data_8YSL
# 
_entry.id   8YSL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8YSL         pdb_00008ysl 10.2210/pdb8ysl/pdb 
WWPDB D_1300046304 ?            ?                   
# 
_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       2025-01-29 
# 
_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                        8YSL 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              chyeah6599@nchu.edu.tw 
_pdbx_contact_author.name_first         Yeh 
_pdbx_contact_author.name_last          Chen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7740-0446 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, Y.-C.' 1 ? 
'Yang, C.-S.' 2 ? 
'Hou, M.-H.'  3 ? 
'Chen, Y.'    4 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            295 
_citation.language                  ? 
_citation.page_first                139534 
_citation.page_last                 139534 
_citation.title                     
'Structural insights into signaling promiscuity of the CBASS anti-phage defense system from a radiation-resistant bacterium.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2025.139534 
_citation.pdbx_database_id_PubMed   39761885 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yang, C.S.'  1 ? 
primary 'Shie, M.Y.'  2 ? 
primary 'Huang, S.W.' 3 ? 
primary 'Wang, Y.C.'  4 ? 
primary 'Hou, M.H.'   5 ? 
primary 'Chen, C.J.'  6 ? 
primary 'Chen, Y.'    7 ? 
# 
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 Nucleotidyltransferase      39349.109 1   ? ? ? 'The first residue should be annotated as Met0' 
2 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE" 507.181   1   ? ? ? ?                                               
3 non-polymer syn 
;URIDINE 5'-TRIPHOSPHATE
;
484.141   1   ? ? ? ?                                               
4 non-polymer syn 'MAGNESIUM ION'             24.305    2   ? ? ? ?                                               
5 water       nat water                       18.015    288 ? ? ? ?                                               
# 
_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       
;MMAPVQKQFREFHDRIKLAQYDENQTLRDERDAVLTAVREGLKKVFADRGEAAPTFTPFNQGSYAMNTGVKPLEGGEYDI
DVGIILNIAKDDHDPVEVKKWIRDALKDYGNGAEIRRSCVTVFKPGYHVDLAVYADPELSGGTLCIAKGKENSGDEHRLW
QISDPQGFQDRIASKLSGDDAAQFRRCIRYLKRWRDFRFSSDGNAAPLGIGLTAAAYWWFQVSKRTDPVSQNVTYDDRDA
LEQFVQTMLDNFHDTWDSKDQRSYPRLTVELPVQPYNDVFEKMTGMQMESFKSKLQALLNALKTAKSRLELHDACKALAD
HFGSEFPVPEKDKSAVHTAPAIVGSGSSG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MMAPVQKQFREFHDRIKLAQYDENQTLRDERDAVLTAVREGLKKVFADRGEAAPTFTPFNQGSYAMNTGVKPLEGGEYDI
DVGIILNIAKDDHDPVEVKKWIRDALKDYGNGAEIRRSCVTVFKPGYHVDLAVYADPELSGGTLCIAKGKENSGDEHRLW
QISDPQGFQDRIASKLSGDDAAQFRRCIRYLKRWRDFRFSSDGNAAPLGIGLTAAAYWWFQVSKRTDPVSQNVTYDDRDA
LEQFVQTMLDNFHDTWDSKDQRSYPRLTVELPVQPYNDVFEKMTGMQMESFKSKLQALLNALKTAKSRLELHDACKALAD
HFGSEFPVPEKDKSAVHTAPAIVGSGSSG
;
_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 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
3 
;URIDINE 5'-TRIPHOSPHATE
;
UTP 
4 'MAGNESIUM ION'             MG  
5 water                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   MET n 
1 3   ALA n 
1 4   PRO n 
1 5   VAL n 
1 6   GLN n 
1 7   LYS n 
1 8   GLN n 
1 9   PHE n 
1 10  ARG n 
1 11  GLU n 
1 12  PHE n 
1 13  HIS n 
1 14  ASP n 
1 15  ARG n 
1 16  ILE n 
1 17  LYS n 
1 18  LEU n 
1 19  ALA n 
1 20  GLN n 
1 21  TYR n 
1 22  ASP n 
1 23  GLU n 
1 24  ASN n 
1 25  GLN n 
1 26  THR n 
1 27  LEU n 
1 28  ARG n 
1 29  ASP n 
1 30  GLU n 
1 31  ARG n 
1 32  ASP n 
1 33  ALA n 
1 34  VAL n 
1 35  LEU n 
1 36  THR n 
1 37  ALA n 
1 38  VAL n 
1 39  ARG n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  LYS n 
1 44  LYS n 
1 45  VAL n 
1 46  PHE n 
1 47  ALA n 
1 48  ASP n 
1 49  ARG n 
1 50  GLY n 
1 51  GLU n 
1 52  ALA n 
1 53  ALA n 
1 54  PRO n 
1 55  THR n 
1 56  PHE n 
1 57  THR n 
1 58  PRO n 
1 59  PHE n 
1 60  ASN n 
1 61  GLN n 
1 62  GLY n 
1 63  SER n 
1 64  TYR n 
1 65  ALA n 
1 66  MET n 
1 67  ASN n 
1 68  THR n 
1 69  GLY n 
1 70  VAL n 
1 71  LYS n 
1 72  PRO n 
1 73  LEU n 
1 74  GLU n 
1 75  GLY n 
1 76  GLY n 
1 77  GLU n 
1 78  TYR n 
1 79  ASP n 
1 80  ILE n 
1 81  ASP n 
1 82  VAL n 
1 83  GLY n 
1 84  ILE n 
1 85  ILE n 
1 86  LEU n 
1 87  ASN n 
1 88  ILE n 
1 89  ALA n 
1 90  LYS n 
1 91  ASP n 
1 92  ASP n 
1 93  HIS n 
1 94  ASP n 
1 95  PRO n 
1 96  VAL n 
1 97  GLU n 
1 98  VAL n 
1 99  LYS n 
1 100 LYS n 
1 101 TRP n 
1 102 ILE n 
1 103 ARG n 
1 104 ASP n 
1 105 ALA n 
1 106 LEU n 
1 107 LYS n 
1 108 ASP n 
1 109 TYR n 
1 110 GLY n 
1 111 ASN n 
1 112 GLY n 
1 113 ALA n 
1 114 GLU n 
1 115 ILE n 
1 116 ARG n 
1 117 ARG n 
1 118 SER n 
1 119 CYS n 
1 120 VAL n 
1 121 THR n 
1 122 VAL n 
1 123 PHE n 
1 124 LYS n 
1 125 PRO n 
1 126 GLY n 
1 127 TYR n 
1 128 HIS n 
1 129 VAL n 
1 130 ASP n 
1 131 LEU n 
1 132 ALA n 
1 133 VAL n 
1 134 TYR n 
1 135 ALA n 
1 136 ASP n 
1 137 PRO n 
1 138 GLU n 
1 139 LEU n 
1 140 SER n 
1 141 GLY n 
1 142 GLY n 
1 143 THR n 
1 144 LEU n 
1 145 CYS n 
1 146 ILE n 
1 147 ALA n 
1 148 LYS n 
1 149 GLY n 
1 150 LYS n 
1 151 GLU n 
1 152 ASN n 
1 153 SER n 
1 154 GLY n 
1 155 ASP n 
1 156 GLU n 
1 157 HIS n 
1 158 ARG n 
1 159 LEU n 
1 160 TRP n 
1 161 GLN n 
1 162 ILE n 
1 163 SER n 
1 164 ASP n 
1 165 PRO n 
1 166 GLN n 
1 167 GLY n 
1 168 PHE n 
1 169 GLN n 
1 170 ASP n 
1 171 ARG n 
1 172 ILE n 
1 173 ALA n 
1 174 SER n 
1 175 LYS n 
1 176 LEU n 
1 177 SER n 
1 178 GLY n 
1 179 ASP n 
1 180 ASP n 
1 181 ALA n 
1 182 ALA n 
1 183 GLN n 
1 184 PHE n 
1 185 ARG n 
1 186 ARG n 
1 187 CYS n 
1 188 ILE n 
1 189 ARG n 
1 190 TYR n 
1 191 LEU n 
1 192 LYS n 
1 193 ARG n 
1 194 TRP n 
1 195 ARG n 
1 196 ASP n 
1 197 PHE n 
1 198 ARG n 
1 199 PHE n 
1 200 SER n 
1 201 SER n 
1 202 ASP n 
1 203 GLY n 
1 204 ASN n 
1 205 ALA n 
1 206 ALA n 
1 207 PRO n 
1 208 LEU n 
1 209 GLY n 
1 210 ILE n 
1 211 GLY n 
1 212 LEU n 
1 213 THR n 
1 214 ALA n 
1 215 ALA n 
1 216 ALA n 
1 217 TYR n 
1 218 TRP n 
1 219 TRP n 
1 220 PHE n 
1 221 GLN n 
1 222 VAL n 
1 223 SER n 
1 224 LYS n 
1 225 ARG n 
1 226 THR n 
1 227 ASP n 
1 228 PRO n 
1 229 VAL n 
1 230 SER n 
1 231 GLN n 
1 232 ASN n 
1 233 VAL n 
1 234 THR n 
1 235 TYR n 
1 236 ASP n 
1 237 ASP n 
1 238 ARG n 
1 239 ASP n 
1 240 ALA n 
1 241 LEU n 
1 242 GLU n 
1 243 GLN n 
1 244 PHE n 
1 245 VAL n 
1 246 GLN n 
1 247 THR n 
1 248 MET n 
1 249 LEU n 
1 250 ASP n 
1 251 ASN n 
1 252 PHE n 
1 253 HIS n 
1 254 ASP n 
1 255 THR n 
1 256 TRP n 
1 257 ASP n 
1 258 SER n 
1 259 LYS n 
1 260 ASP n 
1 261 GLN n 
1 262 ARG n 
1 263 SER n 
1 264 TYR n 
1 265 PRO n 
1 266 ARG n 
1 267 LEU n 
1 268 THR n 
1 269 VAL n 
1 270 GLU n 
1 271 LEU n 
1 272 PRO n 
1 273 VAL n 
1 274 GLN n 
1 275 PRO n 
1 276 TYR n 
1 277 ASN n 
1 278 ASP n 
1 279 VAL n 
1 280 PHE n 
1 281 GLU n 
1 282 LYS n 
1 283 MET n 
1 284 THR n 
1 285 GLY n 
1 286 MET n 
1 287 GLN n 
1 288 MET n 
1 289 GLU n 
1 290 SER n 
1 291 PHE n 
1 292 LYS n 
1 293 SER n 
1 294 LYS n 
1 295 LEU n 
1 296 GLN n 
1 297 ALA n 
1 298 LEU n 
1 299 LEU n 
1 300 ASN n 
1 301 ALA n 
1 302 LEU n 
1 303 LYS n 
1 304 THR n 
1 305 ALA n 
1 306 LYS n 
1 307 SER n 
1 308 ARG n 
1 309 LEU n 
1 310 GLU n 
1 311 LEU n 
1 312 HIS n 
1 313 ASP n 
1 314 ALA n 
1 315 CYS n 
1 316 LYS n 
1 317 ALA n 
1 318 LEU n 
1 319 ALA n 
1 320 ASP n 
1 321 HIS n 
1 322 PHE n 
1 323 GLY n 
1 324 SER n 
1 325 GLU n 
1 326 PHE n 
1 327 PRO n 
1 328 VAL n 
1 329 PRO n 
1 330 GLU n 
1 331 LYS n 
1 332 ASP n 
1 333 LYS n 
1 334 SER n 
1 335 ALA n 
1 336 VAL n 
1 337 HIS n 
1 338 THR n 
1 339 ALA n 
1 340 PRO n 
1 341 ALA n 
1 342 ILE n 
1 343 VAL n 
1 344 GLY n 
1 345 SER n 
1 346 GLY n 
1 347 SER n 
1 348 SER n 
1 349 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   349 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 DVJ83_15700 
_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      'Deinococcus wulumuqiensis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     980427 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                       ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
UTP non-polymer         . 
;URIDINE 5'-TRIPHOSPHATE
;
? 'C9 H15 N2 O15 P3'  484.141 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   0   MET MET A . n 
A 1 2   MET 2   1   1   MET MET A . n 
A 1 3   ALA 3   2   2   ALA ALA A . n 
A 1 4   PRO 4   3   3   PRO PRO A . n 
A 1 5   VAL 5   4   4   VAL VAL A . n 
A 1 6   GLN 6   5   5   GLN GLN A . n 
A 1 7   LYS 7   6   6   LYS LYS A . n 
A 1 8   GLN 8   7   7   GLN GLN A . n 
A 1 9   PHE 9   8   8   PHE PHE A . n 
A 1 10  ARG 10  9   9   ARG ARG A . n 
A 1 11  GLU 11  10  10  GLU GLU A . n 
A 1 12  PHE 12  11  11  PHE PHE A . n 
A 1 13  HIS 13  12  12  HIS HIS A . n 
A 1 14  ASP 14  13  13  ASP ASP A . n 
A 1 15  ARG 15  14  14  ARG ARG A . n 
A 1 16  ILE 16  15  15  ILE ILE A . n 
A 1 17  LYS 17  16  16  LYS LYS A . n 
A 1 18  LEU 18  17  17  LEU LEU A . n 
A 1 19  ALA 19  18  18  ALA ALA A . n 
A 1 20  GLN 20  19  19  GLN GLN A . n 
A 1 21  TYR 21  20  20  TYR TYR A . n 
A 1 22  ASP 22  21  21  ASP ASP A . n 
A 1 23  GLU 23  22  22  GLU GLU A . n 
A 1 24  ASN 24  23  23  ASN ASN A . n 
A 1 25  GLN 25  24  24  GLN GLN A . n 
A 1 26  THR 26  25  25  THR THR A . n 
A 1 27  LEU 27  26  26  LEU LEU A . n 
A 1 28  ARG 28  27  27  ARG ARG A . n 
A 1 29  ASP 29  28  28  ASP ASP A . n 
A 1 30  GLU 30  29  29  GLU GLU A . n 
A 1 31  ARG 31  30  30  ARG ARG A . n 
A 1 32  ASP 32  31  31  ASP ASP A . n 
A 1 33  ALA 33  32  32  ALA ALA A . n 
A 1 34  VAL 34  33  33  VAL VAL A . n 
A 1 35  LEU 35  34  34  LEU LEU A . n 
A 1 36  THR 36  35  35  THR THR A . n 
A 1 37  ALA 37  36  36  ALA ALA A . n 
A 1 38  VAL 38  37  37  VAL VAL A . n 
A 1 39  ARG 39  38  38  ARG ARG A . n 
A 1 40  GLU 40  39  39  GLU GLU A . n 
A 1 41  GLY 41  40  40  GLY GLY A . n 
A 1 42  LEU 42  41  41  LEU LEU A . n 
A 1 43  LYS 43  42  42  LYS LYS A . n 
A 1 44  LYS 44  43  43  LYS LYS A . n 
A 1 45  VAL 45  44  44  VAL VAL A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  ALA 47  46  46  ALA ALA A . n 
A 1 48  ASP 48  47  47  ASP ASP A . n 
A 1 49  ARG 49  48  48  ARG ARG A . n 
A 1 50  GLY 50  49  49  GLY GLY A . n 
A 1 51  GLU 51  50  50  GLU GLU A . n 
A 1 52  ALA 52  51  51  ALA ALA A . n 
A 1 53  ALA 53  52  52  ALA ALA A . n 
A 1 54  PRO 54  53  53  PRO PRO A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  PHE 56  55  55  PHE PHE A . n 
A 1 57  THR 57  56  56  THR THR A . n 
A 1 58  PRO 58  57  57  PRO PRO A . n 
A 1 59  PHE 59  58  58  PHE PHE A . n 
A 1 60  ASN 60  59  59  ASN ASN A . n 
A 1 61  GLN 61  60  60  GLN GLN A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  SER 63  62  62  SER SER A . n 
A 1 64  TYR 64  63  63  TYR TYR A . n 
A 1 65  ALA 65  64  64  ALA ALA A . n 
A 1 66  MET 66  65  65  MET MET A . n 
A 1 67  ASN 67  66  66  ASN ASN A . n 
A 1 68  THR 68  67  67  THR THR A . n 
A 1 69  GLY 69  68  68  GLY GLY A . n 
A 1 70  VAL 70  69  69  VAL VAL A . n 
A 1 71  LYS 71  70  70  LYS LYS A . n 
A 1 72  PRO 72  71  71  PRO PRO A . n 
A 1 73  LEU 73  72  72  LEU LEU A . n 
A 1 74  GLU 74  73  73  GLU GLU A . n 
A 1 75  GLY 75  74  74  GLY GLY A . n 
A 1 76  GLY 76  75  75  GLY GLY A . n 
A 1 77  GLU 77  76  76  GLU GLU A . n 
A 1 78  TYR 78  77  77  TYR TYR A . n 
A 1 79  ASP 79  78  78  ASP ASP A . n 
A 1 80  ILE 80  79  79  ILE ILE A . n 
A 1 81  ASP 81  80  80  ASP ASP A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  ILE 84  83  83  ILE ILE A . n 
A 1 85  ILE 85  84  84  ILE ILE A . n 
A 1 86  LEU 86  85  85  LEU LEU A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  ILE 88  87  87  ILE ILE A . n 
A 1 89  ALA 89  88  88  ALA ALA A . n 
A 1 90  LYS 90  89  89  LYS LYS A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  ASP 92  91  91  ASP ASP A . n 
A 1 93  HIS 93  92  92  HIS HIS A . n 
A 1 94  ASP 94  93  93  ASP ASP A . n 
A 1 95  PRO 95  94  94  PRO PRO A . n 
A 1 96  VAL 96  95  95  VAL VAL A . n 
A 1 97  GLU 97  96  96  GLU GLU A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  LYS 99  98  98  LYS LYS A . n 
A 1 100 LYS 100 99  99  LYS LYS A . n 
A 1 101 TRP 101 100 100 TRP TRP A . n 
A 1 102 ILE 102 101 101 ILE ILE A . n 
A 1 103 ARG 103 102 102 ARG ARG A . n 
A 1 104 ASP 104 103 103 ASP ASP A . n 
A 1 105 ALA 105 104 104 ALA ALA A . n 
A 1 106 LEU 106 105 105 LEU LEU A . n 
A 1 107 LYS 107 106 106 LYS LYS A . n 
A 1 108 ASP 108 107 107 ASP ASP A . n 
A 1 109 TYR 109 108 108 TYR TYR A . n 
A 1 110 GLY 110 109 109 GLY GLY A . n 
A 1 111 ASN 111 110 110 ASN ASN A . n 
A 1 112 GLY 112 111 111 GLY GLY A . n 
A 1 113 ALA 113 112 112 ALA ALA A . n 
A 1 114 GLU 114 113 113 GLU GLU A . n 
A 1 115 ILE 115 114 114 ILE ILE A . n 
A 1 116 ARG 116 115 115 ARG ARG A . n 
A 1 117 ARG 117 116 116 ARG ARG A . n 
A 1 118 SER 118 117 117 SER SER A . n 
A 1 119 CYS 119 118 118 CYS CYS A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 THR 121 120 120 THR THR A . n 
A 1 122 VAL 122 121 121 VAL VAL A . n 
A 1 123 PHE 123 122 122 PHE PHE A . n 
A 1 124 LYS 124 123 123 LYS LYS A . n 
A 1 125 PRO 125 124 124 PRO PRO A . n 
A 1 126 GLY 126 125 125 GLY GLY A . n 
A 1 127 TYR 127 126 126 TYR TYR A . n 
A 1 128 HIS 128 127 127 HIS HIS A . n 
A 1 129 VAL 129 128 128 VAL VAL A . n 
A 1 130 ASP 130 129 129 ASP ASP A . n 
A 1 131 LEU 131 130 130 LEU LEU A . n 
A 1 132 ALA 132 131 131 ALA ALA A . n 
A 1 133 VAL 133 132 132 VAL VAL A . n 
A 1 134 TYR 134 133 133 TYR TYR A . n 
A 1 135 ALA 135 134 134 ALA ALA A . n 
A 1 136 ASP 136 135 135 ASP ASP A . n 
A 1 137 PRO 137 136 136 PRO PRO A . n 
A 1 138 GLU 138 137 137 GLU GLU A . n 
A 1 139 LEU 139 138 138 LEU LEU A . n 
A 1 140 SER 140 139 139 SER SER A . n 
A 1 141 GLY 141 140 140 GLY GLY A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 THR 143 142 142 THR THR A . n 
A 1 144 LEU 144 143 143 LEU LEU A . n 
A 1 145 CYS 145 144 144 CYS CYS A . n 
A 1 146 ILE 146 145 145 ILE ILE A . n 
A 1 147 ALA 147 146 146 ALA ALA A . n 
A 1 148 LYS 148 147 147 LYS LYS A . n 
A 1 149 GLY 149 148 148 GLY GLY A . n 
A 1 150 LYS 150 149 149 LYS LYS A . n 
A 1 151 GLU 151 150 150 GLU GLU A . n 
A 1 152 ASN 152 151 151 ASN ASN A . n 
A 1 153 SER 153 152 152 SER SER A . n 
A 1 154 GLY 154 153 153 GLY GLY A . n 
A 1 155 ASP 155 154 154 ASP ASP A . n 
A 1 156 GLU 156 155 155 GLU GLU A . n 
A 1 157 HIS 157 156 156 HIS HIS A . n 
A 1 158 ARG 158 157 157 ARG ARG A . n 
A 1 159 LEU 159 158 158 LEU LEU A . n 
A 1 160 TRP 160 159 159 TRP TRP A . n 
A 1 161 GLN 161 160 160 GLN GLN A . n 
A 1 162 ILE 162 161 161 ILE ILE A . n 
A 1 163 SER 163 162 162 SER SER A . n 
A 1 164 ASP 164 163 163 ASP ASP A . n 
A 1 165 PRO 165 164 164 PRO PRO A . n 
A 1 166 GLN 166 165 165 GLN GLN A . n 
A 1 167 GLY 167 166 166 GLY GLY A . n 
A 1 168 PHE 168 167 167 PHE PHE A . n 
A 1 169 GLN 169 168 168 GLN GLN A . n 
A 1 170 ASP 170 169 169 ASP ASP A . n 
A 1 171 ARG 171 170 170 ARG ARG A . n 
A 1 172 ILE 172 171 171 ILE ILE A . n 
A 1 173 ALA 173 172 172 ALA ALA A . n 
A 1 174 SER 174 173 173 SER SER A . n 
A 1 175 LYS 175 174 174 LYS LYS A . n 
A 1 176 LEU 176 175 175 LEU LEU A . n 
A 1 177 SER 177 176 176 SER SER A . n 
A 1 178 GLY 178 177 177 GLY GLY A . n 
A 1 179 ASP 179 178 178 ASP ASP A . n 
A 1 180 ASP 180 179 179 ASP ASP A . n 
A 1 181 ALA 181 180 180 ALA ALA A . n 
A 1 182 ALA 182 181 181 ALA ALA A . n 
A 1 183 GLN 183 182 182 GLN GLN A . n 
A 1 184 PHE 184 183 183 PHE PHE A . n 
A 1 185 ARG 185 184 184 ARG ARG A . n 
A 1 186 ARG 186 185 185 ARG ARG A . n 
A 1 187 CYS 187 186 186 CYS CYS A . n 
A 1 188 ILE 188 187 187 ILE ILE A . n 
A 1 189 ARG 189 188 188 ARG ARG A . n 
A 1 190 TYR 190 189 189 TYR TYR A . n 
A 1 191 LEU 191 190 190 LEU LEU A . n 
A 1 192 LYS 192 191 191 LYS LYS A . n 
A 1 193 ARG 193 192 192 ARG ARG A . n 
A 1 194 TRP 194 193 193 TRP TRP A . n 
A 1 195 ARG 195 194 194 ARG ARG A . n 
A 1 196 ASP 196 195 195 ASP ASP A . n 
A 1 197 PHE 197 196 196 PHE PHE A . n 
A 1 198 ARG 198 197 197 ARG ARG A . n 
A 1 199 PHE 199 198 198 PHE PHE A . n 
A 1 200 SER 200 199 199 SER SER A . n 
A 1 201 SER 201 200 200 SER SER A . n 
A 1 202 ASP 202 201 201 ASP ASP A . n 
A 1 203 GLY 203 202 202 GLY GLY A . n 
A 1 204 ASN 204 203 203 ASN ASN A . n 
A 1 205 ALA 205 204 204 ALA ALA A . n 
A 1 206 ALA 206 205 205 ALA ALA A . n 
A 1 207 PRO 207 206 206 PRO PRO A . n 
A 1 208 LEU 208 207 207 LEU LEU A . n 
A 1 209 GLY 209 208 208 GLY GLY A . n 
A 1 210 ILE 210 209 209 ILE ILE A . n 
A 1 211 GLY 211 210 210 GLY GLY A . n 
A 1 212 LEU 212 211 211 LEU LEU A . n 
A 1 213 THR 213 212 212 THR THR A . n 
A 1 214 ALA 214 213 213 ALA ALA A . n 
A 1 215 ALA 215 214 214 ALA ALA A . n 
A 1 216 ALA 216 215 215 ALA ALA A . n 
A 1 217 TYR 217 216 216 TYR TYR A . n 
A 1 218 TRP 218 217 217 TRP TRP A . n 
A 1 219 TRP 219 218 218 TRP TRP A . n 
A 1 220 PHE 220 219 219 PHE PHE A . n 
A 1 221 GLN 221 220 220 GLN GLN A . n 
A 1 222 VAL 222 221 221 VAL VAL A . n 
A 1 223 SER 223 222 222 SER SER A . n 
A 1 224 LYS 224 223 223 LYS LYS A . n 
A 1 225 ARG 225 224 224 ARG ARG A . n 
A 1 226 THR 226 225 225 THR THR A . n 
A 1 227 ASP 227 226 226 ASP ASP A . n 
A 1 228 PRO 228 227 227 PRO PRO A . n 
A 1 229 VAL 229 228 228 VAL VAL A . n 
A 1 230 SER 230 229 229 SER SER A . n 
A 1 231 GLN 231 230 230 GLN GLN A . n 
A 1 232 ASN 232 231 231 ASN ASN A . n 
A 1 233 VAL 233 232 232 VAL VAL A . n 
A 1 234 THR 234 233 233 THR THR A . n 
A 1 235 TYR 235 234 234 TYR TYR A . n 
A 1 236 ASP 236 235 235 ASP ASP A . n 
A 1 237 ASP 237 236 236 ASP ASP A . n 
A 1 238 ARG 238 237 237 ARG ARG A . n 
A 1 239 ASP 239 238 238 ASP ASP A . n 
A 1 240 ALA 240 239 239 ALA ALA A . n 
A 1 241 LEU 241 240 240 LEU LEU A . n 
A 1 242 GLU 242 241 241 GLU GLU A . n 
A 1 243 GLN 243 242 242 GLN GLN A . n 
A 1 244 PHE 244 243 243 PHE PHE A . n 
A 1 245 VAL 245 244 244 VAL VAL A . n 
A 1 246 GLN 246 245 245 GLN GLN A . n 
A 1 247 THR 247 246 246 THR THR A . n 
A 1 248 MET 248 247 247 MET MET A . n 
A 1 249 LEU 249 248 248 LEU LEU A . n 
A 1 250 ASP 250 249 249 ASP ASP A . n 
A 1 251 ASN 251 250 250 ASN ASN A . n 
A 1 252 PHE 252 251 251 PHE PHE A . n 
A 1 253 HIS 253 252 252 HIS HIS A . n 
A 1 254 ASP 254 253 253 ASP ASP A . n 
A 1 255 THR 255 254 254 THR THR A . n 
A 1 256 TRP 256 255 255 TRP TRP A . n 
A 1 257 ASP 257 256 256 ASP ASP A . n 
A 1 258 SER 258 257 257 SER SER A . n 
A 1 259 LYS 259 258 258 LYS LYS A . n 
A 1 260 ASP 260 259 259 ASP ASP A . n 
A 1 261 GLN 261 260 260 GLN GLN A . n 
A 1 262 ARG 262 261 261 ARG ARG A . n 
A 1 263 SER 263 262 262 SER SER A . n 
A 1 264 TYR 264 263 263 TYR TYR A . n 
A 1 265 PRO 265 264 264 PRO PRO A . n 
A 1 266 ARG 266 265 265 ARG ARG A . n 
A 1 267 LEU 267 266 266 LEU LEU A . n 
A 1 268 THR 268 267 267 THR THR A . n 
A 1 269 VAL 269 268 268 VAL VAL A . n 
A 1 270 GLU 270 269 269 GLU GLU A . n 
A 1 271 LEU 271 270 270 LEU LEU A . n 
A 1 272 PRO 272 271 271 PRO PRO A . n 
A 1 273 VAL 273 272 272 VAL VAL A . n 
A 1 274 GLN 274 273 273 GLN GLN A . n 
A 1 275 PRO 275 274 274 PRO PRO A . n 
A 1 276 TYR 276 275 275 TYR TYR A . n 
A 1 277 ASN 277 276 276 ASN ASN A . n 
A 1 278 ASP 278 277 277 ASP ASP A . n 
A 1 279 VAL 279 278 278 VAL VAL A . n 
A 1 280 PHE 280 279 279 PHE PHE A . n 
A 1 281 GLU 281 280 280 GLU GLU A . n 
A 1 282 LYS 282 281 281 LYS LYS A . n 
A 1 283 MET 283 282 282 MET MET A . n 
A 1 284 THR 284 283 283 THR THR A . n 
A 1 285 GLY 285 284 284 GLY GLY A . n 
A 1 286 MET 286 285 285 MET MET A . n 
A 1 287 GLN 287 286 286 GLN GLN A . n 
A 1 288 MET 288 287 287 MET MET A . n 
A 1 289 GLU 289 288 288 GLU GLU A . n 
A 1 290 SER 290 289 289 SER SER A . n 
A 1 291 PHE 291 290 290 PHE PHE A . n 
A 1 292 LYS 292 291 291 LYS LYS A . n 
A 1 293 SER 293 292 292 SER SER A . n 
A 1 294 LYS 294 293 293 LYS LYS A . n 
A 1 295 LEU 295 294 294 LEU LEU A . n 
A 1 296 GLN 296 295 295 GLN GLN A . n 
A 1 297 ALA 297 296 296 ALA ALA A . n 
A 1 298 LEU 298 297 297 LEU LEU A . n 
A 1 299 LEU 299 298 298 LEU LEU A . n 
A 1 300 ASN 300 299 299 ASN ASN A . n 
A 1 301 ALA 301 300 300 ALA ALA A . n 
A 1 302 LEU 302 301 301 LEU LEU A . n 
A 1 303 LYS 303 302 302 LYS LYS A . n 
A 1 304 THR 304 303 303 THR THR A . n 
A 1 305 ALA 305 304 304 ALA ALA A . n 
A 1 306 LYS 306 305 305 LYS LYS A . n 
A 1 307 SER 307 306 306 SER SER A . n 
A 1 308 ARG 308 307 307 ARG ARG A . n 
A 1 309 LEU 309 308 308 LEU LEU A . n 
A 1 310 GLU 310 309 309 GLU GLU A . n 
A 1 311 LEU 311 310 310 LEU LEU A . n 
A 1 312 HIS 312 311 311 HIS HIS A . n 
A 1 313 ASP 313 312 312 ASP ASP A . n 
A 1 314 ALA 314 313 313 ALA ALA A . n 
A 1 315 CYS 315 314 314 CYS CYS A . n 
A 1 316 LYS 316 315 315 LYS LYS A . n 
A 1 317 ALA 317 316 316 ALA ALA A . n 
A 1 318 LEU 318 317 317 LEU LEU A . n 
A 1 319 ALA 319 318 318 ALA ALA A . n 
A 1 320 ASP 320 319 319 ASP ASP A . n 
A 1 321 HIS 321 320 320 HIS HIS A . n 
A 1 322 PHE 322 321 321 PHE PHE A . n 
A 1 323 GLY 323 322 322 GLY GLY A . n 
A 1 324 SER 324 323 323 SER SER A . n 
A 1 325 GLU 325 324 324 GLU GLU A . n 
A 1 326 PHE 326 325 325 PHE PHE A . n 
A 1 327 PRO 327 326 326 PRO PRO A . n 
A 1 328 VAL 328 327 327 VAL VAL A . n 
A 1 329 PRO 329 328 328 PRO PRO A . n 
A 1 330 GLU 330 329 329 GLU GLU A . n 
A 1 331 LYS 331 330 330 LYS LYS A . n 
A 1 332 ASP 332 331 ?   ?   ?   A . n 
A 1 333 LYS 333 332 ?   ?   ?   A . n 
A 1 334 SER 334 333 ?   ?   ?   A . n 
A 1 335 ALA 335 334 ?   ?   ?   A . n 
A 1 336 VAL 336 335 ?   ?   ?   A . n 
A 1 337 HIS 337 336 ?   ?   ?   A . n 
A 1 338 THR 338 337 ?   ?   ?   A . n 
A 1 339 ALA 339 338 ?   ?   ?   A . n 
A 1 340 PRO 340 339 ?   ?   ?   A . n 
A 1 341 ALA 341 340 ?   ?   ?   A . n 
A 1 342 ILE 342 341 ?   ?   ?   A . n 
A 1 343 VAL 343 342 ?   ?   ?   A . n 
A 1 344 GLY 344 343 ?   ?   ?   A . n 
A 1 345 SER 345 344 ?   ?   ?   A . n 
A 1 346 GLY 346 345 ?   ?   ?   A . n 
A 1 347 SER 347 346 ?   ?   ?   A . n 
A 1 348 SER 348 347 ?   ?   ?   A . n 
A 1 349 GLY 349 348 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 UTP ? ? UTP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 ATP 1   401 401 ATP ATP A . 
C 3 UTP 1   402 402 UTP UTP A . 
D 4 MG  1   403 501 MG  MG  A . 
E 4 MG  1   404 502 MG  MG  A . 
F 5 HOH 1   501 296 HOH HOH A . 
F 5 HOH 2   502 83  HOH HOH A . 
F 5 HOH 3   503 88  HOH HOH A . 
F 5 HOH 4   504 198 HOH HOH A . 
F 5 HOH 5   505 190 HOH HOH A . 
F 5 HOH 6   506 228 HOH HOH A . 
F 5 HOH 7   507 161 HOH HOH A . 
F 5 HOH 8   508 108 HOH HOH A . 
F 5 HOH 9   509 110 HOH HOH A . 
F 5 HOH 10  510 102 HOH HOH A . 
F 5 HOH 11  511 196 HOH HOH A . 
F 5 HOH 12  512 65  HOH HOH A . 
F 5 HOH 13  513 243 HOH HOH A . 
F 5 HOH 14  514 214 HOH HOH A . 
F 5 HOH 15  515 74  HOH HOH A . 
F 5 HOH 16  516 169 HOH HOH A . 
F 5 HOH 17  517 54  HOH HOH A . 
F 5 HOH 18  518 124 HOH HOH A . 
F 5 HOH 19  519 30  HOH HOH A . 
F 5 HOH 20  520 135 HOH HOH A . 
F 5 HOH 21  521 153 HOH HOH A . 
F 5 HOH 22  522 8   HOH HOH A . 
F 5 HOH 23  523 266 HOH HOH A . 
F 5 HOH 24  524 131 HOH HOH A . 
F 5 HOH 25  525 61  HOH HOH A . 
F 5 HOH 26  526 253 HOH HOH A . 
F 5 HOH 27  527 70  HOH HOH A . 
F 5 HOH 28  528 92  HOH HOH A . 
F 5 HOH 29  529 205 HOH HOH A . 
F 5 HOH 30  530 220 HOH HOH A . 
F 5 HOH 31  531 265 HOH HOH A . 
F 5 HOH 32  532 204 HOH HOH A . 
F 5 HOH 33  533 186 HOH HOH A . 
F 5 HOH 34  534 264 HOH HOH A . 
F 5 HOH 35  535 294 HOH HOH A . 
F 5 HOH 36  536 138 HOH HOH A . 
F 5 HOH 37  537 112 HOH HOH A . 
F 5 HOH 38  538 49  HOH HOH A . 
F 5 HOH 39  539 87  HOH HOH A . 
F 5 HOH 40  540 244 HOH HOH A . 
F 5 HOH 41  541 53  HOH HOH A . 
F 5 HOH 42  542 123 HOH HOH A . 
F 5 HOH 43  543 212 HOH HOH A . 
F 5 HOH 44  544 71  HOH HOH A . 
F 5 HOH 45  545 117 HOH HOH A . 
F 5 HOH 46  546 155 HOH HOH A . 
F 5 HOH 47  547 248 HOH HOH A . 
F 5 HOH 48  548 25  HOH HOH A . 
F 5 HOH 49  549 35  HOH HOH A . 
F 5 HOH 50  550 38  HOH HOH A . 
F 5 HOH 51  551 99  HOH HOH A . 
F 5 HOH 52  552 182 HOH HOH A . 
F 5 HOH 53  553 270 HOH HOH A . 
F 5 HOH 54  554 19  HOH HOH A . 
F 5 HOH 55  555 89  HOH HOH A . 
F 5 HOH 56  556 43  HOH HOH A . 
F 5 HOH 57  557 85  HOH HOH A . 
F 5 HOH 58  558 36  HOH HOH A . 
F 5 HOH 59  559 10  HOH HOH A . 
F 5 HOH 60  560 167 HOH HOH A . 
F 5 HOH 61  561 164 HOH HOH A . 
F 5 HOH 62  562 103 HOH HOH A . 
F 5 HOH 63  563 12  HOH HOH A . 
F 5 HOH 64  564 29  HOH HOH A . 
F 5 HOH 65  565 129 HOH HOH A . 
F 5 HOH 66  566 133 HOH HOH A . 
F 5 HOH 67  567 20  HOH HOH A . 
F 5 HOH 68  568 62  HOH HOH A . 
F 5 HOH 69  569 11  HOH HOH A . 
F 5 HOH 70  570 57  HOH HOH A . 
F 5 HOH 71  571 157 HOH HOH A . 
F 5 HOH 72  572 2   HOH HOH A . 
F 5 HOH 73  573 107 HOH HOH A . 
F 5 HOH 74  574 18  HOH HOH A . 
F 5 HOH 75  575 24  HOH HOH A . 
F 5 HOH 76  576 193 HOH HOH A . 
F 5 HOH 77  577 173 HOH HOH A . 
F 5 HOH 78  578 47  HOH HOH A . 
F 5 HOH 79  579 146 HOH HOH A . 
F 5 HOH 80  580 34  HOH HOH A . 
F 5 HOH 81  581 116 HOH HOH A . 
F 5 HOH 82  582 31  HOH HOH A . 
F 5 HOH 83  583 206 HOH HOH A . 
F 5 HOH 84  584 172 HOH HOH A . 
F 5 HOH 85  585 144 HOH HOH A . 
F 5 HOH 86  586 80  HOH HOH A . 
F 5 HOH 87  587 125 HOH HOH A . 
F 5 HOH 88  588 14  HOH HOH A . 
F 5 HOH 89  589 275 HOH HOH A . 
F 5 HOH 90  590 5   HOH HOH A . 
F 5 HOH 91  591 63  HOH HOH A . 
F 5 HOH 92  592 137 HOH HOH A . 
F 5 HOH 93  593 40  HOH HOH A . 
F 5 HOH 94  594 42  HOH HOH A . 
F 5 HOH 95  595 151 HOH HOH A . 
F 5 HOH 96  596 219 HOH HOH A . 
F 5 HOH 97  597 97  HOH HOH A . 
F 5 HOH 98  598 52  HOH HOH A . 
F 5 HOH 99  599 7   HOH HOH A . 
F 5 HOH 100 600 51  HOH HOH A . 
F 5 HOH 101 601 39  HOH HOH A . 
F 5 HOH 102 602 140 HOH HOH A . 
F 5 HOH 103 603 45  HOH HOH A . 
F 5 HOH 104 604 109 HOH HOH A . 
F 5 HOH 105 605 285 HOH HOH A . 
F 5 HOH 106 606 150 HOH HOH A . 
F 5 HOH 107 607 195 HOH HOH A . 
F 5 HOH 108 608 293 HOH HOH A . 
F 5 HOH 109 609 171 HOH HOH A . 
F 5 HOH 110 610 79  HOH HOH A . 
F 5 HOH 111 611 197 HOH HOH A . 
F 5 HOH 112 612 72  HOH HOH A . 
F 5 HOH 113 613 1   HOH HOH A . 
F 5 HOH 114 614 28  HOH HOH A . 
F 5 HOH 115 615 231 HOH HOH A . 
F 5 HOH 116 616 114 HOH HOH A . 
F 5 HOH 117 617 90  HOH HOH A . 
F 5 HOH 118 618 158 HOH HOH A . 
F 5 HOH 119 619 6   HOH HOH A . 
F 5 HOH 120 620 17  HOH HOH A . 
F 5 HOH 121 621 163 HOH HOH A . 
F 5 HOH 122 622 27  HOH HOH A . 
F 5 HOH 123 623 194 HOH HOH A . 
F 5 HOH 124 624 16  HOH HOH A . 
F 5 HOH 125 625 148 HOH HOH A . 
F 5 HOH 126 626 60  HOH HOH A . 
F 5 HOH 127 627 168 HOH HOH A . 
F 5 HOH 128 628 224 HOH HOH A . 
F 5 HOH 129 629 13  HOH HOH A . 
F 5 HOH 130 630 75  HOH HOH A . 
F 5 HOH 131 631 184 HOH HOH A . 
F 5 HOH 132 632 50  HOH HOH A . 
F 5 HOH 133 633 67  HOH HOH A . 
F 5 HOH 134 634 77  HOH HOH A . 
F 5 HOH 135 635 217 HOH HOH A . 
F 5 HOH 136 636 55  HOH HOH A . 
F 5 HOH 137 637 126 HOH HOH A . 
F 5 HOH 138 638 152 HOH HOH A . 
F 5 HOH 139 639 241 HOH HOH A . 
F 5 HOH 140 640 81  HOH HOH A . 
F 5 HOH 141 641 78  HOH HOH A . 
F 5 HOH 142 642 162 HOH HOH A . 
F 5 HOH 143 643 9   HOH HOH A . 
F 5 HOH 144 644 3   HOH HOH A . 
F 5 HOH 145 645 59  HOH HOH A . 
F 5 HOH 146 646 95  HOH HOH A . 
F 5 HOH 147 647 254 HOH HOH A . 
F 5 HOH 148 648 76  HOH HOH A . 
F 5 HOH 149 649 15  HOH HOH A . 
F 5 HOH 150 650 178 HOH HOH A . 
F 5 HOH 151 651 4   HOH HOH A . 
F 5 HOH 152 652 96  HOH HOH A . 
F 5 HOH 153 653 48  HOH HOH A . 
F 5 HOH 154 654 46  HOH HOH A . 
F 5 HOH 155 655 37  HOH HOH A . 
F 5 HOH 156 656 41  HOH HOH A . 
F 5 HOH 157 657 221 HOH HOH A . 
F 5 HOH 158 658 120 HOH HOH A . 
F 5 HOH 159 659 261 HOH HOH A . 
F 5 HOH 160 660 249 HOH HOH A . 
F 5 HOH 161 661 93  HOH HOH A . 
F 5 HOH 162 662 154 HOH HOH A . 
F 5 HOH 163 663 141 HOH HOH A . 
F 5 HOH 164 664 200 HOH HOH A . 
F 5 HOH 165 665 113 HOH HOH A . 
F 5 HOH 166 666 160 HOH HOH A . 
F 5 HOH 167 667 272 HOH HOH A . 
F 5 HOH 168 668 276 HOH HOH A . 
F 5 HOH 169 669 165 HOH HOH A . 
F 5 HOH 170 670 132 HOH HOH A . 
F 5 HOH 171 671 149 HOH HOH A . 
F 5 HOH 172 672 91  HOH HOH A . 
F 5 HOH 173 673 295 HOH HOH A . 
F 5 HOH 174 674 139 HOH HOH A . 
F 5 HOH 175 675 58  HOH HOH A . 
F 5 HOH 176 676 189 HOH HOH A . 
F 5 HOH 177 677 159 HOH HOH A . 
F 5 HOH 178 678 69  HOH HOH A . 
F 5 HOH 179 679 286 HOH HOH A . 
F 5 HOH 180 680 145 HOH HOH A . 
F 5 HOH 181 681 202 HOH HOH A . 
F 5 HOH 182 682 268 HOH HOH A . 
F 5 HOH 183 683 170 HOH HOH A . 
F 5 HOH 184 684 73  HOH HOH A . 
F 5 HOH 185 685 32  HOH HOH A . 
F 5 HOH 186 686 104 HOH HOH A . 
F 5 HOH 187 687 118 HOH HOH A . 
F 5 HOH 188 688 111 HOH HOH A . 
F 5 HOH 189 689 181 HOH HOH A . 
F 5 HOH 190 690 203 HOH HOH A . 
F 5 HOH 191 691 44  HOH HOH A . 
F 5 HOH 192 692 226 HOH HOH A . 
F 5 HOH 193 693 175 HOH HOH A . 
F 5 HOH 194 694 100 HOH HOH A . 
F 5 HOH 195 695 236 HOH HOH A . 
F 5 HOH 196 696 180 HOH HOH A . 
F 5 HOH 197 697 66  HOH HOH A . 
F 5 HOH 198 698 210 HOH HOH A . 
F 5 HOH 199 699 119 HOH HOH A . 
F 5 HOH 200 700 56  HOH HOH A . 
F 5 HOH 201 701 86  HOH HOH A . 
F 5 HOH 202 702 106 HOH HOH A . 
F 5 HOH 203 703 22  HOH HOH A . 
F 5 HOH 204 704 250 HOH HOH A . 
F 5 HOH 205 705 94  HOH HOH A . 
F 5 HOH 206 706 105 HOH HOH A . 
F 5 HOH 207 707 273 HOH HOH A . 
F 5 HOH 208 708 98  HOH HOH A . 
F 5 HOH 209 709 218 HOH HOH A . 
F 5 HOH 210 710 289 HOH HOH A . 
F 5 HOH 211 711 26  HOH HOH A . 
F 5 HOH 212 712 240 HOH HOH A . 
F 5 HOH 213 713 23  HOH HOH A . 
F 5 HOH 214 714 136 HOH HOH A . 
F 5 HOH 215 715 82  HOH HOH A . 
F 5 HOH 216 716 229 HOH HOH A . 
F 5 HOH 217 717 281 HOH HOH A . 
F 5 HOH 218 718 277 HOH HOH A . 
F 5 HOH 219 719 192 HOH HOH A . 
F 5 HOH 220 720 269 HOH HOH A . 
F 5 HOH 221 721 127 HOH HOH A . 
F 5 HOH 222 722 21  HOH HOH A . 
F 5 HOH 223 723 222 HOH HOH A . 
F 5 HOH 224 724 64  HOH HOH A . 
F 5 HOH 225 725 215 HOH HOH A . 
F 5 HOH 226 726 179 HOH HOH A . 
F 5 HOH 227 727 256 HOH HOH A . 
F 5 HOH 228 728 122 HOH HOH A . 
F 5 HOH 229 729 142 HOH HOH A . 
F 5 HOH 230 730 199 HOH HOH A . 
F 5 HOH 231 731 166 HOH HOH A . 
F 5 HOH 232 732 260 HOH HOH A . 
F 5 HOH 233 733 33  HOH HOH A . 
F 5 HOH 234 734 188 HOH HOH A . 
F 5 HOH 235 735 283 HOH HOH A . 
F 5 HOH 236 736 255 HOH HOH A . 
F 5 HOH 237 737 143 HOH HOH A . 
F 5 HOH 238 738 252 HOH HOH A . 
F 5 HOH 239 739 251 HOH HOH A . 
F 5 HOH 240 740 267 HOH HOH A . 
F 5 HOH 241 741 237 HOH HOH A . 
F 5 HOH 242 742 176 HOH HOH A . 
F 5 HOH 243 743 271 HOH HOH A . 
F 5 HOH 244 744 225 HOH HOH A . 
F 5 HOH 245 745 263 HOH HOH A . 
F 5 HOH 246 746 223 HOH HOH A . 
F 5 HOH 247 747 287 HOH HOH A . 
F 5 HOH 248 748 234 HOH HOH A . 
F 5 HOH 249 749 101 HOH HOH A . 
F 5 HOH 250 750 128 HOH HOH A . 
F 5 HOH 251 751 208 HOH HOH A . 
F 5 HOH 252 752 68  HOH HOH A . 
F 5 HOH 253 753 247 HOH HOH A . 
F 5 HOH 254 754 246 HOH HOH A . 
F 5 HOH 255 755 292 HOH HOH A . 
F 5 HOH 256 756 257 HOH HOH A . 
F 5 HOH 257 757 258 HOH HOH A . 
F 5 HOH 258 758 174 HOH HOH A . 
F 5 HOH 259 759 191 HOH HOH A . 
F 5 HOH 260 760 121 HOH HOH A . 
F 5 HOH 261 761 278 HOH HOH A . 
F 5 HOH 262 762 288 HOH HOH A . 
F 5 HOH 263 763 185 HOH HOH A . 
F 5 HOH 264 764 274 HOH HOH A . 
F 5 HOH 265 765 238 HOH HOH A . 
F 5 HOH 266 766 209 HOH HOH A . 
F 5 HOH 267 767 242 HOH HOH A . 
F 5 HOH 268 768 213 HOH HOH A . 
F 5 HOH 269 769 187 HOH HOH A . 
F 5 HOH 270 770 177 HOH HOH A . 
F 5 HOH 271 771 134 HOH HOH A . 
F 5 HOH 272 772 230 HOH HOH A . 
F 5 HOH 273 773 130 HOH HOH A . 
F 5 HOH 274 774 291 HOH HOH A . 
F 5 HOH 275 775 262 HOH HOH A . 
F 5 HOH 276 776 284 HOH HOH A . 
F 5 HOH 277 777 84  HOH HOH A . 
F 5 HOH 278 778 290 HOH HOH A . 
F 5 HOH 279 779 147 HOH HOH A . 
F 5 HOH 280 780 207 HOH HOH A . 
F 5 HOH 281 781 201 HOH HOH A . 
F 5 HOH 282 782 156 HOH HOH A . 
F 5 HOH 283 783 282 HOH HOH A . 
F 5 HOH 284 784 245 HOH HOH A . 
F 5 HOH 285 785 227 HOH HOH A . 
F 5 HOH 286 786 280 HOH HOH A . 
F 5 HOH 287 787 259 HOH HOH A . 
F 5 HOH 288 788 279 HOH HOH A . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     SER 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      152 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     OG 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    A 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    SER 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     153 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    OG 
# 
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   ? ? ? 1.17.1-3660 1 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? Blu-Ice  ? ? ? .           2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
# 
_cell.angle_alpha                  74.95 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   73.03 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  84.42 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YSL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     35.269 
_cell.length_a_esd                 ? 
_cell.length_b                     46.118 
_cell.length_b_esd                 ? 
_cell.length_c                     60.466 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        1 
_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                         8YSL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 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                   8YSL 
_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             2.31 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.71 
_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    
;0.1 M Potassium thiocyanate, 
30% w/v Polyethylene glycol monomethyl ether 2,000.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-03-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00000 
_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                        'NSRRC BEAMLINE TPS 05A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'TPS 05A' 
_diffrn_source.pdbx_synchrotron_site       NSRRC 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YSL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.98 
_reflns.d_resolution_low                               30.0 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     23777 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           97.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.293 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.042 
_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                                    1.98 
_reflns_shell.d_res_low                                     2.05 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2356 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.946 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8YSL 
_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                            1.98 
_refine.ls_d_res_low                             26.59 
_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                     23574 
_refine.ls_number_reflns_R_free                  1242 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.71 
_refine.ls_percent_reflns_R_free                 8.48 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1655 
_refine.ls_R_factor_R_free                       0.2003 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1622 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               NONE 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2654 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         62 
_refine_hist.number_atoms_solvent             288 
_refine_hist.number_atoms_total               3004 
_refine_hist.d_res_high                       1.98 
_refine_hist.d_res_low                        26.59 
# 
_struct.entry_id                     8YSL 
_struct.title                        
'Crystal structure of the Deinococcus wulumuqiensis CD-NTase DwCdnB in complex with UTP and ATP' 
_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        8YSL 
_struct_keywords.text            'CD-NTase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A345ILN6_9DEIO 
_struct_ref.pdbx_db_accession          A0A345ILN6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAPVQKQFREFHDRIKLAQYDENQTLRDERDAVLTAVREGLKKVFADRGEAAPTFTPFNQGSYAMNTGVKPLEGGEYDID
VGIILNIAKDDHDPVEVKKWIRDALKDYGNGAEIRRSCVTVFKPGYHVDLAVYADPELSGGTLCIAKGKENSGDEHRLWQ
ISDPQGFQDRIASKLSGDDAAQFRRCIRYLKRWRDFRFSSDGNAAPLGIGLTAAAYWWFQVSKRTDPVSQNVTYDDRDAL
EQFVQTMLDNFHDTWDSKDQRSYPRLTVELPVQPYNDVFEKMTGMQMESFKSKLQALLNALKTAKSRLELHDACKALADH
FGSEFPVPEKDKSAVHTAPAIVGSGSSG
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YSL 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 349 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A345ILN6 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  348 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       348 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             8YSL 
_struct_ref_seq_dif.mon_id                       MET 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      1 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   A0A345ILN6 
_struct_ref_seq_dif.db_mon_id                    ? 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          ? 
_struct_ref_seq_dif.details                      'initiating methionine' 
_struct_ref_seq_dif.pdbx_auth_seq_num            0 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_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)' 1920  ? 
1 MORE         -28   ? 
1 'SSA (A^2)'  15730 ? 
# 
_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 
# 
_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 VAL A 5   ? LYS A 17  ? VAL A 4   LYS A 16  1 ? 13 
HELX_P HELX_P2  AA2 GLN A 20  ? GLU A 23  ? GLN A 19  GLU A 22  5 ? 4  
HELX_P HELX_P3  AA3 ASN A 24  ? ASP A 48  ? ASN A 23  ASP A 47  1 ? 25 
HELX_P HELX_P4  AA4 GLN A 61  ? ASN A 67  ? GLN A 60  ASN A 66  1 ? 7  
HELX_P HELX_P5  AA5 ALA A 89  ? HIS A 93  ? ALA A 88  HIS A 92  5 ? 5  
HELX_P HELX_P6  AA6 ASP A 94  ? LEU A 106 ? ASP A 93  LEU A 105 1 ? 13 
HELX_P HELX_P7  AA7 PRO A 137 ? SER A 140 ? PRO A 136 SER A 139 5 ? 4  
HELX_P HELX_P8  AA8 ASP A 164 ? LYS A 175 ? ASP A 163 LYS A 174 1 ? 12 
HELX_P HELX_P9  AA9 SER A 177 ? PHE A 199 ? SER A 176 PHE A 198 1 ? 23 
HELX_P HELX_P10 AB1 ASP A 202 ? ALA A 206 ? ASP A 201 ALA A 205 5 ? 5  
HELX_P HELX_P11 AB2 LEU A 208 ? PHE A 220 ? LEU A 207 PHE A 219 1 ? 13 
HELX_P HELX_P12 AB3 ASP A 236 ? ASN A 251 ? ASP A 235 ASN A 250 1 ? 16 
HELX_P HELX_P13 AB4 THR A 284 ? ARG A 308 ? THR A 283 ARG A 307 1 ? 25 
HELX_P HELX_P14 AB5 GLU A 310 ? GLY A 323 ? GLU A 309 GLY A 322 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 79  OD2   ? ? ? 1_555 D MG  . MG ? ? A ASP 78  A MG  403 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc2  metalc ? ? A ASP 79  OD1   ? ? ? 1_555 E MG  . MG ? ? A ASP 78  A MG  404 1_555 ? ? ? ? ? ? ? 2.670 ? ? 
metalc3  metalc ? ? A ASP 79  OD2   ? ? ? 1_555 E MG  . MG ? ? A ASP 78  A MG  404 1_555 ? ? ? ? ? ? ? 2.561 ? ? 
metalc4  metalc ? ? A ASP 81  OD2   ? ? ? 1_555 D MG  . MG ? ? A ASP 80  A MG  403 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc5  metalc ? ? A ASP 81  OD1   ? ? ? 1_555 E MG  . MG ? ? A ASP 80  A MG  404 1_555 ? ? ? ? ? ? ? 2.319 ? ? 
metalc6  metalc ? ? A ASP 130 OD2   ? ? ? 1_555 E MG  . MG ? ? A ASP 129 A MG  404 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
metalc7  metalc ? ? B ATP .   O2G   ? ? ? 1_555 D MG  . MG ? ? A ATP 401 A MG  403 1_555 ? ? ? ? ? ? ? 1.940 ? ? 
metalc8  metalc ? ? B ATP .   O2B   ? ? ? 1_555 D MG  . MG ? ? A ATP 401 A MG  403 1_555 ? ? ? ? ? ? ? 1.946 ? ? 
metalc9  metalc ? ? B ATP .   O2A   ? ? ? 1_555 D MG  . MG ? ? A ATP 401 A MG  403 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc10 metalc ? ? B ATP .   O2A   ? ? ? 1_555 E MG  . MG ? ? A ATP 401 A MG  404 1_555 ? ? ? ? ? ? ? 2.724 ? ? 
metalc11 metalc ? ? C UTP .   "O2'" B ? ? 1_555 E MG  . MG ? ? A UTP 402 A MG  404 1_555 ? ? ? ? ? ? ? 2.978 ? ? 
metalc12 metalc ? ? C UTP .   "O3'" A ? ? 1_555 E MG  . MG ? ? A UTP 402 A MG  404 1_555 ? ? ? ? ? ? ? 2.457 ? ? 
metalc13 metalc ? ? C UTP .   "O3'" B ? ? 1_555 E MG  . MG ? ? A UTP 402 A MG  404 1_555 ? ? ? ? ? ? ? 2.489 ? ? 
metalc14 metalc ? ? D MG  .   MG    ? ? ? 1_555 F HOH . O  ? ? A MG  403 A HOH 579 1_555 ? ? ? ? ? ? ? 2.071 ? ? 
metalc15 metalc ? ? E MG  .   MG    ? ? ? 1_555 F HOH . O  ? ? A MG  404 A HOH 662 1_555 ? ? ? ? ? ? ? 2.550 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD2   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 OD2   ? A ASP 81  ? A ASP 80  ? 1_555 89.8  ? 
2  OD2   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O2G   ? B ATP .   ? A ATP 401 ? 1_555 97.7  ? 
3  OD2   ? A ASP 81  ? A ASP 80  ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O2G   ? B ATP .   ? A ATP 401 ? 1_555 172.3 ? 
4  OD2   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O2B   ? B ATP .   ? A ATP 401 ? 1_555 171.2 ? 
5  OD2   ? A ASP 81  ? A ASP 80  ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O2B   ? B ATP .   ? A ATP 401 ? 1_555 86.5  ? 
6  O2G   ? B ATP .   ? A ATP 401 ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O2B   ? B ATP .   ? A ATP 401 ? 1_555 85.9  ? 
7  OD2   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O2A   ? B ATP .   ? A ATP 401 ? 1_555 85.9  ? 
8  OD2   ? A ASP 81  ? A ASP 80  ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O2A   ? B ATP .   ? A ATP 401 ? 1_555 87.1  ? 
9  O2G   ? B ATP .   ? A ATP 401 ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O2A   ? B ATP .   ? A ATP 401 ? 1_555 91.6  ? 
10 O2B   ? B ATP .   ? A ATP 401 ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O2A   ? B ATP .   ? A ATP 401 ? 1_555 85.9  ? 
11 OD2   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O     ? F HOH .   ? A HOH 579 ? 1_555 95.3  ? 
12 OD2   ? A ASP 81  ? A ASP 80  ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O     ? F HOH .   ? A HOH 579 ? 1_555 82.8  ? 
13 O2G   ? B ATP .   ? A ATP 401 ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O     ? F HOH .   ? A HOH 579 ? 1_555 98.3  ? 
14 O2B   ? B ATP .   ? A ATP 401 ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O     ? F HOH .   ? A HOH 579 ? 1_555 92.2  ? 
15 O2A   ? B ATP .   ? A ATP 401 ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O     ? F HOH .   ? A HOH 579 ? 1_555 169.8 ? 
16 OD1   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 OD2   ? A ASP 79  ? A ASP 78  ? 1_555 49.7  ? 
17 OD1   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 OD1   ? A ASP 81  ? A ASP 80  ? 1_555 96.5  ? 
18 OD2   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 OD1   ? A ASP 81  ? A ASP 80  ? 1_555 74.0  ? 
19 OD1   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 OD2   ? A ASP 130 ? A ASP 129 ? 1_555 70.4  ? 
20 OD2   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 OD2   ? A ASP 130 ? A ASP 129 ? 1_555 117.2 ? 
21 OD1   ? A ASP 81  ? A ASP 80  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 OD2   ? A ASP 130 ? A ASP 129 ? 1_555 98.9  ? 
22 OD1   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O2A   ? B ATP .   ? A ATP 401 ? 1_555 110.5 ? 
23 OD2   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O2A   ? B ATP .   ? A ATP 401 ? 1_555 63.8  ? 
24 OD1   ? A ASP 81  ? A ASP 80  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O2A   ? B ATP .   ? A ATP 401 ? 1_555 81.7  ? 
25 OD2   ? A ASP 130 ? A ASP 129 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O2A   ? B ATP .   ? A ATP 401 ? 1_555 179.0 ? 
26 OD1   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O2'" B C UTP .   ? A UTP 402 ? 1_555 153.2 ? 
27 OD2   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O2'" B C UTP .   ? A UTP 402 ? 1_555 137.8 ? 
28 OD1   ? A ASP 81  ? A ASP 80  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O2'" B C UTP .   ? A UTP 402 ? 1_555 69.4  ? 
29 OD2   ? A ASP 130 ? A ASP 129 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O2'" B C UTP .   ? A UTP 402 ? 1_555 88.9  ? 
30 O2A   ? B ATP .   ? A ATP 401 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O2'" B C UTP .   ? A UTP 402 ? 1_555 90.5  ? 
31 OD1   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" A C UTP .   ? A UTP 402 ? 1_555 136.1 ? 
32 OD2   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" A C UTP .   ? A UTP 402 ? 1_555 144.6 ? 
33 OD1   ? A ASP 81  ? A ASP 80  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" A C UTP .   ? A UTP 402 ? 1_555 126.0 ? 
34 OD2   ? A ASP 130 ? A ASP 129 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" A C UTP .   ? A UTP 402 ? 1_555 90.5  ? 
35 O2A   ? B ATP .   ? A ATP 401 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" A C UTP .   ? A UTP 402 ? 1_555 88.5  ? 
36 "O2'" B C UTP .   ? A UTP 402 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" A C UTP .   ? A UTP 402 ? 1_555 57.7  ? 
37 OD1   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" B C UTP .   ? A UTP 402 ? 1_555 137.4 ? 
38 OD2   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" B C UTP .   ? A UTP 402 ? 1_555 141.9 ? 
39 OD1   ? A ASP 81  ? A ASP 80  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" B C UTP .   ? A UTP 402 ? 1_555 125.4 ? 
40 OD2   ? A ASP 130 ? A ASP 129 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" B C UTP .   ? A UTP 402 ? 1_555 93.6  ? 
41 O2A   ? B ATP .   ? A ATP 401 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" B C UTP .   ? A UTP 402 ? 1_555 85.3  ? 
42 "O2'" B C UTP .   ? A UTP 402 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" B C UTP .   ? A UTP 402 ? 1_555 57.9  ? 
43 "O3'" A C UTP .   ? A UTP 402 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 "O3'" B C UTP .   ? A UTP 402 ? 1_555 3.2   ? 
44 OD1   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O     ? F HOH .   ? A HOH 662 ? 1_555 67.6  ? 
45 OD2   ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O     ? F HOH .   ? A HOH 662 ? 1_555 77.1  ? 
46 OD1   ? A ASP 81  ? A ASP 80  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O     ? F HOH .   ? A HOH 662 ? 1_555 150.7 ? 
47 OD2   ? A ASP 130 ? A ASP 129 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O     ? F HOH .   ? A HOH 662 ? 1_555 98.4  ? 
48 O2A   ? B ATP .   ? A ATP 401 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O     ? F HOH .   ? A HOH 662 ? 1_555 81.5  ? 
49 "O2'" B C UTP .   ? A UTP 402 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O     ? F HOH .   ? A HOH 662 ? 1_555 134.4 ? 
50 "O3'" A C UTP .   ? A UTP 402 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O     ? F HOH .   ? A HOH 662 ? 1_555 77.3  ? 
