 -6.018  7.746   1.00 38.76  ? 513 THR B C      1 
ATOM   3426 O O      . THR B 1 174 ? -9.378  -6.231  6.944   1.00 38.25  ? 513 THR B O      1 
ATOM   3427 C CB     . THR B 1 174 ? -10.723 -7.659  9.591   1.00 36.68  ? 513 THR B CB     1 
ATOM   3428 O OG1    . THR B 1 174 ? -10.747 -7.810  11.016  1.00 38.49  ? 513 THR B OG1    1 
ATOM   3429 C CG2    . THR B 1 174 ? -9.905  -8.789  8.982   1.00 38.39  ? 513 THR B CG2    1 
ATOM   3430 N N      . ARG B 1 175 ? -11.477 -5.537  7.359   1.00 37.43  ? 514 ARG B N      1 
ATOM   3431 C CA     . ARG B 1 175 ? -11.700 -5.159  5.967   1.00 42.83  ? 514 ARG B CA     1 
ATOM   3432 C C      . ARG B 1 175 ? -10.699 -4.099  5.526   1.00 42.56  ? 514 ARG B C      1 
ATOM   3433 O O      . ARG B 1 175 ? -9.994  -4.268  4.523   1.00 36.95  ? 514 ARG B O      1 
ATOM   3434 C CB     . ARG B 1 175 ? -13.133 -4.661  5.787   1.00 46.19  ? 514 ARG B CB     1 
ATOM   3435 C CG     . ARG B 1 175 ? -14.187 -5.682  6.169   1.00 60.25  ? 514 ARG B CG     1 
ATOM   3436 C CD     . ARG B 1 175 ? -15.578 -5.074  6.176   1.00 64.46  ? 514 ARG B CD     1 
ATOM   3437 N NE     . ARG B 1 175 ? -16.607 -6.092  6.355   1.00 68.09  ? 514 ARG B NE     1 
ATOM   3438 C CZ     . ARG B 1 175 ? -16.938 -6.626  7.523   1.00 64.38  ? 514 ARG B CZ     1 
ATOM   3439 N NH1    . ARG B 1 175 ? -16.337 -6.263  8.645   1.00 64.76  ? 514 ARG B NH1    1 
ATOM   3440 N NH2    . ARG B 1 175 ? -17.892 -7.551  7.566   1.00 60.68  ? 514 ARG B NH2    1 
ATOM   3441 N N      . HIS B 1 176 ? -10.615 -2.998  6.276   1.00 38.74  ? 515 HIS B N      1 
ATOM   3442 C CA     . HIS B 1 176 ? -9.704  -1.920  5.909   1.00 38.91  ? 515 HIS B CA     1 
ATOM   3443 C C      . HIS B 1 176 ? -8.253  -2.386  5.887   1.00 39.81  ? 515 HIS B C      1 
ATOM   3444 O O      . HIS B 1 176 ? -7.441  -1.846  5.126   1.00 36.83  ? 515 HIS B O      1 
ATOM   3445 C CB     . HIS B 1 176 ? -9.867  -0.747  6.876   1.00 36.37  ? 515 HIS B CB     1 
ATOM   3446 C CG     . HIS B 1 176 ? -9.050  0.450   6.510   1.00 37.18  ? 515 HIS B CG     1 
ATOM   3447 N ND1    . HIS B 1 176 ? -9.463  1.374   5.574   1.00 40.72  ? 515 HIS B ND1    1 
ATOM   3448 C CD2    . HIS B 1 176 ? -7.838  0.868   6.943   1.00 40.51  ? 515 HIS B CD2    1 
ATOM   3449 C CE1    . HIS B 1 176 ? -8.542  2.313   5.451   1.00 43.07  ? 515 HIS B CE1    1 
ATOM   3450 N NE2    . HIS B 1 176 ? -7.545  2.029   6.270   1.00 42.20  ? 515 HIS B NE2    1 
ATOM   3451 N N      . VAL B 1 177 ? -7.908  -3.379  6.707   1.00 39.12  ? 516 VAL B N      1 
ATOM   3452 C CA     . VAL B 1 177 ? -6.521  -3.829  6.770   1.00 36.84  ? 516 VAL B CA     1 
ATOM   3453 C C      . VAL B 1 177 ? -6.175  -4.734  5.593   1.00 35.47  ? 516 VAL B C      1 
ATOM   3454 O O      . VAL B 1 177 ? -5.005  -4.820  5.200   1.00 37.30  ? 516 VAL B O      1 
ATOM   3455 C CB     . VAL B 1 177 ? -6.246  -4.528  8.111   1.00 31.49  ? 516 VAL B CB     1 
ATOM   3456 C CG1    . VAL B 1 177 ? -4.806  -4.999  8.171   1.00 30.41  ? 516 VAL B CG1    1 
ATOM   3457 C CG2    . VAL B 1 177 ? -6.549  -3.590  9.266   1.00 30.17  ? 516 VAL B CG2    1 
ATOM   3458 N N      . ILE B 1 178 ? -7.162  -5.425  5.017   1.00 31.17  ? 517 ILE B N      1 
ATOM   3459 C CA     . ILE B 1 178 ? -6.902  -6.210  3.814   1.00 38.47  ? 517 ILE B CA     1 
ATOM   3460 C C      . ILE B 1 178 ? -6.702  -5.290  2.617   1.00 37.86  ? 517 ILE B C      1 
ATOM   3461 O O      . ILE B 1 178 ? -5.794  -5.495  1.803   1.00 35.29  ? 517 ILE B O      1 
ATOM   3462 C CB     . ILE B 1 178 ? -8.038  -7.219  3.573   1.00 40.05  ? 517 ILE B CB     1 
ATOM   3463 C CG1    . ILE B 1 178 ? -8.111  -8.219  4.729   1.00 35.94  ? 517 ILE B CG1    1 
ATOM   3464 C CG2    . ILE B 1 178 ? -7.839  -7.940  2.246   1.00 33.96  ? 517 ILE B CG2    1 
ATOM   3465 C CD1    . ILE B 1 178 ? -9.357  -9.075  4.714   1.00 34.57  ? 517 ILE B CD1    1 
ATOM   3466 N N      . GLY B 1 179 ? -7.536  -4.254  2.498   1.00 39.09  ? 518 GLY B N      1 
ATOM   3467 C CA     . GLY B 1 179 ? -7.342  -3.285  1.431   1.00 33.18  ? 518 GLY B CA     1 
ATOM   3468 C C      . GLY B 1 179 ? -5.957  -2.669  1.459   1.00 31.46  ? 518 GLY B C      1 
ATOM   3469 O O      . GLY B 1 179 ? -5.238  -2.677  0.457   1.00 33.84  ? 518 GLY B O      1 
ATOM   3470 N N      . THR B 1 180 ? -5.559  -2.136  2.616   1.00 28.98  ? 519 THR B N      1 
ATOM   3471 C CA     . THR B 1 180 ? -4.231  -1.544  2.738   1.00 35.12  ? 519 THR B CA     1 
ATOM   3472 C C      . THR B 1 180 ? -3.134  -2.534  2.365   1.00 37.63  ? 519 THR B C      1 
ATOM   3473 O O      . THR B 1 180 ? -2.073  -2.128  1.877   1.00 32.19  ? 519 THR B O      1 
ATOM   3474 C CB     . THR B 1 180 ? -4.007  -1.030  4.163   1.00 40.54  ? 519 THR B CB     1 
ATOM   3475 O OG1    . THR B 1 180 ? -4.141  -2.113  5.095   1.00 33.54  ? 519 THR B OG1    1 
ATOM   3476 C CG2    . THR B 1 180 ? -5.014  0.060   4.506   1.00 43.50  ? 519 THR B CG2    1 
ATOM   3477 N N      . GLN B 1 181 ? -3.370  -3.830  2.577   1.00 35.41  ? 520 GLN B N      1 
ATOM   3478 C CA     . GLN B 1 181 ? -2.313  -4.815  2.370   1.00 32.54  ? 520 GLN B CA     1 
ATOM   3479 C C      . GLN B 1 181 ? -1.917  -4.911  0.901   1.00 34.68  ? 520 GLN B C      1 
ATOM   3480 O O      . GLN B 1 181 ? -0.728  -5.028  0.580   1.00 36.92  ? 520 GLN B O      1 
ATOM   3481 C CB     . GLN B 1 181 ? -2.759  -6.179  2.897   1.00 31.84  ? 520 GLN B CB     1 
ATOM   3482 C CG     . GLN B 1 181 ? -1.617  -7.165  3.091   1.00 29.91  ? 520 GLN B CG     1 
ATOM   3483 C CD     . GLN B 1 181 ? -2.094  -8.548  3.484   1.00 27.05  ? 520 GLN B CD     1 
ATOM   3484 O OE1    . GLN B 1 181 ? -3.289  -8.775  3.678   1.00 28.58  ? 520 GLN B OE1    1 
ATOM   3485 N NE2    . GLN B 1 181 ? -1.160  -9.484  3.598   1.00 28.17  ? 520 GLN B NE2    1 
ATOM   3486 N N      . GLY B 1 182 ? -2.891  -4.858  -0.004  1.00 30.73  ? 521 GLY B N      1 
ATOM   3487 C CA     . GLY B 1 182 ? -2.615  -5.074  -1.411  1.00 29.86  ? 521 GLY B CA     1 
ATOM   3488 C C      . GLY B 1 182 ? -2.507  -3.823  -2.260  1.00 26.64  ? 521 GLY B C      1 
ATOM   3489 O O      . GLY B 1 182 ? -2.009  -3.883  -3.388  1.00 27.73  ? 521 GLY B O      1 
ATOM   3490 N N      . TYR B 1 183 ? -2.964  -2.684  -1.738  1.00 26.30  ? 522 TYR B N      1 
ATOM   3491 C CA     . TYR B 1 183 ? -2.990  -1.443  -2.503  1.00 25.30  ? 522 TYR B CA     1 
ATOM   3492 C C      . TYR B 1 183 ? -2.006  -0.389  -2.019  1.00 24.54  ? 522 TYR B C      1 
ATOM   3493 O O      . TYR B 1 183 ? -1.526  0.401   -2.832  1.00 26.75  ? 522 TYR B O      1 
ATOM   3494 C CB     . TYR B 1 183 ? -4.398  -0.829  -2.482  1.00 27.29  ? 522 TYR B CB     1 
ATOM   3495 C CG     . TYR B 1 183 ? -5.455  -1.626  -3.217  1.00 26.14  ? 522 TYR B CG     1 
ATOM   3496 C CD1    . TYR B 1 183 ? -5.587  -1.537  -4.596  1.00 27.28  ? 522 TYR B CD1    1 
ATOM   3497 C CD2    . TYR B 1 183 ? -6.337  -2.448  -2.527  1.00 26.39  ? 522 TYR B CD2    1 
ATOM   3498 C CE1    . TYR B 1 183 ? -6.557  -2.256  -5.270  1.00 28.60  ? 522 TYR B CE1    1 
ATOM   3499 C CE2    . TYR B 1 183 ? -7.310  -3.169  -3.191  1.00 27.82  ? 522 TYR B CE2    1 
ATOM   3500 C CZ     . TYR B 1 183 ? -7.416  -3.070  -4.561  1.00 28.90  ? 522 TYR B CZ     1 
ATOM   3501 O OH     . TYR B 1 183 ? -8.384  -3.789  -5.226  1.00 30.58  ? 522 TYR B OH     1 
ATOM   3502 N N      . MET B 1 184 ? -1.702  -0.346  -0.725  1.00 23.38  ? 523 MET B N      1 
ATOM   3503 C CA     . MET B 1 184 ? -0.897  0.743   -0.188  1.00 23.67  ? 523 MET B CA     1 
ATOM   3504 C C      . MET B 1 184 ? 0.565   0.597   -0.590  1.00 22.27  ? 523 MET B C      1 
ATOM   3505 O O      . MET B 1 184 ? 1.114   -0.508  -0.615  1.00 26.97  ? 523 MET B O      1 
ATOM   3506 C CB     . MET B 1 184 ? -1.029  0.801   1.333   1.00 26.25  ? 523 MET B CB     1 
ATOM   3507 C CG     . MET B 1 184 ? -2.384  1.306   1.788   1.00 28.96  ? 523 MET B CG     1 
ATOM   3508 S SD     . MET B 1 184 ? -2.761  2.910   1.057   1.00 36.58  ? 523 MET B SD     1 
ATOM   3509 C CE     . MET B 1 184 ? -4.541  2.801   0.876   1.00 33.94  ? 523 MET B CE     1 
ATOM   3510 N N      . ALA B 1 185 ? 1.196   1.732   -0.906  1.00 21.34  ? 524 ALA B N      1 
ATOM   3511 C CA     . ALA B 1 185 ? 2.569   1.749   -1.379  1.00 20.59  ? 524 ALA B CA     1 
ATOM   3512 C C      . ALA B 1 185 ? 3.550   1.731   -0.209  1.00 20.54  ? 524 ALA B C      1 
ATOM   3513 O O      . ALA B 1 185 ? 3.236   2.210   0.884   1.00 23.56  ? 524 ALA B O      1 
ATOM   3514 C CB     . ALA B 1 185 ? 2.821   2.981   -2.240  1.00 20.93  ? 524 ALA B CB     1 
ATOM   3515 N N      . PRO B 1 186 ? 4.752   1.189   -0.421  1.00 23.42  ? 525 PRO B N      1 
ATOM   3516 C CA     . PRO B 1 186 ? 5.708   1.086   0.693   1.00 24.54  ? 525 PRO B CA     1 
ATOM   3517 C C      . PRO B 1 186 ? 6.014   2.418   1.356   1.00 23.28  ? 525 PRO B C      1 
ATOM   3518 O O      . PRO B 1 186 ? 6.164   2.472   2.583   1.00 24.16  ? 525 PRO B O      1 
ATOM   3519 C CB     . PRO B 1 186 ? 6.953   0.482   0.026   1.00 26.08  ? 525 PRO B CB     1 
ATOM   3520 C CG     . PRO B 1 186 ? 6.442   -0.196  -1.205  1.00 28.67  ? 525 PRO B CG     1 
ATOM   3521 C CD     . PRO B 1 186 ? 5.294   0.639   -1.675  1.00 24.89  ? 525 PRO B CD     1 
ATOM   3522 N N      . GLU B 1 187 ? 6.116   3.501   0.580   1.00 24.91  ? 526 GLU B N      1 
ATOM   3523 C CA     . GLU B 1 187 ? 6.472   4.786   1.174   1.00 23.64  ? 526 GLU B CA     1 
ATOM   3524 C C      . GLU B 1 187 ? 5.367   5.312   2.080   1.00 17.87  ? 526 GLU B C      1 
ATOM   3525 O O      . GLU B 1 187 ? 5.647   6.071   3.015   1.00 21.22  ? 526 GLU B O      1 
ATOM   3526 C CB     . GLU B 1 187 ? 6.806   5.810   0.086   1.00 18.37  ? 526 GLU B CB     1 
ATOM   3527 C CG     . GLU B 1 187 ? 5.607   6.340   -0.680  1.00 22.11  ? 526 GLU B CG     1 
ATOM   3528 C CD     . GLU B 1 187 ? 5.341   5.567   -1.955  1.00 20.45  ? 526 GLU B CD     1 
ATOM   3529 O OE1    . GLU B 1 187 ? 5.923   4.475   -2.118  1.00 17.87  ? 526 GLU B OE1    1 
ATOM   3530 O OE2    . GLU B 1 187 ? 4.557   6.058   -2.797  1.00 19.58  ? 526 GLU B OE2    1 
ATOM   3531 N N      . TYR B 1 188 ? 4.116   4.930   1.830   1.00 14.24  ? 527 TYR B N      1 
ATOM   3532 C CA     . TYR B 1 188 ? 3.040   5.298   2.743   1.00 22.98  ? 527 TYR B CA     1 
ATOM   3533 C C      . TYR B 1 188 ? 2.936   4.340   3.922   1.00 25.01  ? 527 TYR B C      1 
ATOM   3534 O O      . TYR B 1 188 ? 2.706   4.777   5.056   1.00 19.65  ? 527 TYR B O      1 
ATOM   3535 C CB     . TYR B 1 188 ? 1.698   5.353   2.005   1.00 24.74  ? 527 TYR B CB     1 
ATOM   3536 C CG     . TYR B 1 188 ? 0.557   5.812   2.885   1.00 21.17  ? 527 TYR B CG     1 
ATOM   3537 C CD1    . TYR B 1 188 ? 0.522   7.107   3.383   1.00 24.76  ? 527 TYR B CD1    1 
ATOM   3538 C CD2    . TYR B 1 188 ? -0.476  4.950   3.226   1.00 21.13  ? 527 TYR B CD2    1 
ATOM   3539 C CE1    . TYR B 1 188 ? -0.512  7.533   4.195   1.00 25.30  ? 527 TYR B CE1    1 
ATOM   3540 C CE2    . TYR B 1 188 ? -1.514  5.367   4.034   1.00 21.34  ? 527 TYR B CE2    1 
ATOM   3541 C CZ     . TYR B 1 188 ? -1.528  6.658   4.516   1.00 23.68  ? 527 TYR B CZ     1 
ATOM   3542 O OH     . TYR B 1 188 ? -2.561  7.076   5.324   1.00 28.06  ? 527 TYR B OH     1 
ATOM   3543 N N      . ILE B 1 189 ? 3.105   3.038   3.676   1.00 24.34  ? 528 ILE B N      1 
ATOM   3544 C CA     . ILE B 1 189 ? 3.024   2.056   4.754   1.00 23.07  ? 528 ILE B CA     1 
ATOM   3545 C C      . ILE B 1 189 ? 4.162   2.257   5.745   1.00 21.68  ? 528 ILE B C      1 
ATOM   3546 O O      . ILE B 1 189 ? 3.970   2.157   6.963   1.00 22.00  ? 528 ILE B O      1 
ATOM   3547 C CB     . ILE B 1 189 ? 3.030   0.627   4.177   1.00 22.40  ? 528 ILE B CB     1 
ATOM   3548 C CG1    . ILE B 1 189 ? 1.855   0.428   3.218   1.00 20.06  ? 528 ILE B CG1    1 
ATOM   3549 C CG2    . ILE B 1 189 ? 3.004   -0.405  5.301   1.00 30.51  ? 528 ILE B CG2    1 
ATOM   3550 C CD1    . ILE B 1 189 ? 1.853   -0.922  2.530   1.00 22.38  ? 528 ILE B CD1    1 
ATOM   3551 N N      . GLU B 1 190 ? 5.361   2.545   5.243   1.00 22.49  ? 529 GLU B N      1 
ATOM   3552 C CA     . GLU B 1 190 ? 6.537   2.637   6.098   1.00 23.83  ? 529 GLU B CA     1 
ATOM   3553 C C      . GLU B 1 190 ? 6.812   4.051   6.593   1.00 23.35  ? 529 GLU B C      1 
ATOM   3554 O O      . GLU B 1 190 ? 7.337   4.215   7.700   1.00 20.73  ? 529 GLU B O      1 
ATOM   3555 C CB     . GLU B 1 190 ? 7.765   2.099   5.358   1.00 27.05  ? 529 GLU B CB     1 
ATOM   3556 C CG     . GLU B 1 190 ? 7.651   0.627   4.981   1.00 34.45  ? 529 GLU B CG     1 
ATOM   3557 C CD     . GLU B 1 190 ? 8.903   0.085   4.317   1.00 35.98  ? 529 GLU B CD     1 
ATOM   3558 O OE1    . GLU B 1 190 ? 9.894   0.836   4.197   1.00 31.32  ? 529 GLU B OE1    1 
ATOM   3559 O OE2    . GLU B 1 190 ? 8.895   -1.098  3.914   1.00 42.80  ? 529 GLU B OE2    1 
ATOM   3560 N N      . ASN B 1 191 ? 6.465   5.078   5.812   1.00 20.21  ? 530 ASN B N      1 
ATOM   3561 C CA     . ASN B 1 191 ? 6.737   6.454   6.203   1.00 19.10  ? 530 ASN B CA     1 
ATOM   3562 C C      . ASN B 1 191 ? 5.562   7.399   5.988   1.00 21.53  ? 530 ASN B C      1 
ATOM   3563 O O      . ASN B 1 191 ? 5.696   8.595   6.267   1.00 21.98  ? 530 ASN B O      1 
ATOM   3564 C CB     . ASN B 1 191 ? 7.961   6.993   5.446   1.00 21.91  ? 530 ASN B CB     1 
ATOM   3565 C CG     . ASN B 1 191 ? 9.156   6.062   5.533   1.00 26.87  ? 530 ASN B CG     1 
ATOM   3566 O OD1    . ASN B 1 191 ? 9.923   6.101   6.497   1.00 28.60  ? 530 ASN B OD1    1 
ATOM   3567 N ND2    . ASN B 1 191 ? 9.320   5.216   4.522   1.00 25.93  ? 530 ASN B ND2    1 
ATOM   3568 N N      . GLY B 1 192 ? 4.422   6.905   5.508   1.00 22.11  ? 531 GLY B N      1 
ATOM   3569 C CA     . GLY B 1 192 ? 3.272   7.761   5.285   1.00 18.35  ? 531 GLY B CA     1 
ATOM   3570 C C      . GLY B 1 192 ? 3.478   8.833   4.243   1.00 20.51  ? 531 GLY B C      1 
ATOM   3571 O O      . GLY B 1 192 ? 2.813   9.871   4.294   1.00 18.74  ? 531 GLY B O      1 
ATOM   3572 N N      . LEU B 1 193 ? 4.383   8.613   3.291   1.00 19.20  ? 532 LEU B N      1 
ATOM   3573 C CA     . LEU B 1 193 ? 4.690   9.613   2.273   1.00 19.11  ? 532 LEU B CA     1 
ATOM   3574 C C      . LEU B 1 193 ? 3.589   9.605   1.222   1.00 20.04  ? 532 LEU B C      1 
ATOM   3575 O O      . LEU B 1 193 ? 3.448   8.639   0.466   1.00 23.15  ? 532 LEU B O      1 
ATOM   3576 C CB     . LEU B 1 193 ? 6.051   9.338   1.644   1.00 20.97  ? 532 LEU B CB     1 
ATOM   3577 C CG     . LEU B 1 193 ? 6.415   10.259  0.478   1.00 25.58  ? 532 LEU B CG     1 
ATOM   3578 C CD1    . LEU B 1 193 ? 6.409   11.716  0.916   1.00 24.62  ? 532 LEU B CD1    1 
ATOM   3579 C CD2    . LEU B 1 193 ? 7.764   9.876   -0.112  1.00 21.52  ? 532 LEU B CD2    1 
ATOM   3580 N N      . ILE B 1 194 ? 2.813   10.679  1.166   1.00 22.03  ? 533 ILE B N      1 
ATOM   3581 C CA     . ILE B 1 194 ? 1.690   10.792  0.245   1.00 18.49  ? 533 ILE B CA     1 
ATOM   3582 C C      . ILE B 1 194 ? 2.174   11.524  -1.001  1.00 22.30  ? 533 ILE B C      1 
ATOM   3583 O O      . ILE B 1 194 ? 2.480   12.721  -0.952  1.00 24.29  ? 533 ILE B O      1 
ATOM   3584 C CB     . ILE B 1 194 ? 0.501   11.510  0.895   1.00 21.50  ? 533 ILE B CB     1 
ATOM   3585 C CG1    . ILE B 1 194 ? 0.047   10.748  2.142   1.00 24.57  ? 533 ILE B CG1    1 
ATOM   3586 C CG2    . ILE B 1 194 ? -0.646  11.638  -0.091  1.00 25.59  ? 533 ILE B CG2    1 
ATOM   3587 C CD1    . ILE B 1 194 ? -1.125  11.368  2.854   1.00 26.67  ? 533 ILE B CD1    1 
ATOM   3588 N N      . THR B 1 195 ? 2.249   10.810  -2.124  1.00 21.57  ? 534 THR B N      1 
ATOM   3589 C CA     . THR B 1 195 ? 2.583   11.416  -3.408  1.00 19.38  ? 534 THR B CA     1 
ATOM   3590 C C      . THR B 1 195 ? 1.635   10.888  -4.479  1.00 20.62  ? 534 THR B C      1 
ATOM   3591 O O      . THR B 1 195 ? 0.964   9.874   -4.263  1.00 21.83  ? 534 THR B O      1 
ATOM   3592 C CB     . THR B 1 195 ? 4.036   11.114  -3.783  1.00 18.32  ? 534 THR B CB     1 
ATOM   3593 O OG1    . THR B 1 195 ? 4.204   9.696   -3.913  1.00 24.67  ? 534 THR B OG1    1 
ATOM   3594 C CG2    . THR B 1 195 ? 4.984   11.625  -2.701  1.00 20.79  ? 534 THR B CG2    1 
ATOM   3595 N N      . PRO B 1 196 ? 1.562   11.517  -5.652  1.00 18.83  ? 535 PRO B N      1 
ATOM   3596 C CA     . PRO B 1 196 ? 0.818   10.895  -6.759  1.00 20.72  ? 535 PRO B CA     1 
ATOM   3597 C C      . PRO B 1 196 ? 1.280   9.468   -7.080  1.00 20.92  ? 535 PRO B C      1 
ATOM   3598 O O      . PRO B 1 196 ? 0.581   8.761   -7.822  1.00 20.64  ? 535 PRO B O      1 
ATOM   3599 C CB     . PRO B 1 196 ? 1.073   11.849  -7.941  1.00 20.96  ? 535 PRO B CB     1 
ATOM   3600 C CG     . PRO B 1 196 ? 2.253   12.635  -7.563  1.00 23.29  ? 535 PRO B CG     1 
ATOM   3601 C CD     . PRO B 1 196 ? 2.207   12.772  -6.062  1.00 20.05  ? 535 PRO B CD     1 
ATOM   3602 N N      . LYS B 1 197 ? 2.442   9.036   -6.571  1.00 23.51  ? 536 LYS B N      1 
ATOM   3603 C CA     . LYS B 1 197 ? 2.932   7.688   -6.854  1.00 19.08  ? 536 LYS B CA     1 
ATOM   3604 C C      . LYS B 1 197 ? 2.115   6.617   -6.142  1.00 19.68  ? 536 LYS B C      1 
ATOM   3605 O O      . LYS B 1 197 ? 1.968   5.508   -6.668  1.00 22.91  ? 536 LYS B O      1 
ATOM   3606 C CB     . LYS B 1 197 ? 4.406   7.569   -6.467  1.00 21.07  ? 536 LYS B CB     1 
ATOM   3607 C CG     . LYS B 1 197 ? 5.313   8.480   -7.270  1.00 20.99  ? 536 LYS B CG     1 
ATOM   3608 C CD     . LYS B 1 197 ? 5.072   8.256   -8.755  1.00 20.83  ? 536 LYS B CD     1 
ATOM   3609 C CE     . LYS B 1 197 ? 6.053   9.030   -9.618  1.00 21.49  ? 536 LYS B CE     1 
ATOM   3610 N NZ     . LYS B 1 197 ? 5.826   8.790   -11.073 1.00 25.87  ? 536 LYS B NZ     1 
ATOM   3611 N N      . MET B 1 198 ? 1.593   6.910   -4.948  1.00 22.00  ? 537 MET B N      1 
ATOM   3612 C CA     . MET B 1 198 ? 0.771   5.920   -4.258  1.00 17.89  ? 537 MET B CA     1 
ATOM   3613 C C      . MET B 1 198 ? -0.488  5.599   -5.052  1.00 18.54  ? 537 MET B C      1 
ATOM   3614 O O      . MET B 1 198 ? -0.952  4.453   -5.040  1.00 19.91  ? 537 MET B O      1 
ATOM   3615 C CB     . MET B 1 198 ? 0.422   6.407   -2.851  1.00 17.41  ? 537 MET B CB     1 
ATOM   3616 C CG     . MET B 1 198 ? -0.608  7.517   -2.791  1.00 19.57  ? 537 MET B CG     1 
ATOM   3617 S SD     . MET B 1 198 ? -1.017  7.947   -1.086  1.00 28.39  ? 537 MET B SD     1 
ATOM   3618 C CE     . MET B 1 198 ? -1.464  6.343   -0.427  1.00 25.89  ? 537 MET B CE     1 
ATOM   3619 N N      . ASP B 1 199 ? -1.046  6.587   -5.757  1.00 21.86  ? 538 ASP B N      1 
ATOM   3620 C CA     . ASP B 1 199 ? -2.145  6.307   -6.676  1.00 18.51  ? 538 ASP B CA     1 
ATOM   3621 C C      . ASP B 1 199 ? -1.670  5.479   -7.864  1.00 15.75  ? 538 ASP B C      1 
ATOM   3622 O O      . ASP B 1 199 ? -2.377  4.572   -8.318  1.00 14.24  ? 538 ASP B O      1 
ATOM   3623 C CB     . ASP B 1 199 ? -2.784  7.613   -7.153  1.00 16.00  ? 538 ASP B CB     1 
ATOM   3624 C CG     . ASP B 1 199 ? -3.788  8.167   -6.161  1.00 21.76  ? 538 ASP B CG     1 
ATOM   3625 O OD1    . ASP B 1 199 ? -4.070  7.481   -5.155  1.00 20.22  ? 538 ASP B OD1    1 
ATOM   3626 O OD2    . ASP B 1 199 ? -4.299  9.285   -6.391  1.00 23.85  ? 538 ASP B OD2    1 
ATOM   3627 N N      . VAL B 1 200 ? -0.476  5.778   -8.383  1.00 14.33  ? 539 VAL B N      1 
ATOM   3628 C CA     . VAL B 1 200 ? 0.074   4.981   -9.476  1.00 21.02  ? 539 VAL B CA     1 
ATOM   3629 C C      . VAL B 1 200 ? 0.284   3.543   -9.025  1.00 19.44  ? 539 VAL B C      1 
ATOM   3630 O O      . VAL B 1 200 ? 0.068   2.595   -9.792  1.00 17.62  ? 539 VAL B O      1 
ATOM   3631 C CB     . VAL B 1 200 ? 1.382   5.609   -9.995  1.00 19.73  ? 539 VAL B CB     1 
ATOM   3632 C CG1    . VAL B 1 200 ? 2.040   4.695   -11.019 1.00 20.26  ? 539 VAL B CG1    1 
ATOM   3633 C CG2    . VAL B 1 200 ? 1.113   6.982   -10.593 1.00 17.90  ? 539 VAL B CG2    1 
ATOM   3634 N N      . PHE B 1 201 ? 0.705   3.358   -7.773  1.00 21.37  ? 540 PHE B N      1 
ATOM   3635 C CA     . PHE B 1 201 ? 0.871   2.016   -7.227  1.00 18.88  ? 540 PHE B CA     1 
ATOM   3636 C C      . PHE B 1 201 ? -0.449  1.253   -7.257  1.00 16.06  ? 540 PHE B C      1 
ATOM   3637 O O      . PHE B 1 201 ? -0.577  0.228   -7.936  1.00 20.01  ? 540 PHE B O      1 
ATOM   3638 C CB     . PHE B 1 201 ? 1.421   2.106   -5.802  1.00 19.09  ? 540 PHE B CB     1 
ATOM   3639 C CG     . PHE B 1 201 ? 1.839   0.784   -5.221  1.00 18.37  ? 540 PHE B CG     1 
ATOM   3640 C CD1    . PHE B 1 201 ? 0.932   -0.005  -4.533  1.00 18.67  ? 540 PHE B CD1    1 
ATOM   3641 C CD2    . PHE B 1 201 ? 3.142   0.339   -5.350  1.00 19.79  ? 540 PHE B CD2    1 
ATOM   3642 C CE1    . PHE B 1 201 ? 1.315   -1.217  -3.994  1.00 18.51  ? 540 PHE B CE1    1 
ATOM   3643 C CE2    . PHE B 1 201 ? 3.532   -0.873  -4.812  1.00 25.13  ? 540 PHE B CE2    1 
ATOM   3644 C CZ     . PHE B 1 201 ? 2.617   -1.652  -4.133  1.00 17.98  ? 540 PHE B CZ     1 
ATOM   3645 N N      . ALA B 1 202 ? -1.452  1.755   -6.529  1.00 17.82  ? 541 ALA B N      1 
ATOM   3646 C CA     . ALA B 1 202 ? -2.745  1.080   -6.463  1.00 17.29  ? 541 ALA B CA     1 
ATOM   3647 C C      . ALA B 1 202 ? -3.308  0.826   -7.856  1.00 18.13  ? 541 ALA B C      1 
ATOM   3648 O O      . ALA B 1 202 ? -3.775  -0.278  -8.159  1.00 18.09  ? 541 ALA B O      1 
ATOM   3649 C CB     . ALA B 1 202 ? -3.724  1.905   -5.628  1.00 12.74  ? 541 ALA B CB     1 
ATOM   3650 N N      . PHE B 1 203 ? -3.280  1.846   -8.719  1.00 16.85  ? 542 PHE B N      1 
ATOM   3651 C CA     . PHE B 1 203 ? -3.705  1.651   -10.100 1.00 14.60  ? 542 PHE B CA     1 
ATOM   3652 C C      . PHE B 1 203 ? -2.971  0.477   -10.732 1.00 18.92  ? 542 PHE B C      1 
ATOM   3653 O O      . PHE B 1 203 ? -3.556  -0.291  -11.506 1.00 21.60  ? 542 PHE B O      1 
ATOM   3654 C CB     . PHE B 1 203 ? -3.479  2.930   -10.909 1.00 14.55  ? 542 PHE B CB     1 
ATOM   3655 C CG     . PHE B 1 203 ? -4.069  2.888   -12.290 1.00 15.28  ? 542 PHE B CG     1 
ATOM   3656 C CD1    . PHE B 1 203 ? -5.348  2.396   -12.495 1.00 18.18  ? 542 PHE B CD1    1 
ATOM   3657 C CD2    . PHE B 1 203 ? -3.356  3.358   -13.381 1.00 16.75  ? 542 PHE B CD2    1 
ATOM   3658 C CE1    . PHE B 1 203 ? -5.902  2.358   -13.765 1.00 18.22  ? 542 PHE B CE1    1 
ATOM   3659 C CE2    . PHE B 1 203 ? -3.904  3.326   -14.654 1.00 17.40  ? 542 PHE B CE2    1 
ATOM   3660 C CZ     . PHE B 1 203 ? -5.179  2.825   -14.845 1.00 16.45  ? 542 PHE B CZ     1 
ATOM   3661 N N      . GLY B 1 204 ? -1.687  0.314   -10.406 1.00 16.42  ? 543 GLY B N      1 
ATOM   3662 C CA     . GLY B 1 204 ? -0.964  -0.858  -10.870 1.00 18.76  ? 543 GLY B CA     1 
ATOM   3663 C C      . GLY B 1 204 ? -1.603  -2.151  -10.402 1.00 21.48  ? 543 GLY B C      1 
ATOM   3664 O O      . GLY B 1 204 ? -1.751  -3.099  -11.178 1.00 18.13  ? 543 GLY B O      1 
ATOM   3665 N N      . VAL B 1 205 ? -2.000  -2.203  -9.128  1.00 22.86  ? 544 VAL B N      1 
ATOM   3666 C CA     . VAL B 1 205 ? -2.679  -3.387  -8.609  1.00 16.13  ? 544 VAL B CA     1 
ATOM   3667 C C      . VAL B 1 205 ? -4.016  -3.584  -9.309  1.00 17.59  ? 544 VAL B C      1 
ATOM   3668 O O      . VAL B 1 205 ? -4.412  -4.714  -9.619  1.00 18.02  ? 544 VAL B O      1 
ATOM   3669 C CB     . VAL B 1 205 ? -2.851  -3.280  -7.084  1.00 18.65  ? 544 VAL B CB     1 
ATOM   3670 C CG1    . VAL B 1 205 ? -3.786  -4.367  -6.581  1.00 19.69  ? 544 VAL B CG1    1 
ATOM   3671 C CG2    . VAL B 1 205 ? -1.500  -3.372  -6.392  1.00 16.76  ? 544 VAL B CG2    1 
ATOM   3672 N N      . VAL B 1 206 ? -4.736  -2.490  -9.566  1.00 16.51  ? 545 VAL B N      1 
ATOM   3673 C CA     . VAL B 1 206 ? -6.013  -2.595  -10.267 1.00 17.24  ? 545 VAL B CA     1 
ATOM   3674 C C      . VAL B 1 206 ? -5.808  -3.204  -11.646 1.00 19.69  ? 545 VAL B C      1 
ATOM   3675 O O      . VAL B 1 206 ? -6.569  -4.081  -12.074 1.00 22.14  ? 545 VAL B O      1 
ATOM   3676 C CB     . VAL B 1 206 ? -6.695  -1.218  -10.352 1.00 15.05  ? 545 VAL B CB     1 
ATOM   3677 C CG1    . VAL B 1 206 ? -7.920  -1.288  -11.249 1.00 12.13  ? 545 VAL B CG1    1 
ATOM   3678 C CG2    . VAL B 1 206 ? -7.072  -0.727  -8.965  1.00 16.14  ? 545 VAL B CG2    1 
ATOM   3679 N N      . ILE B 1 207 ? -4.776  -2.754  -12.363 1.00 17.19  ? 546 ILE B N      1 
ATOM   3680 C CA     . ILE B 1 207 ? -4.488  -3.311  -13.681 1.00 17.27  ? 546 ILE B CA     1 
ATOM   3681 C C      . ILE B 1 207 ? -4.211  -4.806  -13.578 1.00 19.24  ? 546 ILE B C      1 
ATOM   3682 O O      . ILE B 1 207 ? -4.679  -5.598  -14.405 1.00 20.97  ? 546 ILE B O      1 
ATOM   3683 C CB     . ILE B 1 207 ? -3.317  -2.556  -14.337 1.00 17.30  ? 546 ILE B CB     1 
ATOM   3684 C CG1    . ILE B 1 207 ? -3.700  -1.094  -14.588 1.00 17.80  ? 546 ILE B CG1    1 
ATOM   3685 C CG2    . ILE B 1 207 ? -2.897  -3.240  -15.631 1.00 15.56  ? 546 ILE B CG2    1 
ATOM   3686 C CD1    . ILE B 1 207 ? -2.570  -0.247  -15.126 1.00 19.14  ? 546 ILE B CD1    1 
ATOM   3687 N N      . LEU B 1 208 ? -3.453  -5.217  -12.559 1.00 17.89  ? 547 LEU B N      1 
ATOM   3688 C CA     . LEU B 1 208 ? -3.211  -6.641  -12.351 1.00 19.13  ? 547 LEU B CA     1 
ATOM   3689 C C      . LEU B 1 208 ? -4.501  -7.392  -12.043 1.00 21.25  ? 547 LEU B C      1 
ATOM   3690 O O      . LEU B 1 208 ? -4.658  -8.546  -12.458 1.00 21.78  ? 547 LEU B O      1 
ATOM   3691 C CB     . LEU B 1 208 ? -2.191  -6.842  -11.229 1.00 19.72  ? 547 LEU B CB     1 
ATOM   3692 C CG     . LEU B 1 208 ? -0.767  -6.351  -11.499 1.00 18.90  ? 547 LEU B CG     1 
ATOM   3693 C CD1    . LEU B 1 208 ? 0.102   -6.560  -10.272 1.00 20.64  ? 547 LEU B CD1    1 
ATOM   3694 C CD2    . LEU B 1 208 ? -0.168  -7.052  -12.712 1.00 20.39  ? 547 LEU B CD2    1 
ATOM   3695 N N      . GLU B 1 209 ? -5.428  -6.766  -11.310 1.00 18.55  ? 548 GLU B N      1 
ATOM   3696 C CA     . GLU B 1 209 ? -6.732  -7.386  -11.104 1.00 19.12  ? 548 GLU B CA     1 
ATOM   3697 C C      . GLU B 1 209 ? -7.463  -7.564  -12.427 1.00 19.88  ? 548 GLU B C      1 
ATOM   3698 O O      . GLU B 1 209 ? -8.114  -8.590  -12.653 1.00 20.49  ? 548 GLU B O      1 
ATOM   3699 C CB     . GLU B 1 209 ? -7.576  -6.548  -10.143 1.00 20.65  ? 548 GLU B CB     1 
ATOM   3700 C CG     . GLU B 1 209 ? -6.975  -6.369  -8.763  1.00 20.56  ? 548 GLU B CG     1 
ATOM   3701 C CD     . GLU B 1 209 ? -7.873  -5.569  -7.839  1.00 22.55  ? 548 GLU B CD     1 
ATOM   3702 O OE1    . GLU B 1 209 ? -9.036  -5.978  -7.637  1.00 25.18  ? 548 GLU B OE1    1 
ATOM   3703 O OE2    . GLU B 1 209 ? -7.417  -4.527  -7.320  1.00 23.67  ? 548 GLU B OE2    1 
ATOM   3704 N N      . LEU B 1 210 ? -7.372  -6.569  -13.312 1.00 18.71  ? 549 LEU B N      1 
ATOM   3705 C CA     . LEU B 1 210 ? -8.035  -6.667  -14.608 1.00 20.99  ? 549 LEU B CA     1 
ATOM   3706 C C      . LEU B 1 210 ? -7.437  -7.783  -15.457 1.00 23.54  ? 549 LEU B C      1 
ATOM   3707 O O      . LEU B 1 210 ? -8.170  -8.522  -16.125 1.00 20.28  ? 549 LEU B O      1 
ATOM   3708 C CB     . LEU B 1 210 ? -7.948  -5.325  -15.336 1.00 15.84  ? 549 LEU B CB     1 
ATOM   3709 C CG     . LEU B 1 210 ? -8.864  -4.224  -14.800 1.00 17.89  ? 549 LEU B CG     1 
ATOM   3710 C CD1    . LEU B 1 210 ? -8.459  -2.866  -15.345 1.00 14.41  ? 549 LEU B CD1    1 
ATOM   3711 C CD2    . LEU B 1 210 ? -10.311 -4.533  -15.158 1.00 20.52  ? 549 LEU B CD2    1 
ATOM   3712 N N      . LEU B 1 211 ? -6.110  -7.923  -15.441 1.00 21.77  ? 550 LEU B N      1 
ATOM   3713 C CA     . LEU B 1 211 ? -5.461  -8.948  -16.254 1.00 20.74  ? 550 LEU B CA     1 
ATOM   3714 C C      . LEU B 1 211 ? -5.744  -10.344 -15.712 1.00 21.13  ? 550 LEU B C      1 
ATOM   3715 O O      . LEU B 1 211 ? -6.108  -11.254 -16.466 1.00 20.18  ? 550 LEU B O      1 
ATOM   3716 C CB     . LEU B 1 211 ? -3.955  -8.692  -16.310 1.00 19.12  ? 550 LEU B CB     1 
ATOM   3717 C CG     . LEU B 1 211 ? -3.495  -7.363  -16.907 1.00 18.33  ? 550 LEU B CG     1 
ATOM   3718 C CD1    . LEU B 1 211 ? -2.024  -7.125  -16.602 1.00 22.94  ? 550 LEU B CD1    1 
ATOM   3719 C CD2    . LEU B 1 211 ? -3.741  -7.347  -18.405 1.00 22.55  ? 550 LEU B CD2    1 
ATOM   3720 N N      . SER B 1 212 ? -5.578  -10.531 -14.404 1.00 22.73  ? 551 SER B N      1 
ATOM   3721 C CA     . SER B 1 212 ? -5.653  -11.847 -13.788 1.00 19.90  ? 551 SER B CA     1 
ATOM   3722 C C      . SER B 1 212 ? -7.023  -12.178 -13.219 1.00 21.12  ? 551 SER B C      1 
ATOM   3723 O O      . SER B 1 212 ? -7.380  -13.358 -13.148 1.00 21.74  ? 551 SER B O      1 
ATOM   3724 C CB     . SER B 1 212 ? -4.617  -11.960 -12.665 1.00 22.28  ? 551 SER B CB     1 
ATOM   3725 O OG     . SER B 1 212 ? -4.889  -11.025 -11.635 1.00 20.31  ? 551 SER B OG     1 
ATOM   3726 N N      . GLY B 1 213 ? -7.795  -11.174 -12.810 1.00 22.08  ? 552 GLY B N      1 
ATOM   3727 C CA     . GLY B 1 213 ? -9.030  -11.435 -12.100 1.00 23.16  ? 552 GLY B CA     1 
ATOM   3728 C C      . GLY B 1 213 ? -8.847  -11.909 -10.677 1.00 19.64  ? 552 GLY B C      1 
ATOM   3729 O O      . GLY B 1 213 ? -9.834  -12.263 -10.024 1.00 18.95  ? 552 GLY B O      1 
ATOM   3730 N N      . ARG B 1 214 ? -7.616  -11.923 -10.174 1.00 18.82  ? 553 ARG B N      1 
ATOM   3731 C CA     . ARG B 1 214 ? -7.338  -12.412 -8.835  1.00 19.75  ? 553 ARG B CA     1 
ATOM   3732 C C      . ARG B 1 214 ? -7.595  -11.326 -7.796  1.00 22.94  ? 553 ARG B C      1 
ATOM   3733 O O      . ARG B 1 214 ? -7.682  -10.134 -8.106  1.00 21.75  ? 553 ARG B O      1 
ATOM   3734 C CB     . ARG B 1 214 ? -5.891  -12.892 -8.723  1.00 19.24  ? 553 ARG B CB     1 
ATOM   3735 C CG     . ARG B 1 214 ? -5.487  -13.914 -9.765  1.00 20.45  ? 553 ARG B CG     1 
ATOM   3736 C CD     . ARG B 1 214 ? -4.033  -14.301 -9.596  1.00 20.98  ? 553 ARG B CD     1 
ATOM   3737 N NE     . ARG B 1 214 ? -3.640  -15.365 -10.510 1.00 29.47  ? 553 ARG B NE     1 
ATOM   3738 C CZ     . ARG B 1 214 ? -2.454  -15.956 -10.499 1.00 33.87  ? 553 ARG B CZ     1 
ATOM   3739 N NH1    . ARG B 1 214 ? -1.517  -15.609 -9.632  1.00 33.79  ? 553 ARG B NH1    1 
ATOM   3740 N NH2    . ARG B 1 214 ? -2.202  -16.923 -11.379 1.00 30.98  ? 553 ARG B NH2    1 
ATOM   3741 N N      . GLU B 1 215 ? -7.715  -11.759 -6.545  1.00 22.06  ? 554 GLU B N      1 
ATOM   3742 C CA     . GLU B 1 215 ? -7.819  -10.837 -5.427  1.00 22.30  ? 554 GLU B CA     1 
ATOM   3743 C C      . GLU B 1 215 ? -6.452  -10.236 -5.122  1.00 23.24  ? 554 GLU B C      1 
ATOM   3744 O O      . GLU B 1 215 ? -5.418  -10.899 -5.252  1.00 21.96  ? 554 GLU B O      1 
ATOM   3745 C CB     . GLU B 1 215 ? -8.371  -11.552 -4.193  1.00 25.88  ? 554 GLU B CB     1 
ATOM   3746 C CG     . GLU B 1 215 ? -9.704  -12.265 -4.419  1.00 26.02  ? 554 GLU B CG     1 
ATOM   3747 C CD     . GLU B 1 215 ? -10.904 -11.379 -4.135  1.00 33.01  ? 554 GLU B CD     1 
ATOM   3748 O OE1    . GLU B 1 215 ? -10.705 -10.220 -3.712  1.00 36.35  ? 554 GLU B OE1    1 
ATOM   3749 O OE2    . GLU B 1 215 ? -12.047 -11.844 -4.328  1.00 36.31  ? 554 GLU B OE2    1 
ATOM   3750 N N      . VAL B 1 216 ? -6.453  -8.962  -4.719  1.00 22.65  ? 555 VAL B N      1 
ATOM   3751 C CA     . VAL B 1 216 ? -5.195  -8.276  -4.439  1.00 17.27  ? 555 VAL B CA     1 
ATOM   3752 C C      . VAL B 1 216 ? -4.390  -9.035  -3.396  1.00 22.17  ? 555 VAL B C      1 
ATOM   3753 O O      . VAL B 1 216 ? -3.154  -9.062  -3.452  1.00 22.07  ? 555 VAL B O      1 
ATOM   3754 C CB     . VAL B 1 216 ? -5.459  -6.823  -3.999  1.00 20.26  ? 555 VAL B CB     1 
ATOM   3755 C CG1    . VAL B 1 216 ? -6.282  -6.094  -5.050  1.00 23.64  ? 555 VAL B CG1    1 
ATOM   3756 C CG2    . VAL B 1 216 ? -6.156  -6.792  -2.647  1.00 25.51  ? 555 VAL B CG2    1 
ATOM   3757 N N      . VAL B 1 217 ? -5.065  -9.663  -2.438  1.00 21.91  ? 556 VAL B N      1 
ATOM   3758 C CA     . VAL B 1 217 ? -4.427  -10.482 -1.415  1.00 20.36  ? 556 VAL B CA     1 
ATOM   3759 C C      . VAL B 1 217 ? -5.036  -11.873 -1.514  1.00 23.51  ? 556 VAL B C      1 
ATOM   3760 O O      . VAL B 1 217 ? -6.203  -12.075 -1.155  1.00 22.47  ? 556 VAL B O      1 
ATOM   3761 C CB     . VAL B 1 217 ? -4.606  -9.896  -0.008  1.00 21.48  ? 556 VAL B CB     1 
ATOM   3762 C CG1    . VAL B 1 217 ? -3.990  -10.818 1.035   1.00 27.65  ? 556 VAL B CG1    1 
ATOM   3763 C CG2    . VAL B 1 217 ? -3.990  -8.507  0.069   1.00 24.35  ? 556 VAL B CG2    1 
ATOM   3764 N N      . GLY B 1 218 ? -4.253  -12.831 -2.010  1.00 23.90  ? 557 GLY B N      1 
ATOM   3765 C CA     . GLY B 1 218 ? -4.706  -14.189 -2.191  1.00 24.70  ? 557 GLY B CA     1 
ATOM   3766 C C      . GLY B 1 218 ? -4.015  -15.168 -1.254  1.00 34.03  ? 557 GLY B C      1 
ATOM   3767 O O      . GLY B 1 218 ? -3.191  -14.813 -0.414  1.00 37.62  ? 557 GLY B O      1 
ATOM   3768 N N      . SER B 1 219 ? -4.382  -16.434 -1.421  1.00 32.84  ? 558 SER B N      1 
ATOM   3769 C CA     . SER B 1 219 ? -3.804  -17.519 -0.642  1.00 29.55  ? 558 SER B CA     1 
ATOM   3770 C C      . SER B 1 219 ? -2.606  -18.085 -1.392  1.00 35.37  ? 558 SER B C      1 
ATOM   3771 O O      . SER B 1 219 ? -2.735  -18.511 -2.545  1.00 35.77  ? 558 SER B O      1 
ATOM   3772 C CB     . SER B 1 219 ? -4.839  -18.614 -0.389  1.00 39.01  ? 558 SER B CB     1 
ATOM   3773 O OG     . SER B 1 219 ? -6.063  -18.067 0.068   1.00 52.97  ? 558 SER B OG     1 
ATOM   3774 N N      . ASP B 1 220 ? -1.440  -18.076 -0.747  1.00 35.56  ? 559 ASP B N      1 
ATOM   3775 C CA     . ASP B 1 220 ? -0.288  -18.764 -1.312  1.00 37.01  ? 559 ASP B CA     1 
ATOM   3776 C C      . ASP B 1 220 ? -0.603  -20.251 -1.385  1.00 40.39  ? 559 ASP B C      1 
ATOM   3777 O O      . ASP B 1 220 ? -0.771  -20.904 -0.351  1.00 39.64  ? 559 ASP B O      1 
ATOM   3778 C CB     . ASP B 1 220 ? 0.971   -18.511 -0.478  1.00 36.55  ? 559 ASP B CB     1 
ATOM   3779 C CG     . ASP B 1 220 ? 2.231   -19.037 -1.147  1.00 39.59  ? 559 ASP B CG     1 
ATOM   3780 O OD1    . ASP B 1 220 ? 2.123   -19.920 -2.025  1.00 41.55  ? 559 ASP B OD1    1 
ATOM   3781 O OD2    . ASP B 1 220 ? 3.334   -18.568 -0.793  1.00 35.13  ? 559 ASP B OD2    1 
ATOM   3782 N N      . LYS B 1 221 ? -0.708  -20.794 -2.597  1.00 38.91  ? 560 LYS B N      1 
ATOM   3783 C CA     . LYS B 1 221 ? -1.103  -22.188 -2.759  1.00 38.37  ? 560 LYS B CA     1 
ATOM   3784 C C      . LYS B 1 221 ? 0.084   -23.139 -2.846  1.00 43.12  ? 560 LYS B C      1 
ATOM   3785 O O      . LYS B 1 221 ? -0.002  -24.266 -2.344  1.00 45.09  ? 560 LYS B O      1 
ATOM   3786 C CB     . LYS B 1 221 ? -1.988  -22.340 -3.999  1.00 40.60  ? 560 LYS B CB     1 
ATOM   3787 C CG     . LYS B 1 221 ? -3.325  -21.627 -3.878  1.00 38.91  ? 560 LYS B CG     1 
ATOM   3788 C CD     . LYS B 1 221 ? -4.236  -21.941 -5.049  1.00 42.24  ? 560 LYS B CD     1 
ATOM   3789 C CE     . LYS B 1 221 ? -5.609  -21.313 -4.860  1.00 47.90  ? 560 LYS B CE     1 
ATOM   3790 N NZ     . LYS B 1 221 ? -6.515  -21.602 -6.008  1.00 49.63  ? 560 LYS B NZ     1 
ATOM   3791 N N      . SER B 1 222 ? 1.189   -22.721 -3.469  1.00 62.46  ? 561 SER B N      1 
ATOM   3792 C CA     . SER B 1 222 ? 2.382   -23.563 -3.485  1.00 58.59  ? 561 SER B CA     1 
ATOM   3793 C C      . SER B 1 222 ? 2.843   -23.868 -2.066  1.00 54.75  ? 561 SER B C      1 
ATOM   3794 O O      . SER B 1 222 ? 3.156   -25.017 -1.734  1.00 56.35  ? 561 SER B O      1 
ATOM   3795 C CB     . SER B 1 222 ? 3.496   -22.884 -4.284  1.00 66.15  ? 561 SER B CB     1 
ATOM   3796 O OG     . SER B 1 222 ? 4.611   -23.746 -4.442  1.00 94.49  ? 561 SER B OG     1 
ATOM   3797 N N      . ASN B 1 223 ? 2.901   -22.844 -1.218  1.00 41.21  ? 562 ASN B N      1 
ATOM   3798 C CA     . ASN B 1 223 ? 3.161   -23.016 0.204   1.00 39.97  ? 562 ASN B CA     1 
ATOM   3799 C C      . ASN B 1 223 ? 1.830   -23.129 0.935   1.00 39.36  ? 562 ASN B C      1 
ATOM   3800 O O      . ASN B 1 223 ? 0.958   -22.269 0.785   1.00 43.11  ? 562 ASN B O      1 
ATOM   3801 C CB     . ASN B 1 223 ? 3.977   -21.843 0.750   1.00 36.01  ? 562 ASN B CB     1 
ATOM   3802 C CG     . ASN B 1 223 ? 4.307   -21.993 2.225   1.00 37.65  ? 562 ASN B CG     1 
ATOM   3803 O OD1    . ASN B 1 223 ? 4.396   -23.107 2.747   1.00 37.19  ? 562 ASN B OD1    1 
ATOM   3804 N ND2    . ASN B 1 223 ? 4.489   -20.865 2.905   1.00 33.69  ? 562 ASN B ND2    1 
ATOM   3805 N N      . GLY B 1 224 ? 1.681   -24.187 1.726   1.00 34.33  ? 563 GLY B N      1 
ATOM   3806 C CA     . GLY B 1 224 ? 0.411   -24.501 2.353   1.00 36.76  ? 563 GLY B CA     1 
ATOM   3807 C C      . GLY B 1 224 ? -0.234  -23.384 3.150   1.00 32.58  ? 563 GLY B C      1 
ATOM   3808 O O      . GLY B 1 224 ? -1.419  -23.469 3.485   1.00 32.54  ? 563 GLY B O      1 
ATOM   3809 N N      . LEU B 1 225 ? 0.522   -22.331 3.457   1.00 33.55  ? 564 LEU B N      1 
ATOM   3810 C CA     . LEU B 1 225 ? 0.039   -21.251 4.307   1.00 33.52  ? 564 LEU B CA     1 
ATOM   3811 C C      . LEU B 1 225 ? 0.544   -19.919 3.769   1.00 30.01  ? 564 LEU B C      1 
ATOM   3812 O O      . LEU B 1 225 ? 1.274   -19.859 2.775   1.00 35.01  ? 564 LEU B O      1 
ATOM   3813 C CB     . LEU B 1 225 ? 0.482   -21.455 5.762   1.00 29.83  ? 564 LEU B CB     1 
ATOM   3814 C CG     . LEU B 1 225 ? -0.050  -22.696 6.478   1.00 31.59  ? 564 LEU B CG     1 
ATOM   3815 C CD1    . LEU B 1 225 ? 0.501   -22.773 7.891   1.00 31.87  ? 564 LEU B CD1    1 
ATOM   3816 C CD2    . LEU B 1 225 ? -1.569  -22.691 6.493   1.00 32.04  ? 564 LEU B CD2    1 
ATOM   3817 N N      . GLY B 1 226 ? 0.148   -18.842 4.440   1.00 29.14  ? 565 GLY B N      1 
ATOM   3818 C CA     . GLY B 1 226 ? 0.593   -17.508 4.098   1.00 31.83  ? 565 GLY B CA     1 
ATOM   3819 C C      . GLY B 1 226 ? -0.249  -16.867 3.008   1.00 35.46  ? 565 GLY B C      1 
ATOM   3820 O O      . GLY B 1 226 ? -0.976  -17.525 2.265   1.00 39.42  ? 565 GLY B O      1 
ATOM   3821 N N      . ASP B 1 227 ? -0.137  -15.545 2.921   1.00 34.85  ? 566 ASP B N      1 
ATOM   3822 C CA     . ASP B 1 227 ? -0.809  -14.760 1.897   1.00 32.45  ? 566 ASP B CA     1 
ATOM   3823 C C      . ASP B 1 227 ? 0.134   -14.485 0.733   1.00 34.28  ? 566 ASP B C      1 
ATOM   3824 O O      . ASP B 1 227 ? 1.358   -14.571 0.856   1.00 36.87  ? 566 ASP B O      1 
ATOM   3825 C CB     . ASP B 1 227 ? -1.325  -13.438 2.471   1.00 34.15  ? 566 ASP B CB     1 
ATOM   3826 C CG     . ASP B 1 227 ? -2.435  -13.632 3.482   1.00 33.95  ? 566 ASP B CG     1 
ATOM   3827 O OD1    . ASP B 1 227 ? -3.132  -14.667 3.410   1.00 37.94  ? 566 ASP B OD1    1 
ATOM   3828 O OD2    . ASP B 1 227 ? -2.613  -12.747 4.345   1.00 32.11  ? 566 ASP B OD2    1 
ATOM   3829 N N      . GLN B 1 228 ? -0.459  -14.148 -0.410  1.00 33.16  ? 567 GLN B N      1 
ATOM   3830 C CA     . GLN B 1 228 ? 0.289   -13.831 -1.619  1.00 30.53  ? 567 GLN B CA     1 
ATOM   3831 C C      . GLN B 1 228 ? -0.228  -12.512 -2.168  1.00 28.37  ? 567 GLN B C      1 
ATOM   3832 O O      . GLN B 1 228 ? -1.407  -12.406 -2.524  1.00 28.35  ? 567 GLN B O      1 
ATOM   3833 C CB     . GLN B 1 228 ? 0.154   -14.947 -2.659  1.00 32.48  ? 567 GLN B CB     1 
ATOM   3834 C CG     . GLN B 1 228 ? 1.135   -14.846 -3.812  1.00 32.90  ? 567 GLN B CG     1 
ATOM   3835 C CD     . GLN B 1 228 ? 0.995   -15.991 -4.793  1.00 38.24  ? 567 GLN B CD     1 
ATOM   3836 O OE1    . GLN B 1 228 ? -0.026  -16.680 -4.817  1.00 38.07  ? 567 GLN B OE1    1 
ATOM   3837 N NE2    . GLN B 1 228 ? 2.024   -16.204 -5.607  1.00 41.36  ? 567 GLN B NE2    1 
ATOM   3838 N N      . LEU B 1 229 ? 0.644   -11.511 -2.228  1.00 26.85  ? 568 LEU B N      1 
ATOM   3839 C CA     . LEU B 1 229 ? 0.249   -10.192 -2.697  1.00 25.62  ? 568 LEU B CA     1 
ATOM   3840 C C      . LEU B 1 229 ? 0.282   -10.132 -4.218  1.00 24.17  ? 568 LEU B C      1 
ATOM   3841 O O      . LEU B 1 229 ? 1.223   -10.612 -4.855  1.00 23.77  ? 568 LEU B O      1 
ATOM   3842 C CB     . LEU B 1 229 ? 1.162   -9.118  -2.105  1.00 23.90  ? 568 LEU B CB     1 
ATOM   3843 C CG     . LEU B 1 229 ? 1.153   -9.005  -0.579  1.00 30.18  ? 568 LEU B CG     1 
ATOM   3844 C CD1    . LEU B 1 229 ? 1.997   -7.827  -0.116  1.00 32.11  ? 568 LEU B CD1    1 
ATOM   3845 C CD2    . LEU B 1 229 ? -0.272  -8.887  -0.056  1.00 27.69  ? 568 LEU B CD2    1 
ATOM   3846 N N      . LEU B 1 230 ? -0.759  -9.530  -4.797  1.00 25.74  ? 569 LEU B N      1 
ATOM   3847 C CA     . LEU B 1 230 ? -0.857  -9.461  -6.251  1.00 24.71  ? 569 LEU B CA     1 
ATOM   3848 C C      . LEU B 1 230 ? 0.268   -8.621  -6.844  1.00 25.64  ? 569 LEU B C      1 
ATOM   3849 O O      . LEU B 1 230 ? 0.836   -8.978  -7.883  1.00 24.52  ? 569 LEU B O      1 
ATOM   3850 C CB     . LEU B 1 230 ? -2.221  -8.901  -6.655  1.00 20.77  ? 569 LEU B CB     1 
ATOM   3851 C CG     . LEU B 1 230 ? -2.549  -8.923  -8.147  1.00 21.84  ? 569 LEU B CG     1 
ATOM   3852 C CD1    . LEU B 1 230 ? -2.376  -10.326 -8.706  1.00 17.67  ? 569 LEU B CD1    1 
ATOM   3853 C CD2    . LEU B 1 230 ? -3.962  -8.418  -8.390  1.00 20.54  ? 569 LEU B CD2    1 
ATOM   3854 N N      . ALA B 1 231 ? 0.609   -7.503  -6.196  1.00 27.13  ? 570 ALA B N      1 
ATOM   3855 C CA     . ALA B 1 231 ? 1.669   -6.645  -6.714  1.00 23.74  ? 570 ALA B CA     1 
ATOM   3856 C C      . ALA B 1 231 ? 2.994   -7.388  -6.824  1.00 25.28  ? 570 ALA B C      1 
ATOM   3857 O O      . ALA B 1 231 ? 3.794   -7.096  -7.720  1.00 25.25  ? 570 ALA B O      1 
ATOM   3858 C CB     . ALA B 1 231 ? 1.827   -5.408  -5.830  1.00 24.16  ? 570 ALA B CB     1 
ATOM   3859 N N      . SER B 1 232 ? 3.244   -8.348  -5.931  1.00 23.66  ? 571 SER B N      1 
ATOM   3860 C CA     . SER B 1 232 ? 4.515   -9.064  -5.951  1.00 27.38  ? 571 SER B CA     1 
ATOM   3861 C C      . SER B 1 232 ? 4.517   -10.211 -6.953  1.00 27.93  ? 571 SER B C      1 
ATOM   3862 O O      . SER B 1 232 ? 5.582   -10.580 -7.460  1.00 29.09  ? 571 SER B O      1 
ATOM   3863 C CB     . SER B 1 232 ? 4.851   -9.589  -4.553  1.00 24.35  ? 571 SER B CB     1 
ATOM   3864 O OG     . SER B 1 232 ? 3.935   -10.591 -4.146  1.00 31.41  ? 571 SER B OG     1 
ATOM   3865 N N      . THR B 1 233 ? 3.349   -10.785 -7.254  1.00 27.79  ? 572 THR B N      1 
ATOM   3866 C CA     . THR B 1 233 ? 3.308   -11.901 -8.194  1.00 28.02  ? 572 THR B CA     1 
ATOM   3867 C C      . THR B 1 233 ? 3.695   -11.466 -9.602  1.00 27.77  ? 572 THR B C      1 
ATOM   3868 O O      . THR B 1 233 ? 4.252   -12.265 -10.363 1.00 32.80  ? 572 THR B O      1 
ATOM   3869 C CB     . THR B 1 233 ? 1.919   -12.541 -8.203  1.00 25.70  ? 572 THR B CB     1 
ATOM   3870 O OG1    . THR B 1 233 ? 0.964   -11.617 -8.738  1.00 35.45  ? 572 THR B OG1    1 
ATOM   3871 C CG2    . THR B 1 233 ? 1.504   -12.932 -6.793  1.00 25.88  ? 572 THR B CG2    1 
ATOM   3872 N N      . VAL B 1 234 ? 3.414   -10.213 -9.968  1.00 27.20  ? 573 VAL B N      1 
ATOM   3873 C CA     . VAL B 1 234 ? 3.778   -9.741  -11.300 1.00 25.03  ? 573 VAL B CA     1 
ATOM   3874 C C      . VAL B 1 234 ? 5.288   -9.760  -11.482 1.00 27.67  ? 573 VAL B C      1 
ATOM   3875 O O      . VAL B 1 234 ? 5.785   -10.018 -12.585 1.00 30.24  ? 573 VAL B O      1 
ATOM   3876 C CB     . VAL B 1 234 ? 3.199   -8.335  -11.551 1.00 28.86  ? 573 VAL B CB     1 
ATOM   3877 C CG1    . VAL B 1 234 ? 3.916   -7.303  -10.696 1.00 25.04  ? 573 VAL B CG1    1 
ATOM   3878 C CG2    . VAL B 1 234 ? 3.296   -7.979  -13.029 1.00 30.76  ? 573 VAL B CG2    1 
ATOM   3879 N N      . ASN B 1 235 ? 6.042   -9.488  -10.414 1.00 27.62  ? 574 ASN B N      1 
ATOM   3880 C CA     . ASN B 1 235 ? 7.498   -9.554  -10.501 1.00 29.74  ? 574 ASN B CA     1 
ATOM   3881 C C      . ASN B 1 235 ? 7.956   -10.962 -10.855 1.00 35.36  ? 574 ASN B C      1 
ATOM   3882 O O      . ASN B 1 235 ? 8.780   -11.153 -11.758 1.00 36.07  ? 574 ASN B O      1 
ATOM   3883 C CB     . ASN B 1 235 ? 8.123   -9.099  -9.182  1.00 31.11  ? 574 ASN B CB     1 
ATOM   3884 C CG     . ASN B 1 235 ? 7.718   -7.689  -8.799  1.00 29.65  ? 574 ASN B CG     1 
ATOM   3885 O OD1    . ASN B 1 235 ? 7.581   -6.814  -9.655  1.00 29.98  ? 574 ASN B OD1    1 
ATOM   3886 N ND2    . ASN B 1 235 ? 7.522   -7.462  -7.504  1.00 30.02  ? 574 ASN B ND2    1 
ATOM   3887 N N      . GLN B 1 236 ? 7.430   -11.966 -10.149 1.00 33.49  ? 575 GLN B N      1 
ATOM   3888 C CA     . GLN B 1 236 ? 7.780   -13.349 -10.457 1.00 34.51  ? 575 GLN B CA     1 
ATOM   3889 C C      . GLN B 1 236 ? 7.378   -13.712 -11.881 1.00 34.52  ? 575 GLN B C      1 
ATOM   3890 O O      . GLN B 1 236 ? 8.116   -14.412 -12.585 1.00 37.42  ? 575 GLN B O      1 
ATOM   3891 C CB     . GLN B 1 236 ? 7.109   -14.295 -9.462  1.00 39.48  ? 575 GLN B CB     1 
ATOM   3892 C CG     . GLN B 1 236 ? 7.158   -13.831 -8.016  1.00 56.40  ? 575 GLN B CG     1 
ATOM   3893 C CD     . GLN B 1 236 ? 6.380   -14.748 -7.091  1.00 59.33  ? 575 GLN B CD     1 
ATOM   3894 O OE1    . GLN B 1 236 ? 5.995   -15.852 -7.476  1.00 66.75  ? 575 GLN B OE1    1 
ATOM   3895 N NE2    . GLN B 1 236 ? 6.140   -14.292 -5.866  1.00 51.18  ? 575 GLN B NE2    1 
ATOM   3896 N N      . VAL B 1 237 ? 6.209   -13.242 -12.324 1.00 28.38  ? 576 VAL B N      1 
ATOM   3897 C CA     . VAL B 1 237 ? 5.705   -13.630 -13.636 1.00 26.91  ? 576 VAL B CA     1 
ATOM   3898 C C      . VAL B 1 237 ? 6.552   -13.035 -14.752 1.00 33.75  ? 576 VAL B C      1 
ATOM   3899 O O      . VAL B 1 237 ? 6.732   -13.663 -15.803 1.00 35.06  ? 576 VAL B O      1 
ATOM   3900 C CB     . VAL B 1 237 ? 4.226   -13.226 -13.777 1.00 25.73  ? 576 VAL B CB     1 
ATOM   3901 C CG1    . VAL B 1 237 ? 3.768   -13.397 -15.214 1.00 24.95  ? 576 VAL B CG1    1 
ATOM   3902 C CG2    . VAL B 1 237 ? 3.363   -14.050 -12.837 1.00 23.71  ? 576 VAL B CG2    1 
ATOM   3903 N N      . LEU B 1 238 ? 7.085   -11.831 -14.558 1.00 31.78  ? 577 LEU B N      1 
ATOM   3904 C CA     . LEU B 1 238 ? 7.842   -11.148 -15.597 1.00 29.69  ? 577 LEU B CA     1 
ATOM   3905 C C      . LEU B 1 238 ? 9.350   -11.258 -15.416 1.00 39.17  ? 577 LEU B C      1 
ATOM   3906 O O      . LEU B 1 238 ? 10.099  -10.701 -16.225 1.00 40.94  ? 577 LEU B O      1 
ATOM   3907 C CB     . LEU B 1 238 ? 7.432   -9.674  -15.659 1.00 30.60  ? 577 LEU B CB     1 
ATOM   3908 C CG     . LEU B 1 238 ? 5.957   -9.440  -15.987 1.00 32.34  ? 577 LEU B CG     1 
ATOM   3909 C CD1    . LEU B 1 238 ? 5.656   -7.956  -16.134 1.00 33.48  ? 577 LEU B CD1    1 
ATOM   3910 C CD2    . LEU B 1 238 ? 5.560   -10.201 -17.242 1.00 30.10  ? 577 LEU B CD2    1 
ATOM   3911 N N      . GLU B 1 239 ? 9.815   -11.962 -14.389 1.00 39.24  ? 578 GLU B N      1 
ATOM   3912 C CA     . GLU B 1 239 ? 11.243  -12.129 -14.163 1.00 35.82  ? 578 GLU B CA     1 
ATOM   3913 C C      . GLU B 1 239 ? 11.763  -13.353 -14.905 1.00 35.25  ? 578 GLU B C      1 
ATOM   3914 O O      . GLU B 1 239 ? 11.054  -14.348 -15.079 1.00 38.15  ? 578 GLU B O      1 
ATOM   3915 C CB     . GLU B 1 239 ? 11.550  -12.271 -12.672 1.00 38.48  ? 578 GLU B CB     1 
ATOM   3916 C CG     . GLU B 1 239 ? 11.265  -13.659 -12.121 1.00 40.37  ? 578 GLU B CG     1 
ATOM   3917 C CD     . GLU B 1 239 ? 11.779  -13.847 -10.708 1.00 46.91  ? 578 GLU B CD     1 
ATOM   3918 O OE1    . GLU B 1 239 ? 12.669  -13.077 -10.288 1.00 50.15  ? 578 GLU B OE1    1 
ATOM   3919 O OE2    . GLU B 1 239 ? 11.291  -14.766 -10.017 1.00 52.90  ? 578 GLU B OE2    1 
ATOM   3920 N N      . GLY B 1 240 ? 13.017  -13.267 -15.342 1.00 39.26  ? 579 GLY B N      1 
ATOM   3921 C CA     . GLY B 1 240 ? 13.680  -14.416 -15.926 1.00 40.37  ? 579 GLY B CA     1 
ATOM   3922 C C      . GLY B 1 240 ? 13.085  -14.835 -17.260 1.00 43.36  ? 579 GLY B C      1 
ATOM   3923 O O      . GLY B 1 240 ? 12.556  -14.024 -18.027 1.00 46.17  ? 579 GLY B O      1 
ATOM   3924 N N      . ASP B 1 241 ? 13.176  -16.132 -17.534 1.00 41.60  ? 580 ASP B N      1 
ATOM   3925 C CA     . ASP B 1 241 ? 12.752  -16.708 -18.800 1.00 44.45  ? 580 ASP B CA     1 
ATOM   3926 C C      . ASP B 1 241 ? 11.408  -17.412 -18.651 1.00 41.21  ? 580 ASP B C      1 
ATOM   3927 O O      . ASP B 1 241 ? 10.907  -17.636 -17.546 1.00 38.89  ? 580 ASP B O      1 
ATOM   3928 C CB     . ASP B 1 241 ? 13.810  -17.685 -19.319 1.00 47.01  ? 580 ASP B CB     1 
ATOM   3929 C CG     . ASP B 1 241 ? 15.193  -17.070 -19.373 1.00 47.02  ? 580 ASP B CG     1 
ATOM   3930 O OD1    . ASP B 1 241 ? 15.317  -15.921 -19.844 1.00 48.98  ? 580 ASP B OD1    1 
ATOM   3931 O OD2    . ASP B 1 241 ? 16.156  -17.734 -18.934 1.00 52.82  ? 580 ASP B OD2    1 
ATOM   3932 N N      . ASN B 1 242 ? 10.825  -17.766 -19.797 1.00 43.25  ? 581 ASN B N      1 
ATOM   3933 C CA     . ASN B 1 242 ? 9.543   -18.462 -19.854 1.00 42.61  ? 581 ASN B CA     1 
ATOM   3934 C C      . ASN B 1 242 ? 8.395   -17.581 -19.375 1.00 40.58  ? 581 ASN B C      1 
ATOM   3935 O O      . ASN B 1 242 ? 7.442   -18.067 -18.762 1.00 41.71  ? 581 ASN B O      1 
ATOM   3936 C CB     . ASN B 1 242 ? 9.585   -19.768 -19.055 1.00 33.95  ? 581 ASN B CB     1 
ATOM   3937 C CG     . ASN B 1 242 ? 10.660  -20.715 -19.550 1.00 42.87  ? 581 ASN B CG     1 
ATOM   3938 O OD1    . ASN B 1 242 ? 11.777  -20.732 -19.031 1.00 46.98  ? 581 ASN B OD1    1 
ATOM   3939 N ND2    . ASN B 1 242 ? 10.332  -21.504 -20.566 1.00 48.93  ? 581 ASN B ND2    1 
ATOM   3940 N N      . VAL B 1 243 ? 8.480   -16.278 -19.653 1.00 37.58  ? 582 VAL B N      1 
ATOM   3941 C CA     . VAL B 1 243 ? 7.422   -15.360 -19.248 1.00 37.49  ? 582 VAL B CA     1 
ATOM   3942 C C      . VAL B 1 243 ? 6.140   -15.633 -20.023 1.00 37.46  ? 582 VAL B C      1 
ATOM   3943 O O      . VAL B 1 243 ? 5.040   -15.324 -19.547 1.00 30.67  ? 582 VAL B O      1 
ATOM   3944 C CB     . VAL B 1 243 ? 7.890   -13.904 -19.422 1.00 38.20  ? 582 VAL B CB     1 
ATOM   3945 C CG1    . VAL B 1 243 ? 6.751   -12.940 -19.139 1.00 33.14  ? 582 VAL B CG1    1 
ATOM   3946 C CG2    . VAL B 1 243 ? 9.077   -13.618 -18.513 1.00 37.88  ? 582 VAL B CG2    1 
ATOM   3947 N N      . ARG B 1 244 ? 6.251   -16.214 -21.220 1.00 40.83  ? 583 ARG B N      1 
ATOM   3948 C CA     . ARG B 1 244 ? 5.063   -16.543 -22.002 1.00 33.18  ? 583 ARG B CA     1 
ATOM   3949 C C      . ARG B 1 244 ? 4.146   -17.482 -21.228 1.00 32.81  ? 583 ARG B C      1 
ATOM   3950 O O      . ARG B 1 244 ? 2.984   -17.158 -20.958 1.00 30.77  ? 583 ARG B O      1 
ATOM   3951 C CB     . ARG B 1 244 ? 5.470   -17.164 -23.338 1.00 36.90  ? 583 ARG B CB     1 
ATOM   3952 C CG     . ARG B 1 244 ? 4.298   -17.664 -24.166 1.00 43.46  ? 583 ARG B CG     1 
ATOM   3953 C CD     . ARG B 1 244 ? 4.753   -18.226 -25.505 1.00 46.07  ? 583 ARG B CD     1 
ATOM   3954 N NE     . ARG B 1 244 ? 3.628   -18.428 -26.411 1.00 51.47  ? 583 ARG B NE     1 
ATOM   3955 C CZ     . ARG B 1 244 ? 3.745   -18.722 -27.699 1.00 51.85  ? 583 ARG B CZ     1 
ATOM   3956 N NH1    . ARG B 1 244 ? 4.930   -18.866 -28.270 1.00 57.83  ? 583 ARG B NH1    1 
ATOM   3957 N NH2    . ARG B 1 244 ? 2.646   -18.874 -28.432 1.00 50.68  ? 583 ARG B NH2    1 
ATOM   3958 N N      . GLU B 1 245 ? 4.657   -18.660 -20.862 1.00 33.03  ? 584 GLU B N      1 
ATOM   3959 C CA     . GLU B 1 245 ? 3.854   -19.612 -20.101 1.00 32.12  ? 584 GLU B CA     1 
ATOM   3960 C C      . GLU B 1 245 ? 3.352   -18.990 -18.804 1.00 30.80  ? 584 GLU B C      1 
ATOM   3961 O O      . GLU B 1 245 ? 2.165   -19.090 -18.470 1.00 28.95  ? 584 GLU B O      1 
ATOM   3962 C CB     . GLU B 1 245 ? 4.667   -20.875 -19.809 1.00 34.00  ? 584 GLU B CB     1 
ATOM   3963 C CG     . GLU B 1 245 ? 4.960   -21.736 -21.027 1.00 41.34  ? 584 GLU B CG     1 
ATOM   3964 C CD     . GLU B 1 245 ? 5.954   -21.094 -21.975 1.00 50.13  ? 584 GLU B CD     1 
ATOM   3965 O OE1    . GLU B 1 245 ? 6.931   -20.484 -21.489 1.00 47.57  ? 584 GLU B OE1    1 
ATOM   3966 O OE2    . GLU B 1 245 ? 5.752   -21.195 -23.205 1.00 58.67  ? 584 GLU B OE2    1 
ATOM   3967 N N      . LYS B 1 246 ? 4.247   -18.338 -18.059 1.00 30.97  ? 585 LYS B N      1 
ATOM   3968 C CA     . LYS B 1 246 ? 3.860   -17.765 -16.775 1.00 25.11  ? 585 LYS B CA     1 
ATOM   3969 C C      . LYS B 1 246 ? 2.779   -16.706 -16.945 1.00 27.70  ? 585 LYS B C      1 
ATOM   3970 O O      . LYS B 1 246 ? 1.839   -16.633 -16.145 1.00 31.39  ? 585 LYS B O      1 
ATOM   3971 C CB     . LYS B 1 246 ? 5.085   -17.184 -16.070 1.00 26.44  ? 585 LYS B CB     1 
ATOM   3972 C CG     . LYS B 1 246 ? 6.138   -18.222 -15.720 1.00 33.26  ? 585 LYS B CG     1 
ATOM   3973 C CD     . LYS B 1 246 ? 7.214   -17.648 -14.814 1.00 31.99  ? 585 LYS B CD     1 
ATOM   3974 C CE     . LYS B 1 246 ? 8.002   -16.556 -15.512 1.00 29.67  ? 585 LYS B CE     1 
ATOM   3975 N NZ     . LYS B 1 246 ? 9.054   -15.992 -14.624 1.00 30.78  ? 585 LYS B NZ     1 
ATOM   3976 N N      . LEU B 1 247 ? 2.888   -15.878 -17.986 1.00 27.05  ? 586 LEU B N      1 
ATOM   3977 C CA     . LEU B 1 247 ? 1.866   -14.865 -18.228 1.00 23.86  ? 586 LEU B CA     1 
ATOM   3978 C C      . LEU B 1 247 ? 0.538   -15.509 -18.612 1.00 26.18  ? 586 LEU B C      1 
ATOM   3979 O O      . LEU B 1 247 ? -0.519  -15.130 -18.093 1.00 25.52  ? 586 LEU B O      1 
ATOM   3980 C CB     . LEU B 1 247 ? 2.332   -13.894 -19.312 1.00 23.24  ? 586 LEU B CB     1 
ATOM   3981 C CG     . LEU B 1 247 ? 1.388   -12.731 -19.626 1.00 22.15  ? 586 LEU B CG     1 
ATOM   3982 C CD1    . LEU B 1 247 ? 0.983   -12.009 -18.351 1.00 19.54  ? 586 LEU B CD1    1 
ATOM   3983 C CD2    . LEU B 1 247 ? 2.040   -11.765 -20.605 1.00 27.75  ? 586 LEU B CD2    1 
ATOM   3984 N N      . ARG B 1 248 ? 0.572   -16.488 -19.522 1.00 25.48  ? 587 ARG B N      1 
ATOM   3985 C CA     . ARG B 1 248 ? -0.661  -17.163 -19.916 1.00 23.91  ? 587 ARG B CA     1 
ATOM   3986 C C      . ARG B 1 248 ? -1.340  -17.812 -18.717 1.00 27.96  ? 587 ARG B C      1 
ATOM   3987 O O      . ARG B 1 248 ? -2.570  -17.777 -18.597 1.00 33.41  ? 587 ARG B O      1 
ATOM   3988 C CB     . ARG B 1 248 ? -0.378  -18.202 -21.001 1.00 28.84  ? 587 ARG B CB     1 
ATOM   3989 C CG     . ARG B 1 248 ? -0.039  -17.603 -22.356 1.00 33.33  ? 587 ARG B CG     1 
ATOM   3990 C CD     . ARG B 1 248 ? -0.101  -18.643 -23.468 1.00 36.66  ? 587 ARG B CD     1 
ATOM   3991 N NE     . ARG B 1 248 ? 0.741   -19.800 -23.191 1.00 50.50  ? 587 ARG B NE     1 
ATOM   3992 C CZ     . ARG B 1 248 ? 0.283   -21.004 -22.879 1.00 63.62  ? 587 ARG B CZ     1 
ATOM   3993 N NH1    . ARG B 1 248 ? -1.015  -21.256 -22.819 1.00 57.28  ? 587 ARG B NH1    1 
ATOM   3994 N NH2    . ARG B 1 248 ? 1.148   -21.983 -22.628 1.00 63.31  ? 587 ARG B NH2    1 
ATOM   3995 N N      . GLY B 1 249 ? -0.557  -18.410 -17.816 1.00 24.52  ? 588 GLY B N      1 
ATOM   3996 C CA     . GLY B 1 249 ? -1.138  -18.971 -16.609 1.00 26.37  ? 588 GLY B CA     1 
ATOM   3997 C C      . GLY B 1 249 ? -1.626  -17.913 -15.640 1.00 27.54  ? 588 GLY B C      1 
ATOM   3998 O O      . GLY B 1 249 ? -2.567  -18.150 -14.877 1.00 28.54  ? 588 GLY B O      1 
ATOM   3999 N N      . PHE B 1 250 ? -1.002  -16.733 -15.660 1.00 27.56  ? 589 PHE B N      1 
ATOM   4000 C CA     . PHE B 1 250 ? -1.403  -15.648 -14.773 1.00 22.70  ? 589 PHE B CA     1 
ATOM   4001 C C      . PHE B 1 250 ? -2.662  -14.945 -15.266 1.00 26.02  ? 589 PHE B C      1 
ATOM   4002 O O      . PHE B 1 250 ? -3.444  -14.440 -14.452 1.00 28.75  ? 589 PHE B O      1 
ATOM   4003 C CB     . PHE B 1 250 ? -0.252  -14.651 -14.632 1.00 22.35  ? 589 PHE B CB     1 
ATOM   4004 C CG     . PHE B 1 250 ? -0.569  -13.465 -13.767 1.00 26.06  ? 589 PHE B CG     1 
ATOM   4005 C CD1    . PHE B 1 250 ? -0.616  -13.589 -12.388 1.00 25.43  ? 589 PHE B CD1    1 
ATOM   4006 C CD2    . PHE B 1 250 ? -0.800  -12.220 -14.332 1.00 23.65  ? 589 PHE B CD2    1 
ATOM   4007 C CE1    . PHE B 1 250 ? -0.902  -12.497 -11.588 1.00 27.20  ? 589 PHE B CE1    1 
ATOM   4008 C CE2    . PHE B 1 250 ? -1.085  -11.126 -13.538 1.00 24.12  ? 589 PHE B CE2    1 
ATOM   4009 C CZ     . PHE B 1 250 ? -1.135  -11.265 -12.164 1.00 19.19  ? 589 PHE B CZ     1 
ATOM   4010 N N      . MET B 1 251 ? -2.877  -14.910 -16.579 1.00 25.98  ? 590 MET B N      1 
ATOM   4011 C CA     . MET B 1 251 ? -4.037  -14.228 -17.136 1.00 25.42  ? 590 MET B CA     1 
ATOM   4012 C C      . MET B 1 251 ? -5.330  -14.855 -16.626 1.00 22.50  ? 590 MET B C      1 
ATOM   4013 O O      . MET B 1 251 ? -5.403  -16.056 -16.357 1.00 22.40  ? 590 MET B O      1 
ATOM   4014 C CB     . MET B 1 251 ? -3.994  -14.273 -18.663 1.00 19.72  ? 590 MET B CB     1 
ATOM   4015 C CG     . MET B 1 251 ? -2.886  -13.433 -19.276 1.00 19.33  ? 590 MET B CG     1 
ATOM   4016 S SD     . MET B 1 251 ? -3.111  -11.674 -18.963 1.00 25.55  ? 590 MET B SD     1 
ATOM   4017 C CE     . MET B 1 251 ? -4.710  -11.403 -19.723 1.00 20.79  ? 590 MET B CE     1 
ATOM   4018 N N      . ASP B 1 252 ? -6.357  -14.021 -16.500 1.00 21.52  ? 591 ASP B N      1 
ATOM   4019 C CA     . ASP B 1 252 ? -7.647  -14.462 -15.989 1.00 24.35  ? 591 ASP B CA     1 
ATOM   4020 C C      . ASP B 1 252 ? -8.187  -15.609 -16.836 1.00 26.58  ? 591 ASP B C      1 
ATOM   4021 O O      . ASP B 1 252 ? -8.312  -15.461 -18.062 1.00 28.20  ? 591 ASP B O      1 
ATOM   4022 C CB     . ASP B 1 252 ? -8.639  -13.300 -15.980 1.00 25.78  ? 591 ASP B CB     1 
ATOM   4023 C CG     . ASP B 1 252 ? -9.937  -13.641 -15.266 1.00 25.18  ? 591 ASP B CG     1 
ATOM   4024 O OD1    . ASP B 1 252 ? -10.346 -14.821 -15.283 1.00 25.77  ? 591 ASP B OD1    1 
ATOM   4025 O OD2    . ASP B 1 252 ? -10.552 -12.723 -14.684 1.00 28.10  ? 591 ASP B OD2    1 
ATOM   4026 N N      . PRO B 1 253 ? -8.516  -16.756 -16.238 1.00 25.26  ? 592 PRO B N      1 
ATOM   4027 C CA     . PRO B 1 253 ? -9.084  -17.854 -17.035 1.00 28.43  ? 592 PRO B CA     1 
ATOM   4028 C C      . PRO B 1 253 ? -10.381 -17.482 -17.733 1.00 31.68  ? 592 PRO B C      1 
ATOM   4029 O O      . PRO B 1 253 ? -10.649 -17.986 -18.830 1.00 34.58  ? 592 PRO B O      1 
ATOM   4030 C CB     . PRO B 1 253 ? -9.300  -18.964 -15.995 1.00 27.92  ? 592 PRO B CB     1 
ATOM   4031 C CG     . PRO B 1 253 ? -8.373  -18.625 -14.871 1.00 26.20  ? 592 PRO B CG     1 
ATOM   4032 C CD     . PRO B 1 253 ? -8.326  -17.130 -14.827 1.00 25.49  ? 592 PRO B CD     1 
ATOM   4033 N N      . ASN B 1 254 ? -11.194 -16.609 -17.131 1.00 28.80  ? 593 ASN B N      1 
ATOM   4034 C CA     . ASN B 1 254 ? -12.470 -16.239 -17.734 1.00 31.70  ? 593 ASN B CA     1 
ATOM   4035 C C      . ASN B 1 254 ? -12.299 -15.602 -19.106 1.00 33.40  ? 593 ASN B C      1 
ATOM   4036 O O      . ASN B 1 254 ? -13.225 -15.658 -19.922 1.00 36.05  ? 593 ASN B O      1 
ATOM   4037 C CB     . ASN B 1 254 ? -13.234 -15.292 -16.808 1.00 31.84  ? 593 ASN B CB     1 
ATOM   4038 C CG     . ASN B 1 254 ? -13.619 -15.946 -15.498 1.00 32.55  ? 593 ASN B CG     1 
ATOM   4039 O OD1    . ASN B 1 254 ? -13.195 -15.514 -14.426 1.00 39.49  ? 593 ASN B OD1    1 
ATOM   4040 N ND2    . ASN B 1 254 ? -14.426 -16.998 -15.577 1.00 32.68  ? 593 ASN B ND2    1 
ATOM   4041 N N      . LEU B 1 255 ? -11.146 -14.992 -19.376 1.00 34.49  ? 594 LEU B N      1 
ATOM   4042 C CA     . LEU B 1 255 ? -10.869 -14.468 -20.707 1.00 36.30  ? 594 LEU B CA     1 
ATOM   4043 C C      . LEU B 1 255 ? -10.639 -15.566 -21.734 1.00 39.88  ? 594 LEU B C      1 
ATOM   4044 O O      . LEU B 1 255 ? -10.480 -15.254 -22.920 1.00 38.17  ? 594 LEU B O      1 
ATOM   4045 C CB     . LEU B 1 255 ? -9.652  -13.542 -20.661 1.00 29.02  ? 594 LEU B CB     1 
ATOM   4046 C CG     . LEU B 1 255 ? -9.806  -12.250 -19.860 1.00 27.42  ? 594 LEU B CG     1 
ATOM   4047 C CD1    . LEU B 1 255 ? -8.451  -11.599 -19.641 1.00 22.81  ? 594 LEU B CD1    1 
ATOM   4048 C CD2    . LEU B 1 255 ? -10.752 -11.295 -20.568 1.00 27.91  ? 594 LEU B CD2    1 
ATOM   4049 N N      . ARG B 1 256 ? -10.628 -16.832 -21.315 1.00 39.44  ? 595 ARG B N      1 
ATOM   4050 C CA     . ARG B 1 256 ? -10.288 -17.930 -22.209 1.00 42.11  ? 595 ARG B CA     1 
ATOM   4051 C C      . ARG B 1 256 ? -8.981  -17.606 -22.919 1.00 46.69  ? 595 ARG B C      1 
ATOM   4052 O O      . ARG B 1 256 ? -7.965  -17.340 -22.269 1.00 58.82  ? 595 ARG B O      1 
ATOM   4053 C CB     . ARG B 1 256 ? -11.419 -18.185 -23.209 1.00 44.69  ? 595 ARG B CB     1 
ATOM   4054 C CG     . ARG B 1 256 ? -12.779 -18.418 -22.553 1.00 54.06  ? 595 ARG B CG     1 
ATOM   4055 C CD     . ARG B 1 256 ? -13.686 -19.296 -23.412 1.00 67.11  ? 595 ARG B CD     1 
ATOM   4056 N NE     . ARG B 1 256 ? -14.281 -18.580 -24.535 1.00 68.67  ? 595 ARG B NE     1 
ATOM   4057 C CZ     . ARG B 1 256 ? -15.534 -18.146 -24.568 1.00 68.80  ? 595 ARG B CZ     1 
ATOM   4058 N NH1    . ARG B 1 256 ? -16.356 -18.328 -23.548 1.00 69.57  ? 595 ARG B NH1    1 
ATOM   4059 N NH2    . ARG B 1 256 ? -15.975 -17.518 -25.655 1.00 61.68  ? 595 ARG B NH2    1 
ATOM   4060 N N      . ASP B 1 257 ? -8.995  -17.612 -24.252 1.00 44.66  ? 596 ASP B N      1 
ATOM   4061 C CA     . ASP B 1 257 ? -7.852  -17.172 -25.042 1.00 39.39  ? 596 ASP B CA     1 
ATOM   4062 C C      . ASP B 1 257 ? -8.206  -15.985 -25.929 1.00 35.79  ? 596 ASP B C      1 
ATOM   4063 O O      . ASP B 1 257 ? -7.531  -15.738 -26.934 1.00 37.31  ? 596 ASP B O      1 
ATOM   4064 C CB     . ASP B 1 257 ? -7.305  -18.328 -25.881 1.00 45.04  ? 596 ASP B CB     1 
ATOM   4065 C CG     . ASP B 1 257 ? -6.816  -19.484 -25.028 1.00 51.71  ? 596 ASP B CG     1 
ATOM   4066 O OD1    . ASP B 1 257 ? -6.263  -19.224 -23.938 1.00 46.11  ? 596 ASP B OD1    1 
ATOM   4067 O OD2    . ASP B 1 257 ? -6.989  -20.649 -25.444 1.00 64.41  ? 596 ASP B OD2    1 
ATOM   4068 N N      . GLU B 1 258 ? -9.252  -15.243 -25.571 1.00 32.68  ? 597 GLU B N      1 
ATOM   4069 C CA     . GLU B 1 258 ? -9.738  -14.129 -26.383 1.00 34.26  ? 597 GLU B CA     1 
ATOM   4070 C C      . GLU B 1 258 ? -9.124  -12.809 -25.914 1.00 31.57  ? 597 GLU B C      1 
ATOM   4071 O O      . GLU B 1 258 ? -9.803  -11.892 -25.454 1.00 30.12  ? 597 GLU B O      1 
ATOM   4072 C CB     . GLU B 1 258 ? -11.260 -14.079 -26.346 1.00 35.71  ? 597 GLU B CB     1 
