data_9I11
# 
_entry.id   9I11 
# 
_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   9I11         pdb_00009i11 10.2210/pdb9i11/pdb 
WWPDB D_1292144688 ?            ?                   
# 
_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                        9I11 
_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 
PDB '9I10 contains the same protein complexed with a similar inhibitor' 9I10 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 'SULFATE ION'                                                                                               
96.063    4   ?        ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                                                                              
62.068    2   ?        ? ? ? 
4 non-polymer syn '(2~{Z},5~{Z})-2-(3-hydroxyphenyl)imino-5-[(4-methoxy-3-oxidanyl-phenyl)methylidene]-1,3-thiazolidin-4-one' 
342.369   1   ?        ? ? ? 
5 water       nat water                                                                                                       
18.015    253 ?        ? ? ? 
# 
_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 'SULFATE ION'                                                                                               SO4   
3 1,2-ETHANEDIOL                                                                                              EDO   
4 '(2~{Z},5~{Z})-2-(3-hydroxyphenyl)imino-5-[(4-methoxy-3-oxidanyl-phenyl)methylidene]-1,3-thiazolidin-4-one' A1IYW 
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 
A1IYW non-polymer         . 
'(2~{Z},5~{Z})-2-(3-hydroxyphenyl)imino-5-[(4-methoxy-3-oxidanyl-phenyl)methylidene]-1,3-thiazolidin-4-one' ?                 
'C17 H14 N2 O4 S' 342.369 
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        A1IYW 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IYW 
_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 SO4   1   401 401  SO4   SO4 A . 
C 2 SO4   1   402 501  SO4   SO4 A . 
D 2 SO4   1   403 601  SO4   SO4 A . 
E 3 EDO   1   404 701  EDO   EDO A . 
F 3 EDO   1   405 801  EDO   EDO A . 
G 4 A1IYW 1   406 901  A1IYW C16 A . 
H 2 SO4   1   407 1001 SO4   SO4 A . 
I 5 HOH   1   501 176  HOH   HOH A . 
I 5 HOH   2   502 221  HOH   HOH A . 
I 5 HOH   3   503 252  HOH   HOH A . 
I 5 HOH   4   504 21   HOH   HOH A . 
I 5 HOH   5   505 102  HOH   HOH A . 
I 5 HOH   6   506 193  HOH   HOH A . 
I 5 HOH   7   507 168  HOH   HOH A . 
I 5 HOH   8   508 126  HOH   HOH A . 
I 5 HOH   9   509 172  HOH   HOH A . 
I 5 HOH   10  510 175  HOH   HOH A . 
I 5 HOH   11  511 174  HOH   HOH A . 
I 5 HOH   12  512 173  HOH   HOH A . 
I 5 HOH   13  513 229  HOH   HOH A . 
I 5 HOH   14  514 129  HOH   HOH A . 
I 5 HOH   15  515 75   HOH   HOH A . 
I 5 HOH   16  516 139  HOH   HOH A . 
I 5 HOH   17  517 209  HOH   HOH A . 
I 5 HOH   18  518 247  HOH   HOH A . 
I 5 HOH   19  519 62   HOH   HOH A . 
I 5 HOH   20  520 67   HOH   HOH A . 
I 5 HOH   21  521 124  HOH   HOH A . 
I 5 HOH   22  522 246  HOH   HOH A . 
I 5 HOH   23  523 93   HOH   HOH A . 
I 5 HOH   24  524 150  HOH   HOH A . 
I 5 HOH   25  525 171  HOH   HOH A . 
I 5 HOH   26  526 110  HOH   HOH A . 
I 5 HOH   27  527 118  HOH   HOH A . 
I 5 HOH   28  528 167  HOH   HOH A . 
I 5 HOH   29  529 123  HOH   HOH A . 
I 5 HOH   30  530 33   HOH   HOH A . 
I 5 HOH   31  531 22   HOH   HOH A . 
I 5 HOH   32  532 63   HOH   HOH A . 
I 5 HOH   33  533 131  HOH   HOH A . 
I 5 HOH   34  534 157  HOH   HOH A . 
I 5 HOH   35  535 232  HOH   HOH A . 
I 5 HOH   36  536 236  HOH   HOH A . 
I 5 HOH   37  537 42   HOH   HOH A . 
I 5 HOH   38  538 30   HOH   HOH A . 
I 5 HOH   39  539 34   HOH   HOH A . 
I 5 HOH   40  540 166  HOH   HOH A . 
I 5 HOH   41  541 194  HOH   HOH A . 
I 5 HOH   42  542 207  HOH   HOH A . 
I 5 HOH   43  543 11   HOH   HOH A . 
I 5 HOH   44  544 86   HOH   HOH A . 
I 5 HOH   45  545 56   HOH   HOH A . 
I 5 HOH   46  546 44   HOH   HOH A . 
I 5 HOH   47  547 19   HOH   HOH A . 
I 5 HOH   48  548 203  HOH   HOH A . 
I 5 HOH   49  549 177  HOH   HOH A . 
I 5 HOH   50  550 14   HOH   HOH A . 
I 5 HOH   51  551 37   HOH   HOH A . 
I 5 HOH   52  552 111  HOH   HOH A . 
I 5 HOH   53  553 81   HOH   HOH A . 
I 5 HOH   54  554 16   HOH   HOH A . 
I 5 HOH   55  555 20   HOH   HOH A . 
I 5 HOH   56  556 101  HOH   HOH A . 
I 5 HOH   57  557 97   HOH   HOH A . 
I 5 HOH   58  558 183  HOH   HOH A . 
I 5 HOH   59  559 130  HOH   HOH A . 
I 5 HOH   60  560 187  HOH   HOH A . 
I 5 HOH   61  561 88   HOH   HOH A . 
I 5 HOH   62  562 98   HOH   HOH A . 
I 5 HOH   63  563 32   HOH   HOH A . 
I 5 HOH   64  564 223  HOH   HOH A . 
I 5 HOH   65  565 89   HOH   HOH A . 
I 5 HOH   66  566 26   HOH   HOH A . 
I 5 HOH   67  567 23   HOH   HOH A . 
I 5 HOH   68  568 40   HOH   HOH A . 
I 5 HOH   69  569 60   HOH   HOH A . 
I 5 HOH   70  570 84   HOH   HOH A . 
I 5 HOH   71  571 51   HOH   HOH A . 
I 5 HOH   72  572 162  HOH   HOH A . 
I 5 HOH   73  573 18   HOH   HOH A . 
I 5 HOH   74  574 179  HOH   HOH A . 
I 5 HOH   75  575 6    HOH   HOH A . 
I 5 HOH   76  576 159  HOH   HOH A . 
I 5 HOH   77  577 184  HOH   HOH A . 
I 5 HOH   78  578 17   HOH   HOH A . 
I 5 HOH   79  579 4    HOH   HOH A . 
I 5 HOH   80  580 169  HOH   HOH A . 
I 5 HOH   81  581 113  HOH   HOH A . 
I 5 HOH   82  582 180  HOH   HOH A . 
I 5 HOH   83  583 155  HOH   HOH A . 
I 5 HOH   84  584 77   HOH   HOH A . 
I 5 HOH   85  585 64   HOH   HOH A . 
I 5 HOH   86  586 69   HOH   HOH A . 
I 5 HOH   87  587 8    HOH   HOH A . 
I 5 HOH   88  588 73   HOH   HOH A . 
I 5 HOH   89  589 55   HOH   HOH A . 
I 5 HOH   90  590 7    HOH   HOH A . 
I 5 HOH   91  591 147  HOH   HOH A . 
I 5 HOH   92  592 132  HOH   HOH A . 
I 5 HOH   93  593 39   HOH   HOH A . 
I 5 HOH   94  594 35   HOH   HOH A . 
I 5 HOH   95  595 83   HOH   HOH A . 
I 5 HOH   96  596 46   HOH   HOH A . 
I 5 HOH   97  597 135  HOH   HOH A . 
I 5 HOH   98  598 25   HOH   HOH A . 
I 5 HOH   99  599 224  HOH   HOH A . 
I 5 HOH   100 600 204  HOH   HOH A . 
I 5 HOH   101 601 105  HOH   HOH A . 
I 5 HOH   102 602 29   HOH   HOH A . 
I 5 HOH   103 603 178  HOH   HOH A . 
I 5 HOH   104 604 231  HOH   HOH A . 
I 5 HOH   105 605 182  HOH   HOH A . 
I 5 HOH   106 606 114  HOH   HOH A . 
I 5 HOH   107 607 145  HOH   HOH A . 
I 5 HOH   108 608 13   HOH   HOH A . 
I 5 HOH   109 609 234  HOH   HOH A . 
I 5 HOH   110 610 142  HOH   HOH A . 
I 5 HOH   111 611 146  HOH   HOH A . 
I 5 HOH   112 612 10   HOH   HOH A . 
I 5 HOH   113 613 1    HOH   HOH A . 
I 5 HOH   114 614 47   HOH   HOH A . 
I 5 HOH   115 615 90   HOH   HOH A . 
I 5 HOH   116 616 12   HOH   HOH A . 
I 5 HOH   117 617 127  HOH   HOH A . 
I 5 HOH   118 618 3    HOH   HOH A . 
I 5 HOH   119 619 38   HOH   HOH A . 
I 5 HOH   120 620 141  HOH   HOH A . 
I 5 HOH   121 621 48   HOH   HOH A . 
I 5 HOH   122 622 5    HOH   HOH A . 
I 5 HOH   123 623 196  HOH   HOH A . 
I 5 HOH   124 624 143  HOH   HOH A . 
I 5 HOH   125 625 158  HOH   HOH A . 
I 5 HOH   126 626 82   HOH   HOH A . 
I 5 HOH   127 627 91   HOH   HOH A . 
I 5 HOH   128 628 225  HOH   HOH A . 
I 5 HOH   129 629 228  HOH   HOH A . 
I 5 HOH   130 630 96   HOH   HOH A . 
I 5 HOH   131 631 186  HOH   HOH A . 
I 5 HOH   132 632 245  HOH   HOH A . 
I 5 HOH   133 633 227  HOH   HOH A . 
I 5 HOH   134 634 9    HOH   HOH A . 
I 5 HOH   135 635 104  HOH   HOH A . 
I 5 HOH   136 636 74   HOH   HOH A . 
I 5 HOH   137 637 27   HOH   HOH A . 
I 5 HOH   138 638 70   HOH   HOH A . 
I 5 HOH   139 639 85   HOH   HOH A . 
I 5 HOH   140 640 125  HOH   HOH A . 
I 5 HOH   141 641 226  HOH   HOH A . 
I 5 HOH   142 642 15   HOH   HOH A . 
I 5 HOH   143 643 214  HOH   HOH A . 
I 5 HOH   144 644 163  HOH   HOH A . 
I 5 HOH   145 645 106  HOH   HOH A . 
I 5 HOH   146 646 161  HOH   HOH A . 
I 5 HOH   147 647 230  HOH   HOH A . 
I 5 HOH   148 648 112  HOH   HOH A . 
I 5 HOH   149 649 28   HOH   HOH A . 
I 5 HOH   150 650 24   HOH   HOH A . 
I 5 HOH   151 651 36   HOH   HOH A . 
I 5 HOH   152 652 53   HOH   HOH A . 
I 5 HOH   153 653 72   HOH   HOH A . 
I 5 HOH   154 654 66   HOH   HOH A . 
I 5 HOH   155 655 149  HOH   HOH A . 
I 5 HOH   156 656 181  HOH   HOH A . 
I 5 HOH   157 657 103  HOH   HOH A . 
I 5 HOH   158 658 137  HOH   HOH A . 
I 5 HOH   159 659 117  HOH   HOH A . 
I 5 HOH   160 660 2    HOH   HOH A . 
I 5 HOH   161 661 238  HOH   HOH A . 
I 5 HOH   162 662 71   HOH   HOH A . 
I 5 HOH   163 663 249  HOH   HOH A . 
I 5 HOH   164 664 218  HOH   HOH A . 
I 5 HOH   165 665 115  HOH   HOH A . 
I 5 HOH   166 666 78   HOH   HOH A . 
I 5 HOH   167 667 119  HOH   HOH A . 
I 5 HOH   168 668 41   HOH   HOH A . 
I 5 HOH   169 669 144  HOH   HOH A . 
I 5 HOH   170 670 58   HOH   HOH A . 
I 5 HOH   171 671 189  HOH   HOH A . 
I 5 HOH   172 672 198  HOH   HOH A . 
I 5 HOH   173 673 206  HOH   HOH A . 
I 5 HOH   174 674 138  HOH   HOH A . 
I 5 HOH   175 675 201  HOH   HOH A . 
I 5 HOH   176 676 65   HOH   HOH A . 
I 5 HOH   177 677 31   HOH   HOH A . 
I 5 HOH   178 678 45   HOH   HOH A . 
I 5 HOH   179 679 208  HOH   HOH A . 
I 5 HOH   180 680 54   HOH   HOH A . 
I 5 HOH   181 681 156  HOH   HOH A . 
I 5 HOH   182 682 107  HOH   HOH A . 
I 5 HOH   183 683 100  HOH   HOH A . 
I 5 HOH   184 684 59   HOH   HOH A . 
I 5 HOH   185 685 237  HOH   HOH A . 
I 5 HOH   186 686 151  HOH   HOH A . 
I 5 HOH   187 687 50   HOH   HOH A . 
I 5 HOH   188 688 170  HOH   HOH A . 
I 5 HOH   189 689 152  HOH   HOH A . 
I 5 HOH   190 690 191  HOH   HOH A . 
I 5 HOH   191 691 43   HOH   HOH A . 
I 5 HOH   192 692 80   HOH   HOH A . 
I 5 HOH   193 693 153  HOH   HOH A . 
I 5 HOH   194 694 205  HOH   HOH A . 
I 5 HOH   195 695 79   HOH   HOH A . 
I 5 HOH   196 696 87   HOH   HOH A . 
I 5 HOH   197 697 188  HOH   HOH A . 
I 5 HOH   198 698 76   HOH   HOH A . 
I 5 HOH   199 699 216  HOH   HOH A . 
I 5 HOH   200 700 133  HOH   HOH A . 
I 5 HOH   201 701 243  HOH   HOH A . 
I 5 HOH   202 702 233  HOH   HOH A . 
I 5 HOH   203 703 240  HOH   HOH A . 
I 5 HOH   204 704 212  HOH   HOH A . 
I 5 HOH   205 705 211  HOH   HOH A . 
I 5 HOH   206 706 195  HOH   HOH A . 
I 5 HOH   207 707 108  HOH   HOH A . 
I 5 HOH   208 708 253  HOH   HOH A . 
I 5 HOH   209 709 61   HOH   HOH A . 
I 5 HOH   210 710 235  HOH   HOH A . 
I 5 HOH   211 711 200  HOH   HOH A . 
I 5 HOH   212 712 92   HOH   HOH A . 
I 5 HOH   213 713 242  HOH   HOH A . 
I 5 HOH   214 714 222  HOH   HOH A . 
I 5 HOH   215 715 210  HOH   HOH A . 
I 5 HOH   216 716 219  HOH   HOH A . 
I 5 HOH   217 717 121  HOH   HOH A . 
I 5 HOH   218 718 57   HOH   HOH A . 
I 5 HOH   219 719 241  HOH   HOH A . 
I 5 HOH   220 720 239  HOH   HOH A . 
I 5 HOH   221 721 250  HOH   HOH A . 
I 5 HOH   222 722 251  HOH   HOH A . 
I 5 HOH   223 723 185  HOH   HOH A . 
I 5 HOH   224 724 136  HOH   HOH A . 
I 5 HOH   225 725 52   HOH   HOH A . 
I 5 HOH   226 726 213  HOH   HOH A . 
I 5 HOH   227 727 215  HOH   HOH A . 
I 5 HOH   228 728 49   HOH   HOH A . 
I 5 HOH   229 729 217  HOH   HOH A . 
I 5 HOH   230 730 202  HOH   HOH A . 
I 5 HOH   231 731 140  HOH   HOH A . 
I 5 HOH   232 732 165  HOH   HOH A . 
I 5 HOH   233 733 95   HOH   HOH A . 
I 5 HOH   234 734 190  HOH   HOH A . 
I 5 HOH   235 735 120  HOH   HOH A . 
I 5 HOH   236 736 154  HOH   HOH A . 
I 5 HOH   237 737 248  HOH   HOH A . 
I 5 HOH   238 738 199  HOH   HOH A . 
I 5 HOH   239 739 68   HOH   HOH A . 
I 5 HOH   240 740 148  HOH   HOH A . 
I 5 HOH   241 741 122  HOH   HOH A . 
I 5 HOH   242 742 160  HOH   HOH A . 
I 5 HOH   243 743 109  HOH   HOH A . 
I 5 HOH   244 744 220  HOH   HOH A . 
I 5 HOH   245 745 164  HOH   HOH A . 
I 5 HOH   246 746 244  HOH   HOH A . 
I 5 HOH   247 747 192  HOH   HOH A . 
I 5 HOH   248 748 134  HOH   HOH A . 
I 5 HOH   249 749 197  HOH   HOH A . 
I 5 HOH   250 750 116  HOH   HOH A . 
I 5 HOH   251 751 99   HOH   HOH A . 
I 5 HOH   252 752 128  HOH   HOH A . 
I 5 HOH   253 753 94   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                   111.59 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9I11 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.484 
_cell.length_a_esd                 ? 
_cell.length_b                     46.630 
_cell.length_b_esd                 ? 
_cell.length_c                     63.303 
_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                         9I11 
_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                   9I11 
_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             2.04 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.77 
_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                                       9I11 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.60 
_reflns.d_resolution_low                               58.86 
_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                                     41951 
_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                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.93 
_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                                0.047 
_reflns.pdbx_Rpim_I_all                                0.019 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       255811 
_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                              0.043 
_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                                    1.60 
_reflns_shell.d_res_low                                     1.63 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           9943 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2063 
_reflns_shell.percent_possible_obs                          98.5 
_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                               4.8 
_reflns_shell.pdbx_chi_squared                              0.86 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.5 
_reflns_shell.pdbx_Rrim_I_all                               0.639 
_reflns_shell.pdbx_Rpim_I_all                               0.285 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.796 
_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                                  0.567 
_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                                 9I11 
_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                            1.600 
_refine.ls_d_res_low                             36.550 
_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                     41924 
_refine.ls_number_reflns_R_free                  2054 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.60 
_refine.ls_percent_reflns_R_free                 4.90 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1651 
_refine.ls_R_factor_R_free                       0.1959 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1635 
_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                          1.35 
_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                 19.82 
_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.details                          ? 
_refine_hist.d_res_high                       1.600 
_refine_hist.d_res_low                        36.550 
_refine_hist.number_atoms_solvent             253 
_refine_hist.number_atoms_total               3078 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2773 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 2921 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.848  ? 3956 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.926 ? 1735 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055  ? 405  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 504  ? 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' 1.6000 1.6372 . . 128 2610 99.00  . . . . 0.2285 . . . . . . . . . . . 0.2805 
'X-RAY DIFFRACTION' 1.6372 1.6782 . . 139 2655 100.00 . . . . 0.2074 . . . . . . . . . . . 0.2290 
'X-RAY DIFFRACTION' 1.6782 1.7236 . . 141 2653 100.00 . . . . 0.2013 . . . . . . . . . . . 0.2582 
'X-RAY DIFFRACTION' 1.7236 1.7743 . . 138 2641 100.00 . . . . 0.1889 . . . . . . . . . . . 0.2165 
'X-RAY DIFFRACTION' 1.7743 1.8315 . . 144 2622 99.00  . . . . 0.1855 . . . . . . . . . . . 0.2284 
'X-RAY DIFFRACTION' 1.8315 1.8970 . . 148 2609 100.00 . . . . 0.1735 . . . . . . . . . . . 0.2177 
'X-RAY DIFFRACTION' 1.8970 1.9729 . . 134 2684 100.00 . . . . 0.1778 . . . . . . . . . . . 0.2123 
'X-RAY DIFFRACTION' 1.9729 2.0627 . . 136 2626 100.00 . . . . 0.1652 . . . . . . . . . . . 0.1986 
'X-RAY DIFFRACTION' 2.0627 2.1715 . . 138 2659 99.00  . . . . 0.1641 . . . . . . . . . . . 0.1997 
'X-RAY DIFFRACTION' 2.1715 2.3075 . . 128 2662 100.00 . . . . 0.1699 . . . . . . . . . . . 0.1722 
'X-RAY DIFFRACTION' 2.3075 2.4856 . . 143 2646 100.00 . . . . 0.1658 . . . . . . . . . . . 0.2009 
'X-RAY DIFFRACTION' 2.4856 2.7357 . . 119 2702 100.00 . . . . 0.1728 . . . . . . . . . . . 0.2257 
'X-RAY DIFFRACTION' 2.7357 3.1314 . . 147 2666 100.00 . . . . 0.1682 . . . . . . . . . . . 0.1954 
'X-RAY DIFFRACTION' 3.1314 3.9444 . . 132 2695 100.00 . . . . 0.1481 . . . . . . . . . . . 0.1753 
'X-RAY DIFFRACTION' 3.9444 36.55  . . 139 2740 99.00  . . . . 0.1476 . . . . . . . . . . . 0.1816 
# 
_struct.entry_id                     9I11 
_struct.title                        'Human protein kinase CK2 alpha in complex with TN16' 
_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        9I11 
_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 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I 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              9I11 
_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)' 1200  ? 
1 MORE         -48   ? 
1 'SSA (A^2)'  15510 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_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 ? GLN A 124 ? ASP A 120 GLN A 126 1 ? 7  
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 HIS A 164 ? ARG A 167 ? HIS A 166 ARG A 169 5 ? 4  
HELX_P HELX_P10 AB1 ASP A 173 ? ALA A 177 ? ASP A 175 ALA A 179 5 ? 5  
HELX_P HELX_P11 AB2 SER A 192 ? LYS A 196 ? SER A 194 LYS A 198 5 ? 5  
HELX_P HELX_P12 AB3 GLY A 197 ? VAL A 202 ? GLY A 199 VAL A 204 1 ? 6  
HELX_P HELX_P13 AB4 TYR A 209 ? ARG A 226 ? TYR A 211 ARG A 228 1 ? 18 
HELX_P HELX_P14 AB5 ASP A 235 ? GLY A 248 ? ASP A 237 GLY A 250 1 ? 14 
HELX_P HELX_P15 AB6 GLY A 248 ? TYR A 259 ? GLY A 250 TYR A 261 1 ? 12 
HELX_P HELX_P16 AB7 ASP A 264 ? ILE A 270 ? ASP A 266 ILE A 272 5 ? 7  
HELX_P HELX_P17 AB8 ARG A 278 ? VAL A 283 ? ARG A 280 VAL A 285 5 ? 6  
HELX_P HELX_P18 AB9 ASN A 287 ? VAL A 291 ? ASN A 289 VAL A 293 5 ? 5  
HELX_P HELX_P19 AC1 SER A 292 ? LEU A 303 ? SER A 294 LEU A 305 1 ? 12 
HELX_P HELX_P20 AC2 ASP A 306 ? ARG A 310 ? ASP A 308 ARG A 312 5 ? 5  
HELX_P HELX_P21 AC3 THR A 312 ? GLU A 318 ? THR A 314 GLU A 320 1 ? 7  
HELX_P HELX_P22 AC4 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       -3.69 
# 
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 VAL A 40  ? N VAL A 42  O GLU A 53  ? O GLU A 55  
AA1 2 3 N PHE A 52  ? N PHE A 54  O VAL A 65  ? O VAL A 67  
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                   9I11 
_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 GLN A 126 ? ? -68.98  0.12   
2 1 ASP A 156 ? ? -148.60 47.10  
3 1 ASP A 175 ? ? 60.82   68.71  
4 1 ALA A 193 ? ? 62.56   156.33 
5 1 MET A 208 ? ? -93.91  58.54  
6 1 HIS A 234 ? ? -107.88 72.91  
# 
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 18.8826 -18.4065 -46.2684 0.2022 ? 0.0089 ? 0.0060  ? 0.2345 ? -0.0633 ? 0.2750 ? 0.5395 ? 0.1877  
? 0.0956  ? 0.0708 ? -0.0282 ? 0.4269 ? -0.0573 ? 0.0393 ? -0.1180 ? 0.0350 ? 0.0208 ? -0.1148 ? 0.1078  ? 0.1464  ? -0.0000 ? 
2 'X-RAY DIFFRACTION' ? refined 17.3213 -11.9897 -46.9551 0.2049 ? 0.0200 ? -0.0359 ? 0.2114 ? -0.0364 ? 0.2481 ? 0.3037 ? 0.2139  
? -0.0359 ? 0.1247 ? -0.0287 ? 0.4022 ? -0.0842 ? 0.0251 ? 0.0366  ? 0.1379 ? 0.0662 ? -0.1722 ? -0.1723 ? 0.0934  ? -0.0001 ? 
3 'X-RAY DIFFRACTION' ? refined -3.8553 -13.0178 -41.7912 0.1709 ? 0.0160 ? -0.0066 ? 0.1598 ? -0.0050 ? 0.1543 ? 0.9229 ? -0.0159 
? -0.4666 ? 0.3803 ? -0.0194 ? 0.7512 ? -0.0016 ? 0.1268 ? 0.0036  ? 0.0634 ? 0.0330 ? -0.0459 ? 0.0016  ? -0.1096 ? 0.0000  ? 
# 
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 74 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 75 through 129 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 130 through 330 )
;
# 
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 
A1IYW C21  C Y N 1   
A1IYW C15  C N N 2   
A1IYW C10  C N N 3   
A1IYW C13  C N N 4   
A1IYW C01  C N N 5   
A1IYW C03  C Y N 6   
A1IYW C04  C Y N 7   
A1IYW C06  C Y N 8   
A1IYW C07  C Y N 9   
A1IYW C08  C Y N 10  
A1IYW C09  C Y N 11  
A1IYW C11  C N N 12  
A1IYW C18  C Y N 13  
A1IYW C19  C Y N 14  
A1IYW C20  C Y N 15  
A1IYW C22  C Y N 16  
A1IYW C23  C Y N 17  
A1IYW N14  N N N 18  
A1IYW N17  N N N 19  
A1IYW O02  O N N 20  
A1IYW O05  O N N 21  
A1IYW O16  O N N 22  
A1IYW O24  O N N 23  
A1IYW S12  S N N 24  
A1IYW H1   H N N 25  
A1IYW H2   H N N 26  
A1IYW H3   H N N 27  
A1IYW H4   H N N 28  
A1IYW H5   H N N 29  
A1IYW H6   H N N 30  
A1IYW H7   H N N 31  
A1IYW H8   H N N 32  
A1IYW H9   H N N 33  
A1IYW H10  H N N 34  
A1IYW H11  H N N 35  
A1IYW H13  H N N 36  
A1IYW H14  H N N 37  
A1IYW H12  H N N 38  
ALA   N    N N N 39  
ALA   CA   C N S 40  
ALA   C    C N N 41  
ALA   O    O N N 42  
ALA   CB   C N N 43  
ALA   OXT  O N N 44  
ALA   H    H N N 45  
ALA   H2   H N N 46  
ALA   HA   H N N 47  
ALA   HB1  H N N 48  
ALA   HB2  H N N 49  
ALA   HB3  H N N 50  
ALA   HXT  H N N 51  
ARG   N    N N N 52  
ARG   CA   C N S 53  
ARG   C    C N N 54  
ARG   O    O N N 55  
ARG   CB   C N N 56  
ARG   CG   C N N 57  
ARG   CD   C N N 58  
ARG   NE   N N N 59  
ARG   CZ   C N N 60  
ARG   NH1  N N N 61  
ARG   NH2  N N N 62  
ARG   OXT  O N N 63  
ARG   H    H N N 64  
ARG   H2   H N N 65  
ARG   HA   H N N 66  
ARG   HB2  H N N 67  
ARG   HB3  H N N 68  
ARG   HG2  H N N 69  
ARG   HG3  H N N 70  
ARG   HD2  H N N 71  
ARG   HD3  H N N 72  
ARG   HE   H N N 73  
ARG   HH11 H N N 74  
ARG   HH12 H N N 75  
ARG   HH21 H N N 76  
ARG   HH22 H N N 77  
ARG   HXT  H N N 78  
ASN   N    N N N 79  
ASN   CA   C N S 80  
ASN   C    C N N 81  
ASN   O    O N N 82  
ASN   CB   C N N 83  
ASN   CG   C N N 84  
ASN   OD1  O N N 85  
ASN   ND2  N N N 86  
ASN   OXT  O N N 87  
ASN   H    H N N 88  
ASN   H2   H N N 89  
ASN   HA   H N N 90  
ASN   HB2  H N N 91  
ASN   HB3  H N N 92  
ASN   HD21 H N N 93  
ASN   HD22 H N N 94  
ASN   HXT  H N N 95  
ASP   N    N N N 96  
ASP   CA   C N S 97  
ASP   C    C N N 98  
ASP   O    O N N 99  
ASP   CB   C N N 100 
ASP   CG   C N N 101 
ASP   OD1  O N N 102 
ASP   OD2  O N N 103 
ASP   OXT  O N N 104 
ASP   H    H N N 105 
ASP   H2   H N N 106 
ASP   HA   H N N 107 
ASP   HB2  H N N 108 
ASP   HB3  H N N 109 
ASP   HD2  H N N 110 
ASP   HXT  H N N 111 
CYS   N    N N N 112 
CYS   CA   C N R 113 
CYS   C    C N N 114 
CYS   O    O N N 115 
CYS   CB   C N N 116 
CYS   SG   S N N 117 
CYS   OXT  O N N 118 
CYS   H    H N N 119 
CYS   H2   H N N 120 
CYS   HA   H N N 121 
CYS   HB2  H N N 122 
CYS   HB3  H N N 123 
CYS   HG   H N N 124 
CYS   HXT  H N N 125 
EDO   C1   C N N 126 
EDO   O1   O N N 127 
EDO   C2   C N N 128 
EDO   O2   O N N 129 
EDO   H11  H N N 130 
EDO   H12  H N N 131 
EDO   HO1  H N N 132 
EDO   H21  H N N 133 
EDO   H22  H N N 134 
EDO   HO2  H N N 135 
GLN   N    N N N 136 
GLN   CA   C N S 137 
GLN   C    C N N 138 
GLN   O    O N N 139 
GLN   CB   C N N 140 
GLN   CG   C N N 141 
GLN   CD   C N N 142 
GLN   OE1  O N N 143 
GLN   NE2  N N N 144 
GLN   OXT  O N N 145 
GLN   H    H N N 146 
GLN   H2   H N N 147 
GLN   HA   H N N 148 
GLN   HB2  H N N 149 
GLN   HB3  H N N 150 
GLN   HG2  H N N 151 
GLN   HG3  H N N 152 
GLN   HE21 H N N 153 
GLN   HE22 H N N 154 
GLN   HXT  H N N 155 
GLU   N    N N N 156 
GLU   CA   C N S 157 
GLU   C    C N N 158 
GLU   O    O N N 159 
GLU   CB   C N N 160 
GLU   CG   C N N 161 
GLU   CD   C N N 162 
GLU   OE1  O N N 163 
GLU   OE2  O N N 164 
GLU   OXT  O N N 165 
GLU   H    H N N 166 
GLU   H2   H N N 167 
GLU   HA   H N N 168 
GLU   HB2  H N N 169 
GLU   HB3  H N N 170 
GLU   HG2  H N N 171 
GLU   HG3  H N N 172 
GLU   HE2  H N N 173 
GLU   HXT  H N N 174 
GLY   N    N N N 175 
GLY   CA   C N N 176 
GLY   C    C N N 177 
GLY   O    O N N 178 
GLY   OXT  O N N 179 
GLY   H    H N N 180 
GLY   H2   H N N 181 
GLY   HA2  H N N 182 
GLY   HA3  H N N 183 
GLY   HXT  H N N 184 
HIS   N    N N N 185 
HIS   CA   C N S 186 
HIS   C    C N N 187 
HIS   O    O N N 188 
HIS   CB   C N N 189 
HIS   CG   C Y N 190 
HIS   ND1  N Y N 191 
HIS   CD2  C Y N 192 
HIS   CE1  C Y N 193 
HIS   NE2  N Y N 194 
HIS   OXT  O N N 195 
HIS   H    H N N 196 
HIS   H2   H N N 197 
HIS   HA   H N N 198 
HIS   HB2  H N N 199 
HIS   HB3  H N N 200 
HIS   HD1  H N N 201 
HIS   HD2  H N N 202 
HIS   HE1  H N N 203 
HIS   HE2  H N N 204 
HIS   HXT  H N N 205 
HOH   O    O N N 206 
HOH   H1   H N N 207 
HOH   H2   H N N 208 
ILE   N    N N N 209 
ILE   CA   C N S 210 
ILE   C    C N N 211 
ILE   O    O N N 212 
ILE   CB   C N S 213 
ILE   CG1  C N N 214 
ILE   CG2  C N N 215 
ILE   CD1  C N N 216 
ILE   OXT  O N N 217 
ILE   H    H N N 218 
ILE   H2   H N N 219 
ILE   HA   H N N 220 
ILE   HB   H N N 221 
ILE   HG12 H N N 222 
ILE   HG13 H N N 223 
ILE   HG21 H N N 224 
ILE   HG22 H N N 225 
ILE   HG23 H N N 226 
ILE   HD11 H N N 227 
ILE   HD12 H N N 228 
ILE   HD13 H N N 229 
ILE   HXT  H N N 230 
LEU   N    N N N 231 
LEU   CA   C N S 232 
LEU   C    C N N 233 
LEU   O    O N N 234 
LEU   CB   C N N 235 
LEU   CG   C N N 236 
LEU   CD1  C N N 237 
LEU   CD2  C N N 238 
LEU   OXT  O N N 239 
LEU   H    H N N 240 
LEU   H2   H N N 241 
LEU   HA   H N N 242 
LEU   HB2  H N N 243 
LEU   HB3  H N N 244 
LEU   HG   H N N 245 
LEU   HD11 H N N 246 
LEU   HD12 H N N 247 
LEU   HD13 H N N 248 
LEU   HD21 H N N 249 
LEU   HD22 H N N 250 
LEU   HD23 H N N 251 
LEU   HXT  H N N 252 
LYS   N    N N N 253 
LYS   CA   C N S 254 
LYS   C    C N N 255 
LYS   O    O N N 256 
LYS   CB   C N N 257 
LYS   CG   C N N 258 
LYS   CD   C N N 259 
LYS   CE   C N N 260 
LYS   NZ   N N N 261 
LYS   OXT  O N N 262 
LYS   H    H N N 263 
LYS   H2   H N N 264 
LYS   HA   H N N 265 
LYS   HB2  H N N 266 
LYS   HB3  H N N 267 
LYS   HG2  H N N 268 
LYS   HG3  H N N 269 
LYS   HD2  H N N 270 
LYS   HD3  H N N 271 
LYS   HE2  H N N 272 
LYS   HE3  H N N 273 
LYS   HZ1  H N N 274 
LYS   HZ2  H N N 275 
LYS   HZ3  H N N 276 
LYS   HXT  H N N 277 
MET   N    N N N 278 
MET   CA   C N S 279 
MET   C    C N N 280 
MET   O    O N N 281 
MET   CB   C N N 282 
MET   CG   C N N 283 
MET   SD   S N N 284 
MET   CE   C N N 285 
MET   OXT  O N N 286 
MET   H    H N N 287 
MET   H2   H N N 288 
MET   HA   H N N 289 
MET   HB2  H N N 290 
MET   HB3  H N N 291 
MET   HG2  H N N 292 
MET   HG3  H N N 293 
MET   HE1  H N N 294 
MET   HE2  H N N 295 
MET   HE3  H N N 296 
MET   HXT  H N N 297 
PHE   N    N N N 298 
PHE   CA   C N S 299 
PHE   C    C N N 300 
PHE   O    O N N 301 
PHE   CB   C N N 302 
PHE   CG   C Y N 303 
PHE   CD1  C Y N 304 
PHE   CD2  C Y N 305 
PHE   CE1  C Y N 306 
PHE   CE2  C Y N 307 
PHE   CZ   C Y N 308 
PHE   OXT  O N N 309 
PHE   H    H N N 310 
PHE   H2   H N N 311 
PHE   HA   H N N 312 
PHE   HB2  H N N 313 
PHE   HB3  H N N 314 
PHE   HD1  H N N 315 
PHE   HD2  H N N 316 
PHE   HE1  H N N 317 
PHE   HE2  H N N 318 
PHE   HZ   H N N 319 
PHE   HXT  H N N 320 
PRO   N    N N N 321 
PRO   CA   C N S 322 
PRO   C    C N N 323 
PRO   O    O N N 324 
PRO   CB   C N N 325 
PRO   CG   C N N 326 
PRO   CD   C N N 327 
PRO   OXT  O N N 328 
PRO   H    H N N 329 
PRO   HA   H N N 330 
PRO   HB2  H N N 331 
PRO   HB3  H N N 332 
PRO   HG2  H N N 333 
PRO   HG3  H N N 334 
PRO   HD2  H N N 335 
PRO   HD3  H N N 336 
PRO   HXT  H N N 337 
SER   N    N N N 338 
SER   CA   C N S 339 
SER   C    C N N 340 
SER   O    O N N 341 
SER   CB   C N N 342 
SER   OG   O N N 343 
SER   OXT  O N N 344 
SER   H    H N N 345 
SER   H2   H N N 346 
SER   HA   H N N 347 
SER   HB2  H N N 348 
SER   HB3  H N N 349 
SER   HG   H N N 350 
SER   HXT  H N N 351 
SO4   S    S N N 352 
SO4   O1   O N N 353 
SO4   O2   O N N 354 
SO4   O3   O N N 355 
SO4   O4   O N N 356 
THR   N    N N N 357 
THR   CA   C N S 358 
THR   C    C N N 359 
THR   O    O N N 360 
THR   CB   C N R 361 
THR   OG1  O N N 362 
THR   CG2  C N N 363 
THR   OXT  O N N 364 
THR   H    H N N 365 
THR   H2   H N N 366 
THR   HA   H N N 367 
THR   HB   H N N 368 
THR   HG1  H N N 369 
THR   HG21 H N N 370 
THR   HG22 H N N 371 
THR   HG23 H N N 372 
THR   HXT  H N N 373 
TRP   N    N N N 374 
TRP   CA   C N S 375 
TRP   C    C N N 376 
TRP   O    O N N 377 
TRP   CB   C N N 378 
TRP   CG   C Y N 379 
TRP   CD1  C Y N 380 
TRP   CD2  C Y N 381 
TRP   NE1  N Y N 382 
TRP   CE2  C Y N 383 
TRP   CE3  C Y N 384 
TRP   CZ2  C Y N 385 
TRP   CZ3  C Y N 386 
TRP   CH2  C Y N 387 
TRP   OXT  O N N 388 
TRP   H    H N N 389 
TRP   H2   H N N 390 
TRP   HA   H N N 391 
TRP   HB2  H N N 392 
TRP   HB3  H N N 393 
TRP   HD1  H N N 394 
TRP   HE1  H N N 395 
TRP   HE3  H N N 396 
TRP   HZ2  H N N 397 
TRP   HZ3  H N N 398 
TRP   HH2  H N N 399 
TRP   HXT  H N N 400 
TYR   N    N N N 401 
TYR   CA   C N S 402 
TYR   C    C N N 403 
TYR   O    O N N 404 
TYR   CB   C N N 405 
TYR   CG   C Y N 406 
TYR   CD1  C Y N 407 
TYR   CD2  C Y N 408 
TYR   CE1  C Y N 409 
TYR   CE2  C Y N 410 
TYR   CZ   C Y N 411 
TYR   OH   O N N 412 
TYR   OXT  O N N 413 
TYR   H    H N N 414 
TYR   H2   H N N 415 
TYR   HA   H N N 416 
TYR   HB2  H N N 417 
TYR   HB3  H N N 418 
TYR   HD1  H N N 419 
TYR   HD2  H N N 420 
TYR   HE1  H N N 421 
TYR   HE2  H N N 422 
TYR   HH   H N N 423 
TYR   HXT  H N N 424 
VAL   N    N N N 425 
VAL   CA   C N S 426 
VAL   C    C N N 427 
VAL   O    O N N 428 
VAL   CB   C N N 429 
VAL   CG1  C N N 430 
VAL   CG2  C N N 431 
VAL   OXT  O N N 432 
VAL   H    H N N 433 
VAL   H2   H N N 434 
VAL   HA   H N N 435 
VAL   HB   H N N 436 
VAL   HG11 H N N 437 
VAL   HG12 H N N 438 
VAL   HG13 H N N 439 
VAL   HG21 H N N 440 
VAL   HG22 H N N 441 
VAL   HG23 H N N 442 
VAL   HXT  H N N 443 
# 
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 
A1IYW O05 C04  sing N N 1   
A1IYW C04 C06  doub Y N 2   
A1IYW C04 C03  sing Y N 3   
A1IYW O02 C03  sing N N 4   
A1IYW O02 C01  sing N N 5   
A1IYW C06 C07  sing Y N 6   
A1IYW C03 C09  doub Y N 7   
A1IYW C07 C10  sing N N 8   
A1IYW C07 C08  doub Y N 9   
A1IYW C09 C08  sing Y N 10  
A1IYW C10 C11  doub N Z 11  
A1IYW O16 C15  doub N N 12  
A1IYW C11 C15  sing N N 13  
A1IYW C11 S12  sing N N 14  
A1IYW C15 N14  sing N N 15  
A1IYW S12 C13  sing N N 16  
A1IYW N14 C13  sing N N 17  
A1IYW C13 N17  doub N N 18  
A1IYW N17 C18  sing N N 19  
A1IYW C18 C23  doub Y N 20  
A1IYW C18 C19  sing Y N 21  
A1IYW C23 C22  sing Y N 22  
A1IYW C19 C20  doub Y N 23  
A1IYW C22 C21  doub Y N 24  
A1IYW C20 C21  sing Y N 25  
A1IYW C20 O24  sing N N 26  
A1IYW C21 H1   sing N N 27  
A1IYW C10 H2   sing N N 28  
A1IYW C01 H3   sing N N 29  
A1IYW C01 H4   sing N N 30  
A1IYW C01 H5   sing N N 31  
A1IYW C06 H6   sing N N 32  
A1IYW C08 H7   sing N N 33  
A1IYW C09 H8   sing N N 34  
A1IYW C19 H9   sing N N 35  
A1IYW C22 H10  sing N N 36  
A1IYW C23 H11  sing N N 37  
A1IYW O05 H13  sing N N 38  
A1IYW O24 H14  sing N N 39  
A1IYW N14 H12  sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
EDO   C1  O1   sing N N 123 
EDO   C1  C2   sing N N 124 
EDO   C1  H11  sing N N 125 
EDO   C1  H12  sing N N 126 
EDO   O1  HO1  sing N N 127 
EDO   C2  O2   sing N N 128 
EDO   C2  H21  sing N N 129 
EDO   C2  H22  sing N N 130 
EDO   O2  HO2  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
SO4   S   O1   doub N N 339 
SO4   S   O2   doub N N 340 
SO4   S   O3   sing N N 341 
SO4   S   O4   sing N N 342 
THR   N   CA   sing N N 343 
THR   N   H    sing N N 344 
THR   N   H2   sing N N 345 
THR   CA  C    sing N N 346 
THR   CA  CB   sing N N 347 
THR   CA  HA   sing N N 348 
THR   C   O    doub N N 349 
THR   C   OXT  sing N N 350 
THR   CB  OG1  sing N N 351 
THR   CB  CG2  sing N N 352 
THR   CB  HB   sing N N 353 
THR   OG1 HG1  sing N N 354 
THR   CG2 HG21 sing N N 355 
THR   CG2 HG22 sing N N 356 
THR   CG2 HG23 sing N N 357 
THR   OXT HXT  sing N N 358 
TRP   N   CA   sing N N 359 
TRP   N   H    sing N N 360 
TRP   N   H2   sing N N 361 
TRP   CA  C    sing N N 362 
TRP   CA  CB   sing N N 363 
TRP   CA  HA   sing N N 364 
TRP   C   O    doub N N 365 
TRP   C   OXT  sing N N 366 
TRP   CB  CG   sing N N 367 
TRP   CB  HB2  sing N N 368 
TRP   CB  HB3  sing N N 369 
TRP   CG  CD1  doub Y N 370 
TRP   CG  CD2  sing Y N 371 
TRP   CD1 NE1  sing Y N 372 
TRP   CD1 HD1  sing N N 373 
TRP   CD2 CE2  doub Y N 374 
TRP   CD2 CE3  sing Y N 375 
TRP   NE1 CE2  sing Y N 376 
TRP   NE1 HE1  sing N N 377 
TRP   CE2 CZ2  sing Y N 378 
TRP   CE3 CZ3  doub Y N 379 
TRP   CE3 HE3  sing N N 380 
TRP   CZ2 CH2  doub Y N 381 
TRP   CZ2 HZ2  sing N N 382 
TRP   CZ3 CH2  sing Y N 383 
TRP   CZ3 HZ3  sing N N 384 
TRP   CH2 HH2  sing N N 385 
TRP   OXT HXT  sing N N 386 
TYR   N   CA   sing N N 387 
TYR   N   H    sing N N 388 
TYR   N   H2   sing N N 389 
TYR   CA  C    sing N N 390 
TYR   CA  CB   sing N N 391 
TYR   CA  HA   sing N N 392 
TYR   C   O    doub N N 393 
TYR   C   OXT  sing N N 394 
TYR   CB  CG   sing N N 395 
TYR   CB  HB2  sing N N 396 
TYR   CB  HB3  sing N N 397 
TYR   CG  CD1  doub Y N 398 
TYR   CG  CD2  sing Y N 399 
TYR   CD1 CE1  sing Y N 400 
TYR   CD1 HD1  sing N N 401 
TYR   CD2 CE2  doub Y N 402 
TYR   CD2 HD2  sing N N 403 
TYR   CE1 CZ   doub Y N 404 
TYR   CE1 HE1  sing N N 405 
TYR   CE2 CZ   sing Y N 406 
TYR   CE2 HE2  sing N N 407 
TYR   CZ  OH   sing N N 408 
TYR   OH  HH   sing N N 409 
TYR   OXT HXT  sing N N 410 
VAL   N   CA   sing N N 411 
VAL   N   H    sing N N 412 
VAL   N   H2   sing N N 413 
VAL   CA  C    sing N N 414 
VAL   CA  CB   sing N N 415 
VAL   CA  HA   sing N N 416 
VAL   C   O    doub N N 417 
VAL   C   OXT  sing N N 418 
VAL   CB  CG1  sing N N 419 
VAL   CB  CG2  sing N N 420 
VAL   CB  HB   sing N N 421 
VAL   CG1 HG11 sing N N 422 
VAL   CG1 HG12 sing N N 423 
VAL   CG1 HG13 sing N N 424 
VAL   CG2 HG21 sing N N 425 
VAL   CG2 HG22 sing N N 426 
VAL   CG2 HG23 sing N N 427 
VAL   OXT HXT  sing N N 428 
# 
_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                    9I11 
_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]   0.017099 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006768 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021445 
_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]   0.016990 
_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   ? -7.473  -37.544 -29.011 1.00 46.57 ? 3   GLY   A N   1 
ATOM   2    C CA  . GLY   A 1 1   ? -6.471  -36.601 -29.481 1.00 47.10 ? 3   GLY   A CA  1 
ATOM   3    C C   . GLY   A 1 1   ? -7.007  -35.601 -30.491 1.00 44.88 ? 3   GLY   A C   1 
ATOM   4    O O   . GLY   A 1 1   ? -8.177  -35.657 -30.863 1.00 46.02 ? 3   GLY   A O   1 
ATOM   5    N N   . PRO   A 1 2   ? -6.154  -34.684 -30.939 1.00 48.86 ? 4   PRO   A N   1 
ATOM   6    C CA  . PRO   A 1 2   ? -6.599  -33.690 -31.919 1.00 45.86 ? 4   PRO   A CA  1 
ATOM   7    C C   . PRO   A 1 2   ? -6.808  -34.323 -33.284 1.00 40.85 ? 4   PRO   A C   1 
ATOM   8    O O   . PRO   A 1 2   ? -6.103  -35.255 -33.683 1.00 40.83 ? 4   PRO   A O   1 
ATOM   9    C CB  . PRO   A 1 2   ? -5.451  -32.671 -31.952 1.00 51.41 ? 4   PRO   A CB  1 
ATOM   10   C CG  . PRO   A 1 2   ? -4.541  -33.037 -30.795 1.00 53.90 ? 4   PRO   A CG  1 
ATOM   11   C CD  . PRO   A 1 2   ? -4.740  -34.504 -30.580 1.00 52.29 ? 4   PRO   A CD  1 
ATOM   12   N N   . VAL   A 1 3   ? -7.803  -33.809 -33.992 1.00 28.78 ? 5   VAL   A N   1 
ATOM   13   C CA  . VAL   A 1 3   ? -8.110  -34.282 -35.347 1.00 27.16 ? 5   VAL   A CA  1 
ATOM   14   C C   . VAL   A 1 3   ? -7.008  -33.820 -36.292 1.00 25.52 ? 5   VAL   A C   1 
ATOM   15   O O   . VAL   A 1 3   ? -6.570  -32.662 -36.195 1.00 26.68 ? 5   VAL   A O   1 
ATOM   16   C CB  . VAL   A 1 3   ? -9.474  -33.747 -35.783 1.00 25.72 ? 5   VAL   A CB  1 
ATOM   17   C CG1 . VAL   A 1 3   ? -9.760  -34.072 -37.237 1.00 28.78 ? 5   VAL   A CG1 1 
ATOM   18   C CG2 . VAL   A 1 3   ? -10.571 -34.301 -34.873 1.00 30.47 ? 5   VAL   A CG2 1 
ATOM   19   N N   . PRO   A 1 4   ? -6.516  -34.669 -37.196 1.00 23.85 ? 6   PRO   A N   1 
ATOM   20   C CA  . PRO   A 1 4   ? -5.447  -34.239 -38.107 1.00 24.38 ? 6   PRO   A CA  1 
ATOM   21   C C   . PRO   A 1 4   ? -5.973  -33.315 -39.190 1.00 25.59 ? 6   PRO   A C   1 
ATOM   22   O O   . PRO   A 1 4   ? -7.174  -33.215 -39.439 1.00 25.40 ? 6   PRO   A O   1 
ATOM   23   C CB  . PRO   A 1 4   ? -4.940  -35.556 -38.710 1.00 28.61 ? 6   PRO   A CB  1 
ATOM   24   C CG  . PRO   A 1 4   ? -6.110  -36.483 -38.608 1.00 35.38 ? 6   PRO   A CG  1 
ATOM   25   C CD  . PRO   A 1 4   ? -6.814  -36.108 -37.334 1.00 31.22 ? 6   PRO   A CD  1 
ATOM   26   N N   . SER   A 1 5   ? -5.037  -32.647 -39.858 1.00 21.86 ? 7   SER   A N   1 
ATOM   27   C CA  . SER   A 1 5   ? -5.362  -31.667 -40.883 1.00 22.16 ? 7   SER   A CA  1 
ATOM   28   C C   . SER   A 1 5   ? -4.347  -31.780 -42.012 1.00 21.59 ? 7   SER   A C   1 
ATOM   29   O O   . SER   A 1 5   ? -3.191  -32.146 -41.780 1.00 25.96 ? 7   SER   A O   1 
ATOM   30   C CB  . SER   A 1 5   ? -5.369  -30.249 -40.278 1.00 24.93 ? 7   SER   A CB  1 
ATOM   31   O OG  . SER   A 1 5   ? -5.590  -29.250 -41.257 1.00 25.07 ? 7   SER   A OG  1 
ATOM   32   N N   . ARG   A 1 6   ? -4.792  -31.464 -43.232 1.00 23.08 ? 8   ARG   A N   1 
ATOM   33   C CA  . ARG   A 1 6   ? -3.948  -31.383 -44.421 1.00 22.62 ? 8   ARG   A CA  1 
ATOM   34   C C   . ARG   A 1 6   ? -4.200  -30.058 -45.127 1.00 26.72 ? 8   ARG   A C   1 
ATOM   35   O O   . ARG   A 1 6   ? -5.318  -29.532 -45.097 1.00 25.72 ? 8   ARG   A O   1 
ATOM   36   C CB  . ARG   A 1 6   ? -4.240  -32.527 -45.426 1.00 28.02 ? 8   ARG   A CB  1 
ATOM   37   C CG  . ARG   A 1 6   ? -3.969  -33.908 -44.918 1.00 38.69 ? 8   ARG   A CG  1 
ATOM   38   C CD  . ARG   A 1 6   ? -2.486  -34.109 -44.733 1.00 44.99 ? 8   ARG   A CD  1 
ATOM   39   N NE  . ARG   A 1 6   ? -2.163  -35.507 -44.464 1.00 44.42 ? 8   ARG   A NE  1 
ATOM   40   C CZ  . ARG   A 1 6   ? -2.117  -36.043 -43.249 1.00 41.27 ? 8   ARG   A CZ  1 
ATOM   41   N NH1 . ARG   A 1 6   ? -2.377  -35.300 -42.173 1.00 35.40 ? 8   ARG   A NH1 1 
ATOM   42   N NH2 . ARG   A 1 6   ? -1.814  -37.324 -43.113 1.00 39.48 ? 8   ARG   A NH2 1 
ATOM   43   N N   . ALA   A 1 7   ? -3.168  -29.535 -45.793 1.00 21.13 ? 9   ALA   A N   1 
ATOM   44   C CA  . ALA   A 1 7   ? -3.384  -28.412 -46.699 1.00 21.31 ? 9   ALA   A CA  1 
ATOM   45   C C   . ALA   A 1 7   ? -4.352  -28.815 -47.810 1.00 20.38 ? 9   ALA   A C   1 
ATOM   46   O O   . ALA   A 1 7   ? -4.338  -29.955 -48.285 1.00 26.26 ? 9   ALA   A O   1 
ATOM   47   C CB  . ALA   A 1 7   ? -2.062  -27.942 -47.304 1.00 21.77 ? 9   ALA   A CB  1 
ATOM   48   N N   . ARG   A 1 8   ? -5.217  -27.881 -48.210 1.00 23.32 ? 10  ARG   A N   1 
ATOM   49   C CA  . ARG   A 1 8   ? -6.153  -28.183 -49.286 1.00 20.74 ? 10  ARG   A CA  1 
ATOM   50   C C   . ARG   A 1 8   ? -5.542  -27.989 -50.667 1.00 22.61 ? 10  ARG   A C   1 
ATOM   51   O O   . ARG   A 1 8   ? -6.153  -28.405 -51.662 1.00 24.41 ? 10  ARG   A O   1 
ATOM   52   C CB  . ARG   A 1 8   ? -7.410  -27.317 -49.158 1.00 24.79 ? 10  ARG   A CB  1 
ATOM   53   C CG  . ARG   A 1 8   ? -8.102  -27.403 -47.805 1.00 29.97 ? 10  ARG   A CG  1 
ATOM   54   C CD  . ARG   A 1 8   ? -9.371  -26.575 -47.820 1.00 38.88 ? 10  ARG   A CD  1 
ATOM   55   N NE  . ARG   A 1 8   ? -9.088  -25.171 -48.112 1.00 48.88 ? 10  ARG   A NE  1 
ATOM   56   C CZ  . ARG   A 1 8   ? -9.962  -24.327 -48.654 1.00 51.28 ? 10  ARG   A CZ  1 
ATOM   57   N NH1 . ARG   A 1 8   ? -11.181 -24.745 -48.972 1.00 50.71 ? 10  ARG   A NH1 1 
ATOM   58   N NH2 . ARG   A 1 8   ? -9.615  -23.064 -48.880 1.00 49.39 ? 10  ARG   A NH2 1 
ATOM   59   N N   . VAL   A 1 9   ? -4.365  -27.362 -50.754 1.00 22.49 ? 11  VAL   A N   1 
ATOM   60   C CA  . VAL   A 1 9   ? -3.649  -27.180 -52.013 1.00 22.14 ? 11  VAL   A CA  1 
ATOM   61   C C   . VAL   A 1 9   ? -2.174  -27.459 -51.768 1.00 23.64 ? 11  VAL   A C   1 
ATOM   62   O O   . VAL   A 1 9   ? -1.686  -27.391 -50.639 1.00 21.94 ? 11  VAL   A O   1 
ATOM   63   C CB  . VAL   A 1 9   ? -3.825  -25.765 -52.614 1.00 22.01 ? 11  VAL   A CB  1 
ATOM   64   C CG1 . VAL   A 1 9   ? -5.267  -25.503 -52.910 1.00 23.02 ? 11  VAL   A CG1 1 
ATOM   65   C CG2 . VAL   A 1 9   ? -3.281  -24.708 -51.683 1.00 22.89 ? 11  VAL   A CG2 1 
ATOM   66   N N   . TYR   A 1 10  ? -1.466  -27.781 -52.853 1.00 20.49 ? 12  TYR   A N   1 
ATOM   67   C CA  . TYR   A 1 10  ? -0.022  -28.040 -52.821 1.00 24.38 ? 12  TYR   A CA  1 
ATOM   68   C C   . TYR   A 1 10  ? 0.335   -29.059 -51.746 1.00 23.39 ? 12  TYR   A C   1 
ATOM   69   O O   . TYR   A 1 10  ? 1.419   -29.022 -51.163 1.00 24.86 ? 12  TYR   A O   1 
ATOM   70   C CB  . TYR   A 1 10  ? 0.765   -26.747 -52.617 1.00 23.11 ? 12  TYR   A CB  1 
ATOM   71   C CG  . TYR   A 1 10  ? 0.465   -25.689 -53.641 1.00 23.73 ? 12  TYR   A CG  1 
ATOM   72   C CD1 . TYR   A 1 10  ? 0.504   -25.975 -55.001 1.00 21.86 ? 12  TYR   A CD1 1 
ATOM   73   C CD2 . TYR   A 1 10  ? 0.144   -24.393 -53.245 1.00 20.71 ? 12  TYR   A CD2 1 
ATOM   74   C CE1 . TYR   A 1 10  ? 0.238   -24.988 -55.941 1.00 24.10 ? 12  TYR   A CE1 1 
ATOM   75   C CE2 . TYR   A 1 10  ? -0.128  -23.410 -54.165 1.00 24.15 ? 12  TYR   A CE2 1 
ATOM   76   C CZ  . TYR   A 1 10  ? -0.084  -23.714 -55.519 1.00 20.92 ? 12  TYR   A CZ  1 
ATOM   77   O OH  . TYR   A 1 10  ? -0.355  -22.716 -56.435 1.00 25.76 ? 12  TYR   A OH  1 
ATOM   78   N N   . THR   A 1 11  ? -0.584  -29.991 -51.502 1.00 24.77 ? 13  THR   A N   1 
ATOM   79   C CA  . THR   A 1 11  ? -0.438  -30.917 -50.389 1.00 22.40 ? 13  THR   A CA  1 
ATOM   80   C C   . THR   A 1 11  ? 0.774   -31.816 -50.564 1.00 25.11 ? 13  THR   A C   1 
ATOM   81   O O   . THR   A 1 11  ? 1.505   -32.083 -49.601 1.00 27.53 ? 13  THR   A O   1 
ATOM   82   C CB  . THR   A 1 11  ? -1.701  -31.767 -50.264 1.00 26.18 ? 13  THR   A CB  1 
ATOM   83   O OG1 . THR   A 1 11  ? -2.851  -30.927 -50.412 1.00 30.18 ? 13  THR   A OG1 1 
ATOM   84   C CG2 . THR   A 1 11  ? -1.740  -32.459 -48.922 1.00 27.15 ? 13  THR   A CG2 1 
ATOM   85   N N   . ASP   A 1 12  ? 1.003   -32.293 -51.790 1.00 26.40 ? 14  ASP   A N   1 
ATOM   86   C CA  . ASP   A 1 12  ? 1.971   -33.345 -52.063 1.00 25.39 ? 14  ASP   A CA  1 
ATOM   87   C C   . ASP   A 1 12  ? 3.210   -32.838 -52.799 1.00 26.46 ? 14  ASP   A C   1 
ATOM   88   O O   . ASP   A 1 12  ? 3.952   -33.640 -53.372 1.00 26.31 ? 14  ASP   A O   1 
ATOM   89   C CB  . ASP   A 1 12  ? 1.304   -34.468 -52.868 1.00 28.12 ? 14  ASP   A CB  1 
ATOM   90   C CG  . ASP   A 1 12  ? -0.091  -34.826 -52.346 1.00 40.23 ? 14  ASP   A CG  1 
ATOM   91   O OD1 . ASP   A 1 12  ? -1.075  -34.692 -53.109 1.00 46.15 ? 14  ASP   A OD1 1 
ATOM   92   O OD2 . ASP   A 1 12  ? -0.208  -35.233 -51.172 1.00 39.64 ? 14  ASP   A OD2 1 
ATOM   93   N N   . VAL   A 1 13  ? 3.465   -31.526 -52.777 1.00 25.50 ? 15  VAL   A N   1 
ATOM   94   C CA  . VAL   A 1 13  ? 4.567   -30.971 -53.562 1.00 23.33 ? 15  VAL   A CA  1 
ATOM   95   C C   . VAL   A 1 13  ? 5.894   -31.599 -53.158 1.00 26.68 ? 15  VAL   A C   1 
ATOM   96   O O   . VAL   A 1 13  ? 6.679   -32.029 -54.008 1.00 25.91 ? 15  VAL   A O   1 
ATOM   97   C CB  . VAL   A 1 13  ? 4.608   -29.439 -53.424 1.00 25.43 ? 15  VAL   A CB  1 
ATOM   98   C CG1 . VAL   A 1 13  ? 5.996   -28.911 -53.806 1.00 28.32 ? 15  VAL   A CG1 1 
ATOM   99   C CG2 . VAL   A 1 13  ? 3.547   -28.825 -54.305 1.00 25.14 ? 15  VAL   A CG2 1 
ATOM   100  N N   . ASN   A 1 14  ? 6.187   -31.633 -51.861 1.00 24.66 ? 16  ASN   A N   1 
ATOM   101  C CA  . ASN   A 1 14  ? 7.477   -32.168 -51.436 1.00 24.03 ? 16  ASN   A CA  1 
ATOM   102  C C   . ASN   A 1 14  ? 7.518   -33.682 -51.524 1.00 26.76 ? 16  ASN   A C   1 
ATOM   103  O O   . ASN   A 1 14  ? 8.596   -34.263 -51.689 1.00 28.95 ? 16  ASN   A O   1 
ATOM   104  C CB  . ASN   A 1 14  ? 7.797   -31.705 -50.022 1.00 27.16 ? 16  ASN   A CB  1 
ATOM   105  C CG  . ASN   A 1 14  ? 8.139   -30.244 -49.975 1.00 26.20 ? 16  ASN   A CG  1 
ATOM   106  O OD1 . ASN   A 1 14  ? 8.898   -29.751 -50.810 1.00 27.83 ? 16  ASN   A OD1 1 
ATOM   107  N ND2 . ASN   A 1 14  ? 7.550   -29.527 -49.029 1.00 23.53 ? 16  ASN   A ND2 1 
ATOM   108  N N   . THR   A 1 15  ? 6.358   -34.328 -51.434 1.00 25.99 ? 17  THR   A N   1 
ATOM   109  C CA  . THR   A 1 15  ? 6.294   -35.772 -51.599 1.00 30.98 ? 17  THR   A CA  1 
ATOM   110  C C   . THR   A 1 15  ? 6.931   -36.205 -52.908 1.00 33.62 ? 17  THR   A C   1 
ATOM   111  O O   . THR   A 1 15  ? 7.693   -37.180 -52.952 1.00 40.31 ? 17  THR   A O   1 
ATOM   112  C CB  . THR   A 1 15  ? 4.841   -36.231 -51.556 1.00 36.05 ? 17  THR   A CB  1 
ATOM   113  O OG1 . THR   A 1 15  ? 4.283   -35.954 -50.263 1.00 40.81 ? 17  THR   A OG1 1 
ATOM   114  C CG2 . THR   A 1 15  ? 4.762   -37.702 -51.879 1.00 43.69 ? 17  THR   A CG2 1 
ATOM   115  N N   . HIS   A 1 16  ? 6.641   -35.488 -53.986 1.00 32.17 ? 18  HIS   A N   1 
ATOM   116  C CA  . HIS   A 1 16  ? 7.064   -35.924 -55.305 1.00 31.76 ? 18  HIS   A CA  1 
ATOM   117  C C   . HIS   A 1 16  ? 8.248   -35.138 -55.849 1.00 31.90 ? 18  HIS   A C   1 
ATOM   118  O O   . HIS   A 1 16  ? 8.758   -35.477 -56.924 1.00 30.66 ? 18  HIS   A O   1 
ATOM   119  C CB  . HIS   A 1 16  ? 5.867   -35.881 -56.246 1.00 40.72 ? 18  HIS   A CB  1 
ATOM   120  C CG  . HIS   A 1 16  ? 4.745   -36.758 -55.784 1.00 49.77 ? 18  HIS   A CG  1 
ATOM   121  N ND1 . HIS   A 1 16  ? 4.769   -38.129 -55.926 1.00 51.29 ? 18  HIS   A ND1 1 
ATOM   122  C CD2 . HIS   A 1 16  ? 3.596   -36.468 -55.128 1.00 51.13 ? 18  HIS   A CD2 1 
ATOM   123  C CE1 . HIS   A 1 16  ? 3.668   -38.643 -55.407 1.00 52.74 ? 18  HIS   A CE1 1 
ATOM   124  N NE2 . HIS   A 1 16  ? 2.940   -37.657 -54.915 1.00 50.41 ? 18  HIS   A NE2 1 
ATOM   125  N N   . ARG   A 1 17  ? 8.721   -34.128 -55.119 1.00 32.04 ? 19  ARG   A N   1 
ATOM   126  C CA  . ARG   A 1 17  ? 10.045  -33.580 -55.363 1.00 31.66 ? 19  ARG   A CA  1 
ATOM   127  C C   . ARG   A 1 17  ? 11.109  -34.604 -54.973 1.00 29.95 ? 19  ARG   A C   1 
ATOM   128  O O   . ARG   A 1 17  ? 10.872  -35.463 -54.121 1.00 36.78 ? 19  ARG   A O   1 
ATOM   129  C CB  . ARG   A 1 17  ? 10.259  -32.302 -54.550 1.00 32.50 ? 19  ARG   A CB  1 
ATOM   130  C CG  . ARG   A 1 17  ? 9.403   -31.120 -54.962 1.00 39.38 ? 19  ARG   A CG  1 
ATOM   131  C CD  . ARG   A 1 17  ? 10.209  -30.094 -55.721 1.00 36.35 ? 19  ARG   A CD  1 
ATOM   132  N NE  . ARG   A 1 17  ? 9.381   -29.032 -56.286 1.00 29.98 ? 19  ARG   A NE  1 
ATOM   133  C CZ  . ARG   A 1 17  ? 9.796   -28.242 -57.270 1.00 32.82 ? 19  ARG   A CZ  1 
ATOM   134  N NH1 . ARG   A 1 17  ? 11.012  -28.419 -57.778 1.00 29.58 ? 19  ARG   A NH1 1 
ATOM   135  N NH2 . ARG   A 1 17  ? 9.008   -27.296 -57.759 1.00 38.43 ? 19  ARG   A NH2 1 
ATOM   136  N N   . PRO   A 1 18  ? 12.301  -34.523 -55.565 1.00 29.71 ? 20  PRO   A N   1 
ATOM   137  C CA  . PRO   A 1 18  ? 13.402  -35.370 -55.090 1.00 29.31 ? 20  PRO   A CA  1 
ATOM   138  C C   . PRO   A 1 18  ? 13.737  -35.038 -53.644 1.00 29.94 ? 20  PRO   A C   1 
ATOM   139  O O   . PRO   A 1 18  ? 13.501  -33.925 -53.167 1.00 27.42 ? 20  PRO   A O   1 
ATOM   140  C CB  . PRO   A 1 18  ? 14.557  -35.027 -56.036 1.00 32.01 ? 20  PRO   A CB  1 
ATOM   141  C CG  . PRO   A 1 18  ? 14.228  -33.667 -56.553 1.00 35.56 ? 20  PRO   A CG  1 
ATOM   142  C CD  . PRO   A 1 18  ? 12.727  -33.622 -56.650 1.00 32.09 ? 20  PRO   A CD  1 
ATOM   143  N N   . ARG   A 1 19  ? 14.278  -36.031 -52.934 1.00 31.36 ? 21  ARG   A N   1 
ATOM   144  C CA  . ARG   A 1 19  ? 14.589  -35.832 -51.521 1.00 29.42 ? 21  ARG   A CA  1 
ATOM   145  C C   . ARG   A 1 19  ? 15.530  -34.651 -51.324 1.00 29.32 ? 21  ARG   A C   1 
ATOM   146  O O   . ARG   A 1 19  ? 15.355  -33.858 -50.392 1.00 31.79 ? 21  ARG   A O   1 
ATOM   147  C CB  . ARG   A 1 19  ? 15.189  -37.107 -50.926 1.00 38.60 ? 21  ARG   A CB  1 
ATOM   148  C CG  . ARG   A 1 19  ? 15.973  -36.886 -49.633 1.00 43.49 ? 21  ARG   A CG  1 
ATOM   149  C CD  . ARG   A 1 19  ? 16.107  -38.167 -48.823 1.00 55.44 ? 21  ARG   A CD  1 
ATOM   150  N NE  . ARG   A 1 19  ? 14.853  -38.518 -48.162 1.00 68.06 ? 21  ARG   A NE  1 
ATOM   151  C CZ  . ARG   A 1 19  ? 13.993  -39.431 -48.606 1.00 74.79 ? 21  ARG   A CZ  1 
ATOM   152  N NH1 . ARG   A 1 19  ? 14.246  -40.108 -49.719 1.00 77.68 ? 21  ARG   A NH1 1 
ATOM   153  N NH2 . ARG   A 1 19  ? 12.879  -39.667 -47.930 1.00 73.23 ? 21  ARG   A NH2 1 
ATOM   154  N N   . GLU   A 1 20  ? 16.522  -34.504 -52.209 1.00 31.20 ? 22  GLU   A N   1 
ATOM   155  C CA  . GLU   A 1 20  ? 17.461  -33.390 -52.120 1.00 29.36 ? 22  GLU   A CA  1 
ATOM   156  C C   . GLU   A 1 20  ? 16.760  -32.036 -52.054 1.00 28.59 ? 22  GLU   A C   1 
ATOM   157  O O   . GLU   A 1 20  ? 17.323  -31.072 -51.521 1.00 29.83 ? 22  GLU   A O   1 
ATOM   158  C CB  . GLU   A 1 20  ? 18.410  -33.426 -53.323 1.00 34.78 ? 22  GLU   A CB  1 
ATOM   159  C CG  . GLU   A 1 20  ? 17.683  -33.434 -54.667 1.00 54.39 ? 22  GLU   A CG  1 
ATOM   160  C CD  . GLU   A 1 20  ? 18.487  -34.074 -55.785 1.00 69.14 ? 22  GLU   A CD  1 
ATOM   161  O OE1 . GLU   A 1 20  ? 18.185  -33.791 -56.964 1.00 72.15 ? 22  GLU   A OE1 1 
ATOM   162  O OE2 . GLU   A 1 20  ? 19.413  -34.859 -55.488 1.00 74.71 ? 22  GLU   A OE2 1 
ATOM   163  N N   . TYR   A 1 21  ? 15.535  -31.936 -52.586 1.00 25.08 ? 23  TYR   A N   1 
ATOM   164  C CA  . TYR   A 1 21  ? 14.861  -30.640 -52.616 1.00 24.64 ? 23  TYR   A CA  1 
ATOM   165  C C   . TYR   A 1 21  ? 14.514  -30.150 -51.214 1.00 25.51 ? 23  TYR   A C   1 
ATOM   166  O O   . TYR   A 1 21  ? 14.705  -28.965 -50.901 1.00 23.78 ? 23  TYR   A O   1 
ATOM   167  C CB  . TYR   A 1 21  ? 13.599  -30.714 -53.479 1.00 24.53 ? 23  TYR   A CB  1 
ATOM   168  C CG  . TYR   A 1 21  ? 12.827  -29.409 -53.517 1.00 22.43 ? 23  TYR   A CG  1 
ATOM   169  C CD1 . TYR   A 1 21  ? 13.202  -28.393 -54.383 1.00 24.39 ? 23  TYR   A CD1 1 
ATOM   170  C CD2 . TYR   A 1 21  ? 11.737  -29.188 -52.681 1.00 23.46 ? 23  TYR   A CD2 1 
ATOM   171  C CE1 . TYR   A 1 21  ? 12.515  -27.191 -54.424 1.00 20.95 ? 23  TYR   A CE1 1 
ATOM   172  C CE2 . TYR   A 1 21  ? 11.051  -27.989 -52.708 1.00 22.50 ? 23  TYR   A CE2 1 
ATOM   173  C CZ  . TYR   A 1 21  ? 11.431  -27.001 -53.587 1.00 23.04 ? 23  TYR   A CZ  1 
ATOM   174  O OH  . TYR   A 1 21  ? 10.761  -25.805 -53.637 1.00 24.92 ? 23  TYR   A OH  1 
ATOM   175  N N   . TRP   A 1 22  ? 13.985  -31.037 -50.363 1.00 25.68 ? 24  TRP   A N   1 
ATOM   176  C CA  . TRP   A 1 22  ? 13.500  -30.659 -49.040 1.00 24.79 ? 24  TRP   A CA  1 
ATOM   177  C C   . TRP   A 1 22  ? 14.378  -31.151 -47.896 1.00 23.10 ? 24  TRP   A C   1 
ATOM   178  O O   . TRP   A 1 22  ? 14.164  -30.736 -46.754 1.00 25.66 ? 24  TRP   A O   1 
ATOM   179  C CB  . TRP   A 1 22  ? 12.062  -31.174 -48.835 1.00 25.27 ? 24  TRP   A CB  1 
ATOM   180  C CG  . TRP   A 1 22  ? 11.902  -32.652 -49.112 1.00 23.87 ? 24  TRP   A CG  1 
ATOM   181  C CD1 . TRP   A 1 22  ? 11.364  -33.220 -50.236 1.00 23.78 ? 24  TRP   A CD1 1 
ATOM   182  C CD2 . TRP   A 1 22  ? 12.263  -33.741 -48.248 1.00 28.39 ? 24  TRP   A CD2 1 
ATOM   183  N NE1 . TRP   A 1 22  ? 11.384  -34.595 -50.129 1.00 30.33 ? 24  TRP   A NE1 1 
ATOM   184  C CE2 . TRP   A 1 22  ? 11.921  -34.938 -48.918 1.00 31.45 ? 24  TRP   A CE2 1 
ATOM   185  C CE3 . TRP   A 1 22  ? 12.840  -33.824 -46.976 1.00 31.65 ? 24  TRP   A CE3 1 
ATOM   186  C CZ2 . TRP   A 1 22  ? 12.145  -36.199 -48.359 1.00 34.91 ? 24  TRP   A CZ2 1 
ATOM   187  C CZ3 . TRP   A 1 22  ? 13.062  -35.075 -46.424 1.00 34.09 ? 24  TRP   A CZ3 1 
ATOM   188  C CH2 . TRP   A 1 22  ? 12.714  -36.247 -47.117 1.00 34.13 ? 24  TRP   A CH2 1 
ATOM   189  N N   . ASP   A 1 23  ? 15.359  -32.021 -48.162 1.00 28.49 ? 25  ASP   A N   1 
ATOM   190  C CA  . ASP   A 1 23  ? 16.188  -32.599 -47.101 1.00 26.27 ? 25  ASP   A CA  1 
ATOM   191  C C   . ASP   A 1 23  ? 17.347  -31.647 -46.801 1.00 25.61 ? 25  ASP   A C   1 
ATOM   192  O O   . ASP   A 1 23  ? 18.506  -31.885 -47.140 1.00 28.20 ? 25  ASP   A O   1 
ATOM   193  C CB  . ASP   A 1 23  ? 16.678  -33.985 -47.509 1.00 31.99 ? 25  ASP   A CB  1 
ATOM   194  C CG  . ASP   A 1 23  ? 17.502  -34.665 -46.425 1.00 38.96 ? 25  ASP   A CG  1 
ATOM   195  O OD1 . ASP   A 1 23  ? 17.438  -34.240 -45.248 1.00 36.57 ? 25  ASP   A OD1 1 
ATOM   196  O OD2 . ASP   A 1 23  ? 18.226  -35.629 -46.761 1.00 39.88 ? 25  ASP   A OD2 1 
ATOM   197  N N   . TYR   A 1 24  ? 17.010  -30.539 -46.136 1.00 28.36 ? 26  TYR   A N   1 
ATOM   198  C CA  . TYR   A 1 24  ? 17.989  -29.481 -45.936 1.00 29.03 ? 26  TYR   A CA  1 
ATOM   199  C C   . TYR   A 1 24  ? 19.104  -29.875 -44.971 1.00 29.79 ? 26  TYR   A C   1 
ATOM   200  O O   . TYR   A 1 24  ? 20.187  -29.284 -45.026 1.00 30.44 ? 26  TYR   A O   1 
ATOM   201  C CB  . TYR   A 1 24  ? 17.285  -28.208 -45.448 1.00 26.16 ? 26  TYR   A CB  1 
ATOM   202  C CG  . TYR   A 1 24  ? 16.458  -28.374 -44.188 1.00 26.91 ? 26  TYR   A CG  1 
ATOM   203  C CD1 . TYR   A 1 24  ? 15.091  -28.620 -44.257 1.00 25.14 ? 26  TYR   A CD1 1 
ATOM   204  C CD2 . TYR   A 1 24  ? 17.042  -28.267 -42.932 1.00 29.14 ? 26  TYR   A CD2 1 
ATOM   205  C CE1 . TYR   A 1 24  ? 14.332  -28.754 -43.109 1.00 30.30 ? 26  TYR   A CE1 1 
ATOM   206  C CE2 . TYR   A 1 24  ? 16.290  -28.402 -41.784 1.00 29.14 ? 26  TYR   A CE2 1 
ATOM   207  C CZ  . TYR   A 1 24  ? 14.940  -28.647 -41.880 1.00 31.41 ? 26  TYR   A CZ  1 
ATOM   208  O OH  . TYR   A 1 24  ? 14.186  -28.784 -40.738 1.00 39.89 ? 26  TYR   A OH  1 
ATOM   209  N N   . GLU   A 1 25  ? 18.872  -30.853 -44.096 1.00 32.79 ? 27  GLU   A N   1 
ATOM   210  C CA  . GLU   A 1 25  ? 19.922  -31.276 -43.179 1.00 36.78 ? 27  GLU   A CA  1 
ATOM   211  C C   . GLU   A 1 25  ? 21.116  -31.872 -43.909 1.00 36.25 ? 27  GLU   A C   1 
ATOM   212  O O   . GLU   A 1 25  ? 22.229  -31.851 -43.371 1.00 40.25 ? 27  GLU   A O   1 
ATOM   213  C CB  . GLU   A 1 25  ? 19.362  -32.276 -42.167 1.00 40.31 ? 27  GLU   A CB  1 
ATOM   214  C CG  . GLU   A 1 25  ? 18.337  -31.668 -41.237 1.00 50.90 ? 27  GLU   A CG  1 
ATOM   215  C CD  . GLU   A 1 25  ? 17.540  -32.707 -40.475 1.00 60.94 ? 27  GLU   A CD  1 
ATOM   216  O OE1 . GLU   A 1 25  ? 18.128  -33.398 -39.616 1.00 63.53 ? 27  GLU   A OE1 1 
ATOM   217  O OE2 . GLU   A 1 25  ? 16.327  -32.843 -40.748 1.00 64.03 ? 27  GLU   A OE2 1 
ATOM   218  N N   . SER   A 1 26  ? 20.917  -32.385 -45.121 1.00 33.96 ? 28  SER   A N   1 
ATOM   219  C CA  . SER   A 1 26  ? 21.994  -32.971 -45.905 1.00 37.62 ? 28  SER   A CA  1 
ATOM   220  C C   . SER   A 1 26  ? 22.584  -31.991 -46.905 1.00 36.66 ? 28  SER   A C   1 
ATOM   221  O O   . SER   A 1 26  ? 23.489  -32.359 -47.659 1.00 37.60 ? 28  SER   A O   1 
ATOM   222  C CB  . SER   A 1 26  ? 21.492  -34.217 -46.639 1.00 43.09 ? 28  SER   A CB  1 
ATOM   223  O OG  . SER   A 1 26  ? 21.023  -35.186 -45.719 1.00 51.75 ? 28  SER   A OG  1 
ATOM   224  N N   . HIS   A 1 27  ? 22.095  -30.758 -46.924 1.00 32.21 ? 29  HIS   A N   1 
ATOM   225  C CA  . HIS   A 1 27  ? 22.559  -29.774 -47.888 1.00 30.82 ? 29  HIS   A CA  1 
ATOM   226  C C   . HIS   A 1 27  ? 24.019  -29.415 -47.634 1.00 32.41 ? 29  HIS   A C   1 
ATOM   227  O O   . HIS   A 1 27  ? 24.448  -29.250 -46.490 1.00 34.54 ? 29  HIS   A O   1 
ATOM   228  C CB  . HIS   A 1 27  ? 21.681  -28.525 -47.809 1.00 32.70 ? 29  HIS   A CB  1 
ATOM   229  C CG  . HIS   A 1 27  ? 22.050  -27.467 -48.796 1.00 31.13 ? 29  HIS   A CG  1 
ATOM   230  N ND1 . HIS   A 1 27  ? 21.942  -27.652 -50.156 1.00 32.82 ? 29  HIS   A ND1 1 
ATOM   231  C CD2 . HIS   A 1 27  ? 22.539  -26.217 -48.621 1.00 35.56 ? 29  HIS   A CD2 1 
ATOM   232  C CE1 . HIS   A 1 27  ? 22.343  -26.558 -50.779 1.00 35.79 ? 29  HIS   A CE1 1 
ATOM   233  N NE2 . HIS   A 1 27  ? 22.710  -25.672 -49.870 1.00 36.59 ? 29  HIS   A NE2 1 
ATOM   234  N N   . VAL   A 1 28  ? 24.787  -29.295 -48.711 1.00 31.52 ? 30  VAL   A N   1 
ATOM   235  C CA  . VAL   A 1 28  ? 26.187  -28.886 -48.634 1.00 31.40 ? 30  VAL   A CA  1 
ATOM   236  C C   . VAL   A 1 28  ? 26.285  -27.464 -49.169 1.00 34.27 ? 30  VAL   A C   1 
ATOM   237  O O   . VAL   A 1 28  ? 25.960  -27.205 -50.335 1.00 38.04 ? 30  VAL   A O   1 
ATOM   238  C CB  . VAL   A 1 28  ? 27.105  -29.845 -49.404 1.00 34.50 ? 30  VAL   A CB  1 
ATOM   239  C CG1 . VAL   A 1 28  ? 28.538  -29.319 -49.396 1.00 34.72 ? 30  VAL   A CG1 1 
ATOM   240  C CG2 . VAL   A 1 28  ? 27.041  -31.230 -48.777 1.00 36.55 ? 30  VAL   A CG2 1 
ATOM   241  N N   . VAL   A 1 29  ? 26.717  -26.545 -48.315 1.00 33.90 ? 31  VAL   A N   1 
ATOM   242  C CA  . VAL   A 1 29  ? 26.731  -25.127 -48.656 1.00 32.15 ? 31  VAL   A CA  1 
ATOM   243  C C   . VAL   A 1 29  ? 27.877  -24.847 -49.615 1.00 32.45 ? 31  VAL   A C   1 
ATOM   244  O O   . VAL   A 1 29  ? 28.996  -25.344 -49.437 1.00 38.46 ? 31  VAL   A O   1 
ATOM   245  C CB  . VAL   A 1 29  ? 26.840  -24.273 -47.379 1.00 32.77 ? 31  VAL   A CB  1 
ATOM   246  C CG1 . VAL   A 1 29  ? 26.987  -22.801 -47.723 1.00 35.61 ? 31  VAL   A CG1 1 
ATOM   247  C CG2 . VAL   A 1 29  ? 25.619  -24.502 -46.488 1.00 36.01 ? 31  VAL   A CG2 1 
ATOM   248  N N   . GLU   A 1 30  ? 27.599  -24.056 -50.648 1.00 40.13 ? 32  GLU   A N   1 
ATOM   249  C CA  . GLU   A 1 30  ? 28.631  -23.582 -51.570 1.00 43.99 ? 32  GLU   A CA  1 
ATOM   250  C C   . GLU   A 1 30  ? 29.082  -22.206 -51.091 1.00 36.99 ? 32  GLU   A C   1 
ATOM   251  O O   . GLU   A 1 30  ? 28.355  -21.219 -51.236 1.00 36.05 ? 32  GLU   A O   1 
ATOM   252  C CB  . GLU   A 1 30  ? 28.100  -23.529 -52.999 1.00 54.23 ? 32  GLU   A CB  1 
ATOM   253  C CG  . GLU   A 1 30  ? 27.412  -24.805 -53.479 1.00 66.10 ? 32  GLU   A CG  1 
ATOM   254  C CD  . GLU   A 1 30  ? 28.388  -25.909 -53.848 1.00 74.60 ? 32  GLU   A CD  1 
ATOM   255  O OE1 . GLU   A 1 30  ? 28.296  -27.007 -53.259 1.00 77.77 ? 32  GLU   A OE1 1 
ATOM   256  O OE2 . GLU   A 1 30  ? 29.246  -25.679 -54.729 1.00 78.50 ? 32  GLU   A OE2 1 
ATOM   257  N N   . TRP   A 1 31  ? 30.276  -22.134 -50.506 1.00 33.42 ? 33  TRP   A N   1 
ATOM   258  C CA  . TRP   A 1 31  ? 30.749  -20.885 -49.922 1.00 29.70 ? 33  TRP   A CA  1 
ATOM   259  C C   . TRP   A 1 31  ? 31.380  -19.988 -50.979 1.00 31.43 ? 33  TRP   A C   1 
ATOM   260  O O   . TRP   A 1 31  ? 32.140  -20.448 -51.837 1.00 34.50 ? 33  TRP   A O   1 
ATOM   261  C CB  . TRP   A 1 31  ? 31.766  -21.150 -48.807 1.00 34.47 ? 33  TRP   A CB  1 
ATOM   262  C CG  . TRP   A 1 31  ? 31.261  -22.039 -47.707 1.00 33.93 ? 33  TRP   A CG  1 
ATOM   263  C CD1 . TRP   A 1 31  ? 31.463  -23.385 -47.587 1.00 35.97 ? 33  TRP   A CD1 1 
ATOM   264  C CD2 . TRP   A 1 31  ? 30.477  -21.649 -46.570 1.00 32.04 ? 33  TRP   A CD2 1 
ATOM   265  N NE1 . TRP   A 1 31  ? 30.850  -23.856 -46.452 1.00 36.60 ? 33  TRP   A NE1 1 
ATOM   266  C CE2 . TRP   A 1 31  ? 30.238  -22.812 -45.810 1.00 37.51 ? 33  TRP   A CE2 1 
ATOM   267  C CE3 . TRP   A 1 31  ? 29.943  -20.431 -46.126 1.00 29.68 ? 33  TRP   A CE3 1 
ATOM   268  C CZ2 . TRP   A 1 31  ? 29.495  -22.794 -44.629 1.00 40.74 ? 33  TRP   A CZ2 1 
ATOM   269  C CZ3 . TRP   A 1 31  ? 29.210  -20.416 -44.953 1.00 37.83 ? 33  TRP   A CZ3 1 
ATOM   270  C CH2 . TRP   A 1 31  ? 28.991  -21.591 -44.218 1.00 40.71 ? 33  TRP   A CH2 1 
ATOM   271  N N   . GLY   A 1 32  ? 31.080  -18.695 -50.896 1.00 27.23 ? 34  GLY   A N   1 
ATOM   272  C CA  . GLY   A 1 32  ? 31.712  -17.701 -51.736 1.00 25.57 ? 34  GLY   A CA  1 
ATOM   273  C C   . GLY   A 1 32  ? 32.931  -17.106 -51.055 1.00 27.29 ? 34  GLY   A C   1 
ATOM   274  O O   . GLY   A 1 32  ? 33.419  -17.602 -50.039 1.00 31.11 ? 34  GLY   A O   1 
ATOM   275  N N   . ASN   A 1 33  ? 33.407  -15.999 -51.618 1.00 27.51 ? 35  ASN   A N   1 
ATOM   276  C CA  . ASN   A 1 33  ? 34.615  -15.325 -51.142 1.00 28.01 ? 35  ASN   A CA  1 
ATOM   277  C C   . ASN   A 1 33  ? 34.230  -14.184 -50.199 1.00 27.18 ? 35  ASN   A C   1 
ATOM   278  O O   . ASN   A 1 33  ? 33.630  -13.196 -50.625 1.00 26.95 ? 35  ASN   A O   1 
ATOM   279  C CB  . ASN   A 1 33  ? 35.418  -14.806 -52.333 1.00 34.12 ? 35  ASN   A CB  1 
ATOM   280  C CG  . ASN   A 1 33  ? 36.851  -14.547 -51.988 1.00 47.16 ? 35  ASN   A CG  1 
ATOM   281  O OD1 . ASN   A 1 33  ? 37.346  -15.037 -50.976 1.00 58.86 ? 35  ASN   A OD1 1 
ATOM   282  N ND2 . ASN   A 1 33  ? 37.541  -13.788 -52.834 1.00 49.42 ? 35  ASN   A ND2 1 
ATOM   283  N N   . GLN   A 1 34  ? 34.591  -14.309 -48.916 1.00 25.67 ? 36  GLN   A N   1 
ATOM   284  C CA  . GLN   A 1 34  ? 34.208  -13.287 -47.946 1.00 27.20 ? 36  GLN   A CA  1 
ATOM   285  C C   . GLN   A 1 34  ? 34.812  -11.919 -48.264 1.00 25.76 ? 36  GLN   A C   1 
ATOM   286  O O   . GLN   A 1 34  ? 34.213  -10.887 -47.929 1.00 25.15 ? 36  GLN   A O   1 
ATOM   287  C CB  . GLN   A 1 34  ? 34.608  -13.731 -46.535 1.00 30.94 ? 36  GLN   A CB  1 
ATOM   288  C CG  . GLN   A 1 34  ? 34.114  -12.820 -45.419 1.00 30.52 ? 36  GLN   A CG  1 
ATOM   289  C CD  . GLN   A 1 34  ? 35.134  -11.756 -45.029 1.00 33.33 ? 36  GLN   A CD  1 
ATOM   290  O OE1 . GLN   A 1 34  ? 36.307  -11.854 -45.380 1.00 31.65 ? 36  GLN   A OE1 1 
ATOM   291  N NE2 . GLN   A 1 34  ? 34.683  -10.731 -44.308 1.00 33.25 ? 36  GLN   A NE2 1 
ATOM   292  N N   . ASP   A 1 35  ? 35.999  -11.872 -48.883 1.00 29.05 ? 37  ASP   A N   1 
ATOM   293  C CA  . ASP   A 1 35  ? 36.594  -10.569 -49.151 1.00 31.31 ? 37  ASP   A CA  1 
ATOM   294  C C   . ASP   A 1 35  ? 35.959  -9.844  -50.329 1.00 31.86 ? 37  ASP   A C   1 
ATOM   295  O O   . ASP   A 1 35  ? 36.388  -8.726  -50.637 1.00 31.07 ? 37  ASP   A O   1 
ATOM   296  C CB  . ASP   A 1 35  ? 38.099  -10.688 -49.390 1.00 40.03 ? 37  ASP   A CB  1 
ATOM   297  C CG  . ASP   A 1 35  ? 38.448  -11.800 -50.336 1.00 61.45 ? 37  ASP   A CG  1 
ATOM   298  O OD1 . ASP   A 1 35  ? 38.506  -12.958 -49.877 1.00 71.55 ? 37  ASP   A OD1 1 
ATOM   299  O OD2 . ASP   A 1 35  ? 38.659  -11.520 -51.535 1.00 69.83 ? 37  ASP   A OD2 1 
ATOM   300  N N   . ASP   A 1 36  ? 34.940  -10.424 -50.982 1.00 28.77 ? 38  ASP   A N   1 
ATOM   301  C CA  . ASP   A 1 36  ? 34.239  -9.710  -52.038 1.00 28.05 ? 38  ASP   A CA  1 
ATOM   302  C C   . ASP   A 1 36  ? 33.334  -8.608  -51.503 1.00 27.68 ? 38  ASP   A C   1 
ATOM   303  O O   . ASP   A 1 36  ? 32.846  -7.795  -52.298 1.00 30.47 ? 38  ASP   A O   1 
ATOM   304  C CB  . ASP   A 1 36  ? 33.375  -10.666 -52.869 1.00 30.37 ? 38  ASP   A CB  1 
ATOM   305  C CG  . ASP   A 1 36  ? 34.179  -11.578 -53.776 1.00 33.52 ? 38  ASP   A CG  1 
ATOM   306  O OD1 . ASP   A 1 36  ? 35.415  -11.418 -53.887 1.00 33.30 ? 38  ASP   A OD1 1 
ATOM   307  O OD2 . ASP   A 1 36  ? 33.544  -12.474 -54.382 1.00 37.57 ? 38  ASP   A OD2 1 
ATOM   308  N N   . TYR   A 1 37  ? 33.077  -8.569  -50.190 1.00 27.28 ? 39  TYR   A N   1 
ATOM   309  C CA  . TYR   A 1 37  ? 32.032  -7.723  -49.625 1.00 24.96 ? 39  TYR   A CA  1 
ATOM   310  C C   . TYR   A 1 37  ? 32.619  -6.841  -48.540 1.00 30.97 ? 39  TYR   A C   1 
ATOM   311  O O   . TYR   A 1 37  ? 33.325  -7.332  -47.652 1.00 37.65 ? 39  TYR   A O   1 
ATOM   312  C CB  . TYR   A 1 37  ? 30.877  -8.573  -49.068 1.00 25.68 ? 39  TYR   A CB  1 
ATOM   313  C CG  . TYR   A 1 37  ? 30.371  -9.527  -50.106 1.00 23.52 ? 39  TYR   A CG  1 
ATOM   314  C CD1 . TYR   A 1 37  ? 30.740  -10.870 -50.100 1.00 26.39 ? 39  TYR   A CD1 1 
ATOM   315  C CD2 . TYR   A 1 37  ? 29.577  -9.071  -51.143 1.00 24.30 ? 39  TYR   A CD2 1 
ATOM   316  C CE1 . TYR   A 1 37  ? 30.296  -11.735 -51.078 1.00 28.64 ? 39  TYR   A CE1 1 
ATOM   317  C CE2 . TYR   A 1 37  ? 29.135  -9.922  -52.125 1.00 24.38 ? 39  TYR   A CE2 1 
ATOM   318  C CZ  . TYR   A 1 37  ? 29.489  -11.251 -52.088 1.00 26.70 ? 39  TYR   A CZ  1 
ATOM   319  O OH  . TYR   A 1 37  ? 29.038  -12.082 -53.085 1.00 29.81 ? 39  TYR   A OH  1 
ATOM   320  N N   . GLN   A 1 38  ? 32.346  -5.542  -48.631 1.00 27.96 ? 40  GLN   A N   1 
ATOM   321  C CA  . GLN   A 1 38  ? 32.784  -4.564  -47.642 1.00 26.89 ? 40  GLN   A CA  1 
ATOM   322  C C   . GLN   A 1 38  ? 31.555  -4.009  -46.937 1.00 29.07 ? 40  GLN   A C   1 
ATOM   323  O O   . GLN   A 1 38  ? 30.655  -3.474  -47.593 1.00 29.44 ? 40  GLN   A O   1 
ATOM   324  C CB  . GLN   A 1 38  ? 33.583  -3.445  -48.307 1.00 36.35 ? 40  GLN   A CB  1 
ATOM   325  C CG  . GLN   A 1 38  ? 34.810  -3.961  -49.031 1.00 50.41 ? 40  GLN   A CG  1 
ATOM   326  C CD  . GLN   A 1 38  ? 35.877  -2.903  -49.228 1.00 64.49 ? 40  GLN   A CD  1 
ATOM   327  O OE1 . GLN   A 1 38  ? 35.582  -1.758  -49.576 1.00 72.40 ? 40  GLN   A OE1 1 
ATOM   328  N NE2 . GLN   A 1 38  ? 37.130  -3.283  -49.000 1.00 64.22 ? 40  GLN   A NE2 1 
ATOM   329  N N   . LEU   A 1 39  ? 31.504  -4.158  -45.612 1.00 25.42 ? 41  LEU   A N   1 
ATOM   330  C CA  . LEU   A 1 39  ? 30.356  -3.663  -44.864 1.00 24.81 ? 41  LEU   A CA  1 
ATOM   331  C C   . LEU   A 1 39  ? 30.398  -2.139  -44.805 1.00 27.66 ? 41  LEU   A C   1 
ATOM   332  O O   . LEU   A 1 39  ? 31.465  -1.541  -44.625 1.00 28.96 ? 41  LEU   A O   1 
ATOM   333  C CB  . LEU   A 1 39  ? 30.335  -4.252  -43.451 1.00 24.50 ? 41  LEU   A CB  1 
ATOM   334  C CG  . LEU   A 1 39  ? 30.332  -5.778  -43.321 1.00 26.34 ? 41  LEU   A CG  1 
ATOM   335  C CD1 . LEU   A 1 39  ? 30.494  -6.191  -41.863 1.00 30.10 ? 41  LEU   A CD1 1 
ATOM   336  C CD2 . LEU   A 1 39  ? 29.048  -6.362  -43.910 1.00 25.20 ? 41  LEU   A CD2 1 
ATOM   337  N N   . VAL   A 1 40  ? 29.231  -1.514  -44.960 1.00 28.38 ? 42  VAL   A N   1 
ATOM   338  C CA  . VAL   A 1 40  ? 29.102  -0.060  -45.030 1.00 28.51 ? 42  VAL   A CA  1 
ATOM   339  C C   . VAL   A 1 40  ? 28.424  0.507   -43.783 1.00 33.99 ? 42  VAL   A C   1 
ATOM   340  O O   . VAL   A 1 40  ? 28.925  1.451   -43.167 1.00 32.37 ? 42  VAL   A O   1 
ATOM   341  C CB  . VAL   A 1 40  ? 28.352  0.368   -46.312 1.00 35.66 ? 42  VAL   A CB  1 
ATOM   342  C CG1 . VAL   A 1 40  ? 28.109  1.863   -46.310 1.00 37.02 ? 42  VAL   A CG1 1 
ATOM   343  C CG2 . VAL   A 1 40  ? 29.147  -0.032  -47.534 1.00 33.36 ? 42  VAL   A CG2 1 
ATOM   344  N N   . ARG   A 1 41  ? 27.275  -0.044  -43.406 1.00 31.28 ? 43  ARG   A N   1 
ATOM   345  C CA  . ARG   A 1 41  ? 26.589  0.416   -42.208 1.00 29.72 ? 43  ARG   A CA  1 
ATOM   346  C C   . ARG   A 1 41  ? 25.644  -0.673  -41.724 1.00 30.48 ? 43  ARG   A C   1 
ATOM   347  O O   . ARG   A 1 41  ? 25.130  -1.468  -42.514 1.00 29.03 ? 43  ARG   A O   1 
ATOM   348  C CB  . ARG   A 1 41  ? 25.822  1.720   -42.459 1.00 37.08 ? 43  ARG   A CB  1 
ATOM   349  C CG  . ARG   A 1 41  ? 24.539  1.561   -43.248 1.00 45.22 ? 43  ARG   A CG  1 
ATOM   350  C CD  . ARG   A 1 41  ? 23.866  2.907   -43.439 1.00 53.52 ? 43  ARG   A CD  1 
ATOM   351  N NE  . ARG   A 1 41  ? 24.598  3.715   -44.405 1.00 58.53 ? 43  ARG   A NE  1 
ATOM   352  C CZ  . ARG   A 1 41  ? 24.203  3.910   -45.657 1.00 64.77 ? 43  ARG   A CZ  1 
ATOM   353  N NH1 . ARG   A 1 41  ? 23.070  3.368   -46.081 1.00 64.82 ? 43  ARG   A NH1 1 
ATOM   354  N NH2 . ARG   A 1 41  ? 24.932  4.651   -46.479 1.00 66.18 ? 43  ARG   A NH2 1 
ATOM   355  N N   . LYS   A 1 42  ? 25.436  -0.706  -40.412 1.00 27.49 ? 44  LYS   A N   1 
ATOM   356  C CA  . LYS   A 1 42  ? 24.504  -1.650  -39.810 1.00 25.11 ? 44  LYS   A CA  1 
ATOM   357  C C   . LYS   A 1 42  ? 23.080  -1.157  -40.000 1.00 29.14 ? 44  LYS   A C   1 
ATOM   358  O O   . LYS   A 1 42  ? 22.782  0.007   -39.722 1.00 31.37 ? 44  LYS   A O   1 
ATOM   359  C CB  . LYS   A 1 42  ? 24.810  -1.816  -38.322 1.00 29.43 ? 44  LYS   A CB  1 
ATOM   360  C CG  . LYS   A 1 42  ? 24.049  -2.928  -37.621 1.00 33.51 ? 44  LYS   A CG  1 
ATOM   361  C CD  . LYS   A 1 42  ? 24.828  -3.388  -36.382 1.00 44.73 ? 44  LYS   A CD  1 
ATOM   362  C CE  . LYS   A 1 42  ? 23.932  -3.561  -35.159 1.00 48.48 ? 44  LYS   A CE  1 
ATOM   363  N NZ  . LYS   A 1 42  ? 24.726  -3.797  -33.909 1.00 47.34 ? 44  LYS   A NZ  1 
ATOM   364  N N   . LEU   A 1 43  ? 22.204  -2.045  -40.471 1.00 23.19 ? 45  LEU   A N   1 
ATOM   365  C CA  . LEU   A 1 43  ? 20.800  -1.716  -40.699 1.00 25.73 ? 45  LEU   A CA  1 
ATOM   366  C C   . LEU   A 1 43  ? 19.874  -2.216  -39.599 1.00 32.42 ? 45  LEU   A C   1 
ATOM   367  O O   . LEU   A 1 43  ? 18.823  -1.610  -39.371 1.00 37.11 ? 45  LEU   A O   1 
ATOM   368  C CB  . LEU   A 1 43  ? 20.325  -2.288  -42.041 1.00 26.75 ? 45  LEU   A CB  1 
ATOM   369  C CG  . LEU   A 1 43  ? 21.025  -1.752  -43.291 1.00 28.76 ? 45  LEU   A CG  1 
ATOM   370  C CD1 . LEU   A 1 43  ? 20.402  -2.354  -44.527 1.00 30.09 ? 45  LEU   A CD1 1 
ATOM   371  C CD2 . LEU   A 1 43  ? 20.966  -0.232  -43.349 1.00 30.10 ? 45  LEU   A CD2 1 
ATOM   372  N N   . GLY   A 1 44  ? 20.219  -3.303  -38.921 1.00 31.11 ? 46  GLY   A N   1 
ATOM   373  C CA  . GLY   A 1 44  ? 19.372  -3.801  -37.853 1.00 32.03 ? 46  GLY   A CA  1 
ATOM   374  C C   . GLY   A 1 44  ? 20.046  -4.935  -37.117 1.00 31.28 ? 46  GLY   A C   1 
ATOM   375  O O   . GLY   A 1 44  ? 21.101  -5.430  -37.520 1.00 28.02 ? 46  GLY   A O   1 
ATOM   376  N N   . ARG   A 1 45  ? 19.417  -5.327  -36.009 1.00 26.17 ? 47  ARG   A N   1 
ATOM   377  C CA  . ARG   A 1 45  ? 19.871  -6.442  -35.195 1.00 29.58 ? 47  ARG   A CA  1 
ATOM   378  C C   . ARG   A 1 45  ? 18.659  -7.170  -34.631 1.00 31.37 ? 47  ARG   A C   1 
ATOM   379  O O   . ARG   A 1 45  ? 17.626  -6.560  -34.350 1.00 33.36 ? 47  ARG   A O   1 
ATOM   380  C CB  . ARG   A 1 45  ? 20.793  -5.978  -34.044 1.00 33.05 ? 47  ARG   A CB  1 
ATOM   381  C CG  . ARG   A 1 45  ? 20.916  -6.993  -32.913 1.00 44.71 ? 47  ARG   A CG  1 