51 "O3'" B C UTP .   ? A UTP 402 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O     ? F HOH .   ? A HOH 662 ? 1_555 76.7  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLN 
_struct_mon_prot_cis.label_seq_id           274 
_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           GLN 
_struct_mon_prot_cis.auth_seq_id            273 
_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    275 
_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     274 
_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       3.60 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 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 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 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 PHE A 56  ? ASN A 60  ? PHE A 55  ASN A 59  
AA1 2 TYR A 78  ? LEU A 86  ? TYR A 77  LEU A 85  
AA1 3 TYR A 127 ? ALA A 135 ? TYR A 126 ALA A 134 
AA1 4 CYS A 119 ? LYS A 124 ? CYS A 118 LYS A 123 
AA1 5 GLY A 112 ? ARG A 116 ? GLY A 111 ARG A 115 
AA2 1 CYS A 145 ? LYS A 148 ? CYS A 144 LYS A 147 
AA2 2 LEU A 159 ? ILE A 162 ? LEU A 158 ILE A 161 
AA3 1 LYS A 224 ? THR A 226 ? LYS A 223 THR A 225 
AA3 2 VAL A 233 ? TYR A 235 ? VAL A 232 TYR A 234 
AA4 1 PHE A 252 ? ASP A 257 ? PHE A 251 ASP A 256 
AA4 2 ARG A 262 ? LEU A 267 ? ARG A 261 LEU A 266 
# 
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 PHE A 59  ? N PHE A 58  O GLY A 83  ? O GLY A 82  
AA1 2 3 N LEU A 86  ? N LEU A 85  O TYR A 134 ? O TYR A 133 
AA1 3 4 O LEU A 131 ? O LEU A 130 N VAL A 120 ? N VAL A 119 
AA1 4 5 O CYS A 119 ? O CYS A 118 N ARG A 116 ? N ARG A 115 
AA2 1 2 N LYS A 148 ? N LYS A 147 O LEU A 159 ? O LEU A 158 
AA3 1 2 N ARG A 225 ? N ARG A 224 O THR A 234 ? O THR A 233 
AA4 1 2 N ASP A 257 ? N ASP A 256 O ARG A 262 ? O ARG A 261 
# 
_pdbx_entry_details.entry_id                   8YSL 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 682 ? ? O A HOH 722 ? ? 1.98 
2 1 O A HOH 718 ? ? O A HOH 761 ? ? 2.07 
3 1 O A HOH 717 ? ? O A HOH 783 ? ? 2.09 
4 1 O A HOH 553 ? ? O A HOH 720 ? ? 2.09 
5 1 O A HOH 720 ? ? O A HOH 743 ? ? 2.10 
6 1 N A VAL 4   ? ? O A HOH 501 ? ? 2.17 
7 1 O A HOH 545 ? ? O A HOH 743 ? ? 2.17 
8 1 O A HOH 609 ? ? O A HOH 669 ? ? 2.17 
9 1 O A HOH 505 ? ? O A HOH 763 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     513 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     767 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_655 
_pdbx_validate_symm_contact.dist              2.19 
# 
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 PRO A 124 ? ? -52.71  107.38 
2 1 ASP A 154 ? ? -137.28 -37.77 
3 1 ASP A 201 ? ? -150.28 88.55  
4 1 GLN A 230 ? ? 58.29   16.74  
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       788 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.71 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ASP 331 ? A ASP 332 
2  1 Y 1 A LYS 332 ? A LYS 333 
3  1 Y 1 A SER 333 ? A SER 334 
4  1 Y 1 A ALA 334 ? A ALA 335 
5  1 Y 1 A VAL 335 ? A VAL 336 
6  1 Y 1 A HIS 336 ? A HIS 337 
7  1 Y 1 A THR 337 ? A THR 338 
8  1 Y 1 A ALA 338 ? A ALA 339 
9  1 Y 1 A PRO 339 ? A PRO 340 
10 1 Y 1 A ALA 340 ? A ALA 341 
11 1 Y 1 A ILE 341 ? A ILE 342 
12 1 Y 1 A VAL 342 ? A VAL 343 
13 1 Y 1 A GLY 343 ? A GLY 344 
14 1 Y 1 A SER 344 ? A SER 345 
15 1 Y 1 A GLY 345 ? A GLY 346 
16 1 Y 1 A SER 346 ? A SER 347 
17 1 Y 1 A SER 347 ? A SER 348 
18 1 Y 1 A GLY 348 ? A GLY 349 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
ATP PG     P  N N 74  
ATP O1G    O  N N 75  
ATP O2G    O  N N 76  
ATP O3G    O  N N 77  
ATP PB     P  N R 78  
ATP O1B    O  N N 79  
ATP O2B    O  N N 80  
ATP O3B    O  N N 81  
ATP PA     P  N R 82  
ATP O1A    O  N N 83  
ATP O2A    O  N N 84  
ATP O3A    O  N N 85  
ATP "O5'"  O  N N 86  
ATP "C5'"  C  N N 87  
ATP "C4'"  C  N R 88  
ATP "O4'"  O  N N 89  
ATP "C3'"  C  N S 90  
ATP "O3'"  O  N N 91  
ATP "C2'"  C  N R 92  
ATP "O2'"  O  N N 93  
ATP "C1'"  C  N R 94  
ATP N9     N  Y N 95  
ATP C8     C  Y N 96  
ATP N7     N  Y N 97  
ATP C5     C  Y N 98  
ATP C6     C  Y N 99  
ATP N6     N  N N 100 
ATP N1     N  Y N 101 
ATP C2     C  Y N 102 
ATP N3     N  Y N 103 
ATP C4     C  Y N 104 
ATP HOG2   H  N N 105 
ATP HOG3   H  N N 106 
ATP HOB2   H  N N 107 
ATP HOA2   H  N N 108 
ATP "H5'1" H  N N 109 
ATP "H5'2" H  N N 110 
ATP "H4'"  H  N N 111 
ATP "H3'"  H  N N 112 
ATP "HO3'" H  N N 113 
ATP "H2'"  H  N N 114 
ATP "HO2'" H  N N 115 
ATP "H1'"  H  N N 116 
ATP H8     H  N N 117 
ATP HN61   H  N N 118 
ATP HN62   H  N N 119 
ATP H2     H  N N 120 
CYS N      N  N N 121 
CYS CA     C  N R 122 
CYS C      C  N N 123 
CYS O      O  N N 124 
CYS CB     C  N N 125 
CYS SG     S  N N 126 
CYS OXT    O  N N 127 
CYS H      H  N N 128 
CYS H2     H  N N 129 
CYS HA     H  N N 130 
CYS HB2    H  N N 131 
CYS HB3    H  N N 132 
CYS HG     H  N N 133 
CYS HXT    H  N N 134 
GLN N      N  N N 135 
GLN CA     C  N S 136 
GLN C      C  N N 137 
GLN O      O  N N 138 
GLN CB     C  N N 139 
GLN CG     C  N N 140 
GLN CD     C  N N 141 
GLN OE1    O  N N 142 
GLN NE2    N  N N 143 
GLN OXT    O  N N 144 
GLN H      H  N N 145 
GLN H2     H  N N 146 
GLN HA     H  N N 147 
GLN HB2    H  N N 148 
GLN HB3    H  N N 149 
GLN HG2    H  N N 150 
GLN HG3    H  N N 151 
GLN HE21   H  N N 152 
GLN HE22   H  N N 153 
GLN HXT    H  N N 154 
GLU N      N  N N 155 
GLU CA     C  N S 156 
GLU C      C  N N 157 
GLU O      O  N N 158 
GLU CB     C  N N 159 
GLU CG     C  N N 160 
GLU CD     C  N N 161 
GLU OE1    O  N N 162 
GLU OE2    O  N N 163 
GLU OXT    O  N N 164 
GLU H      H  N N 165 
GLU H2     H  N N 166 
GLU HA     H  N N 167 
GLU HB2    H  N N 168 
GLU HB3    H  N N 169 
GLU HG2    H  N N 170 
GLU HG3    H  N N 171 
GLU HE2    H  N N 172 
GLU HXT    H  N N 173 
GLY N      N  N N 174 
GLY CA     C  N N 175 
GLY C      C  N N 176 
GLY O      O  N N 177 
GLY OXT    O  N N 178 
GLY H      H  N N 179 
GLY H2     H  N N 180 
GLY HA2    H  N N 181 
GLY HA3    H  N N 182 
GLY HXT    H  N N 183 
HIS N      N  N N 184 
HIS CA     C  N S 185 
HIS C      C  N N 186 
HIS O      O  N N 187 
HIS CB     C  N N 188 
HIS CG     C  Y N 189 
HIS ND1    N  Y N 190 
HIS CD2    C  Y N 191 
HIS CE1    C  Y N 192 
HIS NE2    N  Y N 193 
HIS OXT    O  N N 194 
HIS H      H  N N 195 
HIS H2     H  N N 196 
HIS HA     H  N N 197 
HIS HB2    H  N N 198 
HIS HB3    H  N N 199 
HIS HD1    H  N N 200 
HIS HD2    H  N N 201 
HIS HE1    H  N N 202 
HIS HE2    H  N N 203 
HIS HXT    H  N N 204 
HOH O      O  N N 205 
HOH H1     H  N N 206 
HOH H2     H  N N 207 
ILE N      N  N N 208 
ILE CA     C  N S 209 
ILE C      C  N N 210 
ILE O      O  N N 211 
ILE CB     C  N S 212 
ILE CG1    C  N N 213 
ILE CG2    C  N N 214 
ILE CD1    C  N N 215 
ILE OXT    O  N N 216 
ILE H      H  N N 217 
ILE H2     H  N N 218 
ILE HA     H  N N 219 
ILE HB     H  N N 220 
ILE HG12   H  N N 221 
ILE HG13   H  N N 222 
ILE HG21   H  N N 223 
ILE HG22   H  N N 224 
ILE HG23   H  N N 225 
ILE HD11   H  N N 226 
ILE HD12   H  N N 227 
ILE HD13   H  N N 228 
ILE HXT    H  N N 229 
LEU N      N  N N 230 
LEU CA     C  N S 231 
LEU C      C  N N 232 
LEU O      O  N N 233 
LEU CB     C  N N 234 
LEU CG     C  N N 235 
LEU CD1    C  N N 236 
LEU CD2    C  N N 237 
LEU OXT    O  N N 238 
LEU H      H  N N 239 
LEU H2     H  N N 240 
LEU HA     H  N N 241 
LEU HB2    H  N N 242 
LEU HB3    H  N N 243 
LEU HG     H  N N 244 
LEU HD11   H  N N 245 
LEU HD12   H  N N 246 
LEU HD13   H  N N 247 
LEU HD21   H  N N 248 
LEU HD22   H  N N 249 
LEU HD23   H  N N 250 
LEU HXT    H  N N 251 
LYS N      N  N N 252 
LYS CA     C  N S 253 
LYS C      C  N N 254 
LYS O      O  N N 255 
LYS CB     C  N N 256 
LYS CG     C  N N 257 
LYS CD     C  N N 258 
LYS CE     C  N N 259 
LYS NZ     N  N N 260 
LYS OXT    O  N N 261 
LYS H      H  N N 262 
LYS H2     H  N N 263 
LYS HA     H  N N 264 
LYS HB2    H  N N 265 
LYS HB3    H  N N 266 
LYS HG2    H  N N 267 
LYS HG3    H  N N 268 
LYS HD2    H  N N 269 
LYS HD3    H  N N 270 
LYS HE2    H  N N 271 
LYS HE3    H  N N 272 
LYS HZ1    H  N N 273 
LYS HZ2    H  N N 274 
LYS HZ3    H  N N 275 
LYS HXT    H  N N 276 
MET N      N  N N 277 
MET CA     C  N S 278 
MET C      C  N N 279 
MET O      O  N N 280 
MET CB     C  N N 281 
MET CG     C  N N 282 
MET SD     S  N N 283 
MET CE     C  N N 284 
MET OXT    O  N N 285 
MET H      H  N N 286 
MET H2     H  N N 287 
MET HA     H  N N 288 
MET HB2    H  N N 289 
MET HB3    H  N N 290 
MET HG2    H  N N 291 
MET HG3    H  N N 292 
MET HE1    H  N N 293 
MET HE2    H  N N 294 
MET HE3    H  N N 295 
MET HXT    H  N N 296 
MG  MG     MG 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 
THR N      N  N N 352 
THR CA     C  N S 353 
THR C      C  N N 354 
THR O      O  N N 355 
THR CB     C  N R 356 
THR OG1    O  N N 357 
THR CG2    C  N N 358 
THR OXT    O  N N 359 
THR H      H  N N 360 
THR H2     H  N N 361 
THR HA     H  N N 362 
THR HB     H  N N 363 
THR HG1    H  N N 364 
THR HG21   H  N N 365 
THR HG22   H  N N 366 
THR HG23   H  N N 367 
THR HXT    H  N N 368 
TRP N      N  N N 369 
TRP CA     C  N S 370 
TRP C      C  N N 371 
TRP O      O  N N 372 
TRP CB     C  N N 373 
TRP CG     C  Y N 374 
TRP CD1    C  Y N 375 
TRP CD2    C  Y N 376 
TRP NE1    N  Y N 377 
TRP CE2    C  Y N 378 
TRP CE3    C  Y N 379 
TRP CZ2    C  Y N 380 
TRP CZ3    C  Y N 381 
TRP CH2    C  Y N 382 
TRP OXT    O  N N 383 
TRP H      H  N N 384 
TRP H2     H  N N 385 
TRP HA     H  N N 386 
TRP HB2    H  N N 387 
TRP HB3    H  N N 388 
TRP HD1    H  N N 389 
TRP HE1    H  N N 390 
TRP HE3    H  N N 391 
TRP HZ2    H  N N 392 
TRP HZ3    H  N N 393 
TRP HH2    H  N N 394 
TRP HXT    H  N N 395 
TYR N      N  N N 396 
TYR CA     C  N S 397 
TYR C      C  N N 398 
TYR O      O  N N 399 
TYR CB     C  N N 400 
TYR CG     C  Y N 401 
TYR CD1    C  Y N 402 
TYR CD2    C  Y N 403 
TYR CE1    C  Y N 404 
TYR CE2    C  Y N 405 
TYR CZ     C  Y N 406 
TYR OH     O  N N 407 
TYR OXT    O  N N 408 
TYR H      H  N N 409 
TYR H2     H  N N 410 
TYR HA     H  N N 411 
TYR HB2    H  N N 412 
TYR HB3    H  N N 413 
TYR HD1    H  N N 414 
TYR HD2    H  N N 415 
TYR HE1    H  N N 416 
TYR HE2    H  N N 417 
TYR HH     H  N N 418 
TYR HXT    H  N N 419 
UTP PA     P  N R 420 
UTP O1A    O  N N 421 
UTP O2A    O  N N 422 
UTP O3A    O  N N 423 
UTP "O5'"  O  N N 424 
UTP PB     P  N S 425 
UTP O1B    O  N N 426 
UTP O2B    O  N N 427 
UTP O3B    O  N N 428 
UTP PG     P  N N 429 
UTP O1G    O  N N 430 
UTP O2G    O  N N 431 
UTP O3G    O  N N 432 
UTP "C5'"  C  N N 433 
UTP "C4'"  C  N R 434 
UTP "O4'"  O  N N 435 
UTP "C1'"  C  N R 436 
UTP "C2'"  C  N R 437 
UTP "O2'"  O  N N 438 
UTP "C3'"  C  N S 439 
UTP "O3'"  O  N N 440 
UTP N1     N  Y N 441 
UTP C6     C  Y N 442 
UTP C2     C  Y N 443 
UTP O2     O  N N 444 
UTP N3     N  Y N 445 
UTP C4     C  Y N 446 
UTP O4     O  N N 447 
UTP C5     C  Y N 448 
UTP H2A    H  N N 449 
UTP H1B    H  N N 450 
UTP H1G    H  N N 451 
UTP H3G    H  N N 452 
UTP "H5'1" H  N N 453 
UTP "H5'2" H  N N 454 
UTP "H4'"  H  N N 455 
UTP "H1'"  H  N N 456 
UTP "H2'"  H  N N 457 
UTP HA     H  N N 458 
UTP "H3'"  H  N N 459 
UTP HB     H  N N 460 
UTP H6     H  N N 461 
UTP H3     H  N N 462 
UTP H5     H  N N 463 
VAL N      N  N N 464 
VAL CA     C  N S 465 
VAL C      C  N N 466 
VAL O      O  N N 467 
VAL CB     C  N N 468 
VAL CG1    C  N N 469 
VAL CG2    C  N N 470 
VAL OXT    O  N N 471 
VAL H      H  N N 472 
VAL H2     H  N N 473 
VAL HA     H  N N 474 
VAL HB     H  N N 475 
VAL HG11   H  N N 476 
VAL HG12   H  N N 477 
VAL HG13   H  N N 478 
VAL HG21   H  N N 479 
VAL HG22   H  N N 480 
VAL HG23   H  N N 481 
VAL HXT    H  N N 482 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
ATP PG    O1G    doub N N 70  
ATP PG    O2G    sing N N 71  
ATP PG    O3G    sing N N 72  
ATP PG    O3B    sing N N 73  
ATP O2G   HOG2   sing N N 74  
ATP O3G   HOG3   sing N N 75  
ATP PB    O1B    doub N N 76  
ATP PB    O2B    sing N N 77  
ATP PB    O3B    sing N N 78  
ATP PB    O3A    sing N N 79  
ATP O2B   HOB2   sing N N 80  
ATP PA    O1A    doub N N 81  
ATP PA    O2A    sing N N 82  
ATP PA    O3A    sing N N 83  
ATP PA    "O5'"  sing N N 84  
ATP O2A   HOA2   sing N N 85  
ATP "O5'" "C5'"  sing N N 86  
ATP "C5'" "C4'"  sing N N 87  
ATP "C5'" "H5'1" sing N N 88  
ATP "C5'" "H5'2" sing N N 89  
ATP "C4'" "O4'"  sing N N 90  
ATP "C4'" "C3'"  sing N N 91  
ATP "C4'" "H4'"  sing N N 92  
ATP "O4'" "C1'"  sing N N 93  
ATP "C3'" "O3'"  sing N N 94  
ATP "C3'" "C2'"  sing N N 95  
ATP "C3'" "H3'"  sing N N 96  
ATP "O3'" "HO3'" sing N N 97  
ATP "C2'" "O2'"  sing N N 98  
ATP "C2'" "C1'"  sing N N 99  
ATP "C2'" "H2'"  sing N N 100 
ATP "O2'" "HO2'" sing N N 101 
ATP "C1'" N9     sing N N 102 
ATP "C1'" "H1'"  sing N N 103 
ATP N9    C8     sing Y N 104 
ATP N9    C4     sing Y N 105 
ATP C8    N7     doub Y N 106 
ATP C8    H8     sing N N 107 
ATP N7    C5     sing Y N 108 
ATP C5    C6     sing Y N 109 
ATP C5    C4     doub Y N 110 
ATP C6    N6     sing N N 111 
ATP C6    N1     doub Y N 112 
ATP N6    HN61   sing N N 113 
ATP N6    HN62   sing N N 114 
ATP N1    C2     sing Y N 115 
ATP C2    N3     doub Y N 116 
ATP C2    H2     sing N N 117 
ATP N3    C4     sing Y N 118 
CYS N     CA     sing N N 119 
CYS N     H      sing N N 120 
CYS N     H2     sing N N 121 
CYS CA    C      sing N N 122 
CYS CA    CB     sing N N 123 
CYS CA    HA     sing N N 124 
CYS C     O      doub N N 125 
CYS C     OXT    sing N N 126 
CYS CB    SG     sing N N 127 
CYS CB    HB2    sing N N 128 
CYS CB    HB3    sing N N 129 
CYS SG    HG     sing N N 130 
CYS OXT   HXT    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 
THR N     CA     sing N N 339 
THR N     H      sing N N 340 
THR N     H2     sing N N 341 
THR CA    C      sing N N 342 
THR CA    CB     sing N N 343 
THR CA    HA     sing N N 344 
THR C     O      doub N N 345 
THR C     OXT    sing N N 346 
THR CB    OG1    sing N N 347 
THR CB    CG2    sing N N 348 
THR CB    HB     sing N N 349 
THR OG1   HG1    sing N N 350 
THR CG2   HG21   sing N N 351 
THR CG2   HG22   sing N N 352 
THR CG2   HG23   sing N N 353 
THR OXT   HXT    sing N N 354 
TRP N     CA     sing N N 355 
TRP N     H      sing N N 356 
TRP N     H2     sing N N 357 
TRP CA    C      sing N N 358 
TRP CA    CB     sing N N 359 
TRP CA    HA     sing N N 360 
TRP C     O      doub N N 361 
TRP C     OXT    sing N N 362 
TRP CB    CG     sing N N 363 
TRP CB    HB2    sing N N 364 
TRP CB    HB3    sing N N 365 
TRP CG    CD1    doub Y N 366 
TRP CG    CD2    sing Y N 367 
TRP CD1   NE1    sing Y N 368 
TRP CD1   HD1    sing N N 369 
TRP CD2   CE2    doub Y N 370 
TRP CD2   CE3    sing Y N 371 
TRP NE1   CE2    sing Y N 372 
TRP NE1   HE1    sing N N 373 
TRP CE2   CZ2    sing Y N 374 
TRP CE3   CZ3    doub Y N 375 
TRP CE3   HE3    sing N N 376 
TRP CZ2   CH2    doub Y N 377 
TRP CZ2   HZ2    sing N N 378 
TRP CZ3   CH2    sing Y N 379 
TRP CZ3   HZ3    sing N N 380 
TRP CH2   HH2    sing N N 381 
TRP OXT   HXT    sing N N 382 
TYR N     CA     sing N N 383 
TYR N     H      sing N N 384 
TYR N     H2     sing N N 385 
TYR CA    C      sing N N 386 
TYR CA    CB     sing N N 387 
TYR CA    HA     sing N N 388 
TYR C     O      doub N N 389 
TYR C     OXT    sing N N 390 
TYR CB    CG     sing N N 391 
TYR CB    HB2    sing N N 392 
TYR CB    HB3    sing N N 393 
TYR CG    CD1    doub Y N 394 
TYR CG    CD2    sing Y N 395 
TYR CD1   CE1    sing Y N 396 
TYR CD1   HD1    sing N N 397 
TYR CD2   CE2    doub Y N 398 
TYR CD2   HD2    sing N N 399 
TYR CE1   CZ     doub Y N 400 
TYR CE1   HE1    sing N N 401 
TYR CE2   CZ     sing Y N 402 
TYR CE2   HE2    sing N N 403 
TYR CZ    OH     sing N N 404 
TYR OH    HH     sing N N 405 
TYR OXT   HXT    sing N N 406 
UTP PA    O1A    doub N N 407 
UTP PA    O2A    sing N N 408 
UTP PA    O3A    sing N N 409 
UTP PA    "O5'"  sing N N 410 
UTP O2A   H2A    sing N N 411 
UTP O3A   PB     sing N N 412 
UTP "O5'" "C5'"  sing N N 413 
UTP PB    O1B    sing N N 414 
UTP PB    O2B    doub N N 415 
UTP PB    O3B    sing N N 416 
UTP O1B   H1B    sing N N 417 
UTP O3B   PG     sing N N 418 
UTP PG    O1G    sing N N 419 
UTP PG    O2G    doub N N 420 
UTP PG    O3G    sing N N 421 
UTP O1G   H1G    sing N N 422 
UTP O3G   H3G    sing N N 423 
UTP "C5'" "C4'"  sing N N 424 
UTP "C5'" "H5'1" sing N N 425 
UTP "C5'" "H5'2" sing N N 426 
UTP "C4'" "O4'"  sing N N 427 
UTP "C4'" "C3'"  sing N N 428 
UTP "C4'" "H4'"  sing N N 429 
UTP "O4'" "C1'"  sing N N 430 
UTP "C1'" "C2'"  sing N N 431 
UTP "C1'" N1     sing N N 432 
UTP "C1'" "H1'"  sing N N 433 
UTP "C2'" "O2'"  sing N N 434 
UTP "C2'" "C3'"  sing N N 435 
UTP "C2'" "H2'"  sing N N 436 
UTP "O2'" HA     sing N N 437 
UTP "C3'" "O3'"  sing N N 438 
UTP "C3'" "H3'"  sing N N 439 
UTP "O3'" HB     sing N N 440 
UTP N1    C6     sing Y N 441 
UTP N1    C2     sing Y N 442 
UTP C6    C5     doub Y N 443 
UTP C6    H6     sing N N 444 
UTP C2    O2     doub N N 445 
UTP C2    N3     sing Y N 446 
UTP N3    C4     sing Y N 447 
UTP N3    H3     sing N N 448 
UTP C4    O4     doub N N 449 
UTP C4    C5     sing Y N 450 
UTP C5    H5     sing N N 451 
VAL N     CA     sing N N 452 
VAL N     H      sing N N 453 
VAL N     H2     sing N N 454 
VAL CA    C      sing N N 455 
VAL CA    CB     sing N N 456 
VAL CA    HA     sing N N 457 
VAL C     O      doub N N 458 
VAL C     OXT    sing N N 459 
VAL CB    CG1    sing N N 460 
VAL CB    CG2    sing N N 461 
VAL CB    HB     sing N N 462 
VAL CG1   HG11   sing N N 463 
VAL CG1   HG12   sing N N 464 
VAL CG1   HG13   sing N N 465 
VAL CG2   HG21   sing N N 466 
VAL CG2   HG22   sing N N 467 
VAL CG2   HG23   sing N N 468 
VAL OXT   HXT    sing N N 469 
# 
_pdbx_audit_support.funding_organization   'Ministry of Science and Technology (MoST, Taiwan)' 
_pdbx_audit_support.country                Taiwan 
_pdbx_audit_support.grant_number           111-2311-B-039-001-MY3 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'apo DwCdnB' 
# 
_atom_sites.entry_id                    8YSL 
_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]   0.028354 
_atom_sites.fract_transf_matrix[1][2]   -0.002770 
_atom_sites.fract_transf_matrix[1][3]   -0.008226 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021787 
_atom_sites.fract_transf_matrix[2][3]   -0.005457 
_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]   0.017825 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . MET A 1 1   ? -0.304  23.351  -33.970 1.00 50.87  ?  0   MET A N     1 
ATOM   2    C  CA    . MET A 1 1   ? -1.275  24.040  -33.126 1.00 51.12  ?  0   MET A CA    1 
ATOM   3    C  C     . MET A 1 1   ? -1.739  23.184  -31.950 1.00 47.58  ?  0   MET A C     1 
ATOM   4    O  O     . MET A 1 1   ? -1.640  21.957  -31.982 1.00 49.11  ?  0   MET A O     1 
ATOM   5    C  CB    . MET A 1 1   ? -2.484  24.477  -33.954 1.00 52.11  ?  0   MET A CB    1 
ATOM   6    C  CG    . MET A 1 1   ? -2.277  25.784  -34.696 1.00 57.50  ?  0   MET A CG    1 
ATOM   7    S  SD    . MET A 1 1   ? -3.705  26.235  -35.696 1.00 59.65  ?  0   MET A SD    1 
ATOM   8    C  CE    . MET A 1 1   ? -5.046  25.806  -34.583 1.00 54.13  ?  0   MET A CE    1 
ATOM   9    N  N     . MET A 1 2   ? -2.255  23.851  -30.919 1.00 44.32  ?  1   MET A N     1 
ATOM   10   C  CA    . MET A 1 2   ? -2.735  23.166  -29.725 1.00 42.59  ?  1   MET A CA    1 
ATOM   11   C  C     . MET A 1 2   ? -3.891  22.226  -30.054 1.00 35.24  ?  1   MET A C     1 
ATOM   12   O  O     . MET A 1 2   ? -4.739  22.516  -30.902 1.00 29.04  ?  1   MET A O     1 
ATOM   13   C  CB    . MET A 1 2   ? -3.178  24.186  -28.674 1.00 48.67  ?  1   MET A CB    1 
ATOM   14   C  CG    . MET A 1 2   ? -2.046  24.756  -27.841 1.00 55.59  ?  1   MET A CG    1 
ATOM   15   S  SD    . MET A 1 2   ? -1.813  23.826  -26.314 1.00 59.91  ?  1   MET A SD    1 
ATOM   16   C  CE    . MET A 1 2   ? -3.145  24.485  -25.312 1.00 59.52  ?  1   MET A CE    1 
ATOM   17   N  N     . ALA A 1 3   ? -3.916  21.090  -29.357 1.00 37.61  ?  2   ALA A N     1 
ATOM   18   C  CA    . ALA A 1 3   ? -4.979  20.109  -29.524 1.00 40.49  ?  2   ALA A CA    1 
ATOM   19   C  C     . ALA A 1 3   ? -6.332  20.709  -29.129 1.00 41.68  ?  2   ALA A C     1 
ATOM   20   O  O     . ALA A 1 3   ? -6.391  21.639  -28.319 1.00 36.31  ?  2   ALA A O     1 
ATOM   21   C  CB    . ALA A 1 3   ? -4.676  18.867  -28.685 1.00 41.77  ?  2   ALA A CB    1 
ATOM   22   N  N     . PRO A 1 4   ? -7.446  20.177  -29.691 1.00 51.29  ?  3   PRO A N     1 
ATOM   23   C  CA    . PRO A 1 4   ? -8.775  20.801  -29.533 1.00 54.29  ?  3   PRO A CA    1 
ATOM   24   C  C     . PRO A 1 4   ? -9.148  21.356  -28.158 1.00 53.26  ?  3   PRO A C     1 
ATOM   25   O  O     . PRO A 1 4   ? -9.403  22.558  -28.035 1.00 61.14  ?  3   PRO A O     1 
ATOM   26   C  CB    . PRO A 1 4   ? -9.720  19.656  -29.920 1.00 55.45  ?  3   PRO A CB    1 
ATOM   27   C  CG    . PRO A 1 4   ? -8.960  18.896  -30.957 1.00 53.30  ?  3   PRO A CG    1 
ATOM   28   C  CD    . PRO A 1 4   ? -7.491  19.028  -30.618 1.00 52.12  ?  3   PRO A CD    1 
ATOM   29   N  N     . VAL A 1 5   ? -9.213  20.511  -27.127 1.00 32.19  ?  4   VAL A N     1 
ATOM   30   C  CA    . VAL A 1 5   ? -9.677  20.938  -25.805 1.00 22.41  ?  4   VAL A CA    1 
ATOM   31   C  C     . VAL A 1 5   ? -8.538  20.856  -24.793 1.00 16.11  ?  4   VAL A C     1 
ATOM   32   O  O     . VAL A 1 5   ? -8.770  20.732  -23.584 1.00 18.35  ?  4   VAL A O     1 
ATOM   33   C  CB    . VAL A 1 5   ? -10.878 20.094  -25.338 1.00 25.55  ?  4   VAL A CB    1 
ATOM   34   C  CG1   . VAL A 1 5   ? -12.062 20.271  -26.287 1.00 26.51  ?  4   VAL A CG1   1 
ATOM   35   C  CG2   . VAL A 1 5   ? -10.500 18.637  -25.252 1.00 30.57  ?  4   VAL A CG2   1 
ATOM   36   N  N     . GLN A 1 6   ? -7.296  20.935  -25.276 1.00 14.72  ?  5   GLN A N     1 
ATOM   37   C  CA    . GLN A 1 6   ? -6.148  20.773  -24.388 1.00 15.96  ?  5   GLN A CA    1 
ATOM   38   C  C     . GLN A 1 6   ? -6.105  21.859  -23.316 1.00 14.85  ?  5   GLN A C     1 
ATOM   39   O  O     . GLN A 1 6   ? -5.776  21.583  -22.156 1.00 15.74  ?  5   GLN A O     1 
ATOM   40   C  CB    . GLN A 1 6   ? -4.854  20.770  -25.202 1.00 17.06  ?  5   GLN A CB    1 
ATOM   41   C  CG    . GLN A 1 6   ? -3.583  20.589  -24.360 1.00 18.84  ?  5   GLN A CG    1 
ATOM   42   C  CD    . GLN A 1 6   ? -3.502  19.214  -23.720 1.00 16.79  ?  5   GLN A CD    1 
ATOM   43   O  OE1   . GLN A 1 6   ? -4.317  18.337  -24.004 1.00 17.43  ?  5   GLN A OE1   1 
ATOM   44   N  NE2   . GLN A 1 6   ? -2.501  19.013  -22.872 1.00 12.59  ?  5   GLN A NE2   1 
ATOM   45   N  N     . LYS A 1 7   ? -6.428  23.101  -23.682 1.00 17.98  ?  6   LYS A N     1 
ATOM   46   C  CA    . LYS A 1 7   ? -6.386  24.185  -22.704 1.00 19.87  ?  6   LYS A CA    1 
ATOM   47   C  C     . LYS A 1 7   ? -7.314  23.897  -21.534 1.00 17.44  ?  6   LYS A C     1 
ATOM   48   O  O     . LYS A 1 7   ? -6.949  24.100  -20.369 1.00 14.71  ?  6   LYS A O     1 
ATOM   49   C  CB    . LYS A 1 7   ? -6.765  25.511  -23.366 1.00 23.48  ?  6   LYS A CB    1 
ATOM   50   C  CG    . LYS A 1 7   ? -6.881  26.675  -22.387 1.00 27.70  ?  6   LYS A CG    1 
ATOM   51   C  CD    . LYS A 1 7   ? -7.244  27.966  -23.104 1.00 34.22  ?  6   LYS A CD    1 
ATOM   52   C  CE    . LYS A 1 7   ? -7.317  29.162  -22.156 1.00 43.50  ?  6   LYS A CE    1 
ATOM   53   N  NZ    . LYS A 1 7   ? -8.650  29.290  -21.498 1.00 47.74  1  6   LYS A NZ    1 
ATOM   54   N  N     . GLN A 1 8   ? -8.516  23.401  -21.830 1.00 15.83  ?  7   GLN A N     1 
ATOM   55   C  CA    . GLN A 1 8   ? -9.486  23.135  -20.776 1.00 14.90  ?  7   GLN A CA    1 
ATOM   56   C  C     . GLN A 1 8   ? -9.088  21.928  -19.944 1.00 16.07  ?  7   GLN A C     1 
ATOM   57   O  O     . GLN A 1 8   ? -9.330  21.914  -18.734 1.00 16.70  ?  7   GLN A O     1 
ATOM   58   C  CB    . GLN A 1 8   ? -10.882 22.946  -21.368 1.00 15.60  ?  7   GLN A CB    1 
ATOM   59   C  CG    . GLN A 1 8   ? -11.527 24.247  -21.870 1.00 18.53  ?  7   GLN A CG    1 
ATOM   60   C  CD    . GLN A 1 8   ? -10.833 24.837  -23.086 1.00 20.69  ?  7   GLN A CD    1 
ATOM   61   O  OE1   . GLN A 1 8   ? -10.600 26.057  -23.162 1.00 24.71  ?  7   GLN A OE1   1 
ATOM   62   N  NE2   . GLN A 1 8   ? -10.501 23.986  -24.044 1.00 16.83  ?  7   GLN A NE2   1 
ATOM   63   N  N     . PHE A 1 9   ? -8.469  20.911  -20.553 1.00 16.96  ?  8   PHE A N     1 
ATOM   64   C  CA    . PHE A 1 9   ? -7.935  19.824  -19.739 1.00 12.94  ?  8   PHE A CA    1 
ATOM   65   C  C     . PHE A 1 9   ? -6.864  20.334  -18.783 1.00 13.37  ?  8   PHE A C     1 
ATOM   66   O  O     . PHE A 1 9   ? -6.829  19.930  -17.620 1.00 15.93  ?  8   PHE A O     1 
ATOM   67   C  CB    . PHE A 1 9   ? -7.367  18.702  -20.606 1.00 16.95  ?  8   PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 9   ? -8.328  17.570  -20.830 1.00 17.21  ?  8   PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 9   ? -8.619  16.675  -19.802 1.00 16.54  ?  8   PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 9   ? -8.933  17.398  -22.060 1.00 13.85  ?  8   PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 9   ? -9.513  15.626  -20.005 1.00 16.99  ?  8   PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 9   ? -9.825  16.354  -22.271 1.00 17.21  ?  8   PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 9   ? -10.114 15.466  -21.243 1.00 15.41  ?  8   PHE A CZ    1 
ATOM   74   N  N     . ARG A 1 10  ? -5.972  21.210  -19.255 1.00 12.13  ?  9   ARG A N     1 
ATOM   75   C  CA    . ARG A 1 10  ? -4.922  21.716  -18.373 1.00 15.86  ?  9   ARG A CA    1 
ATOM   76   C  C     . ARG A 1 10  ? -5.502  22.573  -17.248 1.00 12.17  ?  9   ARG A C     1 
ATOM   77   O  O     . ARG A 1 10  ? -5.028  22.513  -16.108 1.00 19.47  ?  9   ARG A O     1 
ATOM   78   C  CB    . ARG A 1 10  ? -3.887  22.501  -19.181 1.00 19.75  ?  9   ARG A CB    1 
ATOM   79   C  CG    . ARG A 1 10  ? -3.092  21.657  -20.191 1.00 17.75  ?  9   ARG A CG    1 
ATOM   80   C  CD    . ARG A 1 10  ? -2.316  20.532  -19.524 1.00 14.42  ?  9   ARG A CD    1 
ATOM   81   N  NE    . ARG A 1 10  ? -1.363  21.002  -18.518 1.00 19.68  ?  9   ARG A NE    1 
ATOM   82   C  CZ    . ARG A 1 10  ? -0.072  21.220  -18.755 1.00 24.11  ?  9   ARG A CZ    1 
ATOM   83   N  NH1   . ARG A 1 10  ? 0.420   21.023  -19.969 1.00 24.46  1  9   ARG A NH1   1 
ATOM   84   N  NH2   . ARG A 1 10  ? 0.727   21.639  -17.784 1.00 23.74  ?  9   ARG A NH2   1 
ATOM   85   N  N     . GLU A 1 11  ? -6.529  23.372  -17.547 1.00 13.32  ?  10  GLU A N     1 
ATOM   86   C  CA    . GLU A 1 11  ? -7.207  24.138  -16.500 1.00 16.22  ?  10  GLU A CA    1 
ATOM   87   C  C     . GLU A 1 11  ? -7.901  23.221  -15.491 1.00 18.47  ?  10  GLU A C     1 
ATOM   88   O  O     . GLU A 1 11  ? -7.821  23.443  -14.274 1.00 16.50  ?  10  GLU A O     1 
ATOM   89   C  CB    . GLU A 1 11  ? -8.213  25.096  -17.140 1.00 16.28  ?  10  GLU A CB    1 
ATOM   90   C  CG    . GLU A 1 11  ? -7.558  26.164  -18.029 1.00 18.32  ?  10  GLU A CG    1 
ATOM   91   C  CD    . GLU A 1 11  ? -8.566  27.069  -18.719 1.00 24.51  ?  10  GLU A CD    1 
ATOM   92   O  OE1   . GLU A 1 11  ? -8.188  28.192  -19.113 1.00 31.98  ?  10  GLU A OE1   1 
ATOM   93   O  OE2   . GLU A 1 11  ? -9.732  26.665  -18.880 1.00 27.13  -1 10  GLU A OE2   1 
ATOM   94   N  N     . PHE A 1 12  ? -8.604  22.199  -15.985 1.00 15.86  ?  11  PHE A N     1 
ATOM   95   C  CA    . PHE A 1 12  ? -9.171  21.162  -15.128 1.00 15.24  ?  11  PHE A CA    1 
ATOM   96   C  C     . PHE A 1 12  ? -8.108  20.555  -14.217 1.00 15.90  ?  11  PHE A C     1 
ATOM   97   O  O     . PHE A 1 12  ? -8.305  20.429  -13.001 1.00 17.26  ?  11  PHE A O     1 
ATOM   98   C  CB    . PHE A 1 12  ? -9.817  20.099  -16.029 1.00 14.89  ?  11  PHE A CB    1 
ATOM   99   C  CG    . PHE A 1 12  ? -10.410 18.935  -15.298 1.00 16.71  ?  11  PHE A CG    1 
ATOM   100  C  CD1   . PHE A 1 12  ? -11.307 19.129  -14.253 1.00 18.14  ?  11  PHE A CD1   1 
ATOM   101  C  CD2   . PHE A 1 12  ? -10.111 17.637  -15.694 1.00 16.02  ?  11  PHE A CD2   1 
ATOM   102  C  CE1   . PHE A 1 12  ? -11.864 18.044  -13.589 1.00 19.57  ?  11  PHE A CE1   1 
ATOM   103  C  CE2   . PHE A 1 12  ? -10.670 16.548  -15.043 1.00 13.90  ?  11  PHE A CE2   1 
ATOM   104  C  CZ    . PHE A 1 12  ? -11.547 16.754  -13.983 1.00 12.81  ?  11  PHE A CZ    1 
ATOM   105  N  N     . HIS A 1 13  ? -6.960  20.185  -14.793 1.00 13.15  ?  12  HIS A N     1 
ATOM   106  C  CA    . HIS A 1 13  ? -5.890  19.602  -13.989 1.00 14.57  ?  12  HIS A CA    1 
ATOM   107  C  C     . HIS A 1 13  ? -5.401  20.575  -12.927 1.00 14.11  ?  12  HIS A C     1 
ATOM   108  O  O     . HIS A 1 13  ? -5.159  20.183  -11.777 1.00 14.52  ?  12  HIS A O     1 
ATOM   109  C  CB    . HIS A 1 13  ? -4.716  19.176  -14.869 1.00 13.47  ?  12  HIS A CB    1 
ATOM   110  C  CG    . HIS A 1 13  ? -3.580  18.612  -14.081 1.00 16.74  ?  12  HIS A CG    1 
ATOM   111  N  ND1   . HIS A 1 13  ? -2.419  19.314  -13.841 1.00 15.52  ?  12  HIS A ND1   1 
ATOM   112  C  CD2   . HIS A 1 13  ? -3.453  17.433  -13.423 1.00 13.82  ?  12  HIS A CD2   1 
ATOM   113  C  CE1   . HIS A 1 13  ? -1.615  18.583  -13.087 1.00 13.70  ?  12  HIS A CE1   1 
ATOM   114  N  NE2   . HIS A 1 13  ? -2.219  17.439  -12.820 1.00 14.26  ?  12  HIS A NE2   1 
ATOM   115  N  N     . ASP A 1 14  ? -5.232  21.845  -13.306 1.00 15.38  ?  13  ASP A N     1 
ATOM   116  C  CA    . ASP A 1 14  ? -4.866  22.881  -12.347 1.00 18.61  ?  13  ASP A CA    1 
ATOM   117  C  C     . ASP A 1 14  ? -5.837  22.908  -11.180 1.00 19.37  ?  13  ASP A C     1 
ATOM   118  O  O     . ASP A 1 14  ? -5.441  23.152  -10.035 1.00 18.47  ?  13  ASP A O     1 
ATOM   119  C  CB    . ASP A 1 14  ? -4.846  24.253  -13.027 1.00 20.35  ?  13  ASP A CB    1 
ATOM   120  C  CG    . ASP A 1 14  ? -3.654  24.445  -13.938 1.00 25.07  ?  13  ASP A CG    1 
ATOM   121  O  OD1   . ASP A 1 14  ? -2.650  23.728  -13.783 1.00 23.57  ?  13  ASP A OD1   1 
ATOM   122  O  OD2   . ASP A 1 14  ? -3.728  25.330  -14.817 1.00 29.79  -1 13  ASP A OD2   1 
ATOM   123  N  N     . ARG A 1 15  ? -7.118  22.666  -11.458 1.00 19.15  ?  14  ARG A N     1 
ATOM   124  C  CA    . ARG A 1 15  ? -8.133  22.782  -10.415 1.00 16.66  ?  14  ARG A CA    1 
ATOM   125  C  C     . ARG A 1 15  ? -8.234  21.541  -9.538  1.00 18.11  ?  14  ARG A C     1 
ATOM   126  O  O     . ARG A 1 15  ? -8.660  21.649  -8.381  1.00 18.97  ?  14  ARG A O     1 
ATOM   127  C  CB    . ARG A 1 15  ? -9.488  23.081  -11.045 1.00 19.99  ?  14  ARG A CB    1 
ATOM   128  C  CG    . ARG A 1 15  ? -9.586  24.500  -11.552 1.00 19.40  ?  14  ARG A CG    1 
ATOM   129  C  CD    . ARG A 1 15  ? -10.587 24.658  -12.680 1.00 20.41  ?  14  ARG A CD    1 
ATOM   130  N  NE    . ARG A 1 15  ? -10.812 26.078  -12.929 1.00 26.19  ?  14  ARG A NE    1 
ATOM   131  C  CZ    . ARG A 1 15  ? -9.942  26.867  -13.555 1.00 29.19  ?  14  ARG A CZ    1 
ATOM   132  N  NH1   . ARG A 1 15  ? -8.795  26.369  -14.012 1.00 28.65  1  14  ARG A NH1   1 
ATOM   133  N  NH2   . ARG A 1 15  ? -10.216 28.153  -13.725 1.00 29.07  ?  14  ARG A NH2   1 
ATOM   134  N  N     . ILE A 1 16  ? -7.868  20.365  -10.052 1.00 14.50  ?  15  ILE A N     1 
ATOM   135  C  CA    . ILE A 1 16  ? -8.019  19.140  -9.269  1.00 16.44  ?  15  ILE A CA    1 
ATOM   136  C  C     . ILE A 1 16  ? -6.723  18.667  -8.614  1.00 18.20  ?  15  ILE A C     1 
ATOM   137  O  O     . ILE A 1 16  ? -6.782  17.865  -7.670  1.00 16.47  ?  15  ILE A O     1 
ATOM   138  C  CB    . ILE A 1 16  ? -8.600  17.992  -10.122 1.00 16.32  ?  15  ILE A CB    1 
ATOM   139  C  CG1   . ILE A 1 16  ? -7.572  17.532  -11.157 1.00 11.58  ?  15  ILE A CG1   1 
ATOM   140  C  CG2   . ILE A 1 16  ? -9.899  18.419  -10.800 1.00 14.93  ?  15  ILE A CG2   1 
ATOM   141  C  CD1   . ILE A 1 16  ? -8.050  16.347  -12.004 1.00 12.77  ?  15  ILE A CD1   1 
ATOM   142  N  N     . LYS A 1 17  ? -5.562  19.103  -9.097  1.00 17.94  ?  16  LYS A N     1 
ATOM   143  C  CA    . LYS A 1 17  ? -4.312  18.579  -8.568  1.00 20.49  ?  16  LYS A CA    1 
ATOM   144  C  C     . LYS A 1 17  ? -4.112  19.019  -7.123  1.00 21.66  ?  16  LYS A C     1 
ATOM   145  O  O     . LYS A 1 17  ? -4.492  20.126  -6.726  1.00 21.61  ?  16  LYS A O     1 
ATOM   146  C  CB    . LYS A 1 17  ? -3.125  19.023  -9.431  1.00 23.63  ?  16  LYS A CB    1 
ATOM   147  C  CG    . LYS A 1 17  ? -2.854  20.524  -9.438  1.00 31.34  ?  16  LYS A CG    1 
ATOM   148  C  CD    . LYS A 1 17  ? -1.686  20.858  -10.364 1.00 38.30  ?  16  LYS A CD    1 
ATOM   149  C  CE    . LYS A 1 17  ? -1.388  22.356  -10.392 1.00 42.15  ?  16  LYS A CE    1 
ATOM   150  N  NZ    . LYS A 1 17  ? -0.335  22.687  -11.398 1.00 43.00  1  16  LYS A NZ    1 
ATOM   151  N  N     . LEU A 1 18  ? -3.546  18.121  -6.327  1.00 21.20  ?  17  LEU A N     1 
ATOM   152  C  CA    . LEU A 1 18  ? -3.098  18.424  -4.977  1.00 24.72  ?  17  LEU A CA    1 
ATOM   153  C  C     . LEU A 1 18  ? -1.587  18.256  -4.945  1.00 23.45  ?  17  LEU A C     1 
ATOM   154  O  O     . LEU A 1 18  ? -1.066  17.245  -5.425  1.00 22.69  ?  17  LEU A O     1 
ATOM   155  C  CB    . LEU A 1 18  ? -3.770  17.505  -3.953  1.00 26.38  ?  17  LEU A CB    1 
ATOM   156  C  CG    . LEU A 1 18  ? -3.338  17.647  -2.490  1.00 25.93  ?  17  LEU A CG    1 
ATOM   157  C  CD1   . LEU A 1 18  ? -3.624  19.044  -1.960  1.00 23.49  ?  17  LEU A CD1   1 
ATOM   158  C  CD2   . LEU A 1 18  ? -4.041  16.607  -1.653  1.00 26.73  ?  17  LEU A CD2   1 
ATOM   159  N  N     . ALA A 1 19  ? -0.889  19.252  -4.405  1.00 21.68  ?  18  ALA A N     1 
ATOM   160  C  CA    . ALA A 1 19  ? 0.568   19.219  -4.399  1.00 23.22  ?  18  ALA A CA    1 
ATOM   161  C  C     . ALA A 1 19  ? 1.087   18.055  -3.559  1.00 24.00  ?  18  ALA A C     1 
ATOM   162  O  O     . ALA A 1 19  ? 0.551   17.743  -2.491  1.00 23.12  ?  18  ALA A O     1 
ATOM   163  C  CB    . ALA A 1 19  ? 1.126   20.546  -3.876  1.00 25.16  ?  18  ALA A CB    1 
ATOM   164  N  N     . GLN A 1 20  ? 2.141   17.410  -4.052  1.00 24.37  ?  19  GLN A N     1 
ATOM   165  C  CA    . GLN A 1 20  ? 2.723   16.259  -3.382  1.00 22.87  ?  19  GLN A CA    1 
ATOM   166  C  C     . GLN A 1 20  ? 3.368   16.667  -2.055  1.00 23.93  ?  19  GLN A C     1 
ATOM   167  O  O     . GLN A 1 20  ? 3.503   17.853  -1.732  1.00 24.64  ?  19  GLN A O     1 
ATOM   168  C  CB    . GLN A 1 20  ? 3.762   15.598  -4.282  1.00 21.54  ?  19  GLN A CB    1 
ATOM   169  C  CG    . GLN A 1 20  ? 4.910   16.524  -4.623  1.00 25.46  ?  19  GLN A CG    1 
ATOM   170  C  CD    . GLN A 1 20  ? 5.954   15.872  -5.495  1.00 25.08  ?  19  GLN A CD    1 
ATOM   171  O  OE1   . GLN A 1 20  ? 6.383   14.751  -5.234  1.00 24.82  ?  19  GLN A OE1   1 
ATOM   172  N  NE2   . GLN A 1 20  ? 6.378   16.579  -6.538  1.00 27.63  ?  19  GLN A NE2   1 
ATOM   173  N  N     . TYR A 1 21  ? 3.793   15.649  -1.295  1.00 21.63  ?  20  TYR A N     1 
ATOM   174  C  CA    . TYR A 1 21  ? 4.407   15.868  0.014   1.00 25.30  ?  20  TYR A CA    1 
ATOM   175  C  C     . TYR A 1 21  ? 5.521   16.908  -0.050  1.00 26.91  ?  20  TYR A C     1 
ATOM   176  O  O     . TYR A 1 21  ? 5.537   17.866  0.729   1.00 28.03  ?  20  TYR A O     1 
ATOM   177  C  CB    . TYR A 1 21  ? 4.963   14.549  0.563   1.00 22.00  ?  20  TYR A CB    1 
ATOM   178  C  CG    . TYR A 1 21  ? 3.958   13.624  1.210   1.00 22.82  ?  20  TYR A CG    1 
ATOM   179  C  CD1   . TYR A 1 21  ? 3.078   14.080  2.182   1.00 21.61  ?  20  TYR A CD1   1 
ATOM   180  C  CD2   . TYR A 1 21  ? 3.908   12.278  0.858   1.00 22.32  ?  20  TYR A CD2   1 
ATOM   181  C  CE1   . TYR A 1 21  ? 2.173   13.224  2.785   1.00 24.73  ?  20  TYR A CE1   1 
ATOM   182  C  CE2   . TYR A 1 21  ? 3.005   11.413  1.456   1.00 23.64  ?  20  TYR A CE2   1 
ATOM   183  C  CZ    . TYR A 1 21  ? 2.138   11.889  2.417   1.00 24.64  ?  20  TYR A CZ    1 
ATOM   184  O  OH    . TYR A 1 21  ? 1.235   11.026  3.014   1.00 21.97  ?  20  TYR A OH    1 
ATOM   185  N  N     . ASP A 1 22  ? 6.467   16.732  -0.980  1.00 29.67  ?  21  ASP A N     1 
ATOM   186  C  CA    . ASP A 1 22  ? 7.627   17.615  -1.076  1.00 34.34  ?  21  ASP A CA    1 
ATOM   187  C  C     . ASP A 1 22  ? 7.268   19.043  -1.473  1.00 34.13  ?  21  ASP A C     1 
ATOM   188  O  O     . ASP A 1 22  ? 8.136   19.920  -1.397  1.00 32.16  ?  21  ASP A O     1 
ATOM   189  C  CB    . ASP A 1 22  ? 8.639   17.051  -2.077  1.00 39.69  ?  21  ASP A CB    1 
ATOM   190  C  CG    . ASP A 1 22  ? 9.332   15.797  -1.569  1.00 46.05  ?  21  ASP A CG    1 
ATOM   191  O  OD1   . ASP A 1 22  ? 9.132   15.429  -0.394  1.00 48.18  ?  21  ASP A OD1   1 
ATOM   192  O  OD2   . ASP A 1 22  ? 10.082  15.177  -2.353  1.00 48.78  -1 21  ASP A OD2   1 
ATOM   193  N  N     . GLU A 1 23  ? 6.030   19.297  -1.901  1.00 32.06  ?  22  GLU A N     1 
ATOM   194  C  CA    . GLU A 1 23  ? 5.590   20.638  -2.266  1.00 32.88  ?  22  GLU A CA    1 
ATOM   195  C  C     . GLU A 1 23  ? 4.401   21.106  -1.440  1.00 32.38  ?  22  GLU A C     1 
ATOM   196  O  O     . GLU A 1 23  ? 3.759   22.094  -1.810  1.00 36.38  ?  22  GLU A O     1 
ATOM   197  C  CB    . GLU A 1 23  ? 5.216   20.705  -3.751  1.00 31.56  ?  22  GLU A CB    1 
ATOM   198  C  CG    . GLU A 1 23  ? 6.230   20.119  -4.714  1.00 34.78  ?  22  GLU A CG    1 
ATOM   199  C  CD    . GLU A 1 23  ? 5.821   20.329  -6.162  1.00 37.40  ?  22  GLU A CD    1 
ATOM   200  O  OE1   . GLU A 1 23  ? 5.723   21.496  -6.587  1.00 41.26  ?  22  GLU A OE1   1 
ATOM   201  O  OE2   . GLU A 1 23  ? 5.577   19.336  -6.875  1.00 38.16  -1 22  GLU A OE2   1 
ATOM   202  N  N     . ASN A 1 24  ? 4.070   20.414  -0.351  1.00 31.82  ?  23  ASN A N     1 
ATOM   203  C  CA    . ASN A 1 24  ? 2.845   20.690  0.400   1.00 32.41  ?  23  ASN A CA    1 
ATOM   204  C  C     . ASN A 1 24  ? 3.183   20.648  1.886   1.00 31.52  ?  23  ASN A C     1 
ATOM   205  O  O     . ASN A 1 24  ? 3.240   19.570  2.484   1.00 31.44  ?  23  ASN A O     1 
ATOM   206  C  CB    . ASN A 1 24  ? 1.755   19.685  0.046   1.00 31.67  ?  23  ASN A CB    1 
ATOM   207  C  CG    . ASN A 1 24  ? 0.378   20.131  0.491   1.00 30.11  ?  23  ASN A CG    1 
ATOM   208  O  OD1   . ASN A 1 24  ? 0.214   20.757  1.540   1.00 34.37  ?  23  ASN A OD1   1 
ATOM   209  N  ND2   . ASN A 1 24  ? -0.626  19.809  -0.314  1.00 26.64  ?  23  ASN A ND2   1 
ATOM   210  N  N     . GLN A 1 25  ? 3.382   21.824  2.485   1.00 33.21  ?  24  GLN A N     1 
ATOM   211  C  CA    . GLN A 1 25  ? 3.778   21.864  3.888   1.00 34.57  ?  24  GLN A CA    1 
ATOM   212  C  C     . GLN A 1 25  ? 2.647   21.419  4.805   1.00 33.26  ?  24  GLN A C     1 
ATOM   213  O  O     . GLN A 1 25  ? 2.907   20.816  5.849   1.00 35.95  ?  24  GLN A O     1 
ATOM   214  C  CB    . GLN A 1 25  ? 4.253   23.268  4.261   1.00 42.57  ?  24  GLN A CB    1 
ATOM   215  C  CG    . GLN A 1 25  ? 5.148   23.310  5.493   1.00 51.61  ?  24  GLN A CG    1 
ATOM   216  C  CD    . GLN A 1 25  ? 6.342   24.229  5.308   1.00 58.46  ?  24  GLN A CD    1 
ATOM   217  O  OE1   . GLN A 1 25  ? 7.476   23.859  5.616   1.00 62.70  ?  24  GLN A OE1   1 
ATOM   218  N  NE2   . GLN A 1 25  ? 6.094   25.432  4.798   1.00 58.93  ?  24  GLN A NE2   1 
ATOM   219  N  N     . THR A 1 26  ? 1.393   21.697  4.436   1.00 32.00  ?  25  THR A N     1 
ATOM   220  C  CA    . THR A 1 26  ? 0.266   21.269  5.261   1.00 32.99  ?  25  THR A CA    1 
ATOM   221  C  C     . THR A 1 26  ? 0.205   19.749  5.373   1.00 32.52  ?  25  THR A C     1 
ATOM   222  O  O     . THR A 1 26  ? -0.009  19.203  6.465   1.00 35.82  ?  25  THR A O     1 
ATOM   223  C  CB    . THR A 1 26  ? -1.043  21.805  4.679   1.00 36.49  ?  25  THR A CB    1 
ATOM   224  O  OG1   . THR A 1 26  ? -0.918  23.211  4.431   1.00 38.36  ?  25  THR A OG1   1 
ATOM   225  C  CG2   . THR A 1 26  ? -2.198  21.561  5.642   1.00 36.82  ?  25  THR A CG2   1 
ATOM   226  N  N     . LEU A 1 27  ? 0.385   19.049  4.250   1.00 32.60  ?  26  LEU A N     1 
ATOM   227  C  CA    . LEU A 1 27  ? 0.381   17.591  4.290   1.00 28.61  ?  26  LEU A CA    1 
ATOM   228  C  C     . LEU A 1 27  ? 1.543   17.065  5.120   1.00 28.00  ?  26  LEU A C     1 
ATOM   229  O  O     . LEU A 1 27  ? 1.370   16.134  5.918   1.00 27.25  ?  26  LEU A O     1 
ATOM   230  C  CB    . LEU A 1 27  ? 0.424   17.019  2.874   1.00 23.65  ?  26  LEU A CB    1 
ATOM   231  C  CG    . LEU A 1 27  ? -0.861  17.207  2.061   1.00 27.89  ?  26  LEU A CG    1 
ATOM   232  C  CD1   . LEU A 1 27  ? -0.728  16.574  0.686   1.00 24.76  ?  26  LEU A CD1   1 
ATOM   233  C  CD2   . LEU A 1 27  ? -2.058  16.633  2.806   1.00 26.22  ?  26  LEU A CD2   1 
ATOM   234  N  N     . ARG A 1 28  ? 2.733   17.648  4.947   1.00 27.01  ?  27  ARG A N     1 
ATOM   235  C  CA    . ARG A 1 28  ? 3.879   17.226  5.748   1.00 30.35  ?  27  ARG A CA    1 
ATOM   236  C  C     . ARG A 1 28  ? 3.612   17.428  7.234   1.00 30.91  ?  27  ARG A C     1 
ATOM   237  O  O     . ARG A 1 28  ? 3.931   16.558  8.049   1.00 34.81  ?  27  ARG A O     1 
ATOM   238  C  CB    . ARG A 1 28  ? 5.143   17.978  5.322   1.00 28.76  ?  27  ARG A CB    1 
ATOM   239  C  CG    . ARG A 1 28  ? 5.611   17.662  3.906   1.00 28.86  ?  27  ARG A CG    1 
ATOM   240  C  CD    . ARG A 1 28  ? 7.049   18.109  3.649   1.00 25.13  ?  27  ARG A CD    1 
ATOM   241  N  NE    . ARG A 1 28  ? 7.263   19.521  3.958   1.00 26.86  ?  27  ARG A NE    1 
ATOM   242  C  CZ    . ARG A 1 28  ? 7.089   20.516  3.091   1.00 31.30  ?  27  ARG A CZ    1 
ATOM   243  N  NH1   . ARG A 1 28  ? 6.687   20.264  1.852   1.00 27.42  1  27  ARG A NH1   1 
ATOM   244  N  NH2   . ARG A 1 28  ? 7.313   21.770  3.466   1.00 33.87  ?  27  ARG A NH2   1 
ATOM   245  N  N     . ASP A 1 29  ? 2.995   18.553  7.600   1.00 32.35  ?  28  ASP A N     1 
ATOM   246  C  CA    . ASP A 1 29  ? 2.751   18.842  9.011   1.00 34.16  ?  28  ASP A CA    1 
ATOM   247  C  C     . ASP A 1 29  ? 1.726   17.886  9.605   1.00 34.52  ?  28  ASP A C     1 
ATOM   248  O  O     . ASP A 1 29  ? 1.901   17.408  10.729  1.00 34.96  ?  28  ASP A O     1 
ATOM   249  C  CB    . ASP A 1 29  ? 2.297   20.292  9.183   1.00 39.04  ?  28  ASP A CB    1 
ATOM   250  C  CG    . ASP A 1 29  ? 3.405   21.290  8.896   1.00 40.32  ?  28  ASP A CG    1 
ATOM   251  O  OD1   . ASP A 1 29  ? 4.573   20.870  8.751   1.00 38.93  ?  28  ASP A OD1   1 
ATOM   252  O  OD2   . ASP A 1 29  ? 3.105   22.499  8.812   1.00 42.03  -1 28  ASP A OD2   1 
ATOM   253  N  N     . GLU A 1 30  ? 0.654   17.585  8.867   1.00 35.89  ?  29  GLU A N     1 
ATOM   254  C  CA    . GLU A 1 30  ? -0.329  16.631  9.382   1.00 38.00  ?  29  GLU A CA    1 
ATOM   255  C  C     . GLU A 1 30  ? 0.271   15.231  9.516   1.00 36.40  ?  29  GLU A C     1 
ATOM   256  O  O     . GLU A 1 30  ? 0.082   14.555  10.543  1.00 37.00  ?  29  GLU A O     1 
ATOM   257  C  CB    . GLU A 1 30  ? -1.561  16.623  8.477   1.00 38.13  ?  29  GLU A CB    1 
ATOM   258  C  CG    . GLU A 1 30  ? -2.302  17.953  8.473   1.00 43.29  ?  29  GLU A CG    1 
ATOM   259  C  CD    . GLU A 1 30  ? -3.212  18.118  7.272   1.00 47.65  ?  29  GLU A CD    1 
ATOM   260  O  OE1   . GLU A 1 30  ? -4.208  18.867  7.374   1.00 49.24  ?  29  GLU A OE1   1 
ATOM   261  O  OE2   . GLU A 1 30  ? -2.930  17.502  6.223   1.00 48.02  -1 29  GLU A OE2   1 
ATOM   262  N  N     . ARG A 1 31  ? 1.010   14.791  8.494   1.00 36.08  ?  30  ARG A N     1 
ATOM   263  C  CA    . ARG A 1 31  ? 1.692   13.504  8.556   1.00 34.16  ?  30  ARG A CA    1 
ATOM   264  C  C     . ARG A 1 31  ? 2.615   13.427  9.767   1.00 33.97  ?  30  ARG A C     1 
ATOM   265  O  O     . ARG A 1 31  ? 2.578   12.454  10.533  1.00 31.07  ?  30  ARG A O     1 
ATOM   266  C  CB    . ARG A 1 31  ? 2.477   13.282  7.260   1.00 34.57  ?  30  ARG A CB    1 
ATOM   267  C  CG    . ARG A 1 31  ? 3.519   12.174  7.333   1.00 32.40  ?  30  ARG A CG    1 
ATOM   268  C  CD    . ARG A 1 31  ? 4.565   12.354  6.252   1.00 31.01  ?  30  ARG A CD    1 
ATOM   269  N  NE    . ARG A 1 31  ? 5.453   13.474  6.549   1.00 33.11  ?  30  ARG A NE    1 
ATOM   270  C  CZ    . ARG A 1 31  ? 6.292   14.025  5.677   1.00 32.22  ?  30  ARG A CZ    1 
ATOM   271  N  NH1   . ARG A 1 31  ? 6.359   13.575  4.431   1.00 30.04  1  30  ARG A NH1   1 
ATOM   272  N  NH2   . ARG A 1 31  ? 7.060   15.040  6.053   1.00 31.81  ?  30  ARG A NH2   1 
ATOM   273  N  N     . ASP A 1 32  ? 3.442   14.460  9.962   1.00 35.10  ?  31  ASP A N     1 
ATOM   274  C  CA    . ASP A 1 32  ? 4.407   14.455  11.055  1.00 38.69  ?  31  ASP A CA    1 
ATOM   275  C  C     . ASP A 1 32  ? 3.727   14.533  12.416  1.00 39.04  ?  31  ASP A C     1 
ATOM   276  O  O     . ASP A 1 32  ? 4.231   13.959  13.388  1.00 39.71  ?  31  ASP A O     1 
ATOM   277  C  CB    . ASP A 1 32  ? 5.392   15.610  10.884  1.00 41.02  ?  31  ASP A CB    1 
ATOM   278  C  CG    . ASP A 1 32  ? 6.287   15.436  9.672   1.00 43.10  ?  31  ASP A CG    1 
ATOM   279  O  OD1   . ASP A 1 32  ? 6.414   14.289  9.186   1.00 42.54  ?  31  ASP A OD1   1 
ATOM   280  O  OD2   . ASP A 1 32  ? 6.869   16.443  9.209   1.00 42.57  -1 31  ASP A OD2   1 
ATOM   281  N  N     . ALA A 1 33  ? 2.601   15.244  12.514  1.00 38.82  ?  32  ALA A N     1 
ATOM   282  C  CA    . ALA A 1 33  ? 1.841   15.234  13.758  1.00 39.18  ?  32  ALA A CA    1 
ATOM   283  C  C     . ALA A 1 33  ? 1.391   13.822  14.104  1.00 41.18  ?  32  ALA A C     1 
ATOM   284  O  O     . ALA A 1 33  ? 1.513   13.385  15.258  1.00 41.71  ?  32  ALA A O     1 
ATOM   285  C  CB    . ALA A 1 33  ? 0.639   16.173  13.654  1.00 38.78  ?  32  ALA A CB    1 
ATOM   286  N  N     . VAL A 1 34  ? 0.887   13.084  13.110  1.00 39.03  ?  33  VAL A N     1 
ATOM   287  C  CA    . VAL A 1 34  ? 0.478   11.705  13.378  1.00 39.00  ?  33  VAL A CA    1 
ATOM   288  C  C     . VAL A 1 34  ? 1.680   10.853  13.778  1.00 39.00  ?  33  VAL A C     1 
ATOM   289  O  O     . VAL A 1 34  ? 1.591   10.023  14.694  1.00 37.91  ?  33  VAL A O     1 
ATOM   290  C  CB    . VAL A 1 34  ? -0.270  11.116  12.168  1.00 37.27  ?  33  VAL A CB    1 
ATOM   291  C  CG1   . VAL A 1 34  ? -0.349  9.599   12.272  1.00 35.02  ?  33  VAL A CG1   1 
ATOM   292  C  CG2   . VAL A 1 34  ? -1.670  11.711  12.099  1.00 35.70  ?  33  VAL A CG2   1 
ATOM   293  N  N     . LEU A 1 35  ? 2.823   11.051  13.115  1.00 38.71  ?  34  LEU A N     1 
ATOM   294  C  CA    . LEU A 1 35  ? 4.011   10.260  13.443  1.00 39.88  ?  34  LEU A CA    1 
ATOM   295  C  C     . LEU A 1 35  ? 4.480   10.520  14.875  1.00 41.11  ?  34  LEU A C     1 
ATOM   296  O  O     . LEU A 1 35  ? 4.821   9.582   15.614  1.00 40.64  ?  34  LEU A O     1 
ATOM   297  C  CB    . LEU A 1 35  ? 5.133   10.557  12.447  1.00 38.45  ?  34  LEU A CB    1 
ATOM   298  C  CG    . LEU A 1 35  ? 4.903   10.142  10.990  1.00 34.38  ?  34  LEU A CG    1 
ATOM   299  C  CD1   . LEU A 1 35  ? 6.094   10.520  10.124  1.00 32.36  ?  34  LEU A CD1   1 
ATOM   300  C  CD2   . LEU A 1 35  ? 4.620   8.647   10.885  1.00 33.58  ?  34  LEU A CD2   1 
ATOM   301  N  N     . THR A 1 36  ? 4.513   11.790  15.284  1.00 42.21  ?  35  THR A N     1 
ATOM   302  C  CA    . THR A 1 36  ? 4.844   12.112  16.669  1.00 43.95  ?  35  THR A CA    1 
ATOM   303  C  C     . THR A 1 36  ? 3.857   11.460  17.627  1.00 45.50  ?  35  THR A C     1 
ATOM   304  O  O     . THR A 1 36  ? 4.249   10.928  18.679  1.00 46.85  ?  35  THR A O     1 
ATOM   305  C  CB    . THR A 1 36  ? 4.852   13.628  16.868  1.00 44.19  ?  35  THR A CB    1 
ATOM   306  O  OG1   . THR A 1 36  ? 5.775   14.225  15.950  1.00 41.36  ?  35  THR A OG1   1 
ATOM   307  C  CG2   . THR A 1 36  ? 5.253   13.982  18.300  1.00 47.91  ?  35  THR A CG2   1 
ATOM   308  N  N     . ALA A 1 37  ? 2.567   11.507  17.283  1.00 44.95  ?  36  ALA A N     1 
ATOM   309  C  CA    . ALA A 1 37  ? 1.552   10.895  18.129  1.00 42.38  ?  36  ALA A CA    1 
ATOM   310  C  C     . ALA A 1 37  ? 1.791   9.400   18.289  1.00 41.36  ?  36  ALA A C     1 
ATOM   311  O  O     . ALA A 1 37  ? 1.623   8.857   19.386  1.00 43.94  ?  36  ALA A O     1 
ATOM   312  C  CB    . ALA A 1 37  ? 0.163   11.163  17.557  1.00 43.34  ?  36  ALA A CB    1 
ATOM   313  N  N     . VAL A 1 38  ? 2.201   8.716   17.215  1.00 38.51  ?  37  VAL A N     1 
ATOM   314  C  CA    . VAL A 1 38  ? 2.452   7.281   17.352  1.00 43.59  ?  37  VAL A CA    1 
ATOM   315  C  C     . VAL A 1 38  ? 3.707   7.035   18.183  1.00 47.42  ?  37  VAL A C     1 
ATOM   316  O  O     . VAL A 1 38  ? 3.770   6.059   18.933  1.00 47.29  ?  37  VAL A O     1 
ATOM   317  C  CB    . VAL A 1 38  ? 2.532   6.552   15.989  1.00 44.47  ?  37  VAL A CB    1 
ATOM   318  C  CG1   . VAL A 1 38  ? 1.406   6.965   15.059  1.00 36.69  ?  37  VAL A CG1   1 
ATOM   319  C  CG2   . VAL A 1 38  ? 3.876   6.731   15.327  1.00 48.50  ?  37  VAL A CG2   1 
ATOM   320  N  N     . ARG A 1 39  ? 4.708   7.917   18.101  1.00 47.95  ?  38  ARG A N     1 
ATOM   321  C  CA    . ARG A 1 39  ? 5.891   7.745   18.948  1.00 49.51  ?  38  ARG A CA    1 
ATOM   322  C  C     . ARG A 1 39  ? 5.529   7.840   20.432  1.00 52.94  ?  38  ARG A C     1 
ATOM   323  O  O     . ARG A 1 39  ? 5.873   6.957   21.236  1.00 53.02  ?  38  ARG A O     1 
ATOM   324  C  CB    . ARG A 1 39  ? 6.955   8.780   18.582  1.00 51.54  ?  38  ARG A CB    1 
