data_9I10
# 
_entry.id   9I10 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9I10         pdb_00009i10 10.2210/pdb9i10/pdb 
WWPDB D_1292144686 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
# 
_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                        9I10 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-15 
_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           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB '8C6M contains the same protein complexed with a similar inhibitor' 8C6M unspecified 
PDB '8C6N contains the same protein complexed with a similar inhibitor' 8C6N unspecified 
PDB '9I0Z contains the same protein complexed with a similar inhibitor' 9I0Z unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              graziano.lolli@unitn.it 
_pdbx_contact_author.name_first         Graziano 
_pdbx_contact_author.name_last          Lolli 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8536-5599 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dalle Vedove, A.' 1 ? 
'Cazzanelli, G.'   2 ? 
'Lolli, G.'        3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Switching off CK2-mediated activation of survivin offers new therapeutic opportunities in neuroblastoma' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cazzanelli, G.'   1  ? 
primary 'Dalle Vedove, A.' 2  ? 
primary 'Broso, F.'        3  ? 
primary 'Burigotto, M.'    4  ? 
primary 'Zasso, J.'        5  ? 
primary 'Aiello, G.'       6  ? 
primary 'Zonta, F.'        7  ? 
primary 'Astolfi, A.'      8  ? 
primary 'Barreca, M.L.'    9  ? 
primary 'Ruzzene, M.'      10 ? 
primary 'Tiberi, L.'       11 ? 
primary 'Fava, L.L.'       12 ? 
primary 'Quattrone, A.'    13 ? 
primary 'Lolli, G.'        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 'Casein kinase II subunit alpha'                                                                           
39303.820 1   2.7.11.1 ? ? ? 
2 non-polymer syn '(2~{Z},5~{Z})-5-[(4-methoxy-3-oxidanyl-phenyl)methylidene]-2-(3-methylphenyl)imino-1,3-thiazolidin-4-one' 
340.396   1   ?        ? ? ? 
3 non-polymer syn 'SULFATE ION'                                                                                              
96.063    3   ?        ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                                                             
62.068    1   ?        ? ? ? 
5 water       nat water                                                                                                      
18.015    348 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'CK II alpha' 
# 
_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       
;GPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREI
KILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV
MIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQL
VRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHP
YFYTVVKD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREI
KILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV
MIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQL
VRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHP
YFYTVVKD
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2~{Z},5~{Z})-5-[(4-methoxy-3-oxidanyl-phenyl)methylidene]-2-(3-methylphenyl)imino-1,3-thiazolidin-4-one' A1IYV 
3 'SULFATE ION'                                                                                              SO4   
4 1,2-ETHANEDIOL                                                                                             EDO   
5 water                                                                                                      HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   VAL n 
1 4   PRO n 
1 5   SER n 
1 6   ARG n 
1 7   ALA n 
1 8   ARG n 
1 9   VAL n 
1 10  TYR n 
1 11  THR n 
1 12  ASP n 
1 13  VAL n 
1 14  ASN n 
1 15  THR n 
1 16  HIS n 
1 17  ARG n 
1 18  PRO n 
1 19  ARG n 
1 20  GLU n 
1 21  TYR n 
1 22  TRP n 
1 23  ASP n 
1 24  TYR n 
1 25  GLU n 
1 26  SER n 
1 27  HIS n 
1 28  VAL n 
1 29  VAL n 
1 30  GLU n 
1 31  TRP n 
1 32  GLY n 
1 33  ASN n 
1 34  GLN n 
1 35  ASP n 
1 36  ASP n 
1 37  TYR n 
1 38  GLN n 
1 39  LEU n 
1 40  VAL n 
1 41  ARG n 
1 42  LYS n 
1 43  LEU n 
1 44  GLY n 
1 45  ARG n 
1 46  GLY n 
1 47  LYS n 
1 48  TYR n 
1 49  SER n 
1 50  GLU n 
1 51  VAL n 
1 52  PHE n 
1 53  GLU n 
1 54  ALA n 
1 55  ILE n 
1 56  ASN n 
1 57  ILE n 
1 58  THR n 
1 59  ASN n 
1 60  ASN n 
1 61  GLU n 
1 62  LYS n 
1 63  VAL n 
1 64  VAL n 
1 65  VAL n 
1 66  LYS n 
1 67  ILE n 
1 68  LEU n 
1 69  LYS n 
1 70  PRO n 
1 71  VAL n 
1 72  LYS n 
1 73  LYS n 
1 74  LYS n 
1 75  LYS n 
1 76  ILE n 
1 77  LYS n 
1 78  ARG n 
1 79  GLU n 
1 80  ILE n 
1 81  LYS n 
1 82  ILE n 
1 83  LEU n 
1 84  GLU n 
1 85  ASN n 
1 86  LEU n 
1 87  ARG n 
1 88  GLY n 
1 89  GLY n 
1 90  PRO n 
1 91  ASN n 
1 92  ILE n 
1 93  ILE n 
1 94  THR n 
1 95  LEU n 
1 96  ALA n 
1 97  ASP n 
1 98  ILE n 
1 99  VAL n 
1 100 LYS n 
1 101 ASP n 
1 102 PRO n 
1 103 VAL n 
1 104 SER n 
1 105 ARG n 
1 106 THR n 
1 107 PRO n 
1 108 ALA n 
1 109 LEU n 
1 110 VAL n 
1 111 PHE n 
1 112 GLU n 
1 113 HIS n 
1 114 VAL n 
1 115 ASN n 
1 116 ASN n 
1 117 THR n 
1 118 ASP n 
1 119 PHE n 
1 120 LYS n 
1 121 GLN n 
1 122 LEU n 
1 123 TYR n 
1 124 GLN n 
1 125 THR n 
1 126 LEU n 
1 127 THR n 
1 128 ASP n 
1 129 TYR n 
1 130 ASP n 
1 131 ILE n 
1 132 ARG n 
1 133 PHE n 
1 134 TYR n 
1 135 MET n 
1 136 TYR n 
1 137 GLU n 
1 138 ILE n 
1 139 LEU n 
1 140 LYS n 
1 141 ALA n 
1 142 LEU n 
1 143 ASP n 
1 144 TYR n 
1 145 CYS n 
1 146 HIS n 
1 147 SER n 
1 148 MET n 
1 149 GLY n 
1 150 ILE n 
1 151 MET n 
1 152 HIS n 
1 153 ARG n 
1 154 ASP n 
1 155 VAL n 
1 156 LYS n 
1 157 PRO n 
1 158 HIS n 
1 159 ASN n 
1 160 VAL n 
1 161 MET n 
1 162 ILE n 
1 163 ASP n 
1 164 HIS n 
1 165 GLU n 
1 166 HIS n 
1 167 ARG n 
1 168 LYS n 
1 169 LEU n 
1 170 ARG n 
1 171 LEU n 
1 172 ILE n 
1 173 ASP n 
1 174 TRP n 
1 175 GLY n 
1 176 LEU n 
1 177 ALA n 
1 178 GLU n 
1 179 PHE n 
1 180 TYR n 
1 181 HIS n 
1 182 PRO n 
1 183 GLY n 
1 184 GLN n 
1 185 GLU n 
1 186 TYR n 
1 187 ASN n 
1 188 VAL n 
1 189 ARG n 
1 190 VAL n 
1 191 ALA n 
1 192 SER n 
1 193 ARG n 
1 194 TYR n 
1 195 PHE n 
1 196 LYS n 
1 197 GLY n 
1 198 PRO n 
1 199 GLU n 
1 200 LEU n 
1 201 LEU n 
1 202 VAL n 
1 203 ASP n 
1 204 TYR n 
1 205 GLN n 
1 206 MET n 
1 207 TYR n 
1 208 ASP n 
1 209 TYR n 
1 210 SER n 
1 211 LEU n 
1 212 ASP n 
1 213 MET n 
1 214 TRP n 
1 215 SER n 
1 216 LEU n 
1 217 GLY n 
1 218 CYS n 
1 219 MET n 
1 220 LEU n 
1 221 ALA n 
1 222 SER n 
1 223 MET n 
1 224 ILE n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 GLU n 
1 229 PRO n 
1 230 PHE n 
1 231 PHE n 
1 232 HIS n 
1 233 GLY n 
1 234 HIS n 
1 235 ASP n 
1 236 ASN n 
1 237 TYR n 
1 238 ASP n 
1 239 GLN n 
1 240 LEU n 
1 241 VAL n 
1 242 ARG n 
1 243 ILE n 
1 244 ALA n 
1 245 LYS n 
1 246 VAL n 
1 247 LEU n 
1 248 GLY n 
1 249 THR n 
1 250 GLU n 
1 251 ASP n 
1 252 LEU n 
1 253 TYR n 
1 254 ASP n 
1 255 TYR n 
1 256 ILE n 
1 257 ASP n 
1 258 LYS n 
1 259 TYR n 
1 260 ASN n 
1 261 ILE n 
1 262 GLU n 
1 263 LEU n 
1 264 ASP n 
1 265 PRO n 
1 266 ARG n 
1 267 PHE n 
1 268 ASN n 
1 269 ASP n 
1 270 ILE n 
1 271 LEU n 
1 272 GLY n 
1 273 ARG n 
1 274 HIS n 
1 275 SER n 
1 276 ARG n 
1 277 LYS n 
1 278 ARG n 
1 279 TRP n 
1 280 GLU n 
1 281 ARG n 
1 282 PHE n 
1 283 VAL n 
1 284 HIS n 
1 285 SER n 
1 286 GLU n 
1 287 ASN n 
1 288 GLN n 
1 289 HIS n 
1 290 LEU n 
1 291 VAL n 
1 292 SER n 
1 293 PRO n 
1 294 GLU n 
1 295 ALA n 
1 296 LEU n 
1 297 ASP n 
1 298 PHE n 
1 299 LEU n 
1 300 ASP n 
1 301 LYS n 
1 302 LEU n 
1 303 LEU n 
1 304 ARG n 
1 305 TYR n 
1 306 ASP n 
1 307 HIS n 
1 308 GLN n 
1 309 SER n 
1 310 ARG n 
1 311 LEU n 
1 312 THR n 
1 313 ALA n 
1 314 ARG n 
1 315 GLU n 
1 316 ALA n 
1 317 MET n 
1 318 GLU n 
1 319 HIS n 
1 320 PRO n 
1 321 TYR n 
1 322 PHE n 
1 323 TYR n 
1 324 THR n 
1 325 VAL n 
1 326 VAL n 
1 327 LYS n 
1 328 ASP 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                   328 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CSNK2A1, CK2A1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IYV non-polymer         . 
'(2~{Z},5~{Z})-5-[(4-methoxy-3-oxidanyl-phenyl)methylidene]-2-(3-methylphenyl)imino-1,3-thiazolidin-4-one' 
'PEPTIDE DERIVED CHROMOPHORE' 'C18 H16 N2 O3 S' 340.396 
ALA   'L-peptide linking' y ALANINE ?                             'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ?                             'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                             'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                             'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE ?                             'C3 H7 N O2 S'    121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL'             'C2 H6 O2'        62.068  
GLN   'L-peptide linking' y GLUTAMINE ?                             'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                             'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE ?                             'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE ?                             'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER ?                             'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                             'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE ?                             'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE ?                             'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE ?                             'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?                             'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ?                             'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE ?                             'C3 H7 N O3'      105.093 
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   GLY 1   3   3   GLY GLY A . n 
A 1 2   PRO 2   4   4   PRO PRO A . n 
A 1 3   VAL 3   5   5   VAL VAL A . n 
A 1 4   PRO 4   6   6   PRO PRO A . n 
A 1 5   SER 5   7   7   SER SER A . n 
A 1 6   ARG 6   8   8   ARG ARG A . n 
A 1 7   ALA 7   9   9   ALA ALA A . n 
A 1 8   ARG 8   10  10  ARG ARG A . n 
A 1 9   VAL 9   11  11  VAL VAL A . n 
A 1 10  TYR 10  12  12  TYR TYR A . n 
A 1 11  THR 11  13  13  THR THR A . n 
A 1 12  ASP 12  14  14  ASP ASP A . n 
A 1 13  VAL 13  15  15  VAL VAL A . n 
A 1 14  ASN 14  16  16  ASN ASN A . n 
A 1 15  THR 15  17  17  THR THR A . n 
A 1 16  HIS 16  18  18  HIS HIS A . n 
A 1 17  ARG 17  19  19  ARG ARG A . n 
A 1 18  PRO 18  20  20  PRO PRO A . n 
A 1 19  ARG 19  21  21  ARG ARG A . n 
A 1 20  GLU 20  22  22  GLU GLU A . n 
A 1 21  TYR 21  23  23  TYR TYR A . n 
A 1 22  TRP 22  24  24  TRP TRP A . n 
A 1 23  ASP 23  25  25  ASP ASP A . n 
A 1 24  TYR 24  26  26  TYR TYR A . n 
A 1 25  GLU 25  27  27  GLU GLU A . n 
A 1 26  SER 26  28  28  SER SER A . n 
A 1 27  HIS 27  29  29  HIS HIS A . n 
A 1 28  VAL 28  30  30  VAL VAL A . n 
A 1 29  VAL 29  31  31  VAL VAL A . n 
A 1 30  GLU 30  32  32  GLU GLU A . n 
A 1 31  TRP 31  33  33  TRP TRP A . n 
A 1 32  GLY 32  34  34  GLY GLY A . n 
A 1 33  ASN 33  35  35  ASN ASN A . n 
A 1 34  GLN 34  36  36  GLN GLN A . n 
A 1 35  ASP 35  37  37  ASP ASP A . n 
A 1 36  ASP 36  38  38  ASP ASP A . n 
A 1 37  TYR 37  39  39  TYR TYR A . n 
A 1 38  GLN 38  40  40  GLN GLN A . n 
A 1 39  LEU 39  41  41  LEU LEU A . n 
A 1 40  VAL 40  42  42  VAL VAL A . n 
A 1 41  ARG 41  43  43  ARG ARG A . n 
A 1 42  LYS 42  44  44  LYS LYS A . n 
A 1 43  LEU 43  45  45  LEU LEU A . n 
A 1 44  GLY 44  46  46  GLY GLY A . n 
A 1 45  ARG 45  47  47  ARG ARG A . n 
A 1 46  GLY 46  48  48  GLY GLY A . n 
A 1 47  LYS 47  49  49  LYS LYS A . n 
A 1 48  TYR 48  50  50  TYR TYR A . n 
A 1 49  SER 49  51  51  SER SER A . n 
A 1 50  GLU 50  52  52  GLU GLU A . n 
A 1 51  VAL 51  53  53  VAL VAL A . n 
A 1 52  PHE 52  54  54  PHE PHE A . n 
A 1 53  GLU 53  55  55  GLU GLU A . n 
A 1 54  ALA 54  56  56  ALA ALA A . n 
A 1 55  ILE 55  57  57  ILE ILE A . n 
A 1 56  ASN 56  58  58  ASN ASN A . n 
A 1 57  ILE 57  59  59  ILE ILE A . n 
A 1 58  THR 58  60  60  THR THR A . n 
A 1 59  ASN 59  61  61  ASN ASN A . n 
A 1 60  ASN 60  62  62  ASN ASN A . n 
A 1 61  GLU 61  63  63  GLU GLU A . n 
A 1 62  LYS 62  64  64  LYS LYS A . n 
A 1 63  VAL 63  65  65  VAL VAL A . n 
A 1 64  VAL 64  66  66  VAL VAL A . n 
A 1 65  VAL 65  67  67  VAL VAL A . n 
A 1 66  LYS 66  68  68  LYS LYS A . n 
A 1 67  ILE 67  69  69  ILE ILE A . n 
A 1 68  LEU 68  70  70  LEU LEU A . n 
A 1 69  LYS 69  71  71  LYS LYS A . n 
A 1 70  PRO 70  72  72  PRO PRO A . n 
A 1 71  VAL 71  73  73  VAL VAL A . n 
A 1 72  LYS 72  74  74  LYS LYS A . n 
A 1 73  LYS 73  75  75  LYS LYS A . n 
A 1 74  LYS 74  76  76  LYS LYS A . n 
A 1 75  LYS 75  77  77  LYS LYS A . n 
A 1 76  ILE 76  78  78  ILE ILE A . n 
A 1 77  LYS 77  79  79  LYS LYS A . n 
A 1 78  ARG 78  80  80  ARG ARG A . n 
A 1 79  GLU 79  81  81  GLU GLU A . n 
A 1 80  ILE 80  82  82  ILE ILE A . n 
A 1 81  LYS 81  83  83  LYS LYS A . n 
A 1 82  ILE 82  84  84  ILE ILE A . n 
A 1 83  LEU 83  85  85  LEU LEU A . n 
A 1 84  GLU 84  86  86  GLU GLU A . n 
A 1 85  ASN 85  87  87  ASN ASN A . n 
A 1 86  LEU 86  88  88  LEU LEU A . n 
A 1 87  ARG 87  89  89  ARG ARG A . n 
A 1 88  GLY 88  90  90  GLY GLY A . n 
A 1 89  GLY 89  91  91  GLY GLY A . n 
A 1 90  PRO 90  92  92  PRO PRO A . n 
A 1 91  ASN 91  93  93  ASN ASN A . n 
A 1 92  ILE 92  94  94  ILE ILE A . n 
A 1 93  ILE 93  95  95  ILE ILE A . n 
A 1 94  THR 94  96  96  THR THR A . n 
A 1 95  LEU 95  97  97  LEU LEU A . n 
A 1 96  ALA 96  98  98  ALA ALA A . n 
A 1 97  ASP 97  99  99  ASP ASP A . n 
A 1 98  ILE 98  100 100 ILE ILE A . n 
A 1 99  VAL 99  101 101 VAL VAL A . n 
A 1 100 LYS 100 102 102 LYS LYS A . n 
A 1 101 ASP 101 103 103 ASP ASP A . n 
A 1 102 PRO 102 104 104 PRO PRO A . n 
A 1 103 VAL 103 105 105 VAL VAL A . n 
A 1 104 SER 104 106 106 SER SER A . n 
A 1 105 ARG 105 107 107 ARG ARG A . n 
A 1 106 THR 106 108 108 THR THR A . n 
A 1 107 PRO 107 109 109 PRO PRO A . n 
A 1 108 ALA 108 110 110 ALA ALA A . n 
A 1 109 LEU 109 111 111 LEU LEU A . n 
A 1 110 VAL 110 112 112 VAL VAL A . n 
A 1 111 PHE 111 113 113 PHE PHE A . n 
A 1 112 GLU 112 114 114 GLU GLU A . n 
A 1 113 HIS 113 115 115 HIS HIS A . n 
A 1 114 VAL 114 116 116 VAL VAL A . n 
A 1 115 ASN 115 117 117 ASN ASN A . n 
A 1 116 ASN 116 118 118 ASN ASN A . n 
A 1 117 THR 117 119 119 THR THR A . n 
A 1 118 ASP 118 120 120 ASP ASP A . n 
A 1 119 PHE 119 121 121 PHE PHE A . n 
A 1 120 LYS 120 122 122 LYS LYS A . n 
A 1 121 GLN 121 123 123 GLN GLN A . n 
A 1 122 LEU 122 124 124 LEU LEU A . n 
A 1 123 TYR 123 125 125 TYR TYR A . n 
A 1 124 GLN 124 126 126 GLN GLN A . n 
A 1 125 THR 125 127 127 THR THR A . n 
A 1 126 LEU 126 128 128 LEU LEU A . n 
A 1 127 THR 127 129 129 THR THR A . n 
A 1 128 ASP 128 130 130 ASP ASP A . n 
A 1 129 TYR 129 131 131 TYR TYR A . n 
A 1 130 ASP 130 132 132 ASP ASP A . n 
A 1 131 ILE 131 133 133 ILE ILE A . n 
A 1 132 ARG 132 134 134 ARG ARG A . n 
A 1 133 PHE 133 135 135 PHE PHE A . n 
A 1 134 TYR 134 136 136 TYR TYR A . n 
A 1 135 MET 135 137 137 MET MET A . n 
A 1 136 TYR 136 138 138 TYR TYR A . n 
A 1 137 GLU 137 139 139 GLU GLU A . n 
A 1 138 ILE 138 140 140 ILE ILE A . n 
A 1 139 LEU 139 141 141 LEU LEU A . n 
A 1 140 LYS 140 142 142 LYS LYS A . n 
A 1 141 ALA 141 143 143 ALA ALA A . n 
A 1 142 LEU 142 144 144 LEU LEU A . n 
A 1 143 ASP 143 145 145 ASP ASP A . n 
A 1 144 TYR 144 146 146 TYR TYR A . n 
A 1 145 CYS 145 147 147 CYS CYS A . n 
A 1 146 HIS 146 148 148 HIS HIS A . n 
A 1 147 SER 147 149 149 SER SER A . n 
A 1 148 MET 148 150 150 MET MET A . n 
A 1 149 GLY 149 151 151 GLY GLY A . n 
A 1 150 ILE 150 152 152 ILE ILE A . n 
A 1 151 MET 151 153 153 MET MET A . n 
A 1 152 HIS 152 154 154 HIS HIS A . n 
A 1 153 ARG 153 155 155 ARG ARG A . n 
A 1 154 ASP 154 156 156 ASP ASP A . n 
A 1 155 VAL 155 157 157 VAL VAL A . n 
A 1 156 LYS 156 158 158 LYS LYS A . n 
A 1 157 PRO 157 159 159 PRO PRO A . n 
A 1 158 HIS 158 160 160 HIS HIS A . n 
A 1 159 ASN 159 161 161 ASN ASN A . n 
A 1 160 VAL 160 162 162 VAL VAL A . n 
A 1 161 MET 161 163 163 MET MET A . n 
A 1 162 ILE 162 164 164 ILE ILE A . n 
A 1 163 ASP 163 165 165 ASP ASP A . n 
A 1 164 HIS 164 166 166 HIS HIS A . n 
A 1 165 GLU 165 167 167 GLU GLU A . n 
A 1 166 HIS 166 168 168 HIS HIS A . n 
A 1 167 ARG 167 169 169 ARG ARG A . n 
A 1 168 LYS 168 170 170 LYS LYS A . n 
A 1 169 LEU 169 171 171 LEU LEU A . n 
A 1 170 ARG 170 172 172 ARG ARG A . n 
A 1 171 LEU 171 173 173 LEU LEU A . n 
A 1 172 ILE 172 174 174 ILE ILE A . n 
A 1 173 ASP 173 175 175 ASP ASP A . n 
A 1 174 TRP 174 176 176 TRP TRP A . n 
A 1 175 GLY 175 177 177 GLY GLY A . n 
A 1 176 LEU 176 178 178 LEU LEU A . n 
A 1 177 ALA 177 179 179 ALA ALA A . n 
A 1 178 GLU 178 180 180 GLU GLU A . n 
A 1 179 PHE 179 181 181 PHE PHE A . n 
A 1 180 TYR 180 182 182 TYR TYR A . n 
A 1 181 HIS 181 183 183 HIS HIS A . n 
A 1 182 PRO 182 184 184 PRO PRO A . n 
A 1 183 GLY 183 185 185 GLY GLY A . n 
A 1 184 GLN 184 186 186 GLN GLN A . n 
A 1 185 GLU 185 187 187 GLU GLU A . n 
A 1 186 TYR 186 188 188 TYR TYR A . n 
A 1 187 ASN 187 189 189 ASN ASN A . n 
A 1 188 VAL 188 190 190 VAL VAL A . n 
A 1 189 ARG 189 191 191 ARG ARG A . n 
A 1 190 VAL 190 192 192 VAL VAL A . n 
A 1 191 ALA 191 193 193 ALA ALA A . n 
A 1 192 SER 192 194 194 SER SER A . n 
A 1 193 ARG 193 195 195 ARG ARG A . n 
A 1 194 TYR 194 196 196 TYR TYR A . n 
A 1 195 PHE 195 197 197 PHE PHE A . n 
A 1 196 LYS 196 198 198 LYS LYS A . n 
A 1 197 GLY 197 199 199 GLY GLY A . n 
A 1 198 PRO 198 200 200 PRO PRO A . n 
A 1 199 GLU 199 201 201 GLU GLU A . n 
A 1 200 LEU 200 202 202 LEU LEU A . n 
A 1 201 LEU 201 203 203 LEU LEU A . n 
A 1 202 VAL 202 204 204 VAL VAL A . n 
A 1 203 ASP 203 205 205 ASP ASP A . n 
A 1 204 TYR 204 206 206 TYR TYR A . n 
A 1 205 GLN 205 207 207 GLN GLN A . n 
A 1 206 MET 206 208 208 MET MET A . n 
A 1 207 TYR 207 209 209 TYR TYR A . n 
A 1 208 ASP 208 210 210 ASP ASP A . n 
A 1 209 TYR 209 211 211 TYR TYR A . n 
A 1 210 SER 210 212 212 SER SER A . n 
A 1 211 LEU 211 213 213 LEU LEU A . n 
A 1 212 ASP 212 214 214 ASP ASP A . n 
A 1 213 MET 213 215 215 MET MET A . n 
A 1 214 TRP 214 216 216 TRP TRP A . n 
A 1 215 SER 215 217 217 SER SER A . n 
A 1 216 LEU 216 218 218 LEU LEU A . n 
A 1 217 GLY 217 219 219 GLY GLY A . n 
A 1 218 CYS 218 220 220 CYS CYS A . n 
A 1 219 MET 219 221 221 MET MET A . n 
A 1 220 LEU 220 222 222 LEU LEU A . n 
A 1 221 ALA 221 223 223 ALA ALA A . n 
A 1 222 SER 222 224 224 SER SER A . n 
A 1 223 MET 223 225 225 MET MET A . n 
A 1 224 ILE 224 226 226 ILE ILE A . n 
A 1 225 PHE 225 227 227 PHE PHE A . n 
A 1 226 ARG 226 228 228 ARG ARG A . n 
A 1 227 LYS 227 229 229 LYS LYS A . n 
A 1 228 GLU 228 230 230 GLU GLU A . n 
A 1 229 PRO 229 231 231 PRO PRO A . n 
A 1 230 PHE 230 232 232 PHE PHE A . n 
A 1 231 PHE 231 233 233 PHE PHE A . n 
A 1 232 HIS 232 234 234 HIS HIS A . n 
A 1 233 GLY 233 235 235 GLY GLY A . n 
A 1 234 HIS 234 236 236 HIS HIS A . n 
A 1 235 ASP 235 237 237 ASP ASP A . n 
A 1 236 ASN 236 238 238 ASN ASN A . n 
A 1 237 TYR 237 239 239 TYR TYR A . n 
A 1 238 ASP 238 240 240 ASP ASP A . n 
A 1 239 GLN 239 241 241 GLN GLN A . n 
A 1 240 LEU 240 242 242 LEU LEU A . n 
A 1 241 VAL 241 243 243 VAL VAL A . n 
A 1 242 ARG 242 244 244 ARG ARG A . n 
A 1 243 ILE 243 245 245 ILE ILE A . n 
A 1 244 ALA 244 246 246 ALA ALA A . n 
A 1 245 LYS 245 247 247 LYS LYS A . n 
A 1 246 VAL 246 248 248 VAL VAL A . n 
A 1 247 LEU 247 249 249 LEU LEU A . n 
A 1 248 GLY 248 250 250 GLY GLY A . n 
A 1 249 THR 249 251 251 THR THR A . n 
A 1 250 GLU 250 252 252 GLU GLU A . n 
A 1 251 ASP 251 253 253 ASP ASP A . n 
A 1 252 LEU 252 254 254 LEU LEU A . n 
A 1 253 TYR 253 255 255 TYR TYR A . n 
A 1 254 ASP 254 256 256 ASP ASP A . n 
A 1 255 TYR 255 257 257 TYR TYR A . n 
A 1 256 ILE 256 258 258 ILE ILE A . n 
A 1 257 ASP 257 259 259 ASP ASP A . n 
A 1 258 LYS 258 260 260 LYS LYS A . n 
A 1 259 TYR 259 261 261 TYR TYR A . n 
A 1 260 ASN 260 262 262 ASN ASN A . n 
A 1 261 ILE 261 263 263 ILE ILE A . n 
A 1 262 GLU 262 264 264 GLU GLU A . n 
A 1 263 LEU 263 265 265 LEU LEU A . n 
A 1 264 ASP 264 266 266 ASP ASP A . n 
A 1 265 PRO 265 267 267 PRO PRO A . n 
A 1 266 ARG 266 268 268 ARG ARG A . n 
A 1 267 PHE 267 269 269 PHE PHE A . n 
A 1 268 ASN 268 270 270 ASN ASN A . n 
A 1 269 ASP 269 271 271 ASP ASP A . n 
A 1 270 ILE 270 272 272 ILE ILE A . n 
A 1 271 LEU 271 273 273 LEU LEU A . n 
A 1 272 GLY 272 274 274 GLY GLY A . n 
A 1 273 ARG 273 275 275 ARG ARG A . n 
A 1 274 HIS 274 276 276 HIS HIS A . n 
A 1 275 SER 275 277 277 SER SER A . n 
A 1 276 ARG 276 278 278 ARG ARG A . n 
A 1 277 LYS 277 279 279 LYS LYS A . n 
A 1 278 ARG 278 280 280 ARG ARG A . n 
A 1 279 TRP 279 281 281 TRP TRP A . n 
A 1 280 GLU 280 282 282 GLU GLU A . n 
A 1 281 ARG 281 283 283 ARG ARG A . n 
A 1 282 PHE 282 284 284 PHE PHE A . n 
A 1 283 VAL 283 285 285 VAL VAL A . n 
A 1 284 HIS 284 286 286 HIS HIS A . n 
A 1 285 SER 285 287 287 SER SER A . n 
A 1 286 GLU 286 288 288 GLU GLU A . n 
A 1 287 ASN 287 289 289 ASN ASN A . n 
A 1 288 GLN 288 290 290 GLN GLN A . n 
A 1 289 HIS 289 291 291 HIS HIS A . n 
A 1 290 LEU 290 292 292 LEU LEU A . n 
A 1 291 VAL 291 293 293 VAL VAL A . n 
A 1 292 SER 292 294 294 SER SER A . n 
A 1 293 PRO 293 295 295 PRO PRO A . n 
A 1 294 GLU 294 296 296 GLU GLU A . n 
A 1 295 ALA 295 297 297 ALA ALA A . n 
A 1 296 LEU 296 298 298 LEU LEU A . n 
A 1 297 ASP 297 299 299 ASP ASP A . n 
A 1 298 PHE 298 300 300 PHE PHE A . n 
A 1 299 LEU 299 301 301 LEU LEU A . n 
A 1 300 ASP 300 302 302 ASP ASP A . n 
A 1 301 LYS 301 303 303 LYS LYS A . n 
A 1 302 LEU 302 304 304 LEU LEU A . n 
A 1 303 LEU 303 305 305 LEU LEU A . n 
A 1 304 ARG 304 306 306 ARG ARG A . n 
A 1 305 TYR 305 307 307 TYR TYR A . n 
A 1 306 ASP 306 308 308 ASP ASP A . n 
A 1 307 HIS 307 309 309 HIS HIS A . n 
A 1 308 GLN 308 310 310 GLN GLN A . n 
A 1 309 SER 309 311 311 SER SER A . n 
A 1 310 ARG 310 312 312 ARG ARG A . n 
A 1 311 LEU 311 313 313 LEU LEU A . n 
A 1 312 THR 312 314 314 THR THR A . n 
A 1 313 ALA 313 315 315 ALA ALA A . n 
A 1 314 ARG 314 316 316 ARG ARG A . n 
A 1 315 GLU 315 317 317 GLU GLU A . n 
A 1 316 ALA 316 318 318 ALA ALA A . n 
A 1 317 MET 317 319 319 MET MET A . n 
A 1 318 GLU 318 320 320 GLU GLU A . n 
A 1 319 HIS 319 321 321 HIS HIS A . n 
A 1 320 PRO 320 322 322 PRO PRO A . n 
A 1 321 TYR 321 323 323 TYR TYR A . n 
A 1 322 PHE 322 324 324 PHE PHE A . n 
A 1 323 TYR 323 325 325 TYR TYR A . n 
A 1 324 THR 324 326 326 THR THR A . n 
A 1 325 VAL 325 327 327 VAL VAL A . n 
A 1 326 VAL 326 328 328 VAL VAL A . n 
A 1 327 LYS 327 329 329 LYS LYS A . n 
A 1 328 ASP 328 330 330 ASP ASP A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IYV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IYV 
_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 
B 2 A1IYV 1   401 401 A1IYV C12 A . 
C 3 SO4   1   402 501 SO4   SO4 A . 
D 3 SO4   1   403 601 SO4   SO4 A . 
E 3 SO4   1   404 701 SO4   SO4 A . 
F 4 EDO   1   405 801 EDO   EDO A . 
G 5 HOH   1   501 232 HOH   HOH A . 
G 5 HOH   2   502 191 HOH   HOH A . 
G 5 HOH   3   503 165 HOH   HOH A . 
G 5 HOH   4   504 316 HOH   HOH A . 
G 5 HOH   5   505 262 HOH   HOH A . 
G 5 HOH   6   506 143 HOH   HOH A . 
G 5 HOH   7   507 235 HOH   HOH A . 
G 5 HOH   8   508 241 HOH   HOH A . 
G 5 HOH   9   509 332 HOH   HOH A . 
G 5 HOH   10  510 298 HOH   HOH A . 
G 5 HOH   11  511 135 HOH   HOH A . 
G 5 HOH   12  512 287 HOH   HOH A . 
G 5 HOH   13  513 31  HOH   HOH A . 
G 5 HOH   14  514 210 HOH   HOH A . 
G 5 HOH   15  515 252 HOH   HOH A . 
G 5 HOH   16  516 282 HOH   HOH A . 
G 5 HOH   17  517 278 HOH   HOH A . 
G 5 HOH   18  518 99  HOH   HOH A . 
G 5 HOH   19  519 326 HOH   HOH A . 
G 5 HOH   20  520 285 HOH   HOH A . 
G 5 HOH   21  521 297 HOH   HOH A . 
G 5 HOH   22  522 92  HOH   HOH A . 
G 5 HOH   23  523 215 HOH   HOH A . 
G 5 HOH   24  524 66  HOH   HOH A . 
G 5 HOH   25  525 126 HOH   HOH A . 
G 5 HOH   26  526 251 HOH   HOH A . 
G 5 HOH   27  527 51  HOH   HOH A . 
G 5 HOH   28  528 55  HOH   HOH A . 
G 5 HOH   29  529 52  HOH   HOH A . 
G 5 HOH   30  530 343 HOH   HOH A . 
G 5 HOH   31  531 233 HOH   HOH A . 
G 5 HOH   32  532 88  HOH   HOH A . 
G 5 HOH   33  533 75  HOH   HOH A . 
G 5 HOH   34  534 200 HOH   HOH A . 
G 5 HOH   35  535 340 HOH   HOH A . 
G 5 HOH   36  536 138 HOH   HOH A . 
G 5 HOH   37  537 169 HOH   HOH A . 
G 5 HOH   38  538 32  HOH   HOH A . 
G 5 HOH   39  539 107 HOH   HOH A . 
G 5 HOH   40  540 144 HOH   HOH A . 
G 5 HOH   41  541 146 HOH   HOH A . 
G 5 HOH   42  542 50  HOH   HOH A . 
G 5 HOH   43  543 37  HOH   HOH A . 
G 5 HOH   44  544 213 HOH   HOH A . 
G 5 HOH   45  545 78  HOH   HOH A . 
G 5 HOH   46  546 65  HOH   HOH A . 
G 5 HOH   47  547 136 HOH   HOH A . 
G 5 HOH   48  548 226 HOH   HOH A . 
G 5 HOH   49  549 234 HOH   HOH A . 
G 5 HOH   50  550 183 HOH   HOH A . 
G 5 HOH   51  551 238 HOH   HOH A . 
G 5 HOH   52  552 230 HOH   HOH A . 
G 5 HOH   53  553 168 HOH   HOH A . 
G 5 HOH   54  554 272 HOH   HOH A . 
G 5 HOH   55  555 35  HOH   HOH A . 
G 5 HOH   56  556 18  HOH   HOH A . 
G 5 HOH   57  557 172 HOH   HOH A . 
G 5 HOH   58  558 134 HOH   HOH A . 
G 5 HOH   59  559 207 HOH   HOH A . 
G 5 HOH   60  560 106 HOH   HOH A . 
G 5 HOH   61  561 25  HOH   HOH A . 
G 5 HOH   62  562 153 HOH   HOH A . 
G 5 HOH   63  563 58  HOH   HOH A . 
G 5 HOH   64  564 151 HOH   HOH A . 
G 5 HOH   65  565 120 HOH   HOH A . 
G 5 HOH   66  566 158 HOH   HOH A . 
G 5 HOH   67  567 15  HOH   HOH A . 
G 5 HOH   68  568 67  HOH   HOH A . 
G 5 HOH   69  569 198 HOH   HOH A . 
G 5 HOH   70  570 250 HOH   HOH A . 
G 5 HOH   71  571 277 HOH   HOH A . 
G 5 HOH   72  572 68  HOH   HOH A . 
G 5 HOH   73  573 324 HOH   HOH A . 
G 5 HOH   74  574 38  HOH   HOH A . 
G 5 HOH   75  575 14  HOH   HOH A . 
G 5 HOH   76  576 48  HOH   HOH A . 
G 5 HOH   77  577 9   HOH   HOH A . 
G 5 HOH   78  578 122 HOH   HOH A . 
G 5 HOH   79  579 26  HOH   HOH A . 
G 5 HOH   80  580 161 HOH   HOH A . 
G 5 HOH   81  581 60  HOH   HOH A . 
G 5 HOH   82  582 20  HOH   HOH A . 
G 5 HOH   83  583 13  HOH   HOH A . 
G 5 HOH   84  584 117 HOH   HOH A . 
G 5 HOH   85  585 236 HOH   HOH A . 
G 5 HOH   86  586 72  HOH   HOH A . 
G 5 HOH   87  587 96  HOH   HOH A . 
G 5 HOH   88  588 155 HOH   HOH A . 
G 5 HOH   89  589 184 HOH   HOH A . 
G 5 HOH   90  590 36  HOH   HOH A . 
G 5 HOH   91  591 334 HOH   HOH A . 
G 5 HOH   92  592 28  HOH   HOH A . 
G 5 HOH   93  593 173 HOH   HOH A . 
G 5 HOH   94  594 131 HOH   HOH A . 
G 5 HOH   95  595 127 HOH   HOH A . 
G 5 HOH   96  596 109 HOH   HOH A . 
G 5 HOH   97  597 276 HOH   HOH A . 
G 5 HOH   98  598 212 HOH   HOH A . 
G 5 HOH   99  599 53  HOH   HOH A . 
G 5 HOH   100 600 164 HOH   HOH A . 
G 5 HOH   101 601 87  HOH   HOH A . 
G 5 HOH   102 602 171 HOH   HOH A . 
G 5 HOH   103 603 300 HOH   HOH A . 
G 5 HOH   104 604 91  HOH   HOH A . 
G 5 HOH   105 605 27  HOH   HOH A . 
G 5 HOH   106 606 54  HOH   HOH A . 
G 5 HOH   107 607 76  HOH   HOH A . 
G 5 HOH   108 608 203 HOH   HOH A . 
G 5 HOH   109 609 34  HOH   HOH A . 
G 5 HOH   110 610 268 HOH   HOH A . 
G 5 HOH   111 611 312 HOH   HOH A . 
G 5 HOH   112 612 40  HOH   HOH A . 
G 5 HOH   113 613 255 HOH   HOH A . 
G 5 HOH   114 614 64  HOH   HOH A . 
G 5 HOH   115 615 39  HOH   HOH A . 
G 5 HOH   116 616 77  HOH   HOH A . 
G 5 HOH   117 617 156 HOH   HOH A . 
G 5 HOH   118 618 74  HOH   HOH A . 
G 5 HOH   119 619 12  HOH   HOH A . 
G 5 HOH   120 620 328 HOH   HOH A . 
G 5 HOH   121 621 132 HOH   HOH A . 
G 5 HOH   122 622 59  HOH   HOH A . 
G 5 HOH   123 623 22  HOH   HOH A . 
G 5 HOH   124 624 29  HOH   HOH A . 
G 5 HOH   125 625 194 HOH   HOH A . 
G 5 HOH   126 626 305 HOH   HOH A . 
G 5 HOH   127 627 19  HOH   HOH A . 
G 5 HOH   128 628 6   HOH   HOH A . 
G 5 HOH   129 629 292 HOH   HOH A . 
G 5 HOH   130 630 322 HOH   HOH A . 
G 5 HOH   131 631 10  HOH   HOH A . 
G 5 HOH   132 632 4   HOH   HOH A . 
G 5 HOH   133 633 3   HOH   HOH A . 
G 5 HOH   134 634 23  HOH   HOH A . 
G 5 HOH   135 635 16  HOH   HOH A . 
G 5 HOH   136 636 202 HOH   HOH A . 
G 5 HOH   137 637 112 HOH   HOH A . 
G 5 HOH   138 638 49  HOH   HOH A . 
G 5 HOH   139 639 163 HOH   HOH A . 
G 5 HOH   140 640 119 HOH   HOH A . 
G 5 HOH   141 641 5   HOH   HOH A . 
G 5 HOH   142 642 166 HOH   HOH A . 
G 5 HOH   143 643 8   HOH   HOH A . 
G 5 HOH   144 644 86  HOH   HOH A . 
G 5 HOH   145 645 229 HOH   HOH A . 
G 5 HOH   146 646 45  HOH   HOH A . 
G 5 HOH   147 647 160 HOH   HOH A . 
G 5 HOH   148 648 303 HOH   HOH A . 
G 5 HOH   149 649 246 HOH   HOH A . 
G 5 HOH   150 650 42  HOH   HOH A . 
G 5 HOH   151 651 47  HOH   HOH A . 
G 5 HOH   152 652 43  HOH   HOH A . 
G 5 HOH   153 653 11  HOH   HOH A . 
G 5 HOH   154 654 240 HOH   HOH A . 
G 5 HOH   155 655 299 HOH   HOH A . 
G 5 HOH   156 656 56  HOH   HOH A . 
G 5 HOH   157 657 2   HOH   HOH A . 
G 5 HOH   158 658 114 HOH   HOH A . 
G 5 HOH   159 659 319 HOH   HOH A . 
G 5 HOH   160 660 81  HOH   HOH A . 
G 5 HOH   161 661 281 HOH   HOH A . 
G 5 HOH   162 662 7   HOH   HOH A . 
G 5 HOH   163 663 214 HOH   HOH A . 
G 5 HOH   164 664 254 HOH   HOH A . 
G 5 HOH   165 665 219 HOH   HOH A . 
G 5 HOH   166 666 21  HOH   HOH A . 
G 5 HOH   167 667 118 HOH   HOH A . 
G 5 HOH   168 668 102 HOH   HOH A . 
G 5 HOH   169 669 17  HOH   HOH A . 
G 5 HOH   170 670 116 HOH   HOH A . 
G 5 HOH   171 671 199 HOH   HOH A . 
G 5 HOH   172 672 187 HOH   HOH A . 
G 5 HOH   173 673 80  HOH   HOH A . 
G 5 HOH   174 674 347 HOH   HOH A . 
G 5 HOH   175 675 82  HOH   HOH A . 
G 5 HOH   176 676 152 HOH   HOH A . 
G 5 HOH   177 677 137 HOH   HOH A . 
G 5 HOH   178 678 209 HOH   HOH A . 
G 5 HOH   179 679 98  HOH   HOH A . 
G 5 HOH   180 680 290 HOH   HOH A . 
G 5 HOH   181 681 206 HOH   HOH A . 
G 5 HOH   182 682 24  HOH   HOH A . 
G 5 HOH   183 683 304 HOH   HOH A . 
G 5 HOH   184 684 139 HOH   HOH A . 
G 5 HOH   185 685 142 HOH   HOH A . 
G 5 HOH   186 686 192 HOH   HOH A . 
G 5 HOH   187 687 85  HOH   HOH A . 
G 5 HOH   188 688 349 HOH   HOH A . 
G 5 HOH   189 689 185 HOH   HOH A . 
G 5 HOH   190 690 330 HOH   HOH A . 
G 5 HOH   191 691 110 HOH   HOH A . 
G 5 HOH   192 692 124 HOH   HOH A . 
G 5 HOH   193 693 1   HOH   HOH A . 
G 5 HOH   194 694 216 HOH   HOH A . 
G 5 HOH   195 695 105 HOH   HOH A . 
G 5 HOH   196 696 111 HOH   HOH A . 
G 5 HOH   197 697 204 HOH   HOH A . 
G 5 HOH   198 698 73  HOH   HOH A . 
G 5 HOH   199 699 231 HOH   HOH A . 
G 5 HOH   200 700 311 HOH   HOH A . 
G 5 HOH   201 701 217 HOH   HOH A . 
G 5 HOH   202 702 333 HOH   HOH A . 
G 5 HOH   203 703 46  HOH   HOH A . 
G 5 HOH   204 704 237 HOH   HOH A . 
G 5 HOH   205 705 93  HOH   HOH A . 
G 5 HOH   206 706 178 HOH   HOH A . 
G 5 HOH   207 707 44  HOH   HOH A . 
G 5 HOH   208 708 225 HOH   HOH A . 
G 5 HOH   209 709 63  HOH   HOH A . 
G 5 HOH   210 710 83  HOH   HOH A . 
G 5 HOH   211 711 288 HOH   HOH A . 
G 5 HOH   212 712 125 HOH   HOH A . 
G 5 HOH   213 713 90  HOH   HOH A . 
G 5 HOH   214 714 271 HOH   HOH A . 
G 5 HOH   215 715 218 HOH   HOH A . 
G 5 HOH   216 716 97  HOH   HOH A . 
G 5 HOH   217 717 69  HOH   HOH A . 
G 5 HOH   218 718 149 HOH   HOH A . 
G 5 HOH   219 719 348 HOH   HOH A . 
G 5 HOH   220 720 145 HOH   HOH A . 
G 5 HOH   221 721 128 HOH   HOH A . 
G 5 HOH   222 722 242 HOH   HOH A . 
G 5 HOH   223 723 274 HOH   HOH A . 
G 5 HOH   224 724 339 HOH   HOH A . 
G 5 HOH   225 725 179 HOH   HOH A . 
G 5 HOH   226 726 84  HOH   HOH A . 
G 5 HOH   227 727 30  HOH   HOH A . 
G 5 HOH   228 728 33  HOH   HOH A . 
G 5 HOH   229 729 175 HOH   HOH A . 
G 5 HOH   230 730 79  HOH   HOH A . 
G 5 HOH   231 731 133 HOH   HOH A . 
G 5 HOH   232 732 315 HOH   HOH A . 
G 5 HOH   233 733 104 HOH   HOH A . 
G 5 HOH   234 734 257 HOH   HOH A . 
G 5 HOH   235 735 61  HOH   HOH A . 
G 5 HOH   236 736 141 HOH   HOH A . 
G 5 HOH   237 737 150 HOH   HOH A . 
G 5 HOH   238 738 129 HOH   HOH A . 
G 5 HOH   239 739 159 HOH   HOH A . 
G 5 HOH   240 740 121 HOH   HOH A . 
G 5 HOH   241 741 308 HOH   HOH A . 
G 5 HOH   242 742 154 HOH   HOH A . 
G 5 HOH   243 743 265 HOH   HOH A . 
G 5 HOH   244 744 57  HOH   HOH A . 
G 5 HOH   245 745 249 HOH   HOH A . 
G 5 HOH   246 746 62  HOH   HOH A . 
G 5 HOH   247 747 174 HOH   HOH A . 
G 5 HOH   248 748 253 HOH   HOH A . 
G 5 HOH   249 749 291 HOH   HOH A . 
G 5 HOH   250 750 264 HOH   HOH A . 
G 5 HOH   251 751 269 HOH   HOH A . 
G 5 HOH   252 752 170 HOH   HOH A . 
G 5 HOH   253 753 294 HOH   HOH A . 
G 5 HOH   254 754 140 HOH   HOH A . 
G 5 HOH   255 755 283 HOH   HOH A . 
G 5 HOH   256 756 245 HOH   HOH A . 
G 5 HOH   257 757 310 HOH   HOH A . 
G 5 HOH   258 758 190 HOH   HOH A . 
G 5 HOH   259 759 180 HOH   HOH A . 
G 5 HOH   260 760 256 HOH   HOH A . 
G 5 HOH   261 761 186 HOH   HOH A . 
G 5 HOH   262 762 323 HOH   HOH A . 
G 5 HOH   263 763 244 HOH   HOH A . 
G 5 HOH   264 764 167 HOH   HOH A . 
G 5 HOH   265 765 101 HOH   HOH A . 
G 5 HOH   266 766 309 HOH   HOH A . 
G 5 HOH   267 767 337 HOH   HOH A . 
G 5 HOH   268 768 341 HOH   HOH A . 
G 5 HOH   269 769 318 HOH   HOH A . 
G 5 HOH   270 770 108 HOH   HOH A . 
G 5 HOH   271 771 196 HOH   HOH A . 
G 5 HOH   272 772 261 HOH   HOH A . 
G 5 HOH   273 773 342 HOH   HOH A . 
G 5 HOH   274 774 148 HOH   HOH A . 
G 5 HOH   275 775 181 HOH   HOH A . 
G 5 HOH   276 776 335 HOH   HOH A . 
G 5 HOH   277 777 182 HOH   HOH A . 
G 5 HOH   278 778 273 HOH   HOH A . 
G 5 HOH   279 779 177 HOH   HOH A . 
G 5 HOH   280 780 227 HOH   HOH A . 
G 5 HOH   281 781 344 HOH   HOH A . 
G 5 HOH   282 782 71  HOH   HOH A . 
G 5 HOH   283 783 296 HOH   HOH A . 
G 5 HOH   284 784 275 HOH   HOH A . 
G 5 HOH   285 785 353 HOH   HOH A . 
G 5 HOH   286 786 280 HOH   HOH A . 
G 5 HOH   287 787 345 HOH   HOH A . 
G 5 HOH   288 788 89  HOH   HOH A . 
G 5 HOH   289 789 201 HOH   HOH A . 
G 5 HOH   290 790 338 HOH   HOH A . 
G 5 HOH   291 791 286 HOH   HOH A . 
G 5 HOH   292 792 188 HOH   HOH A . 
G 5 HOH   293 793 208 HOH   HOH A . 
G 5 HOH   294 794 193 HOH   HOH A . 
G 5 HOH   295 795 113 HOH   HOH A . 
G 5 HOH   296 796 289 HOH   HOH A . 
G 5 HOH   297 797 331 HOH   HOH A . 
G 5 HOH   298 798 162 HOH   HOH A . 
G 5 HOH   299 799 157 HOH   HOH A . 
G 5 HOH   300 800 41  HOH   HOH A . 
G 5 HOH   301 801 327 HOH   HOH A . 
G 5 HOH   302 802 329 HOH   HOH A . 
G 5 HOH   303 803 147 HOH   HOH A . 
G 5 HOH   304 804 267 HOH   HOH A . 
G 5 HOH   305 805 295 HOH   HOH A . 
G 5 HOH   306 806 302 HOH   HOH A . 
G 5 HOH   307 807 189 HOH   HOH A . 
G 5 HOH   308 808 306 HOH   HOH A . 
G 5 HOH   309 809 95  HOH   HOH A . 
G 5 HOH   310 810 221 HOH   HOH A . 
G 5 HOH   311 811 115 HOH   HOH A . 
G 5 HOH   312 812 336 HOH   HOH A . 
G 5 HOH   313 813 224 HOH   HOH A . 
G 5 HOH   314 814 123 HOH   HOH A . 
G 5 HOH   315 815 351 HOH   HOH A . 
G 5 HOH   316 816 220 HOH   HOH A . 
G 5 HOH   317 817 266 HOH   HOH A . 
G 5 HOH   318 818 317 HOH   HOH A . 
G 5 HOH   319 819 284 HOH   HOH A . 
G 5 HOH   320 820 176 HOH   HOH A . 
G 5 HOH   321 821 270 HOH   HOH A . 
G 5 HOH   322 822 205 HOH   HOH A . 
G 5 HOH   323 823 263 HOH   HOH A . 
G 5 HOH   324 824 247 HOH   HOH A . 
G 5 HOH   325 825 301 HOH   HOH A . 
G 5 HOH   326 826 259 HOH   HOH A . 
G 5 HOH   327 827 211 HOH   HOH A . 
G 5 HOH   328 828 279 HOH   HOH A . 
G 5 HOH   329 829 100 HOH   HOH A . 
G 5 HOH   330 830 94  HOH   HOH A . 
G 5 HOH   331 831 130 HOH   HOH A . 
G 5 HOH   332 832 325 HOH   HOH A . 
G 5 HOH   333 833 258 HOH   HOH A . 
G 5 HOH   334 834 70  HOH   HOH A . 
G 5 HOH   335 835 260 HOH   HOH A . 
G 5 HOH   336 836 243 HOH   HOH A . 
G 5 HOH   337 837 195 HOH   HOH A . 
G 5 HOH   338 838 222 HOH   HOH A . 
G 5 HOH   339 839 350 HOH   HOH A . 
G 5 HOH   340 840 248 HOH   HOH A . 
G 5 HOH   341 841 197 HOH   HOH A . 
G 5 HOH   342 842 293 HOH   HOH A . 
G 5 HOH   343 843 103 HOH   HOH A . 
G 5 HOH   344 844 228 HOH   HOH A . 
G 5 HOH   345 845 352 HOH   HOH A . 
G 5 HOH   346 846 239 HOH   HOH A . 
G 5 HOH   347 847 307 HOH   HOH A . 
G 5 HOH   348 848 223 HOH   HOH A . 
# 
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  ? ? ? '(1.11.1_2575: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   111.57 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9I10 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.352 
_cell.length_a_esd                 ? 
_cell.length_b                     46.394 
_cell.length_b_esd                 ? 
_cell.length_c                     63.356 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9I10 
_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                   9I10 
_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             2.03 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.38 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '32% PEG4000, 0.2 M Lithium Sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-22 
_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   1.000 
_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                        'ELETTRA BEAMLINE 11.2C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11.2C 
_diffrn_source.pdbx_synchrotron_site       ELETTRA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9I10 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.50 
_reflns.d_resolution_low                               58.92 
_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                                     50608 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.98 
_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                                0.063 
_reflns.pdbx_Rpim_I_all                                0.025 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       322530 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.058 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.50 
_reflns_shell.d_res_low                                     1.53 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           16053 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2447 
_reflns_shell.percent_possible_obs                          100.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.6 
_reflns_shell.pdbx_chi_squared                              0.95 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.5 
_reflns_shell.pdbx_Rrim_I_all                               0.838 
_reflns_shell.pdbx_Rpim_I_all                               0.323 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.850 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.771 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9I10 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.500 
_refine.ls_d_res_low                             36.450 
_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                     50572 
_refine.ls_number_reflns_R_free                  2509 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.81 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1646 
_refine.ls_R_factor_R_free                       0.1933 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1631 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_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                 19.92 
_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                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2773 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.number_atoms_solvent             348 
_refine_hist.number_atoms_total               3164 
_refine_hist.d_res_high                       1.500 
_refine_hist.d_res_low                        36.450 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 2905 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.865  ? 3934 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.633 ? 1728 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.057  ? 404  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 502  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.5000 1.5289 . . 129 2627 100.00 . . . . 0.2295 . . . . . . . . . . . 0.2326 
'X-RAY DIFFRACTION' 1.5289 1.5601 . . 136 2685 100.00 . . . . 0.2204 . . . . . . . . . . . 0.2548 
'X-RAY DIFFRACTION' 1.5601 1.5940 . . 150 2642 100.00 . . . . 0.2136 . . . . . . . . . . . 0.3083 
'X-RAY DIFFRACTION' 1.5940 1.6311 . . 154 2637 100.00 . . . . 0.2071 . . . . . . . . . . . 0.2402 
'X-RAY DIFFRACTION' 1.6311 1.6719 . . 143 2649 100.00 . . . . 0.1906 . . . . . . . . . . . 0.2469 
'X-RAY DIFFRACTION' 1.6719 1.7171 . . 110 2704 100.00 . . . . 0.1847 . . . . . . . . . . . 0.2074 
'X-RAY DIFFRACTION' 1.7171 1.7676 . . 148 2635 100.00 . . . . 0.1760 . . . . . . . . . . . 0.2316 
'X-RAY DIFFRACTION' 1.7676 1.8246 . . 122 2666 100.00 . . . . 0.1761 . . . . . . . . . . . 0.2194 
'X-RAY DIFFRACTION' 1.8246 1.8898 . . 133 2660 100.00 . . . . 0.1704 . . . . . . . . . . . 0.2146 
'X-RAY DIFFRACTION' 1.8898 1.9655 . . 136 2689 100.00 . . . . 0.1726 . . . . . . . . . . . 0.2029 
'X-RAY DIFFRACTION' 1.9655 2.0549 . . 137 2652 100.00 . . . . 0.1662 . . . . . . . . . . . 0.1979 
'X-RAY DIFFRACTION' 2.0549 2.1633 . . 131 2672 100.00 . . . . 0.1605 . . . . . . . . . . . 0.1930 
'X-RAY DIFFRACTION' 2.1633 2.2988 . . 136 2689 100.00 . . . . 0.1607 . . . . . . . . . . . 0.1982 
'X-RAY DIFFRACTION' 2.2988 2.4762 . . 159 2638 100.00 . . . . 0.1622 . . . . . . . . . . . 0.2061 
'X-RAY DIFFRACTION' 2.4762 2.7254 . . 132 2701 100.00 . . . . 0.1713 . . . . . . . . . . . 0.1877 
'X-RAY DIFFRACTION' 2.7254 3.1195 . . 136 2692 100.00 . . . . 0.1646 . . . . . . . . . . . 0.1603 
'X-RAY DIFFRACTION' 3.1195 3.9296 . . 160 2684 100.00 . . . . 0.1396 . . . . . . . . . . . 0.1829 
'X-RAY DIFFRACTION' 3.9296 36.450 . . 157 2741 99.00  . . . . 0.1485 . . . . . . . . . . . 0.1746 
# 
_struct.entry_id                     9I10 
_struct.title                        'Human protein kinase CK2 alpha in complex with TN12' 
_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        9I10 
_struct_keywords.text            'kinase domain, transferase' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CSK21_HUMAN 
_struct_ref.pdbx_db_accession          P68400 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREI
KILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV
MIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQL
VRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHP
YFYTVVKD
;
_struct_ref.pdbx_align_begin           3 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9I10 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 328 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P68400 
_struct_ref_seq.db_align_beg                  3 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  330 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       3 
_struct_ref_seq.pdbx_auth_seq_align_end       330 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 850   ? 
1 MORE         -43   ? 
1 'SSA (A^2)'  15390 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 12  ? ARG A 17  ? ASP A 14  ARG A 19  1 ? 6  
HELX_P HELX_P2  AA2 PRO A 18  ? ASP A 23  ? PRO A 20  ASP A 25  1 ? 6  
HELX_P HELX_P3  AA3 TYR A 24  ? HIS A 27  ? TYR A 26  HIS A 29  5 ? 4  
HELX_P HELX_P4  AA4 ASN A 33  ? ASP A 35  ? ASN A 35  ASP A 37  5 ? 3  
HELX_P HELX_P5  AA5 LYS A 72  ? ARG A 87  ? LYS A 74  ARG A 89  1 ? 16 
HELX_P HELX_P6  AA6 ASP A 118 ? TYR A 123 ? ASP A 120 TYR A 125 1 ? 6  
HELX_P HELX_P7  AA7 THR A 127 ? MET A 148 ? THR A 129 MET A 150 1 ? 22 
HELX_P HELX_P8  AA8 LYS A 156 ? HIS A 158 ? LYS A 158 HIS A 160 5 ? 3  
HELX_P HELX_P9  AA9 ASP A 173 ? ALA A 177 ? ASP A 175 ALA A 179 5 ? 5  
HELX_P HELX_P10 AB1 SER A 192 ? LYS A 196 ? SER A 194 LYS A 198 5 ? 5  
HELX_P HELX_P11 AB2 GLY A 197 ? VAL A 202 ? GLY A 199 VAL A 204 1 ? 6  
HELX_P HELX_P12 AB3 TYR A 209 ? ARG A 226 ? TYR A 211 ARG A 228 1 ? 18 
HELX_P HELX_P13 AB4 ASP A 235 ? GLY A 248 ? ASP A 237 GLY A 250 1 ? 14 
HELX_P HELX_P14 AB5 GLY A 248 ? TYR A 259 ? GLY A 250 TYR A 261 1 ? 12 
HELX_P HELX_P15 AB6 ASP A 264 ? ILE A 270 ? ASP A 266 ILE A 272 5 ? 7  
HELX_P HELX_P16 AB7 ARG A 278 ? VAL A 283 ? ARG A 280 VAL A 285 5 ? 6  
HELX_P HELX_P17 AB8 ASN A 287 ? VAL A 291 ? ASN A 289 VAL A 293 5 ? 5  
HELX_P HELX_P18 AB9 SER A 292 ? LEU A 303 ? SER A 294 LEU A 305 1 ? 12 
HELX_P HELX_P19 AC1 ASP A 306 ? ARG A 310 ? ASP A 308 ARG A 312 5 ? 5  
HELX_P HELX_P20 AC2 THR A 312 ? GLU A 318 ? THR A 314 GLU A 320 1 ? 7  
HELX_P HELX_P21 AC3 HIS A 319 ? TYR A 323 ? HIS A 321 TYR A 325 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           228 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLU 
_struct_mon_prot_cis.auth_seq_id            230 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    229 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     231 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -5.73 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 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 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 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 TYR A 37  ? ARG A 45  ? TYR A 39  ARG A 47  
AA1 2 SER A 49  ? ASN A 56  ? SER A 51  ASN A 58  
AA1 3 LYS A 62  ? LEU A 68  ? LYS A 64  LEU A 70  
AA1 4 THR A 106 ? GLU A 112 ? THR A 108 GLU A 114 
AA1 5 LEU A 95  ? ASP A 101 ? LEU A 97  ASP A 103 
AA2 1 ILE A 150 ? MET A 151 ? ILE A 152 MET A 153 
AA2 2 GLU A 178 ? PHE A 179 ? GLU A 180 PHE A 181 
AA3 1 VAL A 160 ? ASP A 163 ? VAL A 162 ASP A 165 
AA3 2 LYS A 168 ? LEU A 171 ? LYS A 170 LEU A 173 
# 
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 LEU A 43  ? N LEU A 45  O VAL A 51  ? O VAL A 53  
AA1 2 3 N GLU A 50  ? N GLU A 52  O ILE A 67  ? O ILE A 69  
AA1 3 4 N VAL A 64  ? N VAL A 66  O PHE A 111 ? O PHE A 113 
AA1 4 5 O ALA A 108 ? O ALA A 110 N VAL A 99  ? N VAL A 101 
AA2 1 2 N MET A 151 ? N MET A 153 O GLU A 178 ? O GLU A 180 
AA3 1 2 N MET A 161 ? N MET A 163 O ARG A 170 ? O ARG A 172 
# 
_pdbx_entry_details.entry_id                   9I10 
_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 ASP A 156 ? ? -148.36 42.92  
2 1 ALA A 193 ? ? 63.52   157.22 
3 1 MET A 208 ? ? -93.22  57.46  
4 1 HIS A 234 ? ? -108.54 73.20  
# 
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 15.2957  -24.7131 -47.9483 0.1831 ? 0.0249  ? 0.0314  ? 0.1293 ? -0.0615 ? 0.3023 ? 0.4389 ? 
0.0370  ? -0.3412 ? -0.1913 ? -0.1013 ? 0.9761 ? -0.2249 ? 0.2156  ? -0.3366 ? -0.0336 ? 0.1470  ? -0.1716 ? 0.1514  ? 0.0296  ? 
-0.0111 ? 
2 'X-RAY DIFFRACTION' ? refined 21.7584  -13.9563 -45.9387 0.1254 ? -0.0030 ? -0.0134 ? 0.1730 ? -0.0193 ? 0.1672 ? 1.1000 ? 
0.2373  ? 0.1265  ? 0.4546  ? 0.4732  ? 0.3311 ? -0.0252 ? 0.0641  ? -0.0566 ? 0.0269  ? -0.0029 ? -0.0637 ? 0.0558  ? 0.1162  ? 
-0.0000 ? 
3 'X-RAY DIFFRACTION' ? refined 8.5451   -6.5980  -49.3656 0.1567 ? 0.0127  ? -0.0267 ? 0.1453 ? -0.0243 ? 0.1698 ? 0.5135 ? 
-0.0891 ? -0.1559 ? -0.1164 ? -0.4383 ? 0.9079 ? -0.0667 ? 0.1536  ? 0.0930  ? 0.0992  ? 0.0516  ? -0.1461 ? -0.1222 ? -0.0976 ? 
0.0024  ? 
4 'X-RAY DIFFRACTION' ? refined 3.5706   -15.5259 -42.4944 0.1431 ? 0.0051  ? -0.0063 ? 0.1134 ? -0.0215 ? 0.1359 ? 1.4475 ? 
0.1088  ? -0.5775 ? 0.2228  ? -0.1531 ? 0.3200 ? -0.0360 ? 0.0756  ? -0.0585 ? 0.0409  ? 0.0411  ? -0.0863 ? -0.0050 ? -0.0364 ? 
-0.0001 ? 
5 'X-RAY DIFFRACTION' ? refined -10.2214 -14.9973 -29.6174 0.1810 ? 0.0083  ? -0.0143 ? 0.1185 ? -0.0006 ? 0.1125 ? 0.7795 ? 
-0.2050 ? -0.3733 ? 0.3324  ? -0.1931 ? 0.6093 ? -0.0972 ? -0.1093 ? 0.0186  ? 0.1509  ? 0.0315  ? 0.0163  ? -0.0165 ? -0.0472 ? 
0.0000  ? 
6 'X-RAY DIFFRACTION' ? refined -10.3194 -8.6917  -48.8745 0.1264 ? 0.0077  ? -0.0028 ? 0.2157 ? 0.0207  ? 0.1258 ? 0.3717 ? 
-0.0691 ? -0.3430 ? 0.4609  ? -0.0813 ? 0.6554 ? 0.0047  ? 0.2434  ? 0.0095  ? 0.0355  ? 0.0353  ? 0.0446  ? -0.0289 ? -0.2689 ? 
0.0011  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 3 through 44 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 45 through 103 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 104 through 149 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 150 through 227 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 228 through 280 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 281 through 330 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       848 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.17 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
A1IYV C01  C N N 1   
A1IYV C03  C Y N 2   
A1IYV C04  C Y N 3   
A1IYV C06  C Y N 4   
A1IYV C07  C Y N 5   
A1IYV C08  C Y N 6   
A1IYV C09  C Y N 7   
A1IYV C10  C N N 8   
A1IYV C11  C N N 9   
A1IYV C13  C N N 10  
A1IYV C15  C N N 11  
A1IYV C18  C Y N 12  
A1IYV C19  C Y N 13  
A1IYV C20  C Y N 14  
A1IYV C21  C Y N 15  
A1IYV C22  C Y N 16  
A1IYV C23  C Y N 17  
A1IYV C24  C N N 18  
A1IYV N14  N N N 19  
A1IYV N17  N N N 20  
A1IYV O02  O N N 21  
A1IYV O05  O N N 22  
A1IYV O16  O N N 23  
A1IYV S12  S N N 24  
A1IYV H1   H N N 25  
A1IYV H2   H N N 26  
A1IYV H3   H N N 27  
A1IYV H4   H N N 28  
A1IYV H5   H N N 29  
A1IYV H6   H N N 30  
A1IYV H7   H N N 31  
A1IYV H9   H N N 32  
A1IYV H10  H N N 33  
A1IYV H11  H N N 34  
A1IYV H12  H N N 35  
A1IYV H13  H N N 36  
A1IYV H14  H N N 37  
A1IYV H15  H N N 38  
A1IYV H17  H N N 39  
A1IYV H8   H N N 40  
ALA   N    N N N 41  
ALA   CA   C N S 42  
ALA   C    C N N 43  
ALA   O    O N N 44  
ALA   CB   C N N 45  
ALA   OXT  O N N 46  
ALA   H    H N N 47  
ALA   H2   H N N 48  
ALA   HA   H N N 49  
ALA   HB1  H N N 50  
ALA   HB2  H N N 51  
ALA   HB3  H N N 52  
ALA   HXT  H N N 53  
ARG   N    N N N 54  
ARG   CA   C N S 55  
ARG   C    C N N 56  
ARG   O    O N N 57  
ARG   CB   C N N 58  
ARG   CG   C N N 59  
ARG   CD   C N N 60  
ARG   NE   N N N 61  
ARG   CZ   C N N 62  
ARG   NH1  N N N 63  
ARG   NH2  N N N 64  
ARG   OXT  O N N 65  
ARG   H    H N N 66  
ARG   H2   H N N 67  
ARG   HA   H N N 68  
ARG   HB2  H N N 69  
ARG   HB3  H N N 70  
ARG   HG2  H N N 71  
ARG   HG3  H N N 72  
ARG   HD2  H N N 73  
ARG   HD3  H N N 74  
ARG   HE   H N N 75  
ARG   HH11 H N N 76  
ARG   HH12 H N N 77  
ARG   HH21 H N N 78  
ARG   HH22 H N N 79  
ARG   HXT  H N N 80  
ASN   N    N N N 81  
ASN   CA   C N S 82  
ASN   C    C N N 83  
ASN   O    O N N 84  
ASN   CB   C N N 85  
ASN   CG   C N N 86  
ASN   OD1  O N N 87  
ASN   ND2  N N N 88  
ASN   OXT  O N N 89  
ASN   H    H N N 90  
ASN   H2   H N N 91  
ASN   HA   H N N 92  
ASN   HB2  H N N 93  
ASN   HB3  H N N 94  
ASN   HD21 H N N 95  
ASN   HD22 H N N 96  
ASN   HXT  H N N 97  
ASP   N    N N N 98  
ASP   CA   C N S 99  
ASP   C    C N N 100 
ASP   O    O N N 101 
ASP   CB   C N N 102 
ASP   CG   C N N 103 
ASP   OD1  O N N 104 
ASP   OD2  O N N 105 
ASP   OXT  O N N 106 
ASP   H    H N N 107 
ASP   H2   H N N 108 
ASP   HA   H N N 109 
ASP   HB2  H N N 110 
ASP   HB3  H N N 111 
ASP   HD2  H N N 112 
ASP   HXT  H N N 113 
CYS   N    N N N 114 
CYS   CA   C N R 115 
CYS   C    C N N 116 
CYS   O    O N N 117 
CYS   CB   C N N 118 
CYS   SG   S N N 119 
CYS   OXT  O N N 120 
CYS   H    H N N 121 
CYS   H2   H N N 122 
CYS   HA   H N N 123 
CYS   HB2  H N N 124 
CYS   HB3  H N N 125 
CYS   HG   H N N 126 
CYS   HXT  H N N 127 
EDO   C1   C N N 128 
EDO   O1   O N N 129 
EDO   C2   C N N 130 
EDO   O2   O N N 131 
EDO   H11  H N N 132 
EDO   H12  H N N 133 
EDO   HO1  H N N 134 
EDO   H21  H N N 135 
EDO   H22  H N N 136 
EDO   HO2  H N N 137 
GLN   N    N N N 138 
GLN   CA   C N S 139 
GLN   C    C N N 140 
GLN   O    O N N 141 
GLN   CB   C N N 142 
GLN   CG   C N N 143 
GLN   CD   C N N 144 
GLN   OE1  O N N 145 
GLN   NE2  N N N 146 
GLN   OXT  O N N 147 
GLN   H    H N N 148 
GLN   H2   H N N 149 
GLN   HA   H N N 150 
GLN   HB2  H N N 151 
GLN   HB3  H N N 152 
GLN   HG2  H N N 153 
GLN   HG3  H N N 154 
GLN   HE21 H N N 155 
GLN   HE22 H N N 156 
GLN   HXT  H N N 157 
GLU   N    N N N 158 
GLU   CA   C N S 159 
GLU   C    C N N 160 
GLU   O    O N N 161 
GLU   CB   C N N 162 
GLU   CG   C N N 163 
GLU   CD   C N N 164 
GLU   OE1  O N N 165 
GLU   OE2  O N N 166 
GLU   OXT  O N N 167 
GLU   H    H N N 168 
GLU   H2   H N N 169 
GLU   HA   H N N 170 
GLU   HB2  H N N 171 
GLU   HB3  H N N 172 
GLU   HG2  H N N 173 
GLU   HG3  H N N 174 
GLU   HE2  H N N 175 
GLU   HXT  H N N 176 
GLY   N    N N N 177 
GLY   CA   C N N 178 
GLY   C    C N N 179 
GLY   O    O N N 180 
GLY   OXT  O N N 181 
GLY   H    H N N 182 
GLY   H2   H N N 183 
GLY   HA2  H N N 184 
GLY   HA3  H N N 185 
GLY   HXT  H N N 186 
HIS   N    N N N 187 
HIS   CA   C N S 188 
HIS   C    C N N 189 
HIS   O    O N N 190 
HIS   CB   C N N 191 
HIS   CG   C Y N 192 
HIS   ND1  N Y N 193 
HIS   CD2  C Y N 194 
HIS   CE1  C Y N 195 
HIS   NE2  N Y N 196 
HIS   OXT  O N N 197 
HIS   H    H N N 198 
HIS   H2   H N N 199 
HIS   HA   H N N 200 
HIS   HB2  H N N 201 
HIS   HB3  H N N 202 
HIS   HD1  H N N 203 
HIS   HD2  H N N 204 
HIS   HE1  H N N 205 
HIS   HE2  H N N 206 
HIS   HXT  H N N 207 
HOH   O    O N N 208 
HOH   H1   H N N 209 
HOH   H2   H N N 210 
ILE   N    N N N 211 
ILE   CA   C N S 212 
ILE   C    C N N 213 
ILE   O    O N N 214 
ILE   CB   C N S 215 
ILE   CG1  C N N 216 
ILE   CG2  C N N 217 
ILE   CD1  C N N 218 
ILE   OXT  O N N 219 
ILE   H    H N N 220 
ILE   H2   H N N 221 
ILE   HA   H N N 222 
ILE   HB   H N N 223 
ILE   HG12 H N N 224 
ILE   HG13 H N N 225 
ILE   HG21 H N N 226 
ILE   HG22 H N N 227 
ILE   HG23 H N N 228 
ILE   HD11 H N N 229 
ILE   HD12 H N N 230 
ILE   HD13 H N N 231 
ILE   HXT  H N N 232 
LEU   N    N N N 233 
LEU   CA   C N S 234 
LEU   C    C N N 235 
LEU   O    O N N 236 
LEU   CB   C N N 237 
LEU   CG   C N N 238 
LEU   CD1  C N N 239 
LEU   CD2  C N N 240 
LEU   OXT  O N N 241 
LEU   H    H N N 242 
LEU   H2   H N N 243 
LEU   HA   H N N 244 
LEU   HB2  H N N 245 
LEU   HB3  H N N 246 
LEU   HG   H N N 247 
LEU   HD11 H N N 248 
LEU   HD12 H N N 249 
LEU   HD13 H N N 250 
LEU   HD21 H N N 251 
LEU   HD22 H N N 252 
LEU   HD23 H N N 253 
LEU   HXT  H N N 254 
LYS   N    N N N 255 
LYS   CA   C N S 256 
LYS   C    C N N 257 
LYS   O    O N N 258 
LYS   CB   C N N 259 
LYS   CG   C N N 260 
LYS   CD   C N N 261 
LYS   CE   C N N 262 
LYS   NZ   N N N 263 
LYS   OXT  O N N 264 
LYS   H    H N N 265 
LYS   H2   H N N 266 
LYS   HA   H N N 267 
LYS   HB2  H N N 268 
LYS   HB3  H N N 269 
LYS   HG2  H N N 270 
LYS   HG3  H N N 271 
LYS   HD2  H N N 272 
LYS   HD3  H N N 273 
LYS   HE2  H N N 274 
LYS   HE3  H N N 275 
LYS   HZ1  H N N 276 
LYS   HZ2  H N N 277 
LYS   HZ3  H N N 278 
LYS   HXT  H N N 279 
MET   N    N N N 280 
MET   CA   C N S 281 
MET   C    C N N 282 
MET   O    O N N 283 
MET   CB   C N N 284 
MET   CG   C N N 285 
MET   SD   S N N 286 
MET   CE   C N N 287 
MET   OXT  O N N 288 
MET   H    H N N 289 
MET   H2   H N N 290 
MET   HA   H N N 291 
MET   HB2  H N N 292 
MET   HB3  H N N 293 
MET   HG2  H N N 294 
MET   HG3  H N N 295 
MET   HE1  H N N 296 
MET   HE2  H N N 297 
MET   HE3  H N N 298 
MET   HXT  H N N 299 
PHE   N    N N N 300 
PHE   CA   C N S 301 
PHE   C    C N N 302 
PHE   O    O N N 303 
PHE   CB   C N N 304 
PHE   CG   C Y N 305 
PHE   CD1  C Y N 306 
PHE   CD2  C Y N 307 
PHE   CE1  C Y N 308 
PHE   CE2  C Y N 309 
PHE   CZ   C Y N 310 
PHE   OXT  O N N 311 
PHE   H    H N N 312 
PHE   H2   H N N 313 
PHE   HA   H N N 314 
PHE   HB2  H N N 315 
PHE   HB3  H N N 316 
PHE   HD1  H N N 317 
PHE   HD2  H N N 318 
PHE   HE1  H N N 319 
PHE   HE2  H N N 320 
PHE   HZ   H N N 321 
PHE   HXT  H N N 322 
PRO   N    N N N 323 
PRO   CA   C N S 324 
PRO   C    C N N 325 
PRO   O    O N N 326 
PRO   CB   C N N 327 
PRO   CG   C N N 328 
PRO   CD   C N N 329 
PRO   OXT  O N N 330 
PRO   H    H N N 331 
PRO   HA   H N N 332 
PRO   HB2  H N N 333 
PRO   HB3  H N N 334 
PRO   HG2  H N N 335 
PRO   HG3  H N N 336 
PRO   HD2  H N N 337 
PRO   HD3  H N N 338 
PRO   HXT  H N N 339 
SER   N    N N N 340 
SER   CA   C N S 341 
SER   C    C N N 342 
SER   O    O N N 343 
SER   CB   C N N 344 
SER   OG   O N N 345 
SER   OXT  O N N 346 
SER   H    H N N 347 
SER   H2   H N N 348 
SER   HA   H N N 349 
SER   HB2  H N N 350 
SER   HB3  H N N 351 
SER   HG   H N N 352 
SER   HXT  H N N 353 
SO4   S    S N N 354 
SO4   O1   O N N 355 
SO4   O2   O N N 356 
SO4   O3   O N N 357 
SO4   O4   O N N 358 
THR   N    N N N 359 
THR   CA   C N S 360 
THR   C    C N N 361 
THR   O    O N N 362 
THR   CB   C N R 363 
THR   OG1  O N N 364 
THR   CG2  C N N 365 
THR   OXT  O N N 366 
THR   H    H N N 367 
THR   H2   H N N 368 
THR   HA   H N N 369 
THR   HB   H N N 370 
THR   HG1  H N N 371 
THR   HG21 H N N 372 
THR   HG22 H N N 373 
THR   HG23 H N N 374 
THR   HXT  H N N 375 
TRP   N    N N N 376 
TRP   CA   C N S 377 
TRP   C    C N N 378 
TRP   O    O N N 379 
TRP   CB   C N N 380 
TRP   CG   C Y N 381 
TRP   CD1  C Y N 382 
TRP   CD2  C Y N 383 
TRP   NE1  N Y N 384 
TRP   CE2  C Y N 385 
TRP   CE3  C Y N 386 
TRP   CZ2  C Y N 387 
TRP   CZ3  C Y N 388 
TRP   CH2  C Y N 389 
TRP   OXT  O N N 390 
TRP   H    H N N 391 
TRP   H2   H N N 392 
TRP   HA   H N N 393 
TRP   HB2  H N N 394 
TRP   HB3  H N N 395 
TRP   HD1  H N N 396 
TRP   HE1  H N N 397 
TRP   HE3  H N N 398 
TRP   HZ2  H N N 399 
TRP   HZ3  H N N 400 
TRP   HH2  H N N 401 
TRP   HXT  H N N 402 
TYR   N    N N N 403 
TYR   CA   C N S 404 
TYR   C    C N N 405 
TYR   O    O N N 406 
TYR   CB   C N N 407 
TYR   CG   C Y N 408 
TYR   CD1  C Y N 409 
TYR   CD2  C Y N 410 
TYR   CE1  C Y N 411 
TYR   CE2  C Y N 412 
TYR   CZ   C Y N 413 
TYR   OH   O N N 414 
TYR   OXT  O N N 415 
TYR   H    H N N 416 
TYR   H2   H N N 417 
TYR   HA   H N N 418 
TYR   HB2  H N N 419 
TYR   HB3  H N N 420 
TYR   HD1  H N N 421 
TYR   HD2  H N N 422 
TYR   HE1  H N N 423 
TYR   HE2  H N N 424 
TYR   HH   H N N 425 
TYR   HXT  H N N 426 
VAL   N    N N N 427 
VAL   CA   C N S 428 
VAL   C    C N N 429 
VAL   O    O N N 430 
VAL   CB   C N N 431 
VAL   CG1  C N N 432 
VAL   CG2  C N N 433 
VAL   OXT  O N N 434 
VAL   H    H N N 435 
VAL   H2   H N N 436 
VAL   HA   H N N 437 
VAL   HB   H N N 438 
VAL   HG11 H N N 439 
VAL   HG12 H N N 440 
VAL   HG13 H N N 441 
VAL   HG21 H N N 442 
VAL   HG22 H N N 443 
VAL   HG23 H N N 444 
VAL   HXT  H N N 445 
# 
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 
A1IYV O05 C04  sing N N 1   
A1IYV C04 C06  doub Y N 2   
A1IYV C04 C03  sing Y N 3   
A1IYV O02 C03  sing N N 4   
A1IYV O02 C01  sing N N 5   
A1IYV C06 C07  sing Y N 6   
A1IYV C03 C09  doub Y N 7   
A1IYV C07 C10  sing N N 8   
A1IYV C07 C08  doub Y N 9   
A1IYV C09 C08  sing Y N 10  
A1IYV C10 C11  doub N Z 11  
A1IYV O16 C15  doub N N 12  
A1IYV C11 C15  sing N N 13  
A1IYV C11 S12  sing N N 14  
A1IYV C15 N14  sing N N 15  
A1IYV S12 C13  sing N N 16  
A1IYV N14 C13  sing N N 17  
A1IYV C13 N17  doub N N 18  
A1IYV N17 C18  sing N N 19  
A1IYV C23 C18  doub Y N 20  
A1IYV C23 C22  sing Y N 21  
A1IYV C18 C19  sing Y N 22  
A1IYV C22 C21  doub Y N 23  
A1IYV C19 C20  doub Y N 24  
A1IYV C21 C20  sing Y N 25  
A1IYV C20 C24  sing N N 26  
A1IYV C01 H1   sing N N 27  
A1IYV C01 H2   sing N N 28  
A1IYV C01 H3   sing N N 29  
A1IYV C06 H4   sing N N 30  
A1IYV C08 H5   sing N N 31  
A1IYV C09 H6   sing N N 32  
A1IYV C10 H7   sing N N 33  
A1IYV C19 H9   sing N N 34  
A1IYV C21 H10  sing N N 35  
A1IYV C22 H11  sing N N 36  
A1IYV C23 H12  sing N N 37  
A1IYV C24 H13  sing N N 38  
A1IYV C24 H14  sing N N 39  
A1IYV C24 H15  sing N N 40  
A1IYV O05 H17  sing N N 41  
A1IYV N14 H8   sing N N 42  
ALA   N   CA   sing N N 43  
ALA   N   H    sing N N 44  
ALA   N   H2   sing N N 45  
ALA   CA  C    sing N N 46  
ALA   CA  CB   sing N N 47  
ALA   CA  HA   sing N N 48  
ALA   C   O    doub N N 49  
ALA   C   OXT  sing N N 50  
ALA   CB  HB1  sing N N 51  
ALA   CB  HB2  sing N N 52  
ALA   CB  HB3  sing N N 53  
ALA   OXT HXT  sing N N 54  
ARG   N   CA   sing N N 55  
ARG   N   H    sing N N 56  
ARG   N   H2   sing N N 57  
ARG   CA  C    sing N N 58  
ARG   CA  CB   sing N N 59  
ARG   CA  HA   sing N N 60  
ARG   C   O    doub N N 61  
ARG   C   OXT  sing N N 62  
ARG   CB  CG   sing N N 63  
ARG   CB  HB2  sing N N 64  
ARG   CB  HB3  sing N N 65  
ARG   CG  CD   sing N N 66  
ARG   CG  HG2  sing N N 67  
ARG   CG  HG3  sing N N 68  
ARG   CD  NE   sing N N 69  
ARG   CD  HD2  sing N N 70  
ARG   CD  HD3  sing N N 71  
ARG   NE  CZ   sing N N 72  
ARG   NE  HE   sing N N 73  
ARG   CZ  NH1  sing N N 74  
ARG   CZ  NH2  doub N N 75  
ARG   NH1 HH11 sing N N 76  
ARG   NH1 HH12 sing N N 77  
ARG   NH2 HH21 sing N N 78  
ARG   NH2 HH22 sing N N 79  
ARG   OXT HXT  sing N N 80  
ASN   N   CA   sing N N 81  
ASN   N   H    sing N N 82  
ASN   N   H2   sing N N 83  
ASN   CA  C    sing N N 84  
ASN   CA  CB   sing N N 85  
ASN   CA  HA   sing N N 86  
ASN   C   O    doub N N 87  
ASN   C   OXT  sing N N 88  
ASN   CB  CG   sing N N 89  
ASN   CB  HB2  sing N N 90  
ASN   CB  HB3  sing N N 91  
ASN   CG  OD1  doub N N 92  
ASN   CG  ND2  sing N N 93  
ASN   ND2 HD21 sing N N 94  
ASN   ND2 HD22 sing N N 95  
ASN   OXT HXT  sing N N 96  
ASP   N   CA   sing N N 97  
ASP   N   H    sing N N 98  
ASP   N   H2   sing N N 99  
ASP   CA  C    sing N N 100 
ASP   CA  CB   sing N N 101 
ASP   CA  HA   sing N N 102 
ASP   C   O    doub N N 103 
ASP   C   OXT  sing N N 104 
ASP   CB  CG   sing N N 105 
ASP   CB  HB2  sing N N 106 
ASP   CB  HB3  sing N N 107 
ASP   CG  OD1  doub N N 108 
ASP   CG  OD2  sing N N 109 
ASP   OD2 HD2  sing N N 110 
ASP   OXT HXT  sing N N 111 
CYS   N   CA   sing N N 112 
CYS   N   H    sing N N 113 
CYS   N   H2   sing N N 114 
CYS   CA  C    sing N N 115 
CYS   CA  CB   sing N N 116 
CYS   CA  HA   sing N N 117 
CYS   C   O    doub N N 118 
CYS   C   OXT  sing N N 119 
CYS   CB  SG   sing N N 120 
CYS   CB  HB2  sing N N 121 
CYS   CB  HB3  sing N N 122 
CYS   SG  HG   sing N N 123 
CYS   OXT HXT  sing N N 124 
EDO   C1  O1   sing N N 125 
EDO   C1  C2   sing N N 126 
EDO   C1  H11  sing N N 127 
EDO   C1  H12  sing N N 128 
EDO   O1  HO1  sing N N 129 
EDO   C2  O2   sing N N 130 
EDO   C2  H21  sing N N 131 
EDO   C2  H22  sing N N 132 
EDO   O2  HO2  sing N N 133 
GLN   N   CA   sing N N 134 
GLN   N   H    sing N N 135 
GLN   N   H2   sing N N 136 
GLN   CA  C    sing N N 137 
GLN   CA  CB   sing N N 138 
GLN   CA  HA   sing N N 139 
GLN   C   O    doub N N 140 
GLN   C   OXT  sing N N 141 
GLN   CB  CG   sing N N 142 
GLN   CB  HB2  sing N N 143 
GLN   CB  HB3  sing N N 144 
GLN   CG  CD   sing N N 145 
GLN   CG  HG2  sing N N 146 
GLN   CG  HG3  sing N N 147 
GLN   CD  OE1  doub N N 148 
GLN   CD  NE2  sing N N 149 
GLN   NE2 HE21 sing N N 150 
GLN   NE2 HE22 sing N N 151 
GLN   OXT HXT  sing N N 152 
GLU   N   CA   sing N N 153 
GLU   N   H    sing N N 154 
GLU   N   H2   sing N N 155 
GLU   CA  C    sing N N 156 
GLU   CA  CB   sing N N 157 
GLU   CA  HA   sing N N 158 
GLU   C   O    doub N N 159 
GLU   C   OXT  sing N N 160 
GLU   CB  CG   sing N N 161 
GLU   CB  HB2  sing N N 162 
GLU   CB  HB3  sing N N 163 
GLU   CG  CD   sing N N 164 
GLU   CG  HG2  sing N N 165 
GLU   CG  HG3  sing N N 166 
GLU   CD  OE1  doub N N 167 
GLU   CD  OE2  sing N N 168 
GLU   OE2 HE2  sing N N 169 
GLU   OXT HXT  sing N N 170 
GLY   N   CA   sing N N 171 
GLY   N   H    sing N N 172 
GLY   N   H2   sing N N 173 
GLY   CA  C    sing N N 174 
GLY   CA  HA2  sing N N 175 
GLY   CA  HA3  sing N N 176 
GLY   C   O    doub N N 177 
GLY   C   OXT  sing N N 178 
GLY   OXT HXT  sing N N 179 
HIS   N   CA   sing N N 180 
HIS   N   H    sing N N 181 
HIS   N   H2   sing N N 182 
HIS   CA  C    sing N N 183 
HIS   CA  CB   sing N N 184 
HIS   CA  HA   sing N N 185 
HIS   C   O    doub N N 186 
HIS   C   OXT  sing N N 187 
HIS   CB  CG   sing N N 188 
HIS   CB  HB2  sing N N 189 
HIS   CB  HB3  sing N N 190 
HIS   CG  ND1  sing Y N 191 
HIS   CG  CD2  doub Y N 192 
HIS   ND1 CE1  doub Y N 193 
HIS   ND1 HD1  sing N N 194 
HIS   CD2 NE2  sing Y N 195 
HIS   CD2 HD2  sing N N 196 
HIS   CE1 NE2  sing Y N 197 
HIS   CE1 HE1  sing N N 198 
HIS   NE2 HE2  sing N N 199 
HIS   OXT HXT  sing N N 200 
HOH   O   H1   sing N N 201 
HOH   O   H2   sing N N 202 
ILE   N   CA   sing N N 203 
ILE   N   H    sing N N 204 
ILE   N   H2   sing N N 205 
ILE   CA  C    sing N N 206 
ILE   CA  CB   sing N N 207 
ILE   CA  HA   sing N N 208 
ILE   C   O    doub N N 209 
ILE   C   OXT  sing N N 210 
ILE   CB  CG1  sing N N 211 
ILE   CB  CG2  sing N N 212 
ILE   CB  HB   sing N N 213 
ILE   CG1 CD1  sing N N 214 
ILE   CG1 HG12 sing N N 215 
ILE   CG1 HG13 sing N N 216 
ILE   CG2 HG21 sing N N 217 
ILE   CG2 HG22 sing N N 218 
ILE   CG2 HG23 sing N N 219 
ILE   CD1 HD11 sing N N 220 
ILE   CD1 HD12 sing N N 221 
ILE   CD1 HD13 sing N N 222 
ILE   OXT HXT  sing N N 223 
LEU   N   CA   sing N N 224 
LEU   N   H    sing N N 225 
LEU   N   H2   sing N N 226 
LEU   CA  C    sing N N 227 
LEU   CA  CB   sing N N 228 
LEU   CA  HA   sing N N 229 
LEU   C   O    doub N N 230 
LEU   C   OXT  sing N N 231 
LEU   CB  CG   sing N N 232 
LEU   CB  HB2  sing N N 233 
LEU   CB  HB3  sing N N 234 
LEU   CG  CD1  sing N N 235 
LEU   CG  CD2  sing N N 236 
LEU   CG  HG   sing N N 237 
LEU   CD1 HD11 sing N N 238 
LEU   CD1 HD12 sing N N 239 
LEU   CD1 HD13 sing N N 240 
LEU   CD2 HD21 sing N N 241 
LEU   CD2 HD22 sing N N 242 
LEU   CD2 HD23 sing N N 243 
LEU   OXT HXT  sing N N 244 
LYS   N   CA   sing N N 245 
LYS   N   H    sing N N 246 
LYS   N   H2   sing N N 247 
LYS   CA  C    sing N N 248 
LYS   CA  CB   sing N N 249 
LYS   CA  HA   sing N N 250 
LYS   C   O    doub N N 251 
LYS   C   OXT  sing N N 252 
LYS   CB  CG   sing N N 253 
LYS   CB  HB2  sing N N 254 
LYS   CB  HB3  sing N N 255 
LYS   CG  CD   sing N N 256 
LYS   CG  HG2  sing N N 257 
LYS   CG  HG3  sing N N 258 
LYS   CD  CE   sing N N 259 
LYS   CD  HD2  sing N N 260 
LYS   CD  HD3  sing N N 261 
LYS   CE  NZ   sing N N 262 
LYS   CE  HE2  sing N N 263 
LYS   CE  HE3  sing N N 264 
LYS   NZ  HZ1  sing N N 265 
LYS   NZ  HZ2  sing N N 266 
LYS   NZ  HZ3  sing N N 267 
LYS   OXT HXT  sing N N 268 
MET   N   CA   sing N N 269 
MET   N   H    sing N N 270 
MET   N   H2   sing N N 271 
MET   CA  C    sing N N 272 
MET   CA  CB   sing N N 273 
MET   CA  HA   sing N N 274 
MET   C   O    doub N N 275 
MET   C   OXT  sing N N 276 
MET   CB  CG   sing N N 277 
MET   CB  HB2  sing N N 278 
MET   CB  HB3  sing N N 279 
MET   CG  SD   sing N N 280 
MET   CG  HG2  sing N N 281 
MET   CG  HG3  sing N N 282 
MET   SD  CE   sing N N 283 
MET   CE  HE1  sing N N 284 
MET   CE  HE2  sing N N 285 
MET   CE  HE3  sing N N 286 
MET   OXT HXT  sing N N 287 
PHE   N   CA   sing N N 288 
PHE   N   H    sing N N 289 
PHE   N   H2   sing N N 290 
PHE   CA  C    sing N N 291 
PHE   CA  CB   sing N N 292 
PHE   CA  HA   sing N N 293 
PHE   C   O    doub N N 294 
PHE   C   OXT  sing N N 295 
PHE   CB  CG   sing N N 296 
PHE   CB  HB2  sing N N 297 
PHE   CB  HB3  sing N N 298 
PHE   CG  CD1  doub Y N 299 
PHE   CG  CD2  sing Y N 300 
PHE   CD1 CE1  sing Y N 301 
PHE   CD1 HD1  sing N N 302 
PHE   CD2 CE2  doub Y N 303 
PHE   CD2 HD2  sing N N 304 
PHE   CE1 CZ   doub Y N 305 
PHE   CE1 HE1  sing N N 306 
PHE   CE2 CZ   sing Y N 307 
PHE   CE2 HE2  sing N N 308 
PHE   CZ  HZ   sing N N 309 
PHE   OXT HXT  sing N N 310 
PRO   N   CA   sing N N 311 
PRO   N   CD   sing N N 312 
PRO   N   H    sing N N 313 
PRO   CA  C    sing N N 314 
PRO   CA  CB   sing N N 315 
PRO   CA  HA   sing N N 316 
PRO   C   O    doub N N 317 
PRO   C   OXT  sing N N 318 
PRO   CB  CG   sing N N 319 
PRO   CB  HB2  sing N N 320 
PRO   CB  HB3  sing N N 321 
PRO   CG  CD   sing N N 322 
PRO   CG  HG2  sing N N 323 
PRO   CG  HG3  sing N N 324 
PRO   CD  HD2  sing N N 325 
PRO   CD  HD3  sing N N 326 
PRO   OXT HXT  sing N N 327 
SER   N   CA   sing N N 328 
SER   N   H    sing N N 329 
SER   N   H2   sing N N 330 
SER   CA  C    sing N N 331 
SER   CA  CB   sing N N 332 
SER   CA  HA   sing N N 333 
SER   C   O    doub N N 334 
SER   C   OXT  sing N N 335 
SER   CB  OG   sing N N 336 
SER   CB  HB2  sing N N 337 
SER   CB  HB3  sing N N 338 
SER   OG  HG   sing N N 339 
SER   OXT HXT  sing N N 340 
SO4   S   O1   doub N N 341 
SO4   S   O2   doub N N 342 
SO4   S   O3   sing N N 343 
SO4   S   O4   sing N N 344 
THR   N   CA   sing N N 345 
THR   N   H    sing N N 346 
THR   N   H2   sing N N 347 
THR   CA  C    sing N N 348 
THR   CA  CB   sing N N 349 
THR   CA  HA   sing N N 350 
THR   C   O    doub N N 351 
THR   C   OXT  sing N N 352 
THR   CB  OG1  sing N N 353 
THR   CB  CG2  sing N N 354 
THR   CB  HB   sing N N 355 
THR   OG1 HG1  sing N N 356 
THR   CG2 HG21 sing N N 357 
THR   CG2 HG22 sing N N 358 
THR   CG2 HG23 sing N N 359 
THR   OXT HXT  sing N N 360 
TRP   N   CA   sing N N 361 
TRP   N   H    sing N N 362 
TRP   N   H2   sing N N 363 
TRP   CA  C    sing N N 364 
TRP   CA  CB   sing N N 365 
TRP   CA  HA   sing N N 366 
TRP   C   O    doub N N 367 
TRP   C   OXT  sing N N 368 
TRP   CB  CG   sing N N 369 
TRP   CB  HB2  sing N N 370 
TRP   CB  HB3  sing N N 371 
TRP   CG  CD1  doub Y N 372 
TRP   CG  CD2  sing Y N 373 
TRP   CD1 NE1  sing Y N 374 
TRP   CD1 HD1  sing N N 375 
TRP   CD2 CE2  doub Y N 376 
TRP   CD2 CE3  sing Y N 377 
TRP   NE1 CE2  sing Y N 378 
TRP   NE1 HE1  sing N N 379 
TRP   CE2 CZ2  sing Y N 380 
TRP   CE3 CZ3  doub Y N 381 
TRP   CE3 HE3  sing N N 382 
TRP   CZ2 CH2  doub Y N 383 
TRP   CZ2 HZ2  sing N N 384 
TRP   CZ3 CH2  sing Y N 385 
TRP   CZ3 HZ3  sing N N 386 
TRP   CH2 HH2  sing N N 387 
TRP   OXT HXT  sing N N 388 
TYR   N   CA   sing N N 389 
TYR   N   H    sing N N 390 
TYR   N   H2   sing N N 391 
TYR   CA  C    sing N N 392 
TYR   CA  CB   sing N N 393 
TYR   CA  HA   sing N N 394 
TYR   C   O    doub N N 395 
TYR   C   OXT  sing N N 396 
TYR   CB  CG   sing N N 397 
TYR   CB  HB2  sing N N 398 
TYR   CB  HB3  sing N N 399 
TYR   CG  CD1  doub Y N 400 
TYR   CG  CD2  sing Y N 401 
TYR   CD1 CE1  sing Y N 402 
TYR   CD1 HD1  sing N N 403 
TYR   CD2 CE2  doub Y N 404 
TYR   CD2 HD2  sing N N 405 
TYR   CE1 CZ   doub Y N 406 
TYR   CE1 HE1  sing N N 407 
TYR   CE2 CZ   sing Y N 408 
TYR   CE2 HE2  sing N N 409 
TYR   CZ  OH   sing N N 410 
TYR   OH  HH   sing N N 411 
TYR   OXT HXT  sing N N 412 
VAL   N   CA   sing N N 413 
VAL   N   H    sing N N 414 
VAL   N   H2   sing N N 415 
VAL   CA  C    sing N N 416 
VAL   CA  CB   sing N N 417 
VAL   CA  HA   sing N N 418 
VAL   C   O    doub N N 419 
VAL   C   OXT  sing N N 420 
VAL   CB  CG1  sing N N 421 
VAL   CB  CG2  sing N N 422 
VAL   CB  HB   sing N N 423 
VAL   CG1 HG11 sing N N 424 
VAL   CG1 HG12 sing N N 425 
VAL   CG1 HG13 sing N N 426 
VAL   CG2 HG21 sing N N 427 
VAL   CG2 HG22 sing N N 428 
VAL   CG2 HG23 sing N N 429 
VAL   OXT HXT  sing N N 430 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           'PoC Road to Market 2023' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3Q04 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9I10 
_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]   0.017137 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006776 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021555 
_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]   0.016973 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLY   A 1 1   ? -7.438  -37.234 -28.769 1.00 39.85 ? 3   GLY   A N   1 
ATOM   2    C CA  . GLY   A 1 1   ? -6.473  -36.241 -29.213 1.00 38.12 ? 3   GLY   A CA  1 
ATOM   3    C C   . GLY   A 1 1   ? -7.001  -35.345 -30.316 1.00 39.30 ? 3   GLY   A C   1 
ATOM   4    O O   . GLY   A 1 1   ? -8.172  -35.436 -30.683 1.00 39.31 ? 3   GLY   A O   1 
ATOM   5    N N   . PRO   A 1 2   ? -6.142  -34.480 -30.854 1.00 39.93 ? 4   PRO   A N   1 
ATOM   6    C CA  . PRO   A 1 2   ? -6.596  -33.542 -31.884 1.00 29.89 ? 4   PRO   A CA  1 
ATOM   7    C C   . PRO   A 1 2   ? -6.848  -34.248 -33.204 1.00 29.42 ? 4   PRO   A C   1 
ATOM   8    O O   . PRO   A 1 2   ? -6.172  -35.215 -33.565 1.00 32.56 ? 4   PRO   A O   1 
ATOM   9    C CB  . PRO   A 1 2   ? -5.435  -32.544 -32.009 1.00 33.15 ? 4   PRO   A CB  1 
ATOM   10   C CG  . PRO   A 1 2   ? -4.418  -32.943 -30.958 1.00 37.70 ? 4   PRO   A CG  1 
ATOM   11   C CD  . PRO   A 1 2   ? -4.695  -34.372 -30.612 1.00 38.14 ? 4   PRO   A CD  1 
ATOM   12   N N   . VAL   A 1 3   ? -7.833  -33.740 -33.928 1.00 23.25 ? 5   VAL   A N   1 
ATOM   13   C CA  . VAL   A 1 3   ? -8.136  -34.232 -35.277 1.00 24.29 ? 5   VAL   A CA  1 
ATOM   14   C C   . VAL   A 1 3   ? -7.053  -33.752 -36.233 1.00 19.91 ? 5   VAL   A C   1 
ATOM   15   O O   . VAL   A 1 3   ? -6.654  -32.577 -36.164 1.00 20.42 ? 5   VAL   A O   1 
ATOM   16   C CB  . VAL   A 1 3   ? -9.519  -33.734 -35.709 1.00 22.50 ? 5   VAL   A CB  1 
ATOM   17   C CG1 . VAL   A 1 3   ? -9.783  -33.979 -37.184 1.00 21.39 ? 5   VAL   A CG1 1 
ATOM   18   C CG2 . VAL   A 1 3   ? -10.603 -34.383 -34.850 1.00 28.27 ? 5   VAL   A CG2 1 
ATOM   19   N N   . PRO   A 1 4   ? -6.557  -34.592 -37.138 1.00 18.05 ? 6   PRO   A N   1 
ATOM   20   C CA  . PRO   A 1 4   ? -5.509  -34.146 -38.070 1.00 17.39 ? 6   PRO   A CA  1 
ATOM   21   C C   . PRO   A 1 4   ? -6.058  -33.212 -39.141 1.00 18.26 ? 6   PRO   A C   1 
ATOM   22   O O   . PRO   A 1 4   ? -7.266  -33.070 -39.333 1.00 20.87 ? 6   PRO   A O   1 
ATOM   23   C CB  . PRO   A 1 4   ? -4.988  -35.451 -38.678 1.00 20.67 ? 6   PRO   A CB  1 
ATOM   24   C CG  . PRO   A 1 4   ? -6.137  -36.411 -38.550 1.00 23.27 ? 6   PRO   A CG  1 
ATOM   25   C CD  . PRO   A 1 4   ? -6.864  -36.030 -37.276 1.00 22.19 ? 6   PRO   A CD  1 
ATOM   26   N N   . SER   A 1 5   ? -5.129  -32.549 -39.834 1.00 18.35 ? 7   SER   A N   1 
ATOM   27   C CA  . SER   A 1 5   ? -5.440  -31.576 -40.872 1.00 17.68 ? 7   SER   A CA  1 
ATOM   28   C C   . SER   A 1 5   ? -4.424  -31.708 -41.998 1.00 16.69 ? 7   SER   A C   1 
ATOM   29   O O   . SER   A 1 5   ? -3.280  -32.090 -41.756 1.00 20.79 ? 7   SER   A O   1 
ATOM   30   C CB  . SER   A 1 5   ? -5.410  -30.142 -40.309 1.00 16.51 ? 7   SER   A CB  1 
ATOM   31   O OG  . SER   A 1 5   ? -5.654  -29.181 -41.314 1.00 17.83 ? 7   SER   A OG  1 
ATOM   32   N N   . ARG   A 1 6   ? -4.856  -31.389 -43.225 1.00 19.39 ? 8   ARG   A N   1 
ATOM   33   C CA  . ARG   A 1 6   ? -4.006  -31.320 -44.416 1.00 18.32 ? 8   ARG   A CA  1 
ATOM   34   C C   . ARG   A 1 6   ? -4.237  -29.998 -45.131 1.00 20.16 ? 8   ARG   A C   1 
ATOM   35   O O   . ARG   A 1 6   ? -5.362  -29.483 -45.139 1.00 18.48 ? 8   ARG   A O   1 
ATOM   36   C CB  . ARG   A 1 6   ? -4.336  -32.437 -45.434 1.00 23.65 ? 8   ARG   A CB  1 
ATOM   37   C CG  . ARG   A 1 6   ? -4.064  -33.825 -44.979 1.00 29.05 ? 8   ARG   A CG  1 
ATOM   38   C CD  . ARG   A 1 6   ? -2.579  -33.990 -44.774 1.00 31.42 ? 8   ARG   A CD  1 
ATOM   39   N NE  . ARG   A 1 6   ? -2.233  -35.364 -44.437 1.00 34.74 ? 8   ARG   A NE  1 
ATOM   40   C CZ  . ARG   A 1 6   ? -2.301  -35.871 -43.212 1.00 35.63 ? 8   ARG   A CZ  1 
ATOM   41   N NH1 . ARG   A 1 6   ? -2.722  -35.125 -42.185 1.00 25.60 ? 8   ARG   A NH1 1 
ATOM   42   N NH2 . ARG   A 1 6   ? -1.958  -37.131 -43.018 1.00 35.74 ? 8   ARG   A NH2 1 
ATOM   43   N N   . ALA   A 1 7   ? -3.189  -29.471 -45.768 1.00 18.37 ? 9   ALA   A N   1 
ATOM   44   C CA  . ALA   A 1 7   ? -3.376  -28.379 -46.719 1.00 16.82 ? 9   ALA   A CA  1 