ATOM   382  C CD  . ARG   A 1 45  ? 21.532  -6.424  -31.657 1.00 51.77 ? 47  ARG   A CD  1 
ATOM   383  N NE  . ARG   A 1 45  ? 22.990  -6.409  -31.718 1.00 54.95 ? 47  ARG   A NE  1 
ATOM   384  C CZ  . ARG   A 1 45  ? 23.777  -6.189  -30.669 1.00 58.86 ? 47  ARG   A CZ  1 
ATOM   385  N NH1 . ARG   A 1 45  ? 23.247  -5.978  -29.469 1.00 52.08 ? 47  ARG   A NH1 1 
ATOM   386  N NH2 . ARG   A 1 45  ? 25.096  -6.187  -30.817 1.00 59.80 ? 47  ARG   A NH2 1 
ATOM   387  N N   . GLY   A 1 46  ? 18.794  -8.486  -34.484 1.00 31.34 ? 48  GLY   A N   1 
ATOM   388  C CA  . GLY   A 1 46  ? 17.794  -9.292  -33.820 1.00 34.44 ? 48  GLY   A CA  1 
ATOM   389  C C   . GLY   A 1 46  ? 18.453  -10.321 -32.926 1.00 35.90 ? 48  GLY   A C   1 
ATOM   390  O O   . GLY   A 1 46  ? 19.676  -10.350 -32.781 1.00 39.09 ? 48  GLY   A O   1 
ATOM   391  N N   . LYS   A 1 47  ? 17.619  -11.181 -32.335 1.00 33.85 ? 49  LYS   A N   1 
ATOM   392  C CA  . LYS   A 1 47  ? 18.154  -12.206 -31.447 1.00 37.38 ? 49  LYS   A CA  1 
ATOM   393  C C   . LYS   A 1 47  ? 19.079  -13.161 -32.183 1.00 36.41 ? 49  LYS   A C   1 
ATOM   394  O O   . LYS   A 1 47  ? 19.995  -13.726 -31.575 1.00 39.27 ? 49  LYS   A O   1 
ATOM   395  C CB  . LYS   A 1 47  ? 17.014  -12.976 -30.777 1.00 49.12 ? 49  LYS   A CB  1 
ATOM   396  C CG  . LYS   A 1 47  ? 16.410  -12.248 -29.586 1.00 60.60 ? 49  LYS   A CG  1 
ATOM   397  C CD  . LYS   A 1 47  ? 15.344  -13.085 -28.896 1.00 66.63 ? 49  LYS   A CD  1 
ATOM   398  C CE  . LYS   A 1 47  ? 15.887  -14.447 -28.486 1.00 68.11 ? 49  LYS   A CE  1 
ATOM   399  N NZ  . LYS   A 1 47  ? 15.208  -14.965 -27.263 1.00 68.76 ? 49  LYS   A NZ  1 
ATOM   400  N N   . TYR   A 1 48  ? 18.884  -13.332 -33.489 1.00 34.01 ? 50  TYR   A N   1 
ATOM   401  C CA  . TYR   A 1 48  ? 19.605  -14.354 -34.232 1.00 34.88 ? 50  TYR   A CA  1 
ATOM   402  C C   . TYR   A 1 48  ? 20.540  -13.828 -35.314 1.00 31.44 ? 50  TYR   A C   1 
ATOM   403  O O   . TYR   A 1 48  ? 21.171  -14.645 -35.989 1.00 28.73 ? 50  TYR   A O   1 
ATOM   404  C CB  . TYR   A 1 48  ? 18.618  -15.335 -34.880 1.00 41.89 ? 50  TYR   A CB  1 
ATOM   405  C CG  . TYR   A 1 48  ? 17.735  -16.066 -33.896 1.00 51.90 ? 50  TYR   A CG  1 
ATOM   406  C CD1 . TYR   A 1 48  ? 16.368  -15.836 -33.861 1.00 56.52 ? 50  TYR   A CD1 1 
ATOM   407  C CD2 . TYR   A 1 48  ? 18.272  -16.980 -32.999 1.00 56.80 ? 50  TYR   A CD2 1 
ATOM   408  C CE1 . TYR   A 1 48  ? 15.555  -16.502 -32.963 1.00 64.75 ? 50  TYR   A CE1 1 
ATOM   409  C CE2 . TYR   A 1 48  ? 17.469  -17.650 -32.096 1.00 63.96 ? 50  TYR   A CE2 1 
ATOM   410  C CZ  . TYR   A 1 48  ? 16.111  -17.408 -32.081 1.00 68.26 ? 50  TYR   A CZ  1 
ATOM   411  O OH  . TYR   A 1 48  ? 15.307  -18.074 -31.183 1.00 71.51 ? 50  TYR   A OH  1 
ATOM   412  N N   . SER   A 1 49  ? 20.645  -12.514 -35.516 1.00 31.60 ? 51  SER   A N   1 
ATOM   413  C CA  . SER   A 1 49  ? 21.509  -12.005 -36.582 1.00 29.31 ? 51  SER   A CA  1 
ATOM   414  C C   . SER   A 1 49  ? 21.674  -10.495 -36.466 1.00 27.22 ? 51  SER   A C   1 
ATOM   415  O O   . SER   A 1 49  ? 20.960  -9.819  -35.720 1.00 29.41 ? 51  SER   A O   1 
ATOM   416  C CB  . SER   A 1 49  ? 20.947  -12.340 -37.960 1.00 25.99 ? 51  SER   A CB  1 
ATOM   417  O OG  . SER   A 1 49  ? 19.627  -11.812 -38.078 1.00 30.28 ? 51  SER   A OG  1 
ATOM   418  N N   . GLU   A 1 50  ? 22.629  -9.977  -37.241 1.00 23.67 ? 52  GLU   A N   1 
ATOM   419  C CA  . GLU   A 1 50  ? 22.748  -8.558  -37.534 1.00 23.92 ? 52  GLU   A CA  1 
ATOM   420  C C   . GLU   A 1 50  ? 22.740  -8.389  -39.046 1.00 25.26 ? 52  GLU   A C   1 
ATOM   421  O O   . GLU   A 1 50  ? 23.199  -9.266  -39.782 1.00 25.51 ? 52  GLU   A O   1 
ATOM   422  C CB  . GLU   A 1 50  ? 24.033  -7.957  -36.938 1.00 25.20 ? 52  GLU   A CB  1 
ATOM   423  C CG  . GLU   A 1 50  ? 24.103  -8.098  -35.424 1.00 31.83 ? 52  GLU   A CG  1 
ATOM   424  C CD  . GLU   A 1 50  ? 25.197  -7.248  -34.814 1.00 43.52 ? 52  GLU   A CD  1 
ATOM   425  O OE1 . GLU   A 1 50  ? 26.337  -7.270  -35.335 1.00 40.86 ? 52  GLU   A OE1 1 
ATOM   426  O OE2 . GLU   A 1 50  ? 24.908  -6.547  -33.823 1.00 48.39 ? 52  GLU   A OE2 1 
ATOM   427  N N   . VAL   A 1 51  ? 22.152  -7.285  -39.505 1.00 23.44 ? 53  VAL   A N   1 
ATOM   428  C CA  . VAL   A 1 51  ? 22.028  -7.030  -40.969 1.00 21.29 ? 53  VAL   A CA  1 
ATOM   429  C C   . VAL   A 1 51  ? 22.742  -5.719  -41.318 1.00 25.65 ? 53  VAL   A C   1 
ATOM   430  O O   . VAL   A 1 51  ? 22.610  -4.747  -40.561 1.00 25.92 ? 53  VAL   A O   1 
ATOM   431  C CB  . VAL   A 1 51  ? 20.563  -7.079  -41.445 1.00 28.19 ? 53  VAL   A CB  1 
ATOM   432  C CG1 . VAL   A 1 51  ? 19.742  -5.935  -40.887 1.00 33.35 ? 53  VAL   A CG1 1 
ATOM   433  C CG2 . VAL   A 1 51  ? 20.474  -7.118  -42.957 1.00 29.17 ? 53  VAL   A CG2 1 
ATOM   434  N N   . PHE   A 1 52  ? 23.447  -5.721  -42.449 1.00 21.49 ? 54  PHE   A N   1 
ATOM   435  C CA  . PHE   A 1 52  ? 24.296  -4.618  -42.872 1.00 20.43 ? 54  PHE   A CA  1 
ATOM   436  C C   . PHE   A 1 52  ? 24.038  -4.290  -44.330 1.00 24.57 ? 54  PHE   A C   1 
ATOM   437  O O   . PHE   A 1 52  ? 23.785  -5.175  -45.151 1.00 26.24 ? 54  PHE   A O   1 
ATOM   438  C CB  . PHE   A 1 52  ? 25.792  -4.967  -42.735 1.00 20.95 ? 54  PHE   A CB  1 
ATOM   439  C CG  . PHE   A 1 52  ? 26.219  -5.278  -41.337 1.00 21.30 ? 54  PHE   A CG  1 
ATOM   440  C CD1 . PHE   A 1 52  ? 25.999  -6.532  -40.793 1.00 21.14 ? 54  PHE   A CD1 1 
ATOM   441  C CD2 . PHE   A 1 52  ? 26.848  -4.311  -40.558 1.00 22.75 ? 54  PHE   A CD2 1 
ATOM   442  C CE1 . PHE   A 1 52  ? 26.379  -6.817  -39.495 1.00 24.44 ? 54  PHE   A CE1 1 
ATOM   443  C CE2 . PHE   A 1 52  ? 27.236  -4.591  -39.263 1.00 23.62 ? 54  PHE   A CE2 1 
ATOM   444  C CZ  . PHE   A 1 52  ? 26.996  -5.846  -38.725 1.00 26.83 ? 54  PHE   A CZ  1 
ATOM   445  N N   . GLU   A 1 53  ? 24.146  -3.009  -44.651 1.00 23.60 ? 55  GLU   A N   1 
ATOM   446  C CA  . GLU   A 1 53  ? 24.381  -2.607  -46.027 1.00 25.39 ? 55  GLU   A CA  1 
ATOM   447  C C   . GLU   A 1 53  ? 25.853  -2.830  -46.354 1.00 24.24 ? 55  GLU   A C   1 
ATOM   448  O O   . GLU   A 1 53  ? 26.728  -2.607  -45.513 1.00 27.93 ? 55  GLU   A O   1 
ATOM   449  C CB  . GLU   A 1 53  ? 24.003  -1.140  -46.221 1.00 32.41 ? 55  GLU   A CB  1 
ATOM   450  C CG  . GLU   A 1 53  ? 24.075  -0.642  -47.649 1.00 39.93 ? 55  GLU   A CG  1 
ATOM   451  C CD  . GLU   A 1 53  ? 23.658  0.814   -47.761 1.00 50.89 ? 55  GLU   A CD  1 
ATOM   452  O OE1 . GLU   A 1 53  ? 24.540  1.671   -47.970 1.00 53.91 ? 55  GLU   A OE1 1 
ATOM   453  O OE2 . GLU   A 1 53  ? 22.449  1.104   -47.621 1.00 51.45 ? 55  GLU   A OE2 1 
ATOM   454  N N   . ALA   A 1 54  ? 26.122  -3.307  -47.569 1.00 24.72 ? 56  ALA   A N   1 
ATOM   455  C CA  . ALA   A 1 54  ? 27.489  -3.601  -47.973 1.00 24.63 ? 56  ALA   A CA  1 
ATOM   456  C C   . ALA   A 1 54  ? 27.636  -3.314  -49.457 1.00 25.08 ? 56  ALA   A C   1 
ATOM   457  O O   . ALA   A 1 54  ? 26.660  -3.045  -50.162 1.00 28.48 ? 56  ALA   A O   1 
ATOM   458  C CB  . ALA   A 1 54  ? 27.870  -5.053  -47.664 1.00 25.13 ? 56  ALA   A CB  1 
ATOM   459  N N   . ILE   A 1 55  ? 28.882  -3.366  -49.920 1.00 31.23 ? 57  ILE   A N   1 
ATOM   460  C CA  . ILE   A 1 55  ? 29.214  -3.205  -51.327 1.00 30.88 ? 57  ILE   A CA  1 
ATOM   461  C C   . ILE   A 1 55  ? 29.907  -4.475  -51.787 1.00 30.34 ? 57  ILE   A C   1 
ATOM   462  O O   . ILE   A 1 55  ? 30.834  -4.956  -51.126 1.00 30.11 ? 57  ILE   A O   1 
ATOM   463  C CB  . ILE   A 1 55  ? 30.117  -1.982  -51.573 1.00 38.45 ? 57  ILE   A CB  1 
ATOM   464  C CG1 . ILE   A 1 55  ? 29.473  -0.702  -51.032 1.00 43.84 ? 57  ILE   A CG1 1 
ATOM   465  C CG2 . ILE   A 1 55  ? 30.431  -1.850  -53.056 1.00 39.44 ? 57  ILE   A CG2 1 
ATOM   466  C CD1 . ILE   A 1 55  ? 28.626  0.040   -52.033 1.00 49.88 ? 57  ILE   A CD1 1 
ATOM   467  N N   . ASN   A 1 56  ? 29.460  -5.016  -52.911 1.00 26.19 ? 58  ASN   A N   1 
ATOM   468  C CA  . ASN   A 1 56  ? 30.179  -6.092  -53.580 1.00 28.72 ? 58  ASN   A CA  1 
ATOM   469  C C   . ASN   A 1 56  ? 31.260  -5.446  -54.438 1.00 32.03 ? 58  ASN   A C   1 
ATOM   470  O O   . ASN   A 1 56  ? 30.955  -4.845  -55.471 1.00 36.15 ? 58  ASN   A O   1 
ATOM   471  C CB  . ASN   A 1 56  ? 29.202  -6.918  -54.413 1.00 31.72 ? 58  ASN   A CB  1 
ATOM   472  C CG  . ASN   A 1 56  ? 29.860  -8.081  -55.130 1.00 31.65 ? 58  ASN   A CG  1 
ATOM   473  O OD1 . ASN   A 1 56  ? 31.076  -8.141  -55.272 1.00 32.43 ? 58  ASN   A OD1 1 
ATOM   474  N ND2 . ASN   A 1 56  ? 29.036  -9.015  -55.605 1.00 37.87 ? 58  ASN   A ND2 1 
ATOM   475  N N   . ILE   A 1 57  ? 32.525  -5.557  -54.017 1.00 29.58 ? 59  ILE   A N   1 
ATOM   476  C CA  . ILE   A 1 57  ? 33.585  -4.819  -54.705 1.00 30.66 ? 59  ILE   A CA  1 
ATOM   477  C C   . ILE   A 1 57  ? 33.980  -5.435  -56.038 1.00 34.30 ? 59  ILE   A C   1 
ATOM   478  O O   . ILE   A 1 57  ? 34.702  -4.791  -56.809 1.00 34.63 ? 59  ILE   A O   1 
ATOM   479  C CB  . ILE   A 1 57  ? 34.842  -4.660  -53.826 1.00 30.09 ? 59  ILE   A CB  1 
ATOM   480  C CG1 . ILE   A 1 57  ? 35.460  -6.015  -53.478 1.00 28.80 ? 59  ILE   A CG1 1 
ATOM   481  C CG2 . ILE   A 1 57  ? 34.492  -3.899  -52.562 1.00 32.71 ? 59  ILE   A CG2 1 
ATOM   482  C CD1 . ILE   A 1 57  ? 36.874  -5.908  -52.896 1.00 36.40 ? 59  ILE   A CD1 1 
ATOM   483  N N   . THR   A 1 58  ? 33.521  -6.651  -56.349 1.00 33.24 ? 60  THR   A N   1 
ATOM   484  C CA  . THR   A 1 58  ? 33.788  -7.200  -57.675 1.00 37.85 ? 60  THR   A CA  1 
ATOM   485  C C   . THR   A 1 58  ? 32.877  -6.609  -58.745 1.00 42.01 ? 60  THR   A C   1 
ATOM   486  O O   . THR   A 1 58  ? 33.148  -6.799  -59.937 1.00 45.64 ? 60  THR   A O   1 
ATOM   487  C CB  . THR   A 1 58  ? 33.662  -8.731  -57.677 1.00 32.42 ? 60  THR   A CB  1 
ATOM   488  O OG1 . THR   A 1 58  ? 32.288  -9.112  -57.532 1.00 42.68 ? 60  THR   A OG1 1 
ATOM   489  C CG2 . THR   A 1 58  ? 34.491  -9.343  -56.552 1.00 40.56 ? 60  THR   A CG2 1 
ATOM   490  N N   . ASN   A 1 59  ? 31.823  -5.883  -58.350 1.00 43.22 ? 61  ASN   A N   1 
ATOM   491  C CA  . ASN   A 1 59  ? 30.966  -5.198  -59.311 1.00 41.80 ? 61  ASN   A CA  1 
ATOM   492  C C   . ASN   A 1 59  ? 30.449  -3.860  -58.790 1.00 41.42 ? 61  ASN   A C   1 
ATOM   493  O O   . ASN   A 1 59  ? 29.597  -3.249  -59.449 1.00 51.19 ? 61  ASN   A O   1 
ATOM   494  C CB  . ASN   A 1 59  ? 29.791  -6.096  -59.714 1.00 44.54 ? 61  ASN   A CB  1 
ATOM   495  C CG  . ASN   A 1 59  ? 28.998  -6.602  -58.519 1.00 51.02 ? 61  ASN   A CG  1 
ATOM   496  O OD1 . ASN   A 1 59  ? 28.960  -5.970  -57.463 1.00 47.48 ? 61  ASN   A OD1 1 
ATOM   497  N ND2 . ASN   A 1 59  ? 28.344  -7.745  -58.690 1.00 57.84 ? 61  ASN   A ND2 1 
ATOM   498  N N   . ASN   A 1 60  ? 30.933  -3.393  -57.636 1.00 44.70 ? 62  ASN   A N   1 
ATOM   499  C CA  . ASN   A 1 60  ? 30.536  -2.110  -57.040 1.00 45.29 ? 62  ASN   A CA  1 
ATOM   500  C C   . ASN   A 1 60  ? 29.018  -1.974  -56.908 1.00 47.62 ? 62  ASN   A C   1 
ATOM   501  O O   . ASN   A 1 60  ? 28.472  -0.873  -56.993 1.00 54.25 ? 62  ASN   A O   1 
ATOM   502  C CB  . ASN   A 1 60  ? 31.119  -0.926  -57.822 1.00 47.28 ? 62  ASN   A CB  1 
ATOM   503  C CG  . ASN   A 1 60  ? 32.532  -0.560  -57.367 1.00 54.48 ? 62  ASN   A CG  1 
ATOM   504  O OD1 . ASN   A 1 60  ? 33.184  -1.311  -56.632 1.00 45.56 ? 62  ASN   A OD1 1 
ATOM   505  N ND2 . ASN   A 1 60  ? 33.009  0.598   -57.807 1.00 59.40 ? 62  ASN   A ND2 1 
ATOM   506  N N   . GLU   A 1 61  ? 28.327  -3.087  -56.678 1.00 44.76 ? 63  GLU   A N   1 
ATOM   507  C CA  . GLU   A 1 61  ? 26.887  -3.081  -56.453 1.00 47.96 ? 63  GLU   A CA  1 
ATOM   508  C C   . GLU   A 1 61  ? 26.594  -3.165  -54.961 1.00 44.65 ? 63  GLU   A C   1 
ATOM   509  O O   . GLU   A 1 61  ? 27.287  -3.871  -54.222 1.00 40.03 ? 63  GLU   A O   1 
ATOM   510  C CB  . GLU   A 1 61  ? 26.211  -4.249  -57.176 1.00 54.00 ? 63  GLU   A CB  1 
ATOM   511  C CG  . GLU   A 1 61  ? 26.533  -4.346  -58.657 1.00 65.18 ? 63  GLU   A CG  1 
ATOM   512  C CD  . GLU   A 1 61  ? 25.602  -3.528  -59.527 1.00 73.80 ? 63  GLU   A CD  1 
ATOM   513  O OE1 . GLU   A 1 61  ? 25.394  -3.921  -60.694 1.00 75.10 ? 63  GLU   A OE1 1 
ATOM   514  O OE2 . GLU   A 1 61  ? 25.078  -2.498  -59.051 1.00 78.04 ? 63  GLU   A OE2 1 
ATOM   515  N N   . LYS   A 1 62  ? 25.568  -2.441  -54.518 1.00 41.60 ? 64  LYS   A N   1 
ATOM   516  C CA  . LYS   A 1 62  ? 25.123  -2.575  -53.139 1.00 35.08 ? 64  LYS   A CA  1 
ATOM   517  C C   . LYS   A 1 62  ? 24.491  -3.945  -52.929 1.00 31.07 ? 64  LYS   A C   1 
ATOM   518  O O   . LYS   A 1 62  ? 23.767  -4.453  -53.789 1.00 30.04 ? 64  LYS   A O   1 
ATOM   519  C CB  . LYS   A 1 62  ? 24.116  -1.479  -52.777 1.00 42.62 ? 64  LYS   A CB  1 
ATOM   520  C CG  . LYS   A 1 62  ? 24.584  -0.058  -53.060 1.00 49.98 ? 64  LYS   A CG  1 
ATOM   521  C CD  . LYS   A 1 62  ? 23.542  0.977   -52.635 1.00 54.00 ? 64  LYS   A CD  1 
ATOM   522  C CE  . LYS   A 1 62  ? 23.612  1.263   -51.143 1.00 56.13 ? 64  LYS   A CE  1 
ATOM   523  N NZ  . LYS   A 1 62  ? 22.769  2.424   -50.739 1.00 56.42 ? 64  LYS   A NZ  1 
ATOM   524  N N   . VAL   A 1 63  ? 24.773  -4.547  -51.778 1.00 26.37 ? 65  VAL   A N   1 
ATOM   525  C CA  . VAL   A 1 63  ? 24.140  -5.773  -51.337 1.00 26.90 ? 65  VAL   A CA  1 
ATOM   526  C C   . VAL   A 1 63  ? 23.749  -5.597  -49.874 1.00 23.09 ? 65  VAL   A C   1 
ATOM   527  O O   . VAL   A 1 63  ? 24.076  -4.595  -49.237 1.00 24.55 ? 65  VAL   A O   1 
ATOM   528  C CB  . VAL   A 1 63  ? 25.046  -7.009  -51.521 1.00 23.92 ? 65  VAL   A CB  1 
ATOM   529  C CG1 . VAL   A 1 63  ? 25.301  -7.278  -53.004 1.00 28.57 ? 65  VAL   A CG1 1 
ATOM   530  C CG2 . VAL   A 1 63  ? 26.375  -6.831  -50.777 1.00 24.94 ? 65  VAL   A CG2 1 
ATOM   531  N N   . VAL   A 1 64  ? 23.063  -6.598  -49.337 1.00 22.37 ? 66  VAL   A N   1 
ATOM   532  C CA  . VAL   A 1 64  ? 22.694  -6.622  -47.928 1.00 21.12 ? 66  VAL   A CA  1 
ATOM   533  C C   . VAL   A 1 64  ? 23.235  -7.913  -47.334 1.00 23.28 ? 66  VAL   A C   1 
ATOM   534  O O   . VAL   A 1 64  ? 23.060  -8.990  -47.916 1.00 23.86 ? 66  VAL   A O   1 
ATOM   535  C CB  . VAL   A 1 64  ? 21.170  -6.501  -47.744 1.00 20.55 ? 66  VAL   A CB  1 
ATOM   536  C CG1 . VAL   A 1 64  ? 20.778  -6.874  -46.329 1.00 20.36 ? 66  VAL   A CG1 1 
ATOM   537  C CG2 . VAL   A 1 64  ? 20.742  -5.066  -48.054 1.00 21.90 ? 66  VAL   A CG2 1 
ATOM   538  N N   . VAL   A 1 65  ? 23.937  -7.801  -46.210 1.00 20.76 ? 67  VAL   A N   1 
ATOM   539  C CA  . VAL   A 1 65  ? 24.608  -8.937  -45.597 1.00 19.92 ? 67  VAL   A CA  1 
ATOM   540  C C   . VAL   A 1 65  ? 23.972  -9.197  -44.241 1.00 20.22 ? 67  VAL   A C   1 
ATOM   541  O O   . VAL   A 1 65  ? 23.994  -8.322  -43.363 1.00 22.00 ? 67  VAL   A O   1 
ATOM   542  C CB  . VAL   A 1 65  ? 26.113  -8.686  -45.438 1.00 21.99 ? 67  VAL   A CB  1 
ATOM   543  C CG1 . VAL   A 1 65  ? 26.774  -9.903  -44.801 1.00 24.79 ? 67  VAL   A CG1 1 
ATOM   544  C CG2 . VAL   A 1 65  ? 26.730  -8.354  -46.782 1.00 24.29 ? 67  VAL   A CG2 1 
ATOM   545  N N   . LYS   A 1 66  ? 23.464  -10.413 -44.051 1.00 22.04 ? 68  LYS   A N   1 
ATOM   546  C CA  . LYS   A 1 66  ? 22.912  -10.862 -42.773 1.00 18.58 ? 68  LYS   A CA  1 
ATOM   547  C C   . LYS   A 1 66  ? 23.918  -11.817 -42.126 1.00 20.51 ? 68  LYS   A C   1 
ATOM   548  O O   . LYS   A 1 66  ? 24.131  -12.933 -42.613 1.00 20.11 ? 68  LYS   A O   1 
ATOM   549  C CB  . LYS   A 1 66  ? 21.549  -11.532 -42.983 1.00 20.37 ? 68  LYS   A CB  1 
ATOM   550  C CG  . LYS   A 1 66  ? 20.954  -12.081 -41.700 1.00 21.29 ? 68  LYS   A CG  1 
ATOM   551  C CD  . LYS   A 1 66  ? 19.472  -12.343 -41.835 1.00 27.07 ? 68  LYS   A CD  1 
ATOM   552  C CE  . LYS   A 1 66  ? 19.177  -13.631 -42.555 1.00 28.52 ? 68  LYS   A CE  1 
ATOM   553  N NZ  . LYS   A 1 66  ? 17.704  -13.915 -42.428 1.00 27.63 ? 68  LYS   A NZ  1 
ATOM   554  N N   . ILE   A 1 67  ? 24.535  -11.386 -41.033 1.00 20.19 ? 69  ILE   A N   1 
ATOM   555  C CA  . ILE   A 1 67  ? 25.531  -12.194 -40.337 1.00 20.89 ? 69  ILE   A CA  1 
ATOM   556  C C   . ILE   A 1 67  ? 24.840  -12.874 -39.167 1.00 23.79 ? 69  ILE   A C   1 
ATOM   557  O O   . ILE   A 1 67  ? 24.390  -12.204 -38.230 1.00 27.09 ? 69  ILE   A O   1 
ATOM   558  C CB  . ILE   A 1 67  ? 26.717  -11.347 -39.851 1.00 21.99 ? 69  ILE   A CB  1 
ATOM   559  C CG1 . ILE   A 1 67  ? 27.328  -10.546 -41.005 1.00 21.53 ? 69  ILE   A CG1 1 
ATOM   560  C CG2 . ILE   A 1 67  ? 27.768  -12.250 -39.209 1.00 26.29 ? 69  ILE   A CG2 1 
ATOM   561  C CD1 . ILE   A 1 67  ? 28.497  -9.697  -40.581 1.00 23.44 ? 69  ILE   A CD1 1 
ATOM   562  N N   . LEU   A 1 68  ? 24.771  -14.199 -39.206 1.00 25.37 ? 70  LEU   A N   1 
ATOM   563  C CA  . LEU   A 1 68  ? 24.000  -14.927 -38.209 1.00 27.71 ? 70  LEU   A CA  1 
ATOM   564  C C   . LEU   A 1 68  ? 24.692  -14.917 -36.853 1.00 29.20 ? 70  LEU   A C   1 
ATOM   565  O O   . LEU   A 1 68  ? 25.922  -14.984 -36.759 1.00 33.62 ? 70  LEU   A O   1 
ATOM   566  C CB  . LEU   A 1 68  ? 23.786  -16.369 -38.660 1.00 29.06 ? 70  LEU   A CB  1 
ATOM   567  C CG  . LEU   A 1 68  ? 23.163  -16.547 -40.045 1.00 35.33 ? 70  LEU   A CG  1 
ATOM   568  C CD1 . LEU   A 1 68  ? 22.825  -18.008 -40.258 1.00 33.41 ? 70  LEU   A CD1 1 
ATOM   569  C CD2 . LEU   A 1 68  ? 21.934  -15.667 -40.217 1.00 41.09 ? 70  LEU   A CD2 1 
ATOM   570  N N   . LYS   A 1 69  ? 23.896  -14.817 -35.800 1.00 31.46 ? 71  LYS   A N   1 
ATOM   571  C CA  . LYS   A 1 69  ? 24.386  -15.186 -34.488 1.00 32.18 ? 71  LYS   A CA  1 
ATOM   572  C C   . LYS   A 1 69  ? 24.317  -16.705 -34.369 1.00 40.99 ? 71  LYS   A C   1 
ATOM   573  O O   . LYS   A 1 69  ? 23.716  -17.367 -35.216 1.00 37.04 ? 71  LYS   A O   1 
ATOM   574  C CB  . LYS   A 1 69  ? 23.566  -14.482 -33.409 1.00 31.72 ? 71  LYS   A CB  1 
ATOM   575  C CG  . LYS   A 1 69  ? 23.730  -12.967 -33.448 1.00 37.39 ? 71  LYS   A CG  1 
ATOM   576  C CD  . LYS   A 1 69  ? 22.820  -12.266 -32.460 1.00 44.21 ? 71  LYS   A CD  1 
ATOM   577  C CE  . LYS   A 1 69  ? 22.957  -10.757 -32.586 1.00 45.00 ? 71  LYS   A CE  1 
ATOM   578  N NZ  . LYS   A 1 69  ? 22.186  -10.032 -31.541 1.00 49.46 ? 71  LYS   A NZ  1 
ATOM   579  N N   . PRO   A 1 70  ? 24.971  -17.294 -33.371 1.00 54.41 ? 72  PRO   A N   1 
ATOM   580  C CA  . PRO   A 1 70  ? 24.944  -18.758 -33.257 1.00 59.93 ? 72  PRO   A CA  1 
ATOM   581  C C   . PRO   A 1 70  ? 23.523  -19.297 -33.147 1.00 61.19 ? 72  PRO   A C   1 
ATOM   582  O O   . PRO   A 1 70  ? 22.726  -18.844 -32.323 1.00 64.27 ? 72  PRO   A O   1 
ATOM   583  C CB  . PRO   A 1 70  ? 25.759  -19.022 -31.987 1.00 61.11 ? 72  PRO   A CB  1 
ATOM   584  C CG  . PRO   A 1 70  ? 26.740  -17.900 -31.967 1.00 59.08 ? 72  PRO   A CG  1 
ATOM   585  C CD  . PRO   A 1 70  ? 25.978  -16.700 -32.473 1.00 56.24 ? 72  PRO   A CD  1 
ATOM   586  N N   . VAL   A 1 71  ? 23.210  -20.262 -34.013 1.00 59.03 ? 73  VAL   A N   1 
ATOM   587  C CA  . VAL   A 1 71  ? 21.928  -20.956 -34.013 1.00 58.23 ? 73  VAL   A CA  1 
ATOM   588  C C   . VAL   A 1 71  ? 22.166  -22.319 -34.648 1.00 55.67 ? 73  VAL   A C   1 
ATOM   589  O O   . VAL   A 1 71  ? 23.144  -22.521 -35.369 1.00 51.56 ? 73  VAL   A O   1 
ATOM   590  C CB  . VAL   A 1 71  ? 20.835  -20.158 -34.768 1.00 56.26 ? 73  VAL   A CB  1 
ATOM   591  C CG1 . VAL   A 1 71  ? 21.176  -20.047 -36.243 1.00 49.85 ? 73  VAL   A CG1 1 
ATOM   592  C CG2 . VAL   A 1 71  ? 19.450  -20.778 -34.562 1.00 62.32 ? 73  VAL   A CG2 1 
ATOM   593  N N   . LYS   A 1 72  ? 21.274  -23.267 -34.356 1.00 56.29 ? 74  LYS   A N   1 
ATOM   594  C CA  . LYS   A 1 72  ? 21.440  -24.639 -34.826 1.00 57.33 ? 74  LYS   A CA  1 
ATOM   595  C C   . LYS   A 1 72  ? 21.703  -24.676 -36.324 1.00 48.76 ? 74  LYS   A C   1 
ATOM   596  O O   . LYS   A 1 72  ? 21.000  -24.029 -37.107 1.00 41.39 ? 74  LYS   A O   1 
ATOM   597  C CB  . LYS   A 1 72  ? 20.197  -25.463 -34.486 1.00 63.14 ? 74  LYS   A CB  1 
ATOM   598  C CG  . LYS   A 1 72  ? 20.106  -25.839 -33.021 1.00 68.36 ? 74  LYS   A CG  1 
ATOM   599  C CD  . LYS   A 1 72  ? 18.905  -25.200 -32.350 1.00 68.67 ? 74  LYS   A CD  1 
ATOM   600  C CE  . LYS   A 1 72  ? 17.613  -25.865 -32.786 1.00 67.81 ? 74  LYS   A CE  1 
ATOM   601  N NZ  . LYS   A 1 72  ? 16.692  -26.074 -31.632 1.00 68.11 ? 74  LYS   A NZ  1 
ATOM   602  N N   . LYS   A 1 73  ? 22.744  -25.421 -36.713 1.00 42.32 ? 75  LYS   A N   1 
ATOM   603  C CA  . LYS   A 1 73  ? 23.125  -25.506 -38.120 1.00 45.45 ? 75  LYS   A CA  1 
ATOM   604  C C   . LYS   A 1 73  ? 21.987  -26.044 -38.970 1.00 39.69 ? 75  LYS   A C   1 
ATOM   605  O O   . LYS   A 1 73  ? 21.909  -25.742 -40.166 1.00 41.00 ? 75  LYS   A O   1 
ATOM   606  C CB  . LYS   A 1 73  ? 24.368  -26.387 -38.283 1.00 52.83 ? 75  LYS   A CB  1 
ATOM   607  C CG  . LYS   A 1 73  ? 25.649  -25.779 -37.722 1.00 62.87 ? 75  LYS   A CG  1 
ATOM   608  C CD  . LYS   A 1 73  ? 26.125  -24.589 -38.544 1.00 67.27 ? 75  LYS   A CD  1 
ATOM   609  C CE  . LYS   A 1 73  ? 27.110  -24.999 -39.633 1.00 66.76 ? 75  LYS   A CE  1 
ATOM   610  N NZ  . LYS   A 1 73  ? 27.305  -23.910 -40.642 1.00 62.94 ? 75  LYS   A NZ  1 
ATOM   611  N N   . LYS   A 1 74  ? 21.114  -26.857 -38.373 1.00 33.21 ? 76  LYS   A N   1 
ATOM   612  C CA  . LYS   A 1 74  ? 19.922  -27.324 -39.067 1.00 31.86 ? 76  LYS   A CA  1 
ATOM   613  C C   . LYS   A 1 74  ? 19.093  -26.153 -39.576 1.00 31.71 ? 76  LYS   A C   1 
ATOM   614  O O   . LYS   A 1 74  ? 18.602  -26.175 -40.712 1.00 32.42 ? 76  LYS   A O   1 
ATOM   615  C CB  . LYS   A 1 74  ? 19.102  -28.198 -38.117 1.00 43.82 ? 76  LYS   A CB  1 
ATOM   616  C CG  . LYS   A 1 74  ? 18.162  -29.166 -38.779 1.00 53.62 ? 76  LYS   A CG  1 
ATOM   617  C CD  . LYS   A 1 74  ? 17.378  -29.940 -37.735 1.00 59.70 ? 76  LYS   A CD  1 
ATOM   618  C CE  . LYS   A 1 74  ? 16.608  -28.998 -36.825 1.00 62.29 ? 76  LYS   A CE  1 
ATOM   619  N NZ  . LYS   A 1 74  ? 15.670  -28.132 -37.592 1.00 65.60 ? 76  LYS   A NZ  1 
ATOM   620  N N   . LYS   A 1 75  ? 18.931  -25.115 -38.750 1.00 30.30 ? 77  LYS   A N   1 
ATOM   621  C CA  . LYS   A 1 75  ? 18.097  -23.979 -39.140 1.00 30.69 ? 77  LYS   A CA  1 
ATOM   622  C C   . LYS   A 1 75  ? 18.814  -23.071 -40.134 1.00 25.67 ? 77  LYS   A C   1 
ATOM   623  O O   . LYS   A 1 75  ? 18.161  -22.439 -40.978 1.00 27.38 ? 77  LYS   A O   1 
ATOM   624  C CB  . LYS   A 1 75  ? 17.666  -23.198 -37.893 1.00 40.12 ? 77  LYS   A CB  1 
ATOM   625  C CG  . LYS   A 1 75  ? 17.879  -21.677 -37.957 1.00 52.23 ? 77  LYS   A CG  1 
ATOM   626  C CD  . LYS   A 1 75  ? 16.719  -20.940 -38.643 1.00 54.84 ? 77  LYS   A CD  1 
ATOM   627  C CE  . LYS   A 1 75  ? 17.141  -19.557 -39.160 1.00 43.35 ? 77  LYS   A CE  1 
ATOM   628  N NZ  . LYS   A 1 75  ? 18.303  -19.590 -40.122 1.00 32.74 ? 77  LYS   A NZ  1 
ATOM   629  N N   . ILE   A 1 76  ? 20.144  -22.985 -40.046 1.00 26.66 ? 78  ILE   A N   1 
ATOM   630  C CA  . ILE   A 1 76  ? 20.906  -22.242 -41.043 1.00 27.35 ? 78  ILE   A CA  1 
ATOM   631  C C   . ILE   A 1 76  ? 20.783  -22.913 -42.402 1.00 25.90 ? 78  ILE   A C   1 
ATOM   632  O O   . ILE   A 1 76  ? 20.559  -22.255 -43.426 1.00 24.61 ? 78  ILE   A O   1 
ATOM   633  C CB  . ILE   A 1 76  ? 22.381  -22.120 -40.615 1.00 28.85 ? 78  ILE   A CB  1 
ATOM   634  C CG1 . ILE   A 1 76  ? 22.494  -21.431 -39.256 1.00 29.58 ? 78  ILE   A CG1 1 
ATOM   635  C CG2 . ILE   A 1 76  ? 23.160  -21.347 -41.666 1.00 32.68 ? 78  ILE   A CG2 1 
ATOM   636  C CD1 . ILE   A 1 76  ? 23.905  -21.479 -38.664 1.00 34.13 ? 78  ILE   A CD1 1 
ATOM   637  N N   . LYS   A 1 77  ? 20.955  -24.239 -42.435 1.00 26.55 ? 79  LYS   A N   1 
ATOM   638  C CA  . LYS   A 1 77  ? 20.796  -24.976 -43.684 1.00 27.04 ? 79  LYS   A CA  1 
ATOM   639  C C   . LYS   A 1 77  ? 19.367  -24.896 -44.204 1.00 25.37 ? 79  LYS   A C   1 
ATOM   640  O O   . LYS   A 1 77  ? 19.145  -24.881 -45.418 1.00 25.51 ? 79  LYS   A O   1 
ATOM   641  C CB  . LYS   A 1 77  ? 21.208  -26.436 -43.496 1.00 27.98 ? 79  LYS   A CB  1 
ATOM   642  C CG  . LYS   A 1 77  ? 22.714  -26.626 -43.321 1.00 29.57 ? 79  LYS   A CG  1 
ATOM   643  C CD  . LYS   A 1 77  ? 23.082  -28.082 -43.526 1.00 34.51 ? 79  LYS   A CD  1 
ATOM   644  C CE  . LYS   A 1 77  ? 24.563  -28.311 -43.305 1.00 45.19 ? 79  LYS   A CE  1 
ATOM   645  N NZ  . LYS   A 1 77  ? 24.891  -29.749 -43.492 1.00 52.68 ? 79  LYS   A NZ  1 
ATOM   646  N N   . ARG   A 1 78  ? 18.382  -24.869 -43.304 1.00 22.62 ? 80  ARG   A N   1 
ATOM   647  C CA  . ARG   A 1 78  ? 16.995  -24.770 -43.745 1.00 22.82 ? 80  ARG   A CA  1 
ATOM   648  C C   . ARG   A 1 78  ? 16.761  -23.465 -44.495 1.00 21.94 ? 80  ARG   A C   1 
ATOM   649  O O   . ARG   A 1 78  ? 16.195  -23.460 -45.596 1.00 22.25 ? 80  ARG   A O   1 
ATOM   650  C CB  . ARG   A 1 78  ? 16.055  -24.870 -42.541 1.00 21.77 ? 80  ARG   A CB  1 
ATOM   651  C CG  . ARG   A 1 78  ? 14.587  -24.896 -42.900 1.00 25.26 ? 80  ARG   A CG  1 
ATOM   652  C CD  . ARG   A 1 78  ? 13.723  -24.988 -41.643 1.00 24.33 ? 80  ARG   A CD  1 
ATOM   653  N NE  . ARG   A 1 78  ? 13.817  -23.766 -40.842 1.00 28.12 ? 80  ARG   A NE  1 
ATOM   654  C CZ  . ARG   A 1 78  ? 13.328  -23.635 -39.615 1.00 31.89 ? 80  ARG   A CZ  1 
ATOM   655  N NH1 . ARG   A 1 78  ? 12.743  -24.666 -39.024 1.00 27.86 ? 80  ARG   A NH1 1 
ATOM   656  N NH2 . ARG   A 1 78  ? 13.435  -22.474 -38.975 1.00 29.10 ? 80  ARG   A NH2 1 
ATOM   657  N N   . GLU   A 1 79  ? 17.196  -22.343 -43.905 1.00 21.78 ? 81  GLU   A N   1 
ATOM   658  C CA  . GLU   A 1 79  ? 17.002  -21.046 -44.553 1.00 21.63 ? 81  GLU   A CA  1 
ATOM   659  C C   . GLU   A 1 79  ? 17.765  -20.973 -45.870 1.00 23.38 ? 81  GLU   A C   1 
ATOM   660  O O   . GLU   A 1 79  ? 17.234  -20.478 -46.869 1.00 22.37 ? 81  GLU   A O   1 
ATOM   661  C CB  . GLU   A 1 79  ? 17.419  -19.903 -43.629 1.00 21.73 ? 81  GLU   A CB  1 
ATOM   662  C CG  . GLU   A 1 79  ? 17.207  -18.518 -44.260 1.00 21.14 ? 81  GLU   A CG  1 
ATOM   663  C CD  . GLU   A 1 79  ? 17.546  -17.360 -43.341 1.00 24.46 ? 81  GLU   A CD  1 
ATOM   664  O OE1 . GLU   A 1 79  ? 17.925  -17.591 -42.174 1.00 27.38 ? 81  GLU   A OE1 1 
ATOM   665  O OE2 . GLU   A 1 79  ? 17.435  -16.196 -43.787 1.00 26.28 ? 81  GLU   A OE2 1 
ATOM   666  N N   . ILE   A 1 80  ? 19.013  -21.456 -45.890 1.00 22.54 ? 82  ILE   A N   1 
ATOM   667  C CA  . ILE   A 1 80  ? 19.794  -21.445 -47.129 1.00 22.33 ? 82  ILE   A CA  1 
ATOM   668  C C   . ILE   A 1 80  ? 19.109  -22.271 -48.212 1.00 20.06 ? 82  ILE   A C   1 
ATOM   669  O O   . ILE   A 1 80  ? 18.967  -21.825 -49.358 1.00 23.05 ? 82  ILE   A O   1 
ATOM   670  C CB  . ILE   A 1 80  ? 21.225  -21.951 -46.878 1.00 20.65 ? 82  ILE   A CB  1 
ATOM   671  C CG1 . ILE   A 1 80  ? 22.033  -20.904 -46.112 1.00 21.63 ? 82  ILE   A CG1 1 
ATOM   672  C CG2 . ILE   A 1 80  ? 21.883  -22.307 -48.213 1.00 27.41 ? 82  ILE   A CG2 1 
ATOM   673  C CD1 . ILE   A 1 80  ? 23.401  -21.405 -45.595 1.00 25.94 ? 82  ILE   A CD1 1 
ATOM   674  N N   . LYS   A 1 81  ? 18.671  -23.491 -47.873 1.00 20.89 ? 83  LYS   A N   1 
ATOM   675  C CA  . LYS   A 1 81  ? 18.043  -24.353 -48.874 1.00 21.82 ? 83  LYS   A CA  1 
ATOM   676  C C   . LYS   A 1 81  ? 16.769  -23.730 -49.432 1.00 21.13 ? 83  LYS   A C   1 
ATOM   677  O O   . LYS   A 1 81  ? 16.516  -23.784 -50.642 1.00 22.91 ? 83  LYS   A O   1 
ATOM   678  C CB  . LYS   A 1 81  ? 17.740  -25.728 -48.277 1.00 26.04 ? 83  LYS   A CB  1 
ATOM   679  C CG  . LYS   A 1 81  ? 17.232  -26.736 -49.310 1.00 24.60 ? 83  LYS   A CG  1 
ATOM   680  C CD  . LYS   A 1 81  ? 18.324  -27.024 -50.333 1.00 31.94 ? 83  LYS   A CD  1 
ATOM   681  C CE  . LYS   A 1 81  ? 17.804  -27.850 -51.495 1.00 34.11 ? 83  LYS   A CE  1 
ATOM   682  N NZ  . LYS   A 1 81  ? 18.931  -28.201 -52.399 1.00 37.00 ? 83  LYS   A NZ  1 
ATOM   683  N N   . ILE   A 1 82  ? 15.965  -23.114 -48.562 1.00 20.30 ? 84  ILE   A N   1 
ATOM   684  C CA  . ILE   A 1 82  ? 14.719  -22.492 -48.996 1.00 21.05 ? 84  ILE   A CA  1 
ATOM   685  C C   . ILE   A 1 82  ? 15.005  -21.321 -49.934 1.00 19.94 ? 84  ILE   A C   1 
ATOM   686  O O   . ILE   A 1 82  ? 14.368  -21.174 -50.986 1.00 22.16 ? 84  ILE   A O   1 
ATOM   687  C CB  . ILE   A 1 82  ? 13.896  -22.074 -47.761 1.00 20.76 ? 84  ILE   A CB  1 
ATOM   688  C CG1 . ILE   A 1 82  ? 13.301  -23.339 -47.122 1.00 24.13 ? 84  ILE   A CG1 1 
ATOM   689  C CG2 . ILE   A 1 82  ? 12.827  -21.022 -48.121 1.00 20.69 ? 84  ILE   A CG2 1 
ATOM   690  C CD1 . ILE   A 1 82  ? 12.587  -23.130 -45.793 1.00 21.26 ? 84  ILE   A CD1 1 
ATOM   691  N N   . LEU   A 1 83  ? 15.960  -20.467 -49.561 1.00 19.97 ? 85  LEU   A N   1 
ATOM   692  C CA  . LEU   A 1 83  ? 16.325  -19.336 -50.413 1.00 18.76 ? 85  LEU   A CA  1 
ATOM   693  C C   . LEU   A 1 83  ? 16.833  -19.796 -51.777 1.00 20.73 ? 85  LEU   A C   1 
ATOM   694  O O   . LEU   A 1 83  ? 16.509  -19.188 -52.802 1.00 20.65 ? 85  LEU   A O   1 
ATOM   695  C CB  . LEU   A 1 83  ? 17.388  -18.484 -49.720 1.00 20.18 ? 85  LEU   A CB  1 
ATOM   696  C CG  . LEU   A 1 83  ? 16.912  -17.639 -48.544 1.00 20.37 ? 85  LEU   A CG  1 
ATOM   697  C CD1 . LEU   A 1 83  ? 18.116  -17.152 -47.748 1.00 23.66 ? 85  LEU   A CD1 1 
ATOM   698  C CD2 . LEU   A 1 83  ? 16.071  -16.467 -49.067 1.00 22.72 ? 85  LEU   A CD2 1 
ATOM   699  N N   . GLU   A 1 84  ? 17.631  -20.867 -51.813 1.00 23.29 ? 86  GLU   A N   1 
ATOM   700  C CA  . GLU   A 1 84  ? 18.095  -21.371 -53.107 1.00 24.10 ? 86  GLU   A CA  1 
ATOM   701  C C   . GLU   A 1 84  ? 16.957  -22.011 -53.907 1.00 24.36 ? 86  GLU   A C   1 
ATOM   702  O O   . GLU   A 1 84  ? 16.879  -21.846 -55.132 1.00 24.47 ? 86  GLU   A O   1 
ATOM   703  C CB  . GLU   A 1 84  ? 19.247  -22.348 -52.900 1.00 21.71 ? 86  GLU   A CB  1 
ATOM   704  C CG  . GLU   A 1 84  ? 20.504  -21.651 -52.377 1.00 27.25 ? 86  GLU   A CG  1 
ATOM   705  C CD  . GLU   A 1 84  ? 21.671  -22.598 -52.177 1.00 36.86 ? 86  GLU   A CD  1 
ATOM   706  O OE1 . GLU   A 1 84  ? 21.465  -23.833 -52.244 1.00 41.98 ? 86  GLU   A OE1 1 
ATOM   707  O OE2 . GLU   A 1 84  ? 22.795  -22.100 -51.949 1.00 40.40 ? 86  GLU   A OE2 1 
ATOM   708  N N   . ASN   A 1 85  ? 16.057  -22.733 -53.238 1.00 23.30 ? 87  ASN   A N   1 
ATOM   709  C CA  . ASN   A 1 85  ? 14.916  -23.321 -53.943 1.00 21.65 ? 87  ASN   A CA  1 
ATOM   710  C C   . ASN   A 1 85  ? 14.023  -22.255 -54.572 1.00 23.03 ? 87  ASN   A C   1 
ATOM   711  O O   . ASN   A 1 85  ? 13.474  -22.461 -55.662 1.00 23.62 ? 87  ASN   A O   1 
ATOM   712  C CB  . ASN   A 1 85  ? 14.094  -24.192 -52.990 1.00 22.51 ? 87  ASN   A CB  1 
ATOM   713  C CG  . ASN   A 1 85  ? 14.768  -25.521 -52.679 1.00 22.88 ? 87  ASN   A CG  1 
ATOM   714  O OD1 . ASN   A 1 85  ? 15.756  -25.894 -53.308 1.00 24.89 ? 87  ASN   A OD1 1 
ATOM   715  N ND2 . ASN   A 1 85  ? 14.220  -26.247 -51.715 1.00 24.05 ? 87  ASN   A ND2 1 
ATOM   716  N N   . LEU   A 1 86  ? 13.851  -21.116 -53.896 1.00 21.24 ? 88  LEU   A N   1 
ATOM   717  C CA  . LEU   A 1 86  ? 12.911  -20.083 -54.313 1.00 20.43 ? 88  LEU   A CA  1 
ATOM   718  C C   . LEU   A 1 86  ? 13.543  -19.010 -55.191 1.00 23.12 ? 88  LEU   A C   1 
ATOM   719  O O   . LEU   A 1 86  ? 12.811  -18.169 -55.726 1.00 23.23 ? 88  LEU   A O   1 
ATOM   720  C CB  . LEU   A 1 86  ? 12.279  -19.396 -53.088 1.00 19.72 ? 88  LEU   A CB  1 
ATOM   721  C CG  . LEU   A 1 86  ? 11.442  -20.291 -52.179 1.00 20.68 ? 88  LEU   A CG  1 
ATOM   722  C CD1 . LEU   A 1 86  ? 10.927  -19.507 -50.970 1.00 21.56 ? 88  LEU   A CD1 1 
ATOM   723  C CD2 . LEU   A 1 86  ? 10.310  -20.898 -52.985 1.00 21.85 ? 88  LEU   A CD2 1 
ATOM   724  N N   . ARG   A 1 87  ? 14.869  -19.023 -55.340 1.00 20.88 ? 89  ARG   A N   1 
ATOM   725  C CA  . ARG   A 1 87  ? 15.573  -17.960 -56.052 1.00 20.54 ? 89  ARG   A CA  1 
ATOM   726  C C   . ARG   A 1 87  ? 15.037  -17.807 -57.470 1.00 25.09 ? 89  ARG   A C   1 
ATOM   727  O O   . ARG   A 1 87  ? 14.857  -18.794 -58.189 1.00 24.80 ? 89  ARG   A O   1 
ATOM   728  C CB  . ARG   A 1 87  ? 17.072  -18.260 -56.084 1.00 22.42 ? 89  ARG   A CB  1 
ATOM   729  C CG  . ARG   A 1 87  ? 17.910  -17.105 -56.625 1.00 23.85 ? 89  ARG   A CG  1 
ATOM   730  C CD  . ARG   A 1 87  ? 19.351  -17.211 -56.126 1.00 28.01 ? 89  ARG   A CD  1 
ATOM   731  N NE  . ARG   A 1 87  ? 19.878  -18.563 -56.285 1.00 30.18 ? 89  ARG   A NE  1 
ATOM   732  C CZ  . ARG   A 1 87  ? 20.877  -19.060 -55.561 1.00 33.29 ? 89  ARG   A CZ  1 
ATOM   733  N NH1 . ARG   A 1 87  ? 21.455  -18.314 -54.623 1.00 31.92 ? 89  ARG   A NH1 1 
ATOM   734  N NH2 . ARG   A 1 87  ? 21.298  -20.304 -55.769 1.00 34.40 ? 89  ARG   A NH2 1 
ATOM   735  N N   . GLY   A 1 88  ? 14.799  -16.554 -57.871 1.00 22.90 ? 90  GLY   A N   1 
ATOM   736  C CA  . GLY   A 1 88  ? 14.232  -16.237 -59.166 1.00 24.80 ? 90  GLY   A CA  1 
ATOM   737  C C   . GLY   A 1 88  ? 12.718  -16.166 -59.203 1.00 28.12 ? 90  GLY   A C   1 
ATOM   738  O O   . GLY   A 1 88  ? 12.156  -15.670 -60.189 1.00 25.92 ? 90  GLY   A O   1 
ATOM   739  N N   . GLY   A 1 89  ? 12.040  -16.642 -58.164 1.00 20.61 ? 91  GLY   A N   1 
ATOM   740  C CA  . GLY   A 1 89  ? 10.598  -16.601 -58.110 1.00 20.47 ? 91  GLY   A CA  1 
ATOM   741  C C   . GLY   A 1 89  ? 10.090  -15.183 -57.954 1.00 22.11 ? 91  GLY   A C   1 
ATOM   742  O O   . GLY   A 1 89  ? 10.822  -14.276 -57.543 1.00 20.72 ? 91  GLY   A O   1 
ATOM   743  N N   . PRO   A 1 90  ? 8.815   -14.965 -58.266 1.00 20.86 ? 92  PRO   A N   1 
ATOM   744  C CA  . PRO   A 1 90  ? 8.259   -13.605 -58.243 1.00 17.41 ? 92  PRO   A CA  1 
ATOM   745  C C   . PRO   A 1 90  ? 8.330   -12.978 -56.861 1.00 17.90 ? 92  PRO   A C   1 
ATOM   746  O O   . PRO   A 1 90  ? 7.753   -13.489 -55.895 1.00 20.57 ? 92  PRO   A O   1 
ATOM   747  C CB  . PRO   A 1 90  ? 6.795   -13.809 -58.669 1.00 23.94 ? 92  PRO   A CB  1 
ATOM   748  C CG  . PRO   A 1 90  ? 6.714   -15.186 -59.194 1.00 31.24 ? 92  PRO   A CG  1 
ATOM   749  C CD  . PRO   A 1 90  ? 7.801   -15.982 -58.572 1.00 25.63 ? 92  PRO   A CD  1 
ATOM   750  N N   . ASN   A 1 91  ? 9.022   -11.841 -56.781 1.00 19.07 ? 93  ASN   A N   1 
ATOM   751  C CA  . ASN   A 1 91  ? 9.063   -10.999 -55.585 1.00 18.24 ? 93  ASN   A CA  1 
ATOM   752  C C   . ASN   A 1 91  ? 9.679   -11.707 -54.378 1.00 22.33 ? 93  ASN   A C   1 
ATOM   753  O O   . ASN   A 1 91  ? 9.431   -11.313 -53.238 1.00 22.30 ? 93  ASN   A O   1 
ATOM   754  C CB  . ASN   A 1 91  ? 7.660   -10.472 -55.260 1.00 21.80 ? 93  ASN   A CB  1 
ATOM   755  C CG  . ASN   A 1 91  ? 7.105   -9.600  -56.379 1.00 22.63 ? 93  ASN   A CG  1 
ATOM   756  O OD1 . ASN   A 1 91  ? 7.866   -8.949  -57.106 1.00 23.94 ? 93  ASN   A OD1 1 
ATOM   757  N ND2 . ASN   A 1 91  ? 5.793   -9.589  -56.531 1.00 19.85 ? 93  ASN   A ND2 1 
ATOM   758  N N   . ILE   A 1 92  ? 10.487  -12.737 -54.617 1.00 19.32 ? 94  ILE   A N   1 
ATOM   759  C CA  . ILE   A 1 92  ? 11.267  -13.407 -53.574 1.00 16.65 ? 94  ILE   A CA  1 
ATOM   760  C C   . ILE   A 1 92  ? 12.641  -12.749 -53.525 1.00 17.23 ? 94  ILE   A C   1 
ATOM   761  O O   . ILE   A 1 92  ? 13.294  -12.619 -54.566 1.00 19.19 ? 94  ILE   A O   1 
ATOM   762  C CB  . ILE   A 1 92  ? 11.402  -14.910 -53.885 1.00 21.30 ? 94  ILE   A CB  1 
ATOM   763  C CG1 . ILE   A 1 92  ? 10.035  -15.562 -54.126 1.00 25.88 ? 94  ILE   A CG1 1 
ATOM   764  C CG2 . ILE   A 1 92  ? 12.193  -15.624 -52.788 1.00 23.26 ? 94  ILE   A CG2 1 
ATOM   765  C CD1 . ILE   A 1 92  ? 9.187   -15.650 -52.912 1.00 22.96 ? 94  ILE   A CD1 1 
ATOM   766  N N   . ILE   A 1 93  ? 13.096  -12.355 -52.322 1.00 16.02 ? 95  ILE   A N   1 
ATOM   767  C CA  . ILE   A 1 93  ? 14.439  -11.787 -52.193 1.00 16.80 ? 95  ILE   A CA  1 
ATOM   768  C C   . ILE   A 1 93  ? 15.463  -12.772 -52.735 1.00 17.64 ? 95  ILE   A C   1 
ATOM   769  O O   . ILE   A 1 93  ? 15.383  -13.987 -52.491 1.00 18.84 ? 95  ILE   A O   1 
ATOM   770  C CB  . ILE   A 1 93  ? 14.751  -11.404 -50.732 1.00 16.97 ? 95  ILE   A CB  1 
ATOM   771  C CG1 . ILE   A 1 93  ? 15.959  -10.469 -50.668 1.00 18.06 ? 95  ILE   A CG1 1 
ATOM   772  C CG2 . ILE   A 1 93  ? 14.972  -12.618 -49.832 1.00 18.82 ? 95  ILE   A CG2 1 
ATOM   773  C CD1 . ILE   A 1 93  ? 15.680  -9.106  -51.236 1.00 18.90 ? 95  ILE   A CD1 1 
ATOM   774  N N   . THR   A 1 94  ? 16.443  -12.250 -53.481 1.00 18.00 ? 96  THR   A N   1 
ATOM   775  C CA  . THR   A 1 94  ? 17.461  -13.080 -54.116 1.00 17.98 ? 96  THR   A CA  1 
ATOM   776  C C   . THR   A 1 94  ? 18.663  -13.241 -53.188 1.00 21.07 ? 96  THR   A C   1 
ATOM   777  O O   . THR   A 1 94  ? 19.303  -12.252 -52.812 1.00 21.33 ? 96  THR   A O   1 
ATOM   778  C CB  . THR   A 1 94  ? 17.913  -12.464 -55.441 1.00 22.15 ? 96  THR   A CB  1 
ATOM   779  O OG1 . THR   A 1 94  ? 16.804  -12.417 -56.351 1.00 26.67 ? 96  THR   A OG1 1 
ATOM   780  C CG2 . THR   A 1 94  ? 19.041  -13.288 -56.056 1.00 28.14 ? 96  THR   A CG2 1 
ATOM   781  N N   . LEU   A 1 95  ? 18.958  -14.482 -52.818 1.00 20.55 ? 97  LEU   A N   1 
ATOM   782  C CA  . LEU   A 1 95  ? 20.220  -14.810 -52.160 1.00 19.27 ? 97  LEU   A CA  1 
ATOM   783  C C   . LEU   A 1 95  ? 21.333  -14.815 -53.201 1.00 22.12 ? 97  LEU   A C   1 
ATOM   784  O O   . LEU   A 1 95  ? 21.342  -15.661 -54.103 1.00 28.25 ? 97  LEU   A O   1 
ATOM   785  C CB  . LEU   A 1 95  ? 20.119  -16.172 -51.477 1.00 20.01 ? 97  LEU   A CB  1 
ATOM   786  C CG  . LEU   A 1 95  ? 21.388  -16.641 -50.761 1.00 19.45 ? 97  LEU   A CG  1 
ATOM   787  C CD1 . LEU   A 1 95  ? 21.683  -15.759 -49.555 1.00 22.20 ? 97  LEU   A CD1 1 
ATOM   788  C CD2 . LEU   A 1 95  ? 21.224  -18.089 -50.331 1.00 23.90 ? 97  LEU   A CD2 1 
ATOM   789  N N   . ALA   A 1 96  ? 22.283  -13.892 -53.069 1.00 21.46 ? 98  ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 96  ? 23.370  -13.789 -54.040 1.00 26.46 ? 98  ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 96  ? 24.597  -14.613 -53.669 1.00 28.77 ? 98  ALA   A C   1 
ATOM   792  O O   . ALA   A 1 96  ? 25.325  -15.060 -54.566 1.00 27.33 ? 98  ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 96  ? 23.783  -12.326 -54.213 1.00 25.82 ? 98  ALA   A CB  1 
ATOM   794  N N   . ASP   A 1 97  ? 24.844  -14.843 -52.381 1.00 23.27 ? 99  ASP   A N   1 
ATOM   795  C CA  . ASP   A 1 97  ? 26.078  -15.498 -51.956 1.00 23.43 ? 99  ASP   A CA  1 
ATOM   796  C C   . ASP   A 1 97  ? 25.937  -15.916 -50.498 1.00 25.25 ? 99  ASP   A C   1 
ATOM   797  O O   . ASP   A 1 97  ? 25.036  -15.469 -49.781 1.00 22.63 ? 99  ASP   A O   1 
ATOM   798  C CB  . ASP   A 1 97  ? 27.277  -14.567 -52.142 1.00 24.35 ? 99  ASP   A CB  1 
ATOM   799  C CG  . ASP   A 1 97  ? 28.565  -15.307 -52.466 1.00 28.03 ? 99  ASP   A CG  1 
ATOM   800  O OD1 . ASP   A 1 97  ? 28.608  -16.551 -52.350 1.00 28.10 ? 99  ASP   A OD1 1 
ATOM   801  O OD2 . ASP   A 1 97  ? 29.547  -14.623 -52.837 1.00 32.30 ? 99  ASP   A OD2 1 
ATOM   802  N N   . ILE   A 1 98  ? 26.854  -16.780 -50.072 1.00 21.26 ? 100 ILE   A N   1 
ATOM   803  C CA  . ILE   A 1 98  ? 26.965  -17.234 -48.692 1.00 22.33 ? 100 ILE   A CA  1 
ATOM   804  C C   . ILE   A 1 98  ? 28.450  -17.267 -48.382 1.00 21.54 ? 100 ILE   A C   1 
ATOM   805  O O   . ILE   A 1 98  ? 29.220  -17.876 -49.131 1.00 26.29 ? 100 ILE   A O   1 
ATOM   806  C CB  . ILE   A 1 98  ? 26.365  -18.638 -48.474 1.00 26.31 ? 100 ILE   A CB  1 
ATOM   807  C CG1 . ILE   A 1 98  ? 24.972  -18.764 -49.099 1.00 29.26 ? 100 ILE   A CG1 1 
ATOM   808  C CG2 . ILE   A 1 98  ? 26.339  -18.976 -46.986 1.00 30.31 ? 100 ILE   A CG2 1 
ATOM   809  C CD1 . ILE   A 1 98  ? 24.557  -20.213 -49.328 1.00 30.53 ? 100 ILE   A CD1 1 
ATOM   810  N N   . VAL   A 1 99  ? 28.863  -16.596 -47.304 1.00 22.80 ? 101 VAL   A N   1 
ATOM   811  C CA  . VAL   A 1 99  ? 30.275  -16.537 -46.943 1.00 20.81 ? 101 VAL   A CA  1 
ATOM   812  C C   . VAL   A 1 99  ? 30.422  -16.815 -45.452 1.00 25.02 ? 101 VAL   A C   1 
ATOM   813  O O   . VAL   A 1 99  ? 29.467  -16.719 -44.681 1.00 26.64 ? 101 VAL   A O   1 
ATOM   814  C CB  . VAL   A 1 99  ? 30.924  -15.178 -47.304 1.00 22.18 ? 101 VAL   A CB  1 
ATOM   815  C CG1 . VAL   A 1 99  ? 30.757  -14.864 -48.796 1.00 22.79 ? 101 VAL   A CG1 1 
ATOM   816  C CG2 . VAL   A 1 99  ? 30.363  -14.075 -46.447 1.00 26.06 ? 101 VAL   A CG2 1 
ATOM   817  N N   . LYS   A 1 100 ? 31.647  -17.169 -45.053 1.00 23.78 ? 102 LYS   A N   1 
ATOM   818  C CA  . LYS   A 1 100 ? 31.994  -17.339 -43.644 1.00 27.00 ? 102 LYS   A CA  1 
ATOM   819  C C   . LYS   A 1 100 ? 32.554  -16.031 -43.101 1.00 27.14 ? 102 LYS   A C   1 
ATOM   820  O O   . LYS   A 1 100 ? 33.617  -15.572 -43.544 1.00 29.53 ? 102 LYS   A O   1 
ATOM   821  C CB  . LYS   A 1 100 ? 33.028  -18.450 -43.448 1.00 30.11 ? 102 LYS   A CB  1 
ATOM   822  C CG  . LYS   A 1 100 ? 32.627  -19.814 -43.986 1.00 43.24 ? 102 LYS   A CG  1 
ATOM   823  C CD  . LYS   A 1 100 ? 33.652  -20.863 -43.573 1.00 55.39 ? 102 LYS   A CD  1 
ATOM   824  C CE  . LYS   A 1 100 ? 33.751  -21.976 -44.599 1.00 62.72 ? 102 LYS   A CE  1 
ATOM   825  N NZ  . LYS   A 1 100 ? 35.164  -22.422 -44.785 1.00 70.80 ? 102 LYS   A NZ  1 
ATOM   826  N N   . ASP   A 1 101 ? 31.879  -15.459 -42.112 1.00 26.32 ? 103 ASP   A N   1 
ATOM   827  C CA  . ASP   A 1 101 ? 32.419  -14.256 -41.502 1.00 27.06 ? 103 ASP   A CA  1 
ATOM   828  C C   . ASP   A 1 101 ? 33.550  -14.618 -40.543 1.00 27.65 ? 103 ASP   A C   1 
ATOM   829  O O   . ASP   A 1 101 ? 33.363  -15.453 -39.651 1.00 29.47 ? 103 ASP   A O   1 
ATOM   830  C CB  . ASP   A 1 101 ? 31.347  -13.469 -40.759 1.00 26.11 ? 103 ASP   A CB  1 
ATOM   831  C CG  . ASP   A 1 101 ? 31.861  -12.133 -40.269 1.00 28.92 ? 103 ASP   A CG  1 
ATOM   832  O OD1 . ASP   A 1 101 ? 31.855  -11.168 -41.063 1.00 33.73 ? 103 ASP   A OD1 1 
ATOM   833  O OD2 . ASP   A 1 101 ? 32.302  -12.047 -39.103 1.00 31.77 ? 103 ASP   A OD2 1 
ATOM   834  N N   . PRO   A 1 102 ? 34.723  -14.004 -40.684 1.00 30.48 ? 104 PRO   A N   1 
ATOM   835  C CA  . PRO   A 1 102 ? 35.855  -14.384 -39.819 1.00 30.03 ? 104 PRO   A CA  1 
ATOM   836  C C   . PRO   A 1 102 ? 35.737  -13.883 -38.391 1.00 30.35 ? 104 PRO   A C   1 
ATOM   837  O O   . PRO   A 1 102 ? 36.423  -14.418 -37.504 1.00 29.97 ? 104 PRO   A O   1 
ATOM   838  C CB  . PRO   A 1 102 ? 37.059  -13.747 -40.526 1.00 33.38 ? 104 PRO   A CB  1 
ATOM   839  C CG  . PRO   A 1 102 ? 36.480  -12.543 -41.208 1.00 29.66 ? 104 PRO   A CG  1 
ATOM   840  C CD  . PRO   A 1 102 ? 35.067  -12.932 -41.637 1.00 26.41 ? 104 PRO   A CD  1 
ATOM   841  N N   . VAL   A 1 103 ? 34.929  -12.852 -38.145 1.00 25.83 ? 105 VAL   A N   1 
ATOM   842  C CA  . VAL   A 1 103 ? 34.801  -12.304 -36.799 1.00 27.92 ? 105 VAL   A CA  1 
ATOM   843  C C   . VAL   A 1 103 ? 33.748  -13.064 -36.012 1.00 29.45 ? 105 VAL   A C   1 
ATOM   844  O O   . VAL   A 1 103 ? 33.981  -13.483 -34.870 1.00 31.24 ? 105 VAL   A O   1 
ATOM   845  C CB  . VAL   A 1 103 ? 34.470  -10.800 -36.857 1.00 27.37 ? 105 VAL   A CB  1 
ATOM   846  C CG1 . VAL   A 1 103 ? 34.165  -10.264 -35.444 1.00 27.73 ? 105 VAL   A CG1 1 
ATOM   847  C CG2 . VAL   A 1 103 ? 35.620  -10.022 -37.485 1.00 32.01 ? 105 VAL   A CG2 1 
ATOM   848  N N   . SER   A 1 104 ? 32.573  -13.240 -36.610 1.00 28.82 ? 106 SER   A N   1 
ATOM   849  C CA  . SER   A 1 104 ? 31.478  -13.919 -35.935 1.00 27.53 ? 106 SER   A CA  1 
ATOM   850  C C   . SER   A 1 104 ? 31.689  -15.415 -35.868 1.00 33.00 ? 106 SER   A C   1 
ATOM   851  O O   . SER   A 1 104 ? 31.101  -16.066 -34.996 1.00 36.01 ? 106 SER   A O   1 
ATOM   852  C CB  . SER   A 1 104 ? 30.152  -13.647 -36.647 1.00 27.18 ? 106 SER   A CB  1 
ATOM   853  O OG  . SER   A 1 104 ? 30.130  -14.293 -37.905 1.00 29.25 ? 106 SER   A OG  1 
ATOM   854  N N   . ARG   A 1 105 ? 32.505  -15.967 -36.772 1.00 27.35 ? 107 ARG   A N   1 
ATOM   855  C CA  . ARG   A 1 105 ? 32.659  -17.414 -36.917 1.00 29.39 ? 107 ARG   A CA  1 
ATOM   856  C C   . ARG   A 1 105 ? 31.328  -18.073 -37.276 1.00 35.61 ? 107 ARG   A C   1 
ATOM   857  O O   . ARG   A 1 105 ? 31.049  -19.205 -36.871 1.00 39.46 ? 107 ARG   A O   1 
ATOM   858  C CB  . ARG   A 1 105 ? 33.258  -18.041 -35.647 1.00 36.26 ? 107 ARG   A CB  1 
ATOM   859  C CG  . ARG   A 1 105 ? 34.469  -17.270 -35.099 1.00 39.52 ? 107 ARG   A CG  1 
ATOM   860  C CD  . ARG   A 1 105 ? 34.940  -17.787 -33.730 1.00 40.85 ? 107 ARG   A CD  1 
ATOM   861  N NE  . ARG   A 1 105 ? 35.277  -19.207 -33.765 1.00 36.62 ? 107 ARG   A NE  1 
ATOM   862  C CZ  . ARG   A 1 105 ? 36.390  -19.690 -34.301 1.00 37.53 ? 107 ARG   A CZ  1 
ATOM   863  N NH1 . ARG   A 1 105 ? 37.268  -18.864 -34.852 1.00 42.04 ? 107 ARG   A NH1 1 
ATOM   864  N NH2 . ARG   A 1 105 ? 36.624  -20.994 -34.292 1.00 38.58 ? 107 ARG   A NH2 1 
ATOM   865  N N   . THR   A 1 106 ? 30.487  -17.362 -38.041 1.00 30.61 ? 108 THR   A N   1 
ATOM   866  C CA  . THR   A 1 106 ? 29.172  -17.854 -38.450 1.00 28.76 ? 108 THR   A CA  1 
ATOM   867  C C   . THR   A 1 106 ? 28.950  -17.564 -39.932 1.00 28.59 ? 108 THR   A C   1 
ATOM   868  O O   . THR   A 1 106 ? 29.692  -16.765 -40.517 1.00 26.95 ? 108 THR   A O   1 
ATOM   869  C CB  . THR   A 1 106 ? 28.052  -17.200 -37.627 1.00 28.39 ? 108 THR   A CB  1 
ATOM   870  O OG1 . THR   A 1 106 ? 28.059  -15.783 -37.844 1.00 29.88 ? 108 THR   A OG1 1 
ATOM   871  C CG2 . THR   A 1 106 ? 28.203  -17.497 -36.133 1.00 34.90 ? 108 THR   A CG2 1 
ATOM   872  N N   . PRO   A 1 107 ? 27.939  -18.160 -40.565 1.00 28.60 ? 109 PRO   A N   1 
ATOM   873  C CA  . PRO   A 1 107 ? 27.645  -17.816 -41.960 1.00 27.63 ? 109 PRO   A CA  1 
ATOM   874  C C   . PRO   A 1 107 ? 27.070  -16.416 -42.087 1.00 29.76 ? 109 PRO   A C   1 
ATOM   875  O O   . PRO   A 1 107 ? 26.377  -15.914 -41.199 1.00 27.57 ? 109 PRO   A O   1 
ATOM   876  C CB  . PRO   A 1 107 ? 26.606  -18.866 -42.377 1.00 27.57 ? 109 PRO   A CB  1 
ATOM   877  C CG  . PRO   A 1 107 ? 26.768  -19.975 -41.376 1.00 29.45 ? 109 PRO   A CG  1 
ATOM   878  C CD  . PRO   A 1 107 ? 27.106  -19.285 -40.103 1.00 31.08 ? 109 PRO   A CD  1 
ATOM   879  N N   . ALA   A 1 108 ? 27.352  -15.794 -43.228 1.00 23.59 ? 110 ALA   A N   1 
ATOM   880  C CA  . ALA   A 1 108 ? 26.794  -14.501 -43.597 1.00 23.51 ? 110 ALA   A CA  1 
ATOM   881  C C   . ALA   A 1 108 ? 26.094  -14.660 -44.936 1.00 23.37 ? 110 ALA   A C   1 
ATOM   882  O O   . ALA   A 1 108 ? 26.727  -15.022 -45.937 1.00 26.02 ? 110 ALA   A O   1 
ATOM   883  C CB  . ALA   A 1 108 ? 27.874  -13.422 -43.677 1.00 27.97 ? 110 ALA   A CB  1 
ATOM   884  N N   . LEU   A 1 109 ? 24.793  -14.401 -44.956 1.00 19.69 ? 111 LEU   A N   1 
ATOM   885  C CA  . LEU   A 1 109 ? 24.018  -14.482 -46.184 1.00 19.01 ? 111 LEU   A CA  1 
ATOM   886  C C   . LEU   A 1 109 ? 24.048  -13.133 -46.889 1.00 22.99 ? 111 LEU   A C   1 
ATOM   887  O O   . LEU   A 1 109 ? 23.819  -12.094 -46.261 1.00 22.93 ? 111 LEU   A O   1 
ATOM   888  C CB  . LEU   A 1 109 ? 22.576  -14.885 -45.879 1.00 19.76 ? 111 LEU   A CB  1 
ATOM   889  C CG  . LEU   A 1 109 ? 22.394  -16.228 -45.167 1.00 24.73 ? 111 LEU   A CG  1 
ATOM   890  C CD1 . LEU   A 1 109 ? 20.910  -16.521 -44.948 1.00 24.46 ? 111 LEU   A CD1 1 
ATOM   891  C CD2 . LEU   A 1 109 ? 23.046  -17.342 -45.949 1.00 39.34 ? 111 LEU   A CD2 1 
ATOM   892  N N   . VAL   A 1 110 ? 24.296  -13.151 -48.196 1.00 19.61 ? 112 VAL   A N   1 
ATOM   893  C CA  . VAL   A 1 110 ? 24.390  -11.940 -49.005 1.00 19.23 ? 112 VAL   A CA  1 
ATOM   894  C C   . VAL   A 1 110 ? 23.168  -11.885 -49.920 1.00 19.76 ? 112 VAL   A C   1 
ATOM   895  O O   . VAL   A 1 110 ? 22.930  -12.813 -50.702 1.00 21.32 ? 112 VAL   A O   1 
ATOM   896  C CB  . VAL   A 1 110 ? 25.696  -11.922 -49.814 1.00 21.86 ? 112 VAL   A CB  1 
ATOM   897  C CG1 . VAL   A 1 110 ? 25.808  -10.640 -50.656 1.00 23.74 ? 112 VAL   A CG1 1 
ATOM   898  C CG2 . VAL   A 1 110 ? 26.900  -12.084 -48.880 1.00 20.91 ? 112 VAL   A CG2 1 
ATOM   899  N N   . PHE   A 1 111 ? 22.407  -10.795 -49.830 1.00 18.78 ? 113 PHE   A N   1 
ATOM   900  C CA  . PHE   A 1 111 ? 21.162  -10.610 -50.568 1.00 20.80 ? 113 PHE   A CA  1 
ATOM   901  C C   . PHE   A 1 111 ? 21.272  -9.439  -51.533 1.00 21.43 ? 113 PHE   A C   1 
ATOM   902  O O   . PHE   A 1 111 ? 22.035  -8.493  -51.303 1.00 22.83 ? 113 PHE   A O   1 
ATOM   903  C CB  . PHE   A 1 111 ? 19.985  -10.313 -49.627 1.00 21.46 ? 113 PHE   A CB  1 
ATOM   904  C CG  . PHE   A 1 111 ? 19.680  -11.414 -48.667 1.00 20.50 ? 113 PHE   A CG  1 
ATOM   905  C CD1 . PHE   A 1 111 ? 18.872  -12.466 -49.048 1.00 17.90 ? 113 PHE   A CD1 1 
ATOM   906  C CD2 . PHE   A 1 111 ? 20.187  -11.390 -47.375 1.00 23.57 ? 113 PHE   A CD2 1 
ATOM   907  C CE1 . PHE   A 1 111 ? 18.566  -13.478 -48.166 1.00 22.28 ? 113 PHE   A CE1 1 
ATOM   908  C CE2 . PHE   A 1 111 ? 19.898  -12.405 -46.482 1.00 24.25 ? 113 PHE   A CE2 1 
ATOM   909  C CZ  . PHE   A 1 111 ? 19.074  -13.456 -46.882 1.00 21.83 ? 113 PHE   A CZ  1 
ATOM   910  N N   . GLU   A 1 112 ? 20.459  -9.486  -52.593 1.00 20.43 ? 114 GLU   A N   1 
ATOM   911  C CA  . GLU   A 1 112 ? 20.253  -8.288  -53.393 1.00 22.79 ? 114 GLU   A CA  1 
ATOM   912  C C   . GLU   A 1 112 ? 19.753  -7.166  -52.491 1.00 24.57 ? 114 GLU   A C   1 
ATOM   913  O O   . GLU   A 1 112 ? 19.128  -7.407  -51.449 1.00 25.68 ? 114 GLU   A O   1 
ATOM   914  C CB  . GLU   A 1 112 ? 19.242  -8.557  -54.514 1.00 24.62 ? 114 GLU   A CB  1 
ATOM   915  C CG  . GLU   A 1 112 ? 17.834  -8.727  -53.979 1.00 24.75 ? 114 GLU   A CG  1 
ATOM   916  C CD  . GLU   A 1 112 ? 16.759  -8.897  -55.057 1.00 30.71 ? 114 GLU   A CD  1 
ATOM   917  O OE1 . GLU   A 1 112 ? 16.746  -8.134  -56.044 1.00 39.50 ? 114 GLU   A OE1 1 
ATOM   918  O OE2 . GLU   A 1 112 ? 15.919  -9.802  -54.903 1.00 24.76 ? 114 GLU   A OE2 1 
ATOM   919  N N   . HIS   A 1 113 ? 20.034  -5.927  -52.888 1.00 23.02 ? 115 HIS   A N   1 
ATOM   920  C CA  . HIS   A 1 113 ? 19.664  -4.746  -52.116 1.00 25.67 ? 115 HIS   A CA  1 
ATOM   921  C C   . HIS   A 1 113 ? 18.354  -4.157  -52.634 1.00 25.81 ? 115 HIS   A C   1 
ATOM   922  O O   . HIS   A 1 113 ? 18.179  -4.000  -53.844 1.00 27.53 ? 115 HIS   A O   1 
ATOM   923  C CB  . HIS   A 1 113 ? 20.779  -3.697  -52.194 1.00 26.60 ? 115 HIS   A CB  1 
ATOM   924  C CG  . HIS   A 1 113 ? 20.440  -2.397  -51.535 1.00 31.38 ? 115 HIS   A CG  1 
ATOM   925  N ND1 . HIS   A 1 113 ? 19.950  -1.313  -52.234 1.00 31.99 ? 115 HIS   A ND1 1 
ATOM   926  C CD2 . HIS   A 1 113 ? 20.514  -2.007  -50.241 1.00 36.88 ? 115 HIS   A CD2 1 
ATOM   927  C CE1 . HIS   A 1 113 ? 19.743  -0.312  -51.398 1.00 32.99 ? 115 HIS   A CE1 1 
ATOM   928  N NE2 . HIS   A 1 113 ? 20.073  -0.708  -50.182 1.00 35.91 ? 115 HIS   A NE2 1 
ATOM   929  N N   . VAL   A 1 114 ? 17.447  -3.822  -51.719 1.00 25.11 ? 116 VAL   A N   1 
ATOM   930  C CA  . VAL   A 1 114 ? 16.222  -3.093  -52.040 1.00 26.24 ? 116 VAL   A CA  1 
ATOM   931  C C   . VAL   A 1 114 ? 16.302  -1.719  -51.387 1.00 24.21 ? 116 VAL   A C   1 
ATOM   932  O O   . VAL   A 1 114 ? 16.584  -1.610  -50.188 1.00 28.50 ? 116 VAL   A O   1 
ATOM   933  C CB  . VAL   A 1 114 ? 14.965  -3.850  -51.567 1.00 23.46 ? 116 VAL   A CB  1 
ATOM   934  C CG1 . VAL   A 1 114 ? 13.704  -3.034  -51.889 1.00 27.11 ? 116 VAL   A CG1 1 
ATOM   935  C CG2 . VAL   A 1 114 ? 14.899  -5.228  -52.209 1.00 24.25 ? 116 VAL   A CG2 1 
ATOM   936  N N   . ASN   A 1 115 ? 16.065  -0.670  -52.173 1.00 28.82 ? 117 ASN   A N   1 
ATOM   937  C CA  . ASN   A 1 115 ? 16.042  0.700   -51.658 1.00 33.19 ? 117 ASN   A CA  1 
ATOM   938  C C   . ASN   A 1 115 ? 14.678  0.949   -51.019 1.00 38.18 ? 117 ASN   A C   1 
ATOM   939  O O   . ASN   A 1 115 ? 13.749  1.453   -51.651 1.00 42.74 ? 117 ASN   A O   1 
ATOM   940  C CB  . ASN   A 1 115 ? 16.334  1.695   -52.774 1.00 41.22 ? 117 ASN   A CB  1 
ATOM   941  C CG  . ASN   A 1 115 ? 16.397  3.122   -52.276 1.00 51.29 ? 117 ASN   A CG  1 
ATOM   942  O OD1 . ASN   A 1 115 ? 16.662  3.369   -51.100 1.00 56.72 ? 117 ASN   A OD1 1 
ATOM   943  N ND2 . ASN   A 1 115 ? 16.148  4.072   -53.170 1.00 55.49 ? 117 ASN   A ND2 1 
ATOM   944  N N   . ASN   A 1 116 ? 14.570  0.614   -49.738 1.00 41.09 ? 118 ASN   A N   1 
ATOM   945  C CA  . ASN   A 1 116 ? 13.292  0.481   -49.051 1.00 48.07 ? 118 ASN   A CA  1 
ATOM   946  C C   . ASN   A 1 116 ? 12.881  1.771   -48.339 1.00 49.83 ? 118 ASN   A C   1 
ATOM   947  O O   . ASN   A 1 116 ? 13.722  2.585   -47.955 1.00 45.91 ? 118 ASN   A O   1 
ATOM   948  C CB  . ASN   A 1 116 ? 13.393  -0.676  -48.049 1.00 51.98 ? 118 ASN   A CB  1 
ATOM   949  C CG  . ASN   A 1 116 ? 12.226  -0.738  -47.088 1.00 58.98 ? 118 ASN   A CG  1 
ATOM   950  O OD1 . ASN   A 1 116 ? 12.392  -0.530  -45.886 1.00 61.35 ? 118 ASN   A OD1 1 
ATOM   951  N ND2 . ASN   A 1 116 ? 11.038  -1.029  -47.608 1.00 53.77 ? 118 ASN   A ND2 1 
ATOM   952  N N   . THR   A 1 117 ? 11.566  1.960   -48.187 1.00 53.66 ? 119 THR   A N   1 
ATOM   953  C CA  . THR   A 1 117 ? 11.007  2.903   -47.223 1.00 58.67 ? 119 THR   A CA  1 
ATOM   954  C C   . THR   A 1 117 ? 10.397  2.129   -46.061 1.00 57.51 ? 119 THR   A C   1 
ATOM   955  O O   . THR   A 1 117 ? 9.702   1.131   -46.273 1.00 57.00 ? 119 THR   A O   1 
ATOM   956  C CB  . THR   A 1 117 ? 9.931   3.803   -47.845 1.00 65.91 ? 119 THR   A CB  1 
ATOM   957  O OG1 . THR   A 1 117 ? 9.165   3.059   -48.801 1.00 70.49 ? 119 THR   A OG1 1 
ATOM   958  C CG2 . THR   A 1 117 ? 10.550  4.998   -48.523 1.00 66.20 ? 119 THR   A CG2 1 
ATOM   959  N N   . ASP   A 1 118 ? 10.625  2.635   -44.845 1.00 55.80 ? 120 ASP   A N   1 
ATOM   960  C CA  . ASP   A 1 118 ? 10.084  2.001   -43.614 1.00 60.38 ? 120 ASP   A CA  1 
ATOM   961  C C   . ASP   A 1 118 ? 8.560   1.935   -43.712 1.00 53.71 ? 120 ASP   A C   1 
ATOM   962  O O   . ASP   A 1 118 ? 7.951   2.926   -44.140 1.00 57.04 ? 120 ASP   A O   1 
ATOM   963  C CB  . ASP   A 1 118 ? 10.602  2.681   -42.351 1.00 68.63 ? 120 ASP   A CB  1 
ATOM   964  C CG  . ASP   A 1 118 ? 11.801  1.942   -41.799 1.00 79.43 ? 120 ASP   A CG  1 
ATOM   965  O OD1 . ASP   A 1 118 ? 12.935  2.387   -42.064 1.00 85.19 ? 120 ASP   A OD1 1 
ATOM   966  O OD2 . ASP   A 1 118 ? 11.587  0.904   -41.144 1.00 84.37 ? 120 ASP   A OD2 1 
ATOM   967  N N   . PHE   A 1 119 ? 7.973   0.818   -43.282 1.00 49.76 ? 121 PHE   A N   1 
ATOM   968  C CA  . PHE   A 1 119 ? 6.536   0.660   -43.468 1.00 52.00 ? 121 PHE   A CA  1 
ATOM   969  C C   . PHE   A 1 119 ? 5.752   1.690   -42.668 1.00 58.54 ? 121 PHE   A C   1 
ATOM   970  O O   . PHE   A 1 119 ? 4.702   2.148   -43.127 1.00 57.63 ? 121 PHE   A O   1 
ATOM   971  C CB  . PHE   A 1 119 ? 6.096   -0.766  -43.108 1.00 47.50 ? 121 PHE   A CB  1 
ATOM   972  C CG  . PHE   A 1 119 ? 5.822   -0.978  -41.643 1.00 50.11 ? 121 PHE   A CG  1 
ATOM   973  C CD1 . PHE   A 1 119 ? 6.837   -1.358  -40.782 1.00 56.51 ? 121 PHE   A CD1 1 
ATOM   974  C CD2 . PHE   A 1 119 ? 4.541   -0.820  -41.131 1.00 50.35 ? 121 PHE   A CD2 1 
ATOM   975  C CE1 . PHE   A 1 119 ? 6.583   -1.561  -39.435 1.00 57.35 ? 121 PHE   A CE1 1 
ATOM   976  C CE2 . PHE   A 1 119 ? 4.284   -1.020  -39.789 1.00 53.64 ? 121 PHE   A CE2 1 
ATOM   977  C CZ  . PHE   A 1 119 ? 5.305   -1.392  -38.940 1.00 55.54 ? 121 PHE   A CZ  1 
ATOM   978  N N   . LYS   A 1 120 ? 6.247   2.077   -41.488 1.00 65.91 ? 122 LYS   A N   1 
ATOM   979  C CA  . LYS   A 1 120 ? 5.543   3.078   -40.693 1.00 74.46 ? 122 LYS   A CA  1 
ATOM   980  C C   . LYS   A 1 120 ? 5.350   4.370   -41.481 1.00 74.89 ? 122 LYS   A C   1 
ATOM   981  O O   . LYS   A 1 120 ? 4.298   5.013   -41.388 1.00 80.52 ? 122 LYS   A O   1 
ATOM   982  C CB  . LYS   A 1 120 ? 6.297   3.345   -39.389 1.00 80.59 ? 122 LYS   A CB  1 
ATOM   983  C CG  . LYS   A 1 120 ? 5.685   4.453   -38.544 1.00 89.47 ? 122 LYS   A CG  1 
ATOM   984  C CD  . LYS   A 1 120 ? 6.693   5.042   -37.563 1.00 93.19 ? 122 LYS   A CD  1 
ATOM   985  C CE  . LYS   A 1 120 ? 6.746   4.255   -36.262 1.00 95.98 ? 122 LYS   A CE  1 
ATOM   986  N NZ  . LYS   A 1 120 ? 5.483   4.396   -35.482 1.00 96.67 ? 122 LYS   A NZ  1 
ATOM   987  N N   . GLN   A 1 121 ? 6.344   4.747   -42.287 1.00 66.79 ? 123 GLN   A N   1 
ATOM   988  C CA  . GLN   A 1 121 ? 6.229   5.945   -43.114 1.00 64.37 ? 123 GLN   A CA  1 
ATOM   989  C C   . GLN   A 1 121 ? 5.527   5.654   -44.435 1.00 57.48 ? 123 GLN   A C   1 
ATOM   990  O O   . GLN   A 1 121 ? 4.703   6.454   -44.895 1.00 55.12 ? 123 GLN   A O   1 
ATOM   991  C CB  . GLN   A 1 121 ? 7.617   6.535   -43.367 1.00 73.18 ? 123 GLN   A CB  1 
ATOM   992  C CG  . GLN   A 1 121 ? 8.224   7.276   -42.176 1.00 79.78 ? 123 GLN   A CG  1 
ATOM   993  C CD  . GLN   A 1 121 ? 8.535   6.375   -40.987 1.00 85.63 ? 123 GLN   A CD  1 
ATOM   994  O OE1 . GLN   A 1 121 ? 8.409   5.151   -41.062 1.00 89.00 ? 123 GLN   A OE1 1 
ATOM   995  N NE2 . GLN   A 1 121 ? 8.947   6.985   -39.881 1.00 85.60 ? 123 GLN   A NE2 1 
ATOM   996  N N   . LEU   A 1 122 ? 5.839   4.517   -45.060 1.00 45.38 ? 124 LEU   A N   1 
ATOM   997  C CA  . LEU   A 1 122 ? 5.190   4.165   -46.315 1.00 42.88 ? 124 LEU   A CA  1 
ATOM   998  C C   . LEU   A 1 122 ? 3.690   3.978   -46.127 1.00 37.38 ? 124 LEU   A C   1 
ATOM   999  O O   . LEU   A 1 122 ? 2.893   4.383   -46.981 1.00 41.87 ? 124 LEU   A O   1 
ATOM   1000 C CB  . LEU   A 1 122 ? 5.823   2.899   -46.891 1.00 47.00 ? 124 LEU   A CB  1 
ATOM   1001 C CG  . LEU   A 1 122 ? 5.518   2.613   -48.356 1.00 51.53 ? 124 LEU   A CG  1 
ATOM   1002 C CD1 . LEU   A 1 122 ? 5.960   3.784   -49.220 1.00 50.38 ? 124 LEU   A CD1 1 
ATOM   1003 C CD2 . LEU   A 1 122 ? 6.202   1.331   -48.793 1.00 52.29 ? 124 LEU   A CD2 1 
ATOM   1004 N N   . TYR   A 1 123 ? 3.279   3.387   -45.003 1.00 28.85 ? 125 TYR   A N   1 
ATOM   1005 C CA  . TYR   A 1 123 ? 1.858   3.090   -44.855 1.00 30.63 ? 125 TYR   A CA  1 
ATOM   1006 C C   . TYR   A 1 123 ? 1.018   4.351   -44.648 1.00 36.29 ? 125 TYR   A C   1 
ATOM   1007 O O   . TYR   A 1 123 ? -0.160  4.359   -45.025 1.00 35.81 ? 125 TYR   A O   1 
ATOM   1008 C CB  . TYR   A 1 123 ? 1.642   2.072   -43.729 1.00 37.80 ? 125 TYR   A CB  1 
ATOM   1009 C CG  . TYR   A 1 123 ? 2.082   0.649   -44.090 1.00 47.65 ? 125 TYR   A CG  1 
ATOM   1010 C CD1 . TYR   A 1 123 ? 2.945   0.409   -45.158 1.00 53.43 ? 125 TYR   A CD1 1 
ATOM   1011 C CD2 . TYR   A 1 123 ? 1.624   -0.451  -43.369 1.00 53.49 ? 125 TYR   A CD2 1 
ATOM   1012 C CE1 . TYR   A 1 123 ? 3.347   -0.876  -45.492 1.00 57.53 ? 125 TYR   A CE1 1 
ATOM   1013 C CE2 . TYR   A 1 123 ? 2.021   -1.743  -43.698 1.00 57.25 ? 125 TYR   A CE2 1 
ATOM   1014 C CZ  . TYR   A 1 123 ? 2.882   -1.948  -44.762 1.00 60.76 ? 125 TYR   A CZ  1 
ATOM   1015 O OH  . TYR   A 1 123 ? 3.280   -3.226  -45.097 1.00 62.89 ? 125 TYR   A OH  1 
ATOM   1016 N N   . GLN   A 1 124 ? 1.598   5.430   -44.115 1.00 30.37 ? 126 GLN   A N   1 
ATOM   1017 C CA  . GLN   A 1 124 ? 0.872   6.697   -44.028 1.00 32.10 ? 126 GLN   A CA  1 
ATOM   1018 C C   . GLN   A 1 124 ? 0.630   7.335   -45.392 1.00 32.84 ? 126 GLN   A C   1 
ATOM   1019 O O   . GLN   A 1 124 ? 0.003   8.398   -45.468 1.00 34.07 ? 126 GLN   A O   1 
ATOM   1020 C CB  . GLN   A 1 124 ? 1.634   7.685   -43.138 1.00 38.93 ? 126 GLN   A CB  1 
ATOM   1021 C CG  . GLN   A 1 124 ? 1.928   7.188   -41.729 1.00 50.95 ? 126 GLN   A CG  1 
ATOM   1022 C CD  . GLN   A 1 124 ? 0.904   7.658   -40.712 1.00 59.39 ? 126 GLN   A CD  1 
ATOM   1023 O OE1 . GLN   A 1 124 ? -0.030  8.388   -41.046 1.00 61.97 ? 126 GLN   A OE1 1 
ATOM   1024 N NE2 . GLN   A 1 124 ? 1.076   7.242   -39.462 1.00 62.40 ? 126 GLN   A NE2 1 
ATOM   1025 N N   . THR   A 1 125 ? 1.082   6.699   -46.466 1.00 37.40 ? 127 THR   A N   1 
ATOM   1026 C CA  . THR   A 1 125 ? 1.197   7.344   -47.764 1.00 43.89 ? 127 THR   A CA  1 
ATOM   1027 C C   . THR   A 1 125 ? 0.464   6.588   -48.868 1.00 47.21 ? 127 THR   A C   1 
ATOM   1028 O O   . THR   A 1 125 ? -0.088  7.201   -49.790 1.00 54.28 ? 127 THR   A O   1 
ATOM   1029 C CB  . THR   A 1 125 ? 2.679   7.481   -48.102 1.00 54.86 ? 127 THR   A CB  1 
ATOM   1030 O OG1 . THR   A 1 125 ? 3.197   8.677   -47.507 1.00 58.35 ? 127 THR   A OG1 1 
ATOM   1031 C CG2 . THR   A 1 125 ? 2.883   7.502   -49.580 1.00 59.99 ? 127 THR   A CG2 1 
ATOM   1032 N N   . LEU   A 1 126 ? 0.444   5.262   -48.781 1.00 38.26 ? 128 LEU   A N   1 
ATOM   1033 C CA  . LEU   A 1 126 ? -0.132  4.452   -49.847 1.00 36.32 ? 128 LEU   A CA  1 
ATOM   1034 C C   . LEU   A 1 126 ? -1.606  4.784   -50.059 1.00 38.68 ? 128 LEU   A C   1 
ATOM   1035 O O   . LEU   A 1 126 ? -2.361  4.984   -49.105 1.00 36.76 ? 128 LEU   A O   1 
ATOM   1036 C CB  . LEU   A 1 126 ? 0.032   2.968   -49.524 1.00 38.03 ? 128 LEU   A CB  1 
ATOM   1037 C CG  . LEU   A 1 126 ? 1.468   2.493   -49.302 1.00 44.53 ? 128 LEU   A CG  1 
ATOM   1038 C CD1 . LEU   A 1 126 ? 1.500   0.999   -49.055 1.00 40.69 ? 128 LEU   A CD1 1 
ATOM   1039 C CD2 . LEU   A 1 126 ? 2.351   2.861   -50.485 1.00 48.52 ? 128 LEU   A CD2 1 
ATOM   1040 N N   . THR   A 1 127 ? -2.002  4.860   -51.329 1.00 31.98 ? 129 THR   A N   1 
ATOM   1041 C CA  . THR   A 1 127 ? -3.386  5.046   -51.731 1.00 27.46 ? 129 THR   A CA  1 
ATOM   1042 C C   . THR   A 1 127 ? -4.110  3.702   -51.773 1.00 28.49 ? 129 THR   A C   1 
ATOM   1043 O O   . THR   A 1 127 ? -3.506  2.634   -51.628 1.00 31.16 ? 129 THR   A O   1 
ATOM   1044 C CB  . THR   A 1 127 ? -3.459  5.711   -53.106 1.00 25.63 ? 129 THR   A CB  1 
ATOM   1045 O OG1 . THR   A 1 127 ? -2.934  4.810   -54.084 1.00 26.23 ? 129 THR   A OG1 1 
ATOM   1046 C CG2 . THR   A 1 127 ? -2.649  6.986   -53.129 1.00 27.30 ? 129 THR   A CG2 1 
ATOM   1047 N N   . ASP   A 1 128 ? -5.432  3.763   -51.963 1.00 28.47 ? 130 ASP   A N   1 
ATOM   1048 C CA  . ASP   A 1 128 ? -6.207  2.549   -52.200 1.00 27.71 ? 130 ASP   A CA  1 
ATOM   1049 C C   . ASP   A 1 128 ? -5.597  1.734   -53.336 1.00 27.91 ? 130 ASP   A C   1 
ATOM   1050 O O   . ASP   A 1 128 ? -5.401  0.517   -53.211 1.00 30.28 ? 130 ASP   A O   1 
ATOM   1051 C CB  . ASP   A 1 128 ? -7.667  2.916   -52.497 1.00 29.63 ? 130 ASP   A CB  1 
ATOM   1052 C CG  . ASP   A 1 128 ? -8.525  1.717   -52.880 1.00 32.00 ? 130 ASP   A CG  1 
ATOM   1053 O OD1 . ASP   A 1 128 ? -8.475  0.672   -52.200 1.00 32.02 ? 130 ASP   A OD1 1 
ATOM   1054 O OD2 . ASP   A 1 128 ? -9.292  1.838   -53.854 1.00 39.68 ? 130 ASP   A OD2 1 
ATOM   1055 N N   . TYR   A 1 129 ? -5.237  2.404   -54.438 1.00 27.29 ? 131 TYR   A N   1 
ATOM   1056 C CA  . TYR   A 1 129 ? -4.654  1.685   -55.565 1.00 25.21 ? 131 TYR   A CA  1 
ATOM   1057 C C   . TYR   A 1 129 ? -3.310  1.064   -55.189 1.00 29.44 ? 131 TYR   A C   1 
ATOM   1058 O O   . TYR   A 1 129 ? -3.047  -0.098  -55.526 1.00 28.65 ? 131 TYR   A O   1 
ATOM   1059 C CB  . TYR   A 1 129 ? -4.511  2.607   -56.781 1.00 26.98 ? 131 TYR   A CB  1 
ATOM   1060 C CG  . TYR   A 1 129 ? -4.068  1.848   -58.007 1.00 32.81 ? 131 TYR   A CG  1 
ATOM   1061 C CD1 . TYR   A 1 129 ? -4.988  1.177   -58.810 1.00 31.85 ? 131 TYR   A CD1 1 
ATOM   1062 C CD2 . TYR   A 1 129 ? -2.719  1.770   -58.344 1.00 33.89 ? 131 TYR   A CD2 1 
ATOM   1063 C CE1 . TYR   A 1 129 ? -4.571  0.460   -59.930 1.00 36.62 ? 131 TYR   A CE1 1 
ATOM   1064 C CE2 . TYR   A 1 129 ? -2.298  1.058   -59.452 1.00 36.53 ? 131 TYR   A CE2 1 
ATOM   1065 C CZ  . TYR   A 1 129 ? -3.227  0.408   -60.243 1.00 40.78 ? 131 TYR   A CZ  1 
ATOM   1066 O OH  . TYR   A 1 129 ? -2.792  -0.297  -61.344 1.00 41.54 ? 131 TYR   A OH  1 
ATOM   1067 N N   . ASP   A 1 130 ? -2.452  1.814   -54.483 1.00 26.83 ? 132 ASP   A N   1 
ATOM   1068 C CA  . ASP   A 1 130 ? -1.169  1.257   -54.040 1.00 30.27 ? 132 ASP   A CA  1 
ATOM   1069 C C   . ASP   A 1 130 ? -1.364  -0.016  -53.216 1.00 29.23 ? 132 ASP   A C   1 
ATOM   1070 O O   . ASP   A 1 130 ? -0.640  -1.004  -53.400 1.00 27.47 ? 132 ASP   A O   1 
ATOM   1071 C CB  . ASP   A 1 130 ? -0.386  2.274   -53.201 1.00 28.77 ? 132 ASP   A CB  1 
ATOM   1072 C CG  . ASP   A 1 130 ? 0.082   3.478   -53.985 1.00 37.40 ? 132 ASP   A CG  1 
ATOM   1073 O OD1 . ASP   A 1 130 ? 0.363   3.368   -55.201 1.00 39.48 ? 132 ASP   A OD1 1 
ATOM   1074 O OD2 . ASP   A 1 130 ? 0.188   4.553   -53.353 1.00 32.91 ? 132 ASP   A OD2 1 
ATOM   1075 N N   . ILE   A 1 131 ? -2.313  0.000   -52.275 1.00 25.25 ? 133 ILE   A N   1 
ATOM   1076 C CA  . ILE   A 1 131 ? -2.506  -1.144  -51.383 1.00 25.25 ? 133 ILE   A CA  1 
ATOM   1077 C C   . ILE   A 1 131 ? -2.915  -2.377  -52.178 1.00 28.44 ? 133 ILE   A C   1 
ATOM   1078 O O   . ILE   A 1 131 ? -2.393  -3.478  -51.966 1.00 25.33 ? 133 ILE   A O   1 
ATOM   1079 C CB  . ILE   A 1 131 ? -3.541  -0.806  -50.296 1.00 28.43 ? 133 ILE   A CB  1 
ATOM   1080 C CG1 . ILE   A 1 131 ? -2.982  0.258   -49.346 1.00 26.52 ? 133 ILE   A CG1 1 
ATOM   1081 C CG2 . ILE   A 1 131 ? -3.978  -2.067  -49.536 1.00 25.43 ? 133 ILE   A CG2 1 
ATOM   1082 C CD1 . ILE   A 1 131 ? -4.029  0.851   -48.418 1.00 32.68 ? 133 ILE   A CD1 1 
ATOM   1083 N N   . ARG   A 1 132 ? -3.866  -2.214  -53.100 1.00 22.30 ? 134 ARG   A N   1 
ATOM   1084 C CA  . ARG   A 1 132 ? -4.268  -3.341  -53.931 1.00 24.38 ? 134 ARG   A CA  1 
ATOM   1085 C C   . ARG   A 1 132 ? -3.086  -3.866  -54.725 1.00 22.04 ? 134 ARG   A C   1 
ATOM   1086 O O   . ARG   A 1 132 ? -2.879  -5.082  -54.815 1.00 22.13 ? 134 ARG   A O   1 
ATOM   1087 C CB  . ARG   A 1 132 ? -5.395  -2.922  -54.870 1.00 22.64 ? 134 ARG   A CB  1 
ATOM   1088 C CG  . ARG   A 1 132 ? -6.601  -2.337  -54.145 1.00 22.53 ? 134 ARG   A CG  1 
ATOM   1089 C CD  . ARG   A 1 132 ? -7.811  -2.305  -55.036 1.00 27.47 ? 134 ARG   A CD  1 
ATOM   1090 N NE  . ARG   A 1 132 ? -8.823  -1.361  -54.576 1.00 24.76 ? 134 ARG   A NE  1 
ATOM   1091 C CZ  . ARG   A 1 132 ? -10.118 -1.517  -54.796 1.00 23.89 ? 134 ARG   A CZ  1 
ATOM   1092 N NH1 . ARG   A 1 132 ? -10.551 -2.596  -55.437 1.00 27.89 ? 134 ARG   A NH1 1 
ATOM   1093 N NH2 . ARG   A 1 132 ? -10.978 -0.603  -54.369 1.00 28.90 ? 134 ARG   A NH2 1 
ATOM   1094 N N   . PHE   A 1 133 ? -2.310  -2.955  -55.320 1.00 23.70 ? 135 PHE   A N   1 
ATOM   1095 C CA  . PHE   A 1 133 ? -1.164  -3.346  -56.137 1.00 20.61 ? 135 PHE   A CA  1 
ATOM   1096 C C   . PHE   A 1 133 ? -0.164  -4.151  -55.326 1.00 21.58 ? 135 PHE   A C   1 
ATOM   1097 O O   . PHE   A 1 133 ? 0.262   -5.237  -55.740 1.00 21.71 ? 135 PHE   A O   1 
ATOM   1098 C CB  . PHE   A 1 133 ? -0.498  -2.098  -56.721 1.00 21.13 ? 135 PHE   A CB  1 
ATOM   1099 C CG  . PHE   A 1 133 ? 0.761   -2.383  -57.485 1.00 26.04 ? 135 PHE   A CG  1 
ATOM   1100 C CD1 . PHE   A 1 133 ? 0.712   -2.746  -58.818 1.00 31.23 ? 135 PHE   A CD1 1 
ATOM   1101 C CD2 . PHE   A 1 133 ? 1.997   -2.287  -56.866 1.00 26.29 ? 135 PHE   A CD2 1 
ATOM   1102 C CE1 . PHE   A 1 133 ? 1.880   -3.009  -59.527 1.00 33.12 ? 135 PHE   A CE1 1 
ATOM   1103 C CE2 . PHE   A 1 133 ? 3.163   -2.544  -57.576 1.00 31.25 ? 135 PHE   A CE2 1 
ATOM   1104 C CZ  . PHE   A 1 133 ? 3.097   -2.910  -58.898 1.00 32.17 ? 135 PHE   A CZ  1 
ATOM   1105 N N   . TYR   A 1 134 ? 0.218   -3.637  -54.161 1.00 21.35 ? 136 TYR   A N   1 
ATOM   1106 C CA  . TYR   A 1 134 ? 1.249   -4.318  -53.392 1.00 21.72 ? 136 TYR   A CA  1 
ATOM   1107 C C   . TYR   A 1 134 ? 0.717   -5.597  -52.756 1.00 20.07 ? 136 TYR   A C   1 
ATOM   1108 O O   . TYR   A 1 134 ? 1.455   -6.577  -52.642 1.00 22.02 ? 136 TYR   A O   1 
ATOM   1109 C CB  . TYR   A 1 134 ? 1.845   -3.367  -52.350 1.00 21.99 ? 136 TYR   A CB  1 
ATOM   1110 C CG  . TYR   A 1 134 ? 2.752   -2.306  -52.947 1.00 24.19 ? 136 TYR   A CG  1 
ATOM   1111 C CD1 . TYR   A 1 134 ? 3.845   -2.662  -53.726 1.00 25.00 ? 136 TYR   A CD1 1 
ATOM   1112 C CD2 . TYR   A 1 134 ? 2.538   -0.955  -52.701 1.00 27.57 ? 136 TYR   A CD2 1 
ATOM   1113 C CE1 . TYR   A 1 134 ? 4.694   -1.707  -54.263 1.00 23.67 ? 136 TYR   A CE1 1 
ATOM   1114 C CE2 . TYR   A 1 134 ? 3.376   0.013   -53.234 1.00 27.14 ? 136 TYR   A CE2 1 
ATOM   1115 C CZ  . TYR   A 1 134 ? 4.455   -0.371  -54.015 1.00 25.98 ? 136 TYR   A CZ  1 
ATOM   1116 O OH  . TYR   A 1 134 ? 5.298   0.577   -54.550 1.00 28.27 ? 136 TYR   A OH  1 
ATOM   1117 N N   . MET   A 1 135 ? -0.564  -5.633  -52.369 1.00 20.66 ? 137 MET   A N   1 
ATOM   1118 C CA  . MET   A 1 135 ? -1.137  -6.897  -51.905 1.00 21.73 ? 137 MET   A CA  1 
ATOM   1119 C C   . MET   A 1 135 ? -1.074  -7.964  -52.988 1.00 20.57 ? 137 MET   A C   1 
ATOM   1120 O O   . MET   A 1 135 ? -0.777  -9.130  -52.701 1.00 20.16 ? 137 MET   A O   1 
ATOM   1121 C CB  . MET   A 1 135 ? -2.587  -6.694  -51.458 1.00 21.53 ? 137 MET   A CB  1 
ATOM   1122 C CG  . MET   A 1 135 ? -2.735  -6.064  -50.096 1.00 23.13 ? 137 MET   A CG  1 
ATOM   1123 S SD  . MET   A 1 135 ? -2.398  -7.290  -48.804 1.00 30.44 ? 137 MET   A SD  1 
ATOM   1124 C CE  . MET   A 1 135 ? -3.602  -8.548  -49.246 1.00 42.55 ? 137 MET   A CE  1 
ATOM   1125 N N   . TYR   A 1 136 ? -1.355  -7.582  -54.243 1.00 17.66 ? 138 TYR   A N   1 
ATOM   1126 C CA  . TYR   A 1 136 ? -1.265  -8.525  -55.351 1.00 18.40 ? 138 TYR   A CA  1 
ATOM   1127 C C   . TYR   A 1 136 ? 0.162   -9.022  -55.521 1.00 18.11 ? 138 TYR   A C   1 
ATOM   1128 O O   . TYR   A 1 136 ? 0.391   -10.214 -55.760 1.00 19.86 ? 138 TYR   A O   1 
ATOM   1129 C CB  . TYR   A 1 136 ? -1.767  -7.869  -56.635 1.00 21.50 ? 138 TYR   A CB  1 
ATOM   1130 C CG  . TYR   A 1 136 ? -2.087  -8.841  -57.741 1.00 23.08 ? 138 TYR   A CG  1 
ATOM   1131 C CD1 . TYR   A 1 136 ? -3.254  -9.583  -57.710 1.00 25.14 ? 138 TYR   A CD1 1 
ATOM   1132 C CD2 . TYR   A 1 136 ? -1.235  -9.005  -58.823 1.00 22.70 ? 138 TYR   A CD2 1 
ATOM   1133 C CE1 . TYR   A 1 136 ? -3.566  -10.466 -58.708 1.00 24.88 ? 138 TYR   A CE1 1 
ATOM   1134 C CE2 . TYR   A 1 136 ? -1.546  -9.892  -59.843 1.00 29.61 ? 138 TYR   A CE2 1 
ATOM   1135 C CZ  . TYR   A 1 136 ? -2.719  -10.616 -59.778 1.00 26.87 ? 138 TYR   A CZ  1 
ATOM   1136 O OH  . TYR   A 1 136 ? -3.056  -11.505 -60.776 1.00 32.42 ? 138 TYR   A OH  1 
ATOM   1137 N N   . GLU   A 1 137 ? 1.133   -8.124  -55.379 1.00 18.21 ? 139 GLU   A N   1 