ATOM   4073 C CG     . GLU B 1 258 ? -11.922 -15.362 -26.819 1.00 38.03  ? 597 GLU B CG     1 
ATOM   4074 C CD     . GLU B 1 258 ? -13.429 -15.249 -26.880 1.00 45.77  ? 597 GLU B CD     1 
ATOM   4075 O OE1    . GLU B 1 258 ? -13.962 -14.204 -26.450 1.00 43.19  ? 597 GLU B OE1    1 
ATOM   4076 O OE2    . GLU B 1 258 ? -14.080 -16.201 -27.361 1.00 51.00  ? 597 GLU B OE2    1 
ATOM   4077 N N      . TYR B 1 259 ? -7.801  -12.734 -26.046 1.00 29.02  ? 598 TYR B N      1 
ATOM   4078 C CA     . TYR B 1 259 ? -7.053  -11.529 -25.720 1.00 26.17  ? 598 TYR B CA     1 
ATOM   4079 C C      . TYR B 1 259 ? -5.712  -11.603 -26.427 1.00 26.15  ? 598 TYR B C      1 
ATOM   4080 O O      . TYR B 1 259 ? -5.196  -12.703 -26.650 1.00 28.10  ? 598 TYR B O      1 
ATOM   4081 C CB     . TYR B 1 259 ? -6.853  -11.387 -24.204 1.00 24.07  ? 598 TYR B CB     1 
ATOM   4082 C CG     . TYR B 1 259 ? -5.926  -12.423 -23.606 1.00 27.48  ? 598 TYR B CG     1 
ATOM   4083 C CD1    . TYR B 1 259 ? -4.553  -12.211 -23.560 1.00 26.46  ? 598 TYR B CD1    1 
ATOM   4084 C CD2    . TYR B 1 259 ? -6.421  -13.611 -23.084 1.00 31.15  ? 598 TYR B CD2    1 
ATOM   4085 C CE1    . TYR B 1 259 ? -3.702  -13.154 -23.017 1.00 23.83  ? 598 TYR B CE1    1 
ATOM   4086 C CE2    . TYR B 1 259 ? -5.577  -14.559 -22.537 1.00 24.89  ? 598 TYR B CE2    1 
ATOM   4087 C CZ     . TYR B 1 259 ? -4.219  -14.324 -22.506 1.00 22.78  ? 598 TYR B CZ     1 
ATOM   4088 O OH     . TYR B 1 259 ? -3.371  -15.261 -21.965 1.00 23.46  ? 598 TYR B OH     1 
ATOM   4089 N N      . PRO B 1 260 ? -5.127  -10.462 -26.798 1.00 25.70  ? 599 PRO B N      1 
ATOM   4090 C CA     . PRO B 1 260 ? -3.783  -10.468 -27.395 1.00 25.75  ? 599 PRO B CA     1 
ATOM   4091 C C      . PRO B 1 260 ? -2.730  -10.634 -26.309 1.00 23.93  ? 599 PRO B C      1 
ATOM   4092 O O      . PRO B 1 260 ? -2.615  -9.801  -25.408 1.00 24.96  ? 599 PRO B O      1 
ATOM   4093 C CB     . PRO B 1 260 ? -3.692  -9.093  -28.068 1.00 26.26  ? 599 PRO B CB     1 
ATOM   4094 C CG     . PRO B 1 260 ? -4.574  -8.227  -27.230 1.00 25.45  ? 599 PRO B CG     1 
ATOM   4095 C CD     . PRO B 1 260 ? -5.703  -9.107  -26.742 1.00 25.60  ? 599 PRO B CD     1 
ATOM   4096 N N      . LEU B 1 261 ? -1.959  -11.721 -26.395 1.00 25.25  ? 600 LEU B N      1 
ATOM   4097 C CA     . LEU B 1 261 ? -0.973  -12.009 -25.358 1.00 23.40  ? 600 LEU B CA     1 
ATOM   4098 C C      . LEU B 1 261 ? 0.108   -10.937 -25.312 1.00 24.59  ? 600 LEU B C      1 
ATOM   4099 O O      . LEU B 1 261 ? 0.467   -10.446 -24.235 1.00 27.20  ? 600 LEU B O      1 
ATOM   4100 C CB     . LEU B 1 261 ? -0.353  -13.387 -25.586 1.00 22.72  ? 600 LEU B CB     1 
ATOM   4101 C CG     . LEU B 1 261 ? 0.735   -13.772 -24.584 1.00 27.73  ? 600 LEU B CG     1 
ATOM   4102 C CD1    . LEU B 1 261 ? 0.183   -13.754 -23.168 1.00 29.14  ? 600 LEU B CD1    1 
ATOM   4103 C CD2    . LEU B 1 261 ? 1.322   -15.136 -24.917 1.00 32.56  ? 600 LEU B CD2    1 
ATOM   4104 N N      . ASP B 1 262 ? 0.645   -10.563 -26.476 1.00 25.77  ? 601 ASP B N      1 
ATOM   4105 C CA     . ASP B 1 262 ? 1.697   -9.552  -26.510 1.00 27.66  ? 601 ASP B CA     1 
ATOM   4106 C C      . ASP B 1 262 ? 1.227   -8.246  -25.883 1.00 25.29  ? 601 ASP B C      1 
ATOM   4107 O O      . ASP B 1 262 ? 1.984   -7.588  -25.159 1.00 25.32  ? 601 ASP B O      1 
ATOM   4108 C CB     . ASP B 1 262 ? 2.159   -9.323  -27.948 1.00 29.24  ? 601 ASP B CB     1 
ATOM   4109 C CG     . ASP B 1 262 ? 1.042   -8.839  -28.846 1.00 28.54  ? 601 ASP B CG     1 
ATOM   4110 O OD1    . ASP B 1 262 ? -0.119  -9.242  -28.619 1.00 30.38  ? 601 ASP B OD1    1 
ATOM   4111 O OD2    . ASP B 1 262 ? 1.323   -8.056  -29.776 1.00 32.21  ? 601 ASP B OD2    1 
ATOM   4112 N N      . LEU B 1 263 ? -0.020  -7.852  -26.148 1.00 26.35  ? 602 LEU B N      1 
ATOM   4113 C CA     . LEU B 1 263 ? -0.550  -6.640  -25.534 1.00 27.17  ? 602 LEU B CA     1 
ATOM   4114 C C      . LEU B 1 263 ? -0.811  -6.849  -24.047 1.00 26.85  ? 602 LEU B C      1 
ATOM   4115 O O      . LEU B 1 263 ? -0.583  -5.942  -23.237 1.00 25.43  ? 602 LEU B O      1 
ATOM   4116 C CB     . LEU B 1 263 ? -1.820  -6.197  -26.262 1.00 24.32  ? 602 LEU B CB     1 
ATOM   4117 C CG     . LEU B 1 263 ? -1.574  -5.734  -27.702 1.00 23.14  ? 602 LEU B CG     1 
ATOM   4118 C CD1    . LEU B 1 263 ? -2.865  -5.285  -28.367 1.00 20.36  ? 602 LEU B CD1    1 
ATOM   4119 C CD2    . LEU B 1 263 ? -0.529  -4.626  -27.736 1.00 23.15  ? 602 LEU B CD2    1 
ATOM   4120 N N      . ALA B 1 264 ? -1.286  -8.038  -23.668 1.00 25.18  ? 603 ALA B N      1 
ATOM   4121 C CA     . ALA B 1 264 ? -1.413  -8.359  -22.250 1.00 24.31  ? 603 ALA B CA     1 
ATOM   4122 C C      . ALA B 1 264 ? -0.065  -8.258  -21.550 1.00 27.99  ? 603 ALA B C      1 
ATOM   4123 O O      . ALA B 1 264 ? 0.022   -7.761  -20.420 1.00 27.48  ? 603 ALA B O      1 
ATOM   4124 C CB     . ALA B 1 264 ? -2.010  -9.755  -22.076 1.00 21.02  ? 603 ALA B CB     1 
ATOM   4125 N N      . PHE B 1 265 ? 1.000   -8.727  -22.207 1.00 24.57  ? 604 PHE B N      1 
ATOM   4126 C CA     . PHE B 1 265 ? 2.344   -8.558  -21.664 1.00 26.82  ? 604 PHE B CA     1 
ATOM   4127 C C      . PHE B 1 265 ? 2.660   -7.084  -21.450 1.00 29.77  ? 604 PHE B C      1 
ATOM   4128 O O      . PHE B 1 265 ? 3.129   -6.685  -20.377 1.00 27.81  ? 604 PHE B O      1 
ATOM   4129 C CB     . PHE B 1 265 ? 3.367   -9.203  -22.601 1.00 26.31  ? 604 PHE B CB     1 
ATOM   4130 C CG     . PHE B 1 265 ? 4.792   -8.829  -22.301 1.00 28.99  ? 604 PHE B CG     1 
ATOM   4131 C CD1    . PHE B 1 265 ? 5.432   -9.321  -21.176 1.00 30.95  ? 604 PHE B CD1    1 
ATOM   4132 C CD2    . PHE B 1 265 ? 5.499   -8.000  -23.156 1.00 30.98  ? 604 PHE B CD2    1 
ATOM   4133 C CE1    . PHE B 1 265 ? 6.746   -8.983  -20.903 1.00 34.21  ? 604 PHE B CE1    1 
ATOM   4134 C CE2    . PHE B 1 265 ? 6.814   -7.660  -22.889 1.00 32.56  ? 604 PHE B CE2    1 
ATOM   4135 C CZ     . PHE B 1 265 ? 7.437   -8.152  -21.761 1.00 32.42  ? 604 PHE B CZ     1 
ATOM   4136 N N      . SER B 1 266 ? 2.403   -6.258  -22.467 1.00 26.40  ? 605 SER B N      1 
ATOM   4137 C CA     . SER B 1 266 ? 2.617   -4.821  -22.332 1.00 26.18  ? 605 SER B CA     1 
ATOM   4138 C C      . SER B 1 266 ? 1.859   -4.262  -21.135 1.00 27.08  ? 605 SER B C      1 
ATOM   4139 O O      . SER B 1 266 ? 2.401   -3.460  -20.366 1.00 25.06  ? 605 SER B O      1 
ATOM   4140 C CB     . SER B 1 266 ? 2.190   -4.109  -23.614 1.00 25.45  ? 605 SER B CB     1 
ATOM   4141 O OG     . SER B 1 266 ? 2.854   -4.648  -24.742 1.00 31.97  ? 605 SER B OG     1 
ATOM   4142 N N      . MET B 1 267 ? 0.602   -4.676  -20.961 1.00 24.48  ? 606 MET B N      1 
ATOM   4143 C CA     . MET B 1 267 ? -0.192  -4.167  -19.848 1.00 26.40  ? 606 MET B CA     1 
ATOM   4144 C C      . MET B 1 267 ? 0.331   -4.675  -18.510 1.00 27.14  ? 606 MET B C      1 
ATOM   4145 O O      . MET B 1 267 ? 0.271   -3.952  -17.509 1.00 24.24  ? 606 MET B O      1 
ATOM   4146 C CB     . MET B 1 267 ? -1.661  -4.548  -20.036 1.00 23.20  ? 606 MET B CB     1 
ATOM   4147 C CG     . MET B 1 267 ? -2.634  -3.659  -19.280 1.00 26.97  ? 606 MET B CG     1 
ATOM   4148 S SD     . MET B 1 267 ? -4.340  -3.908  -19.804 1.00 27.85  ? 606 MET B SD     1 
ATOM   4149 C CE     . MET B 1 267 ? -4.213  -3.531  -21.547 1.00 22.68  ? 606 MET B CE     1 
ATOM   4150 N N      . ALA B 1 268 ? 0.843   -5.908  -18.470 1.00 27.34  ? 607 ALA B N      1 
ATOM   4151 C CA     . ALA B 1 268 ? 1.491   -6.391  -17.256 1.00 26.22  ? 607 ALA B CA     1 
ATOM   4152 C C      . ALA B 1 268 ? 2.821   -5.689  -17.022 1.00 29.49  ? 607 ALA B C      1 
ATOM   4153 O O      . ALA B 1 268 ? 3.217   -5.479  -15.870 1.00 28.74  ? 607 ALA B O      1 
ATOM   4154 C CB     . ALA B 1 268 ? 1.693   -7.904  -17.330 1.00 23.80  ? 607 ALA B CB     1 
ATOM   4155 N N      . GLU B 1 269 ? 3.518   -5.314  -18.097 1.00 27.81  ? 608 GLU B N      1 
ATOM   4156 C CA     . GLU B 1 269 ? 4.791   -4.616  -17.952 1.00 28.07  ? 608 GLU B CA     1 
ATOM   4157 C C      . GLU B 1 269 ? 4.597   -3.255  -17.296 1.00 24.74  ? 608 GLU B C      1 
ATOM   4158 O O      . GLU B 1 269 ? 5.302   -2.908  -16.341 1.00 30.39  ? 608 GLU B O      1 
ATOM   4159 C CB     . GLU B 1 269 ? 5.466   -4.464  -19.315 1.00 28.27  ? 608 GLU B CB     1 
ATOM   4160 C CG     . GLU B 1 269 ? 6.883   -3.919  -19.244 1.00 33.58  ? 608 GLU B CG     1 
ATOM   4161 C CD     . GLU B 1 269 ? 7.864   -4.930  -18.682 1.00 41.38  ? 608 GLU B CD     1 
ATOM   4162 O OE1    . GLU B 1 269 ? 7.641   -6.145  -18.876 1.00 40.00  ? 608 GLU B OE1    1 
ATOM   4163 O OE2    . GLU B 1 269 ? 8.855   -4.513  -18.045 1.00 46.59  ? 608 GLU B OE2    1 
ATOM   4164 N N      . ILE B 1 270 ? 3.646   -2.466  -17.798 1.00 23.38  ? 609 ILE B N      1 
ATOM   4165 C CA     . ILE B 1 270 ? 3.402   -1.150  -17.218 1.00 24.67  ? 609 ILE B CA     1 
ATOM   4166 C C      . ILE B 1 270 ? 2.866   -1.287  -15.799 1.00 23.48  ? 609 ILE B C      1 
ATOM   4167 O O      . ILE B 1 270 ? 3.226   -0.509  -14.907 1.00 24.99  ? 609 ILE B O      1 
ATOM   4168 C CB     . ILE B 1 270 ? 2.448   -0.338  -18.114 1.00 25.22  ? 609 ILE B CB     1 
ATOM   4169 C CG1    . ILE B 1 270 ? 2.430   1.130   -17.681 1.00 25.41  ? 609 ILE B CG1    1 
ATOM   4170 C CG2    . ILE B 1 270 ? 1.045   -0.935  -18.088 1.00 24.58  ? 609 ILE B CG2    1 
ATOM   4171 C CD1    . ILE B 1 270 ? 3.795   1.789   -17.713 1.00 25.17  ? 609 ILE B CD1    1 
ATOM   4172 N N      . ALA B 1 271 ? 2.004   -2.279  -15.564 1.00 21.73  ? 610 ALA B N      1 
ATOM   4173 C CA     . ALA B 1 271 ? 1.517   -2.528  -14.212 1.00 21.15  ? 610 ALA B CA     1 
ATOM   4174 C C      . ALA B 1 271 ? 2.660   -2.905  -13.281 1.00 25.69  ? 610 ALA B C      1 
ATOM   4175 O O      . ALA B 1 271 ? 2.664   -2.525  -12.103 1.00 25.00  ? 610 ALA B O      1 
ATOM   4176 C CB     . ALA B 1 271 ? 0.453   -3.624  -14.229 1.00 19.54  ? 610 ALA B CB     1 
ATOM   4177 N N      . LYS B 1 272 ? 3.638   -3.658  -13.788 1.00 25.06  ? 611 LYS B N      1 
ATOM   4178 C CA     . LYS B 1 272 ? 4.813   -3.979  -12.985 1.00 25.81  ? 611 LYS B CA     1 
ATOM   4179 C C      . LYS B 1 272 ? 5.549   -2.711  -12.571 1.00 23.15  ? 611 LYS B C      1 
ATOM   4180 O O      . LYS B 1 272 ? 5.926   -2.549  -11.405 1.00 23.26  ? 611 LYS B O      1 
ATOM   4181 C CB     . LYS B 1 272 ? 5.741   -4.915  -13.760 1.00 26.62  ? 611 LYS B CB     1 
ATOM   4182 C CG     . LYS B 1 272 ? 7.014   -5.284  -13.010 1.00 29.05  ? 611 LYS B CG     1 
ATOM   4183 C CD     . LYS B 1 272 ? 7.957   -6.104  -13.878 1.00 32.70  ? 611 LYS B CD     1 
ATOM   4184 C CE     . LYS B 1 272 ? 9.207   -6.499  -13.111 1.00 36.33  ? 611 LYS B CE     1 
ATOM   4185 N NZ     . LYS B 1 272 ? 10.165  -7.250  -13.967 1.00 46.03  ? 611 LYS B NZ     1 
ATOM   4186 N N      . ARG B 1 273 ? 5.756   -1.792  -13.518 1.00 24.20  ? 612 ARG B N      1 
ATOM   4187 C CA     . ARG B 1 273 ? 6.444   -0.546  -13.199 1.00 21.22  ? 612 ARG B CA     1 
ATOM   4188 C C      . ARG B 1 273 ? 5.641   0.305   -12.224 1.00 21.50  ? 612 ARG B C      1 
ATOM   4189 O O      . ARG B 1 273 ? 6.222   1.080   -11.455 1.00 27.07  ? 612 ARG B O      1 
ATOM   4190 C CB     . ARG B 1 273 ? 6.727   0.238   -14.480 1.00 21.00  ? 612 ARG B CB     1 
ATOM   4191 C CG     . ARG B 1 273 ? 7.473   -0.553  -15.544 1.00 27.44  ? 612 ARG B CG     1 
ATOM   4192 C CD     . ARG B 1 273 ? 7.767   0.304   -16.763 1.00 27.36  ? 612 ARG B CD     1 
ATOM   4193 N NE     . ARG B 1 273 ? 8.417   -0.457  -17.823 1.00 37.92  ? 612 ARG B NE     1 
ATOM   4194 C CZ     . ARG B 1 273 ? 8.861   0.067   -18.958 1.00 38.99  ? 612 ARG B CZ     1 
ATOM   4195 N NH1    . ARG B 1 273 ? 8.753   1.361   -19.211 1.00 36.70  ? 612 ARG B NH1    1 
ATOM   4196 N NH2    . ARG B 1 273 ? 9.431   -0.727  -19.860 1.00 33.64  ? 612 ARG B NH2    1 
ATOM   4197 N N      . CYS B 1 274 ? 4.310   0.174   -12.238 1.00 19.19  ? 613 CYS B N      1 
ATOM   4198 C CA     . CYS B 1 274 ? 3.468   0.975   -11.353 1.00 23.45  ? 613 CYS B CA     1 
ATOM   4199 C C      . CYS B 1 274 ? 3.591   0.526   -9.901  1.00 22.76  ? 613 CYS B C      1 
ATOM   4200 O O      . CYS B 1 274 ? 3.474   1.346   -8.985  1.00 26.72  ? 613 CYS B O      1 
ATOM   4201 C CB     . CYS B 1 274 ? 2.008   0.917   -11.818 1.00 23.33  ? 613 CYS B CB     1 
ATOM   4202 S SG     . CYS B 1 274 ? 1.659   1.815   -13.356 1.00 22.53  ? 613 CYS B SG     1 
ATOM   4203 N N      . VAL B 1 275 ? 3.831   -0.762  -9.678  1.00 23.67  ? 614 VAL B N      1 
ATOM   4204 C CA     . VAL B 1 275 ? 3.982   -1.309  -8.346  1.00 18.83  ? 614 VAL B CA     1 
ATOM   4205 C C      . VAL B 1 275 ? 5.455   -1.370  -7.933  1.00 23.66  ? 614 VAL B C      1 
ATOM   4206 O O      . VAL B 1 275 ? 5.807   -2.094  -7.001  1.00 26.09  ? 614 VAL B O      1 
ATOM   4207 C CB     . VAL B 1 275 ? 3.299   -2.683  -8.223  1.00 21.55  ? 614 VAL B CB     1 
ATOM   4208 C CG1    . VAL B 1 275 ? 1.856   -2.588  -8.675  1.00 18.91  ? 614 VAL B CG1    1 
ATOM   4209 C CG2    . VAL B 1 275 ? 4.029   -3.728  -9.050  1.00 22.74  ? 614 VAL B CG2    1 
ATOM   4210 N N      . ALA B 1 276 ? 6.326   -0.609  -8.602  1.00 27.34  ? 615 ALA B N      1 
ATOM   4211 C CA     . ALA B 1 276 ? 7.741   -0.604  -8.223  1.00 26.16  ? 615 ALA B CA     1 
ATOM   4212 C C      . ALA B 1 276 ? 7.927   -0.077  -6.800  1.00 28.80  ? 615 ALA B C      1 
ATOM   4213 O O      . ALA B 1 276 ? 7.404   0.982   -6.437  1.00 25.85  ? 615 ALA B O      1 
ATOM   4214 C CB     . ALA B 1 276 ? 8.576   0.234   -9.201  1.00 25.59  ? 615 ALA B CB     1 
ATOM   4215 N N      . ARG B 1 277 ? 8.733   -0.792  -6.006  1.00 30.28  ? 616 ARG B N      1 
ATOM   4216 C CA     . ARG B 1 277 ? 8.943   -0.384  -4.616  1.00 33.48  ? 616 ARG B CA     1 
ATOM   4217 C C      . ARG B 1 277 ? 9.461   1.048   -4.509  1.00 35.82  ? 616 ARG B C      1 
ATOM   4218 O O      . ARG B 1 277 ? 9.125   1.765   -3.556  1.00 41.96  ? 616 ARG B O      1 
ATOM   4219 C CB     . ARG B 1 277 ? 9.903   -1.348  -3.913  1.00 44.61  ? 616 ARG B CB     1 
ATOM   4220 C CG     . ARG B 1 277 ? 10.469  -0.823  -2.607  1.00 54.66  ? 616 ARG B CG     1 
ATOM   4221 C CD     . ARG B 1 277 ? 11.051  -1.952  -1.779  1.00 57.85  ? 616 ARG B CD     1 
ATOM   4222 N NE     . ARG B 1 277 ? 10.008  -2.789  -1.199  1.00 66.23  ? 616 ARG B NE     1 
ATOM   4223 C CZ     . ARG B 1 277 ? 9.479   -2.595  0.002   1.00 60.88  ? 616 ARG B CZ     1 
ATOM   4224 N NH1    . ARG B 1 277 ? 9.875   -1.599  0.778   1.00 57.35  ? 616 ARG B NH1    1 
ATOM   4225 N NH2    . ARG B 1 277 ? 8.532   -3.422  0.435   1.00 57.91  ? 616 ARG B NH2    1 
ATOM   4226 N N      . ASP B 1 278 ? 10.266  1.484   -5.472  1.00 37.14  ? 617 ASP B N      1 
ATOM   4227 C CA     . ASP B 1 278 ? 10.800  2.840   -5.493  1.00 36.69  ? 617 ASP B CA     1 
ATOM   4228 C C      . ASP B 1 278 ? 9.813   3.761   -6.202  1.00 34.10  ? 617 ASP B C      1 
ATOM   4229 O O      . ASP B 1 278 ? 9.551   3.595   -7.399  1.00 33.22  ? 617 ASP B O      1 
ATOM   4230 C CB     . ASP B 1 278 ? 12.161  2.870   -6.185  1.00 35.33  ? 617 ASP B CB     1 
ATOM   4231 C CG     . ASP B 1 278 ? 13.230  2.128   -5.405  1.00 54.12  ? 617 ASP B CG     1 
ATOM   4232 O OD1    . ASP B 1 278 ? 12.958  1.718   -4.256  1.00 57.09  ? 617 ASP B OD1    1 
ATOM   4233 O OD2    . ASP B 1 278 ? 14.344  1.954   -5.943  1.00 64.50  ? 617 ASP B OD2    1 
ATOM   4234 N N      . LEU B 1 279 ? 9.278   4.738   -5.464  1.00 31.48  ? 618 LEU B N      1 
ATOM   4235 C CA     . LEU B 1 279 ? 8.252   5.612   -6.027  1.00 30.42  ? 618 LEU B CA     1 
ATOM   4236 C C      . LEU B 1 279 ? 8.743   6.307   -7.292  1.00 32.99  ? 618 LEU B C      1 
ATOM   4237 O O      . LEU B 1 279 ? 7.977   6.488   -8.246  1.00 32.31  ? 618 LEU B O      1 
ATOM   4238 C CB     . LEU B 1 279 ? 7.804   6.645   -4.990  1.00 28.13  ? 618 LEU B CB     1 
ATOM   4239 C CG     . LEU B 1 279 ? 8.831   7.668   -4.501  1.00 34.81  ? 618 LEU B CG     1 
ATOM   4240 C CD1    . LEU B 1 279 ? 8.126   8.883   -3.921  1.00 30.69  ? 618 LEU B CD1    1 
ATOM   4241 C CD2    . LEU B 1 279 ? 9.758   7.047   -3.467  1.00 33.59  ? 618 LEU B CD2    1 
ATOM   4242 N N      . ASN B 1 280 ? 10.015  6.704   -7.322  1.00 37.54  ? 619 ASN B N      1 
ATOM   4243 C CA     . ASN B 1 280 ? 10.546  7.401   -8.488  1.00 40.62  ? 619 ASN B CA     1 
ATOM   4244 C C      . ASN B 1 280 ? 10.702  6.491   -9.700  1.00 46.43  ? 619 ASN B C      1 
ATOM   4245 O O      . ASN B 1 280 ? 10.867  7.001   -10.814 1.00 47.84  ? 619 ASN B O      1 
ATOM   4246 C CB     . ASN B 1 280 ? 11.886  8.049   -8.143  1.00 43.30  ? 619 ASN B CB     1 
ATOM   4247 C CG     . ASN B 1 280 ? 11.756  9.124   -7.081  1.00 47.41  ? 619 ASN B CG     1 
ATOM   4248 O OD1    . ASN B 1 280 ? 10.809  9.911   -7.090  1.00 48.29  ? 619 ASN B OD1    1 
ATOM   4249 N ND2    . ASN B 1 280 ? 12.707  9.158   -6.155  1.00 46.34  ? 619 ASN B ND2    1 
ATOM   4250 N N      . SER B 1 281 ? 10.657  5.168   -9.516  1.00 41.75  ? 620 SER B N      1 
ATOM   4251 C CA     . SER B 1 281 ? 10.696  4.256   -10.654 1.00 29.90  ? 620 SER B CA     1 
ATOM   4252 C C      . SER B 1 281 ? 9.331   4.110   -11.309 1.00 32.02  ? 620 SER B C      1 
ATOM   4253 O O      . SER B 1 281 ? 9.251   3.896   -12.524 1.00 37.50  ? 620 SER B O      1 
ATOM   4254 C CB     . SER B 1 281 ? 11.216  2.885   -10.219 1.00 33.68  ? 620 SER B CB     1 
ATOM   4255 O OG     . SER B 1 281 ? 12.536  2.980   -9.715  1.00 54.86  ? 620 SER B OG     1 
ATOM   4256 N N      . ARG B 1 282 ? 8.259   4.219   -10.534 1.00 30.65  ? 621 ARG B N      1 
ATOM   4257 C CA     . ARG B 1 282 ? 6.927   4.181   -11.112 1.00 28.27  ? 621 ARG B CA     1 
ATOM   4258 C C      . ARG B 1 282 ? 6.776   5.316   -12.121 1.00 28.86  ? 621 ARG B C      1 
ATOM   4259 O O      . ARG B 1 282 ? 7.319   6.408   -11.915 1.00 31.00  ? 621 ARG B O      1 
ATOM   4260 C CB     . ARG B 1 282 ? 5.865   4.301   -10.020 1.00 23.47  ? 621 ARG B CB     1 
ATOM   4261 C CG     . ARG B 1 282 ? 6.031   3.294   -8.901  1.00 21.80  ? 621 ARG B CG     1 
ATOM   4262 C CD     . ARG B 1 282 ? 5.254   3.705   -7.668  1.00 21.28  ? 621 ARG B CD     1 
ATOM   4263 N NE     . ARG B 1 282 ? 5.790   3.070   -6.471  1.00 24.32  ? 621 ARG B NE     1 
ATOM   4264 C CZ     . ARG B 1 282 ? 5.435   3.384   -5.233  1.00 22.88  ? 621 ARG B CZ     1 
ATOM   4265 N NH1    . ARG B 1 282 ? 4.528   4.316   -4.990  1.00 21.91  ? 621 ARG B NH1    1 
ATOM   4266 N NH2    . ARG B 1 282 ? 6.008   2.751   -4.213  1.00 24.42  ? 621 ARG B NH2    1 
ATOM   4267 N N      . PRO B 1 283 ? 6.060   5.098   -13.216 1.00 24.73  ? 622 PRO B N      1 
ATOM   4268 C CA     . PRO B 1 283 ? 5.902   6.147   -14.223 1.00 28.34  ? 622 PRO B CA     1 
ATOM   4269 C C      . PRO B 1 283 ? 4.863   7.174   -13.790 1.00 27.27  ? 622 PRO B C      1 
ATOM   4270 O O      . PRO B 1 283 ? 4.113   6.985   -12.832 1.00 25.26  ? 622 PRO B O      1 
ATOM   4271 C CB     . PRO B 1 283 ? 5.434   5.371   -15.456 1.00 26.20  ? 622 PRO B CB     1 
ATOM   4272 C CG     . PRO B 1 283 ? 4.658   4.232   -14.881 1.00 24.41  ? 622 PRO B CG     1 
ATOM   4273 C CD     . PRO B 1 283 ? 5.336   3.868   -13.580 1.00 25.53  ? 622 PRO B CD     1 
ATOM   4274 N N      . ASN B 1 284 ? 4.840   8.284   -14.519 1.00 23.92  ? 623 ASN B N      1 
ATOM   4275 C CA     . ASN B 1 284 ? 3.776   9.257   -14.338 1.00 22.97  ? 623 ASN B CA     1 
ATOM   4276 C C      . ASN B 1 284 ? 2.474   8.706   -14.908 1.00 25.13  ? 623 ASN B C      1 
ATOM   4277 O O      . ASN B 1 284 ? 2.469   7.945   -15.880 1.00 27.49  ? 623 ASN B O      1 
ATOM   4278 C CB     . ASN B 1 284 ? 4.133   10.577  -15.018 1.00 24.42  ? 623 ASN B CB     1 
ATOM   4279 C CG     . ASN B 1 284 ? 3.277   11.730  -14.534 1.00 29.78  ? 623 ASN B CG     1 
ATOM   4280 O OD1    . ASN B 1 284 ? 2.076   11.785  -14.807 1.00 30.42  ? 623 ASN B OD1    1 
ATOM   4281 N ND2    . ASN B 1 284 ? 3.892   12.661  -13.813 1.00 32.04  ? 623 ASN B ND2    1 
ATOM   4282 N N      . VAL B 1 285 ? 1.357   9.089   -14.287 1.00 23.21  ? 624 VAL B N      1 
ATOM   4283 C CA     . VAL B 1 285 ? 0.067   8.585   -14.746 1.00 20.84  ? 624 VAL B CA     1 
ATOM   4284 C C      . VAL B 1 285 ? -0.173  8.972   -16.197 1.00 22.46  ? 624 VAL B C      1 
ATOM   4285 O O      . VAL B 1 285 ? -0.793  8.215   -16.956 1.00 24.72  ? 624 VAL B O      1 
ATOM   4286 C CB     . VAL B 1 285 ? -1.068  9.084   -13.829 1.00 25.51  ? 624 VAL B CB     1 
ATOM   4287 C CG1    . VAL B 1 285 ? -1.208  10.596  -13.926 1.00 26.06  ? 624 VAL B CG1    1 
ATOM   4288 C CG2    . VAL B 1 285 ? -2.375  8.390   -14.181 1.00 19.72  ? 624 VAL B CG2    1 
ATOM   4289 N N      . SER B 1 286 ? 0.317   10.143  -16.613 1.00 22.21  ? 625 SER B N      1 
ATOM   4290 C CA     . SER B 1 286 ? 0.176   10.544  -18.009 1.00 25.74  ? 625 SER B CA     1 
ATOM   4291 C C      . SER B 1 286 ? 0.862   9.559   -18.945 1.00 25.48  ? 625 SER B C      1 
ATOM   4292 O O      . SER B 1 286 ? 0.398   9.345   -20.072 1.00 24.77  ? 625 SER B O      1 
ATOM   4293 C CB     . SER B 1 286 ? 0.740   11.951  -18.213 1.00 25.86  ? 625 SER B CB     1 
ATOM   4294 O OG     . SER B 1 286 ? 2.149   11.958  -18.068 1.00 26.92  ? 625 SER B OG     1 
ATOM   4295 N N      . GLU B 1 287 ? 1.968   8.954   -18.503 1.00 21.72  ? 626 GLU B N      1 
ATOM   4296 C CA     . GLU B 1 287 ? 2.623   7.934   -19.314 1.00 21.66  ? 626 GLU B CA     1 
ATOM   4297 C C      . GLU B 1 287 ? 1.783   6.666   -19.380 1.00 26.15  ? 626 GLU B C      1 
ATOM   4298 O O      . GLU B 1 287 ? 1.616   6.080   -20.457 1.00 28.31  ? 626 GLU B O      1 
ATOM   4299 C CB     . GLU B 1 287 ? 4.011   7.630   -18.754 1.00 22.67  ? 626 GLU B CB     1 
ATOM   4300 C CG     . GLU B 1 287 ? 4.999   8.773   -18.904 1.00 32.32  ? 626 GLU B CG     1 
ATOM   4301 C CD     . GLU B 1 287 ? 6.284   8.538   -18.136 1.00 37.46  ? 626 GLU B CD     1 
ATOM   4302 O OE1    . GLU B 1 287 ? 6.243   7.824   -17.112 1.00 33.81  ? 626 GLU B OE1    1 
ATOM   4303 O OE2    . GLU B 1 287 ? 7.335   9.065   -18.557 1.00 47.85  ? 626 GLU B OE2    1 
ATOM   4304 N N      . VAL B 1 288 ? 1.247   6.227   -18.239 1.00 22.60  ? 627 VAL B N      1 
ATOM   4305 C CA     . VAL B 1 288 ? 0.372   5.058   -18.228 1.00 23.45  ? 627 VAL B CA     1 
ATOM   4306 C C      . VAL B 1 288 ? -0.846  5.301   -19.110 1.00 23.05  ? 627 VAL B C      1 
ATOM   4307 O O      . VAL B 1 288 ? -1.246  4.435   -19.898 1.00 24.36  ? 627 VAL B O      1 
ATOM   4308 C CB     . VAL B 1 288 ? -0.036  4.709   -16.784 1.00 21.90  ? 627 VAL B CB     1 
ATOM   4309 C CG1    . VAL B 1 288 ? -0.782  3.383   -16.746 1.00 19.95  ? 627 VAL B CG1    1 
ATOM   4310 C CG2    . VAL B 1 288 ? 1.186   4.673   -15.879 1.00 18.77  ? 627 VAL B CG2    1 
ATOM   4311 N N      . PHE B 1 289 ? -1.451  6.486   -18.996 1.00 24.61  ? 628 PHE B N      1 
ATOM   4312 C CA     . PHE B 1 289 ? -2.605  6.815   -19.826 1.00 23.67  ? 628 PHE B CA     1 
ATOM   4313 C C      . PHE B 1 289 ? -2.266  6.745   -21.309 1.00 24.16  ? 628 PHE B C      1 
ATOM   4314 O O      . PHE B 1 289 ? -3.134  6.427   -22.130 1.00 23.65  ? 628 PHE B O      1 
ATOM   4315 C CB     . PHE B 1 289 ? -3.135  8.203   -19.455 1.00 23.07  ? 628 PHE B CB     1 
ATOM   4316 C CG     . PHE B 1 289 ? -4.413  8.576   -20.155 1.00 20.06  ? 628 PHE B CG     1 
ATOM   4317 C CD1    . PHE B 1 289 ? -5.499  7.719   -20.142 1.00 20.35  ? 628 PHE B CD1    1 
ATOM   4318 C CD2    . PHE B 1 289 ? -4.532  9.791   -20.810 1.00 21.30  ? 628 PHE B CD2    1 
ATOM   4319 C CE1    . PHE B 1 289 ? -6.677  8.058   -20.781 1.00 21.93  ? 628 PHE B CE1    1 
ATOM   4320 C CE2    . PHE B 1 289 ? -5.709  10.137  -21.450 1.00 23.07  ? 628 PHE B CE2    1 
ATOM   4321 C CZ     . PHE B 1 289 ? -6.782  9.268   -21.435 1.00 20.90  ? 628 PHE B CZ     1 
ATOM   4322 N N      . MET B 1 290 ? -1.015  7.033   -21.674 1.00 22.45  ? 629 MET B N      1 
ATOM   4323 C CA     . MET B 1 290 ? -0.614  6.926   -23.073 1.00 22.84  ? 629 MET B CA     1 
ATOM   4324 C C      . MET B 1 290 ? -0.411  5.473   -23.486 1.00 25.58  ? 629 MET B C      1 
ATOM   4325 O O      . MET B 1 290 ? -0.755  5.092   -24.610 1.00 26.52  ? 629 MET B O      1 
ATOM   4326 C CB     . MET B 1 290 ? 0.658   7.740   -23.323 1.00 21.48  ? 629 MET B CB     1 
ATOM   4327 C CG     . MET B 1 290 ? 1.237   7.595   -24.725 1.00 24.56  ? 629 MET B CG     1 
ATOM   4328 S SD     . MET B 1 290 ? 2.373   6.201   -24.876 1.00 29.55  ? 629 MET B SD     1 
ATOM   4329 C CE     . MET B 1 290 ? 3.630   6.674   -23.693 1.00 25.89  ? 629 MET B CE     1 
ATOM   4330 N N      . ILE B 1 291 ? 0.144   4.649   -22.595 1.00 24.48  ? 630 ILE B N      1 
ATOM   4331 C CA     . ILE B 1 291 ? 0.372   3.245   -22.924 1.00 23.75  ? 630 ILE B CA     1 
ATOM   4332 C C      . ILE B 1 291 ? -0.955  2.529   -23.145 1.00 25.88  ? 630 ILE B C      1 
ATOM   4333 O O      . ILE B 1 291 ? -1.125  1.788   -24.120 1.00 24.14  ? 630 ILE B O      1 
ATOM   4334 C CB     . ILE B 1 291 ? 1.205   2.564   -21.823 1.00 23.95  ? 630 ILE B CB     1 
ATOM   4335 C CG1    . ILE B 1 291 ? 2.549   3.273   -21.655 1.00 25.42  ? 630 ILE B CG1    1 
ATOM   4336 C CG2    . ILE B 1 291 ? 1.415   1.093   -22.150 1.00 26.44  ? 630 ILE B CG2    1 
ATOM   4337 C CD1    . ILE B 1 291 ? 3.394   3.275   -22.905 1.00 23.38  ? 630 ILE B CD1    1 
ATOM   4338 N N      . LEU B 1 292 ? -1.917  2.741   -22.243 1.00 28.40  ? 631 LEU B N      1 
ATOM   4339 C CA     . LEU B 1 292 ? -3.220  2.104   -22.395 1.00 25.87  ? 631 LEU B CA     1 
ATOM   4340 C C      . LEU B 1 292 ? -3.934  2.599   -23.645 1.00 23.89  ? 631 LEU B C      1 
ATOM   4341 O O      . LEU B 1 292 ? -4.582  1.816   -24.349 1.00 26.92  ? 631 LEU B O      1 
ATOM   4342 C CB     . LEU B 1 292 ? -4.072  2.355   -21.151 1.00 21.85  ? 631 LEU B CB     1 
ATOM   4343 C CG     . LEU B 1 292 ? -3.575  1.672   -19.877 1.00 20.34  ? 631 LEU B CG     1 
ATOM   4344 C CD1    . LEU B 1 292 ? -4.310  2.193   -18.651 1.00 22.33  ? 631 LEU B CD1    1 
ATOM   4345 C CD2    . LEU B 1 292 ? -3.729  0.163   -19.996 1.00 18.67  ? 631 LEU B CD2    1 
ATOM   4346 N N      . SER B 1 293 ? -3.825  3.897   -23.939 1.00 25.88  ? 632 SER B N      1 
ATOM   4347 C CA     . SER B 1 293 ? -4.481  4.445   -25.123 1.00 27.64  ? 632 SER B CA     1 
ATOM   4348 C C      . SER B 1 293 ? -3.939  3.810   -26.398 1.00 28.78  ? 632 SER B C      1 
ATOM   4349 O O      . SER B 1 293 ? -4.705  3.483   -27.313 1.00 29.50  ? 632 SER B O      1 
ATOM   4350 C CB     . SER B 1 293 ? -4.309  5.964   -25.166 1.00 23.31  ? 632 SER B CB     1 
ATOM   4351 O OG     . SER B 1 293 ? -4.893  6.578   -24.028 1.00 28.92  ? 632 SER B OG     1 
ATOM   4352 N N      . LYS B 1 294 ? -2.619  3.632   -26.481 1.00 26.92  ? 633 LYS B N      1 
ATOM   4353 C CA     . LYS B 1 294 ? -2.029  3.002   -27.656 1.00 28.47  ? 633 LYS B CA     1 
ATOM   4354 C C      . LYS B 1 294 ? -2.282  1.500   -27.682 1.00 29.95  ? 633 LYS B C      1 
ATOM   4355 O O      . LYS B 1 294 ? -2.315  0.901   -28.763 1.00 33.79  ? 633 LYS B O      1 
ATOM   4356 C CB     . LYS B 1 294 ? -0.528  3.290   -27.710 1.00 26.42  ? 633 LYS B CB     1 
ATOM   4357 C CG     . LYS B 1 294 ? -0.188  4.763   -27.837 1.00 23.72  ? 633 LYS B CG     1 
ATOM   4358 C CD     . LYS B 1 294 ? 1.297   4.974   -28.070 1.00 30.21  ? 633 LYS B CD     1 
ATOM   4359 C CE     . LYS B 1 294 ? 1.602   6.436   -28.353 1.00 26.03  ? 633 LYS B CE     1 
ATOM   4360 N NZ     . LYS B 1 294 ? 0.809   6.947   -29.507 1.00 35.36  ? 633 LYS B NZ     1 
ATOM   4361 N N      . ILE B 1 295 ? -2.453  0.877   -26.513 1.00 31.76  ? 634 ILE B N      1 
ATOM   4362 C CA     . ILE B 1 295 ? -2.873  -0.520  -26.474 1.00 28.09  ? 634 ILE B CA     1 
ATOM   4363 C C      . ILE B 1 295 ? -4.283  -0.661  -27.028 1.00 31.51  ? 634 ILE B C      1 
ATOM   4364 O O      . ILE B 1 295 ? -4.583  -1.603  -27.770 1.00 31.82  ? 634 ILE B O      1 
ATOM   4365 C CB     . ILE B 1 295 ? -2.773  -1.070  -25.039 1.00 26.79  ? 634 ILE B CB     1 
ATOM   4366 C CG1    . ILE B 1 295 ? -1.310  -1.264  -24.636 1.00 31.07  ? 634 ILE B CG1    1 
ATOM   4367 C CG2    . ILE B 1 295 ? -3.559  -2.368  -24.902 1.00 23.74  ? 634 ILE B CG2    1 
ATOM   4368 C CD1    . ILE B 1 295 ? -1.130  -1.795  -23.226 1.00 26.93  ? 634 ILE B CD1    1 
ATOM   4369 N N      . GLN B 1 296 ? -5.169  0.273   -26.677 1.00 34.76  ? 635 GLN B N      1 
ATOM   4370 C CA     . GLN B 1 296 ? -6.555  0.210   -27.126 1.00 33.04  ? 635 GLN B CA     1 
ATOM   4371 C C      . GLN B 1 296 ? -6.706  0.643   -28.578 1.00 41.91  ? 635 GLN B C      1 
ATOM   4372 O O      . GLN B 1 296 ? -7.642  0.203   -29.255 1.00 44.88  ? 635 GLN B O      1 
ATOM   4373 C CB     . GLN B 1 296 ? -7.432  1.077   -26.221 1.00 27.74  ? 635 GLN B CB     1 
ATOM   4374 C CG     . GLN B 1 296 ? -8.922  0.841   -26.374 1.00 36.18  ? 635 GLN B CG     1 
ATOM   4375 C CD     . GLN B 1 296 ? -9.742  1.752   -25.484 1.00 36.02  ? 635 GLN B CD     1 
ATOM   4376 O OE1    . GLN B 1 296 ? -9.271  2.807   -25.058 1.00 34.40  ? 635 GLN B OE1    1 
ATOM   4377 N NE2    . GLN B 1 296 ? -10.974 1.348   -25.194 1.00 33.58  ? 635 GLN B NE2    1 
ATOM   4378 N N      . SER B 1 297 ? -5.805  1.492   -29.067 1.00 54.65  ? 636 SER B N      1 
ATOM   4379 C CA     . SER B 1 297 ? -5.835  1.965   -30.450 1.00 58.87  ? 636 SER B CA     1 
ATOM   4380 C C      . SER B 1 297 ? -7.231  2.423   -30.862 1.00 63.88  ? 636 SER B C      1 
ATOM   4381 O O      . SER B 1 297 ? -7.711  2.083   -31.944 1.00 74.28  ? 636 SER B O      1 
ATOM   4382 C CB     . SER B 1 297 ? -5.339  0.874   -31.402 1.00 51.09  ? 636 SER B CB     1 
ATOM   4383 O OG     . SER B 1 297 ? -6.190  -0.259  -31.369 1.00 61.99  ? 636 SER B OG     1 
HETATM 4384 C C1     . GOL C 2 .   ? -5.124  30.323  -37.968 1.00 42.42  ? 701 GOL A C1     1 
HETATM 4385 O O1     . GOL C 2 .   ? -5.599  31.303  -38.837 1.00 41.76  ? 701 GOL A O1     1 
HETATM 4386 C C2     . GOL C 2 .   ? -3.645  30.064  -38.346 1.00 40.78  ? 701 GOL A C2     1 
HETATM 4387 O O2     . GOL C 2 .   ? -2.874  31.216  -38.249 1.00 36.34  ? 701 GOL A O2     1 
HETATM 4388 C C3     . GOL C 2 .   ? -3.172  28.962  -37.367 1.00 35.12  ? 701 GOL A C3     1 
HETATM 4389 O O3     . GOL C 2 .   ? -2.081  28.334  -37.967 1.00 31.30  ? 701 GOL A O3     1 
HETATM 4390 S S      . SO4 D 3 .   ? -9.513  40.979  -47.599 1.00 46.53  ? 702 SO4 A S      1 
HETATM 4391 O O1     . SO4 D 3 .   ? -8.124  41.037  -48.049 1.00 43.17  ? 702 SO4 A O1     1 
HETATM 4392 O O2     . SO4 D 3 .   ? -10.288 42.021  -48.267 1.00 41.85  ? 702 SO4 A O2     1 
HETATM 4393 O O3     . SO4 D 3 .   ? -10.074 39.670  -47.923 1.00 39.71  ? 702 SO4 A O3     1 
HETATM 4394 O O4     . SO4 D 3 .   ? -9.564  41.187  -46.154 1.00 44.72  ? 702 SO4 A O4     1 
HETATM 4395 C C1     . GOL E 2 .   ? -15.769 28.920  -32.809 1.00 45.37  ? 703 GOL A C1     1 
HETATM 4396 O O1     . GOL E 2 .   ? -15.081 28.838  -33.998 1.00 44.27  ? 703 GOL A O1     1 
HETATM 4397 C C2     . GOL E 2 .   ? -15.500 27.611  -32.034 1.00 41.16  ? 703 GOL A C2     1 
HETATM 4398 O O2     . GOL E 2 .   ? -14.234 27.152  -32.212 1.00 42.54  ? 703 GOL A O2     1 
HETATM 4399 C C3     . GOL E 2 .   ? -15.807 28.051  -30.591 1.00 39.91  ? 703 GOL A C3     1 
HETATM 4400 O O3     . GOL E 2 .   ? -17.022 27.465  -30.226 1.00 29.01  ? 703 GOL A O3     1 
HETATM 4401 H H11    . GOL E 2 .   ? -15.490 29.675  -32.268 1.00 55.09  ? 703 GOL A H11    1 
HETATM 4402 H H12    . GOL E 2 .   ? -16.725 29.024  -32.938 1.00 55.09  ? 703 GOL A H12    1 
HETATM 4403 H HO1    . GOL E 2 .   ? -14.527 29.491  -34.005 1.00 53.76  ? 703 GOL A HO1    1 
HETATM 4404 H H2     . GOL E 2 .   ? -16.055 26.870  -32.324 1.00 50.04  ? 703 GOL A H2     1 
HETATM 4405 H HO2    . GOL E 2 .   ? -13.731 27.809  -32.210 1.00 51.69  ? 703 GOL A HO2    1 
HETATM 4406 H H31    . GOL E 2 .   ? -15.824 29.020  -30.557 1.00 48.53  ? 703 GOL A H31    1 
HETATM 4407 H H32    . GOL E 2 .   ? -15.068 27.787  -30.021 1.00 48.53  ? 703 GOL A H32    1 
HETATM 4408 H HO3    . GOL E 2 .   ? -16.822 26.843  -29.664 1.00 35.46  ? 703 GOL A HO3    1 
HETATM 4409 P PG     . ANP F 4 .   ? -12.917 36.151  -33.689 1.00 82.84  ? 704 ANP A PG     1 
HETATM 4410 O O1G    . ANP F 4 .   ? -13.339 37.142  -34.739 1.00 71.06  ? 704 ANP A O1G    1 
HETATM 4411 O O2G    . ANP F 4 .   ? -13.532 36.586  -32.297 1.00 71.60  ? 704 ANP A O2G    1 
HETATM 4412 O O3G    . ANP F 4 .   ? -11.339 36.147  -33.563 1.00 59.82  ? 704 ANP A O3G    1 
HETATM 4413 P PB     . ANP F 4 .   ? -13.584 34.290  -35.699 1.00 59.02  ? 704 ANP A PB     1 
HETATM 4414 O O1B    . ANP F 4 .   ? -14.008 35.541  -36.412 1.00 70.16  ? 704 ANP A O1B    1 
HETATM 4415 O O2B    . ANP F 4 .   ? -12.190 33.863  -36.243 1.00 59.37  ? 704 ANP A O2B    1 
HETATM 4416 N N3B    . ANP F 4 .   ? -13.354 34.546  -34.053 1.00 52.62  ? 704 ANP A N3B    1 
HETATM 4417 P PA     . ANP F 4 .   ? -15.431 32.279  -34.973 1.00 50.51  ? 704 ANP A PA     1 
HETATM 4418 O O1A    . ANP F 4 .   ? -15.946 31.038  -35.600 1.00 49.59  ? 704 ANP A O1A    1 
HETATM 4419 O O2A    . ANP F 4 .   ? -14.477 32.035  -33.799 1.00 53.71  ? 704 ANP A O2A    1 
HETATM 4420 O O3A    . ANP F 4 .   ? -14.634 33.171  -36.042 1.00 55.42  ? 704 ANP A O3A    1 
HETATM 4421 O "O5'"  . ANP F 4 .   ? -16.679 33.154  -34.532 1.00 50.29  ? 704 ANP A "O5'"  1 
HETATM 4422 C "C5'"  . ANP F 4 .   ? -16.372 34.359  -33.829 1.00 52.21  ? 704 ANP A "C5'"  1 
HETATM 4423 C "C4'"  . ANP F 4 .   ? -17.595 35.001  -33.245 1.00 46.19  ? 704 ANP A "C4'"  1 
HETATM 4424 O "O4'"  . ANP F 4 .   ? -18.479 33.975  -32.752 1.00 48.33  ? 704 ANP A "O4'"  1 
HETATM 4425 C "C3'"  . ANP F 4 .   ? -17.294 35.909  -32.056 1.00 46.59  ? 704 ANP A "C3'"  1 
HETATM 4426 O "O3'"  . ANP F 4 .   ? -18.180 37.021  -31.989 1.00 55.22  ? 704 ANP A "O3'"  1 
HETATM 4427 C "C2'"  . ANP F 4 .   ? -17.433 34.956  -30.869 1.00 44.29  ? 704 ANP A "C2'"  1 
HETATM 4428 O "O2'"  . ANP F 4 .   ? -17.806 35.626  -29.671 1.00 44.88  ? 704 ANP A "O2'"  1 
HETATM 4429 C "C1'"  . ANP F 4 .   ? -18.562 34.039  -31.341 1.00 46.77  ? 704 ANP A "C1'"  1 
HETATM 4430 N N9     . ANP F 4 .   ? -18.482 32.684  -30.814 1.00 39.98  ? 704 ANP A N9     1 
HETATM 4431 C C8     . ANP F 4 .   ? -17.816 31.613  -31.352 1.00 37.57  ? 704 ANP A C8     1 
HETATM 4432 N N7     . ANP F 4 .   ? -17.925 30.507  -30.656 1.00 31.73  ? 704 ANP A N7     1 
HETATM 4433 C C5     . ANP F 4 .   ? -18.722 30.879  -29.580 1.00 31.40  ? 704 ANP A C5     1 
HETATM 4434 C C6     . ANP F 4 .   ? -19.211 30.159  -28.472 1.00 28.41  ? 704 ANP A C6     1 
HETATM 4435 N N6     . ANP F 4 .   ? -18.958 28.870  -28.249 1.00 24.38  ? 704 ANP A N6     1 
HETATM 4436 N N1     . ANP F 4 .   ? -19.977 30.828  -27.582 1.00 30.18  ? 704 ANP A N1     1 
HETATM 4437 C C2     . ANP F 4 .   ? -20.232 32.121  -27.796 1.00 29.28  ? 704 ANP A C2     1 
HETATM 4438 N N3     . ANP F 4 .   ? -19.826 32.900  -28.801 1.00 33.56  ? 704 ANP A N3     1 
HETATM 4439 C C4     . ANP F 4 .   ? -19.068 32.212  -29.666 1.00 30.81  ? 704 ANP A C4     1 
HETATM 4440 H HNB1   . ANP F 4 .   ? -12.686 33.999  -33.771 1.00 63.79  ? 704 ANP A HNB1   1 
HETATM 4441 H "H5'1" . ANP F 4 .   ? -15.752 34.150  -33.109 1.00 63.30  ? 704 ANP A "H5'1" 1 
HETATM 4442 H "H5'2" . ANP F 4 .   ? -15.953 34.982  -34.448 1.00 63.30  ? 704 ANP A "H5'2" 1 
HETATM 4443 H "H4'"  . ANP F 4 .   ? -18.105 35.501  -33.915 1.00 56.08  ? 704 ANP A "H4'"  1 
HETATM 4444 H "H3'"  . ANP F 4 .   ? -16.386 36.215  -32.121 1.00 56.56  ? 704 ANP A "H3'"  1 
HETATM 4445 H "HO3'" . ANP F 4 .   ? -18.687 36.967  -31.265 1.00 66.90  ? 704 ANP A "HO3'" 1 
HETATM 4446 H "H2'"  . ANP F 4 .   ? -16.624 34.441  -30.759 1.00 53.79  ? 704 ANP A "H2'"  1 
HETATM 4447 H "HO2'" . ANP F 4 .   ? -17.909 35.027  -29.023 1.00 54.50  ? 704 ANP A "HO2'" 1 
HETATM 4448 H "H1'"  . ANP F 4 .   ? -19.402 34.452  -31.088 1.00 56.77  ? 704 ANP A "H1'"  1 
HETATM 4449 H H8     . ANP F 4 .   ? -17.315 31.668  -32.164 1.00 45.73  ? 704 ANP A H8     1 
HETATM 4450 H HN61   . ANP F 4 .   ? -19.308 28.450  -27.505 1.00 29.91  ? 704 ANP A HN61   1 
HETATM 4451 H HN62   . ANP F 4 .   ? -18.431 28.405  -28.833 1.00 29.91  ? 704 ANP A HN62   1 
HETATM 4452 H H2     . ANP F 4 .   ? -20.788 32.555  -27.128 1.00 35.78  ? 704 ANP A H2     1 
HETATM 4453 C C1     . GOL G 2 .   ? -18.959 6.998   -3.093  1.00 30.43  ? 701 GOL B C1     1 
HETATM 4454 O O1     . GOL G 2 .   ? -18.001 7.225   -2.110  1.00 34.14  ? 701 GOL B O1     1 
HETATM 4455 C C2     . GOL G 2 .   ? -19.190 8.349   -3.809  1.00 32.34  ? 701 GOL B C2     1 
HETATM 4456 O O2     . GOL G 2 .   ? -20.064 8.226   -4.881  1.00 32.88  ? 701 GOL B O2     1 
HETATM 4457 C C3     . GOL G 2 .   ? -17.783 8.805   -4.250  1.00 33.43  ? 701 GOL B C3     1 
HETATM 4458 O O3     . GOL G 2 .   ? -17.816 10.194  -4.333  1.00 34.67  ? 701 GOL B O3     1 
HETATM 4459 S S      . SO4 H 3 .   ? -13.946 -6.260  12.342  1.00 58.67  ? 702 SO4 B S      1 
HETATM 4460 O O1     . SO4 H 3 .   ? -14.844 -7.404  12.477  1.00 47.96  ? 702 SO4 B O1     1 
HETATM 4461 O O2     . SO4 H 3 .   ? -13.780 -5.938  10.926  1.00 49.55  ? 702 SO4 B O2     1 
HETATM 4462 O O3     . SO4 H 3 .   ? -12.646 -6.583  12.924  1.00 50.40  ? 702 SO4 B O3     1 
HETATM 4463 O O4     . SO4 H 3 .   ? -14.516 -5.110  13.041  1.00 47.34  ? 702 SO4 B O4     1 
HETATM 4464 P PG     . ANP I 4 .   ? -16.124 -0.746  3.215   1.00 98.87  ? 703 ANP B PG     1 
HETATM 4465 O O1G    . ANP I 4 .   ? -17.060 -1.899  3.030   1.00 88.58  ? 703 ANP B O1G    1 
HETATM 4466 O O2G    . ANP I 4 .   ? -15.246 -0.995  4.501   1.00 83.34  ? 703 ANP B O2G    1 
HETATM 4467 O O3G    . ANP I 4 .   ? -15.186 -0.614  1.946   1.00 94.74  ? 703 ANP B O3G    1 
HETATM 4468 P PB     . ANP I 4 .   ? -16.348 1.968   2.589   1.00 86.19  ? 703 ANP B PB     1 
HETATM 4469 O O1B    . ANP I 4 .   ? -17.115 3.210   2.905   1.00 75.51  ? 703 ANP B O1B    1 
HETATM 4470 O O2B    . ANP I 4 .   ? -14.868 2.143   3.042   1.00 74.71  ? 703 ANP B O2B    1 
HETATM 4471 N N3B    . ANP I 4 .   ? -17.021 0.676   3.425   1.00 87.16  ? 703 ANP B N3B    1 
HETATM 4472 P PA     . ANP I 4 .   ? -17.610 1.037   0.319   1.00 82.98  ? 703 ANP B PA     1 
HETATM 4473 O O1A    . ANP I 4 .   ? -17.243 0.669   -1.070  1.00 65.08  ? 703 ANP B O1A    1 
HETATM 4474 O O2A    . ANP I 4 .   ? -18.068 -0.146  1.175   1.00 79.18  ? 703 ANP B O2A    1 
HETATM 4475 O O3A    . ANP I 4 .   ? -16.378 1.739   1.045   1.00 78.98  ? 703 ANP B O3A    1 
HETATM 4476 O "O5'"  . ANP I 4 .   ? -18.757 2.114   0.251   1.00 64.95  ? 703 ANP B "O5'"  1 
HETATM 4477 C "C5'"  . ANP I 4 .   ? -19.375 2.347   -1.009  1.00 56.73  ? 703 ANP B "C5'"  1 
HETATM 4478 C "C4'"  . ANP I 4 .   ? -20.617 1.509   -1.148  1.00 59.29  ? 703 ANP B "C4'"  1 
HETATM 4479 O "O4'"  . ANP I 4 .   ? -21.669 2.315   -1.722  1.00 57.70  ? 703 ANP B "O4'"  1 
HETATM 4480 C "C3'"  . ANP I 4 .   ? -20.466 0.327   -2.097  1.00 60.23  ? 703 ANP B "C3'"  1 
HETATM 4481 O "O3'"  . ANP I 4 .   ? -21.344 -0.739  -1.750  1.00 61.77  ? 703 ANP B "O3'"  1 
HETATM 4482 C "C2'"  . ANP I 4 .   ? -20.764 0.971   -3.452  1.00 53.39  ? 703 ANP B "C2'"  1 
HETATM 4483 O "O2'"  . ANP I 4 .   ? -21.209 0.001   -4.389  1.00 56.86  ? 703 ANP B "O2'"  1 
HETATM 4484 C "C1'"  . ANP I 4 .   ? -21.866 1.968   -3.084  1.00 52.03  ? 703 ANP B "C1'"  1 
HETATM 4485 N N9     . ANP I 4 .   ? -21.846 3.199   -3.872  1.00 45.16  ? 703 ANP B N9     1 
HETATM 4486 C C8     . ANP I 4 .   ? -21.170 4.349   -3.561  1.00 40.64  ? 703 ANP B C8     1 
HETATM 4487 N N7     . ANP I 4 .   ? -21.327 5.315   -4.435  1.00 33.36  ? 703 ANP B N7     1 
HETATM 4488 C C5     . ANP I 4 .   ? -22.168 4.761   -5.388  1.00 32.76  ? 703 ANP B C5     1 
HETATM 4489 C C6     . ANP I 4 .   ? -22.717 5.275   -6.579  1.00 33.19  ? 703 ANP B C6     1 
HETATM 4490 N N6     . ANP I 4 .   ? -22.488 6.511   -7.029  1.00 34.92  ? 703 ANP B N6     1 
HETATM 4491 N N1     . ANP I 4 .   ? -23.520 4.461   -7.302  1.00 31.43  ? 703 ANP B N1     1 
HETATM 4492 C C2     . ANP I 4 .   ? -23.750 3.222   -6.855  1.00 33.29  ? 703 ANP B C2     1 
HETATM 4493 N N3     . ANP I 4 .   ? -23.290 2.630   -5.749  1.00 35.79  ? 703 ANP B N3     1 
HETATM 4494 C C4     . ANP I 4 .   ? -22.498 3.458   -5.054  1.00 39.31  ? 703 ANP B C4     1 
HETATM 4495 H HNB1   . ANP I 4 .   ? -17.039 0.880   4.310   1.00 105.24 ? 703 ANP B HNB1   1 
HETATM 4496 H "H5'1" . ANP I 4 .   ? -18.750 2.116   -1.719  1.00 68.72  ? 703 ANP B "H5'1" 1 
HETATM 4497 H "H5'2" . ANP I 4 .   ? -19.612 3.288   -1.079  1.00 68.72  ? 703 ANP B "H5'2" 1 
HETATM 4498 H "H4'"  . ANP I 4 .   ? -20.936 1.193   -0.278  1.00 71.79  ? 703 ANP B "H4'"  1 
HETATM 4499 H "H3'"  . ANP I 4 .   ? -19.559 0.012   -2.090  1.00 72.92  ? 703 ANP B "H3'"  1 
HETATM 4500 H "HO3'" . ANP I 4 .   ? -20.870 -1.339  -1.301  1.00 74.77  ? 703 ANP B "HO3'" 1 
HETATM 4501 H "H2'"  . ANP I 4 .   ? -20.011 1.475   -3.784  1.00 64.71  ? 703 ANP B "H2'"  1 
HETATM 4502 H "HO2'" . ANP I 4 .   ? -21.697 -0.600  -3.955  1.00 68.88  ? 703 ANP B "HO2'" 1 
HETATM 4503 H "H1'"  . ANP I 4 .   ? -22.717 1.513   -3.185  1.00 63.08  ? 703 ANP B "H1'"  1 
HETATM 4504 H H8     . ANP I 4 .   ? -20.631 4.440   -2.776  1.00 49.41  ? 703 ANP B H8     1 
HETATM 4505 H HN61   . ANP I 4 .   ? -22.865 6.790   -7.825  1.00 42.55  ? 703 ANP B HN61   1 
HETATM 4506 H HN62   . ANP I 4 .   ? -21.955 7.080   -6.552  1.00 42.55  ? 703 ANP B HN62   1 
HETATM 4507 H H2     . ANP I 4 .   ? -24.333 2.678   -7.410  1.00 40.60  ? 703 ANP B H2     1 
HETATM 4508 O O      . HOH J 5 .   ? 7.620   27.724  -32.910 1.00 16.39  ? 801 HOH A O      1 
HETATM 4509 O O      . HOH J 5 .   ? -1.094  29.411  -30.577 1.00 20.57  ? 802 HOH A O      1 
HETATM 4510 O O      . HOH J 5 .   ? 4.559   19.221  -25.501 1.00 21.63  ? 803 HOH A O      1 
HETATM 4511 O O      . HOH J 5 .   ? -14.054 26.946  -50.541 1.00 57.42  ? 804 HOH A O      1 
HETATM 4512 O O      . HOH J 5 .   ? 4.923   60.049  -11.972 1.00 26.72  ? 805 HOH A O      1 
HETATM 4513 O O      . HOH J 5 .   ? -15.341 23.873  -20.787 1.00 18.44  ? 806 HOH A O      1 
HETATM 4514 O O      . HOH J 5 .   ? -1.167  52.753  -14.644 1.00 25.07  ? 807 HOH A O      1 
HETATM 4515 O O      . HOH J 5 .   ? -10.256 13.715  -21.329 1.00 26.89  ? 808 HOH A O      1 
HETATM 4516 O O      . HOH J 5 .   ? -19.000 47.255  -25.344 1.00 43.09  ? 809 HOH A O      1 
HETATM 4517 O O      . HOH J 5 .   ? 5.955   53.185  -21.363 1.00 26.98  ? 810 HOH A O      1 
HETATM 4518 O O      . HOH J 5 .   ? -12.313 25.101  -33.959 1.00 23.20  ? 811 HOH A O      1 
HETATM 4519 O O      . HOH J 5 .   ? 2.248   41.911  -31.079 1.00 29.71  ? 812 HOH A O      1 
HETATM 4520 O O      . HOH J 5 .   ? 13.931  51.274  -13.222 1.00 34.58  ? 813 HOH A O      1 
HETATM 4521 O O      . HOH J 5 .   ? -14.147 33.979  -31.242 1.00 38.91  ? 814 HOH A O      1 
HETATM 4522 O O      . HOH J 5 .   ? -2.116  33.121  -32.774 1.00 27.10  ? 815 HOH A O      1 
HETATM 4523 O O      . HOH J 5 .   ? -3.226  22.289  -16.873 1.00 21.54  ? 816 HOH A O      1 
HETATM 4524 O O      . HOH J 5 .   ? -3.969  52.732  -15.313 1.00 29.96  ? 817 HOH A O      1 
HETATM 4525 O O      . HOH J 5 .   ? -17.386 8.904   -36.329 1.00 37.61  ? 818 HOH A O      1 
HETATM 4526 O O      . HOH J 5 .   ? 16.858  47.828  -16.027 1.00 34.92  ? 819 HOH A O      1 
HETATM 4527 O O      . HOH J 5 .   ? -6.873  14.508  -24.333 1.00 31.92  ? 820 HOH A O      1 
HETATM 4528 O O      . HOH J 5 .   ? 1.677   17.805  -13.152 1.00 21.33  ? 821 HOH A O      1 
HETATM 4529 O O      . HOH J 5 .   ? 2.819   32.410  -32.249 1.00 13.97  ? 822 HOH A O      1 
HETATM 4530 O O      . HOH J 5 .   ? 14.724  35.163  -35.599 1.00 47.77  ? 823 HOH A O      1 
HETATM 4531 O O      . HOH J 5 .   ? 4.632   22.882  -20.439 1.00 17.20  ? 824 HOH A O      1 
HETATM 4532 O O      . HOH J 5 .   ? -8.936  47.060  -10.987 1.00 24.05  ? 825 HOH A O      1 
HETATM 4533 O O      . HOH J 5 .   ? 4.665   24.598  -23.023 1.00 18.79  ? 826 HOH A O      1 
HETATM 4534 O O      . HOH J 5 .   ? -9.179  32.787  -35.246 1.00 34.56  ? 827 HOH A O      1 
HETATM 4535 O O      . HOH J 5 .   ? -1.062  9.647   -25.987 1.00 20.92  ? 828 HOH A O      1 
HETATM 4536 O O      . HOH J 5 .   ? 6.455   21.127  -18.792 1.00 35.66  ? 829 HOH A O      1 
HETATM 4537 O O      . HOH J 5 .   ? -9.968  25.609  -14.304 1.00 32.32  ? 830 HOH A O      1 
HETATM 4538 O O      . HOH J 5 .   ? -11.630 16.577  -18.743 1.00 27.22  ? 831 HOH A O      1 
HETATM 4539 O O      . HOH J 5 .   ? 0.023   31.394  -32.769 1.00 24.43  ? 832 HOH A O      1 
HETATM 4540 O O      . HOH J 5 .   ? -3.570  50.129  -29.223 1.00 23.23  ? 833 HOH A O      1 
HETATM 4541 O O      . HOH J 5 .   ? 8.590   52.799  -4.243  1.00 39.84  ? 834 HOH A O      1 
HETATM 4542 O O      . HOH J 5 .   ? -1.040  51.880  -22.289 1.00 21.50  ? 835 HOH A O      1 
HETATM 4543 O O      . HOH J 5 .   ? 13.839  30.883  -36.790 1.00 35.32  ? 836 HOH A O      1 
HETATM 4544 O O      . HOH J 5 .   ? 1.739   49.134  -6.570  1.00 16.78  ? 837 HOH A O      1 
HETATM 4545 O O      . HOH J 5 .   ? -0.934  34.130  -3.237  1.00 37.89  ? 838 HOH A O      1 
HETATM 4546 O O      . HOH J 5 .   ? -7.574  35.914  -10.506 1.00 32.16  ? 839 HOH A O      1 
HETATM 4547 O O      . HOH J 5 .   ? -14.582 20.021  -25.407 1.00 32.16  ? 840 HOH A O      1 
HETATM 4548 O O      . HOH J 5 .   ? -28.776 24.743  -43.180 1.00 33.16  ? 841 HOH A O      1 
HETATM 4549 O O      . HOH J 5 .   ? 14.126  27.887  -21.230 1.00 26.47  ? 842 HOH A O      1 
HETATM 4550 O O      . HOH J 5 .   ? -12.425 31.926  -38.476 1.00 53.48  ? 843 HOH A O      1 
HETATM 4551 O O      . HOH J 5 .   ? 14.581  53.231  -5.887  1.00 46.62  ? 844 HOH A O      1 
HETATM 4552 O O      . HOH J 5 .   ? -9.759  47.693  -21.274 1.00 22.06  ? 845 HOH A O      1 
HETATM 4553 O O      . HOH J 5 .   ? 9.949   40.304  -29.419 1.00 25.39  ? 846 HOH A O      1 
HETATM 4554 O O      . HOH J 5 .   ? 16.029  42.706  -21.732 1.00 36.49  ? 847 HOH A O      1 
HETATM 4555 O O      . HOH J 5 .   ? -9.493  28.466  -45.449 1.00 62.12  ? 848 HOH A O      1 
HETATM 4556 O O      . HOH J 5 .   ? -14.166 27.088  -38.501 1.00 41.38  ? 849 HOH A O      1 
HETATM 4557 O O      . HOH J 5 .   ? -6.295  39.623  -36.750 1.00 30.02  ? 850 HOH A O      1 
HETATM 4558 O O      . HOH J 5 .   ? -3.654  34.757  -37.831 1.00 37.71  ? 851 HOH A O      1 
HETATM 4559 O O      . HOH J 5 .   ? -31.235 10.115  -30.580 1.00 26.84  ? 852 HOH A O      1 
HETATM 4560 O O      . HOH J 5 .   ? -21.859 30.904  -17.066 1.00 26.67  ? 853 HOH A O      1 
HETATM 4561 O O      . HOH J 5 .   ? -6.828  14.263  -21.752 1.00 24.26  ? 854 HOH A O      1 
HETATM 4562 O O      . HOH J 5 .   ? -23.247 31.716  -18.915 1.00 31.95  ? 855 HOH A O      1 
HETATM 4563 O O      . HOH J 5 .   ? -24.931 22.323  -23.891 1.00 28.70  ? 856 HOH A O      1 
HETATM 4564 O O      . HOH J 5 .   ? -6.055  37.823  -8.166  1.00 26.72  ? 857 HOH A O      1 
HETATM 4565 O O      . HOH J 5 .   ? 11.400  53.052  -23.835 1.00 36.43  ? 858 HOH A O      1 
HETATM 4566 O O      . HOH J 5 .   ? 4.273   51.441  -5.932  1.00 34.19  ? 859 HOH A O      1 
HETATM 4567 O O      . HOH J 5 .   ? 11.602  23.340  -28.360 1.00 25.89  ? 860 HOH A O      1 
HETATM 4568 O O      . HOH J 5 .   ? -10.863 49.040  -12.564 1.00 19.22  ? 861 HOH A O      1 
HETATM 4569 O O      . HOH J 5 .   ? 4.889   17.676  -18.025 1.00 21.90  ? 862 HOH A O      1 
HETATM 4570 O O      . HOH J 5 .   ? -17.196 31.626  -49.756 1.00 29.35  ? 863 HOH A O      1 
HETATM 4571 O O      . HOH J 5 .   ? -10.683 29.736  -9.704  1.00 34.67  ? 864 HOH A O      1 
HETATM 4572 O O      . HOH J 5 .   ? -15.903 7.819   -25.866 1.00 26.69  ? 865 HOH A O      1 
HETATM 4573 O O      . HOH J 5 .   ? -18.303 22.800  -19.697 1.00 27.45  ? 866 HOH A O      1 
HETATM 4574 O O      . HOH J 5 .   ? -15.930 16.264  -25.650 1.00 38.07  ? 867 HOH A O      1 
HETATM 4575 O O      . HOH J 5 .   ? 6.939   47.529  -39.200 1.00 22.19  ? 868 HOH A O      1 
HETATM 4576 O O      . HOH J 5 .   ? 7.107   24.475  -13.900 1.00 21.44  ? 869 HOH A O      1 
HETATM 4577 O O      . HOH J 5 .   ? -4.095  7.217   -28.444 1.00 22.61  ? 870 HOH A O      1 
HETATM 4578 O O      . HOH J 5 .   ? -8.544  30.783  -8.037  1.00 38.08  ? 871 HOH A O      1 
HETATM 4579 O O      . HOH J 5 .   ? -19.447 37.567  -41.919 1.00 43.16  ? 872 HOH A O      1 
HETATM 4580 O O      . HOH J 5 .   ? 13.729  44.257  -15.236 1.00 37.65  ? 873 HOH A O      1 
HETATM 4581 O O      . HOH J 5 .   ? -17.273 16.319  -18.855 1.00 39.57  ? 874 HOH A O      1 
HETATM 4582 O O      . HOH J 5 .   ? 16.267  38.048  -39.401 1.00 32.81  ? 875 HOH A O      1 
HETATM 4583 O O      . HOH J 5 .   ? -16.654 49.650  -14.584 1.00 35.94  ? 876 HOH A O      1 
HETATM 4584 O O      . HOH J 5 .   ? 4.320   17.896  -12.431 1.00 24.75  ? 877 HOH A O      1 
HETATM 4585 O O      . HOH J 5 .   ? -13.508 43.628  -40.488 1.00 35.04  ? 878 HOH A O      1 
HETATM 4586 O O      . HOH J 5 .   ? 9.982   56.278  -9.734  1.00 39.11  ? 879 HOH A O      1 
HETATM 4587 O O      . HOH J 5 .   ? -18.201 44.481  -24.357 1.00 23.32  ? 880 HOH A O      1 
HETATM 4588 O O      . HOH J 5 .   ? 1.532   57.499  -8.551  1.00 40.32  ? 881 HOH A O      1 
HETATM 4589 O O      . HOH J 5 .   ? 6.730   52.114  -25.214 1.00 30.19  ? 882 HOH A O      1 
HETATM 4590 O O      . HOH J 5 .   ? -25.872 12.152  -44.474 1.00 31.17  ? 883 HOH A O      1 
HETATM 4591 O O      . HOH J 5 .   ? -15.446 20.694  -16.659 1.00 23.82  ? 884 HOH A O      1 
HETATM 4592 O O      . HOH J 5 .   ? -2.447  49.810  -42.410 1.00 42.24  ? 885 HOH A O      1 
HETATM 4593 O O      . HOH J 5 .   ? -14.177 52.297  -17.411 1.00 34.18  ? 886 HOH A O      1 
HETATM 4594 O O      . HOH J 5 .   ? -32.605 40.102  -38.091 1.00 41.02  ? 887 HOH A O      1 
HETATM 4595 O O      . HOH J 5 .   ? 7.058   49.371  -8.391  1.00 33.52  ? 888 HOH A O      1 
HETATM 4596 O O      . HOH J 5 .   ? -17.418 36.859  -47.446 1.00 31.78  ? 889 HOH A O      1 
HETATM 4597 O O      . HOH J 5 .   ? -18.254 34.260  -48.916 1.00 38.90  ? 890 HOH A O      1 
HETATM 4598 O O      . HOH J 5 .   ? 7.420   20.589  -25.764 1.00 32.61  ? 891 HOH A O      1 
HETATM 4599 O O      . HOH J 5 .   ? -25.912 41.492  -35.799 1.00 42.86  ? 892 HOH A O      1 
HETATM 4600 O O      . HOH J 5 .   ? -18.583 37.714  -10.847 1.00 31.87  ? 893 HOH A O      1 
HETATM 4601 O O      . HOH J 5 .   ? -19.682 51.890  -15.220 1.00 30.56  ? 894 HOH A O      1 
HETATM 4602 O O      . HOH J 5 .   ? -9.389  44.712  -40.173 1.00 27.29  ? 895 HOH A O      1 
HETATM 4603 O O      . HOH J 5 .   ? -15.728 45.214  -40.871 1.00 36.99  ? 896 HOH A O      1 
HETATM 4604 O O      . HOH J 5 .   ? -25.686 43.459  -33.246 1.00 24.79  ? 897 HOH A O      1 
HETATM 4605 O O      . HOH J 5 .   ? -20.408 45.271  -33.888 1.00 29.25  ? 898 HOH A O      1 
HETATM 4606 O O      . HOH K 5 .   ? -6.251  2.165   -2.515  1.00 22.16  ? 801 HOH B O      1 
HETATM 4607 O O      . HOH K 5 .   ? -12.892 -12.786 -14.147 1.00 30.62  ? 802 HOH B O      1 
HETATM 4608 O O      . HOH K 5 .   ? 9.191   4.749   9.207   1.00 23.56  ? 803 HOH B O      1 
HETATM 4609 O O      . HOH K 5 .   ? 0.101   20.551  -14.061 1.00 19.77  ? 804 HOH B O      1 
HETATM 4610 O O      . HOH K 5 .   ? 10.279  -3.404  -19.946 1.00 33.29  ? 805 HOH B O      1 
HETATM 4611 O O      . HOH K 5 .   ? 1.693   14.071  -11.953 1.00 18.14  ? 806 HOH B O      1 
HETATM 4612 O O      . HOH K 5 .   ? -6.484  13.064  -19.056 1.00 23.43  ? 807 HOH B O      1 
HETATM 4613 O O      . HOH K 5 .   ? -8.835  22.021  -14.670 1.00 20.09  ? 808 HOH B O      1 
HETATM 4614 O O      . HOH K 5 .   ? -1.273  3.120   -2.470  1.00 22.03  ? 809 HOH B O      1 
HETATM 4615 O O      . HOH K 5 .   ? 3.760   -11.151 -1.436  1.00 26.18  ? 810 HOH B O      1 
HETATM 4616 O O      . HOH K 5 .   ? -1.614  -14.167 -7.258  1.00 27.28  ? 811 HOH B O      1 
HETATM 4617 O O      . HOH K 5 .   ? -4.221  9.327   5.256   1.00 29.84  ? 812 HOH B O      1 
HETATM 4618 O O      . HOH K 5 .   ? -16.848 14.152  -12.031 1.00 26.47  ? 813 HOH B O      1 
HETATM 4619 O O      . HOH K 5 .   ? -5.019  -16.356 -12.765 1.00 22.60  ? 814 HOH B O      1 
HETATM 4620 O O      . HOH K 5 .   ? -10.546 8.856   -23.943 1.00 28.02  ? 815 HOH B O      1 
HETATM 4621 O O      . HOH K 5 .   ? 4.178   -23.472 -24.035 1.00 40.17  ? 816 HOH B O      1 
HETATM 4622 O O      . HOH K 5 .   ? -40.943 -3.924  4.750   1.00 36.56  ? 817 HOH B O      1 
HETATM 4623 O O      . HOH K 5 .   ? -21.886 6.651   -21.046 1.00 32.65  ? 818 HOH B O      1 
HETATM 4624 O O      . HOH K 5 .   ? 1.141   11.269  -12.091 1.00 19.07  ? 819 HOH B O      1 
HETATM 4625 O O      . HOH K 5 .   ? 11.853  2.559   5.545   1.00 36.29  ? 820 HOH B O      1 
HETATM 4626 O O      . HOH K 5 .   ? -12.255 22.610  -11.612 1.00 35.75  ? 821 HOH B O      1 
HETATM 4627 O O      . HOH K 5 .   ? 1.395   -17.909 -13.522 1.00 27.59  ? 822 HOH B O      1 
HETATM 4628 O O      . HOH K 5 .   ? -13.036 12.208  1.692   1.00 40.67  ? 823 HOH B O      1 
HETATM 4629 O O      . HOH K 5 .   ? -32.626 10.634  8.258   1.00 31.18  ? 824 HOH B O      1 
HETATM 4630 O O      . HOH K 5 .   ? -15.918 27.297  -3.177  1.00 52.15  ? 825 HOH B O      1 
HETATM 4631 O O      . HOH K 5 .   ? -11.247 -3.729  -3.800  1.00 24.23  ? 826 HOH B O      1 
HETATM 4632 O O      . HOH K 5 .   ? -17.805 3.336   -3.790  1.00 33.66  ? 827 HOH B O      1 
HETATM 4633 O O      . HOH K 5 .   ? -12.019 8.028   -21.244 1.00 30.00  ? 828 HOH B O      1 
HETATM 4634 O O      . HOH K 5 .   ? -20.479 7.229   7.541   1.00 50.67  ? 829 HOH B O      1 
HETATM 4635 O O      . HOH K 5 .   ? -3.915  -14.842 6.402   1.00 36.29  ? 830 HOH B O      1 
HETATM 4636 O O      . HOH K 5 .   ? -28.626 12.864  -10.434 1.00 29.17  ? 831 HOH B O      1 
HETATM 4637 O O      . HOH K 5 .   ? -19.323 -12.186 -15.075 1.00 47.78  ? 832 HOH B O      1 
HETATM 4638 O O      . HOH K 5 .   ? 8.044   -11.809 -5.829  1.00 43.76  ? 833 HOH B O      1 
HETATM 4639 O O      . HOH K 5 .   ? -21.063 -8.477  -19.698 1.00 32.23  ? 834 HOH B O      1 
HETATM 4640 O O      . HOH K 5 .   ? 10.372  -3.210  -7.208  1.00 21.10  ? 835 HOH B O      1 
HETATM 4641 O O      . HOH K 5 .   ? -43.617 15.907  0.647   1.00 35.63  ? 836 HOH B O      1 
HETATM 4642 O O      . HOH K 5 .   ? -14.413 14.890  -18.843 1.00 27.72  ? 837 HOH B O      1 
HETATM 4643 O O      . HOH K 5 .   ? -27.621 -1.191  -9.464  1.00 41.82  ? 838 HOH B O      1 
HETATM 4644 O O      . HOH K 5 .   ? -12.771 1.819   0.630   1.00 29.55  ? 839 HOH B O      1 
HETATM 4645 O O      . HOH K 5 .   ? -26.341 5.413   -24.704 1.00 42.14  ? 840 HOH B O      1 
HETATM 4646 O O      . HOH K 5 .   ? -0.509  21.388  -11.943 1.00 19.61  ? 841 HOH B O      1 
HETATM 4647 O O      . HOH K 5 .   ? -27.435 18.253  -11.202 1.00 26.76  ? 842 HOH B O      1 
HETATM 4648 O O      . HOH K 5 .   ? 2.881   -3.343  -0.896  1.00 31.34  ? 843 HOH B O      1 
HETATM 4649 O O      . HOH K 5 .   ? 6.603   -3.581  -4.089  1.00 35.13  ? 844 HOH B O      1 
HETATM 4650 O O      . HOH K 5 .   ? 6.858   11.711  -12.535 1.00 23.89  ? 845 HOH B O      1 
HETATM 4651 O O      . HOH K 5 .   ? -18.017 -13.900 -4.571  1.00 41.81  ? 846 HOH B O      1 
HETATM 4652 O O      . HOH K 5 .   ? -41.725 13.389  -4.537  1.00 25.90  ? 847 HOH B O      1 
HETATM 4653 O O      . HOH K 5 .   ? -39.100 3.987   7.809   1.00 25.29  ? 848 HOH B O      1 
HETATM 4654 O O      . HOH K 5 .   ? -20.915 18.542  -12.844 1.00 35.91  ? 849 HOH B O      1 
HETATM 4655 O O      . HOH K 5 .   ? -18.336 23.485  -11.762 1.00 33.11  ? 850 HOH B O      1 
HETATM 4656 O O      . HOH K 5 .   ? -10.723 -8.262  -0.777  1.00 30.95  ? 851 HOH B O      1 
HETATM 4657 O O      . HOH K 5 .   ? 1.267   -17.697 -8.719  1.00 32.71  ? 852 HOH B O      1 
HETATM 4658 O O      . HOH K 5 .   ? -28.869 9.321   10.523  1.00 41.25  ? 853 HOH B O      1 
HETATM 4659 O O      . HOH K 5 .   ? 8.496   3.937   -16.666 1.00 24.58  ? 854 HOH B O      1 
HETATM 4660 O O      . HOH K 5 .   ? 3.827   13.169  -21.063 1.00 28.68  ? 855 HOH B O      1 
HETATM 4661 O O      . HOH K 5 .   ? -7.922  -15.412 -6.261  1.00 16.59  ? 856 HOH B O      1 
HETATM 4662 O O      . HOH K 5 .   ? -32.126 17.205  -11.222 1.00 22.35  ? 857 HOH B O      1 
HETATM 4663 O O      . HOH K 5 .   ? -21.848 25.140  -2.227  1.00 40.63  ? 858 HOH B O      1 
HETATM 4664 O O      . HOH K 5 .   ? -20.260 -16.240 -8.453  1.00 44.56  ? 859 HOH B O      1 
HETATM 4665 O O      . HOH K 5 .   ? -35.413 20.092  -6.055  1.00 35.77  ? 860 HOH B O      1 
HETATM 4666 O O      . HOH K 5 .   ? -3.436  -19.861 5.701   1.00 28.40  ? 861 HOH B O      1 
HETATM 4667 O O      . HOH K 5 .   ? -14.237 -12.919 -22.735 1.00 24.17  ? 862 HOH B O      1 
HETATM 4668 O O      . HOH K 5 .   ? -22.121 -9.186  -11.001 1.00 34.45  ? 863 HOH B O      1 
HETATM 4669 O O      . HOH K 5 .   ? 11.490  1.631   -15.123 1.00 30.32  ? 864 HOH B O      1 
HETATM 4670 O O      . HOH K 5 .   ? -10.234 12.991  2.314   1.00 40.11  ? 865 HOH B O      1 
HETATM 4671 O O      . HOH K 5 .   ? -34.409 5.023   9.365   1.00 24.29  ? 866 HOH B O      1 
HETATM 4672 O O      . HOH K 5 .   ? -3.328  -22.409 -15.753 1.00 33.98  ? 867 HOH B O      1 
HETATM 4673 O O      . HOH K 5 .   ? -24.380 22.707  -13.771 1.00 42.19  ? 868 HOH B O      1 
HETATM 4674 O O      . HOH K 5 .   ? -16.686 3.758   9.659   1.00 29.06  ? 869 HOH B O      1 
HETATM 4675 O O      . HOH K 5 .   ? -13.397 -9.646  4.919   1.00 32.16  ? 870 HOH B O      1 
HETATM 4676 O O      . HOH K 5 .   ? -3.182  -24.010 -26.608 1.00 32.03  ? 871 HOH B O      1 
HETATM 4677 O O      . HOH K 5 .   ? -40.676 27.415  -4.154  1.00 30.77  ? 872 HOH B O      1 
HETATM 4678 O O      . HOH K 5 .   ? -4.952  -23.097 -29.570 1.00 29.51  ? 873 HOH B O      1 
HETATM 4679 O O      . HOH K 5 .   ? -22.986 8.899   14.366  1.00 27.79  ? 874 HOH B O      1 
HETATM 4680 O O      . HOH K 5 .   ? -35.956 15.527  -19.354 1.00 32.84  ? 875 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   . SER A 1   ? 0.9649 0.8850 1.1079 -0.1439 -0.1370 0.0231  340 SER A N   
2    C CA  . SER A 1   ? 0.9863 0.9187 1.1330 -0.1407 -0.1424 0.0035  340 SER A CA  
3    C C   . SER A 1   ? 1.1671 1.1405 1.2953 -0.1391 -0.1229 0.0049  340 SER A C   
4    O O   . SER A 1   ? 1.1388 1.1266 1.2670 -0.1342 -0.1261 -0.0110 340 SER A O   
5    C CB  . SER A 1   ? 1.0196 0.9421 1.2007 -0.1642 -0.1630 0.0099  340 SER A CB  
6    O OG  . SER A 1   ? 1.0881 1.0199 1.2756 -0.1596 -0.1713 -0.0120 340 SER A OG  
7    N N   . LEU A 2   ? 1.0678 1.0593 1.1818 -0.1422 -0.1046 0.0228  341 LEU A N   
8    C CA  . LEU A 2   ? 0.8866 0.9157 0.9847 -0.1385 -0.0864 0.0232  341 LEU A CA  
9    C C   . LEU A 2   ? 0.9509 1.0065 1.0707 -0.1555 -0.0912 0.0234  341 LEU A C   
10   O O   . LEU A 2   ? 1.2833 1.3412 1.4264 -0.1801 -0.0974 0.0395  341 LEU A O   
11   C CB  . LEU A 2   ? 0.8538 0.8807 0.9247 -0.1114 -0.0800 0.0032  341 LEU A CB  
12   C CG  . LEU A 2   ? 0.8568 0.8677 0.9070 -0.0964 -0.0703 0.0041  341 LEU A CG  
13   C CD1 . LEU A 2   ? 0.8828 0.8933 0.9059 -0.0732 -0.0648 -0.0152 341 LEU A CD1 
14   C CD2 . LEU A 2   ? 1.0875 1.1162 1.1311 -0.1036 -0.0541 0.0245  341 LEU A CD2 
15   N N   . THR A 3   ? 0.7484 0.8250 0.8626 -0.1442 -0.0893 0.0069  342 THR A N   
16   C CA  . THR A 3   ? 0.7049 0.8098 0.8434 -0.1580 -0.0947 0.0032  342 THR A CA  
17   C C   . THR A 3   ? 0.7649 0.8653 0.8978 -0.1398 -0.1067 -0.0221 342 THR A C   
18   O O   . THR A 3   ? 0.7166 0.8254 0.8255 -0.1202 -0.0996 -0.0319 342 THR A O   
19   C CB  . THR A 3   ? 0.5995 0.7487 0.7392 -0.1649 -0.0770 0.0119  342 THR A CB  
20   O OG1 . THR A 3   ? 0.5743 0.7287 0.7149 -0.1825 -0.0662 0.0354  342 THR A OG1 
21   C CG2 . THR A 3   ? 0.6116 0.7949 0.7809 -0.1786 -0.0823 0.0053  342 THR A CG2 
22   N N   . VAL A 4   ? 0.7540 0.8401 0.9084 -0.1468 -0.1261 -0.0320 343 VAL A N   
23   C CA  . VAL A 4   ? 0.7539 0.8346 0.9025 -0.1306 -0.1404 -0.0571 343 VAL A CA  
24   C C   . VAL A 4   ? 0.7624 0.8819 0.9218 -0.1319 -0.1393 -0.0631 343 VAL A C   
25   O O   . VAL A 4   ? 0.7647 0.9111 0.9561 -0.1532 -0.1387 -0.0546 343 VAL A O   
26   C CB  . VAL A 4   ? 0.6941 0.7478 0.8660 -0.1382 -0.1634 -0.0676 343 VAL A CB  
27   C CG1 . VAL A 4   ? 0.6900 0.7447 0.8582 -0.1240 -0.1794 -0.0942 343 VAL A CG1 
28   C CG2 . VAL A 4   ? 0.7572 0.7716 0.9184 -0.1306 -0.1668 -0.0679 343 VAL A CG2 
29   N N   . TYR A 5   ? 0.6620 0.7855 0.7957 -0.1096 -0.1395 -0.0776 344 TYR A N   
30   C CA  . TYR A 5   ? 0.5954 0.7533 0.7368 -0.1056 -0.1400 -0.0846 344 TYR A CA  
31   C C   . TYR A 5   ? 0.6283 0.7825 0.7739 -0.0968 -0.1623 -0.1068 344 TYR A C   
32   O O   . TYR A 5   ? 0.6554 0.7801 0.7777 -0.0835 -0.1730 -0.1193 344 TYR A O   
33   C CB  . TYR A 5   ? 0.5897 0.7542 0.6990 -0.0870 -0.1260 -0.0820 344 TYR A CB  
34   C CG  . TYR A 5   ? 0.5820 0.7664 0.6955 -0.0961 -0.1049 -0.0637 344 TYR A CG  
35   C CD1 . TYR A 5   ? 0.5236 0.7497 0.6652 -0.1073 -0.0988 -0.0613 344 TYR A CD1 
36   C CD2 . TYR A 5   ? 0.5679 0.7323 0.6582 -0.0929 -0.0914 -0.0509 344 TYR A CD2 
37   C CE1 . TYR A 5   ? 0.4756 0.7227 0.6190 -0.1153 -0.0796 -0.0470 344 TYR A CE1 
38   C CE2 . TYR A 5   ? 0.5440 0.7269 0.6366 -0.1009 -0.0736 -0.0354 344 TYR A CE2 
39   C CZ  . TYR A 5   ? 0.5635 0.7876 0.6812 -0.1121 -0.0677 -0.0337 344 TYR A CZ  
40   O OH  . TYR A 5   ? 0.4841 0.7292 0.6021 -0.1198 -0.0500 -0.0205 344 TYR A OH  
41   N N   . LYS A 6   ? 0.6090 0.7961 0.7848 -0.1039 -0.1694 -0.1131 345 LYS A N   
42   C CA  . LYS A 6   ? 0.4940 0.6836 0.6743 -0.0938 -0.1915 -0.1345 345 LYS A CA  
43   C C   . LYS A 6   ? 0.4704 0.6672 0.6207 -0.0706 -0.1912 -0.1407 345 LYS A C   