ATOM   45   C C   . ALA   A 1 7   ? -4.337  -28.805 -47.823 1.00 18.29 ? 9   ALA   A C   1 
ATOM   46   O O   . ALA   A 1 7   ? -4.325  -29.956 -48.268 1.00 23.29 ? 9   ALA   A O   1 
ATOM   47   C CB  . ALA   A 1 7   ? -2.039  -27.956 -47.339 1.00 16.52 ? 9   ALA   A CB  1 
ATOM   48   N N   . ARG   A 1 8   ? -5.188  -27.881 -48.252 1.00 18.29 ? 10  ARG   A N   1 
ATOM   49   C CA  . ARG   A 1 8   ? -6.112  -28.192 -49.337 1.00 19.52 ? 10  ARG   A CA  1 
ATOM   50   C C   . ARG   A 1 8   ? -5.491  -27.995 -50.711 1.00 19.18 ? 10  ARG   A C   1 
ATOM   51   O O   . ARG   A 1 8   ? -6.110  -28.382 -51.714 1.00 22.17 ? 10  ARG   A O   1 
ATOM   52   C CB  . ARG   A 1 8   ? -7.381  -27.341 -49.211 1.00 19.28 ? 10  ARG   A CB  1 
ATOM   53   C CG  . ARG   A 1 8   ? -8.158  -27.631 -47.949 1.00 21.04 ? 10  ARG   A CG  1 
ATOM   54   C CD  . ARG   A 1 8   ? -8.868  -26.391 -47.438 1.00 37.94 ? 10  ARG   A CD  1 
ATOM   55   N NE  . ARG   A 1 8   ? -10.029 -25.988 -48.231 1.00 49.05 ? 10  ARG   A NE  1 
ATOM   56   C CZ  . ARG   A 1 8   ? -10.205 -24.769 -48.742 1.00 49.56 ? 10  ARG   A CZ  1 
ATOM   57   N NH1 . ARG   A 1 8   ? -9.296  -23.821 -48.547 1.00 49.06 ? 10  ARG   A NH1 1 
ATOM   58   N NH2 . ARG   A 1 8   ? -11.297 -24.491 -49.439 1.00 51.41 ? 10  ARG   A NH2 1 
ATOM   59   N N   . VAL   A 1 9   ? -4.284  -27.418 -50.775 1.00 17.52 ? 11  VAL   A N   1 
ATOM   60   C CA  . VAL   A 1 9   ? -3.534  -27.219 -52.007 1.00 18.31 ? 11  VAL   A CA  1 
ATOM   61   C C   . VAL   A 1 9   ? -2.081  -27.565 -51.736 1.00 20.36 ? 11  VAL   A C   1 
ATOM   62   O O   . VAL   A 1 9   ? -1.621  -27.555 -50.592 1.00 19.32 ? 11  VAL   A O   1 
ATOM   63   C CB  . VAL   A 1 9   ? -3.622  -25.776 -52.547 1.00 20.74 ? 11  VAL   A CB  1 
ATOM   64   C CG1 . VAL   A 1 9   ? -5.020  -25.462 -52.959 1.00 21.88 ? 11  VAL   A CG1 1 
ATOM   65   C CG2 . VAL   A 1 9   ? -3.112  -24.780 -51.515 1.00 20.71 ? 11  VAL   A CG2 1 
ATOM   66   N N   . TYR   A 1 10  ? -1.364  -27.874 -52.817 1.00 18.26 ? 12  TYR   A N   1 
ATOM   67   C CA  . TYR   A 1 10  ? 0.072   -28.147 -52.767 1.00 18.65 ? 12  TYR   A CA  1 
ATOM   68   C C   . TYR   A 1 10  ? 0.402   -29.138 -51.665 1.00 18.20 ? 12  TYR   A C   1 
ATOM   69   O O   . TYR   A 1 10  ? 1.443   -29.051 -51.013 1.00 22.37 ? 12  TYR   A O   1 
ATOM   70   C CB  . TYR   A 1 10  ? 0.877   -26.863 -52.586 1.00 19.01 ? 12  TYR   A CB  1 
ATOM   71   C CG  . TYR   A 1 10  ? 0.569   -25.798 -53.601 1.00 19.84 ? 12  TYR   A CG  1 
ATOM   72   C CD1 . TYR   A 1 10  ? 0.602   -26.071 -54.966 1.00 18.99 ? 12  TYR   A CD1 1 
ATOM   73   C CD2 . TYR   A 1 10  ? 0.242   -24.509 -53.191 1.00 19.71 ? 12  TYR   A CD2 1 
ATOM   74   C CE1 . TYR   A 1 10  ? 0.334   -25.076 -55.893 1.00 20.49 ? 12  TYR   A CE1 1 
ATOM   75   C CE2 . TYR   A 1 10  ? -0.025  -23.520 -54.105 1.00 19.10 ? 12  TYR   A CE2 1 
ATOM   76   C CZ  . TYR   A 1 10  ? 0.015   -23.803 -55.452 1.00 18.28 ? 12  TYR   A CZ  1 
ATOM   77   O OH  . TYR   A 1 10  ? -0.259  -22.806 -56.359 1.00 25.97 ? 12  TYR   A OH  1 
ATOM   78   N N   . THR   A 1 11  ? -0.516  -30.076 -51.441 1.00 20.52 ? 13  THR   A N   1 
ATOM   79   C CA  . THR   A 1 11  ? -0.388  -30.979 -50.313 1.00 22.00 ? 13  THR   A CA  1 
ATOM   80   C C   . THR   A 1 11  ? 0.836   -31.869 -50.457 1.00 24.89 ? 13  THR   A C   1 
ATOM   81   O O   . THR   A 1 11  ? 1.572   -32.077 -49.490 1.00 25.04 ? 13  THR   A O   1 
ATOM   82   C CB  . THR   A 1 11  ? -1.658  -31.818 -50.179 1.00 23.16 ? 13  THR   A CB  1 
ATOM   83   O OG1 . THR   A 1 11  ? -2.807  -30.978 -50.379 1.00 24.32 ? 13  THR   A OG1 1 
ATOM   84   C CG2 . THR   A 1 11  ? -1.726  -32.429 -48.804 1.00 22.09 ? 13  THR   A CG2 1 
ATOM   85   N N   . ASP   A 1 12  ? 1.097   -32.369 -51.668 1.00 25.21 ? 14  ASP   A N   1 
ATOM   86   C CA  . ASP   A 1 12  ? 2.091   -33.413 -51.886 1.00 23.65 ? 14  ASP   A CA  1 
ATOM   87   C C   . ASP   A 1 12  ? 3.304   -32.923 -52.672 1.00 24.59 ? 14  ASP   A C   1 
ATOM   88   O O   . ASP   A 1 12  ? 4.038   -33.733 -53.252 1.00 25.86 ? 14  ASP   A O   1 
ATOM   89   C CB  . ASP   A 1 12  ? 1.436   -34.601 -52.593 1.00 26.49 ? 14  ASP   A CB  1 
ATOM   90   C CG  . ASP   A 1 12  ? 0.225   -35.130 -51.836 1.00 41.36 ? 14  ASP   A CG  1 
ATOM   91   O OD1 . ASP   A 1 12  ? 0.365   -35.437 -50.633 1.00 47.27 ? 14  ASP   A OD1 1 
ATOM   92   O OD2 . ASP   A 1 12  ? -0.865  -35.219 -52.439 1.00 47.17 ? 14  ASP   A OD2 1 
ATOM   93   N N   . VAL   A 1 13  ? 3.546   -31.614 -52.686 1.00 23.07 ? 15  VAL   A N   1 
ATOM   94   C CA  . VAL   A 1 13  ? 4.631   -31.092 -53.508 1.00 21.47 ? 15  VAL   A CA  1 
ATOM   95   C C   . VAL   A 1 13  ? 5.967   -31.670 -53.065 1.00 24.99 ? 15  VAL   A C   1 
ATOM   96   O O   . VAL   A 1 13  ? 6.785   -32.080 -53.894 1.00 24.29 ? 15  VAL   A O   1 
ATOM   97   C CB  . VAL   A 1 13  ? 4.633   -29.555 -53.476 1.00 25.97 ? 15  VAL   A CB  1 
ATOM   98   C CG1 . VAL   A 1 13  ? 3.519   -29.013 -54.342 1.00 25.58 ? 15  VAL   A CG1 1 
ATOM   99   C CG2 . VAL   A 1 13  ? 4.462   -29.079 -52.074 1.00 39.08 ? 15  VAL   A CG2 1 
ATOM   100  N N   . ASN   A 1 14  ? 6.209   -31.732 -51.757 1.00 24.39 ? 16  ASN   A N   1 
ATOM   101  C CA  . ASN   A 1 14  ? 7.508   -32.206 -51.298 1.00 25.03 ? 16  ASN   A CA  1 
ATOM   102  C C   . ASN   A 1 14  ? 7.638   -33.722 -51.387 1.00 26.99 ? 16  ASN   A C   1 
ATOM   103  O O   . ASN   A 1 14  ? 8.750   -34.228 -51.573 1.00 32.96 ? 16  ASN   A O   1 
ATOM   104  C CB  . ASN   A 1 14  ? 7.772   -31.718 -49.875 1.00 23.19 ? 16  ASN   A CB  1 
ATOM   105  C CG  . ASN   A 1 14  ? 8.140   -30.254 -49.834 1.00 21.78 ? 16  ASN   A CG  1 
ATOM   106  O OD1 . ASN   A 1 14  ? 8.947   -29.789 -50.644 1.00 24.90 ? 16  ASN   A OD1 1 
ATOM   107  N ND2 . ASN   A 1 14  ? 7.551   -29.512 -48.910 1.00 20.83 ? 16  ASN   A ND2 1 
ATOM   108  N N   . THR   A 1 15  ? 6.527   -34.452 -51.274 1.00 27.78 ? 17  THR   A N   1 
ATOM   109  C CA  . THR   A 1 15  ? 6.580   -35.905 -51.390 1.00 31.89 ? 17  THR   A CA  1 
ATOM   110  C C   . THR   A 1 15  ? 7.185   -36.321 -52.726 1.00 30.47 ? 17  THR   A C   1 
ATOM   111  O O   . THR   A 1 15  ? 7.978   -37.268 -52.796 1.00 36.93 ? 17  THR   A O   1 
ATOM   112  C CB  . THR   A 1 15  ? 5.176   -36.496 -51.232 1.00 37.01 ? 17  THR   A CB  1 
ATOM   113  O OG1 . THR   A 1 15  ? 4.488   -35.844 -50.152 1.00 37.03 ? 17  THR   A OG1 1 
ATOM   114  C CG2 . THR   A 1 15  ? 5.254   -37.989 -50.951 1.00 47.37 ? 17  THR   A CG2 1 
ATOM   115  N N   . HIS   A 1 16  ? 6.852   -35.598 -53.789 1.00 35.42 ? 18  HIS   A N   1 
ATOM   116  C CA  . HIS   A 1 16  ? 7.255   -35.963 -55.138 1.00 30.22 ? 18  HIS   A CA  1 
ATOM   117  C C   . HIS   A 1 16  ? 8.451   -35.174 -55.648 1.00 29.05 ? 18  HIS   A C   1 
ATOM   118  O O   . HIS   A 1 16  ? 8.927   -35.450 -56.751 1.00 30.48 ? 18  HIS   A O   1 
ATOM   119  C CB  . HIS   A 1 16  ? 6.066   -35.807 -56.079 1.00 31.93 ? 18  HIS   A CB  1 
ATOM   120  C CG  . HIS   A 1 16  ? 4.897   -36.651 -55.680 1.00 35.06 ? 18  HIS   A CG  1 
ATOM   121  N ND1 . HIS   A 1 16  ? 4.895   -38.023 -55.814 1.00 37.90 ? 18  HIS   A ND1 1 
ATOM   122  C CD2 . HIS   A 1 16  ? 3.713   -36.328 -55.108 1.00 35.59 ? 18  HIS   A CD2 1 
ATOM   123  C CE1 . HIS   A 1 16  ? 3.750   -38.506 -55.366 1.00 38.80 ? 18  HIS   A CE1 1 
ATOM   124  N NE2 . HIS   A 1 16  ? 3.013   -37.498 -54.933 1.00 37.61 ? 18  HIS   A NE2 1 
ATOM   125  N N   . ARG   A 1 17  ? 8.935   -34.194 -54.888 1.00 29.53 ? 19  ARG   A N   1 
ATOM   126  C CA  . ARG   A 1 17  ? 10.244  -33.626 -55.150 1.00 28.61 ? 19  ARG   A CA  1 
ATOM   127  C C   . ARG   A 1 17  ? 11.315  -34.665 -54.838 1.00 28.28 ? 19  ARG   A C   1 
ATOM   128  O O   . ARG   A 1 17  ? 11.081  -35.592 -54.058 1.00 34.72 ? 19  ARG   A O   1 
ATOM   129  C CB  . ARG   A 1 17  ? 10.472  -32.386 -54.285 1.00 26.10 ? 19  ARG   A CB  1 
ATOM   130  C CG  . ARG   A 1 17  ? 9.638   -31.166 -54.633 1.00 32.34 ? 19  ARG   A CG  1 
ATOM   131  C CD  . ARG   A 1 17  ? 10.411  -30.257 -55.553 1.00 32.72 ? 19  ARG   A CD  1 
ATOM   132  N NE  . ARG   A 1 17  ? 9.626   -29.137 -56.063 1.00 27.86 ? 19  ARG   A NE  1 
ATOM   133  C CZ  . ARG   A 1 17  ? 10.066  -28.331 -57.024 1.00 25.69 ? 19  ARG   A CZ  1 
ATOM   134  N NH1 . ARG   A 1 17  ? 11.268  -28.541 -57.549 1.00 24.64 ? 19  ARG   A NH1 1 
ATOM   135  N NH2 . ARG   A 1 17  ? 9.318   -27.329 -57.463 1.00 37.74 ? 19  ARG   A NH2 1 
ATOM   136  N N   . PRO   A 1 18  ? 12.502  -34.534 -55.424 1.00 30.21 ? 20  PRO   A N   1 
ATOM   137  C CA  . PRO   A 1 18  ? 13.628  -35.347 -54.952 1.00 31.38 ? 20  PRO   A CA  1 
ATOM   138  C C   . PRO   A 1 18  ? 13.939  -35.001 -53.502 1.00 36.83 ? 20  PRO   A C   1 
ATOM   139  O O   . PRO   A 1 18  ? 13.721  -33.874 -53.055 1.00 28.29 ? 20  PRO   A O   1 
ATOM   140  C CB  . PRO   A 1 18  ? 14.776  -34.969 -55.896 1.00 32.08 ? 20  PRO   A CB  1 
ATOM   141  C CG  . PRO   A 1 18  ? 14.363  -33.700 -56.551 1.00 35.45 ? 20  PRO   A CG  1 
ATOM   142  C CD  . PRO   A 1 18  ? 12.865  -33.651 -56.545 1.00 30.60 ? 20  PRO   A CD  1 
ATOM   143  N N   . ARG   A 1 19  ? 14.424  -36.001 -52.756 1.00 33.70 ? 21  ARG   A N   1 
ATOM   144  C CA  . ARG   A 1 19  ? 14.635  -35.820 -51.321 1.00 29.79 ? 21  ARG   A CA  1 
ATOM   145  C C   . ARG   A 1 19  ? 15.551  -34.636 -51.034 1.00 26.62 ? 21  ARG   A C   1 
ATOM   146  O O   . ARG   A 1 19  ? 15.323  -33.879 -50.083 1.00 29.74 ? 21  ARG   A O   1 
ATOM   147  C CB  . ARG   A 1 19  ? 15.206  -37.099 -50.705 1.00 35.55 ? 21  ARG   A CB  1 
ATOM   148  C CG  . ARG   A 1 19  ? 15.603  -36.959 -49.234 1.00 40.92 ? 21  ARG   A CG  1 
ATOM   149  C CD  . ARG   A 1 19  ? 16.250  -38.229 -48.703 1.00 57.61 ? 21  ARG   A CD  1 
ATOM   150  N NE  . ARG   A 1 19  ? 15.414  -39.403 -48.940 1.00 70.25 ? 21  ARG   A NE  1 
ATOM   151  C CZ  . ARG   A 1 19  ? 14.662  -39.991 -48.014 1.00 78.94 ? 21  ARG   A CZ  1 
ATOM   152  N NH1 . ARG   A 1 19  ? 14.641  -39.525 -46.771 1.00 80.32 ? 21  ARG   A NH1 1 
ATOM   153  N NH2 . ARG   A 1 19  ? 13.935  -41.053 -48.330 1.00 80.67 ? 21  ARG   A NH2 1 
ATOM   154  N N   . GLU   A 1 20  ? 16.587  -34.455 -51.857 1.00 28.17 ? 22  GLU   A N   1 
ATOM   155  C CA  . GLU   A 1 20  ? 17.522  -33.354 -51.672 1.00 25.69 ? 22  GLU   A CA  1 
ATOM   156  C C   . GLU   A 1 20  ? 16.833  -31.993 -51.649 1.00 25.88 ? 22  GLU   A C   1 
ATOM   157  O O   . GLU   A 1 20  ? 17.385  -31.049 -51.076 1.00 27.29 ? 22  GLU   A O   1 
ATOM   158  C CB  . GLU   A 1 20  ? 18.593  -33.397 -52.777 1.00 26.15 ? 22  GLU   A CB  1 
ATOM   159  C CG  . GLU   A 1 20  ? 18.253  -34.300 -53.978 1.00 45.99 ? 22  GLU   A CG  1 
ATOM   160  C CD  . GLU   A 1 20  ? 18.302  -35.802 -53.666 1.00 57.24 ? 22  GLU   A CD  1 
ATOM   161  O OE1 . GLU   A 1 20  ? 19.162  -36.232 -52.866 1.00 63.03 ? 22  GLU   A OE1 1 
ATOM   162  O OE2 . GLU   A 1 20  ? 17.459  -36.548 -54.209 1.00 57.31 ? 22  GLU   A OE2 1 
ATOM   163  N N   . TYR   A 1 21  ? 15.640  -31.875 -52.237 1.00 23.91 ? 23  TYR   A N   1 
ATOM   164  C CA  . TYR   A 1 21  ? 14.942  -30.591 -52.256 1.00 21.30 ? 23  TYR   A CA  1 
ATOM   165  C C   . TYR   A 1 21  ? 14.569  -30.136 -50.849 1.00 21.47 ? 23  TYR   A C   1 
ATOM   166  O O   . TYR   A 1 21  ? 14.740  -28.964 -50.500 1.00 22.02 ? 23  TYR   A O   1 
ATOM   167  C CB  . TYR   A 1 21  ? 13.694  -30.686 -53.138 1.00 24.43 ? 23  TYR   A CB  1 
ATOM   168  C CG  . TYR   A 1 21  ? 12.916  -29.388 -53.232 1.00 21.09 ? 23  TYR   A CG  1 
ATOM   169  C CD1 . TYR   A 1 21  ? 13.283  -28.404 -54.132 1.00 21.00 ? 23  TYR   A CD1 1 
ATOM   170  C CD2 . TYR   A 1 21  ? 11.817  -29.147 -52.412 1.00 19.98 ? 23  TYR   A CD2 1 
ATOM   171  C CE1 . TYR   A 1 21  ? 12.588  -27.209 -54.216 1.00 19.31 ? 23  TYR   A CE1 1 
ATOM   172  C CE2 . TYR   A 1 21  ? 11.120  -27.960 -52.482 1.00 19.47 ? 23  TYR   A CE2 1 
ATOM   173  C CZ  . TYR   A 1 21  ? 11.493  -27.000 -53.394 1.00 20.03 ? 23  TYR   A CZ  1 
ATOM   174  O OH  . TYR   A 1 21  ? 10.804  -25.810 -53.477 1.00 21.98 ? 23  TYR   A OH  1 
ATOM   175  N N   . TRP   A 1 22  ? 14.009  -31.037 -50.039 1.00 24.14 ? 24  TRP   A N   1 
ATOM   176  C CA  . TRP   A 1 22  ? 13.511  -30.671 -48.720 1.00 23.91 ? 24  TRP   A CA  1 
ATOM   177  C C   . TRP   A 1 22  ? 14.380  -31.174 -47.572 1.00 19.29 ? 24  TRP   A C   1 
ATOM   178  O O   . TRP   A 1 22  ? 14.191  -30.733 -46.435 1.00 23.24 ? 24  TRP   A O   1 
ATOM   179  C CB  . TRP   A 1 22  ? 12.066  -31.180 -48.537 1.00 21.85 ? 24  TRP   A CB  1 
ATOM   180  C CG  . TRP   A 1 22  ? 11.900  -32.642 -48.850 1.00 20.99 ? 24  TRP   A CG  1 
ATOM   181  C CD1 . TRP   A 1 22  ? 11.398  -33.188 -50.004 1.00 24.16 ? 24  TRP   A CD1 1 
ATOM   182  C CD2 . TRP   A 1 22  ? 12.244  -33.748 -48.003 1.00 25.23 ? 24  TRP   A CD2 1 
ATOM   183  N NE1 . TRP   A 1 22  ? 11.408  -34.562 -49.921 1.00 29.37 ? 24  TRP   A NE1 1 
ATOM   184  C CE2 . TRP   A 1 22  ? 11.912  -34.929 -48.701 1.00 27.11 ? 24  TRP   A CE2 1 
ATOM   185  C CE3 . TRP   A 1 22  ? 12.782  -33.853 -46.715 1.00 26.46 ? 24  TRP   A CE3 1 
ATOM   186  C CZ2 . TRP   A 1 22  ? 12.116  -36.200 -48.161 1.00 30.89 ? 24  TRP   A CZ2 1 
ATOM   187  C CZ3 . TRP   A 1 22  ? 12.988  -35.120 -46.183 1.00 29.83 ? 24  TRP   A CZ3 1 
ATOM   188  C CH2 . TRP   A 1 22  ? 12.648  -36.275 -46.905 1.00 25.23 ? 24  TRP   A CH2 1 
ATOM   189  N N   . ASP   A 1 23  ? 15.331  -32.074 -47.827 1.00 27.19 ? 25  ASP   A N   1 
ATOM   190  C CA  . ASP   A 1 23  ? 16.165  -32.640 -46.765 1.00 22.12 ? 25  ASP   A CA  1 
ATOM   191  C C   . ASP   A 1 23  ? 17.333  -31.690 -46.501 1.00 25.45 ? 25  ASP   A C   1 
ATOM   192  O O   . ASP   A 1 23  ? 18.481  -31.936 -46.888 1.00 26.79 ? 25  ASP   A O   1 
ATOM   193  C CB  . ASP   A 1 23  ? 16.635  -34.035 -47.162 1.00 29.06 ? 25  ASP   A CB  1 
ATOM   194  C CG  . ASP   A 1 23  ? 17.454  -34.715 -46.082 1.00 36.67 ? 25  ASP   A CG  1 
ATOM   195  O OD1 . ASP   A 1 23  ? 17.357  -34.324 -44.901 1.00 33.55 ? 25  ASP   A OD1 1 
ATOM   196  O OD2 . ASP   A 1 23  ? 18.205  -35.655 -46.425 1.00 39.41 ? 25  ASP   A OD2 1 
ATOM   197  N N   . TYR   A 1 24  ? 17.028  -30.577 -45.817 1.00 26.23 ? 26  TYR   A N   1 
ATOM   198  C CA  . TYR   A 1 24  ? 18.006  -29.501 -45.684 1.00 22.44 ? 26  TYR   A CA  1 
ATOM   199  C C   . TYR   A 1 24  ? 19.156  -29.852 -44.752 1.00 27.06 ? 26  TYR   A C   1 
ATOM   200  O O   . TYR   A 1 24  ? 20.232  -29.256 -44.871 1.00 28.53 ? 26  TYR   A O   1 
ATOM   201  C CB  . TYR   A 1 24  ? 17.325  -28.217 -45.208 1.00 23.14 ? 26  TYR   A CB  1 
ATOM   202  C CG  . TYR   A 1 24  ? 16.514  -28.359 -43.940 1.00 27.45 ? 26  TYR   A CG  1 
ATOM   203  C CD1 . TYR   A 1 24  ? 15.152  -28.634 -43.993 1.00 26.29 ? 26  TYR   A CD1 1 
ATOM   204  C CD2 . TYR   A 1 24  ? 17.104  -28.196 -42.691 1.00 28.05 ? 26  TYR   A CD2 1 
ATOM   205  C CE1 . TYR   A 1 24  ? 14.401  -28.751 -42.841 1.00 32.69 ? 26  TYR   A CE1 1 
ATOM   206  C CE2 . TYR   A 1 24  ? 16.355  -28.309 -41.531 1.00 30.37 ? 26  TYR   A CE2 1 
ATOM   207  C CZ  . TYR   A 1 24  ? 15.010  -28.591 -41.618 1.00 35.07 ? 26  TYR   A CZ  1 
ATOM   208  O OH  . TYR   A 1 24  ? 14.262  -28.709 -40.470 1.00 46.50 ? 26  TYR   A OH  1 
ATOM   209  N N   . GLU   A 1 25  ? 18.959  -30.798 -43.832 1.00 28.02 ? 27  GLU   A N   1 
ATOM   210  C CA  . GLU   A 1 25  ? 20.052  -31.212 -42.960 1.00 32.69 ? 27  GLU   A CA  1 
ATOM   211  C C   . GLU   A 1 25  ? 21.218  -31.803 -43.742 1.00 30.90 ? 27  GLU   A C   1 
ATOM   212  O O   . GLU   A 1 25  ? 22.355  -31.773 -43.257 1.00 35.54 ? 27  GLU   A O   1 
ATOM   213  C CB  . GLU   A 1 25  ? 19.541  -32.213 -41.925 1.00 38.98 ? 27  GLU   A CB  1 
ATOM   214  C CG  . GLU   A 1 25  ? 18.494  -31.623 -40.997 1.00 46.91 ? 27  GLU   A CG  1 
ATOM   215  C CD  . GLU   A 1 25  ? 17.666  -32.678 -40.298 1.00 56.91 ? 27  GLU   A CD  1 
ATOM   216  O OE1 . GLU   A 1 25  ? 18.150  -33.255 -39.300 1.00 59.06 ? 27  GLU   A OE1 1 
ATOM   217  O OE2 . GLU   A 1 25  ? 16.530  -32.935 -40.754 1.00 61.89 ? 27  GLU   A OE2 1 
ATOM   218  N N   . SER   A 1 26  ? 20.968  -32.320 -44.944 1.00 31.03 ? 28  SER   A N   1 
ATOM   219  C CA  . SER   A 1 26  ? 22.004  -32.910 -45.781 1.00 30.65 ? 28  SER   A CA  1 
ATOM   220  C C   . SER   A 1 26  ? 22.626  -31.904 -46.734 1.00 28.05 ? 28  SER   A C   1 
ATOM   221  O O   . SER   A 1 26  ? 23.594  -32.237 -47.425 1.00 30.29 ? 28  SER   A O   1 
ATOM   222  C CB  . SER   A 1 26  ? 21.428  -34.077 -46.587 1.00 35.15 ? 28  SER   A CB  1 
ATOM   223  O OG  . SER   A 1 26  ? 20.933  -35.093 -45.734 1.00 46.68 ? 28  SER   A OG  1 
ATOM   224  N N   . HIS   A 1 27  ? 22.098  -30.688 -46.781 1.00 29.94 ? 29  HIS   A N   1 
ATOM   225  C CA  . HIS   A 1 27  ? 22.569  -29.694 -47.732 1.00 28.58 ? 29  HIS   A CA  1 
ATOM   226  C C   . HIS   A 1 27  ? 24.026  -29.332 -47.469 1.00 31.48 ? 29  HIS   A C   1 
ATOM   227  O O   . HIS   A 1 27  ? 24.434  -29.114 -46.327 1.00 30.14 ? 29  HIS   A O   1 
ATOM   228  C CB  . HIS   A 1 27  ? 21.686  -28.453 -47.651 1.00 31.79 ? 29  HIS   A CB  1 
ATOM   229  C CG  . HIS   A 1 27  ? 22.116  -27.350 -48.563 1.00 28.26 ? 29  HIS   A CG  1 
ATOM   230  N ND1 . HIS   A 1 27  ? 22.045  -27.451 -49.935 1.00 26.47 ? 29  HIS   A ND1 1 
ATOM   231  C CD2 . HIS   A 1 27  ? 22.627  -26.124 -48.298 1.00 30.51 ? 29  HIS   A CD2 1 
ATOM   232  C CE1 . HIS   A 1 27  ? 22.489  -26.330 -50.477 1.00 28.37 ? 29  HIS   A CE1 1 
ATOM   233  N NE2 . HIS   A 1 27  ? 22.850  -25.510 -49.506 1.00 29.57 ? 29  HIS   A NE2 1 
ATOM   234  N N   . VAL   A 1 28  ? 24.813  -29.274 -48.534 1.00 26.61 ? 30  VAL   A N   1 
ATOM   235  C CA  . VAL   A 1 28  ? 26.206  -28.850 -48.455 1.00 28.45 ? 30  VAL   A CA  1 
ATOM   236  C C   . VAL   A 1 28  ? 26.280  -27.404 -48.928 1.00 27.99 ? 30  VAL   A C   1 
ATOM   237  O O   . VAL   A 1 28  ? 25.967  -27.105 -50.087 1.00 32.05 ? 30  VAL   A O   1 
ATOM   238  C CB  . VAL   A 1 28  ? 27.119  -29.758 -49.290 1.00 29.72 ? 30  VAL   A CB  1 
ATOM   239  C CG1 . VAL   A 1 28  ? 28.567  -29.263 -49.234 1.00 28.18 ? 30  VAL   A CG1 1 
ATOM   240  C CG2 . VAL   A 1 28  ? 27.024  -31.188 -48.795 1.00 33.21 ? 30  VAL   A CG2 1 
ATOM   241  N N   . VAL   A 1 29  ? 26.674  -26.504 -48.029 1.00 25.53 ? 31  VAL   A N   1 
ATOM   242  C CA  . VAL   A 1 29  ? 26.712  -25.086 -48.362 1.00 24.42 ? 31  VAL   A CA  1 
ATOM   243  C C   . VAL   A 1 29  ? 27.862  -24.819 -49.321 1.00 28.11 ? 31  VAL   A C   1 
ATOM   244  O O   . VAL   A 1 29  ? 28.987  -25.296 -49.122 1.00 29.63 ? 31  VAL   A O   1 
ATOM   245  C CB  . VAL   A 1 29  ? 26.834  -24.234 -47.091 1.00 29.67 ? 31  VAL   A CB  1 
ATOM   246  C CG1 . VAL   A 1 29  ? 27.106  -22.778 -47.450 1.00 31.62 ? 31  VAL   A CG1 1 
ATOM   247  C CG2 . VAL   A 1 29  ? 25.560  -24.348 -46.258 1.00 30.00 ? 31  VAL   A CG2 1 
ATOM   248  N N   . GLU   A 1 30  ? 27.588  -24.050 -50.366 1.00 30.18 ? 32  GLU   A N   1 
ATOM   249  C CA  . GLU   A 1 30  ? 28.620  -23.590 -51.285 1.00 30.85 ? 32  GLU   A CA  1 
ATOM   250  C C   . GLU   A 1 30  ? 29.017  -22.171 -50.883 1.00 27.08 ? 32  GLU   A C   1 
ATOM   251  O O   . GLU   A 1 30  ? 28.205  -21.241 -50.967 1.00 29.90 ? 32  GLU   A O   1 
ATOM   252  C CB  . GLU   A 1 30  ? 28.134  -23.671 -52.730 1.00 41.51 ? 32  GLU   A CB  1 
ATOM   253  C CG  . GLU   A 1 30  ? 27.950  -25.111 -53.196 1.00 56.02 ? 32  GLU   A CG  1 
ATOM   254  C CD  . GLU   A 1 30  ? 27.910  -25.252 -54.705 1.00 67.17 ? 32  GLU   A CD  1 
ATOM   255  O OE1 . GLU   A 1 30  ? 26.990  -24.686 -55.336 1.00 68.63 ? 32  GLU   A OE1 1 
ATOM   256  O OE2 . GLU   A 1 30  ? 28.803  -25.929 -55.260 1.00 71.76 ? 32  GLU   A OE2 1 
ATOM   257  N N   . TRP   A 1 31  ? 30.258  -22.018 -50.424 1.00 28.02 ? 33  TRP   A N   1 
ATOM   258  C CA  . TRP   A 1 31  ? 30.727  -20.768 -49.840 1.00 21.97 ? 33  TRP   A CA  1 
ATOM   259  C C   . TRP   A 1 31  ? 31.355  -19.877 -50.901 1.00 23.16 ? 33  TRP   A C   1 
ATOM   260  O O   . TRP   A 1 31  ? 32.131  -20.341 -51.741 1.00 27.02 ? 33  TRP   A O   1 
ATOM   261  C CB  . TRP   A 1 31  ? 31.750  -21.036 -48.732 1.00 26.66 ? 33  TRP   A CB  1 
ATOM   262  C CG  . TRP   A 1 31  ? 31.248  -21.932 -47.650 1.00 25.51 ? 33  TRP   A CG  1 
ATOM   263  C CD1 . TRP   A 1 31  ? 31.453  -23.278 -47.540 1.00 30.10 ? 33  TRP   A CD1 1 
ATOM   264  C CD2 . TRP   A 1 31  ? 30.456  -21.553 -46.520 1.00 27.73 ? 33  TRP   A CD2 1 
ATOM   265  N NE1 . TRP   A 1 31  ? 30.836  -23.758 -46.414 1.00 30.57 ? 33  TRP   A NE1 1 
ATOM   266  C CE2 . TRP   A 1 31  ? 30.220  -22.719 -45.766 1.00 30.35 ? 33  TRP   A CE2 1 
ATOM   267  C CE3 . TRP   A 1 31  ? 29.920  -20.340 -46.073 1.00 24.81 ? 33  TRP   A CE3 1 
ATOM   268  C CZ2 . TRP   A 1 31  ? 29.461  -22.709 -44.591 1.00 32.31 ? 33  TRP   A CZ2 1 
ATOM   269  C CZ3 . TRP   A 1 31  ? 29.170  -20.333 -44.904 1.00 33.89 ? 33  TRP   A CZ3 1 
ATOM   270  C CH2 . TRP   A 1 31  ? 28.954  -21.509 -44.176 1.00 36.46 ? 33  TRP   A CH2 1 
ATOM   271  N N   . GLY   A 1 32  ? 31.033  -18.590 -50.838 1.00 20.75 ? 34  GLY   A N   1 
ATOM   272  C CA  . GLY   A 1 32  ? 31.655  -17.596 -51.683 1.00 22.13 ? 34  GLY   A CA  1 
ATOM   273  C C   . GLY   A 1 32  ? 32.892  -16.993 -51.038 1.00 23.97 ? 34  GLY   A C   1 
ATOM   274  O O   . GLY   A 1 32  ? 33.404  -17.470 -50.025 1.00 23.54 ? 34  GLY   A O   1 
ATOM   275  N N   . ASN   A 1 33  ? 33.359  -15.902 -51.642 1.00 21.66 ? 35  ASN   A N   1 
ATOM   276  C CA  . ASN   A 1 33  ? 34.561  -15.194 -51.207 1.00 23.50 ? 35  ASN   A CA  1 
ATOM   277  C C   . ASN   A 1 33  ? 34.169  -14.079 -50.239 1.00 21.03 ? 35  ASN   A C   1 
ATOM   278  O O   . ASN   A 1 33  ? 33.599  -13.065 -50.649 1.00 21.16 ? 35  ASN   A O   1 
ATOM   279  C CB  . ASN   A 1 33  ? 35.287  -14.634 -52.427 1.00 29.93 ? 35  ASN   A CB  1 
ATOM   280  C CG  . ASN   A 1 33  ? 36.766  -14.487 -52.208 1.00 56.26 ? 35  ASN   A CG  1 
ATOM   281  O OD1 . ASN   A 1 33  ? 37.329  -15.098 -51.301 1.00 73.34 ? 35  ASN   A OD1 1 
ATOM   282  N ND2 . ASN   A 1 33  ? 37.414  -13.687 -53.047 1.00 62.71 ? 35  ASN   A ND2 1 
ATOM   283  N N   . GLN   A 1 34  ? 34.500  -14.248 -48.954 1.00 21.22 ? 36  GLN   A N   1 
ATOM   284  C CA  . GLN   A 1 34  ? 34.130  -13.246 -47.960 1.00 19.55 ? 36  GLN   A CA  1 
ATOM   285  C C   . GLN   A 1 34  ? 34.735  -11.872 -48.257 1.00 18.41 ? 36  GLN   A C   1 
ATOM   286  O O   . GLN   A 1 34  ? 34.141  -10.848 -47.899 1.00 21.44 ? 36  GLN   A O   1 
ATOM   287  C CB  . GLN   A 1 34  ? 34.532  -13.730 -46.563 1.00 24.24 ? 36  GLN   A CB  1 
ATOM   288  C CG  . GLN   A 1 34  ? 34.063  -12.839 -45.418 1.00 24.61 ? 36  GLN   A CG  1 
ATOM   289  C CD  . GLN   A 1 34  ? 35.063  -11.751 -45.057 1.00 25.73 ? 36  GLN   A CD  1 
ATOM   290  O OE1 . GLN   A 1 34  ? 36.250  -11.847 -45.372 1.00 25.57 ? 36  GLN   A OE1 1 
ATOM   291  N NE2 . GLN   A 1 34  ? 34.580  -10.702 -44.399 1.00 25.28 ? 36  GLN   A NE2 1 
ATOM   292  N N   . ASP   A 1 35  ? 35.907  -11.811 -48.903 1.00 20.05 ? 37  ASP   A N   1 
ATOM   293  C CA  . ASP   A 1 35  ? 36.484  -10.498 -49.179 1.00 21.21 ? 37  ASP   A CA  1 
ATOM   294  C C   . ASP   A 1 35  ? 35.795  -9.760  -50.321 1.00 21.40 ? 37  ASP   A C   1 
ATOM   295  O O   . ASP   A 1 35  ? 36.158  -8.612  -50.596 1.00 24.35 ? 37  ASP   A O   1 
ATOM   296  C CB  . ASP   A 1 35  ? 37.977  -10.620 -49.480 1.00 27.16 ? 37  ASP   A CB  1 
ATOM   297  C CG  . ASP   A 1 35  ? 38.278  -11.750 -50.415 1.00 38.65 ? 37  ASP   A CG  1 
ATOM   298  O OD1 . ASP   A 1 35  ? 38.048  -12.910 -50.020 1.00 42.00 ? 37  ASP   A OD1 1 
ATOM   299  O OD2 . ASP   A 1 35  ? 38.727  -11.480 -51.548 1.00 50.91 ? 37  ASP   A OD2 1 
ATOM   300  N N   . ASP   A 1 36  ? 34.816  -10.375 -50.988 1.00 19.61 ? 38  ASP   A N   1 
ATOM   301  C CA  . ASP   A 1 36  ? 34.072  -9.664  -52.018 1.00 19.17 ? 38  ASP   A CA  1 
ATOM   302  C C   . ASP   A 1 36  ? 33.153  -8.588  -51.449 1.00 19.82 ? 38  ASP   A C   1 
ATOM   303  O O   . ASP   A 1 36  ? 32.647  -7.767  -52.222 1.00 22.18 ? 38  ASP   A O   1 
ATOM   304  C CB  . ASP   A 1 36  ? 33.219  -10.638 -52.830 1.00 22.66 ? 38  ASP   A CB  1 
ATOM   305  C CG  . ASP   A 1 36  ? 34.024  -11.476 -53.808 1.00 28.11 ? 38  ASP   A CG  1 
ATOM   306  O OD1 . ASP   A 1 36  ? 35.235  -11.212 -54.002 1.00 25.50 ? 38  ASP   A OD1 1 
ATOM   307  O OD2 . ASP   A 1 36  ? 33.420  -12.411 -54.387 1.00 30.63 ? 38  ASP   A OD2 1 
ATOM   308  N N   . TYR   A 1 37  ? 32.899  -8.583  -50.136 1.00 21.13 ? 39  TYR   A N   1 
ATOM   309  C CA  . TYR   A 1 37  ? 31.825  -7.786  -49.553 1.00 19.74 ? 39  TYR   A CA  1 
ATOM   310  C C   . TYR   A 1 37  ? 32.405  -6.923  -48.453 1.00 21.81 ? 39  TYR   A C   1 
ATOM   311  O O   . TYR   A 1 37  ? 33.020  -7.440  -47.516 1.00 28.65 ? 39  TYR   A O   1 
ATOM   312  C CB  . TYR   A 1 37  ? 30.704  -8.677  -49.004 1.00 17.65 ? 39  TYR   A CB  1 
ATOM   313  C CG  . TYR   A 1 37  ? 30.218  -9.588  -50.069 1.00 16.81 ? 39  TYR   A CG  1 
ATOM   314  C CD1 . TYR   A 1 37  ? 30.578  -10.931 -50.090 1.00 19.88 ? 39  TYR   A CD1 1 
ATOM   315  C CD2 . TYR   A 1 37  ? 29.463  -9.092  -51.121 1.00 16.11 ? 39  TYR   A CD2 1 
ATOM   316  C CE1 . TYR   A 1 37  ? 30.161  -11.759 -51.095 1.00 17.77 ? 39  TYR   A CE1 1 
ATOM   317  C CE2 . TYR   A 1 37  ? 29.042  -9.911  -52.140 1.00 16.39 ? 39  TYR   A CE2 1 
ATOM   318  C CZ  . TYR   A 1 37  ? 29.386  -11.246 -52.125 1.00 17.89 ? 39  TYR   A CZ  1 
ATOM   319  O OH  . TYR   A 1 37  ? 28.988  -12.068 -53.143 1.00 22.03 ? 39  TYR   A OH  1 
ATOM   320  N N   . GLN   A 1 38  ? 32.221  -5.615  -48.574 1.00 20.00 ? 40  GLN   A N   1 
ATOM   321  C CA  . GLN   A 1 38  ? 32.678  -4.670  -47.568 1.00 20.42 ? 40  GLN   A CA  1 
ATOM   322  C C   . GLN   A 1 38  ? 31.467  -4.085  -46.863 1.00 20.66 ? 40  GLN   A C   1 
ATOM   323  O O   . GLN   A 1 38  ? 30.594  -3.495  -47.513 1.00 23.06 ? 40  GLN   A O   1 
ATOM   324  C CB  . GLN   A 1 38  ? 33.526  -3.570  -48.202 1.00 30.74 ? 40  GLN   A CB  1 
ATOM   325  C CG  . GLN   A 1 38  ? 34.692  -4.129  -48.991 1.00 46.74 ? 40  GLN   A CG  1 
ATOM   326  C CD  . GLN   A 1 38  ? 35.826  -3.141  -49.160 1.00 56.48 ? 40  GLN   A CD  1 
ATOM   327  O OE1 . GLN   A 1 38  ? 35.656  -1.937  -48.967 1.00 64.35 ? 40  GLN   A OE1 1 
ATOM   328  N NE2 . GLN   A 1 38  ? 36.999  -3.652  -49.514 1.00 50.66 ? 40  GLN   A NE2 1 
ATOM   329  N N   . LEU   A 1 39  ? 31.418  -4.242  -45.540 1.00 18.00 ? 41  LEU   A N   1 
ATOM   330  C CA  . LEU   A 1 39  ? 30.291  -3.712  -44.784 1.00 18.30 ? 41  LEU   A CA  1 
ATOM   331  C C   . LEU   A 1 39  ? 30.357  -2.189  -44.749 1.00 22.83 ? 41  LEU   A C   1 
ATOM   332  O O   . LEU   A 1 39  ? 31.435  -1.600  -44.633 1.00 23.35 ? 41  LEU   A O   1 
ATOM   333  C CB  . LEU   A 1 39  ? 30.281  -4.279  -43.366 1.00 19.63 ? 41  LEU   A CB  1 
ATOM   334  C CG  . LEU   A 1 39  ? 30.251  -5.801  -43.226 1.00 19.34 ? 41  LEU   A CG  1 
ATOM   335  C CD1 . LEU   A 1 39  ? 30.355  -6.174  -41.756 1.00 23.25 ? 41  LEU   A CD1 1 
ATOM   336  C CD2 . LEU   A 1 39  ? 29.000  -6.418  -43.862 1.00 18.26 ? 41  LEU   A CD2 1 
ATOM   337  N N   . VAL   A 1 40  ? 29.194  -1.552  -44.872 1.00 20.97 ? 42  VAL   A N   1 
ATOM   338  C CA  . VAL   A 1 40  ? 29.093  -0.103  -44.961 1.00 20.95 ? 42  VAL   A CA  1 
ATOM   339  C C   . VAL   A 1 40  ? 28.364  0.486   -43.759 1.00 25.58 ? 42  VAL   A C   1 
ATOM   340  O O   . VAL   A 1 40  ? 28.814  1.475   -43.174 1.00 24.11 ? 42  VAL   A O   1 
ATOM   341  C CB  . VAL   A 1 40  ? 28.395  0.302   -46.280 1.00 26.41 ? 42  VAL   A CB  1 
ATOM   342  C CG1 . VAL   A 1 40  ? 28.088  1.794   -46.301 1.00 26.11 ? 42  VAL   A CG1 1 
ATOM   343  C CG2 . VAL   A 1 40  ? 29.240  -0.089  -47.477 1.00 27.55 ? 42  VAL   A CG2 1 
ATOM   344  N N   . ARG   A 1 41  ? 27.246  -0.118  -43.365 1.00 23.07 ? 43  ARG   A N   1 
ATOM   345  C CA  . ARG   A 1 41  ? 26.375  0.466   -42.362 1.00 27.05 ? 43  ARG   A CA  1 
ATOM   346  C C   . ARG   A 1 41  ? 25.549  -0.644  -41.733 1.00 22.96 ? 43  ARG   A C   1 
ATOM   347  O O   . ARG   A 1 41  ? 25.033  -1.507  -42.445 1.00 23.68 ? 43  ARG   A O   1 
ATOM   348  C CB  . ARG   A 1 41  ? 25.470  1.513   -43.013 1.00 40.57 ? 43  ARG   A CB  1 
ATOM   349  C CG  . ARG   A 1 41  ? 24.831  2.432   -42.045 1.00 54.39 ? 43  ARG   A CG  1 
ATOM   350  C CD  . ARG   A 1 41  ? 23.850  3.368   -42.716 1.00 57.33 ? 43  ARG   A CD  1 
ATOM   351  N NE  . ARG   A 1 41  ? 24.224  3.640   -44.095 1.00 57.78 ? 43  ARG   A NE  1 
ATOM   352  C CZ  . ARG   A 1 41  ? 23.421  3.433   -45.130 1.00 65.96 ? 43  ARG   A CZ  1 
ATOM   353  N NH1 . ARG   A 1 41  ? 22.193  2.971   -44.931 1.00 66.16 ? 43  ARG   A NH1 1 
ATOM   354  N NH2 . ARG   A 1 41  ? 23.841  3.701   -46.359 1.00 68.33 ? 43  ARG   A NH2 1 
ATOM   355  N N   . LYS   A 1 42  ? 25.433  -0.630  -40.410 1.00 21.83 ? 44  LYS   A N   1 
ATOM   356  C CA  . LYS   A 1 42  ? 24.546  -1.569  -39.734 1.00 22.26 ? 44  LYS   A CA  1 
ATOM   357  C C   . LYS   A 1 42  ? 23.107  -1.100  -39.887 1.00 21.92 ? 44  LYS   A C   1 
ATOM   358  O O   . LYS   A 1 42  ? 22.806  0.075   -39.658 1.00 25.76 ? 44  LYS   A O   1 
ATOM   359  C CB  . LYS   A 1 42  ? 24.913  -1.696  -38.253 1.00 24.10 ? 44  LYS   A CB  1 
ATOM   360  C CG  . LYS   A 1 42  ? 24.133  -2.777  -37.509 1.00 28.59 ? 44  LYS   A CG  1 
ATOM   361  C CD  . LYS   A 1 42  ? 24.886  -3.292  -36.286 1.00 34.72 ? 44  LYS   A CD  1 
ATOM   362  C CE  . LYS   A 1 42  ? 25.204  -2.178  -35.298 1.00 43.53 ? 44  LYS   A CE  1 
ATOM   363  N NZ  . LYS   A 1 42  ? 26.010  -2.675  -34.133 1.00 48.72 ? 44  LYS   A NZ  1 
ATOM   364  N N   . LEU   A 1 43  ? 22.221  -2.010  -40.291 1.00 21.97 ? 45  LEU   A N   1 
ATOM   365  C CA  . LEU   A 1 43  ? 20.814  -1.672  -40.491 1.00 24.19 ? 45  LEU   A CA  1 
ATOM   366  C C   . LEU   A 1 43  ? 19.924  -2.135  -39.349 1.00 30.37 ? 45  LEU   A C   1 
ATOM   367  O O   . LEU   A 1 43  ? 18.942  -1.461  -39.026 1.00 33.46 ? 45  LEU   A O   1 
ATOM   368  C CB  . LEU   A 1 43  ? 20.296  -2.270  -41.807 1.00 26.42 ? 45  LEU   A CB  1 
ATOM   369  C CG  . LEU   A 1 43  ? 20.961  -1.765  -43.089 1.00 26.89 ? 45  LEU   A CG  1 
ATOM   370  C CD1 . LEU   A 1 43  ? 20.335  -2.426  -44.309 1.00 24.99 ? 45  LEU   A CD1 1 
ATOM   371  C CD2 . LEU   A 1 43  ? 20.872  -0.251  -43.191 1.00 31.80 ? 45  LEU   A CD2 1 
ATOM   372  N N   . GLY   A 1 44  ? 20.230  -3.269  -38.735 1.00 26.23 ? 46  GLY   A N   1 
ATOM   373  C CA  . GLY   A 1 44  ? 19.405  -3.735  -37.636 1.00 31.11 ? 46  GLY   A CA  1 
ATOM   374  C C   . GLY   A 1 44  ? 20.070  -4.881  -36.915 1.00 27.04 ? 46  GLY   A C   1 
ATOM   375  O O   . GLY   A 1 44  ? 21.064  -5.448  -37.380 1.00 23.04 ? 46  GLY   A O   1 
ATOM   376  N N   . ARG   A 1 45  ? 19.506  -5.201  -35.750 1.00 22.66 ? 47  ARG   A N   1 
ATOM   377  C CA  . ARG   A 1 45  ? 19.952  -6.311  -34.922 1.00 23.45 ? 47  ARG   A CA  1 
ATOM   378  C C   . ARG   A 1 45  ? 18.717  -7.019  -34.390 1.00 30.79 ? 47  ARG   A C   1 
ATOM   379  O O   . ARG   A 1 45  ? 17.669  -6.396  -34.194 1.00 29.65 ? 47  ARG   A O   1 
ATOM   380  C CB  . ARG   A 1 45  ? 20.887  -5.866  -33.796 1.00 27.17 ? 47  ARG   A CB  1 
ATOM   381  C CG  . ARG   A 1 45  ? 21.168  -6.999  -32.815 1.00 36.43 ? 47  ARG   A CG  1 
ATOM   382  C CD  . ARG   A 1 45  ? 21.859  -6.542  -31.570 1.00 48.06 ? 47  ARG   A CD  1 
ATOM   383  N NE  . ARG   A 1 45  ? 23.279  -6.332  -31.806 1.00 53.39 ? 47  ARG   A NE  1 
ATOM   384  C CZ  . ARG   A 1 45  ? 24.118  -5.879  -30.885 1.00 51.40 ? 47  ARG   A CZ  1 
ATOM   385  N NH1 . ARG   A 1 45  ? 23.665  -5.593  -29.671 1.00 49.63 ? 47  ARG   A NH1 1 
ATOM   386  N NH2 . ARG   A 1 45  ? 25.401  -5.710  -31.179 1.00 47.98 ? 47  ARG   A NH2 1 
ATOM   387  N N   . GLY   A 1 46  ? 18.853  -8.324  -34.161 1.00 28.00 ? 48  GLY   A N   1 
ATOM   388  C CA  . GLY   A 1 46  ? 17.797  -9.132  -33.593 1.00 26.69 ? 48  GLY   A CA  1 
ATOM   389  C C   . GLY   A 1 46  ? 18.384  -10.286 -32.814 1.00 30.01 ? 48  GLY   A C   1 
ATOM   390  O O   . GLY   A 1 46  ? 19.605  -10.378 -32.651 1.00 33.55 ? 48  GLY   A O   1 
ATOM   391  N N   . LYS   A 1 47  ? 17.528  -11.181 -32.323 1.00 34.42 ? 49  LYS   A N   1 
ATOM   392  C CA  . LYS   A 1 47  ? 18.024  -12.300 -31.536 1.00 36.54 ? 49  LYS   A CA  1 
ATOM   393  C C   . LYS   A 1 47  ? 18.804  -13.298 -32.378 1.00 34.82 ? 49  LYS   A C   1 
ATOM   394  O O   . LYS   A 1 47  ? 19.635  -14.031 -31.830 1.00 44.78 ? 49  LYS   A O   1 
ATOM   395  C CB  . LYS   A 1 47  ? 16.865  -13.005 -30.827 1.00 46.80 ? 49  LYS   A CB  1 
ATOM   396  C CG  . LYS   A 1 47  ? 16.967  -12.957 -29.312 1.00 56.66 ? 49  LYS   A CG  1 
ATOM   397  C CD  . LYS   A 1 47  ? 17.068  -11.521 -28.820 1.00 59.42 ? 49  LYS   A CD  1 
ATOM   398  C CE  . LYS   A 1 47  ? 17.620  -11.456 -27.403 1.00 66.59 ? 49  LYS   A CE  1 
ATOM   399  N NZ  . LYS   A 1 47  ? 17.803  -10.051 -26.936 1.00 66.60 ? 49  LYS   A NZ  1 
ATOM   400  N N   . TYR   A 1 48  ? 18.589  -13.316 -33.694 1.00 36.53 ? 50  TYR   A N   1 
ATOM   401  C CA  . TYR   A 1 48  ? 19.166  -14.340 -34.553 1.00 35.65 ? 50  TYR   A CA  1 
ATOM   402  C C   . TYR   A 1 48  ? 20.228  -13.834 -35.520 1.00 29.55 ? 50  TYR   A C   1 
ATOM   403  O O   . TYR   A 1 48  ? 20.922  -14.661 -36.120 1.00 28.41 ? 50  TYR   A O   1 
ATOM   404  C CB  . TYR   A 1 48  ? 18.061  -15.033 -35.362 1.00 41.25 ? 50  TYR   A CB  1 
ATOM   405  C CG  . TYR   A 1 48  ? 17.117  -15.850 -34.517 1.00 51.41 ? 50  TYR   A CG  1 
ATOM   406  C CD1 . TYR   A 1 48  ? 17.588  -16.597 -33.448 1.00 54.75 ? 50  TYR   A CD1 1 
ATOM   407  C CD2 . TYR   A 1 48  ? 15.755  -15.864 -34.781 1.00 55.26 ? 50  TYR   A CD2 1 
ATOM   408  C CE1 . TYR   A 1 48  ? 16.730  -17.343 -32.667 1.00 63.15 ? 50  TYR   A CE1 1 
ATOM   409  C CE2 . TYR   A 1 48  ? 14.886  -16.606 -34.005 1.00 61.48 ? 50  TYR   A CE2 1 
ATOM   410  C CZ  . TYR   A 1 48  ? 15.379  -17.345 -32.948 1.00 67.09 ? 50  TYR   A CZ  1 
ATOM   411  O OH  . TYR   A 1 48  ? 14.521  -18.089 -32.169 1.00 68.94 ? 50  TYR   A OH  1 
ATOM   412  N N   . SER   A 1 49  ? 20.358  -12.523 -35.716 1.00 23.50 ? 51  SER   A N   1 
ATOM   413  C CA  . SER   A 1 49  ? 21.306  -12.026 -36.711 1.00 20.59 ? 51  SER   A CA  1 
ATOM   414  C C   . SER   A 1 49  ? 21.512  -10.527 -36.533 1.00 22.91 ? 51  SER   A C   1 
ATOM   415  O O   . SER   A 1 49  ? 20.800  -9.861  -35.780 1.00 21.70 ? 51  SER   A O   1 
ATOM   416  C CB  . SER   A 1 49  ? 20.831  -12.307 -38.136 1.00 22.19 ? 51  SER   A CB  1 
ATOM   417  O OG  . SER   A 1 49  ? 19.659  -11.548 -38.407 1.00 30.33 ? 51  SER   A OG  1 
ATOM   418  N N   . GLU   A 1 50  ? 22.517  -10.008 -37.238 1.00 18.88 ? 52  GLU   A N   1 
ATOM   419  C CA  . GLU   A 1 50  ? 22.681  -8.584  -37.479 1.00 19.72 ? 52  GLU   A CA  1 
ATOM   420  C C   . GLU   A 1 50  ? 22.698  -8.364  -38.983 1.00 22.85 ? 52  GLU   A C   1 
ATOM   421  O O   . GLU   A 1 50  ? 23.218  -9.196  -39.732 1.00 22.01 ? 52  GLU   A O   1 
ATOM   422  C CB  . GLU   A 1 50  ? 23.980  -8.027  -36.866 1.00 19.75 ? 52  GLU   A CB  1 
ATOM   423  C CG  . GLU   A 1 50  ? 24.005  -7.966  -35.346 1.00 28.20 ? 52  GLU   A CG  1 
ATOM   424  C CD  . GLU   A 1 50  ? 25.206  -7.189  -34.824 1.00 40.36 ? 52  GLU   A CD  1 
ATOM   425  O OE1 . GLU   A 1 50  ? 26.286  -7.256  -35.456 1.00 39.75 ? 52  GLU   A OE1 1 
ATOM   426  O OE2 . GLU   A 1 50  ? 25.067  -6.499  -33.791 1.00 43.63 ? 52  GLU   A OE2 1 
ATOM   427  N N   . VAL   A 1 51  ? 22.156  -7.237  -39.425 1.00 20.95 ? 53  VAL   A N   1 
ATOM   428  C CA  . VAL   A 1 51  ? 21.959  -6.973  -40.844 1.00 16.52 ? 53  VAL   A CA  1 
ATOM   429  C C   . VAL   A 1 51  ? 22.679  -5.680  -41.200 1.00 20.16 ? 53  VAL   A C   1 
ATOM   430  O O   . VAL   A 1 51  ? 22.596  -4.691  -40.467 1.00 20.42 ? 53  VAL   A O   1 
ATOM   431  C CB  . VAL   A 1 51  ? 20.462  -6.906  -41.200 1.00 24.51 ? 53  VAL   A CB  1 
ATOM   432  C CG1 . VAL   A 1 51  ? 20.263  -6.442  -42.627 1.00 26.44 ? 53  VAL   A CG1 1 
ATOM   433  C CG2 . VAL   A 1 51  ? 19.869  -8.269  -41.044 1.00 27.18 ? 53  VAL   A CG2 1 
ATOM   434  N N   . PHE   A 1 52  ? 23.394  -5.702  -42.318 1.00 16.09 ? 54  PHE   A N   1 
ATOM   435  C CA  . PHE   A 1 52  ? 24.232  -4.602  -42.756 1.00 17.92 ? 54  PHE   A CA  1 
ATOM   436  C C   . PHE   A 1 52  ? 23.949  -4.271  -44.210 1.00 19.33 ? 54  PHE   A C   1 
ATOM   437  O O   . PHE   A 1 52  ? 23.666  -5.157  -45.019 1.00 19.79 ? 54  PHE   A O   1 
ATOM   438  C CB  . PHE   A 1 52  ? 25.716  -4.960  -42.652 1.00 18.44 ? 54  PHE   A CB  1 
ATOM   439  C CG  . PHE   A 1 52  ? 26.180  -5.244  -41.259 1.00 17.74 ? 54  PHE   A CG  1 
ATOM   440  C CD1 . PHE   A 1 52  ? 25.948  -6.484  -40.673 1.00 16.77 ? 54  PHE   A CD1 1 
ATOM   441  C CD2 . PHE   A 1 52  ? 26.846  -4.274  -40.537 1.00 19.34 ? 54  PHE   A CD2 1 
ATOM   442  C CE1 . PHE   A 1 52  ? 26.379  -6.750  -39.382 1.00 19.80 ? 54  PHE   A CE1 1 
ATOM   443  C CE2 . PHE   A 1 52  ? 27.282  -4.529  -39.241 1.00 20.23 ? 54  PHE   A CE2 1 
ATOM   444  C CZ  . PHE   A 1 52  ? 27.050  -5.767  -38.663 1.00 20.75 ? 54  PHE   A CZ  1 
ATOM   445  N N   . GLU   A 1 53  ? 24.066  -2.990  -44.542 1.00 19.00 ? 55  GLU   A N   1 
ATOM   446  C CA  . GLU   A 1 53  ? 24.286  -2.608  -45.926 1.00 22.81 ? 55  GLU   A CA  1 
ATOM   447  C C   . GLU   A 1 53  ? 25.763  -2.802  -46.258 1.00 20.45 ? 55  GLU   A C   1 
ATOM   448  O O   . GLU   A 1 53  ? 26.642  -2.529  -45.434 1.00 21.88 ? 55  GLU   A O   1 
ATOM   449  C CB  . GLU   A 1 53  ? 23.855  -1.161  -46.157 1.00 27.56 ? 55  GLU   A CB  1 
ATOM   450  C CG  . GLU   A 1 53  ? 23.993  -0.670  -47.579 1.00 35.06 ? 55  GLU   A CG  1 
ATOM   451  C CD  . GLU   A 1 53  ? 23.601  0.789   -47.710 1.00 48.73 ? 55  GLU   A CD  1 
ATOM   452  O OE1 . GLU   A 1 53  ? 22.410  1.107   -47.497 1.00 51.32 ? 55  GLU   A OE1 1 
ATOM   453  O OE2 . GLU   A 1 53  ? 24.485  1.619   -48.006 1.00 51.15 ? 55  GLU   A OE2 1 
ATOM   454  N N   . ALA   A 1 54  ? 26.034  -3.323  -47.450 1.00 19.41 ? 56  ALA   A N   1 
ATOM   455  C CA  . ALA   A 1 54  ? 27.400  -3.599  -47.863 1.00 16.69 ? 56  ALA   A CA  1 
ATOM   456  C C   . ALA   A 1 54  ? 27.550  -3.281  -49.340 1.00 19.51 ? 56  ALA   A C   1 
ATOM   457  O O   . ALA   A 1 54  ? 26.578  -2.993  -50.044 1.00 20.85 ? 56  ALA   A O   1 
ATOM   458  C CB  . ALA   A 1 54  ? 27.791  -5.058  -47.586 1.00 20.84 ? 56  ALA   A CB  1 
ATOM   459  N N   . ILE   A 1 55  ? 28.794  -3.330  -49.804 1.00 22.85 ? 57  ILE   A N   1 
ATOM   460  C CA  . ILE   A 1 55  ? 29.119  -3.165  -51.211 1.00 21.63 ? 57  ILE   A CA  1 
ATOM   461  C C   . ILE   A 1 55  ? 29.809  -4.431  -51.682 1.00 21.13 ? 57  ILE   A C   1 
ATOM   462  O O   . ILE   A 1 55  ? 30.707  -4.947  -51.003 1.00 20.46 ? 57  ILE   A O   1 
ATOM   463  C CB  . ILE   A 1 55  ? 30.002  -1.930  -51.460 1.00 25.71 ? 57  ILE   A CB  1 
ATOM   464  C CG1 . ILE   A 1 55  ? 29.228  -0.656  -51.130 1.00 33.39 ? 57  ILE   A CG1 1 
ATOM   465  C CG2 . ILE   A 1 55  ? 30.494  -1.909  -52.903 1.00 26.41 ? 57  ILE   A CG2 1 
ATOM   466  C CD1 . ILE   A 1 55  ? 29.986  0.612   -51.444 1.00 45.88 ? 57  ILE   A CD1 1 
ATOM   467  N N   . ASN   A 1 56  ? 29.362  -4.944  -52.818 1.00 18.22 ? 58  ASN   A N   1 
ATOM   468  C CA  . ASN   A 1 56  ? 30.041  -6.024  -53.521 1.00 18.27 ? 58  ASN   A CA  1 
ATOM   469  C C   . ASN   A 1 56  ? 31.115  -5.387  -54.385 1.00 21.32 ? 58  ASN   A C   1 
ATOM   470  O O   . ASN   A 1 56  ? 30.805  -4.774  -55.412 1.00 23.05 ? 58  ASN   A O   1 
ATOM   471  C CB  . ASN   A 1 56  ? 29.026  -6.797  -54.359 1.00 22.12 ? 58  ASN   A CB  1 
ATOM   472  C CG  . ASN   A 1 56  ? 29.636  -7.963  -55.111 1.00 22.78 ? 58  ASN   A CG  1 
ATOM   473  O OD1 . ASN   A 1 56  ? 30.859  -8.078  -55.241 1.00 22.92 ? 58  ASN   A OD1 1 
ATOM   474  N ND2 . ASN   A 1 56  ? 28.775  -8.831  -55.630 1.00 27.28 ? 58  ASN   A ND2 1 
ATOM   475  N N   . ILE   A 1 57  ? 32.382  -5.533  -53.985 1.00 21.05 ? 59  ILE   A N   1 
ATOM   476  C CA  . ILE   A 1 57  ? 33.449  -4.831  -54.699 1.00 20.18 ? 59  ILE   A CA  1 
ATOM   477  C C   . ILE   A 1 57  ? 33.836  -5.504  -56.007 1.00 23.58 ? 59  ILE   A C   1 
ATOM   478  O O   . ILE   A 1 57  ? 34.738  -5.009  -56.698 1.00 25.14 ? 59  ILE   A O   1 
ATOM   479  C CB  . ILE   A 1 57  ? 34.691  -4.646  -53.805 1.00 26.25 ? 59  ILE   A CB  1 
ATOM   480  C CG1 . ILE   A 1 57  ? 35.346  -5.983  -53.489 1.00 21.26 ? 59  ILE   A CG1 1 
ATOM   481  C CG2 . ILE   A 1 57  ? 34.308  -3.908  -52.534 1.00 23.31 ? 59  ILE   A CG2 1 
ATOM   482  C CD1 . ILE   A 1 57  ? 36.765  -5.835  -52.899 1.00 24.76 ? 59  ILE   A CD1 1 
ATOM   483  N N   . THR   A 1 58  ? 33.186  -6.608  -56.386 1.00 26.16 ? 60  THR   A N   1 
ATOM   484  C CA  . THR   A 1 58  ? 33.403  -7.158  -57.721 1.00 26.18 ? 60  THR   A CA  1 
ATOM   485  C C   . THR   A 1 58  ? 32.511  -6.504  -58.770 1.00 28.84 ? 60  THR   A C   1 
ATOM   486  O O   . THR   A 1 58  ? 32.792  -6.639  -59.968 1.00 30.40 ? 60  THR   A O   1 
ATOM   487  C CB  . THR   A 1 58  ? 33.188  -8.680  -57.736 1.00 27.25 ? 60  THR   A CB  1 
ATOM   488  O OG1 . THR   A 1 58  ? 31.800  -8.980  -57.562 1.00 31.48 ? 60  THR   A OG1 1 
ATOM   489  C CG2 . THR   A 1 58  ? 33.988  -9.343  -56.631 1.00 31.52 ? 60  THR   A CG2 1 
ATOM   490  N N   . ASN   A 1 59  ? 31.459  -5.788  -58.353 1.00 29.13 ? 61  ASN   A N   1 
ATOM   491  C CA  . ASN   A 1 59  ? 30.627  -5.022  -59.274 1.00 26.98 ? 61  ASN   A CA  1 
ATOM   492  C C   . ASN   A 1 59  ? 30.247  -3.651  -58.730 1.00 23.98 ? 61  ASN   A C   1 
ATOM   493  O O   . ASN   A 1 59  ? 29.471  -2.943  -59.381 1.00 30.03 ? 61  ASN   A O   1 
ATOM   494  C CB  . ASN   A 1 59  ? 29.353  -5.798  -59.642 1.00 28.02 ? 61  ASN   A CB  1 
ATOM   495  C CG  . ASN   A 1 59  ? 28.509  -6.168  -58.430 1.00 27.76 ? 61  ASN   A CG  1 
ATOM   496  O OD1 . ASN   A 1 59  ? 28.635  -5.575  -57.360 1.00 27.99 ? 61  ASN   A OD1 1 
ATOM   497  N ND2 . ASN   A 1 59  ? 27.636  -7.155  -58.604 1.00 31.20 ? 61  ASN   A ND2 1 
ATOM   498  N N   . ASN   A 1 60  ? 30.773  -3.258  -57.569 1.00 25.55 ? 62  ASN   A N   1 
ATOM   499  C CA  . ASN   A 1 60  ? 30.464  -1.982  -56.914 1.00 22.73 ? 62  ASN   A CA  1 
ATOM   500  C C   . ASN   A 1 60  ? 28.963  -1.770  -56.744 1.00 24.49 ? 62  ASN   A C   1 
ATOM   501  O O   . ASN   A 1 60  ? 28.467  -0.644  -56.821 1.00 35.81 ? 62  ASN   A O   1 
ATOM   502  C CB  . ASN   A 1 60  ? 31.111  -0.802  -57.647 1.00 25.72 ? 62  ASN   A CB  1 
ATOM   503  C CG  . ASN   A 1 60  ? 32.621  -0.742  -57.432 1.00 34.41 ? 62  ASN   A CG  1 
ATOM   504  O OD1 . ASN   A 1 60  ? 33.339  -0.044  -58.153 1.00 40.91 ? 62  ASN   A OD1 1 
ATOM   505  N ND2 . ASN   A 1 60  ? 33.109  -1.488  -56.441 1.00 28.33 ? 62  ASN   A ND2 1 
ATOM   506  N N   . GLU   A 1 61  ? 28.236  -2.845  -56.467 1.00 23.77 ? 63  GLU   A N   1 
ATOM   507  C CA  . GLU   A 1 61  ? 26.801  -2.771  -56.242 1.00 29.25 ? 63  GLU   A CA  1 
ATOM   508  C C   . GLU   A 1 61  ? 26.483  -2.959  -54.766 1.00 28.28 ? 63  GLU   A C   1 
ATOM   509  O O   . GLU   A 1 61  ? 27.173  -3.690  -54.048 1.00 24.65 ? 63  GLU   A O   1 
ATOM   510  C CB  . GLU   A 1 61  ? 26.057  -3.818  -57.075 1.00 37.33 ? 63  GLU   A CB  1 
ATOM   511  C CG  . GLU   A 1 61  ? 26.063  -3.502  -58.562 1.00 47.95 ? 63  GLU   A CG  1 
ATOM   512  C CD  . GLU   A 1 61  ? 25.503  -4.624  -59.412 1.00 61.22 ? 63  GLU   A CD  1 
ATOM   513  O OE1 . GLU   A 1 61  ? 25.035  -5.634  -58.844 1.00 64.17 ? 63  GLU   A OE1 1 
ATOM   514  O OE2 . GLU   A 1 61  ? 25.537  -4.494  -60.655 1.00 61.47 ? 63  GLU   A OE2 1 
ATOM   515  N N   . LYS   A 1 62  ? 25.432  -2.280  -54.316 1.00 27.52 ? 64  LYS   A N   1 
ATOM   516  C CA  . LYS   A 1 62  ? 24.963  -2.471  -52.955 1.00 22.31 ? 64  LYS   A CA  1 
ATOM   517  C C   . LYS   A 1 62  ? 24.358  -3.854  -52.787 1.00 22.52 ? 64  LYS   A C   1 
ATOM   518  O O   . LYS   A 1 62  ? 23.673  -4.371  -53.675 1.00 21.99 ? 64  LYS   A O   1 
ATOM   519  C CB  . LYS   A 1 62  ? 23.933  -1.408  -52.583 1.00 23.56 ? 64  LYS   A CB  1 
ATOM   520  C CG  . LYS   A 1 62  ? 24.503  -0.014  -52.478 1.00 31.14 ? 64  LYS   A CG  1 
ATOM   521  C CD  . LYS   A 1 62  ? 23.457  0.966   -51.990 1.00 38.45 ? 64  LYS   A CD  1 
ATOM   522  C CE  . LYS   A 1 62  ? 24.029  2.366   -51.924 1.00 44.88 ? 64  LYS   A CE  1 
ATOM   523  N NZ  . LYS   A 1 62  ? 22.999  3.351   -51.522 1.00 47.62 ? 64  LYS   A NZ  1 
ATOM   524  N N   . VAL   A 1 63  ? 24.622  -4.453  -51.631 1.00 17.51 ? 65  VAL   A N   1 
ATOM   525  C CA  . VAL   A 1 63  ? 24.023  -5.711  -51.219 1.00 17.49 ? 65  VAL   A CA  1 
ATOM   526  C C   . VAL   A 1 63  ? 23.659  -5.561  -49.752 1.00 16.22 ? 65  VAL   A C   1 
ATOM   527  O O   . VAL   A 1 63  ? 24.026  -4.584  -49.096 1.00 18.36 ? 65  VAL   A O   1 
ATOM   528  C CB  . VAL   A 1 63  ? 24.959  -6.920  -51.422 1.00 16.44 ? 65  VAL   A CB  1 
ATOM   529  C CG1 . VAL   A 1 63  ? 25.222  -7.158  -52.899 1.00 22.43 ? 65  VAL   A CG1 1 
ATOM   530  C CG2 . VAL   A 1 63  ? 26.285  -6.693  -50.680 1.00 17.90 ? 65  VAL   A CG2 1 
ATOM   531  N N   . VAL   A 1 64  ? 22.933  -6.544  -49.234 1.00 17.32 ? 66  VAL   A N   1 
ATOM   532  C CA  . VAL   A 1 64  ? 22.578  -6.595  -47.821 1.00 15.28 ? 66  VAL   A CA  1 
ATOM   533  C C   . VAL   A 1 64  ? 23.157  -7.875  -47.241 1.00 17.14 ? 66  VAL   A C   1 
ATOM   534  O O   . VAL   A 1 64  ? 23.020  -8.951  -47.829 1.00 18.65 ? 66  VAL   A O   1 
ATOM   535  C CB  . VAL   A 1 64  ? 21.053  -6.510  -47.617 1.00 16.27 ? 66  VAL   A CB  1 
ATOM   536  C CG1 . VAL   A 1 64  ? 20.681  -6.847  -46.176 1.00 19.34 ? 66  VAL   A CG1 1 
ATOM   537  C CG2 . VAL   A 1 64  ? 20.580  -5.105  -47.970 1.00 17.79 ? 66  VAL   A CG2 1 
ATOM   538  N N   . VAL   A 1 65  ? 23.852  -7.755  -46.116 1.00 16.73 ? 67  VAL   A N   1 
ATOM   539  C CA  . VAL   A 1 65  ? 24.524  -8.890  -45.505 1.00 14.45 ? 67  VAL   A CA  1 
ATOM   540  C C   . VAL   A 1 65  ? 23.872  -9.171  -44.163 1.00 18.21 ? 67  VAL   A C   1 
ATOM   541  O O   . VAL   A 1 65  ? 23.836  -8.297  -43.287 1.00 16.88 ? 67  VAL   A O   1 
ATOM   542  C CB  . VAL   A 1 65  ? 26.026  -8.633  -45.333 1.00 14.69 ? 67  VAL   A CB  1 
ATOM   543  C CG1 . VAL   A 1 65  ? 26.657  -9.805  -44.575 1.00 18.54 ? 67  VAL   A CG1 1 
ATOM   544  C CG2 . VAL   A 1 65  ? 26.659  -8.416  -46.686 1.00 16.65 ? 67  VAL   A CG2 1 
ATOM   545  N N   . LYS   A 1 66  ? 23.384  -10.398 -43.991 1.00 14.64 ? 68  LYS   A N   1 
ATOM   546  C CA  . LYS   A 1 66  ? 22.812  -10.853 -42.728 1.00 14.04 ? 68  LYS   A CA  1 
ATOM   547  C C   . LYS   A 1 66  ? 23.801  -11.804 -42.059 1.00 16.29 ? 68  LYS   A C   1 
ATOM   548  O O   . LYS   A 1 66  ? 24.010  -12.931 -42.526 1.00 16.95 ? 68  LYS   A O   1 
ATOM   549  C CB  . LYS   A 1 66  ? 21.462  -11.521 -42.982 1.00 16.74 ? 68  LYS   A CB  1 
ATOM   550  C CG  . LYS   A 1 66  ? 20.788  -12.126 -41.770 1.00 18.85 ? 68  LYS   A CG  1 
ATOM   551  C CD  . LYS   A 1 66  ? 19.308  -12.300 -42.053 1.00 30.24 ? 68  LYS   A CD  1 
ATOM   552  C CE  . LYS   A 1 66  ? 18.890  -13.748 -42.027 1.00 35.20 ? 68  LYS   A CE  1 
ATOM   553  N NZ  . LYS   A 1 66  ? 17.397  -13.870 -42.117 1.00 20.66 ? 68  LYS   A NZ  1 
ATOM   554  N N   . ILE   A 1 67  ? 24.430  -11.343 -40.985 1.00 16.28 ? 69  ILE   A N   1 
ATOM   555  C CA  . ILE   A 1 67  ? 25.427  -12.144 -40.276 1.00 16.64 ? 69  ILE   A CA  1 
ATOM   556  C C   . ILE   A 1 67  ? 24.700  -12.861 -39.150 1.00 21.55 ? 69  ILE   A C   1 
ATOM   557  O O   . ILE   A 1 67  ? 24.216  -12.226 -38.208 1.00 20.67 ? 69  ILE   A O   1 
ATOM   558  C CB  . ILE   A 1 67  ? 26.584  -11.292 -39.748 1.00 19.41 ? 69  ILE   A CB  1 
ATOM   559  C CG1 . ILE   A 1 67  ? 27.243  -10.554 -40.912 1.00 17.70 ? 69  ILE   A CG1 1 
ATOM   560  C CG2 . ILE   A 1 67  ? 27.618  -12.179 -39.063 1.00 20.52 ? 69  ILE   A CG2 1 
ATOM   561  C CD1 . ILE   A 1 67  ? 28.417  -9.690  -40.504 1.00 17.77 ? 69  ILE   A CD1 1 
ATOM   562  N N   . LEU   A 1 68  ? 24.609  -14.181 -39.254 1.00 20.53 ? 70  LEU   A N   1 
ATOM   563  C CA  . LEU   A 1 68  ? 23.783  -14.930 -38.324 1.00 24.27 ? 70  LEU   A CA  1 
ATOM   564  C C   . LEU   A 1 68  ? 24.436  -14.986 -36.953 1.00 26.30 ? 70  LEU   A C   1 
ATOM   565  O O   . LEU   A 1 68  ? 25.660  -15.107 -36.828 1.00 28.58 ? 70  LEU   A O   1 
ATOM   566  C CB  . LEU   A 1 68  ? 23.527  -16.345 -38.845 1.00 22.93 ? 70  LEU   A CB  1 
ATOM   567  C CG  . LEU   A 1 68  ? 22.855  -16.449 -40.217 1.00 22.91 ? 70  LEU   A CG  1 
ATOM   568  C CD1 . LEU   A 1 68  ? 22.654  -17.905 -40.593 1.00 27.09 ? 70  LEU   A CD1 1 
ATOM   569  C CD2 . LEU   A 1 68  ? 21.525  -15.697 -40.240 1.00 28.37 ? 70  LEU   A CD2 1 
ATOM   570  N N   . LYS   A 1 69  ? 23.616  -14.860 -35.919 1.00 28.74 ? 71  LYS   A N   1 
ATOM   571  C CA  . LYS   A 1 69  ? 24.079  -15.152 -34.583 1.00 31.07 ? 71  LYS   A CA  1 
ATOM   572  C C   . LYS   A 1 69  ? 24.156  -16.667 -34.416 1.00 27.36 ? 71  LYS   A C   1 
ATOM   573  O O   . LYS   A 1 69  ? 23.577  -17.415 -35.206 1.00 31.89 ? 71  LYS   A O   1 
ATOM   574  C CB  . LYS   A 1 69  ? 23.152  -14.515 -33.547 1.00 34.12 ? 71  LYS   A CB  1 
ATOM   575  C CG  . LYS   A 1 69  ? 23.291  -12.995 -33.482 1.00 37.26 ? 71  LYS   A CG  1 
ATOM   576  C CD  . LYS   A 1 69  ? 22.492  -12.382 -32.345 1.00 44.10 ? 71  LYS   A CD  1 
ATOM   577  C CE  . LYS   A 1 69  ? 22.744  -10.882 -32.262 1.00 46.28 ? 71  LYS   A CE  1 
ATOM   578  N NZ  . LYS   A 1 69  ? 22.082  -10.267 -31.076 1.00 51.27 ? 71  LYS   A NZ  1 
ATOM   579  N N   . PRO   A 1 70  ? 24.908  -17.149 -33.429 1.00 41.52 ? 72  PRO   A N   1 
ATOM   580  C CA  . PRO   A 1 70  ? 24.980  -18.602 -33.206 1.00 49.56 ? 72  PRO   A CA  1 
ATOM   581  C C   . PRO   A 1 70  ? 23.601  -19.215 -33.002 1.00 53.98 ? 72  PRO   A C   1 
ATOM   582  O O   . PRO   A 1 70  ? 22.897  -18.907 -32.039 1.00 57.58 ? 72  PRO   A O   1 
ATOM   583  C CB  . PRO   A 1 70  ? 25.851  -18.717 -31.951 1.00 50.34 ? 72  PRO   A CB  1 
ATOM   584  C CG  . PRO   A 1 70  ? 26.744  -17.523 -32.028 1.00 49.33 ? 72  PRO   A CG  1 
ATOM   585  C CD  . PRO   A 1 70  ? 25.908  -16.418 -32.628 1.00 42.05 ? 72  PRO   A CD  1 
ATOM   586  N N   . VAL   A 1 71  ? 23.215  -20.084 -33.938 1.00 58.67 ? 73  VAL   A N   1 
ATOM   587  C CA  . VAL   A 1 71  ? 21.990  -20.871 -33.858 1.00 61.29 ? 73  VAL   A CA  1 
ATOM   588  C C   . VAL   A 1 71  ? 22.292  -22.240 -34.461 1.00 60.75 ? 73  VAL   A C   1 
ATOM   589  O O   . VAL   A 1 71  ? 23.324  -22.443 -35.103 1.00 59.58 ? 73  VAL   A O   1 
ATOM   590  C CB  . VAL   A 1 71  ? 20.803  -20.187 -34.574 1.00 60.87 ? 73  VAL   A CB  1 
ATOM   591  C CG1 . VAL   A 1 71  ? 20.920  -20.339 -36.082 1.00 59.83 ? 73  VAL   A CG1 1 
ATOM   592  C CG2 . VAL   A 1 71  ? 19.466  -20.720 -34.060 1.00 64.27 ? 73  VAL   A CG2 1 
ATOM   593  N N   . LYS   A 1 72  ? 21.386  -23.191 -34.238 1.00 58.77 ? 74  LYS   A N   1 
ATOM   594  C CA  . LYS   A 1 72  ? 21.678  -24.573 -34.596 1.00 59.91 ? 74  LYS   A CA  1 
ATOM   595  C C   . LYS   A 1 72  ? 21.854  -24.726 -36.103 1.00 56.55 ? 74  LYS   A C   1 
ATOM   596  O O   . LYS   A 1 72  ? 21.155  -24.093 -36.900 1.00 52.38 ? 74  LYS   A O   1 
ATOM   597  C CB  . LYS   A 1 72  ? 20.578  -25.508 -34.093 1.00 64.17 ? 74  LYS   A CB  1 
ATOM   598  C CG  . LYS   A 1 72  ? 21.133  -26.728 -33.362 1.00 67.73 ? 74  LYS   A CG  1 
ATOM   599  C CD  . LYS   A 1 72  ? 20.226  -27.939 -33.503 1.00 68.89 ? 74  LYS   A CD  1 
ATOM   600  C CE  . LYS   A 1 72  ? 20.109  -28.368 -34.955 1.00 65.75 ? 74  LYS   A CE  1 
ATOM   601  N NZ  . LYS   A 1 72  ? 21.441  -28.550 -35.600 1.00 62.77 ? 74  LYS   A NZ  1 
ATOM   602  N N   . LYS   A 1 73  ? 22.799  -25.592 -36.479 1.00 57.33 ? 75  LYS   A N   1 
ATOM   603  C CA  . LYS   A 1 73  ? 23.216  -25.729 -37.871 1.00 55.83 ? 75  LYS   A CA  1 
ATOM   604  C C   . LYS   A 1 73  ? 22.058  -26.111 -38.786 1.00 48.66 ? 75  LYS   A C   1 
ATOM   605  O O   . LYS   A 1 73  ? 22.052  -25.738 -39.966 1.00 42.46 ? 75  LYS   A O   1 
ATOM   606  C CB  . LYS   A 1 73  ? 24.348  -26.759 -37.957 1.00 58.03 ? 75  LYS   A CB  1 
ATOM   607  C CG  . LYS   A 1 73  ? 24.756  -27.206 -39.354 1.00 59.42 ? 75  LYS   A CG  1 
ATOM   608  C CD  . LYS   A 1 73  ? 26.068  -27.990 -39.295 1.00 62.89 ? 75  LYS   A CD  1 
ATOM   609  C CE  . LYS   A 1 73  ? 26.077  -29.175 -40.252 1.00 65.33 ? 75  LYS   A CE  1 
ATOM   610  N NZ  . LYS   A 1 73  ? 25.056  -30.202 -39.894 1.00 66.95 ? 75  LYS   A NZ  1 
ATOM   611  N N   . LYS   A 1 74  ? 21.067  -26.841 -38.268 1.00 39.07 ? 76  LYS   A N   1 
ATOM   612  C CA  . LYS   A 1 74  ? 19.962  -27.252 -39.125 1.00 38.33 ? 76  LYS   A CA  1 
ATOM   613  C C   . LYS   A 1 74  ? 19.068  -26.071 -39.483 1.00 30.04 ? 76  LYS   A C   1 
ATOM   614  O O   . LYS   A 1 74  ? 18.537  -26.019 -40.598 1.00 29.74 ? 76  LYS   A O   1 
ATOM   615  C CB  . LYS   A 1 74  ? 19.161  -28.380 -38.463 1.00 48.84 ? 76  LYS   A CB  1 
ATOM   616  C CG  . LYS   A 1 74  ? 17.901  -27.953 -37.725 1.00 54.53 ? 76  LYS   A CG  1 
ATOM   617  C CD  . LYS   A 1 74  ? 17.086  -29.158 -37.268 1.00 56.76 ? 76  LYS   A CD  1 
ATOM   618  C CE  . LYS   A 1 74  ? 15.753  -28.722 -36.664 1.00 60.44 ? 76  LYS   A CE  1 
ATOM   619  N NZ  . LYS   A 1 74  ? 14.911  -29.877 -36.234 1.00 61.91 ? 76  LYS   A NZ  1 
ATOM   620  N N   . LYS   A 1 75  ? 18.917  -25.102 -38.574 1.00 25.66 ? 77  LYS   A N   1 
ATOM   621  C CA  . LYS   A 1 75  ? 18.100  -23.928 -38.871 1.00 30.06 ? 77  LYS   A CA  1 
ATOM   622  C C   . LYS   A 1 75  ? 18.788  -23.013 -39.876 1.00 28.79 ? 77  LYS   A C   1 
ATOM   623  O O   . LYS   A 1 75  ? 18.119  -22.401 -40.722 1.00 26.76 ? 77  LYS   A O   1 
ATOM   624  C CB  . LYS   A 1 75  ? 17.786  -23.176 -37.577 1.00 38.96 ? 77  LYS   A CB  1 
ATOM   625  C CG  . LYS   A 1 75  ? 17.110  -21.830 -37.770 1.00 48.55 ? 77  LYS   A CG  1 
ATOM   626  C CD  . LYS   A 1 75  ? 16.649  -21.242 -36.441 1.00 52.39 ? 77  LYS   A CD  1 
ATOM   627  C CE  . LYS   A 1 75  ? 16.132  -19.821 -36.615 1.00 52.05 ? 77  LYS   A CE  1 
ATOM   628  N NZ  . LYS   A 1 75  ? 16.160  -19.398 -38.045 1.00 49.48 ? 77  LYS   A NZ  1 
ATOM   629  N N   . ILE   A 1 76  ? 20.116  -22.911 -39.799 1.00 24.96 ? 78  ILE   A N   1 
ATOM   630  C CA  . ILE   A 1 76  ? 20.874  -22.193 -40.817 1.00 24.49 ? 78  ILE   A CA  1 
ATOM   631  C C   . ILE   A 1 76  ? 20.724  -22.878 -42.167 1.00 26.40 ? 78  ILE   A C   1 
ATOM   632  O O   . ILE   A 1 76  ? 20.506  -22.227 -43.198 1.00 20.97 ? 78  ILE   A O   1 
ATOM   633  C CB  . ILE   A 1 76  ? 22.353  -22.096 -40.407 1.00 26.80 ? 78  ILE   A CB  1 
ATOM   634  C CG1 . ILE   A 1 76  ? 22.483  -21.375 -39.068 1.00 33.13 ? 78  ILE   A CG1 1 
ATOM   635  C CG2 . ILE   A 1 76  ? 23.163  -21.400 -41.491 1.00 32.07 ? 78  ILE   A CG2 1 
ATOM   636  C CD1 . ILE   A 1 76  ? 23.893  -21.382 -38.510 1.00 36.17 ? 78  ILE   A CD1 1 
ATOM   637  N N   . LYS   A 1 77  ? 20.868  -24.207 -42.184 1.00 20.95 ? 79  LYS   A N   1 
ATOM   638  C CA  . LYS   A 1 77  ? 20.740  -24.939 -43.437 1.00 22.62 ? 79  LYS   A CA  1 
ATOM   639  C C   . LYS   A 1 77  ? 19.327  -24.855 -43.989 1.00 17.46 ? 79  LYS   A C   1 
ATOM   640  O O   . LYS   A 1 77  ? 19.138  -24.851 -45.210 1.00 18.64 ? 79  LYS   A O   1 
ATOM   641  C CB  . LYS   A 1 77  ? 21.126  -26.402 -43.242 1.00 23.70 ? 79  LYS   A CB  1 
ATOM   642  C CG  . LYS   A 1 77  ? 22.617  -26.623 -43.081 1.00 24.63 ? 79  LYS   A CG  1 
ATOM   643  C CD  . LYS   A 1 77  ? 22.976  -28.075 -43.350 1.00 27.02 ? 79  LYS   A CD  1 
ATOM   644  C CE  . LYS   A 1 77  ? 24.478  -28.277 -43.301 1.00 42.17 ? 79  LYS   A CE  1 
ATOM   645  N NZ  . LYS   A 1 77  ? 24.851  -29.661 -43.701 1.00 49.30 ? 79  LYS   A NZ  1 
ATOM   646  N N   . ARG   A 1 78  ? 18.325  -24.815 -43.106 1.00 21.22 ? 80  ARG   A N   1 
ATOM   647  C CA  . ARG   A 1 78  ? 16.942  -24.713 -43.549 1.00 21.51 ? 80  ARG   A CA  1 
ATOM   648  C C   . ARG   A 1 78  ? 16.707  -23.402 -44.286 1.00 16.58 ? 80  ARG   A C   1 
ATOM   649  O O   . ARG   A 1 78  ? 16.136  -23.391 -45.380 1.00 15.82 ? 80  ARG   A O   1 
ATOM   650  C CB  . ARG   A 1 78  ? 16.006  -24.842 -42.349 1.00 17.76 ? 80  ARG   A CB  1 
ATOM   651  C CG  . ARG   A 1 78  ? 14.537  -24.788 -42.714 1.00 18.16 ? 80  ARG   A CG  1 
ATOM   652  C CD  . ARG   A 1 78  ? 13.666  -24.951 -41.484 1.00 19.60 ? 80  ARG   A CD  1 
ATOM   653  N NE  . ARG   A 1 78  ? 13.719  -23.741 -40.666 1.00 20.37 ? 80  ARG   A NE  1 
ATOM   654  C CZ  . ARG   A 1 78  ? 13.181  -23.629 -39.455 1.00 21.88 ? 80  ARG   A CZ  1 
ATOM   655  N NH1 . ARG   A 1 78  ? 12.576  -24.666 -38.892 1.00 26.00 ? 80  ARG   A NH1 1 
ATOM   656  N NH2 . ARG   A 1 78  ? 13.269  -22.478 -38.801 1.00 24.81 ? 80  ARG   A NH2 1 
ATOM   657  N N   . GLU   A 1 79  ? 17.148  -22.284 -43.697 1.00 15.50 ? 81  GLU   A N   1 
ATOM   658  C CA  . GLU   A 1 79  ? 16.965  -20.987 -44.350 1.00 16.52 ? 81  GLU   A CA  1 
ATOM   659  C C   . GLU   A 1 79  ? 17.730  -20.922 -45.671 1.00 15.77 ? 81  GLU   A C   1 
ATOM   660  O O   . GLU   A 1 79  ? 17.200  -20.446 -46.681 1.00 16.72 ? 81  GLU   A O   1 
ATOM   661  C CB  . GLU   A 1 79  ? 17.398  -19.855 -43.418 1.00 18.07 ? 81  GLU   A CB  1 
ATOM   662  C CG  . GLU   A 1 79  ? 17.173  -18.468 -44.023 1.00 17.33 ? 81  GLU   A CG  1 
ATOM   663  C CD  . GLU   A 1 79  ? 17.510  -17.300 -43.111 1.00 18.12 ? 81  GLU   A CD  1 
ATOM   664  O OE1 . GLU   A 1 79  ? 17.955  -17.506 -41.959 1.00 18.71 ? 81  GLU   A OE1 1 
ATOM   665  O OE2 . GLU   A 1 79  ? 17.324  -16.152 -43.564 1.00 19.64 ? 81  GLU   A OE2 1 
ATOM   666  N N   . ILE   A 1 80  ? 18.978  -21.399 -45.682 1.00 16.80 ? 82  ILE   A N   1 
ATOM   667  C CA  . ILE   A 1 80  ? 19.777  -21.404 -46.906 1.00 18.04 ? 82  ILE   A CA  1 
ATOM   668  C C   . ILE   A 1 80  ? 19.103  -22.235 -47.990 1.00 16.20 ? 82  ILE   A C   1 
ATOM   669  O O   . ILE   A 1 80  ? 18.946  -21.790 -49.133 1.00 17.45 ? 82  ILE   A O   1 
ATOM   670  C CB  . ILE   A 1 80  ? 21.194  -21.926 -46.610 1.00 17.17 ? 82  ILE   A CB  1 
ATOM   671  C CG1 . ILE   A 1 80  ? 21.966  -20.935 -45.737 1.00 19.26 ? 82  ILE   A CG1 1 
ATOM   672  C CG2 . ILE   A 1 80  ? 21.920  -22.263 -47.917 1.00 23.17 ? 82  ILE   A CG2 1 
ATOM   673  C CD1 . ILE   A 1 80  ? 23.332  -21.453 -45.268 1.00 20.94 ? 82  ILE   A CD1 1 
ATOM   674  N N   . LYS   A 1 81  ? 18.678  -23.459 -47.645 1.00 16.98 ? 83  LYS   A N   1 
ATOM   675  C CA  . LYS   A 1 81  ? 18.065  -24.330 -48.645 1.00 19.37 ? 83  LYS   A CA  1 
ATOM   676  C C   . LYS   A 1 81  ? 16.779  -23.729 -49.191 1.00 15.68 ? 83  LYS   A C   1 
ATOM   677  O O   . LYS   A 1 81  ? 16.520  -23.788 -50.397 1.00 17.27 ? 83  LYS   A O   1 
ATOM   678  C CB  . LYS   A 1 81  ? 17.801  -25.717 -48.061 1.00 22.41 ? 83  LYS   A CB  1 
ATOM   679  C CG  . LYS   A 1 81  ? 17.301  -26.727 -49.094 1.00 19.79 ? 83  LYS   A CG  1 
ATOM   680  C CD  . LYS   A 1 81  ? 18.406  -27.122 -50.092 1.00 22.80 ? 83  LYS   A CD  1 
ATOM   681  C CE  . LYS   A 1 81  ? 17.814  -27.853 -51.289 1.00 23.71 ? 83  LYS   A CE  1 
ATOM   682  N NZ  . LYS   A 1 81  ? 18.854  -28.267 -52.274 1.00 28.76 ? 83  LYS   A NZ  1 
ATOM   683  N N   . ILE   A 1 82  ? 15.958  -23.141 -48.312 1.00 16.47 ? 84  ILE   A N   1 
ATOM   684  C CA  . ILE   A 1 82  ? 14.724  -22.511 -48.759 1.00 16.37 ? 84  ILE   A CA  1 
ATOM   685  C C   . ILE   A 1 82  ? 15.017  -21.346 -49.700 1.00 16.99 ? 84  ILE   A C   1 
ATOM   686  O O   . ILE   A 1 82  ? 14.383  -21.208 -50.754 1.00 16.32 ? 84  ILE   A O   1 
ATOM   687  C CB  . ILE   A 1 82  ? 13.888  -22.097 -47.531 1.00 15.59 ? 84  ILE   A CB  1 
ATOM   688  C CG1 . ILE   A 1 82  ? 13.314  -23.375 -46.905 1.00 19.35 ? 84  ILE   A CG1 1 
ATOM   689  C CG2 . ILE   A 1 82  ? 12.802  -21.106 -47.918 1.00 17.57 ? 84  ILE   A CG2 1 
ATOM   690  C CD1 . ILE   A 1 82  ? 12.533  -23.162 -45.628 1.00 16.71 ? 84  ILE   A CD1 1 
ATOM   691  N N   . LEU   A 1 83  ? 15.988  -20.499 -49.347 1.00 16.08 ? 85  LEU   A N   1 
ATOM   692  C CA  . LEU   A 1 83  ? 16.337  -19.373 -50.211 1.00 14.14 ? 85  LEU   A CA  1 
ATOM   693  C C   . LEU   A 1 83  ? 16.866  -19.844 -51.562 1.00 15.06 ? 85  LEU   A C   1 
ATOM   694  O O   . LEU   A 1 83  ? 16.552  -19.251 -52.605 1.00 17.17 ? 85  LEU   A O   1 
ATOM   695  C CB  . LEU   A 1 83  ? 17.371  -18.492 -49.517 1.00 15.73 ? 85  LEU   A CB  1 
ATOM   696  C CG  . LEU   A 1 83  ? 16.873  -17.635 -48.357 1.00 15.68 ? 85  LEU   A CG  1 
ATOM   697  C CD1 . LEU   A 1 83  ? 18.065  -17.128 -47.537 1.00 15.90 ? 85  LEU   A CD1 1 
ATOM   698  C CD2 . LEU   A 1 83  ? 16.034  -16.472 -48.884 1.00 17.00 ? 85  LEU   A CD2 1 
ATOM   699  N N   . GLU   A 1 84  ? 17.655  -20.920 -51.566 1.00 18.32 ? 86  GLU   A N   1 
ATOM   700  C CA  . GLU   A 1 84  ? 18.135  -21.451 -52.836 1.00 21.22 ? 86  GLU   A CA  1 
ATOM   701  C C   . GLU   A 1 84  ? 17.003  -22.083 -53.634 1.00 20.82 ? 86  GLU   A C   1 
ATOM   702  O O   . GLU   A 1 84  ? 16.936  -21.915 -54.856 1.00 19.01 ? 86  GLU   A O   1 
ATOM   703  C CB  . GLU   A 1 84  ? 19.265  -22.444 -52.596 1.00 20.33 ? 86  GLU   A CB  1 
ATOM   704  C CG  . GLU   A 1 84  ? 20.533  -21.735 -52.135 1.00 22.57 ? 86  GLU   A CG  1 
ATOM   705  C CD  . GLU   A 1 84  ? 21.722  -22.659 -52.009 1.00 30.43 ? 86  GLU   A CD  1 
ATOM   706  O OE1 . GLU   A 1 84  ? 21.582  -23.870 -52.294 1.00 31.72 ? 86  GLU   A OE1 1 
ATOM   707  O OE2 . GLU   A 1 84  ? 22.803  -22.162 -51.623 1.00 30.18 ? 86  GLU   A OE2 1 
ATOM   708  N N   . ASN   A 1 85  ? 16.071  -22.766 -52.959 1.00 19.14 ? 87  ASN   A N   1 
ATOM   709  C CA  . ASN   A 1 85  ? 14.955  -23.379 -53.678 1.00 19.30 ? 87  ASN   A CA  1 
ATOM   710  C C   . ASN   A 1 85  ? 14.066  -22.332 -54.334 1.00 16.59 ? 87  ASN   A C   1 
ATOM   711  O O   . ASN   A 1 85  ? 13.544  -22.552 -55.433 1.00 17.77 ? 87  ASN   A O   1 
ATOM   712  C CB  . ASN   A 1 85  ? 14.112  -24.239 -52.736 1.00 17.69 ? 87  ASN   A CB  1 
ATOM   713  C CG  . ASN   A 1 85  ? 14.770  -25.562 -52.401 1.00 18.42 ? 87  ASN   A CG  1 
ATOM   714  O OD1 . ASN   A 1 85  ? 15.753  -25.953 -53.021 1.00 21.74 ? 87  ASN   A OD1 1 
ATOM   715  N ND2 . ASN   A 1 85  ? 14.221  -26.262 -51.411 1.00 19.76 ? 87  ASN   A ND2 1 
ATOM   716  N N   . LEU   A 1 86  ? 13.876  -21.190 -53.672 1.00 17.16 ? 88  LEU   A N   1 
ATOM   717  C CA  . LEU   A 1 86  ? 12.948  -20.167 -54.136 1.00 16.43 ? 88  LEU   A CA  1 
ATOM   718  C C   . LEU   A 1 86  ? 13.603  -19.108 -55.012 1.00 16.43 ? 88  LEU   A C   1 
ATOM   719  O O   . LEU   A 1 86  ? 12.893  -18.250 -55.545 1.00 18.55 ? 88  LEU   A O   1 
ATOM   720  C CB  . LEU   A 1 86  ? 12.276  -19.472 -52.942 1.00 16.97 ? 88  LEU   A CB  1 
ATOM   721  C CG  . LEU   A 1 86  ? 11.454  -20.375 -52.034 1.00 16.88 ? 88  LEU   A CG  1 
ATOM   722  C CD1 . LEU   A 1 86  ? 10.891  -19.572 -50.860 1.00 17.46 ? 88  LEU   A CD1 1 
ATOM   723  C CD2 . LEU   A 1 86  ? 10.335  -21.028 -52.835 1.00 17.70 ? 88  LEU   A CD2 1 
ATOM   724  N N   . ARG   A 1 87  ? 14.926  -19.144 -55.171 1.00 15.78 ? 89  ARG   A N   1 
ATOM   725  C CA  . ARG   A 1 87  ? 15.620  -18.084 -55.884 1.00 18.50 ? 89  ARG   A CA  1 
ATOM   726  C C   . ARG   A 1 87  ? 15.089  -17.939 -57.303 1.00 18.43 ? 89  ARG   A C   1 
ATOM   727  O O   . ARG   A 1 87  ? 14.880  -18.927 -58.015 1.00 19.38 ? 89  ARG   A O   1 
ATOM   728  C CB  . ARG   A 1 87  ? 17.118  -18.372 -55.902 1.00 20.00 ? 89  ARG   A CB  1 
ATOM   729  C CG  . ARG   A 1 87  ? 17.964  -17.223 -56.421 1.00 20.04 ? 89  ARG   A CG  1 
ATOM   730  C CD  . ARG   A 1 87  ? 19.389  -17.347 -55.888 1.00 22.88 ? 89  ARG   A CD  1 
ATOM   731  N NE  . ARG   A 1 87  ? 19.920  -18.697 -56.058 1.00 24.21 ? 89  ARG   A NE  1 
ATOM   732  C CZ  . ARG   A 1 87  ? 20.914  -19.205 -55.331 1.00 27.76 ? 89  ARG   A CZ  1 
ATOM   733  N NH1 . ARG   A 1 87  ? 21.488  -18.476 -54.374 1.00 24.86 ? 89  ARG   A NH1 1 
ATOM   734  N NH2 . ARG   A 1 87  ? 21.340  -20.442 -55.555 1.00 29.61 ? 89  ARG   A NH2 1 
ATOM   735  N N   . GLY   A 1 88  ? 14.868  -16.689 -57.710 1.00 18.64 ? 90  GLY   A N   1 
ATOM   736  C CA  . GLY   A 1 88  ? 14.312  -16.383 -59.012 1.00 18.71 ? 90  GLY   A CA  1 
ATOM   737  C C   . GLY   A 1 88  ? 12.800  -16.331 -59.065 1.00 24.09 ? 90  GLY   A C   1 
ATOM   738  O O   . GLY   A 1 88  ? 12.245  -15.854 -60.068 1.00 22.27 ? 90  GLY   A O   1 
ATOM   739  N N   . GLY   A 1 89  ? 12.119  -16.801 -58.023 1.00 19.21 ? 91  GLY   A N   1 
ATOM   740  C CA  . GLY   A 1 89  ? 10.678  -16.764 -57.975 1.00 19.60 ? 91  GLY   A CA  1 
ATOM   741  C C   . GLY   A 1 89  ? 10.145  -15.350 -57.847 1.00 19.35 ? 91  GLY   A C   1 
ATOM   742  O O   . GLY   A 1 89  ? 10.848  -14.426 -57.432 1.00 18.31 ? 91  GLY   A O   1 
ATOM   743  N N   . PRO   A 1 90  ? 8.876   -15.160 -58.196 1.00 17.44 ? 92  PRO   A N   1 
ATOM   744  C CA  . PRO   A 1 90  ? 8.295   -13.809 -58.205 1.00 14.58 ? 92  PRO   A CA  1 
ATOM   745  C C   . PRO   A 1 90  ? 8.352   -13.161 -56.834 1.00 15.51 ? 92  PRO   A C   1 
ATOM   746  O O   . PRO   A 1 90  ? 7.791   -13.679 -55.867 1.00 16.59 ? 92  PRO   A O   1 
ATOM   747  C CB  . PRO   A 1 90  ? 6.844   -14.052 -58.635 1.00 18.97 ? 92  PRO   A CB  1 
ATOM   748  C CG  . PRO   A 1 90  ? 6.818   -15.407 -59.215 1.00 28.01 ? 92  PRO   A CG  1 
ATOM   749  C CD  . PRO   A 1 90  ? 7.894   -16.193 -58.552 1.00 21.67 ? 92  PRO   A CD  1 
ATOM   750  N N   . ASN   A 1 91  ? 9.020   -12.007 -56.764 1.00 14.41 ? 93  ASN   A N   1 
ATOM   751  C CA  . ASN   A 1 91  ? 9.067   -11.156 -55.577 1.00 13.68 ? 93  ASN   A CA  1 
ATOM   752  C C   . ASN   A 1 91  ? 9.716   -11.842 -54.371 1.00 16.47 ? 93  ASN   A C   1 
ATOM   753  O O   . ASN   A 1 91  ? 9.529   -11.403 -53.239 1.00 17.52 ? 93  ASN   A O   1 
ATOM   754  C CB  . ASN   A 1 91  ? 7.658   -10.639 -55.251 1.00 16.29 ? 93  ASN   A CB  1 
ATOM   755  C CG  . ASN   A 1 91  ? 7.121   -9.759  -56.360 1.00 21.50 ? 93  ASN   A CG  1 
ATOM   756  O OD1 . ASN   A 1 91  ? 7.896   -9.174  -57.123 1.00 19.02 ? 93  ASN   A OD1 1 
ATOM   757  N ND2 . ASN   A 1 91  ? 5.810   -9.673  -56.475 1.00 18.18 ? 93  ASN   A ND2 1 
ATOM   758  N N   . ILE   A 1 92  ? 10.497  -12.895 -54.590 1.00 17.64 ? 94  ILE   A N   1 
ATOM   759  C CA  . ILE   A 1 92  ? 11.285  -13.526 -53.531 1.00 14.59 ? 94  ILE   A CA  1 
ATOM   760  C C   . ILE   A 1 92  ? 12.639  -12.832 -53.479 1.00 15.76 ? 94  ILE   A C   1 
ATOM   761  O O   . ILE   A 1 92  ? 13.285  -12.672 -54.518 1.00 14.79 ? 94  ILE   A O   1 
ATOM   762  C CB  . ILE   A 1 92  ? 11.479  -15.028 -53.808 1.00 16.66 ? 94  ILE   A CB  1 
ATOM   763  C CG1 . ILE   A 1 92  ? 10.149  -15.739 -54.099 1.00 19.42 ? 94  ILE   A CG1 1 
ATOM   764  C CG2 . ILE   A 1 92  ? 12.271  -15.684 -52.664 1.00 19.66 ? 94  ILE   A CG2 1 
ATOM   765  C CD1 . ILE   A 1 92  ? 9.195   -15.753 -52.927 1.00 15.71 ? 94  ILE   A CD1 1 
ATOM   766  N N   . ILE   A 1 93  ? 13.077  -12.424 -52.282 1.00 13.96 ? 95  ILE   A N   1 
ATOM   767  C CA  . ILE   A 1 93  ? 14.417  -11.846 -52.155 1.00 11.97 ? 95  ILE   A CA  1 
ATOM   768  C C   . ILE   A 1 93  ? 15.460  -12.833 -52.670 1.00 12.28 ? 95  ILE   A C   1 
ATOM   769  O O   . ILE   A 1 93  ? 15.386  -14.040 -52.404 1.00 14.88 ? 95  ILE   A O   1 
ATOM   770  C CB  . ILE   A 1 93  ? 14.695  -11.444 -50.693 1.00 12.70 ? 95  ILE   A CB  1 
ATOM   771  C CG1 . ILE   A 1 93  ? 15.889  -10.488 -50.612 1.00 11.86 ? 95  ILE   A CG1 1 
ATOM   772  C CG2 . ILE   A 1 93  ? 14.971  -12.654 -49.803 1.00 13.97 ? 95  ILE   A CG2 1 
ATOM   773  C CD1 . ILE   A 1 93  ? 15.574  -9.099  -51.124 1.00 16.20 ? 95  ILE   A CD1 1 
ATOM   774  N N   . THR   A 1 94  ? 16.442  -12.314 -53.414 1.00 14.26 ? 96  THR   A N   1 
ATOM   775  C CA  . THR   A 1 94  ? 17.494  -13.125 -54.024 1.00 14.24 ? 96  THR   A CA  1 
ATOM   776  C C   . THR   A 1 94  ? 18.674  -13.270 -53.072 1.00 15.01 ? 96  THR   A C   1 
ATOM   777  O O   . THR   A 1 94  ? 19.292  -12.275 -52.681 1.00 15.69 ? 96  THR   A O   1 
ATOM   778  C CB  . THR   A 1 94  ? 17.963  -12.491 -55.331 1.00 15.43 ? 96  THR   A CB  1 
ATOM   779  O OG1 . THR   A 1 94  ? 16.880  -12.506 -56.268 1.00 21.21 ? 96  THR   A OG1 1 
ATOM   780  C CG2 . THR   A 1 94  ? 19.145  -13.269 -55.909 1.00 19.68 ? 96  THR   A CG2 1 
ATOM   781  N N   . LEU   A 1 95  ? 18.975  -14.508 -52.699 1.00 15.31 ? 97  LEU   A N   1 
ATOM   782  C CA  . LEU   A 1 95  ? 20.240  -14.833 -52.043 1.00 13.84 ? 97  LEU   A CA  1 
ATOM   783  C C   . LEU   A 1 95  ? 21.338  -14.803 -53.093 1.00 15.90 ? 97  LEU   A C   1 
ATOM   784  O O   . LEU   A 1 95  ? 21.361  -15.645 -53.996 1.00 21.03 ? 97  LEU   A O   1 
ATOM   785  C CB  . LEU   A 1 95  ? 20.151  -16.198 -51.380 1.00 16.69 ? 97  LEU   A CB  1 
ATOM   786  C CG  . LEU   A 1 95  ? 21.383  -16.659 -50.594 1.00 16.36 ? 97  LEU   A CG  1 
ATOM   787  C CD1 . LEU   A 1 95  ? 21.668  -15.704 -49.444 1.00 16.10 ? 97  LEU   A CD1 1 
ATOM   788  C CD2 . LEU   A 1 95  ? 21.200  -18.088 -50.078 1.00 18.57 ? 97  LEU   A CD2 1 
ATOM   789  N N   . ALA   A 1 96  ? 22.246  -13.843 -52.973 1.00 14.12 ? 98  ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 96  ? 23.322  -13.692 -53.945 1.00 18.35 ? 98  ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 96  ? 24.544  -14.527 -53.606 1.00 20.90 ? 98  ALA   A C   1 
ATOM   792  O O   . ALA   A 1 96  ? 25.264  -14.953 -54.518 1.00 20.53 ? 98  ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 96  ? 23.731  -12.223 -54.048 1.00 21.62 ? 98  ALA   A CB  1 
ATOM   794  N N   . ASP   A 1 97  ? 24.791  -14.774 -52.325 1.00 16.89 ? 99  ASP   A N   1 
ATOM   795  C CA  . ASP   A 1 97  ? 26.021  -15.424 -51.896 1.00 18.91 ? 99  ASP   A CA  1 
ATOM   796  C C   . ASP   A 1 97  ? 25.872  -15.828 -50.437 1.00 17.01 ? 99  ASP   A C   1 
ATOM   797  O O   . ASP   A 1 97  ? 24.976  -15.363 -49.725 1.00 16.91 ? 99  ASP   A O   1 
ATOM   798  C CB  . ASP   A 1 97  ? 27.229  -14.491 -52.080 1.00 19.83 ? 99  ASP   A CB  1 
ATOM   799  C CG  . ASP   A 1 97  ? 28.507  -15.231 -52.424 1.00 22.70 ? 99  ASP   A CG  1 
ATOM   800  O OD1 . ASP   A 1 97  ? 28.550  -16.470 -52.330 1.00 20.80 ? 99  ASP   A OD1 1 
ATOM   801  O OD2 . ASP   A 1 97  ? 29.477  -14.551 -52.807 1.00 25.99 ? 99  ASP   A OD2 1 
ATOM   802  N N   . ILE   A 1 98  ? 26.767  -16.716 -50.008 1.00 17.06 ? 100 ILE   A N   1 
ATOM   803  C CA  . ILE   A 1 98  ? 26.886  -17.139 -48.620 1.00 17.85 ? 100 ILE   A CA  1 
ATOM   804  C C   . ILE   A 1 98  ? 28.370  -17.168 -48.321 1.00 16.16 ? 100 ILE   A C   1 
ATOM   805  O O   . ILE   A 1 98  ? 29.129  -17.807 -49.054 1.00 18.51 ? 100 ILE   A O   1 
ATOM   806  C CB  . ILE   A 1 98  ? 26.294  -18.540 -48.373 1.00 20.93 ? 100 ILE   A CB  1 
ATOM   807  C CG1 . ILE   A 1 98  ? 24.896  -18.684 -48.976 1.00 23.61 ? 100 ILE   A CG1 1 
ATOM   808  C CG2 . ILE   A 1 98  ? 26.319  -18.865 -46.885 1.00 25.03 ? 100 ILE   A CG2 1 
ATOM   809  C CD1 . ILE   A 1 98  ? 24.544  -20.139 -49.262 1.00 23.74 ? 100 ILE   A CD1 1 
ATOM   810  N N   . VAL   A 1 99  ? 28.794  -16.480 -47.263 1.00 16.55 ? 101 VAL   A N   1 
ATOM   811  C CA  . VAL   A 1 99  ? 30.210  -16.432 -46.926 1.00 14.66 ? 101 VAL   A CA  1 
ATOM   812  C C   . VAL   A 1 99  ? 30.377  -16.685 -45.433 1.00 18.18 ? 101 VAL   A C   1 
ATOM   813  O O   . VAL   A 1 99  ? 29.438  -16.558 -44.648 1.00 19.23 ? 101 VAL   A O   1 
ATOM   814  C CB  . VAL   A 1 99  ? 30.888  -15.096 -47.340 1.00 16.62 ? 101 VAL   A CB  1 
ATOM   815  C CG1 . VAL   A 1 99  ? 30.721  -14.833 -48.845 1.00 19.85 ? 101 VAL   A CG1 1 
ATOM   816  C CG2 . VAL   A 1 99  ? 30.379  -13.922 -46.502 1.00 18.65 ? 101 VAL   A CG2 1 
ATOM   817  N N   . LYS   A 1 100 ? 31.599  -17.060 -45.047 1.00 17.42 ? 102 LYS   A N   1 
ATOM   818  C CA  . LYS   A 1 100 ? 31.941  -17.288 -43.646 1.00 18.56 ? 102 LYS   A CA  1 
ATOM   819  C C   . LYS   A 1 100 ? 32.476  -15.990 -43.058 1.00 17.05 ? 102 LYS   A C   1 
ATOM   820  O O   . LYS   A 1 100 ? 33.515  -15.489 -43.503 1.00 20.72 ? 102 LYS   A O   1 
ATOM   821  C CB  . LYS   A 1 100 ? 32.987  -18.395 -43.495 1.00 21.18 ? 102 LYS   A CB  1 
ATOM   822  C CG  . LYS   A 1 100 ? 32.604  -19.753 -44.060 1.00 28.47 ? 102 LYS   A CG  1 
ATOM   823  C CD  . LYS   A 1 100 ? 33.760  -20.739 -43.874 1.00 39.05 ? 102 LYS   A CD  1 
ATOM   824  C CE  . LYS   A 1 100 ? 33.986  -21.585 -45.117 1.00 48.33 ? 102 LYS   A CE  1 
ATOM   825  N NZ  . LYS   A 1 100 ? 35.349  -22.205 -45.134 1.00 56.49 ? 102 LYS   A NZ  1 
ATOM   826  N N   . ASP   A 1 101 ? 31.776  -15.441 -42.080 1.00 17.35 ? 103 ASP   A N   1 
ATOM   827  C CA  . ASP   A 1 101 ? 32.282  -14.223 -41.481 1.00 17.58 ? 103 ASP   A CA  1 
ATOM   828  C C   . ASP   A 1 101 ? 33.399  -14.572 -40.505 1.00 18.83 ? 103 ASP   A C   1 
ATOM   829  O O   . ASP   A 1 101 ? 33.210  -15.424 -39.632 1.00 20.94 ? 103 ASP   A O   1 
ATOM   830  C CB  . ASP   A 1 101 ? 31.190  -13.431 -40.764 1.00 16.44 ? 103 ASP   A CB  1 
ATOM   831  C CG  . ASP   A 1 101 ? 31.701  -12.094 -40.278 1.00 24.48 ? 103 ASP   A CG  1 
ATOM   832  O OD1 . ASP   A 1 101 ? 31.710  -11.135 -41.074 1.00 22.31 ? 103 ASP   A OD1 1 
ATOM   833  O OD2 . ASP   A 1 101 ? 32.161  -12.009 -39.120 1.00 23.88 ? 103 ASP   A OD2 1 
ATOM   834  N N   . PRO   A 1 102 ? 34.565  -13.933 -40.621 1.00 21.32 ? 104 PRO   A N   1 
ATOM   835  C CA  . PRO   A 1 102 ? 35.703  -14.309 -39.767 1.00 24.65 ? 104 PRO   A CA  1 
ATOM   836  C C   . PRO   A 1 102 ? 35.594  -13.818 -38.335 1.00 21.62 ? 104 PRO   A C   1 
ATOM   837  O O   . PRO   A 1 102 ? 36.289  -14.358 -37.460 1.00 22.35 ? 104 PRO   A O   1 
ATOM   838  C CB  . PRO   A 1 102 ? 36.899  -13.654 -40.477 1.00 23.39 ? 104 PRO   A CB  1 
ATOM   839  C CG  . PRO   A 1 102 ? 36.303  -12.473 -41.191 1.00 25.13 ? 104 PRO   A CG  1 
ATOM   840  C CD  . PRO   A 1 102 ? 34.898  -12.889 -41.602 1.00 17.97 ? 104 PRO   A CD  1 
ATOM   841  N N   . VAL   A 1 103 ? 34.779  -12.800 -38.076 1.00 20.13 ? 105 VAL   A N   1 
ATOM   842  C CA  . VAL   A 1 103 ? 34.624  -12.257 -36.727 1.00 20.99 ? 105 VAL   A CA  1 
ATOM   843  C C   . VAL   A 1 103 ? 33.565  -13.018 -35.957 1.00 18.60 ? 105 VAL   A C   1 
ATOM   844  O O   . VAL   A 1 103 ? 33.788  -13.440 -34.820 1.00 20.95 ? 105 VAL   A O   1 
ATOM   845  C CB  . VAL   A 1 103 ? 34.278  -10.753 -36.785 1.00 22.83 ? 105 VAL   A CB  1 
ATOM   846  C CG1 . VAL   A 1 103 ? 34.033  -10.203 -35.374 1.00 21.79 ? 105 VAL   A CG1 1 
ATOM   847  C CG2 . VAL   A 1 103 ? 35.377  -9.974  -37.484 1.00 22.38 ? 105 VAL   A CG2 1 
ATOM   848  N N   . SER   A 1 104 ? 32.400  -13.200 -36.571 1.00 20.52 ? 106 SER   A N   1 
ATOM   849  C CA  . SER   A 1 104 ? 31.311  -13.882 -35.896 1.00 19.21 ? 106 SER   A CA  1 
ATOM   850  C C   . SER   A 1 104 ? 31.528  -15.379 -35.833 1.00 23.57 ? 106 SER   A C   1 
ATOM   851  O O   . SER   A 1 104 ? 30.935  -16.038 -34.970 1.00 27.36 ? 106 SER   A O   1 
ATOM   852  C CB  . SER   A 1 104 ? 29.990  -13.600 -36.608 1.00 20.14 ? 106 SER   A CB  1 
ATOM   853  O OG  . SER   A 1 104 ? 29.955  -14.259 -37.861 1.00 19.66 ? 106 SER   A OG  1 
ATOM   854  N N   . ARG   A 1 105 ? 32.346  -15.920 -36.740 1.00 21.61 ? 107 ARG   A N   1 
ATOM   855  C CA  . ARG   A 1 105 ? 32.523  -17.365 -36.889 1.00 26.53 ? 107 ARG   A CA  1 
ATOM   856  C C   . ARG   A 1 105 ? 31.198  -18.036 -37.248 1.00 27.18 ? 107 ARG   A C   1 
ATOM   857  O O   . ARG   A 1 105 ? 30.906  -19.153 -36.815 1.00 30.94 ? 107 ARG   A O   1 
ATOM   858  C CB  . ARG   A 1 105 ? 33.128  -17.982 -35.625 1.00 29.35 ? 107 ARG   A CB  1 
ATOM   859  C CG  . ARG   A 1 105 ? 34.357  -17.223 -35.129 1.00 31.36 ? 107 ARG   A CG  1 