ATOM   1138 C CA  . GLU   A 1 137 ? 2.532   -8.522  -55.498 1.00 20.44 ? 139 GLU   A CA  1 
ATOM   1139 C C   . GLU   A 1 137 ? 2.952   -9.459  -54.367 1.00 20.05 ? 139 GLU   A C   1 
ATOM   1140 O O   . GLU   A 1 137 ? 3.738   -10.384 -54.593 1.00 17.68 ? 139 GLU   A O   1 
ATOM   1141 C CB  . GLU   A 1 137 ? 3.424   -7.281  -55.541 1.00 22.08 ? 139 GLU   A CB  1 
ATOM   1142 C CG  . GLU   A 1 137 ? 3.193   -6.407  -56.780 1.00 23.26 ? 139 GLU   A CG  1 
ATOM   1143 C CD  . GLU   A 1 137 ? 3.487   -7.149  -58.079 1.00 27.58 ? 139 GLU   A CD  1 
ATOM   1144 O OE1 . GLU   A 1 137 ? 4.509   -7.859  -58.138 1.00 29.61 ? 139 GLU   A OE1 1 
ATOM   1145 O OE2 . GLU   A 1 137 ? 2.695   -7.047  -59.040 1.00 30.65 ? 139 GLU   A OE2 1 
ATOM   1146 N N   . ILE   A 1 138 ? 2.444   -9.249  -53.147 1.00 18.26 ? 140 ILE   A N   1 
ATOM   1147 C CA  . ILE   A 1 138 ? 2.736   -10.191 -52.065 1.00 17.15 ? 140 ILE   A CA  1 
ATOM   1148 C C   . ILE   A 1 138 ? 2.125   -11.552 -52.367 1.00 21.73 ? 140 ILE   A C   1 
ATOM   1149 O O   . ILE   A 1 138 ? 2.742   -12.598 -52.131 1.00 18.00 ? 140 ILE   A O   1 
ATOM   1150 C CB  . ILE   A 1 138 ? 2.236   -9.648  -50.712 1.00 20.10 ? 140 ILE   A CB  1 
ATOM   1151 C CG1 . ILE   A 1 138 ? 2.955   -8.353  -50.334 1.00 21.49 ? 140 ILE   A CG1 1 
ATOM   1152 C CG2 . ILE   A 1 138 ? 2.430   -10.699 -49.602 1.00 21.71 ? 140 ILE   A CG2 1 
ATOM   1153 C CD1 . ILE   A 1 138 ? 2.262   -7.601  -49.190 1.00 23.79 ? 140 ILE   A CD1 1 
ATOM   1154 N N   . LEU   A 1 139 ? 0.889   -11.564 -52.879 1.00 19.39 ? 141 LEU   A N   1 
ATOM   1155 C CA  . LEU   A 1 139 ? 0.247   -12.828 -53.213 1.00 20.93 ? 141 LEU   A CA  1 
ATOM   1156 C C   . LEU   A 1 139 ? 1.045   -13.601 -54.254 1.00 18.32 ? 141 LEU   A C   1 
ATOM   1157 O O   . LEU   A 1 139 ? 1.097   -14.837 -54.207 1.00 20.32 ? 141 LEU   A O   1 
ATOM   1158 C CB  . LEU   A 1 139 ? -1.183  -12.579 -53.702 1.00 18.55 ? 141 LEU   A CB  1 
ATOM   1159 C CG  . LEU   A 1 139 ? -2.174  -12.271 -52.586 1.00 20.69 ? 141 LEU   A CG  1 
ATOM   1160 C CD1 . LEU   A 1 139 ? -3.475  -11.771 -53.217 1.00 21.11 ? 141 LEU   A CD1 1 
ATOM   1161 C CD2 . LEU   A 1 139 ? -2.446  -13.507 -51.726 1.00 20.03 ? 141 LEU   A CD2 1 
ATOM   1162 N N   . LYS   A 1 140 ? 1.664   -12.898 -55.214 1.00 18.80 ? 142 LYS   A N   1 
ATOM   1163 C CA  . LYS   A 1 140 ? 2.505   -13.593 -56.180 1.00 20.63 ? 142 LYS   A CA  1 
ATOM   1164 C C   . LYS   A 1 140 ? 3.630   -14.335 -55.475 1.00 19.33 ? 142 LYS   A C   1 
ATOM   1165 O O   . LYS   A 1 140 ? 3.939   -15.483 -55.819 1.00 20.53 ? 142 LYS   A O   1 
ATOM   1166 C CB  . LYS   A 1 140 ? 3.092   -12.614 -57.191 1.00 24.13 ? 142 LYS   A CB  1 
ATOM   1167 C CG  . LYS   A 1 140 ? 2.124   -12.096 -58.213 1.00 23.84 ? 142 LYS   A CG  1 
ATOM   1168 C CD  . LYS   A 1 140 ? 2.872   -11.177 -59.163 1.00 30.32 ? 142 LYS   A CD  1 
ATOM   1169 C CE  . LYS   A 1 140 ? 1.934   -10.403 -60.066 1.00 40.53 ? 142 LYS   A CE  1 
ATOM   1170 N NZ  . LYS   A 1 140 ? 2.700   -9.382  -60.837 1.00 43.37 ? 142 LYS   A NZ  1 
ATOM   1171 N N   . ALA   A 1 141 ? 4.239   -13.698 -54.470 1.00 18.42 ? 143 ALA   A N   1 
ATOM   1172 C CA  . ALA   A 1 141 ? 5.341   -14.337 -53.757 1.00 18.68 ? 143 ALA   A CA  1 
ATOM   1173 C C   . ALA   A 1 141 ? 4.840   -15.516 -52.940 1.00 18.25 ? 143 ALA   A C   1 
ATOM   1174 O O   . ALA   A 1 141 ? 5.479   -16.572 -52.905 1.00 17.10 ? 143 ALA   A O   1 
ATOM   1175 C CB  . ALA   A 1 141 ? 6.047   -13.331 -52.845 1.00 17.05 ? 143 ALA   A CB  1 
ATOM   1176 N N   . LEU   A 1 142 ? 3.686   -15.347 -52.285 1.00 18.37 ? 144 LEU   A N   1 
ATOM   1177 C CA  . LEU   A 1 142 ? 3.148   -16.412 -51.447 1.00 17.80 ? 144 LEU   A CA  1 
ATOM   1178 C C   . LEU   A 1 142 ? 2.632   -17.582 -52.278 1.00 16.82 ? 144 LEU   A C   1 
ATOM   1179 O O   . LEU   A 1 142 ? 2.856   -18.742 -51.917 1.00 17.66 ? 144 LEU   A O   1 
ATOM   1180 C CB  . LEU   A 1 142 ? 2.048   -15.863 -50.539 1.00 16.27 ? 144 LEU   A CB  1 
ATOM   1181 C CG  . LEU   A 1 142 ? 2.528   -14.975 -49.390 1.00 18.55 ? 144 LEU   A CG  1 
ATOM   1182 C CD1 . LEU   A 1 142 ? 1.323   -14.473 -48.586 1.00 18.99 ? 144 LEU   A CD1 1 
ATOM   1183 C CD2 . LEU   A 1 142 ? 3.520   -15.717 -48.492 1.00 16.27 ? 144 LEU   A CD2 1 
ATOM   1184 N N   . ASP   A 1 143 ? 1.922   -17.325 -53.381 1.00 16.99 ? 145 ASP   A N   1 
ATOM   1185 C CA  . ASP   A 1 143 ? 1.539   -18.474 -54.193 1.00 20.86 ? 145 ASP   A CA  1 
ATOM   1186 C C   . ASP   A 1 143 ? 2.768   -19.202 -54.715 1.00 20.06 ? 145 ASP   A C   1 
ATOM   1187 O O   . ASP   A 1 143 ? 2.790   -20.441 -54.764 1.00 20.86 ? 145 ASP   A O   1 
ATOM   1188 C CB  . ASP   A 1 143 ? 0.642   -18.088 -55.357 1.00 23.71 ? 145 ASP   A CB  1 
ATOM   1189 C CG  . ASP   A 1 143 ? 0.249   -19.308 -56.170 1.00 31.01 ? 145 ASP   A CG  1 
ATOM   1190 O OD1 . ASP   A 1 143 ? -0.292  -20.268 -55.562 1.00 24.80 ? 145 ASP   A OD1 1 
ATOM   1191 O OD2 . ASP   A 1 143 ? 0.515   -19.329 -57.390 1.00 33.10 ? 145 ASP   A OD2 1 
ATOM   1192 N N   . TYR   A 1 144 ? 3.821   -18.461 -55.076 1.00 18.09 ? 146 TYR   A N   1 
ATOM   1193 C CA  . TYR   A 1 144 ? 5.025   -19.130 -55.545 1.00 19.36 ? 146 TYR   A CA  1 
ATOM   1194 C C   . TYR   A 1 144 ? 5.611   -20.026 -54.457 1.00 17.16 ? 146 TYR   A C   1 
ATOM   1195 O O   . TYR   A 1 144 ? 5.839   -21.220 -54.679 1.00 19.44 ? 146 TYR   A O   1 
ATOM   1196 C CB  . TYR   A 1 144 ? 6.075   -18.131 -56.035 1.00 18.67 ? 146 TYR   A CB  1 
ATOM   1197 C CG  . TYR   A 1 144 ? 7.227   -18.842 -56.708 1.00 18.95 ? 146 TYR   A CG  1 
ATOM   1198 C CD1 . TYR   A 1 144 ? 7.070   -19.392 -57.969 1.00 24.16 ? 146 TYR   A CD1 1 
ATOM   1199 C CD2 . TYR   A 1 144 ? 8.461   -18.988 -56.082 1.00 19.75 ? 146 TYR   A CD2 1 
ATOM   1200 C CE1 . TYR   A 1 144 ? 8.110   -20.043 -58.605 1.00 26.51 ? 146 TYR   A CE1 1 
ATOM   1201 C CE2 . TYR   A 1 144 ? 9.513   -19.650 -56.716 1.00 19.13 ? 146 TYR   A CE2 1 
ATOM   1202 C CZ  . TYR   A 1 144 ? 9.324   -20.174 -57.972 1.00 23.69 ? 146 TYR   A CZ  1 
ATOM   1203 O OH  . TYR   A 1 144 ? 10.357  -20.828 -58.600 1.00 25.26 ? 146 TYR   A OH  1 
ATOM   1204 N N   . CYS   A 1 145 ? 5.854   -19.484 -53.262 1.00 18.45 ? 147 CYS   A N   1 
ATOM   1205 C CA  . CYS   A 1 145 ? 6.528   -20.319 -52.275 1.00 19.39 ? 147 CYS   A CA  1 
ATOM   1206 C C   . CYS   A 1 145 ? 5.633   -21.470 -51.808 1.00 19.56 ? 147 CYS   A C   1 
ATOM   1207 O O   . CYS   A 1 145 ? 6.120   -22.597 -51.631 1.00 18.25 ? 147 CYS   A O   1 
ATOM   1208 C CB  . CYS   A 1 145 ? 7.065   -19.477 -51.110 1.00 19.88 ? 147 CYS   A CB  1 
ATOM   1209 S SG  . CYS   A 1 145 ? 5.915   -18.767 -49.942 1.00 21.99 ? 147 CYS   A SG  1 
ATOM   1210 N N   . HIS   A 1 146 ? 4.324   -21.231 -51.722 1.00 19.02 ? 148 HIS   A N   1 
ATOM   1211 C CA  . HIS   A 1 146 ? 3.412   -22.344 -51.356 1.00 17.64 ? 148 HIS   A CA  1 
ATOM   1212 C C   . HIS   A 1 146 ? 3.460   -23.405 -52.465 1.00 17.16 ? 148 HIS   A C   1 
ATOM   1213 O O   . HIS   A 1 146 ? 3.521   -24.589 -52.136 1.00 17.71 ? 148 HIS   A O   1 
ATOM   1214 C CB  . HIS   A 1 146 ? 1.984   -21.837 -51.132 1.00 16.57 ? 148 HIS   A CB  1 
ATOM   1215 C CG  . HIS   A 1 146 ? 1.853   -20.896 -49.985 1.00 15.81 ? 148 HIS   A CG  1 
ATOM   1216 N ND1 . HIS   A 1 146 ? 0.718   -20.145 -49.777 1.00 15.90 ? 148 HIS   A ND1 1 
ATOM   1217 C CD2 . HIS   A 1 146 ? 2.705   -20.590 -48.986 1.00 17.13 ? 148 HIS   A CD2 1 
ATOM   1218 C CE1 . HIS   A 1 146 ? 0.881   -19.408 -48.700 1.00 17.22 ? 148 HIS   A CE1 1 
ATOM   1219 N NE2 . HIS   A 1 146 ? 2.093   -19.659 -48.200 1.00 16.72 ? 148 HIS   A NE2 1 
ATOM   1220 N N   . SER   A 1 147 ? 3.422   -22.979 -53.731 1.00 19.59 ? 149 SER   A N   1 
ATOM   1221 C CA  . SER   A 1 147 ? 3.470   -23.931 -54.843 1.00 16.25 ? 149 SER   A CA  1 
ATOM   1222 C C   . SER   A 1 147 ? 4.782   -24.697 -54.871 1.00 20.02 ? 149 SER   A C   1 
ATOM   1223 O O   . SER   A 1 147 ? 4.855   -25.787 -55.463 1.00 20.60 ? 149 SER   A O   1 
ATOM   1224 C CB  . SER   A 1 147 ? 3.256   -23.199 -56.176 1.00 19.04 ? 149 SER   A CB  1 
ATOM   1225 O OG  . SER   A 1 147 ? 4.448   -22.546 -56.608 1.00 21.52 ? 149 SER   A OG  1 
ATOM   1226 N N   . MET   A 1 148 ? 5.816   -24.142 -54.243 1.00 19.59 ? 150 MET   A N   1 
ATOM   1227 C CA  . MET   A 1 148 ? 7.114   -24.776 -54.113 1.00 22.00 ? 150 MET   A CA  1 
ATOM   1228 C C   . MET   A 1 148 ? 7.245   -25.527 -52.798 1.00 20.94 ? 150 MET   A C   1 
ATOM   1229 O O   . MET   A 1 148 ? 8.342   -25.962 -52.444 1.00 22.11 ? 150 MET   A O   1 
ATOM   1230 C CB  . MET   A 1 148 ? 8.206   -23.712 -54.271 1.00 19.89 ? 150 MET   A CB  1 
ATOM   1231 C CG  . MET   A 1 148 ? 8.187   -23.047 -55.648 1.00 21.71 ? 150 MET   A CG  1 
ATOM   1232 S SD  . MET   A 1 148 ? 8.840   -24.140 -56.944 1.00 24.93 ? 150 MET   A SD  1 
ATOM   1233 C CE  . MET   A 1 148 ? 10.601  -24.043 -56.549 1.00 23.41 ? 150 MET   A CE  1 
ATOM   1234 N N   . GLY   A 1 149 ? 6.143   -25.710 -52.072 1.00 19.67 ? 151 GLY   A N   1 
ATOM   1235 C CA  . GLY   A 1 149 ? 6.175   -26.531 -50.879 1.00 21.19 ? 151 GLY   A CA  1 
ATOM   1236 C C   . GLY   A 1 149 ? 6.679   -25.865 -49.617 1.00 20.55 ? 151 GLY   A C   1 
ATOM   1237 O O   . GLY   A 1 149 ? 7.060   -26.565 -48.677 1.00 19.43 ? 151 GLY   A O   1 
ATOM   1238 N N   . ILE   A 1 150 ? 6.681   -24.538 -49.549 1.00 19.13 ? 152 ILE   A N   1 
ATOM   1239 C CA  . ILE   A 1 150 ? 7.292   -23.817 -48.439 1.00 19.93 ? 152 ILE   A CA  1 
ATOM   1240 C C   . ILE   A 1 150 ? 6.282   -22.851 -47.832 1.00 19.15 ? 152 ILE   A C   1 
ATOM   1241 O O   . ILE   A 1 150 ? 5.558   -22.149 -48.552 1.00 19.51 ? 152 ILE   A O   1 
ATOM   1242 C CB  . ILE   A 1 150 ? 8.563   -23.088 -48.930 1.00 19.36 ? 152 ILE   A CB  1 
ATOM   1243 C CG1 . ILE   A 1 150 ? 9.621   -24.148 -49.278 1.00 17.79 ? 152 ILE   A CG1 1 
ATOM   1244 C CG2 . ILE   A 1 150 ? 9.029   -22.049 -47.900 1.00 19.00 ? 152 ILE   A CG2 1 
ATOM   1245 C CD1 . ILE   A 1 150 ? 10.674  -23.695 -50.272 1.00 26.61 ? 152 ILE   A CD1 1 
ATOM   1246 N N   . MET   A 1 151 ? 6.217   -22.814 -46.501 1.00 17.75 ? 153 MET   A N   1 
ATOM   1247 C CA  . MET   A 1 151 ? 5.461   -21.767 -45.824 1.00 18.53 ? 153 MET   A CA  1 
ATOM   1248 C C   . MET   A 1 151 ? 6.420   -20.763 -45.195 1.00 16.24 ? 153 MET   A C   1 
ATOM   1249 O O   . MET   A 1 151 ? 7.487   -21.136 -44.687 1.00 17.64 ? 153 MET   A O   1 
ATOM   1250 C CB  . MET   A 1 151 ? 4.498   -22.329 -44.769 1.00 27.46 ? 153 MET   A CB  1 
ATOM   1251 C CG  . MET   A 1 151 ? 5.007   -23.442 -43.925 1.00 27.60 ? 153 MET   A CG  1 
ATOM   1252 S SD  . MET   A 1 151 ? 3.698   -24.274 -42.952 1.00 25.62 ? 153 MET   A SD  1 
ATOM   1253 C CE  . MET   A 1 151 ? 4.682   -25.634 -42.335 1.00 26.97 ? 153 MET   A CE  1 
ATOM   1254 N N   . HIS   A 1 152 ? 6.051   -19.483 -45.262 1.00 18.15 ? 154 HIS   A N   1 
ATOM   1255 C CA  . HIS   A 1 152 ? 6.952   -18.423 -44.813 1.00 15.11 ? 154 HIS   A CA  1 
ATOM   1256 C C   . HIS   A 1 152 ? 6.980   -18.322 -43.288 1.00 16.94 ? 154 HIS   A C   1 
ATOM   1257 O O   . HIS   A 1 152 ? 8.061   -18.286 -42.679 1.00 18.14 ? 154 HIS   A O   1 
ATOM   1258 C CB  . HIS   A 1 152 ? 6.547   -17.085 -45.454 1.00 16.48 ? 154 HIS   A CB  1 
ATOM   1259 C CG  . HIS   A 1 152 ? 7.485   -15.955 -45.132 1.00 16.44 ? 154 HIS   A CG  1 
ATOM   1260 N ND1 . HIS   A 1 152 ? 7.457   -15.275 -43.929 1.00 18.37 ? 154 HIS   A ND1 1 
ATOM   1261 C CD2 . HIS   A 1 152 ? 8.484   -15.393 -45.855 1.00 18.38 ? 154 HIS   A CD2 1 
ATOM   1262 C CE1 . HIS   A 1 152 ? 8.404   -14.353 -43.923 1.00 18.64 ? 154 HIS   A CE1 1 
ATOM   1263 N NE2 . HIS   A 1 152 ? 9.036   -14.395 -45.084 1.00 16.30 ? 154 HIS   A NE2 1 
ATOM   1264 N N   . ARG   A 1 153 ? 5.804   -18.289 -42.660 1.00 16.71 ? 155 ARG   A N   1 
ATOM   1265 C CA  . ARG   A 1 153 ? 5.607   -18.330 -41.210 1.00 18.65 ? 155 ARG   A CA  1 
ATOM   1266 C C   . ARG   A 1 153 ? 6.054   -17.067 -40.485 1.00 19.42 ? 155 ARG   A C   1 
ATOM   1267 O O   . ARG   A 1 153 ? 6.075   -17.055 -39.244 1.00 19.17 ? 155 ARG   A O   1 
ATOM   1268 C CB  . ARG   A 1 153 ? 6.296   -19.541 -40.567 1.00 19.12 ? 155 ARG   A CB  1 
ATOM   1269 C CG  . ARG   A 1 153 ? 5.845   -20.866 -41.191 1.00 16.45 ? 155 ARG   A CG  1 
ATOM   1270 C CD  . ARG   A 1 153 ? 6.083   -22.047 -40.248 1.00 15.99 ? 155 ARG   A CD  1 
ATOM   1271 N NE  . ARG   A 1 153 ? 7.500   -22.156 -39.887 1.00 17.41 ? 155 ARG   A NE  1 
ATOM   1272 C CZ  . ARG   A 1 153 ? 7.997   -23.073 -39.062 1.00 21.22 ? 155 ARG   A CZ  1 
ATOM   1273 N NH1 . ARG   A 1 153 ? 7.199   -23.985 -38.506 1.00 20.33 ? 155 ARG   A NH1 1 
ATOM   1274 N NH2 . ARG   A 1 153 ? 9.303   -23.088 -38.798 1.00 19.35 ? 155 ARG   A NH2 1 
ATOM   1275 N N   . ASP   A 1 154 ? 6.376   -15.992 -41.197 1.00 17.44 ? 156 ASP   A N   1 
ATOM   1276 C CA  . ASP   A 1 154 ? 6.656   -14.723 -40.522 1.00 13.85 ? 156 ASP   A CA  1 
ATOM   1277 C C   . ASP   A 1 154 ? 6.234   -13.571 -41.428 1.00 16.72 ? 156 ASP   A C   1 
ATOM   1278 O O   . ASP   A 1 154 ? 6.951   -12.585 -41.600 1.00 17.77 ? 156 ASP   A O   1 
ATOM   1279 C CB  . ASP   A 1 154 ? 8.135   -14.638 -40.128 1.00 16.04 ? 156 ASP   A CB  1 
ATOM   1280 C CG  . ASP   A 1 154 ? 8.416   -13.587 -39.046 1.00 20.75 ? 156 ASP   A CG  1 
ATOM   1281 O OD1 . ASP   A 1 154 ? 7.490   -13.160 -38.322 1.00 20.93 ? 156 ASP   A OD1 1 
ATOM   1282 O OD2 . ASP   A 1 154 ? 9.600   -13.189 -38.913 1.00 24.21 ? 156 ASP   A OD2 1 
ATOM   1283 N N   . VAL   A 1 155 ? 5.026   -13.660 -41.995 1.00 16.20 ? 157 VAL   A N   1 
ATOM   1284 C CA  . VAL   A 1 155 ? 4.533   -12.560 -42.810 1.00 15.27 ? 157 VAL   A CA  1 
ATOM   1285 C C   . VAL   A 1 155 ? 4.143   -11.407 -41.892 1.00 19.31 ? 157 VAL   A C   1 
ATOM   1286 O O   . VAL   A 1 155 ? 3.375   -11.581 -40.937 1.00 18.41 ? 157 VAL   A O   1 
ATOM   1287 C CB  . VAL   A 1 155 ? 3.347   -13.013 -43.676 1.00 17.09 ? 157 VAL   A CB  1 
ATOM   1288 C CG1 . VAL   A 1 155 ? 2.747   -11.829 -44.390 1.00 18.54 ? 157 VAL   A CG1 1 
ATOM   1289 C CG2 . VAL   A 1 155 ? 3.804   -14.099 -44.668 1.00 20.58 ? 157 VAL   A CG2 1 
ATOM   1290 N N   . LYS   A 1 156 ? 4.699   -10.235 -42.161 1.00 16.61 ? 158 LYS   A N   1 
ATOM   1291 C CA  . LYS   A 1 156 ? 4.428   -9.018  -41.404 1.00 17.57 ? 158 LYS   A CA  1 
ATOM   1292 C C   . LYS   A 1 156 ? 5.005   -7.849  -42.201 1.00 17.98 ? 158 LYS   A C   1 
ATOM   1293 O O   . LYS   A 1 156 ? 5.817   -8.060  -43.104 1.00 16.80 ? 158 LYS   A O   1 
ATOM   1294 C CB  . LYS   A 1 156 ? 5.046   -9.088  -39.993 1.00 17.61 ? 158 LYS   A CB  1 
ATOM   1295 C CG  . LYS   A 1 156 ? 6.565   -9.239  -39.991 1.00 17.67 ? 158 LYS   A CG  1 
ATOM   1296 C CD  . LYS   A 1 156 ? 7.135   -9.379  -38.578 1.00 19.90 ? 158 LYS   A CD  1 
ATOM   1297 C CE  . LYS   A 1 156 ? 8.641   -9.488  -38.602 1.00 25.05 ? 158 LYS   A CE  1 
ATOM   1298 N NZ  . LYS   A 1 156 ? 9.188   -9.599  -37.208 1.00 34.14 ? 158 LYS   A NZ  1 
ATOM   1299 N N   . PRO   A 1 157 ? 4.584   -6.611  -41.903 1.00 18.51 ? 159 PRO   A N   1 
ATOM   1300 C CA  . PRO   A 1 157 ? 5.040   -5.479  -42.727 1.00 18.56 ? 159 PRO   A CA  1 
ATOM   1301 C C   . PRO   A 1 157 ? 6.552   -5.325  -42.780 1.00 18.05 ? 159 PRO   A C   1 
ATOM   1302 O O   . PRO   A 1 157 ? 7.088   -4.944  -43.825 1.00 20.34 ? 159 PRO   A O   1 
ATOM   1303 C CB  . PRO   A 1 157 ? 4.376   -4.273  -42.051 1.00 23.28 ? 159 PRO   A CB  1 
ATOM   1304 C CG  . PRO   A 1 157 ? 3.143   -4.832  -41.431 1.00 21.27 ? 159 PRO   A CG  1 
ATOM   1305 C CD  . PRO   A 1 157 ? 3.496   -6.222  -40.987 1.00 18.37 ? 159 PRO   A CD  1 
ATOM   1306 N N   . HIS   A 1 158 ? 7.245   -5.608  -41.674 1.00 17.31 ? 160 HIS   A N   1 
ATOM   1307 C CA  . HIS   A 1 158 ? 8.702   -5.475  -41.622 1.00 20.09 ? 160 HIS   A CA  1 
ATOM   1308 C C   . HIS   A 1 158 ? 9.410   -6.436  -42.563 1.00 22.11 ? 160 HIS   A C   1 
ATOM   1309 O O   . HIS   A 1 158 ? 10.600  -6.244  -42.842 1.00 23.61 ? 160 HIS   A O   1 
ATOM   1310 C CB  . HIS   A 1 158 ? 9.201   -5.709  -40.200 1.00 25.88 ? 160 HIS   A CB  1 
ATOM   1311 C CG  . HIS   A 1 158 ? 9.169   -4.484  -39.339 1.00 54.57 ? 160 HIS   A CG  1 
ATOM   1312 N ND1 . HIS   A 1 158 ? 8.604   -4.470  -38.081 1.00 60.73 ? 160 HIS   A ND1 1 
ATOM   1313 C CD2 . HIS   A 1 158 ? 9.647   -3.234  -39.552 1.00 62.09 ? 160 HIS   A CD2 1 
ATOM   1314 C CE1 . HIS   A 1 158 ? 8.731   -3.263  -37.559 1.00 64.56 ? 160 HIS   A CE1 1 
ATOM   1315 N NE2 . HIS   A 1 158 ? 9.362   -2.495  -38.429 1.00 62.87 ? 160 HIS   A NE2 1 
ATOM   1316 N N   . ASN   A 1 159 ? 8.726   -7.480  -43.039 1.00 18.91 ? 161 ASN   A N   1 
ATOM   1317 C CA  . ASN   A 1 159 ? 9.352   -8.445  -43.934 1.00 16.25 ? 161 ASN   A CA  1 
ATOM   1318 C C   . ASN   A 1 159 ? 8.919   -8.273  -45.383 1.00 15.45 ? 161 ASN   A C   1 
ATOM   1319 O O   . ASN   A 1 159 ? 9.146   -9.170  -46.208 1.00 18.66 ? 161 ASN   A O   1 
ATOM   1320 C CB  . ASN   A 1 159 ? 9.070   -9.863  -43.454 1.00 18.75 ? 161 ASN   A CB  1 
ATOM   1321 C CG  . ASN   A 1 159 ? 9.886   -10.215 -42.226 1.00 21.07 ? 161 ASN   A CG  1 
ATOM   1322 O OD1 . ASN   A 1 159 ? 10.919  -9.578  -41.926 1.00 21.83 ? 161 ASN   A OD1 1 
ATOM   1323 N ND2 . ASN   A 1 159 ? 9.438   -11.227 -41.504 1.00 17.92 ? 161 ASN   A ND2 1 
ATOM   1324 N N   . VAL   A 1 160 ? 8.317   -7.140  -45.710 1.00 19.26 ? 162 VAL   A N   1 
ATOM   1325 C CA  . VAL   A 1 160 ? 7.925   -6.816  -47.075 1.00 19.31 ? 162 VAL   A CA  1 
ATOM   1326 C C   . VAL   A 1 160 ? 8.692   -5.552  -47.426 1.00 22.35 ? 162 VAL   A C   1 
ATOM   1327 O O   . VAL   A 1 160 ? 8.335   -4.455  -46.979 1.00 27.96 ? 162 VAL   A O   1 
ATOM   1328 C CB  . VAL   A 1 160 ? 6.409   -6.624  -47.216 1.00 20.98 ? 162 VAL   A CB  1 
ATOM   1329 C CG1 . VAL   A 1 160 ? 6.043   -6.268  -48.634 1.00 24.25 ? 162 VAL   A CG1 1 
ATOM   1330 C CG2 . VAL   A 1 160 ? 5.675   -7.887  -46.789 1.00 25.97 ? 162 VAL   A CG2 1 
ATOM   1331 N N   . MET   A 1 161 ? 9.775   -5.695  -48.188 1.00 21.61 ? 163 MET   A N   1 
ATOM   1332 C CA  . MET   A 1 161 ? 10.581  -4.550  -48.582 1.00 22.84 ? 163 MET   A CA  1 
ATOM   1333 C C   . MET   A 1 161 ? 10.014  -3.953  -49.859 1.00 23.64 ? 163 MET   A C   1 
ATOM   1334 O O   . MET   A 1 161 ? 9.842   -4.661  -50.855 1.00 26.17 ? 163 MET   A O   1 
ATOM   1335 C CB  . MET   A 1 161 ? 12.041  -4.953  -48.798 1.00 23.93 ? 163 MET   A CB  1 
ATOM   1336 C CG  . MET   A 1 161 ? 12.771  -5.374  -47.526 1.00 30.41 ? 163 MET   A CG  1 
ATOM   1337 S SD  . MET   A 1 161 ? 13.040  -3.976  -46.421 1.00 32.71 ? 163 MET   A SD  1 
ATOM   1338 C CE  . MET   A 1 161 ? 12.396  -4.598  -44.875 1.00 39.15 ? 163 MET   A CE  1 
ATOM   1339 N N   . ILE   A 1 162 ? 9.738   -2.651  -49.832 1.00 22.59 ? 164 ILE   A N   1 
ATOM   1340 C CA  . ILE   A 1 162 ? 9.151   -1.960  -50.973 1.00 21.93 ? 164 ILE   A CA  1 
ATOM   1341 C C   . ILE   A 1 162 ? 10.036  -0.779  -51.360 1.00 26.87 ? 164 ILE   A C   1 
ATOM   1342 O O   . ILE   A 1 162 ? 10.317  0.093   -50.530 1.00 29.23 ? 164 ILE   A O   1 
ATOM   1343 C CB  . ILE   A 1 162 ? 7.719   -1.484  -50.675 1.00 20.74 ? 164 ILE   A CB  1 
ATOM   1344 C CG1 . ILE   A 1 162 ? 6.823   -2.679  -50.355 1.00 23.69 ? 164 ILE   A CG1 1 
ATOM   1345 C CG2 . ILE   A 1 162 ? 7.178   -0.670  -51.846 1.00 24.74 ? 164 ILE   A CG2 1 
ATOM   1346 C CD1 . ILE   A 1 162 ? 5.431   -2.294  -49.820 1.00 25.49 ? 164 ILE   A CD1 1 
ATOM   1347 N N   . ASP   A 1 163 ? 10.464  -0.751  -52.620 1.00 25.94 ? 165 ASP   A N   1 
ATOM   1348 C CA  . ASP   A 1 163 ? 11.080  0.424   -53.235 1.00 31.37 ? 165 ASP   A CA  1 
ATOM   1349 C C   . ASP   A 1 163 ? 9.960   1.119   -54.001 1.00 29.80 ? 165 ASP   A C   1 
ATOM   1350 O O   . ASP   A 1 163 ? 9.667   0.785   -55.148 1.00 30.95 ? 165 ASP   A O   1 
ATOM   1351 C CB  . ASP   A 1 163 ? 12.241  0.028   -54.142 1.00 31.57 ? 165 ASP   A CB  1 
ATOM   1352 C CG  . ASP   A 1 163 ? 12.840  1.214   -54.888 1.00 36.35 ? 165 ASP   A CG  1 
ATOM   1353 O OD1 . ASP   A 1 163 ? 12.327  2.346   -54.766 1.00 35.69 ? 165 ASP   A OD1 1 
ATOM   1354 O OD2 . ASP   A 1 163 ? 13.836  1.012   -55.606 1.00 32.86 ? 165 ASP   A OD2 1 
ATOM   1355 N N   . HIS   A 1 164 ? 9.332   2.101   -53.349 1.00 27.41 ? 166 HIS   A N   1 
ATOM   1356 C CA  . HIS   A 1 164 ? 8.120   2.696   -53.903 1.00 28.97 ? 166 HIS   A CA  1 
ATOM   1357 C C   . HIS   A 1 164 ? 8.402   3.443   -55.198 1.00 36.77 ? 166 HIS   A C   1 
ATOM   1358 O O   . HIS   A 1 164 ? 7.521   3.542   -56.057 1.00 37.23 ? 166 HIS   A O   1 
ATOM   1359 C CB  . HIS   A 1 164 ? 7.484   3.627   -52.869 1.00 26.79 ? 166 HIS   A CB  1 
ATOM   1360 C CG  . HIS   A 1 164 ? 6.091   4.052   -53.211 1.00 31.44 ? 166 HIS   A CG  1 
ATOM   1361 N ND1 . HIS   A 1 164 ? 5.127   3.167   -53.640 1.00 32.96 ? 166 HIS   A ND1 1 
ATOM   1362 C CD2 . HIS   A 1 164 ? 5.497   5.269   -53.176 1.00 33.19 ? 166 HIS   A CD2 1 
ATOM   1363 C CE1 . HIS   A 1 164 ? 3.998   3.819   -53.854 1.00 38.19 ? 166 HIS   A CE1 1 
ATOM   1364 N NE2 . HIS   A 1 164 ? 4.195   5.096   -53.581 1.00 38.74 ? 166 HIS   A NE2 1 
ATOM   1365 N N   . GLU   A 1 165 ? 9.623   3.958   -55.362 1.00 38.59 ? 167 GLU   A N   1 
ATOM   1366 C CA  . GLU   A 1 165 ? 9.962   4.695   -56.575 1.00 41.91 ? 167 GLU   A CA  1 
ATOM   1367 C C   . GLU   A 1 165 ? 9.840   3.816   -57.812 1.00 39.57 ? 167 GLU   A C   1 
ATOM   1368 O O   . GLU   A 1 165 ? 9.356   4.266   -58.856 1.00 40.87 ? 167 GLU   A O   1 
ATOM   1369 C CB  . GLU   A 1 165 ? 11.375  5.266   -56.452 1.00 51.88 ? 167 GLU   A CB  1 
ATOM   1370 C CG  . GLU   A 1 165 ? 11.910  5.901   -57.721 1.00 61.37 ? 167 GLU   A CG  1 
ATOM   1371 C CD  . GLU   A 1 165 ? 13.119  6.778   -57.460 1.00 71.36 ? 167 GLU   A CD  1 
ATOM   1372 O OE1 . GLU   A 1 165 ? 13.435  7.013   -56.273 1.00 71.77 ? 167 GLU   A OE1 1 
ATOM   1373 O OE2 . GLU   A 1 165 ? 13.751  7.233   -58.439 1.00 75.16 ? 167 GLU   A OE2 1 
ATOM   1374 N N   . HIS   A 1 166 ? 10.269  2.558   -57.717 1.00 39.55 ? 168 HIS   A N   1 
ATOM   1375 C CA  . HIS   A 1 166 ? 10.198  1.628   -58.834 1.00 39.52 ? 168 HIS   A CA  1 
ATOM   1376 C C   . HIS   A 1 166 ? 9.073   0.615   -58.689 1.00 36.81 ? 168 HIS   A C   1 
ATOM   1377 O O   . HIS   A 1 166 ? 9.019   -0.345  -59.465 1.00 35.43 ? 168 HIS   A O   1 
ATOM   1378 C CB  . HIS   A 1 166 ? 11.536  0.909   -59.004 1.00 43.29 ? 168 HIS   A CB  1 
ATOM   1379 C CG  . HIS   A 1 166 ? 12.665  1.834   -59.324 1.00 51.72 ? 168 HIS   A CG  1 
ATOM   1380 N ND1 . HIS   A 1 166 ? 13.575  2.254   -58.378 1.00 53.31 ? 168 HIS   A ND1 1 
ATOM   1381 C CD2 . HIS   A 1 166 ? 13.009  2.452   -60.478 1.00 53.48 ? 168 HIS   A CD2 1 
ATOM   1382 C CE1 . HIS   A 1 166 ? 14.442  3.077   -58.940 1.00 54.92 ? 168 HIS   A CE1 1 
ATOM   1383 N NE2 . HIS   A 1 166 ? 14.120  3.215   -60.213 1.00 55.92 ? 168 HIS   A NE2 1 
ATOM   1384 N N   . ARG   A 1 167 ? 8.172   0.816   -57.723 1.00 34.67 ? 169 ARG   A N   1 
ATOM   1385 C CA  . ARG   A 1 167 ? 7.042   -0.084  -57.495 1.00 31.45 ? 169 ARG   A CA  1 
ATOM   1386 C C   . ARG   A 1 167 ? 7.514   -1.532  -57.391 1.00 28.35 ? 169 ARG   A C   1 
ATOM   1387 O O   . ARG   A 1 167 ? 6.902   -2.451  -57.937 1.00 33.30 ? 169 ARG   A O   1 
ATOM   1388 C CB  . ARG   A 1 167 ? 5.987   0.084   -58.586 1.00 35.04 ? 169 ARG   A CB  1 
ATOM   1389 C CG  . ARG   A 1 167 ? 5.491   1.517   -58.731 1.00 39.05 ? 169 ARG   A CG  1 
ATOM   1390 C CD  . ARG   A 1 167 ? 4.941   2.037   -57.410 1.00 45.30 ? 169 ARG   A CD  1 
ATOM   1391 N NE  . ARG   A 1 167 ? 4.033   3.172   -57.576 1.00 54.94 ? 169 ARG   A NE  1 
ATOM   1392 C CZ  . ARG   A 1 167 ? 4.348   4.440   -57.319 1.00 56.10 ? 169 ARG   A CZ  1 
ATOM   1393 N NH1 . ARG   A 1 167 ? 5.558   4.755   -56.880 1.00 48.53 ? 169 ARG   A NH1 1 
ATOM   1394 N NH2 . ARG   A 1 167 ? 3.446   5.399   -57.499 1.00 59.21 ? 169 ARG   A NH2 1 
ATOM   1395 N N   . LYS   A 1 168 ? 8.619   -1.723  -56.676 1.00 26.44 ? 170 LYS   A N   1 
ATOM   1396 C CA  . LYS   A 1 168 ? 9.307   -3.001  -56.537 1.00 31.41 ? 170 LYS   A CA  1 
ATOM   1397 C C   . LYS   A 1 168 ? 9.102   -3.544  -55.127 1.00 25.98 ? 170 LYS   A C   1 
ATOM   1398 O O   . LYS   A 1 168 ? 9.270   -2.808  -54.151 1.00 29.66 ? 170 LYS   A O   1 
ATOM   1399 C CB  . LYS   A 1 168 ? 10.800  -2.811  -56.823 1.00 30.63 ? 170 LYS   A CB  1 
ATOM   1400 C CG  . LYS   A 1 168 ? 11.688  -3.999  -56.506 1.00 34.78 ? 170 LYS   A CG  1 
ATOM   1401 C CD  . LYS   A 1 168 ? 13.120  -3.535  -56.238 1.00 41.03 ? 170 LYS   A CD  1 
ATOM   1402 C CE  . LYS   A 1 168 ? 14.092  -4.078  -57.261 1.00 40.56 ? 170 LYS   A CE  1 
ATOM   1403 N NZ  . LYS   A 1 168 ? 15.490  -3.657  -56.935 1.00 40.33 ? 170 LYS   A NZ  1 
ATOM   1404 N N   . LEU   A 1 169 ? 8.770   -4.832  -55.018 1.00 23.44 ? 171 LEU   A N   1 
ATOM   1405 C CA  . LEU   A 1 169 ? 8.479   -5.455  -53.731 1.00 20.83 ? 171 LEU   A CA  1 
ATOM   1406 C C   . LEU   A 1 169 ? 9.250   -6.760  -53.588 1.00 22.57 ? 171 LEU   A C   1 
ATOM   1407 O O   . LEU   A 1 169 ? 9.325   -7.549  -54.538 1.00 21.49 ? 171 LEU   A O   1 
ATOM   1408 C CB  . LEU   A 1 169 ? 6.956   -5.701  -53.596 1.00 22.57 ? 171 LEU   A CB  1 
ATOM   1409 C CG  . LEU   A 1 169 ? 6.440   -6.291  -52.286 1.00 22.20 ? 171 LEU   A CG  1 
ATOM   1410 C CD1 . LEU   A 1 169 ? 5.028   -5.785  -51.987 1.00 20.73 ? 171 LEU   A CD1 1 
ATOM   1411 C CD2 . LEU   A 1 169 ? 6.462   -7.818  -52.321 1.00 22.09 ? 171 LEU   A CD2 1 
ATOM   1412 N N   . ARG   A 1 170 ? 9.803   -7.000  -52.391 1.00 19.83 ? 172 ARG   A N   1 
ATOM   1413 C CA  . ARG   A 1 170 ? 10.455  -8.268  -52.093 1.00 17.24 ? 172 ARG   A CA  1 
ATOM   1414 C C   . ARG   A 1 170 ? 10.032  -8.781  -50.727 1.00 18.53 ? 172 ARG   A C   1 
ATOM   1415 O O   . ARG   A 1 170 ? 10.090  -8.048  -49.731 1.00 18.71 ? 172 ARG   A O   1 
ATOM   1416 C CB  . ARG   A 1 170 ? 11.987  -8.140  -52.123 1.00 17.66 ? 172 ARG   A CB  1 
ATOM   1417 C CG  . ARG   A 1 170 ? 12.554  -7.761  -53.483 1.00 21.24 ? 172 ARG   A CG  1 
ATOM   1418 C CD  . ARG   A 1 170 ? 12.458  -8.912  -54.458 1.00 24.43 ? 172 ARG   A CD  1 
ATOM   1419 N NE  . ARG   A 1 170 ? 13.105  -8.581  -55.725 1.00 24.57 ? 172 ARG   A NE  1 
ATOM   1420 C CZ  . ARG   A 1 170 ? 12.490  -8.066  -56.786 1.00 29.91 ? 172 ARG   A CZ  1 
ATOM   1421 N NH1 . ARG   A 1 170 ? 11.183  -7.815  -56.766 1.00 27.37 ? 172 ARG   A NH1 1 
ATOM   1422 N NH2 . ARG   A 1 170 ? 13.189  -7.811  -57.883 1.00 37.25 ? 172 ARG   A NH2 1 
ATOM   1423 N N   . LEU   A 1 171 ? 9.648   -10.048 -50.683 1.00 17.54 ? 173 LEU   A N   1 
ATOM   1424 C CA  . LEU   A 1 171 ? 9.382   -10.732 -49.423 1.00 15.07 ? 173 LEU   A CA  1 
ATOM   1425 C C   . LEU   A 1 171 ? 10.711  -11.245 -48.862 1.00 18.75 ? 173 LEU   A C   1 
ATOM   1426 O O   . LEU   A 1 171 ? 11.413  -12.017 -49.527 1.00 18.71 ? 173 LEU   A O   1 
ATOM   1427 C CB  . LEU   A 1 171 ? 8.390   -11.873 -49.654 1.00 19.85 ? 173 LEU   A CB  1 
ATOM   1428 C CG  . LEU   A 1 171 ? 7.947   -12.718 -48.456 1.00 21.83 ? 173 LEU   A CG  1 
ATOM   1429 C CD1 . LEU   A 1 171 ? 7.336   -11.859 -47.348 1.00 20.98 ? 173 LEU   A CD1 1 
ATOM   1430 C CD2 . LEU   A 1 171 ? 6.973   -13.785 -48.927 1.00 22.59 ? 173 LEU   A CD2 1 
ATOM   1431 N N   . ILE   A 1 172 ? 11.055  -10.826 -47.645 1.00 16.50 ? 174 ILE   A N   1 
ATOM   1432 C CA  . ILE   A 1 172 ? 12.364  -11.135 -47.063 1.00 17.26 ? 174 ILE   A CA  1 
ATOM   1433 C C   . ILE   A 1 172 ? 12.216  -11.982 -45.801 1.00 18.84 ? 174 ILE   A C   1 
ATOM   1434 O O   . ILE   A 1 172 ? 11.101  -12.340 -45.393 1.00 18.12 ? 174 ILE   A O   1 
ATOM   1435 C CB  . ILE   A 1 172 ? 13.157  -9.856  -46.734 1.00 18.38 ? 174 ILE   A CB  1 
ATOM   1436 C CG1 . ILE   A 1 172 ? 12.440  -9.026  -45.665 1.00 20.08 ? 174 ILE   A CG1 1 
ATOM   1437 C CG2 . ILE   A 1 172 ? 13.425  -9.015  -47.990 1.00 18.51 ? 174 ILE   A CG2 1 
ATOM   1438 C CD1 . ILE   A 1 172 ? 13.379  -8.052  -44.939 1.00 20.62 ? 174 ILE   A CD1 1 
ATOM   1439 N N   . ASP   A 1 173 ? 13.354  -12.311 -45.190 1.00 19.79 ? 175 ASP   A N   1 
ATOM   1440 C CA  . ASP   A 1 173 ? 13.465  -12.955 -43.874 1.00 22.97 ? 175 ASP   A CA  1 
ATOM   1441 C C   . ASP   A 1 173 ? 12.793  -14.330 -43.829 1.00 19.27 ? 175 ASP   A C   1 
ATOM   1442 O O   . ASP   A 1 173 ? 11.779  -14.559 -43.155 1.00 21.00 ? 175 ASP   A O   1 
ATOM   1443 C CB  . ASP   A 1 173 ? 12.930  -12.053 -42.758 1.00 22.75 ? 175 ASP   A CB  1 
ATOM   1444 C CG  . ASP   A 1 173 ? 13.368  -12.513 -41.373 1.00 34.41 ? 175 ASP   A CG  1 
ATOM   1445 O OD1 . ASP   A 1 173 ? 13.928  -13.624 -41.251 1.00 33.04 ? 175 ASP   A OD1 1 
ATOM   1446 O OD2 . ASP   A 1 173 ? 13.161  -11.748 -40.408 1.00 39.68 ? 175 ASP   A OD2 1 
ATOM   1447 N N   . TRP   A 1 174 ? 13.420  -15.249 -44.560 1.00 18.70 ? 176 TRP   A N   1 
ATOM   1448 C CA  . TRP   A 1 174 ? 12.989  -16.635 -44.640 1.00 20.38 ? 176 TRP   A CA  1 
ATOM   1449 C C   . TRP   A 1 174 ? 13.540  -17.506 -43.512 1.00 17.52 ? 176 TRP   A C   1 
ATOM   1450 O O   . TRP   A 1 174 ? 13.529  -18.743 -43.625 1.00 20.48 ? 176 TRP   A O   1 
ATOM   1451 C CB  . TRP   A 1 174 ? 13.364  -17.192 -46.020 1.00 19.62 ? 176 TRP   A CB  1 
ATOM   1452 C CG  . TRP   A 1 174 ? 12.624  -16.422 -47.082 1.00 18.77 ? 176 TRP   A CG  1 
ATOM   1453 C CD1 . TRP   A 1 174 ? 12.967  -15.205 -47.593 1.00 18.15 ? 176 TRP   A CD1 1 
ATOM   1454 C CD2 . TRP   A 1 174 ? 11.380  -16.781 -47.693 1.00 17.78 ? 176 TRP   A CD2 1 
ATOM   1455 N NE1 . TRP   A 1 174 ? 12.022  -14.795 -48.505 1.00 16.98 ? 176 TRP   A NE1 1 
ATOM   1456 C CE2 . TRP   A 1 174 ? 11.042  -15.746 -48.590 1.00 17.54 ? 176 TRP   A CE2 1 
ATOM   1457 C CE3 . TRP   A 1 174 ? 10.537  -17.885 -47.585 1.00 17.80 ? 176 TRP   A CE3 1 
ATOM   1458 C CZ2 . TRP   A 1 174 ? 9.873   -15.770 -49.367 1.00 19.71 ? 176 TRP   A CZ2 1 
ATOM   1459 C CZ3 . TRP   A 1 174 ? 9.377   -17.911 -48.355 1.00 16.57 ? 176 TRP   A CZ3 1 
ATOM   1460 C CH2 . TRP   A 1 174 ? 9.058   -16.858 -49.238 1.00 20.09 ? 176 TRP   A CH2 1 
ATOM   1461 N N   . GLY   A 1 175 ? 13.964  -16.883 -42.405 1.00 17.97 ? 177 GLY   A N   1 
ATOM   1462 C CA  . GLY   A 1 175 ? 14.577  -17.597 -41.293 1.00 18.41 ? 177 GLY   A CA  1 
ATOM   1463 C C   . GLY   A 1 175 ? 13.630  -18.481 -40.502 1.00 20.68 ? 177 GLY   A C   1 
ATOM   1464 O O   . GLY   A 1 175 ? 14.088  -19.371 -39.773 1.00 23.66 ? 177 GLY   A O   1 
ATOM   1465 N N   . LEU   A 1 176 ? 12.325  -18.241 -40.600 1.00 18.59 ? 178 LEU   A N   1 
ATOM   1466 C CA  . LEU   A 1 176 ? 11.350  -19.113 -39.966 1.00 20.19 ? 178 LEU   A CA  1 
ATOM   1467 C C   . LEU   A 1 176 ? 10.638  -20.024 -40.961 1.00 20.01 ? 178 LEU   A C   1 
ATOM   1468 O O   . LEU   A 1 176 ? 9.821   -20.850 -40.546 1.00 21.65 ? 178 LEU   A O   1 
ATOM   1469 C CB  . LEU   A 1 176 ? 10.312  -18.274 -39.192 1.00 20.77 ? 178 LEU   A CB  1 
ATOM   1470 C CG  . LEU   A 1 176 ? 10.788  -17.544 -37.938 1.00 25.29 ? 178 LEU   A CG  1 
ATOM   1471 C CD1 . LEU   A 1 176 ? 9.613   -16.847 -37.258 1.00 25.70 ? 178 LEU   A CD1 1 
ATOM   1472 C CD2 . LEU   A 1 176 ? 11.442  -18.513 -36.994 1.00 30.20 ? 178 LEU   A CD2 1 
ATOM   1473 N N   . ALA   A 1 177 ? 10.944  -19.925 -42.251 1.00 17.27 ? 179 ALA   A N   1 
ATOM   1474 C CA  . ALA   A 1 177 ? 10.193  -20.690 -43.244 1.00 17.45 ? 179 ALA   A CA  1 
ATOM   1475 C C   . ALA   A 1 177 ? 10.450  -22.185 -43.094 1.00 18.92 ? 179 ALA   A C   1 
ATOM   1476 O O   . ALA   A 1 177 ? 11.499  -22.612 -42.602 1.00 19.36 ? 179 ALA   A O   1 
ATOM   1477 C CB  . ALA   A 1 177 ? 10.549  -20.221 -44.655 1.00 19.24 ? 179 ALA   A CB  1 
ATOM   1478 N N   . GLU   A 1 178 ? 9.463   -22.990 -43.492 1.00 17.04 ? 180 GLU   A N   1 
ATOM   1479 C CA  . GLU   A 1 178 ? 9.600   -24.443 -43.396 1.00 19.37 ? 180 GLU   A CA  1 
ATOM   1480 C C   . GLU   A 1 178 ? 9.017   -25.117 -44.624 1.00 16.63 ? 180 GLU   A C   1 
ATOM   1481 O O   . GLU   A 1 178 ? 8.159   -24.563 -45.321 1.00 18.97 ? 180 GLU   A O   1 
ATOM   1482 C CB  . GLU   A 1 178 ? 8.895   -25.021 -42.158 1.00 21.07 ? 180 GLU   A CB  1 
ATOM   1483 C CG  . GLU   A 1 178 ? 9.799   -25.538 -41.046 1.00 26.88 ? 180 GLU   A CG  1 
ATOM   1484 C CD  . GLU   A 1 178 ? 10.664  -26.753 -41.406 1.00 30.13 ? 180 GLU   A CD  1 
ATOM   1485 O OE1 . GLU   A 1 178 ? 11.243  -27.341 -40.471 1.00 34.93 ? 180 GLU   A OE1 1 
ATOM   1486 O OE2 . GLU   A 1 178 ? 10.798  -27.122 -42.592 1.00 29.45 ? 180 GLU   A OE2 1 
ATOM   1487 N N   . PHE   A 1 179 ? 9.470   -26.350 -44.864 1.00 18.61 ? 181 PHE   A N   1 
ATOM   1488 C CA  . PHE   A 1 179 ? 8.859   -27.205 -45.876 1.00 19.37 ? 181 PHE   A CA  1 
ATOM   1489 C C   . PHE   A 1 179 ? 7.569   -27.831 -45.351 1.00 21.08 ? 181 PHE   A C   1 
ATOM   1490 O O   . PHE   A 1 179 ? 7.538   -28.362 -44.234 1.00 22.48 ? 181 PHE   A O   1 
ATOM   1491 C CB  . PHE   A 1 179 ? 9.826   -28.318 -46.289 1.00 22.89 ? 181 PHE   A CB  1 
ATOM   1492 C CG  . PHE   A 1 179 ? 11.040  -27.829 -47.010 1.00 20.57 ? 181 PHE   A CG  1 
ATOM   1493 C CD1 . PHE   A 1 179 ? 12.158  -27.414 -46.306 1.00 22.56 ? 181 PHE   A CD1 1 
ATOM   1494 C CD2 . PHE   A 1 179 ? 11.056  -27.777 -48.393 1.00 24.02 ? 181 PHE   A CD2 1 
ATOM   1495 C CE1 . PHE   A 1 179 ? 13.284  -26.958 -46.973 1.00 22.11 ? 181 PHE   A CE1 1 
ATOM   1496 C CE2 . PHE   A 1 179 ? 12.176  -27.326 -49.076 1.00 22.05 ? 181 PHE   A CE2 1 
ATOM   1497 C CZ  . PHE   A 1 179 ? 13.293  -26.915 -48.366 1.00 20.85 ? 181 PHE   A CZ  1 
ATOM   1498 N N   . TYR   A 1 180 ? 6.506   -27.782 -46.158 1.00 18.95 ? 182 TYR   A N   1 
ATOM   1499 C CA  . TYR   A 1 180 ? 5.248   -28.414 -45.778 1.00 20.59 ? 182 TYR   A CA  1 
ATOM   1500 C C   . TYR   A 1 180 ? 5.258   -29.904 -46.135 1.00 22.41 ? 182 TYR   A C   1 
ATOM   1501 O O   . TYR   A 1 180 ? 5.444   -30.280 -47.299 1.00 23.07 ? 182 TYR   A O   1 
ATOM   1502 C CB  . TYR   A 1 180 ? 4.047   -27.734 -46.438 1.00 18.20 ? 182 TYR   A CB  1 
ATOM   1503 C CG  . TYR   A 1 180 ? 2.786   -28.499 -46.085 1.00 20.23 ? 182 TYR   A CG  1 
ATOM   1504 C CD1 . TYR   A 1 180 ? 2.278   -28.459 -44.789 1.00 20.67 ? 182 TYR   A CD1 1 
ATOM   1505 C CD2 . TYR   A 1 180 ? 2.169   -29.333 -47.008 1.00 19.74 ? 182 TYR   A CD2 1 
ATOM   1506 C CE1 . TYR   A 1 180 ? 1.150   -29.199 -44.440 1.00 20.35 ? 182 TYR   A CE1 1 
ATOM   1507 C CE2 . TYR   A 1 180 ? 1.048   -30.066 -46.667 1.00 21.49 ? 182 TYR   A CE2 1 
ATOM   1508 C CZ  . TYR   A 1 180 ? 0.545   -30.003 -45.383 1.00 19.46 ? 182 TYR   A CZ  1 
ATOM   1509 O OH  . TYR   A 1 180 ? -0.585  -30.743 -45.056 1.00 21.70 ? 182 TYR   A OH  1 
ATOM   1510 N N   . HIS   A 1 181 ? 5.004   -30.745 -45.138 1.00 19.61 ? 183 HIS   A N   1 
ATOM   1511 C CA  . HIS   A 1 181 ? 4.867   -32.180 -45.336 1.00 22.94 ? 183 HIS   A CA  1 
ATOM   1512 C C   . HIS   A 1 181 ? 3.556   -32.623 -44.705 1.00 22.44 ? 183 HIS   A C   1 
ATOM   1513 O O   . HIS   A 1 181 ? 3.317   -32.331 -43.517 1.00 24.21 ? 183 HIS   A O   1 
ATOM   1514 C CB  . HIS   A 1 181 ? 6.030   -32.936 -44.697 1.00 22.68 ? 183 HIS   A CB  1 
ATOM   1515 C CG  . HIS   A 1 181 ? 7.366   -32.651 -45.313 1.00 26.43 ? 183 HIS   A CG  1 
ATOM   1516 N ND1 . HIS   A 1 181 ? 7.813   -33.291 -46.452 1.00 26.52 ? 183 HIS   A ND1 1 
ATOM   1517 C CD2 . HIS   A 1 181 ? 8.369   -31.830 -44.923 1.00 26.56 ? 183 HIS   A CD2 1 
ATOM   1518 C CE1 . HIS   A 1 181 ? 9.030   -32.863 -46.742 1.00 27.36 ? 183 HIS   A CE1 1 
ATOM   1519 N NE2 . HIS   A 1 181 ? 9.390   -31.975 -45.832 1.00 25.84 ? 183 HIS   A NE2 1 
ATOM   1520 N N   . PRO   A 1 182 ? 2.697   -33.339 -45.431 1.00 21.90 ? 184 PRO   A N   1 
ATOM   1521 C CA  . PRO   A 1 182 ? 1.399   -33.732 -44.861 1.00 23.77 ? 184 PRO   A CA  1 
ATOM   1522 C C   . PRO   A 1 182 ? 1.577   -34.503 -43.561 1.00 24.69 ? 184 PRO   A C   1 
ATOM   1523 O O   . PRO   A 1 182 ? 2.378   -35.442 -43.475 1.00 26.18 ? 184 PRO   A O   1 
ATOM   1524 C CB  . PRO   A 1 182 ? 0.782   -34.612 -45.952 1.00 28.38 ? 184 PRO   A CB  1 
ATOM   1525 C CG  . PRO   A 1 182 ? 1.453   -34.201 -47.203 1.00 34.99 ? 184 PRO   A CG  1 
ATOM   1526 C CD  . PRO   A 1 182 ? 2.843   -33.769 -46.832 1.00 27.21 ? 184 PRO   A CD  1 
ATOM   1527 N N   . GLY   A 1 183 ? 0.836   -34.079 -42.536 1.00 26.42 ? 185 GLY   A N   1 
ATOM   1528 C CA  . GLY   A 1 183 ? 0.839   -34.760 -41.263 1.00 23.23 ? 185 GLY   A CA  1 
ATOM   1529 C C   . GLY   A 1 183 ? 1.936   -34.343 -40.314 1.00 25.53 ? 185 GLY   A C   1 
ATOM   1530 O O   . GLY   A 1 183 ? 1.945   -34.807 -39.166 1.00 27.09 ? 185 GLY   A O   1 
ATOM   1531 N N   . GLN   A 1 184 ? 2.855   -33.484 -40.743 1.00 24.86 ? 186 GLN   A N   1 
ATOM   1532 C CA  . GLN   A 1 184 ? 3.936   -33.053 -39.870 1.00 26.14 ? 186 GLN   A CA  1 
ATOM   1533 C C   . GLN   A 1 184 ? 3.410   -32.067 -38.839 1.00 26.15 ? 186 GLN   A C   1 
ATOM   1534 O O   . GLN   A 1 184 ? 2.581   -31.208 -39.151 1.00 24.28 ? 186 GLN   A O   1 
ATOM   1535 C CB  . GLN   A 1 184 ? 5.063   -32.418 -40.687 1.00 24.74 ? 186 GLN   A CB  1 
ATOM   1536 C CG  . GLN   A 1 184 ? 6.367   -32.232 -39.931 1.00 37.85 ? 186 GLN   A CG  1 
ATOM   1537 C CD  . GLN   A 1 184 ? 7.571   -32.176 -40.856 1.00 49.37 ? 186 GLN   A CD  1 
ATOM   1538 O OE1 . GLN   A 1 184 ? 8.415   -31.285 -40.746 1.00 57.16 ? 186 GLN   A OE1 1 
ATOM   1539 N NE2 . GLN   A 1 184 ? 7.657   -33.134 -41.774 1.00 46.28 ? 186 GLN   A NE2 1 
ATOM   1540 N N   . GLU   A 1 185 ? 3.883   -32.204 -37.604 1.00 24.62 ? 187 GLU   A N   1 
ATOM   1541 C CA  . GLU   A 1 185 ? 3.581   -31.257 -36.539 1.00 24.31 ? 187 GLU   A CA  1 
ATOM   1542 C C   . GLU   A 1 185 ? 4.710   -30.242 -36.439 1.00 24.85 ? 187 GLU   A C   1 
ATOM   1543 O O   . GLU   A 1 185 ? 5.887   -30.617 -36.384 1.00 28.73 ? 187 GLU   A O   1 
ATOM   1544 C CB  . GLU   A 1 185 ? 3.378   -31.980 -35.210 1.00 26.68 ? 187 GLU   A CB  1 
ATOM   1545 C CG  . GLU   A 1 185 ? 2.170   -32.908 -35.237 1.00 34.69 ? 187 GLU   A CG  1 
ATOM   1546 C CD  . GLU   A 1 185 ? 1.721   -33.341 -33.858 1.00 47.30 ? 187 GLU   A CD  1 
ATOM   1547 O OE1 . GLU   A 1 185 ? 2.573   -33.469 -32.957 1.00 54.94 ? 187 GLU   A OE1 1 
ATOM   1548 O OE2 . GLU   A 1 185 ? 0.505   -33.543 -33.675 1.00 54.38 ? 187 GLU   A OE2 1 
ATOM   1549 N N   . TYR   A 1 186 ? 4.351   -28.960 -36.441 1.00 23.85 ? 188 TYR   A N   1 
ATOM   1550 C CA  . TYR   A 1 186 ? 5.306   -27.863 -36.495 1.00 19.98 ? 188 TYR   A CA  1 
ATOM   1551 C C   . TYR   A 1 186 ? 5.318   -27.083 -35.186 1.00 25.48 ? 188 TYR   A C   1 
ATOM   1552 O O   . TYR   A 1 186 ? 4.374   -27.122 -34.397 1.00 24.05 ? 188 TYR   A O   1 
ATOM   1553 C CB  . TYR   A 1 186 ? 4.983   -26.914 -37.657 1.00 21.15 ? 188 TYR   A CB  1 
ATOM   1554 C CG  . TYR   A 1 186 ? 5.151   -27.571 -39.000 1.00 20.85 ? 188 TYR   A CG  1 
ATOM   1555 C CD1 . TYR   A 1 186 ? 6.411   -27.683 -39.572 1.00 20.94 ? 188 TYR   A CD1 1 
ATOM   1556 C CD2 . TYR   A 1 186 ? 4.066   -28.109 -39.682 1.00 21.14 ? 188 TYR   A CD2 1 
ATOM   1557 C CE1 . TYR   A 1 186 ? 6.588   -28.296 -40.791 1.00 22.51 ? 188 TYR   A CE1 1 
ATOM   1558 C CE2 . TYR   A 1 186 ? 4.239   -28.734 -40.918 1.00 18.63 ? 188 TYR   A CE2 1 
ATOM   1559 C CZ  . TYR   A 1 186 ? 5.506   -28.821 -41.454 1.00 23.48 ? 188 TYR   A CZ  1 
ATOM   1560 O OH  . TYR   A 1 186 ? 5.712   -29.428 -42.669 1.00 24.41 ? 188 TYR   A OH  1 
ATOM   1561 N N   . ASN   A 1 187 ? 6.423   -26.379 -34.966 1.00 21.46 ? 189 ASN   A N   1 
ATOM   1562 C CA  . ASN   A 1 187 ? 6.552   -25.490 -33.819 1.00 21.43 ? 189 ASN   A CA  1 
ATOM   1563 C C   . ASN   A 1 187 ? 5.545   -24.347 -33.945 1.00 21.69 ? 189 ASN   A C   1 
ATOM   1564 O O   . ASN   A 1 187 ? 5.433   -23.718 -35.000 1.00 21.19 ? 189 ASN   A O   1 
ATOM   1565 C CB  . ASN   A 1 187 ? 7.995   -24.970 -33.770 1.00 24.24 ? 189 ASN   A CB  1 
ATOM   1566 C CG  . ASN   A 1 187 ? 8.285   -24.062 -32.583 1.00 31.51 ? 189 ASN   A CG  1 
ATOM   1567 O OD1 . ASN   A 1 187 ? 7.472   -23.889 -31.683 1.00 26.59 ? 189 ASN   A OD1 1 
ATOM   1568 N ND2 . ASN   A 1 187 ? 9.487   -23.489 -32.577 1.00 43.94 ? 189 ASN   A ND2 1 
ATOM   1569 N N   . VAL   A 1 188 ? 4.797   -24.078 -32.870 1.00 20.90 ? 190 VAL   A N   1 
ATOM   1570 C CA  . VAL   A 1 188 ? 3.831   -22.978 -32.919 1.00 21.89 ? 190 VAL   A CA  1 
ATOM   1571 C C   . VAL   A 1 188 ? 4.443   -21.639 -32.526 1.00 20.99 ? 190 VAL   A C   1 
ATOM   1572 O O   . VAL   A 1 188 ? 3.766   -20.604 -32.641 1.00 24.64 ? 190 VAL   A O   1 
ATOM   1573 C CB  . VAL   A 1 188 ? 2.570   -23.231 -32.054 1.00 22.84 ? 190 VAL   A CB  1 
ATOM   1574 C CG1 . VAL   A 1 188 ? 1.804   -24.466 -32.531 1.00 23.74 ? 190 VAL   A CG1 1 
ATOM   1575 C CG2 . VAL   A 1 188 ? 2.907   -23.330 -30.570 1.00 24.03 ? 190 VAL   A CG2 1 
ATOM   1576 N N   . ARG   A 1 189 ? 5.707   -21.614 -32.086 1.00 21.86 ? 191 ARG   A N   1 
ATOM   1577 C CA  . ARG   A 1 189 ? 6.378   -20.363 -31.722 1.00 25.43 ? 191 ARG   A CA  1 
ATOM   1578 C C   . ARG   A 1 189 ? 7.018   -19.748 -32.967 1.00 26.73 ? 191 ARG   A C   1 
ATOM   1579 O O   . ARG   A 1 189 ? 8.240   -19.653 -33.114 1.00 26.94 ? 191 ARG   A O   1 
ATOM   1580 C CB  . ARG   A 1 189 ? 7.405   -20.606 -30.617 1.00 25.19 ? 191 ARG   A CB  1 
ATOM   1581 C CG  . ARG   A 1 189 ? 6.789   -21.147 -29.337 1.00 28.87 ? 191 ARG   A CG  1 
ATOM   1582 C CD  . ARG   A 1 189 ? 7.829   -21.240 -28.226 1.00 41.85 ? 191 ARG   A CD  1 
ATOM   1583 N NE  . ARG   A 1 189 ? 8.180   -19.924 -27.696 1.00 47.85 ? 191 ARG   A NE  1 
ATOM   1584 C CZ  . ARG   A 1 189 ? 9.234   -19.686 -26.922 1.00 57.09 ? 191 ARG   A CZ  1 
ATOM   1585 N NH1 . ARG   A 1 189 ? 10.054  -20.674 -26.593 1.00 58.22 ? 191 ARG   A NH1 1 
ATOM   1586 N NH2 . ARG   A 1 189 ? 9.473   -18.457 -26.486 1.00 58.87 ? 191 ARG   A NH2 1 
ATOM   1587 N N   . VAL   A 1 190 ? 6.147   -19.349 -33.889 1.00 22.22 ? 192 VAL   A N   1 
ATOM   1588 C CA  . VAL   A 1 190 ? 6.527   -18.659 -35.108 1.00 19.14 ? 192 VAL   A CA  1 
ATOM   1589 C C   . VAL   A 1 190 ? 5.612   -17.454 -35.276 1.00 21.08 ? 192 VAL   A C   1 
ATOM   1590 O O   . VAL   A 1 190 ? 4.608   -17.306 -34.579 1.00 22.14 ? 192 VAL   A O   1 
ATOM   1591 C CB  . VAL   A 1 190 ? 6.444   -19.565 -36.355 1.00 20.52 ? 192 VAL   A CB  1 
ATOM   1592 C CG1 . VAL   A 1 190 ? 7.397   -20.751 -36.214 1.00 21.20 ? 192 VAL   A CG1 1 
ATOM   1593 C CG2 . VAL   A 1 190 ? 4.999   -20.031 -36.587 1.00 22.39 ? 192 VAL   A CG2 1 
ATOM   1594 N N   . ALA   A 1 191 ? 5.974   -16.596 -36.235 1.00 23.24 ? 193 ALA   A N   1 
ATOM   1595 C CA  . ALA   A 1 191 ? 5.319   -15.322 -36.518 1.00 21.01 ? 193 ALA   A CA  1 
ATOM   1596 C C   . ALA   A 1 191 ? 5.392   -14.331 -35.357 1.00 22.03 ? 193 ALA   A C   1 
ATOM   1597 O O   . ALA   A 1 191 ? 5.606   -14.705 -34.197 1.00 24.53 ? 193 ALA   A O   1 
ATOM   1598 C CB  . ALA   A 1 191 ? 3.853   -15.541 -36.922 1.00 17.92 ? 193 ALA   A CB  1 
ATOM   1599 N N   . SER   A 1 192 ? 5.275   -13.048 -35.676 1.00 18.75 ? 194 SER   A N   1 
ATOM   1600 C CA  . SER   A 1 192 ? 5.153   -12.016 -34.658 1.00 18.92 ? 194 SER   A CA  1 
ATOM   1601 C C   . SER   A 1 192 ? 3.766   -12.060 -34.030 1.00 20.14 ? 194 SER   A C   1 
ATOM   1602 O O   . SER   A 1 192 ? 2.784   -12.401 -34.689 1.00 20.18 ? 194 SER   A O   1 
ATOM   1603 C CB  . SER   A 1 192 ? 5.387   -10.643 -35.278 1.00 24.45 ? 194 SER   A CB  1 
ATOM   1604 O OG  . SER   A 1 192 ? 4.717   -9.631  -34.546 1.00 37.30 ? 194 SER   A OG  1 
ATOM   1605 N N   . ARG   A 1 193 ? 3.686   -11.667 -32.750 1.00 19.61 ? 195 ARG   A N   1 
ATOM   1606 C CA  . ARG   A 1 193 ? 2.449   -11.830 -31.979 1.00 16.64 ? 195 ARG   A CA  1 
ATOM   1607 C C   . ARG   A 1 193 ? 1.214   -11.347 -32.738 1.00 21.24 ? 195 ARG   A C   1 
ATOM   1608 O O   . ARG   A 1 193 ? 0.202   -12.051 -32.798 1.00 19.86 ? 195 ARG   A O   1 
ATOM   1609 C CB  . ARG   A 1 193 ? 2.554   -11.089 -30.646 1.00 20.20 ? 195 ARG   A CB  1 
ATOM   1610 C CG  . ARG   A 1 193 ? 1.279   -11.160 -29.806 1.00 22.39 ? 195 ARG   A CG  1 
ATOM   1611 C CD  . ARG   A 1 193 ? 1.328   -10.192 -28.628 1.00 24.91 ? 195 ARG   A CD  1 
ATOM   1612 N NE  . ARG   A 1 193 ? 2.593   -10.278 -27.920 1.00 29.83 ? 195 ARG   A NE  1 
ATOM   1613 C CZ  . ARG   A 1 193 ? 3.200   -9.246  -27.349 1.00 35.06 ? 195 ARG   A CZ  1 
ATOM   1614 N NH1 . ARG   A 1 193 ? 2.655   -8.036  -27.395 1.00 32.37 ? 195 ARG   A NH1 1 
ATOM   1615 N NH2 . ARG   A 1 193 ? 4.361   -9.427  -26.734 1.00 36.69 ? 195 ARG   A NH2 1 
ATOM   1616 N N   . TYR   A 1 194 ? 1.274   -10.137 -33.312 1.00 19.52 ? 196 TYR   A N   1 
ATOM   1617 C CA  . TYR   A 1 194 ? 0.085   -9.534  -33.926 1.00 17.42 ? 196 TYR   A CA  1 
ATOM   1618 C C   . TYR   A 1 194 ? -0.347  -10.250 -35.193 1.00 19.34 ? 196 TYR   A C   1 
ATOM   1619 O O   . TYR   A 1 194 ? -1.472  -10.023 -35.671 1.00 18.62 ? 196 TYR   A O   1 
ATOM   1620 C CB  . TYR   A 1 194 ? 0.346   -8.062  -34.238 1.00 18.64 ? 196 TYR   A CB  1 
ATOM   1621 C CG  . TYR   A 1 194 ? 0.952   -7.309  -33.082 1.00 20.05 ? 196 TYR   A CG  1 
ATOM   1622 C CD1 . TYR   A 1 194 ? 0.402   -7.396  -31.815 1.00 22.07 ? 196 TYR   A CD1 1 
ATOM   1623 C CD2 . TYR   A 1 194 ? 2.094   -6.544  -33.255 1.00 27.61 ? 196 TYR   A CD2 1 
ATOM   1624 C CE1 . TYR   A 1 194 ? 0.959   -6.720  -30.743 1.00 25.65 ? 196 TYR   A CE1 1 
ATOM   1625 C CE2 . TYR   A 1 194 ? 2.663   -5.860  -32.181 1.00 32.27 ? 196 TYR   A CE2 1 
ATOM   1626 C CZ  . TYR   A 1 194 ? 2.084   -5.953  -30.935 1.00 29.77 ? 196 TYR   A CZ  1 
ATOM   1627 O OH  . TYR   A 1 194 ? 2.630   -5.286  -29.863 1.00 29.79 ? 196 TYR   A OH  1 
ATOM   1628 N N   . PHE   A 1 195 ? 0.508   -11.116 -35.734 1.00 16.50 ? 197 PHE   A N   1 
ATOM   1629 C CA  . PHE   A 1 195 ? 0.239   -11.798 -36.994 1.00 14.63 ? 197 PHE   A CA  1 
ATOM   1630 C C   . PHE   A 1 195 ? 0.081   -13.299 -36.809 1.00 17.89 ? 197 PHE   A C   1 
ATOM   1631 O O   . PHE   A 1 195 ? -0.069  -14.028 -37.798 1.00 19.49 ? 197 PHE   A O   1 
ATOM   1632 C CB  . PHE   A 1 195 ? 1.370   -11.453 -37.981 1.00 17.71 ? 197 PHE   A CB  1 
ATOM   1633 C CG  . PHE   A 1 195 ? 1.508   -9.975  -38.180 1.00 16.99 ? 197 PHE   A CG  1 
ATOM   1634 C CD1 . PHE   A 1 195 ? 0.710   -9.324  -39.118 1.00 17.10 ? 197 PHE   A CD1 1 
ATOM   1635 C CD2 . PHE   A 1 195 ? 2.339   -9.221  -37.360 1.00 19.70 ? 197 PHE   A CD2 1 
ATOM   1636 C CE1 . PHE   A 1 195 ? 0.788   -7.946  -39.260 1.00 19.37 ? 197 PHE   A CE1 1 
ATOM   1637 C CE2 . PHE   A 1 195 ? 2.430   -7.854  -37.508 1.00 18.83 ? 197 PHE   A CE2 1 
ATOM   1638 C CZ  . PHE   A 1 195 ? 1.643   -7.216  -38.444 1.00 20.22 ? 197 PHE   A CZ  1 
ATOM   1639 N N   . LYS   A 1 196 ? 0.088   -13.774 -35.563 1.00 15.94 ? 198 LYS   A N   1 
ATOM   1640 C CA  . LYS   A 1 196 ? -0.064  -15.198 -35.295 1.00 14.75 ? 198 LYS   A CA  1 
ATOM   1641 C C   . LYS   A 1 196 ? -1.484  -15.636 -35.601 1.00 16.55 ? 198 LYS   A C   1 
ATOM   1642 O O   . LYS   A 1 196 ? -2.440  -14.994 -35.155 1.00 17.88 ? 198 LYS   A O   1 
ATOM   1643 C CB  . LYS   A 1 196 ? 0.245   -15.495 -33.829 1.00 15.89 ? 198 LYS   A CB  1 
ATOM   1644 C CG  . LYS   A 1 196 ? 1.717   -15.391 -33.456 1.00 16.67 ? 198 LYS   A CG  1 
ATOM   1645 C CD  . LYS   A 1 196 ? 1.872   -15.548 -31.959 1.00 15.80 ? 198 LYS   A CD  1 
ATOM   1646 C CE  . LYS   A 1 196 ? 3.327   -15.343 -31.529 1.00 19.42 ? 198 LYS   A CE  1 
ATOM   1647 N NZ  . LYS   A 1 196 ? 4.155   -16.519 -31.923 1.00 22.91 ? 198 LYS   A NZ  1 
ATOM   1648 N N   . GLY   A 1 197 ? -1.617  -16.740 -36.341 1.00 18.42 ? 199 GLY   A N   1 
ATOM   1649 C CA  . GLY   A 1 197 ? -2.921  -17.305 -36.626 1.00 18.02 ? 199 GLY   A CA  1 
ATOM   1650 C C   . GLY   A 1 197 ? -3.515  -17.998 -35.413 1.00 17.48 ? 199 GLY   A C   1 
ATOM   1651 O O   . GLY   A 1 197 ? -2.806  -18.426 -34.494 1.00 17.82 ? 199 GLY   A O   1 
ATOM   1652 N N   . PRO   A 1 198 ? -4.845  -18.092 -35.380 1.00 15.54 ? 200 PRO   A N   1 
ATOM   1653 C CA  . PRO   A 1 198 ? -5.512  -18.823 -34.288 1.00 17.43 ? 200 PRO   A CA  1 
ATOM   1654 C C   . PRO   A 1 198 ? -4.948  -20.211 -34.063 1.00 18.97 ? 200 PRO   A C   1 
ATOM   1655 O O   . PRO   A 1 198 ? -4.894  -20.664 -32.908 1.00 18.75 ? 200 PRO   A O   1 
ATOM   1656 C CB  . PRO   A 1 198 ? -6.980  -18.874 -34.750 1.00 20.01 ? 200 PRO   A CB  1 
ATOM   1657 C CG  . PRO   A 1 198 ? -7.132  -17.673 -35.631 1.00 21.69 ? 200 PRO   A CG  1 
ATOM   1658 C CD  . PRO   A 1 198 ? -5.800  -17.479 -36.317 1.00 19.06 ? 200 PRO   A CD  1 
ATOM   1659 N N   . GLU   A 1 199 ? -4.510  -20.901 -35.120 1.00 18.32 ? 201 GLU   A N   1 
ATOM   1660 C CA  . GLU   A 1 199 ? -3.968  -22.245 -34.934 1.00 16.93 ? 201 GLU   A CA  1 
ATOM   1661 C C   . GLU   A 1 199 ? -2.761  -22.224 -34.004 1.00 17.18 ? 201 GLU   A C   1 
ATOM   1662 O O   . GLU   A 1 199 ? -2.597  -23.122 -33.165 1.00 18.55 ? 201 GLU   A O   1 
ATOM   1663 C CB  . GLU   A 1 199 ? -3.600  -22.877 -36.287 1.00 20.76 ? 201 GLU   A CB  1 
ATOM   1664 C CG  . GLU   A 1 199 ? -2.618  -22.084 -37.175 1.00 21.63 ? 201 GLU   A CG  1 
ATOM   1665 C CD  . GLU   A 1 199 ? -3.323  -21.146 -38.153 1.00 21.55 ? 201 GLU   A CD  1 
ATOM   1666 O OE1 . GLU   A 1 199 ? -4.136  -20.321 -37.694 1.00 21.62 ? 201 GLU   A OE1 1 
ATOM   1667 O OE2 . GLU   A 1 199 ? -3.065  -21.229 -39.378 1.00 19.97 ? 201 GLU   A OE2 1 
ATOM   1668 N N   . LEU   A 1 200 ? -1.911  -21.197 -34.127 1.00 15.88 ? 202 LEU   A N   1 
ATOM   1669 C CA  . LEU   A 1 200 ? -0.772  -21.072 -33.221 1.00 17.21 ? 202 LEU   A CA  1 
ATOM   1670 C C   . LEU   A 1 200 ? -1.238  -20.753 -31.810 1.00 19.73 ? 202 LEU   A C   1 
ATOM   1671 O O   . LEU   A 1 200 ? -0.713  -21.301 -30.832 1.00 20.12 ? 202 LEU   A O   1 
ATOM   1672 C CB  . LEU   A 1 200 ? 0.175   -19.981 -33.714 1.00 16.50 ? 202 LEU   A CB  1 
ATOM   1673 C CG  . LEU   A 1 200 ? 0.569   -20.037 -35.187 1.00 18.48 ? 202 LEU   A CG  1 
ATOM   1674 C CD1 . LEU   A 1 200 ? 1.578   -18.939 -35.478 1.00 18.60 ? 202 LEU   A CD1 1 
ATOM   1675 C CD2 . LEU   A 1 200 ? 1.136   -21.408 -35.530 1.00 18.54 ? 202 LEU   A CD2 1 
ATOM   1676 N N   . LEU   A 1 201 ? -2.243  -19.884 -31.693 1.00 17.12 ? 203 LEU   A N   1 
ATOM   1677 C CA  . LEU   A 1 201 ? -2.685  -19.409 -30.392 1.00 16.98 ? 203 LEU   A CA  1 
ATOM   1678 C C   . LEU   A 1 201 ? -3.464  -20.462 -29.614 1.00 19.76 ? 203 LEU   A C   1 
ATOM   1679 O O   . LEU   A 1 201 ? -3.590  -20.335 -28.393 1.00 22.50 ? 203 LEU   A O   1 
ATOM   1680 C CB  . LEU   A 1 201 ? -3.525  -18.142 -30.574 1.00 17.37 ? 203 LEU   A CB  1 
ATOM   1681 C CG  . LEU   A 1 201 ? -2.781  -16.992 -31.262 1.00 19.07 ? 203 LEU   A CG  1 
ATOM   1682 C CD1 . LEU   A 1 201 ? -3.734  -15.862 -31.622 1.00 19.37 ? 203 LEU   A CD1 1 
ATOM   1683 C CD2 . LEU   A 1 201 ? -1.617  -16.479 -30.397 1.00 20.27 ? 203 LEU   A CD2 1 
ATOM   1684 N N   . VAL   A 1 202 ? -3.979  -21.500 -30.272 1.00 22.11 ? 204 VAL   A N   1 
ATOM   1685 C CA  . VAL   A 1 202 ? -4.614  -22.610 -29.568 1.00 22.46 ? 204 VAL   A CA  1 
ATOM   1686 C C   . VAL   A 1 202 ? -3.729  -23.853 -29.550 1.00 22.97 ? 204 VAL   A C   1 
ATOM   1687 O O   . VAL   A 1 202 ? -4.187  -24.924 -29.140 1.00 24.40 ? 204 VAL   A O   1 
ATOM   1688 C CB  . VAL   A 1 202 ? -6.007  -22.937 -30.145 1.00 21.75 ? 204 VAL   A CB  1 
ATOM   1689 C CG1 . VAL   A 1 202 ? -6.928  -21.729 -30.067 1.00 23.71 ? 204 VAL   A CG1 1 
ATOM   1690 C CG2 . VAL   A 1 202 ? -5.903  -23.446 -31.586 1.00 22.11 ? 204 VAL   A CG2 1 
ATOM   1691 N N   . ASP   A 1 203 ? -2.476  -23.739 -30.010 1.00 21.02 ? 205 ASP   A N   1 
ATOM   1692 C CA  . ASP   A 1 203 ? -1.472  -24.807 -29.933 1.00 20.33 ? 205 ASP   A CA  1 
ATOM   1693 C C   . ASP   A 1 203 ? -1.819  -25.992 -30.841 1.00 23.08 ? 205 ASP   A C   1 
ATOM   1694 O O   . ASP   A 1 203 ? -1.591  -27.155 -30.487 1.00 26.89 ? 205 ASP   A O   1 
ATOM   1695 C CB  . ASP   A 1 203 ? -1.269  -25.267 -28.482 1.00 23.24 ? 205 ASP   A CB  1 
ATOM   1696 C CG  . ASP   A 1 203 ? 0.086   -25.921 -28.258 1.00 43.01 ? 205 ASP   A CG  1 
ATOM   1697 O OD1 . ASP   A 1 203 ? 0.935   -25.873 -29.173 1.00 44.24 ? 205 ASP   A OD1 1 
ATOM   1698 O OD2 . ASP   A 1 203 ? 0.298   -26.486 -27.163 1.00 55.94 ? 205 ASP   A OD2 1 
ATOM   1699 N N   . TYR   A 1 204 ? -2.350  -25.702 -32.029 1.00 20.45 ? 206 TYR   A N   1 
ATOM   1700 C CA  . TYR   A 1 204 ? -2.612  -26.731 -33.034 1.00 19.63 ? 206 TYR   A CA  1 
ATOM   1701 C C   . TYR   A 1 204 ? -1.403  -26.804 -33.966 1.00 20.23 ? 206 TYR   A C   1 
ATOM   1702 O O   . TYR   A 1 204 ? -1.140  -25.866 -34.723 1.00 20.82 ? 206 TYR   A O   1 
ATOM   1703 C CB  . TYR   A 1 204 ? -3.896  -26.435 -33.811 1.00 18.55 ? 206 TYR   A CB  1 
ATOM   1704 C CG  . TYR   A 1 204 ? -4.240  -27.571 -34.727 1.00 20.19 ? 206 TYR   A CG  1 
ATOM   1705 C CD1 . TYR   A 1 204 ? -4.798  -28.741 -34.225 1.00 23.11 ? 206 TYR   A CD1 1 
ATOM   1706 C CD2 . TYR   A 1 204 ? -3.982  -27.492 -36.091 1.00 20.29 ? 206 TYR   A CD2 1 
ATOM   1707 C CE1 . TYR   A 1 204 ? -5.104  -29.801 -35.066 1.00 22.77 ? 206 TYR   A CE1 1 
ATOM   1708 C CE2 . TYR   A 1 204 ? -4.267  -28.549 -36.933 1.00 20.68 ? 206 TYR   A CE2 1 
ATOM   1709 C CZ  . TYR   A 1 204 ? -4.830  -29.697 -36.414 1.00 22.44 ? 206 TYR   A CZ  1 
ATOM   1710 O OH  . TYR   A 1 204 ? -5.119  -30.752 -37.250 1.00 23.24 ? 206 TYR   A OH  1 
ATOM   1711 N N   . GLN   A 1 205 ? -0.664  -27.920 -33.914 1.00 19.53 ? 207 GLN   A N   1 
ATOM   1712 C CA  . GLN   A 1 205 ? 0.644   -27.980 -34.564 1.00 19.17 ? 207 GLN   A CA  1 
ATOM   1713 C C   . GLN   A 1 205 ? 0.609   -28.445 -36.013 1.00 20.70 ? 207 GLN   A C   1 
ATOM   1714 O O   . GLN   A 1 205 ? 1.603   -28.261 -36.726 1.00 20.76 ? 207 GLN   A O   1 
ATOM   1715 C CB  . GLN   A 1 205 ? 1.587   -28.903 -33.779 1.00 22.61 ? 207 GLN   A CB  1 
ATOM   1716 C CG  . GLN   A 1 205 ? 1.903   -28.386 -32.397 1.00 22.85 ? 207 GLN   A CG  1 
ATOM   1717 C CD  . GLN   A 1 205 ? 2.904   -29.258 -31.670 1.00 29.85 ? 207 GLN   A CD  1 
ATOM   1718 O OE1 . GLN   A 1 205 ? 2.536   -30.046 -30.803 1.00 34.06 ? 207 GLN   A OE1 1 
ATOM   1719 N NE2 . GLN   A 1 205 ? 4.180   -29.121 -32.027 1.00 28.43 ? 207 GLN   A NE2 1 
ATOM   1720 N N   . MET   A 1 206 ? -0.477  -29.058 -36.469 1.00 19.68 ? 208 MET   A N   1 
ATOM   1721 C CA  . MET   A 1 206 ? -0.497  -29.641 -37.811 1.00 17.41 ? 208 MET   A CA  1 
ATOM   1722 C C   . MET   A 1 206 ? -1.075  -28.633 -38.807 1.00 18.79 ? 208 MET   A C   1 
ATOM   1723 O O   . MET   A 1 206 ? -2.087  -28.870 -39.479 1.00 20.97 ? 208 MET   A O   1 
ATOM   1724 C CB  . MET   A 1 206 ? -1.278  -30.952 -37.802 1.00 22.19 ? 208 MET   A CB  1 
ATOM   1725 C CG  . MET   A 1 206 ? -1.037  -31.832 -39.030 1.00 26.53 ? 208 MET   A CG  1 
ATOM   1726 S SD  . MET   A 1 206 ? -1.863  -33.443 -38.955 1.00 24.72 ? 208 MET   A SD  1 
ATOM   1727 C CE  . MET   A 1 206 ? -1.180  -34.104 -37.440 1.00 29.36 ? 208 MET   A CE  1 
ATOM   1728 N N   . TYR   A 1 207 ? -0.414  -27.473 -38.879 1.00 19.10 ? 209 TYR   A N   1 
ATOM   1729 C CA  . TYR   A 1 207 ? -0.878  -26.365 -39.704 1.00 16.43 ? 209 TYR   A CA  1 
ATOM   1730 C C   . TYR   A 1 207 ? -0.140  -26.354 -41.052 1.00 19.06 ? 209 TYR   A C   1 
ATOM   1731 O O   . TYR   A 1 207 ? 0.635   -27.260 -41.368 1.00 20.65 ? 209 TYR   A O   1 
ATOM   1732 C CB  . TYR   A 1 207 ? -0.740  -25.043 -38.939 1.00 16.19 ? 209 TYR   A CB  1 
ATOM   1733 C CG  . TYR   A 1 207 ? 0.676   -24.657 -38.534 1.00 17.80 ? 209 TYR   A CG  1 
ATOM   1734 C CD1 . TYR   A 1 207 ? 1.544   -24.091 -39.471 1.00 17.57 ? 209 TYR   A CD1 1 
ATOM   1735 C CD2 . TYR   A 1 207 ? 1.131   -24.818 -37.222 1.00 17.66 ? 209 TYR   A CD2 1 
ATOM   1736 C CE1 . TYR   A 1 207 ? 2.846   -23.722 -39.124 1.00 18.16 ? 209 TYR   A CE1 1 
ATOM   1737 C CE2 . TYR   A 1 207 ? 2.440   -24.445 -36.861 1.00 17.36 ? 209 TYR   A CE2 1 
ATOM   1738 C CZ  . TYR   A 1 207 ? 3.282   -23.897 -37.819 1.00 17.97 ? 209 TYR   A CZ  1 
ATOM   1739 O OH  . TYR   A 1 207 ? 4.558   -23.518 -37.474 1.00 19.02 ? 209 TYR   A OH  1 
ATOM   1740 N N   . ASP   A 1 208 ? -0.409  -25.342 -41.877 1.00 17.76 ? 210 ASP   A N   1 
ATOM   1741 C CA  . ASP   A 1 208 ? 0.104   -25.391 -43.248 1.00 17.28 ? 210 ASP   A CA  1 
ATOM   1742 C C   . ASP   A 1 208 ? 0.228   -23.977 -43.813 1.00 16.29 ? 210 ASP   A C   1 
ATOM   1743 O O   . ASP   A 1 208 ? 0.270   -22.994 -43.057 1.00 16.73 ? 210 ASP   A O   1 
ATOM   1744 C CB  . ASP   A 1 208 ? -0.771  -26.312 -44.119 1.00 20.67 ? 210 ASP   A CB  1 
ATOM   1745 C CG  . ASP   A 1 208 ? -2.229  -25.884 -44.158 1.00 21.05 ? 210 ASP   A CG  1 
ATOM   1746 O OD1 . ASP   A 1 208 ? -3.094  -26.577 -43.557 1.00 23.36 ? 210 ASP   A OD1 1 
ATOM   1747 O OD2 . ASP   A 1 208 ? -2.519  -24.845 -44.788 1.00 23.48 ? 210 ASP   A OD2 1 
ATOM   1748 N N   . TYR   A 1 209 ? 0.317   -23.883 -45.146 1.00 16.46 ? 211 TYR   A N   1 
ATOM   1749 C CA  . TYR   A 1 209 ? 0.483   -22.607 -45.835 1.00 15.95 ? 211 TYR   A CA  1 
ATOM   1750 C C   . TYR   A 1 209 ? -0.557  -21.582 -45.430 1.00 15.08 ? 211 TYR   A C   1 
ATOM   1751 O O   . TYR   A 1 209 ? -0.312  -20.370 -45.537 1.00 16.28 ? 211 TYR   A O   1 
ATOM   1752 C CB  . TYR   A 1 209 ? 0.362   -22.792 -47.350 1.00 16.48 ? 211 TYR   A CB  1 
ATOM   1753 C CG  . TYR   A 1 209 ? 1.081   -23.970 -47.960 1.00 17.00 ? 211 TYR   A CG  1 
ATOM   1754 C CD1 . TYR   A 1 209 ? 0.364   -25.073 -48.408 1.00 17.51 ? 211 TYR   A CD1 1 
ATOM   1755 C CD2 . TYR   A 1 209 ? 2.467   -23.973 -48.110 1.00 16.77 ? 211 TYR   A CD2 1 
ATOM   1756 C CE1 . TYR   A 1 209 ? 1.003   -26.163 -48.990 1.00 18.37 ? 211 TYR   A CE1 1 
ATOM   1757 C CE2 . TYR   A 1 209 ? 3.115   -25.050 -48.691 1.00 18.04 ? 211 TYR   A CE2 1 
ATOM   1758 C CZ  . TYR   A 1 209 ? 2.383   -26.137 -49.137 1.00 19.60 ? 211 TYR   A CZ  1 
ATOM   1759 O OH  . TYR   A 1 209 ? 3.021   -27.210 -49.720 1.00 19.07 ? 211 TYR   A OH  1 
ATOM   1760 N N   . SER   A 1 210 ? -1.747  -22.039 -45.023 1.00 16.19 ? 212 SER   A N   1 
ATOM   1761 C CA  . SER   A 1 210 ? -2.830  -21.108 -44.729 1.00 16.08 ? 212 SER   A CA  1 
ATOM   1762 C C   . SER   A 1 210 ? -2.509  -20.188 -43.545 1.00 15.10 ? 212 SER   A C   1 
ATOM   1763 O O   . SER   A 1 210 ? -3.137  -19.133 -43.405 1.00 16.39 ? 212 SER   A O   1 
ATOM   1764 C CB  . SER   A 1 210 ? -4.113  -21.906 -44.498 1.00 16.86 ? 212 SER   A CB  1 
ATOM   1765 O OG  . SER   A 1 210 ? -3.908  -22.915 -43.515 1.00 17.81 ? 212 SER   A OG  1 
ATOM   1766 N N   . LEU   A 1 211 ? -1.524  -20.541 -42.707 1.00 14.92 ? 213 LEU   A N   1 
ATOM   1767 C CA  . LEU   A 1 211 ? -1.044  -19.601 -41.692 1.00 15.07 ? 213 LEU   A CA  1 
ATOM   1768 C C   . LEU   A 1 211 ? -0.642  -18.263 -42.308 1.00 17.00 ? 213 LEU   A C   1 
ATOM   1769 O O   . LEU   A 1 211 ? -0.969  -17.195 -41.770 1.00 16.05 ? 213 LEU   A O   1 
ATOM   1770 C CB  . LEU   A 1 211 ? 0.149   -20.203 -40.937 1.00 18.96 ? 213 LEU   A CB  1 
ATOM   1771 C CG  . LEU   A 1 211 ? 0.893   -19.221 -40.036 1.00 18.32 ? 213 LEU   A CG  1 
ATOM   1772 C CD1 . LEU   A 1 211 ? 0.006   -18.727 -38.885 1.00 18.99 ? 213 LEU   A CD1 1 
ATOM   1773 C CD2 . LEU   A 1 211 ? 2.178   -19.867 -39.510 1.00 17.62 ? 213 LEU   A CD2 1 
ATOM   1774 N N   . ASP   A 1 212 ? 0.067   -18.301 -43.445 1.00 16.78 ? 214 ASP   A N   1 
ATOM   1775 C CA  . ASP   A 1 212 ? 0.526   -17.069 -44.084 1.00 17.32 ? 214 ASP   A CA  1 
ATOM   1776 C C   . ASP   A 1 212 ? -0.647  -16.207 -44.525 1.00 16.11 ? 214 ASP   A C   1 
ATOM   1777 O O   . ASP   A 1 212 ? -0.533  -14.972 -44.595 1.00 16.30 ? 214 ASP   A O   1 
ATOM   1778 C CB  . ASP   A 1 212 ? 1.405   -17.387 -45.300 1.00 16.15 ? 214 ASP   A CB  1 
ATOM   1779 C CG  . ASP   A 1 212 ? 2.743   -18.016 -44.929 1.00 17.99 ? 214 ASP   A CG  1 
ATOM   1780 O OD1 . ASP   A 1 212 ? 3.218   -17.845 -43.773 1.00 17.44 ? 214 ASP   A OD1 1 
ATOM   1781 O OD2 . ASP   A 1 212 ? 3.322   -18.690 -45.814 1.00 17.43 ? 214 ASP   A OD2 1 
ATOM   1782 N N   . MET   A 1 213 ? -1.777  -16.837 -44.833 1.00 16.44 ? 215 MET   A N   1 
ATOM   1783 C CA  . MET   A 1 213 ? -2.935  -16.085 -45.291 1.00 15.62 ? 215 MET   A CA  1 
ATOM   1784 C C   . MET   A 1 213 ? -3.611  -15.348 -44.143 1.00 14.78 ? 215 MET   A C   1 
ATOM   1785 O O   . MET   A 1 213 ? -4.128  -14.235 -44.348 1.00 16.35 ? 215 MET   A O   1 
ATOM   1786 C CB  . MET   A 1 213 ? -3.912  -17.024 -46.011 1.00 18.44 ? 215 MET   A CB  1 
ATOM   1787 C CG  . MET   A 1 213 ? -3.289  -17.782 -47.183 1.00 18.72 ? 215 MET   A CG  1 
ATOM   1788 S SD  . MET   A 1 213 ? -2.457  -16.740 -48.413 1.00 20.55 ? 215 MET   A SD  1 
ATOM   1789 C CE  . MET   A 1 213 ? -3.854  -15.830 -49.068 1.00 21.28 ? 215 MET   A CE  1 
ATOM   1790 N N   . TRP   A 1 214 ? -3.607  -15.929 -42.935 1.00 15.70 ? 216 TRP   A N   1 
ATOM   1791 C CA  . TRP   A 1 214 ? -4.059  -15.170 -41.773 1.00 15.21 ? 216 TRP   A CA  1 
ATOM   1792 C C   . TRP   A 1 214 ? -3.171  -13.954 -41.553 1.00 15.42 ? 216 TRP   A C   1 
ATOM   1793 O O   . TRP   A 1 214 ? -3.659  -12.833 -41.386 1.00 17.21 ? 216 TRP   A O   1 
ATOM   1794 C CB  . TRP   A 1 214 ? -4.071  -16.030 -40.508 1.00 15.17 ? 216 TRP   A CB  1 
ATOM   1795 C CG  . TRP   A 1 214 ? -4.453  -15.198 -39.297 1.00 16.05 ? 216 TRP   A CG  1 
ATOM   1796 C CD1 . TRP   A 1 214 ? -3.614  -14.481 -38.482 1.00 15.97 ? 216 TRP   A CD1 1 
ATOM   1797 C CD2 . TRP   A 1 214 ? -5.778  -14.980 -38.798 1.00 16.16 ? 216 TRP   A CD2 1 
ATOM   1798 N NE1 . TRP   A 1 214 ? -4.339  -13.835 -37.512 1.00 16.21 ? 216 TRP   A NE1 1 
ATOM   1799 C CE2 . TRP   A 1 214 ? -5.671  -14.125 -37.682 1.00 16.38 ? 216 TRP   A CE2 1 
ATOM   1800 C CE3 . TRP   A 1 214 ? -7.040  -15.438 -39.182 1.00 17.45 ? 216 TRP   A CE3 1 
ATOM   1801 C CZ2 . TRP   A 1 214 ? -6.784  -13.715 -36.942 1.00 17.20 ? 216 TRP   A CZ2 1 
ATOM   1802 C CZ3 . TRP   A 1 214 ? -8.154  -15.025 -38.447 1.00 15.42 ? 216 TRP   A CZ3 1 
ATOM   1803 C CH2 . TRP   A 1 214 ? -8.019  -14.170 -37.348 1.00 19.34 ? 216 TRP   A CH2 1 
ATOM   1804 N N   . SER   A 1 215 ? -1.851  -14.165 -41.534 1.00 14.48 ? 217 SER   A N   1 
ATOM   1805 C CA  . SER   A 1 215 ? -0.938  -13.044 -41.339 1.00 13.95 ? 217 SER   A CA  1 
ATOM   1806 C C   . SER   A 1 215 ? -1.169  -11.953 -42.385 1.00 16.78 ? 217 SER   A C   1 
ATOM   1807 O O   . SER   A 1 215 ? -1.170  -10.759 -42.056 1.00 16.62 ? 217 SER   A O   1 
ATOM   1808 C CB  . SER   A 1 215 ? 0.505   -13.553 -41.379 1.00 17.03 ? 217 SER   A CB  1 
ATOM   1809 O OG  . SER   A 1 215 ? 0.707   -14.593 -40.423 1.00 17.93 ? 217 SER   A OG  1 
ATOM   1810 N N   . LEU   A 1 216 ? -1.361  -12.342 -43.652 1.00 17.41 ? 218 LEU   A N   1 
ATOM   1811 C CA  . LEU   A 1 216 ? -1.621  -11.352 -44.698 1.00 17.58 ? 218 LEU   A CA  1 
ATOM   1812 C C   . LEU   A 1 216 ? -2.912  -10.590 -44.426 1.00 15.70 ? 218 LEU   A C   1 
ATOM   1813 O O   . LEU   A 1 216 ? -2.982  -9.368  -44.638 1.00 18.67 ? 218 LEU   A O   1 
ATOM   1814 C CB  . LEU   A 1 216 ? -1.680  -12.031 -46.069 1.00 19.50 ? 218 LEU   A CB  1 
ATOM   1815 C CG  . LEU   A 1 216 ? -1.878  -11.072 -47.247 1.00 20.78 ? 218 LEU   A CG  1 
ATOM   1816 C CD1 . LEU   A 1 216 ? -0.582  -10.340 -47.533 1.00 21.69 ? 218 LEU   A CD1 1 
ATOM   1817 C CD2 . LEU   A 1 216 ? -2.356  -11.841 -48.482 1.00 26.38 ? 218 LEU   A CD2 1 
ATOM   1818 N N   . GLY   A 1 217 ? -3.942  -11.291 -43.952 1.00 16.43 ? 219 GLY   A N   1 
ATOM   1819 C CA  . GLY   A 1 217 ? -5.181  -10.615 -43.592 1.00 16.61 ? 219 GLY   A CA  1 
ATOM   1820 C C   . GLY   A 1 217 ? -4.990  -9.590  -42.487 1.00 18.69 ? 219 GLY   A C   1 
ATOM   1821 O O   . GLY   A 1 217 ? -5.589  -8.513  -42.516 1.00 19.85 ? 219 GLY   A O   1 
ATOM   1822 N N   . CYS   A 1 218 ? -4.158  -9.914  -41.487 1.00 16.87 ? 220 CYS   A N   1 
ATOM   1823 C CA  . CYS   A 1 218 ? -3.841  -8.930  -40.455 1.00 16.73 ? 220 CYS   A CA  1 
ATOM   1824 C C   . CYS   A 1 218 ? -3.178  -7.693  -41.047 1.00 21.98 ? 220 CYS   A C   1 
ATOM   1825 O O   . CYS   A 1 218 ? -3.480  -6.565  -40.642 1.00 19.89 ? 220 CYS   A O   1 
ATOM   1826 C CB  . CYS   A 1 218 ? -2.927  -9.540  -39.394 1.00 15.67 ? 220 CYS   A CB  1 
ATOM   1827 S SG  . CYS   A 1 218 ? -3.687  -10.857 -38.434 1.00 17.97 ? 220 CYS   A SG  1 
ATOM   1828 N N   . MET   A 1 219 ? -2.253  -7.886  -41.992 1.00 17.73 ? 221 MET   A N   1 
ATOM   1829 C CA  . MET   A 1 219 ? -1.636  -6.743  -42.664 1.00 19.79 ? 221 MET   A CA  1 
ATOM   1830 C C   . MET   A 1 219 ? -2.677  -5.920  -43.413 1.00 20.35 ? 221 MET   A C   1 
ATOM   1831 O O   . MET   A 1 219 ? -2.713  -4.690  -43.293 1.00 21.45 ? 221 MET   A O   1 
ATOM   1832 C CB  . MET   A 1 219 ? -0.539  -7.229  -43.619 1.00 21.98 ? 221 MET   A CB  1 
ATOM   1833 C CG  . MET   A 1 219 ? 0.639   -7.850  -42.918 1.00 26.69 ? 221 MET   A CG  1 
ATOM   1834 S SD  . MET   A 1 219 ? 1.966   -8.178  -44.105 1.00 27.30 ? 221 MET   A SD  1 
ATOM   1835 C CE  . MET   A 1 219 ? 1.964   -6.663  -45.014 1.00 20.01 ? 221 MET   A CE  1 
ATOM   1836 N N   . LEU   A 1 220 ? -3.530  -6.585  -44.193 1.00 19.07 ? 222 LEU   A N   1 
ATOM   1837 C CA  . LEU   A 1 220 ? -4.558  -5.879  -44.956 1.00 20.40 ? 222 LEU   A CA  1 
ATOM   1838 C C   . LEU   A 1 220 ? -5.459  -5.064  -44.035 1.00 20.08 ? 222 LEU   A C   1 
ATOM   1839 O O   . LEU   A 1 220 ? -5.722  -3.883  -44.291 1.00 21.63 ? 222 LEU   A O   1 
ATOM   1840 C CB  . LEU   A 1 220 ? -5.380  -6.877  -45.773 1.00 20.79 ? 222 LEU   A CB  1 
ATOM   1841 C CG  . LEU   A 1 220 ? -6.538  -6.322  -46.600 1.00 20.39 ? 222 LEU   A CG  1 
ATOM   1842 C CD1 . LEU   A 1 220 ? -5.991  -5.484  -47.743 1.00 22.21 ? 222 LEU   A CD1 1 
ATOM   1843 C CD2 . LEU   A 1 220 ? -7.392  -7.462  -47.131 1.00 22.59 ? 222 LEU   A CD2 1 
ATOM   1844 N N   . ALA   A 1 221 ? -5.917  -5.674  -42.938 1.00 17.66 ? 223 ALA   A N   1 
ATOM   1845 C CA  . ALA   A 1 221 ? -6.786  -4.968  -42.004 1.00 17.88 ? 223 ALA   A CA  1 
ATOM   1846 C C   . ALA   A 1 221 ? -6.115  -3.709  -41.477 1.00 21.03 ? 223 ALA   A C   1 
ATOM   1847 O O   . ALA   A 1 221 ? -6.739  -2.643  -41.406 1.00 19.52 ? 223 ALA   A O   1 
ATOM   1848 C CB  . ALA   A 1 221 ? -7.175  -5.886  -40.842 1.00 18.24 ? 223 ALA   A CB  1 
ATOM   1849 N N   . SER   A 1 222 ? -4.834  -3.804  -41.110 1.00 20.28 ? 224 SER   A N   1 
ATOM   1850 C CA  A SER   A 1 222 ? -4.141  -2.633  -40.583 0.77 23.32 ? 224 SER   A CA  1 
ATOM   1851 C CA  B SER   A 1 222 ? -4.143  -2.633  -40.584 0.23 22.61 ? 224 SER   A CA  1 
ATOM   1852 C C   . SER   A 1 222 ? -4.039  -1.526  -41.622 1.00 23.15 ? 224 SER   A C   1 
ATOM   1853 O O   . SER   A 1 222 ? -4.101  -0.341  -41.272 1.00 26.70 ? 224 SER   A O   1 
ATOM   1854 C CB  A SER   A 1 222 ? -2.742  -3.019  -40.082 0.77 21.73 ? 224 SER   A CB  1 
ATOM   1855 C CB  B SER   A 1 222 ? -2.751  -3.019  -40.082 0.23 22.73 ? 224 SER   A CB  1 
ATOM   1856 O OG  A SER   A 1 222 ? -1.834  -3.303  -41.147 0.77 22.48 ? 224 SER   A OG  1 
ATOM   1857 O OG  B SER   A 1 222 ? -2.827  -3.691  -38.839 0.23 26.05 ? 224 SER   A OG  1 
ATOM   1858 N N   . MET   A 1 223 ? -3.898  -1.888  -42.898 1.00 21.04 ? 225 MET   A N   1 
ATOM   1859 C CA  . MET   A 1 223 ? -3.733  -0.884  -43.946 1.00 24.25 ? 225 MET   A CA  1 
ATOM   1860 C C   . MET   A 1 223 ? -5.057  -0.233  -44.333 1.00 24.43 ? 225 MET   A C   1 
ATOM   1861 O O   . MET   A 1 223 ? -5.136  0.997   -44.425 1.00 26.53 ? 225 MET   A O   1 
ATOM   1862 C CB  . MET   A 1 223 ? -3.055  -1.508  -45.167 1.00 27.42 ? 225 MET   A CB  1 
ATOM   1863 C CG  . MET   A 1 223 ? -1.644  -2.006  -44.853 1.00 31.77 ? 225 MET   A CG  1 
ATOM   1864 S SD  . MET   A 1 223 ? -0.805  -2.828  -46.220 1.00 44.02 ? 225 MET   A SD  1 
ATOM   1865 C CE  . MET   A 1 223 ? -2.077  -3.937  -46.818 1.00 49.68 ? 225 MET   A CE  1 
ATOM   1866 N N   . ILE   A 1 224 ? -6.107  -1.024  -44.560 1.00 22.97 ? 226 ILE   A N   1 
ATOM   1867 C CA  . ILE   A 1 224 ? -7.339  -0.391  -45.039 1.00 22.08 ? 226 ILE   A CA  1 
ATOM   1868 C C   . ILE   A 1 224 ? -8.061  0.325   -43.909 1.00 21.53 ? 226 ILE   A C   1 
ATOM   1869 O O   . ILE   A 1 224 ? -8.804  1.281   -44.164 1.00 25.76 ? 226 ILE   A O   1 
ATOM   1870 C CB  . ILE   A 1 224 ? -8.273  -1.391  -45.746 1.00 23.49 ? 226 ILE   A CB  1 
ATOM   1871 C CG1 . ILE   A 1 224 ? -8.867  -2.398  -44.755 1.00 22.72 ? 226 ILE   A CG1 1 
ATOM   1872 C CG2 . ILE   A 1 224 ? -7.544  -2.079  -46.913 1.00 27.28 ? 226 ILE   A CG2 1 
ATOM   1873 C CD1 . ILE   A 1 224 ? -9.866  -3.370  -45.403 1.00 24.77 ? 226 ILE   A CD1 1 
ATOM   1874 N N   . PHE   A 1 225 ? -7.872  -0.104  -42.658 1.00 20.97 ? 227 PHE   A N   1 
ATOM   1875 C CA  . PHE   A 1 225 ? -8.548  0.532   -41.531 1.00 23.02 ? 227 PHE   A CA  1 
ATOM   1876 C C   . PHE   A 1 225 ? -7.669  1.537   -40.798 1.00 24.19 ? 227 PHE   A C   1 
ATOM   1877 O O   . PHE   A 1 225 ? -8.163  2.216   -39.887 1.00 27.38 ? 227 PHE   A O   1 
ATOM   1878 C CB  . PHE   A 1 225 ? -9.041  -0.514  -40.516 1.00 22.84 ? 227 PHE   A CB  1 
ATOM   1879 C CG  . PHE   A 1 225 ? -10.138 -1.399  -41.024 1.00 22.57 ? 227 PHE   A CG  1 
ATOM   1880 C CD1 . PHE   A 1 225 ? -11.189 -0.882  -41.764 1.00 20.87 ? 227 PHE   A CD1 1 
ATOM   1881 C CD2 . PHE   A 1 225 ? -10.112 -2.760  -40.759 1.00 20.54 ? 227 PHE   A CD2 1 
ATOM   1882 C CE1 . PHE   A 1 225 ? -12.205 -1.711  -42.224 1.00 26.50 ? 227 PHE   A CE1 1 
ATOM   1883 C CE2 . PHE   A 1 225 ? -11.120 -3.591  -41.221 1.00 22.31 ? 227 PHE   A CE2 1 
ATOM   1884 C CZ  . PHE   A 1 225 ? -12.162 -3.068  -41.955 1.00 23.16 ? 227 PHE   A CZ  1 
ATOM   1885 N N   . ARG   A 1 226 ? -6.391  1.645   -41.162 1.00 24.35 ? 228 ARG   A N   1 
ATOM   1886 C CA  . ARG   A 1 226 ? -5.470  2.607   -40.550 1.00 26.95 ? 228 ARG   A CA  1 
ATOM   1887 C C   . ARG   A 1 226 ? -5.327  2.361   -39.052 1.00 31.16 ? 228 ARG   A C   1 
ATOM   1888 O O   . ARG   A 1 226 ? -5.446  3.275   -38.230 1.00 30.61 ? 228 ARG   A O   1 
ATOM   1889 C CB  . ARG   A 1 226 ? -5.919  4.048   -40.811 1.00 34.17 ? 228 ARG   A CB  1 
ATOM   1890 C CG  . ARG   A 1 226 ? -6.237  4.338   -42.250 1.00 43.18 ? 228 ARG   A CG  1 
ATOM   1891 C CD  . ARG   A 1 226 ? -5.034  4.105   -43.130 1.00 55.43 ? 228 ARG   A CD  1 
ATOM   1892 N NE  . ARG   A 1 226 ? -3.812  4.708   -42.608 1.00 67.61 ? 228 ARG   A NE  1 
ATOM   1893 C CZ  . ARG   A 1 226 ? -3.585  6.016   -42.533 1.00 75.16 ? 228 ARG   A CZ  1 
ATOM   1894 N NH1 . ARG   A 1 226 ? -4.508  6.885   -42.927 1.00 78.92 ? 228 ARG   A NH1 1 