ATOM   325  C  CG    . ARG A 1 39  ? 7.846   8.363   17.424  1.00 54.94  ?  38  ARG A CG    1 
ATOM   326  C  CD    . ARG A 1 39  ? 8.926   9.396   17.137  1.00 59.69  ?  38  ARG A CD    1 
ATOM   327  N  NE    . ARG A 1 39  ? 8.376   10.622  16.564  1.00 63.31  ?  38  ARG A NE    1 
ATOM   328  C  CZ    . ARG A 1 39  ? 8.289   10.863  15.260  1.00 63.83  ?  38  ARG A CZ    1 
ATOM   329  N  NH1   . ARG A 1 39  ? 8.718   9.961   14.384  1.00 63.21  1  38  ARG A NH1   1 
ATOM   330  N  NH2   . ARG A 1 39  ? 7.775   12.007  14.830  1.00 63.31  ?  38  ARG A NH2   1 
ATOM   331  N  N     . GLU A 1 40  ? 4.821   8.907   20.809  1.00 55.35  ?  39  GLU A N     1 
ATOM   332  C  CA    . GLU A 1 40  ? 4.427   9.067   22.209  1.00 61.64  ?  39  GLU A CA    1 
ATOM   333  C  C     . GLU A 1 40  ? 3.469   7.961   22.649  1.00 60.36  ?  39  GLU A C     1 
ATOM   334  O  O     . GLU A 1 40  ? 3.566   7.443   23.776  1.00 61.52  ?  39  GLU A O     1 
ATOM   335  C  CB    . GLU A 1 40  ? 3.801   10.444  22.418  1.00 69.81  ?  39  GLU A CB    1 
ATOM   336  C  CG    . GLU A 1 40  ? 4.741   11.597  22.107  1.00 76.47  ?  39  GLU A CG    1 
ATOM   337  C  CD    . GLU A 1 40  ? 4.093   12.949  22.325  1.00 83.88  ?  39  GLU A CD    1 
ATOM   338  O  OE1   . GLU A 1 40  ? 2.859   12.994  22.516  1.00 86.93  ?  39  GLU A OE1   1 
ATOM   339  O  OE2   . GLU A 1 40  ? 4.816   13.968  22.307  1.00 86.59  -1 39  GLU A OE2   1 
ATOM   340  N  N     . GLY A 1 41  ? 2.546   7.572   21.769  1.00 56.27  ?  40  GLY A N     1 
ATOM   341  C  CA    . GLY A 1 41  ? 1.641   6.490   22.092  1.00 52.43  ?  40  GLY A CA    1 
ATOM   342  C  C     . GLY A 1 41  ? 2.351   5.170   22.289  1.00 47.74  ?  40  GLY A C     1 
ATOM   343  O  O     . GLY A 1 41  ? 1.953   4.377   23.140  1.00 47.69  ?  40  GLY A O     1 
ATOM   344  N  N     . LEU A 1 42  ? 3.409   4.914   21.514  1.00 43.86  ?  41  LEU A N     1 
ATOM   345  C  CA    . LEU A 1 42  ? 4.182   3.691   21.704  1.00 43.90  ?  41  LEU A CA    1 
ATOM   346  C  C     . LEU A 1 42  ? 4.916   3.712   23.036  1.00 45.83  ?  41  LEU A C     1 
ATOM   347  O  O     . LEU A 1 42  ? 4.998   2.681   23.719  1.00 42.90  ?  41  LEU A O     1 
ATOM   348  C  CB    . LEU A 1 42  ? 5.167   3.497   20.552  1.00 42.01  ?  41  LEU A CB    1 
ATOM   349  C  CG    . LEU A 1 42  ? 4.572   2.980   19.241  1.00 38.38  ?  41  LEU A CG    1 
ATOM   350  C  CD1   . LEU A 1 42  ? 5.667   2.742   18.204  1.00 34.01  ?  41  LEU A CD1   1 
ATOM   351  C  CD2   . LEU A 1 42  ? 3.763   1.711   19.496  1.00 38.92  ?  41  LEU A CD2   1 
ATOM   352  N  N     . LYS A 1 43  ? 5.473   4.871   23.407  1.00 48.84  ?  42  LYS A N     1 
ATOM   353  C  CA    . LYS A 1 43  ? 5.989   5.034   24.765  1.00 55.99  ?  42  LYS A CA    1 
ATOM   354  C  C     . LYS A 1 43  ? 4.963   4.563   25.789  1.00 57.89  ?  42  LYS A C     1 
ATOM   355  O  O     . LYS A 1 43  ? 5.250   3.711   26.642  1.00 59.22  ?  42  LYS A O     1 
ATOM   356  C  CB    . LYS A 1 43  ? 6.353   6.496   25.028  1.00 61.22  ?  42  LYS A CB    1 
ATOM   357  C  CG    . LYS A 1 43  ? 7.756   6.902   24.627  1.00 66.33  ?  42  LYS A CG    1 
ATOM   358  C  CD    . LYS A 1 43  ? 8.004   8.353   25.020  1.00 70.76  ?  42  LYS A CD    1 
ATOM   359  C  CE    . LYS A 1 43  ? 9.430   8.792   24.733  1.00 71.83  ?  42  LYS A CE    1 
ATOM   360  N  NZ    . LYS A 1 43  ? 9.649   10.213  25.127  1.00 72.19  1  42  LYS A NZ    1 
ATOM   361  N  N     . LYS A 1 44  ? 3.743   5.097   25.695  1.00 58.96  ?  43  LYS A N     1 
ATOM   362  C  CA    . LYS A 1 44  ? 2.716   4.753   26.678  1.00 62.51  ?  43  LYS A CA    1 
ATOM   363  C  C     . LYS A 1 44  ? 2.328   3.276   26.604  1.00 61.45  ?  43  LYS A C     1 
ATOM   364  O  O     . LYS A 1 44  ? 2.119   2.632   27.639  1.00 61.84  ?  43  LYS A O     1 
ATOM   365  C  CB    . LYS A 1 44  ? 1.490   5.645   26.489  1.00 66.98  ?  43  LYS A CB    1 
ATOM   366  C  CG    . LYS A 1 44  ? 1.763   7.121   26.743  1.00 72.34  ?  43  LYS A CG    1 
ATOM   367  C  CD    . LYS A 1 44  ? 0.473   7.910   26.873  1.00 76.24  ?  43  LYS A CD    1 
ATOM   368  C  CE    . LYS A 1 44  ? 0.747   9.365   27.213  1.00 79.26  ?  43  LYS A CE    1 
ATOM   369  N  NZ    . LYS A 1 44  ? -0.515  10.126  27.437  1.00 81.69  1  43  LYS A NZ    1 
ATOM   370  N  N     . VAL A 1 45  ? 2.238   2.721   25.394  1.00 57.30  ?  44  VAL A N     1 
ATOM   371  C  CA    . VAL A 1 45  ? 1.775   1.346   25.222  1.00 54.09  ?  44  VAL A CA    1 
ATOM   372  C  C     . VAL A 1 45  ? 2.792   0.363   25.788  1.00 53.67  ?  44  VAL A C     1 
ATOM   373  O  O     . VAL A 1 45  ? 2.423   -0.671  26.357  1.00 52.64  ?  44  VAL A O     1 
ATOM   374  C  CB    . VAL A 1 45  ? 1.475   1.067   23.735  1.00 51.10  ?  44  VAL A CB    1 
ATOM   375  C  CG1   . VAL A 1 45  ? 1.382   -0.429  23.466  1.00 50.01  ?  44  VAL A CG1   1 
ATOM   376  C  CG2   . VAL A 1 45  ? 0.184   1.757   23.312  1.00 48.73  ?  44  VAL A CG2   1 
ATOM   377  N  N     . PHE A 1 46  ? 4.081   0.665   25.648  1.00 52.65  ?  45  PHE A N     1 
ATOM   378  C  CA    . PHE A 1 46  ? 5.121   -0.217  26.158  1.00 51.39  ?  45  PHE A CA    1 
ATOM   379  C  C     . PHE A 1 46  ? 5.534   0.110   27.587  1.00 54.41  ?  45  PHE A C     1 
ATOM   380  O  O     . PHE A 1 46  ? 6.367   -0.608  28.150  1.00 53.33  ?  45  PHE A O     1 
ATOM   381  C  CB    . PHE A 1 46  ? 6.339   -0.182  25.232  1.00 48.18  ?  45  PHE A CB    1 
ATOM   382  C  CG    . PHE A 1 46  ? 6.190   -1.059  24.022  1.00 47.70  ?  45  PHE A CG    1 
ATOM   383  C  CD1   . PHE A 1 46  ? 5.365   -0.681  22.974  1.00 46.78  ?  45  PHE A CD1   1 
ATOM   384  C  CD2   . PHE A 1 46  ? 6.854   -2.272  23.944  1.00 46.94  ?  45  PHE A CD2   1 
ATOM   385  C  CE1   . PHE A 1 46  ? 5.213   -1.491  21.866  1.00 48.18  ?  45  PHE A CE1   1 
ATOM   386  C  CE2   . PHE A 1 46  ? 6.707   -3.088  22.841  1.00 48.81  ?  45  PHE A CE2   1 
ATOM   387  C  CZ    . PHE A 1 46  ? 5.884   -2.698  21.798  1.00 49.11  ?  45  PHE A CZ    1 
ATOM   388  N  N     . ALA A 1 47  ? 4.981   1.175   28.178  1.00 63.39  ?  46  ALA A N     1 
ATOM   389  C  CA    . ALA A 1 47  ? 5.216   1.441   29.596  1.00 68.36  ?  46  ALA A CA    1 
ATOM   390  C  C     . ALA A 1 47  ? 4.883   0.236   30.473  1.00 73.42  ?  46  ALA A C     1 
ATOM   391  O  O     . ALA A 1 47  ? 5.574   -0.028  31.464  1.00 75.36  ?  46  ALA A O     1 
ATOM   392  C  CB    . ALA A 1 47  ? 4.407   2.660   30.040  1.00 70.78  ?  46  ALA A CB    1 
ATOM   393  N  N     . ASP A 1 48  ? 3.827   -0.505  30.137  1.00 74.65  ?  47  ASP A N     1 
ATOM   394  C  CA    . ASP A 1 48  ? 3.445   -1.673  30.922  1.00 77.12  ?  47  ASP A CA    1 
ATOM   395  C  C     . ASP A 1 48  ? 4.017   -2.974  30.365  1.00 74.15  ?  47  ASP A C     1 
ATOM   396  O  O     . ASP A 1 48  ? 3.573   -4.056  30.764  1.00 74.12  ?  47  ASP A O     1 
ATOM   397  C  CB    . ASP A 1 48  ? 1.918   -1.764  31.041  1.00 79.97  ?  47  ASP A CB    1 
ATOM   398  C  CG    . ASP A 1 48  ? 1.218   -1.781  29.696  1.00 80.26  ?  47  ASP A CG    1 
ATOM   399  O  OD1   . ASP A 1 48  ? 1.896   -1.964  28.666  1.00 79.98  ?  47  ASP A OD1   1 
ATOM   400  O  OD2   . ASP A 1 48  ? -0.019  -1.608  29.672  1.00 81.33  -1 47  ASP A OD2   1 
ATOM   401  N  N     . ARG A 1 49  ? 4.989   -2.892  29.457  1.00 68.97  ?  48  ARG A N     1 
ATOM   402  C  CA    . ARG A 1 49  ? 5.732   -4.055  28.996  1.00 61.81  ?  48  ARG A CA    1 
ATOM   403  C  C     . ARG A 1 49  ? 7.086   -4.203  29.675  1.00 54.55  ?  48  ARG A C     1 
ATOM   404  O  O     . ARG A 1 49  ? 7.700   -5.270  29.568  1.00 50.97  ?  48  ARG A O     1 
ATOM   405  C  CB    . ARG A 1 49  ? 5.946   -3.988  27.480  1.00 62.39  ?  48  ARG A CB    1 
ATOM   406  C  CG    . ARG A 1 49  ? 4.906   -4.721  26.662  1.00 65.01  ?  48  ARG A CG    1 
ATOM   407  C  CD    . ARG A 1 49  ? 5.571   -5.772  25.791  1.00 66.15  ?  48  ARG A CD    1 
ATOM   408  N  NE    . ARG A 1 49  ? 4.733   -6.151  24.661  1.00 66.26  ?  48  ARG A NE    1 
ATOM   409  C  CZ    . ARG A 1 49  ? 5.090   -7.028  23.730  1.00 65.39  ?  48  ARG A CZ    1 
ATOM   410  N  NH1   . ARG A 1 49  ? 6.276   -7.621  23.796  1.00 64.76  1  48  ARG A NH1   1 
ATOM   411  N  NH2   . ARG A 1 49  ? 4.261   -7.311  22.733  1.00 64.49  ?  48  ARG A NH2   1 
ATOM   412  N  N     . GLY A 1 50  ? 7.563   -3.165  30.358  1.00 53.50  ?  49  GLY A N     1 
ATOM   413  C  CA    . GLY A 1 50  ? 8.865   -3.222  30.992  1.00 56.07  ?  49  GLY A CA    1 
ATOM   414  C  C     . GLY A 1 50  ? 10.016  -3.054  30.033  1.00 53.91  ?  49  GLY A C     1 
ATOM   415  O  O     . GLY A 1 50  ? 11.113  -3.558  30.293  1.00 52.48  ?  49  GLY A O     1 
ATOM   416  N  N     . GLU A 1 51  ? 9.798   -2.354  28.925  1.00 55.93  ?  50  GLU A N     1 
ATOM   417  C  CA    . GLU A 1 51  ? 10.805  -2.241  27.884  1.00 55.43  ?  50  GLU A CA    1 
ATOM   418  C  C     . GLU A 1 51  ? 10.544  -0.967  27.097  1.00 52.91  ?  50  GLU A C     1 
ATOM   419  O  O     . GLU A 1 51  ? 9.407   -0.497  27.015  1.00 51.77  ?  50  GLU A O     1 
ATOM   420  C  CB    . GLU A 1 51  ? 10.773  -3.470  26.970  1.00 58.91  ?  50  GLU A CB    1 
ATOM   421  C  CG    . GLU A 1 51  ? 11.870  -3.531  25.933  1.00 63.78  ?  50  GLU A CG    1 
ATOM   422  C  CD    . GLU A 1 51  ? 11.808  -4.807  25.124  1.00 66.45  ?  50  GLU A CD    1 
ATOM   423  O  OE1   . GLU A 1 51  ? 12.881  -5.352  24.791  1.00 68.53  ?  50  GLU A OE1   1 
ATOM   424  O  OE2   . GLU A 1 51  ? 10.682  -5.269  24.836  1.00 65.95  -1 50  GLU A OE2   1 
ATOM   425  N  N     . ALA A 1 52  ? 11.611  -0.402  26.540  1.00 51.40  ?  51  ALA A N     1 
ATOM   426  C  CA    . ALA A 1 52  ? 11.466  0.762   25.681  1.00 51.83  ?  51  ALA A CA    1 
ATOM   427  C  C     . ALA A 1 52  ? 10.699  0.386   24.421  1.00 47.42  ?  51  ALA A C     1 
ATOM   428  O  O     . ALA A 1 52  ? 10.826  -0.729  23.906  1.00 39.54  ?  51  ALA A O     1 
ATOM   429  C  CB    . ALA A 1 52  ? 12.834  1.335   25.314  1.00 53.05  ?  51  ALA A CB    1 
ATOM   430  N  N     . ALA A 1 53  ? 9.885   1.320   23.934  1.00 50.04  ?  52  ALA A N     1 
ATOM   431  C  CA    . ALA A 1 53  ? 9.123   1.073   22.724  1.00 48.22  ?  52  ALA A CA    1 
ATOM   432  C  C     . ALA A 1 53  ? 10.071  0.836   21.549  1.00 45.59  ?  52  ALA A C     1 
ATOM   433  O  O     . ALA A 1 53  ? 11.157  1.420   21.486  1.00 46.50  ?  52  ALA A O     1 
ATOM   434  C  CB    . ALA A 1 53  ? 8.195   2.248   22.421  1.00 50.13  ?  52  ALA A CB    1 
ATOM   435  N  N     . PRO A 1 54  ? 9.695   -0.031  20.614  1.00 41.73  ?  53  PRO A N     1 
ATOM   436  C  CA    . PRO A 1 54  ? 10.505  -0.195  19.406  1.00 41.35  ?  53  PRO A CA    1 
ATOM   437  C  C     . PRO A 1 54  ? 10.469  1.067   18.560  1.00 38.33  ?  53  PRO A C     1 
ATOM   438  O  O     . PRO A 1 54  ? 9.453   1.764   18.492  1.00 36.65  ?  53  PRO A O     1 
ATOM   439  C  CB    . PRO A 1 54  ? 9.836   -1.371  18.687  1.00 44.25  ?  53  PRO A CB    1 
ATOM   440  C  CG    . PRO A 1 54  ? 8.414   -1.315  19.148  1.00 43.93  ?  53  PRO A CG    1 
ATOM   441  C  CD    . PRO A 1 54  ? 8.484   -0.867  20.584  1.00 43.71  ?  53  PRO A CD    1 
ATOM   442  N  N     . THR A 1 55  ? 11.597  1.362   17.927  1.00 37.20  ?  54  THR A N     1 
ATOM   443  C  CA    . THR A 1 55  ? 11.675  2.485   17.008  1.00 35.40  ?  54  THR A CA    1 
ATOM   444  C  C     . THR A 1 55  ? 11.125  2.089   15.640  1.00 32.77  ?  54  THR A C     1 
ATOM   445  O  O     . THR A 1 55  ? 10.982  0.906   15.314  1.00 32.46  ?  54  THR A O     1 
ATOM   446  C  CB    . THR A 1 55  ? 13.118  2.960   16.873  1.00 36.60  ?  54  THR A CB    1 
ATOM   447  O  OG1   . THR A 1 55  ? 13.908  1.903   16.321  1.00 39.16  ?  54  THR A OG1   1 
ATOM   448  C  CG2   . THR A 1 55  ? 13.678  3.335   18.237  1.00 37.10  ?  54  THR A CG2   1 
ATOM   449  N  N     . PHE A 1 56  ? 10.813  3.095   14.830  1.00 34.78  ?  55  PHE A N     1 
ATOM   450  C  CA    . PHE A 1 56  ? 10.334  2.842   13.479  1.00 32.43  ?  55  PHE A CA    1 
ATOM   451  C  C     . PHE A 1 56  ? 10.925  3.869   12.527  1.00 33.83  ?  55  PHE A C     1 
ATOM   452  O  O     . PHE A 1 56  ? 11.314  4.970   12.926  1.00 34.76  ?  55  PHE A O     1 
ATOM   453  C  CB    . PHE A 1 56  ? 8.798   2.865   13.400  1.00 29.78  ?  55  PHE A CB    1 
ATOM   454  C  CG    . PHE A 1 56  ? 8.196   4.207   13.701  1.00 33.59  ?  55  PHE A CG    1 
ATOM   455  C  CD1   . PHE A 1 56  ? 8.059   5.161   12.706  1.00 30.37  ?  55  PHE A CD1   1 
ATOM   456  C  CD2   . PHE A 1 56  ? 7.767   4.515   14.983  1.00 39.91  ?  55  PHE A CD2   1 
ATOM   457  C  CE1   . PHE A 1 56  ? 7.517   6.395   12.980  1.00 34.81  ?  55  PHE A CE1   1 
ATOM   458  C  CE2   . PHE A 1 56  ? 7.220   5.750   15.261  1.00 41.57  ?  55  PHE A CE2   1 
ATOM   459  C  CZ    . PHE A 1 56  ? 7.098   6.692   14.257  1.00 38.44  ?  55  PHE A CZ    1 
ATOM   460  N  N     . THR A 1 57  ? 10.979  3.485   11.252  1.00 34.97  ?  56  THR A N     1 
ATOM   461  C  CA    . THR A 1 57  ? 11.399  4.369   10.170  1.00 33.63  ?  56  THR A CA    1 
ATOM   462  C  C     . THR A 1 57  ? 10.200  4.676   9.287   1.00 29.46  ?  56  THR A C     1 
ATOM   463  O  O     . THR A 1 57  ? 9.628   3.747   8.695   1.00 26.72  ?  56  THR A O     1 
ATOM   464  C  CB    . THR A 1 57  ? 12.514  3.732   9.342   1.00 35.31  ?  56  THR A CB    1 
ATOM   465  O  OG1   . THR A 1 57  ? 13.548  3.266   10.215  1.00 42.83  ?  56  THR A OG1   1 
ATOM   466  C  CG2   . THR A 1 57  ? 13.103  4.749   8.373   1.00 33.04  ?  56  THR A CG2   1 
ATOM   467  N  N     . PRO A 1 58  ? 9.767   5.931   9.193   1.00 28.79  ?  57  PRO A N     1 
ATOM   468  C  CA    . PRO A 1 58  ? 8.638   6.272   8.327   1.00 28.94  ?  57  PRO A CA    1 
ATOM   469  C  C     . PRO A 1 58  ? 9.082   6.581   6.903   1.00 29.98  ?  57  PRO A C     1 
ATOM   470  O  O     . PRO A 1 58  ? 10.227  6.949   6.640   1.00 28.17  ?  57  PRO A O     1 
ATOM   471  C  CB    . PRO A 1 58  ? 8.062   7.524   9.001   1.00 29.01  ?  57  PRO A CB    1 
ATOM   472  C  CG    . PRO A 1 58  ? 9.260   8.190   9.581   1.00 27.67  ?  57  PRO A CG    1 
ATOM   473  C  CD    . PRO A 1 58  ? 10.206  7.082   10.002  1.00 27.49  ?  57  PRO A CD    1 
ATOM   474  N  N     . PHE A 1 59  ? 8.143   6.402   5.974   1.00 27.36  ?  58  PHE A N     1 
ATOM   475  C  CA    . PHE A 1 59  ? 8.392   6.744   4.580   1.00 27.90  ?  58  PHE A CA    1 
ATOM   476  C  C     . PHE A 1 59  ? 7.076   7.089   3.896   1.00 25.60  ?  58  PHE A C     1 
ATOM   477  O  O     . PHE A 1 59  ? 6.027   6.516   4.206   1.00 25.17  ?  58  PHE A O     1 
ATOM   478  C  CB    . PHE A 1 59  ? 9.122   5.619   3.826   1.00 26.38  ?  58  PHE A CB    1 
ATOM   479  C  CG    . PHE A 1 59  ? 8.341   4.334   3.709   1.00 24.07  ?  58  PHE A CG    1 
ATOM   480  C  CD1   . PHE A 1 59  ? 8.380   3.386   4.727   1.00 22.45  ?  58  PHE A CD1   1 
ATOM   481  C  CD2   . PHE A 1 59  ? 7.604   4.056   2.566   1.00 22.69  ?  58  PHE A CD2   1 
ATOM   482  C  CE1   . PHE A 1 59  ? 7.678   2.198   4.619   1.00 21.09  ?  58  PHE A CE1   1 
ATOM   483  C  CE2   . PHE A 1 59  ? 6.894   2.863   2.448   1.00 23.38  ?  58  PHE A CE2   1 
ATOM   484  C  CZ    . PHE A 1 59  ? 6.931   1.934   3.479   1.00 20.95  ?  58  PHE A CZ    1 
ATOM   485  N  N     . ASN A 1 60  ? 7.146   8.050   2.976   1.00 24.64  ?  59  ASN A N     1 
ATOM   486  C  CA    . ASN A 1 60  ? 5.966   8.488   2.243   1.00 22.85  ?  59  ASN A CA    1 
ATOM   487  C  C     . ASN A 1 60  ? 5.421   7.369   1.367   1.00 21.26  ?  59  ASN A C     1 
ATOM   488  O  O     . ASN A 1 60  ? 6.180   6.654   0.706   1.00 19.48  ?  59  ASN A O     1 
ATOM   489  C  CB    . ASN A 1 60  ? 6.301   9.702   1.375   1.00 23.37  ?  59  ASN A CB    1 
ATOM   490  C  CG    . ASN A 1 60  ? 6.662   10.927  2.195   1.00 23.95  ?  59  ASN A CG    1 
ATOM   491  O  OD1   . ASN A 1 60  ? 6.263   11.057  3.357   1.00 23.59  ?  59  ASN A OD1   1 
ATOM   492  N  ND2   . ASN A 1 60  ? 7.409   11.838  1.589   1.00 20.94  ?  59  ASN A ND2   1 
ATOM   493  N  N     . GLN A 1 61  ? 4.093   7.232   1.354   1.00 22.38  ?  60  GLN A N     1 
ATOM   494  C  CA    . GLN A 1 61  ? 3.397   6.271   0.509   1.00 19.27  ?  60  GLN A CA    1 
ATOM   495  C  C     . GLN A 1 61  ? 2.295   6.964   -0.283  1.00 19.78  ?  60  GLN A C     1 
ATOM   496  O  O     . GLN A 1 61  ? 1.942   8.119   -0.032  1.00 18.99  ?  60  GLN A O     1 
ATOM   497  C  CB    . GLN A 1 61  ? 2.791   5.128   1.335   1.00 17.37  ?  60  GLN A CB    1 
ATOM   498  C  CG    . GLN A 1 61  ? 3.817   4.159   1.885   1.00 22.09  ?  60  GLN A CG    1 
ATOM   499  C  CD    . GLN A 1 61  ? 3.238   2.783   2.130   1.00 23.43  ?  60  GLN A CD    1 
ATOM   500  O  OE1   . GLN A 1 61  ? 3.513   2.159   3.149   1.00 26.70  ?  60  GLN A OE1   1 
ATOM   501  N  NE2   . GLN A 1 61  ? 2.441   2.295   1.186   1.00 23.49  ?  60  GLN A NE2   1 
ATOM   502  N  N     . GLY A 1 62  ? 1.754   6.241   -1.262  1.00 18.53  ?  61  GLY A N     1 
ATOM   503  C  CA    . GLY A 1 62  ? 0.550   6.699   -1.929  1.00 17.54  ?  61  GLY A CA    1 
ATOM   504  C  C     . GLY A 1 62  ? 0.721   7.890   -2.867  1.00 16.23  ?  61  GLY A C     1 
ATOM   505  O  O     . GLY A 1 62  ? 1.821   8.280   -3.278  1.00 16.50  ?  61  GLY A O     1 
ATOM   506  N  N     . SER A 1 63  ? -0.434  8.468   -3.207  1.00 15.66  ?  62  SER A N     1 
ATOM   507  C  CA    . SER A 1 63  ? -0.492  9.466   -4.268  1.00 17.84  ?  62  SER A CA    1 
ATOM   508  C  C     . SER A 1 63  ? 0.255   10.734  -3.893  1.00 17.99  ?  62  SER A C     1 
ATOM   509  O  O     . SER A 1 63  ? 0.800   11.410  -4.772  1.00 19.27  ?  62  SER A O     1 
ATOM   510  C  CB    . SER A 1 63  ? -1.945  9.793   -4.605  1.00 15.09  ?  62  SER A CB    1 
ATOM   511  O  OG    . SER A 1 63  ? -2.611  10.346  -3.486  1.00 19.53  ?  62  SER A OG    1 
ATOM   512  N  N     . TYR A 1 64  ? 0.282   11.081  -2.605  1.00 17.93  ?  63  TYR A N     1 
ATOM   513  C  CA    . TYR A 1 64  ? 0.999   12.281  -2.199  1.00 20.35  ?  63  TYR A CA    1 
ATOM   514  C  C     . TYR A 1 64  ? 2.507   12.075  -2.271  1.00 20.54  ?  63  TYR A C     1 
ATOM   515  O  O     . TYR A 1 64  ? 3.257   13.051  -2.382  1.00 22.86  ?  63  TYR A O     1 
ATOM   516  C  CB    . TYR A 1 64  ? 0.563   12.703  -0.791  1.00 24.84  ?  63  TYR A CB    1 
ATOM   517  C  CG    . TYR A 1 64  ? -0.942  12.907  -0.610  1.00 28.16  ?  63  TYR A CG    1 
ATOM   518  C  CD1   . TYR A 1 64  ? -1.818  12.918  -1.695  1.00 31.34  ?  63  TYR A CD1   1 
ATOM   519  C  CD2   . TYR A 1 64  ? -1.481  13.093  0.656   1.00 34.21  ?  63  TYR A CD2   1 
ATOM   520  C  CE1   . TYR A 1 64  ? -3.185  13.108  -1.518  1.00 31.39  ?  63  TYR A CE1   1 
ATOM   521  C  CE2   . TYR A 1 64  ? -2.841  13.288  0.841   1.00 36.13  ?  63  TYR A CE2   1 
ATOM   522  C  CZ    . TYR A 1 64  ? -3.688  13.291  -0.246  1.00 35.13  ?  63  TYR A CZ    1 
ATOM   523  O  OH    . TYR A 1 64  ? -5.040  13.485  -0.045  1.00 36.26  ?  63  TYR A OH    1 
ATOM   524  N  N     . ALA A 1 65  ? 2.963   10.826  -2.231  1.00 17.18  ?  64  ALA A N     1 
ATOM   525  C  CA    . ALA A 1 65  ? 4.364   10.534  -2.506  1.00 17.85  ?  64  ALA A CA    1 
ATOM   526  C  C     . ALA A 1 65  ? 4.639   10.460  -4.001  1.00 20.03  ?  64  ALA A C     1 
ATOM   527  O  O     . ALA A 1 65  ? 5.726   10.839  -4.451  1.00 22.22  ?  64  ALA A O     1 
ATOM   528  C  CB    . ALA A 1 65  ? 4.762   9.221   -1.835  1.00 16.37  ?  64  ALA A CB    1 
ATOM   529  N  N     . MET A 1 66  ? 3.675   9.984   -4.781  1.00 20.75  ?  65  MET A N     1 
ATOM   530  C  CA    . MET A 1 66  ? 3.874   9.773   -6.207  1.00 19.19  ?  65  MET A CA    1 
ATOM   531  C  C     . MET A 1 66  ? 3.482   10.972  -7.060  1.00 18.00  ?  65  MET A C     1 
ATOM   532  O  O     . MET A 1 66  ? 3.610   10.898  -8.288  1.00 16.76  ?  65  MET A O     1 
ATOM   533  C  CB    . MET A 1 66  ? 3.088   8.542   -6.665  1.00 18.03  ?  65  MET A CB    1 
ATOM   534  C  CG    . MET A 1 66  ? 3.587   7.259   -6.040  1.00 17.47  ?  65  MET A CG    1 
ATOM   535  S  SD    . MET A 1 66  ? 2.743   5.789   -6.652  1.00 19.17  ?  65  MET A SD    1 
ATOM   536  C  CE    . MET A 1 66  ? 1.299   5.767   -5.595  1.00 20.16  ?  65  MET A CE    1 
ATOM   537  N  N     . ASN A 1 67  ? 3.015   12.066  -6.447  1.00 18.19  ?  66  ASN A N     1 
ATOM   538  C  CA    . ASN A 1 67  ? 2.576   13.253  -7.187  1.00 18.38  ?  66  ASN A CA    1 
ATOM   539  C  C     . ASN A 1 67  ? 1.417   12.914  -8.126  1.00 19.72  ?  66  ASN A C     1 
ATOM   540  O  O     . ASN A 1 67  ? 1.349   13.382  -9.265  1.00 16.64  ?  66  ASN A O     1 
ATOM   541  C  CB    . ASN A 1 67  ? 3.739   13.888  -7.952  1.00 19.00  ?  66  ASN A CB    1 
ATOM   542  C  CG    . ASN A 1 67  ? 3.451   15.301  -8.384  1.00 18.86  ?  66  ASN A CG    1 
ATOM   543  O  OD1   . ASN A 1 67  ? 2.550   15.951  -7.859  1.00 22.24  ?  66  ASN A OD1   1 
ATOM   544  N  ND2   . ASN A 1 67  ? 4.222   15.791  -9.344  1.00 18.19  ?  66  ASN A ND2   1 
ATOM   545  N  N     . THR A 1 68  ? 0.499   12.080  -7.637  1.00 17.55  ?  67  THR A N     1 
ATOM   546  C  CA    . THR A 1 68  ? -0.728  11.741  -8.348  1.00 19.73  ?  67  THR A CA    1 
ATOM   547  C  C     . THR A 1 68  ? -1.967  12.104  -7.538  1.00 18.42  ?  67  THR A C     1 
ATOM   548  O  O     . THR A 1 68  ? -3.059  11.593  -7.812  1.00 19.56  ?  67  THR A O     1 
ATOM   549  C  CB    . THR A 1 68  ? -0.742  10.251  -8.684  1.00 16.44  ?  67  THR A CB    1 
ATOM   550  O  OG1   . THR A 1 68  ? -0.525  9.503   -7.479  1.00 17.36  ?  67  THR A OG1   1 
ATOM   551  C  CG2   . THR A 1 68  ? 0.371   9.920   -9.690  1.00 15.32  ?  67  THR A CG2   1 
ATOM   552  N  N     . GLY A 1 69  ? -1.819  12.959  -6.531  1.00 17.56  ?  68  GLY A N     1 
ATOM   553  C  CA    . GLY A 1 69  ? -2.929  13.246  -5.644  1.00 18.90  ?  68  GLY A CA    1 
ATOM   554  C  C     . GLY A 1 69  ? -3.882  14.272  -6.227  1.00 18.70  ?  68  GLY A C     1 
ATOM   555  O  O     . GLY A 1 69  ? -3.500  15.134  -7.018  1.00 17.18  ?  68  GLY A O     1 
ATOM   556  N  N     . VAL A 1 70  ? -5.147  14.168  -5.817  1.00 18.74  ?  69  VAL A N     1 
ATOM   557  C  CA    . VAL A 1 70  ? -6.197  15.086  -6.239  1.00 16.30  ?  69  VAL A CA    1 
ATOM   558  C  C     . VAL A 1 70  ? -6.850  15.680  -5.003  1.00 17.80  ?  69  VAL A C     1 
ATOM   559  O  O     . VAL A 1 70  ? -6.861  15.074  -3.927  1.00 17.92  ?  69  VAL A O     1 
ATOM   560  C  CB    . VAL A 1 70  ? -7.267  14.408  -7.129  1.00 17.80  ?  69  VAL A CB    1 
ATOM   561  C  CG1   . VAL A 1 70  ? -6.731  14.178  -8.535  1.00 17.06  ?  69  VAL A CG1   1 
ATOM   562  C  CG2   . VAL A 1 70  ? -7.747  13.105  -6.495  1.00 17.44  ?  69  VAL A CG2   1 
ATOM   563  N  N     . LYS A 1 71  ? -7.393  16.880  -5.159  1.00 17.55  ?  70  LYS A N     1 
ATOM   564  C  CA    . LYS A 1 71  ? -8.189  17.446  -4.088  1.00 19.53  ?  70  LYS A CA    1 
ATOM   565  C  C     . LYS A 1 71  ? -9.488  16.655  -3.950  1.00 24.08  ?  70  LYS A C     1 
ATOM   566  O  O     . LYS A 1 71  ? -10.073 16.237  -4.953  1.00 24.84  ?  70  LYS A O     1 
ATOM   567  C  CB    . LYS A 1 71  ? -8.498  18.917  -4.365  1.00 21.87  ?  70  LYS A CB    1 
ATOM   568  C  CG    . LYS A 1 71  ? -7.259  19.813  -4.384  1.00 24.12  ?  70  LYS A CG    1 
ATOM   569  C  CD    . LYS A 1 71  ? -7.627  21.269  -4.641  1.00 25.22  ?  70  LYS A CD    1 
ATOM   570  C  CE    . LYS A 1 71  ? -6.477  22.186  -4.279  1.00 30.03  ?  70  LYS A CE    1 
ATOM   571  N  NZ    . LYS A 1 71  ? -6.660  23.542  -4.864  1.00 36.94  1  70  LYS A NZ    1 
ATOM   572  N  N     . PRO A 1 72  ? -9.952  16.414  -2.732  1.00 27.45  ?  71  PRO A N     1 
ATOM   573  C  CA    . PRO A 1 72  ? -11.261 15.777  -2.569  1.00 31.10  ?  71  PRO A CA    1 
ATOM   574  C  C     . PRO A 1 72  ? -12.378 16.704  -3.023  1.00 30.68  ?  71  PRO A C     1 
ATOM   575  O  O     . PRO A 1 72  ? -12.236 17.929  -3.038  1.00 29.88  ?  71  PRO A O     1 
ATOM   576  C  CB    . PRO A 1 72  ? -11.340 15.511  -1.064  1.00 34.72  ?  71  PRO A CB    1 
ATOM   577  C  CG    . PRO A 1 72  ? -10.445 16.549  -0.463  1.00 35.16  ?  71  PRO A CG    1 
ATOM   578  C  CD    . PRO A 1 72  ? -9.319  16.731  -1.441  1.00 27.99  ?  71  PRO A CD    1 
ATOM   579  N  N     . LEU A 1 73  ? -13.494 16.102  -3.410  1.00 27.17  ?  72  LEU A N     1 
ATOM   580  C  CA    . LEU A 1 73  ? -14.701 16.880  -3.610  1.00 27.59  ?  72  LEU A CA    1 
ATOM   581  C  C     . LEU A 1 73  ? -15.167 17.452  -2.274  1.00 31.84  ?  72  LEU A C     1 
ATOM   582  O  O     . LEU A 1 73  ? -14.734 17.022  -1.200  1.00 33.34  ?  72  LEU A O     1 
ATOM   583  C  CB    . LEU A 1 73  ? -15.795 16.022  -4.239  1.00 27.82  ?  72  LEU A CB    1 
ATOM   584  C  CG    . LEU A 1 73  ? -15.555 15.507  -5.661  1.00 33.54  ?  72  LEU A CG    1 
ATOM   585  C  CD1   . LEU A 1 73  ? -16.720 14.630  -6.084  1.00 36.41  ?  72  LEU A CD1   1 
ATOM   586  C  CD2   . LEU A 1 73  ? -15.372 16.660  -6.638  1.00 34.42  ?  72  LEU A CD2   1 
ATOM   587  N  N     . GLU A 1 74  ? -16.047 18.449  -2.348  1.00 40.17  ?  73  GLU A N     1 
ATOM   588  C  CA    . GLU A 1 74  ? -16.575 19.062  -1.133  1.00 44.85  ?  73  GLU A CA    1 
ATOM   589  C  C     . GLU A 1 74  ? -17.224 18.002  -0.252  1.00 43.37  ?  73  GLU A C     1 
ATOM   590  O  O     . GLU A 1 74  ? -18.060 17.219  -0.712  1.00 43.04  ?  73  GLU A O     1 
ATOM   591  C  CB    . GLU A 1 74  ? -17.581 20.160  -1.485  1.00 53.98  ?  73  GLU A CB    1 
ATOM   592  C  CG    . GLU A 1 74  ? -18.102 20.939  -0.280  1.00 63.70  ?  73  GLU A CG    1 
ATOM   593  C  CD    . GLU A 1 74  ? -19.048 22.063  -0.671  1.00 69.63  ?  73  GLU A CD    1 
ATOM   594  O  OE1   . GLU A 1 74  ? -19.369 22.185  -1.874  1.00 69.73  ?  73  GLU A OE1   1 
ATOM   595  O  OE2   . GLU A 1 74  ? -19.468 22.827  0.226   1.00 72.79  -1 73  GLU A OE2   1 
ATOM   596  N  N     . GLY A 1 75  ? -16.816 17.962  1.015   1.00 44.33  ?  74  GLY A N     1 
ATOM   597  C  CA    . GLY A 1 75  ? -17.271 16.943  1.933   1.00 43.40  ?  74  GLY A CA    1 
ATOM   598  C  C     . GLY A 1 75  ? -16.385 15.718  2.019   1.00 45.69  ?  74  GLY A C     1 
ATOM   599  O  O     . GLY A 1 75  ? -16.582 14.895  2.924   1.00 48.34  ?  74  GLY A O     1 
ATOM   600  N  N     . GLY A 1 76  ? -15.419 15.566  1.108   1.00 41.07  ?  75  GLY A N     1 
ATOM   601  C  CA    . GLY A 1 76  ? -14.490 14.457  1.156   1.00 39.80  ?  75  GLY A CA    1 
ATOM   602  C  C     . GLY A 1 76  ? -13.295 14.743  2.050   1.00 37.60  ?  75  GLY A C     1 
ATOM   603  O  O     . GLY A 1 76  ? -13.127 15.835  2.591   1.00 38.12  ?  75  GLY A O     1 
ATOM   604  N  N     . GLU A 1 77  ? -12.443 13.727  2.192   1.00 35.44  ?  76  GLU A N     1 
ATOM   605  C  CA    . GLU A 1 77  ? -11.295 13.789  3.083   1.00 38.17  ?  76  GLU A CA    1 
ATOM   606  C  C     . GLU A 1 77  ? -9.994  13.597  2.314   1.00 35.38  ?  76  GLU A C     1 
ATOM   607  O  O     . GLU A 1 77  ? -9.946  12.881  1.308   1.00 30.55  ?  76  GLU A O     1 
ATOM   608  C  CB    . GLU A 1 77  ? -11.380 12.719  4.185   1.00 45.12  ?  76  GLU A CB    1 
ATOM   609  C  CG    . GLU A 1 77  ? -12.554 12.864  5.137   1.00 50.64  ?  76  GLU A CG    1 
ATOM   610  C  CD    . GLU A 1 77  ? -12.548 11.806  6.231   1.00 54.26  ?  76  GLU A CD    1 
ATOM   611  O  OE1   . GLU A 1 77  ? -11.520 11.110  6.385   1.00 53.23  ?  76  GLU A OE1   1 
ATOM   612  O  OE2   . GLU A 1 77  ? -13.571 11.670  6.937   1.00 56.69  -1 76  GLU A OE2   1 
ATOM   613  N  N     . TYR A 1 78  ? -8.935  14.235  2.811   1.00 36.23  ?  77  TYR A N     1 
ATOM   614  C  CA    . TYR A 1 78  ? -7.591  13.917  2.358   1.00 36.88  ?  77  TYR A CA    1 
ATOM   615  C  C     . TYR A 1 78  ? -7.182  12.540  2.867   1.00 33.08  ?  77  TYR A C     1 
ATOM   616  O  O     . TYR A 1 78  ? -7.656  12.065  3.905   1.00 31.90  ?  77  TYR A O     1 
ATOM   617  C  CB    . TYR A 1 78  ? -6.578  14.960  2.838   1.00 41.57  ?  77  TYR A CB    1 
ATOM   618  C  CG    . TYR A 1 78  ? -6.807  16.354  2.305   1.00 46.02  ?  77  TYR A CG    1 
ATOM   619  C  CD1   . TYR A 1 78  ? -7.669  17.233  2.947   1.00 48.28  ?  77  TYR A CD1   1 
ATOM   620  C  CD2   . TYR A 1 78  ? -6.153  16.794  1.163   1.00 49.26  ?  77  TYR A CD2   1 
ATOM   621  C  CE1   . TYR A 1 78  ? -7.881  18.513  2.459   1.00 51.33  ?  77  TYR A CE1   1 
ATOM   622  C  CE2   . TYR A 1 78  ? -6.355  18.069  0.668   1.00 53.20  ?  77  TYR A CE2   1 
ATOM   623  C  CZ    . TYR A 1 78  ? -7.220  18.925  1.320   1.00 56.72  ?  77  TYR A CZ    1 
ATOM   624  O  OH    . TYR A 1 78  ? -7.423  20.196  0.828   1.00 62.53  ?  77  TYR A OH    1 
ATOM   625  N  N     . ASP A 1 79  ? -6.274  11.909  2.128   1.00 30.62  ?  78  ASP A N     1 
ATOM   626  C  CA    . ASP A 1 79  ? -5.853  10.532  2.368   1.00 29.42  ?  78  ASP A CA    1 
ATOM   627  C  C     . ASP A 1 79  ? -4.331  10.546  2.478   1.00 29.03  ?  78  ASP A C     1 
ATOM   628  O  O     . ASP A 1 79  ? -3.635  10.480  1.463   1.00 28.03  ?  78  ASP A O     1 
ATOM   629  C  CB    . ASP A 1 79  ? -6.348  9.637   1.236   1.00 32.15  ?  78  ASP A CB    1 
ATOM   630  C  CG    . ASP A 1 79  ? -5.987  8.187   1.432   1.00 35.77  ?  78  ASP A CG    1 
ATOM   631  O  OD1   . ASP A 1 79  ? -6.521  7.560   2.375   1.00 40.73  ?  78  ASP A OD1   1 
ATOM   632  O  OD2   . ASP A 1 79  ? -5.180  7.670   0.632   1.00 28.87  -1 78  ASP A OD2   1 
ATOM   633  N  N     . ILE A 1 80  ? -3.814  10.647  3.699   1.00 26.84  ?  79  ILE A N     1 
ATOM   634  C  CA    . ILE A 1 80  ? -2.377  10.770  3.921   1.00 27.15  ?  79  ILE A CA    1 
ATOM   635  C  C     . ILE A 1 80  ? -1.820  9.368   4.151   1.00 24.87  ?  79  ILE A C     1 
ATOM   636  O  O     . ILE A 1 80  ? -2.050  8.761   5.198   1.00 25.64  ?  79  ILE A O     1 
ATOM   637  C  CB    . ILE A 1 80  ? -2.071  11.704  5.097   1.00 34.27  ?  79  ILE A CB    1 
ATOM   638  C  CG1   . ILE A 1 80  ? -2.452  13.141  4.735   1.00 38.16  ?  79  ILE A CG1   1 
ATOM   639  C  CG2   . ILE A 1 80  ? -0.603  11.632  5.494   1.00 35.35  ?  79  ILE A CG2   1 
ATOM   640  C  CD1   . ILE A 1 80  ? -2.147  14.144  5.828   1.00 41.69  ?  79  ILE A CD1   1 
ATOM   641  N  N     . ASP A 1 81  ? -1.097  8.847   3.162   1.00 23.45  ?  80  ASP A N     1 
ATOM   642  C  CA    . ASP A 1 81  ? -0.582  7.484   3.198   1.00 25.84  ?  80  ASP A CA    1 
ATOM   643  C  C     . ASP A 1 81  ? 0.874   7.509   3.648   1.00 26.58  ?  80  ASP A C     1 
ATOM   644  O  O     . ASP A 1 81  ? 1.701   8.205   3.045   1.00 25.52  ?  80  ASP A O     1 
ATOM   645  C  CB    . ASP A 1 81  ? -0.704  6.822   1.825   1.00 21.97  ?  80  ASP A CB    1 
ATOM   646  C  CG    . ASP A 1 81  ? -2.141  6.750   1.331   1.00 22.22  ?  80  ASP A CG    1 
ATOM   647  O  OD1   . ASP A 1 81  ? -3.024  6.296   2.090   1.00 25.70  ?  80  ASP A OD1   1 
ATOM   648  O  OD2   . ASP A 1 81  ? -2.389  7.159   0.177   1.00 23.39  -1 80  ASP A OD2   1 
ATOM   649  N  N     . VAL A 1 82  ? 1.186   6.755   4.705   1.00 24.30  ?  81  VAL A N     1 
ATOM   650  C  CA    . VAL A 1 82  ? 2.554   6.646   5.201   1.00 23.39  ?  81  VAL A CA    1 
ATOM   651  C  C     . VAL A 1 82  ? 2.822   5.198   5.595   1.00 24.84  ?  81  VAL A C     1 
ATOM   652  O  O     . VAL A 1 82  ? 1.919   4.470   6.017   1.00 24.42  ?  81  VAL A O     1 
ATOM   653  C  CB    . VAL A 1 82  ? 2.825   7.583   6.403   1.00 26.07  ?  81  VAL A CB    1 
ATOM   654  C  CG1   . VAL A 1 82  ? 2.646   9.034   6.014   1.00 27.46  ?  81  VAL A CG1   1 
ATOM   655  C  CG2   . VAL A 1 82  ? 1.920   7.232   7.574   1.00 29.67  ?  81  VAL A CG2   1 
ATOM   656  N  N     . GLY A 1 83  ? 4.071   4.777   5.443   1.00 24.67  ?  82  GLY A N     1 
ATOM   657  C  CA    . GLY A 1 83  ? 4.520   3.474   5.909   1.00 23.82  ?  82  GLY A CA    1 
ATOM   658  C  C     . GLY A 1 83  ? 5.441   3.675   7.102   1.00 25.96  ?  82  GLY A C     1 
ATOM   659  O  O     . GLY A 1 83  ? 6.178   4.657   7.158   1.00 24.11  ?  82  GLY A O     1 
ATOM   660  N  N     . ILE A 1 84  ? 5.377   2.755   8.058   1.00 27.37  ?  83  ILE A N     1 
ATOM   661  C  CA    . ILE A 1 84  ? 6.292   2.768   9.194   1.00 30.50  ?  83  ILE A CA    1 
ATOM   662  C  C     . ILE A 1 84  ? 6.879   1.370   9.348   1.00 28.29  ?  83  ILE A C     1 
ATOM   663  O  O     . ILE A 1 84  ? 6.139   0.386   9.493   1.00 29.31  ?  83  ILE A O     1 
ATOM   664  C  CB    . ILE A 1 84  ? 5.617   3.237   10.496  1.00 29.08  ?  83  ILE A CB    1 
ATOM   665  C  CG1   . ILE A 1 84  ? 4.341   2.453   10.784  1.00 30.53  ?  83  ILE A CG1   1 
ATOM   666  C  CG2   . ILE A 1 84  ? 5.309   4.732   10.437  1.00 27.98  ?  83  ILE A CG2   1 
ATOM   667  C  CD1   . ILE A 1 84  ? 3.809   2.687   12.192  1.00 29.61  ?  83  ILE A CD1   1 
ATOM   668  N  N     . ILE A 1 85  ? 8.202   1.280   9.279   1.00 26.38  ?  84  ILE A N     1 
ATOM   669  C  CA    . ILE A 1 85  ? 8.922   0.025   9.436   1.00 24.10  ?  84  ILE A CA    1 
ATOM   670  C  C     . ILE A 1 85  ? 9.367   -0.048  10.889  1.00 24.71  ?  84  ILE A C     1 
ATOM   671  O  O     . ILE A 1 85  ? 10.283  0.672   11.297  1.00 27.06  ?  84  ILE A O     1 
ATOM   672  C  CB    . ILE A 1 85  ? 10.124  -0.063  8.489   1.00 26.42  ?  84  ILE A CB    1 
ATOM   673  C  CG1   . ILE A 1 85  ? 9.712   0.265   7.049   1.00 26.18  ?  84  ILE A CG1   1 
ATOM   674  C  CG2   . ILE A 1 85  ? 10.765  -1.441  8.583   1.00 27.49  ?  84  ILE A CG2   1 
ATOM   675  C  CD1   . ILE A 1 85  ? 10.890  0.544   6.139   1.00 23.72  ?  84  ILE A CD1   1 
ATOM   676  N  N     . LEU A 1 86  ? 8.708   -0.890  11.678  1.00 27.30  ?  85  LEU A N     1 
ATOM   677  C  CA    . LEU A 1 86  ? 9.094   -1.057  13.067  1.00 32.85  ?  85  LEU A CA    1 
ATOM   678  C  C     . LEU A 1 86  ? 10.349  -1.915  13.163  1.00 33.57  ?  85  LEU A C     1 
ATOM   679  O  O     . LEU A 1 86  ? 10.583  -2.815  12.349  1.00 32.07  ?  85  LEU A O     1 
ATOM   680  C  CB    . LEU A 1 86  ? 7.959   -1.681  13.881  1.00 38.39  ?  85  LEU A CB    1 
ATOM   681  C  CG    . LEU A 1 86  ? 6.893   -0.705  14.391  1.00 46.16  ?  85  LEU A CG    1 
ATOM   682  C  CD1   . LEU A 1 86  ? 6.000   -0.200  13.256  1.00 48.37  ?  85  LEU A CD1   1 
ATOM   683  C  CD2   . LEU A 1 86  ? 6.057   -1.332  15.497  1.00 47.96  ?  85  LEU A CD2   1 
ATOM   684  N  N     . ASN A 1 87  ? 11.170  -1.610  14.166  1.00 33.38  ?  86  ASN A N     1 
ATOM   685  C  CA    . ASN A 1 87  ? 12.431  -2.312  14.393  1.00 32.88  ?  86  ASN A CA    1 
ATOM   686  C  C     . ASN A 1 87  ? 12.165  -3.628  15.133  1.00 32.95  ?  86  ASN A C     1 
ATOM   687  O  O     . ASN A 1 87  ? 12.581  -3.835  16.272  1.00 32.05  ?  86  ASN A O     1 
ATOM   688  C  CB    . ASN A 1 87  ? 13.388  -1.406  15.162  1.00 38.56  ?  86  ASN A CB    1 
ATOM   689  C  CG    . ASN A 1 87  ? 14.784  -1.993  15.309  1.00 42.23  ?  86  ASN A CG    1 
ATOM   690  O  OD1   . ASN A 1 87  ? 15.246  -2.762  14.466  1.00 42.56  ?  86  ASN A OD1   1 
ATOM   691  N  ND2   . ASN A 1 87  ? 15.464  -1.622  16.388  1.00 43.91  ?  86  ASN A ND2   1 
ATOM   692  N  N     . ILE A 1 88  ? 11.435  -4.524  14.459  1.00 31.46  ?  87  ILE A N     1 
ATOM   693  C  CA    . ILE A 1 88  ? 11.017  -5.795  15.041  1.00 31.83  ?  87  ILE A CA    1 
ATOM   694  C  C     . ILE A 1 88  ? 11.198  -6.909  14.018  1.00 31.78  ?  87  ILE A C     1 
ATOM   695  O  O     . ILE A 1 88  ? 11.237  -6.677  12.807  1.00 31.41  ?  87  ILE A O     1 
ATOM   696  C  CB    . ILE A 1 88  ? 9.549   -5.773  15.525  1.00 31.78  ?  87  ILE A CB    1 
ATOM   697  C  CG1   . ILE A 1 88  ? 8.607   -5.586  14.335  1.00 32.35  ?  87  ILE A CG1   1 
ATOM   698  C  CG2   . ILE A 1 88  ? 9.331   -4.690  16.573  1.00 35.69  ?  87  ILE A CG2   1 
ATOM   699  C  CD1   . ILE A 1 88  ? 7.161   -5.429  14.726  1.00 34.75  ?  87  ILE A CD1   1 
ATOM   700  N  N     . ALA A 1 89  ? 11.307  -8.133  14.528  1.00 32.15  ?  88  ALA A N     1 
ATOM   701  C  CA    . ALA A 1 89  ? 11.370  -9.328  13.699  1.00 32.27  ?  88  ALA A CA    1 
ATOM   702  C  C     . ALA A 1 89  ? 9.963   -9.862  13.473  1.00 31.60  ?  88  ALA A C     1 
ATOM   703  O  O     . ALA A 1 89  ? 9.221   -10.084 14.435  1.00 33.90  ?  88  ALA A O     1 
ATOM   704  C  CB    . ALA A 1 89  ? 12.237  -10.399 14.361  1.00 33.98  ?  88  ALA A CB    1 
ATOM   705  N  N     . LYS A 1 90  ? 9.605   -10.088 12.207  1.00 29.39  ?  89  LYS A N     1 
ATOM   706  C  CA    . LYS A 1 90  ? 8.221   -10.435 11.895  1.00 32.82  ?  89  LYS A CA    1 
ATOM   707  C  C     . LYS A 1 90  ? 7.814   -11.767 12.518  1.00 31.95  ?  89  LYS A C     1 
ATOM   708  O  O     . LYS A 1 90  ? 6.657   -11.933 12.924  1.00 30.16  ?  89  LYS A O     1 
ATOM   709  C  CB    . LYS A 1 90  ? 8.001   -10.457 10.376  1.00 32.77  ?  89  LYS A CB    1 
ATOM   710  C  CG    . LYS A 1 90  ? 8.622   -11.631 9.627   1.00 34.66  ?  89  LYS A CG    1 
ATOM   711  C  CD    . LYS A 1 90  ? 8.371   -11.518 8.122   1.00 34.42  ?  89  LYS A CD    1 
ATOM   712  C  CE    . LYS A 1 90  ? 8.934   -12.712 7.368   1.00 36.36  ?  89  LYS A CE    1 
ATOM   713  N  NZ    . LYS A 1 90  ? 8.398   -14.003 7.899   1.00 38.24  1  89  LYS A NZ    1 
ATOM   714  N  N     . ASP A 1 91  ? 8.742   -12.719 12.619  1.00 32.24  ?  90  ASP A N     1 
ATOM   715  C  CA    . ASP A 1 91  ? 8.405   -14.019 13.186  1.00 34.62  ?  90  ASP A CA    1 
ATOM   716  C  C     . ASP A 1 91  ? 8.227   -13.977 14.696  1.00 38.59  ?  90  ASP A C     1 
ATOM   717  O  O     . ASP A 1 91  ? 7.680   -14.928 15.264  1.00 41.84  ?  90  ASP A O     1 
ATOM   718  C  CB    . ASP A 1 91  ? 9.477   -15.047 12.828  1.00 37.50  ?  90  ASP A CB    1 
ATOM   719  C  CG    . ASP A 1 91  ? 9.533   -15.336 11.345  1.00 41.75  ?  90  ASP A CG    1 
ATOM   720  O  OD1   . ASP A 1 91  ? 8.508   -15.143 10.656  1.00 42.98  ?  90  ASP A OD1   1 
ATOM   721  O  OD2   . ASP A 1 91  ? 10.604  -15.759 10.868  1.00 44.42  -1 90  ASP A OD2   1 
ATOM   722  N  N     . ASP A 1 92  ? 8.675   -12.912 15.356  1.00 37.68  ?  91  ASP A N     1 
ATOM   723  C  CA    . ASP A 1 92  ? 8.527   -12.780 16.797  1.00 40.30  ?  91  ASP A CA    1 
ATOM   724  C  C     . ASP A 1 92  ? 7.198   -12.168 17.207  1.00 41.49  ?  91  ASP A C     1 
ATOM   725  O  O     . ASP A 1 92  ? 6.919   -12.093 18.408  1.00 45.83  ?  91  ASP A O     1 
ATOM   726  C  CB    . ASP A 1 92  ? 9.666   -11.929 17.369  1.00 43.49  ?  91  ASP A CB    1 
ATOM   727  C  CG    . ASP A 1 92  ? 11.003  -12.637 17.326  1.00 45.43  ?  91  ASP A CG    1 
ATOM   728  O  OD1   . ASP A 1 92  ? 11.020  -13.858 17.078  1.00 45.38  ?  91  ASP A OD1   1 
ATOM   729  O  OD2   . ASP A 1 92  ? 12.037  -11.970 17.542  1.00 47.05  -1 91  ASP A OD2   1 
ATOM   730  N  N     . HIS A 1 93  ? 6.374   -11.728 16.256  1.00 37.24  ?  92  HIS A N     1 
ATOM   731  C  CA    . HIS A 1 93  ? 5.180   -10.971 16.600  1.00 35.06  ?  92  HIS A CA    1 
ATOM   732  C  C     . HIS A 1 93  ? 4.053   -11.284 15.628  1.00 35.43  ?  92  HIS A C     1 
ATOM   733  O  O     . HIS A 1 93  ? 4.283   -11.624 14.463  1.00 34.86  ?  92  HIS A O     1 
ATOM   734  C  CB    . HIS A 1 93  ? 5.449   -9.459  16.602  1.00 35.71  ?  92  HIS A CB    1 
ATOM   735  C  CG    . HIS A 1 93  ? 6.632   -9.055  17.426  1.00 39.34  ?  92  HIS A CG    1 
ATOM   736  N  ND1   . HIS A 1 93  ? 6.602   -9.012  18.803  1.00 43.10  ?  92  HIS A ND1   1 
ATOM   737  C  CD2   . HIS A 1 93  ? 7.881   -8.676  17.065  1.00 39.42  ?  92  HIS A CD2   1 
ATOM   738  C  CE1   . HIS A 1 93  ? 7.782   -8.626  19.255  1.00 43.31  ?  92  HIS A CE1   1 
ATOM   739  N  NE2   . HIS A 1 93  ? 8.575   -8.414  18.220  1.00 42.16  ?  92  HIS A NE2   1 
ATOM   740  N  N     . ASP A 1 94  ? 2.837   -11.148 16.121  1.00 34.48  ?  93  ASP A N     1 
ATOM   741  C  CA    . ASP A 1 94  ? 1.627   -11.298 15.329  1.00 37.06  ?  93  ASP A CA    1 
ATOM   742  C  C     . ASP A 1 94  ? 1.309   -9.985  14.611  1.00 35.88  ?  93  ASP A C     1 
ATOM   743  O  O     . ASP A 1 94  ? 1.416   -8.911  15.211  1.00 35.52  ?  93  ASP A O     1 
ATOM   744  C  CB    . ASP A 1 94  ? 0.460   -11.701 16.230  1.00 42.01  ?  93  ASP A CB    1 
ATOM   745  C  CG    . ASP A 1 94  ? -0.825  -11.908 15.468  1.00 45.57  ?  93  ASP A CG    1 
ATOM   746  O  OD1   . ASP A 1 94  ? -1.007  -13.002 14.894  1.00 48.08  ?  93  ASP A OD1   1 
ATOM   747  O  OD2   . ASP A 1 94  ? -1.651  -10.976 15.445  1.00 45.66  -1 93  ASP A OD2   1 
ATOM   748  N  N     . PRO A 1 95  ? 0.921   -10.039 13.330  1.00 35.45  ?  94  PRO A N     1 
ATOM   749  C  CA    . PRO A 1 95  ? 0.650   -8.782  12.601  1.00 36.59  ?  94  PRO A CA    1 
ATOM   750  C  C     . PRO A 1 95  ? -0.421  -7.931  13.257  1.00 37.98  ?  94  PRO A C     1 
ATOM   751  O  O     . PRO A 1 95  ? -0.260  -6.706  13.385  1.00 37.46  ?  94  PRO A O     1 
ATOM   752  C  CB    . PRO A 1 95  ? 0.215   -9.272  11.211  1.00 39.24  ?  94  PRO A CB    1 
ATOM   753  C  CG    . PRO A 1 95  ? 0.714   -10.671 11.106  1.00 39.96  ?  94  PRO A CG    1 
ATOM   754  C  CD    . PRO A 1 95  ? 0.706   -11.230 12.492  1.00 37.61  ?  94  PRO A CD    1 
ATOM   755  N  N     . VAL A 1 96  ? -1.522  -8.558  13.678  1.00 38.25  ?  95  VAL A N     1 
ATOM   756  C  CA    . VAL A 1 96  ? -2.587  -7.825  14.354  1.00 38.52  ?  95  VAL A CA    1 
ATOM   757  C  C     . VAL A 1 96  ? -2.097  -7.278  15.685  1.00 39.91  ?  95  VAL A C     1 
ATOM   758  O  O     . VAL A 1 96  ? -2.509  -6.194  16.102  1.00 40.35  ?  95  VAL A O     1 
ATOM   759  C  CB    . VAL A 1 96  ? -3.828  -8.724  14.526  1.00 38.31  ?  95  VAL A CB    1 
ATOM   760  C  CG1   . VAL A 1 96  ? -4.948  -7.963  15.226  1.00 34.56  ?  95  VAL A CG1   1 
ATOM   761  C  CG2   . VAL A 1 96  ? -4.296  -9.228  13.170  1.00 39.60  ?  95  VAL A CG2   1 
ATOM   762  N  N     . GLU A 1 97  ? -1.197  -7.998  16.360  1.00 39.55  ?  96  GLU A N     1 
ATOM   763  C  CA    . GLU A 1 97  ? -0.621  -7.494  17.606  1.00 39.11  ?  96  GLU A CA    1 
ATOM   764  C  C     . GLU A 1 97  ? 0.151   -6.193  17.382  1.00 35.61  ?  96  GLU A C     1 
ATOM   765  O  O     . GLU A 1 97  ? 0.008   -5.233  18.150  1.00 37.16  ?  96  GLU A O     1 
ATOM   766  C  CB    . GLU A 1 97  ? 0.282   -8.567  18.222  1.00 40.95  ?  96  GLU A CB    1 
ATOM   767  C  CG    . GLU A 1 97  ? 1.227   -8.072  19.303  1.00 46.15  ?  96  GLU A CG    1 
ATOM   768  C  CD    . GLU A 1 97  ? 2.384   -9.033  19.545  1.00 53.37  ?  96  GLU A CD    1 
ATOM   769  O  OE1   . GLU A 1 97  ? 2.358   -10.156 18.994  1.00 55.13  ?  96  GLU A OE1   1 
ATOM   770  O  OE2   . GLU A 1 97  ? 3.325   -8.664  20.281  1.00 56.03  -1 96  GLU A OE2   1 
ATOM   771  N  N     . VAL A 1 98  ? 0.969   -6.139  16.327  1.00 32.70  ?  97  VAL A N     1 
ATOM   772  C  CA    . VAL A 1 98  ? 1.758   -4.940  16.042  1.00 33.43  ?  97  VAL A CA    1 
ATOM   773  C  C     . VAL A 1 98  ? 0.855   -3.788  15.600  1.00 36.05  ?  97  VAL A C     1 
ATOM   774  O  O     . VAL A 1 98  ? 1.023   -2.631  16.029  1.00 37.58  ?  97  VAL A O     1 
ATOM   775  C  CB    . VAL A 1 98  ? 2.827   -5.271  14.984  1.00 32.05  ?  97  VAL A CB    1 
ATOM   776  C  CG1   . VAL A 1 98  ? 3.655   -4.045  14.642  1.00 29.71  ?  97  VAL A CG1   1 
ATOM   777  C  CG2   . VAL A 1 98  ? 3.716   -6.412  15.479  1.00 31.71  ?  97  VAL A CG2   1 
ATOM   778  N  N     . LYS A 1 99  ? -0.118  -4.079  14.734  1.00 35.82  ?  98  LYS A N     1 
ATOM   779  C  CA    . LYS A 1 99  ? -1.063  -3.037  14.356  1.00 36.79  ?  98  LYS A CA    1 
ATOM   780  C  C     . LYS A 1 99  ? -1.869  -2.559  15.557  1.00 38.39  ?  98  LYS A C     1 
ATOM   781  O  O     . LYS A 1 99  ? -2.247  -1.387  15.622  1.00 37.47  ?  98  LYS A O     1 
ATOM   782  C  CB    . LYS A 1 99  ? -1.980  -3.533  13.237  1.00 37.28  ?  98  LYS A CB    1 
ATOM   783  C  CG    . LYS A 1 99  ? -1.342  -3.447  11.854  1.00 34.18  ?  98  LYS A CG    1 
ATOM   784  C  CD    . LYS A 1 99  ? -2.358  -3.673  10.739  1.00 34.67  ?  98  LYS A CD    1 
ATOM   785  C  CE    . LYS A 1 99  ? -2.881  -5.101  10.741  1.00 37.91  ?  98  LYS A CE    1 
ATOM   786  N  NZ    . LYS A 1 99  ? -3.823  -5.350  9.609   1.00 36.61  1  98  LYS A NZ    1 
ATOM   787  N  N     . LYS A 1 100 ? -2.120  -3.436  16.532  1.00 37.67  ?  99  LYS A N     1 
ATOM   788  C  CA    . LYS A 1 100 ? -2.805  -3.002  17.742  1.00 36.13  ?  99  LYS A CA    1 
ATOM   789  C  C     . LYS A 1 100 ? -1.906  -2.116  18.590  1.00 35.02  ?  99  LYS A C     1 
ATOM   790  O  O     . LYS A 1 100 ? -2.388  -1.176  19.225  1.00 35.09  ?  99  LYS A O     1 
ATOM   791  C  CB    . LYS A 1 100 ? -3.284  -4.205  18.551  1.00 36.77  ?  99  LYS A CB    1 
ATOM   792  C  CG    . LYS A 1 100 ? -4.022  -3.812  19.822  1.00 37.98  ?  99  LYS A CG    1 
ATOM   793  C  CD    . LYS A 1 100 ? -4.462  -5.026  20.612  1.00 41.34  ?  99  LYS A CD    1 
ATOM   794  C  CE    . LYS A 1 100 ? -5.164  -4.612  21.893  1.00 45.38  ?  99  LYS A CE    1 
ATOM   795  N  NZ    . LYS A 1 100 ? -6.280  -3.674  21.601  1.00 49.68  1  99  LYS A NZ    1 
ATOM   796  N  N     . TRP A 1 101 ? -0.606  -2.420  18.639  1.00 38.63  ?  100 TRP A N     1 
ATOM   797  C  CA    . TRP A 1 101 ? 0.344   -1.469  19.215  1.00 39.99  ?  100 TRP A CA    1 
ATOM   798  C  C     . TRP A 1 101 ? 0.100   -0.081  18.649  1.00 39.66  ?  100 TRP A C     1 
ATOM   799  O  O     . TRP A 1 101 ? -0.081  0.893   19.392  1.00 39.95  ?  100 TRP A O     1 
ATOM   800  C  CB    . TRP A 1 101 ? 1.786   -1.868  18.908  1.00 42.39  ?  100 TRP A CB    1 
ATOM   801  C  CG    . TRP A 1 101 ? 2.293   -3.130  19.497  1.00 44.72  ?  100 TRP A CG    1 
ATOM   802  C  CD1   . TRP A 1 101 ? 1.726   -3.876  20.489  1.00 46.30  ?  100 TRP A CD1   1 
ATOM   803  C  CD2   . TRP A 1 101 ? 3.502   -3.798  19.129  1.00 45.59  ?  100 TRP A CD2   1 
ATOM   804  N  NE1   . TRP A 1 101 ? 2.510   -4.975  20.756  1.00 45.89  ?  100 TRP A NE1   1 
ATOM   805  C  CE2   . TRP A 1 101 ? 3.606   -4.948  19.933  1.00 45.52  ?  100 TRP A CE2   1 
ATOM   806  C  CE3   . TRP A 1 101 ? 4.506   -3.536  18.190  1.00 45.23  ?  100 TRP A CE3   1 
ATOM   807  C  CZ2   . TRP A 1 101 ? 4.675   -5.834  19.828  1.00 46.24  ?  100 TRP A CZ2   1 
ATOM   808  C  CZ3   . TRP A 1 101 ? 5.563   -4.416  18.086  1.00 45.93  ?  100 TRP A CZ3   1 
ATOM   809  C  CH2   . TRP A 1 101 ? 5.640   -5.552  18.900  1.00 46.01  ?  100 TRP A CH2   1 
ATOM   810  N  N     . ILE A 1 102 ? 0.087   0.016   17.318  1.00 37.70  ?  101 ILE A N     1 
ATOM   811  C  CA    . ILE A 1 102 ? -0.036  1.327   16.680  1.00 36.82  ?  101 ILE A CA    1 
ATOM   812  C  C     . ILE A 1 102 ? -1.403  1.946   16.959  1.00 39.62  ?  101 ILE A C     1 
ATOM   813  O  O     . ILE A 1 102 ? -1.510  3.148   17.233  1.00 39.57  ?  101 ILE A O     1 
ATOM   814  C  CB    . ILE A 1 102 ? 0.243   1.220   15.171  1.00 30.89  ?  101 ILE A CB    1 
ATOM   815  C  CG1   . ILE A 1 102 ? 1.657   0.686   14.940  1.00 29.85  ?  101 ILE A CG1   1 
ATOM   816  C  CG2   . ILE A 1 102 ? 0.063   2.579   14.499  1.00 29.63  ?  101 ILE A CG2   1 
ATOM   817  C  CD1   . ILE A 1 102 ? 2.743   1.518   15.593  1.00 25.99  ?  101 ILE A CD1   1 
ATOM   818  N  N     . ARG A 1 103 ? -2.467  1.142   16.900  1.00 42.71  ?  102 ARG A N     1 
ATOM   819  C  CA    . ARG A 1 103 ? -3.813  1.664   17.125  1.00 45.71  ?  102 ARG A CA    1 
ATOM   820  C  C     . ARG A 1 103 ? -3.981  2.175   18.550  1.00 45.94  ?  102 ARG A C     1 
ATOM   821  O  O     . ARG A 1 103 ? -4.556  3.248   18.765  1.00 44.04  ?  102 ARG A O     1 
ATOM   822  C  CB    . ARG A 1 103 ? -4.853  0.585   16.826  1.00 49.99  ?  102 ARG A CB    1 
ATOM   823  C  CG    . ARG A 1 103 ? -6.280  1.107   16.795  1.00 55.26  ?  102 ARG A CG    1 
ATOM   824  C  CD    . ARG A 1 103 ? -7.260  0.102   17.378  1.00 60.09  ?  102 ARG A CD    1 
ATOM   825  N  NE    . ARG A 1 103 ? -7.086  -0.053  18.819  1.00 63.10  ?  102 ARG A NE    1 
ATOM   826  C  CZ    . ARG A 1 103 ? -7.643  0.744   19.725  1.00 69.47  ?  102 ARG A CZ    1 
ATOM   827  N  NH1   . ARG A 1 103 ? -8.411  1.754   19.339  1.00 70.86  1  102 ARG A NH1   1 
ATOM   828  N  NH2   . ARG A 1 103 ? -7.431  0.531   21.017  1.00 73.50  ?  102 ARG A NH2   1 
ATOM   829  N  N     . ASP A 1 104 ? -3.498  1.413   19.537  1.00 48.00  ?  103 ASP A N     1 
ATOM   830  C  CA    . ASP A 1 104 ? -3.550  1.855   20.925  1.00 49.59  ?  103 ASP A CA    1 
ATOM   831  C  C     . ASP A 1 104 ? -2.686  3.087   21.143  1.00 48.74  ?  103 ASP A C     1 
ATOM   832  O  O     . ASP A 1 104 ? -3.009  3.931   21.987  1.00 49.30  ?  103 ASP A O     1 
ATOM   833  C  CB    . ASP A 1 104 ? -3.105  0.726   21.860  1.00 48.70  ?  103 ASP A CB    1 
ATOM   834  C  CG    . ASP A 1 104 ? -4.077  -0.450  21.877  1.00 49.02  ?  103 ASP A CG    1 
ATOM   835  O  OD1   . ASP A 1 104 ? -5.130  -0.389  21.205  1.00 47.81  ?  103 ASP A OD1   1 
ATOM   836  O  OD2   . ASP A 1 104 ? -3.783  -1.444  22.574  1.00 49.40  -1 103 ASP A OD2   1 
ATOM   837  N  N     . ALA A 1 105 ? -1.588  3.206   20.394  1.00 46.62  ?  104 ALA A N     1 
ATOM   838  C  CA    . ALA A 1 105 ? -0.776  4.414   20.470  1.00 45.82  ?  104 ALA A CA    1 
ATOM   839  C  C     . ALA A 1 105 ? -1.587  5.646   20.083  1.00 45.26  ?  104 ALA A C     1 
ATOM   840  O  O     . ALA A 1 105 ? -1.442  6.712   20.693  1.00 44.19  ?  104 ALA A O     1 
ATOM   841  C  CB    . ALA A 1 105 ? 0.453   4.272   19.574  1.00 42.92  ?  104 ALA A CB    1 
ATOM   842  N  N     . LEU A 1 106 ? -2.458  5.512   19.082  1.00 45.12  ?  105 LEU A N     1 
ATOM   843  C  CA    . LEU A 1 106 ? -3.276  6.607   18.579  1.00 47.27  ?  105 LEU A CA    1 