ATOM   860  C CD  . ARG   A 1 105 ? 34.811  -17.708 -33.758 1.00 32.23 ? 107 ARG   A CD  1 
ATOM   861  N NE  . ARG   A 1 105 ? 35.164  -19.122 -33.775 1.00 27.18 ? 107 ARG   A NE  1 
ATOM   862  C CZ  . ARG   A 1 105 ? 36.284  -19.601 -34.300 1.00 27.87 ? 107 ARG   A CZ  1 
ATOM   863  N NH1 . ARG   A 1 105 ? 37.162  -18.777 -34.862 1.00 31.51 ? 107 ARG   A NH1 1 
ATOM   864  N NH2 . ARG   A 1 105 ? 36.528  -20.902 -34.268 1.00 31.37 ? 107 ARG   A NH2 1 
ATOM   865  N N   . THR   A 1 106 ? 30.375  -17.332 -38.038 1.00 21.58 ? 108 THR   A N   1 
ATOM   866  C CA  . THR   A 1 106 ? 29.072  -17.833 -38.470 1.00 23.65 ? 108 THR   A CA  1 
ATOM   867  C C   . THR   A 1 106 ? 28.852  -17.505 -39.945 1.00 24.93 ? 108 THR   A C   1 
ATOM   868  O O   . THR   A 1 106 ? 29.579  -16.677 -40.510 1.00 19.09 ? 108 THR   A O   1 
ATOM   869  C CB  . THR   A 1 106 ? 27.938  -17.228 -37.632 1.00 21.62 ? 108 THR   A CB  1 
ATOM   870  O OG1 . THR   A 1 106 ? 27.862  -15.816 -37.857 1.00 21.15 ? 108 THR   A OG1 1 
ATOM   871  C CG2 . THR   A 1 106 ? 28.115  -17.514 -36.137 1.00 25.85 ? 108 THR   A CG2 1 
ATOM   872  N N   . PRO   A 1 107 ? 27.853  -18.100 -40.597 1.00 21.70 ? 109 PRO   A N   1 
ATOM   873  C CA  . PRO   A 1 107 ? 27.573  -17.737 -41.987 1.00 18.01 ? 109 PRO   A CA  1 
ATOM   874  C C   . PRO   A 1 107 ? 26.984  -16.341 -42.093 1.00 18.57 ? 109 PRO   A C   1 
ATOM   875  O O   . PRO   A 1 107 ? 26.239  -15.881 -41.222 1.00 20.44 ? 109 PRO   A O   1 
ATOM   876  C CB  . PRO   A 1 107 ? 26.555  -18.797 -42.434 1.00 20.76 ? 109 PRO   A CB  1 
ATOM   877  C CG  . PRO   A 1 107 ? 26.724  -19.918 -41.462 1.00 20.90 ? 109 PRO   A CG  1 
ATOM   878  C CD  . PRO   A 1 107 ? 27.018  -19.234 -40.164 1.00 22.36 ? 109 PRO   A CD  1 
ATOM   879  N N   . ALA   A 1 108 ? 27.309  -15.677 -43.197 1.00 16.08 ? 110 ALA   A N   1 
ATOM   880  C CA  . ALA   A 1 108 ? 26.750  -14.383 -43.564 1.00 16.40 ? 110 ALA   A CA  1 
ATOM   881  C C   . ALA   A 1 108 ? 26.056  -14.542 -44.909 1.00 17.94 ? 110 ALA   A C   1 
ATOM   882  O O   . ALA   A 1 108 ? 26.694  -14.897 -45.904 1.00 19.34 ? 110 ALA   A O   1 
ATOM   883  C CB  . ALA   A 1 108 ? 27.836  -13.305 -43.624 1.00 19.24 ? 110 ALA   A CB  1 
ATOM   884  N N   . LEU   A 1 109 ? 24.752  -14.298 -44.935 1.00 14.60 ? 111 LEU   A N   1 
ATOM   885  C CA  . LEU   A 1 109 ? 23.969  -14.416 -46.156 1.00 13.69 ? 111 LEU   A CA  1 
ATOM   886  C C   . LEU   A 1 109 ? 23.987  -13.080 -46.880 1.00 16.42 ? 111 LEU   A C   1 
ATOM   887  O O   . LEU   A 1 109 ? 23.751  -12.036 -46.262 1.00 17.59 ? 111 LEU   A O   1 
ATOM   888  C CB  . LEU   A 1 109 ? 22.530  -14.802 -45.829 1.00 15.13 ? 111 LEU   A CB  1 
ATOM   889  C CG  . LEU   A 1 109 ? 22.355  -16.098 -45.047 1.00 15.03 ? 111 LEU   A CG  1 
ATOM   890  C CD1 . LEU   A 1 109 ? 20.862  -16.389 -44.831 1.00 17.07 ? 111 LEU   A CD1 1 
ATOM   891  C CD2 . LEU   A 1 109 ? 23.020  -17.271 -45.724 1.00 26.64 ? 111 LEU   A CD2 1 
ATOM   892  N N   . VAL   A 1 110 ? 24.263  -13.106 -48.180 1.00 14.16 ? 112 VAL   A N   1 
ATOM   893  C CA  . VAL   A 1 110 ? 24.346  -11.889 -48.978 1.00 14.50 ? 112 VAL   A CA  1 
ATOM   894  C C   . VAL   A 1 110 ? 23.126  -11.839 -49.882 1.00 14.46 ? 112 VAL   A C   1 
ATOM   895  O O   . VAL   A 1 110 ? 22.910  -12.755 -50.683 1.00 16.78 ? 112 VAL   A O   1 
ATOM   896  C CB  . VAL   A 1 110 ? 25.643  -11.834 -49.798 1.00 15.58 ? 112 VAL   A CB  1 
ATOM   897  C CG1 . VAL   A 1 110 ? 25.728  -10.528 -50.597 1.00 19.64 ? 112 VAL   A CG1 1 
ATOM   898  C CG2 . VAL   A 1 110 ? 26.847  -11.991 -48.878 1.00 18.79 ? 112 VAL   A CG2 1 
ATOM   899  N N   . PHE   A 1 111 ? 22.345  -10.773 -49.755 1.00 13.55 ? 113 PHE   A N   1 
ATOM   900  C CA  . PHE   A 1 111 ? 21.098  -10.590 -50.488 1.00 13.36 ? 113 PHE   A CA  1 
ATOM   901  C C   . PHE   A 1 111 ? 21.207  -9.420  -51.453 1.00 14.98 ? 113 PHE   A C   1 
ATOM   902  O O   . PHE   A 1 111 ? 21.953  -8.460  -51.222 1.00 16.85 ? 113 PHE   A O   1 
ATOM   903  C CB  . PHE   A 1 111 ? 19.923  -10.308 -49.547 1.00 14.56 ? 113 PHE   A CB  1 
ATOM   904  C CG  . PHE   A 1 111 ? 19.626  -11.410 -48.588 1.00 13.89 ? 113 PHE   A CG  1 
ATOM   905  C CD1 . PHE   A 1 111 ? 18.836  -12.480 -48.966 1.00 13.87 ? 113 PHE   A CD1 1 
ATOM   906  C CD2 . PHE   A 1 111 ? 20.104  -11.354 -47.280 1.00 18.27 ? 113 PHE   A CD2 1 
ATOM   907  C CE1 . PHE   A 1 111 ? 18.531  -13.487 -48.068 1.00 16.75 ? 113 PHE   A CE1 1 
ATOM   908  C CE2 . PHE   A 1 111 ? 19.813  -12.368 -46.382 1.00 18.11 ? 113 PHE   A CE2 1 
ATOM   909  C CZ  . PHE   A 1 111 ? 19.023  -13.435 -46.773 1.00 15.55 ? 113 PHE   A CZ  1 
ATOM   910  N N   . GLU   A 1 112 ? 20.417  -9.486  -52.523 1.00 15.39 ? 114 GLU   A N   1 
ATOM   911  C CA  . GLU   A 1 112 ? 20.193  -8.289  -53.314 1.00 16.90 ? 114 GLU   A CA  1 
ATOM   912  C C   . GLU   A 1 112 ? 19.686  -7.174  -52.410 1.00 19.57 ? 114 GLU   A C   1 
ATOM   913  O O   . GLU   A 1 112 ? 19.014  -7.418  -51.400 1.00 20.30 ? 114 GLU   A O   1 
ATOM   914  C CB  . GLU   A 1 112 ? 19.172  -8.563  -54.420 1.00 22.02 ? 114 GLU   A CB  1 
ATOM   915  C CG  . GLU   A 1 112 ? 17.795  -8.826  -53.850 1.00 21.96 ? 114 GLU   A CG  1 
ATOM   916  C CD  . GLU   A 1 112 ? 16.712  -8.911  -54.898 1.00 30.97 ? 114 GLU   A CD  1 
ATOM   917  O OE1 . GLU   A 1 112 ? 16.650  -8.019  -55.769 1.00 43.39 ? 114 GLU   A OE1 1 
ATOM   918  O OE2 . GLU   A 1 112 ? 15.925  -9.874  -54.847 1.00 21.69 ? 114 GLU   A OE2 1 
ATOM   919  N N   . HIS   A 1 113 ? 19.999  -5.938  -52.779 1.00 20.98 ? 115 HIS   A N   1 
ATOM   920  C CA  . HIS   A 1 113 ? 19.598  -4.775  -52.000 1.00 19.85 ? 115 HIS   A CA  1 
ATOM   921  C C   . HIS   A 1 113 ? 18.307  -4.190  -52.558 1.00 21.12 ? 115 HIS   A C   1 
ATOM   922  O O   . HIS   A 1 113 ? 18.153  -4.057  -53.771 1.00 22.65 ? 115 HIS   A O   1 
ATOM   923  C CB  . HIS   A 1 113 ? 20.712  -3.720  -52.015 1.00 21.27 ? 115 HIS   A CB  1 
ATOM   924  C CG  . HIS   A 1 113 ? 20.336  -2.432  -51.352 1.00 24.41 ? 115 HIS   A CG  1 
ATOM   925  N ND1 . HIS   A 1 113 ? 19.907  -1.329  -52.060 1.00 24.90 ? 115 HIS   A ND1 1 
ATOM   926  C CD2 . HIS   A 1 113 ? 20.310  -2.076  -50.046 1.00 28.38 ? 115 HIS   A CD2 1 
ATOM   927  C CE1 . HIS   A 1 113 ? 19.649  -0.344  -51.218 1.00 24.42 ? 115 HIS   A CE1 1 
ATOM   928  N NE2 . HIS   A 1 113 ? 19.886  -0.771  -49.990 1.00 28.13 ? 115 HIS   A NE2 1 
ATOM   929  N N   . VAL   A 1 114 ? 17.371  -3.858  -51.670 1.00 19.67 ? 116 VAL   A N   1 
ATOM   930  C CA  . VAL   A 1 114 ? 16.163  -3.127  -52.041 1.00 21.16 ? 116 VAL   A CA  1 
ATOM   931  C C   . VAL   A 1 114 ? 16.250  -1.735  -51.436 1.00 20.95 ? 116 VAL   A C   1 
ATOM   932  O O   . VAL   A 1 114 ? 16.476  -1.587  -50.230 1.00 22.37 ? 116 VAL   A O   1 
ATOM   933  C CB  . VAL   A 1 114 ? 14.879  -3.839  -51.575 1.00 17.23 ? 116 VAL   A CB  1 
ATOM   934  C CG1 . VAL   A 1 114 ? 13.640  -3.010  -51.982 1.00 20.70 ? 116 VAL   A CG1 1 
ATOM   935  C CG2 . VAL   A 1 114 ? 14.790  -5.234  -52.170 1.00 20.48 ? 116 VAL   A CG2 1 
ATOM   936  N N   . ASN   A 1 115 ? 16.057  -0.715  -52.269 1.00 23.91 ? 117 ASN   A N   1 
ATOM   937  C CA  . ASN   A 1 115 ? 16.017  0.668   -51.801 1.00 27.47 ? 117 ASN   A CA  1 
ATOM   938  C C   . ASN   A 1 115 ? 14.609  0.943   -51.281 1.00 23.25 ? 117 ASN   A C   1 
ATOM   939  O O   . ASN   A 1 115 ? 13.750  1.505   -51.965 1.00 30.02 ? 117 ASN   A O   1 
ATOM   940  C CB  . ASN   A 1 115 ? 16.409  1.621   -52.921 1.00 32.45 ? 117 ASN   A CB  1 
ATOM   941  C CG  . ASN   A 1 115 ? 16.468  3.054   -52.462 1.00 42.36 ? 117 ASN   A CG  1 
ATOM   942  O OD1 . ASN   A 1 115 ? 16.653  3.331   -51.279 1.00 53.70 ? 117 ASN   A OD1 1 
ATOM   943  N ND2 . ASN   A 1 115 ? 16.303  3.979   -53.396 1.00 44.80 ? 117 ASN   A ND2 1 
ATOM   944  N N   . ASN   A 1 116 ? 14.365  0.524   -50.045 1.00 26.53 ? 118 ASN   A N   1 
ATOM   945  C CA  . ASN   A 1 116 ? 13.011  0.484   -49.513 1.00 33.54 ? 118 ASN   A CA  1 
ATOM   946  C C   . ASN   A 1 116 ? 12.688  1.716   -48.672 1.00 35.38 ? 118 ASN   A C   1 
ATOM   947  O O   . ASN   A 1 116 ? 13.575  2.432   -48.206 1.00 29.55 ? 118 ASN   A O   1 
ATOM   948  C CB  . ASN   A 1 116 ? 12.808  -0.776  -48.668 1.00 32.81 ? 118 ASN   A CB  1 
ATOM   949  C CG  . ASN   A 1 116 ? 13.292  -0.604  -47.251 1.00 36.61 ? 118 ASN   A CG  1 
ATOM   950  O OD1 . ASN   A 1 116 ? 14.468  -0.322  -47.015 1.00 40.80 ? 118 ASN   A OD1 1 
ATOM   951  N ND2 . ASN   A 1 116 ? 12.380  -0.752  -46.291 1.00 39.91 ? 118 ASN   A ND2 1 
ATOM   952  N N   . THR   A 1 117 ? 11.390  1.948   -48.474 1.00 38.30 ? 119 THR   A N   1 
ATOM   953  C CA  . THR   A 1 117 ? 10.897  2.971   -47.559 1.00 41.56 ? 119 THR   A CA  1 
ATOM   954  C C   . THR   A 1 117 ? 10.205  2.316   -46.369 1.00 44.55 ? 119 THR   A C   1 
ATOM   955  O O   . THR   A 1 117 ? 9.462   1.342   -46.529 1.00 44.55 ? 119 THR   A O   1 
ATOM   956  C CB  . THR   A 1 117 ? 9.935   3.939   -48.259 1.00 56.51 ? 119 THR   A CB  1 
ATOM   957  O OG1 . THR   A 1 117 ? 9.553   3.412   -49.536 1.00 53.15 ? 119 THR   A OG1 1 
ATOM   958  C CG2 . THR   A 1 117 ? 10.600  5.296   -48.454 1.00 60.76 ? 119 THR   A CG2 1 
ATOM   959  N N   . ASP   A 1 118 ? 10.447  2.868   -45.178 1.00 49.48 ? 120 ASP   A N   1 
ATOM   960  C CA  . ASP   A 1 118 ? 9.986   2.255   -43.936 1.00 48.91 ? 120 ASP   A CA  1 
ATOM   961  C C   . ASP   A 1 118 ? 8.469   2.127   -43.908 1.00 35.34 ? 120 ASP   A C   1 
ATOM   962  O O   . ASP   A 1 118 ? 7.748   3.039   -44.318 1.00 52.02 ? 120 ASP   A O   1 
ATOM   963  C CB  . ASP   A 1 118 ? 10.465  3.082   -42.744 1.00 62.29 ? 120 ASP   A CB  1 
ATOM   964  C CG  . ASP   A 1 118 ? 11.393  2.309   -41.841 1.00 72.49 ? 120 ASP   A CG  1 
ATOM   965  O OD1 . ASP   A 1 118 ? 11.150  2.282   -40.616 1.00 78.59 ? 120 ASP   A OD1 1 
ATOM   966  O OD2 . ASP   A 1 118 ? 12.354  1.707   -42.363 1.00 77.50 ? 120 ASP   A OD2 1 
ATOM   967  N N   . PHE   A 1 119 ? 7.982   0.980   -43.418 1.00 35.48 ? 121 PHE   A N   1 
ATOM   968  C CA  . PHE   A 1 119 ? 6.545   0.732   -43.489 1.00 46.69 ? 121 PHE   A CA  1 
ATOM   969  C C   . PHE   A 1 119 ? 5.776   1.686   -42.587 1.00 54.90 ? 121 PHE   A C   1 
ATOM   970  O O   . PHE   A 1 119 ? 4.632   2.038   -42.896 1.00 55.37 ? 121 PHE   A O   1 
ATOM   971  C CB  . PHE   A 1 119 ? 6.223   -0.738  -43.162 1.00 48.96 ? 121 PHE   A CB  1 
ATOM   972  C CG  . PHE   A 1 119 ? 6.021   -1.033  -41.691 1.00 49.06 ? 121 PHE   A CG  1 
ATOM   973  C CD1 . PHE   A 1 119 ? 7.062   -1.542  -40.923 1.00 53.65 ? 121 PHE   A CD1 1 
ATOM   974  C CD2 . PHE   A 1 119 ? 4.781   -0.850  -41.090 1.00 46.61 ? 121 PHE   A CD2 1 
ATOM   975  C CE1 . PHE   A 1 119 ? 6.880   -1.830  -39.580 1.00 49.47 ? 121 PHE   A CE1 1 
ATOM   976  C CE2 . PHE   A 1 119 ? 4.595   -1.131  -39.748 1.00 45.77 ? 121 PHE   A CE2 1 
ATOM   977  C CZ  . PHE   A 1 119 ? 5.644   -1.625  -38.992 1.00 45.25 ? 121 PHE   A CZ  1 
ATOM   978  N N   . LYS   A 1 120 ? 6.386   2.128   -41.484 1.00 55.87 ? 122 LYS   A N   1 
ATOM   979  C CA  . LYS   A 1 120 ? 5.724   3.103   -40.624 1.00 60.58 ? 122 LYS   A CA  1 
ATOM   980  C C   . LYS   A 1 120 ? 5.551   4.440   -41.330 1.00 64.87 ? 122 LYS   A C   1 
ATOM   981  O O   . LYS   A 1 120 ? 4.663   5.222   -40.970 1.00 76.13 ? 122 LYS   A O   1 
ATOM   982  C CB  . LYS   A 1 120 ? 6.506   3.273   -39.323 1.00 56.29 ? 122 LYS   A CB  1 
ATOM   983  C CG  . LYS   A 1 120 ? 6.446   2.060   -38.416 1.00 55.06 ? 122 LYS   A CG  1 
ATOM   984  C CD  . LYS   A 1 120 ? 7.684   1.967   -37.548 1.00 57.89 ? 122 LYS   A CD  1 
ATOM   985  C CE  . LYS   A 1 120 ? 8.933   1.883   -38.409 1.00 59.13 ? 122 LYS   A CE  1 
ATOM   986  N NZ  . LYS   A 1 120 ? 9.936   0.940   -37.847 1.00 57.22 ? 122 LYS   A NZ  1 
ATOM   987  N N   . GLN   A 1 121 ? 6.376   4.719   -42.337 1.00 52.64 ? 123 GLN   A N   1 
ATOM   988  C CA  . GLN   A 1 121 ? 6.189   5.907   -43.159 1.00 52.87 ? 123 GLN   A CA  1 
ATOM   989  C C   . GLN   A 1 121 ? 5.464   5.604   -44.463 1.00 50.87 ? 123 GLN   A C   1 
ATOM   990  O O   . GLN   A 1 121 ? 4.696   6.441   -44.951 1.00 58.75 ? 123 GLN   A O   1 
ATOM   991  C CB  . GLN   A 1 121 ? 7.543   6.549   -43.462 1.00 60.52 ? 123 GLN   A CB  1 
ATOM   992  C CG  . GLN   A 1 121 ? 8.541   6.404   -42.331 1.00 65.08 ? 123 GLN   A CG  1 
ATOM   993  C CD  . GLN   A 1 121 ? 9.742   7.304   -42.499 1.00 71.49 ? 123 GLN   A CD  1 
ATOM   994  O OE1 . GLN   A 1 121 ? 10.265  7.466   -43.603 1.00 73.70 ? 123 GLN   A OE1 1 
ATOM   995  N NE2 . GLN   A 1 121 ? 10.181  7.911   -41.402 1.00 71.29 ? 123 GLN   A NE2 1 
ATOM   996  N N   . LEU   A 1 122 ? 5.686   4.417   -45.030 1.00 38.05 ? 124 LEU   A N   1 
ATOM   997  C CA  . LEU   A 1 122 ? 5.050   4.054   -46.290 1.00 27.18 ? 124 LEU   A CA  1 
ATOM   998  C C   . LEU   A 1 122 ? 3.547   3.858   -46.119 1.00 29.74 ? 124 LEU   A C   1 
ATOM   999  O O   . LEU   A 1 122 ? 2.757   4.208   -47.005 1.00 31.10 ? 124 LEU   A O   1 
ATOM   1000 C CB  . LEU   A 1 122 ? 5.690   2.779   -46.836 1.00 31.75 ? 124 LEU   A CB  1 
ATOM   1001 C CG  . LEU   A 1 122 ? 5.231   2.284   -48.204 1.00 44.22 ? 124 LEU   A CG  1 
ATOM   1002 C CD1 . LEU   A 1 122 ? 5.742   3.204   -49.294 1.00 43.60 ? 124 LEU   A CD1 1 
ATOM   1003 C CD2 . LEU   A 1 122 ? 5.714   0.863   -48.430 1.00 48.03 ? 124 LEU   A CD2 1 
ATOM   1004 N N   . TYR   A 1 123 ? 3.123   3.290   -44.998 1.00 21.41 ? 125 TYR   A N   1 
ATOM   1005 C CA  . TYR   A 1 123 ? 1.698   3.009   -44.881 1.00 24.45 ? 125 TYR   A CA  1 
ATOM   1006 C C   . TYR   A 1 123 ? 0.882   4.290   -44.702 1.00 27.95 ? 125 TYR   A C   1 
ATOM   1007 O O   . TYR   A 1 123 ? -0.309  4.300   -45.031 1.00 30.41 ? 125 TYR   A O   1 
ATOM   1008 C CB  . TYR   A 1 123 ? 1.451   1.989   -43.761 1.00 34.91 ? 125 TYR   A CB  1 
ATOM   1009 C CG  . TYR   A 1 123 ? 1.907   0.567   -44.103 1.00 38.72 ? 125 TYR   A CG  1 
ATOM   1010 C CD1 . TYR   A 1 123 ? 2.794   0.330   -45.152 1.00 40.32 ? 125 TYR   A CD1 1 
ATOM   1011 C CD2 . TYR   A 1 123 ? 1.438   -0.533  -43.388 1.00 37.83 ? 125 TYR   A CD2 1 
ATOM   1012 C CE1 . TYR   A 1 123 ? 3.214   -0.952  -45.470 1.00 44.25 ? 125 TYR   A CE1 1 
ATOM   1013 C CE2 . TYR   A 1 123 ? 1.852   -1.825  -43.705 1.00 43.19 ? 125 TYR   A CE2 1 
ATOM   1014 C CZ  . TYR   A 1 123 ? 2.740   -2.026  -44.749 1.00 47.00 ? 125 TYR   A CZ  1 
ATOM   1015 O OH  . TYR   A 1 123 ? 3.160   -3.299  -45.079 1.00 47.25 ? 125 TYR   A OH  1 
ATOM   1016 N N   . GLN   A 1 124 ? 1.514   5.386   -44.262 1.00 24.86 ? 126 GLN   A N   1 
ATOM   1017 C CA  . GLN   A 1 124 ? 0.852   6.689   -44.222 1.00 27.28 ? 126 GLN   A CA  1 
ATOM   1018 C C   . GLN   A 1 124 ? 0.501   7.227   -45.605 1.00 27.03 ? 126 GLN   A C   1 
ATOM   1019 O O   . GLN   A 1 124 ? -0.371  8.097   -45.711 1.00 27.94 ? 126 GLN   A O   1 
ATOM   1020 C CB  . GLN   A 1 124 ? 1.740   7.724   -43.515 1.00 32.40 ? 126 GLN   A CB  1 
ATOM   1021 C CG  . GLN   A 1 124 ? 1.979   7.484   -42.035 1.00 43.10 ? 126 GLN   A CG  1 
ATOM   1022 C CD  . GLN   A 1 124 ? 0.791   7.880   -41.180 1.00 52.80 ? 126 GLN   A CD  1 
ATOM   1023 O OE1 . GLN   A 1 124 ? -0.157  8.499   -41.663 1.00 47.50 ? 126 GLN   A OE1 1 
ATOM   1024 N NE2 . GLN   A 1 124 ? 0.836   7.522   -39.902 1.00 54.50 ? 126 GLN   A NE2 1 
ATOM   1025 N N   . THR   A 1 125 ? 1.169   6.764   -46.667 1.00 25.14 ? 127 THR   A N   1 
ATOM   1026 C CA  . THR   A 1 125 ? 1.031   7.395   -47.972 1.00 24.24 ? 127 THR   A CA  1 
ATOM   1027 C C   . THR   A 1 125 ? 0.377   6.525   -49.036 1.00 30.28 ? 127 THR   A C   1 
ATOM   1028 O O   . THR   A 1 125 ? -0.072  7.065   -50.054 1.00 31.97 ? 127 THR   A O   1 
ATOM   1029 C CB  . THR   A 1 125 ? 2.404   7.849   -48.489 1.00 37.88 ? 127 THR   A CB  1 
ATOM   1030 O OG1 . THR   A 1 125 ? 3.218   6.704   -48.765 1.00 41.47 ? 127 THR   A OG1 1 
ATOM   1031 C CG2 . THR   A 1 125 ? 3.098   8.710   -47.445 1.00 39.99 ? 127 THR   A CG2 1 
ATOM   1032 N N   . LEU   A 1 126 ? 0.304   5.213   -48.835 1.00 30.12 ? 128 LEU   A N   1 
ATOM   1033 C CA  . LEU   A 1 126 ? -0.230  4.337   -49.870 1.00 31.70 ? 128 LEU   A CA  1 
ATOM   1034 C C   . LEU   A 1 126 ? -1.699  4.641   -50.150 1.00 30.25 ? 128 LEU   A C   1 
ATOM   1035 O O   . LEU   A 1 126 ? -2.505  4.824   -49.232 1.00 29.10 ? 128 LEU   A O   1 
ATOM   1036 C CB  . LEU   A 1 126 ? -0.065  2.872   -49.472 1.00 32.45 ? 128 LEU   A CB  1 
ATOM   1037 C CG  . LEU   A 1 126 ? 1.367   2.339   -49.401 1.00 35.25 ? 128 LEU   A CG  1 
ATOM   1038 C CD1 . LEU   A 1 126 ? 1.357   0.827   -49.287 1.00 37.54 ? 128 LEU   A CD1 1 
ATOM   1039 C CD2 . LEU   A 1 126 ? 2.188   2.782   -50.602 1.00 32.38 ? 128 LEU   A CD2 1 
ATOM   1040 N N   . THR   A 1 127 ? -2.037  4.708   -51.435 1.00 26.72 ? 129 THR   A N   1 
ATOM   1041 C CA  . THR   A 1 127 ? -3.406  4.899   -51.877 1.00 22.47 ? 129 THR   A CA  1 
ATOM   1042 C C   . THR   A 1 127 ? -4.144  3.563   -51.910 1.00 23.44 ? 129 THR   A C   1 
ATOM   1043 O O   . THR   A 1 127 ? -3.554  2.489   -51.765 1.00 22.48 ? 129 THR   A O   1 
ATOM   1044 C CB  . THR   A 1 127 ? -3.437  5.539   -53.267 1.00 23.77 ? 129 THR   A CB  1 
ATOM   1045 O OG1 . THR   A 1 127 ? -2.880  4.629   -54.220 1.00 22.76 ? 129 THR   A OG1 1 
ATOM   1046 C CG2 . THR   A 1 127 ? -2.634  6.831   -53.286 1.00 24.58 ? 129 THR   A CG2 1 
ATOM   1047 N N   . ASP   A 1 128 ? -5.461  3.642   -52.110 1.00 22.12 ? 130 ASP   A N   1 
ATOM   1048 C CA  . ASP   A 1 128 ? -6.256  2.435   -52.335 1.00 21.27 ? 130 ASP   A CA  1 
ATOM   1049 C C   . ASP   A 1 128 ? -5.651  1.595   -53.458 1.00 22.62 ? 130 ASP   A C   1 
ATOM   1050 O O   . ASP   A 1 128 ? -5.429  0.387   -53.299 1.00 21.38 ? 130 ASP   A O   1 
ATOM   1051 C CB  . ASP   A 1 128 ? -7.705  2.830   -52.644 1.00 21.72 ? 130 ASP   A CB  1 
ATOM   1052 C CG  . ASP   A 1 128 ? -8.578  1.650   -53.038 1.00 28.56 ? 130 ASP   A CG  1 
ATOM   1053 O OD1 . ASP   A 1 128 ? -8.514  0.597   -52.378 1.00 24.77 ? 130 ASP   A OD1 1 
ATOM   1054 O OD2 . ASP   A 1 128 ? -9.368  1.789   -53.991 1.00 32.40 ? 130 ASP   A OD2 1 
ATOM   1055 N N   . TYR   A 1 129 ? -5.314  2.239   -54.579 1.00 21.03 ? 131 TYR   A N   1 
ATOM   1056 C CA  . TYR   A 1 129 ? -4.706  1.517   -55.685 1.00 19.33 ? 131 TYR   A CA  1 
ATOM   1057 C C   . TYR   A 1 129 ? -3.374  0.896   -55.275 1.00 19.55 ? 131 TYR   A C   1 
ATOM   1058 O O   . TYR   A 1 129 ? -3.102  -0.261  -55.610 1.00 21.27 ? 131 TYR   A O   1 
ATOM   1059 C CB  . TYR   A 1 129 ? -4.521  2.447   -56.885 1.00 19.80 ? 131 TYR   A CB  1 
ATOM   1060 C CG  . TYR   A 1 129 ? -4.074  1.694   -58.105 1.00 19.75 ? 131 TYR   A CG  1 
ATOM   1061 C CD1 . TYR   A 1 129 ? -4.986  1.036   -58.911 1.00 24.75 ? 131 TYR   A CD1 1 
ATOM   1062 C CD2 . TYR   A 1 129 ? -2.725  1.614   -58.433 1.00 20.60 ? 131 TYR   A CD2 1 
ATOM   1063 C CE1 . TYR   A 1 129 ? -4.583  0.332   -60.024 1.00 27.23 ? 131 TYR   A CE1 1 
ATOM   1064 C CE2 . TYR   A 1 129 ? -2.306  0.906   -59.547 1.00 24.84 ? 131 TYR   A CE2 1 
ATOM   1065 C CZ  . TYR   A 1 129 ? -3.247  0.270   -60.341 1.00 27.21 ? 131 TYR   A CZ  1 
ATOM   1066 O OH  . TYR   A 1 129 ? -2.849  -0.438  -61.447 1.00 33.65 ? 131 TYR   A OH  1 
ATOM   1067 N N   . ASP   A 1 130 ? -2.554  1.640   -54.523 1.00 20.27 ? 132 ASP   A N   1 
ATOM   1068 C CA  . ASP   A 1 130 ? -1.261  1.117   -54.069 1.00 21.34 ? 132 ASP   A CA  1 
ATOM   1069 C C   . ASP   A 1 130 ? -1.435  -0.165  -53.260 1.00 19.75 ? 132 ASP   A C   1 
ATOM   1070 O O   . ASP   A 1 130 ? -0.687  -1.135  -53.444 1.00 20.27 ? 132 ASP   A O   1 
ATOM   1071 C CB  . ASP   A 1 130 ? -0.527  2.148   -53.207 1.00 23.40 ? 132 ASP   A CB  1 
ATOM   1072 C CG  . ASP   A 1 130 ? 0.039   3.309   -53.989 1.00 29.07 ? 132 ASP   A CG  1 
ATOM   1073 O OD1 . ASP   A 1 130 ? 0.308   3.172   -55.202 1.00 26.00 ? 132 ASP   A OD1 1 
ATOM   1074 O OD2 . ASP   A 1 130 ? 0.235   4.374   -53.354 1.00 26.73 ? 132 ASP   A OD2 1 
ATOM   1075 N N   . ILE   A 1 131 ? -2.389  -0.166  -52.327 1.00 20.00 ? 133 ILE   A N   1 
ATOM   1076 C CA  . ILE   A 1 131 ? -2.599  -1.311  -51.441 1.00 17.26 ? 133 ILE   A CA  1 
ATOM   1077 C C   . ILE   A 1 131 ? -3.002  -2.539  -52.240 1.00 21.88 ? 133 ILE   A C   1 
ATOM   1078 O O   . ILE   A 1 131 ? -2.488  -3.642  -52.013 1.00 19.36 ? 133 ILE   A O   1 
ATOM   1079 C CB  . ILE   A 1 131 ? -3.649  -0.963  -50.371 1.00 24.02 ? 133 ILE   A CB  1 
ATOM   1080 C CG1 . ILE   A 1 131 ? -3.148  0.187   -49.493 1.00 21.97 ? 133 ILE   A CG1 1 
ATOM   1081 C CG2 . ILE   A 1 131 ? -3.987  -2.184  -49.513 1.00 18.99 ? 133 ILE   A CG2 1 
ATOM   1082 C CD1 . ILE   A 1 131 ? -4.188  0.691   -48.505 1.00 27.91 ? 133 ILE   A CD1 1 
ATOM   1083 N N   . ARG   A 1 132 ? -3.918  -2.371  -53.196 1.00 18.25 ? 134 ARG   A N   1 
ATOM   1084 C CA  . ARG   A 1 132 ? -4.317  -3.499  -54.033 1.00 18.11 ? 134 ARG   A CA  1 
ATOM   1085 C C   . ARG   A 1 132 ? -3.119  -4.025  -54.814 1.00 18.42 ? 134 ARG   A C   1 
ATOM   1086 O O   . ARG   A 1 132 ? -2.897  -5.241  -54.896 1.00 18.18 ? 134 ARG   A O   1 
ATOM   1087 C CB  . ARG   A 1 132 ? -5.447  -3.083  -54.975 1.00 17.22 ? 134 ARG   A CB  1 
ATOM   1088 C CG  . ARG   A 1 132 ? -6.636  -2.476  -54.247 1.00 18.82 ? 134 ARG   A CG  1 
ATOM   1089 C CD  . ARG   A 1 132 ? -7.830  -2.462  -55.120 1.00 24.63 ? 134 ARG   A CD  1 
ATOM   1090 N NE  . ARG   A 1 132 ? -8.841  -1.519  -54.651 1.00 21.35 ? 134 ARG   A NE  1 
ATOM   1091 C CZ  . ARG   A 1 132 ? -10.127 -1.632  -54.948 1.00 20.96 ? 134 ARG   A CZ  1 
ATOM   1092 N NH1 . ARG   A 1 132 ? -10.535 -2.657  -55.679 1.00 24.48 ? 134 ARG   A NH1 1 
ATOM   1093 N NH2 . ARG   A 1 132 ? -10.990 -0.724  -54.526 1.00 22.84 ? 134 ARG   A NH2 1 
ATOM   1094 N N   . PHE   A 1 133 ? -2.342  -3.108  -55.401 1.00 19.38 ? 135 PHE   A N   1 
ATOM   1095 C CA  . PHE   A 1 133 ? -1.190  -3.482  -56.214 1.00 17.07 ? 135 PHE   A CA  1 
ATOM   1096 C C   . PHE   A 1 133 ? -0.185  -4.282  -55.402 1.00 18.85 ? 135 PHE   A C   1 
ATOM   1097 O O   . PHE   A 1 133 ? 0.240   -5.373  -55.805 1.00 20.13 ? 135 PHE   A O   1 
ATOM   1098 C CB  . PHE   A 1 133 ? -0.540  -2.216  -56.774 1.00 18.96 ? 135 PHE   A CB  1 
ATOM   1099 C CG  . PHE   A 1 133 ? 0.688   -2.480  -57.602 1.00 23.68 ? 135 PHE   A CG  1 
ATOM   1100 C CD1 . PHE   A 1 133 ? 0.590   -2.752  -58.958 1.00 29.58 ? 135 PHE   A CD1 1 
ATOM   1101 C CD2 . PHE   A 1 133 ? 1.943   -2.453  -57.017 1.00 23.01 ? 135 PHE   A CD2 1 
ATOM   1102 C CE1 . PHE   A 1 133 ? 1.736   -2.993  -59.719 1.00 26.50 ? 135 PHE   A CE1 1 
ATOM   1103 C CE2 . PHE   A 1 133 ? 3.087   -2.696  -57.773 1.00 28.72 ? 135 PHE   A CE2 1 
ATOM   1104 C CZ  . PHE   A 1 133 ? 2.977   -2.966  -59.120 1.00 27.14 ? 135 PHE   A CZ  1 
ATOM   1105 N N   . TYR   A 1 134 ? 0.195   -3.756  -54.244 1.00 16.54 ? 136 TYR   A N   1 
ATOM   1106 C CA  . TYR   A 1 134 ? 1.217   -4.425  -53.449 1.00 16.39 ? 136 TYR   A CA  1 
ATOM   1107 C C   . TYR   A 1 134 ? 0.680   -5.697  -52.807 1.00 17.14 ? 136 TYR   A C   1 
ATOM   1108 O O   . TYR   A 1 134 ? 1.422   -6.671  -52.656 1.00 16.88 ? 136 TYR   A O   1 
ATOM   1109 C CB  . TYR   A 1 134 ? 1.795   -3.459  -52.415 1.00 18.86 ? 136 TYR   A CB  1 
ATOM   1110 C CG  . TYR   A 1 134 ? 2.722   -2.419  -53.024 1.00 22.59 ? 136 TYR   A CG  1 
ATOM   1111 C CD1 . TYR   A 1 134 ? 3.791   -2.799  -53.828 1.00 19.43 ? 136 TYR   A CD1 1 
ATOM   1112 C CD2 . TYR   A 1 134 ? 2.529   -1.062  -52.799 1.00 22.14 ? 136 TYR   A CD2 1 
ATOM   1113 C CE1 . TYR   A 1 134 ? 4.639   -1.859  -54.393 1.00 19.62 ? 136 TYR   A CE1 1 
ATOM   1114 C CE2 . TYR   A 1 134 ? 3.374   -0.111  -53.361 1.00 23.85 ? 136 TYR   A CE2 1 
ATOM   1115 C CZ  . TYR   A 1 134 ? 4.427   -0.517  -54.150 1.00 22.18 ? 136 TYR   A CZ  1 
ATOM   1116 O OH  . TYR   A 1 134 ? 5.263   0.429   -54.707 1.00 25.17 ? 136 TYR   A OH  1 
ATOM   1117 N N   . MET   A 1 135 ? -0.609  -5.743  -52.454 1.00 17.13 ? 137 MET   A N   1 
ATOM   1118 C CA  . MET   A 1 135 ? -1.163  -7.009  -51.988 1.00 14.12 ? 137 MET   A CA  1 
ATOM   1119 C C   . MET   A 1 135 ? -1.057  -8.087  -53.057 1.00 17.35 ? 137 MET   A C   1 
ATOM   1120 O O   . MET   A 1 135 ? -0.725  -9.239  -52.758 1.00 16.60 ? 137 MET   A O   1 
ATOM   1121 C CB  . MET   A 1 135 ? -2.623  -6.815  -51.584 1.00 16.38 ? 137 MET   A CB  1 
ATOM   1122 C CG  . MET   A 1 135 ? -2.818  -6.177  -50.226 1.00 17.83 ? 137 MET   A CG  1 
ATOM   1123 S SD  . MET   A 1 135 ? -2.440  -7.348  -48.899 1.00 22.67 ? 137 MET   A SD  1 
ATOM   1124 C CE  . MET   A 1 135 ? -3.682  -8.601  -49.202 1.00 34.95 ? 137 MET   A CE  1 
ATOM   1125 N N   . TYR   A 1 136 ? -1.350  -7.731  -54.311 1.00 16.90 ? 138 TYR   A N   1 
ATOM   1126 C CA  . TYR   A 1 136 ? -1.238  -8.688  -55.401 1.00 15.61 ? 138 TYR   A CA  1 
ATOM   1127 C C   . TYR   A 1 136 ? 0.204   -9.156  -55.555 1.00 14.06 ? 138 TYR   A C   1 
ATOM   1128 O O   . TYR   A 1 136 ? 0.455   -10.344 -55.783 1.00 17.17 ? 138 TYR   A O   1 
ATOM   1129 C CB  . TYR   A 1 136 ? -1.759  -8.058  -56.693 1.00 16.95 ? 138 TYR   A CB  1 
ATOM   1130 C CG  . TYR   A 1 136 ? -2.081  -9.028  -57.797 1.00 18.63 ? 138 TYR   A CG  1 
ATOM   1131 C CD1 . TYR   A 1 136 ? -3.245  -9.777  -57.769 1.00 18.65 ? 138 TYR   A CD1 1 
ATOM   1132 C CD2 . TYR   A 1 136 ? -1.232  -9.179  -58.882 1.00 20.41 ? 138 TYR   A CD2 1 
ATOM   1133 C CE1 . TYR   A 1 136 ? -3.552  -10.660 -58.779 1.00 20.97 ? 138 TYR   A CE1 1 
ATOM   1134 C CE2 . TYR   A 1 136 ? -1.532  -10.062 -59.906 1.00 25.23 ? 138 TYR   A CE2 1 
ATOM   1135 C CZ  . TYR   A 1 136 ? -2.697  -10.802 -59.847 1.00 22.18 ? 138 TYR   A CZ  1 
ATOM   1136 O OH  . TYR   A 1 136 ? -2.995  -11.681 -60.865 1.00 30.43 ? 138 TYR   A OH  1 
ATOM   1137 N N   . GLU   A 1 137 ? 1.163   -8.237  -55.407 1.00 15.15 ? 139 GLU   A N   1 
ATOM   1138 C CA  . GLU   A 1 137 ? 2.568   -8.610  -55.506 1.00 16.65 ? 139 GLU   A CA  1 
ATOM   1139 C C   . GLU   A 1 137 ? 2.972   -9.556  -54.383 1.00 16.78 ? 139 GLU   A C   1 
ATOM   1140 O O   . GLU   A 1 137 ? 3.745   -10.497 -54.617 1.00 14.51 ? 139 GLU   A O   1 
ATOM   1141 C CB  . GLU   A 1 137 ? 3.442   -7.354  -55.510 1.00 17.20 ? 139 GLU   A CB  1 
ATOM   1142 C CG  . GLU   A 1 137 ? 3.252   -6.482  -56.759 1.00 17.29 ? 139 GLU   A CG  1 
ATOM   1143 C CD  . GLU   A 1 137 ? 3.546   -7.220  -58.068 1.00 19.26 ? 139 GLU   A CD  1 
ATOM   1144 O OE1 . GLU   A 1 137 ? 4.618   -7.856  -58.160 1.00 24.11 ? 139 GLU   A OE1 1 
ATOM   1145 O OE2 . GLU   A 1 137 ? 2.722   -7.160  -59.009 1.00 27.00 ? 139 GLU   A OE2 1 
ATOM   1146 N N   . ILE   A 1 138 ? 2.473   -9.326  -53.159 1.00 15.37 ? 140 ILE   A N   1 
ATOM   1147 C CA  . ILE   A 1 138 ? 2.751   -10.253 -52.057 1.00 14.25 ? 140 ILE   A CA  1 
ATOM   1148 C C   . ILE   A 1 138 ? 2.167   -11.624 -52.364 1.00 17.71 ? 140 ILE   A C   1 
ATOM   1149 O O   . ILE   A 1 138 ? 2.794   -12.660 -52.106 1.00 14.78 ? 140 ILE   A O   1 
ATOM   1150 C CB  . ILE   A 1 138 ? 2.199   -9.719  -50.719 1.00 16.84 ? 140 ILE   A CB  1 
ATOM   1151 C CG1 . ILE   A 1 138 ? 2.843   -8.391  -50.329 1.00 16.64 ? 140 ILE   A CG1 1 
ATOM   1152 C CG2 . ILE   A 1 138 ? 2.449   -10.742 -49.600 1.00 16.46 ? 140 ILE   A CG2 1 
ATOM   1153 C CD1 . ILE   A 1 138 ? 2.200   -7.739  -49.115 1.00 16.41 ? 140 ILE   A CD1 1 
ATOM   1154 N N   . LEU   A 1 139 ? 0.949   -11.650 -52.904 1.00 14.71 ? 141 LEU   A N   1 
ATOM   1155 C CA  . LEU   A 1 139 ? 0.311   -12.919 -53.216 1.00 15.77 ? 141 LEU   A CA  1 
ATOM   1156 C C   . LEU   A 1 139 ? 1.100   -13.713 -54.247 1.00 14.53 ? 141 LEU   A C   1 
ATOM   1157 O O   . LEU   A 1 139 ? 1.120   -14.950 -54.195 1.00 17.82 ? 141 LEU   A O   1 
ATOM   1158 C CB  . LEU   A 1 139 ? -1.102  -12.666 -53.726 1.00 15.28 ? 141 LEU   A CB  1 
ATOM   1159 C CG  . LEU   A 1 139 ? -2.093  -12.331 -52.615 1.00 16.32 ? 141 LEU   A CG  1 
ATOM   1160 C CD1 . LEU   A 1 139 ? -3.385  -11.791 -53.209 1.00 20.90 ? 141 LEU   A CD1 1 
ATOM   1161 C CD2 . LEU   A 1 139 ? -2.376  -13.554 -51.749 1.00 14.91 ? 141 LEU   A CD2 1 
ATOM   1162 N N   . LYS   A 1 140 ? 1.728   -13.026 -55.216 1.00 14.69 ? 142 LYS   A N   1 
ATOM   1163 C CA  . LYS   A 1 140 ? 2.571   -13.729 -56.180 1.00 15.14 ? 142 LYS   A CA  1 
ATOM   1164 C C   . LYS   A 1 140 ? 3.705   -14.458 -55.469 1.00 15.04 ? 142 LYS   A C   1 
ATOM   1165 O O   . LYS   A 1 140 ? 4.019   -15.608 -55.799 1.00 17.23 ? 142 LYS   A O   1 
ATOM   1166 C CB  . LYS   A 1 140 ? 3.157   -12.756 -57.203 1.00 17.80 ? 142 LYS   A CB  1 
ATOM   1167 C CG  . LYS   A 1 140 ? 2.174   -12.191 -58.206 1.00 23.03 ? 142 LYS   A CG  1 
ATOM   1168 C CD  . LYS   A 1 140 ? 2.932   -11.281 -59.160 1.00 27.80 ? 142 LYS   A CD  1 
ATOM   1169 C CE  . LYS   A 1 140 ? 2.010   -10.547 -60.118 1.00 27.98 ? 142 LYS   A CE  1 
ATOM   1170 N NZ  . LYS   A 1 140 ? 2.798   -9.597  -60.963 1.00 35.34 ? 142 LYS   A NZ  1 
ATOM   1171 N N   . ALA   A 1 141 ? 4.307   -13.806 -54.465 1.00 15.06 ? 143 ALA   A N   1 
ATOM   1172 C CA  . ALA   A 1 141 ? 5.379   -14.429 -53.699 1.00 15.44 ? 143 ALA   A CA  1 
ATOM   1173 C C   . ALA   A 1 141 ? 4.857   -15.597 -52.876 1.00 14.52 ? 143 ALA   A C   1 
ATOM   1174 O O   . ALA   A 1 141 ? 5.483   -16.665 -52.836 1.00 14.54 ? 143 ALA   A O   1 
ATOM   1175 C CB  . ALA   A 1 141 ? 6.045   -13.395 -52.786 1.00 13.06 ? 143 ALA   A CB  1 
ATOM   1176 N N   . LEU   A 1 142 ? 3.693   -15.420 -52.240 1.00 14.47 ? 144 LEU   A N   1 
ATOM   1177 C CA  . LEU   A 1 142 ? 3.153   -16.478 -51.393 1.00 13.16 ? 144 LEU   A CA  1 
ATOM   1178 C C   . LEU   A 1 142 ? 2.653   -17.660 -52.212 1.00 14.38 ? 144 LEU   A C   1 
ATOM   1179 O O   . LEU   A 1 142 ? 2.917   -18.811 -51.850 1.00 14.54 ? 144 LEU   A O   1 
ATOM   1180 C CB  . LEU   A 1 142 ? 2.044   -15.937 -50.497 1.00 12.70 ? 144 LEU   A CB  1 
ATOM   1181 C CG  . LEU   A 1 142 ? 2.503   -14.996 -49.396 1.00 13.04 ? 144 LEU   A CG  1 
ATOM   1182 C CD1 . LEU   A 1 142 ? 1.305   -14.474 -48.610 1.00 15.58 ? 144 LEU   A CD1 1 
ATOM   1183 C CD2 . LEU   A 1 142 ? 3.454   -15.726 -48.467 1.00 13.72 ? 144 LEU   A CD2 1 
ATOM   1184 N N   . ASP   A 1 143 ? 1.939   -17.415 -53.314 1.00 12.96 ? 145 ASP   A N   1 
ATOM   1185 C CA  . ASP   A 1 143 ? 1.561   -18.561 -54.132 1.00 17.21 ? 145 ASP   A CA  1 
ATOM   1186 C C   . ASP   A 1 143 ? 2.795   -19.293 -54.636 1.00 17.35 ? 145 ASP   A C   1 
ATOM   1187 O O   . ASP   A 1 143 ? 2.813   -20.531 -54.678 1.00 18.14 ? 145 ASP   A O   1 
ATOM   1188 C CB  . ASP   A 1 143 ? 0.686   -18.168 -55.314 1.00 19.33 ? 145 ASP   A CB  1 
ATOM   1189 C CG  . ASP   A 1 143 ? 0.268   -19.387 -56.120 1.00 26.64 ? 145 ASP   A CG  1 
ATOM   1190 O OD1 . ASP   A 1 143 ? -0.301  -20.324 -55.512 1.00 19.60 ? 145 ASP   A OD1 1 
ATOM   1191 O OD2 . ASP   A 1 143 ? 0.555   -19.438 -57.332 1.00 27.63 ? 145 ASP   A OD2 1 
ATOM   1192 N N   . TYR   A 1 144 ? 3.844   -18.552 -55.012 1.00 15.77 ? 146 TYR   A N   1 
ATOM   1193 C CA  . TYR   A 1 144 ? 5.057   -19.228 -55.458 1.00 15.98 ? 146 TYR   A CA  1 
ATOM   1194 C C   . TYR   A 1 144 ? 5.633   -20.107 -54.355 1.00 13.55 ? 146 TYR   A C   1 
ATOM   1195 O O   . TYR   A 1 144 ? 5.883   -21.299 -54.572 1.00 16.18 ? 146 TYR   A O   1 
ATOM   1196 C CB  . TYR   A 1 144 ? 6.114   -18.238 -55.949 1.00 16.89 ? 146 TYR   A CB  1 
ATOM   1197 C CG  . TYR   A 1 144 ? 7.295   -18.948 -56.580 1.00 17.35 ? 146 TYR   A CG  1 
ATOM   1198 C CD1 . TYR   A 1 144 ? 7.165   -19.560 -57.819 1.00 16.54 ? 146 TYR   A CD1 1 
ATOM   1199 C CD2 . TYR   A 1 144 ? 8.518   -19.044 -55.927 1.00 16.76 ? 146 TYR   A CD2 1 
ATOM   1200 C CE1 . TYR   A 1 144 ? 8.227   -20.213 -58.412 1.00 18.09 ? 146 TYR   A CE1 1 
ATOM   1201 C CE2 . TYR   A 1 144 ? 9.598   -19.700 -56.513 1.00 16.82 ? 146 TYR   A CE2 1 
ATOM   1202 C CZ  . TYR   A 1 144 ? 9.438   -20.280 -57.754 1.00 18.64 ? 146 TYR   A CZ  1 
ATOM   1203 O OH  . TYR   A 1 144 ? 10.505  -20.930 -58.337 1.00 22.16 ? 146 TYR   A OH  1 
ATOM   1204 N N   . CYS   A 1 145 ? 5.878   -19.547 -53.165 1.00 13.89 ? 147 CYS   A N   1 
ATOM   1205 C CA  . CYS   A 1 145 ? 6.552   -20.368 -52.166 1.00 14.63 ? 147 CYS   A CA  1 
ATOM   1206 C C   . CYS   A 1 145 ? 5.658   -21.523 -51.709 1.00 14.82 ? 147 CYS   A C   1 
ATOM   1207 O O   . CYS   A 1 145 ? 6.141   -22.649 -51.535 1.00 15.80 ? 147 CYS   A O   1 
ATOM   1208 C CB  . CYS   A 1 145 ? 7.075   -19.508 -51.003 1.00 14.46 ? 147 CYS   A CB  1 
ATOM   1209 S SG  . CYS   A 1 145 ? 5.895   -18.820 -49.834 1.00 16.76 ? 147 CYS   A SG  1 
ATOM   1210 N N   . HIS   A 1 146 ? 4.346   -21.290 -51.598 1.00 14.35 ? 148 HIS   A N   1 
ATOM   1211 C CA  . HIS   A 1 146 ? 3.445   -22.394 -51.282 1.00 14.81 ? 148 HIS   A CA  1 
ATOM   1212 C C   . HIS   A 1 146 ? 3.493   -23.469 -52.365 1.00 14.92 ? 148 HIS   A C   1 
ATOM   1213 O O   . HIS   A 1 146 ? 3.546   -24.664 -52.058 1.00 14.50 ? 148 HIS   A O   1 
ATOM   1214 C CB  . HIS   A 1 146 ? 2.008   -21.893 -51.086 1.00 12.58 ? 148 HIS   A CB  1 
ATOM   1215 C CG  . HIS   A 1 146 ? 1.863   -20.947 -49.939 1.00 13.38 ? 148 HIS   A CG  1 
ATOM   1216 N ND1 . HIS   A 1 146 ? 0.746   -20.160 -49.753 1.00 14.18 ? 148 HIS   A ND1 1 
ATOM   1217 C CD2 . HIS   A 1 146 ? 2.716   -20.642 -48.930 1.00 13.83 ? 148 HIS   A CD2 1 
ATOM   1218 C CE1 . HIS   A 1 146 ? 0.913   -19.419 -48.671 1.00 13.26 ? 148 HIS   A CE1 1 
ATOM   1219 N NE2 . HIS   A 1 146 ? 2.108   -19.685 -48.160 1.00 13.23 ? 148 HIS   A NE2 1 
ATOM   1220 N N   . SER   A 1 147 ? 3.453   -23.065 -53.637 1.00 14.47 ? 149 SER   A N   1 
ATOM   1221 C CA  . SER   A 1 147 ? 3.530   -24.023 -54.742 1.00 13.58 ? 149 SER   A CA  1 
ATOM   1222 C C   . SER   A 1 147 ? 4.855   -24.771 -54.752 1.00 15.84 ? 149 SER   A C   1 
ATOM   1223 O O   . SER   A 1 147 ? 4.950   -25.847 -55.356 1.00 17.98 ? 149 SER   A O   1 
ATOM   1224 C CB  . SER   A 1 147 ? 3.329   -23.300 -56.073 1.00 16.80 ? 149 SER   A CB  1 
ATOM   1225 O OG  . SER   A 1 147 ? 4.544   -22.660 -56.496 1.00 18.74 ? 149 SER   A OG  1 
ATOM   1226 N N   . MET   A 1 148 ? 5.884   -24.214 -54.107 1.00 16.10 ? 150 MET   A N   1 
ATOM   1227 C CA  . MET   A 1 148 ? 7.188   -24.844 -53.965 1.00 19.14 ? 150 MET   A CA  1 
ATOM   1228 C C   . MET   A 1 148 ? 7.317   -25.593 -52.649 1.00 16.37 ? 150 MET   A C   1 
ATOM   1229 O O   . MET   A 1 148 ? 8.422   -25.979 -52.274 1.00 18.51 ? 150 MET   A O   1 
ATOM   1230 C CB  . MET   A 1 148 ? 8.291   -23.785 -54.103 1.00 19.46 ? 150 MET   A CB  1 
ATOM   1231 C CG  . MET   A 1 148 ? 8.293   -23.109 -55.454 1.00 18.13 ? 150 MET   A CG  1 
ATOM   1232 S SD  . MET   A 1 148 ? 8.942   -24.210 -56.749 1.00 21.45 ? 150 MET   A SD  1 
ATOM   1233 C CE  . MET   A 1 148 ? 10.702  -24.113 -56.425 1.00 20.55 ? 150 MET   A CE  1 
ATOM   1234 N N   . GLY   A 1 149 ? 6.210   -25.803 -51.934 1.00 17.05 ? 151 GLY   A N   1 
ATOM   1235 C CA  . GLY   A 1 149 ? 6.245   -26.604 -50.727 1.00 18.23 ? 151 GLY   A CA  1 
ATOM   1236 C C   . GLY   A 1 149 ? 6.717   -25.908 -49.472 1.00 14.37 ? 151 GLY   A C   1 
ATOM   1237 O O   . GLY   A 1 149 ? 7.102   -26.583 -48.518 1.00 17.78 ? 151 GLY   A O   1 
ATOM   1238 N N   . ILE   A 1 150 ? 6.699   -24.582 -49.434 1.00 14.69 ? 152 ILE   A N   1 
ATOM   1239 C CA  . ILE   A 1 150 ? 7.285   -23.841 -48.325 1.00 15.99 ? 152 ILE   A CA  1 
ATOM   1240 C C   . ILE   A 1 150 ? 6.263   -22.870 -47.748 1.00 15.75 ? 152 ILE   A C   1 
ATOM   1241 O O   . ILE   A 1 150 ? 5.560   -22.174 -48.491 1.00 16.87 ? 152 ILE   A O   1 
ATOM   1242 C CB  . ILE   A 1 150 ? 8.564   -23.112 -48.787 1.00 16.66 ? 152 ILE   A CB  1 
ATOM   1243 C CG1 . ILE   A 1 150 ? 9.650   -24.157 -49.122 1.00 17.78 ? 152 ILE   A CG1 1 
ATOM   1244 C CG2 . ILE   A 1 150 ? 9.017   -22.089 -47.731 1.00 16.22 ? 152 ILE   A CG2 1 
ATOM   1245 C CD1 . ILE   A 1 150 ? 10.728  -23.675 -50.086 1.00 23.87 ? 152 ILE   A CD1 1 
ATOM   1246 N N   . MET   A 1 151 ? 6.176   -22.823 -46.417 1.00 14.19 ? 153 MET   A N   1 
ATOM   1247 C CA  . MET   A 1 151 ? 5.423   -21.772 -45.739 1.00 13.97 ? 153 MET   A CA  1 
ATOM   1248 C C   . MET   A 1 151 ? 6.384   -20.782 -45.098 1.00 12.92 ? 153 MET   A C   1 
ATOM   1249 O O   . MET   A 1 151 ? 7.424   -21.169 -44.547 1.00 13.92 ? 153 MET   A O   1 
ATOM   1250 C CB  . MET   A 1 151 ? 4.467   -22.326 -44.686 1.00 21.84 ? 153 MET   A CB  1 
ATOM   1251 C CG  . MET   A 1 151 ? 4.982   -23.437 -43.851 1.00 19.30 ? 153 MET   A CG  1 
ATOM   1252 S SD  . MET   A 1 151 ? 3.655   -24.261 -42.897 1.00 20.72 ? 153 MET   A SD  1 
ATOM   1253 C CE  . MET   A 1 151 ? 4.630   -25.610 -42.247 1.00 25.31 ? 153 MET   A CE  1 
ATOM   1254 N N   . HIS   A 1 152 ? 6.035   -19.500 -45.193 1.00 12.26 ? 154 HIS   A N   1 
ATOM   1255 C CA  . HIS   A 1 152 ? 6.932   -18.447 -44.740 1.00 11.82 ? 154 HIS   A CA  1 
ATOM   1256 C C   . HIS   A 1 152 ? 6.941   -18.336 -43.217 1.00 11.45 ? 154 HIS   A C   1 
ATOM   1257 O O   . HIS   A 1 152 ? 8.012   -18.317 -42.591 1.00 13.57 ? 154 HIS   A O   1 
ATOM   1258 C CB  . HIS   A 1 152 ? 6.559   -17.120 -45.405 1.00 12.79 ? 154 HIS   A CB  1 
ATOM   1259 C CG  . HIS   A 1 152 ? 7.494   -15.994 -45.071 1.00 12.97 ? 154 HIS   A CG  1 
ATOM   1260 N ND1 . HIS   A 1 152 ? 7.423   -15.291 -43.889 1.00 13.24 ? 154 HIS   A ND1 1 
ATOM   1261 C CD2 . HIS   A 1 152 ? 8.522   -15.451 -45.767 1.00 14.01 ? 154 HIS   A CD2 1 
ATOM   1262 C CE1 . HIS   A 1 152 ? 8.369   -14.368 -43.864 1.00 13.30 ? 154 HIS   A CE1 1 
ATOM   1263 N NE2 . HIS   A 1 152 ? 9.043   -14.434 -44.999 1.00 11.72 ? 154 HIS   A NE2 1 
ATOM   1264 N N   . ARG   A 1 153 ? 5.756   -18.281 -42.608 1.00 11.56 ? 155 ARG   A N   1 
ATOM   1265 C CA  . ARG   A 1 153 ? 5.532   -18.318 -41.160 1.00 14.66 ? 155 ARG   A CA  1 
ATOM   1266 C C   . ARG   A 1 153 ? 5.970   -17.048 -40.447 1.00 13.39 ? 155 ARG   A C   1 
ATOM   1267 O O   . ARG   A 1 153 ? 5.979   -17.020 -39.216 1.00 16.00 ? 155 ARG   A O   1 
ATOM   1268 C CB  . ARG   A 1 153 ? 6.205   -19.528 -40.493 1.00 13.78 ? 155 ARG   A CB  1 
ATOM   1269 C CG  . ARG   A 1 153 ? 5.801   -20.859 -41.119 1.00 12.28 ? 155 ARG   A CG  1 
ATOM   1270 C CD  . ARG   A 1 153 ? 6.035   -22.030 -40.189 1.00 14.37 ? 155 ARG   A CD  1 
ATOM   1271 N NE  . ARG   A 1 153 ? 7.437   -22.128 -39.824 1.00 14.43 ? 155 ARG   A NE  1 
ATOM   1272 C CZ  . ARG   A 1 153 ? 7.930   -23.037 -38.990 1.00 17.74 ? 155 ARG   A CZ  1 
ATOM   1273 N NH1 . ARG   A 1 153 ? 7.134   -23.947 -38.436 1.00 16.70 ? 155 ARG   A NH1 1 
ATOM   1274 N NH2 . ARG   A 1 153 ? 9.227   -23.042 -38.716 1.00 15.52 ? 155 ARG   A NH2 1 
ATOM   1275 N N   . ASP   A 1 154 ? 6.302   -15.986 -41.169 1.00 12.62 ? 156 ASP   A N   1 
ATOM   1276 C CA  . ASP   A 1 154 ? 6.607   -14.722 -40.506 1.00 11.06 ? 156 ASP   A CA  1 
ATOM   1277 C C   . ASP   A 1 154 ? 6.196   -13.563 -41.400 1.00 14.07 ? 156 ASP   A C   1 
ATOM   1278 O O   . ASP   A 1 154 ? 6.905   -12.559 -41.508 1.00 13.55 ? 156 ASP   A O   1 
ATOM   1279 C CB  . ASP   A 1 154 ? 8.094   -14.630 -40.128 1.00 12.93 ? 156 ASP   A CB  1 
ATOM   1280 C CG  . ASP   A 1 154 ? 8.374   -13.587 -39.046 1.00 17.21 ? 156 ASP   A CG  1 
ATOM   1281 O OD1 . ASP   A 1 154 ? 7.448   -13.200 -38.291 1.00 18.81 ? 156 ASP   A OD1 1 
ATOM   1282 O OD2 . ASP   A 1 154 ? 9.546   -13.162 -38.942 1.00 19.34 ? 156 ASP   A OD2 1 
ATOM   1283 N N   . VAL   A 1 155 ? 5.017   -13.667 -42.021 1.00 12.30 ? 157 VAL   A N   1 
ATOM   1284 C CA  . VAL   A 1 155 ? 4.529   -12.574 -42.848 1.00 12.56 ? 157 VAL   A CA  1 
ATOM   1285 C C   . VAL   A 1 155 ? 4.104   -11.420 -41.946 1.00 14.86 ? 157 VAL   A C   1 
ATOM   1286 O O   . VAL   A 1 155 ? 3.324   -11.603 -40.998 1.00 13.84 ? 157 VAL   A O   1 
ATOM   1287 C CB  . VAL   A 1 155 ? 3.378   -13.052 -43.746 1.00 13.73 ? 157 VAL   A CB  1 
ATOM   1288 C CG1 . VAL   A 1 155 ? 2.710   -11.850 -44.421 1.00 17.41 ? 157 VAL   A CG1 1 
ATOM   1289 C CG2 . VAL   A 1 155 ? 3.891   -14.079 -44.783 1.00 15.47 ? 157 VAL   A CG2 1 
ATOM   1290 N N   . LYS   A 1 156 ? 4.651   -10.241 -42.205 1.00 13.20 ? 158 LYS   A N   1 
ATOM   1291 C CA  . LYS   A 1 156 ? 4.371   -9.024  -41.454 1.00 13.11 ? 158 LYS   A CA  1 
ATOM   1292 C C   . LYS   A 1 156 ? 4.954   -7.859  -42.247 1.00 14.28 ? 158 LYS   A C   1 
ATOM   1293 O O   . LYS   A 1 156 ? 5.762   -8.082  -43.149 1.00 12.96 ? 158 LYS   A O   1 
ATOM   1294 C CB  . LYS   A 1 156 ? 4.976   -9.086  -40.040 1.00 13.74 ? 158 LYS   A CB  1 
ATOM   1295 C CG  . LYS   A 1 156 ? 6.487   -9.212  -40.022 1.00 14.85 ? 158 LYS   A CG  1 
ATOM   1296 C CD  . LYS   A 1 156 ? 7.012   -9.286  -38.596 1.00 16.14 ? 158 LYS   A CD  1 
ATOM   1297 C CE  . LYS   A 1 156 ? 8.512   -9.450  -38.572 1.00 21.28 ? 158 LYS   A CE  1 
ATOM   1298 N NZ  . LYS   A 1 156 ? 9.015   -9.387  -37.152 1.00 28.09 ? 158 LYS   A NZ  1 
ATOM   1299 N N   . PRO   A 1 157 ? 4.529   -6.619  -41.961 1.00 13.15 ? 159 PRO   A N   1 
ATOM   1300 C CA  . PRO   A 1 157 ? 5.013   -5.487  -42.771 1.00 15.88 ? 159 PRO   A CA  1 
ATOM   1301 C C   . PRO   A 1 157 ? 6.527   -5.358  -42.822 1.00 14.52 ? 159 PRO   A C   1 
ATOM   1302 O O   . PRO   A 1 157 ? 7.063   -5.008  -43.878 1.00 15.98 ? 159 PRO   A O   1 
ATOM   1303 C CB  . PRO   A 1 157 ? 4.364   -4.275  -42.084 1.00 15.29 ? 159 PRO   A CB  1 
ATOM   1304 C CG  . PRO   A 1 157 ? 3.105   -4.832  -41.494 1.00 15.25 ? 159 PRO   A CG  1 
ATOM   1305 C CD  . PRO   A 1 157 ? 3.478   -6.198  -41.012 1.00 15.26 ? 159 PRO   A CD  1 
ATOM   1306 N N   . HIS   A 1 158 ? 7.212   -5.635  -41.706 1.00 15.16 ? 160 HIS   A N   1 
ATOM   1307 C CA  . HIS   A 1 158 ? 8.668   -5.536  -41.622 1.00 15.88 ? 160 HIS   A CA  1 
ATOM   1308 C C   . HIS   A 1 158 ? 9.364   -6.475  -42.592 1.00 16.83 ? 160 HIS   A C   1 
ATOM   1309 O O   . HIS   A 1 158 ? 10.543  -6.267  -42.898 1.00 18.63 ? 160 HIS   A O   1 
ATOM   1310 C CB  . HIS   A 1 158 ? 9.151   -5.864  -40.206 1.00 20.69 ? 160 HIS   A CB  1 
ATOM   1311 C CG  . HIS   A 1 158 ? 8.240   -5.408  -39.101 1.00 42.65 ? 160 HIS   A CG  1 
ATOM   1312 N ND1 . HIS   A 1 158 ? 6.923   -5.810  -38.991 1.00 44.01 ? 160 HIS   A ND1 1 
ATOM   1313 C CD2 . HIS   A 1 158 ? 8.481   -4.620  -38.025 1.00 45.90 ? 160 HIS   A CD2 1 
ATOM   1314 C CE1 . HIS   A 1 158 ? 6.386   -5.267  -37.913 1.00 50.61 ? 160 HIS   A CE1 1 
ATOM   1315 N NE2 . HIS   A 1 158 ? 7.310   -4.542  -37.308 1.00 51.08 ? 160 HIS   A NE2 1 
ATOM   1316 N N   . ASN   A 1 159 ? 8.686   -7.518  -43.067 1.00 14.58 ? 161 ASN   A N   1 
ATOM   1317 C CA  . ASN   A 1 159 ? 9.312   -8.490  -43.953 1.00 13.14 ? 161 ASN   A CA  1 
ATOM   1318 C C   . ASN   A 1 159 ? 8.885   -8.327  -45.400 1.00 11.19 ? 161 ASN   A C   1 
ATOM   1319 O O   . ASN   A 1 159 ? 9.146   -9.218  -46.220 1.00 14.35 ? 161 ASN   A O   1 
ATOM   1320 C CB  . ASN   A 1 159 ? 9.017   -9.902  -43.465 1.00 13.03 ? 161 ASN   A CB  1 
ATOM   1321 C CG  . ASN   A 1 159 ? 9.820   -10.249 -42.231 1.00 16.82 ? 161 ASN   A CG  1 
ATOM   1322 O OD1 . ASN   A 1 159 ? 10.849  -9.610  -41.950 1.00 17.24 ? 161 ASN   A OD1 1 
ATOM   1323 N ND2 . ASN   A 1 159 ? 9.374   -11.242 -41.484 1.00 14.79 ? 161 ASN   A ND2 1 
ATOM   1324 N N   . VAL   A 1 160 ? 8.251   -7.214  -45.733 1.00 13.33 ? 162 VAL   A N   1 
ATOM   1325 C CA  . VAL   A 1 160 ? 7.897   -6.877  -47.101 1.00 14.86 ? 162 VAL   A CA  1 
ATOM   1326 C C   . VAL   A 1 160 ? 8.684   -5.618  -47.435 1.00 19.73 ? 162 VAL   A C   1 
ATOM   1327 O O   . VAL   A 1 160 ? 8.356   -4.524  -46.960 1.00 21.96 ? 162 VAL   A O   1 
ATOM   1328 C CB  . VAL   A 1 160 ? 6.389   -6.669  -47.258 1.00 18.09 ? 162 VAL   A CB  1 
ATOM   1329 C CG1 . VAL   A 1 160 ? 6.055   -6.394  -48.692 1.00 18.59 ? 162 VAL   A CG1 1 
ATOM   1330 C CG2 . VAL   A 1 160 ? 5.667   -7.919  -46.795 1.00 18.69 ? 162 VAL   A CG2 1 
ATOM   1331 N N   . MET   A 1 161 ? 9.752   -5.764  -48.213 1.00 16.84 ? 163 MET   A N   1 
ATOM   1332 C CA  . MET   A 1 161 ? 10.555  -4.621  -48.626 1.00 17.89 ? 163 MET   A CA  1 
ATOM   1333 C C   . MET   A 1 161 ? 9.960   -4.036  -49.900 1.00 16.51 ? 163 MET   A C   1 
ATOM   1334 O O   . MET   A 1 161 ? 9.788   -4.747  -50.893 1.00 20.96 ? 163 MET   A O   1 
ATOM   1335 C CB  . MET   A 1 161 ? 12.012  -5.031  -48.855 1.00 17.41 ? 163 MET   A CB  1 
ATOM   1336 C CG  . MET   A 1 161 ? 12.770  -5.419  -47.584 1.00 21.90 ? 163 MET   A CG  1 
ATOM   1337 S SD  . MET   A 1 161 ? 13.049  -4.000  -46.499 1.00 23.80 ? 163 MET   A SD  1 
ATOM   1338 C CE  . MET   A 1 161 ? 12.068  -4.449  -45.074 1.00 32.96 ? 163 MET   A CE  1 
ATOM   1339 N N   . ILE   A 1 162 ? 9.641   -2.745  -49.874 1.00 17.31 ? 164 ILE   A N   1 
ATOM   1340 C CA  . ILE   A 1 162 ? 9.025   -2.084  -51.017 1.00 17.61 ? 164 ILE   A CA  1 
ATOM   1341 C C   . ILE   A 1 162 ? 9.895   -0.911  -51.439 1.00 21.79 ? 164 ILE   A C   1 
ATOM   1342 O O   . ILE   A 1 162 ? 10.145  0.000   -50.641 1.00 21.92 ? 164 ILE   A O   1 
ATOM   1343 C CB  . ILE   A 1 162 ? 7.597   -1.616  -50.701 1.00 17.84 ? 164 ILE   A CB  1 
ATOM   1344 C CG1 . ILE   A 1 162 ? 6.700   -2.826  -50.479 1.00 19.23 ? 164 ILE   A CG1 1 
ATOM   1345 C CG2 . ILE   A 1 162 ? 7.075   -0.748  -51.833 1.00 25.04 ? 164 ILE   A CG2 1 
ATOM   1346 C CD1 . ILE   A 1 162 ? 5.275   -2.459  -50.030 1.00 21.81 ? 164 ILE   A CD1 1 
ATOM   1347 N N   . ASP   A 1 163 ? 10.353  -0.939  -52.691 1.00 23.29 ? 165 ASP   A N   1 
ATOM   1348 C CA  . ASP   A 1 163 ? 10.967  0.217   -53.340 1.00 23.39 ? 165 ASP   A CA  1 
ATOM   1349 C C   . ASP   A 1 163 ? 9.858   0.933   -54.098 1.00 27.74 ? 165 ASP   A C   1 
ATOM   1350 O O   . ASP   A 1 163 ? 9.567   0.607   -55.252 1.00 31.01 ? 165 ASP   A O   1 
ATOM   1351 C CB  . ASP   A 1 163 ? 12.103  -0.206  -54.269 1.00 23.08 ? 165 ASP   A CB  1 
ATOM   1352 C CG  . ASP   A 1 163 ? 12.761  0.976   -54.970 1.00 26.55 ? 165 ASP   A CG  1 
ATOM   1353 O OD1 . ASP   A 1 163 ? 12.206  2.097   -54.935 1.00 30.01 ? 165 ASP   A OD1 1 
ATOM   1354 O OD2 . ASP   A 1 163 ? 13.847  0.790   -55.561 1.00 28.76 ? 165 ASP   A OD2 1 
ATOM   1355 N N   . HIS   A 1 164 ? 9.257   1.931   -53.448 1.00 22.42 ? 166 HIS   A N   1 
ATOM   1356 C CA  . HIS   A 1 164 ? 8.057   2.554   -53.992 1.00 26.25 ? 166 HIS   A CA  1 
ATOM   1357 C C   . HIS   A 1 164 ? 8.336   3.295   -55.294 1.00 33.84 ? 166 HIS   A C   1 
ATOM   1358 O O   . HIS   A 1 164 ? 7.426   3.459   -56.117 1.00 36.16 ? 166 HIS   A O   1 
ATOM   1359 C CB  . HIS   A 1 164 ? 7.457   3.503   -52.957 1.00 26.95 ? 166 HIS   A CB  1 
ATOM   1360 C CG  . HIS   A 1 164 ? 6.047   3.904   -53.257 1.00 32.26 ? 166 HIS   A CG  1 
ATOM   1361 N ND1 . HIS   A 1 164 ? 5.132   3.036   -53.813 1.00 31.24 ? 166 HIS   A ND1 1 
ATOM   1362 C CD2 . HIS   A 1 164 ? 5.392   5.075   -53.072 1.00 31.14 ? 166 HIS   A CD2 1 
ATOM   1363 C CE1 . HIS   A 1 164 ? 3.975   3.657   -53.963 1.00 34.88 ? 166 HIS   A CE1 1 
ATOM   1364 N NE2 . HIS   A 1 164 ? 4.105   4.894   -53.518 1.00 35.71 ? 166 HIS   A NE2 1 
ATOM   1365 N N   . GLU   A 1 165 ? 9.576   3.748   -55.499 1.00 33.53 ? 167 GLU   A N   1 
ATOM   1366 C CA  . GLU   A 1 165 ? 9.901   4.486   -56.716 1.00 31.55 ? 167 GLU   A CA  1 
ATOM   1367 C C   . GLU   A 1 165 ? 9.753   3.607   -57.950 1.00 38.51 ? 167 GLU   A C   1 
ATOM   1368 O O   . GLU   A 1 165 ? 9.235   4.053   -58.980 1.00 44.82 ? 167 GLU   A O   1 
ATOM   1369 C CB  . GLU   A 1 165 ? 11.321  5.046   -56.630 1.00 36.76 ? 167 GLU   A CB  1 
ATOM   1370 C CG  . GLU   A 1 165 ? 11.700  5.931   -57.804 1.00 46.54 ? 167 GLU   A CG  1 
ATOM   1371 C CD  . GLU   A 1 165 ? 13.189  6.196   -57.880 1.00 59.31 ? 167 GLU   A CD  1 
ATOM   1372 O OE1 . GLU   A 1 165 ? 13.961  5.433   -57.262 1.00 61.38 ? 167 GLU   A OE1 1 
ATOM   1373 O OE2 . GLU   A 1 165 ? 13.589  7.166   -58.560 1.00 62.61 ? 167 GLU   A OE2 1 
ATOM   1374 N N   . HIS   A 1 166 ? 10.197  2.355   -57.866 1.00 34.88 ? 168 HIS   A N   1 
ATOM   1375 C CA  . HIS   A 1 166 ? 10.119  1.424   -58.982 1.00 28.49 ? 168 HIS   A CA  1 
ATOM   1376 C C   . HIS   A 1 166 ? 8.994   0.414   -58.834 1.00 28.51 ? 168 HIS   A C   1 
ATOM   1377 O O   . HIS   A 1 166 ? 8.919   -0.525  -59.631 1.00 31.50 ? 168 HIS   A O   1 
ATOM   1378 C CB  . HIS   A 1 166 ? 11.452  0.705   -59.156 1.00 30.63 ? 168 HIS   A CB  1 
ATOM   1379 C CG  . HIS   A 1 166 ? 12.581  1.630   -59.479 1.00 42.03 ? 168 HIS   A CG  1 
ATOM   1380 N ND1 . HIS   A 1 166 ? 13.527  2.004   -58.549 1.00 44.43 ? 168 HIS   A ND1 1 
ATOM   1381 C CD2 . HIS   A 1 166 ? 12.894  2.285   -60.621 1.00 44.08 ? 168 HIS   A CD2 1 
ATOM   1382 C CE1 . HIS   A 1 166 ? 14.385  2.837   -59.111 1.00 45.02 ? 168 HIS   A CE1 1 
ATOM   1383 N NE2 . HIS   A 1 166 ? 14.023  3.025   -60.367 1.00 46.68 ? 168 HIS   A NE2 1 
ATOM   1384 N N   . ARG   A 1 167 ? 8.122   0.588   -57.839 1.00 26.82 ? 169 ARG   A N   1 
ATOM   1385 C CA  . ARG   A 1 167 ? 6.971   -0.293  -57.634 1.00 24.22 ? 169 ARG   A CA  1 
ATOM   1386 C C   . ARG   A 1 167 ? 7.418   -1.748  -57.517 1.00 23.35 ? 169 ARG   A C   1 
ATOM   1387 O O   . ARG   A 1 167 ? 6.794   -2.658  -58.064 1.00 31.08 ? 169 ARG   A O   1 
ATOM   1388 C CB  . ARG   A 1 167 ? 5.949   -0.115  -58.757 1.00 29.97 ? 169 ARG   A CB  1 
ATOM   1389 C CG  . ARG   A 1 167 ? 5.531   1.333   -58.960 1.00 33.07 ? 169 ARG   A CG  1 
ATOM   1390 C CD  . ARG   A 1 167 ? 4.440   1.730   -57.984 1.00 45.62 ? 169 ARG   A CD  1 
ATOM   1391 N NE  . ARG   A 1 167 ? 3.112   1.612   -58.588 1.00 53.00 ? 169 ARG   A NE  1 
ATOM   1392 C CZ  . ARG   A 1 167 ? 1.978   1.499   -57.902 1.00 53.32 ? 169 ARG   A CZ  1 
ATOM   1393 N NH1 . ARG   A 1 167 ? 1.993   1.474   -56.579 1.00 52.75 ? 169 ARG   A NH1 1 
ATOM   1394 N NH2 . ARG   A 1 167 ? 0.824   1.402   -58.542 1.00 54.99 ? 169 ARG   A NH2 1 
ATOM   1395 N N   . LYS   A 1 168 ? 8.527   -1.951  -56.807 1.00 23.79 ? 170 LYS   A N   1 
ATOM   1396 C CA  . LYS   A 1 168 ? 9.188   -3.241  -56.642 1.00 24.01 ? 170 LYS   A CA  1 
ATOM   1397 C C   . LYS   A 1 168 ? 9.008   -3.728  -55.210 1.00 20.28 ? 170 LYS   A C   1 
ATOM   1398 O O   . LYS   A 1 168 ? 9.151   -2.951  -54.263 1.00 24.93 ? 170 LYS   A O   1 
ATOM   1399 C CB  . LYS   A 1 168 ? 10.683  -3.135  -56.975 1.00 28.68 ? 170 LYS   A CB  1 
ATOM   1400 C CG  . LYS   A 1 168 ? 11.483  -4.390  -56.648 1.00 33.88 ? 170 LYS   A CG  1 
ATOM   1401 C CD  . LYS   A 1 168 ? 12.893  -4.358  -57.230 1.00 42.02 ? 170 LYS   A CD  1 
ATOM   1402 C CE  . LYS   A 1 168 ? 13.789  -3.402  -56.471 1.00 36.34 ? 170 LYS   A CE  1 
ATOM   1403 N NZ  . LYS   A 1 168 ? 15.216  -3.505  -56.912 1.00 42.20 ? 170 LYS   A NZ  1 
ATOM   1404 N N   . LEU   A 1 169 ? 8.687   -5.014  -55.056 1.00 16.29 ? 171 LEU   A N   1 
ATOM   1405 C CA  . LEU   A 1 169 ? 8.418   -5.608  -53.754 1.00 15.33 ? 171 LEU   A CA  1 
ATOM   1406 C C   . LEU   A 1 169 ? 9.218   -6.895  -53.607 1.00 16.33 ? 171 LEU   A C   1 
ATOM   1407 O O   . LEU   A 1 169 ? 9.310   -7.684  -54.554 1.00 17.78 ? 171 LEU   A O   1 
ATOM   1408 C CB  . LEU   A 1 169 ? 6.916   -5.874  -53.596 1.00 20.17 ? 171 LEU   A CB  1 
ATOM   1409 C CG  . LEU   A 1 169 ? 6.422   -6.443  -52.274 1.00 18.70 ? 171 LEU   A CG  1 
ATOM   1410 C CD1 . LEU   A 1 169 ? 5.024   -5.906  -52.006 1.00 15.34 ? 171 LEU   A CD1 1 
ATOM   1411 C CD2 . LEU   A 1 169 ? 6.437   -7.976  -52.278 1.00 19.35 ? 171 LEU   A CD2 1 
ATOM   1412 N N   . ARG   A 1 170 ? 9.784   -7.117  -52.412 1.00 14.97 ? 172 ARG   A N   1 
ATOM   1413 C CA  . ARG   A 1 170 ? 10.437  -8.378  -52.097 1.00 12.54 ? 172 ARG   A CA  1 
ATOM   1414 C C   . ARG   A 1 170 ? 10.010  -8.869  -50.723 1.00 12.46 ? 172 ARG   A C   1 
ATOM   1415 O O   . ARG   A 1 170 ? 10.035  -8.107  -49.749 1.00 16.15 ? 172 ARG   A O   1 
ATOM   1416 C CB  . ARG   A 1 170 ? 11.971  -8.251  -52.126 1.00 13.85 ? 172 ARG   A CB  1 
ATOM   1417 C CG  . ARG   A 1 170 ? 12.547  -7.908  -53.507 1.00 15.99 ? 172 ARG   A CG  1 
ATOM   1418 C CD  . ARG   A 1 170 ? 12.436  -9.073  -54.468 1.00 18.03 ? 172 ARG   A CD  1 
ATOM   1419 N NE  . ARG   A 1 170 ? 13.047  -8.785  -55.769 1.00 19.98 ? 172 ARG   A NE  1 
ATOM   1420 C CZ  . ARG   A 1 170 ? 12.403  -8.253  -56.805 1.00 20.66 ? 172 ARG   A CZ  1 
ATOM   1421 N NH1 . ARG   A 1 170 ? 11.120  -7.927  -56.718 1.00 22.26 ? 172 ARG   A NH1 1 
ATOM   1422 N NH2 . ARG   A 1 170 ? 13.047  -8.042  -57.943 1.00 27.81 ? 172 ARG   A NH2 1 
ATOM   1423 N N   . LEU   A 1 171 ? 9.649   -10.148 -50.656 1.00 13.58 ? 173 LEU   A N   1 
ATOM   1424 C CA  . LEU   A 1 171 ? 9.375   -10.830 -49.399 1.00 13.02 ? 173 LEU   A CA  1 
ATOM   1425 C C   . LEU   A 1 171 ? 10.705  -11.346 -48.840 1.00 13.92 ? 173 LEU   A C   1 
ATOM   1426 O O   . LEU   A 1 171 ? 11.415  -12.119 -49.506 1.00 13.71 ? 173 LEU   A O   1 
ATOM   1427 C CB  . LEU   A 1 171 ? 8.363   -11.964 -49.618 1.00 13.72 ? 173 LEU   A CB  1 
ATOM   1428 C CG  . LEU   A 1 171 ? 7.938   -12.772 -48.391 1.00 15.15 ? 173 LEU   A CG  1 
ATOM   1429 C CD1 . LEU   A 1 171 ? 7.344   -11.863 -47.310 1.00 17.25 ? 173 LEU   A CD1 1 
ATOM   1430 C CD2 . LEU   A 1 171 ? 6.923   -13.840 -48.816 1.00 16.75 ? 173 LEU   A CD2 1 
ATOM   1431 N N   . ILE   A 1 172 ? 11.042  -10.907 -47.626 1.00 12.81 ? 174 ILE   A N   1 
ATOM   1432 C CA  . ILE   A 1 172 ? 12.347  -11.188 -47.019 1.00 12.48 ? 174 ILE   A CA  1 
ATOM   1433 C C   . ILE   A 1 172 ? 12.189  -12.016 -45.747 1.00 13.02 ? 174 ILE   A C   1 
ATOM   1434 O O   . ILE   A 1 172 ? 11.068  -12.363 -45.339 1.00 13.22 ? 174 ILE   A O   1 
ATOM   1435 C CB  . ILE   A 1 172 ? 13.117  -9.892  -46.703 1.00 14.33 ? 174 ILE   A CB  1 
ATOM   1436 C CG1 . ILE   A 1 172 ? 12.386  -9.034  -45.657 1.00 13.57 ? 174 ILE   A CG1 1 
ATOM   1437 C CG2 . ILE   A 1 172 ? 13.403  -9.093  -47.973 1.00 16.00 ? 174 ILE   A CG2 1 
ATOM   1438 C CD1 . ILE   A 1 172 ? 13.309  -8.020  -44.940 1.00 15.32 ? 174 ILE   A CD1 1 
ATOM   1439 N N   . ASP   A 1 173 ? 13.317  -12.319 -45.105 1.00 13.80 ? 175 ASP   A N   1 
ATOM   1440 C CA  . ASP   A 1 173 ? 13.428  -12.990 -43.803 1.00 14.09 ? 175 ASP   A CA  1 
ATOM   1441 C C   . ASP   A 1 173 ? 12.768  -14.368 -43.740 1.00 13.57 ? 175 ASP   A C   1 
ATOM   1442 O O   . ASP   A 1 173 ? 11.791  -14.605 -43.008 1.00 14.72 ? 175 ASP   A O   1 
ATOM   1443 C CB  . ASP   A 1 173 ? 12.902  -12.139 -42.648 1.00 17.41 ? 175 ASP   A CB  1 
ATOM   1444 C CG  . ASP   A 1 173 ? 13.438  -12.621 -41.301 1.00 30.20 ? 175 ASP   A CG  1 
ATOM   1445 O OD1 . ASP   A 1 173 ? 13.381  -11.855 -40.315 1.00 38.60 ? 175 ASP   A OD1 1 
ATOM   1446 O OD2 . ASP   A 1 173 ? 13.970  -13.755 -41.246 1.00 29.38 ? 175 ASP   A OD2 1 
ATOM   1447 N N   . TRP   A 1 174 ? 13.385  -15.281 -44.482 1.00 13.50 ? 176 TRP   A N   1 
ATOM   1448 C CA  . TRP   A 1 174 ? 12.959  -16.670 -44.550 1.00 13.25 ? 176 TRP   A CA  1 
ATOM   1449 C C   . TRP   A 1 174 ? 13.507  -17.542 -43.424 1.00 11.91 ? 176 TRP   A C   1 
ATOM   1450 O O   . TRP   A 1 174 ? 13.454  -18.778 -43.525 1.00 14.61 ? 176 TRP   A O   1 
ATOM   1451 C CB  . TRP   A 1 174 ? 13.323  -17.224 -45.936 1.00 14.13 ? 176 TRP   A CB  1 
ATOM   1452 C CG  . TRP   A 1 174 ? 12.604  -16.446 -47.003 1.00 16.01 ? 176 TRP   A CG  1 
ATOM   1453 C CD1 . TRP   A 1 174 ? 12.974  -15.234 -47.545 1.00 14.46 ? 176 TRP   A CD1 1 
ATOM   1454 C CD2 . TRP   A 1 174 ? 11.362  -16.794 -47.612 1.00 13.92 ? 176 TRP   A CD2 1 
ATOM   1455 N NE1 . TRP   A 1 174 ? 12.033  -14.824 -48.468 1.00 14.03 ? 176 TRP   A NE1 1 
ATOM   1456 C CE2 . TRP   A 1 174 ? 11.036  -15.763 -48.521 1.00 13.72 ? 176 TRP   A CE2 1 
ATOM   1457 C CE3 . TRP   A 1 174 ? 10.497  -17.887 -47.492 1.00 15.65 ? 176 TRP   A CE3 1 
ATOM   1458 C CZ2 . TRP   A 1 174 ? 9.874   -15.787 -49.290 1.00 13.43 ? 176 TRP   A CZ2 1 
ATOM   1459 C CZ3 . TRP   A 1 174 ? 9.336   -17.899 -48.249 1.00 15.68 ? 176 TRP   A CZ3 1 
ATOM   1460 C CH2 . TRP   A 1 174 ? 9.043   -16.869 -49.148 1.00 15.83 ? 176 TRP   A CH2 1 
ATOM   1461 N N   . GLY   A 1 175 ? 13.966  -16.921 -42.332 1.00 13.67 ? 177 GLY   A N   1 
ATOM   1462 C CA  . GLY   A 1 175 ? 14.553  -17.652 -41.219 1.00 14.10 ? 177 GLY   A CA  1 
ATOM   1463 C C   . GLY   A 1 175 ? 13.583  -18.498 -40.411 1.00 16.00 ? 177 GLY   A C   1 
ATOM   1464 O O   . GLY   A 1 175 ? 14.023  -19.407 -39.698 1.00 18.32 ? 177 GLY   A O   1 
ATOM   1465 N N   . LEU   A 1 176 ? 12.283  -18.215 -40.485 1.00 15.78 ? 178 LEU   A N   1 
ATOM   1466 C CA  . LEU   A 1 176 ? 11.279  -19.061 -39.848 1.00 15.81 ? 178 LEU   A CA  1 
ATOM   1467 C C   . LEU   A 1 176 ? 10.573  -19.988 -40.829 1.00 17.01 ? 178 LEU   A C   1 
ATOM   1468 O O   . LEU   A 1 176 ? 9.731   -20.783 -40.406 1.00 17.69 ? 178 LEU   A O   1 
ATOM   1469 C CB  . LEU   A 1 176 ? 10.228  -18.211 -39.112 1.00 15.02 ? 178 LEU   A CB  1 
ATOM   1470 C CG  . LEU   A 1 176 ? 10.697  -17.499 -37.842 1.00 21.85 ? 178 LEU   A CG  1 
ATOM   1471 C CD1 . LEU   A 1 176 ? 9.530   -16.791 -37.152 1.00 23.97 ? 178 LEU   A CD1 1 
ATOM   1472 C CD2 . LEU   A 1 176 ? 11.361  -18.491 -36.918 1.00 28.16 ? 178 LEU   A CD2 1 
ATOM   1473 N N   . ALA   A 1 177 ? 10.890  -19.914 -42.116 1.00 13.58 ? 179 ALA   A N   1 
ATOM   1474 C CA  . ALA   A 1 177 ? 10.161  -20.686 -43.114 1.00 15.01 ? 179 ALA   A CA  1 
ATOM   1475 C C   . ALA   A 1 177 ? 10.412  -22.182 -42.956 1.00 15.00 ? 179 ALA   A C   1 
ATOM   1476 O O   . ALA   A 1 177 ? 11.452  -22.618 -42.453 1.00 16.26 ? 179 ALA   A O   1 
ATOM   1477 C CB  . ALA   A 1 177 ? 10.545  -20.224 -44.521 1.00 14.48 ? 179 ALA   A CB  1 
ATOM   1478 N N   . GLU   A 1 178 ? 9.437   -22.982 -43.391 1.00 15.30 ? 180 GLU   A N   1 
ATOM   1479 C CA  . GLU   A 1 178 ? 9.536   -24.433 -43.270 1.00 17.12 ? 180 GLU   A CA  1 
ATOM   1480 C C   . GLU   A 1 178 ? 8.960   -25.100 -44.505 1.00 15.38 ? 180 GLU   A C   1 
ATOM   1481 O O   . GLU   A 1 178 ? 8.120   -24.535 -45.210 1.00 16.71 ? 180 GLU   A O   1 
ATOM   1482 C CB  . GLU   A 1 178 ? 8.784   -24.993 -42.051 1.00 19.32 ? 180 GLU   A CB  1 
ATOM   1483 C CG  . GLU   A 1 178 ? 9.641   -25.462 -40.888 1.00 24.18 ? 180 GLU   A CG  1 
ATOM   1484 C CD  . GLU   A 1 178 ? 10.510  -26.691 -41.175 1.00 28.33 ? 180 GLU   A CD  1 
ATOM   1485 O OE1 . GLU   A 1 178 ? 11.082  -27.220 -40.203 1.00 28.94 ? 180 GLU   A OE1 1 
ATOM   1486 O OE2 . GLU   A 1 178 ? 10.644  -27.126 -42.340 1.00 23.51 ? 180 GLU   A OE2 1 
ATOM   1487 N N   . PHE   A 1 179 ? 9.425   -26.324 -44.748 1.00 15.27 ? 181 PHE   A N   1 
ATOM   1488 C CA  . PHE   A 1 179 ? 8.820   -27.199 -45.741 1.00 14.98 ? 181 PHE   A CA  1 
ATOM   1489 C C   . PHE   A 1 179 ? 7.542   -27.813 -45.200 1.00 18.38 ? 181 PHE   A C   1 
ATOM   1490 O O   . PHE   A 1 179 ? 7.514   -28.312 -44.069 1.00 19.26 ? 181 PHE   A O   1 
ATOM   1491 C CB  . PHE   A 1 179 ? 9.790   -28.319 -46.117 1.00 19.68 ? 181 PHE   A CB  1 
ATOM   1492 C CG  . PHE   A 1 179 ? 11.026  -27.839 -46.802 1.00 17.24 ? 181 PHE   A CG  1 
ATOM   1493 C CD1 . PHE   A 1 179 ? 12.125  -27.432 -46.075 1.00 16.66 ? 181 PHE   A CD1 1 
ATOM   1494 C CD2 . PHE   A 1 179 ? 11.077  -27.787 -48.184 1.00 20.48 ? 181 PHE   A CD2 1 
ATOM   1495 C CE1 . PHE   A 1 179 ? 13.268  -26.979 -46.718 1.00 19.34 ? 181 PHE   A CE1 1 
ATOM   1496 C CE2 . PHE   A 1 179 ? 12.212  -27.341 -48.833 1.00 17.13 ? 181 PHE   A CE2 1 
ATOM   1497 C CZ  . PHE   A 1 179 ? 13.301  -26.933 -48.102 1.00 17.60 ? 181 PHE   A CZ  1 
ATOM   1498 N N   . TYR   A 1 180 ? 6.494   -27.790 -46.013 1.00 16.57 ? 182 TYR   A N   1 
ATOM   1499 C CA  . TYR   A 1 180 ? 5.229   -28.410 -45.645 1.00 16.98 ? 182 TYR   A CA  1 
ATOM   1500 C C   . TYR   A 1 180 ? 5.242   -29.898 -45.993 1.00 17.67 ? 182 TYR   A C   1 
ATOM   1501 O O   . TYR   A 1 180 ? 5.422   -30.276 -47.157 1.00 17.85 ? 182 TYR   A O   1 
ATOM   1502 C CB  . TYR   A 1 180 ? 4.049   -27.726 -46.332 1.00 15.93 ? 182 TYR   A CB  1 
ATOM   1503 C CG  . TYR   A 1 180 ? 2.783   -28.476 -45.991 1.00 16.94 ? 182 TYR   A CG  1 
ATOM   1504 C CD1 . TYR   A 1 180 ? 2.277   -28.441 -44.699 1.00 17.66 ? 182 TYR   A CD1 1 
ATOM   1505 C CD2 . TYR   A 1 180 ? 2.156   -29.279 -46.930 1.00 16.92 ? 182 TYR   A CD2 1 
ATOM   1506 C CE1 . TYR   A 1 180 ? 1.144   -29.167 -44.356 1.00 15.29 ? 182 TYR   A CE1 1 
ATOM   1507 C CE2 . TYR   A 1 180 ? 1.034   -29.998 -46.602 1.00 19.17 ? 182 TYR   A CE2 1 
ATOM   1508 C CZ  . TYR   A 1 180 ? 0.534   -29.939 -45.322 1.00 17.21 ? 182 TYR   A CZ  1 
ATOM   1509 O OH  . TYR   A 1 180 ? -0.588  -30.682 -45.022 1.00 17.85 ? 182 TYR   A OH  1 
ATOM   1510 N N   . HIS   A 1 181 ? 4.989   -30.735 -44.992 1.00 17.90 ? 183 HIS   A N   1 
ATOM   1511 C CA  . HIS   A 1 181 ? 4.851   -32.170 -45.188 1.00 22.08 ? 183 HIS   A CA  1 
ATOM   1512 C C   . HIS   A 1 181 ? 3.536   -32.598 -44.564 1.00 21.01 ? 183 HIS   A C   1 
ATOM   1513 O O   . HIS   A 1 181 ? 3.299   -32.308 -43.375 1.00 22.31 ? 183 HIS   A O   1 
ATOM   1514 C CB  . HIS   A 1 181 ? 6.006   -32.936 -44.546 1.00 24.20 ? 183 HIS   A CB  1 
ATOM   1515 C CG  . HIS   A 1 181 ? 7.350   -32.636 -45.135 1.00 23.30 ? 183 HIS   A CG  1 
ATOM   1516 N ND1 . HIS   A 1 181 ? 7.782   -33.180 -46.328 1.00 25.62 ? 183 HIS   A ND1 1 
ATOM   1517 C CD2 . HIS   A 1 181 ? 8.366   -31.864 -44.683 1.00 23.96 ? 183 HIS   A CD2 1 
ATOM   1518 C CE1 . HIS   A 1 181 ? 9.006   -32.751 -46.585 1.00 23.54 ? 183 HIS   A CE1 1 
ATOM   1519 N NE2 . HIS   A 1 181 ? 9.387   -31.957 -45.600 1.00 21.58 ? 183 HIS   A NE2 1 
ATOM   1520 N N   . PRO   A 1 182 ? 2.657   -33.279 -45.304 1.00 21.70 ? 184 PRO   A N   1 
ATOM   1521 C CA  . PRO   A 1 182 ? 1.345   -33.655 -44.753 1.00 19.26 ? 184 PRO   A CA  1 
ATOM   1522 C C   . PRO   A 1 182 ? 1.478   -34.454 -43.463 1.00 22.59 ? 184 PRO   A C   1 
ATOM   1523 O O   . PRO   A 1 182 ? 2.267   -35.395 -43.372 1.00 21.62 ? 184 PRO   A O   1 
ATOM   1524 C CB  . PRO   A 1 182 ? 0.724   -34.502 -45.866 1.00 23.79 ? 184 PRO   A CB  1 
ATOM   1525 C CG  . PRO   A 1 182 ? 1.371   -34.044 -47.099 1.00 30.52 ? 184 PRO   A CG  1 
ATOM   1526 C CD  . PRO   A 1 182 ? 2.781   -33.645 -46.725 1.00 24.36 ? 184 PRO   A CD  1 
ATOM   1527 N N   . GLY   A 1 183 ? 0.685   -34.075 -42.463 1.00 20.78 ? 185 GLY   A N   1 
ATOM   1528 C CA  . GLY   A 1 183 ? 0.698   -34.756 -41.193 1.00 24.05 ? 185 GLY   A CA  1 
ATOM   1529 C C   . GLY   A 1 183 ? 1.779   -34.327 -40.227 1.00 22.66 ? 185 GLY   A C   1 
ATOM   1530 O O   . GLY   A 1 183 ? 1.772   -34.783 -39.079 1.00 23.75 ? 185 GLY   A O   1 
ATOM   1531 N N   . GLN   A 1 184 ? 2.705   -33.468 -40.643 1.00 21.23 ? 186 GLN   A N   1 
ATOM   1532 C CA  . GLN   A 1 184 ? 3.774   -33.027 -39.762 1.00 22.24 ? 186 GLN   A CA  1 
ATOM   1533 C C   . GLN   A 1 184 ? 3.255   -32.013 -38.753 1.00 21.65 ? 186 GLN   A C   1 
ATOM   1534 O O   . GLN   A 1 184 ? 2.459   -31.132 -39.090 1.00 19.76 ? 186 GLN   A O   1 
ATOM   1535 C CB  . GLN   A 1 184 ? 4.911   -32.421 -40.587 1.00 24.12 ? 186 GLN   A CB  1 
ATOM   1536 C CG  . GLN   A 1 184 ? 6.174   -32.073 -39.823 1.00 27.37 ? 186 GLN   A CG  1 
ATOM   1537 C CD  . GLN   A 1 184 ? 7.388   -31.992 -40.748 1.00 34.41 ? 186 GLN   A CD  1 
ATOM   1538 O OE1 . GLN   A 1 184 ? 8.194   -31.062 -40.663 1.00 39.40 ? 186 GLN   A OE1 1 
ATOM   1539 N NE2 . GLN   A 1 184 ? 7.515   -32.970 -41.641 1.00 34.66 ? 186 GLN   A NE2 1 
ATOM   1540 N N   . GLU   A 1 185 ? 3.691   -32.157 -37.507 1.00 21.30 ? 187 GLU   A N   1 
ATOM   1541 C CA  . GLU   A 1 185 ? 3.389   -31.192 -36.456 1.00 22.42 ? 187 GLU   A CA  1 
ATOM   1542 C C   . GLU   A 1 185 ? 4.527   -30.186 -36.356 1.00 24.71 ? 187 GLU   A C   1 
ATOM   1543 O O   . GLU   A 1 185 ? 5.701   -30.568 -36.298 1.00 26.39 ? 187 GLU   A O   1 
ATOM   1544 C CB  . GLU   A 1 185 ? 3.179   -31.896 -35.117 1.00 26.30 ? 187 GLU   A CB  1 
ATOM   1545 C CG  . GLU   A 1 185 ? 2.011   -32.885 -35.139 1.00 31.45 ? 187 GLU   A CG  1 
ATOM   1546 C CD  . GLU   A 1 185 ? 1.587   -33.337 -33.752 1.00 43.73 ? 187 GLU   A CD  1 
ATOM   1547 O OE1 . GLU   A 1 185 ? 0.375   -33.285 -33.457 1.00 45.58 ? 187 GLU   A OE1 1 
ATOM   1548 O OE2 . GLU   A 1 185 ? 2.459   -33.738 -32.952 1.00 48.37 ? 187 GLU   A OE2 1 
ATOM   1549 N N   . TYR   A 1 186 ? 4.179   -28.905 -36.333 1.00 19.22 ? 188 TYR   A N   1 
ATOM   1550 C CA  . TYR   A 1 186 ? 5.156   -27.829 -36.379 1.00 16.18 ? 188 TYR   A CA  1 
ATOM   1551 C C   . TYR   A 1 186 ? 5.173   -27.061 -35.064 1.00 16.52 ? 188 TYR   A C   1 
ATOM   1552 O O   . TYR   A 1 186 ? 4.220   -27.102 -34.280 1.00 19.81 ? 188 TYR   A O   1 
ATOM   1553 C CB  . TYR   A 1 186 ? 4.853   -26.876 -37.543 1.00 17.59 ? 188 TYR   A CB  1 
ATOM   1554 C CG  . TYR   A 1 186 ? 5.043   -27.534 -38.892 1.00 16.02 ? 188 TYR   A CG  1 
ATOM   1555 C CD1 . TYR   A 1 186 ? 6.305   -27.621 -39.457 1.00 20.18 ? 188 TYR   A CD1 1 
ATOM   1556 C CD2 . TYR   A 1 186 ? 3.972   -28.111 -39.576 1.00 18.43 ? 188 TYR   A CD2 1 
ATOM   1557 C CE1 . TYR   A 1 186 ? 6.503   -28.230 -40.673 1.00 22.00 ? 188 TYR   A CE1 1 
ATOM   1558 C CE2 . TYR   A 1 186 ? 4.166   -28.728 -40.804 1.00 17.53 ? 188 TYR   A CE2 1 
ATOM   1559 C CZ  . TYR   A 1 186 ? 5.439   -28.783 -41.339 1.00 19.03 ? 188 TYR   A CZ  1 
ATOM   1560 O OH  . TYR   A 1 186 ? 5.636   -29.394 -42.556 1.00 20.01 ? 188 TYR   A OH  1 
ATOM   1561 N N   . ASN   A 1 187 ? 6.271   -26.342 -34.839 1.00 17.22 ? 189 ASN   A N   1 
ATOM   1562 C CA  . ASN   A 1 187 ? 6.369   -25.451 -33.688 1.00 16.63 ? 189 ASN   A CA  1 
ATOM   1563 C C   . ASN   A 1 187 ? 5.363   -24.311 -33.836 1.00 16.14 ? 189 ASN   A C   1 
ATOM   1564 O O   . ASN   A 1 187 ? 5.239   -23.721 -34.911 1.00 18.70 ? 189 ASN   A O   1 
ATOM   1565 C CB  . ASN   A 1 187 ? 7.805   -24.915 -33.591 1.00 20.13 ? 189 ASN   A CB  1 
ATOM   1566 C CG  . ASN   A 1 187 ? 8.045   -24.028 -32.383 1.00 26.31 ? 189 ASN   A CG  1 
ATOM   1567 O OD1 . ASN   A 1 187 ? 7.215   -23.908 -31.489 1.00 26.01 ? 189 ASN   A OD1 1 
ATOM   1568 N ND2 . ASN   A 1 187 ? 9.225   -23.410 -32.348 1.00 40.59 ? 189 ASN   A ND2 1 
ATOM   1569 N N   . VAL   A 1 188 ? 4.623   -24.013 -32.768 1.00 18.67 ? 190 VAL   A N   1 
ATOM   1570 C CA  . VAL   A 1 188 ? 3.678   -22.901 -32.831 1.00 17.30 ? 190 VAL   A CA  1 
ATOM   1571 C C   . VAL   A 1 188 ? 4.313   -21.571 -32.442 1.00 16.61 ? 190 VAL   A C   1 
ATOM   1572 O O   . VAL   A 1 188 ? 3.667   -20.521 -32.593 1.00 20.25 ? 190 VAL   A O   1 
ATOM   1573 C CB  . VAL   A 1 188 ? 2.418   -23.147 -31.965 1.00 18.54 ? 190 VAL   A CB  1 
ATOM   1574 C CG1 . VAL   A 1 188 ? 1.657   -24.391 -32.435 1.00 21.46 ? 190 VAL   A CG1 1 
ATOM   1575 C CG2 . VAL   A 1 188 ? 2.762   -23.233 -30.480 1.00 19.95 ? 190 VAL   A CG2 1 
ATOM   1576 N N   . ARG   A 1 189 ? 5.572   -21.570 -31.997 1.00 19.12 ? 191 ARG   A N   1 
ATOM   1577 C CA  . ARG   A 1 189 ? 6.258   -20.332 -31.628 1.00 22.48 ? 191 ARG   A CA  1 
ATOM   1578 C C   . ARG   A 1 189 ? 6.920   -19.707 -32.857 1.00 20.99 ? 191 ARG   A C   1 
ATOM   1579 O O   . ARG   A 1 189 ? 8.145   -19.566 -32.960 1.00 23.30 ? 191 ARG   A O   1 
ATOM   1580 C CB  . ARG   A 1 189 ? 7.274   -20.599 -30.519 1.00 21.05 ? 191 ARG   A CB  1 
ATOM   1581 C CG  . ARG   A 1 189 ? 6.641   -21.050 -29.207 1.00 27.15 ? 191 ARG   A CG  1 
ATOM   1582 C CD  . ARG   A 1 189 ? 7.650   -20.966 -28.066 1.00 43.27 ? 191 ARG   A CD  1 
ATOM   1583 N NE  . ARG   A 1 189 ? 7.989   -19.580 -27.752 1.00 55.80 ? 191 ARG   A NE  1 
ATOM   1584 C CZ  . ARG   A 1 189 ? 9.035   -19.208 -27.019 1.00 61.81 ? 191 ARG   A CZ  1 
ATOM   1585 N NH1 . ARG   A 1 189 ? 9.259   -17.921 -26.787 1.00 59.87 ? 191 ARG   A NH1 1 
ATOM   1586 N NH2 . ARG   A 1 189 ? 9.862   -20.121 -26.526 1.00 62.58 ? 191 ARG   A NH2 1 
ATOM   1587 N N   . VAL   A 1 190 ? 6.068   -19.347 -33.813 1.00 18.22 ? 192 VAL   A N   1 
ATOM   1588 C CA  . VAL   A 1 190 ? 6.467   -18.672 -35.036 1.00 16.20 ? 192 VAL   A CA  1 
ATOM   1589 C C   . VAL   A 1 190 ? 5.577   -17.447 -35.220 1.00 17.51 ? 192 VAL   A C   1 
ATOM   1590 O O   . VAL   A 1 190 ? 4.573   -17.268 -34.525 1.00 17.34 ? 192 VAL   A O   1 
ATOM   1591 C CB  . VAL   A 1 190 ? 6.375   -19.593 -36.272 1.00 17.41 ? 192 VAL   A CB  1 
ATOM   1592 C CG1 . VAL   A 1 190 ? 7.315   -20.797 -36.118 1.00 20.44 ? 192 VAL   A CG1 1 
ATOM   1593 C CG2 . VAL   A 1 190 ? 4.928   -20.055 -36.485 1.00 17.80 ? 192 VAL   A CG2 1 
ATOM   1594 N N   . ALA   A 1 191 ? 5.954   -16.610 -36.193 1.00 19.14 ? 193 ALA   A N   1 
ATOM   1595 C CA  . ALA   A 1 191 ? 5.282   -15.356 -36.532 1.00 17.83 ? 193 ALA   A CA  1 
ATOM   1596 C C   . ALA   A 1 191 ? 5.337   -14.347 -35.390 1.00 18.09 ? 193 ALA   A C   1 
ATOM   1597 O O   . ALA   A 1 191 ? 5.528   -14.703 -34.221 1.00 25.53 ? 193 ALA   A O   1 
ATOM   1598 C CB  . ALA   A 1 191 ? 3.825   -15.611 -36.951 1.00 16.48 ? 193 ALA   A CB  1 
ATOM   1599 N N   . SER   A 1 192 ? 5.195   -13.071 -35.714 1.00 16.32 ? 194 SER   A N   1 
ATOM   1600 C CA  . SER   A 1 192 ? 5.128   -12.059 -34.680 1.00 14.89 ? 194 SER   A CA  1 
ATOM   1601 C C   . SER   A 1 192 ? 3.725   -12.012 -34.083 1.00 14.99 ? 194 SER   A C   1 
ATOM   1602 O O   . SER   A 1 192 ? 2.738   -12.288 -34.770 1.00 14.81 ? 194 SER   A O   1 
ATOM   1603 C CB  . SER   A 1 192 ? 5.495   -10.699 -35.259 1.00 24.42 ? 194 SER   A CB  1 
ATOM   1604 O OG  . SER   A 1 192 ? 6.861   -10.689 -35.638 1.00 48.36 ? 194 SER   A OG  1 
ATOM   1605 N N   . ARG   A 1 193 ? 3.648   -11.645 -32.795 1.00 15.05 ? 195 ARG   A N   1 
ATOM   1606 C CA  . ARG   A 1 193 ? 2.401   -11.727 -32.024 1.00 12.38 ? 195 ARG   A CA  1 
ATOM   1607 C C   . ARG   A 1 193 ? 1.169   -11.265 -32.796 1.00 14.70 ? 195 ARG   A C   1 
ATOM   1608 O O   . ARG   A 1 193 ? 0.164   -11.984 -32.873 1.00 14.73 ? 195 ARG   A O   1 
ATOM   1609 C CB  . ARG   A 1 193 ? 2.512   -10.898 -30.747 1.00 15.43 ? 195 ARG   A CB  1 
ATOM   1610 C CG  . ARG   A 1 193 ? 1.270   -11.022 -29.857 1.00 16.38 ? 195 ARG   A CG  1 
ATOM   1611 C CD  . ARG   A 1 193 ? 1.293   -9.994  -28.737 1.00 20.62 ? 195 ARG   A CD  1 
ATOM   1612 N NE  . ARG   A 1 193 ? 2.533   -10.073 -27.980 1.00 26.06 ? 195 ARG   A NE  1 
ATOM   1613 C CZ  . ARG   A 1 193 ? 3.152   -9.024  -27.459 1.00 30.56 ? 195 ARG   A CZ  1 
ATOM   1614 N NH1 . ARG   A 1 193 ? 2.645   -7.805  -27.604 1.00 27.04 ? 195 ARG   A NH1 1 
ATOM   1615 N NH2 . ARG   A 1 193 ? 4.286   -9.193  -26.796 1.00 32.60 ? 195 ARG   A NH2 1 
ATOM   1616 N N   . TYR   A 1 194 ? 1.234   -10.062 -33.373 1.00 14.08 ? 196 TYR   A N   1 
ATOM   1617 C CA  . TYR   A 1 194 ? 0.043   -9.459  -33.976 1.00 13.34 ? 196 TYR   A CA  1 
ATOM   1618 C C   . TYR   A 1 194 ? -0.397  -10.192 -35.232 1.00 14.70 ? 196 TYR   A C   1 
ATOM   1619 O O   . TYR   A 1 194 ? -1.531  -9.993  -35.691 1.00 14.04 ? 196 TYR   A O   1 
ATOM   1620 C CB  . TYR   A 1 194 ? 0.285   -7.986  -34.312 1.00 15.28 ? 196 TYR   A CB  1 
ATOM   1621 C CG  . TYR   A 1 194 ? 0.891   -7.194  -33.185 1.00 14.21 ? 196 TYR   A CG  1 
ATOM   1622 C CD1 . TYR   A 1 194 ? 0.371   -7.266  -31.909 1.00 14.76 ? 196 TYR   A CD1 1 
ATOM   1623 C CD2 . TYR   A 1 194 ? 2.009   -6.392  -33.404 1.00 20.11 ? 196 TYR   A CD2 1 
ATOM   1624 C CE1 . TYR   A 1 194 ? 0.922   -6.533  -30.865 1.00 18.11 ? 196 TYR   A CE1 1 
ATOM   1625 C CE2 . TYR   A 1 194 ? 2.568   -5.657  -32.366 1.00 24.46 ? 196 TYR   A CE2 1 
ATOM   1626 C CZ  . TYR   A 1 194 ? 2.020   -5.744  -31.100 1.00 24.58 ? 196 TYR   A CZ  1 
ATOM   1627 O OH  . TYR   A 1 194 ? 2.560   -5.033  -30.051 1.00 27.74 ? 196 TYR   A OH  1 
ATOM   1628 N N   . PHE   A 1 195 ? 0.471   -11.032 -35.799 1.00 13.13 ? 197 PHE   A N   1 
ATOM   1629 C CA  . PHE   A 1 195 ? 0.196   -11.734 -37.045 1.00 11.06 ? 197 PHE   A CA  1 
ATOM   1630 C C   . PHE   A 1 195 ? 0.052   -13.232 -36.847 1.00 12.25 ? 197 PHE   A C   1 
ATOM   1631 O O   . PHE   A 1 195 ? -0.099  -13.972 -37.825 1.00 14.36 ? 197 PHE   A O   1 
ATOM   1632 C CB  . PHE   A 1 195 ? 1.306   -11.398 -38.053 1.00 12.09 ? 197 PHE   A CB  1 
ATOM   1633 C CG  . PHE   A 1 195 ? 1.462   -9.931  -38.230 1.00 11.05 ? 197 PHE   A CG  1 
ATOM   1634 C CD1 . PHE   A 1 195 ? 0.690   -9.248  -39.147 1.00 12.50 ? 197 PHE   A CD1 1 
ATOM   1635 C CD2 . PHE   A 1 195 ? 2.316   -9.214  -37.395 1.00 14.31 ? 197 PHE   A CD2 1 
ATOM   1636 C CE1 . PHE   A 1 195 ? 0.776   -7.866  -39.248 1.00 14.42 ? 197 PHE   A CE1 1 
ATOM   1637 C CE2 . PHE   A 1 195 ? 2.417   -7.852  -37.510 1.00 13.98 ? 197 PHE   A CE2 1 
ATOM   1638 C CZ  . PHE   A 1 195 ? 1.645   -7.178  -38.431 1.00 15.75 ? 197 PHE   A CZ  1 
ATOM   1639 N N   . LYS   A 1 196 ? 0.075   -13.693 -35.599 1.00 13.36 ? 198 LYS   A N   1 
ATOM   1640 C CA  . LYS   A 1 196 ? -0.079  -15.112 -35.319 1.00 12.97 ? 198 LYS   A CA  1 
ATOM   1641 C C   . LYS   A 1 196 ? -1.498  -15.563 -35.640 1.00 13.14 ? 198 LYS   A C   1 
ATOM   1642 O O   . LYS   A 1 196 ? -2.469  -14.933 -35.204 1.00 14.66 ? 198 LYS   A O   1 
ATOM   1643 C CB  . LYS   A 1 196 ? 0.223   -15.388 -33.849 1.00 15.04 ? 198 LYS   A CB  1 
ATOM   1644 C CG  . LYS   A 1 196 ? 1.701   -15.265 -33.472 1.00 13.12 ? 198 LYS   A CG  1 
ATOM   1645 C CD  . LYS   A 1 196 ? 1.851   -15.411 -31.970 1.00 13.41 ? 198 LYS   A CD  1 
ATOM   1646 C CE  . LYS   A 1 196 ? 3.299   -15.244 -31.539 1.00 16.37 ? 198 LYS   A CE  1 
ATOM   1647 N NZ  . LYS   A 1 196 ? 4.082   -16.465 -31.875 1.00 20.06 ? 198 LYS   A NZ  1 
ATOM   1648 N N   . GLY   A 1 197 ? -1.616  -16.668 -36.374 1.00 14.44 ? 199 GLY   A N   1 
ATOM   1649 C CA  . GLY   A 1 197 ? -2.920  -17.229 -36.671 1.00 15.14 ? 199 GLY   A CA  1 
ATOM   1650 C C   . GLY   A 1 197 ? -3.533  -17.892 -35.455 1.00 12.62 ? 199 GLY   A C   1 
ATOM   1651 O O   . GLY   A 1 197 ? -2.838  -18.302 -34.521 1.00 13.56 ? 199 GLY   A O   1 
ATOM   1652 N N   . PRO   A 1 198 ? -4.857  -18.008 -35.452 1.00 11.96 ? 200 PRO   A N   1 
ATOM   1653 C CA  . PRO   A 1 198 ? -5.540  -18.741 -34.371 1.00 15.21 ? 200 PRO   A CA  1 
ATOM   1654 C C   . PRO   A 1 198 ? -4.972  -20.124 -34.109 1.00 17.66 ? 200 PRO   A C   1 
ATOM   1655 O O   . PRO   A 1 198 ? -4.931  -20.541 -32.938 1.00 15.66 ? 200 PRO   A O   1 
ATOM   1656 C CB  . PRO   A 1 198 ? -6.990  -18.813 -34.879 1.00 15.51 ? 200 PRO   A CB  1 
ATOM   1657 C CG  . PRO   A 1 198 ? -7.142  -17.600 -35.746 1.00 17.58 ? 200 PRO   A CG  1 
ATOM   1658 C CD  . PRO   A 1 198 ? -5.794  -17.398 -36.406 1.00 15.33 ? 200 PRO   A CD  1 
ATOM   1659 N N   . GLU   A 1 199 ? -4.526  -20.846 -35.152 1.00 13.61 ? 201 GLU   A N   1 
ATOM   1660 C CA  . GLU   A 1 199 ? -3.948  -22.173 -34.934 1.00 15.17 ? 201 GLU   A CA  1 
ATOM   1661 C C   . GLU   A 1 199 ? -2.756  -22.106 -33.985 1.00 16.37 ? 201 GLU   A C   1 
ATOM   1662 O O   . GLU   A 1 199 ? -2.571  -22.991 -33.142 1.00 16.37 ? 201 GLU   A O   1 
ATOM   1663 C CB  . GLU   A 1 199 ? -3.536  -22.826 -36.268 1.00 14.99 ? 201 GLU   A CB  1 
ATOM   1664 C CG  . GLU   A 1 199 ? -2.575  -22.032 -37.190 1.00 15.23 ? 201 GLU   A CG  1 
ATOM   1665 C CD  . GLU   A 1 199 ? -3.310  -21.110 -38.160 1.00 14.87 ? 201 GLU   A CD  1 
ATOM   1666 O OE1 . GLU   A 1 199 ? -4.115  -20.281 -37.689 1.00 16.64 ? 201 GLU   A OE1 1 
ATOM   1667 O OE2 . GLU   A 1 199 ? -3.071  -21.190 -39.387 1.00 15.25 ? 201 GLU   A OE2 1 
ATOM   1668 N N   . LEU   A 1 200 ? -1.936  -21.060 -34.099 1.00 13.06 ? 202 LEU   A N   1 
ATOM   1669 C CA  . LEU   A 1 200 ? -0.808  -20.938 -33.187 1.00 13.35 ? 202 LEU   A CA  1 
ATOM   1670 C C   . LEU   A 1 200 ? -1.276  -20.610 -31.782 1.00 14.30 ? 202 LEU   A C   1 
ATOM   1671 O O   . LEU   A 1 200 ? -0.724  -21.116 -30.796 1.00 16.39 ? 202 LEU   A O   1 
ATOM   1672 C CB  . LEU   A 1 200 ? 0.133   -19.854 -33.684 1.00 12.49 ? 202 LEU   A CB  1 
ATOM   1673 C CG  . LEU   A 1 200 ? 0.562   -19.955 -35.137 1.00 13.78 ? 202 LEU   A CG  1 
ATOM   1674 C CD1 . LEU   A 1 200 ? 1.533   -18.834 -35.493 1.00 14.80 ? 202 LEU   A CD1 1 