ATOM   1895 N NH2 . ARG   A 1 226 ? -2.432  6.457   -42.048 1.00 76.12 ? 228 ARG   A NH2 1 
ATOM   1896 N N   . LYS   A 1 227 ? -5.078  1.105   -38.692 1.00 25.00 ? 229 LYS   A N   1 
ATOM   1897 C CA  . LYS   A 1 227 ? -4.862  0.740   -37.297 1.00 27.36 ? 229 LYS   A CA  1 
ATOM   1898 C C   . LYS   A 1 227 ? -3.753  -0.298  -37.272 1.00 29.58 ? 229 LYS   A C   1 
ATOM   1899 O O   . LYS   A 1 227 ? -3.975  -1.445  -37.664 1.00 26.76 ? 229 LYS   A O   1 
ATOM   1900 C CB  . LYS   A 1 227 ? -6.135  0.195   -36.656 1.00 27.70 ? 229 LYS   A CB  1 
ATOM   1901 C CG  . LYS   A 1 227 ? -5.960  -0.154  -35.191 1.00 30.56 ? 229 LYS   A CG  1 
ATOM   1902 C CD  . LYS   A 1 227 ? -7.195  -0.794  -34.598 1.00 31.04 ? 229 LYS   A CD  1 
ATOM   1903 C CE  . LYS   A 1 227 ? -7.044  -0.917  -33.091 1.00 32.91 ? 229 LYS   A CE  1 
ATOM   1904 N NZ  . LYS   A 1 227 ? -5.960  -1.869  -32.707 1.00 31.35 ? 229 LYS   A NZ  1 
ATOM   1905 N N   . GLU   A 1 228 ? -2.564  0.088   -36.815 1.00 32.12 ? 230 GLU   A N   1 
ATOM   1906 C CA  . GLU   A 1 228 ? -1.406  -0.792  -36.914 1.00 39.11 ? 230 GLU   A CA  1 
ATOM   1907 C C   . GLU   A 1 228 ? -0.811  -1.010  -35.530 1.00 35.74 ? 230 GLU   A C   1 
ATOM   1908 O O   . GLU   A 1 228 ? -0.408  -0.034  -34.876 1.00 40.77 ? 230 GLU   A O   1 
ATOM   1909 C CB  . GLU   A 1 228 ? -0.360  -0.212  -37.870 1.00 47.00 ? 230 GLU   A CB  1 
ATOM   1910 C CG  . GLU   A 1 228 ? 0.465   -1.261  -38.615 1.00 54.06 ? 230 GLU   A CG  1 
ATOM   1911 C CD  . GLU   A 1 228 ? 1.536   -1.905  -37.748 1.00 56.33 ? 230 GLU   A CD  1 
ATOM   1912 O OE1 . GLU   A 1 228 ? 1.813   -3.111  -37.931 1.00 52.75 ? 230 GLU   A OE1 1 
ATOM   1913 O OE2 . GLU   A 1 228 ? 2.105   -1.202  -36.886 1.00 55.66 ? 230 GLU   A OE2 1 
ATOM   1914 N N   . PRO   A 1 229 ? -0.764  -2.250  -35.024 1.00 29.56 ? 231 PRO   A N   1 
ATOM   1915 C CA  . PRO   A 1 229 ? -1.326  -3.425  -35.692 1.00 23.45 ? 231 PRO   A CA  1 
ATOM   1916 C C   . PRO   A 1 229 ? -2.830  -3.499  -35.462 1.00 26.42 ? 231 PRO   A C   1 
ATOM   1917 O O   . PRO   A 1 229 ? -3.351  -2.795  -34.596 1.00 26.38 ? 231 PRO   A O   1 
ATOM   1918 C CB  . PRO   A 1 229 ? -0.610  -4.584  -35.003 1.00 25.75 ? 231 PRO   A CB  1 
ATOM   1919 C CG  . PRO   A 1 229 ? -0.450  -4.103  -33.607 1.00 30.36 ? 231 PRO   A CG  1 
ATOM   1920 C CD  . PRO   A 1 229 ? -0.178  -2.605  -33.719 1.00 33.40 ? 231 PRO   A CD  1 
ATOM   1921 N N   . PHE   A 1 230 ? -3.529  -4.341  -36.225 1.00 20.61 ? 232 PHE   A N   1 
ATOM   1922 C CA  . PHE   A 1 230 ? -4.978  -4.389  -36.090 1.00 20.09 ? 232 PHE   A CA  1 
ATOM   1923 C C   . PHE   A 1 230 ? -5.340  -5.096  -34.788 1.00 20.22 ? 232 PHE   A C   1 
ATOM   1924 O O   . PHE   A 1 230 ? -5.977  -4.502  -33.909 1.00 21.13 ? 232 PHE   A O   1 
ATOM   1925 C CB  . PHE   A 1 230 ? -5.605  -5.043  -37.326 1.00 21.30 ? 232 PHE   A CB  1 
ATOM   1926 C CG  . PHE   A 1 230 ? -7.110  -4.977  -37.335 1.00 19.37 ? 232 PHE   A CG  1 
ATOM   1927 C CD1 . PHE   A 1 230 ? -7.756  -3.771  -37.569 1.00 18.07 ? 232 PHE   A CD1 1 
ATOM   1928 C CD2 . PHE   A 1 230 ? -7.873  -6.105  -37.076 1.00 19.60 ? 232 PHE   A CD2 1 
ATOM   1929 C CE1 . PHE   A 1 230 ? -9.134  -3.682  -37.550 1.00 21.27 ? 232 PHE   A CE1 1 
ATOM   1930 C CE2 . PHE   A 1 230 ? -9.266  -6.025  -37.067 1.00 23.39 ? 232 PHE   A CE2 1 
ATOM   1931 C CZ  . PHE   A 1 230 ? -9.892  -4.807  -37.303 1.00 27.81 ? 232 PHE   A CZ  1 
ATOM   1932 N N   . PHE   A 1 231 ? -4.956  -6.366  -34.649 1.00 18.85 ? 233 PHE   A N   1 
ATOM   1933 C CA  . PHE   A 1 231 ? -5.172  -7.123  -33.415 1.00 20.21 ? 233 PHE   A CA  1 
ATOM   1934 C C   . PHE   A 1 231 ? -3.984  -6.901  -32.485 1.00 21.41 ? 233 PHE   A C   1 
ATOM   1935 O O   . PHE   A 1 231 ? -2.926  -7.506  -32.669 1.00 20.46 ? 233 PHE   A O   1 
ATOM   1936 C CB  . PHE   A 1 231 ? -5.332  -8.606  -33.725 1.00 19.31 ? 233 PHE   A CB  1 
ATOM   1937 C CG  . PHE   A 1 231 ? -6.511  -8.954  -34.600 1.00 18.05 ? 233 PHE   A CG  1 
ATOM   1938 C CD1 . PHE   A 1 231 ? -7.820  -8.784  -34.157 1.00 20.36 ? 233 PHE   A CD1 1 
ATOM   1939 C CD2 . PHE   A 1 231 ? -6.303  -9.525  -35.849 1.00 17.68 ? 233 PHE   A CD2 1 
ATOM   1940 C CE1 . PHE   A 1 231 ? -8.904  -9.146  -34.974 1.00 19.16 ? 233 PHE   A CE1 1 
ATOM   1941 C CE2 . PHE   A 1 231 ? -7.373  -9.897  -36.664 1.00 17.73 ? 233 PHE   A CE2 1 
ATOM   1942 C CZ  . PHE   A 1 231 ? -8.684  -9.706  -36.219 1.00 17.86 ? 233 PHE   A CZ  1 
ATOM   1943 N N   . HIS   A 1 232 ? -4.151  -6.039  -31.483 1.00 23.27 ? 234 HIS   A N   1 
ATOM   1944 C CA  . HIS   A 1 232 ? -3.026  -5.503  -30.708 1.00 23.68 ? 234 HIS   A CA  1 
ATOM   1945 C C   . HIS   A 1 232 ? -3.008  -6.114  -29.306 1.00 24.78 ? 234 HIS   A C   1 
ATOM   1946 O O   . HIS   A 1 232 ? -3.322  -5.458  -28.303 1.00 27.13 ? 234 HIS   A O   1 
ATOM   1947 C CB  . HIS   A 1 232 ? -3.132  -3.975  -30.662 1.00 27.62 ? 234 HIS   A CB  1 
ATOM   1948 C CG  . HIS   A 1 232 ? -1.852  -3.286  -30.303 1.00 36.76 ? 234 HIS   A CG  1 
ATOM   1949 N ND1 . HIS   A 1 232 ? -1.668  -1.930  -30.473 1.00 43.38 ? 234 HIS   A ND1 1 
ATOM   1950 C CD2 . HIS   A 1 232 ? -0.691  -3.763  -29.795 1.00 41.27 ? 234 HIS   A CD2 1 
ATOM   1951 C CE1 . HIS   A 1 232 ? -0.451  -1.601  -30.079 1.00 44.98 ? 234 HIS   A CE1 1 
ATOM   1952 N NE2 . HIS   A 1 232 ? 0.163   -2.694  -29.663 1.00 40.44 ? 234 HIS   A NE2 1 
ATOM   1953 N N   . GLY   A 1 233 ? -2.620  -7.388  -29.233 1.00 21.26 ? 235 GLY   A N   1 
ATOM   1954 C CA  . GLY   A 1 233 ? -2.632  -8.090  -27.961 1.00 20.03 ? 235 GLY   A CA  1 
ATOM   1955 C C   . GLY   A 1 233 ? -1.419  -7.754  -27.110 1.00 21.93 ? 235 GLY   A C   1 
ATOM   1956 O O   . GLY   A 1 233 ? -0.343  -7.449  -27.617 1.00 23.87 ? 235 GLY   A O   1 
ATOM   1957 N N   . HIS   A 1 234 ? -1.602  -7.808  -25.792 1.00 23.63 ? 236 HIS   A N   1 
ATOM   1958 C CA  A HIS   A 1 234 ? -0.461  -7.536  -24.927 0.53 23.83 ? 236 HIS   A CA  1 
ATOM   1959 C CA  B HIS   A 1 234 ? -0.527  -7.562  -24.832 0.47 24.04 ? 236 HIS   A CA  1 
ATOM   1960 C C   . HIS   A 1 234 ? 0.363   -8.780  -24.620 1.00 26.83 ? 236 HIS   A C   1 
ATOM   1961 O O   . HIS   A 1 234 ? 1.490   -8.645  -24.121 1.00 29.54 ? 236 HIS   A O   1 
ATOM   1962 C CB  A HIS   A 1 234 ? -0.902  -6.836  -23.627 0.53 27.98 ? 236 HIS   A CB  1 
ATOM   1963 C CB  B HIS   A 1 234 ? -1.123  -7.133  -23.489 0.47 25.47 ? 236 HIS   A CB  1 
ATOM   1964 C CG  A HIS   A 1 234 ? -1.795  -7.648  -22.741 0.53 26.14 ? 236 HIS   A CG  1 
ATOM   1965 C CG  B HIS   A 1 234 ? -2.006  -5.926  -23.575 0.47 29.22 ? 236 HIS   A CG  1 
ATOM   1966 N ND1 A HIS   A 1 234 ? -3.099  -7.287  -22.478 0.53 29.36 ? 236 HIS   A ND1 1 
ATOM   1967 N ND1 B HIS   A 1 234 ? -1.722  -4.849  -24.387 0.47 34.39 ? 236 HIS   A ND1 1 
ATOM   1968 C CD2 A HIS   A 1 234 ? -1.559  -8.763  -22.009 0.53 31.06 ? 236 HIS   A CD2 1 
ATOM   1969 C CD2 B HIS   A 1 234 ? -3.167  -5.626  -22.946 0.47 32.12 ? 236 HIS   A CD2 1 
ATOM   1970 C CE1 A HIS   A 1 234 ? -3.638  -8.162  -21.648 0.53 29.74 ? 236 HIS   A CE1 1 
ATOM   1971 C CE1 B HIS   A 1 234 ? -2.668  -3.936  -24.255 0.47 32.85 ? 236 HIS   A CE1 1 
ATOM   1972 N NE2 A HIS   A 1 234 ? -2.725  -9.068  -21.347 0.53 27.60 ? 236 HIS   A NE2 1 
ATOM   1973 N NE2 B HIS   A 1 234 ? -3.557  -4.383  -23.386 0.47 34.12 ? 236 HIS   A NE2 1 
ATOM   1974 N N   . ASP   A 1 235 ? -0.130  -9.968  -24.953 1.00 22.03 ? 237 ASP   A N   1 
ATOM   1975 C CA  . ASP   A 1 235 ? 0.611   -11.219 -24.862 1.00 24.19 ? 237 ASP   A CA  1 
ATOM   1976 C C   . ASP   A 1 235 ? -0.145  -12.233 -25.714 1.00 24.21 ? 237 ASP   A C   1 
ATOM   1977 O O   . ASP   A 1 235 ? -1.167  -11.901 -26.323 1.00 21.23 ? 237 ASP   A O   1 
ATOM   1978 C CB  . ASP   A 1 235 ? 0.812   -11.673 -23.401 1.00 23.04 ? 237 ASP   A CB  1 
ATOM   1979 C CG  . ASP   A 1 235 ? -0.493  -11.988 -22.662 1.00 30.33 ? 237 ASP   A CG  1 
ATOM   1980 O OD1 . ASP   A 1 235 ? -1.503  -12.365 -23.283 1.00 26.45 ? 237 ASP   A OD1 1 
ATOM   1981 O OD2 . ASP   A 1 235 ? -0.503  -11.880 -21.415 1.00 34.52 ? 237 ASP   A OD2 1 
ATOM   1982 N N   . ASN   A 1 236 ? 0.353   -13.476 -25.758 1.00 22.13 ? 238 ASN   A N   1 
ATOM   1983 C CA  . ASN   A 1 236 ? -0.259  -14.430 -26.685 1.00 22.28 ? 238 ASN   A CA  1 
ATOM   1984 C C   . ASN   A 1 236 ? -1.676  -14.811 -26.266 1.00 23.07 ? 238 ASN   A C   1 
ATOM   1985 O O   . ASN   A 1 236 ? -2.494  -15.148 -27.125 1.00 25.95 ? 238 ASN   A O   1 
ATOM   1986 C CB  . ASN   A 1 236 ? 0.609   -15.680 -26.850 1.00 22.08 ? 238 ASN   A CB  1 
ATOM   1987 C CG  . ASN   A 1 236 ? 1.927   -15.389 -27.571 1.00 30.38 ? 238 ASN   A CG  1 
ATOM   1988 O OD1 . ASN   A 1 236 ? 2.041   -14.419 -28.321 1.00 27.39 ? 238 ASN   A OD1 1 
ATOM   1989 N ND2 . ASN   A 1 236 ? 2.935   -16.226 -27.325 1.00 29.59 ? 238 ASN   A ND2 1 
ATOM   1990 N N   . TYR   A 1 237 ? -1.999  -14.751 -24.971 1.00 20.02 ? 239 TYR   A N   1 
ATOM   1991 C CA  . TYR   A 1 237 ? -3.369  -15.036 -24.553 1.00 21.04 ? 239 TYR   A CA  1 
ATOM   1992 C C   . TYR   A 1 237 ? -4.298  -13.892 -24.935 1.00 22.31 ? 239 TYR   A C   1 
ATOM   1993 O O   . TYR   A 1 237 ? -5.368  -14.106 -25.532 1.00 19.30 ? 239 TYR   A O   1 
ATOM   1994 C CB  . TYR   A 1 237 ? -3.409  -15.294 -23.044 1.00 22.59 ? 239 TYR   A CB  1 
ATOM   1995 C CG  . TYR   A 1 237 ? -2.417  -16.352 -22.640 1.00 28.54 ? 239 TYR   A CG  1 
ATOM   1996 C CD1 . TYR   A 1 237 ? -1.262  -16.018 -21.950 1.00 28.32 ? 239 TYR   A CD1 1 
ATOM   1997 C CD2 . TYR   A 1 237 ? -2.616  -17.680 -22.989 1.00 33.45 ? 239 TYR   A CD2 1 
ATOM   1998 C CE1 . TYR   A 1 237 ? -0.346  -16.983 -21.599 1.00 35.53 ? 239 TYR   A CE1 1 
ATOM   1999 C CE2 . TYR   A 1 237 ? -1.702  -18.651 -22.645 1.00 40.39 ? 239 TYR   A CE2 1 
ATOM   2000 C CZ  . TYR   A 1 237 ? -0.569  -18.296 -21.951 1.00 42.34 ? 239 TYR   A CZ  1 
ATOM   2001 O OH  . TYR   A 1 237 ? 0.347   -19.264 -21.602 1.00 45.86 ? 239 TYR   A OH  1 
ATOM   2002 N N   . ASP   A 1 238 ? -3.903  -12.663 -24.601 1.00 20.61 ? 240 ASP   A N   1 
ATOM   2003 C CA  . ASP   A 1 238 ? -4.705  -11.507 -24.972 1.00 19.89 ? 240 ASP   A CA  1 
ATOM   2004 C C   . ASP   A 1 238 ? -4.846  -11.378 -26.482 1.00 20.55 ? 240 ASP   A C   1 
ATOM   2005 O O   . ASP   A 1 238 ? -5.867  -10.876 -26.963 1.00 20.31 ? 240 ASP   A O   1 
ATOM   2006 C CB  . ASP   A 1 238 ? -4.092  -10.238 -24.379 1.00 20.92 ? 240 ASP   A CB  1 
ATOM   2007 C CG  . ASP   A 1 238 ? -4.948  -9.023  -24.606 1.00 25.22 ? 240 ASP   A CG  1 
ATOM   2008 O OD1 . ASP   A 1 238 ? -6.127  -9.028  -24.179 1.00 25.93 ? 240 ASP   A OD1 1 
ATOM   2009 O OD2 . ASP   A 1 238 ? -4.449  -8.057  -25.220 1.00 24.72 ? 240 ASP   A OD2 1 
ATOM   2010 N N   . GLN   A 1 239 ? -3.840  -11.825 -27.242 1.00 19.69 ? 241 GLN   A N   1 
ATOM   2011 C CA  . GLN   A 1 239 ? -3.949  -11.808 -28.698 1.00 17.42 ? 241 GLN   A CA  1 
ATOM   2012 C C   . GLN   A 1 239 ? -5.180  -12.585 -29.165 1.00 17.79 ? 241 GLN   A C   1 
ATOM   2013 O O   . GLN   A 1 239 ? -5.935  -12.107 -30.015 1.00 18.01 ? 241 GLN   A O   1 
ATOM   2014 C CB  . GLN   A 1 239 ? -2.673  -12.380 -29.328 1.00 14.83 ? 241 GLN   A CB  1 
ATOM   2015 C CG  . GLN   A 1 239 ? -2.609  -12.233 -30.836 1.00 17.68 ? 241 GLN   A CG  1 
ATOM   2016 C CD  . GLN   A 1 239 ? -2.523  -10.784 -31.273 1.00 17.22 ? 241 GLN   A CD  1 
ATOM   2017 O OE1 . GLN   A 1 239 ? -2.055  -9.917  -30.531 1.00 19.82 ? 241 GLN   A OE1 1 
ATOM   2018 N NE2 . GLN   A 1 239 ? -2.983  -10.513 -32.496 1.00 16.70 ? 241 GLN   A NE2 1 
ATOM   2019 N N   . LEU   A 1 240 ? -5.408  -13.781 -28.608 1.00 17.39 ? 242 LEU   A N   1 
ATOM   2020 C CA  . LEU   A 1 240 ? -6.597  -14.538 -29.003 1.00 17.55 ? 242 LEU   A CA  1 
ATOM   2021 C C   . LEU   A 1 240 ? -7.870  -13.831 -28.552 1.00 16.81 ? 242 LEU   A C   1 
ATOM   2022 O O   . LEU   A 1 240 ? -8.872  -13.832 -29.276 1.00 17.85 ? 242 LEU   A O   1 
ATOM   2023 C CB  . LEU   A 1 240 ? -6.536  -15.966 -28.450 1.00 16.67 ? 242 LEU   A CB  1 
ATOM   2024 C CG  . LEU   A 1 240 ? -7.651  -16.901 -28.934 1.00 17.86 ? 242 LEU   A CG  1 
ATOM   2025 C CD1 . LEU   A 1 240 ? -7.652  -17.032 -30.462 1.00 18.70 ? 242 LEU   A CD1 1 
ATOM   2026 C CD2 . LEU   A 1 240 ? -7.533  -18.284 -28.297 1.00 19.98 ? 242 LEU   A CD2 1 
ATOM   2027 N N   . VAL   A 1 241 ? -7.840  -13.183 -27.377 1.00 17.27 ? 243 VAL   A N   1 
ATOM   2028 C CA  . VAL   A 1 241 ? -9.024  -12.450 -26.923 1.00 17.90 ? 243 VAL   A CA  1 
ATOM   2029 C C   . VAL   A 1 241 ? -9.330  -11.293 -27.871 1.00 17.55 ? 243 VAL   A C   1 
ATOM   2030 O O   . VAL   A 1 241 ? -10.494 -11.034 -28.196 1.00 18.49 ? 243 VAL   A O   1 
ATOM   2031 C CB  . VAL   A 1 241 ? -8.852  -11.957 -25.472 1.00 20.42 ? 243 VAL   A CB  1 
ATOM   2032 C CG1 . VAL   A 1 241 ? -10.100 -11.194 -25.040 1.00 20.54 ? 243 VAL   A CG1 1 
ATOM   2033 C CG2 . VAL   A 1 241 ? -8.596  -13.128 -24.515 1.00 22.50 ? 243 VAL   A CG2 1 
ATOM   2034 N N   . ARG   A 1 242 ? -8.293  -10.591 -28.349 1.00 17.42 ? 244 ARG   A N   1 
ATOM   2035 C CA  . ARG   A 1 242 ? -8.529  -9.495  -29.293 1.00 17.88 ? 244 ARG   A CA  1 
ATOM   2036 C C   . ARG   A 1 242 ? -9.161  -10.009 -30.573 1.00 18.80 ? 244 ARG   A C   1 
ATOM   2037 O O   . ARG   A 1 242 ? -10.040 -9.355  -31.148 1.00 21.34 ? 244 ARG   A O   1 
ATOM   2038 C CB  . ARG   A 1 242 ? -7.227  -8.773  -29.650 1.00 21.90 ? 244 ARG   A CB  1 
ATOM   2039 C CG  . ARG   A 1 242 ? -6.435  -8.210  -28.498 1.00 27.45 ? 244 ARG   A CG  1 
ATOM   2040 C CD  . ARG   A 1 242 ? -7.240  -7.214  -27.706 1.00 30.75 ? 244 ARG   A CD  1 
ATOM   2041 N NE  . ARG   A 1 242 ? -6.425  -6.551  -26.688 1.00 41.17 ? 244 ARG   A NE  1 
ATOM   2042 C CZ  . ARG   A 1 242 ? -6.149  -5.250  -26.685 1.00 52.14 ? 244 ARG   A CZ  1 
ATOM   2043 N NH1 . ARG   A 1 242 ? -6.628  -4.465  -27.642 1.00 56.11 ? 244 ARG   A NH1 1 
ATOM   2044 N NH2 . ARG   A 1 242 ? -5.402  -4.730  -25.721 1.00 54.00 ? 244 ARG   A NH2 1 
ATOM   2045 N N   . ILE   A 1 243 ? -8.717  -11.174 -31.041 1.00 16.48 ? 245 ILE   A N   1 
ATOM   2046 C CA  . ILE   A 1 243 ? -9.312  -11.748 -32.241 1.00 13.87 ? 245 ILE   A CA  1 
ATOM   2047 C C   . ILE   A 1 243 ? -10.765 -12.127 -31.979 1.00 16.29 ? 245 ILE   A C   1 
ATOM   2048 O O   . ILE   A 1 243 ? -11.650 -11.854 -32.799 1.00 17.45 ? 245 ILE   A O   1 
ATOM   2049 C CB  . ILE   A 1 243 ? -8.485  -12.955 -32.718 1.00 15.45 ? 245 ILE   A CB  1 
ATOM   2050 C CG1 . ILE   A 1 243 ? -7.094  -12.489 -33.177 1.00 15.31 ? 245 ILE   A CG1 1 
ATOM   2051 C CG2 . ILE   A 1 243 ? -9.252  -13.691 -33.845 1.00 18.10 ? 245 ILE   A CG2 1 
ATOM   2052 C CD1 . ILE   A 1 243 ? -6.090  -13.626 -33.381 1.00 15.30 ? 245 ILE   A CD1 1 
ATOM   2053 N N   . ALA   A 1 244 ? -11.034 -12.755 -30.831 1.00 15.77 ? 246 ALA   A N   1 
ATOM   2054 C CA  . ALA   A 1 244 ? -12.389 -13.205 -30.514 1.00 17.68 ? 246 ALA   A CA  1 
ATOM   2055 C C   . ALA   A 1 244 ? -13.360 -12.051 -30.325 1.00 20.58 ? 246 ALA   A C   1 
ATOM   2056 O O   . ALA   A 1 244 ? -14.565 -12.229 -30.534 1.00 19.24 ? 246 ALA   A O   1 
ATOM   2057 C CB  . ALA   A 1 244 ? -12.355 -14.071 -29.258 1.00 17.89 ? 246 ALA   A CB  1 
ATOM   2058 N N   . LYS   A 1 245 ? -12.873 -10.865 -29.949 1.00 18.19 ? 247 LYS   A N   1 
ATOM   2059 C CA  . LYS   A 1 245 ? -13.785 -9.726  -29.859 1.00 18.16 ? 247 LYS   A CA  1 
ATOM   2060 C C   . LYS   A 1 245 ? -14.263 -9.254  -31.228 1.00 18.65 ? 247 LYS   A C   1 
ATOM   2061 O O   . LYS   A 1 245 ? -15.254 -8.512  -31.303 1.00 21.87 ? 247 LYS   A O   1 
ATOM   2062 C CB  . LYS   A 1 245 ? -13.125 -8.582  -29.098 1.00 19.46 ? 247 LYS   A CB  1 
ATOM   2063 C CG  . LYS   A 1 245 ? -12.941 -8.868  -27.622 1.00 21.97 ? 247 LYS   A CG  1 
ATOM   2064 C CD  . LYS   A 1 245 ? -12.278 -7.687  -26.924 1.00 27.41 ? 247 LYS   A CD  1 
ATOM   2065 C CE  . LYS   A 1 245 ? -12.203 -7.928  -25.425 1.00 36.05 ? 247 LYS   A CE  1 
ATOM   2066 N NZ  . LYS   A 1 245 ? -11.543 -6.810  -24.686 1.00 44.49 ? 247 LYS   A NZ  1 
ATOM   2067 N N   . VAL   A 1 246 ? -13.613 -9.674  -32.306 1.00 17.57 ? 248 VAL   A N   1 
ATOM   2068 C CA  . VAL   A 1 246 ? -14.014 -9.328  -33.665 1.00 17.44 ? 248 VAL   A CA  1 
ATOM   2069 C C   . VAL   A 1 246 ? -14.705 -10.503 -34.354 1.00 18.30 ? 248 VAL   A C   1 
ATOM   2070 O O   . VAL   A 1 246 ? -15.807 -10.360 -34.894 1.00 19.79 ? 248 VAL   A O   1 
ATOM   2071 C CB  . VAL   A 1 246 ? -12.790 -8.843  -34.483 1.00 16.28 ? 248 VAL   A CB  1 
ATOM   2072 C CG1 . VAL   A 1 246 ? -13.204 -8.500  -35.908 1.00 19.49 ? 248 VAL   A CG1 1 
ATOM   2073 C CG2 . VAL   A 1 246 ? -12.125 -7.633  -33.823 1.00 18.82 ? 248 VAL   A CG2 1 
ATOM   2074 N N   . LEU   A 1 247 ? -14.066 -11.681 -34.347 1.00 16.10 ? 249 LEU   A N   1 
ATOM   2075 C CA  A LEU   A 1 247 ? -14.644 -12.850 -35.002 0.57 16.48 ? 249 LEU   A CA  1 
ATOM   2076 C CA  B LEU   A 1 247 ? -14.625 -12.865 -34.991 0.43 16.71 ? 249 LEU   A CA  1 
ATOM   2077 C C   . LEU   A 1 247 ? -15.678 -13.567 -34.140 1.00 17.59 ? 249 LEU   A C   1 
ATOM   2078 O O   . LEU   A 1 247 ? -16.432 -14.397 -34.671 1.00 18.81 ? 249 LEU   A O   1 
ATOM   2079 C CB  A LEU   A 1 247 ? -13.541 -13.827 -35.415 0.57 16.89 ? 249 LEU   A CB  1 
ATOM   2080 C CB  B LEU   A 1 247 ? -13.504 -13.845 -35.340 0.43 17.15 ? 249 LEU   A CB  1 
ATOM   2081 C CG  A LEU   A 1 247 ? -12.840 -13.531 -36.750 0.57 15.03 ? 249 LEU   A CG  1 
ATOM   2082 C CG  B LEU   A 1 247 ? -12.421 -13.333 -36.292 0.43 16.50 ? 249 LEU   A CG  1 
ATOM   2083 C CD1 A LEU   A 1 247 ? -12.039 -12.232 -36.697 0.57 18.19 ? 249 LEU   A CD1 1 
ATOM   2084 C CD1 B LEU   A 1 247 ? -11.463 -14.460 -36.690 0.43 16.93 ? 249 LEU   A CD1 1 
ATOM   2085 C CD2 A LEU   A 1 247 ? -11.948 -14.695 -37.163 0.57 16.78 ? 249 LEU   A CD2 1 
ATOM   2086 C CD2 B LEU   A 1 247 ? -13.071 -12.692 -37.510 0.43 17.06 ? 249 LEU   A CD2 1 
ATOM   2087 N N   . GLY   A 1 248 ? -15.746 -13.258 -32.850 1.00 17.35 ? 250 GLY   A N   1 
ATOM   2088 C CA  . GLY   A 1 248 ? -16.738 -13.823 -31.959 1.00 17.89 ? 250 GLY   A CA  1 
ATOM   2089 C C   . GLY   A 1 248 ? -16.281 -15.128 -31.337 1.00 19.22 ? 250 GLY   A C   1 
ATOM   2090 O O   . GLY   A 1 248 ? -15.449 -15.856 -31.878 1.00 20.00 ? 250 GLY   A O   1 
ATOM   2091 N N   . THR   A 1 249 ? -16.859 -15.431 -30.169 1.00 18.49 ? 251 THR   A N   1 
ATOM   2092 C CA  . THR   A 1 249 ? -16.450 -16.632 -29.453 1.00 16.37 ? 251 THR   A CA  1 
ATOM   2093 C C   . THR   A 1 249 ? -17.148 -17.893 -29.955 1.00 16.65 ? 251 THR   A C   1 
ATOM   2094 O O   . THR   A 1 249 ? -16.589 -18.990 -29.833 1.00 20.26 ? 251 THR   A O   1 
ATOM   2095 C CB  . THR   A 1 249 ? -16.670 -16.452 -27.948 1.00 17.85 ? 251 THR   A CB  1 
ATOM   2096 O OG1 . THR   A 1 249 ? -17.972 -15.892 -27.709 1.00 20.25 ? 251 THR   A OG1 1 
ATOM   2097 C CG2 . THR   A 1 249 ? -15.612 -15.514 -27.370 1.00 20.46 ? 251 THR   A CG2 1 
ATOM   2098 N N   . GLU   A 1 250 ? -18.370 -17.788 -30.489 1.00 17.89 ? 252 GLU   A N   1 
ATOM   2099 C CA  . GLU   A 1 250 ? -19.035 -19.012 -30.928 1.00 20.43 ? 252 GLU   A CA  1 
ATOM   2100 C C   . GLU   A 1 250 ? -18.271 -19.682 -32.063 1.00 17.85 ? 252 GLU   A C   1 
ATOM   2101 O O   . GLU   A 1 250 ? -18.148 -20.913 -32.099 1.00 22.05 ? 252 GLU   A O   1 
ATOM   2102 C CB  . GLU   A 1 250 ? -20.477 -18.719 -31.335 1.00 21.78 ? 252 GLU   A CB  1 
ATOM   2103 C CG  . GLU   A 1 250 ? -21.353 -18.362 -30.138 1.00 26.53 ? 252 GLU   A CG  1 
ATOM   2104 C CD  . GLU   A 1 250 ? -21.618 -19.555 -29.228 1.00 45.25 ? 252 GLU   A CD  1 
ATOM   2105 O OE1 . GLU   A 1 250 ? -22.575 -20.312 -29.499 1.00 54.70 ? 252 GLU   A OE1 1 
ATOM   2106 O OE2 . GLU   A 1 250 ? -20.870 -19.741 -28.247 1.00 53.44 ? 252 GLU   A OE2 1 
ATOM   2107 N N   . ASP   A 1 251 ? -17.713 -18.896 -32.984 1.00 19.27 ? 253 ASP   A N   1 
ATOM   2108 C CA  . ASP   A 1 251 ? -16.979 -19.533 -34.068 1.00 19.48 ? 253 ASP   A CA  1 
ATOM   2109 C C   . ASP   A 1 251 ? -15.603 -20.007 -33.627 1.00 17.65 ? 253 ASP   A C   1 
ATOM   2110 O O   . ASP   A 1 251 ? -15.059 -20.934 -34.240 1.00 18.50 ? 253 ASP   A O   1 
ATOM   2111 C CB  . ASP   A 1 251 ? -16.894 -18.597 -35.270 1.00 19.07 ? 253 ASP   A CB  1 
ATOM   2112 C CG  . ASP   A 1 251 ? -18.242 -18.454 -35.977 1.00 26.03 ? 253 ASP   A CG  1 
ATOM   2113 O OD1 . ASP   A 1 251 ? -18.970 -19.468 -36.067 1.00 25.46 ? 253 ASP   A OD1 1 
ATOM   2114 O OD2 . ASP   A 1 251 ? -18.589 -17.342 -36.425 1.00 25.86 ? 253 ASP   A OD2 1 
ATOM   2115 N N   . LEU   A 1 252 ? -15.046 -19.416 -32.565 1.00 17.96 ? 254 LEU   A N   1 
ATOM   2116 C CA  . LEU   A 1 252 ? -13.832 -19.960 -31.967 1.00 16.16 ? 254 LEU   A CA  1 
ATOM   2117 C C   . LEU   A 1 252 ? -14.108 -21.341 -31.387 1.00 18.11 ? 254 LEU   A C   1 
ATOM   2118 O O   . LEU   A 1 252 ? -13.327 -22.280 -31.588 1.00 19.41 ? 254 LEU   A O   1 
ATOM   2119 C CB  . LEU   A 1 252 ? -13.311 -19.012 -30.887 1.00 17.02 ? 254 LEU   A CB  1 
ATOM   2120 C CG  . LEU   A 1 252 ? -12.100 -19.507 -30.083 1.00 18.18 ? 254 LEU   A CG  1 
ATOM   2121 C CD1 . LEU   A 1 252 ? -10.925 -19.849 -30.997 1.00 19.14 ? 254 LEU   A CD1 1 
ATOM   2122 C CD2 . LEU   A 1 252 ? -11.687 -18.455 -29.082 1.00 20.12 ? 254 LEU   A CD2 1 
ATOM   2123 N N   . TYR   A 1 253 ? -15.237 -21.489 -30.691 1.00 20.25 ? 255 TYR   A N   1 
ATOM   2124 C CA  . TYR   A 1 253 ? -15.584 -22.798 -30.158 1.00 19.21 ? 255 TYR   A CA  1 
ATOM   2125 C C   . TYR   A 1 253 ? -15.889 -23.791 -31.271 1.00 19.70 ? 255 TYR   A C   1 
ATOM   2126 O O   . TYR   A 1 253 ? -15.503 -24.961 -31.176 1.00 20.83 ? 255 TYR   A O   1 
ATOM   2127 C CB  . TYR   A 1 253 ? -16.744 -22.674 -29.172 1.00 20.70 ? 255 TYR   A CB  1 
ATOM   2128 C CG  . TYR   A 1 253 ? -16.271 -22.350 -27.772 1.00 23.29 ? 255 TYR   A CG  1 
ATOM   2129 C CD1 . TYR   A 1 253 ? -15.701 -23.333 -26.970 1.00 24.83 ? 255 TYR   A CD1 1 
ATOM   2130 C CD2 . TYR   A 1 253 ? -16.381 -21.069 -27.251 1.00 26.51 ? 255 TYR   A CD2 1 
ATOM   2131 C CE1 . TYR   A 1 253 ? -15.260 -23.054 -25.691 1.00 26.60 ? 255 TYR   A CE1 1 
ATOM   2132 C CE2 . TYR   A 1 253 ? -15.940 -20.783 -25.967 1.00 28.21 ? 255 TYR   A CE2 1 
ATOM   2133 C CZ  . TYR   A 1 253 ? -15.380 -21.779 -25.197 1.00 28.10 ? 255 TYR   A CZ  1 
ATOM   2134 O OH  . TYR   A 1 253 ? -14.942 -21.513 -23.914 1.00 34.48 ? 255 TYR   A OH  1 
ATOM   2135 N N   . ASP   A 1 254 ? -16.538 -23.346 -32.356 1.00 19.42 ? 256 ASP   A N   1 
ATOM   2136 C CA  . ASP   A 1 254 ? -16.721 -24.243 -33.498 1.00 22.03 ? 256 ASP   A CA  1 
ATOM   2137 C C   . ASP   A 1 254 ? -15.380 -24.736 -34.029 1.00 19.11 ? 256 ASP   A C   1 
ATOM   2138 O O   . ASP   A 1 254 ? -15.240 -25.911 -34.392 1.00 22.00 ? 256 ASP   A O   1 
ATOM   2139 C CB  . ASP   A 1 254 ? -17.484 -23.550 -34.622 1.00 23.14 ? 256 ASP   A CB  1 
ATOM   2140 C CG  . ASP   A 1 254 ? -18.958 -23.350 -34.313 1.00 28.98 ? 256 ASP   A CG  1 
ATOM   2141 O OD1 . ASP   A 1 254 ? -19.566 -22.507 -34.994 1.00 30.72 ? 256 ASP   A OD1 1 
ATOM   2142 O OD2 . ASP   A 1 254 ? -19.506 -24.006 -33.399 1.00 28.25 ? 256 ASP   A OD2 1 
ATOM   2143 N N   . TYR   A 1 255 ? -14.395 -23.837 -34.104 1.00 17.70 ? 257 TYR   A N   1 
ATOM   2144 C CA  . TYR   A 1 255 ? -13.076 -24.177 -34.627 1.00 18.97 ? 257 TYR   A CA  1 
ATOM   2145 C C   . TYR   A 1 255 ? -12.399 -25.218 -33.757 1.00 20.57 ? 257 TYR   A C   1 
ATOM   2146 O O   . TYR   A 1 255 ? -11.987 -26.278 -34.241 1.00 21.93 ? 257 TYR   A O   1 
ATOM   2147 C CB  . TYR   A 1 255 ? -12.229 -22.905 -34.719 1.00 19.52 ? 257 TYR   A CB  1 
ATOM   2148 C CG  . TYR   A 1 255 ? -10.780 -23.101 -35.137 1.00 18.96 ? 257 TYR   A CG  1 
ATOM   2149 C CD1 . TYR   A 1 255 ? -10.458 -23.823 -36.288 1.00 18.63 ? 257 TYR   A CD1 1 
ATOM   2150 C CD2 . TYR   A 1 255 ? -9.743  -22.520 -34.408 1.00 20.17 ? 257 TYR   A CD2 1 
ATOM   2151 C CE1 . TYR   A 1 255 ? -9.146  -23.987 -36.689 1.00 19.91 ? 257 TYR   A CE1 1 
ATOM   2152 C CE2 . TYR   A 1 255 ? -8.409  -22.677 -34.814 1.00 19.19 ? 257 TYR   A CE2 1 
ATOM   2153 C CZ  . TYR   A 1 255 ? -8.129  -23.411 -35.958 1.00 22.25 ? 257 TYR   A CZ  1 
ATOM   2154 O OH  . TYR   A 1 255 ? -6.821  -23.576 -36.385 1.00 22.72 ? 257 TYR   A OH  1 
ATOM   2155 N N   . ILE   A 1 256 ? -12.295 -24.954 -32.452 1.00 21.72 ? 258 ILE   A N   1 
ATOM   2156 C CA  . ILE   A 1 256 ? -11.586 -25.922 -31.629 1.00 23.18 ? 258 ILE   A CA  1 
ATOM   2157 C C   . ILE   A 1 256 ? -12.393 -27.212 -31.501 1.00 24.15 ? 258 ILE   A C   1 
ATOM   2158 O O   . ILE   A 1 256 ? -11.811 -28.294 -31.363 1.00 26.13 ? 258 ILE   A O   1 
ATOM   2159 C CB  . ILE   A 1 256 ? -11.212 -25.320 -30.260 1.00 24.76 ? 258 ILE   A CB  1 
ATOM   2160 C CG1 . ILE   A 1 256 ? -12.456 -24.992 -29.438 1.00 22.81 ? 258 ILE   A CG1 1 
ATOM   2161 C CG2 . ILE   A 1 256 ? -10.362 -24.060 -30.450 1.00 23.61 ? 258 ILE   A CG2 1 
ATOM   2162 C CD1 . ILE   A 1 256 ? -12.140 -24.656 -27.986 1.00 24.05 ? 258 ILE   A CD1 1 
ATOM   2163 N N   . ASP   A 1 257 ? -13.727 -27.141 -31.600 1.00 20.61 ? 259 ASP   A N   1 
ATOM   2164 C CA  . ASP   A 1 257 ? -14.526 -28.367 -31.539 1.00 18.27 ? 259 ASP   A CA  1 
ATOM   2165 C C   . ASP   A 1 257 ? -14.345 -29.209 -32.797 1.00 24.50 ? 259 ASP   A C   1 
ATOM   2166 O O   . ASP   A 1 257 ? -14.360 -30.443 -32.726 1.00 25.31 ? 259 ASP   A O   1 
ATOM   2167 C CB  . ASP   A 1 257 ? -16.014 -28.047 -31.337 1.00 21.37 ? 259 ASP   A CB  1 
ATOM   2168 C CG  . ASP   A 1 257 ? -16.333 -27.547 -29.929 1.00 21.17 ? 259 ASP   A CG  1 
ATOM   2169 O OD1 . ASP   A 1 257 ? -15.450 -27.600 -29.049 1.00 25.32 ? 259 ASP   A OD1 1 
ATOM   2170 O OD2 . ASP   A 1 257 ? -17.478 -27.088 -29.720 1.00 26.50 ? 259 ASP   A OD2 1 
ATOM   2171 N N   . LYS   A 1 258 ? -14.183 -28.563 -33.960 1.00 23.00 ? 260 LYS   A N   1 
ATOM   2172 C CA  . LYS   A 1 258 ? -13.955 -29.309 -35.197 1.00 28.42 ? 260 LYS   A CA  1 
ATOM   2173 C C   . LYS   A 1 258 ? -12.691 -30.154 -35.109 1.00 25.89 ? 260 LYS   A C   1 
ATOM   2174 O O   . LYS   A 1 258 ? -12.674 -31.308 -35.553 1.00 27.48 ? 260 LYS   A O   1 
ATOM   2175 C CB  . LYS   A 1 258 ? -13.872 -28.356 -36.392 1.00 22.44 ? 260 LYS   A CB  1 
ATOM   2176 C CG  . LYS   A 1 258 ? -13.344 -29.023 -37.663 1.00 22.27 ? 260 LYS   A CG  1 
ATOM   2177 C CD  . LYS   A 1 258 ? -13.365 -28.091 -38.854 1.00 23.84 ? 260 LYS   A CD  1 
ATOM   2178 C CE  . LYS   A 1 258 ? -12.742 -28.777 -40.065 1.00 25.53 ? 260 LYS   A CE  1 
ATOM   2179 N NZ  . LYS   A 1 258 ? -12.590 -27.864 -41.231 1.00 27.58 ? 260 LYS   A NZ  1 
ATOM   2180 N N   . TYR   A 1 259 ? -11.628 -29.608 -34.529 1.00 20.71 ? 261 TYR   A N   1 
ATOM   2181 C CA  . TYR   A 1 259 ? -10.360 -30.312 -34.442 1.00 26.10 ? 261 TYR   A CA  1 
ATOM   2182 C C   . TYR   A 1 259 ? -10.183 -31.009 -33.098 1.00 30.09 ? 261 TYR   A C   1 
ATOM   2183 O O   . TYR   A 1 259 ? -9.101  -31.538 -32.822 1.00 29.36 ? 261 TYR   A O   1 
ATOM   2184 C CB  . TYR   A 1 259 ? -9.204  -29.345 -34.742 1.00 24.78 ? 261 TYR   A CB  1 
ATOM   2185 C CG  . TYR   A 1 259 ? -9.291  -28.820 -36.163 1.00 23.26 ? 261 TYR   A CG  1 
ATOM   2186 C CD1 . TYR   A 1 259 ? -8.766  -29.549 -37.227 1.00 25.14 ? 261 TYR   A CD1 1 
ATOM   2187 C CD2 . TYR   A 1 259 ? -9.947  -27.622 -36.444 1.00 23.37 ? 261 TYR   A CD2 1 
ATOM   2188 C CE1 . TYR   A 1 259 ? -8.882  -29.091 -38.535 1.00 22.66 ? 261 TYR   A CE1 1 
ATOM   2189 C CE2 . TYR   A 1 259 ? -10.065 -27.152 -37.739 1.00 23.69 ? 261 TYR   A CE2 1 
ATOM   2190 C CZ  . TYR   A 1 259 ? -9.526  -27.888 -38.784 1.00 23.68 ? 261 TYR   A CZ  1 
ATOM   2191 O OH  . TYR   A 1 259 ? -9.650  -27.413 -40.071 1.00 23.65 ? 261 TYR   A OH  1 
ATOM   2192 N N   . ASN   A 1 260 ? -11.249 -31.070 -32.289 1.00 26.26 ? 262 ASN   A N   1 
ATOM   2193 C CA  . ASN   A 1 260 ? -11.215 -31.710 -30.972 1.00 30.02 ? 262 ASN   A CA  1 
ATOM   2194 C C   . ASN   A 1 260 ? -10.066 -31.153 -30.129 1.00 25.05 ? 262 ASN   A C   1 
ATOM   2195 O O   . ASN   A 1 260 ? -9.334  -31.897 -29.473 1.00 35.16 ? 262 ASN   A O   1 
ATOM   2196 C CB  . ASN   A 1 260 ? -11.129 -33.240 -31.100 1.00 32.18 ? 262 ASN   A CB  1 
ATOM   2197 C CG  . ASN   A 1 260 ? -12.414 -33.870 -31.652 1.00 40.06 ? 262 ASN   A CG  1 
ATOM   2198 O OD1 . ASN   A 1 260 ? -13.393 -33.183 -31.931 1.00 41.07 ? 262 ASN   A OD1 1 
ATOM   2199 N ND2 . ASN   A 1 260 ? -12.402 -35.188 -31.814 1.00 46.61 ? 262 ASN   A ND2 1 
ATOM   2200 N N   . ILE   A 1 261 ? -9.898  -29.781 -30.181 1.00 28.07 ? 263 ILE   A N   1 
ATOM   2201 C CA  . ILE   A 1 261 ? -8.920  -28.978 -29.444 1.00 30.68 ? 263 ILE   A CA  1 
ATOM   2202 C C   . ILE   A 1 261 ? -9.577  -28.456 -28.173 1.00 26.22 ? 263 ILE   A C   1 
ATOM   2203 O O   . ILE   A 1 261 ? -10.768 -28.131 -28.158 1.00 29.64 ? 263 ILE   A O   1 
ATOM   2204 C CB  . ILE   A 1 261 ? -8.424  -27.788 -30.303 1.00 32.16 ? 263 ILE   A CB  1 
ATOM   2205 C CG1 . ILE   A 1 261 ? -7.718  -28.240 -31.576 1.00 39.99 ? 263 ILE   A CG1 1 
ATOM   2206 C CG2 . ILE   A 1 261 ? -7.540  -26.817 -29.503 1.00 33.27 ? 263 ILE   A CG2 1 
ATOM   2207 C CD1 . ILE   A 1 261 ? -7.382  -27.073 -32.485 1.00 39.66 ? 263 ILE   A CD1 1 
ATOM   2208 N N   . GLU   A 1 262 ? -8.790  -28.331 -27.106 1.00 27.44 ? 264 GLU   A N   1 
ATOM   2209 C CA  . GLU   A 1 262 ? -9.238  -27.760 -25.843 1.00 31.70 ? 264 GLU   A CA  1 
ATOM   2210 C C   . GLU   A 1 262 ? -8.500  -26.448 -25.599 1.00 32.76 ? 264 GLU   A C   1 
ATOM   2211 O O   . GLU   A 1 262 ? -7.282  -26.382 -25.777 1.00 31.66 ? 264 GLU   A O   1 
ATOM   2212 C CB  . GLU   A 1 262 ? -8.975  -28.764 -24.716 1.00 36.49 ? 264 GLU   A CB  1 
ATOM   2213 C CG  . GLU   A 1 262 ? -9.473  -28.378 -23.364 1.00 44.96 ? 264 GLU   A CG  1 
ATOM   2214 C CD  . GLU   A 1 262 ? -9.777  -29.600 -22.512 1.00 41.78 ? 264 GLU   A CD  1 
ATOM   2215 O OE1 . GLU   A 1 262 ? -10.810 -29.581 -21.814 1.00 45.56 ? 264 GLU   A OE1 1 
ATOM   2216 O OE2 . GLU   A 1 262 ? -8.992  -30.577 -22.552 1.00 37.15 ? 264 GLU   A OE2 1 
ATOM   2217 N N   . LEU   A 1 263 ? -9.224  -25.400 -25.203 1.00 31.71 ? 265 LEU   A N   1 
ATOM   2218 C CA  . LEU   A 1 263 ? -8.541  -24.156 -24.871 1.00 31.23 ? 265 LEU   A CA  1 
ATOM   2219 C C   . LEU   A 1 263 ? -7.762  -24.288 -23.566 1.00 32.18 ? 265 LEU   A C   1 
ATOM   2220 O O   . LEU   A 1 263 ? -8.132  -25.046 -22.663 1.00 32.92 ? 265 LEU   A O   1 
ATOM   2221 C CB  . LEU   A 1 263 ? -9.524  -22.990 -24.750 1.00 29.72 ? 265 LEU   A CB  1 
ATOM   2222 C CG  . LEU   A 1 263 ? -10.056 -22.351 -26.028 1.00 30.07 ? 265 LEU   A CG  1 
ATOM   2223 C CD1 . LEU   A 1 263 ? -11.062 -21.275 -25.670 1.00 29.16 ? 265 LEU   A CD1 1 
ATOM   2224 C CD2 . LEU   A 1 263 ? -8.916  -21.783 -26.866 1.00 32.55 ? 265 LEU   A CD2 1 
ATOM   2225 N N   . ASP   A 1 264 ? -6.670  -23.541 -23.480 1.00 27.10 ? 266 ASP   A N   1 
ATOM   2226 C CA  . ASP   A 1 264 ? -5.958  -23.383 -22.223 1.00 29.78 ? 266 ASP   A CA  1 
ATOM   2227 C C   . ASP   A 1 264 ? -6.948  -22.950 -21.145 1.00 29.41 ? 266 ASP   A C   1 
ATOM   2228 O O   . ASP   A 1 264 ? -7.729  -22.015 -21.369 1.00 27.67 ? 266 ASP   A O   1 
ATOM   2229 C CB  . ASP   A 1 264 ? -4.846  -22.339 -22.390 1.00 31.53 ? 266 ASP   A CB  1 
ATOM   2230 C CG  . ASP   A 1 264 ? -3.835  -22.336 -21.246 1.00 32.61 ? 266 ASP   A CG  1 
ATOM   2231 O OD1 . ASP   A 1 264 ? -4.209  -22.529 -20.072 1.00 32.43 ? 266 ASP   A OD1 1 
ATOM   2232 O OD2 . ASP   A 1 264 ? -2.645  -22.101 -21.527 1.00 35.50 ? 266 ASP   A OD2 1 
ATOM   2233 N N   . PRO   A 1 265 ? -6.984  -23.619 -19.992 1.00 27.22 ? 267 PRO   A N   1 
ATOM   2234 C CA  . PRO   A 1 265 ? -7.920  -23.194 -18.944 1.00 23.91 ? 267 PRO   A CA  1 
ATOM   2235 C C   . PRO   A 1 265 ? -7.698  -21.774 -18.479 1.00 28.01 ? 267 PRO   A C   1 
ATOM   2236 O O   . PRO   A 1 265 ? -8.613  -21.184 -17.894 1.00 29.59 ? 267 PRO   A O   1 
ATOM   2237 C CB  . PRO   A 1 265 ? -7.671  -24.203 -17.812 1.00 25.67 ? 267 PRO   A CB  1 
ATOM   2238 C CG  . PRO   A 1 265 ? -6.351  -24.807 -18.118 1.00 32.08 ? 267 PRO   A CG  1 
ATOM   2239 C CD  . PRO   A 1 265 ? -6.239  -24.827 -19.608 1.00 30.72 ? 267 PRO   A CD  1 
ATOM   2240 N N   . ARG   A 1 266 ? -6.531  -21.182 -18.739 1.00 28.18 ? 268 ARG   A N   1 
ATOM   2241 C CA  . ARG   A 1 266 ? -6.357  -19.801 -18.317 1.00 30.87 ? 268 ARG   A CA  1 
ATOM   2242 C C   . ARG   A 1 266 ? -7.261  -18.837 -19.083 1.00 28.37 ? 268 ARG   A C   1 
ATOM   2243 O O   . ARG   A 1 266 ? -7.454  -17.708 -18.618 1.00 28.62 ? 268 ARG   A O   1 
ATOM   2244 C CB  . ARG   A 1 266 ? -4.888  -19.401 -18.435 1.00 46.52 ? 268 ARG   A CB  1 
ATOM   2245 C CG  . ARG   A 1 266 ? -4.522  -18.536 -19.608 1.00 55.93 ? 268 ARG   A CG  1 
ATOM   2246 C CD  . ARG   A 1 266 ? -3.053  -18.185 -19.490 1.00 63.52 ? 268 ARG   A CD  1 
ATOM   2247 N NE  . ARG   A 1 266 ? -2.225  -19.389 -19.478 1.00 67.56 ? 268 ARG   A NE  1 
ATOM   2248 C CZ  . ARG   A 1 266 ? -1.011  -19.464 -18.941 1.00 71.27 ? 268 ARG   A CZ  1 
ATOM   2249 N NH1 . ARG   A 1 266 ? -0.471  -18.404 -18.354 1.00 71.84 ? 268 ARG   A NH1 1 
ATOM   2250 N NH2 . ARG   A 1 266 ? -0.338  -20.606 -18.987 1.00 71.38 ? 268 ARG   A NH2 1 
ATOM   2251 N N   . PHE   A 1 267 ? -7.862  -19.265 -20.202 1.00 24.34 ? 269 PHE   A N   1 
ATOM   2252 C CA  . PHE   A 1 267 ? -8.852  -18.424 -20.873 1.00 21.69 ? 269 PHE   A CA  1 
ATOM   2253 C C   . PHE   A 1 267 ? -10.190 -18.375 -20.147 1.00 28.39 ? 269 PHE   A C   1 
ATOM   2254 O O   . PHE   A 1 267 ? -11.042 -17.566 -20.532 1.00 33.80 ? 269 PHE   A O   1 
ATOM   2255 C CB  . PHE   A 1 267 ? -9.100  -18.894 -22.310 1.00 24.25 ? 269 PHE   A CB  1 
ATOM   2256 C CG  . PHE   A 1 267 ? -7.973  -18.588 -23.255 1.00 21.08 ? 269 PHE   A CG  1 
ATOM   2257 C CD1 . PHE   A 1 267 ? -7.106  -19.588 -23.674 1.00 20.08 ? 269 PHE   A CD1 1 
ATOM   2258 C CD2 . PHE   A 1 267 ? -7.786  -17.299 -23.734 1.00 22.92 ? 269 PHE   A CD2 1 
ATOM   2259 C CE1 . PHE   A 1 267 ? -6.057  -19.297 -24.533 1.00 23.77 ? 269 PHE   A CE1 1 
ATOM   2260 C CE2 . PHE   A 1 267 ? -6.745  -17.005 -24.594 1.00 23.52 ? 269 PHE   A CE2 1 
ATOM   2261 C CZ  . PHE   A 1 267 ? -5.884  -17.995 -25.000 1.00 22.81 ? 269 PHE   A CZ  1 
ATOM   2262 N N   . ASN   A 1 268 ? -10.402 -19.210 -19.120 1.00 31.73 ? 270 ASN   A N   1 
ATOM   2263 C CA  . ASN   A 1 268 ? -11.703 -19.239 -18.452 1.00 34.20 ? 270 ASN   A CA  1 
ATOM   2264 C C   . ASN   A 1 268 ? -12.078 -17.878 -17.876 1.00 36.16 ? 270 ASN   A C   1 
ATOM   2265 O O   . ASN   A 1 268 ? -13.263 -17.525 -17.849 1.00 41.10 ? 270 ASN   A O   1 
ATOM   2266 C CB  . ASN   A 1 268 ? -11.719 -20.288 -17.336 1.00 38.34 ? 270 ASN   A CB  1 
ATOM   2267 C CG  . ASN   A 1 268 ? -11.684 -21.713 -17.860 1.00 38.49 ? 270 ASN   A CG  1 
ATOM   2268 O OD1 . ASN   A 1 268 ? -11.415 -22.654 -17.113 1.00 47.11 ? 270 ASN   A OD1 1 
ATOM   2269 N ND2 . ASN   A 1 268 ? -11.946 -21.877 -19.145 1.00 36.98 ? 270 ASN   A ND2 1 
ATOM   2270 N N   . ASP   A 1 269 ? -11.097 -17.098 -17.426 1.00 32.20 ? 271 ASP   A N   1 
ATOM   2271 C CA  . ASP   A 1 269 ? -11.354 -15.829 -16.762 1.00 37.66 ? 271 ASP   A CA  1 
ATOM   2272 C C   . ASP   A 1 269 ? -11.115 -14.614 -17.653 1.00 38.94 ? 271 ASP   A C   1 
ATOM   2273 O O   . ASP   A 1 269 ? -11.268 -13.487 -17.172 1.00 41.05 ? 271 ASP   A O   1 
ATOM   2274 C CB  . ASP   A 1 269 ? -10.487 -15.701 -15.503 1.00 55.58 ? 271 ASP   A CB  1 
ATOM   2275 C CG  . ASP   A 1 269 ? -10.753 -16.801 -14.496 1.00 73.41 ? 271 ASP   A CG  1 
ATOM   2276 O OD1 . ASP   A 1 269 ? -9.779  -17.358 -13.943 1.00 78.57 ? 271 ASP   A OD1 1 
ATOM   2277 O OD2 . ASP   A 1 269 ? -11.940 -17.122 -14.269 1.00 78.08 ? 271 ASP   A OD2 1 
ATOM   2278 N N   . ILE   A 1 270 ? -10.741 -14.797 -18.910 1.00 30.69 ? 272 ILE   A N   1 
ATOM   2279 C CA  . ILE   A 1 270 ? -10.407 -13.638 -19.750 1.00 27.26 ? 272 ILE   A CA  1 
ATOM   2280 C C   . ILE   A 1 270 ? -11.130 -13.620 -21.082 1.00 26.46 ? 272 ILE   A C   1 
ATOM   2281 O O   . ILE   A 1 270 ? -11.142 -12.563 -21.740 1.00 25.80 ? 272 ILE   A O   1 
ATOM   2282 C CB  . ILE   A 1 270 ? -8.882  -13.547 -19.973 1.00 27.61 ? 272 ILE   A CB  1 
ATOM   2283 C CG1 . ILE   A 1 270 ? -8.340  -14.831 -20.611 1.00 24.93 ? 272 ILE   A CG1 1 
ATOM   2284 C CG2 . ILE   A 1 270 ? -8.173  -13.216 -18.671 1.00 29.46 ? 272 ILE   A CG2 1 
ATOM   2285 C CD1 . ILE   A 1 270 ? -6.897  -14.722 -21.091 1.00 27.68 ? 272 ILE   A CD1 1 
ATOM   2286 N N   . LEU   A 1 271 ? -11.733 -14.722 -21.543 1.00 26.16 ? 273 LEU   A N   1 
ATOM   2287 C CA  . LEU   A 1 271 ? -12.220 -14.770 -22.919 1.00 22.28 ? 273 LEU   A CA  1 
ATOM   2288 C C   . LEU   A 1 271 ? -13.582 -14.100 -23.069 1.00 27.29 ? 273 LEU   A C   1 
ATOM   2289 O O   . LEU   A 1 271 ? -13.827 -13.411 -24.062 1.00 28.07 ? 273 LEU   A O   1 
ATOM   2290 C CB  . LEU   A 1 271 ? -12.285 -16.219 -23.408 1.00 25.73 ? 273 LEU   A CB  1 
ATOM   2291 C CG  . LEU   A 1 271 ? -12.722 -16.453 -24.858 1.00 27.33 ? 273 LEU   A CG  1 
ATOM   2292 C CD1 . LEU   A 1 271 ? -11.808 -15.725 -25.839 1.00 24.48 ? 273 LEU   A CD1 1 
ATOM   2293 C CD2 . LEU   A 1 271 ? -12.752 -17.943 -25.160 1.00 30.18 ? 273 LEU   A CD2 1 
ATOM   2294 N N   . GLY   A 1 272 ? -14.475 -14.302 -22.115 1.00 26.85 ? 274 GLY   A N   1 
ATOM   2295 C CA  . GLY   A 1 272 ? -15.802 -13.729 -22.219 1.00 27.14 ? 274 GLY   A CA  1 
ATOM   2296 C C   . GLY   A 1 272 ? -16.629 -14.347 -23.339 1.00 24.92 ? 274 GLY   A C   1 
ATOM   2297 O O   . GLY   A 1 272 ? -16.291 -15.385 -23.925 1.00 26.50 ? 274 GLY   A O   1 
ATOM   2298 N N   . ARG   A 1 273 ? -17.752 -13.685 -23.618 1.00 22.48 ? 275 ARG   A N   1 
ATOM   2299 C CA  . ARG   A 1 273 ? -18.626 -14.034 -24.730 1.00 23.41 ? 275 ARG   A CA  1 
ATOM   2300 C C   . ARG   A 1 273 ? -18.737 -12.836 -25.660 1.00 25.43 ? 275 ARG   A C   1 
ATOM   2301 O O   . ARG   A 1 273 ? -19.000 -11.717 -25.206 1.00 27.39 ? 275 ARG   A O   1 
ATOM   2302 C CB  . ARG   A 1 273 ? -20.020 -14.450 -24.244 1.00 25.91 ? 275 ARG   A CB  1 
ATOM   2303 C CG  . ARG   A 1 273 ? -20.040 -15.709 -23.394 1.00 28.45 ? 275 ARG   A CG  1 
ATOM   2304 C CD  . ARG   A 1 273 ? -21.455 -16.291 -23.324 1.00 30.23 ? 275 ARG   A CD  1 
ATOM   2305 N NE  . ARG   A 1 273 ? -22.387 -15.414 -22.617 1.00 33.51 ? 275 ARG   A NE  1 
ATOM   2306 C CZ  . ARG   A 1 273 ? -23.710 -15.558 -22.635 1.00 37.68 ? 275 ARG   A CZ  1 
ATOM   2307 N NH1 . ARG   A 1 273 ? -24.263 -16.541 -23.334 1.00 41.05 ? 275 ARG   A NH1 1 
ATOM   2308 N NH2 . ARG   A 1 273 ? -24.482 -14.715 -21.960 1.00 38.76 ? 275 ARG   A NH2 1 
ATOM   2309 N N   . HIS   A 1 274 ? -18.529 -13.066 -26.958 1.00 18.88 ? 276 HIS   A N   1 
ATOM   2310 C CA  . HIS   A 1 274 ? -18.497 -11.987 -27.935 1.00 18.60 ? 276 HIS   A CA  1 
ATOM   2311 C C   . HIS   A 1 274 ? -19.200 -12.407 -29.210 1.00 18.78 ? 276 HIS   A C   1 
ATOM   2312 O O   . HIS   A 1 274 ? -18.919 -13.477 -29.755 1.00 20.23 ? 276 HIS   A O   1 
ATOM   2313 C CB  . HIS   A 1 274 ? -17.051 -11.585 -28.257 1.00 18.70 ? 276 HIS   A CB  1 
ATOM   2314 C CG  . HIS   A 1 274 ? -16.290 -11.171 -27.051 1.00 19.75 ? 276 HIS   A CG  1 
ATOM   2315 N ND1 . HIS   A 1 274 ? -16.490 -9.952  -26.439 1.00 23.05 ? 276 HIS   A ND1 1 
ATOM   2316 C CD2 . HIS   A 1 274 ? -15.373 -11.827 -26.302 1.00 20.84 ? 276 HIS   A CD2 1 
ATOM   2317 C CE1 . HIS   A 1 274 ? -15.708 -9.864  -25.379 1.00 20.02 ? 276 HIS   A CE1 1 
ATOM   2318 N NE2 . HIS   A 1 274 ? -15.020 -10.987 -25.274 1.00 23.49 ? 276 HIS   A NE2 1 
ATOM   2319 N N   . SER   A 1 275 ? -20.097 -11.552 -29.689 1.00 18.72 ? 277 SER   A N   1 
ATOM   2320 C CA  . SER   A 1 275 ? -20.687 -11.740 -31.004 1.00 17.95 ? 277 SER   A CA  1 
ATOM   2321 C C   . SER   A 1 275 ? -19.652 -11.488 -32.100 1.00 20.56 ? 277 SER   A C   1 
ATOM   2322 O O   . SER   A 1 275 ? -18.672 -10.766 -31.909 1.00 23.01 ? 277 SER   A O   1 
ATOM   2323 C CB  . SER   A 1 275 ? -21.855 -10.777 -31.191 1.00 24.82 ? 277 SER   A CB  1 
ATOM   2324 O OG  . SER   A 1 275 ? -21.365 -9.451  -31.115 1.00 30.87 ? 277 SER   A OG  1 
ATOM   2325 N N   . ARG   A 1 276 ? -19.888 -12.084 -33.267 1.00 18.71 ? 278 ARG   A N   1 
ATOM   2326 C CA  . ARG   A 1 276 ? -19.104 -11.723 -34.444 1.00 17.34 ? 278 ARG   A CA  1 
ATOM   2327 C C   . ARG   A 1 276 ? -19.513 -10.335 -34.917 1.00 18.46 ? 278 ARG   A C   1 
ATOM   2328 O O   . ARG   A 1 276 ? -20.703 -9.996  -34.930 1.00 21.78 ? 278 ARG   A O   1 
ATOM   2329 C CB  . ARG   A 1 276 ? -19.303 -12.752 -35.562 1.00 20.82 ? 278 ARG   A CB  1 
ATOM   2330 C CG  . ARG   A 1 276 ? -18.309 -12.631 -36.725 1.00 21.11 ? 278 ARG   A CG  1 
ATOM   2331 C CD  . ARG   A 1 276 ? -18.082 -14.000 -37.403 1.00 20.40 ? 278 ARG   A CD  1 
ATOM   2332 N NE  . ARG   A 1 276 ? -16.873 -14.044 -38.240 1.00 22.99 ? 278 ARG   A NE  1 
ATOM   2333 C CZ  . ARG   A 1 276 ? -16.162 -15.153 -38.454 1.00 25.16 ? 278 ARG   A CZ  1 
ATOM   2334 N NH1 . ARG   A 1 276 ? -16.527 -16.289 -37.873 1.00 23.50 ? 278 ARG   A NH1 1 
ATOM   2335 N NH2 . ARG   A 1 276 ? -15.073 -15.131 -39.228 1.00 23.04 ? 278 ARG   A NH2 1 
ATOM   2336 N N   . LYS   A 1 277 ? -18.531 -9.518  -35.290 1.00 19.39 ? 279 LYS   A N   1 
ATOM   2337 C CA  . LYS   A 1 277 ? -18.785 -8.141  -35.695 1.00 17.59 ? 279 LYS   A CA  1 
ATOM   2338 C C   . LYS   A 1 277 ? -18.846 -8.023  -37.215 1.00 22.21 ? 279 LYS   A C   1 
ATOM   2339 O O   . LYS   A 1 277 ? -18.271 -8.834  -37.950 1.00 25.79 ? 279 LYS   A O   1 
ATOM   2340 C CB  . LYS   A 1 277 ? -17.701 -7.200  -35.147 1.00 18.12 ? 279 LYS   A CB  1 
ATOM   2341 C CG  . LYS   A 1 277 ? -17.472 -7.294  -33.644 1.00 19.54 ? 279 LYS   A CG  1 
ATOM   2342 C CD  . LYS   A 1 277 ? -18.772 -7.182  -32.863 1.00 18.99 ? 279 LYS   A CD  1 
ATOM   2343 C CE  . LYS   A 1 277 ? -18.552 -7.040  -31.369 1.00 19.73 ? 279 LYS   A CE  1 
ATOM   2344 N NZ  . LYS   A 1 277 ? -17.973 -8.260  -30.726 1.00 22.56 ? 279 LYS   A NZ  1 
ATOM   2345 N N   . ARG   A 1 278 ? -19.533 -6.983  -37.688 1.00 20.27 ? 280 ARG   A N   1 
ATOM   2346 C CA  . ARG   A 1 278 ? -19.490 -6.650  -39.109 1.00 21.54 ? 280 ARG   A CA  1 
ATOM   2347 C C   . ARG   A 1 278 ? -18.322 -5.708  -39.347 1.00 26.43 ? 280 ARG   A C   1 
ATOM   2348 O O   . ARG   A 1 278 ? -18.051 -4.827  -38.529 1.00 25.30 ? 280 ARG   A O   1 
ATOM   2349 C CB  . ARG   A 1 278 ? -20.802 -6.013  -39.577 1.00 27.88 ? 280 ARG   A CB  1 
ATOM   2350 C CG  . ARG   A 1 278 ? -22.003 -6.919  -39.337 1.00 27.28 ? 280 ARG   A CG  1 
ATOM   2351 C CD  . ARG   A 1 278 ? -23.260 -6.457  -40.038 1.00 29.85 ? 280 ARG   A CD  1 
ATOM   2352 N NE  . ARG   A 1 278 ? -24.418 -7.102  -39.436 1.00 31.70 ? 280 ARG   A NE  1 
ATOM   2353 C CZ  . ARG   A 1 278 ? -24.989 -8.220  -39.880 1.00 33.43 ? 280 ARG   A CZ  1 
ATOM   2354 N NH1 . ARG   A 1 278 ? -24.520 -8.835  -40.957 1.00 32.14 ? 280 ARG   A NH1 1 
ATOM   2355 N NH2 . ARG   A 1 278 ? -26.039 -8.724  -39.240 1.00 30.18 ? 280 ARG   A NH2 1 
ATOM   2356 N N   . TRP   A 1 279 ? -17.620 -5.905  -40.468 1.00 22.24 ? 281 TRP   A N   1 
ATOM   2357 C CA  . TRP   A 1 279 ? -16.410 -5.129  -40.713 1.00 21.52 ? 281 TRP   A CA  1 
ATOM   2358 C C   . TRP   A 1 279 ? -16.694 -3.645  -40.874 1.00 24.92 ? 281 TRP   A C   1 
ATOM   2359 O O   . TRP   A 1 279 ? -15.789 -2.832  -40.653 1.00 24.99 ? 281 TRP   A O   1 
ATOM   2360 C CB  . TRP   A 1 279 ? -15.679 -5.664  -41.949 1.00 23.39 ? 281 TRP   A CB  1 
ATOM   2361 C CG  . TRP   A 1 279 ? -15.147 -7.036  -41.744 1.00 24.27 ? 281 TRP   A CG  1 
ATOM   2362 C CD1 . TRP   A 1 279 ? -15.636 -8.198  -42.273 1.00 28.78 ? 281 TRP   A CD1 1 
ATOM   2363 C CD2 . TRP   A 1 279 ? -14.018 -7.404  -40.935 1.00 23.24 ? 281 TRP   A CD2 1 
ATOM   2364 N NE1 . TRP   A 1 279 ? -14.878 -9.267  -41.846 1.00 25.46 ? 281 TRP   A NE1 1 
ATOM   2365 C CE2 . TRP   A 1 279 ? -13.881 -8.807  -41.021 1.00 28.05 ? 281 TRP   A CE2 1 
ATOM   2366 C CE3 . TRP   A 1 279 ? -13.117 -6.685  -40.139 1.00 23.58 ? 281 TRP   A CE3 1 
ATOM   2367 C CZ2 . TRP   A 1 279 ? -12.873 -9.502  -40.352 1.00 24.29 ? 281 TRP   A CZ2 1 
ATOM   2368 C CZ3 . TRP   A 1 279 ? -12.116 -7.377  -39.473 1.00 23.72 ? 281 TRP   A CZ3 1 
ATOM   2369 C CH2 . TRP   A 1 279 ? -12.009 -8.774  -39.577 1.00 25.15 ? 281 TRP   A CH2 1 
ATOM   2370 N N   . GLU   A 1 280 ? -17.925 -3.275  -41.249 1.00 24.48 ? 282 GLU   A N   1 
ATOM   2371 C CA  . GLU   A 1 280 ? -18.274 -1.871  -41.425 1.00 28.22 ? 282 GLU   A CA  1 
ATOM   2372 C C   . GLU   A 1 280 ? -18.054 -1.042  -40.161 1.00 25.49 ? 282 GLU   A C   1 
ATOM   2373 O O   . GLU   A 1 280 ? -17.837 0.171   -40.258 1.00 26.62 ? 282 GLU   A O   1 
ATOM   2374 C CB  . GLU   A 1 280 ? -19.729 -1.752  -41.884 1.00 31.49 ? 282 GLU   A CB  1 
ATOM   2375 C CG  . GLU   A 1 280 ? -19.948 -2.137  -43.346 1.00 34.99 ? 282 GLU   A CG  1 
ATOM   2376 C CD  . GLU   A 1 280 ? -20.026 -3.641  -43.583 1.00 38.94 ? 282 GLU   A CD  1 
ATOM   2377 O OE1 . GLU   A 1 280 ? -20.207 -4.037  -44.754 1.00 40.56 ? 282 GLU   A OE1 1 
ATOM   2378 O OE2 . GLU   A 1 280 ? -19.912 -4.435  -42.619 1.00 34.92 ? 282 GLU   A OE2 1 
ATOM   2379 N N   . ARG   A 1 281 ? -18.077 -1.658  -38.981 1.00 28.04 ? 283 ARG   A N   1 
ATOM   2380 C CA  . ARG   A 1 281 ? -17.878 -0.876  -37.765 1.00 27.31 ? 283 ARG   A CA  1 
ATOM   2381 C C   . ARG   A 1 281 ? -16.483 -0.266  -37.685 1.00 29.81 ? 283 ARG   A C   1 
ATOM   2382 O O   . ARG   A 1 281 ? -16.281 0.686   -36.923 1.00 27.61 ? 283 ARG   A O   1 
ATOM   2383 C CB  . ARG   A 1 281 ? -18.137 -1.735  -36.524 1.00 31.13 ? 283 ARG   A CB  1 
ATOM   2384 C CG  . ARG   A 1 281 ? -17.068 -2.768  -36.231 1.00 31.89 ? 283 ARG   A CG  1 
ATOM   2385 C CD  . ARG   A 1 281 ? -16.879 -2.940  -34.729 1.00 39.26 ? 283 ARG   A CD  1 
ATOM   2386 N NE  . ARG   A 1 281 ? -18.120 -3.315  -34.064 1.00 40.98 ? 283 ARG   A NE  1 
ATOM   2387 C CZ  . ARG   A 1 281 ? -18.297 -3.309  -32.745 1.00 32.54 ? 283 ARG   A CZ  1 
ATOM   2388 N NH1 . ARG   A 1 281 ? -17.314 -2.935  -31.930 1.00 35.68 ? 283 ARG   A NH1 1 
ATOM   2389 N NH2 . ARG   A 1 281 ? -19.466 -3.667  -32.248 1.00 34.84 ? 283 ARG   A NH2 1 
ATOM   2390 N N   . PHE   A 1 282 ? -15.523 -0.771  -38.450 1.00 23.85 ? 284 PHE   A N   1 
ATOM   2391 C CA  . PHE   A 1 282 ? -14.169 -0.234  -38.405 1.00 24.97 ? 284 PHE   A CA  1 
ATOM   2392 C C   . PHE   A 1 282 ? -13.933 0.861   -39.435 1.00 23.85 ? 284 PHE   A C   1 
ATOM   2393 O O   . PHE   A 1 282 ? -12.836 1.435   -39.466 1.00 26.31 ? 284 PHE   A O   1 
ATOM   2394 C CB  . PHE   A 1 282 ? -13.149 -1.368  -38.576 1.00 23.19 ? 284 PHE   A CB  1 
ATOM   2395 C CG  . PHE   A 1 282 ? -13.294 -2.449  -37.541 1.00 24.28 ? 284 PHE   A CG  1 
ATOM   2396 C CD1 . PHE   A 1 282 ? -12.949 -2.205  -36.218 1.00 30.99 ? 284 PHE   A CD1 1 
ATOM   2397 C CD2 . PHE   A 1 282 ? -13.821 -3.687  -37.875 1.00 22.82 ? 284 PHE   A CD2 1 
ATOM   2398 C CE1 . PHE   A 1 282 ? -13.109 -3.183  -35.251 1.00 26.21 ? 284 PHE   A CE1 1 
ATOM   2399 C CE2 . PHE   A 1 282 ? -13.994 -4.666  -36.908 1.00 26.18 ? 284 PHE   A CE2 1 
ATOM   2400 C CZ  . PHE   A 1 282 ? -13.634 -4.414  -35.596 1.00 27.29 ? 284 PHE   A CZ  1 
ATOM   2401 N N   . VAL   A 1 283 ? -14.935 1.170   -40.256 1.00 24.35 ? 285 VAL   A N   1 
ATOM   2402 C CA  . VAL   A 1 283 ? -14.842 2.208   -41.277 1.00 24.42 ? 285 VAL   A CA  1 
ATOM   2403 C C   . VAL   A 1 283 ? -15.202 3.548   -40.656 1.00 23.21 ? 285 VAL   A C   1 
ATOM   2404 O O   . VAL   A 1 283 ? -16.207 3.660   -39.949 1.00 28.36 ? 285 VAL   A O   1 
ATOM   2405 C CB  . VAL   A 1 283 ? -15.778 1.899   -42.459 1.00 26.39 ? 285 VAL   A CB  1 
ATOM   2406 C CG1 . VAL   A 1 283 ? -15.624 2.965   -43.555 1.00 29.94 ? 285 VAL   A CG1 1 
ATOM   2407 C CG2 . VAL   A 1 283 ? -15.508 0.506   -43.005 1.00 26.73 ? 285 VAL   A CG2 1 
ATOM   2408 N N   . HIS   A 1 284 ? -14.405 4.575   -40.943 1.00 23.44 ? 286 HIS   A N   1 
ATOM   2409 C CA  . HIS   A 1 284 ? -14.723 5.929   -40.508 1.00 22.08 ? 286 HIS   A CA  1 
ATOM   2410 C C   . HIS   A 1 284 ? -14.238 6.903   -41.571 1.00 27.12 ? 286 HIS   A C   1 
ATOM   2411 O O   . HIS   A 1 284 ? -13.686 6.506   -42.602 1.00 28.81 ? 286 HIS   A O   1 
ATOM   2412 C CB  . HIS   A 1 284 ? -14.117 6.231   -39.129 1.00 27.74 ? 286 HIS   A CB  1 
ATOM   2413 C CG  . HIS   A 1 284 ? -12.664 5.885   -39.011 1.00 26.96 ? 286 HIS   A CG  1 
ATOM   2414 N ND1 . HIS   A 1 284 ? -11.678 6.537   -39.724 1.00 27.95 ? 286 HIS   A ND1 1 
ATOM   2415 C CD2 . HIS   A 1 284 ? -12.029 4.962   -38.251 1.00 28.06 ? 286 HIS   A CD2 1 
ATOM   2416 C CE1 . HIS   A 1 284 ? -10.500 6.022   -39.414 1.00 28.00 ? 286 HIS   A CE1 1 
ATOM   2417 N NE2 . HIS   A 1 284 ? -10.686 5.069   -38.517 1.00 25.53 ? 286 HIS   A NE2 1 
ATOM   2418 N N   . SER   A 1 285 ? -14.444 8.196   -41.313 1.00 29.85 ? 287 SER   A N   1 
ATOM   2419 C CA  . SER   A 1 285 ? -14.156 9.195   -42.335 1.00 26.06 ? 287 SER   A CA  1 
ATOM   2420 C C   . SER   A 1 285 ? -12.678 9.256   -42.708 1.00 27.58 ? 287 SER   A C   1 
ATOM   2421 O O   . SER   A 1 285 ? -12.348 9.722   -43.803 1.00 32.63 ? 287 SER   A O   1 
ATOM   2422 C CB  . SER   A 1 285 ? -14.641 10.571  -41.871 1.00 31.38 ? 287 SER   A CB  1 
ATOM   2423 O OG  . SER   A 1 285 ? -14.199 10.869  -40.558 1.00 41.63 ? 287 SER   A OG  1 
ATOM   2424 N N   . GLU   A 1 286 ? -11.781 8.780   -41.850 1.00 25.53 ? 288 GLU   A N   1 
ATOM   2425 C CA  . GLU   A 1 286 ? -10.355 8.894   -42.123 1.00 25.38 ? 288 GLU   A CA  1 
ATOM   2426 C C   . GLU   A 1 286 ? -9.768  7.652   -42.778 1.00 32.17 ? 288 GLU   A C   1 
ATOM   2427 O O   . GLU   A 1 286 ? -8.591  7.669   -43.155 1.00 34.77 ? 288 GLU   A O   1 
ATOM   2428 C CB  . GLU   A 1 286 ? -9.597  9.224   -40.835 1.00 27.39 ? 288 GLU   A CB  1 
ATOM   2429 C CG  . GLU   A 1 286 ? -9.810  10.657  -40.358 1.00 28.39 ? 288 GLU   A CG  1 
ATOM   2430 C CD  . GLU   A 1 286 ? -11.231 10.914  -39.862 1.00 39.37 ? 288 GLU   A CD  1 
ATOM   2431 O OE1 . GLU   A 1 286 ? -11.728 10.142  -39.007 1.00 35.70 ? 288 GLU   A OE1 1 
ATOM   2432 O OE2 . GLU   A 1 286 ? -11.856 11.886  -40.339 1.00 41.73 ? 288 GLU   A OE2 1 
ATOM   2433 N N   . ASN   A 1 287 ? -10.550 6.579   -42.937 1.00 27.00 ? 289 ASN   A N   1 
ATOM   2434 C CA  . ASN   A 1 287 ? -10.089 5.433   -43.712 1.00 22.48 ? 289 ASN   A CA  1 
ATOM   2435 C C   . ASN   A 1 287 ? -11.030 5.034   -44.843 1.00 25.62 ? 289 ASN   A C   1 
ATOM   2436 O O   . ASN   A 1 287 ? -10.714 4.096   -45.576 1.00 25.96 ? 289 ASN   A O   1 
ATOM   2437 C CB  . ASN   A 1 287 ? -9.841  4.213   -42.798 1.00 22.73 ? 289 ASN   A CB  1 
ATOM   2438 C CG  . ASN   A 1 287 ? -11.108 3.712   -42.093 1.00 19.99 ? 289 ASN   A CG  1 
ATOM   2439 O OD1 . ASN   A 1 287 ? -12.231 3.915   -42.549 1.00 23.45 ? 289 ASN   A OD1 1 
ATOM   2440 N ND2 . ASN   A 1 287 ? -10.910 3.021   -40.973 1.00 23.04 ? 289 ASN   A ND2 1 
ATOM   2441 N N   . GLN   A 1 288 ? -12.174 5.707   -45.016 1.00 24.08 ? 290 GLN   A N   1 
ATOM   2442 C CA  . GLN   A 1 288 ? -13.154 5.182   -45.965 1.00 26.10 ? 290 GLN   A CA  1 
ATOM   2443 C C   . GLN   A 1 288 ? -12.652 5.218   -47.404 1.00 25.98 ? 290 GLN   A C   1 
ATOM   2444 O O   . GLN   A 1 288 ? -13.171 4.477   -48.246 1.00 32.86 ? 290 GLN   A O   1 
ATOM   2445 C CB  . GLN   A 1 288 ? -14.479 5.933   -45.845 1.00 31.81 ? 290 GLN   A CB  1 
ATOM   2446 C CG  . GLN   A 1 288 ? -14.417 7.390   -46.211 1.00 36.37 ? 290 GLN   A CG  1 
ATOM   2447 C CD  . GLN   A 1 288 ? -15.772 8.061   -46.049 1.00 49.51 ? 290 GLN   A CD  1 
ATOM   2448 O OE1 . GLN   A 1 288 ? -16.138 8.944   -46.822 1.00 56.48 ? 290 GLN   A OE1 1 
ATOM   2449 N NE2 . GLN   A 1 288 ? -16.523 7.638   -45.040 1.00 56.86 ? 290 GLN   A NE2 1 
ATOM   2450 N N   . HIS   A 1 289 ? -11.650 6.041   -47.698 1.00 25.09 ? 291 HIS   A N   1 
ATOM   2451 C CA  . HIS   A 1 289 ? -11.084 6.078   -49.040 1.00 26.31 ? 291 HIS   A CA  1 
ATOM   2452 C C   . HIS   A 1 289 ? -10.290 4.820   -49.365 1.00 31.73 ? 291 HIS   A C   1 
ATOM   2453 O O   . HIS   A 1 289 ? -9.968  4.595   -50.537 1.00 31.29 ? 291 HIS   A O   1 
ATOM   2454 C CB  . HIS   A 1 289 ? -10.203 7.324   -49.213 1.00 31.06 ? 291 HIS   A CB  1 
ATOM   2455 C CG  . HIS   A 1 289 ? -9.015  7.366   -48.303 1.00 29.24 ? 291 HIS   A CG  1 
ATOM   2456 N ND1 . HIS   A 1 289 ? -9.123  7.589   -46.947 1.00 32.94 ? 291 HIS   A ND1 1 
ATOM   2457 C CD2 . HIS   A 1 289 ? -7.693  7.199   -48.552 1.00 33.26 ? 291 HIS   A CD2 1 
ATOM   2458 C CE1 . HIS   A 1 289 ? -7.920  7.566   -46.401 1.00 32.22 ? 291 HIS   A CE1 1 
ATOM   2459 N NE2 . HIS   A 1 289 ? -7.034  7.330   -47.353 1.00 32.42 ? 291 HIS   A NE2 1 
ATOM   2460 N N   . LEU   A 1 290 ? -9.986  3.999   -48.364 1.00 28.66 ? 292 LEU   A N   1 
ATOM   2461 C CA  . LEU   A 1 290 ? -9.259  2.747   -48.542 1.00 24.03 ? 292 LEU   A CA  1 
ATOM   2462 C C   . LEU   A 1 290 ? -10.167 1.532   -48.469 1.00 24.84 ? 292 LEU   A C   1 
ATOM   2463 O O   . LEU   A 1 290 ? -9.692  0.404   -48.675 1.00 25.97 ? 292 LEU   A O   1 
ATOM   2464 C CB  . LEU   A 1 290 ? -8.156  2.622   -47.484 1.00 27.44 ? 292 LEU   A CB  1 
ATOM   2465 C CG  . LEU   A 1 290 ? -7.139  3.762   -47.390 1.00 28.65 ? 292 LEU   A CG  1 
ATOM   2466 C CD1 . LEU   A 1 290 ? -6.169  3.506   -46.277 1.00 28.47 ? 292 LEU   A CD1 1 
ATOM   2467 C CD2 . LEU   A 1 290 ? -6.384  3.948   -48.699 1.00 31.59 ? 292 LEU   A CD2 1 
ATOM   2468 N N   . VAL   A 1 291 ? -11.456 1.730   -48.195 1.00 25.09 ? 293 VAL   A N   1 
ATOM   2469 C CA  . VAL   A 1 291 ? -12.402 0.647   -47.980 1.00 26.12 ? 293 VAL   A CA  1 
ATOM   2470 C C   . VAL   A 1 291 ? -13.412 0.628   -49.117 1.00 27.41 ? 293 VAL   A C   1 
ATOM   2471 O O   . VAL   A 1 291 ? -13.852 1.677   -49.605 1.00 34.61 ? 293 VAL   A O   1 
ATOM   2472 C CB  . VAL   A 1 291 ? -13.093 0.787   -46.608 1.00 29.63 ? 293 VAL   A CB  1 
ATOM   2473 C CG1 . VAL   A 1 291 ? -14.060 -0.364  -46.368 1.00 35.34 ? 293 VAL   A CG1 1 
ATOM   2474 C CG2 . VAL   A 1 291 ? -12.044 0.840   -45.505 1.00 30.30 ? 293 VAL   A CG2 1 
ATOM   2475 N N   . SER   A 1 292 ? -13.771 -0.573  -49.542 1.00 30.97 ? 294 SER   A N   1 
ATOM   2476 C CA  . SER   A 1 292 ? -14.757 -0.833  -50.566 1.00 24.30 ? 294 SER   A CA  1 
ATOM   2477 C C   . SER   A 1 292 ? -15.458 -2.121  -50.189 1.00 29.13 ? 294 SER   A C   1 
ATOM   2478 O O   . SER   A 1 292 ? -14.927 -2.902  -49.383 1.00 24.96 ? 294 SER   A O   1 
ATOM   2479 C CB  . SER   A 1 292 ? -14.102 -0.985  -51.945 1.00 26.11 ? 294 SER   A CB  1 
ATOM   2480 O OG  . SER   A 1 292 ? -13.116 -1.999  -51.876 1.00 27.97 ? 294 SER   A OG  1 
ATOM   2481 N N   . PRO   A 1 293 ? -16.637 -2.388  -50.742 1.00 27.43 ? 295 PRO   A N   1 
ATOM   2482 C CA  . PRO   A 1 293 ? -17.254 -3.703  -50.512 1.00 29.33 ? 295 PRO   A CA  1 
ATOM   2483 C C   . PRO   A 1 293 ? -16.324 -4.848  -50.872 1.00 26.18 ? 295 PRO   A C   1 
ATOM   2484 O O   . PRO   A 1 293 ? -16.287 -5.870  -50.173 1.00 25.41 ? 295 PRO   A O   1 
ATOM   2485 C CB  . PRO   A 1 293 ? -18.501 -3.662  -51.411 1.00 28.91 ? 295 PRO   A CB  1 
ATOM   2486 C CG  . PRO   A 1 293 ? -18.819 -2.215  -51.527 1.00 35.35 ? 295 PRO   A CG  1 
ATOM   2487 C CD  . PRO   A 1 293 ? -17.501 -1.512  -51.566 1.00 29.47 ? 295 PRO   A CD  1 
ATOM   2488 N N   . GLU   A 1 294 ? -15.541 -4.676  -51.944 1.00 27.43 ? 296 GLU   A N   1 
ATOM   2489 C CA  . GLU   A 1 294 ? -14.601 -5.711  -52.365 1.00 22.10 ? 296 GLU   A CA  1 
ATOM   2490 C C   . GLU   A 1 294 ? -13.511 -5.936  -51.321 1.00 25.54 ? 296 GLU   A C   1 
ATOM   2491 O O   . GLU   A 1 294 ? -13.137 -7.082  -51.053 1.00 22.56 ? 296 GLU   A O   1 
ATOM   2492 C CB  . GLU   A 1 294 ? -13.982 -5.339  -53.713 1.00 26.42 ? 296 GLU   A CB  1 
ATOM   2493 C CG  . GLU   A 1 294 ? -14.953 -5.399  -54.898 1.00 28.34 ? 296 GLU   A CG  1 
ATOM   2494 C CD  . GLU   A 1 294 ? -15.887 -4.203  -54.973 1.00 43.25 ? 296 GLU   A CD  1 
ATOM   2495 O OE1 . GLU   A 1 294 ? -15.579 -3.162  -54.350 1.00 32.78 ? 296 GLU   A OE1 1 
ATOM   2496 O OE2 . GLU   A 1 294 ? -16.933 -4.302  -55.662 1.00 50.86 ? 296 GLU   A OE2 1 
ATOM   2497 N N   . ALA   A 1 295 ? -12.989 -4.857  -50.730 1.00 21.17 ? 297 ALA   A N   1 
ATOM   2498 C CA  . ALA   A 1 295 ? -11.948 -4.994  -49.711 1.00 21.21 ? 297 ALA   A CA  1 
ATOM   2499 C C   . ALA   A 1 295 ? -12.473 -5.712  -48.481 1.00 20.83 ? 297 ALA   A C   1 
ATOM   2500 O O   . ALA   A 1 295 ? -11.777 -6.556  -47.904 1.00 22.11 ? 297 ALA   A O   1 
ATOM   2501 C CB  . ALA   A 1 295 ? -11.413 -3.621  -49.316 1.00 21.47 ? 297 ALA   A CB  1 
ATOM   2502 N N   . LEU   A 1 296 ? -13.697 -5.388  -48.059 1.00 22.02 ? 298 LEU   A N   1 
ATOM   2503 C CA  . LEU   A 1 296 ? -14.220 -6.014  -46.854 1.00 21.22 ? 298 LEU   A CA  1 
ATOM   2504 C C   . LEU   A 1 296 ? -14.516 -7.489  -47.094 1.00 23.23 ? 298 LEU   A C   1 
ATOM   2505 O O   . LEU   A 1 296 ? -14.255 -8.326  -46.219 1.00 23.03 ? 298 LEU   A O   1 
ATOM   2506 C CB  . LEU   A 1 296 ? -15.464 -5.269  -46.370 1.00 23.25 ? 298 LEU   A CB  1 
ATOM   2507 C CG  . LEU   A 1 296 ? -15.201 -3.826  -45.947 1.00 24.02 ? 298 LEU   A CG  1 
ATOM   2508 C CD1 . LEU   A 1 296 ? -16.451 -3.268  -45.302 1.00 26.24 ? 298 LEU   A CD1 1 
ATOM   2509 C CD2 . LEU   A 1 296 ? -14.019 -3.724  -44.996 1.00 30.95 ? 298 LEU   A CD2 1 
ATOM   2510 N N   . ASP   A 1 297 ? -15.034 -7.830  -48.275 1.00 21.62 ? 299 ASP   A N   1 
ATOM   2511 C CA  . ASP   A 1 297 ? -15.278 -9.238  -48.574 1.00 25.17 ? 299 ASP   A CA  1 
ATOM   2512 C C   . ASP   A 1 297 ? -13.976 -10.020 -48.630 1.00 25.94 ? 299 ASP   A C   1 
ATOM   2513 O O   . ASP   A 1 297 ? -13.894 -11.130 -48.094 1.00 22.52 ? 299 ASP   A O   1 
ATOM   2514 C CB  . ASP   A 1 297 ? -16.030 -9.411  -49.891 1.00 23.56 ? 299 ASP   A CB  1 
ATOM   2515 C CG  . ASP   A 1 297 ? -16.327 -10.875 -50.183 1.00 29.81 ? 299 ASP   A CG  1 
ATOM   2516 O OD1 . ASP   A 1 297 ? -17.039 -11.516 -49.371 1.00 33.40 ? 299 ASP   A OD1 1 
ATOM   2517 O OD2 . ASP   A 1 297 ? -15.836 -11.401 -51.194 1.00 29.88 ? 299 ASP   A OD2 1 
ATOM   2518 N N   . PHE   A 1 298 ? -12.959 -9.466  -49.296 1.00 22.81 ? 300 PHE   A N   1 
ATOM   2519 C CA  . PHE   A 1 298 ? -11.662 -10.133 -49.370 1.00 20.46 ? 300 PHE   A CA  1 
ATOM   2520 C C   . PHE   A 1 298 ? -11.075 -10.337 -47.973 1.00 22.27 ? 300 PHE   A C   1 
ATOM   2521 O O   . PHE   A 1 298 ? -10.642 -11.445 -47.622 1.00 19.16 ? 300 PHE   A O   1 
ATOM   2522 C CB  . PHE   A 1 298 ? -10.726 -9.319  -50.270 1.00 18.54 ? 300 PHE   A CB  1 
ATOM   2523 C CG  . PHE   A 1 298 ? -9.319  -9.855  -50.350 1.00 20.46 ? 300 PHE   A CG  1 
ATOM   2524 C CD1 . PHE   A 1 298 ? -9.087  -11.193 -50.620 1.00 24.58 ? 300 PHE   A CD1 1 
ATOM   2525 C CD2 . PHE   A 1 298 ? -8.238  -9.004  -50.215 1.00 26.49 ? 300 PHE   A CD2 1 
ATOM   2526 C CE1 . PHE   A 1 298 ? -7.793  -11.689 -50.715 1.00 27.42 ? 300 PHE   A CE1 1 
ATOM   2527 C CE2 . PHE   A 1 298 ? -6.929  -9.500  -50.305 1.00 24.13 ? 300 PHE   A CE2 1 
ATOM   2528 C CZ  . PHE   A 1 298 ? -6.724  -10.848 -50.554 1.00 26.18 ? 300 PHE   A CZ  1 
ATOM   2529 N N   . LEU   A 1 299 ? -11.093 -9.288  -47.146 1.00 19.27 ? 301 LEU   A N   1 
ATOM   2530 C CA  . LEU   A 1 299 ? -10.571 -9.397  -45.783 1.00 20.54 ? 301 LEU   A CA  1 
ATOM   2531 C C   . LEU   A 1 299 ? -11.324 -10.461 -44.999 1.00 20.47 ? 301 LEU   A C   1 
ATOM   2532 O O   . LEU   A 1 299 ? -10.725 -11.279 -44.290 1.00 19.71 ? 301 LEU   A O   1 
ATOM   2533 C CB  . LEU   A 1 299 ? -10.676 -8.045  -45.076 1.00 19.54 ? 301 LEU   A CB  1 
ATOM   2534 C CG  . LEU   A 1 299 ? -10.225 -8.057  -43.611 1.00 21.22 ? 301 LEU   A CG  1 
ATOM   2535 C CD1 . LEU   A 1 299 ? -8.712  -8.296  -43.551 1.00 18.49 ? 301 LEU   A CD1 1 
ATOM   2536 C CD2 . LEU   A 1 299 ? -10.614 -6.747  -42.911 1.00 22.15 ? 301 LEU   A CD2 1 
ATOM   2537 N N   . ASP   A 1 300 ? -12.650 -10.450 -45.117 1.00 19.11 ? 302 ASP   A N   1 
ATOM   2538 C CA  . ASP   A 1 300 ? -13.489 -11.419 -44.426 1.00 17.93 ? 302 ASP   A CA  1 
ATOM   2539 C C   . ASP   A 1 300 ? -13.119 -12.851 -44.777 1.00 22.10 ? 302 ASP   A C   1 
ATOM   2540 O O   . ASP   A 1 300 ? -13.298 -13.753 -43.951 1.00 20.85 ? 302 ASP   A O   1 
ATOM   2541 C CB  . ASP   A 1 300 ? -14.944 -11.158 -44.808 1.00 17.49 ? 302 ASP   A CB  1 
ATOM   2542 C CG  . ASP   A 1 300 ? -15.915 -11.975 -43.993 1.00 28.36 ? 302 ASP   A CG  1 
ATOM   2543 O OD1 . ASP   A 1 300 ? -15.835 -11.921 -42.748 1.00 25.89 ? 302 ASP   A OD1 1 
ATOM   2544 O OD2 . ASP   A 1 300 ? -16.770 -12.646 -44.605 1.00 30.58 ? 302 ASP   A OD2 1 
ATOM   2545 N N   . LYS   A 1 301 ? -12.668 -13.092 -46.009 1.00 18.55 ? 303 LYS   A N   1 
ATOM   2546 C CA  . LYS   A 1 301 ? -12.345 -14.441 -46.451 1.00 18.67 ? 303 LYS   A CA  1 
ATOM   2547 C C   . LYS   A 1 301 ? -10.908 -14.854 -46.137 1.00 18.41 ? 303 LYS   A C   1 
ATOM   2548 O O   . LYS   A 1 301 ? -10.572 -16.036 -46.285 1.00 20.17 ? 303 LYS   A O   1 
ATOM   2549 C CB  . LYS   A 1 301 ? -12.611 -14.574 -47.958 1.00 20.33 ? 303 LYS   A CB  1 
ATOM   2550 C CG  . LYS   A 1 301 ? -14.092 -14.468 -48.291 1.00 22.41 ? 303 LYS   A CG  1 
ATOM   2551 C CD  . LYS   A 1 301 ? -14.300 -14.380 -49.801 1.00 29.90 ? 303 LYS   A CD  1 
ATOM   2552 C CE  . LYS   A 1 301 ? -15.725 -14.759 -50.195 1.00 38.52 ? 303 LYS   A CE  1 
ATOM   2553 N NZ  . LYS   A 1 301 ? -16.742 -13.966 -49.445 1.00 41.76 ? 303 LYS   A NZ  1 
ATOM   2554 N N   . LEU   A 1 302 ? -10.054 -13.916 -45.726 1.00 18.87 ? 304 LEU   A N   1 
ATOM   2555 C CA  . LEU   A 1 302 ? -8.739  -14.258 -45.192 1.00 17.58 ? 304 LEU   A CA  1 
ATOM   2556 C C   . LEU   A 1 302 ? -8.801  -14.537 -43.700 1.00 19.86 ? 304 LEU   A C   1 
ATOM   2557 O O   . LEU   A 1 302 ? -8.188  -15.496 -43.223 1.00 19.95 ? 304 LEU   A O   1 
ATOM   2558 C CB  . LEU   A 1 302 ? -7.741  -13.128 -45.439 1.00 15.81 ? 304 LEU   A CB  1 
ATOM   2559 C CG  . LEU   A 1 302 ? -7.398  -12.795 -46.893 1.00 17.67 ? 304 LEU   A CG  1 
ATOM   2560 C CD1 . LEU   A 1 302 ? -6.599  -11.496 -46.926 1.00 22.06 ? 304 LEU   A CD1 1 
ATOM   2561 C CD2 . LEU   A 1 302 ? -6.657  -13.940 -47.577 1.00 20.25 ? 304 LEU   A CD2 1 
ATOM   2562 N N   . LEU   A 1 303 ? -9.516  -13.700 -42.940 1.00 18.00 ? 305 LEU   A N   1 
ATOM   2563 C CA  . LEU   A 1 303 ? -9.504  -13.793 -41.479 1.00 16.49 ? 305 LEU   A CA  1 
ATOM   2564 C C   . LEU   A 1 303 ? -10.604 -14.747 -41.024 1.00 20.26 ? 305 LEU   A C   1 
ATOM   2565 O O   . LEU   A 1 303 ? -11.667 -14.338 -40.546 1.00 22.22 ? 305 LEU   A O   1 
ATOM   2566 C CB  . LEU   A 1 303 ? -9.658  -12.414 -40.850 1.00 19.28 ? 305 LEU   A CB  1 
ATOM   2567 C CG  . LEU   A 1 303 ? -8.486  -11.463 -41.097 1.00 16.99 ? 305 LEU   A CG  1 
ATOM   2568 C CD1 . LEU   A 1 303 ? -8.748  -10.110 -40.427 1.00 18.59 ? 305 LEU   A CD1 1 
ATOM   2569 C CD2 . LEU   A 1 303 ? -7.153  -12.089 -40.602 1.00 17.62 ? 305 LEU   A CD2 1 
ATOM   2570 N N   . ARG   A 1 304 ? -10.345 -16.046 -41.208 1.00 17.03 ? 306 ARG   A N   1 
ATOM   2571 C CA  . ARG   A 1 304 ? -11.200 -17.113 -40.694 1.00 16.65 ? 306 ARG   A CA  1 
ATOM   2572 C C   . ARG   A 1 304 ? -10.448 -17.861 -39.608 1.00 15.89 ? 306 ARG   A C   1 
ATOM   2573 O O   . ARG   A 1 304 ? -9.256  -18.124 -39.759 1.00 16.70 ? 306 ARG   A O   1 
ATOM   2574 C CB  . ARG   A 1 304 ? -11.581 -18.131 -41.779 1.00 21.53 ? 306 ARG   A CB  1 
ATOM   2575 C CG  . ARG   A 1 304 ? -11.931 -17.579 -43.130 1.00 24.58 ? 306 ARG   A CG  1 
ATOM   2576 C CD  . ARG   A 1 304 ? -13.115 -16.648 -43.067 1.00 22.52 ? 306 ARG   A CD  1 
ATOM   2577 N NE  . ARG   A 1 304 ? -14.297 -17.234 -42.444 1.00 24.31 ? 306 ARG   A NE  1 
ATOM   2578 C CZ  . ARG   A 1 304 ? -15.470 -16.612 -42.380 1.00 32.78 ? 306 ARG   A CZ  1 
ATOM   2579 N NH1 . ARG   A 1 304 ? -16.509 -17.193 -41.797 1.00 29.42 ? 306 ARG   A NH1 1 
ATOM   2580 N NH2 . ARG   A 1 304 ? -15.601 -15.400 -42.902 1.00 32.12 ? 306 ARG   A NH2 1 
ATOM   2581 N N   . TYR   A 1 305 ? -11.138 -18.226 -38.522 1.00 17.50 ? 307 TYR   A N   1 
ATOM   2582 C CA  . TYR   A 1 305 ? -10.509 -19.091 -37.525 1.00 17.10 ? 307 TYR   A CA  1 
ATOM   2583 C C   . TYR   A 1 305 ? -9.988  -20.368 -38.163 1.00 17.96 ? 307 TYR   A C   1 
ATOM   2584 O O   . TYR   A 1 305 ? -8.820  -20.732 -38.000 1.00 18.49 ? 307 TYR   A O   1 
ATOM   2585 C CB  . TYR   A 1 305 ? -11.499 -19.483 -36.429 1.00 19.50 ? 307 TYR   A CB  1 
ATOM   2586 C CG  . TYR   A 1 305 ? -11.840 -18.438 -35.404 1.00 18.16 ? 307 TYR   A CG  1 
ATOM   2587 C CD1 . TYR   A 1 305 ? -10.879 -17.957 -34.531 1.00 17.32 ? 307 TYR   A CD1 1 
ATOM   2588 C CD2 . TYR   A 1 305 ? -13.146 -17.986 -35.271 1.00 17.76 ? 307 TYR   A CD2 1 
ATOM   2589 C CE1 . TYR   A 1 305 ? -11.192 -17.003 -33.561 1.00 16.78 ? 307 TYR   A CE1 1 
ATOM   2590 C CE2 . TYR   A 1 305 ? -13.475 -17.057 -34.306 1.00 15.79 ? 307 TYR   A CE2 1 
ATOM   2591 C CZ  . TYR   A 1 305 ? -12.498 -16.567 -33.458 1.00 16.61 ? 307 TYR   A CZ  1 
ATOM   2592 O OH  . TYR   A 1 305 ? -12.822 -15.646 -32.503 1.00 19.17 ? 307 TYR   A OH  1 
ATOM   2593 N N   . ASP   A 1 306 ? -10.855 -21.062 -38.895 1.00 18.11 ? 308 ASP   A N   1 
ATOM   2594 C CA  . ASP   A 1 306 ? -10.521 -22.361 -39.467 1.00 15.98 ? 308 ASP   A CA  1 
ATOM   2595 C C   . ASP   A 1 306 ? -9.517  -22.185 -40.600 1.00 16.94 ? 308 ASP   A C   1 
ATOM   2596 O O   . ASP   A 1 306 ? -9.831  -21.598 -41.642 1.00 18.67 ? 308 ASP   A O   1 
ATOM   2597 C CB  . ASP   A 1 306 ? -11.794 -23.041 -39.951 1.00 16.43 ? 308 ASP   A CB  1 
ATOM   2598 C CG  . ASP   A 1 306 ? -11.579 -24.506 -40.284 1.00 23.07 ? 308 ASP   A CG  1 
ATOM   2599 O OD1 . ASP   A 1 306 ? -10.410 -24.938 -40.392 1.00 23.56 ? 308 ASP   A OD1 1 
ATOM   2600 O OD2 . ASP   A 1 306 ? -12.594 -25.221 -40.425 1.00 26.17 ? 308 ASP   A OD2 1 
ATOM   2601 N N   . HIS   A 1 307 ? -8.297  -22.676 -40.386 1.00 17.51 ? 309 HIS   A N   1 
ATOM   2602 C CA  . HIS   A 1 307 ? -7.255  -22.524 -41.399 1.00 15.67 ? 309 HIS   A CA  1 
ATOM   2603 C C   . HIS   A 1 307 ? -7.661  -23.172 -42.720 1.00 21.12 ? 309 HIS   A C   1 
ATOM   2604 O O   . HIS   A 1 307 ? -7.261  -22.695 -43.791 1.00 21.39 ? 309 HIS   A O   1 
ATOM   2605 C CB  . HIS   A 1 307 ? -5.934  -23.091 -40.875 1.00 17.37 ? 309 HIS   A CB  1 
ATOM   2606 C CG  . HIS   A 1 307 ? -6.040  -24.485 -40.337 1.00 20.93 ? 309 HIS   A CG  1 
ATOM   2607 N ND1 . HIS   A 1 307 ? -6.482  -24.762 -39.062 1.00 19.07 ? 309 HIS   A ND1 1 
ATOM   2608 C CD2 . HIS   A 1 307 ? -5.763  -25.684 -40.907 1.00 22.41 ? 309 HIS   A CD2 1 
ATOM   2609 C CE1 . HIS   A 1 307 ? -6.473  -26.070 -38.868 1.00 21.53 ? 309 HIS   A CE1 1 
ATOM   2610 N NE2 . HIS   A 1 307 ? -6.040  -26.652 -39.973 1.00 22.22 ? 309 HIS   A NE2 1 
ATOM   2611 N N   . GLN   A 1 308 ? -8.524  -24.194 -42.669 1.00 19.82 ? 310 GLN   A N   1 
ATOM   2612 C CA  . GLN   A 1 308 ? -9.009  -24.862 -43.871 1.00 20.82 ? 310 GLN   A CA  1 
ATOM   2613 C C   . GLN   A 1 308 ? -10.059 -24.060 -44.631 1.00 24.59 ? 310 GLN   A C   1 
ATOM   2614 O O   . GLN   A 1 308 ? -10.435 -24.462 -45.739 1.00 27.78 ? 310 GLN   A O   1 
ATOM   2615 C CB  . GLN   A 1 308 ? -9.590  -26.236 -43.523 1.00 22.23 ? 310 GLN   A CB  1 
ATOM   2616 C CG  . GLN   A 1 308 ? -8.548  -27.240 -43.081 1.00 23.53 ? 310 GLN   A CG  1 
ATOM   2617 C CD  . GLN   A 1 308 ? -9.140  -28.605 -42.753 1.00 30.14 ? 310 GLN   A CD  1 
ATOM   2618 O OE1 . GLN   A 1 308 ? -10.343 -28.837 -42.923 1.00 29.57 ? 310 GLN   A OE1 1 
ATOM   2619 N NE2 . GLN   A 1 308 ? -8.294  -29.515 -42.284 1.00 27.24 ? 310 GLN   A NE2 1 
ATOM   2620 N N   . SER   A 1 309 ? -10.527 -22.944 -44.083 1.00 20.64 ? 311 SER   A N   1 
ATOM   2621 C CA  . SER   A 1 309 ? -11.561 -22.137 -44.716 1.00 20.58 ? 311 SER   A CA  1 
ATOM   2622 C C   . SER   A 1 309 ? -11.033 -20.860 -45.349 1.00 18.58 ? 311 SER   A C   1 
ATOM   2623 O O   . SER   A 1 309 ? -11.799 -20.159 -46.020 1.00 24.11 ? 311 SER   A O   1 
ATOM   2624 C CB  . SER   A 1 309 ? -12.628 -21.770 -43.690 1.00 23.15 ? 311 SER   A CB  1 
ATOM   2625 O OG  . SER   A 1 309 ? -13.280 -22.939 -43.234 1.00 24.39 ? 311 SER   A OG  1 
ATOM   2626 N N   . ARG   A 1 310 ? -9.764  -20.525 -45.133 1.00 17.18 ? 312 ARG   A N   1 
ATOM   2627 C CA  . ARG   A 1 310 ? -9.201  -19.295 -45.666 1.00 18.25 ? 312 ARG   A CA  1 
ATOM   2628 C C   . ARG   A 1 310 ? -8.941  -19.415 -47.160 1.00 16.34 ? 312 ARG   A C   1 
ATOM   2629 O O   . ARG   A 1 310 ? -8.643  -20.500 -47.673 1.00 18.60 ? 312 ARG   A O   1 
ATOM   2630 C CB  . ARG   A 1 310 ? -7.891  -18.964 -44.946 1.00 15.46 ? 312 ARG   A CB  1 
ATOM   2631 C CG  . ARG   A 1 310 ? -8.060  -18.789 -43.445 1.00 15.35 ? 312 ARG   A CG  1 
ATOM   2632 C CD  . ARG   A 1 310 ? -6.712  -18.611 -42.729 1.00 13.94 ? 312 ARG   A CD  1 
ATOM   2633 N NE  . ARG   A 1 310 ? -6.907  -18.852 -41.293 1.00 16.51 ? 312 ARG   A NE  1 
ATOM   2634 C CZ  . ARG   A 1 310 ? -5.986  -19.346 -40.480 1.00 15.28 ? 312 ARG   A CZ  1 
ATOM   2635 N NH1 . ARG   A 1 310 ? -4.754  -19.613 -40.919 1.00 16.41 ? 312 ARG   A NH1 1 
ATOM   2636 N NH2 . ARG   A 1 310 ? -6.300  -19.569 -39.214 1.00 17.16 ? 312 ARG   A NH2 1 
ATOM   2637 N N   . LEU   A 1 311 ? -9.046  -18.282 -47.859 1.00 18.17 ? 313 LEU   A N   1 
ATOM   2638 C CA  . LEU   A 1 311 ? -8.626  -18.245 -49.255 1.00 17.16 ? 313 LEU   A CA  1 
ATOM   2639 C C   . LEU   A 1 311 ? -7.197  -18.744 -49.369 1.00 19.25 ? 313 LEU   A C   1 
ATOM   2640 O O   . LEU   A 1 311 ? -6.357  -18.463 -48.503 1.00 20.03 ? 313 LEU   A O   1 
ATOM   2641 C CB  . LEU   A 1 311 ? -8.694  -16.816 -49.804 1.00 19.92 ? 313 LEU   A CB  1 
ATOM   2642 C CG  . LEU   A 1 311 ? -10.065 -16.188 -50.000 1.00 24.54 ? 313 LEU   A CG  1 
ATOM   2643 C CD1 . LEU   A 1 311 ? -9.881  -14.774 -50.493 1.00 24.00 ? 313 LEU   A CD1 1 
ATOM   2644 C CD2 . LEU   A 1 311 ? -10.855 -17.012 -51.000 1.00 27.99 ? 313 LEU   A CD2 1 
ATOM   2645 N N   . THR   A 1 312 ? -6.931  -19.503 -50.429 1.00 17.20 ? 314 THR   A N   1 
ATOM   2646 C CA  . THR   A 1 312 ? -5.547  -19.762 -50.798 1.00 18.42 ? 314 THR   A CA  1 
ATOM   2647 C C   . THR   A 1 312 ? -4.988  -18.541 -51.509 1.00 18.88 ? 314 THR   A C   1 
ATOM   2648 O O   . THR   A 1 312 ? -5.727  -17.647 -51.915 1.00 19.88 ? 314 THR   A O   1 
ATOM   2649 C CB  . THR   A 1 312 ? -5.417  -20.992 -51.695 1.00 22.59 ? 314 THR   A CB  1 
ATOM   2650 O OG1 . THR   A 1 312 ? -6.042  -20.739 -52.964 1.00 22.75 ? 314 THR   A OG1 1 
ATOM   2651 C CG2 . THR   A 1 312 ? -6.064  -22.212 -51.049 1.00 22.27 ? 314 THR   A CG2 1 