ATOM   844  C  C     . LEU A 1 106 ? -4.693  6.588   19.143  1.00 51.93  ?  105 LEU A C     1 
ATOM   845  O  O     . LEU A 1 106 ? -5.593  7.199   18.556  1.00 52.08  ?  105 LEU A O     1 
ATOM   846  C  CB    . LEU A 1 106 ? -3.327  6.563   17.051  1.00 44.21  ?  105 LEU A CB    1 
ATOM   847  C  CG    . LEU A 1 106 ? -2.022  6.798   16.294  1.00 45.16  ?  105 LEU A CG    1 
ATOM   848  C  CD1   . LEU A 1 106 ? -2.179  6.406   14.835  1.00 43.12  ?  105 LEU A CD1   1 
ATOM   849  C  CD2   . LEU A 1 106 ? -1.612  8.251   16.411  1.00 45.90  ?  105 LEU A CD2   1 
ATOM   850  N  N     . LYS A 1 107 ? -4.903  5.907   20.272  1.00 57.06  ?  106 LYS A N     1 
ATOM   851  C  CA    . LYS A 1 107 ? -6.256  5.693   20.780  1.00 64.37  ?  106 LYS A CA    1 
ATOM   852  C  C     . LYS A 1 107 ? -6.971  7.013   21.054  1.00 70.21  ?  106 LYS A C     1 
ATOM   853  O  O     . LYS A 1 107 ? -8.169  7.149   20.774  1.00 69.44  ?  106 LYS A O     1 
ATOM   854  C  CB    . LYS A 1 107 ? -6.199  4.834   22.045  1.00 66.67  ?  106 LYS A CB    1 
ATOM   855  C  CG    . LYS A 1 107 ? -7.457  4.027   22.331  1.00 69.15  ?  106 LYS A CG    1 
ATOM   856  C  CD    . LYS A 1 107 ? -7.243  3.088   23.513  1.00 71.27  ?  106 LYS A CD    1 
ATOM   857  C  CE    . LYS A 1 107 ? -8.480  2.250   23.808  1.00 72.17  ?  106 LYS A CE    1 
ATOM   858  N  NZ    . LYS A 1 107 ? -8.269  1.344   24.977  1.00 72.22  1  106 LYS A NZ    1 
ATOM   859  N  N     . ASP A 1 108 ? -6.251  8.004   21.582  1.00 75.47  ?  107 ASP A N     1 
ATOM   860  C  CA    . ASP A 1 108 ? -6.837  9.274   21.993  1.00 78.60  ?  107 ASP A CA    1 
ATOM   861  C  C     . ASP A 1 108 ? -6.419  10.427  21.085  1.00 73.18  ?  107 ASP A C     1 
ATOM   862  O  O     . ASP A 1 108 ? -6.360  11.579  21.521  1.00 72.97  ?  107 ASP A O     1 
ATOM   863  C  CB    . ASP A 1 108 ? -6.467  9.578   23.443  1.00 86.69  ?  107 ASP A CB    1 
ATOM   864  C  CG    . ASP A 1 108 ? -6.826  8.445   24.383  1.00 93.49  ?  107 ASP A CG    1 
ATOM   865  O  OD1   . ASP A 1 108 ? -7.907  7.844   24.205  1.00 95.62  ?  107 ASP A OD1   1 
ATOM   866  O  OD2   . ASP A 1 108 ? -6.025  8.149   25.295  1.00 96.01  -1 107 ASP A OD2   1 
ATOM   867  N  N     . TYR A 1 109 ? -6.128  10.135  19.822  1.00 68.87  ?  108 TYR A N     1 
ATOM   868  C  CA    . TYR A 1 109 ? -5.737  11.144  18.846  1.00 63.99  ?  108 TYR A CA    1 
ATOM   869  C  C     . TYR A 1 109 ? -6.887  11.348  17.871  1.00 61.95  ?  108 TYR A C     1 
ATOM   870  O  O     . TYR A 1 109 ? -7.332  10.393  17.225  1.00 61.11  ?  108 TYR A O     1 
ATOM   871  C  CB    . TYR A 1 109 ? -4.466  10.723  18.107  1.00 60.37  ?  108 TYR A CB    1 
ATOM   872  C  CG    . TYR A 1 109 ? -3.907  11.770  17.167  1.00 58.94  ?  108 TYR A CG    1 
ATOM   873  C  CD1   . TYR A 1 109 ? -2.995  12.717  17.612  1.00 57.78  ?  108 TYR A CD1   1 
ATOM   874  C  CD2   . TYR A 1 109 ? -4.282  11.801  15.829  1.00 60.19  ?  108 TYR A CD2   1 
ATOM   875  C  CE1   . TYR A 1 109 ? -2.477  13.670  16.753  1.00 57.76  ?  108 TYR A CE1   1 
ATOM   876  C  CE2   . TYR A 1 109 ? -3.771  12.750  14.963  1.00 59.71  ?  108 TYR A CE2   1 
ATOM   877  C  CZ    . TYR A 1 109 ? -2.869  13.682  15.429  1.00 59.76  ?  108 TYR A CZ    1 
ATOM   878  O  OH    . TYR A 1 109 ? -2.358  14.627  14.567  1.00 59.22  ?  108 TYR A OH    1 
ATOM   879  N  N     . GLY A 1 110 ? -7.370  12.585  17.776  1.00 60.89  ?  109 GLY A N     1 
ATOM   880  C  CA    . GLY A 1 110 ? -8.418  12.935  16.837  1.00 60.74  ?  109 GLY A CA    1 
ATOM   881  C  C     . GLY A 1 110 ? -9.694  12.148  17.062  1.00 61.68  ?  109 GLY A C     1 
ATOM   882  O  O     . GLY A 1 110 ? -10.055 11.790  18.188  1.00 63.29  ?  109 GLY A O     1 
ATOM   883  N  N     . ASN A 1 111 ? -10.392 11.868  15.960  1.00 64.08  ?  110 ASN A N     1 
ATOM   884  C  CA    . ASN A 1 111 ? -11.642 11.120  16.014  1.00 65.90  ?  110 ASN A CA    1 
ATOM   885  C  C     . ASN A 1 111 ? -11.441 9.642   16.326  1.00 65.00  ?  110 ASN A C     1 
ATOM   886  O  O     . ASN A 1 111 ? -12.433 8.909   16.410  1.00 68.36  ?  110 ASN A O     1 
ATOM   887  C  CB    . ASN A 1 111 ? -12.401 11.262  14.692  1.00 69.80  ?  110 ASN A CB    1 
ATOM   888  C  CG    . ASN A 1 111 ? -12.601 12.709  14.283  1.00 74.83  ?  110 ASN A CG    1 
ATOM   889  O  OD1   . ASN A 1 111 ? -11.747 13.562  14.527  1.00 77.08  ?  110 ASN A OD1   1 
ATOM   890  N  ND2   . ASN A 1 111 ? -13.737 12.994  13.657  1.00 75.45  ?  110 ASN A ND2   1 
ATOM   891  N  N     . GLY A 1 112 ? -10.208 9.187   16.494  1.00 60.77  ?  111 GLY A N     1 
ATOM   892  C  CA    . GLY A 1 112 ? -9.920  7.807   16.822  1.00 59.39  ?  111 GLY A CA    1 
ATOM   893  C  C     . GLY A 1 112 ? -9.003  7.158   15.802  1.00 57.30  ?  111 GLY A C     1 
ATOM   894  O  O     . GLY A 1 112 ? -8.548  7.777   14.841  1.00 57.02  ?  111 GLY A O     1 
ATOM   895  N  N     . ALA A 1 113 ? -8.735  5.877   16.045  1.00 52.55  ?  112 ALA A N     1 
ATOM   896  C  CA    . ALA A 1 113 ? -7.886  5.074   15.179  1.00 48.16  ?  112 ALA A CA    1 
ATOM   897  C  C     . ALA A 1 113 ? -8.401  3.644   15.187  1.00 48.04  ?  112 ALA A C     1 
ATOM   898  O  O     . ALA A 1 113 ? -8.944  3.170   16.189  1.00 50.50  ?  112 ALA A O     1 
ATOM   899  C  CB    . ALA A 1 113 ? -6.420  5.115   15.623  1.00 44.77  ?  112 ALA A CB    1 
ATOM   900  N  N     . GLU A 1 114 ? -8.226  2.958   14.061  1.00 43.37  ?  113 GLU A N     1 
ATOM   901  C  CA    . GLU A 1 114 ? -8.776  1.620   13.919  1.00 42.06  ?  113 GLU A CA    1 
ATOM   902  C  C     . GLU A 1 114 ? -7.855  0.753   13.074  1.00 38.21  ?  113 GLU A C     1 
ATOM   903  O  O     . GLU A 1 114 ? -7.152  1.238   12.179  1.00 37.70  ?  113 GLU A O     1 
ATOM   904  C  CB    . GLU A 1 114 ? -10.183 1.649   13.305  1.00 45.70  ?  113 GLU A CB    1 
ATOM   905  C  CG    . GLU A 1 114 ? -10.250 2.197   11.893  1.00 50.11  ?  113 GLU A CG    1 
ATOM   906  C  CD    . GLU A 1 114 ? -11.676 2.313   11.388  1.00 56.37  ?  113 GLU A CD    1 
ATOM   907  O  OE1   . GLU A 1 114 ? -12.590 2.488   12.221  1.00 60.64  ?  113 GLU A OE1   1 
ATOM   908  O  OE2   . GLU A 1 114 ? -11.887 2.225   10.160  1.00 58.10  -1 113 GLU A OE2   1 
ATOM   909  N  N     . ILE A 1 115 ? -7.883  -0.542  13.376  1.00 36.73  ?  114 ILE A N     1 
ATOM   910  C  CA    . ILE A 1 115 ? -7.109  -1.548  12.664  1.00 39.71  ?  114 ILE A CA    1 
ATOM   911  C  C     . ILE A 1 115 ? -7.912  -2.004  11.455  1.00 39.60  ?  114 ILE A C     1 
ATOM   912  O  O     . ILE A 1 115 ? -9.040  -2.492  11.594  1.00 40.61  ?  114 ILE A O     1 
ATOM   913  C  CB    . ILE A 1 115 ? -6.779  -2.739  13.575  1.00 41.66  ?  114 ILE A CB    1 
ATOM   914  C  CG1   . ILE A 1 115 ? -6.061  -2.268  14.838  1.00 44.10  ?  114 ILE A CG1   1 
ATOM   915  C  CG2   . ILE A 1 115 ? -5.944  -3.767  12.823  1.00 43.46  ?  114 ILE A CG2   1 
ATOM   916  C  CD1   . ILE A 1 115 ? -5.982  -3.321  15.913  1.00 44.94  ?  114 ILE A CD1   1 
ATOM   917  N  N     . ARG A 1 116 ? -7.338  -1.843  10.270  1.00 37.14  ?  115 ARG A N     1 
ATOM   918  C  CA    . ARG A 1 116 ? -7.908  -2.334  9.032   1.00 36.58  ?  115 ARG A CA    1 
ATOM   919  C  C     . ARG A 1 116 ? -6.976  -3.389  8.456   1.00 36.04  ?  115 ARG A C     1 
ATOM   920  O  O     . ARG A 1 116 ? -5.787  -3.445  8.793   1.00 40.84  ?  115 ARG A O     1 
ATOM   921  C  CB    . ARG A 1 116 ? -8.122  -1.186  8.045   1.00 37.93  ?  115 ARG A CB    1 
ATOM   922  C  CG    . ARG A 1 116 ? -8.887  -0.024  8.662   1.00 41.87  ?  115 ARG A CG    1 
ATOM   923  C  CD    . ARG A 1 116 ? -8.932  1.169   7.734   1.00 45.35  ?  115 ARG A CD    1 
ATOM   924  N  NE    . ARG A 1 116 ? -9.485  0.813   6.433   1.00 50.04  ?  115 ARG A NE    1 
ATOM   925  C  CZ    . ARG A 1 116 ? -9.464  1.608   5.370   1.00 51.18  ?  115 ARG A CZ    1 
ATOM   926  N  NH1   . ARG A 1 116 ? -8.910  2.813   5.453   1.00 51.33  1  115 ARG A NH1   1 
ATOM   927  N  NH2   . ARG A 1 116 ? -9.993  1.195   4.224   1.00 48.82  ?  115 ARG A NH2   1 
ATOM   928  N  N     . ARG A 1 117 ? -7.533  -4.217  7.566   1.00 35.18  ?  116 ARG A N     1 
ATOM   929  C  CA    . ARG A 1 117 ? -6.815  -5.389  7.070   1.00 38.34  ?  116 ARG A CA    1 
ATOM   930  C  C     . ARG A 1 117 ? -5.402  -5.053  6.616   1.00 34.11  ?  116 ARG A C     1 
ATOM   931  O  O     . ARG A 1 117 ? -4.492  -5.876  6.760   1.00 31.94  ?  116 ARG A O     1 
ATOM   932  C  CB    . ARG A 1 117 ? -7.590  -6.033  5.917   1.00 44.12  ?  116 ARG A CB    1 
ATOM   933  C  CG    . ARG A 1 117 ? -8.945  -6.605  6.313   1.00 51.73  ?  116 ARG A CG    1 
ATOM   934  C  CD    . ARG A 1 117 ? -9.653  -7.220  5.112   1.00 57.47  ?  116 ARG A CD    1 
ATOM   935  N  NE    . ARG A 1 117 ? -11.088 -7.377  5.335   1.00 62.40  ?  116 ARG A NE    1 
ATOM   936  C  CZ    . ARG A 1 117 ? -11.648 -8.460  5.863   1.00 66.32  ?  116 ARG A CZ    1 
ATOM   937  N  NH1   . ARG A 1 117 ? -10.894 -9.490  6.227   1.00 66.15  1  116 ARG A NH1   1 
ATOM   938  N  NH2   . ARG A 1 117 ? -12.964 -8.512  6.029   1.00 69.16  ?  116 ARG A NH2   1 
ATOM   939  N  N     . SER A 1 118 ? -5.187  -3.851  6.088   1.00 31.52  ?  117 SER A N     1 
ATOM   940  C  CA    . SER A 1 118 ? -3.891  -3.498  5.538   1.00 30.39  ?  117 SER A CA    1 
ATOM   941  C  C     . SER A 1 118 ? -3.199  -2.347  6.254   1.00 27.82  ?  117 SER A C     1 
ATOM   942  O  O     . SER A 1 118 ? -2.071  -2.001  5.876   1.00 28.35  ?  117 SER A O     1 
ATOM   943  C  CB    . SER A 1 118 ? -4.031  -3.156  4.050   1.00 34.90  ?  117 SER A CB    1 
ATOM   944  O  OG    . SER A 1 118 ? -4.640  -4.219  3.340   1.00 38.01  ?  117 SER A OG    1 
ATOM   945  N  N     . CYS A 1 119 ? -3.807  -1.746  7.273   1.00 28.56  ?  118 CYS A N     1 
ATOM   946  C  CA    . CYS A 1 119 ? -3.176  -0.560  7.848   1.00 26.01  ?  118 CYS A CA    1 
ATOM   947  C  C     . CYS A 1 119 ? -3.831  -0.239  9.184   1.00 31.57  ?  118 CYS A C     1 
ATOM   948  O  O     . CYS A 1 119 ? -4.719  -0.952  9.656   1.00 36.37  ?  118 CYS A O     1 
ATOM   949  C  CB    . CYS A 1 119 ? -3.264  0.641   6.901   1.00 25.55  ?  118 CYS A CB    1 
ATOM   950  S  SG    . CYS A 1 119 ? -4.946  1.288   6.628   1.00 31.24  ?  118 CYS A SG    1 
ATOM   951  N  N     . VAL A 1 120 ? -3.350  0.830   9.807   1.00 30.11  ?  119 VAL A N     1 
ATOM   952  C  CA    . VAL A 1 120 ? -4.028  1.472   10.921  1.00 34.12  ?  119 VAL A CA    1 
ATOM   953  C  C     . VAL A 1 120 ? -4.416  2.858   10.439  1.00 34.95  ?  119 VAL A C     1 
ATOM   954  O  O     . VAL A 1 120 ? -3.554  3.625   9.992   1.00 35.11  ?  119 VAL A O     1 
ATOM   955  C  CB    . VAL A 1 120 ? -3.141  1.550   12.175  1.00 34.89  ?  119 VAL A CB    1 
ATOM   956  C  CG1   . VAL A 1 120 ? -3.790  2.437   13.224  1.00 32.11  ?  119 VAL A CG1   1 
ATOM   957  C  CG2   . VAL A 1 120 ? -2.885  0.161   12.733  1.00 36.56  ?  119 VAL A CG2   1 
ATOM   958  N  N     . THR A 1 121 ? -5.703  3.173   10.492  1.00 29.87  ?  120 THR A N     1 
ATOM   959  C  CA    . THR A 1 121 ? -6.190  4.462   10.023  1.00 30.55  ?  120 THR A CA    1 
ATOM   960  C  C     . THR A 1 121 ? -6.580  5.315   11.217  1.00 35.76  ?  120 THR A C     1 
ATOM   961  O  O     . THR A 1 121 ? -7.315  4.856   12.097  1.00 33.13  ?  120 THR A O     1 
ATOM   962  C  CB    . THR A 1 121 ? -7.379  4.306   9.074   1.00 32.46  ?  120 THR A CB    1 
ATOM   963  O  OG1   . THR A 1 121 ? -6.942  3.686   7.859   1.00 33.76  ?  120 THR A OG1   1 
ATOM   964  C  CG2   . THR A 1 121 ? -7.980  5.663   8.746   1.00 31.05  ?  120 THR A CG2   1 
ATOM   965  N  N     . VAL A 1 122 ? -6.073  6.542   11.250  1.00 38.76  ?  121 VAL A N     1 
ATOM   966  C  CA    . VAL A 1 122 ? -6.440  7.521   12.265  1.00 43.39  ?  121 VAL A CA    1 
ATOM   967  C  C     . VAL A 1 122 ? -7.208  8.641   11.579  1.00 43.77  ?  121 VAL A C     1 
ATOM   968  O  O     . VAL A 1 122 ? -6.884  9.031   10.450  1.00 39.47  ?  121 VAL A O     1 
ATOM   969  C  CB    . VAL A 1 122 ? -5.205  8.055   13.021  1.00 47.65  ?  121 VAL A CB    1 
ATOM   970  C  CG1   . VAL A 1 122 ? -4.199  8.647   12.059  1.00 48.02  ?  121 VAL A CG1   1 
ATOM   971  C  CG2   . VAL A 1 122 ? -5.615  9.077   14.075  1.00 51.59  ?  121 VAL A CG2   1 
ATOM   972  N  N     . PHE A 1 123 ? -8.245  9.138   12.247  1.00 48.75  ?  122 PHE A N     1 
ATOM   973  C  CA    . PHE A 1 123 ? -9.156  10.102  11.648  1.00 48.42  ?  122 PHE A CA    1 
ATOM   974  C  C     . PHE A 1 123 ? -8.967  11.483  12.264  1.00 48.86  ?  122 PHE A C     1 
ATOM   975  O  O     . PHE A 1 123 ? -8.628  11.615  13.443  1.00 49.32  ?  122 PHE A O     1 
ATOM   976  C  CB    . PHE A 1 123 ? -10.605 9.639   11.804  1.00 46.05  ?  122 PHE A CB    1 
ATOM   977  C  CG    . PHE A 1 123 ? -10.900 8.353   11.086  1.00 45.02  ?  122 PHE A CG    1 
ATOM   978  C  CD1   . PHE A 1 123 ? -11.328 8.365   9.768   1.00 47.04  ?  122 PHE A CD1   1 
ATOM   979  C  CD2   . PHE A 1 123 ? -10.735 7.135   11.720  1.00 43.65  ?  122 PHE A CD2   1 
ATOM   980  C  CE1   . PHE A 1 123 ? -11.596 7.185   9.101   1.00 47.42  ?  122 PHE A CE1   1 
ATOM   981  C  CE2   . PHE A 1 123 ? -11.002 5.953   11.059  1.00 44.80  ?  122 PHE A CE2   1 
ATOM   982  C  CZ    . PHE A 1 123 ? -11.433 5.977   9.748   1.00 46.27  ?  122 PHE A CZ    1 
ATOM   983  N  N     . LYS A 1 124 ? -9.204  12.513  11.451  1.00 50.59  ?  123 LYS A N     1 
ATOM   984  C  CA    . LYS A 1 124 ? -8.977  13.901  11.819  1.00 53.36  ?  123 LYS A CA    1 
ATOM   985  C  C     . LYS A 1 124 ? -9.953  14.744  11.013  1.00 53.21  ?  123 LYS A C     1 
ATOM   986  O  O     . LYS A 1 124 ? -10.359 14.329  9.920   1.00 50.19  ?  123 LYS A O     1 
ATOM   987  C  CB    . LYS A 1 124 ? -7.526  14.317  11.520  1.00 55.24  ?  123 LYS A CB    1 
ATOM   988  C  CG    . LYS A 1 124 ? -6.872  15.201  12.570  1.00 58.84  ?  123 LYS A CG    1 
ATOM   989  C  CD    . LYS A 1 124 ? -6.847  14.525  13.929  1.00 59.77  ?  123 LYS A CD    1 
ATOM   990  C  CE    . LYS A 1 124 ? -6.915  15.550  15.052  1.00 65.08  ?  123 LYS A CE    1 
ATOM   991  N  NZ    . LYS A 1 124 ? -5.746  16.470  15.078  1.00 68.29  1  123 LYS A NZ    1 
ATOM   992  N  N     . PRO A 1 125 ? -10.360 15.920  11.521  1.00 55.35  ?  124 PRO A N     1 
ATOM   993  C  CA    . PRO A 1 125 ? -11.286 16.765  10.753  1.00 53.81  ?  124 PRO A CA    1 
ATOM   994  C  C     . PRO A 1 125 ? -10.800 17.035  9.339   1.00 51.22  ?  124 PRO A C     1 
ATOM   995  O  O     . PRO A 1 125 ? -9.843  17.785  9.130   1.00 55.00  ?  124 PRO A O     1 
ATOM   996  C  CB    . PRO A 1 125 ? -11.353 18.058  11.578  1.00 57.44  ?  124 PRO A CB    1 
ATOM   997  C  CG    . PRO A 1 125 ? -10.171 17.998  12.504  1.00 60.49  ?  124 PRO A CG    1 
ATOM   998  C  CD    . PRO A 1 125 ? -10.000 16.545  12.803  1.00 57.80  ?  124 PRO A CD    1 
ATOM   999  N  N     . GLY A 1 126 ? -11.449 16.405  8.364   1.00 43.73  ?  125 GLY A N     1 
ATOM   1000 C  CA    . GLY A 1 126 ? -11.151 16.638  6.969   1.00 43.84  ?  125 GLY A CA    1 
ATOM   1001 C  C     . GLY A 1 126 ? -10.141 15.700  6.344   1.00 43.00  ?  125 GLY A C     1 
ATOM   1002 O  O     . GLY A 1 126 ? -9.893  15.808  5.136   1.00 42.46  ?  125 GLY A O     1 
ATOM   1003 N  N     . TYR A 1 127 ? -9.546  14.785  7.109   1.00 45.12  ?  126 TYR A N     1 
ATOM   1004 C  CA    . TYR A 1 127 ? -8.585  13.872  6.502   1.00 43.18  ?  126 TYR A CA    1 
ATOM   1005 C  C     . TYR A 1 127 ? -8.350  12.676  7.410   1.00 39.67  ?  126 TYR A C     1 
ATOM   1006 O  O     . TYR A 1 127 ? -8.601  12.722  8.617   1.00 37.88  ?  126 TYR A O     1 
ATOM   1007 C  CB    . TYR A 1 127 ? -7.256  14.573  6.195   1.00 46.50  ?  126 TYR A CB    1 
ATOM   1008 C  CG    . TYR A 1 127 ? -6.467  14.998  7.411   1.00 50.20  ?  126 TYR A CG    1 
ATOM   1009 C  CD1   . TYR A 1 127 ? -6.743  16.196  8.063   1.00 52.80  ?  126 TYR A CD1   1 
ATOM   1010 C  CD2   . TYR A 1 127 ? -5.432  14.212  7.897   1.00 50.49  ?  126 TYR A CD2   1 
ATOM   1011 C  CE1   . TYR A 1 127 ? -6.017  16.588  9.171   1.00 52.73  ?  126 TYR A CE1   1 
ATOM   1012 C  CE2   . TYR A 1 127 ? -4.703  14.596  9.004   1.00 51.28  ?  126 TYR A CE2   1 
ATOM   1013 C  CZ    . TYR A 1 127 ? -4.998  15.783  9.636   1.00 53.09  ?  126 TYR A CZ    1 
ATOM   1014 O  OH    . TYR A 1 127 ? -4.269  16.162  10.739  1.00 54.53  ?  126 TYR A OH    1 
ATOM   1015 N  N     . HIS A 1 128 ? -7.853  11.604  6.804   1.00 38.50  ?  127 HIS A N     1 
ATOM   1016 C  CA    . HIS A 1 128 ? -7.442  10.421  7.539   1.00 40.28  ?  127 HIS A CA    1 
ATOM   1017 C  C     . HIS A 1 128 ? -6.035  10.035  7.113   1.00 36.38  ?  127 HIS A C     1 
ATOM   1018 O  O     . HIS A 1 128 ? -5.639  10.235  5.960   1.00 32.53  ?  127 HIS A O     1 
ATOM   1019 C  CB    . HIS A 1 128 ? -8.405  9.249   7.317   1.00 42.67  ?  127 HIS A CB    1 
ATOM   1020 C  CG    . HIS A 1 128 ? -8.527  8.831   5.886   1.00 41.56  ?  127 HIS A CG    1 
ATOM   1021 N  ND1   . HIS A 1 128 ? -9.549  9.262   5.069   1.00 39.87  ?  127 HIS A ND1   1 
ATOM   1022 C  CD2   . HIS A 1 128 ? -7.750  8.026   5.124   1.00 40.00  ?  127 HIS A CD2   1 
ATOM   1023 C  CE1   . HIS A 1 128 ? -9.400  8.738   3.866   1.00 38.84  ?  127 HIS A CE1   1 
ATOM   1024 N  NE2   . HIS A 1 128 ? -8.315  7.985   3.873   1.00 38.89  ?  127 HIS A NE2   1 
ATOM   1025 N  N     . VAL A 1 129 ? -5.281  9.496   8.065   1.00 37.09  ?  128 VAL A N     1 
ATOM   1026 C  CA    . VAL A 1 129 ? -3.922  9.022   7.832   1.00 33.48  ?  128 VAL A CA    1 
ATOM   1027 C  C     . VAL A 1 129 ? -3.935  7.501   7.898   1.00 30.39  ?  128 VAL A C     1 
ATOM   1028 O  O     . VAL A 1 129 ? -4.367  6.915   8.900   1.00 32.83  ?  128 VAL A O     1 
ATOM   1029 C  CB    . VAL A 1 129 ? -2.930  9.614   8.843   1.00 32.82  ?  128 VAL A CB    1 
ATOM   1030 C  CG1   . VAL A 1 129 ? -1.520  9.106   8.568   1.00 32.88  ?  128 VAL A CG1   1 
ATOM   1031 C  CG2   . VAL A 1 129 ? -2.978  11.132  8.797   1.00 35.02  ?  128 VAL A CG2   1 
ATOM   1032 N  N     . ASP A 1 130 ? -3.465  6.871   6.825   1.00 29.96  ?  129 ASP A N     1 
ATOM   1033 C  CA    . ASP A 1 130 ? -3.360  5.422   6.722   1.00 28.27  ?  129 ASP A CA    1 
ATOM   1034 C  C     . ASP A 1 130 ? -1.894  5.038   6.911   1.00 28.10  ?  129 ASP A C     1 
ATOM   1035 O  O     . ASP A 1 130 ? -1.048  5.327   6.051   1.00 25.23  ?  129 ASP A O     1 
ATOM   1036 C  CB    . ASP A 1 130 ? -3.893  4.932   5.376   1.00 28.60  ?  129 ASP A CB    1 
ATOM   1037 C  CG    . ASP A 1 130 ? -5.369  5.246   5.178   1.00 30.88  ?  129 ASP A CG    1 
ATOM   1038 O  OD1   . ASP A 1 130 ? -6.067  5.483   6.186   1.00 31.56  ?  129 ASP A OD1   1 
ATOM   1039 O  OD2   . ASP A 1 130 ? -5.832  5.253   4.014   1.00 30.79  -1 129 ASP A OD2   1 
ATOM   1040 N  N     . LEU A 1 131 ? -1.594  4.397   8.038   1.00 27.84  ?  130 LEU A N     1 
ATOM   1041 C  CA    . LEU A 1 131 ? -0.248  3.946   8.360   1.00 29.85  ?  130 LEU A CA    1 
ATOM   1042 C  C     . LEU A 1 131 ? -0.161  2.459   8.050   1.00 27.54  ?  130 LEU A C     1 
ATOM   1043 O  O     . LEU A 1 131 ? -0.731  1.634   8.773   1.00 30.88  ?  130 LEU A O     1 
ATOM   1044 C  CB    . LEU A 1 131 ? 0.086   4.211   9.827   1.00 34.20  ?  130 LEU A CB    1 
ATOM   1045 C  CG    . LEU A 1 131 ? -0.073  5.638   10.346  1.00 39.22  ?  130 LEU A CG    1 
ATOM   1046 C  CD1   . LEU A 1 131 ? -1.448  5.832   10.963  1.00 42.76  ?  130 LEU A CD1   1 
ATOM   1047 C  CD2   . LEU A 1 131 ? 1.021   5.966   11.350  1.00 43.00  ?  130 LEU A CD2   1 
ATOM   1048 N  N     . ALA A 1 132 ? 0.515   2.131   6.957   1.00 24.19  ?  131 ALA A N     1 
ATOM   1049 C  CA    . ALA A 1 132 ? 0.905   0.756   6.709   1.00 22.74  ?  131 ALA A CA    1 
ATOM   1050 C  C     . ALA A 1 132 ? 2.041   0.390   7.653   1.00 24.66  ?  131 ALA A C     1 
ATOM   1051 O  O     . ALA A 1 132 ? 2.935   1.199   7.920   1.00 23.45  ?  131 ALA A O     1 
ATOM   1052 C  CB    . ALA A 1 132 ? 1.325   0.572   5.251   1.00 20.09  ?  131 ALA A CB    1 
ATOM   1053 N  N     . VAL A 1 133 ? 1.981   -0.820  8.191   1.00 25.16  ?  132 VAL A N     1 
ATOM   1054 C  CA    . VAL A 1 133 ? 2.848   -1.237  9.286   1.00 24.38  ?  132 VAL A CA    1 
ATOM   1055 C  C     . VAL A 1 133 ? 3.694   -2.398  8.791   1.00 26.82  ?  132 VAL A C     1 
ATOM   1056 O  O     . VAL A 1 133 ? 3.153   -3.420  8.347   1.00 29.07  ?  132 VAL A O     1 
ATOM   1057 C  CB    . VAL A 1 133 ? 2.032   -1.629  10.527  1.00 26.32  ?  132 VAL A CB    1 
ATOM   1058 C  CG1   . VAL A 1 133 ? 2.950   -2.037  11.661  1.00 27.69  ?  132 VAL A CG1   1 
ATOM   1059 C  CG2   . VAL A 1 133 ? 1.136   -0.469  10.947  1.00 27.24  ?  132 VAL A CG2   1 
ATOM   1060 N  N     . TYR A 1 134 ? 5.016   -2.245  8.866   1.00 23.11  ?  133 TYR A N     1 
ATOM   1061 C  CA    . TYR A 1 134 ? 5.938   -3.234  8.340   1.00 23.02  ?  133 TYR A CA    1 
ATOM   1062 C  C     . TYR A 1 134 ? 6.921   -3.678  9.415   1.00 23.56  ?  133 TYR A C     1 
ATOM   1063 O  O     . TYR A 1 134 ? 7.199   -2.956  10.373  1.00 24.66  ?  133 TYR A O     1 
ATOM   1064 C  CB    . TYR A 1 134 ? 6.726   -2.678  7.143   1.00 21.76  ?  133 TYR A CB    1 
ATOM   1065 C  CG    . TYR A 1 134 ? 5.871   -2.054  6.058   1.00 19.57  ?  133 TYR A CG    1 
ATOM   1066 C  CD1   . TYR A 1 134 ? 5.460   -0.729  6.151   1.00 19.14  ?  133 TYR A CD1   1 
ATOM   1067 C  CD2   . TYR A 1 134 ? 5.496   -2.782  4.934   1.00 21.03  ?  133 TYR A CD2   1 
ATOM   1068 C  CE1   . TYR A 1 134 ? 4.690   -0.146  5.161   1.00 21.75  ?  133 TYR A CE1   1 
ATOM   1069 C  CE2   . TYR A 1 134 ? 4.725   -2.208  3.938   1.00 22.38  ?  133 TYR A CE2   1 
ATOM   1070 C  CZ    . TYR A 1 134 ? 4.323   -0.889  4.059   1.00 23.86  ?  133 TYR A CZ    1 
ATOM   1071 O  OH    . TYR A 1 134 ? 3.555   -0.311  3.073   1.00 23.43  ?  133 TYR A OH    1 
ATOM   1072 N  N     . ALA A 1 135 ? 7.464   -4.874  9.231   1.00 27.44  ?  134 ALA A N     1 
ATOM   1073 C  CA    . ALA A 1 135 ? 8.546   -5.355  10.074  1.00 23.24  ?  134 ALA A CA    1 
ATOM   1074 C  C     . ALA A 1 135 ? 9.887   -4.982  9.457   1.00 28.12  ?  134 ALA A C     1 
ATOM   1075 O  O     . ALA A 1 135 ? 9.989   -4.688  8.263   1.00 28.94  ?  134 ALA A O     1 
ATOM   1076 C  CB    . ALA A 1 135 ? 8.452   -6.868  10.263  1.00 23.71  ?  134 ALA A CB    1 
ATOM   1077 N  N     . ASP A 1 136 ? 10.921  -4.991  10.289  1.00 30.94  ?  135 ASP A N     1 
ATOM   1078 C  CA    . ASP A 1 136 ? 12.265  -4.627  9.838   1.00 30.84  ?  135 ASP A CA    1 
ATOM   1079 C  C     . ASP A 1 136 ? 12.819  -5.716  8.929   1.00 28.37  ?  135 ASP A C     1 
ATOM   1080 O  O     . ASP A 1 136 ? 12.934  -6.870  9.361   1.00 29.60  ?  135 ASP A O     1 
ATOM   1081 C  CB    . ASP A 1 136 ? 13.180  -4.420  11.045  1.00 34.71  ?  135 ASP A CB    1 
ATOM   1082 C  CG    . ASP A 1 136 ? 14.518  -3.783  10.683  1.00 36.47  ?  135 ASP A CG    1 
ATOM   1083 O  OD1   . ASP A 1 136 ? 14.996  -3.938  9.538   1.00 36.65  ?  135 ASP A OD1   1 
ATOM   1084 O  OD2   . ASP A 1 136 ? 15.105  -3.130  11.569  1.00 38.87  -1 135 ASP A OD2   1 
ATOM   1085 N  N     . PRO A 1 137 ? 13.171  -5.405  7.680   1.00 27.50  ?  136 PRO A N     1 
ATOM   1086 C  CA    . PRO A 1 137 ? 13.764  -6.437  6.812   1.00 30.26  ?  136 PRO A CA    1 
ATOM   1087 C  C     . PRO A 1 137 ? 15.047  -7.031  7.369   1.00 37.65  ?  136 PRO A C     1 
ATOM   1088 O  O     . PRO A 1 137 ? 15.301  -8.224  7.164   1.00 39.13  ?  136 PRO A O     1 
ATOM   1089 C  CB    . PRO A 1 137 ? 14.016  -5.684  5.497   1.00 31.05  ?  136 PRO A CB    1 
ATOM   1090 C  CG    . PRO A 1 137 ? 13.047  -4.523  5.525   1.00 30.03  ?  136 PRO A CG    1 
ATOM   1091 C  CD    . PRO A 1 137 ? 12.948  -4.132  6.969   1.00 27.76  ?  136 PRO A CD    1 
ATOM   1092 N  N     . GLU A 1 138 ? 15.862  -6.237  8.071   1.00 43.12  ?  137 GLU A N     1 
ATOM   1093 C  CA    . GLU A 1 138 ? 17.111  -6.752  8.629   1.00 47.61  ?  137 GLU A CA    1 
ATOM   1094 C  C     . GLU A 1 138 ? 16.858  -7.857  9.644   1.00 45.24  ?  137 GLU A C     1 
ATOM   1095 O  O     . GLU A 1 138 ? 17.695  -8.751  9.813   1.00 48.26  ?  137 GLU A O     1 
ATOM   1096 C  CB    . GLU A 1 138 ? 17.905  -5.620  9.284   1.00 54.24  ?  137 GLU A CB    1 
ATOM   1097 C  CG    . GLU A 1 138 ? 18.287  -4.488  8.343   1.00 61.78  ?  137 GLU A CG    1 
ATOM   1098 C  CD    . GLU A 1 138 ? 19.356  -4.889  7.346   1.00 68.46  ?  137 GLU A CD    1 
ATOM   1099 O  OE1   . GLU A 1 138 ? 20.172  -5.780  7.670   1.00 71.75  ?  137 GLU A OE1   1 
ATOM   1100 O  OE2   . GLU A 1 138 ? 19.380  -4.314  6.237   1.00 70.64  -1 137 GLU A OE2   1 
ATOM   1101 N  N     . LEU A 1 139 ? 15.719  -7.812  10.325  1.00 39.58  ?  138 LEU A N     1 
ATOM   1102 C  CA    . LEU A 1 139 ? 15.366  -8.787  11.344  1.00 38.69  ?  138 LEU A CA    1 
ATOM   1103 C  C     . LEU A 1 139 ? 14.351  -9.808  10.855  1.00 35.92  ?  138 LEU A C     1 
ATOM   1104 O  O     . LEU A 1 139 ? 13.940  -10.671 11.633  1.00 37.99  ?  138 LEU A O     1 
ATOM   1105 C  CB    . LEU A 1 139 ? 14.818  -8.068  12.579  1.00 35.76  ?  138 LEU A CB    1 
ATOM   1106 C  CG    . LEU A 1 139 ? 15.744  -6.995  13.152  1.00 32.58  ?  138 LEU A CG    1 
ATOM   1107 C  CD1   . LEU A 1 139 ? 15.032  -6.202  14.234  1.00 29.26  ?  138 LEU A CD1   1 
ATOM   1108 C  CD2   . LEU A 1 139 ? 17.017  -7.643  13.696  1.00 32.77  ?  138 LEU A CD2   1 
ATOM   1109 N  N     . SER A 1 140 ? 13.946  -9.737  9.587   1.00 32.44  ?  139 SER A N     1 
ATOM   1110 C  CA    . SER A 1 140 ? 12.874  -10.573 9.064   1.00 33.92  ?  139 SER A CA    1 
ATOM   1111 C  C     . SER A 1 140 ? 13.304  -11.298 7.796   1.00 38.88  ?  139 SER A C     1 
ATOM   1112 O  O     . SER A 1 140 ? 12.477  -11.585 6.927   1.00 43.24  ?  139 SER A O     1 
ATOM   1113 C  CB    . SER A 1 140 ? 11.620  -9.738  8.810   1.00 30.38  ?  139 SER A CB    1 
ATOM   1114 O  OG    . SER A 1 140 ? 11.301  -8.972  9.960   1.00 29.53  ?  139 SER A OG    1 
ATOM   1115 N  N     . GLY A 1 141 ? 14.596  -11.592 7.672   1.00 38.73  ?  140 GLY A N     1 
ATOM   1116 C  CA    . GLY A 1 141 ? 15.073  -12.358 6.541   1.00 38.57  ?  140 GLY A CA    1 
ATOM   1117 C  C     . GLY A 1 141 ? 15.276  -11.574 5.268   1.00 39.69  ?  140 GLY A C     1 
ATOM   1118 O  O     . GLY A 1 141 ? 15.363  -12.176 4.193   1.00 40.96  ?  140 GLY A O     1 
ATOM   1119 N  N     . GLY A 1 142 ? 15.357  -10.248 5.350   1.00 38.65  ?  141 GLY A N     1 
ATOM   1120 C  CA    . GLY A 1 142 ? 15.629  -9.427  4.189   1.00 36.50  ?  141 GLY A CA    1 
ATOM   1121 C  C     . GLY A 1 142 ? 14.417  -9.013  3.384   1.00 35.69  ?  141 GLY A C     1 
ATOM   1122 O  O     . GLY A 1 142 ? 14.572  -8.302  2.386   1.00 34.51  ?  141 GLY A O     1 
ATOM   1123 N  N     . THR A 1 143 ? 13.218  -9.420  3.784   1.00 36.82  ?  142 THR A N     1 
ATOM   1124 C  CA    . THR A 1 143 ? 12.001  -9.092  3.060   1.00 38.00  ?  142 THR A CA    1 
ATOM   1125 C  C     . THR A 1 143 ? 11.205  -8.043  3.827   1.00 33.18  ?  142 THR A C     1 
ATOM   1126 O  O     . THR A 1 143 ? 11.135  -8.077  5.060   1.00 33.57  ?  142 THR A O     1 
ATOM   1127 C  CB    . THR A 1 143 ? 11.154  -10.348 2.824   1.00 42.70  ?  142 THR A CB    1 
ATOM   1128 O  OG1   . THR A 1 143 ? 9.969   -10.003 2.099   1.00 50.30  ?  142 THR A OG1   1 
ATOM   1129 C  CG2   . THR A 1 143 ? 10.767  -11.001 4.142   1.00 43.65  ?  142 THR A CG2   1 
ATOM   1130 N  N     . LEU A 1 144 ? 10.625  -7.096  3.094   1.00 28.50  ?  143 LEU A N     1 
ATOM   1131 C  CA    . LEU A 1 144 ? 9.746   -6.092  3.680   1.00 25.05  ?  143 LEU A CA    1 
ATOM   1132 C  C     . LEU A 1 144 ? 8.320   -6.631  3.686   1.00 23.93  ?  143 LEU A C     1 
ATOM   1133 O  O     . LEU A 1 144 ? 7.737   -6.861  2.623   1.00 22.89  ?  143 LEU A O     1 
ATOM   1134 C  CB    . LEU A 1 144 ? 9.819   -4.780  2.898   1.00 25.12  ?  143 LEU A CB    1 
ATOM   1135 C  CG    . LEU A 1 144 ? 9.004   -3.622  3.483   1.00 26.03  ?  143 LEU A CG    1 
ATOM   1136 C  CD1   . LEU A 1 144 ? 9.513   -3.261  4.867   1.00 25.26  ?  143 LEU A CD1   1 
ATOM   1137 C  CD2   . LEU A 1 144 ? 9.040   -2.406  2.565   1.00 27.72  ?  143 LEU A CD2   1 
ATOM   1138 N  N     . CYS A 1 145 ? 7.752   -6.817  4.874   1.00 23.75  ?  144 CYS A N     1 
ATOM   1139 C  CA    . CYS A 1 145 ? 6.430   -7.415  5.004   1.00 22.09  ?  144 CYS A CA    1 
ATOM   1140 C  C     . CYS A 1 145 ? 5.494   -6.463  5.728   1.00 22.26  ?  144 CYS A C     1 
ATOM   1141 O  O     . CYS A 1 145 ? 5.856   -5.890  6.761   1.00 25.42  ?  144 CYS A O     1 
ATOM   1142 C  CB    . CYS A 1 145 ? 6.497   -8.758  5.742   1.00 25.16  ?  144 CYS A CB    1 
ATOM   1143 S  SG    . CYS A 1 145 ? 7.379   -10.041 4.826   1.00 26.97  ?  144 CYS A SG    1 
ATOM   1144 N  N     . ILE A 1 146 ? 4.301   -6.307  5.179   1.00 19.17  ?  145 ILE A N     1 
ATOM   1145 C  CA    . ILE A 1 146 ? 3.228   -5.511  5.754   1.00 21.77  ?  145 ILE A CA    1 
ATOM   1146 C  C     . ILE A 1 146 ? 2.361   -6.418  6.620   1.00 24.37  ?  145 ILE A C     1 
ATOM   1147 O  O     . ILE A 1 146 ? 2.199   -7.616  6.343   1.00 26.99  ?  145 ILE A O     1 
ATOM   1148 C  CB    . ILE A 1 146 ? 2.417   -4.820  4.634   1.00 22.19  ?  145 ILE A CB    1 
ATOM   1149 C  CG1   . ILE A 1 146 ? 1.443   -3.794  5.211   1.00 19.18  ?  145 ILE A CG1   1 
ATOM   1150 C  CG2   . ILE A 1 146 ? 1.680   -5.845  3.782   1.00 21.94  ?  145 ILE A CG2   1 
ATOM   1151 C  CD1   . ILE A 1 146 ? 0.843   -2.880  4.163   1.00 23.38  ?  145 ILE A CD1   1 
ATOM   1152 N  N     . ALA A 1 147 ? 1.811   -5.847  7.687   1.00 23.58  ?  146 ALA A N     1 
ATOM   1153 C  CA    . ALA A 1 147 ? 0.991   -6.594  8.636   1.00 31.06  ?  146 ALA A CA    1 
ATOM   1154 C  C     . ALA A 1 147 ? -0.450  -6.644  8.133   1.00 31.50  ?  146 ALA A C     1 
ATOM   1155 O  O     . ALA A 1 147 ? -1.155  -5.630  8.156   1.00 28.30  ?  146 ALA A O     1 
ATOM   1156 C  CB    . ALA A 1 147 ? 1.071   -5.950  10.017  1.00 33.96  ?  146 ALA A CB    1 
ATOM   1157 N  N     . LYS A 1 148 ? -0.888  -7.818  7.680   1.00 29.66  ?  147 LYS A N     1 
ATOM   1158 C  CA    . LYS A 1 148 ? -2.204  -8.025  7.101   1.00 31.55  ?  147 LYS A CA    1 
ATOM   1159 C  C     . LYS A 1 148 ? -3.085  -8.781  8.085   1.00 34.31  ?  147 LYS A C     1 
ATOM   1160 O  O     . LYS A 1 148 ? -2.622  -9.709  8.761   1.00 32.68  ?  147 LYS A O     1 
ATOM   1161 C  CB    . LYS A 1 148 ? -2.101  -8.821  5.796   1.00 40.65  ?  147 LYS A CB    1 
ATOM   1162 C  CG    . LYS A 1 148 ? -2.749  -8.165  4.593   1.00 45.30  ?  147 LYS A CG    1 
ATOM   1163 C  CD    . LYS A 1 148 ? -1.881  -7.066  4.043   1.00 45.21  ?  147 LYS A CD    1 
ATOM   1164 C  CE    . LYS A 1 148 ? -2.547  -6.387  2.859   1.00 51.07  ?  147 LYS A CE    1 
ATOM   1165 N  NZ    . LYS A 1 148 ? -2.953  -7.336  1.787   1.00 55.93  1  147 LYS A NZ    1 
ATOM   1166 N  N     . GLY A 1 149 ? -4.357  -8.394  8.149   1.00 35.85  ?  148 GLY A N     1 
ATOM   1167 C  CA    . GLY A 1 149 ? -5.296  -9.052  9.035   1.00 41.64  ?  148 GLY A CA    1 
ATOM   1168 C  C     . GLY A 1 149 ? -5.840  -8.148  10.121  1.00 42.81  ?  148 GLY A C     1 
ATOM   1169 O  O     . GLY A 1 149 ? -5.203  -7.163  10.505  1.00 39.32  ?  148 GLY A O     1 
ATOM   1170 N  N     . LYS A 1 150 ? -7.029  -8.470  10.616  1.00 48.06  ?  149 LYS A N     1 
ATOM   1171 C  CA    . LYS A 1 150 ? -7.655  -7.756  11.717  1.00 52.15  ?  149 LYS A CA    1 
ATOM   1172 C  C     . LYS A 1 150 ? -8.120  -8.777  12.746  1.00 53.01  ?  149 LYS A C     1 
ATOM   1173 O  O     . LYS A 1 150 ? -7.956  -9.987  12.564  1.00 51.53  ?  149 LYS A O     1 
ATOM   1174 C  CB    . LYS A 1 150 ? -8.818  -6.885  11.224  1.00 54.87  ?  149 LYS A CB    1 
ATOM   1175 C  CG    . LYS A 1 150 ? -9.713  -7.582  10.211  1.00 57.37  ?  149 LYS A CG    1 
ATOM   1176 C  CD    . LYS A 1 150 ? -10.991 -6.801  9.940   1.00 58.39  ?  149 LYS A CD    1 
ATOM   1177 C  CE    . LYS A 1 150 ? -10.704 -5.446  9.325   1.00 57.28  ?  149 LYS A CE    1 
ATOM   1178 N  NZ    . LYS A 1 150 ? -11.955 -4.790  8.845   1.00 57.67  1  149 LYS A NZ    1 
ATOM   1179 N  N     . GLU A 1 151 ? -8.696  -8.283  13.845  1.00 58.36  ?  150 GLU A N     1 
ATOM   1180 C  CA    . GLU A 1 151 ? -9.245  -9.190  14.848  1.00 67.54  ?  150 GLU A CA    1 
ATOM   1181 C  C     . GLU A 1 151 ? -10.368 -10.033 14.262  1.00 74.43  ?  150 GLU A C     1 
ATOM   1182 O  O     . GLU A 1 151 ? -10.437 -11.245 14.496  1.00 75.35  ?  150 GLU A O     1 
ATOM   1183 C  CB    . GLU A 1 151 ? -9.750  -8.405  16.056  1.00 67.64  ?  150 GLU A CB    1 
ATOM   1184 C  CG    . GLU A 1 151 ? -8.739  -7.460  16.679  1.00 67.53  ?  150 GLU A CG    1 
ATOM   1185 C  CD    . GLU A 1 151 ? -8.857  -6.042  16.157  1.00 68.54  ?  150 GLU A CD    1 
ATOM   1186 O  OE1   . GLU A 1 151 ? -8.960  -5.865  14.924  1.00 68.17  ?  150 GLU A OE1   1 
ATOM   1187 O  OE2   . GLU A 1 151 ? -8.856  -5.105  16.984  1.00 69.19  -1 150 GLU A OE2   1 
ATOM   1188 N  N     . ASN A 1 152 ? -11.255 -9.405  13.490  1.00 82.54  ?  151 ASN A N     1 
ATOM   1189 C  CA    . ASN A 1 152 ? -12.353 -10.120 12.854  1.00 89.00  ?  151 ASN A CA    1 
ATOM   1190 C  C     . ASN A 1 152 ? -11.877 -11.027 11.727  1.00 90.88  ?  151 ASN A C     1 
ATOM   1191 O  O     . ASN A 1 152 ? -12.596 -11.963 11.360  1.00 91.04  ?  151 ASN A O     1 
ATOM   1192 C  CB    . ASN A 1 152 ? -13.378 -9.116  12.323  1.00 93.81  ?  151 ASN A CB    1 
ATOM   1193 C  CG    . ASN A 1 152 ? -14.642 -9.782  11.821  1.00 99.14  ?  151 ASN A CG    1 
ATOM   1194 O  OD1   . ASN A 1 152 ? -15.046 -10.832 12.321  1.00 102.64 ?  151 ASN A OD1   1 
ATOM   1195 N  ND2   . ASN A 1 152 ? -15.273 -9.173  10.825  1.00 99.95  ?  151 ASN A ND2   1 
ATOM   1196 N  N     . SER A 1 153 ? -10.686 -10.774 11.174  1.00 91.17  ?  152 SER A N     1 
ATOM   1197 C  CA    . SER A 1 153 ? -10.200 -11.570 10.051  1.00 89.59  ?  152 SER A CA    1 
ATOM   1198 C  C     . SER A 1 153 ? -10.059 -13.040 10.419  1.00 89.48  ?  152 SER A C     1 
ATOM   1199 O  O     . SER A 1 153 ? -10.282 -13.915 9.574   1.00 87.16  ?  152 SER A O     1 
ATOM   1200 C  CB    . SER A 1 153 ? -8.862  -11.020 9.553   1.00 87.13  ?  152 SER A CB    1 
ATOM   1201 N  N     . GLY A 1 154 ? -9.687  -13.333 11.663  1.00 91.99  ?  153 GLY A N     1 
ATOM   1202 C  CA    . GLY A 1 154 ? -9.624  -14.705 12.121  1.00 94.69  ?  153 GLY A CA    1 
ATOM   1203 C  C     . GLY A 1 154 ? -8.221  -15.243 12.305  1.00 96.24  ?  153 GLY A C     1 
ATOM   1204 O  O     . GLY A 1 154 ? -7.487  -14.798 13.193  1.00 95.82  ?  153 GLY A O     1 
ATOM   1205 N  N     . ASP A 1 155 ? -7.840  -16.207 11.467  1.00 98.18  ?  154 ASP A N     1 
ATOM   1206 C  CA    . ASP A 1 155 ? -6.566  -16.901 11.611  1.00 99.57  ?  154 ASP A CA    1 
ATOM   1207 C  C     . ASP A 1 155 ? -5.890  -17.081 10.257  1.00 98.96  ?  154 ASP A C     1 
ATOM   1208 O  O     . ASP A 1 155 ? -4.665  -16.971 10.145  1.00 97.26  ?  154 ASP A O     1 
ATOM   1209 C  CB    . ASP A 1 155 ? -6.784  -18.259 12.284  1.00 101.35 ?  154 ASP A CB    1 
ATOM   1210 C  CG    . ASP A 1 155 ? -5.488  -18.998 12.549  1.00 102.23 ?  154 ASP A CG    1 
ATOM   1211 O  OD1   . ASP A 1 155 ? -4.423  -18.348 12.585  1.00 101.88 ?  154 ASP A OD1   1 
ATOM   1212 O  OD2   . ASP A 1 155 ? -5.538  -20.236 12.719  1.00 103.27 -1 154 ASP A OD2   1 
ATOM   1213 N  N     . GLU A 1 156 ? -6.686  -17.355 9.222   1.00 101.41 ?  155 GLU A N     1 
ATOM   1214 C  CA    . GLU A 1 156 ? -6.137  -17.611 7.895   1.00 102.51 ?  155 GLU A CA    1 
ATOM   1215 C  C     . GLU A 1 156 ? -5.759  -16.326 7.169   1.00 100.02 ?  155 GLU A C     1 
ATOM   1216 O  O     . GLU A 1 156 ? -4.800  -16.322 6.387   1.00 99.44  ?  155 GLU A O     1 
ATOM   1217 C  CB    . GLU A 1 156 ? -7.145  -18.405 7.062   1.00 105.98 ?  155 GLU A CB    1 
ATOM   1218 C  CG    . GLU A 1 156 ? -6.622  -18.889 5.719   1.00 107.54 ?  155 GLU A CG    1 
ATOM   1219 C  CD    . GLU A 1 156 ? -7.717  -19.488 4.855   1.00 109.13 ?  155 GLU A CD    1 
ATOM   1220 O  OE1   . GLU A 1 156 ? -8.816  -18.896 4.792   1.00 109.38 ?  155 GLU A OE1   1 
ATOM   1221 O  OE2   . GLU A 1 156 ? -7.482  -20.554 4.247   1.00 109.37 -1 155 GLU A OE2   1 
ATOM   1222 N  N     . HIS A 1 157 ? -6.488  -15.236 7.409   1.00 97.37  ?  156 HIS A N     1 
ATOM   1223 C  CA    . HIS A 1 157 ? -6.269  -13.969 6.722   1.00 91.87  ?  156 HIS A CA    1 
ATOM   1224 C  C     . HIS A 1 157 ? -5.375  -13.023 7.517   1.00 82.17  ?  156 HIS A C     1 
ATOM   1225 O  O     . HIS A 1 157 ? -5.475  -11.801 7.366   1.00 82.21  ?  156 HIS A O     1 
ATOM   1226 C  CB    . HIS A 1 157 ? -7.609  -13.300 6.416   1.00 97.09  ?  156 HIS A CB    1 
ATOM   1227 C  CG    . HIS A 1 157 ? -8.535  -14.149 5.602   1.00 102.21 ?  156 HIS A CG    1 
ATOM   1228 N  ND1   . HIS A 1 157 ? -8.099  -15.224 4.857   1.00 103.31 ?  156 HIS A ND1   1 
ATOM   1229 C  CD2   . HIS A 1 157 ? -9.875  -14.083 5.417   1.00 104.03 ?  156 HIS A CD2   1 
ATOM   1230 C  CE1   . HIS A 1 157 ? -9.129  -15.782 4.247   1.00 103.82 ?  156 HIS A CE1   1 
ATOM   1231 N  NE2   . HIS A 1 157 ? -10.219 -15.109 4.570   1.00 103.99 ?  156 HIS A NE2   1 
ATOM   1232 N  N     . ARG A 1 158 ? -4.493  -13.567 8.353   1.00 71.01  ?  157 ARG A N     1 
ATOM   1233 C  CA    . ARG A 1 158 ? -3.644  -12.779 9.242   1.00 61.14  ?  157 ARG A CA    1 
ATOM   1234 C  C     . ARG A 1 158 ? -2.197  -13.208 9.031   1.00 51.60  ?  157 ARG A C     1 
ATOM   1235 O  O     . ARG A 1 158 ? -1.820  -14.323 9.405   1.00 53.03  ?  157 ARG A O     1 
ATOM   1236 C  CB    . ARG A 1 158 ? -4.069  -12.974 10.697  1.00 60.89  ?  157 ARG A CB    1 
ATOM   1237 C  CG    . ARG A 1 158 ? -3.176  -12.303 11.711  1.00 61.49  ?  157 ARG A CG    1 
ATOM   1238 C  CD    . ARG A 1 158 ? -3.557  -12.722 13.120  1.00 63.13  ?  157 ARG A CD    1 
ATOM   1239 N  NE    . ARG A 1 158 ? -4.978  -12.527 13.394  1.00 62.68  ?  157 ARG A NE    1 
ATOM   1240 C  CZ    . ARG A 1 158 ? -5.517  -12.581 14.608  1.00 62.63  ?  157 ARG A CZ    1 
ATOM   1241 N  NH1   . ARG A 1 158 ? -6.821  -12.394 14.767  1.00 61.94  1  157 ARG A NH1   1 
ATOM   1242 N  NH2   . ARG A 1 158 ? -4.751  -12.816 15.665  1.00 63.49  ?  157 ARG A NH2   1 
ATOM   1243 N  N     . LEU A 1 159 ? -1.383  -12.333 8.442   1.00 39.87  ?  158 LEU A N     1 
ATOM   1244 C  CA    . LEU A 1 159 ? -0.038  -12.743 8.059   1.00 36.96  ?  158 LEU A CA    1 
ATOM   1245 C  C     . LEU A 1 159 ? 0.837   -11.523 7.798   1.00 33.49  ?  158 LEU A C     1 
ATOM   1246 O  O     . LEU A 1 159 ? 0.359   -10.399 7.636   1.00 31.12  ?  158 LEU A O     1 
ATOM   1247 C  CB    . LEU A 1 159 ? -0.067  -13.643 6.819   1.00 37.66  ?  158 LEU A CB    1 
ATOM   1248 C  CG    . LEU A 1 159 ? -0.549  -12.995 5.518   1.00 38.82  ?  158 LEU A CG    1 
ATOM   1249 C  CD1   . LEU A 1 159 ? 0.206   -13.576 4.330   1.00 42.24  ?  158 LEU A CD1   1 
ATOM   1250 C  CD2   . LEU A 1 159 ? -2.054  -13.169 5.335   1.00 35.76  ?  158 LEU A CD2   1 
ATOM   1251 N  N     . TRP A 1 160 ? 2.141   -11.770 7.753   1.00 33.87  ?  159 TRP A N     1 
ATOM   1252 C  CA    . TRP A 1 160 ? 3.103   -10.787 7.272   1.00 34.01  ?  159 TRP A CA    1 
ATOM   1253 C  C     . TRP A 1 160 ? 3.293   -11.031 5.780   1.00 33.58  ?  159 TRP A C     1 
ATOM   1254 O  O     . TRP A 1 160 ? 3.880   -12.043 5.380   1.00 37.06  ?  159 TRP A O     1 
ATOM   1255 C  CB    . TRP A 1 160 ? 4.424   -10.902 8.027   1.00 29.84  ?  159 TRP A CB    1 
ATOM   1256 C  CG    . TRP A 1 160 ? 4.356   -10.474 9.463   1.00 29.55  ?  159 TRP A CG    1 
ATOM   1257 C  CD1   . TRP A 1 160 ? 4.239   -11.283 10.558  1.00 32.46  ?  159 TRP A CD1   1 
ATOM   1258 C  CD2   . TRP A 1 160 ? 4.417   -9.130  9.962   1.00 28.30  ?  159 TRP A CD2   1 
ATOM   1259 N  NE1   . TRP A 1 160 ? 4.215   -10.525 11.708  1.00 34.02  ?  159 TRP A NE1   1 
ATOM   1260 C  CE2   . TRP A 1 160 ? 4.329   -9.202  11.369  1.00 33.32  ?  159 TRP A CE2   1 
ATOM   1261 C  CE3   . TRP A 1 160 ? 4.531   -7.875  9.355   1.00 28.85  ?  159 TRP A CE3   1 
ATOM   1262 C  CZ2   . TRP A 1 160 ? 4.351   -8.067  12.176  1.00 33.37  ?  159 TRP A CZ2   1 
ATOM   1263 C  CZ3   . TRP A 1 160 ? 4.556   -6.749  10.159  1.00 30.33  ?  159 TRP A CZ3   1 
ATOM   1264 C  CH2   . TRP A 1 160 ? 4.466   -6.853  11.555  1.00 32.29  ?  159 TRP A CH2   1 
ATOM   1265 N  N     . GLN A 1 161 ? 2.798   -10.119 4.953   1.00 29.67  ?  160 GLN A N     1 
ATOM   1266 C  CA    . GLN A 1 161 ? 2.824   -10.309 3.508   1.00 26.29  ?  160 GLN A CA    1 
ATOM   1267 C  C     . GLN A 1 161 ? 3.950   -9.503  2.881   1.00 24.78  ?  160 GLN A C     1 
ATOM   1268 O  O     . GLN A 1 161 ? 4.114   -8.319  3.186   1.00 24.89  ?  160 GLN A O     1 
ATOM   1269 C  CB    . GLN A 1 161 ? 1.490   -9.907  2.876   1.00 27.69  ?  160 GLN A CB    1 
ATOM   1270 C  CG    . GLN A 1 161 ? 1.367   -10.340 1.422   1.00 31.99  ?  160 GLN A CG    1 
ATOM   1271 C  CD    . GLN A 1 161 ? 0.079   -9.873  0.787   1.00 36.82  ?  160 GLN A CD    1 
ATOM   1272 O  OE1   . GLN A 1 161 ? -0.375  -8.755  1.031   1.00 36.08  ?  160 GLN A OE1   1 
ATOM   1273 N  NE2   . GLN A 1 161 ? -0.521  -10.730 -0.035  1.00 38.59  ?  160 GLN A NE2   1 
ATOM   1274 N  N     . ILE A 1 162 ? 4.707   -10.144 1.985   1.00 23.25  ?  161 ILE A N     1 
ATOM   1275 C  CA    . ILE A 1 162 ? 5.754   -9.438  1.258   1.00 21.74  ?  161 ILE A CA    1 
ATOM   1276 C  C     . ILE A 1 162 ? 5.147   -8.262  0.507   1.00 21.51  ?  161 ILE A C     1 
ATOM   1277 O  O     . ILE A 1 162 ? 4.067   -8.361  -0.093  1.00 23.91  ?  161 ILE A O     1 
ATOM   1278 C  CB    . ILE A 1 162 ? 6.497   -10.397 0.313   1.00 26.25  ?  161 ILE A CB    1 
ATOM   1279 C  CG1   . ILE A 1 162 ? 7.600   -9.655  -0.448  1.00 29.15  ?  161 ILE A CG1   1 
ATOM   1280 C  CG2   . ILE A 1 162 ? 5.527   -11.074 -0.648  1.00 26.08  ?  161 ILE A CG2   1 
ATOM   1281 C  CD1   . ILE A 1 162 ? 8.621   -10.580 -1.089  1.00 36.97  ?  161 ILE A CD1   1 
ATOM   1282 N  N     . SER A 1 163 ? 5.835   -7.126  0.563   1.00 20.05  ?  162 SER A N     1 
ATOM   1283 C  CA    . SER A 1 163 ? 5.301   -5.865  0.074   1.00 23.20  ?  162 SER A CA    1 
ATOM   1284 C  C     . SER A 1 163 ? 6.447   -5.054  -0.518  1.00 22.30  ?  162 SER A C     1 
ATOM   1285 O  O     . SER A 1 163 ? 7.609   -5.232  -0.138  1.00 22.81  ?  162 SER A O     1 
ATOM   1286 C  CB    . SER A 1 163 ? 4.601   -5.105  1.217   1.00 27.02  ?  162 SER A CB    1 
ATOM   1287 O  OG    . SER A 1 163 ? 3.952   -3.931  0.769   1.00 32.86  ?  162 SER A OG    1 
ATOM   1288 N  N     . ASP A 1 164 ? 6.117   -4.174  -1.467  1.00 19.55  ?  163 ASP A N     1 
ATOM   1289 C  CA    . ASP A 1 164 ? 7.149   -3.364  -2.107  1.00 20.43  ?  163 ASP A CA    1 
ATOM   1290 C  C     . ASP A 1 164 ? 6.588   -2.000  -2.493  1.00 19.40  ?  163 ASP A C     1 
ATOM   1291 O  O     . ASP A 1 164 ? 6.547   -1.664  -3.682  1.00 19.94  ?  163 ASP A O     1 
ATOM   1292 C  CB    . ASP A 1 164 ? 7.708   -4.078  -3.343  1.00 20.42  ?  163 ASP A CB    1 
ATOM   1293 C  CG    . ASP A 1 164 ? 8.974   -3.418  -3.885  1.00 23.50  ?  163 ASP A CG    1 
ATOM   1294 O  OD1   . ASP A 1 164 ? 9.550   -2.553  -3.188  1.00 21.73  ?  163 ASP A OD1   1 
ATOM   1295 O  OD2   . ASP A 1 164 ? 9.395   -3.764  -5.010  1.00 23.27  -1 163 ASP A OD2   1 
ATOM   1296 N  N     . PRO A 1 165 ? 6.149   -1.188  -1.525  1.00 22.50  ?  164 PRO A N     1 
ATOM   1297 C  CA    . PRO A 1 165 ? 5.548   0.105   -1.891  1.00 23.90  ?  164 PRO A CA    1 
ATOM   1298 C  C     . PRO A 1 165 ? 6.534   1.069   -2.519  1.00 22.66  ?  164 PRO A C     1 
ATOM   1299 O  O     . PRO A 1 165 ? 6.158   1.838   -3.414  1.00 20.08  ?  164 PRO A O     1 
ATOM   1300 C  CB    . PRO A 1 165 ? 5.012   0.631   -0.551  1.00 22.37  ?  164 PRO A CB    1 
ATOM   1301 C  CG    . PRO A 1 165 ? 5.894   -0.021  0.479   1.00 20.93  ?  164 PRO A CG    1 
ATOM   1302 C  CD    . PRO A 1 165 ? 6.159   -1.398  -0.064  1.00 22.24  ?  164 PRO A CD    1 
ATOM   1303 N  N     . GLN A 1 166 ? 7.787   1.068   -2.074  1.00 20.76  ?  165 GLN A N     1 
ATOM   1304 C  CA    . GLN A 1 166 ? 8.748   1.970   -2.692  1.00 24.79  ?  165 GLN A CA    1 
ATOM   1305 C  C     . GLN A 1 166 ? 9.123   1.497   -4.091  1.00 22.72  ?  165 GLN A C     1 
ATOM   1306 O  O     . GLN A 1 166 ? 9.354   2.324   -4.972  1.00 22.65  ?  165 GLN A O     1 
ATOM   1307 C  CB    . GLN A 1 166 ? 9.977   2.129   -1.792  1.00 29.14  ?  165 GLN A CB    1 
ATOM   1308 C  CG    . GLN A 1 166 ? 9.617   2.787   -0.462  1.00 34.18  ?  165 GLN A CG    1 
ATOM   1309 C  CD    . GLN A 1 166 ? 10.819  3.300   0.303   1.00 39.34  ?  165 GLN A CD    1 
ATOM   1310 O  OE1   . GLN A 1 166 ? 11.713  2.535   0.658   1.00 45.02  ?  165 GLN A OE1   1 
ATOM   1311 N  NE2   . GLN A 1 166 ? 10.844  4.605   0.562   1.00 36.28  ?  165 GLN A NE2   1 
ATOM   1312 N  N     . GLY A 1 167 ? 9.147   0.180   -4.323  1.00 21.40  ?  166 GLY A N     1 
ATOM   1313 C  CA    . GLY A 1 167 ? 9.309   -0.315  -5.680  1.00 16.41  ?  166 GLY A CA    1 
ATOM   1314 C  C     . GLY A 1 167 ? 8.168   0.114   -6.588  1.00 15.37  ?  166 GLY A C     1 
ATOM   1315 O  O     . GLY A 1 167 ? 8.390   0.512   -7.733  1.00 16.81  ?  166 GLY A O     1 
ATOM   1316 N  N     . PHE A 1 168 ? 6.932   0.054   -6.084  1.00 13.80  ?  167 PHE A N     1 
ATOM   1317 C  CA    . PHE A 1 168 ? 5.798   0.526   -6.870  1.00 15.60  ?  167 PHE A CA    1 
ATOM   1318 C  C     . PHE A 1 168 ? 5.917   2.015   -7.164  1.00 14.13  ?  167 PHE A C     1 
ATOM   1319 O  O     . PHE A 1 168 ? 5.683   2.457   -8.298  1.00 15.66  ?  167 PHE A O     1 
ATOM   1320 C  CB    . PHE A 1 168 ? 4.483   0.239   -6.142  1.00 18.67  ?  167 PHE A CB    1 
ATOM   1321 C  CG    . PHE A 1 168 ? 3.279   0.699   -6.901  1.00 18.82  ?  167 PHE A CG    1 
ATOM   1322 C  CD1   . PHE A 1 168 ? 2.998   0.176   -8.155  1.00 18.61  ?  167 PHE A CD1   1 
ATOM   1323 C  CD2   . PHE A 1 168 ? 2.442   1.664   -6.381  1.00 19.81  ?  167 PHE A CD2   1 
ATOM   1324 C  CE1   . PHE A 1 168 ? 1.901   0.609   -8.874  1.00 19.59  ?  167 PHE A CE1   1 
ATOM   1325 C  CE2   . PHE A 1 168 ? 1.343   2.099   -7.097  1.00 20.73  ?  167 PHE A CE2   1 
ATOM   1326 C  CZ    . PHE A 1 168 ? 1.069   1.569   -8.341  1.00 19.76  ?  167 PHE A CZ    1 
ATOM   1327 N  N     . GLN A 1 169 ? 6.276   2.806   -6.151  1.00 14.30  ?  168 GLN A N     1 
ATOM   1328 C  CA    . GLN A 1 169 ? 6.405   4.243   -6.351  1.00 18.38  ?  168 GLN A CA    1 
ATOM   1329 C  C     . GLN A 1 169 ? 7.494   4.549   -7.368  1.00 18.69  ?  168 GLN A C     1 
ATOM   1330 O  O     . GLN A 1 169 ? 7.334   5.436   -8.218  1.00 17.32  ?  168 GLN A O     1 
ATOM   1331 C  CB    . GLN A 1 169 ? 6.692   4.925   -5.012  1.00 21.54  ?  168 GLN A CB    1 
ATOM   1332 C  CG    . GLN A 1 169 ? 5.517   4.853   -4.041  1.00 21.91  ?  168 GLN A CG    1 
ATOM   1333 C  CD    . GLN A 1 169 ? 5.931   5.078   -2.597  1.00 27.26  ?  168 GLN A CD    1 
ATOM   1334 O  OE1   . GLN A 1 169 ? 5.387   4.455   -1.685  1.00 29.69  ?  168 GLN A OE1   1 
ATOM   1335 N  NE2   . GLN A 1 169 ? 6.897   5.968   -2.383  1.00 27.54  ?  168 GLN A NE2   1 
ATOM   1336 N  N     . ASP A 1 170 ? 8.610   3.817   -7.290  1.00 17.35  ?  169 ASP A N     1 
ATOM   1337 C  CA    . ASP A 1 170 ? 9.675   3.949   -8.271  1.00 17.05  ?  169 ASP A CA    1 
ATOM   1338 C  C     . ASP A 1 170 ? 9.176   3.611   -9.668  1.00 17.59  ?  169 ASP A C     1 
ATOM   1339 O  O     . ASP A 1 170 ? 9.531   4.289   -10.641 1.00 16.11  ?  169 ASP A O     1 
ATOM   1340 C  CB    . ASP A 1 170 ? 10.846  3.042   -7.883  1.00 18.39  ?  169 ASP A CB    1 
ATOM   1341 C  CG    . ASP A 1 170 ? 11.989  3.116   -8.871  1.00 26.15  ?  169 ASP A CG    1 
ATOM   1342 O  OD1   . ASP A 1 170 ? 12.401  4.240   -9.228  1.00 25.03  ?  169 ASP A OD1   1 
ATOM   1343 O  OD2   . ASP A 1 170 ? 12.470  2.047   -9.296  1.00 30.43  -1 169 ASP A OD2   1 
ATOM   1344 N  N     . ARG A 1 171 ? 8.349   2.567   -9.785  1.00 15.15  ?  170 ARG A N     1 
ATOM   1345 C  CA    . ARG A 1 171 ? 7.805   2.198   -11.091 1.00 18.59  ?  170 ARG A CA    1 
ATOM   1346 C  C     . ARG A 1 171 ? 6.941   3.313   -11.666 1.00 17.84  ?  170 ARG A C     1 
ATOM   1347 O  O     . ARG A 1 171 ? 7.003   3.608   -12.866 1.00 15.76  ?  170 ARG A O     1 
ATOM   1348 C  CB    . ARG A 1 171 ? 7.002   0.903   -10.975 1.00 19.30  ?  170 ARG A CB    1 
ATOM   1349 C  CG    . ARG A 1 171 ? 7.859   -0.329  -10.725 1.00 26.82  ?  170 ARG A CG    1 
ATOM   1350 C  CD    . ARG A 1 171 ? 8.208   -1.057  -12.008 1.00 29.68  ?  170 ARG A CD    1 
ATOM   1351 N  NE    . ARG A 1 171 ? 9.381   -1.912  -11.839 1.00 32.71  ?  170 ARG A NE    1 
ATOM   1352 C  CZ    . ARG A 1 171 ? 9.846   -2.739  -12.772 1.00 32.68  ?  170 ARG A CZ    1 
ATOM   1353 N  NH1   . ARG A 1 171 ? 9.226   -2.842  -13.945 1.00 29.17  1  170 ARG A NH1   1 
ATOM   1354 N  NH2   . ARG A 1 171 ? 10.932  -3.466  -12.531 1.00 28.51  ?  170 ARG A NH2   1 
ATOM   1355 N  N     . ILE A 1 172 ? 6.131   3.946   -10.821 1.00 16.73  ?  171 ILE A N     1 
ATOM   1356 C  CA    . ILE A 1 172 ? 5.276   5.022   -11.308 1.00 14.62  ?  171 ILE A CA    1 
ATOM   1357 C  C     . ILE A 1 172 ? 6.110   6.239   -11.692 1.00 20.34  ?  171 ILE A C     1 
ATOM   1358 O  O     . ILE A 1 172 ? 5.834   6.904   -12.699 1.00 20.50  ?  171 ILE A O     1 
ATOM   1359 C  CB    . ILE A 1 172 ? 4.203   5.371   -10.261 1.00 13.63  ?  171 ILE A CB    1 
ATOM   1360 C  CG1   . ILE A 1 172 ? 3.308   4.161   -10.002 1.00 14.64  ?  171 ILE A CG1   1 
ATOM   1361 C  CG2   . ILE A 1 172 ? 3.369   6.570   -10.727 1.00 16.32  ?  171 ILE A CG2   1 
ATOM   1362 C  CD1   . ILE A 1 172 ? 2.579   3.673   -11.240 1.00 11.93  ?  171 ILE A CD1   1 