ATOM   1675 C CD2 . LEU   A 1 200 ? 1.128   -21.339 -35.468 1.00 14.12 ? 202 LEU   A CD2 1 
ATOM   1676 N N   . LEU   A 1 201 ? -2.299  -19.763 -31.677 1.00 14.47 ? 203 LEU   A N   1 
ATOM   1677 C CA  . LEU   A 1 201 ? -2.753  -19.269 -30.392 1.00 15.02 ? 203 LEU   A CA  1 
ATOM   1678 C C   . LEU   A 1 201 ? -3.540  -20.312 -29.617 1.00 15.70 ? 203 LEU   A C   1 
ATOM   1679 O O   . LEU   A 1 201 ? -3.639  -20.204 -28.389 1.00 18.47 ? 203 LEU   A O   1 
ATOM   1680 C CB  . LEU   A 1 201 ? -3.594  -18.008 -30.613 1.00 14.11 ? 203 LEU   A CB  1 
ATOM   1681 C CG  . LEU   A 1 201 ? -2.848  -16.885 -31.346 1.00 14.76 ? 203 LEU   A CG  1 
ATOM   1682 C CD1 . LEU   A 1 201 ? -3.781  -15.743 -31.710 1.00 15.22 ? 203 LEU   A CD1 1 
ATOM   1683 C CD2 . LEU   A 1 201 ? -1.700  -16.368 -30.482 1.00 15.72 ? 203 LEU   A CD2 1 
ATOM   1684 N N   . VAL   A 1 202 ? -4.081  -21.328 -30.292 1.00 17.83 ? 204 VAL   A N   1 
ATOM   1685 C CA  . VAL   A 1 202 ? -4.745  -22.432 -29.604 1.00 17.94 ? 204 VAL   A CA  1 
ATOM   1686 C C   . VAL   A 1 202 ? -3.867  -23.683 -29.566 1.00 16.21 ? 204 VAL   A C   1 
ATOM   1687 O O   . VAL   A 1 202 ? -4.336  -24.746 -29.148 1.00 19.99 ? 204 VAL   A O   1 
ATOM   1688 C CB  . VAL   A 1 202 ? -6.125  -22.746 -30.223 1.00 16.56 ? 204 VAL   A CB  1 
ATOM   1689 C CG1 . VAL   A 1 202 ? -7.039  -21.516 -30.202 1.00 19.24 ? 204 VAL   A CG1 1 
ATOM   1690 C CG2 . VAL   A 1 202 ? -6.001  -23.298 -31.650 1.00 15.99 ? 204 VAL   A CG2 1 
ATOM   1691 N N   . ASP   A 1 203 ? -2.599  -23.578 -30.002 1.00 18.41 ? 205 ASP   A N   1 
ATOM   1692 C CA  . ASP   A 1 203 ? -1.607  -24.658 -29.908 1.00 17.59 ? 205 ASP   A CA  1 
ATOM   1693 C C   . ASP   A 1 203 ? -1.960  -25.845 -30.809 1.00 23.34 ? 205 ASP   A C   1 
ATOM   1694 O O   . ASP   A 1 203 ? -1.759  -27.004 -30.437 1.00 27.38 ? 205 ASP   A O   1 
ATOM   1695 C CB  . ASP   A 1 203 ? -1.425  -25.108 -28.449 1.00 18.11 ? 205 ASP   A CB  1 
ATOM   1696 C CG  . ASP   A 1 203 ? -0.100  -25.810 -28.205 1.00 41.59 ? 205 ASP   A CG  1 
ATOM   1697 O OD1 . ASP   A 1 203 ? 0.751   -25.841 -29.121 1.00 44.33 ? 205 ASP   A OD1 1 
ATOM   1698 O OD2 . ASP   A 1 203 ? 0.085   -26.334 -27.084 1.00 51.60 ? 205 ASP   A OD2 1 
ATOM   1699 N N   . TYR   A 1 204 ? -2.471  -25.563 -32.008 1.00 16.05 ? 206 TYR   A N   1 
ATOM   1700 C CA  . TYR   A 1 204 ? -2.728  -26.607 -32.998 1.00 15.26 ? 206 TYR   A CA  1 
ATOM   1701 C C   . TYR   A 1 204 ? -1.521  -26.707 -33.934 1.00 14.69 ? 206 TYR   A C   1 
ATOM   1702 O O   . TYR   A 1 204 ? -1.240  -25.786 -34.709 1.00 16.83 ? 206 TYR   A O   1 
ATOM   1703 C CB  . TYR   A 1 204 ? -4.013  -26.322 -33.775 1.00 14.93 ? 206 TYR   A CB  1 
ATOM   1704 C CG  . TYR   A 1 204 ? -4.351  -27.459 -34.708 1.00 16.04 ? 206 TYR   A CG  1 
ATOM   1705 C CD1 . TYR   A 1 204 ? -4.918  -28.629 -34.225 1.00 18.29 ? 206 TYR   A CD1 1 
ATOM   1706 C CD2 . TYR   A 1 204 ? -4.061  -27.380 -36.066 1.00 15.37 ? 206 TYR   A CD2 1 
ATOM   1707 C CE1 . TYR   A 1 204 ? -5.201  -29.687 -35.078 1.00 19.09 ? 206 TYR   A CE1 1 
ATOM   1708 C CE2 . TYR   A 1 204 ? -4.327  -28.435 -36.921 1.00 18.05 ? 206 TYR   A CE2 1 
ATOM   1709 C CZ  . TYR   A 1 204 ? -4.898  -29.582 -36.420 1.00 17.13 ? 206 TYR   A CZ  1 
ATOM   1710 O OH  . TYR   A 1 204 ? -5.184  -30.634 -37.260 1.00 20.26 ? 206 TYR   A OH  1 
ATOM   1711 N N   . GLN   A 1 205 ? -0.802  -27.827 -33.861 1.00 14.78 ? 207 GLN   A N   1 
ATOM   1712 C CA  . GLN   A 1 205 ? 0.506   -27.912 -34.501 1.00 14.62 ? 207 GLN   A CA  1 
ATOM   1713 C C   . GLN   A 1 205 ? 0.470   -28.371 -35.956 1.00 18.28 ? 207 GLN   A C   1 
ATOM   1714 O O   . GLN   A 1 205 ? 1.464   -28.182 -36.669 1.00 16.95 ? 207 GLN   A O   1 
ATOM   1715 C CB  . GLN   A 1 205 ? 1.412   -28.859 -33.702 1.00 19.23 ? 207 GLN   A CB  1 
ATOM   1716 C CG  . GLN   A 1 205 ? 1.763   -28.352 -32.316 1.00 19.01 ? 207 GLN   A CG  1 
ATOM   1717 C CD  . GLN   A 1 205 ? 2.727   -29.278 -31.603 1.00 21.37 ? 207 GLN   A CD  1 
ATOM   1718 O OE1 . GLN   A 1 205 ? 2.326   -30.072 -30.753 1.00 28.38 ? 207 GLN   A OE1 1 
ATOM   1719 N NE2 . GLN   A 1 205 ? 4.007   -29.195 -31.967 1.00 25.37 ? 207 GLN   A NE2 1 
ATOM   1720 N N   . MET   A 1 206 ? -0.620  -28.974 -36.424 1.00 15.53 ? 208 MET   A N   1 
ATOM   1721 C CA  . MET   A 1 206 ? -0.640  -29.566 -37.765 1.00 14.72 ? 208 MET   A CA  1 
ATOM   1722 C C   . MET   A 1 206 ? -1.180  -28.556 -38.781 1.00 16.68 ? 208 MET   A C   1 
ATOM   1723 O O   . MET   A 1 206 ? -2.141  -28.798 -39.509 1.00 16.18 ? 208 MET   A O   1 
ATOM   1724 C CB  . MET   A 1 206 ? -1.446  -30.863 -37.770 1.00 18.84 ? 208 MET   A CB  1 
ATOM   1725 C CG  . MET   A 1 206 ? -1.128  -31.773 -38.959 1.00 19.39 ? 208 MET   A CG  1 
ATOM   1726 S SD  . MET   A 1 206 ? -1.954  -33.382 -38.907 1.00 21.26 ? 208 MET   A SD  1 
ATOM   1727 C CE  . MET   A 1 206 ? -1.263  -34.084 -37.415 1.00 27.72 ? 208 MET   A CE  1 
ATOM   1728 N N   . TYR   A 1 207 ? -0.505  -27.405 -38.843 1.00 16.39 ? 209 TYR   A N   1 
ATOM   1729 C CA  . TYR   A 1 207 ? -0.949  -26.297 -39.678 1.00 15.45 ? 209 TYR   A CA  1 
ATOM   1730 C C   . TYR   A 1 207 ? -0.195  -26.312 -41.010 1.00 18.18 ? 209 TYR   A C   1 
ATOM   1731 O O   . TYR   A 1 207 ? 0.597   -27.214 -41.288 1.00 18.64 ? 209 TYR   A O   1 
ATOM   1732 C CB  . TYR   A 1 207 ? -0.793  -24.969 -38.923 1.00 14.20 ? 209 TYR   A CB  1 
ATOM   1733 C CG  . TYR   A 1 207 ? 0.624   -24.602 -38.500 1.00 12.84 ? 209 TYR   A CG  1 
ATOM   1734 C CD1 . TYR   A 1 207 ? 1.502   -24.036 -39.415 1.00 14.12 ? 209 TYR   A CD1 1 
ATOM   1735 C CD2 . TYR   A 1 207 ? 1.059   -24.769 -37.175 1.00 13.09 ? 209 TYR   A CD2 1 
ATOM   1736 C CE1 . TYR   A 1 207 ? 2.791   -23.678 -39.040 1.00 14.98 ? 209 TYR   A CE1 1 
ATOM   1737 C CE2 . TYR   A 1 207 ? 2.359   -24.408 -36.790 1.00 13.73 ? 209 TYR   A CE2 1 
ATOM   1738 C CZ  . TYR   A 1 207 ? 3.206   -23.869 -37.731 1.00 14.88 ? 209 TYR   A CZ  1 
ATOM   1739 O OH  . TYR   A 1 207 ? 4.478   -23.492 -37.371 1.00 16.13 ? 209 TYR   A OH  1 
ATOM   1740 N N   . ASP   A 1 208 ? -0.467  -25.327 -41.860 1.00 13.87 ? 210 ASP   A N   1 
ATOM   1741 C CA  . ASP   A 1 208 ? 0.063   -25.389 -43.218 1.00 12.87 ? 210 ASP   A CA  1 
ATOM   1742 C C   . ASP   A 1 208 ? 0.207   -23.978 -43.783 1.00 11.91 ? 210 ASP   A C   1 
ATOM   1743 O O   . ASP   A 1 208 ? 0.231   -22.994 -43.037 1.00 12.28 ? 210 ASP   A O   1 
ATOM   1744 C CB  . ASP   A 1 208 ? -0.831  -26.293 -44.089 1.00 15.01 ? 210 ASP   A CB  1 
ATOM   1745 C CG  . ASP   A 1 208 ? -2.282  -25.821 -44.147 1.00 18.04 ? 210 ASP   A CG  1 
ATOM   1746 O OD1 . ASP   A 1 208 ? -3.162  -26.511 -43.573 1.00 17.89 ? 210 ASP   A OD1 1 
ATOM   1747 O OD2 . ASP   A 1 208 ? -2.560  -24.767 -44.765 1.00 17.25 ? 210 ASP   A OD2 1 
ATOM   1748 N N   . TYR   A 1 209 ? 0.310   -23.896 -45.118 1.00 14.16 ? 211 TYR   A N   1 
ATOM   1749 C CA  . TYR   A 1 209 ? 0.473   -22.630 -45.830 1.00 14.33 ? 211 TYR   A CA  1 
ATOM   1750 C C   . TYR   A 1 209 ? -0.557  -21.592 -45.422 1.00 12.63 ? 211 TYR   A C   1 
ATOM   1751 O O   . TYR   A 1 209 ? -0.303  -20.381 -45.507 1.00 13.18 ? 211 TYR   A O   1 
ATOM   1752 C CB  . TYR   A 1 209 ? 0.342   -22.843 -47.341 1.00 12.43 ? 211 TYR   A CB  1 
ATOM   1753 C CG  . TYR   A 1 209 ? 1.056   -24.034 -47.929 1.00 13.68 ? 211 TYR   A CG  1 
ATOM   1754 C CD1 . TYR   A 1 209 ? 0.340   -25.121 -48.432 1.00 13.87 ? 211 TYR   A CD1 1 
ATOM   1755 C CD2 . TYR   A 1 209 ? 2.448   -24.057 -48.021 1.00 14.03 ? 211 TYR   A CD2 1 
ATOM   1756 C CE1 . TYR   A 1 209 ? 0.994   -26.210 -48.996 1.00 15.19 ? 211 TYR   A CE1 1 
ATOM   1757 C CE2 . TYR   A 1 209 ? 3.111   -25.145 -48.578 1.00 15.12 ? 211 TYR   A CE2 1 
ATOM   1758 C CZ  . TYR   A 1 209 ? 2.379   -26.207 -49.069 1.00 13.78 ? 211 TYR   A CZ  1 
ATOM   1759 O OH  . TYR   A 1 209 ? 3.038   -27.269 -49.620 1.00 16.73 ? 211 TYR   A OH  1 
ATOM   1760 N N   . SER   A 1 210 ? -1.745  -22.041 -45.026 1.00 12.60 ? 212 SER   A N   1 
ATOM   1761 C CA  . SER   A 1 210 ? -2.830  -21.118 -44.718 1.00 11.48 ? 212 SER   A CA  1 
ATOM   1762 C C   . SER   A 1 210 ? -2.517  -20.206 -43.531 1.00 11.22 ? 212 SER   A C   1 
ATOM   1763 O O   . SER   A 1 210 ? -3.161  -19.162 -43.379 1.00 12.34 ? 212 SER   A O   1 
ATOM   1764 C CB  . SER   A 1 210 ? -4.118  -21.912 -44.475 1.00 15.29 ? 212 SER   A CB  1 
ATOM   1765 O OG  . SER   A 1 210 ? -3.924  -22.904 -43.475 1.00 15.43 ? 212 SER   A OG  1 
ATOM   1766 N N   . LEU   A 1 211 ? -1.518  -20.551 -42.705 1.00 11.57 ? 213 LEU   A N   1 
ATOM   1767 C CA  . LEU   A 1 211 ? -1.063  -19.616 -41.681 1.00 12.89 ? 213 LEU   A CA  1 
ATOM   1768 C C   . LEU   A 1 211 ? -0.663  -18.284 -42.299 1.00 11.53 ? 213 LEU   A C   1 
ATOM   1769 O O   . LEU   A 1 211 ? -0.994  -17.214 -41.760 1.00 12.50 ? 213 LEU   A O   1 
ATOM   1770 C CB  . LEU   A 1 211 ? 0.113   -20.229 -40.917 1.00 14.20 ? 213 LEU   A CB  1 
ATOM   1771 C CG  . LEU   A 1 211 ? 0.888   -19.260 -40.027 1.00 14.53 ? 213 LEU   A CG  1 
ATOM   1772 C CD1 . LEU   A 1 211 ? 0.004   -18.720 -38.895 1.00 15.95 ? 213 LEU   A CD1 1 
ATOM   1773 C CD2 . LEU   A 1 211 ? 2.159   -19.909 -39.477 1.00 14.49 ? 213 LEU   A CD2 1 
ATOM   1774 N N   . ASP   A 1 212 ? 0.052   -18.329 -43.440 1.00 11.49 ? 214 ASP   A N   1 
ATOM   1775 C CA  . ASP   A 1 212 ? 0.520   -17.102 -44.079 1.00 11.85 ? 214 ASP   A CA  1 
ATOM   1776 C C   . ASP   A 1 212 ? -0.647  -16.242 -44.531 1.00 12.11 ? 214 ASP   A C   1 
ATOM   1777 O O   . ASP   A 1 212 ? -0.521  -15.016 -44.600 1.00 12.41 ? 214 ASP   A O   1 
ATOM   1778 C CB  . ASP   A 1 212 ? 1.412   -17.409 -45.286 1.00 11.57 ? 214 ASP   A CB  1 
ATOM   1779 C CG  . ASP   A 1 212 ? 2.729   -18.024 -44.904 1.00 14.65 ? 214 ASP   A CG  1 
ATOM   1780 O OD1 . ASP   A 1 212 ? 3.194   -17.824 -43.759 1.00 13.69 ? 214 ASP   A OD1 1 
ATOM   1781 O OD2 . ASP   A 1 212 ? 3.279   -18.718 -45.770 1.00 13.88 ? 214 ASP   A OD2 1 
ATOM   1782 N N   . MET   A 1 213 ? -1.790  -16.866 -44.825 1.00 12.22 ? 215 MET   A N   1 
ATOM   1783 C CA  . MET   A 1 213 ? -2.944  -16.111 -45.300 1.00 13.00 ? 215 MET   A CA  1 
ATOM   1784 C C   . MET   A 1 213 ? -3.624  -15.355 -44.169 1.00 12.63 ? 215 MET   A C   1 
ATOM   1785 O O   . MET   A 1 213 ? -4.135  -14.250 -44.394 1.00 12.55 ? 215 MET   A O   1 
ATOM   1786 C CB  . MET   A 1 213 ? -3.922  -17.052 -46.009 1.00 13.27 ? 215 MET   A CB  1 
ATOM   1787 C CG  . MET   A 1 213 ? -3.281  -17.773 -47.206 1.00 13.76 ? 215 MET   A CG  1 
ATOM   1788 S SD  . MET   A 1 213 ? -2.448  -16.710 -48.418 1.00 16.17 ? 215 MET   A SD  1 
ATOM   1789 C CE  . MET   A 1 213 ? -3.819  -15.721 -49.011 1.00 19.24 ? 215 MET   A CE  1 
ATOM   1790 N N   . TRP   A 1 214 ? -3.634  -15.916 -42.959 1.00 12.08 ? 216 TRP   A N   1 
ATOM   1791 C CA  . TRP   A 1 214 ? -4.079  -15.144 -41.802 1.00 10.77 ? 216 TRP   A CA  1 
ATOM   1792 C C   . TRP   A 1 214 ? -3.198  -13.925 -41.604 1.00 11.11 ? 216 TRP   A C   1 
ATOM   1793 O O   . TRP   A 1 214 ? -3.692  -12.800 -41.459 1.00 12.95 ? 216 TRP   A O   1 
ATOM   1794 C CB  . TRP   A 1 214 ? -4.064  -15.994 -40.535 1.00 11.50 ? 216 TRP   A CB  1 
ATOM   1795 C CG  . TRP   A 1 214 ? -4.463  -15.154 -39.342 1.00 11.84 ? 216 TRP   A CG  1 
ATOM   1796 C CD1 . TRP   A 1 214 ? -3.644  -14.407 -38.549 1.00 12.21 ? 216 TRP   A CD1 1 
ATOM   1797 C CD2 . TRP   A 1 214 ? -5.793  -14.944 -38.849 1.00 11.57 ? 216 TRP   A CD2 1 
ATOM   1798 N NE1 . TRP   A 1 214 ? -4.373  -13.765 -37.585 1.00 12.88 ? 216 TRP   A NE1 1 
ATOM   1799 C CE2 . TRP   A 1 214 ? -5.697  -14.072 -37.750 1.00 11.14 ? 216 TRP   A CE2 1 
ATOM   1800 C CE3 . TRP   A 1 214 ? -7.049  -15.422 -39.230 1.00 12.83 ? 216 TRP   A CE3 1 
ATOM   1801 C CZ2 . TRP   A 1 214 ? -6.818  -13.654 -37.022 1.00 11.89 ? 216 TRP   A CZ2 1 
ATOM   1802 C CZ3 . TRP   A 1 214 ? -8.160  -15.020 -38.504 1.00 12.40 ? 216 TRP   A CZ3 1 
ATOM   1803 C CH2 . TRP   A 1 214 ? -8.035  -14.144 -37.415 1.00 14.45 ? 216 TRP   A CH2 1 
ATOM   1804 N N   . SER   A 1 215 ? -1.876  -14.137 -41.589 1.00 11.67 ? 217 SER   A N   1 
ATOM   1805 C CA  . SER   A 1 215 ? -0.959  -13.027 -41.391 1.00 11.35 ? 217 SER   A CA  1 
ATOM   1806 C C   . SER   A 1 215 ? -1.182  -11.946 -42.439 1.00 11.24 ? 217 SER   A C   1 
ATOM   1807 O O   . SER   A 1 215 ? -1.187  -10.750 -42.118 1.00 11.16 ? 217 SER   A O   1 
ATOM   1808 C CB  . SER   A 1 215 ? 0.481   -13.552 -41.441 1.00 11.84 ? 217 SER   A CB  1 
ATOM   1809 O OG  . SER   A 1 215 ? 0.673   -14.605 -40.508 1.00 14.08 ? 217 SER   A OG  1 
ATOM   1810 N N   . LEU   A 1 216 ? -1.385  -12.357 -43.699 1.00 11.61 ? 218 LEU   A N   1 
ATOM   1811 C CA  . LEU   A 1 216 ? -1.656  -11.403 -44.766 1.00 11.74 ? 218 LEU   A CA  1 
ATOM   1812 C C   . LEU   A 1 216 ? -2.947  -10.640 -44.499 1.00 13.18 ? 218 LEU   A C   1 
ATOM   1813 O O   . LEU   A 1 216 ? -3.014  -9.423  -44.716 1.00 14.34 ? 218 LEU   A O   1 
ATOM   1814 C CB  . LEU   A 1 216 ? -1.713  -12.125 -46.114 1.00 13.84 ? 218 LEU   A CB  1 
ATOM   1815 C CG  . LEU   A 1 216 ? -1.917  -11.181 -47.302 1.00 16.70 ? 218 LEU   A CG  1 
ATOM   1816 C CD1 . LEU   A 1 216 ? -0.650  -10.387 -47.571 1.00 17.71 ? 218 LEU   A CD1 1 
ATOM   1817 C CD2 . LEU   A 1 216 ? -2.335  -11.966 -48.532 1.00 22.73 ? 218 LEU   A CD2 1 
ATOM   1818 N N   . GLY   A 1 217 ? -3.982  -11.331 -44.024 1.00 11.92 ? 219 GLY   A N   1 
ATOM   1819 C CA  . GLY   A 1 217 ? -5.214  -10.631 -43.685 1.00 13.27 ? 219 GLY   A CA  1 
ATOM   1820 C C   . GLY   A 1 217 ? -5.016  -9.599  -42.585 1.00 13.92 ? 219 GLY   A C   1 
ATOM   1821 O O   . GLY   A 1 217 ? -5.616  -8.525  -42.614 1.00 14.58 ? 219 GLY   A O   1 
ATOM   1822 N N   . CYS   A 1 218 ? -4.176  -9.914  -41.595 1.00 11.75 ? 220 CYS   A N   1 
ATOM   1823 C CA  . CYS   A 1 218 ? -3.857  -8.934  -40.563 1.00 11.97 ? 220 CYS   A CA  1 
ATOM   1824 C C   . CYS   A 1 218 ? -3.197  -7.701  -41.158 1.00 15.78 ? 220 CYS   A C   1 
ATOM   1825 O O   . CYS   A 1 218 ? -3.505  -6.572  -40.761 1.00 14.24 ? 220 CYS   A O   1 
ATOM   1826 C CB  . CYS   A 1 218 ? -2.933  -9.547  -39.518 1.00 11.19 ? 220 CYS   A CB  1 
ATOM   1827 S SG  . CYS   A 1 218 ? -3.717  -10.829 -38.527 1.00 13.57 ? 220 CYS   A SG  1 
ATOM   1828 N N   . MET   A 1 219 ? -2.268  -7.899  -42.102 1.00 12.84 ? 221 MET   A N   1 
ATOM   1829 C CA  . MET   A 1 219 ? -1.650  -6.758  -42.768 1.00 16.13 ? 221 MET   A CA  1 
ATOM   1830 C C   . MET   A 1 219 ? -2.693  -5.947  -43.518 1.00 13.78 ? 221 MET   A C   1 
ATOM   1831 O O   . MET   A 1 219 ? -2.728  -4.717  -43.413 1.00 15.06 ? 221 MET   A O   1 
ATOM   1832 C CB  . MET   A 1 219 ? -0.557  -7.232  -43.724 1.00 18.37 ? 221 MET   A CB  1 
ATOM   1833 C CG  . MET   A 1 219 ? 0.598   -7.863  -43.021 1.00 16.71 ? 221 MET   A CG  1 
ATOM   1834 S SD  . MET   A 1 219 ? 1.952   -8.235  -44.156 1.00 20.39 ? 221 MET   A SD  1 
ATOM   1835 C CE  . MET   A 1 219 ? 2.086   -6.691  -45.000 1.00 16.97 ? 221 MET   A CE  1 
ATOM   1836 N N   . LEU   A 1 220 ? -3.548  -6.626  -44.285 1.00 13.79 ? 222 LEU   A N   1 
ATOM   1837 C CA  . LEU   A 1 220 ? -4.567  -5.926  -45.065 1.00 15.08 ? 222 LEU   A CA  1 
ATOM   1838 C C   . LEU   A 1 220 ? -5.475  -5.098  -44.159 1.00 14.47 ? 222 LEU   A C   1 
ATOM   1839 O O   . LEU   A 1 220 ? -5.760  -3.928  -44.445 1.00 16.93 ? 222 LEU   A O   1 
ATOM   1840 C CB  . LEU   A 1 220 ? -5.385  -6.929  -45.884 1.00 17.77 ? 222 LEU   A CB  1 
ATOM   1841 C CG  . LEU   A 1 220 ? -6.519  -6.343  -46.728 1.00 17.37 ? 222 LEU   A CG  1 
ATOM   1842 C CD1 . LEU   A 1 220 ? -5.920  -5.485  -47.842 1.00 18.37 ? 222 LEU   A CD1 1 
ATOM   1843 C CD2 . LEU   A 1 220 ? -7.394  -7.459  -47.289 1.00 20.25 ? 222 LEU   A CD2 1 
ATOM   1844 N N   . ALA   A 1 221 ? -5.934  -5.694  -43.059 1.00 12.98 ? 223 ALA   A N   1 
ATOM   1845 C CA  . ALA   A 1 221 ? -6.820  -4.980  -42.145 1.00 13.93 ? 223 ALA   A CA  1 
ATOM   1846 C C   . ALA   A 1 221 ? -6.158  -3.716  -41.631 1.00 15.22 ? 223 ALA   A C   1 
ATOM   1847 O O   . ALA   A 1 221 ? -6.788  -2.654  -41.565 1.00 15.19 ? 223 ALA   A O   1 
ATOM   1848 C CB  . ALA   A 1 221 ? -7.212  -5.882  -40.983 1.00 15.62 ? 223 ALA   A CB  1 
ATOM   1849 N N   . SER   A 1 222 ? -4.875  -3.809  -41.278 1.00 16.12 ? 224 SER   A N   1 
ATOM   1850 C CA  A SER   A 1 222 ? -4.176  -2.636  -40.768 0.81 18.44 ? 224 SER   A CA  1 
ATOM   1851 C CA  B SER   A 1 222 ? -4.168  -2.638  -40.772 0.19 17.40 ? 224 SER   A CA  1 
ATOM   1852 C C   . SER   A 1 222 ? -4.051  -1.551  -41.829 1.00 17.55 ? 224 SER   A C   1 
ATOM   1853 O O   . SER   A 1 222 ? -4.105  -0.360  -41.499 1.00 19.17 ? 224 SER   A O   1 
ATOM   1854 C CB  A SER   A 1 222 ? -2.796  -3.036  -40.232 0.81 15.25 ? 224 SER   A CB  1 
ATOM   1855 C CB  B SER   A 1 222 ? -2.780  -3.035  -40.269 0.19 17.41 ? 224 SER   A CB  1 
ATOM   1856 O OG  A SER   A 1 222 ? -1.876  -3.369  -41.268 0.81 16.62 ? 224 SER   A OG  1 
ATOM   1857 O OG  B SER   A 1 222 ? -2.867  -3.793  -39.077 0.19 22.27 ? 224 SER   A OG  1 
ATOM   1858 N N   . MET   A 1 223 ? -3.904  -1.934  -43.097 1.00 16.92 ? 225 MET   A N   1 
ATOM   1859 C CA  . MET   A 1 223 ? -3.730  -0.940  -44.152 1.00 19.43 ? 225 MET   A CA  1 
ATOM   1860 C C   . MET   A 1 223 ? -5.049  -0.274  -44.527 1.00 18.97 ? 225 MET   A C   1 
ATOM   1861 O O   . MET   A 1 223 ? -5.122  0.959   -44.599 1.00 21.75 ? 225 MET   A O   1 
ATOM   1862 C CB  . MET   A 1 223 ? -3.074  -1.578  -45.374 1.00 22.13 ? 225 MET   A CB  1 
ATOM   1863 C CG  . MET   A 1 223 ? -1.690  -2.132  -45.065 1.00 25.07 ? 225 MET   A CG  1 
ATOM   1864 S SD  . MET   A 1 223 ? -0.882  -3.002  -46.426 1.00 43.23 ? 225 MET   A SD  1 
ATOM   1865 C CE  . MET   A 1 223 ? -2.144  -4.144  -46.971 1.00 47.19 ? 225 MET   A CE  1 
ATOM   1866 N N   . ILE   A 1 224 ? -6.105  -1.058  -44.753 1.00 18.59 ? 226 ILE   A N   1 
ATOM   1867 C CA  . ILE   A 1 224 ? -7.339  -0.425  -45.221 1.00 19.39 ? 226 ILE   A CA  1 
ATOM   1868 C C   . ILE   A 1 224 ? -8.057  0.304   -44.087 1.00 18.08 ? 226 ILE   A C   1 
ATOM   1869 O O   . ILE   A 1 224 ? -8.758  1.290   -44.342 1.00 19.52 ? 226 ILE   A O   1 
ATOM   1870 C CB  . ILE   A 1 224 ? -8.279  -1.428  -45.915 1.00 18.09 ? 226 ILE   A CB  1 
ATOM   1871 C CG1 . ILE   A 1 224 ? -8.858  -2.434  -44.920 1.00 17.56 ? 226 ILE   A CG1 1 
ATOM   1872 C CG2 . ILE   A 1 224 ? -7.583  -2.115  -47.086 1.00 23.58 ? 226 ILE   A CG2 1 
ATOM   1873 C CD1 . ILE   A 1 224 ? -9.869  -3.388  -45.548 1.00 21.29 ? 226 ILE   A CD1 1 
ATOM   1874 N N   . PHE   A 1 225 ? -7.874  -0.116  -42.829 1.00 17.24 ? 227 PHE   A N   1 
ATOM   1875 C CA  . PHE   A 1 225 ? -8.546  0.552   -41.716 1.00 16.80 ? 227 PHE   A CA  1 
ATOM   1876 C C   . PHE   A 1 225 ? -7.666  1.577   -41.016 1.00 18.19 ? 227 PHE   A C   1 
ATOM   1877 O O   . PHE   A 1 225 ? -8.157  2.294   -40.137 1.00 21.36 ? 227 PHE   A O   1 
ATOM   1878 C CB  . PHE   A 1 225 ? -9.036  -0.468  -40.676 1.00 16.79 ? 227 PHE   A CB  1 
ATOM   1879 C CG  . PHE   A 1 225 ? -10.117 -1.388  -41.176 1.00 16.25 ? 227 PHE   A CG  1 
ATOM   1880 C CD1 . PHE   A 1 225 ? -11.199 -0.892  -41.888 1.00 15.65 ? 227 PHE   A CD1 1 
ATOM   1881 C CD2 . PHE   A 1 225 ? -10.052 -2.748  -40.925 1.00 16.10 ? 227 PHE   A CD2 1 
ATOM   1882 C CE1 . PHE   A 1 225 ? -12.209 -1.738  -42.348 1.00 18.26 ? 227 PHE   A CE1 1 
ATOM   1883 C CE2 . PHE   A 1 225 ? -11.056 -3.604  -41.386 1.00 16.56 ? 227 PHE   A CE2 1 
ATOM   1884 C CZ  . PHE   A 1 225 ? -12.134 -3.091  -42.104 1.00 17.58 ? 227 PHE   A CZ  1 
ATOM   1885 N N   . ARG   A 1 226 ? -6.386  1.655   -41.371 1.00 19.89 ? 228 ARG   A N   1 
ATOM   1886 C CA  . ARG   A 1 226 ? -5.468  2.619   -40.766 1.00 23.20 ? 228 ARG   A CA  1 
ATOM   1887 C C   . ARG   A 1 226 ? -5.360  2.395   -39.262 1.00 25.60 ? 228 ARG   A C   1 
ATOM   1888 O O   . ARG   A 1 226 ? -5.545  3.306   -38.453 1.00 25.91 ? 228 ARG   A O   1 
ATOM   1889 C CB  . ARG   A 1 226 ? -5.901  4.054   -41.072 1.00 27.17 ? 228 ARG   A CB  1 
ATOM   1890 C CG  . ARG   A 1 226 ? -6.128  4.311   -42.527 1.00 32.97 ? 228 ARG   A CG  1 
ATOM   1891 C CD  . ARG   A 1 226 ? -4.852  4.130   -43.289 1.00 45.76 ? 228 ARG   A CD  1 
ATOM   1892 N NE  . ARG   A 1 226 ? -3.737  4.815   -42.654 1.00 62.12 ? 228 ARG   A NE  1 
ATOM   1893 C CZ  . ARG   A 1 226 ? -3.562  6.132   -42.660 1.00 71.48 ? 228 ARG   A CZ  1 
ATOM   1894 N NH1 . ARG   A 1 226 ? -2.508  6.652   -42.049 1.00 72.80 ? 228 ARG   A NH1 1 
ATOM   1895 N NH2 . ARG   A 1 226 ? -4.439  6.929   -43.263 1.00 74.89 ? 228 ARG   A NH2 1 
ATOM   1896 N N   . LYS   A 1 227 ? -5.078  1.152   -38.888 1.00 20.89 ? 229 LYS   A N   1 
ATOM   1897 C CA  . LYS   A 1 227 ? -4.897  0.774   -37.492 1.00 22.60 ? 229 LYS   A CA  1 
ATOM   1898 C C   . LYS   A 1 227 ? -3.805  -0.288  -37.471 1.00 21.22 ? 229 LYS   A C   1 
ATOM   1899 O O   . LYS   A 1 227 ? -4.053  -1.441  -37.826 1.00 21.35 ? 229 LYS   A O   1 
ATOM   1900 C CB  . LYS   A 1 227 ? -6.186  0.259   -36.867 1.00 23.65 ? 229 LYS   A CB  1 
ATOM   1901 C CG  . LYS   A 1 227 ? -5.998  -0.099  -35.406 1.00 23.85 ? 229 LYS   A CG  1 
ATOM   1902 C CD  . LYS   A 1 227 ? -7.237  -0.701  -34.792 1.00 27.38 ? 229 LYS   A CD  1 
ATOM   1903 C CE  . LYS   A 1 227 ? -7.056  -0.849  -33.291 1.00 28.84 ? 229 LYS   A CE  1 
ATOM   1904 N NZ  . LYS   A 1 227 ? -5.966  -1.793  -32.935 1.00 27.26 ? 229 LYS   A NZ  1 
ATOM   1905 N N   . GLU   A 1 228 ? -2.600  0.102   -37.073 1.00 25.34 ? 230 GLU   A N   1 
ATOM   1906 C CA  . GLU   A 1 228 ? -1.448  -0.785  -37.178 1.00 23.74 ? 230 GLU   A CA  1 
ATOM   1907 C C   . GLU   A 1 228 ? -0.822  -0.978  -35.806 1.00 23.71 ? 230 GLU   A C   1 
ATOM   1908 O O   . GLU   A 1 228 ? -0.389  0.007   -35.186 1.00 27.50 ? 230 GLU   A O   1 
ATOM   1909 C CB  . GLU   A 1 228 ? -0.412  -0.234  -38.166 1.00 30.75 ? 230 GLU   A CB  1 
ATOM   1910 C CG  . GLU   A 1 228 ? 0.453   -1.310  -38.846 1.00 32.58 ? 230 GLU   A CG  1 
ATOM   1911 C CD  . GLU   A 1 228 ? 1.462   -1.966  -37.908 1.00 37.08 ? 230 GLU   A CD  1 
ATOM   1912 O OE1 . GLU   A 1 228 ? 1.999   -1.267  -37.019 1.00 36.59 ? 230 GLU   A OE1 1 
ATOM   1913 O OE2 . GLU   A 1 228 ? 1.716   -3.182  -38.061 1.00 27.84 ? 230 GLU   A OE2 1 
ATOM   1914 N N   . PRO   A 1 229 ? -0.761  -2.205  -35.280 1.00 21.83 ? 231 PRO   A N   1 
ATOM   1915 C CA  . PRO   A 1 229 ? -1.364  -3.404  -35.871 1.00 17.54 ? 231 PRO   A CA  1 
ATOM   1916 C C   . PRO   A 1 229 ? -2.870  -3.439  -35.631 1.00 20.70 ? 231 PRO   A C   1 
ATOM   1917 O O   . PRO   A 1 229 ? -3.397  -2.703  -34.792 1.00 21.37 ? 231 PRO   A O   1 
ATOM   1918 C CB  . PRO   A 1 229 ? -0.668  -4.539  -35.121 1.00 19.63 ? 231 PRO   A CB  1 
ATOM   1919 C CG  . PRO   A 1 229 ? -0.451  -3.968  -33.767 1.00 25.75 ? 231 PRO   A CG  1 
ATOM   1920 C CD  . PRO   A 1 229 ? -0.089  -2.511  -34.005 1.00 26.53 ? 231 PRO   A CD  1 
ATOM   1921 N N   . PHE   A 1 230 ? -3.563  -4.299  -36.372 1.00 15.12 ? 232 PHE   A N   1 
ATOM   1922 C CA  . PHE   A 1 230 ? -5.013  -4.353  -36.235 1.00 14.30 ? 232 PHE   A CA  1 
ATOM   1923 C C   . PHE   A 1 230 ? -5.395  -5.052  -34.932 1.00 17.98 ? 232 PHE   A C   1 
ATOM   1924 O O   . PHE   A 1 230 ? -6.091  -4.469  -34.092 1.00 18.88 ? 232 PHE   A O   1 
ATOM   1925 C CB  . PHE   A 1 230 ? -5.634  -5.038  -37.447 1.00 15.04 ? 232 PHE   A CB  1 
ATOM   1926 C CG  . PHE   A 1 230 ? -7.125  -4.959  -37.457 1.00 15.52 ? 232 PHE   A CG  1 
ATOM   1927 C CD1 . PHE   A 1 230 ? -7.748  -3.748  -37.671 1.00 15.57 ? 232 PHE   A CD1 1 
ATOM   1928 C CD2 . PHE   A 1 230 ? -7.893  -6.079  -37.221 1.00 16.19 ? 232 PHE   A CD2 1 
ATOM   1929 C CE1 . PHE   A 1 230 ? -9.123  -3.646  -37.667 1.00 16.35 ? 232 PHE   A CE1 1 
ATOM   1930 C CE2 . PHE   A 1 230 ? -9.283  -5.989  -37.215 1.00 20.48 ? 232 PHE   A CE2 1 
ATOM   1931 C CZ  . PHE   A 1 230 ? -9.892  -4.766  -37.442 1.00 19.93 ? 232 PHE   A CZ  1 
ATOM   1932 N N   . PHE   A 1 231 ? -4.967  -6.301  -34.755 1.00 15.01 ? 233 PHE   A N   1 
ATOM   1933 C CA  . PHE   A 1 231 ? -5.188  -7.055  -33.518 1.00 14.79 ? 233 PHE   A CA  1 
ATOM   1934 C C   . PHE   A 1 231 ? -4.001  -6.814  -32.594 1.00 18.02 ? 233 PHE   A C   1 
ATOM   1935 O O   . PHE   A 1 231 ? -2.936  -7.402  -32.783 1.00 17.08 ? 233 PHE   A O   1 
ATOM   1936 C CB  . PHE   A 1 231 ? -5.324  -8.541  -33.820 1.00 14.95 ? 233 PHE   A CB  1 
ATOM   1937 C CG  . PHE   A 1 231 ? -6.487  -8.908  -34.722 1.00 12.76 ? 233 PHE   A CG  1 
ATOM   1938 C CD1 . PHE   A 1 231 ? -7.806  -8.739  -34.306 1.00 15.58 ? 233 PHE   A CD1 1 
ATOM   1939 C CD2 . PHE   A 1 231 ? -6.252  -9.503  -35.957 1.00 15.28 ? 233 PHE   A CD2 1 
ATOM   1940 C CE1 . PHE   A 1 231 ? -8.863  -9.124  -35.134 1.00 14.66 ? 233 PHE   A CE1 1 
ATOM   1941 C CE2 . PHE   A 1 231 ? -7.290  -9.883  -36.793 1.00 13.51 ? 233 PHE   A CE2 1 
ATOM   1942 C CZ  . PHE   A 1 231 ? -8.613  -9.699  -36.373 1.00 17.77 ? 233 PHE   A CZ  1 
ATOM   1943 N N   . HIS   A 1 232 ? -4.171  -5.952  -31.596 1.00 17.56 ? 234 HIS   A N   1 
ATOM   1944 C CA  . HIS   A 1 232 ? -3.053  -5.400  -30.838 1.00 18.20 ? 234 HIS   A CA  1 
ATOM   1945 C C   . HIS   A 1 232 ? -3.039  -6.002  -29.436 1.00 19.55 ? 234 HIS   A C   1 
ATOM   1946 O O   . HIS   A 1 232 ? -3.359  -5.342  -28.444 1.00 22.78 ? 234 HIS   A O   1 
ATOM   1947 C CB  . HIS   A 1 232 ? -3.161  -3.876  -30.810 1.00 21.80 ? 234 HIS   A CB  1 
ATOM   1948 C CG  . HIS   A 1 232 ? -1.881  -3.178  -30.465 1.00 25.97 ? 234 HIS   A CG  1 
ATOM   1949 N ND1 . HIS   A 1 232 ? -1.641  -1.860  -30.795 1.00 29.98 ? 234 HIS   A ND1 1 
ATOM   1950 C CD2 . HIS   A 1 232 ? -0.771  -3.612  -29.823 1.00 32.82 ? 234 HIS   A CD2 1 
ATOM   1951 C CE1 . HIS   A 1 232 ? -0.440  -1.513  -30.370 1.00 32.20 ? 234 HIS   A CE1 1 
ATOM   1952 N NE2 . HIS   A 1 232 ? 0.110   -2.558  -29.777 1.00 31.66 ? 234 HIS   A NE2 1 
ATOM   1953 N N   . GLY   A 1 233 ? -2.640  -7.272  -29.359 1.00 16.91 ? 235 GLY   A N   1 
ATOM   1954 C CA  . GLY   A 1 233 ? -2.624  -7.971  -28.082 1.00 17.22 ? 235 GLY   A CA  1 
ATOM   1955 C C   . GLY   A 1 233 ? -1.415  -7.630  -27.223 1.00 18.30 ? 235 GLY   A C   1 
ATOM   1956 O O   . GLY   A 1 233 ? -0.322  -7.343  -27.719 1.00 20.61 ? 235 GLY   A O   1 
ATOM   1957 N N   . HIS   A 1 234 ? -1.623  -7.680  -25.899 1.00 22.65 ? 236 HIS   A N   1 
ATOM   1958 C CA  . HIS   A 1 234 ? -0.549  -7.439  -24.932 1.00 22.27 ? 236 HIS   A CA  1 
ATOM   1959 C C   . HIS   A 1 234 ? 0.350   -8.649  -24.734 1.00 22.26 ? 236 HIS   A C   1 
ATOM   1960 O O   . HIS   A 1 234 ? 1.488   -8.502  -24.256 1.00 26.10 ? 236 HIS   A O   1 
ATOM   1961 C CB  . HIS   A 1 234 ? -1.131  -7.046  -23.569 1.00 28.51 ? 236 HIS   A CB  1 
ATOM   1962 C CG  . HIS   A 1 234 ? -2.065  -5.877  -23.618 1.00 50.85 ? 236 HIS   A CG  1 
ATOM   1963 N ND1 . HIS   A 1 234 ? -3.295  -5.883  -22.996 1.00 57.47 ? 236 HIS   A ND1 1 
ATOM   1964 C CD2 . HIS   A 1 234 ? -1.947  -4.662  -24.205 1.00 58.23 ? 236 HIS   A CD2 1 
ATOM   1965 C CE1 . HIS   A 1 234 ? -3.897  -4.725  -23.202 1.00 60.12 ? 236 HIS   A CE1 1 
ATOM   1966 N NE2 . HIS   A 1 234 ? -3.100  -3.966  -23.933 1.00 56.50 ? 236 HIS   A NE2 1 
ATOM   1967 N N   . ASP   A 1 235 ? -0.147  -9.838  -25.048 1.00 17.70 ? 237 ASP   A N   1 
ATOM   1968 C CA  . ASP   A 1 235 ? 0.593   -11.087 -24.959 1.00 17.90 ? 237 ASP   A CA  1 
ATOM   1969 C C   . ASP   A 1 235 ? -0.159  -12.075 -25.840 1.00 17.72 ? 237 ASP   A C   1 
ATOM   1970 O O   . ASP   A 1 235 ? -1.128  -11.700 -26.507 1.00 17.31 ? 237 ASP   A O   1 
ATOM   1971 C CB  . ASP   A 1 235 ? 0.753   -11.561 -23.503 1.00 19.18 ? 237 ASP   A CB  1 
ATOM   1972 C CG  . ASP   A 1 235 ? -0.576  -11.779 -22.792 1.00 28.23 ? 237 ASP   A CG  1 
ATOM   1973 O OD1 . ASP   A 1 235 ? -1.541  -12.270 -23.413 1.00 22.48 ? 237 ASP   A OD1 1 
ATOM   1974 O OD2 . ASP   A 1 235 ? -0.647  -11.491 -21.580 1.00 32.97 ? 237 ASP   A OD2 1 
ATOM   1975 N N   . ASN   A 1 236 ? 0.268   -13.338 -25.842 1.00 18.81 ? 238 ASN   A N   1 
ATOM   1976 C CA  . ASN   A 1 236 ? -0.327  -14.290 -26.777 1.00 18.31 ? 238 ASN   A CA  1 
ATOM   1977 C C   . ASN   A 1 236 ? -1.740  -14.690 -26.373 1.00 17.69 ? 238 ASN   A C   1 
ATOM   1978 O O   . ASN   A 1 236 ? -2.535  -15.075 -27.237 1.00 19.08 ? 238 ASN   A O   1 
ATOM   1979 C CB  . ASN   A 1 236 ? 0.557   -15.532 -26.905 1.00 20.52 ? 238 ASN   A CB  1 
ATOM   1980 C CG  . ASN   A 1 236 ? 1.859   -15.249 -27.659 1.00 21.95 ? 238 ASN   A CG  1 
ATOM   1981 O OD1 . ASN   A 1 236 ? 1.976   -14.253 -28.373 1.00 23.26 ? 238 ASN   A OD1 1 
ATOM   1982 N ND2 . ASN   A 1 236 ? 2.849   -16.125 -27.483 1.00 26.88 ? 238 ASN   A ND2 1 
ATOM   1983 N N   . TYR   A 1 237 ? -2.080  -14.599 -25.089 1.00 17.46 ? 239 TYR   A N   1 
ATOM   1984 C CA  . TYR   A 1 237 ? -3.442  -14.899 -24.666 1.00 16.79 ? 239 TYR   A CA  1 
ATOM   1985 C C   . TYR   A 1 237 ? -4.376  -13.749 -25.015 1.00 16.70 ? 239 TYR   A C   1 
ATOM   1986 O O   . TYR   A 1 237 ? -5.443  -13.948 -25.615 1.00 14.91 ? 239 TYR   A O   1 
ATOM   1987 C CB  . TYR   A 1 237 ? -3.446  -15.202 -23.165 1.00 19.38 ? 239 TYR   A CB  1 
ATOM   1988 C CG  . TYR   A 1 237 ? -2.369  -16.212 -22.840 1.00 25.66 ? 239 TYR   A CG  1 
ATOM   1989 C CD1 . TYR   A 1 237 ? -1.222  -15.843 -22.155 1.00 26.21 ? 239 TYR   A CD1 1 
ATOM   1990 C CD2 . TYR   A 1 237 ? -2.476  -17.521 -23.285 1.00 31.08 ? 239 TYR   A CD2 1 
ATOM   1991 C CE1 . TYR   A 1 237 ? -0.226  -16.770 -21.888 1.00 32.32 ? 239 TYR   A CE1 1 
ATOM   1992 C CE2 . TYR   A 1 237 ? -1.493  -18.448 -23.028 1.00 37.08 ? 239 TYR   A CE2 1 
ATOM   1993 C CZ  . TYR   A 1 237 ? -0.368  -18.069 -22.338 1.00 35.39 ? 239 TYR   A CZ  1 
ATOM   1994 O OH  . TYR   A 1 237 ? 0.608   -19.005 -22.078 1.00 38.27 ? 239 TYR   A OH  1 
ATOM   1995 N N   . ASP   A 1 238 ? -3.965  -12.528 -24.688 1.00 16.52 ? 240 ASP   A N   1 
ATOM   1996 C CA  . ASP   A 1 238 ? -4.764  -11.366 -25.057 1.00 15.14 ? 240 ASP   A CA  1 
ATOM   1997 C C   . ASP   A 1 238 ? -4.894  -11.239 -26.572 1.00 14.05 ? 240 ASP   A C   1 
ATOM   1998 O O   . ASP   A 1 238 ? -5.901  -10.735 -27.069 1.00 14.82 ? 240 ASP   A O   1 
ATOM   1999 C CB  . ASP   A 1 238 ? -4.152  -10.099 -24.454 1.00 16.78 ? 240 ASP   A CB  1 
ATOM   2000 C CG  . ASP   A 1 238 ? -4.991  -8.868  -24.721 1.00 20.45 ? 240 ASP   A CG  1 
ATOM   2001 O OD1 . ASP   A 1 238 ? -6.167  -8.847  -24.299 1.00 21.43 ? 240 ASP   A OD1 1 
ATOM   2002 O OD2 . ASP   A 1 238 ? -4.488  -7.923  -25.360 1.00 19.95 ? 240 ASP   A OD2 1 
ATOM   2003 N N   . GLN   A 1 239 ? -3.898  -11.709 -27.324 1.00 15.00 ? 241 GLN   A N   1 
ATOM   2004 C CA  . GLN   A 1 239 ? -3.998  -11.681 -28.777 1.00 14.81 ? 241 GLN   A CA  1 
ATOM   2005 C C   . GLN   A 1 239 ? -5.223  -12.454 -29.256 1.00 12.72 ? 241 GLN   A C   1 
ATOM   2006 O O   . GLN   A 1 239 ? -5.965  -11.984 -30.126 1.00 13.20 ? 241 GLN   A O   1 
ATOM   2007 C CB  . GLN   A 1 239 ? -2.724  -12.256 -29.390 1.00 11.62 ? 241 GLN   A CB  1 
ATOM   2008 C CG  . GLN   A 1 239 ? -2.632  -12.122 -30.900 1.00 12.91 ? 241 GLN   A CG  1 
ATOM   2009 C CD  . GLN   A 1 239 ? -2.564  -10.678 -31.371 1.00 12.17 ? 241 GLN   A CD  1 
ATOM   2010 O OE1 . GLN   A 1 239 ? -2.082  -9.798  -30.657 1.00 15.23 ? 241 GLN   A OE1 1 
ATOM   2011 N NE2 . GLN   A 1 239 ? -3.024  -10.433 -32.590 1.00 12.97 ? 241 GLN   A NE2 1 
ATOM   2012 N N   . LEU   A 1 240 ? -5.449  -13.645 -28.697 1.00 12.99 ? 242 LEU   A N   1 
ATOM   2013 C CA  . LEU   A 1 240 ? -6.622  -14.411 -29.103 1.00 11.00 ? 242 LEU   A CA  1 
ATOM   2014 C C   . LEU   A 1 240 ? -7.905  -13.728 -28.642 1.00 13.52 ? 242 LEU   A C   1 
ATOM   2015 O O   . LEU   A 1 240 ? -8.900  -13.725 -29.372 1.00 13.40 ? 242 LEU   A O   1 
ATOM   2016 C CB  . LEU   A 1 240 ? -6.533  -15.845 -28.572 1.00 12.96 ? 242 LEU   A CB  1 
ATOM   2017 C CG  . LEU   A 1 240 ? -7.673  -16.767 -29.005 1.00 13.46 ? 242 LEU   A CG  1 
ATOM   2018 C CD1 . LEU   A 1 240 ? -7.751  -16.863 -30.539 1.00 14.15 ? 242 LEU   A CD1 1 
ATOM   2019 C CD2 . LEU   A 1 240 ? -7.516  -18.138 -28.372 1.00 14.96 ? 242 LEU   A CD2 1 
ATOM   2020 N N   . VAL   A 1 241 ? -7.896  -13.118 -27.451 1.00 13.21 ? 243 VAL   A N   1 
ATOM   2021 C CA  . VAL   A 1 241 ? -9.077  -12.368 -27.009 1.00 13.37 ? 243 VAL   A CA  1 
ATOM   2022 C C   . VAL   A 1 241 ? -9.385  -11.221 -27.971 1.00 14.02 ? 243 VAL   A C   1 
ATOM   2023 O O   . VAL   A 1 241 ? -10.550 -10.987 -28.313 1.00 14.45 ? 243 VAL   A O   1 
ATOM   2024 C CB  . VAL   A 1 241 ? -8.897  -11.863 -25.567 1.00 16.33 ? 243 VAL   A CB  1 
ATOM   2025 C CG1 . VAL   A 1 241 ? -10.124 -11.027 -25.155 1.00 17.50 ? 243 VAL   A CG1 1 
ATOM   2026 C CG2 . VAL   A 1 241 ? -8.714  -13.039 -24.610 1.00 16.57 ? 243 VAL   A CG2 1 
ATOM   2027 N N   . ARG   A 1 242 ? -8.357  -10.490 -28.423 1.00 14.01 ? 244 ARG   A N   1 
ATOM   2028 C CA  . ARG   A 1 242 ? -8.590  -9.397  -29.373 1.00 13.96 ? 244 ARG   A CA  1 
ATOM   2029 C C   . ARG   A 1 242 ? -9.212  -9.915  -30.659 1.00 12.29 ? 244 ARG   A C   1 
ATOM   2030 O O   . ARG   A 1 242 ? -10.098 -9.269  -31.237 1.00 15.27 ? 244 ARG   A O   1 
ATOM   2031 C CB  . ARG   A 1 242 ? -7.284  -8.675  -29.719 1.00 16.49 ? 244 ARG   A CB  1 
ATOM   2032 C CG  . ARG   A 1 242 ? -6.489  -8.096  -28.568 1.00 23.99 ? 244 ARG   A CG  1 
ATOM   2033 C CD  . ARG   A 1 242 ? -7.278  -7.035  -27.845 1.00 26.07 ? 244 ARG   A CD  1 
ATOM   2034 N NE  . ARG   A 1 242 ? -6.478  -6.354  -26.824 1.00 31.83 ? 244 ARG   A NE  1 
ATOM   2035 C CZ  . ARG   A 1 242 ? -6.172  -5.060  -26.851 1.00 42.23 ? 244 ARG   A CZ  1 
ATOM   2036 N NH1 . ARG   A 1 242 ? -6.592  -4.292  -27.848 1.00 42.12 ? 244 ARG   A NH1 1 
ATOM   2037 N NH2 . ARG   A 1 242 ? -5.450  -4.528  -25.875 1.00 44.00 ? 244 ARG   A NH2 1 
ATOM   2038 N N   . ILE   A 1 243 ? -8.739  -11.063 -31.145 1.00 12.35 ? 245 ILE   A N   1 
ATOM   2039 C CA  . ILE   A 1 243 ? -9.335  -11.661 -32.334 1.00 13.65 ? 245 ILE   A CA  1 
ATOM   2040 C C   . ILE   A 1 243 ? -10.779 -12.043 -32.069 1.00 13.36 ? 245 ILE   A C   1 
ATOM   2041 O O   . ILE   A 1 243 ? -11.662 -11.807 -32.902 1.00 14.18 ? 245 ILE   A O   1 
ATOM   2042 C CB  . ILE   A 1 243 ? -8.513  -12.876 -32.793 1.00 11.81 ? 245 ILE   A CB  1 
ATOM   2043 C CG1 . ILE   A 1 243 ? -7.131  -12.408 -33.242 1.00 12.39 ? 245 ILE   A CG1 1 
ATOM   2044 C CG2 . ILE   A 1 243 ? -9.257  -13.586 -33.927 1.00 13.40 ? 245 ILE   A CG2 1 
ATOM   2045 C CD1 . ILE   A 1 243 ? -6.123  -13.548 -33.450 1.00 13.05 ? 245 ILE   A CD1 1 
ATOM   2046 N N   . ALA   A 1 244 ? -11.039 -12.640 -30.907 1.00 12.02 ? 246 ALA   A N   1 
ATOM   2047 C CA  . ALA   A 1 244 ? -12.391 -13.093 -30.591 1.00 12.58 ? 246 ALA   A CA  1 
ATOM   2048 C C   . ALA   A 1 244 ? -13.376 -11.946 -30.411 1.00 14.43 ? 246 ALA   A C   1 
ATOM   2049 O O   . ALA   A 1 244 ? -14.576 -12.141 -30.616 1.00 15.07 ? 246 ALA   A O   1 
ATOM   2050 C CB  . ALA   A 1 244 ? -12.367 -13.957 -29.341 1.00 12.36 ? 246 ALA   A CB  1 
ATOM   2051 N N   . LYS   A 1 245 ? -12.908 -10.758 -30.030 1.00 12.56 ? 247 LYS   A N   1 
ATOM   2052 C CA  . LYS   A 1 245 ? -13.814 -9.619  -29.964 1.00 13.48 ? 247 LYS   A CA  1 
ATOM   2053 C C   . LYS   A 1 245 ? -14.273 -9.155  -31.338 1.00 15.02 ? 247 LYS   A C   1 
ATOM   2054 O O   . LYS   A 1 245 ? -15.258 -8.408  -31.424 1.00 17.95 ? 247 LYS   A O   1 
ATOM   2055 C CB  . LYS   A 1 245 ? -13.152 -8.475  -29.203 1.00 15.11 ? 247 LYS   A CB  1 
ATOM   2056 C CG  . LYS   A 1 245 ? -13.015 -8.739  -27.725 1.00 16.40 ? 247 LYS   A CG  1 
ATOM   2057 C CD  . LYS   A 1 245 ? -12.369 -7.551  -27.034 1.00 20.99 ? 247 LYS   A CD  1 
ATOM   2058 C CE  . LYS   A 1 245 ? -12.263 -7.781  -25.543 1.00 27.93 ? 247 LYS   A CE  1 
ATOM   2059 N NZ  . LYS   A 1 245 ? -11.536 -6.655  -24.881 1.00 42.35 ? 247 LYS   A NZ  1 
ATOM   2060 N N   . VAL   A 1 246 ? -13.627 -9.598  -32.412 1.00 12.80 ? 248 VAL   A N   1 
ATOM   2061 C CA  . VAL   A 1 246 ? -14.007 -9.242  -33.773 1.00 14.51 ? 248 VAL   A CA  1 
ATOM   2062 C C   . VAL   A 1 246 ? -14.702 -10.404 -34.475 1.00 14.01 ? 248 VAL   A C   1 
ATOM   2063 O O   . VAL   A 1 246 ? -15.794 -10.247 -35.029 1.00 15.23 ? 248 VAL   A O   1 
ATOM   2064 C CB  . VAL   A 1 246 ? -12.771 -8.768  -34.574 1.00 12.34 ? 248 VAL   A CB  1 
ATOM   2065 C CG1 . VAL   A 1 246 ? -13.182 -8.438  -35.998 1.00 13.85 ? 248 VAL   A CG1 1 
ATOM   2066 C CG2 . VAL   A 1 246 ? -12.133 -7.561  -33.914 1.00 15.65 ? 248 VAL   A CG2 1 
ATOM   2067 N N   . LEU   A 1 247 ? -14.086 -11.585 -34.449 1.00 12.06 ? 249 LEU   A N   1 
ATOM   2068 C CA  A LEU   A 1 247 ? -14.657 -12.756 -35.095 0.62 11.79 ? 249 LEU   A CA  1 
ATOM   2069 C CA  B LEU   A 1 247 ? -14.645 -12.765 -35.089 0.38 11.95 ? 249 LEU   A CA  1 
ATOM   2070 C C   . LEU   A 1 247 ? -15.677 -13.476 -34.224 1.00 14.32 ? 249 LEU   A C   1 
ATOM   2071 O O   . LEU   A 1 247 ? -16.414 -14.320 -34.743 1.00 14.28 ? 249 LEU   A O   1 
ATOM   2072 C CB  A LEU   A 1 247 ? -13.554 -13.735 -35.499 0.62 12.28 ? 249 LEU   A CB  1 
ATOM   2073 C CB  B LEU   A 1 247 ? -13.529 -13.743 -35.451 0.38 12.47 ? 249 LEU   A CB  1 
ATOM   2074 C CG  A LEU   A 1 247 ? -12.830 -13.488 -36.829 0.62 11.50 ? 249 LEU   A CG  1 
ATOM   2075 C CG  B LEU   A 1 247 ? -12.462 -13.272 -36.441 0.38 12.49 ? 249 LEU   A CG  1 
ATOM   2076 C CD1 A LEU   A 1 247 ? -11.991 -12.217 -36.786 0.62 12.58 ? 249 LEU   A CD1 1 
ATOM   2077 C CD1 B LEU   A 1 247 ? -11.516 -14.413 -36.761 0.38 12.18 ? 249 LEU   A CD1 1 
ATOM   2078 C CD2 A LEU   A 1 247 ? -11.962 -14.676 -37.221 0.62 12.76 ? 249 LEU   A CD2 1 
ATOM   2079 C CD2 B LEU   A 1 247 ? -13.126 -12.742 -37.701 0.38 11.40 ? 249 LEU   A CD2 1 
ATOM   2080 N N   . GLY   A 1 248 ? -15.736 -13.161 -32.941 1.00 12.35 ? 250 GLY   A N   1 
ATOM   2081 C CA  . GLY   A 1 248 ? -16.731 -13.731 -32.044 1.00 13.26 ? 250 GLY   A CA  1 
ATOM   2082 C C   . GLY   A 1 248 ? -16.267 -15.018 -31.395 1.00 14.08 ? 250 GLY   A C   1 
ATOM   2083 O O   . GLY   A 1 248 ? -15.445 -15.766 -31.932 1.00 15.35 ? 250 GLY   A O   1 
ATOM   2084 N N   . THR   A 1 249 ? -16.846 -15.303 -30.224 1.00 14.01 ? 251 THR   A N   1 
ATOM   2085 C CA  . THR   A 1 249 ? -16.438 -16.493 -29.495 1.00 15.34 ? 251 THR   A CA  1 
ATOM   2086 C C   . THR   A 1 249 ? -17.133 -17.759 -29.983 1.00 13.17 ? 251 THR   A C   1 
ATOM   2087 O O   . THR   A 1 249 ? -16.561 -18.847 -29.854 1.00 15.37 ? 251 THR   A O   1 
ATOM   2088 C CB  . THR   A 1 249 ? -16.662 -16.311 -27.998 1.00 15.08 ? 251 THR   A CB  1 
ATOM   2089 O OG1 . THR   A 1 249 ? -17.966 -15.765 -27.769 1.00 15.54 ? 251 THR   A OG1 1 
ATOM   2090 C CG2 . THR   A 1 249 ? -15.601 -15.362 -27.425 1.00 17.39 ? 251 THR   A CG2 1 
ATOM   2091 N N   . GLU   A 1 250 ? -18.352 -17.674 -30.519 1.00 15.55 ? 252 GLU   A N   1 
ATOM   2092 C CA  . GLU   A 1 250 ? -19.014 -18.908 -30.943 1.00 17.05 ? 252 GLU   A CA  1 
ATOM   2093 C C   . GLU   A 1 250 ? -18.257 -19.598 -32.073 1.00 14.82 ? 252 GLU   A C   1 
ATOM   2094 O O   . GLU   A 1 250 ? -18.102 -20.825 -32.068 1.00 16.45 ? 252 GLU   A O   1 
ATOM   2095 C CB  . GLU   A 1 250 ? -20.453 -18.619 -31.355 1.00 14.90 ? 252 GLU   A CB  1 
ATOM   2096 C CG  . GLU   A 1 250 ? -21.305 -18.173 -30.172 1.00 19.62 ? 252 GLU   A CG  1 
ATOM   2097 C CD  . GLU   A 1 250 ? -21.793 -19.336 -29.334 1.00 44.72 ? 252 GLU   A CD  1 
ATOM   2098 O OE1 . GLU   A 1 250 ? -22.933 -19.792 -29.569 1.00 54.61 ? 252 GLU   A OE1 1 
ATOM   2099 O OE2 . GLU   A 1 250 ? -21.038 -19.800 -28.452 1.00 50.35 ? 252 GLU   A OE2 1 
ATOM   2100 N N   . ASP   A 1 251 ? -17.746 -18.832 -33.038 1.00 13.54 ? 253 ASP   A N   1 
ATOM   2101 C CA  . ASP   A 1 251 ? -16.978 -19.454 -34.104 1.00 14.63 ? 253 ASP   A CA  1 
ATOM   2102 C C   . ASP   A 1 251 ? -15.590 -19.891 -33.648 1.00 14.61 ? 253 ASP   A C   1 
ATOM   2103 O O   . ASP   A 1 251 ? -15.031 -20.820 -34.234 1.00 14.24 ? 253 ASP   A O   1 
ATOM   2104 C CB  . ASP   A 1 251 ? -16.896 -18.502 -35.295 1.00 15.46 ? 253 ASP   A CB  1 
ATOM   2105 C CG  . ASP   A 1 251 ? -18.228 -18.346 -35.979 1.00 19.31 ? 253 ASP   A CG  1 
ATOM   2106 O OD1 . ASP   A 1 251 ? -18.930 -19.365 -36.108 1.00 20.70 ? 253 ASP   A OD1 1 
ATOM   2107 O OD2 . ASP   A 1 251 ? -18.592 -17.221 -36.348 1.00 21.40 ? 253 ASP   A OD2 1 
ATOM   2108 N N   . LEU   A 1 252 ? -15.046 -19.276 -32.595 1.00 12.85 ? 254 LEU   A N   1 
ATOM   2109 C CA  . LEU   A 1 252 ? -13.828 -19.814 -32.004 1.00 15.04 ? 254 LEU   A CA  1 
ATOM   2110 C C   . LEU   A 1 252 ? -14.095 -21.191 -31.413 1.00 14.22 ? 254 LEU   A C   1 
ATOM   2111 O O   . LEU   A 1 252 ? -13.307 -22.129 -31.610 1.00 14.63 ? 254 LEU   A O   1 
ATOM   2112 C CB  . LEU   A 1 252 ? -13.292 -18.854 -30.940 1.00 12.37 ? 254 LEU   A CB  1 
ATOM   2113 C CG  . LEU   A 1 252 ? -12.109 -19.357 -30.118 1.00 13.72 ? 254 LEU   A CG  1 
ATOM   2114 C CD1 . LEU   A 1 252 ? -10.917 -19.732 -31.023 1.00 15.46 ? 254 LEU   A CD1 1 
ATOM   2115 C CD2 . LEU   A 1 252 ? -11.698 -18.297 -29.122 1.00 16.96 ? 254 LEU   A CD2 1 
ATOM   2116 N N   . TYR   A 1 253 ? -15.206 -21.339 -30.691 1.00 14.76 ? 255 TYR   A N   1 
ATOM   2117 C CA  . TYR   A 1 253 ? -15.536 -22.651 -30.148 1.00 13.21 ? 255 TYR   A CA  1 
ATOM   2118 C C   . TYR   A 1 253 ? -15.841 -23.644 -31.260 1.00 13.53 ? 255 TYR   A C   1 
ATOM   2119 O O   . TYR   A 1 253 ? -15.446 -24.809 -31.166 1.00 14.51 ? 255 TYR   A O   1 
ATOM   2120 C CB  . TYR   A 1 253 ? -16.695 -22.545 -29.153 1.00 14.25 ? 255 TYR   A CB  1 
ATOM   2121 C CG  . TYR   A 1 253 ? -16.203 -22.231 -27.762 1.00 16.11 ? 255 TYR   A CG  1 
ATOM   2122 C CD1 . TYR   A 1 253 ? -15.680 -23.237 -26.955 1.00 20.65 ? 255 TYR   A CD1 1 
ATOM   2123 C CD2 . TYR   A 1 253 ? -16.231 -20.935 -27.259 1.00 21.52 ? 255 TYR   A CD2 1 
ATOM   2124 C CE1 . TYR   A 1 253 ? -15.216 -22.967 -25.685 1.00 22.45 ? 255 TYR   A CE1 1 
ATOM   2125 C CE2 . TYR   A 1 253 ? -15.761 -20.658 -25.978 1.00 23.20 ? 255 TYR   A CE2 1 
ATOM   2126 C CZ  . TYR   A 1 253 ? -15.248 -21.681 -25.206 1.00 21.26 ? 255 TYR   A CZ  1 
ATOM   2127 O OH  . TYR   A 1 253 ? -14.789 -21.432 -23.926 1.00 32.73 ? 255 TYR   A OH  1 
ATOM   2128 N N   . ASP   A 1 254 ? -16.474 -23.195 -32.354 1.00 13.76 ? 256 ASP   A N   1 
ATOM   2129 C CA  . ASP   A 1 254 ? -16.678 -24.107 -33.483 1.00 15.50 ? 256 ASP   A CA  1 
ATOM   2130 C C   . ASP   A 1 254 ? -15.347 -24.604 -34.022 1.00 14.00 ? 256 ASP   A C   1 
ATOM   2131 O O   . ASP   A 1 254 ? -15.201 -25.787 -34.353 1.00 18.83 ? 256 ASP   A O   1 
ATOM   2132 C CB  . ASP   A 1 254 ? -17.449 -23.433 -34.615 1.00 15.60 ? 256 ASP   A CB  1 
ATOM   2133 C CG  . ASP   A 1 254 ? -18.912 -23.217 -34.298 1.00 20.35 ? 256 ASP   A CG  1 
ATOM   2134 O OD1 . ASP   A 1 254 ? -19.501 -22.371 -34.994 1.00 23.63 ? 256 ASP   A OD1 1 
ATOM   2135 O OD2 . ASP   A 1 254 ? -19.466 -23.859 -33.373 1.00 20.32 ? 256 ASP   A OD2 1 
ATOM   2136 N N   . TYR   A 1 255 ? -14.368 -23.709 -34.109 1.00 13.51 ? 257 TYR   A N   1 
ATOM   2137 C CA  . TYR   A 1 255 ? -13.056 -24.077 -34.621 1.00 13.00 ? 257 TYR   A CA  1 
ATOM   2138 C C   . TYR   A 1 255 ? -12.397 -25.123 -33.742 1.00 16.67 ? 257 TYR   A C   1 
ATOM   2139 O O   . TYR   A 1 255 ? -11.973 -26.181 -34.225 1.00 15.10 ? 257 TYR   A O   1 
ATOM   2140 C CB  . TYR   A 1 255 ? -12.180 -22.826 -34.714 1.00 12.84 ? 257 TYR   A CB  1 
ATOM   2141 C CG  . TYR   A 1 255 ? -10.735 -23.043 -35.144 1.00 14.78 ? 257 TYR   A CG  1 
ATOM   2142 C CD1 . TYR   A 1 255 ? -10.432 -23.777 -36.280 1.00 15.03 ? 257 TYR   A CD1 1 
ATOM   2143 C CD2 . TYR   A 1 255 ? -9.696  -22.439 -34.447 1.00 16.66 ? 257 TYR   A CD2 1 
ATOM   2144 C CE1 . TYR   A 1 255 ? -9.111  -23.949 -36.691 1.00 14.98 ? 257 TYR   A CE1 1 
ATOM   2145 C CE2 . TYR   A 1 255 ? -8.371  -22.604 -34.852 1.00 17.28 ? 257 TYR   A CE2 1 
ATOM   2146 C CZ  . TYR   A 1 255 ? -8.096  -23.356 -35.978 1.00 17.45 ? 257 TYR   A CZ  1 
ATOM   2147 O OH  . TYR   A 1 255 ? -6.782  -23.514 -36.409 1.00 17.59 ? 257 TYR   A OH  1 
ATOM   2148 N N   . ILE   A 1 256 ? -12.276 -24.839 -32.446 1.00 14.54 ? 258 ILE   A N   1 
ATOM   2149 C CA  . ILE   A 1 256 ? -11.558 -25.793 -31.616 1.00 15.01 ? 258 ILE   A CA  1 
ATOM   2150 C C   . ILE   A 1 256 ? -12.348 -27.090 -31.484 1.00 16.52 ? 258 ILE   A C   1 
ATOM   2151 O O   . ILE   A 1 256 ? -11.753 -28.162 -31.348 1.00 18.25 ? 258 ILE   A O   1 
ATOM   2152 C CB  . ILE   A 1 256 ? -11.194 -25.183 -30.251 1.00 16.55 ? 258 ILE   A CB  1 
ATOM   2153 C CG1 . ILE   A 1 256 ? -12.442 -24.861 -29.437 1.00 15.70 ? 258 ILE   A CG1 1 
ATOM   2154 C CG2 . ILE   A 1 256 ? -10.318 -23.937 -30.447 1.00 17.73 ? 258 ILE   A CG2 1 
ATOM   2155 C CD1 . ILE   A 1 256 ? -12.117 -24.445 -28.002 1.00 19.21 ? 258 ILE   A CD1 1 
ATOM   2156 N N   . ASP   A 1 257 ? -13.686 -27.032 -31.555 1.00 15.52 ? 259 ASP   A N   1 
ATOM   2157 C CA  . ASP   A 1 257 ? -14.483 -28.261 -31.497 1.00 15.86 ? 259 ASP   A CA  1 
ATOM   2158 C C   . ASP   A 1 257 ? -14.293 -29.105 -32.752 1.00 17.19 ? 259 ASP   A C   1 
ATOM   2159 O O   . ASP   A 1 257 ? -14.278 -30.342 -32.678 1.00 19.54 ? 259 ASP   A O   1 
ATOM   2160 C CB  . ASP   A 1 257 ? -15.965 -27.932 -31.298 1.00 15.57 ? 259 ASP   A CB  1 
ATOM   2161 C CG  . ASP   A 1 257 ? -16.266 -27.420 -29.902 1.00 16.54 ? 259 ASP   A CG  1 
ATOM   2162 O OD1 . ASP   A 1 257 ? -15.367 -27.484 -29.040 1.00 20.56 ? 259 ASP   A OD1 1 
ATOM   2163 O OD2 . ASP   A 1 257 ? -17.413 -26.952 -29.672 1.00 21.75 ? 259 ASP   A OD2 1 
ATOM   2164 N N   . LYS   A 1 258 ? -14.144 -28.456 -33.913 1.00 17.59 ? 260 LYS   A N   1 
ATOM   2165 C CA  . LYS   A 1 258 ? -13.893 -29.198 -35.146 1.00 20.06 ? 260 LYS   A CA  1 
ATOM   2166 C C   . LYS   A 1 258 ? -12.622 -30.026 -35.037 1.00 19.94 ? 260 LYS   A C   1 
ATOM   2167 O O   . LYS   A 1 258 ? -12.597 -31.188 -35.448 1.00 22.66 ? 260 LYS   A O   1 
ATOM   2168 C CB  . LYS   A 1 258 ? -13.814 -28.245 -36.341 1.00 15.79 ? 260 LYS   A CB  1 
ATOM   2169 C CG  . LYS   A 1 258 ? -13.393 -28.931 -37.638 1.00 20.04 ? 260 LYS   A CG  1 
ATOM   2170 C CD  . LYS   A 1 258 ? -13.359 -27.996 -38.836 1.00 23.35 ? 260 LYS   A CD  1 
ATOM   2171 C CE  . LYS   A 1 258 ? -12.655 -28.671 -40.027 1.00 21.36 ? 260 LYS   A CE  1 
ATOM   2172 N NZ  . LYS   A 1 258 ? -12.598 -27.807 -41.224 1.00 23.14 ? 260 LYS   A NZ  1 
ATOM   2173 N N   . TYR   A 1 259 ? -11.561 -29.462 -34.465 1.00 17.62 ? 261 TYR   A N   1 
ATOM   2174 C CA  . TYR   A 1 259 ? -10.286 -30.162 -34.381 1.00 17.60 ? 261 TYR   A CA  1 
ATOM   2175 C C   . TYR   A 1 259 ? -10.104 -30.858 -33.037 1.00 19.36 ? 261 TYR   A C   1 
ATOM   2176 O O   . TYR   A 1 259 ? -9.022  -31.392 -32.768 1.00 23.70 ? 261 TYR   A O   1 
ATOM   2177 C CB  . TYR   A 1 259 ? -9.135  -29.193 -34.694 1.00 17.74 ? 261 TYR   A CB  1 
ATOM   2178 C CG  . TYR   A 1 259 ? -9.238  -28.687 -36.117 1.00 17.53 ? 261 TYR   A CG  1 
ATOM   2179 C CD1 . TYR   A 1 259 ? -8.771  -29.459 -37.191 1.00 17.68 ? 261 TYR   A CD1 1 
ATOM   2180 C CD2 . TYR   A 1 259 ? -9.842  -27.467 -36.405 1.00 18.71 ? 261 TYR   A CD2 1 
ATOM   2181 C CE1 . TYR   A 1 259 ? -8.909  -29.022 -38.496 1.00 18.01 ? 261 TYR   A CE1 1 
ATOM   2182 C CE2 . TYR   A 1 259 ? -9.978  -27.020 -37.702 1.00 16.67 ? 261 TYR   A CE2 1 
ATOM   2183 C CZ  . TYR   A 1 259 ? -9.499  -27.796 -38.755 1.00 16.12 ? 261 TYR   A CZ  1 
ATOM   2184 O OH  . TYR   A 1 259 ? -9.632  -27.352 -40.052 1.00 18.22 ? 261 TYR   A OH  1 
ATOM   2185 N N   . ASN   A 1 260 ? -11.164 -30.901 -32.216 1.00 18.10 ? 262 ASN   A N   1 
ATOM   2186 C CA  . ASN   A 1 260 ? -11.149 -31.557 -30.904 1.00 20.95 ? 262 ASN   A CA  1 
ATOM   2187 C C   . ASN   A 1 260 ? -9.986  -31.039 -30.053 1.00 22.02 ? 262 ASN   A C   1 
ATOM   2188 O O   . ASN   A 1 260 ? -9.256  -31.810 -29.426 1.00 30.29 ? 262 ASN   A O   1 
ATOM   2189 C CB  . ASN   A 1 260 ? -11.120 -33.087 -31.051 1.00 22.97 ? 262 ASN   A CB  1 
ATOM   2190 C CG  . ASN   A 1 260 ? -12.436 -33.662 -31.602 1.00 26.08 ? 262 ASN   A CG  1 
ATOM   2191 O OD1 . ASN   A 1 260 ? -13.317 -32.931 -32.048 1.00 39.90 ? 262 ASN   A OD1 1 
ATOM   2192 N ND2 . ASN   A 1 260 ? -12.561 -34.984 -31.568 1.00 32.88 ? 262 ASN   A ND2 1 
ATOM   2193 N N   . ILE   A 1 261 ? -9.818  -29.690 -30.064 1.00 25.35 ? 263 ILE   A N   1 
ATOM   2194 C CA  . ILE   A 1 261 ? -8.831  -28.893 -29.332 1.00 29.87 ? 263 ILE   A CA  1 
ATOM   2195 C C   . ILE   A 1 261 ? -9.480  -28.343 -28.068 1.00 23.01 ? 263 ILE   A C   1 
ATOM   2196 O O   . ILE   A 1 261 ? -10.656 -27.968 -28.081 1.00 24.05 ? 263 ILE   A O   1 
ATOM   2197 C CB  . ILE   A 1 261 ? -8.343  -27.715 -30.214 1.00 30.05 ? 263 ILE   A CB  1 
ATOM   2198 C CG1 . ILE   A 1 261 ? -7.572  -28.174 -31.447 1.00 38.03 ? 263 ILE   A CG1 1 
ATOM   2199 C CG2 . ILE   A 1 261 ? -7.549  -26.669 -29.416 1.00 27.01 ? 263 ILE   A CG2 1 
ATOM   2200 C CD1 . ILE   A 1 261 ? -7.346  -27.029 -32.413 1.00 35.25 ? 263 ILE   A CD1 1 
ATOM   2201 N N   . GLU   A 1 262 ? -8.709  -28.235 -26.981 1.00 23.32 ? 264 GLU   A N   1 
ATOM   2202 C CA  . GLU   A 1 262 ? -9.128  -27.513 -25.781 1.00 24.19 ? 264 GLU   A CA  1 
ATOM   2203 C C   . GLU   A 1 262 ? -8.349  -26.215 -25.635 1.00 23.35 ? 264 GLU   A C   1 
ATOM   2204 O O   . GLU   A 1 262 ? -7.129  -26.190 -25.826 1.00 23.99 ? 264 GLU   A O   1 
ATOM   2205 C CB  . GLU   A 1 262 ? -8.893  -28.328 -24.511 1.00 30.15 ? 264 GLU   A CB  1 
ATOM   2206 C CG  . GLU   A 1 262 ? -9.838  -29.447 -24.248 1.00 32.20 ? 264 GLU   A CG  1 
ATOM   2207 C CD  . GLU   A 1 262 ? -9.751  -29.877 -22.803 1.00 33.85 ? 264 GLU   A CD  1 
ATOM   2208 O OE1 . GLU   A 1 262 ? -10.580 -29.400 -22.000 1.00 36.10 ? 264 GLU   A OE1 1 
ATOM   2209 O OE2 . GLU   A 1 262 ? -8.825  -30.653 -22.464 1.00 33.65 ? 264 GLU   A OE2 1 
ATOM   2210 N N   . LEU   A 1 263 ? -9.043  -25.142 -25.260 1.00 24.15 ? 265 LEU   A N   1 
ATOM   2211 C CA  . LEU   A 1 263 ? -8.341  -23.917 -24.910 1.00 24.49 ? 265 LEU   A CA  1 
ATOM   2212 C C   . LEU   A 1 263 ? -7.581  -24.096 -23.602 1.00 22.84 ? 265 LEU   A C   1 
ATOM   2213 O O   . LEU   A 1 263 ? -7.981  -24.859 -22.716 1.00 28.14 ? 265 LEU   A O   1 
ATOM   2214 C CB  . LEU   A 1 263 ? -9.310  -22.741 -24.775 1.00 26.08 ? 265 LEU   A CB  1 
ATOM   2215 C CG  . LEU   A 1 263 ? -9.943  -22.197 -26.048 1.00 22.78 ? 265 LEU   A CG  1 
ATOM   2216 C CD1 . LEU   A 1 263 ? -10.863 -21.035 -25.713 1.00 25.89 ? 265 LEU   A CD1 1 
ATOM   2217 C CD2 . LEU   A 1 263 ? -8.871  -21.780 -27.046 1.00 26.02 ? 265 LEU   A CD2 1 
ATOM   2218 N N   . ASP   A 1 264 ? -6.473  -23.385 -23.495 1.00 22.87 ? 266 ASP   A N   1 
ATOM   2219 C CA  . ASP   A 1 264 ? -5.802  -23.215 -22.217 1.00 24.87 ? 266 ASP   A CA  1 
ATOM   2220 C C   . ASP   A 1 264 ? -6.825  -22.774 -21.170 1.00 25.40 ? 266 ASP   A C   1 
ATOM   2221 O O   . ASP   A 1 264 ? -7.580  -21.826 -21.416 1.00 23.83 ? 266 ASP   A O   1 
ATOM   2222 C CB  . ASP   A 1 264 ? -4.694  -22.167 -22.382 1.00 25.39 ? 266 ASP   A CB  1 
ATOM   2223 C CG  . ASP   A 1 264 ? -3.743  -22.093 -21.199 1.00 25.44 ? 266 ASP   A CG  1 
ATOM   2224 O OD1 . ASP   A 1 264 ? -4.174  -22.241 -20.042 1.00 26.04 ? 266 ASP   A OD1 1 
ATOM   2225 O OD2 . ASP   A 1 264 ? -2.548  -21.842 -21.439 1.00 31.82 ? 266 ASP   A OD2 1 
ATOM   2226 N N   . PRO   A 1 265 ? -6.913  -23.444 -20.018 1.00 22.81 ? 267 PRO   A N   1 
ATOM   2227 C CA  . PRO   A 1 265 ? -7.898  -23.020 -19.011 1.00 21.08 ? 267 PRO   A CA  1 
ATOM   2228 C C   . PRO   A 1 265 ? -7.702  -21.593 -18.542 1.00 24.20 ? 267 PRO   A C   1 
ATOM   2229 O O   . PRO   A 1 265 ? -8.619  -21.024 -17.945 1.00 25.13 ? 267 PRO   A O   1 
ATOM   2230 C CB  . PRO   A 1 265 ? -7.694  -24.024 -17.864 1.00 22.52 ? 267 PRO   A CB  1 
ATOM   2231 C CG  . PRO   A 1 265 ? -6.358  -24.592 -18.090 1.00 25.59 ? 267 PRO   A CG  1 
ATOM   2232 C CD  . PRO   A 1 265 ? -6.140  -24.612 -19.569 1.00 19.85 ? 267 PRO   A CD  1 
ATOM   2233 N N   . ARG   A 1 266 ? -6.548  -20.978 -18.807 1.00 23.31 ? 268 ARG   A N   1 
ATOM   2234 C CA  . ARG   A 1 266 ? -6.403  -19.597 -18.374 1.00 28.51 ? 268 ARG   A CA  1 
ATOM   2235 C C   . ARG   A 1 266 ? -7.304  -18.644 -19.154 1.00 28.32 ? 268 ARG   A C   1 
ATOM   2236 O O   . ARG   A 1 266 ? -7.502  -17.508 -18.708 1.00 26.46 ? 268 ARG   A O   1 
ATOM   2237 C CB  . ARG   A 1 266 ? -4.940  -19.164 -18.459 1.00 36.74 ? 268 ARG   A CB  1 
ATOM   2238 C CG  . ARG   A 1 266 ? -4.487  -18.669 -19.800 1.00 38.66 ? 268 ARG   A CG  1 
ATOM   2239 C CD  . ARG   A 1 266 ? -3.050  -18.190 -19.700 1.00 42.22 ? 268 ARG   A CD  1 
ATOM   2240 N NE  . ARG   A 1 266 ? -2.092  -19.286 -19.810 1.00 41.07 ? 268 ARG   A NE  1 
ATOM   2241 C CZ  . ARG   A 1 266 ? -0.811  -19.198 -19.469 1.00 50.73 ? 268 ARG   A CZ  1 
ATOM   2242 N NH1 . ARG   A 1 266 ? -0.332  -18.070 -18.960 1.00 53.90 ? 268 ARG   A NH1 1 
ATOM   2243 N NH2 . ARG   A 1 266 ? -0.014  -20.250 -19.608 1.00 48.44 ? 268 ARG   A NH2 1 
ATOM   2244 N N   . PHE   A 1 267 ? -7.894  -19.090 -20.270 1.00 23.54 ? 269 PHE   A N   1 
ATOM   2245 C CA  . PHE   A 1 267 ? -8.870  -18.268 -20.979 1.00 20.19 ? 269 PHE   A CA  1 
ATOM   2246 C C   . PHE   A 1 267 ? -10.212 -18.178 -20.270 1.00 26.23 ? 269 PHE   A C   1 
ATOM   2247 O O   . PHE   A 1 267 ? -11.020 -17.319 -20.638 1.00 27.79 ? 269 PHE   A O   1 
ATOM   2248 C CB  . PHE   A 1 267 ? -9.089  -18.801 -22.392 1.00 18.86 ? 269 PHE   A CB  1 
ATOM   2249 C CG  . PHE   A 1 267 ? -7.971  -18.478 -23.334 1.00 18.67 ? 269 PHE   A CG  1 
ATOM   2250 C CD1 . PHE   A 1 267 ? -7.064  -19.450 -23.725 1.00 18.59 ? 269 PHE   A CD1 1 
ATOM   2251 C CD2 . PHE   A 1 267 ? -7.820  -17.191 -23.820 1.00 21.17 ? 269 PHE   A CD2 1 
ATOM   2252 C CE1 . PHE   A 1 267 ? -6.027  -19.143 -24.588 1.00 20.43 ? 269 PHE   A CE1 1 
ATOM   2253 C CE2 . PHE   A 1 267 ? -6.784  -16.876 -24.683 1.00 19.40 ? 269 PHE   A CE2 1 
ATOM   2254 C CZ  . PHE   A 1 267 ? -5.895  -17.844 -25.072 1.00 20.15 ? 269 PHE   A CZ  1 
ATOM   2255 N N   . ASN   A 1 268 ? -10.470 -19.019 -19.263 1.00 28.49 ? 270 ASN   A N   1 
ATOM   2256 C CA  . ASN   A 1 268 ? -11.784 -19.015 -18.623 1.00 30.30 ? 270 ASN   A CA  1 
ATOM   2257 C C   . ASN   A 1 268 ? -12.107 -17.667 -17.992 1.00 31.69 ? 270 ASN   A C   1 
ATOM   2258 O O   . ASN   A 1 268 ? -13.280 -17.282 -17.924 1.00 37.33 ? 270 ASN   A O   1 
ATOM   2259 C CB  . ASN   A 1 268 ? -11.868 -20.119 -17.566 1.00 37.39 ? 270 ASN   A CB  1 
ATOM   2260 C CG  . ASN   A 1 268 ? -11.846 -21.513 -18.168 1.00 44.02 ? 270 ASN   A CG  1 
ATOM   2261 O OD1 . ASN   A 1 268 ? -11.481 -22.481 -17.502 1.00 52.72 ? 270 ASN   A OD1 1 
ATOM   2262 N ND2 . ASN   A 1 268 ? -12.232 -21.619 -19.431 1.00 44.07 ? 270 ASN   A ND2 1 
ATOM   2263 N N   . ASP   A 1 269 ? -11.095 -16.928 -17.545 1.00 29.32 ? 271 ASP   A N   1 
ATOM   2264 C CA  . ASP   A 1 269 ? -11.322 -15.650 -16.885 1.00 36.88 ? 271 ASP   A CA  1 
ATOM   2265 C C   . ASP   A 1 269 ? -11.222 -14.450 -17.818 1.00 34.94 ? 271 ASP   A C   1 
ATOM   2266 O O   . ASP   A 1 269 ? -11.595 -13.345 -17.412 1.00 39.25 ? 271 ASP   A O   1 
ATOM   2267 C CB  . ASP   A 1 269 ? -10.326 -15.447 -15.734 1.00 51.60 ? 271 ASP   A CB  1 
ATOM   2268 C CG  . ASP   A 1 269 ? -10.528 -16.435 -14.602 1.00 68.19 ? 271 ASP   A CG  1 
ATOM   2269 O OD1 . ASP   A 1 269 ? -9.538  -16.749 -13.905 1.00 73.39 ? 271 ASP   A OD1 1 
ATOM   2270 O OD2 . ASP   A 1 269 ? -11.670 -16.907 -14.417 1.00 71.35 ? 271 ASP   A OD2 1 
ATOM   2271 N N   . ILE   A 1 270 ? -10.730 -14.619 -19.041 1.00 25.27 ? 272 ILE   A N   1 
ATOM   2272 C CA  . ILE   A 1 270 ? -10.415 -13.475 -19.887 1.00 25.31 ? 272 ILE   A CA  1 
ATOM   2273 C C   . ILE   A 1 270 ? -11.154 -13.473 -21.218 1.00 21.36 ? 272 ILE   A C   1 
ATOM   2274 O O   . ILE   A 1 270 ? -11.230 -12.411 -21.852 1.00 23.46 ? 272 ILE   A O   1 
ATOM   2275 C CB  . ILE   A 1 270 ? -8.894  -13.368 -20.135 1.00 23.72 ? 272 ILE   A CB  1 
ATOM   2276 C CG1 . ILE   A 1 270 ? -8.360  -14.640 -20.804 1.00 21.50 ? 272 ILE   A CG1 1 
ATOM   2277 C CG2 . ILE   A 1 270 ? -8.163  -13.085 -18.836 1.00 27.17 ? 272 ILE   A CG2 1 
ATOM   2278 C CD1 . ILE   A 1 270 ? -6.905  -14.538 -21.281 1.00 24.97 ? 272 ILE   A CD1 1 
ATOM   2279 N N   . LEU   A 1 271 ? -11.703 -14.603 -21.674 1.00 21.99 ? 273 LEU   A N   1 
ATOM   2280 C CA  . LEU   A 1 271 ? -12.222 -14.679 -23.038 1.00 19.60 ? 273 LEU   A CA  1 
ATOM   2281 C C   . LEU   A 1 271 ? -13.582 -13.999 -23.194 1.00 22.67 ? 273 LEU   A C   1 
ATOM   2282 O O   . LEU   A 1 271 ? -13.818 -13.315 -24.191 1.00 24.10 ? 273 LEU   A O   1 
ATOM   2283 C CB  . LEU   A 1 271 ? -12.300 -16.138 -23.488 1.00 23.10 ? 273 LEU   A CB  1 
ATOM   2284 C CG  . LEU   A 1 271 ? -12.716 -16.344 -24.944 1.00 24.26 ? 273 LEU   A CG  1 
ATOM   2285 C CD1 . LEU   A 1 271 ? -11.765 -15.600 -25.874 1.00 26.10 ? 273 LEU   A CD1 1 
ATOM   2286 C CD2 . LEU   A 1 271 ? -12.728 -17.824 -25.282 1.00 26.27 ? 273 LEU   A CD2 1 
ATOM   2287 N N   . GLY   A 1 272 ? -14.491 -14.183 -22.240 1.00 21.95 ? 274 GLY   A N   1 
ATOM   2288 C CA  . GLY   A 1 272 ? -15.815 -13.586 -22.332 1.00 20.47 ? 274 GLY   A CA  1 
ATOM   2289 C C   . GLY   A 1 272 ? -16.666 -14.217 -23.432 1.00 19.80 ? 274 GLY   A C   1 
ATOM   2290 O O   . GLY   A 1 272 ? -16.339 -15.266 -23.995 1.00 21.75 ? 274 GLY   A O   1 
ATOM   2291 N N   . ARG   A 1 273 ? -17.787 -13.554 -23.724 1.00 19.24 ? 275 ARG   A N   1 
ATOM   2292 C CA  . ARG   A 1 273 ? -18.670 -13.912 -24.831 1.00 17.20 ? 275 ARG   A CA  1 
ATOM   2293 C C   . ARG   A 1 273 ? -18.791 -12.712 -25.760 1.00 18.48 ? 275 ARG   A C   1 
ATOM   2294 O O   . ARG   A 1 273 ? -19.120 -11.609 -25.314 1.00 23.57 ? 275 ARG   A O   1 
ATOM   2295 C CB  . ARG   A 1 273 ? -20.068 -14.328 -24.348 1.00 20.06 ? 275 ARG   A CB  1 
ATOM   2296 C CG  . ARG   A 1 273 ? -20.091 -15.550 -23.444 1.00 23.33 ? 275 ARG   A CG  1 
ATOM   2297 C CD  . ARG   A 1 273 ? -21.507 -16.121 -23.370 1.00 23.80 ? 275 ARG   A CD  1 
ATOM   2298 N NE  . ARG   A 1 273 ? -22.427 -15.284 -22.606 1.00 24.52 ? 275 ARG   A NE  1 
ATOM   2299 C CZ  . ARG   A 1 273 ? -23.741 -15.491 -22.549 1.00 21.90 ? 275 ARG   A CZ  1 
ATOM   2300 N NH1 . ARG   A 1 273 ? -24.284 -16.495 -23.231 1.00 29.38 ? 275 ARG   A NH1 1 
ATOM   2301 N NH2 . ARG   A 1 273 ? -24.516 -14.690 -21.828 1.00 23.73 ? 275 ARG   A NH2 1 
ATOM   2302 N N   . HIS   A 1 274 ? -18.531 -12.926 -27.052 1.00 14.29 ? 276 HIS   A N   1 
ATOM   2303 C CA  . HIS   A 1 274 ? -18.489 -11.835 -28.011 1.00 12.84 ? 276 HIS   A CA  1 
ATOM   2304 C C   . HIS   A 1 274 ? -19.189 -12.258 -29.282 1.00 13.58 ? 276 HIS   A C   1 
ATOM   2305 O O   . HIS   A 1 274 ? -18.943 -13.352 -29.790 1.00 15.36 ? 276 HIS   A O   1 
ATOM   2306 C CB  . HIS   A 1 274 ? -17.039 -11.442 -28.330 1.00 13.43 ? 276 HIS   A CB  1 
ATOM   2307 C CG  . HIS   A 1 274 ? -16.267 -11.043 -27.117 1.00 14.25 ? 276 HIS   A CG  1 
ATOM   2308 N ND1 . HIS   A 1 274 ? -16.431 -9.818  -26.506 1.00 17.11 ? 276 HIS   A ND1 1 
ATOM   2309 C CD2 . HIS   A 1 274 ? -15.369 -11.723 -26.366 1.00 15.77 ? 276 HIS   A CD2 1 
ATOM   2310 C CE1 . HIS   A 1 274 ? -15.647 -9.750  -25.446 1.00 18.46 ? 276 HIS   A CE1 1 
ATOM   2311 N NE2 . HIS   A 1 274 ? -14.987 -10.891 -25.342 1.00 19.21 ? 276 HIS   A NE2 1 
ATOM   2312 N N   . SER   A 1 275 ? -20.056 -11.394 -29.787 1.00 14.41 ? 277 SER   A N   1 
ATOM   2313 C CA  . SER   A 1 275 ? -20.650 -11.619 -31.092 1.00 13.96 ? 277 SER   A CA  1 
ATOM   2314 C C   . SER   A 1 275 ? -19.614 -11.407 -32.192 1.00 16.82 ? 277 SER   A C   1 
ATOM   2315 O O   . SER   A 1 275 ? -18.611 -10.712 -32.013 1.00 18.11 ? 277 SER   A O   1 
ATOM   2316 C CB  . SER   A 1 275 ? -21.806 -10.654 -31.307 1.00 18.85 ? 277 SER   A CB  1 
ATOM   2317 O OG  . SER   A 1 275 ? -21.323 -9.334  -31.134 1.00 27.06 ? 277 SER   A OG  1 
ATOM   2318 N N   . ARG   A 1 276 ? -19.868 -12.010 -33.347 1.00 14.56 ? 278 ARG   A N   1 
ATOM   2319 C CA  . ARG   A 1 276 ? -19.085 -11.673 -34.531 1.00 13.25 ? 278 ARG   A CA  1 
ATOM   2320 C C   . ARG   A 1 276 ? -19.508 -10.293 -35.025 1.00 15.43 ? 278 ARG   A C   1 
ATOM   2321 O O   . ARG   A 1 276 ? -20.700 -9.955  -35.022 1.00 16.43 ? 278 ARG   A O   1 
ATOM   2322 C CB  . ARG   A 1 276 ? -19.286 -12.733 -35.617 1.00 12.67 ? 278 ARG   A CB  1 
ATOM   2323 C CG  . ARG   A 1 276 ? -18.300 -12.628 -36.803 1.00 13.35 ? 278 ARG   A CG  1 
ATOM   2324 C CD  . ARG   A 1 276 ? -18.058 -14.001 -37.430 1.00 14.69 ? 278 ARG   A CD  1 
ATOM   2325 N NE  . ARG   A 1 276 ? -16.865 -14.041 -38.286 1.00 17.18 ? 278 ARG   A NE  1 
ATOM   2326 C CZ  . ARG   A 1 276 ? -16.152 -15.143 -38.511 1.00 17.55 ? 278 ARG   A CZ  1 
ATOM   2327 N NH1 . ARG   A 1 276 ? -16.477 -16.284 -37.928 1.00 17.97 ? 278 ARG   A NH1 1 
ATOM   2328 N NH2 . ARG   A 1 276 ? -15.089 -15.105 -39.314 1.00 16.03 ? 278 ARG   A NH2 1 
ATOM   2329 N N   . LYS   A 1 277 ? -18.535 -9.486  -35.427 1.00 15.65 ? 279 LYS   A N   1 
ATOM   2330 C CA  . LYS   A 1 277 ? -18.785 -8.116  -35.842 1.00 14.08 ? 279 LYS   A CA  1 
ATOM   2331 C C   . LYS   A 1 277 ? -18.838 -8.040  -37.361 1.00 18.56 ? 279 LYS   A C   1 
ATOM   2332 O O   . LYS   A 1 277 ? -18.290 -8.890  -38.071 1.00 22.97 ? 279 LYS   A O   1 
ATOM   2333 C CB  . LYS   A 1 277 ? -17.692 -7.177  -35.304 1.00 15.20 ? 279 LYS   A CB  1 
ATOM   2334 C CG  . LYS   A 1 277 ? -17.490 -7.235  -33.794 1.00 13.79 ? 279 LYS   A CG  1 
ATOM   2335 C CD  . LYS   A 1 277 ? -18.793 -7.100  -33.002 1.00 13.04 ? 279 LYS   A CD  1 
ATOM   2336 C CE  . LYS   A 1 277 ? -18.555 -7.012  -31.493 1.00 15.31 ? 279 LYS   A CE  1 
ATOM   2337 N NZ  . LYS   A 1 277 ? -18.012 -8.272  -30.881 1.00 18.12 ? 279 LYS   A NZ  1 
ATOM   2338 N N   . ARG   A 1 278 ? -19.497 -7.000  -37.860 1.00 16.32 ? 280 ARG   A N   1 
ATOM   2339 C CA  . ARG   A 1 278 ? -19.463 -6.693  -39.282 1.00 18.65 ? 280 ARG   A CA  1 
ATOM   2340 C C   . ARG   A 1 278 ? -18.310 -5.735  -39.535 1.00 18.46 ? 280 ARG   A C   1 
ATOM   2341 O O   . ARG   A 1 278 ? -18.043 -4.845  -38.722 1.00 19.06 ? 280 ARG   A O   1 
ATOM   2342 C CB  . ARG   A 1 278 ? -20.783 -6.078  -39.744 1.00 19.78 ? 280 ARG   A CB  1 
ATOM   2343 C CG  . ARG   A 1 278 ? -21.978 -6.999  -39.516 1.00 23.45 ? 280 ARG   A CG  1 
ATOM   2344 C CD  . ARG   A 1 278 ? -23.241 -6.469  -40.139 1.00 22.71 ? 280 ARG   A CD  1 
ATOM   2345 N NE  . ARG   A 1 278 ? -24.405 -7.090  -39.515 1.00 23.93 ? 280 ARG   A NE  1 
ATOM   2346 C CZ  . ARG   A 1 278 ? -24.981 -8.215  -39.929 1.00 25.63 ? 280 ARG   A CZ  1 
ATOM   2347 N NH1 . ARG   A 1 278 ? -24.527 -8.865  -40.990 1.00 22.36 ? 280 ARG   A NH1 1 
ATOM   2348 N NH2 . ARG   A 1 278 ? -26.027 -8.693  -39.270 1.00 21.54 ? 280 ARG   A NH2 1 
ATOM   2349 N N   . TRP   A 1 279 ? -17.612 -5.939  -40.654 1.00 18.98 ? 281 TRP   A N   1 
ATOM   2350 C CA  . TRP   A 1 279 ? -16.387 -5.187  -40.899 1.00 16.87 ? 281 TRP   A CA  1 
ATOM   2351 C C   . TRP   A 1 279 ? -16.649 -3.697  -41.061 1.00 22.38 ? 281 TRP   A C   1 
ATOM   2352 O O   . TRP   A 1 279 ? -15.734 -2.895  -40.836 1.00 20.34 ? 281 TRP   A O   1 
ATOM   2353 C CB  . TRP   A 1 279 ? -15.667 -5.744  -42.130 1.00 18.68 ? 281 TRP   A CB  1 
ATOM   2354 C CG  . TRP   A 1 279 ? -15.124 -7.106  -41.898 1.00 18.31 ? 281 TRP   A CG  1 
ATOM   2355 C CD1 . TRP   A 1 279 ? -15.601 -8.284  -42.403 1.00 25.78 ? 281 TRP   A CD1 1 
ATOM   2356 C CD2 . TRP   A 1 279 ? -14.018 -7.446  -41.058 1.00 16.46 ? 281 TRP   A CD2 1 
ATOM   2357 N NE1 . TRP   A 1 279 ? -14.850 -9.335  -41.936 1.00 19.73 ? 281 TRP   A NE1 1 
ATOM   2358 C CE2 . TRP   A 1 279 ? -13.866 -8.847  -41.110 1.00 19.39 ? 281 TRP   A CE2 1 
ATOM   2359 C CE3 . TRP   A 1 279 ? -13.134 -6.698  -40.268 1.00 19.43 ? 281 TRP   A CE3 1 
ATOM   2360 C CZ2 . TRP   A 1 279 ? -12.868 -9.514  -40.403 1.00 18.87 ? 281 TRP   A CZ2 1 
ATOM   2361 C CZ3 . TRP   A 1 279 ? -12.147 -7.361  -39.566 1.00 20.02 ? 281 TRP   A CZ3 1 
ATOM   2362 C CH2 . TRP   A 1 279 ? -12.017 -8.757  -39.637 1.00 20.73 ? 281 TRP   A CH2 1 
ATOM   2363 N N   . GLU   A 1 280 ? -17.876 -3.309  -41.416 1.00 21.44 ? 282 GLU   A N   1 
ATOM   2364 C CA  . GLU   A 1 280 ? -18.193 -1.898  -41.590 1.00 21.98 ? 282 GLU   A CA  1 
ATOM   2365 C C   . GLU   A 1 280 ? -17.991 -1.097  -40.309 1.00 20.25 ? 282 GLU   A C   1 
ATOM   2366 O O   . GLU   A 1 280 ? -17.810 0.125   -40.372 1.00 23.12 ? 282 GLU   A O   1 
ATOM   2367 C CB  . GLU   A 1 280 ? -19.632 -1.750  -42.095 1.00 25.45 ? 282 GLU   A CB  1 
ATOM   2368 C CG  . GLU   A 1 280 ? -19.828 -2.141  -43.564 1.00 26.49 ? 282 GLU   A CG  1 
ATOM   2369 C CD  . GLU   A 1 280 ? -20.030 -3.641  -43.798 1.00 31.47 ? 282 GLU   A CD  1 
ATOM   2370 O OE1 . GLU   A 1 280 ? -20.298 -4.016  -44.964 1.00 34.09 ? 282 GLU   A OE1 1 
ATOM   2371 O OE2 . GLU   A 1 280 ? -19.925 -4.446  -42.840 1.00 30.06 ? 282 GLU   A OE2 1 
ATOM   2372 N N   . ARG   A 1 281 ? -18.000 -1.754  -39.152 1.00 20.07 ? 283 ARG   A N   1 
ATOM   2373 C CA  . ARG   A 1 281 ? -17.801 -1.035  -37.900 1.00 22.75 ? 283 ARG   A CA  1 
ATOM   2374 C C   . ARG   A 1 281 ? -16.441 -0.339  -37.837 1.00 22.78 ? 283 ARG   A C   1 
ATOM   2375 O O   . ARG   A 1 281 ? -16.296 0.652   -37.115 1.00 23.48 ? 283 ARG   A O   1 
ATOM   2376 C CB  . ARG   A 1 281 ? -17.978 -2.012  -36.727 1.00 31.41 ? 283 ARG   A CB  1 
ATOM   2377 C CG  . ARG   A 1 281 ? -16.860 -2.009  -35.701 1.00 39.65 ? 283 ARG   A CG  1 
ATOM   2378 C CD  . ARG   A 1 281 ? -16.875 -3.266  -34.842 1.00 43.52 ? 283 ARG   A CD  1 
ATOM   2379 N NE  . ARG   A 1 281 ? -18.140 -3.451  -34.138 1.00 47.01 ? 283 ARG   A NE  1 
ATOM   2380 C CZ  . ARG   A 1 281 ? -18.316 -3.245  -32.834 1.00 34.61 ? 283 ARG   A CZ  1 
ATOM   2381 N NH1 . ARG   A 1 281 ? -17.308 -2.841  -32.070 1.00 35.40 ? 283 ARG   A NH1 1 
ATOM   2382 N NH2 . ARG   A 1 281 ? -19.507 -3.446  -32.300 1.00 32.68 ? 283 ARG   A NH2 1 
ATOM   2383 N N   . PHE   A 1 282 ? -15.449 -0.808  -38.587 1.00 17.81 ? 284 PHE   A N   1 
ATOM   2384 C CA  . PHE   A 1 282 ? -14.114 -0.231  -38.505 1.00 17.84 ? 284 PHE   A CA  1 
ATOM   2385 C C   . PHE   A 1 282 ? -13.882 0.863   -39.537 1.00 18.04 ? 284 PHE   A C   1 
ATOM   2386 O O   . PHE   A 1 282 ? -12.792 1.450   -39.570 1.00 19.35 ? 284 PHE   A O   1 
ATOM   2387 C CB  . PHE   A 1 282 ? -13.066 -1.339  -38.650 1.00 18.42 ? 284 PHE   A CB  1 
ATOM   2388 C CG  . PHE   A 1 282 ? -13.238 -2.439  -37.643 1.00 21.46 ? 284 PHE   A CG  1 
ATOM   2389 C CD1 . PHE   A 1 282 ? -12.863 -2.248  -36.322 1.00 23.96 ? 284 PHE   A CD1 1 
ATOM   2390 C CD2 . PHE   A 1 282 ? -13.819 -3.643  -38.005 1.00 17.28 ? 284 PHE   A CD2 1 
ATOM   2391 C CE1 . PHE   A 1 282 ? -13.038 -3.246  -35.390 1.00 22.32 ? 284 PHE   A CE1 1 
ATOM   2392 C CE2 . PHE   A 1 282 ? -14.005 -4.646  -37.071 1.00 22.92 ? 284 PHE   A CE2 1 
ATOM   2393 C CZ  . PHE   A 1 282 ? -13.618 -4.449  -35.765 1.00 25.47 ? 284 PHE   A CZ  1 
ATOM   2394 N N   . VAL   A 1 283 ? -14.868 1.137   -40.371 1.00 18.57 ? 285 VAL   A N   1 
ATOM   2395 C CA  . VAL   A 1 283 ? -14.794 2.190   -41.372 1.00 18.50 ? 285 VAL   A CA  1 
ATOM   2396 C C   . VAL   A 1 283 ? -15.153 3.522   -40.731 1.00 20.64 ? 285 VAL   A C   1 
ATOM   2397 O O   . VAL   A 1 283 ? -16.116 3.627   -39.963 1.00 21.57 ? 285 VAL   A O   1 
ATOM   2398 C CB  . VAL   A 1 283 ? -15.733 1.853   -42.542 1.00 19.05 ? 285 VAL   A CB  1 
ATOM   2399 C CG1 . VAL   A 1 283 ? -15.687 2.934   -43.628 1.00 23.01 ? 285 VAL   A CG1 1 
ATOM   2400 C CG2 . VAL   A 1 283 ? -15.394 0.484   -43.100 1.00 20.84 ? 285 VAL   A CG2 1 
ATOM   2401 N N   . HIS   A 1 284 ? -14.383 4.553   -41.055 1.00 17.50 ? 286 HIS   A N   1 
ATOM   2402 C CA  . HIS   A 1 284 ? -14.661 5.903   -40.590 1.00 18.13 ? 286 HIS   A CA  1 
ATOM   2403 C C   . HIS   A 1 284 ? -14.163 6.887   -41.639 1.00 19.35 ? 286 HIS   A C   1 
ATOM   2404 O O   . HIS   A 1 284 ? -13.590 6.503   -42.665 1.00 18.94 ? 286 HIS   A O   1 
ATOM   2405 C CB  . HIS   A 1 284 ? -14.033 6.159   -39.213 1.00 19.98 ? 286 HIS   A CB  1 
ATOM   2406 C CG  . HIS   A 1 284 ? -12.579 5.812   -39.131 1.00 17.90 ? 286 HIS   A CG  1 
ATOM   2407 N ND1 . HIS   A 1 284 ? -11.615 6.466   -39.870 1.00 19.84 ? 286 HIS   A ND1 1 
ATOM   2408 C CD2 . HIS   A 1 284 ? -11.924 4.887   -38.390 1.00 17.92 ? 286 HIS   A CD2 1 
ATOM   2409 C CE1 . HIS   A 1 284 ? -10.431 5.957   -39.590 1.00 19.01 ? 286 HIS   A CE1 1 
ATOM   2410 N NE2 . HIS   A 1 284 ? -10.589 4.997   -38.694 1.00 18.27 ? 286 HIS   A NE2 1 
ATOM   2411 N N   . SER   A 1 285 ? -14.370 8.177   -41.374 1.00 21.87 ? 287 SER   A N   1 
ATOM   2412 C CA  . SER   A 1 285 ? -14.090 9.178   -42.395 1.00 21.10 ? 287 SER   A CA  1 
ATOM   2413 C C   . SER   A 1 285 ? -12.614 9.234   -42.786 1.00 19.27 ? 287 SER   A C   1 
ATOM   2414 O O   . SER   A 1 285 ? -12.302 9.678   -43.897 1.00 24.11 ? 287 SER   A O   1 
ATOM   2415 C CB  . SER   A 1 285 ? -14.569 10.553  -41.922 1.00 28.54 ? 287 SER   A CB  1 
ATOM   2416 O OG  . SER   A 1 285 ? -14.031 10.872  -40.651 1.00 36.04 ? 287 SER   A OG  1 
ATOM   2417 N N   . GLU   A 1 286 ? -11.704 8.764   -41.932 1.00 19.86 ? 288 GLU   A N   1 
ATOM   2418 C CA  . GLU   A 1 286 ? -10.284 8.870   -42.251 1.00 19.70 ? 288 GLU   A CA  1 
ATOM   2419 C C   . GLU   A 1 286 ? -9.714  7.626   -42.915 1.00 24.99 ? 288 GLU   A C   1 
ATOM   2420 O O   . GLU   A 1 286 ? -8.542  7.640   -43.308 1.00 29.52 ? 288 GLU   A O   1 
ATOM   2421 C CB  . GLU   A 1 286 ? -9.481  9.190   -40.992 1.00 21.35 ? 288 GLU   A CB  1 
ATOM   2422 C CG  . GLU   A 1 286 ? -9.647  10.628  -40.529 1.00 26.54 ? 288 GLU   A CG  1 
ATOM   2423 C CD  . GLU   A 1 286 ? -11.046 10.913  -40.002 1.00 30.48 ? 288 GLU   A CD  1 
ATOM   2424 O OE1 . GLU   A 1 286 ? -11.547 10.134  -39.151 1.00 26.82 ? 288 GLU   A OE1 1 
ATOM   2425 O OE2 . GLU   A 1 286 ? -11.651 11.913  -40.449 1.00 33.69 ? 288 GLU   A OE2 1 
ATOM   2426 N N   . ASN   A 1 287 ? -10.494 6.558   -43.057 1.00 19.17 ? 289 ASN   A N   1 
ATOM   2427 C CA  . ASN   A 1 287 ? -10.028 5.407   -43.816 1.00 18.18 ? 289 ASN   A CA  1 
ATOM   2428 C C   . ASN   A 1 287 ? -10.971 5.016   -44.947 1.00 17.08 ? 289 ASN   A C   1 
ATOM   2429 O O   . ASN   A 1 287 ? -10.660 4.084   -45.688 1.00 19.96 ? 289 ASN   A O   1 
ATOM   2430 C CB  . ASN   A 1 287 ? -9.772  4.194   -42.892 1.00 16.98 ? 289 ASN   A CB  1 
ATOM   2431 C CG  . ASN   A 1 287 ? -11.041 3.664   -42.212 1.00 14.53 ? 289 ASN   A CG  1 
ATOM   2432 O OD1 . ASN   A 1 287 ? -12.152 3.870   -42.694 1.00 16.87 ? 289 ASN   A OD1 1 
ATOM   2433 N ND2 . ASN   A 1 287 ? -10.864 2.951   -41.104 1.00 18.19 ? 289 ASN   A ND2 1 
ATOM   2434 N N   . GLN   A 1 288 ? -12.111 5.697   -45.120 1.00 19.37 ? 290 GLN   A N   1 
ATOM   2435 C CA  . GLN   A 1 288 ? -13.107 5.159   -46.042 1.00 20.73 ? 290 GLN   A CA  1 
ATOM   2436 C C   . GLN   A 1 288 ? -12.625 5.157   -47.490 1.00 20.71 ? 290 GLN   A C   1 
ATOM   2437 O O   . GLN   A 1 288 ? -13.135 4.366   -48.290 1.00 24.91 ? 290 GLN   A O   1 
ATOM   2438 C CB  . GLN   A 1 288 ? -14.421 5.924   -45.914 1.00 26.27 ? 290 GLN   A CB  1 
ATOM   2439 C CG  . GLN   A 1 288 ? -14.369 7.351   -46.386 1.00 28.16 ? 290 GLN   A CG  1 
ATOM   2440 C CD  . GLN   A 1 288 ? -15.716 8.046   -46.241 1.00 44.92 ? 290 GLN   A CD  1 
ATOM   2441 O OE1 . GLN   A 1 288 ? -15.793 9.180   -45.769 1.00 53.77 ? 290 GLN   A OE1 1 
ATOM   2442 N NE2 . GLN   A 1 288 ? -16.783 7.366   -46.656 1.00 47.97 ? 290 GLN   A NE2 1 
ATOM   2443 N N   . HIS   A 1 289 ? -11.655 6.004   -47.835 1.00 20.08 ? 291 HIS   A N   1 
ATOM   2444 C CA  . HIS   A 1 289 ? -11.107 6.007   -49.187 1.00 21.06 ? 291 HIS   A CA  1 
ATOM   2445 C C   . HIS   A 1 289 ? -10.317 4.742   -49.495 1.00 21.91 ? 291 HIS   A C   1 
ATOM   2446 O O   . HIS   A 1 289 ? -10.053 4.472   -50.670 1.00 24.21 ? 291 HIS   A O   1 
ATOM   2447 C CB  . HIS   A 1 289 ? -10.227 7.246   -49.411 1.00 24.71 ? 291 HIS   A CB  1 
ATOM   2448 C CG  . HIS   A 1 289 ? -9.008  7.300   -48.549 1.00 25.85 ? 291 HIS   A CG  1 
ATOM   2449 N ND1 . HIS   A 1 289 ? -9.066  7.523   -47.192 1.00 26.27 ? 291 HIS   A ND1 1 
ATOM   2450 C CD2 . HIS   A 1 289 ? -7.693  7.171   -48.853 1.00 26.01 ? 291 HIS   A CD2 1 
ATOM   2451 C CE1 . HIS   A 1 289 ? -7.843  7.519   -46.692 1.00 26.86 ? 291 HIS   A CE1 1 
ATOM   2452 N NE2 . HIS   A 1 289 ? -6.991  7.310   -47.680 1.00 26.16 ? 291 HIS   A NE2 1 
ATOM   2453 N N   . LEU   A 1 290 ? -9.957  3.959   -48.481 1.00 21.31 ? 292 LEU   A N   1 
ATOM   2454 C CA  . LEU   A 1 290 ? -9.231  2.707   -48.665 1.00 18.49 ? 292 LEU   A CA  1 
ATOM   2455 C C   . LEU   A 1 290 ? -10.146 1.496   -48.622 1.00 18.28 ? 292 LEU   A C   1 
ATOM   2456 O O   . LEU   A 1 290 ? -9.685  0.377   -48.878 1.00 20.66 ? 292 LEU   A O   1 
ATOM   2457 C CB  . LEU   A 1 290 ? -8.149  2.554   -47.589 1.00 18.72 ? 292 LEU   A CB  1 
ATOM   2458 C CG  . LEU   A 1 290 ? -7.197  3.741   -47.458 1.00 20.47 ? 292 LEU   A CG  1 
ATOM   2459 C CD1 . LEU   A 1 290 ? -6.190  3.509   -46.368 1.00 22.54 ? 292 LEU   A CD1 1 
ATOM   2460 C CD2 . LEU   A 1 290 ? -6.487  3.974   -48.793 1.00 25.34 ? 292 LEU   A CD2 1 
ATOM   2461 N N   . VAL   A 1 291 ? -11.423 1.695   -48.323 1.00 18.87 ? 293 VAL   A N   1 
ATOM   2462 C CA  . VAL   A 1 291 ? -12.369 0.612   -48.110 1.00 20.41 ? 293 VAL   A CA  1 
ATOM   2463 C C   . VAL   A 1 291 ? -13.359 0.590   -49.264 1.00 23.23 ? 293 VAL   A C   1 
ATOM   2464 O O   . VAL   A 1 291 ? -13.780 1.639   -49.769 1.00 31.76 ? 293 VAL   A O   1 
ATOM   2465 C CB  . VAL   A 1 291 ? -13.087 0.763   -46.752 1.00 23.78 ? 293 VAL   A CB  1 
ATOM   2466 C CG1 . VAL   A 1 291 ? -14.048 -0.401  -46.505 1.00 28.57 ? 293 VAL   A CG1 1 
ATOM   2467 C CG2 . VAL   A 1 291 ? -12.066 0.849   -45.638 1.00 20.89 ? 293 VAL   A CG2 1 
ATOM   2468 N N   . SER   A 1 292 ? -13.705 -0.612  -49.693 1.00 22.90 ? 294 SER   A N   1 
ATOM   2469 C CA  . SER   A 1 292 ? -14.671 -0.885  -50.741 1.00 20.33 ? 294 SER   A CA  1 
ATOM   2470 C C   . SER   A 1 292 ? -15.372 -2.174  -50.353 1.00 21.46 ? 294 SER   A C   1 
ATOM   2471 O O   . SER   A 1 292 ? -14.862 -2.928  -49.521 1.00 19.59 ? 294 SER   A O   1 
ATOM   2472 C CB  . SER   A 1 292 ? -13.991 -1.061  -52.103 1.00 22.13 ? 294 SER   A CB  1 
ATOM   2473 O OG  . SER   A 1 292 ? -13.006 -2.090  -52.022 1.00 22.01 ? 294 SER   A OG  1 
ATOM   2474 N N   . PRO   A 1 293 ? -16.529 -2.466  -50.946 1.00 21.31 ? 295 PRO   A N   1 
ATOM   2475 C CA  . PRO   A 1 293 ? -17.146 -3.769  -50.651 1.00 20.34 ? 295 PRO   A CA  1 
ATOM   2476 C C   . PRO   A 1 293 ? -16.243 -4.930  -51.022 1.00 22.92 ? 295 PRO   A C   1 
ATOM   2477 O O   . PRO   A 1 293 ? -16.214 -5.944  -50.307 1.00 20.20 ? 295 PRO   A O   1 
ATOM   2478 C CB  . PRO   A 1 293 ? -18.443 -3.742  -51.480 1.00 26.96 ? 295 PRO   A CB  1 
ATOM   2479 C CG  . PRO   A 1 293 ? -18.728 -2.292  -51.671 1.00 34.51 ? 295 PRO   A CG  1 
ATOM   2480 C CD  . PRO   A 1 293 ? -17.390 -1.628  -51.801 1.00 24.39 ? 295 PRO   A CD  1 
ATOM   2481 N N   . GLU   A 1 294 ? -15.472 -4.782  -52.107 1.00 21.28 ? 296 GLU   A N   1 
ATOM   2482 C CA  . GLU   A 1 294 ? -14.525 -5.821  -52.503 1.00 16.87 ? 296 GLU   A CA  1 
ATOM   2483 C C   . GLU   A 1 294 ? -13.453 -6.025  -51.439 1.00 19.05 ? 296 GLU   A C   1 
ATOM   2484 O O   . GLU   A 1 294 ? -13.111 -7.166  -51.120 1.00 17.92 ? 296 GLU   A O   1 
ATOM   2485 C CB  . GLU   A 1 294 ? -13.881 -5.483  -53.852 1.00 20.33 ? 296 GLU   A CB  1 
ATOM   2486 C CG  . GLU   A 1 294 ? -14.843 -5.582  -55.050 1.00 23.31 ? 296 GLU   A CG  1 
ATOM   2487 C CD  . GLU   A 1 294 ? -15.783 -4.393  -55.170 1.00 39.49 ? 296 GLU   A CD  1 
ATOM   2488 O OE1 . GLU   A 1 294 ? -15.543 -3.362  -54.503 1.00 26.86 ? 296 GLU   A OE1 1 
ATOM   2489 O OE2 . GLU   A 1 294 ? -16.771 -4.495  -55.936 1.00 46.65 ? 296 GLU   A OE2 1 
ATOM   2490 N N   . ALA   A 1 295 ? -12.909 -4.931  -50.883 1.00 17.35 ? 297 ALA   A N   1 