ATOM   2652 N N   . ALA   A 1 313 ? -3.654  -18.490 -51.633 1.00 17.69 ? 315 ALA   A N   1 
ATOM   2653 C CA  . ALA   A 1 313 ? -3.058  -17.362 -52.340 1.00 16.56 ? 315 ALA   A CA  1 
ATOM   2654 C C   . ALA   A 1 313 ? -3.594  -17.248 -53.765 1.00 19.46 ? 315 ALA   A C   1 
ATOM   2655 O O   . ALA   A 1 313 ? -3.871  -16.142 -54.234 1.00 22.58 ? 315 ALA   A O   1 
ATOM   2656 C CB  . ALA   A 1 313 ? -1.529  -17.478 -52.333 1.00 17.70 ? 315 ALA   A CB  1 
ATOM   2657 N N   . ARG   A 1 314 ? -3.761  -18.384 -54.459 1.00 21.13 ? 316 ARG   A N   1 
ATOM   2658 C CA  . ARG   A 1 314 ? -4.262  -18.372 -55.832 1.00 23.26 ? 316 ARG   A CA  1 
ATOM   2659 C C   . ARG   A 1 314 ? -5.715  -17.928 -55.879 1.00 24.80 ? 316 ARG   A C   1 
ATOM   2660 O O   . ARG   A 1 314 ? -6.098  -17.114 -56.731 1.00 28.33 ? 316 ARG   A O   1 
ATOM   2661 C CB  . ARG   A 1 314 ? -4.110  -19.761 -56.450 1.00 28.47 ? 316 ARG   A CB  1 
ATOM   2662 C CG  . ARG   A 1 314 ? -4.236  -19.770 -57.946 1.00 38.58 ? 316 ARG   A CG  1 
ATOM   2663 C CD  . ARG   A 1 314 ? -2.999  -19.144 -58.574 1.00 41.72 ? 316 ARG   A CD  1 
ATOM   2664 N NE  . ARG   A 1 314 ? -3.189  -18.937 -60.002 1.00 46.96 ? 316 ARG   A NE  1 
ATOM   2665 C CZ  . ARG   A 1 314 ? -2.806  -19.797 -60.939 1.00 54.11 ? 316 ARG   A CZ  1 
ATOM   2666 N NH1 . ARG   A 1 314 ? -2.198  -20.926 -60.600 1.00 52.23 ? 316 ARG   A NH1 1 
ATOM   2667 N NH2 . ARG   A 1 314 ? -3.024  -19.521 -62.215 1.00 62.20 ? 316 ARG   A NH2 1 
ATOM   2668 N N   . GLU   A 1 315 ? -6.548  -18.462 -54.977 1.00 25.18 ? 317 GLU   A N   1 
ATOM   2669 C CA  . GLU   A 1 315 ? -7.930  -17.998 -54.899 1.00 26.21 ? 317 GLU   A CA  1 
ATOM   2670 C C   . GLU   A 1 315 ? -7.984  -16.509 -54.616 1.00 21.18 ? 317 GLU   A C   1 
ATOM   2671 O O   . GLU   A 1 315 ? -8.817  -15.791 -55.175 1.00 26.80 ? 317 GLU   A O   1 
ATOM   2672 C CB  . GLU   A 1 315 ? -8.697  -18.742 -53.808 1.00 26.43 ? 317 GLU   A CB  1 
ATOM   2673 C CG  . GLU   A 1 315 ? -9.027  -20.172 -54.098 1.00 30.65 ? 317 GLU   A CG  1 
ATOM   2674 C CD  . GLU   A 1 315 ? -9.795  -20.797 -52.949 1.00 29.93 ? 317 GLU   A CD  1 
ATOM   2675 O OE1 . GLU   A 1 315 ? -9.395  -20.614 -51.770 1.00 23.77 ? 317 GLU   A OE1 1 
ATOM   2676 O OE2 . GLU   A 1 315 ? -10.823 -21.439 -53.227 1.00 28.32 ? 317 GLU   A OE2 1 
ATOM   2677 N N   . ALA   A 1 316 ? -7.102  -16.028 -53.732 1.00 22.90 ? 318 ALA   A N   1 
ATOM   2678 C CA  . ALA   A 1 316 ? -7.102  -14.613 -53.382 1.00 16.70 ? 318 ALA   A CA  1 
ATOM   2679 C C   . ALA   A 1 316 ? -6.806  -13.743 -54.601 1.00 24.20 ? 318 ALA   A C   1 
ATOM   2680 O O   . ALA   A 1 316 ? -7.379  -12.655 -54.751 1.00 24.79 ? 318 ALA   A O   1 
ATOM   2681 C CB  . ALA   A 1 316 ? -6.076  -14.342 -52.275 1.00 20.51 ? 318 ALA   A CB  1 
ATOM   2682 N N   . MET   A 1 317 ? -5.907  -14.199 -55.475 1.00 22.33 ? 319 MET   A N   1 
ATOM   2683 C CA  A MET   A 1 317 ? -5.595  -13.398 -56.651 0.38 23.60 ? 319 MET   A CA  1 
ATOM   2684 C CA  B MET   A 1 317 ? -5.568  -13.453 -56.683 0.62 23.52 ? 319 MET   A CA  1 
ATOM   2685 C C   . MET   A 1 317 ? -6.731  -13.375 -57.664 1.00 23.26 ? 319 MET   A C   1 
ATOM   2686 O O   . MET   A 1 317 ? -6.721  -12.513 -58.554 1.00 25.26 ? 319 MET   A O   1 
ATOM   2687 C CB  A MET   A 1 317 ? -4.308  -13.898 -57.300 0.38 23.88 ? 319 MET   A CB  1 
ATOM   2688 C CB  B MET   A 1 317 ? -4.346  -14.090 -57.350 0.62 22.73 ? 319 MET   A CB  1 
ATOM   2689 C CG  A MET   A 1 317 ? -3.085  -13.639 -56.431 0.38 22.11 ? 319 MET   A CG  1 
ATOM   2690 C CG  B MET   A 1 317 ? -3.099  -14.053 -56.464 0.62 23.58 ? 319 MET   A CG  1 
ATOM   2691 S SD  A MET   A 1 317 ? -1.510  -13.933 -57.251 0.38 26.67 ? 319 MET   A SD  1 
ATOM   2692 S SD  B MET   A 1 317 ? -1.667  -14.957 -57.103 0.62 21.97 ? 319 MET   A SD  1 
ATOM   2693 C CE  A MET   A 1 317 ? -1.914  -15.431 -58.150 0.38 25.75 ? 319 MET   A CE  1 
ATOM   2694 C CE  B MET   A 1 317 ? -1.304  -13.977 -58.564 0.62 25.99 ? 319 MET   A CE  1 
ATOM   2695 N N   . GLU   A 1 318 ? -7.715  -14.265 -57.535 1.00 23.92 ? 320 GLU   A N   1 
ATOM   2696 C CA  . GLU   A 1 318 ? -8.926  -14.219 -58.355 1.00 21.02 ? 320 GLU   A CA  1 
ATOM   2697 C C   . GLU   A 1 318 ? -9.982  -13.264 -57.808 1.00 23.34 ? 320 GLU   A C   1 
ATOM   2698 O O   . GLU   A 1 318 ? -11.041 -13.124 -58.433 1.00 25.05 ? 320 GLU   A O   1 
ATOM   2699 C CB  . GLU   A 1 318 ? -9.546  -15.622 -58.481 1.00 28.54 ? 320 GLU   A CB  1 
ATOM   2700 C CG  . GLU   A 1 318 ? -8.602  -16.724 -58.933 1.00 30.73 ? 320 GLU   A CG  1 
ATOM   2701 C CD  . GLU   A 1 318 ? -8.406  -16.779 -60.433 1.00 35.26 ? 320 GLU   A CD  1 
ATOM   2702 O OE1 . GLU   A 1 318 ? -9.409  -16.945 -61.174 1.00 39.09 ? 320 GLU   A OE1 1 
ATOM   2703 O OE2 . GLU   A 1 318 ? -7.242  -16.661 -60.875 1.00 36.05 ? 320 GLU   A OE2 1 
ATOM   2704 N N   . HIS   A 1 319 ? -9.745  -12.619 -56.648 1.00 22.60 ? 321 HIS   A N   1 
ATOM   2705 C CA  . HIS   A 1 319 ? -10.822 -11.905 -55.964 1.00 26.16 ? 321 HIS   A CA  1 
ATOM   2706 C C   . HIS   A 1 319 ? -11.116 -10.569 -56.647 1.00 27.56 ? 321 HIS   A C   1 
ATOM   2707 O O   . HIS   A 1 319 ? -10.198 -9.900  -57.122 1.00 25.89 ? 321 HIS   A O   1 
ATOM   2708 C CB  . HIS   A 1 319 ? -10.462 -11.667 -54.491 1.00 25.32 ? 321 HIS   A CB  1 
ATOM   2709 C CG  . HIS   A 1 319 ? -11.617 -11.196 -53.671 1.00 22.44 ? 321 HIS   A CG  1 
ATOM   2710 N ND1 . HIS   A 1 319 ? -12.014 -9.877  -53.633 1.00 23.32 ? 321 HIS   A ND1 1 
ATOM   2711 C CD2 . HIS   A 1 319 ? -12.475 -11.873 -52.873 1.00 25.77 ? 321 HIS   A CD2 1 
ATOM   2712 C CE1 . HIS   A 1 319 ? -13.074 -9.762  -52.851 1.00 25.91 ? 321 HIS   A CE1 1 
ATOM   2713 N NE2 . HIS   A 1 319 ? -13.375 -10.958 -52.377 1.00 25.92 ? 321 HIS   A NE2 1 
ATOM   2714 N N   . PRO   A 1 320 ? -12.402 -10.149 -56.697 1.00 22.15 ? 322 PRO   A N   1 
ATOM   2715 C CA  . PRO   A 1 320 ? -12.753 -8.863  -57.332 1.00 25.93 ? 322 PRO   A CA  1 
ATOM   2716 C C   . PRO   A 1 320 ? -12.005 -7.639  -56.799 1.00 22.26 ? 322 PRO   A C   1 
ATOM   2717 O O   . PRO   A 1 320 ? -11.905 -6.627  -57.504 1.00 26.93 ? 322 PRO   A O   1 
ATOM   2718 C CB  . PRO   A 1 320 ? -14.261 -8.749  -57.056 1.00 28.15 ? 322 PRO   A CB  1 
ATOM   2719 C CG  . PRO   A 1 320 ? -14.714 -10.167 -57.019 1.00 26.82 ? 322 PRO   A CG  1 
ATOM   2720 C CD  . PRO   A 1 320 ? -13.596 -10.931 -56.332 1.00 23.88 ? 322 PRO   A CD  1 
ATOM   2721 N N   . TYR   A 1 321 ? -11.477 -7.707  -55.569 1.00 23.51 ? 323 TYR   A N   1 
ATOM   2722 C CA  . TYR   A 1 321 ? -10.683 -6.611  -55.024 1.00 21.46 ? 323 TYR   A CA  1 
ATOM   2723 C C   . TYR   A 1 321 ? -9.526  -6.240  -55.951 1.00 22.67 ? 323 TYR   A C   1 
ATOM   2724 O O   . TYR   A 1 321 ? -9.117  -5.077  -55.998 1.00 24.45 ? 323 TYR   A O   1 
ATOM   2725 C CB  . TYR   A 1 321 ? -10.170 -7.014  -53.633 1.00 22.98 ? 323 TYR   A CB  1 
ATOM   2726 C CG  . TYR   A 1 321 ? -9.275  -6.028  -52.904 1.00 21.37 ? 323 TYR   A CG  1 
ATOM   2727 C CD1 . TYR   A 1 321 ? -9.740  -4.780  -52.531 1.00 22.77 ? 323 TYR   A CD1 1 
ATOM   2728 C CD2 . TYR   A 1 321 ? -7.978  -6.380  -52.534 1.00 25.70 ? 323 TYR   A CD2 1 
ATOM   2729 C CE1 . TYR   A 1 321 ? -8.946  -3.904  -51.840 1.00 22.11 ? 323 TYR   A CE1 1 
ATOM   2730 C CE2 . TYR   A 1 321 ? -7.169  -5.505  -51.840 1.00 25.40 ? 323 TYR   A CE2 1 
ATOM   2731 C CZ  . TYR   A 1 321 ? -7.662  -4.267  -51.490 1.00 27.44 ? 323 TYR   A CZ  1 
ATOM   2732 O OH  . TYR   A 1 321 ? -6.877  -3.383  -50.798 1.00 27.19 ? 323 TYR   A OH  1 
ATOM   2733 N N   . PHE   A 1 322 ? -9.008  -7.201  -56.715 1.00 24.81 ? 324 PHE   A N   1 
ATOM   2734 C CA  . PHE   A 1 322 ? -7.869  -6.965  -57.585 1.00 22.82 ? 324 PHE   A CA  1 
ATOM   2735 C C   . PHE   A 1 322 ? -8.268  -6.664  -59.015 1.00 21.88 ? 324 PHE   A C   1 
ATOM   2736 O O   . PHE   A 1 322 ? -7.394  -6.522  -59.872 1.00 23.10 ? 324 PHE   A O   1 
ATOM   2737 C CB  . PHE   A 1 322 ? -6.919  -8.170  -57.536 1.00 20.05 ? 324 PHE   A CB  1 
ATOM   2738 C CG  . PHE   A 1 322 ? -6.354  -8.405  -56.166 1.00 24.69 ? 324 PHE   A CG  1 
ATOM   2739 C CD1 . PHE   A 1 322 ? -5.489  -7.478  -55.602 1.00 23.45 ? 324 PHE   A CD1 1 
ATOM   2740 C CD2 . PHE   A 1 322 ? -6.725  -9.518  -55.424 1.00 22.63 ? 324 PHE   A CD2 1 
ATOM   2741 C CE1 . PHE   A 1 322 ? -4.971  -7.668  -54.336 1.00 26.48 ? 324 PHE   A CE1 1 
ATOM   2742 C CE2 . PHE   A 1 322 ? -6.225  -9.708  -54.147 1.00 27.29 ? 324 PHE   A CE2 1 
ATOM   2743 C CZ  . PHE   A 1 322 ? -5.344  -8.784  -53.606 1.00 22.60 ? 324 PHE   A CZ  1 
ATOM   2744 N N   . TYR   A 1 323 ? -9.566  -6.528  -59.293 1.00 24.33 ? 325 TYR   A N   1 
ATOM   2745 C CA  . TYR   A 1 323 ? -9.970  -6.237  -60.660 1.00 19.72 ? 325 TYR   A CA  1 
ATOM   2746 C C   . TYR   A 1 323 ? -9.440  -4.888  -61.138 1.00 22.81 ? 325 TYR   A C   1 
ATOM   2747 O O   . TYR   A 1 323 ? -9.137  -4.740  -62.321 1.00 24.81 ? 325 TYR   A O   1 
ATOM   2748 C CB  . TYR   A 1 323 ? -11.494 -6.271  -60.790 1.00 22.62 ? 325 TYR   A CB  1 
ATOM   2749 C CG  . TYR   A 1 323 ? -12.141 -7.650  -60.754 1.00 27.32 ? 325 TYR   A CG  1 
ATOM   2750 C CD1 . TYR   A 1 323 ? -11.384 -8.816  -60.693 1.00 29.14 ? 325 TYR   A CD1 1 
ATOM   2751 C CD2 . TYR   A 1 323 ? -13.526 -7.775  -60.802 1.00 26.12 ? 325 TYR   A CD2 1 
ATOM   2752 C CE1 . TYR   A 1 323 ? -11.982 -10.065 -60.664 1.00 27.33 ? 325 TYR   A CE1 1 
ATOM   2753 C CE2 . TYR   A 1 323 ? -14.130 -9.016  -60.770 1.00 33.81 ? 325 TYR   A CE2 1 
ATOM   2754 C CZ  . TYR   A 1 323 ? -13.362 -10.158 -60.708 1.00 34.84 ? 325 TYR   A CZ  1 
ATOM   2755 O OH  . TYR   A 1 323 ? -13.981 -11.390 -60.675 1.00 36.78 ? 325 TYR   A OH  1 
ATOM   2756 N N   . THR   A 1 324 ? -9.281  -3.905  -60.236 1.00 25.51 ? 326 THR   A N   1 
ATOM   2757 C CA  . THR   A 1 324 ? -8.823  -2.590  -60.689 1.00 26.33 ? 326 THR   A CA  1 
ATOM   2758 C C   . THR   A 1 324 ? -7.305  -2.498  -60.838 1.00 27.06 ? 326 THR   A C   1 
ATOM   2759 O O   . THR   A 1 324 ? -6.816  -1.527  -61.430 1.00 28.43 ? 326 THR   A O   1 
ATOM   2760 C CB  . THR   A 1 324 ? -9.301  -1.493  -59.735 1.00 30.42 ? 326 THR   A CB  1 
ATOM   2761 O OG1 . THR   A 1 324 ? -9.022  -0.207  -60.307 1.00 35.35 ? 326 THR   A OG1 1 
ATOM   2762 C CG2 . THR   A 1 324 ? -8.602  -1.601  -58.416 1.00 31.28 ? 326 THR   A CG2 1 
ATOM   2763 N N   . VAL   A 1 325 ? -6.560  -3.497  -60.377 1.00 25.52 ? 327 VAL   A N   1 
ATOM   2764 C CA  . VAL   A 1 325 ? -5.100  -3.487  -60.485 1.00 24.74 ? 327 VAL   A CA  1 
ATOM   2765 C C   . VAL   A 1 325 ? -4.699  -3.786  -61.919 1.00 22.98 ? 327 VAL   A C   1 
ATOM   2766 O O   . VAL   A 1 325 ? -5.159  -4.772  -62.504 1.00 26.98 ? 327 VAL   A O   1 
ATOM   2767 C CB  . VAL   A 1 325 ? -4.478  -4.518  -59.534 1.00 22.02 ? 327 VAL   A CB  1 
ATOM   2768 C CG1 . VAL   A 1 325 ? -2.962  -4.626  -59.745 1.00 25.19 ? 327 VAL   A CG1 1 
ATOM   2769 C CG2 . VAL   A 1 325 ? -4.772  -4.148  -58.110 1.00 28.76 ? 327 VAL   A CG2 1 
ATOM   2770 N N   . VAL   A 1 326 ? -3.816  -2.955  -62.485 1.00 24.02 ? 328 VAL   A N   1 
ATOM   2771 C CA  . VAL   A 1 326 ? -3.376  -3.168  -63.856 1.00 27.67 ? 328 VAL   A CA  1 
ATOM   2772 C C   . VAL   A 1 326 ? -2.511  -4.413  -63.917 1.00 28.98 ? 328 VAL   A C   1 
ATOM   2773 O O   . VAL   A 1 326 ? -1.518  -4.536  -63.186 1.00 29.23 ? 328 VAL   A O   1 
ATOM   2774 C CB  . VAL   A 1 326 ? -2.606  -1.952  -64.397 1.00 34.48 ? 328 VAL   A CB  1 
ATOM   2775 C CG1 . VAL   A 1 326 ? -2.080  -2.252  -65.792 1.00 41.04 ? 328 VAL   A CG1 1 
ATOM   2776 C CG2 . VAL   A 1 326 ? -3.479  -0.725  -64.430 1.00 41.90 ? 328 VAL   A CG2 1 
ATOM   2777 N N   . LYS   A 1 327 ? -2.874  -5.333  -64.806 1.00 34.94 ? 329 LYS   A N   1 
ATOM   2778 C CA  . LYS   A 1 327 ? -2.139  -6.578  -64.964 1.00 45.20 ? 329 LYS   A CA  1 
ATOM   2779 C C   . LYS   A 1 327 ? -1.122  -6.437  -66.088 1.00 57.15 ? 329 LYS   A C   1 
ATOM   2780 O O   . LYS   A 1 327 ? -1.397  -5.809  -67.114 1.00 56.51 ? 329 LYS   A O   1 
ATOM   2781 C CB  . LYS   A 1 327 ? -3.095  -7.737  -65.256 1.00 47.29 ? 329 LYS   A CB  1 
ATOM   2782 C CG  . LYS   A 1 327 ? -4.213  -7.905  -64.231 1.00 50.49 ? 329 LYS   A CG  1 
ATOM   2783 C CD  . LYS   A 1 327 ? -3.672  -8.030  -62.811 1.00 44.38 ? 329 LYS   A CD  1 
ATOM   2784 C CE  . LYS   A 1 327 ? -4.788  -8.384  -61.831 1.00 34.89 ? 329 LYS   A CE  1 
ATOM   2785 N NZ  . LYS   A 1 327 ? -6.055  -7.664  -62.167 1.00 37.63 ? 329 LYS   A NZ  1 
ATOM   2786 N N   . ASP   A 1 328 ? 0.057   -7.014  -65.882 1.00 67.60 ? 330 ASP   A N   1 
ATOM   2787 C CA  . ASP   A 1 328 ? 1.139   -6.907  -66.855 1.00 75.27 ? 330 ASP   A CA  1 
ATOM   2788 C C   . ASP   A 1 328 ? 1.197   -8.139  -67.756 1.00 74.30 ? 330 ASP   A C   1 
ATOM   2789 O O   . ASP   A 1 328 ? 0.468   -8.232  -68.746 1.00 72.66 ? 330 ASP   A O   1 
ATOM   2790 C CB  . ASP   A 1 328 ? 2.479   -6.708  -66.143 1.00 82.56 ? 330 ASP   A CB  1 
ATOM   2791 C CG  . ASP   A 1 328 ? 2.435   -5.590  -65.115 1.00 88.29 ? 330 ASP   A CG  1 
ATOM   2792 O OD1 . ASP   A 1 328 ? 2.333   -5.891  -63.905 1.00 88.11 ? 330 ASP   A OD1 1 
ATOM   2793 O OD2 . ASP   A 1 328 ? 2.491   -4.409  -65.519 1.00 91.29 ? 330 ASP   A OD2 1 
HETATM 2794 S S   . SO4   B 2 .   ? 11.322  -23.535 -35.807 1.00 50.85 ? 401 SO4   A S   1 
HETATM 2795 O O1  . SO4   B 2 .   ? 12.287  -22.545 -36.277 1.00 47.76 ? 401 SO4   A O1  1 
HETATM 2796 O O2  . SO4   B 2 .   ? 10.121  -22.846 -35.343 1.00 52.19 ? 401 SO4   A O2  1 
HETATM 2797 O O3  . SO4   B 2 .   ? 10.960  -24.449 -36.883 1.00 47.40 ? 401 SO4   A O3  1 
HETATM 2798 O O4  . SO4   B 2 .   ? 11.894  -24.296 -34.701 1.00 59.05 ? 401 SO4   A O4  1 
HETATM 2799 S S   . SO4   C 2 .   ? -14.600 -19.183 -39.319 1.00 22.97 ? 402 SO4   A S   1 
HETATM 2800 O O1  . SO4   C 2 .   ? -14.926 -19.396 -40.727 1.00 28.40 ? 402 SO4   A O1  1 
HETATM 2801 O O2  . SO4   C 2 .   ? -13.994 -17.850 -39.141 1.00 19.37 ? 402 SO4   A O2  1 
HETATM 2802 O O3  . SO4   C 2 .   ? -15.851 -19.232 -38.562 1.00 27.70 ? 402 SO4   A O3  1 
HETATM 2803 O O4  . SO4   C 2 .   ? -13.739 -20.265 -38.848 1.00 20.62 ? 402 SO4   A O4  1 
HETATM 2804 S S   . SO4   D 2 .   ? 6.451   -16.574 -29.138 1.00 62.06 ? 403 SO4   A S   1 
HETATM 2805 O O1  . SO4   D 2 .   ? 7.805   -16.541 -28.588 1.00 67.38 ? 403 SO4   A O1  1 
HETATM 2806 O O2  . SO4   D 2 .   ? 5.791   -15.304 -28.847 1.00 59.97 ? 403 SO4   A O2  1 
HETATM 2807 O O3  . SO4   D 2 .   ? 6.525   -16.789 -30.586 1.00 54.56 ? 403 SO4   A O3  1 
HETATM 2808 O O4  . SO4   D 2 .   ? 5.704   -17.665 -28.518 1.00 63.59 ? 403 SO4   A O4  1 
HETATM 2809 C C1  . EDO   E 3 .   ? -10.130 -4.096  -33.620 1.00 41.92 ? 404 EDO   A C1  1 
HETATM 2810 O O1  . EDO   E 3 .   ? -9.666  -3.073  -32.735 1.00 51.23 ? 404 EDO   A O1  1 
HETATM 2811 C C2  . EDO   E 3 .   ? -9.133  -5.244  -33.624 1.00 31.47 ? 404 EDO   A C2  1 
HETATM 2812 O O2  . EDO   E 3 .   ? -8.613  -5.427  -32.301 1.00 33.59 ? 404 EDO   A O2  1 
HETATM 2813 C C1  . EDO   F 3 .   ? -2.095  -21.626 -50.160 1.00 22.52 ? 405 EDO   A C1  1 
HETATM 2814 O O1  . EDO   F 3 .   ? -1.720  -20.554 -50.997 1.00 20.85 ? 405 EDO   A O1  1 
HETATM 2815 C C2  . EDO   F 3 .   ? -2.644  -21.017 -48.876 1.00 27.42 ? 405 EDO   A C2  1 
HETATM 2816 O O2  . EDO   F 3 .   ? -3.270  -22.064 -48.151 1.00 25.26 ? 405 EDO   A O2  1 
HETATM 2817 C C21 . A1IYW G 4 .   ? 17.202  -7.363  -38.305 1.00 32.18 ? 406 A1IYW A C21 1 
HETATM 2818 C C15 . A1IYW G 4 .   ? 16.402  -11.141 -44.835 1.00 21.20 ? 406 A1IYW A C15 1 
HETATM 2819 C C10 . A1IYW G 4 .   ? 16.918  -9.163  -46.177 1.00 22.84 ? 406 A1IYW A C10 1 
HETATM 2820 C C13 . A1IYW G 4 .   ? 16.533  -10.255 -42.415 1.00 26.22 ? 406 A1IYW A C13 1 
HETATM 2821 C C01 . A1IYW G 4 .   ? 17.467  -2.787  -47.189 1.00 36.34 ? 406 A1IYW A C01 1 
HETATM 2822 C C03 . A1IYW G 4 .   ? 17.167  -5.145  -47.643 1.00 24.48 ? 406 A1IYW A C03 1 
HETATM 2823 C C04 . A1IYW G 4 .   ? 17.344  -6.235  -48.503 1.00 22.35 ? 406 A1IYW A C04 1 
HETATM 2824 C C06 . A1IYW G 4 .   ? 17.262  -7.539  -48.037 1.00 19.08 ? 406 A1IYW A C06 1 
HETATM 2825 C C07 . A1IYW G 4 .   ? 17.000  -7.742  -46.636 1.00 21.86 ? 406 A1IYW A C07 1 
HETATM 2826 C C08 . A1IYW G 4 .   ? 16.815  -6.663  -45.771 1.00 21.43 ? 406 A1IYW A C08 1 
HETATM 2827 C C09 . A1IYW G 4 .   ? 16.906  -5.355  -46.248 1.00 23.99 ? 406 A1IYW A C09 1 
HETATM 2828 C C11 . A1IYW G 4 .   ? 16.761  -9.617  -44.957 1.00 21.78 ? 406 A1IYW A C11 1 
HETATM 2829 C C18 . A1IYW G 4 .   ? 16.697  -9.313  -40.197 1.00 30.24 ? 406 A1IYW A C18 1 
HETATM 2830 C C19 . A1IYW G 4 .   ? 17.798  -9.440  -39.315 1.00 37.03 ? 406 A1IYW A C19 1 
HETATM 2831 C C20 . A1IYW G 4 .   ? 18.042  -8.448  -38.383 1.00 37.73 ? 406 A1IYW A C20 1 
HETATM 2832 C C22 . A1IYW G 4 .   ? 16.105  -7.251  -39.163 1.00 33.23 ? 406 A1IYW A C22 1 
HETATM 2833 C C23 . A1IYW G 4 .   ? 15.864  -8.263  -40.131 1.00 28.75 ? 406 A1IYW A C23 1 
HETATM 2834 N N14 . A1IYW G 4 .   ? 16.267  -11.504 -43.241 1.00 24.00 ? 406 A1IYW A N14 1 
HETATM 2835 N N17 . A1IYW G 4 .   ? 16.471  -10.396 -41.185 1.00 27.61 ? 406 A1IYW A N17 1 
HETATM 2836 O O02 . A1IYW G 4 .   ? 17.248  -3.826  -48.175 1.00 30.91 ? 406 A1IYW A O02 1 
HETATM 2837 O O05 . A1IYW G 4 .   ? 17.616  -5.987  -49.895 1.00 25.68 ? 406 A1IYW A O05 1 
HETATM 2838 O O16 . A1IYW G 4 .   ? 16.229  -11.919 -45.746 1.00 22.10 ? 406 A1IYW A O16 1 
HETATM 2839 O O24 . A1IYW G 4 .   ? 19.150  -8.577  -37.529 1.00 43.88 ? 406 A1IYW A O24 1 
HETATM 2840 S S12 . A1IYW G 4 .   ? 16.877  -8.942  -43.442 1.00 25.74 ? 406 A1IYW A S12 1 
HETATM 2841 S S   . SO4   H 2 .   ? 17.327  -29.839 -32.794 1.00 96.05 ? 407 SO4   A S   1 
HETATM 2842 O O1  . SO4   H 2 .   ? 17.563  -30.804 -33.865 1.00 93.89 ? 407 SO4   A O1  1 
HETATM 2843 O O2  . SO4   H 2 .   ? 18.591  -29.217 -32.404 1.00 93.84 ? 407 SO4   A O2  1 
HETATM 2844 O O3  . SO4   H 2 .   ? 16.405  -28.808 -33.260 1.00 98.98 ? 407 SO4   A O3  1 
HETATM 2845 O O4  . SO4   H 2 .   ? 16.739  -30.525 -31.647 1.00 95.72 ? 407 SO4   A O4  1 
HETATM 2846 O O   . HOH   I 5 .   ? -21.358 -3.851  -33.555 1.00 41.84 ? 501 HOH   A O   1 
HETATM 2847 O O   . HOH   I 5 .   ? -8.848  -18.924 -15.366 1.00 51.51 ? 502 HOH   A O   1 
HETATM 2848 O O   . HOH   I 5 .   ? 16.607  -35.019 -38.957 1.00 55.11 ? 503 HOH   A O   1 
HETATM 2849 O O   . HOH   I 5 .   ? -2.099  -5.828  -38.230 1.00 22.19 ? 504 HOH   A O   1 
HETATM 2850 O O   . HOH   I 5 .   ? -11.043 -21.398 -49.720 1.00 41.50 ? 505 HOH   A O   1 
HETATM 2851 O O   . HOH   I 5 .   ? 14.834  3.999   -55.163 1.00 45.54 ? 506 HOH   A O   1 
HETATM 2852 O O   . HOH   I 5 .   ? -13.131 -28.454 -27.963 1.00 35.00 ? 507 HOH   A O   1 
HETATM 2853 O O   . HOH   I 5 .   ? -0.399  -21.351 -59.077 1.00 42.46 ? 508 HOH   A O   1 
HETATM 2854 O O   . HOH   I 5 .   ? 1.906   -36.080 -49.968 1.00 42.63 ? 509 HOH   A O   1 
HETATM 2855 O O   . HOH   I 5 .   ? -2.013  9.390   -40.137 1.00 38.47 ? 510 HOH   A O   1 
HETATM 2856 O O   . HOH   I 5 .   ? 8.951   -1.465  -46.491 1.00 47.97 ? 511 HOH   A O   1 
HETATM 2857 O O   . HOH   I 5 .   ? 3.923   -12.947 -27.819 1.00 38.95 ? 512 HOH   A O   1 
HETATM 2858 O O   . HOH   I 5 .   ? -0.034  -3.694  -25.728 1.00 55.26 ? 513 HOH   A O   1 
HETATM 2859 O O   . HOH   I 5 .   ? -13.705 10.450  -37.585 1.00 48.63 ? 514 HOH   A O   1 
HETATM 2860 O O   . HOH   I 5 .   ? 10.298  3.334   -50.964 1.00 43.04 ? 515 HOH   A O   1 
HETATM 2861 O O   . HOH   I 5 .   ? 27.850  -19.213 -52.564 1.00 42.62 ? 516 HOH   A O   1 
HETATM 2862 O O   . HOH   I 5 .   ? 26.752  -2.381  -33.873 1.00 41.01 ? 517 HOH   A O   1 
HETATM 2863 O O   . HOH   I 5 .   ? 23.091  -8.000  -28.021 1.00 56.97 ? 518 HOH   A O   1 
HETATM 2864 O O   . HOH   I 5 .   ? -12.712 -22.363 -51.881 1.00 46.26 ? 519 HOH   A O   1 
HETATM 2865 O O   . HOH   I 5 .   ? 5.678   -3.522  -45.729 1.00 38.75 ? 520 HOH   A O   1 
HETATM 2866 O O   . HOH   I 5 .   ? -22.842 -7.640  -32.028 1.00 36.58 ? 521 HOH   A O   1 
HETATM 2867 O O   . HOH   I 5 .   ? -11.763 -17.729 -60.779 1.00 48.42 ? 522 HOH   A O   1 
HETATM 2868 O O   . HOH   I 5 .   ? -10.767 -22.087 -21.373 1.00 42.02 ? 523 HOH   A O   1 
HETATM 2869 O O   . HOH   I 5 .   ? 0.392   -5.979  -59.047 1.00 38.77 ? 524 HOH   A O   1 
HETATM 2870 O O   . HOH   I 5 .   ? -5.254  -17.182 -59.378 1.00 42.42 ? 525 HOH   A O   1 
HETATM 2871 O O   . HOH   I 5 .   ? -17.573 6.579   -42.974 1.00 47.14 ? 526 HOH   A O   1 
HETATM 2872 O O   . HOH   I 5 .   ? -5.387  -12.526 -60.954 1.00 44.67 ? 527 HOH   A O   1 
HETATM 2873 O O   . HOH   I 5 .   ? 2.676   -18.897 -31.088 1.00 32.89 ? 528 HOH   A O   1 
HETATM 2874 O O   . HOH   I 5 .   ? 7.771   -15.549 -32.447 1.00 51.24 ? 529 HOH   A O   1 
HETATM 2875 O O   . HOH   I 5 .   ? -7.512  -0.768  -50.301 1.00 29.04 ? 530 HOH   A O   1 
HETATM 2876 O O   . HOH   I 5 .   ? -3.230  -24.565 -47.550 1.00 23.45 ? 531 HOH   A O   1 
HETATM 2877 O O   . HOH   I 5 .   ? -20.559 -16.804 -37.999 1.00 32.89 ? 532 HOH   A O   1 
HETATM 2878 O O   . HOH   I 5 .   ? -15.074 -24.518 -40.262 1.00 42.36 ? 533 HOH   A O   1 
HETATM 2879 O O   . HOH   I 5 .   ? 39.067  -3.608  -47.321 1.00 43.67 ? 534 HOH   A O   1 
HETATM 2880 O O   . HOH   I 5 .   ? 26.121  -24.772 -42.783 1.00 59.20 ? 535 HOH   A O   1 
HETATM 2881 O O   . HOH   I 5 .   ? 12.615  -9.150  -40.006 1.00 46.64 ? 536 HOH   A O   1 
HETATM 2882 O O   . HOH   I 5 .   ? -12.028 -27.295 -22.025 1.00 40.36 ? 537 HOH   A O   1 
HETATM 2883 O O   . HOH   I 5 .   ? 31.986  -14.909 -53.688 1.00 31.47 ? 538 HOH   A O   1 
HETATM 2884 O O   . HOH   I 5 .   ? 12.859  -20.901 -57.885 1.00 28.02 ? 539 HOH   A O   1 
HETATM 2885 O O   . HOH   I 5 .   ? 8.387   -12.132 -36.078 1.00 34.07 ? 540 HOH   A O   1 
HETATM 2886 O O   . HOH   I 5 .   ? 20.015  0.157   -47.317 1.00 45.37 ? 541 HOH   A O   1 
HETATM 2887 O O   . HOH   I 5 .   ? 27.775  -9.089  -36.575 1.00 49.70 ? 542 HOH   A O   1 
HETATM 2888 O O   . HOH   I 5 .   ? -0.610  -31.538 -42.544 1.00 21.60 ? 543 HOH   A O   1 
HETATM 2889 O O   . HOH   I 5 .   ? -5.406  -24.819 -26.768 1.00 41.18 ? 544 HOH   A O   1 
HETATM 2890 O O   . HOH   I 5 .   ? -15.226 -21.942 -41.349 1.00 30.87 ? 545 HOH   A O   1 
HETATM 2891 O O   . HOH   I 5 .   ? 24.555  -23.655 -50.745 1.00 33.90 ? 546 HOH   A O   1 
HETATM 2892 O O   . HOH   I 5 .   ? -13.882 -12.940 -40.883 1.00 21.80 ? 547 HOH   A O   1 
HETATM 2893 O O   . HOH   I 5 .   ? 6.354   -5.635  -38.826 1.00 31.82 ? 548 HOH   A O   1 
HETATM 2894 O O   . HOH   I 5 .   ? -15.210 -31.859 -30.541 1.00 43.36 ? 549 HOH   A O   1 
HETATM 2895 O O   . HOH   I 5 .   ? -3.133  -28.842 -42.193 1.00 22.72 ? 550 HOH   A O   1 
HETATM 2896 O O   . HOH   I 5 .   ? -0.383  0.391   -62.203 1.00 29.02 ? 551 HOH   A O   1 
HETATM 2897 O O   . HOH   I 5 .   ? 28.203  -5.515  -34.654 1.00 42.72 ? 552 HOH   A O   1 
HETATM 2898 O O   . HOH   I 5 .   ? 3.316   -27.038 -29.168 1.00 36.25 ? 553 HOH   A O   1 
HETATM 2899 O O   . HOH   I 5 .   ? 36.210  -13.724 -33.443 1.00 27.55 ? 554 HOH   A O   1 
HETATM 2900 O O   . HOH   I 5 .   ? -10.272 -6.664  -30.620 1.00 25.92 ? 555 HOH   A O   1 
HETATM 2901 O O   . HOH   I 5 .   ? 36.102  -16.512 -43.770 1.00 34.31 ? 556 HOH   A O   1 
HETATM 2902 O O   . HOH   I 5 .   ? 16.169  -13.002 -39.945 1.00 34.21 ? 557 HOH   A O   1 
HETATM 2903 O O   . HOH   I 5 .   ? -1.358  -32.154 -53.916 1.00 41.86 ? 558 HOH   A O   1 
HETATM 2904 O O   . HOH   I 5 .   ? -8.594  3.360   -37.503 1.00 37.47 ? 559 HOH   A O   1 
HETATM 2905 O O   . HOH   I 5 .   ? -18.327 -15.224 -41.757 1.00 42.05 ? 560 HOH   A O   1 
HETATM 2906 O O   . HOH   I 5 .   ? 6.464   -27.481 -56.926 1.00 30.09 ? 561 HOH   A O   1 
HETATM 2907 O O   . HOH   I 5 .   ? -10.966 9.369   -46.076 1.00 39.90 ? 562 HOH   A O   1 
HETATM 2908 O O   . HOH   I 5 .   ? -19.550 -17.876 -26.825 1.00 30.95 ? 563 HOH   A O   1 
HETATM 2909 O O   . HOH   I 5 .   ? 9.953   -14.949 -61.556 1.00 47.24 ? 564 HOH   A O   1 
HETATM 2910 O O   . HOH   I 5 .   ? 23.565  -19.711 -52.930 1.00 45.17 ? 565 HOH   A O   1 
HETATM 2911 O O   . HOH   I 5 .   ? -7.029  -22.841 -46.473 1.00 26.90 ? 566 HOH   A O   1 
HETATM 2912 O O   . HOH   I 5 .   ? 16.280  -32.507 -43.531 1.00 38.86 ? 567 HOH   A O   1 
HETATM 2913 O O   . HOH   I 5 .   ? -6.561  -4.690  -30.705 1.00 29.01 ? 568 HOH   A O   1 
HETATM 2914 O O   . HOH   I 5 .   ? 0.051   -4.571  -39.377 1.00 30.13 ? 569 HOH   A O   1 
HETATM 2915 O O   . HOH   I 5 .   ? -11.445 -8.289  -22.421 1.00 51.78 ? 570 HOH   A O   1 
HETATM 2916 O O   . HOH   I 5 .   ? -18.223 -19.615 -39.812 1.00 35.18 ? 571 HOH   A O   1 
HETATM 2917 O O   . HOH   I 5 .   ? 15.835  -8.562  -58.561 1.00 45.86 ? 572 HOH   A O   1 
HETATM 2918 O O   . HOH   I 5 .   ? -19.979 -15.375 -31.384 1.00 22.39 ? 573 HOH   A O   1 
HETATM 2919 O O   . HOH   I 5 .   ? 20.881  -29.945 -51.161 1.00 43.08 ? 574 HOH   A O   1 
HETATM 2920 O O   . HOH   I 5 .   ? 15.960  -14.622 -45.616 1.00 22.02 ? 575 HOH   A O   1 
HETATM 2921 O O   . HOH   I 5 .   ? -19.344 -25.558 -30.976 1.00 48.49 ? 576 HOH   A O   1 
HETATM 2922 O O   . HOH   I 5 .   ? -15.702 -9.698  -38.188 1.00 30.85 ? 577 HOH   A O   1 
HETATM 2923 O O   . HOH   I 5 .   ? -12.728 -17.771 -46.939 1.00 22.33 ? 578 HOH   A O   1 
HETATM 2924 O O   . HOH   I 5 .   ? -5.410  -20.691 -47.172 1.00 22.00 ? 579 HOH   A O   1 
HETATM 2925 O O   . HOH   I 5 .   ? -17.828 -8.083  -28.010 1.00 39.46 ? 580 HOH   A O   1 
HETATM 2926 O O   . HOH   I 5 .   ? 10.137  -27.839 -38.030 1.00 36.82 ? 581 HOH   A O   1 
HETATM 2927 O O   . HOH   I 5 .   ? 3.227   -27.133 -57.189 1.00 39.64 ? 582 HOH   A O   1 
HETATM 2928 O O   . HOH   I 5 .   ? 0.828   -17.166 -59.030 1.00 47.82 ? 583 HOH   A O   1 
HETATM 2929 O O   . HOH   I 5 .   ? -11.527 -15.436 -55.117 1.00 36.77 ? 584 HOH   A O   1 
HETATM 2930 O O   . HOH   I 5 .   ? -18.008 -12.877 -41.392 1.00 34.49 ? 585 HOH   A O   1 
HETATM 2931 O O   . HOH   I 5 .   ? 8.008   -6.242  -57.483 1.00 39.72 ? 586 HOH   A O   1 
HETATM 2932 O O   . HOH   I 5 .   ? -2.321  -20.788 -53.658 1.00 21.55 ? 587 HOH   A O   1 
HETATM 2933 O O   . HOH   I 5 .   ? 10.357  -36.820 -51.795 1.00 39.48 ? 588 HOH   A O   1 
HETATM 2934 O O   . HOH   I 5 .   ? -9.097  -32.193 -41.105 1.00 35.37 ? 589 HOH   A O   1 
HETATM 2935 O O   . HOH   I 5 .   ? 0.927   -29.964 -40.992 1.00 21.77 ? 590 HOH   A O   1 
HETATM 2936 O O   . HOH   I 5 .   ? -8.336  -7.457  -24.648 1.00 43.38 ? 591 HOH   A O   1 
HETATM 2937 O O   . HOH   I 5 .   ? -12.361 -13.886 -60.727 1.00 40.43 ? 592 HOH   A O   1 
HETATM 2938 O O   . HOH   I 5 .   ? -4.405  -22.374 -54.459 1.00 26.61 ? 593 HOH   A O   1 
HETATM 2939 O O   . HOH   I 5 .   ? 21.663  -5.658  -55.097 1.00 33.38 ? 594 HOH   A O   1 
HETATM 2940 O O   . HOH   I 5 .   ? 17.726  -15.887 -40.018 1.00 39.08 ? 595 HOH   A O   1 
HETATM 2941 O O   . HOH   I 5 .   ? -14.997 -21.796 -36.933 1.00 26.60 ? 596 HOH   A O   1 
HETATM 2942 O O   . HOH   I 5 .   ? -14.395 -16.052 -19.887 1.00 40.13 ? 597 HOH   A O   1 
HETATM 2943 O O   . HOH   I 5 .   ? 4.223   -31.598 -49.584 1.00 26.61 ? 598 HOH   A O   1 
HETATM 2944 O O   . HOH   I 5 .   ? -3.616  -35.299 -34.889 1.00 50.49 ? 599 HOH   A O   1 
HETATM 2945 O O   . HOH   I 5 .   ? 14.806  -14.341 -56.213 1.00 32.49 ? 600 HOH   A O   1 
HETATM 2946 O O   . HOH   I 5 .   ? -9.889  6.151   -52.823 1.00 40.82 ? 601 HOH   A O   1 
HETATM 2947 O O   . HOH   I 5 .   ? -10.713 -0.657  -51.246 1.00 29.04 ? 602 HOH   A O   1 
HETATM 2948 O O   . HOH   I 5 .   ? -15.655 -11.778 -39.276 1.00 37.07 ? 603 HOH   A O   1 
HETATM 2949 O O   . HOH   I 5 .   ? -2.583  5.114   -46.144 1.00 41.92 ? 604 HOH   A O   1 
HETATM 2950 O O   . HOH   I 5 .   ? 19.444  -31.214 -49.738 1.00 39.28 ? 605 HOH   A O   1 
HETATM 2951 O O   . HOH   I 5 .   ? -10.124 -32.537 -26.890 1.00 42.93 ? 606 HOH   A O   1 
HETATM 2952 O O   . HOH   I 5 .   ? -7.090  -14.391 -62.469 1.00 40.72 ? 607 HOH   A O   1 
HETATM 2953 O O   . HOH   I 5 .   ? 10.457  -16.905 -42.399 1.00 18.88 ? 608 HOH   A O   1 
HETATM 2954 O O   . HOH   I 5 .   ? 18.972  -35.929 -43.660 1.00 55.70 ? 609 HOH   A O   1 
HETATM 2955 O O   . HOH   I 5 .   ? -13.506 -25.653 -43.792 1.00 43.67 ? 610 HOH   A O   1 
HETATM 2956 O O   . HOH   I 5 .   ? 13.535  -0.313  -43.361 1.00 47.56 ? 611 HOH   A O   1 
HETATM 2957 O O   . HOH   I 5 .   ? 11.882  -30.966 -45.119 1.00 26.60 ? 612 HOH   A O   1 
HETATM 2958 O O   . HOH   I 5 .   ? -2.902  -7.715  -36.276 1.00 18.37 ? 613 HOH   A O   1 
HETATM 2959 O O   . HOH   I 5 .   ? -8.727  -10.788 -59.415 1.00 26.55 ? 614 HOH   A O   1 
HETATM 2960 O O   . HOH   I 5 .   ? 26.333  -9.181  -56.245 1.00 48.42 ? 615 HOH   A O   1 
HETATM 2961 O O   . HOH   I 5 .   ? 4.803   -12.447 -38.453 1.00 20.93 ? 616 HOH   A O   1 
HETATM 2962 O O   . HOH   I 5 .   ? -12.450 -27.148 -49.573 1.00 47.15 ? 617 HOH   A O   1 
HETATM 2963 O O   . HOH   I 5 .   ? -3.231  -12.324 -35.088 1.00 16.63 ? 618 HOH   A O   1 
HETATM 2964 O O   . HOH   I 5 .   ? -7.019  -10.636 -22.086 1.00 29.41 ? 619 HOH   A O   1 
HETATM 2965 O O   . HOH   I 5 .   ? 4.810   -36.159 -44.652 1.00 37.40 ? 620 HOH   A O   1 
HETATM 2966 O O   . HOH   I 5 .   ? -13.425 -1.806  -55.511 1.00 33.02 ? 621 HOH   A O   1 
HETATM 2967 O O   . HOH   I 5 .   ? -18.373 -16.146 -33.661 1.00 20.96 ? 622 HOH   A O   1 
HETATM 2968 O O   . HOH   I 5 .   ? -0.031  -21.200 -28.113 1.00 43.82 ? 623 HOH   A O   1 
HETATM 2969 O O   . HOH   I 5 .   ? -22.264 -7.711  -34.464 1.00 34.24 ? 624 HOH   A O   1 
HETATM 2970 O O   . HOH   I 5 .   ? -9.587  -2.767  -29.943 1.00 54.22 ? 625 HOH   A O   1 
HETATM 2971 O O   . HOH   I 5 .   ? 20.072  -25.878 -53.576 1.00 35.10 ? 626 HOH   A O   1 
HETATM 2972 O O   . HOH   I 5 .   ? -5.627  -18.228 -62.560 1.00 32.88 ? 627 HOH   A O   1 
HETATM 2973 O O   . HOH   I 5 .   ? 29.852  4.024   -43.833 1.00 51.55 ? 628 HOH   A O   1 
HETATM 2974 O O   . HOH   I 5 .   ? -3.955  7.007   -45.690 1.00 46.07 ? 629 HOH   A O   1 
HETATM 2975 O O   . HOH   I 5 .   ? -19.022 -8.952  -24.640 1.00 38.69 ? 630 HOH   A O   1 
HETATM 2976 O O   . HOH   I 5 .   ? 17.009  -12.451 -35.408 1.00 42.51 ? 631 HOH   A O   1 
HETATM 2977 O O   . HOH   I 5 .   ? 36.482  -2.644  -57.258 1.00 56.78 ? 632 HOH   A O   1 
HETATM 2978 O O   . HOH   I 5 .   ? 14.059  -21.327 -42.611 1.00 21.80 ? 633 HOH   A O   1 
HETATM 2979 O O   . HOH   I 5 .   ? -2.366  -23.301 -41.172 1.00 19.96 ? 634 HOH   A O   1 
HETATM 2980 O O   . HOH   I 5 .   ? 11.588  -14.866 -40.026 1.00 29.85 ? 635 HOH   A O   1 
HETATM 2981 O O   . HOH   I 5 .   ? -5.703  -25.393 -46.947 1.00 25.44 ? 636 HOH   A O   1 
HETATM 2982 O O   . HOH   I 5 .   ? -5.726  -26.496 -44.602 1.00 29.08 ? 637 HOH   A O   1 
HETATM 2983 O O   . HOH   I 5 .   ? -2.661  2.358   -44.649 1.00 40.27 ? 638 HOH   A O   1 
HETATM 2984 O O   . HOH   I 5 .   ? 15.603  -1.139  -55.056 1.00 33.98 ? 639 HOH   A O   1 
HETATM 2985 O O   . HOH   I 5 .   ? 6.208   -35.272 -47.702 1.00 39.00 ? 640 HOH   A O   1 
HETATM 2986 O O   . HOH   I 5 .   ? 3.917   -21.310 -59.110 1.00 46.09 ? 641 HOH   A O   1 
HETATM 2987 O O   . HOH   I 5 .   ? 16.793  -16.402 -53.279 1.00 20.47 ? 642 HOH   A O   1 
HETATM 2988 O O   . HOH   I 5 .   ? 11.744  4.646   -53.202 1.00 56.10 ? 643 HOH   A O   1 
HETATM 2989 O O   . HOH   I 5 .   ? -2.675  -18.162 -26.806 1.00 35.22 ? 644 HOH   A O   1 
HETATM 2990 O O   . HOH   I 5 .   ? -13.940 13.499  -39.274 1.00 50.96 ? 645 HOH   A O   1 
HETATM 2991 O O   . HOH   I 5 .   ? 15.903  -22.131 -57.788 1.00 44.00 ? 646 HOH   A O   1 
HETATM 2992 O O   . HOH   I 5 .   ? 4.109   -4.570  -37.099 1.00 49.26 ? 647 HOH   A O   1 
HETATM 2993 O O   . HOH   I 5 .   ? -15.993 3.556   -49.526 1.00 53.48 ? 648 HOH   A O   1 
HETATM 2994 O O   . HOH   I 5 .   ? 8.580   -26.024 -36.944 1.00 24.92 ? 649 HOH   A O   1 
HETATM 2995 O O   . HOH   I 5 .   ? -17.413 -27.591 -35.174 1.00 33.79 ? 650 HOH   A O   1 
HETATM 2996 O O   . HOH   I 5 .   ? 33.595  -17.629 -47.182 1.00 31.47 ? 651 HOH   A O   1 
HETATM 2997 O O   . HOH   I 5 .   ? -9.604  -10.207 -21.196 1.00 32.73 ? 652 HOH   A O   1 
HETATM 2998 O O   . HOH   I 5 .   ? 10.825  -29.988 -42.570 1.00 36.17 ? 653 HOH   A O   1 
HETATM 2999 O O   . HOH   I 5 .   ? 3.174   -16.330 -58.451 1.00 28.11 ? 654 HOH   A O   1 
HETATM 3000 O O   . HOH   I 5 .   ? -19.683 2.091   -41.347 1.00 46.49 ? 655 HOH   A O   1 
HETATM 3001 O O   . HOH   I 5 .   ? 0.240   -6.046  -61.478 1.00 39.65 ? 656 HOH   A O   1 
HETATM 3002 O O   . HOH   I 5 .   ? 36.049  -16.645 -48.064 1.00 42.14 ? 657 HOH   A O   1 
HETATM 3003 O O   . HOH   I 5 .   ? 25.817  -11.126 -35.968 1.00 38.21 ? 658 HOH   A O   1 
HETATM 3004 O O   . HOH   I 5 .   ? -9.035  -5.603  -25.887 1.00 46.34 ? 659 HOH   A O   1 
HETATM 3005 O O   . HOH   I 5 .   ? 3.072   -15.920 -41.618 1.00 17.68 ? 660 HOH   A O   1 
HETATM 3006 O O   . HOH   I 5 .   ? -8.026  -9.741  -61.734 1.00 40.72 ? 661 HOH   A O   1 
HETATM 3007 O O   . HOH   I 5 .   ? 19.721  -0.615  -55.036 1.00 50.99 ? 662 HOH   A O   1 
HETATM 3008 O O   . HOH   I 5 .   ? -4.182  7.157   -48.484 1.00 51.65 ? 663 HOH   A O   1 
HETATM 3009 O O   . HOH   I 5 .   ? -17.689 -2.128  -57.439 1.00 50.37 ? 664 HOH   A O   1 
HETATM 3010 O O   . HOH   I 5 .   ? -3.183  -0.579  -32.706 1.00 46.89 ? 665 HOH   A O   1 
HETATM 3011 O O   . HOH   I 5 .   ? 2.605   -14.510 -24.199 1.00 35.83 ? 666 HOH   A O   1 
HETATM 3012 O O   . HOH   I 5 .   ? -2.568  2.806   -35.723 1.00 51.03 ? 667 HOH   A O   1 
HETATM 3013 O O   . HOH   I 5 .   ? -11.328 -3.673  -58.152 1.00 34.69 ? 668 HOH   A O   1 
HETATM 3014 O O   . HOH   I 5 .   ? -20.096 -22.650 -30.759 1.00 45.43 ? 669 HOH   A O   1 
HETATM 3015 O O   . HOH   I 5 .   ? -6.948  6.248   -52.343 1.00 34.49 ? 670 HOH   A O   1 
HETATM 3016 O O   . HOH   I 5 .   ? -18.625 -10.643 -40.235 1.00 44.86 ? 671 HOH   A O   1 
HETATM 3017 O O   . HOH   I 5 .   ? 27.636  -16.017 -56.104 1.00 57.79 ? 672 HOH   A O   1 
HETATM 3018 O O   . HOH   I 5 .   ? 1.241   1.694   -57.449 1.00 46.48 ? 673 HOH   A O   1 
HETATM 3019 O O   . HOH   I 5 .   ? 32.135  -24.351 -51.051 1.00 41.60 ? 674 HOH   A O   1 
HETATM 3020 O O   . HOH   I 5 .   ? -18.646 -6.568  -48.547 1.00 42.17 ? 675 HOH   A O   1 
HETATM 3021 O O   . HOH   I 5 .   ? 5.383   -34.694 -37.107 1.00 36.16 ? 676 HOH   A O   1 
HETATM 3022 O O   . HOH   I 5 .   ? -11.957 -25.518 -24.100 1.00 31.85 ? 677 HOH   A O   1 
HETATM 3023 O O   . HOH   I 5 .   ? 5.460   -25.878 -30.628 1.00 34.56 ? 678 HOH   A O   1 
HETATM 3024 O O   . HOH   I 5 .   ? -3.474  -21.741 -25.794 1.00 44.81 ? 679 HOH   A O   1 
HETATM 3025 O O   . HOH   I 5 .   ? -12.922 -23.323 -22.731 1.00 33.14 ? 680 HOH   A O   1 
HETATM 3026 O O   . HOH   I 5 .   ? -18.830 -7.153  -43.094 1.00 41.07 ? 681 HOH   A O   1 
HETATM 3027 O O   . HOH   I 5 .   ? -1.686  -31.570 -33.977 1.00 49.76 ? 682 HOH   A O   1 
HETATM 3028 O O   . HOH   I 5 .   ? 10.795  -10.780 -58.921 1.00 42.64 ? 683 HOH   A O   1 
HETATM 3029 O O   . HOH   I 5 .   ? -1.591  -30.094 -32.101 1.00 29.46 ? 684 HOH   A O   1 
HETATM 3030 O O   . HOH   I 5 .   ? -16.662 11.831  -39.173 1.00 51.15 ? 685 HOH   A O   1 
HETATM 3031 O O   . HOH   I 5 .   ? 30.341  -26.977 -47.330 1.00 50.42 ? 686 HOH   A O   1 
HETATM 3032 O O   . HOH   I 5 .   ? -21.183 -5.528  -35.668 1.00 38.75 ? 687 HOH   A O   1 
HETATM 3033 O O   . HOH   I 5 .   ? -5.683  -22.513 -26.110 1.00 36.53 ? 688 HOH   A O   1 
HETATM 3034 O O   . HOH   I 5 .   ? -12.785 -37.693 -30.220 1.00 48.15 ? 689 HOH   A O   1 
HETATM 3035 O O   . HOH   I 5 .   ? 12.056  -8.792  -37.504 1.00 47.32 ? 690 HOH   A O   1 
HETATM 3036 O O   . HOH   I 5 .   ? -13.213 -10.588 -22.915 1.00 30.28 ? 691 HOH   A O   1 
HETATM 3037 O O   . HOH   I 5 .   ? 33.756  -5.545  -44.197 1.00 37.39 ? 692 HOH   A O   1 
HETATM 3038 O O   . HOH   I 5 .   ? 10.142  -23.322 -60.276 1.00 41.03 ? 693 HOH   A O   1 
HETATM 3039 O O   . HOH   I 5 .   ? 17.518  -36.703 -54.019 1.00 44.20 ? 694 HOH   A O   1 
HETATM 3040 O O   . HOH   I 5 .   ? 17.359  -29.124 -54.805 1.00 38.30 ? 695 HOH   A O   1 
HETATM 3041 O O   . HOH   I 5 .   ? -10.787 1.304   -37.250 1.00 31.96 ? 696 HOH   A O   1 
HETATM 3042 O O   . HOH   I 5 .   ? 27.890  -27.574 -45.728 1.00 46.91 ? 697 HOH   A O   1 
HETATM 3043 O O   . HOH   I 5 .   ? -17.954 -10.968 -22.277 1.00 39.50 ? 698 HOH   A O   1 
HETATM 3044 O O   . HOH   I 5 .   ? -3.255  -30.809 -53.434 1.00 52.72 ? 699 HOH   A O   1 
HETATM 3045 O O   . HOH   I 5 .   ? 37.444  -15.762 -34.957 1.00 32.35 ? 700 HOH   A O   1 
HETATM 3046 O O   . HOH   I 5 .   ? 4.234   -6.051  -61.515 1.00 51.86 ? 701 HOH   A O   1 
HETATM 3047 O O   . HOH   I 5 .   ? 17.400  0.501   -41.069 1.00 49.67 ? 702 HOH   A O   1 
HETATM 3048 O O   . HOH   I 5 .   ? 27.879  -29.189 -43.857 1.00 59.45 ? 703 HOH   A O   1 
HETATM 3049 O O   . HOH   I 5 .   ? 5.365   -23.208 -59.454 1.00 50.34 ? 704 HOH   A O   1 
HETATM 3050 O O   . HOH   I 5 .   ? -7.943  -30.935 -45.822 1.00 43.57 ? 705 HOH   A O   1 
HETATM 3051 O O   . HOH   I 5 .   ? -6.685  -30.434 -26.364 1.00 46.60 ? 706 HOH   A O   1 
HETATM 3052 O O   . HOH   I 5 .   ? -22.172 -8.279  -42.851 1.00 41.90 ? 707 HOH   A O   1 
HETATM 3053 O O   . HOH   I 5 .   ? 19.061  -21.599 -57.422 1.00 54.02 ? 708 HOH   A O   1 
HETATM 3054 O O   . HOH   I 5 .   ? -3.250  -12.475 -20.170 1.00 49.21 ? 709 HOH   A O   1 
HETATM 3055 O O   . HOH   I 5 .   ? -16.295 8.993   -38.990 1.00 34.76 ? 710 HOH   A O   1 
HETATM 3056 O O   . HOH   I 5 .   ? -6.513  6.173   -38.306 1.00 46.29 ? 711 HOH   A O   1 
HETATM 3057 O O   . HOH   I 5 .   ? -5.000  -10.905 -20.284 1.00 44.69 ? 712 HOH   A O   1 
HETATM 3058 O O   . HOH   I 5 .   ? 0.511   -8.319  -62.776 1.00 51.52 ? 713 HOH   A O   1 
HETATM 3059 O O   . HOH   I 5 .   ? -7.422  -28.514 -20.828 1.00 47.81 ? 714 HOH   A O   1 
HETATM 3060 O O   . HOH   I 5 .   ? -7.940  -32.204 -43.874 1.00 42.15 ? 715 HOH   A O   1 
HETATM 3061 O O   . HOH   I 5 .   ? 3.179   -19.508 -28.853 1.00 51.64 ? 716 HOH   A O   1 
HETATM 3062 O O   . HOH   I 5 .   ? -5.517  -15.660 -17.187 1.00 41.09 ? 717 HOH   A O   1 
HETATM 3063 O O   . HOH   I 5 .   ? -17.722 -21.844 -37.749 1.00 35.61 ? 718 HOH   A O   1 
HETATM 3064 O O   . HOH   I 5 .   ? -19.703 -2.882  -55.053 1.00 49.15 ? 719 HOH   A O   1 
HETATM 3065 O O   . HOH   I 5 .   ? -15.521 -28.164 -42.419 1.00 49.41 ? 720 HOH   A O   1 
HETATM 3066 O O   . HOH   I 5 .   ? -2.074  -23.087 -24.531 1.00 50.32 ? 721 HOH   A O   1 
HETATM 3067 O O   . HOH   I 5 .   ? 32.610  -8.292  -44.657 1.00 55.04 ? 722 HOH   A O   1 
HETATM 3068 O O   . HOH   I 5 .   ? -5.718  -27.173 -22.815 1.00 46.09 ? 723 HOH   A O   1 
HETATM 3069 O O   . HOH   I 5 .   ? -20.690 -21.442 -37.955 1.00 42.14 ? 724 HOH   A O   1 
HETATM 3070 O O   . HOH   I 5 .   ? -9.787  -5.139  -28.379 1.00 37.50 ? 725 HOH   A O   1 
HETATM 3071 O O   . HOH   I 5 .   ? 12.733  -11.576 -57.777 1.00 44.14 ? 726 HOH   A O   1 
HETATM 3072 O O   . HOH   I 5 .   ? -14.635 -5.096  -58.641 1.00 47.55 ? 727 HOH   A O   1 
HETATM 3073 O O   . HOH   I 5 .   ? -14.574 -24.530 -37.834 1.00 32.31 ? 728 HOH   A O   1 
HETATM 3074 O O   . HOH   I 5 .   ? 2.181   -18.596 -25.077 1.00 48.40 ? 729 HOH   A O   1 
HETATM 3075 O O   . HOH   I 5 .   ? 36.050  -19.484 -37.923 1.00 41.56 ? 730 HOH   A O   1 
HETATM 3076 O O   . HOH   I 5 .   ? 23.774  -30.679 -51.709 1.00 49.38 ? 731 HOH   A O   1 
HETATM 3077 O O   . HOH   I 5 .   ? 7.236   -27.820 -30.872 1.00 48.21 ? 732 HOH   A O   1 
HETATM 3078 O O   . HOH   I 5 .   ? 6.016   -24.607 -28.507 1.00 53.33 ? 733 HOH   A O   1 
HETATM 3079 O O   . HOH   I 5 .   ? 1.246   -23.002 -59.637 1.00 54.84 ? 734 HOH   A O   1 
HETATM 3080 O O   . HOH   I 5 .   ? -19.854 -17.250 -40.354 1.00 37.01 ? 735 HOH   A O   1 
HETATM 3081 O O   . HOH   I 5 .   ? -17.822 -7.939  -45.504 1.00 49.82 ? 736 HOH   A O   1 
HETATM 3082 O O   . HOH   I 5 .   ? 14.410  6.744   -62.068 1.00 53.54 ? 737 HOH   A O   1 
HETATM 3083 O O   . HOH   I 5 .   ? -17.172 -26.043 -37.588 1.00 50.39 ? 738 HOH   A O   1 
HETATM 3084 O O   . HOH   I 5 .   ? -15.295 -9.741  -21.696 1.00 43.66 ? 739 HOH   A O   1 
HETATM 3085 O O   . HOH   I 5 .   ? 1.775   -22.848 -27.013 1.00 47.38 ? 740 HOH   A O   1 
HETATM 3086 O O   . HOH   I 5 .   ? -0.256  -19.259 -26.562 1.00 50.26 ? 741 HOH   A O   1 
HETATM 3087 O O   . HOH   I 5 .   ? -17.758 -30.197 -34.736 1.00 48.77 ? 742 HOH   A O   1 
HETATM 3088 O O   . HOH   I 5 .   ? 36.583  -17.937 -41.854 1.00 44.72 ? 743 HOH   A O   1 
HETATM 3089 O O   . HOH   I 5 .   ? -20.841 -24.064 -29.069 1.00 54.85 ? 744 HOH   A O   1 
HETATM 3090 O O   . HOH   I 5 .   ? -14.131 -1.818  -58.063 1.00 55.52 ? 745 HOH   A O   1 
HETATM 3091 O O   . HOH   I 5 .   ? -18.438 -24.427 -38.676 1.00 55.92 ? 746 HOH   A O   1 
HETATM 3092 O O   . HOH   I 5 .   ? 36.007  -15.429 -31.525 1.00 43.34 ? 747 HOH   A O   1 
HETATM 3093 O O   . HOH   I 5 .   ? 4.334   -21.955 -27.270 1.00 47.51 ? 748 HOH   A O   1 
HETATM 3094 O O   . HOH   I 5 .   ? -19.717 -9.389  -42.118 1.00 47.69 ? 749 HOH   A O   1 
HETATM 3095 O O   . HOH   I 5 .   ? -13.475 -15.350 -53.212 1.00 35.33 ? 750 HOH   A O   1 
HETATM 3096 O O   . HOH   I 5 .   ? -14.348 -18.249 -49.191 1.00 43.19 ? 751 HOH   A O   1 
HETATM 3097 O O   . HOH   I 5 .   ? 3.275   -14.692 -60.505 1.00 36.51 ? 752 HOH   A O   1 
HETATM 3098 O O   . HOH   I 5 .   ? -14.206 -17.602 -52.066 1.00 39.06 ? 753 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   ? 0.6497 0.5479 0.5717 -0.0566 -0.0053 0.0008  3   GLY A N   
2    C CA  . GLY A 1   ? 0.6530 0.5546 0.5818 -0.0508 -0.0043 -0.0033 3   GLY A CA  
3    C C   . GLY A 1   ? 0.6231 0.5302 0.5520 -0.0509 -0.0008 -0.0097 3   GLY A C   
4    O O   . GLY A 1   ? 0.6389 0.5472 0.5626 -0.0554 0.0010  -0.0111 3   GLY A O   
5    N N   . PRO A 2   ? 0.6704 0.5810 0.6052 -0.0461 0.0000  -0.0134 4   PRO A N   
6    C CA  . PRO A 2   ? 0.6304 0.5463 0.5658 -0.0461 0.0030  -0.0191 4   PRO A CA  
7    C C   . PRO A 2   ? 0.5696 0.4770 0.5053 -0.0471 0.0062  -0.0220 4   PRO A C   
8    O O   . PRO A 2   ? 0.5718 0.4692 0.5103 -0.0452 0.0064  -0.0213 4   PRO A O   
9    C CB  . PRO A 2   ? 0.6969 0.6176 0.6389 -0.0407 0.0024  -0.0214 4   PRO A CB  
10   C CG  . PRO A 2   ? 0.7280 0.6481 0.6719 -0.0384 -0.0011 -0.0167 4   PRO A CG  
11   C CD  . PRO A 2   ? 0.7118 0.6221 0.6530 -0.0407 -0.0020 -0.0123 4   PRO A CD  
12   N N   . VAL A 3   ? 0.4164 0.3281 0.3492 -0.0500 0.0087  -0.0254 5   VAL A N   
13   C CA  . VAL A 3   ? 0.3980 0.3034 0.3307 -0.0515 0.0120  -0.0287 5   VAL A CA  
14   C C   . VAL A 3   ? 0.3752 0.2795 0.3150 -0.0467 0.0135  -0.0325 5   VAL A C   
15   O O   . VAL A 3   ? 0.3861 0.2982 0.3293 -0.0438 0.0129  -0.0342 5   VAL A O   
16   C CB  . VAL A 3   ? 0.3790 0.2912 0.3069 -0.0560 0.0140  -0.0310 5   VAL A CB  
17   C CG1 . VAL A 3   ? 0.4193 0.3267 0.3473 -0.0576 0.0175  -0.0347 5   VAL A CG1 
18   C CG2 . VAL A 3   ? 0.4412 0.3548 0.3619 -0.0611 0.0126  -0.0271 5   VAL A CG2 
19   N N   . PRO A 4   ? 0.3563 0.2513 0.2985 -0.0457 0.0152  -0.0341 6   PRO A N   
20   C CA  . PRO A 4   ? 0.3609 0.2557 0.3099 -0.0413 0.0167  -0.0378 6   PRO A CA  
21   C C   . PRO A 4   ? 0.3738 0.2753 0.3230 -0.0428 0.0195  -0.0424 6   PRO A C   
22   O O   . PRO A 4   ? 0.3723 0.2765 0.3164 -0.0473 0.0208  -0.0430 6   PRO A O   
23   C CB  . PRO A 4   ? 0.4178 0.3007 0.3686 -0.0404 0.0178  -0.0382 6   PRO A CB  
24   C CG  . PRO A 4   ? 0.5078 0.3851 0.4516 -0.0460 0.0183  -0.0364 6   PRO A CG  
25   C CD  . PRO A 4   ? 0.4544 0.3382 0.3935 -0.0484 0.0156  -0.0323 6   PRO A CD  
26   N N   . SER A 5   ? 0.3237 0.2280 0.2789 -0.0390 0.0203  -0.0453 7   SER A N   
27   C CA  . SER A 5   ? 0.3248 0.2359 0.2811 -0.0399 0.0225  -0.0493 7   SER A CA  
28   C C   . SER A 5   ? 0.3166 0.2250 0.2787 -0.0371 0.0245  -0.0527 7   SER A C   
29   O O   . SER A 5   ? 0.3716 0.2763 0.3383 -0.0330 0.0235  -0.0520 7   SER A O   
30   C CB  . SER A 5   ? 0.3561 0.2774 0.3137 -0.0386 0.0207  -0.0490 7   SER A CB  
31   O OG  . SER A 5   ? 0.3551 0.2828 0.3145 -0.0391 0.0225  -0.0523 7   SER A OG  
32   N N   . ARG A 6   ? 0.3346 0.2458 0.2965 -0.0394 0.0274  -0.0563 8   ARG A N   
33   C CA  . ARG A 6   ? 0.3270 0.2382 0.2941 -0.0375 0.0295  -0.0600 8   ARG A CA  
34   C C   . ARG A 6   ? 0.3752 0.2963 0.3438 -0.0384 0.0304  -0.0622 8   ARG A C   
35   O O   . ARG A 6   ? 0.3623 0.2881 0.3269 -0.0419 0.0306  -0.0617 8   ARG A O   
36   C CB  . ARG A 6   ? 0.3985 0.3023 0.3638 -0.0401 0.0326  -0.0626 8   ARG A CB  
37   C CG  . ARG A 6   ? 0.5376 0.4304 0.5020 -0.0392 0.0320  -0.0609 8   ARG A CG  
38   C CD  . ARG A 6   ? 0.6161 0.5061 0.5873 -0.0333 0.0309  -0.0610 8   ARG A CD  
39   N NE  . ARG A 6   ? 0.6127 0.4912 0.5839 -0.0321 0.0306  -0.0599 8   ARG A NE  
40   C CZ  . ARG A 6   ? 0.5750 0.4485 0.5447 -0.0311 0.0277  -0.0552 8   ARG A CZ  
41   N NH1 . ARG A 6   ? 0.4992 0.3789 0.4670 -0.0313 0.0249  -0.0515 8   ARG A NH1 
42   N NH2 . ARG A 6   ? 0.5557 0.4183 0.5260 -0.0301 0.0275  -0.0543 8   ARG A NH2 
43   N N   . ALA A 7   ? 0.3013 0.2256 0.2758 -0.0355 0.0309  -0.0644 9   ALA A N   
44   C CA  . ALA A 7   ? 0.3002 0.2330 0.2764 -0.0370 0.0320  -0.0666 9   ALA A CA  
45   C C   . ALA A 7   ? 0.2898 0.2222 0.2624 -0.0418 0.0352  -0.0689 9   ALA A C   
46   O O   . ALA A 7   ? 0.3669 0.2925 0.3383 -0.0429 0.0372  -0.0704 9   ALA A O   
47   C CB  . ALA A 7   ? 0.3027 0.2387 0.2857 -0.0335 0.0322  -0.0685 9   ALA A CB  
48   N N   . ARG A 8   ? 0.3250 0.2649 0.2960 -0.0447 0.0356  -0.0691 10  ARG A N   
49   C CA  . ARG A 8   ? 0.2931 0.2340 0.2608 -0.0495 0.0385  -0.0711 10  ARG A CA  
50   C C   . ARG A 8   ? 0.3143 0.2586 0.2861 -0.0498 0.0408  -0.0745 10  ARG A C   
51   O O   . ARG A 8   ? 0.3379 0.2824 0.3072 -0.0538 0.0435  -0.0766 10  ARG A O   
52   C CB  . ARG A 8   ? 0.3433 0.2910 0.3076 -0.0526 0.0379  -0.0697 10  ARG A CB  
53   C CG  . ARG A 8   ? 0.4107 0.3570 0.3708 -0.0527 0.0357  -0.0666 10  ARG A CG  
54   C CD  . ARG A 8   ? 0.5220 0.4759 0.4792 -0.0557 0.0356  -0.0658 10  ARG A CD  
55   N NE  . ARG A 8   ? 0.6445 0.6063 0.6064 -0.0539 0.0345  -0.0662 10  ARG A NE  
56   C CZ  . ARG A 8   ? 0.6726 0.6416 0.6341 -0.0562 0.0349  -0.0664 10  ARG A CZ  
57   N NH1 . ARG A 8   ? 0.6667 0.6369 0.6232 -0.0606 0.0365  -0.0663 10  ARG A NH1 
58   N NH2 . ARG A 8   ? 0.6451 0.6202 0.6113 -0.0543 0.0336  -0.0666 10  ARG A NH2 
59   N N   . VAL A 9   ? 0.3099 0.2572 0.2876 -0.0461 0.0397  -0.0750 11  VAL A N   
60   C CA  . VAL A 9   ? 0.3027 0.2540 0.2847 -0.0462 0.0418  -0.0781 11  VAL A CA  
61   C C   . VAL A 9   ? 0.3208 0.2694 0.3082 -0.0412 0.0410  -0.0788 11  VAL A C   
62   O O   . VAL A 9   ? 0.2997 0.2457 0.2882 -0.0376 0.0384  -0.0764 11  VAL A O   
63   C CB  . VAL A 9   ? 0.2968 0.2583 0.2811 -0.0476 0.0411  -0.0778 11  VAL A CB  
64   C CG1 . VAL A 9   ? 0.3100 0.2749 0.2896 -0.0523 0.0419  -0.0770 11  VAL A CG1 
65   C CG2 . VAL A 9   ? 0.3058 0.2705 0.2934 -0.0440 0.0377  -0.0753 11  VAL A CG2 
66   N N   . TYR A 10  ? 0.2793 0.2292 0.2701 -0.0411 0.0434  -0.0822 12  TYR A N   
67   C CA  . TYR A 10  ? 0.3270 0.2757 0.3235 -0.0364 0.0431  -0.0835 12  TYR A CA  
68   C C   . TYR A 10  ? 0.3179 0.2568 0.3139 -0.0329 0.0419  -0.0820 12  TYR A C   
69   O O   . TYR A 10  ? 0.3353 0.2737 0.3357 -0.0282 0.0401  -0.0811 12  TYR A O   
70   C CB  . TYR A 10  ? 0.3068 0.2633 0.3080 -0.0340 0.0406  -0.0820 12  TYR A CB  
71   C CG  . TYR A 10  ? 0.3111 0.2771 0.3133 -0.0374 0.0414  -0.0828 12  TYR A CG  
72   C CD1 . TYR A 10  ? 0.2861 0.2555 0.2891 -0.0402 0.0445  -0.0862 12  TYR A CD1 
73   C CD2 . TYR A 10  ? 0.2709 0.2426 0.2734 -0.0379 0.0388  -0.0800 12  TYR A CD2 
74   C CE1 . TYR A 10  ? 0.3110 0.2897 0.3151 -0.0436 0.0449  -0.0864 12  TYR A CE1 
75   C CE2 . TYR A 10  ? 0.3113 0.2913 0.3150 -0.0410 0.0391  -0.0802 12  TYR A CE2 
76   C CZ  . TYR A 10  ? 0.2690 0.2526 0.2734 -0.0439 0.0421  -0.0832 12  TYR A CZ  
77   O OH  . TYR A 10  ? 0.3268 0.3192 0.3326 -0.0473 0.0422  -0.0829 12  TYR A OH  
78   N N   . THR A 11  ? 0.3397 0.2713 0.3303 -0.0353 0.0427  -0.0817 13  THR A N   
79   C CA  . THR A 11  ? 0.3131 0.2354 0.3025 -0.0327 0.0411  -0.0793 13  THR A CA  
80   C C   . THR A 11  ? 0.3477 0.2645 0.3420 -0.0284 0.0419  -0.0814 13  THR A C   
81   O O   . THR A 11  ? 0.3788 0.2918 0.3755 -0.0241 0.0395  -0.0790 13  THR A O   
82   C CB  . THR A 11  ? 0.3655 0.2811 0.3480 -0.0370 0.0421  -0.0787 13  THR A CB  
83   O OG1 . THR A 11  ? 0.4154 0.3376 0.3938 -0.0413 0.0422  -0.0778 13  THR A OG1 
84   C CG2 . THR A 11  ? 0.3811 0.2888 0.3615 -0.0351 0.0396  -0.0750 13  THR A CG2 
85   N N   . ASP A 12  ? 0.3634 0.2802 0.3593 -0.0295 0.0452  -0.0861 14  ASP A N   
86   C CA  . ASP A 12  ? 0.3514 0.2619 0.3515 -0.0258 0.0465  -0.0889 14  ASP A CA  
87   C C   . ASP A 12  ? 0.3600 0.2782 0.3671 -0.0226 0.0474  -0.0919 14  ASP A C   
88   O O   . ASP A 12  ? 0.3579 0.2729 0.3687 -0.0202 0.0494  -0.0957 14  ASP A O   
89   C CB  . ASP A 12  ? 0.3895 0.2929 0.3861 -0.0293 0.0498  -0.0926 14  ASP A CB  
90   C CG  . ASP A 12  ? 0.5473 0.4452 0.5362 -0.0339 0.0493  -0.0899 14  ASP A CG  
91   O OD1 . ASP A 12  ? 0.6227 0.5236 0.6073 -0.0393 0.0514  -0.0916 14  ASP A OD1 
92   O OD2 . ASP A 12  ? 0.5426 0.4339 0.5298 -0.0323 0.0467  -0.0859 14  ASP A OD2 
93   N N   . VAL A 13  ? 0.3438 0.2721 0.3529 -0.0226 0.0459  -0.0903 15  VAL A N   
94   C CA  . VAL A 13  ? 0.3115 0.2483 0.3268 -0.0206 0.0467  -0.0930 15  VAL A CA  
95   C C   . VAL A 13  ? 0.3530 0.2865 0.3743 -0.0144 0.0460  -0.0935 15  VAL A C   
96   O O   . VAL A 13  ? 0.3413 0.2765 0.3669 -0.0126 0.0484  -0.0977 15  VAL A O   
97   C CB  . VAL A 13  ? 0.3343 0.2813 0.3506 -0.0215 0.0445  -0.0903 15  VAL A CB  
98   C CG1 . VAL A 13  ? 0.3660 0.3208 0.3893 -0.0182 0.0442  -0.0917 15  VAL A CG1 
99   C CG2 . VAL A 13  ? 0.3300 0.2827 0.3425 -0.0274 0.0461  -0.0912 15  VAL A CG2 
100  N N   . ASN A 14  ? 0.3286 0.2580 0.3504 -0.0109 0.0427  -0.0892 16  ASN A N   
101  C CA  . ASN A 14  ? 0.3193 0.2464 0.3472 -0.0049 0.0417  -0.0891 16  ASN A CA  
102  C C   . ASN A 14  ? 0.3575 0.2735 0.3856 -0.0030 0.0435  -0.0913 16  ASN A C   
103  O O   . ASN A 14  ? 0.3838 0.2985 0.4178 0.0018  0.0440  -0.0935 16  ASN A O   
104  C CB  . ASN A 14  ? 0.3589 0.2859 0.3872 -0.0020 0.0376  -0.0837 16  ASN A CB  
105  C CG  . ASN A 14  ? 0.3425 0.2806 0.3726 -0.0025 0.0358  -0.0823 16  ASN A CG  
106  O OD1 . ASN A 14  ? 0.3589 0.3049 0.3935 -0.0019 0.0370  -0.0849 16  ASN A OD1 
107  N ND2 . ASN A 14  ? 0.3094 0.2485 0.3360 -0.0040 0.0330  -0.0782 16  ASN A ND2 
108  N N   . THR A 15  ? 0.3526 0.2604 0.3744 -0.0067 0.0442  -0.0910 17  THR A N   
109  C CA  . THR A 15  ? 0.4197 0.3161 0.4413 -0.0056 0.0459  -0.0933 17  THR A CA  
110  C C   . THR A 15  ? 0.4510 0.3495 0.4770 -0.0046 0.0497  -0.0999 17  THR A C   
111  O O   . THR A 15  ? 0.5363 0.4284 0.5667 -0.0002 0.0504  -0.1022 17  THR A O   
112  C CB  . THR A 15  ? 0.4889 0.3784 0.5025 -0.0113 0.0467  -0.0925 17  THR A CB  
113  O OG1 . THR A 15  ? 0.5512 0.4385 0.5608 -0.0119 0.0432  -0.0865 17  THR A OG1 
114  C CG2 . THR A 15  ? 0.5898 0.4674 0.6030 -0.0108 0.0487  -0.0956 17  THR A CG2 
115  N N   . HIS A 16  ? 0.4299 0.3377 0.4549 -0.0086 0.0521  -0.1032 18  HIS A N   
116  C CA  . HIS A 16  ? 0.4228 0.3332 0.4508 -0.0088 0.0560  -0.1099 18  HIS A CA  
117  C C   . HIS A 16  ? 0.4182 0.3408 0.4530 -0.0060 0.0563  -0.1118 18  HIS A C   
118  O O   . HIS A 16  ? 0.4002 0.3264 0.4384 -0.0057 0.0595  -0.1176 18  HIS A O   
119  C CB  . HIS A 16  ? 0.5377 0.4496 0.5597 -0.0159 0.0588  -0.1126 18  HIS A CB  
120  C CG  . HIS A 16  ? 0.6585 0.5585 0.6740 -0.0188 0.0587  -0.1111 18  HIS A CG  
121  N ND1 . HIS A 16  ? 0.6816 0.5700 0.6971 -0.0176 0.0604  -0.1143 18  HIS A ND1 
122  C CD2 . HIS A 16  ? 0.6787 0.5764 0.6877 -0.0227 0.0570  -0.1066 18  HIS A CD2 
123  C CE1 . HIS A 16  ? 0.7051 0.5847 0.7141 -0.0211 0.0597  -0.1117 18  HIS A CE1 
124  N NE2 . HIS A 16  ? 0.6750 0.5604 0.6799 -0.0242 0.0576  -0.1070 18  HIS A NE2 
125  N N   . ARG A 17  ? 0.4172 0.3462 0.4540 -0.0041 0.0531  -0.1073 19  ARG A N   
126  C CA  . ARG A 17  ? 0.4068 0.3454 0.4507 -0.0002 0.0527  -0.1084 19  ARG A CA  
127  C C   . ARG A 17  ? 0.3852 0.3176 0.4350 0.0066  0.0525  -0.1096 19  ARG A C   
128  O O   . ARG A 17  ? 0.4761 0.3970 0.5245 0.0087  0.0512  -0.1073 19  ARG A O   
129  C CB  . ARG A 17  ? 0.4149 0.3605 0.4592 0.0001  0.0490  -0.1030 19  ARG A CB  
130  C CG  . ARG A 17  ? 0.5010 0.4543 0.5411 -0.0058 0.0488  -0.1017 19  ARG A CG  
131  C CD  . ARG A 17  ? 0.4567 0.4233 0.5013 -0.0063 0.0490  -0.1030 19  ARG A CD  
132  N NE  . ARG A 17  ? 0.3748 0.3485 0.4158 -0.0121 0.0491  -0.1022 19  ARG A NE  
133  C CZ  . ARG A 17  ? 0.4061 0.3913 0.4498 -0.0144 0.0501  -0.1040 19  ARG A CZ  
134  N NH1 . ARG A 17  ? 0.3611 0.3520 0.4109 -0.0113 0.0513  -0.1070 19  ARG A NH1 
135  N NH2 . ARG A 17  ? 0.4762 0.4673 0.5168 -0.0196 0.0499  -0.1027 19  ARG A NH2 
136  N N   . PRO A 18  ? 0.3773 0.3175 0.4341 0.0101  0.0538  -0.1130 20  PRO A N   
137  C CA  . PRO A 18  ? 0.3717 0.3072 0.4349 0.0173  0.0531  -0.1135 20  PRO A CA  
138  C C   . PRO A 18  ? 0.3800 0.3135 0.4441 0.0206  0.0485  -0.1066 20  PRO A C   
139  O O   . PRO A 18  ? 0.3468 0.2864 0.4084 0.0182  0.0461  -0.1024 20  PRO A O   
140  C CB  . PRO A 18  ? 0.3995 0.3473 0.4695 0.0194  0.0551  -0.1180 20  PRO A CB  
141  C CG  . PRO A 18  ? 0.4412 0.4011 0.5086 0.0140  0.0549  -0.1170 20  PRO A CG  
142  C CD  . PRO A 18  ? 0.4019 0.3562 0.4611 0.0077  0.0555  -0.1161 20  PRO A CD  
143  N N   . ARG A 19  ? 0.3998 0.3245 0.4674 0.0262  0.0473  -0.1054 21  ARG A N   
144  C CA  . ARG A 19  ? 0.3757 0.2981 0.4439 0.0293  0.0429  -0.0987 21  ARG A CA  
145  C C   . ARG A 19  ? 0.3687 0.3043 0.4411 0.0309  0.0409  -0.0966 21  ARG A C   
146  O O   . ARG A 19  ? 0.4000 0.3379 0.4699 0.0298  0.0376  -0.0913 21  ARG A O   
147  C CB  . ARG A 19  ? 0.4939 0.4060 0.5667 0.0355  0.0420  -0.0980 21  ARG A CB  
148  C CG  . ARG A 19  ? 0.5543 0.4676 0.6305 0.0401  0.0377  -0.0918 21  ARG A CG  
149  C CD  . ARG A 19  ? 0.7093 0.6096 0.7874 0.0446  0.0360  -0.0891 21  ARG A CD  
150  N NE  . ARG A 19  ? 0.8753 0.7651 0.9456 0.0404  0.0347  -0.0854 21  ARG A NE  
151  C CZ  . ARG A 19  ? 0.9654 0.8446 1.0318 0.0379  0.0368  -0.0881 21  ARG A CZ  
152  N NH1 . ARG A 19  ? 1.0016 0.8785 1.0713 0.0392  0.0406  -0.0949 21  ARG A NH1 
153  N NH2 . ARG A 19  ? 0.9506 0.8217 1.0099 0.0338  0.0353  -0.0842 21  ARG A NH2 
154  N N   . GLU A 20  ? 0.3874 0.3321 0.4659 0.0332  0.0429  -0.1010 22  GLU A N   
155  C CA  . GLU A 20  ? 0.3584 0.3162 0.4410 0.0342  0.0412  -0.0993 22  GLU A CA  
156  C C   . GLU A 20  ? 0.3482 0.3125 0.4254 0.0283  0.0397  -0.0966 22  GLU A C   
157  O O   . GLU A 20  ? 0.3608 0.3329 0.4398 0.0288  0.0370  -0.0931 22  GLU A O   
158  C CB  . GLU A 20  ? 0.4217 0.3891 0.5105 0.0360  0.0443  -0.1053 22  GLU A CB  
159  C CG  . GLU A 20  ? 0.6705 0.6401 0.7561 0.0308  0.0484  -0.1109 22  GLU A CG  
160  C CD  . GLU A 20  ? 0.8537 0.8280 0.9453 0.0335  0.0522  -0.1179 22  GLU A CD  
161  O OE1 . GLU A 20  ? 0.8901 0.8710 0.9802 0.0291  0.0553  -0.1224 22  GLU A OE1 
162  O OE2 . GLU A 20  ? 0.9231 0.8948 1.0209 0.0401  0.0520  -0.1189 22  GLU A OE2 
163  N N   . TYR A 21  ? 0.3069 0.2682 0.3778 0.0227  0.0415  -0.0980 23  TYR A N   
164  C CA  . TYR A 21  ? 0.3007 0.2685 0.3671 0.0172  0.0403  -0.0956 23  TYR A CA  
165  C C   . TYR A 21  ? 0.3139 0.2783 0.3771 0.0173  0.0362  -0.0894 23  TYR A C   
166  O O   . TYR A 21  ? 0.2894 0.2615 0.3527 0.0160  0.0338  -0.0868 23  TYR A O   
167  C CB  . TYR A 21  ? 0.3021 0.2674 0.3626 0.0114  0.0431  -0.0983 23  TYR A CB  
168  C CG  . TYR A 21  ? 0.2750 0.2463 0.3311 0.0060  0.0417  -0.0958 23  TYR A CG  
169  C CD1 . TYR A 21  ? 0.2951 0.2784 0.3533 0.0034  0.0423  -0.0972 23  TYR A CD1 
170  C CD2 . TYR A 21  ? 0.2920 0.2574 0.3420 0.0035  0.0397  -0.0919 23  TYR A CD2 
171  C CE1 . TYR A 21  ? 0.2510 0.2393 0.3058 -0.0012 0.0408  -0.0947 23  TYR A CE1 
172  C CE2 . TYR A 21  ? 0.2791 0.2500 0.3257 -0.0009 0.0385  -0.0898 23  TYR A CE2 
173  C CZ  . TYR A 21  ? 0.2815 0.2633 0.3305 -0.0032 0.0390  -0.0912 23  TYR A CZ  
174  O OH  . TYR A 21  ? 0.3046 0.2914 0.3507 -0.0074 0.0375  -0.0890 23  TYR A OH  
175  N N   . TRP A 22  ? 0.3208 0.2739 0.3811 0.0187  0.0352  -0.0871 24  TRP A N   
176  C CA  . TRP A 22  ? 0.3119 0.2617 0.3683 0.0181  0.0315  -0.0815 24  TRP A CA  
177  C C   . TRP A 22  ? 0.2903 0.2370 0.3506 0.0237  0.0286  -0.0778 24  TRP A C   
178  O O   . TRP A 22  ? 0.3237 0.2697 0.3815 0.0234  0.0254  -0.0730 24  TRP A O   
179  C CB  . TRP A 22  ? 0.3236 0.2639 0.3726 0.0143  0.0322  -0.0807 24  TRP A CB  
180  C CG  . TRP A 22  ? 0.3093 0.2390 0.3584 0.0159  0.0344  -0.0831 24  TRP A CG  
181  C CD1 . TRP A 22  ? 0.3099 0.2366 0.3573 0.0132  0.0381  -0.0879 24  TRP A CD1 
182  C CD2 . TRP A 22  ? 0.3692 0.2895 0.4201 0.0202  0.0328  -0.0806 24  TRP A CD2 
183  N NE1 . TRP A 22  ? 0.3962 0.3119 0.4443 0.0158  0.0391  -0.0890 24  TRP A NE1 
184  C CE2 . TRP A 22  ? 0.4111 0.3224 0.4614 0.0201  0.0357  -0.0844 24  TRP A CE2 
185  C CE3 . TRP A 22  ? 0.4103 0.3290 0.4633 0.0241  0.0291  -0.0755 24  TRP A CE3 
186  C CZ2 . TRP A 22  ? 0.4581 0.3583 0.5101 0.0239  0.0350  -0.0831 24  TRP A CZ2 
187  C CZ3 . TRP A 22  ? 0.4440 0.3524 0.4987 0.0277  0.0283  -0.0739 24  TRP A CZ3 
188  C CH2 . TRP A 22  ? 0.4478 0.3468 0.5021 0.0277  0.0312  -0.0777 24  TRP A CH2 
189  N N   . ASP A 23  ? 0.3570 0.3022 0.4234 0.0287  0.0297  -0.0799 25  ASP A N   
190  C CA  . ASP A 23  ? 0.3287 0.2705 0.3992 0.0342  0.0269  -0.0762 25  ASP A CA  
191  C C   . ASP A 23  ? 0.3148 0.2682 0.3903 0.0366  0.0247  -0.0744 25  ASP A C   
192  O O   . ASP A 23  ? 0.3436 0.3018 0.4262 0.0410  0.0253  -0.0762 25  ASP A O   
193  C CB  . ASP A 23  ? 0.4020 0.3364 0.4771 0.0388  0.0290  -0.0792 25  ASP A CB  
194  C CG  . ASP A 23  ? 0.4901 0.4204 0.5698 0.0447  0.0260  -0.0749 25  ASP A CG  
195  O OD1 . ASP A 23  ? 0.4604 0.3913 0.5380 0.0445  0.0223  -0.0692 25  ASP A OD1 
196  O OD2 . ASP A 23  ? 0.5010 0.4278 0.5866 0.0497  0.0273  -0.0774 25  ASP A OD2 
197  N N   . TYR A 24  ? 0.3491 0.3072 0.4211 0.0335  0.0221  -0.0710 26  TYR A N   
198  C CA  . TYR A 24  ? 0.3526 0.3221 0.4285 0.0345  0.0201  -0.0696 26  TYR A CA  
199  C C   . TYR A 24  ? 0.3602 0.3305 0.4413 0.0401  0.0173  -0.0661 26  TYR A C   
200  O O   . TYR A 24  ? 0.3634 0.3435 0.4497 0.0421  0.0164  -0.0660 26  TYR A O   
201  C CB  . TYR A 24  ? 0.3167 0.2900 0.3873 0.0297  0.0180  -0.0671 26  TYR A CB  
202  C CG  . TYR A 24  ? 0.3304 0.2965 0.3955 0.0287  0.0154  -0.0627 26  TYR A CG  
203  C CD1 . TYR A 24  ? 0.3126 0.2715 0.3710 0.0248  0.0166  -0.0630 26  TYR A CD1 
204  C CD2 . TYR A 24  ? 0.3577 0.3252 0.4242 0.0312  0.0118  -0.0581 26  TYR A CD2 
205  C CE1 . TYR A 24  ? 0.3814 0.3349 0.4349 0.0235  0.0143  -0.0591 26  TYR A CE1 
206  C CE2 . TYR A 24  ? 0.3612 0.3233 0.4226 0.0299  0.0095  -0.0541 26  TYR A CE2 
207  C CZ  . TYR A 24  ? 0.3945 0.3497 0.4494 0.0261  0.0108  -0.0547 26  TYR A CZ  
208  O OH  . TYR A 24  ? 0.5050 0.4557 0.5548 0.0245  0.0085  -0.0508 26  TYR A OH  
209  N N   . GLU A 25  ? 0.4016 0.3624 0.4818 0.0425  0.0159  -0.0630 27  GLU A N   
210  C CA  . GLU A 25  ? 0.4501 0.4117 0.5355 0.0479  0.0132  -0.0592 27  GLU A CA  
211  C C   . GLU A 25  ? 0.4395 0.4045 0.5333 0.0533  0.0150  -0.0624 27  GLU A C   
212  O O   . GLU A 25  ? 0.4864 0.4570 0.5859 0.0576  0.0128  -0.0599 27  GLU A O   
213  C CB  . GLU A 25  ? 0.4997 0.4499 0.5822 0.0490  0.0113  -0.0550 27  GLU A CB  
214  C CG  . GLU A 25  ? 0.6368 0.5854 0.7117 0.0443  0.0090  -0.0512 27  GLU A CG  
215  C CD  . GLU A 25  ? 0.7692 0.7061 0.8401 0.0440  0.0079  -0.0478 27  GLU A CD  
216  O OE1 . GLU A 25  ? 0.8019 0.7358 0.8760 0.0480  0.0054  -0.0437 27  GLU A OE1 
217  O OE2 . GLU A 25  ? 0.8125 0.7434 0.8771 0.0397  0.0095  -0.0491 27  GLU A OE2 
218  N N   . SER A 26  ? 0.4109 0.3735 0.5057 0.0531  0.0189  -0.0680 28  SER A N   
219  C CA  . SER A 26  ? 0.4535 0.4197 0.5562 0.0581  0.0211  -0.0720 28  SER A CA  
220  C C   . SER A 26  ? 0.4359 0.4155 0.5414 0.0565  0.0228  -0.0759 28  SER A C   
221  O O   . SER A 26  ? 0.4440 0.4287 0.5560 0.0601  0.0249  -0.0798 28  SER A O   
222  C CB  . SER A 26  ? 0.5264 0.4819 0.6291 0.0592  0.0244  -0.0764 28  SER A CB  
223  O OG  . SER A 26  ? 0.6410 0.5838 0.7416 0.0609  0.0226  -0.0726 28  SER A OG  
224  N N   . HIS A 27  ? 0.3792 0.3647 0.4799 0.0510  0.0219  -0.0748 29  HIS A N   
225  C CA  . HIS A 27  ? 0.3569 0.3548 0.4595 0.0485  0.0234  -0.0779 29  HIS A CA  
226  C C   . HIS A 27  ? 0.3709 0.3797 0.4807 0.0525  0.0216  -0.0766 29  HIS A C   
227  O O   . HIS A 27  ? 0.3975 0.4068 0.5082 0.0547  0.0180  -0.0717 29  HIS A O   
228  C CB  . HIS A 27  ? 0.3819 0.3825 0.4780 0.0419  0.0222  -0.0762 29  HIS A CB  
229  C CG  . HIS A 27  ? 0.3575 0.3701 0.4550 0.0386  0.0233  -0.0789 29  HIS A CG  
230  N ND1 . HIS A 27  ? 0.3777 0.3932 0.4761 0.0369  0.0271  -0.0842 29  HIS A ND1 
231  C CD2 . HIS A 27  ? 0.4101 0.4326 0.5084 0.0365  0.0209  -0.0768 29  HIS A CD2 
232  C CE1 . HIS A 27  ? 0.4110 0.4382 0.5108 0.0338  0.0270  -0.0849 29  HIS A CE1 
233  N NE2 . HIS A 27  ? 0.4198 0.4510 0.5195 0.0335  0.0232  -0.0805 29  HIS A NE2 
234  N N   . VAL A 28  ? 0.3548 0.3731 0.4697 0.0534  0.0240  -0.0810 30  VAL A N   
235  C CA  . VAL A 28  ? 0.3469 0.3773 0.4687 0.0567  0.0227  -0.0802 30  VAL A CA  
236  C C   . VAL A 28  ? 0.3800 0.4220 0.5002 0.0512  0.0222  -0.0805 30  VAL A C   
237  O O   . VAL A 28  ? 0.4268 0.4726 0.5459 0.0476  0.0251  -0.0847 30  VAL A O   
238  C CB  . VAL A 28  ? 0.3826 0.4161 0.5121 0.0622  0.0256  -0.0849 30  VAL A CB  
239  C CG1 . VAL A 28  ? 0.3782 0.4261 0.5147 0.0650  0.0242  -0.0842 30  VAL A CG1 
240  C CG2 . VAL A 28  ? 0.4120 0.4331 0.5435 0.0679  0.0254  -0.0840 30  VAL A CG2 
241  N N   . VAL A 29  ? 0.3734 0.4211 0.4935 0.0503  0.0185  -0.0760 31  VAL A N   
242  C CA  . VAL A 29  ? 0.3488 0.4059 0.4668 0.0447  0.0174  -0.0754 31  VAL A CA  
243  C C   . VAL A 29  ? 0.3459 0.4168 0.4703 0.0454  0.0189  -0.0784 31  VAL A C   
244  O O   . VAL A 29  ? 0.4181 0.4942 0.5490 0.0508  0.0187  -0.0785 31  VAL A O   
245  C CB  . VAL A 29  ? 0.3571 0.4152 0.4729 0.0436  0.0129  -0.0699 31  VAL A CB  
246  C CG1 . VAL A 29  ? 0.3902 0.4581 0.5048 0.0381  0.0115  -0.0693 31  VAL A CG1 
247  C CG2 . VAL A 29  ? 0.4045 0.4500 0.5136 0.0422  0.0117  -0.0672 31  VAL A CG2 
248  N N   . GLU A 30  ? 0.4417 0.5189 0.5643 0.0401  0.0204  -0.0809 32  GLU A N   
249  C CA  . GLU A 30  ? 0.4839 0.5758 0.6117 0.0394  0.0215  -0.0833 32  GLU A CA  
250  C C   . GLU A 30  ? 0.3927 0.4929 0.5199 0.0358  0.0177  -0.0791 32  GLU A C   
251  O O   . GLU A 30  ? 0.3825 0.4822 0.5048 0.0300  0.0166  -0.0779 32  GLU A O   
252  C CB  . GLU A 30  ? 0.6131 0.7079 0.7394 0.0352  0.0252  -0.0880 32  GLU A CB  
253  C CG  . GLU A 30  ? 0.7671 0.8519 0.8924 0.0374  0.0289  -0.0923 32  GLU A CG  
254  C CD  . GLU A 30  ? 0.8713 0.9595 1.0039 0.0438  0.0314  -0.0963 32  GLU A CD  
255  O OE1 . GLU A 30  ? 0.9145 0.9923 1.0482 0.0491  0.0317  -0.0963 32  GLU A OE1 
256  O OE2 . GLU A 30  ? 0.9147 1.0159 1.0520 0.0437  0.0330  -0.0993 32  GLU A OE2 
257  N N   . TRP A 31  ? 0.3433 0.4510 0.4757 0.0394  0.0155  -0.0770 33  TRP A N   
258  C CA  . TRP A 31  ? 0.2939 0.4088 0.4257 0.0362  0.0116  -0.0729 33  TRP A CA  
259  C C   . TRP A 31  ? 0.3103 0.4392 0.4446 0.0320  0.0122  -0.0745 33  TRP A C   
260  O O   . TRP A 31  ? 0.3445 0.4822 0.4841 0.0341  0.0147  -0.0779 33  TRP A O   
261  C CB  . TRP A 31  ? 0.3520 0.4698 0.4881 0.0414  0.0089  -0.0695 33  TRP A CB  
262  C CG  . TRP A 31  ? 0.3499 0.4550 0.4841 0.0455  0.0079  -0.0673 33  TRP A CG  
263  C CD1 . TRP A 31  ? 0.3764 0.4761 0.5142 0.0518  0.0096  -0.0685 33  TRP A CD1 
264  C CD2 . TRP A 31  ? 0.3309 0.4274 0.4592 0.0435  0.0050  -0.0633 33  TRP A CD2 
265  N NE1 . TRP A 31  ? 0.3893 0.4776 0.5237 0.0536  0.0078  -0.0651 33  TRP A NE1 
266  C CE2 . TRP A 31  ? 0.4033 0.4899 0.5318 0.0485  0.0050  -0.0620 33  TRP A CE2 
267  C CE3 . TRP A 31  ? 0.3029 0.3990 0.4259 0.0379  0.0023  -0.0609 33  TRP A CE3 
268  C CZ2 . TRP A 31  ? 0.4491 0.5265 0.5724 0.0478  0.0024  -0.0583 33  TRP A CZ2 
269  C CZ3 . TRP A 31  ? 0.4108 0.4977 0.5288 0.0376  -0.0001 -0.0577 33  TRP A CZ3 
270  C CH2 . TRP A 31  ? 0.4502 0.5284 0.5684 0.0424  0.0001  -0.0563 33  TRP A CH2 
271  N N   . GLY A 32  ? 0.2576 0.3888 0.3881 0.0260  0.0096  -0.0720 34  GLY A N   
272  C CA  . GLY A 32  ? 0.2316 0.3760 0.3641 0.0213  0.0091  -0.0723 34  GLY A CA  
273  C C   . GLY A 32  ? 0.2488 0.4030 0.3851 0.0221  0.0058  -0.0691 34  GLY A C   
274  O O   . GLY A 32  ? 0.2972 0.4493 0.4355 0.0271  0.0042  -0.0671 34  GLY A O   
275  N N   . ASN A 33  ? 0.2478 0.4128 0.3848 0.0168  0.0044  -0.0682 35  ASN A N   
276  C CA  . ASN A 33  ? 0.2492 0.4253 0.3898 0.0165  0.0012  -0.0653 35  ASN A CA  
277  C C   . ASN A 33  ? 0.2420 0.4131 0.3778 0.0123  -0.0031 -0.0612 35  ASN A C   
278  O O   . ASN A 33  ? 0.2406 0.4108 0.3727 0.0062  -0.0042 -0.0605 35  ASN A O   
279  C CB  . ASN A 33  ? 0.3202 0.5116 0.4645 0.0129  0.0022  -0.0669 35  ASN A CB  
280  C CG  . ASN A 33  ? 0.4792 0.6838 0.6288 0.0143  0.0001  -0.0650 35  ASN A CG  
281  O OD1 . ASN A 33  ? 0.6272 0.8302 0.7790 0.0195  -0.0013 -0.0633 35  ASN A OD1 
282  N ND2 . ASN A 33  ? 0.5025 0.7209 0.6544 0.0097  -0.0003 -0.0651 35  ASN A ND2 
283  N N   . GLN A 34  ? 0.2236 0.3920 0.3597 0.0156  -0.0058 -0.0583 36  GLN A N   
284  C CA  . GLN A 34  ? 0.2462 0.4097 0.3777 0.0119  -0.0098 -0.0548 36  GLN A CA  
285  C C   . GLN A 34  ? 0.2244 0.3979 0.3564 0.0057  -0.0125 -0.0531 36  GLN A C   
286  O O   . GLN A 34  ? 0.2199 0.3884 0.3474 0.0009  -0.0152 -0.0514 36  GLN A O   
287  C CB  . GLN A 34  ? 0.2943 0.4549 0.4265 0.0166  -0.0120 -0.0522 36  GLN A CB  
288  C CG  . GLN A 34  ? 0.2928 0.4471 0.4198 0.0133  -0.0158 -0.0492 36  GLN A CG  
289  C CD  . GLN A 34  ? 0.3243 0.4890 0.4530 0.0100  -0.0195 -0.0466 36  GLN A CD  
290  O OE1 . GLN A 34  ? 0.2973 0.4740 0.4313 0.0112  -0.0194 -0.0464 36  GLN A OE1 
291  N NE2 . GLN A 34  ? 0.3264 0.4866 0.4506 0.0058  -0.0227 -0.0447 36  GLN A NE2 
292  N N   . ASP A 35  ? 0.2597 0.4473 0.3970 0.0057  -0.0121 -0.0535 37  ASP A N   
293  C CA  . ASP A 35  ? 0.2850 0.4821 0.4227 -0.0005 -0.0151 -0.0515 37  ASP A CA  
294  C C   . ASP A 35  ? 0.2924 0.4902 0.4279 -0.0068 -0.0142 -0.0526 37  ASP A C   
295  O O   . ASP A 35  ? 0.2800 0.4851 0.4155 -0.0126 -0.0167 -0.0508 37  ASP A O   
296  C CB  . ASP A 35  ? 0.3879 0.6012 0.5320 0.0010  -0.0152 -0.0512 37  ASP A CB  
297  C CG  . ASP A 35  ? 0.6556 0.8749 0.8045 0.0054  -0.0108 -0.0549 37  ASP A CG  
298  O OD1 . ASP A 35  ? 0.7841 0.9992 0.9352 0.0123  -0.0091 -0.0561 37  ASP A OD1 
299  O OD2 . ASP A 35  ? 0.7581 0.9864 0.9086 0.0018  -0.0092 -0.0567 37  ASP A OD2 
300  N N   . ASP A 36  ? 0.2565 0.4466 0.3898 -0.0062 -0.0109 -0.0554 38  ASP A N   
301  C CA  . ASP A 36  ? 0.2483 0.4384 0.3791 -0.0123 -0.0104 -0.0560 38  ASP A CA  
302  C C   . ASP A 36  ? 0.2486 0.4291 0.3741 -0.0170 -0.0137 -0.0534 38  ASP A C   
303  O O   . ASP A 36  ? 0.2843 0.4655 0.4081 -0.0227 -0.0142 -0.0530 38  ASP A O   
304  C CB  . ASP A 36  ? 0.2797 0.4646 0.4096 -0.0104 -0.0059 -0.0597 38  ASP A CB  
305  C CG  . ASP A 36  ? 0.3143 0.5100 0.4495 -0.0074 -0.0022 -0.0630 38  ASP A CG  
306  O OD1 . ASP A 36  ? 0.3056 0.5142 0.4454 -0.0071 -0.0030 -0.0624 38  ASP A OD1 
307  O OD2 . ASP A 36  ? 0.3672 0.5583 0.5018 -0.0052 0.0016  -0.0665 38  ASP A OD2 
308  N N   . TYR A 37  ? 0.2473 0.4191 0.3703 -0.0146 -0.0159 -0.0518 39  TYR A N   
309  C CA  . TYR A 37  ? 0.2232 0.3841 0.3410 -0.0179 -0.0184 -0.0504 39  TYR A CA  
310  C C   . TYR A 37  ? 0.2991 0.4612 0.4164 -0.0194 -0.0229 -0.0475 39  TYR A C   
311  O O   . TYR A 37  ? 0.3825 0.5467 0.5015 -0.0154 -0.0236 -0.0468 39  TYR A O   
312  C CB  . TYR A 37  ? 0.2381 0.3857 0.3521 -0.0138 -0.0165 -0.0518 39  TYR A CB  
313  C CG  . TYR A 37  ? 0.2108 0.3574 0.3253 -0.0122 -0.0120 -0.0548 39  TYR A CG  
314  C CD1 . TYR A 37  ? 0.2460 0.3934 0.3633 -0.0062 -0.0090 -0.0569 39  TYR A CD1 
315  C CD2 . TYR A 37  ? 0.2218 0.3673 0.3343 -0.0168 -0.0109 -0.0557 39  TYR A CD2 
316  C CE1 . TYR A 37  ? 0.2747 0.4211 0.3924 -0.0050 -0.0049 -0.0601 39  TYR A CE1 
317  C CE2 . TYR A 37  ? 0.2226 0.3680 0.3355 -0.0157 -0.0068 -0.0586 39  TYR A CE2 
318  C CZ  . TYR A 37  ? 0.2511 0.3968 0.3664 -0.0099 -0.0037 -0.0610 39  TYR A CZ  
319  O OH  . TYR A 37  ? 0.2906 0.4360 0.4062 -0.0092 0.0004  -0.0644 39  TYR A OH  
320  N N   . GLN A 38  ? 0.2620 0.4229 0.3772 -0.0254 -0.0259 -0.0459 40  GLN A N   
321  C CA  . GLN A 38  ? 0.2489 0.4098 0.3631 -0.0278 -0.0303 -0.0436 40  GLN A CA  
322  C C   . GLN A 38  ? 0.2826 0.4302 0.3917 -0.0290 -0.0319 -0.0436 40  GLN A C   
323  O O   . GLN A 38  ? 0.2897 0.4323 0.3968 -0.0324 -0.0318 -0.0439 40  GLN A O   
324  C CB  . GLN A 38  ? 0.3647 0.5355 0.4811 -0.0340 -0.0329 -0.0417 40  GLN A CB  
325  C CG  . GLN A 38  ? 0.5361 0.7215 0.6577 -0.0330 -0.0312 -0.0418 40  GLN A CG  
326  C CD  . GLN A 38  ? 0.7100 0.9064 0.8339 -0.0385 -0.0346 -0.0393 40  GLN A CD  
327  O OE1 . GLN A 38  ? 0.8112 1.0061 0.9335 -0.0447 -0.0372 -0.0378 40  GLN A OE1 
328  N NE2 . GLN A 38  ? 0.7015 0.9093 0.8293 -0.0363 -0.0348 -0.0388 40  GLN A NE2 
329  N N   . LEU A 39  ? 0.2387 0.3812 0.3459 -0.0261 -0.0335 -0.0432 41  LEU A N   
330  C CA  . LEU A 39  ? 0.2365 0.3672 0.3389 -0.0270 -0.0349 -0.0436 41  LEU A CA  
331  C C   . LEU A 39  ? 0.2730 0.4034 0.3744 -0.0330 -0.0389 -0.0424 41  LEU A C   
332  O O   . LEU A 39  ? 0.2862 0.4243 0.3898 -0.0355 -0.0416 -0.0408 41  LEU A O   
333  C CB  . LEU A 39  ? 0.2347 0.3610 0.3352 -0.0226 -0.0355 -0.0436 41  LEU A CB  
334  C CG  . LEU A 39  ? 0.2578 0.3835 0.3593 -0.0164 -0.0321 -0.0443 41  LEU A CG  
335  C CD1 . LEU A 39  ? 0.3069 0.4300 0.4069 -0.0129 -0.0335 -0.0433 41  LEU A CD1 