44   O O   . LYS A 6   ? 0.4274 0.6501 0.5834 -0.0695 -0.1784 -0.1330 345 LYS A O   
45   C CB  . LYS A 6   ? 0.4544 0.6781 0.6863 -0.1131 -0.2005 -0.1392 345 LYS A CB  
46   C CG  . LYS A 6   ? 0.5235 0.7518 0.7893 -0.1426 -0.1938 -0.1234 345 LYS A CG  
47   C CD  . LYS A 6   ? 0.6102 0.8822 0.9271 -0.1630 -0.1982 -0.1266 345 LYS A CD  
48   C CE  . LYS A 6   ? 0.5936 0.8834 0.9384 -0.1945 -0.1829 -0.1041 345 LYS A CE  
49   N NZ  . LYS A 6   ? 0.6111 0.8622 0.9623 -0.2106 -0.1929 -0.0947 345 LYS A NZ  
50   N N   . TYR A 7   ? 0.4742 0.6478 0.5922 -0.0524 -0.2063 -0.1548 346 TYR A N   
51   C CA  . TYR A 7   ? 0.4787 0.6535 0.5639 -0.0313 -0.2091 -0.1579 346 TYR A CA  
52   C C   . TYR A 7   ? 0.4640 0.6756 0.5805 -0.0309 -0.2153 -0.1620 346 TYR A C   
53   O O   . TYR A 7   ? 0.4577 0.6769 0.5597 -0.0185 -0.2101 -0.1571 346 TYR A O   
54   C CB  . TYR A 7   ? 0.5472 0.6971 0.5971 -0.0158 -0.2287 -0.1740 346 TYR A CB  
55   C CG  . TYR A 7   ? 0.5241 0.6725 0.5380 0.0039  -0.2364 -0.1754 346 TYR A CG  
56   C CD1 . TYR A 7   ? 0.5201 0.6543 0.4933 0.0140  -0.2209 -0.1619 346 TYR A CD1 
57   C CD2 . TYR A 7   ? 0.5496 0.7094 0.5712 0.0118  -0.2609 -0.1895 346 TYR A CD2 
58   C CE1 . TYR A 7   ? 0.5606 0.6900 0.5005 0.0301  -0.2298 -0.1603 346 TYR A CE1 
59   C CE2 . TYR A 7   ? 0.5585 0.7131 0.5464 0.0294  -0.2712 -0.1886 346 TYR A CE2 
60   C CZ  . TYR A 7   ? 0.5562 0.6946 0.5027 0.0378  -0.2557 -0.1730 346 TYR A CZ  
61   O OH  . TYR A 7   ? 0.5770 0.7071 0.4897 0.0533  -0.2677 -0.1692 346 TYR A OH  
62   N N   . GLU A 8   ? 0.4653 0.7007 0.6278 -0.0443 -0.2271 -0.1719 347 GLU A N   
63   C CA  . GLU A 8   ? 0.4529 0.7294 0.6527 -0.0446 -0.2326 -0.1790 347 GLU A CA  
64   C C   . GLU A 8   ? 0.4217 0.7235 0.6317 -0.0483 -0.2088 -0.1656 347 GLU A C   
65   O O   . GLU A 8   ? 0.4144 0.7308 0.6221 -0.0335 -0.2103 -0.1689 347 GLU A O   
66   C CB  . GLU A 8   ? 0.4563 0.7583 0.7094 -0.0644 -0.2434 -0.1890 347 GLU A CB  
67   C CG  . GLU A 8   ? 0.4907 0.7624 0.7384 -0.0692 -0.2602 -0.1977 347 GLU A CG  
68   C CD  . GLU A 8   ? 0.5883 0.8808 0.8909 -0.0954 -0.2653 -0.2006 347 GLU A CD  
69   O OE1 . GLU A 8   ? 0.4729 0.8083 0.8181 -0.1050 -0.2636 -0.2033 347 GLU A OE1 
70   O OE2 . GLU A 8   ? 0.6175 0.8831 0.9212 -0.1066 -0.2702 -0.1994 347 GLU A OE2 
71   N N   . ASP A 9   ? 0.4060 0.7122 0.6274 -0.0680 -0.1884 -0.1509 348 ASP A N   
72   C CA  . ASP A 9   ? 0.3787 0.7108 0.6082 -0.0731 -0.1654 -0.1390 348 ASP A CA  
73   C C   . ASP A 9   ? 0.3734 0.6857 0.5611 -0.0516 -0.1585 -0.1333 348 ASP A C   
74   O O   . ASP A 9   ? 0.3545 0.6911 0.5505 -0.0477 -0.1468 -0.1310 348 ASP A O   
75   C CB  . ASP A 9   ? 0.3906 0.7209 0.6276 -0.0970 -0.1471 -0.1212 348 ASP A CB  
76   C CG  . ASP A 9   ? 0.4438 0.7864 0.7200 -0.1210 -0.1555 -0.1233 348 ASP A CG  
77   O OD1 . ASP A 9   ? 0.3797 0.7613 0.6958 -0.1276 -0.1627 -0.1353 348 ASP A OD1 
78   O OD2 . ASP A 9   ? 0.4979 0.8109 0.7676 -0.1331 -0.1562 -0.1136 348 ASP A OD2 
79   N N   . LEU A 10  ? 0.3919 0.6618 0.5354 -0.0380 -0.1656 -0.1318 349 LEU A N   
80   C CA  . LEU A 10  ? 0.4011 0.6510 0.5042 -0.0198 -0.1596 -0.1247 349 LEU A CA  
81   C C   . LEU A 10  ? 0.4017 0.6587 0.5022 -0.0010 -0.1777 -0.1356 349 LEU A C   
82   O O   . LEU A 10  ? 0.4056 0.6688 0.5010 0.0092  -0.1722 -0.1313 349 LEU A O   
83   C CB  . LEU A 10  ? 0.4309 0.6378 0.4883 -0.0139 -0.1589 -0.1195 349 LEU A CB  
84   C CG  . LEU A 10  ? 0.4044 0.5988 0.4657 -0.0300 -0.1461 -0.1108 349 LEU A CG  
85   C CD1 . LEU A 10  ? 0.4453 0.6017 0.4630 -0.0207 -0.1440 -0.1089 349 LEU A CD1 
86   C CD2 . LEU A 10  ? 0.3761 0.5895 0.4543 -0.0424 -0.1241 -0.0958 349 LEU A CD2 
87   N N   . GLN A 11  ? 0.4248 0.6797 0.5299 0.0042  -0.2016 -0.1499 350 GLN A N   
88   C CA  . GLN A 11  ? 0.4384 0.7009 0.5457 0.0216  -0.2230 -0.1604 350 GLN A CA  
89   C C   . GLN A 11  ? 0.4141 0.7190 0.5673 0.0211  -0.2184 -0.1659 350 GLN A C   
90   O O   . GLN A 11  ? 0.4139 0.7190 0.5607 0.0366  -0.2226 -0.1653 350 GLN A O   
91   C CB  . GLN A 11  ? 0.4648 0.7266 0.5811 0.0234  -0.2498 -0.1771 350 GLN A CB  
92   C CG  . GLN A 11  ? 0.4999 0.7210 0.5624 0.0335  -0.2629 -0.1772 350 GLN A CG  
93   C CD  . GLN A 11  ? 0.5271 0.7505 0.6006 0.0353  -0.2909 -0.1959 350 GLN A CD  
94   O OE1 . GLN A 11  ? 0.5190 0.7646 0.6381 0.0214  -0.2928 -0.2051 350 GLN A OE1 
95   N NE2 . GLN A 11  ? 0.5723 0.7673 0.6019 0.0499  -0.3047 -0.1952 350 GLN A NE2 
96   N N   . ASN A 12  ? 0.3959 0.7383 0.5970 0.0028  -0.2100 -0.1718 351 ASN A N   
97   C CA  . ASN A 12  ? 0.3750 0.7665 0.6242 0.0013  -0.2051 -0.1814 351 ASN A CA  
98   C C   . ASN A 12  ? 0.3533 0.7499 0.5929 0.0036  -0.1825 -0.1704 351 ASN A C   
99   O O   . ASN A 12  ? 0.3450 0.7659 0.6054 0.0155  -0.1848 -0.1798 351 ASN A O   
100  C CB  . ASN A 12  ? 0.3636 0.7960 0.6629 -0.0230 -0.1982 -0.1878 351 ASN A CB  
101  C CG  . ASN A 12  ? 0.3867 0.8121 0.6980 -0.0266 -0.2209 -0.1989 351 ASN A CG  
102  O OD1 . ASN A 12  ? 0.4125 0.8128 0.7034 -0.0081 -0.2422 -0.2054 351 ASN A OD1 
103  N ND2 . ASN A 12  ? 0.3843 0.8247 0.7235 -0.0512 -0.2140 -0.1969 351 ASN A ND2 
104  N N   . ALA A 13  ? 0.3701 0.7443 0.5808 -0.0068 -0.1620 -0.1523 352 ALA A N   
105  C CA  . ALA A 13  ? 0.4136 0.7913 0.6139 -0.0050 -0.1413 -0.1420 352 ALA A CA  
106  C C   . ALA A 13  ? 0.4648 0.8132 0.6327 0.0186  -0.1510 -0.1399 352 ALA A C   
107  O O   . ALA A 13  ? 0.5239 0.8861 0.6999 0.0265  -0.1440 -0.1411 352 ALA A O   
108  C CB  . ALA A 13  ? 0.3633 0.7209 0.5402 -0.0210 -0.1206 -0.1231 352 ALA A CB  
109  N N   . THR A 14  ? 0.4246 0.7331 0.5554 0.0293  -0.1676 -0.1367 353 THR A N   
110  C CA  . THR A 14  ? 0.4526 0.7289 0.5468 0.0485  -0.1777 -0.1304 353 THR A CA  
111  C C   . THR A 14  ? 0.4953 0.7751 0.6014 0.0656  -0.2073 -0.1439 353 THR A C   
112  O O   . THR A 14  ? 0.5784 0.8259 0.6496 0.0804  -0.2218 -0.1370 353 THR A O   
113  C CB  . THR A 14  ? 0.4753 0.7066 0.5153 0.0486  -0.1761 -0.1169 353 THR A CB  
114  O OG1 . THR A 14  ? 0.5404 0.7641 0.5754 0.0476  -0.1938 -0.1259 353 THR A OG1 
115  C CG2 . THR A 14  ? 0.4508 0.6772 0.4822 0.0336  -0.1495 -0.1046 353 THR A CG2 
116  N N   . ASN A 15  ? 0.4400 0.7589 0.5953 0.0631  -0.2173 -0.1622 354 ASN A N   
117  C CA  . ASN A 15  ? 0.4595 0.7839 0.6318 0.0794  -0.2486 -0.1773 354 ASN A CA  
118  C C   . ASN A 15  ? 0.4969 0.7766 0.6208 0.0869  -0.2687 -0.1705 354 ASN A C   
119  O O   . ASN A 15  ? 0.5501 0.8019 0.6512 0.1021  -0.2855 -0.1657 354 ASN A O   
120  C CB  . ASN A 15  ? 0.5078 0.8317 0.6902 0.0959  -0.2524 -0.1786 354 ASN A CB  
121  C CG  . ASN A 15  ? 0.5152 0.8879 0.7540 0.0912  -0.2374 -0.1935 354 ASN A CG  
122  O OD1 . ASN A 15  ? 0.4545 0.8618 0.7165 0.0730  -0.2166 -0.1960 354 ASN A OD1 
123  N ND2 . ASN A 15  ? 0.4919 0.8666 0.7513 0.1069  -0.2475 -0.2031 354 ASN A ND2 
124  N N   . PHE A 16  ? 0.4630 0.7332 0.5699 0.0742  -0.2637 -0.1684 355 PHE A N   
125  C CA  . PHE A 16  ? 0.4962 0.7288 0.5543 0.0799  -0.2804 -0.1648 355 PHE A CA  
126  C C   . PHE A 16  ? 0.6395 0.8329 0.6409 0.0902  -0.2779 -0.1462 355 PHE A C   
127  O O   . PHE A 16  ? 0.6552 0.8193 0.6197 0.1001  -0.2944 -0.1404 355 PHE A O   
128  C CB  . PHE A 16  ? 0.5272 0.7580 0.5984 0.0870  -0.3024 -0.1746 355 PHE A CB  
129  C CG  . PHE A 16  ? 0.5150 0.7796 0.6376 0.0745  -0.3026 -0.1904 355 PHE A CG  
130  C CD1 . PHE A 16  ? 0.4867 0.7936 0.6658 0.0688  -0.2928 -0.1992 355 PHE A CD1 
131  C CD2 . PHE A 16  ? 0.5343 0.7889 0.6484 0.0673  -0.3110 -0.1965 355 PHE A CD2 
132  C CE1 . PHE A 16  ? 0.4789 0.8173 0.7039 0.0545  -0.2908 -0.2112 355 PHE A CE1 
133  C CE2 . PHE A 16  ? 0.5258 0.8093 0.6881 0.0540  -0.3115 -0.2092 355 PHE A CE2 
134  C CZ  . PHE A 16  ? 0.4984 0.8240 0.7156 0.0467  -0.3009 -0.2153 355 PHE A CZ  
135  N N   . PHE A 17  ? 0.6418 0.8321 0.6366 0.0843  -0.2511 -0.1330 356 PHE A N   
136  C CA  . PHE A 17  ? 0.5942 0.7507 0.5406 0.0907  -0.2443 -0.1143 356 PHE A CA  
137  C C   . PHE A 17  ? 0.6744 0.8189 0.6142 0.1078  -0.2691 -0.1119 356 PHE A C   
138  O O   . PHE A 17  ? 0.7834 0.8952 0.6766 0.1148  -0.2831 -0.1010 356 PHE A O   
139  C CB  . PHE A 17  ? 0.5526 0.6787 0.4453 0.0870  -0.2410 -0.1066 356 PHE A CB  
140  C CG  . PHE A 17  ? 0.5518 0.6856 0.4540 0.0718  -0.2206 -0.1101 356 PHE A CG  
141  C CD1 . PHE A 17  ? 0.5334 0.6622 0.4281 0.0636  -0.1931 -0.0982 356 PHE A CD1 
142  C CD2 . PHE A 17  ? 0.5486 0.6936 0.4700 0.0658  -0.2311 -0.1255 356 PHE A CD2 
143  C CE1 . PHE A 17  ? 0.4819 0.6148 0.3870 0.0503  -0.1777 -0.1005 356 PHE A CE1 
144  C CE2 . PHE A 17  ? 0.5385 0.6867 0.4710 0.0516  -0.2154 -0.1277 356 PHE A CE2 
145  C CZ  . PHE A 17  ? 0.4792 0.6205 0.4033 0.0441  -0.1892 -0.1148 356 PHE A CZ  
146  N N   . SER A 18  ? 0.9431 1.1151 0.9318 0.1135  -0.2731 -0.1220 357 SER A N   
147  C CA  . SER A 18  ? 1.0238 1.1875 1.0249 0.1284  -0.2950 -0.1236 357 SER A CA  
148  C C   . SER A 18  ? 1.0576 1.2034 1.0469 0.1363  -0.2920 -0.1106 357 SER A C   
149  O O   . SER A 18  ? 1.0415 1.2040 1.0714 0.1440  -0.2949 -0.1198 357 SER A O   
150  C CB  . SER A 18  ? 0.9812 1.1861 1.0473 0.1298  -0.2986 -0.1455 357 SER A CB  
151  O OG  . SER A 18  ? 0.9553 1.1944 1.0585 0.1260  -0.2794 -0.1524 357 SER A OG  
152  N N   . GLU A 19  ? 0.8020 0.9139 0.7374 0.1340  -0.2852 -0.0900 358 GLU A N   
153  C CA  . GLU A 19  ? 0.6995 0.7927 0.6248 0.1383  -0.2789 -0.0756 358 GLU A CA  
154  C C   . GLU A 19  ? 0.7363 0.8636 0.7102 0.1352  -0.2575 -0.0865 358 GLU A C   
155  O O   . GLU A 19  ? 0.7464 0.8699 0.7352 0.1434  -0.2602 -0.0852 358 GLU A O   
156  C CB  . GLU A 19  ? 0.7591 0.8244 0.6804 0.1501  -0.3036 -0.0684 358 GLU A CB  
157  C CG  . GLU A 19  ? 0.8198 0.8526 0.6938 0.1482  -0.3174 -0.0551 358 GLU A CG  
158  C CD  . GLU A 19  ? 0.7868 0.7873 0.5993 0.1394  -0.3048 -0.0301 358 GLU A CD  
159  O OE1 . GLU A 19  ? 0.8250 0.8050 0.6270 0.1406  -0.3025 -0.0146 358 GLU A OE1 
160  O OE2 . GLU A 19  ? 0.7549 0.7517 0.5318 0.1308  -0.2962 -0.0271 358 GLU A OE2 
161  N N   . GLU A 20  ? 0.7675 0.9284 0.7663 0.1228  -0.2375 -0.0976 359 GLU A N   
162  C CA  . GLU A 20  ? 0.6360 0.8224 0.6582 0.1125  -0.2079 -0.0995 359 GLU A CA  
163  C C   . GLU A 20  ? 0.6291 0.7885 0.6086 0.1025  -0.1848 -0.0789 359 GLU A C   
164  O O   . GLU A 20  ? 0.6477 0.8237 0.6392 0.0923  -0.1600 -0.0776 359 GLU A O   
165  C CB  . GLU A 20  ? 0.5860 0.8143 0.6449 0.0997  -0.1961 -0.1143 359 GLU A CB  
166  C CG  . GLU A 20  ? 0.6637 0.9331 0.7776 0.1065  -0.2112 -0.1379 359 GLU A CG  
167  C CD  . GLU A 20  ? 0.7571 1.0700 0.9064 0.0891  -0.1945 -0.1489 359 GLU A CD  
168  O OE1 . GLU A 20  ? 0.6403 0.9474 0.7710 0.0728  -0.1726 -0.1369 359 GLU A OE1 
169  O OE2 . GLU A 20  ? 0.7340 1.0871 0.9311 0.0912  -0.2038 -0.1692 359 GLU A OE2 
170  N N   . ASN A 21  ? 0.6384 0.7587 0.5687 0.1051  -0.1930 -0.0633 360 ASN A N   
171  C CA  . ASN A 21  ? 0.6408 0.7383 0.5308 0.0956  -0.1716 -0.0460 360 ASN A CA  
172  C C   . ASN A 21  ? 0.6588 0.7481 0.5494 0.0967  -0.1594 -0.0355 360 ASN A C   
173  O O   . ASN A 21  ? 0.6343 0.7141 0.5330 0.1078  -0.1754 -0.0343 360 ASN A O   
174  C CB  . ASN A 21  ? 0.6174 0.6807 0.4544 0.0977  -0.1839 -0.0338 360 ASN A CB  
175  C CG  . ASN A 21  ? 0.7883 0.8236 0.6049 0.1084  -0.2041 -0.0210 360 ASN A CG  
176  O OD1 . ASN A 21  ? 0.8673 0.9093 0.7158 0.1192  -0.2222 -0.0284 360 ASN A OD1 
177  N ND2 . ASN A 21  ? 0.8454 0.8498 0.6100 0.1048  -0.2015 -0.0020 360 ASN A ND2 
178  N N   . LYS A 22  ? 0.6395 0.7316 0.5238 0.0857  -0.1329 -0.0288 361 LYS A N   
179  C CA  . LYS A 22  ? 0.7230 0.7981 0.5938 0.0852  -0.1213 -0.0150 361 LYS A CA  
180  C C   . LYS A 22  ? 0.8034 0.8406 0.6250 0.0867  -0.1290 0.0030  361 LYS A C   
181  O O   . LYS A 22  ? 0.8825 0.9082 0.6790 0.0886  -0.1431 0.0038  361 LYS A O   
182  C CB  . LYS A 22  ? 0.6555 0.7429 0.5308 0.0730  -0.0930 -0.0123 361 LYS A CB  
183  C CG  . LYS A 22  ? 0.6573 0.7772 0.5750 0.0715  -0.0835 -0.0234 361 LYS A CG  
184  C CD  . LYS A 22  ? 0.6906 0.8019 0.6138 0.0783  -0.0839 -0.0191 361 LYS A CD  
185  C CE  . LYS A 22  ? 0.6162 0.7501 0.5595 0.0711  -0.0628 -0.0220 361 LYS A CE  
186  N NZ  . LYS A 22  ? 0.7371 0.9134 0.7219 0.0710  -0.0620 -0.0411 361 LYS A NZ  
187  N N   . ILE A 23  ? 0.8631 0.8823 0.6700 0.0846  -0.1195 0.0177  362 ILE A N   
188  C CA  . ILE A 23  ? 0.9239 0.9088 0.6861 0.0842  -0.1273 0.0371  362 ILE A CA  
189  C C   . ILE A 23  ? 0.9668 0.9452 0.6886 0.0777  -0.1218 0.0407  362 ILE A C   
190  O O   . ILE A 23  ? 1.0721 1.0346 0.7640 0.0810  -0.1404 0.0457  362 ILE A O   
191  C CB  . ILE A 23  ? 0.9707 0.9419 0.7264 0.0790  -0.1124 0.0519  362 ILE A CB  
192  C CG1 . ILE A 23  ? 0.9696 0.9478 0.7667 0.0870  -0.1203 0.0447  362 ILE A CG1 
193  C CG2 . ILE A 23  ? 1.1411 1.0788 0.8502 0.0754  -0.1196 0.0743  362 ILE A CG2 
194  C CD1 . ILE A 23  ? 0.9258 0.8763 0.7125 0.0865  -0.1237 0.0618  362 ILE A CD1 
195  N N   . LYS A 24  ? 0.9681 0.9587 0.6887 0.0689  -0.0977 0.0372  363 LYS A N   
196  C CA  . LYS A 24  ? 1.0933 1.0796 0.7790 0.0638  -0.0914 0.0367  363 LYS A CA  
197  C C   . LYS A 24  ? 1.0018 0.9931 0.6862 0.0692  -0.1121 0.0240  363 LYS A C   
198  O O   . LYS A 24  ? 1.0384 1.0487 0.7612 0.0726  -0.1199 0.0097  363 LYS A O   
199  C CB  . LYS A 24  ? 1.1981 1.1993 0.8962 0.0559  -0.0666 0.0300  363 LYS A CB  
200  C CG  . LYS A 24  ? 1.0962 1.0948 0.7636 0.0519  -0.0594 0.0254  363 LYS A CG  
201  C CD  . LYS A 24  ? 1.0830 1.0705 0.7167 0.0463  -0.0422 0.0382  363 LYS A CD  
202  C CE  . LYS A 24  ? 1.0212 1.0140 0.6371 0.0424  -0.0306 0.0275  363 LYS A CE  
203  N NZ  . LYS A 24  ? 0.9912 0.9803 0.5815 0.0438  -0.0458 0.0205  363 LYS A NZ  
204  N N   . GLY A 25  ? 0.8680 0.8441 0.5077 0.0693  -0.1209 0.0290  364 GLY A N   
205  C CA  . GLY A 25  ? 0.8996 0.8794 0.5340 0.0744  -0.1416 0.0162  364 GLY A CA  
206  C C   . GLY A 25  ? 0.8525 0.8539 0.5159 0.0715  -0.1344 -0.0038 364 GLY A C   
207  O O   . GLY A 25  ? 0.9225 0.9350 0.6083 0.0757  -0.1519 -0.0174 364 GLY A O   
208  N N   . SER A 26  ? 0.8007 0.8077 0.4663 0.0638  -0.1101 -0.0054 365 SER A N   
209  C CA  . SER A 26  ? 0.7326 0.7555 0.4257 0.0593  -0.1038 -0.0217 365 SER A CA  
210  C C   . SER A 26  ? 0.6443 0.6864 0.3883 0.0555  -0.0969 -0.0247 365 SER A C   
211  O O   . SER A 26  ? 0.6034 0.6589 0.3740 0.0499  -0.0945 -0.0359 365 SER A O   
212  C CB  . SER A 26  ? 0.7644 0.7832 0.4375 0.0537  -0.0837 -0.0232 365 SER A CB  
213  O OG  . SER A 26  ? 0.8499 0.8632 0.5145 0.0505  -0.0648 -0.0086 365 SER A OG  
214  N N   . VAL A 27  ? 0.6754 0.7195 0.4332 0.0578  -0.0943 -0.0154 366 VAL A N   
215  C CA  . VAL A 27  ? 0.6491 0.7142 0.4501 0.0535  -0.0846 -0.0180 366 VAL A CA  
216  C C   . VAL A 27  ? 0.5792 0.6614 0.4116 0.0597  -0.1027 -0.0272 366 VAL A C   
217  O O   . VAL A 27  ? 0.6138 0.6871 0.4407 0.0691  -0.1165 -0.0232 366 VAL A O   
218  C CB  . VAL A 27  ? 0.6292 0.6886 0.4274 0.0520  -0.0680 -0.0051 366 VAL A CB  
219  C CG1 . VAL A 27  ? 0.6360 0.7200 0.4761 0.0482  -0.0597 -0.0093 366 VAL A CG1 
220  C CG2 . VAL A 27  ? 0.6637 0.7112 0.4374 0.0458  -0.0496 0.0015  366 VAL A CG2 
221  N N   . TYR A 28  ? 0.4536 0.5607 0.3212 0.0540  -0.1034 -0.0397 367 TYR A N   
222  C CA  . TYR A 28  ? 0.4816 0.6141 0.3874 0.0582  -0.1174 -0.0519 367 TYR A CA  
223  C C   . TYR A 28  ? 0.4772 0.6415 0.4228 0.0485  -0.1011 -0.0560 367 TYR A C   
224  O O   . TYR A 28  ? 0.4710 0.6370 0.4163 0.0365  -0.0836 -0.0506 367 TYR A O   
225  C CB  . TYR A 28  ? 0.4967 0.6354 0.4097 0.0588  -0.1361 -0.0649 367 TYR A CB  
226  C CG  . TYR A 28  ? 0.5106 0.6223 0.3844 0.0692  -0.1560 -0.0626 367 TYR A CG  
227  C CD1 . TYR A 28  ? 0.5210 0.6086 0.3513 0.0668  -0.1510 -0.0563 367 TYR A CD1 
228  C CD2 . TYR A 28  ? 0.5474 0.6591 0.4273 0.0815  -0.1808 -0.0674 367 TYR A CD2 
229  C CE1 . TYR A 28  ? 0.5486 0.6144 0.3383 0.0746  -0.1683 -0.0536 367 TYR A CE1 
230  C CE2 . TYR A 28  ? 0.6212 0.7072 0.4612 0.0897  -0.2008 -0.0629 367 TYR A CE2 
231  C CZ  . TYR A 28  ? 0.6047 0.6686 0.3976 0.0854  -0.1937 -0.0554 367 TYR A CZ  
232  O OH  . TYR A 28  ? 0.6358 0.6770 0.3845 0.0922  -0.2128 -0.0504 367 TYR A OH  
233  N N   . ARG A 29  ? 0.4548 0.6452 0.4346 0.0538  -0.1080 -0.0661 368 ARG A N   
234  C CA  . ARG A 29  ? 0.4452 0.6740 0.4640 0.0440  -0.0938 -0.0729 368 ARG A CA  
235  C C   . ARG A 29  ? 0.4532 0.7115 0.5045 0.0361  -0.1012 -0.0864 368 ARG A C   
236  O O   . ARG A 29  ? 0.4462 0.7121 0.5120 0.0456  -0.1216 -0.0988 368 ARG A O   
237  C CB  . ARG A 29  ? 0.3348 0.5813 0.3759 0.0543  -0.0954 -0.0799 368 ARG A CB  
238  C CG  . ARG A 29  ? 0.3811 0.6730 0.4598 0.0438  -0.0792 -0.0888 368 ARG A CG  
239  C CD  . ARG A 29  ? 0.3712 0.6786 0.4680 0.0548  -0.0785 -0.0973 368 ARG A CD  
240  N NE  . ARG A 29  ? 0.4478 0.7998 0.5730 0.0432  -0.0596 -0.1049 368 ARG A NE  
241  C CZ  . ARG A 29  ? 0.6247 0.9975 0.7668 0.0495  -0.0538 -0.1143 368 ARG A CZ  
242  N NH1 . ARG A 29  ? 0.6580 1.0085 0.7954 0.0676  -0.0666 -0.1170 368 ARG A NH1 
243  N NH2 . ARG A 29  ? 0.5059 0.9227 0.6694 0.0368  -0.0354 -0.1210 368 ARG A NH2 
244  N N   . ALA A 30  ? 0.4264 0.7002 0.4899 0.0181  -0.0862 -0.0833 369 ALA A N   
245  C CA  . ALA A 30  ? 0.4796 0.7833 0.5770 0.0058  -0.0904 -0.0937 369 ALA A CA  
246  C C   . ALA A 30  ? 0.5142 0.8654 0.6492 -0.0051 -0.0757 -0.0990 369 ALA A C   
247  O O   . ALA A 30  ? 0.4607 0.8160 0.5900 -0.0164 -0.0563 -0.0878 369 ALA A O   
248  C CB  . ALA A 30  ? 0.4345 0.7194 0.5194 -0.0087 -0.0868 -0.0855 369 ALA A CB  
249  N N   . SER A 31  ? 0.7019 1.0908 0.8750 -0.0015 -0.0851 -0.1170 370 SER A N   
250  C CA  . SER A 31  ? 0.6550 1.0982 0.8673 -0.0123 -0.0710 -0.1264 370 SER A CA  
251  C C   . SER A 31  ? 0.6653 1.1385 0.9084 -0.0327 -0.0709 -0.1307 370 SER A C   
252  O O   . SER A 31  ? 0.8112 1.2955 1.0771 -0.0276 -0.0889 -0.1451 370 SER A O   
253  C CB  . SER A 31  ? 0.6706 1.1405 0.9099 0.0066  -0.0809 -0.1467 370 SER A CB  
254  O OG  . SER A 31  ? 0.6833 1.1537 0.9398 0.0180  -0.1056 -0.1609 370 SER A OG  
255  N N   . PHE A 32  ? 0.5302 1.0153 0.7742 -0.0563 -0.0523 -0.1173 371 PHE A N   
256  C CA  . PHE A 32  ? 0.5175 1.0246 0.7881 -0.0794 -0.0523 -0.1166 371 PHE A CA  
257  C C   . PHE A 32  ? 0.5881 1.1078 0.8555 -0.1053 -0.0305 -0.0982 371 PHE A C   
258  O O   . PHE A 32  ? 0.6891 1.1862 0.9260 -0.1036 -0.0190 -0.0840 371 PHE A O   
259  C CB  . PHE A 32  ? 0.4839 0.9478 0.7387 -0.0779 -0.0707 -0.1130 371 PHE A CB  
260  C CG  . PHE A 32  ? 0.5174 0.9304 0.7300 -0.0796 -0.0659 -0.0936 371 PHE A CG  
261  C CD1 . PHE A 32  ? 0.5306 0.9067 0.7050 -0.0594 -0.0672 -0.0894 371 PHE A CD1 
262  C CD2 . PHE A 32  ? 0.6467 1.0492 0.8604 -0.1018 -0.0611 -0.0798 371 PHE A CD2 
263  C CE1 . PHE A 32  ? 0.5232 0.8576 0.6628 -0.0606 -0.0620 -0.0740 371 PHE A CE1 
264  C CE2 . PHE A 32  ? 0.6503 1.0074 0.8298 -0.1015 -0.0583 -0.0648 371 PHE A CE2 
265  C CZ  . PHE A 32  ? 0.5480 0.8733 0.6912 -0.0805 -0.0579 -0.0631 371 PHE A CZ  
266  N N   . LYS A 33  ? 0.5381 1.0940 0.8376 -0.1302 -0.0260 -0.0976 372 LYS A N   
267  C CA  . LYS A 33  ? 0.5837 1.1379 0.8738 -0.1556 -0.0083 -0.0752 372 LYS A CA  
268  C C   . LYS A 33  ? 0.6346 1.1973 0.9048 -0.1515 0.0118  -0.0699 372 LYS A C   
269  O O   . LYS A 33  ? 0.6965 1.2413 0.9420 -0.1633 0.0227  -0.0496 372 LYS A O   
270  C CB  . LYS A 33  ? 0.6366 1.1440 0.9025 -0.1650 -0.0146 -0.0559 372 LYS A CB  
271  C CG  . LYS A 33  ? 0.8683 1.3734 1.1314 -0.1941 -0.0032 -0.0320 372 LYS A CG  
272  C CD  . LYS A 33  ? 0.9772 1.4263 1.2158 -0.1970 -0.0127 -0.0156 372 LYS A CD  
273  C CE  . LYS A 33  ? 0.9471 1.3913 1.1842 -0.2260 -0.0050 0.0098  372 LYS A CE  
274  N NZ  . LYS A 33  ? 0.9484 1.3347 1.1642 -0.2257 -0.0160 0.0238  372 LYS A NZ  
275  N N   . GLY A 34  ? 0.6000 1.1869 0.8802 -0.1336 0.0143  -0.0892 373 GLY A N   
276  C CA  . GLY A 34  ? 0.4522 1.0461 0.7141 -0.1273 0.0297  -0.0892 373 GLY A CA  
277  C C   . GLY A 34  ? 0.5123 1.0790 0.7468 -0.1132 0.0290  -0.0833 373 GLY A C   
278  O O   . GLY A 34  ? 0.5058 1.0757 0.7407 -0.0915 0.0255  -0.0982 373 GLY A O   
279  N N   . ASP A 35  ? 0.5919 1.1302 0.8039 -0.1254 0.0313  -0.0616 374 ASP A N   
280  C CA  . ASP A 35  ? 0.5708 1.0834 0.7565 -0.1143 0.0326  -0.0536 374 ASP A CA  
281  C C   . ASP A 35  ? 0.4754 0.9445 0.6487 -0.0916 0.0139  -0.0598 374 ASP A C   
282  O O   . ASP A 35  ? 0.4605 0.9063 0.6333 -0.0955 0.0021  -0.0565 374 ASP A O   
283  C CB  . ASP A 35  ? 0.5506 1.0340 0.7114 -0.1322 0.0396  -0.0276 374 ASP A CB  
284  C CG  . ASP A 35  ? 0.6374 1.0873 0.7662 -0.1193 0.0437  -0.0186 374 ASP A CG  
285  O OD1 . ASP A 35  ? 0.8424 1.2902 0.9666 -0.0977 0.0422  -0.0312 374 ASP A OD1 
286  O OD2 . ASP A 35  ? 0.6848 1.1077 0.7942 -0.1303 0.0470  0.0011  374 ASP A OD2 
287  N N   . ASP A 36  ? 0.4038 0.8606 0.5657 -0.0685 0.0104  -0.0684 375 ASP A N   
288  C CA  . ASP A 36  ? 0.3997 0.8150 0.5444 -0.0478 -0.0071 -0.0718 375 ASP A CA  
289  C C   . ASP A 36  ? 0.3882 0.7520 0.4958 -0.0485 -0.0066 -0.0534 375 ASP A C   
290  O O   . ASP A 36  ? 0.4286 0.7857 0.5242 -0.0609 0.0062  -0.0387 375 ASP A O   
291  C CB  . ASP A 36  ? 0.4151 0.8306 0.5593 -0.0251 -0.0122 -0.0838 375 ASP A CB  
292  C CG  . ASP A 36  ? 0.4974 0.9536 0.6803 -0.0168 -0.0222 -0.1073 375 ASP A CG  
293  O OD1 . ASP A 36  ? 0.5052 0.9975 0.7170 -0.0309 -0.0208 -0.1144 375 ASP A OD1 
294  O OD2 . ASP A 36  ? 0.4334 0.8854 0.6199 0.0038  -0.0325 -0.1188 375 ASP A OD2 
295  N N   . ALA A 37  ? 0.3312 0.6599 0.4208 -0.0346 -0.0215 -0.0554 376 ALA A N   
296  C CA  . ALA A 37  ? 0.3649 0.6488 0.4212 -0.0332 -0.0216 -0.0425 376 ALA A CA  
297  C C   . ALA A 37  ? 0.3607 0.6142 0.3918 -0.0129 -0.0340 -0.0460 376 ALA A C   
298  O O   . ALA A 37  ? 0.3845 0.6479 0.4250 -0.0006 -0.0456 -0.0570 376 ALA A O   
299  C CB  . ALA A 37  ? 0.3356 0.6102 0.3969 -0.0473 -0.0269 -0.0395 376 ALA A CB  
300  N N   . ALA A 38  ? 0.3370 0.5542 0.3364 -0.0101 -0.0320 -0.0364 377 ALA A N   
301  C CA  . ALA A 38  ? 0.3285 0.5158 0.2975 0.0053  -0.0420 -0.0366 377 ALA A CA  
302  C C   . ALA A 38  ? 0.4006 0.5661 0.3533 0.0034  -0.0497 -0.0384 377 ALA A C   
303  O O   . ALA A 38  ? 0.4124 0.5691 0.3636 -0.0064 -0.0417 -0.0334 377 ALA A O   
304  C CB  . ALA A 38  ? 0.2979 0.4655 0.2422 0.0111  -0.0306 -0.0253 377 ALA A CB  
305  N N   . VAL A 39  ? 0.4196 0.5762 0.3610 0.0133  -0.0669 -0.0467 378 VAL A N   
306  C CA  . VAL A 39  ? 0.4067 0.5450 0.3315 0.0134  -0.0767 -0.0524 378 VAL A CA  
307  C C   . VAL A 39  ? 0.4381 0.5480 0.3183 0.0247  -0.0777 -0.0477 378 VAL A C   
308  O O   . VAL A 39  ? 0.4261 0.5310 0.2914 0.0350  -0.0853 -0.0449 378 VAL A O   
309  C CB  . VAL A 39  ? 0.4345 0.5865 0.3786 0.0146  -0.0969 -0.0665 378 VAL A CB  
310  C CG1 . VAL A 39  ? 0.5168 0.6503 0.4447 0.0143  -0.1076 -0.0746 378 VAL A CG1 
311  C CG2 . VAL A 39  ? 0.4306 0.6168 0.4210 0.0015  -0.0938 -0.0705 378 VAL A CG2 
312  N N   . LYS A 40  ? 0.4706 0.5629 0.3307 0.0222  -0.0706 -0.0470 379 LYS A N   
313  C CA  . LYS A 40  ? 0.5294 0.5997 0.3464 0.0304  -0.0689 -0.0441 379 LYS A CA  
314  C C   . LYS A 40  ? 0.5890 0.6503 0.3902 0.0327  -0.0817 -0.0579 379 LYS A C   
315  O O   . LYS A 40  ? 0.5613 0.6221 0.3778 0.0264  -0.0807 -0.0662 379 LYS A O   
316  C CB  . LYS A 40  ? 0.5165 0.5780 0.3238 0.0271  -0.0483 -0.0351 379 LYS A CB  
317  C CG  . LYS A 40  ? 0.6383 0.6827 0.4056 0.0324  -0.0440 -0.0365 379 LYS A CG  
318  C CD  . LYS A 40  ? 0.6586 0.6984 0.4248 0.0289  -0.0243 -0.0310 379 LYS A CD  
319  C CE  . LYS A 40  ? 0.6342 0.6749 0.3980 0.0290  -0.0127 -0.0153 379 LYS A CE  
320  N NZ  . LYS A 40  ? 0.7493 0.7805 0.4778 0.0350  -0.0161 -0.0081 379 LYS A NZ  
321  N N   . ILE A 41  ? 0.6319 0.6852 0.4026 0.0416  -0.0953 -0.0604 380 ILE A N   
322  C CA  . ILE A 41  ? 0.6421 0.6879 0.3917 0.0451  -0.1088 -0.0748 380 ILE A CA  
323  C C   . ILE A 41  ? 0.6332 0.6654 0.3422 0.0475  -0.0961 -0.0743 380 ILE A C   
324  O O   . ILE A 41  ? 0.6622 0.6878 0.3426 0.0500  -0.0868 -0.0607 380 ILE A O   
325  C CB  . ILE A 41  ? 0.5817 0.6272 0.3169 0.0532  -0.1320 -0.0779 380 ILE A CB  
326  C CG1 . ILE A 41  ? 0.5962 0.6602 0.3763 0.0518  -0.1427 -0.0796 380 ILE A CG1 
327  C CG2 . ILE A 41  ? 0.6638 0.7040 0.3795 0.0563  -0.1478 -0.0952 380 ILE A CG2 
328  C CD1 . ILE A 41  ? 0.6043 0.6687 0.3767 0.0613  -0.1682 -0.0834 380 ILE A CD1 
329  N N   . LEU A 42  ? 0.6534 0.6827 0.3619 0.0465  -0.0959 -0.0901 381 LEU A N   
330  C CA  . LEU A 42  ? 0.6626 0.6848 0.3374 0.0494  -0.0834 -0.0952 381 LEU A CA  
331  C C   . LEU A 42  ? 0.7682 0.7882 0.4231 0.0544  -0.0979 -0.1172 381 LEU A C   
332  O O   . LEU A 42  ? 0.7578 0.7792 0.4405 0.0529  -0.1129 -0.1315 381 LEU A O   
333  C CB  . LEU A 42  ? 0.6694 0.6914 0.3688 0.0445  -0.0653 -0.0954 381 LEU A CB  
334  C CG  . LEU A 42  ? 0.6364 0.6612 0.3508 0.0398  -0.0492 -0.0749 381 LEU A CG  
335  C CD1 . LEU A 42  ? 0.6274 0.6508 0.3643 0.0357  -0.0346 -0.0762 381 LEU A CD1 
336  C CD2 . LEU A 42  ? 0.5826 0.6046 0.2596 0.0432  -0.0406 -0.0606 381 LEU A CD2 
337  N N   . LYS A 43  ? 0.7822 0.8000 0.3886 0.0592  -0.0932 -0.1201 382 LYS A N   
338  C CA  . LYS A 43  ? 0.7706 0.7885 0.3522 0.0642  -0.1059 -0.1418 382 LYS A CA  
339  C C   . LYS A 43  ? 0.7825 0.8013 0.3840 0.0655  -0.1016 -0.1658 382 LYS A C   
340  O O   . LYS A 43  ? 0.7345 0.7541 0.3471 0.0639  -0.0823 -0.1642 382 LYS A O   
341  C CB  . LYS A 43  ? 0.8086 0.8251 0.3473 0.0606  -0.0951 -0.1302 382 LYS A CB  
342  C CG  . LYS A 43  ? 0.8289 0.8475 0.3458 0.0615  -0.1007 -0.1495 382 LYS A CG  
343  C CD  . LYS A 43  ? 0.8962 0.9124 0.4122 0.0642  -0.1276 -0.1556 382 LYS A CD  
344  C CE  . LYS A 43  ? 0.8274 0.8460 0.3148 0.0644  -0.1320 -0.1721 382 LYS A CE  
345  N NZ  . LYS A 43  ? 0.8623 0.8820 0.3028 0.0570  -0.1174 -0.1571 382 LYS A NZ  
346  N N   . GLY A 44  ? 0.7492 0.7666 0.3591 0.0686  -0.1215 -0.1887 383 GLY A N   
347  C CA  . GLY A 44  ? 0.7027 0.7178 0.3345 0.0707  -0.1221 -0.2141 383 GLY A CA  
348  C C   . GLY A 44  ? 0.7161 0.7247 0.4057 0.0631  -0.1197 -0.2090 383 GLY A C   
349  O O   . GLY A 44  ? 0.7122 0.7217 0.4208 0.0561  -0.1114 -0.1851 383 GLY A O   
350  N N   . ASP A 45  ? 0.6911 0.6925 0.4084 0.0641  -0.1281 -0.2313 384 ASP A N   
351  C CA  . ASP A 45  ? 0.6832 0.6753 0.4535 0.0555  -0.1282 -0.2255 384 ASP A CA  
352  C C   . ASP A 45  ? 0.6650 0.6565 0.4367 0.0565  -0.1054 -0.2169 384 ASP A C   
353  O O   . ASP A 45  ? 0.6438 0.6347 0.4070 0.0649  -0.0996 -0.2367 384 ASP A O   
354  C CB  . ASP A 45  ? 0.7027 0.6832 0.5035 0.0561  -0.1487 -0.2519 384 ASP A CB  
355  C CG  . ASP A 45  ? 0.7237 0.6918 0.5794 0.0438  -0.1535 -0.2416 384 ASP A CG  
356  O OD1 . ASP A 45  ? 0.7124 0.6847 0.5814 0.0339  -0.1428 -0.2142 384 ASP A OD1 
357  O OD2 . ASP A 45  ? 0.6622 0.6161 0.5472 0.0435  -0.1689 -0.2608 384 ASP A OD2 
358  N N   . VAL A 46  ? 0.6801 0.6738 0.4639 0.0486  -0.0929 -0.1894 385 VAL A N   
359  C CA  . VAL A 46  ? 0.7357 0.7288 0.5253 0.0485  -0.0730 -0.1794 385 VAL A CA  
360  C C   . VAL A 46  ? 0.7063 0.6878 0.5450 0.0393  -0.0784 -0.1725 385 VAL A C   
361  O O   . VAL A 46  ? 0.6856 0.6668 0.5368 0.0346  -0.0653 -0.1546 385 VAL A O   
362  C CB  . VAL A 46  ? 0.7677 0.7706 0.5341 0.0464  -0.0556 -0.1540 385 VAL A CB  
363  C CG1 . VAL A 46  ? 0.6901 0.7015 0.4053 0.0539  -0.0506 -0.1584 385 VAL A CG1 
364  C CG2 . VAL A 46  ? 0.7763 0.7818 0.5610 0.0372  -0.0626 -0.1346 385 VAL A CG2 
365  N N   . SER A 47  ? 0.6797 0.6507 0.5460 0.0356  -0.0990 -0.1858 386 SER A N   
366  C CA  . SER A 47  ? 0.7155 0.6732 0.6277 0.0238  -0.1072 -0.1766 386 SER A CA  
367  C C   . SER A 47  ? 0.7222 0.6686 0.6481 0.0285  -0.1000 -0.1806 386 SER A C   
368  O O   . SER A 47  ? 0.6615 0.6009 0.6126 0.0190  -0.0972 -0.1615 386 SER A O   
369  C CB  . SER A 47  ? 0.7279 0.6744 0.6665 0.0189  -0.1324 -0.1924 386 SER A CB  
370  O OG  . SER A 47  ? 0.9699 0.9035 0.9516 0.0036  -0.1414 -0.1784 386 SER A OG  
371  N N   . SER A 48  ? 0.7126 0.6593 0.6224 0.0432  -0.0974 -0.2063 387 SER A N   
372  C CA  . SER A 48  ? 0.6807 0.6189 0.6088 0.0499  -0.0925 -0.2152 387 SER A CA  
373  C C   . SER A 48  ? 0.6830 0.6297 0.6050 0.0472  -0.0709 -0.1911 387 SER A C   
374  O O   . SER A 48  ? 0.7324 0.6678 0.6834 0.0442  -0.0717 -0.1827 387 SER A O   
375  C CB  . SER A 48  ? 0.7114 0.6569 0.6205 0.0669  -0.0905 -0.2502 387 SER A CB  
376  O OG  . SER A 48  ? 0.7887 0.7555 0.6488 0.0715  -0.0760 -0.2508 387 SER A OG  
377  N N   . GLU A 49  ? 0.7097 0.6748 0.5950 0.0482  -0.0534 -0.1794 388 GLU A N   
378  C CA  . GLU A 49  ? 0.7179 0.6911 0.5978 0.0456  -0.0337 -0.1578 388 GLU A CA  
379  C C   . GLU A 49  ? 0.6455 0.6125 0.5500 0.0314  -0.0369 -0.1303 388 GLU A C   
380  O O   . GLU A 49  ? 0.6562 0.6224 0.5729 0.0287  -0.0277 -0.1162 388 GLU A O   
381  C CB  . GLU A 49  ? 0.7943 0.7855 0.6304 0.0485  -0.0174 -0.1508 388 GLU A CB  
382  C CG  . GLU A 49  ? 0.7220 0.7250 0.5280 0.0602  -0.0078 -0.1736 388 GLU A CG  
383  C CD  . GLU A 49  ? 0.7556 0.7569 0.5504 0.0662  -0.0236 -0.1994 388 GLU A CD  
384  O OE1 . GLU A 49  ? 0.6845 0.6813 0.4753 0.0613  -0.0377 -0.1940 388 GLU A OE1 
385  O OE2 . GLU A 49  ? 0.8341 0.8403 0.6260 0.0764  -0.0225 -0.2271 388 GLU A OE2 
386  N N   . ILE A 50  ? 0.6881 0.6535 0.6006 0.0219  -0.0498 -0.1232 389 ILE A N   
387  C CA  . ILE A 50  ? 0.6322 0.5978 0.5661 0.0069  -0.0511 -0.0982 389 ILE A CA  
388  C C   . ILE A 50  ? 0.6162 0.5631 0.5862 -0.0003 -0.0619 -0.0945 389 ILE A C   
389  O O   . ILE A 50  ? 0.5906 0.5373 0.5725 -0.0091 -0.0564 -0.0738 389 ILE A O   
390  C CB  . ILE A 50  ? 0.6096 0.5831 0.5457 -0.0017 -0.0617 -0.0946 389 ILE A CB  
391  C CG1 . ILE A 50  ? 0.6060 0.5948 0.5064 0.0064  -0.0540 -0.0966 389 ILE A CG1 
392  C CG2 . ILE A 50  ? 0.5904 0.5700 0.5495 -0.0186 -0.0613 -0.0708 389 ILE A CG2 
393  C CD1 . ILE A 50  ? 0.6099 0.6055 0.5118 0.0029  -0.0684 -0.1016 389 ILE A CD1 
394  N N   . ASN A 51  ? 0.5765 0.5064 0.5644 0.0032  -0.0794 -0.1145 390 ASN A N   
395  C CA  . ASN A 51  ? 0.5924 0.4993 0.6167 -0.0037 -0.0943 -0.1107 390 ASN A CA  
396  C C   . ASN A 51  ? 0.5788 0.4812 0.6080 0.0032  -0.0847 -0.1066 390 ASN A C   
397  O O   . ASN A 51  ? 0.5840 0.4685 0.6408 -0.0047 -0.0956 -0.0945 390 ASN A O   
398  C CB  . ASN A 51  ? 0.6050 0.4931 0.6480 0.0023  -0.1160 -0.1378 390 ASN A CB  
399  C CG  . ASN A 51  ? 0.7320 0.6229 0.7766 -0.0061 -0.1289 -0.1417 390 ASN A CG  
400  O OD1 . ASN A 51  ? 0.7173 0.6188 0.7641 -0.0216 -0.1270 -0.1199 390 ASN A OD1 
401  N ND2 . ASN A 51  ? 0.7201 0.6042 0.7646 0.0044  -0.1424 -0.1715 390 ASN A ND2 
402  N N   . ILE A 52  ? 0.5319 0.4502 0.5356 0.0167  -0.0659 -0.1156 391 ILE A N   
403  C CA  . ILE A 52  ? 0.6139 0.5330 0.6228 0.0229  -0.0548 -0.1118 391 ILE A CA  
404  C C   . ILE A 52  ? 0.5620 0.4956 0.5568 0.0144  -0.0381 -0.0840 391 ILE A C   
405  O O   . ILE A 52  ? 0.5393 0.4666 0.5505 0.0082  -0.0388 -0.0672 391 ILE A O   
406  C CB  . ILE A 52  ? 0.6771 0.6080 0.6701 0.0412  -0.0431 -0.1393 391 ILE A CB  
407  C CG1 . ILE A 52  ? 0.6255 0.5454 0.6307 0.0509  -0.0599 -0.1712 391 ILE A CG1 
408  C CG2 . ILE A 52  ? 0.6148 0.5477 0.6211 0.0478  -0.0336 -0.1384 391 ILE A CG2 
409  C CD1 . ILE A 52  ? 0.6313 0.5251 0.6803 0.0524  -0.0810 -0.1786 391 ILE A CD1 
410  N N   . LEU A 53  ? 0.5378 0.4902 0.5026 0.0142  -0.0248 -0.0794 392 LEU A N   
411  C CA  . LEU A 53  ? 0.5878 0.5544 0.5401 0.0081  -0.0098 -0.0568 392 LEU A CA  
412  C C   . LEU A 53  ? 0.5222 0.4888 0.4885 -0.0086 -0.0167 -0.0348 392 LEU A C   
413  O O   . LEU A 53  ? 0.5306 0.5071 0.4941 -0.0144 -0.0068 -0.0167 392 LEU A O   
414  C CB  . LEU A 53  ? 0.5979 0.5814 0.5160 0.0135  0.0032  -0.0592 392 LEU A CB  
415  C CG  . LEU A 53  ? 0.5696 0.5600 0.4669 0.0265  0.0160  -0.0750 392 LEU A CG  
416  C CD1 . LEU A 53  ? 0.5577 0.5599 0.4188 0.0295  0.0231  -0.0761 392 LEU A CD1 
417  C CD2 . LEU A 53  ? 0.5163 0.5118 0.4190 0.0279  0.0302  -0.0658 392 LEU A CD2 
418  N N   . LYS A 54  ? 0.5056 0.4636 0.4874 -0.0172 -0.0331 -0.0366 393 LYS A N   
419  C CA  . LYS A 54  ? 0.4825 0.4449 0.4787 -0.0356 -0.0383 -0.0156 393 LYS A CA  
420  C C   . LYS A 54  ? 0.5021 0.4539 0.5158 -0.0446 -0.0412 0.0021  393 LYS A C   
421  O O   . LYS A 54  ? 0.5084 0.4683 0.5290 -0.0613 -0.0419 0.0223  393 LYS A O   
422  C CB  . LYS A 54  ? 0.5140 0.4688 0.5267 -0.0446 -0.0562 -0.0216 393 LYS A CB  
423  C CG  . LYS A 54  ? 0.5189 0.4454 0.5571 -0.0452 -0.0754 -0.0303 393 LYS A CG  
424  C CD  . LYS A 54  ? 0.5014 0.4209 0.5569 -0.0551 -0.0936 -0.0366 393 LYS A CD  
425  C CE  . LYS A 54  ? 0.5660 0.4541 0.6531 -0.0605 -0.1160 -0.0392 393 LYS A CE  
426  N NZ  . LYS A 54  ? 0.6436 0.5248 0.7512 -0.0738 -0.1346 -0.0422 393 LYS A NZ  
427  N N   . ARG A 55  ? 0.4662 0.4024 0.4874 -0.0343 -0.0434 -0.0056 394 ARG A N   
428  C CA  . ARG A 55  ? 0.4839 0.4097 0.5200 -0.0411 -0.0475 0.0116  394 ARG A CA  
429  C C   . ARG A 55  ? 0.4631 0.4098 0.4828 -0.0443 -0.0299 0.0284  394 ARG A C   
430  O O   . ARG A 55  ? 0.4219 0.3668 0.4488 -0.0558 -0.0329 0.0484  394 ARG A O   
431  C CB  . ARG A 55  ? 0.4662 0.3736 0.5165 -0.0260 -0.0539 -0.0045 394 ARG A CB  
432  C CG  . ARG A 55  ? 0.4740 0.3973 0.5075 -0.0100 -0.0342 -0.0158 394 ARG A CG  
433  C CD  . ARG A 55  ? 0.4472 0.3597 0.4956 0.0070  -0.0391 -0.0412 394 ARG A CD  
434  N NE  . ARG A 55  ? 0.4518 0.3800 0.4919 0.0183  -0.0212 -0.0469 394 ARG A NE  
435  C CZ  . ARG A 55  ? 0.4992 0.4475 0.5150 0.0270  -0.0026 -0.0594 394 ARG A CZ  
436  N NH1 . ARG A 55  ? 0.5444 0.4990 0.5392 0.0274  -0.0001 -0.0680 394 ARG A NH1 
437  N NH2 . ARG A 55  ? 0.4358 0.3980 0.4482 0.0345  0.0130  -0.0624 394 ARG A NH2 
438  N N   . ILE A 56  ? 0.4765 0.4420 0.4737 -0.0347 -0.0129 0.0208  395 ILE A N   
439  C CA  . ILE A 56  ? 0.4268 0.4104 0.4101 -0.0350 0.0030  0.0327  395 ILE A CA  
440  C C   . ILE A 56  ? 0.4074 0.4097 0.3859 -0.0488 0.0055  0.0464  395 ILE A C   
441  O O   . ILE A 56  ? 0.4567 0.4713 0.4246 -0.0467 0.0092  0.0396  395 ILE A O   
442  C CB  . ILE A 56  ? 0.3522 0.3455 0.3155 -0.0200 0.0181  0.0198  395 ILE A CB  
443  C CG1 . ILE A 56  ? 0.4583 0.4397 0.4284 -0.0070 0.0176  0.0033  395 ILE A CG1 
444  C CG2 . ILE A 56  ? 0.4124 0.4215 0.3650 -0.0210 0.0321  0.0320  395 ILE A CG2 
445  C CD1 . ILE A 56  ? 0.4572 0.4497 0.4057 0.0051  0.0326  -0.0100 395 ILE A CD1 
446  N N   . ASN A 57  ? 0.4086 0.4148 0.3949 -0.0628 0.0031  0.0650  396 ASN A N   
447  C CA  . ASN A 57  ? 0.4113 0.4422 0.3936 -0.0762 0.0086  0.0767  396 ASN A CA  
448  C C   . ASN A 57  ? 0.3870 0.4287 0.3649 -0.0814 0.0157  0.0915  396 ASN A C   
449  O O   . ASN A 57  ? 0.4205 0.4469 0.4055 -0.0852 0.0083  0.1013  396 ASN A O   
450  C CB  . ASN A 57  ? 0.4041 0.4345 0.4012 -0.0944 -0.0037 0.0848  396 ASN A CB  
451  C CG  . ASN A 57  ? 0.5104 0.5110 0.5241 -0.1008 -0.0208 0.0917  396 ASN A CG  
452  O OD1 . ASN A 57  ? 0.8187 0.8142 0.8360 -0.1113 -0.0249 0.1094  396 ASN A OD1 
453  N ND2 . ASN A 57  ? 0.5090 0.4890 0.5333 -0.0943 -0.0327 0.0771  396 ASN A ND2 
454  N N   . HIS A 58  ? 0.3051 0.3727 0.2720 -0.0808 0.0282  0.0918  397 HIS A N   
455  C CA  . HIS A 58  ? 0.2660 0.3462 0.2268 -0.0831 0.0358  0.1016  397 HIS A CA  
456  C C   . HIS A 58  ? 0.2510 0.3636 0.2055 -0.0860 0.0461  0.0995  397 HIS A C   
457  O O   . HIS A 58  ? 0.2462 0.3670 0.1990 -0.0788 0.0490  0.0877  397 HIS A O   
458  C CB  . HIS A 58  ? 0.3125 0.3805 0.2683 -0.0671 0.0411  0.0950  397 HIS A CB  
459  C CG  . HIS A 58  ? 0.2522 0.3291 0.2047 -0.0693 0.0457  0.1044  397 HIS A CG  
460  N ND1 . HIS A 58  ? 0.2372 0.3278 0.1842 -0.0620 0.0534  0.0949  397 HIS A ND1 
461  C CD2 . HIS A 58  ? 0.2631 0.3290 0.2207 -0.0730 0.0389  0.1148  397 HIS A CD2 
462  C CE1 . HIS A 58  ? 0.3038 0.3919 0.2517 -0.0610 0.0518  0.0972  397 HIS A CE1 
463  N NE2 . HIS A 58  ? 0.3158 0.3924 0.2684 -0.0686 0.0441  0.1113  397 HIS A NE2 
464  N N   . ALA A 59  ? 0.2505 0.3708 0.2061 -0.0876 0.0462  0.1006  398 ALA A N   
465  C CA  . ALA A 59  ? 0.2419 0.3846 0.1984 -0.0846 0.0508  0.0901  398 ALA A CA  
466  C C   . ALA A 59  ? 0.2263 0.3692 0.1788 -0.0680 0.0569  0.0764  398 ALA A C   
467  O O   . ALA A 59  ? 0.2199 0.3811 0.1755 -0.0654 0.0591  0.0676  398 ALA A O   
468  C CB  . ALA A 59  ? 0.2536 0.4033 0.2092 -0.0889 0.0494  0.0932  398 ALA A CB  
469  N N   . ASN A 60  ? 0.2315 0.3549 0.1782 -0.0577 0.0590  0.0752  399 ASN A N   
470  C CA  . ASN A 60  ? 0.2324 0.3510 0.1746 -0.0439 0.0634  0.0646  399 ASN A CA  
471  C C   . ASN A 60  ? 0.2623 0.3710 0.1962 -0.0378 0.0654  0.0628  399 ASN A C   
472  O O   . ASN A 60  ? 0.2414 0.3388 0.1689 -0.0278 0.0684  0.0571  399 ASN A O   
473  C CB  . ASN A 60  ? 0.2428 0.3497 0.1843 -0.0382 0.0649  0.0633  399 ASN A CB  
474  C CG  . ASN A 60  ? 0.2446 0.3640 0.1903 -0.0435 0.0628  0.0645  399 ASN A CG  
475  O OD1 . ASN A 60  ? 0.2553 0.3700 0.2007 -0.0478 0.0604  0.0715  399 ASN A OD1 
476  N ND2 . ASN A 60  ? 0.2247 0.3630 0.1737 -0.0434 0.0634  0.0578  399 ASN A ND2 
477  N N   . ILE A 61  ? 0.2873 0.4006 0.2200 -0.0455 0.0631  0.0681  400 ILE A N   
478  C CA  . ILE A 61  ? 0.2858 0.3858 0.2107 -0.0373 0.0611  0.0604  400 ILE A CA  
479  C C   . ILE A 61  ? 0.2806 0.3918 0.2094 -0.0406 0.0550  0.0547  400 ILE A C   
480  O O   . ILE A 61  ? 0.2602 0.3838 0.2012 -0.0533 0.0510  0.0592  400 ILE A O   
481  C CB  . ILE A 61  ? 0.2750 0.3526 0.2034 -0.0369 0.0560  0.0601  400 ILE A CB  
482  C CG1 . ILE A 61  ? 0.2863 0.3551 0.2137 -0.0312 0.0620  0.0627  400 ILE A CG1 
483  C CG2 . ILE A 61  ? 0.3102 0.3758 0.2310 -0.0288 0.0520  0.0480  400 ILE A CG2 
484  C CD1 . ILE A 61  ? 0.2676 0.3168 0.2034 -0.0288 0.0562  0.0594  400 ILE A CD1 
485  N N   . ILE A 62  ? 0.2731 0.3808 0.1917 -0.0303 0.0535  0.0456  401 ILE A N   
486  C CA  . ILE A 62  ? 0.3431 0.4625 0.2671 -0.0315 0.0460  0.0386  401 ILE A CA  
487  C C   . ILE A 62  ? 0.3799 0.4927 0.3141 -0.0405 0.0374  0.0378  401 ILE A C   
488  O O   . ILE A 62  ? 0.4101 0.5014 0.3381 -0.0363 0.0333  0.0337  401 ILE A O   
489  C CB  . ILE A 62  ? 0.3401 0.4512 0.2481 -0.0183 0.0428  0.0305  401 ILE A CB  
490  C CG1 . ILE A 62  ? 0.3141 0.4428 0.2315 -0.0178 0.0343  0.0230  401 ILE A CG1 
491  C CG2 . ILE A 62  ? 0.3261 0.4148 0.2196 -0.0132 0.0394  0.0257  401 ILE A CG2 
492  C CD1 . ILE A 62  ? 0.2652 0.4209 0.1981 -0.0207 0.0383  0.0231  401 ILE A CD1 
493  N N   . ARG A 63  ? 0.3329 0.4653 0.2843 -0.0537 0.0345  0.0409  402 ARG A N   
494  C CA  . ARG A 63  ? 0.3456 0.4714 0.3105 -0.0662 0.0255  0.0436  402 ARG A CA  
495  C C   . ARG A 63  ? 0.3697 0.4918 0.3375 -0.0623 0.0147  0.0309  402 ARG A C   
496  O O   . ARG A 63  ? 0.3744 0.5128 0.3423 -0.0568 0.0134  0.0228  402 ARG A O   
497  C CB  . ARG A 63  ? 0.3404 0.4915 0.3218 -0.0853 0.0277  0.0542  402 ARG A CB  
498  C CG  . ARG A 63  ? 0.5240 0.6647 0.5199 -0.1022 0.0179  0.0627  402 ARG A CG  
499  C CD  . ARG A 63  ? 0.4637 0.6331 0.4721 -0.1240 0.0219  0.0759  402 ARG A CD  
500  N NE  . ARG A 63  ? 0.5566 0.7452 0.5838 -0.1361 0.0162  0.0717  402 ARG A NE  
501  C CZ  . ARG A 63  ? 0.7136 0.8883 0.7554 -0.1503 0.0042  0.0773  402 ARG A CZ  
502  N NH1 . ARG A 63  ? 0.7974 0.9372 0.8377 -0.1532 -0.0048 0.0868  402 ARG A NH1 
503  N NH2 . ARG A 63  ? 0.6053 0.8014 0.6666 -0.1616 -0.0002 0.0724  402 ARG A NH2 
504  N N   . LEU A 64  ? 0.4000 0.5002 0.3717 -0.0645 0.0049  0.0280  403 LEU A N   
505  C CA  . LEU A 64  ? 0.3773 0.4715 0.3517 -0.0611 -0.0075 0.0145  403 LEU A CA  
506  C C   . LEU A 64  ? 0.4265 0.5320 0.4275 -0.0797 -0.0164 0.0183  403 LEU A C   
507  O O   . LEU A 64  ? 0.5352 0.6276 0.5487 -0.0920 -0.0213 0.0272  403 LEU A O   
508  C CB  . LEU A 64  ? 0.4077 0.4726 0.3710 -0.0509 -0.0133 0.0050  403 LEU A CB  
509  C CG  . LEU A 64  ? 0.4540 0.5106 0.4190 -0.0474 -0.0280 -0.0111 403 LEU A CG  
510  C CD1 . LEU A 64  ? 0.4852 0.5544 0.4343 -0.0369 -0.0291 -0.0199 403 LEU A CD1 
511  C CD2 . LEU A 64  ? 0.5281 0.5588 0.4849 -0.0380 -0.0329 -0.0227 403 LEU A CD2 
512  N N   . SER A 65  ? 0.4048 0.5349 0.4163 -0.0824 -0.0194 0.0119  404 SER A N   
513  C CA  . SER A 65  ? 0.3843 0.5294 0.4234 -0.1016 -0.0271 0.0145  404 SER A CA  
514  C C   . SER A 65  ? 0.4705 0.5905 0.5177 -0.1026 -0.0441 0.0055  404 SER A C   
515  O O   . SER A 65  ? 0.5720 0.6828 0.6381 -0.1194 -0.0517 0.0138  404 SER A O   
516  C CB  . SER A 65  ? 0.3837 0.5656 0.4359 -0.1025 -0.0259 0.0066  404 SER A CB  
517  O OG  . SER A 65  ? 0.4530 0.6608 0.5028 -0.1028 -0.0112 0.0127  404 SER A OG  
518  N N   . GLY A 66  ? 0.4630 0.5711 0.4953 -0.0852 -0.0515 -0.0114 405 GLY A N   
519  C CA  . GLY A 66  ? 0.5523 0.6385 0.5906 -0.0838 -0.0683 -0.0243 405 GLY A CA  
520  C C   . GLY A 66  ? 0.5307 0.6093 0.5438 -0.0632 -0.0734 -0.0422 405 GLY A C   
521  O O   . GLY A 66  ? 0.5126 0.5973 0.5021 -0.0506 -0.0638 -0.0416 405 GLY A O   
522  N N   . PHE A 67  ? 0.5246 0.5894 0.5423 -0.0608 -0.0900 -0.0579 406 PHE A N   
523  C CA  . PHE A 67  ? 0.5857 0.6434 0.5764 -0.0428 -0.0971 -0.0755 406 PHE A CA  
524  C C   . PHE A 67  ? 0.6032 0.6630 0.6109 -0.0460 -0.1176 -0.0912 406 PHE A C   
525  O O   . PHE A 67  ? 0.6172 0.6791 0.6588 -0.0624 -0.1265 -0.0892 406 PHE A O   
526  C CB  . PHE A 67  ? 0.6280 0.6607 0.5935 -0.0301 -0.0938 -0.0837 406 PHE A CB  
527  C CG  . PHE A 67  ? 0.6641 0.6756 0.6489 -0.0347 -0.1065 -0.0939 406 PHE A CG  
528  C CD1 . PHE A 67  ? 0.7120 0.7128 0.7202 -0.0466 -0.1043 -0.0811 406 PHE A CD1 
529  C CD2 . PHE A 67  ? 0.6425 0.6431 0.6218 -0.0264 -0.1225 -0.1168 406 PHE A CD2 
530  C CE1 . PHE A 67  ? 0.8311 0.8084 0.8601 -0.0502 -0.1193 -0.0905 406 PHE A CE1 
531  C CE2 . PHE A 67  ? 0.6968 0.6762 0.6972 -0.0294 -0.1363 -0.1289 406 PHE A CE2 
532  C CZ  . PHE A 67  ? 0.7592 0.7256 0.7858 -0.0411 -0.1353 -0.1155 406 PHE A CZ  
533  N N   . CYS A 68  ? 0.5915 0.6507 0.5745 -0.0311 -0.1260 -0.1059 407 CYS A N   
534  C CA  . CYS A 68  ? 0.5752 0.6367 0.5695 -0.0310 -0.1473 -0.1234 407 CYS A CA  
535  C C   . CYS A 68  ? 0.6296 0.6766 0.5838 -0.0126 -0.1548 -0.1407 407 CYS A C   
536  O O   . CYS A 68  ? 0.5945 0.6436 0.5138 -0.0007 -0.1464 -0.1365 407 CYS A O   
537  C CB  . CYS A 68  ? 0.5679 0.6584 0.5805 -0.0351 -0.1522 -0.1210 407 CYS A CB  
538  S SG  . CYS A 68  ? 0.6470 0.7428 0.6699 -0.0314 -0.1803 -0.1440 407 CYS A SG  
539  N N   . VAL A 69  ? 0.6715 0.7040 0.6304 -0.0112 -0.1708 -0.1600 408 VAL A N   
540  C CA  . VAL A 69  ? 0.6400 0.6624 0.5609 0.0050  -0.1797 -0.1802 408 VAL A CA  
541  C C   . VAL A 69  ? 0.6524 0.6836 0.5816 0.0058  -0.2032 -0.1949 408 VAL A C   
542  O O   . VAL A 69  ? 0.5897 0.6197 0.5565 -0.0046 -0.2186 -0.2041 408 VAL A O   
543  C CB  . VAL A 69  ? 0.5851 0.5865 0.5042 0.0089  -0.1816 -0.1965 408 VAL A CB  
544  C CG1 . VAL A 69  ? 0.6173 0.6145 0.4884 0.0262  -0.1835 -0.2158 408 VAL A CG1 
545  C CG2 . VAL A 69  ? 0.6661 0.6597 0.5938 0.0045  -0.1623 -0.1810 408 VAL A CG2 
546  N N   . TYR A 70  ? 0.6679 0.7069 0.5635 0.0173  -0.2076 -0.1963 409 TYR A N   
547  C CA  . TYR A 70  ? 0.6476 0.6962 0.5494 0.0198  -0.2315 -0.2097 409 TYR A CA  
548  C C   . TYR A 70  ? 0.7220 0.7640 0.5686 0.0363  -0.2400 -0.2206 409 TYR A C   
549  O O   . TYR A 70  ? 0.6961 0.7394 0.5074 0.0438  -0.2299 -0.2067 409 TYR A O   
550  C CB  . TYR A 70  ? 0.6786 0.7505 0.6079 0.0138  -0.2323 -0.1960 409 TYR A CB  
551  C CG  . TYR A 70  ? 0.6382 0.7233 0.5868 0.0146  -0.2584 -0.2108 409 TYR A CG  
552  C CD1 . TYR A 70  ? 0.6543 0.7456 0.6500 0.0012  -0.2718 -0.2218 409 TYR A CD1 
553  C CD2 . TYR A 70  ? 0.6775 0.7681 0.5988 0.0279  -0.2713 -0.2130 409 TYR A CD2 
554  C CE1 . TYR A 70  ? 0.6786 0.7841 0.6956 0.0015  -0.2962 -0.2366 409 TYR A CE1 
555  C CE2 . TYR A 70  ? 0.6772 0.7804 0.6183 0.0296  -0.2971 -0.2274 409 TYR A CE2 
556  C CZ  . TYR A 70  ? 0.6947 0.8061 0.6845 0.0163  -0.3070 -0.2386 409 TYR A CZ  
557  O OH  . TYR A 70  ? 0.6971 0.8197 0.7093 0.0168  -0.3235 -0.2466 409 TYR A OH  
558  N N   . LYS A 71  ? 0.7980 0.8327 0.6367 0.0411  -0.2592 -0.2451 410 LYS A N   
559  C CA  . LYS A 71  ? 0.8074 0.8378 0.5966 0.0537  -0.2647 -0.2520 410 LYS A CA  
560  C C   . LYS A 71  ? 0.7484 0.7720 0.4866 0.0610  -0.2430 -0.2429 410 LYS A C   
561  O O   . LYS A 71  ? 0.7437 0.7687 0.4444 0.0660  -0.2378 -0.2279 410 LYS A O   
562  C CB  . LYS A 71  ? 0.7298 0.7709 0.5175 0.0564  -0.2777 -0.2427 410 LYS A CB  
563  C CG  . LYS A 71  ? 0.7278 0.7790 0.5661 0.0494  -0.2981 -0.2536 410 LYS A CG  
564  C CD  . LYS A 71  ? 0.7531 0.8157 0.5924 0.0540  -0.3115 -0.2468 410 LYS A CD  
565  C CE  . LYS A 71  ? 0.7356 0.8109 0.6278 0.0464  -0.3297 -0.2588 410 LYS A CE  
566  N NZ  . LYS A 71  ? 0.8408 0.9293 0.7406 0.0518  -0.3433 -0.2541 410 LYS A NZ  
567  N N   . GLY A 72  ? 0.7266 0.7426 0.4671 0.0604  -0.2305 -0.2517 411 GLY A N   
568  C CA  . GLY A 72  ? 0.8191 0.8318 0.5172 0.0664  -0.2084 -0.2470 411 GLY A CA  
569  C C   . GLY A 72  ? 0.8299 0.8455 0.5163 0.0648  -0.1886 -0.2221 411 GLY A C   
570  O O   . GLY A 72  ? 0.8369 0.8521 0.4856 0.0687  -0.1703 -0.2157 411 GLY A O   
571  N N   . ASN A 73  ? 0.8776 0.8979 0.6019 0.0565  -0.1869 -0.2037 412 ASN A N   
572  C CA  . ASN A 73  ? 0.7634 0.7865 0.4855 0.0536  -0.1661 -0.1779 412 ASN A CA  
573  C C   . ASN A 73  ? 0.7269 0.7523 0.5006 0.0422  -0.1567 -0.1684 412 ASN A C   
574  O O   . ASN A 73  ? 0.7179 0.7466 0.5320 0.0344  -0.1694 -0.1753 412 ASN A O   
575  C CB  . ASN A 73  ? 0.8370 0.8662 0.5448 0.0566  -0.1740 -0.1626 412 ASN A CB  
576  C CG  . ASN A 73  ? 0.9069 0.9306 0.5541 0.0659  -0.1773 -0.1614 412 ASN A CG  
577  O OD1 . ASN A 73  ? 0.8564 0.8766 0.4740 0.0668  -0.1602 -0.1456 412 ASN A OD1 
578  N ND2 . ASN A 73  ? 0.8885 0.9111 0.5238 0.0689  -0.1955 -0.1732 412 ASN A ND2 
579  N N   . THR A 74  ? 0.7518 0.7763 0.5230 0.0400  -0.1346 -0.1517 413 THR A N   
580  C CA  . THR A 74  ? 0.7775 0.8044 0.5900 0.0290  -0.1240 -0.1396 413 THR A CA  
581  C C   . THR A 74  ? 0.7421 0.7814 0.5618 0.0259  -0.1161 -0.1188 413 THR A C   
582  O O   . THR A 74  ? 0.7353 0.7736 0.5246 0.0322  -0.1064 -0.1081 413 THR A O   
583  C CB  . THR A 74  ? 0.7857 0.8028 0.5945 0.0295  -0.1066 -0.1388 413 THR A CB  
584  O OG1 . THR A 74  ? 0.8540 0.8605 0.6644 0.0331  -0.1158 -0.1619 413 THR A OG1 
585  C CG2 . THR A 74  ? 0.8523 0.8710 0.6988 0.0177  -0.0968 -0.1229 413 THR A CG2 
586  N N   . TYR A 75  ? 0.6402 0.6923 0.5009 0.0155  -0.1205 -0.1140 414 TYR A N   
587  C CA  . TYR A 75  ? 0.6065 0.6750 0.4812 0.0122  -0.1130 -0.0983 414 TYR A CA  
588  C C   . TYR A 75  ? 0.5455 0.6182 0.4470 0.0000  -0.0971 -0.0858 414 TYR A C   
589  O O   . TYR A 75  ? 0.5884 0.6647 0.5224 -0.0124 -0.1015 -0.0877 414 TYR A O   
590  C CB  . TYR A 75  ? 0.5891 0.6766 0.4902 0.0097  -0.1298 -0.1044 414 TYR A CB  
591  C CG  . TYR A 75  ? 0.5627 0.6453 0.4402 0.0210  -0.1502 -0.1176 414 TYR A CG  
592  C CD1 . TYR A 75  ? 0.5749 0.6573 0.4258 0.0324  -0.1549 -0.1123 414 TYR A CD1 
593  C CD2 . TYR A 75  ? 0.5992 0.6761 0.4814 0.0201  -0.1668 -0.1354 414 TYR A CD2 
594  C CE1 . TYR A 75  ? 0.5790 0.6557 0.4053 0.0423  -0.1758 -0.1225 414 TYR A CE1 
595  C CE2 . TYR A 75  ? 0.6149 0.6882 0.4733 0.0305  -0.1869 -0.1480 414 TYR A CE2 
596  C CZ  . TYR A 75  ? 0.5801 0.6534 0.4091 0.0414  -0.1914 -0.1407 414 TYR A CZ  
597  O OH  . TYR A 75  ? 0.5952 0.6637 0.3976 0.0512  -0.2134 -0.1514 414 TYR A OH  
598  N N   . LEU A 76  ? 0.5398 0.6112 0.4274 0.0026  -0.0800 -0.0723 415 LEU A N   
599  C CA  . LEU A 76  ? 0.4704 0.5458 0.3785 -0.0078 -0.0654 -0.0595 415 LEU A CA  
600  C C   . LEU A 76  ? 0.4579 0.5569 0.3839 -0.0124 -0.0596 -0.0494 415 LEU A C   
601  O O   . LEU A 76  ? 0.5028 0.6074 0.4151 -0.0029 -0.0601 -0.0482 415 LEU A O   
602  C CB  . LEU A 76  ? 0.4491 0.5092 0.3337 -0.0022 -0.0503 -0.0534 415 LEU A CB  
603  C CG  . LEU A 76  ? 0.5027 0.5437 0.3758 0.0019  -0.0529 -0.0656 415 LEU A CG  
604  C CD1 . LEU A 76  ? 0.4922 0.5267 0.3266 0.0149  -0.0562 -0.0762 415 LEU A CD1 
605  C CD2 . LEU A 76  ? 0.5028 0.5351 0.3794 0.0000  -0.0387 -0.0583 415 LEU A CD2 
606  N N   . VAL A 77  ? 0.4061 0.5192 0.3626 -0.0273 -0.0548 -0.0424 416 VAL A N   
607  C CA  . VAL A 77  ? 0.4107 0.5527 0.3878 -0.0336 -0.0482 -0.0359 416 VAL A CA  
608  C C   . VAL A 77  ? 0.3521 0.4946 0.3290 -0.0402 -0.0313 -0.0213 416 VAL A C   
609  O O   . VAL A 77  ? 0.3897 0.5261 0.3778 -0.0528 -0.0287 -0.0141 416 VAL A O   
610  C CB  . VAL A 77  ? 0.4203 0.5862 0.4334 -0.0482 -0.0564 -0.0403 416 VAL A CB  
611  C CG1 . VAL A 77  ? 0.4044 0.6070 0.4382 -0.0517 -0.0497 -0.0390 416 VAL A CG1 
612  C CG2 . VAL A 77  ? 0.4072 0.5676 0.4216 -0.0424 -0.0757 -0.0559 416 VAL A CG2 
613  N N   . TYR A 78  ? 0.3643 0.5125 0.3291 -0.0318 -0.0218 -0.0167 417 TYR A N   
614  C CA  . TYR A 78  ? 0.3322 0.4835 0.2962 -0.0365 -0.0068 -0.0044 417 TYR A CA  
615  C C   . TYR A 78  ? 0.3363 0.5224 0.3215 -0.0430 -0.0010 -0.0032 417 TYR A C   
616  O O   . TYR A 78  ? 0.3735 0.5804 0.3729 -0.0402 -0.0080 -0.0131 417 TYR A O   
617  C CB  . TYR A 78  ? 0.3348 0.4675 0.2710 -0.0229 0.0002  -0.0012 417 TYR A CB  
618  C CG  . TYR A 78  ? 0.3745 0.4789 0.2884 -0.0163 -0.0020 -0.0041 417 TYR A CG  
619  C CD1 . TYR A 78  ? 0.3876 0.4821 0.2851 -0.0072 -0.0130 -0.0142 417 TYR A CD1 
620  C CD2 . TYR A 78  ? 0.4072 0.4970 0.3163 -0.0186 0.0064  0.0018  417 TYR A CD2 
621  C CE1 . TYR A 78  ? 0.3828 0.4564 0.2583 -0.0013 -0.0136 -0.0194 417 TYR A CE1 
622  C CE2 . TYR A 78  ? 0.4191 0.4881 0.3108 -0.0117 0.0054  -0.0045 417 TYR A CE2 
623  C CZ  . TYR A 78  ? 0.3885 0.4509 0.2625 -0.0034 -0.0036 -0.0156 417 TYR A CZ  
624  O OH  . TYR A 78  ? 0.5643 0.6109 0.4196 0.0033  -0.0032 -0.0243 417 TYR A OH  
625  N N   . GLU A 79  ? 0.2829 0.4770 0.2707 -0.0512 0.0114  0.0074  418 GLU A N   
626  C CA  . GLU A 79  ? 0.2538 0.4832 0.2573 -0.0557 0.0191  0.0065  418 GLU A CA  
627  C C   . GLU A 79  ? 0.2936 0.5248 0.2895 -0.0378 0.0182  -0.0017 418 GLU A C   
628  O O   . GLU A 79  ? 0.3561 0.5613 0.3298 -0.0268 0.0198  0.0021  418 GLU A O   
629  C CB  . GLU A 79  ? 0.2338 0.4691 0.2361 -0.0676 0.0314  0.0199  418 GLU A CB  
630  C CG  . GLU A 79  ? 0.2973 0.5058 0.2775 -0.0581 0.0371  0.0270  418 GLU A CG  
631  C CD  . GLU A 79  ? 0.3461 0.5671 0.3267 -0.0676 0.0479  0.0377  418 GLU A CD  
632  O OE1 . GLU A 79  ? 0.2559 0.5115 0.2485 -0.0740 0.0536  0.0348  418 GLU A OE1 
633  O OE2 . GLU A 79  ? 0.3296 0.5277 0.2988 -0.0683 0.0502  0.0476  418 GLU A OE2 
634  N N   . PHE A 80  ? 0.3326 0.5946 0.3490 -0.0352 0.0148  -0.0135 419 PHE A N   
635  C CA  . PHE A 80  ? 0.3255 0.5878 0.3395 -0.0177 0.0101  -0.0222 419 PHE A CA  
636  C C   . PHE A 80  ? 0.2890 0.5575 0.2995 -0.0161 0.0221  -0.0182 419 PHE A C   
637  O O   . PHE A 80  ? 0.2614 0.5582 0.2846 -0.0280 0.0329  -0.0170 419 PHE A O   
638  C CB  . PHE A 80  ? 0.2971 0.5927 0.3400 -0.0140 0.0010  -0.0390 419 PHE A CB  
639  C CG  . PHE A 80  ? 0.3068 0.6014 0.3521 0.0048  -0.0077 -0.0490 419 PHE A CG  
640  C CD1 . PHE A 80  ? 0.3149 0.5753 0.3398 0.0190  -0.0221 -0.0476 419 PHE A CD1 
641  C CD2 . PHE A 80  ? 0.2491 0.5766 0.3169 0.0080  -0.0026 -0.0601 419 PHE A CD2 
642  C CE1 . PHE A 80  ? 0.3245 0.5794 0.3520 0.0354  -0.0332 -0.0543 419 PHE A CE1 
643  C CE2 . PHE A 80  ? 0.3067 0.6300 0.3804 0.0262  -0.0137 -0.0705 419 PHE A CE2 
644  C CZ  . PHE A 80  ? 0.3524 0.6372 0.4064 0.0396  -0.0299 -0.0662 419 PHE A CZ  
645  N N   . ALA A 81  ? 0.2657 0.5082 0.2579 -0.0027 0.0199  -0.0155 420 ALA A N   
646  C CA  . ALA A 81  ? 0.2399 0.4839 0.2292 0.0006  0.0287  -0.0129 420 ALA A CA  
647  C C   . ALA A 81  ? 0.2998 0.5524 0.3020 0.0155  0.0192  -0.0261 420 ALA A C   
648  O O   . ALA A 81  ? 0.3083 0.5326 0.2968 0.0276  0.0089  -0.0240 420 ALA A O   
649  C CB  . ALA A 81  ? 0.2960 0.5037 0.2583 0.0025  0.0334  0.0009  420 ALA A CB  
650  N N   . GLU A 82  ? 0.3298 0.6223 0.3588 0.0144  0.0218  -0.0400 421 GLU A N   
651  C CA  . GLU A 82  ? 0.2547 0.5568 0.3008 0.0299  0.0125  -0.0555 421 GLU A CA  
652  C C   . GLU A 82  ? 0.2658 0.5497 0.3005 0.0354  0.0170  -0.0501 421 GLU A C   
653  O O   . GLU A 82  ? 0.3250 0.6086 0.3481 0.0253  0.0309  -0.0402 421 GLU A O   
654  C CB  . GLU A 82  ? 0.2592 0.6150 0.3397 0.0273  0.0160  -0.0755 421 GLU A CB  
655  C CG  . GLU A 82  ? 0.3477 0.7336 0.4305 0.0146  0.0343  -0.0750 421 GLU A CG  
656  C CD  . GLU A 82  ? 0.4291 0.8724 0.5451 0.0140  0.0385  -0.0983 421 GLU A CD  
657  O OE1 . GLU A 82  ? 0.4038 0.8703 0.5387 0.0099  0.0347  -0.1072 421 GLU A OE1 
658  O OE2 . GLU A 82  ? 0.4842 0.9278 0.5977 0.0161  0.0412  -0.1050 421 GLU A OE2 
659  N N   . ASN A 83  ? 0.2748 0.5419 0.3140 0.0512  0.0033  -0.0565 422 ASN A N   
660  C CA  . ASN A 83  ? 0.3393 0.5839 0.3707 0.0577  0.0030  -0.0520 422 ASN A CA  
661  C C   . ASN A 83  ? 0.3123 0.5104 0.3110 0.0564  0.0018  -0.0305 422 ASN A C   
662  O O   . ASN A 83  ? 0.3424 0.5194 0.3317 0.0581  0.0040  -0.0226 422 ASN A O   
663  C CB  . ASN A 83  ? 0.2534 0.5209 0.2889 0.0496  0.0194  -0.0541 422 ASN A CB  
664  C CG  . ASN A 83  ? 0.2377 0.5533 0.3043 0.0528  0.0207  -0.0781 422 ASN A CG  
665  O OD1 . ASN A 83  ? 0.2790 0.6000 0.3676 0.0677  0.0074  -0.0956 422 ASN A OD1 
666  N ND2 . ASN A 83  ? 0.2930 0.6446 0.3621 0.0384  0.0363  -0.0794 422 ASN A ND2 
667  N N   . ASN A 84  ? 0.2778 0.4622 0.2598 0.0526  -0.0008 -0.0221 423 ASN A N   
668  C CA  . ASN A 84  ? 0.3262 0.4707 0.2782 0.0545  -0.0065 -0.0065 423 ASN A CA  
669  C C   . ASN A 84  ? 0.3357 0.4636 0.2681 0.0464  0.0090  0.0081  423 ASN A C   
670  O O   . ASN A 84  ? 0.3281 0.4706 0.2623 0.0367  0.0228  0.0095  423 ASN A O   
671  C CB  . ASN A 84  ? 0.3710 0.4956 0.3252 0.0678  -0.0263 -0.0083 423 ASN A CB  
672  C CG  . ASN A 84  ? 0.3971 0.5473 0.3835 0.0779  -0.0414 -0.0286 423 ASN A CG  
673  O OD1 . ASN A 84  ? 0.4999 0.6583 0.4890 0.0788  -0.0495 -0.0337 423 ASN A OD1 
674  N ND2 . ASN A 84  ? 0.3238 0.4891 0.3372 0.0859  -0.0453 -0.0424 423 ASN A ND2 
675  N N   . SER A 85  ? 0.3133 0.4113 0.2282 0.0494  0.0061  0.0194  424 SER A N   
676  C CA  . SER A 85  ? 0.3162 0.3978 0.2126 0.0422  0.0197  0.0331  424 SER A CA  
677  C C   . SER A 85  ? 0.3243 0.4021 0.2320 0.0440  0.0215  0.0340  424 SER A C   
678  O O   . SER A 85  ? 0.3502 0.4263 0.2729 0.0525  0.0085  0.0272  424 SER A O   
679  C CB  . SER A 85  ? 0.3302 0.3829 0.1955 0.0415  0.0167  0.0463  424 SER A CB  
680  O OG  . SER A 85  ? 0.3623 0.3928 0.2217 0.0460  0.0062  0.0541  424 SER A OG  
681  N N   . LEU A 86  ? 0.3004 0.3768 0.2033 0.0366  0.0360  0.0410  425 LEU A N   
682  C CA  . LEU A 86  ? 0.3050 0.3774 0.2187 0.0373  0.0378  0.0419  425 LEU A CA  
683  C C   . LEU A 86  ? 0.3122 0.3558 0.2189 0.0414  0.0262  0.0505  425 LEU A C   
684  O O   . LEU A 86  ? 0.3406 0.3807 0.2648 0.0469  0.0171  0.0452  425 LEU A O   
685  C CB  . LEU A 86  ? 0.2960 0.3689 0.2039 0.0285  0.0538  0.0496  425 LEU A CB  
686  C CG  . LEU A 86  ? 0.2924 0.3626 0.2120 0.0278  0.0565  0.0504  425 LEU A CG  
687  C CD1 . LEU A 86  ? 0.2293 0.3240 0.1716 0.0321  0.0526  0.0348  425 LEU A CD1 
688  C CD2 . LEU A 86  ? 0.2312 0.3011 0.1450 0.0196  0.0708  0.0582  425 LEU A CD2 
689  N N   . ASP A 87  ? 0.3187 0.3412 0.1992 0.0383  0.0254  0.0639  426 ASP A N   
690  C CA  . ASP A 87  ? 0.3435 0.3369 0.2127 0.0394  0.0134  0.0762  426 ASP A CA  
691  C C   . ASP A 87  ? 0.4091 0.3981 0.2966 0.0510  -0.0090 0.0670  426 ASP A C   
692  O O   . ASP A 87  ? 0.4716 0.4425 0.3695 0.0538  -0.0204 0.0704  426 ASP A O   
693  C CB  . ASP A 87  ? 0.3603 0.3379 0.1946 0.0342  0.0150  0.0899  426 ASP A CB  
694  C CG  . ASP A 87  ? 0.4286 0.3756 0.2448 0.0310  0.0049  0.1077  426 ASP A CG  
695  O OD1 . ASP A 87  ? 0.5653 0.4973 0.3828 0.0382  -0.0166 0.1087  426 ASP A OD1 
696  O OD2 . ASP A 87  ? 0.4916 0.4302 0.2939 0.0207  0.0176  0.1210  426 ASP A OD2 
697  N N   . ASP A 88  ? 0.3655 0.3711 0.2607 0.0579  -0.0166 0.0541  427 ASP A N   
698  C CA  . ASP A 88  ? 0.3971 0.4032 0.3150 0.0706  -0.0386 0.0415  427 ASP A CA  
699  C C   . ASP A 88  ? 0.4090 0.4270 0.3596 0.0764  -0.0408 0.0272  427 ASP A C   
700  O O   . ASP A 88  ? 0.4913 0.4940 0.4586 0.0858  -0.0605 0.0227  427 ASP A O   
701  C CB  . ASP A 88  ? 0.3540 0.3858 0.2810 0.0756  -0.0423 0.0267  427 ASP A CB  
702  C CG  . ASP A 88  ? 0.4139 0.4342 0.3100 0.0711  -0.0426 0.0378  427 ASP A CG  
703  O OD1 . ASP A 88  ? 0.4614 0.4509 0.3329 0.0708  -0.0532 0.0534  427 ASP A OD1 
704  O OD2 . ASP A 88  ? 0.4172 0.4592 0.3128 0.0671  -0.0326 0.0313  427 ASP A OD2 
705  N N   . TRP A 89  ? 0.3740 0.4188 0.3342 0.0712  -0.0226 0.0191  428 TRP A N   
706  C CA  . TRP A 89  ? 0.3325 0.3940 0.3219 0.0767  -0.0241 0.0024  428 TRP A CA  
707  C C   . TRP A 89  ? 0.3875 0.4229 0.3762 0.0735  -0.0251 0.0131  428 TRP A C   
708  O O   . TRP A 89  ? 0.4721 0.5020 0.4845 0.0820  -0.0390 0.0021  428 TRP A O   
709  C CB  . TRP A 89  ? 0.2961 0.3972 0.2930 0.0710  -0.0058 -0.0089 428 TRP A CB  
710  C CG  . TRP A 89  ? 0.3224 0.4562 0.3331 0.0752  -0.0079 -0.0255 428 TRP A CG  
711  C CD1 . TRP A 89  ? 0.3570 0.4979 0.3553 0.0702  -0.0039 -0.0208 428 TRP A CD1 
712  C CD2 . TRP A 89  ? 0.2873 0.4536 0.3296 0.0848  -0.0147 -0.0511 428 TRP A CD2 
713  N NE1 . TRP A 89  ? 0.3088 0.4846 0.3298 0.0748  -0.0075 -0.0402 428 TRP A NE1 
714  C CE2 . TRP A 89  ? 0.3007 0.4947 0.3489 0.0839  -0.0132 -0.0596 428 TRP A CE2 
715  C CE3 . TRP A 89  ? 0.3604 0.5371 0.4285 0.0943  -0.0220 -0.0696 428 TRP A CE3 
716  C CZ2 . TRP A 89  ? 0.2918 0.5266 0.3710 0.0913  -0.0170 -0.0855 428 TRP A CZ2 
717  C CZ3 . TRP A 89  ? 0.3852 0.6020 0.4830 0.1031  -0.0262 -0.0972 428 TRP A CZ3 
718  C CH2 . TRP A 89  ? 0.3686 0.6157 0.4719 0.1012  -0.0228 -0.1048 428 TRP A CH2 
719  N N   . LEU A 90  ? 0.4112 0.4313 0.3760 0.0615  -0.0112 0.0328  429 LEU A N   
720  C CA  . LEU A 90  ? 0.3980 0.3966 0.3643 0.0561  -0.0104 0.0434  429 LEU A CA  
721  C C   . LEU A 90  ? 0.4347 0.3949 0.3958 0.0575  -0.0293 0.0574  429 LEU A C   
722  O O   . LEU A 90  ? 0.4555 0.3968 0.4264 0.0544  -0.0344 0.0633  429 LEU A O   
723  C CB  . LEU A 90  ? 0.3089 0.3073 0.2546 0.0428  0.0108  0.0585  429 LEU A CB  
724  C CG  . LEU A 90  ? 0.2790 0.3085 0.2304 0.0394  0.0276  0.0491  429 LEU A CG  
725  C CD1 . LEU A 90  ? 0.2727 0.2977 0.2065 0.0283  0.0447  0.0636  429 LEU A CD1 
726  C CD2 . LEU A 90  ? 0.3054 0.3495 0.2828 0.0435  0.0249  0.0340  429 LEU A CD2 
727  N N   . HIS A 91  ? 0.4627 0.4099 0.4088 0.0611  -0.0414 0.0636  430 HIS A N   
728  C CA  . HIS A 91  ? 0.5448 0.4527 0.4791 0.0602  -0.0607 0.0816  430 HIS A CA  
729  C C   . HIS A 91  ? 0.6386 0.5408 0.5878 0.0754  -0.0872 0.0699  430 HIS A C   
730  O O   . HIS A 91  ? 0.7220 0.6048 0.6500 0.0760  -0.1002 0.0823  430 HIS A O   
731  C CB  . HIS A 91  ? 0.5126 0.4060 0.4051 0.0471  -0.0498 0.1059  430 HIS A CB  
732  C CG  . HIS A 91  ? 0.4928 0.3969 0.3745 0.0338  -0.0234 0.1138  430 HIS A CG  
733  N ND1 . HIS A 91  ? 0.4769 0.3995 0.3380 0.0283  -0.0039 0.1146  430 HIS A ND1 
734  C CD2 . HIS A 91  ? 0.4630 0.3622 0.3550 0.0256  -0.0150 0.1196  430 HIS A CD2 
735  C CE1 . HIS A 91  ? 0.4085 0.3377 0.2686 0.0182  0.0152  0.1199  430 HIS A CE1 
736  N NE2 . HIS A 91  ? 0.4388 0.3550 0.3172 0.0160  0.0094  0.1234  430 HIS A NE2 
737  N N   . SER A 92  ? 0.9336 0.8549 0.9206 0.0884  -0.0961 0.0442  431 SER A N   
738  C CA  . SER A 92  ? 0.9512 0.8734 0.9614 0.1050  -0.1215 0.0273  431 SER A CA  
739  C C   . SER A 92  ? 1.0672 0.9930 1.1203 0.1178  -0.1367 0.0044  431 SER A C   
740  O O   . SER A 92  ? 1.1400 1.0897 1.2085 0.1162  -0.1219 -0.0093 431 SER A O   
741  C CB  . SER A 92  ? 0.9118 0.8738 0.9253 0.1100  -0.1126 0.0099  431 SER A CB  
742  O OG  . SER A 92  ? 0.9749 0.9427 1.0156 0.1266  -0.1368 -0.0091 431 SER A OG  
743  N N   . MET A 104 ? 0.4944 0.7068 0.6980 0.1584  -0.0915 -0.1703 443 MET A N   
744  C CA  . MET A 104 ? 0.4625 0.6956 0.6502 0.1449  -0.0672 -0.1669 443 MET A CA  
745  C C   . MET A 104 ? 0.5282 0.7169 0.6812 0.1311  -0.0599 -0.1322 443 MET A C   
746  O O   . MET A 104 ? 0.5422 0.6969 0.6733 0.1263  -0.0639 -0.1077 443 MET A O   
747  C CB  . MET A 104 ? 0.4841 0.7676 0.6632 0.1336  -0.0442 -0.1714 443 MET A CB  
748  C CG  . MET A 104 ? 0.6914 0.9900 0.8473 0.1172  -0.0207 -0.1607 443 MET A CG  
749  S SD  . MET A 104 ? 0.4794 0.8242 0.6193 0.0997  0.0034  -0.1556 443 MET A SD  
750  C CE  . MET A 104 ? 0.3887 0.7325 0.5004 0.0829  0.0222  -0.1387 443 MET A CE  
751  N N   . CYS A 105 ? 0.4322 0.6241 0.5810 0.1248  -0.0493 -0.1318 444 CYS A N   
752  C CA  . CYS A 105 ? 0.4008 0.5608 0.5212 0.1110  -0.0391 -0.1027 444 CYS A CA  
753  C C   . CYS A 105 ? 0.3672 0.5591 0.4716 0.0978  -0.0150 -0.1002 444 CYS A C   
754  O O   . CYS A 105 ? 0.4746 0.7082 0.5919 0.0997  -0.0087 -0.1223 444 CYS A O   
755  C CB  . CYS A 105 ? 0.5090 0.6358 0.6413 0.1149  -0.0524 -0.1015 444 CYS A CB  
756  S SG  . CYS A 105 ? 0.6464 0.7228 0.7923 0.1264  -0.0837 -0.0950 444 CYS A SG  
757  N N   . LEU A 106 ? 0.3172 0.4901 0.3932 0.0844  -0.0024 -0.0734 445 LEU A N   
758  C CA  . LEU A 106 ? 0.2346 0.4310 0.2948 0.0717  0.0172  -0.0675 445 LEU A CA  
759  C C   . LEU A 106 ? 0.2537 0.4559 0.3214 0.0710  0.0191  -0.0751 445 LEU A C   
760  O O   . LEU A 106 ? 0.2625 0.4330 0.3316 0.0710  0.0133  -0.0658 445 LEU A O   
761  C CB  . LEU A 106 ? 0.2346 0.4067 0.2674 0.0600  0.0272  -0.0398 445 LEU A CB  
762  C CG  . LEU A 106 ? 0.2739 0.4432 0.2951 0.0587  0.0272  -0.0320 445 LEU A CG  
763  C CD1 . LEU A 106 ? 0.2851 0.4292 0.2805 0.0486  0.0362  -0.0079 445 LEU A CD1 
764  C CD2 . LEU A 106 ? 0.2244 0.4358 0.2510 0.0556  0.0346  -0.0445 445 LEU A CD2 
765  N N   . SER A 107 ? 0.2029 0.4470 0.2751 0.0692  0.0270  -0.0918 446 SER A N   
766  C CA  . SER A 107 ? 0.2022 0.4562 0.2787 0.0682  0.0286  -0.1006 446 SER A CA  