ATOM   2491 C CA  . ALA   A 1 295 ? -11.883 -5.055  -49.845 1.00 16.10 ? 297 ALA   A CA  1 
ATOM   2492 C C   . ALA   A 1 295 ? -12.414 -5.781  -48.622 1.00 17.95 ? 297 ALA   A C   1 
ATOM   2493 O O   . ALA   A 1 295 ? -11.725 -6.640  -48.055 1.00 16.27 ? 297 ALA   A O   1 
ATOM   2494 C CB  . ALA   A 1 295 ? -11.360 -3.676  -49.446 1.00 18.15 ? 297 ALA   A CB  1 
ATOM   2495 N N   . LEU   A 1 296 ? -13.634 -5.442  -48.192 1.00 18.58 ? 298 LEU   A N   1 
ATOM   2496 C CA  . LEU   A 1 296 ? -14.187 -6.063  -46.994 1.00 16.45 ? 298 LEU   A CA  1 
ATOM   2497 C C   . LEU   A 1 296 ? -14.497 -7.535  -47.226 1.00 16.14 ? 298 LEU   A C   1 
ATOM   2498 O O   . LEU   A 1 296 ? -14.263 -8.366  -46.338 1.00 16.83 ? 298 LEU   A O   1 
ATOM   2499 C CB  . LEU   A 1 296 ? -15.444 -5.326  -46.534 1.00 17.73 ? 298 LEU   A CB  1 
ATOM   2500 C CG  . LEU   A 1 296 ? -15.220 -3.878  -46.123 1.00 19.24 ? 298 LEU   A CG  1 
ATOM   2501 C CD1 . LEU   A 1 296 ? -16.499 -3.304  -45.531 1.00 20.71 ? 298 LEU   A CD1 1 
ATOM   2502 C CD2 . LEU   A 1 296 ? -14.065 -3.768  -45.136 1.00 23.92 ? 298 LEU   A CD2 1 
ATOM   2503 N N   . ASP   A 1 297 ? -15.001 -7.886  -48.404 1.00 16.62 ? 299 ASP   A N   1 
ATOM   2504 C CA  . ASP   A 1 297 ? -15.239 -9.297  -48.679 1.00 17.95 ? 299 ASP   A CA  1 
ATOM   2505 C C   . ASP   A 1 297 ? -13.930 -10.072 -48.734 1.00 18.13 ? 299 ASP   A C   1 
ATOM   2506 O O   . ASP   A 1 297 ? -13.851 -11.186 -48.209 1.00 17.33 ? 299 ASP   A O   1 
ATOM   2507 C CB  . ASP   A 1 297 ? -16.006 -9.487  -49.981 1.00 17.06 ? 299 ASP   A CB  1 
ATOM   2508 C CG  . ASP   A 1 297 ? -16.311 -10.949 -50.246 1.00 21.55 ? 299 ASP   A CG  1 
ATOM   2509 O OD1 . ASP   A 1 297 ? -17.022 -11.575 -49.424 1.00 22.52 ? 299 ASP   A OD1 1 
ATOM   2510 O OD2 . ASP   A 1 297 ? -15.831 -11.484 -51.260 1.00 23.35 ? 299 ASP   A OD2 1 
ATOM   2511 N N   . PHE   A 1 298 ? -12.910 -9.511  -49.394 1.00 15.96 ? 300 PHE   A N   1 
ATOM   2512 C CA  . PHE   A 1 298 ? -11.603 -10.157 -49.441 1.00 16.88 ? 300 PHE   A CA  1 
ATOM   2513 C C   . PHE   A 1 298 ? -11.051 -10.354 -48.036 1.00 18.57 ? 300 PHE   A C   1 
ATOM   2514 O O   . PHE   A 1 298 ? -10.612 -11.451 -47.675 1.00 14.00 ? 300 PHE   A O   1 
ATOM   2515 C CB  . PHE   A 1 298 ? -10.656 -9.321  -50.303 1.00 15.02 ? 300 PHE   A CB  1 
ATOM   2516 C CG  . PHE   A 1 298 ? -9.270  -9.887  -50.424 1.00 18.46 ? 300 PHE   A CG  1 
ATOM   2517 C CD1 . PHE   A 1 298 ? -9.072  -11.229 -50.693 1.00 17.07 ? 300 PHE   A CD1 1 
ATOM   2518 C CD2 . PHE   A 1 298 ? -8.169  -9.057  -50.326 1.00 21.26 ? 300 PHE   A CD2 1 
ATOM   2519 C CE1 . PHE   A 1 298 ? -7.793  -11.748 -50.823 1.00 18.77 ? 300 PHE   A CE1 1 
ATOM   2520 C CE2 . PHE   A 1 298 ? -6.873  -9.575  -50.452 1.00 17.75 ? 300 PHE   A CE2 1 
ATOM   2521 C CZ  . PHE   A 1 298 ? -6.696  -10.917 -50.691 1.00 19.77 ? 300 PHE   A CZ  1 
ATOM   2522 N N   . LEU   A 1 299 ? -11.085 -9.302  -47.220 1.00 15.16 ? 301 LEU   A N   1 
ATOM   2523 C CA  . LEU   A 1 299 ? -10.567 -9.415  -45.860 1.00 17.73 ? 301 LEU   A CA  1 
ATOM   2524 C C   . LEU   A 1 299 ? -11.313 -10.492 -45.090 1.00 14.67 ? 301 LEU   A C   1 
ATOM   2525 O O   . LEU   A 1 299 ? -10.706 -11.320 -44.391 1.00 15.12 ? 301 LEU   A O   1 
ATOM   2526 C CB  . LEU   A 1 299 ? -10.690 -8.072  -45.143 1.00 15.37 ? 301 LEU   A CB  1 
ATOM   2527 C CG  . LEU   A 1 299 ? -10.182 -8.080  -43.701 1.00 16.01 ? 301 LEU   A CG  1 
ATOM   2528 C CD1 . LEU   A 1 299 ? -8.667  -8.367  -43.647 1.00 13.30 ? 301 LEU   A CD1 1 
ATOM   2529 C CD2 . LEU   A 1 299 ? -10.499 -6.749  -43.018 1.00 19.32 ? 301 LEU   A CD2 1 
ATOM   2530 N N   . ASP   A 1 300 ? -12.639 -10.488 -45.219 1.00 14.14 ? 302 ASP   A N   1 
ATOM   2531 C CA  . ASP   A 1 300 ? -13.482 -11.457 -44.541 1.00 15.15 ? 302 ASP   A CA  1 
ATOM   2532 C C   . ASP   A 1 300 ? -13.114 -12.886 -44.900 1.00 19.78 ? 302 ASP   A C   1 
ATOM   2533 O O   . ASP   A 1 300 ? -13.258 -13.782 -44.067 1.00 16.68 ? 302 ASP   A O   1 
ATOM   2534 C CB  . ASP   A 1 300 ? -14.936 -11.192 -44.906 1.00 14.69 ? 302 ASP   A CB  1 
ATOM   2535 C CG  . ASP   A 1 300 ? -15.905 -11.986 -44.060 1.00 21.13 ? 302 ASP   A CG  1 
ATOM   2536 O OD1 . ASP   A 1 300 ? -15.769 -11.967 -42.822 1.00 20.34 ? 302 ASP   A OD1 1 
ATOM   2537 O OD2 . ASP   A 1 300 ? -16.821 -12.602 -44.657 1.00 24.97 ? 302 ASP   A OD2 1 
ATOM   2538 N N   . LYS   A 1 301 ? -12.682 -13.127 -46.139 1.00 15.00 ? 303 LYS   A N   1 
ATOM   2539 C CA  . LYS   A 1 301 ? -12.333 -14.472 -46.581 1.00 15.30 ? 303 LYS   A CA  1 
ATOM   2540 C C   . LYS   A 1 301 ? -10.907 -14.889 -46.221 1.00 15.11 ? 303 LYS   A C   1 
ATOM   2541 O O   . LYS   A 1 301 ? -10.584 -16.075 -46.344 1.00 16.54 ? 303 LYS   A O   1 
ATOM   2542 C CB  . LYS   A 1 301 ? -12.557 -14.582 -48.092 1.00 15.38 ? 303 LYS   A CB  1 
ATOM   2543 C CG  . LYS   A 1 301 ? -14.064 -14.565 -48.416 1.00 19.19 ? 303 LYS   A CG  1 
ATOM   2544 C CD  . LYS   A 1 301 ? -14.308 -14.330 -49.893 1.00 23.32 ? 303 LYS   A CD  1 
ATOM   2545 C CE  . LYS   A 1 301 ? -15.689 -14.824 -50.330 1.00 25.52 ? 303 LYS   A CE  1 
ATOM   2546 N NZ  . LYS   A 1 301 ? -16.800 -14.236 -49.513 1.00 32.01 ? 303 LYS   A NZ  1 
ATOM   2547 N N   . LEU   A 1 302 ? -10.051 -13.953 -45.800 1.00 13.97 ? 304 LEU   A N   1 
ATOM   2548 C CA  . LEU   A 1 302 ? -8.737  -14.285 -45.260 1.00 13.57 ? 304 LEU   A CA  1 
ATOM   2549 C C   . LEU   A 1 302 ? -8.803  -14.557 -43.772 1.00 15.85 ? 304 LEU   A C   1 
ATOM   2550 O O   . LEU   A 1 302 ? -8.181  -15.506 -43.281 1.00 13.32 ? 304 LEU   A O   1 
ATOM   2551 C CB  . LEU   A 1 302 ? -7.757  -13.137 -45.500 1.00 13.05 ? 304 LEU   A CB  1 
ATOM   2552 C CG  . LEU   A 1 302 ? -7.384  -12.809 -46.947 1.00 14.47 ? 304 LEU   A CG  1 
ATOM   2553 C CD1 . LEU   A 1 302 ? -6.551  -11.540 -46.998 1.00 17.61 ? 304 LEU   A CD1 1 
ATOM   2554 C CD2 . LEU   A 1 302 ? -6.608  -13.954 -47.594 1.00 16.27 ? 304 LEU   A CD2 1 
ATOM   2555 N N   . LEU   A 1 303 ? -9.534  -13.720 -43.034 1.00 14.61 ? 305 LEU   A N   1 
ATOM   2556 C CA  . LEU   A 1 303 ? -9.531  -13.798 -41.574 1.00 13.41 ? 305 LEU   A CA  1 
ATOM   2557 C C   . LEU   A 1 303 ? -10.625 -14.759 -41.113 1.00 14.22 ? 305 LEU   A C   1 
ATOM   2558 O O   . LEU   A 1 303 ? -11.701 -14.362 -40.642 1.00 16.93 ? 305 LEU   A O   1 
ATOM   2559 C CB  . LEU   A 1 303 ? -9.689  -12.415 -40.958 1.00 15.57 ? 305 LEU   A CB  1 
ATOM   2560 C CG  . LEU   A 1 303 ? -8.507  -11.475 -41.207 1.00 12.99 ? 305 LEU   A CG  1 
ATOM   2561 C CD1 . LEU   A 1 303 ? -8.723  -10.156 -40.470 1.00 15.22 ? 305 LEU   A CD1 1 
ATOM   2562 C CD2 . LEU   A 1 303 ? -7.190  -12.120 -40.753 1.00 14.92 ? 305 LEU   A CD2 1 
ATOM   2563 N N   . ARG   A 1 304 ? -10.349 -16.056 -41.264 1.00 13.51 ? 306 ARG   A N   1 
ATOM   2564 C CA  . ARG   A 1 304 ? -11.201 -17.119 -40.727 1.00 12.65 ? 306 ARG   A CA  1 
ATOM   2565 C C   . ARG   A 1 304 ? -10.448 -17.838 -39.623 1.00 12.55 ? 306 ARG   A C   1 
ATOM   2566 O O   . ARG   A 1 304 ? -9.246  -18.086 -39.761 1.00 12.72 ? 306 ARG   A O   1 
ATOM   2567 C CB  . ARG   A 1 304 ? -11.566 -18.171 -41.784 1.00 15.81 ? 306 ARG   A CB  1 
ATOM   2568 C CG  . ARG   A 1 304 ? -11.886 -17.651 -43.147 1.00 18.68 ? 306 ARG   A CG  1 
ATOM   2569 C CD  . ARG   A 1 304 ? -13.057 -16.702 -43.131 1.00 17.05 ? 306 ARG   A CD  1 
ATOM   2570 N NE  . ARG   A 1 304 ? -14.253 -17.244 -42.505 1.00 19.39 ? 306 ARG   A NE  1 
ATOM   2571 C CZ  . ARG   A 1 304 ? -15.375 -16.553 -42.393 1.00 23.52 ? 306 ARG   A CZ  1 
ATOM   2572 N NH1 . ARG   A 1 304 ? -16.434 -17.090 -41.803 1.00 24.35 ? 306 ARG   A NH1 1 
ATOM   2573 N NH2 . ARG   A 1 304 ? -15.431 -15.319 -42.880 1.00 23.14 ? 306 ARG   A NH2 1 
ATOM   2574 N N   . TYR   A 1 305 ? -11.142 -18.213 -38.551 1.00 13.56 ? 307 TYR   A N   1 
ATOM   2575 C CA  . TYR   A 1 305 ? -10.505 -19.067 -37.547 1.00 12.66 ? 307 TYR   A CA  1 
ATOM   2576 C C   . TYR   A 1 305 ? -9.993  -20.350 -38.182 1.00 14.68 ? 307 TYR   A C   1 
ATOM   2577 O O   . TYR   A 1 305 ? -8.818  -20.715 -38.029 1.00 13.81 ? 307 TYR   A O   1 
ATOM   2578 C CB  . TYR   A 1 305 ? -11.490 -19.442 -36.445 1.00 13.35 ? 307 TYR   A CB  1 
ATOM   2579 C CG  . TYR   A 1 305 ? -11.831 -18.384 -35.432 1.00 11.58 ? 307 TYR   A CG  1 
ATOM   2580 C CD1 . TYR   A 1 305 ? -10.867 -17.883 -34.561 1.00 13.45 ? 307 TYR   A CD1 1 
ATOM   2581 C CD2 . TYR   A 1 305 ? -13.135 -17.929 -35.312 1.00 13.78 ? 307 TYR   A CD2 1 
ATOM   2582 C CE1 . TYR   A 1 305 ? -11.187 -16.924 -33.610 1.00 12.08 ? 307 TYR   A CE1 1 
ATOM   2583 C CE2 . TYR   A 1 305 ? -13.469 -16.988 -34.369 1.00 13.04 ? 307 TYR   A CE2 1 
ATOM   2584 C CZ  . TYR   A 1 305 ? -12.499 -16.491 -33.507 1.00 13.75 ? 307 TYR   A CZ  1 
ATOM   2585 O OH  . TYR   A 1 305 ? -12.822 -15.554 -32.555 1.00 15.14 ? 307 TYR   A OH  1 
ATOM   2586 N N   . ASP   A 1 306 ? -10.866 -21.041 -38.915 1.00 13.08 ? 308 ASP   A N   1 
ATOM   2587 C CA  . ASP   A 1 306 ? -10.526 -22.334 -39.495 1.00 14.12 ? 308 ASP   A CA  1 
ATOM   2588 C C   . ASP   A 1 306 ? -9.527  -22.130 -40.620 1.00 13.99 ? 308 ASP   A C   1 
ATOM   2589 O O   . ASP   A 1 306 ? -9.860  -21.565 -41.666 1.00 15.50 ? 308 ASP   A O   1 
ATOM   2590 C CB  . ASP   A 1 306 ? -11.772 -23.035 -40.013 1.00 13.03 ? 308 ASP   A CB  1 
ATOM   2591 C CG  . ASP   A 1 306 ? -11.532 -24.497 -40.309 1.00 17.23 ? 308 ASP   A CG  1 
ATOM   2592 O OD1 . ASP   A 1 306 ? -10.358 -24.908 -40.443 1.00 18.16 ? 308 ASP   A OD1 1 
ATOM   2593 O OD2 . ASP   A 1 306 ? -12.530 -25.240 -40.385 1.00 21.13 ? 308 ASP   A OD2 1 
ATOM   2594 N N   . HIS   A 1 307 ? -8.294  -22.584 -40.394 1.00 13.06 ? 309 HIS   A N   1 
ATOM   2595 C CA  . HIS   A 1 307 ? -7.255  -22.450 -41.412 1.00 13.43 ? 309 HIS   A CA  1 
ATOM   2596 C C   . HIS   A 1 307 ? -7.665  -23.116 -42.722 1.00 14.97 ? 309 HIS   A C   1 
ATOM   2597 O O   . HIS   A 1 307 ? -7.287  -22.642 -43.803 1.00 15.41 ? 309 HIS   A O   1 
ATOM   2598 C CB  . HIS   A 1 307 ? -5.937  -23.020 -40.876 1.00 15.00 ? 309 HIS   A CB  1 
ATOM   2599 C CG  . HIS   A 1 307 ? -6.051  -24.419 -40.336 1.00 15.38 ? 309 HIS   A CG  1 
ATOM   2600 N ND1 . HIS   A 1 307 ? -6.510  -24.702 -39.065 1.00 13.73 ? 309 HIS   A ND1 1 
ATOM   2601 C CD2 . HIS   A 1 307 ? -5.739  -25.615 -40.896 1.00 18.47 ? 309 HIS   A CD2 1 
ATOM   2602 C CE1 . HIS   A 1 307 ? -6.508  -26.011 -38.878 1.00 15.77 ? 309 HIS   A CE1 1 
ATOM   2603 N NE2 . HIS   A 1 307 ? -6.040  -26.587 -39.971 1.00 16.89 ? 309 HIS   A NE2 1 
ATOM   2604 N N   . GLN   A 1 308 ? -8.506  -24.156 -42.655 1.00 14.09 ? 310 GLN   A N   1 
ATOM   2605 C CA  . GLN   A 1 308 ? -8.973  -24.828 -43.860 1.00 14.43 ? 310 GLN   A CA  1 
ATOM   2606 C C   . GLN   A 1 308 ? -9.983  -24.007 -44.651 1.00 17.73 ? 310 GLN   A C   1 
ATOM   2607 O O   . GLN   A 1 308 ? -10.242 -24.333 -45.812 1.00 21.82 ? 310 GLN   A O   1 
ATOM   2608 C CB  . GLN   A 1 308 ? -9.592  -26.189 -43.510 1.00 16.56 ? 310 GLN   A CB  1 
ATOM   2609 C CG  . GLN   A 1 308 ? -8.554  -27.226 -43.103 1.00 18.98 ? 310 GLN   A CG  1 
ATOM   2610 C CD  . GLN   A 1 308 ? -9.170  -28.568 -42.733 1.00 22.62 ? 310 GLN   A CD  1 
ATOM   2611 O OE1 . GLN   A 1 308 ? -10.369 -28.785 -42.911 1.00 23.48 ? 310 GLN   A OE1 1 
ATOM   2612 N NE2 . GLN   A 1 308 ? -8.346  -29.472 -42.212 1.00 22.57 ? 310 GLN   A NE2 1 
ATOM   2613 N N   . SER   A 1 309 ? -10.548 -22.959 -44.060 1.00 15.85 ? 311 SER   A N   1 
ATOM   2614 C CA  . SER   A 1 309 ? -11.560 -22.136 -44.700 1.00 17.31 ? 311 SER   A CA  1 
ATOM   2615 C C   . SER   A 1 309 ? -11.011 -20.877 -45.351 1.00 15.79 ? 311 SER   A C   1 
ATOM   2616 O O   . SER   A 1 309 ? -11.752 -20.203 -46.073 1.00 17.21 ? 311 SER   A O   1 
ATOM   2617 C CB  . SER   A 1 309 ? -12.607 -21.733 -43.667 1.00 17.55 ? 311 SER   A CB  1 
ATOM   2618 O OG  . SER   A 1 309 ? -13.315 -22.882 -43.235 1.00 21.81 ? 311 SER   A OG  1 
ATOM   2619 N N   . ARG   A 1 310 ? -9.752  -20.530 -45.104 1.00 14.13 ? 312 ARG   A N   1 
ATOM   2620 C CA  . ARG   A 1 310 ? -9.201  -19.302 -45.660 1.00 14.65 ? 312 ARG   A CA  1 
ATOM   2621 C C   . ARG   A 1 310 ? -8.954  -19.448 -47.155 1.00 13.20 ? 312 ARG   A C   1 
ATOM   2622 O O   . ARG   A 1 310 ? -8.659  -20.541 -47.647 1.00 15.88 ? 312 ARG   A O   1 
ATOM   2623 C CB  . ARG   A 1 310 ? -7.882  -18.961 -44.959 1.00 13.94 ? 312 ARG   A CB  1 
ATOM   2624 C CG  . ARG   A 1 310 ? -8.037  -18.768 -43.455 1.00 12.87 ? 312 ARG   A CG  1 
ATOM   2625 C CD  . ARG   A 1 310 ? -6.696  -18.538 -42.750 1.00 12.25 ? 312 ARG   A CD  1 
ATOM   2626 N NE  . ARG   A 1 310 ? -6.890  -18.787 -41.319 1.00 13.00 ? 312 ARG   A NE  1 
ATOM   2627 C CZ  . ARG   A 1 310 ? -5.993  -19.313 -40.492 1.00 11.85 ? 312 ARG   A CZ  1 
ATOM   2628 N NH1 . ARG   A 1 310 ? -4.753  -19.602 -40.913 1.00 11.06 ? 312 ARG   A NH1 1 
ATOM   2629 N NH2 . ARG   A 1 310 ? -6.331  -19.533 -39.232 1.00 13.32 ? 312 ARG   A NH2 1 
ATOM   2630 N N   . LEU   A 1 311 ? -9.056  -18.325 -47.877 1.00 14.64 ? 313 LEU   A N   1 
ATOM   2631 C CA  . LEU   A 1 311 ? -8.570  -18.287 -49.256 1.00 14.77 ? 313 LEU   A CA  1 
ATOM   2632 C C   . LEU   A 1 311 ? -7.137  -18.794 -49.333 1.00 15.39 ? 313 LEU   A C   1 
ATOM   2633 O O   . LEU   A 1 311 ? -6.297  -18.485 -48.475 1.00 14.39 ? 313 LEU   A O   1 
ATOM   2634 C CB  . LEU   A 1 311 ? -8.618  -16.862 -49.829 1.00 14.56 ? 313 LEU   A CB  1 
ATOM   2635 C CG  . LEU   A 1 311 ? -9.995  -16.234 -50.048 1.00 18.57 ? 313 LEU   A CG  1 
ATOM   2636 C CD1 . LEU   A 1 311 ? -9.795  -14.825 -50.564 1.00 22.17 ? 313 LEU   A CD1 1 
ATOM   2637 C CD2 . LEU   A 1 311 ? -10.784 -17.061 -51.041 1.00 23.46 ? 313 LEU   A CD2 1 
ATOM   2638 N N   . THR   A 1 312 ? -6.860  -19.590 -50.360 1.00 14.38 ? 314 THR   A N   1 
ATOM   2639 C CA  . THR   A 1 312 ? -5.475  -19.837 -50.729 1.00 15.28 ? 314 THR   A CA  1 
ATOM   2640 C C   . THR   A 1 312 ? -4.925  -18.624 -51.469 1.00 15.23 ? 314 THR   A C   1 
ATOM   2641 O O   . THR   A 1 312 ? -5.663  -17.745 -51.918 1.00 16.72 ? 314 THR   A O   1 
ATOM   2642 C CB  . THR   A 1 312 ? -5.338  -21.087 -51.600 1.00 16.23 ? 314 THR   A CB  1 
ATOM   2643 O OG1 . THR   A 1 312 ? -5.956  -20.855 -52.871 1.00 17.76 ? 314 THR   A OG1 1 
ATOM   2644 C CG2 . THR   A 1 312 ? -5.969  -22.313 -50.913 1.00 19.06 ? 314 THR   A CG2 1 
ATOM   2645 N N   . ALA   A 1 313 ? -3.600  -18.592 -51.619 1.00 14.51 ? 315 ALA   A N   1 
ATOM   2646 C CA  . ALA   A 1 313 ? -2.999  -17.470 -52.323 1.00 15.26 ? 315 ALA   A CA  1 
ATOM   2647 C C   . ALA   A 1 313 ? -3.526  -17.348 -53.747 1.00 14.48 ? 315 ALA   A C   1 
ATOM   2648 O O   . ALA   A 1 313 ? -3.821  -16.240 -54.202 1.00 16.57 ? 315 ALA   A O   1 
ATOM   2649 C CB  . ALA   A 1 313 ? -1.476  -17.608 -52.324 1.00 14.34 ? 315 ALA   A CB  1 
ATOM   2650 N N   . ARG   A 1 314 ? -3.645  -18.475 -54.463 1.00 17.03 ? 316 ARG   A N   1 
ATOM   2651 C CA  . ARG   A 1 314 ? -4.157  -18.440 -55.831 1.00 19.46 ? 316 ARG   A CA  1 
ATOM   2652 C C   . ARG   A 1 314 ? -5.611  -18.000 -55.858 1.00 19.43 ? 316 ARG   A C   1 
ATOM   2653 O O   . ARG   A 1 314 ? -6.011  -17.182 -56.698 1.00 21.52 ? 316 ARG   A O   1 
ATOM   2654 C CB  . ARG   A 1 314 ? -4.012  -19.808 -56.489 1.00 22.64 ? 316 ARG   A CB  1 
ATOM   2655 C CG  . ARG   A 1 314 ? -4.449  -19.786 -57.940 1.00 35.11 ? 316 ARG   A CG  1 
ATOM   2656 C CD  . ARG   A 1 314 ? -3.514  -18.935 -58.779 1.00 46.15 ? 316 ARG   A CD  1 
ATOM   2657 N NE  . ARG   A 1 314 ? -2.385  -19.723 -59.249 1.00 50.28 ? 316 ARG   A NE  1 
ATOM   2658 C CZ  . ARG   A 1 314 ? -2.274  -20.202 -60.483 1.00 45.98 ? 316 ARG   A CZ  1 
ATOM   2659 N NH1 . ARG   A 1 314 ? -1.212  -20.919 -60.818 1.00 46.38 ? 316 ARG   A NH1 1 
ATOM   2660 N NH2 . ARG   A 1 314 ? -3.213  -19.950 -61.385 1.00 37.56 ? 316 ARG   A NH2 1 
ATOM   2661 N N   . GLU   A 1 315 ? -6.432  -18.557 -54.961 1.00 20.70 ? 317 GLU   A N   1 
ATOM   2662 C CA  . GLU   A 1 315 ? -7.819  -18.104 -54.874 1.00 20.17 ? 317 GLU   A CA  1 
ATOM   2663 C C   . GLU   A 1 315 ? -7.886  -16.614 -54.599 1.00 17.46 ? 317 GLU   A C   1 
ATOM   2664 O O   . GLU   A 1 315 ? -8.711  -15.902 -55.180 1.00 22.65 ? 317 GLU   A O   1 
ATOM   2665 C CB  . GLU   A 1 315 ? -8.571  -18.845 -53.776 1.00 21.00 ? 317 GLU   A CB  1 
ATOM   2666 C CG  . GLU   A 1 315 ? -8.916  -20.270 -54.062 1.00 24.55 ? 317 GLU   A CG  1 
ATOM   2667 C CD  . GLU   A 1 315 ? -9.706  -20.862 -52.918 1.00 22.39 ? 317 GLU   A CD  1 
ATOM   2668 O OE1 . GLU   A 1 315 ? -9.287  -20.727 -51.742 1.00 19.47 ? 317 GLU   A OE1 1 
ATOM   2669 O OE2 . GLU   A 1 315 ? -10.771 -21.442 -53.196 1.00 23.06 ? 317 GLU   A OE2 1 
ATOM   2670 N N   . ALA   A 1 316 ? -7.020  -16.121 -53.707 1.00 18.73 ? 318 ALA   A N   1 
ATOM   2671 C CA  . ALA   A 1 316 ? -7.044  -14.705 -53.379 1.00 14.93 ? 318 ALA   A CA  1 
ATOM   2672 C C   . ALA   A 1 316 ? -6.754  -13.854 -54.610 1.00 19.51 ? 318 ALA   A C   1 
ATOM   2673 O O   . ALA   A 1 316 ? -7.356  -12.790 -54.797 1.00 18.01 ? 318 ALA   A O   1 
ATOM   2674 C CB  . ALA   A 1 316 ? -6.034  -14.412 -52.264 1.00 15.73 ? 318 ALA   A CB  1 
ATOM   2675 N N   . MET   A 1 317 ? -5.826  -14.301 -55.463 1.00 18.05 ? 319 MET   A N   1 
ATOM   2676 C CA  A MET   A 1 317 ? -5.515  -13.512 -56.647 0.34 20.29 ? 319 MET   A CA  1 
ATOM   2677 C CA  B MET   A 1 317 ? -5.491  -13.563 -56.676 0.66 21.26 ? 319 MET   A CA  1 
ATOM   2678 C C   . MET   A 1 317 ? -6.657  -13.499 -57.655 1.00 16.60 ? 319 MET   A C   1 
ATOM   2679 O O   . MET   A 1 317 ? -6.665  -12.635 -58.538 1.00 20.98 ? 319 MET   A O   1 
ATOM   2680 C CB  A MET   A 1 317 ? -4.230  -14.013 -57.298 0.34 18.71 ? 319 MET   A CB  1 
ATOM   2681 C CB  B MET   A 1 317 ? -4.269  -14.196 -57.344 0.66 16.21 ? 319 MET   A CB  1 
ATOM   2682 C CG  A MET   A 1 317 ? -3.005  -13.695 -56.457 0.34 15.24 ? 319 MET   A CG  1 
ATOM   2683 C CG  B MET   A 1 317 ? -3.051  -14.224 -56.417 0.66 17.87 ? 319 MET   A CG  1 
ATOM   2684 S SD  A MET   A 1 317 ? -1.453  -14.153 -57.229 0.34 19.97 ? 319 MET   A SD  1 
ATOM   2685 S SD  B MET   A 1 317 ? -1.598  -15.062 -57.068 0.66 17.62 ? 319 MET   A SD  1 
ATOM   2686 C CE  A MET   A 1 317 ? -1.931  -15.683 -58.022 0.34 19.29 ? 319 MET   A CE  1 
ATOM   2687 C CE  B MET   A 1 317 ? -1.199  -13.957 -58.420 0.66 22.96 ? 319 MET   A CE  1 
ATOM   2688 N N   . GLU   A 1 318 ? -7.635  -14.407 -57.525 1.00 18.37 ? 320 GLU   A N   1 
ATOM   2689 C CA  . GLU   A 1 318 ? -8.830  -14.379 -58.363 1.00 19.42 ? 320 GLU   A CA  1 
ATOM   2690 C C   . GLU   A 1 318 ? -9.893  -13.412 -57.844 1.00 19.96 ? 320 GLU   A C   1 
ATOM   2691 O O   . GLU   A 1 318 ? -10.918 -13.230 -58.514 1.00 20.88 ? 320 GLU   A O   1 
ATOM   2692 C CB  . GLU   A 1 318 ? -9.456  -15.780 -58.457 1.00 23.69 ? 320 GLU   A CB  1 
ATOM   2693 C CG  . GLU   A 1 318 ? -8.563  -16.909 -58.982 1.00 21.09 ? 320 GLU   A CG  1 
ATOM   2694 C CD  . GLU   A 1 318 ? -8.376  -16.904 -60.483 1.00 26.19 ? 320 GLU   A CD  1 
ATOM   2695 O OE1 . GLU   A 1 318 ? -9.356  -17.148 -61.224 1.00 30.88 ? 320 GLU   A OE1 1 
ATOM   2696 O OE2 . GLU   A 1 318 ? -7.228  -16.677 -60.923 1.00 26.60 ? 320 GLU   A OE2 1 
ATOM   2697 N N   . HIS   A 1 319 ? -9.686  -12.789 -56.676 1.00 18.40 ? 321 HIS   A N   1 
ATOM   2698 C CA  . HIS   A 1 319 ? -10.772 -12.070 -56.017 1.00 21.61 ? 321 HIS   A CA  1 
ATOM   2699 C C   . HIS   A 1 319 ? -11.065 -10.745 -56.728 1.00 21.75 ? 321 HIS   A C   1 
ATOM   2700 O O   . HIS   A 1 319 ? -10.145 -10.079 -57.214 1.00 20.53 ? 321 HIS   A O   1 
ATOM   2701 C CB  . HIS   A 1 319 ? -10.429 -11.809 -54.545 1.00 19.08 ? 321 HIS   A CB  1 
ATOM   2702 C CG  . HIS   A 1 319 ? -11.588 -11.313 -53.748 1.00 17.99 ? 321 HIS   A CG  1 
ATOM   2703 N ND1 . HIS   A 1 319 ? -11.973 -9.990  -53.744 1.00 20.82 ? 321 HIS   A ND1 1 
ATOM   2704 C CD2 . HIS   A 1 319 ? -12.463 -11.967 -52.949 1.00 18.89 ? 321 HIS   A CD2 1 
ATOM   2705 C CE1 . HIS   A 1 319 ? -13.047 -9.852  -52.983 1.00 19.92 ? 321 HIS   A CE1 1 
ATOM   2706 N NE2 . HIS   A 1 319 ? -13.358 -11.034 -52.483 1.00 20.33 ? 321 HIS   A NE2 1 
ATOM   2707 N N   . PRO   A 1 320 ? -12.334 -10.329 -56.779 1.00 18.54 ? 322 PRO   A N   1 
ATOM   2708 C CA  . PRO   A 1 320 ? -12.683 -9.048  -57.427 1.00 20.29 ? 322 PRO   A CA  1 
ATOM   2709 C C   . PRO   A 1 320 ? -11.946 -7.822  -56.906 1.00 18.81 ? 322 PRO   A C   1 
ATOM   2710 O O   . PRO   A 1 320 ? -11.860 -6.826  -57.640 1.00 23.03 ? 322 PRO   A O   1 
ATOM   2711 C CB  . PRO   A 1 320 ? -14.191 -8.937  -57.157 1.00 21.63 ? 322 PRO   A CB  1 
ATOM   2712 C CG  . PRO   A 1 320 ? -14.641 -10.358 -57.158 1.00 21.57 ? 322 PRO   A CG  1 
ATOM   2713 C CD  . PRO   A 1 320 ? -13.539 -11.110 -56.440 1.00 19.26 ? 322 PRO   A CD  1 
ATOM   2714 N N   . TYR   A 1 321 ? -11.422 -7.848  -55.674 1.00 18.83 ? 323 TYR   A N   1 
ATOM   2715 C CA  . TYR   A 1 321 ? -10.623 -6.734  -55.173 1.00 17.35 ? 323 TYR   A CA  1 
ATOM   2716 C C   . TYR   A 1 321 ? -9.486  -6.368  -56.127 1.00 16.15 ? 323 TYR   A C   1 
ATOM   2717 O O   . TYR   A 1 321 ? -9.090  -5.201  -56.205 1.00 18.67 ? 323 TYR   A O   1 
ATOM   2718 C CB  . TYR   A 1 321 ? -10.091 -7.108  -53.778 1.00 18.03 ? 323 TYR   A CB  1 
ATOM   2719 C CG  . TYR   A 1 321 ? -9.225  -6.106  -53.040 1.00 18.10 ? 323 TYR   A CG  1 
ATOM   2720 C CD1 . TYR   A 1 321 ? -9.710  -4.862  -52.665 1.00 18.27 ? 323 TYR   A CD1 1 
ATOM   2721 C CD2 . TYR   A 1 321 ? -7.941  -6.447  -52.650 1.00 20.40 ? 323 TYR   A CD2 1 
ATOM   2722 C CE1 . TYR   A 1 321 ? -8.946  -3.979  -51.951 1.00 16.23 ? 323 TYR   A CE1 1 
ATOM   2723 C CE2 . TYR   A 1 321 ? -7.164  -5.564  -51.942 1.00 18.17 ? 323 TYR   A CE2 1 
ATOM   2724 C CZ  . TYR   A 1 321 ? -7.668  -4.333  -51.594 1.00 22.46 ? 323 TYR   A CZ  1 
ATOM   2725 O OH  . TYR   A 1 321 ? -6.887  -3.459  -50.885 1.00 21.24 ? 323 TYR   A OH  1 
ATOM   2726 N N   . PHE   A 1 322 ? -8.972  -7.336  -56.875 1.00 19.86 ? 324 PHE   A N   1 
ATOM   2727 C CA  . PHE   A 1 322 ? -7.828  -7.100  -57.742 1.00 18.44 ? 324 PHE   A CA  1 
ATOM   2728 C C   . PHE   A 1 322 ? -8.220  -6.798  -59.175 1.00 18.02 ? 324 PHE   A C   1 
ATOM   2729 O O   . PHE   A 1 322 ? -7.337  -6.601  -60.011 1.00 18.31 ? 324 PHE   A O   1 
ATOM   2730 C CB  . PHE   A 1 322 ? -6.874  -8.301  -57.686 1.00 16.56 ? 324 PHE   A CB  1 
ATOM   2731 C CG  . PHE   A 1 322 ? -6.322  -8.539  -56.317 1.00 19.96 ? 324 PHE   A CG  1 
ATOM   2732 C CD1 . PHE   A 1 322 ? -5.436  -7.630  -55.762 1.00 17.26 ? 324 PHE   A CD1 1 
ATOM   2733 C CD2 . PHE   A 1 322 ? -6.731  -9.631  -55.562 1.00 18.86 ? 324 PHE   A CD2 1 
ATOM   2734 C CE1 . PHE   A 1 322 ? -4.921  -7.817  -54.494 1.00 18.01 ? 324 PHE   A CE1 1 
ATOM   2735 C CE2 . PHE   A 1 322 ? -6.232  -9.826  -54.286 1.00 20.47 ? 324 PHE   A CE2 1 
ATOM   2736 C CZ  . PHE   A 1 322 ? -5.333  -8.909  -53.748 1.00 17.36 ? 324 PHE   A CZ  1 
ATOM   2737 N N   . TYR   A 1 323 ? -9.517  -6.712  -59.473 1.00 21.21 ? 325 TYR   A N   1 
ATOM   2738 C CA  . TYR   A 1 323 ? -9.925  -6.400  -60.836 1.00 17.90 ? 325 TYR   A CA  1 
ATOM   2739 C C   . TYR   A 1 323 ? -9.414  -5.035  -61.295 1.00 18.11 ? 325 TYR   A C   1 
ATOM   2740 O O   . TYR   A 1 323 ? -9.137  -4.860  -62.483 1.00 21.25 ? 325 TYR   A O   1 
ATOM   2741 C CB  . TYR   A 1 323 ? -11.451 -6.450  -60.960 1.00 21.37 ? 325 TYR   A CB  1 
ATOM   2742 C CG  . TYR   A 1 323 ? -12.098 -7.826  -60.885 1.00 21.36 ? 325 TYR   A CG  1 
ATOM   2743 C CD1 . TYR   A 1 323 ? -11.341 -8.998  -60.850 1.00 22.29 ? 325 TYR   A CD1 1 
ATOM   2744 C CD2 . TYR   A 1 323 ? -13.481 -7.943  -60.854 1.00 24.21 ? 325 TYR   A CD2 1 
ATOM   2745 C CE1 . TYR   A 1 323 ? -11.954 -10.247 -60.785 1.00 22.37 ? 325 TYR   A CE1 1 
ATOM   2746 C CE2 . TYR   A 1 323 ? -14.098 -9.177  -60.783 1.00 29.69 ? 325 TYR   A CE2 1 
ATOM   2747 C CZ  . TYR   A 1 323 ? -13.341 -10.325 -60.758 1.00 29.49 ? 325 TYR   A CZ  1 
ATOM   2748 O OH  . TYR   A 1 323 ? -13.990 -11.542 -60.685 1.00 26.92 ? 325 TYR   A OH  1 
ATOM   2749 N N   . THR   A 1 324 ? -9.288  -4.056  -60.378 1.00 22.02 ? 326 THR   A N   1 
ATOM   2750 C CA  . THR   A 1 324 ? -8.834  -2.729  -60.796 1.00 23.18 ? 326 THR   A CA  1 
ATOM   2751 C C   . THR   A 1 324 ? -7.322  -2.636  -60.958 1.00 21.73 ? 326 THR   A C   1 
ATOM   2752 O O   . THR   A 1 324 ? -6.842  -1.675  -61.573 1.00 25.76 ? 326 THR   A O   1 
ATOM   2753 C CB  . THR   A 1 324 ? -9.282  -1.649  -59.807 1.00 26.59 ? 326 THR   A CB  1 
ATOM   2754 O OG1 . THR   A 1 324 ? -9.053  -0.353  -60.380 1.00 33.76 ? 326 THR   A OG1 1 
ATOM   2755 C CG2 . THR   A 1 324 ? -8.504  -1.743  -58.528 1.00 27.16 ? 326 THR   A CG2 1 
ATOM   2756 N N   . VAL   A 1 325 ? -6.575  -3.621  -60.479 1.00 21.21 ? 327 VAL   A N   1 
ATOM   2757 C CA  . VAL   A 1 325 ? -5.116  -3.591  -60.581 1.00 20.45 ? 327 VAL   A CA  1 
ATOM   2758 C C   . VAL   A 1 325 ? -4.706  -3.912  -62.007 1.00 19.27 ? 327 VAL   A C   1 
ATOM   2759 O O   . VAL   A 1 325 ? -5.116  -4.936  -62.567 1.00 20.39 ? 327 VAL   A O   1 
ATOM   2760 C CB  . VAL   A 1 325 ? -4.486  -4.587  -59.601 1.00 17.56 ? 327 VAL   A CB  1 
ATOM   2761 C CG1 . VAL   A 1 325 ? -2.980  -4.742  -59.841 1.00 19.06 ? 327 VAL   A CG1 1 
ATOM   2762 C CG2 . VAL   A 1 325 ? -4.738  -4.143  -58.187 1.00 25.84 ? 327 VAL   A CG2 1 
ATOM   2763 N N   . VAL   A 1 326 ? -3.890  -3.037  -62.600 1.00 20.45 ? 328 VAL   A N   1 
ATOM   2764 C CA  . VAL   A 1 326 ? -3.418  -3.260  -63.957 1.00 23.09 ? 328 VAL   A CA  1 
ATOM   2765 C C   . VAL   A 1 326 ? -2.544  -4.498  -63.983 1.00 21.16 ? 328 VAL   A C   1 
ATOM   2766 O O   . VAL   A 1 326 ? -1.566  -4.599  -63.229 1.00 21.65 ? 328 VAL   A O   1 
ATOM   2767 C CB  . VAL   A 1 326 ? -2.633  -2.046  -64.475 1.00 29.96 ? 328 VAL   A CB  1 
ATOM   2768 C CG1 . VAL   A 1 326 ? -1.961  -2.395  -65.787 1.00 34.63 ? 328 VAL   A CG1 1 
ATOM   2769 C CG2 . VAL   A 1 326 ? -3.541  -0.845  -64.643 1.00 37.86 ? 328 VAL   A CG2 1 
ATOM   2770 N N   . LYS   A 1 327 ? -2.874  -5.433  -64.866 1.00 25.12 ? 329 LYS   A N   1 
ATOM   2771 C CA  . LYS   A 1 327 ? -2.082  -6.648  -64.978 1.00 31.67 ? 329 LYS   A CA  1 
ATOM   2772 C C   . LYS   A 1 327 ? -0.976  -6.472  -66.012 1.00 49.30 ? 329 LYS   A C   1 
ATOM   2773 O O   . LYS   A 1 327 ? -1.083  -5.663  -66.937 1.00 49.32 ? 329 LYS   A O   1 
ATOM   2774 C CB  . LYS   A 1 327 ? -2.961  -7.847  -65.341 1.00 40.04 ? 329 LYS   A CB  1 
ATOM   2775 C CG  . LYS   A 1 327 ? -4.043  -8.160  -64.309 1.00 46.10 ? 329 LYS   A CG  1 
ATOM   2776 C CD  . LYS   A 1 327 ? -3.491  -8.174  -62.881 1.00 37.92 ? 329 LYS   A CD  1 
ATOM   2777 C CE  . LYS   A 1 327 ? -4.600  -8.451  -61.850 1.00 29.13 ? 329 LYS   A CE  1 
ATOM   2778 N NZ  . LYS   A 1 327 ? -5.849  -7.635  -62.067 1.00 29.94 ? 329 LYS   A NZ  1 
ATOM   2779 N N   . ASP   A 1 328 ? 0.098   -7.235  -65.829 1.00 56.94 ? 330 ASP   A N   1 
ATOM   2780 C CA  . ASP   A 1 328 ? 1.294   -7.148  -66.664 1.00 62.64 ? 330 ASP   A CA  1 
ATOM   2781 C C   . ASP   A 1 328 ? 1.249   -8.151  -67.813 1.00 58.67 ? 330 ASP   A C   1 
ATOM   2782 O O   . ASP   A 1 328 ? 0.340   -8.127  -68.640 1.00 56.92 ? 330 ASP   A O   1 
ATOM   2783 C CB  . ASP   A 1 328 ? 2.543   -7.388  -65.814 1.00 68.75 ? 330 ASP   A CB  1 
ATOM   2784 C CG  . ASP   A 1 328 ? 2.583   -6.512  -64.575 1.00 75.81 ? 330 ASP   A CG  1 
ATOM   2785 O OD1 . ASP   A 1 328 ? 3.441   -5.606  -64.508 1.00 77.62 ? 330 ASP   A OD1 1 
ATOM   2786 O OD2 . ASP   A 1 328 ? 1.743   -6.717  -63.675 1.00 77.88 ? 330 ASP   A OD2 1 
HETATM 2787 C C01 . A1IYV B 2 .   ? 17.159  -2.889  -47.384 1.00 23.63 ? 401 A1IYV A C01 1 
HETATM 2788 C C03 . A1IYV B 2 .   ? 16.991  -5.229  -47.671 1.00 21.51 ? 401 A1IYV A C03 1 
HETATM 2789 C C04 . A1IYV B 2 .   ? 17.229  -6.321  -48.488 1.00 19.60 ? 401 A1IYV A C04 1 
HETATM 2790 C C06 . A1IYV B 2 .   ? 17.204  -7.596  -47.974 1.00 16.50 ? 401 A1IYV A C06 1 
HETATM 2791 C C07 . A1IYV B 2 .   ? 16.937  -7.766  -46.633 1.00 17.90 ? 401 A1IYV A C07 1 
HETATM 2792 C C08 . A1IYV B 2 .   ? 16.698  -6.677  -45.798 1.00 20.78 ? 401 A1IYV A C08 1 
HETATM 2793 C C09 . A1IYV B 2 .   ? 16.721  -5.396  -46.321 1.00 22.25 ? 401 A1IYV A C09 1 
HETATM 2794 C C10 . A1IYV B 2 .   ? 16.927  -9.198  -46.155 1.00 20.57 ? 401 A1IYV A C10 1 
HETATM 2795 C C11 . A1IYV B 2 .   ? 16.703  -9.646  -44.936 1.00 21.86 ? 401 A1IYV A C11 1 
HETATM 2796 C C13 . A1IYV B 2 .   ? 16.344  -10.185 -42.404 1.00 25.56 ? 401 A1IYV A C13 1 
HETATM 2797 C C15 . A1IYV B 2 .   ? 16.354  -11.164 -44.785 1.00 18.72 ? 401 A1IYV A C15 1 
HETATM 2798 C C18 . A1IYV B 2 .   ? 16.348  -9.155  -40.261 1.00 28.71 ? 401 A1IYV A C18 1 
HETATM 2799 C C19 . A1IYV B 2 .   ? 17.304  -9.216  -39.279 1.00 31.36 ? 401 A1IYV A C19 1 
HETATM 2800 C C20 . A1IYV B 2 .   ? 17.411  -8.163  -38.400 1.00 35.73 ? 401 A1IYV A C20 1 
HETATM 2801 C C21 . A1IYV B 2 .   ? 16.561  -7.074  -38.476 1.00 34.63 ? 401 A1IYV A C21 1 
HETATM 2802 C C22 . A1IYV B 2 .   ? 15.583  -7.028  -39.456 1.00 31.94 ? 401 A1IYV A C22 1 
HETATM 2803 C C23 . A1IYV B 2 .   ? 15.474  -8.083  -40.350 1.00 35.08 ? 401 A1IYV A C23 1 
HETATM 2804 C C24 . A1IYV B 2 .   ? 18.494  -8.253  -37.354 1.00 41.13 ? 401 A1IYV A C24 1 
HETATM 2805 N N14 . A1IYV B 2 .   ? 16.147  -11.476 -43.195 1.00 21.72 ? 401 A1IYV A N14 1 
HETATM 2806 N N17 . A1IYV B 2 .   ? 16.218  -10.258 -41.172 1.00 28.66 ? 401 A1IYV A N17 1 
HETATM 2807 O O02 . A1IYV B 2 .   ? 17.035  -3.967  -48.273 1.00 23.56 ? 401 A1IYV A O02 1 
HETATM 2808 O O05 . A1IYV B 2 .   ? 17.486  -6.108  -49.837 1.00 22.86 ? 401 A1IYV A O05 1 
HETATM 2809 O O16 . A1IYV B 2 .   ? 16.248  -11.955 -45.660 1.00 19.24 ? 401 A1IYV A O16 1 
HETATM 2810 S S12 . A1IYV B 2 .   ? 16.737  -8.927  -43.446 1.00 22.58 ? 401 A1IYV A S12 1 
HETATM 2811 S S   . SO4   C 3 .   ? -14.563 -19.124 -39.320 1.00 16.22 ? 402 SO4   A S   1 
HETATM 2812 O O1  . SO4   C 3 .   ? -14.877 -19.336 -40.737 1.00 21.30 ? 402 SO4   A O1  1 
HETATM 2813 O O2  . SO4   C 3 .   ? -13.958 -17.801 -39.124 1.00 15.37 ? 402 SO4   A O2  1 
HETATM 2814 O O3  . SO4   C 3 .   ? -15.807 -19.162 -38.556 1.00 18.54 ? 402 SO4   A O3  1 
HETATM 2815 O O4  . SO4   C 3 .   ? -13.728 -20.210 -38.849 1.00 16.10 ? 402 SO4   A O4  1 
HETATM 2816 S S   . SO4   D 3 .   ? 11.332  -23.674 -35.756 1.00 41.68 ? 403 SO4   A S   1 
HETATM 2817 O O1  . SO4   D 3 .   ? 12.347  -24.674 -36.083 1.00 52.57 ? 403 SO4   A O1  1 
HETATM 2818 O O2  . SO4   D 3 .   ? 11.824  -22.349 -36.140 1.00 42.75 ? 403 SO4   A O2  1 
HETATM 2819 O O3  . SO4   D 3 .   ? 10.113  -23.988 -36.482 1.00 36.58 ? 403 SO4   A O3  1 
HETATM 2820 O O4  . SO4   D 3 .   ? 11.048  -23.697 -34.325 1.00 55.62 ? 403 SO4   A O4  1 
HETATM 2821 S S   . SO4   E 3 .   ? 6.378   -16.466 -29.159 1.00 65.81 ? 404 SO4   A S   1 
HETATM 2822 O O1  . SO4   E 3 .   ? 6.542   -16.709 -30.593 1.00 59.49 ? 404 SO4   A O1  1 
HETATM 2823 O O2  . SO4   E 3 .   ? 7.685   -16.505 -28.507 1.00 73.04 ? 404 SO4   A O2  1 
HETATM 2824 O O3  . SO4   E 3 .   ? 5.777   -15.151 -28.946 1.00 65.25 ? 404 SO4   A O3  1 
HETATM 2825 O O4  . SO4   E 3 .   ? 5.520   -17.498 -28.585 1.00 65.49 ? 404 SO4   A O4  1 
HETATM 2826 C C1  . EDO   F 4 .   ? -9.422  -3.586  -33.822 1.00 34.10 ? 405 EDO   A C1  1 
HETATM 2827 O O1  . EDO   F 4 .   ? -10.207 -3.081  -32.733 1.00 33.60 ? 405 EDO   A O1  1 
HETATM 2828 C C2  . EDO   F 4 .   ? -9.231  -5.094  -33.681 1.00 22.09 ? 405 EDO   A C2  1 
HETATM 2829 O O2  . EDO   F 4 .   ? -8.553  -5.376  -32.450 1.00 29.34 ? 405 EDO   A O2  1 
HETATM 2830 O O   . HOH   G 5 .   ? -2.221  -5.894  -38.377 1.00 16.45 ? 501 HOH   A O   1 
HETATM 2831 O O   . HOH   G 5 .   ? -6.976  -6.978  -63.971 1.00 40.27 ? 502 HOH   A O   1 
HETATM 2832 O O   . HOH   G 5 .   ? 12.194  -10.185 -39.232 1.00 36.46 ? 503 HOH   A O   1 
HETATM 2833 O O   . HOH   G 5 .   ? 12.208  -29.355 -39.596 1.00 40.48 ? 504 HOH   A O   1 
HETATM 2834 O O   . HOH   G 5 .   ? 0.590   -8.411  -62.547 1.00 39.57 ? 505 HOH   A O   1 
HETATM 2835 O O   . HOH   G 5 .   ? -0.209  -21.814 -58.901 1.00 36.81 ? 506 HOH   A O   1 
HETATM 2836 O O   . HOH   G 5 .   ? -21.407 -3.816  -33.623 1.00 33.16 ? 507 HOH   A O   1 
HETATM 2837 O O   . HOH   G 5 .   ? 8.621   -12.207 -36.047 1.00 36.22 ? 508 HOH   A O   1 
HETATM 2838 O O   . HOH   G 5 .   ? 2.906   -26.821 -29.167 1.00 37.90 ? 509 HOH   A O   1 
HETATM 2839 O O   . HOH   G 5 .   ? 16.830  -7.886  -27.219 1.00 44.72 ? 510 HOH   A O   1 
HETATM 2840 O O   . HOH   G 5 .   ? 15.286  -21.939 -40.427 1.00 36.83 ? 511 HOH   A O   1 
HETATM 2841 O O   . HOH   G 5 .   ? 27.374  -9.048  -36.683 1.00 38.43 ? 512 HOH   A O   1 
HETATM 2842 O O   . HOH   G 5 .   ? -13.075 -28.222 -27.837 1.00 27.29 ? 513 HOH   A O   1 
HETATM 2843 O O   . HOH   G 5 .   ? 34.814  -8.690  -46.422 1.00 49.77 ? 514 HOH   A O   1 
HETATM 2844 O O   . HOH   G 5 .   ? 12.386  7.309   -60.704 1.00 43.88 ? 515 HOH   A O   1 
HETATM 2845 O O   . HOH   G 5 .   ? 34.584  -0.596  -54.656 1.00 46.57 ? 516 HOH   A O   1 
HETATM 2846 O O   . HOH   G 5 .   ? 18.976  -35.877 -43.796 1.00 52.92 ? 517 HOH   A O   1 
HETATM 2847 O O   . HOH   G 5 .   ? 31.711  -10.945 -43.568 1.00 28.35 ? 518 HOH   A O   1 
HETATM 2848 O O   . HOH   G 5 .   ? -5.931  8.628   -42.186 1.00 45.50 ? 519 HOH   A O   1 
HETATM 2849 O O   . HOH   G 5 .   ? 39.195  -9.065  -52.033 1.00 41.80 ? 520 HOH   A O   1 
HETATM 2850 O O   . HOH   G 5 .   ? -1.439  -37.042 -49.945 1.00 38.74 ? 521 HOH   A O   1 
HETATM 2851 O O   . HOH   G 5 .   ? 0.805   -17.360 -58.732 1.00 31.20 ? 522 HOH   A O   1 
HETATM 2852 O O   . HOH   G 5 .   ? 16.846  -5.010  -55.715 1.00 47.38 ? 523 HOH   A O   1 
HETATM 2853 O O   . HOH   G 5 .   ? 3.856   -12.650 -27.830 1.00 31.96 ? 524 HOH   A O   1 
HETATM 2854 O O   . HOH   G 5 .   ? -22.915 -7.658  -32.170 1.00 34.70 ? 525 HOH   A O   1 
HETATM 2855 O O   . HOH   G 5 .   ? 17.353  -23.526 -56.771 1.00 40.31 ? 526 HOH   A O   1 
HETATM 2856 O O   . HOH   G 5 .   ? 24.648  -23.576 -50.580 1.00 27.07 ? 527 HOH   A O   1 
HETATM 2857 O O   . HOH   G 5 .   ? -13.585 10.306  -37.627 1.00 28.97 ? 528 HOH   A O   1 
HETATM 2858 O O   . HOH   G 5 .   ? 0.056   -4.523  -39.460 1.00 22.88 ? 529 HOH   A O   1 
HETATM 2859 O O   . HOH   G 5 .   ? -5.261  -24.574 -26.776 1.00 49.96 ? 530 HOH   A O   1 
HETATM 2860 O O   . HOH   G 5 .   ? 16.340  -32.448 -43.253 1.00 38.26 ? 531 HOH   A O   1 
HETATM 2861 O O   . HOH   G 5 .   ? -11.822 -27.164 -22.037 1.00 37.15 ? 532 HOH   A O   1 
HETATM 2862 O O   . HOH   G 5 .   ? 18.602  -19.298 -40.244 1.00 29.01 ? 533 HOH   A O   1 
HETATM 2863 O O   . HOH   G 5 .   ? 16.404  -26.602 -55.416 1.00 35.29 ? 534 HOH   A O   1 
HETATM 2864 O O   . HOH   G 5 .   ? 7.670   -15.561 -32.593 1.00 51.94 ? 535 HOH   A O   1 
HETATM 2865 O O   . HOH   G 5 .   ? -5.404  -12.557 -61.042 1.00 39.07 ? 536 HOH   A O   1 
HETATM 2866 O O   . HOH   G 5 .   ? 2.517   1.249   -36.941 1.00 48.12 ? 537 HOH   A O   1 
HETATM 2867 O O   . HOH   G 5 .   ? 8.453   -25.941 -36.761 1.00 20.84 ? 538 HOH   A O   1 
HETATM 2868 O O   . HOH   G 5 .   ? 2.670   -18.798 -30.953 1.00 26.79 ? 539 HOH   A O   1 
HETATM 2869 O O   . HOH   G 5 .   ? 20.060  -0.944  -54.615 1.00 41.72 ? 540 HOH   A O   1 
HETATM 2870 O O   . HOH   G 5 .   ? -12.377 -13.889 -60.554 1.00 39.72 ? 541 HOH   A O   1 
HETATM 2871 O O   . HOH   G 5 .   ? -20.621 -16.841 -37.922 1.00 26.51 ? 542 HOH   A O   1 
HETATM 2872 O O   . HOH   G 5 .   ? 12.989  -21.092 -57.584 1.00 22.89 ? 543 HOH   A O   1 
HETATM 2873 O O   . HOH   G 5 .   ? -11.660 -18.109 -60.483 1.00 35.93 ? 544 HOH   A O   1 
HETATM 2874 O O   . HOH   G 5 .   ? 0.376   -6.041  -58.816 1.00 26.84 ? 545 HOH   A O   1 
HETATM 2875 O O   . HOH   G 5 .   ? -9.426  -5.552  -25.943 1.00 30.27 ? 546 HOH   A O   1 
HETATM 2876 O O   . HOH   G 5 .   ? 0.043   -31.336 -30.870 1.00 31.73 ? 547 HOH   A O   1 
HETATM 2877 O O   . HOH   G 5 .   ? 27.441  -4.113  -30.785 1.00 40.70 ? 548 HOH   A O   1 
HETATM 2878 O O   . HOH   G 5 .   ? -2.132  9.287   -40.123 1.00 25.37 ? 549 HOH   A O   1 
HETATM 2879 O O   . HOH   G 5 .   ? 12.727  -26.560 -58.468 1.00 29.84 ? 550 HOH   A O   1 
HETATM 2880 O O   . HOH   G 5 .   ? -4.136  7.155   -45.864 1.00 39.29 ? 551 HOH   A O   1 
HETATM 2881 O O   . HOH   G 5 .   ? 38.907  -3.834  -47.715 1.00 36.94 ? 552 HOH   A O   1 
HETATM 2882 O O   . HOH   G 5 .   ? 5.670   -8.792  -60.381 1.00 36.69 ? 553 HOH   A O   1 
HETATM 2883 O O   . HOH   G 5 .   ? -3.943  -35.398 -34.957 1.00 47.51 ? 554 HOH   A O   1 
HETATM 2884 O O   . HOH   G 5 .   ? -7.479  -0.925  -50.430 1.00 25.24 ? 555 HOH   A O   1 
HETATM 2885 O O   . HOH   G 5 .   ? -13.866 -12.875 -40.972 1.00 17.88 ? 556 HOH   A O   1 
HETATM 2886 O O   . HOH   G 5 .   ? 3.524   -4.283  -36.465 1.00 49.24 ? 557 HOH   A O   1 
HETATM 2887 O O   . HOH   G 5 .   ? 10.217  -34.583 -58.899 1.00 44.06 ? 558 HOH   A O   1 
HETATM 2888 O O   . HOH   G 5 .   ? 28.177  -5.522  -34.786 1.00 37.19 ? 559 HOH   A O   1 
HETATM 2889 O O   . HOH   G 5 .   ? 5.696   -3.546  -45.814 1.00 33.58 ? 560 HOH   A O   1 
HETATM 2890 O O   . HOH   G 5 .   ? 31.943  -14.869 -53.730 1.00 22.53 ? 561 HOH   A O   1 
HETATM 2891 O O   . HOH   G 5 .   ? 19.477  -31.211 -49.450 1.00 28.71 ? 562 HOH   A O   1 
HETATM 2892 O O   . HOH   G 5 .   ? -6.594  -4.551  -30.859 1.00 24.16 ? 563 HOH   A O   1 
HETATM 2893 O O   . HOH   G 5 .   ? 9.841   -27.844 -37.937 1.00 30.37 ? 564 HOH   A O   1 
HETATM 2894 O O   . HOH   G 5 .   ? -10.832 -21.503 -49.720 1.00 33.68 ? 565 HOH   A O   1 
HETATM 2895 O O   . HOH   G 5 .   ? -15.068 -24.425 -40.319 1.00 32.06 ? 566 HOH   A O   1 
HETATM 2896 O O   . HOH   G 5 .   ? -3.118  -28.739 -42.105 1.00 16.87 ? 567 HOH   A O   1 
HETATM 2897 O O   . HOH   G 5 .   ? 20.140  -25.824 -53.409 1.00 27.74 ? 568 HOH   A O   1 
HETATM 2898 O O   . HOH   G 5 .   ? -17.094 -6.570  -57.589 1.00 42.79 ? 569 HOH   A O   1 
HETATM 2899 O O   . HOH   G 5 .   ? -2.857  2.360   -44.825 1.00 33.95 ? 570 HOH   A O   1 
HETATM 2900 O O   . HOH   G 5 .   ? 27.356  -2.980  -61.898 1.00 43.72 ? 571 HOH   A O   1 
HETATM 2901 O O   . HOH   G 5 .   ? -8.743  3.140   -37.667 1.00 23.62 ? 572 HOH   A O   1 
HETATM 2902 O O   . HOH   G 5 .   ? 33.912  -1.992  -43.693 1.00 38.00 ? 573 HOH   A O   1 
HETATM 2903 O O   . HOH   G 5 .   ? -7.028  -10.417 -22.307 1.00 23.67 ? 574 HOH   A O   1 
HETATM 2904 O O   . HOH   G 5 .   ? -0.682  -31.497 -42.468 1.00 18.43 ? 575 HOH   A O   1 
HETATM 2905 O O   . HOH   G 5 .   ? -0.400  0.149   -62.372 1.00 25.67 ? 576 HOH   A O   1 
HETATM 2906 O O   . HOH   G 5 .   ? 0.871   -29.895 -40.865 1.00 17.85 ? 577 HOH   A O   1 
HETATM 2907 O O   . HOH   G 5 .   ? 1.589   6.498   -54.294 1.00 40.87 ? 578 HOH   A O   1 
HETATM 2908 O O   . HOH   G 5 .   ? -10.281 -6.567  -30.769 1.00 22.66 ? 579 HOH   A O   1 
HETATM 2909 O O   . HOH   G 5 .   ? -12.353 -26.950 -49.739 1.00 39.32 ? 580 HOH   A O   1 
HETATM 2910 O O   . HOH   G 5 .   ? 15.493  -1.276  -55.017 1.00 24.74 ? 581 HOH   A O   1 
HETATM 2911 O O   . HOH   G 5 .   ? -19.916 -15.300 -31.383 1.00 17.81 ? 582 HOH   A O   1 
HETATM 2912 O O   . HOH   G 5 .   ? -12.603 -17.828 -47.031 1.00 18.46 ? 583 HOH   A O   1 
HETATM 2913 O O   . HOH   G 5 .   ? 8.070   -6.497  -57.431 1.00 30.10 ? 584 HOH   A O   1 
HETATM 2914 O O   . HOH   G 5 .   ? 9.805   -1.198  -47.381 1.00 35.23 ? 585 HOH   A O   1 
HETATM 2915 O O   . HOH   G 5 .   ? -17.888 -12.739 -41.331 1.00 32.11 ? 586 HOH   A O   1 
HETATM 2916 O O   . HOH   G 5 .   ? -11.396 -15.578 -55.079 1.00 31.46 ? 587 HOH   A O   1 
HETATM 2917 O O   . HOH   G 5 .   ? -19.061 -25.057 -30.688 1.00 32.13 ? 588 HOH   A O   1 
HETATM 2918 O O   . HOH   G 5 .   ? -8.451  -7.418  -24.584 1.00 39.98 ? 589 HOH   A O   1 
HETATM 2919 O O   . HOH   G 5 .   ? -4.440  -22.436 -54.471 1.00 23.14 ? 590 HOH   A O   1 
HETATM 2920 O O   . HOH   G 5 .   ? -15.727 -9.779  -38.089 1.00 28.98 ? 591 HOH   A O   1 
HETATM 2921 O O   . HOH   G 5 .   ? -15.213 -21.929 -41.461 1.00 22.85 ? 592 HOH   A O   1 
HETATM 2922 O O   . HOH   G 5 .   ? 10.388  -36.761 -51.655 1.00 40.49 ? 593 HOH   A O   1 
HETATM 2923 O O   . HOH   G 5 .   ? -13.565 13.536  -39.413 1.00 39.18 ? 594 HOH   A O   1 
HETATM 2924 O O   . HOH   G 5 .   ? -10.509 -22.014 -21.493 1.00 34.74 ? 595 HOH   A O   1 
HETATM 2925 O O   . HOH   G 5 .   ? 10.741  -29.828 -42.608 1.00 32.11 ? 596 HOH   A O   1 
HETATM 2926 O O   . HOH   G 5 .   ? -1.392  -21.590 -23.885 1.00 42.12 ? 597 HOH   A O   1 
HETATM 2927 O O   . HOH   G 5 .   ? 37.194  -9.328  -54.096 1.00 43.26 ? 598 HOH   A O   1 
HETATM 2928 O O   . HOH   G 5 .   ? -18.130 -19.652 -39.884 1.00 25.44 ? 599 HOH   A O   1 
HETATM 2929 O O   . HOH   G 5 .   ? -13.303 -25.512 -43.930 1.00 33.59 ? 600 HOH   A O   1 
HETATM 2930 O O   . HOH   G 5 .   ? 6.654   -27.478 -56.714 1.00 25.77 ? 601 HOH   A O   1 
HETATM 2931 O O   . HOH   G 5 .   ? -2.663  4.842   -46.286 1.00 32.21 ? 602 HOH   A O   1 
HETATM 2932 O O   . HOH   G 5 .   ? -5.657  -32.083 -49.327 1.00 40.77 ? 603 HOH   A O   1 
HETATM 2933 O O   . HOH   G 5 .   ? -10.984 9.221   -46.239 1.00 31.13 ? 604 HOH   A O   1 
HETATM 2934 O O   . HOH   G 5 .   ? -7.075  -22.705 -46.520 1.00 19.16 ? 605 HOH   A O   1 
HETATM 2935 O O   . HOH   G 5 .   ? 36.090  -16.303 -43.884 1.00 22.93 ? 606 HOH   A O   1 
HETATM 2936 O O   . HOH   G 5 .   ? -8.599  -10.941 -59.451 1.00 21.40 ? 607 HOH   A O   1 
HETATM 2937 O O   . HOH   G 5 .   ? -1.735  -31.675 -34.094 1.00 43.07 ? 608 HOH   A O   1 
HETATM 2938 O O   . HOH   G 5 .   ? -10.742 -0.729  -51.333 1.00 21.97 ? 609 HOH   A O   1 
HETATM 2939 O O   . HOH   G 5 .   ? 0.025   -21.003 -28.170 1.00 38.90 ? 610 HOH   A O   1 
HETATM 2940 O O   . HOH   G 5 .   ? -18.046 -11.221 -46.914 1.00 32.23 ? 611 HOH   A O   1 
HETATM 2941 O O   . HOH   G 5 .   ? 21.727  -5.723  -55.042 1.00 29.23 ? 612 HOH   A O   1 
HETATM 2942 O O   . HOH   G 5 .   ? -14.019 -33.241 -36.571 1.00 39.53 ? 613 HOH   A O   1 
HETATM 2943 O O   . HOH   G 5 .   ? -9.210  -32.057 -40.976 1.00 25.48 ? 614 HOH   A O   1 
HETATM 2944 O O   . HOH   G 5 .   ? -14.920 -21.739 -36.912 1.00 23.81 ? 615 HOH   A O   1 
HETATM 2945 O O   . HOH   G 5 .   ? -12.907 -23.162 -22.938 1.00 27.08 ? 616 HOH   A O   1 
HETATM 2946 O O   . HOH   G 5 .   ? -9.382  -2.495  -30.182 1.00 41.33 ? 617 HOH   A O   1 
HETATM 2947 O O   . HOH   G 5 .   ? -19.469 -28.602 -30.436 1.00 32.61 ? 618 HOH   A O   1 
HETATM 2948 O O   . HOH   G 5 .   ? 15.911  -14.674 -45.484 1.00 16.79 ? 619 HOH   A O   1 
HETATM 2949 O O   . HOH   G 5 .   ? 10.462  -16.923 -42.372 1.00 14.41 ? 620 HOH   A O   1 
HETATM 2950 O O   . HOH   G 5 .   ? -6.943  -14.400 -62.434 1.00 31.45 ? 621 HOH   A O   1 
HETATM 2951 O O   . HOH   G 5 .   ? -13.475 -1.880  -55.556 1.00 27.86 ? 622 HOH   A O   1 
HETATM 2952 O O   . HOH   G 5 .   ? -5.705  -26.564 -44.631 1.00 20.54 ? 623 HOH   A O   1 
HETATM 2953 O O   . HOH   G 5 .   ? 14.962  -14.490 -56.049 1.00 21.37 ? 624 HOH   A O   1 
HETATM 2954 O O   . HOH   G 5 .   ? 23.980  -24.729 -53.353 1.00 37.81 ? 625 HOH   A O   1 
HETATM 2955 O O   . HOH   G 5 .   ? 0.991   0.592   -32.868 1.00 43.75 ? 626 HOH   A O   1 
HETATM 2956 O O   . HOH   G 5 .   ? 36.131  -13.683 -33.379 1.00 21.76 ? 627 HOH   A O   1 
HETATM 2957 O O   . HOH   G 5 .   ? -5.265  -20.692 -47.169 1.00 16.82 ? 628 HOH   A O   1 
HETATM 2958 O O   . HOH   G 5 .   ? 0.121   -5.952  -61.506 1.00 38.25 ? 629 HOH   A O   1 
HETATM 2959 O O   . HOH   G 5 .   ? -16.580 -11.295 -53.920 1.00 39.64 ? 630 HOH   A O   1 
HETATM 2960 O O   . HOH   G 5 .   ? -2.242  -20.895 -53.619 1.00 17.54 ? 631 HOH   A O   1 
HETATM 2961 O O   . HOH   G 5 .   ? -2.463  -23.267 -41.148 1.00 16.22 ? 632 HOH   A O   1 
HETATM 2962 O O   . HOH   G 5 .   ? -1.747  -20.734 -50.824 1.00 14.65 ? 633 HOH   A O   1 
HETATM 2963 O O   . HOH   G 5 .   ? -17.306 -27.453 -35.056 1.00 24.79 ? 634 HOH   A O   1 
HETATM 2964 O O   . HOH   G 5 .   ? 11.892  -31.003 -44.881 1.00 25.53 ? 635 HOH   A O   1 
HETATM 2965 O O   . HOH   G 5 .   ? 18.634  -18.156 -37.837 1.00 39.95 ? 636 HOH   A O   1 
HETATM 2966 O O   . HOH   G 5 .   ? -9.899  6.092   -52.920 1.00 30.74 ? 637 HOH   A O   1 
HETATM 2967 O O   . HOH   G 5 .   ? -9.743  -10.119 -21.336 1.00 25.92 ? 638 HOH   A O   1 
HETATM 2968 O O   . HOH   G 5 .   ? 17.726  -15.905 -39.697 1.00 34.18 ? 639 HOH   A O   1 
HETATM 2969 O O   . HOH   G 5 .   ? -3.391  -0.678  -32.884 1.00 32.99 ? 640 HOH   A O   1 
HETATM 2970 O O   . HOH   G 5 .   ? -2.966  -7.703  -36.367 1.00 14.20 ? 641 HOH   A O   1 
HETATM 2971 O O   . HOH   G 5 .   ? 6.092   -35.139 -47.362 1.00 32.39 ? 642 HOH   A O   1 
HETATM 2972 O O   . HOH   G 5 .   ? 13.983  -21.317 -42.504 1.00 17.12 ? 643 HOH   A O   1 
HETATM 2973 O O   . HOH   G 5 .   ? -17.432 -7.772  -28.125 1.00 37.08 ? 644 HOH   A O   1 
HETATM 2974 O O   . HOH   G 5 .   ? -9.909  -25.816 -20.929 1.00 41.40 ? 645 HOH   A O   1 
HETATM 2975 O O   . HOH   G 5 .   ? 3.269   -16.466 -58.357 1.00 23.07 ? 646 HOH   A O   1 
HETATM 2976 O O   . HOH   G 5 .   ? -22.168 -7.590  -34.707 1.00 26.68 ? 647 HOH   A O   1 
HETATM 2977 O O   . HOH   G 5 .   ? -7.005  -33.020 -28.275 1.00 37.85 ? 648 HOH   A O   1 
HETATM 2978 O O   . HOH   G 5 .   ? 6.280   -24.396 -28.891 1.00 38.78 ? 649 HOH   A O   1 
HETATM 2979 O O   . HOH   G 5 .   ? 4.295   -31.406 -49.559 1.00 22.37 ? 650 HOH   A O   1 
HETATM 2980 O O   . HOH   G 5 .   ? -19.497 -17.935 -26.852 1.00 26.01 ? 651 HOH   A O   1 
HETATM 2981 O O   . HOH   G 5 .   ? -15.127 -31.664 -30.311 1.00 28.58 ? 652 HOH   A O   1 
HETATM 2982 O O   . HOH   G 5 .   ? -18.412 -16.026 -33.737 1.00 18.07 ? 653 HOH   A O   1 
HETATM 2983 O O   . HOH   G 5 .   ? -7.896  -30.593 -45.663 1.00 30.56 ? 654 HOH   A O   1 
HETATM 2984 O O   . HOH   G 5 .   ? 3.906   -21.390 -58.932 1.00 40.88 ? 655 HOH   A O   1 
HETATM 2985 O O   . HOH   G 5 .   ? -5.544  -18.202 -62.597 1.00 23.88 ? 656 HOH   A O   1 
HETATM 2986 O O   . HOH   G 5 .   ? -3.247  -12.220 -35.184 1.00 13.08 ? 657 HOH   A O   1 
HETATM 2987 O O   . HOH   G 5 .   ? -2.719  -18.033 -26.835 1.00 24.81 ? 658 HOH   A O   1 
HETATM 2988 O O   . HOH   G 5 .   ? 37.020  -6.677  -48.727 1.00 50.97 ? 659 HOH   A O   1 
HETATM 2989 O O   . HOH   G 5 .   ? 11.604  -14.770 -40.019 1.00 26.19 ? 660 HOH   A O   1 
HETATM 2990 O O   . HOH   G 5 .   ? -19.441 2.158   -41.476 1.00 42.65 ? 661 HOH   A O   1 
HETATM 2991 O O   . HOH   G 5 .   ? 4.723   -12.426 -38.430 1.00 17.66 ? 662 HOH   A O   1 
HETATM 2992 O O   . HOH   G 5 .   ? -18.497 -6.516  -48.730 1.00 34.27 ? 663 HOH   A O   1 
HETATM 2993 O O   . HOH   G 5 .   ? -6.357  6.022   -38.416 1.00 42.11 ? 664 HOH   A O   1 
HETATM 2994 O O   . HOH   G 5 .   ? 6.429   -32.034 -56.710 1.00 44.00 ? 665 HOH   A O   1 
HETATM 2995 O O   . HOH   G 5 .   ? -3.179  -24.577 -47.529 1.00 18.52 ? 666 HOH   A O   1 
HETATM 2996 O O   . HOH   G 5 .   ? 23.490  -19.630 -52.710 1.00 38.32 ? 667 HOH   A O   1 
HETATM 2997 O O   . HOH   G 5 .   ? -10.049 -32.325 -26.742 1.00 35.40 ? 668 HOH   A O   1 
HETATM 2998 O O   . HOH   G 5 .   ? 16.808  -16.454 -53.070 1.00 17.49 ? 669 HOH   A O   1 
HETATM 2999 O O   . HOH   G 5 .   ? 19.810  0.003   -47.130 1.00 42.94 ? 670 HOH   A O   1 
HETATM 3000 O O   . HOH   G 5 .   ? 7.794   -9.612  -59.938 1.00 48.87 ? 671 HOH   A O   1 
HETATM 3001 O O   . HOH   G 5 .   ? 30.189  -26.514 -46.761 1.00 42.90 ? 672 HOH   A O   1 
HETATM 3002 O O   . HOH   G 5 .   ? 3.256   -27.329 -57.113 1.00 29.22 ? 673 HOH   A O   1 
HETATM 3003 O O   . HOH   G 5 .   ? 26.692  -6.493  -62.337 1.00 45.07 ? 674 HOH   A O   1 
HETATM 3004 O O   . HOH   G 5 .   ? 14.280  -24.992 -56.727 1.00 25.07 ? 675 HOH   A O   1 
HETATM 3005 O O   . HOH   G 5 .   ? 16.028  -12.736 -39.544 1.00 39.65 ? 676 HOH   A O   1 
HETATM 3006 O O   . HOH   G 5 .   ? -18.428 -15.052 -41.581 1.00 33.47 ? 677 HOH   A O   1 
HETATM 3007 O O   . HOH   G 5 .   ? 37.697  -9.505  -46.152 1.00 30.08 ? 678 HOH   A O   1 
HETATM 3008 O O   . HOH   G 5 .   ? 23.928  -30.759 -50.819 1.00 40.00 ? 679 HOH   A O   1 
HETATM 3009 O O   . HOH   G 5 .   ? -6.737  -1.830  -30.173 1.00 42.20 ? 680 HOH   A O   1 
HETATM 3010 O O   . HOH   G 5 .   ? 10.001  -26.192 -60.006 1.00 43.43 ? 681 HOH   A O   1 
HETATM 3011 O O   . HOH   G 5 .   ? 33.434  -17.694 -47.165 1.00 21.88 ? 682 HOH   A O   1 
HETATM 3012 O O   . HOH   G 5 .   ? 10.726  -21.940 -30.393 1.00 51.06 ? 683 HOH   A O   1 
HETATM 3013 O O   . HOH   G 5 .   ? 30.815  -11.791 -55.437 1.00 36.56 ? 684 HOH   A O   1 
HETATM 3014 O O   . HOH   G 5 .   ? 20.883  -29.896 -51.048 1.00 32.60 ? 685 HOH   A O   1 
HETATM 3015 O O   . HOH   G 5 .   ? 26.316  0.166   -49.684 1.00 35.74 ? 686 HOH   A O   1 
HETATM 3016 O O   . HOH   G 5 .   ? 4.731   -36.136 -44.665 1.00 27.32 ? 687 HOH   A O   1 
HETATM 3017 O O   . HOH   G 5 .   ? 2.676   -20.570 -18.630 1.00 47.87 ? 688 HOH   A O   1 
HETATM 3018 O O   . HOH   G 5 .   ? -4.149  7.142   -48.747 1.00 42.76 ? 689 HOH   A O   1 
HETATM 3019 O O   . HOH   G 5 .   ? -15.716 -11.655 -39.427 1.00 33.42 ? 690 HOH   A O   1 
HETATM 3020 O O   . HOH   G 5 .   ? -3.161  -12.371 -20.472 1.00 37.99 ? 691 HOH   A O   1 
HETATM 3021 O O   . HOH   G 5 .   ? -11.385 -8.232  -22.470 1.00 47.18 ? 692 HOH   A O   1 
HETATM 3022 O O   . HOH   G 5 .   ? 3.036   -15.872 -41.637 1.00 13.77 ? 693 HOH   A O   1 
HETATM 3023 O O   . HOH   G 5 .   ? -15.011 3.226   -36.834 1.00 40.64 ? 694 HOH   A O   1 
HETATM 3024 O O   . HOH   G 5 .   ? -18.886 -8.775  -24.789 1.00 29.27 ? 695 HOH   A O   1 
HETATM 3025 O O   . HOH   G 5 .   ? 32.174  -24.109 -51.013 1.00 33.72 ? 696 HOH   A O   1 
HETATM 3026 O O   . HOH   G 5 .   ? 11.821  -8.678  -37.307 1.00 37.84 ? 697 HOH   A O   1 
HETATM 3027 O O   . HOH   G 5 .   ? -10.748 1.230   -37.524 1.00 22.37 ? 698 HOH   A O   1 
HETATM 3028 O O   . HOH   G 5 .   ? 33.155  -12.429 -32.175 1.00 40.93 ? 699 HOH   A O   1 
HETATM 3029 O O   . HOH   G 5 .   ? 4.881   4.550   -56.986 1.00 45.07 ? 700 HOH   A O   1 
HETATM 3030 O O   . HOH   G 5 .   ? -12.865 -19.562 -53.916 1.00 39.90 ? 701 HOH   A O   1 
HETATM 3031 O O   . HOH   G 5 .   ? -5.242  -22.252 -25.870 1.00 40.04 ? 702 HOH   A O   1 
HETATM 3032 O O   . HOH   G 5 .   ? -13.194 -10.610 -23.023 1.00 25.15 ? 703 HOH   A O   1 
HETATM 3033 O O   . HOH   G 5 .   ? 5.162   -25.789 -30.522 1.00 28.67 ? 704 HOH   A O   1 
HETATM 3034 O O   . HOH   G 5 .   ? -20.040 -22.450 -30.621 1.00 31.51 ? 705 HOH   A O   1 
HETATM 3035 O O   . HOH   G 5 .   ? -7.953  -9.635  -61.748 1.00 33.80 ? 706 HOH   A O   1 
HETATM 3036 O O   . HOH   G 5 .   ? -5.785  -25.304 -47.009 1.00 20.77 ? 707 HOH   A O   1 
HETATM 3037 O O   . HOH   G 5 .   ? -2.518  2.904   -36.214 1.00 39.07 ? 708 HOH   A O   1 
HETATM 3038 O O   . HOH   G 5 .   ? 17.401  -29.166 -54.657 1.00 26.73 ? 709 HOH   A O   1 
HETATM 3039 O O   . HOH   G 5 .   ? 2.509   -14.328 -24.228 1.00 31.87 ? 710 HOH   A O   1 
HETATM 3040 O O   . HOH   G 5 .   ? -11.427 12.680  -43.274 1.00 47.83 ? 711 HOH   A O   1 
HETATM 3041 O O   . HOH   G 5 .   ? 10.689  -10.887 -58.905 1.00 30.15 ? 712 HOH   A O   1 
HETATM 3042 O O   . HOH   G 5 .   ? -5.935  -26.944 -22.410 1.00 34.84 ? 713 HOH   A O   1 
HETATM 3043 O O   . HOH   G 5 .   ? -13.019 -37.767 -30.748 1.00 44.51 ? 714 HOH   A O   1 
HETATM 3044 O O   . HOH   G 5 .   ? -5.891  -28.982 -26.596 1.00 36.79 ? 715 HOH   A O   1 
HETATM 3045 O O   . HOH   G 5 .   ? -22.202 -8.685  -42.782 1.00 32.34 ? 716 HOH   A O   1 
HETATM 3046 O O   . HOH   G 5 .   ? -11.447 -3.976  -58.237 1.00 32.84 ? 717 HOH   A O   1 
HETATM 3047 O O   . HOH   G 5 .   ? 32.487  -8.190  -44.721 1.00 39.29 ? 718 HOH   A O   1 
HETATM 3048 O O   . HOH   G 5 .   ? 38.561  -13.013 -46.773 1.00 56.90 ? 719 HOH   A O   1 
HETATM 3049 O O   . HOH   G 5 .   ? 36.497  -16.305 -48.287 1.00 34.87 ? 720 HOH   A O   1 
HETATM 3050 O O   . HOH   G 5 .   ? 25.942  -8.423  -56.327 1.00 35.99 ? 721 HOH   A O   1 
HETATM 3051 O O   . HOH   G 5 .   ? 25.812  -11.233 -35.935 1.00 31.45 ? 722 HOH   A O   1 
HETATM 3052 O O   . HOH   G 5 .   ? 16.516  2.200   -48.341 1.00 50.67 ? 723 HOH   A O   1 
HETATM 3053 O O   . HOH   G 5 .   ? -2.943  -21.990 -26.141 1.00 50.31 ? 724 HOH   A O   1 
HETATM 3054 O O   . HOH   G 5 .   ? 10.254  -23.321 -60.057 1.00 27.55 ? 725 HOH   A O   1 
HETATM 3055 O O   . HOH   G 5 .   ? -6.799  6.239   -52.580 1.00 25.66 ? 726 HOH   A O   1 
HETATM 3056 O O   . HOH   G 5 .   ? -1.672  -30.051 -32.111 1.00 23.23 ? 727 HOH   A O   1 
HETATM 3057 O O   . HOH   G 5 .   ? -11.805 -25.216 -24.183 1.00 24.58 ? 728 HOH   A O   1 
HETATM 3058 O O   . HOH   G 5 .   ? 16.736  -0.524  -45.112 1.00 40.38 ? 729 HOH   A O   1 
HETATM 3059 O O   . HOH   G 5 .   ? 33.619  -5.621  -44.089 1.00 27.84 ? 730 HOH   A O   1 
HETATM 3060 O O   . HOH   G 5 .   ? 5.413   -34.545 -37.076 1.00 34.41 ? 731 HOH   A O   1 
HETATM 3061 O O   . HOH   G 5 .   ? 12.782  -11.991 -57.372 1.00 49.72 ? 732 HOH   A O   1 
HETATM 3062 O O   . HOH   G 5 .   ? -17.955 -10.930 -22.326 1.00 31.23 ? 733 HOH   A O   1 
HETATM 3063 O O   . HOH   G 5 .   ? 7.782   -7.636  -35.078 1.00 38.27 ? 734 HOH   A O   1 
HETATM 3064 O O   . HOH   G 5 .   ? -21.042 -5.384  -35.875 1.00 33.42 ? 735 HOH   A O   1 
HETATM 3065 O O   . HOH   G 5 .   ? -23.193 -18.831 -24.754 1.00 45.81 ? 736 HOH   A O   1 
HETATM 3066 O O   . HOH   G 5 .   ? -16.707 -0.675  -55.143 1.00 41.94 ? 737 HOH   A O   1 
HETATM 3067 O O   . HOH   G 5 .   ? -19.054 -10.498 -40.486 1.00 44.75 ? 738 HOH   A O   1 
HETATM 3068 O O   . HOH   G 5 .   ? 37.333  -15.782 -34.923 1.00 23.82 ? 739 HOH   A O   1 
HETATM 3069 O O   . HOH   G 5 .   ? 4.079   -6.025  -61.599 1.00 44.97 ? 740 HOH   A O   1 
HETATM 3070 O O   . HOH   G 5 .   ? -6.435  -32.440 -22.844 1.00 52.84 ? 741 HOH   A O   1 
HETATM 3071 O O   . HOH   G 5 .   ? 8.306   -29.995 -37.851 1.00 39.47 ? 742 HOH   A O   1 
HETATM 3072 O O   . HOH   G 5 .   ? 19.541  -19.742 -58.864 1.00 41.88 ? 743 HOH   A O   1 
HETATM 3073 O O   . HOH   G 5 .   ? -27.161 -16.136 -22.041 1.00 27.22 ? 744 HOH   A O   1 
HETATM 3074 O O   . HOH   G 5 .   ? -15.372 -28.173 -42.394 1.00 43.46 ? 745 HOH   A O   1 
HETATM 3075 O O   . HOH   G 5 .   ? -16.327 8.848   -39.156 1.00 26.83 ? 746 HOH   A O   1 
HETATM 3076 O O   . HOH   G 5 .   ? 5.637   -23.697 -59.133 1.00 40.59 ? 747 HOH   A O   1 
HETATM 3077 O O   . HOH   G 5 .   ? -7.738  -32.201 -43.821 1.00 35.59 ? 748 HOH   A O   1 
HETATM 3078 O O   . HOH   G 5 .   ? -2.228  -36.014 -47.420 1.00 50.28 ? 749 HOH   A O   1 
HETATM 3079 O O   . HOH   G 5 .   ? 27.822  -27.332 -45.321 1.00 36.69 ? 750 HOH   A O   1 
HETATM 3080 O O   . HOH   G 5 .   ? 15.948  -21.790 -57.762 1.00 39.26 ? 751 HOH   A O   1 
HETATM 3081 O O   . HOH   G 5 .   ? -14.719 -5.421  -31.921 1.00 31.71 ? 752 HOH   A O   1 
HETATM 3082 O O   . HOH   G 5 .   ? 32.916  -21.434 -36.342 1.00 47.06 ? 753 HOH   A O   1 
HETATM 3083 O O   . HOH   G 5 .   ? 23.898  -0.554  -56.371 1.00 40.35 ? 754 HOH   A O   1 
HETATM 3084 O O   . HOH   G 5 .   ? 32.534  -18.397 -40.161 1.00 37.44 ? 755 HOH   A O   1 
HETATM 3085 O O   . HOH   G 5 .   ? 30.714  -7.825  -61.947 1.00 30.74 ? 756 HOH   A O   1 
HETATM 3086 O O   . HOH   G 5 .   ? 4.205   -9.771  -23.440 1.00 42.91 ? 757 HOH   A O   1 
HETATM 3087 O O   . HOH   G 5 .   ? -22.391 -6.321  -44.869 1.00 38.48 ? 758 HOH   A O   1 
HETATM 3088 O O   . HOH   G 5 .   ? 6.187   -11.957 -31.014 1.00 36.75 ? 759 HOH   A O   1 
HETATM 3089 O O   . HOH   G 5 .   ? -18.795 -7.388  -43.156 1.00 38.03 ? 760 HOH   A O   1 
HETATM 3090 O O   . HOH   G 5 .   ? -17.139 -15.194 -46.384 1.00 38.85 ? 761 HOH   A O   1 
HETATM 3091 O O   . HOH   G 5 .   ? 11.228  -19.709 -61.131 1.00 48.88 ? 762 HOH   A O   1 
HETATM 3092 O O   . HOH   G 5 .   ? 4.008   -8.588  -33.589 1.00 33.32 ? 763 HOH   A O   1 
HETATM 3093 O O   . HOH   G 5 .   ? -5.294  -15.546 -17.611 1.00 37.32 ? 764 HOH   A O   1 
HETATM 3094 O O   . HOH   G 5 .   ? -17.735 -21.763 -37.790 1.00 29.67 ? 765 HOH   A O   1 
HETATM 3095 O O   . HOH   G 5 .   ? -16.496 12.250  -46.094 1.00 46.60 ? 766 HOH   A O   1 
HETATM 3096 O O   . HOH   G 5 .   ? 17.600  -2.891  -34.706 1.00 44.17 ? 767 HOH   A O   1 
HETATM 3097 O O   . HOH   G 5 .   ? 15.877  -9.335  -58.558 1.00 46.97 ? 768 HOH   A O   1 
HETATM 3098 O O   . HOH   G 5 .   ? -14.770 -1.047  -32.743 1.00 48.42 ? 769 HOH   A O   1 
HETATM 3099 O O   . HOH   G 5 .   ? 26.336  -31.978 -37.585 1.00 39.84 ? 770 HOH   A O   1 
HETATM 3100 O O   . HOH   G 5 .   ? -18.056 -6.983  -52.695 1.00 37.68 ? 771 HOH   A O   1 
HETATM 3101 O O   . HOH   G 5 .   ? -16.855 11.791  -39.460 1.00 40.03 ? 772 HOH   A O   1 
HETATM 3102 O O   . HOH   G 5 .   ? 6.276   -35.913 -41.899 1.00 49.57 ? 773 HOH   A O   1 
HETATM 3103 O O   . HOH   G 5 .   ? -20.730 -21.393 -37.847 1.00 32.73 ? 774 HOH   A O   1 
HETATM 3104 O O   . HOH   G 5 .   ? -3.915  -29.400 -30.425 1.00 34.83 ? 775 HOH   A O   1 
HETATM 3105 O O   . HOH   G 5 .   ? 5.885   -6.420  -26.275 1.00 49.48 ? 776 HOH   A O   1 
HETATM 3106 O O   . HOH   G 5 .   ? -14.547 -5.412  -58.804 1.00 40.76 ? 777 HOH   A O   1 
HETATM 3107 O O   . HOH   G 5 .   ? 30.458  -19.894 -33.663 1.00 51.20 ? 778 HOH   A O   1 
HETATM 3108 O O   . HOH   G 5 .   ? 35.877  -19.429 -37.798 1.00 35.66 ? 779 HOH   A O   1 
HETATM 3109 O O   . HOH   G 5 .   ? 2.036   -18.501 -25.290 1.00 42.96 ? 780 HOH   A O   1 
HETATM 3110 O O   . HOH   G 5 .   ? 11.646  -27.951 -36.090 1.00 47.00 ? 781 HOH   A O   1 
HETATM 3111 O O   . HOH   G 5 .   ? -9.830  -4.880  -28.548 1.00 33.52 ? 782 HOH   A O   1 
HETATM 3112 O O   . HOH   G 5 .   ? 0.885   -2.291  -63.259 1.00 36.56 ? 783 HOH   A O   1 
HETATM 3113 O O   . HOH   G 5 .   ? -15.144 -17.723 -45.728 1.00 32.64 ? 784 HOH   A O   1 
HETATM 3114 O O   . HOH   G 5 .   ? 38.126  -14.485 -44.272 1.00 49.39 ? 785 HOH   A O   1 
HETATM 3115 O O   . HOH   G 5 .   ? 32.687  -21.435 -33.298 1.00 49.07 ? 786 HOH   A O   1 
HETATM 3116 O O   . HOH   G 5 .   ? 4.526   -28.428 -28.648 1.00 49.32 ? 787 HOH   A O   1 
HETATM 3117 O O   . HOH   G 5 .   ? -14.551 -24.502 -37.679 1.00 27.65 ? 788 HOH   A O   1 
HETATM 3118 O O   . HOH   G 5 .   ? -19.861 -3.142  -55.028 1.00 44.01 ? 789 HOH   A O   1 
HETATM 3119 O O   . HOH   G 5 .   ? -6.224  -34.922 -42.567 1.00 46.97 ? 790 HOH   A O   1 
HETATM 3120 O O   . HOH   G 5 .   ? -17.724 -7.988  -45.758 1.00 40.56 ? 791 HOH   A O   1 
HETATM 3121 O O   . HOH   G 5 .   ? -17.524 6.384   -38.243 1.00 36.95 ? 792 HOH   A O   1 
HETATM 3122 O O   . HOH   G 5 .   ? -9.460  -12.859 -61.769 1.00 35.15 ? 793 HOH   A O   1 
HETATM 3123 O O   . HOH   G 5 .   ? -17.113 -25.918 -37.400 1.00 41.68 ? 794 HOH   A O   1 
HETATM 3124 O O   . HOH   G 5 .   ? -19.767 -17.144 -40.418 1.00 25.55 ? 795 HOH   A O   1 
HETATM 3125 O O   . HOH   G 5 .   ? 13.745  -32.507 -43.294 1.00 43.46 ? 796 HOH   A O   1 
HETATM 3126 O O   . HOH   G 5 .   ? 12.113  -39.089 -50.833 1.00 41.35 ? 797 HOH   A O   1 
HETATM 3127 O O   . HOH   G 5 .   ? -16.350 -8.893  -53.804 1.00 28.92 ? 798 HOH   A O   1 
HETATM 3128 O O   . HOH   G 5 .   ? 5.388   -6.696  -35.038 1.00 38.49 ? 799 HOH   A O   1 
HETATM 3129 O O   . HOH   G 5 .   ? -3.125  -21.975 -48.464 1.00 20.10 ? 800 HOH   A O   1 
HETATM 3130 O O   . HOH   G 5 .   ? -15.642 1.095   -33.493 1.00 49.39 ? 801 HOH   A O   1 
HETATM 3131 O O   . HOH   G 5 .   ? 18.050  -7.978  -30.281 1.00 42.63 ? 802 HOH   A O   1 
HETATM 3132 O O   . HOH   G 5 .   ? -12.748 -4.976  -30.741 1.00 43.92 ? 803 HOH   A O   1 
HETATM 3133 O O   . HOH   G 5 .   ? 7.061   -27.604 -30.462 1.00 43.24 ? 804 HOH   A O   1 
HETATM 3134 O O   . HOH   G 5 .   ? 1.619   -22.864 -26.895 1.00 46.02 ? 805 HOH   A O   1 
HETATM 3135 O O   . HOH   G 5 .   ? 19.417  -9.324  -58.028 1.00 40.76 ? 806 HOH   A O   1 
HETATM 3136 O O   . HOH   G 5 .   ? -3.203  2.035   -33.626 1.00 42.76 ? 807 HOH   A O   1 
HETATM 3137 O O   . HOH   G 5 .   ? -4.935  -0.975  -28.700 1.00 50.27 ? 808 HOH   A O   1 
HETATM 3138 O O   . HOH   G 5 .   ? -15.340 -9.515  -21.806 1.00 37.33 ? 809 HOH   A O   1 
HETATM 3139 O O   . HOH   G 5 .   ? 32.488  -16.941 -55.272 1.00 41.88 ? 810 HOH   A O   1 
HETATM 3140 O O   . HOH   G 5 .   ? -7.523  3.494   -35.088 1.00 47.68 ? 811 HOH   A O   1 
HETATM 3141 O O   . HOH   G 5 .   ? -17.275 -6.679  -24.333 1.00 43.64 ? 812 HOH   A O   1 
HETATM 3142 O O   . HOH   G 5 .   ? -0.637  -16.602 -60.850 1.00 41.02 ? 813 HOH   A O   1 
HETATM 3143 O O   . HOH   G 5 .   ? -0.313  -19.253 -26.377 1.00 40.74 ? 814 HOH   A O   1 
HETATM 3144 O O   . HOH   G 5 .   ? 20.870  -33.654 -50.318 1.00 47.83 ? 815 HOH   A O   1 
HETATM 3145 O O   . HOH   G 5 .   ? -17.567 -8.419  -56.290 1.00 38.86 ? 816 HOH   A O   1 
HETATM 3146 O O   . HOH   G 5 .   ? -16.285 1.754   -52.960 1.00 43.66 ? 817 HOH   A O   1 
HETATM 3147 O O   . HOH   G 5 .   ? 9.419   -18.276 -61.687 1.00 50.76 ? 818 HOH   A O   1 
HETATM 3148 O O   . HOH   G 5 .   ? 21.497  -10.327 -56.384 1.00 48.46 ? 819 HOH   A O   1 
HETATM 3149 O O   . HOH   G 5 .   ? -18.704 -24.340 -38.509 1.00 38.55 ? 820 HOH   A O   1 
HETATM 3150 O O   . HOH   G 5 .   ? 2.788   -13.864 -21.606 1.00 42.76 ? 821 HOH   A O   1 
HETATM 3151 O O   . HOH   G 5 .   ? -14.109 -2.794  -58.702 1.00 40.03 ? 822 HOH   A O   1 
HETATM 3152 O O   . HOH   G 5 .   ? -15.368 -14.252 -54.414 1.00 37.12 ? 823 HOH   A O   1 
HETATM 3153 O O   . HOH   G 5 .   ? -28.457 -16.352 -23.965 1.00 44.54 ? 824 HOH   A O   1 
HETATM 3154 O O   . HOH   G 5 .   ? -3.276  -37.515 -35.742 1.00 45.13 ? 825 HOH   A O   1 
HETATM 3155 O O   . HOH   G 5 .   ? -19.807 -9.305  -42.303 1.00 36.59 ? 826 HOH   A O   1 
HETATM 3156 O O   . HOH   G 5 .   ? 5.131   -13.151 -61.868 1.00 40.56 ? 827 HOH   A O   1 
HETATM 3157 O O   . HOH   G 5 .   ? -15.092 0.960   -54.921 1.00 46.38 ? 828 HOH   A O   1 
HETATM 3158 O O   . HOH   G 5 .   ? -5.147  -10.746 -20.492 1.00 32.01 ? 829 HOH   A O   1 
HETATM 3159 O O   . HOH   G 5 .   ? 36.758  -17.976 -41.900 1.00 29.54 ? 830 HOH   A O   1 
HETATM 3160 O O   . HOH   G 5 .   ? 36.046  -17.829 -46.232 1.00 31.61 ? 831 HOH   A O   1 
HETATM 3161 O O   . HOH   G 5 .   ? -16.169 4.331   -34.705 1.00 49.41 ? 832 HOH   A O   1 
HETATM 3162 O O   . HOH   G 5 .   ? -22.552 -15.357 -31.366 1.00 39.62 ? 833 HOH   A O   1 
HETATM 3163 O O   . HOH   G 5 .   ? -14.056 -18.301 -49.337 1.00 32.06 ? 834 HOH   A O   1 
HETATM 3164 O O   . HOH   G 5 .   ? 4.344   -18.460 -59.413 1.00 37.84 ? 835 HOH   A O   1 
HETATM 3165 O O   . HOH   G 5 .   ? -13.397 -15.529 -53.169 1.00 28.78 ? 836 HOH   A O   1 
HETATM 3166 O O   . HOH   G 5 .   ? 22.583  -12.802 -57.556 1.00 43.12 ? 837 HOH   A O   1 
HETATM 3167 O O   . HOH   G 5 .   ? -9.532  -9.446  -18.678 1.00 44.35 ? 838 HOH   A O   1 
HETATM 3168 O O   . HOH   G 5 .   ? -3.692  -14.915 -19.293 1.00 52.54 ? 839 HOH   A O   1 
HETATM 3169 O O   . HOH   G 5 .   ? -4.691  11.224  -48.563 1.00 41.32 ? 840 HOH   A O   1 
HETATM 3170 O O   . HOH   G 5 .   ? 37.001  -1.468  -53.769 1.00 34.58 ? 841 HOH   A O   1 
HETATM 3171 O O   . HOH   G 5 .   ? -10.789 1.036   -35.033 1.00 39.86 ? 842 HOH   A O   1 
HETATM 3172 O O   . HOH   G 5 .   ? 3.572   -14.834 -60.609 1.00 30.12 ? 843 HOH   A O   1 
HETATM 3173 O O   . HOH   G 5 .   ? 0.908   -14.760 -61.501 1.00 42.57 ? 844 HOH   A O   1 
HETATM 3174 O O   . HOH   G 5 .   ? 6.857   -4.621  -27.412 1.00 53.12 ? 845 HOH   A O   1 
HETATM 3175 O O   . HOH   G 5 .   ? -14.133 -17.732 -52.152 1.00 27.67 ? 846 HOH   A O   1 
HETATM 3176 O O   . HOH   G 5 .   ? 29.680  -33.080 -40.906 1.00 44.78 ? 847 HOH   A O   1 
HETATM 3177 O O   . HOH   G 5 .   ? -18.987 -24.158 -41.155 1.00 49.15 ? 848 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLY A 1   ? 0.5391 0.3915 0.5837 0.0405  0.0031  0.0382  3   GLY A N   
2    C CA  . GLY A 1   ? 0.5151 0.3753 0.5579 0.0445  0.0000  0.0356  3   GLY A CA  
3    C C   . GLY A 1   ? 0.5277 0.3925 0.5730 0.0415  0.0002  0.0375  3   GLY A C   
4    O O   . GLY A 1   ? 0.5278 0.3975 0.5683 0.0341  0.0011  0.0389  3   GLY A O   
5    N N   . PRO A 2   ? 0.5340 0.4045 0.5786 0.0443  -0.0016 0.0348  4   PRO A N   
6    C CA  . PRO A 2   ? 0.4045 0.2840 0.4473 0.0411  -0.0029 0.0358  4   PRO A CA  
7    C C   . PRO A 2   ? 0.3995 0.2801 0.4382 0.0265  0.0069  0.0243  4   PRO A C   
8    O O   . PRO A 2   ? 0.4413 0.3076 0.4881 0.0228  0.0160  0.0169  4   PRO A O   
9    C CB  . PRO A 2   ? 0.4446 0.3289 0.4861 0.0475  -0.0066 0.0344  4   PRO A CB  
10   C CG  . PRO A 2   ? 0.5047 0.3874 0.5403 0.0518  -0.0076 0.0312  4   PRO A CG  
11   C CD  . PRO A 2   ? 0.5119 0.3832 0.5541 0.0486  -0.0024 0.0301  4   PRO A CD  
12   N N   . VAL A 3   ? 0.3197 0.2184 0.3453 0.0183  0.0052  0.0229  5   VAL A N   
13   C CA  . VAL A 3   ? 0.3328 0.2370 0.3531 0.0037  0.0139  0.0120  5   VAL A CA  
14   C C   . VAL A 3   ? 0.2759 0.1795 0.3009 0.0040  0.0168  0.0059  5   VAL A C   
15   O O   . VAL A 3   ? 0.2804 0.1910 0.3046 0.0122  0.0098  0.0110  5   VAL A O   
16   C CB  . VAL A 3   ? 0.3079 0.2345 0.3125 -0.0040 0.0104  0.0135  5   VAL A CB  
17   C CG1 . VAL A 3   ? 0.2924 0.2292 0.2910 -0.0184 0.0183  0.0027  5   VAL A CG1 
18   C CG2 . VAL A 3   ? 0.3824 0.3095 0.3822 -0.0063 0.0089  0.0181  5   VAL A CG2 
19   N N   . PRO A 4   ? 0.2535 0.1493 0.2832 -0.0047 0.0269  -0.0049 6   PRO A N   
20   C CA  . PRO A 4   ? 0.2434 0.1396 0.2779 -0.0045 0.0296  -0.0107 6   PRO A CA  
21   C C   . PRO A 4   ? 0.2509 0.1688 0.2742 -0.0112 0.0275  -0.0129 6   PRO A C   
22   O O   . PRO A 4   ? 0.2828 0.2158 0.2945 -0.0179 0.0258  -0.0115 6   PRO A O   
23   C CB  . PRO A 4   ? 0.2875 0.1688 0.3289 -0.0126 0.0416  -0.0217 6   PRO A CB  
24   C CG  . PRO A 4   ? 0.3231 0.2035 0.3577 -0.0226 0.0460  -0.0239 6   PRO A CG  
25   C CD  . PRO A 4   ? 0.3093 0.1932 0.3404 -0.0145 0.0366  -0.0121 6   PRO A CD  
26   N N   . SER A 5   ? 0.2501 0.1702 0.2769 -0.0090 0.0276  -0.0158 7   SER A N   
27   C CA  . SER A 5   ? 0.2381 0.1777 0.2558 -0.0137 0.0257  -0.0174 7   SER A CA  
28   C C   . SER A 5   ? 0.2242 0.1614 0.2484 -0.0185 0.0325  -0.0271 7   SER A C   
29   O O   . SER A 5   ? 0.2775 0.1990 0.3134 -0.0131 0.0351  -0.0292 7   SER A O   
30   C CB  . SER A 5   ? 0.2223 0.1696 0.2353 -0.0023 0.0149  -0.0067 7   SER A CB  
31   O OG  . SER A 5   ? 0.2362 0.2010 0.2401 -0.0061 0.0136  -0.0078 7   SER A OG  
32   N N   . ARG A 6   ? 0.2553 0.2095 0.2719 -0.0283 0.0353  -0.0329 8   ARG A N   
33   C CA  . ARG A 6   ? 0.2396 0.1960 0.2605 -0.0333 0.0408  -0.0417 8   ARG A CA  
34   C C   . ARG A 6   ? 0.2592 0.2356 0.2712 -0.0332 0.0358  -0.0388 8   ARG A C   
35   O O   . ARG A 6   ? 0.2366 0.2289 0.2367 -0.0352 0.0318  -0.0339 8   ARG A O   
36   C CB  . ARG A 6   ? 0.3067 0.2649 0.3272 -0.0483 0.0516  -0.0539 8   ARG A CB  
37   C CG  . ARG A 6   ? 0.3793 0.3167 0.4078 -0.0503 0.0588  -0.0588 8   ARG A CG  
38   C CD  . ARG A 6   ? 0.4107 0.3307 0.4525 -0.0416 0.0606  -0.0602 8   ARG A CD  
39   N NE  . ARG A 6   ? 0.4571 0.3562 0.5067 -0.0430 0.0689  -0.0654 8   ARG A NE  
40   C CZ  . ARG A 6   ? 0.4721 0.3565 0.5254 -0.0357 0.0673  -0.0591 8   ARG A CZ  
41   N NH1 . ARG A 6   ? 0.3446 0.2334 0.3947 -0.0266 0.0573  -0.0477 8   ARG A NH1 
42   N NH2 . ARG A 6   ? 0.4777 0.3426 0.5375 -0.0373 0.0759  -0.0643 8   ARG A NH2 
43   N N   . ALA A 7   ? 0.2348 0.2110 0.2520 -0.0312 0.0363  -0.0419 9   ALA A N   
44   C CA  . ALA A 7   ? 0.2116 0.2069 0.2205 -0.0338 0.0340  -0.0415 9   ALA A CA  
45   C C   . ALA A 7   ? 0.2269 0.2397 0.2282 -0.0478 0.0402  -0.0489 9   ALA A C   
46   O O   . ALA A 7   ? 0.2904 0.2982 0.2963 -0.0573 0.0486  -0.0584 9   ALA A O   
47   C CB  . ALA A 7   ? 0.2064 0.1980 0.2232 -0.0315 0.0352  -0.0456 9   ALA A CB  
48   N N   . ARG A 8   ? 0.2242 0.2576 0.2133 -0.0492 0.0364  -0.0443 10  ARG A N   
49   C CA  . ARG A 8   ? 0.2356 0.2891 0.2169 -0.0625 0.0421  -0.0508 10  ARG A CA  
50   C C   . ARG A 8   ? 0.2271 0.2903 0.2113 -0.0694 0.0473  -0.0593 10  ARG A C   
51   O O   . ARG A 8   ? 0.2610 0.3406 0.2407 -0.0817 0.0533  -0.0665 10  ARG A O   
52   C CB  . ARG A 8   ? 0.2308 0.3047 0.1972 -0.0608 0.0363  -0.0419 10  ARG A CB  
53   C CG  . ARG A 8   ? 0.2564 0.3241 0.2191 -0.0559 0.0318  -0.0343 10  ARG A CG  
54   C CD  . ARG A 8   ? 0.4705 0.5500 0.4211 -0.0464 0.0229  -0.0219 10  ARG A CD  
55   N NE  . ARG A 8   ? 0.6066 0.7134 0.5437 -0.0531 0.0237  -0.0209 10  ARG A NE  
56   C CZ  . ARG A 8   ? 0.6108 0.7332 0.5389 -0.0487 0.0202  -0.0154 10  ARG A CZ  
57   N NH1 . ARG A 8   ? 0.6071 0.7192 0.5378 -0.0383 0.0156  -0.0108 10  ARG A NH1 
58   N NH2 . ARG A 8   ? 0.6297 0.7781 0.5456 -0.0546 0.0216  -0.0144 10  ARG A NH2 
59   N N   . VAL A 9   ? 0.2067 0.2608 0.1981 -0.0621 0.0451  -0.0587 11  VAL A N   
60   C CA  . VAL A 9   ? 0.2129 0.2742 0.2084 -0.0676 0.0495  -0.0665 11  VAL A CA  
61   C C   . VAL A 9   ? 0.2412 0.2817 0.2505 -0.0622 0.0509  -0.0700 11  VAL A C   
62   O O   . VAL A 9   ? 0.2322 0.2556 0.2462 -0.0520 0.0464  -0.0640 11  VAL A O   
63   C CB  . VAL A 9   ? 0.2410 0.3192 0.2279 -0.0638 0.0443  -0.0604 11  VAL A CB  
64   C CG1 . VAL A 9   ? 0.2522 0.3537 0.2255 -0.0693 0.0440  -0.0574 11  VAL A CG1 
65   C CG2 . VAL A 9   ? 0.2448 0.3112 0.2310 -0.0494 0.0354  -0.0494 11  VAL A CG2 
66   N N   . TYR A 10  ? 0.2116 0.2549 0.2272 -0.0691 0.0572  -0.0799 12  TYR A N   
67   C CA  . TYR A 10  ? 0.2177 0.2448 0.2460 -0.0646 0.0591  -0.0840 12  TYR A CA  
68   C C   . TYR A 10  ? 0.2169 0.2212 0.2533 -0.0595 0.0606  -0.0836 12  TYR A C   
69   O O   . TYR A 10  ? 0.2718 0.2616 0.3166 -0.0500 0.0581  -0.0807 12  TYR A O   
70   C CB  . TYR A 10  ? 0.2222 0.2495 0.2506 -0.0548 0.0517  -0.0768 12  TYR A CB  
71   C CG  . TYR A 10  ? 0.2286 0.2770 0.2483 -0.0585 0.0499  -0.0759 12  TYR A CG  
72   C CD1 . TYR A 10  ? 0.2127 0.2752 0.2335 -0.0695 0.0566  -0.0856 12  TYR A CD1 
73   C CD2 . TYR A 10  ? 0.2282 0.2824 0.2384 -0.0508 0.0419  -0.0650 12  TYR A CD2 
74   C CE1 . TYR A 10  ? 0.2277 0.3102 0.2407 -0.0723 0.0551  -0.0842 12  TYR A CE1 
75   C CE2 . TYR A 10  ? 0.2172 0.2897 0.2189 -0.0533 0.0406  -0.0635 12  TYR A CE2 
76   C CZ  . TYR A 10  ? 0.2013 0.2885 0.2047 -0.0640 0.0472  -0.0728 12  TYR A CZ  
77   O OH  . TYR A 10  ? 0.2951 0.4014 0.2901 -0.0661 0.0461  -0.0708 12  TYR A OH  
78   N N   . THR A 11  ? 0.2480 0.2503 0.2815 -0.0658 0.0647  -0.0861 13  THR A N   
79   C CA  . THR A 11  ? 0.2717 0.2530 0.3112 -0.0606 0.0657  -0.0842 13  THR A CA  
80   C C   . THR A 11  ? 0.3098 0.2738 0.3621 -0.0597 0.0727  -0.0920 13  THR A C   
81   O O   . THR A 11  ? 0.3147 0.2617 0.3749 -0.0495 0.0707  -0.0877 13  THR A O   
82   C CB  . THR A 11  ? 0.2880 0.2716 0.3206 -0.0694 0.0696  -0.0862 13  THR A CB  
83   O OG1 . THR A 11  ? 0.2997 0.3047 0.3195 -0.0722 0.0645  -0.0807 13  THR A OG1 
84   C CG2 . THR A 11  ? 0.2796 0.2441 0.3158 -0.0619 0.0678  -0.0804 13  THR A CG2 
85   N N   . ASP A 12  ? 0.3114 0.2806 0.3660 -0.0699 0.0808  -0.1033 14  ASP A N   
86   C CA  . ASP A 12  ? 0.2935 0.2462 0.3590 -0.0706 0.0891  -0.1120 14  ASP A CA  
87   C C   . ASP A 12  ? 0.3018 0.2586 0.3740 -0.0685 0.0896  -0.1160 14  ASP A C   
88   O O   . ASP A 12  ? 0.3180 0.2671 0.3976 -0.0720 0.0977  -0.1254 14  ASP A O   
89   C CB  . ASP A 12  ? 0.3306 0.2825 0.3934 -0.0845 0.0996  -0.1230 14  ASP A CB  
90   C CG  . ASP A 12  ? 0.5226 0.4708 0.5782 -0.0877 0.0995  -0.1194 14  ASP A CG  
91   O OD1 . ASP A 12  ? 0.6018 0.5331 0.6610 -0.0784 0.0970  -0.1128 14  ASP A OD1 
92   O OD2 . ASP A 12  ? 0.5942 0.5577 0.6405 -0.0994 0.1019  -0.1230 14  ASP A OD2 
93   N N   . VAL A 13  ? 0.2795 0.2481 0.3491 -0.0628 0.0812  -0.1090 15  VAL A N   
94   C CA  . VAL A 13  ? 0.2554 0.2300 0.3302 -0.0622 0.0815  -0.1129 15  VAL A CA  
95   C C   . VAL A 13  ? 0.3018 0.2585 0.3891 -0.0542 0.0842  -0.1148 15  VAL A C   
96   O O   . VAL A 13  ? 0.2910 0.2473 0.3848 -0.0576 0.0903  -0.1234 15  VAL A O   
97   C CB  . VAL A 13  ? 0.3100 0.2981 0.3787 -0.0570 0.0718  -0.1041 15  VAL A CB  
98   C CG1 . VAL A 13  ? 0.3016 0.3112 0.3591 -0.0662 0.0714  -0.1048 15  VAL A CG1 
99   C CG2 . VAL A 13  ? 0.4798 0.4587 0.5464 -0.0458 0.0638  -0.0923 15  VAL A CG2 
100  N N   . ASN A 14  ? 0.2979 0.2402 0.3885 -0.0432 0.0800  -0.1066 16  ASN A N   
101  C CA  . ASN A 14  ? 0.3071 0.2344 0.4093 -0.0345 0.0823  -0.1072 16  ASN A CA  
102  C C   . ASN A 14  ? 0.3352 0.2470 0.4433 -0.0377 0.0930  -0.1156 16  ASN A C   
103  O O   . ASN A 14  ? 0.4096 0.3176 0.5251 -0.0335 0.0958  -0.1165 16  ASN A O   
104  C CB  . ASN A 14  ? 0.2860 0.2049 0.3901 -0.0214 0.0742  -0.0955 16  ASN A CB  
105  C CG  . ASN A 14  ? 0.2654 0.1960 0.3661 -0.0167 0.0650  -0.0886 16  ASN A CG  
106  O OD1 . ASN A 14  ? 0.3015 0.2400 0.4047 -0.0184 0.0654  -0.0925 16  ASN A OD1 
107  N ND2 . ASN A 14  ? 0.2552 0.1866 0.3496 -0.0111 0.0568  -0.0784 16  ASN A ND2 
108  N N   . THR A 15  ? 0.3484 0.2561 0.4509 -0.0446 0.0969  -0.1176 17  THR A N   
109  C CA  . THR A 15  ? 0.4030 0.3012 0.5076 -0.0475 0.1051  -0.1208 17  THR A CA  
110  C C   . THR A 15  ? 0.3815 0.2871 0.4890 -0.0547 0.1119  -0.1300 17  THR A C   
111  O O   . THR A 15  ? 0.4644 0.3615 0.5774 -0.0516 0.1169  -0.1309 17  THR A O   
112  C CB  . THR A 15  ? 0.4713 0.3671 0.5678 -0.0564 0.1084  -0.1228 17  THR A CB  
113  O OG1 . THR A 15  ? 0.4739 0.3665 0.5667 -0.0513 0.1013  -0.1151 17  THR A OG1 
114  C CG2 . THR A 15  ? 0.6065 0.4883 0.7050 -0.0561 0.1155  -0.1231 17  THR A CG2 
115  N N   . HIS A 16  ? 0.4401 0.3622 0.5434 -0.0639 0.1119  -0.1364 18  HIS A N   
116  C CA  . HIS A 16  ? 0.3704 0.3022 0.4756 -0.0721 0.1184  -0.1452 18  HIS A CA  
117  C C   . HIS A 16  ? 0.3509 0.2906 0.4624 -0.0675 0.1152  -0.1459 18  HIS A C   
118  O O   . HIS A 16  ? 0.3653 0.3131 0.4797 -0.0732 0.1202  -0.1528 18  HIS A O   
119  C CB  . HIS A 16  ? 0.3896 0.3379 0.4858 -0.0864 0.1211  -0.1518 18  HIS A CB  
120  C CG  . HIS A 16  ? 0.4335 0.3757 0.5230 -0.0924 0.1250  -0.1520 18  HIS A CG  
121  N ND1 . HIS A 16  ? 0.4725 0.4042 0.5634 -0.0956 0.1336  -0.1555 18  HIS A ND1 
122  C CD2 . HIS A 16  ? 0.4423 0.3867 0.5233 -0.0957 0.1214  -0.1490 18  HIS A CD2 
123  C CE1 . HIS A 16  ? 0.4875 0.4156 0.5710 -0.1009 0.1353  -0.1549 18  HIS A CE1 
124  N NE2 . HIS A 16  ? 0.4718 0.4080 0.5493 -0.1012 0.1279  -0.1509 18  HIS A NE2 
125  N N   . ARG A 17  ? 0.3569 0.2948 0.4704 -0.0577 0.1072  -0.1390 19  ARG A N   
126  C CA  . ARG A 17  ? 0.3416 0.2834 0.4620 -0.0515 0.1046  -0.1386 19  ARG A CA  
127  C C   . ARG A 17  ? 0.3388 0.2683 0.4674 -0.0443 0.1085  -0.1370 19  ARG A C   
128  O O   . ARG A 17  ? 0.4248 0.3408 0.5535 -0.0408 0.1107  -0.1332 19  ARG A O   
129  C CB  . ARG A 17  ? 0.3100 0.2516 0.4300 -0.0425 0.0953  -0.1309 19  ARG A CB  
130  C CG  . ARG A 17  ? 0.3864 0.3461 0.4961 -0.0471 0.0881  -0.1264 19  ARG A CG  
131  C CD  . ARG A 17  ? 0.3861 0.3605 0.4967 -0.0488 0.0856  -0.1284 19  ARG A CD  
132  N NE  . ARG A 17  ? 0.3219 0.3142 0.4223 -0.0538 0.0801  -0.1249 19  ARG A NE  
133  C CZ  . ARG A 17  ? 0.2898 0.2971 0.3891 -0.0574 0.0785  -0.1271 19  ARG A CZ  
134  N NH1 . ARG A 17  ? 0.2738 0.2806 0.3819 -0.0567 0.0817  -0.1330 19  ARG A NH1 
135  N NH2 . ARG A 17  ? 0.4405 0.4635 0.5299 -0.0613 0.0740  -0.1232 19  ARG A NH2 
136  N N   . PRO A 18  ? 0.3595 0.2939 0.4944 -0.0421 0.1092  -0.1396 20  PRO A N   
137  C CA  . PRO A 18  ? 0.3757 0.2990 0.5175 -0.0332 0.1112  -0.1365 20  PRO A CA  
138  C C   . PRO A 18  ? 0.4472 0.3620 0.5902 -0.0208 0.1042  -0.1254 20  PRO A C   