336  C CD2 . LEU A 39  ? 0.2472 0.3642 0.3461 -0.0152 -0.0288 -0.0463 41  LEU A CD2 
337  N N   . VAL A 40  ? 0.2862 0.4075 0.3845 -0.0354 -0.0394 -0.0431 42  VAL A N   
338  C CA  . VAL A 40  ? 0.2887 0.4080 0.3864 -0.0410 -0.0431 -0.0421 42  VAL A CA  
339  C C   . VAL A 40  ? 0.3626 0.4724 0.4565 -0.0408 -0.0456 -0.0430 42  VAL A C   
340  O O   . VAL A 40  ? 0.3418 0.4524 0.4356 -0.0437 -0.0492 -0.0422 42  VAL A O   
341  C CB  . VAL A 40  ? 0.3799 0.4972 0.4777 -0.0445 -0.0423 -0.0419 42  VAL A CB  
342  C CG1 . VAL A 40  ? 0.3987 0.5122 0.4958 -0.0500 -0.0463 -0.0407 42  VAL A CG1 
343  C CG2 . VAL A 40  ? 0.3459 0.4743 0.4475 -0.0457 -0.0403 -0.0410 42  VAL A CG2 
344  N N   . ARG A 41  ? 0.3323 0.4333 0.4230 -0.0376 -0.0436 -0.0447 43  ARG A N   
345  C CA  . ARG A 41  ? 0.3163 0.4092 0.4035 -0.0371 -0.0455 -0.0460 43  ARG A CA  
346  C C   . ARG A 41  ? 0.3291 0.4157 0.4133 -0.0322 -0.0425 -0.0476 43  ARG A C   
347  O O   . ARG A 41  ? 0.3111 0.3966 0.3954 -0.0305 -0.0392 -0.0480 43  ARG A O   
348  C CB  . ARG A 41  ? 0.4122 0.4986 0.4982 -0.0413 -0.0480 -0.0464 43  ARG A CB  
349  C CG  . ARG A 41  ? 0.5178 0.5979 0.6026 -0.0410 -0.0457 -0.0472 43  ARG A CG  
350  C CD  . ARG A 41  ? 0.6250 0.6991 0.7094 -0.0450 -0.0486 -0.0473 43  ARG A CD  
351  N NE  . ARG A 41  ? 0.6855 0.7652 0.7733 -0.0499 -0.0506 -0.0450 43  ARG A NE  
352  C CZ  . ARG A 41  ? 0.7638 0.8442 0.8531 -0.0524 -0.0498 -0.0437 43  ARG A CZ  
353  N NH1 . ARG A 41  ? 0.7665 0.8422 0.8543 -0.0504 -0.0469 -0.0447 43  ARG A NH1 
354  N NH2 . ARG A 41  ? 0.7787 0.8650 0.8709 -0.0573 -0.0519 -0.0412 43  ARG A NH2 
355  N N   . LYS A 42  ? 0.2933 0.3762 0.3748 -0.0304 -0.0437 -0.0484 44  LYS A N   
356  C CA  . LYS A 42  ? 0.2663 0.3432 0.3445 -0.0264 -0.0414 -0.0497 44  LYS A CA  
357  C C   . LYS A 42  ? 0.3212 0.3894 0.3966 -0.0275 -0.0410 -0.0514 44  LYS A C   
358  O O   . LYS A 42  ? 0.3508 0.4158 0.4254 -0.0304 -0.0438 -0.0523 44  LYS A O   
359  C CB  . LYS A 42  ? 0.3216 0.3988 0.3978 -0.0245 -0.0430 -0.0498 44  LYS A CB  
360  C CG  . LYS A 42  ? 0.3758 0.4484 0.4490 -0.0204 -0.0408 -0.0504 44  LYS A CG  
361  C CD  . LYS A 42  ? 0.5166 0.5934 0.5894 -0.0182 -0.0421 -0.0492 44  LYS A CD  
362  C CE  . LYS A 42  ? 0.5675 0.6388 0.6356 -0.0169 -0.0425 -0.0504 44  LYS A CE  
363  N NZ  . LYS A 42  ? 0.5515 0.6278 0.6193 -0.0158 -0.0444 -0.0490 44  LYS A NZ  
364  N N   . LEU A 43  ? 0.2476 0.3121 0.3216 -0.0252 -0.0377 -0.0521 45  LEU A N   
365  C CA  . LEU A 43  ? 0.2832 0.3401 0.3546 -0.0259 -0.0370 -0.0536 45  LEU A CA  
366  C C   . LEU A 43  ? 0.3712 0.4224 0.4384 -0.0231 -0.0362 -0.0551 45  LEU A C   
367  O O   . LEU A 43  ? 0.4332 0.4786 0.4981 -0.0240 -0.0369 -0.0567 45  LEU A O   
368  C CB  . LEU A 43  ? 0.2957 0.3525 0.3680 -0.0260 -0.0337 -0.0533 45  LEU A CB  
369  C CG  . LEU A 43  ? 0.3179 0.3806 0.3941 -0.0294 -0.0342 -0.0519 45  LEU A CG  
370  C CD1 . LEU A 43  ? 0.3347 0.3972 0.4112 -0.0295 -0.0309 -0.0520 45  LEU A CD1 
371  C CD2 . LEU A 43  ? 0.3351 0.3965 0.4122 -0.0336 -0.0379 -0.0515 45  LEU A CD2 
372  N N   . GLY A 44  ? 0.3544 0.4071 0.4207 -0.0198 -0.0349 -0.0545 46  GLY A N   
373  C CA  . GLY A 44  ? 0.3690 0.4170 0.4311 -0.0175 -0.0344 -0.0556 46  GLY A CA  
374  C C   . GLY A 44  ? 0.3586 0.4095 0.4205 -0.0142 -0.0337 -0.0541 46  GLY A C   
375  O O   . GLY A 44  ? 0.3144 0.3707 0.3797 -0.0132 -0.0332 -0.0525 46  GLY A O   
376  N N   . ARG A 45  ? 0.2961 0.3440 0.3543 -0.0126 -0.0338 -0.0546 47  ARG A N   
377  C CA  . ARG A 45  ? 0.3389 0.3886 0.3964 -0.0096 -0.0333 -0.0528 47  ARG A CA  
378  C C   . ARG A 45  ? 0.3649 0.4090 0.4180 -0.0080 -0.0317 -0.0534 47  ARG A C   
379  O O   . ARG A 45  ? 0.3925 0.4327 0.4425 -0.0095 -0.0321 -0.0555 47  ARG A O   
380  C CB  . ARG A 45  ? 0.3810 0.4358 0.4388 -0.0101 -0.0365 -0.0520 47  ARG A CB  
381  C CG  . ARG A 45  ? 0.5290 0.5848 0.5849 -0.0073 -0.0366 -0.0502 47  ARG A CG  
382  C CD  . ARG A 45  ? 0.6171 0.6776 0.6722 -0.0084 -0.0398 -0.0499 47  ARG A CD  
383  N NE  . ARG A 45  ? 0.6536 0.7215 0.7129 -0.0082 -0.0412 -0.0477 47  ARG A NE  
384  C CZ  . ARG A 45  ? 0.7012 0.7747 0.7604 -0.0087 -0.0439 -0.0465 47  ARG A CZ  
385  N NH1 . ARG A 45  ? 0.6170 0.6896 0.6722 -0.0095 -0.0453 -0.0474 47  ARG A NH1 
386  N NH2 . ARG A 45  ? 0.7093 0.7901 0.7726 -0.0085 -0.0450 -0.0444 47  ARG A NH2 
387  N N   . GLY A 46  ? 0.3647 0.4084 0.4177 -0.0050 -0.0300 -0.0516 48  GLY A N   
388  C CA  . GLY A 46  ? 0.4070 0.4460 0.4557 -0.0037 -0.0288 -0.0514 48  GLY A CA  
389  C C   . GLY A 46  ? 0.4246 0.4659 0.4734 -0.0010 -0.0293 -0.0486 48  GLY A C   
390  O O   . GLY A 46  ? 0.4620 0.5088 0.5143 0.0000  -0.0307 -0.0469 48  GLY A O   
391  N N   . LYS A 47  ? 0.4013 0.4386 0.4463 0.0002  -0.0283 -0.0478 49  LYS A N   
392  C CA  . LYS A 47  ? 0.4454 0.4843 0.4904 0.0026  -0.0290 -0.0446 49  LYS A CA  
393  C C   . LYS A 47  ? 0.4312 0.4711 0.4810 0.0057  -0.0276 -0.0426 49  LYS A C   
394  O O   . LYS A 47  ? 0.4655 0.5090 0.5174 0.0079  -0.0289 -0.0398 49  LYS A O   
395  C CB  . LYS A 47  ? 0.5974 0.6315 0.6374 0.0029  -0.0281 -0.0440 49  LYS A CB  
396  C CG  . LYS A 47  ? 0.7437 0.7794 0.7793 0.0006  -0.0302 -0.0451 49  LYS A CG  
397  C CD  . LYS A 47  ? 0.8229 0.8551 0.8537 0.0007  -0.0294 -0.0440 49  LYS A CD  
398  C CE  . LYS A 47  ? 0.8414 0.8733 0.8731 0.0033  -0.0295 -0.0397 49  LYS A CE  
399  N NZ  . LYS A 47  ? 0.8513 0.8832 0.8781 0.0026  -0.0305 -0.0378 49  LYS A NZ  
400  N N   . TYR A 48  ? 0.4012 0.4383 0.4528 0.0059  -0.0250 -0.0442 50  TYR A N   
401  C CA  . TYR A 48  ? 0.4108 0.4481 0.4665 0.0089  -0.0231 -0.0430 50  TYR A CA  
402  C C   . TYR A 48  ? 0.3638 0.4062 0.4246 0.0087  -0.0227 -0.0441 50  TYR A C   
403  O O   . TYR A 48  ? 0.3279 0.3713 0.3926 0.0113  -0.0209 -0.0437 50  TYR A O   
404  C CB  . TYR A 48  ? 0.5027 0.5325 0.5564 0.0098  -0.0199 -0.0438 50  TYR A CB  
405  C CG  . TYR A 48  ? 0.6328 0.6576 0.6817 0.0101  -0.0201 -0.0422 50  TYR A CG  
406  C CD1 . TYR A 48  ? 0.6945 0.7146 0.7383 0.0077  -0.0192 -0.0439 50  TYR A CD1 
407  C CD2 . TYR A 48  ? 0.6944 0.7196 0.7441 0.0128  -0.0214 -0.0388 50  TYR A CD2 
408  C CE1 . TYR A 48  ? 0.8016 0.8179 0.8409 0.0077  -0.0194 -0.0423 50  TYR A CE1 
409  C CE2 . TYR A 48  ? 0.7879 0.8089 0.8331 0.0127  -0.0218 -0.0369 50  TYR A CE2 
410  C CZ  . TYR A 48  ? 0.8456 0.8623 0.8855 0.0100  -0.0207 -0.0388 50  TYR A CZ  
411  O OH  . TYR A 48  ? 0.8895 0.9028 0.9248 0.0096  -0.0211 -0.0368 50  TYR A OH  
412  N N   . SER A 49  ? 0.3646 0.4104 0.4257 0.0055  -0.0242 -0.0457 51  SER A N   
413  C CA  . SER A 49  ? 0.3323 0.3834 0.3980 0.0047  -0.0238 -0.0465 51  SER A CA  
414  C C   . SER A 49  ? 0.3047 0.3592 0.3702 0.0009  -0.0265 -0.0474 51  SER A C   
415  O O   . SER A 49  ? 0.3346 0.3865 0.3964 -0.0010 -0.0281 -0.0482 51  SER A O   
416  C CB  . SER A 49  ? 0.2911 0.3390 0.3574 0.0043  -0.0205 -0.0484 51  SER A CB  
417  O OG  . SER A 49  ? 0.3484 0.3914 0.4106 0.0013  -0.0202 -0.0502 51  SER A OG  
418  N N   . GLU A 50  ? 0.2563 0.3170 0.3261 -0.0002 -0.0269 -0.0475 52  GLU A N   
419  C CA  . GLU A 50  ? 0.2584 0.3217 0.3287 -0.0042 -0.0290 -0.0485 52  GLU A CA  
420  C C   . GLU A 50  ? 0.2741 0.3386 0.3469 -0.0058 -0.0270 -0.0496 52  GLU A C   
421  O O   . GLU A 50  ? 0.2756 0.3425 0.3513 -0.0036 -0.0246 -0.0494 52  GLU A O   
422  C CB  . GLU A 50  ? 0.2712 0.3421 0.3440 -0.0050 -0.0321 -0.0470 52  GLU A CB  
423  C CG  . GLU A 50  ? 0.3560 0.4270 0.4264 -0.0038 -0.0342 -0.0458 52  GLU A CG  
424  C CD  . GLU A 50  ? 0.5010 0.5792 0.5732 -0.0057 -0.0376 -0.0448 52  GLU A CD  
425  O OE1 . GLU A 50  ? 0.4635 0.5488 0.5401 -0.0055 -0.0378 -0.0436 52  GLU A OE1 
426  O OE2 . GLU A 50  ? 0.5641 0.6412 0.6332 -0.0076 -0.0399 -0.0455 52  GLU A OE2 
427  N N   . VAL A 51  ? 0.2519 0.3148 0.3237 -0.0096 -0.0279 -0.0508 53  VAL A N   
428  C CA  . VAL A 51  ? 0.2237 0.2878 0.2976 -0.0117 -0.0262 -0.0515 53  VAL A CA  
429  C C   . VAL A 51  ? 0.2764 0.3456 0.3527 -0.0157 -0.0290 -0.0511 53  VAL A C   
430  O O   . VAL A 51  ? 0.2809 0.3484 0.3556 -0.0178 -0.0319 -0.0512 53  VAL A O   
431  C CB  . VAL A 51  ? 0.3146 0.3713 0.3851 -0.0126 -0.0243 -0.0530 53  VAL A CB  
432  C CG1 . VAL A 51  ? 0.3822 0.4345 0.4505 -0.0090 -0.0216 -0.0533 53  VAL A CG1 
433  C CG2 . VAL A 51  ? 0.3256 0.3844 0.3981 -0.0150 -0.0226 -0.0535 53  VAL A CG2 
434  N N   . PHE A 52  ? 0.2203 0.2958 0.3004 -0.0169 -0.0280 -0.0506 54  PHE A N   
435  C CA  . PHE A 52  ? 0.2038 0.2857 0.2867 -0.0207 -0.0306 -0.0496 54  PHE A CA  
436  C C   . PHE A 52  ? 0.2551 0.3389 0.3397 -0.0239 -0.0292 -0.0498 54  PHE A C   
437  O O   . PHE A 52  ? 0.2758 0.3600 0.3610 -0.0223 -0.0258 -0.0506 54  PHE A O   
438  C CB  . PHE A 52  ? 0.2059 0.2972 0.2928 -0.0193 -0.0312 -0.0482 54  PHE A CB  
439  C CG  . PHE A 52  ? 0.2108 0.3020 0.2967 -0.0165 -0.0328 -0.0475 54  PHE A CG  
440  C CD1 . PHE A 52  ? 0.2100 0.2983 0.2949 -0.0118 -0.0307 -0.0475 54  PHE A CD1 
441  C CD2 . PHE A 52  ? 0.2281 0.3224 0.3140 -0.0189 -0.0365 -0.0465 54  PHE A CD2 
442  C CE1 . PHE A 52  ? 0.2519 0.3407 0.3359 -0.0095 -0.0324 -0.0464 54  PHE A CE1 
443  C CE2 . PHE A 52  ? 0.2392 0.3342 0.3241 -0.0167 -0.0380 -0.0457 54  PHE A CE2 
444  C CZ  . PHE A 52  ? 0.2811 0.3735 0.3650 -0.0120 -0.0360 -0.0455 54  PHE A CZ  
445  N N   . GLU A 53  ? 0.2421 0.3273 0.3275 -0.0284 -0.0320 -0.0490 55  GLU A N   
446  C CA  . GLU A 53  ? 0.2620 0.3525 0.3501 -0.0321 -0.0315 -0.0482 55  GLU A CA  
447  C C   . GLU A 53  ? 0.2424 0.3440 0.3347 -0.0321 -0.0316 -0.0471 55  GLU A C   
448  O O   . GLU A 53  ? 0.2877 0.3927 0.3809 -0.0316 -0.0340 -0.0463 55  GLU A O   
449  C CB  . GLU A 53  ? 0.3520 0.4399 0.4397 -0.0371 -0.0349 -0.0473 55  GLU A CB  
450  C CG  . GLU A 53  ? 0.4447 0.5376 0.5349 -0.0414 -0.0347 -0.0460 55  GLU A CG  
451  C CD  . GLU A 53  ? 0.5848 0.6739 0.6748 -0.0462 -0.0384 -0.0447 55  GLU A CD  
452  O OE1 . GLU A 53  ? 0.6204 0.7149 0.7129 -0.0500 -0.0414 -0.0429 55  GLU A OE1 
453  O OE2 . GLU A 53  ? 0.5955 0.6761 0.6831 -0.0460 -0.0385 -0.0456 55  GLU A OE2 
454  N N   . ALA A 54  ? 0.2456 0.3534 0.3403 -0.0327 -0.0290 -0.0473 56  ALA A N   
455  C CA  . ALA A 54  ? 0.2392 0.3585 0.3382 -0.0325 -0.0287 -0.0467 56  ALA A CA  
456  C C   . ALA A 54  ? 0.2418 0.3681 0.3431 -0.0365 -0.0276 -0.0463 56  ALA A C   
457  O O   . ALA A 54  ? 0.2867 0.4088 0.3864 -0.0390 -0.0268 -0.0466 56  ALA A O   
458  C CB  . ALA A 54  ? 0.2447 0.3654 0.3448 -0.0264 -0.0256 -0.0481 56  ALA A CB  
459  N N   . ILE A 55  ? 0.3144 0.4525 0.4198 -0.0374 -0.0276 -0.0456 57  ILE A N   
460  C CA  . ILE A 55  ? 0.3061 0.4533 0.4140 -0.0411 -0.0264 -0.0454 57  ILE A CA  
461  C C   . ILE A 55  ? 0.2955 0.4507 0.4066 -0.0370 -0.0225 -0.0474 57  ILE A C   
462  O O   . ILE A 55  ? 0.2903 0.4499 0.4037 -0.0333 -0.0227 -0.0475 57  ILE A O   
463  C CB  . ILE A 55  ? 0.3983 0.5540 0.5085 -0.0468 -0.0303 -0.0425 57  ILE A CB  
464  C CG1 . ILE A 55  ? 0.4705 0.6174 0.5779 -0.0507 -0.0344 -0.0407 57  ILE A CG1 
465  C CG2 . ILE A 55  ? 0.4066 0.5726 0.5194 -0.0511 -0.0289 -0.0421 57  ILE A CG2 
466  C CD1 . ILE A 55  ? 0.5481 0.6925 0.6547 -0.0557 -0.0349 -0.0396 57  ILE A CD1 
467  N N   . ASN A 56  ? 0.2422 0.3993 0.3536 -0.0375 -0.0191 -0.0492 58  ASN A N   
468  C CA  . ASN A 56  ? 0.2700 0.4362 0.3850 -0.0344 -0.0154 -0.0516 58  ASN A CA  
469  C C   . ASN A 56  ? 0.3057 0.4866 0.4245 -0.0390 -0.0166 -0.0503 58  ASN A C   
470  O O   . ASN A 56  ? 0.3567 0.5414 0.4753 -0.0445 -0.0166 -0.0495 58  ASN A O   
471  C CB  . ASN A 56  ? 0.3099 0.4720 0.4233 -0.0334 -0.0112 -0.0545 58  ASN A CB  
472  C CG  . ASN A 56  ? 0.3049 0.4754 0.4220 -0.0300 -0.0071 -0.0577 58  ASN A CG  
473  O OD1 . ASN A 56  ? 0.3097 0.4915 0.4310 -0.0294 -0.0073 -0.0577 58  ASN A OD1 
474  N ND2 . ASN A 56  ? 0.3861 0.5513 0.5016 -0.0279 -0.0032 -0.0607 58  ASN A ND2 
475  N N   . ILE A 57  ? 0.2706 0.4602 0.3930 -0.0371 -0.0176 -0.0497 59  ILE A N   
476  C CA  . ILE A 57  ? 0.2784 0.4824 0.4042 -0.0420 -0.0193 -0.0479 59  ILE A CA  
477  C C   . ILE A 57  ? 0.3195 0.5352 0.4485 -0.0426 -0.0155 -0.0504 59  ILE A C   
478  O O   . ILE A 57  ? 0.3187 0.5469 0.4501 -0.0477 -0.0167 -0.0489 59  ILE A O   
479  C CB  . ILE A 57  ? 0.2680 0.4787 0.3965 -0.0403 -0.0218 -0.0463 59  ILE A CB  
480  C CG1 . ILE A 57  ? 0.2495 0.4635 0.3812 -0.0327 -0.0187 -0.0490 59  ILE A CG1 
481  C CG2 . ILE A 57  ? 0.3058 0.5061 0.4310 -0.0410 -0.0259 -0.0440 59  ILE A CG2 
482  C CD1 . ILE A 57  ? 0.3408 0.5658 0.4765 -0.0314 -0.0208 -0.0474 59  ILE A CD1 
483  N N   . THR A 58  ? 0.3071 0.5197 0.4362 -0.0378 -0.0111 -0.0541 60  THR A N   
484  C CA  . THR A 58  ? 0.3610 0.5844 0.4928 -0.0387 -0.0073 -0.0570 60  THR A CA  
485  C C   . THR A 58  ? 0.4147 0.6376 0.5439 -0.0451 -0.0070 -0.0564 60  THR A C   
486  O O   . THR A 58  ? 0.4563 0.6903 0.5876 -0.0478 -0.0045 -0.0581 60  THR A O   
487  C CB  . THR A 58  ? 0.2928 0.5131 0.4259 -0.0314 -0.0026 -0.0616 60  THR A CB  
488  O OG1 . THR A 58  ? 0.4291 0.6350 0.5577 -0.0302 -0.0012 -0.0627 60  THR A OG1 
489  C CG2 . THR A 58  ? 0.3951 0.6150 0.5309 -0.0247 -0.0032 -0.0617 60  THR A CG2 
490  N N   . ASN A 59  ? 0.4355 0.6464 0.5604 -0.0478 -0.0094 -0.0540 61  ASN A N   
491  C CA  . ASN A 59  ? 0.4184 0.6287 0.5410 -0.0541 -0.0098 -0.0526 61  ASN A CA  
492  C C   . ASN A 59  ? 0.4171 0.6196 0.5370 -0.0585 -0.0147 -0.0483 61  ASN A C   
493  O O   . ASN A 59  ? 0.5425 0.7423 0.6604 -0.0634 -0.0154 -0.0467 61  ASN A O   
494  C CB  . ASN A 59  ? 0.4568 0.6590 0.5767 -0.0518 -0.0057 -0.0558 61  ASN A CB  
495  C CG  . ASN A 59  ? 0.5451 0.7316 0.6617 -0.0462 -0.0056 -0.0567 61  ASN A CG  
496  O OD1 . ASN A 59  ? 0.5031 0.6827 0.6183 -0.0458 -0.0092 -0.0541 61  ASN A OD1 
497  N ND2 . ASN A 59  ? 0.6338 0.8148 0.7491 -0.0423 -0.0016 -0.0603 61  ASN A ND2 
498  N N   . ASN A 60  ? 0.4599 0.6587 0.5798 -0.0571 -0.0181 -0.0464 62  ASN A N   
499  C CA  . ASN A 60  ? 0.4707 0.6618 0.5883 -0.0609 -0.0229 -0.0428 62  ASN A CA  
500  C C   . ASN A 60  ? 0.5062 0.6834 0.6197 -0.0609 -0.0227 -0.0429 62  ASN A C   
501  O O   . ASN A 60  ? 0.5921 0.7648 0.7042 -0.0656 -0.0260 -0.0401 62  ASN A O   
502  C CB  . ASN A 60  ? 0.4920 0.6930 0.6115 -0.0687 -0.0262 -0.0392 62  ASN A CB  
503  C CG  . ASN A 60  ? 0.5790 0.7896 0.7015 -0.0694 -0.0287 -0.0376 62  ASN A CG  
504  O OD1 . ASN A 60  ? 0.4649 0.6772 0.5888 -0.0639 -0.0275 -0.0395 62  ASN A OD1 
505  N ND2 . ASN A 60  ? 0.6387 0.8559 0.7623 -0.0764 -0.0325 -0.0339 62  ASN A ND2 
506  N N   . GLU A 61  ? 0.4729 0.6432 0.5846 -0.0555 -0.0191 -0.0461 63  GLU A N   
507  C CA  . GLU A 61  ? 0.5191 0.6764 0.6268 -0.0549 -0.0186 -0.0465 63  GLU A CA  
508  C C   . GLU A 61  ? 0.4817 0.6278 0.5870 -0.0503 -0.0201 -0.0468 63  GLU A C   
509  O O   . GLU A 61  ? 0.4225 0.5697 0.5289 -0.0456 -0.0194 -0.0481 63  GLU A O   
510  C CB  . GLU A 61  ? 0.5962 0.7527 0.7029 -0.0525 -0.0136 -0.0498 63  GLU A CB  
511  C CG  . GLU A 61  ? 0.7329 0.9017 0.8419 -0.0566 -0.0115 -0.0503 63  GLU A CG  
512  C CD  . GLU A 61  ? 0.8430 1.0108 0.9503 -0.0626 -0.0126 -0.0480 63  GLU A CD  
513  O OE1 . GLU A 61  ? 0.8571 1.0316 0.9648 -0.0650 -0.0096 -0.0492 63  GLU A OE1 
514  O OE2 . GLU A 61  ? 0.8996 1.0601 1.0053 -0.0650 -0.0163 -0.0449 63  GLU A OE2 
515  N N   . LYS A 62  ? 0.4475 0.5833 0.5498 -0.0518 -0.0224 -0.0455 64  LYS A N   
516  C CA  . LYS A 62  ? 0.3694 0.4945 0.4689 -0.0476 -0.0234 -0.0463 64  LYS A CA  
517  C C   . LYS A 62  ? 0.3210 0.4408 0.4185 -0.0422 -0.0192 -0.0493 64  LYS A C   
518  O O   . LYS A 62  ? 0.3086 0.4277 0.4051 -0.0427 -0.0162 -0.0506 64  LYS A O   
519  C CB  . LYS A 62  ? 0.4688 0.5847 0.5657 -0.0503 -0.0265 -0.0447 64  LYS A CB  
520  C CG  . LYS A 62  ? 0.5603 0.6798 0.6591 -0.0561 -0.0309 -0.0416 64  LYS A CG  
521  C CD  . LYS A 62  ? 0.6154 0.7246 0.7120 -0.0580 -0.0340 -0.0405 64  LYS A CD  
522  C CE  . LYS A 62  ? 0.6453 0.7474 0.7402 -0.0552 -0.0364 -0.0412 64  LYS A CE  
523  N NZ  . LYS A 62  ? 0.6523 0.7454 0.7458 -0.0574 -0.0398 -0.0404 64  LYS A NZ  
524  N N   . VAL A 63  ? 0.2631 0.3790 0.3599 -0.0373 -0.0192 -0.0502 65  VAL A N   
525  C CA  . VAL A 63  ? 0.2728 0.3819 0.3674 -0.0322 -0.0160 -0.0525 65  VAL A CA  
526  C C   . VAL A 63  ? 0.2285 0.3286 0.3201 -0.0297 -0.0183 -0.0520 65  VAL A C   
527  O O   . VAL A 63  ? 0.2470 0.3471 0.3388 -0.0316 -0.0220 -0.0504 65  VAL A O   
528  C CB  . VAL A 63  ? 0.2321 0.3473 0.3296 -0.0280 -0.0130 -0.0543 65  VAL A CB  
529  C CG1 . VAL A 63  ? 0.2872 0.4112 0.3872 -0.0304 -0.0102 -0.0555 65  VAL A CG1 
530  C CG2 . VAL A 63  ? 0.2418 0.3633 0.3423 -0.0265 -0.0154 -0.0530 65  VAL A CG2 
531  N N   . VAL A 64  ? 0.2226 0.3155 0.3116 -0.0255 -0.0160 -0.0536 66  VAL A N   
532  C CA  . VAL A 64  ? 0.2103 0.2957 0.2964 -0.0229 -0.0177 -0.0533 66  VAL A CA  
533  C C   . VAL A 64  ? 0.2374 0.3229 0.3243 -0.0175 -0.0158 -0.0541 66  VAL A C   
534  O O   . VAL A 64  ? 0.2447 0.3299 0.3320 -0.0153 -0.0123 -0.0557 66  VAL A O   
535  C CB  . VAL A 64  ? 0.2078 0.2835 0.2894 -0.0234 -0.0172 -0.0540 66  VAL A CB  
536  C CG1 . VAL A 64  ? 0.2088 0.2775 0.2873 -0.0200 -0.0180 -0.0542 66  VAL A CG1 
537  C CG2 . VAL A 64  ? 0.2253 0.3003 0.3066 -0.0283 -0.0201 -0.0529 66  VAL A CG2 
538  N N   . VAL A 65  ? 0.2049 0.2915 0.2924 -0.0156 -0.0183 -0.0529 67  VAL A N   
539  C CA  . VAL A 65  ? 0.1934 0.2812 0.2823 -0.0106 -0.0171 -0.0529 67  VAL A CA  
540  C C   . VAL A 65  ? 0.2011 0.2808 0.2862 -0.0082 -0.0183 -0.0523 67  VAL A C   
541  O O   . VAL A 65  ? 0.2245 0.3034 0.3081 -0.0098 -0.0215 -0.0513 67  VAL A O   
542  C CB  . VAL A 65  ? 0.2148 0.3126 0.3082 -0.0103 -0.0190 -0.0515 67  VAL A CB  
543  C CG1 . VAL A 65  ? 0.2491 0.3480 0.3446 -0.0046 -0.0179 -0.0512 67  VAL A CG1 
544  C CG2 . VAL A 65  ? 0.2397 0.3465 0.3368 -0.0132 -0.0181 -0.0519 67  VAL A CG2 
545  N N   . LYS A 66  ? 0.2265 0.3007 0.3101 -0.0045 -0.0157 -0.0531 68  LYS A N   
546  C CA  . LYS A 66  ? 0.1862 0.2536 0.2663 -0.0021 -0.0165 -0.0524 68  LYS A CA  
547  C C   . LYS A 66  ? 0.2086 0.2791 0.2915 0.0024  -0.0166 -0.0510 68  LYS A C   
548  O O   . LYS A 66  ? 0.2029 0.2733 0.2880 0.0056  -0.0139 -0.0517 68  LYS A O   
549  C CB  . LYS A 66  ? 0.2131 0.2718 0.2891 -0.0016 -0.0139 -0.0537 68  LYS A CB  
550  C CG  . LYS A 66  ? 0.2282 0.2803 0.3004 0.0007  -0.0146 -0.0528 68  LYS A CG  
551  C CD  . LYS A 66  ? 0.3056 0.3497 0.3731 -0.0003 -0.0128 -0.0540 68  LYS A CD  
552  C CE  . LYS A 66  ? 0.3251 0.3659 0.3928 0.0018  -0.0091 -0.0551 68  LYS A CE  
553  N NZ  . LYS A 66  ? 0.3182 0.3510 0.3806 0.0008  -0.0078 -0.0559 68  LYS A NZ  
554  N N   . ILE A 67  ? 0.2035 0.2769 0.2867 0.0028  -0.0198 -0.0491 69  ILE A N   
555  C CA  . ILE A 67  ? 0.2102 0.2873 0.2963 0.0069  -0.0204 -0.0473 69  ILE A CA  
556  C C   . ILE A 67  ? 0.2506 0.3205 0.3329 0.0092  -0.0208 -0.0461 69  ILE A C   
557  O O   . ILE A 67  ? 0.2944 0.3620 0.3730 0.0073  -0.0232 -0.0454 69  ILE A O   
558  C CB  . ILE A 67  ? 0.2203 0.3062 0.3091 0.0056  -0.0236 -0.0456 69  ILE A CB  
559  C CG1 . ILE A 67  ? 0.2109 0.3042 0.3030 0.0024  -0.0235 -0.0465 69  ILE A CG1 
560  C CG2 . ILE A 67  ? 0.2720 0.3626 0.3645 0.0102  -0.0241 -0.0434 69  ILE A CG2 
561  C CD1 . ILE A 67  ? 0.2313 0.3335 0.3260 0.0007  -0.0268 -0.0448 69  ILE A CD1 
562  N N   . LEU A 68  ? 0.2715 0.3378 0.3547 0.0132  -0.0186 -0.0458 70  LEU A N   
563  C CA  . LEU A 68  ? 0.3049 0.3638 0.3842 0.0150  -0.0188 -0.0445 70  LEU A CA  
564  C C   . LEU A 68  ? 0.3225 0.3849 0.4021 0.0165  -0.0220 -0.0414 70  LEU A C   
565  O O   . LEU A 68  ? 0.3744 0.4442 0.4587 0.0184  -0.0231 -0.0399 70  LEU A O   
566  C CB  . LEU A 68  ? 0.3233 0.3770 0.4037 0.0188  -0.0157 -0.0448 70  LEU A CB  
567  C CG  . LEU A 68  ? 0.4038 0.4546 0.4840 0.0175  -0.0122 -0.0481 70  LEU A CG  
568  C CD1 . LEU A 68  ? 0.3816 0.4257 0.4620 0.0210  -0.0095 -0.0485 70  LEU A CD1 
569  C CD2 . LEU A 68  ? 0.4799 0.5265 0.5549 0.0130  -0.0122 -0.0495 70  LEU A CD2 
570  N N   . LYS A 69  ? 0.3543 0.4121 0.4290 0.0154  -0.0234 -0.0404 71  LYS A N   
571  C CA  . LYS A 69  ? 0.3627 0.4227 0.4373 0.0173  -0.0259 -0.0371 71  LYS A CA  
572  C C   . LYS A 69  ? 0.4755 0.5307 0.5512 0.0217  -0.0244 -0.0353 71  LYS A C   
573  O O   . LYS A 69  ? 0.4275 0.4768 0.5029 0.0226  -0.0214 -0.0370 71  LYS A O   
574  C CB  . LYS A 69  ? 0.3595 0.4172 0.4284 0.0143  -0.0281 -0.0370 71  LYS A CB  
575  C CG  . LYS A 69  ? 0.4300 0.4922 0.4984 0.0102  -0.0300 -0.0388 71  LYS A CG  
576  C CD  . LYS A 69  ? 0.5192 0.5787 0.5820 0.0073  -0.0318 -0.0396 71  LYS A CD  
577  C CE  . LYS A 69  ? 0.5281 0.5908 0.5908 0.0034  -0.0336 -0.0418 71  LYS A CE  
578  N NZ  . LYS A 69  ? 0.5869 0.6477 0.6446 0.0009  -0.0355 -0.0429 71  LYS A NZ  
579  N N   . PRO A 70  ? 0.6442 0.7019 0.7214 0.0244  -0.0264 -0.0317 72  PRO A N   
580  C CA  . PRO A 70  ? 0.7153 0.7679 0.7940 0.0287  -0.0252 -0.0296 72  PRO A CA  
581  C C   . PRO A 70  ? 0.7365 0.7790 0.8096 0.0276  -0.0237 -0.0302 72  PRO A C   
582  O O   . PRO A 70  ? 0.7778 0.8186 0.8456 0.0247  -0.0251 -0.0297 72  PRO A O   
583  C CB  . PRO A 70  ? 0.7279 0.7857 0.8083 0.0306  -0.0284 -0.0251 72  PRO A CB  
584  C CG  . PRO A 70  ? 0.6980 0.7658 0.7809 0.0289  -0.0304 -0.0255 72  PRO A CG  
585  C CD  . PRO A 70  ? 0.6637 0.7302 0.7428 0.0240  -0.0297 -0.0293 72  PRO A CD  
586  N N   . VAL A 71  ? 0.7107 0.7470 0.7850 0.0298  -0.0207 -0.0315 73  VAL A N   
587  C CA  . VAL A 71  ? 0.7054 0.7320 0.7749 0.0290  -0.0190 -0.0319 73  VAL A CA  
588  C C   . VAL A 71  ? 0.6735 0.6950 0.7467 0.0332  -0.0167 -0.0318 73  VAL A C   
589  O O   . VAL A 71  ? 0.6181 0.6436 0.6973 0.0360  -0.0156 -0.0329 73  VAL A O   
590  C CB  . VAL A 71  ? 0.6829 0.7067 0.7481 0.0248  -0.0171 -0.0358 73  VAL A CB  
591  C CG1 . VAL A 71  ? 0.5998 0.6253 0.6689 0.0251  -0.0143 -0.0392 73  VAL A CG1 
592  C CG2 . VAL A 71  ? 0.7645 0.7794 0.8240 0.0234  -0.0158 -0.0358 73  VAL A CG2 
593  N N   . LYS A 72  ? 0.6855 0.6981 0.7552 0.0335  -0.0159 -0.0306 74  LYS A N   
594  C CA  . LYS A 72  ? 0.6997 0.7059 0.7726 0.0375  -0.0140 -0.0304 74  LYS A CA  
595  C C   . LYS A 72  ? 0.5897 0.5966 0.6664 0.0383  -0.0106 -0.0350 74  LYS A C   
596  O O   . LYS A 72  ? 0.4976 0.5040 0.5712 0.0348  -0.0087 -0.0385 74  LYS A O   
597  C CB  . LYS A 72  ? 0.7785 0.7745 0.8459 0.0361  -0.0133 -0.0293 74  LYS A CB  
598  C CG  . LYS A 72  ? 0.8458 0.8408 0.9108 0.0364  -0.0167 -0.0240 74  LYS A CG  
599  C CD  . LYS A 72  ? 0.8527 0.8467 0.9100 0.0314  -0.0176 -0.0238 74  LYS A CD  
600  C CE  . LYS A 72  ? 0.8465 0.8309 0.8990 0.0295  -0.0151 -0.0252 74  LYS A CE  
601  N NZ  . LYS A 72  ? 0.8533 0.8350 0.8996 0.0269  -0.0170 -0.0219 74  LYS A NZ  
602  N N   . LYS A 73  ? 0.4922 0.5297 0.5859 0.0556  -0.0642 -0.0360 75  LYS A N   
603  C CA  . LYS A 73  ? 0.5255 0.5712 0.6302 0.0532  -0.0594 -0.0373 75  LYS A CA  
604  C C   . LYS A 73  ? 0.4534 0.4989 0.5557 0.0546  -0.0521 -0.0378 75  LYS A C   
605  O O   . LYS A 73  ? 0.4673 0.5170 0.5737 0.0519  -0.0475 -0.0391 75  LYS A O   
606  C CB  . LYS A 73  ? 0.6107 0.6657 0.7308 0.0534  -0.0605 -0.0371 75  LYS A CB  
607  C CG  . LYS A 73  ? 0.7353 0.7931 0.8603 0.0509  -0.0672 -0.0367 75  LYS A CG  
608  C CD  . LYS A 73  ? 0.7895 0.8500 0.9166 0.0456  -0.0669 -0.0382 75  LYS A CD  
609  C CE  . LYS A 73  ? 0.7738 0.8459 0.9170 0.0435  -0.0642 -0.0393 75  LYS A CE  
610  N NZ  . LYS A 73  ? 0.7243 0.7988 0.8684 0.0382  -0.0624 -0.0408 75  LYS A NZ  
611  N N   . LYS A 74  ? 0.3750 0.4160 0.4707 0.0586  -0.0509 -0.0369 76  LYS A N   
612  C CA  . LYS A 74  ? 0.3595 0.3998 0.4512 0.0599  -0.0443 -0.0373 76  LYS A CA  
613  C C   . LYS A 74  ? 0.3620 0.3983 0.4445 0.0577  -0.0420 -0.0380 76  LYS A C   
614  O O   . LYS A 74  ? 0.3691 0.4090 0.4536 0.0562  -0.0362 -0.0387 76  LYS A O   
615  C CB  . LYS A 74  ? 0.5155 0.5502 0.5991 0.0641  -0.0446 -0.0360 76  LYS A CB  
616  C CG  . LYS A 74  ? 0.6394 0.6755 0.7226 0.0658  -0.0379 -0.0362 76  LYS A CG  
617  C CD  . LYS A 74  ? 0.7212 0.7515 0.7955 0.0697  -0.0390 -0.0348 76  LYS A CD  
618  C CE  . LYS A 74  ? 0.7617 0.7836 0.8213 0.0702  -0.0422 -0.0344 76  LYS A CE  
619  N NZ  . LYS A 74  ? 0.8065 0.8269 0.8592 0.0687  -0.0379 -0.0353 76  LYS A NZ  
620  N N   . LYS A 75  ? 0.3499 0.3789 0.4224 0.0574  -0.0465 -0.0376 77  LYS A N   
621  C CA  . LYS A 75  ? 0.3595 0.3837 0.4227 0.0559  -0.0446 -0.0381 77  LYS A CA  
622  C C   . LYS A 75  ? 0.2923 0.3208 0.3622 0.0512  -0.0441 -0.0390 77  LYS A C   
623  O O   . LYS A 75  ? 0.3153 0.3432 0.3819 0.0496  -0.0402 -0.0393 77  LYS A O   
624  C CB  . LYS A 75  ? 0.4866 0.5010 0.5367 0.0572  -0.0493 -0.0377 77  LYS A CB  
625  C CG  . LYS A 75  ? 0.6430 0.6529 0.6884 0.0540  -0.0518 -0.0384 77  LYS A CG  
626  C CD  . LYS A 75  ? 0.6800 0.6863 0.7175 0.0539  -0.0473 -0.0386 77  LYS A CD  
627  C CE  . LYS A 75  ? 0.5352 0.5396 0.5724 0.0499  -0.0486 -0.0392 77  LYS A CE  
628  N NZ  . LYS A 75  ? 0.3934 0.4066 0.4440 0.0458  -0.0482 -0.0396 77  LYS A NZ  
629  N N   . ILE A 76  ? 0.3003 0.3333 0.3795 0.0489  -0.0479 -0.0393 78  ILE A N   
630  C CA  . ILE A 76  ? 0.3047 0.3430 0.3914 0.0442  -0.0473 -0.0402 78  ILE A CA  
631  C C   . ILE A 76  ? 0.2805 0.3273 0.3762 0.0430  -0.0406 -0.0408 78  ILE A C   
632  O O   . ILE A 76  ? 0.2634 0.3121 0.3594 0.0398  -0.0373 -0.0413 78  ILE A O   
633  C CB  . ILE A 76  ? 0.3195 0.3619 0.4147 0.0420  -0.0529 -0.0403 78  ILE A CB  
634  C CG1 . ILE A 76  ? 0.3347 0.3688 0.4204 0.0426  -0.0595 -0.0397 78  ILE A CG1 
635  C CG2 . ILE A 76  ? 0.3636 0.4118 0.4663 0.0367  -0.0521 -0.0413 78  ILE A CG2 
636  C CD1 . ILE A 76  ? 0.3882 0.4267 0.4819 0.0410  -0.0654 -0.0395 78  ILE A CD1 
637  N N   . LYS A 77  ? 0.2845 0.3365 0.3878 0.0455  -0.0386 -0.0409 79  LYS A N   
638  C CA  . LYS A 77  ? 0.2854 0.3451 0.3968 0.0445  -0.0319 -0.0418 79  LYS A CA  
639  C C   . LYS A 77  ? 0.2684 0.3248 0.3707 0.0452  -0.0265 -0.0415 79  LYS A C   
640  O O   . LYS A 77  ? 0.2671 0.3289 0.3733 0.0425  -0.0213 -0.0422 79  LYS A O   
641  C CB  . LYS A 77  ? 0.2928 0.3572 0.4131 0.0475  -0.0309 -0.0419 79  LYS A CB  
642  C CG  . LYS A 77  ? 0.3066 0.3774 0.4394 0.0464  -0.0349 -0.0423 79  LYS A CG  
643  C CD  . LYS A 77  ? 0.3635 0.4404 0.5071 0.0489  -0.0321 -0.0428 79  LYS A CD  
644  C CE  . LYS A 77  ? 0.4924 0.5760 0.6488 0.0484  -0.0361 -0.0430 79  LYS A CE  
645  N NZ  . LYS A 77  ? 0.5819 0.6709 0.7489 0.0514  -0.0332 -0.0434 79  LYS A NZ  
646  N N   . ARG A 78  ? 0.2404 0.2885 0.3306 0.0487  -0.0277 -0.0405 80  ARG A N   
647  C CA  . ARG A 78  ? 0.2468 0.2921 0.3280 0.0495  -0.0228 -0.0401 80  ARG A CA  
648  C C   . ARG A 78  ? 0.2372 0.2816 0.3150 0.0460  -0.0219 -0.0400 80  ARG A C   
649  O O   . ARG A 78  ? 0.2393 0.2878 0.3181 0.0441  -0.0164 -0.0401 80  ARG A O   
650  C CB  . ARG A 78  ? 0.2407 0.2772 0.3093 0.0538  -0.0250 -0.0390 80  ARG A CB  
651  C CG  . ARG A 78  ? 0.2888 0.3230 0.3481 0.0552  -0.0200 -0.0385 80  ARG A CG  
652  C CD  . ARG A 78  ? 0.2839 0.3098 0.3309 0.0593  -0.0224 -0.0377 80  ARG A CD  
653  N NE  . ARG A 78  ? 0.3369 0.3554 0.3762 0.0593  -0.0276 -0.0376 80  ARG A NE  
654  C CZ  . ARG A 78  ? 0.3906 0.4014 0.4195 0.0622  -0.0310 -0.0372 80  ARG A CZ  
655  N NH1 . ARG A 78  ? 0.3411 0.3510 0.3664 0.0655  -0.0300 -0.0367 80  ARG A NH1 
656  N NH2 . ARG A 78  ? 0.3599 0.3639 0.3819 0.0618  -0.0353 -0.0374 80  ARG A NH2 
657  N N   . GLU A 79  ? 0.2384 0.2773 0.3120 0.0448  -0.0272 -0.0399 81  GLU A N   
658  C CA  . GLU A 79  ? 0.2383 0.2752 0.3083 0.0415  -0.0267 -0.0397 81  GLU A CA  
659  C C   . GLU A 79  ? 0.2536 0.2998 0.3350 0.0367  -0.0239 -0.0404 81  GLU A C   
660  O O   . GLU A 79  ? 0.2406 0.2886 0.3208 0.0342  -0.0201 -0.0400 81  GLU A O   
661  C CB  . GLU A 79  ? 0.2444 0.2733 0.3079 0.0410  -0.0331 -0.0396 81  GLU A CB  
662  C CG  . GLU A 79  ? 0.2395 0.2651 0.2986 0.0377  -0.0328 -0.0393 81  GLU A CG  
663  C CD  . GLU A 79  ? 0.2871 0.3036 0.3388 0.0371  -0.0387 -0.0394 81  GLU A CD  
664  O OE1 . GLU A 79  ? 0.3260 0.3390 0.3755 0.0391  -0.0432 -0.0397 81  GLU A OE1 
665  O OE2 . GLU A 79  ? 0.3126 0.3254 0.3605 0.0344  -0.0389 -0.0391 81  GLU A OE2 
666  N N   . ILE A 80  ? 0.2370 0.2896 0.3297 0.0351  -0.0259 -0.0414 82  ILE A N   
667  C CA  . ILE A 80  ? 0.2274 0.2895 0.3316 0.0304  -0.0232 -0.0424 82  ILE A CA  
668  C C   . ILE A 80  ? 0.1953 0.2639 0.3031 0.0301  -0.0158 -0.0427 82  ILE A C   
669  O O   . ILE A 80  ? 0.2310 0.3040 0.3409 0.0262  -0.0122 -0.0428 82  ILE A O   
670  C CB  . ILE A 80  ? 0.2000 0.2684 0.3161 0.0295  -0.0264 -0.0434 82  ILE A CB  
671  C CG1 . ILE A 80  ? 0.2148 0.2787 0.3285 0.0277  -0.0333 -0.0432 82  ILE A CG1 
672  C CG2 . ILE A 80  ? 0.2775 0.3573 0.4065 0.0254  -0.0221 -0.0448 82  ILE A CG2 
673  C CD1 . ILE A 80  ? 0.2640 0.3334 0.3882 0.0276  -0.0375 -0.0438 82  ILE A CD1 
674  N N   . LYS A 81  ? 0.2055 0.2746 0.3136 0.0340  -0.0136 -0.0428 83  LYS A N   
675  C CA  . LYS A 81  ? 0.2142 0.2894 0.3256 0.0335  -0.0065 -0.0434 83  LYS A CA  
676  C C   . LYS A 81  ? 0.2096 0.2820 0.3113 0.0328  -0.0029 -0.0421 83  LYS A C   
677  O O   . LYS A 81  ? 0.2288 0.3076 0.3341 0.0294  0.0023  -0.0424 83  LYS A O   
678  C CB  . LYS A 81  ? 0.2677 0.3423 0.3795 0.0381  -0.0051 -0.0435 83  LYS A CB  
679  C CG  . LYS A 81  ? 0.2456 0.3270 0.3619 0.0372  0.0023  -0.0445 83  LYS A CG  
680  C CD  . LYS A 81  ? 0.3305 0.4220 0.4610 0.0332  0.0047  -0.0464 83  LYS A CD  
681  C CE  . LYS A 81  ? 0.3544 0.4528 0.4889 0.0313  0.0125  -0.0475 83  LYS A CE  
682  N NZ  . LYS A 81  ? 0.3829 0.4912 0.5317 0.0277  0.0147  -0.0498 83  LYS A NZ  
683  N N   . ILE A 82  ? 0.2062 0.2693 0.2956 0.0358  -0.0057 -0.0407 84  ILE A N   
684  C CA  . ILE A 82  ? 0.2199 0.2800 0.2998 0.0357  -0.0026 -0.0394 84  ILE A CA  
685  C C   . ILE A 82  ? 0.2045 0.2667 0.2863 0.0308  -0.0024 -0.0389 84  ILE A C   
686  O O   . ILE A 82  ? 0.2315 0.2978 0.3128 0.0284  0.0024  -0.0382 84  ILE A O   
687  C CB  . ILE A 82  ? 0.2241 0.2736 0.2911 0.0402  -0.0060 -0.0382 84  ILE A CB  
688  C CG1 . ILE A 82  ? 0.2679 0.3167 0.3322 0.0445  -0.0044 -0.0383 84  ILE A CG1 
689  C CG2 . ILE A 82  ? 0.2278 0.2731 0.2852 0.0399  -0.0044 -0.0367 84  ILE A CG2 
690  C CD1 . ILE A 82  ? 0.2387 0.2779 0.2910 0.0491  -0.0079 -0.0375 84  ILE A CD1 
691  N N   . LEU A 83  ? 0.2053 0.2647 0.2888 0.0289  -0.0077 -0.0392 85  LEU A N   
692  C CA  . LEU A 83  ? 0.1889 0.2498 0.2741 0.0239  -0.0080 -0.0387 85  LEU A CA  
693  C C   . LEU A 83  ? 0.2062 0.2787 0.3027 0.0191  -0.0033 -0.0397 85  LEU A C   
694  O O   . LEU A 83  ? 0.2044 0.2797 0.3006 0.0154  -0.0005 -0.0387 85  LEU A O   
695  C CB  . LEU A 83  ? 0.2081 0.2646 0.2940 0.0225  -0.0145 -0.0392 85  LEU A CB  
696  C CG  . LEU A 83  ? 0.2187 0.2630 0.2924 0.0257  -0.0192 -0.0383 85  LEU A CG  
697  C CD1 . LEU A 83  ? 0.2605 0.3019 0.3364 0.0244  -0.0256 -0.0392 85  LEU A CD1 
698  C CD2 . LEU A 83  ? 0.2528 0.2921 0.3182 0.0244  -0.0179 -0.0367 85  LEU A CD2 
699  N N   . GLU A 84  ? 0.2330 0.3124 0.3398 0.0191  -0.0025 -0.0415 86  GLU A N   
700  C CA  . GLU A 84  ? 0.2358 0.3265 0.3535 0.0146  0.0024  -0.0428 86  GLU A CA  
701  C C   . GLU A 84  ? 0.2386 0.3330 0.3540 0.0148  0.0093  -0.0423 86  GLU A C   
702  O O   . GLU A 84  ? 0.2365 0.3378 0.3556 0.0101  0.0135  -0.0424 86  GLU A O   
703  C CB  . GLU A 84  ? 0.1995 0.2963 0.3290 0.0150  0.0016  -0.0449 86  GLU A CB  
704  C CG  . GLU A 84  ? 0.2686 0.3646 0.4023 0.0134  -0.0047 -0.0454 86  GLU A CG  
705  C CD  . GLU A 84  ? 0.3838 0.4866 0.5299 0.0140  -0.0056 -0.0473 86  GLU A CD  
706  O OE1 . GLU A 84  ? 0.4462 0.5524 0.5965 0.0166  -0.0020 -0.0482 86  GLU A OE1 
707  O OE2 . GLU A 84  ? 0.4263 0.5310 0.5778 0.0117  -0.0101 -0.0478 86  GLU A OE2 
708  N N   . ASN A 85  ? 0.2289 0.3188 0.3377 0.0198  0.0104  -0.0419 87  ASN A N   
709  C CA  . ASN A 85  ? 0.2080 0.3012 0.3136 0.0198  0.0168  -0.0413 87  ASN A CA  
710  C C   . ASN A 85  ? 0.2286 0.3202 0.3265 0.0176  0.0182  -0.0391 87  ASN A C   
711  O O   . ASN A 85  ? 0.2334 0.3316 0.3326 0.0146  0.0237  -0.0387 87  ASN A O   
712  C CB  . ASN A 85  ? 0.2228 0.3107 0.3216 0.0256  0.0171  -0.0410 87  ASN A CB  
713  C CG  . ASN A 85  ? 0.2236 0.3148 0.3307 0.0274  0.0178  -0.0430 87  ASN A CG  
714  O OD1 . ASN A 85  ? 0.2429 0.3415 0.3615 0.0243  0.0191  -0.0448 87  ASN A OD1 
715  N ND2 . ASN A 85  ? 0.2422 0.3280 0.3436 0.0323  0.0170  -0.0427 87  ASN A ND2 
716  N N   . LEU A 86  ? 0.2114 0.2943 0.3013 0.0192  0.0134  -0.0375 88  LEU A N   
717  C CA  . LEU A 86  ? 0.2050 0.2847 0.2865 0.0183  0.0143  -0.0351 88  LEU A CA  
718  C C   . LEU A 86  ? 0.2369 0.3193 0.3223 0.0126  0.0134  -0.0345 88  LEU A C   
719  O O   . LEU A 86  ? 0.2407 0.3215 0.3204 0.0112  0.0145  -0.0322 88  LEU A O   
720  C CB  . LEU A 86  ? 0.2039 0.2717 0.2736 0.0233  0.0099  -0.0338 88  LEU A CB  
721  C CG  . LEU A 86  ? 0.2193 0.2835 0.2827 0.0290  0.0107  -0.0340 88  LEU A CG  
722  C CD1 . LEU A 86  ? 0.2381 0.2908 0.2902 0.0334  0.0062  -0.0330 88  LEU A CD1 
723  C CD2 . LEU A 86  ? 0.2330 0.3028 0.2943 0.0288  0.0172  -0.0330 88  LEU A CD2 
724  N N   . ARG A 87  ? 0.2040 0.2904 0.2989 0.0093  0.0112  -0.0363 89  ARG A N   
725  C CA  . ARG A 87  ? 0.1979 0.2863 0.2963 0.0037  0.0095  -0.0358 89  ARG A CA  
726  C C   . ARG A 87  ? 0.2526 0.3484 0.3524 -0.0010 0.0149  -0.0345 89  ARG A C   
727  O O   . ARG A 87  ? 0.2442 0.3487 0.3494 -0.0024 0.0202  -0.0355 89  ARG A O   
728  C CB  . ARG A 87  ? 0.2159 0.3101 0.3257 0.0007  0.0074  -0.0382 89  ARG A CB  
729  C CG  . ARG A 87  ? 0.2327 0.3279 0.3454 -0.0050 0.0046  -0.0378 89  ARG A CG  
730  C CD  . ARG A 87  ? 0.2820 0.3792 0.4030 -0.0062 0.0003  -0.0400 89  ARG A CD  
731  N NE  . ARG A 87  ? 0.3031 0.4092 0.4345 -0.0056 0.0032  -0.0424 89  ARG A NE  
732  C CZ  . ARG A 87  ? 0.3398 0.4472 0.4777 -0.0039 -0.0001 -0.0442 89  ARG A CZ  
733  N NH1 . ARG A 87  ? 0.3259 0.4264 0.4605 -0.0031 -0.0065 -0.0438 89  ARG A NH1 
734  N NH2 . ARG A 87  ? 0.3481 0.4634 0.4956 -0.0031 0.0030  -0.0463 89  ARG A NH2 
735  N N   . GLY A 88  ? 0.2276 0.3199 0.3225 -0.0036 0.0134  -0.0321 90  GLY A N   
736  C CA  . GLY A 88  ? 0.2496 0.3481 0.3447 -0.0081 0.0178  -0.0302 90  GLY A CA  
737  C C   . GLY A 88  ? 0.2958 0.3912 0.3813 -0.0047 0.0207  -0.0276 90  GLY A C   
738  O O   . GLY A 88  ? 0.2673 0.3663 0.3513 -0.0081 0.0234  -0.0252 90  GLY A O   
739  N N   . GLY A 89  ? 0.2050 0.2941 0.2840 0.0017  0.0200  -0.0278 91  GLY A N   
740  C CA  . GLY A 89  ? 0.2073 0.2936 0.2770 0.0053  0.0225  -0.0254 91  GLY A CA  
741  C C   . GLY A 89  ? 0.2337 0.3113 0.2949 0.0063  0.0194  -0.0225 91  GLY A C   
742  O O   . GLY A 89  ? 0.2185 0.2896 0.2793 0.0055  0.0145  -0.0227 91  GLY A O   
743  N N   . PRO A 90  ? 0.2204 0.2977 0.2747 0.0081  0.0223  -0.0198 92  PRO A N   
744  C CA  . PRO A 90  ? 0.1818 0.2513 0.2285 0.0090  0.0199  -0.0167 92  PRO A CA  
745  C C   . PRO A 90  ? 0.1947 0.2512 0.2342 0.0143  0.0145  -0.0174 92  PRO A C   
746  O O   . PRO A 90  ? 0.2318 0.2839 0.2659 0.0199  0.0142  -0.0183 92  PRO A O   
747  C CB  . PRO A 90  ? 0.2654 0.3381 0.3063 0.0113  0.0245  -0.0140 92  PRO A CB  
748  C CG  . PRO A 90  ? 0.3523 0.4359 0.3989 0.0095  0.0296  -0.0156 92  PRO A CG  
749  C CD  . PRO A 90  ? 0.2791 0.3628 0.3320 0.0097  0.0277  -0.0194 92  PRO A CD  
750  N N   . ASN A 91  ? 0.2119 0.2619 0.2509 0.0121  0.0102  -0.0170 93  ASN A N   
751  C CA  . ASN A 91  ? 0.2083 0.2450 0.2396 0.0162  0.0050  -0.0173 93  ASN A CA  
752  C C   . ASN A 91  ? 0.2609 0.2945 0.2930 0.0192  0.0020  -0.0206 93  ASN A C   
753  O O   . ASN A 91  ? 0.2665 0.2899 0.2910 0.0238  -0.0013 -0.0212 93  ASN A O   
754  C CB  . ASN A 91  ? 0.2592 0.2892 0.2801 0.0215  0.0059  -0.0149 93  ASN A CB  
755  C CG  . ASN A 91  ? 0.2694 0.3013 0.2892 0.0187  0.0079  -0.0112 93  ASN A CG  
756  O OD1 . ASN A 91  ? 0.2840 0.3172 0.3083 0.0131  0.0066  -0.0104 93  ASN A OD1 
757  N ND2 . ASN A 91  ? 0.2359 0.2683 0.2499 0.0223  0.0110  -0.0087 93  ASN A ND2 
758  N N   . ILE A 92  ? 0.2168 0.2590 0.2581 0.0167  0.0033  -0.0228 94  ILE A N   
759  C CA  . ILE A 92  ? 0.1829 0.2232 0.2267 0.0188  0.0001  -0.0257 94  ILE A CA  
760  C C   . ILE A 92  ? 0.1890 0.2277 0.2379 0.0145  -0.0044 -0.0269 94  ILE A C   
761  O O   . ILE A 92  ? 0.2088 0.2549 0.2654 0.0087  -0.0031 -0.0267 94  ILE A O   
762  C CB  . ILE A 92  ? 0.2357 0.2863 0.2871 0.0185  0.0041  -0.0273 94  ILE A CB  
763  C CG1 . ILE A 92  ? 0.2943 0.3478 0.3410 0.0216  0.0092  -0.0260 94  ILE A CG1 
764  C CG2 . ILE A 92  ? 0.2603 0.3089 0.3145 0.0210  0.0007  -0.0299 94  ILE A CG2 
765  C CD1 . ILE A 92  ? 0.2636 0.3085 0.3004 0.0282  0.0076  -0.0259 94  ILE A CD1 
766  N N   . ILE A 93  ? 0.1780 0.2077 0.2227 0.0169  -0.0097 -0.0281 95  ILE A N   
767  C CA  . ILE A 93  ? 0.1867 0.2153 0.2362 0.0127  -0.0142 -0.0293 95  ILE A CA  
768  C C   . ILE A 93  ? 0.1893 0.2296 0.2514 0.0092  -0.0128 -0.0311 95  ILE A C   
769  O O   . ILE A 93  ? 0.2015 0.2469 0.2673 0.0119  -0.0107 -0.0324 95  ILE A O   
770  C CB  . ILE A 93  ? 0.1946 0.2125 0.2376 0.0160  -0.0199 -0.0306 95  ILE A CB  
771  C CG1 . ILE A 93  ? 0.2086 0.2235 0.2541 0.0112  -0.0247 -0.0313 95  ILE A CG1 
772  C CG2 . ILE A 93  ? 0.2165 0.2366 0.2620 0.0197  -0.0206 -0.0325 95  ILE A CG2 
773  C CD1 . ILE A 93  ? 0.2229 0.2318 0.2632 0.0084  -0.0252 -0.0293 95  ILE A CD1 
774  N N   . THR A 94  ? 0.1900 0.2349 0.2589 0.0030  -0.0138 -0.0313 96  THR A N   
775  C CA  . THR A 94  ? 0.1816 0.2383 0.2631 -0.0009 -0.0122 -0.0332 96  THR A CA  
776  C C   . THR A 94  ? 0.2196 0.2753 0.3054 -0.0007 -0.0173 -0.0353 96  THR A C   
777  O O   . THR A 94  ? 0.2257 0.2757 0.3092 -0.0030 -0.0221 -0.0353 96  THR A O   
778  C CB  . THR A 94  ? 0.2304 0.2937 0.3175 -0.0080 -0.0105 -0.0323 96  THR A CB  
779  O OG1 . THR A 94  ? 0.2879 0.3537 0.3718 -0.0083 -0.0056 -0.0302 96  THR A OG1 
780  C CG2 . THR A 94  ? 0.2976 0.3734 0.3981 -0.0121 -0.0090 -0.0346 96  THR A CG2 
781  N N   . LEU A 95  ? 0.2093 0.2704 0.3012 0.0019  -0.0164 -0.0370 97  LEU A N   
782  C CA  . LEU A 95  ? 0.1899 0.2534 0.2888 0.0014  -0.0205 -0.0389 97  LEU A CA  
783  C C   . LEU A 95  ? 0.2184 0.2928 0.3292 -0.0050 -0.0195 -0.0400 97  LEU A C   
784  O O   . LEU A 95  ? 0.2900 0.3744 0.4089 -0.0064 -0.0145 -0.0408 97  LEU A O   
785  C CB  . LEU A 95  ? 0.1976 0.2634 0.2993 0.0065  -0.0196 -0.0400 97  LEU A CB  
786  C CG  . LEU A 95  ? 0.1868 0.2557 0.2964 0.0067  -0.0238 -0.0417 97  LEU A CG  
787  C CD1 . LEU A 95  ? 0.2277 0.2864 0.3295 0.0078  -0.0305 -0.0413 97  LEU A CD1 
788  C CD2 . LEU A 95  ? 0.2407 0.3131 0.3542 0.0114  -0.0218 -0.0425 97  LEU A CD2 
789  N N   . ALA A 96  ? 0.2102 0.2829 0.3221 -0.0090 -0.0240 -0.0402 98  ALA A N   
790  C CA  . ALA A 96  ? 0.2665 0.3495 0.3892 -0.0156 -0.0234 -0.0412 98  ALA A CA  
791  C C   . ALA A 96  ? 0.2894 0.3804 0.4234 -0.0156 -0.0253 -0.0435 98  ALA A C   
792  O O   . ALA A 96  ? 0.2636 0.3661 0.4088 -0.0195 -0.0227 -0.0449 98  ALA A O   
793  C CB  . ALA A 96  ? 0.2617 0.3395 0.3801 -0.0207 -0.0271 -0.0402 98  ALA A CB  
794  N N   . ASP A 97  ? 0.2224 0.3079 0.3538 -0.0113 -0.0298 -0.0438 99  ASP A N   
795  C CA  . ASP A 97  ? 0.2186 0.3112 0.3604 -0.0114 -0.0325 -0.0455 99  ASP A CA  
796  C C   . ASP A 97  ? 0.2457 0.3311 0.3824 -0.0054 -0.0365 -0.0453 99  ASP A C   
797  O O   . ASP A 97  ? 0.2203 0.2945 0.3448 -0.0021 -0.0379 -0.0441 99  ASP A O   
798  C CB  . ASP A 97  ? 0.2280 0.3234 0.3738 -0.0177 -0.0366 -0.0460 99  ASP A CB  
799  C CG  . ASP A 97  ? 0.2652 0.3738 0.4261 -0.0200 -0.0365 -0.0480 99  ASP A CG  
800  O OD1 . ASP A 97  ? 0.2618 0.3761 0.4298 -0.0160 -0.0341 -0.0490 99  ASP A OD1 
801  O OD2 . ASP A 97  ? 0.3162 0.4294 0.4817 -0.0258 -0.0389 -0.0485 99  ASP A OD2 
802  N N   . ILE A 98  ? 0.1898 0.2819 0.3361 -0.0040 -0.0382 -0.0465 100 ILE A N   
803  C CA  . ILE A 98  ? 0.2060 0.2930 0.3494 0.0010  -0.0426 -0.0462 100 ILE A CA  
804  C C   . ILE A 98  ? 0.1903 0.2844 0.3436 -0.0015 -0.0471 -0.0471 100 ILE A C   
805  O O   . ILE A 98  ? 0.2424 0.3480 0.4085 -0.0035 -0.0447 -0.0484 100 ILE A O   
806  C CB  . ILE A 98  ? 0.2551 0.3439 0.4008 0.0069  -0.0391 -0.0464 100 ILE A CB  
807  C CG1 . ILE A 98  ? 0.2958 0.3814 0.4345 0.0084  -0.0333 -0.0457 100 ILE A CG1 
808  C CG2 . ILE A 98  ? 0.3096 0.3917 0.4501 0.0119  -0.0439 -0.0456 100 ILE A CG2 
809  C CD1 . ILE A 98  ? 0.3083 0.3991 0.4525 0.0123  -0.0283 -0.0464 100 ILE A CD1 
810  N N   . VAL A 99  ? 0.2105 0.2979 0.3579 -0.0016 -0.0535 -0.0465 101 VAL A N   
811  C CA  . VAL A 99  ? 0.1802 0.2742 0.3362 -0.0043 -0.0583 -0.0471 101 VAL A CA  
812  C C   . VAL A 99  ? 0.2369 0.3254 0.3885 -0.0001 -0.0638 -0.0463 101 VAL A C   
813  O O   . VAL A 99  ? 0.2647 0.3427 0.4048 0.0037  -0.0645 -0.0454 101 VAL A O   
814  C CB  . VAL A 99  ? 0.1984 0.2917 0.3525 -0.0113 -0.0612 -0.0473 101 VAL A CB  
815  C CG1 . VAL A 99  ? 0.2032 0.3019 0.3610 -0.0159 -0.0559 -0.0479 101 VAL A CG1 
816  C CG2 . VAL A 99  ? 0.2573 0.3365 0.3962 -0.0112 -0.0651 -0.0463 101 VAL A CG2 
817  N N   . LYS A 100 ? 0.2153 0.3117 0.3767 -0.0009 -0.0676 -0.0466 102 LYS A N   
818  C CA  . LYS A 100 ? 0.2584 0.3509 0.4166 0.0020  -0.0736 -0.0456 102 LYS A CA  
819  C C   . LYS A 100 ? 0.2642 0.3515 0.4156 -0.0029 -0.0795 -0.0454 102 LYS A C   
820  O O   . LYS A 100 ? 0.2894 0.3842 0.4482 -0.0082 -0.0813 -0.0461 102 LYS A O   
821  C CB  . LYS A 100 ? 0.2892 0.3932 0.4618 0.0039  -0.0750 -0.0457 102 LYS A CB  
822  C CG  . LYS A 100 ? 0.4509 0.5605 0.6316 0.0085  -0.0692 -0.0461 102 LYS A CG  
823  C CD  . LYS A 100 ? 0.5972 0.7164 0.7910 0.0111  -0.0715 -0.0459 102 LYS A CD  
824  C CE  . LYS A 100 ? 0.6824 0.8115 0.8891 0.0127  -0.0652 -0.0472 102 LYS A CE  
825  N NZ  . LYS A 100 ? 0.7750 0.9172 0.9977 0.0115  -0.0669 -0.0479 102 LYS A NZ  
826  N N   . ASP A 101 ? 0.2626 0.3375 0.4001 -0.0012 -0.0825 -0.0447 103 ASP A N   
827  C CA  . ASP A 101 ? 0.2761 0.3454 0.4066 -0.0057 -0.0882 -0.0447 103 ASP A CA  
828  C C   . ASP A 101 ? 0.2797 0.3547 0.4162 -0.0059 -0.0942 -0.0442 103 ASP A C   
829  O O   . ASP A 101 ? 0.3032 0.3772 0.4391 -0.0008 -0.0958 -0.0432 103 ASP A O   
830  C CB  . ASP A 101 ? 0.2749 0.3288 0.3884 -0.0041 -0.0894 -0.0443 103 ASP A CB  
831  C CG  . ASP A 101 ? 0.3153 0.3624 0.4210 -0.0094 -0.0945 -0.0446 103 ASP A CG  
832  O OD1 . ASP A 101 ? 0.3778 0.4227 0.4811 -0.0141 -0.0931 -0.0451 103 ASP A OD1 
833  O OD2 . ASP A 101 ? 0.3536 0.3980 0.4556 -0.0093 -0.1000 -0.0443 103 ASP A OD2 
834  N N   . PRO A 102 ? 0.3118 0.3928 0.4536 -0.0117 -0.0977 -0.0446 104 PRO A N   
835  C CA  . PRO A 102 ? 0.3014 0.3895 0.4500 -0.0120 -0.1034 -0.0439 104 PRO A CA  
836  C C   . PRO A 102 ? 0.3129 0.3909 0.4493 -0.0115 -0.1093 -0.0430 104 PRO A C   
837  O O   . PRO A 102 ? 0.3050 0.3878 0.4458 -0.0101 -0.1139 -0.0420 104 PRO A O   
838  C CB  . PRO A 102 ? 0.3379 0.4353 0.4950 -0.0190 -0.1048 -0.0448 104 PRO A CB  
839  C CG  . PRO A 102 ? 0.2969 0.3857 0.4444 -0.0234 -0.1026 -0.0456 104 PRO A CG  
840  C CD  . PRO A 102 ? 0.2598 0.3418 0.4017 -0.0184 -0.0967 -0.0456 104 PRO A CD  
841  N N   . VAL A 103 ? 0.2650 0.3296 0.3866 -0.0129 -0.1095 -0.0435 105 VAL A N   
842  C CA  . VAL A 103 ? 0.2990 0.3536 0.4083 -0.0130 -0.1149 -0.0431 105 VAL A CA  
843  C C   . VAL A 103 ? 0.3228 0.3707 0.4254 -0.0060 -0.1139 -0.0423 105 VAL A C   
844  O O   . VAL A 103 ? 0.3463 0.3937 0.4470 -0.0040 -0.1183 -0.0413 105 VAL A O   
845  C CB  . VAL A 103 ? 0.3003 0.3431 0.3967 -0.0178 -0.1156 -0.0442 105 VAL A CB  
846  C CG1 . VAL A 103 ? 0.3134 0.3444 0.3958 -0.0174 -0.1204 -0.0442 105 VAL A CG1 
847  C CG2 . VAL A 103 ? 0.3548 0.4041 0.4573 -0.0254 -0.1176 -0.0448 105 VAL A CG2 
848  N N   . SER A 104 ? 0.3180 0.3607 0.4164 -0.0025 -0.1081 -0.0426 106 SER A N   
849  C CA  . SER A 104 ? 0.3063 0.3423 0.3975 0.0038  -0.1067 -0.0420 106 SER A CA  
850  C C   . SER A 104 ? 0.3687 0.4142 0.4710 0.0085  -0.1057 -0.0408 106 SER A C   
851  O O   . SER A 104 ? 0.4099 0.4512 0.5071 0.0133  -0.1065 -0.0399 106 SER A O   
852  C CB  . SER A 104 ? 0.3068 0.3353 0.3906 0.0059  -0.1007 -0.0426 106 SER A CB  
853  O OG  . SER A 104 ? 0.3264 0.3638 0.4211 0.0065  -0.0953 -0.0427 106 SER A OG  
854  N N   . ARG A 105 ? 0.2880 0.3460 0.4052 0.0073  -0.1038 -0.0409 107 ARG A N   
855  C CA  . ARG A 105 ? 0.3070 0.3740 0.4358 0.0120  -0.1017 -0.0400 107 ARG A CA  
856  C C   . ARG A 105 ? 0.3887 0.4510 0.5133 0.0170  -0.0957 -0.0401 107 ARG A C   
857  O O   . ARG A 105 ? 0.4361 0.4999 0.5634 0.0220  -0.0950 -0.0390 107 ARG A O   
858  C CB  . ARG A 105 ? 0.3927 0.4619 0.5233 0.0143  -0.1075 -0.0383 107 ARG A CB  
859  C CG  . ARG A 105 ? 0.4323 0.5048 0.5644 0.0090  -0.1141 -0.0381 107 ARG A CG  
860  C CD  . ARG A 105 ? 0.4490 0.5224 0.5807 0.0111  -0.1203 -0.0361 107 ARG A CD  
861  N NE  . ARG A 105 ? 0.3881 0.4709 0.5325 0.0159  -0.1194 -0.0346 107 ARG A NE  
862  C CZ  . ARG A 105 ? 0.3900 0.4860 0.5502 0.0149  -0.1197 -0.0344 107 ARG A CZ  
863  N NH1 . ARG A 105 ? 0.4436 0.5453 0.6085 0.0091  -0.1209 -0.0355 107 ARG A NH1 
864  N NH2 . ARG A 105 ? 0.3971 0.5004 0.5683 0.0198  -0.1187 -0.0330 107 ARG A NH2 
865  N N   . THR A 106 ? 0.3297 0.3861 0.4473 0.0156  -0.0915 -0.0411 108 THR A N   
866  C CA  . THR A 106 ? 0.3094 0.3614 0.4221 0.0197  -0.0856 -0.0412 108 THR A CA  
867  C C   . THR A 106 ? 0.3044 0.3603 0.4215 0.0170  -0.0798 -0.0422 108 THR A C   
868  O O   . THR A 106 ? 0.2812 0.3406 0.4022 0.0117  -0.0808 -0.0430 108 THR A O   
869  C CB  . THR A 106 ? 0.3149 0.3532 0.4108 0.0215  -0.0867 -0.0410 108 THR A CB  
870  O OG1 . THR A 106 ? 0.3382 0.3703 0.4267 0.0169  -0.0878 -0.0419 108 THR A OG1 
871  C CG2 . THR A 106 ? 0.4004 0.4347 0.4910 0.0240  -0.0923 -0.0400 108 THR A CG2 
872  N N   . PRO A 107 ? 0.3049 0.3604 0.4212 0.0201  -0.0738 -0.0423 109 PRO A N   
873  C CA  . PRO A 107 ? 0.2906 0.3493 0.4098 0.0172  -0.0683 -0.0432 109 PRO A CA  
874  C C   . PRO A 107 ? 0.3247 0.3738 0.4321 0.0142  -0.0687 -0.0432 109 PRO A C   
875  O O   . PRO A 107 ? 0.3047 0.3431 0.3997 0.0163  -0.0710 -0.0428 109 PRO A O   
876  C CB  . PRO A 107 ? 0.2896 0.3491 0.4091 0.0217  -0.0623 -0.0430 109 PRO A CB  
877  C CG  . PRO A 107 ? 0.3123 0.3726 0.4341 0.0265  -0.0647 -0.0422 109 PRO A CG  
878  C CD  . PRO A 107 ? 0.3378 0.3912 0.4518 0.0261  -0.0716 -0.0416 109 PRO A CD  
879  N N   . ALA A 108 ? 0.2438 0.2971 0.3555 0.0094  -0.0663 -0.0438 110 ALA A N   
880  C CA  . ALA A 108 ? 0.2487 0.2938 0.3506 0.0064  -0.0658 -0.0437 110 ALA A CA  
881  C C   . ALA A 108 ? 0.2448 0.2938 0.3494 0.0058  -0.0591 -0.0436 110 ALA A C   
882  O O   . ALA A 108 ? 0.2710 0.3306 0.3870 0.0027  -0.0564 -0.0443 110 ALA A O   
883  C CB  . ALA A 108 ? 0.3045 0.3502 0.4080 0.0001  -0.0701 -0.0441 110 ALA A CB  
884  N N   . LEU A 109 ? 0.2044 0.2451 0.2985 0.0086  -0.0563 -0.0429 111 LEU A N   
885  C CA  . LEU A 109 ? 0.1944 0.2383 0.2897 0.0079  -0.0500 -0.0425 111 LEU A CA  
886  C C   . LEU A 109 ? 0.2473 0.2877 0.3387 0.0027  -0.0502 -0.0420 111 LEU A C   
887  O O   . LEU A 109 ? 0.2535 0.2832 0.3346 0.0025  -0.0536 -0.0416 111 LEU A O   
888  C CB  . LEU A 109 ? 0.2091 0.2466 0.2952 0.0135  -0.0468 -0.0417 111 LEU A CB  
889  C CG  . LEU A 109 ? 0.2705 0.3103 0.3589 0.0188  -0.0464 -0.0419 111 LEU A CG  
890  C CD1 . LEU A 109 ? 0.2724 0.3060 0.3510 0.0236  -0.0430 -0.0411 111 LEU A CD1 
891  C CD2 . LEU A 109 ? 0.4465 0.4990 0.5491 0.0178  -0.0432 -0.0427 111 LEU A CD2 
892  N N   . VAL A 110 ? 0.1989 0.2479 0.2983 -0.0014 -0.0464 -0.0421 112 VAL A N   
893  C CA  . VAL A 110 ? 0.1955 0.2425 0.2925 -0.0069 -0.0463 -0.0415 112 VAL A CA  
894  C C   . VAL A 110 ? 0.2039 0.2500 0.2969 -0.0060 -0.0406 -0.0401 112 VAL A C   
895  O O   . VAL A 110 ? 0.2182 0.2733 0.3183 -0.0056 -0.0356 -0.0404 112 VAL A O   
896  C CB  . VAL A 110 ? 0.2211 0.2792 0.3303 -0.0132 -0.0467 -0.0425 112 VAL A CB  
897  C CG1 . VAL A 110 ? 0.2466 0.3025 0.3530 -0.0194 -0.0468 -0.0416 112 VAL A CG1 
898  C CG2 . VAL A 110 ? 0.2067 0.2670 0.3207 -0.0137 -0.0523 -0.0436 112 VAL A CG2 
899  N N   . PHE A 111 ? 0.1987 0.2342 0.2806 -0.0059 -0.0413 -0.0388 113 PHE A N   
900  C CA  . PHE A 111 ? 0.2268 0.2602 0.3034 -0.0046 -0.0366 -0.0370 113 PHE A CA  
901  C C   . PHE A 111 ? 0.2356 0.2677 0.3110 -0.0104 -0.0363 -0.0357 113 PHE A C   
902  O O   . PHE A 111 ? 0.2553 0.2829 0.3291 -0.0142 -0.0407 -0.0359 113 PHE A O   
903  C CB  . PHE A 111 ? 0.2436 0.2648 0.3071 0.0013  -0.0373 -0.0362 113 PHE A CB  
904  C CG  . PHE A 111 ? 0.2316 0.2528 0.2944 0.0072  -0.0374 -0.0371 113 PHE A CG  
905  C CD1 . PHE A 111 ? 0.1961 0.2229 0.2610 0.0104  -0.0323 -0.0368 113 PHE A CD1 
906  C CD2 . PHE A 111 ? 0.2734 0.2890 0.3331 0.0091  -0.0426 -0.0382 113 PHE A CD2 
907  C CE1 . PHE A 111 ? 0.2522 0.2785 0.3159 0.0156  -0.0324 -0.0375 113 PHE A CE1 
908  C CE2 . PHE A 111 ? 0.2823 0.2979 0.3411 0.0143  -0.0428 -0.0388 113 PHE A CE2 
909  C CZ  . PHE A 111 ? 0.2493 0.2700 0.3100 0.0176  -0.0377 -0.0385 113 PHE A CZ  
910  N N   . GLU A 112 ? 0.2216 0.2574 0.2971 -0.0111 -0.0312 -0.0341 114 GLU A N   
911  C CA  . GLU A 112 ? 0.2541 0.2862 0.3257 -0.0154 -0.0310 -0.0322 114 GLU A CA  
912  C C   . GLU A 112 ? 0.2860 0.3026 0.3449 -0.0127 -0.0348 -0.0312 114 GLU A C   
913  O O   . GLU A 112 ? 0.3048 0.3143 0.3568 -0.0067 -0.0358 -0.0317 114 GLU A O   
914  C CB  . GLU A 112 ? 0.2753 0.3127 0.3474 -0.0154 -0.0250 -0.0302 114 GLU A CB  
915  C CG  . GLU A 112 ? 0.2826 0.3128 0.3452 -0.0085 -0.0231 -0.0290 114 GLU A CG  
916  C CD  . GLU A 112 ? 0.3565 0.3916 0.4185 -0.0085 -0.0174 -0.0267 114 GLU A CD  
917  O OE1 . GLU A 112 ? 0.4672 0.5039 0.5298 -0.0132 -0.0164 -0.0248 114 GLU A OE1 
918  O OE2 . GLU A 112 ? 0.2807 0.3184 0.3416 -0.0039 -0.0140 -0.0268 114 GLU A OE2 
919  N N   . HIS A 113 ? 0.2692 0.2805 0.3249 -0.0174 -0.0369 -0.0300 115 HIS A N   
920  C CA  . HIS A 113 ? 0.3118 0.3079 0.3557 -0.0157 -0.0405 -0.0293 115 HIS A CA  
921  C C   . HIS A 113 ? 0.3180 0.3081 0.3544 -0.0134 -0.0374 -0.0265 115 HIS A C   
922  O O   . HIS A 113 ? 0.3366 0.3328 0.3767 -0.0170 -0.0342 -0.0245 115 HIS A O   
923  C CB  . HIS A 113 ? 0.3246 0.3172 0.3689 -0.0224 -0.0449 -0.0297 115 HIS A CB  
924  C CG  . HIS A 113 ? 0.3945 0.3711 0.4268 -0.0215 -0.0483 -0.0290 115 HIS A CG  
925  N ND1 . HIS A 113 ? 0.4061 0.3761 0.4331 -0.0237 -0.0476 -0.0265 115 HIS A ND1 
926  C CD2 . HIS A 113 ? 0.4705 0.4361 0.4948 -0.0187 -0.0525 -0.0305 115 HIS A CD2 
927  C CE1 . HIS A 113 ? 0.4273 0.3825 0.4437 -0.0221 -0.0509 -0.0266 115 HIS A CE1 
928  N NE2 . HIS A 113 ? 0.4659 0.4182 0.4804 -0.0192 -0.0539 -0.0291 115 HIS A NE2 
929  N N   . VAL A 114 ? 0.3165 0.2951 0.3423 -0.0074 -0.0383 -0.0263 116 VAL A N   
930  C CA  . VAL A 114 ? 0.3361 0.3072 0.3537 -0.0046 -0.0361 -0.0236 116 VAL A CA  
931  C C   . VAL A 114 ? 0.3186 0.2744 0.3267 -0.0049 -0.0404 -0.0235 116 VAL A C   
932  O O   . VAL A 114 ? 0.3772 0.3253 0.3803 -0.0026 -0.0440 -0.0258 116 VAL A O   
933  C CB  . VAL A 114 ? 0.3025 0.2732 0.3158 0.0030  -0.0329 -0.0234 116 VAL A CB  
934  C CG1 . VAL A 114 ? 0.3540 0.3172 0.3589 0.0060  -0.0307 -0.0205 116 VAL A CG1 
935  C CG2 . VAL A 114 ? 0.3046 0.2899 0.3270 0.0029  -0.0285 -0.0236 116 VAL A CG2 
936  N N   . ASN A 115 ? 0.3795 0.3307 0.3848 -0.0078 -0.0400 -0.0209 117 ASN A N   
937  C CA  . ASN A 115 ? 0.4433 0.3790 0.4389 -0.0081 -0.0436 -0.0206 117 ASN A CA  
938  C C   . ASN A 115 ? 0.5132 0.4388 0.4988 -0.0002 -0.0421 -0.0199 117 ASN A C   
939  O O   . ASN A 115 ? 0.5729 0.4957 0.5551 0.0015  -0.0395 -0.0169 117 ASN A O   
940  C CB  . ASN A 115 ? 0.5449 0.4795 0.5417 -0.0144 -0.0437 -0.0179 117 ASN A CB  
941  C CG  . ASN A 115 ? 0.6813 0.5993 0.6683 -0.0151 -0.0475 -0.0176 117 ASN A CG  
942  O OD1 . ASN A 115 ? 0.7550 0.6638 0.7362 -0.0132 -0.0509 -0.0202 117 ASN A OD1 
943  N ND2 . ASN A 115 ? 0.7365 0.6505 0.7215 -0.0182 -0.0469 -0.0144 117 ASN A ND2 
944  N N   . ASN A 116 ? 0.5535 0.4737 0.5342 0.0045  -0.0439 -0.0225 118 ASN A N   
945  C CA  . ASN A 116 ? 0.6466 0.5607 0.6194 0.0124  -0.0420 -0.0225 118 ASN A CA  
946  C C   . ASN A 116 ? 0.6784 0.5753 0.6397 0.0148  -0.0445 -0.0227 118 ASN A C   
947  O O   . ASN A 116 ? 0.6324 0.5211 0.5909 0.0109  -0.0485 -0.0240 118 ASN A O   
948  C CB  . ASN A 116 ? 0.6941 0.6126 0.6681 0.0159  -0.0425 -0.0253 118 ASN A CB  
949  C CG  . ASN A 116 ? 0.7886 0.6993 0.7532 0.0237  -0.0416 -0.0260 118 ASN A CG  
950  O OD1 . ASN A 116 ? 0.8236 0.7256 0.7818 0.0257  -0.0448 -0.0285 118 ASN A OD1 
951  N ND2 . ASN A 116 ? 0.7217 0.6359 0.6853 0.0278  -0.0371 -0.0238 118 ASN A ND2 
952  N N   . THR A 117 ? 0.7308 0.6224 0.6854 0.0212  -0.0418 -0.0214 119 THR A N   
953  C CA  . THR A 117 ? 0.8034 0.6791 0.7466 0.0255  -0.0436 -0.0225 119 THR A CA  
954  C C   . THR A 117 ? 0.7905 0.6655 0.7292 0.0320  -0.0430 -0.0250 119 THR A C   
955  O O   . THR A 117 ? 0.7798 0.6644 0.7216 0.0355  -0.0395 -0.0242 119 THR A O   
956  C CB  . THR A 117 ? 0.8990 0.7680 0.8372 0.0285  -0.0410 -0.0192 119 THR A CB  
957  O OG1 . THR A 117 ? 0.9510 0.8323 0.8949 0.0301  -0.0364 -0.0162 119 THR A OG1 
958  C CG2 . THR A 117 ? 0.9050 0.7672 0.8430 0.0227  -0.0432 -0.0174 119 THR A CG2 
959  N N   . ASP A 118 ? 0.7750 0.6389 0.7062 0.0332  -0.0465 -0.0280 120 ASP A N   
960  C CA  . ASP A 118 ? 0.8351 0.6977 0.7613 0.0390  -0.0463 -0.0305 120 ASP A CA  
961  C C   . ASP A 118 ? 0.7531 0.6138 0.6740 0.0461  -0.0422 -0.0290 120 ASP A C   
962  O O   . ASP A 118 ? 0.7991 0.6522 0.7158 0.0475  -0.0410 -0.0270 120 ASP A O   
963  C CB  . ASP A 118 ? 0.9466 0.7964 0.8645 0.0387  -0.0507 -0.0339 120 ASP A CB  
964  C CG  . ASP A 118 ? 1.0799 0.9354 1.0027 0.0345  -0.0544 -0.0362 120 ASP A CG  
965  O OD1 . ASP A 118 ? 1.1578 1.0043 1.0747 0.0330  -0.0583 -0.0390 120 ASP A OD1 
966  O OD2 . ASP A 118 ? 1.1347 1.0039 1.0673 0.0324  -0.0533 -0.0353 120 ASP A OD2 
967  N N   . PHE A 119 ? 0.7005 0.5684 0.6218 0.0504  -0.0401 -0.0297 121 PHE A N   
968  C CA  . PHE A 119 ? 0.7297 0.5988 0.6475 0.0567  -0.0358 -0.0280 121 PHE A CA  
969  C C   . PHE A 119 ? 0.8210 0.6755 0.7276 0.0617  -0.0362 -0.0291 121 PHE A C   
970  O O   . PHE A 119 ? 0.8113 0.6636 0.7150 0.0657  -0.0332 -0.0268 121 PHE A O   
971  C CB  . PHE A 119 ? 0.6683 0.5479 0.5884 0.0599  -0.0335 -0.0288 121 PHE A CB  
972  C CG  . PHE A 119 ? 0.7062 0.5793 0.6184 0.0641  -0.0353 -0.0321 121 PHE A CG  
973  C CD1 . PHE A 119 ? 0.7873 0.6596 0.7001 0.0614  -0.0393 -0.0349 121 PHE A CD1 
974  C CD2 . PHE A 119 ? 0.7136 0.5819 0.6176 0.0707  -0.0329 -0.0323 121 PHE A CD2 
975  C CE1 . PHE A 119 ? 0.8024 0.6691 0.7076 0.0649  -0.0409 -0.0378 121 PHE A CE1 
976  C CE2 . PHE A 119 ? 0.7596 0.6223 0.6561 0.0743  -0.0344 -0.0355 121 PHE A CE2 
977  C CZ  . PHE A 119 ? 0.7838 0.6456 0.6807 0.0712  -0.0385 -0.0382 121 PHE A CZ  
978  N N   . LYS A 120 ? 0.9199 0.7643 0.8201 0.0615  -0.0399 -0.0326 122 LYS A N   
979  C CA  . LYS A 120 ? 1.0367 0.8666 0.9260 0.0661  -0.0403 -0.0342 122 LYS A CA  
980  C C   . LYS A 120 ? 1.0455 0.8668 0.9331 0.0653  -0.0398 -0.0318 122 LYS A C   
981  O O   . LYS A 120 ? 1.1214 0.9352 1.0027 0.0708  -0.0376 -0.0311 122 LYS A O   
982  C CB  . LYS A 120 ? 1.1194 0.9400 1.0026 0.0645  -0.0447 -0.0384 122 LYS A CB  
983  C CG  . LYS A 120 ? 1.2411 1.0456 1.1128 0.0684  -0.0452 -0.0406 122 LYS A CG  
984  C CD  . LYS A 120 ? 1.2935 1.0875 1.1599 0.0644  -0.0500 -0.0443 122 LYS A CD  
985  C CE  . LYS A 120 ? 1.3296 1.1251 1.1921 0.0661  -0.0516 -0.0477 122 LYS A CE  
986  N NZ  . LYS A 120 ? 1.3435 1.1327 1.1969 0.0733  -0.0491 -0.0494 122 LYS A NZ  
987  N N   . GLN A 121 ? 0.9406 0.7632 0.8339 0.0587  -0.0417 -0.0303 123 GLN A N   
988  C CA  . GLN A 121 ? 0.9128 0.7277 0.8051 0.0572  -0.0414 -0.0275 123 GLN A CA  
989  C C   . GLN A 121 ? 0.8200 0.6454 0.7186 0.0582  -0.0373 -0.0229 123 GLN A C   
990  O O   . GLN A 121 ? 0.7931 0.6126 0.6885 0.0613  -0.0354 -0.0202 123 GLN A O   
991  C CB  . GLN A 121 ? 1.0247 0.8360 0.9196 0.0492  -0.0454 -0.0280 123 GLN A CB  
992  C CG  . GLN A 121 ? 1.1158 0.9129 1.0024 0.0478  -0.0495 -0.0320 123 GLN A CG  
993  C CD  . GLN A 121 ? 1.1893 0.9897 1.0745 0.0488  -0.0512 -0.0358 123 GLN A CD  
994  O OE1 . GLN A 121 ? 1.2257 1.0392 1.1168 0.0501  -0.0496 -0.0355 123 GLN A OE1 
995  N NE2 . GLN A 121 ? 1.1956 0.9839 1.0728 0.0481  -0.0545 -0.0394 123 GLN A NE2 
996  N N   . LEU A 122 ? 0.6585 0.4994 0.5662 0.0554  -0.0359 -0.0217 124 LEU A N   
997  C CA  . LEU A 122 ? 0.6212 0.4730 0.5349 0.0558  -0.0319 -0.0175 124 LEU A CA  
998  C C   . LEU A 122 ? 0.5529 0.4052 0.4620 0.0637  -0.0281 -0.0164 124 LEU A C   
999  O O   . LEU A 122 ? 0.6091 0.4630 0.5188 0.0656  -0.0254 -0.0125 124 LEU A O   
1000 C CB  . LEU A 122 ? 0.6646 0.5326 0.5884 0.0514  -0.0310 -0.0173 124 LEU A CB  
1001 C CG  . LEU A 122 ? 0.7156 0.5955 0.6470 0.0491  -0.0275 -0.0130 124 LEU A CG  
1002 C CD1 . LEU A 122 ? 0.7025 0.5768 0.6348 0.0443  -0.0289 -0.0104 124 LEU A CD1 
1003 C CD2 . LEU A 122 ? 0.7169 0.6120 0.6580 0.0449  -0.0265 -0.0137 124 LEU A CD2 
1004 N N   . TYR A 123 ? 0.4468 0.2982 0.3512 0.0684  -0.0279 -0.0195 125 TYR A N   
1005 C CA  . TYR A 123 ? 0.4697 0.3236 0.3703 0.0756  -0.0241 -0.0185 125 TYR A CA  
1006 C C   . TYR A 123 ? 0.5486 0.3891 0.4412 0.0806  -0.0236 -0.0176 125 TYR A C   
1007 O O   . TYR A 123 ? 0.5418 0.3856 0.4333 0.0857  -0.0200 -0.0150 125 TYR A O   
1008 C CB  . TYR A 123 ? 0.5604 0.4174 0.4582 0.0790  -0.0240 -0.0220 125 TYR A CB  
1009 C CG  . TYR A 123 ? 0.6774 0.5496 0.5835 0.0758  -0.0229 -0.0219 125 TYR A CG  
1010 C CD1 . TYR A 123 ? 0.7448 0.6253 0.6601 0.0693  -0.0232 -0.0200 125 TYR A CD1 
1011 C CD2 . TYR A 123 ? 0.7499 0.6280 0.6545 0.0792  -0.0216 -0.0237 125 TYR A CD2 
1012 C CE1 . TYR A 123 ? 0.7896 0.6836 0.7127 0.0666  -0.0220 -0.0201 125 TYR A CE1 
1013 C CE2 . TYR A 123 ? 0.7907 0.6818 0.7028 0.0764  -0.0206 -0.0236 125 TYR A CE2 
1014 C CZ  . TYR A 123 ? 0.8294 0.7283 0.7508 0.0703  -0.0207 -0.0219 125 TYR A CZ  
1015 O OH  . TYR A 123 ? 0.8496 0.7611 0.7788 0.0677  -0.0194 -0.0220 125 TYR A OH  
1016 N N   . GLN A 124 ? 0.4802 0.3062 0.3675 0.0792  -0.0270 -0.0196 126 GLN A N   
1017 C CA  . GLN A 124 ? 0.5089 0.3215 0.3892 0.0836  -0.0266 -0.0187 126 GLN A CA  
1018 C C   . GLN A 124 ? 0.5163 0.3307 0.4009 0.0820  -0.0250 -0.0134 126 GLN A C   
1019 O O   . GLN A 124 ? 0.5370 0.3408 0.4167 0.0857  -0.0245 -0.0118 126 GLN A O   
1020 C CB  . GLN A 124 ? 0.6032 0.3994 0.4766 0.0817  -0.0306 -0.0223 126 GLN A CB  
1021 C CG  . GLN A 124 ? 0.7581 0.5513 0.6264 0.0827  -0.0326 -0.0275 126 GLN A CG  
1022 C CD  . GLN A 124 ? 0.8718 0.6546 0.7303 0.0903  -0.0313 -0.0301 126 GLN A CD  
1023 O OE1 . GLN A 124 ? 0.9072 0.6845 0.7628 0.0951  -0.0289 -0.0279 126 GLN A OE1 
1024 N NE2 . GLN A 124 ? 0.9125 0.6926 0.7658 0.0913  -0.0329 -0.0346 126 GLN A NE2 
1025 N N   . THR A 125 ? 0.5666 0.3942 0.4602 0.0768  -0.0243 -0.0105 127 THR A N   
1026 C CA  . THR A 125 ? 0.6468 0.4757 0.5449 0.0730  -0.0239 -0.0058 127 THR A CA  
1027 C C   . THR A 125 ? 0.6815 0.5262 0.5862 0.0736  -0.0198 -0.0015 127 THR A C   
1028 O O   . THR A 125 ? 0.7705 0.6154 0.6764 0.0742  -0.0182 0.0031  127 THR A O   
1029 C CB  . THR A 125 ? 0.7844 0.6132 0.6871 0.0642  -0.0274 -0.0066 127 THR A CB  
1030 O OG1 . THR A 125 ? 0.8364 0.6482 0.7325 0.0631  -0.0309 -0.0085 127 THR A OG1 
1031 C CG2 . THR A 125 ? 0.8436 0.6818 0.7541 0.0590  -0.0262 -0.0019 127 THR A CG2 
1032 N N   . LEU A 126 ? 0.5622 0.4201 0.4712 0.0734  -0.0180 -0.0028 128 LEU A N   
1033 C CA  . LEU A 126 ? 0.5302 0.4039 0.4459 0.0728  -0.0141 0.0009  128 LEU A CA  
1034 C C   . LEU A 126 ? 0.5613 0.4350 0.4733 0.0797  -0.0107 0.0042  128 LEU A C   
1035 O O   . LEU A 126 ? 0.5418 0.4083 0.4467 0.0865  -0.0103 0.0022  128 LEU A O   
1036 C CB  . LEU A 126 ? 0.5465 0.4325 0.4660 0.0721  -0.0127 -0.0017 128 LEU A CB  
1037 C CG  . LEU A 126 ? 0.6266 0.5145 0.5508 0.0657  -0.0159 -0.0049 128 LEU A CG  
1038 C CD1 . LEU A 126 ? 0.5726 0.4727 0.5007 0.0658  -0.0141 -0.0069 128 LEU A CD1 
1039 C CD2 . LEU A 126 ? 0.6736 0.5652 0.6047 0.0581  -0.0168 -0.0023 128 LEU A CD2 
1040 N N   . THR A 127 ? 0.4720 0.3542 0.3889 0.0779  -0.0084 0.0092  129 THR A N   
1041 C CA  . THR A 127 ? 0.4142 0.2997 0.3293 0.0837  -0.0049 0.0132  129 THR A CA  
1042 C C   . THR A 127 ? 0.4215 0.3221 0.3390 0.0858  -0.0010 0.0131  129 THR A C   
1043 O O   . THR A 127 ? 0.4513 0.3599 0.3726 0.0823  -0.0010 0.0104  129 THR A O   
1044 C CB  . THR A 127 ? 0.3886 0.2771 0.3080 0.0801  -0.0043 0.0190  129 THR A CB  
1045 O OG1 . THR A 127 ? 0.3883 0.2920 0.3161 0.0732  -0.0029 0.0204  129 THR A OG1 
1046 C CG2 . THR A 127 ? 0.4153 0.2893 0.3326 0.0770  -0.0082 0.0192  129 THR A CG2 
1047 N N   . ASP A 128 ? 0.3492 0.3723 0.3604 0.0727  0.0512  0.0862  130 ASP A N   
1048 C CA  . ASP A 128 ? 0.3349 0.3753 0.3427 0.0713  0.0450  0.0834  130 ASP A CA  
1049 C C   . ASP A 128 ? 0.3332 0.3869 0.3401 0.0679  0.0418  0.0818  130 ASP A C   
1050 O O   . ASP A 128 ? 0.3624 0.4208 0.3674 0.0623  0.0362  0.0738  130 ASP A O   
1051 C CB  . ASP A 128 ? 0.3552 0.4084 0.3622 0.0784  0.0470  0.0917  130 ASP A CB  
1052 C CG  . ASP A 128 ? 0.3795 0.4530 0.3835 0.0767  0.0412  0.0891  130 ASP A CG  
1053 O OD1 . ASP A 128 ? 0.3808 0.4525 0.3832 0.0708  0.0361  0.0801  130 ASP A OD1 
1054 O OD2 . ASP A 128 ? 0.4708 0.5625 0.4744 0.0813  0.0419  0.0965  130 ASP A OD2 
1055 N N   . TYR A 129 ? 0.3234 0.3821 0.3316 0.0711  0.0459  0.0893  131 TYR A N   
1056 C CA  . TYR A 129 ? 0.2930 0.3648 0.3000 0.0682  0.0435  0.0878  131 TYR A CA  
1057 C C   . TYR A 129 ? 0.3497 0.4108 0.3582 0.0609  0.0408  0.0784  131 TYR A C   
1058 O O   . TYR A 129 ? 0.3374 0.4071 0.3440 0.0563  0.0360  0.0720  131 TYR A O   
1059 C CB  . TYR A 129 ? 0.3128 0.3915 0.3207 0.0735  0.0490  0.0985  131 TYR A CB  
1060 C CG  . TYR A 129 ? 0.3820 0.4769 0.3876 0.0709  0.0466  0.0974  131 TYR A CG  
1061 C CD1 . TYR A 129 ? 0.3638 0.4811 0.3654 0.0722  0.0433  0.0989  131 TYR A CD1 
1062 C CD2 . TYR A 129 ? 0.3973 0.4856 0.4047 0.0668  0.0475  0.0940  131 TYR A CD2 
1063 C CE1 . TYR A 129 ? 0.4200 0.5523 0.4191 0.0693  0.0413  0.0968  131 TYR A CE1 
1064 C CE2 . TYR A 129 ? 0.4267 0.5295 0.4319 0.0643  0.0456  0.0924  131 TYR A CE2 
1065 C CZ  . TYR A 129 ? 0.4748 0.5992 0.4755 0.0656  0.0426  0.0937  131 TYR A CZ  
1066 O OH  . TYR A 129 ? 0.4804 0.6192 0.4785 0.0628  0.0410  0.0913  131 TYR A OH  
1067 N N   . ASP A 130 ? 0.3217 0.3642 0.3337 0.0597  0.0439  0.0771  132 ASP A N   
1068 C CA  . ASP A 130 ? 0.3676 0.4009 0.3816 0.0530  0.0411  0.0682  132 ASP A CA  
1069 C C   . ASP A 130 ? 0.3551 0.3890 0.3667 0.0486  0.0344  0.0590  132 ASP A C   
1070 O O   . ASP A 130 ? 0.3318 0.3687 0.3433 0.0440  0.0307  0.0526  132 ASP A O   
1071 C CB  . ASP A 130 ? 0.3537 0.3675 0.3718 0.0520  0.0450  0.0674  132 ASP A CB  
1072 C CG  . ASP A 130 ? 0.4631 0.4734 0.4846 0.0551  0.0522  0.0755  132 ASP A CG  
1073 O OD1 . ASP A 130 ? 0.4857 0.5072 0.5071 0.0560  0.0534  0.0797  132 ASP A OD1 
1074 O OD2 . ASP A 130 ? 0.4103 0.4057 0.4346 0.0563  0.0572  0.0774  132 ASP A OD2 
1075 N N   . ILE A 131 ? 0.3065 0.3368 0.3162 0.0501  0.0334  0.0583  133 ILE A N   
1076 C CA  . ILE A 131 ? 0.3076 0.3367 0.3150 0.0460  0.0278  0.0502  133 ILE A CA  
1077 C C   . ILE A 131 ? 0.3434 0.3889 0.3482 0.0441  0.0239  0.0478  133 ILE A C   
1078 O O   . ILE A 131 ? 0.3043 0.3494 0.3086 0.0394  0.0199  0.0405  133 ILE A O   
1079 C CB  . ILE A 131 ? 0.3505 0.3737 0.3562 0.0485  0.0282  0.0509  133 ILE A CB  
1080 C CG1 . ILE A 131 ? 0.3316 0.3366 0.3395 0.0488  0.0316  0.0504  133 ILE A CG1 
1081 C CG2 . ILE A 131 ? 0.3128 0.3379 0.3155 0.0450  0.0228  0.0439  133 ILE A CG2 
1082 C CD1 . ILE A 131 ? 0.4121 0.4111 0.4185 0.0524  0.0338  0.0525  133 ILE A CD1 
1083 N N   . ARG A 132 ? 0.2613 0.3218 0.2644 0.0479  0.0253  0.0540  134 ARG A N   
1084 C CA  . ARG A 132 ? 0.2828 0.3602 0.2834 0.0455  0.0219  0.0512  134 ARG A CA  
1085 C C   . ARG A 132 ? 0.2521 0.3316 0.2536 0.0418  0.0213  0.0475  134 ARG A C   
1086 O O   . ARG A 132 ? 0.2524 0.3358 0.2527 0.0372  0.0178  0.0403  134 ARG A O   
1087 C CB  . ARG A 132 ? 0.2555 0.3504 0.2544 0.0504  0.0237  0.0591  134 ARG A CB  
1088 C CG  . ARG A 132 ? 0.2544 0.3485 0.2532 0.0549  0.0250  0.0636  134 ARG A CG  
1089 C CD  . ARG A 132 ? 0.3104 0.4258 0.3074 0.0588  0.0251  0.0697  134 ARG A CD  
1090 N NE  . ARG A 132 ? 0.2760 0.3908 0.2741 0.0653  0.0282  0.0771  134 ARG A NE  
1091 C CZ  . ARG A 132 ? 0.2597 0.3911 0.2569 0.0681  0.0272  0.0804  134 ARG A CZ  
1092 N NH1 . ARG A 132 ? 0.3050 0.4545 0.3001 0.0641  0.0231  0.0762  134 ARG A NH1 
1093 N NH2 . ARG A 132 ? 0.3230 0.4532 0.3217 0.0747  0.0306  0.0876  134 ARG A NH2 
1094 N N   . PHE A 133 ? 0.2733 0.3499 0.2771 0.0440  0.0251  0.0526  135 PHE A N   
1095 C CA  . PHE A 133 ? 0.2329 0.3122 0.2379 0.0409  0.0252  0.0498  135 PHE A CA  
1096 C C   . PHE A 133 ? 0.2484 0.3161 0.2555 0.0357  0.0221  0.0407  135 PHE A C   
1097 O O   . PHE A 133 ? 0.2484 0.3217 0.2549 0.0320  0.0197  0.0348  135 PHE A O   
1098 C CB  . PHE A 133 ? 0.2399 0.3154 0.2477 0.0442  0.0307  0.0573  135 PHE A CB  
1099 C CG  . PHE A 133 ? 0.3008 0.3779 0.3106 0.0411  0.0314  0.0547  135 PHE A CG  
1100 C CD1 . PHE A 133 ? 0.3620 0.4555 0.3691 0.0415  0.0319  0.0567  135 PHE A CD1 
1101 C CD2 . PHE A 133 ? 0.3072 0.3702 0.3215 0.0379  0.0316  0.0503  135 PHE A CD2 
1102 C CE1 . PHE A 133 ? 0.3849 0.4799 0.3938 0.0389  0.0330  0.0542  135 PHE A CE1 
1103 C CE2 . PHE A 133 ? 0.3685 0.4337 0.3853 0.0353  0.0325  0.0481  135 PHE A CE2 
1104 C CZ  . PHE A 133 ? 0.3759 0.4566 0.3899 0.0359  0.0334  0.0501  135 PHE A CZ  
1105 N N   . TYR A 134 ? 0.2499 0.3018 0.2594 0.0354  0.0224  0.0395  136 TYR A N   
1106 C CA  . TYR A 134 ? 0.2571 0.2992 0.2690 0.0310  0.0194  0.0317  136 TYR A CA  
1107 C C   . TYR A 134 ? 0.2368 0.2801 0.2458 0.0284  0.0148  0.0254  136 TYR A C   
1108 O O   . TYR A 134 ? 0.2615 0.3034 0.2716 0.0250  0.0123  0.0192  136 TYR A O   
1109 C CB  . TYR A 134 ? 0.2647 0.2911 0.2799 0.0311  0.0210  0.0319  136 TYR A CB  
1110 C CG  . TYR A 134 ? 0.2923 0.3153 0.3116 0.0318  0.0256  0.0361  136 TYR A CG  
1111 C CD1 . TYR A 134 ? 0.3002 0.3273 0.3224 0.0294  0.0258  0.0342  136 TYR A CD1 
1112 C CD2 . TYR A 134 ? 0.3373 0.3522 0.3581 0.0347  0.0303  0.0418  136 TYR A CD2 
1113 C CE1 . TYR A 134 ? 0.2830 0.3071 0.3095 0.0297  0.0305  0.0381  136 TYR A CE1 
1114 C CE2 . TYR A 134 ? 0.3317 0.3426 0.3568 0.0350  0.0352  0.0457  136 TYR A CE2 
1115 C CZ  . TYR A 134 ? 0.3144 0.3302 0.3424 0.0323  0.0352  0.0438  136 TYR A CZ  
1116 O OH  . TYR A 134 ? 0.3432 0.3552 0.3758 0.0323  0.0405  0.0477  136 TYR A OH  
1117 N N   . MET A 135 ? 0.2442 0.2907 0.2500 0.0302  0.0141  0.0270  137 MET A N   
1118 C CA  . MET A 135 ? 0.2578 0.3067 0.2610 0.0274  0.0104  0.0213  137 MET A CA  
1119 C C   . MET A 135 ? 0.2394 0.3008 0.2415 0.0246  0.0093  0.0179  137 MET A C   
1120 O O   . MET A 135 ? 0.2350 0.2941 0.2369 0.0210  0.0069  0.0113  137 MET A O   
1121 C CB  . MET A 135 ? 0.2552 0.3076 0.2554 0.0297  0.0104  0.0243  137 MET A CB  
1122 C CG  . MET A 135 ? 0.2800 0.3187 0.2803 0.0312  0.0106  0.0248  137 MET A CG  
1123 S SD  . MET A 135 ? 0.3762 0.4051 0.3754 0.0269  0.0064  0.0166  137 MET A SD  
1124 C CE  . MET A 135 ? 0.5261 0.5683 0.5223 0.0248  0.0046  0.0143  137 MET A CE  
1125 N N   . TYR A 136 ? 0.1984 0.2729 0.1996 0.0264  0.0115  0.0223  138 TYR A N   
1126 C CA  . TYR A 136 ? 0.2041 0.2913 0.2038 0.0236  0.0109  0.0186  138 TYR A CA  
1127 C C   . TYR A 136 ? 0.2014 0.2825 0.2041 0.0209  0.0109  0.0137  138 TYR A C   
1128 O O   . TYR A 136 ? 0.2229 0.3066 0.2250 0.0172  0.0094  0.0070  138 TYR A O   
1129 C CB  . TYR A 136 ? 0.2387 0.3418 0.2366 0.0266  0.0133  0.0251  138 TYR A CB  
1130 C CG  . TYR A 136 ? 0.2540 0.3738 0.2490 0.0236  0.0124  0.0211  138 TYR A CG  
1131 C CD1 . TYR A 136 ? 0.2778 0.4074 0.2700 0.0216  0.0103  0.0180  138 TYR A CD1 
1132 C CD2 . TYR A 136 ? 0.2472 0.3733 0.2421 0.0225  0.0140  0.0200  138 TYR A CD2 
1133 C CE1 . TYR A 136 ? 0.2702 0.4154 0.2597 0.0181  0.0096  0.0134  138 TYR A CE1 
1134 C CE2 . TYR A 136 ? 0.3305 0.4723 0.3223 0.0194  0.0134  0.0155  138 TYR A CE2 
1135 C CZ  . TYR A 136 ? 0.2936 0.4449 0.2826 0.0170  0.0112  0.0120  138 TYR A CZ  
1136 O OH  . TYR A 136 ? 0.3596 0.5268 0.3454 0.0131  0.0107  0.0066  138 TYR A OH  
1137 N N   . GLU A 137 ? 0.2044 0.2769 0.2105 0.0225  0.0127  0.0168  139 GLU A N   
1138 C CA  . GLU A 137 ? 0.2331 0.3004 0.2429 0.0202  0.0128  0.0125  139 GLU A CA  
1139 C C   . GLU A 137 ? 0.2313 0.2878 0.2426 0.0175  0.0096  0.0058  139 GLU A C   
1140 O O   . GLU A 137 ? 0.2007 0.2572 0.2138 0.0151  0.0089  0.0005  139 GLU A O   
1141 C CB  . GLU A 137 ? 0.2547 0.3156 0.2685 0.0221  0.0157  0.0174  139 GLU A CB  
1142 C CG  . GLU A 137 ? 0.2666 0.3380 0.2793 0.0250  0.0197  0.0247  139 GLU A CG  
1143 C CD  . GLU A 137 ? 0.3174 0.4020 0.3285 0.0234  0.0203  0.0224  139 GLU A CD  
1144 O OE1 . GLU A 137 ? 0.3431 0.4250 0.3570 0.0205  0.0197  0.0167  139 GLU A OE1 
1145 O OE2 . GLU A 137 ? 0.3530 0.4516 0.3601 0.0250  0.0215  0.0261  139 GLU A OE2 
1146 N N   . ILE A 138 ? 0.2119 0.2596 0.2224 0.0183  0.0079  0.0062  140 ILE A N   
1147 C CA  . ILE A 138 ? 0.2006 0.2393 0.2116 0.0162  0.0048  0.0006  140 ILE A CA  
1148 C C   . ILE A 138 ? 0.2575 0.3022 0.2658 0.0137  0.0037  -0.0042 140 ILE A C   
1149 O O   . ILE A 138 ? 0.2112 0.2517 0.2209 0.0117  0.0025  -0.0094 140 ILE A O   
1150 C CB  . ILE A 138 ? 0.2417 0.2706 0.2515 0.0175  0.0035  0.0022  140 ILE A CB  
1151 C CG1 . ILE A 138 ? 0.2607 0.2821 0.2736 0.0191  0.0050  0.0054  140 ILE A CG1 
1152 C CG2 . ILE A 138 ? 0.2649 0.2859 0.2742 0.0158  0.0004  -0.0030 140 ILE A CG2 
1153 C CD1 . ILE A 138 ? 0.2932 0.3066 0.3041 0.0207  0.0048  0.0076  140 ILE A CD1 
1154 N N   . LEU A 139 ? 0.2259 0.2805 0.2304 0.0139  0.0042  -0.0025 141 LEU A N   
1155 C CA  . LEU A 139 ? 0.2440 0.3051 0.2461 0.0107  0.0035  -0.0077 141 LEU A CA  