767  C C   . SER A 107 ? 0.2036 0.4404 0.2588 0.0551  0.0391  -0.0764 446 SER A C   
768  O O   . SER A 107 ? 0.2253 0.4462 0.2630 0.0472  0.0463  -0.0550 446 SER A O   
769  C CB  . SER A 107 ? 0.1971 0.5044 0.2788 0.0682  0.0352  -0.1242 446 SER A CB  
770  O OG  . SER A 107 ? 0.1920 0.5104 0.2515 0.0529  0.0457  -0.1089 446 SER A OG  
771  N N   . TRP A 108 ? 0.3032 0.3155 0.1673 -0.0045 0.0488  0.0328  447 TRP A N   
772  C CA  . TRP A 108 ? 0.2869 0.3111 0.1450 -0.0018 0.0404  0.0251  447 TRP A CA  
773  C C   . TRP A 108 ? 0.2768 0.2978 0.1311 0.0080  0.0437  0.0298  447 TRP A C   
774  O O   . TRP A 108 ? 0.3320 0.3651 0.1930 0.0068  0.0394  0.0282  447 TRP A O   
775  C CB  . TRP A 108 ? 0.2984 0.3200 0.1389 0.0021  0.0349  0.0158  447 TRP A CB  
776  C CG  . TRP A 108 ? 0.2815 0.3144 0.1146 0.0076  0.0264  0.0084  447 TRP A CG  
777  C CD1 . TRP A 108 ? 0.3000 0.3256 0.1144 0.0213  0.0262  0.0076  447 TRP A CD1 
778  C CD2 . TRP A 108 ? 0.2985 0.3520 0.1426 0.0007  0.0174  0.0012  447 TRP A CD2 
779  N NE1 . TRP A 108 ? 0.3110 0.3523 0.1244 0.0232  0.0168  0.0002  447 TRP A NE1 
780  C CE2 . TRP A 108 ? 0.3143 0.3732 0.1468 0.0105  0.0114  -0.0037 447 TRP A CE2 
781  C CE3 . TRP A 108 ? 0.2780 0.3451 0.1402 -0.0118 0.0145  -0.0009 447 TRP A CE3 
782  C CZ2 . TRP A 108 ? 0.3182 0.3969 0.1586 0.0075  0.0026  -0.0107 447 TRP A CZ2 
783  C CZ3 . TRP A 108 ? 0.2491 0.3345 0.1184 -0.0147 0.0067  -0.0075 447 TRP A CZ3 
784  C CH2 . TRP A 108 ? 0.2950 0.3867 0.1544 -0.0054 0.0007  -0.0124 447 TRP A CH2 
785  N N   . PHE A 109 ? 0.2779 0.2813 0.1212 0.0182  0.0525  0.0359  448 PHE A N   
786  C CA  . PHE A 109 ? 0.3181 0.3155 0.1579 0.0281  0.0581  0.0414  448 PHE A CA  
787  C C   . PHE A 109 ? 0.3361 0.3415 0.1979 0.0215  0.0594  0.0464  448 PHE A C   
788  O O   . PHE A 109 ? 0.3525 0.3642 0.2154 0.0242  0.0572  0.0455  448 PHE A O   
789  C CB  . PHE A 109 ? 0.3617 0.3370 0.1898 0.0390  0.0702  0.0493  448 PHE A CB  
790  C CG  . PHE A 109 ? 0.4338 0.4000 0.2600 0.0495  0.0789  0.0564  448 PHE A CG  
791  C CD1 . PHE A 109 ? 0.4992 0.4622 0.3080 0.0612  0.0765  0.0525  448 PHE A CD1 
792  C CD2 . PHE A 109 ? 0.3814 0.3429 0.2275 0.0469  0.0881  0.0659  448 PHE A CD2 
793  C CE1 . PHE A 109 ? 0.5993 0.5535 0.4116 0.0698  0.0835  0.0579  448 PHE A CE1 
794  C CE2 . PHE A 109 ? 0.4105 0.3637 0.2611 0.0549  0.0948  0.0705  448 PHE A CE2 
795  C CZ  . PHE A 109 ? 0.6094 0.5581 0.4422 0.0666  0.0932  0.0669  448 PHE A CZ  
796  N N   . GLN A 110 ? 0.3264 0.3312 0.2053 0.0130  0.0626  0.0515  449 GLN A N   
797  C CA  . GLN A 110 ? 0.3274 0.3393 0.2270 0.0067  0.0623  0.0553  449 GLN A CA  
798  C C   . GLN A 110 ? 0.3189 0.3482 0.2225 0.0001  0.0519  0.0482  449 GLN A C   
799  O O   . GLN A 110 ? 0.3236 0.3574 0.2335 0.0005  0.0506  0.0487  449 GLN A O   
800  C CB  . GLN A 110 ? 0.3069 0.3165 0.2230 -0.0006 0.0658  0.0611  449 GLN A CB  
801  C CG  . GLN A 110 ? 0.2664 0.2591 0.1833 0.0060  0.0778  0.0699  449 GLN A CG  
802  C CD  . GLN A 110 ? 0.3324 0.3246 0.2672 -0.0008 0.0807  0.0758  449 GLN A CD  
803  O OE1 . GLN A 110 ? 0.3707 0.3675 0.3049 -0.0072 0.0767  0.0730  449 GLN A OE1 
804  N NE2 . GLN A 110 ? 0.3131 0.2999 0.2653 0.0007  0.0881  0.0841  449 GLN A NE2 
805  N N   . ARG A 111 ? 0.2957 0.3341 0.1962 -0.0060 0.0452  0.0417  450 ARG A N   
806  C CA  . ARG A 111 ? 0.2794 0.3339 0.1842 -0.0118 0.0367  0.0356  450 ARG A CA  
807  C C   . ARG A 111 ? 0.3014 0.3607 0.1967 -0.0044 0.0337  0.0318  450 ARG A C   
808  O O   . ARG A 111 ? 0.3303 0.3986 0.2313 -0.0063 0.0302  0.0305  450 ARG A O   
809  C CB  . ARG A 111 ? 0.2824 0.3443 0.1861 -0.0188 0.0319  0.0295  450 ARG A CB  
810  C CG  . ARG A 111 ? 0.2676 0.3251 0.1803 -0.0260 0.0351  0.0335  450 ARG A CG  
811  C CD  . ARG A 111 ? 0.2892 0.3489 0.1978 -0.0311 0.0330  0.0277  450 ARG A CD  
812  N NE  . ARG A 111 ? 0.3225 0.3749 0.2368 -0.0360 0.0378  0.0323  450 ARG A NE  
813  C CZ  . ARG A 111 ? 0.3159 0.3744 0.2391 -0.0442 0.0367  0.0321  450 ARG A CZ  
814  N NH1 . ARG A 111 ? 0.2938 0.3653 0.2214 -0.0487 0.0314  0.0275  450 ARG A NH1 
815  N NH2 . ARG A 111 ? 0.2433 0.2939 0.1704 -0.0471 0.0418  0.0371  450 ARG A NH2 
816  N N   . VAL A 112 ? 0.3174 0.3699 0.1965 0.0050  0.0351  0.0300  451 VAL A N   
817  C CA  . VAL A 112 ? 0.3002 0.3565 0.1687 0.0140  0.0327  0.0271  451 VAL A CA  
818  C C   . VAL A 112 ? 0.3030 0.3513 0.1749 0.0194  0.0395  0.0340  451 VAL A C   
819  O O   . VAL A 112 ? 0.3045 0.3597 0.1766 0.0218  0.0372  0.0326  451 VAL A O   
820  C CB  . VAL A 112 ? 0.3337 0.3835 0.1819 0.0242  0.0318  0.0233  451 VAL A CB  
821  C CG1 . VAL A 112 ? 0.3441 0.3969 0.1802 0.0355  0.0299  0.0213  451 VAL A CG1 
822  C CG2 . VAL A 112 ? 0.2862 0.3453 0.1334 0.0177  0.0237  0.0147  451 VAL A CG2 
823  N N   . GLN A 113 ? 0.3257 0.3592 0.2015 0.0214  0.0487  0.0417  452 GLN A N   
824  C CA  . GLN A 113 ? 0.3529 0.3784 0.2360 0.0252  0.0560  0.0482  452 GLN A CA  
825  C C   . GLN A 113 ? 0.3241 0.3601 0.2241 0.0160  0.0512  0.0472  452 GLN A C   
826  O O   . GLN A 113 ? 0.3486 0.3846 0.2494 0.0192  0.0521  0.0476  452 GLN A O   
827  C CB  . GLN A 113 ? 0.4217 0.4313 0.3116 0.0271  0.0669  0.0568  452 GLN A CB  
828  C CG  . GLN A 113 ? 0.4805 0.4807 0.3817 0.0305  0.0758  0.0637  452 GLN A CG  
829  C CD  . GLN A 113 ? 0.5980 0.5882 0.4821 0.0445  0.0824  0.0654  452 GLN A CD  
830  O OE1 . GLN A 113 ? 0.5924 0.5880 0.4737 0.0467  0.0795  0.0626  452 GLN A OE1 
831  N NE2 . GLN A 113 ? 0.6969 0.6713 0.5680 0.0550  0.0920  0.0704  452 GLN A NE2 
832  N N   . ILE A 114 ? 0.2734 0.3171 0.1853 0.0051  0.0462  0.0458  453 ILE A N   
833  C CA  . ILE A 114 ? 0.2721 0.3239 0.1976 -0.0028 0.0412  0.0448  453 ILE A CA  
834  C C   . ILE A 114 ? 0.3067 0.3703 0.2249 -0.0021 0.0346  0.0386  453 ILE A C   
835  O O   . ILE A 114 ? 0.3226 0.3876 0.2448 -0.0022 0.0334  0.0384  453 ILE A O   
836  C CB  . ILE A 114 ? 0.2667 0.3232 0.2034 -0.0127 0.0378  0.0452  453 ILE A CB  
837  C CG1 . ILE A 114 ? 0.2422 0.2879 0.1906 -0.0132 0.0446  0.0524  453 ILE A CG1 
838  C CG2 . ILE A 114 ? 0.2133 0.2791 0.1584 -0.0194 0.0309  0.0425  453 ILE A CG2 
839  C CD1 . ILE A 114 ? 0.2590 0.3079 0.2162 -0.0210 0.0423  0.0535  453 ILE A CD1 
840  N N   . ALA A 115 ? 0.2928 0.3649 0.2009 -0.0014 0.0301  0.0332  454 ALA A N   
841  C CA  . ALA A 115 ? 0.2804 0.3646 0.1832 0.0002  0.0246  0.0278  454 ALA A CA  
842  C C   . ALA A 115 ? 0.2952 0.3744 0.1891 0.0107  0.0280  0.0292  454 ALA A C   
843  O O   . ALA A 115 ? 0.2917 0.3772 0.1853 0.0118  0.0256  0.0273  454 ALA A O   
844  C CB  . ALA A 115 ? 0.2343 0.3284 0.1304 -0.0003 0.0195  0.0216  454 ALA A CB  
845  N N   . HIS A 116 ? 0.2582 0.3247 0.1439 0.0193  0.0346  0.0329  455 HIS A N   
846  C CA  . HIS A 116 ? 0.2943 0.3540 0.1698 0.0308  0.0395  0.0350  455 HIS A CA  
847  C C   . HIS A 116 ? 0.2685 0.3206 0.1548 0.0292  0.0446  0.0394  455 HIS A C   
848  O O   . HIS A 116 ? 0.2688 0.3217 0.1508 0.0341  0.0452  0.0388  455 HIS A O   
849  C CB  . HIS A 116 ? 0.3316 0.3775 0.1936 0.0414  0.0465  0.0384  455 HIS A CB  
850  C CG  . HIS A 116 ? 0.3162 0.3536 0.1647 0.0553  0.0526  0.0410  455 HIS A CG  
851  N ND1 . HIS A 116 ? 0.3837 0.4048 0.2355 0.0602  0.0639  0.0485  455 HIS A ND1 
852  C CD2 . HIS A 116 ? 0.3065 0.3484 0.1408 0.0649  0.0486  0.0369  455 HIS A CD2 
853  C CE1 . HIS A 116 ? 0.4290 0.4442 0.2672 0.0727  0.0676  0.0493  455 HIS A CE1 
854  N NE2 . HIS A 116 ? 0.3317 0.3592 0.1619 0.0750  0.0570  0.0416  455 HIS A NE2 
855  N N   . ASP A 117 ? 0.2960 0.3408 0.1970 0.0224  0.0481  0.0437  456 ASP A N   
856  C CA  . ASP A 117 ? 0.2766 0.3147 0.1908 0.0196  0.0515  0.0467  456 ASP A CA  
857  C C   . ASP A 117 ? 0.2636 0.3125 0.1812 0.0136  0.0434  0.0418  456 ASP A C   
858  O O   . ASP A 117 ? 0.2844 0.3289 0.2034 0.0157  0.0452  0.0419  456 ASP A O   
859  C CB  . ASP A 117 ? 0.2814 0.3129 0.2135 0.0127  0.0546  0.0513  456 ASP A CB  
860  C CG  . ASP A 117 ? 0.3042 0.3233 0.2333 0.0193  0.0644  0.0573  456 ASP A CG  
861  O OD1 . ASP A 117 ? 0.3085 0.3189 0.2235 0.0306  0.0714  0.0594  456 ASP A OD1 
862  O OD2 . ASP A 117 ? 0.3409 0.3581 0.2805 0.0142  0.0657  0.0603  456 ASP A OD2 
863  N N   . VAL A 118 ? 0.2376 0.2992 0.1559 0.0066  0.0352  0.0375  457 VAL A N   
864  C CA  . VAL A 118 ? 0.2023 0.2729 0.1220 0.0019  0.0285  0.0333  457 VAL A CA  
865  C C   . VAL A 118 ? 0.2369 0.3129 0.1437 0.0096  0.0280  0.0305  457 VAL A C   
866  O O   . VAL A 118 ? 0.2093 0.2845 0.1154 0.0103  0.0273  0.0294  457 VAL A O   
867  C CB  . VAL A 118 ? 0.2211 0.3025 0.1445 -0.0065 0.0219  0.0305  457 VAL A CB  
868  C CG1 . VAL A 118 ? 0.2483 0.3372 0.1710 -0.0099 0.0163  0.0269  457 VAL A CG1 
869  C CG2 . VAL A 118 ? 0.2478 0.3237 0.1836 -0.0131 0.0224  0.0339  457 VAL A CG2 
870  N N   . ALA A 119 ? 0.2221 0.3034 0.1182 0.0158  0.0280  0.0290  458 ALA A N   
871  C CA  . ALA A 119 ? 0.2177 0.3046 0.1021 0.0247  0.0276  0.0268  458 ALA A CA  
872  C C   . ALA A 119 ? 0.2687 0.3420 0.1484 0.0332  0.0353  0.0308  458 ALA A C   
873  O O   . ALA A 119 ? 0.2603 0.3354 0.1343 0.0381  0.0357  0.0298  458 ALA A O   
874  C CB  . ALA A 119 ? 0.2220 0.3164 0.0965 0.0305  0.0252  0.0240  458 ALA A CB  
875  N N   . ASP A 120 ? 0.2779 0.3368 0.1604 0.0353  0.0426  0.0357  459 ASP A N   
876  C CA  . ASP A 120 ? 0.2777 0.3216 0.1582 0.0428  0.0519  0.0402  459 ASP A CA  
877  C C   . ASP A 120 ? 0.2438 0.2843 0.1350 0.0365  0.0512  0.0395  459 ASP A C   
878  O O   . ASP A 120 ? 0.2524 0.2863 0.1383 0.0427  0.0558  0.0403  459 ASP A O   
879  C CB  . ASP A 120 ? 0.2576 0.2867 0.1425 0.0451  0.0608  0.0462  459 ASP A CB  
880  C CG  . ASP A 120 ? 0.3012 0.3137 0.1813 0.0558  0.0728  0.0517  459 ASP A CG  
881  O OD1 . ASP A 120 ? 0.4025 0.4151 0.2735 0.0623  0.0739  0.0506  459 ASP A OD1 
882  O OD2 . ASP A 120 ? 0.3391 0.3379 0.2247 0.0581  0.0822  0.0575  459 ASP A OD2 
883  N N   . ALA A 121 ? 0.2570 0.3012 0.1622 0.0248  0.0454  0.0378  460 ALA A N   
884  C CA  . ALA A 121 ? 0.2315 0.2721 0.1455 0.0188  0.0428  0.0360  460 ALA A CA  
885  C C   . ALA A 121 ? 0.2520 0.3024 0.1560 0.0195  0.0369  0.0313  460 ALA A C   
886  O O   . ALA A 121 ? 0.2665 0.3106 0.1682 0.0215  0.0384  0.0303  460 ALA A O   
887  C CB  . ALA A 121 ? 0.2225 0.2640 0.1528 0.0075  0.0376  0.0356  460 ALA A CB  
888  N N   . LEU A 122 ? 0.2493 0.3144 0.1481 0.0180  0.0310  0.0285  461 LEU A N   
889  C CA  . LEU A 122 ? 0.2217 0.2968 0.1123 0.0195  0.0268  0.0249  461 LEU A CA  
890  C C   . LEU A 122 ? 0.2733 0.3471 0.1517 0.0310  0.0317  0.0257  461 LEU A C   
891  O O   . LEU A 122 ? 0.2972 0.3721 0.1699 0.0336  0.0313  0.0241  461 LEU A O   
892  C CB  . LEU A 122 ? 0.2122 0.3034 0.1027 0.0158  0.0210  0.0222  461 LEU A CB  
893  C CG  . LEU A 122 ? 0.2035 0.2964 0.1038 0.0050  0.0163  0.0215  461 LEU A CG  
894  C CD1 . LEU A 122 ? 0.2094 0.3173 0.1096 0.0016  0.0122  0.0189  461 LEU A CD1 
895  C CD2 . LEU A 122 ? 0.2584 0.3451 0.1609 0.0012  0.0137  0.0203  461 LEU A CD2 
896  N N   . ASN A 123 ? 0.2663 0.3368 0.1390 0.0391  0.0368  0.0284  462 ASN A N   
897  C CA  . ASN A 123 ? 0.2780 0.3457 0.1377 0.0518  0.0421  0.0299  462 ASN A CA  
898  C C   . ASN A 123 ? 0.2839 0.3348 0.1441 0.0541  0.0493  0.0323  462 ASN A C   
899  O O   . ASN A 123 ? 0.2791 0.3292 0.1302 0.0610  0.0516  0.0320  462 ASN A O   
900  C CB  . ASN A 123 ? 0.2573 0.3225 0.1088 0.0609  0.0460  0.0324  462 ASN A CB  
901  C CG  . ASN A 123 ? 0.2820 0.3424 0.1243 0.0735  0.0494  0.0331  462 ASN A CG  
902  O OD1 . ASN A 123 ? 0.2828 0.3278 0.1204 0.0814  0.0580  0.0375  462 ASN A OD1 
903  N ND2 . ASN A 123 ? 0.3129 0.3854 0.1551 0.0752  0.0428  0.0290  462 ASN A ND2 
904  N N   . TYR A 124 ? 0.2872 0.3247 0.1591 0.0484  0.0530  0.0347  463 TYR A N   
905  C CA  . TYR A 124 ? 0.2794 0.3005 0.1555 0.0488  0.0594  0.0361  463 TYR A CA  
906  C C   . TYR A 124 ? 0.3144 0.3375 0.1919 0.0424  0.0531  0.0313  463 TYR A C   
907  O O   . TYR A 124 ? 0.3316 0.3461 0.2026 0.0472  0.0572  0.0310  463 TYR A O   
908  C CB  . TYR A 124 ? 0.2710 0.2796 0.1637 0.0429  0.0641  0.0392  463 TYR A CB  
909  C CG  . TYR A 124 ? 0.3230 0.3176 0.2278 0.0376  0.0666  0.0383  463 TYR A CG  
910  C CD1 . TYR A 124 ? 0.3367 0.3154 0.2390 0.0451  0.0776  0.0413  463 TYR A CD1 
911  C CD2 . TYR A 124 ? 0.3324 0.3290 0.2514 0.0255  0.0578  0.0342  463 TYR A CD2 
912  C CE1 . TYR A 124 ? 0.3918 0.3570 0.3069 0.0394  0.0797  0.0396  463 TYR A CE1 
913  C CE2 . TYR A 124 ? 0.2993 0.2834 0.2302 0.0204  0.0584  0.0321  463 TYR A CE2 
914  C CZ  . TYR A 124 ? 0.3723 0.3407 0.3021 0.0268  0.0694  0.0345  463 TYR A CZ  
915  O OH  . TYR A 124 ? 0.4159 0.3712 0.3591 0.0210  0.0698  0.0315  463 TYR A OH  
916  N N   . LEU A 125 ? 0.3038 0.3368 0.1879 0.0326  0.0436  0.0279  464 LEU A N   
917  C CA  . LEU A 125 ? 0.2731 0.3060 0.1564 0.0274  0.0375  0.0235  464 LEU A CA  
918  C C   . LEU A 125 ? 0.2768 0.3165 0.1446 0.0350  0.0378  0.0222  464 LEU A C   
919  O O   . LEU A 125 ? 0.3100 0.3418 0.1722 0.0361  0.0383  0.0201  464 LEU A O   
920  C CB  . LEU A 125 ? 0.2841 0.3264 0.1750 0.0174  0.0283  0.0209  464 LEU A CB  
921  C CG  . LEU A 125 ? 0.3325 0.3687 0.2402 0.0091  0.0265  0.0218  464 LEU A CG  
922  C CD1 . LEU A 125 ? 0.2579 0.3042 0.1701 0.0010  0.0177  0.0197  464 LEU A CD1 
923  C CD2 . LEU A 125 ? 0.3520 0.3728 0.2678 0.0064  0.0273  0.0201  464 LEU A CD2 
924  N N   . HIS A 126 ? 0.2780 0.3323 0.1394 0.0404  0.0374  0.0231  465 HIS A N   
925  C CA  . HIS A 126 ? 0.3136 0.3781 0.1638 0.0468  0.0367  0.0218  465 HIS A CA  
926  C C   . HIS A 126 ? 0.2724 0.3303 0.1114 0.0592  0.0446  0.0244  465 HIS A C   
927  O O   . HIS A 126 ? 0.3543 0.4160 0.1851 0.0646  0.0451  0.0236  465 HIS A O   
928  C CB  . HIS A 126 ? 0.3057 0.3904 0.1570 0.0468  0.0320  0.0209  465 HIS A CB  
929  C CG  . HIS A 126 ? 0.2548 0.3471 0.1148 0.0357  0.0253  0.0185  465 HIS A CG  
930  N ND1 . HIS A 126 ? 0.2301 0.3389 0.0940 0.0333  0.0212  0.0172  465 HIS A ND1 
931  C CD2 . HIS A 126 ? 0.2352 0.3200 0.1005 0.0271  0.0219  0.0172  465 HIS A CD2 
932  C CE1 . HIS A 126 ? 0.2271 0.3376 0.0978 0.0238  0.0170  0.0158  465 HIS A CE1 
933  N NE2 . HIS A 126 ? 0.2416 0.3380 0.1124 0.0204  0.0169  0.0158  465 HIS A NE2 
934  N N   . ASN A 127 ? 0.3158 0.3629 0.1544 0.0645  0.0515  0.0279  466 ASN A N   
935  C CA  . ASN A 127 ? 0.2927 0.3343 0.1201 0.0778  0.0590  0.0308  466 ASN A CA  
936  C C   . ASN A 127 ? 0.3098 0.3286 0.1360 0.0810  0.0694  0.0340  466 ASN A C   
937  O O   . ASN A 127 ? 0.3568 0.3665 0.1736 0.0886  0.0757  0.0351  466 ASN A O   
938  C CB  . ASN A 127 ? 0.3072 0.3565 0.1377 0.0828  0.0564  0.0315  466 ASN A CB  
939  C CG  . ASN A 127 ? 0.2860 0.3559 0.1228 0.0786  0.0460  0.0273  466 ASN A CG  
940  O OD1 . ASN A 127 ? 0.3343 0.4116 0.1758 0.0741  0.0418  0.0263  466 ASN A OD1 
941  N ND2 . ASN A 127 ? 0.3057 0.3842 0.1428 0.0804  0.0428  0.0253  466 ASN A ND2 
942  N N   . TYR A 128 ? 0.3298 0.3386 0.1682 0.0748  0.0718  0.0355  467 TYR A N   
943  C CA  . TYR A 128 ? 0.3884 0.3756 0.2298 0.0782  0.0832  0.0393  467 TYR A CA  
944  C C   . TYR A 128 ? 0.3835 0.3583 0.2415 0.0659  0.0818  0.0366  467 TYR A C   
945  O O   . TYR A 128 ? 0.3322 0.2885 0.1958 0.0674  0.0914  0.0388  467 TYR A O   
946  C CB  . TYR A 128 ? 0.3222 0.3054 0.1643 0.0839  0.0900  0.0446  467 TYR A CB  
947  C CG  . TYR A 128 ? 0.3232 0.3195 0.1491 0.0957  0.0884  0.0458  467 TYR A CG  
948  C CD1 . TYR A 128 ? 0.3332 0.3278 0.1526 0.1055  0.0886  0.0457  467 TYR A CD1 
949  C CD2 . TYR A 128 ? 0.3115 0.3216 0.1408 0.0924  0.0801  0.0441  467 TYR A CD2 
950  C CE1 . TYR A 128 ? 0.3318 0.3386 0.1487 0.1121  0.0810  0.0444  467 TYR A CE1 
951  C CE2 . TYR A 128 ? 0.3263 0.3475 0.1526 0.0986  0.0727  0.0419  467 TYR A CE2 
952  C CZ  . TYR A 128 ? 0.3509 0.3709 0.1713 0.1087  0.0732  0.0422  467 TYR A CZ  
953  O OH  . TYR A 128 ? 0.3981 0.4297 0.2157 0.1157  0.0662  0.0403  467 TYR A OH  
954  N N   . ALA A 129 ? 0.3426 0.3267 0.2089 0.0544  0.0704  0.0316  468 ALA A N   
955  C CA  . ALA A 129 ? 0.3591 0.3321 0.2367 0.0446  0.0668  0.0274  468 ALA A CA  
956  C C   . ALA A 129 ? 0.4118 0.3741 0.2775 0.0499  0.0706  0.0253  468 ALA A C   
957  O O   . ALA A 129 ? 0.5223 0.4926 0.3714 0.0576  0.0703  0.0254  468 ALA A O   
958  C CB  . ALA A 129 ? 0.3526 0.3380 0.2358 0.0339  0.0535  0.0225  468 ALA A CB  
959  N N   . ASN A 130 ? 0.3749 0.3186 0.2499 0.0461  0.0746  0.0236  469 ASN A N   
960  C CA  . ASN A 130 ? 0.4360 0.3651 0.2999 0.0513  0.0800  0.0217  469 ASN A CA  
961  C C   . ASN A 130 ? 0.4671 0.3907 0.3344 0.0416  0.0697  0.0137  469 ASN A C   
962  O O   . ASN A 130 ? 0.5604 0.4702 0.4436 0.0336  0.0689  0.0102  469 ASN A O   
963  C CB  . ASN A 130 ? 0.4175 0.3265 0.2882 0.0559  0.0945  0.0258  469 ASN A CB  
964  C CG  . ASN A 130 ? 0.4440 0.3380 0.2994 0.0645  0.1030  0.0257  469 ASN A CG  
965  O OD1 . ASN A 130 ? 0.4909 0.3866 0.3297 0.0778  0.1114  0.0308  469 ASN A OD1 
966  N ND2 . ASN A 130 ? 0.5440 0.4231 0.4047 0.0575  0.1006  0.0194  469 ASN A ND2 
967  N N   . PRO A 131 ? 0.4668 0.4000 0.3194 0.0422  0.0616  0.0104  470 PRO A N   
968  C CA  . PRO A 131 ? 0.4375 0.3882 0.2743 0.0504  0.0613  0.0134  470 PRO A CA  
969  C C   . PRO A 131 ? 0.4427 0.4136 0.2862 0.0451  0.0530  0.0139  470 PRO A C   
970  O O   . PRO A 131 ? 0.4781 0.4492 0.3366 0.0354  0.0470  0.0121  470 PRO A O   
971  C CB  . PRO A 131 ? 0.4594 0.4058 0.2806 0.0522  0.0577  0.0090  470 PRO A CB  
972  C CG  . PRO A 131 ? 0.4924 0.4292 0.3230 0.0406  0.0481  0.0021  470 PRO A CG  
973  C CD  . PRO A 131 ? 0.5118 0.4368 0.3624 0.0353  0.0522  0.0026  470 PRO A CD  
974  N N   . PRO A 132 ? 0.4382 0.4262 0.2718 0.0513  0.0525  0.0163  471 PRO A N   
975  C CA  . PRO A 132 ? 0.3684 0.3748 0.2084 0.0460  0.0452  0.0165  471 PRO A CA  
976  C C   . PRO A 132 ? 0.3804 0.3883 0.2239 0.0362  0.0351  0.0117  471 PRO A C   
977  O O   . PRO A 132 ? 0.4172 0.4163 0.2524 0.0359  0.0327  0.0081  471 PRO A O   
978  C CB  . PRO A 132 ? 0.3288 0.3517 0.1575 0.0550  0.0466  0.0186  471 PRO A CB  
979  C CG  . PRO A 132 ? 0.3924 0.4058 0.2106 0.0666  0.0564  0.0216  471 PRO A CG  
980  C CD  . PRO A 132 ? 0.4303 0.4219 0.2481 0.0638  0.0592  0.0192  471 PRO A CD  
981  N N   . HIS A 133 ? 0.3558 0.3741 0.2100 0.0291  0.0293  0.0118  472 HIS A N   
982  C CA  . HIS A 133 ? 0.3470 0.3665 0.2050 0.0203  0.0199  0.0081  472 HIS A CA  
983  C C   . HIS A 133 ? 0.3356 0.3732 0.1960 0.0177  0.0162  0.0095  472 HIS A C   
984  O O   . HIS A 133 ? 0.2930 0.3385 0.1606 0.0178  0.0186  0.0126  472 HIS A O   
985  C CB  . HIS A 133 ? 0.3702 0.3786 0.2440 0.0123  0.0166  0.0063  472 HIS A CB  
986  C CG  . HIS A 133 ? 0.4010 0.4108 0.2788 0.0043  0.0060  0.0024  472 HIS A CG  
987  N ND1 . HIS A 133 ? 0.3844 0.4032 0.2742 -0.0019 0.0016  0.0038  472 HIS A ND1 
988  C CD2 . HIS A 133 ? 0.4136 0.4158 0.2831 0.0026  -0.0012 -0.0028 472 HIS A CD2 
989  C CE1 . HIS A 133 ? 0.3499 0.3673 0.2390 -0.0068 -0.0077 0.0000  472 HIS A CE1 
990  N NE2 . HIS A 133 ? 0.4333 0.4406 0.3096 -0.0040 -0.0099 -0.0043 472 HIS A NE2 
991  N N   . VAL A 134 ? 0.3233 0.3662 0.1769 0.0159  0.0111  0.0074  473 VAL A N   
992  C CA  . VAL A 134 ? 0.2874 0.3459 0.1442 0.0127  0.0082  0.0085  473 VAL A CA  
993  C C   . VAL A 134 ? 0.3194 0.3751 0.1854 0.0040  0.0014  0.0072  473 VAL A C   
994  O O   . VAL A 134 ? 0.3452 0.3902 0.2083 0.0015  -0.0039 0.0039  473 VAL A O   
995  C CB  . VAL A 134 ? 0.2969 0.3626 0.1418 0.0165  0.0086  0.0081  473 VAL A CB  
996  C CG1 . VAL A 134 ? 0.3395 0.4190 0.1897 0.0120  0.0061  0.0090  473 VAL A CG1 
997  C CG2 . VAL A 134 ? 0.3562 0.4280 0.1947 0.0255  0.0151  0.0099  473 VAL A CG2 
998  N N   . HIS A 135 ? 0.3167 0.3816 0.1932 0.0000  0.0010  0.0094  474 HIS A N   
999  C CA  . HIS A 135 ? 0.3582 0.4211 0.2448 -0.0075 -0.0047 0.0091  474 HIS A CA  
1000 C C   . HIS A 135 ? 0.3266 0.3914 0.2057 -0.0096 -0.0102 0.0073  474 HIS A C   
1001 O O   . HIS A 135 ? 0.3697 0.4250 0.2469 -0.0117 -0.0164 0.0044  474 HIS A O   
1002 C CB  . HIS A 135 ? 0.3375 0.4090 0.2349 -0.0103 -0.0024 0.0124  474 HIS A CB  
1003 C CG  . HIS A 135 ? 0.2674 0.3356 0.1773 -0.0170 -0.0067 0.0130  474 HIS A CG  
1004 N ND1 . HIS A 135 ? 0.2836 0.3526 0.1931 -0.0212 -0.0131 0.0117  474 HIS A ND1 
1005 C CD2 . HIS A 135 ? 0.3069 0.3711 0.2304 -0.0195 -0.0048 0.0154  474 HIS A CD2 
1006 C CE1 . HIS A 135 ? 0.3385 0.4052 0.2613 -0.0260 -0.0159 0.0129  474 HIS A CE1 
1007 N NE2 . HIS A 135 ? 0.3739 0.4378 0.3063 -0.0254 -0.0106 0.0153  474 HIS A NE2 
1008 N N   . LYS A 136 ? 0.3110 0.3876 0.1860 -0.0086 -0.0078 0.0088  475 LYS A N   
1009 C CA  . LYS A 136 ? 0.3543 0.4332 0.2212 -0.0089 -0.0099 0.0084  475 LYS A CA  
1010 C C   . LYS A 136 ? 0.3062 0.3872 0.1805 -0.0149 -0.0138 0.0096  475 LYS A C   
1011 O O   . LYS A 136 ? 0.3070 0.3907 0.1752 -0.0149 -0.0138 0.0103  475 LYS A O   
1012 C CB  . LYS A 136 ? 0.3073 0.3737 0.1598 -0.0054 -0.0134 0.0054  475 LYS A CB  
1013 C CG  . LYS A 136 ? 0.3672 0.4318 0.2085 0.0017  -0.0083 0.0049  475 LYS A CG  
1014 C CD  . LYS A 136 ? 0.3868 0.4432 0.2103 0.0062  -0.0094 0.0033  475 LYS A CD  
1015 C CE  . LYS A 136 ? 0.4942 0.5328 0.3102 0.0060  -0.0168 -0.0014 475 LYS A CE  
1016 N NZ  . LYS A 136 ? 0.5849 0.6148 0.3996 0.0088  -0.0146 -0.0034 475 LYS A NZ  
1017 N N   . ASN A 137 ? 0.3139 0.3932 0.2009 -0.0193 -0.0159 0.0104  476 ASN A N   
1018 C CA  . ASN A 137 ? 0.3429 0.4227 0.2367 -0.0242 -0.0199 0.0116  476 ASN A CA  
1019 C C   . ASN A 137 ? 0.3197 0.4047 0.2278 -0.0279 -0.0169 0.0146  476 ASN A C   
1020 O O   . ASN A 137 ? 0.3442 0.4260 0.2625 -0.0316 -0.0201 0.0157  476 ASN A O   
1021 C CB  . ASN A 137 ? 0.3543 0.4233 0.2486 -0.0254 -0.0283 0.0089  476 ASN A CB  
1022 C CG  . ASN A 137 ? 0.3911 0.4611 0.2899 -0.0288 -0.0331 0.0103  476 ASN A CG  
1023 O OD1 . ASN A 137 ? 0.4738 0.5502 0.3696 -0.0293 -0.0299 0.0130  476 ASN A OD1 
1024 N ND2 . ASN A 137 ? 0.4578 0.5215 0.3651 -0.0312 -0.0407 0.0085  476 ASN A ND2 
1025 N N   . LEU A 138 ? 0.2946 0.3874 0.2032 -0.0263 -0.0109 0.0157  477 LEU A N   
1026 C CA  . LEU A 138 ? 0.2638 0.3599 0.1826 -0.0285 -0.0078 0.0182  477 LEU A CA  
1027 C C   . LEU A 138 ? 0.2993 0.4014 0.2212 -0.0328 -0.0075 0.0198  477 LEU A C   
1028 O O   . LEU A 138 ? 0.2991 0.4090 0.2165 -0.0327 -0.0053 0.0192  477 LEU A O   
1029 C CB  . LEU A 138 ? 0.2423 0.3436 0.1583 -0.0240 -0.0028 0.0180  477 LEU A CB  
1030 C CG  . LEU A 138 ? 0.2626 0.3649 0.1854 -0.0244 0.0006  0.0202  477 LEU A CG  
1031 C CD1 . LEU A 138 ? 0.1842 0.2755 0.1150 -0.0246 0.0016  0.0225  477 LEU A CD1 
1032 C CD2 . LEU A 138 ? 0.2320 0.3410 0.1491 -0.0189 0.0040  0.0191  477 LEU A CD2 
1033 N N   . LYS A 139 ? 0.2668 0.3650 0.1975 -0.0364 -0.0090 0.0220  478 LYS A N   
1034 C CA  . LYS A 139 ? 0.2923 0.3941 0.2259 -0.0402 -0.0081 0.0241  478 LYS A CA  
1035 C C   . LYS A 139 ? 0.2692 0.3680 0.2136 -0.0424 -0.0061 0.0272  478 LYS A C   
1036 O O   . LYS A 139 ? 0.2847 0.3779 0.2361 -0.0414 -0.0063 0.0282  478 LYS A O   
1037 C CB  . LYS A 139 ? 0.2999 0.3986 0.2299 -0.0412 -0.0129 0.0243  478 LYS A CB  
1038 C CG  . LYS A 139 ? 0.3492 0.4482 0.2663 -0.0379 -0.0140 0.0219  478 LYS A CG  
1039 C CD  . LYS A 139 ? 0.3378 0.4303 0.2489 -0.0370 -0.0201 0.0217  478 LYS A CD  
1040 C CE  . LYS A 139 ? 0.3372 0.4291 0.2330 -0.0330 -0.0188 0.0207  478 LYS A CE  
1041 N NZ  . LYS A 139 ? 0.2880 0.3799 0.1772 -0.0294 -0.0174 0.0180  478 LYS A NZ  
1042 N N   . SER A 140 ? 0.2513 0.3533 0.1977 -0.0452 -0.0032 0.0290  479 SER A N   
1043 C CA  . SER A 140 ? 0.2744 0.3726 0.2298 -0.0468 -0.0005 0.0326  479 SER A CA  
1044 C C   . SER A 140 ? 0.2783 0.3709 0.2434 -0.0480 -0.0044 0.0352  479 SER A C   
1045 O O   . SER A 140 ? 0.2400 0.3280 0.2152 -0.0477 -0.0023 0.0380  479 SER A O   
1046 C CB  . SER A 140 ? 0.2429 0.3440 0.1974 -0.0499 0.0031  0.0337  479 SER A CB  
1047 O OG  . SER A 140 ? 0.3212 0.4234 0.2733 -0.0519 0.0012  0.0343  479 SER A OG  
1048 N N   . GLY A 141 ? 0.2924 0.3852 0.2548 -0.0486 -0.0102 0.0342  480 GLY A N   
1049 C CA  . GLY A 141 ? 0.3333 0.4222 0.3055 -0.0494 -0.0160 0.0356  480 GLY A CA  
1050 C C   . GLY A 141 ? 0.3013 0.3860 0.2803 -0.0484 -0.0194 0.0334  480 GLY A C   
1051 O O   . GLY A 141 ? 0.2966 0.3784 0.2897 -0.0498 -0.0232 0.0346  480 GLY A O   
1052 N N   . ASN A 142 ? 0.3302 0.4143 0.3007 -0.0460 -0.0178 0.0302  481 ASN A N   
1053 C CA  . ASN A 142 ? 0.2873 0.3657 0.2633 -0.0447 -0.0194 0.0281  481 ASN A CA  
1054 C C   . ASN A 142 ? 0.2605 0.3358 0.2443 -0.0433 -0.0114 0.0310  481 ASN A C   
1055 O O   . ASN A 142 ? 0.3063 0.3754 0.2997 -0.0428 -0.0108 0.0308  481 ASN A O   
1056 C CB  . ASN A 142 ? 0.2747 0.3524 0.2360 -0.0416 -0.0212 0.0236  481 ASN A CB  
1057 C CG  . ASN A 142 ? 0.4122 0.4898 0.3637 -0.0414 -0.0288 0.0207  481 ASN A CG  
1058 O OD1 . ASN A 142 ? 0.5465 0.6212 0.5043 -0.0431 -0.0360 0.0200  481 ASN A OD1 
1059 N ND2 . ASN A 142 ? 0.3660 0.4464 0.3019 -0.0387 -0.0271 0.0191  481 ASN A ND2 
1060 N N   . ILE A 143 ? 0.2553 0.3338 0.2348 -0.0422 -0.0049 0.0336  482 ILE A N   
1061 C CA  . ILE A 143 ? 0.2691 0.3433 0.2517 -0.0390 0.0032  0.0366  482 ILE A CA  
1062 C C   . ILE A 143 ? 0.2340 0.3040 0.2328 -0.0411 0.0060  0.0417  482 ILE A C   
1063 O O   . ILE A 143 ? 0.2490 0.3214 0.2483 -0.0429 0.0073  0.0442  482 ILE A O   
1064 C CB  . ILE A 143 ? 0.2284 0.3072 0.1980 -0.0362 0.0076  0.0360  482 ILE A CB  
1065 C CG1 . ILE A 143 ? 0.2455 0.3293 0.2024 -0.0334 0.0055  0.0315  482 ILE A CG1 
1066 C CG2 . ILE A 143 ? 0.2036 0.2762 0.1741 -0.0317 0.0156  0.0395  482 ILE A CG2 
1067 C CD1 . ILE A 143 ? 0.2282 0.3204 0.1752 -0.0325 0.0067  0.0295  482 ILE A CD1 
1068 N N   . LEU A 144 ? 0.2397 0.3031 0.2527 -0.0409 0.0074  0.0433  483 LEU A N   
1069 C CA  . LEU A 144 ? 0.2886 0.3486 0.3204 -0.0426 0.0109  0.0487  483 LEU A CA  
1070 C C   . LEU A 144 ? 0.2591 0.3125 0.2892 -0.0377 0.0226  0.0539  483 LEU A C   
1071 O O   . LEU A 144 ? 0.2443 0.2952 0.2601 -0.0326 0.0272  0.0528  483 LEU A O   
1072 C CB  . LEU A 144 ? 0.2148 0.2710 0.2663 -0.0451 0.0074  0.0480  483 LEU A CB  
1073 C CG  . LEU A 144 ? 0.2795 0.3402 0.3314 -0.0489 -0.0054 0.0421  483 LEU A CG  
1074 C CD1 . LEU A 144 ? 0.2731 0.3300 0.3476 -0.0519 -0.0097 0.0407  483 LEU A CD1 
1075 C CD2 . LEU A 144 ? 0.2980 0.3659 0.3467 -0.0512 -0.0113 0.0428  483 LEU A CD2 
1076 N N   . LEU A 145 ? 0.2533 0.3036 0.2973 -0.0385 0.0275  0.0597  484 LEU A N   
1077 C CA  . LEU A 145 ? 0.2819 0.3236 0.3246 -0.0330 0.0394  0.0656  484 LEU A CA  
1078 C C   . LEU A 145 ? 0.2921 0.3272 0.3597 -0.0332 0.0455  0.0714  484 LEU A C   
1079 O O   . LEU A 145 ? 0.3189 0.3587 0.4062 -0.0387 0.0395  0.0716  484 LEU A O   
1080 C CB  . LEU A 145 ? 0.2891 0.3322 0.3227 -0.0328 0.0416  0.0678  484 LEU A CB  
1081 C CG  . LEU A 145 ? 0.2527 0.3042 0.2679 -0.0349 0.0348  0.0620  484 LEU A CG  
1082 C CD1 . LEU A 145 ? 0.2373 0.2890 0.2483 -0.0363 0.0371  0.0644  484 LEU A CD1 
1083 C CD2 . LEU A 145 ? 0.2462 0.2974 0.2429 -0.0299 0.0362  0.0579  484 LEU A CD2 
1084 N N   . ASP A 146 ? 0.2604 0.2845 0.3275 -0.0268 0.0575  0.0761  485 ASP A N   
1085 C CA  . ASP A 146 ? 0.2853 0.3019 0.3777 -0.0264 0.0660  0.0826  485 ASP A CA  
1086 C C   . ASP A 146 ? 0.3406 0.3518 0.4357 -0.0231 0.0757  0.0906  485 ASP A C   
1087 O O   . ASP A 146 ? 0.3708 0.3855 0.4512 -0.0231 0.0732  0.0900  485 ASP A O   
1088 C CB  . ASP A 146 ? 0.2492 0.2550 0.3412 -0.0207 0.0750  0.0838  485 ASP A CB  
1089 C CG  . ASP A 146 ? 0.3192 0.3151 0.3867 -0.0103 0.0859  0.0869  485 ASP A CG  
1090 O OD1 . ASP A 146 ? 0.3513 0.3496 0.4008 -0.0083 0.0846  0.0865  485 ASP A OD1 
1091 O OD2 . ASP A 146 ? 0.3673 0.3521 0.4332 -0.0037 0.0958  0.0897  485 ASP A OD2 
1092 N N   . GLY A 147 ? 0.2915 0.2933 0.4061 -0.0201 0.0876  0.0983  486 GLY A N   
1093 C CA  . GLY A 147 ? 0.3201 0.3157 0.4354 -0.0152 0.0952  0.1036  486 GLY A CA  
1094 C C   . GLY A 147 ? 0.3588 0.3452 0.4427 -0.0063 0.1013  0.1035  486 GLY A C   
1095 O O   . GLY A 147 ? 0.3346 0.3186 0.4108 -0.0037 0.1021  0.1040  486 GLY A O   
1096 N N   . LYS A 148 ? 0.3611 0.3420 0.4265 -0.0011 0.1053  0.1025  487 LYS A N   
1097 C CA  . LYS A 148 ? 0.3263 0.3000 0.3605 0.0076  0.1087  0.1010  487 LYS A CA  
1098 C C   . LYS A 148 ? 0.3363 0.3215 0.3508 0.0035  0.0978  0.0941  487 LYS A C   
1099 O O   . LYS A 148 ? 0.3873 0.3693 0.3766 0.0102  0.0981  0.0908  487 LYS A O   
1100 C CB  . LYS A 148 ? 0.3366 0.2971 0.3605 0.0186  0.1182  0.1024  487 LYS A CB  
1101 C CG  . LYS A 148 ? 0.3585 0.3065 0.3952 0.0262  0.1283  0.1064  487 LYS A CG  
1102 C CD  . LYS A 148 ? 0.4132 0.3485 0.4449 0.0366  0.1386  0.1082  487 LYS A CD  
1103 C CE  . LYS A 148 ? 0.4653 0.3880 0.5039 0.0466  0.1502  0.1120  487 LYS A CE  
1104 N NZ  . LYS A 148 ? 0.5123 0.4282 0.5704 0.0504  0.1600  0.1149  487 LYS A NZ  
1105 N N   . PHE A 149 ? 0.3040 0.3030 0.3297 -0.0066 0.0859  0.0896  488 PHE A N   
1106 C CA  . PHE A 149 ? 0.3062 0.3168 0.3160 -0.0109 0.0742  0.0814  488 PHE A CA  
1107 C C   . PHE A 149 ? 0.3429 0.3555 0.3360 -0.0068 0.0710  0.0755  488 PHE A C   
1108 O O   . PHE A 149 ? 0.4100 0.4264 0.3831 -0.0048 0.0671  0.0705  488 PHE A O   
1109 C CB  . PHE A 149 ? 0.3215 0.3304 0.3167 -0.0098 0.0754  0.0815  488 PHE A CB  
1110 C CG  . PHE A 149 ? 0.3404 0.3507 0.3507 -0.0151 0.0760  0.0860  488 PHE A CG  
1111 C CD1 . PHE A 149 ? 0.3669 0.3671 0.3904 -0.0116 0.0868  0.0948  488 PHE A CD1 
1112 C CD2 . PHE A 149 ? 0.3431 0.3644 0.3548 -0.0227 0.0666  0.0821  488 PHE A CD2 
1113 C CE1 . PHE A 149 ? 0.3970 0.3992 0.4341 -0.0154 0.0846  0.0964  488 PHE A CE1 
1114 C CE2 . PHE A 149 ? 0.3290 0.3515 0.3537 -0.0265 0.0672  0.0867  488 PHE A CE2 
1115 C CZ  . PHE A 149 ? 0.3639 0.3773 0.4019 -0.0230 0.0767  0.0947  488 PHE A CZ  
1116 N N   . ARG A 150 ? 0.2892 0.2993 0.2915 -0.0058 0.0727  0.0760  489 ARG A N   
1117 C CA  . ARG A 150 ? 0.2691 0.2809 0.2579 -0.0019 0.0700  0.0710  489 ARG A CA  
1118 C C   . ARG A 150 ? 0.2743 0.2974 0.2706 -0.0100 0.0587  0.0651  489 ARG A C   
1119 O O   . ARG A 150 ? 0.2787 0.3045 0.2945 -0.0169 0.0549  0.0658  489 ARG A O   
1120 C CB  . ARG A 150 ? 0.3101 0.3084 0.3012 0.0062  0.0814  0.0759  489 ARG A CB  
1121 C CG  . ARG A 150 ? 0.3667 0.3510 0.3519 0.0151  0.0945  0.0834  489 ARG A CG  
1122 C CD  . ARG A 150 ? 0.4316 0.4010 0.4176 0.0244  0.1076  0.0889  489 ARG A CD  
1123 N NE  . ARG A 150 ? 0.5079 0.4787 0.4788 0.0292  0.1048  0.0842  489 ARG A NE  
1124 C CZ  . ARG A 150 ? 0.5336 0.5086 0.4787 0.0355  0.1002  0.0794  489 ARG A CZ  
1125 N NH1 . ARG A 150 ? 0.5137 0.4917 0.4447 0.0368  0.0968  0.0777  489 ARG A NH1 
1126 N NH2 . ARG A 150 ? 0.4947 0.4710 0.4288 0.0404  0.0986  0.0761  489 ARG A NH2 
1127 N N   . GLY A 151 ? 0.2576 0.2873 0.2378 -0.0083 0.0530  0.0591  490 GLY A N   
1128 C CA  . GLY A 151 ? 0.1964 0.2363 0.1789 -0.0148 0.0426  0.0534  490 GLY A CA  
1129 C C   . GLY A 151 ? 0.2060 0.2414 0.2000 -0.0159 0.0423  0.0528  490 GLY A C   
1130 O O   . GLY A 151 ? 0.2772 0.3032 0.2704 -0.0098 0.0500  0.0551  490 GLY A O   
1131 N N   . LYS A 152 ? 0.2687 0.3098 0.2725 -0.0233 0.0332  0.0495  491 LYS A N   
1132 C CA  . LYS A 152 ? 0.2718 0.3089 0.2869 -0.0257 0.0304  0.0472  491 LYS A CA  
1133 C C   . LYS A 152 ? 0.2781 0.3235 0.2860 -0.0300 0.0188  0.0407  491 LYS A C   
1134 O O   . LYS A 152 ? 0.2945 0.3449 0.3103 -0.0357 0.0112  0.0396  491 LYS A O   
1135 C CB  . LYS A 152 ? 0.2316 0.2640 0.2726 -0.0301 0.0319  0.0508  491 LYS A CB  
1136 C CG  . LYS A 152 ? 0.2246 0.2476 0.2739 -0.0254 0.0452  0.0584  491 LYS A CG  
1137 C CD  . LYS A 152 ? 0.2174 0.2285 0.2734 -0.0213 0.0540  0.0601  491 LYS A CD  
1138 C CE  . LYS A 152 ? 0.2373 0.2372 0.3001 -0.0152 0.0690  0.0687  491 LYS A CE  
1139 N NZ  . LYS A 152 ? 0.2755 0.2625 0.3488 -0.0116 0.0793  0.0713  491 LYS A NZ  
1140 N N   . VAL A 153 ? 0.2822 0.3283 0.2745 -0.0263 0.0179  0.0370  492 VAL A N   
1141 C CA  . VAL A 153 ? 0.3085 0.3607 0.2922 -0.0290 0.0086  0.0314  492 VAL A CA  
1142 C C   . VAL A 153 ? 0.2997 0.3469 0.2967 -0.0338 0.0017  0.0285  492 VAL A C   
1143 O O   . VAL A 153 ? 0.3436 0.3822 0.3548 -0.0342 0.0052  0.0296  492 VAL A O   
1144 C CB  . VAL A 153 ? 0.2767 0.3298 0.2427 -0.0231 0.0104  0.0287  492 VAL A CB  
1145 C CG1 . VAL A 153 ? 0.4126 0.4736 0.3671 -0.0248 0.0028  0.0243  492 VAL A CG1 
1146 C CG2 . VAL A 153 ? 0.2580 0.3135 0.2144 -0.0168 0.0177  0.0315  492 VAL A CG2 
1147 N N   . SER A 154 ? 0.3422 0.3944 0.3346 -0.0372 -0.0080 0.0246  493 SER A N   
1148 C CA  . SER A 154 ? 0.3908 0.4390 0.3955 -0.0416 -0.0168 0.0211  493 SER A CA  
1149 C C   . SER A 154 ? 0.4615 0.5083 0.4515 -0.0409 -0.0254 0.0147  493 SER A C   
1150 O O   . SER A 154 ? 0.5243 0.5628 0.5146 -0.0403 -0.0269 0.0108  493 SER A O   
1151 C CB  . SER A 154 ? 0.3270 0.3807 0.3445 -0.0460 -0.0217 0.0234  493 SER A CB  
1152 O OG  . SER A 154 ? 0.5072 0.5682 0.5100 -0.0458 -0.0260 0.0228  493 SER A OG  
1153 N N   . ASN A 155 ? 0.4017 0.4551 0.3783 -0.0407 -0.0302 0.0138  494 ASN A N   
1154 C CA  . ASN A 155 ? 0.4714 0.5221 0.4340 -0.0395 -0.0389 0.0083  494 ASN A CA  
1155 C C   . ASN A 155 ? 0.4580 0.5066 0.4019 -0.0344 -0.0343 0.0065  494 ASN A C   
1156 O O   . ASN A 155 ? 0.4355 0.4888 0.3633 -0.0316 -0.0340 0.0064  494 ASN A O   
1157 C CB  . ASN A 155 ? 0.4373 0.4943 0.3925 -0.0401 -0.0440 0.0091  494 ASN A CB  
1158 C CG  . ASN A 155 ? 0.4661 0.5239 0.4376 -0.0440 -0.0515 0.0096  494 ASN A CG  
1159 O OD1 . ASN A 155 ? 0.4355 0.4921 0.4276 -0.0471 -0.0504 0.0111  494 ASN A OD1 
1160 N ND2 . ASN A 155 ? 0.5824 0.6421 0.5450 -0.0431 -0.0586 0.0087  494 ASN A ND2 
1161 N N   . PHE A 156 ? 0.4675 0.5086 0.4148 -0.0328 -0.0301 0.0054  495 PHE A N   
1162 C CA  . PHE A 156 ? 0.4520 0.4908 0.3828 -0.0271 -0.0250 0.0043  495 PHE A CA  
1163 C C   . PHE A 156 ? 0.4809 0.5087 0.4021 -0.0256 -0.0307 -0.0018 495 PHE A C   
1164 O O   . PHE A 156 ? 0.4944 0.5194 0.4004 -0.0202 -0.0266 -0.0026 495 PHE A O   
1165 C CB  . PHE A 156 ? 0.4134 0.4501 0.3496 -0.0240 -0.0146 0.0078  495 PHE A CB  
1166 C CG  . PHE A 156 ? 0.4102 0.4385 0.3663 -0.0273 -0.0129 0.0086  495 PHE A CG  
1167 C CD1 . PHE A 156 ? 0.5635 0.5797 0.5243 -0.0284 -0.0153 0.0042  495 PHE A CD1 
1168 C CD2 . PHE A 156 ? 0.3810 0.4126 0.3518 -0.0291 -0.0080 0.0138  495 PHE A CD2 
1169 C CE1 . PHE A 156 ? 0.6012 0.6099 0.5840 -0.0319 -0.0128 0.0050  495 PHE A CE1 
1170 C CE2 . PHE A 156 ? 0.5179 0.5417 0.5090 -0.0318 -0.0048 0.0153  495 PHE A CE2 
1171 C CZ  . PHE A 156 ? 0.6358 0.6486 0.6343 -0.0335 -0.0070 0.0110  495 PHE A CZ  
1172 N N   . GLY A 157 ? 0.5755 0.5967 0.5045 -0.0297 -0.0403 -0.0062 496 GLY A N   
1173 C CA  . GLY A 157 ? 0.6747 0.6837 0.5932 -0.0281 -0.0466 -0.0130 496 GLY A CA  
1174 C C   . GLY A 157 ? 0.7189 0.7230 0.6435 -0.0322 -0.0604 -0.0189 496 GLY A C   
1175 O O   . GLY A 157 ? 0.7809 0.7884 0.7276 -0.0376 -0.0641 -0.0182 496 GLY A O   
1176 N N   . LEU A 158 ? 0.6338 0.6301 0.5385 -0.0288 -0.0681 -0.0246 497 LEU A N   
1177 C CA  . LEU A 158 ? 0.6620 0.6524 0.5685 -0.0310 -0.0831 -0.0316 497 LEU A CA  
1178 C C   . LEU A 158 ? 0.7156 0.7164 0.6249 -0.0321 -0.0891 -0.0287 497 LEU A C   
1179 O O   . LEU A 158 ? 0.6560 0.6529 0.5559 -0.0304 -0.1013 -0.0336 497 LEU A O   
1180 C CB  . LEU A 158 ? 0.6002 0.5839 0.5320 -0.0373 -0.0876 -0.0363 497 LEU A CB  
1181 C CG  . LEU A 158 ? 0.6244 0.5912 0.5479 -0.0365 -0.0935 -0.0455 497 LEU A CG  
1182 C CD1 . LEU A 158 ? 0.6215 0.5828 0.5753 -0.0438 -0.0953 -0.0492 497 LEU A CD1 
1183 C CD2 . LEU A 158 ? 0.6026 0.5632 0.5065 -0.0334 -0.1088 -0.0530 497 LEU A CD2 
1184 N N   . ALA A 159 ? 0.7543 0.7674 0.6752 -0.0341 -0.0808 -0.0210 498 ALA A N   
1185 C CA  . ALA A 159 ? 0.7174 0.7401 0.6387 -0.0344 -0.0836 -0.0170 498 ALA A CA  
1186 C C   . ALA A 159 ? 0.8175 0.8441 0.7155 -0.0290 -0.0773 -0.0132 498 ALA A C   
1187 O O   . ALA A 159 ? 0.8067 0.8393 0.7013 -0.0283 -0.0788 -0.0100 498 ALA A O   
1188 C CB  . ALA A 159 ? 0.5881 0.6205 0.5342 -0.0395 -0.0776 -0.0108 498 ALA A CB  
1189 N N   . ARG A 160 ? 0.6676 0.6911 0.5510 -0.0250 -0.0697 -0.0132 499 ARG A N   
1190 C CA  . ARG A 160 ? 0.6935 0.7206 0.5567 -0.0197 -0.0636 -0.0100 499 ARG A CA  
1191 C C   . ARG A 160 ? 0.7064 0.7238 0.5474 -0.0142 -0.0718 -0.0140 499 ARG A C   
1192 O O   . ARG A 160 ? 0.7486 0.7547 0.5853 -0.0133 -0.0816 -0.0207 499 ARG A O   
1193 C CB  . ARG A 160 ? 0.6634 0.6912 0.5200 -0.0166 -0.0533 -0.0086 499 ARG A CB  
1194 C CG  . ARG A 160 ? 0.5768 0.6131 0.4516 -0.0201 -0.0453 -0.0046 499 ARG A CG  
1195 C CD  . ARG A 160 ? 0.5568 0.5908 0.4263 -0.0163 -0.0375 -0.0046 499 ARG A CD  
1196 N NE  . ARG A 160 ? 0.5649 0.5854 0.4349 -0.0160 -0.0412 -0.0096 499 ARG A NE  
1197 C CZ  . ARG A 160 ? 0.5470 0.5614 0.4103 -0.0119 -0.0354 -0.0105 499 ARG A CZ  
1198 N NH1 . ARG A 160 ? 0.5335 0.5554 0.3894 -0.0071 -0.0263 -0.0067 499 ARG A NH1 
1199 N NH2 . ARG A 160 ? 0.5123 0.5128 0.3770 -0.0126 -0.0388 -0.0155 499 ARG A NH2 
1200 N N   . VAL A 161 ? 0.7030 0.7241 0.5295 -0.0099 -0.0672 -0.0100 500 VAL A N   
1201 C CA  . VAL A 161 ? 0.7403 0.7535 0.5481 -0.0045 -0.0748 -0.0119 500 VAL A CA  
1202 C C   . VAL A 161 ? 0.9266 0.9239 0.7130 0.0017  -0.0808 -0.0185 500 VAL A C   
1203 O O   . VAL A 161 ? 0.8936 0.8810 0.6719 0.0039  -0.0936 -0.0243 500 VAL A O   
1204 C CB  . VAL A 161 ? 0.6579 0.6766 0.4544 -0.0006 -0.0656 -0.0054 500 VAL A CB  
1205 C CG1 . VAL A 161 ? 0.5876 0.5936 0.3549 0.0089  -0.0678 -0.0069 500 VAL A CG1 
1206 C CG2 . VAL A 161 ? 0.6114 0.6389 0.4217 -0.0047 -0.0667 -0.0012 500 VAL A CG2 
1207 N N   . MET A 162 ? 0.8410 0.8352 0.6172 0.0051  -0.0722 -0.0180 501 MET A N   
1208 C CA  . MET A 162 ? 0.7559 0.7336 0.5103 0.0114  -0.0762 -0.0240 501 MET A CA  
1209 C C   . MET A 162 ? 0.7755 0.7480 0.5404 0.0078  -0.0770 -0.0287 501 MET A C   
1210 O O   . MET A 162 ? 0.7881 0.7460 0.5357 0.0126  -0.0791 -0.0338 501 MET A O   
1211 C CB  . MET A 162 ? 0.7098 0.6848 0.4414 0.0200  -0.0651 -0.0198 501 MET A CB  
1212 C CG  . MET A 162 ? 0.6344 0.6050 0.3530 0.0254  -0.0650 -0.0177 501 MET A CG  
1213 S SD  . MET A 162 ? 0.7465 0.7007 0.4540 0.0286  -0.0815 -0.0267 501 MET A SD  
1214 C CE  . MET A 162 ? 0.6341 0.5973 0.3523 0.0257  -0.0890 -0.0243 501 MET A CE  
1215 N N   . GLU A 163 ? 0.7452 0.7277 0.5369 -0.0001 -0.0748 -0.0270 502 GLU A N   
1216 C CA  . GLU A 163 ? 0.7731 0.7485 0.5759 -0.0034 -0.0756 -0.0314 502 GLU A CA  
1217 C C   . GLU A 163 ? 0.8579 0.8223 0.6662 -0.0067 -0.0907 -0.0401 502 GLU A C   
1218 O O   . GLU A 163 ? 0.9185 0.8699 0.7252 -0.0069 -0.0935 -0.0464 502 GLU A O   
1219 C CB  . GLU A 163 ? 0.7454 0.7332 0.5737 -0.0094 -0.0674 -0.0263 502 GLU A CB  
1220 C CG  . GLU A 163 ? 0.7344 0.7346 0.5594 -0.0066 -0.0546 -0.0188 502 GLU A CG  
1221 C CD  . GLU A 163 ? 0.6708 0.6654 0.4727 0.0014  -0.0486 -0.0187 502 GLU A CD  
1222 O OE1 . GLU A 163 ? 0.7008 0.6843 0.4966 0.0039  -0.0475 -0.0223 502 GLU A OE1 
1223 O OE2 . GLU A 163 ? 0.5905 0.5913 0.3811 0.0053  -0.0442 -0.0149 502 GLU A OE2 
1224 N N   . ASN A 164 ? 0.8340 0.8031 0.6494 -0.0091 -0.1005 -0.0408 503 ASN A N   
1225 C CA  . ASN A 164 ? 0.7831 0.7437 0.6050 -0.0118 -0.1167 -0.0497 503 ASN A CA  
1226 C C   . ASN A 164 ? 0.8779 0.8199 0.6710 -0.0047 -0.1246 -0.0579 503 ASN A C   
1227 O O   . ASN A 164 ? 0.8092 0.7466 0.5742 0.0038  -0.1238 -0.0564 503 ASN A O   
1228 C CB  . ASN A 164 ? 0.8175 0.7871 0.6474 -0.0132 -0.1258 -0.0482 503 ASN A CB  
1229 C CG  . ASN A 164 ? 0.8956 0.8721 0.7078 -0.0073 -0.1184 -0.0404 503 ASN A CG  
1230 O OD1 . ASN A 164 ? 0.8388 0.8291 0.6652 -0.0107 -0.1102 -0.0328 503 ASN A OD1 
1231 N ND2 . ASN A 164 ? 0.9262 0.8920 0.7071 0.0017  -0.1205 -0.0424 503 ASN A ND2 
1232 N N   . GLU A 165 ? 1.0850 1.0150 0.8848 -0.0080 -0.1315 -0.0666 504 GLU A N   
1233 C CA  . GLU A 165 ? 1.0148 0.9248 0.7874 -0.0017 -0.1407 -0.0760 504 GLU A CA  
1234 C C   . GLU A 165 ? 1.0351 0.9415 0.7948 0.0023  -0.1578 -0.0815 504 GLU A C   
1235 O O   . GLU A 165 ? 1.0697 0.9689 0.8021 0.0118  -0.1558 -0.0807 504 GLU A O   
1236 C CB  . GLU A 165 ? 0.9297 0.8275 0.7161 -0.0073 -0.1448 -0.0847 504 GLU A CB  
1237 C CG  . GLU A 165 ? 1.1373 1.0123 0.8958 -0.0014 -0.1549 -0.0958 504 GLU A CG  
1238 C CD  . GLU A 165 ? 1.1305 0.9951 0.8567 0.0083  -0.1419 -0.0920 504 GLU A CD  
1239 O OE1 . GLU A 165 ? 0.9966 0.8735 0.7212 0.0107  -0.1267 -0.0810 504 GLU A OE1 
1240 O OE2 . GLU A 165 ? 0.9652 0.8092 0.6679 0.0134  -0.1472 -0.1004 504 GLU A OE2 
1241 N N   . GLY A 166 ? 0.9125 0.8271 0.6986 -0.0046 -0.1700 -0.0850 505 GLY A N   
1242 C CA  . GLY A 166 ? 0.8298 0.7490 0.6126 -0.0006 -0.1794 -0.0855 505 GLY A CA  
1243 C C   . GLY A 166 ? 1.0045 0.9362 0.7791 0.0039  -0.1691 -0.0739 505 GLY A C   
1244 O O   . GLY A 166 ? 1.0306 0.9763 0.8250 -0.0018 -0.1672 -0.0682 505 GLY A O   
1245 N N   . GLY A 167 ? 1.2038 1.1298 0.9507 0.0139  -0.1618 -0.0702 506 GLY A N   
1246 C CA  . GLY A 167 ? 1.2231 1.1592 0.9630 0.0182  -0.1518 -0.0598 506 GLY A CA  
1247 C C   . GLY A 167 ? 1.3161 1.2618 1.0691 0.0172  -0.1611 -0.0590 506 GLY A C   
1248 O O   . GLY A 167 ? 1.3592 1.3044 1.1263 0.0139  -0.1755 -0.0664 506 GLY A O   
1249 N N   . ASP A 168 ? 1.1196 1.0742 0.8684 0.0201  -0.1523 -0.0497 507 ASP A N   
1250 C CA  . ASP A 168 ? 1.1820 1.1463 0.9431 0.0194  -0.1592 -0.0474 507 ASP A CA  
1251 C C   . ASP A 168 ? 1.1284 1.0920 0.8695 0.0281  -0.1509 -0.0397 507 ASP A C   
1252 O O   . ASP A 168 ? 1.1538 1.1147 0.8798 0.0319  -0.1366 -0.0337 507 ASP A O   
1253 C CB  . ASP A 168 ? 1.3668 1.3458 1.1552 0.0100  -0.1583 -0.0432 507 ASP A CB  
1254 C CG  . ASP A 168 ? 1.4837 1.4639 1.2982 0.0008  -0.1688 -0.0507 507 ASP A CG  
1255 O OD1 . ASP A 168 ? 1.4574 1.4303 1.2740 0.0012  -0.1805 -0.0596 507 ASP A OD1 
1256 O OD2 . ASP A 168 ? 1.4913 1.4794 1.3259 -0.0070 -0.1640 -0.0472 507 ASP A OD2 
1257 N N   . GLU A 169 ? 1.0488 1.0147 0.7915 0.0314  -0.1598 -0.0400 508 GLU A N   
1258 C CA  . GLU A 169 ? 0.9447 0.9105 0.6724 0.0391  -0.1529 -0.0323 508 GLU A CA  
1259 C C   . GLU A 169 ? 0.9863 0.9658 0.7319 0.0356  -0.1555 -0.0271 508 GLU A C   
1260 O O   . GLU A 169 ? 0.9164 0.8959 0.6510 0.0416  -0.1494 -0.0201 508 GLU A O   
1261 C CB  . GLU A 169 ? 0.8954 0.8479 0.6011 0.0497  -0.1602 -0.0365 508 GLU A CB  
1262 C CG  . GLU A 169 ? 0.8422 0.7793 0.5225 0.0568  -0.1518 -0.0372 508 GLU A CG  
1263 C CD  . GLU A 169 ? 0.7666 0.7037 0.4354 0.0604  -0.1329 -0.0270 508 GLU A CD  
1264 O OE1 . GLU A 169 ? 0.8640 0.8013 0.5250 0.0662  -0.1285 -0.0208 508 GLU A OE1 
1265 O OE2 . GLU A 169 ? 0.7001 0.6372 0.3687 0.0574  -0.1222 -0.0250 508 GLU A OE2 
1266 N N   . GLY A 170 ? 0.9079 0.8978 0.6813 0.0265  -0.1637 -0.0300 509 GLY A N   
1267 C CA  . GLY A 170 ? 0.7491 0.7524 0.5416 0.0225  -0.1639 -0.0240 509 GLY A CA  
1268 C C   . GLY A 170 ? 0.7745 0.7834 0.5713 0.0173  -0.1502 -0.0168 509 GLY A C   
1269 O O   . GLY A 170 ? 0.8131 0.8304 0.6335 0.0085  -0.1520 -0.0161 509 GLY A O   
1270 N N   . PHE A 171 ? 0.7797 0.7832 0.5545 0.0225  -0.1362 -0.0113 510 PHE A N   
1271 C CA  . PHE A 171 ? 0.6624 0.6693 0.4375 0.0184  -0.1222 -0.0060 510 PHE A CA  
1272 C C   . PHE A 171 ? 0.6561 0.6666 0.4243 0.0213  -0.1103 0.0036  510 PHE A C   
1273 O O   . PHE A 171 ? 0.6564 0.6606 0.4080 0.0291  -0.1068 0.0067  510 PHE A O   
1274 C CB  . PHE A 171 ? 0.6592 0.6571 0.4178 0.0213  -0.1144 -0.0084 510 PHE A CB  
1275 C CG  . PHE A 171 ? 0.5708 0.5725 0.3263 0.0196  -0.0981 -0.0022 510 PHE A CG  
1276 C CD1 . PHE A 171 ? 0.5292 0.5408 0.3064 0.0104  -0.0931 -0.0014 510 PHE A CD1 
1277 C CD2 . PHE A 171 ? 0.5596 0.5565 0.2982 0.0256  -0.0850 0.0032  510 PHE A CD2 
1278 C CE1 . PHE A 171 ? 0.5664 0.5841 0.3458 0.0082  -0.0774 0.0038  510 PHE A CE1 
1279 C CE2 . PHE A 171 ? 0.5745 0.5766 0.3143 0.0235  -0.0700 0.0084  510 PHE A CE2 
1280 C CZ  . PHE A 171 ? 0.5745 0.5878 0.3334 0.0152  -0.0671 0.0083  510 PHE A CZ  
1281 N N   . GLN A 172 ? 0.6373 0.6595 0.4278 0.0124  -0.0993 0.0089  511 GLN A N   
1282 C CA  . GLN A 172 ? 0.5981 0.6249 0.3887 0.0126  -0.0856 0.0177  511 GLN A CA  
1283 C C   . GLN A 172 ? 0.5806 0.6060 0.3605 0.0132  -0.0703 0.0206  511 GLN A C   
1284 O O   . GLN A 172 ? 0.5706 0.6040 0.3662 0.0056  -0.0628 0.0209  511 GLN A O   
1285 C CB  . GLN A 172 ? 0.6354 0.6749 0.4558 0.0029  -0.0825 0.0212  511 GLN A CB  
1286 C CG  . GLN A 172 ? 0.6614 0.7042 0.4962 0.0022  -0.0962 0.0196  511 GLN A CG  
1287 C CD  . GLN A 172 ? 0.7852 0.8392 0.6488 -0.0066 -0.0911 0.0239  511 GLN A CD  
1288 O OE1 . GLN A 172 ? 0.8660 0.9231 0.7313 -0.0072 -0.0810 0.0308  511 GLN A OE1 
1289 N NE2 . GLN A 172 ? 0.7788 0.8375 0.6646 -0.0133 -0.0972 0.0200  511 GLN A NE2 
1290 N N   . LEU A 173 ? 0.5846 0.5995 0.3379 0.0232  -0.0655 0.0229  512 LEU A N   
1291 C CA  . LEU A 173 ? 0.5566 0.5698 0.3002 0.0248  -0.0510 0.0257  512 LEU A CA  
1292 C C   . LEU A 173 ? 0.5070 0.5312 0.2679 0.0177  -0.0359 0.0321  512 LEU A C   
1293 O O   . LEU A 173 ? 0.4981 0.5302 0.2711 0.0116  -0.0282 0.0318  512 LEU A O   
1294 C CB  . LEU A 173 ? 0.5147 0.5133 0.2376 0.0340  -0.0465 0.0269  512 LEU A CB  
1295 C CG  . LEU A 173 ? 0.4833 0.4792 0.2004 0.0357  -0.0308 0.0300  512 LEU A CG  
1296 C CD1 . LEU A 173 ? 0.4941 0.4950 0.2186 0.0307  -0.0313 0.0257  512 LEU A CD1 
1297 C CD2 . LEU A 173 ? 0.5165 0.4978 0.2134 0.0461  -0.0285 0.0302  512 LEU A CD2 
1298 N N   . THR A 174 ? 0.5071 0.5315 0.2690 0.0189  -0.0317 0.0377  513 THR A N   
1299 C CA  . THR A 174 ? 0.4510 0.4838 0.2280 0.0123  -0.0172 0.0432  513 THR A CA  
1300 C C   . THR A 174 ? 0.4928 0.5387 0.2965 0.0006  -0.0180 0.0408  513 THR A C   
1301 O O   . THR A 174 ? 0.4583 0.5119 0.2738 -0.0052 -0.0070 0.0427  513 THR A O   
1302 C CB  . THR A 174 ? 0.4784 0.5082 0.2532 0.0151  -0.0142 0.0490  513 THR A CB  
1303 O OG1 . THR A 174 ? 0.5606 0.5768 0.3079 0.0277  -0.0123 0.0519  513 THR A OG1 
1304 C CG2 . THR A 174 ? 0.4270 0.4638 0.2172 0.0079  0.0010  0.0540  513 THR A CG2 
1305 N N   . ARG A 175 ? 0.5068 0.5550 0.3206 -0.0024 -0.0308 0.0366  514 ARG A N   
1306 C CA  . ARG A 175 ? 0.4788 0.5374 0.3163 -0.0120 -0.0309 0.0352  514 ARG A CA  
1307 C C   . ARG A 175 ? 0.4724 0.5341 0.3121 -0.0143 -0.0292 0.0311  514 ARG A C   
1308 O O   . ARG A 175 ? 0.4557 0.5257 0.3081 -0.0201 -0.0217 0.0318  514 ARG A O   
1309 C CB  . ARG A 175 ? 0.5517 0.6111 0.4010 -0.0139 -0.0435 0.0330  514 ARG A CB  
1310 C CG  . ARG A 175 ? 0.5360 0.6039 0.4093 -0.0225 -0.0424 0.0329  514 ARG A CG  
1311 C CD  . ARG A 175 ? 0.7003 0.7691 0.5870 -0.0237 -0.0528 0.0327  514 ARG A CD  
1312 N NE  . ARG A 175 ? 0.8903 0.9641 0.7978 -0.0302 -0.0540 0.0310  514 ARG A NE  
1313 C CZ  . ARG A 175 ? 0.8643 0.9363 0.7762 -0.0310 -0.0610 0.0257  514 ARG A CZ  
1314 N NH1 . ARG A 175 ? 0.7932 0.8585 0.6897 -0.0262 -0.0684 0.0208  514 ARG A NH1 
1315 N NH2 . ARG A 175 ? 0.8873 0.9629 0.8185 -0.0363 -0.0598 0.0255  514 ARG A NH2 
1316 N N   . HIS A 176 ? 0.4940 0.5484 0.3202 -0.0092 -0.0363 0.0267  515 HIS A N   
1317 C CA  . HIS A 176 ? 0.4943 0.5503 0.3201 -0.0099 -0.0338 0.0234  515 HIS A CA  
1318 C C   . HIS A 176 ? 0.4312 0.4916 0.2534 -0.0092 -0.0203 0.0266  515 HIS A C   
1319 O O   . HIS A 176 ? 0.4313 0.4988 0.2618 -0.0123 -0.0158 0.0254  515 HIS A O   
1320 C CB  . HIS A 176 ? 0.4649 0.5096 0.2732 -0.0034 -0.0429 0.0182  515 HIS A CB  
1321 C CG  . HIS A 176 ? 0.4441 0.4882 0.2476 -0.0022 -0.0390 0.0156  515 HIS A CG  
1322 N ND1 . HIS A 176 ? 0.4680 0.5162 0.2853 -0.0072 -0.0411 0.0124  515 HIS A ND1 
1323 C CD2 . HIS A 176 ? 0.5108 0.5501 0.2972 0.0041  -0.0321 0.0163  515 HIS A CD2 
1324 C CE1 . HIS A 176 ? 0.5409 0.5873 0.3493 -0.0038 -0.0363 0.0111  515 HIS A CE1 
1325 N NE2 . HIS A 176 ? 0.5270 0.5684 0.3172 0.0028  -0.0309 0.0134  515 HIS A NE2 
1326 N N   . VAL A 177 ? 0.4252 0.4815 0.2360 -0.0047 -0.0135 0.0309  516 VAL A N   
1327 C CA  . VAL A 177 ? 0.4312 0.4918 0.2413 -0.0041 0.0001  0.0342  516 VAL A CA  
1328 C C   . VAL A 177 ? 0.4683 0.5412 0.2998 -0.0128 0.0075  0.0362  516 VAL A C   
1329 O O   . VAL A 177 ? 0.4942 0.5756 0.3340 -0.0154 0.0156  0.0363  516 VAL A O   
1330 C CB  . VAL A 177 ? 0.4068 0.4566 0.1967 0.0046  0.0064  0.0385  516 VAL A CB  
1331 C CG1 . VAL A 177 ? 0.4333 0.4873 0.2248 0.0054  0.0213  0.0419  516 VAL A CG1 
1332 C CG2 . VAL A 177 ? 0.4332 0.4691 0.1992 0.0140  -0.0027 0.0355  516 VAL A CG2 
1333 N N   . ILE A 178 ? 0.4454 0.5194 0.2861 -0.0170 0.0046  0.0377  517 ILE A N   
1334 C CA  . ILE A 178 ? 0.4413 0.5249 0.3005 -0.0250 0.0109  0.0390  517 ILE A CA  
1335 C C   . ILE A 178 ? 0.4088 0.5016 0.2811 -0.0300 0.0084  0.0349  517 ILE A C   
1336 O O   . ILE A 178 ? 0.3932 0.4949 0.2753 -0.0338 0.0150  0.0343  517 ILE A O   
1337 C CB  . ILE A 178 ? 0.4335 0.5145 0.2980 -0.0274 0.0083  0.0417  517 ILE A CB  
1338 C CG1 . ILE A 178 ? 0.4019 0.4739 0.2526 -0.0214 0.0127  0.0465  517 ILE A CG1 
1339 C CG2 . ILE A 178 ? 0.4142 0.5034 0.2964 -0.0355 0.0140  0.0422  517 ILE A CG2 
1340 C CD1 . ILE A 178 ? 0.3626 0.4319 0.2175 -0.0225 0.0105  0.0498  517 ILE A CD1 
1341 N N   . GLY A 179 ? 0.4435 0.5339 0.3164 -0.0296 -0.0013 0.0320  518 GLY A N   
1342 C CA  . GLY A 179 ? 0.3666 0.4634 0.2492 -0.0325 -0.0029 0.0288  518 GLY A CA  
1343 C C   . GLY A 179 ? 0.3708 0.4711 0.2478 -0.0294 0.0009  0.0269  518 GLY A C   
1344 O O   . GLY A 179 ? 0.4270 0.5361 0.3129 -0.0316 0.0037  0.0253  518 GLY A O   
1345 N N   . THR A 180 ? 0.4176 0.5109 0.2790 -0.0232 0.0011  0.0271  519 THR A N   
1346 C CA  . THR A 180 ? 0.4293 0.5252 0.2848 -0.0192 0.0057  0.0261  519 THR A CA  
1347 C C   . THR A 180 ? 0.4507 0.5586 0.3174 -0.0222 0.0157  0.0277  519 THR A C   
1348 O O   . THR A 180 ? 0.4073 0.5247 0.2815 -0.0228 0.0175  0.0257  519 THR A O   
1349 C CB  . THR A 180 ? 0.4485 0.5326 0.2833 -0.0112 0.0058  0.0270  519 THR A CB  
1350 O OG1 . THR A 180 ? 0.5827 0.6574 0.4078 -0.0080 -0.0042 0.0231  519 THR A OG1 
1351 C CG2 . THR A 180 ? 0.4556 0.5434 0.2860 -0.0070 0.0153  0.0284  519 THR A CG2 
1352 N N   . GLN A 181 ? 0.4407 0.5485 0.3094 -0.0239 0.0221  0.0311  520 GLN A N   
1353 C CA  . GLN A 181 ? 0.4301 0.5490 0.3118 -0.0274 0.0317  0.0320  520 GLN A CA  
1354 C C   . GLN A 181 ? 0.3987 0.5288 0.2981 -0.0347 0.0297  0.0290  520 GLN A C   
1355 O O   . GLN A 181 ? 0.4168 0.5589 0.3278 -0.0368 0.0337  0.0271  520 GLN A O   
1356 C CB  . GLN A 181 ? 0.4264 0.5403 0.3064 -0.0276 0.0401  0.0365  520 GLN A CB  
1357 C CG  . GLN A 181 ? 0.4230 0.5320 0.3054 -0.0316 0.0372  0.0379  520 GLN A CG  
1358 C CD  . GLN A 181 ? 0.3683 0.4736 0.2516 -0.0324 0.0477  0.0424  520 GLN A CD  
1359 O OE1 . GLN A 181 ? 0.3389 0.4489 0.2286 -0.0330 0.0580  0.0437  520 GLN A OE1 
1360 N NE2 . GLN A 181 ? 0.3894 0.4862 0.2675 -0.0322 0.0458  0.0452  520 GLN A NE2 
1361 N N   . GLY A 182 ? 0.3886 0.5150 0.2902 -0.0378 0.0235  0.0284  521 GLY A N   
1362 C CA  . GLY A 182 ? 0.3166 0.4508 0.2320 -0.0436 0.0224  0.0261  521 GLY A CA  
1363 C C   . GLY A 182 ? 0.3877 0.5272 0.3054 -0.0422 0.0175  0.0226  521 GLY A C   
1364 O O   . GLY A 182 ? 0.2924 0.4410 0.2200 -0.0450 0.0180  0.0200  521 GLY A O   
1365 N N   . TYR A 183 ? 0.3762 0.5095 0.2843 -0.0373 0.0127  0.0223  522 TYR A N   
1366 C CA  . TYR A 183 ? 0.2665 0.4022 0.1756 -0.0351 0.0089  0.0197  522 TYR A CA  
1367 C C   . TYR A 183 ? 0.2566 0.3955 0.1595 -0.0295 0.0102  0.0184  522 TYR A C   
1368 O O   . TYR A 183 ? 0.2791 0.4241 0.1849 -0.0274 0.0095  0.0164  522 TYR A O   
1369 C CB  . TYR A 183 ? 0.2843 0.4093 0.1901 -0.0345 0.0027  0.0200  522 TYR A CB  
1370 C CG  . TYR A 183 ? 0.2994 0.4220 0.2134 -0.0392 0.0014  0.0215  522 TYR A CG  
1371 C CD1 . TYR A 183 ? 0.3218 0.4390 0.2352 -0.0414 0.0009  0.0241  522 TYR A CD1 
1372 C CD2 . TYR A 183 ? 0.2995 0.4243 0.2206 -0.0403 0.0013  0.0208  522 TYR A CD2 
1373 C CE1 . TYR A 183 ? 0.3240 0.4390 0.2451 -0.0451 0.0005  0.0261  522 TYR A CE1 
1374 C CE2 . TYR A 183 ? 0.2882 0.4096 0.2160 -0.0438 0.0013  0.0227  522 TYR A CE2 
1375 C CZ  . TYR A 183 ? 0.3549 0.4718 0.2834 -0.0465 0.0009  0.0254  522 TYR A CZ  
1376 O OH  . TYR A 183 ? 0.3293 0.4429 0.2648 -0.0494 0.0015  0.0279  522 TYR A OH  
1377 N N   . MET A 184 ? 0.3065 0.4406 0.1995 -0.0259 0.0126  0.0199  523 MET A N   
1378 C CA  . MET A 184 ? 0.2940 0.4281 0.1786 -0.0195 0.0139  0.0192  523 MET A CA  
1379 C C   . MET A 184 ? 0.3015 0.4505 0.1954 -0.0188 0.0200  0.0189  523 MET A C   
1380 O O   . MET A 184 ? 0.3068 0.4634 0.2105 -0.0227 0.0249  0.0198  523 MET A O   
1381 C CB  . MET A 184 ? 0.2886 0.4108 0.1574 -0.0148 0.0147  0.0210  523 MET A CB  
1382 C CG  . MET A 184 ? 0.3796 0.4875 0.2380 -0.0136 0.0066  0.0196  523 MET A CG  
1383 S SD  . MET A 184 ? 0.4861 0.5913 0.3440 -0.0113 0.0018  0.0162  523 MET A SD  
1384 C CE  . MET A 184 ? 0.5100 0.5983 0.3592 -0.0112 -0.0078 0.0140  523 MET A CE  
1385 N N   . ALA A 185 ? 0.2903 0.4436 0.1822 -0.0138 0.0197  0.0175  524 ALA A N   
1386 C CA  . ALA A 185 ? 0.2557 0.4247 0.1577 -0.0121 0.0244  0.0170  524 ALA A CA  
1387 C C   . ALA A 185 ? 0.2800 0.4487 0.1778 -0.0084 0.0319  0.0200  524 ALA A C   
1388 O O   . ALA A 185 ? 0.3290 0.4834 0.2105 -0.0042 0.0325  0.0218  524 ALA A O   
1389 C CB  . ALA A 185 ? 0.2443 0.4176 0.1445 -0.0065 0.0220  0.0152  524 ALA A CB  
1390 N N   . PRO A 186 ? 0.3048 0.4886 0.2174 -0.0096 0.0378  0.0203  525 PRO A N   
1391 C CA  . PRO A 186 ? 0.3039 0.4868 0.2143 -0.0058 0.0472  0.0242  525 PRO A CA  
1392 C C   . PRO A 186 ? 0.3206 0.4967 0.2154 0.0037  0.0493  0.0259  525 PRO A C   
1393 O O   . PRO A 186 ? 0.2946 0.4583 0.1758 0.0084  0.0548  0.0294  525 PRO A O   
1394 C CB  . PRO A 186 ? 0.3389 0.5422 0.2737 -0.0097 0.0521  0.0232  525 PRO A CB  
1395 C CG  . PRO A 186 ? 0.3193 0.5345 0.2634 -0.0114 0.0440  0.0183  525 PRO A CG  
1396 C CD  . PRO A 186 ? 0.3144 0.5163 0.2467 -0.0137 0.0363  0.0169  525 PRO A CD  
1397 N N   . GLU A 187 ? 0.2945 0.4764 0.1894 0.0076  0.0454  0.0237  526 GLU A N   
1398 C CA  . GLU A 187 ? 0.3169 0.4886 0.1984 0.0167  0.0473  0.0250  526 GLU A CA  
1399 C C   . GLU A 187 ? 0.2865 0.4317 0.1477 0.0188  0.0426  0.0243  526 GLU A C   
1400 O O   . GLU A 187 ? 0.2678 0.3994 0.1154 0.0256  0.0451  0.0253  526 GLU A O   
1401 C CB  . GLU A 187 ? 0.2526 0.4339 0.1388 0.0207  0.0441  0.0228  526 GLU A CB  
1402 C CG  . GLU A 187 ? 0.2470 0.4181 0.1278 0.0192  0.0353  0.0195  526 GLU A CG  
1403 C CD  . GLU A 187 ? 0.2387 0.4242 0.1324 0.0126  0.0310  0.0171  526 GLU A CD  
1404 O OE1 . GLU A 187 ? 0.2976 0.4995 0.2066 0.0085  0.0334  0.0168  526 GLU A OE1 
1405 O OE2 . GLU A 187 ? 0.2236 0.4007 0.1144 0.0114  0.0251  0.0151  526 GLU A OE2 
1406 N N   . TYR A 188 ? 0.2931 0.4314 0.1523 0.0131  0.0358  0.0224  527 TYR A N   
1407 C CA  . TYR A 188 ? 0.3217 0.4379 0.1634 0.0146  0.0309  0.0214  527 TYR A CA  
1408 C C   . TYR A 188 ? 0.3018 0.4095 0.1348 0.0151  0.0347  0.0241  527 TYR A C   
1409 O O   . TYR A 188 ? 0.3270 0.4177 0.1425 0.0208  0.0351  0.0245  527 TYR A O   
1410 C CB  . TYR A 188 ? 0.2864 0.3999 0.1308 0.0090  0.0222  0.0186  527 TYR A CB  
1411 C CG  . TYR A 188 ? 0.3009 0.3952 0.1294 0.0100  0.0158  0.0168  527 TYR A CG  
1412 C CD1 . TYR A 188 ? 0.3448 0.4269 0.1616 0.0147  0.0130  0.0144  527 TYR A CD1 
1413 C CD2 . TYR A 188 ? 0.2923 0.3814 0.1173 0.0066  0.0122  0.0173  527 TYR A CD2 
1414 C CE1 . TYR A 188 ? 0.3638 0.4301 0.1662 0.0153  0.0059  0.0118  527 TYR A CE1 
1415 C CE2 . TYR A 188 ? 0.2998 0.3735 0.1107 0.0080  0.0046  0.0150  527 TYR A CE2 
1416 C CZ  . TYR A 188 ? 0.3455 0.4084 0.1454 0.0121  0.0010  0.0119  527 TYR A CZ  
1417 O OH  . TYR A 188 ? 0.3556 0.4046 0.1421 0.0132  -0.0078 0.0084  527 TYR A OH  
1418 N N   . ILE A 189 ? 0.2967 0.4151 0.1408 0.0096  0.0379  0.0261  528 ILE A N   
1419 C CA  . ILE A 189 ? 0.3386 0.4484 0.1747 0.0107  0.0430  0.0296  528 ILE A CA  
1420 C C   . ILE A 189 ? 0.3496 0.4545 0.1784 0.0183  0.0528  0.0328  528 ILE A C   
1421 O O   . ILE A 189 ? 0.3678 0.4565 0.1808 0.0230  0.0556  0.0350  528 ILE A O   
1422 C CB  . ILE A 189 ? 0.3075 0.4310 0.1597 0.0030  0.0471  0.0315  528 ILE A CB  
1423 C CG1 . ILE A 189 ? 0.3280 0.4556 0.1877 -0.0044 0.0379  0.0284  528 ILE A CG1 
1424 C CG2 . ILE A 189 ? 0.3596 0.4717 0.2024 0.0051  0.0531  0.0356  528 ILE A CG2 
1425 C CD1 . ILE A 189 ? 0.3539 0.4648 0.1992 -0.0034 0.0293  0.0272  528 ILE A CD1 
1426 N N   . GLU A 190 ? 0.3260 0.4446 0.1661 0.0202  0.0580  0.0334  529 GLU A N   
1427 C CA  . GLU A 190 ? 0.3385 0.4557 0.1764 0.0269  0.0689  0.0374  529 GLU A CA  
1428 C C   . GLU A 190 ? 0.3577 0.4614 0.1800 0.0349  0.0673  0.0362  529 GLU A C   
1429 O O   . GLU A 190 ? 0.3295 0.4212 0.1402 0.0415  0.0741  0.0392  529 GLU A O   
1430 C CB  . GLU A 190 ? 0.3324 0.4756 0.1956 0.0242  0.0768  0.0392  529 GLU A CB  
1431 C CG  . GLU A 190 ? 0.3644 0.5214 0.2457 0.0153  0.0800  0.0400  529 GLU A CG  
1432 C CD  . GLU A 190 ? 0.4532 0.6362 0.3629 0.0116  0.0868  0.0404  529 GLU A CD  
1433 O OE1 . GLU A 190 ? 0.4273 0.6188 0.3414 0.0175  0.0909  0.0415  529 GLU A OE1 
1434 O OE2 . GLU A 190 ? 0.5048 0.6976 0.4340 0.0027  0.0868  0.0387  529 GLU A OE2 
1435 N N   . ASN A 191 ? 0.3045 0.4090 0.1263 0.0346  0.0592  0.0322  530 ASN A N   
1436 C CA  . ASN A 191 ? 0.3174 0.4101 0.1264 0.0415  0.0587  0.0312  530 ASN A CA  
1437 C C   . ASN A 191 ? 0.3202 0.3984 0.1171 0.0403  0.0478  0.0262  530 ASN A C   
1438 O O   . ASN A 191 ? 0.3316 0.3991 0.1177 0.0454  0.0471  0.0248  530 ASN A O   
1439 C CB  . ASN A 191 ? 0.3510 0.4617 0.1746 0.0445  0.0634  0.0324  530 ASN A CB  
1440 C CG  . ASN A 191 ? 0.4227 0.5527 0.2638 0.0444  0.0739  0.0369  530 ASN A CG  
1441 O OD1 . ASN A 191 ? 0.4157 0.5668 0.2763 0.0383  0.0736  0.0364  530 ASN A OD1 
1442 N ND2 . ASN A 191 ? 0.4031 0.5262 0.2387 0.0508  0.0835  0.0411  530 ASN A ND2 
1443 N N   . GLY A 192 ? 0.3319 0.4098 0.1312 0.0338  0.0401  0.0237  531 GLY A N   
1444 C CA  . GLY A 192 ? 0.3252 0.3918 0.1164 0.0324  0.0306  0.0193  531 GLY A CA  
1445 C C   . GLY A 192 ? 0.3246 0.3978 0.1233 0.0332  0.0297  0.0177  531 GLY A C   
1446 O O   . GLY A 192 ? 0.3621 0.4235 0.1515 0.0342  0.0248  0.0146  531 GLY A O   
1447 N N   . LEU A 193 ? 0.3198 0.4120 0.1347 0.0332  0.0345  0.0197  532 LEU A N   
1448 C CA  . LEU A 193 ? 0.2847 0.3837 0.1062 0.0355  0.0340  0.0186  532 LEU A CA  
1449 C C   . LEU A 193 ? 0.2888 0.3889 0.1160 0.0300  0.0270  0.0159  532 LEU A C   
1450 O O   . LEU A 193 ? 0.2782 0.3911 0.1182 0.0245  0.0253  0.0161  532 LEU A O   
1451 C CB  . LEU A 193 ? 0.3036 0.4248 0.1410 0.0376  0.0398  0.0211  532 LEU A CB  
1452 C CG  . LEU A 193 ? 0.3106 0.4408 0.1551 0.0409  0.0384  0.0202  532 LEU A CG  
1453 C CD1 . LEU A 193 ? 0.3224 0.4365 0.1532 0.0477  0.0398  0.0199  532 LEU A CD1 
1454 C CD2 . LEU A 193 ? 0.3331 0.4888 0.1938 0.0430  0.0425  0.0220  532 LEU A CD2 
1455 N N   . ILE A 194 ? 0.2889 0.3757 0.1066 0.0317  0.0236  0.0137  533 ILE A N   
1456 C CA  . ILE A 194 ? 0.2729 0.3584 0.0940 0.0274  0.0181  0.0116  533 ILE A CA  
1457 C C   . ILE A 194 ? 0.2711 0.3628 0.0985 0.0310  0.0204  0.0120  533 ILE A C   
1458 O O   . ILE A 194 ? 0.3298 0.4124 0.1485 0.0367  0.0227  0.0116  533 ILE A O   
1459 C CB  . ILE A 194 ? 0.2937 0.3611 0.0994 0.0270  0.0129  0.0087  533 ILE A CB  
1460 C CG1 . ILE A 194 ? 0.2922 0.3537 0.0912 0.0241  0.0092  0.0082  533 ILE A CG1 
1461 C CG2 . ILE A 194 ? 0.3036 0.3717 0.1136 0.0237  0.0087  0.0072  533 ILE A CG2 
1462 C CD1 . ILE A 194 ? 0.3385 0.3826 0.1211 0.0249  0.0020  0.0042  533 ILE A CD1 
1463 N N   . THR A 195 ? 0.2531 0.3596 0.0947 0.0284  0.0198  0.0126  534 THR A N   
1464 C CA  . THR A 195 ? 0.2539 0.3658 0.1007 0.0323  0.0210  0.0128  534 THR A CA  
1465 C C   . THR A 195 ? 0.2688 0.3837 0.1226 0.0272  0.0176  0.0123  534 THR A C   
1466 O O   . THR A 195 ? 0.3092 0.4263 0.1671 0.0203  0.0145  0.0120  534 THR A O   
1467 C CB  . THR A 195 ? 0.2564 0.3862 0.1129 0.0366  0.0237  0.0140  534 THR A CB  
1468 O OG1 . THR A 195 ? 0.3182 0.4639 0.1872 0.0313  0.0213  0.0134  534 THR A OG1 
1469 C CG2 . THR A 195 ? 0.2515 0.3823 0.1041 0.0399  0.0278  0.0154  534 THR A CG2 
1470 N N   . PRO A 196 ? 0.3709 0.2788 0.1202 0.0162  0.0172  -0.0435 535 PRO A N   
1471 C CA  . PRO A 196 ? 0.3594 0.2838 0.1285 0.0088  0.0100  -0.0354 535 PRO A CA  
1472 C C   . PRO A 196 ? 0.3500 0.3092 0.1459 0.0087  0.0143  -0.0316 535 PRO A C   
1473 O O   . PRO A 196 ? 0.3604 0.3365 0.1731 0.0033  0.0088  -0.0253 535 PRO A O   
1474 C CB  . PRO A 196 ? 0.3600 0.2618 0.1201 0.0142  0.0073  -0.0353 535 PRO A CB  
1475 C CG  . PRO A 196 ? 0.4088 0.2876 0.1501 0.0292  0.0139  -0.0434 535 PRO A CG  
1476 C CD  . PRO A 196 ? 0.4128 0.2876 0.1417 0.0268  0.0179  -0.0488 535 PRO A CD  
1477 N N   . LYS A 197 ? 0.3586 0.3267 0.1575 0.0143  0.0245  -0.0357 536 LYS A N   
1478 C CA  . LYS A 197 ? 0.2958 0.2872 0.1142 0.0098  0.0291  -0.0324 536 LYS A CA  
1479 C C   . LYS A 197 ? 0.3049 0.3114 0.1303 0.0016  0.0250  -0.0267 536 LYS A C   
1480 O O   . LYS A 197 ? 0.3239 0.3395 0.1657 -0.0047 0.0241  -0.0213 536 LYS A O   
1481 C CB  . LYS A 197 ? 0.3242 0.3194 0.1440 0.0188  0.0425  -0.0379 536 LYS A CB  
1482 C CG  . LYS A 197 ? 0.3293 0.3198 0.1514 0.0369  0.0442  -0.0422 536 LYS A CG  
1483 C CD  . LYS A 197 ? 0.3536 0.3536 0.1921 0.0405  0.0371  -0.0371 536 LYS A CD  
1484 C CE  . LYS A 197 ? 0.3713 0.3721 0.2124 0.0614  0.0370  -0.0413 536 LYS A CE  
1485 N NZ  . LYS A 197 ? 0.3547 0.3676 0.2093 0.0658  0.0287  -0.0370 536 LYS A NZ  
1486 N N   . MET A 198 ? 0.3236 0.3226 0.1313 0.0031  0.0224  -0.0275 537 MET A N   
1487 C CA  . MET A 198 ? 0.3075 0.3101 0.1152 0.0022  0.0173  -0.0205 537 MET A CA  
1488 C C   . MET A 198 ? 0.2748 0.2768 0.0934 0.0015  0.0070  -0.0147 537 MET A C   
1489 O O   . MET A 198 ? 0.2943 0.2982 0.1191 0.0026  0.0044  -0.0088 537 MET A O   
1490 C CB  . MET A 198 ? 0.3088 0.2940 0.0908 -0.0002 0.0166  -0.0233 537 MET A CB  