139  O O   . PRO A 18  ? 0.3381 0.2578 0.4789 -0.0180 0.0970  -0.1209 20  PRO A O   
140  C CB  . PRO A 18  ? 0.3793 0.3130 0.5267 -0.0338 0.1119  -0.1415 20  PRO A CB  
141  C CG  . PRO A 18  ? 0.4180 0.3673 0.5616 -0.0400 0.1077  -0.1446 20  PRO A CG  
142  C CD  . PRO A 18  ? 0.3588 0.3098 0.4940 -0.0477 0.1081  -0.1455 20  PRO A CD  
143  N N   . ARG A 19  ? 0.4108 0.3132 0.5565 -0.0136 0.1063  -0.1208 21  ARG A N   
144  C CA  . ARG A 19  ? 0.3635 0.2589 0.5094 -0.0024 0.0998  -0.1098 21  ARG A CA  
145  C C   . ARG A 19  ? 0.3197 0.2232 0.4686 0.0045  0.0924  -0.1052 21  ARG A C   
146  O O   . ARG A 19  ? 0.3599 0.2636 0.5066 0.0100  0.0850  -0.0972 21  ARG A O   
147  C CB  . ARG A 19  ? 0.4400 0.3230 0.5879 0.0041  0.1037  -0.1063 21  ARG A CB  
148  C CG  . ARG A 19  ? 0.5096 0.3879 0.6573 0.0159  0.0969  -0.0949 21  ARG A CG  
149  C CD  . ARG A 19  ? 0.7241 0.5917 0.8732 0.0223  0.1010  -0.0921 21  ARG A CD  
150  N NE  . ARG A 19  ? 0.8885 0.7457 1.0349 0.0163  0.1086  -0.0964 21  ARG A NE  
151  C CZ  . ARG A 19  ? 1.0029 0.8510 1.1454 0.0180  0.1081  -0.0914 21  ARG A CZ  
152  N NH1 . ARG A 19  ? 1.0207 0.8693 1.1616 0.0259  0.1002  -0.0818 21  ARG A NH1 
153  N NH2 . ARG A 19  ? 1.0288 0.8677 1.1687 0.0116  0.1158  -0.0962 21  ARG A NH2 
154  N N   . GLU A 20  ? 0.3353 0.2461 0.4890 0.0039  0.0943  -0.1102 22  GLU A N   
155  C CA  . GLU A 20  ? 0.3000 0.2192 0.4568 0.0096  0.0880  -0.1069 22  GLU A CA  
156  C C   . GLU A 20  ? 0.3012 0.2281 0.4541 0.0068  0.0816  -0.1057 22  GLU A C   
157  O O   . GLU A 20  ? 0.3174 0.2481 0.4712 0.0130  0.0750  -0.1001 22  GLU A O   
158  C CB  . GLU A 20  ? 0.3013 0.2286 0.4636 0.0071  0.0920  -0.1146 22  GLU A CB  
159  C CG  . GLU A 20  ? 0.5526 0.4799 0.7149 -0.0025 0.1007  -0.1245 22  GLU A CG  
160  C CD  . GLU A 20  ? 0.6996 0.6132 0.8623 0.0001  0.1071  -0.1238 22  GLU A CD  
161  O OE1 . GLU A 20  ? 0.7742 0.6813 0.9394 0.0100  0.1062  -0.1177 22  GLU A OE1 
162  O OE2 . GLU A 20  ? 0.7026 0.6123 0.8624 -0.0080 0.1131  -0.1293 22  GLU A OE2 
163  N N   . TYR A 21  ? 0.2772 0.2064 0.4248 -0.0023 0.0836  -0.1109 23  TYR A N   
164  C CA  . TYR A 21  ? 0.2435 0.1797 0.3859 -0.0048 0.0779  -0.1101 23  TYR A CA  
165  C C   . TYR A 21  ? 0.2489 0.1782 0.3886 0.0037  0.0706  -0.0990 23  TYR A C   
166  O O   . TYR A 21  ? 0.2548 0.1899 0.3919 0.0071  0.0632  -0.0935 23  TYR A O   
167  C CB  . TYR A 21  ? 0.2838 0.2250 0.4195 -0.0166 0.0818  -0.1175 23  TYR A CB  
168  C CG  . TYR A 21  ? 0.2407 0.1950 0.3657 -0.0199 0.0735  -0.1114 23  TYR A CG  
169  C CD1 . TYR A 21  ? 0.2354 0.2050 0.3574 -0.0241 0.0704  -0.1128 23  TYR A CD1 
170  C CD2 . TYR A 21  ? 0.2302 0.1813 0.3477 -0.0183 0.0688  -0.1039 23  TYR A CD2 
171  C CE1 . TYR A 21  ? 0.2138 0.1943 0.3254 -0.0263 0.0634  -0.1068 23  TYR A CE1 
172  C CE2 . TYR A 21  ? 0.2233 0.1860 0.3305 -0.0203 0.0616  -0.0979 23  TYR A CE2 
173  C CZ  . TYR A 21  ? 0.2267 0.2035 0.3307 -0.0242 0.0592  -0.0994 23  TYR A CZ  
174  O OH  . TYR A 21  ? 0.2517 0.2390 0.3446 -0.0255 0.0526  -0.0931 23  TYR A OH  
175  N N   . TRP A 22  ? 0.2867 0.2057 0.4249 0.0063  0.0718  -0.0943 24  TRP A N   
176  C CA  . TRP A 22  ? 0.2867 0.2004 0.4214 0.0133  0.0648  -0.0838 24  TRP A CA  
177  C C   . TRP A 22  ? 0.2293 0.1372 0.3665 0.0234  0.0621  -0.0749 24  TRP A C   
178  O O   . TRP A 22  ? 0.2810 0.1873 0.4147 0.0297  0.0552  -0.0655 24  TRP A O   
179  C CB  . TRP A 22  ? 0.2644 0.1724 0.3935 0.0084  0.0670  -0.0844 24  TRP A CB  
180  C CG  . TRP A 22  ? 0.2554 0.1563 0.3857 0.0040  0.0754  -0.0893 24  TRP A CG  
181  C CD1 . TRP A 22  ? 0.2952 0.1987 0.4241 -0.0069 0.0830  -0.0996 24  TRP A CD1 
182  C CD2 . TRP A 22  ? 0.3118 0.2026 0.4440 0.0101  0.0769  -0.0841 24  TRP A CD2 
183  N NE1 . TRP A 22  ? 0.3639 0.2580 0.4942 -0.0077 0.0895  -0.1010 24  TRP A NE1 
184  C CE2 . TRP A 22  ? 0.3373 0.2231 0.4696 0.0028  0.0859  -0.0917 24  TRP A CE2 
185  C CE3 . TRP A 22  ? 0.3288 0.2152 0.4614 0.0206  0.0716  -0.0739 24  TRP A CE3 
186  C CZ2 . TRP A 22  ? 0.3885 0.2634 0.5219 0.0063  0.0899  -0.0894 24  TRP A CZ2 
187  C CZ3 . TRP A 22  ? 0.3743 0.2513 0.5077 0.0238  0.0753  -0.0719 24  TRP A CZ3 
188  C CH2 . TRP A 22  ? 0.3181 0.1887 0.4521 0.0170  0.0845  -0.0795 24  TRP A CH2 
189  N N   . ASP A 23  ? 0.3283 0.2341 0.4705 0.0250  0.0672  -0.0776 25  ASP A N   
190  C CA  . ASP A 23  ? 0.2653 0.1663 0.4086 0.0342  0.0653  -0.0700 25  ASP A CA  
191  C C   . ASP A 23  ? 0.3040 0.2131 0.4497 0.0400  0.0598  -0.0662 25  ASP A C   
192  O O   . ASP A 23  ? 0.3183 0.2303 0.4692 0.0422  0.0627  -0.0689 25  ASP A O   
193  C CB  . ASP A 23  ? 0.3543 0.2488 0.5011 0.0337  0.0735  -0.0747 25  ASP A CB  
194  C CG  . ASP A 23  ? 0.4522 0.3417 0.5992 0.0432  0.0722  -0.0674 25  ASP A CG  
195  O OD1 . ASP A 23  ? 0.4139 0.3037 0.5570 0.0490  0.0654  -0.0587 25  ASP A OD1 
196  O OD2 . ASP A 23  ? 0.4870 0.3728 0.6375 0.0448  0.0782  -0.0707 25  ASP A OD2 
197  N N   . TYR A 24  ? 0.3141 0.2268 0.4556 0.0425  0.0520  -0.0597 26  TYR A N   
198  C CA  . TYR A 24  ? 0.2629 0.1838 0.4061 0.0462  0.0469  -0.0570 26  TYR A CA  
199  C C   . TYR A 24  ? 0.3209 0.2422 0.4650 0.0544  0.0452  -0.0509 26  TYR A C   
200  O O   . TYR A 24  ? 0.3359 0.2645 0.4837 0.0569  0.0436  -0.0510 26  TYR A O   
201  C CB  . TYR A 24  ? 0.2727 0.1964 0.4099 0.0463  0.0392  -0.0517 26  TYR A CB  
202  C CG  . TYR A 24  ? 0.3318 0.2502 0.4611 0.0500  0.0345  -0.0428 26  TYR A CG  
203  C CD1 . TYR A 24  ? 0.3200 0.2334 0.4455 0.0462  0.0354  -0.0435 26  TYR A CD1 
204  C CD2 . TYR A 24  ? 0.3405 0.2599 0.4654 0.0569  0.0293  -0.0343 26  TYR A CD2 
205  C CE1 . TYR A 24  ? 0.4049 0.3144 0.5230 0.0495  0.0310  -0.0358 26  TYR A CE1 
206  C CE2 . TYR A 24  ? 0.3740 0.2898 0.4903 0.0596  0.0250  -0.0272 26  TYR A CE2 
207  C CZ  . TYR A 24  ? 0.4362 0.3471 0.5494 0.0561  0.0257  -0.0278 26  TYR A CZ  
208  O OH  . TYR A 24  ? 0.5846 0.4928 0.6892 0.0587  0.0215  -0.0212 26  TYR A OH  
209  N N   . GLU A 25  ? 0.3366 0.2510 0.4772 0.0585  0.0456  -0.0461 27  GLU A N   
210  C CA  . GLU A 25  ? 0.3952 0.3107 0.5361 0.0663  0.0446  -0.0411 27  GLU A CA  
211  C C   . GLU A 25  ? 0.3692 0.2868 0.5179 0.0676  0.0508  -0.0468 27  GLU A C   
212  O O   . GLU A 25  ? 0.4259 0.3483 0.5761 0.0740  0.0495  -0.0437 27  GLU A O   
213  C CB  . GLU A 25  ? 0.4793 0.3867 0.6150 0.0698  0.0444  -0.0363 27  GLU A CB  
214  C CG  . GLU A 25  ? 0.5828 0.4896 0.7100 0.0696  0.0377  -0.0301 27  GLU A CG  
215  C CD  . GLU A 25  ? 0.7136 0.6119 0.8369 0.0703  0.0388  -0.0278 27  GLU A CD  
216  O OE1 . GLU A 25  ? 0.7420 0.6391 0.8629 0.0762  0.0374  -0.0236 27  GLU A OE1 
217  O OE2 . GLU A 25  ? 0.7785 0.6717 0.9013 0.0649  0.0412  -0.0307 27  GLU A OE2 
218  N N   . SER A 26  ? 0.3704 0.2852 0.5233 0.0617  0.0575  -0.0553 28  SER A N   
219  C CA  . SER A 26  ? 0.3628 0.2795 0.5222 0.0623  0.0638  -0.0614 28  SER A CA  
220  C C   . SER A 26  ? 0.3245 0.2522 0.4890 0.0589  0.0633  -0.0669 28  SER A C   
221  O O   . SER A 26  ? 0.3497 0.2814 0.5197 0.0597  0.0678  -0.0719 28  SER A O   
222  C CB  . SER A 26  ? 0.4225 0.3305 0.5828 0.0569  0.0720  -0.0684 28  SER A CB  
223  O OG  . SER A 26  ? 0.5732 0.4708 0.7295 0.0602  0.0731  -0.0639 28  SER A OG  
224  N N   . HIS A 27  ? 0.3475 0.2802 0.5101 0.0553  0.0579  -0.0661 29  HIS A N   
225  C CA  . HIS A 27  ? 0.3252 0.2684 0.4922 0.0512  0.0573  -0.0722 29  HIS A CA  
226  C C   . HIS A 27  ? 0.3573 0.3094 0.5292 0.0573  0.0555  -0.0701 29  HIS A C   
227  O O   . HIS A 27  ? 0.3409 0.2936 0.5106 0.0640  0.0509  -0.0617 29  HIS A O   
228  C CB  . HIS A 27  ? 0.3665 0.3121 0.5292 0.0475  0.0512  -0.0706 29  HIS A CB  
229  C CG  . HIS A 27  ? 0.3171 0.2735 0.4833 0.0433  0.0500  -0.0768 29  HIS A CG  
230  N ND1 . HIS A 27  ? 0.2919 0.2532 0.4608 0.0356  0.0554  -0.0876 29  HIS A ND1 
231  C CD2 . HIS A 27  ? 0.3428 0.3067 0.5097 0.0452  0.0441  -0.0743 29  HIS A CD2 
232  C CE1 . HIS A 27  ? 0.3127 0.2857 0.4795 0.0318  0.0513  -0.0891 29  HIS A CE1 
233  N NE2 . HIS A 27  ? 0.3281 0.3026 0.4927 0.0371  0.0443  -0.0807 29  HIS A NE2 
234  N N   . VAL A 28  ? 0.2910 0.2511 0.4692 0.0547  0.0594  -0.0780 30  VAL A N   
235  C CA  . VAL A 28  ? 0.3087 0.2798 0.4925 0.0595  0.0581  -0.0774 30  VAL A CA  
236  C C   . VAL A 28  ? 0.2986 0.2806 0.4843 0.0550  0.0536  -0.0807 30  VAL A C   
237  O O   . VAL A 28  ? 0.3481 0.3346 0.5349 0.0474  0.0560  -0.0896 30  VAL A O   
238  C CB  . VAL A 28  ? 0.3220 0.2961 0.5112 0.0603  0.0653  -0.0838 30  VAL A CB  
239  C CG1 . VAL A 28  ? 0.2959 0.2838 0.4910 0.0653  0.0639  -0.0833 30  VAL A CG1 
240  C CG2 . VAL A 28  ? 0.3711 0.3330 0.5576 0.0653  0.0698  -0.0805 30  VAL A CG2 
241  N N   . VAL A 29  ? 0.2659 0.2528 0.4512 0.0593  0.0471  -0.0739 31  VAL A N   
242  C CA  . VAL A 29  ? 0.2498 0.2462 0.4318 0.0539  0.0412  -0.0747 31  VAL A CA  
243  C C   . VAL A 29  ? 0.2908 0.3020 0.4754 0.0501  0.0425  -0.0803 31  VAL A C   
244  O O   . VAL A 29  ? 0.3051 0.3224 0.4980 0.0565  0.0454  -0.0808 31  VAL A O   
245  C CB  . VAL A 29  ? 0.3174 0.3144 0.4958 0.0587  0.0335  -0.0650 31  VAL A CB  
246  C CG1 . VAL A 29  ? 0.3418 0.3489 0.5106 0.0513  0.0266  -0.0637 31  VAL A CG1 
247  C CG2 . VAL A 29  ? 0.3275 0.3110 0.5015 0.0610  0.0313  -0.0595 31  VAL A CG2 
248  N N   . GLU A 30  ? 0.3173 0.3349 0.4944 0.0399  0.0404  -0.0844 32  GLU A N   
249  C CA  . GLU A 30  ? 0.3206 0.3533 0.4985 0.0350  0.0403  -0.0890 32  GLU A CA  
250  C C   . GLU A 30  ? 0.2730 0.3133 0.4427 0.0323  0.0320  -0.0830 32  GLU A C   
251  O O   . GLU A 30  ? 0.3132 0.3506 0.4723 0.0265  0.0271  -0.0803 32  GLU A O   
252  C CB  . GLU A 30  ? 0.4553 0.4914 0.6307 0.0254  0.0438  -0.0975 32  GLU A CB  
253  C CG  . GLU A 30  ? 0.6385 0.6680 0.8222 0.0275  0.0529  -0.1047 32  GLU A CG  
254  C CD  . GLU A 30  ? 0.7770 0.8145 0.9607 0.0184  0.0572  -0.1143 32  GLU A CD  
255  O OE1 . GLU A 30  ? 0.7978 0.8364 0.9734 0.0098  0.0552  -0.1157 32  GLU A OE1 
256  O OE2 . GLU A 30  ? 0.8306 0.8738 1.0221 0.0201  0.0626  -0.1203 32  GLU A OE2 
257  N N   . TRP A 31  ? 0.2802 0.3302 0.4544 0.0367  0.0306  -0.0808 33  TRP A N   
258  C CA  . TRP A 31  ? 0.2038 0.2602 0.3707 0.0349  0.0232  -0.0747 33  TRP A CA  
259  C C   . TRP A 31  ? 0.2163 0.2859 0.3779 0.0254  0.0212  -0.0788 33  TRP A C   
260  O O   . TRP A 31  ? 0.2596 0.3395 0.4275 0.0241  0.0253  -0.0851 33  TRP A O   
261  C CB  . TRP A 31  ? 0.2590 0.3208 0.4330 0.0441  0.0227  -0.0698 33  TRP A CB  
262  C CG  . TRP A 31  ? 0.2464 0.2963 0.4265 0.0541  0.0249  -0.0654 33  TRP A CG  
263  C CD1 . TRP A 31  ? 0.3020 0.3484 0.4932 0.0623  0.0319  -0.0676 33  TRP A CD1 
264  C CD2 . TRP A 31  ? 0.2797 0.3193 0.4548 0.0572  0.0202  -0.0578 33  TRP A CD2 
265  N NE1 . TRP A 31  ? 0.3112 0.3457 0.5046 0.0701  0.0319  -0.0617 33  TRP A NE1 
266  C CE2 . TRP A 31  ? 0.3128 0.3436 0.4968 0.0671  0.0245  -0.0556 33  TRP A CE2 
267  C CE3 . TRP A 31  ? 0.2476 0.2840 0.4111 0.0527  0.0129  -0.0525 33  TRP A CE3 
268  C CZ2 . TRP A 31  ? 0.3416 0.3619 0.5240 0.0723  0.0214  -0.0485 33  TRP A CZ2 
269  C CZ3 . TRP A 31  ? 0.3668 0.3925 0.5284 0.0582  0.0100  -0.0456 33  TRP A CZ3 
270  C CH2 . TRP A 31  ? 0.3985 0.4170 0.5699 0.0678  0.0140  -0.0436 33  TRP A CH2 
271  N N   . GLY A 32  ? 0.1900 0.2590 0.3394 0.0190  0.0150  -0.0750 34  GLY A N   
272  C CA  . GLY A 32  ? 0.2057 0.2864 0.3486 0.0101  0.0124  -0.0774 34  GLY A CA  
273  C C   . GLY A 32  ? 0.2257 0.3169 0.3680 0.0110  0.0087  -0.0738 34  GLY A C   
274  O O   . GLY A 32  ? 0.2177 0.3100 0.3667 0.0192  0.0090  -0.0702 34  GLY A O   
275  N N   . ASN A 33  ? 0.1966 0.2962 0.3303 0.0021  0.0054  -0.0747 35  ASN A N   
276  C CA  . ASN A 33  ? 0.2167 0.3282 0.3480 0.0002  0.0019  -0.0723 35  ASN A CA  
277  C C   . ASN A 33  ? 0.1926 0.2949 0.3115 -0.0015 -0.0041 -0.0648 35  ASN A C   
278  O O   . ASN A 33  ? 0.2005 0.2968 0.3068 -0.0090 -0.0071 -0.0638 35  ASN A O   
279  C CB  . ASN A 33  ? 0.2946 0.4199 0.4227 -0.0092 0.0019  -0.0776 35  ASN A CB  
280  C CG  . ASN A 33  ? 0.6211 0.7637 0.7527 -0.0094 0.0010  -0.0778 35  ASN A CG  
281  O OD1 . ASN A 33  ? 0.8334 0.9802 0.9730 -0.0011 0.0019  -0.0752 35  ASN A OD1 
282  N ND2 . ASN A 33  ? 0.7010 0.8551 0.8266 -0.0189 -0.0007 -0.0807 35  ASN A ND2 
283  N N   . GLN A 34  ? 0.1940 0.2958 0.3163 0.0056  -0.0057 -0.0595 36  GLN A N   
284  C CA  . GLN A 34  ? 0.1797 0.2724 0.2906 0.0045  -0.0111 -0.0527 36  GLN A CA  
285  C C   . GLN A 34  ? 0.1676 0.2661 0.2656 -0.0060 -0.0151 -0.0523 36  GLN A C   
286  O O   . GLN A 34  ? 0.2143 0.3016 0.2988 -0.0099 -0.0190 -0.0481 36  GLN A O   
287  C CB  . GLN A 34  ? 0.2361 0.3306 0.3543 0.0138  -0.0118 -0.0475 36  GLN A CB  
288  C CG  . GLN A 34  ? 0.2476 0.3320 0.3554 0.0139  -0.0171 -0.0404 36  GLN A CG  
289  C CD  . GLN A 34  ? 0.2613 0.3555 0.3607 0.0073  -0.0209 -0.0386 36  GLN A CD  
290  O OE1 . GLN A 34  ? 0.2520 0.3633 0.3562 0.0050  -0.0196 -0.0416 36  GLN A OE1 
291  N NE2 . GLN A 34  ? 0.2637 0.3471 0.3498 0.0039  -0.0254 -0.0337 36  GLN A NE2 
292  N N   . ASP A 35  ? 0.1818 0.2973 0.2828 -0.0107 -0.0140 -0.0566 37  ASP A N   
293  C CA  . ASP A 35  ? 0.1991 0.3196 0.2872 -0.0214 -0.0176 -0.0562 37  ASP A CA  
294  C C   . ASP A 35  ? 0.2076 0.3208 0.2847 -0.0301 -0.0180 -0.0586 37  ASP A C   
295  O O   . ASP A 35  ? 0.2486 0.3632 0.3133 -0.0393 -0.0207 -0.0581 37  ASP A O   
296  C CB  . ASP A 35  ? 0.2652 0.4075 0.3592 -0.0241 -0.0167 -0.0597 37  ASP A CB  
297  C CG  . ASP A 35  ? 0.4028 0.5555 0.5104 -0.0207 -0.0116 -0.0660 37  ASP A CG  
298  O OD1 . ASP A 35  ? 0.4420 0.5923 0.5616 -0.0104 -0.0083 -0.0659 37  ASP A OD1 
299  O OD2 . ASP A 35  ? 0.5554 0.7177 0.6613 -0.0282 -0.0108 -0.0710 37  ASP A OD2 
300  N N   . ASP A 36  ? 0.1861 0.2919 0.2671 -0.0276 -0.0151 -0.0612 38  ASP A N   
301  C CA  . ASP A 36  ? 0.1861 0.2858 0.2566 -0.0352 -0.0153 -0.0626 38  ASP A CA  
302  C C   . ASP A 36  ? 0.2053 0.2878 0.2598 -0.0369 -0.0190 -0.0562 38  ASP A C   
303  O O   . ASP A 36  ? 0.2407 0.3183 0.2837 -0.0436 -0.0196 -0.0562 38  ASP A O   
304  C CB  . ASP A 36  ? 0.2283 0.3257 0.3070 -0.0321 -0.0109 -0.0670 38  ASP A CB  
305  C CG  . ASP A 36  ? 0.2877 0.4013 0.3788 -0.0331 -0.0067 -0.0745 38  ASP A CG  
306  O OD1 . ASP A 36  ? 0.2496 0.3773 0.3421 -0.0369 -0.0075 -0.0765 38  ASP A OD1 
307  O OD2 . ASP A 36  ? 0.3175 0.4297 0.4166 -0.0303 -0.0026 -0.0787 38  ASP A OD2 
308  N N   . TYR A 37  ? 0.2254 0.2988 0.2787 -0.0307 -0.0213 -0.0506 39  TYR A N   
309  C CA  . TYR A 37  ? 0.2182 0.2739 0.2579 -0.0302 -0.0243 -0.0445 39  TYR A CA  
310  C C   . TYR A 37  ? 0.2483 0.3012 0.2793 -0.0317 -0.0282 -0.0397 39  TYR A C   
311  O O   . TYR A 37  ? 0.3299 0.3889 0.3698 -0.0264 -0.0287 -0.0384 39  TYR A O   
312  C CB  . TYR A 37  ? 0.1929 0.2386 0.2392 -0.0207 -0.0232 -0.0422 39  TYR A CB  
313  C CG  . TYR A 37  ? 0.1780 0.2276 0.2331 -0.0201 -0.0188 -0.0477 39  TYR A CG  
314  C CD1 . TYR A 37  ? 0.2087 0.2661 0.2806 -0.0143 -0.0151 -0.0518 39  TYR A CD1 
315  C CD2 . TYR A 37  ? 0.1731 0.2195 0.2196 -0.0257 -0.0180 -0.0492 39  TYR A CD2 
316  C CE1 . TYR A 37  ? 0.1785 0.2391 0.2578 -0.0146 -0.0106 -0.0575 39  TYR A CE1 
317  C CE2 . TYR A 37  ? 0.1722 0.2238 0.2266 -0.0261 -0.0138 -0.0547 39  TYR A CE2 
318  C CZ  . TYR A 37  ? 0.1837 0.2419 0.2543 -0.0209 -0.0101 -0.0591 39  TYR A CZ  
319  O OH  . TYR A 37  ? 0.2320 0.2949 0.3101 -0.0219 -0.0055 -0.0652 39  TYR A OH  
320  N N   . GLN A 38  ? 0.2341 0.2782 0.2477 -0.0389 -0.0306 -0.0370 40  GLN A N   
321  C CA  . GLN A 38  ? 0.2447 0.2838 0.2473 -0.0416 -0.0340 -0.0327 40  GLN A CA  
322  C C   . GLN A 38  ? 0.2586 0.2774 0.2490 -0.0380 -0.0362 -0.0264 40  GLN A C   
323  O O   . GLN A 38  ? 0.2963 0.3044 0.2754 -0.0405 -0.0358 -0.0253 40  GLN A O   
324  C CB  . GLN A 38  ? 0.3779 0.4217 0.3686 -0.0534 -0.0347 -0.0346 40  GLN A CB  
325  C CG  . GLN A 38  ? 0.5696 0.6345 0.5719 -0.0571 -0.0326 -0.0408 40  GLN A CG  
326  C CD  . GLN A 38  ? 0.6935 0.7664 0.6859 -0.0681 -0.0340 -0.0421 40  GLN A CD  
327  O OE1 . GLN A 38  ? 0.8032 0.8637 0.7780 -0.0745 -0.0358 -0.0389 40  GLN A OE1 
328  N NE2 . GLN A 38  ? 0.6094 0.7030 0.6126 -0.0703 -0.0328 -0.0466 40  GLN A NE2 
329  N N   . LEU A 39  ? 0.2256 0.2402 0.2181 -0.0320 -0.0384 -0.0222 41  LEU A N   
330  C CA  . LEU A 39  ? 0.2394 0.2355 0.2206 -0.0279 -0.0406 -0.0161 41  LEU A CA  
331  C C   . LEU A 39  ? 0.3076 0.2923 0.2675 -0.0361 -0.0425 -0.0135 41  LEU A C   
332  O O   . LEU A 39  ? 0.3136 0.3048 0.2689 -0.0435 -0.0432 -0.0149 41  LEU A O   
333  C CB  . LEU A 39  ? 0.2535 0.2493 0.2430 -0.0195 -0.0425 -0.0124 41  LEU A CB  
334  C CG  . LEU A 39  ? 0.2398 0.2451 0.2498 -0.0105 -0.0404 -0.0143 41  LEU A CG  
335  C CD1 . LEU A 39  ? 0.2873 0.2927 0.3036 -0.0029 -0.0425 -0.0099 41  LEU A CD1 
336  C CD2 . LEU A 39  ? 0.2277 0.2254 0.2406 -0.0060 -0.0383 -0.0148 41  LEU A CD2 
337  N N   . VAL A 40  ? 0.2942 0.2620 0.2405 -0.0349 -0.0430 -0.0096 42  VAL A N   
338  C CA  . VAL A 40  ? 0.3059 0.2598 0.2304 -0.0419 -0.0438 -0.0068 42  VAL A CA  
339  C C   . VAL A 40  ? 0.3742 0.3107 0.2870 -0.0372 -0.0464 -0.0003 42  VAL A C   
340  O O   . VAL A 40  ? 0.3626 0.2914 0.2619 -0.0424 -0.0478 0.0016  42  VAL A O   
341  C CB  . VAL A 40  ? 0.3796 0.3285 0.2954 -0.0451 -0.0414 -0.0075 42  VAL A CB  
342  C CG1 . VAL A 40  ? 0.3897 0.3208 0.2815 -0.0503 -0.0418 -0.0033 42  VAL A CG1 
343  C CG2 . VAL A 40  ? 0.3852 0.3513 0.3104 -0.0514 -0.0390 -0.0141 42  VAL A CG2 
344  N N   . ARG A 41  ? 0.3428 0.2733 0.2603 -0.0275 -0.0470 0.0029  43  ARG A N   
345  C CA  . ARG A 41  ? 0.4030 0.3165 0.3084 -0.0224 -0.0494 0.0094  43  ARG A CA  
346  C C   . ARG A 41  ? 0.3461 0.2612 0.2651 -0.0114 -0.0504 0.0115  43  ARG A C   
347  O O   . ARG A 41  ? 0.3497 0.2709 0.2789 -0.0081 -0.0485 0.0093  43  ARG A O   
348  C CB  . ARG A 41  ? 0.5862 0.4836 0.4715 -0.0243 -0.0484 0.0126  43  ARG A CB  
349  C CG  . ARG A 41  ? 0.7733 0.6518 0.6415 -0.0214 -0.0505 0.0189  43  ARG A CG  
350  C CD  . ARG A 41  ? 0.8221 0.6852 0.6711 -0.0214 -0.0488 0.0227  43  ARG A CD  
351  N NE  . ARG A 41  ? 0.8267 0.6955 0.6729 -0.0290 -0.0458 0.0190  43  ARG A NE  
352  C CZ  . ARG A 41  ? 0.9296 0.8006 0.7759 -0.0269 -0.0435 0.0191  43  ARG A CZ  
353  N NH1 . ARG A 41  ? 0.9327 0.8005 0.7808 -0.0178 -0.0440 0.0227  43  ARG A NH1 
354  N NH2 . ARG A 41  ? 0.9583 0.8356 0.8024 -0.0342 -0.0408 0.0155  43  ARG A NH2 
355  N N   . LYS A 42  ? 0.3336 0.2435 0.2525 -0.0063 -0.0533 0.0155  44  LYS A N   
356  C CA  . LYS A 42  ? 0.3357 0.2449 0.2652 0.0042  -0.0545 0.0185  44  LYS A CA  
357  C C   . LYS A 42  ? 0.3410 0.2351 0.2569 0.0084  -0.0549 0.0232  44  LYS A C   
358  O O   . LYS A 42  ? 0.4006 0.2806 0.2977 0.0063  -0.0560 0.0270  44  LYS A O   
359  C CB  . LYS A 42  ? 0.3572 0.2671 0.2913 0.0084  -0.0575 0.0215  44  LYS A CB  
360  C CG  . LYS A 42  ? 0.4093 0.3204 0.3565 0.0192  -0.0586 0.0244  44  LYS A CG  
361  C CD  . LYS A 42  ? 0.4799 0.4001 0.4392 0.0228  -0.0604 0.0254  44  LYS A CD  
362  C CE  . LYS A 42  ? 0.5986 0.5112 0.5443 0.0199  -0.0634 0.0288  44  LYS A CE  
363  N NZ  . LYS A 42  ? 0.6562 0.5806 0.6142 0.0229  -0.0649 0.0296  44  LYS A NZ  
364  N N   . LEU A 43  ? 0.2279 0.2939 0.3128 -0.0245 -0.0313 -0.0223 45  LEU A N   
365  C CA  . LEU A 43  ? 0.2573 0.3181 0.3438 -0.0259 -0.0324 -0.0240 45  LEU A CA  
366  C C   . LEU A 43  ? 0.3366 0.3970 0.4205 -0.0259 -0.0321 -0.0288 45  LEU A C   
367  O O   . LEU A 43  ? 0.3741 0.4335 0.4638 -0.0278 -0.0336 -0.0328 45  LEU A O   
368  C CB  . LEU A 43  ? 0.2892 0.3447 0.3698 -0.0251 -0.0316 -0.0205 45  LEU A CB  
369  C CG  . LEU A 43  ? 0.2945 0.3504 0.3767 -0.0260 -0.0319 -0.0155 45  LEU A CG  
370  C CD1 . LEU A 43  ? 0.2739 0.3259 0.3495 -0.0253 -0.0311 -0.0129 45  LEU A CD1 
371  C CD2 . LEU A 43  ? 0.3534 0.4090 0.4459 -0.0289 -0.0348 -0.0151 45  LEU A CD2 
372  N N   . GLY A 44  ? 0.2865 0.3478 0.3623 -0.0241 -0.0304 -0.0286 46  GLY A N   
373  C CA  . GLY A 44  ? 0.3496 0.4108 0.4218 -0.0249 -0.0298 -0.0325 46  GLY A CA  
374  C C   . GLY A 44  ? 0.3004 0.3629 0.3639 -0.0230 -0.0285 -0.0306 46  GLY A C   
375  O O   . GLY A 44  ? 0.2506 0.3134 0.3113 -0.0204 -0.0281 -0.0268 46  GLY A O   
376  N N   . ARG A 45  ? 0.2458 0.3096 0.3056 -0.0244 -0.0281 -0.0337 47  ARG A N   
377  C CA  . ARG A 45  ? 0.2586 0.3229 0.3094 -0.0230 -0.0274 -0.0315 47  ARG A CA  
378  C C   . ARG A 45  ? 0.3551 0.4157 0.3992 -0.0251 -0.0256 -0.0334 47  ARG A C   
379  O O   . ARG A 45  ? 0.3388 0.4010 0.3867 -0.0284 -0.0254 -0.0386 47  ARG A O   
380  C CB  . ARG A 45  ? 0.3023 0.3752 0.3549 -0.0233 -0.0291 -0.0327 47  ARG A CB  
381  C CG  . ARG A 45  ? 0.4229 0.4959 0.4653 -0.0223 -0.0290 -0.0302 47  ARG A CG  
382  C CD  . ARG A 45  ? 0.5668 0.6492 0.6100 -0.0231 -0.0309 -0.0323 47  ARG A CD  
383  N NE  . ARG A 45  ? 0.6315 0.7182 0.6788 -0.0199 -0.0327 -0.0304 47  ARG A NE  
384  C CZ  . ARG A 45  ? 0.6024 0.6983 0.6521 -0.0198 -0.0347 -0.0323 47  ARG A CZ  
385  N NH1 . ARG A 45  ? 0.5786 0.6808 0.6263 -0.0228 -0.0351 -0.0361 47  ARG A NH1 
386  N NH2 . ARG A 45  ? 0.5563 0.6561 0.6105 -0.0168 -0.0362 -0.0311 47  ARG A NH2 
387  N N   . GLY A 46  ? 0.3243 0.3801 0.3593 -0.0234 -0.0244 -0.0294 48  GLY A N   
388  C CA  . GLY A 46  ? 0.3115 0.3633 0.3392 -0.0257 -0.0224 -0.0303 48  GLY A CA  
389  C C   . GLY A 46  ? 0.3572 0.4075 0.3756 -0.0244 -0.0226 -0.0255 48  GLY A C   
390  O O   . GLY A 46  ? 0.4010 0.4544 0.4194 -0.0215 -0.0248 -0.0223 48  GLY A O   
391  N N   . LYS A 47  ? 0.4172 0.4626 0.4279 -0.0266 -0.0205 -0.0248 49  LYS A N   
392  C CA  . LYS A 47  ? 0.4479 0.4908 0.4495 -0.0256 -0.0211 -0.0193 49  LYS A CA  
393  C C   . LYS A 47  ? 0.4285 0.4650 0.4297 -0.0205 -0.0219 -0.0139 49  LYS A C   
394  O O   . LYS A 47  ? 0.5564 0.5920 0.5529 -0.0182 -0.0240 -0.0090 49  LYS A O   
395  C CB  . LYS A 47  ? 0.5821 0.6207 0.5755 -0.0300 -0.0183 -0.0197 49  LYS A CB  
396  C CG  . LYS A 47  ? 0.7072 0.7520 0.6934 -0.0336 -0.0191 -0.0191 49  LYS A CG  
397  C CD  . LYS A 47  ? 0.7362 0.7926 0.7290 -0.0359 -0.0203 -0.0255 49  LYS A CD  
398  C CE  . LYS A 47  ? 0.8264 0.8911 0.8126 -0.0380 -0.0222 -0.0243 49  LYS A CE  
399  N NZ  . LYS A 47  ? 0.8197 0.8968 0.8142 -0.0399 -0.0234 -0.0314 49  LYS A NZ  
400  N N   . TYR A 48  ? 0.4496 0.4824 0.4561 -0.0186 -0.0205 -0.0151 50  TYR A N   
401  C CA  . TYR A 48  ? 0.4401 0.4674 0.4471 -0.0142 -0.0206 -0.0114 50  TYR A CA  
402  C C   . TYR A 48  ? 0.3589 0.3906 0.3732 -0.0108 -0.0222 -0.0116 50  TYR A C   
403  O O   . TYR A 48  ? 0.3449 0.3741 0.3604 -0.0071 -0.0226 -0.0091 50  TYR A O   
404  C CB  . TYR A 48  ? 0.5137 0.5336 0.5202 -0.0149 -0.0174 -0.0128 50  TYR A CB  
405  C CG  . TYR A 48  ? 0.6468 0.6609 0.6458 -0.0181 -0.0153 -0.0120 50  TYR A CG  
406  C CD1 . TYR A 48  ? 0.6920 0.7041 0.6842 -0.0180 -0.0168 -0.0069 50  TYR A CD1 
407  C CD2 . TYR A 48  ? 0.6967 0.7076 0.6955 -0.0213 -0.0120 -0.0161 50  TYR A CD2 
408  C CE1 . TYR A 48  ? 0.8028 0.8094 0.7874 -0.0217 -0.0147 -0.0054 50  TYR A CE1 
409  C CE2 . TYR A 48  ? 0.7793 0.7852 0.7714 -0.0249 -0.0096 -0.0156 50  TYR A CE2 
410  C CZ  . TYR A 48  ? 0.8536 0.8572 0.8382 -0.0253 -0.0108 -0.0099 50  TYR A CZ  
411  O OH  . TYR A 48  ? 0.8812 0.8798 0.8584 -0.0296 -0.0082 -0.0087 50  TYR A OH  
412  N N   . SER A 49  ? 0.2783 0.3164 0.2981 -0.0122 -0.0228 -0.0146 51  SER A N   
413  C CA  . SER A 49  ? 0.2379 0.2799 0.2643 -0.0098 -0.0237 -0.0146 51  SER A CA  
414  C C   . SER A 49  ? 0.2630 0.3121 0.2952 -0.0120 -0.0249 -0.0173 51  SER A C   
415  O O   . SER A 49  ? 0.2471 0.2979 0.2794 -0.0152 -0.0250 -0.0201 51  SER A O   
416  C CB  . SER A 49  ? 0.2587 0.2970 0.2873 -0.0090 -0.0216 -0.0152 51  SER A CB  
417  O OG  . SER A 49  ? 0.3617 0.3990 0.3918 -0.0122 -0.0205 -0.0183 51  SER A OG  
418  N N   . GLU A 50  ? 0.2087 0.2622 0.2466 -0.0104 -0.0258 -0.0168 52  GLU A N   
419  C CA  . GLU A 50  ? 0.2152 0.2738 0.2603 -0.0125 -0.0265 -0.0190 52  GLU A CA  
420  C C   . GLU A 50  ? 0.2542 0.3115 0.3026 -0.0124 -0.0254 -0.0181 52  GLU A C   
421  O O   . GLU A 50  ? 0.2443 0.3007 0.2912 -0.0099 -0.0245 -0.0163 52  GLU A O   
422  C CB  . GLU A 50  ? 0.2116 0.2781 0.2608 -0.0117 -0.0285 -0.0192 52  GLU A CB  
423  C CG  . GLU A 50  ? 0.3183 0.3884 0.3649 -0.0125 -0.0300 -0.0206 52  GLU A CG  
424  C CD  . GLU A 50  ? 0.4673 0.5464 0.5198 -0.0119 -0.0320 -0.0221 52  GLU A CD  
425  O OE1 . GLU A 50  ? 0.4576 0.5391 0.5135 -0.0096 -0.0323 -0.0208 52  GLU A OE1 
426  O OE2 . GLU A 50  ? 0.5064 0.5908 0.5605 -0.0141 -0.0331 -0.0252 52  GLU A OE2 
427  N N   . VAL A 51  ? 0.2283 0.2861 0.2816 -0.0150 -0.0257 -0.0195 53  VAL A N   
428  C CA  . VAL A 51  ? 0.1721 0.2283 0.2273 -0.0155 -0.0250 -0.0181 53  VAL A CA  
429  C C   . VAL A 51  ? 0.2142 0.2751 0.2766 -0.0173 -0.0262 -0.0175 53  VAL A C   
430  O O   . VAL A 51  ? 0.2149 0.2781 0.2827 -0.0192 -0.0277 -0.0195 53  VAL A O   
431  C CB  . VAL A 51  ? 0.2756 0.3263 0.3295 -0.0171 -0.0246 -0.0196 53  VAL A CB  
432  C CG1 . VAL A 51  ? 0.2996 0.3495 0.3555 -0.0179 -0.0247 -0.0178 53  VAL A CG1 
433  C CG2 . VAL A 51  ? 0.3132 0.3592 0.3604 -0.0154 -0.0228 -0.0200 53  VAL A CG2 
434  N N   . PHE A 52  ? 0.1618 0.2248 0.2248 -0.0171 -0.0253 -0.0150 54  PHE A N   
435  C CA  . PHE A 52  ? 0.1814 0.2489 0.2506 -0.0192 -0.0258 -0.0137 54  PHE A CA  
436  C C   . PHE A 52  ? 0.1999 0.2659 0.2686 -0.0211 -0.0253 -0.0107 54  PHE A C   
437  O O   . PHE A 52  ? 0.2080 0.2725 0.2714 -0.0199 -0.0238 -0.0099 54  PHE A O   
438  C CB  . PHE A 52  ? 0.1855 0.2593 0.2558 -0.0175 -0.0250 -0.0137 54  PHE A CB  
439  C CG  . PHE A 52  ? 0.1757 0.2521 0.2463 -0.0155 -0.0261 -0.0160 54  PHE A CG  
440  C CD1 . PHE A 52  ? 0.1664 0.2401 0.2308 -0.0125 -0.0261 -0.0163 54  PHE A CD1 
441  C CD2 . PHE A 52  ? 0.1919 0.2737 0.2691 -0.0167 -0.0274 -0.0177 54  PHE A CD2 
442  C CE1 . PHE A 52  ? 0.2041 0.2803 0.2678 -0.0109 -0.0276 -0.0176 54  PHE A CE1 
443  C CE2 . PHE A 52  ? 0.2021 0.2875 0.2791 -0.0149 -0.0287 -0.0200 54  PHE A CE2 
444  C CZ  . PHE A 52  ? 0.2120 0.2946 0.2817 -0.0120 -0.0290 -0.0196 54  PHE A CZ  
445  N N   . GLU A 53  ? 0.1934 0.2602 0.2681 -0.0241 -0.0266 -0.0090 55  GLU A N   
446  C CA  . GLU A 53  ? 0.2417 0.3093 0.3157 -0.0265 -0.0260 -0.0050 55  GLU A CA  
447  C C   . GLU A 53  ? 0.2092 0.2839 0.2837 -0.0267 -0.0238 -0.0044 55  GLU A C   
448  O O   . GLU A 53  ? 0.2244 0.3032 0.3037 -0.0263 -0.0239 -0.0064 55  GLU A O   
449  C CB  . GLU A 53  ? 0.3005 0.3654 0.3811 -0.0299 -0.0287 -0.0027 55  GLU A CB  
450  C CG  . GLU A 53  ? 0.3960 0.4610 0.4750 -0.0330 -0.0286 0.0027  55  GLU A CG  
451  C CD  . GLU A 53  ? 0.5679 0.6290 0.6545 -0.0363 -0.0320 0.0056  55  GLU A CD  
452  O OE1 . GLU A 53  ? 0.6018 0.6573 0.6908 -0.0358 -0.0349 0.0045  55  GLU A OE1 
453  O OE2 . GLU A 53  ? 0.5961 0.6600 0.6873 -0.0394 -0.0317 0.0086  55  GLU A OE2 
454  N N   . ALA A 54  ? 0.1967 0.2739 0.2666 -0.0273 -0.0217 -0.0025 56  ALA A N   
455  C CA  . ALA A 54  ? 0.1594 0.2444 0.2301 -0.0278 -0.0193 -0.0030 56  ALA A CA  
456  C C   . ALA A 54  ? 0.1951 0.2830 0.2630 -0.0317 -0.0177 0.0008  56  ALA A C   
457  O O   . ALA A 54  ? 0.2147 0.2983 0.2792 -0.0333 -0.0189 0.0039  56  ALA A O   
458  C CB  . ALA A 54  ? 0.2123 0.2997 0.2800 -0.0235 -0.0177 -0.0066 56  ALA A CB  
459  N N   . ILE A 55  ? 0.2343 0.3302 0.3037 -0.0334 -0.0151 0.0002  57  ILE A N   
460  C CA  . ILE A 55  ? 0.2184 0.3193 0.2842 -0.0376 -0.0129 0.0031  57  ILE A CA  
461  C C   . ILE A 55  ? 0.2102 0.3189 0.2738 -0.0357 -0.0097 -0.0013 57  ILE A C   
462  O O   . ILE A 55  ? 0.1989 0.3117 0.2668 -0.0329 -0.0089 -0.0058 57  ILE A O   
463  C CB  . ILE A 55  ? 0.2672 0.3719 0.3378 -0.0429 -0.0122 0.0062  57  ILE A CB  
464  C CG1 . ILE A 55  ? 0.3660 0.4625 0.4401 -0.0450 -0.0157 0.0107  57  ILE A CG1 
465  C CG2 . ILE A 55  ? 0.2752 0.3870 0.3411 -0.0478 -0.0091 0.0089  57  ILE A CG2 
466  C CD1 . ILE A 55  ? 0.5217 0.6203 0.6010 -0.0506 -0.0152 0.0145  57  ILE A CD1 
467  N N   . ASN A 56  ? 0.1746 0.2855 0.2322 -0.0369 -0.0082 -0.0005 58  ASN A N   
468  C CA  . ASN A 56  ? 0.1726 0.2927 0.2291 -0.0362 -0.0049 -0.0051 58  ASN A CA  
469  C C   . ASN A 56  ? 0.2077 0.3374 0.2649 -0.0420 -0.0020 -0.0039 58  ASN A C   
470  O O   . ASN A 56  ? 0.2308 0.3620 0.2829 -0.0471 -0.0014 0.0009  58  ASN A O   
471  C CB  . ASN A 56  ? 0.2236 0.3428 0.2739 -0.0353 -0.0045 -0.0055 58  ASN A CB  
472  C CG  . ASN A 56  ? 0.2286 0.3579 0.2790 -0.0345 -0.0011 -0.0113 58  ASN A CG  
473  O OD1 . ASN A 56  ? 0.2260 0.3642 0.2807 -0.0357 0.0013  -0.0146 58  ASN A OD1 
474  N ND2 . ASN A 56  ? 0.2871 0.4156 0.3339 -0.0325 -0.0007 -0.0133 58  ASN A ND2 
475  N N   . ILE A 57  ? 0.1999 0.3365 0.2634 -0.0416 -0.0002 -0.0083 59  ILE A N   
476  C CA  . ILE A 57  ? 0.1853 0.3312 0.2503 -0.0477 0.0029  -0.0076 59  ILE A CA  
477  C C   . ILE A 57  ? 0.2257 0.3830 0.2871 -0.0508 0.0069  -0.0106 59  ILE A C   
478  O O   . ILE A 57  ? 0.2423 0.4088 0.3043 -0.0567 0.0101  -0.0105 59  ILE A O   
479  C CB  . ILE A 57  ? 0.2577 0.4079 0.3318 -0.0465 0.0034  -0.0119 59  ILE A CB  
480  C CG1 . ILE A 57  ? 0.1911 0.3472 0.2695 -0.0411 0.0042  -0.0201 59  ILE A CG1 
481  C CG2 . ILE A 57  ? 0.2225 0.3630 0.3002 -0.0441 -0.0004 -0.0093 59  ILE A CG2 
482  C CD1 . ILE A 57  ? 0.2299 0.3936 0.3174 -0.0406 0.0051  -0.0253 59  ILE A CD1 
483  N N   . THR A 58  ? 0.2594 0.4171 0.3175 -0.0474 0.0070  -0.0137 60  THR A N   
484  C CA  . THR A 58  ? 0.2570 0.4263 0.3114 -0.0510 0.0107  -0.0165 60  THR A CA  
485  C C   . THR A 58  ? 0.2944 0.4623 0.3389 -0.0562 0.0104  -0.0093 60  THR A C   
486  O O   . THR A 58  ? 0.3120 0.4911 0.3521 -0.0612 0.0138  -0.0102 60  THR A O   
487  C CB  . THR A 58  ? 0.2689 0.4408 0.3257 -0.0452 0.0112  -0.0242 60  THR A CB  
488  O OG1 . THR A 58  ? 0.3275 0.4890 0.3795 -0.0417 0.0084  -0.0214 60  THR A OG1 
489  C CG2 . THR A 58  ? 0.3200 0.4914 0.3863 -0.0394 0.0103  -0.0303 60  THR A CG2 
490  N N   . ASN A 59  ? 0.3034 0.4587 0.3447 -0.0554 0.0064  -0.0024 61  ASN A N   
491  C CA  . ASN A 59  ? 0.2798 0.4327 0.3127 -0.0602 0.0050  0.0055  61  ASN A CA  
492  C C   . ASN A 59  ? 0.2452 0.3870 0.2791 -0.0620 0.0012  0.0135  61  ASN A C   
493  O O   . ASN A 59  ? 0.3252 0.4628 0.3531 -0.0654 -0.0011 0.0208  61  ASN A O   
494  C CB  . ASN A 59  ? 0.2958 0.4454 0.3235 -0.0567 0.0033  0.0045  61  ASN A CB  
495  C CG  . ASN A 59  ? 0.2952 0.4327 0.3268 -0.0496 -0.0001 0.0027  61  ASN A CG  
496  O OD1 . ASN A 59  ? 0.2991 0.4289 0.3356 -0.0481 -0.0022 0.0044  61  ASN A OD1 
497  N ND2 . ASN A 59  ? 0.3399 0.4761 0.3693 -0.0457 -0.0004 -0.0009 61  ASN A ND2 
498  N N   . ASN A 60  ? 0.2638 0.4011 0.3057 -0.0599 0.0003  0.0122  62  ASN A N   
499  C CA  . ASN A 60  ? 0.2302 0.3576 0.2757 -0.0612 -0.0032 0.0182  62  ASN A CA  
500  C C   . ASN A 60  ? 0.2572 0.3734 0.3000 -0.0586 -0.0080 0.0220  62  ASN A C   
501  O O   . ASN A 60  ? 0.4028 0.5119 0.4460 -0.0614 -0.0112 0.0287  62  ASN A O   
502  C CB  . ASN A 60  ? 0.2673 0.3980 0.3120 -0.0692 -0.0020 0.0248  62  ASN A CB  
503  C CG  . ASN A 60  ? 0.3723 0.5123 0.4230 -0.0716 0.0022  0.0205  62  ASN A CG  
504  O OD1 . ASN A 60  ? 0.4530 0.5987 0.5026 -0.0787 0.0048  0.0241  62  ASN A OD1 
505  N ND2 . ASN A 60  ? 0.2924 0.4341 0.3497 -0.0658 0.0027  0.0126  62  ASN A ND2 
506  N N   . GLU A 61  ? 0.2494 0.3634 0.2904 -0.0530 -0.0085 0.0173  63  GLU A N   
507  C CA  . GLU A 61  ? 0.3228 0.4269 0.3618 -0.0501 -0.0126 0.0192  63  GLU A CA  
508  C C   . GLU A 61  ? 0.3107 0.4075 0.3561 -0.0448 -0.0145 0.0152  63  GLU A C   
509  O O   . GLU A 61  ? 0.2626 0.3626 0.3114 -0.0417 -0.0125 0.0098  63  GLU A O   
510  C CB  . GLU A 61  ? 0.4264 0.5335 0.4585 -0.0484 -0.0117 0.0168  63  GLU A CB  
511  C CG  . GLU A 61  ? 0.5612 0.6750 0.5857 -0.0540 -0.0109 0.0217  63  GLU A CG  
512  C CD  . GLU A 61  ? 0.7293 0.8490 0.7477 -0.0523 -0.0093 0.0177  63  GLU A CD  
513  O OE1 . GLU A 61  ? 0.7668 0.8840 0.7875 -0.0468 -0.0090 0.0115  63  GLU A OE1 
514  O OE2 . GLU A 61  ? 0.7323 0.8595 0.7437 -0.0569 -0.0083 0.0208  63  GLU A OE2 
515  N N   . LYS A 62  ? 0.3037 0.3911 0.3508 -0.0440 -0.0186 0.0178  64  LYS A N   
516  C CA  . LYS A 62  ? 0.2381 0.3193 0.2902 -0.0396 -0.0203 0.0137  64  LYS A CA  
517  C C   . LYS A 62  ? 0.2422 0.3228 0.2905 -0.0349 -0.0191 0.0086  64  LYS A C   
518  O O   . LYS A 62  ? 0.2372 0.3184 0.2799 -0.0348 -0.0189 0.0088  64  LYS A O   
519  C CB  . LYS A 62  ? 0.2557 0.3280 0.3116 -0.0402 -0.0249 0.0167  64  LYS A CB  
520  C CG  . LYS A 62  ? 0.3498 0.4211 0.4123 -0.0443 -0.0265 0.0210  64  LYS A CG  
521  C CD  . LYS A 62  ? 0.4432 0.5058 0.5118 -0.0442 -0.0314 0.0225  64  LYS A CD  
522  C CE  . LYS A 62  ? 0.5225 0.5837 0.5991 -0.0483 -0.0332 0.0268  64  LYS A CE  
523  N NZ  . LYS A 62  ? 0.5574 0.6102 0.6418 -0.0483 -0.0384 0.0278  64  LYS A NZ  
524  N N   . VAL A 63  ? 0.1781 0.2576 0.2295 -0.0313 -0.0185 0.0041  65  VAL A N   
525  C CA  . VAL A 63  ? 0.1795 0.2566 0.2286 -0.0269 -0.0177 -0.0003 65  VAL A CA  
526  C C   . VAL A 63  ? 0.1641 0.2353 0.2169 -0.0246 -0.0196 -0.0023 65  VAL A C   
527  O O   . VAL A 63  ? 0.1896 0.2604 0.2475 -0.0261 -0.0212 -0.0012 65  VAL A O   
528  C CB  . VAL A 63  ? 0.1641 0.2480 0.2124 -0.0248 -0.0144 -0.0040 65  VAL A CB  
529  C CG1 . VAL A 63  ? 0.2388 0.3300 0.2833 -0.0274 -0.0121 -0.0034 65  VAL A CG1 
530  C CG2 . VAL A 63  ? 0.1795 0.2675 0.2330 -0.0246 -0.0139 -0.0051 65  VAL A CG2 
531  N N   . VAL A 64  ? 0.1802 0.2474 0.2307 -0.0214 -0.0193 -0.0055 66  VAL A N   
532  C CA  . VAL A 64  ? 0.1551 0.2178 0.2077 -0.0195 -0.0206 -0.0078 66  VAL A CA  
533  C C   . VAL A 64  ? 0.1788 0.2427 0.2299 -0.0161 -0.0188 -0.0104 66  VAL A C   
534  O O   . VAL A 64  ? 0.1987 0.2630 0.2469 -0.0143 -0.0170 -0.0118 66  VAL A O   
535  C CB  . VAL A 64  ? 0.1703 0.2262 0.2217 -0.0195 -0.0221 -0.0090 66  VAL A CB  
536  C CG1 . VAL A 64  ? 0.2102 0.2625 0.2622 -0.0179 -0.0225 -0.0120 66  VAL A CG1 
537  C CG2 . VAL A 64  ? 0.1888 0.2430 0.2439 -0.0225 -0.0250 -0.0064 66  VAL A CG2 
538  N N   . VAL A 65  ? 0.1723 0.2373 0.2261 -0.0151 -0.0196 -0.0111 67  VAL A N   
539  C CA  . VAL A 65  ? 0.1433 0.2094 0.1963 -0.0116 -0.0189 -0.0129 67  VAL A CA  
540  C C   . VAL A 65  ? 0.1933 0.2540 0.2445 -0.0104 -0.0202 -0.0138 67  VAL A C   
541  O O   . VAL A 65  ? 0.1756 0.2367 0.2291 -0.0118 -0.0219 -0.0140 67  VAL A O   
542  C CB  . VAL A 65  ? 0.1426 0.2157 0.1999 -0.0113 -0.0190 -0.0130 67  VAL A CB  
543  C CG1 . VAL A 65  ? 0.1913 0.2647 0.2484 -0.0072 -0.0194 -0.0147 67  VAL A CG1 
544  C CG2 . VAL A 65  ? 0.1650 0.2442 0.2235 -0.0133 -0.0171 -0.0124 67  VAL A CG2 
545  N N   . LYS A 66  ? 0.1508 0.2072 0.1982 -0.0081 -0.0193 -0.0147 68  LYS A N   
546  C CA  . LYS A 66  ? 0.1459 0.1974 0.1903 -0.0073 -0.0201 -0.0152 68  LYS A CA  
547  C C   . LYS A 66  ? 0.1742 0.2267 0.2182 -0.0040 -0.0208 -0.0146 68  LYS A C   
548  O O   . LYS A 66  ? 0.1832 0.2342 0.2268 -0.0014 -0.0198 -0.0148 68  LYS A O   
549  C CB  . LYS A 66  ? 0.1834 0.2284 0.2241 -0.0075 -0.0186 -0.0163 68  LYS A CB  
550  C CG  . LYS A 66  ? 0.2133 0.2530 0.2499 -0.0074 -0.0186 -0.0167 68  LYS A CG  
551  C CD  . LYS A 66  ? 0.3601 0.3945 0.3945 -0.0091 -0.0171 -0.0188 68  LYS A CD  
552  C CE  . LYS A 66  ? 0.4259 0.4547 0.4570 -0.0074 -0.0151 -0.0190 68  LYS A CE  
553  N NZ  . LYS A 66  ? 0.2438 0.2679 0.2731 -0.0094 -0.0135 -0.0218 68  LYS A NZ  
554  N N   . ILE A 67  ? 0.1728 0.2281 0.2177 -0.0039 -0.0228 -0.0141 69  ILE A N   
555  C CA  . ILE A 67  ? 0.1769 0.2336 0.2217 -0.0005 -0.0245 -0.0133 69  ILE A CA  
556  C C   . ILE A 67  ? 0.2433 0.2938 0.2820 -0.0002 -0.0252 -0.0119 69  ILE A C   
557  O O   . ILE A 67  ? 0.2327 0.2835 0.2691 -0.0026 -0.0260 -0.0122 69  ILE A O   
558  C CB  . ILE A 67  ? 0.2080 0.2723 0.2571 -0.0005 -0.0264 -0.0138 69  ILE A CB  
559  C CG1 . ILE A 67  ? 0.1825 0.2526 0.2373 -0.0017 -0.0251 -0.0149 69  ILE A CG1 
560  C CG2 . ILE A 67  ? 0.2215 0.2874 0.2708 0.0035  -0.0288 -0.0130 69  ILE A CG2 
561  C CD1 . ILE A 67  ? 0.1789 0.2569 0.2392 -0.0020 -0.0265 -0.0160 69  ILE A CD1 
562  N N   . LEU A 68  ? 0.2328 0.2780 0.2693 0.0023  -0.0249 -0.0107 70  LEU A N   
563  C CA  . LEU A 68  ? 0.2847 0.3228 0.3148 0.0018  -0.0249 -0.0088 70  LEU A CA  
564  C C   . LEU A 68  ? 0.3107 0.3506 0.3379 0.0027  -0.0282 -0.0064 70  LEU A C   
565  O O   . LEU A 68  ? 0.3371 0.3813 0.3676 0.0058  -0.0307 -0.0057 70  LEU A O   
566  C CB  . LEU A 68  ? 0.2701 0.3014 0.2997 0.0042  -0.0237 -0.0080 70  LEU A CB  
567  C CG  . LEU A 68  ? 0.2693 0.2997 0.3016 0.0036  -0.0205 -0.0108 70  LEU A CG  
568  C CD1 . LEU A 68  ? 0.3240 0.3482 0.3571 0.0061  -0.0194 -0.0107 70  LEU A CD1 
569  C CD2 . LEU A 68  ? 0.3401 0.3686 0.3694 -0.0005 -0.0186 -0.0125 70  LEU A CD2 
570  N N   . LYS A 69  ? 0.3445 0.3820 0.3655 -0.0003 -0.0281 -0.0055 71  LYS A N   
571  C CA  . LYS A 69  ? 0.3754 0.4138 0.3914 0.0003  -0.0311 -0.0025 71  LYS A CA  
572  C C   . LYS A 69  ? 0.3323 0.3626 0.3447 0.0031  -0.0322 0.0018  71  LYS A C   
573  O O   . LYS A 69  ? 0.3916 0.4153 0.4049 0.0036  -0.0298 0.0016  71  LYS A O   
574  C CB  . LYS A 69  ? 0.4154 0.4553 0.4259 -0.0045 -0.0304 -0.0036 71  LYS A CB  
575  C CG  . LYS A 69  ? 0.4504 0.4991 0.4661 -0.0068 -0.0305 -0.0080 71  LYS A CG  
576  C CD  . LYS A 69  ? 0.5374 0.5894 0.5490 -0.0114 -0.0301 -0.0101 71  LYS A CD  
577  C CE  . LYS A 69  ? 0.5594 0.6206 0.5786 -0.0133 -0.0307 -0.0149 71  LYS A CE  
578  N NZ  . LYS A 69  ? 0.6217 0.6880 0.6384 -0.0177 -0.0306 -0.0183 71  LYS A NZ  
579  N N   . PRO A 70  ? 0.5126 0.5432 0.5218 0.0052  -0.0360 0.0056  72  PRO A N   
580  C CA  . PRO A 70  ? 0.6184 0.6401 0.6247 0.0079  -0.0377 0.0106  72  PRO A CA  
581  C C   . PRO A 70  ? 0.6796 0.6923 0.6790 0.0042  -0.0345 0.0123  72  PRO A C   
582  O O   . PRO A 70  ? 0.7278 0.7408 0.7193 -0.0002 -0.0337 0.0134  72  PRO A O   
583  C CB  . PRO A 70  ? 0.6287 0.6534 0.6307 0.0096  -0.0429 0.0147  72  PRO A CB  
584  C CG  . PRO A 70  ? 0.6100 0.6463 0.6178 0.0104  -0.0442 0.0106  72  PRO A CG  
585  C CD  . PRO A 70  ? 0.5161 0.5557 0.5260 0.0061  -0.0396 0.0055  72  PRO A CD  
586  N N   . VAL A 71  ? 0.7401 0.7458 0.7433 0.0057  -0.0322 0.0118  73  VAL A N   
587  C CA  . VAL A 71  ? 0.7780 0.7743 0.7763 0.0027  -0.0290 0.0132  73  VAL A CA  
588  C C   . VAL A 71  ? 0.7721 0.7604 0.7756 0.0069  -0.0297 0.0152  73  VAL A C   
589  O O   . VAL A 71  ? 0.7536 0.7448 0.7653 0.0117  -0.0320 0.0140  73  VAL A O   
590  C CB  . VAL A 71  ? 0.7720 0.7695 0.7712 -0.0011 -0.0241 0.0075  73  VAL A CB  
591  C CG1 . VAL A 71  ? 0.7557 0.7537 0.7638 0.0017  -0.0223 0.0035  73  VAL A CG1 
592  C CG2 . VAL A 71  ? 0.8200 0.8099 0.8122 -0.0057 -0.0208 0.0085  73  VAL A CG2 
593  N N   . LYS A 72  ? 0.7517 0.7301 0.7513 0.0049  -0.0277 0.0178  74  LYS A N   
594  C CA  . LYS A 72  ? 0.7672 0.7370 0.7722 0.0087  -0.0289 0.0203  74  LYS A CA  
595  C C   . LYS A 72  ? 0.7199 0.6924 0.7364 0.0119  -0.0268 0.0140  74  LYS A C   
596  O O   . LYS A 72  ? 0.6654 0.6418 0.6831 0.0096  -0.0227 0.0085  74  LYS A O   
597  C CB  . LYS A 72  ? 0.8268 0.7854 0.8258 0.0050  -0.0264 0.0240  74  LYS A CB  
598  C CG  . LYS A 72  ? 0.8754 0.8246 0.8733 0.0076  -0.0309 0.0320  74  LYS A CG  
599  C CD  . LYS A 72  ? 0.8940 0.8309 0.8926 0.0059  -0.0279 0.0339  74  LYS A CD  
600  C CE  . LYS A 72  ? 0.8500 0.7867 0.8614 0.0090  -0.0250 0.0268  74  LYS A CE  
601  N NZ  . LYS A 72  ? 0.8069 0.7483 0.8296 0.0158  -0.0292 0.0249  74  LYS A NZ  
602  N N   . LYS A 73  ? 0.7275 0.6982 0.7526 0.0172  -0.0299 0.0146  75  LYS A N   
603  C CA  . LYS A 73  ? 0.7030 0.6787 0.7396 0.0205  -0.0284 0.0080  75  LYS A CA  
604  C C   . LYS A 73  ? 0.6125 0.5848 0.6516 0.0183  -0.0230 0.0035  75  LYS A C   
605  O O   . LYS A 73  ? 0.5296 0.5090 0.5745 0.0188  -0.0204 -0.0028 75  LYS A O   
606  C CB  . LYS A 73  ? 0.7285 0.7019 0.7747 0.0263  -0.0330 0.0092  75  LYS A CB  
607  C CG  . LYS A 73  ? 0.7400 0.7180 0.7996 0.0297  -0.0314 0.0019  75  LYS A CG  
608  C CD  . LYS A 73  ? 0.7804 0.7586 0.8504 0.0357  -0.0368 0.0022  75  LYS A CD  
609  C CE  . LYS A 73  ? 0.8078 0.7832 0.8912 0.0387  -0.0357 -0.0028 75  LYS A CE  
610  N NZ  . LYS A 73  ? 0.8334 0.7954 0.9150 0.0373  -0.0343 0.0010  75  LYS A NZ  
611  N N   . LYS A 74  ? 0.4960 0.4581 0.5304 0.0157  -0.0212 0.0065  76  LYS A N   
612  C CA  . LYS A 74  ? 0.4866 0.4458 0.5242 0.0138  -0.0160 0.0015  76  LYS A CA  
613  C C   . LYS A 74  ? 0.3812 0.3466 0.4136 0.0096  -0.0123 -0.0027 76  LYS A C   
614  O O   . LYS A 74  ? 0.3746 0.3434 0.4119 0.0094  -0.0089 -0.0089 76  LYS A O   
615  C CB  . LYS A 74  ? 0.6249 0.5712 0.6597 0.0118  -0.0148 0.0058  76  LYS A CB  
616  C CG  . LYS A 74  ? 0.7019 0.6447 0.7254 0.0055  -0.0114 0.0073  76  LYS A CG  
617  C CD  . LYS A 74  ? 0.7348 0.6650 0.7569 0.0031  -0.0093 0.0106  76  LYS A CD  
618  C CE  . LYS A 74  ? 0.7854 0.7138 0.7974 -0.0038 -0.0050 0.0102  76  LYS A CE  
619  N NZ  . LYS A 74  ? 0.8085 0.7247 0.8189 -0.0070 -0.0022 0.0132  76  LYS A NZ  
620  N N   . LYS A 75  ? 0.3279 0.2958 0.3513 0.0064  -0.0132 0.0001  77  LYS A N   
621  C CA  . LYS A 75  ? 0.3829 0.3566 0.4028 0.0026  -0.0104 -0.0042 77  LYS A CA  
622  C C   . LYS A 75  ? 0.3615 0.3455 0.3868 0.0047  -0.0111 -0.0081 77  LYS A C   
623  O O   . LYS A 75  ? 0.3341 0.3221 0.3607 0.0031  -0.0086 -0.0129 77  LYS A O   
624  C CB  . LYS A 75  ? 0.4987 0.4728 0.5090 -0.0015 -0.0113 -0.0009 77  LYS A CB  
625  C CG  . LYS A 75  ? 0.6185 0.5993 0.6269 -0.0049 -0.0095 -0.0054 77  LYS A CG  
626  C CD  . LYS A 75  ? 0.6698 0.6511 0.6697 -0.0095 -0.0098 -0.0034 77  LYS A CD  
627  C CE  . LYS A 75  ? 0.6628 0.6516 0.6634 -0.0123 -0.0090 -0.0084 77  LYS A CE  
628  N NZ  . LYS A 75  ? 0.6265 0.6191 0.6344 -0.0100 -0.0083 -0.0127 77  LYS A NZ  
629  N N   . ILE A 76  ? 0.3104 0.2989 0.3390 0.0081  -0.0147 -0.0062 78  ILE A N   
630  C CA  . ILE A 76  ? 0.2993 0.2976 0.3337 0.0099  -0.0150 -0.0099 78  ILE A CA  
631  C C   . ILE A 76  ? 0.3205 0.3200 0.3625 0.0117  -0.0125 -0.0149 78  ILE A C   
632  O O   . ILE A 76  ? 0.2489 0.2551 0.2928 0.0106  -0.0105 -0.0190 78  ILE A O   
633  C CB  . ILE A 76  ? 0.3261 0.3288 0.3633 0.0132  -0.0193 -0.0075 78  ILE A CB  
634  C CG1 . ILE A 76  ? 0.4088 0.4117 0.4384 0.0113  -0.0218 -0.0032 78  ILE A CG1 
635  C CG2 . ILE A 76  ? 0.3873 0.4004 0.4307 0.0144  -0.0190 -0.0116 78  ILE A CG2 
636  C CD1 . ILE A 76  ? 0.4451 0.4519 0.4772 0.0148  -0.0264 -0.0007 78  ILE A CD1 
637  N N   . LYS A 77  ? 0.2518 0.2453 0.2988 0.0144  -0.0127 -0.0146 79  LYS A N   
638  C CA  . LYS A 77  ? 0.2695 0.2650 0.3249 0.0162  -0.0102 -0.0203 79  LYS A CA  
639  C C   . LYS A 77  ? 0.2055 0.1994 0.2585 0.0130  -0.0060 -0.0239 79  LYS A C   
640  O O   . LYS A 77  ? 0.2168 0.2169 0.2746 0.0133  -0.0036 -0.0295 79  LYS A O   
641  C CB  . LYS A 77  ? 0.2831 0.2716 0.3458 0.0198  -0.0116 -0.0195 79  LYS A CB  
642  C CG  . LYS A 77  ? 0.2915 0.2837 0.3606 0.0241  -0.0159 -0.0184 79  LYS A CG  
643  C CD  . LYS A 77  ? 0.3197 0.3070 0.4000 0.0281  -0.0170 -0.0202 79  LYS A CD  
644  C CE  . LYS A 77  ? 0.5072 0.4995 0.5957 0.0327  -0.0216 -0.0206 79  LYS A CE  
645  N NZ  . LYS A 77  ? 0.5940 0.5829 0.6963 0.0369  -0.0228 -0.0239 79  LYS A NZ  
646  N N   . ARG A 78  ? 0.2581 0.2444 0.3038 0.0098  -0.0049 -0.0211 80  ARG A N   
647  C CA  . ARG A 78  ? 0.2629 0.2477 0.3067 0.0067  -0.0011 -0.0251 80  ARG A CA  
648  C C   . ARG A 78  ? 0.1982 0.1918 0.2401 0.0050  -0.0007 -0.0281 80  ARG A C   
649  O O   . ARG A 78  ? 0.1861 0.1838 0.2311 0.0048  0.0016  -0.0333 80  ARG A O   
650  C CB  . ARG A 78  ? 0.2209 0.1968 0.2570 0.0031  -0.0001 -0.0218 80  ARG A CB  
651  C CG  . ARG A 78  ? 0.2269 0.2011 0.2618 -0.0002 0.0039  -0.0266 80  ARG A CG  
652  C CD  . ARG A 78  ? 0.2503 0.2165 0.2779 -0.0044 0.0053  -0.0237 80  ARG A CD  
653  N NE  . ARG A 78  ? 0.2612 0.2311 0.2817 -0.0070 0.0034  -0.0214 80  ARG A NE  
654  C CZ  . ARG A 78  ? 0.2841 0.2499 0.2972 -0.0111 0.0039  -0.0187 80  ARG A CZ  
655  N NH1 . ARG A 78  ? 0.3401 0.2971 0.3508 -0.0133 0.0063  -0.0170 80  ARG A NH1 
656  N NH2 . ARG A 78  ? 0.3212 0.2921 0.3295 -0.0133 0.0022  -0.0179 80  ARG A NH2 
657  N N   . GLU A 79  ? 0.1849 0.1820 0.2221 0.0038  -0.0031 -0.0249 81  GLU A N   
658  C CA  . GLU A 79  ? 0.1957 0.2003 0.2318 0.0021  -0.0032 -0.0270 81  GLU A CA  
659  C C   . GLU A 79  ? 0.1814 0.1945 0.2231 0.0042  -0.0032 -0.0297 81  GLU A C   
660  O O   . GLU A 79  ? 0.1918 0.2097 0.2340 0.0030  -0.0019 -0.0329 81  GLU A O   
661  C CB  . GLU A 79  ? 0.2161 0.2227 0.2479 0.0004  -0.0059 -0.0233 81  GLU A CB  
662  C CG  . GLU A 79  ? 0.2046 0.2177 0.2362 -0.0016 -0.0064 -0.0249 81  GLU A CG  
663  C CD  . GLU A 79  ? 0.2147 0.2300 0.2437 -0.0034 -0.0089 -0.0223 81  GLU A CD  
664  O OE1 . GLU A 79  ? 0.2239 0.2369 0.2503 -0.0032 -0.0102 -0.0193 81  GLU A OE1 
665  O OE2 . GLU A 79  ? 0.2322 0.2519 0.2621 -0.0051 -0.0097 -0.0232 81  GLU A OE2 
666  N N   . ILE A 80  ? 0.1922 0.2079 0.2382 0.0072  -0.0047 -0.0286 82  ILE A N   
667  C CA  . ILE A 80  ? 0.2029 0.2279 0.2547 0.0088  -0.0043 -0.0319 82  ILE A CA  
668  C C   . ILE A 80  ? 0.1777 0.2040 0.2339 0.0093  -0.0012 -0.0374 82  ILE A C   
669  O O   . ILE A 80  ? 0.1906 0.2248 0.2474 0.0082  0.0001  -0.0407 82  ILE A O   
670  C CB  . ILE A 80  ? 0.1893 0.2165 0.2465 0.0121  -0.0065 -0.0308 82  ILE A CB  
671  C CG1 . ILE A 80  ? 0.2165 0.2454 0.2700 0.0115  -0.0095 -0.0263 82  ILE A CG1 
672  C CG2 . ILE A 80  ? 0.2596 0.2965 0.3244 0.0136  -0.0052 -0.0360 82  ILE A CG2 
673  C CD1 . ILE A 80  ? 0.2356 0.2660 0.2942 0.0151  -0.0123 -0.0252 82  ILE A CD1 
674  N N   . LYS A 81  ? 0.1891 0.2078 0.2484 0.0108  -0.0001 -0.0385 83  LYS A N   
675  C CA  . LYS A 81  ? 0.2169 0.2372 0.2819 0.0115  0.0030  -0.0447 83  LYS A CA  
676  C C   . LYS A 81  ? 0.1713 0.1928 0.2318 0.0085  0.0050  -0.0473 83  LYS A C   
677  O O   . LYS A 81  ? 0.1879 0.2170 0.2513 0.0085  0.0068  -0.0525 83  LYS A O   
678  C CB  . LYS A 81  ? 0.2572 0.2676 0.3269 0.0133  0.0037  -0.0449 83  LYS A CB  
679  C CG  . LYS A 81  ? 0.2204 0.2331 0.2986 0.0144  0.0069  -0.0522 83  LYS A CG  
680  C CD  . LYS A 81  ? 0.2517 0.2750 0.3395 0.0172  0.0067  -0.0571 83  LYS A CD  
681  C CE  . LYS A 81  ? 0.2589 0.2879 0.3542 0.0175  0.0102  -0.0657 83  LYS A CE  
682  N NZ  . LYS A 81  ? 0.3155 0.3563 0.4208 0.0197  0.0104  -0.0718 83  LYS A NZ  
683  N N   . ILE A 82  ? 0.1858 0.2007 0.2393 0.0061  0.0046  -0.0441 84  ILE A N   
684  C CA  . ILE A 82  ? 0.1853 0.2012 0.2354 0.0035  0.0058  -0.0469 84  ILE A CA  
685  C C   . ILE A 82  ? 0.1905 0.2162 0.2389 0.0026  0.0044  -0.0470 84  ILE A C   
686  O O   . ILE A 82  ? 0.1801 0.2110 0.2291 0.0020  0.0054  -0.0510 84  ILE A O   
687  C CB  . ILE A 82  ? 0.1802 0.1879 0.2244 0.0008  0.0055  -0.0441 84  ILE A CB  
688  C CG1 . ILE A 82  ? 0.2303 0.2287 0.2761 0.0009  0.0079  -0.0450 84  ILE A CG1 
689  C CG2 . ILE A 82  ? 0.2055 0.2155 0.2467 -0.0017 0.0054  -0.0466 84  ILE A CG2 
690  C CD1 . ILE A 82  ? 0.2015 0.1922 0.2413 -0.0023 0.0083  -0.0425 84  ILE A CD1 
691  N N   . LEU A 83  ? 0.1787 0.2072 0.2250 0.0023  0.0018  -0.0425 85  LEU A N   
692  C CA  . LEU A 83  ? 0.1519 0.1889 0.1966 0.0009  0.0005  -0.0417 85  LEU A CA  
693  C C   . LEU A 83  ? 0.1589 0.2056 0.2077 0.0020  0.0020  -0.0455 85  LEU A C   
694  O O   . LEU A 83  ? 0.1840 0.2374 0.2309 0.0004  0.0020  -0.0467 85  LEU A O   
695  C CB  . LEU A 83  ? 0.1721 0.2103 0.2151 0.0004  -0.0021 -0.0366 85  LEU A CB  
696  C CG  . LEU A 83  ? 0.1750 0.2071 0.2139 -0.0015 -0.0040 -0.0333 85  LEU A CG  
697  C CD1 . LEU A 83  ? 0.1774 0.2107 0.2162 -0.0012 -0.0061 -0.0292 85  LEU A CD1 
698  C CD2 . LEU A 83  ? 0.1917 0.2258 0.2285 -0.0040 -0.0051 -0.0335 85  LEU A CD2 
699  N N   . GLU A 84  ? 0.1979 0.2457 0.2525 0.0046  0.0031  -0.0476 86  GLU A N   
700  C CA  . GLU A 84  ? 0.2294 0.2876 0.2892 0.0054  0.0049  -0.0528 86  GLU A CA  
701  C C   . GLU A 84  ? 0.2235 0.2828 0.2849 0.0053  0.0074  -0.0586 86  GLU A C   
702  O O   . GLU A 84  ? 0.1970 0.2666 0.2586 0.0042  0.0084  -0.0621 86  GLU A O   
703  C CB  . GLU A 84  ? 0.2153 0.2744 0.2828 0.0084  0.0051  -0.0545 86  GLU A CB  
704  C CG  . GLU A 84  ? 0.2429 0.3050 0.3096 0.0083  0.0027  -0.0502 86  GLU A CG  
705  C CD  . GLU A 84  ? 0.3387 0.4033 0.4141 0.0116  0.0023  -0.0527 86  GLU A CD  
706  O OE1 . GLU A 84  ? 0.3528 0.4167 0.4358 0.0139  0.0038  -0.0577 86  GLU A OE1 
707  O OE2 . GLU A 84  ? 0.3345 0.4020 0.4103 0.0119  0.0004  -0.0500 86  GLU A OE2 
708  N N   . ASN A 85  ? 0.2051 0.2546 0.2675 0.0061  0.0084  -0.0597 87  ASN A N   
709  C CA  . ASN A 85  ? 0.2059 0.2565 0.2707 0.0060  0.0109  -0.0660 87  ASN A CA  
710  C C   . ASN A 85  ? 0.1724 0.2271 0.2309 0.0036  0.0100  -0.0660 87  ASN A C   
711  O O   . ASN A 85  ? 0.1842 0.2465 0.2444 0.0034  0.0114  -0.0714 87  ASN A O   
712  C CB  . ASN A 85  ? 0.1889 0.2275 0.2556 0.0066  0.0124  -0.0667 87  ASN A CB  
713  C CG  . ASN A 85  ? 0.1967 0.2315 0.2717 0.0094  0.0135  -0.0682 87  ASN A CG  
714  O OD1 . ASN A 85  ? 0.2340 0.2766 0.3153 0.0112  0.0135  -0.0707 87  ASN A OD1 
715  N ND2 . ASN A 85  ? 0.2173 0.2403 0.2930 0.0095  0.0143  -0.0667 87  ASN A ND2 
716  N N   . LEU A 86  ? 0.1832 0.2334 0.2353 0.0018  0.0074  -0.0604 88  LEU A N   
717  C CA  . LEU A 86  ? 0.1749 0.2270 0.2222 -0.0002 0.0057  -0.0600 88  LEU A CA  
718  C C   . LEU A 86  ? 0.1731 0.2343 0.2168 -0.0018 0.0034  -0.0567 88  LEU A C   
719  O O   . LEU A 86  ? 0.2005 0.2638 0.2405 -0.0034 0.0014  -0.0559 88  LEU A O   
720  C CB  . LEU A 86  ? 0.1863 0.2285 0.2300 -0.0016 0.0039  -0.0566 88  LEU A CB  
721  C CG  . LEU A 86  ? 0.1876 0.2205 0.2333 -0.0012 0.0062  -0.0594 88  LEU A CG  
722  C CD1 . LEU A 86  ? 0.1987 0.2242 0.2406 -0.0033 0.0045  -0.0564 88  LEU A CD1 
723  C CD2 . LEU A 86  ? 0.1963 0.2312 0.2449 -0.0009 0.0085  -0.0665 88  LEU A CD2 
724  N N   . ARG A 87  ? 0.1626 0.2294 0.2076 -0.0016 0.0037  -0.0547 89  ARG A N   
725  C CA  . ARG A 87  ? 0.1956 0.2705 0.2369 -0.0039 0.0018  -0.0508 89  ARG A CA  
726  C C   . ARG A 87  ? 0.1924 0.2767 0.2313 -0.0052 0.0020  -0.0536 89  ARG A C   
727  O O   . ARG A 87  ? 0.2013 0.2915 0.2437 -0.0041 0.0046  -0.0601 89  ARG A O   
728  C CB  . ARG A 87  ? 0.2116 0.2922 0.2560 -0.0034 0.0029  -0.0503 89  ARG A CB  
729  C CG  . ARG A 87  ? 0.2109 0.2988 0.2515 -0.0063 0.0014  -0.0455 89  ARG A CG  
730  C CD  . ARG A 87  ? 0.2451 0.3349 0.2894 -0.0056 0.0018  -0.0443 89  ARG A CD  
731  N NE  . ARG A 87  ? 0.2582 0.3519 0.3097 -0.0029 0.0044  -0.0504 89  ARG A NE  
732  C CZ  . ARG A 87  ? 0.3020 0.3940 0.3587 -0.0007 0.0043  -0.0507 89  ARG A CZ  
733  N NH1 . ARG A 87  ? 0.2675 0.3547 0.3225 -0.0009 0.0021  -0.0454 89  ARG A NH1 
734  N NH2 . ARG A 87  ? 0.3216 0.4171 0.3863 0.0020  0.0062  -0.0568 89  ARG A NH2 
735  N N   . GLY A 88  ? 0.1964 0.2824 0.2296 -0.0078 -0.0011 -0.0487 90  GLY A N   
736  C CA  . GLY A 88  ? 0.1957 0.2901 0.2251 -0.0094 -0.0020 -0.0498 90  GLY A CA  
737  C C   . GLY A 88  ? 0.2657 0.3553 0.2944 -0.0085 -0.0036 -0.0524 90  GLY A C   
738  O O   . GLY A 88  ? 0.2419 0.3375 0.2667 -0.0098 -0.0057 -0.0521 90  GLY A O   
739  N N   . GLY A 89  ? 0.2061 0.2856 0.2383 -0.0066 -0.0028 -0.0550 91  GLY A N   
740  C CA  . GLY A 89  ? 0.2124 0.2873 0.2449 -0.0059 -0.0041 -0.0585 91  GLY A CA  
741  C C   . GLY A 89  ? 0.2117 0.2827 0.2408 -0.0075 -0.0092 -0.0532 91  GLY A C   
742  O O   . GLY A 89  ? 0.1999 0.2686 0.2272 -0.0090 -0.0114 -0.0467 91  GLY A O   
743  N N   . PRO A 90  ? 0.1878 0.2579 0.2170 -0.0070 -0.0113 -0.0565 92  PRO A N   
744  C CA  . PRO A 90  ? 0.1533 0.2201 0.1806 -0.0082 -0.0169 -0.0522 92  PRO A CA  
745  C C   . PRO A 90  ? 0.1675 0.2245 0.1973 -0.0088 -0.0182 -0.0492 92  PRO A C   
746  O O   . PRO A 90  ? 0.1823 0.2328 0.2154 -0.0079 -0.0161 -0.0536 92  PRO A O   
747  C CB  . PRO A 90  ? 0.2082 0.2753 0.2374 -0.0068 -0.0182 -0.0587 92  PRO A CB  
748  C CG  . PRO A 90  ? 0.3201 0.3936 0.3505 -0.0054 -0.0134 -0.0655 92  PRO A CG  
749  C CD  . PRO A 90  ? 0.2398 0.3117 0.2720 -0.0053 -0.0087 -0.0651 92  PRO A CD  
750  N N   . ASN A 91  ? 0.1544 0.2108 0.1825 -0.0105 -0.0216 -0.0420 93  ASN A N   
751  C CA  . ASN A 91  ? 0.1466 0.1953 0.1777 -0.0114 -0.0237 -0.0392 93  ASN A CA  
752  C C   . ASN A 91  ? 0.1828 0.2276 0.2155 -0.0110 -0.0196 -0.0403 93  ASN A C   
753  O O   . ASN A 91  ? 0.1971 0.2359 0.2325 -0.0115 -0.0204 -0.0403 93  ASN A O   
754  C CB  . ASN A 91  ? 0.1802 0.2236 0.2152 -0.0110 -0.0272 -0.0430 93  ASN A CB  
755  C CG  . ASN A 91  ? 0.2456 0.2919 0.2795 -0.0112 -0.0327 -0.0403 93  ASN A CG  
756  O OD1 . ASN A 91  ? 0.2141 0.2646 0.2442 -0.0127 -0.0347 -0.0336 93  ASN A OD1 
757  N ND2 . ASN A 91  ? 0.2031 0.2474 0.2402 -0.0100 -0.0353 -0.0455 93  ASN A ND2 
758  N N   . ILE A 92  ? 0.1967 0.2454 0.2280 -0.0101 -0.0155 -0.0413 94  ILE A N   
759  C CA  . ILE A 92  ? 0.1588 0.2041 0.1913 -0.0095 -0.0124 -0.0411 94  ILE A CA  
760  C C   . ILE A 92  ? 0.1729 0.2214 0.2044 -0.0106 -0.0135 -0.0350 94  ILE A C   
761  O O   . ILE A 92  ? 0.1590 0.2147 0.1884 -0.0114 -0.0136 -0.0327 94  ILE A O   
762  C CB  . ILE A 92  ? 0.1839 0.2316 0.2174 -0.0076 -0.0079 -0.0456 94  ILE A CB  
763  C CG1 . ILE A 92  ? 0.2189 0.2651 0.2539 -0.0066 -0.0065 -0.0523 94  ILE A CG1 
764  C CG2 . ILE A 92  ? 0.2230 0.2662 0.2579 -0.0067 -0.0057 -0.0446 94  ILE A CG2 
765  C CD1 . ILE A 92  ? 0.1744 0.2117 0.2110 -0.0070 -0.0062 -0.0547 94  ILE A CD1 
766  N N   . ILE A 93  ? 0.1513 0.1950 0.1842 -0.0111 -0.0141 -0.0326 95  ILE A N   
767  C CA  . ILE A 93  ? 0.1251 0.1720 0.1579 -0.0121 -0.0147 -0.0277 95  ILE A CA  
768  C C   . ILE A 93  ? 0.1271 0.1801 0.1595 -0.0108 -0.0115 -0.0285 95  ILE A C   
769  O O   . ILE A 93  ? 0.1601 0.2115 0.1937 -0.0087 -0.0088 -0.0322 95  ILE A O   
770  C CB  . ILE A 93  ? 0.1353 0.1771 0.1702 -0.0123 -0.0155 -0.0264 95  ILE A CB  
771  C CG1 . ILE A 93  ? 0.1232 0.1683 0.1590 -0.0138 -0.0171 -0.0215 95  ILE A CG1 
772  C CG2 . ILE A 93  ? 0.1524 0.1912 0.1872 -0.0104 -0.0125 -0.0287 95  ILE A CG2 
773  C CD1 . ILE A 93  ? 0.1777 0.2232 0.2147 -0.0162 -0.0208 -0.0182 95  ILE A CD1 
774  N N   . THR A 94  ? 0.1501 0.2100 0.1815 -0.0124 -0.0119 -0.0251 96  THR A N   
775  C CA  . THR A 94  ? 0.1472 0.2148 0.1792 -0.0117 -0.0090 -0.0266 96  THR A CA  
776  C C   . THR A 94  ? 0.1561 0.2230 0.1910 -0.0107 -0.0084 -0.0254 96  THR A C   
777  O O   . THR A 94  ? 0.1647 0.2317 0.1998 -0.0124 -0.0102 -0.0214 96  THR A O   
778  C CB  . THR A 94  ? 0.1600 0.2368 0.1893 -0.0146 -0.0094 -0.0241 96  THR A CB  
779  O OG1 . THR A 94  ? 0.2338 0.3121 0.2600 -0.0151 -0.0102 -0.0255 96  THR A OG1 
780  C CG2 . THR A 94  ? 0.2103 0.2964 0.2411 -0.0144 -0.0062 -0.0266 96  THR A CG2 
781  N N   . LEU A 95  ? 0.1594 0.2254 0.1970 -0.0079 -0.0062 -0.0290 97  LEU A N   
782  C CA  . LEU A 95  ? 0.1392 0.2066 0.1800 -0.0064 -0.0059 -0.0285 97  LEU A CA  
783  C C   . LEU A 95  ? 0.1611 0.2396 0.2035 -0.0076 -0.0045 -0.0293 97  LEU A C   
784  O O   . LEU A 95  ? 0.2236 0.3080 0.2676 -0.0069 -0.0022 -0.0336 97  LEU A O   
785  C CB  . LEU A 95  ? 0.1760 0.2384 0.2198 -0.0030 -0.0046 -0.0317 97  LEU A CB  
786  C CG  . LEU A 95  ? 0.1704 0.2331 0.2180 -0.0007 -0.0050 -0.0312 97  LEU A CG  
787  C CD1 . LEU A 95  ? 0.1691 0.2279 0.2148 -0.0016 -0.0076 -0.0267 97  LEU A CD1 
788  C CD2 . LEU A 95  ? 0.1993 0.2562 0.2501 0.0027  -0.0041 -0.0338 97  LEU A CD2 
789  N N   . ALA A 96  ? 0.1374 0.2193 0.1798 -0.0097 -0.0055 -0.0258 98  ALA A N   
790  C CA  . ALA A 96  ? 0.1869 0.2799 0.2304 -0.0117 -0.0039 -0.0266 98  ALA A CA  
791  C C   . ALA A 96  ? 0.2156 0.3130 0.2653 -0.0092 -0.0027 -0.0301 98  ALA A C   
792  O O   . ALA A 96  ? 0.2067 0.3142 0.2590 -0.0099 -0.0004 -0.0339 98  ALA A O   
793  C CB  . ALA A 96  ? 0.2284 0.3233 0.2697 -0.0157 -0.0054 -0.0211 98  ALA A CB  
794  N N   . ASP A 97  ? 0.1663 0.2568 0.2185 -0.0062 -0.0043 -0.0294 99  ASP A N   
795  C CA  . ASP A 97  ? 0.1887 0.2827 0.2471 -0.0035 -0.0043 -0.0321 99  ASP A CA  
796  C C   . ASP A 97  ? 0.1677 0.2518 0.2268 0.0000  -0.0067 -0.0305 99  ASP A C   
797  O O   . ASP A 97  ? 0.1706 0.2467 0.2252 -0.0007 -0.0081 -0.0272 99  ASP A O   
798  C CB  . ASP A 97  ? 0.1970 0.2992 0.2571 -0.0062 -0.0042 -0.0309 99  ASP A CB  
799  C CG  . ASP A 97  ? 0.2279 0.3394 0.2953 -0.0046 -0.0029 -0.0363 99  ASP A CG  
800  O OD1 . ASP A 97  ? 0.2025 0.3130 0.2747 -0.0007 -0.0027 -0.0405 99  ASP A OD1 
801  O OD2 . ASP A 97  ? 0.2661 0.3862 0.3351 -0.0074 -0.0019 -0.0365 99  ASP A OD2 
802  N N   . ILE A 98  ? 0.1660 0.2512 0.2310 0.0035  -0.0074 -0.0330 100 ILE A N   
803  C CA  . ILE A 98  ? 0.1785 0.2557 0.2441 0.0068  -0.0101 -0.0310 100 ILE A CA  
804  C C   . ILE A 98  ? 0.1529 0.2365 0.2246 0.0087  -0.0116 -0.0324 100 ILE A C   
805  O O   . ILE A 98  ? 0.1780 0.2689 0.2564 0.0100  -0.0105 -0.0373 100 ILE A O   
806  C CB  . ILE A 98  ? 0.2193 0.2893 0.2867 0.0102  -0.0101 -0.0326 100 ILE A CB  
807  C CG1 . ILE A 98  ? 0.2559 0.3221 0.3192 0.0084  -0.0078 -0.0333 100 ILE A CG1 
808  C CG2 . ILE A 98  ? 0.2747 0.3357 0.3406 0.0127  -0.0132 -0.0289 100 ILE A CG2 
809  C CD1 . ILE A 98  ? 0.2569 0.3200 0.3250 0.0113  -0.0065 -0.0373 100 ILE A CD1 
810  N N   . VAL A 99  ? 0.1589 0.2407 0.2293 0.0089  -0.0142 -0.0292 101 VAL A N   
811  C CA  . VAL A 99  ? 0.1307 0.2191 0.2072 0.0108  -0.0159 -0.0309 101 VAL A CA  
812  C C   . VAL A 99  ? 0.1779 0.2595 0.2534 0.0140  -0.0199 -0.0280 101 VAL A C   
813  O O   . VAL A 99  ? 0.1960 0.2695 0.2652 0.0134  -0.0208 -0.0242 101 VAL A O   
814  C CB  . VAL A 99  ? 0.1526 0.2495 0.2295 0.0067  -0.0148 -0.0308 101 VAL A CB  
815  C CG1 . VAL A 99  ? 0.1913 0.2952 0.2677 0.0029  -0.0110 -0.0329 101 VAL A CG1 
816  C CG2 . VAL A 99  ? 0.1815 0.2738 0.2532 0.0043  -0.0162 -0.0261 101 VAL A CG2 
817  N N   . LYS A 100 ? 0.1646 0.2507 0.2467 0.0174  -0.0223 -0.0301 102 LYS A N   
818  C CA  . LYS A 100 ? 0.1809 0.2623 0.2621 0.0206  -0.0268 -0.0272 102 LYS A CA  
819  C C   . LYS A 100 ? 0.1603 0.2470 0.2404 0.0185  -0.0278 -0.0261 102 LYS A C   
820  O O   . LYS A 100 ? 0.2017 0.2978 0.2878 0.0178  -0.0272 -0.0295 102 LYS A O   
821  C CB  . LYS A 100 ? 0.2105 0.2939 0.3004 0.0260  -0.0298 -0.0302 102 LYS A CB  
822  C CG  . LYS A 100 ? 0.3030 0.3818 0.3969 0.0286  -0.0292 -0.0323 102 LYS A CG  
823  C CD  . LYS A 100 ? 0.4326 0.5139 0.5372 0.0341  -0.0330 -0.0357 102 LYS A CD  
824  C CE  . LYS A 100 ? 0.5452 0.6316 0.6595 0.0352  -0.0305 -0.0427 102 LYS A CE  
825  N NZ  . LYS A 100 ? 0.6420 0.7352 0.7692 0.0398  -0.0338 -0.0483 102 LYS A NZ  
826  N N   . ASP A 101 ? 0.1682 0.2495 0.2416 0.0170  -0.0290 -0.0220 103 ASP A N   
827  C CA  . ASP A 101 ? 0.1692 0.2560 0.2429 0.0150  -0.0301 -0.0217 103 ASP A CA  
828  C C   . ASP A 101 ? 0.1826 0.2726 0.2601 0.0192  -0.0344 -0.0224 103 ASP A C   
829  O O   . ASP A 101 ? 0.2125 0.2962 0.2868 0.0224  -0.0376 -0.0197 103 ASP A O   
830  C CB  . ASP A 101 ? 0.1587 0.2404 0.2254 0.0118  -0.0300 -0.0185 103 ASP A CB  
831  C CG  . ASP A 101 ? 0.2576 0.3458 0.3266 0.0094  -0.0306 -0.0192 103 ASP A CG  
832  O OD1 . ASP A 101 ? 0.2280 0.3201 0.2995 0.0058  -0.0281 -0.0202 103 ASP A OD1 
833  O OD2 . ASP A 101 ? 0.2495 0.3395 0.3183 0.0111  -0.0338 -0.0188 103 ASP A OD2 
834  N N   . PRO A 102 ? 0.2094 0.2893 0.3114 -0.0097 -0.0457 0.0286  104 PRO A N   
835  C CA  . PRO A 102 ? 0.2460 0.3400 0.3505 -0.0094 -0.0451 0.0350  104 PRO A CA  
836  C C   . PRO A 102 ? 0.2093 0.3001 0.3122 -0.0132 -0.0500 0.0325  104 PRO A C   
837  O O   . PRO A 102 ? 0.2143 0.3159 0.3191 -0.0114 -0.0482 0.0364  104 PRO A O   
838  C CB  . PRO A 102 ? 0.2242 0.3323 0.3324 -0.0146 -0.0486 0.0441  104 PRO A CB  
839  C CG  . PRO A 102 ? 0.2500 0.3477 0.3571 -0.0207 -0.0544 0.0409  104 PRO A CG  
840  C CD  . PRO A 102 ? 0.1656 0.2479 0.2694 -0.0157 -0.0505 0.0321  104 PRO A CD  
841  N N   . VAL A 103 ? 0.1961 0.2732 0.2956 -0.0183 -0.0561 0.0265  105 VAL A N   
842  C CA  . VAL A 103 ? 0.2093 0.2820 0.3062 -0.0219 -0.0611 0.0234  105 VAL A CA  
843  C C   . VAL A 103 ? 0.1830 0.2465 0.2772 -0.0153 -0.0574 0.0163  105 VAL A C   
844  O O   . VAL A 103 ? 0.2108 0.2796 0.3057 -0.0135 -0.0567 0.0165  105 VAL A O   
845  C CB  . VAL A 103 ? 0.2378 0.2989 0.3310 -0.0302 -0.0694 0.0206  105 VAL A CB  
846  C CG1 . VAL A 103 ? 0.2280 0.2827 0.3172 -0.0334 -0.0744 0.0164  105 VAL A CG1 
847  C CG2 . VAL A 103 ? 0.2278 0.2986 0.3239 -0.0375 -0.0736 0.0283  105 VAL A CG2 
848  N N   . SER A 104 ? 0.2124 0.2633 0.3040 -0.0117 -0.0550 0.0104  106 SER A N   
849  C CA  . SER A 104 ? 0.1997 0.2417 0.2885 -0.0059 -0.0518 0.0039  106 SER A CA  
850  C C   . SER A 104 ? 0.2514 0.3010 0.3431 0.0016  -0.0436 0.0058  106 SER A C   
851  O O   . SER A 104 ? 0.3009 0.3472 0.3916 0.0061  -0.0411 0.0022  106 SER A O   
852  C CB  . SER A 104 ? 0.2176 0.2452 0.3023 -0.0050 -0.0518 -0.0024 106 SER A CB  
853  O OG  . SER A 104 ? 0.2104 0.2401 0.2967 -0.0020 -0.0463 -0.0011 106 SER A OG  
854  N N   . ARG A 105 ? 0.2224 0.2815 0.3172 0.0033  -0.0392 0.0114  107 ARG A N   
855  C CA  . ARG A 105 ? 0.2827 0.3465 0.3789 0.0110  -0.0304 0.0132  107 ARG A CA  
856  C C   . ARG A 105 ? 0.2967 0.3470 0.3892 0.0155  -0.0262 0.0060  107 ARG A C   
857  O O   . ARG A 105 ? 0.3449 0.3937 0.4370 0.0215  -0.0203 0.0045  107 ARG A O   
858  C CB  . ARG A 105 ? 0.3143 0.3878 0.4130 0.0141  -0.0283 0.0165  107 ARG A CB  
859  C CG  . ARG A 105 ? 0.3341 0.4217 0.4359 0.0084  -0.0334 0.0233  107 ARG A CG  
860  C CD  . ARG A 105 ? 0.3410 0.4384 0.4451 0.0108  -0.0320 0.0258  107 ARG A CD  
861  N NE  . ARG A 105 ? 0.2739 0.3785 0.3802 0.0195  -0.0227 0.0295  107 ARG A NE  
862  C CZ  . ARG A 105 ? 0.2774 0.3956 0.3862 0.0219  -0.0182 0.0378  107 ARG A CZ  
863  N NH1 . ARG A 105 ? 0.3199 0.4474 0.4300 0.0159  -0.0227 0.0435  107 ARG A NH1 
864  N NH2 . ARG A 105 ? 0.3198 0.4424 0.4296 0.0306  -0.0092 0.0409  107 ARG A NH2 
865  N N   . THR A 106 ? 0.2299 0.2705 0.3196 0.0123  -0.0292 0.0017  108 THR A N   
866  C CA  . THR A 106 ? 0.2614 0.2902 0.3471 0.0152  -0.0259 -0.0049 108 THR A CA  
867  C C   . THR A 106 ? 0.2786 0.3052 0.3634 0.0133  -0.0255 -0.0053 108 THR A C   
868  O O   . THR A 106 ? 0.2018 0.2344 0.2890 0.0091  -0.0291 -0.0011 108 THR A O   
869  C CB  . THR A 106 ? 0.2403 0.2587 0.3226 0.0137  -0.0306 -0.0109 108 THR A CB  
870  O OG1 . THR A 106 ? 0.2359 0.2510 0.3169 0.0078  -0.0377 -0.0112 108 THR A OG1 
871  C CG2 . THR A 106 ? 0.2924 0.3139 0.3759 0.0158  -0.0314 -0.0107 108 THR A CG2 
872  N N   . PRO A 107 ? 0.2414 0.2602 0.3228 0.0157  -0.0214 -0.0102 109 PRO A N   
873  C CA  . PRO A 107 ? 0.1953 0.2131 0.2759 0.0136  -0.0211 -0.0108 109 PRO A CA  
874  C C   . PRO A 107 ? 0.2044 0.2172 0.2839 0.0084  -0.0281 -0.0126 109 PRO A C   
875  O O   . PRO A 107 ? 0.2314 0.2368 0.3082 0.0075  -0.0316 -0.0162 109 PRO A O   
876  C CB  . PRO A 107 ? 0.2341 0.2444 0.3104 0.0172  -0.0150 -0.0162 109 PRO A CB  
877  C CG  . PRO A 107 ? 0.2360 0.2459 0.3122 0.0220  -0.0106 -0.0163 109 PRO A CG  
878  C CD  . PRO A 107 ? 0.2530 0.2650 0.3314 0.0205  -0.0161 -0.0147 109 PRO A CD  
879  N N   . ALA A 108 ? 0.1709 0.1877 0.2522 0.0053  -0.0296 -0.0099 110 ALA A N   
880  C CA  . ALA A 108 ? 0.1769 0.1890 0.2572 0.0007  -0.0351 -0.0110 110 ALA A CA  
881  C C   . ALA A 108 ? 0.1969 0.2085 0.2761 0.0013  -0.0317 -0.0130 110 ALA A C   
882  O O   . ALA A 108 ? 0.2110 0.2306 0.2931 0.0019  -0.0287 -0.0098 110 ALA A O   
883  C CB  . ALA A 108 ? 0.2094 0.2278 0.2936 -0.0043 -0.0408 -0.0051 110 ALA A CB  
884  N N   . LEU A 109 ? 0.1590 0.1621 0.2338 0.0012  -0.0321 -0.0181 111 LEU A N   
885  C CA  . LEU A 109 ? 0.1478 0.1512 0.2211 0.0013  -0.0290 -0.0202 111 LEU A CA  
886  C C   . LEU A 109 ? 0.1811 0.1863 0.2565 -0.0027 -0.0333 -0.0175 111 LEU A C   
887  O O   . LEU A 109 ? 0.1984 0.1976 0.2724 -0.0050 -0.0386 -0.0175 111 LEU A O   
888  C CB  . LEU A 109 ? 0.1709 0.1659 0.2383 0.0030  -0.0271 -0.0262 111 LEU A CB  
889  C CG  . LEU A 109 ? 0.1713 0.1633 0.2364 0.0067  -0.0230 -0.0291 111 LEU A CG  
890  C CD1 . LEU A 109 ? 0.2014 0.1864 0.2607 0.0077  -0.0217 -0.0344 111 LEU A CD1 
891  C CD2 . LEU A 109 ? 0.3163 0.3133 0.3828 0.0090  -0.0168 -0.0281 111 LEU A CD2 
892  N N   . VAL A 110 ? 0.1489 0.1619 0.2273 -0.0033 -0.0311 -0.0152 112 VAL A N   
893  C CA  . VAL A 110 ? 0.1510 0.1673 0.2325 -0.0068 -0.0347 -0.0117 112 VAL A CA  
894  C C   . VAL A 110 ? 0.1516 0.1673 0.2305 -0.0064 -0.0319 -0.0150 112 VAL A C   
895  O O   . VAL A 110 ? 0.1796 0.2001 0.2580 -0.0045 -0.0267 -0.0168 112 VAL A O   
896  C CB  . VAL A 110 ? 0.1585 0.1870 0.2465 -0.0079 -0.0348 -0.0054 112 VAL A CB  
897  C CG1 . VAL A 110 ? 0.2075 0.2395 0.2992 -0.0119 -0.0388 -0.0014 112 VAL A CG1 
898  C CG2 . VAL A 110 ? 0.1975 0.2287 0.2877 -0.0083 -0.0370 -0.0017 112 VAL A CG2 
899  N N   . PHE A 111 ? 0.1428 0.1526 0.2195 -0.0081 -0.0353 -0.0156 113 PHE A N   
900  C CA  . PHE A 111 ? 0.1414 0.1510 0.2150 -0.0077 -0.0330 -0.0181 113 PHE A CA  
901  C C   . PHE A 111 ? 0.1589 0.1737 0.2366 -0.0102 -0.0352 -0.0137 113 PHE A C   
902  O O   . PHE A 111 ? 0.1821 0.1954 0.2629 -0.0128 -0.0400 -0.0095 113 PHE A O   
903  C CB  . PHE A 111 ? 0.1625 0.1614 0.2293 -0.0064 -0.0344 -0.0220 113 PHE A CB  
904  C CG  . PHE A 111 ? 0.1569 0.1509 0.2197 -0.0038 -0.0323 -0.0263 113 PHE A CG  
905  C CD1 . PHE A 111 ? 0.1572 0.1530 0.2167 -0.0022 -0.0272 -0.0300 113 PHE A CD1 
906  C CD2 . PHE A 111 ? 0.2148 0.2024 0.2768 -0.0032 -0.0357 -0.0265 113 PHE A CD2 
907  C CE1 . PHE A 111 ? 0.1965 0.1874 0.2525 0.0001  -0.0253 -0.0336 113 PHE A CE1 
908  C CE2 . PHE A 111 ? 0.2151 0.1990 0.2741 -0.0005 -0.0336 -0.0300 113 PHE A CE2 
909  C CZ  . PHE A 111 ? 0.1832 0.1684 0.2392 0.0013  -0.0284 -0.0334 113 PHE A CZ  
910  N N   . GLU A 112 ? 0.1621 0.1830 0.2397 -0.0098 -0.0317 -0.0145 114 GLU A N   
911  C CA  . GLU A 112 ? 0.1791 0.2037 0.2595 -0.0115 -0.0334 -0.0106 114 GLU A CA  
912  C C   . GLU A 112 ? 0.2184 0.2307 0.2945 -0.0119 -0.0378 -0.0105 114 GLU A C   
913  O O   . GLU A 112 ? 0.2330 0.2358 0.3026 -0.0100 -0.0381 -0.0145 114 GLU A O   
914  C CB  . GLU A 112 ? 0.2415 0.2742 0.3209 -0.0106 -0.0286 -0.0122 114 GLU A CB  
915  C CG  . GLU A 112 ? 0.2458 0.2715 0.3171 -0.0088 -0.0268 -0.0169 114 GLU A CG  
916  C CD  . GLU A 112 ? 0.3574 0.3920 0.4273 -0.0086 -0.0226 -0.0177 114 GLU A CD  
917  O OE1 . GLU A 112 ? 0.5110 0.5527 0.5848 -0.0095 -0.0228 -0.0136 114 GLU A OE1 
918  O OE2 . GLU A 112 ? 0.2415 0.2765 0.3062 -0.0079 -0.0190 -0.0222 114 GLU A OE2 
919  N N   . HIS A 113 ? 0.2353 0.2474 0.3146 -0.0141 -0.0411 -0.0057 115 HIS A N   
920  C CA  . HIS A 113 ? 0.2269 0.2260 0.3015 -0.0145 -0.0451 -0.0053 115 HIS A CA  
921  C C   . HIS A 113 ? 0.2441 0.2431 0.3151 -0.0123 -0.0426 -0.0053 115 HIS A C   
922  O O   . HIS A 113 ? 0.2582 0.2685 0.3339 -0.0126 -0.0399 -0.0024 115 HIS A O   
923  C CB  . HIS A 113 ? 0.2438 0.2411 0.3231 -0.0187 -0.0503 0.0001  115 HIS A CB  
924  C CG  . HIS A 113 ? 0.2903 0.2729 0.3642 -0.0194 -0.0543 0.0007  115 HIS A CG  
925  N ND1 . HIS A 113 ? 0.2967 0.2782 0.3710 -0.0198 -0.0544 0.0044  115 HIS A ND1 
926  C CD2 . HIS A 113 ? 0.3477 0.3157 0.4148 -0.0196 -0.0581 -0.0019 115 HIS A CD2 
927  C CE1 . HIS A 113 ? 0.2983 0.2638 0.3659 -0.0200 -0.0579 0.0039  115 HIS A CE1 
928  N NE2 . HIS A 113 ? 0.3496 0.3068 0.4126 -0.0200 -0.0604 -0.0001 115 HIS A NE2 
929  N N   . VAL A 114 ? 0.2324 0.2198 0.2951 -0.0098 -0.0434 -0.0081 116 VAL A N   
930  C CA  . VAL A 114 ? 0.2532 0.2393 0.3115 -0.0071 -0.0414 -0.0070 116 VAL A CA  
931  C C   . VAL A 114 ? 0.2566 0.2284 0.3111 -0.0074 -0.0459 -0.0047 116 VAL A C   
932  O O   . VAL A 114 ? 0.2805 0.2394 0.3300 -0.0073 -0.0496 -0.0072 116 VAL A O   
933  C CB  . VAL A 114 ? 0.2064 0.1913 0.2570 -0.0032 -0.0383 -0.0115 116 VAL A CB  
934  C CG1 . VAL A 114 ? 0.2518 0.2370 0.2975 -0.0001 -0.0360 -0.0093 116 VAL A CG1 
935  C CG2 . VAL A 114 ? 0.2425 0.2399 0.2959 -0.0037 -0.0339 -0.0142 116 VAL A CG2 
936  N N   . ASN A 115 ? 0.2928 0.2665 0.3493 -0.0076 -0.0452 0.0001  117 ASN A N   
937  C CA  . ASN A 115 ? 0.3444 0.3030 0.3961 -0.0075 -0.0487 0.0025  117 ASN A CA  
938  C C   . ASN A 115 ? 0.2972 0.2478 0.3385 -0.0017 -0.0465 0.0005  117 ASN A C   
939  O O   . ASN A 115 ? 0.3822 0.3365 0.4219 0.0013  -0.0431 0.0036  117 ASN A O   
940  C CB  . ASN A 115 ? 0.4035 0.3676 0.4620 -0.0099 -0.0486 0.0090  117 ASN A CB  
941  C CG  . ASN A 115 ? 0.5364 0.4833 0.5898 -0.0104 -0.0521 0.0116  117 ASN A CG  
942  O OD1 . ASN A 115 ? 0.6877 0.6184 0.7340 -0.0109 -0.0561 0.0086  117 ASN A OD1 
943  N ND2 . ASN A 115 ? 0.5653 0.5152 0.6219 -0.0102 -0.0505 0.0173  117 ASN A ND2 
944  N N   . ASN A 116 ? 0.3444 0.2851 0.3785 0.0003  -0.0483 -0.0044 118 ASN A N   
945  C CA  . ASN A 116 ? 0.4378 0.3742 0.4622 0.0063  -0.0460 -0.0066 118 ASN A CA  
946  C C   . ASN A 116 ? 0.4707 0.3881 0.4855 0.0093  -0.0489 -0.0061 118 ASN A C   
947  O O   . ASN A 116 ? 0.4011 0.3062 0.4156 0.0059  -0.0535 -0.0058 118 ASN A O   
948  C CB  . ASN A 116 ? 0.4289 0.3669 0.4509 0.0075  -0.0459 -0.0120 118 ASN A CB  
949  C CG  . ASN A 116 ? 0.4836 0.4066 0.5007 0.0074  -0.0509 -0.0153 118 ASN A CG  
950  O OD1 . ASN A 116 ? 0.5371 0.4552 0.5581 0.0029  -0.0549 -0.0149 118 ASN A OD1 
951  N ND2 . ASN A 116 ? 0.5307 0.4469 0.5388 0.0124  -0.0509 -0.0183 118 ASN A ND2 
952  N N   . THR A 117 ? 0.5115 0.4264 0.5175 0.0156  -0.0460 -0.0060 119 THR A N   
953  C CA  . THR A 117 ? 0.5627 0.4591 0.5572 0.0202  -0.0480 -0.0062 119 THR A CA  
954  C C   . THR A 117 ? 0.6046 0.4970 0.5911 0.0247  -0.0487 -0.0110 119 THR A C   
955  O O   . THR A 117 ? 0.6002 0.5053 0.5870 0.0269  -0.0453 -0.0120 119 THR A O   
956  C CB  . THR A 117 ? 0.7537 0.6500 0.7436 0.0252  -0.0439 -0.0011 119 THR A CB  
957  O OG1 . THR A 117 ? 0.7017 0.6186 0.6992 0.0245  -0.0388 0.0021  119 THR A OG1 
958  C CG2 . THR A 117 ? 0.8122 0.6945 0.8018 0.0229  -0.0463 0.0024  119 THR A CG2 
959  N N   . ASP A 118 ? 0.6756 0.5502 0.6544 0.0259  -0.0531 -0.0137 120 ASP A N   
960  C CA  . ASP A 118 ? 0.6719 0.5424 0.6439 0.0298  -0.0547 -0.0184 120 ASP A CA  
961  C C   . ASP A 118 ? 0.5011 0.3765 0.4651 0.0377  -0.0505 -0.0171 120 ASP A C   
962  O O   . ASP A 118 ? 0.7156 0.5873 0.6737 0.0422  -0.0480 -0.0132 120 ASP A O   
963  C CB  . ASP A 118 ? 0.8509 0.7008 0.8150 0.0300  -0.0600 -0.0211 120 ASP A CB  
964  C CG  . ASP A 118 ? 0.9787 0.8286 0.9469 0.0258  -0.0642 -0.0257 120 ASP A CG  
965  O OD1 . ASP A 118 ? 1.0616 0.9025 1.0221 0.0293  -0.0668 -0.0293 120 ASP A OD1 
966  O OD2 . ASP A 118 ? 1.0353 0.8951 1.0142 0.0194  -0.0646 -0.0252 120 ASP A OD2 
967  N N   . PHE A 119 ? 0.4999 0.3843 0.4639 0.0395  -0.0497 -0.0200 121 PHE A N   
968  C CA  . PHE A 119 ? 0.6414 0.5339 0.5987 0.0461  -0.0458 -0.0181 121 PHE A CA  
969  C C   . PHE A 119 ? 0.7547 0.6328 0.6986 0.0541  -0.0469 -0.0175 121 PHE A C   
970  O O   . PHE A 119 ? 0.7614 0.6438 0.6986 0.0603  -0.0431 -0.0136 121 PHE A O   
971  C CB  . PHE A 119 ? 0.6649 0.5700 0.6253 0.0454  -0.0449 -0.0211 121 PHE A CB  
972  C CG  . PHE A 119 ? 0.6710 0.5680 0.6249 0.0494  -0.0483 -0.0249 121 PHE A CG  
973  C CD1 . PHE A 119 ? 0.7292 0.6214 0.6879 0.0455  -0.0523 -0.0292 121 PHE A CD1 
974  C CD2 . PHE A 119 ? 0.6438 0.5399 0.5872 0.0573  -0.0474 -0.0236 121 PHE A CD2 
975  C CE1 . PHE A 119 ? 0.6799 0.5663 0.6334 0.0493  -0.0553 -0.0325 121 PHE A CE1 
976  C CE2 . PHE A 119 ? 0.6371 0.5271 0.5750 0.0613  -0.0507 -0.0268 121 PHE A CE2 
977  C CZ  . PHE A 119 ? 0.6302 0.5155 0.5735 0.0572  -0.0546 -0.0314 121 PHE A CZ  
978  N N   . LYS A 120 ? 0.7741 0.6354 0.7134 0.0543  -0.0519 -0.0211 122 LYS A N   
979  C CA  . LYS A 120 ? 0.8435 0.6891 0.7690 0.0622  -0.0530 -0.0209 122 LYS A CA  
980  C C   . LYS A 120 ? 0.9027 0.7387 0.8233 0.0643  -0.0508 -0.0163 122 LYS A C   
981  O O   . LYS A 120 ? 1.0525 0.8793 0.9608 0.0727  -0.0493 -0.0142 122 LYS A O   
982  C CB  . LYS A 120 ? 0.7957 0.6256 0.7177 0.0609  -0.0590 -0.0263 122 LYS A CB  
983  C CG  . LYS A 120 ? 0.7764 0.6146 0.7008 0.0613  -0.0607 -0.0303 122 LYS A CG  
984  C CD  . LYS A 120 ? 0.8141 0.6436 0.7419 0.0559  -0.0662 -0.0351 122 LYS A CD  
985  C CE  . LYS A 120 ? 0.8246 0.6578 0.7641 0.0463  -0.0668 -0.0344 122 LYS A CE  
986  N NZ  . LYS A 120 ? 0.7958 0.6345 0.7436 0.0408  -0.0697 -0.0380 122 LYS A NZ  
987  N N   . GLN A 121 ? 0.7440 0.5824 0.6738 0.0575  -0.0504 -0.0142 123 GLN A N   
988  C CA  . GLN A 121 ? 0.7499 0.5820 0.6768 0.0593  -0.0476 -0.0090 123 GLN A CA  
989  C C   . GLN A 121 ? 0.7160 0.5684 0.6485 0.0604  -0.0414 -0.0035 123 GLN A C   
990  O O   . GLN A 121 ? 0.8182 0.6692 0.7447 0.0661  -0.0373 0.0017  123 GLN A O   
991  C CB  . GLN A 121 ? 0.8482 0.6699 0.7813 0.0511  -0.0511 -0.0092 123 GLN A CB  
992  C CG  . GLN A 121 ? 0.9102 0.7197 0.8427 0.0464  -0.0576 -0.0152 123 GLN A CG  
993  C CD  . GLN A 121 ? 0.9952 0.7911 0.9302 0.0390  -0.0615 -0.0147 123 GLN A CD  
994  O OE1 . GLN A 121 ? 1.0174 0.8211 0.9619 0.0339  -0.0601 -0.0108 123 GLN A OE1 
995  N NE2 . GLN A 121 ? 1.0022 0.7781 0.9285 0.0383  -0.0664 -0.0186 123 GLN A NE2 
996  N N   . LEU A 122 ? 0.5436 0.4151 0.4872 0.0551  -0.0403 -0.0046 124 LEU A N   
997  C CA  . LEU A 122 ? 0.3972 0.2892 0.3464 0.0550  -0.0346 0.0000  124 LEU A CA  
998  C C   . LEU A 122 ? 0.4298 0.3302 0.3699 0.0631  -0.0306 0.0026  124 LEU A C   
999  O O   . LEU A 122 ? 0.4438 0.3551 0.3829 0.0663  -0.0254 0.0083  124 LEU A O   
1000 C CB  . LEU A 122 ? 0.4455 0.3536 0.4072 0.0474  -0.0347 -0.0026 124 LEU A CB  
1001 C CG  . LEU A 122 ? 0.5938 0.5239 0.5627 0.0455  -0.0293 0.0011  124 LEU A CG  
1002 C CD1 . LEU A 122 ? 0.5835 0.5146 0.5585 0.0431  -0.0278 0.0059  124 LEU A CD1 
1003 C CD2 . LEU A 122 ? 0.6347 0.5777 0.6125 0.0392  -0.0296 -0.0030 124 LEU A CD2 
1004 N N   . TYR A 123 ? 0.3276 0.2249 0.2612 0.0665  -0.0328 -0.0011 125 TYR A N   
1005 C CA  . TYR A 123 ? 0.3650 0.2733 0.2907 0.0737  -0.0291 0.0020  125 TYR A CA  
1006 C C   . TYR A 123 ? 0.4171 0.3149 0.3302 0.0832  -0.0267 0.0070  125 TYR A C   
1007 O O   . TYR A 123 ? 0.4458 0.3560 0.3534 0.0891  -0.0221 0.0122  125 TYR A O   
1008 C CB  . TYR A 123 ? 0.4979 0.4075 0.4210 0.0747  -0.0320 -0.0027 125 TYR A CB  
1009 C CG  . TYR A 123 ? 0.5376 0.4617 0.4719 0.0667  -0.0323 -0.0062 125 TYR A CG  
1010 C CD1 . TYR A 123 ? 0.5519 0.4825 0.4977 0.0588  -0.0314 -0.0065 125 TYR A CD1 
1011 C CD2 . TYR A 123 ? 0.5244 0.4555 0.4574 0.0673  -0.0333 -0.0090 125 TYR A CD2 
1012 C CE1 . TYR A 123 ? 0.5946 0.5371 0.5495 0.0522  -0.0313 -0.0098 125 TYR A CE1 
1013 C CE2 . TYR A 123 ? 0.5854 0.5279 0.5277 0.0602  -0.0331 -0.0121 125 TYR A CE2 
1014 C CZ  . TYR A 123 ? 0.6285 0.5761 0.5813 0.0529  -0.0319 -0.0127 125 TYR A CZ  
1015 O OH  . TYR A 123 ? 0.6256 0.5832 0.5865 0.0464  -0.0313 -0.0159 125 TYR A OH  
1016 N N   . GLN A 124 ? 0.3868 0.2624 0.2952 0.0845  -0.0295 0.0060  126 GLN A N   
1017 C CA  . GLN A 124 ? 0.4256 0.2890 0.3219 0.0933  -0.0267 0.0110  126 GLN A CA  
1018 C C   . GLN A 124 ? 0.4173 0.2921 0.3175 0.0938  -0.0207 0.0184  126 GLN A C   
1019 O O   . GLN A 124 ? 0.4333 0.3047 0.3235 0.1026  -0.0164 0.0241  126 GLN A O   
1020 C CB  . GLN A 124 ? 0.5016 0.3371 0.3923 0.0929  -0.0312 0.0077  126 GLN A CB  
1021 C CG  . GLN A 124 ? 0.6441 0.4656 0.5279 0.0943  -0.0369 0.0010  126 GLN A CG  