ATOM   1363 N  N     . ALA A 1 173 ? 7.142   6.549   -10.904 1.00 19.25  ?  172 ALA A N     1 
ATOM   1364 C  CA    . ALA A 1 173 ? 7.990   7.697   -11.212 1.00 19.86  ?  172 ALA A CA    1 
ATOM   1365 C  C     . ALA A 1 173 ? 8.855   7.462   -12.447 1.00 18.58  ?  172 ALA A C     1 
ATOM   1366 O  O     . ALA A 1 173 ? 9.204   8.416   -13.150 1.00 21.12  ?  172 ALA A O     1 
ATOM   1367 C  CB    . ALA A 1 173 ? 8.882   8.031   -10.014 1.00 20.44  ?  172 ALA A CB    1 
ATOM   1368 N  N     . SER A 1 174 ? 9.206   6.215   -12.735 1.00 18.82  ?  173 SER A N     1 
ATOM   1369 C  CA    . SER A 1 174 ? 10.240  5.931   -13.719 1.00 17.47  ?  173 SER A CA    1 
ATOM   1370 C  C     . SER A 1 174 ? 9.696   5.551   -15.088 1.00 19.00  ?  173 SER A C     1 
ATOM   1371 O  O     . SER A 1 174 ? 10.478  5.494   -16.044 1.00 22.32  ?  173 SER A O     1 
ATOM   1372 C  CB    . SER A 1 174 ? 11.148  4.803   -13.215 1.00 20.29  ?  173 SER A CB    1 
ATOM   1373 O  OG    . SER A 1 174 ? 11.760  5.168   -11.997 1.00 22.35  ?  173 SER A OG    1 
ATOM   1374 N  N     . LYS A 1 175 ? 8.391   5.285   -15.209 1.00 17.01  ?  174 LYS A N     1 
ATOM   1375 C  CA    . LYS A 1 175 ? 7.858   4.781   -16.472 1.00 17.55  ?  174 LYS A CA    1 
ATOM   1376 C  C     . LYS A 1 175 ? 8.178   5.727   -17.618 1.00 20.42  ?  174 LYS A C     1 
ATOM   1377 O  O     . LYS A 1 175 ? 8.501   5.287   -18.728 1.00 21.71  ?  174 LYS A O     1 
ATOM   1378 C  CB    . LYS A 1 175 ? 6.349   4.576   -16.362 1.00 19.21  ?  174 LYS A CB    1 
ATOM   1379 C  CG    . LYS A 1 175 ? 5.703   4.066   -17.641 1.00 19.00  ?  174 LYS A CG    1 
ATOM   1380 C  CD    . LYS A 1 175 ? 4.189   3.990   -17.485 1.00 21.08  ?  174 LYS A CD    1 
ATOM   1381 C  CE    . LYS A 1 175 ? 3.489   3.737   -18.813 1.00 21.17  ?  174 LYS A CE    1 
ATOM   1382 N  NZ    . LYS A 1 175 ? 3.820   2.405   -19.398 1.00 23.16  1  174 LYS A NZ    1 
ATOM   1383 N  N     . LEU A 1 176 ? 8.112   7.032   -17.354 1.00 18.06  ?  175 LEU A N     1 
ATOM   1384 C  CA    . LEU A 1 176 ? 8.358   8.076   -18.333 1.00 20.17  ?  175 LEU A CA    1 
ATOM   1385 C  C     . LEU A 1 176 ? 9.139   9.180   -17.631 1.00 18.49  ?  175 LEU A C     1 
ATOM   1386 O  O     . LEU A 1 176 ? 9.389   9.114   -16.424 1.00 18.27  ?  175 LEU A O     1 
ATOM   1387 C  CB    . LEU A 1 176 ? 7.035   8.601   -18.917 1.00 17.94  ?  175 LEU A CB    1 
ATOM   1388 C  CG    . LEU A 1 176 ? 6.154   7.597   -19.674 1.00 16.16  ?  175 LEU A CG    1 
ATOM   1389 C  CD1   . LEU A 1 176 ? 4.695   8.062   -19.715 1.00 14.10  ?  175 LEU A CD1   1 
ATOM   1390 C  CD2   . LEU A 1 176 ? 6.682   7.394   -21.086 1.00 16.11  ?  175 LEU A CD2   1 
ATOM   1391 N  N     . SER A 1 177 ? 9.514   10.214  -18.377 1.00 15.09  ?  176 SER A N     1 
ATOM   1392 C  CA    . SER A 1 177 ? 10.225  11.339  -17.785 1.00 18.11  ?  176 SER A CA    1 
ATOM   1393 C  C     . SER A 1 177 ? 9.655   12.633  -18.341 1.00 17.73  ?  176 SER A C     1 
ATOM   1394 O  O     . SER A 1 177 ? 8.922   12.634  -19.330 1.00 14.89  ?  176 SER A O     1 
ATOM   1395 C  CB    . SER A 1 177 ? 11.735  11.254  -18.053 1.00 19.40  ?  176 SER A CB    1 
ATOM   1396 O  OG    . SER A 1 177 ? 12.016  11.423  -19.432 1.00 20.94  ?  176 SER A OG    1 
ATOM   1397 N  N     . GLY A 1 178 ? 9.990   13.742  -17.678 1.00 15.87  ?  177 GLY A N     1 
ATOM   1398 C  CA    . GLY A 1 178 ? 9.696   15.062  -18.221 1.00 17.59  ?  177 GLY A CA    1 
ATOM   1399 C  C     . GLY A 1 178 ? 8.214   15.305  -18.441 1.00 17.59  ?  177 GLY A C     1 
ATOM   1400 O  O     . GLY A 1 178 ? 7.362   14.923  -17.629 1.00 15.68  ?  177 GLY A O     1 
ATOM   1401 N  N     . ASP A 1 179 ? 7.900   15.964  -19.562 1.00 18.81  ?  178 ASP A N     1 
ATOM   1402 C  CA    . ASP A 1 179 ? 6.513   16.287  -19.876 1.00 20.49  ?  178 ASP A CA    1 
ATOM   1403 C  C     . ASP A 1 179 ? 5.694   15.055  -20.262 1.00 18.69  ?  178 ASP A C     1 
ATOM   1404 O  O     . ASP A 1 179 ? 4.466   15.076  -20.119 1.00 16.63  ?  178 ASP A O     1 
ATOM   1405 C  CB    . ASP A 1 179 ? 6.456   17.328  -20.996 1.00 17.42  ?  178 ASP A CB    1 
ATOM   1406 C  CG    . ASP A 1 179 ? 7.073   18.661  -20.596 1.00 24.06  ?  178 ASP A CG    1 
ATOM   1407 O  OD1   . ASP A 1 179 ? 7.198   18.928  -19.380 1.00 24.02  ?  178 ASP A OD1   1 
ATOM   1408 O  OD2   . ASP A 1 179 ? 7.421   19.443  -21.506 1.00 25.23  -1 178 ASP A OD2   1 
ATOM   1409 N  N     . ASP A 1 180 ? 6.333   13.984  -20.742 1.00 19.27  ?  179 ASP A N     1 
ATOM   1410 C  CA    . ASP A 1 180 ? 5.610   12.725  -20.922 1.00 19.23  ?  179 ASP A CA    1 
ATOM   1411 C  C     . ASP A 1 180 ? 5.053   12.230  -19.591 1.00 16.64  ?  179 ASP A C     1 
ATOM   1412 O  O     . ASP A 1 180 ? 3.874   11.850  -19.484 1.00 15.33  ?  179 ASP A O     1 
ATOM   1413 C  CB    . ASP A 1 180 ? 6.530   11.659  -21.516 1.00 20.52  ?  179 ASP A CB    1 
ATOM   1414 C  CG    . ASP A 1 180 ? 6.915   11.930  -22.954 1.00 24.14  ?  179 ASP A CG    1 
ATOM   1415 O  OD1   . ASP A 1 180 ? 6.381   12.873  -23.574 1.00 22.21  ?  179 ASP A OD1   1 
ATOM   1416 O  OD2   . ASP A 1 180 ? 7.762   11.168  -23.465 1.00 23.40  -1 179 ASP A OD2   1 
ATOM   1417 N  N     . ALA A 1 181 ? 5.911   12.200  -18.569 1.00 15.08  ?  180 ALA A N     1 
ATOM   1418 C  CA    . ALA A 1 181 ? 5.484   11.790  -17.237 1.00 18.31  ?  180 ALA A CA    1 
ATOM   1419 C  C     . ALA A 1 181 ? 4.462   12.761  -16.672 1.00 16.27  ?  180 ALA A C     1 
ATOM   1420 O  O     . ALA A 1 181 ? 3.558   12.355  -15.930 1.00 14.81  ?  180 ALA A O     1 
ATOM   1421 C  CB    . ALA A 1 181 ? 6.693   11.683  -16.306 1.00 17.31  ?  180 ALA A CB    1 
ATOM   1422 N  N     . ALA A 1 182 ? 4.583   14.043  -17.023 1.00 17.79  ?  181 ALA A N     1 
ATOM   1423 C  CA    . ALA A 1 182 ? 3.555   15.005  -16.638 1.00 19.71  ?  181 ALA A CA    1 
ATOM   1424 C  C     . ALA A 1 182 ? 2.189   14.602  -17.193 1.00 18.43  ?  181 ALA A C     1 
ATOM   1425 O  O     . ALA A 1 182 ? 1.187   14.614  -16.469 1.00 16.26  ?  181 ALA A O     1 
ATOM   1426 C  CB    . ALA A 1 182 ? 3.947   16.408  -17.110 1.00 17.18  ?  181 ALA A CB    1 
ATOM   1427 N  N     . GLN A 1 183 ? 2.125   14.246  -18.483 1.00 11.32  ?  182 GLN A N     1 
ATOM   1428 C  CA    . GLN A 1 183 ? 0.827   13.859  -19.044 1.00 15.66  ?  182 GLN A CA    1 
ATOM   1429 C  C     . GLN A 1 183 ? 0.296   12.585  -18.383 1.00 17.06  ?  182 GLN A C     1 
ATOM   1430 O  O     . GLN A 1 183 ? -0.904  12.472  -18.099 1.00 14.70  ?  182 GLN A O     1 
ATOM   1431 C  CB    . GLN A 1 183 ? 0.919   13.674  -20.558 1.00 14.93  ?  182 GLN A CB    1 
ATOM   1432 C  CG    . GLN A 1 183 ? -0.454  13.509  -21.204 1.00 15.81  ?  182 GLN A CG    1 
ATOM   1433 C  CD    . GLN A 1 183 ? -0.388  13.213  -22.684 1.00 18.16  ?  182 GLN A CD    1 
ATOM   1434 O  OE1   . GLN A 1 183 ? 0.337   12.316  -23.123 1.00 16.71  ?  182 GLN A OE1   1 
ATOM   1435 N  NE2   . GLN A 1 183 ? -1.151  13.966  -23.465 1.00 18.10  ?  182 GLN A NE2   1 
ATOM   1436 N  N     . PHE A 1 184 ? 1.180   11.610  -18.159 1.00 16.02  ?  183 PHE A N     1 
ATOM   1437 C  CA    . PHE A 1 184 ? 0.838   10.391  -17.421 1.00 16.99  ?  183 PHE A CA    1 
ATOM   1438 C  C     . PHE A 1 184 ? 0.156   10.718  -16.087 1.00 18.25  ?  183 PHE A C     1 
ATOM   1439 O  O     . PHE A 1 184 ? -0.959  10.242  -15.796 1.00 14.37  ?  183 PHE A O     1 
ATOM   1440 C  CB    . PHE A 1 184 ? 2.145   9.603   -17.243 1.00 16.94  ?  183 PHE A CB    1 
ATOM   1441 C  CG    . PHE A 1 184 ? 2.065   8.378   -16.379 1.00 19.26  ?  183 PHE A CG    1 
ATOM   1442 C  CD1   . PHE A 1 184 ? 1.331   7.264   -16.762 1.00 16.99  ?  183 PHE A CD1   1 
ATOM   1443 C  CD2   . PHE A 1 184 ? 2.851   8.294   -15.235 1.00 14.66  ?  183 PHE A CD2   1 
ATOM   1444 C  CE1   . PHE A 1 184 ? 1.328   6.120   -15.974 1.00 14.36  ?  183 PHE A CE1   1 
ATOM   1445 C  CE2   . PHE A 1 184 ? 2.853   7.159   -14.451 1.00 15.35  ?  183 PHE A CE2   1 
ATOM   1446 C  CZ    . PHE A 1 184 ? 2.092   6.073   -14.817 1.00 15.27  ?  183 PHE A CZ    1 
ATOM   1447 N  N     . ARG A 1 185 ? 0.801   11.571  -15.282 1.00 14.11  ?  184 ARG A N     1 
ATOM   1448 C  CA    . ARG A 1 185 ? 0.246   11.926  -13.978 1.00 14.54  ?  184 ARG A CA    1 
ATOM   1449 C  C     . ARG A 1 185 ? -1.062  12.703  -14.119 1.00 14.26  ?  184 ARG A C     1 
ATOM   1450 O  O     . ARG A 1 185 ? -2.002  12.483  -13.344 1.00 13.78  ?  184 ARG A O     1 
ATOM   1451 C  CB    . ARG A 1 185 ? 1.275   12.720  -13.164 1.00 12.97  ?  184 ARG A CB    1 
ATOM   1452 C  CG    . ARG A 1 185 ? 2.501   11.899  -12.750 1.00 16.70  ?  184 ARG A CG    1 
ATOM   1453 C  CD    . ARG A 1 185 ? 3.402   12.679  -11.793 1.00 16.49  ?  184 ARG A CD    1 
ATOM   1454 N  NE    . ARG A 1 185 ? 3.881   13.927  -12.382 1.00 17.43  ?  184 ARG A NE    1 
ATOM   1455 C  CZ    . ARG A 1 185 ? 4.994   14.039  -13.106 1.00 18.59  ?  184 ARG A CZ    1 
ATOM   1456 N  NH1   . ARG A 1 185 ? 5.752   12.978  -13.334 1.00 20.13  1  184 ARG A NH1   1 
ATOM   1457 N  NH2   . ARG A 1 185 ? 5.354   15.218  -13.596 1.00 22.96  ?  184 ARG A NH2   1 
ATOM   1458 N  N     . ARG A 1 186 ? -1.152  13.595  -15.115 1.00 12.46  ?  185 ARG A N     1 
ATOM   1459 C  CA    . ARG A 1 186 ? -2.400  14.324  -15.332 1.00 13.20  ?  185 ARG A CA    1 
ATOM   1460 C  C     . ARG A 1 186 ? -3.547  13.364  -15.608 1.00 17.46  ?  185 ARG A C     1 
ATOM   1461 O  O     . ARG A 1 186 ? -4.661  13.554  -15.108 1.00 15.40  ?  185 ARG A O     1 
ATOM   1462 C  CB    . ARG A 1 186 ? -2.265  15.312  -16.494 1.00 14.57  ?  185 ARG A CB    1 
ATOM   1463 C  CG    . ARG A 1 186 ? -1.371  16.523  -16.224 1.00 11.31  ?  185 ARG A CG    1 
ATOM   1464 C  CD    . ARG A 1 186 ? -1.684  17.674  -17.185 1.00 14.79  ?  185 ARG A CD    1 
ATOM   1465 N  NE    . ARG A 1 186 ? -1.444  17.345  -18.592 1.00 16.65  ?  185 ARG A NE    1 
ATOM   1466 C  CZ    . ARG A 1 186 ? -0.242  17.384  -19.170 1.00 17.28  ?  185 ARG A CZ    1 
ATOM   1467 N  NH1   . ARG A 1 186 ? 0.830   17.722  -18.461 1.00 16.42  1  185 ARG A NH1   1 
ATOM   1468 N  NH2   . ARG A 1 186 ? -0.108  17.074  -20.454 1.00 13.01  ?  185 ARG A NH2   1 
ATOM   1469 N  N     . CYS A 1 187 ? -3.290  12.321  -16.394 1.00 17.58  ?  186 CYS A N     1 
ATOM   1470 C  CA    . CYS A 1 187 ? -4.377  11.428  -16.782 1.00 17.06  ?  186 CYS A CA    1 
ATOM   1471 C  C     . CYS A 1 187 ? -4.810  10.549  -15.618 1.00 17.41  ?  186 CYS A C     1 
ATOM   1472 O  O     . CYS A 1 187 ? -6.011  10.273  -15.447 1.00 16.52  ?  186 CYS A O     1 
ATOM   1473 C  CB    . CYS A 1 187 ? -3.954  10.595  -17.985 1.00 17.42  ?  186 CYS A CB    1 
ATOM   1474 S  SG    . CYS A 1 187 ? -3.999  11.567  -19.491 1.00 21.64  ?  186 CYS A SG    1 
ATOM   1475 N  N     . ILE A 1 188 ? -3.848  10.113  -14.797 1.00 14.94  ?  187 ILE A N     1 
ATOM   1476 C  CA    . ILE A 1 188 ? -4.222  9.448   -13.548 1.00 13.08  ?  187 ILE A CA    1 
ATOM   1477 C  C     . ILE A 1 188 ? -5.127  10.354  -12.713 1.00 14.43  ?  187 ILE A C     1 
ATOM   1478 O  O     . ILE A 1 188 ? -6.152  9.911   -12.167 1.00 13.75  ?  187 ILE A O     1 
ATOM   1479 C  CB    . ILE A 1 188 ? -2.965  9.020   -12.768 1.00 12.59  ?  187 ILE A CB    1 
ATOM   1480 C  CG1   . ILE A 1 188 ? -2.232  7.895   -13.512 1.00 15.25  ?  187 ILE A CG1   1 
ATOM   1481 C  CG2   . ILE A 1 188 ? -3.337  8.611   -11.357 1.00 10.52  ?  187 ILE A CG2   1 
ATOM   1482 C  CD1   . ILE A 1 188 ? -0.822  7.577   -12.977 1.00 16.10  ?  187 ILE A CD1   1 
ATOM   1483 N  N     . ARG A 1 189 ? -4.764  11.640  -12.594 1.00 13.81  ?  188 ARG A N     1 
ATOM   1484 C  CA    . ARG A 1 189 ? -5.585  12.555  -11.798 1.00 14.31  ?  188 ARG A CA    1 
ATOM   1485 C  C     . ARG A 1 189 ? -6.974  12.737  -12.405 1.00 12.92  ?  188 ARG A C     1 
ATOM   1486 O  O     . ARG A 1 189 ? -7.975  12.789  -11.672 1.00 14.98  ?  188 ARG A O     1 
ATOM   1487 C  CB    . ARG A 1 189 ? -4.897  13.915  -11.652 1.00 13.38  ?  188 ARG A CB    1 
ATOM   1488 C  CG    . ARG A 1 189 ? -3.677  13.928  -10.724 1.00 15.01  ?  188 ARG A CG    1 
ATOM   1489 C  CD    . ARG A 1 189 ? -3.223  15.365  -10.495 1.00 19.06  ?  188 ARG A CD    1 
ATOM   1490 N  NE    . ARG A 1 189 ? -2.268  15.497  -9.400  1.00 21.67  ?  188 ARG A NE    1 
ATOM   1491 C  CZ    . ARG A 1 189 ? -0.975  15.751  -9.565  1.00 25.90  ?  188 ARG A CZ    1 
ATOM   1492 N  NH1   . ARG A 1 189 ? -0.476  15.905  -10.786 1.00 26.37  1  188 ARG A NH1   1 
ATOM   1493 N  NH2   . ARG A 1 189 ? -0.182  15.855  -8.507  1.00 26.84  ?  188 ARG A NH2   1 
ATOM   1494 N  N     . TYR A 1 190 ? -7.049  12.893  -13.733 1.00 14.66  ?  189 TYR A N     1 
ATOM   1495 C  CA    . TYR A 1 190 ? -8.346  13.038  -14.397 1.00 15.62  ?  189 TYR A CA    1 
ATOM   1496 C  C     . TYR A 1 190 ? -9.250  11.869  -14.045 1.00 15.62  ?  189 TYR A C     1 
ATOM   1497 O  O     . TYR A 1 190 ? -10.444 12.041  -13.761 1.00 16.81  ?  189 TYR A O     1 
ATOM   1498 C  CB    . TYR A 1 190 ? -8.191  13.102  -15.922 1.00 13.14  ?  189 TYR A CB    1 
ATOM   1499 C  CG    . TYR A 1 190 ? -7.362  14.238  -16.494 1.00 14.81  ?  189 TYR A CG    1 
ATOM   1500 C  CD1   . TYR A 1 190 ? -7.361  15.506  -15.919 1.00 13.90  ?  189 TYR A CD1   1 
ATOM   1501 C  CD2   . TYR A 1 190 ? -6.588  14.033  -17.630 1.00 15.93  ?  189 TYR A CD2   1 
ATOM   1502 C  CE1   . TYR A 1 190 ? -6.601  16.541  -16.468 1.00 15.72  ?  189 TYR A CE1   1 
ATOM   1503 C  CE2   . TYR A 1 190 ? -5.828  15.054  -18.184 1.00 15.56  ?  189 TYR A CE2   1 
ATOM   1504 C  CZ    . TYR A 1 190 ? -5.835  16.300  -17.604 1.00 17.17  ?  189 TYR A CZ    1 
ATOM   1505 O  OH    . TYR A 1 190 ? -5.067  17.302  -18.165 1.00 15.00  ?  189 TYR A OH    1 
ATOM   1506 N  N     . LEU A 1 191 ? -8.694  10.658  -14.091 1.00 17.18  ?  190 LEU A N     1 
ATOM   1507 C  CA    . LEU A 1 191 ? -9.512  9.485   -13.801 1.00 16.29  ?  190 LEU A CA    1 
ATOM   1508 C  C     . LEU A 1 191 ? -9.868  9.398   -12.321 1.00 13.93  ?  190 LEU A C     1 
ATOM   1509 O  O     . LEU A 1 191 ? -10.933 8.883   -11.975 1.00 14.12  ?  190 LEU A O     1 
ATOM   1510 C  CB    . LEU A 1 191 ? -8.798  8.219   -14.274 1.00 18.16  ?  190 LEU A CB    1 
ATOM   1511 C  CG    . LEU A 1 191 ? -8.752  8.109   -15.801 1.00 25.59  ?  190 LEU A CG    1 
ATOM   1512 C  CD1   . LEU A 1 191 ? -8.256  6.743   -16.230 1.00 25.74  ?  190 LEU A CD1   1 
ATOM   1513 C  CD2   . LEU A 1 191 ? -10.123 8.391   -16.408 1.00 27.29  ?  190 LEU A CD2   1 
ATOM   1514 N  N     . LYS A 1 192 ? -9.020  9.922   -11.434 1.00 13.63  ?  191 LYS A N     1 
ATOM   1515 C  CA    . LYS A 1 192 ? -9.400  9.955   -10.023 1.00 14.69  ?  191 LYS A CA    1 
ATOM   1516 C  C     . LYS A 1 192 ? -10.567 10.911  -9.781  1.00 14.98  ?  191 LYS A C     1 
ATOM   1517 O  O     . LYS A 1 192 ? -11.477 10.602  -9.000  1.00 13.62  ?  191 LYS A O     1 
ATOM   1518 C  CB    . LYS A 1 192 ? -8.199  10.332  -9.160  1.00 14.32  ?  191 LYS A CB    1 
ATOM   1519 C  CG    . LYS A 1 192 ? -7.215  9.191   -8.977  1.00 17.07  ?  191 LYS A CG    1 
ATOM   1520 C  CD    . LYS A 1 192 ? -6.038  9.605   -8.117  1.00 16.95  ?  191 LYS A CD    1 
ATOM   1521 C  CE    . LYS A 1 192 ? -5.143  8.424   -7.812  1.00 18.48  ?  191 LYS A CE    1 
ATOM   1522 N  NZ    . LYS A 1 192 ? -3.981  8.888   -7.009  1.00 19.94  1  191 LYS A NZ    1 
ATOM   1523 N  N     . ARG A 1 193 ? -10.576 12.066  -10.456 1.00 15.28  ?  192 ARG A N     1 
ATOM   1524 C  CA    . ARG A 1 193 ? -11.719 12.971  -10.300 1.00 14.98  ?  192 ARG A CA    1 
ATOM   1525 C  C     . ARG A 1 193 ? -12.979 12.387  -10.938 1.00 16.29  ?  192 ARG A C     1 
ATOM   1526 O  O     . ARG A 1 193 ? -14.083 12.548  -10.404 1.00 14.51  ?  192 ARG A O     1 
ATOM   1527 C  CB    . ARG A 1 193 ? -11.408 14.351  -10.882 1.00 15.56  ?  192 ARG A CB    1 
ATOM   1528 C  CG    . ARG A 1 193 ? -12.588 15.353  -10.820 1.00 16.85  ?  192 ARG A CG    1 
ATOM   1529 C  CD    . ARG A 1 193 ? -13.249 15.454  -9.421  1.00 17.94  ?  192 ARG A CD    1 
ATOM   1530 N  NE    . ARG A 1 193 ? -12.361 16.015  -8.403  1.00 15.79  ?  192 ARG A NE    1 
ATOM   1531 C  CZ    . ARG A 1 193 ? -12.239 17.311  -8.126  1.00 20.52  ?  192 ARG A CZ    1 
ATOM   1532 N  NH1   . ARG A 1 193 ? -12.953 18.217  -8.791  1.00 19.39  1  192 ARG A NH1   1 
ATOM   1533 N  NH2   . ARG A 1 193 ? -11.400 17.703  -7.171  1.00 21.43  ?  192 ARG A NH2   1 
ATOM   1534 N  N     . TRP A 1 194 ? -12.840 11.732  -12.095 1.00 16.39  ?  193 TRP A N     1 
ATOM   1535 C  CA    . TRP A 1 194 ? -13.956 10.982  -12.670 1.00 14.65  ?  193 TRP A CA    1 
ATOM   1536 C  C     . TRP A 1 194 ? -14.495 9.957   -11.673 1.00 17.08  ?  193 TRP A C     1 
ATOM   1537 O  O     . TRP A 1 194 ? -15.716 9.825   -11.492 1.00 15.46  ?  193 TRP A O     1 
ATOM   1538 C  CB    . TRP A 1 194 ? -13.504 10.299  -13.966 1.00 14.98  ?  193 TRP A CB    1 
ATOM   1539 C  CG    . TRP A 1 194 ? -14.456 9.241   -14.502 1.00 12.12  ?  193 TRP A CG    1 
ATOM   1540 C  CD1   . TRP A 1 194 ? -15.672 9.455   -15.096 1.00 13.07  ?  193 TRP A CD1   1 
ATOM   1541 C  CD2   . TRP A 1 194 ? -14.245 7.820   -14.521 1.00 11.93  ?  193 TRP A CD2   1 
ATOM   1542 N  NE1   . TRP A 1 194 ? -16.231 8.251   -15.476 1.00 15.25  ?  193 TRP A NE1   1 
ATOM   1543 C  CE2   . TRP A 1 194 ? -15.378 7.235   -15.130 1.00 15.13  ?  193 TRP A CE2   1 
ATOM   1544 C  CE3   . TRP A 1 194 ? -13.213 6.985   -14.072 1.00 16.57  ?  193 TRP A CE3   1 
ATOM   1545 C  CZ2   . TRP A 1 194 ? -15.505 5.847   -15.308 1.00 15.82  ?  193 TRP A CZ2   1 
ATOM   1546 C  CZ3   . TRP A 1 194 ? -13.339 5.602   -14.251 1.00 14.11  ?  193 TRP A CZ3   1 
ATOM   1547 C  CH2   . TRP A 1 194 ? -14.476 5.052   -14.859 1.00 14.75  ?  193 TRP A CH2   1 
ATOM   1548 N  N     . ARG A 1 195 ? -13.591 9.225   -11.014 1.00 15.92  ?  194 ARG A N     1 
ATOM   1549 C  CA    . ARG A 1 195 ? -13.984 8.277   -9.973  1.00 17.67  ?  194 ARG A CA    1 
ATOM   1550 C  C     . ARG A 1 195 ? -14.786 8.964   -8.873  1.00 15.08  ?  194 ARG A C     1 
ATOM   1551 O  O     . ARG A 1 195 ? -15.832 8.468   -8.447  1.00 15.93  ?  194 ARG A O     1 
ATOM   1552 C  CB    . ARG A 1 195 ? -12.742 7.604   -9.374  1.00 18.75  ?  194 ARG A CB    1 
ATOM   1553 C  CG    . ARG A 1 195 ? -13.016 6.865   -8.051  1.00 22.48  ?  194 ARG A CG    1 
ATOM   1554 C  CD    . ARG A 1 195 ? -11.785 6.818   -7.131  1.00 26.34  ?  194 ARG A CD    1 
ATOM   1555 N  NE    . ARG A 1 195 ? -11.368 8.154   -6.711  1.00 32.56  ?  194 ARG A NE    1 
ATOM   1556 C  CZ    . ARG A 1 195 ? -10.228 8.426   -6.078  1.00 36.02  ?  194 ARG A CZ    1 
ATOM   1557 N  NH1   . ARG A 1 195 ? -9.375  7.450   -5.784  1.00 36.37  1  194 ARG A NH1   1 
ATOM   1558 N  NH2   . ARG A 1 195 ? -9.938  9.680   -5.742  1.00 35.31  ?  194 ARG A NH2   1 
ATOM   1559 N  N     . ASP A 1 196 ? -14.294 10.102  -8.384  1.00 14.01  ?  195 ASP A N     1 
ATOM   1560 C  CA    . ASP A 1 196 ? -14.993 10.770  -7.295  1.00 15.21  ?  195 ASP A CA    1 
ATOM   1561 C  C     . ASP A 1 196 ? -16.341 11.319  -7.743  1.00 15.46  ?  195 ASP A C     1 
ATOM   1562 O  O     . ASP A 1 196 ? -17.297 11.323  -6.959  1.00 17.44  ?  195 ASP A O     1 
ATOM   1563 C  CB    . ASP A 1 196 ? -14.136 11.894  -6.718  1.00 21.38  ?  195 ASP A CB    1 
ATOM   1564 C  CG    . ASP A 1 196 ? -12.906 11.381  -6.007  1.00 23.91  ?  195 ASP A CG    1 
ATOM   1565 O  OD1   . ASP A 1 196 ? -12.870 10.186  -5.648  1.00 25.69  ?  195 ASP A OD1   1 
ATOM   1566 O  OD2   . ASP A 1 196 ? -11.973 12.178  -5.805  1.00 28.21  -1 195 ASP A OD2   1 
ATOM   1567 N  N     . PHE A 1 197 ? -16.444 11.768  -8.993  1.00 10.79  ?  196 PHE A N     1 
ATOM   1568 C  CA    . PHE A 1 197 ? -17.682 12.384  -9.454  1.00 15.37  ?  196 PHE A CA    1 
ATOM   1569 C  C     . PHE A 1 197 ? -18.752 11.341  -9.773  1.00 16.94  ?  196 PHE A C     1 
ATOM   1570 O  O     . PHE A 1 197 ? -19.931 11.542  -9.459  1.00 14.69  ?  196 PHE A O     1 
ATOM   1571 C  CB    . PHE A 1 197 ? -17.398 13.260  -10.680 1.00 12.56  ?  196 PHE A CB    1 
ATOM   1572 C  CG    . PHE A 1 197 ? -18.610 13.961  -11.225 1.00 18.21  ?  196 PHE A CG    1 
ATOM   1573 C  CD1   . PHE A 1 197 ? -19.351 14.824  -10.419 1.00 20.41  ?  196 PHE A CD1   1 
ATOM   1574 C  CD2   . PHE A 1 197 ? -19.004 13.777  -12.545 1.00 16.06  ?  196 PHE A CD2   1 
ATOM   1575 C  CE1   . PHE A 1 197 ? -20.469 15.481  -10.917 1.00 19.58  ?  196 PHE A CE1   1 
ATOM   1576 C  CE2   . PHE A 1 197 ? -20.122 14.432  -13.050 1.00 16.31  ?  196 PHE A CE2   1 
ATOM   1577 C  CZ    . PHE A 1 197 ? -20.856 15.284  -12.233 1.00 18.74  ?  196 PHE A CZ    1 
ATOM   1578 N  N     . ARG A 1 198 ? -18.373 10.220  -10.381 1.00 14.23  ?  197 ARG A N     1 
ATOM   1579 C  CA    . ARG A 1 198 ? -19.363 9.270   -10.881 1.00 14.74  ?  197 ARG A CA    1 
ATOM   1580 C  C     . ARG A 1 198 ? -19.496 8.007   -10.049 1.00 19.31  ?  197 ARG A C     1 
ATOM   1581 O  O     . ARG A 1 198 ? -20.285 7.124   -10.415 1.00 20.45  ?  197 ARG A O     1 
ATOM   1582 C  CB    . ARG A 1 198 ? -19.046 8.897   -12.329 1.00 17.95  ?  197 ARG A CB    1 
ATOM   1583 C  CG    . ARG A 1 198 ? -19.062 10.089  -13.256 1.00 19.66  ?  197 ARG A CG    1 
ATOM   1584 C  CD    . ARG A 1 198 ? -19.768 9.739   -14.546 1.00 26.76  ?  197 ARG A CD    1 
ATOM   1585 N  NE    . ARG A 1 198 ? -21.214 9.632   -14.372 1.00 23.83  ?  197 ARG A NE    1 
ATOM   1586 C  CZ    . ARG A 1 198 ? -22.015 9.002   -15.226 1.00 28.17  ?  197 ARG A CZ    1 
ATOM   1587 N  NH1   . ARG A 1 198 ? -21.506 8.414   -16.306 1.00 28.73  1  197 ARG A NH1   1 
ATOM   1588 N  NH2   . ARG A 1 198 ? -23.322 8.958   -15.006 1.00 24.59  ?  197 ARG A NH2   1 
ATOM   1589 N  N     . PHE A 1 199 ? -18.762 7.883   -8.946  1.00 15.40  ?  198 PHE A N     1 
ATOM   1590 C  CA    . PHE A 1 199 ? -18.902 6.725   -8.073  1.00 19.98  ?  198 PHE A CA    1 
ATOM   1591 C  C     . PHE A 1 199 ? -19.219 7.160   -6.644  1.00 32.12  ?  198 PHE A C     1 
ATOM   1592 O  O     . PHE A 1 199 ? -18.899 6.460   -5.682  1.00 37.06  ?  198 PHE A O     1 
ATOM   1593 C  CB    . PHE A 1 199 ? -17.648 5.847   -8.127  1.00 15.88  ?  198 PHE A CB    1 
ATOM   1594 C  CG    . PHE A 1 199 ? -17.381 5.243   -9.489  1.00 19.05  ?  198 PHE A CG    1 
ATOM   1595 C  CD1   . PHE A 1 199 ? -16.856 6.012   -10.517 1.00 16.37  ?  198 PHE A CD1   1 
ATOM   1596 C  CD2   . PHE A 1 199 ? -17.644 3.898   -9.735  1.00 20.12  ?  198 PHE A CD2   1 
ATOM   1597 C  CE1   . PHE A 1 199 ? -16.614 5.455   -11.768 1.00 19.82  ?  198 PHE A CE1   1 
ATOM   1598 C  CE2   . PHE A 1 199 ? -17.396 3.332   -10.978 1.00 19.35  ?  198 PHE A CE2   1 
ATOM   1599 C  CZ    . PHE A 1 199 ? -16.877 4.111   -11.996 1.00 20.69  ?  198 PHE A CZ    1 
ATOM   1600 N  N     . SER A 1 200 ? -19.867 8.321   -6.505  1.00 39.05  ?  199 SER A N     1 
ATOM   1601 C  CA    . SER A 1 200 ? -20.225 8.868   -5.201  1.00 46.21  ?  199 SER A CA    1 
ATOM   1602 C  C     . SER A 1 200 ? -21.465 8.218   -4.595  1.00 50.97  ?  199 SER A C     1 
ATOM   1603 O  O     . SER A 1 200 ? -21.620 8.249   -3.369  1.00 52.70  ?  199 SER A O     1 
ATOM   1604 C  CB    . SER A 1 200 ? -20.451 10.379  -5.308  1.00 46.46  ?  199 SER A CB    1 
ATOM   1605 O  OG    . SER A 1 200 ? -21.541 10.673  -6.167  1.00 46.27  ?  199 SER A OG    1 
ATOM   1606 N  N     . SER A 1 201 ? -22.354 7.644   -5.414  1.00 49.49  ?  200 SER A N     1 
ATOM   1607 C  CA    . SER A 1 201 ? -23.537 6.982   -4.869  1.00 49.46  ?  200 SER A CA    1 
ATOM   1608 C  C     . SER A 1 201 ? -23.188 5.720   -4.096  1.00 49.07  ?  200 SER A C     1 
ATOM   1609 O  O     . SER A 1 201 ? -23.964 5.306   -3.228  1.00 50.01  ?  200 SER A O     1 
ATOM   1610 C  CB    . SER A 1 201 ? -24.530 6.624   -5.978  1.00 45.84  ?  200 SER A CB    1 
ATOM   1611 O  OG    . SER A 1 201 ? -24.946 7.768   -6.698  1.00 45.97  ?  200 SER A OG    1 
ATOM   1612 N  N     . ASP A 1 202 ? -22.044 5.101   -4.396  1.00 46.66  ?  201 ASP A N     1 
ATOM   1613 C  CA    . ASP A 1 202 ? -21.640 3.855   -3.744  1.00 47.55  ?  201 ASP A CA    1 
ATOM   1614 C  C     . ASP A 1 202 ? -20.110 3.834   -3.720  1.00 49.66  ?  201 ASP A C     1 
ATOM   1615 O  O     . ASP A 1 202 ? -19.471 3.311   -4.636  1.00 47.75  ?  201 ASP A O     1 
ATOM   1616 C  CB    . ASP A 1 202 ? -22.214 2.643   -4.465  1.00 48.58  ?  201 ASP A CB    1 
ATOM   1617 C  CG    . ASP A 1 202 ? -22.051 1.360   -3.675  1.00 52.63  ?  201 ASP A CG    1 
ATOM   1618 O  OD1   . ASP A 1 202 ? -21.493 1.410   -2.556  1.00 53.41  ?  201 ASP A OD1   1 
ATOM   1619 O  OD2   . ASP A 1 202 ? -22.483 0.299   -4.176  1.00 54.99  -1 201 ASP A OD2   1 
ATOM   1620 N  N     . GLY A 1 203 ? -19.539 4.409   -2.657  1.00 53.38  ?  202 GLY A N     1 
ATOM   1621 C  CA    . GLY A 1 203 ? -18.091 4.491   -2.550  1.00 55.01  ?  202 GLY A CA    1 
ATOM   1622 C  C     . GLY A 1 203 ? -17.405 3.139   -2.558  1.00 55.78  ?  202 GLY A C     1 
ATOM   1623 O  O     . GLY A 1 203 ? -16.259 3.023   -3.003  1.00 53.15  ?  202 GLY A O     1 
ATOM   1624 N  N     . ASN A 1 204 ? -18.087 2.101   -2.067  1.00 58.75  ?  203 ASN A N     1 
ATOM   1625 C  CA    . ASN A 1 204 ? -17.513 0.761   -2.105  1.00 60.14  ?  203 ASN A CA    1 
ATOM   1626 C  C     . ASN A 1 204 ? -17.376 0.255   -3.537  1.00 54.39  ?  203 ASN A C     1 
ATOM   1627 O  O     . ASN A 1 204 ? -16.449 -0.506  -3.840  1.00 53.64  ?  203 ASN A O     1 
ATOM   1628 C  CB    . ASN A 1 204 ? -18.366 -0.197  -1.269  1.00 69.33  ?  203 ASN A CB    1 
ATOM   1629 C  CG    . ASN A 1 204 ? -17.725 -1.566  -1.106  1.00 75.07  ?  203 ASN A CG    1 
ATOM   1630 O  OD1   . ASN A 1 204 ? -18.106 -2.527  -1.776  1.00 77.29  ?  203 ASN A OD1   1 
ATOM   1631 N  ND2   . ASN A 1 204 ? -16.746 -1.660  -0.211  1.00 76.41  ?  203 ASN A ND2   1 
ATOM   1632 N  N     . ALA A 1 205 ? -18.271 0.676   -4.430  1.00 48.39  ?  204 ALA A N     1 
ATOM   1633 C  CA    . ALA A 1 205 ? -18.208 0.260   -5.825  1.00 43.59  ?  204 ALA A CA    1 
ATOM   1634 C  C     . ALA A 1 205 ? -17.128 0.982   -6.622  1.00 40.89  ?  204 ALA A C     1 
ATOM   1635 O  O     . ALA A 1 205 ? -16.864 0.590   -7.763  1.00 39.65  ?  204 ALA A O     1 
ATOM   1636 C  CB    . ALA A 1 205 ? -19.567 0.481   -6.496  1.00 38.16  ?  204 ALA A CB    1 
ATOM   1637 N  N     . ALA A 1 206 ? -16.494 2.009   -6.053  1.00 39.23  ?  205 ALA A N     1 
ATOM   1638 C  CA    . ALA A 1 206 ? -15.627 2.880   -6.838  1.00 37.69  ?  205 ALA A CA    1 
ATOM   1639 C  C     . ALA A 1 206 ? -14.311 2.179   -7.178  1.00 39.94  ?  205 ALA A C     1 
ATOM   1640 O  O     . ALA A 1 206 ? -13.743 1.473   -6.334  1.00 43.76  ?  205 ALA A O     1 
ATOM   1641 C  CB    . ALA A 1 206 ? -15.341 4.175   -6.077  1.00 36.97  ?  205 ALA A CB    1 
ATOM   1642 N  N     . PRO A 1 207 ? -13.796 2.357   -8.397  1.00 33.56  ?  206 PRO A N     1 
ATOM   1643 C  CA    . PRO A 1 207 ? -12.475 1.808   -8.736  1.00 30.50  ?  206 PRO A CA    1 
ATOM   1644 C  C     . PRO A 1 207 ? -11.390 2.590   -8.012  1.00 32.34  ?  206 PRO A C     1 
ATOM   1645 O  O     . PRO A 1 207 ? -11.242 3.798   -8.207  1.00 32.84  ?  206 PRO A O     1 
ATOM   1646 C  CB    . PRO A 1 207 ? -12.391 1.993   -10.253 1.00 30.48  ?  206 PRO A CB    1 
ATOM   1647 C  CG    . PRO A 1 207 ? -13.250 3.184   -10.520 1.00 31.45  ?  206 PRO A CG    1 
ATOM   1648 C  CD    . PRO A 1 207 ? -14.375 3.120   -9.516  1.00 29.12  ?  206 PRO A CD    1 
ATOM   1649 N  N     . LEU A 1 208 ? -10.631 1.890   -7.177  1.00 27.32  ?  207 LEU A N     1 
ATOM   1650 C  CA    . LEU A 1 208 ? -9.648  2.542   -6.335  1.00 34.37  ?  207 LEU A CA    1 
ATOM   1651 C  C     . LEU A 1 208 ? -8.668  3.360   -7.170  1.00 29.52  ?  207 LEU A C     1 
ATOM   1652 O  O     . LEU A 1 208 ? -8.379  3.043   -8.329  1.00 30.44  ?  207 LEU A O     1 
ATOM   1653 C  CB    . LEU A 1 208 ? -8.905  1.500   -5.504  1.00 42.98  ?  207 LEU A CB    1 
ATOM   1654 C  CG    . LEU A 1 208 ? -9.773  0.794   -4.456  1.00 46.66  ?  207 LEU A CG    1 
ATOM   1655 C  CD1   . LEU A 1 208 ? -8.998  -0.334  -3.789  1.00 51.37  ?  207 LEU A CD1   1 
ATOM   1656 C  CD2   . LEU A 1 208 ? -10.282 1.797   -3.421  1.00 42.25  ?  207 LEU A CD2   1 
ATOM   1657 N  N     . GLY A 1 209 ? -8.188  4.448   -6.575  1.00 22.44  ?  208 GLY A N     1 
ATOM   1658 C  CA    . GLY A 1 209 ? -7.134  5.216   -7.206  1.00 21.65  ?  208 GLY A CA    1 
ATOM   1659 C  C     . GLY A 1 209 ? -5.890  4.394   -7.471  1.00 15.88  ?  208 GLY A C     1 
ATOM   1660 O  O     . GLY A 1 209 ? -5.220  4.591   -8.484  1.00 20.23  ?  208 GLY A O     1 
ATOM   1661 N  N     . ILE A 1 210 ? -5.564  3.462   -6.572  1.00 21.32  ?  209 ILE A N     1 
ATOM   1662 C  CA    . ILE A 1 210 ? -4.403  2.599   -6.788  1.00 20.85  ?  209 ILE A CA    1 
ATOM   1663 C  C     . ILE A 1 210 ? -4.621  1.721   -8.013  1.00 20.19  ?  209 ILE A C     1 
ATOM   1664 O  O     . ILE A 1 210 ? -3.691  1.462   -8.790  1.00 23.44  ?  209 ILE A O     1 
ATOM   1665 C  CB    . ILE A 1 210 ? -4.117  1.761   -5.526  1.00 22.00  ?  209 ILE A CB    1 
ATOM   1666 C  CG1   . ILE A 1 210 ? -3.030  0.721   -5.804  1.00 25.34  ?  209 ILE A CG1   1 
ATOM   1667 C  CG2   . ILE A 1 210 ? -5.371  1.037   -5.068  1.00 22.85  ?  209 ILE A CG2   1 
ATOM   1668 C  CD1   . ILE A 1 210 ? -1.686  1.309   -6.052  1.00 25.93  ?  209 ILE A CD1   1 
ATOM   1669 N  N     . GLY A 1 211 ? -5.857  1.261   -8.210  1.00 18.87  ?  210 GLY A N     1 
ATOM   1670 C  CA    . GLY A 1 211 ? -6.170  0.487   -9.397  1.00 20.32  ?  210 GLY A CA    1 
ATOM   1671 C  C     . GLY A 1 211 ? -5.970  1.277   -10.676 1.00 20.03  ?  210 GLY A C     1 
ATOM   1672 O  O     . GLY A 1 211 ? -5.373  0.780   -11.634 1.00 16.63  ?  210 GLY A O     1 
ATOM   1673 N  N     . LEU A 1 212 ? -6.455  2.523   -10.705 1.00 17.23  ?  211 LEU A N     1 
ATOM   1674 C  CA    . LEU A 1 212 ? -6.277  3.358   -11.890 1.00 18.34  ?  211 LEU A CA    1 
ATOM   1675 C  C     . LEU A 1 212 ? -4.806  3.692   -12.107 1.00 15.79  ?  211 LEU A C     1 
ATOM   1676 O  O     . LEU A 1 212 ? -4.346  3.788   -13.248 1.00 15.23  ?  211 LEU A O     1 
ATOM   1677 C  CB    . LEU A 1 212 ? -7.105  4.639   -11.758 1.00 20.43  ?  211 LEU A CB    1 
ATOM   1678 C  CG    . LEU A 1 212 ? -8.616  4.470   -11.547 1.00 23.89  ?  211 LEU A CG    1 
ATOM   1679 C  CD1   . LEU A 1 212 ? -9.263  5.794   -11.150 1.00 24.71  ?  211 LEU A CD1   1 
ATOM   1680 C  CD2   . LEU A 1 212 ? -9.262  3.918   -12.797 1.00 24.50  ?  211 LEU A CD2   1 
ATOM   1681 N  N     . THR A 1 213 ? -4.052  3.865   -11.021 1.00 13.23  ?  212 THR A N     1 
ATOM   1682 C  CA    . THR A 1 213 ? -2.626  4.156   -11.136 1.00 13.75  ?  212 THR A CA    1 
ATOM   1683 C  C     . THR A 1 213 ? -1.872  2.969   -11.734 1.00 16.21  ?  212 THR A C     1 
ATOM   1684 O  O     . THR A 1 213 ? -1.043  3.128   -12.641 1.00 15.06  ?  212 THR A O     1 
ATOM   1685 C  CB    . THR A 1 213 ? -2.072  4.519   -9.752  1.00 14.90  ?  212 THR A CB    1 
ATOM   1686 O  OG1   . THR A 1 213 ? -2.862  5.575   -9.185  1.00 16.77  ?  212 THR A OG1   1 
ATOM   1687 C  CG2   . THR A 1 213 ? -0.613  4.958   -9.845  1.00 14.50  ?  212 THR A CG2   1 
ATOM   1688 N  N     . ALA A 1 214 ? -2.152  1.764   -11.238 1.00 17.00  ?  213 ALA A N     1 
ATOM   1689 C  CA    . ALA A 1 214 ? -1.513  0.576   -11.795 1.00 18.10  ?  213 ALA A CA    1 
ATOM   1690 C  C     . ALA A 1 214 ? -1.949  0.340   -13.239 1.00 14.92  ?  213 ALA A C     1 
ATOM   1691 O  O     . ALA A 1 214 ? -1.126  -0.020  -14.098 1.00 16.05  ?  213 ALA A O     1 
ATOM   1692 C  CB    . ALA A 1 214 ? -1.826  -0.635  -10.912 1.00 16.13  ?  213 ALA A CB    1 
ATOM   1693 N  N     . ALA A 1 215 ? -3.236  0.560   -13.536 1.00 13.75  ?  214 ALA A N     1 
ATOM   1694 C  CA    . ALA A 1 215 ? -3.695  0.432   -14.916 1.00 15.57  ?  214 ALA A CA    1 
ATOM   1695 C  C     . ALA A 1 215 ? -2.948  1.395   -15.826 1.00 18.91  ?  214 ALA A C     1 
ATOM   1696 O  O     . ALA A 1 215 ? -2.554  1.025   -16.936 1.00 17.03  ?  214 ALA A O     1 
ATOM   1697 C  CB    . ALA A 1 215 ? -5.203  0.674   -15.013 1.00 15.30  ?  214 ALA A CB    1 
ATOM   1698 N  N     . ALA A 1 216 ? -2.739  2.640   -15.373 1.00 16.37  ?  215 ALA A N     1 
ATOM   1699 C  CA    . ALA A 1 216 ? -1.962  3.583   -16.174 1.00 14.44  ?  215 ALA A CA    1 
ATOM   1700 C  C     . ALA A 1 216 ? -0.530  3.102   -16.356 1.00 14.21  ?  215 ALA A C     1 
ATOM   1701 O  O     . ALA A 1 216 ? 0.043   3.241   -17.443 1.00 18.31  ?  215 ALA A O     1 
ATOM   1702 C  CB    . ALA A 1 216 ? -1.990  4.973   -15.538 1.00 13.22  ?  215 ALA A CB    1 
ATOM   1703 N  N     . TYR A 1 217 ? 0.067   2.536   -15.303 1.00 14.35  ?  216 TYR A N     1 
ATOM   1704 C  CA    . TYR A 1 217 ? 1.403   1.960   -15.453 1.00 16.17  ?  216 TYR A CA    1 
ATOM   1705 C  C     . TYR A 1 217 ? 1.437   0.949   -16.595 1.00 16.41  ?  216 TYR A C     1 
ATOM   1706 O  O     . TYR A 1 217 ? 2.370   0.945   -17.414 1.00 15.30  ?  216 TYR A O     1 
ATOM   1707 C  CB    . TYR A 1 217 ? 1.856   1.297   -14.149 1.00 17.66  ?  216 TYR A CB    1 
ATOM   1708 C  CG    . TYR A 1 217 ? 3.134   0.499   -14.317 1.00 17.40  ?  216 TYR A CG    1 
ATOM   1709 C  CD1   . TYR A 1 217 ? 4.377   1.116   -14.236 1.00 18.30  ?  216 TYR A CD1   1 
ATOM   1710 C  CD2   . TYR A 1 217 ? 3.096   -0.869  -14.592 1.00 20.13  ?  216 TYR A CD2   1 
ATOM   1711 C  CE1   . TYR A 1 217 ? 5.556   0.386   -14.413 1.00 19.53  ?  216 TYR A CE1   1 
ATOM   1712 C  CE2   . TYR A 1 217 ? 4.269   -1.597  -14.778 1.00 20.28  ?  216 TYR A CE2   1 
ATOM   1713 C  CZ    . TYR A 1 217 ? 5.487   -0.964  -14.682 1.00 21.12  ?  216 TYR A CZ    1 
ATOM   1714 O  OH    . TYR A 1 217 ? 6.643   -1.696  -14.863 1.00 23.19  ?  216 TYR A OH    1 
ATOM   1715 N  N     . TRP A 1 218 ? 0.429   0.081   -16.665 1.00 13.73  ?  217 TRP A N     1 
ATOM   1716 C  CA    . TRP A 1 218 ? 0.463   -0.953  -17.698 1.00 19.68  ?  217 TRP A CA    1 
ATOM   1717 C  C     . TRP A 1 218 ? 0.110   -0.404  -19.078 1.00 19.86  ?  217 TRP A C     1 
ATOM   1718 O  O     . TRP A 1 218 ? 0.669   -0.851  -20.082 1.00 19.68  ?  217 TRP A O     1 
ATOM   1719 C  CB    . TRP A 1 218 ? -0.484  -2.104  -17.351 1.00 18.02  ?  217 TRP A CB    1 
ATOM   1720 C  CG    . TRP A 1 218 ? -0.058  -2.924  -16.168 1.00 18.25  ?  217 TRP A CG    1 
ATOM   1721 C  CD1   . TRP A 1 218 ? -0.696  -3.017  -14.966 1.00 15.48  ?  217 TRP A CD1   1 
ATOM   1722 C  CD2   . TRP A 1 218 ? 1.087   -3.779  -16.083 1.00 19.05  ?  217 TRP A CD2   1 
ATOM   1723 N  NE1   . TRP A 1 218 ? -0.012  -3.866  -14.130 1.00 16.67  ?  217 TRP A NE1   1 
ATOM   1724 C  CE2   . TRP A 1 218 ? 1.088   -4.347  -14.794 1.00 16.94  ?  217 TRP A CE2   1 
ATOM   1725 C  CE3   . TRP A 1 218 ? 2.120   -4.108  -16.966 1.00 23.56  ?  217 TRP A CE3   1 
ATOM   1726 C  CZ2   . TRP A 1 218 ? 2.073   -5.235  -14.370 1.00 19.38  ?  217 TRP A CZ2   1 
ATOM   1727 C  CZ3   . TRP A 1 218 ? 3.101   -4.993  -16.543 1.00 25.28  ?  217 TRP A CZ3   1 
ATOM   1728 C  CH2   . TRP A 1 218 ? 3.070   -5.544  -15.256 1.00 23.45  ?  217 TRP A CH2   1 
ATOM   1729 N  N     . TRP A 1 219 ? -0.805  0.560   -19.160 1.00 18.27  ?  218 TRP A N     1 
ATOM   1730 C  CA    . TRP A 1 219 ? -1.474  0.828   -20.421 1.00 15.24  ?  218 TRP A CA    1 
ATOM   1731 C  C     . TRP A 1 219 ? -1.453  2.271   -20.900 1.00 17.71  ?  218 TRP A C     1 
ATOM   1732 O  O     . TRP A 1 219 ? -1.846  2.510   -22.045 1.00 20.46  ?  218 TRP A O     1 
ATOM   1733 C  CB    . TRP A 1 219 ? -2.937  0.366   -20.343 1.00 17.73  ?  218 TRP A CB    1 
ATOM   1734 C  CG    . TRP A 1 219 ? -3.047  -1.118  -20.142 1.00 18.33  ?  218 TRP A CG    1 
ATOM   1735 C  CD1   . TRP A 1 219 ? -2.365  -2.088  -20.825 1.00 22.08  ?  218 TRP A CD1   1 
ATOM   1736 C  CD2   . TRP A 1 219 ? -3.881  -1.801  -19.200 1.00 16.54  ?  218 TRP A CD2   1 
ATOM   1737 N  NE1   . TRP A 1 219 ? -2.727  -3.337  -20.364 1.00 20.07  ?  218 TRP A NE1   1 
ATOM   1738 C  CE2   . TRP A 1 219 ? -3.656  -3.187  -19.367 1.00 19.39  ?  218 TRP A CE2   1 
ATOM   1739 C  CE3   . TRP A 1 219 ? -4.799  -1.378  -18.233 1.00 21.57  ?  218 TRP A CE3   1 
ATOM   1740 C  CZ2   . TRP A 1 219 ? -4.314  -4.149  -18.604 1.00 20.58  ?  218 TRP A CZ2   1 
ATOM   1741 C  CZ3   . TRP A 1 219 ? -5.455  -2.341  -17.473 1.00 23.57  ?  218 TRP A CZ3   1 
ATOM   1742 C  CH2   . TRP A 1 219 ? -5.210  -3.709  -17.669 1.00 20.73  ?  218 TRP A CH2   1 
ATOM   1743 N  N     . PHE A 1 220 ? -1.040  3.234   -20.086 1.00 17.09  ?  219 PHE A N     1 
ATOM   1744 C  CA    . PHE A 1 220 ? -1.014  4.608   -20.569 1.00 14.63  ?  219 PHE A CA    1 
ATOM   1745 C  C     . PHE A 1 220 ? 0.003   4.762   -21.689 1.00 14.83  ?  219 PHE A C     1 
ATOM   1746 O  O     . PHE A 1 220 ? 1.106   4.212   -21.628 1.00 17.13  ?  219 PHE A O     1 
ATOM   1747 C  CB    . PHE A 1 220 ? -0.677  5.583   -19.446 1.00 14.13  ?  219 PHE A CB    1 
ATOM   1748 C  CG    . PHE A 1 220 ? -0.451  6.987   -19.934 1.00 15.76  ?  219 PHE A CG    1 
ATOM   1749 C  CD1   . PHE A 1 220 ? -1.521  7.848   -20.107 1.00 15.52  ?  219 PHE A CD1   1 
ATOM   1750 C  CD2   . PHE A 1 220 ? 0.827   7.428   -20.258 1.00 13.88  ?  219 PHE A CD2   1 
ATOM   1751 C  CE1   . PHE A 1 220 ? -1.319  9.146   -20.567 1.00 15.87  ?  219 PHE A CE1   1 
ATOM   1752 C  CE2   . PHE A 1 220 ? 1.032   8.719   -20.732 1.00 16.61  ?  219 PHE A CE2   1 
ATOM   1753 C  CZ    . PHE A 1 220 ? -0.047  9.575   -20.886 1.00 12.68  ?  219 PHE A CZ    1 
ATOM   1754 N  N     . GLN A 1 221 ? -0.372  5.527   -22.713 1.00 17.38  ?  220 GLN A N     1 
ATOM   1755 C  CA    . GLN A 1 221 ? 0.530   5.895   -23.797 1.00 16.76  ?  220 GLN A CA    1 
ATOM   1756 C  C     . GLN A 1 221 ? 0.503   7.406   -23.988 1.00 17.41  ?  220 GLN A C     1 
ATOM   1757 O  O     . GLN A 1 221 ? -0.571  8.016   -24.010 1.00 17.58  ?  220 GLN A O     1 
ATOM   1758 C  CB    . GLN A 1 221 ? 0.139   5.193   -25.102 1.00 21.82  ?  220 GLN A CB    1 
ATOM   1759 C  CG    . GLN A 1 221 ? 0.155   3.678   -25.016 1.00 29.54  ?  220 GLN A CG    1 
ATOM   1760 C  CD    . GLN A 1 221 ? 1.557   3.112   -24.884 1.00 39.34  ?  220 GLN A CD    1 
ATOM   1761 O  OE1   . GLN A 1 221 ? 1.742   1.991   -24.408 1.00 47.86  ?  220 GLN A OE1   1 
ATOM   1762 N  NE2   . GLN A 1 221 ? 2.553   3.881   -25.311 1.00 38.53  ?  220 GLN A NE2   1 
ATOM   1763 N  N     . VAL A 1 222 ? 1.681   8.010   -24.138 1.00 20.64  ?  221 VAL A N     1 
ATOM   1764 C  CA    . VAL A 1 222 ? 1.739   9.451   -24.356 1.00 19.23  ?  221 VAL A CA    1 
ATOM   1765 C  C     . VAL A 1 222 ? 1.055   9.803   -25.677 1.00 17.98  ?  221 VAL A C     1 
ATOM   1766 O  O     . VAL A 1 222 ? 1.077   9.031   -26.644 1.00 17.95  ?  221 VAL A O     1 
ATOM   1767 C  CB    . VAL A 1 222 ? 3.200   9.935   -24.334 1.00 21.04  ?  221 VAL A CB    1 
ATOM   1768 C  CG1   . VAL A 1 222 ? 3.289   11.422  -24.650 1.00 22.81  ?  221 VAL A CG1   1 
ATOM   1769 C  CG2   . VAL A 1 222 ? 3.827   9.657   -22.971 1.00 20.73  ?  221 VAL A CG2   1 
ATOM   1770 N  N     . SER A 1 223 ? 0.407   10.965  -25.709 1.00 16.22  ?  222 SER A N     1 
ATOM   1771 C  CA    . SER A 1 223 ? -0.116  11.520  -26.951 1.00 18.25  ?  222 SER A CA    1 
ATOM   1772 C  C     . SER A 1 223 ? 0.417   12.933  -27.120 1.00 17.78  ?  222 SER A C     1 
ATOM   1773 O  O     . SER A 1 223 ? 0.097   13.818  -26.320 1.00 16.38  ?  222 SER A O     1 
ATOM   1774 C  CB    . SER A 1 223 ? -1.643  11.530  -26.966 1.00 17.36  ?  222 SER A CB    1 
ATOM   1775 O  OG    . SER A 1 223 ? -2.104  12.059  -28.195 1.00 17.24  ?  222 SER A OG    1 
ATOM   1776 N  N     . LYS A 1 224 ? 1.214   13.147  -28.165 1.00 19.58  ?  223 LYS A N     1 
ATOM   1777 C  CA    . LYS A 1 224 ? 1.803   14.451  -28.415 1.00 19.51  ?  223 LYS A CA    1 
ATOM   1778 C  C     . LYS A 1 224 ? 2.082   14.606  -29.904 1.00 22.73  ?  223 LYS A C     1 
ATOM   1779 O  O     . LYS A 1 224 ? 2.116   13.631  -30.659 1.00 25.44  ?  223 LYS A O     1 
ATOM   1780 C  CB    . LYS A 1 224 ? 3.089   14.655  -27.599 1.00 21.69  ?  223 LYS A CB    1 
ATOM   1781 C  CG    . LYS A 1 224 ? 4.196   13.640  -27.886 1.00 19.65  ?  223 LYS A CG    1 
ATOM   1782 C  CD    . LYS A 1 224 ? 5.385   13.846  -26.950 1.00 18.19  ?  223 LYS A CD    1 
ATOM   1783 C  CE    . LYS A 1 224 ? 6.450   12.764  -27.166 1.00 21.75  ?  223 LYS A CE    1 
ATOM   1784 N  NZ    . LYS A 1 224 ? 7.605   12.925  -26.233 1.00 19.16  1  223 LYS A NZ    1 
ATOM   1785 N  N     . ARG A 1 225 ? 2.271   15.861  -30.312 1.00 23.43  ?  224 ARG A N     1 
ATOM   1786 C  CA    . ARG A 1 225 ? 2.549   16.238  -31.690 1.00 29.18  ?  224 ARG A CA    1 
ATOM   1787 C  C     . ARG A 1 225 ? 3.755   17.162  -31.721 1.00 29.97  ?  224 ARG A C     1 
ATOM   1788 O  O     . ARG A 1 225 ? 3.872   18.075  -30.897 1.00 28.73  ?  224 ARG A O     1 
ATOM   1789 C  CB    . ARG A 1 225 ? 1.350   16.944  -32.334 1.00 35.03  ?  224 ARG A CB    1 
ATOM   1790 C  CG    . ARG A 1 225 ? 0.122   16.074  -32.516 1.00 47.58  ?  224 ARG A CG    1 
ATOM   1791 C  CD    . ARG A 1 225 ? 0.229   15.215  -33.769 1.00 56.35  ?  224 ARG A CD    1 
ATOM   1792 N  NE    . ARG A 1 225 ? 0.467   16.016  -34.968 1.00 60.88  ?  224 ARG A NE    1 
ATOM   1793 C  CZ    . ARG A 1 225 ? -0.494  16.557  -35.712 1.00 62.68  ?  224 ARG A CZ    1 
ATOM   1794 N  NH1   . ARG A 1 225 ? -1.768  16.390  -35.379 1.00 64.96  1  224 ARG A NH1   1 
ATOM   1795 N  NH2   . ARG A 1 225 ? -0.184  17.268  -36.788 1.00 60.53  ?  224 ARG A NH2   1 
ATOM   1796 N  N     . THR A 1 226 ? 4.648   16.920  -32.674 1.00 33.51  ?  225 THR A N     1 
ATOM   1797 C  CA    . THR A 1 226 ? 5.829   17.742  -32.890 1.00 38.16  ?  225 THR A CA    1 
ATOM   1798 C  C     . THR A 1 226 ? 5.650   18.489  -34.203 1.00 39.90  ?  225 THR A C     1 
ATOM   1799 O  O     . THR A 1 226 ? 5.510   17.862  -35.260 1.00 38.62  ?  225 THR A O     1 
ATOM   1800 C  CB    . THR A 1 226 ? 7.094   16.885  -32.916 1.00 45.65  ?  225 THR A CB    1 
ATOM   1801 O  OG1   . THR A 1 226 ? 7.156   16.094  -31.723 1.00 49.16  ?  225 THR A OG1   1 
ATOM   1802 C  CG2   . THR A 1 226 ? 8.335   17.761  -33.001 1.00 46.20  ?  225 THR A CG2   1 
ATOM   1803 N  N     . ASP A 1 227 ? 5.632   19.815  -34.131 1.00 47.56  ?  226 ASP A N     1 
ATOM   1804 C  CA    . ASP A 1 227 ? 5.401   20.629  -35.318 1.00 52.37  ?  226 ASP A CA    1 
ATOM   1805 C  C     . ASP A 1 227 ? 6.539   20.429  -36.319 1.00 52.41  ?  226 ASP A C     1 
ATOM   1806 O  O     . ASP A 1 227 ? 7.713   20.461  -35.930 1.00 51.06  ?  226 ASP A O     1 
ATOM   1807 C  CB    . ASP A 1 227 ? 5.275   22.103  -34.933 1.00 55.59  ?  226 ASP A CB    1 
ATOM   1808 C  CG    . ASP A 1 227 ? 4.775   22.967  -36.075 1.00 60.71  ?  226 ASP A CG    1 
ATOM   1809 O  OD1   . ASP A 1 227 ? 5.539   23.196  -37.035 1.00 64.38  ?  226 ASP A OD1   1 
ATOM   1810 O  OD2   . ASP A 1 227 ? 3.609   23.409  -36.017 1.00 62.14  -1 226 ASP A OD2   1 
ATOM   1811 N  N     . PRO A 1 228 ? 6.237   20.217  -37.605 1.00 52.19  ?  227 PRO A N     1 
ATOM   1812 C  CA    . PRO A 1 228 ? 7.306   19.918  -38.574 1.00 52.26  ?  227 PRO A CA    1 
ATOM   1813 C  C     . PRO A 1 228 ? 8.196   21.106  -38.912 1.00 54.24  ?  227 PRO A C     1 
ATOM   1814 O  O     . PRO A 1 228 ? 9.207   20.917  -39.605 1.00 54.72  ?  227 PRO A O     1 
ATOM   1815 C  CB    . PRO A 1 228 ? 6.531   19.442  -39.810 1.00 51.37  ?  227 PRO A CB    1 
ATOM   1816 C  CG    . PRO A 1 228 ? 5.198   20.113  -39.691 1.00 49.69  ?  227 PRO A CG    1 
ATOM   1817 C  CD    . PRO A 1 228 ? 4.899   20.167  -38.219 1.00 50.54  ?  227 PRO A CD    1 
ATOM   1818 N  N     . VAL A 1 229 ? 7.865   22.312  -38.458 1.00 51.75  ?  228 VAL A N     1 
ATOM   1819 C  CA    . VAL A 1 229 ? 8.653   23.505  -38.739 1.00 52.45  ?  228 VAL A CA    1 
ATOM   1820 C  C     . VAL A 1 229 ? 9.434   23.957  -37.510 1.00 51.40  ?  228 VAL A C     1 
ATOM   1821 O  O     . VAL A 1 229 ? 10.652  24.127  -37.566 1.00 51.00  ?  228 VAL A O     1 
ATOM   1822 C  CB    . VAL A 1 229 ? 7.762   24.646  -39.281 1.00 52.79  ?  228 VAL A CB    1 
ATOM   1823 C  CG1   . VAL A 1 229 ? 8.600   25.881  -39.576 1.00 50.01  ?  228 VAL A CG1   1 
ATOM   1824 C  CG2   . VAL A 1 229 ? 7.022   24.195  -40.532 1.00 55.09  ?  228 VAL A CG2   1 
ATOM   1825 N  N     . SER A 1 230 ? 8.746   24.154  -36.388 1.00 50.48  ?  229 SER A N     1 
ATOM   1826 C  CA    . SER A 1 230 ? 9.383   24.647  -35.174 1.00 48.96  ?  229 SER A CA    1 
ATOM   1827 C  C     . SER A 1 230 ? 9.850   23.537  -34.244 1.00 46.26  ?  229 SER A C     1 
ATOM   1828 O  O     . SER A 1 230 ? 10.580  23.824  -33.289 1.00 43.11  ?  229 SER A O     1 
ATOM   1829 C  CB    . SER A 1 230 ? 8.420   25.559  -34.410 1.00 47.89  ?  229 SER A CB    1 
ATOM   1830 O  OG    . SER A 1 230 ? 7.247   24.850  -34.051 1.00 43.75  ?  229 SER A OG    1 
ATOM   1831 N  N     . GLN A 1 231 ? 9.447   22.289  -34.495 1.00 46.92  ?  230 GLN A N     1 
ATOM   1832 C  CA    . GLN A 1 231 ? 9.651   21.160  -33.585 1.00 48.57  ?  230 GLN A CA    1 
ATOM   1833 C  C     . GLN A 1 231 ? 9.016   21.405  -32.218 1.00 44.83  ?  230 GLN A C     1 
ATOM   1834 O  O     . GLN A 1 231 ? 9.334   20.710  -31.247 1.00 47.42  ?  230 GLN A O     1 
ATOM   1835 C  CB    . GLN A 1 231 ? 11.139  20.808  -33.437 1.00 50.22  ?  230 GLN A CB    1 
ATOM   1836 C  CG    . GLN A 1 231 ? 11.744  20.183  -34.690 1.00 55.57  ?  230 GLN A CG    1 
ATOM   1837 C  CD    . GLN A 1 231 ? 13.187  19.736  -34.503 1.00 59.61  ?  230 GLN A CD    1 
ATOM   1838 O  OE1   . GLN A 1 231 ? 13.825  20.044  -33.494 1.00 58.36  ?  230 GLN A OE1   1 
ATOM   1839 N  NE2   . GLN A 1 231 ? 13.708  19.002  -35.481 1.00 61.75  ?  230 GLN A NE2   1 
ATOM   1840 N  N     . ASN A 1 232 ? 8.112   22.380  -32.140 1.00 40.65  ?  231 ASN A N     1 
ATOM   1841 C  CA    . ASN A 1 232 ? 7.386   22.668  -30.910 1.00 37.55  ?  231 ASN A CA    1 
ATOM   1842 C  C     . ASN A 1 232 ? 6.423   21.527  -30.586 1.00 31.85  ?  231 ASN A C     1 
ATOM   1843 O  O     . ASN A 1 232 ? 5.645   21.095  -31.440 1.00 33.69  ?  231 ASN A O     1 
ATOM   1844 C  CB    . ASN A 1 232 ? 6.628   23.983  -31.064 1.00 42.13  ?  231 ASN A CB    1 
ATOM   1845 C  CG    . ASN A 1 232 ? 6.419   24.693  -29.752 1.00 48.54  ?  231 ASN A CG    1 
ATOM   1846 O  OD1   . ASN A 1 232 ? 5.867   24.126  -28.809 1.00 50.94  ?  231 ASN A OD1   1 
ATOM   1847 N  ND2   . ASN A 1 232 ? 6.868   25.947  -29.677 1.00 50.26  ?  231 ASN A ND2   1 
ATOM   1848 N  N     . VAL A 1 233 ? 6.466   21.041  -29.350 1.00 29.17  ?  232 VAL A N     1 
ATOM   1849 C  CA    . VAL A 1 233 ? 5.712   19.857  -28.952 1.00 27.34  ?  232 VAL A CA    1 
ATOM   1850 C  C     . VAL A 1 233 ? 4.470   20.295  -28.192 1.00 24.40  ?  232 VAL A C     1 
ATOM   1851 O  O     . VAL A 1 233 ? 4.556   21.115  -27.270 1.00 22.99  ?  232 VAL A O     1 
ATOM   1852 C  CB    . VAL A 1 233 ? 6.579   18.906  -28.110 1.00 26.59  ?  232 VAL A CB    1 
ATOM   1853 C  CG1   . VAL A 1 233 ? 5.730   17.783  -27.519 1.00 27.47  ?  232 VAL A CG1   1 
ATOM   1854 C  CG2   . VAL A 1 233 ? 7.702   18.332  -28.962 1.00 23.94  ?  232 VAL A CG2   1 
ATOM   1855 N  N     . THR A 1 234 ? 3.314   19.763  -28.592 1.00 22.89  ?  233 THR A N     1 
ATOM   1856 C  CA    . THR A 1 234 ? 2.053   19.974  -27.894 1.00 23.59  ?  233 THR A CA    1 
ATOM   1857 C  C     . THR A 1 234 ? 1.474   18.633  -27.462 1.00 20.55  ?  233 THR A C     1 
ATOM   1858 O  O     . THR A 1 234 ? 1.518   17.657  -28.212 1.00 21.92  ?  233 THR A O     1 
ATOM   1859 C  CB    . THR A 1 234 ? 1.033   20.717  -28.774 1.00 27.89  ?  233 THR A CB    1 
ATOM   1860 O  OG1   . THR A 1 234 ? 0.935   20.073  -30.055 1.00 30.87  ?  233 THR A OG1   1 
ATOM   1861 C  CG2   . THR A 1 234 ? 1.457   22.164  -28.969 1.00 31.83  ?  233 THR A CG2   1 
ATOM   1862 N  N     . TYR A 1 235 ? 0.927   18.584  -26.252 1.00 19.41  ?  234 TYR A N     1 
ATOM   1863 C  CA    . TYR A 1 235 ? 0.340   17.353  -25.746 1.00 15.75  ?  234 TYR A CA    1 
ATOM   1864 C  C     . TYR A 1 235 ? -1.163  17.349  -25.990 1.00 18.09  ?  234 TYR A C     1 
ATOM   1865 O  O     . TYR A 1 235 ? -1.800  18.399  -26.109 1.00 18.85  ?  234 TYR A O     1 
ATOM   1866 C  CB    . TYR A 1 235 ? 0.664   17.170  -24.256 1.00 18.06  ?  234 TYR A CB    1 
ATOM   1867 C  CG    . TYR A 1 235 ? 2.090   16.698  -24.060 1.00 22.32  ?  234 TYR A CG    1 
ATOM   1868 C  CD1   . TYR A 1 235 ? 3.147   17.603  -24.065 1.00 23.76  ?  234 TYR A CD1   1 
ATOM   1869 C  CD2   . TYR A 1 235 ? 2.383   15.346  -23.920 1.00 22.08  ?  234 TYR A CD2   1 
ATOM   1870 C  CE1   . TYR A 1 235 ? 4.461   17.170  -23.915 1.00 23.75  ?  234 TYR A CE1   1 
ATOM   1871 C  CE2   . TYR A 1 235 ? 3.694   14.904  -23.770 1.00 21.60  ?  234 TYR A CE2   1 
ATOM   1872 C  CZ    . TYR A 1 235 ? 4.726   15.823  -23.767 1.00 22.70  ?  234 TYR A CZ    1 
ATOM   1873 O  OH    . TYR A 1 235 ? 6.026   15.394  -23.622 1.00 22.12  ?  234 TYR A OH    1 
ATOM   1874 N  N     . ASP A 1 236 ? -1.725  16.140  -26.094 1.00 17.25  ?  235 ASP A N     1 
ATOM   1875 C  CA    . ASP A 1 236 ? -3.135  15.942  -26.432 1.00 17.57  ?  235 ASP A CA    1 
ATOM   1876 C  C     . ASP A 1 236 ? -3.708  15.031  -25.347 1.00 15.94  ?  235 ASP A C     1 
ATOM   1877 O  O     . ASP A 1 236 ? -3.775  13.817  -25.525 1.00 18.31  ?  235 ASP A O     1 
ATOM   1878 C  CB    . ASP A 1 236 ? -3.278  15.346  -27.850 1.00 18.49  ?  235 ASP A CB    1 
ATOM   1879 C  CG    . ASP A 1 236 ? -4.717  15.332  -28.351 1.00 19.37  ?  235 ASP A CG    1 
ATOM   1880 O  OD1   . ASP A 1 236 ? -5.654  15.429  -27.532 1.00 19.53  ?  235 ASP A OD1   1 