1491 C CG  . MET A 198 ? 0.3129 0.2769 0.0820 -0.0047 0.0073  -0.0258 537 MET A CG  
1492 S SD  . MET A 198 ? 0.4910 0.4325 0.2272 -0.0082 0.0061  -0.0304 537 MET A SD  
1493 C CE  . MET A 198 ? 0.3540 0.3084 0.0914 -0.0099 0.0046  -0.0222 537 MET A CE  
1494 N N   . ASP A 199 ? 0.3215 0.3160 0.1392 -0.0009 0.0020  -0.0166 538 ASP A N   
1495 C CA  . ASP A 199 ? 0.2891 0.2856 0.1183 -0.0019 -0.0053 -0.0119 538 ASP A CA  
1496 C C   . ASP A 199 ? 0.2714 0.2759 0.1200 0.0050  -0.0024 -0.0086 538 ASP A C   
1497 O O   . ASP A 199 ? 0.2730 0.2726 0.1264 0.0040  -0.0061 -0.0048 538 ASP A O   
1498 C CB  . ASP A 199 ? 0.3056 0.2883 0.1274 -0.0084 -0.0098 -0.0138 538 ASP A CB  
1499 C CG  . ASP A 199 ? 0.3466 0.3097 0.1476 -0.0172 -0.0154 -0.0164 538 ASP A CG  
1500 O OD1 . ASP A 199 ? 0.3305 0.2940 0.1244 -0.0175 -0.0164 -0.0166 538 ASP A OD1 
1501 O OD2 . ASP A 199 ? 0.3445 0.2887 0.1331 -0.0246 -0.0194 -0.0181 538 ASP A OD2 
1502 N N   . VAL A 200 ? 0.2395 0.2548 0.0972 0.0076  0.0036  -0.0114 539 VAL A N   
1503 C CA  . VAL A 200 ? 0.2616 0.2411 0.1120 -0.0002 0.0073  -0.0085 539 VAL A CA  
1504 C C   . VAL A 200 ? 0.3040 0.2934 0.1598 0.0017  0.0094  -0.0061 539 VAL A C   
1505 O O   . VAL A 200 ? 0.3184 0.3189 0.1857 0.0002  0.0068  -0.0040 539 VAL A O   
1506 C CB  . VAL A 200 ? 0.2850 0.2814 0.1400 -0.0014 0.0140  -0.0143 539 VAL A CB  
1507 C CG1 . VAL A 200 ? 0.3261 0.3392 0.1983 0.0062  0.0158  -0.0134 539 VAL A CG1 
1508 C CG2 . VAL A 200 ? 0.2558 0.2548 0.1089 0.0000  0.0100  -0.0160 539 VAL A CG2 
1509 N N   . PHE A 201 ? 0.2656 0.2521 0.1112 0.0051  0.0143  -0.0063 540 PHE A N   
1510 C CA  . PHE A 201 ? 0.2974 0.2920 0.1437 0.0037  0.0168  -0.0027 540 PHE A CA  
1511 C C   . PHE A 201 ? 0.2984 0.2953 0.1470 0.0027  0.0074  0.0014  540 PHE A C   
1512 O O   . PHE A 201 ? 0.2844 0.2850 0.1386 -0.0004 0.0057  0.0040  540 PHE A O   
1513 C CB  . PHE A 201 ? 0.3117 0.3103 0.1468 0.0074  0.0240  -0.0027 540 PHE A CB  
1514 C CG  . PHE A 201 ? 0.3215 0.3251 0.1525 0.0023  0.0291  0.0022  540 PHE A CG  
1515 C CD1 . PHE A 201 ? 0.3190 0.3299 0.1549 -0.0019 0.0404  0.0018  540 PHE A CD1 
1516 C CD2 . PHE A 201 ? 0.2896 0.2922 0.1115 -0.0006 0.0230  0.0073  540 PHE A CD2 
1517 C CE1 . PHE A 201 ? 0.3221 0.3379 0.1562 -0.0097 0.0451  0.0073  540 PHE A CE1 
1518 C CE2 . PHE A 201 ? 0.2607 0.2619 0.0763 -0.0073 0.0271  0.0132  540 PHE A CE2 
1519 C CZ  . PHE A 201 ? 0.2752 0.2819 0.0961 -0.0123 0.0384  0.0136  540 PHE A CZ  
1520 N N   . ALA A 202 ? 0.2577 0.2563 0.1018 0.0040  0.0010  0.0011  541 ALA A N   
1521 C CA  . ALA A 202 ? 0.2513 0.2511 0.0958 0.0016  -0.0081 0.0042  541 ALA A CA  
1522 C C   . ALA A 202 ? 0.2954 0.2971 0.1533 -0.0002 -0.0118 0.0046  541 ALA A C   
1523 O O   . ALA A 202 ? 0.3006 0.3060 0.1635 -0.0013 -0.0155 0.0075  541 ALA A O   
1524 C CB  . ALA A 202 ? 0.2647 0.2658 0.1013 -0.0011 -0.0147 0.0026  541 ALA A CB  
1525 N N   . PHE A 203 ? 0.2822 0.2846 0.1466 -0.0008 -0.0107 0.0019  542 PHE A N   
1526 C CA  . PHE A 203 ? 0.2431 0.2557 0.1236 -0.0032 -0.0123 0.0026  542 PHE A CA  
1527 C C   . PHE A 203 ? 0.2943 0.3139 0.1844 -0.0027 -0.0092 0.0031  542 PHE A C   
1528 O O   . PHE A 203 ? 0.2888 0.3201 0.1902 -0.0021 -0.0118 0.0041  542 PHE A O   
1529 C CB  . PHE A 203 ? 0.2646 0.2750 0.1458 -0.0029 -0.0103 0.0004  542 PHE A CB  
1530 C CG  . PHE A 203 ? 0.2434 0.2669 0.1389 -0.0044 -0.0111 0.0014  542 PHE A CG  
1531 C CD1 . PHE A 203 ? 0.2067 0.2460 0.1117 -0.0072 -0.0150 0.0036  542 PHE A CD1 
1532 C CD2 . PHE A 203 ? 0.2453 0.2676 0.1433 -0.0024 -0.0078 0.0002  542 PHE A CD2 
1533 C CE1 . PHE A 203 ? 0.2483 0.3033 0.1648 -0.0074 -0.0138 0.0042  542 PHE A CE1 
1534 C CE2 . PHE A 203 ? 0.2498 0.2836 0.1574 -0.0026 -0.0078 0.0011  542 PHE A CE2 
1535 C CZ  . PHE A 203 ? 0.2510 0.3015 0.1676 -0.0050 -0.0098 0.0029  542 PHE A CZ  
1536 N N   . GLY A 204 ? 0.2554 0.2716 0.1410 -0.0023 -0.0032 0.0020  543 GLY A N   
1537 C CA  . GLY A 204 ? 0.2711 0.2972 0.1644 -0.0026 -0.0009 0.0022  543 GLY A CA  
1538 C C   . GLY A 204 ? 0.2918 0.3153 0.1790 -0.0031 -0.0052 0.0063  543 GLY A C   
1539 O O   . GLY A 204 ? 0.3083 0.3390 0.2018 -0.0019 -0.0077 0.0065  543 GLY A O   
1540 N N   . VAL A 205 ? 0.2680 0.2801 0.1398 -0.0031 -0.0071 0.0094  544 VAL A N   
1541 C CA  . VAL A 205 ? 0.2495 0.2568 0.1118 -0.0018 -0.0130 0.0147  544 VAL A CA  
1542 C C   . VAL A 205 ? 0.2671 0.2815 0.1390 0.0005  -0.0225 0.0151  544 VAL A C   
1543 O O   . VAL A 205 ? 0.2912 0.3071 0.1627 0.0033  -0.0277 0.0183  544 VAL A O   
1544 C CB  . VAL A 205 ? 0.2844 0.2849 0.1307 -0.0004 -0.0134 0.0183  544 VAL A CB  
1545 C CG1 . VAL A 205 ? 0.2913 0.2893 0.1282 0.0008  -0.0197 0.0261  544 VAL A CG1 
1546 C CG2 . VAL A 205 ? 0.3059 0.3055 0.1462 -0.0041 -0.0023 0.0177  544 VAL A CG2 
1547 N N   . VAL A 206 ? 0.2494 0.2713 0.1305 -0.0001 -0.0246 0.0127  545 VAL A N   
1548 C CA  . VAL A 206 ? 0.2316 0.2709 0.1270 0.0023  -0.0309 0.0134  545 VAL A CA  
1549 C C   . VAL A 206 ? 0.2644 0.3166 0.1728 0.0070  -0.0276 0.0114  545 VAL A C   
1550 O O   . VAL A 206 ? 0.3106 0.3724 0.2240 0.0143  -0.0327 0.0128  545 VAL A O   
1551 C CB  . VAL A 206 ? 0.2431 0.2909 0.1452 -0.0014 -0.0310 0.0113  545 VAL A CB  
1552 C CG1 . VAL A 206 ? 0.1488 0.2229 0.0690 0.0006  -0.0336 0.0118  545 VAL A CG1 
1553 C CG2 . VAL A 206 ? 0.2759 0.3139 0.1642 -0.0039 -0.0370 0.0122  545 VAL A CG2 
1554 N N   . ILE A 207 ? 0.2548 0.3069 0.1679 0.0053  -0.0202 0.0076  546 ILE A N   
1555 C CA  . ILE A 207 ? 0.2666 0.3281 0.1883 0.0102  -0.0178 0.0043  546 ILE A CA  
1556 C C   . ILE A 207 ? 0.2757 0.3312 0.1884 0.0144  -0.0214 0.0055  546 ILE A C   
1557 O O   . ILE A 207 ? 0.2380 0.3000 0.1533 0.0235  -0.0245 0.0033  546 ILE A O   
1558 C CB  . ILE A 207 ? 0.2292 0.2886 0.1545 0.0076  -0.0118 0.0008  546 ILE A CB  
1559 C CG1 . ILE A 207 ? 0.2141 0.2740 0.1428 0.0051  -0.0101 0.0007  546 ILE A CG1 
1560 C CG2 . ILE A 207 ? 0.2252 0.2918 0.1560 0.0122  -0.0111 -0.0034 546 ILE A CG2 
1561 C CD1 . ILE A 207 ? 0.2155 0.2724 0.1458 0.0051  -0.0066 -0.0017 546 ILE A CD1 
1562 N N   . LEU A 208 ? 0.2710 0.3119 0.1691 0.0089  -0.0207 0.0088  547 LEU A N   
1563 C CA  . LEU A 208 ? 0.2682 0.2983 0.1510 0.0116  -0.0247 0.0123  547 LEU A CA  
1564 C C   . LEU A 208 ? 0.2823 0.3072 0.1627 0.0221  -0.0345 0.0166  547 LEU A C   
1565 O O   . LEU A 208 ? 0.2922 0.3040 0.1737 0.0297  -0.0377 0.0152  547 LEU A O   
1566 C CB  . LEU A 208 ? 0.2753 0.2904 0.1420 0.0008  -0.0197 0.0174  547 LEU A CB  
1567 C CG  . LEU A 208 ? 0.2605 0.2852 0.1334 -0.0075 -0.0096 0.0128  547 LEU A CG  
1568 C CD1 . LEU A 208 ? 0.3035 0.3158 0.1628 -0.0186 -0.0021 0.0179  547 LEU A CD1 
1569 C CD2 . LEU A 208 ? 0.2774 0.3078 0.1660 -0.0065 -0.0092 0.0055  547 LEU A CD2 
1570 N N   . GLU A 209 ? 0.2648 0.2951 0.1484 0.0207  -0.0386 0.0201  548 GLU A N   
1571 C CA  . GLU A 209 ? 0.2271 0.2617 0.1153 0.0321  -0.0490 0.0234  548 GLU A CA  
1572 C C   . GLU A 209 ? 0.2574 0.3129 0.1645 0.0449  -0.0488 0.0169  548 GLU A C   
1573 O O   . GLU A 209 ? 0.2764 0.3285 0.1847 0.0606  -0.0556 0.0169  548 GLU A O   
1574 C CB  . GLU A 209 ? 0.2448 0.2858 0.1361 0.0259  -0.0540 0.0263  548 GLU A CB  
1575 C CG  . GLU A 209 ? 0.2514 0.2701 0.1197 0.0147  -0.0550 0.0316  548 GLU A CG  
1576 C CD  . GLU A 209 ? 0.2796 0.2982 0.1454 0.0129  -0.0640 0.0324  548 GLU A CD  
1577 O OE1 . GLU A 209 ? 0.2978 0.3301 0.1748 0.0198  -0.0749 0.0362  548 GLU A OE1 
1578 O OE2 . GLU A 209 ? 0.3602 0.3702 0.2167 0.0107  -0.0581 0.0272  548 GLU A OE2 
1579 N N   . LEU A 210 ? 0.2537 0.3275 0.1739 0.0395  -0.0406 0.0113  549 LEU A N   
1580 C CA  . LEU A 210 ? 0.2055 0.3014 0.1401 0.0503  -0.0382 0.0053  549 LEU A CA  
1581 C C   . LEU A 210 ? 0.2244 0.3056 0.1532 0.0594  -0.0368 -0.0006 549 LEU A C   
1582 O O   . LEU A 210 ? 0.2713 0.3594 0.2087 0.0732  -0.0368 -0.0056 549 LEU A O   
1583 C CB  . LEU A 210 ? 0.2007 0.3118 0.1444 0.0405  -0.0292 0.0025  549 LEU A CB  
1584 C CG  . LEU A 210 ? 0.2064 0.3309 0.1582 0.0322  -0.0304 0.0062  549 LEU A CG  
1585 C CD1 . LEU A 210 ? 0.1974 0.3248 0.1508 0.0220  -0.0225 0.0048  549 LEU A CD1 
1586 C CD2 . LEU A 210 ? 0.1569 0.3110 0.1251 0.0421  -0.0349 0.0065  549 LEU A CD2 
1587 N N   . LEU A 211 ? 0.2568 0.3161 0.1734 0.0503  -0.0340 -0.0014 550 LEU A N   
1588 C CA  . LEU A 211 ? 0.2759 0.3168 0.1884 0.0538  -0.0327 -0.0083 550 LEU A CA  
1589 C C   . LEU A 211 ? 0.3020 0.3132 0.2046 0.0611  -0.0395 -0.0057 550 LEU A C   
1590 O O   . LEU A 211 ? 0.3036 0.3022 0.2050 0.0724  -0.0410 -0.0124 550 LEU A O   
1591 C CB  . LEU A 211 ? 0.2113 0.2454 0.1190 0.0398  -0.0282 -0.0105 550 LEU A CB  
1592 C CG  . LEU A 211 ? 0.2111 0.2679 0.1254 0.0357  -0.0229 -0.0141 550 LEU A CG  
1593 C CD1 . LEU A 211 ? 0.1741 0.2269 0.0870 0.0244  -0.0203 -0.0159 550 LEU A CD1 
1594 C CD2 . LEU A 211 ? 0.1931 0.2597 0.1109 0.0456  -0.0214 -0.0220 550 LEU A CD2 
1595 N N   . SER A 212 ? 0.2529 0.2487 0.1446 0.0552  -0.0437 0.0039  551 SER A N   
1596 C CA  . SER A 212 ? 0.3176 0.2781 0.1941 0.0606  -0.0507 0.0088  551 SER A CA  
1597 C C   . SER A 212 ? 0.3474 0.3104 0.2248 0.0766  -0.0609 0.0150  551 SER A C   
1598 O O   . SER A 212 ? 0.3506 0.2836 0.2166 0.0877  -0.0683 0.0176  551 SER A O   
1599 C CB  . SER A 212 ? 0.3688 0.3050 0.2272 0.0430  -0.0486 0.0170  551 SER A CB  
1600 O OG  . SER A 212 ? 0.3559 0.3035 0.2088 0.0374  -0.0493 0.0253  551 SER A OG  
1601 N N   . GLY A 213 ? 0.3301 0.3264 0.2202 0.0778  -0.0627 0.0174  552 GLY A N   
1602 C CA  . GLY A 213 ? 0.3061 0.3076 0.1976 0.0901  -0.0748 0.0243  552 GLY A CA  
1603 C C   . GLY A 213 ? 0.3507 0.3196 0.2155 0.0848  -0.0829 0.0361  552 GLY A C   
1604 O O   . GLY A 213 ? 0.3306 0.3010 0.1991 0.0920  -0.0919 0.0414  552 GLY A O   
1605 N N   . ARG A 214 ? 0.3437 0.2875 0.1887 0.0674  -0.0754 0.0392  553 ARG A N   
1606 C CA  . ARG A 214 ? 0.3723 0.2817 0.1870 0.0602  -0.0800 0.0511  553 ARG A CA  
1607 C C   . ARG A 214 ? 0.3880 0.3196 0.2063 0.0488  -0.0784 0.0550  553 ARG A C   
1608 O O   . ARG A 214 ? 0.3467 0.3104 0.1818 0.0423  -0.0735 0.0497  553 ARG A O   
1609 C CB  . ARG A 214 ? 0.3792 0.2619 0.1790 0.0421  -0.0683 0.0518  553 ARG A CB  
1610 C CG  . ARG A 214 ? 0.4216 0.2829 0.2254 0.0462  -0.0667 0.0451  553 ARG A CG  
1611 C CD  . ARG A 214 ? 0.4191 0.2558 0.2098 0.0252  -0.0569 0.0467  553 ARG A CD  
1612 N NE  . ARG A 214 ? 0.5145 0.3227 0.3037 0.0271  -0.0582 0.0408  553 ARG A NE  
1613 C CZ  . ARG A 214 ? 0.5061 0.2901 0.2862 0.0081  -0.0519 0.0412  553 ARG A CZ  
1614 N NH1 . ARG A 214 ? 0.4426 0.2313 0.2168 -0.0131 -0.0419 0.0475  553 ARG A NH1 
1615 N NH2 . ARG A 214 ? 0.5228 0.2781 0.2999 0.0101  -0.0554 0.0344  553 ARG A NH2 
1616 N N   . GLU A 215 ? 0.3948 0.3054 0.1944 0.0465  -0.0830 0.0643  554 GLU A N   
1617 C CA  . GLU A 215 ? 0.3906 0.3158 0.1864 0.0365  -0.0812 0.0674  554 GLU A CA  
1618 C C   . GLU A 215 ? 0.4021 0.3279 0.1900 0.0201  -0.0657 0.0646  554 GLU A C   
1619 O O   . GLU A 215 ? 0.4114 0.3158 0.1872 0.0127  -0.0575 0.0654  554 GLU A O   
1620 C CB  . GLU A 215 ? 0.4212 0.3212 0.1950 0.0395  -0.0894 0.0775  554 GLU A CB  
1621 C CG  . GLU A 215 ? 0.4597 0.3623 0.2441 0.0579  -0.1054 0.0802  554 GLU A CG  
1622 C CD  . GLU A 215 ? 0.4691 0.4137 0.2774 0.0606  -0.1130 0.0777  554 GLU A CD  
1623 O OE1 . GLU A 215 ? 0.4329 0.4046 0.2547 0.0503  -0.1058 0.0714  554 GLU A OE1 
1624 O OE2 . GLU A 215 ? 0.4547 0.4041 0.2678 0.0720  -0.1266 0.0823  554 GLU A OE2 
1625 N N   . VAL A 216 ? 0.3908 0.3417 0.1866 0.0149  -0.0617 0.0606  555 VAL A N   
1626 C CA  . VAL A 216 ? 0.4022 0.3550 0.1936 0.0041  -0.0470 0.0561  555 VAL A CA  
1627 C C   . VAL A 216 ? 0.4516 0.3761 0.2171 -0.0043 -0.0406 0.0632  555 VAL A C   
1628 O O   . VAL A 216 ? 0.4972 0.4178 0.2595 -0.0139 -0.0274 0.0613  555 VAL A O   
1629 C CB  . VAL A 216 ? 0.4262 0.4010 0.2255 0.0042  -0.0460 0.0500  555 VAL A CB  
1630 C CG1 . VAL A 216 ? 0.3377 0.3384 0.1610 0.0106  -0.0505 0.0434  555 VAL A CG1 
1631 C CG2 . VAL A 216 ? 0.4980 0.4666 0.2816 0.0054  -0.0548 0.0554  555 VAL A CG2 
1632 N N   . VAL A 217 ? 0.4038 0.3099 0.1511 -0.0012 -0.0494 0.0716  556 VAL A N   
1633 C CA  . VAL A 217 ? 0.4597 0.3353 0.1793 -0.0094 -0.0442 0.0800  556 VAL A CA  
1634 C C   . VAL A 217 ? 0.5299 0.3770 0.2377 -0.0017 -0.0565 0.0887  556 VAL A C   
1635 O O   . VAL A 217 ? 0.5768 0.4229 0.2808 0.0085  -0.0701 0.0930  556 VAL A O   
1636 C CB  . VAL A 217 ? 0.4868 0.3628 0.1892 -0.0125 -0.0427 0.0820  556 VAL A CB  
1637 C CG1 . VAL A 217 ? 0.5766 0.4215 0.2492 -0.0215 -0.0362 0.0916  556 VAL A CG1 
1638 C CG2 . VAL A 217 ? 0.5022 0.4024 0.2161 -0.0167 -0.0318 0.0722  556 VAL A CG2 
1639 N N   . GLY A 218 ? 0.5441 0.3669 0.2462 -0.0062 -0.0524 0.0911  557 GLY A N   
1640 C CA  . GLY A 218 ? 0.5932 0.3846 0.2853 0.0036  -0.0643 0.0973  557 GLY A CA  
1641 C C   . GLY A 218 ? 0.6367 0.3912 0.2977 -0.0010 -0.0658 0.1088  557 GLY A C   
1642 O O   . GLY A 218 ? 0.7096 0.4620 0.3547 -0.0136 -0.0559 0.1125  557 GLY A O   
1643 N N   . SER A 219 ? 0.6852 0.4098 0.3370 0.0110  -0.0784 0.1142  558 SER A N   
1644 C CA  . SER A 219 ? 0.7475 0.4321 0.3678 0.0086  -0.0820 0.1258  558 SER A CA  
1645 C C   . SER A 219 ? 0.9033 0.5493 0.5069 -0.0069 -0.0721 0.1298  558 SER A C   
1646 O O   . SER A 219 ? 1.0141 0.6268 0.6113 0.0006  -0.0800 0.1315  558 SER A O   
1647 C CB  . SER A 219 ? 0.8520 0.5240 0.4713 0.0313  -0.1017 0.1295  558 SER A CB  
1648 O OG  . SER A 219 ? 0.8596 0.5716 0.4983 0.0431  -0.1110 0.1260  558 SER A OG  
1649 N N   . ASP A 227 ? 0.6717 0.3740 0.2579 -0.0630 -0.0156 0.1304  566 ASP A N   
1650 C CA  . ASP A 227 ? 0.6480 0.3920 0.2570 -0.0549 -0.0155 0.1196  566 ASP A CA  
1651 C C   . ASP A 227 ? 0.6278 0.3992 0.2630 -0.0640 -0.0010 0.1099  566 ASP A C   
1652 O O   . ASP A 227 ? 0.6575 0.4484 0.2959 -0.0726 0.0142  0.1065  566 ASP A O   
1653 C CB  . ASP A 227 ? 0.6349 0.3887 0.2279 -0.0552 -0.0120 0.1209  566 ASP A CB  
1654 C CG  . ASP A 227 ? 0.6730 0.4201 0.2536 -0.0406 -0.0310 0.1250  566 ASP A CG  
1655 O OD1 . ASP A 227 ? 0.7657 0.5037 0.3532 -0.0288 -0.0464 0.1267  566 ASP A OD1 
1656 O OD2 . ASP A 227 ? 0.6699 0.4218 0.2341 -0.0406 -0.0309 0.1260  566 ASP A OD2 
1657 N N   . GLN A 228 ? 0.5786 0.3516 0.2318 -0.0605 -0.0062 0.1052  567 GLN A N   
1658 C CA  . GLN A 228 ? 0.6282 0.4268 0.3059 -0.0684 0.0052  0.0960  567 GLN A CA  
1659 C C   . GLN A 228 ? 0.5553 0.3869 0.2557 -0.0545 -0.0010 0.0858  567 GLN A C   
1660 O O   . GLN A 228 ? 0.5357 0.3652 0.2402 -0.0403 -0.0161 0.0852  567 GLN A O   
1661 C CB  . GLN A 228 ? 0.6563 0.4330 0.3363 -0.0765 0.0043  0.0972  567 GLN A CB  
1662 C CG  . GLN A 228 ? 0.7183 0.5207 0.4212 -0.0905 0.0183  0.0893  567 GLN A CG  
1663 C CD  . GLN A 228 ? 0.8244 0.6036 0.5294 -0.1005 0.0157  0.0896  567 GLN A CD  
1664 O OE1 . GLN A 228 ? 0.8354 0.5820 0.5283 -0.0900 0.0009  0.0926  567 GLN A OE1 
1665 N NE2 . GLN A 228 ? 0.8368 0.6337 0.5598 -0.1199 0.0295  0.0854  567 GLN A NE2 
1666 N N   . LEU A 229 ? 0.5473 0.4099 0.2638 -0.0579 0.0108  0.0776  568 LEU A N   
1667 C CA  . LEU A 229 ? 0.5178 0.4100 0.2554 -0.0463 0.0064  0.0678  568 LEU A CA  
1668 C C   . LEU A 229 ? 0.4851 0.3870 0.2414 -0.0449 0.0040  0.0618  568 LEU A C   
1669 O O   . LEU A 229 ? 0.4771 0.3774 0.2373 -0.0568 0.0127  0.0611  568 LEU A O   
1670 C CB  . LEU A 229 ? 0.5216 0.4369 0.2666 -0.0481 0.0190  0.0612  568 LEU A CB  
1671 C CG  . LEU A 229 ? 0.5266 0.4323 0.2495 -0.0520 0.0253  0.0664  568 LEU A CG  
1672 C CD1 . LEU A 229 ? 0.5132 0.4408 0.2439 -0.0520 0.0388  0.0589  568 LEU A CD1 
1673 C CD2 . LEU A 229 ? 0.5107 0.4061 0.2181 -0.0431 0.0109  0.0702  568 LEU A CD2 
1674 N N   . LEU A 230 ? 0.4637 0.3783 0.2324 -0.0316 -0.0076 0.0574  569 LEU A N   
1675 C CA  . LEU A 230 ? 0.4547 0.3790 0.2386 -0.0283 -0.0109 0.0513  569 LEU A CA  
1676 C C   . LEU A 230 ? 0.4212 0.3714 0.2231 -0.0344 0.0009  0.0424  569 LEU A C   
1677 O O   . LEU A 230 ? 0.4081 0.3676 0.2254 -0.0347 0.0007  0.0364  569 LEU A O   
1678 C CB  . LEU A 230 ? 0.4100 0.3485 0.2066 -0.0128 -0.0239 0.0480  569 LEU A CB  
1679 C CG  . LEU A 230 ? 0.3892 0.3365 0.2002 -0.0057 -0.0290 0.0416  569 LEU A CG  
1680 C CD1 . LEU A 230 ? 0.4230 0.3454 0.2327 -0.0053 -0.0308 0.0426  569 LEU A CD1 
1681 C CD2 . LEU A 230 ? 0.3765 0.3418 0.2014 0.0083  -0.0398 0.0396  569 LEU A CD2 
1682 N N   . ALA A 231 ? 0.4199 0.3830 0.2258 -0.0358 0.0103  0.0397  570 ALA A N   
1683 C CA  . ALA A 231 ? 0.3809 0.3673 0.2050 -0.0377 0.0204  0.0312  570 ALA A CA  
1684 C C   . ALA A 231 ? 0.4353 0.4254 0.2615 -0.0529 0.0334  0.0321  570 ALA A C   
1685 O O   . ALA A 231 ? 0.4307 0.4453 0.2767 -0.0544 0.0406  0.0247  570 ALA A O   
1686 C CB  . ALA A 231 ? 0.3474 0.3408 0.1720 -0.0302 0.0240  0.0277  570 ALA A CB  
1687 N N   . SER A 232 ? 0.4402 0.4079 0.2489 -0.0643 0.0364  0.0411  571 SER A N   
1688 C CA  . SER A 232 ? 0.4818 0.4537 0.2967 -0.0822 0.0492  0.0424  571 SER A CA  
1689 C C   . SER A 232 ? 0.4913 0.4489 0.3127 -0.0899 0.0424  0.0430  571 SER A C   
1690 O O   . SER A 232 ? 0.5585 0.5267 0.3976 -0.1042 0.0500  0.0405  571 SER A O   
1691 C CB  . SER A 232 ? 0.4581 0.4138 0.2556 -0.0900 0.0577  0.0508  571 SER A CB  
1692 O OG  . SER A 232 ? 0.6718 0.5899 0.4431 -0.0908 0.0478  0.0610  571 SER A OG  
1693 N N   . THR A 233 ? 0.4591 0.3949 0.2728 -0.0780 0.0268  0.0442  572 THR A N   
1694 C CA  . THR A 233 ? 0.5157 0.4330 0.3368 -0.0801 0.0186  0.0420  572 THR A CA  
1695 C C   . THR A 233 ? 0.4905 0.4366 0.3435 -0.0757 0.0158  0.0284  572 THR A C   
1696 O O   . THR A 233 ? 0.4909 0.4316 0.3549 -0.0852 0.0142  0.0239  572 THR A O   
1697 C CB  . THR A 233 ? 0.5470 0.4330 0.3494 -0.0653 0.0037  0.0468  572 THR A CB  
1698 O OG1 . THR A 233 ? 0.5798 0.4880 0.3934 -0.0469 -0.0037 0.0406  572 THR A OG1 
1699 C CG2 . THR A 233 ? 0.4825 0.3377 0.2498 -0.0686 0.0036  0.0613  572 THR A CG2 
1700 N N   . VAL A 234 ? 0.4588 0.4325 0.3240 -0.0624 0.0145  0.0220  573 VAL A N   
1701 C CA  . VAL A 234 ? 0.4539 0.4519 0.3440 -0.0566 0.0107  0.0105  573 VAL A CA  
1702 C C   . VAL A 234 ? 0.4262 0.4462 0.3372 -0.0708 0.0184  0.0056  573 VAL A C   
1703 O O   . VAL A 234 ? 0.3970 0.4282 0.3256 -0.0711 0.0126  -0.0031 573 VAL A O   
1704 C CB  . VAL A 234 ? 0.4137 0.4333 0.3085 -0.0421 0.0092  0.0069  573 VAL A CB  
1705 C CG1 . VAL A 234 ? 0.4005 0.4361 0.2936 -0.0455 0.0201  0.0088  573 VAL A CG1 
1706 C CG2 . VAL A 234 ? 0.3774 0.4164 0.2915 -0.0353 0.0043  -0.0032 573 VAL A CG2 
1707 N N   . ASN A 235 ? 0.4725 0.5015 0.3824 -0.0824 0.0314  0.0106  574 ASN A N   
1708 C CA  . ASN A 235 ? 0.4777 0.5347 0.4129 -0.0964 0.0398  0.0061  574 ASN A CA  
1709 C C   . ASN A 235 ? 0.5602 0.5988 0.4981 -0.1148 0.0367  0.0069  574 ASN A C   
1710 O O   . ASN A 235 ? 0.4874 0.5464 0.4506 -0.1224 0.0332  -0.0015 574 ASN A O   
1711 C CB  . ASN A 235 ? 0.5099 0.5828 0.4424 -0.1035 0.0572  0.0110  574 ASN A CB  
1712 C CG  . ASN A 235 ? 0.4990 0.5780 0.4195 -0.0863 0.0594  0.0105  574 ASN A CG  
1713 O OD1 . ASN A 235 ? 0.5206 0.6138 0.4521 -0.0713 0.0521  0.0033  574 ASN A OD1 
1714 N ND2 . ASN A 235 ? 0.4887 0.5537 0.3833 -0.0894 0.0689  0.0184  574 ASN A ND2 
1715 N N   . GLN A 236 ? 0.4632 0.4609 0.3736 -0.1224 0.0364  0.0169  575 GLN A N   
1716 C CA  . GLN A 236 ? 0.5124 0.4822 0.4194 -0.1403 0.0324  0.0182  575 GLN A CA  
1717 C C   . GLN A 236 ? 0.5200 0.4754 0.4303 -0.1300 0.0157  0.0082  575 GLN A C   
1718 O O   . GLN A 236 ? 0.5607 0.5079 0.4798 -0.1444 0.0107  0.0025  575 GLN A O   
1719 C CB  . GLN A 236 ? 0.5770 0.4997 0.4478 -0.1479 0.0350  0.0327  575 GLN A CB  
1720 C CG  . GLN A 236 ? 0.6569 0.5891 0.5155 -0.1566 0.0520  0.0431  575 GLN A CG  
1721 C CD  . GLN A 236 ? 0.7317 0.6159 0.5471 -0.1557 0.0506  0.0580  575 GLN A CD  
1722 O OE1 . GLN A 236 ? 0.7556 0.5959 0.5520 -0.1542 0.0387  0.0620  575 GLN A OE1 
1723 N NE2 . GLN A 236 ? 0.6928 0.5833 0.4903 -0.1548 0.0616  0.0656  575 GLN A NE2 
1724 N N   . VAL A 237 ? 0.4794 0.4323 0.3823 -0.1062 0.0075  0.0053  576 VAL A N   
1725 C CA  . VAL A 237 ? 0.4475 0.3876 0.3505 -0.0944 -0.0058 -0.0046 576 VAL A CA  
1726 C C   . VAL A 237 ? 0.4774 0.4524 0.4068 -0.0957 -0.0093 -0.0173 576 VAL A C   
1727 O O   . VAL A 237 ? 0.5208 0.4837 0.4511 -0.0973 -0.0191 -0.0266 576 VAL A O   
1728 C CB  . VAL A 237 ? 0.3916 0.3255 0.2821 -0.0698 -0.0113 -0.0035 576 VAL A CB  
1729 C CG1 . VAL A 237 ? 0.3733 0.3058 0.2674 -0.0561 -0.0214 -0.0154 576 VAL A CG1 
1730 C CG2 . VAL A 237 ? 0.4131 0.3076 0.2767 -0.0666 -0.0133 0.0078  576 VAL A CG2 
1731 N N   . LEU A 238 ? 0.4064 0.4226 0.3552 -0.0938 -0.0025 -0.0182 577 LEU A N   
1732 C CA  . LEU A 238 ? 0.4068 0.4573 0.3794 -0.0912 -0.0076 -0.0291 577 LEU A CA  
1733 C C   . LEU A 238 ? 0.4424 0.5199 0.4412 -0.1118 -0.0036 -0.0318 577 LEU A C   
1734 O O   . LEU A 238 ? 0.4286 0.5354 0.4490 -0.1107 -0.0106 -0.0412 577 LEU A O   
1735 C CB  . LEU A 238 ? 0.3685 0.4461 0.3463 -0.0731 -0.0048 -0.0293 577 LEU A CB  
1736 C CG  . LEU A 238 ? 0.3529 0.4125 0.3107 -0.0546 -0.0091 -0.0275 577 LEU A CG  
1737 C CD1 . LEU A 238 ? 0.3956 0.4794 0.3581 -0.0405 -0.0072 -0.0281 577 LEU A CD1 
1738 C CD2 . LEU A 238 ? 0.2953 0.3362 0.2451 -0.0490 -0.0202 -0.0352 577 LEU A CD2 
1739 N N   . GLU A 239 ? 0.4624 0.5326 0.4599 -0.1306 0.0073  -0.0236 578 GLU A N   
1740 C CA  . GLU A 239 ? 0.4188 0.5184 0.4443 -0.1532 0.0133  -0.0255 578 GLU A CA  
1741 C C   . GLU A 239 ? 0.4489 0.5235 0.4736 -0.1738 0.0033  -0.0300 578 GLU A C   
1742 O O   . GLU A 239 ? 0.5194 0.5487 0.5180 -0.1692 -0.0066 -0.0311 578 GLU A O   
1743 C CB  . GLU A 239 ? 0.4753 0.5802 0.4980 -0.1658 0.0326  -0.0140 578 GLU A CB  
1744 C CG  . GLU A 239 ? 0.6092 0.6623 0.5998 -0.1804 0.0357  -0.0028 578 GLU A CG  
1745 C CD  . GLU A 239 ? 0.7938 0.8517 0.7778 -0.1954 0.0558  0.0092  578 GLU A CD  
1746 O OE1 . GLU A 239 ? 0.9275 1.0177 0.9191 -0.1848 0.0672  0.0097  578 GLU A OE1 
1747 O OE2 . GLU A 239 ? 0.7134 0.7397 0.6814 -0.2180 0.0606  0.0180  578 GLU A OE2 
1748 N N   . GLY A 240 ? 0.4859 0.5913 0.5406 -0.1968 0.0060  -0.0333 579 GLY A N   
1749 C CA  . GLY A 240 ? 0.5576 0.6394 0.6126 -0.2220 -0.0028 -0.0374 579 GLY A CA  
1750 C C   . GLY A 240 ? 0.5483 0.6076 0.5926 -0.2120 -0.0238 -0.0503 579 GLY A C   
1751 O O   . GLY A 240 ? 0.4986 0.5781 0.5475 -0.1894 -0.0323 -0.0582 579 GLY A O   
1752 N N   . ASP A 241 ? 0.6415 0.6546 0.6679 -0.2300 -0.0317 -0.0524 580 ASP A N   
1753 C CA  . ASP A 241 ? 0.7126 0.6981 0.7250 -0.2242 -0.0509 -0.0662 580 ASP A CA  
1754 C C   . ASP A 241 ? 0.8050 0.7312 0.7747 -0.2043 -0.0540 -0.0640 580 ASP A C   
1755 O O   . ASP A 241 ? 0.7405 0.6420 0.6914 -0.1992 -0.0435 -0.0509 580 ASP A O   
1756 C CB  . ASP A 241 ? 0.8054 0.7785 0.8283 -0.2451 -0.0575 -0.0699 580 ASP A CB  
1757 C CG  . ASP A 241 ? 0.8990 0.9316 0.9678 -0.2582 -0.0524 -0.0687 580 ASP A CG  
1758 O OD1 . ASP A 241 ? 0.8216 0.9054 0.9156 -0.2440 -0.0539 -0.0728 580 ASP A OD1 
1759 O OD2 . ASP A 241 ? 0.8583 0.8852 0.9371 -0.2812 -0.0469 -0.0633 580 ASP A OD2 
1760 N N   . ASN A 242 ? 0.9378 0.8427 0.8920 -0.1916 -0.0690 -0.0776 581 ASN A N   
1761 C CA  . ASN A 242 ? 0.8434 0.6971 0.7608 -0.1693 -0.0724 -0.0786 581 ASN A CA  
1762 C C   . ASN A 242 ? 0.7054 0.5768 0.6197 -0.1410 -0.0632 -0.0701 581 ASN A C   
1763 O O   . ASN A 242 ? 0.7555 0.5931 0.6470 -0.1277 -0.0596 -0.0624 581 ASN A O   
1764 C CB  . ASN A 242 ? 0.8261 0.6177 0.7171 -0.1836 -0.0714 -0.0714 581 ASN A CB  
1765 C CG  . ASN A 242 ? 1.0632 0.8358 0.9579 -0.2087 -0.0796 -0.0788 581 ASN A CG  
1766 O OD1 . ASN A 242 ? 1.2882 1.0579 1.1923 -0.2322 -0.0722 -0.0689 581 ASN A OD1 
1767 N ND2 . ASN A 242 ? 1.2210 0.9866 1.1109 -0.1989 -0.0924 -0.0951 581 ASN A ND2 
1768 N N   . VAL A 243 ? 0.5983 0.5225 0.5356 -0.1318 -0.0606 -0.0715 582 VAL A N   
1769 C CA  . VAL A 243 ? 0.5561 0.4978 0.4913 -0.1084 -0.0523 -0.0639 582 VAL A CA  
1770 C C   . VAL A 243 ? 0.5306 0.4461 0.4416 -0.0838 -0.0573 -0.0688 582 VAL A C   
1771 O O   . VAL A 243 ? 0.5085 0.4182 0.4100 -0.0680 -0.0512 -0.0605 582 VAL A O   
1772 C CB  . VAL A 243 ? 0.4687 0.4656 0.4301 -0.1034 -0.0503 -0.0657 582 VAL A CB  
1773 C CG1 . VAL A 243 ? 0.3852 0.3945 0.3412 -0.0812 -0.0430 -0.0587 582 VAL A CG1 
1774 C CG2 . VAL A 243 ? 0.4794 0.5073 0.4682 -0.1248 -0.0428 -0.0608 582 VAL A CG2 
1775 N N   . ARG A 244 ? 0.5060 0.4074 0.4068 -0.0802 -0.0682 -0.0829 583 ARG A N   
1776 C CA  . ARG A 244 ? 0.4935 0.3736 0.3720 -0.0558 -0.0706 -0.0890 583 ARG A CA  
1777 C C   . ARG A 244 ? 0.4816 0.3162 0.3397 -0.0490 -0.0685 -0.0829 583 ARG A C   
1778 O O   . ARG A 244 ? 0.5175 0.3518 0.3688 -0.0276 -0.0640 -0.0784 583 ARG A O   
1779 C CB  . ARG A 244 ? 0.5278 0.3962 0.3940 -0.0547 -0.0824 -0.1065 583 ARG A CB  
1780 C CG  . ARG A 244 ? 0.5635 0.4747 0.4407 -0.0490 -0.0856 -0.1122 583 ARG A CG  
1781 C CD  . ARG A 244 ? 0.5840 0.4819 0.4438 -0.0464 -0.0965 -0.1285 583 ARG A CD  
1782 N NE  . ARG A 244 ? 0.6551 0.5478 0.5239 -0.0703 -0.1058 -0.1350 583 ARG A NE  
1783 C CZ  . ARG A 244 ? 0.6975 0.5872 0.5589 -0.0729 -0.1121 -0.1460 583 ARG A CZ  
1784 N NH1 . ARG A 244 ? 0.6969 0.5845 0.5385 -0.0545 -0.1096 -0.1501 583 ARG A NH1 
1785 N NH2 . ARG A 244 ? 0.6668 0.5562 0.5416 -0.0954 -0.1208 -0.1522 583 ARG A NH2 
1786 N N   . GLU A 245 ? 0.5236 0.3192 0.3718 -0.0674 -0.0724 -0.0822 584 GLU A N   
1787 C CA  . GLU A 245 ? 0.5483 0.2938 0.3732 -0.0599 -0.0724 -0.0756 584 GLU A CA  
1788 C C   . GLU A 245 ? 0.5267 0.2838 0.3564 -0.0568 -0.0630 -0.0575 584 GLU A C   
1789 O O   . GLU A 245 ? 0.4982 0.2383 0.3150 -0.0359 -0.0628 -0.0522 584 GLU A O   
1790 C CB  . GLU A 245 ? 0.5456 0.2415 0.3556 -0.0835 -0.0789 -0.0778 584 GLU A CB  
1791 C CG  . GLU A 245 ? 0.5895 0.2480 0.3789 -0.0785 -0.0905 -0.0964 584 GLU A CG  
1792 C CD  . GLU A 245 ? 0.7268 0.3595 0.4943 -0.0440 -0.0915 -0.1017 584 GLU A CD  
1793 O OE1 . GLU A 245 ? 0.6609 0.3018 0.4304 -0.0264 -0.0849 -0.0896 584 GLU A OE1 
1794 O OE2 . GLU A 245 ? 0.8686 0.4816 0.6218 -0.0337 -0.0971 -0.1167 584 GLU A OE2 
1795 N N   . LYS A 246 ? 0.4909 0.2780 0.3389 -0.0764 -0.0557 -0.0485 585 LYS A N   
1796 C CA  . LYS A 246 ? 0.4574 0.2536 0.3053 -0.0742 -0.0468 -0.0324 585 LYS A CA  
1797 C C   . LYS A 246 ? 0.4857 0.3139 0.3403 -0.0494 -0.0444 -0.0316 585 LYS A C   
1798 O O   . LYS A 246 ? 0.4890 0.3123 0.3353 -0.0396 -0.0417 -0.0207 585 LYS A O   
1799 C CB  . LYS A 246 ? 0.4492 0.2744 0.3152 -0.0990 -0.0374 -0.0254 585 LYS A CB  
1800 C CG  . LYS A 246 ? 0.5151 0.3088 0.3745 -0.1276 -0.0373 -0.0223 585 LYS A CG  
1801 C CD  . LYS A 246 ? 0.6293 0.4540 0.5061 -0.1508 -0.0242 -0.0129 585 LYS A CD  
1802 C CE  . LYS A 246 ? 0.6375 0.5200 0.5502 -0.1568 -0.0227 -0.0229 585 LYS A CE  
1803 N NZ  . LYS A 246 ? 0.5991 0.5131 0.5319 -0.1800 -0.0090 -0.0155 585 LYS A NZ  
1804 N N   . LEU A 247 ? 0.4612 0.3207 0.3289 -0.0403 -0.0460 -0.0426 586 LEU A N   
1805 C CA  . LEU A 247 ? 0.4115 0.2998 0.2850 -0.0198 -0.0431 -0.0416 586 LEU A CA  
1806 C C   . LEU A 247 ? 0.4238 0.2909 0.2833 0.0030  -0.0473 -0.0452 586 LEU A C   
1807 O O   . LEU A 247 ? 0.3860 0.2642 0.2467 0.0172  -0.0451 -0.0384 586 LEU A O   
1808 C CB  . LEU A 247 ? 0.4102 0.3364 0.2990 -0.0189 -0.0429 -0.0503 586 LEU A CB  
1809 C CG  . LEU A 247 ? 0.3910 0.3427 0.2826 0.0002  -0.0401 -0.0508 586 LEU A CG  
1810 C CD1 . LEU A 247 ? 0.3847 0.3441 0.2777 0.0054  -0.0348 -0.0384 586 LEU A CD1 
1811 C CD2 . LEU A 247 ? 0.3940 0.3794 0.2981 -0.0026 -0.0396 -0.0553 586 LEU A CD2 
1812 N N   . ARG A 248 ? 0.4088 0.2468 0.2556 0.0072  -0.0536 -0.0567 587 ARG A N   
1813 C CA  . ARG A 248 ? 0.4324 0.2476 0.2656 0.0310  -0.0566 -0.0610 587 ARG A CA  
1814 C C   . ARG A 248 ? 0.4190 0.2095 0.2434 0.0370  -0.0580 -0.0478 587 ARG A C   
1815 O O   . ARG A 248 ? 0.4548 0.2572 0.2824 0.0574  -0.0576 -0.0441 587 ARG A O   
1816 C CB  . ARG A 248 ? 0.4696 0.2463 0.2848 0.0326  -0.0634 -0.0758 587 ARG A CB  
1817 C CG  . ARG A 248 ? 0.5042 0.3019 0.3202 0.0388  -0.0635 -0.0911 587 ARG A CG  
1818 C CD  . ARG A 248 ? 0.6545 0.4096 0.4462 0.0511  -0.0694 -0.1067 587 ARG A CD  
1819 N NE  . ARG A 248 ? 0.6881 0.4503 0.4729 0.0468  -0.0727 -0.1223 587 ARG A NE  
1820 C CZ  . ARG A 248 ? 0.7494 0.5384 0.5350 0.0630  -0.0668 -0.1284 587 ARG A CZ  
1821 N NH1 . ARG A 248 ? 0.7404 0.5499 0.5318 0.0849  -0.0581 -0.1245 587 ARG A NH1 
1822 N NH2 . ARG A 248 ? 0.7806 0.5797 0.5641 0.0548  -0.0684 -0.1362 587 ARG A NH2 
1823 N N   . GLY A 249 ? 0.4467 0.2036 0.2595 0.0186  -0.0601 -0.0401 588 GLY A N   
1824 C CA  . GLY A 249 ? 0.4805 0.2100 0.2794 0.0229  -0.0624 -0.0257 588 GLY A CA  
1825 C C   . GLY A 249 ? 0.4608 0.2278 0.2716 0.0252  -0.0575 -0.0137 588 GLY A C   
1826 O O   . GLY A 249 ? 0.5184 0.2745 0.3205 0.0385  -0.0616 -0.0041 588 GLY A O   
1827 N N   . PHE A 250 ? 0.4227 0.2324 0.2521 0.0130  -0.0501 -0.0145 589 PHE A N   
1828 C CA  . PHE A 250 ? 0.4154 0.2578 0.2536 0.0147  -0.0457 -0.0051 589 PHE A CA  
1829 C C   . PHE A 250 ? 0.4271 0.2971 0.2763 0.0371  -0.0476 -0.0088 589 PHE A C   
1830 O O   . PHE A 250 ? 0.4575 0.3432 0.3090 0.0430  -0.0483 -0.0005 589 PHE A O   
1831 C CB  . PHE A 250 ? 0.3958 0.2712 0.2488 -0.0033 -0.0372 -0.0058 589 PHE A CB  
1832 C CG  . PHE A 250 ? 0.3769 0.2796 0.2345 -0.0029 -0.0324 0.0025  589 PHE A CG  
1833 C CD1 . PHE A 250 ? 0.4041 0.2910 0.2462 -0.0096 -0.0310 0.0150  589 PHE A CD1 
1834 C CD2 . PHE A 250 ? 0.3404 0.2806 0.2138 0.0033  -0.0295 -0.0022 589 PHE A CD2 
1835 C CE1 . PHE A 250 ? 0.4078 0.3166 0.2502 -0.0095 -0.0274 0.0210  589 PHE A CE1 
1836 C CE2 . PHE A 250 ? 0.3248 0.2847 0.1995 0.0026  -0.0260 0.0042  589 PHE A CE2 
1837 C CZ  . PHE A 250 ? 0.3514 0.2960 0.2106 -0.0036 -0.0252 0.0150  589 PHE A CZ  
1838 N N   . MET A 251 ? 0.4062 0.2831 0.2615 0.0486  -0.0481 -0.0214 590 MET A N   
1839 C CA  . MET A 251 ? 0.4049 0.3133 0.2729 0.0673  -0.0469 -0.0252 590 MET A CA  
1840 C C   . MET A 251 ? 0.3994 0.2970 0.2642 0.0871  -0.0534 -0.0201 590 MET A C   
1841 O O   . MET A 251 ? 0.4071 0.2640 0.2560 0.0935  -0.0598 -0.0190 590 MET A O   
1842 C CB  . MET A 251 ? 0.3656 0.2802 0.2356 0.0750  -0.0446 -0.0399 590 MET A CB  
1843 C CG  . MET A 251 ? 0.3546 0.2891 0.2304 0.0594  -0.0403 -0.0447 590 MET A CG  
1844 S SD  . MET A 251 ? 0.3261 0.3037 0.2176 0.0527  -0.0342 -0.0357 590 MET A SD  
1845 C CE  . MET A 251 ? 0.2807 0.2854 0.1811 0.0727  -0.0312 -0.0380 590 MET A CE  
1846 N N   . ASP A 252 ? 0.3477 0.2819 0.2283 0.0966  -0.0525 -0.0170 591 ASP A N   
1847 C CA  . ASP A 252 ? 0.3612 0.2973 0.2458 0.1166  -0.0599 -0.0124 591 ASP A CA  
1848 C C   . ASP A 252 ? 0.4359 0.3510 0.3164 0.1389  -0.0624 -0.0225 591 ASP A C   
1849 O O   . ASP A 252 ? 0.4206 0.3531 0.3090 0.1461  -0.0553 -0.0346 591 ASP A O   
1850 C CB  . ASP A 252 ? 0.3410 0.3280 0.2488 0.1209  -0.0574 -0.0110 591 ASP A CB  
1851 C CG  . ASP A 252 ? 0.3354 0.3327 0.2519 0.1384  -0.0673 -0.0045 591 ASP A CG  
1852 O OD1 . ASP A 252 ? 0.3298 0.3020 0.2399 0.1575  -0.0743 -0.0059 591 ASP A OD1 
1853 O OD2 . ASP A 252 ? 0.3739 0.4034 0.3034 0.1333  -0.0694 0.0016  591 ASP A OD2 
1854 N N   . PRO A 253 ? 0.4206 0.2960 0.2858 0.1510  -0.0721 -0.0180 592 PRO A N   
1855 C CA  . PRO A 253 ? 0.4304 0.2816 0.2897 0.1755  -0.0748 -0.0288 592 PRO A CA  
1856 C C   . PRO A 253 ? 0.4367 0.3344 0.3216 0.1994  -0.0703 -0.0369 592 PRO A C   
1857 O O   . PRO A 253 ? 0.5366 0.4291 0.4197 0.2152  -0.0652 -0.0510 592 PRO A O   
1858 C CB  . PRO A 253 ? 0.4785 0.2826 0.3178 0.1855  -0.0880 -0.0183 592 PRO A CB  
1859 C CG  . PRO A 253 ? 0.4729 0.2628 0.2984 0.1578  -0.0892 -0.0042 592 PRO A CG  
1860 C CD  . PRO A 253 ? 0.4154 0.2611 0.2632 0.1432  -0.0810 -0.0030 592 PRO A CD  
1861 N N   . ASN A 254 ? 0.4309 0.3747 0.3390 0.2013  -0.0715 -0.0290 593 ASN A N   
1862 C CA  . ASN A 254 ? 0.3769 0.3702 0.3133 0.2142  -0.0647 -0.0348 593 ASN A CA  
1863 C C   . ASN A 254 ? 0.3777 0.4014 0.3228 0.2101  -0.0499 -0.0460 593 ASN A C   
1864 O O   . ASN A 254 ? 0.3932 0.4496 0.3556 0.2182  -0.0415 -0.0518 593 ASN A O   
1865 C CB  . ASN A 254 ? 0.3531 0.3867 0.3117 0.2074  -0.0691 -0.0236 593 ASN A CB  
1866 C CG  . ASN A 254 ? 0.4253 0.4330 0.3757 0.2131  -0.0834 -0.0131 593 ASN A CG  
1867 O OD1 . ASN A 254 ? 0.4196 0.3925 0.3575 0.2287  -0.0884 -0.0155 593 ASN A OD1 
1868 N ND2 . ASN A 254 ? 0.4487 0.4707 0.4033 0.1995  -0.0900 -0.0015 593 ASN A ND2 
1869 N N   . LEU A 255 ? 0.3878 0.4008 0.3198 0.1921  -0.0456 -0.0477 594 LEU A N   
1870 C CA  . LEU A 255 ? 0.3723 0.4071 0.3061 0.1877  -0.0325 -0.0582 594 LEU A CA  
1871 C C   . LEU A 255 ? 0.4290 0.4371 0.3471 0.2013  -0.0291 -0.0722 594 LEU A C   
1872 O O   . LEU A 255 ? 0.4428 0.4750 0.3658 0.2018  -0.0185 -0.0786 594 LEU A O   
1873 C CB  . LEU A 255 ? 0.3682 0.3964 0.2910 0.1597  -0.0304 -0.0549 594 LEU A CB  
1874 C CG  . LEU A 255 ? 0.2996 0.3576 0.2360 0.1424  -0.0304 -0.0427 594 LEU A CG  
1875 C CD1 . LEU A 255 ? 0.3077 0.3504 0.2315 0.1190  -0.0302 -0.0398 594 LEU A CD1 
1876 C CD2 . LEU A 255 ? 0.2723 0.3793 0.2284 0.1442  -0.0207 -0.0438 594 LEU A CD2 
1877 N N   . ARG A 256 ? 0.4539 0.4090 0.3508 0.2076  -0.0383 -0.0748 595 ARG A N   
1878 C CA  . ARG A 256 ? 0.5074 0.4326 0.3884 0.2180  -0.0373 -0.0863 595 ARG A CA  
1879 C C   . ARG A 256 ? 0.5122 0.4385 0.3812 0.2070  -0.0290 -0.0972 595 ARG A C   
1880 O O   . ARG A 256 ? 0.5733 0.5148 0.4442 0.2146  -0.0207 -0.1046 595 ARG A O   
1881 C CB  . ARG A 256 ? 0.5527 0.5034 0.4514 0.2381  -0.0337 -0.0873 595 ARG A CB  
1882 C CG  . ARG A 256 ? 0.5718 0.5058 0.4744 0.2512  -0.0452 -0.0788 595 ARG A CG  
1883 C CD  . ARG A 256 ? 0.8074 0.7666 0.7284 0.2723  -0.0413 -0.0824 595 ARG A CD  
1884 N NE  . ARG A 256 ? 0.9281 0.8949 0.8455 0.2782  -0.0291 -0.0957 595 ARG A NE  
1885 C CZ  . ARG A 256 ? 0.9202 0.9376 0.8602 0.2816  -0.0164 -0.0985 595 ARG A CZ  
1886 N NH1 . ARG A 256 ? 0.9899 1.0561 0.9601 0.2792  -0.0148 -0.0898 595 ARG A NH1 
1887 N NH2 . ARG A 256 ? 0.8199 0.8372 0.7509 0.2859  -0.0053 -0.1102 595 ARG A NH2 
1888 N N   . ASP A 257 ? 0.4865 0.3966 0.3428 0.1879  -0.0319 -0.0979 596 ASP A N   
1889 C CA  . ASP A 257 ? 0.4924 0.3997 0.3359 0.1744  -0.0280 -0.1067 596 ASP A CA  
1890 C C   . ASP A 257 ? 0.4149 0.3725 0.2731 0.1698  -0.0165 -0.1044 596 ASP A C   
1891 O O   . ASP A 257 ? 0.4448 0.4044 0.2942 0.1570  -0.0141 -0.1081 596 ASP A O   
1892 C CB  . ASP A 257 ? 0.5149 0.3872 0.3400 0.1832  -0.0295 -0.1180 596 ASP A CB  
1893 C CG  . ASP A 257 ? 0.7493 0.5626 0.5534 0.1781  -0.0417 -0.1202 596 ASP A CG  
1894 O OD1 . ASP A 257 ? 0.7931 0.5909 0.5980 0.1735  -0.0485 -0.1114 596 ASP A OD1 
1895 O OD2 . ASP A 257 ? 0.9249 0.7054 0.7103 0.1769  -0.0443 -0.1303 596 ASP A OD2 
1896 N N   . GLU A 258 ? 0.3706 0.3673 0.2511 0.1783  -0.0103 -0.0972 597 GLU A N   
1897 C CA  . GLU A 258 ? 0.3679 0.4077 0.2614 0.1716  0.0008  -0.0936 597 GLU A CA  
1898 C C   . GLU A 258 ? 0.3461 0.4042 0.2454 0.1524  0.0004  -0.0844 597 GLU A C   
1899 O O   . GLU A 258 ? 0.3213 0.4123 0.2390 0.1488  0.0039  -0.0755 597 GLU A O   
1900 C CB  . GLU A 258 ? 0.3581 0.4322 0.2742 0.1851  0.0073  -0.0902 597 GLU A CB  
1901 C CG  . GLU A 258 ? 0.4265 0.4931 0.3383 0.2026  0.0126  -0.1000 597 GLU A CG  
1902 C CD  . GLU A 258 ? 0.3721 0.4811 0.3103 0.2129  0.0212  -0.0969 597 GLU A CD  
1903 O OE1 . GLU A 258 ? 0.3410 0.4876 0.2964 0.2009  0.0269  -0.0886 597 GLU A OE1 
1904 O OE2 . GLU A 258 ? 0.4039 0.5078 0.3460 0.2322  0.0219  -0.1028 597 GLU A OE2 
1905 N N   . TYR A 259 ? 0.3020 0.3376 0.1857 0.1386  -0.0045 -0.0868 598 TYR A N   
1906 C CA  . TYR A 259 ? 0.3055 0.3549 0.1937 0.1200  -0.0053 -0.0784 598 TYR A CA  
1907 C C   . TYR A 259 ? 0.3012 0.3299 0.1748 0.1072  -0.0099 -0.0830 598 TYR A C   
1908 O O   . TYR A 259 ? 0.3042 0.3019 0.1631 0.1097  -0.0160 -0.0925 598 TYR A O   
1909 C CB  . TYR A 259 ? 0.3151 0.3628 0.2080 0.1173  -0.0109 -0.0726 598 TYR A CB  
1910 C CG  . TYR A 259 ? 0.3004 0.3078 0.1821 0.1125  -0.0209 -0.0746 598 TYR A CG  
1911 C CD1 . TYR A 259 ? 0.3092 0.3040 0.1844 0.0941  -0.0257 -0.0744 598 TYR A CD1 
1912 C CD2 . TYR A 259 ? 0.3190 0.3013 0.1981 0.1254  -0.0257 -0.0756 598 TYR A CD2 
1913 C CE1 . TYR A 259 ? 0.3350 0.2953 0.2024 0.0856  -0.0335 -0.0750 598 TYR A CE1 
1914 C CE2 . TYR A 259 ? 0.3476 0.2885 0.2141 0.1178  -0.0344 -0.0754 598 TYR A CE2 
1915 C CZ  . TYR A 259 ? 0.3180 0.2490 0.1792 0.0962  -0.0375 -0.0750 598 TYR A CZ  
1916 O OH  . TYR A 259 ? 0.3774 0.2695 0.2276 0.0851  -0.0447 -0.0742 598 TYR A OH  
1917 N N   . PRO A 260 ? 0.2994 0.3426 0.1769 0.0934  -0.0081 -0.0765 599 PRO A N   
1918 C CA  . PRO A 260 ? 0.3233 0.3518 0.1906 0.0817  -0.0140 -0.0799 599 PRO A CA  
1919 C C   . PRO A 260 ? 0.3491 0.3678 0.2196 0.0710  -0.0222 -0.0786 599 PRO A C   
1920 O O   . PRO A 260 ? 0.2968 0.3304 0.1795 0.0629  -0.0214 -0.0690 599 PRO A O   
1921 C CB  . PRO A 260 ? 0.2769 0.3241 0.1484 0.0741  -0.0090 -0.0718 599 PRO A CB  
1922 C CG  . PRO A 260 ? 0.2847 0.3534 0.1723 0.0744  -0.0035 -0.0618 599 PRO A CG  
1923 C CD  . PRO A 260 ? 0.2805 0.3521 0.1714 0.0885  -0.0012 -0.0659 599 PRO A CD  
1924 N N   . LEU A 261 ? 0.3681 0.3592 0.2264 0.0697  -0.0300 -0.0883 600 LEU A N   
1925 C CA  . LEU A 261 ? 0.3721 0.3525 0.2320 0.0569  -0.0380 -0.0880 600 LEU A CA  
1926 C C   . LEU A 261 ? 0.3402 0.3419 0.2121 0.0429  -0.0392 -0.0819 600 LEU A C   
1927 O O   . LEU A 261 ? 0.4004 0.4097 0.2818 0.0338  -0.0411 -0.0768 600 LEU A O   
1928 C CB  . LEU A 261 ? 0.4178 0.3614 0.2622 0.0529  -0.0473 -0.1000 600 LEU A CB  
1929 C CG  . LEU A 261 ? 0.4050 0.3375 0.2567 0.0335  -0.0542 -0.0968 600 LEU A CG  
1930 C CD1 . LEU A 261 ? 0.3375 0.2707 0.2005 0.0324  -0.0490 -0.0825 600 LEU A CD1 
1931 C CD2 . LEU A 261 ? 0.4459 0.3387 0.2831 0.0253  -0.0633 -0.1074 600 LEU A CD2 
1932 N N   . ASP A 262 ? 0.3541 0.3643 0.2243 0.0423  -0.0382 -0.0821 601 ASP A N   
1933 C CA  . ASP A 262 ? 0.3578 0.3844 0.2377 0.0333  -0.0403 -0.0760 601 ASP A CA  
1934 C C   . ASP A 262 ? 0.3789 0.4230 0.2732 0.0335  -0.0334 -0.0637 601 ASP A C   
1935 O O   . ASP A 262 ? 0.4473 0.4997 0.3525 0.0264  -0.0353 -0.0598 601 ASP A O   
1936 C CB  . ASP A 262 ? 0.4034 0.4308 0.2732 0.0357  -0.0408 -0.0776 601 ASP A CB  
1937 C CG  . ASP A 262 ? 0.4886 0.5284 0.3656 0.0294  -0.0458 -0.0727 601 ASP A CG  
1938 O OD1 . ASP A 262 ? 0.6037 0.6439 0.4847 0.0213  -0.0555 -0.0778 601 ASP A OD1 
1939 O OD2 . ASP A 262 ? 0.4923 0.5410 0.3713 0.0327  -0.0406 -0.0643 601 ASP A OD2 
1940 N N   . LEU A 263 ? 0.3904 0.4408 0.2851 0.0409  -0.0254 -0.0583 602 LEU A N   
1941 C CA  . LEU A 263 ? 0.3010 0.3641 0.2078 0.0391  -0.0199 -0.0476 602 LEU A CA  
1942 C C   . LEU A 263 ? 0.3214 0.3854 0.2351 0.0374  -0.0196 -0.0447 602 LEU A C   
1943 O O   . LEU A 263 ? 0.3031 0.3738 0.2257 0.0326  -0.0173 -0.0371 602 LEU A O   
1944 C CB  . LEU A 263 ? 0.2368 0.3072 0.1421 0.0446  -0.0128 -0.0439 602 LEU A CB  
1945 C CG  . LEU A 263 ? 0.3194 0.3864 0.2119 0.0459  -0.0122 -0.0464 602 LEU A CG  
1946 C CD1 . LEU A 263 ? 0.3203 0.3962 0.2102 0.0495  -0.0037 -0.0428 602 LEU A CD1 
1947 C CD2 . LEU A 263 ? 0.3928 0.4579 0.2844 0.0399  -0.0168 -0.0429 602 LEU A CD2 
1948 N N   . ALA A 264 ? 0.3328 0.3861 0.2387 0.0420  -0.0224 -0.0511 603 ALA A N   
1949 C CA  . ALA A 264 ? 0.2648 0.3146 0.1710 0.0403  -0.0239 -0.0481 603 ALA A CA  
1950 C C   . ALA A 264 ? 0.3382 0.3882 0.2475 0.0279  -0.0274 -0.0474 603 ALA A C   
1951 O O   . ALA A 264 ? 0.3038 0.3612 0.2188 0.0229  -0.0245 -0.0397 603 ALA A O   
1952 C CB  . ALA A 264 ? 0.2692 0.2978 0.1648 0.0490  -0.0274 -0.0543 603 ALA A CB  
1953 N N   . PHE A 265 ? 0.3610 0.4044 0.2682 0.0219  -0.0334 -0.0557 604 PHE A N   
1954 C CA  . PHE A 265 ? 0.3444 0.3950 0.2637 0.0083  -0.0351 -0.0543 604 PHE A CA  
1955 C C   . PHE A 265 ? 0.3125 0.3863 0.2413 0.0091  -0.0314 -0.0486 604 PHE A C   
1956 O O   . PHE A 265 ? 0.3072 0.3906 0.2445 0.0030  -0.0277 -0.0437 604 PHE A O   
1957 C CB  . PHE A 265 ? 0.2844 0.3295 0.2036 0.0011  -0.0437 -0.0647 604 PHE A CB  
1958 C CG  . PHE A 265 ? 0.3726 0.4381 0.3102 -0.0112 -0.0460 -0.0647 604 PHE A CG  
1959 C CD1 . PHE A 265 ? 0.4153 0.4778 0.3646 -0.0263 -0.0432 -0.0612 604 PHE A CD1 
1960 C CD2 . PHE A 265 ? 0.3642 0.4515 0.3080 -0.0068 -0.0499 -0.0667 604 PHE A CD2 
1961 C CE1 . PHE A 265 ? 0.3229 0.4110 0.2936 -0.0372 -0.0435 -0.0617 604 PHE A CE1 
1962 C CE2 . PHE A 265 ? 0.3874 0.4992 0.3518 -0.0152 -0.0529 -0.0679 604 PHE A CE2 
1963 C CZ  . PHE A 265 ? 0.3712 0.4863 0.3516 -0.0305 -0.0490 -0.0658 604 PHE A CZ  
1964 N N   . SER A 266 ? 0.3178 0.3931 0.2474 0.0159  -0.0300 -0.0463 605 SER A N   
1965 C CA  . SER A 266 ? 0.2821 0.3679 0.2200 0.0177  -0.0263 -0.0396 605 SER A CA  
1966 C C   . SER A 266 ? 0.2826 0.3682 0.2231 0.0176  -0.0195 -0.0316 605 SER A C   
1967 O O   . SER A 266 ? 0.2747 0.3681 0.2210 0.0154  -0.0173 -0.0289 605 SER A O   
1968 C CB  . SER A 266 ? 0.3469 0.4289 0.2792 0.0235  -0.0260 -0.0382 605 SER A CB  
1969 O OG  . SER A 266 ? 0.4942 0.5810 0.4301 0.0254  -0.0243 -0.0329 605 SER A OG  
1970 N N   . MET A 267 ? 0.3006 0.3787 0.2366 0.0204  -0.0167 -0.0288 606 MET A N   
1971 C CA  . MET A 267 ? 0.2825 0.3599 0.2209 0.0191  -0.0126 -0.0218 606 MET A CA  
1972 C C   . MET A 267 ? 0.3166 0.3930 0.2525 0.0138  -0.0126 -0.0207 606 MET A C   
1973 O O   . MET A 267 ? 0.2968 0.3731 0.2340 0.0109  -0.0094 -0.0160 606 MET A O   
1974 C CB  . MET A 267 ? 0.2546 0.3318 0.1910 0.0240  -0.0114 -0.0207 606 MET A CB  
1975 C CG  . MET A 267 ? 0.3913 0.4716 0.3318 0.0221  -0.0087 -0.0144 606 MET A CG  
1976 S SD  . MET A 267 ? 0.3839 0.4776 0.3262 0.0292  -0.0074 -0.0146 606 MET A SD  
1977 C CE  . MET A 267 ? 0.3092 0.4034 0.2478 0.0332  -0.0057 -0.0196 606 MET A CE  
1978 N N   . ALA A 268 ? 0.2991 0.3724 0.2277 0.0116  -0.0163 -0.0256 607 ALA A N   
1979 C CA  . ALA A 268 ? 0.2772 0.3462 0.2036 0.0027  -0.0145 -0.0228 607 ALA A CA  
1980 C C   . ALA A 268 ? 0.2638 0.3479 0.2001 -0.0037 -0.0106 -0.0235 607 ALA A C   
1981 O O   . ALA A 268 ? 0.2751 0.3592 0.2107 -0.0096 -0.0045 -0.0186 607 ALA A O   
1982 C CB  . ALA A 268 ? 0.2609 0.3104 0.1849 -0.0020 -0.0180 -0.0254 607 ALA A CB  
1983 N N   . GLU A 269 ? 0.2915 0.3895 0.2362 -0.0015 -0.0141 -0.0298 608 GLU A N   
1984 C CA  . GLU A 269 ? 0.2587 0.3760 0.2170 -0.0041 -0.0115 -0.0314 608 GLU A CA  
1985 C C   . GLU A 269 ? 0.2303 0.3522 0.1836 0.0025  -0.0062 -0.0272 608 GLU A C   
1986 O O   . GLU A 269 ? 0.2916 0.4213 0.2503 -0.0004 0.0008  -0.0259 608 GLU A O   
1987 C CB  . GLU A 269 ? 0.2431 0.3739 0.2102 -0.0008 -0.0199 -0.0389 608 GLU A CB  
1988 C CG  . GLU A 269 ? 0.2905 0.4453 0.2735 0.0022  -0.0194 -0.0407 608 GLU A CG  
1989 C CD  . GLU A 269 ? 0.3154 0.4856 0.3182 -0.0095 -0.0133 -0.0413 608 GLU A CD  
1990 O OE1 . GLU A 269 ? 0.3716 0.5314 0.3750 -0.0224 -0.0121 -0.0409 608 GLU A OE1 
1991 O OE2 . GLU A 269 ? 0.3222 0.5143 0.3396 -0.0055 -0.0090 -0.0421 608 GLU A OE2 
1992 N N   . ILE A 270 ? 0.2304 0.3370 0.1813 0.0097  -0.0075 -0.0228 609 ILE A N   
1993 C CA  . ILE A 270 ? 0.2652 0.3646 0.2140 0.0129  -0.0040 -0.0184 609 ILE A CA  
1994 C C   . ILE A 270 ? 0.2662 0.3544 0.2075 0.0079  0.0004  -0.0140 609 ILE A C   
1995 O O   . ILE A 270 ? 0.2778 0.3606 0.2148 0.0087  0.0037  -0.0126 609 ILE A O   
1996 C CB  . ILE A 270 ? 0.2701 0.3563 0.2159 0.0165  -0.0061 -0.0153 609 ILE A CB  
1997 C CG1 . ILE A 270 ? 0.2965 0.3757 0.2369 0.0190  -0.0047 -0.0132 609 ILE A CG1 
1998 C CG2 . ILE A 270 ? 0.2710 0.3466 0.2136 0.0134  -0.0058 -0.0120 609 ILE A CG2 
1999 C CD1 . ILE A 270 ? 0.2395 0.3328 0.1825 0.0266  -0.0057 -0.0172 609 ILE A CD1 
2000 N N   . ALA A 271 ? 0.2871 0.3693 0.2234 0.0037  -0.0003 -0.0123 610 ALA A N   
2001 C CA  . ALA A 271 ? 0.2612 0.3319 0.1870 -0.0006 0.0025  -0.0076 610 ALA A CA  
2002 C C   . ALA A 271 ? 0.2883 0.3670 0.2107 -0.0070 0.0100  -0.0079 610 ALA A C   
2003 O O   . ALA A 271 ? 0.3108 0.3805 0.2250 -0.0083 0.0148  -0.0052 610 ALA A O   
2004 C CB  . ALA A 271 ? 0.2467 0.3085 0.1651 -0.0010 -0.0018 -0.0048 610 ALA A CB  
2005 N N   . LYS A 272 ? 0.2740 0.3695 0.2027 -0.0127 0.0119  -0.0120 611 LYS A N   
2006 C CA  . LYS A 272 ? 0.3150 0.4192 0.2505 -0.0216 0.0215  -0.0117 611 LYS A CA  
2007 C C   . LYS A 272 ? 0.2686 0.3891 0.2086 -0.0152 0.0287  -0.0150 611 LYS A C   
2008 O O   . LYS A 272 ? 0.2778 0.3943 0.2133 -0.0181 0.0378  -0.0126 611 LYS A O   
2009 C CB  . LYS A 272 ? 0.2391 0.3540 0.1941 -0.0296 0.0195  -0.0158 611 LYS A CB  
2010 C CG  . LYS A 272 ? 0.1870 0.3185 0.1552 -0.0412 0.0308  -0.0156 611 LYS A CG  
2011 C CD  . LYS A 272 ? 0.2997 0.4556 0.2959 -0.0465 0.0270  -0.0227 611 LYS A CD  
2012 C CE  . LYS A 272 ? 0.3952 0.5386 0.3938 -0.0643 0.0252  -0.0212 611 LYS A CE  
2013 N NZ  . LYS A 272 ? 0.3852 0.5312 0.3844 -0.0806 0.0396  -0.0152 611 LYS A NZ  
2014 N N   . ARG A 273 ? 0.2738 0.4042 0.2233 -0.0046 0.0230  -0.0198 612 ARG A N   
2015 C CA  . ARG A 273 ? 0.2335 0.3696 0.1874 0.0047  0.0268  -0.0224 612 ARG A CA  
2016 C C   . ARG A 273 ? 0.2559 0.3624 0.1911 0.0066  0.0280  -0.0180 612 ARG A C   
2017 O O   . ARG A 273 ? 0.2609 0.3659 0.1920 0.0098  0.0358  -0.0197 612 ARG A O   
2018 C CB  . ARG A 273 ? 0.2507 0.3969 0.2116 0.0163  0.0185  -0.0268 612 ARG A CB  
2019 C CG  . ARG A 273 ? 0.2928 0.4609 0.2732 0.0143  0.0124  -0.0315 612 ARG A CG  
2020 C CD  . ARG A 273 ? 0.3051 0.4800 0.2891 0.0275  0.0027  -0.0349 612 ARG A CD  
2021 N NE  . ARG A 273 ? 0.2521 0.4456 0.2549 0.0251  -0.0062 -0.0396 612 ARG A NE  
2022 C CZ  . ARG A 273 ? 0.3444 0.5472 0.3517 0.0358  -0.0168 -0.0428 612 ARG A CZ  
2023 N NH1 . ARG A 273 ? 0.4159 0.6089 0.4097 0.0500  -0.0191 -0.0409 612 ARG A NH1 
2024 N NH2 . ARG A 273 ? 0.4104 0.6298 0.4333 0.0316  -0.0264 -0.0478 612 ARG A NH2 
2025 N N   . CYS A 274 ? 0.2834 0.3678 0.2083 0.0046  0.0210  -0.0134 613 CYS A N   
2026 C CA  . CYS A 274 ? 0.2803 0.3396 0.1882 0.0041  0.0210  -0.0107 613 CYS A CA  
2027 C C   . CYS A 274 ? 0.3417 0.3922 0.2364 -0.0010 0.0279  -0.0082 613 CYS A C   
2028 O O   . CYS A 274 ? 0.3893 0.4239 0.2680 0.0004  0.0313  -0.0086 613 CYS A O   
2029 C CB  . CYS A 274 ? 0.2817 0.3273 0.1870 0.0026  0.0123  -0.0072 613 CYS A CB  
2030 S SG  . CYS A 274 ? 0.2282 0.2755 0.1410 0.0071  0.0067  -0.0084 613 CYS A SG  
2031 N N   . VAL A 275 ? 0.2997 0.3582 0.1972 -0.0073 0.0304  -0.0054 614 VAL A N   
2032 C CA  . VAL A 275 ? 0.2425 0.2910 0.1249 -0.0127 0.0370  -0.0009 614 VAL A CA  
2033 C C   . VAL A 275 ? 0.2956 0.3612 0.1848 -0.0166 0.0508  -0.0030 614 VAL A C   
2034 O O   . VAL A 275 ? 0.2670 0.3284 0.1467 -0.0240 0.0583  0.0018  614 VAL A O   
2035 C CB  . VAL A 275 ? 0.2599 0.3014 0.1362 -0.0193 0.0318  0.0052  614 VAL A CB  
2036 C CG1 . VAL A 275 ? 0.2887 0.3172 0.1610 -0.0134 0.0196  0.0068  614 VAL A CG1 
2037 C CG2 . VAL A 275 ? 0.3262 0.3854 0.2161 -0.0270 0.0330  0.0037  614 VAL A CG2 
2038 N N   . ALA A 276 ? 0.2925 0.3789 0.1993 -0.0113 0.0544  -0.0097 615 ALA A N   
2039 C CA  . ALA A 276 ? 0.2776 0.3849 0.1963 -0.0127 0.0682  -0.0127 615 ALA A CA  
2040 C C   . ALA A 276 ? 0.3480 0.4368 0.2450 -0.0092 0.0778  -0.0116 615 ALA A C   
2041 O O   . ALA A 276 ? 0.3840 0.4477 0.2603 -0.0027 0.0727  -0.0119 615 ALA A O   
2042 C CB  . ALA A 276 ? 0.2574 0.3918 0.2004 -0.0028 0.0674  -0.0207 615 ALA A CB  
2043 N N   . ARG A 277 ? 0.3867 0.4880 0.2877 -0.0144 0.0921  -0.0103 616 ARG A N   
2044 C CA  . ARG A 277 ? 0.4500 0.5357 0.3276 -0.0097 0.1028  -0.0089 616 ARG A CA  
2045 C C   . ARG A 277 ? 0.5353 0.6206 0.4126 0.0035  0.1083  -0.0182 616 ARG A C   
2046 O O   . ARG A 277 ? 0.5357 0.5937 0.3841 0.0097  0.1099  -0.0195 616 ARG A O   
2047 C CB  . ARG A 277 ? 0.5393 0.6401 0.4215 -0.0196 0.1179  -0.0042 616 ARG A CB  
2048 C CG  . ARG A 277 ? 0.6728 0.7592 0.5406 -0.0336 0.1137  0.0060  616 ARG A CG  
2049 C CD  . ARG A 277 ? 0.6522 0.7488 0.5200 -0.0454 0.1298  0.0117  616 ARG A CD  
2050 N NE  . ARG A 277 ? 0.6959 0.7841 0.5389 -0.0377 0.1394  0.0134  616 ARG A NE  
2051 C CZ  . ARG A 277 ? 0.6708 0.7365 0.4827 -0.0403 0.1352  0.0206  616 ARG A CZ  
2052 N NH1 . ARG A 277 ? 0.6082 0.6535 0.4096 -0.0489 0.1221  0.0273  616 ARG A NH1 
2053 N NH2 . ARG A 277 ? 0.6106 0.6749 0.4011 -0.0336 0.1437  0.0205  616 ARG A NH2 
2054 N N   . ASP A 278 ? 0.4792 0.5947 0.3875 0.0084  0.1100  -0.0253 617 ASP A N   
2055 C CA  . ASP A 278 ? 0.4602 0.5782 0.3713 0.0225  0.1132  -0.0348 617 ASP A CA  
2056 C C   . ASP A 278 ? 0.4239 0.5214 0.3234 0.0281  0.0971  -0.0370 617 ASP A C   
2057 O O   . ASP A 278 ? 0.4177 0.5256 0.3321 0.0287  0.0846  -0.0352 617 ASP A O   
2058 C CB  . ASP A 278 ? 0.4357 0.5970 0.3867 0.0295  0.1174  -0.0400 617 ASP A CB  
2059 C CG  . ASP A 278 ? 0.6856 0.8703 0.6513 0.0226  0.1353  -0.0383 617 ASP A CG  
2060 O OD1 . ASP A 278 ? 0.7946 0.9601 0.7360 0.0136  0.1444  -0.0318 617 ASP A OD1 
2061 O OD2 . ASP A 278 ? 0.7140 0.9368 0.7154 0.0267  0.1394  -0.0425 617 ASP A OD2 
2062 N N   . LEU A 279 ? 0.4150 0.4844 0.2873 0.0303  0.0974  -0.0414 618 LEU A N   
2063 C CA  . LEU A 279 ? 0.3896 0.4400 0.2505 0.0321  0.0822  -0.0422 618 LEU A CA  
2064 C C   . LEU A 279 ? 0.4000 0.4659 0.2802 0.0484  0.0756  -0.0455 618 LEU A C   
2065 O O   . LEU A 279 ? 0.4155 0.4761 0.2969 0.0489  0.0626  -0.0420 618 LEU A O   
2066 C CB  . LEU A 279 ? 0.3383 0.3660 0.1714 0.0292  0.0824  -0.0481 618 LEU A CB  
2067 C CG  . LEU A 279 ? 0.4208 0.4512 0.2497 0.0420  0.0938  -0.0583 618 LEU A CG  
2068 C CD1 . LEU A 279 ? 0.5615 0.5878 0.3961 0.0617  0.0875  -0.0624 618 LEU A CD1 
2069 C CD2 . LEU A 279 ? 0.4543 0.4705 0.2555 0.0353  0.0940  -0.0630 618 LEU A CD2 
2070 N N   . ASN A 280 ? 0.4479 0.5328 0.3430 0.0626  0.0843  -0.0522 619 ASN A N   
2071 C CA  . ASN A 280 ? 0.4619 0.5601 0.3734 0.0806  0.0764  -0.0552 619 ASN A CA  
2072 C C   . ASN A 280 ? 0.3799 0.5065 0.3178 0.0783  0.0680  -0.0511 619 ASN A C   
2073 O O   . ASN A 280 ? 0.3573 0.4872 0.3006 0.0901  0.0567  -0.0517 619 ASN A O   
2074 C CB  . ASN A 280 ? 0.5072 0.6225 0.4325 0.0971  0.0870  -0.0633 619 ASN A CB  
2075 C CG  . ASN A 280 ? 0.5433 0.6269 0.4400 0.1055  0.0913  -0.0697 619 ASN A CG  
2076 O OD1 . ASN A 280 ? 0.5960 0.6457 0.4660 0.1051  0.0814  -0.0685 619 ASN A OD1 
2077 N ND2 . ASN A 280 ? 0.5914 0.6861 0.4936 0.1123  0.1063  -0.0770 619 ASN A ND2 
2078 N N   . SER A 281 ? 0.3650 0.5096 0.3166 0.0633  0.0728  -0.0473 620 SER A N   
2079 C CA  . SER A 281 ? 0.3407 0.5094 0.3142 0.0583  0.0638  -0.0448 620 SER A CA  
2080 C C   . SER A 281 ? 0.3466 0.4925 0.3027 0.0522  0.0513  -0.0395 620 SER A C   
2081 O O   . SER A 281 ? 0.3484 0.5069 0.3151 0.0549  0.0411  -0.0394 620 SER A O   
2082 C CB  . SER A 281 ? 0.4096 0.6006 0.4006 0.0427  0.0727  -0.0424 620 SER A CB  
2083 O OG  . SER A 281 ? 0.7933 1.0064 0.8019 0.0465  0.0861  -0.0465 620 SER A OG  
2084 N N   . ARG A 282 ? 0.3444 0.4576 0.2744 0.0438  0.0517  -0.0354 621 ARG A N   
2085 C CA  . ARG A 282 ? 0.3004 0.3932 0.2182 0.0372  0.0404  -0.0300 621 ARG A CA  
2086 C C   . ARG A 282 ? 0.3196 0.4052 0.2330 0.0487  0.0312  -0.0312 621 ARG A C   
2087 O O   . ARG A 282 ? 0.3664 0.4469 0.2735 0.0621  0.0332  -0.0358 621 ARG A O   
2088 C CB  . ARG A 282 ? 0.3026 0.3642 0.1962 0.0269  0.0415  -0.0265 621 ARG A CB  
2089 C CG  . ARG A 282 ? 0.3187 0.3797 0.2086 0.0170  0.0490  -0.0233 621 ARG A CG  
2090 C CD  . ARG A 282 ? 0.3122 0.3420 0.1740 0.0104  0.0496  -0.0215 621 ARG A CD  
2091 N NE  . ARG A 282 ? 0.3682 0.3944 0.2198 0.0067  0.0595  -0.0185 621 ARG A NE  
2092 C CZ  . ARG A 282 ? 0.3816 0.3873 0.2112 0.0061  0.0630  -0.0183 621 ARG A CZ  
2093 N NH1 . ARG A 282 ? 0.3316 0.3320 0.1541 -0.0029 0.0572  -0.0257 621 ARG A NH1 
2094 N NH2 . ARG A 282 ? 0.4275 0.4388 0.2511 0.0093  0.0704  -0.0125 621 ARG A NH2 
2095 N N   . PRO A 283 ? 0.2714 0.3535 0.1858 0.0448  0.0216  -0.0270 622 PRO A N   
2096 C CA  . PRO A 283 ? 0.2694 0.3385 0.1741 0.0533  0.0137  -0.0262 622 PRO A CA  
2097 C C   . PRO A 283 ? 0.3237 0.3605 0.2064 0.0464  0.0128  -0.0235 622 PRO A C   
2098 O O   . PRO A 283 ? 0.3307 0.3576 0.2079 0.0334  0.0152  -0.0215 622 PRO A O   
2099 C CB  . PRO A 283 ? 0.3024 0.3795 0.2170 0.0476  0.0063  -0.0224 622 PRO A CB  
2100 C CG  . PRO A 283 ? 0.3048 0.3818 0.2250 0.0334  0.0091  -0.0195 622 PRO A CG  
2101 C CD  . PRO A 283 ? 0.3136 0.4006 0.2363 0.0329  0.0182  -0.0228 622 PRO A CD  
2102 N N   . ASN A 284 ? 0.3230 0.3430 0.1911 0.0557  0.0084  -0.0236 623 ASN A N   
2103 C CA  . ASN A 284 ? 0.3365 0.3284 0.1844 0.0464  0.0058  -0.0208 623 ASN A CA  
2104 C C   . ASN A 284 ? 0.3559 0.3518 0.2115 0.0302  0.0015  -0.0143 623 ASN A C   
2105 O O   . ASN A 284 ? 0.3119 0.3208 0.1806 0.0312  -0.0010 -0.0119 623 ASN A O   
2106 C CB  . ASN A 284 ? 0.3165 0.2826 0.1419 0.0609  0.0019  -0.0218 623 ASN A CB  
2107 C CG  . ASN A 284 ? 0.3916 0.3510 0.2083 0.0800  0.0067  -0.0298 623 ASN A CG  
2108 O OD1 . ASN A 284 ? 0.4577 0.4134 0.2710 0.0761  0.0134  -0.0339 623 ASN A OD1 
2109 N ND2 . ASN A 284 ? 0.4305 0.3905 0.2444 0.1018  0.0034  -0.0325 623 ASN A ND2 
2110 N N   . VAL A 285 ? 0.3564 0.3448 0.2050 0.0164  0.0006  -0.0123 624 VAL A N   
2111 C CA  . VAL A 285 ? 0.2832 0.2810 0.1401 0.0028  -0.0025 -0.0070 624 VAL A CA  
2112 C C   . VAL A 285 ? 0.3146 0.3099 0.1685 0.0054  -0.0054 -0.0032 624 VAL A C   
2113 O O   . VAL A 285 ? 0.3022 0.3024 0.1638 -0.0010 -0.0062 0.0001  624 VAL A O   
2114 C CB  . VAL A 285 ? 0.2677 0.2721 0.1239 -0.0006 -0.0047 -0.0062 624 VAL A CB  
2115 C CG1 . VAL A 285 ? 0.3337 0.3054 0.1633 -0.0009 -0.0073 -0.0059 624 VAL A CG1 
2116 C CG2 . VAL A 285 ? 0.2279 0.2303 0.0917 0.0054  -0.0072 -0.0023 624 VAL A CG2 
2117 N N   . SER A 286 ? 0.3506 0.3249 0.1862 0.0160  -0.0070 -0.0035 625 SER A N   
2118 C CA  . SER A 286 ? 0.3345 0.3002 0.1617 0.0188  -0.0100 0.0014  625 SER A CA  
2119 C C   . SER A 286 ? 0.3520 0.3360 0.1956 0.0244  -0.0108 0.0012  625 SER A C   
2120 O O   . SER A 286 ? 0.3359 0.3242 0.1803 0.0195  -0.0121 0.0054  625 SER A O   
2121 C CB  . SER A 286 ? 0.3630 0.2917 0.1612 0.0317  -0.0130 0.0010  625 SER A CB  
2122 O OG  . SER A 286 ? 0.4018 0.3330 0.2018 0.0512  -0.0132 -0.0048 625 SER A OG  
2123 N N   . GLU A 287 ? 0.3488 0.3448 0.2045 0.0352  -0.0100 -0.0042 626 GLU A N   
2124 C CA  . GLU A 287 ? 0.2775 0.2930 0.1497 0.0410  -0.0120 -0.0055 626 GLU A CA  
2125 C C   . GLU A 287 ? 0.2729 0.2992 0.1598 0.0284  -0.0100 -0.0043 626 GLU A C   
2126 O O   . GLU A 287 ? 0.3488 0.3800 0.2396 0.0278  -0.0118 -0.0033 626 GLU A O   
2127 C CB  . GLU A 287 ? 0.3037 0.3368 0.1862 0.0553  -0.0117 -0.0119 626 GLU A CB  
2128 C CG  . GLU A 287 ? 0.3552 0.4134 0.2553 0.0601  -0.0153 -0.0147 626 GLU A CG  
2129 C CD  . GLU A 287 ? 0.4065 0.4913 0.3177 0.0736  -0.0155 -0.0222 626 GLU A CD  
2130 O OE1 . GLU A 287 ? 0.3792 0.4601 0.2825 0.0823  -0.0113 -0.0254 626 GLU A OE1 
2131 O OE2 . GLU A 287 ? 0.4338 0.5447 0.3614 0.0747  -0.0192 -0.0262 626 GLU A OE2 
2132 N N   . VAL A 288 ? 0.2650 0.2916 0.1569 0.0205  -0.0066 -0.0049 627 VAL A N   
2133 C CA  . VAL A 288 ? 0.2991 0.3314 0.2018 0.0140  -0.0057 -0.0039 627 VAL A CA  
2134 C C   . VAL A 288 ? 0.2876 0.3123 0.1824 0.0086  -0.0062 -0.0004 627 VAL A C   
2135 O O   . VAL A 288 ? 0.3121 0.3461 0.2154 0.0091  -0.0056 -0.0005 627 VAL A O   
2136 C CB  . VAL A 288 ? 0.3054 0.3356 0.2099 0.0094  -0.0037 -0.0042 627 VAL A CB  
2137 C CG1 . VAL A 288 ? 0.3006 0.3391 0.2159 0.0071  -0.0040 -0.0033 627 VAL A CG1 
2138 C CG2 . VAL A 288 ? 0.2327 0.2711 0.1415 0.0140  -0.0012 -0.0076 627 VAL A CG2 
2139 N N   . PHE A 289 ? 0.2873 0.2958 0.1635 0.0034  -0.0067 0.0026  628 PHE A N   
2140 C CA  . PHE A 289 ? 0.3327 0.3336 0.1975 0.0004  -0.0057 0.0064  628 PHE A CA  
2141 C C   . PHE A 289 ? 0.3443 0.3480 0.2060 0.0016  -0.0062 0.0077  628 PHE A C   
2142 O O   . PHE A 289 ? 0.3392 0.3480 0.2010 0.0016  -0.0032 0.0091  628 PHE A O   
2143 C CB  . PHE A 289 ? 0.3294 0.3185 0.1799 0.0049  -0.0053 0.0094  628 PHE A CB  
2144 C CG  . PHE A 289 ? 0.2891 0.2898 0.1348 -0.0029 -0.0023 0.0156  628 PHE A CG  
2145 C CD1 . PHE A 289 ? 0.2796 0.2988 0.1407 -0.0134 -0.0002 0.0158  628 PHE A CD1 
2146 C CD2 . PHE A 289 ? 0.3308 0.3240 0.1611 -0.0072 -0.0018 0.0219  628 PHE A CD2 
2147 C CE1 . PHE A 289 ? 0.2803 0.3106 0.1400 -0.0263 0.0035  0.0213  628 PHE A CE1 
2148 C CE2 . PHE A 289 ? 0.3698 0.3613 0.1932 -0.0219 0.0020  0.0280  628 PHE A CE2 
2149 C CZ  . PHE A 289 ? 0.3431 0.3568 0.1826 -0.0317 0.0053  0.0274  628 PHE A CZ  
2150 N N   . MET A 290 ? 0.3196 0.3264 0.1810 0.0068  -0.0097 0.0073  629 MET A N   
2151 C CA  . MET A 290 ? 0.2874 0.2966 0.1449 0.0117  -0.0119 0.0084  629 MET A CA  
2152 C C   . MET A 290 ? 0.3034 0.3268 0.1772 0.0163  -0.0116 0.0036  629 MET A C   
2153 O O   . MET A 290 ? 0.3185 0.3428 0.1866 0.0163  -0.0115 0.0040  629 MET A O   
2154 C CB  . MET A 290 ? 0.3286 0.3336 0.1796 0.0243  -0.0173 0.0086  629 MET A CB  
2155 C CG  . MET A 290 ? 0.3326 0.3386 0.1782 0.0316  -0.0220 0.0092  629 MET A CG  
2156 S SD  . MET A 290 ? 0.3858 0.4129 0.2528 0.0408  -0.0256 0.0011  629 MET A SD  
2157 C CE  . MET A 290 ? 0.3487 0.3829 0.2251 0.0539  -0.0278 -0.0035 629 MET A CE  
2158 N N   . ILE A 291 ? 0.3362 0.3709 0.2276 0.0196  -0.0113 -0.0007 630 ILE A N   
2159 C CA  . ILE A 291 ? 0.3175 0.3658 0.2223 0.0223  -0.0116 -0.0049 630 ILE A CA  
2160 C C   . ILE A 291 ? 0.3340 0.3848 0.2402 0.0181  -0.0076 -0.0043 630 ILE A C   
2161 O O   . ILE A 291 ? 0.3457 0.4006 0.2498 0.0201  -0.0074 -0.0062 630 ILE A O   
2162 C CB  . ILE A 291 ? 0.2892 0.3485 0.2087 0.0247  -0.0118 -0.0086 630 ILE A CB  
2163 C CG1 . ILE A 291 ? 0.2916 0.3567 0.2114 0.0327  -0.0153 -0.0109 630 ILE A CG1 
2164 C CG2 . ILE A 291 ? 0.2751 0.3449 0.2039 0.0251  -0.0125 -0.0127 630 ILE A CG2 
2165 C CD1 . ILE A 291 ? 0.3021 0.3714 0.2185 0.0396  -0.0213 -0.0129 630 ILE A CD1 
2166 N N   . LEU A 292 ? 0.3100 0.3605 0.2191 0.0136  -0.0047 -0.0023 631 LEU A N   
2167 C CA  . LEU A 292 ? 0.2959 0.3577 0.2102 0.0124  -0.0014 -0.0021 631 LEU A CA  
2168 C C   . LEU A 292 ? 0.3186 0.3798 0.2206 0.0108  0.0022  0.0003  631 LEU A C   
2169 O O   . LEU A 292 ? 0.3141 0.3893 0.2200 0.0128  0.0056  -0.0013 631 LEU A O   
2170 C CB  . LEU A 292 ? 0.2590 0.3250 0.1787 0.0080  -0.0006 0.0000  631 LEU A CB  
2171 C CG  . LEU A 292 ? 0.2480 0.3148 0.1767 0.0091  -0.0028 -0.0019 631 LEU A CG  
2172 C CD1 . LEU A 292 ? 0.2630 0.3320 0.1925 0.0043  -0.0033 0.0005  631 LEU A CD1 
2173 C CD2 . LEU A 292 ? 0.2237 0.3012 0.1609 0.0140  -0.0032 -0.0054 631 LEU A CD2 
2174 N N   . SER A 293 ? 0.3530 0.3976 0.2373 0.0077  0.0020  0.0041  632 SER A N   
2175 C CA  . SER A 293 ? 0.3291 0.3696 0.1965 0.0048  0.0068  0.0078  632 SER A CA  
2176 C C   . SER A 293 ? 0.3616 0.4012 0.2214 0.0090  0.0060  0.0051  632 SER A C   
2177 O O   . SER A 293 ? 0.3942 0.4376 0.2443 0.0081  0.0120  0.0061  632 SER A O   
2178 C CB  . SER A 293 ? 0.3001 0.3172 0.1442 0.0007  0.0063  0.0137  632 SER A CB  
2179 O OG  . SER A 293 ? 0.3441 0.3659 0.1928 -0.0036 0.0086  0.0169  632 SER A OG  
2180 N N   . LYS A 294 ? 0.3635 0.4011 0.2274 0.0136  -0.0009 0.0016  633 LYS A N   
2181 C CA  . LYS A 294 ? 0.3921 0.4294 0.2469 0.0175  -0.0036 -0.0011 633 LYS A CA  
2182 C C   . LYS A 294 ? 0.4064 0.4570 0.2717 0.0220  -0.0016 -0.0074 633 LYS A C   
2183 O O   . LYS A 294 ? 0.4764 0.5265 0.3290 0.0237  0.0003  -0.0097 633 LYS A O   
2184 C CB  . LYS A 294 ? 0.4140 0.4490 0.2700 0.0223  -0.0125 -0.0022 633 LYS A CB  
2185 C CG  . LYS A 294 ? 0.3704 0.3933 0.2127 0.0207  -0.0156 0.0040  633 LYS A CG  
2186 C CD  . LYS A 294 ? 0.4250 0.4500 0.2678 0.0304  -0.0249 0.0024  633 LYS A CD  
2187 C CE  . LYS A 294 ? 0.4498 0.4620 0.2760 0.0330  -0.0287 0.0092  633 LYS A CE  
2188 N NZ  . LYS A 294 ? 0.4783 0.4804 0.2806 0.0251  -0.0256 0.0163  633 LYS A NZ  
2189 N N   . ILE A 295 ? 0.3653 0.4260 0.2501 0.0239  -0.0021 -0.0104 634 ILE A N   
2190 C CA  . ILE A 295 ? 0.4044 0.4751 0.2958 0.0286  -0.0008 -0.0163 634 ILE A CA  
2191 C C   . ILE A 295 ? 0.4434 0.5262 0.3370 0.0291  0.0069  -0.0154 634 ILE A C   
2192 O O   . ILE A 295 ? 0.4985 0.5904 0.3961 0.0352  0.0085  -0.0208 634 ILE A O   
2193 C CB  . ILE A 295 ? 0.3578 0.4326 0.2646 0.0301  -0.0049 -0.0196 634 ILE A CB  
2194 C CG1 . ILE A 295 ? 0.2995 0.3794 0.2178 0.0269  -0.0026 -0.0154 634 ILE A CG1 
2195 C CG2 . ILE A 295 ? 0.4756 0.5454 0.3832 0.0299  -0.0114 -0.0211 634 ILE A CG2 
2196 C CD1 . ILE A 295 ? 0.3069 0.3876 0.2351 0.0270  -0.0057 -0.0174 634 ILE A CD1 
2197 N N   . GLN A 296 ? 0.4444 0.5287 0.3346 0.0234  0.0117  -0.0093 635 GLN A N   
2198 C CA  . GLN A 296 ? 0.4762 0.5796 0.3714 0.0229  0.0196  -0.0081 635 GLN A CA  
2199 C C   . GLN A 296 ? 0.6946 0.7982 0.5736 0.0244  0.0272  -0.0094 635 GLN A C   
2200 O O   . GLN A 296 ? 0.7077 0.7931 0.5670 0.0233  0.0258  -0.0091 635 GLN A O   
2201 C CB  . GLN A 296 ? 0.4376 0.5447 0.3354 0.0139  0.0220  -0.0010 635 GLN A CB  
2202 C CG  . GLN A 296 ? 0.4842 0.6213 0.3953 0.0117  0.0288  0.0004  635 GLN A CG  
2203 C CD  . GLN A 296 ? 0.4928 0.6363 0.4081 0.0000  0.0289  0.0071  635 GLN A CD  
2204 O OE1 . GLN A 296 ? 0.4355 0.5562 0.3361 -0.0065 0.0274  0.0116  635 GLN A OE1 
2205 N NE2 . GLN A 296 ? 0.4440 0.6186 0.3779 -0.0024 0.0300  0.0076  635 GLN A NE2 
2206 N N   . SER A 297 ? 1.0252 1.1510 0.9120 0.0274  0.0355  -0.0111 636 SER A N   
2207 C CA  . SER A 297 ? 0.9280 1.0568 0.8006 0.0299  0.0455  -0.0135 636 SER A CA  
2208 C C   . SER A 297 ? 1.0212 1.1326 0.8692 0.0208  0.0504  -0.0069 636 SER A C   
2209 O O   . SER A 297 ? 0.8872 0.9929 0.7152 0.0217  0.0579  -0.0085 636 SER A O   
2210 C CB  . SER A 297 ? 0.9231 1.0837 0.8127 0.0329  0.0556  -0.0146 636 SER A CB  
2211 O OG  . SER A 297 ? 1.1650 1.3414 1.0665 0.0222  0.0586  -0.0066 636 SER A OG  
2212 N N   . SER B 1   ? 0.7731 0.6700 0.9985 -0.0465 0.1385  0.1988  340 SER B N   
2213 C CA  . SER B 1   ? 0.8399 0.7349 1.0318 -0.0466 0.1476  0.2066  340 SER B CA  