1156 C C   . LEU A 139 ? 0.2087 0.2751 0.2121 0.0083  0.0047  -0.0122 141 LEU A C   
1157 O O   . LEU A 139 ? 0.2346 0.2995 0.2379 0.0052  0.0044  -0.0184 141 LEU A O   
1158 C CB  . LEU A 139 ? 0.2108 0.2846 0.2094 0.0111  0.0039  -0.0048 141 LEU A CB  
1159 C CG  . LEU A 139 ? 0.2401 0.3090 0.2372 0.0125  0.0028  -0.0024 141 LEU A CG  
1160 C CD1 . LEU A 139 ? 0.2413 0.3248 0.2360 0.0141  0.0036  0.0020  141 LEU A CD1 
1161 C CD2 . LEU A 139 ? 0.2343 0.2964 0.2306 0.0092  0.0012  -0.0082 141 LEU A CD2 
1162 N N   . LYS A 140 ? 0.2123 0.2849 0.2170 0.0097  0.0067  -0.0092 142 LYS A N   
1163 C CA  . LYS A 140 ? 0.2336 0.3109 0.2395 0.0076  0.0082  -0.0137 142 LYS A CA  
1164 C C   . LYS A 140 ? 0.2198 0.2848 0.2298 0.0067  0.0075  -0.0183 142 LYS A C   
1165 O O   . LYS A 140 ? 0.2347 0.3003 0.2451 0.0041  0.0082  -0.0244 142 LYS A O   
1166 C CB  . LYS A 140 ? 0.2751 0.3595 0.2820 0.0097  0.0107  -0.0088 142 LYS A CB  
1167 C CG  . LYS A 140 ? 0.2678 0.3677 0.2705 0.0108  0.0119  -0.0045 142 LYS A CG  
1168 C CD  . LYS A 140 ? 0.3477 0.4529 0.3516 0.0131  0.0149  0.0007  142 LYS A CD  
1169 C CE  . LYS A 140 ? 0.4733 0.5933 0.4732 0.0157  0.0164  0.0074  142 LYS A CE  
1170 N NZ  . LYS A 140 ? 0.5080 0.6305 0.5094 0.0186  0.0198  0.0138  142 LYS A NZ  
1171 N N   . ALA A 141 ? 0.2108 0.2650 0.2239 0.0087  0.0062  -0.0156 143 ALA A N   
1172 C CA  . ALA A 141 ? 0.2160 0.2602 0.2334 0.0084  0.0051  -0.0192 143 ALA A CA  
1173 C C   . ALA A 141 ? 0.2132 0.2513 0.2290 0.0070  0.0035  -0.0234 143 ALA A C   
1174 O O   . ALA A 141 ? 0.1992 0.2335 0.2172 0.0060  0.0039  -0.0280 143 ALA A O   
1175 C CB  . ALA A 141 ? 0.1971 0.2329 0.2179 0.0105  0.0038  -0.0156 143 ALA A CB  
1176 N N   . LEU A 142 ? 0.2165 0.2532 0.2284 0.0070  0.0022  -0.0216 144 LEU A N   
1177 C CA  . LEU A 142 ? 0.2119 0.2423 0.2222 0.0055  0.0011  -0.0250 144 LEU A CA  
1178 C C   . LEU A 142 ? 0.1980 0.2345 0.2065 0.0021  0.0030  -0.0304 144 LEU A C   
1179 O O   . LEU A 142 ? 0.2105 0.2404 0.2201 0.0006  0.0036  -0.0348 144 LEU A O   
1180 C CB  . LEU A 142 ? 0.1944 0.2224 0.2013 0.0065  -0.0005 -0.0215 144 LEU A CB  
1181 C CG  . LEU A 142 ? 0.2260 0.2448 0.2340 0.0092  -0.0024 -0.0180 144 LEU A CG  
1182 C CD1 . LEU A 142 ? 0.2334 0.2507 0.2376 0.0100  -0.0033 -0.0150 144 LEU A CD1 
1183 C CD2 . LEU A 142 ? 0.1995 0.2085 0.2102 0.0095  -0.0040 -0.0205 144 LEU A CD2 
1184 N N   . ASP A 143 ? 0.1967 0.2461 0.2027 0.0006  0.0043  -0.0303 145 ASP A N   
1185 C CA  . ASP A 143 ? 0.2441 0.2999 0.2487 -0.0035 0.0063  -0.0367 145 ASP A CA  
1186 C C   . ASP A 143 ? 0.2339 0.2865 0.2418 -0.0041 0.0084  -0.0413 145 ASP A C   
1187 O O   . ASP A 143 ? 0.2451 0.2940 0.2535 -0.0069 0.0102  -0.0475 145 ASP A O   
1188 C CB  . ASP A 143 ? 0.2758 0.3482 0.2768 -0.0050 0.0072  -0.0361 145 ASP A CB  
1189 C CG  . ASP A 143 ? 0.3665 0.4459 0.3659 -0.0102 0.0093  -0.0440 145 ASP A CG  
1190 O OD1 . ASP A 143 ? 0.2900 0.3633 0.2891 -0.0131 0.0095  -0.0483 145 ASP A OD1 
1191 O OD2 . ASP A 143 ? 0.3896 0.4799 0.3881 -0.0114 0.0110  -0.0462 145 ASP A OD2 
1192 N N   . TYR A 144 ? 0.2078 0.2612 0.2186 -0.0014 0.0086  -0.0384 146 TYR A N   
1193 C CA  . TYR A 144 ? 0.2233 0.2742 0.2379 -0.0016 0.0108  -0.0425 146 TYR A CA  
1194 C C   . TYR A 144 ? 0.1990 0.2360 0.2170 -0.0007 0.0102  -0.0448 146 TYR A C   
1195 O O   . TYR A 144 ? 0.2286 0.2623 0.2478 -0.0025 0.0127  -0.0505 146 TYR A O   
1196 C CB  . TYR A 144 ? 0.2125 0.2667 0.2304 0.0010  0.0112  -0.0386 146 TYR A CB  
1197 C CG  . TYR A 144 ? 0.2147 0.2690 0.2364 0.0007  0.0140  -0.0431 146 TYR A CG  
1198 C CD1 . TYR A 144 ? 0.2783 0.3422 0.2976 -0.0020 0.0171  -0.0479 146 TYR A CD1 
1199 C CD2 . TYR A 144 ? 0.2257 0.2713 0.2535 0.0031  0.0136  -0.0430 146 TYR A CD2 
1200 C CE1 . TYR A 144 ? 0.3068 0.3707 0.3295 -0.0022 0.0202  -0.0524 146 TYR A CE1 
1201 C CE2 . TYR A 144 ? 0.2163 0.2625 0.2481 0.0032  0.0165  -0.0470 146 TYR A CE2 
1202 C CZ  . TYR A 144 ? 0.2720 0.3268 0.3012 0.0006  0.0200  -0.0517 146 TYR A CZ  
1203 O OH  . TYR A 144 ? 0.2905 0.3457 0.3237 0.0009  0.0234  -0.0560 146 TYR A OH  
1204 N N   . CYS A 145 ? 0.2175 0.2463 0.2371 0.0021  0.0073  -0.0403 147 CYS A N   
1205 C CA  . CYS A 145 ? 0.2323 0.2494 0.2551 0.0037  0.0068  -0.0418 147 CYS A CA  
1206 C C   . CYS A 145 ? 0.2372 0.2487 0.2573 0.0014  0.0077  -0.0452 147 CYS A C   
1207 O O   . CYS A 145 ? 0.2222 0.2265 0.2448 0.0016  0.0098  -0.0487 147 CYS A O   
1208 C CB  . CYS A 145 ? 0.2398 0.2509 0.2647 0.0070  0.0032  -0.0367 147 CYS A CB  
1209 S SG  . CYS A 145 ? 0.2694 0.2768 0.2895 0.0074  0.0001  -0.0324 147 CYS A SG  
1210 N N   . HIS A 146 ? 0.2309 0.2457 0.2462 -0.0006 0.0069  -0.0443 148 HIS A N   
1211 C CA  . HIS A 146 ? 0.2156 0.2262 0.2285 -0.0037 0.0085  -0.0480 148 HIS A CA  
1212 C C   . HIS A 146 ? 0.2081 0.2222 0.2216 -0.0074 0.0127  -0.0552 148 HIS A C   
1213 O O   . HIS A 146 ? 0.2177 0.2230 0.2323 -0.0088 0.0154  -0.0592 148 HIS A O   
1214 C CB  . HIS A 146 ? 0.2018 0.2179 0.2101 -0.0055 0.0071  -0.0459 148 HIS A CB  
1215 C CG  . HIS A 146 ? 0.1940 0.2055 0.2013 -0.0021 0.0037  -0.0396 148 HIS A CG  
1216 N ND1 . HIS A 146 ? 0.1944 0.2113 0.1982 -0.0024 0.0024  -0.0364 148 HIS A ND1 
1217 C CD2 . HIS A 146 ? 0.2130 0.2155 0.2223 0.0016  0.0016  -0.0364 148 HIS A CD2 
1218 C CE1 . HIS A 146 ? 0.2134 0.2238 0.2170 0.0009  -0.0001 -0.0318 148 HIS A CE1 
1219 N NE2 . HIS A 146 ? 0.2088 0.2109 0.2155 0.0031  -0.0008 -0.0318 148 HIS A NE2 
1220 N N   . SER A 147 ? 0.2351 0.2618 0.2475 -0.0091 0.0137  -0.0569 149 SER A N   
1221 C CA  . SER A 147 ? 0.1913 0.2225 0.2036 -0.0131 0.0178  -0.0645 149 SER A CA  
1222 C C   . SER A 147 ? 0.2403 0.2626 0.2576 -0.0111 0.0206  -0.0674 149 SER A C   
1223 O O   . SER A 147 ? 0.2481 0.2687 0.2660 -0.0142 0.0248  -0.0744 149 SER A O   
1224 C CB  . SER A 147 ? 0.2219 0.2698 0.2316 -0.0146 0.0180  -0.0647 149 SER A CB  
1225 O OG  . SER A 147 ? 0.2517 0.3013 0.2644 -0.0111 0.0180  -0.0619 149 SER A OG  
1226 N N   . MET A 148 ? 0.2355 0.2523 0.2566 -0.0061 0.0184  -0.0622 150 MET A N   
1227 C CA  . MET A 148 ? 0.2667 0.2757 0.2935 -0.0031 0.0204  -0.0636 150 MET A CA  
1228 C C   . MET A 148 ? 0.2573 0.2521 0.2861 -0.0007 0.0200  -0.0621 150 MET A C   
1229 O O   . MET A 148 ? 0.2727 0.2608 0.3066 0.0030  0.0208  -0.0615 150 MET A O   
1230 C CB  . MET A 148 ? 0.2373 0.2508 0.2677 0.0006  0.0183  -0.0590 150 MET A CB  
1231 C CG  . MET A 148 ? 0.2564 0.2834 0.2850 -0.0014 0.0196  -0.0601 150 MET A CG  
1232 S SD  . MET A 148 ? 0.2956 0.3257 0.3260 -0.0034 0.0256  -0.0684 150 MET A SD  
1233 C CE  . MET A 148 ? 0.2753 0.2996 0.3144 0.0021  0.0256  -0.0655 150 MET A CE  
1234 N N   . GLY A 149 ? 0.2438 0.2347 0.2687 -0.0026 0.0189  -0.0612 151 GLY A N   
1235 C CA  . GLY A 149 ? 0.2672 0.2448 0.2933 -0.0005 0.0192  -0.0598 151 GLY A CA  
1236 C C   . GLY A 149 ? 0.2602 0.2331 0.2874 0.0045  0.0146  -0.0528 151 GLY A C   
1237 O O   . GLY A 149 ? 0.2488 0.2115 0.2779 0.0075  0.0150  -0.0510 151 GLY A O   
1238 N N   . ILE A 150 ? 0.2403 0.2204 0.2663 0.0054  0.0106  -0.0487 152 ILE A N   
1239 C CA  . ILE A 150 ? 0.2509 0.2279 0.2784 0.0097  0.0063  -0.0430 152 ILE A CA  
1240 C C   . ILE A 150 ? 0.2422 0.2211 0.2645 0.0088  0.0030  -0.0394 152 ILE A C   
1241 O O   . ILE A 150 ? 0.2449 0.2321 0.2645 0.0062  0.0031  -0.0397 152 ILE A O   
1242 C CB  . ILE A 150 ? 0.2402 0.2228 0.2727 0.0120  0.0052  -0.0419 152 ILE A CB  
1243 C CG1 . ILE A 150 ? 0.2195 0.1987 0.2576 0.0139  0.0085  -0.0449 152 ILE A CG1 
1244 C CG2 . ILE A 150 ? 0.2354 0.2176 0.2688 0.0149  0.0004  -0.0367 152 ILE A CG2 
1245 C CD1 . ILE A 150 ? 0.3270 0.3140 0.3701 0.0146  0.0095  -0.0460 152 ILE A CD1 
1246 N N   . MET A 151 ? 0.2272 0.1992 0.2481 0.0111  0.0004  -0.0358 153 MET A N   
1247 C CA  . MET A 151 ? 0.2380 0.2115 0.2547 0.0111  -0.0027 -0.0322 153 MET A CA  
1248 C C   . MET A 151 ? 0.2081 0.1819 0.2271 0.0142  -0.0064 -0.0288 153 MET A C   
1249 O O   . MET A 151 ? 0.2257 0.1961 0.2484 0.0170  -0.0075 -0.0281 153 MET A O   
1250 C CB  . MET A 151 ? 0.3549 0.3213 0.3671 0.0107  -0.0028 -0.0310 153 MET A CB  
1251 C CG  . MET A 151 ? 0.3595 0.3163 0.3731 0.0132  -0.0021 -0.0305 153 MET A CG  
1252 S SD  . MET A 151 ? 0.3389 0.2876 0.3470 0.0117  -0.0004 -0.0295 153 MET A SD  
1253 C CE  . MET A 151 ? 0.3583 0.2964 0.3700 0.0155  0.0016  -0.0286 153 MET A CE  
1254 N N   . HIS A 152 ? 0.2313 0.2098 0.2484 0.0136  -0.0080 -0.0267 154 HIS A N   
1255 C CA  . HIS A 152 ? 0.1917 0.1711 0.2114 0.0154  -0.0108 -0.0244 154 HIS A CA  
1256 C C   . HIS A 152 ? 0.2177 0.1909 0.2350 0.0174  -0.0140 -0.0221 154 HIS A C   
1257 O O   . HIS A 152 ? 0.2321 0.2043 0.2528 0.0195  -0.0163 -0.0215 154 HIS A O   
1258 C CB  . HIS A 152 ? 0.2073 0.1927 0.2260 0.0142  -0.0104 -0.0228 154 HIS A CB  
1259 C CG  . HIS A 152 ? 0.2056 0.1915 0.2277 0.0152  -0.0123 -0.0211 154 HIS A CG  
1260 N ND1 . HIS A 152 ? 0.2320 0.2137 0.2522 0.0161  -0.0149 -0.0194 154 HIS A ND1 
1261 C CD2 . HIS A 152 ? 0.2269 0.2173 0.2543 0.0151  -0.0115 -0.0213 154 HIS A CD2 
1262 C CE1 . HIS A 152 ? 0.2335 0.2169 0.2579 0.0160  -0.0158 -0.0191 154 HIS A CE1 
1263 N NE2 . HIS A 152 ? 0.2006 0.1892 0.2296 0.0155  -0.0137 -0.0199 154 HIS A NE2 
1264 N N   . ARG A 153 ? 0.2177 0.1878 0.2292 0.0167  -0.0142 -0.0209 155 ARG A N   
1265 C CA  . ARG A 153 ? 0.2456 0.2098 0.2533 0.0184  -0.0166 -0.0189 155 ARG A CA  
1266 C C   . ARG A 153 ? 0.2552 0.2200 0.2626 0.0192  -0.0196 -0.0175 155 ARG A C   
1267 O O   . ARG A 153 ? 0.2543 0.2153 0.2586 0.0206  -0.0221 -0.0162 155 ARG A O   
1268 C CB  . ARG A 153 ? 0.2526 0.2119 0.2619 0.0208  -0.0172 -0.0187 155 ARG A CB  
1269 C CG  . ARG A 153 ? 0.2196 0.1762 0.2293 0.0197  -0.0134 -0.0206 155 ARG A CG  
1270 C CD  . ARG A 153 ? 0.2164 0.1654 0.2255 0.0224  -0.0131 -0.0191 155 ARG A CD  
1271 N NE  . ARG A 153 ? 0.2327 0.1824 0.2466 0.0261  -0.0154 -0.0178 155 ARG A NE  
1272 C CZ  . ARG A 153 ? 0.2823 0.2270 0.2968 0.0298  -0.0157 -0.0154 155 ARG A CZ  
1273 N NH1 . ARG A 153 ? 0.2749 0.2121 0.2853 0.0300  -0.0134 -0.0140 155 ARG A NH1 
1274 N NH2 . ARG A 153 ? 0.2560 0.2036 0.2755 0.0333  -0.0180 -0.0141 155 ARG A NH2 
1275 N N   . ASP A 154 ? 0.2277 0.1971 0.2379 0.0182  -0.0192 -0.0177 156 ASP A N   
1276 C CA  . ASP A 154 ? 0.1825 0.1514 0.1923 0.0182  -0.0212 -0.0169 156 ASP A CA  
1277 C C   . ASP A 154 ? 0.2175 0.1897 0.2280 0.0168  -0.0187 -0.0162 156 ASP A C   
1278 O O   . ASP A 154 ? 0.2292 0.2027 0.2431 0.0162  -0.0187 -0.0162 156 ASP A O   
1279 C CB  . ASP A 154 ? 0.2080 0.1784 0.2230 0.0190  -0.0239 -0.0179 156 ASP A CB  
1280 C CG  . ASP A 154 ? 0.2687 0.2377 0.2822 0.0186  -0.0265 -0.0181 156 ASP A CG  
1281 O OD1 . ASP A 154 ? 0.2742 0.2393 0.2816 0.0184  -0.0266 -0.0174 156 ASP A OD1 
1282 O OD2 . ASP A 154 ? 0.3097 0.2818 0.3283 0.0182  -0.0284 -0.0193 156 ASP A OD2 
1283 N N   . VAL A 155 ? 0.2115 0.1852 0.2186 0.0162  -0.0163 -0.0152 157 VAL A N   
1284 C CA  . VAL A 155 ? 0.1985 0.1759 0.2058 0.0158  -0.0138 -0.0133 157 VAL A CA  
1285 C C   . VAL A 155 ? 0.2522 0.2250 0.2566 0.0163  -0.0142 -0.0118 157 VAL A C   
1286 O O   . VAL A 155 ? 0.2436 0.2126 0.2432 0.0169  -0.0150 -0.0116 157 VAL A O   
1287 C CB  . VAL A 155 ? 0.2207 0.2031 0.2254 0.0152  -0.0115 -0.0126 157 VAL A CB  
1288 C CG1 . VAL A 155 ? 0.2377 0.2246 0.2421 0.0157  -0.0091 -0.0095 157 VAL A CG1 
1289 C CG2 . VAL A 155 ? 0.2624 0.2493 0.2701 0.0141  -0.0106 -0.0151 157 VAL A CG2 
1290 N N   . LYS A 156 ? 0.2169 0.1898 0.2245 0.0161  -0.0130 -0.0111 158 LYS A N   
1291 C CA  . LYS A 156 ? 0.2314 0.1993 0.2371 0.0163  -0.0123 -0.0102 158 LYS A CA  
1292 C C   . LYS A 156 ? 0.2346 0.2035 0.2450 0.0158  -0.0094 -0.0089 158 LYS A C   
1293 O O   . LYS A 156 ? 0.2165 0.1899 0.2317 0.0150  -0.0090 -0.0092 158 LYS A O   
1294 C CB  . LYS A 156 ? 0.2341 0.1968 0.2384 0.0158  -0.0158 -0.0130 158 LYS A CB  
1295 C CG  . LYS A 156 ? 0.2323 0.1969 0.2423 0.0146  -0.0180 -0.0154 158 LYS A CG  
1296 C CD  . LYS A 156 ? 0.2620 0.2239 0.2703 0.0143  -0.0220 -0.0179 158 LYS A CD  
1297 C CE  . LYS A 156 ? 0.3236 0.2895 0.3385 0.0132  -0.0243 -0.0202 158 LYS A CE  
1298 N NZ  . LYS A 156 ? 0.4396 0.4049 0.4526 0.0130  -0.0285 -0.0224 158 LYS A NZ  
1299 N N   . PRO A 157 ? 0.2431 0.2075 0.2524 0.0162  -0.0069 -0.0074 159 PRO A N   
1300 C CA  . PRO A 157 ? 0.2423 0.2068 0.2562 0.0158  -0.0031 -0.0053 159 PRO A CA  
1301 C C   . PRO A 157 ? 0.2337 0.1983 0.2537 0.0133  -0.0042 -0.0082 159 PRO A C   
1302 O O   . PRO A 157 ? 0.2600 0.2281 0.2848 0.0128  -0.0015 -0.0064 159 PRO A O   
1303 C CB  . PRO A 157 ? 0.3053 0.2624 0.3167 0.0167  -0.0003 -0.0041 159 PRO A CB  
1304 C CG  . PRO A 157 ? 0.2821 0.2388 0.2871 0.0186  -0.0015 -0.0035 159 PRO A CG  
1305 C CD  . PRO A 157 ? 0.2450 0.2043 0.2487 0.0175  -0.0063 -0.0066 159 PRO A CD  
1306 N N   . HIS A 158 ? 0.2251 0.1872 0.2454 0.0116  -0.0080 -0.0123 160 HIS A N   
1307 C CA  . HIS A 158 ? 0.2576 0.2215 0.2843 0.0090  -0.0094 -0.0154 160 HIS A CA  
1308 C C   . HIS A 158 ? 0.2793 0.2505 0.3104 0.0093  -0.0104 -0.0152 160 HIS A C   
1309 O O   . HIS A 158 ? 0.2951 0.2693 0.3328 0.0075  -0.0105 -0.0168 160 HIS A O   
1310 C CB  . HIS A 158 ? 0.3321 0.2939 0.3573 0.0077  -0.0140 -0.0195 160 HIS A CB  
1311 C CG  . HIS A 158 ? 0.6981 0.6533 0.7221 0.0056  -0.0126 -0.0218 160 HIS A CG  
1312 N ND1 . HIS A 158 ? 0.7796 0.7305 0.7972 0.0059  -0.0147 -0.0237 160 HIS A ND1 
1313 C CD2 . HIS A 158 ? 0.7929 0.7448 0.8213 0.0030  -0.0090 -0.0227 160 HIS A CD2 
1314 C CE1 . HIS A 158 ? 0.8300 0.7753 0.8479 0.0034  -0.0124 -0.0262 160 HIS A CE1 
1315 N NE2 . HIS A 158 ? 0.8062 0.7515 0.8309 0.0015  -0.0088 -0.0257 160 HIS A NE2 
1316 N N   . ASN A 159 ? 0.2388 0.2132 0.2666 0.0114  -0.0108 -0.0138 161 ASN A N   
1317 C CA  . ASN A 159 ? 0.2017 0.1825 0.2333 0.0116  -0.0112 -0.0143 161 ASN A CA  
1318 C C   . ASN A 159 ? 0.1898 0.1754 0.2219 0.0122  -0.0072 -0.0113 161 ASN A C   
1319 O O   . ASN A 159 ? 0.2282 0.2193 0.2617 0.0125  -0.0069 -0.0119 161 ASN A O   
1320 C CB  . ASN A 159 ? 0.2344 0.2154 0.2628 0.0130  -0.0142 -0.0157 161 ASN A CB  
1321 C CG  . ASN A 159 ? 0.2640 0.2431 0.2935 0.0129  -0.0184 -0.0182 161 ASN A CG  
1322 O OD1 . ASN A 159 ? 0.2716 0.2517 0.3060 0.0114  -0.0194 -0.0198 161 ASN A OD1 
1323 N ND2 . ASN A 159 ? 0.2261 0.2032 0.2514 0.0145  -0.0207 -0.0185 161 ASN A ND2 
1324 N N   . VAL A 160 ? 0.2390 0.2229 0.2698 0.0125  -0.0038 -0.0080 162 VAL A N   
1325 C CA  . VAL A 160 ? 0.2378 0.2273 0.2688 0.0135  0.0002  -0.0043 162 VAL A CA  
1326 C C   . VAL A 160 ? 0.2751 0.2627 0.3113 0.0124  0.0037  -0.0025 162 VAL A C   
1327 O O   . VAL A 160 ? 0.3485 0.3299 0.3839 0.0126  0.0059  -0.0006 162 VAL A O   
1328 C CB  . VAL A 160 ? 0.2606 0.2508 0.2857 0.0157  0.0018  -0.0007 162 VAL A CB  
1329 C CG1 . VAL A 160 ? 0.2994 0.2973 0.3246 0.0170  0.0056  0.0036  162 VAL A CG1 
1330 C CG2 . VAL A 160 ? 0.3249 0.3165 0.3454 0.0160  -0.0014 -0.0030 162 VAL A CG2 
1331 N N   . MET A 161 ? 0.2623 0.2547 0.3041 0.0111  0.0046  -0.0032 163 MET A N   
1332 C CA  . MET A 161 ? 0.2765 0.2674 0.3240 0.0095  0.0084  -0.0016 163 MET A CA  
1333 C C   . MET A 161 ? 0.2857 0.2806 0.3319 0.0115  0.0135  0.0043  163 MET A C   
1334 O O   . MET A 161 ? 0.3154 0.3187 0.3603 0.0126  0.0139  0.0054  163 MET A O   
1335 C CB  . MET A 161 ? 0.2864 0.2815 0.3412 0.0073  0.0073  -0.0049 163 MET A CB  
1336 C CG  . MET A 161 ? 0.3686 0.3611 0.4257 0.0055  0.0024  -0.0101 163 MET A CG  
1337 S SD  . MET A 161 ? 0.3999 0.3838 0.4591 0.0026  0.0031  -0.0116 163 MET A SD  
1338 C CE  . MET A 161 ? 0.4852 0.4647 0.5378 0.0034  -0.0025 -0.0148 163 MET A CE  
1339 N N   . ILE A 162 ? 0.2742 0.2633 0.3209 0.0119  0.0177  0.0082  164 ILE A N   
1340 C CA  . ILE A 162 ? 0.2651 0.2577 0.3105 0.0146  0.0230  0.0151  164 ILE A CA  
1341 C C   . ILE A 162 ? 0.3268 0.3154 0.3785 0.0130  0.0283  0.0176  164 ILE A C   
1342 O O   . ILE A 162 ? 0.3591 0.3379 0.4136 0.0111  0.0298  0.0162  164 ILE A O   
1343 C CB  . ILE A 162 ? 0.2530 0.2424 0.2925 0.0181  0.0242  0.0192  164 ILE A CB  
1344 C CG1 . ILE A 162 ? 0.2907 0.2850 0.3245 0.0192  0.0194  0.0167  164 ILE A CG1 
1345 C CG2 . ILE A 162 ? 0.3026 0.2963 0.3413 0.0215  0.0300  0.0273  164 ILE A CG2 
1346 C CD1 . ILE A 162 ? 0.3162 0.3074 0.3448 0.0222  0.0199  0.0197  164 ILE A CD1 
1347 N N   . ASP A 163 ? 0.3118 0.3079 0.3657 0.0135  0.0316  0.0210  165 ASP A N   
1348 C CA  . ASP A 163 ? 0.3799 0.3729 0.4389 0.0128  0.0381  0.0255  165 ASP A CA  
1349 C C   . ASP A 163 ? 0.3611 0.3557 0.4155 0.0177  0.0429  0.0342  165 ASP A C   
1350 O O   . ASP A 163 ? 0.3731 0.3782 0.4247 0.0202  0.0441  0.0384  165 ASP A O   
1351 C CB  . ASP A 163 ? 0.3782 0.3791 0.4423 0.0107  0.0390  0.0245  165 ASP A CB  
1352 C CG  . ASP A 163 ? 0.4378 0.4363 0.5070 0.0101  0.0465  0.0299  165 ASP A CG  
1353 O OD1 . ASP A 163 ? 0.4323 0.4227 0.5011 0.0115  0.0513  0.0349  165 ASP A OD1 
1354 O OD2 . ASP A 163 ? 0.3899 0.3945 0.4640 0.0081  0.0480  0.0292  165 ASP A OD2 
1355 N N   . HIS A 164 ? 0.3346 0.3189 0.3881 0.0191  0.0458  0.0369  166 HIS A N   
1356 C CA  . HIS A 164 ? 0.3554 0.3413 0.4042 0.0247  0.0497  0.0454  166 HIS A CA  
1357 C C   . HIS A 164 ? 0.4521 0.4419 0.5031 0.0268  0.0566  0.0535  166 HIS A C   
1358 O O   . HIS A 164 ? 0.4566 0.4547 0.5032 0.0318  0.0587  0.0609  166 HIS A O   
1359 C CB  . HIS A 164 ? 0.3323 0.3050 0.3806 0.0259  0.0521  0.0461  166 HIS A CB  
1360 C CG  . HIS A 164 ? 0.3920 0.3672 0.4353 0.0322  0.0550  0.0541  166 HIS A CG  
1361 N ND1 . HIS A 164 ? 0.4091 0.3969 0.4465 0.0354  0.0510  0.0557  166 HIS A ND1 
1362 C CD2 . HIS A 164 ? 0.4169 0.3837 0.4606 0.0361  0.0616  0.0609  166 HIS A CD2 
1363 C CE1 . HIS A 164 ? 0.4760 0.4646 0.5105 0.0411  0.0546  0.0633  166 HIS A CE1 
1364 N NE2 . HIS A 164 ? 0.4860 0.4616 0.5242 0.0420  0.0612  0.0669  166 HIS A NE2 
1365 N N   . GLU A 165 ? 0.4744 0.4596 0.5323 0.0231  0.0601  0.0524  167 GLU A N   
1366 C CA  . GLU A 165 ? 0.5147 0.5029 0.5749 0.0249  0.0673  0.0605  167 GLU A CA  
1367 C C   . GLU A 165 ? 0.4807 0.4858 0.5369 0.0271  0.0655  0.0631  167 GLU A C   
1368 O O   . GLU A 165 ? 0.4960 0.5077 0.5493 0.0316  0.0701  0.0720  167 GLU A O   
1369 C CB  . GLU A 165 ? 0.6405 0.6213 0.7094 0.0193  0.0709  0.0575  167 GLU A CB  
1370 C CG  . GLU A 165 ? 0.7585 0.7429 0.8304 0.0204  0.0782  0.0651  167 GLU A CG  
1371 C CD  . GLU A 165 ? 0.8854 0.8594 0.9667 0.0149  0.0835  0.0631  167 GLU A CD  
1372 O OE1 . GLU A 165 ? 0.8928 0.8563 0.9777 0.0106  0.0817  0.0561  167 GLU A OE1 
1373 O OE2 . GLU A 165 ? 0.9314 0.9081 1.0163 0.0146  0.0896  0.0684  167 GLU A OE2 
1374 N N   . HIS A 166 ? 0.4782 0.4906 0.5338 0.0241  0.0591  0.0553  168 HIS A N   
1375 C CA  . HIS A 166 ? 0.4739 0.5019 0.5256 0.0254  0.0574  0.0559  168 HIS A CA  
1376 C C   . HIS A 166 ? 0.4394 0.4753 0.4839 0.0274  0.0515  0.0534  168 HIS A C   
1377 O O   . HIS A 166 ? 0.4189 0.4673 0.4600 0.0273  0.0492  0.0515  168 HIS A O   
1378 C CB  . HIS A 166 ? 0.5188 0.5502 0.5757 0.0207  0.0556  0.0492  168 HIS A CB  
1379 C CG  . HIS A 166 ? 0.6247 0.6511 0.6891 0.0184  0.0616  0.0517  168 HIS A CG  
1380 N ND1 . HIS A 166 ? 0.6460 0.6616 0.7180 0.0139  0.0617  0.0468  168 HIS A ND1 
1381 C CD2 . HIS A 166 ? 0.6451 0.6762 0.7106 0.0198  0.0682  0.0588  168 HIS A CD2 
1382 C CE1 . HIS A 166 ? 0.6651 0.6787 0.7430 0.0121  0.0680  0.0503  168 HIS A CE1 
1383 N NE2 . HIS A 166 ? 0.6760 0.6984 0.7502 0.0158  0.0723  0.0580  168 HIS A NE2 
1384 N N   . ARG A 167 ? 0.4155 0.4443 0.4576 0.0288  0.0495  0.0532  169 ARG A N   
1385 C CA  . ARG A 167 ? 0.3746 0.4102 0.4103 0.0304  0.0444  0.0509  169 ARG A CA  
1386 C C   . ARG A 167 ? 0.3337 0.3746 0.3690 0.0267  0.0387  0.0420  169 ARG A C   
1387 O O   . ARG A 167 ? 0.3942 0.4463 0.4246 0.0273  0.0361  0.0406  169 ARG A O   
1388 C CB  . ARG A 167 ? 0.4176 0.4661 0.4477 0.0354  0.0466  0.0589  169 ARG A CB  
1389 C CG  . ARG A 167 ? 0.4699 0.5133 0.5006 0.0401  0.0530  0.0689  169 ARG A CG  
1390 C CD  . ARG A 167 ? 0.5534 0.5830 0.5848 0.0408  0.0525  0.0678  169 ARG A CD  
1391 N NE  . ARG A 167 ? 0.6766 0.7040 0.7068 0.0467  0.0579  0.0776  169 ARG A NE  
1392 C CZ  . ARG A 167 ? 0.6943 0.7084 0.7288 0.0480  0.0644  0.0822  169 ARG A CZ  
1393 N NH1 . ARG A 167 ? 0.6004 0.6028 0.6407 0.0430  0.0660  0.0775  169 ARG A NH1 
1394 N NH2 . ARG A 167 ? 0.7346 0.7471 0.7679 0.0542  0.0696  0.0916  169 ARG A NH2 
1395 N N   . LYS A 168 ? 0.3103 0.3431 0.3511 0.0228  0.0370  0.0359  170 LYS A N   
1396 C CA  . LYS A 168 ? 0.3717 0.4078 0.4138 0.0197  0.0325  0.0280  170 LYS A CA  
1397 C C   . LYS A 168 ? 0.3059 0.3339 0.3475 0.0182  0.0273  0.0221  170 LYS A C   
1398 O O   . LYS A 168 ? 0.3551 0.3726 0.3992 0.0174  0.0275  0.0218  170 LYS A O   
1399 C CB  . LYS A 168 ? 0.3597 0.3947 0.4092 0.0169  0.0347  0.0262  170 LYS A CB  
1400 C CG  . LYS A 168 ? 0.4108 0.4474 0.4634 0.0140  0.0306  0.0183  170 LYS A CG  
1401 C CD  . LYS A 168 ? 0.4884 0.5205 0.5498 0.0110  0.0320  0.0163  170 LYS A CD  
1402 C CE  . LYS A 168 ? 0.4784 0.5195 0.5434 0.0100  0.0338  0.0149  170 LYS A CE  
1403 N NZ  . LYS A 168 ? 0.4734 0.5112 0.5478 0.0069  0.0350  0.0126  170 LYS A NZ  
1404 N N   . LEU A 169 ? 0.2732 0.3059 0.3116 0.0176  0.0231  0.0172  171 LEU A N   
1405 C CA  . LEU A 169 ? 0.2429 0.2688 0.2799 0.0167  0.0183  0.0123  171 LEU A CA  
1406 C C   . LEU A 169 ? 0.2636 0.2913 0.3028 0.0146  0.0150  0.0057  171 LEU A C   
1407 O O   . LEU A 169 ? 0.2474 0.2836 0.2856 0.0144  0.0155  0.0043  171 LEU A O   
1408 C CB  . LEU A 169 ? 0.2662 0.2948 0.2964 0.0188  0.0170  0.0141  171 LEU A CB  
1409 C CG  . LEU A 169 ? 0.2646 0.2864 0.2924 0.0182  0.0128  0.0101  171 LEU A CG  
1410 C CD1 . LEU A 169 ? 0.2479 0.2692 0.2707 0.0208  0.0134  0.0142  171 LEU A CD1 
1411 C CD2 . LEU A 169 ? 0.2624 0.2883 0.2887 0.0166  0.0095  0.0045  171 LEU A CD2 
1412 N N   . ARG A 170 ? 0.2306 0.2505 0.2725 0.0132  0.0117  0.0017  172 ARG A N   
1413 C CA  . ARG A 170 ? 0.1968 0.2175 0.2406 0.0121  0.0084  -0.0039 172 ARG A CA  
1414 C C   . ARG A 170 ? 0.2163 0.2300 0.2576 0.0122  0.0042  -0.0067 172 ARG A C   
1415 O O   . ARG A 170 ? 0.2208 0.2276 0.2627 0.0118  0.0030  -0.0063 172 ARG A O   
1416 C CB  . ARG A 170 ? 0.1994 0.2203 0.2513 0.0105  0.0088  -0.0059 172 ARG A CB  
1417 C CG  . ARG A 170 ? 0.2413 0.2694 0.2962 0.0103  0.0133  -0.0036 172 ARG A CG  
1418 C CD  . ARG A 170 ? 0.2798 0.3160 0.3325 0.0108  0.0138  -0.0058 172 ARG A CD  
1419 N NE  . ARG A 170 ? 0.2782 0.3218 0.3337 0.0105  0.0181  -0.0039 172 ARG A NE  
1420 C CZ  . ARG A 170 ? 0.3450 0.3951 0.3965 0.0115  0.0217  0.0006  172 ARG A CZ  
1421 N NH1 . ARG A 170 ? 0.3148 0.3654 0.3597 0.0130  0.0213  0.0037  172 ARG A NH1 
1422 N NH2 . ARG A 170 ? 0.4347 0.4916 0.4890 0.0112  0.0256  0.0023  172 ARG A NH2 
1423 N N   . LEU A 171 ? 0.2043 0.2196 0.2427 0.0124  0.0022  -0.0097 173 LEU A N   
1424 C CA  . LEU A 171 ? 0.1757 0.1848 0.2120 0.0126  -0.0016 -0.0122 173 LEU A CA  
1425 C C   . LEU A 171 ? 0.2211 0.2282 0.2632 0.0123  -0.0039 -0.0154 173 LEU A C   
1426 O O   . LEU A 171 ? 0.2180 0.2294 0.2635 0.0123  -0.0030 -0.0175 173 LEU A O   
1427 C CB  . LEU A 171 ? 0.2373 0.2485 0.2684 0.0128  -0.0020 -0.0139 173 LEU A CB  
1428 C CG  . LEU A 171 ? 0.2655 0.2703 0.2937 0.0131  -0.0051 -0.0159 173 LEU A CG  
1429 C CD1 . LEU A 171 ? 0.2578 0.2567 0.2828 0.0137  -0.0066 -0.0137 173 LEU A CD1 
1430 C CD2 . LEU A 171 ? 0.2755 0.2834 0.2995 0.0124  -0.0042 -0.0177 173 LEU A CD2 
1431 N N   . ILE A 172 ? 0.1941 0.1957 0.2372 0.0121  -0.0066 -0.0159 174 ILE A N   
1432 C CA  . ILE A 172 ? 0.2015 0.2033 0.2508 0.0120  -0.0091 -0.0183 174 ILE A CA  
1433 C C   . ILE A 172 ? 0.2239 0.2213 0.2705 0.0133  -0.0131 -0.0199 174 ILE A C   
1434 O O   . ILE A 172 ? 0.2183 0.2119 0.2584 0.0140  -0.0137 -0.0193 174 ILE A O   
1435 C CB  . ILE A 172 ? 0.2143 0.2154 0.2685 0.0101  -0.0089 -0.0180 174 ILE A CB  
1436 C CG1 . ILE A 172 ? 0.2397 0.2340 0.2892 0.0095  -0.0102 -0.0173 174 ILE A CG1 
1437 C CG2 . ILE A 172 ? 0.2137 0.2187 0.2712 0.0089  -0.0043 -0.0158 174 ILE A CG2 
1438 C CD1 . ILE A 172 ? 0.2454 0.2382 0.2999 0.0071  -0.0112 -0.0190 174 ILE A CD1 
1439 N N   . ASP A 173 ? 0.2338 0.2325 0.2856 0.0138  -0.0158 -0.0216 175 ASP A N   
1440 C CA  . ASP A 173 ? 0.2757 0.2713 0.3258 0.0154  -0.0199 -0.0224 175 ASP A CA  
1441 C C   . ASP A 173 ? 0.2313 0.2240 0.2771 0.0175  -0.0197 -0.0223 175 ASP A C   
1442 O O   . ASP A 173 ? 0.2570 0.2448 0.2961 0.0179  -0.0203 -0.0215 175 ASP A O   
1443 C CB  . ASP A 173 ? 0.2760 0.2670 0.3214 0.0143  -0.0220 -0.0220 175 ASP A CB  
1444 C CG  . ASP A 173 ? 0.4243 0.4144 0.4689 0.0157  -0.0266 -0.0229 175 ASP A CG  
1445 O OD1 . ASP A 173 ? 0.4053 0.3976 0.4524 0.0181  -0.0280 -0.0229 175 ASP A OD1 
1446 O OD2 . ASP A 173 ? 0.4929 0.4805 0.5344 0.0144  -0.0285 -0.0234 175 ASP A OD2 
1447 N N   . TRP A 174 ? 0.2214 0.2172 0.2718 0.0189  -0.0183 -0.0235 176 TRP A N   
1448 C CA  . TRP A 174 ? 0.2446 0.2373 0.2926 0.0207  -0.0171 -0.0241 176 TRP A CA  
1449 C C   . TRP A 174 ? 0.2088 0.1988 0.2580 0.0238  -0.0201 -0.0235 176 TRP A C   
1450 O O   . TRP A 174 ? 0.2472 0.2344 0.2967 0.0259  -0.0185 -0.0240 176 TRP A O   
1451 C CB  . TRP A 174 ? 0.2322 0.2290 0.2841 0.0204  -0.0132 -0.0260 176 TRP A CB  
1452 C CG  . TRP A 174 ? 0.2214 0.2213 0.2704 0.0177  -0.0104 -0.0258 176 TRP A CG  
1453 C CD1 . TRP A 174 ? 0.2113 0.2155 0.2627 0.0162  -0.0096 -0.0246 176 TRP A CD1 
1454 C CD2 . TRP A 174 ? 0.2111 0.2104 0.2541 0.0164  -0.0080 -0.0264 176 TRP A CD2 
1455 N NE1 . TRP A 174 ? 0.1971 0.2037 0.2443 0.0146  -0.0068 -0.0237 176 TRP A NE1 
1456 C CE2 . TRP A 174 ? 0.2066 0.2112 0.2486 0.0146  -0.0061 -0.0250 176 TRP A CE2 
1457 C CE3 . TRP A 174 ? 0.2140 0.2095 0.2527 0.0163  -0.0071 -0.0279 176 TRP A CE3 
1458 C CZ2 . TRP A 174 ? 0.2349 0.2425 0.2716 0.0131  -0.0039 -0.0249 176 TRP A CZ2 
1459 C CZ3 . TRP A 174 ? 0.1992 0.1974 0.2330 0.0140  -0.0049 -0.0287 176 TRP A CZ3 
1460 C CH2 . TRP A 174 ? 0.2418 0.2468 0.2746 0.0127  -0.0035 -0.0271 176 TRP A CH2 
1461 N N   . GLY A 175 ? 0.2142 0.2049 0.2636 0.0242  -0.0241 -0.0225 177 GLY A N   
1462 C CA  . GLY A 175 ? 0.2195 0.2099 0.2702 0.0277  -0.0274 -0.0213 177 GLY A CA  
1463 C C   . GLY A 175 ? 0.2530 0.2361 0.2966 0.0296  -0.0276 -0.0196 177 GLY A C   
1464 O O   . GLY A 175 ? 0.2908 0.2728 0.3353 0.0333  -0.0291 -0.0178 177 GLY A O   
1465 N N   . LEU A 176 ? 0.2305 0.2087 0.2671 0.0273  -0.0260 -0.0196 178 LEU A N   
1466 C CA  . LEU A 176 ? 0.2552 0.2265 0.2854 0.0285  -0.0254 -0.0182 178 LEU A CA  
1467 C C   . LEU A 176 ? 0.2542 0.2222 0.2837 0.0275  -0.0208 -0.0196 178 LEU A C   
1468 O O   . LEU A 176 ? 0.2786 0.2405 0.3036 0.0280  -0.0194 -0.0188 178 LEU A O   
1469 C CB  . LEU A 176 ? 0.2660 0.2345 0.2888 0.0267  -0.0269 -0.0173 178 LEU A CB  
1470 C CG  . LEU A 176 ? 0.3232 0.2933 0.3445 0.0275  -0.0314 -0.0164 178 LEU A CG  
1471 C CD1 . LEU A 176 ? 0.3323 0.2985 0.3457 0.0258  -0.0317 -0.0159 178 LEU A CD1 
1472 C CD2 . LEU A 176 ? 0.3852 0.3551 0.4071 0.0315  -0.0338 -0.0143 178 LEU A CD2 
1473 N N   . ALA A 177 ? 0.2167 0.1889 0.2504 0.0259  -0.0181 -0.0219 179 ALA A N   
1474 C CA  . ALA A 177 ? 0.2201 0.1906 0.2524 0.0241  -0.0137 -0.0242 179 ALA A CA  
1475 C C   . ALA A 177 ? 0.2400 0.2047 0.2740 0.0265  -0.0114 -0.0247 179 ALA A C   
1476 O O   . ALA A 177 ? 0.2442 0.2086 0.2828 0.0303  -0.0126 -0.0232 179 ALA A O   
1477 C CB  . ALA A 177 ? 0.2392 0.2166 0.2753 0.0220  -0.0113 -0.0266 179 ALA A CB  
1478 N N   . GLU A 178 ? 0.2188 0.1792 0.2495 0.0244  -0.0077 -0.0267 180 GLU A N   
1479 C CA  . GLU A 178 ? 0.2502 0.2032 0.2825 0.0263  -0.0043 -0.0274 180 GLU A CA  
1480 C C   . GLU A 178 ? 0.2157 0.1684 0.2478 0.0225  0.0009  -0.0324 180 GLU A C   
1481 O O   . GLU A 178 ? 0.2447 0.2025 0.2735 0.0184  0.0014  -0.0345 180 GLU A O   
1482 C CB  . GLU A 178 ? 0.2761 0.2209 0.3035 0.0276  -0.0048 -0.0244 180 GLU A CB  
1483 C CG  . GLU A 178 ? 0.3502 0.2911 0.3798 0.0333  -0.0067 -0.0201 180 GLU A CG  
1484 C CD  . GLU A 178 ? 0.3907 0.3275 0.4265 0.0367  -0.0028 -0.0207 180 GLU A CD  
1485 O OE1 . GLU A 178 ? 0.4523 0.3853 0.4895 0.0419  -0.0036 -0.0164 180 GLU A OE1 
1486 O OE2 . GLU A 178 ? 0.3807 0.3183 0.4199 0.0347  0.0013  -0.0251 180 GLU A OE2 
1487 N N   . PHE A 179 ? 0.2415 0.1884 0.2772 0.0242  0.0050  -0.0343 181 PHE A N   
1488 C CA  . PHE A 179 ? 0.2520 0.1968 0.2872 0.0202  0.0106  -0.0399 181 PHE A CA  
1489 C C   . PHE A 179 ? 0.2779 0.2154 0.3077 0.0174  0.0125  -0.0402 181 PHE A C   
1490 O O   . PHE A 179 ? 0.2987 0.2278 0.3275 0.0204  0.0123  -0.0364 181 PHE A O   
1491 C CB  . PHE A 179 ? 0.2961 0.2360 0.3374 0.0230  0.0152  -0.0421 181 PHE A CB  
1492 C CG  . PHE A 179 ? 0.2622 0.2099 0.3093 0.0250  0.0145  -0.0429 181 PHE A CG  
1493 C CD1 . PHE A 179 ? 0.2852 0.2353 0.3368 0.0302  0.0107  -0.0382 181 PHE A CD1 
1494 C CD2 . PHE A 179 ? 0.3035 0.2574 0.3516 0.0215  0.0177  -0.0483 181 PHE A CD2 
1495 C CE1 . PHE A 179 ? 0.2748 0.2328 0.3325 0.0318  0.0103  -0.0390 181 PHE A CE1 
1496 C CE2 . PHE A 179 ? 0.2743 0.2358 0.3279 0.0233  0.0175  -0.0488 181 PHE A CE2 
1497 C CZ  . PHE A 179 ? 0.2567 0.2200 0.3155 0.0284  0.0139  -0.0442 181 PHE A CZ  
1498 N N   . TYR A 180 ? 0.2506 0.1923 0.2770 0.0116  0.0145  -0.0446 182 TYR A N   
1499 C CA  . TYR A 180 ? 0.2747 0.2107 0.2969 0.0081  0.0169  -0.0457 182 TYR A CA  
1500 C C   . TYR A 180 ? 0.3001 0.2268 0.3247 0.0065  0.0236  -0.0504 182 TYR A C   
1501 O O   . TYR A 180 ? 0.3067 0.2365 0.3335 0.0036  0.0273  -0.0565 182 TYR A O   
1502 C CB  . TYR A 180 ? 0.2426 0.1884 0.2605 0.0025  0.0161  -0.0483 182 TYR A CB  
1503 C CG  . TYR A 180 ? 0.2712 0.2118 0.2857 -0.0017 0.0191  -0.0501 182 TYR A CG  
1504 C CD1 . TYR A 180 ? 0.2799 0.2141 0.2913 0.0001  0.0173  -0.0451 182 TYR A CD1 
1505 C CD2 . TYR A 180 ? 0.2646 0.2061 0.2793 -0.0075 0.0240  -0.0571 182 TYR A CD2 
1506 C CE1 . TYR A 180 ? 0.2784 0.2075 0.2873 -0.0038 0.0206  -0.0466 182 TYR A CE1 
1507 C CE2 . TYR A 180 ? 0.2891 0.2258 0.3016 -0.0118 0.0272  -0.0592 182 TYR A CE2 
1508 C CZ  . TYR A 180 ? 0.2665 0.1968 0.2762 -0.0099 0.0255  -0.0536 182 TYR A CZ  
1509 O OH  . TYR A 180 ? 0.2970 0.2226 0.3048 -0.0146 0.0291  -0.0556 182 TYR A OH  
1510 N N   . HIS A 181 ? 0.2687 0.1837 0.2926 0.0081  0.0258  -0.0477 183 HIS A N   
1511 C CA  . HIS A 181 ? 0.3139 0.2178 0.3398 0.0063  0.0330  -0.0517 183 HIS A CA  
1512 C C   . HIS A 181 ? 0.3110 0.2090 0.3326 0.0023  0.0350  -0.0515 183 HIS A C   
1513 O O   . HIS A 181 ? 0.3354 0.2303 0.3541 0.0053  0.0319  -0.0450 183 HIS A O   
1514 C CB  . HIS A 181 ? 0.3126 0.2060 0.3432 0.0135  0.0350  -0.0476 183 HIS A CB  
1515 C CG  . HIS A 181 ? 0.3565 0.2553 0.3925 0.0175  0.0339  -0.0480 183 HIS A CG  
1516 N ND1 . HIS A 181 ? 0.3565 0.2547 0.3966 0.0159  0.0393  -0.0546 183 HIS A ND1 
1517 C CD2 . HIS A 181 ? 0.3552 0.2604 0.3936 0.0230  0.0284  -0.0430 183 HIS A CD2 
1518 C CE1 . HIS A 181 ? 0.3636 0.2676 0.4084 0.0205  0.0372  -0.0531 183 HIS A CE1 
1519 N NE2 . HIS A 181 ? 0.3430 0.2515 0.3871 0.0247  0.0305  -0.0461 183 HIS A NE2 
1520 N N   . PRO A 182 ? 0.3047 0.2014 0.3259 -0.0047 0.0403  -0.0586 184 PRO A N   
1521 C CA  . PRO A 182 ? 0.3311 0.2235 0.3487 -0.0093 0.0424  -0.0587 184 PRO A CA  
1522 C C   . PRO A 182 ? 0.3477 0.2249 0.3655 -0.0046 0.0448  -0.0524 184 PRO A C   
1523 O O   . PRO A 182 ? 0.3690 0.2349 0.3908 -0.0010 0.0495  -0.0520 184 PRO A O   
1524 C CB  . PRO A 182 ? 0.3891 0.2812 0.4081 -0.0173 0.0490  -0.0685 184 PRO A CB  
1525 C CG  . PRO A 182 ? 0.4687 0.3711 0.4897 -0.0179 0.0480  -0.0734 184 PRO A CG  
1526 C CD  . PRO A 182 ? 0.3698 0.2705 0.3935 -0.0093 0.0446  -0.0674 184 PRO A CD  
1527 N N   . GLY A 183 ? 0.3711 0.2483 0.3845 -0.0042 0.0418  -0.0470 185 GLY A N   
1528 C CA  . GLY A 183 ? 0.3355 0.1995 0.3477 -0.0001 0.0440  -0.0406 185 GLY A CA  
1529 C C   . GLY A 183 ? 0.3651 0.2277 0.3773 0.0090  0.0392  -0.0322 185 GLY A C   
1530 O O   . GLY A 183 ? 0.3885 0.2418 0.3989 0.0131  0.0403  -0.0257 185 GLY A O   
1531 N N   . GLN A 184 ? 0.3529 0.2249 0.3670 0.0121  0.0341  -0.0321 186 GLN A N   
1532 C CA  . GLN A 184 ? 0.3687 0.2413 0.3833 0.0202  0.0292  -0.0249 186 GLN A CA  
1533 C C   . GLN A 184 ? 0.3691 0.2468 0.3776 0.0211  0.0232  -0.0198 186 GLN A C   
1534 O O   . GLN A 184 ? 0.3436 0.2297 0.3490 0.0166  0.0207  -0.0223 186 GLN A O   
1535 C CB  . GLN A 184 ? 0.3464 0.2281 0.3655 0.0224  0.0260  -0.0270 186 GLN A CB  
1536 C CG  . GLN A 184 ? 0.5113 0.3936 0.5331 0.0306  0.0222  -0.0206 186 GLN A CG  
1537 C CD  . GLN A 184 ? 0.6534 0.5406 0.6820 0.0328  0.0223  -0.0234 186 GLN A CD  
1538 O OE1 . GLN A 184 ? 0.7484 0.6446 0.7787 0.0360  0.0168  -0.0212 186 GLN A OE1 
1539 N NE2 . GLN A 184 ? 0.6148 0.4962 0.6473 0.0309  0.0290  -0.0287 186 GLN A NE2 
1540 N N   . GLU A 185 ? 0.3518 0.2248 0.3586 0.0274  0.0213  -0.0125 187 GLU A N   
1541 C CA  . GLU A 185 ? 0.3482 0.2262 0.3491 0.0291  0.0155  -0.0077 187 GLU A CA  
1542 C C   . GLU A 185 ? 0.3515 0.2389 0.3540 0.0333  0.0088  -0.0060 187 GLU A C   
1543 O O   . GLU A 185 ? 0.3993 0.2859 0.4065 0.0385  0.0085  -0.0038 187 GLU A O   
1544 C CB  . GLU A 185 ? 0.3828 0.2512 0.3799 0.0330  0.0172  -0.0008 187 GLU A CB  
1545 C CG  . GLU A 185 ? 0.4880 0.3469 0.4833 0.0280  0.0241  -0.0025 187 GLU A CG  
1546 C CD  . GLU A 185 ? 0.6520 0.5033 0.6419 0.0310  0.0253  0.0047  187 GLU A CD  
1547 O OE1 . GLU A 185 ? 0.7497 0.5992 0.7387 0.0382  0.0231  0.0114  187 GLU A OE1 
1548 O OE2 . GLU A 185 ? 0.7438 0.5919 0.7303 0.0260  0.0285  0.0037  187 GLU A OE2 
1549 N N   . TYR A 186 ? 0.3368 0.2334 0.3361 0.0309  0.0039  -0.0071 188 TYR A N   
1550 C CA  . TYR A 186 ? 0.2839 0.1899 0.2852 0.0332  -0.0018 -0.0068 188 TYR A CA  
1551 C C   . TYR A 186 ? 0.3545 0.2632 0.3504 0.0359  -0.0071 -0.0022 188 TYR A C   
1552 O O   . TYR A 186 ? 0.3396 0.2447 0.3293 0.0350  -0.0066 0.0000  188 TYR A O   
1553 C CB  . TYR A 186 ? 0.2955 0.2100 0.2981 0.0283  -0.0027 -0.0121 188 TYR A CB  
1554 C CG  . TYR A 186 ? 0.2901 0.2042 0.2979 0.0258  0.0018  -0.0171 188 TYR A CG  
1555 C CD1 . TYR A 186 ? 0.2882 0.2049 0.3024 0.0286  0.0016  -0.0181 188 TYR A CD1 
1556 C CD2 . TYR A 186 ? 0.2949 0.2068 0.3015 0.0204  0.0064  -0.0212 188 TYR A CD2 
1557 C CE1 . TYR A 186 ? 0.3068 0.2232 0.3254 0.0263  0.0061  -0.0230 188 TYR A CE1 
1558 C CE2 . TYR A 186 ? 0.2616 0.1737 0.2726 0.0177  0.0106  -0.0266 188 TYR A CE2 
1559 C CZ  . TYR A 186 ? 0.3205 0.2344 0.3372 0.0208  0.0106  -0.0275 188 TYR A CZ  
1560 O OH  . TYR A 186 ? 0.3309 0.2450 0.3515 0.0183  0.0151  -0.0332 188 TYR A OH  
1561 N N   . ASN A 187 ? 0.3005 0.2160 0.2988 0.0391  -0.0119 -0.0011 189 ASN A N   
1562 C CA  . ASN A 187 ? 0.3002 0.2202 0.2937 0.0409  -0.0173 0.0018  189 ASN A CA  
1563 C C   . ASN A 187 ? 0.3039 0.2272 0.2928 0.0362  -0.0185 -0.0008 189 ASN A C   
1564 O O   . ASN A 187 ? 0.2952 0.2229 0.2871 0.0328  -0.0180 -0.0048 189 ASN A O   
1565 C CB  . ASN A 187 ? 0.3315 0.2594 0.3300 0.0441  -0.0218 0.0022  189 ASN A CB  
1566 C CG  . ASN A 187 ? 0.4232 0.3567 0.4172 0.0457  -0.0275 0.0043  189 ASN A CG  
1567 O OD1 . ASN A 187 ? 0.3643 0.2953 0.3509 0.0453  -0.0281 0.0062  189 ASN A OD1 
1568 N ND2 . ASN A 187 ? 0.5762 0.5181 0.5751 0.0473  -0.0316 0.0037  189 ASN A ND2 
1569 N N   . VAL A 188 ? 0.2971 0.2185 0.2787 0.0363  -0.0196 0.0016  190 VAL A N   
1570 C CA  . VAL A 188 ? 0.3099 0.2343 0.2875 0.0326  -0.0203 -0.0005 190 VAL A CA  
1571 C C   . VAL A 188 ? 0.2966 0.2276 0.2735 0.0330  -0.0252 -0.0013 190 VAL A C   
1572 O O   . VAL A 188 ? 0.3429 0.2761 0.3173 0.0303  -0.0256 -0.0032 190 VAL A O   
1573 C CB  . VAL A 188 ? 0.3261 0.2455 0.2963 0.0318  -0.0184 0.0018  190 VAL A CB  
1574 C CG1 . VAL A 188 ? 0.3393 0.2522 0.3106 0.0299  -0.0128 0.0017  190 VAL A CG1 
1575 C CG2 . VAL A 188 ? 0.3435 0.2614 0.3081 0.0358  -0.0212 0.0062  190 VAL A CG2 
1576 N N   . ARG A 189 ? 0.3056 0.2400 0.2851 0.0363  -0.0288 -0.0002 191 ARG A N   
1577 C CA  . ARG A 189 ? 0.3485 0.2896 0.3281 0.0359  -0.0333 -0.0018 191 ARG A CA  
1578 C C   . ARG A 189 ? 0.3609 0.3068 0.3481 0.0338  -0.0332 -0.0053 191 ARG A C   
1579 O O   . ARG A 189 ? 0.3599 0.3109 0.3527 0.0352  -0.0356 -0.0059 191 ARG A O   
1580 C CB  . ARG A 189 ? 0.3446 0.2891 0.3235 0.0400  -0.0375 0.0010  191 ARG A CB  
1581 C CG  . ARG A 189 ? 0.3953 0.3357 0.3658 0.0424  -0.0376 0.0050  191 ARG A CG  
1582 C CD  . ARG A 189 ? 0.5583 0.5045 0.5274 0.0466  -0.0423 0.0079  191 ARG A CD  
1583 N NE  . ARG A 189 ? 0.6325 0.5859 0.5995 0.0445  -0.0467 0.0045  191 ARG A NE  
1584 C CZ  . ARG A 189 ? 0.7467 0.7085 0.7139 0.0466  -0.0517 0.0049  191 ARG A CZ  
1585 N NH1 . ARG A 189 ? 0.7592 0.7241 0.7290 0.0517  -0.0531 0.0094  191 ARG A NH1 
1586 N NH2 . ARG A 189 ? 0.7680 0.7356 0.7332 0.0436  -0.0551 0.0008  191 ARG A NH2 
1587 N N   . VAL A 190 ? 0.3039 0.2489 0.2912 0.0304  -0.0302 -0.0075 192 VAL A N   
1588 C CA  . VAL A 190 ? 0.2615 0.2110 0.2547 0.0281  -0.0294 -0.0104 192 VAL A CA  
1589 C C   . VAL A 190 ? 0.2870 0.2371 0.2769 0.0253  -0.0286 -0.0115 192 VAL A C   
1590 O O   . VAL A 190 ? 0.3036 0.2506 0.2871 0.0250  -0.0281 -0.0105 192 VAL A O   
1591 C CB  . VAL A 190 ? 0.2778 0.2265 0.2754 0.0274  -0.0256 -0.0115 192 VAL A CB  
1592 C CG1 . VAL A 190 ? 0.2856 0.2328 0.2872 0.0307  -0.0256 -0.0102 192 VAL A CG1 
1593 C CG2 . VAL A 190 ? 0.3043 0.2491 0.2975 0.0253  -0.0220 -0.0115 192 VAL A CG2 
1594 N N   . ALA A 191 ? 0.3115 0.2658 0.3059 0.0235  -0.0280 -0.0134 193 ALA A N   
1595 C CA  . ALA A 191 ? 0.2834 0.2387 0.2762 0.0215  -0.0269 -0.0141 193 ALA A CA  
1596 C C   . ALA A 191 ? 0.2981 0.2519 0.2871 0.0215  -0.0292 -0.0144 193 ALA A C   
1597 O O   . ALA A 191 ? 0.3315 0.2836 0.3168 0.0230  -0.0318 -0.0138 193 ALA A O   
1598 C CB  . ALA A 191 ? 0.2461 0.1999 0.2351 0.0204  -0.0236 -0.0132 193 ALA A CB  
1599 N N   . SER A 192 ? 0.2561 0.2106 0.2459 0.0199  -0.0281 -0.0154 194 SER A N   
1600 C CA  . SER A 192 ? 0.2603 0.2124 0.2461 0.0193  -0.0292 -0.0165 194 SER A CA  
1601 C C   . SER A 192 ? 0.2796 0.2276 0.2580 0.0200  -0.0276 -0.0150 194 SER A C   
1602 O O   . SER A 192 ? 0.2803 0.2284 0.2580 0.0201  -0.0248 -0.0133 194 SER A O   
1603 C CB  . SER A 192 ? 0.3289 0.2816 0.3185 0.0174  -0.0272 -0.0178 194 SER A CB  
1604 O OG  . SER A 192 ? 0.4946 0.4431 0.4794 0.0169  -0.0260 -0.0185 194 SER A OG  
1605 N N   . ARG A 193 ? 0.2755 0.2210 0.2485 0.0202  -0.0293 -0.0159 195 ARG A N   
1606 C CA  . ARG A 193 ? 0.2416 0.1835 0.2071 0.0211  -0.0279 -0.0145 195 ARG A CA  
1607 C C   . ARG A 193 ? 0.3002 0.2414 0.2656 0.0209  -0.0237 -0.0131 195 ARG A C   
1608 O O   . ARG A 193 ? 0.2837 0.2246 0.2464 0.0215  -0.0220 -0.0111 195 ARG A O   
1609 C CB  . ARG A 193 ? 0.2893 0.2290 0.2492 0.0209  -0.0296 -0.0165 195 ARG A CB  
1610 C CG  . ARG A 193 ? 0.3209 0.2569 0.2728 0.0219  -0.0277 -0.0152 195 ARG A CG  
1611 C CD  . ARG A 193 ? 0.3555 0.2893 0.3018 0.0213  -0.0285 -0.0181 195 ARG A CD  
1612 N NE  . ARG A 193 ? 0.4167 0.3536 0.3629 0.0208  -0.0330 -0.0204 195 ARG A NE  
1613 C CZ  . ARG A 193 ? 0.4832 0.4204 0.4286 0.0187  -0.0342 -0.0248 195 ARG A CZ  
1614 N NH1 . ARG A 193 ? 0.4509 0.3837 0.3955 0.0173  -0.0306 -0.0272 195 ARG A NH1 
1615 N NH2 . ARG A 193 ? 0.5020 0.4443 0.4479 0.0181  -0.0388 -0.0268 195 ARG A NH2 
1616 N N   . TYR A 194 ? 0.2773 0.2186 0.2457 0.0200  -0.0216 -0.0140 196 TYR A N   
1617 C CA  . TYR A 194 ? 0.2509 0.1922 0.2189 0.0206  -0.0175 -0.0119 196 TYR A CA  
1618 C C   . TYR A 194 ? 0.2722 0.2187 0.2439 0.0207  -0.0161 -0.0098 196 TYR A C   
1619 O O   . TYR A 194 ? 0.2626 0.2113 0.2335 0.0214  -0.0131 -0.0076 196 TYR A O   
1620 C CB  . TYR A 194 ? 0.2660 0.2054 0.2368 0.0202  -0.0152 -0.0128 196 TYR A CB  
1621 C CG  . TYR A 194 ? 0.2863 0.2210 0.2545 0.0191  -0.0166 -0.0163 196 TYR A CG  
1622 C CD1 . TYR A 194 ? 0.3153 0.2468 0.2763 0.0197  -0.0172 -0.0172 196 TYR A CD1 
1623 C CD2 . TYR A 194 ? 0.3807 0.3149 0.3535 0.0171  -0.0171 -0.0190 196 TYR A CD2 
1624 C CE1 . TYR A 194 ? 0.3628 0.2910 0.3207 0.0183  -0.0186 -0.0212 196 TYR A CE1 
1625 C CE2 . TYR A 194 ? 0.4415 0.3724 0.4120 0.0153  -0.0184 -0.0231 196 TYR A CE2 
1626 C CZ  . TYR A 194 ? 0.4135 0.3416 0.3763 0.0159  -0.0192 -0.0244 196 TYR A CZ  
1627 O OH  . TYR A 194 ? 0.4155 0.3412 0.3752 0.0138  -0.0205 -0.0291 196 TYR A OH  
1628 N N   . PHE A 195 ? 0.2341 0.1832 0.2096 0.0199  -0.0180 -0.0105 197 PHE A N   
1629 C CA  . PHE A 195 ? 0.2075 0.1618 0.1864 0.0194  -0.0165 -0.0096 197 PHE A CA  
1630 C C   . PHE A 195 ? 0.2493 0.2033 0.2270 0.0191  -0.0174 -0.0098 197 PHE A C   
1631 O O   . PHE A 195 ? 0.2674 0.2253 0.2478 0.0180  -0.0161 -0.0101 197 PHE A O   
1632 C CB  . PHE A 195 ? 0.2434 0.2008 0.2287 0.0187  -0.0167 -0.0104 197 PHE A CB  
1633 C CG  . PHE A 195 ? 0.2340 0.1906 0.2210 0.0188  -0.0149 -0.0099 197 PHE A CG  
1634 C CD1 . PHE A 195 ? 0.2339 0.1940 0.2218 0.0195  -0.0115 -0.0072 197 PHE A CD1 
1635 C CD2 . PHE A 195 ? 0.2697 0.2220 0.2569 0.0183  -0.0164 -0.0118 197 PHE A CD2 
1636 C CE1 . PHE A 195 ? 0.2629 0.2209 0.2523 0.0201  -0.0090 -0.0060 197 PHE A CE1 
1637 C CE2 . PHE A 195 ? 0.2589 0.2090 0.2478 0.0180  -0.0139 -0.0116 197 PHE A CE2 
1638 C CZ  . PHE A 195 ? 0.2755 0.2275 0.2654 0.0192  -0.0100 -0.0085 197 PHE A CZ  
1639 N N   . LYS A 196 ? 0.2277 0.1771 0.2010 0.0198  -0.0191 -0.0098 198 LYS A N   
1640 C CA  . LYS A 196 ? 0.2136 0.1612 0.1855 0.0198  -0.0192 -0.0094 198 LYS A CA  
1641 C C   . LYS A 196 ? 0.2366 0.1857 0.2064 0.0186  -0.0162 -0.0085 198 LYS A C   
1642 O O   . LYS A 196 ? 0.2548 0.2038 0.2209 0.0190  -0.0150 -0.0073 198 LYS A O   
1643 C CB  . LYS A 196 ? 0.2314 0.1740 0.1984 0.0214  -0.0216 -0.0087 198 LYS A CB  
1644 C CG  . LYS A 196 ? 0.2404 0.1832 0.2098 0.0226  -0.0251 -0.0096 198 LYS A CG  
1645 C CD  . LYS A 196 ? 0.2323 0.1722 0.1958 0.0243  -0.0276 -0.0087 198 LYS A CD  
1646 C CE  . LYS A 196 ? 0.2764 0.2188 0.2424 0.0253  -0.0316 -0.0098 198 LYS A CE  
1647 N NZ  . LYS A 196 ? 0.3188 0.2622 0.2895 0.0268  -0.0323 -0.0087 198 LYS A NZ  
1648 N N   . GLY A 197 ? 0.2590 0.2096 0.2313 0.0171  -0.0147 -0.0092 199 GLY A N   
1649 C CA  . GLY A 197 ? 0.2537 0.2065 0.2246 0.0151  -0.0118 -0.0091 199 GLY A CA  
1650 C C   . GLY A 197 ? 0.2504 0.1975 0.2164 0.0154  -0.0113 -0.0076 199 GLY A C   
1651 O O   . GLY A 197 ? 0.2573 0.1985 0.2213 0.0172  -0.0130 -0.0067 199 GLY A O   
1652 N N   . PRO A 198 ? 0.2257 0.1752 0.1896 0.0139  -0.0088 -0.0071 200 PRO A N   
1653 C CA  . PRO A 198 ? 0.2528 0.1971 0.2121 0.0137  -0.0074 -0.0055 200 PRO A CA  
1654 C C   . PRO A 198 ? 0.2742 0.2122 0.2342 0.0133  -0.0068 -0.0056 200 PRO A C   
1655 O O   . PRO A 198 ? 0.2751 0.2067 0.2308 0.0150  -0.0069 -0.0033 200 PRO A O   
1656 C CB  . PRO A 198 ? 0.2834 0.2340 0.2430 0.0110  -0.0043 -0.0057 200 PRO A CB  
1657 C CG  . PRO A 198 ? 0.3011 0.2598 0.2633 0.0116  -0.0049 -0.0059 200 PRO A CG  
1658 C CD  . PRO A 198 ? 0.2667 0.2250 0.2325 0.0124  -0.0071 -0.0073 200 PRO A CD  
1659 N N   . GLU A 199 ? 0.2640 0.2033 0.2290 0.0115  -0.0058 -0.0081 201 GLU A N   
1660 C CA  . GLU A 199 ? 0.2483 0.1804 0.2145 0.0115  -0.0043 -0.0081 201 GLU A CA  
1661 C C   . GLU A 199 ? 0.2538 0.1805 0.2184 0.0159  -0.0074 -0.0055 201 GLU A C   
1662 O O   . GLU A 199 ? 0.2743 0.1940 0.2366 0.0175  -0.0064 -0.0030 201 GLU A O   
1663 C CB  . GLU A 199 ? 0.2940 0.2287 0.2661 0.0089  -0.0025 -0.0118 201 GLU A CB  
1664 C CG  . GLU A 199 ? 0.3019 0.2421 0.2778 0.0101  -0.0051 -0.0134 201 GLU A CG  
1665 C CD  . GLU A 199 ? 0.2972 0.2475 0.2742 0.0079  -0.0050 -0.0149 201 GLU A CD  
1666 O OE1 . GLU A 199 ? 0.2982 0.2512 0.2721 0.0084  -0.0056 -0.0130 201 GLU A OE1 
1667 O OE2 . GLU A 199 ? 0.2740 0.2299 0.2550 0.0061  -0.0042 -0.0177 201 GLU A OE2 
1668 N N   . LEU A 200 ? 0.2357 0.1661 0.2015 0.0178  -0.0110 -0.0059 202 LEU A N   
1669 C CA  . LEU A 200 ? 0.2539 0.1815 0.2185 0.0216  -0.0145 -0.0040 202 LEU A CA  
1670 C C   . LEU A 200 ? 0.2891 0.2140 0.2464 0.0233  -0.0156 -0.0012 202 LEU A C   
1671 O O   . LEU A 200 ? 0.2963 0.2173 0.2507 0.0261  -0.0168 0.0016  202 LEU A O   
1672 C CB  . LEU A 200 ? 0.2420 0.1748 0.2100 0.0222  -0.0176 -0.0057 202 LEU A CB  
1673 C CG  . LEU A 200 ? 0.2634 0.2005 0.2381 0.0204  -0.0164 -0.0085 202 LEU A CG  
1674 C CD1 . LEU A 200 ? 0.2625 0.2039 0.2404 0.0213  -0.0194 -0.0095 202 LEU A CD1 
1675 C CD2 . LEU A 200 ? 0.2642 0.1976 0.2425 0.0209  -0.0146 -0.0089 202 LEU A CD2 
1676 N N   . LEU A 201 ? 0.2563 0.1837 0.2104 0.0218  -0.0149 -0.0016 203 LEU A N   
1677 C CA  . LEU A 201 ? 0.2576 0.1831 0.2046 0.0233  -0.0157 0.0003  203 LEU A CA  
1678 C C   . LEU A 201 ? 0.2960 0.2164 0.2385 0.0234  -0.0129 0.0032  203 LEU A C   
1679 O O   . LEU A 201 ? 0.3335 0.2517 0.2696 0.0253  -0.0138 0.0055  203 LEU A O   
1680 C CB  . LEU A 201 ? 0.2616 0.1910 0.2073 0.0221  -0.0151 -0.0010 203 LEU A CB  
1681 C CG  . LEU A 201 ? 0.2805 0.2139 0.2302 0.0222  -0.0172 -0.0033 203 LEU A CG  
1682 C CD1 . LEU A 201 ? 0.2832 0.2200 0.2326 0.0214  -0.0152 -0.0039 203 LEU A CD1 
1683 C CD2 . LEU A 201 ? 0.2968 0.2289 0.2445 0.0242  -0.0210 -0.0038 203 LEU A CD2 
1684 N N   . VAL A 202 ? 0.3252 0.2439 0.2710 0.0210  -0.0093 0.0030  204 VAL A N   
1685 C CA  . VAL A 202 ? 0.3328 0.2455 0.2753 0.0208  -0.0059 0.0058  204 VAL A CA  
1686 C C   . VAL A 202 ? 0.3404 0.2469 0.2853 0.0226  -0.0051 0.0076  204 VAL A C   
1687 O O   . VAL A 202 ? 0.3611 0.2613 0.3046 0.0222  -0.0013 0.0100  204 VAL A O   
1688 C CB  . VAL A 202 ? 0.3226 0.2371 0.2666 0.0164  -0.0014 0.0043  204 VAL A CB  
1689 C CG1 . VAL A 202 ? 0.3462 0.2670 0.2878 0.0156  -0.0019 0.0036  204 VAL A CG1 
1690 C CG2 . VAL A 202 ? 0.3239 0.2410 0.2752 0.0130  0.0003  0.0006  204 VAL A CG2 
1691 N N   . ASP A 203 ? 0.3138 0.2219 0.2630 0.0246  -0.0080 0.0065  205 ASP A N   
1692 C CA  . ASP A 203 ? 0.3059 0.2087 0.2578 0.0275  -0.0076 0.0087  205 ASP A CA  
1693 C C   . ASP A 203 ? 0.3407 0.2387 0.2977 0.0246  -0.0022 0.0069  205 ASP A C   
1694 O O   . ASP A 203 ? 0.3914 0.2815 0.3487 0.0264  0.0009  0.0098  205 ASP A O   
1695 C CB  . ASP A 203 ? 0.3464 0.2446 0.2920 0.0318  -0.0082 0.0144  205 ASP A CB  
1696 C CG  . ASP A 203 ? 0.5965 0.4928 0.5449 0.0366  -0.0099 0.0173  205 ASP A CG  
1697 O OD1 . ASP A 203 ? 0.6090 0.5079 0.5640 0.0367  -0.0111 0.0146  205 ASP A OD1 
1698 O OD2 . ASP A 203 ? 0.7631 0.6557 0.7068 0.0407  -0.0099 0.0228  205 ASP A OD2 
1699 N N   . TYR A 204 ? 0.3045 0.2073 0.2654 0.0200  -0.0008 0.0021  206 TYR A N   
1700 C CA  . TYR A 204 ? 0.2934 0.1932 0.2594 0.0164  0.0040  -0.0011 206 TYR A CA  
1701 C C   . TYR A 204 ? 0.2984 0.1999 0.2704 0.0177  0.0027  -0.0037 206 TYR A C   
1702 O O   . TYR A 204 ? 0.3023 0.2119 0.2766 0.0168  -0.0001 -0.0065 206 TYR A O   
1703 C CB  . TYR A 204 ? 0.2774 0.1833 0.2440 0.0106  0.0062  -0.0051 206 TYR A CB  
1704 C CG  . TYR A 204 ? 0.2976 0.2006 0.2688 0.0060  0.0114  -0.0091 206 TYR A CG  
1705 C CD1 . TYR A 204 ? 0.3380 0.2319 0.3083 0.0043  0.0166  -0.0078 206 TYR A CD1 
1706 C CD2 . TYR A 204 ? 0.2953 0.2042 0.2715 0.0032  0.0117  -0.0143 206 TYR A CD2 
1707 C CE1 . TYR A 204 ? 0.3333 0.2238 0.3081 -0.0005 0.0221  -0.0123 206 TYR A CE1 
1708 C CE2 . TYR A 204 ? 0.2997 0.2061 0.2798 -0.0014 0.0167  -0.0189 206 TYR A CE2 
1709 C CZ  . TYR A 204 ? 0.3254 0.2223 0.3049 -0.0035 0.0219  -0.0182 206 TYR A CZ  
1710 O OH  . TYR A 204 ? 0.3352 0.2290 0.3188 -0.0087 0.0275  -0.0236 206 TYR A OH  
1711 N N   . GLN A 205 ? 0.2911 0.1850 0.2661 0.0201  0.0053  -0.0024 207 GLN A N   
1712 C CA  . GLN A 205 ? 0.2841 0.1795 0.2646 0.0227  0.0038  -0.0037 207 GLN A CA  
1713 C C   . GLN A 205 ? 0.3012 0.1978 0.2875 0.0186  0.0074  -0.0097 207 GLN A C   
1714 O O   . GLN A 205 ? 0.2992 0.1994 0.2902 0.0200  0.0060  -0.0116 207 GLN A O   
1715 C CB  . GLN A 205 ? 0.3301 0.2176 0.3115 0.0286  0.0046  0.0013  207 GLN A CB  
1716 C CG  . GLN A 205 ? 0.3345 0.2234 0.3104 0.0333  0.0000  0.0070  207 GLN A CG  
1717 C CD  . GLN A 205 ? 0.4246 0.3080 0.4017 0.0398  0.0003  0.0126  207 GLN A CD  
1718 O OE1 . GLN A 205 ? 0.4817 0.3574 0.4551 0.0419  0.0033  0.0174  207 GLN A OE1 
1719 N NE2 . GLN A 205 ? 0.4033 0.2911 0.3857 0.0433  -0.0024 0.0123  207 GLN A NE2 
1720 N N   . MET A 206 ? 0.2891 0.1834 0.2753 0.0132  0.0122  -0.0129 208 MET A N   
1721 C CA  . MET A 206 ? 0.2583 0.1536 0.2495 0.0089  0.0162  -0.0193 208 MET A CA  
1722 C C   . MET A 206 ? 0.2716 0.1796 0.2628 0.0046  0.0140  -0.0236 208 MET A C   
1723 O O   . MET A 206 ? 0.2980 0.2096 0.2893 -0.0012 0.0169  -0.0279 208 MET A O   
1724 C CB  . MET A 206 ? 0.3219 0.2078 0.3135 0.0050  0.0231  -0.0212 208 MET A CB  
1725 C CG  . MET A 206 ? 0.3758 0.2595 0.3729 0.0013  0.0282  -0.0278 208 MET A CG  
1726 S SD  . MET A 206 ? 0.3569 0.2273 0.3552 -0.0037 0.0374  -0.0305 208 MET A SD  
1727 C CE  . MET A 206 ? 0.4210 0.2770 0.4177 0.0044  0.0386  -0.0211 208 MET A CE  
1728 N N   . TYR A 207 ? 0.2731 0.1883 0.2643 0.0076  0.0087  -0.0221 209 TYR A N   
1729 C CA  . TYR A 207 ? 0.2354 0.1624 0.2264 0.0049  0.0064  -0.0245 209 TYR A CA  
1730 C C   . TYR A 207 ? 0.2653 0.1978 0.2611 0.0038  0.0070  -0.0289 209 TYR A C   
1731 O O   . TYR A 207 ? 0.2861 0.2131 0.2856 0.0046  0.0097  -0.0307 209 TYR A O   
1732 C CB  . TYR A 207 ? 0.2322 0.1630 0.2199 0.0083  0.0013  -0.0203 209 TYR A CB  
1733 C CG  . TYR A 207 ? 0.2525 0.1819 0.2420 0.0133  -0.0023 -0.0179 209 TYR A CG  
1734 C CD1 . TYR A 207 ? 0.2461 0.1817 0.2399 0.0137  -0.0038 -0.0199 209 TYR A CD1 
1735 C CD2 . TYR A 207 ? 0.2536 0.1769 0.2406 0.0174  -0.0042 -0.0134 209 TYR A CD2 
1736 C CE1 . TYR A 207 ? 0.2527 0.1883 0.2490 0.0177  -0.0070 -0.0180 209 TYR A CE1 
1737 C CE2 . TYR A 207 ? 0.2487 0.1729 0.2379 0.0217  -0.0078 -0.0115 209 TYR A CE2 
1738 C CZ  . TYR A 207 ? 0.2528 0.1832 0.2469 0.0216  -0.0092 -0.0140 209 TYR A CZ  
1739 O OH  . TYR A 207 ? 0.2644 0.1968 0.2613 0.0253  -0.0127 -0.0124 209 TYR A OH  
1740 N N   . ASP A 208 ? 0.2452 0.1886 0.2410 0.0021  0.0051  -0.0303 210 ASP A N   
1741 C CA  . ASP A 208 ? 0.2357 0.1855 0.2354 0.0003  0.0064  -0.0347 210 ASP A CA  
1742 C C   . ASP A 208 ? 0.2196 0.1801 0.2191 0.0011  0.0030  -0.0334 210 ASP A C   
1743 O O   . ASP A 208 ? 0.2258 0.1865 0.2233 0.0040  -0.0004 -0.0292 210 ASP A O   
1744 C CB  . ASP A 208 ? 0.2778 0.2298 0.2779 -0.0057 0.0110  -0.0405 210 ASP A CB  
1745 C CG  . ASP A 208 ? 0.2810 0.2409 0.2778 -0.0095 0.0107  -0.0407 210 ASP A CG  
1746 O OD1 . ASP A 208 ? 0.3125 0.2674 0.3075 -0.0120 0.0131  -0.0410 210 ASP A OD1 
1747 O OD2 . ASP A 208 ? 0.3082 0.2796 0.3042 -0.0097 0.0084  -0.0402 210 ASP A OD2 
1748 N N   . TYR A 209 ? 0.2183 0.1873 0.2199 -0.0013 0.0043  -0.0372 211 TYR A N   
1749 C CA  . TYR A 209 ? 0.2083 0.1874 0.2101 -0.0004 0.0020  -0.0356 211 TYR A CA  
1750 C C   . TYR A 209 ? 0.1969 0.1810 0.1951 -0.0003 0.0000  -0.0321 211 TYR A C   
1751 O O   . TYR A 209 ? 0.2106 0.1991 0.2088 0.0020  -0.0021 -0.0289 211 TYR A O   
1752 C CB  . TYR A 209 ? 0.2113 0.2005 0.2145 -0.0039 0.0043  -0.0402 211 TYR A CB  
1753 C CG  . TYR A 209 ? 0.2180 0.2034 0.2244 -0.0054 0.0077  -0.0454 211 TYR A CG  
1754 C CD1 . TYR A 209 ? 0.2248 0.2100 0.2306 -0.0102 0.0115  -0.0510 211 TYR A CD1 
1755 C CD2 . TYR A 209 ? 0.2149 0.1971 0.2253 -0.0021 0.0075  -0.0451 211 TYR A CD2 
1756 C CE1 . TYR A 209 ? 0.2361 0.2169 0.2449 -0.0117 0.0155  -0.0563 211 TYR A CE1 
1757 C CE2 . TYR A 209 ? 0.2311 0.2097 0.2447 -0.0031 0.0112  -0.0499 211 TYR A CE2 
1758 C CZ  . TYR A 209 ? 0.2516 0.2289 0.2642 -0.0078 0.0153  -0.0556 211 TYR A CZ  
1759 O OH  . TYR A 209 ? 0.2453 0.2181 0.2612 -0.0088 0.0197  -0.0609 211 TYR A OH  
1760 N N   . SER A 210 ? 0.2121 0.1957 0.2074 -0.0028 0.0013  -0.0326 212 SER A N   
1761 C CA  . SER A 210 ? 0.2096 0.1992 0.2019 -0.0026 0.0000  -0.0294 212 SER A CA  
1762 C C   . SER A 210 ? 0.2000 0.1833 0.1905 0.0017  -0.0029 -0.0244 212 SER A C   
1763 O O   . SER A 210 ? 0.2153 0.2034 0.2039 0.0030  -0.0039 -0.0214 212 SER A O   
1764 C CB  . SER A 210 ? 0.2200 0.2104 0.2104 -0.0065 0.0022  -0.0313 212 SER A CB  
1765 O OG  . SER A 210 ? 0.2363 0.2142 0.2262 -0.0065 0.0035  -0.0316 212 SER A OG  
1766 N N   . LEU A 211 ? 0.2008 0.1741 0.1918 0.0042  -0.0040 -0.0236 213 LEU A N   
1767 C CA  . LEU A 211 ? 0.2046 0.1737 0.1942 0.0079  -0.0070 -0.0199 213 LEU A CA  
1768 C C   . LEU A 211 ? 0.2265 0.2018 0.2176 0.0093  -0.0083 -0.0185 213 LEU A C   
1769 O O   . LEU A 211 ? 0.2151 0.1905 0.2041 0.0109  -0.0095 -0.0157 213 LEU A O   
1770 C CB  . LEU A 211 ? 0.2563 0.2168 0.2472 0.0103  -0.0083 -0.0196 213 LEU A CB  
1771 C CG  . LEU A 211 ? 0.2493 0.2074 0.2394 0.0136  -0.0118 -0.0168 213 LEU A CG  
1772 C CD1 . LEU A 211 ? 0.2606 0.2159 0.2452 0.0143  -0.0126 -0.0143 213 LEU A CD1 
1773 C CD2 . LEU A 211 ? 0.2413 0.1941 0.2339 0.0161  -0.0133 -0.0167 213 LEU A CD2 
1774 N N   . ASP A 212 ? 0.2208 0.2010 0.2158 0.0086  -0.0076 -0.0204 214 ASP A N   
1775 C CA  . ASP A 212 ? 0.2252 0.2109 0.2222 0.0098  -0.0082 -0.0187 214 ASP A CA  
1776 C C   . ASP A 212 ? 0.2080 0.2013 0.2027 0.0096  -0.0072 -0.0164 214 ASP A C   
1777 O O   . ASP A 212 ? 0.2098 0.2047 0.2049 0.0115  -0.0074 -0.0134 214 ASP A O   
1778 C CB  . ASP A 212 ? 0.2073 0.1977 0.2085 0.0089  -0.0070 -0.0212 214 ASP A CB  
1779 C CG  . ASP A 212 ? 0.2316 0.2156 0.2363 0.0102  -0.0079 -0.0226 214 ASP A CG  
1780 O OD1 . ASP A 212 ? 0.2270 0.2044 0.2314 0.0123  -0.0103 -0.0210 214 ASP A OD1 
1781 O OD2 . ASP A 212 ? 0.2226 0.2091 0.2305 0.0093  -0.0062 -0.0256 214 ASP A OD2 
1782 N N   . MET A 213 ? 0.2113 0.2095 0.2041 0.0072  -0.0057 -0.0177 215 MET A N   
1783 C CA  . MET A 213 ? 0.1983 0.2058 0.1894 0.0073  -0.0048 -0.0152 215 MET A CA  
1784 C C   . MET A 213 ? 0.1902 0.1931 0.1783 0.0095  -0.0054 -0.0117 215 MET A C   
1785 O O   . MET A 213 ? 0.2086 0.2164 0.1963 0.0117  -0.0048 -0.0082 215 MET A O   
1786 C CB  . MET A 213 ? 0.2314 0.2474 0.2219 0.0034  -0.0031 -0.0183 215 MET A CB  
1787 C CG  . MET A 213 ? 0.2325 0.2533 0.2254 0.0008  -0.0019 -0.0227 215 MET A CG  
1788 S SD  . MET A 213 ? 0.2523 0.2812 0.2475 0.0029  -0.0018 -0.0205 215 MET A SD  
1789 C CE  . MET A 213 ? 0.2572 0.3010 0.2503 0.0036  -0.0012 -0.0165 215 MET A CE  
1790 N N   . TRP A 214 ? 0.2056 0.1992 0.1917 0.0095  -0.0063 -0.0125 216 TRP A N   
1791 C CA  . TRP A 214 ? 0.2022 0.1906 0.1852 0.0118  -0.0069 -0.0096 216 TRP A CA  
1792 C C   . TRP A 214 ? 0.2057 0.1904 0.1897 0.0146  -0.0079 -0.0077 216 TRP A C   
1793 O O   . TRP A 214 ? 0.2284 0.2140 0.2113 0.0166  -0.0071 -0.0049 216 TRP A O   
1794 C CB  . TRP A 214 ? 0.2057 0.1849 0.1858 0.0114  -0.0076 -0.0105 216 TRP A CB  
1795 C CG  . TRP A 214 ? 0.2198 0.1940 0.1960 0.0139  -0.0082 -0.0080 216 TRP A CG  
1796 C CD1 . TRP A 214 ? 0.2214 0.1890 0.1966 0.0160  -0.0101 -0.0073 216 TRP A CD1 
1797 C CD2 . TRP A 214 ? 0.2216 0.1978 0.1947 0.0141  -0.0067 -0.0062 216 TRP A CD2 
1798 N NE1 . TRP A 214 ? 0.2267 0.1914 0.1978 0.0175  -0.0096 -0.0056 216 TRP A NE1 
1799 C CE2 . TRP A 214 ? 0.2276 0.1974 0.1974 0.0166  -0.0074 -0.0046 216 TRP A CE2 
1800 C CE3 . TRP A 214 ? 0.2356 0.2190 0.2085 0.0121  -0.0047 -0.0062 216 TRP A CE3 
1801 C CZ2 . TRP A 214 ? 0.2392 0.2088 0.2054 0.0177  -0.0059 -0.0028 216 TRP A CZ2 
1802 C CZ3 . TRP A 214 ? 0.2106 0.1948 0.1806 0.0132  -0.0034 -0.0040 216 TRP A CZ3 
1803 C CH2 . TRP A 214 ? 0.2638 0.2408 0.2304 0.0162  -0.0038 -0.0022 216 TRP A CH2 
1804 N N   . SER A 215 ? 0.1945 0.1748 0.1809 0.0146  -0.0095 -0.0094 217 SER A N   
1805 C CA  . SER A 215 ? 0.1883 0.1654 0.1764 0.0163  -0.0104 -0.0083 217 SER A CA  
1806 C C   . SER A 215 ? 0.2212 0.2048 0.2113 0.0172  -0.0082 -0.0058 217 SER A C   
1807 O O   . SER A 215 ? 0.2202 0.2010 0.2101 0.0190  -0.0074 -0.0037 217 SER A O   
1808 C CB  . SER A 215 ? 0.2271 0.2013 0.2186 0.0159  -0.0122 -0.0106 217 SER A CB  
1809 O OG  . SER A 215 ? 0.2409 0.2095 0.2307 0.0159  -0.0139 -0.0120 217 SER A OG  
1810 N N   . LEU A 216 ? 0.2257 0.2180 0.2178 0.0161  -0.0069 -0.0060 218 LEU A N   
1811 C CA  . LEU A 216 ? 0.2248 0.2247 0.2184 0.0174  -0.0047 -0.0028 218 LEU A CA  
1812 C C   . LEU A 216 ? 0.2011 0.2033 0.1920 0.0195  -0.0031 0.0010  218 LEU A C   
1813 O O   . LEU A 216 ? 0.2384 0.2410 0.2302 0.0221  -0.0012 0.0048  218 LEU A O   
1814 C CB  . LEU A 216 ? 0.2451 0.2554 0.2402 0.0156  -0.0039 -0.0040 218 LEU A CB  
1815 C CG  . LEU A 216 ? 0.2579 0.2775 0.2543 0.0173  -0.0016 -0.0001 218 LEU A CG  
1816 C CD1 . LEU A 216 ? 0.2694 0.2852 0.2694 0.0182  -0.0010 0.0008  218 LEU A CD1 
1817 C CD2 . LEU A 216 ? 0.3246 0.3570 0.3207 0.0153  -0.0009 -0.0016 218 LEU A CD2 
1818 N N   . GLY A 217 ? 0.2108 0.2147 0.1989 0.0186  -0.0035 0.0001  219 GLY A N   
1819 C CA  . GLY A 217 ? 0.2130 0.2194 0.1988 0.0208  -0.0019 0.0036  219 GLY A CA  
1820 C C   . GLY A 217 ? 0.2433 0.2393 0.2278 0.0234  -0.0014 0.0051  219 GLY A C   
1821 O O   . GLY A 217 ? 0.2576 0.2547 0.2420 0.0264  0.0010  0.0090  219 GLY A O   
1822 N N   . CYS A 218 ? 0.2239 0.2099 0.2072 0.0222  -0.0035 0.0021  220 CYS A N   
1823 C CA  . CYS A 218 ? 0.2257 0.2023 0.2075 0.0239  -0.0032 0.0024  220 CYS A CA  
1824 C C   . CYS A 218 ? 0.2915 0.2670 0.2768 0.0253  -0.0013 0.0043  220 CYS A C   
1825 O O   . CYS A 218 ? 0.2668 0.2377 0.2514 0.0275  0.0012  0.0063  220 CYS A O   
1826 C CB  . CYS A 218 ? 0.2155 0.1841 0.1958 0.0222  -0.0064 -0.0013 220 CYS A CB  
1827 S SG  . CYS A 218 ? 0.2468 0.2138 0.2223 0.0211  -0.0078 -0.0027 220 CYS A SG  
1828 N N   . MET A 219 ? 0.2352 0.2141 0.2243 0.0240  -0.0018 0.0037  221 MET A N   
1829 C CA  . MET A 219 ? 0.2603 0.2386 0.2531 0.0252  0.0007  0.0060  221 MET A CA  
1830 C C   . MET A 219 ? 0.2653 0.2497 0.2582 0.0284  0.0045  0.0115  221 MET A C   
1831 O O   . MET A 219 ? 0.2805 0.2600 0.2744 0.0307  0.0077  0.0144  221 MET A O   
1832 C CB  . MET A 219 ? 0.2853 0.2678 0.2821 0.0233  -0.0004 0.0045  221 MET A CB  
1833 C CG  . MET A 219 ? 0.3465 0.3233 0.3444 0.0209  -0.0037 -0.0001 221 MET A CG  
1834 S SD  . MET A 219 ? 0.3506 0.3325 0.3543 0.0193  -0.0039 -0.0013 221 MET A SD  
1835 C CE  . MET A 219 ? 0.2568 0.2403 0.2632 0.0210  0.0006  0.0035  221 MET A CE  
1836 N N   . LEU A 220 ? 0.2457 0.2411 0.2378 0.0286  0.0043  0.0131  222 LEU A N   
1837 C CA  . LEU A 220 ? 0.2596 0.2636 0.2520 0.0322  0.0075  0.0188  222 LEU A CA  
1838 C C   . LEU A 220 ? 0.2580 0.2565 0.2484 0.0353  0.0098  0.0214  222 LEU A C   
1839 O O   . LEU A 220 ? 0.2775 0.2750 0.2693 0.0391  0.0137  0.0263  222 LEU A O   
1840 C CB  . LEU A 220 ? 0.2601 0.2782 0.2516 0.0310  0.0063  0.0187  222 LEU A CB  
1841 C CG  . LEU A 220 ? 0.2507 0.2814 0.2424 0.0346  0.0088  0.0247  222 LEU A CG  
1842 C CD1 . LEU A 220 ? 0.2715 0.3066 0.2658 0.0369  0.0113  0.0293  222 LEU A CD1 
1843 C CD2 . LEU A 220 ? 0.2745 0.3189 0.2650 0.0321  0.0069  0.0227  222 LEU A CD2 
1844 N N   . ALA A 221 ? 0.2298 0.2243 0.2169 0.0340  0.0079  0.0182  223 ALA A N   
1845 C CA  . ALA A 221 ? 0.2350 0.2244 0.2199 0.0369  0.0103  0.0200  223 ALA A CA  
1846 C C   . ALA A 221 ? 0.2787 0.2558 0.2644 0.0384  0.0130  0.0203  223 ALA A C   
1847 O O   . ALA A 221 ? 0.2603 0.2352 0.2464 0.0423  0.0173  0.0244  223 ALA A O   
1848 C CB  . ALA A 221 ? 0.2422 0.2279 0.2230 0.0346  0.0077  0.0160  223 ALA A CB  
1849 N N   . SER A 222 ? 0.2717 0.2409 0.2581 0.0352  0.0109  0.0160  224 SER A N   
1850 C CA  A SER A 222 ? 0.3136 0.2715 0.3011 0.0355  0.0135  0.0151  224 SER A CA  
1851 C CA  B SER A 222 ? 0.3045 0.2624 0.2920 0.0355  0.0135  0.0151  224 SER A CA  
1852 C C   . SER A 222 ? 0.3097 0.2686 0.3014 0.0383  0.0182  0.0204  224 SER A C   
1853 O O   . SER A 222 ? 0.3572 0.3075 0.3497 0.0404  0.0227  0.0219  224 SER A O   
1854 C CB  A SER A 222 ? 0.2951 0.2472 0.2833 0.0312  0.0098  0.0094  224 SER A CB  
1855 C CB  B SER A 222 ? 0.3077 0.2598 0.2959 0.0313  0.0098  0.0094  224 SER A CB  
1856 O OG  A SER A 222 ? 0.3015 0.2586 0.2939 0.0297  0.0088  0.0096  224 SER A OG  
1857 O OG  B SER A 222 ? 0.3527 0.3009 0.3364 0.0296  0.0066  0.0052  224 SER A OG  
1858 N N   . MET A 223 ? 0.2787 0.2478 0.2730 0.0385  0.0178  0.0233  225 MET A N   
1859 C CA  . MET A 223 ? 0.3176 0.2883 0.3157 0.0413  0.0224  0.0290  225 MET A CA  
1860 C C   . MET A 223 ? 0.3181 0.2944 0.3157 0.0471  0.0265  0.0361  225 MET A C   
1861 O O   . MET A 223 ? 0.3462 0.3162 0.3458 0.0506  0.0320  0.0405  225 MET A O   
1862 C CB  . MET A 223 ? 0.3537 0.3340 0.3542 0.0395  0.0205  0.0294  225 MET A CB  
1863 C CG  . MET A 223 ? 0.4101 0.3849 0.4123 0.0346  0.0172  0.0231  225 MET A CG  
1864 S SD  . MET A 223 ? 0.5607 0.5462 0.5657 0.0324  0.0152  0.0228  225 MET A SD  
1865 C CE  . MET A 223 ? 0.6288 0.6288 0.6303 0.0334  0.0131  0.0240  225 MET A CE  
1866 N N   . ILE A 224 ? 0.2964 0.2846 0.2919 0.0481  0.0244  0.0374  226 ILE A N   
1867 C CA  . ILE A 224 ? 0.2822 0.2785 0.2781 0.0540  0.0282  0.0449  226 ILE A CA  
1868 C C   . ILE A 224 ? 0.2790 0.2657 0.2734 0.0570  0.0314  0.0454  226 ILE A C   
1869 O O   . ILE A 224 ? 0.3317 0.3196 0.3276 0.0628  0.0365  0.0520  226 ILE A O   
1870 C CB  . ILE A 224 ? 0.2945 0.3088 0.2893 0.0540  0.0252  0.0462  226 ILE A CB  
1871 C CG1 . ILE A 224 ? 0.2858 0.3001 0.2773 0.0510  0.0216  0.0408  226 ILE A CG1 
1872 C CG2 . ILE A 224 ? 0.3389 0.3627 0.3348 0.0510  0.0226  0.0451  226 ILE A CG2 
1873 C CD1 . ILE A 224 ? 0.3061 0.3382 0.2970 0.0503  0.0192  0.0415  226 ILE A CD1 
1874 N N   . PHE A 225 ? 0.2760 0.2535 0.2674 0.0535  0.0289  0.0387  227 PHE A N   
1875 C CA  . PHE A 225 ? 0.3057 0.2742 0.2949 0.0560  0.0320  0.0384  227 PHE A CA  
1876 C C   . PHE A 225 ? 0.3260 0.2775 0.3157 0.0550  0.0352  0.0354  227 PHE A C   
1877 O O   . PHE A 225 ? 0.3699 0.3126 0.3579 0.0572  0.0387  0.0347  227 PHE A O   
1878 C CB  . PHE A 225 ? 0.3044 0.2740 0.2893 0.0532  0.0279  0.0333  227 PHE A CB  
1879 C CG  . PHE A 225 ? 0.2960 0.2812 0.2805 0.0540  0.0259  0.0358  227 PHE A CG  
1880 C CD1 . PHE A 225 ? 0.2700 0.2661 0.2569 0.0594  0.0293  0.0430  227 PHE A CD1 
1881 C CD2 . PHE A 225 ? 0.2696 0.2593 0.2518 0.0493  0.0209  0.0311  227 PHE A CD2 
1882 C CE1 . PHE A 225 ? 0.3359 0.3481 0.3229 0.0594  0.0272  0.0446  227 PHE A CE1 
1883 C CE2 . PHE A 225 ? 0.2872 0.2912 0.2694 0.0491  0.0194  0.0325  227 PHE A CE2 
1884 C CZ  . PHE A 225 ? 0.2931 0.3090 0.2778 0.0539  0.0223  0.0390  227 PHE A CZ  
1885 N N   . ARG A 226 ? 0.3287 0.2757 0.3208 0.0516  0.0342  0.0330  228 ARG A N   
1886 C CA  . ARG A 226 ? 0.3662 0.2981 0.3596 0.0497  0.0373  0.0295  228 ARG A CA  
1887 C C   . ARG A 226 ? 0.4240 0.3472 0.4128 0.0463  0.0348  0.0219  228 ARG A C   
1888 O O   . ARG A 226 ? 0.4212 0.3331 0.4089 0.0471  0.0390  0.0200  228 ARG A O   
1889 C CB  . ARG A 226 ? 0.4591 0.3841 0.4553 0.0549  0.0455  0.0353  228 ARG A CB  
1890 C CG  . ARG A 226 ? 0.5686 0.5035 0.5685 0.0595  0.0484  0.0442  228 ARG A CG  
1891 C CD  . ARG A 226 ? 0.7218 0.6593 0.7248 0.0558  0.0464  0.0436  228 ARG A CD  
1892 N NE  . ARG A 226 ? 0.8801 0.8036 0.8852 0.0513  0.0480  0.0382  228 ARG A NE  
1893 C CZ  . ARG A 226 ? 0.9788 0.8900 0.9869 0.0528  0.0552  0.0401  228 ARG A CZ  
1894 N NH1 . ARG A 226 ? 1.0264 0.9366 1.0357 0.0596  0.0618  0.0480  228 ARG A NH1 
1895 N NH2 . ARG A 226 ? 0.9940 0.8939 1.0042 0.0475  0.0560  0.0340  228 ARG A NH2 
1896 N N   . LYS A 227 ? 0.3451 0.2736 0.3311 0.0427  0.0283  0.0176  229 LYS A N   
1897 C CA  . LYS A 227 ? 0.3788 0.3007 0.3599 0.0395  0.0253  0.0109  229 LYS A CA  
1898 C C   . LYS A 227 ? 0.4058 0.3309 0.3872 0.0347  0.0189  0.0064  229 LYS A C   
1899 O O   . LYS A 227 ? 0.3674 0.3015 0.3481 0.0343  0.0151  0.0072  229 LYS A O   
1900 C CB  . LYS A 227 ? 0.3835 0.3092 0.3599 0.0418  0.0247  0.0118  229 LYS A CB  
1901 C CG  . LYS A 227 ? 0.4237 0.3430 0.3944 0.0390  0.0220  0.0055  229 LYS A CG  
1902 C CD  . LYS A 227 ? 0.4299 0.3536 0.3960 0.0409  0.0215  0.0066  229 LYS A CD  
1903 C CE  . LYS A 227 ? 0.4582 0.3744 0.4179 0.0387  0.0200  0.0009  229 LYS A CE  
1904 N NZ  . LYS A 227 ? 0.4388 0.3557 0.3968 0.0343  0.0138  -0.0036 229 LYS A NZ  
1905 N N   . GLU A 228 ? 0.4400 0.3579 0.4226 0.0311  0.0181  0.0015  230 GLU A N   
1906 C CA  . GLU A 228 ? 0.5267 0.4484 0.5108 0.0271  0.0125  -0.0021 230 GLU A CA  
1907 C C   . GLU A 228 ? 0.4871 0.4036 0.4673 0.0239  0.0090  -0.0086 230 GLU A C   
1908 O O   . GLU A 228 ? 0.5535 0.4618 0.5336 0.0222  0.0113  -0.0122 230 GLU A O   
1909 C CB  . GLU A 228 ? 0.6245 0.5458 0.6153 0.0256  0.0143  -0.0013 230 GLU A CB  
1910 C CG  . GLU A 228 ? 0.7102 0.6399 0.7039 0.0236  0.0098  -0.0017 230 GLU A CG  
1911 C CD  . GLU A 228 ? 0.7395 0.6683 0.7326 0.0197  0.0044  -0.0078 230 GLU A CD  
1912 O OE1 . GLU A 228 ? 0.6920 0.6273 0.6850 0.0191  0.0001  -0.0084 230 GLU A OE1 
1913 O OE2 . GLU A 228 ? 0.7333 0.6552 0.7262 0.0173  0.0048  -0.0121 230 GLU A OE2 
1914 N N   . PRO A 229 ? 0.4084 0.3295 0.3851 0.0229  0.0037  -0.0103 231 PRO A N   
1915 C CA  . PRO A 229 ? 0.3284 0.2579 0.3049 0.0243  0.0016  -0.0069 231 PRO A CA  
1916 C C   . PRO A 229 ? 0.3669 0.2977 0.3393 0.0274  0.0039  -0.0038 231 PRO A C   
1917 O O   . PRO A 229 ? 0.3696 0.2943 0.3385 0.0285  0.0064  -0.0048 231 PRO A O   
1918 C CB  . PRO A 229 ? 0.3576 0.2888 0.3319 0.0220  -0.0041 -0.0105 231 PRO A CB  
1919 C CG  . PRO A 229 ? 0.4197 0.3444 0.3893 0.0210  -0.0048 -0.0145 231 PRO A CG  
1920 C CD  . PRO A 229 ? 0.4595 0.3778 0.4319 0.0203  -0.0004 -0.0157 231 PRO A CD  
1921 N N   . PHE A 230 ? 0.2903 0.2294 0.2634 0.0286  0.0033  -0.0005 232 PHE A N   
1922 C CA  . PHE A 230 ? 0.2837 0.2258 0.2539 0.0314  0.0057  0.0026  232 PHE A CA  
1923 C C   . PHE A 230 ? 0.2882 0.2278 0.2523 0.0305  0.0035  0.0001  232 PHE A C   
1924 O O   . PHE A 230 ? 0.3022 0.2378 0.2626 0.0323  0.0061  0.0002  232 PHE A O   
1925 C CB  . PHE A 230 ? 0.2943 0.2475 0.2673 0.0322  0.0058  0.0064  232 PHE A CB  
1926 C CG  . PHE A 230 ? 0.2686 0.2272 0.2401 0.0351  0.0085  0.0099  232 PHE A CG  
1927 C CD1 . PHE A 230 ? 0.2518 0.2099 0.2247 0.0390  0.0132  0.0139  232 PHE A CD1 
1928 C CD2 . PHE A 230 ? 0.2706 0.2346 0.2395 0.0339  0.0066  0.0095  232 PHE A CD2 
1929 C CE1 . PHE A 230 ? 0.2907 0.2547 0.2627 0.0422  0.0158  0.0175  232 PHE A CE1 
1930 C CE2 . PHE A 230 ? 0.3167 0.2869 0.2849 0.0363  0.0092  0.0126  232 PHE A CE2 
1931 C CZ  . PHE A 230 ? 0.3720 0.3428 0.3419 0.0406  0.0136  0.0167  232 PHE A CZ  
1932 N N   . PHE A 231 ? 0.2705 0.2122 0.2335 0.0282  -0.0007 -0.0019 233 PHE A N   
1933 C CA  . PHE A 231 ? 0.2905 0.2295 0.2476 0.0275  -0.0028 -0.0037 233 PHE A CA  
1934 C C   . PHE A 231 ? 0.3086 0.2413 0.2636 0.0259  -0.0056 -0.0078 233 PHE A C   
1935 O O   . PHE A 231 ? 0.2953 0.2293 0.2526 0.0241  -0.0090 -0.0093 233 PHE A O   
1936 C CB  . PHE A 231 ? 0.2774 0.2216 0.2346 0.0261  -0.0051 -0.0031 233 PHE A CB  
1937 C CG  . PHE A 231 ? 0.2581 0.2103 0.2174 0.0267  -0.0028 0.0000  233 PHE A CG  
1938 C CD1 . PHE A 231 ? 0.2877 0.2415 0.2442 0.0283  -0.0001 0.0019  233 PHE A CD1 
1939 C CD2 . PHE A 231 ? 0.2495 0.2086 0.2134 0.0255  -0.0035 0.0006  233 PHE A CD2 
1940 C CE1 . PHE A 231 ? 0.2686 0.2318 0.2274 0.0286  0.0016  0.0045  233 PHE A CE1 
1941 C CE2 . PHE A 231 ? 0.2466 0.2148 0.2123 0.0255  -0.0017 0.0028  233 PHE A CE2 
1942 C CZ  . PHE A 231 ? 0.2482 0.2188 0.2114 0.0269  0.0007  0.0048  233 PHE A CZ  
1943 N N   . HIS A 232 ? 0.3356 0.2623 0.2864 0.0264  -0.0040 -0.0098 234 HIS A N   
1944 C CA  . HIS A 232 ? 0.3429 0.2646 0.2923 0.0244  -0.0060 -0.0143 234 HIS A CA  
1945 C C   . HIS A 232 ? 0.3598 0.2800 0.3017 0.0239  -0.0089 -0.0166 234 HIS A C   
1946 O O   . HIS A 232 ? 0.3929 0.3085 0.3295 0.0241  -0.0073 -0.0190 234 HIS A O   
1947 C CB  . HIS A 232 ? 0.3944 0.3102 0.3449 0.0248  -0.0015 -0.0158 234 HIS A CB  
1948 C CG  . HIS A 232 ? 0.5110 0.4228 0.4630 0.0218  -0.0028 -0.0207 234 HIS A CG  
1949 N ND1 . HIS A 232 ? 0.5959 0.5017 0.5508 0.0212  0.0015  -0.0225 234 HIS A ND1 
1950 C CD2 . HIS A 232 ? 0.5676 0.4813 0.5192 0.0190  -0.0078 -0.0243 234 HIS A CD2 
1951 C CE1 . HIS A 232 ? 0.6163 0.5203 0.5724 0.0176  -0.0008 -0.0276 234 HIS A CE1 
1952 N NE2 . HIS A 232 ? 0.5576 0.4672 0.5118 0.0163  -0.0067 -0.0287 234 HIS A NE2 
1953 N N   . GLY A 233 ? 0.3142 0.2381 0.2556 0.0234  -0.0128 -0.0157 235 GLY A N   
1954 C CA  . GLY A 233 ? 0.3013 0.2244 0.2355 0.0236  -0.0154 -0.0164 235 GLY A CA  
1955 C C   . GLY A 233 ? 0.3263 0.2486 0.2585 0.0219  -0.0190 -0.0207 235 GLY A C   
1956 O O   . GLY A 233 ? 0.3484 0.2723 0.2862 0.0203  -0.0208 -0.0227 235 GLY A O   
1957 N N   . HIS A 234 ? 0.3510 0.2719 0.2751 0.0222  -0.0200 -0.0223 236 HIS A N   
1958 C CA  A HIS A 234 ? 0.3539 0.2761 0.2755 0.0204  -0.0239 -0.0266 236 HIS A CA  
1959 C CA  B HIS A 234 ? 0.3568 0.2790 0.2777 0.0205  -0.0239 -0.0265 236 HIS A CA  
1960 C C   . HIS A 234 ? 0.3903 0.3177 0.3114 0.0212  -0.0291 -0.0247 236 HIS A C   
1961 O O   . HIS A 234 ? 0.4233 0.3545 0.3445 0.0198  -0.0331 -0.0278 236 HIS A O   
1962 C CB  A HIS A 234 ? 0.4105 0.3296 0.3232 0.0200  -0.0227 -0.0302 236 HIS A CB  
1963 C CB  B HIS A 234 ? 0.3791 0.2985 0.2902 0.0207  -0.0227 -0.0290 236 HIS A CB  
1964 C CG  A HIS A 234 ? 0.3899 0.3091 0.2943 0.0223  -0.0224 -0.0271 236 HIS A CG  
1965 C CG  B HIS A 234 ? 0.4287 0.3422 0.3393 0.0207  -0.0170 -0.0309 236 HIS A CG  
1966 N ND1 A HIS A 234 ? 0.4333 0.3486 0.3336 0.0237  -0.0175 -0.0262 236 HIS A ND1 
1967 N ND1 B HIS A 234 ? 0.4930 0.4034 0.4102 0.0193  -0.0143 -0.0330 236 HIS A ND1 
1968 C CD2 A HIS A 234 ? 0.4526 0.3753 0.3521 0.0236  -0.0259 -0.0247 236 HIS A CD2 
1969 C CD2 B HIS A 234 ? 0.4687 0.3787 0.3731 0.0222  -0.0131 -0.0306 236 HIS A CD2 
1970 C CE1 A HIS A 234 ? 0.4401 0.3565 0.3333 0.0253  -0.0181 -0.0234 236 HIS A CE1 
1971 C CE1 B HIS A 234 ? 0.4760 0.3808 0.3913 0.0203  -0.0088 -0.0337 236 HIS A CE1 
1972 N NE2 A HIS A 234 ? 0.4119 0.3324 0.3043 0.0253  -0.0231 -0.0223 236 HIS A NE2 
1973 N NE2 B HIS A 234 ? 0.4946 0.3994 0.4022 0.0221  -0.0080 -0.0325 236 HIS A NE2 
1974 N N   . ASP A 235 ? 0.3291 0.2573 0.2506 0.0232  -0.0289 -0.0198 237 ASP A N   