ATOM   1881 O  OD2   . ASP A 1 236 ? -4.914  15.205  -29.577 1.00 22.20  -1 235 ASP A OD2   1 
ATOM   1882 N  N     . ASP A 1 237 ? -4.103  15.629  -24.219 1.00 13.17  ?  236 ASP A N     1 
ATOM   1883 C  CA    . ASP A 1 237 ? -4.621  14.845  -23.101 1.00 13.87  ?  236 ASP A CA    1 
ATOM   1884 C  C     . ASP A 1 237 ? -5.909  14.124  -23.469 1.00 16.20  ?  236 ASP A C     1 
ATOM   1885 O  O     . ASP A 1 237 ? -6.156  13.007  -22.996 1.00 15.69  ?  236 ASP A O     1 
ATOM   1886 C  CB    . ASP A 1 237 ? -4.857  15.733  -21.884 1.00 16.43  ?  236 ASP A CB    1 
ATOM   1887 C  CG    . ASP A 1 237 ? -3.571  16.220  -21.258 1.00 16.38  ?  236 ASP A CG    1 
ATOM   1888 O  OD1   . ASP A 1 237 ? -2.502  16.078  -21.902 1.00 14.77  ?  236 ASP A OD1   1 
ATOM   1889 O  OD2   . ASP A 1 237 ? -3.640  16.744  -20.122 1.00 13.83  -1 236 ASP A OD2   1 
ATOM   1890 N  N     . ARG A 1 238 ? -6.761  14.752  -24.289 1.00 17.17  ?  237 ARG A N     1 
ATOM   1891 C  CA    . ARG A 1 238 ? -8.007  14.094  -24.676 1.00 15.89  ?  237 ARG A CA    1 
ATOM   1892 C  C     . ARG A 1 238 ? -7.722  12.801  -25.430 1.00 17.53  ?  237 ARG A C     1 
ATOM   1893 O  O     . ARG A 1 238 ? -8.323  11.757  -25.145 1.00 14.54  ?  237 ARG A O     1 
ATOM   1894 C  CB    . ARG A 1 238 ? -8.878  15.029  -25.522 1.00 15.68  ?  237 ARG A CB    1 
ATOM   1895 C  CG    . ARG A 1 238 ? -10.283 14.491  -25.764 1.00 16.50  ?  237 ARG A CG    1 
ATOM   1896 C  CD    . ARG A 1 238 ? -10.833 14.928  -27.121 1.00 17.89  ?  237 ARG A CD    1 
ATOM   1897 N  NE    . ARG A 1 238 ? -9.916  14.555  -28.189 1.00 21.03  ?  237 ARG A NE    1 
ATOM   1898 C  CZ    . ARG A 1 238 ? -9.789  13.320  -28.667 1.00 20.44  ?  237 ARG A CZ    1 
ATOM   1899 N  NH1   . ARG A 1 238 ? -10.546 12.336  -28.191 1.00 14.61  1  237 ARG A NH1   1 
ATOM   1900 N  NH2   . ARG A 1 238 ? -8.913  13.070  -29.628 1.00 20.52  ?  237 ARG A NH2   1 
ATOM   1901 N  N     . ASP A 1 239 ? -6.791  12.849  -26.391 1.00 18.35  ?  238 ASP A N     1 
ATOM   1902 C  CA    . ASP A 1 239 ? -6.444  11.642  -27.133 1.00 18.33  ?  238 ASP A CA    1 
ATOM   1903 C  C     . ASP A 1 239 ? -5.737  10.627  -26.243 1.00 16.01  ?  238 ASP A C     1 
ATOM   1904 O  O     . ASP A 1 239 ? -5.972  9.417   -26.363 1.00 16.15  ?  238 ASP A O     1 
ATOM   1905 C  CB    . ASP A 1 239 ? -5.571  11.999  -28.337 1.00 18.30  ?  238 ASP A CB    1 
ATOM   1906 C  CG    . ASP A 1 239 ? -5.159  10.779  -29.135 1.00 22.29  ?  238 ASP A CG    1 
ATOM   1907 O  OD1   . ASP A 1 239 ? -6.057  10.115  -29.700 1.00 22.26  ?  238 ASP A OD1   1 
ATOM   1908 O  OD2   . ASP A 1 239 ? -3.944  10.482  -29.198 1.00 21.14  -1 238 ASP A OD2   1 
ATOM   1909 N  N     . ALA A 1 240 ? -4.850  11.093  -25.361 1.00 14.97  ?  239 ALA A N     1 
ATOM   1910 C  CA    . ALA A 1 240 ? -4.173  10.167  -24.456 1.00 16.53  ?  239 ALA A CA    1 
ATOM   1911 C  C     . ALA A 1 240 ? -5.181  9.419   -23.586 1.00 17.16  ?  239 ALA A C     1 
ATOM   1912 O  O     . ALA A 1 240 ? -5.083  8.196   -23.413 1.00 16.19  ?  239 ALA A O     1 
ATOM   1913 C  CB    . ALA A 1 240 ? -3.156  10.921  -23.594 1.00 16.85  ?  239 ALA A CB    1 
ATOM   1914 N  N     . LEU A 1 241 ? -6.176  10.140  -23.055 1.00 13.30  ?  240 LEU A N     1 
ATOM   1915 C  CA    . LEU A 1 241 ? -7.222  9.511   -22.256 1.00 13.85  ?  240 LEU A CA    1 
ATOM   1916 C  C     . LEU A 1 241 ? -8.078  8.572   -23.093 1.00 12.42  ?  240 LEU A C     1 
ATOM   1917 O  O     . LEU A 1 241 ? -8.489  7.517   -22.608 1.00 15.04  ?  240 LEU A O     1 
ATOM   1918 C  CB    . LEU A 1 241 ? -8.117  10.569  -21.608 1.00 15.37  ?  240 LEU A CB    1 
ATOM   1919 C  CG    . LEU A 1 241 ? -7.724  11.180  -20.265 1.00 25.39  ?  240 LEU A CG    1 
ATOM   1920 C  CD1   . LEU A 1 241 ? -8.783  12.199  -19.848 1.00 26.90  ?  240 LEU A CD1   1 
ATOM   1921 C  CD2   . LEU A 1 241 ? -7.559  10.106  -19.191 1.00 22.91  ?  240 LEU A CD2   1 
ATOM   1922 N  N     . GLU A 1 242 ? -8.400  8.954   -24.331 1.00 13.50  ?  241 GLU A N     1 
ATOM   1923 C  CA    . GLU A 1 242 ? -9.188  8.058   -25.176 1.00 17.12  ?  241 GLU A CA    1 
ATOM   1924 C  C     . GLU A 1 242 ? -8.465  6.732   -25.381 1.00 19.56  ?  241 GLU A C     1 
ATOM   1925 O  O     . GLU A 1 242 ? -9.057  5.658   -25.214 1.00 18.83  ?  241 GLU A O     1 
ATOM   1926 C  CB    . GLU A 1 242 ? -9.493  8.717   -26.522 1.00 18.41  ?  241 GLU A CB    1 
ATOM   1927 C  CG    . GLU A 1 242 ? -10.395 7.873   -27.420 1.00 19.41  ?  241 GLU A CG    1 
ATOM   1928 C  CD    . GLU A 1 242 ? -10.510 8.413   -28.840 1.00 20.97  ?  241 GLU A CD    1 
ATOM   1929 O  OE1   . GLU A 1 242 ? -10.345 9.634   -29.056 1.00 22.52  ?  241 GLU A OE1   1 
ATOM   1930 O  OE2   . GLU A 1 242 ? -10.763 7.605   -29.751 1.00 25.65  -1 241 GLU A OE2   1 
ATOM   1931 N  N     . GLN A 1 243 ? -7.178  6.788   -25.742 1.00 17.02  ?  242 GLN A N     1 
ATOM   1932 C  CA    . GLN A 1 243 ? -6.410  5.556   -25.940 1.00 17.71  ?  242 GLN A CA    1 
ATOM   1933 C  C     . GLN A 1 243 ? -6.339  4.736   -24.657 1.00 16.36  ?  242 GLN A C     1 
ATOM   1934 O  O     . GLN A 1 243 ? -6.503  3.508   -24.677 1.00 15.22  ?  242 GLN A O     1 
ATOM   1935 C  CB    . GLN A 1 243 ? -4.991  5.870   -26.418 1.00 18.15  ?  242 GLN A CB    1 
ATOM   1936 C  CG    . GLN A 1 243 ? -4.865  6.577   -27.754 1.00 25.01  ?  242 GLN A CG    1 
ATOM   1937 C  CD    . GLN A 1 243 ? -3.404  6.713   -28.194 1.00 35.01  ?  242 GLN A CD    1 
ATOM   1938 O  OE1   . GLN A 1 243 ? -2.986  7.757   -28.708 1.00 41.75  ?  242 GLN A OE1   1 
ATOM   1939 N  NE2   . GLN A 1 243 ? -2.623  5.655   -27.988 1.00 31.83  ?  242 GLN A NE2   1 
ATOM   1940 N  N     . PHE A 1 244 ? -6.064  5.399   -23.530 1.00 15.40  ?  243 PHE A N     1 
ATOM   1941 C  CA    . PHE A 1 244 ? -5.920  4.690   -22.262 1.00 14.23  ?  243 PHE A CA    1 
ATOM   1942 C  C     . PHE A 1 244 ? -7.233  4.030   -21.842 1.00 16.49  ?  243 PHE A C     1 
ATOM   1943 O  O     . PHE A 1 244 ? -7.253  2.865   -21.424 1.00 15.60  ?  243 PHE A O     1 
ATOM   1944 C  CB    . PHE A 1 244 ? -5.420  5.681   -21.209 1.00 12.38  ?  243 PHE A CB    1 
ATOM   1945 C  CG    . PHE A 1 244 ? -5.283  5.118   -19.833 1.00 16.61  ?  243 PHE A CG    1 
ATOM   1946 C  CD1   . PHE A 1 244 ? -4.927  3.796   -19.624 1.00 15.22  ?  243 PHE A CD1   1 
ATOM   1947 C  CD2   . PHE A 1 244 ? -5.505  5.933   -18.733 1.00 18.48  ?  243 PHE A CD2   1 
ATOM   1948 C  CE1   . PHE A 1 244 ? -4.805  3.301   -18.336 1.00 19.49  ?  243 PHE A CE1   1 
ATOM   1949 C  CE2   . PHE A 1 244 ? -5.384  5.446   -17.450 1.00 19.97  ?  243 PHE A CE2   1 
ATOM   1950 C  CZ    . PHE A 1 244 ? -5.042  4.127   -17.249 1.00 19.31  ?  243 PHE A CZ    1 
ATOM   1951 N  N     . VAL A 1 245 ? -8.346  4.761   -21.953 1.00 15.58  ?  244 VAL A N     1 
ATOM   1952 C  CA    . VAL A 1 245 ? -9.643  4.212   -21.569 1.00 13.55  ?  244 VAL A CA    1 
ATOM   1953 C  C     . VAL A 1 245 ? -10.032 3.069   -22.499 1.00 14.55  ?  244 VAL A C     1 
ATOM   1954 O  O     . VAL A 1 245 ? -10.548 2.037   -22.054 1.00 15.64  ?  244 VAL A O     1 
ATOM   1955 C  CB    . VAL A 1 245 ? -10.707 5.327   -21.559 1.00 12.67  ?  244 VAL A CB    1 
ATOM   1956 C  CG1   . VAL A 1 245 ? -12.116 4.737   -21.540 1.00 13.64  ?  244 VAL A CG1   1 
ATOM   1957 C  CG2   . VAL A 1 245 ? -10.497 6.250   -20.368 1.00 14.29  ?  244 VAL A CG2   1 
ATOM   1958 N  N     . GLN A 1 246 ? -9.796  3.226   -23.804 1.00 16.23  ?  245 GLN A N     1 
ATOM   1959 C  CA    . GLN A 1 246 ? -10.080 2.130   -24.722 1.00 19.19  ?  245 GLN A CA    1 
ATOM   1960 C  C     . GLN A 1 246 ? -9.257  0.895   -24.373 1.00 19.52  ?  245 GLN A C     1 
ATOM   1961 O  O     . GLN A 1 246 ? -9.770  -0.228  -24.415 1.00 14.93  ?  245 GLN A O     1 
ATOM   1962 C  CB    . GLN A 1 246 ? -9.808  2.555   -26.166 1.00 21.31  ?  245 GLN A CB    1 
ATOM   1963 C  CG    . GLN A 1 246 ? -10.159 1.475   -27.178 1.00 22.58  ?  245 GLN A CG    1 
ATOM   1964 C  CD    . GLN A 1 246 ? -11.637 1.137   -27.165 1.00 28.65  ?  245 GLN A CD    1 
ATOM   1965 O  OE1   . GLN A 1 246 ? -12.449 1.880   -27.712 1.00 30.46  ?  245 GLN A OE1   1 
ATOM   1966 N  NE2   . GLN A 1 246 ? -11.995 0.017   -26.535 1.00 24.91  ?  245 GLN A NE2   1 
ATOM   1967 N  N     . THR A 1 247 ? -7.985  1.078   -23.994 1.00 19.01  ?  246 THR A N     1 
ATOM   1968 C  CA    . THR A 1 247 ? -7.158  -0.088  -23.680 1.00 19.92  ?  246 THR A CA    1 
ATOM   1969 C  C     . THR A 1 247 ? -7.641  -0.774  -22.403 1.00 17.16  ?  246 THR A C     1 
ATOM   1970 O  O     . THR A 1 247 ? -7.727  -2.016  -22.339 1.00 17.91  ?  246 THR A O     1 
ATOM   1971 C  CB    . THR A 1 247 ? -5.687  0.329   -23.590 1.00 22.92  ?  246 THR A CB    1 
ATOM   1972 O  OG1   . THR A 1 247 ? -5.277  0.857   -24.859 1.00 24.61  ?  246 THR A OG1   1 
ATOM   1973 C  CG2   . THR A 1 247 ? -4.790  -0.861  -23.238 1.00 20.52  ?  246 THR A CG2   1 
ATOM   1974 N  N     . MET A 1 248 ? -8.010  0.018   -21.392 1.00 15.34  ?  247 MET A N     1 
ATOM   1975 C  CA    . MET A 1 248 ? -8.636  -0.557  -20.200 1.00 15.85  ?  247 MET A CA    1 
ATOM   1976 C  C     . MET A 1 248 ? -9.876  -1.368  -20.567 1.00 19.10  ?  247 MET A C     1 
ATOM   1977 O  O     . MET A 1 248 ? -10.012 -2.530  -20.162 1.00 21.18  ?  247 MET A O     1 
ATOM   1978 C  CB    . MET A 1 248 ? -8.997  0.540   -19.194 1.00 19.23  ?  247 MET A CB    1 
ATOM   1979 C  CG    . MET A 1 248 ? -7.819  1.060   -18.369 1.00 21.27  ?  247 MET A CG    1 
ATOM   1980 S  SD    . MET A 1 248 ? -8.323  2.280   -17.133 1.00 22.70  ?  247 MET A SD    1 
ATOM   1981 C  CE    . MET A 1 248 ? -9.056  1.260   -15.878 1.00 30.76  ?  247 MET A CE    1 
ATOM   1982 N  N     . LEU A 1 249 ? -10.792 -0.767  -21.334 1.00 16.41  ?  248 LEU A N     1 
ATOM   1983 C  CA    . LEU A 1 249 ? -12.003 -1.469  -21.757 1.00 19.13  ?  248 LEU A CA    1 
ATOM   1984 C  C     . LEU A 1 249 ? -11.672 -2.759  -22.498 1.00 21.34  ?  248 LEU A C     1 
ATOM   1985 O  O     . LEU A 1 249 ? -12.324 -3.790  -22.288 1.00 22.37  ?  248 LEU A O     1 
ATOM   1986 C  CB    . LEU A 1 249 ? -12.856 -0.554  -22.637 1.00 17.69  ?  248 LEU A CB    1 
ATOM   1987 C  CG    . LEU A 1 249 ? -13.644 0.547   -21.924 1.00 20.35  ?  248 LEU A CG    1 
ATOM   1988 C  CD1   . LEU A 1 249 ? -14.180 1.578   -22.910 1.00 16.88  ?  248 LEU A CD1   1 
ATOM   1989 C  CD2   . LEU A 1 249 ? -14.786 -0.068  -21.109 1.00 19.35  ?  248 LEU A CD2   1 
ATOM   1990 N  N     . ASP A 1 250 ? -10.656 -2.720  -23.366 1.00 19.69  ?  249 ASP A N     1 
ATOM   1991 C  CA    . ASP A 1 250 ? -10.219 -3.905  -24.093 1.00 21.31  ?  249 ASP A CA    1 
ATOM   1992 C  C     . ASP A 1 250 ? -9.696  -4.990  -23.171 1.00 22.76  ?  249 ASP A C     1 
ATOM   1993 O  O     . ASP A 1 250 ? -9.597  -6.150  -23.591 1.00 23.30  ?  249 ASP A O     1 
ATOM   1994 C  CB    . ASP A 1 250 ? -9.104  -3.558  -25.079 1.00 24.46  ?  249 ASP A CB    1 
ATOM   1995 C  CG    . ASP A 1 250 ? -9.575  -2.711  -26.227 1.00 27.22  ?  249 ASP A CG    1 
ATOM   1996 O  OD1   . ASP A 1 250 ? -10.789 -2.434  -26.328 1.00 28.48  ?  249 ASP A OD1   1 
ATOM   1997 O  OD2   . ASP A 1 250 ? -8.711  -2.319  -27.028 1.00 29.21  -1 249 ASP A OD2   1 
ATOM   1998 N  N     . ASN A 1 251 ? -9.298  -4.640  -21.951 1.00 21.57  ?  250 ASN A N     1 
ATOM   1999 C  CA    . ASN A 1 251 ? -8.778  -5.651  -21.041 1.00 19.37  ?  250 ASN A CA    1 
ATOM   2000 C  C     . ASN A 1 251 ? -9.809  -6.175  -20.040 1.00 21.89  ?  250 ASN A C     1 
ATOM   2001 O  O     . ASN A 1 251 ? -9.448  -6.958  -19.152 1.00 20.21  ?  250 ASN A O     1 
ATOM   2002 C  CB    . ASN A 1 251 ? -7.547  -5.108  -20.323 1.00 17.64  ?  250 ASN A CB    1 
ATOM   2003 C  CG    . ASN A 1 251 ? -6.309  -5.201  -21.188 1.00 22.40  ?  250 ASN A CG    1 
ATOM   2004 O  OD1   . ASN A 1 251 ? -5.651  -6.240  -21.224 1.00 22.21  ?  250 ASN A OD1   1 
ATOM   2005 N  ND2   . ASN A 1 251 ? -5.998  -4.125  -21.915 1.00 20.55  ?  250 ASN A ND2   1 
ATOM   2006 N  N     . PHE A 1 252 ? -11.077 -5.782  -20.163 1.00 17.59  ?  251 PHE A N     1 
ATOM   2007 C  CA    . PHE A 1 252 ? -12.128 -6.465  -19.421 1.00 19.20  ?  251 PHE A CA    1 
ATOM   2008 C  C     . PHE A 1 252 ? -12.370 -7.838  -20.046 1.00 22.19  ?  251 PHE A C     1 
ATOM   2009 O  O     . PHE A 1 252 ? -12.332 -7.990  -21.269 1.00 21.39  ?  251 PHE A O     1 
ATOM   2010 C  CB    . PHE A 1 252 ? -13.428 -5.656  -19.433 1.00 16.54  ?  251 PHE A CB    1 
ATOM   2011 C  CG    . PHE A 1 252 ? -13.470 -4.525  -18.431 1.00 17.71  ?  251 PHE A CG    1 
ATOM   2012 C  CD1   . PHE A 1 252 ? -12.796 -3.335  -18.677 1.00 16.12  ?  251 PHE A CD1   1 
ATOM   2013 C  CD2   . PHE A 1 252 ? -14.219 -4.643  -17.263 1.00 17.22  ?  251 PHE A CD2   1 
ATOM   2014 C  CE1   . PHE A 1 252 ? -12.849 -2.286  -17.768 1.00 18.37  ?  251 PHE A CE1   1 
ATOM   2015 C  CE2   . PHE A 1 252 ? -14.279 -3.605  -16.343 1.00 20.73  ?  251 PHE A CE2   1 
ATOM   2016 C  CZ    . PHE A 1 252 ? -13.597 -2.423  -16.597 1.00 21.93  ?  251 PHE A CZ    1 
ATOM   2017 N  N     . HIS A 1 253 ? -12.604 -8.845  -19.203 1.00 19.18  ?  252 HIS A N     1 
ATOM   2018 C  CA    . HIS A 1 253 ? -12.909 -10.195 -19.664 1.00 21.06  ?  252 HIS A CA    1 
ATOM   2019 C  C     . HIS A 1 253 ? -14.149 -10.704 -18.949 1.00 20.93  ?  252 HIS A C     1 
ATOM   2020 O  O     . HIS A 1 253 ? -14.265 -10.558 -17.730 1.00 20.12  ?  252 HIS A O     1 
ATOM   2021 C  CB    . HIS A 1 253 ? -11.739 -11.153 -19.415 1.00 23.55  ?  252 HIS A CB    1 
ATOM   2022 C  CG    . HIS A 1 253 ? -10.454 -10.713 -20.045 1.00 30.82  ?  252 HIS A CG    1 
ATOM   2023 N  ND1   . HIS A 1 253 ? -10.268 -10.681 -21.411 1.00 32.73  ?  252 HIS A ND1   1 
ATOM   2024 C  CD2   . HIS A 1 253 ? -9.292  -10.285 -19.496 1.00 31.17  ?  252 HIS A CD2   1 
ATOM   2025 C  CE1   . HIS A 1 253 ? -9.046  -10.252 -21.674 1.00 33.19  ?  252 HIS A CE1   1 
ATOM   2026 N  NE2   . HIS A 1 253 ? -8.434  -10.005 -20.530 1.00 30.57  ?  252 HIS A NE2   1 
ATOM   2027 N  N     . ASP A 1 254 ? -15.073 -11.290 -19.706 1.00 20.03  ?  253 ASP A N     1 
ATOM   2028 C  CA    . ASP A 1 254 ? -16.229 -11.938 -19.100 1.00 22.57  ?  253 ASP A CA    1 
ATOM   2029 C  C     . ASP A 1 254 ? -15.778 -13.109 -18.237 1.00 21.73  ?  253 ASP A C     1 
ATOM   2030 O  O     . ASP A 1 254 ? -14.954 -13.926 -18.655 1.00 21.69  ?  253 ASP A O     1 
ATOM   2031 C  CB    . ASP A 1 254 ? -17.201 -12.405 -20.185 1.00 23.99  ?  253 ASP A CB    1 
ATOM   2032 C  CG    . ASP A 1 254 ? -17.831 -11.243 -20.930 1.00 29.82  ?  253 ASP A CG    1 
ATOM   2033 O  OD1   . ASP A 1 254 ? -17.797 -10.111 -20.398 1.00 27.26  ?  253 ASP A OD1   1 
ATOM   2034 O  OD2   . ASP A 1 254 ? -18.362 -11.458 -22.041 1.00 33.33  -1 253 ASP A OD2   1 
ATOM   2035 N  N     . THR A 1 255 ? -16.319 -13.182 -17.024 1.00 20.95  ?  254 THR A N     1 
ATOM   2036 C  CA    . THR A 1 255 ? -15.838 -14.087 -15.989 1.00 19.68  ?  254 THR A CA    1 
ATOM   2037 C  C     . THR A 1 255 ? -17.045 -14.785 -15.390 1.00 20.57  ?  254 THR A C     1 
ATOM   2038 O  O     . THR A 1 255 ? -17.931 -14.125 -14.836 1.00 22.11  ?  254 THR A O     1 
ATOM   2039 C  CB    . THR A 1 255 ? -15.067 -13.315 -14.912 1.00 20.07  ?  254 THR A CB    1 
ATOM   2040 O  OG1   . THR A 1 255 ? -14.020 -12.556 -15.534 1.00 20.42  ?  254 THR A OG1   1 
ATOM   2041 C  CG2   . THR A 1 255 ? -14.463 -14.264 -13.879 1.00 19.82  ?  254 THR A CG2   1 
ATOM   2042 N  N     . TRP A 1 256 ? -17.077 -16.109 -15.508 1.00 18.05  ?  255 TRP A N     1 
ATOM   2043 C  CA    . TRP A 1 256 ? -18.221 -16.883 -15.051 1.00 20.67  ?  255 TRP A CA    1 
ATOM   2044 C  C     . TRP A 1 256 ? -18.323 -16.850 -13.533 1.00 21.49  ?  255 TRP A C     1 
ATOM   2045 O  O     . TRP A 1 256 ? -17.320 -16.940 -12.823 1.00 26.64  ?  255 TRP A O     1 
ATOM   2046 C  CB    . TRP A 1 256 ? -18.096 -18.326 -15.541 1.00 20.49  ?  255 TRP A CB    1 
ATOM   2047 C  CG    . TRP A 1 256 ? -19.252 -19.229 -15.189 1.00 21.96  ?  255 TRP A CG    1 
ATOM   2048 C  CD1   . TRP A 1 256 ? -19.244 -20.260 -14.290 1.00 25.34  ?  255 TRP A CD1   1 
ATOM   2049 C  CD2   . TRP A 1 256 ? -20.565 -19.207 -15.760 1.00 21.62  ?  255 TRP A CD2   1 
ATOM   2050 N  NE1   . TRP A 1 256 ? -20.477 -20.877 -14.261 1.00 24.95  ?  255 TRP A NE1   1 
ATOM   2051 C  CE2   . TRP A 1 256 ? -21.304 -20.248 -15.154 1.00 25.10  ?  255 TRP A CE2   1 
ATOM   2052 C  CE3   . TRP A 1 256 ? -21.189 -18.412 -16.725 1.00 24.45  ?  255 TRP A CE3   1 
ATOM   2053 C  CZ2   . TRP A 1 256 ? -22.633 -20.502 -15.476 1.00 26.76  ?  255 TRP A CZ2   1 
ATOM   2054 C  CZ3   . TRP A 1 256 ? -22.510 -18.666 -17.041 1.00 24.75  ?  255 TRP A CZ3   1 
ATOM   2055 C  CH2   . TRP A 1 256 ? -23.218 -19.703 -16.421 1.00 28.40  ?  255 TRP A CH2   1 
ATOM   2056 N  N     . ASP A 1 257 ? -19.547 -16.711 -13.039 1.00 19.10  ?  256 ASP A N     1 
ATOM   2057 C  CA    . ASP A 1 257 ? -19.870 -16.878 -11.632 1.00 22.48  ?  256 ASP A CA    1 
ATOM   2058 C  C     . ASP A 1 257 ? -20.901 -17.993 -11.517 1.00 21.14  ?  256 ASP A C     1 
ATOM   2059 O  O     . ASP A 1 257 ? -22.020 -17.880 -12.053 1.00 22.22  ?  256 ASP A O     1 
ATOM   2060 C  CB    . ASP A 1 257 ? -20.397 -15.586 -11.010 1.00 25.44  ?  256 ASP A CB    1 
ATOM   2061 C  CG    . ASP A 1 257 ? -20.671 -15.736 -9.526  1.00 31.83  ?  256 ASP A CG    1 
ATOM   2062 O  OD1   . ASP A 1 257 ? -21.784 -16.150 -9.154  1.00 34.96  ?  256 ASP A OD1   1 
ATOM   2063 O  OD2   . ASP A 1 257 ? -19.752 -15.477 -8.728  1.00 38.51  -1 256 ASP A OD2   1 
ATOM   2064 N  N     . SER A 1 258 ? -20.499 -19.068 -10.831 1.00 22.59  ?  257 SER A N     1 
ATOM   2065 C  CA    . SER A 1 258 ? -21.335 -20.253 -10.697 1.00 25.83  ?  257 SER A CA    1 
ATOM   2066 C  C     . SER A 1 258 ? -22.516 -19.997 -9.770  1.00 27.45  ?  257 SER A C     1 
ATOM   2067 O  O     . SER A 1 258 ? -23.606 -20.536 -9.987  1.00 28.05  ?  257 SER A O     1 
ATOM   2068 C  CB    . SER A 1 258 ? -20.496 -21.421 -10.182 1.00 28.18  ?  257 SER A CB    1 
ATOM   2069 O  OG    . SER A 1 258 ? -19.940 -21.131 -8.912  1.00 29.81  ?  257 SER A OG    1 
ATOM   2070 N  N     . LYS A 1 259 ? -22.320 -19.178 -8.734  1.00 33.15  ?  258 LYS A N     1 
ATOM   2071 C  CA    . LYS A 1 259 ? -23.415 -18.865 -7.821  1.00 36.77  ?  258 LYS A CA    1 
ATOM   2072 C  C     . LYS A 1 259 ? -24.544 -18.143 -8.549  1.00 34.13  ?  258 LYS A C     1 
ATOM   2073 O  O     . LYS A 1 259 ? -25.703 -18.568 -8.498  1.00 34.43  ?  258 LYS A O     1 
ATOM   2074 C  CB    . LYS A 1 259 ? -22.900 -18.024 -6.651  1.00 43.95  ?  258 LYS A CB    1 
ATOM   2075 C  CG    . LYS A 1 259 ? -23.995 -17.526 -5.717  1.00 52.31  ?  258 LYS A CG    1 
ATOM   2076 C  CD    . LYS A 1 259 ? -23.511 -16.369 -4.852  1.00 58.26  ?  258 LYS A CD    1 
ATOM   2077 C  CE    . LYS A 1 259 ? -24.679 -15.685 -4.151  1.00 62.94  ?  258 LYS A CE    1 
ATOM   2078 N  NZ    . LYS A 1 259 ? -24.284 -14.406 -3.493  1.00 64.38  1  258 LYS A NZ    1 
ATOM   2079 N  N     . ASP A 1 260 ? -24.221 -17.048 -9.240  1.00 30.30  ?  259 ASP A N     1 
ATOM   2080 C  CA    . ASP A 1 260 ? -25.229 -16.291 -9.969  1.00 28.99  ?  259 ASP A CA    1 
ATOM   2081 C  C     . ASP A 1 260 ? -25.560 -16.899 -11.321 1.00 29.26  ?  259 ASP A C     1 
ATOM   2082 O  O     . ASP A 1 260 ? -26.502 -16.435 -11.973 1.00 29.71  ?  259 ASP A O     1 
ATOM   2083 C  CB    . ASP A 1 260 ? -24.775 -14.842 -10.164 1.00 29.12  ?  259 ASP A CB    1 
ATOM   2084 C  CG    . ASP A 1 260 ? -24.565 -14.118 -8.851  1.00 35.81  ?  259 ASP A CG    1 
ATOM   2085 O  OD1   . ASP A 1 260 ? -24.818 -14.732 -7.792  1.00 38.52  ?  259 ASP A OD1   1 
ATOM   2086 O  OD2   . ASP A 1 260 ? -24.143 -12.940 -8.877  1.00 37.41  -1 259 ASP A OD2   1 
ATOM   2087 N  N     . GLN A 1 261 ? -24.812 -17.914 -11.753 1.00 28.36  ?  260 GLN A N     1 
ATOM   2088 C  CA    . GLN A 1 261 ? -25.045 -18.569 -13.036 1.00 27.66  ?  260 GLN A CA    1 
ATOM   2089 C  C     . GLN A 1 261 ? -24.998 -17.572 -14.188 1.00 25.47  ?  260 GLN A C     1 
ATOM   2090 O  O     . GLN A 1 261 ? -25.853 -17.589 -15.079 1.00 25.92  ?  260 GLN A O     1 
ATOM   2091 C  CB    . GLN A 1 261 ? -26.372 -19.333 -13.034 1.00 30.92  ?  260 GLN A CB    1 
ATOM   2092 C  CG    . GLN A 1 261 ? -26.304 -20.640 -12.291 1.00 32.95  ?  260 GLN A CG    1 
ATOM   2093 C  CD    . GLN A 1 261 ? -25.340 -21.604 -12.942 1.00 36.10  ?  260 GLN A CD    1 
ATOM   2094 O  OE1   . GLN A 1 261 ? -24.288 -21.931 -12.380 1.00 35.94  ?  260 GLN A OE1   1 
ATOM   2095 N  NE2   . GLN A 1 261 ? -25.689 -22.066 -14.139 1.00 35.46  ?  260 GLN A NE2   1 
ATOM   2096 N  N     . ARG A 1 262 ? -23.996 -16.693 -14.174 1.00 22.30  ?  261 ARG A N     1 
ATOM   2097 C  CA    . ARG A 1 262 ? -23.840 -15.759 -15.288 1.00 24.08  ?  261 ARG A CA    1 
ATOM   2098 C  C     . ARG A 1 262 ? -22.417 -15.233 -15.284 1.00 24.43  ?  261 ARG A C     1 
ATOM   2099 O  O     . ARG A 1 262 ? -21.662 -15.460 -14.345 1.00 26.53  ?  261 ARG A O     1 
ATOM   2100 C  CB    . ARG A 1 262 ? -24.833 -14.592 -15.214 1.00 23.85  ?  261 ARG A CB    1 
ATOM   2101 C  CG    . ARG A 1 262 ? -24.699 -13.736 -13.957 1.00 18.75  ?  261 ARG A CG    1 
ATOM   2102 C  CD    . ARG A 1 262 ? -25.323 -12.349 -14.144 1.00 16.98  ?  261 ARG A CD    1 
ATOM   2103 N  NE    . ARG A 1 262 ? -24.460 -11.476 -14.941 1.00 23.75  ?  261 ARG A NE    1 
ATOM   2104 C  CZ    . ARG A 1 262 ? -24.733 -10.200 -15.211 1.00 25.96  ?  261 ARG A CZ    1 
ATOM   2105 N  NH1   . ARG A 1 262 ? -25.848 -9.647  -14.750 1.00 23.13  1  261 ARG A NH1   1 
ATOM   2106 N  NH2   . ARG A 1 262 ? -23.889 -9.474  -15.939 1.00 23.06  ?  261 ARG A NH2   1 
ATOM   2107 N  N     . SER A 1 263 ? -22.062 -14.507 -16.338 1.00 21.19  ?  262 SER A N     1 
ATOM   2108 C  CA    . SER A 1 263 ? -20.746 -13.893 -16.413 1.00 24.38  ?  262 SER A CA    1 
ATOM   2109 C  C     . SER A 1 263 ? -20.836 -12.426 -16.021 1.00 23.04  ?  262 SER A C     1 
ATOM   2110 O  O     . SER A 1 263 ? -21.870 -11.782 -16.204 1.00 19.33  ?  262 SER A O     1 
ATOM   2111 C  CB    . SER A 1 263 ? -20.153 -14.014 -17.817 1.00 28.89  ?  262 SER A CB    1 
ATOM   2112 O  OG    . SER A 1 263 ? -19.799 -15.353 -18.096 1.00 35.33  ?  262 SER A OG    1 
ATOM   2113 N  N     . TYR A 1 264 ? -19.744 -11.915 -15.447 1.00 20.49  ?  263 TYR A N     1 
ATOM   2114 C  CA    . TYR A 1 264 ? -19.566 -10.489 -15.233 1.00 18.93  ?  263 TYR A CA    1 
ATOM   2115 C  C     . TYR A 1 264 ? -18.269 -10.033 -15.883 1.00 20.21  ?  263 TYR A C     1 
ATOM   2116 O  O     . TYR A 1 264 ? -17.285 -10.777 -15.871 1.00 20.95  ?  263 TYR A O     1 
ATOM   2117 C  CB    . TYR A 1 264 ? -19.518 -10.129 -13.738 1.00 19.31  ?  263 TYR A CB    1 
ATOM   2118 C  CG    . TYR A 1 264 ? -20.770 -10.482 -12.967 1.00 24.10  ?  263 TYR A CG    1 
ATOM   2119 C  CD1   . TYR A 1 264 ? -21.877 -9.650  -12.983 1.00 22.25  ?  263 TYR A CD1   1 
ATOM   2120 C  CD2   . TYR A 1 264 ? -20.836 -11.652 -12.212 1.00 25.28  ?  263 TYR A CD2   1 
ATOM   2121 C  CE1   . TYR A 1 264 ? -23.016 -9.971  -12.271 1.00 23.77  ?  263 TYR A CE1   1 
ATOM   2122 C  CE2   . TYR A 1 264 ? -21.965 -11.978 -11.502 1.00 24.04  ?  263 TYR A CE2   1 
ATOM   2123 C  CZ    . TYR A 1 264 ? -23.052 -11.138 -11.534 1.00 23.99  ?  263 TYR A CZ    1 
ATOM   2124 O  OH    . TYR A 1 264 ? -24.179 -11.470 -10.823 1.00 26.05  ?  263 TYR A OH    1 
ATOM   2125 N  N     . PRO A 1 265 ? -18.219 -8.826  -16.441 1.00 20.05  ?  264 PRO A N     1 
ATOM   2126 C  CA    . PRO A 1 265 ? -16.953 -8.339  -17.003 1.00 22.17  ?  264 PRO A CA    1 
ATOM   2127 C  C     . PRO A 1 265 ? -16.013 -7.935  -15.875 1.00 27.50  ?  264 PRO A C     1 
ATOM   2128 O  O     . PRO A 1 265 ? -16.415 -7.242  -14.944 1.00 36.47  ?  264 PRO A O     1 
ATOM   2129 C  CB    . PRO A 1 265 ? -17.379 -7.136  -17.851 1.00 21.92  ?  264 PRO A CB    1 
ATOM   2130 C  CG    . PRO A 1 265 ? -18.626 -6.631  -17.176 1.00 19.11  ?  264 PRO A CG    1 
ATOM   2131 C  CD    . PRO A 1 265 ? -19.278 -7.800  -16.460 1.00 17.16  ?  264 PRO A CD    1 
ATOM   2132 N  N     . ARG A 1 266 ? -14.766 -8.390  -15.944 1.00 21.45  ?  265 ARG A N     1 
ATOM   2133 C  CA    . ARG A 1 266 ? -13.792 -8.116  -14.898 1.00 18.62  ?  265 ARG A CA    1 
ATOM   2134 C  C     . ARG A 1 266 ? -12.519 -7.569  -15.514 1.00 22.54  ?  265 ARG A C     1 
ATOM   2135 O  O     . ARG A 1 266 ? -11.990 -8.144  -16.474 1.00 19.21  ?  265 ARG A O     1 
ATOM   2136 C  CB    . ARG A 1 266 ? -13.456 -9.376  -14.095 1.00 21.42  ?  265 ARG A CB    1 
ATOM   2137 C  CG    . ARG A 1 266 ? -14.565 -9.872  -13.188 1.00 23.58  ?  265 ARG A CG    1 
ATOM   2138 C  CD    . ARG A 1 266 ? -13.975 -10.662 -12.036 1.00 22.36  ?  265 ARG A CD    1 
ATOM   2139 N  NE    . ARG A 1 266 ? -13.178 -9.801  -11.169 1.00 21.57  ?  265 ARG A NE    1 
ATOM   2140 C  CZ    . ARG A 1 266 ? -13.667 -9.135  -10.131 1.00 19.15  ?  265 ARG A CZ    1 
ATOM   2141 N  NH1   . ARG A 1 266 ? -14.957 -9.237  -9.831  1.00 17.08  1  265 ARG A NH1   1 
ATOM   2142 N  NH2   . ARG A 1 266 ? -12.873 -8.368  -9.391  1.00 18.74  ?  265 ARG A NH2   1 
ATOM   2143 N  N     . LEU A 1 267 ? -12.028 -6.473  -14.945 1.00 19.48  ?  266 LEU A N     1 
ATOM   2144 C  CA    . LEU A 1 267 ? -10.710 -5.942  -15.246 1.00 20.15  ?  266 LEU A CA    1 
ATOM   2145 C  C     . LEU A 1 267 ? -9.751  -6.397  -14.151 1.00 19.24  ?  266 LEU A C     1 
ATOM   2146 O  O     . LEU A 1 267 ? -9.947  -6.069  -12.973 1.00 19.80  ?  266 LEU A O     1 
ATOM   2147 C  CB    . LEU A 1 267 ? -10.754 -4.415  -15.331 1.00 19.66  ?  266 LEU A CB    1 
ATOM   2148 C  CG    . LEU A 1 267 ? -9.451  -3.728  -15.721 1.00 17.91  ?  266 LEU A CG    1 
ATOM   2149 C  CD1   . LEU A 1 267 ? -9.022  -4.176  -17.109 1.00 14.62  ?  266 LEU A CD1   1 
ATOM   2150 C  CD2   . LEU A 1 267 ? -9.664  -2.231  -15.680 1.00 15.28  ?  266 LEU A CD2   1 
ATOM   2151 N  N     . THR A 1 268 ? -8.742  -7.175  -14.536 1.00 15.17  ?  267 THR A N     1 
ATOM   2152 C  CA    . THR A 1 268 ? -7.672  -7.593  -13.642 1.00 18.09  ?  267 THR A CA    1 
ATOM   2153 C  C     . THR A 1 268 ? -6.461  -6.702  -13.872 1.00 18.85  ?  267 THR A C     1 
ATOM   2154 O  O     . THR A 1 268 ? -6.009  -6.550  -15.011 1.00 21.74  ?  267 THR A O     1 
ATOM   2155 C  CB    . THR A 1 268 ? -7.284  -9.056  -13.886 1.00 20.61  ?  267 THR A CB    1 
ATOM   2156 O  OG1   . THR A 1 268 ? -8.416  -9.894  -13.652 1.00 20.79  ?  267 THR A OG1   1 
ATOM   2157 C  CG2   . THR A 1 268 ? -6.162  -9.466  -12.946 1.00 23.01  ?  267 THR A CG2   1 
ATOM   2158 N  N     . VAL A 1 269 ? -5.943  -6.107  -12.805 1.00 19.00  ?  268 VAL A N     1 
ATOM   2159 C  CA    . VAL A 1 269 ? -4.786  -5.223  -12.902 1.00 17.76  ?  268 VAL A CA    1 
ATOM   2160 C  C     . VAL A 1 269 ? -3.793  -5.661  -11.836 1.00 19.63  ?  268 VAL A C     1 
ATOM   2161 O  O     . VAL A 1 269 ? -3.936  -5.310  -10.657 1.00 17.47  ?  268 VAL A O     1 
ATOM   2162 C  CB    . VAL A 1 269 ? -5.155  -3.746  -12.748 1.00 21.31  ?  268 VAL A CB    1 
ATOM   2163 C  CG1   . VAL A 1 269 ? -3.895  -2.889  -12.738 1.00 22.59  ?  268 VAL A CG1   1 
ATOM   2164 C  CG2   . VAL A 1 269 ? -6.081  -3.314  -13.880 1.00 20.46  ?  268 VAL A CG2   1 
ATOM   2165 N  N     . GLU A 1 270 ? -2.787  -6.423  -12.250 1.00 20.85  ?  269 GLU A N     1 
ATOM   2166 C  CA    . GLU A 1 270 ? -1.747  -6.877  -11.340 1.00 23.61  ?  269 GLU A CA    1 
ATOM   2167 C  C     . GLU A 1 270 ? -0.867  -5.718  -10.905 1.00 21.20  ?  269 GLU A C     1 
ATOM   2168 O  O     . GLU A 1 270 ? -0.465  -4.881  -11.720 1.00 21.34  ?  269 GLU A O     1 
ATOM   2169 C  CB    . GLU A 1 270 ? -0.873  -7.938  -12.011 1.00 28.55  ?  269 GLU A CB    1 
ATOM   2170 C  CG    . GLU A 1 270 ? -1.622  -9.166  -12.475 1.00 38.16  ?  269 GLU A CG    1 
ATOM   2171 C  CD    . GLU A 1 270 ? -0.726  -10.384 -12.551 1.00 44.85  ?  269 GLU A CD    1 
ATOM   2172 O  OE1   . GLU A 1 270 ? -1.205  -11.486 -12.212 1.00 48.18  ?  269 GLU A OE1   1 
ATOM   2173 O  OE2   . GLU A 1 270 ? 0.459   -10.232 -12.932 1.00 45.86  -1 269 GLU A OE2   1 
ATOM   2174 N  N     . LEU A 1 271 ? -0.563  -5.678  -9.616  1.00 18.52  ?  270 LEU A N     1 
ATOM   2175 C  CA    . LEU A 1 271 ? 0.504   -4.811  -9.151  1.00 18.45  ?  270 LEU A CA    1 
ATOM   2176 C  C     . LEU A 1 271 ? 1.802   -5.228  -9.840  1.00 18.16  ?  270 LEU A C     1 
ATOM   2177 O  O     . LEU A 1 271 ? 2.085   -6.430  -9.937  1.00 17.77  ?  270 LEU A O     1 
ATOM   2178 C  CB    . LEU A 1 271 ? 0.646   -4.902  -7.631  1.00 17.71  ?  270 LEU A CB    1 
ATOM   2179 C  CG    . LEU A 1 271 ? 1.319   -3.702  -6.959  1.00 19.68  ?  270 LEU A CG    1 
ATOM   2180 C  CD1   . LEU A 1 271 ? 0.397   -2.480  -6.994  1.00 16.85  ?  270 LEU A CD1   1 
ATOM   2181 C  CD2   . LEU A 1 271 ? 1.722   -4.037  -5.525  1.00 24.69  ?  270 LEU A CD2   1 
ATOM   2182 N  N     . PRO A 1 272 ? 2.597   -4.284  -10.351 1.00 19.24  ?  271 PRO A N     1 
ATOM   2183 C  CA    . PRO A 1 272 ? 3.838   -4.654  -11.045 1.00 20.41  ?  271 PRO A CA    1 
ATOM   2184 C  C     . PRO A 1 272 ? 4.990   -5.002  -10.117 1.00 20.83  ?  271 PRO A C     1 
ATOM   2185 O  O     . PRO A 1 272 ? 6.094   -5.270  -10.606 1.00 19.91  ?  271 PRO A O     1 
ATOM   2186 C  CB    . PRO A 1 272 ? 4.158   -3.396  -11.859 1.00 17.74  ?  271 PRO A CB    1 
ATOM   2187 C  CG    . PRO A 1 272 ? 3.613   -2.280  -11.016 1.00 18.10  ?  271 PRO A CG    1 
ATOM   2188 C  CD    . PRO A 1 272 ? 2.367   -2.829  -10.358 1.00 16.95  ?  271 PRO A CD    1 
ATOM   2189 N  N     . VAL A 1 273 ? 4.771   -4.994  -8.805  1.00 18.01  ?  272 VAL A N     1 
ATOM   2190 C  CA    . VAL A 1 273 ? 5.755   -5.399  -7.813  1.00 15.79  ?  272 VAL A CA    1 
ATOM   2191 C  C     . VAL A 1 273 ? 5.066   -6.353  -6.842  1.00 18.32  ?  272 VAL A C     1 
ATOM   2192 O  O     . VAL A 1 273 ? 3.865   -6.602  -6.940  1.00 18.07  ?  272 VAL A O     1 
ATOM   2193 C  CB    . VAL A 1 273 ? 6.373   -4.194  -7.067  1.00 21.52  ?  272 VAL A CB    1 
ATOM   2194 C  CG1   . VAL A 1 273 ? 7.079   -3.253  -8.048  1.00 24.98  ?  272 VAL A CG1   1 
ATOM   2195 C  CG2   . VAL A 1 273 ? 5.297   -3.436  -6.295  1.00 20.26  ?  272 VAL A CG2   1 
ATOM   2196 N  N     . GLN A 1 274 ? 5.842   -6.896  -5.910  1.00 17.99  ?  273 GLN A N     1 
ATOM   2197 C  CA    . GLN A 1 274 ? 5.270   -7.773  -4.895  1.00 18.61  ?  273 GLN A CA    1 
ATOM   2198 C  C     . GLN A 1 274 ? 4.155   -7.041  -4.150  1.00 20.17  ?  273 GLN A C     1 
ATOM   2199 O  O     . GLN A 1 274 ? 4.289   -5.848  -3.850  1.00 21.51  ?  273 GLN A O     1 
ATOM   2200 C  CB    . GLN A 1 274 ? 6.350   -8.223  -3.910  1.00 20.67  ?  273 GLN A CB    1 
ATOM   2201 C  CG    . GLN A 1 274 ? 7.390   -9.163  -4.489  1.00 24.06  ?  273 GLN A CG    1 
ATOM   2202 C  CD    . GLN A 1 274 ? 6.907   -10.597 -4.540  1.00 29.41  ?  273 GLN A CD    1 
ATOM   2203 O  OE1   . GLN A 1 274 ? 5.764   -10.892 -4.198  1.00 30.37  ?  273 GLN A OE1   1 
ATOM   2204 N  NE2   . GLN A 1 274 ? 7.778   -11.500 -4.972  1.00 33.99  ?  273 GLN A NE2   1 
ATOM   2205 N  N     . PRO A 1 275 ? 3.048   -7.723  -3.817  1.00 23.49  ?  274 PRO A N     1 
ATOM   2206 C  CA    . PRO A 1 275 ? 2.858   -9.157  -4.053  1.00 23.11  ?  274 PRO A CA    1 
ATOM   2207 C  C     . PRO A 1 275 ? 2.203   -9.514  -5.383  1.00 25.47  ?  274 PRO A C     1 
ATOM   2208 O  O     . PRO A 1 275 ? 1.666   -10.616 -5.483  1.00 26.20  ?  274 PRO A O     1 
ATOM   2209 C  CB    . PRO A 1 275 ? 1.944   -9.566  -2.901  1.00 23.26  ?  274 PRO A CB    1 
ATOM   2210 C  CG    . PRO A 1 275 ? 1.108   -8.362  -2.672  1.00 21.37  ?  274 PRO A CG    1 
ATOM   2211 C  CD    . PRO A 1 275 ? 2.008   -7.177  -2.924  1.00 21.11  ?  274 PRO A CD    1 
ATOM   2212 N  N     . TYR A 1 276 ? 2.226   -8.611  -6.366  1.00 19.17  ?  275 TYR A N     1 
ATOM   2213 C  CA    . TYR A 1 276 ? 1.696   -8.896  -7.703  1.00 21.15  ?  275 TYR A CA    1 
ATOM   2214 C  C     . TYR A 1 276 ? 0.208   -9.237  -7.669  1.00 23.77  ?  275 TYR A C     1 
ATOM   2215 O  O     . TYR A 1 276 ? -0.278  -10.032 -8.477  1.00 25.08  ?  275 TYR A O     1 
ATOM   2216 C  CB    . TYR A 1 276 ? 2.482   -10.025 -8.384  1.00 21.83  ?  275 TYR A CB    1 
ATOM   2217 C  CG    . TYR A 1 276 ? 3.985   -9.793  -8.457  1.00 21.04  ?  275 TYR A CG    1 
ATOM   2218 C  CD1   . TYR A 1 276 ? 4.513   -8.784  -9.250  1.00 21.40  ?  275 TYR A CD1   1 
ATOM   2219 C  CD2   . TYR A 1 276 ? 4.872   -10.603 -7.753  1.00 26.67  ?  275 TYR A CD2   1 
ATOM   2220 C  CE1   . TYR A 1 276 ? 5.885   -8.571  -9.331  1.00 23.10  ?  275 TYR A CE1   1 
ATOM   2221 C  CE2   . TYR A 1 276 ? 6.251   -10.399 -7.831  1.00 28.88  ?  275 TYR A CE2   1 
ATOM   2222 C  CZ    . TYR A 1 276 ? 6.745   -9.382  -8.625  1.00 26.33  ?  275 TYR A CZ    1 
ATOM   2223 O  OH    . TYR A 1 276 ? 8.101   -9.167  -8.709  1.00 30.24  ?  275 TYR A OH    1 
ATOM   2224 N  N     . ASN A 1 277 ? -0.528  -8.644  -6.735  1.00 23.31  ?  276 ASN A N     1 
ATOM   2225 C  CA    . ASN A 1 277 ? -1.941  -8.948  -6.574  1.00 23.89  ?  276 ASN A CA    1 
ATOM   2226 C  C     . ASN A 1 277 ? -2.787  -8.144  -7.551  1.00 22.83  ?  276 ASN A C     1 
ATOM   2227 O  O     . ASN A 1 277 ? -2.406  -7.056  -7.991  1.00 21.37  ?  276 ASN A O     1 
ATOM   2228 C  CB    . ASN A 1 277 ? -2.400  -8.636  -5.150  1.00 20.63  ?  276 ASN A CB    1 
ATOM   2229 C  CG    . ASN A 1 277 ? -2.154  -7.182  -4.772  1.00 25.68  ?  276 ASN A CG    1 
ATOM   2230 O  OD1   . ASN A 1 277 ? -1.028  -6.683  -4.879  1.00 23.93  ?  276 ASN A OD1   1 
ATOM   2231 N  ND2   . ASN A 1 277 ? -3.211  -6.485  -4.366  1.00 25.39  ?  276 ASN A ND2   1 
ATOM   2232 N  N     . ASP A 1 278 ? -3.957  -8.688  -7.870  1.00 21.30  ?  277 ASP A N     1 
ATOM   2233 C  CA    . ASP A 1 278 ? -4.973  -7.962  -8.624  1.00 18.16  ?  277 ASP A CA    1 
ATOM   2234 C  C     . ASP A 1 278 ? -5.531  -6.852  -7.745  1.00 21.08  ?  277 ASP A C     1 
ATOM   2235 O  O     . ASP A 1 278 ? -6.260  -7.120  -6.783  1.00 20.43  ?  277 ASP A O     1 
ATOM   2236 C  CB    . ASP A 1 278 ? -6.073  -8.922  -9.070  1.00 19.78  ?  277 ASP A CB    1 
ATOM   2237 C  CG    . ASP A 1 278 ? -7.219  -8.223  -9.777  1.00 19.92  ?  277 ASP A CG    1 
ATOM   2238 O  OD1   . ASP A 1 278 ? -7.051  -7.067  -10.235 1.00 18.26  ?  277 ASP A OD1   1 
ATOM   2239 O  OD2   . ASP A 1 278 ? -8.303  -8.829  -9.862  1.00 20.48  -1 277 ASP A OD2   1 
ATOM   2240 N  N     . VAL A 1 279 ? -5.197  -5.599  -8.068  1.00 17.33  ?  278 VAL A N     1 
ATOM   2241 C  CA    . VAL A 1 279 ? -5.613  -4.494  -7.214  1.00 21.39  ?  278 VAL A CA    1 
ATOM   2242 C  C     . VAL A 1 279 ? -7.127  -4.281  -7.250  1.00 21.25  ?  278 VAL A C     1 
ATOM   2243 O  O     . VAL A 1 279 ? -7.679  -3.641  -6.349  1.00 20.33  ?  278 VAL A O     1 
ATOM   2244 C  CB    . VAL A 1 279 ? -4.842  -3.213  -7.598  1.00 24.39  ?  278 VAL A CB    1 
ATOM   2245 C  CG1   . VAL A 1 279 ? -3.349  -3.407  -7.338  1.00 26.88  ?  278 VAL A CG1   1 
ATOM   2246 C  CG2   . VAL A 1 279 ? -5.070  -2.863  -9.050  1.00 27.95  ?  278 VAL A CG2   1 
ATOM   2247 N  N     . PHE A 1 280 ? -7.821  -4.829  -8.248  1.00 20.49  ?  279 PHE A N     1 
ATOM   2248 C  CA    . PHE A 1 280 ? -9.273  -4.728  -8.360  1.00 18.57  ?  279 PHE A CA    1 
ATOM   2249 C  C     . PHE A 1 280 ? -10.009 -5.950  -7.809  1.00 20.19  ?  279 PHE A C     1 
ATOM   2250 O  O     . PHE A 1 280 ? -11.230 -6.054  -7.980  1.00 18.21  ?  279 PHE A O     1 
ATOM   2251 C  CB    . PHE A 1 280 ? -9.675  -4.525  -9.822  1.00 20.96  ?  279 PHE A CB    1 
ATOM   2252 C  CG    . PHE A 1 280 ? -9.479  -3.122  -10.326 1.00 23.61  ?  279 PHE A CG    1 
ATOM   2253 C  CD1   . PHE A 1 280 ? -10.162 -2.066  -9.751  1.00 29.71  ?  279 PHE A CD1   1 
ATOM   2254 C  CD2   . PHE A 1 280 ? -8.632  -2.863  -11.385 1.00 27.01  ?  279 PHE A CD2   1 
ATOM   2255 C  CE1   . PHE A 1 280 ? -9.990  -0.775  -10.213 1.00 33.43  ?  279 PHE A CE1   1 
ATOM   2256 C  CE2   . PHE A 1 280 ? -8.459  -1.568  -11.856 1.00 30.58  ?  279 PHE A CE2   1 
ATOM   2257 C  CZ    . PHE A 1 280 ? -9.140  -0.528  -11.270 1.00 31.62  ?  279 PHE A CZ    1 
ATOM   2258 N  N     . GLU A 1 281 ? -9.305  -6.867  -7.141  1.00 20.65  ?  280 GLU A N     1 
ATOM   2259 C  CA    . GLU A 1 281 ? -9.901  -8.157  -6.800  1.00 23.90  ?  280 GLU A CA    1 
ATOM   2260 C  C     . GLU A 1 281 ? -11.105 -8.015  -5.874  1.00 24.39  ?  280 GLU A C     1 
ATOM   2261 O  O     . GLU A 1 281 ? -12.007 -8.858  -5.905  1.00 27.16  ?  280 GLU A O     1 
ATOM   2262 C  CB    . GLU A 1 281 ? -8.849  -9.067  -6.161  1.00 26.19  ?  280 GLU A CB    1 
ATOM   2263 C  CG    . GLU A 1 281 ? -8.240  -8.506  -4.884  1.00 30.10  ?  280 GLU A CG    1 
ATOM   2264 C  CD    . GLU A 1 281 ? -6.952  -9.219  -4.496  1.00 37.84  ?  280 GLU A CD    1 
ATOM   2265 O  OE1   . GLU A 1 281 ? -6.784  -10.395 -4.885  1.00 37.74  ?  280 GLU A OE1   1 
ATOM   2266 O  OE2   . GLU A 1 281 ? -6.104  -8.594  -3.822  1.00 39.78  -1 280 GLU A OE2   1 
ATOM   2267 N  N     . LYS A 1 282 ? -11.148 -6.967  -5.054  1.00 21.24  ?  281 LYS A N     1 
ATOM   2268 C  CA    . LYS A 1 282 ? -12.248 -6.824  -4.105  1.00 25.92  ?  281 LYS A CA    1 
ATOM   2269 C  C     . LYS A 1 282 ? -13.549 -6.348  -4.748  1.00 23.23  ?  281 LYS A C     1 
ATOM   2270 O  O     . LYS A 1 282 ? -14.621 -6.546  -4.163  1.00 22.58  ?  281 LYS A O     1 
ATOM   2271 C  CB    . LYS A 1 282 ? -11.852 -5.868  -2.974  1.00 31.53  ?  281 LYS A CB    1 
ATOM   2272 C  CG    . LYS A 1 282 ? -11.125 -6.541  -1.812  1.00 39.74  ?  281 LYS A CG    1 
ATOM   2273 C  CD    . LYS A 1 282 ? -9.626  -6.320  -1.877  1.00 47.55  ?  281 LYS A CD    1 
ATOM   2274 C  CE    . LYS A 1 282 ? -8.915  -6.919  -0.666  1.00 50.22  ?  281 LYS A CE    1 
ATOM   2275 N  NZ    . LYS A 1 282 ? -7.522  -6.392  -0.534  1.00 49.93  1  281 LYS A NZ    1 
ATOM   2276 N  N     . MET A 1 283 ? -13.494 -5.734  -5.926  1.00 19.88  ?  282 MET A N     1 
ATOM   2277 C  CA    . MET A 1 283 ? -14.718 -5.290  -6.578  1.00 19.58  ?  282 MET A CA    1 
ATOM   2278 C  C     . MET A 1 283 ? -15.542 -6.490  -7.025  1.00 19.84  ?  282 MET A C     1 
ATOM   2279 O  O     . MET A 1 283 ? -15.004 -7.445  -7.592  1.00 23.08  ?  282 MET A O     1 
ATOM   2280 C  CB    . MET A 1 283 ? -14.394 -4.403  -7.775  1.00 22.84  ?  282 MET A CB    1 
ATOM   2281 C  CG    . MET A 1 283 ? -13.779 -3.075  -7.402  1.00 29.06  ?  282 MET A CG    1 
ATOM   2282 S  SD    . MET A 1 283 ? -13.420 -2.073  -8.853  1.00 33.94  ?  282 MET A SD    1 
ATOM   2283 C  CE    . MET A 1 283 ? -15.003 -2.147  -9.707  1.00 23.72  ?  282 MET A CE    1 
ATOM   2284 N  N     . THR A 1 284 ? -16.848 -6.441  -6.773  1.00 16.64  ?  283 THR A N     1 
ATOM   2285 C  CA    . THR A 1 284 ? -17.718 -7.538  -7.166  1.00 20.22  ?  283 THR A CA    1 
ATOM   2286 C  C     . THR A 1 284 ? -17.947 -7.515  -8.677  1.00 18.92  ?  283 THR A C     1 
ATOM   2287 O  O     . THR A 1 284 ? -17.554 -6.582  -9.382  1.00 17.10  ?  283 THR A O     1 
ATOM   2288 C  CB    . THR A 1 284 ? -19.056 -7.471  -6.424  1.00 22.15  ?  283 THR A CB    1 
ATOM   2289 O  OG1   . THR A 1 284 ? -19.796 -6.325  -6.854  1.00 19.31  ?  283 THR A OG1   1 
ATOM   2290 C  CG2   . THR A 1 284 ? -18.839 -7.395  -4.912  1.00 23.08  ?  283 THR A CG2   1 
ATOM   2291 N  N     . GLY A 1 285 ? -18.587 -8.569  -9.179  1.00 17.34  ?  284 GLY A N     1 
ATOM   2292 C  CA    . GLY A 1 285 ? -18.891 -8.623  -10.600 1.00 18.60  ?  284 GLY A CA    1 
ATOM   2293 C  C     . GLY A 1 285 ? -19.870 -7.545  -11.033 1.00 17.96  ?  284 GLY A C     1 
ATOM   2294 O  O     . GLY A 1 285 ? -19.727 -6.959  -12.109 1.00 19.58  ?  284 GLY A O     1 
ATOM   2295 N  N     . MET A 1 286 ? -20.884 -7.272  -10.206 1.00 16.30  ?  285 MET A N     1 
ATOM   2296 C  CA    . MET A 1 286 ? -21.839 -6.206  -10.517 1.00 17.63  ?  285 MET A CA    1 
ATOM   2297 C  C     . MET A 1 286 ? -21.174 -4.832  -10.493 1.00 17.51  ?  285 MET A C     1 
ATOM   2298 O  O     . MET A 1 286 ? -21.452 -3.973  -11.349 1.00 16.62  ?  285 MET A O     1 
ATOM   2299 C  CB    . MET A 1 286 ? -23.000 -6.250  -9.522  1.00 17.16  ?  285 MET A CB    1 
ATOM   2300 C  CG    . MET A 1 286 ? -23.949 -7.420  -9.740  1.00 24.37  ?  285 MET A CG    1 
ATOM   2301 S  SD    . MET A 1 286 ? -24.918 -7.166  -11.233 1.00 28.47  ?  285 MET A SD    1 
ATOM   2302 C  CE    . MET A 1 286 ? -25.920 -5.764  -10.725 1.00 34.28  ?  285 MET A CE    1 
ATOM   2303 N  N     . GLN A 1 287 ? -20.302 -4.604  -9.509  1.00 14.46  ?  286 GLN A N     1 
ATOM   2304 C  CA    . GLN A 1 287 ? -19.546 -3.359  -9.464  1.00 17.59  ?  286 GLN A CA    1 
ATOM   2305 C  C     . GLN A 1 287 ? -18.631 -3.234  -10.671 1.00 17.69  ?  286 GLN A C     1 
ATOM   2306 O  O     . GLN A 1 287 ? -18.445 -2.140  -11.206 1.00 16.21  ?  286 GLN A O     1 
ATOM   2307 C  CB    . GLN A 1 287 ? -18.736 -3.286  -8.171  1.00 17.37  ?  286 GLN A CB    1 
ATOM   2308 C  CG    . GLN A 1 287 ? -19.594 -3.109  -6.940  1.00 22.74  ?  286 GLN A CG    1 
ATOM   2309 C  CD    . GLN A 1 287 ? -18.808 -3.284  -5.656  1.00 29.47  ?  286 GLN A CD    1 
ATOM   2310 O  OE1   . GLN A 1 287 ? -17.662 -3.743  -5.670  1.00 25.79  ?  286 GLN A OE1   1 
ATOM   2311 N  NE2   . GLN A 1 287 ? -19.423 -2.917  -4.532  1.00 30.85  ?  286 GLN A NE2   1 
ATOM   2312 N  N     . MET A 1 288 ? -18.048 -4.352  -11.111 1.00 16.73  ?  287 MET A N     1 
ATOM   2313 C  CA    . MET A 1 288 ? -17.232 -4.332  -12.318 1.00 17.16  ?  287 MET A CA    1 
ATOM   2314 C  C     . MET A 1 288 ? -18.062 -3.988  -13.548 1.00 15.80  ?  287 MET A C     1 
ATOM   2315 O  O     . MET A 1 288 ? -17.612 -3.240  -14.423 1.00 16.38  ?  287 MET A O     1 
ATOM   2316 C  CB    . MET A 1 288 ? -16.554 -5.686  -12.489 1.00 17.97  ?  287 MET A CB    1 
ATOM   2317 C  CG    . MET A 1 288 ? -15.238 -5.786  -11.773 1.00 19.64  ?  287 MET A CG    1 
ATOM   2318 S  SD    . MET A 1 288 ? -13.985 -4.849  -12.656 1.00 20.19  ?  287 MET A SD    1 
ATOM   2319 C  CE    . MET A 1 288 ? -12.732 -4.730  -11.390 1.00 22.55  ?  287 MET A CE    1 
ATOM   2320 N  N     . GLU A 1 289 ? -19.258 -4.563  -13.653 1.00 15.62  ?  288 GLU A N     1 
ATOM   2321 C  CA    . GLU A 1 289 ? -20.141 -4.243  -14.767 1.00 15.00  ?  288 GLU A CA    1 
ATOM   2322 C  C     . GLU A 1 289 ? -20.457 -2.753  -14.801 1.00 17.61  ?  288 GLU A C     1 
ATOM   2323 O  O     . GLU A 1 289 ? -20.410 -2.119  -15.865 1.00 18.54  ?  288 GLU A O     1 
ATOM   2324 C  CB    . GLU A 1 289 ? -21.421 -5.072  -14.649 1.00 16.48  ?  288 GLU A CB    1 
ATOM   2325 C  CG    . GLU A 1 289 ? -22.348 -4.973  -15.822 1.00 21.29  ?  288 GLU A CG    1 
ATOM   2326 C  CD    . GLU A 1 289 ? -23.605 -5.798  -15.620 1.00 27.61  ?  288 GLU A CD    1 
ATOM   2327 O  OE1   . GLU A 1 289 ? -24.433 -5.440  -14.752 1.00 30.91  ?  288 GLU A OE1   1 
ATOM   2328 O  OE2   . GLU A 1 289 ? -23.749 -6.819  -16.316 1.00 32.71  -1 288 GLU A OE2   1 
ATOM   2329 N  N     . SER A 1 290 ? -20.763 -2.174  -13.638 1.00 16.15  ?  289 SER A N     1 
ATOM   2330 C  CA    . SER A 1 290 ? -21.042 -0.740  -13.582 1.00 18.39  ?  289 SER A CA    1 
ATOM   2331 C  C     . SER A 1 290 ? -19.801 0.082   -13.928 1.00 16.07  ?  289 SER A C     1 
ATOM   2332 O  O     . SER A 1 290 ? -19.884 1.079   -14.661 1.00 16.29  ?  289 SER A O     1 
ATOM   2333 C  CB    . SER A 1 290 ? -21.574 -0.374  -12.196 1.00 19.13  ?  289 SER A CB    1 
ATOM   2334 O  OG    . SER A 1 290 ? -21.943 0.989   -12.144 1.00 27.31  ?  289 SER A OG    1 
ATOM   2335 N  N     . PHE A 1 291 ? -18.646 -0.317  -13.395 1.00 17.11  ?  290 PHE A N     1 
ATOM   2336 C  CA    . PHE A 1 291 ? -17.372 0.303   -13.743 1.00 19.01  ?  290 PHE A CA    1 
ATOM   2337 C  C     . PHE A 1 291 ? -17.165 0.310   -15.259 1.00 17.76  ?  290 PHE A C     1 
ATOM   2338 O  O     . PHE A 1 291 ? -16.840 1.342   -15.853 1.00 16.27  ?  290 PHE A O     1 
ATOM   2339 C  CB    . PHE A 1 291 ? -16.264 -0.471  -13.009 1.00 19.13  ?  290 PHE A CB    1 
ATOM   2340 C  CG    . PHE A 1 291 ? -14.857 -0.025  -13.314 1.00 19.14  ?  290 PHE A CG    1 
ATOM   2341 C  CD1   . PHE A 1 291 ? -14.572 1.263   -13.741 1.00 14.13  ?  290 PHE A CD1   1 
ATOM   2342 C  CD2   . PHE A 1 291 ? -13.804 -0.923  -13.158 1.00 22.11  ?  290 PHE A CD2   1 
ATOM   2343 C  CE1   . PHE A 1 291 ? -13.263 1.644   -14.012 1.00 17.00  ?  290 PHE A CE1   1 
ATOM   2344 C  CE2   . PHE A 1 291 ? -12.495 -0.546  -13.425 1.00 21.07  ?  290 PHE A CE2   1 
ATOM   2345 C  CZ    . PHE A 1 291 ? -12.226 0.737   -13.852 1.00 14.73  ?  290 PHE A CZ    1 
ATOM   2346 N  N     . LYS A 1 292 ? -17.362 -0.840  -15.902 1.00 17.83  ?  291 LYS A N     1 
ATOM   2347 C  CA    . LYS A 1 292 ? -17.164 -0.930  -17.345 1.00 18.17  ?  291 LYS A CA    1 
ATOM   2348 C  C     . LYS A 1 292 ? -18.133 -0.024  -18.092 1.00 16.67  ?  291 LYS A C     1 
ATOM   2349 O  O     . LYS A 1 292 ? -17.744 0.659   -19.049 1.00 15.71  ?  291 LYS A O     1 
ATOM   2350 C  CB    . LYS A 1 292 ? -17.328 -2.377  -17.824 1.00 18.77  ?  291 LYS A CB    1 
ATOM   2351 C  CG    . LYS A 1 292 ? -16.861 -2.587  -19.265 1.00 20.91  ?  291 LYS A CG    1 
ATOM   2352 C  CD    . LYS A 1 292 ? -17.086 -4.011  -19.766 1.00 25.22  ?  291 LYS A CD    1 
ATOM   2353 C  CE    . LYS A 1 292 ? -16.547 -4.179  -21.191 1.00 28.58  ?  291 LYS A CE    1 
ATOM   2354 N  NZ    . LYS A 1 292 ? -16.871 -5.522  -21.772 1.00 31.09  1  291 LYS A NZ    1 
ATOM   2355 N  N     . SER A 1 293 ? -19.404 -0.014  -17.680 1.00 13.26  ?  292 SER A N     1 
ATOM   2356 C  CA    . SER A 1 293 ? -20.387 0.814   -18.373 1.00 14.43  ?  292 SER A CA    1 
ATOM   2357 C  C     . SER A 1 293 ? -20.034 2.293   -18.280 1.00 16.35  ?  292 SER A C     1 
ATOM   2358 O  O     . SER A 1 293 ? -20.153 3.036   -19.265 1.00 17.32  ?  292 SER A O     1 
ATOM   2359 C  CB    . SER A 1 293 ? -21.781 0.563   -17.802 1.00 21.53  ?  292 SER A CB    1 
ATOM   2360 O  OG    . SER A 1 293 ? -22.163 -0.783  -18.016 1.00 32.58  ?  292 SER A OG    1 
ATOM   2361 N  N     . LYS A 1 294 ? -19.602 2.743   -17.103 1.00 13.52  ?  293 LYS A N     1 
ATOM   2362 C  CA    . LYS A 1 294 ? -19.246 4.151   -16.968 1.00 14.59  ?  293 LYS A CA    1 
ATOM   2363 C  C     . LYS A 1 294 ? -17.951 4.471   -17.699 1.00 15.02  ?  293 LYS A C     1 
ATOM   2364 O  O     . LYS A 1 294 ? -17.803 5.575   -18.240 1.00 12.88  ?  293 LYS A O     1 
ATOM   2365 C  CB    . LYS A 1 294 ? -19.168 4.526   -15.491 1.00 17.54  ?  293 LYS A CB    1 
ATOM   2366 C  CG    . LYS A 1 294 ? -20.549 4.721   -14.887 1.00 20.97  ?  293 LYS A CG    1 
ATOM   2367 C  CD    . LYS A 1 294 ? -20.486 5.185   -13.431 1.00 24.51  ?  293 LYS A CD    1 
ATOM   2368 C  CE    . LYS A 1 294 ? -20.476 4.010   -12.473 1.00 22.78  ?  293 LYS A CE    1 
ATOM   2369 N  NZ    . LYS A 1 294 ? -20.708 4.450   -11.057 1.00 20.08  1  293 LYS A NZ    1 
ATOM   2370 N  N     . LEU A 1 295 ? -17.015 3.520   -17.748 1.00 12.83  ?  294 LEU A N     1 
ATOM   2371 C  CA    . LEU A 1 295 ? -15.823 3.699   -18.572 1.00 16.59  ?  294 LEU A CA    1 
ATOM   2372 C  C     . LEU A 1 295 ? -16.187 3.868   -20.041 1.00 16.83  ?  294 LEU A C     1 
ATOM   2373 O  O     . LEU A 1 295 ? -15.609 4.706   -20.741 1.00 15.74  ?  294 LEU A O     1 
ATOM   2374 C  CB    . LEU A 1 295 ? -14.886 2.501   -18.414 1.00 18.29  ?  294 LEU A CB    1 
ATOM   2375 C  CG    . LEU A 1 295 ? -13.636 2.648   -17.554 1.00 27.31  ?  294 LEU A CG    1 
ATOM   2376 C  CD1   . LEU A 1 295 ? -12.785 1.377   -17.666 1.00 26.04  ?  294 LEU A CD1   1 
ATOM   2377 C  CD2   . LEU A 1 295 ? -12.829 3.888   -17.947 1.00 20.15  ?  294 LEU A CD2   1 
ATOM   2378 N  N     . GLN A 1 296 ? -17.124 3.050   -20.530 1.00 16.44  ?  295 GLN A N     1 
ATOM   2379 C  CA    . GLN A 1 296 ? -17.569 3.154   -21.913 1.00 19.75  ?  295 GLN A CA    1 
ATOM   2380 C  C     . GLN A 1 296 ? -18.256 4.490   -22.173 1.00 16.78  ?  295 GLN A C     1 
ATOM   2381 O  O     . GLN A 1 296 ? -18.071 5.098   -23.233 1.00 14.75  ?  295 GLN A O     1 
ATOM   2382 C  CB    . GLN A 1 296 ? -18.514 1.992   -22.244 1.00 16.66  ?  295 GLN A CB    1 
ATOM   2383 C  CG    . GLN A 1 296 ? -18.967 1.963   -23.692 1.00 21.63  ?  295 GLN A CG    1 
ATOM   2384 C  CD    . GLN A 1 296 ? -17.818 1.674   -24.650 1.00 23.31  ?  295 GLN A CD    1 
ATOM   2385 O  OE1   . GLN A 1 296 ? -17.140 0.646   -24.535 1.00 23.62  ?  295 GLN A OE1   1 
ATOM   2386 N  NE2   . GLN A 1 296 ? -17.583 2.591   -25.589 1.00 20.82  ?  295 GLN A NE2   1 
ATOM   2387 N  N     . ALA A 1 297 ? -19.067 4.957   -21.222 1.00 16.43  ?  296 ALA A N     1 
ATOM   2388 C  CA    . ALA A 1 297 ? -19.684 6.273   -21.371 1.00 17.25  ?  296 ALA A CA    1 
ATOM   2389 C  C     . ALA A 1 297 ? -18.629 7.381   -21.408 1.00 15.48  ?  296 ALA A C     1 
ATOM   2390 O  O     . ALA A 1 297 ? -18.742 8.336   -22.194 1.00 15.23  ?  296 ALA A O     1 
ATOM   2391 C  CB    . ALA A 1 297 ? -20.692 6.501   -20.243 1.00 17.56  ?  296 ALA A CB    1 
ATOM   2392 N  N     . LEU A 1 298 ? -17.582 7.259   -20.579 1.00 12.98  ?  297 LEU A N     1 
ATOM   2393 C  CA    . LEU A 1 298 ? -16.483 8.222   -20.623 1.00 12.14  ?  297 LEU A CA    1 
ATOM   2394 C  C     . LEU A 1 298 ? -15.779 8.186   -21.972 1.00 14.11  ?  297 LEU A C     1 
ATOM   2395 O  O     . LEU A 1 298 ? -15.457 9.233   -22.544 1.00 12.00  ?  297 LEU A O     1 
ATOM   2396 C  CB    . LEU A 1 298 ? -15.484 7.942   -19.492 1.00 15.37  ?  297 LEU A CB    1 
ATOM   2397 C  CG    . LEU A 1 298 ? -14.184 8.759   -19.472 1.00 15.43  ?  297 LEU A CG    1 
ATOM   2398 C  CD1   . LEU A 1 298 ? -14.464 10.270  -19.443 1.00 14.01  ?  297 LEU A CD1   1 
ATOM   2399 C  CD2   . LEU A 1 298 ? -13.282 8.344   -18.290 1.00 10.88  ?  297 LEU A CD2   1 