1022 C CD  . GLN A 124 ? 0.7746 0.5895 0.6423 0.1065  -0.0353 0.0027  126 GLN A CD  
1023 O OE1 . GLN A 124 ? 0.7082 0.5272 0.5693 0.1134  -0.0298 0.0090  126 GLN A OE1 
1024 N NE2 . GLN A 124 ? 0.7982 0.6100 0.6627 0.1059  -0.0390 -0.0029 126 GLN A NE2 
1025 N N   . THR A 125 ? 0.3842 0.2726 0.2985 0.0851  -0.0199 0.0187  127 THR A N   
1026 C CA  . THR A 125 ? 0.3680 0.2658 0.2873 0.0850  -0.0148 0.0255  127 THR A CA  
1027 C C   . THR A 125 ? 0.4323 0.3593 0.3591 0.0829  -0.0099 0.0289  127 THR A C   
1028 O O   . THR A 125 ? 0.4494 0.3872 0.3780 0.0851  -0.0045 0.0357  127 THR A O   
1029 C CB  . THR A 125 ? 0.5402 0.4293 0.4696 0.0768  -0.0177 0.0243  127 THR A CB  
1030 O OG1 . THR A 125 ? 0.5775 0.4788 0.5195 0.0676  -0.0205 0.0198  127 THR A OG1 
1031 C CG2 . THR A 125 ? 0.5793 0.4394 0.5008 0.0775  -0.0229 0.0207  127 THR A CG2 
1032 N N   . LEU A 126 ? 0.4245 0.3643 0.3555 0.0787  -0.0113 0.0246  128 LEU A N   
1033 C CA  . LEU A 126 ? 0.4333 0.3998 0.3714 0.0752  -0.0070 0.0270  128 LEU A CA  
1034 C C   . LEU A 126 ? 0.4134 0.3932 0.3427 0.0832  -0.0011 0.0343  128 LEU A C   
1035 O O   . LEU A 126 ? 0.4050 0.3785 0.3223 0.0910  -0.0013 0.0352  128 LEU A O   
1036 C CB  . LEU A 126 ? 0.4388 0.4133 0.3811 0.0694  -0.0098 0.0206  128 LEU A CB  
1037 C CG  . LEU A 126 ? 0.4730 0.4405 0.4257 0.0608  -0.0146 0.0142  128 LEU A CG  
1038 C CD1 . LEU A 126 ? 0.4966 0.4761 0.4536 0.0556  -0.0153 0.0094  128 LEU A CD1 
1039 C CD2 . LEU A 126 ? 0.4316 0.4037 0.3949 0.0557  -0.0132 0.0167  128 LEU A CD2 
1040 N N   . THR A 127 ? 0.3601 0.3596 0.2954 0.0816  0.0042  0.0398  129 THR A N   
1041 C CA  . THR A 127 ? 0.3027 0.3198 0.2313 0.0881  0.0105  0.0475  129 THR A CA  
1042 C C   . THR A 127 ? 0.3078 0.3460 0.2366 0.0845  0.0112  0.0459  129 THR A C   
1043 O O   . THR A 127 ? 0.2931 0.3327 0.2285 0.0767  0.0076  0.0390  129 THR A O   
1044 C CB  . THR A 127 ? 0.3121 0.3432 0.2477 0.0875  0.0160  0.0544  129 THR A CB  
1045 O OG1 . THR A 127 ? 0.2893 0.3374 0.2381 0.0774  0.0160  0.0515  129 THR A OG1 
1046 C CG2 . THR A 127 ? 0.3293 0.3391 0.2655 0.0899  0.0151  0.0560  129 THR A CG2 
1047 N N   . ASP A 128 ? 0.2882 0.3429 0.2093 0.0904  0.0162  0.0529  130 ASP A N   
1048 C CA  . ASP A 128 ? 0.2698 0.3475 0.1910 0.0861  0.0176  0.0527  130 ASP A CA  
1049 C C   . ASP A 128 ? 0.2773 0.3703 0.2118 0.0749  0.0183  0.0494  130 ASP A C   
1050 O O   . ASP A 128 ? 0.2591 0.3562 0.1972 0.0676  0.0156  0.0432  130 ASP A O   
1051 C CB  . ASP A 128 ? 0.2722 0.3687 0.1844 0.0936  0.0237  0.0626  130 ASP A CB  
1052 C CG  . ASP A 128 ? 0.3483 0.4676 0.2690 0.0851  0.0247  0.0599  130 ASP A CG  
1053 O OD1 . ASP A 128 ? 0.3014 0.4192 0.2205 0.0809  0.0209  0.0546  130 ASP A OD1 
1054 O OD2 . ASP A 128 ? 0.3881 0.5249 0.3182 0.0827  0.0283  0.0631  130 ASP A OD2 
1055 N N   . TYR A 129 ? 0.2524 0.3524 0.1943 0.0736  0.0219  0.0534  131 TYR A N   
1056 C CA  . TYR A 129 ? 0.2218 0.3364 0.1760 0.0638  0.0226  0.0504  131 TYR A CA  
1057 C C   . TYR A 129 ? 0.2276 0.3259 0.1891 0.0570  0.0166  0.0412  131 TYR A C   
1058 O O   . TYR A 129 ? 0.2444 0.3521 0.2115 0.0490  0.0158  0.0361  131 TYR A O   
1059 C CB  . TYR A 129 ? 0.2225 0.3462 0.1835 0.0647  0.0272  0.0568  131 TYR A CB  
1060 C CG  . TYR A 129 ? 0.2116 0.3544 0.1845 0.0554  0.0287  0.0547  131 TYR A CG  
1061 C CD1 . TYR A 129 ? 0.2658 0.4358 0.2387 0.0521  0.0333  0.0575  131 TYR A CD1 
1062 C CD2 . TYR A 129 ? 0.2217 0.3555 0.2054 0.0497  0.0254  0.0498  131 TYR A CD2 
1063 C CE1 . TYR A 129 ? 0.2883 0.4752 0.2711 0.0435  0.0347  0.0550  131 TYR A CE1 
1064 C CE2 . TYR A 129 ? 0.2662 0.4174 0.2602 0.0418  0.0269  0.0478  131 TYR A CE2 
1065 C CZ  . TYR A 129 ? 0.2878 0.4650 0.2811 0.0388  0.0316  0.0501  131 TYR A CZ  
1066 O OH  . TYR A 129 ? 0.3606 0.5547 0.3632 0.0310  0.0331  0.0476  131 TYR A OH  
1067 N N   . ASP A 130 ? 0.2451 0.3191 0.2058 0.0601  0.0125  0.0391  132 ASP A N   
1068 C CA  . ASP A 130 ? 0.2616 0.3206 0.2288 0.0541  0.0068  0.0311  132 ASP A CA  
1069 C C   . ASP A 130 ? 0.2424 0.3013 0.2067 0.0510  0.0039  0.0248  132 ASP A C   
1070 O O   . ASP A 130 ? 0.2459 0.3066 0.2176 0.0437  0.0020  0.0191  132 ASP A O   
1071 C CB  . ASP A 130 ? 0.2974 0.3302 0.2616 0.0583  0.0027  0.0302  132 ASP A CB  
1072 C CG  . ASP A 130 ? 0.3686 0.3976 0.3382 0.0589  0.0042  0.0349  132 ASP A CG  
1073 O OD1 . ASP A 130 ? 0.3211 0.3663 0.3006 0.0543  0.0070  0.0371  132 ASP A OD1 
1074 O OD2 . ASP A 130 ? 0.3477 0.3567 0.3114 0.0641  0.0025  0.0364  132 ASP A OD2 
1075 N N   . ILE A 131 ? 0.2502 0.3062 0.2036 0.0571  0.0036  0.0261  133 ILE A N   
1076 C CA  . ILE A 131 ? 0.2170 0.2719 0.1671 0.0550  0.0007  0.0208  133 ILE A CA  
1077 C C   . ILE A 131 ? 0.2670 0.3431 0.2211 0.0476  0.0034  0.0195  133 ILE A C   
1078 O O   . ILE A 131 ? 0.2344 0.3087 0.1925 0.0414  0.0010  0.0132  133 ILE A O   
1079 C CB  . ILE A 131 ? 0.3084 0.3586 0.2457 0.0638  0.0002  0.0239  133 ILE A CB  
1080 C CG1 . ILE A 131 ? 0.2921 0.3182 0.2246 0.0707  -0.0030 0.0236  133 ILE A CG1 
1081 C CG2 . ILE A 131 ? 0.2450 0.2972 0.1794 0.0617  -0.0025 0.0194  133 ILE A CG2 
1082 C CD1 . ILE A 131 ? 0.3736 0.3945 0.2925 0.0809  -0.0029 0.0273  133 ILE A CD1 
1083 N N   . ARG A 132 ? 0.2148 0.3113 0.1675 0.0479  0.0086  0.0256  134 ARG A N   
1084 C CA  . ARG A 132 ? 0.2050 0.3222 0.1609 0.0400  0.0114  0.0244  134 ARG A CA  
1085 C C   . ARG A 132 ? 0.2053 0.3220 0.1726 0.0319  0.0107  0.0189  134 ARG A C   
1086 O O   . ARG A 132 ? 0.2002 0.3204 0.1700 0.0250  0.0099  0.0133  134 ARG A O   
1087 C CB  . ARG A 132 ? 0.1871 0.3273 0.1398 0.0418  0.0173  0.0326  134 ARG A CB  
1088 C CG  . ARG A 132 ? 0.2108 0.3526 0.1517 0.0510  0.0185  0.0392  134 ARG A CG  
1089 C CD  . ARG A 132 ? 0.2764 0.4387 0.2207 0.0492  0.0223  0.0443  134 ARG A CD  
1090 N NE  . ARG A 132 ? 0.2370 0.3958 0.1785 0.0578  0.0230  0.0498  134 ARG A NE  
1091 C CZ  . ARG A 132 ? 0.2264 0.3966 0.1733 0.0565  0.0234  0.0520  134 ARG A CZ  
1092 N NH1 . ARG A 132 ? 0.2644 0.4476 0.2182 0.0472  0.0224  0.0494  134 ARG A NH1 
1093 N NH2 . ARG A 132 ? 0.2518 0.4195 0.1966 0.0647  0.0247  0.0566  134 ARG A NH2 
1094 N N   . PHE A 133 ? 0.2167 0.3290 0.1907 0.0331  0.0111  0.0209  135 PHE A N   
1095 C CA  . PHE A 133 ? 0.1834 0.2968 0.1685 0.0264  0.0106  0.0170  135 PHE A CA  
1096 C C   . PHE A 133 ? 0.2105 0.3076 0.1982 0.0230  0.0057  0.0091  135 PHE A C   
1097 O O   . PHE A 133 ? 0.2235 0.3257 0.2156 0.0163  0.0059  0.0042  135 PHE A O   
1098 C CB  . PHE A 133 ? 0.2067 0.3160 0.1978 0.0293  0.0112  0.0214  135 PHE A CB  
1099 C CG  . PHE A 133 ? 0.2620 0.3731 0.2648 0.0232  0.0104  0.0184  135 PHE A CG  
1100 C CD1 . PHE A 133 ? 0.3275 0.4596 0.3367 0.0189  0.0146  0.0202  135 PHE A CD1 
1101 C CD2 . PHE A 133 ? 0.2582 0.3509 0.2653 0.0219  0.0055  0.0141  135 PHE A CD2 
1102 C CE1 . PHE A 133 ? 0.2843 0.4185 0.3040 0.0140  0.0138  0.0178  135 PHE A CE1 
1103 C CE2 . PHE A 133 ? 0.3261 0.4216 0.3437 0.0168  0.0047  0.0121  135 PHE A CE2 
1104 C CZ  . PHE A 133 ? 0.2971 0.4131 0.3209 0.0132  0.0089  0.0140  135 PHE A CZ  
1105 N N   . TYR A 134 ? 0.1890 0.2661 0.1732 0.0277  0.0015  0.0080  136 TYR A N   
1106 C CA  . TYR A 134 ? 0.1911 0.2533 0.1783 0.0248  -0.0030 0.0013  136 TYR A CA  
1107 C C   . TYR A 134 ? 0.2015 0.2659 0.1840 0.0227  -0.0035 -0.0030 136 TYR A C   
1108 O O   . TYR A 134 ? 0.1981 0.2586 0.1848 0.0179  -0.0051 -0.0086 136 TYR A O   
1109 C CB  . TYR A 134 ? 0.2301 0.2714 0.2150 0.0299  -0.0074 0.0014  136 TYR A CB  
1110 C CG  . TYR A 134 ? 0.2769 0.3130 0.2685 0.0296  -0.0080 0.0040  136 TYR A CG  
1111 C CD1 . TYR A 134 ? 0.2318 0.2724 0.2339 0.0236  -0.0082 0.0021  136 TYR A CD1 
1112 C CD2 . TYR A 134 ? 0.2757 0.3023 0.2630 0.0355  -0.0083 0.0088  136 TYR A CD2 
1113 C CE1 . TYR A 134 ? 0.2332 0.2704 0.2420 0.0230  -0.0090 0.0051  136 TYR A CE1 
1114 C CE2 . TYR A 134 ? 0.2970 0.3185 0.2906 0.0347  -0.0089 0.0115  136 TYR A CE2 
1115 C CZ  . TYR A 134 ? 0.2703 0.2977 0.2749 0.0282  -0.0094 0.0098  136 TYR A CZ  
1116 O OH  . TYR A 134 ? 0.3073 0.3307 0.3184 0.0272  -0.0103 0.0132  136 TYR A OH  
1117 N N   . MET A 135 ? 0.2019 0.2734 0.1756 0.0260  -0.0020 0.0000  137 MET A N   
1118 C CA  . MET A 135 ? 0.1635 0.2395 0.1333 0.0229  -0.0023 -0.0034 137 MET A CA  
1119 C C   . MET A 135 ? 0.1983 0.2879 0.1729 0.0144  0.0008  -0.0064 137 MET A C   
1120 O O   . MET A 135 ? 0.1897 0.2757 0.1653 0.0098  -0.0003 -0.0119 137 MET A O   
1121 C CB  . MET A 135 ? 0.1926 0.2773 0.1523 0.0277  -0.0008 0.0016  137 MET A CB  
1122 C CG  . MET A 135 ? 0.2182 0.2881 0.1711 0.0359  -0.0044 0.0027  137 MET A CG  
1123 S SD  . MET A 135 ? 0.2837 0.3417 0.2361 0.0342  -0.0090 -0.0042 137 MET A SD  
1124 C CE  . MET A 135 ? 0.4342 0.5117 0.3820 0.0292  -0.0062 -0.0033 137 MET A CE  
1125 N N   . TYR A 136 ? 0.1865 0.2918 0.1637 0.0124  0.0048  -0.0027 138 TYR A N   
1126 C CA  . TYR A 136 ? 0.1644 0.2830 0.1457 0.0044  0.0079  -0.0057 138 TYR A CA  
1127 C C   . TYR A 136 ? 0.1455 0.2535 0.1351 0.0008  0.0061  -0.0114 138 TYR A C   
1128 O O   . TYR A 136 ? 0.1842 0.2936 0.1747 -0.0051 0.0068  -0.0167 138 TYR A O   
1129 C CB  . TYR A 136 ? 0.1743 0.3123 0.1575 0.0037  0.0124  0.0000  138 TYR A CB  
1130 C CG  . TYR A 136 ? 0.1893 0.3451 0.1736 -0.0044 0.0161  -0.0022 138 TYR A CG  
1131 C CD1 . TYR A 136 ? 0.1881 0.3560 0.1646 -0.0079 0.0180  -0.0018 138 TYR A CD1 
1132 C CD2 . TYR A 136 ? 0.2073 0.3684 0.1999 -0.0087 0.0178  -0.0044 138 TYR A CD2 
1133 C CE1 . TYR A 136 ? 0.2123 0.3959 0.1887 -0.0161 0.0213  -0.0041 138 TYR A CE1 
1134 C CE2 . TYR A 136 ? 0.2629 0.4400 0.2556 -0.0161 0.0213  -0.0068 138 TYR A CE2 
1135 C CZ  . TYR A 136 ? 0.2235 0.4114 0.2079 -0.0201 0.0230  -0.0069 138 TYR A CZ  
1136 O OH  . TYR A 136 ? 0.3241 0.5239 0.3084 -0.0279 0.0252  -0.0096 138 TYR A OH  
1137 N N   . GLU A 137 ? 0.1612 0.2581 0.1562 0.0044  0.0037  -0.0103 139 GLU A N   
1138 C CA  . GLU A 137 ? 0.1806 0.2685 0.1834 0.0015  0.0018  -0.0147 139 GLU A CA  
1139 C C   . GLU A 137 ? 0.1876 0.2617 0.1882 0.0008  -0.0012 -0.0203 139 GLU A C   
1140 O O   . GLU A 137 ? 0.1581 0.2304 0.1627 -0.0034 -0.0008 -0.0249 139 GLU A O   
1141 C CB  . GLU A 137 ? 0.1886 0.2681 0.1970 0.0051  -0.0006 -0.0114 139 GLU A CB  
1142 C CG  . GLU A 137 ? 0.1836 0.2771 0.1962 0.0053  0.0027  -0.0058 139 GLU A CG  
1143 C CD  . GLU A 137 ? 0.2013 0.3104 0.2201 -0.0006 0.0061  -0.0075 139 GLU A CD  
1144 O OE1 . GLU A 137 ? 0.2628 0.3667 0.2868 -0.0037 0.0047  -0.0118 139 GLU A OE1 
1145 O OE2 . GLU A 137 ? 0.2937 0.4206 0.3117 -0.0019 0.0102  -0.0045 139 GLU A OE2 
1146 N N   . ILE A 138 ? 0.1749 0.2396 0.1693 0.0054  -0.0039 -0.0197 140 ILE A N   
1147 C CA  . ILE A 138 ? 0.1652 0.2187 0.1577 0.0050  -0.0065 -0.0245 140 ILE A CA  
1148 C C   . ILE A 138 ? 0.2072 0.2691 0.1967 -0.0004 -0.0036 -0.0278 140 ILE A C   
1149 O O   . ILE A 138 ? 0.1714 0.2271 0.1629 -0.0034 -0.0039 -0.0327 140 ILE A O   
1150 C CB  . ILE A 138 ? 0.2033 0.2472 0.1892 0.0113  -0.0098 -0.0229 140 ILE A CB  
1151 C CG1 . ILE A 138 ? 0.2040 0.2365 0.1917 0.0162  -0.0129 -0.0205 140 ILE A CG1 
1152 C CG2 . ILE A 138 ? 0.2021 0.2366 0.1868 0.0109  -0.0121 -0.0276 140 ILE A CG2 
1153 C CD1 . ILE A 138 ? 0.2067 0.2303 0.1865 0.0230  -0.0157 -0.0186 140 ILE A CD1 
1154 N N   . LEU A 139 ? 0.1661 0.2424 0.1505 -0.0018 -0.0007 -0.0249 141 LEU A N   
1155 C CA  . LEU A 139 ? 0.1781 0.2627 0.1585 -0.0079 0.0018  -0.0279 141 LEU A CA  
1156 C C   . LEU A 139 ? 0.1596 0.2471 0.1452 -0.0142 0.0045  -0.0323 141 LEU A C   
1157 O O   . LEU A 139 ? 0.2029 0.2880 0.1863 -0.0189 0.0056  -0.0370 141 LEU A O   
1158 C CB  . LEU A 139 ? 0.1681 0.2701 0.1423 -0.0087 0.0045  -0.0230 141 LEU A CB  
1159 C CG  . LEU A 139 ? 0.1843 0.2848 0.1509 -0.0032 0.0023  -0.0193 141 LEU A CG  
1160 C CD1 . LEU A 139 ? 0.2380 0.3571 0.1991 -0.0025 0.0053  -0.0127 141 LEU A CD1 
1161 C CD2 . LEU A 139 ? 0.1696 0.2648 0.1321 -0.0059 0.0009  -0.0231 141 LEU A CD2 
1162 N N   . LYS A 140 ? 0.1578 0.2504 0.1498 -0.0141 0.0057  -0.0306 142 LYS A N   
1163 C CA  . LYS A 140 ? 0.1611 0.2562 0.1581 -0.0191 0.0081  -0.0345 142 LYS A CA  
1164 C C   . LYS A 140 ? 0.1642 0.2432 0.1640 -0.0187 0.0061  -0.0394 142 LYS A C   
1165 O O   . LYS A 140 ? 0.1926 0.2702 0.1917 -0.0231 0.0083  -0.0442 142 LYS A O   
1166 C CB  . LYS A 140 ? 0.1897 0.2925 0.1942 -0.0180 0.0090  -0.0311 142 LYS A CB  
1167 C CG  . LYS A 140 ? 0.2500 0.3719 0.2531 -0.0191 0.0123  -0.0264 142 LYS A CG  
1168 C CD  . LYS A 140 ? 0.3054 0.4335 0.3173 -0.0178 0.0129  -0.0231 142 LYS A CD  
1169 C CE  . LYS A 140 ? 0.3013 0.4488 0.3130 -0.0177 0.0163  -0.0174 142 LYS A CE  
1170 N NZ  . LYS A 140 ? 0.3897 0.5425 0.4108 -0.0158 0.0167  -0.0135 142 LYS A NZ  
1171 N N   . ALA A 141 ? 0.1678 0.2344 0.1701 -0.0135 0.0021  -0.0381 143 ALA A N   
1172 C CA  . ALA A 141 ? 0.1763 0.2289 0.1814 -0.0127 0.0002  -0.0418 143 ALA A CA  
1173 C C   . ALA A 141 ? 0.1685 0.2155 0.1676 -0.0141 0.0005  -0.0454 143 ALA A C   
1174 O O   . ALA A 141 ? 0.1705 0.2116 0.1704 -0.0164 0.0020  -0.0497 143 ALA A O   
1175 C CB  . ALA A 141 ? 0.1486 0.1906 0.1570 -0.0073 -0.0043 -0.0392 143 ALA A CB  
1176 N N   . LEU A 142 ? 0.1693 0.2185 0.1622 -0.0126 -0.0006 -0.0434 144 LEU A N   
1177 C CA  . LEU A 142 ? 0.1560 0.2005 0.1436 -0.0139 -0.0007 -0.0462 144 LEU A CA  
1178 C C   . LEU A 142 ? 0.1705 0.2219 0.1540 -0.0210 0.0034  -0.0494 144 LEU A C   
1179 O O   . LEU A 142 ? 0.1756 0.2192 0.1577 -0.0234 0.0044  -0.0536 144 LEU A O   
1180 C CB  . LEU A 142 ? 0.1515 0.1977 0.1333 -0.0100 -0.0032 -0.0425 144 LEU A CB  
1181 C CG  . LEU A 142 ? 0.1586 0.1944 0.1424 -0.0029 -0.0076 -0.0405 144 LEU A CG  
1182 C CD1 . LEU A 142 ? 0.1921 0.2308 0.1690 0.0015  -0.0095 -0.0367 144 LEU A CD1 
1183 C CD2 . LEU A 142 ? 0.1704 0.1934 0.1575 -0.0020 -0.0093 -0.0443 144 LEU A CD2 
1184 N N   . ASP A 143 ? 0.1484 0.2143 0.1299 -0.0247 0.0061  -0.0477 145 ASP A N   
1185 C CA  . ASP A 143 ? 0.2017 0.2734 0.1790 -0.0323 0.0099  -0.0515 145 ASP A CA  
1186 C C   . ASP A 143 ? 0.2047 0.2684 0.1861 -0.0342 0.0120  -0.0565 145 ASP A C   
1187 O O   . ASP A 143 ? 0.2178 0.2761 0.1953 -0.0387 0.0143  -0.0612 145 ASP A O   
1188 C CB  . ASP A 143 ? 0.2231 0.3132 0.1980 -0.0363 0.0126  -0.0488 145 ASP A CB  
1189 C CG  . ASP A 143 ? 0.3157 0.4113 0.2851 -0.0450 0.0164  -0.0533 145 ASP A CG  
1190 O OD1 . ASP A 143 ? 0.2302 0.3211 0.1934 -0.0484 0.0163  -0.0555 145 ASP A OD1 
1191 O OD2 . ASP A 143 ? 0.3249 0.4287 0.2962 -0.0486 0.0194  -0.0548 145 ASP A OD2 
1192 N N   . TYR A 144 ? 0.1826 0.2451 0.1715 -0.0308 0.0113  -0.0552 146 TYR A N   
1193 C CA  . TYR A 144 ? 0.1862 0.2421 0.1790 -0.0317 0.0133  -0.0591 146 TYR A CA  
1194 C C   . TYR A 144 ? 0.1609 0.2011 0.1529 -0.0298 0.0125  -0.0623 146 TYR A C   
1195 O O   . TYR A 144 ? 0.1971 0.2317 0.1860 -0.0330 0.0157  -0.0668 146 TYR A O   
1196 C CB  . TYR A 144 ? 0.1940 0.2522 0.1954 -0.0280 0.0121  -0.0563 146 TYR A CB  
1197 C CG  . TYR A 144 ? 0.2001 0.2545 0.2048 -0.0289 0.0146  -0.0596 146 TYR A CG  
1198 C CD1 . TYR A 144 ? 0.1877 0.2505 0.1902 -0.0337 0.0188  -0.0625 146 TYR A CD1 
1199 C CD2 . TYR A 144 ? 0.1947 0.2380 0.2041 -0.0248 0.0130  -0.0598 146 TYR A CD2 
1200 C CE1 . TYR A 144 ? 0.2078 0.2672 0.2123 -0.0337 0.0214  -0.0655 146 TYR A CE1 
1201 C CE2 . TYR A 144 ? 0.1955 0.2363 0.2074 -0.0249 0.0156  -0.0622 146 TYR A CE2 
1202 C CZ  . TYR A 144 ? 0.2168 0.2653 0.2260 -0.0290 0.0198  -0.0650 146 TYR A CZ  
1203 O OH  . TYR A 144 ? 0.2618 0.3076 0.2726 -0.0283 0.0227  -0.0672 146 TYR A OH  
1204 N N   . CYS A 145 ? 0.1668 0.1994 0.1615 -0.0244 0.0085  -0.0598 147 CYS A N   
1205 C CA  . CYS A 145 ? 0.1806 0.1998 0.1757 -0.0223 0.0081  -0.0624 147 CYS A CA  
1206 C C   . CYS A 145 ? 0.1865 0.2023 0.1742 -0.0258 0.0097  -0.0653 147 CYS A C   
1207 O O   . CYS A 145 ? 0.2024 0.2092 0.1888 -0.0269 0.0123  -0.0689 147 CYS A O   
1208 C CB  . CYS A 145 ? 0.1791 0.1917 0.1788 -0.0161 0.0034  -0.0593 147 CYS A CB  
1209 S SG  . CYS A 145 ? 0.2093 0.2224 0.2049 -0.0129 -0.0008 -0.0562 147 CYS A SG  
1210 N N   . HIS A 146 ? 0.1797 0.2032 0.1622 -0.0277 0.0087  -0.0634 148 HIS A N   
1211 C CA  . HIS A 146 ? 0.1885 0.2105 0.1638 -0.0322 0.0102  -0.0657 148 HIS A CA  
1212 C C   . HIS A 146 ? 0.1912 0.2133 0.1623 -0.0392 0.0151  -0.0704 148 HIS A C   
1213 O O   . HIS A 146 ? 0.1903 0.2031 0.1576 -0.0419 0.0172  -0.0741 148 HIS A O   
1214 C CB  . HIS A 146 ? 0.1583 0.1913 0.1284 -0.0333 0.0083  -0.0618 148 HIS A CB  
1215 C CG  . HIS A 146 ? 0.1683 0.1995 0.1405 -0.0261 0.0037  -0.0576 148 HIS A CG  
1216 N ND1 . HIS A 146 ? 0.1763 0.2176 0.1448 -0.0245 0.0018  -0.0529 148 HIS A ND1 
1217 C CD2 . HIS A 146 ? 0.1758 0.1965 0.1530 -0.0199 0.0009  -0.0573 148 HIS A CD2 
1218 C CE1 . HIS A 146 ? 0.1659 0.2016 0.1365 -0.0174 -0.0021 -0.0503 148 HIS A CE1 
1219 N NE2 . HIS A 146 ? 0.1676 0.1911 0.1438 -0.0149 -0.0029 -0.0530 148 HIS A NE2 
1220 N N   . SER A 147 ? 0.1819 0.2147 0.1534 -0.0423 0.0171  -0.0704 149 SER A N   
1221 C CA  . SER A 147 ? 0.1718 0.2053 0.1390 -0.0489 0.0218  -0.0753 149 SER A CA  
1222 C C   . SER A 147 ? 0.2041 0.2240 0.1738 -0.0466 0.0242  -0.0792 149 SER A C   
1223 O O   . SER A 147 ? 0.2346 0.2496 0.1989 -0.0513 0.0283  -0.0841 149 SER A O   
1224 C CB  . SER A 147 ? 0.2068 0.2560 0.1754 -0.0514 0.0231  -0.0739 149 SER A CB  
1225 O OG  . SER A 147 ? 0.2289 0.2775 0.2057 -0.0465 0.0229  -0.0729 149 SER A OG  
1226 N N   . MET A 148 ? 0.1755 0.2162 0.2201 -0.0353 0.0336  -0.0883 150 MET A N   
1227 C CA  . MET A 148 ? 0.2137 0.2450 0.2685 -0.0345 0.0366  -0.0904 150 MET A CA  
1228 C C   . MET A 148 ? 0.1813 0.1969 0.2439 -0.0313 0.0373  -0.0873 150 MET A C   
1229 O O   . MET A 148 ? 0.2085 0.2153 0.2795 -0.0291 0.0388  -0.0859 150 MET A O   
1230 C CB  . MET A 148 ? 0.2192 0.2497 0.2706 -0.0312 0.0330  -0.0843 150 MET A CB  
1231 C CG  . MET A 148 ? 0.1989 0.2457 0.2443 -0.0341 0.0331  -0.0866 150 MET A CG  
1232 S SD  . MET A 148 ? 0.2350 0.2907 0.2892 -0.0405 0.0407  -0.0994 150 MET A SD  
1233 C CE  . MET A 148 ? 0.2252 0.2686 0.2869 -0.0366 0.0407  -0.0957 150 MET A CE  
1234 N N   . GLY A 149 ? 0.1915 0.2044 0.2519 -0.0306 0.0363  -0.0854 151 GLY A N   
1235 C CA  . GLY A 149 ? 0.2080 0.2080 0.2766 -0.0277 0.0376  -0.0821 151 GLY A CA  
1236 C C   . GLY A 149 ? 0.1634 0.1540 0.2284 -0.0213 0.0319  -0.0714 151 GLY A C   
1237 O O   . GLY A 149 ? 0.2070 0.1884 0.2803 -0.0185 0.0332  -0.0677 151 GLY A O   
1238 N N   . ILE A 150 ? 0.1703 0.1638 0.2241 -0.0192 0.0261  -0.0661 152 ILE A N   
1239 C CA  . ILE A 150 ? 0.1903 0.1762 0.2409 -0.0140 0.0210  -0.0575 152 ILE A CA  
1240 C C   . ILE A 150 ? 0.1907 0.1774 0.2303 -0.0120 0.0163  -0.0524 152 ILE A C   
1241 O O   . ILE A 150 ? 0.2046 0.1995 0.2369 -0.0138 0.0154  -0.0535 152 ILE A O   
1242 C CB  . ILE A 150 ? 0.1985 0.1854 0.2489 -0.0132 0.0193  -0.0563 152 ILE A CB  
1243 C CG1 . ILE A 150 ? 0.2094 0.1937 0.2724 -0.0144 0.0241  -0.0602 152 ILE A CG1 
1244 C CG2 . ILE A 150 ? 0.1965 0.1780 0.2418 -0.0088 0.0135  -0.0484 152 ILE A CG2 
1245 C CD1 . ILE A 150 ? 0.2849 0.2735 0.3486 -0.0155 0.0245  -0.0622 152 ILE A CD1 
1246 N N   . MET A 151 ? 0.1737 0.1529 0.2125 -0.0083 0.0135  -0.0466 153 MET A N   
1247 C CA  . MET A 151 ? 0.1745 0.1531 0.2031 -0.0059 0.0091  -0.0415 153 MET A CA  
1248 C C   . MET A 151 ? 0.1633 0.1382 0.1892 -0.0029 0.0049  -0.0367 153 MET A C   
1249 O O   . MET A 151 ? 0.1755 0.1462 0.2073 -0.0013 0.0046  -0.0350 153 MET A O   
1250 C CB  . MET A 151 ? 0.2757 0.2502 0.3040 -0.0044 0.0090  -0.0390 153 MET A CB  
1251 C CG  . MET A 151 ? 0.2424 0.2109 0.2802 -0.0027 0.0110  -0.0372 153 MET A CG  
1252 S SD  . MET A 151 ? 0.2609 0.2265 0.2998 -0.0016 0.0125  -0.0350 153 MET A SD  
1253 C CE  . MET A 151 ? 0.3158 0.2760 0.3697 0.0004  0.0163  -0.0324 153 MET A CE  
1254 N N   . HIS A 152 ? 0.1570 0.1342 0.1748 -0.0022 0.0022  -0.0345 154 HIS A N   
1255 C CA  . HIS A 152 ? 0.1529 0.1274 0.1689 -0.0001 -0.0011 -0.0313 154 HIS A CA  
1256 C C   . HIS A 152 ? 0.1507 0.1196 0.1648 0.0027  -0.0041 -0.0275 154 HIS A C   
1257 O O   . HIS A 152 ? 0.1772 0.1437 0.1945 0.0040  -0.0059 -0.0259 154 HIS A O   
1258 C CB  . HIS A 152 ? 0.1655 0.1444 0.1758 -0.0003 -0.0018 -0.0301 154 HIS A CB  
1259 C CG  . HIS A 152 ? 0.1689 0.1450 0.1789 0.0012  -0.0041 -0.0278 154 HIS A CG  
1260 N ND1 . HIS A 152 ? 0.1750 0.1463 0.1818 0.0032  -0.0068 -0.0253 154 HIS A ND1 
1261 C CD2 . HIS A 152 ? 0.1804 0.1584 0.1935 0.0007  -0.0039 -0.0281 154 HIS A CD2 
1262 C CE1 . HIS A 152 ? 0.1756 0.1458 0.1840 0.0035  -0.0079 -0.0247 154 HIS A CE1 
1263 N NE2 . HIS A 152 ? 0.1531 0.1270 0.1654 0.0023  -0.0063 -0.0260 154 HIS A NE2 
1264 N N   . ARG A 153 ? 0.1541 0.1221 0.1630 0.0035  -0.0046 -0.0259 155 ARG A N   
1265 C CA  . ARG A 153 ? 0.1954 0.1598 0.2020 0.0059  -0.0069 -0.0226 155 ARG A CA  
1266 C C   . ARG A 153 ? 0.1813 0.1443 0.1832 0.0072  -0.0102 -0.0209 155 ARG A C   
1267 O O   . ARG A 153 ? 0.2154 0.1771 0.2152 0.0088  -0.0123 -0.0188 155 ARG A O   
1268 C CB  . ARG A 153 ? 0.1824 0.1450 0.1963 0.0071  -0.0064 -0.0210 155 ARG A CB  
1269 C CG  . ARG A 153 ? 0.1609 0.1239 0.1818 0.0056  -0.0020 -0.0233 155 ARG A CG  
1270 C CD  . ARG A 153 ? 0.1856 0.1463 0.2140 0.0076  -0.0008 -0.0199 155 ARG A CD  
1271 N NE  . ARG A 153 ? 0.1845 0.1452 0.2186 0.0090  -0.0020 -0.0173 155 ARG A NE  
1272 C CZ  . ARG A 153 ? 0.2238 0.1843 0.2658 0.0113  -0.0011 -0.0126 155 ARG A CZ  
1273 N NH1 . ARG A 153 ? 0.2098 0.1693 0.2555 0.0126  0.0013  -0.0100 155 ARG A NH1 
1274 N NH2 . ARG A 153 ? 0.1935 0.1556 0.2407 0.0126  -0.0025 -0.0100 155 ARG A NH2 
1275 N N   . ASP A 154 ? 0.1715 0.1357 0.1723 0.0063  -0.0102 -0.0220 156 ASP A N   
1276 C CA  . ASP A 154 ? 0.1534 0.1159 0.1511 0.0071  -0.0123 -0.0214 156 ASP A CA  
1277 C C   . ASP A 154 ? 0.1917 0.1554 0.1877 0.0065  -0.0106 -0.0214 156 ASP A C   
1278 O O   . ASP A 154 ? 0.1848 0.1478 0.1825 0.0063  -0.0108 -0.0217 156 ASP A O   
1279 C CB  . ASP A 154 ? 0.1757 0.1380 0.1776 0.0070  -0.0143 -0.0219 156 ASP A CB  
1280 C CG  . ASP A 154 ? 0.2312 0.1925 0.2301 0.0073  -0.0167 -0.0223 156 ASP A CG  
1281 O OD1 . ASP A 154 ? 0.2537 0.2138 0.2472 0.0079  -0.0169 -0.0220 156 ASP A OD1 
1282 O OD2 . ASP A 154 ? 0.2568 0.2189 0.2590 0.0066  -0.0181 -0.0234 156 ASP A OD2 
1283 N N   . VAL A 155 ? 0.1692 0.1355 0.1626 0.0063  -0.0086 -0.0205 157 VAL A N   
1284 C CA  . VAL A 155 ? 0.1718 0.1411 0.1645 0.0063  -0.0067 -0.0188 157 VAL A CA  
1285 C C   . VAL A 155 ? 0.2032 0.1682 0.1932 0.0077  -0.0068 -0.0173 157 VAL A C   
1286 O O   . VAL A 155 ? 0.1925 0.1549 0.1784 0.0086  -0.0076 -0.0171 157 VAL A O   
1287 C CB  . VAL A 155 ? 0.1851 0.1606 0.1759 0.0055  -0.0047 -0.0179 157 VAL A CB  
1288 C CG1 . VAL A 155 ? 0.2305 0.2105 0.2207 0.0062  -0.0026 -0.0142 157 VAL A CG1 
1289 C CG2 . VAL A 155 ? 0.2042 0.1849 0.1987 0.0033  -0.0036 -0.0209 157 VAL A CG2 
1290 N N   . LYS A 156 ? 0.1815 0.1457 0.1746 0.0079  -0.0057 -0.0167 158 LYS A N   
1291 C CA  . LYS A 156 ? 0.1817 0.1416 0.1746 0.0088  -0.0046 -0.0164 158 LYS A CA  
1292 C C   . LYS A 156 ? 0.1943 0.1549 0.1934 0.0088  -0.0019 -0.0149 158 LYS A C   
1293 O O   . LYS A 156 ? 0.1753 0.1393 0.1779 0.0081  -0.0020 -0.0147 158 LYS A O   
1294 C CB  . LYS A 156 ? 0.1918 0.1473 0.1830 0.0083  -0.0073 -0.0200 158 LYS A CB  
1295 C CG  . LYS A 156 ? 0.2045 0.1602 0.1997 0.0071  -0.0094 -0.0225 158 LYS A CG  
1296 C CD  . LYS A 156 ? 0.2219 0.1763 0.2151 0.0065  -0.0123 -0.0256 158 LYS A CD  
1297 C CE  . LYS A 156 ? 0.2849 0.2409 0.2826 0.0053  -0.0145 -0.0275 158 LYS A CE  
1298 N NZ  . LYS A 156 ? 0.3713 0.3289 0.3671 0.0044  -0.0174 -0.0304 158 LYS A NZ  
1299 N N   . PRO A 157 ? 0.1802 0.1377 0.1817 0.0097  0.0011  -0.0135 159 PRO A N   
1300 C CA  . PRO A 157 ? 0.2119 0.1703 0.2213 0.0101  0.0046  -0.0110 159 PRO A CA  
1301 C C   . PRO A 157 ? 0.1936 0.1504 0.2076 0.0085  0.0033  -0.0143 159 PRO A C   
1302 O O   . PRO A 157 ? 0.2090 0.1694 0.2287 0.0087  0.0052  -0.0115 159 PRO A O   
1303 C CB  . PRO A 157 ? 0.2053 0.1584 0.2174 0.0110  0.0084  -0.0105 159 PRO A CB  
1304 C CG  . PRO A 157 ? 0.2072 0.1602 0.2120 0.0119  0.0075  -0.0099 159 PRO A CG  
1305 C CD  . PRO A 157 ? 0.2093 0.1630 0.2075 0.0106  0.0023  -0.0136 159 PRO A CD  
1306 N N   . HIS A 158 ? 0.2037 0.1566 0.2157 0.0071  0.0001  -0.0197 160 HIS A N   
1307 C CA  . HIS A 158 ? 0.2115 0.1638 0.2281 0.0054  -0.0015 -0.0230 160 HIS A CA  
1308 C C   . HIS A 158 ? 0.2217 0.1786 0.2391 0.0053  -0.0032 -0.0216 160 HIS A C   
1309 O O   . HIS A 158 ? 0.2426 0.1998 0.2653 0.0043  -0.0036 -0.0229 160 HIS A O   
1310 C CB  . HIS A 158 ? 0.2742 0.2247 0.2874 0.0039  -0.0052 -0.0283 160 HIS A CB  
1311 C CG  . HIS A 158 ? 0.5546 0.5021 0.5637 0.0039  -0.0044 -0.0304 160 HIS A CG  
1312 N ND1 . HIS A 158 ? 0.5737 0.5212 0.5771 0.0056  -0.0038 -0.0277 160 HIS A ND1 
1313 C CD2 . HIS A 158 ? 0.5962 0.5415 0.6063 0.0021  -0.0039 -0.0356 160 HIS A CD2 
1314 C CE1 . HIS A 158 ? 0.6590 0.6038 0.6600 0.0051  -0.0029 -0.0306 160 HIS A CE1 
1315 N NE2 . HIS A 158 ? 0.6641 0.6077 0.6689 0.0029  -0.0029 -0.0358 160 HIS A NE2 
1316 N N   . ASN A 159 ? 0.1935 0.1540 0.2063 0.0059  -0.0040 -0.0197 161 ASN A N   
1317 C CA  . ASN A 159 ? 0.1735 0.1384 0.1875 0.0053  -0.0050 -0.0197 161 ASN A CA  
1318 C C   . ASN A 159 ? 0.1461 0.1175 0.1617 0.0057  -0.0019 -0.0160 161 ASN A C   
1319 O O   . ASN A 159 ? 0.1843 0.1608 0.2000 0.0048  -0.0021 -0.0166 161 ASN A O   
1320 C CB  . ASN A 159 ? 0.1735 0.1386 0.1829 0.0051  -0.0075 -0.0213 161 ASN A CB  
1321 C CG  . ASN A 159 ? 0.2226 0.1845 0.2320 0.0047  -0.0107 -0.0239 161 ASN A CG  
1322 O OD1 . ASN A 159 ? 0.2270 0.1878 0.2404 0.0040  -0.0115 -0.0254 161 ASN A OD1 
1323 N ND2 . ASN A 159 ? 0.1981 0.1597 0.2040 0.0052  -0.0125 -0.0240 161 ASN A ND2 
1324 N N   . VAL A 160 ? 0.1722 0.1447 0.1897 0.0069  0.0012  -0.0121 162 VAL A N   
1325 C CA  . VAL A 160 ? 0.1878 0.1690 0.2078 0.0076  0.0043  -0.0071 162 VAL A CA  
1326 C C   . VAL A 160 ? 0.2472 0.2271 0.2755 0.0083  0.0071  -0.0046 162 VAL A C   
1327 O O   . VAL A 160 ? 0.2757 0.2510 0.3078 0.0095  0.0097  -0.0027 162 VAL A O   
1328 C CB  . VAL A 160 ? 0.2285 0.2138 0.2452 0.0089  0.0062  -0.0028 162 VAL A CB  
1329 C CG1 . VAL A 160 ? 0.2300 0.2274 0.2491 0.0095  0.0091  0.0029  162 VAL A CG1 
1330 C CG2 . VAL A 160 ? 0.2385 0.2238 0.2478 0.0079  0.0035  -0.0060 162 VAL A CG2 
1331 N N   . MET A 161 ? 0.2080 0.1914 0.2403 0.0076  0.0071  -0.0049 163 MET A N   
1332 C CA  . MET A 161 ? 0.2186 0.2014 0.2598 0.0082  0.0101  -0.0021 163 MET A CA  
1333 C C   . MET A 161 ? 0.1965 0.1896 0.2411 0.0101  0.0143  0.0059  163 MET A C   
1334 O O   . MET A 161 ? 0.2505 0.2540 0.2919 0.0096  0.0139  0.0073  163 MET A O   
1335 C CB  . MET A 161 ? 0.2117 0.1939 0.2561 0.0067  0.0082  -0.0056 163 MET A CB  
1336 C CG  . MET A 161 ? 0.2717 0.2455 0.3148 0.0052  0.0044  -0.0121 163 MET A CG  
1337 S SD  . MET A 161 ? 0.2966 0.2619 0.3459 0.0049  0.0060  -0.0140 163 MET A SD  
1338 C CE  . MET A 161 ? 0.4170 0.3775 0.4576 0.0046  0.0033  -0.0177 163 MET A CE  
1339 N N   . ILE A 162 ? 0.2048 0.1961 0.2567 0.0121  0.0186  0.0111  164 ILE A N   
1340 C CA  . ILE A 162 ? 0.2034 0.2058 0.2600 0.0144  0.0231  0.0206  164 ILE A CA  
1341 C C   . ILE A 162 ? 0.2525 0.2538 0.3215 0.0158  0.0275  0.0249  164 ILE A C   
1342 O O   . ILE A 162 ? 0.2554 0.2461 0.3315 0.0160  0.0300  0.0234  164 ILE A O   
1343 C CB  . ILE A 162 ? 0.2064 0.2093 0.2621 0.0165  0.0256  0.0254  164 ILE A CB  
1344 C CG1 . ILE A 162 ? 0.2267 0.2330 0.2708 0.0151  0.0215  0.0219  164 ILE A CG1 
1345 C CG2 . ILE A 162 ? 0.2910 0.3060 0.3543 0.0195  0.0309  0.0368  164 ILE A CG2 
1346 C CD1 . ILE A 162 ? 0.2601 0.2661 0.3026 0.0170  0.0234  0.0259  164 ILE A CD1 
1347 N N   . ASP A 163 ? 0.2668 0.2794 0.3387 0.0163  0.0289  0.0299  165 ASP A N   
1348 C CA  . ASP A 163 ? 0.2629 0.2779 0.3477 0.0184  0.0342  0.0369  165 ASP A CA  
1349 C C   . ASP A 163 ? 0.3127 0.3391 0.4021 0.0218  0.0392  0.0487  165 ASP A C   
1350 O O   . ASP A 163 ? 0.3495 0.3924 0.4364 0.0226  0.0396  0.0548  165 ASP A O   
1351 C CB  . ASP A 163 ? 0.2564 0.2785 0.3422 0.0173  0.0331  0.0364  165 ASP A CB  
1352 C CG  . ASP A 163 ? 0.2946 0.3197 0.3943 0.0196  0.0388  0.0443  165 ASP A CG  
1353 O OD1 . ASP A 163 ? 0.3356 0.3598 0.4448 0.0224  0.0443  0.0519  165 ASP A OD1 
1354 O OD2 . ASP A 163 ? 0.3208 0.3490 0.4229 0.0187  0.0383  0.0434  165 ASP A OD2 
1355 N N   . HIS A 164 ? 0.2454 0.2641 0.3423 0.0238  0.0436  0.0520  166 HIS A N   
1356 C CA  . HIS A 164 ? 0.2891 0.3179 0.3904 0.0274  0.0484  0.0636  166 HIS A CA  
1357 C C   . HIS A 164 ? 0.3768 0.4196 0.4892 0.0305  0.0537  0.0759  166 HIS A C   
1358 O O   . HIS A 164 ? 0.4007 0.4593 0.5140 0.0331  0.0562  0.0866  166 HIS A O   
1359 C CB  . HIS A 164 ? 0.2997 0.3155 0.4086 0.0288  0.0528  0.0639  166 HIS A CB  
1360 C CG  . HIS A 164 ? 0.3633 0.3880 0.4745 0.0322  0.0567  0.0743  166 HIS A CG  
1361 N ND1 . HIS A 164 ? 0.3494 0.3883 0.4494 0.0322  0.0531  0.0772  166 HIS A ND1 
1362 C CD2 . HIS A 164 ? 0.3459 0.3675 0.4699 0.0356  0.0642  0.0824  166 HIS A CD2 
1363 C CE1 . HIS A 164 ? 0.3916 0.4368 0.4970 0.0356  0.0577  0.0873  166 HIS A CE1 
1364 N NE2 . HIS A 164 ? 0.4007 0.4352 0.5209 0.0380  0.0647  0.0909  166 HIS A NE2 
1365 N N   . GLU A 165 ? 0.3715 0.4100 0.4925 0.0302  0.0555  0.0750  167 GLU A N   
1366 C CA  . GLU A 165 ? 0.3382 0.3899 0.4707 0.0333  0.0610  0.0874  167 GLU A CA  
1367 C C   . GLU A 165 ? 0.4224 0.4954 0.5454 0.0329  0.0578  0.0912  167 GLU A C   
1368 O O   . GLU A 165 ? 0.4946 0.5857 0.6228 0.0362  0.0618  0.1041  167 GLU A O   
1369 C CB  . GLU A 165 ? 0.4037 0.4458 0.5470 0.0326  0.0632  0.0843  167 GLU A CB  
1370 C CG  . GLU A 165 ? 0.5188 0.5732 0.6763 0.0362  0.0698  0.0977  167 GLU A CG  
1371 C CD  . GLU A 165 ? 0.6804 0.7277 0.8456 0.0348  0.0705  0.0937  167 GLU A CD  
1372 O OE1 . GLU A 165 ? 0.7127 0.7501 0.8693 0.0308  0.0645  0.0808  167 GLU A OE1 
1373 O OE2 . GLU A 165 ? 0.7152 0.7674 0.8960 0.0379  0.0773  0.1041  167 GLU A OE2 
1374 N N   . HIS A 166 ? 0.3811 0.4535 0.4908 0.0289  0.0510  0.0801  168 HIS A N   
1375 C CA  . HIS A 166 ? 0.2967 0.3885 0.3971 0.0275  0.0481  0.0809  168 HIS A CA  
1376 C C   . HIS A 166 ? 0.2995 0.3974 0.3864 0.0254  0.0439  0.0765  168 HIS A C   
1377 O O   . HIS A 166 ? 0.3354 0.4481 0.4135 0.0230  0.0411  0.0740  168 HIS A O   
1378 C CB  . HIS A 166 ? 0.3262 0.4144 0.4232 0.0243  0.0447  0.0718  168 HIS A CB  
1379 C CG  . HIS A 166 ? 0.4672 0.5523 0.5774 0.0261  0.0489  0.0765  168 HIS A CG  
1380 N ND1 . HIS A 166 ? 0.5021 0.5678 0.6184 0.0252  0.0487  0.0699  168 HIS A ND1 
1381 C CD2 . HIS A 166 ? 0.4853 0.5851 0.6043 0.0288  0.0536  0.0876  168 HIS A CD2 
1382 C CE1 . HIS A 166 ? 0.5047 0.5724 0.6335 0.0270  0.0532  0.0761  168 HIS A CE1 
1383 N NE2 . HIS A 166 ? 0.5183 0.6063 0.6491 0.0295  0.0563  0.0873  168 HIS A NE2 
1384 N N   . ARG A 167 ? 0.2821 0.3692 0.3677 0.0261  0.0437  0.0752  169 ARG A N   
1385 C CA  . ARG A 167 ? 0.2514 0.3437 0.3253 0.0244  0.0401  0.0718  169 ARG A CA  
1386 C C   . ARG A 167 ? 0.2450 0.3352 0.3071 0.0197  0.0341  0.0589  169 ARG A C   
1387 O O   . ARG A 167 ? 0.3413 0.4449 0.3946 0.0175  0.0319  0.0568  169 ARG A O   
1388 C CB  . ARG A 167 ? 0.3160 0.4326 0.3900 0.0263  0.0426  0.0833  169 ARG A CB  
1389 C CG  . ARG A 167 ? 0.3495 0.4697 0.4376 0.0316  0.0494  0.0980  169 ARG A CG  
1390 C CD  . ARG A 167 ? 0.5113 0.6213 0.6006 0.0334  0.0508  0.0995  169 ARG A CD  
1391 N NE  . ARG A 167 ? 0.5994 0.7291 0.6854 0.0347  0.0514  0.1083  169 ARG A NE  
1392 C CZ  . ARG A 167 ? 0.6060 0.7317 0.6882 0.0351  0.0507  0.1079  169 ARG A CZ  
1393 N NH1 . ARG A 167 ? 0.6069 0.7098 0.6875 0.0342  0.0495  0.0990  169 ARG A NH1 
1394 N NH2 . ARG A 167 ? 0.6212 0.7670 0.7010 0.0362  0.0513  0.1164  169 ARG A NH2 
1395 N N   . LYS A 168 ? 0.2558 0.3296 0.3186 0.0182  0.0320  0.0504  170 LYS A N   
1396 C CA  . LYS A 168 ? 0.2625 0.3323 0.3173 0.0143  0.0273  0.0391  170 LYS A CA  
1397 C C   . LYS A 168 ? 0.2228 0.2752 0.2726 0.0130  0.0238  0.0306  170 LYS A C   
1398 O O   . LYS A 168 ? 0.2845 0.3233 0.3392 0.0144  0.0247  0.0307  170 LYS A O   
1399 C CB  . LYS A 168 ? 0.3209 0.3875 0.3812 0.0137  0.0277  0.0369  170 LYS A CB  
1400 C CG  . LYS A 168 ? 0.3910 0.4509 0.4453 0.0101  0.0234  0.0255  170 LYS A CG  
1401 C CD  . LYS A 168 ? 0.4920 0.5528 0.5517 0.0095  0.0242  0.0244  170 LYS A CD  
1402 C CE  . LYS A 168 ? 0.4219 0.4682 0.4905 0.0110  0.0251  0.0250  170 LYS A CE  
1403 N NZ  . LYS A 168 ? 0.4947 0.5405 0.5682 0.0101  0.0251  0.0228  170 LYS A NZ  
1404 N N   . LEU A 169 ? 0.1749 0.2283 0.2156 0.0102  0.0202  0.0233  171 LEU A N   
1405 C CA  . LEU A 169 ? 0.1691 0.2085 0.2047 0.0091  0.0169  0.0162  171 LEU A CA  
1406 C C   . LEU A 169 ? 0.1844 0.2199 0.2160 0.0061  0.0136  0.0071  171 LEU A C   
1407 O O   . LEU A 169 ? 0.1999 0.2465 0.2292 0.0040  0.0138  0.0049  171 LEU A O   
1408 C CB  . LEU A 169 ? 0.2308 0.2752 0.2604 0.0093  0.0167  0.0180  171 LEU A CB  
1409 C CG  . LEU A 169 ? 0.2182 0.2500 0.2424 0.0087  0.0137  0.0122  171 LEU A CG  
1410 C CD1 . LEU A 169 ? 0.1753 0.2094 0.1982 0.0106  0.0153  0.0178  171 LEU A CD1 
1411 C CD2 . LEU A 169 ? 0.2281 0.2612 0.2459 0.0055  0.0108  0.0044  171 LEU A CD2 
1412 N N   . ARG A 170 ? 0.1721 0.1930 0.2038 0.0057  0.0111  0.0018  172 ARG A N   
1413 C CA  . ARG A 170 ? 0.1436 0.1602 0.1727 0.0034  0.0083  -0.0058 172 ARG A CA  
1414 C C   . ARG A 170 ? 0.1475 0.1533 0.1724 0.0034  0.0055  -0.0095 172 ARG A C   
1415 O O   . ARG A 170 ? 0.1967 0.1939 0.2229 0.0047  0.0048  -0.0087 172 ARG A O   
1416 C CB  . ARG A 170 ? 0.1598 0.1717 0.1947 0.0031  0.0079  -0.0078 172 ARG A CB  
1417 C CG  . ARG A 170 ? 0.1818 0.2047 0.2210 0.0030  0.0107  -0.0045 172 ARG A CG  
1418 C CD  . ARG A 170 ? 0.2053 0.2388 0.2409 0.0005  0.0112  -0.0082 172 ARG A CD  
1419 N NE  . ARG A 170 ? 0.2249 0.2701 0.2642 0.0002  0.0139  -0.0056 172 ARG A NE  
1420 C CZ  . ARG A 170 ? 0.2287 0.2888 0.2675 0.0008  0.0164  0.0004  172 ARG A CZ  
1421 N NH1 . ARG A 170 ? 0.2485 0.3134 0.2838 0.0018  0.0168  0.0046  172 ARG A NH1 
1422 N NH2 . ARG A 170 ? 0.3144 0.3857 0.3564 0.0006  0.0188  0.0028  172 ARG A NH2 
1423 N N   . LEU A 171 ? 0.1627 0.1698 0.1834 0.0016  0.0042  -0.0140 173 LEU A N   
1424 C CA  . LEU A 171 ? 0.1597 0.1577 0.1773 0.0016  0.0017  -0.0173 173 LEU A CA  
1425 C C   . LEU A 171 ? 0.1722 0.1633 0.1935 0.0011  -0.0002 -0.0209 173 LEU A C   
1426 O O   . LEU A 171 ? 0.1674 0.1617 0.1916 -0.0003 0.0005  -0.0236 173 LEU A O   
1427 C CB  . LEU A 171 ? 0.1684 0.1712 0.1817 0.0000  0.0020  -0.0198 173 LEU A CB  
1428 C CG  . LEU A 171 ? 0.1901 0.1849 0.2006 0.0002  -0.0001 -0.0224 173 LEU A CG  
1429 C CD1 . LEU A 171 ? 0.2198 0.2082 0.2275 0.0024  -0.0014 -0.0192 173 LEU A CD1 
1430 C CD2 . LEU A 171 ? 0.2092 0.2099 0.2171 -0.0017 0.0012  -0.0249 173 LEU A CD2 
1431 N N   . ILE A 172 ? 0.1607 0.1435 0.1824 0.0022  -0.0025 -0.0210 174 ILE A N   
1432 C CA  . ILE A 172 ? 0.1568 0.1348 0.1825 0.0019  -0.0045 -0.0233 174 ILE A CA  
1433 C C   . ILE A 172 ? 0.1661 0.1392 0.1894 0.0022  -0.0072 -0.0249 174 ILE A C   
1434 O O   . ILE A 172 ? 0.1704 0.1430 0.1888 0.0026  -0.0073 -0.0246 174 ILE A O   
1435 C CB  . ILE A 172 ? 0.1801 0.1548 0.2097 0.0024  -0.0048 -0.0222 174 ILE A CB  
1436 C CG1 . ILE A 172 ? 0.1730 0.1431 0.1997 0.0032  -0.0054 -0.0216 174 ILE A CG1 
1437 C CG2 . ILE A 172 ? 0.1981 0.1779 0.2319 0.0025  -0.0017 -0.0194 174 ILE A CG2 
1438 C CD1 . ILE A 172 ? 0.1950 0.1609 0.2263 0.0027  -0.0061 -0.0231 174 ILE A CD1 
1439 N N   . ASP A 173 ? 0.1755 0.1461 0.2026 0.0021  -0.0093 -0.0260 175 ASP A N   
1440 C CA  . ASP A 173 ? 0.1804 0.1483 0.2065 0.0028  -0.0120 -0.0263 175 ASP A CA  
1441 C C   . ASP A 173 ? 0.1740 0.1423 0.1991 0.0030  -0.0110 -0.0264 175 ASP A C   
1442 O O   . ASP A 173 ? 0.1906 0.1578 0.2109 0.0037  -0.0114 -0.0257 175 ASP A O   
1443 C CB  . ASP A 173 ? 0.2249 0.1902 0.2463 0.0033  -0.0140 -0.0261 175 ASP A CB  
1444 C CG  . ASP A 173 ? 0.3869 0.3522 0.4084 0.0037  -0.0173 -0.0261 175 ASP A CG  
1445 O OD1 . ASP A 173 ? 0.4943 0.4593 0.5132 0.0034  -0.0191 -0.0270 175 ASP A OD1 
1446 O OD2 . ASP A 173 ? 0.3748 0.3416 0.4001 0.0041  -0.0177 -0.0251 175 ASP A OD2 
1447 N N   . TRP A 174 ? 0.1707 0.1405 0.2017 0.0024  -0.0093 -0.0275 176 TRP A N   
1448 C CA  . TRP A 174 ? 0.1668 0.1367 0.2000 0.0022  -0.0072 -0.0284 176 TRP A CA  
1449 C C   . TRP A 174 ? 0.1490 0.1169 0.1867 0.0037  -0.0086 -0.0262 176 TRP A C   
1450 O O   . TRP A 174 ? 0.1815 0.1489 0.2248 0.0037  -0.0059 -0.0265 176 TRP A O   
1451 C CB  . TRP A 174 ? 0.1751 0.1484 0.2132 0.0003  -0.0034 -0.0315 176 TRP A CB  
1452 C CG  . TRP A 174 ? 0.1991 0.1771 0.2322 -0.0011 -0.0021 -0.0325 176 TRP A CG  
1453 C CD1 . TRP A 174 ? 0.1791 0.1595 0.2111 -0.0010 -0.0025 -0.0312 176 TRP A CD1 
1454 C CD2 . TRP A 174 ? 0.1725 0.1548 0.2018 -0.0025 0.0002  -0.0343 176 TRP A CD2 
1455 N NE1 . TRP A 174 ? 0.1729 0.1595 0.2008 -0.0019 -0.0006 -0.0311 176 TRP A NE1 
1456 C CE2 . TRP A 174 ? 0.1691 0.1574 0.1948 -0.0030 0.0007  -0.0332 176 TRP A CE2 
1457 C CE3 . TRP A 174 ? 0.1943 0.1766 0.2238 -0.0034 0.0020  -0.0366 176 TRP A CE3 
1458 C CZ2 . TRP A 174 ? 0.1643 0.1601 0.1859 -0.0045 0.0026  -0.0340 176 TRP A CZ2 
1459 C CZ3 . TRP A 174 ? 0.1938 0.1827 0.2191 -0.0053 0.0038  -0.0384 176 TRP A CZ3 
1460 C CH2 . TRP A 174 ? 0.1947 0.1909 0.2158 -0.0058 0.0039  -0.0370 176 TRP A CH2 
1461 N N   . GLY A 175 ? 0.1720 0.1396 0.2080 0.0049  -0.0123 -0.0239 177 GLY A N   
1462 C CA  . GLY A 175 ? 0.1757 0.1443 0.2159 0.0065  -0.0141 -0.0205 177 GLY A CA  
1463 C C   . GLY A 175 ? 0.2004 0.1685 0.2391 0.0080  -0.0137 -0.0181 177 GLY A C   
1464 O O   . GLY A 175 ? 0.2273 0.1970 0.2720 0.0097  -0.0137 -0.0143 177 GLY A O   
1465 N N   . LEU A 176 ? 0.2006 0.1669 0.2321 0.0076  -0.0131 -0.0194 178 LEU A N   
1466 C CA  . LEU A 176 ? 0.2015 0.1670 0.2321 0.0088  -0.0121 -0.0174 178 LEU A CA  
1467 C C   . LEU A 176 ? 0.2161 0.1801 0.2502 0.0076  -0.0075 -0.0199 178 LEU A C   
1468 O O   . LEU A 176 ? 0.2247 0.1877 0.2597 0.0084  -0.0059 -0.0186 178 LEU A O   
1469 C CB  . LEU A 176 ? 0.1949 0.1601 0.2156 0.0093  -0.0145 -0.0170 178 LEU A CB  
1470 C CG  . LEU A 176 ? 0.2818 0.2496 0.2989 0.0102  -0.0186 -0.0152 178 LEU A CG  
1471 C CD1 . LEU A 176 ? 0.3119 0.2788 0.3200 0.0104  -0.0197 -0.0155 178 LEU A CD1 
1472 C CD2 . LEU A 176 ? 0.3584 0.3301 0.3814 0.0121  -0.0196 -0.0104 178 LEU A CD2 
1473 N N   . ALA A 177 ? 0.1716 0.1363 0.2082 0.0054  -0.0051 -0.0239 179 ALA A N   
1474 C CA  . ALA A 177 ? 0.1886 0.1540 0.2276 0.0033  -0.0007 -0.0278 179 ALA A CA  
1475 C C   . ALA A 177 ? 0.1855 0.1490 0.2355 0.0037  0.0033  -0.0276 179 ALA A C   
1476 O O   . ALA A 177 ? 0.1993 0.1619 0.2567 0.0054  0.0032  -0.0243 179 ALA A O   
1477 C CB  . ALA A 177 ? 0.1809 0.1496 0.2199 0.0008  0.0010  -0.0321 179 ALA A CB  
1478 N N   . GLU A 178 ? 0.1887 0.1522 0.2406 0.0019  0.0072  -0.0308 180 GLU A N   
1479 C CA  . GLU A 178 ? 0.2085 0.1695 0.2726 0.0020  0.0124  -0.0311 180 GLU A CA  
1480 C C   . GLU A 178 ? 0.1845 0.1476 0.2525 -0.0022 0.0179  -0.0390 180 GLU A C   
1481 O O   . GLU A 178 ? 0.2027 0.1700 0.2622 -0.0047 0.0172  -0.0429 180 GLU A O   
1482 C CB  . GLU A 178 ? 0.2368 0.1954 0.3019 0.0046  0.0122  -0.0259 180 GLU A CB  
1483 C CG  . GLU A 178 ? 0.2961 0.2537 0.3687 0.0085  0.0113  -0.0182 180 GLU A CG  
1484 C CD  . GLU A 178 ? 0.3439 0.2997 0.4329 0.0088  0.0172  -0.0179 180 GLU A CD  
1485 O OE1 . GLU A 178 ? 0.3489 0.3050 0.4458 0.0124  0.0173  -0.0102 180 GLU A OE1 
1486 O OE2 . GLU A 178 ? 0.2811 0.2361 0.3759 0.0056  0.0220  -0.0248 180 GLU A OE2 
1487 N N   . PHE A 179 ? 0.1793 0.1401 0.2608 -0.0030 0.0239  -0.0413 181 PHE A N   
1488 C CA  . PHE A 179 ? 0.1730 0.1357 0.2606 -0.0074 0.0303  -0.0497 181 PHE A CA  
1489 C C   . PHE A 179 ? 0.2164 0.1774 0.3048 -0.0076 0.0322  -0.0494 181 PHE A C   
1490 O O   . PHE A 179 ? 0.2273 0.1836 0.3210 -0.0039 0.0323  -0.0427 181 PHE A O   
1491 C CB  . PHE A 179 ? 0.2280 0.1878 0.3319 -0.0083 0.0371  -0.0525 181 PHE A CB  
1492 C CG  . PHE A 179 ? 0.1963 0.1581 0.3007 -0.0087 0.0364  -0.0539 181 PHE A CG  
1493 C CD1 . PHE A 179 ? 0.1894 0.1487 0.2950 -0.0046 0.0325  -0.0463 181 PHE A CD1 
1494 C CD2 . PHE A 179 ? 0.2357 0.2031 0.3393 -0.0134 0.0394  -0.0629 181 PHE A CD2 
1495 C CE1 . PHE A 179 ? 0.2223 0.1836 0.3288 -0.0051 0.0319  -0.0476 181 PHE A CE1 
1496 C CE2 . PHE A 179 ? 0.1924 0.1619 0.2965 -0.0137 0.0389  -0.0640 181 PHE A CE2 
1497 C CZ  . PHE A 179 ? 0.1991 0.1649 0.3049 -0.0095 0.0352  -0.0562 181 PHE A CZ  
1498 N N   . TYR A 180 ? 0.1933 0.1595 0.2769 -0.0117 0.0338  -0.0563 182 TYR A N   
1499 C CA  . TYR A 180 ? 0.1983 0.1637 0.2833 -0.0126 0.0361  -0.0573 182 TYR A CA  
1500 C C   . TYR A 180 ? 0.2023 0.1651 0.3041 -0.0156 0.0450  -0.0634 182 TYR A C   
1501 O O   . TYR A 180 ? 0.2014 0.1686 0.3080 -0.0205 0.0497  -0.0729 182 TYR A O   
1502 C CB  . TYR A 180 ? 0.1864 0.1598 0.2593 -0.0160 0.0338  -0.0616 182 TYR A CB  
1503 C CG  . TYR A 180 ? 0.1983 0.1711 0.2743 -0.0173 0.0368  -0.0632 182 TYR A CG  
1504 C CD1 . TYR A 180 ? 0.2100 0.1772 0.2840 -0.0129 0.0342  -0.0551 182 TYR A CD1 
1505 C CD2 . TYR A 180 ? 0.1942 0.1723 0.2763 -0.0231 0.0427  -0.0731 182 TYR A CD2 
1506 C CE1 . TYR A 180 ? 0.1789 0.1452 0.2568 -0.0139 0.0373  -0.0561 182 TYR A CE1 
1507 C CE2 . TYR A 180 ? 0.2216 0.1989 0.3079 -0.0245 0.0459  -0.0748 182 TYR A CE2 
1508 C CZ  . TYR A 180 ? 0.1995 0.1705 0.2838 -0.0197 0.0431  -0.0660 182 TYR A CZ  
1509 O OH  . TYR A 180 ? 0.2063 0.1765 0.2956 -0.0212 0.0466  -0.0676 182 TYR A OH  
1510 N N   . HIS A 181 ? 0.2041 0.1606 0.3155 -0.0127 0.0478  -0.0583 183 HIS A N   
1511 C CA  . HIS A 181 ? 0.2522 0.2052 0.3816 -0.0151 0.0572  -0.0633 183 HIS A CA  
1512 C C   . HIS A 181 ? 0.2388 0.1905 0.3688 -0.0150 0.0584  -0.0618 183 HIS A C   
1513 O O   . HIS A 181 ? 0.2579 0.2066 0.3833 -0.0098 0.0540  -0.0517 183 HIS A O   
1514 C CB  . HIS A 181 ? 0.2760 0.2221 0.4214 -0.0110 0.0612  -0.0568 183 HIS A CB  
1515 C CG  . HIS A 181 ? 0.2637 0.2107 0.4107 -0.0111 0.0609  -0.0581 183 HIS A CG  
1516 N ND1 . HIS A 181 ? 0.2897 0.2382 0.4457 -0.0161 0.0676  -0.0686 183 HIS A ND1 
1517 C CD2 . HIS A 181 ? 0.2741 0.2210 0.4154 -0.0070 0.0549  -0.0505 183 HIS A CD2 
1518 C CE1 . HIS A 181 ? 0.2634 0.2122 0.4190 -0.0146 0.0656  -0.0668 183 HIS A CE1 
1519 N NE2 . HIS A 181 ? 0.2417 0.1895 0.3888 -0.0092 0.0579  -0.0558 183 HIS A NE2 
1520 N N   . PRO A 182 ? 0.2449 0.1994 0.3803 -0.0206 0.0643  -0.0718 184 PRO A N   
1521 C CA  . PRO A 182 ? 0.2140 0.1678 0.3499 -0.0208 0.0654  -0.0707 184 PRO A CA  
1522 C C   . PRO A 182 ? 0.2548 0.1998 0.4035 -0.0153 0.0685  -0.0606 184 PRO A C   
1523 O O   . PRO A 182 ? 0.2384 0.1781 0.4048 -0.0143 0.0754  -0.0597 184 PRO A O   
1524 C CB  . PRO A 182 ? 0.2669 0.2252 0.4119 -0.0286 0.0733  -0.0848 184 PRO A CB  
1525 C CG  . PRO A 182 ? 0.3514 0.3170 0.4912 -0.0328 0.0727  -0.0931 184 PRO A CG  
1526 C CD  . PRO A 182 ? 0.2750 0.2354 0.4151 -0.0277 0.0698  -0.0853 184 PRO A CD  
1527 N N   . GLY A 183 ? 0.2349 0.1793 0.3753 -0.0115 0.0637  -0.0524 185 GLY A N   
1528 C CA  . GLY A 183 ? 0.2748 0.2132 0.4258 -0.0060 0.0660  -0.0417 185 GLY A CA  
1529 C C   . GLY A 183 ? 0.2584 0.1953 0.4072 0.0006  0.0611  -0.0297 185 GLY A C   
1530 O O   . GLY A 183 ? 0.2707 0.2052 0.4265 0.0057  0.0620  -0.0192 185 GLY A O   
1531 N N   . GLN A 184 ? 0.2425 0.1819 0.3822 0.0005  0.0561  -0.0307 186 GLN A N   
1532 C CA  . GLN A 184 ? 0.2559 0.1955 0.3936 0.0061  0.0513  -0.0203 186 GLN A CA  
1533 C C   . GLN A 184 ? 0.2532 0.1956 0.3740 0.0096  0.0428  -0.0130 186 GLN A C   
1534 O O   . GLN A 184 ? 0.2333 0.1782 0.3393 0.0073  0.0383  -0.0175 186 GLN A O   
1535 C CB  . GLN A 184 ? 0.2804 0.2218 0.4144 0.0044  0.0490  -0.0246 186 GLN A CB  
1536 C CG  . GLN A 184 ? 0.3211 0.2633 0.4556 0.0093  0.0449  -0.0151 186 GLN A CG  
1537 C CD  . GLN A 184 ? 0.4087 0.3510 0.5477 0.0074  0.0464  -0.0199 186 GLN A CD  
1538 O OE1 . GLN A 184 ? 0.4739 0.4190 0.6040 0.0088  0.0403  -0.0174 186 GLN A OE1 
1539 N NE2 . GLN A 184 ? 0.4080 0.3475 0.5615 0.0039  0.0550  -0.0274 186 GLN A NE2 
1540 N N   . GLU A 185 ? 0.2475 0.1905 0.3715 0.0151  0.0410  -0.0016 187 GLU A N   
1541 C CA  . GLU A 185 ? 0.2654 0.2122 0.3742 0.0185  0.0331  0.0053  187 GLU A CA  
1542 C C   . GLU A 185 ? 0.2962 0.2464 0.3962 0.0196  0.0267  0.0070  187 GLU A C   
1543 O O   . GLU A 185 ? 0.3139 0.2649 0.4238 0.0213  0.0282  0.0106  187 GLU A O   
1544 C CB  . GLU A 185 ? 0.3116 0.2597 0.4282 0.0236  0.0347  0.0167  187 GLU A CB  
1545 C CG  . GLU A 185 ? 0.3749 0.3192 0.5011 0.0226  0.0413  0.0156  187 GLU A CG  
1546 C CD  . GLU A 185 ? 0.5283 0.4750 0.6583 0.0279  0.0417  0.0275  187 GLU A CD  
1547 O OE1 . GLU A 185 ? 0.5538 0.5000 0.6781 0.0276  0.0414  0.0271  187 GLU A OE1 
1548 O OE2 . GLU A 185 ? 0.5829 0.5332 0.7218 0.0325  0.0423  0.0378  187 GLU A OE2 
1549 N N   . TYR A 186 ? 0.2317 0.1842 0.3143 0.0187  0.0200  0.0045  188 TYR A N   
1550 C CA  . TYR A 186 ? 0.1951 0.1505 0.2691 0.0188  0.0143  0.0042  188 TYR A CA  
1551 C C   . TYR A 186 ? 0.2012 0.1613 0.2651 0.0221  0.0082  0.0111  188 TYR A C   
1552 O O   . TYR A 186 ? 0.2440 0.2050 0.3036 0.0237  0.0075  0.0145  188 TYR A O   
1553 C CB  . TYR A 186 ? 0.2167 0.1714 0.2803 0.0146  0.0125  -0.0049 188 TYR A CB  
1554 C CG  . TYR A 186 ? 0.1944 0.1471 0.2671 0.0108  0.0181  -0.0124 188 TYR A CG  
1555 C CD1 . TYR A 186 ? 0.2448 0.1977 0.3241 0.0102  0.0192  -0.0140 188 TYR A CD1 
1556 C CD2 . TYR A 186 ? 0.2244 0.1761 0.2997 0.0076  0.0226  -0.0184 188 TYR A CD2 
1557 C CE1 . TYR A 186 ? 0.2656 0.2173 0.3532 0.0065  0.0247  -0.0215 188 TYR A CE1 
1558 C CE2 . TYR A 186 ? 0.2102 0.1617 0.2940 0.0035  0.0280  -0.0264 188 TYR A CE2 
1559 C CZ  . TYR A 186 ? 0.2274 0.1788 0.3171 0.0030  0.0292  -0.0280 188 TYR A CZ  
1560 O OH  . TYR A 186 ? 0.2368 0.1887 0.3348 -0.0014 0.0350  -0.0367 188 TYR A OH  
1561 N N   . ASN A 187 ? 0.2100 0.1738 0.2704 0.0228  0.0038  0.0125  189 ASN A N   
1562 C CA  . ASN A 187 ? 0.2043 0.1738 0.2540 0.0247  -0.0022 0.0167  189 ASN A CA  
1563 C C   . ASN A 187 ? 0.2036 0.1712 0.2386 0.0227  -0.0052 0.0112  189 ASN A C   
1564 O O   . ASN A 187 ? 0.2383 0.2025 0.2696 0.0197  -0.0050 0.0044  189 ASN A O   
1565 C CB  . ASN A 187 ? 0.2469 0.2209 0.2971 0.0249  -0.0057 0.0177  189 ASN A CB  
1566 C CG  . ASN A 187 ? 0.3258 0.3077 0.3662 0.0262  -0.0116 0.0210  189 ASN A CG  
1567 O OD1 . ASN A 187 ? 0.3232 0.3078 0.3573 0.0276  -0.0130 0.0237  189 ASN A OD1 
1568 N ND2 . ASN A 187 ? 0.5054 0.4917 0.5452 0.0256  -0.0149 0.0204  189 ASN A ND2 
1569 N N   . VAL A 188 ? 0.2371 0.2076 0.2647 0.0245  -0.0075 0.0147  190 VAL A N   
1570 C CA  . VAL A 188 ? 0.2247 0.1933 0.2394 0.0229  -0.0098 0.0101  190 VAL A CA  
1571 C C   . VAL A 188 ? 0.2178 0.1898 0.2236 0.0221  -0.0146 0.0080  190 VAL A C   
1572 O O   . VAL A 188 ? 0.2677 0.2375 0.2642 0.0207  -0.0159 0.0038  190 VAL A O   
1573 C CB  . VAL A 188 ? 0.2415 0.2107 0.2521 0.0247  -0.0093 0.0136  190 VAL A CB  
1574 C CG1 . VAL A 188 ? 0.2768 0.2421 0.2967 0.0247  -0.0040 0.0144  190 VAL A CG1 
1575 C CG2 . VAL A 188 ? 0.2573 0.2344 0.2664 0.0278  -0.0120 0.0206  190 VAL A CG2 
1576 N N   . ARG A 189 ? 0.2467 0.2240 0.2560 0.0229  -0.0169 0.0106  191 ARG A N   
1577 C CA  . ARG A 189 ? 0.2902 0.2714 0.2924 0.0216  -0.0211 0.0076  191 ARG A CA  
1578 C C   . ARG A 189 ? 0.2724 0.2491 0.2760 0.0190  -0.0208 0.0019  191 ARG A C   
1579 O O   . ARG A 189 ? 0.2994 0.2790 0.3070 0.0185  -0.0223 0.0018  191 ARG A O   
1580 C CB  . ARG A 189 ? 0.2678 0.2591 0.2728 0.0233  -0.0239 0.0132  191 ARG A CB  
1581 C CG  . ARG A 189 ? 0.3436 0.3419 0.3460 0.0260  -0.0246 0.0194  191 ARG A CG  
1582 C CD  . ARG A 189 ? 0.5433 0.5550 0.5458 0.0270  -0.0284 0.0239  191 ARG A CD  
1583 N NE  . ARG A 189 ? 0.7040 0.7193 0.6970 0.0240  -0.0322 0.0172  191 ARG A NE  
1584 C CZ  . ARG A 189 ? 0.7764 0.8033 0.7688 0.0232  -0.0359 0.0178  191 ARG A CZ  
1585 N NH1 . ARG A 189 ? 0.7536 0.7828 0.7383 0.0198  -0.0384 0.0102  191 ARG A NH1 
1586 N NH2 . ARG A 189 ? 0.7800 0.8172 0.7806 0.0257  -0.0366 0.0262  191 ARG A NH2 
1587 N N   . VAL A 190 ? 0.2405 0.2109 0.2409 0.0174  -0.0187 -0.0024 192 VAL A N   
1588 C CA  . VAL A 190 ? 0.2159 0.1831 0.2167 0.0150  -0.0180 -0.0074 192 VAL A CA  
1589 C C   . VAL A 190 ? 0.2362 0.2008 0.2284 0.0139  -0.0183 -0.0108 192 VAL A C   
1590 O O   . VAL A 190 ? 0.2360 0.2004 0.2225 0.0147  -0.0185 -0.0098 192 VAL A O   
1591 C CB  . VAL A 190 ? 0.2298 0.1940 0.2379 0.0141  -0.0141 -0.0087 192 VAL A CB  
1592 C CG1 . VAL A 190 ? 0.2640 0.2298 0.2828 0.0154  -0.0127 -0.0053 192 VAL A CG1 
1593 C CG2 . VAL A 190 ? 0.2361 0.1981 0.2421 0.0140  -0.0115 -0.0090 192 VAL A CG2 
1594 N N   . ALA A 191 ? 0.2573 0.2203 0.2496 0.0121  -0.0179 -0.0142 193 ALA A N   
1595 C CA  . ALA A 191 ? 0.2433 0.2041 0.2300 0.0112  -0.0173 -0.0166 193 ALA A CA  
1596 C C   . ALA A 191 ? 0.2480 0.2096 0.2298 0.0113  -0.0194 -0.0177 193 ALA A C   
1597 O O   . ALA A 191 ? 0.3416 0.3065 0.3218 0.0122  -0.0215 -0.0162 193 ALA A O   
1598 C CB  . ALA A 191 ? 0.2276 0.1870 0.2114 0.0115  -0.0149 -0.0159 193 ALA A CB  
1599 N N   . SER A 192 ? 0.2270 0.1863 0.2069 0.0103  -0.0184 -0.0202 194 SER A N   
1600 C CA  . SER A 192 ? 0.2101 0.1696 0.1860 0.0098  -0.0192 -0.0226 194 SER A CA  
1601 C C   . SER A 192 ? 0.2138 0.1719 0.1839 0.0110  -0.0180 -0.0215 194 SER A C   
1602 O O   . SER A 192 ? 0.2123 0.1684 0.1819 0.0118  -0.0159 -0.0194 194 SER A O   
1603 C CB  . SER A 192 ? 0.3308 0.2876 0.3092 0.0083  -0.0173 -0.0257 194 SER A CB  
1604 O OG  . SER A 192 ? 0.6318 0.5903 0.6155 0.0071  -0.0187 -0.0270 194 SER A OG  
1605 N N   . ARG A 193 ? 0.2152 0.1756 0.1810 0.0108  -0.0193 -0.0232 195 ARG A N   
1606 C CA  . ARG A 193 ? 0.1833 0.1434 0.1435 0.0121  -0.0184 -0.0220 195 ARG A CA  
1607 C C   . ARG A 193 ? 0.2147 0.1697 0.1741 0.0127  -0.0149 -0.0210 195 ARG A C   
1608 O O   . ARG A 193 ? 0.2159 0.1705 0.1733 0.0142  -0.0142 -0.0177 195 ARG A O   
1609 C CB  . ARG A 193 ? 0.2225 0.1856 0.1784 0.0108  -0.0191 -0.0261 195 ARG A CB  
1610 C CG  . ARG A 193 ? 0.2364 0.2000 0.1861 0.0122  -0.0182 -0.0248 195 ARG A CG  
1611 C CD  . ARG A 193 ? 0.2905 0.2568 0.2363 0.0103  -0.0178 -0.0305 195 ARG A CD  
1612 N NE  . ARG A 193 ? 0.3565 0.3312 0.3023 0.0085  -0.0213 -0.0330 195 ARG A NE  
1613 C CZ  . ARG A 193 ? 0.4126 0.3900 0.3586 0.0053  -0.0210 -0.0401 195 ARG A CZ  
1614 N NH1 . ARG A 193 ? 0.3698 0.3407 0.3167 0.0039  -0.0167 -0.0453 195 ARG A NH1 
1615 N NH2 . ARG A 193 ? 0.4351 0.4223 0.3812 0.0035  -0.0245 -0.0420 195 ARG A NH2 
1616 N N   . TYR A 194 ? 0.2071 0.1588 0.1689 0.0117  -0.0124 -0.0233 196 TYR A N   
1617 C CA  . TYR A 194 ? 0.1990 0.1473 0.1607 0.0127  -0.0087 -0.0214 196 TYR A CA  
1618 C C   . TYR A 194 ? 0.2151 0.1646 0.1788 0.0134  -0.0081 -0.0175 196 TYR A C   
1619 O O   . TYR A 194 ? 0.2072 0.1564 0.1701 0.0144  -0.0056 -0.0147 196 TYR A O   
1620 C CB  . TYR A 194 ? 0.2231 0.1682 0.1892 0.0118  -0.0054 -0.0238 196 TYR A CB  
1621 C CG  . TYR A 194 ? 0.2099 0.1545 0.1756 0.0100  -0.0054 -0.0296 196 TYR A CG  
1622 C CD1 . TYR A 194 ? 0.2183 0.1642 0.1782 0.0099  -0.0060 -0.0318 196 TYR A CD1 
1623 C CD2 . TYR A 194 ? 0.2829 0.2268 0.2542 0.0080  -0.0048 -0.0334 196 TYR A CD2 
1624 C CE1 . TYR A 194 ? 0.2605 0.2079 0.2197 0.0075  -0.0059 -0.0383 196 TYR A CE1 
1625 C CE2 . TYR A 194 ? 0.3378 0.2824 0.3091 0.0055  -0.0046 -0.0400 196 TYR A CE2 
1626 C CZ  . TYR A 194 ? 0.3406 0.2875 0.3057 0.0052  -0.0052 -0.0427 196 TYR A CZ  
1627 O OH  . TYR A 194 ? 0.3799 0.3296 0.3446 0.0021  -0.0050 -0.0502 196 TYR A OH  
1628 N N   . PHE A 195 ? 0.1935 0.1453 0.1601 0.0128  -0.0100 -0.0173 197 PHE A N   
1629 C CA  . PHE A 195 ? 0.1657 0.1198 0.1348 0.0126  -0.0091 -0.0152 197 PHE A CA  
1630 C C   . PHE A 195 ? 0.1803 0.1360 0.1491 0.0128  -0.0105 -0.0143 197 PHE A C   
1631 O O   . PHE A 195 ? 0.2053 0.1634 0.1769 0.0120  -0.0095 -0.0139 197 PHE A O   
1632 C CB  . PHE A 195 ? 0.1765 0.1319 0.1508 0.0114  -0.0089 -0.0163 197 PHE A CB  
1633 C CG  . PHE A 195 ? 0.1634 0.1168 0.1397 0.0113  -0.0068 -0.0166 197 PHE A CG  
1634 C CD1 . PHE A 195 ? 0.1807 0.1357 0.1587 0.0120  -0.0036 -0.0135 197 PHE A CD1 
1635 C CD2 . PHE A 195 ? 0.2052 0.1560 0.1826 0.0106  -0.0076 -0.0199 197 PHE A CD2 
1636 C CE1 . PHE A 195 ? 0.2044 0.1571 0.1862 0.0123  -0.0006 -0.0130 197 PHE A CE1 
1637 C CE2 . PHE A 195 ? 0.2007 0.1489 0.1815 0.0103  -0.0047 -0.0208 197 PHE A CE2 
1638 C CZ  . PHE A 195 ? 0.2221 0.1706 0.2058 0.0114  -0.0009 -0.0170 197 PHE A CZ  
1639 N N   . LYS A 196 ? 0.1953 0.1506 0.1617 0.0138  -0.0123 -0.0139 198 LYS A N   
1640 C CA  . LYS A 196 ? 0.1894 0.1460 0.1573 0.0145  -0.0128 -0.0120 198 LYS A CA  
1641 C C   . LYS A 196 ? 0.1921 0.1487 0.1585 0.0148  -0.0107 -0.0104 198 LYS A C   
1642 O O   . LYS A 196 ? 0.2133 0.1689 0.1750 0.0157  -0.0100 -0.0095 198 LYS A O   
1643 C CB  . LYS A 196 ? 0.2160 0.1740 0.1816 0.0158  -0.0150 -0.0107 198 LYS A CB  
1644 C CG  . LYS A 196 ? 0.1900 0.1504 0.1582 0.0153  -0.0175 -0.0118 198 LYS A CG  
1645 C CD  . LYS A 196 ? 0.1932 0.1580 0.1582 0.0164  -0.0197 -0.0102 198 LYS A CD  
1646 C CE  . LYS A 196 ? 0.2284 0.1979 0.1958 0.0156  -0.0225 -0.0112 198 LYS A CE  
1647 N NZ  . LYS A 196 ? 0.2719 0.2433 0.2468 0.0165  -0.0227 -0.0077 198 LYS A NZ  
1648 N N   . GLY A 197 ? 0.2065 0.1647 0.1775 0.0139  -0.0094 -0.0104 199 GLY A N   
1649 C CA  . GLY A 197 ? 0.2152 0.1745 0.1857 0.0137  -0.0073 -0.0095 199 GLY A CA  
1650 C C   . GLY A 197 ? 0.1842 0.1421 0.1533 0.0156  -0.0075 -0.0067 199 GLY A C   
1651 O O   . GLY A 197 ? 0.1959 0.1534 0.1661 0.0170  -0.0090 -0.0050 199 GLY A O   
1652 N N   . PRO A 198 ? 0.1765 0.1349 0.1432 0.0159  -0.0060 -0.0055 200 PRO A N   
1653 C CA  . PRO A 198 ? 0.2181 0.1756 0.1842 0.0178  -0.0057 -0.0024 200 PRO A CA  
1654 C C   . PRO A 198 ? 0.2466 0.2041 0.2203 0.0181  -0.0049 -0.0010 200 PRO A C   
1655 O O   . PRO A 198 ? 0.2213 0.1789 0.1950 0.0205  -0.0056 0.0028  200 PRO A O   
1656 C CB  . PRO A 198 ? 0.2219 0.1807 0.1867 0.0170  -0.0036 -0.0021 200 PRO A CB  
1657 C CG  . PRO A 198 ? 0.2487 0.2091 0.2102 0.0159  -0.0036 -0.0035 200 PRO A CG  
1658 C CD  . PRO A 198 ? 0.2190 0.1798 0.1836 0.0146  -0.0045 -0.0061 200 PRO A CD  
1659 N N   . GLU A 199 ? 0.1926 0.1507 0.1736 0.0159  -0.0030 -0.0038 201 GLU A N   
1660 C CA  . GLU A 199 ? 0.2094 0.1669 0.2000 0.0164  -0.0011 -0.0024 201 GLU A CA  
1661 C C   . GLU A 199 ? 0.2243 0.1821 0.2156 0.0188  -0.0036 0.0010  201 GLU A C   
1662 O O   . GLU A 199 ? 0.2222 0.1808 0.2190 0.0210  -0.0028 0.0057  201 GLU A O   
1663 C CB  . GLU A 199 ? 0.2043 0.1624 0.2028 0.0132  0.0017  -0.0073 201 GLU A CB  
1664 C CG  . GLU A 199 ? 0.2074 0.1668 0.2043 0.0114  0.0002  -0.0109 201 GLU A CG  
1665 C CD  . GLU A 199 ? 0.2039 0.1666 0.1945 0.0092  0.0000  -0.0138 201 GLU A CD  
1666 O OE1 . GLU A 199 ? 0.2288 0.1914 0.2120 0.0106  -0.0015 -0.0115 201 GLU A OE1 
1667 O OE2 . GLU A 199 ? 0.2065 0.1728 0.2000 0.0063  0.0015  -0.0180 201 GLU A OE2 
1668 N N   . LEU A 200 ? 0.1838 0.1422 0.1704 0.0184  -0.0065 -0.0008 202 LEU A N   
1669 C CA  . LEU A 200 ? 0.1866 0.1472 0.1736 0.0201  -0.0092 0.0019  202 LEU A CA  
1670 C C   . LEU A 200 ? 0.2000 0.1631 0.1803 0.0225  -0.0112 0.0056  202 LEU A C   
1671 O O   . LEU A 200 ? 0.2242 0.1916 0.2070 0.0246  -0.0123 0.0103  202 LEU A O   
1672 C CB  . LEU A 200 ? 0.1767 0.1374 0.1607 0.0186  -0.0114 -0.0017 202 LEU A CB  
1673 C CG  . LEU A 200 ? 0.1918 0.1511 0.1807 0.0161  -0.0096 -0.0057 202 LEU A CG  
1674 C CD1 . LEU A 200 ? 0.2054 0.1651 0.1918 0.0150  -0.0118 -0.0084 202 LEU A CD1 
1675 C CD2 . LEU A 200 ? 0.1925 0.1518 0.1923 0.0160  -0.0069 -0.0049 202 LEU A CD2 
1676 N N   . LEU A 201 ? 0.2053 0.1670 0.1775 0.0222  -0.0114 0.0040  203 LEU A N   
1677 C CA  . LEU A 201 ? 0.2138 0.1780 0.1788 0.0239  -0.0130 0.0061  203 LEU A CA  
1678 C C   . LEU A 201 ? 0.2211 0.1870 0.1883 0.0263  -0.0115 0.0115  203 LEU A C   
1679 O O   . LEU A 201 ? 0.2562 0.2266 0.2190 0.0282  -0.0129 0.0147  203 LEU A O   
1680 C CB  . LEU A 201 ? 0.2059 0.1672 0.1632 0.0229  -0.0127 0.0025  203 LEU A CB  
1681 C CG  . LEU A 201 ? 0.2149 0.1747 0.1713 0.0208  -0.0135 -0.0021 203 LEU A CG  
1682 C CD1 . LEU A 201 ? 0.2233 0.1801 0.1749 0.0202  -0.0120 -0.0042 203 LEU A CD1 
1683 C CD2 . LEU A 201 ? 0.2264 0.1898 0.1811 0.0207  -0.0163 -0.0033 203 LEU A CD2 
1684 N N   . VAL A 202 ? 0.2467 0.2097 0.2209 0.0260  -0.0083 0.0125  204 VAL A N   
1685 C CA  . VAL A 202 ? 0.2461 0.2104 0.2250 0.0283  -0.0061 0.0180  204 VAL A CA  
1686 C C   . VAL A 202 ? 0.2197 0.1855 0.2107 0.0295  -0.0042 0.0221  204 VAL A C   
1687 O O   . VAL A 202 ? 0.2650 0.2312 0.2633 0.0314  -0.0012 0.0271  204 VAL A O   
1688 C CB  . VAL A 202 ? 0.2296 0.1902 0.2094 0.0272  -0.0030 0.0165  204 VAL A CB  
1689 C CG1 . VAL A 202 ? 0.2675 0.2271 0.2364 0.0266  -0.0043 0.0139  204 VAL A CG1 
1690 C CG2 . VAL A 202 ? 0.2206 0.1786 0.2083 0.0241  -0.0002 0.0119  204 VAL A CG2 
1691 N N   . ASP A 203 ? 0.2461 0.2127 0.2407 0.0286  -0.0054 0.0204  205 ASP A N   
1692 C CA  . ASP A 203 ? 0.2310 0.1997 0.2378 0.0301  -0.0036 0.0249  205 ASP A CA  
1693 C C   . ASP A 203 ? 0.3014 0.2650 0.3205 0.0289  0.0020  0.0236  205 ASP A C   
1694 O O   . ASP A 203 ? 0.3483 0.3127 0.3794 0.0310  0.0056  0.0294  205 ASP A O   
1695 C CB  . ASP A 203 ? 0.2347 0.2108 0.2428 0.0341  -0.0045 0.0339  205 ASP A CB  
1696 C CG  . ASP A 203 ? 0.5268 0.5078 0.5455 0.0359  -0.0042 0.0395  205 ASP A CG  
1697 O OD1 . ASP A 203 ? 0.5608 0.5387 0.5847 0.0340  -0.0036 0.0356  205 ASP A OD1 
1698 O OD2 . ASP A 203 ? 0.6499 0.6388 0.6720 0.0395  -0.0043 0.0483  205 ASP A OD2 
1699 N N   . TYR A 204 ? 0.2111 0.1704 0.2283 0.0252  0.0033  0.0161  206 TYR A N   
1700 C CA  . TYR A 204 ? 0.1984 0.1543 0.2271 0.0229  0.0087  0.0126  206 TYR A CA  
1701 C C   . TYR A 204 ? 0.1894 0.1446 0.2243 0.0208  0.0096  0.0085  206 TYR A C   
1702 O O   . TYR A 204 ? 0.2188 0.1741 0.2465 0.0184  0.0070  0.0031  206 TYR A O   
1703 C CB  . TYR A 204 ? 0.1964 0.1509 0.2200 0.0198  0.0098  0.0068  206 TYR A CB  
1704 C CG  . TYR A 204 ? 0.2071 0.1596 0.2428 0.0167  0.0158  0.0023  206 TYR A CG  
1705 C CD1 . TYR A 204 ? 0.2326 0.1835 0.2790 0.0178  0.0205  0.0057  206 TYR A CD1 
1706 C CD2 . TYR A 204 ? 0.1979 0.1510 0.2353 0.0124  0.0171  -0.0057 206 TYR A CD2 
1707 C CE1 . TYR A 204 ? 0.2391 0.1882 0.2982 0.0144  0.0268  0.0003  206 TYR A CE1 
1708 C CE2 . TYR A 204 ? 0.2282 0.1807 0.2771 0.0088  0.0230  -0.0113 206 TYR A CE2 
1709 C CZ  . TYR A 204 ? 0.2136 0.1637 0.2737 0.0096  0.0280  -0.0087 206 TYR A CZ  
1710 O OH  . TYR A 204 ? 0.2491 0.1986 0.3219 0.0055  0.0347  -0.0154 206 TYR A OH  
1711 N N   . GLN A 205 ? 0.1861 0.1405 0.2352 0.0220  0.0136  0.0116  207 GLN A N   
1712 C CA  . GLN A 205 ? 0.1820 0.1362 0.2373 0.0210  0.0141  0.0093  207 GLN A CA  
1713 C C   . GLN A 205 ? 0.2270 0.1783 0.2892 0.0164  0.0187  0.0005  207 GLN A C   
1714 O O   . GLN A 205 ? 0.2094 0.1609 0.2737 0.0149  0.0185  -0.0030 207 GLN A O   
1715 C CB  . GLN A 205 ? 0.2354 0.1912 0.3039 0.0248  0.0165  0.0178  207 GLN A CB  
1716 C CG  . GLN A 205 ? 0.2330 0.1950 0.2945 0.0289  0.0113  0.0264  207 GLN A CG  
1717 C CD  . GLN A 205 ? 0.2569 0.2229 0.3322 0.0328  0.0137  0.0358  207 GLN A CD  
1718 O OE1 . GLN A 205 ? 0.3424 0.3108 0.4251 0.0361  0.0164  0.0439  207 GLN A OE1 
1719 N NE2 . GLN A 205 ? 0.3056 0.2730 0.3854 0.0325  0.0129  0.0355  207 GLN A NE2 
1720 N N   . MET A 206 ? 0.1915 0.1412 0.2574 0.0139  0.0230  -0.0037 208 MET A N   
1721 C CA  . MET A 206 ? 0.1787 0.1276 0.2529 0.0090  0.0282  -0.0128 208 MET A CA  
1722 C C   . MET A 206 ? 0.2066 0.1592 0.2680 0.0050  0.0251  -0.0202 208 MET A C   
1723 O O   . MET A 206 ? 0.1995 0.1542 0.2610 0.0012  0.0277  -0.0263 208 MET A O   
1724 C CB  . MET A 206 ? 0.2273 0.1737 0.3149 0.0077  0.0354  -0.0141 208 MET A CB  
1725 C CG  . MET A 206 ? 0.2301 0.1754 0.3313 0.0029  0.0425  -0.0232 208 MET A CG  
1726 S SD  . MET A 206 ? 0.2485 0.1900 0.3692 0.0012  0.0525  -0.0253 208 MET A SD  
1727 C CE  . MET A 206 ? 0.3275 0.2650 0.4606 0.0087  0.0544  -0.0109 208 MET A CE  
1728 N N   . TYR A 207 ? 0.2057 0.1600 0.2568 0.0060  0.0196  -0.0193 209 TYR A N   
1729 C CA  . TYR A 207 ? 0.1965 0.1549 0.2358 0.0033  0.0165  -0.0239 209 TYR A CA  
1730 C C   . TYR A 207 ? 0.2289 0.1902 0.2717 -0.0004 0.0184  -0.0308 209 TYR A C   
1731 O O   . TYR A 207 ? 0.2315 0.1908 0.2859 -0.0013 0.0225  -0.0329 209 TYR A O   
1732 C CB  . TYR A 207 ? 0.1847 0.1432 0.2116 0.0065  0.0102  -0.0188 209 TYR A CB  
1733 C CG  . TYR A 207 ? 0.1676 0.1249 0.1953 0.0087  0.0075  -0.0158 209 TYR A CG  
1734 C CD1 . TYR A 207 ? 0.1835 0.1425 0.2103 0.0069  0.0066  -0.0195 209 TYR A CD1 
1735 C CD2 . TYR A 207 ? 0.1707 0.1268 0.1997 0.0127  0.0057  -0.0088 209 TYR A CD2 
1736 C CE1 . TYR A 207 ? 0.1944 0.1527 0.2222 0.0087  0.0041  -0.0169 209 TYR A CE1 
1737 C CE2 . TYR A 207 ? 0.1783 0.1354 0.2080 0.0143  0.0029  -0.0062 209 TYR A CE2 
1738 C CZ  . TYR A 207 ? 0.1928 0.1504 0.2221 0.0122  0.0022  -0.0105 209 TYR A CZ  
1739 O OH  . TYR A 207 ? 0.2080 0.1667 0.2382 0.0136  -0.0006 -0.0081 209 TYR A OH  
1740 N N   . ASP A 208 ? 0.1756 0.1422 0.2091 -0.0026 0.0159  -0.0341 210 ASP A N   
1741 C CA  . ASP A 208 ? 0.1603 0.1319 0.1967 -0.0066 0.0181  -0.0410 210 ASP A CA  
1742 C C   . ASP A 208 ? 0.1502 0.1267 0.1757 -0.0067 0.0139  -0.0404 210 ASP A C   
1743 O O   . ASP A 208 ? 0.1582 0.1322 0.1761 -0.0033 0.0096  -0.0348 210 ASP A O   
1744 C CB  . ASP A 208 ? 0.1839 0.1606 0.2258 -0.0116 0.0233  -0.0486 210 ASP A CB  
1745 C CG  . ASP A 208 ? 0.2234 0.2055 0.2567 -0.0126 0.0216  -0.0483 210 ASP A CG  
1746 O OD1 . ASP A 208 ? 0.2211 0.2008 0.2579 -0.0124 0.0237  -0.0476 210 ASP A OD1 
1747 O OD2 . ASP A 208 ? 0.2141 0.2032 0.2380 -0.0134 0.0186  -0.0481 210 ASP A OD2 
1748 N N   . TYR A 209 ? 0.1760 0.1603 0.2017 -0.0106 0.0157  -0.0463 211 TYR A N   
1749 C CA  . TYR A 209 ? 0.1787 0.1693 0.1963 -0.0108 0.0127  -0.0453 211 TYR A CA  
1750 C C   . TYR A 209 ? 0.1599 0.1523 0.1678 -0.0088 0.0094  -0.0402 211 TYR A C   
1751 O O   . TYR A 209 ? 0.1684 0.1619 0.1704 -0.0070 0.0066  -0.0366 211 TYR A O   
1752 C CB  . TYR A 209 ? 0.1504 0.1525 0.1693 -0.0159 0.0157  -0.0523 211 TYR A CB  
1753 C CG  . TYR A 209 ? 0.1628 0.1649 0.1921 -0.0193 0.0206  -0.0597 211 TYR A CG  
1754 C CD1 . TYR A 209 ? 0.1616 0.1684 0.1970 -0.0238 0.0254  -0.0671 211 TYR A CD1 
1755 C CD2 . TYR A 209 ? 0.1670 0.1648 0.2012 -0.0182 0.0209  -0.0597 211 TYR A CD2 
1756 C CE1 . TYR A 209 ? 0.1746 0.1812 0.2211 -0.0273 0.0310  -0.0748 211 TYR A CE1 
1757 C CE2 . TYR A 209 ? 0.1774 0.1750 0.2223 -0.0213 0.0262  -0.0665 211 TYR A CE2 
1758 C CZ  . TYR A 209 ? 0.1568 0.1586 0.2081 -0.0258 0.0315  -0.0743 211 TYR A CZ  
1759 O OH  . TYR A 209 ? 0.1905 0.1916 0.2536 -0.0291 0.0376  -0.0817 211 TYR A OH  
1760 N N   . SER A 210 ? 0.1597 0.1524 0.1668 -0.0091 0.0103  -0.0400 212 SER A N   
1761 C CA  . SER A 210 ? 0.1475 0.1425 0.1462 -0.0074 0.0079  -0.0354 212 SER A CA  
1762 C C   . SER A 210 ? 0.1486 0.1353 0.1425 -0.0027 0.0044  -0.0291 212 SER A C   
1763 O O   . SER A 210 ? 0.1644 0.1527 0.1519 -0.0011 0.0027  -0.0252 212 SER A O   
1764 C CB  . SER A 210 ? 0.1947 0.1914 0.1947 -0.0088 0.0099  -0.0367 212 SER A CB  
1765 O OG  . SER A 210 ? 0.1976 0.1851 0.2037 -0.0073 0.0112  -0.0363 212 SER A OG  
1766 N N   . LEU A 211 ? 0.1545 0.1333 0.1520 -0.0007 0.0035  -0.0280 213 LEU A N   
1767 C CA  . LEU A 211 ? 0.1745 0.1478 0.1675 0.0029  0.0002  -0.0234 213 LEU A CA  
1768 C C   . LEU A 211 ? 0.1577 0.1338 0.1467 0.0029  -0.0013 -0.0226 213 LEU A C   
1769 O O   . LEU A 211 ? 0.1723 0.1466 0.1560 0.0050  -0.0029 -0.0193 213 LEU A O   
1770 C CB  . LEU A 211 ? 0.1912 0.1589 0.1896 0.0044  -0.0004 -0.0226 213 LEU A CB  
1771 C CG  . LEU A 211 ? 0.1977 0.1621 0.1922 0.0070  -0.0040 -0.0194 213 LEU A CG  
1772 C CD1 . LEU A 211 ? 0.2186 0.1809 0.2064 0.0093  -0.0057 -0.0160 213 LEU A CD1 
1773 C CD2 . LEU A 211 ? 0.1958 0.1578 0.1967 0.0081  -0.0046 -0.0184 213 LEU A CD2 
1774 N N   . ASP A 212 ? 0.1545 0.1352 0.1468 0.0007  -0.0001 -0.0256 214 ASP A N   
1775 C CA  . ASP A 212 ? 0.1587 0.1426 0.1488 0.0010  -0.0009 -0.0241 214 ASP A CA  
1776 C C   . ASP A 212 ? 0.1616 0.1517 0.1469 0.0012  -0.0004 -0.0212 214 ASP A C   
1777 O O   . ASP A 212 ? 0.1658 0.1562 0.1494 0.0028  -0.0010 -0.0178 214 ASP A O   
1778 C CB  . ASP A 212 ? 0.1519 0.1412 0.1466 -0.0015 0.0006  -0.0277 214 ASP A CB  
1779 C CG  . ASP A 212 ? 0.1909 0.1743 0.1913 -0.0012 0.0003  -0.0295 214 ASP A CG  
1780 O OD1 . ASP A 212 ? 0.1814 0.1576 0.1813 0.0013  -0.0020 -0.0270 214 ASP A OD1 
1781 O OD2 . ASP A 212 ? 0.1783 0.1652 0.1838 -0.0037 0.0026  -0.0336 214 ASP A OD2 
1782 N N   . MET A 213 ? 0.1615 0.1570 0.1458 -0.0005 0.0010  -0.0222 215 MET A N   
1783 C CA  . MET A 213 ? 0.1700 0.1734 0.1505 -0.0003 0.0016  -0.0187 215 MET A CA  
1784 C C   . MET A 213 ? 0.1689 0.1655 0.1455 0.0031  0.0005  -0.0141 215 MET A C   
1785 O O   . MET A 213 ? 0.1674 0.1673 0.1421 0.0046  0.0010  -0.0095 215 MET A O   
1786 C CB  . MET A 213 ? 0.1700 0.1830 0.1512 -0.0037 0.0034  -0.0220 215 MET A CB  
1787 C CG  . MET A 213 ? 0.1721 0.1934 0.1574 -0.0077 0.0052  -0.0279 215 MET A CG  
1788 S SD  . MET A 213 ? 0.1995 0.2301 0.1847 -0.0079 0.0053  -0.0258 215 MET A SD  
1789 C CE  . MET A 213 ? 0.2353 0.2795 0.2162 -0.0072 0.0056  -0.0192 215 MET A CE  
1790 N N   . TRP A 214 ? 0.1651 0.1527 0.1411 0.0044  -0.0006 -0.0148 216 TRP A N   
1791 C CA  . TRP A 214 ? 0.1520 0.1331 0.1241 0.0074  -0.0016 -0.0112 216 TRP A CA  
1792 C C   . TRP A 214 ? 0.1576 0.1348 0.1297 0.0089  -0.0023 -0.0098 216 TRP A C   
1793 O O   . TRP A 214 ? 0.1816 0.1583 0.1521 0.0106  -0.0013 -0.0066 216 TRP A O   
1794 C CB  . TRP A 214 ? 0.1638 0.1378 0.1355 0.0085  -0.0027 -0.0120 216 TRP A CB  
1795 C CG  . TRP A 214 ? 0.1714 0.1400 0.1385 0.0112  -0.0036 -0.0092 216 TRP A CG  
1796 C CD1 . TRP A 214 ? 0.1781 0.1416 0.1441 0.0125  -0.0051 -0.0093 216 TRP A CD1 
1797 C CD2 . TRP A 214 ? 0.1693 0.1378 0.1327 0.0125  -0.0028 -0.0065 216 TRP A CD2 
1798 N NE1 . TRP A 214 ? 0.1891 0.1495 0.1509 0.0144  -0.0049 -0.0075 216 TRP A NE1 
1799 C CE2 . TRP A 214 ? 0.1667 0.1297 0.1269 0.0146  -0.0034 -0.0054 216 TRP A CE2 
1800 C CE3 . TRP A 214 ? 0.1838 0.1570 0.1467 0.0118  -0.0013 -0.0053 216 TRP A CE3 
1801 C CZ2 . TRP A 214 ? 0.1781 0.1394 0.1345 0.0163  -0.0024 -0.0030 216 TRP A CZ2 
1802 C CZ3 . TRP A 214 ? 0.1802 0.1517 0.1394 0.0137  -0.0007 -0.0023 216 TRP A CZ3 
1803 C CH2 . TRP A 214 ? 0.2093 0.1746 0.1653 0.0160  -0.0011 -0.0011 216 TRP A CH2 
1804 N N   . SER A 215 ? 0.1646 0.1390 0.1396 0.0084  -0.0035 -0.0124 217 SER A N   
1805 C CA  . SER A 215 ? 0.1615 0.1324 0.1375 0.0094  -0.0040 -0.0119 217 SER A CA  
1806 C C   . SER A 215 ? 0.1577 0.1340 0.1352 0.0095  -0.0019 -0.0090 217 SER A C   
1807 O O   . SER A 215 ? 0.1576 0.1308 0.1356 0.0110  -0.0008 -0.0068 217 SER A O   
1808 C CB  . SER A 215 ? 0.1670 0.1362 0.1467 0.0084  -0.0055 -0.0149 217 SER A CB  
1809 O OG  . SER A 215 ? 0.1965 0.1622 0.1763 0.0087  -0.0070 -0.0161 217 SER A OG  
1810 N N   . LEU A 216 ? 0.1589 0.1443 0.1379 0.0078  -0.0007 -0.0088 218 LEU A N   
1811 C CA  . LEU A 216 ? 0.1573 0.1507 0.1381 0.0081  0.0015  -0.0046 218 LEU A CA  
1812 C C   . LEU A 216 ? 0.1757 0.1704 0.1547 0.0101  0.0032  0.0005  218 LEU A C   
1813 O O   . LEU A 216 ? 0.1891 0.1846 0.1710 0.0120  0.0054  0.0051  218 LEU A O   
1814 C CB  . LEU A 216 ? 0.1795 0.1850 0.1613 0.0054  0.0022  -0.0060 218 LEU A CB  
1815 C CG  . LEU A 216 ? 0.2112 0.2282 0.1952 0.0058  0.0044  -0.0006 218 LEU A CG  
1816 C CD1 . LEU A 216 ? 0.2234 0.2376 0.2118 0.0067  0.0049  0.0003  218 LEU A CD1 
1817 C CD2 . LEU A 216 ? 0.2827 0.3148 0.2661 0.0027  0.0051  -0.0022 218 LEU A CD2 
1818 N N   . GLY A 217 ? 0.1609 0.1556 0.1363 0.0099  0.0027  0.0000  219 GLY A N   
1819 C CA  . GLY A 217 ? 0.1783 0.1737 0.1523 0.0120  0.0044  0.0049  219 GLY A CA  
1820 C C   . GLY A 217 ? 0.1900 0.1746 0.1644 0.0145  0.0052  0.0058  219 GLY A C   
1821 O O   . GLY A 217 ? 0.1974 0.1825 0.1741 0.0165  0.0082  0.0107  219 GLY A O   
1822 N N   . CYS A 218 ? 0.1660 0.1416 0.1390 0.0142  0.0030  0.0010  220 CYS A N   
1823 C CA  . CYS A 218 ? 0.1715 0.1385 0.1450 0.0156  0.0038  0.0002  220 CYS A CA  
1824 C C   . CYS A 218 ? 0.2176 0.1847 0.1973 0.0161  0.0065  0.0022  220 CYS A C   
1825 O O   . CYS A 218 ? 0.1984 0.1615 0.1811 0.0176  0.0097  0.0040  220 CYS A O   
1826 C CB  . CYS A 218 ? 0.1644 0.1252 0.1355 0.0147  0.0006  -0.0050 220 CYS A CB  
1827 S SG  . CYS A 218 ? 0.1969 0.1564 0.1623 0.0149  -0.0016 -0.0061 220 CYS A SG  
1828 N N   . MET A 219 ? 0.1780 0.1494 0.1607 0.0149  0.0057  0.0017  221 MET A N   
1829 C CA  . MET A 219 ? 0.2169 0.1894 0.2065 0.0156  0.0086  0.0044  221 MET A CA  
1830 C C   . MET A 219 ? 0.1837 0.1629 0.1769 0.0176  0.0127  0.0120  221 MET A C   
1831 O O   . MET A 219 ? 0.1990 0.1748 0.1984 0.0193  0.0167  0.0153  221 MET A O   
1832 C CB  . MET A 219 ? 0.2430 0.2203 0.2346 0.0139  0.0070  0.0030  221 MET A CB  
1833 C CG  . MET A 219 ? 0.2246 0.1956 0.2148 0.0123  0.0036  -0.0033 221 MET A CG  
1834 S SD  . MET A 219 ? 0.2682 0.2442 0.2625 0.0107  0.0027  -0.0047 221 MET A SD  
1835 C CE  . MET A 219 ? 0.2213 0.2005 0.2231 0.0122  0.0071  0.0011  221 MET A CE  
1836 N N   . LEU A 220 ? 0.1815 0.1709 0.1718 0.0172  0.0122  0.0151  222 LEU A N   
1837 C CA  . LEU A 220 ? 0.1934 0.1924 0.1872 0.0192  0.0158  0.0235  222 LEU A CA  
1838 C C   . LEU A 220 ? 0.1875 0.1796 0.1829 0.0217  0.0189  0.0264  222 LEU A C   
1839 O O   . LEU A 220 ? 0.2157 0.2091 0.2186 0.0242  0.0237  0.0330  222 LEU A O   
1840 C CB  . LEU A 220 ? 0.2244 0.2367 0.2139 0.0176  0.0141  0.0247  222 LEU A CB  
1841 C CG  . LEU A 220 ? 0.2139 0.2396 0.2064 0.0194  0.0173  0.0340  222 LEU A CG  
1842 C CD1 . LEU A 220 ? 0.2212 0.2560 0.2209 0.0205  0.0201  0.0402  222 LEU A CD1 
1843 C CD2 . LEU A 220 ? 0.2479 0.2863 0.2351 0.0169  0.0151  0.0330  222 LEU A CD2 
1844 N N   . ALA A 221 ? 0.1731 0.1579 0.1623 0.0212  0.0168  0.0218  223 ALA A N   
1845 C CA  . ALA A 221 ? 0.1869 0.1652 0.1770 0.0234  0.0199  0.0237  223 ALA A CA  
1846 C C   . ALA A 221 ? 0.2040 0.1731 0.2011 0.0244  0.0238  0.0226  223 ALA A C   
1847 O O   . ALA A 221 ? 0.2019 0.1695 0.2055 0.0267  0.0291  0.0276  223 ALA A O   
1848 C CB  . ALA A 221 ? 0.2131 0.1853 0.1951 0.0224  0.0167  0.0182  223 ALA A CB  
1849 N N   . SER A 222 ? 0.2174 0.1806 0.2142 0.0225  0.0215  0.0161  224 SER A N   
1850 C CA  A SER A 222 ? 0.2473 0.2021 0.2512 0.0226  0.0252  0.0136  224 SER A CA  
1851 C CA  B SER A 222 ? 0.2341 0.1890 0.2381 0.0226  0.0252  0.0136  224 SER A CA  
1852 C C   . SER A 222 ? 0.2309 0.1899 0.2460 0.0245  0.0306  0.0209  224 SER A C   
1853 O O   . SER A 222 ? 0.2505 0.2034 0.2744 0.0257  0.0364  0.0220  224 SER A O   
1854 C CB  A SER A 222 ? 0.2094 0.1594 0.2108 0.0199  0.0211  0.0053  224 SER A CB  
1855 C CB  B SER A 222 ? 0.2366 0.1868 0.2381 0.0199  0.0211  0.0055  224 SER A CB  
1856 O OG  A SER A 222 ? 0.2243 0.1796 0.2276 0.0190  0.0192  0.0064  224 SER A OG  
1857 O OG  B SER A 222 ? 0.3023 0.2483 0.2954 0.0186  0.0174  -0.0006 224 SER A OG  
1858 N N   . MET A 223 ? 0.2191 0.1889 0.2348 0.0247  0.0293  0.0261  225 MET A N   
1859 C CA  . MET A 223 ? 0.2453 0.2211 0.2720 0.0267  0.0343  0.0342  225 MET A CA  
1860 C C   . MET A 223 ? 0.2355 0.2175 0.2677 0.0301  0.0395  0.0443  225 MET A C   
1861 O O   . MET A 223 ? 0.2677 0.2469 0.3117 0.0326  0.0463  0.0497  225 MET A O   
1862 C CB  . MET A 223 ? 0.2762 0.2631 0.3014 0.0256  0.0312  0.0360  225 MET A CB  
1863 C CG  . MET A 223 ? 0.3167 0.2974 0.3386 0.0227  0.0269  0.0271  225 MET A CG  
1864 S SD  . MET A 223 ? 0.5434 0.5363 0.5631 0.0209  0.0234  0.0276  225 MET A SD  
1865 C CE  . MET A 223 ? 0.5921 0.5976 0.6033 0.0202  0.0208  0.0298  225 MET A CE  
1866 N N   . ILE A 224 ? 0.2303 0.2209 0.2553 0.0303  0.0370  0.0472  226 ILE A N   
1867 C CA  . ILE A 224 ? 0.2356 0.2346 0.2666 0.0336  0.0418  0.0581  226 ILE A CA  
1868 C C   . ILE A 224 ? 0.2217 0.2091 0.2563 0.0354  0.0464  0.0575  226 ILE A C   
1869 O O   . ILE A 224 ? 0.2355 0.2255 0.2804 0.0389  0.0530  0.0667  226 ILE A O   
1870 C CB  . ILE A 224 ? 0.2166 0.2308 0.2399 0.0330  0.0381  0.0617  226 ILE A CB  
1871 C CG1 . ILE A 224 ? 0.2156 0.2234 0.2281 0.0311  0.0338  0.0541  226 ILE A CG1 
1872 C CG2 . ILE A 224 ? 0.2828 0.3098 0.3033 0.0307  0.0344  0.0614  226 ILE A CG2 
1873 C CD1 . ILE A 224 ? 0.2601 0.2824 0.2664 0.0301  0.0308  0.0570  226 ILE A CD1 
1874 N N   . PHE A 225 ? 0.2176 0.1925 0.2448 0.0333  0.0436  0.0472  227 PHE A N   
1875 C CA  . PHE A 225 ? 0.2146 0.1791 0.2446 0.0346  0.0481  0.0455  227 PHE A CA  
1876 C C   . PHE A 225 ? 0.2336 0.1856 0.2719 0.0339  0.0526  0.0396  227 PHE A C   
1877 O O   . PHE A 225 ? 0.2753 0.2186 0.3179 0.0347  0.0578  0.0376  227 PHE A O   
1878 C CB  . PHE A 225 ? 0.2201 0.1803 0.2374 0.0328  0.0430  0.0383  227 PHE A CB  
1879 C CG  . PHE A 225 ? 0.2118 0.1830 0.2225 0.0334  0.0399  0.0435  227 PHE A CG  
1880 C CD1 . PHE A 225 ? 0.1991 0.1796 0.2159 0.0364  0.0441  0.0543  227 PHE A CD1 
1881 C CD2 . PHE A 225 ? 0.2133 0.1859 0.2127 0.0309  0.0331  0.0377  227 PHE A CD2 
1882 C CE1 . PHE A 225 ? 0.2303 0.2223 0.2412 0.0364  0.0411  0.0585  227 PHE A CE1 
1883 C CE2 . PHE A 225 ? 0.2173 0.2001 0.2116 0.0308  0.0307  0.0414  227 PHE A CE2 
1884 C CZ  . PHE A 225 ? 0.2251 0.2180 0.2249 0.0333  0.0345  0.0515  227 PHE A CZ  
1885 N N   . ARG A 226 ? 0.2696 0.1912 0.2949 0.0162  -0.0305 0.0167  228 ARG A N   
1886 C CA  . ARG A 226 ? 0.3144 0.2247 0.3425 0.0141  -0.0321 0.0140  228 ARG A CA  
1887 C C   . ARG A 226 ? 0.3499 0.2533 0.3695 0.0115  -0.0346 0.0068  228 ARG A C   
1888 O O   . ARG A 226 ? 0.3574 0.2516 0.3754 0.0120  -0.0338 0.0027  228 ARG A O   
1889 C CB  . ARG A 226 ? 0.3647 0.2691 0.3987 0.0177  -0.0280 0.0160  228 ARG A CB  
1890 C CG  . ARG A 226 ? 0.4328 0.3451 0.4747 0.0212  -0.0250 0.0237  228 ARG A CG  
1891 C CD  . ARG A 226 ? 0.5920 0.5064 0.6403 0.0185  -0.0274 0.0273  228 ARG A CD  
1892 N NE  . ARG A 226 ? 0.8016 0.7052 0.8533 0.0146  -0.0296 0.0242  228 ARG A NE  
1893 C CZ  . ARG A 226 ? 0.9210 0.8155 0.9793 0.0155  -0.0271 0.0248  228 ARG A CZ  
1894 N NH1 . ARG A 226 ? 0.9398 0.8252 1.0011 0.0109  -0.0297 0.0212  228 ARG A NH1 
1895 N NH2 . ARG A 226 ? 0.9629 0.8576 1.0250 0.0208  -0.0219 0.0290  228 ARG A NH2 
1896 N N   . LYS A 227 ? 0.2905 0.1987 0.3045 0.0091  -0.0375 0.0053  229 LYS A N   
1897 C CA  . LYS A 227 ? 0.3165 0.2202 0.3221 0.0070  -0.0401 -0.0007 229 LYS A CA  
1898 C C   . LYS A 227 ? 0.2979 0.2058 0.3027 0.0034  -0.0439 0.0000  229 LYS A C   
1899 O O   . LYS A 227 ? 0.2979 0.2131 0.3001 0.0036  -0.0434 0.0022  229 LYS A O   
1900 C CB  . LYS A 227 ? 0.3318 0.2377 0.3293 0.0096  -0.0377 -0.0029 229 LYS A CB  
1901 C CG  . LYS A 227 ? 0.3387 0.2403 0.3272 0.0080  -0.0400 -0.0087 229 LYS A CG  
1902 C CD  . LYS A 227 ? 0.3850 0.2894 0.3659 0.0107  -0.0374 -0.0102 229 LYS A CD  
1903 C CE  . LYS A 227 ? 0.4082 0.3077 0.3799 0.0099  -0.0394 -0.0159 229 LYS A CE  