2214 C C   . SER B 1   ? 0.9125 0.8293 1.0823 -0.0367 0.1278  0.2024  340 SER B C   
2215 O O   . SER B 1   ? 0.9702 0.8748 1.0938 -0.0328 0.1260  0.2150  340 SER B O   
2216 C CB  . SER B 1   ? 0.7761 0.6846 0.9963 -0.0614 0.1697  0.1957  340 SER B CB  
2217 O OG  . SER B 1   ? 0.9234 0.8712 1.1847 -0.0637 0.1573  0.1775  340 SER B OG  
2218 N N   . LEU B 2   ? 0.7447 0.6922 0.9442 -0.0354 0.1131  0.1846  341 LEU B N   
2219 C CA  . LEU B 2   ? 0.6324 0.6002 0.8148 -0.0276 0.0967  0.1774  341 LEU B CA  
2220 C C   . LEU B 2   ? 0.6766 0.6408 0.8430 -0.0157 0.0746  0.1823  341 LEU B C   
2221 O O   . LEU B 2   ? 0.7248 0.6703 0.8972 -0.0116 0.0728  0.1927  341 LEU B O   
2222 C CB  . LEU B 2   ? 0.5286 0.5275 0.7485 -0.0316 0.0907  0.1586  341 LEU B CB  
2223 C CG  . LEU B 2   ? 0.5260 0.5361 0.7809 -0.0426 0.1096  0.1548  341 LEU B CG  
2224 C CD1 . LEU B 2   ? 0.4972 0.5357 0.7978 -0.0490 0.0962  0.1418  341 LEU B CD1 
2225 C CD2 . LEU B 2   ? 0.5352 0.5490 0.7764 -0.0416 0.1256  0.1548  341 LEU B CD2 
2226 N N   . THR B 3   ? 0.5746 0.5569 0.7248 -0.0100 0.0596  0.1746  342 THR B N   
2227 C CA  . THR B 3   ? 0.5479 0.5342 0.6903 0.0006  0.0382  0.1763  342 THR B CA  
2228 C C   . THR B 3   ? 0.5064 0.5088 0.6828 0.0003  0.0283  0.1561  342 THR B C   
2229 O O   . THR B 3   ? 0.4843 0.5050 0.6651 -0.0039 0.0260  0.1406  342 THR B O   
2230 C CB  . THR B 3   ? 0.5574 0.5533 0.6582 0.0032  0.0285  0.1782  342 THR B CB  
2231 O OG1 . THR B 3   ? 0.6413 0.6198 0.7024 -0.0031 0.0416  0.1936  342 THR B OG1 
2232 C CG2 . THR B 3   ? 0.5606 0.5621 0.6574 0.0140  0.0059  0.1851  342 THR B CG2 
2233 N N   . VAL B 4   ? 0.5073 0.4993 0.7064 0.0035  0.0245  0.1566  343 VAL B N   
2234 C CA  . VAL B 4   ? 0.4806 0.4813 0.7046 -0.0004 0.0174  0.1364  343 VAL B CA  
2235 C C   . VAL B 4   ? 0.4651 0.4798 0.6773 0.0090  0.0008  0.1304  343 VAL B C   
2236 O O   . VAL B 4   ? 0.4817 0.4918 0.6944 0.0202  -0.0062 0.1420  343 VAL B O   
2237 C CB  . VAL B 4   ? 0.5272 0.5064 0.7799 -0.0036 0.0263  0.1361  343 VAL B CB  
2238 C CG1 . VAL B 4   ? 0.5465 0.5150 0.8116 -0.0177 0.0431  0.1371  343 VAL B CG1 
2239 C CG2 . VAL B 4   ? 0.5525 0.5144 0.8055 0.0120  0.0253  0.1569  343 VAL B CG2 
2240 N N   . TYR B 5   ? 0.4389 0.4714 0.6430 0.0044  -0.0054 0.1135  344 TYR B N   
2241 C CA  . TYR B 5   ? 0.4267 0.4727 0.6186 0.0100  -0.0186 0.1040  344 TYR B CA  
2242 C C   . TYR B 5   ? 0.4108 0.4544 0.6261 0.0060  -0.0217 0.0855  344 TYR B C   
2243 O O   . TYR B 5   ? 0.4037 0.4399 0.6335 -0.0062 -0.0158 0.0746  344 TYR B O   
2244 C CB  . TYR B 5   ? 0.4130 0.4736 0.5808 0.0064  -0.0198 0.0947  344 TYR B CB  
2245 C CG  . TYR B 5   ? 0.4349 0.4956 0.5722 0.0083  -0.0138 0.1085  344 TYR B CG  
2246 C CD1 . TYR B 5   ? 0.4509 0.5048 0.5893 0.0033  0.0017  0.1161  344 TYR B CD1 
2247 C CD2 . TYR B 5   ? 0.4497 0.5172 0.5563 0.0119  -0.0221 0.1126  344 TYR B CD2 
2248 C CE1 . TYR B 5   ? 0.4758 0.5245 0.5827 0.0016  0.0123  0.1261  344 TYR B CE1 
2249 C CE2 . TYR B 5   ? 0.4786 0.5418 0.5484 0.0082  -0.0146 0.1234  344 TYR B CE2 
2250 C CZ  . TYR B 5   ? 0.4907 0.5420 0.5594 0.0029  0.0045  0.1294  344 TYR B CZ  
2251 O OH  . TYR B 5   ? 0.5259 0.5677 0.5547 -0.0040 0.0169  0.1378  344 TYR B OH  
2252 N N   . LYS B 6   ? 0.4544 0.5047 0.6726 0.0139  -0.0304 0.0816  345 LYS B N   
2253 C CA  . LYS B 6   ? 0.4804 0.5270 0.7187 0.0088  -0.0296 0.0609  345 LYS B CA  
2254 C C   . LYS B 6   ? 0.4543 0.5133 0.6710 0.0015  -0.0357 0.0408  345 LYS B C   
2255 O O   . LYS B 6   ? 0.4423 0.5167 0.6356 0.0066  -0.0430 0.0431  345 LYS B O   
2256 C CB  . LYS B 6   ? 0.4895 0.5372 0.7541 0.0218  -0.0329 0.0671  345 LYS B CB  
2257 C CG  . LYS B 6   ? 0.5215 0.5496 0.8142 0.0291  -0.0236 0.0860  345 LYS B CG  
2258 C CD  . LYS B 6   ? 0.5984 0.6250 0.9326 0.0418  -0.0232 0.0892  345 LYS B CD  
2259 C CE  . LYS B 6   ? 0.5706 0.6228 0.9018 0.0579  -0.0440 0.1088  345 LYS B CE  
2260 N NZ  . LYS B 6   ? 0.5598 0.6137 0.9440 0.0735  -0.0451 0.1188  345 LYS B NZ  
2261 N N   . TYR B 7   ? 0.4334 0.4823 0.6541 -0.0129 -0.0314 0.0211  346 TYR B N   
2262 C CA  . TYR B 7   ? 0.4509 0.5055 0.6478 -0.0217 -0.0363 0.0041  346 TYR B CA  
2263 C C   . TYR B 7   ? 0.4630 0.5300 0.6504 -0.0148 -0.0415 -0.0052 346 TYR B C   
2264 O O   . TYR B 7   ? 0.4960 0.5690 0.6577 -0.0183 -0.0445 -0.0144 346 TYR B O   
2265 C CB  . TYR B 7   ? 0.4449 0.4822 0.6433 -0.0414 -0.0320 -0.0146 346 TYR B CB  
2266 C CG  . TYR B 7   ? 0.4508 0.4888 0.6215 -0.0519 -0.0378 -0.0296 346 TYR B CG  
2267 C CD1 . TYR B 7   ? 0.4430 0.4895 0.5986 -0.0532 -0.0445 -0.0211 346 TYR B CD1 
2268 C CD2 . TYR B 7   ? 0.4743 0.5025 0.6368 -0.0603 -0.0346 -0.0515 346 TYR B CD2 
2269 C CE1 . TYR B 7   ? 0.4432 0.4871 0.5746 -0.0612 -0.0498 -0.0314 346 TYR B CE1 
2270 C CE2 . TYR B 7   ? 0.5138 0.5376 0.6463 -0.0708 -0.0388 -0.0640 346 TYR B CE2 
2271 C CZ  . TYR B 7   ? 0.5108 0.5417 0.6270 -0.0705 -0.0474 -0.0526 346 TYR B CZ  
2272 O OH  . TYR B 7   ? 0.4374 0.4610 0.5250 -0.0793 -0.0516 -0.0618 346 TYR B OH  
2273 N N   . GLU B 8   ? 0.4168 0.4884 0.6276 -0.0052 -0.0422 -0.0024 347 GLU B N   
2274 C CA  . GLU B 8   ? 0.3805 0.4702 0.5874 0.0001  -0.0492 -0.0104 347 GLU B CA  
2275 C C   . GLU B 8   ? 0.4166 0.5239 0.5920 0.0056  -0.0580 0.0021  347 GLU B C   
2276 O O   . GLU B 8   ? 0.4387 0.5572 0.5921 0.0020  -0.0608 -0.0104 347 GLU B O   
2277 C CB  . GLU B 8   ? 0.4479 0.5441 0.6970 0.0110  -0.0504 -0.0050 347 GLU B CB  
2278 C CG  . GLU B 8   ? 0.5297 0.6048 0.8119 0.0037  -0.0351 -0.0221 347 GLU B CG  
2279 C CD  . GLU B 8   ? 0.5808 0.6629 0.9159 0.0177  -0.0334 -0.0149 347 GLU B CD  
2280 O OE1 . GLU B 8   ? 0.5551 0.6624 0.8991 0.0330  -0.0494 0.0057  347 GLU B OE1 
2281 O OE2 . GLU B 8   ? 0.7060 0.7679 1.0743 0.0124  -0.0156 -0.0291 347 GLU B OE2 
2282 N N   . ASP B 9   ? 0.4402 0.5468 0.6102 0.0118  -0.0592 0.0253  348 ASP B N   
2283 C CA  . ASP B 9   ? 0.3898 0.5076 0.5250 0.0132  -0.0632 0.0362  348 ASP B CA  
2284 C C   . ASP B 9   ? 0.3886 0.5007 0.4959 0.0049  -0.0539 0.0258  348 ASP B C   
2285 O O   . ASP B 9   ? 0.4474 0.5668 0.5240 0.0016  -0.0528 0.0210  348 ASP B O   
2286 C CB  . ASP B 9   ? 0.4455 0.5585 0.5800 0.0197  -0.0640 0.0635  348 ASP B CB  
2287 C CG  . ASP B 9   ? 0.5190 0.6348 0.6861 0.0305  -0.0732 0.0786  348 ASP B CG  
2288 O OD1 . ASP B 9   ? 0.4813 0.6159 0.6595 0.0346  -0.0853 0.0757  348 ASP B OD1 
2289 O OD2 . ASP B 9   ? 0.5785 0.6781 0.7644 0.0351  -0.0673 0.0936  348 ASP B OD2 
2290 N N   . LEU B 10  ? 0.3933 0.4922 0.5124 0.0006  -0.0470 0.0230  349 LEU B N   
2291 C CA  . LEU B 10  ? 0.3792 0.4746 0.4821 -0.0051 -0.0402 0.0161  349 LEU B CA  
2292 C C   . LEU B 10  ? 0.4237 0.5194 0.5109 -0.0106 -0.0416 -0.0051 349 LEU B C   
2293 O O   . LEU B 10  ? 0.3930 0.4888 0.4563 -0.0121 -0.0353 -0.0100 349 LEU B O   
2294 C CB  . LEU B 10  ? 0.3864 0.4730 0.5105 -0.0102 -0.0380 0.0196  349 LEU B CB  
2295 C CG  . LEU B 10  ? 0.4790 0.5626 0.6223 -0.0075 -0.0341 0.0376  349 LEU B CG  
2296 C CD1 . LEU B 10  ? 0.4334 0.5126 0.5981 -0.0169 -0.0333 0.0379  349 LEU B CD1 
2297 C CD2 . LEU B 10  ? 0.3696 0.4564 0.4972 -0.0021 -0.0256 0.0522  349 LEU B CD2 
2298 N N   . GLN B 11  ? 0.4274 0.5197 0.5276 -0.0148 -0.0460 -0.0190 350 GLN B N   
2299 C CA  . GLN B 11  ? 0.3961 0.4862 0.4800 -0.0217 -0.0451 -0.0408 350 GLN B CA  
2300 C C   . GLN B 11  ? 0.3745 0.4796 0.4378 -0.0190 -0.0454 -0.0445 350 GLN B C   
2301 O O   . GLN B 11  ? 0.3831 0.4845 0.4193 -0.0241 -0.0391 -0.0560 350 GLN B O   
2302 C CB  . GLN B 11  ? 0.3853 0.4684 0.4899 -0.0278 -0.0457 -0.0558 350 GLN B CB  
2303 C CG  . GLN B 11  ? 0.4322 0.4938 0.5355 -0.0414 -0.0429 -0.0648 350 GLN B CG  
2304 C CD  . GLN B 11  ? 0.4650 0.5141 0.5832 -0.0513 -0.0371 -0.0841 350 GLN B CD  
2305 O OE1 . GLN B 11  ? 0.4016 0.4577 0.5507 -0.0439 -0.0349 -0.0826 350 GLN B OE1 
2306 N NE2 . GLN B 11  ? 0.4878 0.5162 0.5848 -0.0688 -0.0334 -0.1016 350 GLN B NE2 
2307 N N   . ASN B 12  ? 0.3488 0.4704 0.4237 -0.0123 -0.0530 -0.0339 351 ASN B N   
2308 C CA  . ASN B 12  ? 0.3668 0.5070 0.4216 -0.0140 -0.0574 -0.0377 351 ASN B CA  
2309 C C   . ASN B 12  ? 0.3982 0.5364 0.4150 -0.0170 -0.0500 -0.0297 351 ASN B C   
2310 O O   . ASN B 12  ? 0.4638 0.6086 0.4509 -0.0250 -0.0466 -0.0408 351 ASN B O   
2311 C CB  . ASN B 12  ? 0.3889 0.5496 0.4700 -0.0064 -0.0721 -0.0243 351 ASN B CB  
2312 C CG  . ASN B 12  ? 0.3708 0.5323 0.4964 -0.0034 -0.0738 -0.0346 351 ASN B CG  
2313 O OD1 . ASN B 12  ? 0.3442 0.4938 0.4707 -0.0114 -0.0648 -0.0574 351 ASN B OD1 
2314 N ND2 . ASN B 12  ? 0.3612 0.5334 0.5234 0.0074  -0.0833 -0.0174 351 ASN B ND2 
2315 N N   . ALA B 13  ? 0.4163 0.5437 0.4339 -0.0127 -0.0441 -0.0125 352 ALA B N   
2316 C CA  . ALA B 13  ? 0.4584 0.5802 0.4433 -0.0167 -0.0314 -0.0059 352 ALA B CA  
2317 C C   . ALA B 13  ? 0.4827 0.5895 0.4553 -0.0204 -0.0142 -0.0188 352 ALA B C   
2318 O O   . ALA B 13  ? 0.5652 0.6658 0.5075 -0.0264 0.0012  -0.0220 352 ALA B O   
2319 C CB  . ALA B 13  ? 0.5074 0.6228 0.5016 -0.0116 -0.0282 0.0166  352 ALA B CB  
2320 N N   . THR B 14  ? 0.4334 0.5320 0.4276 -0.0182 -0.0158 -0.0253 353 THR B N   
2321 C CA  . THR B 14  ? 0.4902 0.5740 0.4766 -0.0201 -0.0032 -0.0332 353 THR B CA  
2322 C C   . THR B 14  ? 0.5112 0.5897 0.4831 -0.0267 -0.0046 -0.0548 353 THR B C   
2323 O O   . THR B 14  ? 0.5852 0.6481 0.5539 -0.0281 0.0013  -0.0599 353 THR B O   
2324 C CB  . THR B 14  ? 0.4471 0.5248 0.4641 -0.0156 -0.0057 -0.0213 353 THR B CB  
2325 O OG1 . THR B 14  ? 0.4354 0.5130 0.4686 -0.0189 -0.0207 -0.0266 353 THR B OG1 
2326 C CG2 . THR B 14  ? 0.3678 0.4506 0.4020 -0.0105 -0.0019 -0.0019 353 THR B CG2 
2327 N N   . ASN B 15  ? 0.4668 0.5580 0.4318 -0.0313 -0.0124 -0.0665 354 ASN B N   
2328 C CA  . ASN B 15  ? 0.4832 0.5701 0.4375 -0.0395 -0.0117 -0.0894 354 ASN B CA  
2329 C C   . ASN B 15  ? 0.4919 0.5619 0.4601 -0.0413 -0.0152 -0.0939 354 ASN B C   
2330 O O   . ASN B 15  ? 0.5809 0.6319 0.5307 -0.0475 -0.0080 -0.1054 354 ASN B O   
2331 C CB  . ASN B 15  ? 0.5762 0.6522 0.4944 -0.0467 0.0056  -0.1025 354 ASN B CB  
2332 C CG  . ASN B 15  ? 0.6597 0.7536 0.5553 -0.0538 0.0074  -0.1074 354 ASN B CG  
2333 O OD1 . ASN B 15  ? 0.6002 0.7019 0.4902 -0.0519 0.0073  -0.0920 354 ASN B OD1 
2334 N ND2 . ASN B 15  ? 0.6698 0.7697 0.5497 -0.0649 0.0090  -0.1291 354 ASN B ND2 
2335 N N   . PHE B 16  ? 0.4330 0.5068 0.4302 -0.0380 -0.0257 -0.0841 355 PHE B N   
2336 C CA  . PHE B 16  ? 0.4184 0.4755 0.4247 -0.0449 -0.0297 -0.0881 355 PHE B CA  
2337 C C   . PHE B 16  ? 0.4502 0.4918 0.4452 -0.0460 -0.0277 -0.0792 355 PHE B C   
2338 O O   . PHE B 16  ? 0.5828 0.6063 0.5670 -0.0561 -0.0306 -0.0860 355 PHE B O   
2339 C CB  . PHE B 16  ? 0.4351 0.4830 0.4336 -0.0564 -0.0270 -0.1131 355 PHE B CB  
2340 C CG  . PHE B 16  ? 0.4223 0.4872 0.4484 -0.0542 -0.0299 -0.1196 355 PHE B CG  
2341 C CD1 . PHE B 16  ? 0.3609 0.4495 0.3888 -0.0489 -0.0316 -0.1213 355 PHE B CD1 
2342 C CD2 . PHE B 16  ? 0.4024 0.4595 0.4546 -0.0585 -0.0306 -0.1232 355 PHE B CD2 
2343 C CE1 . PHE B 16  ? 0.3398 0.4482 0.4016 -0.0448 -0.0374 -0.1230 355 PHE B CE1 
2344 C CE2 . PHE B 16  ? 0.3401 0.4120 0.4272 -0.0537 -0.0310 -0.1271 355 PHE B CE2 
2345 C CZ  . PHE B 16  ? 0.3368 0.4366 0.4321 -0.0453 -0.0362 -0.1252 355 PHE B CZ  
2346 N N   . PHE B 17  ? 0.4449 0.4932 0.4435 -0.0363 -0.0224 -0.0629 356 PHE B N   
2347 C CA  . PHE B 17  ? 0.5088 0.5490 0.5144 -0.0333 -0.0215 -0.0483 356 PHE B CA  
2348 C C   . PHE B 17  ? 0.5645 0.5852 0.5450 -0.0367 -0.0141 -0.0566 356 PHE B C   
2349 O O   . PHE B 17  ? 0.6151 0.6232 0.5956 -0.0413 -0.0225 -0.0509 356 PHE B O   
2350 C CB  . PHE B 17  ? 0.4968 0.5371 0.5246 -0.0391 -0.0366 -0.0385 356 PHE B CB  
2351 C CG  . PHE B 17  ? 0.3968 0.4517 0.4512 -0.0354 -0.0402 -0.0280 356 PHE B CG  
2352 C CD1 . PHE B 17  ? 0.4019 0.4681 0.4760 -0.0257 -0.0346 -0.0101 356 PHE B CD1 
2353 C CD2 . PHE B 17  ? 0.3710 0.4249 0.4321 -0.0422 -0.0458 -0.0364 356 PHE B CD2 
2354 C CE1 . PHE B 17  ? 0.3801 0.4555 0.4750 -0.0235 -0.0361 -0.0002 356 PHE B CE1 
2355 C CE2 . PHE B 17  ? 0.3599 0.4228 0.4453 -0.0383 -0.0470 -0.0255 356 PHE B CE2 
2356 C CZ  . PHE B 17  ? 0.3388 0.4120 0.4388 -0.0292 -0.0430 -0.0070 356 PHE B CZ  
2357 N N   . SER B 18  ? 0.6120 0.6289 0.5686 -0.0360 0.0014  -0.0692 357 SER B N   
2358 C CA  . SER B 18  ? 0.6131 0.6072 0.5439 -0.0390 0.0134  -0.0780 357 SER B CA  
2359 C C   . SER B 18  ? 0.6753 0.6680 0.5897 -0.0358 0.0363  -0.0835 357 SER B C   
2360 O O   . SER B 18  ? 0.7622 0.7684 0.6637 -0.0404 0.0395  -0.0952 357 SER B O   
2361 C CB  . SER B 18  ? 0.8676 0.8485 0.7723 -0.0528 0.0104  -0.1012 357 SER B CB  
2362 O OG  . SER B 18  ? 0.8557 0.8434 0.7742 -0.0596 -0.0057 -0.1038 357 SER B OG  
2363 N N   . GLU B 19  ? 0.6757 0.6512 0.5911 -0.0292 0.0526  -0.0745 358 GLU B N   
2364 C CA  . GLU B 19  ? 0.6011 0.5666 0.4974 -0.0292 0.0812  -0.0820 358 GLU B CA  
2365 C C   . GLU B 19  ? 0.6284 0.6105 0.5379 -0.0252 0.0894  -0.0722 358 GLU B C   
2366 O O   . GLU B 19  ? 0.6898 0.6593 0.5937 -0.0238 0.1168  -0.0715 358 GLU B O   
2367 C CB  . GLU B 19  ? 0.7094 0.6702 0.5644 -0.0437 0.0897  -0.1098 358 GLU B CB  
2368 C CG  . GLU B 19  ? 0.8294 0.7642 0.6634 -0.0498 0.0925  -0.1224 358 GLU B CG  
2369 C CD  . GLU B 19  ? 0.8797 0.8132 0.6779 -0.0659 0.1014  -0.1519 358 GLU B CD  
2370 O OE1 . GLU B 19  ? 0.8529 0.8014 0.6378 -0.0725 0.1110  -0.1614 358 GLU B OE1 
2371 O OE2 . GLU B 19  ? 1.0361 0.9542 0.8184 -0.0742 0.0984  -0.1658 358 GLU B OE2 
2372 N N   . GLU B 20  ? 0.6699 0.6755 0.5946 -0.0246 0.0693  -0.0651 359 GLU B N   
2373 C CA  . GLU B 20  ? 0.5591 0.5766 0.5007 -0.0199 0.0745  -0.0502 359 GLU B CA  
2374 C C   . GLU B 20  ? 0.5475 0.5641 0.5330 -0.0079 0.0759  -0.0289 359 GLU B C   
2375 O O   . GLU B 20  ? 0.5322 0.5583 0.5386 -0.0040 0.0804  -0.0158 359 GLU B O   
2376 C CB  . GLU B 20  ? 0.5533 0.5929 0.4987 -0.0223 0.0525  -0.0474 359 GLU B CB  
2377 C CG  . GLU B 20  ? 0.5499 0.5984 0.4634 -0.0329 0.0468  -0.0650 359 GLU B CG  
2378 C CD  . GLU B 20  ? 0.6852 0.7448 0.5788 -0.0386 0.0508  -0.0606 359 GLU B CD  
2379 O OE1 . GLU B 20  ? 0.7635 0.8112 0.6435 -0.0410 0.0734  -0.0566 359 GLU B OE1 
2380 O OE2 . GLU B 20  ? 0.7105 0.7892 0.6024 -0.0415 0.0318  -0.0604 359 GLU B OE2 
2381 N N   . ASN B 21  ? 0.6365 0.6425 0.6365 -0.0032 0.0708  -0.0241 360 ASN B N   
2382 C CA  . ASN B 21  ? 0.5978 0.6089 0.6456 0.0074  0.0660  -0.0013 360 ASN B CA  
2383 C C   . ASN B 21  ? 0.6117 0.6141 0.6808 0.0165  0.0982  0.0069  360 ASN B C   
2384 O O   . ASN B 21  ? 0.6425 0.6227 0.6895 0.0159  0.1240  -0.0037 360 ASN B O   
2385 C CB  . ASN B 21  ? 0.6192 0.6200 0.6700 0.0076  0.0491  0.0035  360 ASN B CB  
2386 C CG  . ASN B 21  ? 0.7533 0.7685 0.8542 0.0145  0.0314  0.0291  360 ASN B CG  
2387 O OD1 . ASN B 21  ? 0.8125 0.8491 0.9437 0.0156  0.0241  0.0392  360 ASN B OD1 
2388 N ND2 . ASN B 21  ? 0.7609 0.7647 0.8702 0.0178  0.0230  0.0408  360 ASN B ND2 
2389 N N   . LYS B 22  ? 0.5911 0.6090 0.7045 0.0234  0.1003  0.0241  361 LYS B N   
2390 C CA  . LYS B 22  ? 0.6012 0.6120 0.7510 0.0333  0.1317  0.0344  361 LYS B CA  
2391 C C   . LYS B 22  ? 0.6497 0.6636 0.8505 0.0463  0.1217  0.0549  361 LYS B C   
2392 O O   . LYS B 22  ? 0.6646 0.6879 0.8685 0.0446  0.0876  0.0624  361 LYS B O   
2393 C CB  . LYS B 22  ? 0.6145 0.6403 0.7906 0.0331  0.1413  0.0425  361 LYS B CB  
2394 C CG  . LYS B 22  ? 0.5571 0.5821 0.6828 0.0199  0.1429  0.0286  361 LYS B CG  
2395 C CD  . LYS B 22  ? 0.6248 0.6273 0.7156 0.0118  0.1829  0.0156  361 LYS B CD  
2396 C CE  . LYS B 22  ? 0.6576 0.6401 0.6996 0.0046  0.1923  -0.0039 361 LYS B CE  
2397 N NZ  . LYS B 22  ? 0.6563 0.6212 0.6456 -0.0122 0.2224  -0.0201 361 LYS B NZ  
2398 N N   . ILE B 23  ? 0.6968 0.7015 0.9386 0.0583  0.1526  0.0648  362 ILE B N   
2399 C CA  . ILE B 23  ? 0.8341 0.8419 1.1308 0.0733  0.1443  0.0884  362 ILE B CA  
2400 C C   . ILE B 23  ? 0.8162 0.8581 1.1520 0.0733  0.1004  0.1092  362 ILE B C   
2401 O O   . ILE B 23  ? 1.0032 1.0492 1.3588 0.0780  0.0749  0.1270  362 ILE B O   
2402 C CB  . ILE B 23  ? 0.9285 0.9284 1.2828 0.0879  0.1867  0.0986  362 ILE B CB  
2403 C CG1 . ILE B 23  ? 0.8934 0.8520 1.2044 0.0851  0.2314  0.0775  362 ILE B CG1 
2404 C CG2 . ILE B 23  ? 0.8408 0.8550 1.2706 0.1061  0.1714  0.1304  362 ILE B CG2 
2405 C CD1 . ILE B 23  ? 0.9363 0.8792 1.3004 0.0971  0.2816  0.0834  362 ILE B CD1 
2406 N N   . LYS B 24  ? 0.6902 0.7549 1.0342 0.0659  0.0911  0.1078  363 LYS B N   
2407 C CA  . LYS B 24  ? 0.6746 0.7694 1.0469 0.0605  0.0513  0.1229  363 LYS B CA  
2408 C C   . LYS B 24  ? 0.6274 0.7150 0.9415 0.0455  0.0199  0.1108  363 LYS B C   
2409 O O   . LYS B 24  ? 0.6185 0.6911 0.8774 0.0370  0.0267  0.0884  363 LYS B O   
2410 C CB  . LYS B 24  ? 0.6555 0.7716 1.0516 0.0558  0.0558  0.1231  363 LYS B CB  
2411 C CG  . LYS B 24  ? 0.6202 0.7694 1.0588 0.0495  0.0207  0.1402  363 LYS B CG  
2412 C CD  . LYS B 24  ? 0.6427 0.8106 1.1480 0.0608  0.0085  0.1670  363 LYS B CD  
2413 C CE  . LYS B 24  ? 0.6663 0.8622 1.1889 0.0476  -0.0378 0.1821  363 LYS B CE  
2414 N NZ  . LYS B 24  ? 0.6292 0.8437 1.2101 0.0576  -0.0572 0.2118  363 LYS B NZ  
2415 N N   . GLY B 25  ? 0.5845 0.6832 0.9125 0.0407  -0.0144 0.1263  364 GLY B N   
2416 C CA  . GLY B 25  ? 0.6073 0.6969 0.8827 0.0228  -0.0421 0.1145  364 GLY B CA  
2417 C C   . GLY B 25  ? 0.6806 0.7799 0.9374 0.0090  -0.0498 0.1001  364 GLY B C   
2418 O O   . GLY B 25  ? 0.7374 0.8233 0.9474 -0.0052 -0.0621 0.0837  364 GLY B O   
2419 N N   . SER B 26  ? 0.6215 0.7409 0.9156 0.0127  -0.0401 0.1056  365 SER B N   
2420 C CA  . SER B 26  ? 0.5819 0.7074 0.8622 0.0015  -0.0443 0.0949  365 SER B CA  
2421 C C   . SER B 26  ? 0.4730 0.5887 0.7320 0.0073  -0.0168 0.0817  365 SER B C   
2422 O O   . SER B 26  ? 0.5168 0.6305 0.7528 -0.0005 -0.0205 0.0714  365 SER B O   
2423 C CB  . SER B 26  ? 0.6027 0.7568 0.9355 -0.0034 -0.0566 0.1112  365 SER B CB  
2424 O OG  . SER B 26  ? 0.7164 0.8823 1.0610 -0.0156 -0.0885 0.1229  365 SER B OG  
2425 N N   . VAL B 27  ? 0.5065 0.6144 0.7716 0.0192  0.0111  0.0825  366 VAL B N   
2426 C CA  . VAL B 27  ? 0.5006 0.5988 0.7420 0.0206  0.0375  0.0722  366 VAL B CA  
2427 C C   . VAL B 27  ? 0.4973 0.5746 0.6817 0.0179  0.0448  0.0532  366 VAL B C   
2428 O O   . VAL B 27  ? 0.5184 0.5823 0.6941 0.0218  0.0522  0.0498  366 VAL B O   
2429 C CB  . VAL B 27  ? 0.4320 0.5309 0.7106 0.0300  0.0690  0.0815  366 VAL B CB  
2430 C CG1 . VAL B 27  ? 0.4026 0.4844 0.6409 0.0263  0.0978  0.0689  366 VAL B CG1 
2431 C CG2 . VAL B 27  ? 0.4413 0.5648 0.7794 0.0308  0.0630  0.0983  366 VAL B CG2 
2432 N N   . TYR B 28  ? 0.4210 0.4960 0.5693 0.0111  0.0426  0.0418  367 TYR B N   
2433 C CA  . TYR B 28  ? 0.4672 0.5293 0.5653 0.0062  0.0476  0.0235  367 TYR B CA  
2434 C C   . TYR B 28  ? 0.4610 0.5207 0.5333 0.0026  0.0646  0.0202  367 TYR B C   
2435 O O   . TYR B 28  ? 0.4186 0.4866 0.5001 0.0017  0.0603  0.0292  367 TYR B O   
2436 C CB  . TYR B 28  ? 0.4795 0.5444 0.5592 -0.0009 0.0224  0.0131  367 TYR B CB  
2437 C CG  . TYR B 28  ? 0.5439 0.6030 0.6281 -0.0035 0.0074  0.0114  367 TYR B CG  
2438 C CD1 . TYR B 28  ? 0.5247 0.5928 0.6420 -0.0049 -0.0096 0.0254  367 TYR B CD1 
2439 C CD2 . TYR B 28  ? 0.5315 0.5752 0.5828 -0.0075 0.0096  -0.0043 367 TYR B CD2 
2440 C CE1 . TYR B 28  ? 0.4731 0.5339 0.5864 -0.0111 -0.0259 0.0256  367 TYR B CE1 
2441 C CE2 . TYR B 28  ? 0.5541 0.5875 0.6020 -0.0123 -0.0037 -0.0050 367 TYR B CE2 
2442 C CZ  . TYR B 28  ? 0.5064 0.5478 0.5831 -0.0145 -0.0225 0.0109  367 TYR B CZ  
2443 O OH  . TYR B 28  ? 0.5583 0.5874 0.6238 -0.0229 -0.0381 0.0121  367 TYR B OH  
2444 N N   . ARG B 29  ? 0.4962 0.5423 0.5321 -0.0019 0.0842  0.0074  368 ARG B N   
2445 C CA  . ARG B 29  ? 0.4574 0.5001 0.4556 -0.0110 0.0970  0.0030  368 ARG B CA  
2446 C C   . ARG B 29  ? 0.5306 0.5861 0.5062 -0.0161 0.0707  -0.0015 368 ARG B C   
2447 O O   . ARG B 29  ? 0.4918 0.5490 0.4486 -0.0199 0.0608  -0.0158 368 ARG B O   
2448 C CB  . ARG B 29  ? 0.5015 0.5250 0.4635 -0.0189 0.1257  -0.0117 368 ARG B CB  
2449 C CG  . ARG B 29  ? 0.5851 0.6013 0.5039 -0.0332 0.1435  -0.0150 368 ARG B CG  
2450 C CD  . ARG B 29  ? 0.6681 0.6713 0.5348 -0.0484 0.1594  -0.0357 368 ARG B CD  
2451 N NE  . ARG B 29  ? 0.7398 0.7293 0.5612 -0.0666 0.1837  -0.0393 368 ARG B NE  
2452 C CZ  . ARG B 29  ? 0.8257 0.7881 0.6330 -0.0752 0.2258  -0.0483 368 ARG B CZ  
2453 N NH1 . ARG B 29  ? 0.8279 0.7753 0.6681 -0.0639 0.2478  -0.0523 368 ARG B NH1 
2454 N NH2 . ARG B 29  ? 0.8864 0.8340 0.6443 -0.0967 0.2476  -0.0527 368 ARG B NH2 
2455 N N   . ALA B 30  ? 0.5329 0.5969 0.5143 -0.0158 0.0609  0.0113  369 ALA B N   
2456 C CA  . ALA B 30  ? 0.4965 0.5729 0.4663 -0.0178 0.0372  0.0118  369 ALA B CA  
2457 C C   . ALA B 30  ? 0.5625 0.6387 0.4869 -0.0286 0.0420  0.0122  369 ALA B C   
2458 O O   . ALA B 30  ? 0.5206 0.5865 0.4300 -0.0335 0.0586  0.0216  369 ALA B O   
2459 C CB  . ALA B 30  ? 0.4353 0.5180 0.4391 -0.0112 0.0234  0.0274  369 ALA B CB  
2460 N N   . SER B 31  ? 0.6737 0.7614 0.5756 -0.0345 0.0274  0.0019  370 SER B N   
2461 C CA  . SER B 31  ? 0.6588 0.7511 0.5139 -0.0486 0.0262  0.0020  370 SER B CA  
2462 C C   . SER B 31  ? 0.6613 0.7722 0.5257 -0.0445 -0.0026 0.0182  370 SER B C   
2463 O O   . SER B 31  ? 0.7482 0.8784 0.6244 -0.0426 -0.0231 0.0123  370 SER B O   
2464 C CB  . SER B 31  ? 0.6576 0.7532 0.4831 -0.0604 0.0304  -0.0208 370 SER B CB  
2465 O OG  . SER B 31  ? 0.8359 0.9481 0.6863 -0.0544 0.0099  -0.0302 370 SER B OG  
2466 N N   . PHE B 32  ? 0.6704 0.7741 0.5331 -0.0427 -0.0023 0.0393  371 PHE B N   
2467 C CA  . PHE B 32  ? 0.7046 0.8213 0.5703 -0.0394 -0.0272 0.0594  371 PHE B CA  
2468 C C   . PHE B 32  ? 0.7861 0.9088 0.5952 -0.0574 -0.0344 0.0651  371 PHE B C   
2469 O O   . PHE B 32  ? 0.7930 0.9039 0.5564 -0.0748 -0.0142 0.0530  371 PHE B O   
2470 C CB  . PHE B 32  ? 0.6990 0.8012 0.5848 -0.0308 -0.0231 0.0806  371 PHE B CB  
2471 C CG  . PHE B 32  ? 0.6713 0.7708 0.6114 -0.0170 -0.0207 0.0769  371 PHE B CG  
2472 C CD1 . PHE B 32  ? 0.6499 0.7620 0.6273 -0.0073 -0.0387 0.0733  371 PHE B CD1 
2473 C CD2 . PHE B 32  ? 0.6001 0.6847 0.5549 -0.0161 0.0004  0.0769  371 PHE B CD2 
2474 C CE1 . PHE B 32  ? 0.5888 0.6953 0.6074 -0.0002 -0.0357 0.0685  371 PHE B CE1 
2475 C CE2 . PHE B 32  ? 0.4611 0.5460 0.4622 -0.0076 -0.0008 0.0744  371 PHE B CE2 
2476 C CZ  . PHE B 32  ? 0.4932 0.5874 0.5215 -0.0013 -0.0188 0.0697  371 PHE B CZ  
2477 N N   . LYS B 33  ? 0.7999 0.9408 0.6127 -0.0544 -0.0633 0.0845  372 LYS B N   
2478 C CA  . LYS B 33  ? 0.8837 1.0333 0.6412 -0.0736 -0.0771 0.0956  372 LYS B CA  
2479 C C   . LYS B 33  ? 0.9251 1.0438 0.6298 -0.0889 -0.0548 0.1061  372 LYS B C   
2480 O O   . LYS B 33  ? 1.0536 1.1577 0.7652 -0.0815 -0.0559 0.1291  372 LYS B O   
2481 C CB  . LYS B 33  ? 0.8520 1.0270 0.6335 -0.0638 -0.1147 0.1217  372 LYS B CB  
2482 C CG  . LYS B 33  ? 0.8775 1.0682 0.6030 -0.0850 -0.1373 0.1370  372 LYS B CG  
2483 C CD  . LYS B 33  ? 0.9828 1.1938 0.6800 -0.1050 -0.1378 0.1102  372 LYS B CD  
2484 C CE  . LYS B 33  ? 0.9889 1.2205 0.6295 -0.1304 -0.1646 0.1255  372 LYS B CE  
2485 N NZ  . LYS B 33  ? 0.8030 1.0562 0.4168 -0.1529 -0.1645 0.0971  372 LYS B NZ  
2486 N N   . GLY B 34  ? 0.9220 1.0267 0.5738 -0.1116 -0.0307 0.0878  373 GLY B N   
2487 C CA  . GLY B 34  ? 0.9402 1.0108 0.5415 -0.1294 -0.0016 0.0924  373 GLY B CA  
2488 C C   . GLY B 34  ? 1.0023 1.0480 0.6300 -0.1221 0.0389  0.0761  373 GLY B C   
2489 O O   . GLY B 34  ? 0.9691 1.0140 0.6046 -0.1232 0.0569  0.0518  373 GLY B O   
2490 N N   . ASP B 35  ? 1.1802 1.2062 0.8250 -0.1147 0.0533  0.0905  374 ASP B N   
2491 C CA  . ASP B 35  ? 0.9606 0.9682 0.6400 -0.1073 0.0895  0.0785  374 ASP B CA  
2492 C C   . ASP B 35  ? 0.8591 0.8860 0.6062 -0.0840 0.0800  0.0680  374 ASP B C   
2493 O O   . ASP B 35  ? 0.8961 0.9429 0.6786 -0.0685 0.0502  0.0767  374 ASP B O   
2494 C CB  . ASP B 35  ? 0.9615 0.9495 0.6529 -0.1041 0.1028  0.0968  374 ASP B CB  
2495 C CG  . ASP B 35  ? 1.1429 1.1029 0.7608 -0.1308 0.1196  0.1054  374 ASP B CG  
2496 O OD1 . ASP B 35  ? 1.2521 1.2083 0.8080 -0.1538 0.1212  0.0964  374 ASP B OD1 
2497 O OD2 . ASP B 35  ? 1.2688 1.2090 0.8874 -0.1317 0.1322  0.1204  374 ASP B OD2 
2498 N N   . ASP B 36  ? 0.7330 0.7511 0.4969 -0.0826 0.1073  0.0498  375 ASP B N   
2499 C CA  . ASP B 36  ? 0.6230 0.6546 0.4442 -0.0637 0.1001  0.0414  375 ASP B CA  
2500 C C   . ASP B 36  ? 0.5797 0.6092 0.4565 -0.0495 0.1065  0.0529  375 ASP B C   
2501 O O   . ASP B 36  ? 0.6029 0.6214 0.4763 -0.0531 0.1162  0.0666  375 ASP B O   
2502 C CB  . ASP B 36  ? 0.6384 0.6609 0.4521 -0.0684 0.1238  0.0198  375 ASP B CB  
2503 C CG  . ASP B 36  ? 0.7586 0.7901 0.5302 -0.0805 0.1113  0.0050  375 ASP B CG  
2504 O OD1 . ASP B 36  ? 0.8274 0.8756 0.5778 -0.0855 0.0829  0.0130  375 ASP B OD1 
2505 O OD2 . ASP B 36  ? 0.7763 0.7988 0.5394 -0.0849 0.1300  -0.0138 375 ASP B OD2 
2506 N N   . ALA B 37  ? 0.5630 0.5678 0.4004 -0.0449 0.0945  0.0672  376 ALA B N   
2507 C CA  . ALA B 37  ? 0.5075 0.5317 0.3731 -0.0447 0.0922  0.0611  376 ALA B CA  
2508 C C   . ALA B 37  ? 0.4187 0.4479 0.3043 -0.0429 0.0922  0.0602  376 ALA B C   
2509 O O   . ALA B 37  ? 0.4768 0.5013 0.3651 -0.0432 0.0925  0.0656  376 ALA B O   
2510 C CB  . ALA B 37  ? 0.4365 0.4596 0.3135 -0.0417 0.0949  0.0673  376 ALA B CB  
2511 N N   . ALA B 38  ? 0.4009 0.4376 0.2985 -0.0393 0.0976  0.0599  377 ALA B N   
2512 C CA  . ALA B 38  ? 0.4012 0.4425 0.3146 -0.0367 0.0996  0.0624  377 ALA B CA  
2513 C C   . ALA B 38  ? 0.4299 0.4726 0.3460 -0.0399 0.1001  0.0604  377 ALA B C   
2514 O O   . ALA B 38  ? 0.4250 0.4689 0.3410 -0.0436 0.1039  0.0582  377 ALA B O   
2515 C CB  . ALA B 38  ? 0.4098 0.4597 0.3339 -0.0303 0.1077  0.0674  377 ALA B CB  
2516 N N   . VAL B 39  ? 0.4398 0.4827 0.3585 -0.0384 0.0979  0.0616  378 VAL B N   
2517 C CA  . VAL B 39  ? 0.4207 0.4611 0.3335 -0.0416 0.1033  0.0574  378 VAL B CA  
2518 C C   . VAL B 39  ? 0.4174 0.4830 0.3390 -0.0388 0.1026  0.0664  378 VAL B C   
2519 O O   . VAL B 39  ? 0.4377 0.5248 0.3758 -0.0323 0.0951  0.0771  378 VAL B O   
2520 C CB  . VAL B 39  ? 0.4281 0.4670 0.3372 -0.0421 0.1024  0.0570  378 VAL B CB  
2521 C CG1 . VAL B 39  ? 0.4677 0.4922 0.3618 -0.0458 0.1141  0.0472  378 VAL B CG1 
2522 C CG2 . VAL B 39  ? 0.4102 0.4482 0.3240 -0.0414 0.0979  0.0614  378 VAL B CG2 
2523 N N   . LYS B 40  ? 0.4253 0.5004 0.3433 -0.0439 0.1070  0.0666  379 LYS B N   
2524 C CA  . LYS B 40  ? 0.4737 0.5948 0.4012 -0.0504 0.0970  0.0771  379 LYS B CA  
2525 C C   . LYS B 40  ? 0.4985 0.6448 0.4021 -0.0647 0.0953  0.0715  379 LYS B C   
2526 O O   . LYS B 40  ? 0.5068 0.6552 0.3967 -0.0828 0.0997  0.0603  379 LYS B O   
2527 C CB  . LYS B 40  ? 0.4072 0.5497 0.3532 -0.0569 0.0954  0.0860  379 LYS B CB  
2528 C CG  . LYS B 40  ? 0.4780 0.6911 0.4426 -0.0671 0.0799  0.1072  379 LYS B CG  
2529 C CD  . LYS B 40  ? 0.4461 0.6772 0.4427 -0.0629 0.0806  0.1255  379 LYS B CD  
2530 C CE  . LYS B 40  ? 0.4795 0.7864 0.5054 -0.0659 0.0640  0.1578  379 LYS B CE  
2531 N NZ  . LYS B 40  ? 0.6088 0.9292 0.6736 -0.0530 0.0688  0.1825  379 LYS B NZ  
2532 N N   . ILE B 41  ? 0.5787 0.7473 0.4744 -0.0621 0.0898  0.0764  380 ILE B N   
2533 C CA  . ILE B 41  ? 0.5383 0.7322 0.3971 -0.0784 0.0899  0.0656  380 ILE B CA  
2534 C C   . ILE B 41  ? 0.5607 0.8282 0.4146 -0.1109 0.0712  0.0692  380 ILE B C   
2535 O O   . ILE B 41  ? 0.5405 0.8630 0.4250 -0.1073 0.0557  0.0956  380 ILE B O   
2536 C CB  . ILE B 41  ? 0.5038 0.7001 0.3559 -0.0624 0.0923  0.0738  380 ILE B CB  
2537 C CG1 . ILE B 41  ? 0.5175 0.6600 0.3903 -0.0416 0.1020  0.0769  380 ILE B CG1 
2538 C CG2 . ILE B 41  ? 0.4649 0.6583 0.2644 -0.0712 0.1034  0.0554  380 ILE B CG2 
2539 C CD1 . ILE B 41  ? 0.3911 0.5521 0.2705 -0.0311 0.1014  0.0898  380 ILE B CD1 
2540 N N   . LEU B 42  ? 0.5501 0.8219 0.3674 -0.1473 0.0732  0.0432  381 LEU B N   
2541 C CA  . LEU B 42  ? 0.5670 0.9131 0.3698 -0.1937 0.0529  0.0420  381 LEU B CA  
2542 C C   . LEU B 42  ? 0.6929 1.0423 0.4263 -0.2262 0.0536  0.0041  381 LEU B C   
2543 O O   . LEU B 42  ? 0.7364 1.0137 0.4322 -0.2258 0.0778  -0.0320 381 LEU B O   
2544 C CB  . LEU B 42  ? 0.6649 1.0090 0.4837 -0.2223 0.0542  0.0395  381 LEU B CB  
2545 C CG  . LEU B 42  ? 0.5709 0.9246 0.4569 -0.1916 0.0488  0.0785  381 LEU B CG  
2546 C CD1 . LEU B 42  ? 0.4572 0.8050 0.3668 -0.2150 0.0527  0.0790  381 LEU B CD1 
2547 C CD2 . LEU B 42  ? 0.5066 0.9421 0.4231 -0.1863 0.0252  0.1165  381 LEU B CD2 
2548 N N   . LYS B 43  ? 0.7361 1.1662 0.4564 -0.2508 0.0287  0.0134  382 LYS B N   
2549 C CA  . LYS B 43  ? 0.8587 1.2875 0.5093 -0.2780 0.0264  -0.0258 382 LYS B CA  
2550 C C   . LYS B 43  ? 0.9004 1.2849 0.5056 -0.3300 0.0295  -0.0798 382 LYS B C   
2551 O O   . LYS B 43  ? 1.0209 1.4214 0.6497 -0.3618 0.0182  -0.0765 382 LYS B O   
2552 C CB  . LYS B 43  ? 0.8662 1.3994 0.5206 -0.2940 -0.0034 0.0017  382 LYS B CB  
2553 C CG  . LYS B 43  ? 0.9649 1.4991 0.5408 -0.3248 -0.0100 -0.0407 382 LYS B CG  
2554 C CD  . LYS B 43  ? 0.9734 1.4520 0.5049 -0.2841 0.0157  -0.0556 382 LYS B CD  
2555 C CE  . LYS B 43  ? 1.0183 1.4884 0.4611 -0.3109 0.0131  -0.1017 382 LYS B CE  
2556 N NZ  . LYS B 43  ? 1.0611 1.4332 0.4545 -0.3361 0.0336  -0.1674 382 LYS B NZ  
2557 N N   . GLY B 44  ? 0.9245 1.2473 0.4676 -0.3370 0.0468  -0.1296 383 GLY B N   
2558 C CA  . GLY B 44  ? 1.0315 1.2981 0.5370 -0.3855 0.0521  -0.1882 383 GLY B CA  
2559 C C   . GLY B 44  ? 1.2099 1.3677 0.7217 -0.3752 0.0946  -0.2180 383 GLY B C   
2560 O O   . GLY B 44  ? 1.1061 1.2547 0.6629 -0.3664 0.1032  -0.1960 383 GLY B O   
2561 N N   . ASP B 45  ? 1.7198 1.7953 1.1880 -0.3732 0.1256  -0.2645 384 ASP B N   
2562 C CA  . ASP B 45  ? 1.7440 1.7136 1.2284 -0.3704 0.1702  -0.2938 384 ASP B CA  
2563 C C   . ASP B 45  ? 1.7466 1.7031 1.2706 -0.4156 0.1603  -0.3093 384 ASP B C   
2564 O O   . ASP B 45  ? 1.7610 1.6469 1.3267 -0.4063 0.1946  -0.3129 384 ASP B O   
2565 C CB  . ASP B 45  ? 1.8659 1.7576 1.3002 -0.3713 0.2015  -0.3430 384 ASP B CB  
2566 C CG  . ASP B 45  ? 1.9126 1.6948 1.3791 -0.3616 0.2551  -0.3636 384 ASP B CG  
2567 O OD1 . ASP B 45  ? 1.9291 1.6802 1.4360 -0.3925 0.2583  -0.3786 384 ASP B OD1 
2568 O OD2 . ASP B 45  ? 1.9193 1.6504 1.3810 -0.3201 0.2945  -0.3578 384 ASP B OD2 
2569 N N   . VAL B 46  ? 1.3543 1.3816 0.8798 -0.4605 0.1130  -0.3098 385 VAL B N   
2570 C CA  . VAL B 46  ? 1.2710 1.2990 0.8569 -0.5001 0.0948  -0.3110 385 VAL B CA  
2571 C C   . VAL B 46  ? 1.1021 1.2254 0.7476 -0.4986 0.0604  -0.2505 385 VAL B C   
2572 O O   . VAL B 46  ? 1.0980 1.3175 0.7522 -0.5186 0.0165  -0.2222 385 VAL B O   
2573 C CB  . VAL B 46  ? 1.3306 1.3709 0.8948 -0.5496 0.0653  -0.3458 385 VAL B CB  
2574 C CG1 . VAL B 46  ? 1.2461 1.2472 0.8840 -0.5784 0.0634  -0.3531 385 VAL B CG1 
2575 C CG2 . VAL B 46  ? 1.3747 1.3488 0.8613 -0.5479 0.0915  -0.4000 385 VAL B CG2 
2576 N N   . SER B 47  ? 0.9757 1.0741 0.6833 -0.4471 0.0878  -0.2071 386 SER B N   
2577 C CA  . SER B 47  ? 0.7952 0.9530 0.5864 -0.4307 0.0718  -0.1445 386 SER B CA  
2578 C C   . SER B 47  ? 0.7710 0.8726 0.6346 -0.4354 0.0930  -0.1413 386 SER B C   
2579 O O   . SER B 47  ? 0.7705 0.8988 0.6997 -0.4081 0.0962  -0.0898 386 SER B O   
2580 C CB  . SER B 47  ? 0.8164 0.9980 0.6179 -0.3692 0.0842  -0.0953 386 SER B CB  
2581 O OG  . SER B 47  ? 0.9237 1.1685 0.6767 -0.3642 0.0645  -0.0865 386 SER B OG  
2582 N N   . SER B 48  ? 0.8756 0.8967 0.7277 -0.4682 0.1123  -0.1952 387 SER B N   
2583 C CA  . SER B 48  ? 0.9085 0.8740 0.8375 -0.4685 0.1366  -0.1877 387 SER B CA  
2584 C C   . SER B 48  ? 0.8338 0.8676 0.8363 -0.4818 0.1008  -0.1462 387 SER B C   
2585 O O   . SER B 48  ? 0.8194 0.8533 0.8962 -0.4503 0.1148  -0.0999 387 SER B O   
2586 C CB  . SER B 48  ? 0.9683 0.8394 0.8740 -0.4896 0.1610  -0.2488 387 SER B CB  
2587 O OG  . SER B 48  ? 1.0382 0.9351 0.9274 -0.5394 0.1218  -0.2798 387 SER B OG  
2588 N N   . GLU B 49  ? 0.8535 0.9495 0.8370 -0.5236 0.0549  -0.1570 388 GLU B N   
2589 C CA  . GLU B 49  ? 0.8298 0.9974 0.8910 -0.5337 0.0218  -0.1096 388 GLU B CA  
2590 C C   . GLU B 49  ? 0.7260 0.9532 0.8320 -0.4831 0.0268  -0.0391 388 GLU B C   
2591 O O   . GLU B 49  ? 0.7272 0.9681 0.9153 -0.4628 0.0327  0.0051  388 GLU B O   
2592 C CB  . GLU B 49  ? 0.8967 1.1345 0.9230 -0.5799 -0.0290 -0.1233 388 GLU B CB  
2593 C CG  . GLU B 49  ? 0.8944 1.2030 1.0070 -0.5953 -0.0624 -0.0766 388 GLU B CG  
2594 C CD  . GLU B 49  ? 0.8298 1.2402 0.9645 -0.5644 -0.0797 -0.0072 388 GLU B CD  
2595 O OE1 . GLU B 49  ? 0.9060 1.3389 0.9861 -0.5382 -0.0734 0.0013  388 GLU B OE1 
2596 O OE2 . GLU B 49  ? 0.7951 1.2601 1.0064 -0.5637 -0.0960 0.0404  388 GLU B OE2 
2597 N N   . ILE B 50  ? 0.6824 0.9408 0.7367 -0.4580 0.0286  -0.0283 389 ILE B N   
2598 C CA  . ILE B 50  ? 0.6698 0.9682 0.7567 -0.4014 0.0376  0.0313  389 ILE B CA  
2599 C C   . ILE B 50  ? 0.6719 0.9070 0.7928 -0.3535 0.0782  0.0474  389 ILE B C   
2600 O O   . ILE B 50  ? 0.6492 0.9010 0.7990 -0.3037 0.0883  0.0896  389 ILE B O   
2601 C CB  . ILE B 50  ? 0.6410 0.9750 0.6685 -0.3826 0.0335  0.0359  389 ILE B CB  
2602 C CG1 . ILE B 50  ? 0.7478 1.1693 0.7513 -0.4198 -0.0094 0.0398  389 ILE B CG1 
2603 C CG2 . ILE B 50  ? 0.5234 0.8638 0.5781 -0.3141 0.0487  0.0840  389 ILE B CG2 
2604 C CD1 . ILE B 50  ? 0.7414 1.1444 0.6738 -0.4762 -0.0249 -0.0252 389 ILE B CD1 
2605 N N   . ASN B 51  ? 0.6700 0.8288 0.7859 -0.3636 0.1038  0.0137  390 ASN B N   
2606 C CA  . ASN B 51  ? 0.5840 0.6973 0.7395 -0.3183 0.1372  0.0394  390 ASN B CA  
2607 C C   . ASN B 51  ? 0.6278 0.7586 0.8715 -0.3203 0.1363  0.0750  390 ASN B C   
2608 O O   . ASN B 51  ? 0.6851 0.7756 0.9636 -0.3178 0.1527  0.0822  390 ASN B O   
2609 C CB  . ASN B 51  ? 0.6822 0.7124 0.8100 -0.3181 0.1677  0.0018  390 ASN B CB  
2610 C CG  . ASN B 51  ? 0.6999 0.7126 0.7575 -0.2953 0.1799  -0.0149 390 ASN B CG  
2611 O OD1 . ASN B 51  ? 0.5926 0.6546 0.6132 -0.2955 0.1599  -0.0108 390 ASN B OD1 
2612 N ND2 . ASN B 51  ? 0.6816 0.6300 0.7295 -0.2716 0.2120  -0.0264 390 ASN B ND2 
2613 N N   . ILE B 52  ? 0.6249 0.8190 0.8987 -0.3246 0.1164  0.0989  391 ILE B N   
2614 C CA  . ILE B 52  ? 0.5096 0.7194 0.8371 -0.3024 0.1338  0.1312  391 ILE B CA  
2615 C C   . ILE B 52  ? 0.4636 0.6682 0.7432 -0.2449 0.1514  0.1503  391 ILE B C   
2616 O O   . ILE B 52  ? 0.4616 0.6724 0.7548 -0.2200 0.1580  0.1766  391 ILE B O   
2617 C CB  . ILE B 52  ? 0.5268 0.8084 0.8904 -0.3282 0.0982  0.1524  391 ILE B CB  
2618 C CG1 . ILE B 52  ? 0.5930 0.8801 0.9731 -0.3950 0.0659  0.1193  391 ILE B CG1 
2619 C CG2 . ILE B 52  ? 0.5276 0.8246 0.9375 -0.3071 0.1112  0.1897  391 ILE B CG2 
2620 C CD1 . ILE B 52  ? 0.6176 0.9838 0.9952 -0.4269 0.0194  0.1303  391 ILE B CD1 
2621 N N   . LEU B 53  ? 0.5706 0.5220 0.4784 -0.0078 0.1110  -0.0317 392 LEU B N   
2622 C CA  . LEU B 53  ? 0.6020 0.5640 0.4949 0.0110  0.0946  -0.0137 392 LEU B CA  
2623 C C   . LEU B 53  ? 0.5408 0.4864 0.4304 0.0472  0.1064  -0.0011 392 LEU B C   
2624 O O   . LEU B 53  ? 0.5711 0.5132 0.4504 0.0663  0.0996  0.0162  392 LEU B O   
2625 C CB  . LEU B 53  ? 0.5740 0.5721 0.4555 -0.0009 0.0748  -0.0213 392 LEU B CB  
2626 C CG  . LEU B 53  ? 0.5137 0.5305 0.3922 -0.0332 0.0630  -0.0319 392 LEU B CG  
2627 C CD1 . LEU B 53  ? 0.5303 0.5748 0.4001 -0.0450 0.0552  -0.0446 392 LEU B CD1 
2628 C CD2 . LEU B 53  ? 0.4872 0.5072 0.3578 -0.0377 0.0472  -0.0169 392 LEU B CD2 
2629 N N   . LYS B 54  ? 0.5629 0.5008 0.4593 0.0587  0.1235  -0.0094 393 LYS B N   
2630 C CA  . LYS B 54  ? 0.5490 0.4730 0.4409 0.0972  0.1355  0.0042  393 LYS B CA  
2631 C C   . LYS B 54  ? 0.5651 0.4522 0.4540 0.1158  0.1493  0.0242  393 LYS B C   
2632 O O   . LYS B 54  ? 0.5896 0.4734 0.4653 0.1485  0.1488  0.0417  393 LYS B O   
2633 C CB  . LYS B 54  ? 0.6244 0.5366 0.5270 0.1058  0.1580  -0.0070 393 LYS B CB  
2634 C CG  . LYS B 54  ? 0.6722 0.5702 0.5898 0.0738  0.1722  -0.0274 393 LYS B CG  
2635 C CD  . LYS B 54  ? 0.6680 0.5461 0.5965 0.0838  0.1996  -0.0385 393 LYS B CD  
2636 C CE  . LYS B 54  ? 0.6825 0.5075 0.6192 0.0995  0.2322  -0.0290 393 LYS B CE  
2637 N NZ  . LYS B 54  ? 0.6733 0.4730 0.6232 0.1007  0.2626  -0.0442 393 LYS B NZ  
2638 N N   . ARG B 55  ? 0.5703 0.4319 0.4716 0.0957  0.1621  0.0211  394 ARG B N   
2639 C CA  . ARG B 55  ? 0.5925 0.4174 0.4939 0.1099  0.1786  0.0389  394 ARG B CA  
2640 C C   . ARG B 55  ? 0.5524 0.3896 0.4436 0.1066  0.1578  0.0517  394 ARG B C   
2641 O O   . ARG B 55  ? 0.5264 0.3356 0.4172 0.1172  0.1703  0.0669  394 ARG B O   
2642 C CB  . ARG B 55  ? 0.5967 0.3910 0.5210 0.0879  0.2038  0.0270  394 ARG B CB  
2643 C CG  . ARG B 55  ? 0.6503 0.4386 0.5870 0.0787  0.2209  0.0063  394 ARG B CG  
2644 C CD  . ARG B 55  ? 0.7305 0.4659 0.6802 0.0900  0.2614  0.0084  394 ARG B CD  
2645 N NE  . ARG B 55  ? 0.7820 0.5099 0.7496 0.0681  0.2792  -0.0181 394 ARG B NE  
2646 C CZ  . ARG B 55  ? 0.8306 0.5646 0.8171 0.0294  0.2807  -0.0416 394 ARG B CZ  
2647 N NH1 . ARG B 55  ? 0.7960 0.5458 0.7884 0.0092  0.2649  -0.0409 394 ARG B NH1 
2648 N NH2 . ARG B 55  ? 0.8618 0.5883 0.8621 0.0113  0.2984  -0.0673 394 ARG B NH2 
2649 N N   . ILE B 56  ? 0.5040 0.3794 0.3873 0.0923  0.1294  0.0460  395 ILE B N   
2650 C CA  . ILE B 56  ? 0.5017 0.3883 0.3740 0.0904  0.1104  0.0576  395 ILE B CA  
2651 C C   . ILE B 56  ? 0.5178 0.4189 0.3695 0.1188  0.0990  0.0676  395 ILE B C   
2652 O O   . ILE B 56  ? 0.5287 0.4630 0.3745 0.1136  0.0808  0.0585  395 ILE B O   
2653 C CB  . ILE B 56  ? 0.4930 0.4086 0.3685 0.0577  0.0894  0.0461  395 ILE B CB  
2654 C CG1 . ILE B 56  ? 0.5211 0.4300 0.4168 0.0309  0.0989  0.0334  395 ILE B CG1 
2655 C CG2 . ILE B 56  ? 0.4722 0.3950 0.3361 0.0585  0.0727  0.0592  395 ILE B CG2 
2656 C CD1 . ILE B 56  ? 0.4746 0.4145 0.3702 0.0017  0.0785  0.0230  395 ILE B CD1 
2657 N N   . ASN B 57  ? 0.4573 0.3348 0.2980 0.1490  0.1107  0.0856  396 ASN B N   
2658 C CA  . ASN B 57  ? 0.4584 0.3515 0.2782 0.1803  0.1012  0.0947  396 ASN B CA  
2659 C C   . ASN B 57  ? 0.4254 0.3155 0.2354 0.1854  0.0948  0.1048  396 ASN B C   
2660 O O   . ASN B 57  ? 0.4370 0.3046 0.2544 0.1850  0.1113  0.1095  396 ASN B O   
2661 C CB  . ASN B 57  ? 0.5440 0.4193 0.3598 0.2144  0.1218  0.1027  396 ASN B CB  
2662 C CG  . ASN B 57  ? 0.6628 0.5496 0.4940 0.2066  0.1274  0.0860  396 ASN B CG  
2663 O OD1 . ASN B 57  ? 0.6604 0.5850 0.4958 0.1898  0.1085  0.0700  396 ASN B OD1 
2664 N ND2 . ASN B 57  ? 0.7494 0.6011 0.5893 0.2180  0.1560  0.0892  396 ASN B ND2 
2665 N N   . HIS B 58  ? 0.4014 0.3241 0.2066 0.1788  0.0713  0.0969  397 HIS B N   
2666 C CA  . HIS B 58  ? 0.4032 0.3308 0.2126 0.1735  0.0643  0.0943  397 HIS B CA  
2667 C C   . HIS B 58  ? 0.3781 0.3396 0.1832 0.1724  0.0433  0.0838  397 HIS B C   
2668 O O   . HIS B 58  ? 0.3757 0.3577 0.1805 0.1591  0.0298  0.0764  397 HIS B O   
2669 C CB  . HIS B 58  ? 0.3803 0.2950 0.2021 0.1483  0.0624  0.0960  397 HIS B CB  
2670 C CG  . HIS B 58  ? 0.3706 0.2830 0.1972 0.1465  0.0615  0.0958  397 HIS B CG  
2671 N ND1 . HIS B 58  ? 0.3553 0.2848 0.1807 0.1391  0.0453  0.0895  397 HIS B ND1 
2672 C CD2 . HIS B 58  ? 0.3833 0.2776 0.2150 0.1508  0.0768  0.1011  397 HIS B CD2 
2673 C CE1 . HIS B 58  ? 0.3590 0.2797 0.1869 0.1405  0.0504  0.0914  397 HIS B CE1 
2674 N NE2 . HIS B 58  ? 0.3749 0.2766 0.2064 0.1475  0.0687  0.0982  397 HIS B NE2 
2675 N N   . ALA B 59  ? 0.3860 0.3536 0.1864 0.1843  0.0424  0.0820  398 ALA B N   
2676 C CA  . ALA B 59  ? 0.3836 0.3818 0.1812 0.1846  0.0253  0.0713  398 ALA B CA  
2677 C C   . ALA B 59  ? 0.3627 0.3676 0.1679 0.1551  0.0106  0.0649  398 ALA B C   
2678 O O   . ALA B 59  ? 0.3720 0.4030 0.1767 0.1487  -0.0026 0.0542  398 ALA B O   
2679 C CB  . ALA B 59  ? 0.4022 0.4012 0.1905 0.2014  0.0288  0.0716  398 ALA B CB  
2680 N N   . ASN B 60  ? 0.3919 0.3752 0.2044 0.1367  0.0138  0.0706  399 ASN B N   
2681 C CA  . ASN B 60  ? 0.3619 0.3484 0.1792 0.1099  0.0027  0.0670  399 ASN B CA  
2682 C C   . ASN B 60  ? 0.3814 0.3675 0.2015 0.0916  0.0011  0.0676  399 ASN B C   
2683 O O   . ASN B 60  ? 0.3898 0.3708 0.2144 0.0706  -0.0033 0.0689  399 ASN B O   
2684 C CB  . ASN B 60  ? 0.3560 0.3247 0.1791 0.1035  0.0059  0.0721  399 ASN B CB  
2685 C CG  . ASN B 60  ? 0.3553 0.3247 0.1709 0.1206  0.0083  0.0707  399 ASN B CG  
2686 O OD1 . ASN B 60  ? 0.3548 0.3089 0.1712 0.1300  0.0191  0.0762  399 ASN B OD1 
2687 N ND2 . ASN B 60  ? 0.3430 0.3322 0.1500 0.1242  -0.0012 0.0623  399 ASN B ND2 
2688 N N   . ILE B 61  ? 0.3936 0.3860 0.2088 0.1009  0.0055  0.0667  400 ILE B N   
2689 C CA  . ILE B 61  ? 0.4065 0.4030 0.2189 0.0845  0.0053  0.0647  400 ILE B CA  
2690 C C   . ILE B 61  ? 0.3591 0.3839 0.1655 0.0890  0.0010  0.0528  400 ILE B C   
2691 O O   . ILE B 61  ? 0.3482 0.3784 0.1509 0.1142  0.0064  0.0536  400 ILE B O   
2692 C CB  . ILE B 61  ? 0.4220 0.3936 0.2332 0.0898  0.0213  0.0754  400 ILE B CB  
2693 C CG1 . ILE B 61  ? 0.3970 0.3477 0.2204 0.0825  0.0250  0.0839  400 ILE B CG1 
2694 C CG2 . ILE B 61  ? 0.4134 0.3954 0.2330 0.0670  0.0218  0.0639  400 ILE B CG2 
2695 C CD1 . ILE B 61  ? 0.3733 0.2972 0.2008 0.0862  0.0443  0.0935  400 ILE B CD1 
2696 N N   . ILE B 62  ? 0.3924 0.4360 0.1996 0.0653  -0.0076 0.0414  401 ILE B N   
2697 C CA  . ILE B 62  ? 0.3906 0.4663 0.1989 0.0649  -0.0112 0.0259  401 ILE B CA  
2698 C C   . ILE B 62  ? 0.4163 0.4889 0.2326 0.0779  0.0010  0.0243  401 ILE B C   
2699 O O   . ILE B 62  ? 0.4151 0.4676 0.2387 0.0672  0.0108  0.0264  401 ILE B O   
2700 C CB  . ILE B 62  ? 0.3638 0.4512 0.1759 0.0333  -0.0166 0.0150  401 ILE B CB  
2701 C CG1 . ILE B 62  ? 0.3550 0.4731 0.1755 0.0295  -0.0224 -0.0019 401 ILE B CG1 
2702 C CG2 . ILE B 62  ? 0.4112 0.4954 0.2284 0.0184  -0.0093 0.0114  401 ILE B CG2 
2703 C CD1 . ILE B 62  ? 0.3637 0.4859 0.1861 0.0390  -0.0290 -0.0030 401 ILE B CD1 
2704 N N   . ARG B 63  ? 0.4254 0.5179 0.2431 0.1012  0.0012  0.0195  402 ARG B N   
2705 C CA  . ARG B 63  ? 0.4392 0.5227 0.2647 0.1206  0.0158  0.0211  402 ARG B CA  
2706 C C   . ARG B 63  ? 0.4412 0.5468 0.2810 0.1064  0.0183  0.0033  402 ARG B C   
2707 O O   . ARG B 63  ? 0.4408 0.5821 0.2844 0.0985  0.0076  -0.0104 402 ARG B O   
2708 C CB  . ARG B 63  ? 0.5000 0.5931 0.3171 0.1598  0.0160  0.0289  402 ARG B CB  
2709 C CG  . ARG B 63  ? 0.5505 0.6365 0.3750 0.1842  0.0324  0.0312  402 ARG B CG  
2710 C CD  . ARG B 63  ? 0.6607 0.7597 0.4730 0.2272  0.0312  0.0416  402 ARG B CD  
2711 N NE  . ARG B 63  ? 0.7151 0.8674 0.5270 0.2305  0.0102  0.0278  402 ARG B NE  
2712 C CZ  . ARG B 63  ? 0.8734 1.0667 0.6993 0.2374  0.0059  0.0131  402 ARG B CZ  
2713 N NH1 . ARG B 63  ? 0.7222 0.9078 0.5617 0.2435  0.0213  0.0113  402 ARG B NH1 
2714 N NH2 . ARG B 63  ? 0.8753 1.1197 0.7035 0.2374  -0.0132 -0.0018 402 ARG B NH2 
2715 N N   . LEU B 64  ? 0.4821 0.5661 0.3309 0.1021  0.0342  0.0020  403 LEU B N   
2716 C CA  . LEU B 64  ? 0.4584 0.5591 0.3200 0.0922  0.0403  -0.0147 403 LEU B CA  
2717 C C   . LEU B 64  ? 0.4886 0.6041 0.3561 0.1261  0.0470  -0.0151 403 LEU B C   
2718 O O   . LEU B 64  ? 0.5500 0.6381 0.4171 0.1510  0.0628  -0.0036 403 LEU B O   
2719 C CB  . LEU B 64  ? 0.4614 0.5335 0.3296 0.0740  0.0556  -0.0185 403 LEU B CB  
2720 C CG  . LEU B 64  ? 0.4833 0.5677 0.3627 0.0622  0.0648  -0.0370 403 LEU B CG  
2721 C CD1 . LEU B 64  ? 0.4212 0.5399 0.2987 0.0379  0.0508  -0.0502 403 LEU B CD1 
2722 C CD2 . LEU B 64  ? 0.4745 0.5296 0.3594 0.0447  0.0804  -0.0425 403 LEU B CD2 
2723 N N   . SER B 65  ? 0.4949 0.6541 0.3689 0.1279  0.0363  -0.0281 404 SER B N   
2724 C CA  . SER B 65  ? 0.4670 0.6504 0.3486 0.1624  0.0396  -0.0292 404 SER B CA  
2725 C C   . SER B 65  ? 0.4894 0.6636 0.3852 0.1653  0.0592  -0.0368 404 SER B C   
2726 O O   . SER B 65  ? 0.6227 0.7807 0.5200 0.1976  0.0743  -0.0268 404 SER B O   
2727 C CB  . SER B 65  ? 0.4800 0.7197 0.3684 0.1612  0.0213  -0.0438 404 SER B CB  
2728 O OG  . SER B 65  ? 0.5233 0.7694 0.3984 0.1574  0.0052  -0.0393 404 SER B OG  
2729 N N   . GLY B 66  ? 0.4822 0.6648 0.3869 0.1333  0.0610  -0.0538 405 GLY B N   
2730 C CA  . GLY B 66  ? 0.5104 0.6852 0.4279 0.1327  0.0801  -0.0642 405 GLY B CA  
2731 C C   . GLY B 66  ? 0.4224 0.5943 0.3405 0.0914  0.0818  -0.0798 405 GLY B C   
2732 O O   . GLY B 66  ? 0.4186 0.5840 0.3255 0.0657  0.0708  -0.0778 405 GLY B O   
2733 N N   . PHE B 67  ? 0.4160 0.5932 0.3460 0.0867  0.0962  -0.0948 406 PHE B N   
2734 C CA  . PHE B 67  ? 0.4550 0.6310 0.3823 0.0494  0.0993  -0.1105 406 PHE B CA  
2735 C C   . PHE B 67  ? 0.4550 0.6541 0.3971 0.0499  0.1115  -0.1288 406 PHE B C   
2736 O O   . PHE B 67  ? 0.4580 0.6658 0.4141 0.0804  0.1210  -0.1281 406 PHE B O   
2737 C CB  . PHE B 67  ? 0.5033 0.6359 0.4235 0.0344  0.1112  -0.1090 406 PHE B CB  
2738 C CG  . PHE B 67  ? 0.4904 0.5962 0.4216 0.0489  0.1370  -0.1144 406 PHE B CG  
2739 C CD1 . PHE B 67  ? 0.5821 0.6622 0.5176 0.0828  0.1491  -0.0990 406 PHE B CD1 
2740 C CD2 . PHE B 67  ? 0.4686 0.5722 0.4041 0.0291  0.1514  -0.1347 406 PHE B CD2 
2741 C CE1 . PHE B 67  ? 0.5675 0.6169 0.5130 0.0968  0.1768  -0.1031 406 PHE B CE1 
2742 C CE2 . PHE B 67  ? 0.5080 0.5831 0.4543 0.0414  0.1780  -0.1414 406 PHE B CE2 
2743 C CZ  . PHE B 67  ? 0.5536 0.6000 0.5057 0.0753  0.1916  -0.1253 406 PHE B CZ  
2744 N N   . CYS B 68  ? 0.4369 0.6461 0.3746 0.0172  0.1118  -0.1441 407 CYS B N   
2745 C CA  . CYS B 68  ? 0.4403 0.6712 0.3902 0.0124  0.1245  -0.1631 407 CYS B CA  
2746 C C   . CYS B 68  ? 0.4405 0.6598 0.3764 -0.0236 0.1308  -0.1765 407 CYS B C   
2747 O O   . CYS B 68  ? 0.4462 0.6629 0.3641 -0.0475 0.1180  -0.1724 407 CYS B O   
2748 C CB  . CYS B 68  ? 0.4176 0.6983 0.3797 0.0147  0.1135  -0.1697 407 CYS B CB  
2749 S SG  . CYS B 68  ? 0.5186 0.8303 0.4980 0.0054  0.1299  -0.1941 407 CYS B SG  
2750 N N   . VAL B 69  ? 0.4641 0.6770 0.4070 -0.0256 0.1511  -0.1924 408 VAL B N   
2751 C CA  . VAL B 69  ? 0.5413 0.7427 0.4722 -0.0570 0.1545  -0.2035 408 VAL B CA  
2752 C C   . VAL B 69  ? 0.5296 0.7524 0.4733 -0.0596 0.1616  -0.2154 408 VAL B C   
2753 O O   . VAL B 69  ? 0.5597 0.7852 0.5222 -0.0366 0.1765  -0.2206 408 VAL B O   
2754 C CB  . VAL B 69  ? 0.6519 0.8146 0.5795 -0.0608 0.1702  -0.2095 408 VAL B CB  
2755 C CG1 . VAL B 69  ? 0.7427 0.9007 0.6580 -0.0929 0.1685  -0.2205 408 VAL B CG1 
2756 C CG2 . VAL B 69  ? 0.6196 0.7600 0.5398 -0.0561 0.1650  -0.1966 408 VAL B CG2 
2757 N N   . TYR B 70  ? 0.5196 0.7563 0.4538 -0.0857 0.1524  -0.2181 409 TYR B N   
2758 C CA  . TYR B 70  ? 0.5216 0.7794 0.4674 -0.0912 0.1598  -0.2296 409 TYR B CA  
2759 C C   . TYR B 70  ? 0.5690 0.8232 0.4966 -0.1226 0.1556  -0.2321 409 TYR B C   
2760 O O   . TYR B 70  ? 0.5755 0.8328 0.4895 -0.1371 0.1411  -0.2211 409 TYR B O   
2761 C CB  . TYR B 70  ? 0.5059 0.8020 0.4696 -0.0800 0.1526  -0.2284 409 TYR B CB  
2762 C CG  . TYR B 70  ? 0.5170 0.8379 0.4926 -0.0917 0.1588  -0.2404 409 TYR B CG  
2763 C CD1 . TYR B 70  ? 0.5479 0.8776 0.5433 -0.0767 0.1747  -0.2518 409 TYR B CD1 
2764 C CD2 . TYR B 70  ? 0.5228 0.8559 0.4902 -0.1167 0.1506  -0.2394 409 TYR B CD2 
2765 C CE1 . TYR B 70  ? 0.5195 0.8723 0.5265 -0.0877 0.1813  -0.2633 409 TYR B CE1 
2766 C CE2 . TYR B 70  ? 0.5408 0.8947 0.5190 -0.1281 0.1588  -0.2509 409 TYR B CE2 
2767 C CZ  . TYR B 70  ? 0.5540 0.9190 0.5522 -0.1142 0.1736  -0.2635 409 TYR B CZ  
2768 O OH  . TYR B 70  ? 0.5813 0.9672 0.5910 -0.1258 0.1824  -0.2753 409 TYR B OH  
2769 N N   . LYS B 71  ? 0.5445 0.7914 0.4718 -0.1310 0.1693  -0.2451 410 LYS B N   
2770 C CA  . LYS B 71  ? 0.5437 0.7909 0.4542 -0.1574 0.1678  -0.2482 410 LYS B CA  
2771 C C   . LYS B 71  ? 0.5999 0.8322 0.4878 -0.1724 0.1543  -0.2372 410 LYS B C   
2772 O O   . LYS B 71  ? 0.5910 0.8297 0.4643 -0.1873 0.1446  -0.2278 410 LYS B O   
2773 C CB  . LYS B 71  ? 0.5647 0.8377 0.4793 -0.1658 0.1651  -0.2472 410 LYS B CB  
2774 C CG  . LYS B 71  ? 0.6720 0.9548 0.5936 -0.1717 0.1808  -0.2624 410 LYS B CG  
2775 C CD  . LYS B 71  ? 0.6777 0.9609 0.6221 -0.1494 0.1959  -0.2740 410 LYS B CD  
2776 C CE  . LYS B 71  ? 0.6482 0.9410 0.6006 -0.1545 0.2122  -0.2889 410 LYS B CE  
2777 N NZ  . LYS B 71  ? 0.6041 0.8786 0.5333 -0.1759 0.2176  -0.2953 410 LYS B NZ  
2778 N N   . GLY B 72  ? 0.6183 0.8304 0.5047 -0.1670 0.1554  -0.2381 411 GLY B N   
2779 C CA  . GLY B 72  ? 0.7472 0.9487 0.6164 -0.1805 0.1443  -0.2308 411 GLY B CA  
2780 C C   . GLY B 72  ? 0.8084 1.0113 0.6706 -0.1777 0.1263  -0.2109 411 GLY B C   
2781 O O   . GLY B 72  ? 0.9219 1.1184 0.7717 -0.1867 0.1162  -0.2030 411 GLY B O   
2782 N N   . ASN B 73  ? 0.7251 0.9383 0.5961 -0.1653 0.1220  -0.2030 412 ASN B N   
2783 C CA  . ASN B 73  ? 0.6946 0.9071 0.5602 -0.1613 0.1063  -0.1849 412 ASN B CA  
2784 C C   . ASN B 73  ? 0.6446 0.8544 0.5220 -0.1388 0.1080  -0.1841 412 ASN B C   
2785 O O   . ASN B 73  ? 0.6210 0.8409 0.5143 -0.1236 0.1191  -0.1938 412 ASN B O   
2786 C CB  . ASN B 73  ? 0.6612 0.8894 0.5248 -0.1687 0.0995  -0.1759 412 ASN B CB  
2787 C CG  . ASN B 73  ? 0.7418 0.9643 0.5861 -0.1853 0.0923  -0.1648 412 ASN B CG  
2788 O OD1 . ASN B 73  ? 0.7732 0.9872 0.6067 -0.1920 0.0915  -0.1660 412 ASN B OD1 
2789 N ND2 . ASN B 73  ? 0.7658 0.9940 0.6056 -0.1913 0.0883  -0.1549 412 ASN B ND2 
2790 N N   . THR B 74  ? 0.6672 0.8645 0.5370 -0.1343 0.0979  -0.1715 413 THR B N   
2791 C CA  . THR B 74  ? 0.6042 0.7964 0.4806 -0.1116 0.1002  -0.1684 413 THR B CA  
2792 C C   . THR B 74  ? 0.5039 0.7081 0.3781 -0.1057 0.0846  -0.1534 413 THR B C   
2793 O O   . THR B 74  ? 0.5158 0.7160 0.3796 -0.1192 0.0714  -0.1406 413 THR B O   
2794 C CB  . THR B 74  ? 0.6235 0.7894 0.4935 -0.1108 0.1046  -0.1678 413 THR B CB  
2795 O OG1 . THR B 74  ? 0.7536 0.9066 0.6303 -0.1151 0.1225  -0.1849 413 THR B OG1 
2796 C CG2 . THR B 74  ? 0.5165 0.6710 0.3976 -0.0834 0.1048  -0.1552 413 THR B CG2 
2797 N N   . TYR B 75  ? 0.4602 0.6798 0.3463 -0.0833 0.0869  -0.1547 414 TYR B N   
2798 C CA  . TYR B 75  ? 0.4236 0.6592 0.3105 -0.0766 0.0726  -0.1446 414 TYR B CA  
2799 C C   . TYR B 75  ? 0.4322 0.6519 0.3243 -0.0502 0.0672  -0.1297 414 TYR B C   
2800 O O   . TYR B 75  ? 0.4480 0.6645 0.3543 -0.0254 0.0763  -0.1304 414 TYR B O   
2801 C CB  . TYR B 75  ? 0.3379 0.6095 0.2438 -0.0713 0.0742  -0.1556 414 TYR B CB  
2802 C CG  . TYR B 75  ? 0.4208 0.7002 0.3318 -0.0918 0.0821  -0.1666 414 TYR B CG  
2803 C CD1 . TYR B 75  ? 0.4545 0.7340 0.3744 -0.0875 0.0976  -0.1798 414 TYR B CD1 
2804 C CD2 . TYR B 75  ? 0.3546 0.6387 0.2615 -0.1142 0.0765  -0.1630 414 TYR B CD2 
2805 C CE1 . TYR B 75  ? 0.4402 0.7263 0.3628 -0.1056 0.1050  -0.1896 414 TYR B CE1 
2806 C CE2 . TYR B 75  ? 0.3965 0.6871 0.3056 -0.1315 0.0856  -0.1722 414 TYR B CE2 
2807 C CZ  . TYR B 75  ? 0.4797 0.7725 0.3961 -0.1275 0.0988  -0.1857 414 TYR B CZ  
2808 O OH  . TYR B 75  ? 0.4633 0.7619 0.3803 -0.1443 0.1080  -0.1948 414 TYR B OH  
2809 N N   . LEU B 76  ? 0.3888 0.5966 0.2685 -0.0538 0.0540  -0.1148 415 LEU B N   
2810 C CA  . LEU B 76  ? 0.3965 0.5877 0.2779 -0.0301 0.0488  -0.0990 415 LEU B CA  
2811 C C   . LEU B 76  ? 0.3704 0.5863 0.2560 -0.0170 0.0367  -0.0957 415 LEU B C   
2812 O O   . LEU B 76  ? 0.4092 0.6372 0.2878 -0.0345 0.0276  -0.0968 415 LEU B O   
2813 C CB  . LEU B 76  ? 0.3714 0.5345 0.2383 -0.0415 0.0430  -0.0857 415 LEU B CB  
2814 C CG  . LEU B 76  ? 0.4198 0.5623 0.2845 -0.0552 0.0534  -0.0913 415 LEU B CG  
2815 C CD1 . LEU B 76  ? 0.3758 0.5000 0.2298 -0.0659 0.0452  -0.0789 415 LEU B CD1 
2816 C CD2 . LEU B 76  ? 0.3984 0.5238 0.2777 -0.0349 0.0703  -0.0947 415 LEU B CD2 
2817 N N   . VAL B 77  ? 0.3230 0.5462 0.2192 0.0142  0.0376  -0.0921 416 VAL B N   
2818 C CA  . VAL B 77  ? 0.3415 0.5944 0.2423 0.0300  0.0252  -0.0918 416 VAL B CA  
2819 C C   . VAL B 77  ? 0.3596 0.5891 0.2474 0.0456  0.0176  -0.0730 416 VAL B C   
2820 O O   . VAL B 77  ? 0.3386 0.5481 0.2254 0.0717  0.0245  -0.0614 416 VAL B O   
2821 C CB  . VAL B 77  ? 0.3602 0.6448 0.2797 0.0578  0.0295  -0.1003 416 VAL B CB  
2822 C CG1 . VAL B 77  ? 0.3340 0.6612 0.2604 0.0693  0.0143  -0.1058 416 VAL B CG1 
2823 C CG2 . VAL B 77  ? 0.3206 0.6212 0.2538 0.0436  0.0415  -0.1180 416 VAL B CG2 
2824 N N   . TYR B 78  ? 0.3639 0.5931 0.2411 0.0301  0.0061  -0.0694 417 TYR B N   
2825 C CA  . TYR B 78  ? 0.3656 0.5720 0.2292 0.0410  -0.0006 -0.0525 417 TYR B CA  
2826 C C   . TYR B 78  ? 0.3484 0.5833 0.2119 0.0574  -0.0128 -0.0552 417 TYR B C   
2827 O O   . TYR B 78  ? 0.3220 0.5953 0.1962 0.0507  -0.0182 -0.0720 417 TYR B O   
2828 C CB  . TYR B 78  ? 0.3987 0.5819 0.2495 0.0139  -0.0040 -0.0454 417 TYR B CB  
2829 C CG  . TYR B 78  ? 0.4171 0.5714 0.2650 0.0018  0.0049  -0.0398 417 TYR B CG  
2830 C CD1 . TYR B 78  ? 0.4158 0.5400 0.2615 0.0153  0.0102  -0.0259 417 TYR B CD1 
2831 C CD2 . TYR B 78  ? 0.3493 0.5080 0.1966 -0.0238 0.0086  -0.0497 417 TYR B CD2 
2832 C CE1 . TYR B 78  ? 0.4317 0.5344 0.2786 0.0019  0.0182  -0.0248 417 TYR B CE1 
2833 C CE2 . TYR B 78  ? 0.3642 0.5025 0.2086 -0.0355 0.0150  -0.0477 417 TYR B CE2 
2834 C CZ  . TYR B 78  ? 0.3928 0.5049 0.2390 -0.0234 0.0193  -0.0365 417 TYR B CZ  
2835 O OH  . TYR B 78  ? 0.4406 0.5372 0.2876 -0.0373 0.0257  -0.0384 417 TYR B OH  
2836 N N   . GLU B 79  ? 0.3694 0.5863 0.2206 0.0784  -0.0162 -0.0398 418 GLU B N   
2837 C CA  . GLU B 79  ? 0.3545 0.5919 0.2038 0.0897  -0.0283 -0.0416 418 GLU B CA  
2838 C C   . GLU B 79  ? 0.3939 0.6293 0.2513 0.0566  -0.0332 -0.0494 418 GLU B C   
2839 O O   . GLU B 79  ? 0.4260 0.6311 0.2758 0.0347  -0.0300 -0.0420 418 GLU B O   
2840 C CB  . GLU B 79  ? 0.3829 0.5892 0.2183 0.1121  -0.0276 -0.0215 418 GLU B CB  
2841 C CG  . GLU B 79  ? 0.3604 0.5699 0.1998 0.1117  -0.0363 -0.0223 418 GLU B CG  
2842 C CD  . GLU B 79  ? 0.4578 0.6288 0.2845 0.1236  -0.0323 -0.0034 418 GLU B CD  
2843 O OE1 . GLU B 79  ? 0.4538 0.5939 0.2716 0.1282  -0.0230 0.0109  418 GLU B OE1 
2844 O OE2 . GLU B 79  ? 0.3479 0.5202 0.1744 0.1273  -0.0371 -0.0042 418 GLU B OE2 
2845 N N   . PHE B 80  ? 0.3643 0.6328 0.2363 0.0549  -0.0395 -0.0640 419 PHE B N   
2846 C CA  . PHE B 80  ? 0.3840 0.6510 0.2621 0.0259  -0.0402 -0.0730 419 PHE B CA  
2847 C C   . PHE B 80  ? 0.3924 0.6374 0.2599 0.0281  -0.0447 -0.0651 419 PHE B C   
2848 O O   . PHE B 80  ? 0.3731 0.6328 0.2415 0.0494  -0.0503 -0.0659 419 PHE B O   
2849 C CB  . PHE B 80  ? 0.3804 0.6961 0.2817 0.0196  -0.0416 -0.0960 419 PHE B CB  
2850 C CG  . PHE B 80  ? 0.3601 0.6744 0.2676 -0.0098 -0.0385 -0.1064 419 PHE B CG  
2851 C CD1 . PHE B 80  ? 0.3955 0.6922 0.3007 -0.0367 -0.0293 -0.1061 419 PHE B CD1 
2852 C CD2 . PHE B 80  ? 0.3679 0.6981 0.2816 -0.0097 -0.0432 -0.1167 419 PHE B CD2 
2853 C CE1 . PHE B 80  ? 0.4198 0.7138 0.3281 -0.0619 -0.0233 -0.1146 419 PHE B CE1 
2854 C CE2 . PHE B 80  ? 0.4133 0.7411 0.3316 -0.0368 -0.0376 -0.1277 419 PHE B CE2 
2855 C CZ  . PHE B 80  ? 0.4132 0.7221 0.3284 -0.0625 -0.0268 -0.1260 419 PHE B CZ  
2856 N N   . ALA B 81  ? 0.4106 0.6216 0.2670 0.0077  -0.0416 -0.0575 420 ALA B N   
2857 C CA  . ALA B 81  ? 0.3813 0.5712 0.2264 0.0061  -0.0442 -0.0526 420 ALA B CA  
2858 C C   . ALA B 81  ? 0.3846 0.5909 0.2378 -0.0153 -0.0430 -0.0702 420 ALA B C   
2859 O O   . ALA B 81  ? 0.3877 0.5888 0.2429 -0.0379 -0.0360 -0.0734 420 ALA B O   
2860 C CB  . ALA B 81  ? 0.4029 0.5478 0.2307 0.0006  -0.0406 -0.0333 420 ALA B CB  
2861 N N   . GLU B 82  ? 0.3441 0.5710 0.2023 -0.0089 -0.0482 -0.0822 421 GLU B N   
2862 C CA  . GLU B 82  ? 0.4102 0.6622 0.2824 -0.0290 -0.0456 -0.1042 421 GLU B CA  
2863 C C   . GLU B 82  ? 0.4148 0.6386 0.2728 -0.0471 -0.0407 -0.1048 421 GLU B C   
2864 O O   . GLU B 82  ? 0.4217 0.6599 0.2908 -0.0693 -0.0340 -0.1232 421 GLU B O   
2865 C CB  . GLU B 82  ? 0.4541 0.7515 0.3426 -0.0141 -0.0531 -0.1213 421 GLU B CB  
2866 C CG  . GLU B 82  ? 0.4526 0.7421 0.3267 0.0094  -0.0609 -0.1129 421 GLU B CG  
2867 C CD  . GLU B 82  ? 0.4580 0.7983 0.3480 0.0256  -0.0684 -0.1302 421 GLU B CD  
2868 O OE1 . GLU B 82  ? 0.5951 0.9762 0.5086 0.0138  -0.0673 -0.1518 421 GLU B OE1 
2869 O OE2 . GLU B 82  ? 0.5638 0.9049 0.4430 0.0504  -0.0743 -0.1225 421 GLU B OE2 
2870 N N   . ASN B 83  ? 0.3535 0.5386 0.1885 -0.0390 -0.0416 -0.0862 422 ASN B N   
2871 C CA  . ASN B 83  ? 0.3924 0.5509 0.2115 -0.0540 -0.0356 -0.0861 422 ASN B CA  
2872 C C   . ASN B 83  ? 0.3982 0.5219 0.2027 -0.0668 -0.0270 -0.0674 422 ASN B C   
2873 O O   . ASN B 83  ? 0.4405 0.5325 0.2253 -0.0669 -0.0236 -0.0539 422 ASN B O   
2874 C CB  . ASN B 83  ? 0.3658 0.5101 0.1688 -0.0356 -0.0416 -0.0806 422 ASN B CB  
2875 C CG  . ASN B 83  ? 0.3699 0.5477 0.1841 -0.0323 -0.0471 -0.1029 422 ASN B CG  
2876 O OD1 . ASN B 83  ? 0.3756 0.5815 0.2089 -0.0503 -0.0436 -0.1250 422 ASN B OD1 
2877 N ND2 . ASN B 83  ? 0.3972 0.5742 0.2015 -0.0101 -0.0543 -0.0972 422 ASN B ND2 
2878 N N   . ASN B 84  ? 0.3501 0.4806 0.1637 -0.0768 -0.0230 -0.0654 423 ASN B N   
2879 C CA  . ASN B 84  ? 0.3919 0.4948 0.1930 -0.0930 -0.0138 -0.0498 423 ASN B CA  
2880 C C   . ASN B 84  ? 0.3717 0.4438 0.1601 -0.0756 -0.0175 -0.0243 423 ASN B C   
2881 O O   . ASN B 84  ? 0.3688 0.4429 0.1607 -0.0521 -0.0254 -0.0190 423 ASN B O   
2882 C CB  . ASN B 84  ? 0.4201 0.5094 0.2097 -0.1213 -0.0005 -0.0590 423 ASN B CB  
2883 C CG  . ASN B 84  ? 0.4350 0.5583 0.2459 -0.1377 0.0046  -0.0883 423 ASN B CG  
2884 O OD1 . ASN B 84  ? 0.4196 0.5594 0.2424 -0.1498 0.0103  -0.0948 423 ASN B OD1 
2885 N ND2 . ASN B 84  ? 0.4104 0.5452 0.2284 -0.1383 0.0036  -0.1064 423 ASN B ND2 
2886 N N   . SER B 85  ? 0.3412 0.3831 0.1161 -0.0861 -0.0102 -0.0080 424 SER B N   
2887 C CA  . SER B 85  ? 0.3952 0.4124 0.1688 -0.0698 -0.0123 0.0148  424 SER B CA  
2888 C C   . SER B 85  ? 0.4197 0.4123 0.1796 -0.0662 -0.0089 0.0226  424 SER B C   
2889 O O   . SER B 85  ? 0.4410 0.4264 0.1855 -0.0824 -0.0020 0.0123  424 SER B O   
2890 C CB  . SER B 85  ? 0.3722 0.3775 0.1488 -0.0775 -0.0080 0.0279  424 SER B CB  
2891 O OG  . SER B 85  ? 0.3978 0.3795 0.1614 -0.0903 0.0014  0.0356  424 SER B OG  
2892 N N   . LEU B 86  ? 0.3668 0.3467 0.1340 -0.0458 -0.0112 0.0385  425 LEU B N   
2893 C CA  . LEU B 86  ? 0.3729 0.3295 0.1325 -0.0403 -0.0064 0.0485  425 LEU B CA  
2894 C C   . LEU B 86  ? 0.4172 0.3498 0.1697 -0.0554 0.0039  0.0567  425 LEU B C   
2895 O O   . LEU B 86  ? 0.4309 0.3396 0.1673 -0.0617 0.0122  0.0569  425 LEU B O   
2896 C CB  . LEU B 86  ? 0.3973 0.3550 0.1773 -0.0172 -0.0076 0.0629  425 LEU B CB  
2897 C CG  . LEU B 86  ? 0.4106 0.3537 0.1942 -0.0107 -0.0025 0.0741  425 LEU B CG  
2898 C CD1 . LEU B 86  ? 0.3791 0.3130 0.1379 -0.0116 -0.0032 0.0634  425 LEU B CD1 
2899 C CD2 . LEU B 86  ? 0.3006 0.2607 0.1160 0.0020  -0.0039 0.0868  425 LEU B CD2 
2900 N N   . ASP B 87  ? 0.4164 0.3527 0.1791 -0.0596 0.0050  0.0628  426 ASP B N   
2901 C CA  . ASP B 87  ? 0.4228 0.3393 0.1807 -0.0685 0.0156  0.0717  426 ASP B CA  
2902 C C   . ASP B 87  ? 0.4863 0.3866 0.2205 -0.0940 0.0278  0.0589  426 ASP B C   
2903 O O   . ASP B 87  ? 0.6000 0.4713 0.3260 -0.0989 0.0411  0.0643  426 ASP B O   
2904 C CB  . ASP B 87  ? 0.4037 0.3322 0.1718 -0.0676 0.0137  0.0771  426 ASP B CB  
2905 C CG  . ASP B 87  ? 0.4421 0.3555 0.2094 -0.0654 0.0236  0.0915  426 ASP B CG  
2906 O OD1 . ASP B 87  ? 0.5507 0.4452 0.3038 -0.0807 0.0354  0.0895  426 ASP B OD1 
2907 O OD2 . ASP B 87  ? 0.5042 0.4250 0.2846 -0.0479 0.0216  0.1040  426 ASP B OD2 
2908 N N   . ASP B 88  ? 0.4822 0.4047 0.2093 -0.1102 0.0261  0.0391  427 ASP B N   
2909 C CA  . ASP B 88  ? 0.5217 0.4401 0.2353 -0.1370 0.0416  0.0189  427 ASP B CA  
2910 C C   . ASP B 88  ? 0.4974 0.4032 0.2111 -0.1356 0.0463  0.0061  427 ASP B C   
2911 O O   . ASP B 88  ? 0.5147 0.4027 0.2281 -0.1538 0.0637  -0.0069 427 ASP B O   
2912 C CB  . ASP B 88  ? 0.4670 0.4296 0.1969 -0.1453 0.0346  -0.0064 427 ASP B CB  
2913 C CG  . ASP B 88  ? 0.4910 0.4655 0.2230 -0.1475 0.0318  0.0029  427 ASP B CG  
2914 O OD1 . ASP B 88  ? 0.5160 0.4675 0.2444 -0.1533 0.0418  0.0169  427 ASP B OD1 
2915 O OD2 . ASP B 88  ? 0.4882 0.4949 0.2368 -0.1372 0.0186  -0.0047 427 ASP B OD2 
2916 N N   . TRP B 89  ? 0.4870 0.4002 0.2004 -0.1151 0.0331  0.0084  428 TRP B N   
2917 C CA  . TRP B 89  ? 0.4536 0.3584 0.1643 -0.1121 0.0362  -0.0054 428 TRP B CA  
2918 C C   . TRP B 89  ? 0.4746 0.3324 0.1717 -0.1051 0.0478  0.0162  428 TRP B C   
2919 O O   . TRP B 89  ? 0.5742 0.4158 0.2670 -0.1078 0.0566  0.0038  428 TRP B O   
2920 C CB  . TRP B 89  ? 0.4553 0.3924 0.1690 -0.0914 0.0179  -0.0144 428 TRP B CB  
2921 C CG  . TRP B 89  ? 0.4231 0.4079 0.1506 -0.0979 0.0093  -0.0441 428 TRP B CG  
2922 C CD1 . TRP B 89  ? 0.4366 0.4532 0.1756 -0.0977 0.0008  -0.0472 428 TRP B CD1 
2923 C CD2 . TRP B 89  ? 0.4611 0.4705 0.1940 -0.1053 0.0086  -0.0764 428 TRP B CD2 
2924 N NE1 . TRP B 89  ? 0.4104 0.4697 0.1681 -0.1006 -0.0052 -0.0761 428 TRP B NE1 
2925 C CE2 . TRP B 89  ? 0.4206 0.4792 0.1746 -0.1058 -0.0017 -0.0952 428 TRP B CE2 
2926 C CE3 . TRP B 89  ? 0.4994 0.4954 0.2254 -0.1102 0.0158  -0.0918 428 TRP B CE3 
2927 C CZ2 . TRP B 89  ? 0.4311 0.5266 0.2074 -0.1072 -0.0063 -0.1236 428 TRP B CZ2 
2928 C CZ3 . TRP B 89  ? 0.5077 0.5437 0.2454 -0.1176 0.0110  -0.1274 428 TRP B CZ3 
2929 C CH2 . TRP B 89  ? 0.4519 0.5376 0.2207 -0.1130 -0.0010 -0.1392 428 TRP B CH2 
2930 N N   . LEU B 90  ? 0.4796 0.3177 0.1706 -0.0959 0.0481  0.0468  429 LEU B N   
2931 C CA  . LEU B 90  ? 0.4795 0.2887 0.1794 -0.0809 0.0548  0.0654  429 LEU B CA  
2932 C C   . LEU B 90  ? 0.5051 0.2903 0.2103 -0.0892 0.0710  0.0728  429 LEU B C   
2933 O O   . LEU B 90  ? 0.5368 0.2924 0.2405 -0.0859 0.0838  0.0772  429 LEU B O   
2934 C CB  . LEU B 90  ? 0.4429 0.2793 0.1767 -0.0537 0.0391  0.0835  429 LEU B CB  
2935 C CG  . LEU B 90  ? 0.4169 0.2723 0.1555 -0.0383 0.0269  0.0806  429 LEU B CG  
2936 C CD1 . LEU B 90  ? 0.4026 0.2905 0.1806 -0.0212 0.0176  0.0945  429 LEU B CD1 