ATOM   2400 N  N     . LEU A 1 299 ? -15.514 6.984   -22.485 1.00 14.23  ?  298 LEU A N     1 
ATOM   2401 C  CA    . LEU A 1 299 ? -14.870 6.857   -23.792 1.00 15.97  ?  298 LEU A CA    1 
ATOM   2402 C  C     . LEU A 1 299 ? -15.714 7.500   -24.886 1.00 17.81  ?  298 LEU A C     1 
ATOM   2403 O  O     . LEU A 1 299 ? -15.190 8.202   -25.763 1.00 16.34  ?  298 LEU A O     1 
ATOM   2404 C  CB    . LEU A 1 299 ? -14.636 5.382   -24.112 1.00 18.56  ?  298 LEU A CB    1 
ATOM   2405 C  CG    . LEU A 1 299 ? -14.053 5.178   -25.509 1.00 23.63  ?  298 LEU A CG    1 
ATOM   2406 C  CD1   . LEU A 1 299 ? -12.644 5.734   -25.541 1.00 20.37  ?  298 LEU A CD1   1 
ATOM   2407 C  CD2   . LEU A 1 299 ? -14.078 3.721   -25.856 1.00 33.35  ?  298 LEU A CD2   1 
ATOM   2408 N  N     . ASN A 1 300 ? -17.030 7.264   -24.847 1.00 17.62  ?  299 ASN A N     1 
ATOM   2409 C  CA    . ASN A 1 300 ? -17.927 7.867   -25.826 1.00 17.07  ?  299 ASN A CA    1 
ATOM   2410 C  C     . ASN A 1 300 ? -17.881 9.387   -25.744 1.00 17.58  ?  299 ASN A C     1 
ATOM   2411 O  O     . ASN A 1 300 ? -17.912 10.073  -26.773 1.00 18.98  ?  299 ASN A O     1 
ATOM   2412 C  CB    . ASN A 1 300 ? -19.355 7.352   -25.621 1.00 18.01  ?  299 ASN A CB    1 
ATOM   2413 C  CG    . ASN A 1 300 ? -19.483 5.851   -25.885 1.00 23.54  ?  299 ASN A CG    1 
ATOM   2414 O  OD1   . ASN A 1 300 ? -18.588 5.225   -26.457 1.00 25.68  ?  299 ASN A OD1   1 
ATOM   2415 N  ND2   . ASN A 1 300 ? -20.602 5.273   -25.470 1.00 26.58  ?  299 ASN A ND2   1 
ATOM   2416 N  N     . ALA A 1 301 ? -17.787 9.935   -24.529 1.00 17.75  ?  300 ALA A N     1 
ATOM   2417 C  CA    . ALA A 1 301 ? -17.696 11.388  -24.394 1.00 17.09  ?  300 ALA A CA    1 
ATOM   2418 C  C     . ALA A 1 301 ? -16.360 11.919  -24.912 1.00 19.80  ?  300 ALA A C     1 
ATOM   2419 O  O     . ALA A 1 301 ? -16.309 12.986  -25.536 1.00 18.02  ?  300 ALA A O     1 
ATOM   2420 C  CB    . ALA A 1 301 ? -17.895 11.798  -22.937 1.00 19.42  ?  300 ALA A CB    1 
ATOM   2421 N  N     . LEU A 1 302 ? -15.264 11.212  -24.632 1.00 14.67  ?  301 LEU A N     1 
ATOM   2422 C  CA    . LEU A 1 302 ? -13.965 11.610  -25.173 1.00 12.67  ?  301 LEU A CA    1 
ATOM   2423 C  C     . LEU A 1 302 ? -13.991 11.648  -26.700 1.00 16.97  ?  301 LEU A C     1 
ATOM   2424 O  O     . LEU A 1 302 ? -13.444 12.571  -27.321 1.00 17.84  ?  301 LEU A O     1 
ATOM   2425 C  CB    . LEU A 1 302 ? -12.876 10.658  -24.674 1.00 11.01  ?  301 LEU A CB    1 
ATOM   2426 C  CG    . LEU A 1 302 ? -12.520 10.810  -23.190 1.00 16.68  ?  301 LEU A CG    1 
ATOM   2427 C  CD1   . LEU A 1 302 ? -11.779 9.580   -22.664 1.00 14.75  ?  301 LEU A CD1   1 
ATOM   2428 C  CD2   . LEU A 1 302 ? -11.702 12.083  -22.961 1.00 15.48  ?  301 LEU A CD2   1 
ATOM   2429 N  N     . LYS A 1 303 ? -14.634 10.658  -27.321 1.00 17.13  ?  302 LYS A N     1 
ATOM   2430 C  CA    . LYS A 1 303 ? -14.750 10.650  -28.779 1.00 20.86  ?  302 LYS A CA    1 
ATOM   2431 C  C     . LYS A 1 303 ? -15.651 11.772  -29.276 1.00 21.79  ?  302 LYS A C     1 
ATOM   2432 O  O     . LYS A 1 303 ? -15.344 12.419  -30.284 1.00 23.95  ?  302 LYS A O     1 
ATOM   2433 C  CB    . LYS A 1 303 ? -15.286 9.305   -29.265 1.00 22.45  ?  302 LYS A CB    1 
ATOM   2434 C  CG    . LYS A 1 303 ? -14.287 8.170   -29.246 1.00 23.65  ?  302 LYS A CG    1 
ATOM   2435 C  CD    . LYS A 1 303 ? -14.958 6.907   -29.774 1.00 29.40  ?  302 LYS A CD    1 
ATOM   2436 C  CE    . LYS A 1 303 ? -14.014 5.727   -29.797 1.00 34.90  ?  302 LYS A CE    1 
ATOM   2437 N  NZ    . LYS A 1 303 ? -12.791 6.018   -30.584 1.00 41.03  1  302 LYS A NZ    1 
ATOM   2438 N  N     . THR A 1 304 ? -16.777 12.002  -28.596 1.00 19.51  ?  303 THR A N     1 
ATOM   2439 C  CA    . THR A 1 304 ? -17.673 13.092  -28.975 1.00 22.17  ?  303 THR A CA    1 
ATOM   2440 C  C     . THR A 1 304 ? -16.966 14.439  -28.899 1.00 24.50  ?  303 THR A C     1 
ATOM   2441 O  O     . THR A 1 304 ? -17.157 15.302  -29.766 1.00 24.08  ?  303 THR A O     1 
ATOM   2442 C  CB    . THR A 1 304 ? -18.905 13.085  -28.064 1.00 22.17  ?  303 THR A CB    1 
ATOM   2443 O  OG1   . THR A 1 304 ? -19.591 11.839  -28.210 1.00 25.38  ?  303 THR A OG1   1 
ATOM   2444 C  CG2   . THR A 1 304 ? -19.842 14.226  -28.400 1.00 23.41  ?  303 THR A CG2   1 
ATOM   2445 N  N     . ALA A 1 305 ? -16.139 14.632  -27.867 1.00 22.74  ?  304 ALA A N     1 
ATOM   2446 C  CA    . ALA A 1 305 ? -15.400 15.874  -27.692 1.00 20.21  ?  304 ALA A CA    1 
ATOM   2447 C  C     . ALA A 1 305 ? -14.388 16.109  -28.800 1.00 27.81  ?  304 ALA A C     1 
ATOM   2448 O  O     . ALA A 1 305 ? -13.912 17.239  -28.957 1.00 32.03  ?  304 ALA A O     1 
ATOM   2449 C  CB    . ALA A 1 305 ? -14.675 15.879  -26.349 1.00 18.86  ?  304 ALA A CB    1 
ATOM   2450 N  N     . LYS A 1 306 ? -14.024 15.070  -29.546 1.00 22.05  ?  305 LYS A N     1 
ATOM   2451 C  CA    . LYS A 1 306 ? -13.130 15.257  -30.677 1.00 24.82  ?  305 LYS A CA    1 
ATOM   2452 C  C     . LYS A 1 306 ? -13.859 15.839  -31.880 1.00 27.48  ?  305 LYS A C     1 
ATOM   2453 O  O     . LYS A 1 306 ? -13.239 16.509  -32.711 1.00 33.62  ?  305 LYS A O     1 
ATOM   2454 C  CB    . LYS A 1 306 ? -12.472 13.926  -31.051 1.00 27.47  ?  305 LYS A CB    1 
ATOM   2455 C  CG    . LYS A 1 306 ? -11.343 14.045  -32.061 1.00 33.09  ?  305 LYS A CG    1 
ATOM   2456 C  CD    . LYS A 1 306 ? -10.779 12.682  -32.425 1.00 36.09  ?  305 LYS A CD    1 
ATOM   2457 C  CE    . LYS A 1 306 ? -9.589  12.822  -33.366 1.00 38.91  ?  305 LYS A CE    1 
ATOM   2458 N  NZ    . LYS A 1 306 ? -8.972  11.506  -33.705 1.00 40.22  1  305 LYS A NZ    1 
ATOM   2459 N  N     . SER A 1 307 ? -15.165 15.610  -31.988 1.00 33.53  ?  306 SER A N     1 
ATOM   2460 C  CA    . SER A 1 307 ? -15.901 15.942  -33.198 1.00 38.63  ?  306 SER A CA    1 
ATOM   2461 C  C     . SER A 1 307 ? -16.811 17.154  -33.061 1.00 40.34  ?  306 SER A C     1 
ATOM   2462 O  O     . SER A 1 307 ? -17.404 17.570  -34.062 1.00 43.20  ?  306 SER A O     1 
ATOM   2463 C  CB    . SER A 1 307 ? -16.739 14.737  -33.651 1.00 40.08  ?  306 SER A CB    1 
ATOM   2464 O  OG    . SER A 1 307 ? -17.789 14.473  -32.735 1.00 43.81  ?  306 SER A OG    1 
ATOM   2465 N  N     . ARG A 1 308 ? -16.936 17.737  -31.871 1.00 38.88  ?  307 ARG A N     1 
ATOM   2466 C  CA    . ARG A 1 308 ? -17.871 18.840  -31.687 1.00 39.63  ?  307 ARG A CA    1 
ATOM   2467 C  C     . ARG A 1 308 ? -17.377 20.092  -32.395 1.00 42.79  ?  307 ARG A C     1 
ATOM   2468 O  O     . ARG A 1 308 ? -16.215 20.489  -32.253 1.00 41.77  ?  307 ARG A O     1 
ATOM   2469 C  CB    . ARG A 1 308 ? -18.089 19.128  -30.203 1.00 37.30  ?  307 ARG A CB    1 
ATOM   2470 C  CG    . ARG A 1 308 ? -18.814 18.027  -29.441 1.00 40.38  ?  307 ARG A CG    1 
ATOM   2471 C  CD    . ARG A 1 308 ? -20.130 17.638  -30.096 1.00 44.92  ?  307 ARG A CD    1 
ATOM   2472 N  NE    . ARG A 1 308 ? -19.946 16.618  -31.124 1.00 47.17  ?  307 ARG A NE    1 
ATOM   2473 C  CZ    . ARG A 1 308 ? -20.865 16.289  -32.024 1.00 48.24  ?  307 ARG A CZ    1 
ATOM   2474 N  NH1   . ARG A 1 308 ? -22.042 16.901  -32.028 1.00 51.36  1  307 ARG A NH1   1 
ATOM   2475 N  NH2   . ARG A 1 308 ? -20.603 15.352  -32.922 1.00 46.37  ?  307 ARG A NH2   1 
ATOM   2476 N  N     . LEU A 1 309 ? -18.275 20.712  -33.162 1.00 46.12  ?  308 LEU A N     1 
ATOM   2477 C  CA    . LEU A 1 309 ? -17.937 21.955  -33.844 1.00 48.50  ?  308 LEU A CA    1 
ATOM   2478 C  C     . LEU A 1 309 ? -17.753 23.092  -32.850 1.00 45.52  ?  308 LEU A C     1 
ATOM   2479 O  O     . LEU A 1 309 ? -16.855 23.926  -33.010 1.00 49.17  ?  308 LEU A O     1 
ATOM   2480 C  CB    . LEU A 1 309 ? -19.024 22.299  -34.858 1.00 54.17  ?  308 LEU A CB    1 
ATOM   2481 C  CG    . LEU A 1 309 ? -18.693 23.422  -35.835 1.00 59.14  ?  308 LEU A CG    1 
ATOM   2482 C  CD1   . LEU A 1 309 ? -17.643 22.965  -36.842 1.00 61.02  ?  308 LEU A CD1   1 
ATOM   2483 C  CD2   . LEU A 1 309 ? -19.955 23.896  -36.529 1.00 59.17  ?  308 LEU A CD2   1 
ATOM   2484 N  N     . GLU A 1 310 ? -18.588 23.137  -31.816 1.00 36.67  ?  309 GLU A N     1 
ATOM   2485 C  CA    . GLU A 1 310 ? -18.499 24.160  -30.786 1.00 30.66  ?  309 GLU A CA    1 
ATOM   2486 C  C     . GLU A 1 310 ? -17.669 23.643  -29.617 1.00 27.28  ?  309 GLU A C     1 
ATOM   2487 O  O     . GLU A 1 310 ? -17.949 22.564  -29.078 1.00 23.76  ?  309 GLU A O     1 
ATOM   2488 C  CB    . GLU A 1 310 ? -19.896 24.558  -30.305 1.00 33.67  ?  309 GLU A CB    1 
ATOM   2489 C  CG    . GLU A 1 310 ? -20.760 25.234  -31.360 1.00 40.48  ?  309 GLU A CG    1 
ATOM   2490 C  CD    . GLU A 1 310 ? -20.455 26.713  -31.508 1.00 41.06  ?  309 GLU A CD    1 
ATOM   2491 O  OE1   . GLU A 1 310 ? -19.593 27.223  -30.760 1.00 41.32  ?  309 GLU A OE1   1 
ATOM   2492 O  OE2   . GLU A 1 310 ? -21.082 27.366  -32.368 1.00 39.46  -1 309 GLU A OE2   1 
ATOM   2493 N  N     . LEU A 1 311 ? -16.646 24.418  -29.233 1.00 22.61  ?  310 LEU A N     1 
ATOM   2494 C  CA    . LEU A 1 311 ? -15.862 24.093  -28.046 1.00 23.57  ?  310 LEU A CA    1 
ATOM   2495 C  C     . LEU A 1 311 ? -16.763 23.925  -26.830 1.00 20.94  ?  310 LEU A C     1 
ATOM   2496 O  O     . LEU A 1 311 ? -16.517 23.064  -25.979 1.00 19.49  ?  310 LEU A O     1 
ATOM   2497 C  CB    . LEU A 1 311 ? -14.818 25.185  -27.791 1.00 27.19  ?  310 LEU A CB    1 
ATOM   2498 C  CG    . LEU A 1 311 ? -13.816 24.963  -26.652 1.00 28.92  ?  310 LEU A CG    1 
ATOM   2499 C  CD1   . LEU A 1 311 ? -12.818 23.880  -27.005 1.00 27.60  ?  310 LEU A CD1   1 
ATOM   2500 C  CD2   . LEU A 1 311 ? -13.092 26.257  -26.307 1.00 33.37  ?  310 LEU A CD2   1 
ATOM   2501 N  N     . HIS A 1 312 ? -17.826 24.734  -26.742 1.00 22.63  ?  311 HIS A N     1 
ATOM   2502 C  CA    . HIS A 1 312 ? -18.780 24.596  -25.644 1.00 20.76  ?  311 HIS A CA    1 
ATOM   2503 C  C     . HIS A 1 312 ? -19.321 23.173  -25.551 1.00 22.09  ?  311 HIS A C     1 
ATOM   2504 O  O     . HIS A 1 312 ? -19.389 22.597  -24.460 1.00 23.63  ?  311 HIS A O     1 
ATOM   2505 C  CB    . HIS A 1 312 ? -19.940 25.575  -25.816 1.00 22.61  ?  311 HIS A CB    1 
ATOM   2506 C  CG    . HIS A 1 312 ? -21.089 25.303  -24.893 1.00 26.84  ?  311 HIS A CG    1 
ATOM   2507 N  ND1   . HIS A 1 312 ? -21.169 25.838  -23.625 1.00 29.38  ?  311 HIS A ND1   1 
ATOM   2508 C  CD2   . HIS A 1 312 ? -22.193 24.532  -25.044 1.00 29.32  ?  311 HIS A CD2   1 
ATOM   2509 C  CE1   . HIS A 1 312 ? -22.281 25.425  -23.042 1.00 26.62  ?  311 HIS A CE1   1 
ATOM   2510 N  NE2   . HIS A 1 312 ? -22.918 24.629  -23.880 1.00 27.98  ?  311 HIS A NE2   1 
ATOM   2511 N  N     . ASP A 1 313 ? -19.730 22.600  -26.686 1.00 19.36  ?  312 ASP A N     1 
ATOM   2512 C  CA    . ASP A 1 313 ? -20.352 21.277  -26.670 1.00 22.11  ?  312 ASP A CA    1 
ATOM   2513 C  C     . ASP A 1 313 ? -19.341 20.184  -26.332 1.00 23.58  ?  312 ASP A C     1 
ATOM   2514 O  O     . ASP A 1 313 ? -19.656 19.254  -25.578 1.00 24.08  ?  312 ASP A O     1 
ATOM   2515 C  CB    . ASP A 1 313 ? -21.019 20.983  -28.016 1.00 23.60  ?  312 ASP A CB    1 
ATOM   2516 C  CG    . ASP A 1 313 ? -22.081 22.007  -28.393 1.00 30.13  ?  312 ASP A CG    1 
ATOM   2517 O  OD1   . ASP A 1 313 ? -22.642 22.668  -27.491 1.00 31.77  ?  312 ASP A OD1   1 
ATOM   2518 O  OD2   . ASP A 1 313 ? -22.357 22.144  -29.606 1.00 29.72  -1 312 ASP A OD2   1 
ATOM   2519 N  N     . ALA A 1 314 ? -18.125 20.267  -26.883 1.00 24.19  ?  313 ALA A N     1 
ATOM   2520 C  CA    . ALA A 1 314 ? -17.097 19.292  -26.523 1.00 24.00  ?  313 ALA A CA    1 
ATOM   2521 C  C     . ALA A 1 314 ? -16.797 19.340  -25.028 1.00 20.22  ?  313 ALA A C     1 
ATOM   2522 O  O     . ALA A 1 314 ? -16.705 18.296  -24.356 1.00 18.04  ?  313 ALA A O     1 
ATOM   2523 C  CB    . ALA A 1 314 ? -15.829 19.548  -27.337 1.00 24.99  ?  313 ALA A CB    1 
ATOM   2524 N  N     . CYS A 1 315 ? -16.691 20.553  -24.478 1.00 19.21  ?  314 CYS A N     1 
ATOM   2525 C  CA    . CYS A 1 315 ? -16.353 20.687  -23.067 1.00 18.93  ?  314 CYS A CA    1 
ATOM   2526 C  C     . CYS A 1 315 ? -17.498 20.237  -22.172 1.00 18.12  ?  314 CYS A C     1 
ATOM   2527 O  O     . CYS A 1 315 ? -17.261 19.630  -21.122 1.00 16.81  ?  314 CYS A O     1 
ATOM   2528 C  CB    . CYS A 1 315 ? -15.957 22.128  -22.757 1.00 19.16  ?  314 CYS A CB    1 
ATOM   2529 S  SG    . CYS A 1 315 ? -14.330 22.558  -23.434 1.00 18.28  ?  314 CYS A SG    1 
ATOM   2530 N  N     . LYS A 1 316 ? -18.739 20.553  -22.549 1.00 17.23  ?  315 LYS A N     1 
ATOM   2531 C  CA    . LYS A 1 316 ? -19.893 20.085  -21.786 1.00 19.27  ?  315 LYS A CA    1 
ATOM   2532 C  C     . LYS A 1 316 ? -19.956 18.564  -21.779 1.00 18.09  ?  315 LYS A C     1 
ATOM   2533 O  O     . LYS A 1 316 ? -20.199 17.947  -20.729 1.00 18.11  ?  315 LYS A O     1 
ATOM   2534 C  CB    . LYS A 1 316 ? -21.181 20.678  -22.371 1.00 21.88  ?  315 LYS A CB    1 
ATOM   2535 C  CG    . LYS A 1 316 ? -22.472 20.271  -21.652 1.00 26.57  ?  315 LYS A CG    1 
ATOM   2536 C  CD    . LYS A 1 316 ? -22.434 20.688  -20.182 1.00 36.22  ?  315 LYS A CD    1 
ATOM   2537 C  CE    . LYS A 1 316 ? -23.822 20.684  -19.532 1.00 39.63  ?  315 LYS A CE    1 
ATOM   2538 N  NZ    . LYS A 1 316 ? -24.323 19.315  -19.198 1.00 38.22  1  315 LYS A NZ    1 
ATOM   2539 N  N     . ALA A 1 317 ? -19.747 17.942  -22.947 1.00 19.41  ?  316 ALA A N     1 
ATOM   2540 C  CA    . ALA A 1 317 ? -19.717 16.485  -23.009 1.00 18.74  ?  316 ALA A CA    1 
ATOM   2541 C  C     . ALA A 1 317 ? -18.713 15.926  -22.016 1.00 17.90  ?  316 ALA A C     1 
ATOM   2542 O  O     . ALA A 1 317 ? -18.979 14.920  -21.348 1.00 17.50  ?  316 ALA A O     1 
ATOM   2543 C  CB    . ALA A 1 317 ? -19.374 16.021  -24.427 1.00 19.99  ?  316 ALA A CB    1 
ATOM   2544 N  N     . LEU A 1 318 ? -17.551 16.577  -21.897 1.00 15.83  ?  317 LEU A N     1 
ATOM   2545 C  CA    . LEU A 1 318 ? -16.560 16.095  -20.932 1.00 16.56  ?  317 LEU A CA    1 
ATOM   2546 C  C     . LEU A 1 318 ? -16.977 16.376  -19.484 1.00 13.86  ?  317 LEU A C     1 
ATOM   2547 O  O     . LEU A 1 318 ? -16.790 15.531  -18.595 1.00 13.16  ?  317 LEU A O     1 
ATOM   2548 C  CB    . LEU A 1 318 ? -15.207 16.725  -21.242 1.00 15.65  ?  317 LEU A CB    1 
ATOM   2549 C  CG    . LEU A 1 318 ? -14.679 16.244  -22.588 1.00 19.79  ?  317 LEU A CG    1 
ATOM   2550 C  CD1   . LEU A 1 318 ? -13.396 16.986  -22.968 1.00 23.03  ?  317 LEU A CD1   1 
ATOM   2551 C  CD2   . LEU A 1 318 ? -14.457 14.748  -22.544 1.00 20.00  ?  317 LEU A CD2   1 
ATOM   2552 N  N     . ALA A 1 319 ? -17.512 17.569  -19.222 1.00 15.56  ?  318 ALA A N     1 
ATOM   2553 C  CA    . ALA A 1 319 ? -17.912 17.934  -17.866 1.00 18.95  ?  318 ALA A CA    1 
ATOM   2554 C  C     . ALA A 1 319 ? -18.953 16.972  -17.320 1.00 16.95  ?  318 ALA A C     1 
ATOM   2555 O  O     . ALA A 1 319 ? -18.984 16.711  -16.111 1.00 16.24  ?  318 ALA A O     1 
ATOM   2556 C  CB    . ALA A 1 319 ? -18.454 19.367  -17.835 1.00 18.12  ?  318 ALA A CB    1 
ATOM   2557 N  N     . ASP A 1 320 ? -19.803 16.432  -18.196 1.00 16.25  ?  319 ASP A N     1 
ATOM   2558 C  CA    . ASP A 1 320 ? -20.782 15.440  -17.762 1.00 20.21  ?  319 ASP A CA    1 
ATOM   2559 C  C     . ASP A 1 320 ? -20.136 14.241  -17.078 1.00 17.91  ?  319 ASP A C     1 
ATOM   2560 O  O     . ASP A 1 320 ? -20.810 13.542  -16.313 1.00 16.16  ?  319 ASP A O     1 
ATOM   2561 C  CB    . ASP A 1 320 ? -21.615 14.961  -18.950 1.00 19.54  ?  319 ASP A CB    1 
ATOM   2562 C  CG    . ASP A 1 320 ? -22.529 16.030  -19.484 1.00 18.39  ?  319 ASP A CG    1 
ATOM   2563 O  OD1   . ASP A 1 320 ? -22.829 16.982  -18.737 1.00 21.37  ?  319 ASP A OD1   1 
ATOM   2564 O  OD2   . ASP A 1 320 ? -22.956 15.912  -20.651 1.00 20.60  -1 319 ASP A OD2   1 
ATOM   2565 N  N     . HIS A 1 321 ? -18.848 13.981  -17.333 1.00 10.85  ?  320 HIS A N     1 
ATOM   2566 C  CA    . HIS A 1 321 ? -18.156 12.872  -16.693 1.00 11.25  ?  320 HIS A CA    1 
ATOM   2567 C  C     . HIS A 1 321 ? -17.092 13.301  -15.699 1.00 15.33  ?  320 HIS A C     1 
ATOM   2568 O  O     . HIS A 1 321 ? -16.762 12.515  -14.806 1.00 15.91  ?  320 HIS A O     1 
ATOM   2569 C  CB    . HIS A 1 321 ? -17.528 11.956  -17.759 1.00 14.52  ?  320 HIS A CB    1 
ATOM   2570 C  CG    . HIS A 1 321 ? -18.538 11.416  -18.722 1.00 15.07  ?  320 HIS A CG    1 
ATOM   2571 N  ND1   . HIS A 1 321 ? -19.156 10.195  -18.551 1.00 16.01  ?  320 HIS A ND1   1 
ATOM   2572 C  CD2   . HIS A 1 321 ? -19.087 11.966  -19.831 1.00 16.98  ?  320 HIS A CD2   1 
ATOM   2573 C  CE1   . HIS A 1 321 ? -20.027 10.007  -19.528 1.00 17.93  ?  320 HIS A CE1   1 
ATOM   2574 N  NE2   . HIS A 1 321 ? -20.007 11.069  -20.316 1.00 15.69  ?  320 HIS A NE2   1 
ATOM   2575 N  N     . PHE A 1 322 ? -16.567 14.525  -15.812 1.00 16.73  ?  321 PHE A N     1 
ATOM   2576 C  CA    . PHE A 1 322 ? -15.524 14.993  -14.907 1.00 15.37  ?  321 PHE A CA    1 
ATOM   2577 C  C     . PHE A 1 322 ? -16.021 15.930  -13.813 1.00 17.28  ?  321 PHE A C     1 
ATOM   2578 O  O     . PHE A 1 322 ? -15.279 16.177  -12.853 1.00 16.30  ?  321 PHE A O     1 
ATOM   2579 C  CB    . PHE A 1 322 ? -14.410 15.687  -15.701 1.00 17.75  ?  321 PHE A CB    1 
ATOM   2580 C  CG    . PHE A 1 322 ? -13.570 14.736  -16.505 1.00 18.06  ?  321 PHE A CG    1 
ATOM   2581 C  CD1   . PHE A 1 322 ? -12.841 13.731  -15.871 1.00 18.60  ?  321 PHE A CD1   1 
ATOM   2582 C  CD2   . PHE A 1 322 ? -13.515 14.830  -17.883 1.00 18.75  ?  321 PHE A CD2   1 
ATOM   2583 C  CE1   . PHE A 1 322 ? -12.070 12.844  -16.606 1.00 18.23  ?  321 PHE A CE1   1 
ATOM   2584 C  CE2   . PHE A 1 322 ? -12.746 13.952  -18.625 1.00 21.66  ?  321 PHE A CE2   1 
ATOM   2585 C  CZ    . PHE A 1 322 ? -12.024 12.954  -17.990 1.00 20.94  ?  321 PHE A CZ    1 
ATOM   2586 N  N     . GLY A 1 323 ? -17.237 16.450  -13.918 1.00 16.35  ?  322 GLY A N     1 
ATOM   2587 C  CA    . GLY A 1 323 ? -17.802 17.248  -12.845 1.00 15.51  ?  322 GLY A CA    1 
ATOM   2588 C  C     . GLY A 1 323 ? -17.569 18.735  -13.027 1.00 18.26  ?  322 GLY A C     1 
ATOM   2589 O  O     . GLY A 1 323 ? -17.166 19.220  -14.090 1.00 16.05  ?  322 GLY A O     1 
ATOM   2590 N  N     . SER A 1 324 ? -17.794 19.463  -11.927 1.00 15.92  ?  323 SER A N     1 
ATOM   2591 C  CA    . SER A 1 324 ? -17.981 20.910  -11.990 1.00 21.10  ?  323 SER A CA    1 
ATOM   2592 C  C     . SER A 1 324 ? -16.688 21.680  -12.225 1.00 21.61  ?  323 SER A C     1 
ATOM   2593 O  O     . SER A 1 324 ? -16.752 22.841  -12.639 1.00 20.50  ?  323 SER A O     1 
ATOM   2594 C  CB    . SER A 1 324 ? -18.651 21.402  -10.705 1.00 26.29  ?  323 SER A CB    1 
ATOM   2595 O  OG    . SER A 1 324 ? -17.787 21.256  -9.589  1.00 28.07  ?  323 SER A OG    1 
ATOM   2596 N  N     . GLU A 1 325 ? -15.522 21.072  -11.985 1.00 19.61  ?  324 GLU A N     1 
ATOM   2597 C  CA    . GLU A 1 325 ? -14.261 21.764  -12.231 1.00 20.39  ?  324 GLU A CA    1 
ATOM   2598 C  C     . GLU A 1 325 ? -13.823 21.725  -13.688 1.00 19.55  ?  324 GLU A C     1 
ATOM   2599 O  O     . GLU A 1 325 ? -12.840 22.394  -14.036 1.00 19.71  ?  324 GLU A O     1 
ATOM   2600 C  CB    . GLU A 1 325 ? -13.141 21.182  -11.365 1.00 20.62  ?  324 GLU A CB    1 
ATOM   2601 C  CG    . GLU A 1 325 ? -13.397 21.278  -9.866  1.00 29.39  ?  324 GLU A CG    1 
ATOM   2602 C  CD    . GLU A 1 325 ? -13.229 22.680  -9.309  1.00 34.64  ?  324 GLU A CD    1 
ATOM   2603 O  OE1   . GLU A 1 325 ? -12.703 23.561  -10.028 1.00 36.49  ?  324 GLU A OE1   1 
ATOM   2604 O  OE2   . GLU A 1 325 ? -13.627 22.902  -8.145  1.00 35.36  -1 324 GLU A OE2   1 
ATOM   2605 N  N     . PHE A 1 326 ? -14.501 20.969  -14.551 1.00 16.84  ?  325 PHE A N     1 
ATOM   2606 C  CA    . PHE A 1 326 ? -14.112 20.968  -15.954 1.00 19.22  ?  325 PHE A CA    1 
ATOM   2607 C  C     . PHE A 1 326 ? -14.661 22.214  -16.636 1.00 20.16  ?  325 PHE A C     1 
ATOM   2608 O  O     . PHE A 1 326 ? -15.882 22.397  -16.675 1.00 17.72  ?  325 PHE A O     1 
ATOM   2609 C  CB    . PHE A 1 326 ? -14.594 19.723  -16.690 1.00 19.02  ?  325 PHE A CB    1 
ATOM   2610 C  CG    . PHE A 1 326 ? -13.819 19.461  -17.952 1.00 17.95  ?  325 PHE A CG    1 
ATOM   2611 C  CD1   . PHE A 1 326 ? -14.151 20.106  -19.134 1.00 15.99  ?  325 PHE A CD1   1 
ATOM   2612 C  CD2   . PHE A 1 326 ? -12.723 18.616  -17.940 1.00 18.32  ?  325 PHE A CD2   1 
ATOM   2613 C  CE1   . PHE A 1 326 ? -13.416 19.893  -20.292 1.00 19.81  ?  325 PHE A CE1   1 
ATOM   2614 C  CE2   . PHE A 1 326 ? -11.983 18.387  -19.099 1.00 17.10  ?  325 PHE A CE2   1 
ATOM   2615 C  CZ    . PHE A 1 326 ? -12.323 19.024  -20.270 1.00 15.89  ?  325 PHE A CZ    1 
ATOM   2616 N  N     . PRO A 1 327 ? -13.810 23.076  -17.195 1.00 19.76  ?  326 PRO A N     1 
ATOM   2617 C  CA    . PRO A 1 327 ? -14.301 24.341  -17.757 1.00 18.61  ?  326 PRO A CA    1 
ATOM   2618 C  C     . PRO A 1 327 ? -15.189 24.110  -18.965 1.00 16.65  ?  326 PRO A C     1 
ATOM   2619 O  O     . PRO A 1 327 ? -14.907 23.269  -19.823 1.00 13.78  ?  326 PRO A O     1 
ATOM   2620 C  CB    . PRO A 1 327 ? -13.015 25.084  -18.148 1.00 18.14  ?  326 PRO A CB    1 
ATOM   2621 C  CG    . PRO A 1 327 ? -11.906 24.391  -17.369 1.00 19.58  ?  326 PRO A CG    1 
ATOM   2622 C  CD    . PRO A 1 327 ? -12.349 22.952  -17.312 1.00 17.81  ?  326 PRO A CD    1 
ATOM   2623 N  N     . VAL A 1 328 ? -16.279 24.861  -19.024 1.00 15.81  ?  327 VAL A N     1 
ATOM   2624 C  CA    . VAL A 1 328 ? -17.192 24.828  -20.155 1.00 16.72  ?  327 VAL A CA    1 
ATOM   2625 C  C     . VAL A 1 328 ? -17.305 26.237  -20.720 1.00 21.39  ?  327 VAL A C     1 
ATOM   2626 O  O     . VAL A 1 328 ? -18.092 27.053  -20.241 1.00 20.79  ?  327 VAL A O     1 
ATOM   2627 C  CB    . VAL A 1 328 ? -18.575 24.276  -19.760 1.00 20.76  ?  327 VAL A CB    1 
ATOM   2628 C  CG1   . VAL A 1 328 ? -19.474 24.176  -20.991 1.00 20.95  ?  327 VAL A CG1   1 
ATOM   2629 C  CG2   . VAL A 1 328 ? -18.431 22.901  -19.089 1.00 19.70  ?  327 VAL A CG2   1 
ATOM   2630 N  N     . PRO A 1 329 ? -16.507 26.567  -21.734 1.00 22.78  ?  328 PRO A N     1 
ATOM   2631 C  CA    . PRO A 1 329 ? -16.614 27.897  -22.346 1.00 24.37  ?  328 PRO A CA    1 
ATOM   2632 C  C     . PRO A 1 329 ? -18.012 28.140  -22.899 1.00 26.35  ?  328 PRO A C     1 
ATOM   2633 O  O     . PRO A 1 329 ? -18.671 27.225  -23.401 1.00 25.71  ?  328 PRO A O     1 
ATOM   2634 C  CB    . PRO A 1 329 ? -15.564 27.855  -23.463 1.00 24.46  ?  328 PRO A CB    1 
ATOM   2635 C  CG    . PRO A 1 329 ? -14.571 26.827  -22.997 1.00 23.84  ?  328 PRO A CG    1 
ATOM   2636 C  CD    . PRO A 1 329 ? -15.408 25.778  -22.314 1.00 24.33  ?  328 PRO A CD    1 
ATOM   2637 N  N     . GLU A 1 330 ? -18.467 29.387  -22.782 1.00 29.74  ?  329 GLU A N     1 
ATOM   2638 C  CA    . GLU A 1 330 ? -19.783 29.760  -23.277 1.00 36.20  ?  329 GLU A CA    1 
ATOM   2639 C  C     . GLU A 1 330 ? -19.819 29.707  -24.802 1.00 38.93  ?  329 GLU A C     1 
ATOM   2640 O  O     . GLU A 1 330 ? -18.810 29.920  -25.479 1.00 37.49  ?  329 GLU A O     1 
ATOM   2641 C  CB    . GLU A 1 330 ? -20.162 31.162  -22.788 1.00 41.64  ?  329 GLU A CB    1 
ATOM   2642 C  CG    . GLU A 1 330 ? -20.498 31.254  -21.298 1.00 49.44  ?  329 GLU A CG    1 
ATOM   2643 C  CD    . GLU A 1 330 ? -19.266 31.360  -20.401 1.00 58.43  ?  329 GLU A CD    1 
ATOM   2644 O  OE1   . GLU A 1 330 ? -18.127 31.271  -20.916 1.00 61.30  ?  329 GLU A OE1   1 
ATOM   2645 O  OE2   . GLU A 1 330 ? -19.436 31.530  -19.171 1.00 59.24  -1 329 GLU A OE2   1 
ATOM   2646 N  N     . LYS A 1 331 ? -21.001 29.417  -25.338 1.00 44.98  ?  330 LYS A N     1 
ATOM   2647 C  CA    . LYS A 1 331 ? -21.178 29.243  -26.779 1.00 50.96  ?  330 LYS A CA    1 
ATOM   2648 C  C     . LYS A 1 331 ? -21.543 30.555  -27.468 1.00 52.79  ?  330 LYS A C     1 
ATOM   2649 O  O     . LYS A 1 331 ? -21.762 31.573  -26.812 1.00 52.76  ?  330 LYS A O     1 
ATOM   2650 C  CB    . LYS A 1 331 ? -22.252 28.183  -27.054 1.00 55.28  ?  330 LYS A CB    1 
ATOM   2651 C  CG    . LYS A 1 331 ? -22.501 27.880  -28.525 1.00 58.57  ?  330 LYS A CG    1 
ATOM   2652 C  CD    . LYS A 1 331 ? -23.119 26.494  -28.699 1.00 60.45  ?  330 LYS A CD    1 
ATOM   2653 C  CE    . LYS A 1 331 ? -24.343 26.304  -27.810 1.00 61.83  ?  330 LYS A CE    1 
ATOM   2654 N  NZ    . LYS A 1 331 ? -24.862 24.900  -27.837 1.00 61.68  1  330 LYS A NZ    1 
HETATM 2655 P  PG    . ATP B 2 .   ? -5.439  7.738   -3.891  1.00 19.98  ?  401 ATP A PG    1 
HETATM 2656 O  O1G   . ATP B 2 .   ? -6.727  7.220   -4.458  1.00 22.40  ?  401 ATP A O1G   1 
HETATM 2657 O  O2G   . ATP B 2 .   ? -5.314  7.618   -2.394  1.00 20.48  -1 401 ATP A O2G   1 
HETATM 2658 O  O3G   . ATP B 2 .   ? -5.019  9.066   -4.475  1.00 18.13  ?  401 ATP A O3G   1 
HETATM 2659 P  PB    . ATP B 2 .   ? -3.132  6.069   -3.652  1.00 19.91  ?  401 ATP A PB    1 
HETATM 2660 O  O1B   . ATP B 2 .   ? -2.049  5.752   -4.651  1.00 20.73  -1 401 ATP A O1B   1 
HETATM 2661 O  O2B   . ATP B 2 .   ? -2.757  6.939   -2.486  1.00 19.95  ?  401 ATP A O2B   1 
HETATM 2662 O  O3B   . ATP B 2 .   ? -4.349  6.703   -4.495  1.00 21.68  ?  401 ATP A O3B   1 
HETATM 2663 P  PA    . ATP B 2 .   ? -4.297  4.247   -1.737  1.00 23.84  ?  401 ATP A PA    1 
HETATM 2664 O  O1A   . ATP B 2 .   ? -5.497  3.366   -1.942  1.00 25.66  -1 401 ATP A O1A   1 
HETATM 2665 O  O2A   . ATP B 2 .   ? -4.315  5.456   -0.842  1.00 19.91  ?  401 ATP A O2A   1 
HETATM 2666 O  O3A   . ATP B 2 .   ? -3.774  4.658   -3.209  1.00 22.94  ?  401 ATP A O3A   1 
HETATM 2667 O  "O5'" . ATP B 2 .   ? -3.086  3.316   -1.244  1.00 22.17  ?  401 ATP A "O5'" 1 
HETATM 2668 C  "C5'" . ATP B 2 .   ? -1.873  3.908   -0.794  1.00 19.98  ?  401 ATP A "C5'" 1 
HETATM 2669 C  "C4'" . ATP B 2 .   ? -0.742  2.983   -1.224  1.00 20.71  ?  401 ATP A "C4'" 1 
HETATM 2670 O  "O4'" . ATP B 2 .   ? -0.894  1.711   -0.587  1.00 22.59  ?  401 ATP A "O4'" 1 
HETATM 2671 C  "C3'" . ATP B 2 .   ? -0.742  2.682   -2.715  1.00 20.52  ?  401 ATP A "C3'" 1 
HETATM 2672 O  "O3'" . ATP B 2 .   ? 0.007   3.649   -3.455  1.00 22.08  ?  401 ATP A "O3'" 1 
HETATM 2673 C  "C2'" . ATP B 2 .   ? -0.099  1.309   -2.768  1.00 22.56  ?  401 ATP A "C2'" 1 
HETATM 2674 O  "O2'" . ATP B 2 .   ? 1.328   1.409   -2.708  1.00 21.02  ?  401 ATP A "O2'" 1 
HETATM 2675 C  "C1'" . ATP B 2 .   ? -0.564  0.649   -1.483  1.00 22.75  ?  401 ATP A "C1'" 1 
HETATM 2676 N  N9    . ATP B 2 .   ? -1.801  -0.092  -1.799  1.00 22.09  ?  401 ATP A N9    1 
HETATM 2677 C  C8    . ATP B 2 .   ? -3.049  0.320   -1.509  1.00 24.19  ?  401 ATP A C8    1 
HETATM 2678 N  N7    . ATP B 2 .   ? -3.975  -0.576  -1.936  1.00 22.92  ?  401 ATP A N7    1 
HETATM 2679 C  C5    . ATP B 2 .   ? -3.313  -1.587  -2.522  1.00 24.50  ?  401 ATP A C5    1 
HETATM 2680 C  C6    . ATP B 2 .   ? -3.694  -2.857  -3.179  1.00 31.17  ?  401 ATP A C6    1 
HETATM 2681 N  N6    . ATP B 2 .   ? -4.996  -3.211  -3.295  1.00 36.25  ?  401 ATP A N6    1 
HETATM 2682 N  N1    . ATP B 2 .   ? -2.702  -3.638  -3.651  1.00 30.90  ?  401 ATP A N1    1 
HETATM 2683 C  C2    . ATP B 2 .   ? -1.410  -3.279  -3.528  1.00 31.27  ?  401 ATP A C2    1 
HETATM 2684 N  N3    . ATP B 2 .   ? -0.991  -2.141  -2.945  1.00 26.32  ?  401 ATP A N3    1 
HETATM 2685 C  C4    . ATP B 2 .   ? -1.881  -1.267  -2.429  1.00 24.75  ?  401 ATP A C4    1 
HETATM 2686 P  PA    A UTP C 3 .   ? -7.971  -0.850  1.499   0.50 48.16  ?  402 UTP A PA    1 
HETATM 2687 P  PA    B UTP C 3 .   ? -7.564  -1.911  3.706   0.50 50.29  ?  402 UTP A PA    1 
HETATM 2688 O  O1A   A UTP C 3 .   ? -7.722  -1.828  0.349   0.50 48.35  ?  402 UTP A O1A   1 
HETATM 2689 O  O1A   B UTP C 3 .   ? -7.206  -2.442  5.096   0.50 50.17  ?  402 UTP A O1A   1 
HETATM 2690 O  O2A   A UTP C 3 .   ? -8.715  0.346   1.002   0.50 49.77  -1 402 UTP A O2A   1 
HETATM 2691 O  O2A   B UTP C 3 .   ? -6.845  -2.713  2.673   0.50 50.43  -1 402 UTP A O2A   1 
HETATM 2692 O  O3A   A UTP C 3 .   ? -8.842  -1.613  2.690   0.50 50.90  ?  402 UTP A O3A   1 
HETATM 2693 O  O3A   B UTP C 3 .   ? -9.205  -2.031  3.440   0.50 53.01  ?  402 UTP A O3A   1 
HETATM 2694 O  "O5'" A UTP C 3 .   ? -6.524  -0.362  2.150   0.50 46.53  ?  402 UTP A "O5'" 1 
HETATM 2695 O  "O5'" B UTP C 3 .   ? -7.088  -0.324  3.590   0.50 46.95  ?  402 UTP A "O5'" 1 
HETATM 2696 P  PB    A UTP C 3 .   ? -8.186  -2.828  3.610   0.50 51.65  ?  402 UTP A PB    1 
HETATM 2697 P  PB    B UTP C 3 .   ? -10.338 -2.384  4.606   0.50 56.90  ?  402 UTP A PB    1 
HETATM 2698 O  O1B   A UTP C 3 .   ? -7.393  -2.222  4.772   0.50 50.22  ?  402 UTP A O1B   1 
HETATM 2699 O  O1B   B UTP C 3 .   ? -9.949  -3.664  5.347   0.50 57.11  ?  402 UTP A O1B   1 
HETATM 2700 O  O2B   A UTP C 3 .   ? -7.252  -3.662  2.758   0.50 51.08  -1 402 UTP A O2B   1 
HETATM 2701 O  O2B   B UTP C 3 .   ? -10.417 -1.246  5.601   0.50 57.10  -1 402 UTP A O2B   1 
HETATM 2702 O  O3B   A UTP C 3 .   ? -9.410  -3.791  4.180   0.50 54.97  ?  402 UTP A O3B   1 
HETATM 2703 O  O3B   B UTP C 3 .   ? -11.816 -2.605  3.885   0.50 58.86  ?  402 UTP A O3B   1 
HETATM 2704 P  PG    A UTP C 3 .   ? -10.711 -3.241  5.015   0.50 57.45  ?  402 UTP A PG    1 
HETATM 2705 P  PG    B UTP C 3 .   ? -12.741 -3.941  4.105   0.50 61.46  ?  402 UTP A PG    1 
HETATM 2706 O  O1G   A UTP C 3 .   ? -10.318 -2.956  6.465   0.50 56.56  -1 402 UTP A O1G   1 
HETATM 2707 O  O1G   B UTP C 3 .   ? -13.087 -4.093  5.588   0.50 61.54  -1 402 UTP A O1G   1 
HETATM 2708 O  O2G   A UTP C 3 .   ? -11.221 -1.977  4.378   0.50 57.93  ?  402 UTP A O2G   1 
HETATM 2709 O  O2G   B UTP C 3 .   ? -11.983 -5.156  3.645   0.50 60.84  ?  402 UTP A O2G   1 
HETATM 2710 O  O3G   A UTP C 3 .   ? -11.787 -4.296  4.991   0.50 59.45  ?  402 UTP A O3G   1 
HETATM 2711 O  O3G   B UTP C 3 .   ? -14.016 -3.805  3.310   0.50 62.28  ?  402 UTP A O3G   1 
HETATM 2712 C  "C5'" A UTP C 3 .   ? -6.562  0.594   3.188   0.50 45.32  ?  402 UTP A "C5'" 1 
HETATM 2713 C  "C5'" B UTP C 3 .   ? -6.435  0.080   2.406   0.50 46.15  ?  402 UTP A "C5'" 1 
HETATM 2714 C  "C4'" A UTP C 3 .   ? -5.300  1.448   3.107   0.50 44.37  ?  402 UTP A "C4'" 1 
HETATM 2715 C  "C4'" B UTP C 3 .   ? -5.430  1.186   2.725   0.50 44.64  ?  402 UTP A "C4'" 1 
HETATM 2716 O  "O4'" A UTP C 3 .   ? -4.078  0.608   3.626   0.50 42.59  ?  402 UTP A "O4'" 1 
HETATM 2717 O  "O4'" B UTP C 3 .   ? -4.202  0.567   3.493   0.50 42.83  ?  402 UTP A "O4'" 1 
HETATM 2718 C  "C1'" A UTP C 3 .   ? -2.896  1.017   2.721   0.50 40.59  ?  402 UTP A "C1'" 1 
HETATM 2719 C  "C1'" B UTP C 3 .   ? -2.940  1.001   2.716   0.50 40.60  ?  402 UTP A "C1'" 1 
HETATM 2720 C  "C2'" A UTP C 3 .   ? -3.385  1.890   1.834   0.50 42.78  ?  402 UTP A "C2'" 1 
HETATM 2721 C  "C2'" B UTP C 3 .   ? -3.355  1.914   1.831   0.50 42.79  ?  402 UTP A "C2'" 1 
HETATM 2722 O  "O2'" A UTP C 3 .   ? -3.028  3.235   2.213   0.50 42.75  ?  402 UTP A "O2'" 1 
HETATM 2723 O  "O2'" B UTP C 3 .   ? -3.120  3.244   2.337   0.50 42.63  ?  402 UTP A "O2'" 1 
HETATM 2724 C  "C3'" A UTP C 3 .   ? -5.005  1.732   1.860   0.50 43.99  ?  402 UTP A "C3'" 1 
HETATM 2725 C  "C3'" B UTP C 3 .   ? -4.955  1.692   1.609   0.50 43.99  ?  402 UTP A "C3'" 1 
HETATM 2726 O  "O3'" A UTP C 3 .   ? -5.617  2.982   1.458   0.50 45.13  ?  402 UTP A "O3'" 1 
HETATM 2727 O  "O3'" B UTP C 3 .   ? -5.587  2.964   1.322   0.50 45.02  ?  402 UTP A "O3'" 1 
HETATM 2728 N  N1    . UTP C 3 .   ? -2.328  -0.155  2.041   1.00 31.94  ?  402 UTP A N1    1 
HETATM 2729 C  C6    . UTP C 3 .   ? -3.105  -1.127  1.567   1.00 26.72  ?  402 UTP A C6    1 
HETATM 2730 C  C2    . UTP C 3 .   ? -0.978  -0.241  1.899   1.00 28.09  ?  402 UTP A C2    1 
HETATM 2731 O  O2    . UTP C 3 .   ? -0.265  0.642   2.329   1.00 28.83  ?  402 UTP A O2    1 
HETATM 2732 N  N3    . UTP C 3 .   ? -0.425  -1.316  1.274   1.00 25.54  ?  402 UTP A N3    1 
HETATM 2733 C  C4    . UTP C 3 .   ? -1.207  -2.284  0.801   1.00 25.92  ?  402 UTP A C4    1 
HETATM 2734 O  O4    . UTP C 3 .   ? -0.730  -3.232  0.249   1.00 27.09  ?  402 UTP A O4    1 
HETATM 2735 C  C5    . UTP C 3 .   ? -2.565  -2.199  0.943   1.00 26.39  ?  402 UTP A C5    1 
HETATM 2736 MG MG    . MG  D 4 .   ? -3.947  7.438   -1.029  1.00 19.33  ?  403 MG  A MG    1 
HETATM 2737 MG MG    . MG  E 4 .   ? -5.124  5.370   1.758   1.00 26.32  ?  404 MG  A MG    1 
HETATM 2738 O  O     . HOH F 5 .   ? -8.078  18.681  -27.355 1.00 24.32  ?  501 HOH A O     1 
HETATM 2739 O  O     . HOH F 5 .   ? -20.549 2.649   -0.872  1.00 48.55  ?  502 HOH A O     1 
HETATM 2740 O  O     . HOH F 5 .   ? -12.003 3.332   -29.455 1.00 34.87  ?  503 HOH A O     1 
HETATM 2741 O  O     . HOH F 5 .   ? -0.425  5.342   -28.712 1.00 46.17  ?  504 HOH A O     1 
HETATM 2742 O  O     . HOH F 5 .   ? -1.451  19.629  -31.783 1.00 48.27  ?  505 HOH A O     1 
HETATM 2743 O  O     . HOH F 5 .   ? 5.478   26.148  -33.214 1.00 51.25  ?  506 HOH A O     1 
HETATM 2744 O  O     . HOH F 5 .   ? -11.604 12.413  9.356   1.00 50.20  ?  507 HOH A O     1 
HETATM 2745 O  O     . HOH F 5 .   ? 9.187   15.822  5.414   1.00 41.48  ?  508 HOH A O     1 
HETATM 2746 O  O     . HOH F 5 .   ? -6.800  4.076   -3.779  1.00 32.75  ?  509 HOH A O     1 
HETATM 2747 O  O     . HOH F 5 .   ? -24.914 -23.641 -15.737 1.00 30.11  ?  510 HOH A O     1 
HETATM 2748 O  O     . HOH F 5 .   ? 8.923   4.107   18.475  1.00 39.42  ?  511 HOH A O     1 
HETATM 2749 O  O     . HOH F 5 .   ? 7.317   19.444  -23.914 1.00 32.95  ?  512 HOH A O     1 
HETATM 2750 O  O     . HOH F 5 .   ? 10.560  -2.627  -9.848  1.00 51.64  ?  513 HOH A O     1 
HETATM 2751 O  O     . HOH F 5 .   ? -23.170 31.526  -24.838 1.00 48.99  ?  514 HOH A O     1 
HETATM 2752 O  O     . HOH F 5 .   ? 6.394   -4.095  -15.202 1.00 33.39  ?  515 HOH A O     1 
HETATM 2753 O  O     . HOH F 5 .   ? 11.514  3.765   22.063  1.00 42.41  ?  516 HOH A O     1 
HETATM 2754 O  O     . HOH F 5 .   ? 14.385  21.401  -31.536 1.00 28.76  ?  517 HOH A O     1 
HETATM 2755 O  O     . HOH F 5 .   ? -8.534  4.740   3.988   1.00 41.92  ?  518 HOH A O     1 
HETATM 2756 O  O     . HOH F 5 .   ? -11.311 14.401  -6.651  1.00 29.32  ?  519 HOH A O     1 
HETATM 2757 O  O     . HOH F 5 .   ? -6.171  -6.112  -3.839  1.00 38.77  ?  520 HOH A O     1 
HETATM 2758 O  O     . HOH F 5 .   ? -10.728 12.492  -3.678  1.00 43.27  ?  521 HOH A O     1 
HETATM 2759 O  O     . HOH F 5 .   ? 14.910  2.059   -9.803  1.00 23.35  ?  522 HOH A O     1 
HETATM 2760 O  O     . HOH F 5 .   ? -19.373 -5.625  -21.845 1.00 52.78  ?  523 HOH A O     1 
HETATM 2761 O  O     . HOH F 5 .   ? -15.369 -8.233  -2.460  1.00 44.03  ?  524 HOH A O     1 
HETATM 2762 O  O     . HOH F 5 .   ? -9.415  24.398  -26.326 1.00 24.45  ?  525 HOH A O     1 
HETATM 2763 O  O     . HOH F 5 .   ? -25.132 17.016  -21.249 1.00 29.10  ?  526 HOH A O     1 
HETATM 2764 O  O     . HOH F 5 .   ? -22.025 -5.816  -5.812  1.00 24.85  ?  527 HOH A O     1 
HETATM 2765 O  O     . HOH F 5 .   ? -2.446  14.896  12.061  1.00 33.40  ?  528 HOH A O     1 
HETATM 2766 O  O     . HOH F 5 .   ? 9.897   -6.141  -0.692  1.00 35.66  ?  529 HOH A O     1 
HETATM 2767 O  O     . HOH F 5 .   ? -0.597  15.493  -2.382  1.00 35.68  ?  530 HOH A O     1 
HETATM 2768 O  O     . HOH F 5 .   ? -17.350 29.354  -19.457 1.00 42.28  ?  531 HOH A O     1 
HETATM 2769 O  O     . HOH F 5 .   ? -1.979  20.446  -27.591 1.00 37.17  ?  532 HOH A O     1 
HETATM 2770 O  O     . HOH F 5 .   ? 1.843   -3.056  -20.508 1.00 34.32  ?  533 HOH A O     1 
HETATM 2771 O  O     . HOH F 5 .   ? -16.996 29.239  -27.115 1.00 44.92  ?  534 HOH A O     1 
HETATM 2772 O  O     . HOH F 5 .   ? -3.065  -7.899  -0.684  1.00 57.79  ?  535 HOH A O     1 
HETATM 2773 O  O     . HOH F 5 .   ? 11.049  23.632  -30.802 1.00 38.34  ?  536 HOH A O     1 
HETATM 2774 O  O     . HOH F 5 .   ? -17.319 10.465  -4.549  1.00 34.54  ?  537 HOH A O     1 
HETATM 2775 O  O     . HOH F 5 .   ? 1.664   -4.388  -0.284  1.00 26.19  ?  538 HOH A O     1 
HETATM 2776 O  O     . HOH F 5 .   ? -9.066  23.708  -6.910  1.00 38.46  ?  539 HOH A O     1 
HETATM 2777 O  O     . HOH F 5 .   ? 8.087   7.757   -3.782  1.00 45.34  ?  540 HOH A O     1 
HETATM 2778 O  O     . HOH F 5 .   ? -23.563 13.467  -21.129 1.00 26.96  ?  541 HOH A O     1 
HETATM 2779 O  O     . HOH F 5 .   ? -8.673  -11.285 -9.203  1.00 39.85  ?  542 HOH A O     1 
HETATM 2780 O  O     . HOH F 5 .   ? -23.018 28.559  -23.992 1.00 42.60  ?  543 HOH A O     1 
HETATM 2781 O  O     . HOH F 5 .   ? 2.120   -1.358  0.867   1.00 27.10  ?  544 HOH A O     1 
HETATM 2782 O  O     . HOH F 5 .   ? -7.938  9.848   -4.121  1.00 46.22  ?  545 HOH A O     1 
HETATM 2783 O  O     . HOH F 5 .   ? -27.156 9.083   -6.423  1.00 29.58  ?  546 HOH A O     1 
HETATM 2784 O  O     . HOH F 5 .   ? 17.658  -2.716  11.444  1.00 44.68  ?  547 HOH A O     1 
HETATM 2785 O  O     . HOH F 5 .   ? -26.596 -6.857  -14.607 1.00 22.82  ?  548 HOH A O     1 
HETATM 2786 O  O     . HOH F 5 .   ? 2.758   18.313  -6.781  1.00 25.48  ?  549 HOH A O     1 
HETATM 2787 O  O     . HOH F 5 .   ? -6.954  14.298  -30.923 1.00 25.90  ?  550 HOH A O     1 
HETATM 2788 O  O     . HOH F 5 .   ? 0.181   14.973  -5.733  1.00 28.85  ?  551 HOH A O     1 
HETATM 2789 O  O     . HOH F 5 .   ? 12.250  9.288   -20.917 1.00 37.63  ?  552 HOH A O     1 
HETATM 2790 O  O     . HOH F 5 .   ? -6.608  12.892  -2.052  1.00 40.65  ?  553 HOH A O     1 
HETATM 2791 O  O     . HOH F 5 .   ? 3.346   -3.739  -2.611  1.00 22.29  ?  554 HOH A O     1 
HETATM 2792 O  O     . HOH F 5 .   ? -9.267  -4.903  -4.684  1.00 30.76  ?  555 HOH A O     1 
HETATM 2793 O  O     . HOH F 5 .   ? 9.583   -7.266  7.016   1.00 26.83  ?  556 HOH A O     1 
HETATM 2794 O  O     . HOH F 5 .   ? -5.940  -8.565  -20.037 1.00 31.15  ?  557 HOH A O     1 
HETATM 2795 O  O     . HOH F 5 .   ? 2.125   1.623   -21.246 1.00 25.98  ?  558 HOH A O     1 
HETATM 2796 O  O     . HOH F 5 .   ? -18.025 21.699  -15.324 1.00 18.76  ?  559 HOH A O     1 
HETATM 2797 O  O     . HOH F 5 .   ? -13.730 -5.829  -23.170 1.00 34.82  ?  560 HOH A O     1 
HETATM 2798 O  O     . HOH F 5 .   ? 9.612   -10.989 -7.556  1.00 36.22  ?  561 HOH A O     1 
HETATM 2799 O  O     . HOH F 5 .   ? 1.390   20.908  -12.306 1.00 42.59  ?  562 HOH A O     1 
HETATM 2800 O  O     . HOH F 5 .   ? -23.314 13.874  -15.534 1.00 18.65  ?  563 HOH A O     1 
HETATM 2801 O  O     . HOH F 5 .   ? 7.840   14.854  -15.029 1.00 26.81  ?  564 HOH A O     1 
HETATM 2802 O  O     . HOH F 5 .   ? 2.770   7.086   -27.260 1.00 36.73  ?  565 HOH A O     1 
HETATM 2803 O  O     . HOH F 5 .   ? -28.315 -21.932 -14.518 1.00 42.81  ?  566 HOH A O     1 
HETATM 2804 O  O     . HOH F 5 .   ? -8.541  10.577  -30.769 1.00 24.61  ?  567 HOH A O     1 
HETATM 2805 O  O     . HOH F 5 .   ? -2.856  15.415  -31.253 1.00 31.59  ?  568 HOH A O     1 
HETATM 2806 O  O     . HOH F 5 .   ? -1.991  6.968   -7.087  1.00 19.70  ?  569 HOH A O     1 
HETATM 2807 O  O     . HOH F 5 .   ? 11.678  -3.350  -6.324  1.00 35.18  ?  570 HOH A O     1 
HETATM 2808 O  O     . HOH F 5 .   ? -10.893 28.644  -17.518 1.00 39.67  ?  571 HOH A O     1 
HETATM 2809 O  O     . HOH F 5 .   ? -2.901  6.661   -23.572 1.00 12.48  ?  572 HOH A O     1 
HETATM 2810 O  O     . HOH F 5 .   ? 1.586   -7.047  0.407   1.00 29.75  ?  573 HOH A O     1 
HETATM 2811 O  O     . HOH F 5 .   ? -10.552 -7.831  -10.912 1.00 20.48  ?  574 HOH A O     1 
HETATM 2812 O  O     . HOH F 5 .   ? 2.898   3.476   -1.630  1.00 27.72  ?  575 HOH A O     1 
HETATM 2813 O  O     . HOH F 5 .   ? 4.726   -13.863 13.067  1.00 46.48  ?  576 HOH A O     1 
HETATM 2814 O  O     . HOH F 5 .   ? -11.823 24.787  -7.536  1.00 48.78  ?  577 HOH A O     1 
HETATM 2815 O  O     . HOH F 5 .   ? 5.388   9.666   -9.875  1.00 20.89  ?  578 HOH A O     1 
HETATM 2816 O  O     . HOH F 5 .   ? -3.261  9.392   -1.032  1.00 20.01  ?  579 HOH A O     1 
HETATM 2817 O  O     . HOH F 5 .   ? -5.466  22.564  -7.317  1.00 26.58  ?  580 HOH A O     1 
HETATM 2818 O  O     . HOH F 5 .   ? 9.594   8.914   2.263   1.00 30.90  ?  581 HOH A O     1 
HETATM 2819 O  O     . HOH F 5 .   ? -0.361  -2.786  7.806   1.00 24.24  ?  582 HOH A O     1 
HETATM 2820 O  O     . HOH F 5 .   ? -13.772 19.346  -30.638 1.00 40.06  ?  583 HOH A O     1 
HETATM 2821 O  O     . HOH F 5 .   ? -22.356 -7.429  -18.548 1.00 33.93  ?  584 HOH A O     1 
HETATM 2822 O  O     . HOH F 5 .   ? 0.931   14.877  17.433  1.00 36.47  ?  585 HOH A O     1 
HETATM 2823 O  O     . HOH F 5 .   ? -20.367 3.881   -7.124  1.00 34.60  ?  586 HOH A O     1 
HETATM 2824 O  O     . HOH F 5 .   ? 2.835   -14.346 8.207   1.00 43.43  ?  587 HOH A O     1 
HETATM 2825 O  O     . HOH F 5 .   ? -18.352 0.288   -10.007 1.00 19.49  ?  588 HOH A O     1 
HETATM 2826 O  O     . HOH F 5 .   ? -2.218  -5.747  -0.289  1.00 47.18  ?  589 HOH A O     1 
HETATM 2827 O  O     . HOH F 5 .   ? -14.967 18.203  -11.071 1.00 16.34  ?  590 HOH A O     1 
HETATM 2828 O  O     . HOH F 5 .   ? -21.180 9.200   -23.029 1.00 22.88  ?  591 HOH A O     1 
HETATM 2829 O  O     . HOH F 5 .   ? 13.753  -0.782  18.333  1.00 47.72  ?  592 HOH A O     1 
HETATM 2830 O  O     . HOH F 5 .   ? -8.080  -8.050  -17.030 1.00 24.92  ?  593 HOH A O     1 
HETATM 2831 O  O     . HOH F 5 .   ? -22.825 7.761   -11.185 1.00 26.24  ?  594 HOH A O     1 
HETATM 2832 O  O     . HOH F 5 .   ? -10.388 4.901   -29.679 1.00 44.59  ?  595 HOH A O     1 
HETATM 2833 O  O     . HOH F 5 .   ? -17.884 -16.649 -19.552 1.00 42.77  ?  596 HOH A O     1 
HETATM 2834 O  O     . HOH F 5 .   ? -10.701 -10.790 -11.764 1.00 31.78  ?  597 HOH A O     1 
HETATM 2835 O  O     . HOH F 5 .   ? -5.382  11.742  -4.048  1.00 24.89  ?  598 HOH A O     1 
HETATM 2836 O  O     . HOH F 5 .   ? -3.105  4.049   -23.923 1.00 18.64  ?  599 HOH A O     1 
HETATM 2837 O  O     . HOH F 5 .   ? 8.829   -6.293  -5.886  1.00 23.49  ?  600 HOH A O     1 
HETATM 2838 O  O     . HOH F 5 .   ? 6.182   7.878   -7.763  1.00 24.18  ?  601 HOH A O     1 
HETATM 2839 O  O     . HOH F 5 .   ? 10.984  5.721   -19.810 1.00 32.87  ?  602 HOH A O     1 
HETATM 2840 O  O     . HOH F 5 .   ? 6.536   -6.071  -13.194 1.00 27.60  ?  603 HOH A O     1 
HETATM 2841 O  O     . HOH F 5 .   ? -3.003  25.619  -17.449 1.00 29.99  ?  604 HOH A O     1 
HETATM 2842 O  O     . HOH F 5 .   ? -11.279 -12.470 -15.403 1.00 29.84  ?  605 HOH A O     1 
HETATM 2843 O  O     . HOH F 5 .   ? -21.372 29.739  -18.404 1.00 42.77  ?  606 HOH A O     1 
HETATM 2844 O  O     . HOH F 5 .   ? -1.186  24.867  -15.809 1.00 48.38  ?  607 HOH A O     1 
HETATM 2845 O  O     . HOH F 5 .   ? 9.038   18.285  -17.436 1.00 40.07  ?  608 HOH A O     1 
HETATM 2846 O  O     . HOH F 5 .   ? -18.919 18.094  -9.819  1.00 38.48  ?  609 HOH A O     1 
HETATM 2847 O  O     . HOH F 5 .   ? -4.719  -11.079 -6.732  1.00 26.77  ?  610 HOH A O     1 
HETATM 2848 O  O     . HOH F 5 .   ? -13.840 20.475  -6.854  1.00 41.26  ?  611 HOH A O     1 
HETATM 2849 O  O     . HOH F 5 .   ? -18.360 27.209  -28.290 1.00 29.98  ?  612 HOH A O     1 
HETATM 2850 O  O     . HOH F 5 .   ? -18.521 7.938   -17.006 1.00 14.34  ?  613 HOH A O     1 
HETATM 2851 O  O     . HOH F 5 .   ? 6.698   14.390  -2.513  1.00 33.47  ?  614 HOH A O     1 
HETATM 2852 O  O     . HOH F 5 .   ? -16.374 -4.161  -3.181  1.00 41.04  ?  615 HOH A O     1 
HETATM 2853 O  O     . HOH F 5 .   ? -20.850 27.210  -20.100 1.00 35.89  ?  616 HOH A O     1 
HETATM 2854 O  O     . HOH F 5 .   ? -15.102 -0.681  -25.856 1.00 33.05  ?  617 HOH A O     1 
HETATM 2855 O  O     . HOH F 5 .   ? 2.006   -1.274  -2.892  1.00 34.83  ?  618 HOH A O     1 
HETATM 2856 O  O     . HOH F 5 .   ? -6.674  17.501  -25.207 1.00 16.20  ?  619 HOH A O     1 
HETATM 2857 O  O     . HOH F 5 .   ? -0.446  9.534   -0.078  1.00 20.89  ?  620 HOH A O     1 
HETATM 2858 O  O     . HOH F 5 .   ? 8.313   16.424  -24.817 1.00 40.56  ?  621 HOH A O     1 
HETATM 2859 O  O     . HOH F 5 .   ? -11.538 27.717  -20.722 1.00 30.92  ?  622 HOH A O     1 
HETATM 2860 O  O     . HOH F 5 .   ? -14.742 -11.623 -22.454 1.00 41.80  ?  623 HOH A O     1 
HETATM 2861 O  O     . HOH F 5 .   ? 9.384   -1.109  -0.805  1.00 30.81  ?  624 HOH A O     1 
HETATM 2862 O  O     . HOH F 5 .   ? -8.009  16.568  -28.565 1.00 20.52  ?  625 HOH A O     1 
HETATM 2863 O  O     . HOH F 5 .   ? -15.887 -7.897  -20.663 1.00 25.78  ?  626 HOH A O     1 
HETATM 2864 O  O     . HOH F 5 .   ? 3.359   24.243  1.074   1.00 40.47  ?  627 HOH A O     1 
HETATM 2865 O  O     . HOH F 5 .   ? 4.434   -13.225 -3.392  1.00 43.48  ?  628 HOH A O     1 
HETATM 2866 O  O     . HOH F 5 .   ? 4.099   6.589   -24.073 1.00 19.80  ?  629 HOH A O     1 
HETATM 2867 O  O     . HOH F 5 .   ? -22.277 18.236  -25.545 1.00 27.80  ?  630 HOH A O     1 
HETATM 2868 O  O     . HOH F 5 .   ? 8.883   15.375  -26.760 1.00 40.75  ?  631 HOH A O     1 
HETATM 2869 O  O     . HOH F 5 .   ? -10.906 20.442  -6.748  1.00 29.15  ?  632 HOH A O     1 
HETATM 2870 O  O     . HOH F 5 .   ? -23.436 7.168   -17.940 1.00 26.79  ?  633 HOH A O     1 
HETATM 2871 O  O     . HOH F 5 .   ? -8.096  28.923  -15.417 1.00 31.87  ?  634 HOH A O     1 
HETATM 2872 O  O     . HOH F 5 .   ? 0.001   10.429  21.089  1.00 52.80  ?  635 HOH A O     1 
HETATM 2873 O  O     . HOH F 5 .   ? -22.297 2.871   -21.104 1.00 27.33  ?  636 HOH A O     1 
HETATM 2874 O  O     . HOH F 5 .   ? -13.553 1.693   -3.515  1.00 55.33  ?  637 HOH A O     1 
HETATM 2875 O  O     . HOH F 5 .   ? -7.862  7.016   -1.295  1.00 31.81  ?  638 HOH A O     1 
HETATM 2876 O  O     . HOH F 5 .   ? 5.322   25.987  -37.513 1.00 52.61  ?  639 HOH A O     1 
HETATM 2877 O  O     . HOH F 5 .   ? -12.688 26.372  -10.455 1.00 26.44  ?  640 HOH A O     1 
HETATM 2878 O  O     . HOH F 5 .   ? 8.968   6.693   0.090   1.00 27.15  ?  641 HOH A O     1 
HETATM 2879 O  O     . HOH F 5 .   ? -0.750  -11.968 -4.807  1.00 41.99  ?  642 HOH A O     1 
HETATM 2880 O  O     . HOH F 5 .   ? 2.779   17.340  -20.512 1.00 16.11  ?  643 HOH A O     1 
HETATM 2881 O  O     . HOH F 5 .   ? 6.806   8.388   -14.940 1.00 16.64  ?  644 HOH A O     1 
HETATM 2882 O  O     . HOH F 5 .   ? 2.490   -8.069  -12.245 1.00 30.06  ?  645 HOH A O     1 
HETATM 2883 O  O     . HOH F 5 .   ? 12.471  7.005   -8.501  1.00 36.66  ?  646 HOH A O     1 
HETATM 2884 O  O     . HOH F 5 .   ? 7.013   18.393  -16.566 1.00 45.00  ?  647 HOH A O     1 
HETATM 2885 O  O     . HOH F 5 .   ? -1.075  13.830  -30.214 1.00 29.35  ?  648 HOH A O     1 
HETATM 2886 O  O     . HOH F 5 .   ? -0.565  21.156  -22.668 1.00 18.64  ?  649 HOH A O     1 
HETATM 2887 O  O     . HOH F 5 .   ? -14.250 11.057  -32.571 1.00 34.71  ?  650 HOH A O     1 
HETATM 2888 O  O     . HOH F 5 .   ? -2.273  21.709  -15.873 1.00 13.86  ?  651 HOH A O     1 
HETATM 2889 O  O     . HOH F 5 .   ? 11.765  2.985   -16.643 1.00 42.17  ?  652 HOH A O     1 
HETATM 2890 O  O     . HOH F 5 .   ? -6.787  23.877  -26.442 1.00 20.46  ?  653 HOH A O     1 
HETATM 2891 O  O     . HOH F 5 .   ? -21.127 13.201  -22.246 1.00 25.10  ?  654 HOH A O     1 
HETATM 2892 O  O     . HOH F 5 .   ? 6.600   14.328  -10.111 1.00 27.33  ?  655 HOH A O     1 
HETATM 2893 O  O     . HOH F 5 .   ? -6.163  27.380  -14.678 1.00 31.05  ?  656 HOH A O     1 
HETATM 2894 O  O     . HOH F 5 .   ? -5.343  28.176  -19.675 1.00 36.18  ?  657 HOH A O     1 
HETATM 2895 O  O     . HOH F 5 .   ? -1.117  0.528   -24.035 1.00 30.04  ?  658 HOH A O     1 
HETATM 2896 O  O     . HOH F 5 .   ? -2.045  21.875  -3.948  1.00 30.02  ?  659 HOH A O     1 
HETATM 2897 O  O     . HOH F 5 .   ? 4.215   14.714  -34.511 1.00 40.04  ?  660 HOH A O     1 
HETATM 2898 O  O     . HOH F 5 .   ? 0.755   24.065  2.217   1.00 43.57  ?  661 HOH A O     1 
HETATM 2899 O  O     . HOH F 5 .   ? -7.419  5.405   0.648   1.00 42.91  ?  662 HOH A O     1 
HETATM 2900 O  O     . HOH F 5 .   ? 7.708   13.781  12.531  1.00 55.94  ?  663 HOH A O     1 
HETATM 2901 O  O     . HOH F 5 .   ? 13.437  2.256   2.980   1.00 58.13  ?  664 HOH A O     1 
HETATM 2902 O  O     . HOH F 5 .   ? 11.575  -0.372  0.609   1.00 36.82  ?  665 HOH A O     1 
HETATM 2903 O  O     . HOH F 5 .   ? -9.045  5.510   -3.638  1.00 49.69  ?  666 HOH A O     1 
HETATM 2904 O  O     . HOH F 5 .   ? -13.739 13.247  -2.877  1.00 40.37  ?  667 HOH A O     1 
HETATM 2905 O  O     . HOH F 5 .   ? 5.724   3.427   -21.361 1.00 41.61  ?  668 HOH A O     1 
HETATM 2906 O  O     . HOH F 5 .   ? -16.901 18.506  -9.132  1.00 35.80  ?  669 HOH A O     1 
HETATM 2907 O  O     . HOH F 5 .   ? -9.443  -1.710  15.558  1.00 40.33  ?  670 HOH A O     1 
HETATM 2908 O  O     . HOH F 5 .   ? -20.923 -3.369  -18.617 1.00 33.91  ?  671 HOH A O     1 
HETATM 2909 O  O     . HOH F 5 .   ? -17.698 22.851  -7.123  1.00 48.57  ?  672 HOH A O     1 
HETATM 2910 O  O     . HOH F 5 .   ? 10.375  7.542   14.170  1.00 50.20  ?  673 HOH A O     1 
HETATM 2911 O  O     . HOH F 5 .   ? -5.482  -7.425  -17.769 1.00 45.47  ?  674 HOH A O     1 
HETATM 2912 O  O     . HOH F 5 .   ? -10.173 -10.422 -16.029 1.00 26.44  ?  675 HOH A O     1 
HETATM 2913 O  O     . HOH F 5 .   ? 1.005   -11.288 -15.634 1.00 57.00  ?  676 HOH A O     1 
HETATM 2914 O  O     . HOH F 5 .   ? -23.896 -1.206  -15.663 1.00 36.82  ?  677 HOH A O     1 
HETATM 2915 O  O     . HOH F 5 .   ? 5.285   10.099  -12.869 1.00 26.46  ?  678 HOH A O     1 
HETATM 2916 O  O     . HOH F 5 .   ? -11.890 -11.153 -7.763  1.00 36.22  ?  679 HOH A O     1 
HETATM 2917 O  O     . HOH F 5 .   ? -3.926  -4.043  -24.023 1.00 38.51  ?  680 HOH A O     1 
HETATM 2918 O  O     . HOH F 5 .   ? 13.156  0.327   11.912  1.00 47.60  ?  681 HOH A O     1 