1904 N NZ  . LYS A 227 ? 0.3881 0.2902 0.3575 0.0066  -0.0433 -0.0162 229 LYS A NZ  
1905 N N   . GLU A 228 ? 0.3508 0.2542 0.3579 0.0001  -0.0475 -0.0018 230 GLU A N   
1906 C CA  . GLU A 228 ? 0.3286 0.2366 0.3366 -0.0029 -0.0509 0.0000  230 GLU A CA  
1907 C C   . GLU A 228 ? 0.3314 0.2365 0.3330 -0.0055 -0.0548 -0.0053 230 GLU A C   
1908 O O   . GLU A 228 ? 0.3811 0.2796 0.3840 -0.0074 -0.0568 -0.0094 230 GLU A O   
1909 C CB  . GLU A 228 ? 0.4138 0.3222 0.4323 -0.0046 -0.0519 0.0043  230 GLU A CB  
1910 C CG  . GLU A 228 ? 0.4338 0.3497 0.4545 -0.0059 -0.0534 0.0089  230 GLU A CG  
1911 C CD  . GLU A 228 ? 0.4919 0.4085 0.5087 -0.0089 -0.0576 0.0066  230 GLU A CD  
1912 O OE1 . GLU A 228 ? 0.4873 0.3990 0.5040 -0.0114 -0.0606 0.0024  230 GLU A OE1 
1913 O OE2 . GLU A 228 ? 0.3739 0.2963 0.3877 -0.0088 -0.0577 0.0091  230 GLU A OE2 
1914 N N   . PRO A 229 ? 0.3083 0.2180 0.3030 -0.0057 -0.0558 -0.0054 231 PRO A N   
1915 C CA  . PRO A 229 ? 0.2525 0.1687 0.2450 -0.0038 -0.0530 -0.0018 231 PRO A CA  
1916 C C   . PRO A 229 ? 0.2944 0.2102 0.2817 -0.0008 -0.0492 -0.0035 231 PRO A C   
1917 O O   . PRO A 229 ? 0.3060 0.2163 0.2895 0.0003  -0.0489 -0.0078 231 PRO A O   
1918 C CB  . PRO A 229 ? 0.2799 0.1992 0.2668 -0.0052 -0.0553 -0.0021 231 PRO A CB  
1919 C CG  . PRO A 229 ? 0.3607 0.2754 0.3423 -0.0061 -0.0581 -0.0077 231 PRO A CG  
1920 C CD  . PRO A 229 ? 0.3702 0.2792 0.3586 -0.0076 -0.0595 -0.0095 231 PRO A CD  
1921 N N   . PHE A 230 ? 0.2218 0.1435 0.2090 0.0005  -0.0463 -0.0003 232 PHE A N   
1922 C CA  . PHE A 230 ? 0.2124 0.1352 0.1959 0.0032  -0.0427 -0.0015 232 PHE A CA  
1923 C C   . PHE A 230 ? 0.2623 0.1842 0.2366 0.0036  -0.0424 -0.0048 232 PHE A C   
1924 O O   . PHE A 230 ? 0.2764 0.1947 0.2463 0.0055  -0.0412 -0.0081 232 PHE A O   
1925 C CB  . PHE A 230 ? 0.2181 0.1485 0.2048 0.0039  -0.0398 0.0025  232 PHE A CB  
1926 C CG  . PHE A 230 ? 0.2239 0.1570 0.2087 0.0065  -0.0362 0.0019  232 PHE A CG  
1927 C CD1 . PHE A 230 ? 0.2241 0.1553 0.2121 0.0091  -0.0347 0.0020  232 PHE A CD1 
1928 C CD2 . PHE A 230 ? 0.2325 0.1701 0.2127 0.0064  -0.0341 0.0014  232 PHE A CD2 
1929 C CE1 . PHE A 230 ? 0.2334 0.1681 0.2199 0.0119  -0.0312 0.0019  232 PHE A CE1 
1930 C CE2 . PHE A 230 ? 0.2859 0.2271 0.2650 0.0086  -0.0308 0.0011  232 PHE A CE2 
1931 C CZ  . PHE A 230 ? 0.2782 0.2184 0.2605 0.0115  -0.0295 0.0014  232 PHE A CZ  
1932 N N   . PHE A 231 ? 0.2247 0.1497 0.1958 0.0022  -0.0430 -0.0037 233 PHE A N   
1933 C CA  . PHE A 231 ? 0.2249 0.1495 0.1875 0.0029  -0.0425 -0.0059 233 PHE A CA  
1934 C C   . PHE A 231 ? 0.2678 0.1893 0.2277 0.0015  -0.0468 -0.0081 233 PHE A C   
1935 O O   . PHE A 231 ? 0.2545 0.1784 0.2162 -0.0002 -0.0488 -0.0057 233 PHE A O   
1936 C CB  . PHE A 231 ? 0.2257 0.1552 0.1869 0.0023  -0.0401 -0.0031 233 PHE A CB  
1937 C CG  . PHE A 231 ? 0.1958 0.1296 0.1596 0.0029  -0.0362 -0.0015 233 PHE A CG  
1938 C CD1 . PHE A 231 ? 0.2322 0.1666 0.1931 0.0048  -0.0333 -0.0032 233 PHE A CD1 
1939 C CD2 . PHE A 231 ? 0.2245 0.1627 0.1934 0.0014  -0.0353 0.0017  233 PHE A CD2 
1940 C CE1 . PHE A 231 ? 0.2176 0.1577 0.1815 0.0049  -0.0299 -0.0018 233 PHE A CE1 
1941 C CE2 . PHE A 231 ? 0.1996 0.1430 0.1707 0.0014  -0.0321 0.0026  233 PHE A CE2 
1942 C CZ  . PHE A 231 ? 0.2539 0.1987 0.2227 0.0030  -0.0295 0.0008  233 PHE A CZ  
1943 N N   . HIS A 232 ? 0.2650 0.1817 0.2205 0.0024  -0.0481 -0.0126 234 HIS A N   
1944 C CA  . HIS A 232 ? 0.2744 0.1884 0.2287 0.0006  -0.0528 -0.0157 234 HIS A CA  
1945 C C   . HIS A 232 ? 0.2946 0.2094 0.2389 0.0018  -0.0536 -0.0183 234 HIS A C   
1946 O O   . HIS A 232 ? 0.3387 0.2498 0.2772 0.0030  -0.0543 -0.0232 234 HIS A O   
1947 C CB  . HIS A 232 ? 0.3212 0.2285 0.2784 0.0003  -0.0537 -0.0195 234 HIS A CB  
1948 C CG  . HIS A 232 ? 0.3740 0.2789 0.3337 -0.0030 -0.0587 -0.0222 234 HIS A CG  
1949 N ND1 . HIS A 232 ? 0.4248 0.3236 0.3906 -0.0045 -0.0596 -0.0243 234 HIS A ND1 
1950 C CD2 . HIS A 232 ? 0.4606 0.3686 0.4180 -0.0051 -0.0629 -0.0229 234 HIS A CD2 
1951 C CE1 . HIS A 232 ? 0.4525 0.3508 0.4201 -0.0079 -0.0643 -0.0267 234 HIS A CE1 
1952 N NE2 . HIS A 232 ? 0.4453 0.3498 0.4077 -0.0083 -0.0666 -0.0258 234 HIS A NE2 
1953 N N   . GLY A 233 ? 0.2600 0.1800 0.2023 0.0019  -0.0531 -0.0147 235 GLY A N   
1954 C CA  . GLY A 233 ? 0.2664 0.1884 0.1995 0.0037  -0.0532 -0.0159 235 GLY A CA  
1955 C C   . GLY A 233 ? 0.2806 0.2037 0.2111 0.0023  -0.0587 -0.0185 235 GLY A C   
1956 O O   . GLY A 233 ? 0.3073 0.2317 0.2440 -0.0006 -0.0622 -0.0174 235 GLY A O   
1957 N N   . HIS A 234 ? 0.3387 0.2622 0.2597 0.0044  -0.0592 -0.0219 236 HIS A N   
1958 C CA  . HIS A 234 ? 0.3344 0.2606 0.2513 0.0034  -0.0645 -0.0248 236 HIS A CA  
1959 C C   . HIS A 234 ? 0.3320 0.2660 0.2479 0.0039  -0.0653 -0.0196 236 HIS A C   
1960 O O   . HIS A 234 ? 0.3793 0.3177 0.2948 0.0024  -0.0703 -0.0205 236 HIS A O   
1961 C CB  . HIS A 234 ? 0.4175 0.3421 0.3238 0.0060  -0.0648 -0.0305 236 HIS A CB  
1962 C CG  . HIS A 234 ? 0.7032 0.6198 0.6093 0.0063  -0.0633 -0.0356 236 HIS A CG  
1963 N ND1 . HIS A 234 ? 0.7903 0.7043 0.6891 0.0102  -0.0593 -0.0375 236 HIS A ND1 
1964 C CD2 . HIS A 234 ? 0.7965 0.7070 0.7090 0.0036  -0.0649 -0.0389 236 HIS A CD2 
1965 C CE1 . HIS A 234 ? 0.8257 0.7324 0.7261 0.0100  -0.0584 -0.0417 236 HIS A CE1 
1966 N NE2 . HIS A 234 ? 0.7779 0.6820 0.6867 0.0060  -0.0616 -0.0426 236 HIS A NE2 
1967 N N   . ASP A 235 ? 0.2738 0.2095 0.1891 0.0062  -0.0604 -0.0143 237 ASP A N   
1968 C CA  . ASP A 235 ? 0.2746 0.2164 0.1892 0.0074  -0.0596 -0.0085 237 ASP A CA  
1969 C C   . ASP A 235 ? 0.2718 0.2121 0.1895 0.0082  -0.0533 -0.0037 237 ASP A C   
1970 O O   . ASP A 235 ? 0.2671 0.2030 0.1877 0.0076  -0.0508 -0.0052 237 ASP A O   
1971 C CB  . ASP A 235 ? 0.2926 0.2392 0.1971 0.0107  -0.0602 -0.0089 237 ASP A CB  
1972 C CG  . ASP A 235 ? 0.4107 0.3546 0.3075 0.0143  -0.0556 -0.0106 237 ASP A CG  
1973 O OD1 . ASP A 235 ? 0.3382 0.2789 0.2373 0.0149  -0.0502 -0.0082 237 ASP A OD1 
1974 O OD2 . ASP A 235 ? 0.4730 0.4187 0.3611 0.0166  -0.0573 -0.0141 237 ASP A OD2 
1975 N N   . ASN A 236 ? 0.2846 0.2285 0.2016 0.0098  -0.0507 0.0018  238 ASN A N   
1976 C CA  . ASN A 236 ? 0.2777 0.2197 0.1983 0.0098  -0.0449 0.0058  238 ASN A CA  
1977 C C   . ASN A 236 ? 0.2723 0.2118 0.1882 0.0119  -0.0396 0.0048  238 ASN A C   
1978 O O   . ASN A 236 ? 0.2892 0.2266 0.2091 0.0108  -0.0355 0.0058  238 ASN A O   
1979 C CB  . ASN A 236 ? 0.3043 0.2497 0.2257 0.0108  -0.0429 0.0120  238 ASN A CB  
1980 C CG  . ASN A 236 ? 0.3193 0.2672 0.2476 0.0085  -0.0470 0.0140  238 ASN A CG  
1981 O OD1 . ASN A 236 ? 0.3346 0.2808 0.2685 0.0056  -0.0503 0.0114  238 ASN A OD1 
1982 N ND2 . ASN A 236 ? 0.3803 0.3325 0.3083 0.0101  -0.0466 0.0192  238 ASN A ND2 
1983 N N   . TYR A 237 ? 0.2716 0.2122 0.1795 0.0148  -0.0396 0.0029  239 TYR A N   
1984 C CA  . TYR A 237 ? 0.2652 0.2038 0.1689 0.0169  -0.0345 0.0021  239 TYR A CA  
1985 C C   . TYR A 237 ? 0.2647 0.1996 0.1703 0.0157  -0.0353 -0.0028 239 TYR A C   
1986 O O   . TYR A 237 ? 0.2415 0.1748 0.1501 0.0153  -0.0311 -0.0024 239 TYR A O   
1987 C CB  . TYR A 237 ? 0.3004 0.2418 0.1944 0.0211  -0.0340 0.0022  239 TYR A CB  
1988 C CG  . TYR A 237 ? 0.3788 0.3247 0.2714 0.0227  -0.0338 0.0076  239 TYR A CG  
1989 C CD1 . TYR A 237 ? 0.3852 0.3360 0.2746 0.0234  -0.0394 0.0069  239 TYR A CD1 
1990 C CD2 . TYR A 237 ? 0.4467 0.3922 0.3420 0.0233  -0.0278 0.0133  239 TYR A CD2 
1991 C CE1 . TYR A 237 ? 0.4611 0.4172 0.3497 0.0254  -0.0390 0.0126  239 TYR A CE1 
1992 C CE2 . TYR A 237 ? 0.5218 0.4709 0.4162 0.0253  -0.0269 0.0188  239 TYR A CE2 
1993 C CZ  . TYR A 237 ? 0.4996 0.4545 0.3907 0.0265  -0.0325 0.0188  239 TYR A CZ  
1994 O OH  . TYR A 237 ? 0.5347 0.4943 0.4250 0.0291  -0.0313 0.0250  239 TYR A OH  
1995 N N   . ASP A 238 ? 0.2632 0.1968 0.1676 0.0151  -0.0405 -0.0074 240 ASP A N   
1996 C CA  . ASP A 238 ? 0.2463 0.1757 0.1530 0.0143  -0.0409 -0.0117 240 ASP A CA  
1997 C C   . ASP A 238 ? 0.2297 0.1581 0.1462 0.0113  -0.0401 -0.0099 240 ASP A C   
1998 O O   . ASP A 238 ? 0.2393 0.1657 0.1583 0.0114  -0.0379 -0.0112 240 ASP A O   
1999 C CB  . ASP A 238 ? 0.2687 0.1961 0.1729 0.0136  -0.0465 -0.0171 240 ASP A CB  
2000 C CG  . ASP A 238 ? 0.3165 0.2383 0.2223 0.0135  -0.0462 -0.0215 240 ASP A CG  
2001 O OD1 . ASP A 238 ? 0.3307 0.2512 0.2323 0.0163  -0.0423 -0.0226 240 ASP A OD1 
2002 O OD2 . ASP A 238 ? 0.3090 0.2281 0.2209 0.0108  -0.0494 -0.0234 240 ASP A OD2 
2003 N N   . GLN A 239 ? 0.2393 0.1697 0.1611 0.0091  -0.0416 -0.0065 241 GLN A N   
2004 C CA  . GLN A 239 ? 0.2341 0.1643 0.1645 0.0067  -0.0406 -0.0045 241 GLN A CA  
2005 C C   . GLN A 239 ? 0.2071 0.1381 0.1383 0.0072  -0.0349 -0.0029 241 GLN A C   
2006 O O   . GLN A 239 ? 0.2115 0.1424 0.1475 0.0064  -0.0336 -0.0035 241 GLN A O   
2007 C CB  . GLN A 239 ? 0.1913 0.1239 0.1261 0.0049  -0.0424 -0.0007 241 GLN A CB  
2008 C CG  . GLN A 239 ? 0.2048 0.1376 0.1482 0.0027  -0.0420 0.0013  241 GLN A CG  
2009 C CD  . GLN A 239 ? 0.1945 0.1251 0.1427 0.0014  -0.0452 -0.0013 241 GLN A CD  
2010 O OE1 . GLN A 239 ? 0.2344 0.1632 0.1810 0.0012  -0.0490 -0.0044 241 GLN A OE1 
2011 N NE2 . GLN A 239 ? 0.2025 0.1335 0.1569 0.0006  -0.0436 -0.0001 241 GLN A NE2 
2012 N N   . LEU A 240 ? 0.2114 0.1438 0.1384 0.0086  -0.0312 -0.0006 242 LEU A N   
2013 C CA  . LEU A 240 ? 0.1855 0.1188 0.1138 0.0084  -0.0256 0.0006  242 LEU A CA  
2014 C C   . LEU A 240 ? 0.2183 0.1511 0.1442 0.0101  -0.0240 -0.0024 242 LEU A C   
2015 O O   . LEU A 240 ? 0.2150 0.1493 0.1449 0.0092  -0.0213 -0.0025 242 LEU A O   
2016 C CB  . LEU A 240 ? 0.2112 0.1452 0.1360 0.0094  -0.0214 0.0040  242 LEU A CB  
2017 C CG  . LEU A 240 ? 0.2166 0.1511 0.1435 0.0084  -0.0153 0.0052  242 LEU A CG  
2018 C CD1 . LEU A 240 ? 0.2224 0.1581 0.1571 0.0048  -0.0150 0.0054  242 LEU A CD1 
2019 C CD2 . LEU A 240 ? 0.2369 0.1709 0.1605 0.0097  -0.0106 0.0087  242 LEU A CD2 
2020 N N   . VAL A 241 ? 0.2172 0.1483 0.1364 0.0128  -0.0258 -0.0049 243 VAL A N   
2021 C CA  . VAL A 241 ? 0.2205 0.1505 0.1371 0.0149  -0.0242 -0.0078 243 VAL A CA  
2022 C C   . VAL A 241 ? 0.2269 0.1559 0.1497 0.0137  -0.0259 -0.0097 243 VAL A C   
2023 O O   . VAL A 241 ? 0.2313 0.1617 0.1562 0.0144  -0.0228 -0.0099 243 VAL A O   
2024 C CB  . VAL A 241 ? 0.2616 0.1897 0.1693 0.0181  -0.0260 -0.0108 243 VAL A CB  
2025 C CG1 . VAL A 241 ? 0.2779 0.2043 0.1828 0.0207  -0.0240 -0.0138 243 VAL A CG1 
2026 C CG2 . VAL A 241 ? 0.2660 0.1963 0.1674 0.0202  -0.0235 -0.0080 243 VAL A CG2 
2027 N N   . ARG A 242 ? 0.2264 0.1534 0.1525 0.0120  -0.0304 -0.0106 244 ARG A N   
2028 C CA  . ARG A 242 ? 0.2241 0.1499 0.1565 0.0111  -0.0316 -0.0116 244 ARG A CA  
2029 C C   . ARG A 242 ? 0.1991 0.1294 0.1384 0.0097  -0.0286 -0.0085 244 ARG A C   
2030 O O   . ARG A 242 ? 0.2353 0.1669 0.1782 0.0105  -0.0271 -0.0088 244 ARG A O   
2031 C CB  . ARG A 242 ? 0.2557 0.1790 0.1918 0.0091  -0.0365 -0.0123 244 ARG A CB  
2032 C CG  . ARG A 242 ? 0.3538 0.2736 0.2842 0.0095  -0.0404 -0.0159 244 ARG A CG  
2033 C CD  . ARG A 242 ? 0.3830 0.2983 0.3091 0.0119  -0.0398 -0.0204 244 ARG A CD  
2034 N NE  . ARG A 242 ? 0.4589 0.3705 0.3798 0.0118  -0.0439 -0.0250 244 ARG A NE  
2035 C CZ  . ARG A 242 ? 0.5917 0.4979 0.5148 0.0108  -0.0464 -0.0288 244 ARG A CZ  
2036 N NH1 . ARG A 242 ? 0.5888 0.4924 0.5192 0.0105  -0.0449 -0.0279 244 ARG A NH1 
2037 N NH2 . ARG A 242 ? 0.6168 0.5202 0.5348 0.0101  -0.0503 -0.0337 244 ARG A NH2 
2038 N N   . ILE A 243 ? 0.1983 0.1314 0.1395 0.0076  -0.0278 -0.0057 245 ILE A N   
2039 C CA  . ILE A 243 ? 0.2114 0.1491 0.1583 0.0058  -0.0250 -0.0035 245 ILE A CA  
2040 C C   . ILE A 243 ? 0.2071 0.1478 0.1525 0.0068  -0.0205 -0.0039 245 ILE A C   
2041 O O   . ILE A 243 ? 0.2145 0.1596 0.1646 0.0064  -0.0189 -0.0036 245 ILE A O   
2042 C CB  . ILE A 243 ? 0.1873 0.1260 0.1354 0.0035  -0.0245 -0.0009 245 ILE A CB  
2043 C CG1 . ILE A 243 ? 0.1942 0.1313 0.1453 0.0025  -0.0288 0.0001  245 ILE A CG1 
2044 C CG2 . ILE A 243 ? 0.2042 0.1477 0.1571 0.0014  -0.0211 0.0003  245 ILE A CG2 
2045 C CD1 . ILE A 243 ? 0.2025 0.1398 0.1536 0.0011  -0.0285 0.0030  245 ILE A CD1 
2046 N N   . ALA A 244 ? 0.1928 0.1320 0.1319 0.0083  -0.0184 -0.0042 246 ALA A N   
2047 C CA  . ALA A 244 ? 0.1990 0.1415 0.1373 0.0092  -0.0137 -0.0041 246 ALA A CA  
2048 C C   . ALA A 244 ? 0.2224 0.1655 0.1605 0.0119  -0.0134 -0.0059 246 ALA A C   
2049 O O   . ALA A 244 ? 0.2280 0.1760 0.1685 0.0121  -0.0098 -0.0053 246 ALA A O   
2050 C CB  . ALA A 244 ? 0.1991 0.1397 0.1306 0.0108  -0.0112 -0.0034 246 ALA A CB  
2051 N N   . LYS A 245 ? 0.2009 0.1394 0.1368 0.0139  -0.0167 -0.0081 247 LYS A N   
2052 C CA  . LYS A 245 ? 0.2125 0.1509 0.1488 0.0167  -0.0158 -0.0095 247 LYS A CA  
2053 C C   . LYS A 245 ? 0.2276 0.1708 0.1722 0.0157  -0.0155 -0.0080 247 LYS A C   
2054 O O   . LYS A 245 ? 0.2636 0.2088 0.2097 0.0183  -0.0136 -0.0080 247 LYS A O   
2055 C CB  . LYS A 245 ? 0.2371 0.1682 0.1689 0.0188  -0.0191 -0.0128 247 LYS A CB  
2056 C CG  . LYS A 245 ? 0.2576 0.1854 0.1800 0.0210  -0.0189 -0.0148 247 LYS A CG  
2057 C CD  . LYS A 245 ? 0.3195 0.2404 0.2375 0.0224  -0.0225 -0.0190 247 LYS A CD  
2058 C CE  . LYS A 245 ? 0.4116 0.3304 0.3194 0.0249  -0.0225 -0.0214 247 LYS A CE  
2059 N NZ  . LYS A 245 ? 0.5978 0.5101 0.5011 0.0255  -0.0265 -0.0264 247 LYS A NZ  
2060 N N   . VAL A 246 ? 0.1969 0.1427 0.1468 0.0125  -0.0171 -0.0062 248 VAL A N   
2061 C CA  . VAL A 246 ? 0.2141 0.1658 0.1715 0.0117  -0.0169 -0.0044 248 VAL A CA  
2062 C C   . VAL A 246 ? 0.2040 0.1639 0.1647 0.0090  -0.0141 -0.0030 248 VAL A C   
2063 O O   . VAL A 246 ? 0.2156 0.1828 0.1801 0.0096  -0.0120 -0.0021 248 VAL A O   
2064 C CB  . VAL A 246 ? 0.1861 0.1353 0.1474 0.0103  -0.0207 -0.0036 248 VAL A CB  
2065 C CG1 . VAL A 246 ? 0.2004 0.1567 0.1691 0.0100  -0.0202 -0.0013 248 VAL A CG1 
2066 C CG2 . VAL A 246 ? 0.2315 0.1727 0.1906 0.0123  -0.0233 -0.0056 248 VAL A CG2 
2067 N N   . LEU A 247 ? 0.1800 0.1389 0.1394 0.0061  -0.0140 -0.0027 249 LEU A N   
2068 C CA  A LEU A 247 ? 0.1734 0.1386 0.1358 0.0028  -0.0111 -0.0020 249 LEU A CA  
2069 C CA  B LEU A 247 ? 0.1756 0.1407 0.1379 0.0028  -0.0111 -0.0020 249 LEU A CA  
2070 C C   . LEU A 247 ? 0.2059 0.1727 0.1656 0.0030  -0.0069 -0.0024 249 LEU A C   
2071 O O   . LEU A 247 ? 0.2022 0.1752 0.1654 0.0001  -0.0041 -0.0023 249 LEU A O   
2072 C CB  A LEU A 247 ? 0.1804 0.1431 0.1429 -0.0003 -0.0119 -0.0014 249 LEU A CB  
2073 C CB  B LEU A 247 ? 0.1831 0.1455 0.1454 -0.0002 -0.0119 -0.0014 249 LEU A CB  
2074 C CG  A LEU A 247 ? 0.1683 0.1332 0.1357 -0.0018 -0.0145 -0.0004 249 LEU A CG  
2075 C CG  B LEU A 247 ? 0.1824 0.1441 0.1480 -0.0009 -0.0155 -0.0004 249 LEU A CG  
2076 C CD1 A LEU A 247 ? 0.1832 0.1438 0.1509 0.0007  -0.0185 0.0001  249 LEU A CD1 
2077 C CD1 B LEU A 247 ? 0.1793 0.1388 0.1446 -0.0036 -0.0152 0.0005  249 LEU A CD1 
2078 C CD2 A LEU A 247 ? 0.1849 0.1478 0.1521 -0.0048 -0.0139 0.0002  249 LEU A CD2 
2079 C CD2 B LEU A 247 ? 0.1639 0.1337 0.1356 -0.0012 -0.0156 0.0001  249 LEU A CD2 
2080 N N   . GLY A 248 ? 0.1845 0.1463 0.1383 0.0061  -0.0064 -0.0030 250 GLY A N   
2081 C CA  . GLY A 248 ? 0.1965 0.1598 0.1476 0.0071  -0.0022 -0.0029 250 GLY A CA  
2082 C C   . GLY A 248 ? 0.2092 0.1689 0.1568 0.0056  0.0001  -0.0021 250 GLY A C   
2083 O O   . GLY A 248 ? 0.2253 0.1834 0.1744 0.0027  -0.0005 -0.0015 250 GLY A O   
2084 N N   . THR A 249 ? 0.2103 0.1688 0.1533 0.0080  0.0033  -0.0017 251 THR A N   
2085 C CA  . THR A 249 ? 0.2295 0.1845 0.1689 0.0075  0.0061  -0.0002 251 THR A CA  
2086 C C   . THR A 249 ? 0.1990 0.1579 0.1436 0.0034  0.0111  0.0009  251 THR A C   
2087 O O   . THR A 249 ? 0.2282 0.1837 0.1720 0.0017  0.0133  0.0024  251 THR A O   
2088 C CB  . THR A 249 ? 0.2297 0.1818 0.1615 0.0122  0.0077  0.0002  251 THR A CB  
2089 O OG1 . THR A 249 ? 0.2337 0.1901 0.1664 0.0142  0.0101  -0.0002 251 THR A OG1 
2090 C CG2 . THR A 249 ? 0.2628 0.2096 0.1885 0.0152  0.0027  -0.0014 251 THR A CG2 
2091 N N   . GLU A 250 ? 0.2248 0.1910 0.1749 0.0017  0.0131  0.0004  252 GLU A N   
2092 C CA  . GLU A 250 ? 0.2408 0.2108 0.1961 -0.0029 0.0178  0.0008  252 GLU A CA  
2093 C C   . GLU A 250 ? 0.2117 0.1807 0.1706 -0.0076 0.0168  -0.0001 252 GLU A C   
2094 O O   . GLU A 250 ? 0.2330 0.1991 0.1929 -0.0106 0.0206  0.0005  252 GLU A O   
2095 C CB  . GLU A 250 ? 0.2085 0.1882 0.1696 -0.0041 0.0196  0.0001  252 GLU A CB  
2096 C CG  . GLU A 250 ? 0.2691 0.2497 0.2267 0.0006  0.0221  0.0015  252 GLU A CG  
2097 C CD  . GLU A 250 ? 0.5875 0.5669 0.5447 -0.0003 0.0282  0.0034  252 GLU A CD  
2098 O OE1 . GLU A 250 ? 0.7083 0.6951 0.6716 -0.0031 0.0319  0.0037  252 GLU A OE1 
2099 O OE2 . GLU A 250 ? 0.6634 0.6352 0.6146 0.0019  0.0294  0.0049  252 GLU A OE2 
2100 N N   . ASP A 251 ? 0.1943 0.1651 0.1552 -0.0080 0.0120  -0.0013 253 ASP A N   
2101 C CA  . ASP A 251 ? 0.2074 0.1772 0.1711 -0.0119 0.0110  -0.0020 253 ASP A CA  
2102 C C   . ASP A 251 ? 0.2118 0.1726 0.1707 -0.0106 0.0103  -0.0005 253 ASP A C   
2103 O O   . ASP A 251 ? 0.2074 0.1657 0.1678 -0.0137 0.0119  -0.0004 253 ASP A O   
2104 C CB  . ASP A 251 ? 0.2148 0.1903 0.1822 -0.0122 0.0066  -0.0032 253 ASP A CB  
2105 C CG  . ASP A 251 ? 0.2581 0.2444 0.2312 -0.0143 0.0077  -0.0044 253 ASP A CG  
2106 O OD1 . ASP A 251 ? 0.2736 0.2632 0.2497 -0.0183 0.0116  -0.0054 253 ASP A OD1 
2107 O OD2 . ASP A 251 ? 0.2822 0.2739 0.2570 -0.0119 0.0050  -0.0042 253 ASP A OD2 
2108 N N   . LEU A 252 ? 0.1931 0.1492 0.1461 -0.0061 0.0083  0.0008  254 LEU A N   
2109 C CA  . LEU A 252 ? 0.2246 0.1738 0.1731 -0.0047 0.0082  0.0028  254 LEU A CA  
2110 C C   . LEU A 252 ? 0.2154 0.1618 0.1629 -0.0056 0.0145  0.0046  254 LEU A C   
2111 O O   . LEU A 252 ? 0.2221 0.1643 0.1695 -0.0070 0.0165  0.0061  254 LEU A O   
2112 C CB  . LEU A 252 ? 0.1938 0.1400 0.1361 0.0001  0.0046  0.0031  254 LEU A CB  
2113 C CG  . LEU A 252 ? 0.2144 0.1554 0.1514 0.0023  0.0044  0.0055  254 LEU A CG  
2114 C CD1 . LEU A 252 ? 0.2362 0.1753 0.1758 0.0002  0.0024  0.0065  254 LEU A CD1 
2115 C CD2 . LEU A 252 ? 0.2579 0.1975 0.1889 0.0065  0.0002  0.0047  254 LEU A CD2 
2116 N N   . TYR A 253 ? 0.2217 0.1704 0.1688 -0.0048 0.0183  0.0048  255 TYR A N   
2117 C CA  . TYR A 253 ? 0.2028 0.1489 0.1500 -0.0058 0.0250  0.0069  255 TYR A CA  
2118 C C   . TYR A 253 ? 0.2044 0.1513 0.1583 -0.0119 0.0284  0.0055  255 TYR A C   
2119 O O   . TYR A 253 ? 0.2186 0.1602 0.1726 -0.0133 0.0331  0.0072  255 TYR A O   
2120 C CB  . TYR A 253 ? 0.2156 0.1644 0.1614 -0.0035 0.0285  0.0078  255 TYR A CB  
2121 C CG  . TYR A 253 ? 0.2431 0.1884 0.1807 0.0026  0.0279  0.0101  255 TYR A CG  
2122 C CD1 . TYR A 253 ? 0.3034 0.2439 0.2373 0.0045  0.0322  0.0138  255 TYR A CD1 
2123 C CD2 . TYR A 253 ? 0.3127 0.2594 0.2457 0.0066  0.0233  0.0087  255 TYR A CD2 
2124 C CE1 . TYR A 253 ? 0.3294 0.2682 0.2554 0.0103  0.0314  0.0160  255 TYR A CE1 
2125 C CE2 . TYR A 253 ? 0.3376 0.2816 0.2624 0.0120  0.0225  0.0101  255 TYR A CE2 
2126 C CZ  . TYR A 253 ? 0.3154 0.2561 0.2365 0.0138  0.0264  0.0138  255 TYR A CZ  
2127 O OH  . TYR A 253 ? 0.4638 0.4033 0.3764 0.0194  0.0255  0.0153  255 TYR A OH  
2128 N N   . ASP A 254 ? 0.2033 0.1568 0.1626 -0.0154 0.0262  0.0023  256 ASP A N   
2129 C CA  . ASP A 254 ? 0.2229 0.1779 0.1880 -0.0215 0.0287  0.0001  256 ASP A CA  
2130 C C   . ASP A 254 ? 0.2066 0.1551 0.1702 -0.0221 0.0279  0.0006  256 ASP A C   
2131 O O   . ASP A 254 ? 0.2686 0.2128 0.2340 -0.0255 0.0326  0.0003  256 ASP A O   
2132 C CB  . ASP A 254 ? 0.2193 0.1840 0.1897 -0.0244 0.0255  -0.0033 256 ASP A CB  
2133 C CG  . ASP A 254 ? 0.2756 0.2482 0.2494 -0.0251 0.0276  -0.0039 256 ASP A CG  
2134 O OD1 . ASP A 254 ? 0.3132 0.2945 0.2902 -0.0255 0.0242  -0.0055 256 ASP A OD1 
2135 O OD2 . ASP A 254 ? 0.2761 0.2466 0.2496 -0.0249 0.0327  -0.0023 256 ASP A OD2 
2136 N N   . TYR A 255 ? 0.2019 0.1493 0.1623 -0.0187 0.0223  0.0015  257 TYR A N   
2137 C CA  . TYR A 255 ? 0.1975 0.1397 0.1567 -0.0188 0.0211  0.0026  257 TYR A CA  
2138 C C   . TYR A 255 ? 0.2479 0.1821 0.2035 -0.0170 0.0259  0.0061  257 TYR A C   
2139 O O   . TYR A 255 ? 0.2290 0.1586 0.1860 -0.0194 0.0298  0.0064  257 TYR A O   
2140 C CB  . TYR A 255 ? 0.1959 0.1390 0.1529 -0.0154 0.0142  0.0032  257 TYR A CB  
2141 C CG  . TYR A 255 ? 0.2223 0.1610 0.1782 -0.0147 0.0124  0.0051  257 TYR A CG  
2142 C CD1 . TYR A 255 ? 0.2247 0.1625 0.1836 -0.0181 0.0142  0.0040  257 TYR A CD1 
2143 C CD2 . TYR A 255 ? 0.2483 0.1844 0.2002 -0.0106 0.0086  0.0076  257 TYR A CD2 
2144 C CE1 . TYR A 255 ? 0.2257 0.1598 0.1837 -0.0170 0.0127  0.0061  257 TYR A CE1 
2145 C CE2 . TYR A 255 ? 0.2572 0.1904 0.2088 -0.0099 0.0068  0.0097  257 TYR A CE2 
2146 C CZ  . TYR A 255 ? 0.2588 0.1909 0.2134 -0.0129 0.0091  0.0092  257 TYR A CZ  
2147 O OH  . TYR A 255 ? 0.2615 0.1910 0.2160 -0.0118 0.0076  0.0117  257 TYR A OH  
2148 N N   . ILE A 256 ? 0.2230 0.1556 0.1737 -0.0123 0.0258  0.0089  258 ILE A N   
2149 C CA  . ILE A 256 ? 0.2324 0.1585 0.1794 -0.0097 0.0301  0.0131  258 ILE A CA  
2150 C C   . ILE A 256 ? 0.2516 0.1747 0.2015 -0.0126 0.0384  0.0136  258 ILE A C   
2151 O O   . ILE A 256 ? 0.2758 0.1926 0.2251 -0.0123 0.0435  0.0165  258 ILE A O   
2152 C CB  . ILE A 256 ? 0.2539 0.1802 0.1945 -0.0038 0.0278  0.0158  258 ILE A CB  
2153 C CG1 . ILE A 256 ? 0.2425 0.1720 0.1820 -0.0026 0.0296  0.0151  258 ILE A CG1 
2154 C CG2 . ILE A 256 ? 0.2689 0.1973 0.2074 -0.0018 0.0197  0.0148  258 ILE A CG2 
2155 C CD1 . ILE A 256 ? 0.2895 0.2187 0.2216 0.0035  0.0284  0.0178  258 ILE A CD1 
2156 N N   . ASP A 257 ? 0.2362 0.1638 0.1898 -0.0155 0.0404  0.0110  259 ASP A N   
2157 C CA  . ASP A 257 ? 0.2401 0.1651 0.1976 -0.0192 0.0484  0.0110  259 ASP A CA  
2158 C C   . ASP A 257 ? 0.2562 0.1783 0.2185 -0.0250 0.0508  0.0081  259 ASP A C   
2159 O O   . ASP A 257 ? 0.2877 0.2032 0.2517 -0.0271 0.0580  0.0092  259 ASP A O   
2160 C CB  . ASP A 257 ? 0.2328 0.1648 0.1939 -0.0211 0.0494  0.0090  259 ASP A CB  
2161 C CG  . ASP A 257 ? 0.2463 0.1795 0.2025 -0.0152 0.0496  0.0123  259 ASP A CG  
2162 O OD1 . ASP A 257 ? 0.3008 0.2294 0.2509 -0.0101 0.0496  0.0161  259 ASP A OD1 
2163 O OD2 . ASP A 257 ? 0.3096 0.2490 0.2678 -0.0156 0.0497  0.0111  259 ASP A OD2 
2164 N N   . LYS A 258 ? 0.2591 0.1859 0.2234 -0.0275 0.0452  0.0043  260 LYS A N   
2165 C CA  . LYS A 258 ? 0.2900 0.2144 0.2577 -0.0326 0.0471  0.0011  260 LYS A CA  
2166 C C   . LYS A 258 ? 0.2929 0.2074 0.2574 -0.0304 0.0503  0.0045  260 LYS A C   
2167 O O   . LYS A 258 ? 0.3287 0.2370 0.2955 -0.0340 0.0566  0.0035  260 LYS A O   
2168 C CB  . LYS A 258 ? 0.2330 0.1648 0.2023 -0.0342 0.0400  -0.0026 260 LYS A CB  
2169 C CG  . LYS A 258 ? 0.2867 0.2164 0.2582 -0.0387 0.0413  -0.0058 260 LYS A CG  
2170 C CD  . LYS A 258 ? 0.3253 0.2634 0.2984 -0.0398 0.0347  -0.0090 260 LYS A CD  
2171 C CE  . LYS A 258 ? 0.3011 0.2358 0.2745 -0.0427 0.0359  -0.0114 260 LYS A CE  
2172 N NZ  . LYS A 258 ? 0.3203 0.2637 0.2951 -0.0434 0.0298  -0.0139 260 LYS A NZ  
2173 N N   . TYR A 259 ? 0.2657 0.1787 0.2252 -0.0246 0.0466  0.0086  261 TYR A N   
2174 C CA  . TYR A 259 ? 0.2689 0.1741 0.2256 -0.0219 0.0492  0.0126  261 TYR A CA  
2175 C C   . TYR A 259 ? 0.2941 0.1940 0.2476 -0.0175 0.0549  0.0182  261 TYR A C   
2176 O O   . TYR A 259 ? 0.3518 0.2462 0.3025 -0.0140 0.0571  0.0227  261 TYR A O   
2177 C CB  . TYR A 259 ? 0.2706 0.1785 0.2248 -0.0185 0.0416  0.0139  261 TYR A CB  
2178 C CG  . TYR A 259 ? 0.2653 0.1778 0.2228 -0.0225 0.0374  0.0091  261 TYR A CG  
2179 C CD1 . TYR A 259 ? 0.2680 0.1764 0.2272 -0.0254 0.0401  0.0075  261 TYR A CD1 
2180 C CD2 . TYR A 259 ? 0.2771 0.1979 0.2361 -0.0230 0.0311  0.0063  261 TYR A CD2 
2181 C CE1 . TYR A 259 ? 0.2696 0.1832 0.2315 -0.0287 0.0364  0.0032  261 TYR A CE1 
2182 C CE2 . TYR A 259 ? 0.2484 0.1744 0.2105 -0.0261 0.0277  0.0025  261 TYR A CE2 
2183 C CZ  . TYR A 259 ? 0.2420 0.1648 0.2055 -0.0289 0.0301  0.0010  261 TYR A CZ  
2184 O OH  . TYR A 259 ? 0.2658 0.1947 0.2319 -0.0316 0.0266  -0.0026 261 TYR A OH  
2185 N N   . ASN A 260 ? 0.2773 0.1791 0.2313 -0.0176 0.0577  0.0184  262 ASN A N   
2186 C CA  . ASN A 260 ? 0.3157 0.2134 0.2668 -0.0132 0.0637  0.0241  262 ASN A CA  
2187 C C   . ASN A 260 ? 0.3313 0.2297 0.2758 -0.0060 0.0596  0.0291  262 ASN A C   
2188 O O   . ASN A 260 ? 0.4385 0.3320 0.3803 -0.0020 0.0643  0.0347  262 ASN A O   
2189 C CB  . ASN A 260 ? 0.3434 0.2318 0.2974 -0.0155 0.0736  0.0258  262 ASN A CB  
2190 C CG  . ASN A 260 ? 0.3806 0.2688 0.3414 -0.0228 0.0784  0.0209  262 ASN A CG  
2191 O OD1 . ASN A 260 ? 0.5521 0.4481 0.5157 -0.0264 0.0739  0.0160  262 ASN A OD1 
2192 N ND2 . ASN A 260 ? 0.4686 0.3482 0.4324 -0.0250 0.0879  0.0223  262 ASN A ND2 
2193 N N   . ILE A 261 ? 0.3719 0.2770 0.3141 -0.0045 0.0508  0.0270  263 ILE A N   
2194 C CA  . ILE A 261 ? 0.4301 0.3381 0.3666 0.0011  0.0449  0.0299  263 ILE A CA  
2195 C C   . ILE A 261 ? 0.3434 0.2552 0.2756 0.0049  0.0441  0.0308  263 ILE A C   
2196 O O   . ILE A 261 ? 0.3549 0.2697 0.2891 0.0026  0.0442  0.0276  263 ILE A O   
2197 C CB  . ILE A 261 ? 0.4307 0.3429 0.3682 -0.0004 0.0362  0.0262  263 ILE A CB  
2198 C CG1 . ILE A 261 ? 0.5318 0.4408 0.4726 -0.0032 0.0364  0.0257  263 ILE A CG1 
2199 C CG2 . ILE A 261 ? 0.3927 0.3087 0.3249 0.0044  0.0293  0.0277  263 ILE A CG2 
2200 C CD1 . ILE A 261 ? 0.4942 0.4080 0.4372 -0.0052 0.0287  0.0219  263 ILE A CD1 
2201 N N   . GLU A 262 ? 0.3491 0.2618 0.2750 0.0108  0.0430  0.0352  264 GLU A N   
2202 C CA  . GLU A 262 ? 0.3605 0.2776 0.2810 0.0150  0.0407  0.0355  264 GLU A CA  
2203 C C   . GLU A 262 ? 0.3497 0.2712 0.2662 0.0170  0.0314  0.0334  264 GLU A C   
2204 O O   . GLU A 262 ? 0.3581 0.2796 0.2737 0.0182  0.0282  0.0352  264 GLU A O   
2205 C CB  . GLU A 262 ? 0.4381 0.3541 0.3535 0.0207  0.0463  0.0419  264 GLU A CB  
2206 C CG  . GLU A 262 ? 0.4643 0.3765 0.3826 0.0199  0.0560  0.0444  264 GLU A CG  
2207 C CD  . GLU A 262 ? 0.4869 0.4002 0.3990 0.0268  0.0603  0.0506  264 GLU A CD  
2208 O OE1 . GLU A 262 ? 0.5152 0.4323 0.4242 0.0290  0.0602  0.0499  264 GLU A OE1 
2209 O OE2 . GLU A 262 ? 0.4858 0.3969 0.3958 0.0305  0.0637  0.0564  264 GLU A OE2 
2210 N N   . LEU A 263 ? 0.3594 0.2846 0.2737 0.0175  0.0273  0.0297  265 LEU A N   
2211 C CA  . LEU A 263 ? 0.3640 0.2926 0.2740 0.0197  0.0192  0.0276  265 LEU A CA  
2212 C C   . LEU A 263 ? 0.3450 0.2756 0.2474 0.0256  0.0189  0.0316  265 LEU A C   
2213 O O   . LEU A 263 ? 0.4132 0.3436 0.3123 0.0290  0.0248  0.0353  265 LEU A O   
2214 C CB  . LEU A 263 ? 0.3835 0.3146 0.2927 0.0193  0.0158  0.0227  265 LEU A CB  
2215 C CG  . LEU A 263 ? 0.3393 0.2707 0.2555 0.0144  0.0140  0.0184  265 LEU A CG  
2216 C CD1 . LEU A 263 ? 0.3784 0.3123 0.2928 0.0154  0.0113  0.0146  265 LEU A CD1 
2217 C CD2 . LEU A 263 ? 0.3793 0.3103 0.2988 0.0120  0.0087  0.0174  265 LEU A CD2 
2218 N N   . ASP A 264 ? 0.3453 0.2785 0.2452 0.0267  0.0121  0.0308  266 ASP A N   
2219 C CA  . ASP A 264 ? 0.3719 0.3092 0.2638 0.0320  0.0098  0.0330  266 ASP A CA  
2220 C C   . ASP A 264 ? 0.3801 0.3191 0.2660 0.0350  0.0109  0.0310  266 ASP A C   
2221 O O   . ASP A 264 ? 0.3600 0.2985 0.2469 0.0330  0.0081  0.0258  266 ASP A O   
2222 C CB  . ASP A 264 ? 0.3776 0.3181 0.2689 0.0312  0.0009  0.0302  266 ASP A CB  
2223 C CG  . ASP A 264 ? 0.3788 0.3250 0.2627 0.0361  -0.0022 0.0326  266 ASP A CG  
2224 O OD1 . ASP A 264 ? 0.3879 0.3366 0.2648 0.0405  0.0001  0.0337  266 ASP A OD1 
2225 O OD2 . ASP A 264 ? 0.4583 0.4074 0.3434 0.0354  -0.0072 0.0332  266 ASP A OD2 
2226 N N   . PRO A 265 ? 0.3486 0.2896 0.2285 0.0403  0.0153  0.0355  267 PRO A N   
2227 C CA  . PRO A 265 ? 0.3281 0.2710 0.2020 0.0436  0.0166  0.0338  267 PRO A CA  
2228 C C   . PRO A 265 ? 0.3685 0.3143 0.2367 0.0444  0.0086  0.0278  267 PRO A C   
2229 O O   . PRO A 265 ? 0.3816 0.3278 0.2456 0.0463  0.0091  0.0249  267 PRO A O   
2230 C CB  . PRO A 265 ? 0.3474 0.2930 0.2154 0.0497  0.0223  0.0407  267 PRO A CB  
2231 C CG  . PRO A 265 ? 0.3855 0.3323 0.2545 0.0503  0.0211  0.0449  267 PRO A CG  
2232 C CD  . PRO A 265 ? 0.3113 0.2533 0.1895 0.0440  0.0198  0.0428  267 PRO A CD  
2233 N N   . ARG A 266 ? 0.3567 0.3043 0.2249 0.0430  0.0015  0.0257  268 ARG A N   
2234 C CA  . ARG A 266 ? 0.4235 0.3728 0.2868 0.0432  -0.0058 0.0193  268 ARG A CA  
2235 C C   . ARG A 266 ? 0.4209 0.3660 0.2890 0.0393  -0.0072 0.0136  268 ARG A C   
2236 O O   . ARG A 266 ? 0.3989 0.3439 0.2625 0.0400  -0.0114 0.0082  268 ARG A O   
2237 C CB  . ARG A 266 ? 0.5266 0.4794 0.3898 0.0421  -0.0130 0.0184  268 ARG A CB  
2238 C CG  . ARG A 266 ? 0.5491 0.4988 0.4212 0.0364  -0.0169 0.0160  268 ARG A CG  
2239 C CD  . ARG A 266 ? 0.5929 0.5469 0.4644 0.0357  -0.0240 0.0153  268 ARG A CD  
2240 N NE  . ARG A 266 ? 0.5766 0.5339 0.4499 0.0370  -0.0220 0.0221  268 ARG A NE  
2241 C CZ  . ARG A 266 ? 0.6974 0.6610 0.5693 0.0379  -0.0270 0.0236  268 ARG A CZ  
2242 N NH1 . ARG A 266 ? 0.7374 0.7046 0.6058 0.0371  -0.0344 0.0181  268 ARG A NH1 
2243 N NH2 . ARG A 266 ? 0.6667 0.6331 0.5405 0.0397  -0.0242 0.0306  268 ARG A NH2 
2244 N N   . PHE A 267 ? 0.3588 0.3005 0.2353 0.0356  -0.0035 0.0147  269 PHE A N   
2245 C CA  . PHE A 267 ? 0.3158 0.2549 0.1967 0.0326  -0.0041 0.0103  269 PHE A CA  
2246 C C   . PHE A 267 ? 0.3934 0.3326 0.2705 0.0355  0.0004  0.0095  269 PHE A C   
2247 O O   . PHE A 267 ? 0.4129 0.3509 0.2922 0.0343  -0.0005 0.0057  269 PHE A O   
2248 C CB  . PHE A 267 ? 0.2963 0.2334 0.1870 0.0278  -0.0016 0.0116  269 PHE A CB  
2249 C CG  . PHE A 267 ? 0.2924 0.2289 0.1880 0.0245  -0.0068 0.0109  269 PHE A CG  
2250 C CD1 . PHE A 267 ? 0.2905 0.2271 0.1887 0.0236  -0.0055 0.0152  269 PHE A CD1 
2251 C CD2 . PHE A 267 ? 0.3236 0.2594 0.2213 0.0225  -0.0125 0.0063  269 PHE A CD2 
2252 C CE1 . PHE A 267 ? 0.3124 0.2488 0.2150 0.0209  -0.0100 0.0149  269 PHE A CE1 
2253 C CE2 . PHE A 267 ? 0.2997 0.2353 0.2023 0.0196  -0.0170 0.0060  269 PHE A CE2 
2254 C CZ  . PHE A 267 ? 0.3082 0.2443 0.2132 0.0188  -0.0159 0.0103  269 PHE A CZ  
2255 N N   . ASN A 268 ? 0.4232 0.3643 0.2950 0.0397  0.0054  0.0135  270 ASN A N   
2256 C CA  . ASN A 268 ? 0.4469 0.3885 0.3158 0.0426  0.0103  0.0136  270 ASN A CA  
2257 C C   . ASN A 268 ? 0.4667 0.4083 0.3291 0.0451  0.0062  0.0080  270 ASN A C   
2258 O O   . ASN A 268 ? 0.5381 0.4793 0.4009 0.0460  0.0090  0.0065  270 ASN A O   
2259 C CB  . ASN A 268 ? 0.5377 0.4815 0.4015 0.0473  0.0164  0.0194  270 ASN A CB  
2260 C CG  . ASN A 268 ? 0.6198 0.5621 0.4907 0.0449  0.0225  0.0250  270 ASN A CG  
2261 O OD1 . ASN A 268 ? 0.7306 0.6740 0.5984 0.0484  0.0268  0.0305  270 ASN A OD1 
2262 N ND2 . ASN A 268 ? 0.6182 0.5580 0.4984 0.0392  0.0232  0.0236  270 ASN A ND2 
2263 N N   . ASP A 269 ? 0.4385 0.3806 0.2951 0.0462  -0.0002 0.0047  271 ASP A N   
2264 C CA  . ASP A 269 ? 0.5368 0.4779 0.3865 0.0485  -0.0040 -0.0013 271 ASP A CA  
2265 C C   . ASP A 269 ? 0.5117 0.4490 0.3668 0.0443  -0.0090 -0.0067 271 ASP A C   
2266 O O   . ASP A 269 ? 0.5685 0.5035 0.4192 0.0459  -0.0110 -0.0119 271 ASP A O   
2267 C CB  . ASP A 269 ? 0.7256 0.6699 0.5651 0.0520  -0.0082 -0.0027 271 ASP A CB  
2268 C CG  . ASP A 269 ? 0.9366 0.8855 0.7689 0.0577  -0.0031 0.0025  271 ASP A CG  
2269 O OD1 . ASP A 269 ? 1.0029 0.9563 0.8293 0.0601  -0.0056 0.0041  271 ASP A OD1 
2270 O OD2 . ASP A 269 ? 0.9766 0.9250 0.8094 0.0598  0.0036  0.0054  271 ASP A OD2 
2271 N N   . ILE A 270 ? 0.3865 0.3228 0.2508 0.0394  -0.0107 -0.0056 272 ILE A N   
2272 C CA  . ILE A 270 ? 0.3865 0.3196 0.2557 0.0359  -0.0158 -0.0101 272 ILE A CA  
2273 C C   . ILE A 270 ? 0.3334 0.2654 0.2126 0.0324  -0.0135 -0.0091 272 ILE A C   
2274 O O   . ILE A 270 ? 0.3597 0.2891 0.2427 0.0306  -0.0163 -0.0125 272 ILE A O   
2275 C CB  . ILE A 270 ? 0.3657 0.2994 0.2362 0.0333  -0.0218 -0.0106 272 ILE A CB  
2276 C CG1 . ILE A 270 ? 0.3350 0.2709 0.2111 0.0313  -0.0196 -0.0046 272 ILE A CG1 
2277 C CG2 . ILE A 270 ? 0.4120 0.3479 0.2726 0.0364  -0.0254 -0.0130 272 ILE A CG2 
2278 C CD1 . ILE A 270 ? 0.3774 0.3144 0.2569 0.0285  -0.0251 -0.0043 272 ILE A CD1 
2279 N N   . LEU A 271 ? 0.3391 0.2732 0.2230 0.0313  -0.0082 -0.0046 273 LEU A N   
2280 C CA  . LEU A 271 ? 0.3056 0.2400 0.1992 0.0273  -0.0068 -0.0039 273 LEU A CA  
2281 C C   . LEU A 271 ? 0.3436 0.2786 0.2391 0.0283  -0.0044 -0.0057 273 LEU A C   
2282 O O   . LEU A 271 ? 0.3597 0.2946 0.2613 0.0260  -0.0060 -0.0072 273 LEU A O   
2283 C CB  . LEU A 271 ? 0.3478 0.2841 0.2459 0.0252  -0.0021 0.0008  273 LEU A CB  
2284 C CG  . LEU A 271 ? 0.3588 0.2963 0.2666 0.0206  -0.0010 0.0012  273 LEU A CG  
2285 C CD1 . LEU A 271 ? 0.3813 0.3175 0.2931 0.0180  -0.0068 -0.0006 273 LEU A CD1 
2286 C CD2 . LEU A 271 ? 0.3829 0.3211 0.2942 0.0183  0.0039  0.0051  273 LEU A CD2 
2287 N N   . GLY A 272 ? 0.3358 0.2720 0.2261 0.0320  -0.0002 -0.0050 274 GLY A N   
2288 C CA  . GLY A 272 ? 0.3161 0.2536 0.2082 0.0335  0.0027  -0.0061 274 GLY A CA  
2289 C C   . GLY A 272 ? 0.3029 0.2448 0.2047 0.0298  0.0063  -0.0035 274 GLY A C   
2290 O O   . GLY A 272 ? 0.3256 0.2688 0.2319 0.0264  0.0077  -0.0010 274 GLY A O   
2291 N N   . ARG A 273 ? 0.2940 0.2384 0.1988 0.0308  0.0081  -0.0044 275 ARG A N   
2292 C CA  . ARG A 273 ? 0.2630 0.2132 0.1773 0.0273  0.0107  -0.0027 275 ARG A CA  
2293 C C   . ARG A 273 ? 0.2775 0.2283 0.1964 0.0268  0.0074  -0.0048 275 ARG A C   
2294 O O   . ARG A 273 ? 0.3439 0.2925 0.2592 0.0307  0.0068  -0.0067 275 ARG A O   
2295 C CB  . ARG A 273 ? 0.2973 0.2525 0.2125 0.0292  0.0167  -0.0006 275 ARG A CB  
2296 C CG  . ARG A 273 ? 0.3400 0.2949 0.2516 0.0299  0.0211  0.0023  275 ARG A CG  
2297 C CD  . ARG A 273 ? 0.3422 0.3034 0.2585 0.0297  0.0274  0.0049  275 ARG A CD  
2298 N NE  . ARG A 273 ? 0.3523 0.3150 0.2645 0.0350  0.0293  0.0046  275 ARG A NE  
2299 C CZ  . ARG A 273 ? 0.3154 0.2846 0.2320 0.0356  0.0343  0.0068  275 ARG A CZ  
2300 N NH1 . ARG A 273 ? 0.4054 0.3802 0.3309 0.0305  0.0375  0.0090  275 ARG A NH1 
2301 N NH2 . ARG A 273 ? 0.3398 0.3099 0.2521 0.0411  0.0361  0.0067  275 ARG A NH2 
2302 N N   . HIS A 274 ? 0.2209 0.1747 0.1475 0.0224  0.0058  -0.0042 276 HIS A N   
2303 C CA  . HIS A 274 ? 0.2006 0.1552 0.1319 0.0221  0.0026  -0.0054 276 HIS A CA  
2304 C C   . HIS A 274 ? 0.2043 0.1672 0.1446 0.0186  0.0042  -0.0038 276 HIS A C   
2305 O O   . HIS A 274 ? 0.2250 0.1901 0.1685 0.0144  0.0050  -0.0028 276 HIS A O   
2306 C CB  . HIS A 274 ? 0.2104 0.1592 0.1408 0.0207  -0.0026 -0.0069 276 HIS A CB  
2307 C CG  . HIS A 274 ? 0.2260 0.1677 0.1477 0.0235  -0.0048 -0.0091 276 HIS A CG  
2308 N ND1 . HIS A 274 ? 0.2651 0.2025 0.1825 0.0272  -0.0059 -0.0118 276 HIS A ND1 
2309 C CD2 . HIS A 274 ? 0.2481 0.1867 0.1644 0.0234  -0.0059 -0.0089 276 HIS A CD2 
2310 C CE1 . HIS A 274 ? 0.2865 0.2189 0.1959 0.0288  -0.0080 -0.0140 276 HIS A CE1 
2311 N NE2 . HIS A 274 ? 0.2958 0.2294 0.2045 0.0267  -0.0082 -0.0120 276 HIS A NE2 
2312 N N   . SER A 275 ? 0.2118 0.1796 0.1561 0.0203  0.0047  -0.0035 277 SER A N   
2313 C CA  . SER A 275 ? 0.2000 0.1773 0.1530 0.0171  0.0053  -0.0021 277 SER A CA  
2314 C C   . SER A 275 ? 0.2355 0.2116 0.1919 0.0145  0.0011  -0.0025 277 SER A C   
2315 O O   . SER A 275 ? 0.2554 0.2240 0.2088 0.0159  -0.0023 -0.0036 277 SER A O   
2316 C CB  . SER A 275 ? 0.2588 0.2425 0.2150 0.0206  0.0070  -0.0011 277 SER A CB  
2317 O OG  . SER A 275 ? 0.3660 0.3428 0.3193 0.0246  0.0046  -0.0021 277 SER A OG  
2318 N N   . ARG A 276 ? 0.2020 0.1861 0.1650 0.0106  0.0013  -0.0017 278 ARG A N   
2319 C CA  . ARG A 276 ? 0.1838 0.1688 0.1507 0.0089  -0.0022 -0.0015 278 ARG A CA  
2320 C C   . ARG A 276 ? 0.2094 0.1976 0.1794 0.0126  -0.0032 -0.0004 278 ARG A C   
2321 O O   . ARG A 276 ? 0.2189 0.2143 0.1912 0.0148  -0.0006 0.0007  278 ARG A O   
2322 C CB  . ARG A 276 ? 0.1720 0.1650 0.1443 0.0037  -0.0014 -0.0013 278 ARG A CB  
2323 C CG  . ARG A 276 ? 0.1796 0.1728 0.1550 0.0018  -0.0049 -0.0011 278 ARG A CG  
2324 C CD  . ARG A 276 ? 0.1952 0.1907 0.1723 -0.0036 -0.0039 -0.0021 278 ARG A CD  
2325 N NE  . ARG A 276 ? 0.2273 0.2202 0.2054 -0.0050 -0.0068 -0.0019 278 ARG A NE  
2326 C CZ  . ARG A 276 ? 0.2334 0.2229 0.2106 -0.0085 -0.0063 -0.0026 278 ARG A CZ  
2327 N NH1 . ARG A 276 ? 0.2399 0.2275 0.2154 -0.0111 -0.0028 -0.0035 278 ARG A NH1 
2328 N NH2 . ARG A 276 ? 0.2145 0.2020 0.1926 -0.0093 -0.0088 -0.0020 278 ARG A NH2 
2329 N N   . LYS A 277 ? 0.2137 0.1967 0.1841 0.0136  -0.0065 -0.0003 279 LYS A N   
2330 C CA  . LYS A 277 ? 0.1927 0.1766 0.1659 0.0176  -0.0070 0.0011  279 LYS A CA  
2331 C C   . LYS A 277 ? 0.2437 0.2372 0.2242 0.0162  -0.0080 0.0033  279 LYS A C   
2332 O O   . LYS A 277 ? 0.2981 0.2942 0.2803 0.0122  -0.0094 0.0031  279 LYS A O   
2333 C CB  . LYS A 277 ? 0.2120 0.1839 0.1817 0.0196  -0.0096 -0.0003 279 LYS A CB  
2334 C CG  . LYS A 277 ? 0.1999 0.1627 0.1615 0.0209  -0.0093 -0.0030 279 LYS A CG  
2335 C CD  . LYS A 277 ? 0.1904 0.1558 0.1494 0.0243  -0.0053 -0.0031 279 LYS A CD  
2336 C CE  . LYS A 277 ? 0.2252 0.1814 0.1753 0.0264  -0.0051 -0.0059 279 LYS A CE  
2337 N NZ  . LYS A 277 ? 0.2627 0.2174 0.2085 0.0235  -0.0055 -0.0067 279 LYS A NZ  
2338 N N   . ARG A 278 ? 0.2124 0.2110 0.1968 0.0201  -0.0069 0.0057  280 ARG A N   
2339 C CA  . ARG A 278 ? 0.2368 0.2443 0.2276 0.0201  -0.0080 0.0084  280 ARG A CA  
2340 C C   . ARG A 278 ? 0.2371 0.2357 0.2286 0.0218  -0.0104 0.0093  280 ARG A C   
2341 O O   . ARG A 278 ? 0.2490 0.2374 0.2377 0.0247  -0.0102 0.0085  280 ARG A O   
2342 C CB  . ARG A 278 ? 0.2457 0.2650 0.2410 0.0238  -0.0053 0.0114  280 ARG A CB  
2343 C CG  . ARG A 278 ? 0.2885 0.3181 0.2843 0.0218  -0.0029 0.0107  280 ARG A CG  
2344 C CD  . ARG A 278 ? 0.2725 0.3165 0.2738 0.0251  -0.0007 0.0142  280 ARG A CD  
2345 N NE  . ARG A 278 ? 0.2857 0.3367 0.2869 0.0243  0.0021  0.0135  280 ARG A NE  
2346 C CZ  . ARG A 278 ? 0.3025 0.3646 0.3066 0.0192  0.0024  0.0123  280 ARG A CZ  
2347 N NH1 . ARG A 278 ? 0.2583 0.3262 0.2651 0.0147  0.0000  0.0113  280 ARG A NH1 
2348 N NH2 . ARG A 278 ? 0.2489 0.3163 0.2532 0.0187  0.0054  0.0121  280 ARG A NH2 
2349 N N   . TRP A 279 ? 0.2195 0.2881 0.2136 0.0332  0.0195  0.0427  281 TRP A N   
2350 C CA  . TRP A 279 ? 0.1982 0.2550 0.1878 0.0353  0.0179  0.0432  281 TRP A CA  
2351 C C   . TRP A 279 ? 0.2686 0.3253 0.2565 0.0432  0.0206  0.0498  281 TRP A C   
2352 O O   . TRP A 279 ? 0.2494 0.2915 0.2319 0.0457  0.0208  0.0507  281 TRP A O   
2353 C CB  . TRP A 279 ? 0.2173 0.2825 0.2100 0.0307  0.0140  0.0400  281 TRP A CB  
2354 C CG  . TRP A 279 ? 0.2143 0.2745 0.2068 0.0235  0.0118  0.0334  281 TRP A CG  
2355 C CD1 . TRP A 279 ? 0.3032 0.3758 0.3004 0.0176  0.0107  0.0296  281 TRP A CD1 
2356 C CD2 . TRP A 279 ? 0.1991 0.2400 0.1863 0.0215  0.0107  0.0299  281 TRP A CD2 
2357 N NE1 . TRP A 279 ? 0.2312 0.2925 0.2260 0.0123  0.0094  0.0241  281 TRP A NE1 
2358 C CE2 . TRP A 279 ? 0.2352 0.2776 0.2241 0.0148  0.0092  0.0244  281 TRP A CE2 
2359 C CE3 . TRP A 279 ? 0.2447 0.2676 0.2259 0.0245  0.0108  0.0308  281 TRP A CE3 
2360 C CZ2 . TRP A 279 ? 0.2352 0.2619 0.2199 0.0120  0.0079  0.0203  281 TRP A CZ2 
2361 C CZ3 . TRP A 279 ? 0.2583 0.2666 0.2356 0.0212  0.0090  0.0265  281 TRP A CZ3 
2362 C CH2 . TRP A 279 ? 0.2660 0.2765 0.2452 0.0154  0.0076  0.0216  281 TRP A CH2 
2363 N N   . GLU A 280 ? 0.2499 0.3224 0.2422 0.0472  0.0230  0.0545  282 GLU A N   
2364 C CA  . GLU A 280 ? 0.2572 0.3300 0.2478 0.0555  0.0262  0.0614  282 GLU A CA  
2365 C C   . GLU A 280 ? 0.2450 0.2966 0.2279 0.0598  0.0299  0.0632  282 GLU A C   
2366 O O   . GLU A 280 ? 0.2849 0.3296 0.2640 0.0658  0.0325  0.0677  282 GLU A O   
2367 C CB  . GLU A 280 ? 0.2917 0.3864 0.2890 0.0591  0.0282  0.0662  282 GLU A CB  
2368 C CG  . GLU A 280 ? 0.2952 0.4120 0.2992 0.0567  0.0247  0.0660  282 GLU A CG  
2369 C CD  . GLU A 280 ? 0.3531 0.4805 0.3620 0.0478  0.0214  0.0596  282 GLU A CD  
2370 O OE1 . GLU A 280 ? 0.3783 0.5246 0.3923 0.0454  0.0186  0.0591  282 GLU A OE1 
2371 O OE2 . GLU A 280 ? 0.3393 0.4562 0.3467 0.0433  0.0217  0.0552  282 GLU A OE2 
2372 N N   . ARG A 281 ? 0.2474 0.2878 0.2273 0.0567  0.0304  0.0596  283 ARG A N   
2373 C CA  . ARG A 281 ? 0.2909 0.3108 0.2626 0.0605  0.0337  0.0608  283 ARG A CA  
2374 C C   . ARG A 281 ? 0.2993 0.3018 0.2644 0.0607  0.0322  0.0596  283 ARG A C   
2375 O O   . ARG A 281 ? 0.3155 0.3029 0.2737 0.0651  0.0354  0.0620  283 ARG A O   
2376 C CB  . ARG A 281 ? 0.4042 0.4158 0.3735 0.0565  0.0339  0.0567  283 ARG A CB  
2377 C CG  . ARG A 281 ? 0.5193 0.5076 0.4796 0.0547  0.0327  0.0529  283 ARG A CG  
2378 C CD  . ARG A 281 ? 0.5704 0.5535 0.5295 0.0495  0.0317  0.0481  283 ARG A CD  
2379 N NE  . ARG A 281 ? 0.6131 0.6001 0.5731 0.0516  0.0361  0.0503  283 ARG A NE  
2380 C CZ  . ARG A 281 ? 0.4637 0.4352 0.4162 0.0540  0.0393  0.0506  283 ARG A CZ  
2381 N NH1 . ARG A 281 ? 0.4835 0.4348 0.4267 0.0544  0.0382  0.0487  283 ARG A NH1 
2382 N NH2 . ARG A 281 ? 0.4369 0.4136 0.3912 0.0559  0.0435  0.0528  283 ARG A NH2 
2383 N N   . PHE A 282 ? 0.2351 0.2395 0.2023 0.0559  0.0277  0.0560  284 PHE A N   
2384 C CA  . PHE A 282 ? 0.2425 0.2311 0.2044 0.0553  0.0262  0.0545  284 PHE A CA  
2385 C C   . PHE A 282 ? 0.2433 0.2361 0.2061 0.0594  0.0273  0.0589  284 PHE A C   
2386 O O   . PHE A 282 ? 0.2652 0.2459 0.2243 0.0590  0.0265  0.0580  284 PHE A O   
2387 C CB  . PHE A 282 ? 0.2500 0.2365 0.2133 0.0481  0.0211  0.0482  284 PHE A CB  
2388 C CG  . PHE A 282 ? 0.2908 0.2721 0.2526 0.0443  0.0203  0.0441  284 PHE A CG  
2389 C CD1 . PHE A 282 ? 0.3313 0.2939 0.2853 0.0448  0.0211  0.0427  284 PHE A CD1 
2390 C CD2 . PHE A 282 ? 0.2314 0.2262 0.1989 0.0402  0.0191  0.0417  284 PHE A CD2 
2391 C CE1 . PHE A 282 ? 0.3129 0.2703 0.2649 0.0418  0.0207  0.0393  284 PHE A CE1 
2392 C CE2 . PHE A 282 ? 0.3053 0.2945 0.2711 0.0368  0.0190  0.0382  284 PHE A CE2 
2393 C CZ  . PHE A 282 ? 0.3465 0.3170 0.3045 0.0379  0.0199  0.0372  284 PHE A CZ  
2394 N N   . VAL A 283 ? 0.2425 0.2526 0.2103 0.0633  0.0292  0.0635  285 VAL A N   
2395 C CA  . VAL A 283 ? 0.2398 0.2549 0.2082 0.0682  0.0309  0.0686  285 VAL A CA  
2396 C C   . VAL A 283 ? 0.2729 0.2760 0.2352 0.0755  0.0366  0.0739  285 VAL A C   
2397 O O   . VAL A 283 ? 0.2853 0.2879 0.2464 0.0789  0.0399  0.0761  285 VAL A O   
2398 C CB  . VAL A 283 ? 0.2359 0.2759 0.2120 0.0694  0.0302  0.0714  285 VAL A CB  
2399 C CG1 . VAL A 283 ? 0.2839 0.3300 0.2602 0.0751  0.0320  0.0772  285 VAL A CG1 
2400 C CG2 . VAL A 283 ? 0.2536 0.3038 0.2346 0.0616  0.0250  0.0655  285 VAL A CG2 
2401 N N   . HIS A 284 ? 0.2379 0.2307 0.1962 0.0780  0.0381  0.0760  286 HIS A N   
2402 C CA  . HIS A 284 ? 0.2520 0.2326 0.2041 0.0851  0.0441  0.0812  286 HIS A CA  
2403 C C   . HIS A 284 ? 0.2675 0.2485 0.2191 0.0886  0.0458  0.0851  286 HIS A C   
2404 O O   . HIS A 284 ? 0.2578 0.2481 0.2137 0.0853  0.0422  0.0837  286 HIS A O   
2405 C CB  . HIS A 284 ? 0.2863 0.2431 0.2299 0.0833  0.0450  0.0776  286 HIS A CB  
2406 C CG  . HIS A 284 ? 0.2641 0.2100 0.2060 0.0764  0.0404  0.0716  286 HIS A CG  
2407 N ND1 . HIS A 284 ? 0.2903 0.2319 0.2317 0.0759  0.0401  0.0722  286 HIS A ND1 
2408 C CD2 . HIS A 284 ? 0.2670 0.2058 0.2079 0.0700  0.0361  0.0653  286 HIS A CD2 
2409 C CE1 . HIS A 284 ? 0.2829 0.2160 0.2236 0.0694  0.0357  0.0663  286 HIS A CE1 
2410 N NE2 . HIS A 284 ? 0.2742 0.2055 0.2144 0.0659  0.0331  0.0622  286 HIS A NE2 
2411 N N   . SER A 285 ? 0.3037 0.2757 0.2517 0.0924  0.0511  0.0867  287 SER A N   
2412 C CA  . SER A 285 ? 0.2928 0.2673 0.2417 0.0949  0.0536  0.0892  287 SER A CA  
2413 C C   . SER A 285 ? 0.2734 0.2380 0.2206 0.0901  0.0507  0.0861  287 SER A C   
2414 O O   . SER A 285 ? 0.3320 0.3029 0.2814 0.0915  0.0513  0.0884  287 SER A O   
2415 C CB  . SER A 285 ? 0.3916 0.3568 0.3362 0.0995  0.0604  0.0908  287 SER A CB  
2416 O OG  . SER A 285 ? 0.4957 0.4404 0.4333 0.0963  0.0612  0.0863  287 SER A OG  
2417 N N   . GLU A 286 ? 0.2869 0.2371 0.2305 0.0846  0.0476  0.0811  288 GLU A N   
2418 C CA  . GLU A 286 ? 0.2883 0.2291 0.2309 0.0801  0.0451  0.0782  288 GLU A CA  
2419 C C   . GLU A 286 ? 0.3502 0.3013 0.2979 0.0757  0.0392  0.0761  288 GLU A C   
2420 O O   . GLU A 286 ? 0.4089 0.3551 0.3575 0.0715  0.0370  0.0733  288 GLU A O   
2421 C CB  . GLU A 286 ? 0.3183 0.2383 0.2547 0.0758  0.0449  0.0730  288 GLU A CB  
2422 C CG  . GLU A 286 ? 0.3893 0.2982 0.3207 0.0782  0.0505  0.0734  288 GLU A CG  
2423 C CD  . GLU A 286 ? 0.4383 0.3513 0.3684 0.0834  0.0547  0.0759  288 GLU A CD  
2424 O OE1 . GLU A 286 ? 0.3922 0.3053 0.3215 0.0826  0.0531  0.0743  288 GLU A OE1 
2425 O OE2 . GLU A 286 ? 0.4779 0.3943 0.4079 0.0885  0.0599  0.0798  288 GLU A OE2 
2426 N N   . ASN A 287 ? 0.2695 0.2365 0.2224 0.0744  0.0364  0.0750  289 ASN A N   
2427 C CA  . ASN A 287 ? 0.2507 0.2303 0.2098 0.0686  0.0309  0.0708  289 ASN A CA  
2428 C C   . ASN A 287 ? 0.2272 0.2296 0.1922 0.0710  0.0305  0.0740  289 ASN A C   
2429 O O   . ASN A 287 ? 0.2584 0.2720 0.2281 0.0663  0.0263  0.0707  289 ASN A O   
2430 C CB  . ASN A 287 ? 0.2366 0.2124 0.1962 0.0623  0.0267  0.0642  289 ASN A CB  
2431 C CG  . ASN A 287 ? 0.2033 0.1854 0.1635 0.0638  0.0276  0.0647  289 ASN A CG  
2432 O OD1 . ASN A 287 ? 0.2275 0.2231 0.1903 0.0684  0.0300  0.0694  289 ASN A OD1 
2433 N ND2 . ASN A 287 ? 0.2534 0.2264 0.2113 0.0599  0.0257  0.0601  289 ASN A ND2 
2434 N N   . GLN A 288 ? 0.2538 0.2638 0.2185 0.0781  0.0346  0.0803  290 GLN A N   
2435 C CA  . GLN A 288 ? 0.2611 0.2946 0.2319 0.0796  0.0332  0.0827  290 GLN A CA  
2436 C C   . GLN A 288 ? 0.2563 0.3009 0.2299 0.0790  0.0314  0.0837  290 GLN A C   
2437 O O   . GLN A 288 ? 0.3013 0.3651 0.2800 0.0773  0.0284  0.0830  290 GLN A O   
2438 C CB  . GLN A 288 ? 0.3292 0.3693 0.2996 0.0878  0.0381  0.0897  290 GLN A CB  
2439 C CG  . GLN A 288 ? 0.3562 0.3909 0.3227 0.0952  0.0432  0.0963  290 GLN A CG  
2440 C CD  . GLN A 288 ? 0.5655 0.6079 0.5335 0.1016  0.0482  0.1005  290 GLN A CD  
2441 O OE1 . GLN A 288 ? 0.6830 0.7127 0.6471 0.1050  0.0536  0.1014  290 GLN A OE1 
2442 N NE2 . GLN A 288 ? 0.5949 0.6590 0.5686 0.1032  0.0463  0.1030  290 GLN A NE2 
2443 N N   . HIS A 289 ? 0.2533 0.2864 0.2234 0.0802  0.0332  0.0851  291 HIS A N   
2444 C CA  . HIS A 289 ? 0.2618 0.3041 0.2341 0.0797  0.0319  0.0859  291 HIS A CA  
2445 C C   . HIS A 289 ? 0.2701 0.3163 0.2461 0.0712  0.0262  0.0788  291 HIS A C   
2446 O O   . HIS A 289 ? 0.2947 0.3522 0.2730 0.0702  0.0245  0.0789  291 HIS A O   
2447 C CB  . HIS A 289 ? 0.3146 0.3419 0.2823 0.0827  0.0359  0.0892  291 HIS A CB  
2448 C CG  . HIS A 289 ? 0.3367 0.3436 0.3017 0.0775  0.0352  0.0841  291 HIS A CG  
2449 N ND1 . HIS A 289 ? 0.3485 0.3402 0.3096 0.0771  0.0365  0.0824  291 HIS A ND1 
2450 C CD2 . HIS A 289 ? 0.3410 0.3406 0.3066 0.0724  0.0332  0.0804  291 HIS A CD2 
2451 C CE1 . HIS A 289 ? 0.3615 0.3381 0.3209 0.0719  0.0350  0.0778  291 HIS A CE1 
2452 N NE2 . HIS A 289 ? 0.3500 0.3313 0.3125 0.0690  0.0330  0.0765  291 HIS A NE2 
2453 N N   . LEU A 290 ? 0.2655 0.3027 0.2415 0.0656  0.0237  0.0728  292 LEU A N   
2454 C CA  . LEU A 290 ? 0.2278 0.2677 0.2070 0.0580  0.0188  0.0661  292 LEU A CA  
2455 C C   . LEU A 290 ? 0.2191 0.2733 0.2021 0.0549  0.0160  0.0632  292 LEU A C   
2456 O O   . LEU A 290 ? 0.2472 0.3052 0.2328 0.0488  0.0123  0.0578  292 LEU A O   
2457 C CB  . LEU A 290 ? 0.2380 0.2587 0.2147 0.0536  0.0176  0.0612  292 LEU A CB  
2458 C CG  . LEU A 290 ? 0.2666 0.2714 0.2396 0.0555  0.0203  0.0632  292 LEU A CG  
2459 C CD1 . LEU A 290 ? 0.2992 0.2872 0.2701 0.0508  0.0183  0.0581  292 LEU A CD1 
2460 C CD2 . LEU A 290 ? 0.3257 0.3364 0.3007 0.0554  0.0203  0.0646  292 LEU A CD2 
2461 N N   . VAL A 291 ? 0.2237 0.2859 0.2073 0.0590  0.0180  0.0667  293 VAL A N   
2462 C CA  . VAL A 291 ? 0.2378 0.3124 0.2251 0.0559  0.0159  0.0641  293 VAL A CA  
2463 C C   . VAL A 291 ? 0.2647 0.3621 0.2559 0.0585  0.0157  0.0677  293 VAL A C   
2464 O O   . VAL A 291 ? 0.3714 0.4737 0.3617 0.0655  0.0185  0.0743  293 VAL A O   
2465 C CB  . VAL A 291 ? 0.2839 0.3504 0.2693 0.0579  0.0184  0.0649  293 VAL A CB  
2466 C CG1 . VAL A 291 ? 0.3390 0.4180 0.3287 0.0542  0.0166  0.0619  293 VAL A CG1 
2467 C CG2 . VAL A 291 ? 0.2563 0.3004 0.2369 0.0555  0.0183  0.0614  293 VAL A CG2 
2468 N N   . SER A 292 ? 0.2546 0.3657 0.2499 0.0529  0.0122  0.0634  294 SER A N   
2469 C CA  . SER A 292 ? 0.2129 0.3473 0.2124 0.0537  0.0109  0.0654  294 SER A CA  
2470 C C   . SER A 292 ? 0.2229 0.3661 0.2263 0.0474  0.0087  0.0603  294 SER A C   
2471 O O   . SER A 292 ? 0.2037 0.3345 0.2062 0.0422  0.0078  0.0548  294 SER A O   
2472 C CB  . SER A 292 ? 0.2332 0.3752 0.2326 0.0517  0.0086  0.0643  294 SER A CB  
2473 O OG  . SER A 292 ? 0.2344 0.3682 0.2336 0.0440  0.0058  0.0570  294 SER A OG  
2474 N N   . PRO A 293 ? 0.2123 0.3770 0.2203 0.0477  0.0078  0.0618  295 PRO A N   
2475 C CA  . PRO A 293 ? 0.1958 0.3690 0.2078 0.0406  0.0058  0.0563  295 PRO A CA  
2476 C C   . PRO A 293 ? 0.2301 0.3993 0.2415 0.0322  0.0026  0.0486  295 PRO A C   
2477 O O   . PRO A 293 ? 0.1975 0.3607 0.2095 0.0262  0.0020  0.0432  295 PRO A O   
2478 C CB  . PRO A 293 ? 0.2693 0.4685 0.2865 0.0426  0.0049  0.0597  295 PRO A CB  
2479 C CG  . PRO A 293 ? 0.3650 0.5656 0.3806 0.0526  0.0079  0.0683  295 PRO A CG  
2480 C CD  . PRO A 293 ? 0.2449 0.4271 0.2546 0.0546  0.0088  0.0688  295 PRO A CD  
2481 N N   . GLU A 294 ? 0.2092 0.3805 0.2188 0.0320  0.0010  0.0484  296 GLU A N   
2482 C CA  . GLU A 294 ? 0.1553 0.3218 0.1638 0.0247  -0.0015 0.0416  296 GLU A CA  
2483 C C   . GLU A 294 ? 0.1916 0.3350 0.1971 0.0227  -0.0008 0.0383  296 GLU A C   
2484 O O   . GLU A 294 ? 0.1790 0.3173 0.1847 0.0162  -0.0021 0.0321  296 GLU A O   
2485 C CB  . GLU A 294 ? 0.1977 0.3700 0.2045 0.0259  -0.0027 0.0428  296 GLU A CB  
2486 C CG  . GLU A 294 ? 0.2266 0.4233 0.2357 0.0262  -0.0045 0.0444  296 GLU A CG  
2487 C CD  . GLU A 294 ? 0.4276 0.6349 0.4379 0.0347  -0.0027 0.0527  296 GLU A CD  
2488 O OE1 . GLU A 294 ? 0.2727 0.4670 0.2809 0.0409  0.0004  0.0575  296 GLU A OE1 
2489 O OE2 . GLU A 294 ? 0.5101 0.7390 0.5232 0.0353  -0.0043 0.0544  296 GLU A OE2 
2490 N N   . ALA A 295 ? 0.1757 0.3050 0.1783 0.0282  0.0013  0.0423  297 ALA A N   
2491 C CA  . ALA A 295 ? 0.1680 0.2761 0.1677 0.0265  0.0017  0.0394  297 ALA A CA  
2492 C C   . ALA A 295 ? 0.1931 0.2957 0.1931 0.0237  0.0021  0.0364  297 ALA A C   
2493 O O   . ALA A 295 ? 0.1758 0.2675 0.1747 0.0189  0.0010  0.0313  297 ALA A O   
2494 C CB  . ALA A 295 ? 0.1994 0.2945 0.1957 0.0327  0.0041  0.0443  297 ALA A CB  
2495 N N   . LEU A 296 ? 0.1981 0.3082 0.1997 0.0269  0.0040  0.0399  298 LEU A N   
2496 C CA  . LEU A 296 ? 0.1729 0.2774 0.1747 0.0247  0.0050  0.0376  298 LEU A CA  
2497 C C   . LEU A 296 ? 0.1651 0.2781 0.1699 0.0171  0.0032  0.0317  298 LEU A C   
2498 O O   . LEU A 296 ? 0.1779 0.2801 0.1814 0.0131  0.0033  0.0275  298 LEU A O   
2499 C CB  . LEU A 296 ? 0.1865 0.2977 0.1896 0.0303  0.0080  0.0431  298 LEU A CB  
2500 C CG  . LEU A 296 ? 0.2105 0.3108 0.2096 0.0380  0.0108  0.0490  298 LEU A CG  
2501 C CD1 . LEU A 296 ? 0.2270 0.3327 0.2273 0.0434  0.0142  0.0539  298 LEU A CD1 
2502 C CD2 . LEU A 296 ? 0.2795 0.3564 0.2731 0.0371  0.0109  0.0464  298 LEU A CD2 
2503 N N   . ASP A 297 ? 0.1638 0.2955 0.1723 0.0148  0.0016  0.0311  299 ASP A N   
2504 C CA  . ASP A 297 ? 0.1775 0.3163 0.1883 0.0068  0.0001  0.0249  299 ASP A CA  
2505 C C   . ASP A 297 ? 0.1852 0.3106 0.1930 0.0021  -0.0014 0.0194  299 ASP A C   
2506 O O   . ASP A 297 ? 0.1772 0.2966 0.1847 -0.0034 -0.0012 0.0142  299 ASP A O   
2507 C CB  . ASP A 297 ? 0.1572 0.3190 0.1719 0.0051  -0.0017 0.0251  299 ASP A CB  
2508 C CG  . ASP A 297 ? 0.2110 0.3799 0.2278 -0.0038 -0.0029 0.0181  299 ASP A CG  
2509 O OD1 . ASP A 297 ? 0.2227 0.3912 0.2415 -0.0069 -0.0015 0.0162  299 ASP A OD1 
2510 O OD2 . ASP A 297 ? 0.2324 0.4063 0.2484 -0.0079 -0.0049 0.0146  299 ASP A OD2 
2511 N N   . PHE A 298 ? 0.1599 0.2810 0.1656 0.0043  -0.0024 0.0206  300 PHE A N   
2512 C CA  . PHE A 298 ? 0.1765 0.2849 0.1797 0.0006  -0.0035 0.0160  300 PHE A CA  
2513 C C   . PHE A 298 ? 0.2052 0.2945 0.2058 0.0006  -0.0026 0.0145  300 PHE A C   
2514 O O   . PHE A 298 ? 0.1502 0.2319 0.1498 -0.0043 -0.0029 0.0094  300 PHE A O   
2515 C CB  . PHE A 298 ? 0.1539 0.2609 0.1558 0.0040  -0.0042 0.0185  300 PHE A CB  
2516 C CG  . PHE A 298 ? 0.2021 0.2973 0.2022 0.0008  -0.0052 0.0145  300 PHE A CG  
2517 C CD1 . PHE A 298 ? 0.1841 0.2802 0.1844 -0.0056 -0.0060 0.0085  300 PHE A CD1 
2518 C CD2 . PHE A 298 ? 0.2418 0.3257 0.2403 0.0043  -0.0051 0.0167  300 PHE A CD2 
2519 C CE1 . PHE A 298 ? 0.2096 0.2952 0.2085 -0.0079 -0.0065 0.0051  300 PHE A CE1 
2520 C CE2 . PHE A 298 ? 0.2009 0.2751 0.1986 0.0016  -0.0059 0.0132  300 PHE A CE2 
2521 C CZ  . PHE A 298 ? 0.2260 0.3013 0.2240 -0.0042 -0.0066 0.0076  300 PHE A CZ  
2522 N N   . LEU A 299 ? 0.1654 0.2463 0.1642 0.0062  -0.0013 0.0189  301 LEU A N   
2523 C CA  . LEU A 299 ? 0.2052 0.2678 0.2006 0.0064  -0.0006 0.0177  301 LEU A CA  
2524 C C   . LEU A 299 ? 0.1664 0.2288 0.1622 0.0025  0.0003  0.0144  301 LEU A C   
2525 O O   . LEU A 299 ? 0.1769 0.2272 0.1704 -0.0006 0.0001  0.0105  301 LEU A O   
2526 C CB  . LEU A 299 ? 0.1787 0.2337 0.1716 0.0129  0.0010  0.0230  301 LEU A CB  
2527 C CG  . LEU A 299 ? 0.1945 0.2308 0.1830 0.0134  0.0015  0.0219  301 LEU A CG  
2528 C CD1 . LEU A 299 ? 0.1648 0.1889 0.1515 0.0112  -0.0007 0.0186  301 LEU A CD1 
2529 C CD2 . LEU A 299 ? 0.2397 0.2693 0.2251 0.0196  0.0037  0.0270  301 LEU A CD2 
2530 N N   . ASP A 300 ? 0.1542 0.2302 0.1531 0.0027  0.0017  0.0161  302 ASP A N   
2531 C CA  . ASP A 300 ? 0.1661 0.2434 0.1660 -0.0012 0.0032  0.0133  302 ASP A CA  
2532 C C   . ASP A 300 ? 0.2246 0.3019 0.2251 -0.0085 0.0022  0.0070  302 ASP A C   
2533 O O   . ASP A 300 ? 0.1883 0.2578 0.1874 -0.0118 0.0037  0.0038  302 ASP A O   
2534 C CB  . ASP A 300 ? 0.1526 0.2484 0.1573 -0.0001 0.0044  0.0163  302 ASP A CB  
2535 C CG  . ASP A 300 ? 0.2332 0.3301 0.2394 -0.0033 0.0066  0.0144  302 ASP A CG  
2536 O OD1 . ASP A 300 ? 0.2295 0.3112 0.2320 -0.0016 0.0085  0.0147  302 ASP A OD1 
2537 O OD2 . ASP A 300 ? 0.2748 0.3881 0.2858 -0.0075 0.0067  0.0127  302 ASP A OD2 
2538 N N   . LYS A 301 ? 0.1608 0.2464 0.1626 -0.0110 0.0003  0.0050  303 LYS A N   
2539 C CA  . LYS A 301 ? 0.1647 0.2501 0.1664 -0.0179 -0.0001 -0.0011 303 LYS A CA  
2540 C C   . LYS A 301 ? 0.1693 0.2373 0.1673 -0.0185 -0.0007 -0.0038 303 LYS A C   
2541 O O   . LYS A 301 ? 0.1889 0.2533 0.1861 -0.0238 -0.0003 -0.0088 303 LYS A O   
2542 C CB  . LYS A 301 ? 0.1592 0.2618 0.1636 -0.0205 -0.0017 -0.0022 303 LYS A CB  
2543 C CG  . LYS A 301 ? 0.1996 0.3212 0.2083 -0.0218 -0.0013 -0.0010 303 LYS A CG  
2544 C CD  . LYS A 301 ? 0.2452 0.3850 0.2559 -0.0225 -0.0034 -0.0006 303 LYS A CD  
2545 C CE  . LYS A 301 ? 0.2650 0.4245 0.2802 -0.0269 -0.0035 -0.0020 303 LYS A CE  
2546 N NZ  . LYS A 301 ? 0.3442 0.5091 0.3628 -0.0231 -0.0019 0.0025  303 LYS A NZ  
2547 N N   . LEU A 302 ? 0.1592 0.2166 0.1551 -0.0134 -0.0015 -0.0006 304 LEU A N   
2548 C CA  . LEU A 302 ? 0.1606 0.2017 0.1534 -0.0134 -0.0022 -0.0026 304 LEU A CA  
2549 C C   . LEU A 302 ? 0.1951 0.2224 0.1846 -0.0126 -0.0010 -0.0029 304 LEU A C   
2550 O O   . LEU A 302 ? 0.1672 0.1841 0.1546 -0.0152 -0.0007 -0.0063 304 LEU A O   
2551 C CB  . LEU A 302 ? 0.1557 0.1922 0.1478 -0.0088 -0.0038 0.0007  304 LEU A CB  
2552 C CG  . LEU A 302 ? 0.1695 0.2165 0.1639 -0.0089 -0.0049 0.0013  304 LEU A CG  
2553 C CD1 . LEU A 302 ? 0.2113 0.2527 0.2051 -0.0040 -0.0056 0.0052  304 LEU A CD1 
2554 C CD2 . LEU A 302 ? 0.1926 0.2384 0.1871 -0.0137 -0.0053 -0.0037 304 LEU A CD2 
2555 N N   . LEU A 303 ? 0.1799 0.2066 0.1687 -0.0088 0.0001  0.0010  305 LEU A N   
2556 C CA  . LEU A 303 ? 0.1708 0.1833 0.1555 -0.0071 0.0012  0.0013  305 LEU A CA  
2557 C C   . LEU A 303 ? 0.1798 0.1955 0.1651 -0.0106 0.0038  -0.0008 305 LEU A C   
2558 O O   . LEU A 303 ? 0.2125 0.2324 0.1984 -0.0088 0.0058  0.0018  305 LEU A O   
2559 C CB  . LEU A 303 ? 0.2003 0.2085 0.1829 -0.0012 0.0015  0.0062  305 LEU A CB  
2560 C CG  . LEU A 303 ? 0.1700 0.1720 0.1514 0.0019  -0.0007 0.0079  305 LEU A CG  
2561 C CD1 . LEU A 303 ? 0.2015 0.1971 0.1798 0.0074  0.0003  0.0124  305 LEU A CD1 
2562 C CD2 . LEU A 303 ? 0.1997 0.1885 0.1785 0.0001  -0.0026 0.0046  305 LEU A CD2 
2563 N N   . ARG A 304 ? 0.1717 0.1850 0.1567 -0.0158 0.0043  -0.0055 306 ARG A N   
2564 C CA  . ARG A 304 ? 0.1610 0.1739 0.1458 -0.0198 0.0072  -0.0082 306 ARG A CA  
2565 C C   . ARG A 304 ? 0.1676 0.1622 0.1469 -0.0198 0.0080  -0.0101 306 ARG A C   
2566 O O   . ARG A 304 ? 0.1731 0.1597 0.1506 -0.0196 0.0062  -0.0116 306 ARG A O   
2567 C CB  . ARG A 304 ? 0.1962 0.2202 0.1844 -0.0265 0.0079  -0.0125 306 ARG A CB  
2568 C CG  . ARG A 304 ? 0.2251 0.2667 0.2179 -0.0271 0.0060  -0.0117 306 ARG A CG  
2569 C CD  . ARG A 304 ? 0.1993 0.2533 0.1954 -0.0240 0.0065  -0.0073 306 ARG A CD  
2570 N NE  . ARG A 304 ? 0.2271 0.2848 0.2249 -0.0266 0.0094  -0.0080 306 ARG A NE  
2571 C CZ  . ARG A 304 ? 0.2745 0.3434 0.2756 -0.0241 0.0104  -0.0042 306 ARG A CZ  
2572 N NH1 . ARG A 304 ? 0.2833 0.3556 0.2864 -0.0268 0.0134  -0.0049 306 ARG A NH1 
2573 N NH2 . ARG A 304 ? 0.2666 0.3432 0.2693 -0.0188 0.0088  0.0005  306 ARG A NH2 
2574 N N   . TYR A 305 ? 0.1832 0.1717 0.1601 -0.0199 0.0109  -0.0099 307 TYR A N   
2575 C CA  . TYR A 305 ? 0.1794 0.1510 0.1507 -0.0202 0.0120  -0.0119 307 TYR A CA  
2576 C C   . TYR A 305 ? 0.2051 0.1757 0.1769 -0.0254 0.0127  -0.0166 307 TYR A C   
2577 O O   . TYR A 305 ? 0.1987 0.1587 0.1675 -0.0244 0.0114  -0.0178 307 TYR A O   
2578 C CB  . TYR A 305 ? 0.1906 0.1573 0.1594 -0.0205 0.0159  -0.0114 307 TYR A CB  
2579 C CG  . TYR A 305 ? 0.1709 0.1324 0.1366 -0.0149 0.0161  -0.0070 307 TYR A CG  
2580 C CD1 . TYR A 305 ? 0.2015 0.1484 0.1610 -0.0103 0.0141  -0.0055 307 TYR A CD1 
2581 C CD2 . TYR A 305 ? 0.1948 0.1656 0.1633 -0.0143 0.0186  -0.0046 307 TYR A CD2 
2582 C CE1 . TYR A 305 ? 0.1875 0.1285 0.1431 -0.0054 0.0146  -0.0019 307 TYR A CE1 
2583 C CE2 . TYR A 305 ? 0.1885 0.1535 0.1535 -0.0090 0.0195  -0.0007 307 TYR A CE2 
2584 C CZ  . TYR A 305 ? 0.2050 0.1544 0.1630 -0.0047 0.0176  0.0005  307 TYR A CZ  
2585 O OH  . TYR A 305 ? 0.2265 0.1690 0.1799 0.0003  0.0187  0.0040  307 TYR A OH  
2586 N N   . ASP A 306 ? 0.1798 0.1616 0.1554 -0.0310 0.0148  -0.0194 308 ASP A N   
2587 C CA  . ASP A 306 ? 0.1937 0.1738 0.1691 -0.0365 0.0164  -0.0243 308 ASP A CA  
2588 C C   . ASP A 306 ? 0.1901 0.1743 0.1672 -0.0364 0.0132  -0.0253 308 ASP A C   
2589 O O   . ASP A 306 ? 0.2030 0.2017 0.1843 -0.0373 0.0115  -0.0248 308 ASP A O   
2590 C CB  . ASP A 306 ? 0.1746 0.1666 0.1537 -0.0431 0.0193  -0.0273 308 ASP A CB  
2591 C CG  . ASP A 306 ? 0.2303 0.2166 0.2076 -0.0492 0.0223  -0.0327 308 ASP A CG  
2592 O OD1 . ASP A 306 ? 0.2465 0.2228 0.2206 -0.0483 0.0215  -0.0341 308 ASP A OD1 
2593 O OD2 . ASP A 306 ? 0.2774 0.2689 0.2564 -0.0550 0.0256  -0.0355 308 ASP A OD2 
2594 N N   . HIS A 307 ? 0.1836 0.1552 0.1573 -0.0350 0.0127  -0.0264 309 HIS A N   
2595 C CA  . HIS A 307 ? 0.1870 0.1612 0.1622 -0.0347 0.0102  -0.0273 309 HIS A CA  
2596 C C   . HIS A 307 ? 0.2018 0.1875 0.1797 -0.0408 0.0114  -0.0312 309 HIS A C   
2597 O O   . HIS A 307 ? 0.2035 0.1981 0.1840 -0.0406 0.0091  -0.0311 309 HIS A O   
2598 C CB  . HIS A 307 ? 0.2132 0.1720 0.1846 -0.0325 0.0101  -0.0280 309 HIS A CB  
2599 C CG  . HIS A 307 ? 0.2227 0.1712 0.1903 -0.0357 0.0142  -0.0313 309 HIS A CG  
2600 N ND1 . HIS A 307 ? 0.2064 0.1453 0.1702 -0.0345 0.0164  -0.0302 309 HIS A ND1 
2601 C CD2 . HIS A 307 ? 0.2633 0.2087 0.2299 -0.0398 0.0170  -0.0354 309 HIS A CD2 
2602 C CE1 . HIS A 307 ? 0.2359 0.1665 0.1967 -0.0378 0.0204  -0.0335 309 HIS A CE1 
2603 N NE2 . HIS A 307 ? 0.2485 0.1824 0.2108 -0.0411 0.0209  -0.0368 309 HIS A NE2 
2604 N N   . GLN A 308 ? 0.1905 0.1769 0.1679 -0.0463 0.0150  -0.0348 310 GLN A N   
2605 C CA  . GLN A 308 ? 0.1905 0.1878 0.1699 -0.0529 0.0162  -0.0391 310 GLN A CA  
2606 C C   . GLN A 308 ? 0.2242 0.2409 0.2085 -0.0540 0.0142  -0.0377 310 GLN A C   
2607 O O   . GLN A 308 ? 0.2718 0.2997 0.2578 -0.0587 0.0139  -0.0408 310 GLN A O   
2608 C CB  . GLN A 308 ? 0.2201 0.2117 0.1973 -0.0591 0.0210  -0.0436 310 GLN A CB  
2609 C CG  . GLN A 308 ? 0.2585 0.2323 0.2306 -0.0590 0.0237  -0.0459 310 GLN A CG  
2610 C CD  . GLN A 308 ? 0.3078 0.2745 0.2771 -0.0650 0.0292  -0.0502 310 GLN A CD  
2611 O OE1 . GLN A 308 ? 0.3147 0.2910 0.2865 -0.0704 0.0310  -0.0521 310 GLN A OE1 
2612 N NE2 . GLN A 308 ? 0.3144 0.2643 0.2787 -0.0640 0.0322  -0.0515 310 GLN A NE2 
2613 N N   . SER A 309 ? 0.1984 0.2193 0.1846 -0.0496 0.0128  -0.0330 311 SER A N   
2614 C CA  . SER A 309 ? 0.2091 0.2485 0.2001 -0.0496 0.0111  -0.0307 311 SER A CA  
2615 C C   . SER A 309 ? 0.1873 0.2329 0.1797 -0.0442 0.0074  -0.0267 311 SER A C   
2616 O O   . SER A 309 ? 0.1987 0.2603 0.1947 -0.0438 0.0060  -0.0247 311 SER A O   
2617 C CB  . SER A 309 ? 0.2113 0.2518 0.2036 -0.0476 0.0127  -0.0276 311 SER A CB  
2618 O OG  . SER A 309 ? 0.2663 0.3043 0.2582 -0.0535 0.0164  -0.0314 311 SER A OG  
2619 N N   . ARG A 310 ? 0.1712 0.2048 0.1610 -0.0399 0.0060  -0.0253 312 ARG A N   
2620 C CA  . ARG A 310 ? 0.1757 0.2139 0.1669 -0.0349 0.0030  -0.0213 312 ARG A CA  
2621 C C   . ARG A 310 ? 0.1533 0.2025 0.1459 -0.0377 0.0018  -0.0235 312 ARG A C   
2622 O O   . ARG A 310 ? 0.1883 0.2356 0.1796 -0.0427 0.0031  -0.0283 312 ARG A O   
2623 C CB  . ARG A 310 ? 0.1730 0.1954 0.1612 -0.0304 0.0019  -0.0197 312 ARG A CB  
2624 C CG  . ARG A 310 ? 0.1642 0.1748 0.1498 -0.0273 0.0028  -0.0176 312 ARG A CG  
2625 C CD  . ARG A 310 ? 0.1624 0.1579 0.1450 -0.0234 0.0012  -0.0165 312 ARG A CD  
2626 N NE  . ARG A 310 ? 0.1772 0.1607 0.1560 -0.0220 0.0026  -0.0160 312 ARG A NE  
2627 C CZ  . ARG A 310 ? 0.1687 0.1378 0.1437 -0.0208 0.0025  -0.0169 312 ARG A CZ  
2628 N NH1 . ARG A 310 ? 0.1601 0.1249 0.1353 -0.0207 0.0010  -0.0183 312 ARG A NH1 
2629 N NH2 . ARG A 310 ? 0.1919 0.1513 0.1629 -0.0195 0.0040  -0.0163 312 ARG A NH2 
2630 N N   . LEU A 311 ? 0.1671 0.2271 0.1620 -0.0342 -0.0003 -0.0197 313 LEU A N   
2631 C CA  . LEU A 311 ? 0.1659 0.2341 0.1612 -0.0355 -0.0016 -0.0209 313 LEU A CA  
2632 C C   . LEU A 311 ? 0.1788 0.2341 0.1717 -0.0356 -0.0014 -0.0232 313 LEU A C   
2633 O O   . LEU A 311 ? 0.1709 0.2131 0.1627 -0.0319 -0.0017 -0.0214 313 LEU A O   
2634 C CB  . LEU A 311 ? 0.1596 0.2370 0.1567 -0.0300 -0.0036 -0.0154 313 LEU A CB  
2635 C CG  . LEU A 311 ? 0.2041 0.2975 0.2040 -0.0289 -0.0039 -0.0123 313 LEU A CG  
2636 C CD1 . LEU A 311 ? 0.2476 0.3465 0.2483 -0.0227 -0.0053 -0.0066 313 LEU A CD1 
2637 C CD2 . LEU A 311 ? 0.2606 0.3691 0.2618 -0.0351 -0.0040 -0.0164 313 LEU A CD2 
2638 N N   . THR A 312 ? 0.1651 0.2241 0.1571 -0.0400 -0.0009 -0.0274 314 THR A N   
2639 C CA  . THR A 312 ? 0.1800 0.2301 0.1706 -0.0392 -0.0008 -0.0287 314 THR A CA  
2640 C C   . THR A 312 ? 0.1770 0.2327 0.1691 -0.0346 -0.0028 -0.0245 314 THR A C   
2641 O O   . THR A 312 ? 0.1913 0.2591 0.1849 -0.0327 -0.0041 -0.0213 314 THR A O   
2642 C CB  . THR A 312 ? 0.1924 0.2436 0.1808 -0.0452 0.0011  -0.0345 314 THR A CB  
2643 O OG1 . THR A 312 ? 0.2063 0.2736 0.1951 -0.0475 0.0001  -0.0352 314 THR A OG1 
2644 C CG2 . THR A 312 ? 0.2307 0.2762 0.2173 -0.0503 0.0038  -0.0389 314 THR A CG2 
2645 N N   . ALA A 313 ? 0.1709 0.2179 0.1627 -0.0326 -0.0029 -0.0244 315 ALA A N   
2646 C CA  . ALA A 313 ? 0.1784 0.2297 0.1717 -0.0285 -0.0043 -0.0205 315 ALA A CA  
2647 C C   . ALA A 313 ? 0.1637 0.2300 0.1566 -0.0303 -0.0045 -0.0210 315 ALA A C   
2648 O O   . ALA A 313 ? 0.1869 0.2618 0.1809 -0.0268 -0.0057 -0.0167 315 ALA A O   
2649 C CB  . ALA A 313 ? 0.1703 0.2107 0.1639 -0.0270 -0.0040 -0.0209 315 ALA A CB  
2650 N N   . ARG A 314 ? 0.1957 0.2651 0.1864 -0.0357 -0.0032 -0.0262 316 ARG A N   
2651 C CA  . ARG A 314 ? 0.2219 0.3060 0.2115 -0.0379 -0.0036 -0.0272 316 ARG A CA  
2652 C C   . ARG A 314 ? 0.2164 0.3146 0.2072 -0.0383 -0.0050 -0.0254 316 ARG A C   
2653 O O   . ARG A 314 ? 0.2385 0.3494 0.2297 -0.0361 -0.0064 -0.0223 316 ARG A O   
2654 C CB  . ARG A 314 ? 0.2637 0.3466 0.2499 -0.0442 -0.0017 -0.0338 316 ARG A CB  
2655 C CG  . ARG A 314 ? 0.4175 0.5151 0.4015 -0.0467 -0.0023 -0.0353 316 ARG A CG  
2656 C CD  . ARG A 314 ? 0.5570 0.6557 0.5408 -0.0421 -0.0027 -0.0318 316 ARG A CD  
2657 N NE  . ARG A 314 ? 0.6133 0.7027 0.5946 -0.0438 -0.0003 -0.0354 316 ARG A NE  
2658 C CZ  . ARG A 314 ? 0.5582 0.6533 0.5355 -0.0469 0.0007  -0.0388 316 ARG A CZ  
2659 N NH1 . ARG A 314 ? 0.5672 0.6525 0.5423 -0.0480 0.0033  -0.0418 316 ARG A NH1 
2660 N NH2 . ARG A 314 ? 0.4471 0.5578 0.4224 -0.0487 -0.0010 -0.0389 316 ARG A NH2 
2661 N N   . GLU A 315 ? 0.2328 0.3295 0.2243 -0.0411 -0.0044 -0.0273 317 GLU A N   
2662 C CA  . GLU A 315 ? 0.2207 0.3311 0.2145 -0.0411 -0.0056 -0.0251 317 GLU A CA  
2663 C C   . GLU A 315 ? 0.1848 0.2977 0.1807 -0.0337 -0.0069 -0.0179 317 GLU A C   
2664 O O   . GLU A 315 ? 0.2453 0.3729 0.2425 -0.0317 -0.0081 -0.0147 317 GLU A O   
2665 C CB  . GLU A 315 ? 0.2324 0.3384 0.2271 -0.0444 -0.0042 -0.0275 317 GLU A CB  
2666 C CG  . GLU A 315 ? 0.2778 0.3845 0.2706 -0.0525 -0.0025 -0.0344 317 GLU A CG  
2667 C CD  . GLU A 315 ? 0.2515 0.3538 0.2454 -0.0552 -0.0008 -0.0359 317 GLU A CD  
2668 O OE1 . GLU A 315 ? 0.2192 0.3076 0.2130 -0.0518 0.0001  -0.0339 317 GLU A OE1 
2669 O OE2 . GLU A 315 ? 0.2560 0.3692 0.2510 -0.0608 -0.0004 -0.0391 317 GLU A OE2 
2670 N N   . ALA A 316 ? 0.2058 0.3041 0.2018 -0.0294 -0.0065 -0.0153 318 ALA A N   
2671 C CA  . ALA A 316 ? 0.1572 0.2556 0.1545 -0.0227 -0.0072 -0.0089 318 ALA A CA  
2672 C C   . ALA A 316 ? 0.2123 0.3198 0.2094 -0.0197 -0.0080 -0.0057 318 ALA A C   
2673 O O   . ALA A 316 ? 0.1901 0.3060 0.1882 -0.0152 -0.0084 -0.0005 318 ALA A O   
2674 C CB  . ALA A 316 ? 0.1733 0.2540 0.1703 -0.0197 -0.0069 -0.0076 318 ALA A CB  
2675 N N   . MET A 317 ? 0.1949 0.3004 0.1905 -0.0216 -0.0078 -0.0084 319 MET A N   
2676 C CA  A MET A 317 ? 0.2209 0.3344 0.2157 -0.0186 -0.0081 -0.0053 319 MET A CA  
2677 C CA  B MET A 317 ? 0.2332 0.3466 0.2279 -0.0189 -0.0081 -0.0055 319 MET A CA  
2678 C C   . MET A 317 ? 0.1681 0.3005 0.1622 -0.0199 -0.0091 -0.0050 319 MET A C   
2679 O O   . MET A 317 ? 0.2210 0.3619 0.2144 -0.0161 -0.0095 -0.0010 319 MET A O   
2680 C CB  A MET A 317 ? 0.2037 0.3101 0.1969 -0.0203 -0.0072 -0.0082 319 MET A CB  
2681 C CB  B MET A 317 ? 0.1721 0.2789 0.1651 -0.0212 -0.0072 -0.0091 319 MET A CB  
2682 C CG  A MET A 317 ? 0.1647 0.2549 0.1594 -0.0176 -0.0066 -0.0069 319 MET A CG  
2683 C CG  B MET A 317 ? 0.1984 0.2879 0.1927 -0.0198 -0.0065 -0.0092 319 MET A CG  
2684 S SD  A MET A 317 ? 0.2272 0.3103 0.2213 -0.0187 -0.0053 -0.0094 319 MET A SD  
2685 S SD  B MET A 317 ? 0.1983 0.2797 0.1915 -0.0222 -0.0050 -0.0132 319 MET A SD  
2686 C CE  A MET A 317 ? 0.2176 0.3071 0.2083 -0.0256 -0.0046 -0.0163 319 MET A CE  
2687 C CE  B MET A 317 ? 0.2633 0.3532 0.2560 -0.0183 -0.0047 -0.0089 319 MET A CE  
2688 N N   . GLU A 318 ? 0.1879 0.3276 0.1824 -0.0251 -0.0096 -0.0090 320 GLU A N   
2689 C CA  . GLU A 318 ? 0.1946 0.3540 0.1892 -0.0266 -0.0111 -0.0087 320 GLU A CA  
2690 C C   . GLU A 318 ? 0.1976 0.3656 0.1954 -0.0217 -0.0117 -0.0029 320 GLU A C   
2691 O O   . GLU A 318 ? 0.2030 0.3888 0.2016 -0.0218 -0.0131 -0.0016 320 GLU A O   
2692 C CB  . GLU A 318 ? 0.2472 0.4115 0.2413 -0.0349 -0.0112 -0.0158 320 GLU A CB  
2693 C CG  . GLU A 318 ? 0.2183 0.3744 0.2087 -0.0404 -0.0100 -0.0223 320 GLU A CG  
2694 C CD  . GLU A 318 ? 0.2806 0.4471 0.2673 -0.0415 -0.0108 -0.0234 320 GLU A CD  
2695 O OE1 . GLU A 318 ? 0.3347 0.5179 0.3208 -0.0449 -0.0124 -0.0252 320 GLU A OE1 
2696 O OE2 . GLU A 318 ? 0.2892 0.4476 0.2739 -0.0390 -0.0098 -0.0226 320 GLU A OE2 
2697 N N   . HIS A 319 ? 0.1813 0.3372 0.1806 -0.0175 -0.0106 0.0005  321 HIS A N   
2698 C CA  . HIS A 319 ? 0.2189 0.3813 0.2209 -0.0136 -0.0105 0.0051  321 HIS A CA  
2699 C C   . HIS A 319 ? 0.2171 0.3900 0.2192 -0.0066 -0.0108 0.0121  321 HIS A C   
2700 O O   . HIS A 319 ? 0.2043 0.3715 0.2043 -0.0031 -0.0103 0.0147  321 HIS A O   
2701 C CB  . HIS A 319 ? 0.1924 0.3376 0.1949 -0.0112 -0.0090 0.0065  321 HIS A CB  
2702 C CG  . HIS A 319 ? 0.1761 0.3264 0.1811 -0.0083 -0.0083 0.0101  321 HIS A CG  
2703 N ND1 . HIS A 319 ? 0.2102 0.3648 0.2159 -0.0010 -0.0077 0.0171  321 HIS A ND1 
2704 C CD2 . HIS A 319 ? 0.1862 0.3381 0.1933 -0.0115 -0.0077 0.0079  321 HIS A CD2 
2705 C CE1 . HIS A 319 ? 0.1966 0.3556 0.2047 0.0003  -0.0068 0.0191  321 HIS A CE1 
2706 N NE2 . HIS A 319 ? 0.2019 0.3596 0.2111 -0.0060 -0.0068 0.0136  321 HIS A NE2 
2707 N N   . PRO A 320 ? 0.1705 0.3587 0.1751 -0.0043 -0.0113 0.0156  322 PRO A N   
2708 C CA  . PRO A 320 ? 0.1893 0.3877 0.1937 0.0032  -0.0112 0.0230  322 PRO A CA  
2709 C C   . PRO A 320 ? 0.1760 0.3597 0.1790 0.0103  -0.0089 0.0286  322 PRO A C   
2710 O O   . PRO A 320 ? 0.2284 0.4170 0.2298 0.0161  -0.0083 0.0340  322 PRO A O   
2711 C CB  . PRO A 320 ? 0.1997 0.4140 0.2081 0.0043  -0.0116 0.0255  322 PRO A CB  
2712 C CG  . PRO A 320 ? 0.1964 0.4167 0.2063 -0.0047 -0.0130 0.0180  322 PRO A CG  
2713 C CD  . PRO A 320 ? 0.1750 0.3742 0.1828 -0.0090 -0.0119 0.0127  322 PRO A CD  
2714 N N   . TYR A 321 ? 0.1822 0.3480 0.1852 0.0101  -0.0076 0.0275  323 TYR A N   
2715 C CA  . TYR A 321 ? 0.1692 0.3199 0.1703 0.0158  -0.0056 0.0319  323 TYR A CA  
2716 C C   . TYR A 321 ? 0.1559 0.3029 0.1547 0.0169  -0.0054 0.0325  323 TYR A C   
2717 O O   . TYR A 321 ? 0.1902 0.3316 0.1875 0.0227  -0.0035 0.0378  323 TYR A O   
2718 C CB  . TYR A 321 ? 0.1840 0.3163 0.1849 0.0136  -0.0049 0.0288  323 TYR A CB  
2719 C CG  . TYR A 321 ? 0.1912 0.3062 0.1902 0.0181  -0.0032 0.0320  323 TYR A CG  
2720 C CD1 . TYR A 321 ? 0.1941 0.3078 0.1923 0.0247  -0.0010 0.0382  323 TYR A CD1 
2721 C CD2 . TYR A 321 ? 0.2258 0.3256 0.2237 0.0153  -0.0036 0.0284  323 TYR A CD2 
2722 C CE1 . TYR A 321 ? 0.1745 0.2717 0.1705 0.0280  0.0007  0.0405  323 TYR A CE1 
2723 C CE2 . TYR A 321 ? 0.2031 0.2878 0.1995 0.0186  -0.0023 0.0308  323 TYR A CE2 
2724 C CZ  . TYR A 321 ? 0.2584 0.3414 0.2535 0.0246  -0.0002 0.0366  323 TYR A CZ  
2725 O OH  . TYR A 321 ? 0.2489 0.3162 0.2420 0.0272  0.0012  0.0385  323 TYR A OH  
2726 N N   . PHE A 322 ? 0.2022 0.3520 0.2003 0.0114  -0.0069 0.0273  324 PHE A N   
2727 C CA  . PHE A 322 ? 0.1864 0.3318 0.1824 0.0120  -0.0064 0.0274  324 PHE A CA  
2728 C C   . PHE A 322 ? 0.1762 0.3380 0.1705 0.0140  -0.0069 0.0300  324 PHE A C   
2729 O O   . PHE A 322 ? 0.1814 0.3409 0.1735 0.0146  -0.0062 0.0304  324 PHE A O   
2730 C CB  . PHE A 322 ? 0.1656 0.3021 0.1614 0.0055  -0.0071 0.0204  324 PHE A CB  
2731 C CG  . PHE A 322 ? 0.2139 0.3335 0.2108 0.0043  -0.0067 0.0184  324 PHE A CG  
2732 C CD1 . PHE A 322 ? 0.1843 0.2904 0.1812 0.0081  -0.0055 0.0215  324 PHE A CD1 
2733 C CD2 . PHE A 322 ? 0.2004 0.3180 0.1982 -0.0006 -0.0075 0.0135  324 PHE A CD2 
2734 C CE1 . PHE A 322 ? 0.1985 0.2897 0.1960 0.0070  -0.0055 0.0197  324 PHE A CE1 
2735 C CE2 . PHE A 322 ? 0.2257 0.3279 0.2240 -0.0012 -0.0072 0.0121  324 PHE A CE2 
2736 C CZ  . PHE A 322 ? 0.1907 0.2801 0.1887 0.0027  -0.0064 0.0151  324 PHE A CZ  
2737 N N   . TYR A 323 ? 0.2107 0.3893 0.2059 0.0153  -0.0080 0.0322  325 TYR A N   
2738 C CA  . TYR A 323 ? 0.1639 0.3592 0.1569 0.0176  -0.0088 0.0350  325 TYR A CA  
2739 C C   . TYR A 323 ? 0.1687 0.3600 0.1593 0.0253  -0.0063 0.0421  325 TYR A C   
2740 O O   . TYR A 323 ? 0.2071 0.4056 0.1948 0.0266  -0.0063 0.0435  325 TYR A O   
2741 C CB  . TYR A 323 ? 0.2006 0.4155 0.1958 0.0184  -0.0105 0.0368  325 TYR A CB  
2742 C CG  . TYR A 323 ? 0.1970 0.4206 0.1941 0.0101  -0.0130 0.0296  325 TYR A CG  
2743 C CD1 . TYR A 323 ? 0.2121 0.4266 0.2081 0.0026  -0.0135 0.0220  325 TYR A CD1 
2744 C CD2 . TYR A 323 ? 0.2261 0.4673 0.2263 0.0098  -0.0146 0.0307  325 TYR A CD2 
2745 C CE1 . TYR A 323 ? 0.2104 0.4320 0.2077 -0.0051 -0.0152 0.0155  325 TYR A CE1 
2746 C CE2 . TYR A 323 ? 0.2921 0.5414 0.2944 0.0018  -0.0165 0.0241  325 TYR A CE2 
2747 C CZ  . TYR A 323 ? 0.2936 0.5327 0.2941 -0.0058 -0.0167 0.0164  325 TYR A CZ  
2748 O OH  . TYR A 323 ? 0.2581 0.5045 0.2603 -0.0139 -0.0181 0.0099  325 TYR A OH  
2749 N N   . THR A 324 ? 0.2218 0.4013 0.2134 0.0304  -0.0038 0.0467  326 THR A N   
2750 C CA  . THR A 324 ? 0.2389 0.4137 0.2280 0.0376  -0.0008 0.0536  326 THR A CA  
2751 C C   . THR A 324 ? 0.2262 0.3856 0.2139 0.0361  0.0007  0.0518  326 THR A C   
2752 O O   . THR A 324 ? 0.2790 0.4356 0.2643 0.0410  0.0033  0.0568  326 THR A O   
2753 C CB  . THR A 324 ? 0.2843 0.4517 0.2742 0.0437  0.0018  0.0593  326 THR A CB  
2754 O OG1 . THR A 324 ? 0.3767 0.5423 0.3637 0.0511  0.0051  0.0664  326 THR A OG1 
2755 C CG2 . THR A 324 ? 0.2978 0.4452 0.2888 0.0411  0.0026  0.0561  326 THR A CG2 
2756 N N   . VAL A 325 ? 0.2223 0.3722 0.2115 0.0296  -0.0006 0.0452  327 VAL A N   
2757 C CA  . VAL A 325 ? 0.2174 0.3535 0.2063 0.0281  0.0007  0.0434  327 VAL A CA  
2758 C C   . VAL A 325 ? 0.2005 0.3450 0.1868 0.0269  0.0006  0.0424  327 VAL A C   
2759 O O   . VAL A 325 ? 0.2114 0.3665 0.1968 0.0225  -0.0017 0.0380  327 VAL A O   
2760 C CB  . VAL A 325 ? 0.1838 0.3082 0.1751 0.0220  -0.0007 0.0369  327 VAL A CB  
2761 C CG1 . VAL A 325 ? 0.2065 0.3194 0.1982 0.0199  0.0003  0.0345  327 VAL A CG1 
2762 C CG2 . VAL A 325 ? 0.2917 0.4057 0.2845 0.0237  -0.0002 0.0382  327 VAL A CG2 
2763 N N   . VAL A 326 ? 0.2178 0.3569 0.2024 0.0306  0.0034  0.0464  328 VAL A N   
2764 C CA  . VAL A 326 ? 0.2500 0.3957 0.2316 0.0301  0.0039  0.0459  328 VAL A CA  
2765 C C   . VAL A 326 ? 0.2271 0.3672 0.2098 0.0232  0.0028  0.0385  328 VAL A C   
2766 O O   . VAL A 326 ? 0.2371 0.3629 0.2228 0.0212  0.0036  0.0364  328 VAL A O   
2767 C CB  . VAL A 326 ? 0.3398 0.4786 0.3198 0.0354  0.0079  0.0518  328 VAL A CB  
2768 C CG1 . VAL A 326 ? 0.3985 0.5417 0.3754 0.0341  0.0087  0.0505  328 VAL A CG1 
2769 C CG2 . VAL A 326 ? 0.4385 0.5838 0.4163 0.0428  0.0096  0.0596  328 VAL A CG2 
2770 N N   . LYS A 327 ? 0.2742 0.4258 0.2543 0.0196  0.0010  0.0346  329 LYS A N   
2771 C CA  . LYS A 327 ? 0.3589 0.5053 0.3393 0.0133  0.0005  0.0276  329 LYS A CA  
2772 C C   . LYS A 327 ? 0.5839 0.7271 0.5620 0.0142  0.0031  0.0283  329 LYS A C   
2773 O O   . LYS A 327 ? 0.5832 0.7328 0.5579 0.0187  0.0046  0.0333  329 LYS A O   
2774 C CB  . LYS A 327 ? 0.4615 0.6200 0.4398 0.0080  -0.0023 0.0221  329 LYS A CB  
2775 C CG  . LYS A 327 ? 0.5363 0.6980 0.5174 0.0063  -0.0045 0.0208  329 LYS A CG  
2776 C CD  . LYS A 327 ? 0.4366 0.5820 0.4220 0.0057  -0.0040 0.0198  329 LYS A CD  
2777 C CE  . LYS A 327 ? 0.3236 0.4720 0.3113 0.0044  -0.0058 0.0189  329 LYS A CE  
2778 N NZ  . LYS A 327 ? 0.3293 0.4915 0.3167 0.0090  -0.0064 0.0243  329 LYS A NZ  
2779 N N   . ASP A 328 ? 0.6835 0.8164 0.6634 0.0102  0.0039  0.0236  330 ASP A N   
2780 C CA  . ASP A 328 ? 0.7577 0.8857 0.7365 0.0106  0.0068  0.0238  330 ASP A CA  
2781 C C   . ASP A 328 ? 0.7065 0.8427 0.6802 0.0070  0.0066  0.0193  330 ASP A C   
2782 O O   . ASP A 328 ? 0.6814 0.8311 0.6503 0.0078  0.0054  0.0202  330 ASP A O   
2783 C CB  . ASP A 328 ? 0.8385 0.9512 0.8227 0.0086  0.0079  0.0215  330 ASP A CB  
2784 C CG  . ASP A 328 ? 0.9294 1.0332 0.9180 0.0112  0.0077  0.0249  330 ASP A CG  
2785 O OD1 . ASP A 328 ? 0.9541 1.0501 0.9451 0.0139  0.0101  0.0285  330 ASP A OD1 
2786 O OD2 . ASP A 328 ? 0.9550 1.0597 0.9445 0.0103  0.0053  0.0238  330 ASP A OD2 
# 