2937 C CD2 . LEU B 90  ? 0.4578 0.2879 0.1810 -0.0323 0.0334  0.0787  429 LEU B CD2 
2938 N N   . HIS B 91  ? 0.5170 0.3150 0.2285 -0.0979 0.0713  0.0739  430 HIS B N   
2939 C CA  . HIS B 91  ? 0.5365 0.3177 0.2545 -0.0991 0.0843  0.0848  430 HIS B CA  
2940 C C   . HIS B 91  ? 0.7583 0.5227 0.4625 -0.1273 0.1034  0.0675  430 HIS B C   
2941 O O   . HIS B 91  ? 0.8617 0.6042 0.5680 -0.1286 0.1186  0.0748  430 HIS B O   
2942 C CB  . HIS B 91  ? 0.4991 0.3108 0.2383 -0.0818 0.0714  0.1043  430 HIS B CB  
2943 C CG  . HIS B 91  ? 0.5154 0.3546 0.2771 -0.0592 0.0550  0.1163  430 HIS B CG  
2944 N ND1 . HIS B 91  ? 0.5619 0.4308 0.3328 -0.0522 0.0413  0.1124  430 HIS B ND1 
2945 C CD2 . HIS B 91  ? 0.4551 0.2974 0.2341 -0.0449 0.0519  0.1298  430 HIS B CD2 
2946 C CE1 . HIS B 91  ? 0.4692 0.3574 0.2631 -0.0339 0.0337  0.1229  430 HIS B CE1 
2947 N NE2 . HIS B 91  ? 0.4141 0.2904 0.2148 -0.0316 0.0378  0.1340  430 HIS B NE2 
2948 N N   . SER B 92  ? 0.7668 0.5473 0.4612 -0.1503 0.1040  0.0441  431 SER B N   
2949 C CA  . SER B 92  ? 0.9494 0.7248 0.6417 -0.1811 0.1245  0.0218  431 SER B CA  
2950 C C   . SER B 92  ? 0.8397 0.6092 0.5340 -0.1995 0.1373  -0.0082 431 SER B C   
2951 O O   . SER B 92  ? 0.8474 0.5852 0.5343 -0.1924 0.1453  -0.0036 431 SER B O   
2952 C CB  . SER B 92  ? 0.9607 0.7781 0.6578 -0.1939 0.1155  0.0095  431 SER B CB  
2953 O OG  . SER B 92  ? 0.9773 0.8026 0.6807 -0.1757 0.1034  0.0311  431 SER B OG  
2954 N N   . MET B 104 ? 0.8264 0.7640 0.5358 -0.1650 0.0715  -0.2163 443 MET B N   
2955 C CA  . MET B 104 ? 0.9375 0.9056 0.6635 -0.1664 0.0610  -0.2078 443 MET B CA  
2956 C C   . MET B 104 ? 0.9454 0.8854 0.6508 -0.1479 0.0568  -0.1672 443 MET B C   
2957 O O   . MET B 104 ? 0.8468 0.8201 0.5588 -0.1354 0.0395  -0.1568 443 MET B O   
2958 C CB  . MET B 104 ? 0.9435 0.9018 0.6912 -0.2014 0.0830  -0.2222 443 MET B CB  
2959 C CG  . MET B 104 ? 0.9835 0.9808 0.7530 -0.2045 0.0732  -0.2190 443 MET B CG  
2960 S SD  . MET B 104 ? 1.4911 1.4743 1.2839 -0.2452 0.1034  -0.2352 443 MET B SD  
2961 C CE  . MET B 104 ? 1.0795 1.1295 0.9021 -0.2395 0.0845  -0.2369 443 MET B CE  
2962 N N   . CYS B 105 ? 0.9292 0.8107 0.6200 -0.1420 0.0720  -0.1393 444 CYS B N   
2963 C CA  . CYS B 105 ? 0.8364 0.6954 0.5194 -0.1204 0.0668  -0.0961 444 CYS B CA  
2964 C C   . CYS B 105 ? 0.7951 0.6815 0.4691 -0.0894 0.0443  -0.0864 444 CYS B C   
2965 O O   . CYS B 105 ? 0.7867 0.7080 0.4566 -0.0819 0.0326  -0.1104 444 CYS B O   
2966 C CB  . CYS B 105 ? 0.8612 0.6568 0.5324 -0.1190 0.0880  -0.0706 444 CYS B CB  
2967 S SG  . CYS B 105 ? 0.8742 0.6262 0.5513 -0.1501 0.1191  -0.0719 444 CYS B SG  
2968 N N   . LEU B 106 ? 0.6494 0.5204 0.3197 -0.0708 0.0393  -0.0510 445 LEU B N   
2969 C CA  . LEU B 106 ? 0.6123 0.4995 0.2743 -0.0416 0.0234  -0.0378 445 LEU B CA  
2970 C C   . LEU B 106 ? 0.5633 0.4213 0.2077 -0.0274 0.0306  -0.0322 445 LEU B C   
2971 O O   . LEU B 106 ? 0.5630 0.3767 0.2037 -0.0318 0.0472  -0.0179 445 LEU B O   
2972 C CB  . LEU B 106 ? 0.5342 0.4150 0.2020 -0.0302 0.0182  -0.0054 445 LEU B CB  
2973 C CG  . LEU B 106 ? 0.5109 0.4261 0.1933 -0.0378 0.0082  -0.0106 445 LEU B CG  
2974 C CD1 . LEU B 106 ? 0.4578 0.3621 0.1452 -0.0303 0.0058  0.0193  445 LEU B CD1 
2975 C CD2 . LEU B 106 ? 0.4912 0.4532 0.1747 -0.0243 -0.0079 -0.0292 445 LEU B CD2 
2976 N N   . SER B 107 ? 0.5430 0.4261 0.1753 -0.0085 0.0192  -0.0428 446 SER B N   
2977 C CA  . SER B 107 ? 0.5474 0.4061 0.1601 0.0071  0.0258  -0.0385 446 SER B CA  
2978 C C   . SER B 107 ? 0.5325 0.3645 0.1424 0.0291  0.0279  -0.0007 446 SER B C   
2979 O O   . SER B 107 ? 0.5018 0.3438 0.1300 0.0332  0.0209  0.0186  446 SER B O   
2980 C CB  . SER B 107 ? 0.5589 0.4564 0.1556 0.0216  0.0127  -0.0625 446 SER B CB  
2981 O OG  . SER B 107 ? 0.5253 0.4602 0.1433 0.0399  -0.0025 -0.0471 446 SER B OG  
2982 N N   . TRP B 108 ? 0.3098 0.3322 0.2609 0.0173  -0.0489 -0.0572 447 TRP B N   
2983 C CA  . TRP B 108 ? 0.2999 0.3254 0.2329 0.0179  -0.0304 -0.0551 447 TRP B CA  
2984 C C   . TRP B 108 ? 0.2966 0.3169 0.2028 0.0156  -0.0334 -0.0492 447 TRP B C   
2985 O O   . TRP B 108 ? 0.2830 0.3163 0.1937 0.0148  -0.0223 -0.0417 447 TRP B O   
2986 C CB  . TRP B 108 ? 0.3278 0.3352 0.2345 0.0188  -0.0188 -0.0668 447 TRP B CB  
2987 C CG  . TRP B 108 ? 0.3151 0.3227 0.2004 0.0181  0.0003  -0.0654 447 TRP B CG  
2988 C CD1 . TRP B 108 ? 0.3644 0.3506 0.2038 0.0154  0.0039  -0.0680 447 TRP B CD1 
2989 C CD2 . TRP B 108 ? 0.2690 0.2992 0.1796 0.0194  0.0180  -0.0603 447 TRP B CD2 
2990 N NE1 . TRP B 108 ? 0.4067 0.4014 0.2439 0.0142  0.0253  -0.0650 447 TRP B NE1 
2991 C CE2 . TRP B 108 ? 0.3450 0.3682 0.2279 0.0165  0.0330  -0.0607 447 TRP B CE2 
2992 C CE3 . TRP B 108 ? 0.2516 0.3061 0.2050 0.0226  0.0217  -0.0551 447 TRP B CE3 
2993 C CZ2 . TRP B 108 ? 0.3217 0.3647 0.2247 0.0160  0.0509  -0.0570 447 TRP B CZ2 
2994 C CZ3 . TRP B 108 ? 0.2891 0.3618 0.2585 0.0231  0.0368  -0.0512 447 TRP B CZ3 
2995 C CH2 . TRP B 108 ? 0.3035 0.3720 0.2508 0.0195  0.0509  -0.0526 447 TRP B CH2 
2996 N N   . PHE B 109 ? 0.3242 0.3240 0.2023 0.0144  -0.0498 -0.0524 448 PHE B N   
2997 C CA  . PHE B 109 ? 0.3498 0.3395 0.1982 0.0132  -0.0536 -0.0462 448 PHE B CA  
2998 C C   . PHE B 109 ? 0.3135 0.3229 0.1917 0.0140  -0.0580 -0.0348 448 PHE B C   
2999 O O   . PHE B 109 ? 0.3442 0.3548 0.2112 0.0129  -0.0499 -0.0279 448 PHE B O   
3000 C CB  . PHE B 109 ? 0.4104 0.3720 0.2220 0.0129  -0.0741 -0.0516 448 PHE B CB  
3001 C CG  . PHE B 109 ? 0.5153 0.4582 0.2852 0.0122  -0.0762 -0.0458 448 PHE B CG  
3002 C CD1 . PHE B 109 ? 0.5311 0.4620 0.2692 0.0091  -0.0548 -0.0457 448 PHE B CD1 
3003 C CD2 . PHE B 109 ? 0.5661 0.5105 0.3472 0.0130  -0.0928 -0.0372 448 PHE B CD2 
3004 C CE1 . PHE B 109 ? 0.5645 0.4847 0.2816 0.0069  -0.0520 -0.0375 448 PHE B CE1 
3005 C CE2 . PHE B 109 ? 0.5576 0.4891 0.3143 0.0119  -0.0901 -0.0295 448 PHE B CE2 
3006 C CZ  . PHE B 109 ? 0.5934 0.5122 0.3173 0.0087  -0.0703 -0.0296 448 PHE B CZ  
3007 N N   . GLN B 110 ? 0.2988 0.3220 0.2151 0.0157  -0.0692 -0.0330 449 GLN B N   
3008 C CA  . GLN B 110 ? 0.2878 0.3281 0.2321 0.0173  -0.0703 -0.0229 449 GLN B CA  
3009 C C   . GLN B 110 ? 0.2598 0.3162 0.2154 0.0168  -0.0510 -0.0175 449 GLN B C   
3010 O O   . GLN B 110 ? 0.2989 0.3599 0.2540 0.0169  -0.0473 -0.0103 449 GLN B O   
3011 C CB  . GLN B 110 ? 0.2773 0.3296 0.2632 0.0187  -0.0815 -0.0223 449 GLN B CB  
3012 C CG  . GLN B 110 ? 0.2992 0.3390 0.2822 0.0188  -0.1050 -0.0268 449 GLN B CG  
3013 C CD  . GLN B 110 ? 0.2898 0.3436 0.3210 0.0186  -0.1141 -0.0269 449 GLN B CD  
3014 O OE1 . GLN B 110 ? 0.2781 0.3410 0.3327 0.0172  -0.1044 -0.0283 449 GLN B OE1 
3015 N NE2 . GLN B 110 ? 0.3308 0.3858 0.3789 0.0198  -0.1313 -0.0244 449 GLN B NE2 
3016 N N   . ARG B 111 ? 0.2500 0.3140 0.2160 0.0166  -0.0399 -0.0211 450 ARG B N   
3017 C CA  . ARG B 111 ? 0.2124 0.2924 0.1911 0.0163  -0.0253 -0.0162 450 ARG B CA  
3018 C C   . ARG B 111 ? 0.2256 0.3006 0.1779 0.0130  -0.0154 -0.0154 450 ARG B C   
3019 O O   . ARG B 111 ? 0.2760 0.3596 0.2324 0.0113  -0.0104 -0.0093 450 ARG B O   
3020 C CB  . ARG B 111 ? 0.2132 0.3011 0.2104 0.0181  -0.0179 -0.0200 450 ARG B CB  
3021 C CG  . ARG B 111 ? 0.2079 0.2964 0.2294 0.0201  -0.0266 -0.0212 450 ARG B CG  
3022 C CD  . ARG B 111 ? 0.2139 0.3073 0.2533 0.0226  -0.0191 -0.0237 450 ARG B CD  
3023 N NE  . ARG B 111 ? 0.2606 0.3525 0.3241 0.0233  -0.0263 -0.0240 450 ARG B NE  
3024 C CZ  . ARG B 111 ? 0.2613 0.3576 0.3472 0.0259  -0.0211 -0.0222 450 ARG B CZ  
3025 N NH1 . ARG B 111 ? 0.2521 0.3562 0.3410 0.0293  -0.0106 -0.0199 450 ARG B NH1 
3026 N NH2 . ARG B 111 ? 0.2683 0.3609 0.3762 0.0251  -0.0271 -0.0221 450 ARG B NH2 
3027 N N   . VAL B 112 ? 0.2474 0.3067 0.1712 0.0113  -0.0117 -0.0220 451 VAL B N   
3028 C CA  . VAL B 112 ? 0.2642 0.3154 0.1614 0.0071  -0.0007 -0.0206 451 VAL B CA  
3029 C C   . VAL B 112 ? 0.2956 0.3396 0.1806 0.0058  -0.0084 -0.0131 451 VAL B C   
3030 O O   . VAL B 112 ? 0.2848 0.3337 0.1696 0.0023  -0.0002 -0.0081 451 VAL B O   
3031 C CB  . VAL B 112 ? 0.2743 0.3031 0.1354 0.0060  0.0046  -0.0284 451 VAL B CB  
3032 C CG1 . VAL B 112 ? 0.3143 0.3338 0.1490 0.0007  0.0197  -0.0259 451 VAL B CG1 
3033 C CG2 . VAL B 112 ? 0.2607 0.2948 0.1355 0.0085  0.0131  -0.0369 451 VAL B CG2 
3034 N N   . GLN B 113 ? 0.3171 0.3491 0.1942 0.0088  -0.0251 -0.0126 452 GLN B N   
3035 C CA  . GLN B 113 ? 0.3049 0.3286 0.1726 0.0096  -0.0333 -0.0053 452 GLN B CA  
3036 C C   . GLN B 113 ? 0.2995 0.3416 0.1970 0.0104  -0.0297 0.0009  452 GLN B C   
3037 O O   . GLN B 113 ? 0.3628 0.4002 0.2506 0.0084  -0.0254 0.0060  452 GLN B O   
3038 C CB  . GLN B 113 ? 0.3592 0.3709 0.2226 0.0139  -0.0545 -0.0060 452 GLN B CB  
3039 C CG  . GLN B 113 ? 0.4401 0.4420 0.2959 0.0167  -0.0644 0.0018  452 GLN B CG  
3040 C CD  . GLN B 113 ? 0.6720 0.6623 0.5249 0.0214  -0.0881 0.0011  452 GLN B CD  
3041 O OE1 . GLN B 113 ? 0.7518 0.7552 0.6374 0.0238  -0.0989 -0.0017 452 GLN B OE1 
3042 N NE2 . GLN B 113 ? 0.6481 0.6180 0.4738 0.0204  -0.0912 0.0043  452 GLN B NE2 
3043 N N   . ILE B 114 ? 0.2467 0.3068 0.1776 0.0130  -0.0306 0.0004  453 ILE B N   
3044 C CA  . ILE B 114 ? 0.2258 0.2997 0.1789 0.0140  -0.0259 0.0060  453 ILE B CA  
3045 C C   . ILE B 114 ? 0.2643 0.3430 0.2100 0.0090  -0.0131 0.0071  453 ILE B C   
3046 O O   . ILE B 114 ? 0.3170 0.3934 0.2585 0.0076  -0.0104 0.0113  453 ILE B O   
3047 C CB  . ILE B 114 ? 0.1830 0.2720 0.1684 0.0171  -0.0267 0.0060  453 ILE B CB  
3048 C CG1 . ILE B 114 ? 0.2113 0.2978 0.2122 0.0209  -0.0398 0.0058  453 ILE B CG1 
3049 C CG2 . ILE B 114 ? 0.1957 0.2957 0.1952 0.0176  -0.0187 0.0114  453 ILE B CG2 
3050 C CD1 . ILE B 114 ? 0.2217 0.3203 0.2550 0.0225  -0.0395 0.0058  453 ILE B CD1 
3051 N N   . ALA B 115 ? 0.2216 0.3067 0.1677 0.0063  -0.0053 0.0029  454 ALA B N   
3052 C CA  . ALA B 115 ? 0.2418 0.3336 0.1862 0.0007  0.0055  0.0033  454 ALA B CA  
3053 C C   . ALA B 115 ? 0.2661 0.3416 0.1832 -0.0046 0.0092  0.0049  454 ALA B C   
3054 O O   . ALA B 115 ? 0.3003 0.3776 0.2170 -0.0095 0.0140  0.0075  454 ALA B O   
3055 C CB  . ALA B 115 ? 0.2282 0.3300 0.1820 0.0000  0.0137  -0.0018 454 ALA B CB  
3056 N N   . HIS B 116 ? 0.2692 0.3260 0.1609 -0.0040 0.0065  0.0034  455 HIS B N   
3057 C CA  . HIS B 116 ? 0.2932 0.3292 0.1545 -0.0083 0.0094  0.0066  455 HIS B CA  
3058 C C   . HIS B 116 ? 0.2645 0.2948 0.1269 -0.0066 0.0024  0.0127  455 HIS B C   
3059 O O   . HIS B 116 ? 0.2894 0.3111 0.1405 -0.0120 0.0088  0.0158  455 HIS B O   
3060 C CB  . HIS B 116 ? 0.3266 0.3398 0.1559 -0.0061 0.0039  0.0048  455 HIS B CB  
3061 C CG  . HIS B 116 ? 0.3703 0.3598 0.1712 -0.0076 0.0059  0.0094  455 HIS B CG  
3062 N ND1 . HIS B 116 ? 0.3890 0.3709 0.1776 -0.0122 0.0205  0.0088  455 HIS B ND1 
3063 C CD2 . HIS B 116 ? 0.4243 0.4002 0.2162 -0.0049 -0.0047 0.0152  455 HIS B CD2 
3064 C CE1 . HIS B 116 ? 0.3579 0.3213 0.1280 -0.0133 0.0185  0.0142  455 HIS B CE1 
3065 N NE2 . HIS B 116 ? 0.4192 0.3782 0.1908 -0.0086 0.0033  0.0180  455 HIS B NE2 
3066 N N   . ASP B 117 ? 0.2861 0.3207 0.1644 0.0008  -0.0093 0.0140  456 ASP B N   
3067 C CA  . ASP B 117 ? 0.3129 0.3419 0.1951 0.0041  -0.0139 0.0192  456 ASP B CA  
3068 C C   . ASP B 117 ? 0.2460 0.2856 0.1404 0.0004  -0.0050 0.0198  456 ASP B C   
3069 O O   . ASP B 117 ? 0.2617 0.2893 0.1451 -0.0020 -0.0022 0.0225  456 ASP B O   
3070 C CB  . ASP B 117 ? 0.3093 0.3441 0.2130 0.0127  -0.0258 0.0201  456 ASP B CB  
3071 C CG  . ASP B 117 ? 0.3291 0.3509 0.2199 0.0164  -0.0395 0.0193  456 ASP B CG  
3072 O OD1 . ASP B 117 ? 0.3240 0.3253 0.1815 0.0140  -0.0406 0.0205  456 ASP B OD1 
3073 O OD2 . ASP B 117 ? 0.3739 0.4045 0.2866 0.0211  -0.0497 0.0177  456 ASP B OD2 
3074 N N   . VAL B 118 ? 0.1883 0.2476 0.1036 -0.0001 -0.0017 0.0173  457 VAL B N   
3075 C CA  . VAL B 118 ? 0.2653 0.3330 0.1885 -0.0035 0.0036  0.0176  457 VAL B CA  
3076 C C   . VAL B 118 ? 0.2941 0.3590 0.2059 -0.0134 0.0107  0.0161  457 VAL B C   
3077 O O   . VAL B 118 ? 0.2311 0.2919 0.1391 -0.0180 0.0127  0.0165  457 VAL B O   
3078 C CB  . VAL B 118 ? 0.2663 0.3534 0.2120 -0.0008 0.0035  0.0165  457 VAL B CB  
3079 C CG1 . VAL B 118 ? 0.2599 0.3533 0.2082 -0.0047 0.0062  0.0168  457 VAL B CG1 
3080 C CG2 . VAL B 118 ? 0.2521 0.3409 0.2119 0.0074  -0.0012 0.0187  457 VAL B CG2 
3081 N N   . ALA B 119 ? 0.2066 0.2726 0.1133 -0.0174 0.0156  0.0138  458 ALA B N   
3082 C CA  . ALA B 119 ? 0.2276 0.2907 0.1269 -0.0276 0.0250  0.0128  458 ALA B CA  
3083 C C   . ALA B 119 ? 0.2869 0.3241 0.1622 -0.0306 0.0259  0.0163  458 ALA B C   
3084 O O   . ALA B 119 ? 0.2916 0.3247 0.1646 -0.0392 0.0309  0.0165  458 ALA B O   
3085 C CB  . ALA B 119 ? 0.2614 0.3288 0.1596 -0.0301 0.0335  0.0097  458 ALA B CB  
3086 N N   . ASP B 120 ? 0.2908 0.3101 0.1487 -0.0237 0.0200  0.0193  459 ASP B N   
3087 C CA  . ASP B 120 ? 0.3024 0.2963 0.1390 -0.0238 0.0190  0.0238  459 ASP B CA  
3088 C C   . ASP B 120 ? 0.3302 0.3215 0.1702 -0.0250 0.0176  0.0250  459 ASP B C   
3089 O O   . ASP B 120 ? 0.3311 0.3085 0.1616 -0.0320 0.0228  0.0258  459 ASP B O   
3090 C CB  . ASP B 120 ? 0.3602 0.3397 0.1816 -0.0147 0.0084  0.0272  459 ASP B CB  
3091 C CG  . ASP B 120 ? 0.3723 0.3252 0.1716 -0.0145 0.0073  0.0324  459 ASP B CG  
3092 O OD1 . ASP B 120 ? 0.4028 0.3464 0.1966 -0.0221 0.0162  0.0334  459 ASP B OD1 
3093 O OD2 . ASP B 120 ? 0.4143 0.3544 0.2020 -0.0073 -0.0036 0.0356  459 ASP B OD2 
3094 N N   . ALA B 121 ? 0.3115 0.3151 0.1693 -0.0171 0.0115  0.0242  460 ALA B N   
3095 C CA  . ALA B 121 ? 0.2893 0.2875 0.1502 -0.0155 0.0116  0.0242  460 ALA B CA  
3096 C C   . ALA B 121 ? 0.2862 0.2901 0.1489 -0.0262 0.0169  0.0203  460 ALA B C   
3097 O O   . ALA B 121 ? 0.3177 0.3060 0.1701 -0.0299 0.0188  0.0195  460 ALA B O   
3098 C CB  . ALA B 121 ? 0.3058 0.3168 0.1860 -0.0053 0.0075  0.0242  460 ALA B CB  
3099 N N   . LEU B 122 ? 0.3299 0.3555 0.2071 -0.0310 0.0182  0.0174  461 LEU B N   
3100 C CA  . LEU B 122 ? 0.3024 0.3363 0.1862 -0.0414 0.0199  0.0136  461 LEU B CA  
3101 C C   . LEU B 122 ? 0.3136 0.3343 0.1870 -0.0534 0.0267  0.0134  461 LEU B C   
3102 O O   . LEU B 122 ? 0.3098 0.3243 0.1815 -0.0624 0.0267  0.0107  461 LEU B O   
3103 C CB  . LEU B 122 ? 0.2060 0.2676 0.1128 -0.0419 0.0186  0.0114  461 LEU B CB  
3104 C CG  . LEU B 122 ? 0.2032 0.2765 0.1207 -0.0314 0.0129  0.0122  461 LEU B CG  
3105 C CD1 . LEU B 122 ? 0.1858 0.2835 0.1255 -0.0316 0.0113  0.0107  461 LEU B CD1 
3106 C CD2 . LEU B 122 ? 0.2544 0.3186 0.1632 -0.0297 0.0095  0.0119  461 LEU B CD2 
3107 N N   . ASN B 123 ? 0.3225 0.3364 0.1868 -0.0544 0.0328  0.0162  462 ASN B N   
3108 C CA  . ASN B 123 ? 0.3345 0.3308 0.1848 -0.0657 0.0419  0.0178  462 ASN B CA  
3109 C C   . ASN B 123 ? 0.3486 0.3161 0.1791 -0.0663 0.0401  0.0200  462 ASN B C   
3110 O O   . ASN B 123 ? 0.3518 0.3085 0.1795 -0.0782 0.0448  0.0186  462 ASN B O   
3111 C CB  . ASN B 123 ? 0.3472 0.3345 0.1863 -0.0620 0.0475  0.0209  462 ASN B CB  
3112 C CG  . ASN B 123 ? 0.3528 0.3284 0.1855 -0.0738 0.0602  0.0221  462 ASN B CG  
3113 O OD1 . ASN B 123 ? 0.4049 0.3949 0.2548 -0.0868 0.0680  0.0190  462 ASN B OD1 
3114 N ND2 . ASN B 123 ? 0.3547 0.3051 0.1645 -0.0696 0.0622  0.0270  462 ASN B ND2 
3115 N N   . TYR B 124 ? 0.3678 0.3225 0.1874 -0.0536 0.0335  0.0232  463 TYR B N   
3116 C CA  . TYR B 124 ? 0.3946 0.3218 0.1984 -0.0515 0.0322  0.0251  463 TYR B CA  
3117 C C   . TYR B 124 ? 0.3304 0.2602 0.1416 -0.0560 0.0308  0.0188  463 TYR B C   
3118 O O   . TYR B 124 ? 0.3632 0.2725 0.1634 -0.0647 0.0339  0.0171  463 TYR B O   
3119 C CB  . TYR B 124 ? 0.3772 0.2962 0.1770 -0.0353 0.0249  0.0294  463 TYR B CB  
3120 C CG  . TYR B 124 ? 0.4142 0.3110 0.2068 -0.0290 0.0237  0.0300  463 TYR B CG  
3121 C CD1 . TYR B 124 ? 0.4048 0.2691 0.1763 -0.0298 0.0256  0.0348  463 TYR B CD1 
3122 C CD2 . TYR B 124 ? 0.3895 0.2953 0.1952 -0.0215 0.0222  0.0262  463 TYR B CD2 
3123 C CE1 . TYR B 124 ? 0.3994 0.2418 0.1659 -0.0226 0.0256  0.0349  463 TYR B CE1 
3124 C CE2 . TYR B 124 ? 0.3966 0.2806 0.1957 -0.0148 0.0240  0.0259  463 TYR B CE2 
3125 C CZ  . TYR B 124 ? 0.4217 0.2747 0.2028 -0.0150 0.0254  0.0299  463 TYR B CZ  
3126 O OH  . TYR B 124 ? 0.4822 0.3121 0.2582 -0.0070 0.0281  0.0291  463 TYR B OH  
3127 N N   . LEU B 125 ? 0.3537 0.3058 0.1807 -0.0507 0.0260  0.0153  464 LEU B N   
3128 C CA  . LEU B 125 ? 0.3713 0.3222 0.1981 -0.0537 0.0233  0.0094  464 LEU B CA  
3129 C C   . LEU B 125 ? 0.3735 0.3273 0.2041 -0.0705 0.0233  0.0044  464 LEU B C   
3130 O O   . LEU B 125 ? 0.3677 0.3042 0.1872 -0.0770 0.0218  -0.0005 464 LEU B O   
3131 C CB  . LEU B 125 ? 0.3449 0.3184 0.1853 -0.0454 0.0187  0.0081  464 LEU B CB  
3132 C CG  . LEU B 125 ? 0.3905 0.3593 0.2303 -0.0302 0.0194  0.0110  464 LEU B CG  
3133 C CD1 . LEU B 125 ? 0.3559 0.3478 0.2106 -0.0244 0.0167  0.0110  464 LEU B CD1 
3134 C CD2 . LEU B 125 ? 0.3751 0.3177 0.1976 -0.0274 0.0228  0.0083  464 LEU B CD2 
3135 N N   . HIS B 126 ? 0.3356 0.3110 0.1837 -0.0778 0.0252  0.0049  465 HIS B N   
3136 C CA  . HIS B 126 ? 0.3182 0.3047 0.1812 -0.0934 0.0240  -0.0001 465 HIS B CA  
3137 C C   . HIS B 126 ? 0.3576 0.3251 0.2143 -0.1071 0.0329  0.0008  465 HIS B C   
3138 O O   . HIS B 126 ? 0.3983 0.3681 0.2663 -0.1217 0.0309  -0.0044 465 HIS B O   
3139 C CB  . HIS B 126 ? 0.2963 0.3176 0.1879 -0.0941 0.0236  -0.0002 465 HIS B CB  
3140 C CG  . HIS B 126 ? 0.3006 0.3408 0.2010 -0.0832 0.0143  -0.0010 465 HIS B CG  
3141 N ND1 . HIS B 126 ? 0.2711 0.3406 0.1971 -0.0810 0.0124  -0.0009 465 HIS B ND1 
3142 C CD2 . HIS B 126 ? 0.2663 0.2983 0.1530 -0.0738 0.0080  -0.0014 465 HIS B CD2 
3143 C CE1 . HIS B 126 ? 0.2481 0.3253 0.1743 -0.0710 0.0043  -0.0005 465 HIS B CE1 
3144 N NE2 . HIS B 126 ? 0.2475 0.3024 0.1495 -0.0668 0.0023  -0.0007 465 HIS B NE2 
3145 N N   . ASN B 127 ? 0.3605 0.3078 0.1994 -0.1034 0.0416  0.0074  466 ASN B N   
3146 C CA  . ASN B 127 ? 0.3382 0.2687 0.1713 -0.1170 0.0529  0.0102  466 ASN B CA  
3147 C C   . ASN B 127 ? 0.4123 0.3016 0.2144 -0.1147 0.0562  0.0150  466 ASN B C   
3148 O O   . ASN B 127 ? 0.4727 0.3406 0.2687 -0.1278 0.0611  0.0140  466 ASN B O   
3149 C CB  . ASN B 127 ? 0.3838 0.3277 0.2230 -0.1173 0.0635  0.0148  466 ASN B CB  
3150 C CG  . ASN B 127 ? 0.3251 0.3087 0.1991 -0.1198 0.0622  0.0100  466 ASN B CG  
3151 O OD1 . ASN B 127 ? 0.3002 0.2997 0.1986 -0.1308 0.0585  0.0044  466 ASN B OD1 
3152 N ND2 . ASN B 127 ? 0.2960 0.2948 0.1730 -0.1093 0.0638  0.0120  466 ASN B ND2 
3153 N N   . TYR B 128 ? 0.4104 0.2874 0.1948 -0.0984 0.0532  0.0206  467 TYR B N   
3154 C CA  . TYR B 128 ? 0.4547 0.2926 0.2116 -0.0943 0.0555  0.0268  467 TYR B CA  
3155 C C   . TYR B 128 ? 0.4668 0.2944 0.2175 -0.0780 0.0469  0.0263  467 TYR B C   
3156 O O   . TYR B 128 ? 0.5643 0.3686 0.2984 -0.0671 0.0455  0.0332  467 TYR B O   
3157 C CB  . TYR B 128 ? 0.4382 0.2640 0.1776 -0.0909 0.0610  0.0362  467 TYR B CB  
3158 C CG  . TYR B 128 ? 0.3945 0.2390 0.1401 -0.0739 0.0524  0.0379  467 TYR B CG  
3159 C CD1 . TYR B 128 ? 0.4245 0.3020 0.1901 -0.0740 0.0529  0.0344  467 TYR B CD1 
3160 C CD2 . TYR B 128 ? 0.4402 0.2676 0.1727 -0.0584 0.0438  0.0433  467 TYR B CD2 
3161 C CE1 . TYR B 128 ? 0.4212 0.3124 0.1915 -0.0601 0.0451  0.0354  467 TYR B CE1 
3162 C CE2 . TYR B 128 ? 0.4460 0.2898 0.1855 -0.0454 0.0350  0.0447  467 TYR B CE2 
3163 C CZ  . TYR B 128 ? 0.4257 0.3004 0.1831 -0.0468 0.0359  0.0404  467 TYR B CZ  
3164 O OH  . TYR B 128 ? 0.5161 0.4039 0.2789 -0.0354 0.0271  0.0411  467 TYR B OH  
3165 N N   . ALA B 129 ? 0.4140 0.2574 0.1778 -0.0758 0.0416  0.0185  468 ALA B N   
3166 C CA  . ALA B 129 ? 0.4381 0.2668 0.1952 -0.0631 0.0382  0.0166  468 ALA B CA  
3167 C C   . ALA B 129 ? 0.4943 0.2942 0.2377 -0.0724 0.0409  0.0106  468 ALA B C   
3168 O O   . ALA B 129 ? 0.5177 0.3222 0.2654 -0.0887 0.0409  0.0045  468 ALA B O   
3169 C CB  . ALA B 129 ? 0.4332 0.2895 0.2058 -0.0549 0.0332  0.0119  468 ALA B CB  
3170 N N   . ASN B 130 ? 0.5154 0.2852 0.2444 -0.0620 0.0427  0.0119  469 ASN B N   
3171 C CA  . ASN B 130 ? 0.6016 0.3382 0.3144 -0.0689 0.0459  0.0052  469 ASN B CA  
3172 C C   . ASN B 130 ? 0.6318 0.3604 0.3401 -0.0553 0.0464  -0.0009 469 ASN B C   
3173 O O   . ASN B 130 ? 0.8582 0.5725 0.5649 -0.0386 0.0492  0.0040  469 ASN B O   
3174 C CB  . ASN B 130 ? 0.6138 0.3125 0.3097 -0.0698 0.0510  0.0126  469 ASN B CB  
3175 C CG  . ASN B 130 ? 0.7388 0.4014 0.4187 -0.0809 0.0548  0.0051  469 ASN B CG  
3176 O OD1 . ASN B 130 ? 0.8212 0.4898 0.5041 -0.0979 0.0531  -0.0040 469 ASN B OD1 
3177 N ND2 . ASN B 130 ? 0.6980 0.3222 0.3621 -0.0712 0.0587  0.0085  469 ASN B ND2 
3178 N N   . PRO B 131 ? 0.5382 0.2748 0.2442 -0.0611 0.0439  -0.0112 470 PRO B N   
3179 C CA  . PRO B 131 ? 0.5188 0.2750 0.2310 -0.0790 0.0373  -0.0175 470 PRO B CA  
3180 C C   . PRO B 131 ? 0.5385 0.3383 0.2736 -0.0771 0.0325  -0.0135 470 PRO B C   
3181 O O   . PRO B 131 ? 0.5510 0.3654 0.2940 -0.0619 0.0335  -0.0084 470 PRO B O   
3182 C CB  . PRO B 131 ? 0.5769 0.3177 0.2711 -0.0807 0.0348  -0.0296 470 PRO B CB  
3183 C CG  . PRO B 131 ? 0.6578 0.3926 0.3462 -0.0598 0.0417  -0.0279 470 PRO B CG  
3184 C CD  . PRO B 131 ? 0.6960 0.4187 0.3906 -0.0490 0.0478  -0.0177 470 PRO B CD  
3185 N N   . PRO B 132 ? 0.5294 0.3506 0.2784 -0.0923 0.0273  -0.0159 471 PRO B N   
3186 C CA  . PRO B 132 ? 0.4669 0.3282 0.2387 -0.0901 0.0230  -0.0130 471 PRO B CA  
3187 C C   . PRO B 132 ? 0.4925 0.3682 0.2642 -0.0872 0.0147  -0.0192 471 PRO B C   
3188 O O   . PRO B 132 ? 0.5447 0.4032 0.2997 -0.0927 0.0100  -0.0275 471 PRO B O   
3189 C CB  . PRO B 132 ? 0.3980 0.2730 0.1871 -0.1079 0.0230  -0.0130 471 PRO B CB  
3190 C CG  . PRO B 132 ? 0.4987 0.3399 0.2735 -0.1212 0.0264  -0.0166 471 PRO B CG  
3191 C CD  . PRO B 132 ? 0.5744 0.3846 0.3233 -0.1125 0.0255  -0.0215 471 PRO B CD  
3192 N N   . HIS B 133 ? 0.4602 0.3654 0.2480 -0.0783 0.0126  -0.0149 472 HIS B N   
3193 C CA  . HIS B 133 ? 0.4507 0.3671 0.2355 -0.0727 0.0062  -0.0180 472 HIS B CA  
3194 C C   . HIS B 133 ? 0.4384 0.3918 0.2492 -0.0729 0.0002  -0.0148 472 HIS B C   
3195 O O   . HIS B 133 ? 0.4019 0.3721 0.2326 -0.0751 0.0033  -0.0104 472 HIS B O   
3196 C CB  . HIS B 133 ? 0.5293 0.4343 0.3021 -0.0555 0.0136  -0.0153 472 HIS B CB  
3197 C CG  . HIS B 133 ? 0.5285 0.3968 0.2777 -0.0524 0.0209  -0.0189 472 HIS B CG  
3198 N ND1 . HIS B 133 ? 0.5391 0.3831 0.2620 -0.0574 0.0191  -0.0281 472 HIS B ND1 
3199 C CD2 . HIS B 133 ? 0.5060 0.3561 0.2533 -0.0441 0.0294  -0.0149 472 HIS B CD2 
3200 C CE1 . HIS B 133 ? 0.6185 0.4304 0.3251 -0.0521 0.0283  -0.0300 472 HIS B CE1 
3201 N NE2 . HIS B 133 ? 0.5868 0.4026 0.3096 -0.0435 0.0343  -0.0215 472 HIS B NE2 
3202 N N   . VAL B 134 ? 0.4247 0.3876 0.2322 -0.0700 -0.0078 -0.0170 473 VAL B N   
3203 C CA  . VAL B 134 ? 0.3818 0.3761 0.2114 -0.0660 -0.0133 -0.0130 473 VAL B CA  
3204 C C   . VAL B 134 ? 0.4010 0.3927 0.2205 -0.0510 -0.0090 -0.0089 473 VAL B C   
3205 O O   . VAL B 134 ? 0.4094 0.3816 0.2029 -0.0478 -0.0092 -0.0120 473 VAL B O   
3206 C CB  . VAL B 134 ? 0.3673 0.3756 0.2047 -0.0761 -0.0285 -0.0176 473 VAL B CB  
3207 C CG1 . VAL B 134 ? 0.3512 0.3876 0.2084 -0.0687 -0.0343 -0.0127 473 VAL B CG1 
3208 C CG2 . VAL B 134 ? 0.3553 0.3716 0.2130 -0.0918 -0.0307 -0.0210 473 VAL B CG2 
3209 N N   . HIS B 135 ? 0.3619 0.3712 0.2009 -0.0423 -0.0040 -0.0025 474 HIS B N   
3210 C CA  . HIS B 135 ? 0.3710 0.3786 0.2065 -0.0290 0.0020  0.0019  474 HIS B CA  
3211 C C   . HIS B 135 ? 0.4064 0.4146 0.2292 -0.0270 -0.0040 0.0017  474 HIS B C   
3212 O O   . HIS B 135 ? 0.4413 0.4303 0.2440 -0.0201 0.0019  0.0012  474 HIS B O   
3213 C CB  . HIS B 135 ? 0.3968 0.4250 0.2584 -0.0225 0.0049  0.0077  474 HIS B CB  
3214 C CG  . HIS B 135 ? 0.3666 0.3926 0.2312 -0.0102 0.0123  0.0123  474 HIS B CG  
3215 N ND1 . HIS B 135 ? 0.3241 0.3549 0.1877 -0.0047 0.0129  0.0152  474 HIS B ND1 
3216 C CD2 . HIS B 135 ? 0.3966 0.4163 0.2677 -0.0026 0.0194  0.0149  474 HIS B CD2 
3217 C CE1 . HIS B 135 ? 0.3556 0.3840 0.2272 0.0048  0.0221  0.0192  474 HIS B CE1 
3218 N NE2 . HIS B 135 ? 0.3586 0.3818 0.2371 0.0064  0.0250  0.0187  474 HIS B NE2 
3219 N N   . LYS B 136 ? 0.3984 0.4275 0.2357 -0.0312 -0.0150 0.0025  475 LYS B N   
3220 C CA  . LYS B 136 ? 0.4190 0.4490 0.2464 -0.0294 -0.0250 0.0032  475 LYS B CA  
3221 C C   . LYS B 136 ? 0.4002 0.4335 0.2320 -0.0170 -0.0189 0.0107  475 LYS B C   
3222 O O   . LYS B 136 ? 0.4124 0.4466 0.2386 -0.0142 -0.0270 0.0133  475 LYS B O   
3223 C CB  . LYS B 136 ? 0.4495 0.4514 0.2441 -0.0308 -0.0282 -0.0027 475 LYS B CB  
3224 C CG  . LYS B 136 ? 0.4255 0.4190 0.2138 -0.0449 -0.0351 -0.0110 475 LYS B CG  
3225 C CD  . LYS B 136 ? 0.4721 0.4419 0.2314 -0.0468 -0.0427 -0.0176 475 LYS B CD  
3226 C CE  . LYS B 136 ? 0.6722 0.6153 0.4065 -0.0372 -0.0271 -0.0184 475 LYS B CE  
3227 N NZ  . LYS B 136 ? 0.7387 0.6631 0.4442 -0.0361 -0.0328 -0.0227 475 LYS B NZ  
3228 N N   . ASN B 137 ? 0.3528 0.3869 0.1949 -0.0100 -0.0058 0.0144  476 ASN B N   
3229 C CA  . ASN B 137 ? 0.3068 0.3425 0.1550 -0.0006 0.0013  0.0212  476 ASN B CA  
3230 C C   . ASN B 137 ? 0.3495 0.4049 0.2285 0.0032  0.0063  0.0246  476 ASN B C   
3231 O O   . ASN B 137 ? 0.3699 0.4223 0.2558 0.0100  0.0167  0.0279  476 ASN B O   
3232 C CB  . ASN B 137 ? 0.3990 0.4094 0.2240 0.0039  0.0141  0.0215  476 ASN B CB  
3233 C CG  . ASN B 137 ? 0.4115 0.4219 0.2402 0.0105  0.0211  0.0283  476 ASN B CG  
3234 O OD1 . ASN B 137 ? 0.4236 0.4404 0.2526 0.0110  0.0129  0.0323  476 ASN B OD1 
3235 N ND2 . ASN B 137 ? 0.3698 0.3728 0.2030 0.0165  0.0365  0.0301  476 ASN B ND2 
3236 N N   . LEU B 138 ? 0.2829 0.3579 0.1815 -0.0014 -0.0012 0.0234  477 LEU B N   
3237 C CA  . LEU B 138 ? 0.2699 0.3584 0.1937 0.0014  0.0020  0.0248  477 LEU B CA  
3238 C C   . LEU B 138 ? 0.2401 0.3409 0.1802 0.0072  0.0007  0.0297  477 LEU B C   
3239 O O   . LEU B 138 ? 0.2590 0.3702 0.2045 0.0058  -0.0071 0.0304  477 LEU B O   
3240 C CB  . LEU B 138 ? 0.1520 0.2505 0.0861 -0.0060 -0.0019 0.0205  477 LEU B CB  
3241 C CG  . LEU B 138 ? 0.2183 0.3249 0.1696 -0.0034 0.0014  0.0208  477 LEU B CG  
3242 C CD1 . LEU B 138 ? 0.1623 0.2557 0.1084 0.0012  0.0065  0.0220  477 LEU B CD1 
3243 C CD2 . LEU B 138 ? 0.2329 0.3469 0.1899 -0.0110 0.0008  0.0169  477 LEU B CD2 
3244 N N   . LYS B 139 ? 0.2278 0.3275 0.1787 0.0136  0.0079  0.0331  478 LYS B N   
3245 C CA  . LYS B 139 ? 0.2511 0.3588 0.2181 0.0186  0.0083  0.0380  478 LYS B CA  
3246 C C   . LYS B 139 ? 0.2514 0.3619 0.2388 0.0220  0.0133  0.0383  478 LYS B C   
3247 O O   . LYS B 139 ? 0.2649 0.3684 0.2513 0.0229  0.0177  0.0372  478 LYS B O   
3248 C CB  . LYS B 139 ? 0.3200 0.4163 0.2710 0.0225  0.0123  0.0443  478 LYS B CB  
3249 C CG  . LYS B 139 ? 0.3793 0.4696 0.3055 0.0193  0.0038  0.0437  478 LYS B CG  
3250 C CD  . LYS B 139 ? 0.4366 0.5092 0.3374 0.0236  0.0085  0.0502  478 LYS B CD  
3251 C CE  . LYS B 139 ? 0.4404 0.5037 0.3176 0.0199  -0.0047 0.0483  478 LYS B CE  
3252 N NZ  . LYS B 139 ? 0.4193 0.4746 0.2819 0.0125  -0.0091 0.0395  478 LYS B NZ  
3253 N N   . SER B 140 ? 0.2136 0.3337 0.2208 0.0241  0.0113  0.0395  479 SER B N   
3254 C CA  . SER B 140 ? 0.2040 0.3262 0.2315 0.0264  0.0130  0.0387  479 SER B CA  
3255 C C   . SER B 140 ? 0.2496 0.3643 0.2824 0.0298  0.0217  0.0430  479 SER B C   
3256 O O   . SER B 140 ? 0.2630 0.3784 0.3103 0.0309  0.0215  0.0413  479 SER B O   
3257 C CB  . SER B 140 ? 0.1809 0.3104 0.2268 0.0281  0.0106  0.0393  479 SER B CB  
3258 O OG  . SER B 140 ? 0.2568 0.3835 0.3010 0.0310  0.0137  0.0463  479 SER B OG  
3259 N N   . GLY B 141 ? 0.2368 0.3435 0.2580 0.0320  0.0294  0.0488  480 GLY B N   
3260 C CA  . GLY B 141 ? 0.2338 0.3323 0.2593 0.0354  0.0419  0.0528  480 GLY B CA  
3261 C C   . GLY B 141 ? 0.2612 0.3531 0.2782 0.0359  0.0449  0.0492  480 GLY B C   
3262 O O   . GLY B 141 ? 0.2755 0.3650 0.3079 0.0396  0.0544  0.0510  480 GLY B O   
3263 N N   . ASN B 142 ? 0.2740 0.3628 0.2699 0.0323  0.0376  0.0443  481 ASN B N   
3264 C CA  . ASN B 142 ? 0.2520 0.3307 0.2366 0.0326  0.0400  0.0410  481 ASN B CA  
3265 C C   . ASN B 142 ? 0.2426 0.3266 0.2374 0.0310  0.0305  0.0369  481 ASN B C   
3266 O O   . ASN B 142 ? 0.2627 0.3367 0.2470 0.0311  0.0307  0.0347  481 ASN B O   
3267 C CB  . ASN B 142 ? 0.2734 0.3396 0.2239 0.0287  0.0392  0.0384  481 ASN B CB  
3268 C CG  . ASN B 142 ? 0.3641 0.4183 0.2948 0.0311  0.0483  0.0423  481 ASN B CG  
3269 O OD1 . ASN B 142 ? 0.4714 0.5228 0.4124 0.0364  0.0605  0.0471  481 ASN B OD1 
3270 N ND2 . ASN B 142 ? 0.3490 0.3945 0.2508 0.0267  0.0420  0.0400  481 ASN B ND2 
3271 N N   . ILE B 143 ? 0.2310 0.3270 0.2422 0.0296  0.0225  0.0360  482 ILE B N   
3272 C CA  . ILE B 143 ? 0.2629 0.3603 0.2790 0.0285  0.0135  0.0326  482 ILE B CA  
3273 C C   . ILE B 143 ? 0.2418 0.3438 0.2865 0.0336  0.0119  0.0343  482 ILE B C   
3274 O O   . ILE B 143 ? 0.2281 0.3389 0.2916 0.0334  0.0081  0.0341  482 ILE B O   
3275 C CB  . ILE B 143 ? 0.2003 0.3049 0.2125 0.0238  0.0065  0.0292  482 ILE B CB  
3276 C CG1 . ILE B 143 ? 0.2240 0.3275 0.2162 0.0183  0.0077  0.0276  482 ILE B CG1 
3277 C CG2 . ILE B 143 ? 0.1803 0.2814 0.1905 0.0230  -0.0017 0.0259  482 ILE B CG2 
3278 C CD1 . ILE B 143 ? 0.1603 0.2738 0.1552 0.0146  0.0041  0.0246  482 ILE B CD1 
3279 N N   . LEU B 144 ? 0.2456 0.3413 0.2963 0.0381  0.0145  0.0357  483 LEU B N   
3280 C CA  . LEU B 144 ? 0.2160 0.3183 0.3003 0.0432  0.0118  0.0374  483 LEU B CA  
3281 C C   . LEU B 144 ? 0.2221 0.3255 0.3100 0.0423  -0.0056 0.0342  483 LEU B C   
3282 O O   . LEU B 144 ? 0.2840 0.3784 0.3449 0.0395  -0.0120 0.0317  483 LEU B O   
3283 C CB  . LEU B 144 ? 0.1880 0.2836 0.2803 0.0497  0.0209  0.0398  483 LEU B CB  
3284 C CG  . LEU B 144 ? 0.2395 0.3271 0.3162 0.0505  0.0391  0.0418  483 LEU B CG  
3285 C CD1 . LEU B 144 ? 0.3067 0.3825 0.3829 0.0571  0.0488  0.0423  483 LEU B CD1 
3286 C CD2 . LEU B 144 ? 0.2593 0.3552 0.3561 0.0510  0.0500  0.0458  483 LEU B CD2 
3287 N N   . LEU B 145 ? 0.2413 0.3540 0.3615 0.0442  -0.0130 0.0341  484 LEU B N   
3288 C CA  . LEU B 145 ? 0.2296 0.3413 0.3506 0.0430  -0.0318 0.0302  484 LEU B CA  
3289 C C   . LEU B 145 ? 0.2344 0.3457 0.3771 0.0491  -0.0433 0.0318  484 LEU B C   
3290 O O   . LEU B 145 ? 0.2365 0.3525 0.4061 0.0521  -0.0355 0.0328  484 LEU B O   
3291 C CB  . LEU B 145 ? 0.2276 0.3482 0.3673 0.0392  -0.0364 0.0272  484 LEU B CB  
3292 C CG  . LEU B 145 ? 0.2291 0.3463 0.3416 0.0340  -0.0346 0.0233  484 LEU B CG  
3293 C CD1 . LEU B 145 ? 0.2607 0.3780 0.3571 0.0331  -0.0189 0.0267  484 LEU B CD1 
3294 C CD2 . LEU B 145 ? 0.2144 0.3373 0.3465 0.0313  -0.0388 0.0200  484 LEU B CD2 
3295 N N   . ASP B 146 ? 0.2660 0.3660 0.3871 0.0493  -0.0597 0.0298  485 ASP B N   
3296 C CA  . ASP B 146 ? 0.2115 0.3071 0.3445 0.0549  -0.0738 0.0309  485 ASP B CA  
3297 C C   . ASP B 146 ? 0.2681 0.3710 0.4253 0.0517  -0.0813 0.0265  485 ASP B C   
3298 O O   . ASP B 146 ? 0.2341 0.3429 0.3975 0.0458  -0.0791 0.0228  485 ASP B O   
3299 C CB  . ASP B 146 ? 0.2539 0.3300 0.3471 0.0553  -0.0892 0.0311  485 ASP B CB  
3300 C CG  . ASP B 146 ? 0.3012 0.3667 0.3944 0.0629  -0.0946 0.0360  485 ASP B CG  
3301 O OD1 . ASP B 146 ? 0.3892 0.4638 0.5147 0.0687  -0.0855 0.0385  485 ASP B OD1 
3302 O OD2 . ASP B 146 ? 0.3256 0.3716 0.3841 0.0630  -0.1058 0.0371  485 ASP B OD2 
3303 N N   . GLY B 147 ? 0.2908 0.3923 0.4634 0.0555  -0.0912 0.0275  486 GLY B N   
3304 C CA  . GLY B 147 ? 0.2539 0.3594 0.4474 0.0517  -0.1036 0.0235  486 GLY B CA  
3305 C C   . GLY B 147 ? 0.2873 0.3820 0.4534 0.0462  -0.1193 0.0182  486 GLY B C   
3306 O O   . GLY B 147 ? 0.2562 0.3532 0.4375 0.0414  -0.1277 0.0133  486 GLY B O   
3307 N N   . LYS B 148 ? 0.2795 0.3598 0.4037 0.0465  -0.1229 0.0186  487 LYS B N   
3308 C CA  . LYS B 148 ? 0.2923 0.3589 0.3824 0.0413  -0.1334 0.0127  487 LYS B CA  
3309 C C   . LYS B 148 ? 0.3161 0.3842 0.3876 0.0378  -0.1209 0.0108  487 LYS B C   
3310 O O   . LYS B 148 ? 0.3908 0.4444 0.4243 0.0347  -0.1249 0.0065  487 LYS B O   
3311 C CB  . LYS B 148 ? 0.3099 0.3545 0.3608 0.0434  -0.1462 0.0141  487 LYS B CB  
3312 C CG  . LYS B 148 ? 0.3883 0.4302 0.4564 0.0471  -0.1628 0.0152  487 LYS B CG  
3313 C CD  . LYS B 148 ? 0.5635 0.5808 0.5895 0.0496  -0.1750 0.0176  487 LYS B CD  
3314 C CE  . LYS B 148 ? 0.5439 0.5563 0.5618 0.0556  -0.1670 0.0260  487 LYS B CE  
3315 N NZ  . LYS B 148 ? 0.5284 0.5554 0.5912 0.0629  -0.1681 0.0304  487 LYS B NZ  
3316 N N   . PHE B 149 ? 0.2699 0.3541 0.3662 0.0384  -0.1047 0.0137  488 PHE B N   
3317 C CA  . PHE B 149 ? 0.2369 0.3259 0.3238 0.0357  -0.0936 0.0120  488 PHE B CA  
3318 C C   . PHE B 149 ? 0.3006 0.3762 0.3431 0.0344  -0.0856 0.0130  488 PHE B C   
3319 O O   . PHE B 149 ? 0.3013 0.3708 0.3175 0.0298  -0.0803 0.0086  488 PHE B O   
3320 C CB  . PHE B 149 ? 0.2828 0.3707 0.3693 0.0307  -0.0991 0.0042  488 PHE B CB  
3321 C CG  . PHE B 149 ? 0.3029 0.4002 0.4283 0.0286  -0.0990 0.0034  488 PHE B CG  
3322 C CD1 . PHE B 149 ? 0.2389 0.3489 0.3905 0.0277  -0.0828 0.0064  488 PHE B CD1 
3323 C CD2 . PHE B 149 ? 0.2832 0.3740 0.4161 0.0272  -0.1150 -0.0003 488 PHE B CD2 
3324 C CE1 . PHE B 149 ? 0.2353 0.3501 0.4187 0.0250  -0.0815 0.0059  488 PHE B CE1 
3325 C CE2 . PHE B 149 ? 0.2799 0.3783 0.4496 0.0245  -0.1155 -0.0016 488 PHE B CE2 
3326 C CZ  . PHE B 149 ? 0.2551 0.3651 0.4500 0.0231  -0.0980 0.0017  488 PHE B CZ  
3327 N N   . ARG B 150 ? 0.3297 0.4003 0.3664 0.0382  -0.0827 0.0187  489 ARG B N   
3328 C CA  . ARG B 150 ? 0.2914 0.3492 0.2913 0.0357  -0.0727 0.0206  489 ARG B CA  
3329 C C   . ARG B 150 ? 0.2593 0.3267 0.2686 0.0349  -0.0541 0.0235  489 ARG B C   
3330 O O   . ARG B 150 ? 0.2823 0.3606 0.3216 0.0389  -0.0492 0.0262  489 ARG B O   
3331 C CB  . ARG B 150 ? 0.3068 0.3468 0.2884 0.0401  -0.0831 0.0249  489 ARG B CB  
3332 C CG  . ARG B 150 ? 0.3503 0.3768 0.3168 0.0416  -0.1050 0.0228  489 ARG B CG  
3333 C CD  . ARG B 150 ? 0.3682 0.3820 0.2950 0.0349  -0.1025 0.0173  489 ARG B CD  
3334 N NE  . ARG B 150 ? 0.3889 0.3892 0.2809 0.0308  -0.0878 0.0200  489 ARG B NE  
3335 C CZ  . ARG B 150 ? 0.4397 0.4175 0.3001 0.0305  -0.0904 0.0241  489 ARG B CZ  
3336 N NH1 . ARG B 150 ? 0.4175 0.3848 0.2767 0.0342  -0.1054 0.0257  489 ARG B NH1 
3337 N NH2 . ARG B 150 ? 0.4799 0.4474 0.3146 0.0253  -0.0750 0.0265  489 ARG B NH2 
3338 N N   . GLY B 151 ? 0.2682 0.3306 0.2513 0.0295  -0.0436 0.0226  490 GLY B N   
3339 C CA  . GLY B 151 ? 0.2240 0.2935 0.2111 0.0277  -0.0292 0.0242  490 GLY B CA  
3340 C C   . GLY B 151 ? 0.2746 0.3351 0.2597 0.0314  -0.0253 0.0282  490 GLY B C   
3341 O O   . GLY B 151 ? 0.3067 0.3510 0.2711 0.0315  -0.0289 0.0298  490 GLY B O   
3342 N N   . LYS B 152 ? 0.2822 0.3503 0.2865 0.0348  -0.0166 0.0301  491 LYS B N   
3343 C CA  . LYS B 152 ? 0.2843 0.3424 0.2861 0.0388  -0.0091 0.0326  491 LYS B CA  
3344 C C   . LYS B 152 ? 0.2710 0.3311 0.2649 0.0355  0.0041  0.0319  491 LYS B C   
3345 O O   . LYS B 152 ? 0.2208 0.2895 0.2320 0.0384  0.0114  0.0334  491 LYS B O   
3346 C CB  . LYS B 152 ? 0.2510 0.3132 0.2847 0.0481  -0.0107 0.0356  491 LYS B CB  
3347 C CG  . LYS B 152 ? 0.2845 0.3447 0.3279 0.0522  -0.0282 0.0365  491 LYS B CG  
3348 C CD  . LYS B 152 ? 0.2923 0.3324 0.3161 0.0559  -0.0328 0.0391  491 LYS B CD  
3349 C CE  . LYS B 152 ? 0.2635 0.2993 0.2940 0.0610  -0.0533 0.0411  491 LYS B CE  
3350 N NZ  . LYS B 152 ? 0.3675 0.3820 0.3825 0.0669  -0.0582 0.0454  491 LYS B NZ  
3351 N N   . VAL B 153 ? 0.2903 0.3411 0.2572 0.0289  0.0066  0.0298  492 VAL B N   
3352 C CA  . VAL B 153 ? 0.3039 0.3550 0.2600 0.0250  0.0149  0.0285  492 VAL B CA  
3353 C C   . VAL B 153 ? 0.2982 0.3382 0.2533 0.0310  0.0249  0.0295  492 VAL B C   
3354 O O   . VAL B 153 ? 0.3381 0.3667 0.2959 0.0366  0.0261  0.0304  492 VAL B O   
3355 C CB  . VAL B 153 ? 0.3436 0.3879 0.2759 0.0156  0.0135  0.0253  492 VAL B CB  
3356 C CG1 . VAL B 153 ? 0.3142 0.3597 0.2363 0.0113  0.0175  0.0234  492 VAL B CG1 
3357 C CG2 . VAL B 153 ? 0.2853 0.3396 0.2196 0.0106  0.0074  0.0242  492 VAL B CG2 
3358 N N   . SER B 154 ? 0.5408 0.3483 0.2069 0.1414  0.0641  -0.0462 493 SER B N   
3359 C CA  . SER B 154 ? 0.5198 0.3560 0.2059 0.1193  0.0674  -0.0453 493 SER B CA  
3360 C C   . SER B 154 ? 0.4972 0.3367 0.2046 0.0889  0.0736  -0.0363 493 SER B C   
3361 O O   . SER B 154 ? 0.4969 0.3164 0.2041 0.0848  0.0770  -0.0305 493 SER B O   
3362 C CB  . SER B 154 ? 0.5168 0.3835 0.2198 0.1102  0.0428  -0.0524 493 SER B CB  
3363 O OG  . SER B 154 ? 0.5106 0.3787 0.2351 0.0866  0.0207  -0.0504 493 SER B OG  
3364 N N   . ASN B 155 ? 0.5116 0.3800 0.2358 0.0704  0.0749  -0.0350 494 ASN B N   
3365 C CA  . ASN B 155 ? 0.4792 0.3579 0.2239 0.0422  0.0775  -0.0278 494 ASN B CA  
3366 C C   . ASN B 155 ? 0.4719 0.3216 0.2090 0.0423  0.0957  -0.0222 494 ASN B C   
3367 O O   . ASN B 155 ? 0.4819 0.3217 0.2290 0.0279  0.0943  -0.0165 494 ASN B O   
3368 C CB  . ASN B 155 ? 0.4765 0.3631 0.2424 0.0206  0.0564  -0.0246 494 ASN B CB  
3369 C CG  . ASN B 155 ? 0.4885 0.4103 0.2807 -0.0072 0.0527  -0.0170 494 ASN B CG  
3370 O OD1 . ASN B 155 ? 0.5121 0.4536 0.3039 -0.0077 0.0659  -0.0160 494 ASN B OD1 
3371 N ND2 . ASN B 155 ? 0.5095 0.4387 0.3226 -0.0283 0.0336  -0.0112 494 ASN B ND2 
3372 N N   . PHE B 156 ? 0.5433 0.3794 0.2637 0.0585  0.1115  -0.0229 495 PHE B N   
3373 C CA  . PHE B 156 ? 0.5509 0.3605 0.2690 0.0559  0.1267  -0.0153 495 PHE B CA  
3374 C C   . PHE B 156 ? 0.6131 0.4328 0.3471 0.0320  0.1264  -0.0146 495 PHE B C   
3375 O O   . PHE B 156 ? 0.5811 0.4285 0.3200 0.0256  0.1204  -0.0201 495 PHE B O   
3376 C CB  . PHE B 156 ? 0.5632 0.3576 0.2713 0.0756  0.1348  -0.0136 495 PHE B CB  
3377 C CG  . PHE B 156 ? 0.5332 0.3202 0.2355 0.0980  0.1329  -0.0090 495 PHE B CG  
3378 C CD1 . PHE B 156 ? 0.5370 0.3422 0.2356 0.1105  0.1201  -0.0174 495 PHE B CD1 
3379 C CD2 . PHE B 156 ? 0.5451 0.3076 0.2436 0.1076  0.1447  0.0049  495 PHE B CD2 
3380 C CE1 . PHE B 156 ? 0.5866 0.3853 0.2781 0.1323  0.1166  -0.0137 495 PHE B CE1 
3381 C CE2 . PHE B 156 ? 0.5816 0.3412 0.2729 0.1303  0.1432  0.0114  495 PHE B CE2 
3382 C CZ  . PHE B 156 ? 0.5957 0.3733 0.2831 0.1426  0.1279  0.0013  495 PHE B CZ  
3383 N N   . GLY B 157 ? 0.6240 0.4245 0.3662 0.0208  0.1330  -0.0068 496 GLY B N   
3384 C CA  . GLY B 157 ? 0.6566 0.4614 0.4112 0.0009  0.1319  -0.0072 496 GLY B CA  
3385 C C   . GLY B 157 ? 0.7157 0.5391 0.4894 -0.0202 0.1228  -0.0043 496 GLY B C   
3386 O O   . GLY B 157 ? 0.7353 0.5730 0.5132 -0.0217 0.1133  -0.0043 496 GLY B O   
3387 N N   . LEU B 158 ? 0.8745 0.6951 0.6594 -0.0366 0.1235  -0.0021 497 LEU B N   
3388 C CA  . LEU B 158 ? 0.9476 0.7826 0.7493 -0.0561 0.1161  0.0019  497 LEU B CA  
3389 C C   . LEU B 158 ? 0.8996 0.7558 0.7074 -0.0687 0.1118  -0.0023 497 LEU B C   
3390 O O   . LEU B 158 ? 1.0059 0.8883 0.8243 -0.0809 0.1040  0.0004  497 LEU B O   
3391 C CB  . LEU B 158 ? 0.8563 0.6715 0.6668 -0.0621 0.1210  0.0109  497 LEU B CB  
3392 C CG  . LEU B 158 ? 0.8888 0.7123 0.7101 -0.0735 0.1132  0.0159  497 LEU B CG  
3393 C CD1 . LEU B 158 ? 0.7753 0.6021 0.5888 -0.0634 0.1040  0.0141  497 LEU B CD1 
3394 C CD2 . LEU B 158 ? 0.8083 0.6173 0.6369 -0.0746 0.1204  0.0260  497 LEU B CD2 
3395 N N   . PHE B 171 ? 0.4793 0.8141 0.4830 -0.1660 0.0444  0.1434  510 PHE B N   
3396 C CA  . PHE B 171 ? 0.4627 0.7335 0.4505 -0.1734 0.0422  0.1255  510 PHE B CA  
3397 C C   . PHE B 171 ? 0.4559 0.6922 0.4618 -0.1932 0.0229  0.1325  510 PHE B C   
3398 O O   . PHE B 171 ? 0.5273 0.7730 0.5456 -0.1975 0.0171  0.1441  510 PHE B O   
3399 C CB  . PHE B 171 ? 0.4445 0.6850 0.4014 -0.1589 0.0565  0.1058  510 PHE B CB  
3400 C CG  . PHE B 171 ? 0.4459 0.6232 0.3887 -0.1654 0.0545  0.0903  510 PHE B CG  
3401 C CD1 . PHE B 171 ? 0.4570 0.6072 0.3820 -0.1605 0.0592  0.0774  510 PHE B CD1 
3402 C CD2 . PHE B 171 ? 0.4384 0.5839 0.3843 -0.1716 0.0481  0.0882  510 PHE B CD2 
3403 C CE1 . PHE B 171 ? 0.4183 0.5105 0.3314 -0.1602 0.0569  0.0637  510 PHE B CE1 
3404 C CE2 . PHE B 171 ? 0.4352 0.5283 0.3696 -0.1728 0.0463  0.0752  510 PHE B CE2 
3405 C CZ  . PHE B 171 ? 0.4198 0.4878 0.3375 -0.1695 0.0518  0.0648  510 PHE B CZ  
3406 N N   . GLN B 172 ? 0.4590 0.6539 0.4623 -0.2024 0.0125  0.1246  511 GLN B N   
3407 C CA  . GLN B 172 ? 0.5065 0.6624 0.5208 -0.2153 -0.0088 0.1275  511 GLN B CA  
3408 C C   . GLN B 172 ? 0.5382 0.6411 0.5289 -0.2081 -0.0041 0.1095  511 GLN B C   
3409 O O   . GLN B 172 ? 0.5513 0.6170 0.5244 -0.2056 -0.0036 0.0960  511 GLN B O   
3410 C CB  . GLN B 172 ? 0.5540 0.6989 0.5803 -0.2272 -0.0280 0.1302  511 GLN B CB  
3411 C CG  . GLN B 172 ? 0.5751 0.7778 0.6296 -0.2342 -0.0337 0.1494  511 GLN B CG  
3412 C CD  . GLN B 172 ? 0.6204 0.8273 0.6791 -0.2388 -0.0412 0.1447  511 GLN B CD  
3413 O OE1 . GLN B 172 ? 0.7554 0.9326 0.7823 -0.2169 -0.0289 0.1208  511 GLN B OE1 
3414 N NE2 . GLN B 172 ? 0.4798 0.7105 0.5695 -0.2505 -0.0625 0.1595  511 GLN B NE2 
3415 N N   . LEU B 173 ? 0.4969 0.5990 0.4873 -0.2044 -0.0007 0.1108  512 LEU B N   
3416 C CA  . LEU B 173 ? 0.4644 0.5262 0.4370 -0.1963 0.0042  0.0959  512 LEU B CA  
3417 C C   . LEU B 173 ? 0.4965 0.5144 0.4664 -0.1999 -0.0126 0.0920  512 LEU B C   
3418 O O   . LEU B 173 ? 0.5133 0.4970 0.4653 -0.1932 -0.0097 0.0790  512 LEU B O   
3419 C CB  . LEU B 173 ? 0.4255 0.5015 0.4008 -0.1933 0.0090  0.1001  512 LEU B CB  
3420 C CG  . LEU B 173 ? 0.3821 0.4263 0.3433 -0.1852 0.0140  0.0868  512 LEU B CG  
3421 C CD1 . LEU B 173 ? 0.3752 0.4261 0.3221 -0.1761 0.0305  0.0762  512 LEU B CD1 
3422 C CD2 . LEU B 173 ? 0.4299 0.4763 0.3983 -0.1883 0.0077  0.0947  512 LEU B CD2 
3423 N N   . THR B 174 ? 0.4784 0.4960 0.4638 -0.2095 -0.0308 0.1041  513 THR B N   
3424 C CA  . THR B 174 ? 0.4933 0.4670 0.4722 -0.2107 -0.0496 0.1000  513 THR B CA  
3425 C C   . THR B 174 ? 0.5211 0.4643 0.4872 -0.2091 -0.0581 0.0899  513 THR B C   
3426 O O   . THR B 174 ? 0.5355 0.4367 0.4810 -0.2010 -0.0634 0.0787  513 THR B O   
3427 C CB  . THR B 174 ? 0.4723 0.4507 0.4705 -0.2230 -0.0708 0.1164  513 THR B CB  
3428 O OG1 . THR B 174 ? 0.4804 0.4923 0.4897 -0.2254 -0.0616 0.1286  513 THR B OG1 
3429 C CG2 . THR B 174 ? 0.5138 0.4445 0.5002 -0.2212 -0.0906 0.1114  513 THR B CG2 
3430 N N   . ARG B 175 ? 0.4940 0.4584 0.4700 -0.2160 -0.0604 0.0942  514 ARG B N   
3431 C CA  . ARG B 175 ? 0.5771 0.5117 0.5384 -0.2144 -0.0690 0.0834  514 ARG B CA  
3432 C C   . ARG B 175 ? 0.5919 0.5027 0.5226 -0.1998 -0.0471 0.0681  514 ARG B C   
3433 O O   . ARG B 175 ? 0.5425 0.4110 0.4505 -0.1820 -0.0530 0.0545  514 ARG B O   
3434 C CB  . ARG B 175 ? 0.6010 0.5734 0.5804 -0.2246 -0.0715 0.0914  514 ARG B CB  
3435 C CG  . ARG B 175 ? 0.7593 0.7582 0.7718 -0.2371 -0.0923 0.1092  514 ARG B CG  
3436 C CD  . ARG B 175 ? 0.7875 0.8393 0.8222 -0.2453 -0.0901 0.1202  514 ARG B CD  
3437 N NE  . ARG B 175 ? 0.8160 0.8880 0.8829 -0.2575 -0.1125 0.1386  514 ARG B NE  
3438 C CZ  . ARG B 175 ? 0.7513 0.8572 0.8374 -0.2634 -0.1090 0.1589  514 ARG B CZ  
3439 N NH1 . ARG B 175 ? 0.7532 0.8774 0.8300 -0.2561 -0.0863 0.1609  514 ARG B NH1 
3440 N NH2 . ARG B 175 ? 0.6905 0.8103 0.8050 -0.2764 -0.1304 0.1777  514 ARG B NH2 
3441 N N   . HIS B 176 ? 0.5337 0.4751 0.4629 -0.1962 -0.0210 0.0682  515 HIS B N   
3442 C CA  . HIS B 176 ? 0.5500 0.4730 0.4554 -0.1754 0.0002  0.0534  515 HIS B CA  
3443 C C   . HIS B 176 ? 0.5762 0.4664 0.4699 -0.1729 0.0005  0.0504  515 HIS B C   
3444 O O   . HIS B 176 ? 0.5525 0.4188 0.4280 -0.1543 0.0106  0.0404  515 HIS B O   
3445 C CB  . HIS B 176 ? 0.5061 0.4631 0.4127 -0.1740 0.0221  0.0539  515 HIS B CB  
3446 C CG  . HIS B 176 ? 0.5297 0.4664 0.4164 -0.1558 0.0405  0.0408  515 HIS B CG  
3447 N ND1 . HIS B 176 ? 0.5818 0.5100 0.4552 -0.1372 0.0478  0.0312  515 HIS B ND1 
3448 C CD2 . HIS B 176 ? 0.5783 0.5018 0.4591 -0.1542 0.0514  0.0374  515 HIS B CD2 
3449 C CE1 . HIS B 176 ? 0.6222 0.5312 0.4831 -0.1267 0.0627  0.0246  515 HIS B CE1 
3450 N NE2 . HIS B 176 ? 0.6101 0.5167 0.4767 -0.1378 0.0645  0.0283  515 HIS B NE2 
3451 N N   . VAL B 177 ? 0.5594 0.4584 0.4685 -0.1778 -0.0099 0.0568  516 VAL B N   
3452 C CA  . VAL B 177 ? 0.5405 0.4182 0.4411 -0.1695 -0.0093 0.0530  516 VAL B CA  
3453 C C   . VAL B 177 ? 0.5455 0.3758 0.4264 -0.1665 -0.0283 0.0499  516 VAL B C   
3454 O O   . VAL B 177 ? 0.5838 0.3877 0.4459 -0.1561 -0.0243 0.0458  516 VAL B O   
3455 C CB  . VAL B 177 ? 0.4590 0.3601 0.3775 -0.1734 -0.0122 0.0599  516 VAL B CB  
3456 C CG1 . VAL B 177 ? 0.4548 0.3364 0.3642 -0.1663 -0.0119 0.0565  516 VAL B CG1 
3457 C CG2 . VAL B 177 ? 0.4263 0.3644 0.3555 -0.1728 0.0034  0.0612  516 VAL B CG2 
3458 N N   . ILE B 178 ? 0.4948 0.3115 0.3781 -0.1732 -0.0517 0.0517  517 ILE B N   
3459 C CA  . ILE B 178 ? 0.6109 0.3793 0.4715 -0.1586 -0.0746 0.0425  517 ILE B CA  
3460 C C   . ILE B 178 ? 0.6138 0.3728 0.4517 -0.1283 -0.0607 0.0288  517 ILE B C   
3461 O O   . ILE B 178 ? 0.5990 0.3302 0.4117 -0.1035 -0.0618 0.0209  517 ILE B O   
3462 C CB  . ILE B 178 ? 0.6294 0.3884 0.5041 -0.1713 -0.1082 0.0465  517 ILE B CB  
3463 C CG1 . ILE B 178 ? 0.5596 0.3452 0.4609 -0.1834 -0.1146 0.0606  517 ILE B CG1 
3464 C CG2 . ILE B 178 ? 0.5792 0.2854 0.4257 -0.1483 -0.1356 0.0316  517 ILE B CG2 
3465 C CD1 . ILE B 178 ? 0.5316 0.3254 0.4565 -0.1956 -0.1401 0.0703  517 ILE B CD1 
3466 N N   . GLY B 179 ? 0.6186 0.4030 0.4638 -0.1274 -0.0467 0.0273  518 GLY B N   
3467 C CA  . GLY B 179 ? 0.5530 0.3301 0.3776 -0.0993 -0.0309 0.0172  518 GLY B CA  
3468 C C   . GLY B 179 ? 0.5359 0.3099 0.3494 -0.0870 -0.0070 0.0183  518 GLY B C   
3469 O O   . GLY B 179 ? 0.5801 0.3340 0.3716 -0.0606 -0.0044 0.0138  518 GLY B O   
3470 N N   . THR B 180 ? 0.4917 0.2882 0.3214 -0.1050 0.0096  0.0255  519 THR B N   
3471 C CA  . THR B 180 ? 0.5707 0.3670 0.3967 -0.0980 0.0294  0.0284  519 THR B CA  
3472 C C   . THR B 180 ? 0.6138 0.3893 0.4267 -0.0863 0.0205  0.0295  519 THR B C   
3473 O O   . THR B 180 ? 0.5483 0.3218 0.3528 -0.0694 0.0348  0.0324  519 THR B O   
3474 C CB  . THR B 180 ? 0.6250 0.4453 0.4701 -0.1204 0.0409  0.0338  519 THR B CB  
3475 O OG1 . THR B 180 ? 0.5307 0.3570 0.3866 -0.1393 0.0258  0.0389  519 THR B OG1 
3476 C CG2 . THR B 180 ? 0.6535 0.4939 0.5054 -0.1250 0.0506  0.0313  519 THR B CG2 
3477 N N   . GLN B 181 ? 0.5910 0.3518 0.4024 -0.0940 -0.0039 0.0289  520 GLN B N   
3478 C CA  . GLN B 181 ? 0.5670 0.3064 0.3629 -0.0817 -0.0144 0.0291  520 GLN B CA  
3479 C C   . GLN B 181 ? 0.6112 0.3290 0.3774 -0.0443 -0.0171 0.0221  520 GLN B C   
3480 O O   . GLN B 181 ? 0.6447 0.3607 0.3976 -0.0246 -0.0089 0.0251  520 GLN B O   
3481 C CB  . GLN B 181 ? 0.5628 0.2847 0.3622 -0.0982 -0.0436 0.0303  520 GLN B CB  
3482 C CG  . GLN B 181 ? 0.5492 0.2520 0.3351 -0.0906 -0.0533 0.0319  520 GLN B CG  
3483 C CD  . GLN B 181 ? 0.5216 0.1980 0.3084 -0.1055 -0.0862 0.0337  520 GLN B CD  
3484 O OE1 . GLN B 181 ? 0.5350 0.2125 0.3383 -0.1253 -0.1014 0.0367  520 GLN B OE1 
3485 N NE2 . GLN B 181 ? 0.5488 0.2024 0.3191 -0.0959 -0.0983 0.0337  520 GLN B NE2 
3486 N N   . GLY B 182 ? 0.5690 0.2743 0.3242 -0.0316 -0.0283 0.0136  521 GLY B N   
3487 C CA  . GLY B 182 ? 0.5764 0.2596 0.2986 0.0082  -0.0350 0.0054  521 GLY B CA  
3488 C C   . GLY B 182 ? 0.5327 0.2318 0.2476 0.0302  -0.0087 0.0078  521 GLY B C   
3489 O O   . GLY B 182 ? 0.5592 0.2485 0.2459 0.0677  -0.0070 0.0055  521 GLY B O   
3490 N N   . TYR B 183 ? 0.5126 0.2360 0.2506 0.0100  0.0114  0.0131  522 TYR B N   
3491 C CA  . TYR B 183 ? 0.4981 0.2325 0.2308 0.0280  0.0345  0.0165  522 TYR B CA  
3492 C C   . TYR B 183 ? 0.4751 0.2316 0.2256 0.0193  0.0636  0.0310  522 TYR B C   
3493 O O   . TYR B 183 ? 0.5036 0.2660 0.2466 0.0407  0.0822  0.0395  522 TYR B O   
3494 C CB  . TYR B 183 ? 0.5186 0.2587 0.2595 0.0174  0.0322  0.0099  522 TYR B CB  
3495 C CG  . TYR B 183 ? 0.5155 0.2365 0.2411 0.0292  0.0040  -0.0034 522 TYR B CG  
3496 C CD1 . TYR B 183 ? 0.5444 0.2510 0.2409 0.0664  0.0009  -0.0106 522 TYR B CD1 
3497 C CD2 . TYR B 183 ? 0.5139 0.2330 0.2558 0.0031  -0.0207 -0.0074 522 TYR B CD2 
3498 C CE1 . TYR B 183 ? 0.5724 0.2593 0.2550 0.0776  -0.0289 -0.0249 522 TYR B CE1 
3499 C CE2 . TYR B 183 ? 0.5409 0.2420 0.2741 0.0105  -0.0503 -0.0183 522 TYR B CE2 
3500 C CZ  . TYR B 183 ? 0.5707 0.2539 0.2736 0.0479  -0.0557 -0.0288 522 TYR B CZ  
3501 O OH  . TYR B 183 ? 0.6016 0.2645 0.2958 0.0559  -0.0891 -0.0418 522 TYR B OH  
3502 N N   . MET B 184 ? 0.3080 0.3664 0.2137 0.0015  0.0252  0.0324  523 MET B N   
3503 C CA  . MET B 184 ? 0.3076 0.3754 0.2165 0.0003  0.0233  0.0321  523 MET B CA  
3504 C C   . MET B 184 ? 0.2857 0.3642 0.1964 0.0011  0.0236  0.0324  523 MET B C   
3505 O O   . MET B 184 ? 0.3437 0.4261 0.2549 0.0055  0.0256  0.0338  523 MET B O   
3506 C CB  . MET B 184 ? 0.3367 0.4107 0.2499 0.0018  0.0229  0.0340  523 MET B CB  
3507 C CG  . MET B 184 ? 0.3733 0.4416 0.2854 0.0011  0.0219  0.0335  523 MET B CG  
3508 S SD  . MET B 184 ? 0.4749 0.5349 0.3800 -0.0025 0.0193  0.0302  523 MET B SD  
3509 C CE  . MET B 184 ? 0.4443 0.4975 0.3478 -0.0014 0.0192  0.0297  523 MET B CE  
3510 N N   . ALA B 185 ? 0.2722 0.3560 0.1826 -0.0031 0.0216  0.0314  524 ALA B N   
3511 C CA  . ALA B 185 ? 0.2571 0.3552 0.1700 -0.0037 0.0213  0.0319  524 ALA B CA  
3512 C C   . ALA B 185 ? 0.2492 0.3634 0.1677 -0.0026 0.0208  0.0340  524 ALA B C   
3513 O O   . ALA B 185 ? 0.2876 0.4007 0.2068 -0.0039 0.0199  0.0344  524 ALA B O   
3514 C CB  . ALA B 185 ? 0.2624 0.3606 0.1723 -0.0106 0.0189  0.0306  524 ALA B CB  
3515 N N   . PRO B 186 ? 0.2789 0.4098 0.2014 0.0005  0.0214  0.0353  525 PRO B N   
3516 C CA  . PRO B 186 ? 0.2851 0.4339 0.2135 0.0025  0.0209  0.0376  525 PRO B CA  
3517 C C   . PRO B 186 ? 0.2668 0.4216 0.1959 -0.0060 0.0179  0.0375  525 PRO B C   
3518 O O   . PRO B 186 ? 0.2751 0.4358 0.2070 -0.0052 0.0175  0.0387  525 PRO B O   
3519 C CB  . PRO B 186 ? 0.2971 0.4650 0.2289 0.0069  0.0214  0.0387  525 PRO B CB  
3520 C CG  . PRO B 186 ? 0.3359 0.4910 0.2623 0.0105  0.0234  0.0370  525 PRO B CG  
3521 C CD  . PRO B 186 ? 0.2960 0.4320 0.2176 0.0032  0.0225  0.0348  525 PRO B CD  
3522 N N   . GLU B 187 ? 0.2896 0.4422 0.2148 -0.0146 0.0158  0.0361  526 GLU B N   
3523 C CA  . GLU B 187 ? 0.2734 0.4290 0.1959 -0.0238 0.0128  0.0361  526 GLU B CA  
3524 C C   . GLU B 187 ? 0.2085 0.3455 0.1248 -0.0236 0.0125  0.0349  526 GLU B C   
3525 O O   . GLU B 187 ? 0.2510 0.3905 0.1647 -0.0280 0.0107  0.0350  526 GLU B O   
3526 C CB  . GLU B 187 ? 0.2083 0.3636 0.1262 -0.0338 0.0104  0.0356  526 GLU B CB  
3527 C CG  . GLU B 187 ? 0.2667 0.3976 0.1757 -0.0348 0.0101  0.0335  526 GLU B CG  
3528 C CD  . GLU B 187 ? 0.2457 0.3746 0.1566 -0.0302 0.0121  0.0328  526 GLU B CD  
3529 O OE1 . GLU B 187 ? 0.2063 0.3488 0.1238 -0.0241 0.0142  0.0337  526 GLU B OE1 
3530 O OE2 . GLU B 187 ? 0.2419 0.3554 0.1465 -0.0321 0.0115  0.0314  526 GLU B OE2 
3531 N N   . TYR B 188 ? 0.1694 0.2890 0.0827 -0.0185 0.0141  0.0336  527 TYR B N   
3532 C CA  . TYR B 188 ? 0.2861 0.3923 0.1947 -0.0165 0.0139  0.0327  527 TYR B CA  
3533 C C   . TYR B 188 ? 0.3067 0.4209 0.2226 -0.0101 0.0156  0.0344  527 TYR B C   
3534 O O   . TYR B 188 ? 0.2394 0.3534 0.1537 -0.0100 0.0148  0.0344  527 TYR B O   
3535 C CB  . TYR B 188 ? 0.3164 0.4042 0.2194 -0.0144 0.0144  0.0310  527 TYR B CB  
3536 C CG  . TYR B 188 ? 0.2767 0.3533 0.1743 -0.0119 0.0138  0.0300  527 TYR B CG  
3537 C CD1 . TYR B 188 ? 0.3285 0.3968 0.2154 -0.0146 0.0110  0.0287  527 TYR B CD1 
3538 C CD2 . TYR B 188 ? 0.2752 0.3502 0.1773 -0.0067 0.0156  0.0304  527 TYR B CD2 
3539 C CE1 . TYR B 188 ? 0.3410 0.3993 0.2211 -0.0108 0.0102  0.0274  527 TYR B CE1 
3540 C CE2 . TYR B 188 ? 0.2811 0.3503 0.1795 -0.0044 0.0148  0.0297  527 TYR B CE2 
3541 C CZ  . TYR B 188 ? 0.3172 0.3781 0.2044 -0.0059 0.0122  0.0280  527 TYR B CZ  
3542 O OH  . TYR B 188 ? 0.3760 0.4319 0.2583 -0.0024 0.0113  0.0269  527 TYR B OH  
3543 N N   . ILE B 189 ? 0.2941 0.4143 0.2163 -0.0044 0.0179  0.0360  528 ILE B N   
3544 C CA  . ILE B 189 ? 0.2740 0.4006 0.2019 0.0019  0.0194  0.0384  528 ILE B CA  
3545 C C   . ILE B 189 ? 0.2488 0.3935 0.1815 0.0017  0.0184  0.0400  528 ILE B C   
3546 O O   . ILE B 189 ? 0.2505 0.3994 0.1859 0.0043  0.0183  0.0413  528 ILE B O   
3547 C CB  . ILE B 189 ? 0.2654 0.3907 0.1950 0.0081  0.0221  0.0400  528 ILE B CB  
3548 C CG1 . ILE B 189 ? 0.2433 0.3511 0.1676 0.0070  0.0230  0.0384  528 ILE B CG1 
3549 C CG2 . ILE B 189 ? 0.3651 0.4954 0.2986 0.0146  0.0236  0.0433  528 ILE B CG2 
3550 C CD1 . ILE B 189 ? 0.2751 0.3779 0.1973 0.0117  0.0255  0.0394  528 ILE B CD1 
3551 N N   . GLU B 190 ? 0.2541 0.4122 0.1883 -0.0016 0.0173  0.0402  529 GLU B N   
3552 C CA  . GLU B 190 ? 0.2621 0.4414 0.2018 -0.0020 0.0162  0.0420  529 GLU B CA  
3553 C C   . GLU B 190 ? 0.2570 0.4379 0.1924 -0.0118 0.0134  0.0406  529 GLU B C   
3554 O O   . GLU B 190 ? 0.2186 0.4121 0.1569 -0.0123 0.0124  0.0417  529 GLU B O   
3555 C CB  . GLU B 190 ? 0.2950 0.4931 0.2396 0.0000  0.0163  0.0435  529 GLU B CB  
3556 C CG  . GLU B 190 ? 0.3891 0.5849 0.3350 0.0112  0.0193  0.0451  529 GLU B CG  
3557 C CD  . GLU B 190 ? 0.4004 0.6165 0.3500 0.0157  0.0195  0.0465  529 GLU B CD  
3558 O OE1 . GLU B 190 ? 0.3336 0.5696 0.2869 0.0094  0.0171  0.0467  529 GLU B OE1 
3559 O OE2 . GLU B 190 ? 0.4886 0.7011 0.4365 0.0256  0.0221  0.0475  529 GLU B OE2 
3560 N N   . ASN B 191 ? 0.2247 0.3917 0.1514 -0.0195 0.0118  0.0383  530 ASN B N   
3561 C CA  . ASN B 191 ? 0.2145 0.3784 0.1329 -0.0292 0.0089  0.0372  530 ASN B CA  
3562 C C   . ASN B 191 ? 0.2588 0.3956 0.1637 -0.0311 0.0078  0.0346  530 ASN B C   
3563 O O   . ASN B 191 ? 0.2709 0.3996 0.1648 -0.0383 0.0048  0.0335  530 ASN B O   
3564 C CB  . ASN B 191 ? 0.2446 0.4238 0.1640 -0.0392 0.0067  0.0381  530 ASN B CB  
3565 C CG  . ASN B 191 ? 0.2932 0.5022 0.2256 -0.0357 0.0074  0.0407  530 ASN B CG  
3566 O OD1 . ASN B 191 ? 0.3076 0.5346 0.2445 -0.0372 0.0065  0.0422  530 ASN B OD1 
3567 N ND2 . ASN B 191 ? 0.2777 0.4923 0.2151 -0.0301 0.0090  0.0414  530 ASN B ND2 
3568 N N   . GLY B 192 ? 0.2711 0.3938 0.1753 -0.0246 0.0097  0.0336  531 GLY B N   
3569 C CA  . GLY B 192 ? 0.2355 0.3348 0.1270 -0.0244 0.0084  0.0313  531 GLY B CA  
3570 C C   . GLY B 192 ? 0.2696 0.3587 0.1510 -0.0318 0.0056  0.0303  531 GLY B C   
3571 O O   . GLY B 192 ? 0.2581 0.3285 0.1253 -0.0320 0.0029  0.0285  531 GLY B O   
3572 N N   . LEU B 193 ? 0.2468 0.3484 0.1344 -0.0372 0.0056  0.0316  532 LEU B N   
3573 C CA  . LEU B 193 ? 0.2503 0.3457 0.1300 -0.0464 0.0026  0.0314  532 LEU B CA  
3574 C C   . LEU B 193 ? 0.2692 0.3476 0.1444 -0.0419 0.0032  0.0299  532 LEU B C   
3575 O O   . LEU B 193 ? 0.3040 0.3879 0.1876 -0.0376 0.0059  0.0302  532 LEU B O   
3576 C CB  . LEU B 193 ? 0.2629 0.3817 0.1520 -0.0540 0.0023  0.0335  532 LEU B CB  
3577 C CG  . LEU B 193 ? 0.3245 0.4400 0.2073 -0.0652 -0.0007 0.0340  532 LEU B CG  
3578 C CD1 . LEU B 193 ? 0.3228 0.4225 0.1903 -0.0752 -0.0053 0.0337  532 LEU B CD1 
3579 C CD2 . LEU B 193 ? 0.2601 0.4039 0.1538 -0.0717 -0.0008 0.0363  532 LEU B CD2 
3580 N N   . ILE B 194 ? 0.3058 0.3641 0.1671 -0.0421 0.0003  0.0284  533 ILE B N   
3581 C CA  . ILE B 194 ? 0.2676 0.3110 0.1240 -0.0369 0.0004  0.0270  533 ILE B CA  
3582 C C   . ILE B 194 ? 0.3179 0.3592 0.1703 -0.0466 -0.0023 0.0276  533 ILE B C   
3583 O O   . ILE B 194 ? 0.3500 0.3822 0.1909 -0.0549 -0.0067 0.0278  533 ILE B O   
3584 C CB  . ILE B 194 ? 0.3160 0.3415 0.1596 -0.0289 -0.0015 0.0249  533 ILE B CB  
3585 C CG1 . ILE B 194 ? 0.3524 0.3810 0.2001 -0.0210 0.0012  0.0246  533 ILE B CG1 
3586 C CG2 . ILE B 194 ? 0.3727 0.3873 0.2125 -0.0230 -0.0016 0.0236  533 ILE B CG2 
3587 C CD1 . ILE B 194 ? 0.3884 0.4019 0.2232 -0.0116 -0.0007 0.0223  533 ILE B CD1 
3588 N N   . THR B 195 ? 0.3034 0.3521 0.1642 -0.0463 0.0000  0.0282  534 THR B N   
3589 C CA  . THR B 195 ? 0.2773 0.3244 0.1347 -0.0548 -0.0023 0.0289  534 THR B CA  
3590 C C   . THR B 195 ? 0.2942 0.3354 0.1538 -0.0477 -0.0002 0.0277  534 THR B C   
3591 O O   . THR B 195 ? 0.3072 0.3493 0.1728 -0.0382 0.0032  0.0268  534 THR B O   
3592 C CB  . THR B 195 ? 0.2533 0.3230 0.1198 -0.0640 -0.0021 0.0311  534 THR B CB  
3593 O OG1 . THR B 195 ? 0.3243 0.4094 0.2037 -0.0559 0.0021  0.0310  534 THR B OG1 
3594 C CG2 . THR B 195 ? 0.2823 0.3604 0.1472 -0.0721 -0.0043 0.0325  534 THR B CG2 
3595 N N   . PRO B 196 ? 0.2753 0.3104 0.1297 -0.0531 -0.0023 0.0280  535 PRO B N   
3596 C CA  . PRO B 196 ? 0.2986 0.3321 0.1567 -0.0471 -0.0001 0.0270  535 PRO B CA  
3597 C C   . PRO B 196 ? 0.2914 0.3413 0.1621 -0.0433 0.0040  0.0271  535 PRO B C   
3598 O O   . PRO B 196 ? 0.2880 0.3351 0.1612 -0.0373 0.0061  0.0259  535 PRO B O   
3599 C CB  . PRO B 196 ? 0.3056 0.3341 0.1568 -0.0564 -0.0034 0.0280  535 PRO B CB  
3600 C CG  . PRO B 196 ? 0.3346 0.3681 0.1822 -0.0692 -0.0066 0.0302  535 PRO B CG  
3601 C CD  . PRO B 196 ? 0.2958 0.3255 0.1406 -0.0663 -0.0070 0.0296  535 PRO B CD  
3602 N N   . LYS B 197 ? 0.3163 0.3830 0.1940 -0.0464 0.0048  0.0284  536 LYS B N   
3603 C CA  . LYS B 197 ? 0.2518 0.3336 0.1395 -0.0412 0.0081  0.0285  536 LYS B CA  
3604 C C   . LYS B 197 ? 0.2606 0.3360 0.1511 -0.0311 0.0112  0.0273  536 LYS B C   
3605 O O   . LYS B 197 ? 0.2997 0.3772 0.1938 -0.0256 0.0139  0.0267  536 LYS B O   
3606 C CB  . LYS B 197 ? 0.2672 0.3716 0.1616 -0.0461 0.0077  0.0305  536 LYS B CB  
3607 C CG  . LYS B 197 ? 0.2631 0.3783 0.1561 -0.0580 0.0046  0.0322  536 LYS B CG  
3608 C CD  . LYS B 197 ? 0.2613 0.3761 0.1541 -0.0569 0.0053  0.0316  536 LYS B CD  
3609 C CE  . LYS B 197 ? 0.2648 0.3943 0.1576 -0.0691 0.0024  0.0340  536 LYS B CE  
3610 N NZ  . LYS B 197 ? 0.3199 0.4504 0.2127 -0.0675 0.0032  0.0334  536 LYS B NZ  
3611 N N   . MET B 198 ? 0.2935 0.3611 0.1814 -0.0292 0.0108  0.0272  537 MET B N   
3612 C CA  . MET B 198 ? 0.2422 0.3048 0.1328 -0.0215 0.0134  0.0266  537 MET B CA  
3613 C C   . MET B 198 ? 0.2555 0.3057 0.1433 -0.0177 0.0144  0.0252  537 MET B C   
3614 O O   . MET B 198 ? 0.2720 0.3213 0.1630 -0.0134 0.0168  0.0249  537 MET B O   
3615 C CB  . MET B 198 ? 0.2385 0.2966 0.1264 -0.0206 0.0125  0.0268  537 MET B CB  
3616 C CG  . MET B 198 ? 0.2746 0.3166 0.1521 -0.0199 0.0102  0.0256  537 MET B CG  
3617 S SD  . MET B 198 ? 0.3895 0.4269 0.2624 -0.0167 0.0094  0.0254  537 MET B SD  
3618 C CE  . MET B 198 ? 0.3513 0.3968 0.2358 -0.0119 0.0131  0.0262  537 MET B CE  
3619 N N   . ASP B 199 ? 0.3028 0.3438 0.1839 -0.0196 0.0122  0.0243  538 ASP B N   
3620 C CA  . ASP B 199 ? 0.2639 0.2966 0.1430 -0.0164 0.0128  0.0230  538 ASP B CA  
3621 C C   . ASP B 199 ? 0.2256 0.2644 0.1084 -0.0170 0.0144  0.0227  538 ASP B C   
3622 O O   . ASP B 199 ? 0.2075 0.2425 0.0910 -0.0135 0.0162  0.0217  538 ASP B O   
3623 C CB  . ASP B 199 ? 0.2382 0.2611 0.1088 -0.0171 0.0097  0.0224  538 ASP B CB  
3624 C CG  . ASP B 199 ? 0.3163 0.3299 0.1806 -0.0121 0.0085  0.0218  538 ASP B CG  
3625 O OD1 . ASP B 199 ? 0.2953 0.3102 0.1629 -0.0095 0.0103  0.0220  538 ASP B OD1 
3626 O OD2 . ASP B 199 ? 0.3481 0.3544 0.2038 -0.0104 0.0056  0.0213  538 ASP B OD2 
3627 N N   . VAL B 200 ? 0.2036 0.2528 0.0880 -0.0216 0.0136  0.0235  539 VAL B N   
3628 C CA  . VAL B 200 ? 0.2849 0.3419 0.1720 -0.0209 0.0152  0.0230  539 VAL B CA  
3629 C C   . VAL B 200 ? 0.2626 0.3230 0.1530 -0.0152 0.0184  0.0228  539 VAL B C   
3630 O O   . VAL B 200 ? 0.2411 0.2986 0.1297 -0.0117 0.0203  0.0215  539 VAL B O   
3631 C CB  . VAL B 200 ? 0.2630 0.3346 0.1519 -0.0276 0.0135  0.0244  539 VAL B CB  
3632 C CG1 . VAL B 200 ? 0.2649 0.3480 0.1567 -0.0250 0.0154  0.0239  539 VAL B CG1 
3633 C CG2 . VAL B 200 ? 0.2441 0.3090 0.1272 -0.0344 0.0102  0.0248  539 VAL B CG2 
3634 N N   . PHE B 201 ? 0.2843 0.3496 0.1779 -0.0142 0.0188  0.0242  540 PHE B N   
3635 C CA  . PHE B 201 ? 0.2516 0.3187 0.1470 -0.0087 0.0216  0.0245  540 PHE B CA  
3636 C C   . PHE B 201 ? 0.2224 0.2742 0.1138 -0.0060 0.0231  0.0234  540 PHE B C   
3637 O O   . PHE B 201 ? 0.2752 0.3224 0.1628 -0.0034 0.0250  0.0224  540 PHE B O   
3638 C CB  . PHE B 201 ? 0.2501 0.3253 0.1500 -0.0084 0.0213  0.0264  540 PHE B CB  
3639 C CG  . PHE B 201 ? 0.2388 0.3186 0.1406 -0.0024 0.0238  0.0274  540 PHE B CG  
3640 C CD1 . PHE B 201 ? 0.2467 0.3158 0.1468 0.0004  0.0253  0.0278  540 PHE B CD1 
3641 C CD2 . PHE B 201 ? 0.2502 0.3465 0.1552 0.0007  0.0244  0.0283  540 PHE B CD2 
3642 C CE1 . PHE B 201 ? 0.2440 0.3155 0.1439 0.0057  0.0273  0.0292  540 PHE B CE1 
3643 C CE2 . PHE B 201 ? 0.3166 0.4164 0.2219 0.0079  0.0265  0.0294  540 PHE B CE2 
3644 C CZ  . PHE B 201 ? 0.2318 0.3177 0.1338 0.0103  0.0280  0.0299  540 PHE B CZ  
3645 N N   . ALA B 202 ? 0.2471 0.2916 0.1384 -0.0070 0.0221  0.0237  541 ALA B N   
3646 C CA  . ALA B 202 ? 0.2448 0.2788 0.1335 -0.0056 0.0231  0.0234  541 ALA B CA  
3647 C C   . ALA B 202 ? 0.2593 0.2864 0.1433 -0.0056 0.0234  0.0216  541 ALA B C   
3648 O O   . ALA B 202 ? 0.2625 0.2826 0.1422 -0.0045 0.0252  0.0212  541 ALA B O   
3649 C CB  . ALA B 202 ? 0.1877 0.2190 0.0774 -0.0064 0.0214  0.0238  541 ALA B CB  
3650 N N   . PHE B 203 ? 0.2427 0.2710 0.1263 -0.0074 0.0214  0.0205  542 PHE B N   
3651 C CA  . PHE B 203 ? 0.2168 0.2410 0.0968 -0.0071 0.0214  0.0188  542 PHE B CA  
3652 C C   . PHE B 203 ? 0.2725 0.2972 0.1491 -0.0053 0.0237  0.0178  542 PHE B C   
3653 O O   . PHE B 203 ? 0.3102 0.3290 0.1814 -0.0043 0.0246  0.0163  542 PHE B O   
3654 C CB  . PHE B 203 ? 0.2151 0.2427 0.0951 -0.0098 0.0188  0.0184  542 PHE B CB  
3655 C CG  . PHE B 203 ? 0.2264 0.2507 0.1034 -0.0096 0.0184  0.0167  542 PHE B CG  
3656 C CD1 . PHE B 203 ? 0.2659 0.2837 0.1411 -0.0078 0.0186  0.0158  542 PHE B CD1 
3657 C CD2 . PHE B 203 ? 0.2433 0.2733 0.1197 -0.0120 0.0174  0.0163  542 PHE B CD2 
3658 C CE1 . PHE B 203 ? 0.2677 0.2841 0.1404 -0.0077 0.0179  0.0141  542 PHE B CE1 
3659 C CE2 . PHE B 203 ? 0.2533 0.2810 0.1270 -0.0118 0.0169  0.0147  542 PHE B CE2 
3660 C CZ  . PHE B 203 ? 0.2442 0.2648 0.1161 -0.0094 0.0171  0.0134  542 PHE B CZ  