1975 C CA  . ASP A 235 ? 0.3549 0.2868 0.2774 0.0246  -0.0327 -0.0171 237 ASP A CA  
1976 C C   . ASP A 235 ? 0.3546 0.2852 0.2801 0.0258  -0.0301 -0.0126 237 ASP A C   
1977 O O   . ASP A 235 ? 0.3171 0.2457 0.2439 0.0253  -0.0261 -0.0120 237 ASP A O   
1978 C CB  . ASP A 235 ? 0.3426 0.2763 0.2563 0.0260  -0.0357 -0.0166 237 ASP A CB  
1979 C CG  . ASP A 235 ? 0.4390 0.3690 0.3445 0.0274  -0.0325 -0.0140 237 ASP A CG  
1980 O OD1 . ASP A 235 ? 0.3902 0.3173 0.2974 0.0278  -0.0288 -0.0112 237 ASP A OD1 
1981 O OD2 . ASP A 235 ? 0.4946 0.4255 0.3915 0.0280  -0.0339 -0.0149 237 ASP A OD2 
1982 N N   . ASN A 236 ? 0.3272 0.2593 0.2542 0.0273  -0.0321 -0.0096 238 ASN A N   
1983 C CA  . ASN A 236 ? 0.3283 0.2590 0.2592 0.0275  -0.0293 -0.0066 238 ASN A CA  
1984 C C   . ASN A 236 ? 0.3413 0.2688 0.2666 0.0278  -0.0257 -0.0041 238 ASN A C   
1985 O O   . ASN A 236 ? 0.3767 0.3039 0.3054 0.0269  -0.0225 -0.0031 238 ASN A O   
1986 C CB  . ASN A 236 ? 0.3243 0.2561 0.2585 0.0291  -0.0314 -0.0042 238 ASN A CB  
1987 C CG  . ASN A 236 ? 0.4256 0.3614 0.3674 0.0287  -0.0341 -0.0064 238 ASN A CG  
1988 O OD1 . ASN A 236 ? 0.3858 0.3230 0.3319 0.0266  -0.0334 -0.0093 238 ASN A OD1 
1989 N ND2 . ASN A 236 ? 0.4141 0.3521 0.3579 0.0308  -0.0370 -0.0047 238 ASN A ND2 
1990 N N   . TYR A 237 ? 0.3058 0.2320 0.2228 0.0290  -0.0261 -0.0035 239 TYR A N   
1991 C CA  . TYR A 237 ? 0.3214 0.2449 0.2333 0.0291  -0.0222 -0.0012 239 TYR A CA  
1992 C C   . TYR A 237 ? 0.3372 0.2608 0.2498 0.0279  -0.0190 -0.0034 239 TYR A C   
1993 O O   . TYR A 237 ? 0.2982 0.2221 0.2130 0.0273  -0.0154 -0.0019 239 TYR A O   
1994 C CB  . TYR A 237 ? 0.3445 0.2670 0.2468 0.0309  -0.0233 0.0004  239 TYR A CB  
1995 C CG  . TYR A 237 ? 0.4197 0.3430 0.3215 0.0330  -0.0266 0.0033  239 TYR A CG  
1996 C CD1 . TYR A 237 ? 0.4165 0.3436 0.3160 0.0342  -0.0313 0.0018  239 TYR A CD1 
1997 C CD2 . TYR A 237 ? 0.4820 0.4026 0.3863 0.0338  -0.0246 0.0075  239 TYR A CD2 
1998 C CE1 . TYR A 237 ? 0.5072 0.4362 0.4067 0.0368  -0.0342 0.0052  239 TYR A CE1 
1999 C CE2 . TYR A 237 ? 0.5698 0.4905 0.4742 0.0365  -0.0270 0.0108  239 TYR A CE2 
2000 C CZ  . TYR A 237 ? 0.5938 0.5191 0.4958 0.0384  -0.0319 0.0100  239 TYR A CZ  
2001 O OH  . TYR A 237 ? 0.6378 0.5644 0.5403 0.0418  -0.0342 0.0141  239 TYR A OH  
2002 N N   . ASP A 238 ? 0.3162 0.2397 0.2273 0.0276  -0.0201 -0.0070 240 ASP A N   
2003 C CA  . ASP A 238 ? 0.3069 0.2296 0.2192 0.0272  -0.0165 -0.0086 240 ASP A CA  
2004 C C   . ASP A 238 ? 0.3116 0.2365 0.2327 0.0264  -0.0149 -0.0080 240 ASP A C   
2005 O O   . ASP A 238 ? 0.3077 0.2334 0.2304 0.0267  -0.0112 -0.0071 240 ASP A O   
2006 C CB  . ASP A 238 ? 0.3214 0.2424 0.2312 0.0266  -0.0175 -0.0132 240 ASP A CB  
2007 C CG  . ASP A 238 ? 0.3765 0.2950 0.2868 0.0268  -0.0130 -0.0146 240 ASP A CG  
2008 O OD1 . ASP A 238 ? 0.3872 0.3047 0.2933 0.0280  -0.0095 -0.0130 240 ASP A OD1 
2009 O OD2 . ASP A 238 ? 0.3688 0.2864 0.2841 0.0259  -0.0124 -0.0170 240 ASP A OD2 
2010 N N   . GLN A 239 ? 0.2981 0.2250 0.2249 0.0256  -0.0176 -0.0082 241 GLN A N   
2011 C CA  . GLN A 239 ? 0.2657 0.1957 0.2003 0.0248  -0.0161 -0.0075 241 GLN A CA  
2012 C C   . GLN A 239 ? 0.2696 0.2017 0.2047 0.0247  -0.0131 -0.0047 241 GLN A C   
2013 O O   . GLN A 239 ? 0.2701 0.2055 0.2087 0.0245  -0.0104 -0.0040 241 GLN A O   
2014 C CB  . GLN A 239 ? 0.2306 0.1623 0.1706 0.0242  -0.0193 -0.0081 241 GLN A CB  
2015 C CG  . GLN A 239 ? 0.2630 0.1983 0.2106 0.0232  -0.0179 -0.0080 241 GLN A CG  
2016 C CD  . GLN A 239 ? 0.2563 0.1917 0.2064 0.0231  -0.0164 -0.0093 241 GLN A CD  
2017 O OE1 . GLN A 239 ? 0.2910 0.2233 0.2388 0.0231  -0.0172 -0.0116 241 GLN A OE1 
2018 N NE2 . GLN A 239 ? 0.2468 0.1859 0.2017 0.0230  -0.0139 -0.0079 241 GLN A NE2 
2019 N N   . LEU A 240 ? 0.2661 0.1968 0.1980 0.0246  -0.0134 -0.0030 242 LEU A N   
2020 C CA  . LEU A 240 ? 0.2670 0.2000 0.1998 0.0236  -0.0102 -0.0010 242 LEU A CA  
2021 C C   . LEU A 240 ? 0.2585 0.1924 0.1879 0.0243  -0.0069 -0.0002 242 LEU A C   
2022 O O   . LEU A 240 ? 0.2689 0.2077 0.2015 0.0235  -0.0041 0.0008  242 LEU A O   
2023 C CB  . LEU A 240 ? 0.2577 0.1875 0.1880 0.0232  -0.0104 0.0008  242 LEU A CB  
2024 C CG  . LEU A 240 ? 0.2716 0.2033 0.2038 0.0211  -0.0068 0.0021  242 LEU A CG  
2025 C CD1 . LEU A 240 ? 0.2778 0.2150 0.2177 0.0189  -0.0062 0.0006  242 LEU A CD1 
2026 C CD2 . LEU A 240 ? 0.3009 0.2276 0.2306 0.0208  -0.0062 0.0042  242 LEU A CD2 
2027 N N   . VAL A 241 ? 0.2677 0.1978 0.1906 0.0258  -0.0072 -0.0008 243 VAL A N   
2028 C CA  . VAL A 241 ? 0.2766 0.2073 0.1964 0.0269  -0.0036 -0.0003 243 VAL A CA  
2029 C C   . VAL A 241 ? 0.2693 0.2031 0.1943 0.0277  -0.0016 -0.0008 243 VAL A C   
2030 O O   . VAL A 241 ? 0.2793 0.2173 0.2059 0.0284  0.0018  0.0010  243 VAL A O   
2031 C CB  . VAL A 241 ? 0.3129 0.2388 0.2243 0.0283  -0.0041 -0.0016 243 VAL A CB  
2032 C CG1 . VAL A 241 ? 0.3153 0.2415 0.2237 0.0297  0.0003  -0.0012 243 VAL A CG1 
2033 C CG2 . VAL A 241 ? 0.3418 0.2654 0.2475 0.0282  -0.0058 0.0000  243 VAL A CG2 
2034 N N   . ARG A 242 ? 0.2670 0.1995 0.1952 0.0277  -0.0036 -0.0027 244 ARG A N   
2035 C CA  . ARG A 242 ? 0.2704 0.2053 0.2038 0.0288  -0.0012 -0.0024 244 ARG A CA  
2036 C C   . ARG A 242 ? 0.2775 0.2202 0.2167 0.0282  -0.0001 0.0001  244 ARG A C   
2037 O O   . ARG A 242 ? 0.3072 0.2546 0.2492 0.0299  0.0031  0.0022  244 ARG A O   
2038 C CB  . ARG A 242 ? 0.3213 0.2533 0.2577 0.0283  -0.0033 -0.0048 244 ARG A CB  
2039 C CG  . ARG A 242 ? 0.3953 0.3211 0.3267 0.0280  -0.0049 -0.0083 244 ARG A CG  
2040 C CD  . ARG A 242 ? 0.4398 0.3617 0.3667 0.0297  -0.0011 -0.0091 244 ARG A CD  
2041 N NE  . ARG A 242 ? 0.5752 0.4915 0.4975 0.0287  -0.0024 -0.0136 244 ARG A NE  
2042 C CZ  . ARG A 242 ? 0.7152 0.6270 0.6388 0.0286  0.0000  -0.0164 244 ARG A CZ  
2043 N NH1 . ARG A 242 ? 0.7637 0.6754 0.6929 0.0303  0.0041  -0.0143 244 ARG A NH1 
2044 N NH2 . ARG A 242 ? 0.7417 0.6492 0.6609 0.0269  -0.0014 -0.0214 244 ARG A NH2 
2045 N N   . ILE A 243 ? 0.2466 0.1915 0.1880 0.0260  -0.0024 0.0000  245 ILE A N   
2046 C CA  . ILE A 243 ? 0.2092 0.1622 0.1557 0.0247  -0.0013 0.0013  245 ILE A CA  
2047 C C   . ILE A 243 ? 0.2387 0.1963 0.1838 0.0245  0.0016  0.0032  245 ILE A C   
2048 O O   . ILE A 243 ? 0.2494 0.2154 0.1982 0.0249  0.0037  0.0048  245 ILE A O   
2049 C CB  . ILE A 243 ? 0.2284 0.1814 0.1773 0.0221  -0.0039 0.0000  245 ILE A CB  
2050 C CG1 . ILE A 243 ? 0.2264 0.1771 0.1782 0.0224  -0.0064 -0.0016 245 ILE A CG1 
2051 C CG2 . ILE A 243 ? 0.2576 0.2192 0.2108 0.0199  -0.0023 0.0004  245 ILE A CG2 
2052 C CD1 . ILE A 243 ? 0.2262 0.1752 0.1798 0.0207  -0.0090 -0.0030 245 ILE A CD1 
2053 N N   . ALA A 244 ? 0.2356 0.1885 0.1753 0.0240  0.0018  0.0031  246 ALA A N   
2054 C CA  . ALA A 244 ? 0.2588 0.2158 0.1973 0.0234  0.0048  0.0047  246 ALA A CA  
2055 C C   . ALA A 244 ? 0.2945 0.2548 0.2326 0.0263  0.0080  0.0064  246 ALA A C   
2056 O O   . ALA A 244 ? 0.2744 0.2423 0.2144 0.0260  0.0107  0.0080  246 ALA A O   
2057 C CB  . ALA A 244 ? 0.2656 0.2160 0.1980 0.0226  0.0047  0.0048  246 ALA A CB  
2058 N N   . LYS A 245 ? 0.2666 0.2216 0.2027 0.0292  0.0080  0.0057  247 LYS A N   
2059 C CA  . LYS A 245 ? 0.2654 0.2227 0.2018 0.0325  0.0118  0.0075  247 LYS A CA  
2060 C C   . LYS A 245 ? 0.2659 0.2330 0.2095 0.0338  0.0132  0.0099  247 LYS A C   
2061 O O   . LYS A 245 ? 0.3046 0.2765 0.2497 0.0369  0.0167  0.0125  247 LYS A O   
2062 C CB  . LYS A 245 ? 0.2862 0.2343 0.2188 0.0348  0.0122  0.0055  247 LYS A CB  
2063 C CG  . LYS A 245 ? 0.3232 0.2639 0.2476 0.0343  0.0115  0.0034  247 LYS A CG  
2064 C CD  . LYS A 245 ? 0.3961 0.3286 0.3169 0.0358  0.0120  0.0005  247 LYS A CD  
2065 C CE  . LYS A 245 ? 0.5103 0.4373 0.4221 0.0354  0.0115  -0.0017 247 LYS A CE  
2066 N NZ  . LYS A 245 ? 0.6210 0.5406 0.5287 0.0360  0.0119  -0.0058 247 LYS A NZ  
2067 N N   . VAL A 246 ? 0.2496 0.2205 0.1975 0.0318  0.0107  0.0095  248 VAL A N   
2068 C CA  . VAL A 246 ? 0.2422 0.2239 0.1964 0.0328  0.0116  0.0120  248 VAL A CA  
2069 C C   . VAL A 246 ? 0.2486 0.2412 0.2057 0.0294  0.0110  0.0120  248 VAL A C   
2070 O O   . VAL A 246 ? 0.2624 0.2667 0.2228 0.0303  0.0131  0.0145  248 VAL A O   
2071 C CB  . VAL A 246 ? 0.2275 0.2065 0.1845 0.0330  0.0097  0.0113  248 VAL A CB  
2072 C CG1 . VAL A 246 ? 0.2622 0.2532 0.2249 0.0343  0.0108  0.0144  248 VAL A CG1 
2073 C CG2 . VAL A 246 ? 0.2641 0.2323 0.2188 0.0357  0.0108  0.0107  248 VAL A CG2 
2074 N N   . LEU A 247 ? 0.2220 0.2115 0.1783 0.0252  0.0085  0.0091  249 LEU A N   
2075 C CA  A LEU A 247 ? 0.2228 0.2213 0.1820 0.0211  0.0085  0.0081  249 LEU A CA  
2076 C CA  B LEU A 247 ? 0.2258 0.2241 0.1850 0.0210  0.0084  0.0080  249 LEU A CA  
2077 C C   . LEU A 247 ? 0.2373 0.2366 0.1943 0.0192  0.0105  0.0081  249 LEU A C   
2078 O O   . LEU A 247 ? 0.2487 0.2572 0.2088 0.0155  0.0115  0.0073  249 LEU A O   
2079 C CB  A LEU A 247 ? 0.2292 0.2233 0.1892 0.0176  0.0058  0.0049  249 LEU A CB  
2080 C CB  B LEU A 247 ? 0.2329 0.2262 0.1926 0.0176  0.0057  0.0048  249 LEU A CB  
2081 C CG  A LEU A 247 ? 0.2023 0.2019 0.1666 0.0175  0.0043  0.0044  249 LEU A CG  
2082 C CG  B LEU A 247 ? 0.2236 0.2171 0.1861 0.0186  0.0037  0.0044  249 LEU A CG  
2083 C CD1 A LEU A 247 ? 0.2444 0.2384 0.2083 0.0217  0.0037  0.0060  249 LEU A CD1 
2084 C CD1 B LEU A 247 ? 0.2298 0.2200 0.1935 0.0150  0.0017  0.0011  249 LEU A CD1 
2085 C CD2 A LEU A 247 ? 0.2252 0.2216 0.1906 0.0137  0.0024  0.0009  249 LEU A CD2 
2086 C CD2 B LEU A 247 ? 0.2247 0.2317 0.1916 0.0198  0.0049  0.0065  249 LEU A CD2 
2087 N N   . GLY A 248 ? 0.2390 0.2294 0.1907 0.0213  0.0116  0.0088  250 GLY A N   
2088 C CA  . GLY A 248 ? 0.2466 0.2374 0.1958 0.0200  0.0141  0.0094  250 GLY A CA  
2089 C C   . GLY A 248 ? 0.2672 0.2499 0.2132 0.0164  0.0133  0.0077  250 GLY A C   
2090 O O   . GLY A 248 ? 0.2773 0.2574 0.2250 0.0139  0.0112  0.0057  250 GLY A O   
2091 N N   . THR A 249 ? 0.2609 0.2393 0.2022 0.0164  0.0155  0.0087  251 THR A N   
2092 C CA  . THR A 249 ? 0.2382 0.2080 0.1759 0.0138  0.0153  0.0081  251 THR A CA  
2093 C C   . THR A 249 ? 0.2386 0.2136 0.1805 0.0085  0.0176  0.0072  251 THR A C   
2094 O O   . THR A 249 ? 0.2869 0.2549 0.2280 0.0058  0.0174  0.0063  251 THR A O   
2095 C CB  . THR A 249 ? 0.2618 0.2244 0.1919 0.0161  0.0169  0.0099  251 THR A CB  
2096 O OG1 . THR A 249 ? 0.2897 0.2595 0.2203 0.0172  0.0204  0.0114  251 THR A OG1 
2097 C CG2 . THR A 249 ? 0.2990 0.2539 0.2243 0.0200  0.0141  0.0094  251 THR A CG2 
2098 N N   . GLU A 250 ? 0.2487 0.2360 0.1951 0.0067  0.0200  0.0074  252 GLU A N   
2099 C CA  . GLU A 250 ? 0.2777 0.2702 0.2283 0.0007  0.0223  0.0057  252 GLU A CA  
2100 C C   . GLU A 250 ? 0.2435 0.2365 0.1982 -0.0027 0.0204  0.0023  252 GLU A C   
2101 O O   . GLU A 250 ? 0.2979 0.2863 0.2536 -0.0073 0.0219  0.0003  252 GLU A O   
2102 C CB  . GLU A 250 ? 0.2880 0.2960 0.2433 -0.0007 0.0249  0.0062  252 GLU A CB  
2103 C CG  . GLU A 250 ? 0.3498 0.3568 0.3013 0.0017  0.0280  0.0091  252 GLU A CG  
2104 C CD  . GLU A 250 ? 0.5905 0.5897 0.5391 -0.0022 0.0312  0.0092  252 GLU A CD  
2105 O OE1 . GLU A 250 ? 0.7060 0.7132 0.6592 -0.0074 0.0343  0.0081  252 GLU A OE1 
2106 O OE2 . GLU A 250 ? 0.7010 0.6865 0.6428 -0.0001 0.0307  0.0106  252 GLU A OE2 
2107 N N   . ASP A 251 ? 0.2590 0.2569 0.2161 -0.0005 0.0174  0.0017  253 ASP A N   
2108 C CA  . ASP A 251 ? 0.2602 0.2590 0.2210 -0.0037 0.0158  -0.0016 253 ASP A CA  
2109 C C   . ASP A 251 ? 0.2430 0.2271 0.2005 -0.0025 0.0140  -0.0021 253 ASP A C   
2110 O O   . ASP A 251 ? 0.2537 0.2354 0.2139 -0.0059 0.0141  -0.0050 253 ASP A O   
2111 C CB  . ASP A 251 ? 0.2499 0.2602 0.2146 -0.0018 0.0137  -0.0018 253 ASP A CB  
2112 C CG  . ASP A 251 ? 0.3306 0.3585 0.2999 -0.0040 0.0154  -0.0018 253 ASP A CG  
2113 O OD1 . ASP A 251 ? 0.3211 0.3535 0.2927 -0.0097 0.0177  -0.0043 253 ASP A OD1 
2114 O OD2 . ASP A 251 ? 0.3248 0.3622 0.2957 -0.0001 0.0147  0.0008  253 ASP A OD2 
2115 N N   . LEU A 252 ? 0.2518 0.2267 0.2040 0.0021  0.0127  0.0005  254 LEU A N   
2116 C CA  . LEU A 252 ? 0.2344 0.1965 0.1832 0.0033  0.0110  0.0006  254 LEU A CA  
2117 C C   . LEU A 252 ? 0.2617 0.2171 0.2093 0.0000  0.0142  0.0008  254 LEU A C   
2118 O O   . LEU A 252 ? 0.2801 0.2287 0.2289 -0.0014 0.0142  -0.0004 254 LEU A O   
2119 C CB  . LEU A 252 ? 0.2494 0.2051 0.1922 0.0084  0.0090  0.0030  254 LEU A CB  
2120 C CG  . LEU A 252 ? 0.2692 0.2136 0.2080 0.0102  0.0070  0.0038  254 LEU A CG  
2121 C CD1 . LEU A 252 ? 0.2803 0.2234 0.2234 0.0097  0.0045  0.0017  254 LEU A CD1 
2122 C CD2 . LEU A 252 ? 0.2969 0.2376 0.2298 0.0145  0.0048  0.0052  254 LEU A CD2 
2123 N N   . TYR A 253 ? 0.2889 0.2461 0.2346 -0.0012 0.0174  0.0025  255 TYR A N   
2124 C CA  . TYR A 253 ? 0.2781 0.2287 0.2230 -0.0046 0.0212  0.0030  255 TYR A CA  
2125 C C   . TYR A 253 ? 0.2808 0.2355 0.2323 -0.0108 0.0236  -0.0011 255 TYR A C   
2126 O O   . TYR A 253 ? 0.2979 0.2437 0.2500 -0.0133 0.0259  -0.0017 255 TYR A O   
2127 C CB  . TYR A 253 ? 0.2976 0.2497 0.2390 -0.0046 0.0244  0.0057  255 TYR A CB  
2128 C CG  . TYR A 253 ? 0.3364 0.2791 0.2695 0.0004  0.0235  0.0095  255 TYR A CG  
2129 C CD1 . TYR A 253 ? 0.3609 0.2922 0.2901 0.0008  0.0247  0.0119  255 TYR A CD1 
2130 C CD2 . TYR A 253 ? 0.3776 0.3231 0.3067 0.0047  0.0217  0.0107  255 TYR A CD2 
2131 C CE1 . TYR A 253 ? 0.3884 0.3128 0.3095 0.0053  0.0236  0.0154  255 TYR A CE1 
2132 C CE2 . TYR A 253 ? 0.4044 0.3421 0.3254 0.0087  0.0208  0.0134  255 TYR A CE2 
2133 C CZ  . TYR A 253 ? 0.4075 0.3356 0.3244 0.0090  0.0214  0.0158  255 TYR A CZ  
2134 O OH  . TYR A 253 ? 0.4932 0.4153 0.4015 0.0130  0.0203  0.0185  255 TYR A OH  
2135 N N   . ASP A 254 ? 0.2709 0.2394 0.2276 -0.0134 0.0232  -0.0039 256 ASP A N   
2136 C CA  . ASP A 254 ? 0.3002 0.2738 0.2629 -0.0197 0.0250  -0.0088 256 ASP A CA  
2137 C C   . ASP A 254 ? 0.2657 0.2311 0.2294 -0.0192 0.0233  -0.0109 256 ASP A C   
2138 O O   . ASP A 254 ? 0.3030 0.2635 0.2694 -0.0238 0.0263  -0.0141 256 ASP A O   
2139 C CB  . ASP A 254 ? 0.3068 0.2984 0.2742 -0.0215 0.0238  -0.0110 256 ASP A CB  
2140 C CG  . ASP A 254 ? 0.3766 0.3789 0.3454 -0.0234 0.0264  -0.0099 256 ASP A CG  
2141 O OD1 . ASP A 254 ? 0.3928 0.4101 0.3645 -0.0226 0.0250  -0.0098 256 ASP A OD1 
2142 O OD2 . ASP A 254 ? 0.3700 0.3663 0.3371 -0.0255 0.0300  -0.0087 256 ASP A OD2 
2143 N N   . TYR A 255 ? 0.2490 0.2129 0.2108 -0.0138 0.0190  -0.0093 257 TYR A N   
2144 C CA  . TYR A 255 ? 0.2667 0.2243 0.2299 -0.0128 0.0172  -0.0111 257 TYR A CA  
2145 C C   . TYR A 255 ? 0.2928 0.2353 0.2535 -0.0119 0.0190  -0.0094 257 TYR A C   
2146 O O   . TYR A 255 ? 0.3107 0.2479 0.2745 -0.0148 0.0214  -0.0122 257 TYR A O   
2147 C CB  . TYR A 255 ? 0.2736 0.2330 0.2352 -0.0073 0.0124  -0.0093 257 TYR A CB  
2148 C CG  . TYR A 255 ? 0.2679 0.2213 0.2309 -0.0054 0.0102  -0.0105 257 TYR A CG  
2149 C CD1 . TYR A 255 ? 0.2615 0.2171 0.2292 -0.0090 0.0113  -0.0148 257 TYR A CD1 
2150 C CD2 . TYR A 255 ? 0.2866 0.2333 0.2464 -0.0002 0.0069  -0.0077 257 TYR A CD2 
2151 C CE1 . TYR A 255 ? 0.2787 0.2296 0.2482 -0.0071 0.0096  -0.0159 257 TYR A CE1 
2152 C CE2 . TYR A 255 ? 0.2749 0.2176 0.2368 0.0016  0.0048  -0.0087 257 TYR A CE2 
2153 C CZ  . TYR A 255 ? 0.3113 0.2559 0.2780 -0.0017 0.0063  -0.0126 257 TYR A CZ  
2154 O OH  . TYR A 255 ? 0.3176 0.2588 0.2868 0.0002  0.0046  -0.0136 257 TYR A OH  
2155 N N   . ILE A 256 ? 0.3116 0.2472 0.2666 -0.0077 0.0183  -0.0047 258 ILE A N   
2156 C CA  . ILE A 256 ? 0.3354 0.2576 0.2878 -0.0060 0.0199  -0.0021 258 ILE A CA  
2157 C C   . ILE A 256 ? 0.3488 0.2661 0.3028 -0.0111 0.0260  -0.0028 258 ILE A C   
2158 O O   . ILE A 256 ? 0.3771 0.2838 0.3320 -0.0113 0.0287  -0.0022 258 ILE A O   
2159 C CB  . ILE A 256 ? 0.3595 0.2766 0.3047 -0.0002 0.0174  0.0031  258 ILE A CB  
2160 C CG1 . ILE A 256 ? 0.3351 0.2551 0.2764 -0.0008 0.0195  0.0053  258 ILE A CG1 
2161 C CG2 . ILE A 256 ? 0.3438 0.2652 0.2882 0.0040  0.0118  0.0028  258 ILE A CG2 
2162 C CD1 . ILE A 256 ? 0.3555 0.2694 0.2888 0.0042  0.0181  0.0101  258 ILE A CD1 
2163 N N   . ASP A 257 ? 0.3009 0.2261 0.2562 -0.0155 0.0287  -0.0041 259 ASP A N   
2164 C CA  . ASP A 257 ? 0.2718 0.1929 0.2294 -0.0214 0.0349  -0.0054 259 ASP A CA  
2165 C C   . ASP A 257 ? 0.3482 0.2701 0.3125 -0.0270 0.0372  -0.0117 259 ASP A C   
2166 O O   . ASP A 257 ? 0.3611 0.2732 0.3273 -0.0306 0.0425  -0.0128 259 ASP A O   
2167 C CB  . ASP A 257 ? 0.3076 0.2387 0.2656 -0.0250 0.0371  -0.0055 259 ASP A CB  
2168 C CG  . ASP A 257 ? 0.3086 0.2362 0.2597 -0.0204 0.0370  0.0005  259 ASP A CG  
2169 O OD1 . ASP A 257 ? 0.3665 0.2835 0.3122 -0.0151 0.0356  0.0047  259 ASP A OD1 
2170 O OD2 . ASP A 257 ? 0.3730 0.3097 0.3242 -0.0220 0.0383  0.0008  259 ASP A OD2 
2171 N N   . LYS A 258 ? 0.3244 0.2577 0.2920 -0.0279 0.0338  -0.0158 260 LYS A N   
2172 C CA  . LYS A 258 ? 0.3905 0.3255 0.3638 -0.0332 0.0358  -0.0224 260 LYS A CA  
2173 C C   . LYS A 258 ? 0.3634 0.2834 0.3368 -0.0308 0.0371  -0.0220 260 LYS A C   
2174 O O   . LYS A 258 ? 0.3845 0.2981 0.3616 -0.0356 0.0421  -0.0261 260 LYS A O   
2175 C CB  . LYS A 258 ? 0.3089 0.2590 0.2846 -0.0333 0.0313  -0.0257 260 LYS A CB  
2176 C CG  . LYS A 258 ? 0.3048 0.2561 0.2851 -0.0374 0.0326  -0.0323 260 LYS A CG  
2177 C CD  . LYS A 258 ? 0.3186 0.2863 0.3008 -0.0376 0.0286  -0.0351 260 LYS A CD  
2178 C CE  . LYS A 258 ? 0.3386 0.3069 0.3246 -0.0414 0.0300  -0.0417 260 LYS A CE  
2179 N NZ  . LYS A 258 ? 0.3590 0.3426 0.3462 -0.0407 0.0260  -0.0437 260 LYS A NZ  
2180 N N   . TYR A 259 ? 0.3008 0.2153 0.2707 -0.0233 0.0330  -0.0172 261 TYR A N   
2181 C CA  . TYR A 259 ? 0.3730 0.2751 0.3435 -0.0199 0.0337  -0.0162 261 TYR A CA  
2182 C C   . TYR A 259 ? 0.4295 0.3177 0.3961 -0.0165 0.0365  -0.0099 261 TYR A C   
2183 O O   . TYR A 259 ? 0.4237 0.3018 0.3902 -0.0121 0.0368  -0.0074 261 TYR A O   
2184 C CB  . TYR A 259 ? 0.3551 0.2612 0.3251 -0.0143 0.0274  -0.0153 261 TYR A CB  
2185 C CG  . TYR A 259 ? 0.3303 0.2490 0.3044 -0.0176 0.0256  -0.0211 261 TYR A CG  
2186 C CD1 . TYR A 259 ? 0.3529 0.2704 0.3318 -0.0206 0.0279  -0.0264 261 TYR A CD1 
2187 C CD2 . TYR A 259 ? 0.3277 0.2597 0.3008 -0.0178 0.0222  -0.0211 261 TYR A CD2 
2188 C CE1 . TYR A 259 ? 0.3163 0.2464 0.2982 -0.0238 0.0263  -0.0317 261 TYR A CE1 
2189 C CE2 . TYR A 259 ? 0.3265 0.2708 0.3030 -0.0205 0.0207  -0.0256 261 TYR A CE2 
2190 C CZ  . TYR A 259 ? 0.3251 0.2689 0.3057 -0.0236 0.0226  -0.0309 261 TYR A CZ  
2191 O OH  . TYR A 259 ? 0.3194 0.2765 0.3026 -0.0261 0.0211  -0.0351 261 TYR A OH  
2192 N N   . ASN A 260 ? 0.3821 0.2701 0.3456 -0.0183 0.0390  -0.0073 262 ASN A N   
2193 C CA  . ASN A 260 ? 0.4353 0.3111 0.3943 -0.0151 0.0422  -0.0008 262 ASN A CA  
2194 C C   . ASN A 260 ? 0.3753 0.2475 0.3292 -0.0064 0.0369  0.0052  262 ASN A C   
2195 O O   . ASN A 260 ? 0.5076 0.3686 0.4599 -0.0023 0.0387  0.0098  262 ASN A O   
2196 C CB  . ASN A 260 ? 0.4658 0.3284 0.4286 -0.0183 0.0496  -0.0017 262 ASN A CB  
2197 C CG  . ASN A 260 ? 0.5633 0.4286 0.5304 -0.0278 0.0557  -0.0072 262 ASN A CG  
2198 O OD1 . ASN A 260 ? 0.5715 0.4498 0.5390 -0.0316 0.0540  -0.0100 262 ASN A OD1 
2199 N ND2 . ASN A 260 ? 0.6490 0.5022 0.6197 -0.0315 0.0630  -0.0090 262 ASN A ND2 
2200 N N   . ILE A 261 ? 0.4107 0.2934 0.3623 -0.0037 0.0304  0.0049  263 ILE A N   
2201 C CA  . ILE A 261 ? 0.4453 0.3281 0.3922 0.0034  0.0247  0.0090  263 ILE A CA  
2202 C C   . ILE A 261 ? 0.3911 0.2746 0.3306 0.0056  0.0241  0.0135  263 ILE A C   
2203 O O   . ILE A 261 ? 0.4327 0.3218 0.3716 0.0020  0.0260  0.0123  263 ILE A O   
2204 C CB  . ILE A 261 ? 0.4599 0.3529 0.4091 0.0042  0.0190  0.0052  263 ILE A CB  
2205 C CG1 . ILE A 261 ? 0.5567 0.4500 0.5128 0.0023  0.0194  0.0007  263 ILE A CG1 
2206 C CG2 . ILE A 261 ? 0.4751 0.3694 0.4195 0.0104  0.0132  0.0086  263 ILE A CG2 
2207 C CD1 . ILE A 261 ? 0.5481 0.4521 0.5065 0.0025  0.0147  -0.0028 263 ILE A CD1 
2208 N N   . GLU A 262 ? 0.4099 0.2890 0.3436 0.0116  0.0215  0.0187  264 GLU A N   
2209 C CA  . GLU A 262 ? 0.4662 0.3463 0.3919 0.0143  0.0204  0.0228  264 GLU A CA  
2210 C C   . GLU A 262 ? 0.4786 0.3652 0.4010 0.0183  0.0136  0.0223  264 GLU A C   
2211 O O   . GLU A 262 ? 0.4642 0.3504 0.3883 0.0215  0.0099  0.0223  264 GLU A O   
2212 C CB  . GLU A 262 ? 0.5319 0.4020 0.4527 0.0178  0.0233  0.0296  264 GLU A CB  
2213 C CG  . GLU A 262 ? 0.6421 0.5126 0.5538 0.0203  0.0232  0.0342  264 GLU A CG  
2214 C CD  . GLU A 262 ? 0.6061 0.4667 0.5145 0.0212  0.0291  0.0404  264 GLU A CD  
2215 O OE1 . GLU A 262 ? 0.6556 0.5163 0.5594 0.0196  0.0324  0.0425  264 GLU A OE1 
2216 O OE2 . GLU A 262 ? 0.5495 0.4020 0.4601 0.0237  0.0309  0.0435  264 GLU A OE2 
2217 N N   . LEU A 263 ? 0.4645 0.3573 0.3830 0.0180  0.0123  0.0215  265 LEU A N   
2218 C CA  . LEU A 263 ? 0.4580 0.3556 0.3731 0.0215  0.0066  0.0206  265 LEU A CA  
2219 C C   . LEU A 263 ? 0.4738 0.3676 0.3814 0.0265  0.0043  0.0252  265 LEU A C   
2220 O O   . LEU A 263 ? 0.4864 0.3751 0.3891 0.0276  0.0074  0.0299  265 LEU A O   
2221 C CB  . LEU A 263 ? 0.4374 0.3415 0.3501 0.0203  0.0066  0.0186  265 LEU A CB  
2222 C CG  . LEU A 263 ? 0.4372 0.3486 0.3567 0.0170  0.0068  0.0142  265 LEU A CG  
2223 C CD1 . LEU A 263 ? 0.4250 0.3418 0.3413 0.0170  0.0076  0.0137  265 LEU A CD1 
2224 C CD2 . LEU A 263 ? 0.4664 0.3803 0.3903 0.0181  0.0025  0.0114  265 LEU A CD2 
2225 N N   . ASP A 264 ? 0.4085 0.3056 0.3155 0.0294  -0.0012 0.0240  266 ASP A N   
2226 C CA  . ASP A 264 ? 0.4451 0.3421 0.3444 0.0339  -0.0045 0.0274  266 ASP A CA  
2227 C C   . ASP A 264 ? 0.4431 0.3406 0.3337 0.0340  -0.0027 0.0289  266 ASP A C   
2228 O O   . ASP A 264 ? 0.4198 0.3210 0.3104 0.0317  -0.0020 0.0253  266 ASP A O   
2229 C CB  . ASP A 264 ? 0.4649 0.3676 0.3655 0.0354  -0.0105 0.0239  266 ASP A CB  
2230 C CG  . ASP A 264 ? 0.4801 0.3844 0.3744 0.0399  -0.0147 0.0269  266 ASP A CG  
2231 O OD1 . ASP A 264 ? 0.4812 0.3843 0.3669 0.0418  -0.0139 0.0306  266 ASP A OD1 
2232 O OD2 . ASP A 264 ? 0.5144 0.4221 0.4123 0.0414  -0.0191 0.0255  266 ASP A OD2 
2233 N N   . PRO A 265 ? 0.4190 0.3130 0.3023 0.0368  -0.0014 0.0343  267 PRO A N   
2234 C CA  . PRO A 265 ? 0.3796 0.2746 0.2542 0.0369  0.0006  0.0357  267 PRO A CA  
2235 C C   . PRO A 265 ? 0.4312 0.3322 0.3009 0.0377  -0.0035 0.0316  267 PRO A C   
2236 O O   . PRO A 265 ? 0.4526 0.3550 0.3167 0.0370  -0.0014 0.0308  267 PRO A O   
2237 C CB  . PRO A 265 ? 0.4058 0.2964 0.2732 0.0407  0.0020  0.0429  267 PRO A CB  
2238 C CG  . PRO A 265 ? 0.4860 0.3754 0.3576 0.0437  -0.0012 0.0448  267 PRO A CG  
2239 C CD  . PRO A 265 ? 0.4652 0.3541 0.3479 0.0402  -0.0009 0.0401  267 PRO A CD  
2240 N N   . ARG A 266 ? 0.4314 0.3360 0.3033 0.0389  -0.0090 0.0286  268 ARG A N   
2241 C CA  . ARG A 266 ? 0.4653 0.3748 0.3329 0.0389  -0.0122 0.0240  268 ARG A CA  
2242 C C   . ARG A 266 ? 0.4319 0.3425 0.3037 0.0357  -0.0098 0.0193  268 ARG A C   
2243 O O   . ARG A 266 ? 0.4357 0.3486 0.3032 0.0356  -0.0104 0.0158  268 ARG A O   
2244 C CB  . ARG A 266 ? 0.6614 0.5749 0.5313 0.0403  -0.0182 0.0217  268 ARG A CB  
2245 C CG  . ARG A 266 ? 0.7770 0.6926 0.6554 0.0379  -0.0199 0.0161  268 ARG A CG  
2246 C CD  . ARG A 266 ? 0.8713 0.7915 0.7509 0.0392  -0.0258 0.0142  268 ARG A CD  
2247 N NE  . ARG A 266 ? 0.9218 0.8417 0.8037 0.0421  -0.0273 0.0190  268 ARG A NE  
2248 C CZ  . ARG A 266 ? 0.9676 0.8925 0.8481 0.0448  -0.0322 0.0199  268 ARG A CZ  
2249 N NH1 . ARG A 266 ? 0.9740 0.9050 0.8506 0.0443  -0.0363 0.0156  268 ARG A NH1 
2250 N NH2 . ARG A 266 ? 0.9682 0.8924 0.8515 0.0481  -0.0328 0.0250  268 ARG A NH2 
2251 N N   . PHE A 267 ? 0.3786 0.2880 0.2584 0.0332  -0.0067 0.0192  269 PHE A N   
2252 C CA  . PHE A 267 ? 0.3429 0.2548 0.2264 0.0308  -0.0040 0.0160  269 PHE A CA  
2253 C C   . PHE A 267 ? 0.4297 0.3414 0.3077 0.0305  0.0006  0.0176  269 PHE A C   
2254 O O   . PHE A 267 ? 0.4965 0.4110 0.3767 0.0293  0.0028  0.0153  269 PHE A O   
2255 C CB  . PHE A 267 ? 0.3717 0.2845 0.2653 0.0281  -0.0024 0.0151  269 PHE A CB  
2256 C CG  . PHE A 267 ? 0.3289 0.2433 0.2289 0.0280  -0.0062 0.0124  269 PHE A CG  
2257 C CD1 . PHE A 267 ? 0.3156 0.2278 0.2196 0.0283  -0.0076 0.0138  269 PHE A CD1 
2258 C CD2 . PHE A 267 ? 0.3502 0.2681 0.2527 0.0278  -0.0079 0.0086  269 PHE A CD2 
2259 C CE1 . PHE A 267 ? 0.3596 0.2738 0.2697 0.0283  -0.0108 0.0112  269 PHE A CE1 
2260 C CE2 . PHE A 267 ? 0.3553 0.2747 0.2638 0.0275  -0.0110 0.0063  269 PHE A CE2 
2261 C CZ  . PHE A 267 ? 0.3455 0.2636 0.2578 0.0277  -0.0126 0.0075  269 PHE A CZ  
2262 N N   . ASN A 268 ? 0.4753 0.3839 0.3465 0.0317  0.0023  0.0219  270 ASN A N   
2263 C CA  . ASN A 268 ? 0.5082 0.4168 0.3745 0.0312  0.0072  0.0237  270 ASN A CA  
2264 C C   . ASN A 268 ? 0.5337 0.4452 0.3948 0.0322  0.0072  0.0203  270 ASN A C   
2265 O O   . ASN A 268 ? 0.5957 0.5091 0.4569 0.0313  0.0115  0.0200  270 ASN A O   
2266 C CB  . ASN A 268 ? 0.5645 0.4691 0.4232 0.0329  0.0090  0.0294  270 ASN A CB  
2267 C CG  . ASN A 268 ? 0.5661 0.4662 0.4303 0.0315  0.0114  0.0332  270 ASN A CG  
2268 O OD1 . ASN A 268 ? 0.6782 0.5740 0.5376 0.0335  0.0125  0.0384  270 ASN A OD1 
2269 N ND2 . ASN A 268 ? 0.5433 0.4445 0.4174 0.0282  0.0125  0.0306  270 ASN A ND2 
2270 N N   . ASP A 269 ? 0.4849 0.3969 0.3417 0.0340  0.0029  0.0175  271 ASP A N   
2271 C CA  . ASP A 269 ? 0.5555 0.4689 0.4065 0.0349  0.0032  0.0137  271 ASP A CA  
2272 C C   . ASP A 269 ? 0.5691 0.4839 0.4265 0.0340  0.0020  0.0085  271 ASP A C   
2273 O O   . ASP A 269 ? 0.5972 0.5120 0.4506 0.0346  0.0028  0.0047  271 ASP A O   
2274 C CB  . ASP A 269 ? 0.7859 0.6995 0.6265 0.0369  -0.0003 0.0133  271 ASP A CB  
2275 C CG  . ASP A 269 ? 1.0147 0.9271 0.8474 0.0385  0.0014  0.0192  271 ASP A CG  
2276 O OD1 . ASP A 269 ? 1.0813 0.9943 0.9098 0.0404  -0.0024 0.0216  271 ASP A OD1 
2277 O OD2 . ASP A 269 ? 1.0747 0.9861 0.9059 0.0380  0.0067  0.0218  271 ASP A OD2 
2278 N N   . ILE A 270 ? 0.4611 0.3767 0.3282 0.0327  0.0006  0.0081  272 ILE A N   
2279 C CA  . ILE A 270 ? 0.4153 0.3321 0.2883 0.0322  -0.0005 0.0038  272 ILE A CA  
2280 C C   . ILE A 270 ? 0.4011 0.3207 0.2837 0.0309  0.0021  0.0045  272 ILE A C   
2281 O O   . ILE A 270 ? 0.3909 0.3116 0.2778 0.0311  0.0025  0.0019  272 ILE A O   
2282 C CB  . ILE A 270 ? 0.4191 0.3358 0.2941 0.0320  -0.0060 0.0017  272 ILE A CB  
2283 C CG1 . ILE A 270 ? 0.3834 0.3003 0.2636 0.0315  -0.0080 0.0049  272 ILE A CG1 
2284 C CG2 . ILE A 270 ? 0.4458 0.3621 0.3115 0.0331  -0.0089 -0.0003 272 ILE A CG2 
2285 C CD1 . ILE A 270 ? 0.4165 0.3344 0.3010 0.0314  -0.0129 0.0029  272 ILE A CD1 
2286 N N   . LEU A 271 ? 0.3957 0.3166 0.2818 0.0295  0.0040  0.0077  273 LEU A N   
2287 C CA  . LEU A 271 ? 0.3419 0.2671 0.2374 0.0278  0.0054  0.0077  273 LEU A CA  
2288 C C   . LEU A 271 ? 0.4035 0.3331 0.3005 0.0282  0.0099  0.0080  273 LEU A C   
2289 O O   . LEU A 271 ? 0.4098 0.3437 0.3132 0.0284  0.0105  0.0071  273 LEU A O   
2290 C CB  . LEU A 271 ? 0.3844 0.3098 0.2836 0.0255  0.0058  0.0101  273 LEU A CB  
2291 C CG  . LEU A 271 ? 0.3996 0.3306 0.3083 0.0230  0.0070  0.0095  273 LEU A CG  
2292 C CD1 . LEU A 271 ? 0.3612 0.2938 0.2751 0.0234  0.0038  0.0070  273 LEU A CD1 
2293 C CD2 . LEU A 271 ? 0.4353 0.3647 0.3466 0.0202  0.0081  0.0110  273 LEU A CD2 
2294 N N   . GLY A 272 ? 0.3998 0.3290 0.2912 0.0287  0.0132  0.0097  274 GLY A N   
2295 C CA  . GLY A 272 ? 0.4012 0.3354 0.2945 0.0294  0.0177  0.0103  274 GLY A CA  
2296 C C   . GLY A 272 ? 0.3677 0.3095 0.2696 0.0269  0.0196  0.0119  274 GLY A C   
2297 O O   . GLY A 272 ? 0.3864 0.3284 0.2920 0.0241  0.0181  0.0123  274 GLY A O   
2298 N N   . ARG A 273 ? 0.3335 0.2819 0.2387 0.0280  0.0232  0.0125  275 ARG A N   
2299 C CA  . ARG A 273 ? 0.3390 0.2975 0.2528 0.0259  0.0249  0.0135  275 ARG A CA  
2300 C C   . ARG A 273 ? 0.3609 0.3251 0.2803 0.0286  0.0248  0.0132  275 ARG A C   
2301 O O   . ARG A 273 ? 0.3869 0.3497 0.3040 0.0324  0.0269  0.0132  275 ARG A O   
2302 C CB  . ARG A 273 ? 0.3690 0.3330 0.2826 0.0249  0.0296  0.0156  275 ARG A CB  
2303 C CG  . ARG A 273 ? 0.4044 0.3632 0.3133 0.0220  0.0306  0.0168  275 ARG A CG  
2304 C CD  . ARG A 273 ? 0.4234 0.3900 0.3354 0.0194  0.0355  0.0186  275 ARG A CD  
2305 N NE  . ARG A 273 ? 0.4646 0.4346 0.3739 0.0227  0.0392  0.0197  275 ARG A NE  
2306 C CZ  . ARG A 273 ? 0.5130 0.4924 0.4263 0.0216  0.0436  0.0212  275 ARG A CZ  
2307 N NH1 . ARG A 273 ? 0.5509 0.5376 0.4710 0.0165  0.0446  0.0213  275 ARG A NH1 
2308 N NH2 . ARG A 273 ? 0.5267 0.5086 0.4375 0.0253  0.0472  0.0222  275 ARG A NH2 
2309 N N   . HIS A 274 ? 0.2734 0.2438 0.2000 0.0268  0.0229  0.0129  276 HIS A N   
2310 C CA  . HIS A 274 ? 0.2663 0.2421 0.1982 0.0295  0.0227  0.0133  276 HIS A CA  
2311 C C   . HIS A 274 ? 0.2615 0.2506 0.2014 0.0273  0.0230  0.0143  276 HIS A C   
2312 O O   . HIS A 274 ? 0.2785 0.2695 0.2208 0.0230  0.0212  0.0130  276 HIS A O   
2313 C CB  . HIS A 274 ? 0.2703 0.2386 0.2016 0.0301  0.0189  0.0113  276 HIS A CB  
2314 C CG  . HIS A 274 ? 0.2900 0.2468 0.2136 0.0316  0.0180  0.0096  276 HIS A CG  
2315 N ND1 . HIS A 274 ? 0.3340 0.2871 0.2545 0.0353  0.0205  0.0092  276 HIS A ND1 
2316 C CD2 . HIS A 274 ? 0.3082 0.2572 0.2264 0.0301  0.0152  0.0080  276 HIS A CD2 
2317 C CE1 . HIS A 274 ? 0.3010 0.2450 0.2144 0.0353  0.0189  0.0068  276 HIS A CE1 
2318 N NE2 . HIS A 274 ? 0.3463 0.2882 0.2581 0.0324  0.0155  0.0064  276 HIS A NE2 
2319 N N   . SER A 275 ? 0.2561 0.2549 0.2003 0.0305  0.0255  0.0167  277 SER A N   
2320 C CA  . SER A 275 ? 0.2388 0.2525 0.1907 0.0291  0.0253  0.0178  277 SER A CA  
2321 C C   . SER A 275 ? 0.2710 0.2845 0.2257 0.0291  0.0220  0.0170  277 SER A C   
2322 O O   . SER A 275 ? 0.3063 0.3098 0.2584 0.0317  0.0208  0.0165  277 SER A O   
2323 C CB  . SER A 275 ? 0.3210 0.3456 0.2766 0.0337  0.0289  0.0214  277 SER A CB  
2324 O OG  . SER A 275 ? 0.4002 0.4180 0.3546 0.0393  0.0297  0.0228  277 SER A OG  
2325 N N   . ARG A 276 ? 0.2418 0.2672 0.2020 0.0260  0.0208  0.0166  278 ARG A N   
2326 C CA  . ARG A 276 ? 0.2223 0.2507 0.1858 0.0266  0.0183  0.0166  278 ARG A CA  
2327 C C   . ARG A 276 ? 0.2334 0.2682 0.1997 0.0327  0.0202  0.0209  278 ARG A C   
2328 O O   . ARG A 276 ? 0.2710 0.3165 0.2400 0.0351  0.0230  0.0238  278 ARG A O   
2329 C CB  . ARG A 276 ? 0.2609 0.3012 0.2290 0.0213  0.0168  0.0146  278 ARG A CB  
2330 C CG  . ARG A 276 ? 0.2634 0.3052 0.2337 0.0210  0.0140  0.0136  278 ARG A CG  
2331 C CD  . ARG A 276 ? 0.2524 0.2981 0.2246 0.0143  0.0124  0.0093  278 ARG A CD  
2332 N NE  . ARG A 276 ? 0.2860 0.3286 0.2589 0.0136  0.0098  0.0075  278 ARG A NE  
2333 C CZ  . ARG A 276 ? 0.3151 0.3527 0.2879 0.0089  0.0085  0.0033  278 ARG A CZ  
2334 N NH1 . ARG A 276 ? 0.2956 0.3297 0.2674 0.0045  0.0096  0.0007  278 ARG A NH1 
2335 N NH2 . ARG A 276 ? 0.2888 0.3242 0.2625 0.0088  0.0065  0.0018  278 ARG A NH2 
2336 N N   . LYS A 277 ? 0.2474 0.2756 0.2135 0.0355  0.0192  0.0215  279 LYS A N   
2337 C CA  . LYS A 277 ? 0.2228 0.2541 0.1914 0.0418  0.0218  0.0259  279 LYS A CA  
2338 C C   . LYS A 277 ? 0.2748 0.3204 0.2489 0.0423  0.0207  0.0285  279 LYS A C   
2339 O O   . LYS A 277 ? 0.3186 0.3675 0.2937 0.0379  0.0176  0.0258  279 LYS A O   
2340 C CB  . LYS A 277 ? 0.2361 0.2510 0.2013 0.0445  0.0222  0.0252  279 LYS A CB  
2341 C CG  . LYS A 277 ? 0.2609 0.2620 0.2197 0.0437  0.0226  0.0221  279 LYS A CG  
2342 C CD  . LYS A 277 ? 0.2530 0.2579 0.2107 0.0458  0.0263  0.0238  279 LYS A CD  
2343 C CE  . LYS A 277 ? 0.2692 0.2605 0.2199 0.0460  0.0274  0.0211  279 LYS A CE  
2344 N NZ  . LYS A 277 ? 0.3086 0.2940 0.2546 0.0408  0.0241  0.0174  279 LYS A NZ  
2345 N N   . ARG A 278 ? 0.2462 0.3003 0.2238 0.0482  0.0236  0.0340  280 ARG A N   
2346 C CA  . ARG A 278 ? 0.2564 0.3234 0.2385 0.0500  0.0230  0.0375  280 ARG A CA  
2347 C C   . ARG A 278 ? 0.3227 0.3775 0.3040 0.0530  0.0235  0.0387  280 ARG A C   
2348 O O   . ARG A 278 ? 0.3137 0.3548 0.2928 0.0564  0.0262  0.0393  280 ARG A O   
2349 C CB  . ARG A 278 ? 0.3296 0.4135 0.3162 0.0555  0.0259  0.0438  280 ARG A CB  
2350 C CG  . ARG A 278 ? 0.3169 0.4143 0.3051 0.0522  0.0257  0.0424  280 ARG A CG  
2351 C CD  . ARG A 278 ? 0.3405 0.4594 0.3343 0.0568  0.0276  0.0485  280 ARG A CD  
2352 N NE  . ARG A 278 ? 0.3604 0.4884 0.3556 0.0544  0.0286  0.0472  280 ARG A NE  
2353 C CZ  . ARG A 278 ? 0.3764 0.5197 0.3740 0.0479  0.0262  0.0439  280 ARG A CZ  
2354 N NH1 . ARG A 278 ? 0.3570 0.5085 0.3556 0.0433  0.0227  0.0413  280 ARG A NH1 
2355 N NH2 . ARG A 278 ? 0.3323 0.4827 0.3315 0.0458  0.0278  0.0429  280 ARG A NH2 
2356 N N   . TRP A 279 ? 0.2674 0.3274 0.2505 0.0512  0.0211  0.0386  281 TRP A N   
2357 C CA  . TRP A 279 ? 0.2623 0.3106 0.2449 0.0530  0.0215  0.0392  281 TRP A CA  
2358 C C   . TRP A 279 ? 0.3050 0.3518 0.2899 0.0605  0.0263  0.0458  281 TRP A C   
2359 O O   . TRP A 279 ? 0.3109 0.3435 0.2950 0.0621  0.0280  0.0458  281 TRP A O   
2360 C CB  . TRP A 279 ? 0.2829 0.3387 0.2673 0.0497  0.0184  0.0381  281 TRP A CB  
2361 C CG  . TRP A 279 ? 0.2956 0.3486 0.2779 0.0426  0.0145  0.0312  281 TRP A CG  
2362 C CD1 . TRP A 279 ? 0.3483 0.4138 0.3315 0.0379  0.0123  0.0285  281 TRP A CD1 
2363 C CD2 . TRP A 279 ? 0.2892 0.3256 0.2683 0.0394  0.0127  0.0262  281 TRP A CD2 
2364 N NE1 . TRP A 279 ? 0.3100 0.3664 0.2909 0.0323  0.0097  0.0223  281 TRP A NE1 
2365 C CE2 . TRP A 279 ? 0.3494 0.3886 0.3279 0.0335  0.0097  0.0213  281 TRP A CE2 
2366 C CE3 . TRP A 279 ? 0.2996 0.3197 0.2767 0.0409  0.0134  0.0253  281 TRP A CE3 
2367 C CZ2 . TRP A 279 ? 0.3069 0.3333 0.2828 0.0300  0.0075  0.0165  281 TRP A CZ2 
2368 C CZ3 . TRP A 279 ? 0.3059 0.3150 0.2804 0.0369  0.0106  0.0201  281 TRP A CZ3 
2369 C CH2 . TRP A 279 ? 0.3231 0.3354 0.2970 0.0320  0.0076  0.0162  281 TRP A CH2 
2370 N N   . GLU A 280 ? 0.2937 0.3548 0.2816 0.0653  0.0287  0.0515  282 GLU A N   
2371 C CA  . GLU A 280 ? 0.3406 0.4005 0.3311 0.0734  0.0340  0.0588  282 GLU A CA  
2372 C C   . GLU A 280 ? 0.3136 0.3536 0.3015 0.0758  0.0380  0.0573  282 GLU A C   
2373 O O   . GLU A 280 ? 0.3300 0.3619 0.3194 0.0813  0.0427  0.0616  282 GLU A O   
2374 C CB  . GLU A 280 ? 0.3741 0.4540 0.3684 0.0781  0.0358  0.0650  282 GLU A CB  
2375 C CG  . GLU A 280 ? 0.4102 0.5115 0.4076 0.0778  0.0331  0.0683  282 GLU A CG  
2376 C CD  . GLU A 280 ? 0.4571 0.5690 0.4535 0.0694  0.0277  0.0617  282 GLU A CD  
2377 O OE1 . GLU A 280 ? 0.4709 0.6008 0.4693 0.0681  0.0254  0.0631  282 GLU A OE1 
2378 O OE2 . GLU A 280 ? 0.4103 0.5127 0.4038 0.0640  0.0261  0.0551  282 GLU A OE2 
2379 N N   . ARG A 281 ? 0.3500 0.3816 0.3338 0.0718  0.0366  0.0513  283 ARG A N   
2380 C CA  . ARG A 281 ? 0.3478 0.3616 0.3284 0.0737  0.0403  0.0493  283 ARG A CA  
2381 C C   . ARG A 281 ? 0.3853 0.3827 0.3646 0.0723  0.0405  0.0465  283 ARG A C   
2382 O O   . ARG A 281 ? 0.3627 0.3459 0.3405 0.0748  0.0447  0.0456  283 ARG A O   
2383 C CB  . ARG A 281 ? 0.3993 0.4086 0.3751 0.0694  0.0383  0.0435  283 ARG A CB  
2384 C CG  . ARG A 281 ? 0.4124 0.4149 0.3843 0.0621  0.0328  0.0368  283 ARG A CG  
2385 C CD  . ARG A 281 ? 0.5123 0.5015 0.4781 0.0599  0.0329  0.0316  283 ARG A CD  
2386 N NE  . ARG A 281 ? 0.5324 0.5278 0.4970 0.0608  0.0346  0.0324  283 ARG A NE  
2387 C CZ  . ARG A 281 ? 0.4303 0.4165 0.3896 0.0604  0.0361  0.0293  283 ARG A CZ  
2388 N NH1 . ARG A 281 ? 0.4768 0.4476 0.4312 0.0591  0.0358  0.0249  283 ARG A NH1 
2389 N NH2 . ARG A 281 ? 0.4573 0.4505 0.4161 0.0613  0.0380  0.0305  283 ARG A NH2 
2390 N N   . PHE A 282 ? 0.3090 0.3081 0.2890 0.0683  0.0365  0.0448  284 PHE A N   
2391 C CA  . PHE A 282 ? 0.3281 0.3131 0.3076 0.0665  0.0366  0.0420  284 PHE A CA  
2392 C C   . PHE A 282 ? 0.3122 0.2977 0.2962 0.0712  0.0407  0.0483  284 PHE A C   
2393 O O   . PHE A 282 ? 0.3471 0.3209 0.3316 0.0699  0.0417  0.0465  284 PHE A O   
2394 C CB  . PHE A 282 ? 0.3059 0.2912 0.2839 0.0597  0.0304  0.0365  284 PHE A CB  
2395 C CG  . PHE A 282 ? 0.3220 0.3052 0.2954 0.0553  0.0268  0.0310  284 PHE A CG  
2396 C CD1 . PHE A 282 ? 0.4130 0.3825 0.3819 0.0542  0.0274  0.0266  284 PHE A CD1 
2397 C CD2 . PHE A 282 ? 0.2994 0.2948 0.2729 0.0524  0.0234  0.0303  284 PHE A CD2 
2398 C CE1 . PHE A 282 ? 0.3546 0.3226 0.3189 0.0508  0.0245  0.0224  284 PHE A CE1 
2399 C CE2 . PHE A 282 ? 0.3442 0.3369 0.3136 0.0487  0.0210  0.0260  284 PHE A CE2 
2400 C CZ  . PHE A 282 ? 0.3643 0.3434 0.3290 0.0482  0.0215  0.0225  284 PHE A CZ  
2401 N N   . VAL A 283 ? 0.3128 0.3120 0.3004 0.0768  0.0432  0.0558  285 VAL A N   
2402 C CA  . VAL A 283 ? 0.3116 0.3129 0.3034 0.0824  0.0476  0.0633  285 VAL A CA  
2403 C C   . VAL A 283 ? 0.3002 0.2889 0.2930 0.0885  0.0552  0.0666  285 VAL A C   
2404 O O   . VAL A 283 ? 0.3652 0.3550 0.3572 0.0916  0.0575  0.0673  285 VAL A O   
2405 C CB  . VAL A 283 ? 0.3279 0.3518 0.3229 0.0859  0.0467  0.0703  285 VAL A CB  
2406 C CG1 . VAL A 283 ? 0.3708 0.3973 0.3697 0.0922  0.0513  0.0791  285 VAL A CG1 
2407 C CG2 . VAL A 283 ? 0.3286 0.3646 0.3223 0.0792  0.0397  0.0658  285 VAL A CG2 
2408 N N   . HIS A 284 ? 0.3064 0.2830 0.3012 0.0903  0.0596  0.0686  286 HIS A N   
2409 C CA  . HIS A 284 ? 0.2928 0.2568 0.2894 0.0965  0.0680  0.0723  286 HIS A CA  
2410 C C   . HIS A 284 ? 0.3560 0.3174 0.3571 0.1007  0.0729  0.0795  286 HIS A C   
2411 O O   . HIS A 284 ? 0.3739 0.3444 0.3763 0.0987  0.0695  0.0816  286 HIS A O   
2412 C CB  . HIS A 284 ? 0.3725 0.3162 0.3654 0.0923  0.0694  0.0634  286 HIS A CB  
2413 C CG  . HIS A 284 ? 0.3661 0.3010 0.3573 0.0844  0.0651  0.0560  286 HIS A CG  
2414 N ND1 . HIS A 284 ? 0.3798 0.3081 0.3743 0.0838  0.0675  0.0577  286 HIS A ND1 
2415 C CD2 . HIS A 284 ? 0.3824 0.3145 0.3692 0.0771  0.0588  0.0473  286 HIS A CD2 
2416 C CE1 . HIS A 284 ? 0.3829 0.3056 0.3755 0.0763  0.0626  0.0500  286 HIS A CE1 
2417 N NE2 . HIS A 284 ? 0.3524 0.2773 0.3403 0.0725  0.0573  0.0438  286 HIS A NE2 
2418 N N   . SER A 285 ? 0.3940 0.3426 0.3975 0.1066  0.0816  0.0836  287 SER A N   
2419 C CA  . SER A 285 ? 0.3452 0.2915 0.3534 0.1120  0.0877  0.0923  287 SER A CA  
2420 C C   . SER A 285 ? 0.3674 0.3044 0.3760 0.1057  0.0863  0.0884  287 SER A C   
2421 O O   . SER A 285 ? 0.4292 0.3695 0.4412 0.1087  0.0891  0.0956  287 SER A O   
2422 C CB  . SER A 285 ? 0.4166 0.3482 0.4274 0.1193  0.0982  0.0967  287 SER A CB  
2423 O OG  . SER A 285 ? 0.5541 0.4659 0.5619 0.1146  0.1002  0.0869  287 SER A OG  
2424 N N   . GLU A 286 ? 0.3460 0.2726 0.3513 0.0972  0.0821  0.0774  288 GLU A N   
2425 C CA  . GLU A 286 ? 0.3467 0.2644 0.3531 0.0912  0.0811  0.0733  288 GLU A CA  
2426 C C   . GLU A 286 ? 0.4285 0.3600 0.4337 0.0856  0.0724  0.0707  288 GLU A C   
2427 O O   . GLU A 286 ? 0.4624 0.3893 0.4692 0.0810  0.0713  0.0681  288 GLU A O   
2428 C CB  . GLU A 286 ? 0.3793 0.2778 0.3836 0.0852  0.0822  0.0630  288 GLU A CB  
2429 C CG  . GLU A 286 ? 0.3971 0.2780 0.4036 0.0895  0.0925  0.0647  288 GLU A CG  
2430 C CD  . GLU A 286 ? 0.5358 0.4189 0.5411 0.0967  0.0964  0.0686  288 GLU A CD  
2431 O OE1 . GLU A 286 ? 0.4895 0.3770 0.4901 0.0945  0.0915  0.0632  288 GLU A OE1 
2432 O OE2 . GLU A 286 ? 0.5653 0.4459 0.5745 0.1049  0.1046  0.0776  288 GLU A OE2 
2433 N N   . ASN A 287 ? 0.3583 0.3065 0.3612 0.0858  0.0665  0.0711  289 ASN A N   
2434 C CA  . ASN A 287 ? 0.2967 0.2586 0.2989 0.0813  0.0593  0.0694  289 ASN A CA  
2435 C C   . ASN A 287 ? 0.3290 0.3123 0.3323 0.0859  0.0580  0.0773  289 ASN A C   
2436 O O   . ASN A 287 ? 0.3294 0.3249 0.3320 0.0823  0.0526  0.0759  289 ASN A O   
2437 C CB  . ASN A 287 ? 0.3013 0.2631 0.2993 0.0743  0.0520  0.0596  289 ASN A CB  
2438 C CG  . ASN A 287 ? 0.2654 0.2337 0.2605 0.0761  0.0506  0.0591  289 ASN A CG  
2439 O OD1 . ASN A 287 ? 0.3050 0.2844 0.3016 0.0820  0.0530  0.0661  289 ASN A OD1 
2440 N ND2 . ASN A 287 ? 0.3074 0.2696 0.2985 0.0711  0.0467  0.0511  289 ASN A ND2 
2441 N N   . GLN A 288 ? 0.3071 0.2959 0.3121 0.0938  0.0629  0.0854  290 GLN A N   
2442 C CA  . GLN A 288 ? 0.3246 0.3366 0.3303 0.0975  0.0605  0.0917  290 GLN A CA  
2443 C C   . GLN A 288 ? 0.3189 0.3418 0.3263 0.0984  0.0601  0.0974  290 GLN A C   
2444 O O   . GLN A 288 ? 0.3994 0.4429 0.4063 0.0985  0.0560  0.0997  290 GLN A O   
2445 C CB  . GLN A 288 ? 0.3946 0.4116 0.4023 0.1064  0.0659  0.0998  290 GLN A CB  
2446 C CG  . GLN A 288 ? 0.4543 0.4619 0.4657 0.1141  0.0747  0.1087  290 GLN A CG  
2447 C CD  . GLN A 288 ? 0.6180 0.6313 0.6318 0.1235  0.0802  0.1168  290 GLN A CD  
2448 O OE1 . GLN A 288 ? 0.7037 0.7214 0.7210 0.1319  0.0860  0.1277  290 GLN A OE1 
2449 N NE2 . GLN A 288 ? 0.7116 0.7250 0.7236 0.1225  0.0785  0.1120  290 GLN A NE2 
2450 N N   . HIS A 289 ? 0.3113 0.3213 0.3207 0.0986  0.0644  0.0992  291 HIS A N   
2451 C CA  . HIS A 289 ? 0.3231 0.3426 0.3338 0.0992  0.0644  0.1044  291 HIS A CA  
2452 C C   . HIS A 289 ? 0.3903 0.4167 0.3987 0.0909  0.0568  0.0965  291 HIS A C   
2453 O O   . HIS A 289 ? 0.3805 0.4191 0.3892 0.0909  0.0556  0.1000  291 HIS A O   
2454 C CB  . HIS A 289 ? 0.3880 0.3904 0.4018 0.1013  0.0718  0.1084  291 HIS A CB  
2455 C CG  . HIS A 289 ? 0.3717 0.3538 0.3854 0.0939  0.0714  0.0986  291 HIS A CG  
2456 N ND1 . HIS A 289 ? 0.4240 0.3910 0.4367 0.0921  0.0725  0.0922  291 HIS A ND1 
2457 C CD2 . HIS A 289 ? 0.4243 0.4003 0.4389 0.0878  0.0698  0.0939  291 HIS A CD2 
2458 C CE1 . HIS A 289 ? 0.4195 0.3725 0.4323 0.0851  0.0713  0.0840  291 HIS A CE1 
2459 N NE2 . HIS A 289 ? 0.4197 0.3779 0.4340 0.0824  0.0697  0.0849  291 HIS A NE2 
2460 N N   . LEU A 290 ? 0.3545 0.3737 0.3606 0.0842  0.0520  0.0863  292 LEU A N   
2461 C CA  . LEU A 290 ? 0.2949 0.3191 0.2990 0.0766  0.0451  0.0784  292 LEU A CA  
2462 C C   . LEU A 290 ? 0.3009 0.3403 0.3025 0.0745  0.0395  0.0751  292 LEU A C   
2463 O O   . LEU A 290 ? 0.3141 0.3586 0.3140 0.0684  0.0342  0.0688  292 LEU A O   
2464 C CB  . LEU A 290 ? 0.3445 0.3501 0.3480 0.0705  0.0436  0.0694  292 LEU A CB  
2465 C CG  . LEU A 290 ? 0.3643 0.3534 0.3708 0.0707  0.0489  0.0704  292 LEU A CG  
2466 C CD1 . LEU A 290 ? 0.3672 0.3415 0.3729 0.0642  0.0463  0.0607  292 LEU A CD1 
2467 C CD2 . LEU A 290 ? 0.3987 0.3939 0.4077 0.0709  0.0503  0.0748  292 LEU A CD2 
2468 N N   . VAL A 291 ? 0.3018 0.3482 0.3032 0.0792  0.0410  0.0792  293 VAL A N   
2469 C CA  . VAL A 291 ? 0.3111 0.3709 0.3106 0.0768  0.0364  0.0758  293 VAL A CA  
2470 C C   . VAL A 291 ? 0.3192 0.4023 0.3200 0.0813  0.0366  0.0832  293 VAL A C   
2471 O O   . VAL A 291 ? 0.4083 0.4952 0.4114 0.0889  0.0414  0.0926  293 VAL A O   
2472 C CB  . VAL A 291 ? 0.3590 0.4092 0.3575 0.0778  0.0377  0.0733  293 VAL A CB  
2473 C CG1 . VAL A 291 ? 0.4274 0.4911 0.4244 0.0748  0.0333  0.0698  293 VAL A CG1 
2474 C CG2 . VAL A 291 ? 0.3753 0.4039 0.3721 0.0732  0.0373  0.0659  293 VAL A CG2 
2475 N N   . SER A 292 ? 0.3594 0.4584 0.3588 0.0767  0.0314  0.0790  294 SER A N   
2476 C CA  . SER A 292 ? 0.2665 0.3904 0.2666 0.0791  0.0301  0.0839  294 SER A CA  
2477 C C   . SER A 292 ? 0.3247 0.4585 0.3236 0.0732  0.0254  0.0767  294 SER A C   
2478 O O   . SER A 292 ? 0.2767 0.3979 0.2738 0.0668  0.0228  0.0681  294 SER A O   
2479 C CB  . SER A 292 ? 0.2857 0.4209 0.2854 0.0781  0.0290  0.0858  294 SER A CB  
2480 O OG  . SER A 292 ? 0.3122 0.4406 0.3099 0.0699  0.0250  0.0762  294 SER A OG  
2481 N N   . PRO A 293 ? 0.2953 0.4516 0.2954 0.0749  0.0243  0.0799  295 PRO A N   
2482 C CA  . PRO A 293 ? 0.3162 0.4828 0.3154 0.0680  0.0200  0.0723  295 PRO A CA  
2483 C C   . PRO A 293 ? 0.2778 0.4421 0.2747 0.0594  0.0160  0.0634  295 PRO A C   
2484 O O   . PRO A 293 ? 0.2705 0.4286 0.2662 0.0529  0.0136  0.0552  295 PRO A O   
2485 C CB  . PRO A 293 ? 0.3008 0.4956 0.3022 0.0715  0.0195  0.0781  295 PRO A CB  
2486 C CG  . PRO A 293 ? 0.3817 0.5760 0.3854 0.0819  0.0245  0.0895  295 PRO A CG  
2487 C CD  . PRO A 293 ? 0.3144 0.4883 0.3169 0.0834  0.0271  0.0908  295 PRO A CD  
2488 N N   . GLU A 294 ? 0.2924 0.4610 0.2887 0.0597  0.0159  0.0651  296 GLU A N   
2489 C CA  . GLU A 294 ? 0.2263 0.3929 0.2206 0.0522  0.0128  0.0569  296 GLU A CA  
2490 C C   . GLU A 294 ? 0.2786 0.4199 0.2720 0.0487  0.0126  0.0509  296 GLU A C   
2491 O O   . GLU A 294 ? 0.2426 0.3797 0.2347 0.0419  0.0098  0.0425  296 GLU A O   
2492 C CB  . GLU A 294 ? 0.2780 0.4541 0.2718 0.0540  0.0134  0.0609  296 GLU A CB  
2493 C CG  . GLU A 294 ? 0.2927 0.4974 0.2865 0.0559  0.0125  0.0653  296 GLU A CG  
2494 C CD  . GLU A 294 ? 0.4780 0.6914 0.4739 0.0653  0.0157  0.0767  296 GLU A CD  
2495 O OE1 . GLU A 294 ? 0.3507 0.5470 0.3480 0.0709  0.0196  0.0821  296 GLU A OE1 
2496 O OE2 . GLU A 294 ? 0.5660 0.8040 0.5625 0.0671  0.0145  0.0802  296 GLU A OE2 
2497 N N   . ALA A 295 ? 0.2285 0.3533 0.2226 0.0533  0.0157  0.0551  297 ALA A N   
2498 C CA  . ALA A 295 ? 0.2367 0.3392 0.2299 0.0502  0.0153  0.0495  297 ALA A CA  
2499 C C   . ALA A 295 ? 0.2345 0.3304 0.2265 0.0470  0.0136  0.0441  297 ALA A C   
2500 O O   . ALA A 295 ? 0.2547 0.3401 0.2452 0.0417  0.0112  0.0371  297 ALA A O   
2501 C CB  . ALA A 295 ? 0.2446 0.3321 0.2391 0.0555  0.0194  0.0548  297 ALA A CB  
2502 N N   . LEU A 296 ? 0.2475 0.3495 0.2399 0.0504  0.0151  0.0477  298 LEU A N   
2503 C CA  . LEU A 296 ? 0.2400 0.3355 0.2310 0.0475  0.0140  0.0431  298 LEU A CA  
2504 C C   . LEU A 296 ? 0.2623 0.3676 0.2527 0.0406  0.0106  0.0366  298 LEU A C   
2505 O O   . LEU A 296 ? 0.2639 0.3585 0.2525 0.0360  0.0091  0.0305  298 LEU A O   
2506 C CB  . LEU A 296 ? 0.2636 0.3638 0.2558 0.0532  0.0170  0.0488  298 LEU A CB  
2507 C CG  . LEU A 296 ? 0.2775 0.3648 0.2704 0.0599  0.0214  0.0544  298 LEU A CG  
2508 C CD1 . LEU A 296 ? 0.3042 0.3947 0.2981 0.0650  0.0245  0.0588  298 LEU A CD1 
2509 C CD2 . LEU A 296 ? 0.3736 0.4383 0.3642 0.0573  0.0212  0.0494  298 LEU A CD2 
2510 N N   . ASP A 297 ? 0.2348 0.3602 0.2265 0.0396  0.0096  0.0375  299 ASP A N   
2511 C CA  . ASP A 297 ? 0.2769 0.4112 0.2681 0.0321  0.0069  0.0304  299 ASP A CA  
2512 C C   . ASP A 297 ? 0.2912 0.4134 0.2809 0.0270  0.0052  0.0238  299 ASP A C   
2513 O O   . ASP A 297 ? 0.2503 0.3664 0.2391 0.0214  0.0039  0.0172  299 ASP A O   
2514 C CB  . ASP A 297 ? 0.2476 0.4072 0.2403 0.0316  0.0060  0.0320  299 ASP A CB  
2515 C CG  . ASP A 297 ? 0.3238 0.4924 0.3163 0.0231  0.0038  0.0236  299 ASP A CG  
2516 O OD1 . ASP A 297 ? 0.3697 0.5368 0.3626 0.0198  0.0037  0.0202  299 ASP A OD1 
2517 O OD2 . ASP A 297 ? 0.3224 0.4987 0.3142 0.0195  0.0025  0.0200  299 ASP A OD2 
2518 N N   . PHE A 298 ? 0.2526 0.3715 0.2424 0.0291  0.0055  0.0258  300 PHE A N   
2519 C CA  . PHE A 298 ? 0.2268 0.3347 0.2159 0.0249  0.0042  0.0201  300 PHE A CA  
2520 C C   . PHE A 298 ? 0.2570 0.3442 0.2451 0.0239  0.0038  0.0169  300 PHE A C   
2521 O O   . PHE A 298 ? 0.2200 0.3006 0.2073 0.0190  0.0023  0.0107  300 PHE A O   
2522 C CB  . PHE A 298 ? 0.2021 0.3103 0.1919 0.0281  0.0052  0.0239  300 PHE A CB  
2523 C CG  . PHE A 298 ? 0.2301 0.3272 0.2200 0.0246  0.0042  0.0187  300 PHE A CG  
2524 C CD1 . PHE A 298 ? 0.2818 0.3811 0.2711 0.0186  0.0024  0.0113  300 PHE A CD1 
2525 C CD2 . PHE A 298 ? 0.3101 0.3953 0.3010 0.0275  0.0054  0.0213  300 PHE A CD2 
2526 C CE1 . PHE A 298 ? 0.3208 0.4105 0.3106 0.0161  0.0018  0.0069  300 PHE A CE1 
2527 C CE2 . PHE A 298 ? 0.2829 0.3594 0.2745 0.0245  0.0044  0.0167  300 PHE A CE2 
2528 C CZ  . PHE A 298 ? 0.3082 0.3873 0.2993 0.0192  0.0026  0.0097  300 PHE A CZ  
2529 N N   . LEU A 299 ? 0.2224 0.2996 0.2102 0.0287  0.0054  0.0213  301 LEU A N   
2530 C CA  . LEU A 299 ? 0.2451 0.3041 0.2312 0.0279  0.0049  0.0185  301 LEU A CA  
2531 C C   . LEU A 299 ? 0.2447 0.3035 0.2293 0.0242  0.0039  0.0145  301 LEU A C   
2532 O O   . LEU A 299 ? 0.2393 0.2873 0.2224 0.0209  0.0024  0.0098  301 LEU A O   
2533 C CB  . LEU A 299 ? 0.2354 0.2858 0.2214 0.0334  0.0073  0.0235  301 LEU A CB  
2534 C CG  . LEU A 299 ? 0.2632 0.2964 0.2467 0.0327  0.0069  0.0205  301 LEU A CG  
2535 C CD1 . LEU A 299 ? 0.2319 0.2547 0.2158 0.0303  0.0050  0.0167  301 LEU A CD1 
2536 C CD2 . LEU A 299 ? 0.2774 0.3038 0.2605 0.0378  0.0100  0.0248  301 LEU A CD2 
2537 N N   . ASP A 300 ? 0.2233 0.2945 0.2084 0.0250  0.0048  0.0167  302 ASP A N   
2538 C CA  . ASP A 300 ? 0.2082 0.2806 0.1923 0.0212  0.0045  0.0133  302 ASP A CA  
2539 C C   . ASP A 300 ? 0.2608 0.3340 0.2450 0.0146  0.0029  0.0067  302 ASP A C   
2540 O O   . ASP A 300 ? 0.2477 0.3139 0.2305 0.0111  0.0028  0.0031  302 ASP A O   
2541 C CB  . ASP A 300 ? 0.1962 0.2861 0.1821 0.0228  0.0058  0.0168  302 ASP A CB  
2542 C CG  . ASP A 300 ? 0.3337 0.4248 0.3191 0.0194  0.0062  0.0142  302 ASP A CG  
2543 O OD1 . ASP A 300 ? 0.3079 0.3850 0.2909 0.0203  0.0069  0.0139  302 ASP A OD1 
2544 O OD2 . ASP A 300 ? 0.3559 0.4627 0.3433 0.0158  0.0060  0.0123  302 ASP A OD2 
2545 N N   . LYS A 301 ? 0.2125 0.2943 0.1980 0.0128  0.0022  0.0051  303 LYS A N   
2546 C CA  . LYS A 301 ? 0.2135 0.2965 0.1993 0.0064  0.0014  -0.0017 303 LYS A CA  
2547 C C   . LYS A 301 ? 0.2158 0.2828 0.2010 0.0055  0.0005  -0.0048 303 LYS A C   
2548 O O   . LYS A 301 ? 0.2389 0.3031 0.2244 0.0007  0.0004  -0.0104 303 LYS A O   
2549 C CB  . LYS A 301 ? 0.2278 0.3295 0.2151 0.0045  0.0012  -0.0027 303 LYS A CB  
2550 C CG  . LYS A 301 ? 0.2475 0.3679 0.2361 0.0041  0.0016  -0.0008 303 LYS A CG  
2551 C CD  . LYS A 301 ? 0.3353 0.4760 0.3247 0.0033  0.0011  -0.0006 303 LYS A CD  
2552 C CE  . LYS A 301 ? 0.4370 0.5984 0.4280 0.0002  0.0010  -0.0017 303 LYS A CE  
2553 N NZ  . LYS A 301 ? 0.4767 0.6411 0.4688 0.0051  0.0019  0.0046  303 LYS A NZ  
2554 N N   . LEU A 302 ? 0.2252 0.2820 0.2100 0.0099  0.0002  -0.0014 304 LEU A N   
2555 C CA  . LEU A 302 ? 0.2139 0.2556 0.1983 0.0094  -0.0009 -0.0040 304 LEU A CA  
2556 C C   . LEU A 302 ? 0.2480 0.2767 0.2300 0.0097  -0.0012 -0.0045 304 LEU A C   
2557 O O   . LEU A 302 ? 0.2522 0.2720 0.2337 0.0073  -0.0019 -0.0080 304 LEU A O   
2558 C CB  . LEU A 302 ? 0.1925 0.2301 0.1780 0.0133  -0.0011 -0.0008 304 LEU A CB  
2559 C CG  . LEU A 302 ? 0.2117 0.2603 0.1992 0.0136  -0.0006 0.0002  304 LEU A CG  
2560 C CD1 . LEU A 302 ? 0.2688 0.3120 0.2574 0.0179  0.0001  0.0045  304 LEU A CD1 
2561 C CD2 . LEU A 302 ? 0.2438 0.2934 0.2324 0.0094  -0.0012 -0.0054 304 LEU A CD2 
2562 N N   . LEU A 303 ? 0.2253 0.2528 0.2057 0.0128  -0.0005 -0.0007 305 LEU A N   
2563 C CA  . LEU A 303 ? 0.2114 0.2265 0.1887 0.0136  -0.0008 -0.0007 305 LEU A CA  
2564 C C   . LEU A 303 ? 0.2586 0.2765 0.2347 0.0105  0.0003  -0.0023 305 LEU A C   
2565 O O   . LEU A 303 ? 0.2825 0.3041 0.2576 0.0120  0.0017  0.0002  305 LEU A O   
2566 C CB  . LEU A 303 ? 0.2485 0.2596 0.2244 0.0183  0.0001  0.0034  305 LEU A CB  
2567 C CG  . LEU A 303 ? 0.2209 0.2265 0.1982 0.0208  -0.0005 0.0045  305 LEU A CG  
2568 C CD1 . LEU A 303 ? 0.2433 0.2439 0.2192 0.0250  0.0013  0.0079  305 LEU A CD1 
2569 C CD2 . LEU A 303 ? 0.2325 0.2276 0.2093 0.0190  -0.0029 0.0009  305 LEU A CD2 
2570 N N   . ARG A 304 ? 0.2181 0.2343 0.1948 0.0062  0.0001  -0.0065 306 ARG A N   
2571 C CA  . ARG A 304 ? 0.2135 0.2295 0.1894 0.0025  0.0017  -0.0085 306 ARG A CA  
2572 C C   . ARG A 304 ? 0.2099 0.2106 0.1832 0.0022  0.0013  -0.0097 306 ARG A C   
2573 O O   . ARG A 304 ? 0.2221 0.2163 0.1961 0.0026  -0.0001 -0.0111 306 ARG A O   
2574 C CB  . ARG A 304 ? 0.2711 0.2969 0.2499 -0.0030 0.0027  -0.0129 306 ARG A CB  
2575 C CG  . ARG A 304 ? 0.3036 0.3455 0.2850 -0.0031 0.0025  -0.0125 306 ARG A CG  
2576 C CD  . ARG A 304 ? 0.2738 0.3266 0.2553 -0.0004 0.0030  -0.0082 306 ARG A CD  
2577 N NE  . ARG A 304 ? 0.2956 0.3514 0.2769 -0.0032 0.0047  -0.0090 306 ARG A NE  
2578 C CZ  . ARG A 304 ? 0.3988 0.4657 0.3809 -0.0014 0.0056  -0.0056 306 ARG A CZ  
2579 N NH1 . ARG A 304 ? 0.3552 0.4250 0.3376 -0.0044 0.0074  -0.0066 306 ARG A NH1 
2580 N NH2 . ARG A 304 ? 0.3874 0.4626 0.3704 0.0036  0.0051  -0.0010 306 ARG A NH2 
2581 N N   . TYR A 305 ? 0.2328 0.2287 0.2033 0.0018  0.0026  -0.0087 307 TYR A N   
2582 C CA  . TYR A 305 ? 0.2331 0.2157 0.2010 0.0015  0.0026  -0.0093 307 TYR A CA  
2583 C C   . TYR A 305 ? 0.2438 0.2241 0.2145 -0.0023 0.0035  -0.0132 307 TYR A C   
2584 O O   . TYR A 305 ? 0.2534 0.2251 0.2241 -0.0010 0.0024  -0.0137 307 TYR A O   
2585 C CB  . TYR A 305 ? 0.2656 0.2451 0.2303 0.0007  0.0047  -0.0078 307 TYR A CB  
2586 C CG  . TYR A 305 ? 0.2507 0.2280 0.2113 0.0048  0.0043  -0.0042 307 TYR A CG  
2587 C CD1 . TYR A 305 ? 0.2445 0.2122 0.2014 0.0085  0.0021  -0.0028 307 TYR A CD1 
2588 C CD2 . TYR A 305 ? 0.2430 0.2282 0.2034 0.0048  0.0063  -0.0026 307 TYR A CD2 
2589 C CE1 . TYR A 305 ? 0.2399 0.2051 0.1926 0.0118  0.0021  -0.0004 307 TYR A CE1 
2590 C CE2 . TYR A 305 ? 0.2203 0.2028 0.1769 0.0086  0.0065  0.0003  307 TYR A CE2 
2591 C CZ  . TYR A 305 ? 0.2355 0.2076 0.1880 0.0120  0.0045  0.0011  307 TYR A CZ  
2592 O OH  . TYR A 305 ? 0.2703 0.2395 0.2186 0.0153  0.0051  0.0031  307 TYR A OH  
2593 N N   . ASP A 306 ? 0.2421 0.2305 0.2154 -0.0072 0.0059  -0.0162 308 ASP A N   
2594 C CA  . ASP A 306 ? 0.2154 0.2008 0.1912 -0.0117 0.0080  -0.0207 308 ASP A CA  
2595 C C   . ASP A 306 ? 0.2254 0.2141 0.2040 -0.0112 0.0064  -0.0231 308 ASP A C   
2596 O O   . ASP A 306 ? 0.2426 0.2440 0.2230 -0.0120 0.0057  -0.0240 308 ASP A O   
2597 C CB  . ASP A 306 ? 0.2172 0.2118 0.1952 -0.0177 0.0111  -0.0240 308 ASP A CB  
2598 C CG  . ASP A 306 ? 0.3025 0.2911 0.2828 -0.0230 0.0144  -0.0292 308 ASP A CG  
2599 O OD1 . ASP A 306 ? 0.3116 0.2909 0.2925 -0.0216 0.0142  -0.0302 308 ASP A OD1 
2600 O OD2 . ASP A 306 ? 0.3398 0.3329 0.3217 -0.0287 0.0176  -0.0322 308 ASP A OD2 
2601 N N   . HIS A 307 ? 0.2362 0.2141 0.2151 -0.0096 0.0059  -0.0236 309 HIS A N   
2602 C CA  . HIS A 307 ? 0.2110 0.1915 0.1929 -0.0089 0.0047  -0.0257 309 HIS A CA  
2603 C C   . HIS A 307 ? 0.2759 0.2657 0.2607 -0.0143 0.0070  -0.0312 309 HIS A C   
2604 O O   . HIS A 307 ? 0.2760 0.2743 0.2625 -0.0141 0.0059  -0.0325 309 HIS A O   
2605 C CB  . HIS A 307 ? 0.2367 0.2044 0.2190 -0.0062 0.0043  -0.0254 309 HIS A CB  
2606 C CG  . HIS A 307 ? 0.2851 0.2427 0.2673 -0.0084 0.0076  -0.0268 309 HIS A CG  
2607 N ND1 . HIS A 307 ? 0.2653 0.2151 0.2442 -0.0073 0.0084  -0.0235 309 HIS A ND1 
2608 C CD2 . HIS A 307 ? 0.3043 0.2578 0.2895 -0.0116 0.0111  -0.0312 309 HIS A CD2 
2609 C CE1 . HIS A 307 ? 0.2990 0.2401 0.2789 -0.0096 0.0122  -0.0252 309 HIS A CE1 
2610 N NE2 . HIS A 307 ? 0.3058 0.2485 0.2897 -0.0123 0.0141  -0.0300 309 HIS A NE2 
2611 N N   . GLN A 308 ? 0.2594 0.2489 0.2446 -0.0194 0.0103  -0.0345 310 GLN A N   
2612 C CA  . GLN A 308 ? 0.2680 0.2672 0.2559 -0.0255 0.0128  -0.0408 310 GLN A CA  
2613 C C   . GLN A 308 ? 0.3095 0.3272 0.2974 -0.0272 0.0115  -0.0407 310 GLN A C   
2614 O O   . GLN A 308 ? 0.3455 0.3745 0.3353 -0.0322 0.0128  -0.0460 310 GLN A O   
2615 C CB  . GLN A 308 ? 0.2879 0.2801 0.2766 -0.0311 0.0173  -0.0448 310 GLN A CB  
2616 C CG  . GLN A 308 ? 0.3098 0.2849 0.2993 -0.0300 0.0198  -0.0457 310 GLN A CG  
2617 C CD  . GLN A 308 ? 0.3959 0.3628 0.3866 -0.0355 0.0253  -0.0493 310 GLN A CD  
2618 O OE1 . GLN A 308 ? 0.3858 0.3607 0.3771 -0.0412 0.0272  -0.0520 310 GLN A OE1 
2619 N NE2 . GLN A 308 ? 0.3641 0.3152 0.3556 -0.0339 0.0280  -0.0491 310 GLN A NE2 
2620 N N   . SER A 309 ? 0.2589 0.2805 0.2450 -0.0230 0.0092  -0.0349 311 SER A N   
2621 C CA  . SER A 309 ? 0.2520 0.2914 0.2385 -0.0234 0.0082  -0.0336 311 SER A CA  
2622 C C   . SER A 309 ? 0.2245 0.2707 0.2108 -0.0183 0.0054  -0.0297 311 SER A C   
2623 O O   . SER A 309 ? 0.2891 0.3510 0.2760 -0.0178 0.0047  -0.0279 311 SER A O   
2624 C CB  . SER A 309 ? 0.2849 0.3247 0.2699 -0.0221 0.0085  -0.0296 311 SER A CB  
2625 O OG  . SER A 309 ? 0.3018 0.3376 0.2875 -0.0276 0.0116  -0.0331 311 SER A OG  
2626 N N   . ARG A 310 ? 0.2104 0.2460 0.1963 -0.0143 0.0040  -0.0280 312 ARG A N   
2627 C CA  . ARG A 310 ? 0.2223 0.2626 0.2083 -0.0097 0.0020  -0.0242 312 ARG A CA  
2628 C C   . ARG A 310 ? 0.1936 0.2460 0.1813 -0.0119 0.0023  -0.0274 312 ARG A C   
2629 O O   . ARG A 310 ? 0.2221 0.2736 0.2109 -0.0164 0.0038  -0.0333 312 ARG A O   
2630 C CB  . ARG A 310 ? 0.1921 0.2178 0.1776 -0.0055 0.0006  -0.0221 312 ARG A CB  
2631 C CG  . ARG A 310 ? 0.1953 0.2097 0.1782 -0.0031 0.0001  -0.0190 312 ARG A CG  
2632 C CD  . ARG A 310 ? 0.1819 0.1833 0.1644 0.0003  -0.0016 -0.0178 312 ARG A CD  
2633 N NE  . ARG A 310 ? 0.2190 0.2099 0.1984 0.0014  -0.0018 -0.0162 312 ARG A NE  
2634 C CZ  . ARG A 310 ? 0.2074 0.1869 0.1861 0.0028  -0.0026 -0.0162 312 ARG A CZ  
2635 N NH1 . ARG A 310 ? 0.2219 0.1983 0.2032 0.0034  -0.0035 -0.0179 312 ARG A NH1 
2636 N NH2 . ARG A 310 ? 0.2350 0.2069 0.2102 0.0038  -0.0026 -0.0144 312 ARG A NH2 
2637 N N   . LEU A 311 ? 0.2131 0.2763 0.2008 -0.0087 0.0012  -0.0233 313 LEU A N   
2638 C CA  . LEU A 311 ? 0.1964 0.2706 0.1851 -0.0098 0.0013  -0.0253 313 LEU A CA  
2639 C C   . LEU A 311 ? 0.2262 0.2891 0.2161 -0.0100 0.0016  -0.0284 313 LEU A C   
2640 O O   . LEU A 311 ? 0.2406 0.2897 0.2306 -0.0067 0.0007  -0.0261 313 LEU A O   
2641 C CB  . LEU A 311 ? 0.2282 0.3119 0.2168 -0.0047 0.0005  -0.0187 313 LEU A CB  
2642 C CG  . LEU A 311 ? 0.2818 0.3806 0.2699 -0.0033 0.0005  -0.0147 313 LEU A CG  
2643 C CD1 . LEU A 311 ? 0.2731 0.3775 0.2613 0.0027  0.0003  -0.0074 313 LEU A CD1 
2644 C CD2 . LEU A 311 ? 0.3197 0.4357 0.3081 -0.0090 0.0009  -0.0197 313 LEU A CD2 
2645 N N   . THR A 312 ? 0.1978 0.2672 0.1884 -0.0140 0.0028  -0.0340 314 THR A N   
2646 C CA  . THR A 312 ? 0.2152 0.2773 0.2074 -0.0133 0.0033  -0.0362 314 THR A CA  
2647 C C   . THR A 312 ? 0.2187 0.2875 0.2110 -0.0091 0.0023  -0.0314 314 THR A C   
2648 O O   . THR A 312 ? 0.2279 0.3085 0.2190 -0.0072 0.0017  -0.0270 314 THR A O   
2649 C CB  . THR A 312 ? 0.2665 0.3324 0.2593 -0.0189 0.0057  -0.0443 314 THR A CB  
2650 O OG1 . THR A 312 ? 0.2625 0.3476 0.2541 -0.0212 0.0059  -0.0457 314 THR A OG1 
2651 C CG2 . THR A 312 ? 0.2648 0.3238 0.2577 -0.0237 0.0076  -0.0492 314 THR A CG2 
2652 N N   . ALA A 313 ? 0.2055 0.2667 0.1998 -0.0073 0.0024  -0.0317 315 ALA A N   
2653 C CA  . ALA A 313 ? 0.1891 0.2560 0.1840 -0.0038 0.0021  -0.0272 315 ALA A CA  
2654 C C   . ALA A 313 ? 0.2203 0.3056 0.2136 -0.0055 0.0031  -0.0280 315 ALA A C   
2655 O O   . ALA A 313 ? 0.2571 0.3514 0.2495 -0.0022 0.0029  -0.0221 315 ALA A O   
2656 C CB  . ALA A 313 ? 0.2059 0.2631 0.2037 -0.0024 0.0024  -0.0284 315 ALA A CB  
2657 N N   . ARG A 314 ? 0.2396 0.3307 0.2323 -0.0106 0.0045  -0.0352 316 ARG A N   
2658 C CA  . ARG A 314 ? 0.2610 0.3711 0.2517 -0.0130 0.0053  -0.0370 316 ARG A CA  
2659 C C   . ARG A 314 ? 0.2765 0.4005 0.2652 -0.0130 0.0042  -0.0337 316 ARG A C   
2660 O O   . ARG A 314 ? 0.3166 0.4560 0.3037 -0.0108 0.0038  -0.0292 316 ARG A O   
2661 C CB  . ARG A 314 ? 0.3265 0.4383 0.3170 -0.0191 0.0074  -0.0468 316 ARG A CB  
2662 C CG  . ARG A 314 ? 0.4490 0.5795 0.4373 -0.0215 0.0084  -0.0496 316 ARG A CG  
2663 C CD  . ARG A 314 ? 0.4888 0.6184 0.4778 -0.0178 0.0092  -0.0466 316 ARG A CD  
2664 N NE  . ARG A 314 ? 0.5498 0.6989 0.5357 -0.0190 0.0100  -0.0474 316 ARG A NE  
2665 C CZ  . ARG A 314 ? 0.6388 0.7935 0.6235 -0.0234 0.0123  -0.0554 316 ARG A CZ  
2666 N NH1 . ARG A 314 ? 0.6188 0.7599 0.6058 -0.0266 0.0144  -0.0630 316 ARG A NH1 
2667 N NH2 . ARG A 314 ? 0.7361 0.9101 0.7173 -0.0242 0.0128  -0.0555 316 ARG A NH2 
2668 N N   . GLU A 315 ? 0.2829 0.4022 0.2717 -0.0153 0.0038  -0.0356 317 GLU A N   
2669 C CA  . GLU A 315 ? 0.2920 0.4242 0.2798 -0.0149 0.0027  -0.0320 317 GLU A CA  
2670 C C   . GLU A 315 ? 0.2282 0.3607 0.2159 -0.0077 0.0017  -0.0221 317 GLU A C   
2671 O O   . GLU A 315 ? 0.2944 0.4429 0.2812 -0.0054 0.0013  -0.0173 317 GLU A O   
2672 C CB  . GLU A 315 ? 0.2972 0.4215 0.2856 -0.0181 0.0028  -0.0349 317 GLU A CB  
2673 C CG  . GLU A 315 ? 0.3499 0.4764 0.3385 -0.0258 0.0045  -0.0444 317 GLU A CG  
2674 C CD  . GLU A 315 ? 0.3434 0.4612 0.3328 -0.0284 0.0051  -0.0459 317 GLU A CD  
2675 O OE1 . GLU A 315 ? 0.2707 0.3717 0.2605 -0.0249 0.0047  -0.0423 317 GLU A OE1 
2676 O OE2 . GLU A 315 ? 0.3191 0.4481 0.3088 -0.0341 0.0059  -0.0506 317 GLU A OE2 
2677 N N   . ALA A 316 ? 0.2554 0.3703 0.2443 -0.0039 0.0015  -0.0189 318 ALA A N   
2678 C CA  . ALA A 316 ? 0.1776 0.2903 0.1668 0.0025  0.0013  -0.0102 318 ALA A CA  
2679 C C   . ALA A 316 ? 0.2687 0.3935 0.2575 0.0056  0.0022  -0.0055 318 ALA A C   
2680 O O   . ALA A 316 ? 0.2738 0.4058 0.2623 0.0103  0.0026  0.0019  318 ALA A O   
2681 C CB  . ALA A 316 ? 0.2322 0.3244 0.2228 0.0049  0.0010  -0.0092 318 ALA A CB  
2682 N N   . MET A 317 ? 0.2442 0.3711 0.2331 0.0033  0.0029  -0.0094 319 MET A N   
2683 C CA  A MET A 317 ? 0.2567 0.3953 0.2448 0.0063  0.0040  -0.0047 319 MET A CA  
2684 C CA  B MET A 317 ? 0.2556 0.3943 0.2437 0.0060  0.0040  -0.0051 319 MET A CA  
2685 C C   . MET A 317 ? 0.2455 0.4072 0.2311 0.0056  0.0038  -0.0035 319 MET A C   
2686 O O   . MET A 317 ? 0.2673 0.4405 0.2518 0.0094  0.0048  0.0028  319 MET A O   
2687 C CB  A MET A 317 ? 0.2612 0.3962 0.2501 0.0041  0.0051  -0.0094 319 MET A CB  
2688 C CB  B MET A 317 ? 0.2464 0.3821 0.2351 0.0032  0.0050  -0.0106 319 MET A CB  
2689 C CG  A MET A 317 ? 0.2443 0.3595 0.2364 0.0060  0.0053  -0.0088 319 MET A CG  
2690 C CG  B MET A 317 ? 0.2629 0.3783 0.2548 0.0043  0.0051  -0.0113 319 MET A CG  
2691 S SD  A MET A 317 ? 0.3023 0.4149 0.2963 0.0049  0.0070  -0.0122 319 MET A SD  
2692 S SD  B MET A 317 ? 0.2433 0.3545 0.2370 0.0012  0.0065  -0.0183 319 MET A SD  
2693 C CE  A MET A 317 ? 0.2876 0.4117 0.2791 -0.0015 0.0074  -0.0218 319 MET A CE  
2694 C CE  B MET A 317 ? 0.2898 0.4156 0.2822 0.0040  0.0085  -0.0129 319 MET A CE  
2695 N N   . GLU A 318 ? 0.2516 0.4208 0.2364 0.0010  0.0027  -0.0088 320 GLU A N   
2696 C CA  . GLU A 318 ? 0.2077 0.4004 0.1905 0.0002  0.0020  -0.0076 320 GLU A CA  
2697 C C   . GLU A 318 ? 0.2352 0.4327 0.2188 0.0055  0.0015  0.0008  320 GLU A C   
2698 O O   . GLU A 318 ? 0.2502 0.4687 0.2328 0.0058  0.0007  0.0030  320 GLU A O   
2699 C CB  . GLU A 318 ? 0.3008 0.5005 0.2830 -0.0080 0.0014  -0.0179 320 GLU A CB  
2700 C CG  . GLU A 318 ? 0.3308 0.5244 0.3125 -0.0136 0.0025  -0.0274 320 GLU A CG  
2701 C CD  . GLU A 318 ? 0.3829 0.5950 0.3618 -0.0152 0.0031  -0.0295 320 GLU A CD  
2702 O OE1 . GLU A 318 ? 0.4248 0.6588 0.4017 -0.0180 0.0022  -0.0311 320 GLU A OE1 
2703 O OE2 . GLU A 318 ? 0.3952 0.6008 0.3739 -0.0139 0.0045  -0.0296 320 GLU A OE2 
2704 N N   . HIS A 319 ? 0.2313 0.4107 0.2168 0.0096  0.0019  0.0052  321 HIS A N   
2705 C CA  . HIS A 319 ? 0.2752 0.4571 0.2615 0.0138  0.0019  0.0115  321 HIS A CA  
2706 C C   . HIS A 319 ? 0.2891 0.4828 0.2753 0.0212  0.0032  0.0221  321 HIS A C   
2707 O O   . HIS A 319 ? 0.2695 0.4586 0.2555 0.0245  0.0048  0.0260  321 HIS A O   
2708 C CB  . HIS A 319 ? 0.2718 0.4306 0.2596 0.0155  0.0022  0.0122  321 HIS A CB  
2709 C CG  . HIS A 319 ? 0.2345 0.3949 0.2231 0.0186  0.0024  0.0165  321 HIS A CG  
2710 N ND1 . HIS A 319 ? 0.2446 0.4075 0.2339 0.0259  0.0041  0.0259  321 HIS A ND1 
2711 C CD2 . HIS A 319 ? 0.2768 0.4366 0.2657 0.0154  0.0016  0.0129  321 HIS A CD2 
2712 C CE1 . HIS A 319 ? 0.2767 0.4411 0.2668 0.0273  0.0042  0.0277  321 HIS A CE1 
2713 N NE2 . HIS A 319 ? 0.2774 0.4403 0.2672 0.0209  0.0026  0.0199  321 HIS A NE2 
2714 N N   . PRO A 320 ? 0.2153 0.4243 0.2020 0.0243  0.0030  0.0272  322 PRO A N   
2715 C CA  . PRO A 320 ? 0.2594 0.4798 0.2462 0.0323  0.0048  0.0384  322 PRO A CA  
2716 C C   . PRO A 320 ? 0.2187 0.4203 0.2069 0.0389  0.0078  0.0457  322 PRO A C   
2717 O O   . PRO A 320 ? 0.2757 0.4835 0.2639 0.0451  0.0102  0.0545  322 PRO A O   
2718 C CB  . PRO A 320 ? 0.2820 0.5173 0.2702 0.0343  0.0041  0.0416  322 PRO A CB  
2719 C CG  . PRO A 320 ? 0.2629 0.5056 0.2506 0.0254  0.0015  0.0310  322 PRO A CG  
2720 C CD  . PRO A 320 ? 0.2336 0.4527 0.2209 0.0201  0.0014  0.0228  322 PRO A CD  
2721 N N   . TYR A 321 ? 0.2417 0.4205 0.2311 0.0376  0.0081  0.0423  323 TYR A N   
2722 C CA  . TYR A 321 ? 0.2215 0.3816 0.2123 0.0425  0.0109  0.0476  323 TYR A CA  
2723 C C   . TYR A 321 ? 0.2373 0.3962 0.2279 0.0432  0.0125  0.0495  323 TYR A C   
2724 O O   . TYR A 321 ? 0.2619 0.4135 0.2538 0.0486  0.0158  0.0568  323 TYR A O   
2725 C CB  . TYR A 321 ? 0.2479 0.3860 0.2392 0.0392  0.0100  0.0414  323 TYR A CB  
2726 C CG  . TYR A 321 ? 0.2338 0.3516 0.2266 0.0425  0.0125  0.0444  323 TYR A CG  
2727 C CD1 . TYR A 321 ? 0.2525 0.3661 0.2465 0.0490  0.0158  0.0522  323 TYR A CD1 
2728 C CD2 . TYR A 321 ? 0.2935 0.3962 0.2868 0.0388  0.0116  0.0388  323 TYR A CD2 
2729 C CE1 . TYR A 321 ? 0.2500 0.3448 0.2454 0.0511  0.0184  0.0538  323 TYR A CE1 
2730 C CE2 . TYR A 321 ? 0.2950 0.3804 0.2899 0.0410  0.0137  0.0406  323 TYR A CE2 
2731 C CZ  . TYR A 321 ? 0.3219 0.4030 0.3177 0.0467  0.0171  0.0477  323 TYR A CZ  
2732 O OH  . TYR A 321 ? 0.3239 0.3877 0.3215 0.0482  0.0196  0.0487  323 TYR A OH  
2733 N N   . PHE A 322 ? 0.2626 0.4286 0.2516 0.0378  0.0106  0.0430  324 PHE A N   
2734 C CA  . PHE A 322 ? 0.2377 0.4029 0.2266 0.0380  0.0121  0.0440  324 PHE A CA  
2735 C C   . PHE A 322 ? 0.2190 0.4066 0.2057 0.0406  0.0130  0.0496  324 PHE A C   
2736 O O   . PHE A 322 ? 0.2340 0.4237 0.2199 0.0406  0.0145  0.0505  324 PHE A O   
2737 C CB  . PHE A 322 ? 0.2051 0.3629 0.1937 0.0309  0.0101  0.0336  324 PHE A CB  
2738 C CG  . PHE A 322 ? 0.2705 0.4063 0.2611 0.0290  0.0093  0.0291  324 PHE A CG  
2739 C CD1 . PHE A 322 ? 0.2594 0.3790 0.2524 0.0320  0.0113  0.0327  324 PHE A CD1 
2740 C CD2 . PHE A 322 ? 0.2459 0.3780 0.2361 0.0242  0.0068  0.0215  324 PHE A CD2 
2741 C CE1 . PHE A 322 ? 0.3035 0.4048 0.2980 0.0303  0.0103  0.0285  324 PHE A CE1 
2742 C CE2 . PHE A 322 ? 0.3108 0.4238 0.3023 0.0230  0.0060  0.0183  324 PHE A CE2 
2743 C CZ  . PHE A 322 ? 0.2557 0.3540 0.2492 0.0261  0.0075  0.0217  324 PHE A CZ  
2744 N N   . TYR A 323 ? 0.2444 0.4499 0.2300 0.0433  0.0123  0.0538  325 TYR A N   
2745 C CA  . TYR A 323 ? 0.1790 0.4081 0.1622 0.0462  0.0128  0.0596  325 TYR A CA  
2746 C C   . TYR A 323 ? 0.2190 0.4446 0.2029 0.0537  0.0172  0.0708  325 TYR A C   
2747 O O   . TYR A 323 ? 0.2407 0.4797 0.2221 0.0549  0.0182  0.0742  325 TYR A O   
2748 C CB  . TYR A 323 ? 0.2089 0.4589 0.1917 0.0482  0.0112  0.0627  325 TYR A CB  
2749 C CG  . TYR A 323 ? 0.2651 0.5263 0.2467 0.0401  0.0072  0.0520  325 TYR A CG  
2750 C CD1 . TYR A 323 ? 0.2913 0.5441 0.2720 0.0319  0.0056  0.0404  325 TYR A CD1 
2751 C CD2 . TYR A 323 ? 0.2433 0.5240 0.2253 0.0408  0.0054  0.0536  325 TYR A CD2 
2752 C CE1 . TYR A 323 ? 0.2656 0.5272 0.2455 0.0243  0.0029  0.0306  325 TYR A CE1 
2753 C CE2 . TYR A 323 ? 0.3374 0.6282 0.3189 0.0328  0.0023  0.0435  325 TYR A CE2 
2754 C CZ  . TYR A 323 ? 0.3542 0.6349 0.3346 0.0244  0.0013  0.0319  325 TYR A CZ  
2755 O OH  . TYR A 323 ? 0.3758 0.6654 0.3560 0.0162  -0.0010 0.0218  325 TYR A OH  
2756 N N   . THR A 324 ? 0.2584 0.4654 0.2454 0.0585  0.0202  0.0764  326 THR A N   
2757 C CA  . THR A 324 ? 0.2698 0.4726 0.2580 0.0655  0.0253  0.0873  326 THR A CA  
2758 C C   . THR A 324 ? 0.2838 0.4713 0.2729 0.0627  0.0272  0.0846  326 THR A C   
2759 O O   . THR A 324 ? 0.3014 0.4874 0.2912 0.0675  0.0317  0.0930  326 THR A O   
2760 C CB  . THR A 324 ? 0.3251 0.5144 0.3165 0.0718  0.0287  0.0945  326 THR A CB  
2761 O OG1 . THR A 324 ? 0.3877 0.5752 0.3802 0.0792  0.0344  0.1061  326 THR A OG1 
2762 C CG2 . THR A 324 ? 0.3436 0.5073 0.3374 0.0680  0.0285  0.0875  326 THR A CG2 
2763 N N   . VAL A 325 ? 0.2676 0.4452 0.2570 0.0554  0.0243  0.0735  327 VAL A N   
2764 C CA  . VAL A 325 ? 0.2616 0.4259 0.2525 0.0525  0.0259  0.0703  327 VAL A CA  
2765 C C   . VAL A 325 ? 0.2347 0.4156 0.2227 0.0516  0.0263  0.0709  327 VAL A C   
2766 O O   . VAL A 325 ? 0.2810 0.4783 0.2657 0.0479  0.0231  0.0654  327 VAL A O   
2767 C CB  . VAL A 325 ? 0.2314 0.3815 0.2237 0.0457  0.0225  0.0587  327 VAL A CB  
2768 C CG1 . VAL A 325 ? 0.2743 0.4140 0.2687 0.0426  0.0237  0.0551  327 VAL A CG1 
2769 C CG2 . VAL A 325 ? 0.3216 0.4550 0.3163 0.0468  0.0223  0.0585  327 VAL A CG2 
2770 N N   . VAL A 326 ? 0.2489 0.4254 0.2382 0.0544  0.0307  0.0770  328 VAL A N   
2771 C CA  . VAL A 326 ? 0.2911 0.4830 0.2772 0.0538  0.0317  0.0781  328 VAL A CA  
2772 C C   . VAL A 326 ? 0.3087 0.4980 0.2945 0.0461  0.0289  0.0659  328 VAL A C   
2773 O O   . VAL A 326 ? 0.3166 0.4874 0.3064 0.0432  0.0291  0.0610  328 VAL A O   
2774 C CB  . VAL A 326 ? 0.3786 0.5651 0.3665 0.0586  0.0377  0.0880  328 VAL A CB  
2775 C CG1 . VAL A 326 ? 0.4575 0.6599 0.4418 0.0576  0.0388  0.0885  328 VAL A CG1 
2776 C CG2 . VAL A 326 ? 0.4714 0.6608 0.4596 0.0669  0.0413  0.1008  328 VAL A CG2 
2777 N N   . LYS A 327 ? 0.3793 0.5876 0.3606 0.0430  0.0266  0.0611  329 LYS A N   
2778 C CA  . LYS A 327 ? 0.5099 0.7168 0.4907 0.0359  0.0246  0.0494  329 LYS A CA  
2779 C C   . LYS A 327 ? 0.6598 0.8723 0.6394 0.0359  0.0278  0.0508  329 LYS A C   
2780 O O   . LYS A 327 ? 0.6477 0.8756 0.6238 0.0400  0.0301  0.0589  329 LYS A O   
2781 C CB  . LYS A 327 ? 0.5322 0.7554 0.5090 0.0315  0.0207  0.0417  329 LYS A CB  
2782 C CG  . LYS A 327 ? 0.5734 0.7938 0.5512 0.0314  0.0178  0.0406  329 LYS A CG  
2783 C CD  . LYS A 327 ? 0.5028 0.6983 0.4853 0.0298  0.0171  0.0365  329 LYS A CD  
2784 C CE  . LYS A 327 ? 0.3829 0.5768 0.3658 0.0288  0.0142  0.0342  329 LYS A CE  
2785 N NZ  . LYS A 327 ? 0.4129 0.6230 0.3940 0.0339  0.0144  0.0427  329 LYS A NZ  
2786 N N   . ASP A 328 ? 0.7952 0.9955 0.7777 0.0316  0.0281  0.0433  330 ASP A N   
2787 C CA  . ASP A 328 ? 0.8913 1.0950 0.8734 0.0313  0.0315  0.0439  330 ASP A CA  
2788 C C   . ASP A 328 ? 0.8757 1.0939 0.8534 0.0263  0.0302  0.0346  330 ASP A C   
2789 O O   . ASP A 328 ? 0.8500 1.0891 0.8218 0.0269  0.0300  0.0364  330 ASP A O   
2790 C CB  . ASP A 328 ? 0.9885 1.1712 0.9773 0.0301  0.0332  0.0419  330 ASP A CB  
2791 C CG  . ASP A 328 ? 1.0648 1.2315 1.0582 0.0338  0.0344  0.0488  330 ASP A CG  
2792 O OD1 . ASP A 328 ? 1.0661 1.2194 1.0624 0.0320  0.0315  0.0441  330 ASP A OD1 
2793 O OD2 . ASP A 328 ? 1.1024 1.2699 1.0963 0.0385  0.0385  0.0590  330 ASP A OD2 
# 