3661 N N   . GLY B 204 ? 0.2368 0.2712 0.1158 -0.0047 0.0244  0.0186  543 GLY B N   
3662 C CA  . GLY B 204 ? 0.2668 0.3040 0.1419 -0.0015 0.0265  0.0174  543 GLY B CA  
3663 C C   . GLY B 204 ? 0.3051 0.3362 0.1749 0.0007  0.0282  0.0178  543 GLY B C   
3664 O O   . GLY B 204 ? 0.2659 0.2947 0.1281 0.0029  0.0290  0.0160  543 GLY B O   
3665 N N   . VAL B 205 ? 0.3224 0.3512 0.1949 0.0000  0.0283  0.0202  544 VAL B N   
3666 C CA  . VAL B 205 ? 0.2408 0.2643 0.1077 0.0010  0.0295  0.0220  544 VAL B CA  
3667 C C   . VAL B 205 ? 0.2650 0.2782 0.1252 -0.0020 0.0290  0.0212  544 VAL B C   
3668 O O   . VAL B 205 ? 0.2753 0.2838 0.1257 -0.0019 0.0295  0.0217  544 VAL B O   
3669 C CB  . VAL B 205 ? 0.2704 0.2953 0.1429 0.0006  0.0295  0.0252  544 VAL B CB  
3670 C CG1 . VAL B 205 ? 0.2879 0.3062 0.1542 0.0001  0.0302  0.0286  544 VAL B CG1 
3671 C CG2 . VAL B 205 ? 0.2411 0.2771 0.1185 0.0050  0.0301  0.0264  544 VAL B CG2 
3672 N N   . VAL B 206 ? 0.2502 0.2617 0.1155 -0.0037 0.0276  0.0204  545 VAL B N   
3673 C CA  . VAL B 206 ? 0.2616 0.2693 0.1240 -0.0044 0.0268  0.0200  545 VAL B CA  
3674 C C   . VAL B 206 ? 0.2967 0.3015 0.1500 -0.0033 0.0270  0.0170  545 VAL B C   
3675 O O   . VAL B 206 ? 0.3307 0.3334 0.1770 -0.0029 0.0267  0.0172  545 VAL B O   
3676 C CB  . VAL B 206 ? 0.2302 0.2411 0.1006 -0.0055 0.0244  0.0194  545 VAL B CB  
3677 C CG1 . VAL B 206 ? 0.1930 0.2054 0.0625 -0.0072 0.0228  0.0184  545 VAL B CG1 
3678 C CG2 . VAL B 206 ? 0.2415 0.2543 0.1176 -0.0061 0.0239  0.0214  545 VAL B CG2 
3679 N N   . ILE B 207 ? 0.2635 0.2717 0.1178 -0.0027 0.0269  0.0145  546 ILE B N   
3680 C CA  . ILE B 207 ? 0.2677 0.2748 0.1138 -0.0017 0.0270  0.0108  546 ILE B CA  
3681 C C   . ILE B 207 ? 0.2963 0.3028 0.1321 -0.0005 0.0279  0.0096  546 ILE B C   
3682 O O   . ILE B 207 ? 0.3220 0.3262 0.1485 -0.0003 0.0269  0.0063  546 ILE B O   
3683 C CB  . ILE B 207 ? 0.2630 0.2796 0.1148 -0.0008 0.0267  0.0095  546 ILE B CB  
3684 C CG1 . ILE B 207 ? 0.2662 0.2841 0.1259 -0.0031 0.0245  0.0107  546 ILE B CG1 
3685 C CG2 . ILE B 207 ? 0.2425 0.2616 0.0871 0.0015  0.0269  0.0055  546 ILE B CG2 
3686 C CD1 . ILE B 207 ? 0.2786 0.3058 0.1427 -0.0038 0.0238  0.0108  546 ILE B CD1 
3687 N N   . LEU B 208 ? 0.2762 0.2883 0.1151 0.0038  0.0290  0.0122  547 LEU B N   
3688 C CA  . LEU B 208 ? 0.2978 0.3038 0.1251 0.0135  0.0297  0.0126  547 LEU B CA  
3689 C C   . LEU B 208 ? 0.3347 0.3227 0.1499 0.0109  0.0290  0.0152  547 LEU B C   
3690 O O   . LEU B 208 ? 0.3568 0.3197 0.1510 0.0167  0.0284  0.0131  547 LEU B O   
3691 C CB  . LEU B 208 ? 0.3016 0.3138 0.1337 0.0203  0.0313  0.0161  547 LEU B CB  
3692 C CG  . LEU B 208 ? 0.2830 0.3115 0.1238 0.0248  0.0319  0.0143  547 LEU B CG  
3693 C CD1 . LEU B 208 ? 0.3008 0.3370 0.1466 0.0308  0.0331  0.0181  547 LEU B CD1 
3694 C CD2 . LEU B 208 ? 0.3048 0.3335 0.1364 0.0349  0.0320  0.0095  547 LEU B CD2 
3695 N N   . GLU B 209 ? 0.2950 0.2898 0.1202 0.0013  0.0283  0.0196  548 GLU B N   
3696 C CA  . GLU B 209 ? 0.3115 0.2884 0.1267 -0.0050 0.0272  0.0224  548 GLU B CA  
3697 C C   . GLU B 209 ? 0.3272 0.2939 0.1344 -0.0106 0.0247  0.0168  548 GLU B C   
3698 O O   . GLU B 209 ? 0.3441 0.2906 0.1438 -0.0153 0.0214  0.0158  548 GLU B O   
3699 C CB  . GLU B 209 ? 0.3197 0.3123 0.1525 -0.0102 0.0269  0.0274  548 GLU B CB  
3700 C CG  . GLU B 209 ? 0.3137 0.3130 0.1544 -0.0044 0.0291  0.0322  548 GLU B CG  
3701 C CD  . GLU B 209 ? 0.3344 0.3365 0.1860 -0.0087 0.0289  0.0340  548 GLU B CD  
3702 O OE1 . GLU B 209 ? 0.3668 0.3705 0.2196 -0.0160 0.0271  0.0373  548 GLU B OE1 
3703 O OE2 . GLU B 209 ? 0.3443 0.3500 0.2048 -0.0074 0.0289  0.0316  548 GLU B OE2 
3704 N N   . LEU B 210 ? 0.3028 0.2872 0.1210 -0.0093 0.0243  0.0131  549 LEU B N   
3705 C CA  . LEU B 210 ? 0.3359 0.3139 0.1477 -0.0141 0.0220  0.0077  549 LEU B CA  
3706 C C   . LEU B 210 ? 0.3810 0.3387 0.1745 -0.0082 0.0211  0.0016  549 LEU B C   
3707 O O   . LEU B 210 ? 0.3477 0.2890 0.1340 -0.0133 0.0175  -0.0022 549 LEU B O   
3708 C CB  . LEU B 210 ? 0.2589 0.2563 0.0868 -0.0106 0.0216  0.0062  549 LEU B CB  
3709 C CG  . LEU B 210 ? 0.2773 0.2828 0.1197 -0.0143 0.0207  0.0097  549 LEU B CG  
3710 C CD1 . LEU B 210 ? 0.2286 0.2394 0.0796 -0.0100 0.0204  0.0087  549 LEU B CD1 
3711 C CD2 . LEU B 210 ? 0.3121 0.3156 0.1520 -0.0242 0.0182  0.0090  549 LEU B CD2 
3712 N N   . LEU B 211 ? 0.3587 0.3200 0.1484 0.0040  0.0236  0.0003  550 LEU B N   
3713 C CA  . LEU B 211 ? 0.3554 0.3012 0.1313 0.0143  0.0222  -0.0063 550 LEU B CA  
3714 C C   . LEU B 211 ? 0.3746 0.2891 0.1390 0.0154  0.0191  -0.0059 550 LEU B C   
3715 O O   . LEU B 211 ? 0.3750 0.2657 0.1261 0.0151  0.0150  -0.0115 550 LEU B O   
3716 C CB  . LEU B 211 ? 0.3259 0.2918 0.1085 0.0264  0.0250  -0.0070 550 LEU B CB  
3717 C CG  . LEU B 211 ? 0.2992 0.2946 0.1026 0.0199  0.0259  -0.0069 550 LEU B CG  
3718 C CD1 . LEU B 211 ? 0.3494 0.3603 0.1619 0.0267  0.0279  -0.0052 550 LEU B CD1 
3719 C CD2 . LEU B 211 ? 0.3542 0.3494 0.1534 0.0190  0.0243  -0.0132 550 LEU B CD2 
3720 N N   . SER B 212 ? 0.3944 0.3071 0.1621 0.0162  0.0205  0.0010  551 SER B N   
3721 C CA  . SER B 212 ? 0.3730 0.2553 0.1280 0.0185  0.0175  0.0027  551 SER B CA  
3722 C C   . SER B 212 ? 0.3923 0.2612 0.1491 0.0015  0.0142  0.0080  551 SER B C   
3723 O O   . SER B 212 ? 0.4156 0.2528 0.1578 -0.0014 0.0096  0.0080  551 SER B O   
3724 C CB  . SER B 212 ? 0.4006 0.2892 0.1568 0.0300  0.0209  0.0078  551 SER B CB  
3725 O OG  . SER B 212 ? 0.3627 0.2739 0.1352 0.0222  0.0239  0.0152  551 SER B OG  
3726 N N   . GLY B 213 ? 0.3913 0.2835 0.1640 -0.0097 0.0158  0.0126  552 GLY B N   
3727 C CA  . GLY B 213 ? 0.4055 0.2930 0.1815 -0.0248 0.0133  0.0190  552 GLY B CA  
3728 C C   . GLY B 213 ? 0.3628 0.2445 0.1389 -0.0240 0.0142  0.0272  552 GLY B C   
3729 O O   . GLY B 213 ? 0.3550 0.2326 0.1324 -0.0369 0.0119  0.0335  552 GLY B O   
3730 N N   . ARG B 214 ? 0.3521 0.2361 0.1270 -0.0095 0.0175  0.0278  553 ARG B N   
3731 C CA  . ARG B 214 ? 0.3660 0.2444 0.1400 -0.0070 0.0184  0.0356  553 ARG B CA  
3732 C C   . ARG B 214 ? 0.3903 0.2995 0.1819 -0.0114 0.0222  0.0419  553 ARG B C   
3733 O O   . ARG B 214 ? 0.3633 0.2969 0.1662 -0.0126 0.0244  0.0397  553 ARG B O   
3734 C CB  . ARG B 214 ? 0.3652 0.2360 0.1299 0.0118  0.0202  0.0335  553 ARG B CB  
3735 C CG  . ARG B 214 ? 0.3970 0.2380 0.1420 0.0207  0.0166  0.0259  553 ARG B CG  
3736 C CD  . ARG B 214 ? 0.4071 0.2468 0.1433 0.0419  0.0189  0.0241  553 ARG B CD  
3737 N NE  . ARG B 214 ? 0.5323 0.3410 0.2464 0.0533  0.0148  0.0165  553 ARG B NE  
3738 C CZ  . ARG B 214 ? 0.5947 0.3965 0.2958 0.0743  0.0155  0.0139  553 ARG B CZ  
3739 N NH1 . ARG B 214 ? 0.5832 0.4085 0.2920 0.0851  0.0202  0.0185  553 ARG B NH1 
3740 N NH2 . ARG B 214 ? 0.5758 0.3469 0.2544 0.0854  0.0112  0.0061  553 ARG B NH2 
3741 N N   . GLU B 215 ? 0.3799 0.2860 0.1722 -0.0134 0.0224  0.0500  554 GLU B N   
3742 C CA  . GLU B 215 ? 0.3689 0.3026 0.1756 -0.0149 0.0258  0.0558  554 GLU B CA  
3743 C C   . GLU B 215 ? 0.3745 0.3236 0.1849 -0.0008 0.0300  0.0543  554 GLU B C   
3744 O O   . GLU B 215 ? 0.3655 0.3026 0.1665 0.0110  0.0305  0.0525  554 GLU B O   
3745 C CB  . GLU B 215 ? 0.4170 0.3439 0.2225 -0.0218 0.0246  0.0654  554 GLU B CB  
3746 C CG  . GLU B 215 ? 0.4253 0.3378 0.2256 -0.0383 0.0198  0.0685  554 GLU B CG  
3747 C CD  . GLU B 215 ? 0.4995 0.4409 0.3137 -0.0499 0.0203  0.0716  554 GLU B CD  
3748 O OE1 . GLU B 215 ? 0.5263 0.4959 0.3591 -0.0414 0.0237  0.0689  554 GLU B OE1 
3749 O OE2 . GLU B 215 ? 0.5431 0.4809 0.3558 -0.0642 0.0165  0.0742  554 GLU B OE2 
3750 N N   . VAL B 216 ? 0.3509 0.3297 0.1798 -0.0031 0.0312  0.0535  555 VAL B N   
3751 C CA  . VAL B 216 ? 0.2743 0.2677 0.1140 0.0038  0.0322  0.0488  555 VAL B CA  
3752 C C   . VAL B 216 ? 0.3385 0.3285 0.1754 0.0122  0.0335  0.0536  555 VAL B C   
3753 O O   . VAL B 216 ? 0.3350 0.3306 0.1728 0.0222  0.0347  0.0508  555 VAL B O   
3754 C CB  . VAL B 216 ? 0.3027 0.3087 0.1583 -0.0020 0.0315  0.0444  555 VAL B CB  
3755 C CG1 . VAL B 216 ? 0.3463 0.3498 0.2020 -0.0061 0.0309  0.0401  555 VAL B CG1 
3756 C CG2 . VAL B 216 ? 0.3667 0.3744 0.2282 -0.0047 0.0316  0.0487  555 VAL B CG2 
3757 N N   . VAL B 217 ? 0.3388 0.3212 0.1727 0.0081  0.0330  0.0611  556 VAL B N   
3758 C CA  . VAL B 217 ? 0.3226 0.2988 0.1521 0.0157  0.0339  0.0667  556 VAL B CA  
3759 C C   . VAL B 217 ? 0.3810 0.3236 0.1885 0.0148  0.0327  0.0738  556 VAL B C   
3760 O O   . VAL B 217 ? 0.3693 0.3073 0.1771 0.0020  0.0309  0.0794  556 VAL B O   
3761 C CB  . VAL B 217 ? 0.3259 0.3190 0.1712 0.0105  0.0336  0.0684  556 VAL B CB  
3762 C CG1 . VAL B 217 ? 0.4077 0.3949 0.2479 0.0181  0.0343  0.0750  556 VAL B CG1 
3763 C CG2 . VAL B 217 ? 0.3502 0.3633 0.2117 0.0114  0.0339  0.0602  556 VAL B CG2 
3764 N N   . GLY B 218 ? 0.4004 0.3181 0.1895 0.0268  0.0321  0.0720  557 GLY B N   
3765 C CA  . GLY B 218 ? 0.4290 0.3086 0.2009 0.0239  0.0273  0.0740  557 GLY B CA  
3766 C C   . GLY B 218 ? 0.5568 0.4193 0.3168 0.0348  0.0269  0.0803  557 GLY B C   
3767 O O   . GLY B 218 ? 0.5933 0.4764 0.3598 0.0448  0.0308  0.0834  557 GLY B O   
3768 N N   . SER B 219 ? 0.5616 0.3838 0.3022 0.0323  0.0215  0.0823  558 SER B N   
3769 C CA  . SER B 219 ? 0.5341 0.3308 0.2580 0.0430  0.0198  0.0884  558 SER B CA  
3770 C C   . SER B 219 ? 0.6192 0.3986 0.3262 0.0654  0.0192  0.0805  558 SER B C   
3771 O O   . SER B 219 ? 0.6366 0.3921 0.3305 0.0665  0.0154  0.0727  558 SER B O   
3772 C CB  . SER B 219 ? 0.6719 0.4303 0.3802 0.0275  0.0132  0.0955  558 SER B CB  
3773 O OG  . SER B 219 ? 0.8366 0.6154 0.5608 0.0059  0.0135  0.1016  558 SER B OG  
3774 N N   . ASP B 220 ? 0.6168 0.4107 0.3237 0.0839  0.0228  0.0823  559 ASP B N   
3775 C CA  . ASP B 220 ? 0.6467 0.4247 0.3348 0.1078  0.0219  0.0761  559 ASP B CA  
3776 C C   . ASP B 220 ? 0.7186 0.4392 0.3769 0.1103  0.0145  0.0781  559 ASP B C   
3777 O O   . ASP B 220 ? 0.7180 0.4202 0.3680 0.1085  0.0125  0.0878  559 ASP B O   
3778 C CB  . ASP B 220 ? 0.6293 0.4369 0.3227 0.1265  0.0270  0.0792  559 ASP B CB  
3779 C CG  . ASP B 220 ? 0.6748 0.4777 0.3515 0.1532  0.0270  0.0720  559 ASP B CG  
3780 O OD1 . ASP B 220 ? 0.7200 0.4842 0.3746 0.1599  0.0218  0.0661  559 ASP B OD1 
3781 O OD2 . ASP B 220 ? 0.6021 0.4426 0.2901 0.1667  0.0319  0.0710  559 ASP B OD2 
3782 N N   . LYS B 221 ? 0.7158 0.4062 0.3566 0.1138  0.0099  0.0691  560 LYS B N   
3783 C CA  . LYS B 221 ? 0.7395 0.3696 0.3488 0.1136  0.0014  0.0701  560 LYS B CA  
3784 C C   . LYS B 221 ? 0.8176 0.4210 0.3997 0.1438  -0.0007 0.0664  560 LYS B C   
3785 O O   . LYS B 221 ? 0.8645 0.4248 0.4239 0.1463  -0.0065 0.0708  560 LYS B O   
3786 C CB  . LYS B 221 ? 0.7779 0.3848 0.3798 0.0992  -0.0038 0.0622  560 LYS B CB  
3787 C CG  . LYS B 221 ? 0.7429 0.3690 0.3664 0.0690  -0.0032 0.0669  560 LYS B CG  
3788 C CD  . LYS B 221 ? 0.7974 0.3971 0.4104 0.0543  -0.0093 0.0601  560 LYS B CD  
3789 C CE  . LYS B 221 ? 0.8556 0.4758 0.4886 0.0250  -0.0092 0.0658  560 LYS B CE  
3790 N NZ  . LYS B 221 ? 0.8881 0.4862 0.5114 0.0098  -0.0152 0.0594  560 LYS B NZ  
3791 N N   . SER B 222 ? 1.0519 0.6836 0.6376 0.1659  0.0036  0.0577  561 SER B N   
3792 C CA  . SER B 222 ? 1.0171 0.6312 0.5779 0.1978  0.0022  0.0545  561 SER B CA  
3793 C C   . SER B 222 ? 0.9636 0.5872 0.5294 0.2028  0.0047  0.0630  561 SER B C   
3794 O O   . SER B 222 ? 1.0022 0.5921 0.5468 0.2136  0.0005  0.0620  561 SER B O   
3795 C CB  . SER B 222 ? 1.0949 0.7532 0.6652 0.2180  0.0079  0.0448  561 SER B CB  
3796 O OG  . SER B 222 ? 1.4674 1.1106 1.0122 0.2502  0.0062  0.0401  561 SER B OG  
3797 N N   . ASN B 223 ? 0.7663 0.4382 0.3615 0.1939  0.0114  0.0701  562 ASN B N   
3798 C CA  . ASN B 223 ? 0.7425 0.4280 0.3483 0.1932  0.0139  0.0782  562 ASN B CA  
3799 C C   . ASN B 223 ? 0.7384 0.4064 0.3508 0.1648  0.0106  0.0879  562 ASN B C   
3800 O O   . ASN B 223 ? 0.7745 0.4598 0.4038 0.1442  0.0121  0.0904  562 ASN B O   
3801 C CB  . ASN B 223 ? 0.6614 0.4106 0.2963 0.1981  0.0225  0.0793  562 ASN B CB  
3802 C CG  . ASN B 223 ? 0.6732 0.4382 0.3192 0.1985  0.0249  0.0870  562 ASN B CG  
3803 O OD1 . ASN B 223 ? 0.6846 0.4163 0.3121 0.2055  0.0211  0.0899  562 ASN B OD1 
3804 N ND2 . ASN B 223 ? 0.5963 0.4116 0.2721 0.1902  0.0309  0.0898  562 ASN B ND2 
3805 N N   . GLY B 224 ? 0.6896 0.3262 0.2886 0.1635  0.0062  0.0934  563 GLY B N   
3806 C CA  . GLY B 224 ? 0.7258 0.3432 0.3278 0.1364  0.0018  0.1028  563 GLY B CA  
3807 C C   . GLY B 224 ? 0.6472 0.3095 0.2811 0.1166  0.0068  0.1107  563 GLY B C   
3808 O O   . GLY B 224 ? 0.6476 0.3020 0.2868 0.0925  0.0037  0.1178  563 GLY B O   
3809 N N   . LEU B 225 ? 0.6357 0.3476 0.2915 0.1260  0.0144  0.1091  564 LEU B N   
3810 C CA  . LEU B 225 ? 0.6105 0.3666 0.2964 0.1097  0.0189  0.1148  564 LEU B CA  
3811 C C   . LEU B 225 ? 0.5450 0.3449 0.2502 0.1141  0.0251  0.1074  564 LEU B C   
3812 O O   . LEU B 225 ? 0.6118 0.4105 0.3078 0.1294  0.0261  0.0992  564 LEU B O   
3813 C CB  . LEU B 225 ? 0.5553 0.3279 0.2501 0.1134  0.0205  0.1221  564 LEU B CB  
3814 C CG  . LEU B 225 ? 0.5954 0.3305 0.2745 0.1063  0.0143  0.1312  564 LEU B CG  
3815 C CD1 . LEU B 225 ? 0.5884 0.3451 0.2774 0.1119  0.0165  0.1378  564 LEU B CD1 
3816 C CD2 . LEU B 225 ? 0.6027 0.3282 0.2866 0.0784  0.0104  0.1378  564 LEU B CD2 
3817 N N   . GLY B 226 ? 0.5118 0.3512 0.2440 0.1000  0.0286  0.1098  565 GLY B N   
3818 C CA  . GLY B 226 ? 0.5246 0.4066 0.2781 0.1005  0.0335  0.1027  565 GLY B CA  
3819 C C   . GLY B 226 ? 0.5700 0.4512 0.3262 0.0877  0.0330  0.0983  565 GLY B C   
3820 O O   . GLY B 226 ? 0.6382 0.4837 0.3759 0.0825  0.0291  0.0989  565 GLY B O   
3821 N N   . ASP B 227 ? 0.5415 0.4616 0.3211 0.0817  0.0362  0.0930  566 ASP B N   
3822 C CA  . ASP B 227 ? 0.5073 0.4330 0.2925 0.0708  0.0361  0.0876  566 ASP B CA  
3823 C C   . ASP B 227 ? 0.5295 0.4622 0.3106 0.0835  0.0378  0.0788  566 ASP B C   
3824 O O   . ASP B 227 ? 0.5576 0.5038 0.3396 0.0989  0.0397  0.0763  566 ASP B O   
3825 C CB  . ASP B 227 ? 0.5085 0.4684 0.3207 0.0558  0.0370  0.0859  566 ASP B CB  
3826 C CG  . ASP B 227 ? 0.5057 0.4624 0.3221 0.0420  0.0350  0.0935  566 ASP B CG  
3827 O OD1 . ASP B 227 ? 0.5714 0.4987 0.3714 0.0377  0.0323  0.1005  566 ASP B OD1 
3828 O OD2 . ASP B 227 ? 0.4679 0.4494 0.3027 0.0351  0.0354  0.0920  566 ASP B OD2 
3829 N N   . GLN B 228 ? 0.5188 0.4449 0.2963 0.0766  0.0369  0.0742  567 GLN B N   
3830 C CA  . GLN B 228 ? 0.4834 0.4182 0.2584 0.0859  0.0380  0.0655  567 GLN B CA  
3831 C C   . GLN B 228 ? 0.4413 0.4001 0.2366 0.0707  0.0383  0.0605  567 GLN B C   
3832 O O   . GLN B 228 ? 0.4461 0.3926 0.2385 0.0581  0.0368  0.0615  567 GLN B O   
3833 C CB  . GLN B 228 ? 0.5308 0.4255 0.2778 0.0945  0.0346  0.0623  567 GLN B CB  
3834 C CG  . GLN B 228 ? 0.5347 0.4394 0.2761 0.1092  0.0357  0.0533  567 GLN B CG  
3835 C CD  . GLN B 228 ? 0.6232 0.4878 0.3421 0.1169  0.0307  0.0471  567 GLN B CD  
3836 O OE1 . GLN B 228 ? 0.6359 0.4652 0.3453 0.1058  0.0260  0.0487  567 GLN B OE1 
3837 N NE2 . GLN B 228 ? 0.6639 0.5345 0.3730 0.1358  0.0314  0.0400  567 GLN B NE2 
3838 N N   . LEU B 229 ? 0.4046 0.3958 0.2198 0.0711  0.0395  0.0554  568 LEU B N   
3839 C CA  . LEU B 229 ? 0.3771 0.3863 0.2099 0.0569  0.0386  0.0506  568 LEU B CA  
3840 C C   . LEU B 229 ? 0.3627 0.3674 0.1883 0.0586  0.0381  0.0444  568 LEU B C   
3841 O O   . LEU B 229 ? 0.3600 0.3655 0.1777 0.0718  0.0387  0.0412  568 LEU B O   
3842 C CB  . LEU B 229 ? 0.3394 0.3763 0.1926 0.0543  0.0384  0.0483  568 LEU B CB  
3843 C CG  . LEU B 229 ? 0.4137 0.4574 0.2757 0.0522  0.0385  0.0528  568 LEU B CG  
3844 C CD1 . LEU B 229 ? 0.4250 0.4912 0.3040 0.0484  0.0374  0.0497  568 LEU B CD1 
3845 C CD2 . LEU B 229 ? 0.3854 0.4186 0.2480 0.0405  0.0374  0.0558  568 LEU B CD2 
3846 N N   . LEU B 230 ? 0.3825 0.3844 0.2112 0.0458  0.0368  0.0426  569 LEU B N   
3847 C CA  . LEU B 230 ? 0.3732 0.3705 0.1952 0.0462  0.0362  0.0367  569 LEU B CA  
3848 C C   . LEU B 230 ? 0.3728 0.3935 0.2080 0.0477  0.0361  0.0315  569 LEU B C   
3849 O O   . LEU B 230 ? 0.3611 0.3816 0.1890 0.0560  0.0362  0.0272  569 LEU B O   
3850 C CB  . LEU B 230 ? 0.3240 0.3167 0.1484 0.0319  0.0346  0.0363  569 LEU B CB  
3851 C CG  . LEU B 230 ? 0.3431 0.3280 0.1586 0.0312  0.0337  0.0306  569 LEU B CG  
3852 C CD1 . LEU B 230 ? 0.3091 0.2647 0.0976 0.0436  0.0335  0.0289  569 LEU B CD1 
3853 C CD2 . LEU B 230 ? 0.3267 0.3089 0.1449 0.0176  0.0322  0.0313  569 LEU B CD2 
3854 N N   . ALA B 231 ? 0.3799 0.4182 0.2328 0.0396  0.0355  0.0320  570 ALA B N   
3855 C CA  . ALA B 231 ? 0.3276 0.3838 0.1906 0.0388  0.0349  0.0287  570 ALA B CA  
3856 C C   . ALA B 231 ? 0.3444 0.4118 0.2044 0.0535  0.0360  0.0286  570 ALA B C   
3857 O O   . ALA B 231 ? 0.3386 0.4191 0.2017 0.0558  0.0355  0.0257  570 ALA B O   
3858 C CB  . ALA B 231 ? 0.3253 0.3907 0.2019 0.0295  0.0335  0.0297  570 ALA B CB  
3859 N N   . SER B 232 ? 0.3273 0.3905 0.1810 0.0644  0.0374  0.0322  571 SER B N   
3860 C CA  . SER B 232 ? 0.3720 0.4464 0.2221 0.0811  0.0382  0.0323  571 SER B CA  
3861 C C   . SER B 232 ? 0.3913 0.4488 0.2213 0.0961  0.0386  0.0290  571 SER B C   
3862 O O   . SER B 232 ? 0.4023 0.4725 0.2304 0.1097  0.0385  0.0268  571 SER B O   
3863 C CB  . SER B 232 ? 0.3333 0.4087 0.1832 0.0886  0.0394  0.0375  571 SER B CB  
3864 O OG  . SER B 232 ? 0.4378 0.4850 0.2706 0.0930  0.0404  0.0407  571 SER B OG  
3865 N N   . THR B 233 ? 0.4047 0.4328 0.2182 0.0943  0.0385  0.0284  572 THR B N   
3866 C CA  . THR B 233 ? 0.4238 0.4278 0.2131 0.1089  0.0377  0.0240  572 THR B CA  
3867 C C   . THR B 233 ? 0.4140 0.4324 0.2088 0.1085  0.0367  0.0174  572 THR B C   
3868 O O   . THR B 233 ? 0.4846 0.4962 0.2654 0.1248  0.0358  0.0128  572 THR B O   
3869 C CB  . THR B 233 ? 0.4146 0.3795 0.1824 0.1037  0.0365  0.0253  572 THR B CB  
3870 O OG1 . THR B 233 ? 0.5325 0.5029 0.3116 0.0854  0.0359  0.0238  572 THR B OG1 
3871 C CG2 . THR B 233 ? 0.4227 0.3742 0.1863 0.1015  0.0371  0.0337  572 THR B CG2 
3872 N N   . VAL B 234 ? 0.3944 0.4310 0.2080 0.0909  0.0363  0.0170  573 VAL B N   
3873 C CA  . VAL B 234 ? 0.3608 0.4108 0.1795 0.0891  0.0354  0.0120  573 VAL B CA  
3874 C C   . VAL B 234 ? 0.3829 0.4595 0.2091 0.1006  0.0354  0.0118  573 VAL B C   
3875 O O   . VAL B 234 ? 0.4145 0.4978 0.2367 0.1088  0.0345  0.0075  573 VAL B O   
3876 C CB  . VAL B 234 ? 0.4010 0.4604 0.2353 0.0684  0.0347  0.0125  573 VAL B CB  
3877 C CG1 . VAL B 234 ? 0.3397 0.4201 0.1918 0.0606  0.0346  0.0165  573 VAL B CG1 
3878 C CG2 . VAL B 234 ? 0.4228 0.4885 0.2576 0.0661  0.0337  0.0078  573 VAL B CG2 
3879 N N   . ASN B 235 ? 0.3728 0.4667 0.2099 0.1014  0.0360  0.0164  574 ASN B N   
3880 C CA  . ASN B 235 ? 0.3880 0.5101 0.2320 0.1128  0.0355  0.0171  574 ASN B CA  
3881 C C   . ASN B 235 ? 0.4687 0.5810 0.2941 0.1374  0.0353  0.0143  574 ASN B C   
3882 O O   . ASN B 235 ? 0.4722 0.6010 0.2973 0.1480  0.0341  0.0115  574 ASN B O   
3883 C CB  . ASN B 235 ? 0.3952 0.5347 0.2522 0.1095  0.0357  0.0224  574 ASN B CB  
3884 C CG  . ASN B 235 ? 0.3701 0.5144 0.2419 0.0873  0.0350  0.0242  574 ASN B CG  
3885 O OD1 . ASN B 235 ? 0.3712 0.5197 0.2482 0.0760  0.0338  0.0223  574 ASN B OD1 
3886 N ND2 . ASN B 235 ? 0.3741 0.5158 0.2510 0.0822  0.0352  0.0279  574 ASN B ND2 
3887 N N   . GLN B 236 ? 0.4605 0.5436 0.2682 0.1477  0.0361  0.0152  575 GLN B N   
3888 C CA  . GLN B 236 ? 0.4881 0.5514 0.2717 0.1727  0.0349  0.0120  575 GLN B CA  
3889 C C   . GLN B 236 ? 0.4984 0.5450 0.2684 0.1763  0.0329  0.0045  575 GLN B C   
3890 O O   . GLN B 236 ? 0.5379 0.5866 0.2974 0.1954  0.0308  0.0006  575 GLN B O   
3891 C CB  . GLN B 236 ? 0.5710 0.5963 0.3329 0.1800  0.0356  0.0146  575 GLN B CB  
3892 C CG  . GLN B 236 ? 0.7760 0.8143 0.5525 0.1714  0.0378  0.0222  575 GLN B CG  
3893 C CD  . GLN B 236 ? 0.8340 0.8327 0.5876 0.1762  0.0384  0.0259  575 GLN B CD  
3894 O OE1 . GLN B 236 ? 0.9518 0.9099 0.6744 0.1890  0.0364  0.0229  575 GLN B OE1 
3895 N NE2 . GLN B 236 ? 0.7234 0.7308 0.4904 0.1649  0.0401  0.0327  575 GLN B NE2 
3896 N N   . VAL B 237 ? 0.4257 0.4569 0.1958 0.1587  0.0330  0.0025  576 VAL B N   
3897 C CA  . VAL B 237 ? 0.4180 0.4302 0.1740 0.1611  0.0308  -0.0050 576 VAL B CA  
3898 C C   . VAL B 237 ? 0.4880 0.5350 0.2595 0.1613  0.0302  -0.0075 576 VAL B C   
3899 O O   . VAL B 237 ? 0.5114 0.5505 0.2701 0.1737  0.0279  -0.0137 576 VAL B O   
3900 C CB  . VAL B 237 ? 0.4113 0.4016 0.1647 0.1414  0.0307  -0.0058 576 VAL B CB  
3901 C CG1 . VAL B 237 ? 0.4083 0.3869 0.1526 0.1407  0.0282  -0.0136 576 VAL B CG1 
3902 C CG2 . VAL B 237 ? 0.4067 0.3564 0.1377 0.1428  0.0301  -0.0034 576 VAL B CG2 
3903 N N   . LEU B 238 ? 0.4425 0.5256 0.2393 0.1476  0.0317  -0.0028 577 LEU B N   
3904 C CA  . LEU B 238 ? 0.4011 0.5155 0.2113 0.1448  0.0310  -0.0040 577 LEU B CA  
3905 C C   . LEU B 238 ? 0.5073 0.6554 0.3255 0.1588  0.0303  -0.0013 577 LEU B C   
3906 O O   . LEU B 238 ? 0.5161 0.6938 0.3454 0.1570  0.0294  -0.0013 577 LEU B O   
3907 C CB  . LEU B 238 ? 0.4021 0.5295 0.2310 0.1197  0.0318  -0.0009 577 LEU B CB  
3908 C CG  . LEU B 238 ? 0.4351 0.5355 0.2580 0.1057  0.0319  -0.0034 577 LEU B CG  
3909 C CD1 . LEU B 238 ? 0.4404 0.5524 0.2794 0.0842  0.0320  -0.0004 577 LEU B CD1 
3910 C CD2 . LEU B 238 ? 0.4174 0.5017 0.2248 0.1145  0.0305  -0.0106 577 LEU B CD2 
3911 N N   . GLU B 239 ? 0.5697 0.5649 0.3563 0.1114  -0.0128 0.0214  578 GLU B N   
3912 C CA  . GLU B 239 ? 0.5128 0.5447 0.3036 0.1153  -0.0134 0.0270  578 GLU B CA  
3913 C C   . GLU B 239 ? 0.5003 0.5469 0.2922 0.1395  -0.0031 0.0279  578 GLU B C   
3914 O O   . GLU B 239 ? 0.5473 0.5696 0.3328 0.1600  0.0064  0.0272  578 GLU B O   
3915 C CB  . GLU B 239 ? 0.5401 0.5856 0.3362 0.1231  -0.0140 0.0353  578 GLU B CB  
3916 C CG  . GLU B 239 ? 0.5633 0.6053 0.3653 0.1533  -0.0015 0.0446  578 GLU B CG  
3917 C CD  . GLU B 239 ? 0.6343 0.7031 0.4448 0.1613  -0.0006 0.0553  578 GLU B CD  
3918 O OE1 . GLU B 239 ? 0.6652 0.7642 0.4760 0.1475  -0.0102 0.0546  578 GLU B OE1 
3919 O OE2 . GLU B 239 ? 0.7113 0.7716 0.5272 0.1797  0.0103  0.0648  578 GLU B OE2 
3920 N N   . GLY B 240 ? 0.5363 0.6222 0.3333 0.1378  -0.0038 0.0296  579 GLY B N   
3921 C CA  . GLY B 240 ? 0.5426 0.6508 0.3406 0.1650  0.0078  0.0313  579 GLY B CA  
3922 C C   . GLY B 240 ? 0.5904 0.6789 0.3780 0.1677  0.0150  0.0157  579 GLY B C   
3923 O O   . GLY B 240 ? 0.6302 0.7079 0.4159 0.1433  0.0077  0.0068  579 GLY B O   
3924 N N   . ASP B 241 ? 0.5667 0.6473 0.3667 0.1917  0.0310  0.0103  580 ASP B N   
3925 C CA  . ASP B 241 ? 0.6065 0.6715 0.4108 0.1915  0.0401  -0.0118 580 ASP B CA  
3926 C C   . ASP B 241 ? 0.5814 0.5923 0.3922 0.1935  0.0467  -0.0211 580 ASP B C   
3927 O O   . ASP B 241 ? 0.5586 0.5448 0.3742 0.2001  0.0474  -0.0073 580 ASP B O   
3928 C CB  . ASP B 241 ? 0.6248 0.7149 0.4465 0.2136  0.0548  -0.0173 580 ASP B CB  
3929 C CG  . ASP B 241 ? 0.6049 0.7572 0.4245 0.2128  0.0493  -0.0050 580 ASP B CG  
3930 O OD1 . ASP B 241 ? 0.6267 0.8021 0.4323 0.1877  0.0361  -0.0044 580 ASP B OD1 
3931 O OD2 . ASP B 241 ? 0.6643 0.8428 0.5000 0.2363  0.0580  0.0062  580 ASP B OD2 
3932 N N   . ASN B 242 ? 0.6110 0.6091 0.4232 0.1859  0.0512  -0.0448 581 ASN B N   
3933 C CA  . ASN B 242 ? 0.6136 0.5676 0.4378 0.1793  0.0559  -0.0566 581 ASN B CA  
3934 C C   . ASN B 242 ? 0.5992 0.5365 0.4062 0.1659  0.0446  -0.0499 581 ASN B C   
3935 O O   . ASN B 242 ? 0.6212 0.5250 0.4387 0.1660  0.0484  -0.0469 581 ASN B O   
3936 C CB  . ASN B 242 ? 0.5046 0.4281 0.3571 0.1950  0.0698  -0.0485 581 ASN B CB  
3937 C CG  . ASN B 242 ? 0.6074 0.5425 0.4791 0.2087  0.0820  -0.0556 581 ASN B CG  
3938 O OD1 . ASN B 242 ? 0.6503 0.6108 0.5239 0.2257  0.0838  -0.0377 581 ASN B OD1 
3939 N ND2 . ASN B 242 ? 0.6842 0.6044 0.5704 0.2016  0.0906  -0.0832 581 ASN B ND2 
3940 N N   . VAL B 243 ? 0.5603 0.5218 0.3457 0.1509  0.0304  -0.0445 582 VAL B N   
3941 C CA  . VAL B 243 ? 0.5679 0.5145 0.3419 0.1365  0.0190  -0.0361 582 VAL B CA  
3942 C C   . VAL B 243 ? 0.5701 0.5033 0.3499 0.1249  0.0196  -0.0519 582 VAL B C   
3943 O O   . VAL B 243 ? 0.4916 0.4062 0.2676 0.1201  0.0155  -0.0467 582 VAL B O   
3944 C CB  . VAL B 243 ? 0.5694 0.5414 0.3406 0.1172  0.0051  -0.0241 582 VAL B CB  
3945 C CG1 . VAL B 243 ? 0.5105 0.4662 0.2825 0.1023  -0.0032 -0.0176 582 VAL B CG1 
3946 C CG2 . VAL B 243 ? 0.5593 0.5480 0.3321 0.1224  0.0028  -0.0101 582 VAL B CG2 
3947 N N   . ARG B 244 ? 0.6047 0.5524 0.3941 0.1199  0.0248  -0.0720 583 ARG B N   
3948 C CA  . ARG B 244 ? 0.5072 0.4508 0.3028 0.1068  0.0255  -0.0900 583 ARG B CA  
3949 C C   . ARG B 244 ? 0.5111 0.4155 0.3201 0.1125  0.0340  -0.0947 583 ARG B C   
3950 O O   . ARG B 244 ? 0.4900 0.3845 0.2945 0.1055  0.0291  -0.0917 583 ARG B O   
3951 C CB  . ARG B 244 ? 0.5443 0.5099 0.3478 0.1013  0.0318  -0.1132 583 ARG B CB  
3952 C CG  . ARG B 244 ? 0.6261 0.5900 0.4352 0.0870  0.0338  -0.1356 583 ARG B CG  
3953 C CD  . ARG B 244 ? 0.6514 0.6363 0.4626 0.0820  0.0395  -0.1570 583 ARG B CD  
3954 N NE  . ARG B 244 ? 0.7176 0.7110 0.5271 0.0670  0.0362  -0.1741 583 ARG B NE  
3955 C CZ  . ARG B 244 ? 0.7144 0.7337 0.5218 0.0614  0.0361  -0.1910 583 ARG B CZ  
3956 N NH1 . ARG B 244 ? 0.7846 0.8219 0.5908 0.0692  0.0409  -0.1942 583 ARG B NH1 
3957 N NH2 . ARG B 244 ? 0.6945 0.7284 0.5028 0.0486  0.0305  -0.2054 583 ARG B NH2 
3958 N N   . GLU B 245 ? 0.5141 0.3968 0.3440 0.1250  0.0479  -0.0991 584 GLU B N   
3959 C CA  . GLU B 245 ? 0.5082 0.3520 0.3601 0.1277  0.0579  -0.0978 584 GLU B CA  
3960 C C   . GLU B 245 ? 0.4987 0.3303 0.3411 0.1330  0.0525  -0.0699 584 GLU B C   
3961 O O   . GLU B 245 ? 0.4798 0.2937 0.3266 0.1267  0.0532  -0.0689 584 GLU B O   
3962 C CB  . GLU B 245 ? 0.5284 0.3541 0.4092 0.1409  0.0731  -0.0978 584 GLU B CB  
3963 C CG  . GLU B 245 ? 0.6151 0.4442 0.5116 0.1361  0.0820  -0.1307 584 GLU B CG  
3964 C CD  . GLU B 245 ? 0.7196 0.5893 0.5958 0.1364  0.0772  -0.1376 584 GLU B CD  
3965 O OE1 . GLU B 245 ? 0.6851 0.5736 0.5487 0.1491  0.0722  -0.1158 584 GLU B OE1 
3966 O OE2 . GLU B 245 ? 0.8244 0.7093 0.6956 0.1229  0.0786  -0.1631 584 GLU B OE2 
3967 N N   . LYS B 246 ? 0.5014 0.3453 0.3301 0.1448  0.0475  -0.0486 585 LYS B N   
3968 C CA  . LYS B 246 ? 0.4325 0.2694 0.2521 0.1503  0.0426  -0.0243 585 LYS B CA  
3969 C C   . LYS B 246 ? 0.4697 0.3118 0.2710 0.1364  0.0304  -0.0253 585 LYS B C   
3970 O O   . LYS B 246 ? 0.5199 0.3496 0.3233 0.1369  0.0305  -0.0138 585 LYS B O   
3971 C CB  . LYS B 246 ? 0.4470 0.3041 0.2535 0.1624  0.0376  -0.0071 585 LYS B CB  
3972 C CG  . LYS B 246 ? 0.5250 0.3861 0.3527 0.1770  0.0490  0.0010  585 LYS B CG  
3973 C CD  . LYS B 246 ? 0.5041 0.3922 0.3192 0.1902  0.0435  0.0205  585 LYS B CD  
3974 C CE  . LYS B 246 ? 0.4710 0.3905 0.2657 0.1802  0.0313  0.0127  585 LYS B CE  
3975 N NZ  . LYS B 246 ? 0.4771 0.4290 0.2632 0.1860  0.0241  0.0295  585 LYS B NZ  
3976 N N   . LEU B 247 ? 0.4599 0.3236 0.2443 0.1254  0.0209  -0.0364 586 LEU B N   
3977 C CA  . LEU B 247 ? 0.4226 0.2927 0.1913 0.1149  0.0105  -0.0346 586 LEU B CA  
3978 C C   . LEU B 247 ? 0.4488 0.3134 0.2327 0.1066  0.0145  -0.0465 586 LEU B C   
3979 O O   . LEU B 247 ? 0.4423 0.3028 0.2244 0.1052  0.0114  -0.0369 586 LEU B O   
3980 C CB  . LEU B 247 ? 0.4040 0.3064 0.1727 0.1004  0.0005  -0.0355 586 LEU B CB  
3981 C CG  . LEU B 247 ? 0.3857 0.2998 0.1561 0.0887  -0.0080 -0.0276 586 LEU B CG  
3982 C CD1 . LEU B 247 ? 0.3581 0.2549 0.1296 0.0937  -0.0105 -0.0120 586 LEU B CD1 
3983 C CD2 . LEU B 247 ? 0.4464 0.3871 0.2211 0.0758  -0.0125 -0.0247 586 LEU B CD2 
3984 N N   . ARG B 248 ? 0.4339 0.3008 0.2335 0.1004  0.0216  -0.0692 587 ARG B N   
3985 C CA  . ARG B 248 ? 0.4090 0.2737 0.2258 0.0880  0.0252  -0.0846 587 ARG B CA  
3986 C C   . ARG B 248 ? 0.4631 0.2991 0.3001 0.0917  0.0337  -0.0703 587 ARG B C   
3987 O O   . ARG B 248 ? 0.5281 0.3690 0.3725 0.0825  0.0321  -0.0688 587 ARG B O   
3988 C CB  . ARG B 248 ? 0.4659 0.3330 0.2969 0.0804  0.0330  -0.1159 587 ARG B CB  
3989 C CG  . ARG B 248 ? 0.5158 0.4231 0.3274 0.0738  0.0245  -0.1322 587 ARG B CG  
3990 C CD  . ARG B 248 ? 0.5498 0.4655 0.3775 0.0611  0.0320  -0.1652 587 ARG B CD  
3991 N NE  . ARG B 248 ? 0.7301 0.6117 0.5769 0.0705  0.0476  -0.1745 587 ARG B NE  
3992 C CZ  . ARG B 248 ? 0.9009 0.7441 0.7724 0.0687  0.0597  -0.1890 587 ARG B CZ  
3993 N NH1 . ARG B 248 ? 0.8170 0.6566 0.7028 0.0522  0.0587  -0.1997 587 ARG B NH1 
3994 N NH2 . ARG B 248 ? 0.9026 0.7143 0.7885 0.0830  0.0719  -0.1891 587 ARG B NH2 
3995 N N   . GLY B 249 ? 0.4243 0.2358 0.2715 0.1060  0.0435  -0.0571 588 GLY B N   
3996 C CA  . GLY B 249 ? 0.4493 0.2381 0.3145 0.1118  0.0525  -0.0374 588 GLY B CA  
3997 C C   . GLY B 249 ? 0.4666 0.2666 0.3130 0.1182  0.0437  -0.0137 588 GLY B C   
3998 O O   . GLY B 249 ? 0.4774 0.2715 0.3356 0.1181  0.0484  -0.0003 588 GLY B O   
3999 N N   . PHE B 250 ? 0.4710 0.2873 0.2889 0.1232  0.0318  -0.0090 589 PHE B N   
4000 C CA  . PHE B 250 ? 0.4140 0.2368 0.2116 0.1298  0.0238  0.0087  589 PHE B CA  
4001 C C   . PHE B 250 ? 0.4540 0.2901 0.2444 0.1206  0.0166  0.0046  589 PHE B C   
4002 O O   . PHE B 250 ? 0.4902 0.3279 0.2742 0.1269  0.0153  0.0184  589 PHE B O   
4003 C CB  . PHE B 250 ? 0.4154 0.2464 0.1876 0.1356  0.0146  0.0128  589 PHE B CB  
4004 C CG  . PHE B 250 ? 0.4568 0.3043 0.2290 0.1298  0.0098  0.0162  589 PHE B CG  
4005 C CD1 . PHE B 250 ? 0.4414 0.2989 0.2260 0.1312  0.0154  0.0242  589 PHE B CD1 
4006 C CD2 . PHE B 250 ? 0.4222 0.2790 0.1975 0.1198  0.0011  0.0102  589 PHE B CD2 
4007 C CE1 . PHE B 250 ? 0.4586 0.3274 0.2474 0.1274  0.0119  0.0222  589 PHE B CE1 
4008 C CE2 . PHE B 250 ? 0.4228 0.2869 0.2067 0.1154  -0.0006 0.0109  589 PHE B CE2 
4009 C CZ  . PHE B 250 ? 0.3580 0.2259 0.1453 0.1205  0.0043  0.0150  589 PHE B CZ  
4010 N N   . MET B 251 ? 0.4484 0.2992 0.2396 0.1078  0.0126  -0.0136 590 MET B N   
4011 C CA  . MET B 251 ? 0.4362 0.3086 0.2210 0.1011  0.0054  -0.0154 590 MET B CA  
4012 C C   . MET B 251 ? 0.3913 0.2659 0.1978 0.0974  0.0116  -0.0108 590 MET B C   
4013 O O   . MET B 251 ? 0.3861 0.2463 0.2186 0.0921  0.0223  -0.0147 590 MET B O   
4014 C CB  . MET B 251 ? 0.3563 0.2528 0.1403 0.0880  0.0008  -0.0360 590 MET B CB  
4015 C CG  . MET B 251 ? 0.3565 0.2601 0.1177 0.0907  -0.0060 -0.0362 590 MET B CG  
4016 S SD  . MET B 251 ? 0.4296 0.3436 0.1975 0.0902  -0.0143 -0.0126 590 MET B SD  
4017 C CE  . MET B 251 ? 0.3593 0.3034 0.1272 0.0858  -0.0179 -0.0137 590 MET B CE  
4018 N N   . ASP B 252 ? 0.3758 0.2687 0.1732 0.1006  0.0060  -0.0010 591 ASP B N   
4019 C CA  . ASP B 252 ? 0.4011 0.3054 0.2185 0.0976  0.0114  0.0064  591 ASP B CA  
4020 C C   . ASP B 252 ? 0.4152 0.3323 0.2623 0.0758  0.0158  -0.0135 591 ASP B C   
4021 O O   . ASP B 252 ? 0.4283 0.3709 0.2721 0.0646  0.0086  -0.0315 591 ASP B O   
4022 C CB  . ASP B 252 ? 0.4160 0.3458 0.2177 0.1062  0.0041  0.0177  591 ASP B CB  
4023 C CG  . ASP B 252 ? 0.3962 0.3432 0.2172 0.1069  0.0103  0.0298  591 ASP B CG  
4024 O OD1 . ASP B 252 ? 0.3926 0.3424 0.2443 0.0912  0.0181  0.0237  591 ASP B OD1 
4025 O OD2 . ASP B 252 ? 0.4347 0.3919 0.2411 0.1230  0.0084  0.0452  591 ASP B OD2 
4026 N N   . PRO B 253 ? 0.3940 0.2954 0.2706 0.0685  0.0277  -0.0114 592 PRO B N   
4027 C CA  . PRO B 253 ? 0.4212 0.3306 0.3285 0.0438  0.0325  -0.0342 592 PRO B CA  
4028 C C   . PRO B 253 ? 0.4441 0.4033 0.3562 0.0304  0.0241  -0.0412 592 PRO B C   
4029 O O   . PRO B 253 ? 0.4697 0.4500 0.3942 0.0096  0.0214  -0.0682 592 PRO B O   
4030 C CB  . PRO B 253 ? 0.4143 0.2940 0.3526 0.0413  0.0484  -0.0209 592 PRO B CB  
4031 C CG  . PRO B 253 ? 0.4070 0.2608 0.3276 0.0664  0.0519  0.0034  592 PRO B CG  
4032 C CD  . PRO B 253 ? 0.4030 0.2786 0.2868 0.0817  0.0382  0.0117  592 PRO B CD  
4033 N N   . ASN B 254 ? 0.4030 0.3858 0.3053 0.0430  0.0202  -0.0186 593 ASN B N   
4034 C CA  . ASN B 254 ? 0.4194 0.4568 0.3280 0.0339  0.0129  -0.0210 593 ASN B CA  
4035 C C   . ASN B 254 ? 0.4365 0.5068 0.3257 0.0307  0.0001  -0.0377 593 ASN B C   
4036 O O   . ASN B 254 ? 0.4492 0.5711 0.3494 0.0162  -0.0059 -0.0488 593 ASN B O   
4037 C CB  . ASN B 254 ? 0.4194 0.4737 0.3165 0.0553  0.0121  0.0081  593 ASN B CB  
4038 C CG  . ASN B 254 ? 0.4269 0.4646 0.3452 0.0573  0.0251  0.0266  593 ASN B CG  
4039 O OD1 . ASN B 254 ? 0.5287 0.5416 0.4302 0.0791  0.0291  0.0460  593 ASN B OD1 
4040 N ND2 . ASN B 254 ? 0.4106 0.4645 0.3664 0.0334  0.0320  0.0206  593 ASN B ND2 
4041 N N   . LEU B 255 ? 0.4672 0.5149 0.3285 0.0435  -0.0040 -0.0382 594 LEU B N   
4042 C CA  . LEU B 255 ? 0.4854 0.5647 0.3292 0.0402  -0.0142 -0.0519 594 LEU B CA  
4043 C C   . LEU B 255 ? 0.5214 0.6121 0.3819 0.0160  -0.0131 -0.0865 594 LEU B C   
4044 O O   . LEU B 255 ? 0.4920 0.6191 0.3392 0.0114  -0.0213 -0.1006 594 LEU B O   
4045 C CB  . LEU B 255 ? 0.4130 0.4641 0.2254 0.0582  -0.0174 -0.0412 594 LEU B CB  
4046 C CG  . LEU B 255 ? 0.4038 0.4436 0.1943 0.0816  -0.0199 -0.0126 594 LEU B CG  
4047 C CD1 . LEU B 255 ? 0.3660 0.3684 0.1322 0.0926  -0.0210 -0.0066 594 LEU B CD1 
4048 C CD2 . LEU B 255 ? 0.3977 0.4846 0.1783 0.0883  -0.0279 -0.0022 594 LEU B CD2 
4049 N N   . ARG B 256 ? 0.5162 0.5770 0.4053 0.0012  -0.0023 -0.1002 595 ARG B N   
4050 C CA  . ARG B 256 ? 0.5455 0.6040 0.4505 -0.0204 0.0013  -0.1370 595 ARG B CA  
4051 C C   . ARG B 256 ? 0.6149 0.6650 0.4941 -0.0105 -0.0017 -0.1472 595 ARG B C   
4052 O O   . ARG B 256 ? 0.7860 0.7962 0.6524 0.0074  0.0024  -0.1311 595 ARG B O   
4053 C CB  . ARG B 256 ? 0.5529 0.6731 0.4719 -0.0445 -0.0061 -0.1603 595 ARG B CB  
4054 C CG  . ARG B 256 ? 0.6558 0.7963 0.6019 -0.0556 -0.0040 -0.1479 595 ARG B CG  
4055 C CD  . ARG B 256 ? 0.7970 0.9816 0.7713 -0.0902 -0.0061 -0.1822 595 ARG B CD  
4056 N NE  . ARG B 256 ? 0.7950 1.0602 0.7538 -0.0936 -0.0217 -0.1905 595 ARG B NE  
4057 C CZ  . ARG B 256 ? 0.7726 1.1015 0.7401 -0.0975 -0.0292 -0.1775 595 ARG B CZ  
4058 N NH1 . ARG B 256 ? 0.7762 1.0992 0.7677 -0.0996 -0.0226 -0.1565 595 ARG B NH1 
4059 N NH2 . ARG B 256 ? 0.6619 1.0676 0.6142 -0.0979 -0.0430 -0.1837 595 ARG B NH2 
4060 N N   . ASP B 257 ? 0.5771 0.6713 0.4486 -0.0222 -0.0090 -0.1734 596 ASP B N   
4061 C CA  . ASP B 257 ? 0.5168 0.6176 0.3623 -0.0125 -0.0125 -0.1801 596 ASP B CA  
4062 C C   . ASP B 257 ? 0.4592 0.6182 0.2826 -0.0069 -0.0256 -0.1659 596 ASP B C   
4063 O O   . ASP B 257 ? 0.4758 0.6470 0.2950 -0.0053 -0.0273 -0.1639 596 ASP B O   
4064 C CB  . ASP B 257 ? 0.5862 0.6823 0.4428 -0.0277 -0.0060 -0.2221 596 ASP B CB  
4065 C CG  . ASP B 257 ? 0.6848 0.7132 0.5666 -0.0285 0.0099  -0.2290 596 ASP B CG  
4066 O OD1 . ASP B 257 ? 0.6287 0.6157 0.5076 -0.0103 0.0150  -0.1995 596 ASP B OD1 
4067 O OD2 . ASP B 257 ? 0.8417 0.8590 0.7466 -0.0471 0.0178  -0.2638 596 ASP B OD2 
4068 N N   . GLU B 258 ? 0.4118 0.5990 0.2310 -0.0016 -0.0322 -0.1450 597 GLU B N   
4069 C CA  . GLU B 258 ? 0.4190 0.6488 0.2338 0.0060  -0.0402 -0.1202 597 GLU B CA  
4070 C C   . GLU B 258 ? 0.4019 0.5978 0.1998 0.0278  -0.0400 -0.0833 597 GLU B C   
4071 O O   . GLU B 258 ? 0.3834 0.5822 0.1789 0.0402  -0.0420 -0.0576 597 GLU B O   
4072 C CB  . GLU B 258 ? 0.4163 0.6976 0.2428 -0.0001 -0.0455 -0.1178 597 GLU B CB  
4073 C CG  . GLU B 258 ? 0.4266 0.7426 0.2760 -0.0292 -0.0458 -0.1574 597 GLU B CG  
4074 C CD  . GLU B 258 ? 0.4985 0.8779 0.3626 -0.0377 -0.0523 -0.1529 597 GLU B CD  
4075 O OE1 . GLU B 258 ? 0.4645 0.8564 0.3201 -0.0166 -0.0551 -0.1172 597 GLU B OE1 
4076 O OE2 . GLU B 258 ? 0.5452 0.9596 0.4328 -0.0654 -0.0533 -0.1843 597 GLU B OE2 
4077 N N   . TYR B 259 ? 0.3834 0.5458 0.1734 0.0304  -0.0365 -0.0828 598 TYR B N   
4078 C CA  . TYR B 259 ? 0.3611 0.4924 0.1408 0.0425  -0.0358 -0.0545 598 TYR B CA  
4079 C C   . TYR B 259 ? 0.3646 0.4880 0.1411 0.0384  -0.0334 -0.0604 598 TYR B C   
4080 O O   . TYR B 259 ? 0.3888 0.5100 0.1687 0.0314  -0.0298 -0.0848 598 TYR B O   
4081 C CB  . TYR B 259 ? 0.3514 0.4373 0.1261 0.0526  -0.0323 -0.0426 598 TYR B CB  
4082 C CG  . TYR B 259 ? 0.4057 0.4601 0.1783 0.0519  -0.0265 -0.0597 598 TYR B CG  
4083 C CD1 . TYR B 259 ? 0.4010 0.4327 0.1718 0.0531  -0.0236 -0.0552 598 TYR B CD1 
4084 C CD2 . TYR B 259 ? 0.4529 0.5008 0.2300 0.0501  -0.0225 -0.0810 598 TYR B CD2 
4085 C CE1 . TYR B 259 ? 0.3765 0.3808 0.1480 0.0562  -0.0172 -0.0686 598 TYR B CE1 
4086 C CE2 . TYR B 259 ? 0.3828 0.3903 0.1725 0.0491  -0.0130 -0.0911 598 TYR B CE2 
4087 C CZ  . TYR B 259 ? 0.3670 0.3554 0.1431 0.0576  -0.0117 -0.0878 598 TYR B CZ  
4088 O OH  . TYR B 259 ? 0.3827 0.3364 0.1722 0.0601  -0.0017 -0.0949 598 TYR B OH  
4089 N N   . PRO B 260 ? 0.3620 0.4811 0.1336 0.0423  -0.0344 -0.0400 599 PRO B N   
4090 C CA  . PRO B 260 ? 0.3650 0.4801 0.1331 0.0391  -0.0319 -0.0430 599 PRO B CA  
4091 C C   . PRO B 260 ? 0.3563 0.4306 0.1223 0.0405  -0.0277 -0.0413 599 PRO B C   
4092 O O   . PRO B 260 ? 0.3775 0.4276 0.1432 0.0445  -0.0280 -0.0237 599 PRO B O   
4093 C CB  . PRO B 260 ? 0.3691 0.4955 0.1332 0.0424  -0.0344 -0.0205 599 PRO B CB  
4094 C CG  . PRO B 260 ? 0.3645 0.4736 0.1287 0.0490  -0.0360 -0.0026 599 PRO B CG  
4095 C CD  . PRO B 260 ? 0.3609 0.4807 0.1311 0.0500  -0.0368 -0.0148 599 PRO B CD  
4096 N N   . LEU B 261 ? 0.3184 0.4377 0.2033 0.0322  0.0905  -0.0321 600 LEU B N   
4097 C CA  . LEU B 261 ? 0.2924 0.4092 0.1874 0.0389  0.0930  -0.0300 600 LEU B CA  
4098 C C   . LEU B 261 ? 0.2931 0.4341 0.2073 0.0449  0.0873  -0.0212 600 LEU B C   
4099 O O   . LEU B 261 ? 0.3190 0.4678 0.2467 0.0488  0.0806  -0.0160 600 LEU B O   
4100 C CB  . LEU B 261 ? 0.2948 0.3927 0.1757 0.0414  0.1073  -0.0382 600 LEU B CB  
4101 C CG  . LEU B 261 ? 0.3534 0.4549 0.2453 0.0527  0.1079  -0.0367 600 LEU B CG  
4102 C CD1 . LEU B 261 ? 0.3739 0.4664 0.2668 0.0523  0.1013  -0.0351 600 LEU B CD1 
4103 C CD2 . LEU B 261 ? 0.4230 0.5114 0.3026 0.0574  0.1208  -0.0461 600 LEU B CD2 
4104 N N   . ASP B 262 ? 0.3054 0.4557 0.2179 0.0445  0.0917  -0.0202 601 ASP B N   
4105 C CA  . ASP B 262 ? 0.3175 0.4876 0.2459 0.0474  0.0904  -0.0133 601 ASP B CA  
4106 C C   . ASP B 262 ? 0.2806 0.4613 0.2192 0.0440  0.0779  -0.0059 601 ASP B C   
4107 O O   . ASP B 262 ? 0.2722 0.4647 0.2253 0.0461  0.0748  -0.0010 601 ASP B O   
4108 C CB  . ASP B 262 ? 0.3399 0.5120 0.2591 0.0446  0.1003  -0.0142 601 ASP B CB  
4109 C CG  . ASP B 262 ? 0.3388 0.5053 0.2404 0.0379  0.0962  -0.0140 601 ASP B CG  
4110 O OD1 . ASP B 262 ? 0.3669 0.5259 0.2614 0.0355  0.0897  -0.0173 601 ASP B OD1 
4111 O OD2 . ASP B 262 ? 0.3868 0.5563 0.2809 0.0351  0.1002  -0.0108 601 ASP B OD2 
4112 N N   . LEU B 263 ? 0.2976 0.4751 0.2286 0.0389  0.0714  -0.0058 602 LEU B N   
4113 C CA  . LEU B 263 ? 0.3024 0.4876 0.2422 0.0367  0.0612  0.0005  602 LEU B CA  
4114 C C   . LEU B 263 ? 0.2972 0.4776 0.2454 0.0381  0.0558  0.0007  602 LEU B C   
4115 O O   . LEU B 263 ? 0.2743 0.4600 0.2318 0.0381  0.0505  0.0063  602 LEU B O   
4116 C CB  . LEU B 263 ? 0.2690 0.4555 0.1996 0.0332  0.0564  -0.0001 602 LEU B CB  
4117 C CG  . LEU B 263 ? 0.2582 0.4462 0.1747 0.0322  0.0613  0.0015  602 LEU B CG  
4118 C CD1 . LEU B 263 ? 0.2257 0.4169 0.1310 0.0310  0.0547  0.0011  602 LEU B CD1 
4119 C CD2 . LEU B 263 ? 0.2555 0.4473 0.1768 0.0317  0.0651  0.0089  602 LEU B CD2 
4120 N N   . ALA B 264 ? 0.2831 0.4491 0.2243 0.0384  0.0592  -0.0059 603 ALA B N   
4121 C CA  . ALA B 264 ? 0.2750 0.4301 0.2185 0.0400  0.0576  -0.0062 603 ALA B CA  
4122 C C   . ALA B 264 ? 0.3166 0.4785 0.2683 0.0472  0.0573  -0.0020 603 ALA B C   
4123 O O   . ALA B 264 ? 0.3085 0.4704 0.2652 0.0482  0.0521  0.0017  603 ALA B O   
4124 C CB  . ALA B 264 ? 0.2457 0.3782 0.1747 0.0381  0.0659  -0.0148 603 ALA B CB  
4125 N N   . PHE B 265 ? 0.2705 0.4394 0.2235 0.0524  0.0636  -0.0032 604 PHE B N   
4126 C CA  . PHE B 265 ? 0.2889 0.4761 0.2540 0.0613  0.0630  0.0003  604 PHE B CA  
4127 C C   . PHE B 265 ? 0.3162 0.5214 0.2933 0.0563  0.0566  0.0070  604 PHE B C   
4128 O O   . PHE B 265 ? 0.2849 0.5025 0.2690 0.0602  0.0511  0.0106  604 PHE B O   
4129 C CB  . PHE B 265 ? 0.2785 0.4747 0.2463 0.0674  0.0730  -0.0030 604 PHE B CB  
4130 C CG  . PHE B 265 ? 0.2965 0.5222 0.2830 0.0758  0.0732  -0.0001 604 PHE B CG  
4131 C CD1 . PHE B 265 ? 0.3157 0.5528 0.3074 0.0906  0.0691  0.0008  604 PHE B CD1 
4132 C CD2 . PHE B 265 ? 0.3121 0.5544 0.3107 0.0693  0.0786  0.0009  604 PHE B CD2 
4133 C CE1 . PHE B 265 ? 0.3387 0.6087 0.3523 0.0982  0.0684  0.0017  604 PHE B CE1 
4134 C CE2 . PHE B 265 ? 0.3148 0.5869 0.3356 0.0740  0.0808  0.0014  604 PHE B CE2 
4135 C CZ  . PHE B 265 ? 0.3041 0.5928 0.3350 0.0882  0.0746  0.0013  604 PHE B CZ  
4136 N N   . SER B 266 ? 0.2738 0.4791 0.2501 0.0477  0.0583  0.0084  605 SER B N   
4137 C CA  . SER B 266 ? 0.2654 0.4808 0.2485 0.0416  0.0551  0.0141  605 SER B CA  
4138 C C   . SER B 266 ? 0.2792 0.4879 0.2619 0.0397  0.0462  0.0173  605 SER B C   
4139 O O   . SER B 266 ? 0.2474 0.4674 0.2372 0.0380  0.0435  0.0212  605 SER B O   
4140 C CB  . SER B 266 ? 0.2598 0.4723 0.2348 0.0356  0.0588  0.0158  605 SER B CB  
4141 O OG  . SER B 266 ? 0.3424 0.5581 0.3144 0.0367  0.0692  0.0124  605 SER B OG  
4142 N N   . MET B 267 ? 0.2543 0.4469 0.2290 0.0392  0.0432  0.0150  606 MET B N   
4143 C CA  . MET B 267 ? 0.2819 0.4651 0.2562 0.0370  0.0378  0.0168  606 MET B CA  
4144 C C   . MET B 267 ? 0.2913 0.4740 0.2660 0.0423  0.0366  0.0167  606 MET B C   
4145 O O   . MET B 267 ? 0.2543 0.4367 0.2300 0.0407  0.0332  0.0201  606 MET B O   
4146 C CB  . MET B 267 ? 0.2470 0.4194 0.2150 0.0351  0.0372  0.0130  606 MET B CB  
4147 C CG  . MET B 267 ? 0.2966 0.4626 0.2657 0.0318  0.0337  0.0153  606 MET B CG  
4148 S SD  . MET B 267 ? 0.3091 0.4737 0.2752 0.0294  0.0336  0.0102  606 MET B SD  
4149 C CE  . MET B 267 ? 0.2386 0.4199 0.2030 0.0308  0.0325  0.0120  606 MET B CE  
4150 N N   . ALA B 268 ? 0.2949 0.4778 0.2660 0.0505  0.0399  0.0132  607 ALA B N   
4151 C CA  . ALA B 268 ? 0.2799 0.4679 0.2482 0.0613  0.0382  0.0144  607 ALA B CA  
4152 C C   . ALA B 268 ? 0.3057 0.5278 0.2869 0.0657  0.0346  0.0188  607 ALA B C   
4153 O O   . ALA B 268 ? 0.2927 0.5263 0.2730 0.0720  0.0301  0.0213  607 ALA B O   
4154 C CB  . ALA B 268 ? 0.2568 0.4333 0.2144 0.0722  0.0439  0.0094  607 ALA B CB  
4155 N N   . GLU B 269 ? 0.2754 0.5138 0.2676 0.0613  0.0380  0.0187  608 GLU B N   
4156 C CA  . GLU B 269 ? 0.2622 0.5332 0.2709 0.0606  0.0375  0.0204  608 GLU B CA  
4157 C C   . GLU B 269 ? 0.2182 0.4931 0.2287 0.0492  0.0334  0.0249  608 GLU B C   
4158 O O   . GLU B 269 ? 0.2790 0.5777 0.2980 0.0505  0.0291  0.0257  608 GLU B O   
4159 C CB  . GLU B 269 ? 0.2582 0.5382 0.2775 0.0554  0.0461  0.0181  608 GLU B CB  
4160 C CG  . GLU B 269 ? 0.3060 0.6206 0.3492 0.0532  0.0487  0.0167  608 GLU B CG  
4161 C CD  . GLU B 269 ? 0.3922 0.7304 0.4497 0.0698  0.0461  0.0124  608 GLU B CD  
4162 O OE1 . GLU B 269 ? 0.3829 0.7075 0.4296 0.0830  0.0481  0.0104  608 GLU B OE1 
4163 O OE2 . GLU B 269 ? 0.4402 0.8097 0.5204 0.0700  0.0416  0.0104  608 GLU B OE2 
4164 N N   . ILE B 270 ? 0.2109 0.4633 0.2141 0.0387  0.0346  0.0270  609 ILE B N   
4165 C CA  . ILE B 270 ? 0.2285 0.4781 0.2309 0.0285  0.0329  0.0312  609 ILE B CA  
4166 C C   . ILE B 270 ? 0.2185 0.4602 0.2135 0.0320  0.0275  0.0325  609 ILE B C   
4167 O O   . ILE B 270 ? 0.2335 0.4865 0.2296 0.0261  0.0255  0.0353  609 ILE B O   
4168 C CB  . ILE B 270 ? 0.2462 0.4713 0.2408 0.0214  0.0363  0.0328  609 ILE B CB  
4169 C CG1 . ILE B 270 ? 0.2512 0.4710 0.2433 0.0110  0.0382  0.0371  609 ILE B CG1 
4170 C CG2 . ILE B 270 ? 0.2491 0.4501 0.2348 0.0257  0.0334  0.0305  609 ILE B CG2 
4171 C CD1 . ILE B 270 ? 0.2361 0.4811 0.2393 0.0019  0.0431  0.0379  609 ILE B CD1 
4172 N N   . ALA B 271 ? 0.2068 0.4266 0.1922 0.0395  0.0269  0.0296  610 ALA B N   
4173 C CA  . ALA B 271 ? 0.2089 0.4124 0.1825 0.0429  0.0251  0.0294  610 ALA B CA  
4174 C C   . ALA B 271 ? 0.2577 0.4888 0.2296 0.0540  0.0210  0.0305  610 ALA B C   
4175 O O   . ALA B 271 ? 0.2569 0.4786 0.2146 0.0524  0.0165  0.0323  610 ALA B O   
4176 C CB  . ALA B 271 ? 0.2029 0.3747 0.1649 0.0463  0.0284  0.0242  610 ALA B CB  
4177 N N   . LYS B 272 ? 0.2366 0.4971 0.2187 0.0659  0.0207  0.0285  611 LYS B N   
4178 C CA  . LYS B 272 ? 0.2320 0.5270 0.2218 0.0808  0.0136  0.0271  611 LYS B CA  
4179 C C   . LYS B 272 ? 0.1835 0.5033 0.1929 0.0653  0.0046  0.0284  611 LYS B C   
4180 O O   . LYS B 272 ? 0.1897 0.5020 0.1922 0.0662  -0.0113 0.0278  611 LYS B O   
4181 C CB  . LYS B 272 ? 0.2314 0.5434 0.2365 0.0933  0.0147  0.0225  611 LYS B CB  
4182 C CG  . LYS B 272 ? 0.2491 0.5842 0.2705 0.1079  0.0008  0.0187  611 LYS B CG  
4183 C CD  . LYS B 272 ? 0.2854 0.6344 0.3227 0.1175  0.0056  0.0137  611 LYS B CD  
4184 C CE  . LYS B 272 ? 0.3185 0.6881 0.3736 0.1330  -0.0095 0.0092  611 LYS B CE  
4185 N NZ  . LYS B 272 ? 0.4284 0.8163 0.5041 0.1432  -0.0034 0.0044  611 LYS B NZ  
4186 N N   . ARG B 273 ? 0.1860 0.5223 0.2113 0.0485  0.0138  0.0295  612 ARG B N   
4187 C CA  . ARG B 273 ? 0.1341 0.4948 0.1774 0.0305  0.0101  0.0296  612 ARG B CA  
4188 C C   . ARG B 273 ? 0.1584 0.4832 0.1753 0.0183  0.0058  0.0340  612 ARG B C   
4189 O O   . ARG B 273 ? 0.2257 0.5562 0.2468 0.0057  -0.0042 0.0321  612 ARG B O   
4190 C CB  . ARG B 273 ? 0.1307 0.4868 0.1805 0.0150  0.0216  0.0293  612 ARG B CB  
4191 C CG  . ARG B 273 ? 0.2044 0.5698 0.2682 0.0236  0.0264  0.0241  612 ARG B CG  
4192 C CD  . ARG B 273 ? 0.2031 0.5638 0.2727 0.0088  0.0384  0.0239  612 ARG B CD  
4193 N NE  . ARG B 273 ? 0.3302 0.6986 0.4119 0.0161  0.0456  0.0192  612 ARG B NE  
4194 C CZ  . ARG B 273 ? 0.3416 0.7094 0.4305 0.0064  0.0584  0.0178  612 ARG B CZ  
4195 N NH1 . ARG B 273 ? 0.3179 0.6753 0.4014 -0.0104 0.0656  0.0207  612 ARG B NH1 
4196 N NH2 . ARG B 273 ? 0.2680 0.6430 0.3674 0.0139  0.0662  0.0136  612 ARG B NH2 
4197 N N   . CYS B 274 ? 0.1519 0.4369 0.1404 0.0208  0.0134  0.0382  613 CYS B N   
4198 C CA  . CYS B 274 ? 0.2280 0.4732 0.1898 0.0105  0.0123  0.0418  613 CYS B CA  
4199 C C   . CYS B 274 ? 0.2339 0.4550 0.1759 0.0168  -0.0030 0.0392  613 CYS B C   
4200 O O   . CYS B 274 ? 0.2976 0.4953 0.2224 0.0051  -0.0080 0.0401  613 CYS B O   
4201 C CB  . CYS B 274 ? 0.2434 0.4427 0.2002 0.0124  0.0201  0.0404  613 CYS B CB  
4202 S SG  . CYS B 274 ? 0.2302 0.4258 0.2000 0.0052  0.0274  0.0413  613 CYS B SG  
4203 N N   . VAL B 275 ? 0.2464 0.4677 0.1853 0.0356  -0.0097 0.0360  614 VAL B N   
4204 C CA  . VAL B 275 ? 0.2032 0.3963 0.1160 0.0452  -0.0246 0.0344  614 VAL B CA  
4205 C C   . VAL B 275 ? 0.2448 0.4756 0.1788 0.0508  -0.0450 0.0302  614 VAL B C   
4206 O O   . VAL B 275 ? 0.2878 0.4985 0.2050 0.0649  -0.0591 0.0279  614 VAL B O   
4207 C CB  . VAL B 275 ? 0.2568 0.4120 0.1499 0.0614  -0.0181 0.0322  614 VAL B CB  
4208 C CG1 . VAL B 275 ? 0.2354 0.3594 0.1237 0.0514  0.0005  0.0318  614 VAL B CG1 
4209 C CG2 . VAL B 275 ? 0.2544 0.4439 0.1658 0.0801  -0.0187 0.0302  614 VAL B CG2 
4210 N N   . ALA B 276 ? 0.2620 0.5421 0.2347 0.0385  -0.0449 0.0278  615 ALA B N   
4211 C CA  . ALA B 276 ? 0.2222 0.5480 0.2237 0.0416  -0.0644 0.0214  615 ALA B CA  
4212 C C   . ALA B 276 ? 0.2718 0.5731 0.2492 0.0336  -0.0835 0.0192  615 ALA B C   
4213 O O   . ALA B 276 ? 0.2491 0.5259 0.2073 0.0122  -0.0792 0.0213  615 ALA B O   
4214 C CB  . ALA B 276 ? 0.1812 0.5621 0.2288 0.0238  -0.0560 0.0175  615 ALA B CB  
4215 N N   . ARG B 277 ? 0.2910 0.5909 0.2686 0.0498  -0.1023 0.0145  616 ARG B N   
4216 C CA  . ARG B 277 ? 0.3496 0.6224 0.3000 0.0437  -0.1228 0.0122  616 ARG B CA  
4217 C C   . ARG B 277 ? 0.3627 0.6665 0.3318 0.0146  -0.1279 0.0068  616 ARG B C   
4218 O O   . ARG B 277 ? 0.4636 0.7328 0.3980 0.0000  -0.1356 0.0066  616 ARG B O   
4219 C CB  . ARG B 277 ? 0.4884 0.7646 0.4422 0.0655  -0.1441 0.0088  616 ARG B CB  
4220 C CG  . ARG B 277 ? 0.6247 0.8904 0.5618 0.0570  -0.1694 0.0051  616 ARG B CG  
4221 C CD  . ARG B 277 ? 0.6747 0.9260 0.5975 0.0813  -0.1879 0.0066  616 ARG B CD  
4222 N NE  . ARG B 277 ? 0.8219 1.0050 0.6894 0.0936  -0.1791 0.0147  616 ARG B NE  
4223 C CZ  . ARG B 277 ? 0.7877 0.9195 0.6058 0.0861  -0.1841 0.0184  616 ARG B CZ  
4224 N NH1 . ARG B 277 ? 0.7432 0.8813 0.5544 0.0669  -0.2005 0.0155  616 ARG B NH1 
4225 N NH2 . ARG B 277 ? 0.7840 0.8574 0.5590 0.0969  -0.1697 0.0234  616 ARG B NH2 
4226 N N   . ASP B 278 ? 0.3427 0.7057 0.3627 0.0035  -0.1209 0.0017  617 ASP B N   
4227 C CA  . ASP B 278 ? 0.3209 0.7125 0.3608 -0.0286 -0.1208 -0.0046 617 ASP B CA  
4228 C C   . ASP B 278 ? 0.3003 0.6701 0.3251 -0.0506 -0.0959 0.0026  617 ASP B C   
4229 O O   . ASP B 278 ? 0.2793 0.6609 0.3219 -0.0472 -0.0752 0.0070  617 ASP B O   
4230 C CB  . ASP B 278 ? 0.2632 0.7172 0.3619 -0.0315 -0.1197 -0.0143 617 ASP B CB  
4231 C CG  . ASP B 278 ? 0.4903 0.9612 0.6047 -0.0119 -0.1451 -0.0215 617 ASP B CG  
4232 O OD1 . ASP B 278 ? 0.5535 0.9856 0.6301 0.0007  -0.1649 -0.0191 617 ASP B OD1 
4233 O OD2 . ASP B 278 ? 0.5895 1.1095 0.7516 -0.0093 -0.1447 -0.0289 617 ASP B OD2 
4234 N N   . LEU B 279 ? 0.2948 0.6184 0.2829 -0.0707 -0.0944 0.0039  618 LEU B N   
4235 C CA  . LEU B 279 ? 0.3023 0.5844 0.2691 -0.0856 -0.0678 0.0119  618 LEU B CA  
4236 C C   . LEU B 279 ? 0.3107 0.6295 0.3131 -0.1030 -0.0488 0.0107  618 LEU B C   
4237 O O   . LEU B 279 ? 0.3104 0.6109 0.3062 -0.1013 -0.0268 0.0191  618 LEU B O   
4238 C CB  . LEU B 279 ? 0.3048 0.5348 0.2292 -0.1055 -0.0690 0.0116  618 LEU B CB  
4239 C CG  . LEU B 279 ? 0.3789 0.6301 0.3136 -0.1350 -0.0793 0.0005  618 LEU B CG  
4240 C CD1 . LEU B 279 ? 0.3628 0.5515 0.2519 -0.1572 -0.0675 0.0028  618 LEU B CD1 
4241 C CD2 . LEU B 279 ? 0.3514 0.6318 0.2930 -0.1270 -0.1128 -0.0094 618 LEU B CD2 
4242 N N   . ASN B 280 ? 0.3388 0.7096 0.3782 -0.1202 -0.0568 -0.0004 619 ASN B N   
4243 C CA  . ASN B 280 ? 0.3570 0.7592 0.4272 -0.1402 -0.0355 -0.0027 619 ASN B CA  
4244 C C   . ASN B 280 ? 0.4078 0.8466 0.5096 -0.1205 -0.0246 0.0000  619 ASN B C   
4245 O O   . ASN B 280 ? 0.4177 0.8672 0.5328 -0.1334 -0.0019 0.0012  619 ASN B O   
4246 C CB  . ASN B 280 ? 0.3629 0.8145 0.4679 -0.1672 -0.0455 -0.0182 619 ASN B CB  
4247 C CG  . ASN B 280 ? 0.4400 0.8513 0.5100 -0.1931 -0.0520 -0.0222 619 ASN B CG  
4248 O OD1 . ASN B 280 ? 0.4866 0.8352 0.5129 -0.2029 -0.0348 -0.0132 619 ASN B OD1 
4249 N ND2 . ASN B 280 ? 0.4121 0.8513 0.4974 -0.1997 -0.0758 -0.0353 619 ASN B ND2 
4250 N N   . SER B 281 ? 0.3421 0.7937 0.4505 -0.0896 -0.0388 0.0009  620 SER B N   
4251 C CA  . SER B 281 ? 0.1794 0.6497 0.3070 -0.0690 -0.0262 0.0035  620 SER B CA  
4252 C C   . SER B 281 ? 0.2315 0.6585 0.3267 -0.0607 -0.0090 0.0158  620 SER B C   
4253 O O   . SER B 281 ? 0.2975 0.7278 0.3994 -0.0556 0.0082  0.0183  620 SER B O   
4254 C CB  . SER B 281 ? 0.2197 0.7022 0.3580 -0.0379 -0.0441 -0.0007 620 SER B CB  
4255 O OG  . SER B 281 ? 0.4667 0.9824 0.6353 -0.0412 -0.0587 -0.0122 620 SER B OG  
4256 N N   . ARG B 282 ? 0.2463 0.6188 0.2996 -0.0573 -0.0133 0.0221  621 ARG B N   
4257 C CA  . ARG B 282 ? 0.2396 0.5704 0.2641 -0.0502 0.0025  0.0319  621 ARG B CA  
4258 C C   . ARG B 282 ? 0.2496 0.5748 0.2723 -0.0690 0.0235  0.0364  621 ARG B C   
4259 O O   . ARG B 282 ? 0.2756 0.6019 0.3002 -0.0924 0.0266  0.0337  621 ARG B O   
4260 C CB  . ARG B 282 ? 0.2105 0.4867 0.1944 -0.0475 -0.0033 0.0360  621 ARG B CB  
4261 C CG  . ARG B 282 ? 0.1945 0.4647 0.1690 -0.0310 -0.0234 0.0320  621 ARG B CG  
4262 C CD  . ARG B 282 ? 0.2198 0.4361 0.1527 -0.0360 -0.0282 0.0341  621 ARG B CD  
4263 N NE  . ARG B 282 ? 0.2636 0.4760 0.1845 -0.0265 -0.0506 0.0292  621 ARG B NE  
4264 C CZ  . ARG B 282 ? 0.2725 0.4413 0.1556 -0.0316 -0.0588 0.0288  621 ARG B CZ  
4265 N NH1 . ARG B 282 ? 0.2835 0.4093 0.1396 -0.0459 -0.0451 0.0326  621 ARG B NH1 
4266 N NH2 . ARG B 282 ? 0.2976 0.4636 0.1667 -0.0207 -0.0813 0.0246  621 ARG B NH2 
4267 N N   . PRO B 283 ? 0.2061 0.5131 0.2203 -0.0579 0.0353  0.0414  622 PRO B N   
4268 C CA  . PRO B 283 ? 0.2658 0.5406 0.2702 -0.0664 0.0478  0.0430  622 PRO B CA  
4269 C C   . PRO B 283 ? 0.2803 0.5023 0.2535 -0.0708 0.0517  0.0485  622 PRO B C   
4270 O O   . PRO B 283 ? 0.2666 0.4690 0.2242 -0.0656 0.0451  0.0505  622 PRO B O   
4271 C CB  . PRO B 283 ? 0.2420 0.5059 0.2474 -0.0477 0.0509  0.0432  622 PRO B CB  
4272 C CG  . PRO B 283 ? 0.2221 0.4826 0.2226 -0.0306 0.0408  0.0437  622 PRO B CG  
4273 C CD  . PRO B 283 ? 0.2213 0.5177 0.2310 -0.0338 0.0321  0.0422  622 PRO B CD  
4274 N N   . ASN B 284 ? 0.2506 0.4452 0.2130 -0.0786 0.0640  0.0506  623 ASN B N   
4275 C CA  . ASN B 284 ? 0.2659 0.4072 0.1996 -0.0751 0.0700  0.0560  623 ASN B CA  
4276 C C   . ASN B 284 ? 0.3037 0.4214 0.2297 -0.0522 0.0688  0.0577  623 ASN B C   
4277 O O   . ASN B 284 ? 0.3250 0.4577 0.2618 -0.0434 0.0678  0.0558  623 ASN B O   
4278 C CB  . ASN B 284 ? 0.2957 0.4146 0.2176 -0.0863 0.0850  0.0592  623 ASN B CB  
4279 C CG  . ASN B 284 ? 0.3886 0.4598 0.2831 -0.0837 0.0906  0.0656  623 ASN B CG  
4280 O OD1 . ASN B 284 ? 0.4100 0.4543 0.2918 -0.0624 0.0927  0.0714  623 ASN B OD1 
4281 N ND2 . ASN B 284 ? 0.4228 0.4856 0.3089 -0.1061 0.0929  0.0633  623 ASN B ND2 
4282 N N   . VAL B 285 ? 0.2976 0.3792 0.2050 -0.0446 0.0691  0.0597  624 VAL B N   
4283 C CA  . VAL B 285 ? 0.2746 0.3399 0.1773 -0.0294 0.0667  0.0578  624 VAL B CA  
4284 C C   . VAL B 285 ? 0.3006 0.3576 0.1951 -0.0266 0.0731  0.0594  624 VAL B C   
4285 O O   . VAL B 285 ? 0.3226 0.3917 0.2249 -0.0177 0.0670  0.0573  624 VAL B O   
4286 C CB  . VAL B 285 ? 0.3522 0.3814 0.2356 -0.0259 0.0684  0.0577  624 VAL B CB  
4287 C CG1 . VAL B 285 ? 0.3774 0.3724 0.2404 -0.0274 0.0789  0.0626  624 VAL B CG1 
4288 C CG2 . VAL B 285 ? 0.2760 0.3085 0.1650 -0.0172 0.0616  0.0538  624 VAL B CG2 
4289 N N   . SER B 286 ? 0.3100 0.3463 0.1874 -0.0333 0.0862  0.0645  625 SER B N   
4290 C CA  . SER B 286 ? 0.3649 0.3876 0.2254 -0.0332 0.0933  0.0661  625 SER B CA  
4291 C C   . SER B 286 ? 0.3431 0.4004 0.2246 -0.0314 0.0908  0.0635  625 SER B C   
4292 O O   . SER B 286 ? 0.3375 0.3931 0.2104 -0.0265 0.0898  0.0636  625 SER B O   
4293 C CB  . SER B 286 ? 0.3781 0.3773 0.2271 -0.0332 0.1071  0.0744  625 SER B CB  
4294 O OG  . SER B 286 ? 0.3734 0.4069 0.2427 -0.0456 0.1142  0.0794  625 SER B OG  
4295 N N   . GLU B 287 ? 0.2750 0.3672 0.1830 -0.0371 0.0883  0.0610  626 GLU B N   
4296 C CA  . GLU B 287 ? 0.2572 0.3815 0.1844 -0.0351 0.0862  0.0570  626 GLU B CA  
4297 C C   . GLU B 287 ? 0.3070 0.4430 0.2437 -0.0214 0.0727  0.0535  626 GLU B C   
4298 O O   . GLU B 287 ? 0.3328 0.4737 0.2692 -0.0153 0.0727  0.0522  626 GLU B O   
4299 C CB  . GLU B 287 ? 0.2484 0.4114 0.2014 -0.0463 0.0855  0.0536  626 GLU B CB  
4300 C CG  . GLU B 287 ? 0.3716 0.5330 0.3232 -0.0638 0.0999  0.0554  626 GLU B CG  
4301 C CD  . GLU B 287 ? 0.4119 0.6186 0.3927 -0.0792 0.0957  0.0486  626 GLU B CD  
4302 O OE1 . GLU B 287 ? 0.3542 0.5838 0.3468 -0.0762 0.0813  0.0456  626 GLU B OE1 
4303 O OE2 . GLU B 287 ? 0.5352 0.7558 0.5272 -0.0944 0.1070  0.0457  626 GLU B OE2 
4304 N N   . VAL B 288 ? 0.2592 0.3973 0.2022 -0.0172 0.0628  0.0520  627 VAL B N   
4305 C CA  . VAL B 288 ? 0.2653 0.4097 0.2161 -0.0054 0.0530  0.0485  627 VAL B CA  
4306 C C   . VAL B 288 ? 0.2692 0.3982 0.2085 0.0013  0.0532  0.0500  627 VAL B C   
4307 O O   . VAL B 288 ? 0.2801 0.4207 0.2248 0.0085  0.0492  0.0478  627 VAL B O   
4308 C CB  . VAL B 288 ? 0.2459 0.3868 0.1996 -0.0038 0.0466  0.0469  627 VAL B CB  
4309 C CG1 . VAL B 288 ? 0.2169 0.3630 0.1782 0.0061  0.0398  0.0424  627 VAL B CG1 
4310 C CG2 . VAL B 288 ? 0.1969 0.3581 0.1582 -0.0113 0.0453  0.0471  627 VAL B CG2 
4311 N N   . PHE B 289 ? 0.3028 0.4078 0.2246 -0.0007 0.0574  0.0542  628 PHE B N   
4312 C CA  . PHE B 289 ? 0.2967 0.3952 0.2076 0.0075  0.0561  0.0575  628 PHE B CA  
4313 C C   . PHE B 289 ? 0.3041 0.4074 0.2065 0.0086  0.0595  0.0593  628 PHE B C   
4314 O O   . PHE B 289 ? 0.2956 0.4072 0.1957 0.0186  0.0549  0.0605  628 PHE B O   
4315 C CB  . PHE B 289 ? 0.3051 0.3765 0.1950 0.0049  0.0607  0.0630  628 PHE B CB  
4316 C CG  . PHE B 289 ? 0.2697 0.3412 0.1512 0.0185  0.0576  0.0688  628 PHE B CG  
4317 C CD1 . PHE B 289 ? 0.2600 0.3543 0.1589 0.0322  0.0504  0.0668  628 PHE B CD1 
4318 C CD2 . PHE B 289 ? 0.3012 0.3516 0.1565 0.0187  0.0625  0.0769  628 PHE B CD2 
4319 C CE1 . PHE B 289 ? 0.2796 0.3812 0.1725 0.0486  0.0480  0.0726  628 PHE B CE1 
4320 C CE2 . PHE B 289 ? 0.3256 0.3780 0.1728 0.0372  0.0590  0.0839  628 PHE B CE2 
4321 C CZ  . PHE B 289 ? 0.2822 0.3628 0.1492 0.0533  0.0518  0.0816  628 PHE B CZ  
4322 N N   . MET B 290 ? 0.2857 0.3850 0.1823 -0.0014 0.0688  0.0592  629 MET B N   
4323 C CA  . MET B 290 ? 0.2944 0.3941 0.1794 -0.0020 0.0749  0.0601  629 MET B CA  
4324 C C   . MET B 290 ? 0.3132 0.4405 0.2182 0.0040  0.0693  0.0547  629 MET B C   
4325 O O   . MET B 290 ? 0.3275 0.4572 0.2231 0.0091  0.0689  0.0549  629 MET B O   
4326 C CB  . MET B 290 ? 0.2862 0.3715 0.1585 -0.0157 0.0911  0.0612  629 MET B CB  
4327 C CG  . MET B 290 ? 0.3306 0.4132 0.1893 -0.0185 0.1016  0.0610  629 MET B CG  
4328 S SD  . MET B 290 ? 0.3706 0.4900 0.2623 -0.0177 0.1030  0.0540  629 MET B SD  
4329 C CE  . MET B 290 ? 0.3114 0.4459 0.2266 -0.0287 0.1098  0.0533  629 MET B CE  
4330 N N   . ILE B 291 ? 0.2856 0.4309 0.2138 0.0032  0.0649  0.0500  630 ILE B N   
4331 C CA  . ILE B 291 ? 0.2648 0.4306 0.2070 0.0086  0.0604  0.0448  630 ILE B CA  
4332 C C   . ILE B 291 ? 0.2906 0.4599 0.2329 0.0180  0.0512  0.0432  630 ILE B C   
4333 O O   . ILE B 291 ? 0.2676 0.4433 0.2063 0.0217  0.0512  0.0407  630 ILE B O   
4334 C CB  . ILE B 291 ? 0.2559 0.4370 0.2172 0.0072  0.0570  0.0411  630 ILE B CB  
4335 C CG1 . ILE B 291 ? 0.2697 0.4598 0.2365 -0.0027 0.0662  0.0422  630 ILE B CG1 
4336 C CG2 . ILE B 291 ? 0.2800 0.4746 0.2498 0.0136  0.0539  0.0357  630 ILE B CG2 
4337 C CD1 . ILE B 291 ? 0.2433 0.4375 0.2076 -0.0065 0.0787  0.0411  630 ILE B CD1 
4338 N N   . LEU B 292 ? 0.3229 0.4875 0.2687 0.0210  0.0451  0.0439  631 LEU B N   
4339 C CA  . LEU B 292 ? 0.2879 0.4588 0.2364 0.0284  0.0385  0.0411  631 LEU B CA  
4340 C C   . LEU B 292 ? 0.2676 0.4388 0.2013 0.0335  0.0391  0.0445  631 LEU B C   
4341 O O   . LEU B 292 ? 0.3014 0.4862 0.2353 0.0384  0.0353  0.0408  631 LEU B O   
4342 C CB  . LEU B 292 ? 0.2372 0.4019 0.1913 0.0296  0.0351  0.0409  631 LEU B CB  
4343 C CG  . LEU B 292 ? 0.2156 0.3781 0.1790 0.0262  0.0336  0.0371  631 LEU B CG  
4344 C CD1 . LEU B 292 ? 0.2456 0.3947 0.2081 0.0255  0.0336  0.0376  631 LEU B CD1 
4345 C CD2 . LEU B 292 ? 0.1901 0.3607 0.1587 0.0284  0.0307  0.0305  631 LEU B CD2 
4346 N N   . SER B 293 ? 0.3034 0.4594 0.2204 0.0326  0.0440  0.0516  632 SER B N   
4347 C CA  . SER B 293 ? 0.3338 0.4869 0.2297 0.0399  0.0438  0.0566  632 SER B CA  
4348 C C   . SER B 293 ? 0.3510 0.5065 0.2358 0.0379  0.0467  0.0541  632 SER B C   
4349 O O   . SER B 293 ? 0.3605 0.5251 0.2351 0.0457  0.0418  0.0535  632 SER B O   
4350 C CB  . SER B 293 ? 0.2957 0.4219 0.1682 0.0375  0.0499  0.0652  632 SER B CB  
4351 O OG  . SER B 293 ? 0.3662 0.4872 0.2454 0.0402  0.0481  0.0676  632 SER B OG  
4352 N N   . LYS B 294 ? 0.3296 0.4782 0.2149 0.0280  0.0554  0.0520  633 LYS B N   
4353 C CA  . LYS B 294 ? 0.3531 0.5018 0.2269 0.0258  0.0613  0.0490  633 LYS B CA  
4354 C C   . LYS B 294 ? 0.3601 0.5279 0.2501 0.0294  0.0554  0.0410  633 LYS B C   
4355 O O   . LYS B 294 ? 0.4132 0.5812 0.2894 0.0304  0.0575  0.0381  633 LYS B O   
4356 C CB  . LYS B 294 ? 0.3300 0.4713 0.2026 0.0153  0.0751  0.0490  633 LYS B CB  
4357 C CG  . LYS B 294 ? 0.3122 0.4278 0.1614 0.0074  0.0850  0.0555  633 LYS B CG  
4358 C CD  . LYS B 294 ? 0.3964 0.5068 0.2445 -0.0045 0.1027  0.0536  633 LYS B CD  
4359 C CE  . LYS B 294 ? 0.3648 0.4427 0.1815 -0.0159 0.1161  0.0589  633 LYS B CE  
4360 N NZ  . LYS B 294 ? 0.5035 0.5601 0.2801 -0.0150 0.1137  0.0642  633 LYS B NZ  
4361 N N   . ILE B 295 ? 0.3710 0.5507 0.2850 0.0304  0.0493  0.0373  634 ILE B N   
4362 C CA  . ILE B 295 ? 0.3176 0.5088 0.2410 0.0328  0.0446  0.0295  634 ILE B CA  
4363 C C   . ILE B 295 ? 0.3600 0.5607 0.2764 0.0383  0.0378  0.0275  634 ILE B C   
4364 O O   . ILE B 295 ? 0.3641 0.5709 0.2740 0.0386  0.0372  0.0212  634 ILE B O   
4365 C CB  . ILE B 295 ? 0.2936 0.4881 0.2362 0.0321  0.0406  0.0267  634 ILE B CB  
4366 C CG1 . ILE B 295 ? 0.3454 0.5400 0.2950 0.0291  0.0460  0.0269  634 ILE B CG1 
4367 C CG2 . ILE B 295 ? 0.2524 0.4511 0.1985 0.0333  0.0370  0.0187  634 ILE B CG2 
4368 C CD1 . ILE B 295 ? 0.2889 0.4836 0.2509 0.0296  0.0418  0.0248  634 ILE B CD1 
4369 N N   . GLN B 296 ? 0.3994 0.6047 0.3166 0.0435  0.0329  0.0325  635 GLN B N   
4370 C CA  . GLN B 296 ? 0.3721 0.5972 0.2863 0.0515  0.0254  0.0303  635 GLN B CA  
4371 C C   . GLN B 296 ? 0.4948 0.7161 0.3814 0.0565  0.0246  0.0336  635 GLN B C   
4372 O O   . GLN B 296 ? 0.5286 0.7679 0.4089 0.0618  0.0174  0.0284  635 GLN B O   
4373 C CB  . GLN B 296 ? 0.2993 0.5316 0.2231 0.0582  0.0217  0.0346  635 GLN B CB  
4374 C CG  . GLN B 296 ? 0.3938 0.6576 0.3233 0.0674  0.0141  0.0293  635 GLN B CG  
4375 C CD  . GLN B 296 ? 0.3866 0.6579 0.3243 0.0764  0.0128  0.0341  635 GLN B CD  
4376 O OE1 . GLN B 296 ? 0.3764 0.6237 0.3072 0.0774  0.0172  0.0436  635 GLN B OE1 
4377 N NE2 . GLN B 296 ? 0.3397 0.6450 0.2910 0.0821  0.0080  0.0260  635 GLN B NE2 
4378 N N   . SER B 297 ? 0.6711 0.8675 0.5378 0.0536  0.0316  0.0412  636 SER B N   
4379 C CA  . SER B 297 ? 0.7412 0.9231 0.5726 0.0567  0.0319  0.0454  636 SER B CA  
4380 C C   . SER B 297 ? 0.8042 0.9985 0.6245 0.0707  0.0192  0.0477  636 SER B C   
4381 O O   . SER B 297 ? 0.9417 1.1395 0.7411 0.0748  0.0124  0.0447  636 SER B O   
4382 C CB  . SER B 297 ? 0.6470 0.8273 0.4668 0.0509  0.0359  0.0382  636 SER B CB  
4383 O OG  . SER B 297 ? 0.7724 0.9773 0.6056 0.0532  0.0278  0.0284  636 SER B OG  
# 