HETATM 2919 O  O     . HOH F 5 .   ? 2.157   16.479  -12.009 1.00 29.94  ?  682 HOH A O     1 
HETATM 2920 O  O     . HOH F 5 .   ? -23.252 16.700  -23.490 1.00 44.90  ?  683 HOH A O     1 
HETATM 2921 O  O     . HOH F 5 .   ? -15.393 1.514   -27.749 1.00 33.61  ?  684 HOH A O     1 
HETATM 2922 O  O     . HOH F 5 .   ? 8.549   1.803   -14.645 1.00 20.58  ?  685 HOH A O     1 
HETATM 2923 O  O     . HOH F 5 .   ? -18.175 -1.737  -23.094 1.00 31.91  ?  686 HOH A O     1 
HETATM 2924 O  O     . HOH F 5 .   ? 8.190   14.632  2.331   1.00 37.46  ?  687 HOH A O     1 
HETATM 2925 O  O     . HOH F 5 .   ? 8.671   11.348  -13.096 1.00 30.70  ?  688 HOH A O     1 
HETATM 2926 O  O     . HOH F 5 .   ? -19.555 -7.908  -21.380 1.00 37.83  ?  689 HOH A O     1 
HETATM 2927 O  O     . HOH F 5 .   ? -23.012 10.348  -12.091 1.00 36.39  ?  690 HOH A O     1 
HETATM 2928 O  O     . HOH F 5 .   ? -17.437 -13.243 -12.014 1.00 22.70  ?  691 HOH A O     1 
HETATM 2929 O  O     . HOH F 5 .   ? 10.236  12.371  -24.666 1.00 50.08  ?  692 HOH A O     1 
HETATM 2930 O  O     . HOH F 5 .   ? -4.283  3.171   -28.352 1.00 41.28  ?  693 HOH A O     1 
HETATM 2931 O  O     . HOH F 5 .   ? -16.989 -11.425 -10.209 1.00 31.08  ?  694 HOH A O     1 
HETATM 2932 O  O     . HOH F 5 .   ? -7.764  6.027   26.629  1.00 52.29  ?  695 HOH A O     1 
HETATM 2933 O  O     . HOH F 5 .   ? -6.238  2.289   -27.442 1.00 39.77  ?  696 HOH A O     1 
HETATM 2934 O  O     . HOH F 5 .   ? 1.955   10.609  -29.657 1.00 30.97  ?  697 HOH A O     1 
HETATM 2935 O  O     . HOH F 5 .   ? -16.192 26.848  -30.996 1.00 40.25  ?  698 HOH A O     1 
HETATM 2936 O  O     . HOH F 5 .   ? 11.629  -12.729 11.677  1.00 42.45  ?  699 HOH A O     1 
HETATM 2937 O  O     . HOH F 5 .   ? 4.062   4.884   -21.935 1.00 24.60  ?  700 HOH A O     1 
HETATM 2938 O  O     . HOH F 5 .   ? -22.584 6.973   -23.892 1.00 25.37  ?  701 HOH A O     1 
HETATM 2939 O  O     . HOH F 5 .   ? 4.234   -13.130 1.548   1.00 32.98  ?  702 HOH A O     1 
HETATM 2940 O  O     . HOH F 5 .   ? 9.412   9.650   -21.390 1.00 20.34  ?  703 HOH A O     1 
HETATM 2941 O  O     . HOH F 5 .   ? -11.470 9.491   -32.049 1.00 51.79  ?  704 HOH A O     1 
HETATM 2942 O  O     . HOH F 5 .   ? -24.114 1.201   -14.284 1.00 30.13  ?  705 HOH A O     1 
HETATM 2943 O  O     . HOH F 5 .   ? 8.111   19.382  6.905   1.00 38.67  ?  706 HOH A O     1 
HETATM 2944 O  O     . HOH F 5 .   ? -13.923 14.559  7.931   1.00 50.70  ?  707 HOH A O     1 
HETATM 2945 O  O     . HOH F 5 .   ? -0.280  3.668   3.547   1.00 31.77  ?  708 HOH A O     1 
HETATM 2946 O  O     . HOH F 5 .   ? -11.207 9.990   -35.203 1.00 56.88  ?  709 HOH A O     1 
HETATM 2947 O  O     . HOH F 5 .   ? -15.979 3.149   0.082   1.00 58.83  ?  710 HOH A O     1 
HETATM 2948 O  O     . HOH F 5 .   ? -21.682 -9.277  -7.972  1.00 23.53  ?  711 HOH A O     1 
HETATM 2949 O  O     . HOH F 5 .   ? 6.352   22.898  0.239   1.00 47.36  ?  712 HOH A O     1 
HETATM 2950 O  O     . HOH F 5 .   ? 1.234   18.678  -15.526 1.00 18.86  ?  713 HOH A O     1 
HETATM 2951 O  O     . HOH F 5 .   ? -2.528  -6.383  -21.187 1.00 37.74  ?  714 HOH A O     1 
HETATM 2952 O  O     . HOH F 5 .   ? 9.146   14.012  -22.135 1.00 30.41  ?  715 HOH A O     1 
HETATM 2953 O  O     . HOH F 5 .   ? 4.637   22.126  -9.458  1.00 58.64  ?  716 HOH A O     1 
HETATM 2954 O  O     . HOH F 5 .   ? -2.404  -6.949  -15.317 1.00 34.41  ?  717 HOH A O     1 
HETATM 2955 O  O     . HOH F 5 .   ? 5.347   0.069   -17.866 1.00 35.40  ?  718 HOH A O     1 
HETATM 2956 O  O     . HOH F 5 .   ? -16.977 -15.085 -10.287 1.00 35.75  ?  719 HOH A O     1 
HETATM 2957 O  O     . HOH F 5 .   ? -8.644  12.997  -1.571  1.00 41.44  ?  720 HOH A O     1 
HETATM 2958 O  O     . HOH F 5 .   ? -28.324 -10.376 -12.923 1.00 39.96  ?  721 HOH A O     1 
HETATM 2959 O  O     . HOH F 5 .   ? 1.547   16.468  -13.893 1.00 21.51  ?  722 HOH A O     1 
HETATM 2960 O  O     . HOH F 5 .   ? -12.573 3.847   -4.516  1.00 53.67  ?  723 HOH A O     1 
HETATM 2961 O  O     . HOH F 5 .   ? 1.004   21.440  -24.777 1.00 34.20  ?  724 HOH A O     1 
HETATM 2962 O  O     . HOH F 5 .   ? -23.729 11.859  -13.673 1.00 45.77  ?  725 HOH A O     1 
HETATM 2963 O  O     . HOH F 5 .   ? 5.667   18.386  -13.077 1.00 56.77  ?  726 HOH A O     1 
HETATM 2964 O  O     . HOH F 5 .   ? -14.047 22.253  -30.632 1.00 51.57  ?  727 HOH A O     1 
HETATM 2965 O  O     . HOH F 5 .   ? -0.168  -5.179  -21.071 1.00 55.40  ?  728 HOH A O     1 
HETATM 2966 O  O     . HOH F 5 .   ? 10.511  4.182   25.298  1.00 49.74  ?  729 HOH A O     1 
HETATM 2967 O  O     . HOH F 5 .   ? 10.541  5.851   16.507  1.00 39.40  ?  730 HOH A O     1 
HETATM 2968 O  O     . HOH F 5 .   ? -1.117  -5.878  21.118  1.00 34.94  ?  731 HOH A O     1 
HETATM 2969 O  O     . HOH F 5 .   ? -6.958  27.580  -11.608 1.00 51.91  ?  732 HOH A O     1 
HETATM 2970 O  O     . HOH F 5 .   ? 0.403   21.144  -14.579 1.00 26.16  ?  733 HOH A O     1 
HETATM 2971 O  O     . HOH F 5 .   ? -2.932  2.668   -26.258 1.00 37.59  ?  734 HOH A O     1 
HETATM 2972 O  O     . HOH F 5 .   ? -3.947  -12.008 -10.483 1.00 53.44  ?  735 HOH A O     1 
HETATM 2973 O  O     . HOH F 5 .   ? -21.331 18.499  -14.551 1.00 51.76  ?  736 HOH A O     1 
HETATM 2974 O  O     . HOH F 5 .   ? 3.938   8.853   -28.403 1.00 52.60  ?  737 HOH A O     1 
HETATM 2975 O  O     . HOH F 5 .   ? -0.256  11.528  -31.868 1.00 52.64  ?  738 HOH A O     1 
HETATM 2976 O  O     . HOH F 5 .   ? -7.070  6.862   -29.898 1.00 52.30  ?  739 HOH A O     1 
HETATM 2977 O  O     . HOH F 5 .   ? -6.617  -6.780  -25.154 1.00 44.05  ?  740 HOH A O     1 
HETATM 2978 O  O     . HOH F 5 .   ? -14.815 16.218  5.549   1.00 55.51  ?  741 HOH A O     1 
HETATM 2979 O  O     . HOH F 5 .   ? -5.986  12.457  -32.310 1.00 43.10  ?  742 HOH A O     1 
HETATM 2980 O  O     . HOH F 5 .   ? -8.740  11.605  -3.141  1.00 44.69  ?  743 HOH A O     1 
HETATM 2981 O  O     . HOH F 5 .   ? 1.830   18.506  -10.979 1.00 41.44  ?  744 HOH A O     1 
HETATM 2982 O  O     . HOH F 5 .   ? 8.322   11.477  -2.182  1.00 54.07  ?  745 HOH A O     1 
HETATM 2983 O  O     . HOH F 5 .   ? -21.114 11.491  -25.049 1.00 50.91  ?  746 HOH A O     1 
HETATM 2984 O  O     . HOH F 5 .   ? -15.063 -10.369 -4.996  1.00 61.86  ?  747 HOH A O     1 
HETATM 2985 O  O     . HOH F 5 .   ? -17.255 11.027  -33.296 1.00 58.16  ?  748 HOH A O     1 
HETATM 2986 O  O     . HOH F 5 .   ? 7.899   0.903   -16.979 1.00 31.27  ?  749 HOH A O     1 
HETATM 2987 O  O     . HOH F 5 .   ? 3.673   18.063  -12.191 1.00 41.09  ?  750 HOH A O     1 
HETATM 2988 O  O     . HOH F 5 .   ? 4.033   20.059  -18.069 1.00 49.61  ?  751 HOH A O     1 
HETATM 2989 O  O     . HOH F 5 .   ? 7.444   11.597  -10.454 1.00 27.95  ?  752 HOH A O     1 
HETATM 2990 O  O     . HOH F 5 .   ? -25.251 23.838  -21.227 1.00 49.50  ?  753 HOH A O     1 
HETATM 2991 O  O     . HOH F 5 .   ? -0.753  1.245   -26.951 1.00 52.57  ?  754 HOH A O     1 
HETATM 2992 O  O     . HOH F 5 .   ? -26.379 -10.516 -18.384 1.00 48.78  ?  755 HOH A O     1 
HETATM 2993 O  O     . HOH F 5 .   ? -0.359  -12.398 19.946  1.00 47.46  ?  756 HOH A O     1 
HETATM 2994 O  O     . HOH F 5 .   ? 4.463   -14.637 17.374  1.00 54.08  ?  757 HOH A O     1 
HETATM 2995 O  O     . HOH F 5 .   ? 8.293   15.655  13.704  1.00 43.97  ?  758 HOH A O     1 
HETATM 2996 O  O     . HOH F 5 .   ? 5.941   -14.149 3.080   1.00 47.18  ?  759 HOH A O     1 
HETATM 2997 O  O     . HOH F 5 .   ? 3.669   19.843  -21.420 1.00 38.90  ?  760 HOH A O     1 
HETATM 2998 O  O     . HOH F 5 .   ? 4.711   -1.536  -19.011 1.00 40.15  ?  761 HOH A O     1 
HETATM 2999 O  O     . HOH F 5 .   ? -20.669 -11.398 -7.773  1.00 49.99  ?  762 HOH A O     1 
HETATM 3000 O  O     . HOH F 5 .   ? -2.752  17.884  -32.042 1.00 48.19  ?  763 HOH A O     1 
HETATM 3001 O  O     . HOH F 5 .   ? 2.606   22.067  -39.471 1.00 46.74  ?  764 HOH A O     1 
HETATM 3002 O  O     . HOH F 5 .   ? -11.819 21.835  -4.918  1.00 51.04  ?  765 HOH A O     1 
HETATM 3003 O  O     . HOH F 5 .   ? -1.213  -3.503  -23.937 1.00 55.83  ?  766 HOH A O     1 
HETATM 3004 O  O     . HOH F 5 .   ? -23.189 -2.223  -8.331  1.00 51.48  ?  767 HOH A O     1 
HETATM 3005 O  O     . HOH F 5 .   ? 0.466   8.969   -30.496 1.00 46.72  ?  768 HOH A O     1 
HETATM 3006 O  O     . HOH F 5 .   ? -20.177 -0.894  -21.704 1.00 48.12  ?  769 HOH A O     1 
HETATM 3007 O  O     . HOH F 5 .   ? -21.797 -5.493  -2.763  1.00 43.54  ?  770 HOH A O     1 
HETATM 3008 O  O     . HOH F 5 .   ? 6.476   7.554   -24.677 1.00 37.29  ?  771 HOH A O     1 
HETATM 3009 O  O     . HOH F 5 .   ? 3.008   27.010  2.685   1.00 41.26  ?  772 HOH A O     1 
HETATM 3010 O  O     . HOH F 5 .   ? 3.656   21.189  -23.297 1.00 44.84  ?  773 HOH A O     1 
HETATM 3011 O  O     . HOH F 5 .   ? -26.304 -21.127 -18.105 1.00 38.60  ?  774 HOH A O     1 
HETATM 3012 O  O     . HOH F 5 .   ? 9.227   11.189  6.290   1.00 47.13  ?  775 HOH A O     1 
HETATM 3013 O  O     . HOH F 5 .   ? 5.222   -8.299  -13.437 1.00 36.12  ?  776 HOH A O     1 
HETATM 3014 O  O     . HOH F 5 .   ? -23.685 -8.058  -6.302  1.00 44.53  ?  777 HOH A O     1 
HETATM 3015 O  O     . HOH F 5 .   ? 9.742   28.267  -32.849 1.00 56.06  ?  778 HOH A O     1 
HETATM 3016 O  O     . HOH F 5 .   ? -8.271  3.943   -29.813 1.00 46.05  ?  779 HOH A O     1 
HETATM 3017 O  O     . HOH F 5 .   ? -18.986 17.465  -7.631  1.00 37.52  ?  780 HOH A O     1 
HETATM 3018 O  O     . HOH F 5 .   ? 2.625   17.203  17.241  1.00 44.38  ?  781 HOH A O     1 
HETATM 3019 O  O     . HOH F 5 .   ? -20.929 -5.435  -19.919 1.00 41.54  ?  782 HOH A O     1 
HETATM 3020 O  O     . HOH F 5 .   ? -2.084  -6.875  -17.377 1.00 37.69  ?  783 HOH A O     1 
HETATM 3021 O  O     . HOH F 5 .   ? -13.606 12.141  -34.673 1.00 41.71  ?  784 HOH A O     1 
HETATM 3022 O  O     . HOH F 5 .   ? 13.609  -0.605  3.611   1.00 52.95  ?  785 HOH A O     1 
HETATM 3023 O  O     . HOH F 5 .   ? -0.179  -6.853  -18.486 1.00 50.00  ?  786 HOH A O     1 
HETATM 3024 O  O     . HOH F 5 .   ? -2.565  25.307  -21.725 1.00 40.05  ?  787 HOH A O     1 
HETATM 3025 O  O     . HOH F 5 .   ? -30.250 -9.519  -21.075 1.00 49.22  ?  788 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   . MET A 1   ? 0.5918 0.7057 0.6354 -0.0746 -0.0436 0.0698  0   MET A N   
2    C CA  . MET A 1   ? 0.5974 0.7009 0.6442 -0.0741 -0.0480 0.0697  0   MET A CA  
3    C C   . MET A 1   ? 0.5532 0.6524 0.6022 -0.0692 -0.0441 0.0604  0   MET A C   
4    O O   . MET A 1   ? 0.5708 0.6755 0.6196 -0.0655 -0.0371 0.0533  0   MET A O   
5    C CB  . MET A 1   ? 0.6084 0.7149 0.6567 -0.0744 -0.0490 0.0719  0   MET A CB  
6    C CG  . MET A 1   ? 0.6773 0.7825 0.7249 -0.0801 -0.0563 0.0832  0   MET A CG  
7    S SD  . MET A 1   ? 0.7023 0.8120 0.7522 -0.0804 -0.0574 0.0860  0   MET A SD  
8    C CE  . MET A 1   ? 0.6326 0.7363 0.6877 -0.0745 -0.0556 0.0768  0   MET A CE  
9    N N   . MET A 2   ? 0.5147 0.6033 0.5658 -0.0692 -0.0494 0.0608  1   MET A N   
10   C CA  . MET A 2   ? 0.4933 0.5781 0.5466 -0.0651 -0.0467 0.0533  1   MET A CA  
11   C C   . MET A 2   ? 0.3966 0.4894 0.4529 -0.0606 -0.0397 0.0468  1   MET A C   
12   O O   . MET A 2   ? 0.3161 0.4131 0.3740 -0.0607 -0.0399 0.0487  1   MET A O   
13   C CB  . MET A 2   ? 0.5745 0.6459 0.6289 -0.0661 -0.0556 0.0555  1   MET A CB  
14   C CG  . MET A 2   ? 0.6671 0.7269 0.7181 -0.0690 -0.0622 0.0585  1   MET A CG  
15   S SD  . MET A 2   ? 0.7235 0.7791 0.7736 -0.0655 -0.0595 0.0507  1   MET A SD  
16   C CE  . MET A 2   ? 0.7224 0.7654 0.7738 -0.0629 -0.0676 0.0485  1   MET A CE  
17   N N   . ALA A 3   ? 0.4258 0.5198 0.4833 -0.0568 -0.0339 0.0396  2   ALA A N   
18   C CA  . ALA A 3   ? 0.4595 0.5589 0.5202 -0.0523 -0.0274 0.0334  2   ALA A CA  
19   C C   . ALA A 3   ? 0.4733 0.5717 0.5387 -0.0513 -0.0304 0.0344  2   ALA A C   
20   O O   . ALA A 3   ? 0.4073 0.4986 0.4737 -0.0528 -0.0374 0.0378  2   ALA A O   
21   C CB  . ALA A 3   ? 0.4756 0.5743 0.5371 -0.0488 -0.0218 0.0268  2   ALA A CB  
22   N N   . PRO A 4   ? 0.5919 0.6964 0.6606 -0.0483 -0.0260 0.0314  3   PRO A N   
23   C CA  . PRO A 4   ? 0.6275 0.7334 0.7019 -0.0470 -0.0288 0.0334  3   PRO A CA  
24   C C   . PRO A 4   ? 0.6145 0.7156 0.6934 -0.0457 -0.0338 0.0346  3   PRO A C   
25   O O   . PRO A 4   ? 0.7157 0.8110 0.7964 -0.0471 -0.0429 0.0400  3   PRO A O   
26   C CB  . PRO A 4   ? 0.6391 0.7511 0.7165 -0.0428 -0.0213 0.0276  3   PRO A CB  
27   C CG  . PRO A 4   ? 0.6132 0.7266 0.6854 -0.0436 -0.0178 0.0254  3   PRO A CG  
28   C CD  . PRO A 4   ? 0.6012 0.7106 0.6686 -0.0461 -0.0195 0.0268  3   PRO A CD  
29   N N   . VAL A 5   ? 0.3467 0.4489 0.4277 -0.0426 -0.0292 0.0300  4   VAL A N   
30   C CA  . VAL A 5   ? 0.2260 0.3189 0.3068 -0.0373 -0.0320 0.0292  4   VAL A CA  
31   C C   . VAL A 5   ? 0.1523 0.2341 0.2255 -0.0379 -0.0337 0.0274  4   VAL A C   
32   O O   . VAL A 5   ? 0.1867 0.2570 0.2535 -0.0305 -0.0312 0.0231  4   VAL A O   
33   C CB  . VAL A 5   ? 0.2629 0.3605 0.3473 -0.0294 -0.0229 0.0246  4   VAL A CB  
34   C CG1 . VAL A 5   ? 0.2693 0.3767 0.3614 -0.0285 -0.0222 0.0268  4   VAL A CG1 
35   C CG2 . VAL A 5   ? 0.3207 0.4307 0.4100 -0.0317 -0.0153 0.0211  4   VAL A CG2 
36   N N   . GLN A 6   ? 0.1331 0.2192 0.2069 -0.0466 -0.0381 0.0309  5   GLN A N   
37   C CA  . GLN A 6   ? 0.1535 0.2314 0.2217 -0.0481 -0.0400 0.0296  5   GLN A CA  
38   C C   . GLN A 6   ? 0.1509 0.2051 0.2081 -0.0430 -0.0472 0.0290  5   GLN A C   
39   O O   . GLN A 6   ? 0.1680 0.2119 0.2183 -0.0389 -0.0460 0.0250  5   GLN A O   
40   C CB  . GLN A 6   ? 0.1692 0.2469 0.2322 -0.0518 -0.0389 0.0314  5   GLN A CB  
41   C CG  . GLN A 6   ? 0.1954 0.2664 0.2539 -0.0534 -0.0406 0.0309  5   GLN A CG  
42   C CD  . GLN A 6   ? 0.1671 0.2435 0.2273 -0.0501 -0.0326 0.0250  5   GLN A CD  
43   O OE1 . GLN A 6   ? 0.1712 0.2556 0.2356 -0.0465 -0.0251 0.0212  5   GLN A OE1 
44   N NE2 . GLN A 6   ? 0.1167 0.1878 0.1737 -0.0512 -0.0343 0.0245  5   GLN A NE2 
45   N N   . LYS A 7   ? 0.1945 0.2391 0.2495 -0.0432 -0.0551 0.0328  6   LYS A N   
46   C CA  . LYS A 7   ? 0.2302 0.2506 0.2743 -0.0381 -0.0630 0.0316  6   LYS A CA  
47   C C   . LYS A 7   ? 0.2049 0.2158 0.2420 -0.0261 -0.0570 0.0244  6   LYS A C   
48   O O   . LYS A 7   ? 0.1790 0.1740 0.2058 -0.0216 -0.0594 0.0207  6   LYS A O   
49   C CB  . LYS A 7   ? 0.2786 0.2907 0.3228 -0.0394 -0.0721 0.0366  6   LYS A CB  
50   C CG  . LYS A 7   ? 0.3448 0.3302 0.3775 -0.0328 -0.0808 0.0344  6   LYS A CG  
51   C CD  . LYS A 7   ? 0.4297 0.4068 0.4638 -0.0344 -0.0903 0.0399  6   LYS A CD  
52   C CE  . LYS A 7   ? 0.5606 0.5093 0.5830 -0.0276 -0.1002 0.0372  6   LYS A CE  
53   N NZ  . LYS A 7   ? 0.6188 0.5591 0.6360 -0.0138 -0.0953 0.0307  6   LYS A NZ  
54   N N   . GLN A 8   ? 0.1790 0.2004 0.2219 -0.0208 -0.0489 0.0226  7   GLN A N   
55   C CA  . GLN A 8   ? 0.1712 0.1862 0.2088 -0.0091 -0.0425 0.0169  7   GLN A CA  
56   C C   . GLN A 8   ? 0.1848 0.2047 0.2210 -0.0079 -0.0348 0.0130  7   GLN A C   
57   O O   . GLN A 8   ? 0.1997 0.2082 0.2266 0.0005  -0.0327 0.0087  7   GLN A O   
58   C CB  . GLN A 8   ? 0.1734 0.1998 0.2194 -0.0045 -0.0364 0.0173  7   GLN A CB  
59   C CG  . GLN A 8   ? 0.2138 0.2312 0.2591 -0.0020 -0.0437 0.0202  7   GLN A CG  
60   C CD  . GLN A 8   ? 0.2381 0.2596 0.2884 -0.0130 -0.0520 0.0268  7   GLN A CD  
61   O OE1 . GLN A 8   ? 0.2955 0.3022 0.3411 -0.0137 -0.0621 0.0297  7   GLN A OE1 
62   N NE2 . GLN A 8   ? 0.1794 0.2209 0.2391 -0.0214 -0.0480 0.0294  7   GLN A NE2 
63   N N   . PHE A 9   ? 0.1877 0.2242 0.2325 -0.0157 -0.0308 0.0145  8   PHE A N   
64   C CA  . PHE A 9   ? 0.1363 0.1756 0.1796 -0.0151 -0.0251 0.0113  8   PHE A CA  
65   C C   . PHE A 9   ? 0.1512 0.1737 0.1830 -0.0155 -0.0319 0.0104  8   PHE A C   
66   O O   . PHE A 9   ? 0.1885 0.2038 0.2130 -0.0097 -0.0288 0.0066  8   PHE A O   
67   C CB  . PHE A 9   ? 0.1769 0.2358 0.2314 -0.0234 -0.0206 0.0127  8   PHE A CB  
68   C CG  . PHE A 9   ? 0.1723 0.2459 0.2358 -0.0205 -0.0108 0.0106  8   PHE A CG  
69   C CD1 . PHE A 9   ? 0.1645 0.2375 0.2265 -0.0147 -0.0037 0.0071  8   PHE A CD1 
70   C CD2 . PHE A 9   ? 0.1216 0.2095 0.1951 -0.0239 -0.0091 0.0125  8   PHE A CD2 
71   C CE1 . PHE A 9   ? 0.1626 0.2488 0.2340 -0.0127 0.0048  0.0059  8   PHE A CE1 
72   C CE2 . PHE A 9   ? 0.1570 0.2578 0.2393 -0.0217 -0.0009 0.0106  8   PHE A CE2 
73   C CZ  . PHE A 9   ? 0.1347 0.2345 0.2164 -0.0163 0.0059  0.0075  8   PHE A CZ  
74   N N   . ARG A 10  ? 0.1380 0.1545 0.1685 -0.0226 -0.0418 0.0143  9   ARG A N   
75   C CA  . ARG A 10  ? 0.1940 0.1942 0.2143 -0.0238 -0.0495 0.0138  9   ARG A CA  
76   C C   . ARG A 10  ? 0.1592 0.1375 0.1656 -0.0136 -0.0532 0.0096  9   ARG A C   
77   O O   . ARG A 10  ? 0.2592 0.2255 0.2552 -0.0101 -0.0548 0.0062  9   ARG A O   
78   C CB  . ARG A 10  ? 0.2425 0.2420 0.2658 -0.0342 -0.0597 0.0200  9   ARG A CB  
79   C CG  . ARG A 10  ? 0.2059 0.2272 0.2414 -0.0440 -0.0563 0.0240  9   ARG A CG  
80   C CD  . ARG A 10  ? 0.1617 0.1885 0.1975 -0.0447 -0.0513 0.0214  9   ARG A CD  
81   N NE  . ARG A 10  ? 0.2370 0.2475 0.2633 -0.0453 -0.0590 0.0212  9   ARG A NE  
82   C CZ  . ARG A 10  ? 0.2915 0.3039 0.3205 -0.0541 -0.0658 0.0259  9   ARG A CZ  
83   N NH1 . ARG A 10  ? 0.2883 0.3158 0.3252 -0.0585 -0.0612 0.0302  9   ARG A NH1 
84   N NH2 . ARG A 10  ? 0.2950 0.2918 0.3153 -0.0544 -0.0732 0.0255  9   ARG A NH2 
85   N N   . GLU A 11  ? 0.1759 0.1487 0.1815 -0.0083 -0.0547 0.0095  10  GLU A N   
86   C CA  . GLU A 11  ? 0.2235 0.1766 0.2159 0.0031  -0.0570 0.0046  10  GLU A CA  
87   C C   . GLU A 11  ? 0.2522 0.2089 0.2405 0.0128  -0.0461 -0.0006 10  GLU A C   
88   O O   . GLU A 11  ? 0.2369 0.1785 0.2116 0.0201  -0.0474 -0.0051 10  GLU A O   
89   C CB  . GLU A 11  ? 0.2249 0.1740 0.2196 0.0070  -0.0600 0.0060  10  GLU A CB  
90   C CG  . GLU A 11  ? 0.2520 0.1947 0.2494 -0.0020 -0.0722 0.0118  10  GLU A CG  
91   C CD  . GLU A 11  ? 0.3303 0.2700 0.3310 0.0016  -0.0753 0.0139  10  GLU A CD  
92   O OE1 . GLU A 11  ? 0.4295 0.3569 0.4287 -0.0025 -0.0867 0.0176  10  GLU A OE1 
93   O OE2 . GLU A 11  ? 0.3585 0.3083 0.3641 0.0082  -0.0666 0.0123  10  GLU A OE2 
94   N N   . PHE A 12  ? 0.2089 0.1853 0.2086 0.0129  -0.0355 0.0003  11  PHE A N   
95   C CA  . PHE A 12  ? 0.1992 0.1823 0.1978 0.0200  -0.0248 -0.0030 11  PHE A CA  
96   C C   . PHE A 12  ? 0.2111 0.1900 0.2029 0.0180  -0.0250 -0.0047 11  PHE A C   
97   O O   . PHE A 12  ? 0.2349 0.2053 0.2157 0.0263  -0.0222 -0.0084 11  PHE A O   
98   C CB  . PHE A 12  ? 0.1816 0.1877 0.1963 0.0167  -0.0156 -0.0006 11  PHE A CB  
99   C CG  . PHE A 12  ? 0.2010 0.2163 0.2177 0.0223  -0.0047 -0.0026 11  PHE A CG  
100  C CD1 . PHE A 12  ? 0.2242 0.2325 0.2324 0.0341  -0.0004 -0.0054 11  PHE A CD1 
101  C CD2 . PHE A 12  ? 0.1830 0.2148 0.2109 0.0160  0.0013  -0.0012 11  PHE A CD2 
102  C CE1 . PHE A 12  ? 0.2382 0.2564 0.2492 0.0388  0.0098  -0.0060 11  PHE A CE1 
103  C CE2 . PHE A 12  ? 0.1523 0.1925 0.1833 0.0206  0.0108  -0.0022 11  PHE A CE2 
104  C CZ  . PHE A 12  ? 0.1434 0.1772 0.1662 0.0317  0.0151  -0.0040 11  PHE A CZ  
105  N N   . HIS A 13  ? 0.1720 0.1575 0.1700 0.0071  -0.0283 -0.0017 12  HIS A N   
106  C CA  . HIS A 13  ? 0.1927 0.1752 0.1856 0.0047  -0.0290 -0.0027 12  HIS A CA  
107  C C   . HIS A 13  ? 0.2002 0.1597 0.1762 0.0088  -0.0380 -0.0055 12  HIS A C   
108  O O   . HIS A 13  ? 0.2107 0.1637 0.1771 0.0135  -0.0362 -0.0085 12  HIS A O   
109  C CB  . HIS A 13  ? 0.1717 0.1654 0.1749 -0.0074 -0.0319 0.0013  12  HIS A CB  
110  C CG  . HIS A 13  ? 0.2153 0.2062 0.2143 -0.0101 -0.0333 0.0008  12  HIS A CG  
111  N ND1 . HIS A 13  ? 0.2060 0.1851 0.1987 -0.0153 -0.0437 0.0023  12  HIS A ND1 
112  C CD2 . HIS A 13  ? 0.1758 0.1735 0.1760 -0.0082 -0.0259 -0.0008 12  HIS A CD2 
113  C CE1 . HIS A 13  ? 0.1835 0.1631 0.1739 -0.0163 -0.0427 0.0016  12  HIS A CE1 
114  N NE2 . HIS A 13  ? 0.1856 0.1760 0.1802 -0.0120 -0.0319 -0.0003 12  HIS A NE2 
115  N N   . ASP A 14  ? 0.2219 0.1685 0.1939 0.0069  -0.0483 -0.0043 13  ASP A N   
116  C CA  . ASP A 14  ? 0.2763 0.1989 0.2319 0.0114  -0.0581 -0.0076 13  ASP A CA  
117  C C   . ASP A 14  ? 0.2932 0.2066 0.2360 0.0253  -0.0528 -0.0137 13  ASP A C   
118  O O   . ASP A 14  ? 0.2921 0.1900 0.2199 0.0301  -0.0568 -0.0176 13  ASP A O   
119  C CB  . ASP A 14  ? 0.3025 0.2130 0.2576 0.0085  -0.0693 -0.0053 13  ASP A CB  
120  C CG  . ASP A 14  ? 0.3576 0.2732 0.3218 -0.0052 -0.0772 0.0011  13  ASP A CG  
121  O OD1 . ASP A 14  ? 0.3353 0.2579 0.3023 -0.0116 -0.0766 0.0027  13  ASP A OD1 
122  O OD2 . ASP A 14  ? 0.4167 0.3297 0.3855 -0.0095 -0.0841 0.0050  13  ASP A OD2 
123  N N   . ARG A 15  ? 0.2853 0.2086 0.2336 0.0320  -0.0438 -0.0142 14  ARG A N   
124  C CA  . ARG A 15  ? 0.2600 0.1761 0.1968 0.0459  -0.0383 -0.0193 14  ARG A CA  
125  C C   . ARG A 15  ? 0.2756 0.2017 0.2108 0.0497  -0.0278 -0.0205 14  ARG A C   
126  O O   . ARG A 15  ? 0.2940 0.2112 0.2154 0.0605  -0.0252 -0.0249 14  ARG A O   
127  C CB  . ARG A 15  ? 0.2973 0.2205 0.2416 0.0518  -0.0332 -0.0187 14  ARG A CB  
128  C CG  . ARG A 15  ? 0.2961 0.2040 0.2371 0.0523  -0.0440 -0.0188 14  ARG A CG  
129  C CD  . ARG A 15  ? 0.3001 0.2204 0.2549 0.0521  -0.0407 -0.0154 14  ARG A CD  
130  N NE  . ARG A 15  ? 0.3809 0.2838 0.3304 0.0552  -0.0509 -0.0161 14  ARG A NE  
131  C CZ  . ARG A 15  ? 0.4218 0.3151 0.3722 0.0460  -0.0629 -0.0129 14  ARG A CZ  
132  N NH1 . ARG A 15  ? 0.4103 0.3112 0.3669 0.0334  -0.0655 -0.0088 14  ARG A NH1 
133  N NH2 . ARG A 15  ? 0.4275 0.3039 0.3732 0.0495  -0.0724 -0.0135 14  ARG A NH2 
134  N N   . ILE A 16  ? 0.2191 0.1636 0.1680 0.0415  -0.0218 -0.0167 15  ILE A N   
135  C CA  . ILE A 16  ? 0.2404 0.1949 0.1895 0.0448  -0.0119 -0.0171 15  ILE A CA  
136  C C   . ILE A 16  ? 0.2661 0.2160 0.2095 0.0397  -0.0157 -0.0171 15  ILE A C   
137  O O   . ILE A 16  ? 0.2447 0.1976 0.1834 0.0441  -0.0094 -0.0179 15  ILE A O   
138  C CB  . ILE A 16  ? 0.2247 0.2025 0.1928 0.0407  -0.0020 -0.0133 15  ILE A CB  
139  C CG1 . ILE A 16  ? 0.1574 0.1445 0.1380 0.0276  -0.0054 -0.0100 15  ILE A CG1 
140  C CG2 . ILE A 16  ? 0.2028 0.1865 0.1778 0.0453  0.0015  -0.0127 15  ILE A CG2 
141  C CD1 . ILE A 16  ? 0.1593 0.1681 0.1577 0.0233  0.0035  -0.0072 15  ILE A CD1 
142  N N   . LYS A 17  ? 0.2643 0.2085 0.2090 0.0303  -0.0255 -0.0155 16  LYS A N   
143  C CA  . LYS A 17  ? 0.2981 0.2405 0.2399 0.0247  -0.0289 -0.0147 16  LYS A CA  
144  C C   . LYS A 17  ? 0.3259 0.2497 0.2474 0.0326  -0.0330 -0.0191 16  LYS A C   
145  O O   . LYS A 17  ? 0.3352 0.2423 0.2436 0.0394  -0.0388 -0.0229 16  LYS A O   
146  C CB  . LYS A 17  ? 0.3361 0.2774 0.2845 0.0129  -0.0388 -0.0113 16  LYS A CB  
147  C CG  . LYS A 17  ? 0.4436 0.3651 0.3820 0.0127  -0.0514 -0.0124 16  LYS A CG  
148  C CD  . LYS A 17  ? 0.5279 0.4520 0.4753 0.0000  -0.0603 -0.0074 16  LYS A CD  
149  C CE  . LYS A 17  ? 0.5863 0.4902 0.5250 -0.0012 -0.0740 -0.0075 16  LYS A CE  
150  N NZ  . LYS A 17  ? 0.5916 0.5008 0.5413 -0.0141 -0.0820 -0.0011 16  LYS A NZ  
151  N N   . LEU A 18  ? 0.3199 0.2469 0.2386 0.0322  -0.0300 -0.0188 17  LEU A N   
152  C CA  . LEU A 18  ? 0.3764 0.2869 0.2758 0.0378  -0.0350 -0.0224 17  LEU A CA  
153  C C   . LEU A 18  ? 0.3607 0.2686 0.2617 0.0278  -0.0435 -0.0200 17  LEU A C   
154  O O   . LEU A 18  ? 0.3410 0.2647 0.2564 0.0204  -0.0392 -0.0159 17  LEU A O   
155  C CB  . LEU A 18  ? 0.3973 0.3142 0.2910 0.0466  -0.0242 -0.0234 17  LEU A CB  
156  C CG  . LEU A 18  ? 0.4033 0.3055 0.2763 0.0529  -0.0280 -0.0268 17  LEU A CG  
157  C CD1 . LEU A 18  ? 0.3861 0.2664 0.2399 0.0612  -0.0362 -0.0329 17  LEU A CD1 
158  C CD2 . LEU A 18  ? 0.4106 0.3237 0.2815 0.0605  -0.0159 -0.0260 17  LEU A CD2 
159  N N   . ALA A 19  ? 0.3496 0.2376 0.2364 0.0276  -0.0557 -0.0225 18  ALA A N   
160  C CA  . ALA A 19  ? 0.3693 0.2544 0.2584 0.0176  -0.0651 -0.0196 18  ALA A CA  
161  C C   . ALA A 19  ? 0.3773 0.2695 0.2651 0.0177  -0.0602 -0.0185 18  ALA A C   
162  O O   . ALA A 19  ? 0.3717 0.2600 0.2469 0.0270  -0.0551 -0.0216 18  ALA A O   
163  C CB  . ALA A 19  ? 0.4075 0.2681 0.2805 0.0180  -0.0799 -0.0227 18  ALA A CB  
164  N N   . GLN A 20  ? 0.3737 0.2771 0.2750 0.0076  -0.0617 -0.0137 19  GLN A N   
165  C CA  . GLN A 20  ? 0.3515 0.2628 0.2546 0.0066  -0.0576 -0.0118 19  GLN A CA  
166  C C   . GLN A 20  ? 0.3774 0.2708 0.2611 0.0098  -0.0665 -0.0144 19  GLN A C   
167  O O   . GLN A 20  ? 0.3973 0.2717 0.2672 0.0115  -0.0770 -0.0177 19  GLN A O   
168  C CB  . GLN A 20  ? 0.3233 0.2499 0.2454 -0.0047 -0.0583 -0.0063 19  GLN A CB  
169  C CG  . GLN A 20  ? 0.3756 0.2937 0.2981 -0.0133 -0.0719 -0.0041 19  GLN A CG  
170  C CD  . GLN A 20  ? 0.3588 0.2938 0.3002 -0.0238 -0.0720 0.0016  19  GLN A CD  
171  O OE1 . GLN A 20  ? 0.3497 0.2956 0.2978 -0.0248 -0.0668 0.0033  19  GLN A OE1 
172  N NE2 . GLN A 20  ? 0.3873 0.3249 0.3375 -0.0315 -0.0781 0.0047  19  GLN A NE2 
173  N N   . TYR A 21  ? 0.3465 0.2457 0.2294 0.0104  -0.0627 -0.0128 20  TYR A N   
174  C CA  . TYR A 21  ? 0.4042 0.2884 0.2688 0.0135  -0.0703 -0.0149 20  TYR A CA  
175  C C   . TYR A 21  ? 0.4310 0.3005 0.2909 0.0063  -0.0862 -0.0148 20  TYR A C   
176  O O   . TYR A 21  ? 0.4585 0.3076 0.2991 0.0109  -0.0953 -0.0194 20  TYR A O   
177  C CB  . TYR A 21  ? 0.3568 0.2525 0.2267 0.0118  -0.0652 -0.0111 20  TYR A CB  
178  C CG  . TYR A 21  ? 0.3657 0.2694 0.2322 0.0207  -0.0523 -0.0115 20  TYR A CG  
179  C CD1 . TYR A 21  ? 0.3607 0.2533 0.2071 0.0319  -0.0503 -0.0161 20  TYR A CD1 
180  C CD2 . TYR A 21  ? 0.3471 0.2699 0.2309 0.0179  -0.0424 -0.0069 20  TYR A CD2 
181  C CE1 . TYR A 21  ? 0.3980 0.2995 0.2420 0.0397  -0.0384 -0.0153 20  TYR A CE1 
182  C CE2 . TYR A 21  ? 0.3619 0.2923 0.2439 0.0252  -0.0312 -0.0061 20  TYR A CE2 
183  C CZ  . TYR A 21  ? 0.3844 0.3050 0.2468 0.0359  -0.0290 -0.0098 20  TYR A CZ  
184  O OH  . TYR A 21  ? 0.3479 0.2777 0.2092 0.0429  -0.0176 -0.0079 20  TYR A OH  
185  N N   . ASP A 22  ? 0.4566 0.3365 0.3344 -0.0050 -0.0899 -0.0094 21  ASP A N   
186  C CA  . ASP A 22  ? 0.5198 0.3887 0.3964 -0.0132 -0.1050 -0.0075 21  ASP A CA  
187  C C   . ASP A 22  ? 0.5247 0.3777 0.3943 -0.0129 -0.1137 -0.0103 21  ASP A C   
188  O O   . ASP A 22  ? 0.5034 0.3457 0.3727 -0.0181 -0.1241 -0.0083 21  ASP A O   
189  C CB  . ASP A 22  ? 0.5739 0.4611 0.4730 -0.0249 -0.1052 -0.0004 21  ASP A CB  
190  C CG  . ASP A 22  ? 0.6485 0.5475 0.5537 -0.0264 -0.1009 0.0027  21  ASP A CG  
191  O OD1 . ASP A 22  ? 0.6826 0.5743 0.5737 -0.0194 -0.0992 -0.0001 21  ASP A OD1 
192  O OD2 . ASP A 22  ? 0.6712 0.5869 0.5952 -0.0342 -0.0991 0.0080  21  ASP A OD2 
193  N N   . GLU A 23  ? 0.4985 0.3523 0.3673 -0.0064 -0.1062 -0.0134 22  GLU A N   
194  C CA  . GLU A 23  ? 0.5162 0.3546 0.3785 -0.0050 -0.1141 -0.0162 22  GLU A CA  
195  C C   . GLU A 23  ? 0.5212 0.3451 0.3640 0.0087  -0.1110 -0.0239 22  GLU A C   
196  O O   . GLU A 23  ? 0.5767 0.3901 0.4155 0.0120  -0.1146 -0.0267 22  GLU A O   
197  C CB  . GLU A 23  ? 0.4883 0.3413 0.3696 -0.0106 -0.1094 -0.0121 22  GLU A CB  
198  C CG  . GLU A 23  ? 0.5158 0.3876 0.4179 -0.0229 -0.1094 -0.0045 22  GLU A CG  
199  C CD  . GLU A 23  ? 0.5395 0.4241 0.4574 -0.0277 -0.1058 -0.0010 22  GLU A CD  
200  O OE1 . GLU A 23  ? 0.5932 0.4661 0.5085 -0.0297 -0.1146 -0.0006 22  GLU A OE1 
201  O OE2 . GLU A 23  ? 0.5373 0.4429 0.4698 -0.0294 -0.0946 0.0014  22  GLU A OE2 
202  N N   . ASN A 24  ? 0.5179 0.3420 0.3490 0.0171  -0.1042 -0.0270 23  ASN A N   
203  C CA  . ASN A 24  ? 0.5341 0.3493 0.3481 0.0312  -0.0984 -0.0337 23  ASN A CA  
204  C C   . ASN A 24  ? 0.5346 0.3362 0.3268 0.0377  -0.1027 -0.0380 23  ASN A C   
205  O O   . ASN A 24  ? 0.5299 0.3426 0.3221 0.0396  -0.0946 -0.0361 23  ASN A O   
206  C CB  . ASN A 24  ? 0.5141 0.3501 0.3392 0.0360  -0.0813 -0.0320 23  ASN A CB  
207  C CG  . ASN A 24  ? 0.5008 0.3304 0.3129 0.0497  -0.0750 -0.0377 23  ASN A CG  
208  O OD1 . ASN A 24  ? 0.5679 0.3798 0.3581 0.0587  -0.0799 -0.0438 23  ASN A OD1 
209  N ND2 . ASN A 24  ? 0.4474 0.2919 0.2728 0.0515  -0.0643 -0.0360 23  ASN A ND2 
210  N N   . GLN A 25  ? 0.5687 0.3480 0.3453 0.0412  -0.1140 -0.0426 24  GLN A N   
211  C CA  . GLN A 25  ? 0.5941 0.3636 0.3558 0.0467  -0.1166 -0.0449 24  GLN A CA  
212  C C   . GLN A 25  ? 0.5820 0.3535 0.3281 0.0609  -0.1054 -0.0497 24  GLN A C   
213  O O   . GLN A 25  ? 0.6185 0.3917 0.3557 0.0642  -0.1028 -0.0496 24  GLN A O   
214  C CB  . GLN A 25  ? 0.7046 0.4532 0.4596 0.0468  -0.1294 -0.0467 24  GLN A CB  
215  C CG  . GLN A 25  ? 0.8258 0.5649 0.5703 0.0472  -0.1357 -0.0471 24  GLN A CG  
216  C CD  . GLN A 25  ? 0.9143 0.6417 0.6653 0.0377  -0.1495 -0.0435 24  GLN A CD  
217  O OE1 . GLN A 25  ? 0.9656 0.6953 0.7215 0.0300  -0.1538 -0.0393 24  GLN A OE1 
218  N NE2 . GLN A 25  ? 0.9241 0.6393 0.6755 0.0382  -0.1566 -0.0444 24  GLN A NE2 
219  N N   . THR A 26  ? 0.5662 0.3393 0.3103 0.0694  -0.0981 -0.0531 25  THR A N   
220  C CA  . THR A 26  ? 0.5806 0.3594 0.3134 0.0830  -0.0857 -0.0562 25  THR A CA  
221  C C   . THR A 26  ? 0.5668 0.3648 0.3040 0.0820  -0.0742 -0.0520 25  THR A C   
222  O O   . THR A 26  ? 0.6105 0.4124 0.3381 0.0890  -0.0679 -0.0519 25  THR A O   
223  C CB  . THR A 26  ? 0.6239 0.4040 0.3584 0.0910  -0.0793 -0.0591 25  THR A CB  
224  O OG1 . THR A 26  ? 0.6544 0.4167 0.3864 0.0906  -0.0911 -0.0620 25  THR A OG1 
225  C CG2 . THR A 26  ? 0.6294 0.4158 0.3538 0.1053  -0.0673 -0.0612 25  THR A CG2 
226  N N   . LEU A 27  ? 0.5534 0.3696 0.3159 0.0717  -0.0692 -0.0452 26  LEU A N   
227  C CA  . LEU A 27  ? 0.4911 0.3290 0.2668 0.0688  -0.0576 -0.0388 26  LEU A CA  
228  C C   . LEU A 27  ? 0.4865 0.3214 0.2558 0.0644  -0.0635 -0.0367 26  LEU A C   
229  O O   . LEU A 27  ? 0.4756 0.3191 0.2407 0.0687  -0.0557 -0.0345 26  LEU A O   
230  C CB  . LEU A 27  ? 0.4129 0.2692 0.2165 0.0586  -0.0525 -0.0328 26  LEU A CB  
231  C CG  . LEU A 27  ? 0.4607 0.3254 0.2735 0.0630  -0.0436 -0.0334 26  LEU A CG  
232  C CD1 . LEU A 27  ? 0.4062 0.2891 0.2454 0.0525  -0.0393 -0.0276 26  LEU A CD1 
233  C CD2 . LEU A 27  ? 0.4390 0.3122 0.2451 0.0748  -0.0305 -0.0340 26  LEU A CD2 
234  N N   . ARG A 28  ? 0.4781 0.3012 0.2470 0.0556  -0.0777 -0.0368 27  ARG A N   
235  C CA  . ARG A 28  ? 0.5237 0.3431 0.2863 0.0513  -0.0847 -0.0347 27  ARG A CA  
236  C C   . ARG A 28  ? 0.5434 0.3505 0.2805 0.0625  -0.0854 -0.0397 27  ARG A C   
237  O O   . ARG A 28  ? 0.5922 0.4054 0.3250 0.0635  -0.0822 -0.0369 27  ARG A O   
238  C CB  . ARG A 28  ? 0.5061 0.3141 0.2724 0.0403  -0.1008 -0.0340 27  ARG A CB  
239  C CG  . ARG A 28  ? 0.4931 0.3167 0.2868 0.0282  -0.0996 -0.0275 27  ARG A CG  
240  C CD  . ARG A 28  ? 0.4458 0.2633 0.2458 0.0165  -0.1138 -0.0243 27  ARG A CD  
241  N NE  . ARG A 28  ? 0.4765 0.2747 0.2692 0.0176  -0.1233 -0.0275 27  ARG A NE  
242  C CZ  . ARG A 28  ? 0.5327 0.3250 0.3317 0.0147  -0.1278 -0.0277 27  ARG A CZ  
243  N NH1 . ARG A 28  ? 0.4745 0.2796 0.2876 0.0103  -0.1234 -0.0252 27  ARG A NH1 
244  N NH2 . ARG A 28  ? 0.5741 0.3477 0.3652 0.0163  -0.1371 -0.0299 27  ARG A NH2 
245  N N   . ASP A 29  ? 0.5700 0.3633 0.2959 0.0706  -0.0877 -0.0457 28  ASP A N   
246  C CA  . ASP A 29  ? 0.6019 0.3863 0.3096 0.0808  -0.0872 -0.0494 28  ASP A CA  
247  C C   . ASP A 29  ? 0.6034 0.4023 0.3059 0.0905  -0.0721 -0.0483 28  ASP A C   
248  O O   . ASP A 29  ? 0.6117 0.4121 0.3045 0.0943  -0.0700 -0.0474 28  ASP A O   
249  C CB  . ASP A 29  ? 0.6729 0.4395 0.3708 0.0876  -0.0935 -0.0557 28  ASP A CB  
250  C CG  . ASP A 29  ? 0.6935 0.4440 0.3946 0.0787  -0.1092 -0.0560 28  ASP A CG  
251  O OD1 . ASP A 29  ? 0.6720 0.4253 0.3820 0.0677  -0.1151 -0.0514 28  ASP A OD1 
252  O OD2 . ASP A 29  ? 0.7216 0.4577 0.4176 0.0826  -0.1156 -0.0600 28  ASP A OD2 
253  N N   . GLU A 30  ? 0.6142 0.4251 0.3245 0.0943  -0.0612 -0.0475 29  GLU A N   
254  C CA  . GLU A 30  ? 0.6358 0.4631 0.3451 0.1025  -0.0460 -0.0446 29  GLU A CA  
255  C C   . GLU A 30  ? 0.6087 0.4498 0.3243 0.0965  -0.0417 -0.0376 29  GLU A C   
256  O O   . GLU A 30  ? 0.6162 0.4642 0.3254 0.1015  -0.0353 -0.0349 29  GLU A O   
257  C CB  . GLU A 30  ? 0.6304 0.4685 0.3501 0.1067  -0.0355 -0.0445 29  GLU A CB  
258  C CG  . GLU A 30  ? 0.7018 0.5279 0.4150 0.1144  -0.0385 -0.0506 29  GLU A CG  
259  C CD  . GLU A 30  ? 0.7500 0.5840 0.4765 0.1150  -0.0323 -0.0505 29  GLU A CD  
260  O OE1 . GLU A 30  ? 0.7718 0.6036 0.4955 0.1238  -0.0295 -0.0534 29  GLU A OE1 
261  O OE2 . GLU A 30  ? 0.7461 0.5899 0.4883 0.1060  -0.0304 -0.0467 29  GLU A OE2 
262  N N   . ARG A 31  ? 0.5958 0.4439 0.3313 0.0841  -0.0446 -0.0331 30  ARG A N   
263  C CA  . ARG A 31  ? 0.5619 0.4245 0.3114 0.0765  -0.0412 -0.0254 30  ARG A CA  
264  C C   . ARG A 31  ? 0.5691 0.4212 0.3003 0.0772  -0.0496 -0.0257 30  ARG A C   
265  O O   . ARG A 31  ? 0.5301 0.3916 0.2589 0.0797  -0.0431 -0.0211 30  ARG A O   
266  C CB  . ARG A 31  ? 0.5563 0.4263 0.3310 0.0630  -0.0451 -0.0215 30  ARG A CB  
267  C CG  . ARG A 31  ? 0.5212 0.4013 0.3086 0.0543  -0.0459 -0.0147 30  ARG A CG  
268  C CD  . ARG A 31  ? 0.4973 0.3787 0.3024 0.0419  -0.0542 -0.0128 30  ARG A CD  
269  N NE  . ARG A 31  ? 0.5349 0.3969 0.3262 0.0393  -0.0697 -0.0167 30  ARG A NE  
270  C CZ  . ARG A 31  ? 0.5210 0.3800 0.3233 0.0295  -0.0791 -0.0159 30  ARG A CZ  
271  N NH1 . ARG A 31  ? 0.4801 0.3547 0.3066 0.0221  -0.0743 -0.0118 30  ARG A NH1 
272  N NH2 . ARG A 31  ? 0.5264 0.3670 0.3154 0.0273  -0.0938 -0.0190 30  ARG A NH2 
273  N N   . ASP A 32  ? 0.5938 0.4267 0.3132 0.0746  -0.0643 -0.0307 31  ASP A N   
274  C CA  . ASP A 32  ? 0.6448 0.4700 0.3553 0.0728  -0.0722 -0.0303 31  ASP A CA  
275  C C   . ASP A 32  ? 0.6560 0.4786 0.3488 0.0846  -0.0667 -0.0331 31  ASP A C   
276  O O   . ASP A 32  ? 0.6661 0.4905 0.3523 0.0847  -0.0674 -0.0304 31  ASP A O   
277  C CB  . ASP A 32  ? 0.6798 0.4882 0.3907 0.0660  -0.0875 -0.0338 31  ASP A CB  
278  C CG  . ASP A 32  ? 0.6978 0.5113 0.4283 0.0528  -0.0936 -0.0293 31  ASP A CG  
279  O OD1 . ASP A 32  ? 0.6817 0.5108 0.4237 0.0485  -0.0880 -0.0233 31  ASP A OD1 
280  O OD2 . ASP A 32  ? 0.6932 0.4958 0.4285 0.0469  -0.1039 -0.0312 31  ASP A OD2 
281  N N   . ALA A 33  ? 0.6568 0.4757 0.3423 0.0945  -0.0614 -0.0382 32  ALA A N   
282  C CA  . ALA A 33  ? 0.6660 0.4860 0.3367 0.1061  -0.0546 -0.0400 32  ALA A CA  
283  C C   . ALA A 33  ? 0.6830 0.5231 0.3585 0.1080  -0.0416 -0.0326 32  ALA A C   
284  O O   . ALA A 33  ? 0.6923 0.5346 0.3578 0.1116  -0.0399 -0.0307 32  ALA A O   
285  C CB  . ALA A 33  ? 0.6641 0.4797 0.3299 0.1162  -0.0504 -0.0455 32  ALA A CB  
286  N N   . VAL A 34  ? 0.6456 0.5005 0.3368 0.1052  -0.0326 -0.0278 33  VAL A N   
287  C CA  . VAL A 34  ? 0.6364 0.5107 0.3349 0.1062  -0.0203 -0.0196 33  VAL A CA  
288  C C   . VAL A 34  ? 0.6356 0.5114 0.3348 0.0986  -0.0259 -0.0141 33  VAL A C   
289  O O   . VAL A 34  ? 0.6200 0.5046 0.3159 0.1013  -0.0202 -0.0089 33  VAL A O   
290  C CB  . VAL A 34  ? 0.6033 0.4928 0.3201 0.1043  -0.0100 -0.0155 33  VAL A CB  
291  C CG1 . VAL A 34  ? 0.5642 0.4728 0.2935 0.1015  0.0000  -0.0056 33  VAL A CG1 
292  C CG2 . VAL A 34  ? 0.5822 0.4751 0.2992 0.1135  -0.0016 -0.0189 33  VAL A CG2 
293  N N   . LEU A 35  ? 0.6328 0.5006 0.3375 0.0888  -0.0373 -0.0145 34  LEU A N   
294  C CA  . LEU A 35  ? 0.6458 0.5156 0.3537 0.0812  -0.0434 -0.0087 34  LEU A CA  
295  C C   . LEU A 35  ? 0.6699 0.5309 0.3612 0.0844  -0.0491 -0.0108 34  LEU A C   
296  O O   . LEU A 35  ? 0.6618 0.5304 0.3521 0.0838  -0.0469 -0.0046 34  LEU A O   
297  C CB  . LEU A 35  ? 0.6244 0.4894 0.3472 0.0690  -0.0545 -0.0088 34  LEU A CB  
298  C CG  . LEU A 35  ? 0.5581 0.4376 0.3107 0.0616  -0.0479 -0.0056 34  LEU A CG  
299  C CD1 . LEU A 35  ? 0.5294 0.4046 0.2955 0.0499  -0.0594 -0.0055 34  LEU A CD1 
300  C CD2 . LEU A 35  ? 0.5349 0.4349 0.3060 0.0597  -0.0358 0.0028  34  LEU A CD2 
301  N N   . THR A 36  ? 0.6935 0.5382 0.3720 0.0880  -0.0568 -0.0190 35  THR A N   
302  C CA  . THR A 36  ? 0.7243 0.5601 0.3854 0.0924  -0.0617 -0.0217 35  THR A CA  
303  C C   . THR A 36  ? 0.7429 0.5903 0.3957 0.1022  -0.0492 -0.0189 35  THR A C   
304  O O   . THR A 36  ? 0.7618 0.6117 0.4065 0.1029  -0.0498 -0.0157 35  THR A O   
305  C CB  . THR A 36  ? 0.7379 0.5541 0.3871 0.0961  -0.0708 -0.0312 35  THR A CB  
306  O OG1 . THR A 36  ? 0.7018 0.5085 0.3611 0.0861  -0.0823 -0.0325 35  THR A OG1 
307  C CG2 . THR A 36  ? 0.7945 0.6007 0.4250 0.1007  -0.0767 -0.0343 35  THR A CG2 
308  N N   . ALA A 37  ? 0.7322 0.5876 0.3880 0.1094  -0.0379 -0.0196 36  ALA A N   
309  C CA  . ALA A 37  ? 0.6968 0.5654 0.3480 0.1181  -0.0254 -0.0159 36  ALA A CA  
310  C C   . ALA A 37  ? 0.6750 0.5602 0.3362 0.1134  -0.0190 -0.0054 36  ALA A C   
311  O O   . ALA A 37  ? 0.7081 0.5998 0.3615 0.1175  -0.0147 -0.0015 36  ALA A O   
312  C CB  . ALA A 37  ? 0.7043 0.5805 0.3619 0.1251  -0.0147 -0.0174 36  ALA A CB  
313  N N   . VAL A 38  ? 0.6309 0.5229 0.3094 0.1049  -0.0186 -0.0002 37  VAL A N   
314  C CA  . VAL A 38  ? 0.6867 0.5937 0.3759 0.1006  -0.0130 0.0105  37  VAL A CA  
315  C C   . VAL A 38  ? 0.7401 0.6405 0.4213 0.0959  -0.0233 0.0125  37  VAL A C   
316  O O   . VAL A 38  ? 0.7350 0.6452 0.4165 0.0961  -0.0190 0.0201  37  VAL A O   
317  C CB  . VAL A 38  ? 0.6875 0.6041 0.3979 0.0936  -0.0093 0.0160  37  VAL A CB  
318  C CG1 . VAL A 38  ? 0.5848 0.5060 0.3032 0.0971  -0.0012 0.0129  37  VAL A CG1 
319  C CG2 . VAL A 38  ? 0.7397 0.6470 0.4560 0.0837  -0.0223 0.0150  37  VAL A CG2 
320  N N   . ARG A 39  ? 0.7542 0.6385 0.4292 0.0914  -0.0371 0.0063  38  ARG A N   
321  C CA  . ARG A 39  ? 0.7782 0.6567 0.4463 0.0870  -0.0472 0.0081  38  ARG A CA  
322  C C   . ARG A 39  ? 0.8282 0.7057 0.4775 0.0950  -0.0449 0.0068  38  ARG A C   
323  O O   . ARG A 39  ? 0.8273 0.7122 0.4748 0.0940  -0.0438 0.0138  38  ARG A O   
324  C CB  . ARG A 39  ? 0.8099 0.6718 0.4768 0.0805  -0.0623 0.0015  38  ARG A CB  
325  C CG  . ARG A 39  ? 0.8453 0.7103 0.5318 0.0695  -0.0677 0.0059  38  ARG A CG  
326  C CD  . ARG A 39  ? 0.9100 0.7604 0.5975 0.0624  -0.0825 0.0005  38  ARG A CD  
327  N NE  . ARG A 39  ? 0.9607 0.8002 0.6447 0.0651  -0.0841 -0.0078 38  ARG A NE  
328  C CZ  . ARG A 39  ? 0.9622 0.8030 0.6602 0.0604  -0.0844 -0.0084 38  ARG A CZ  
329  N NH1 . ARG A 39  ? 0.9445 0.7969 0.6605 0.0528  -0.0830 -0.0015 38  ARG A NH1 
330  N NH2 . ARG A 39  ? 0.9605 0.7907 0.6543 0.0633  -0.0862 -0.0156 38  ARG A NH2 
331  N N   . GLU A 40  ? 0.8665 0.7349 0.5018 0.1034  -0.0442 -0.0017 39  GLU A N   
332  C CA  . GLU A 40  ? 0.9527 0.8200 0.5692 0.1120  -0.0419 -0.0034 39  GLU A CA  
333  C C   . GLU A 40  ? 0.9288 0.8155 0.5493 0.1167  -0.0274 0.0050  39  GLU A C   
334  O O   . GLU A 40  ? 0.9448 0.8365 0.5559 0.1190  -0.0260 0.0091  39  GLU A O   
335  C CB  . GLU A 40  ? 1.0654 0.9192 0.6679 0.1207  -0.0439 -0.0141 39  GLU A CB  
336  C CG  . GLU A 40  ? 1.1579 0.9913 0.7562 0.1161  -0.0589 -0.0220 39  GLU A CG  
337  C CD  . GLU A 40  ? 1.2610 1.0802 0.8458 0.1253  -0.0611 -0.0320 39  GLU A CD  
338  O OE1 . GLU A 40  ? 1.2984 1.1251 0.8797 0.1350  -0.0502 -0.0329 39  GLU A OE1 
339  O OE2 . GLU A 40  ? 1.3035 1.1045 0.8821 0.1228  -0.0738 -0.0385 39  GLU A OE2 
340  N N   . GLY A 41  ? 0.8681 0.7666 0.5035 0.1178  -0.0167 0.0081  40  GLY A N   
341  C CA  . GLY A 41  ? 0.8103 0.7281 0.4535 0.1210  -0.0032 0.0171  40  GLY A CA  
342  C C   . GLY A 41  ? 0.7446 0.6722 0.3972 0.1136  -0.0031 0.0279  40  GLY A C   
343  O O   . GLY A 41  ? 0.7405 0.6797 0.3917 0.1163  0.0039  0.0350  40  GLY A O   
344  N N   . LEU A 42  ? 0.6934 0.6168 0.3563 0.1043  -0.0110 0.0297  41  LEU A N   
345  C CA  . LEU A 42  ? 0.6882 0.6196 0.3604 0.0975  -0.0124 0.0401  41  LEU A CA  
346  C C   . LEU A 42  ? 0.7200 0.6457 0.3755 0.0979  -0.0199 0.0405  41  LEU A C   
347  O O   . LEU A 42  ? 0.6787 0.6146 0.3366 0.0968  -0.0164 0.0498  41  LEU A O   
348  C CB  . LEU A 42  ? 0.6603 0.5882 0.3477 0.0881  -0.0199 0.0415  41  LEU A CB  
349  C CG  . LEU A 42  ? 0.6039 0.5421 0.3121 0.0860  -0.0112 0.0453  41  LEU A CG  
350  C CD1 . LEU A 42  ? 0.5450 0.4798 0.2672 0.0770  -0.0195 0.0472  41  LEU A CD1 
351  C CD2 . LEU A 42  ? 0.6006 0.5572 0.3210 0.0876  0.0019  0.0559  41  LEU A CD2 
352  N N   . LYS A 43  ? 0.7690 0.6783 0.4085 0.0991  -0.0307 0.0309  42  LYS A N   
353  C CA  . LYS A 43  ? 0.8675 0.7713 0.4887 0.1012  -0.0370 0.0300  42  LYS A CA  
354  C C   . LYS A 43  ? 0.8907 0.8059 0.5030 0.1093  -0.0257 0.0341  42  LYS A C   
355  O O   . LYS A 43  ? 0.9058 0.8285 0.5156 0.1079  -0.0250 0.0421  42  LYS A O   
356  C CB  . LYS A 43  ? 0.9456 0.8303 0.5503 0.1038  -0.0476 0.0177  42  LYS A CB  
357  C CG  . LYS A 43  ? 1.0130 0.8855 0.6218 0.0946  -0.0624 0.0152  42  LYS A CG  
358  C CD  . LYS A 43  ? 1.0810 0.9344 0.6731 0.0980  -0.0723 0.0036  42  LYS A CD  
359  C CE  . LYS A 43  ? 1.0967 0.9385 0.6938 0.0885  -0.0875 0.0016  42  LYS A CE  
360  N NZ  . LYS A 43  ? 1.1131 0.9353 0.6946 0.0916  -0.0972 -0.0092 42  LYS A NZ  
361  N N   . LYS A 44  ? 0.9046 0.8221 0.5135 0.1177  -0.0168 0.0293  43  LYS A N   
362  C CA  . LYS A 44  ? 0.9484 0.8773 0.5493 0.1260  -0.0062 0.0329  43  LYS A CA  
363  C C   . LYS A 44  ? 0.9228 0.8711 0.5411 0.1226  0.0039  0.0463  43  LYS A C   
364  O O   . LYS A 44  ? 0.9267 0.8839 0.5389 0.1249  0.0081  0.0529  43  LYS A O   
365  C CB  . LYS A 44  ? 1.0068 0.9349 0.6034 0.1357  0.0009  0.0254  43  LYS A CB  
366  C CG  . LYS A 44  ? 1.0875 0.9958 0.6655 0.1406  -0.0089 0.0124  43  LYS A CG  
367  C CD  . LYS A 44  ? 1.1388 1.0479 0.7100 0.1520  -0.0012 0.0064  43  LYS A CD  
368  C CE  . LYS A 44  ? 1.1903 1.0786 0.7425 0.1575  -0.0114 -0.0062 43  LYS A CE  
369  N NZ  . LYS A 44  ? 1.2232 1.1125 0.7681 0.1696  -0.0042 -0.0117 43  LYS A NZ  
370  N N   . VAL A 45  ? 0.8607 0.8156 0.5010 0.1169  0.0077  0.0506  44  VAL A N   
371  C CA  . VAL A 45  ? 0.8076 0.7804 0.4670 0.1138  0.0176  0.0630  44  VAL A CA  
372  C C   . VAL A 45  ? 0.8010 0.7759 0.4622 0.1071  0.0121  0.0721  44  VAL A C   
373  O O   . VAL A 45  ? 0.7816 0.7695 0.4490 0.1069  0.0189  0.0822  44  VAL A O   
374  C CB  . VAL A 45  ? 0.7604 0.7383 0.4428 0.1093  0.0221  0.0645  44  VAL A CB  
375  C CG1 . VAL A 45  ? 0.7340 0.7275 0.4386 0.1035  0.0287  0.0776  44  VAL A CG1 
376  C CG2 . VAL A 45  ? 0.7288 0.7101 0.4127 0.1165  0.0305  0.0588  44  VAL A CG2 
377  N N   . PHE A 46  ? 0.7937 0.7561 0.4507 0.1013  -0.0007 0.0690  45  PHE A N   
378  C CA  . PHE A 46  ? 0.7765 0.7402 0.4360 0.0949  -0.0072 0.0775  45  PHE A CA  
379  C C   . PHE A 46  ? 0.8243 0.7823 0.4608 0.0979  -0.0133 0.0758  45  PHE A C   
380  O O   . PHE A 46  ? 0.8100 0.7694 0.4470 0.0929  -0.0189 0.0831  45  PHE A O   
381  C CB  . PHE A 46  ? 0.7349 0.6904 0.4052 0.0865  -0.0179 0.0766  45  PHE A CB  
382  C CG  . PHE A 46  ? 0.7171 0.6820 0.4134 0.0816  -0.0121 0.0834  45  PHE A CG  
383  C CD1 . PHE A 46  ? 0.7016 0.6688 0.4070 0.0837  -0.0051 0.0790  45  PHE A CD1 
384  C CD2 . PHE A 46  ? 0.6997 0.6716 0.4121 0.0753  -0.0135 0.0943  45  PHE A CD2 
385  C CE1 . PHE A 46  ? 0.7082 0.6847 0.4379 0.0793  0.0004  0.0852  45  PHE A CE1 
386  C CE2 . PHE A 46  ? 0.7121 0.6929 0.4496 0.0713  -0.0080 0.1003  45  PHE A CE2 
387  C CZ  . PHE A 46  ? 0.7121 0.6955 0.4582 0.0731  -0.0009 0.0957  45  PHE A CZ  
388  N N   . ALA A 47  ? 0.9468 0.8982 0.5637 0.1060  -0.0127 0.0663  46  ALA A N   
389  C CA  . ALA A 47  ? 1.0184 0.9659 0.6129 0.1100  -0.0169 0.0649  46  ALA A CA  
390  C C   . ALA A 47  ? 1.0771 1.0393 0.6733 0.1102  -0.0096 0.0772  46  ALA A C   
391  O O   . ALA A 47  ? 1.1060 1.0665 0.6908 0.1085  -0.0159 0.0807  46  ALA A O   
392  C CB  . ALA A 47  ? 1.0577 0.9983 0.6333 0.1204  -0.0144 0.0536  46  ALA A CB  
393  N N   . ASP A 48  ? 1.0828 1.0598 0.6939 0.1120  0.0033  0.0841  47  ASP A N   
394  C CA  . ASP A 48  ? 1.1078 1.0992 0.7231 0.1119  0.0104  0.0964  47  ASP A CA  
395  C C   . ASP A 48  ? 1.0602 1.0583 0.6987 0.1025  0.0097  0.1081  47  ASP A C   
396  O O   . ASP A 48  ? 1.0523 1.0633 0.7004 0.1016  0.0169  0.1192  47  ASP A O   
397  C CB  . ASP A 48  ? 1.1383 1.1433 0.7571 0.1195  0.0247  0.0982  47  ASP A CB  
398  C CG  . ASP A 48  ? 1.1331 1.1431 0.7733 0.1186  0.0316  0.0971  47  ASP A CG  
399  O OD1 . ASP A 48  ? 1.1264 1.1316 0.7809 0.1114  0.0267  0.0971  47  ASP A OD1 
400  O OD2 . ASP A 48  ? 1.1427 1.1620 0.7856 0.1252  0.0419  0.0964  47  ASP A OD2 
401  N N   . ARG A 49  ? 0.9943 0.9838 0.6426 0.0957  0.0011  0.1060  48  ARG A N   
402  C CA  . ARG A 49  ? 0.8954 0.8889 0.5643 0.0871  -0.0018 0.1162  48  ARG A CA  
403  C C   . ARG A 49  ? 0.8091 0.7944 0.4691 0.0821  -0.0147 0.1187  48  ARG A C   
404  O O   . ARG A 49  ? 0.7574 0.7465 0.4326 0.0760  -0.0171 0.1286  48  ARG A O   
405  C CB  . ARG A 49  ? 0.8970 0.8882 0.5855 0.0827  -0.0026 0.1136  48  ARG A CB  
406  C CG  . ARG A 49  ? 0.9180 0.9227 0.6293 0.0827  0.0099  0.1191  48  ARG A CG  
407  C CD  . ARG A 49  ? 0.9226 0.9310 0.6598 0.0747  0.0080  0.1271  48  ARG A CD  
408  N NE  . ARG A 49  ? 0.9133 0.9311 0.6730 0.0738  0.0175  0.1288  48  ARG A NE  
409  C CZ  . ARG A 49  ? 0.8923 0.9147 0.6775 0.0674  0.0177  0.1348  48  ARG A CZ  
410  N NH1 . ARG A 49  ? 0.8831 0.9021 0.6753 0.0619  0.0091  0.1398  48  ARG A NH1 
411  N NH2 . ARG A 49  ? 0.8715 0.9024 0.6763 0.0667  0.0262  0.1356  48  ARG A NH2 
412  N N   . GLY A 50  ? 0.8071 0.7814 0.4442 0.0846  -0.0233 0.1101  49  GLY A N   
413  C CA  . GLY A 50  ? 0.8446 0.8118 0.4741 0.0796  -0.0364 0.1121  49  GLY A CA  
414  C C   . GLY A 50  ? 0.8153 0.7752 0.4580 0.0722  -0.0471 0.1101  49  GLY A C   
415  O O   . GLY A 50  ? 0.7960 0.7547 0.4433 0.0662  -0.0564 0.1161  49  GLY A O   
416  N N   . GLU A 51  ? 0.8401 0.7955 0.4896 0.0728  -0.0461 0.1020  50  GLU A N   
417  C CA  . GLU A 51  ? 0.8304 0.7806 0.4952 0.0659  -0.0549 0.1006  50  GLU A CA  
418  C C   . GLU A 51  ? 0.8031 0.7439 0.4635 0.0684  -0.0562 0.0878  50  GLU A C   
419  O O   . GLU A 51  ? 0.7907 0.7322 0.4443 0.0749  -0.0471 0.0825  50  GLU A O   
420  C CB  . GLU A 51  ? 0.8626 0.8221 0.5538 0.0615  -0.0494 0.1106  50  GLU A CB  
421  C CG  . GLU A 51  ? 0.9195 0.8756 0.6283 0.0546  -0.0582 0.1108  50  GLU A CG  
422  C CD  . GLU A 51  ? 0.9413 0.9069 0.6764 0.0514  -0.0521 0.1207  50  GLU A CD  
423  O OE1 . GLU A 51  ? 0.9630 0.9284 0.7126 0.0457  -0.0597 0.1258  50  GLU A OE1 
424  O OE2 . GLU A 51  ? 0.9293 0.9039 0.6725 0.0546  -0.0393 0.1233  50  GLU A OE2 
425  N N   . ALA A 52  ? 0.7852 0.7173 0.4505 0.0631  -0.0677 0.0831  51  ALA A N   
426  C CA  . ALA A 52  ? 0.7944 0.7164 0.4584 0.0639  -0.0700 0.0717  51  ALA A CA  
427  C C   . ALA A 52  ? 0.7308 0.6592 0.4120 0.0639  -0.0603 0.0734  51  ALA A C   
428  O O   . ALA A 52  ? 0.6214 0.5595 0.3214 0.0602  -0.0566 0.0829  51  ALA A O   
429  C CB  . ALA A 52  ? 0.8112 0.7238 0.4806 0.0569  -0.0843 0.0676  51  ALA A CB  
430  N N   . ALA A 53  ? 0.7677 0.6907 0.4429 0.0685  -0.0562 0.0642  52  ALA A N   
431  C CA  . ALA A 53  ? 0.7374 0.6667 0.4282 0.0688  -0.0471 0.0650  52  ALA A CA  
432  C C   . ALA A 53  ? 0.6981 0.6259 0.4081 0.0606  -0.0540 0.0670  52  ALA A C   
433  O O   . ALA A 53  ? 0.7131 0.6315 0.4222 0.0553  -0.0665 0.0629  52  ALA A O   
434  C CB  . ALA A 53  ? 0.7673 0.6897 0.4478 0.0750  -0.0434 0.0541  52  ALA A CB  
435  N N   . PRO A 54  ? 0.6394 0.5774 0.3688 0.0592  -0.0459 0.0734  53  PRO A N   
436  C CA  . PRO A 54  ? 0.6254 0.5650 0.3806 0.0498  -0.0507 0.0730  53  PRO A CA  
437  C C   . PRO A 54  ? 0.5914 0.5210 0.3441 0.0486  -0.0551 0.0622  53  PRO A C   
438  O O   . PRO A 54  ? 0.5752 0.5015 0.3158 0.0552  -0.0494 0.0563  53  PRO A O   
439  C CB  . PRO A 54  ? 0.6475 0.6037 0.4301 0.0477  -0.0379 0.0797  53  PRO A CB  
440  C CG  . PRO A 54  ? 0.6465 0.6070 0.4158 0.0567  -0.0262 0.0802  53  PRO A CG  
441  C CD  . PRO A 54  ? 0.6571 0.6093 0.3945 0.0636  -0.0309 0.0799  53  PRO A CD  
442  N N   . THR A 55  ? 0.5746 0.4997 0.3390 0.0404  -0.0656 0.0602  54  THR A N   
443  C CA  . THR A 55  ? 0.5541 0.4710 0.3201 0.0376  -0.0704 0.0515  54  THR A CA  
444  C C   . THR A 55  ? 0.5077 0.4367 0.3007 0.0342  -0.0606 0.0516  54  THR A C   
445  O O   . THR A 55  ? 0.4923 0.4352 0.3058 0.0320  -0.0525 0.0583  54  THR A O   
446  C CB  . THR A 55  ? 0.5709 0.4798 0.3398 0.0297  -0.0857 0.0503  54  THR A CB  
447  O OG1 . THR A 55  ? 0.5899 0.5115 0.3863 0.0222  -0.0852 0.0576  54  THR A OG1 
448  C CG2 . THR A 55  ? 0.5877 0.4871 0.3350 0.0321  -0.0945 0.0494  54  THR A CG2 
449  N N   . PHE A 56  ? 0.5354 0.4584 0.3278 0.0337  -0.0617 0.0440  55  PHE A N   
450  C CA  . PHE A 56  ? 0.4940 0.4277 0.3106 0.0302  -0.0536 0.0435  55  PHE A CA  
451  C C   . PHE A 56  ? 0.5124 0.4390 0.3342 0.0242  -0.0623 0.0375  55  PHE A C   
452  O O   . PHE A 56  ? 0.5352 0.4469 0.3386 0.0248  -0.0728 0.0324  55  PHE A O   
453  C CB  . PHE A 56  ? 0.4605 0.3985 0.2726 0.0378  -0.0409 0.0416  55  PHE A CB  
454  C CG  . PHE A 56  ? 0.5213 0.4455 0.3093 0.0445  -0.0436 0.0333  55  PHE A CG  
455  C CD1 . PHE A 56  ? 0.4809 0.3998 0.2731 0.0422  -0.0463 0.0268  55  PHE A CD1 
456  C CD2 . PHE A 56  ? 0.6131 0.5296 0.3738 0.0535  -0.0437 0.0321  55  PHE A CD2 
457  C CE1 . PHE A 56  ? 0.5490 0.4542 0.3196 0.0487  -0.0494 0.0190  55  PHE A CE1 
458  C CE2 . PHE A 56  ? 0.6461 0.5492 0.3843 0.0606  -0.0464 0.0237  55  PHE A CE2 
459  C CZ  . PHE A 56  ? 0.6067 0.5036 0.3503 0.0581  -0.0495 0.0170  55  PHE A CZ  
460  N N   . THR A 57  ? 0.5145 0.4523 0.3618 0.0183  -0.0579 0.0385  56  THR A N   
461  C CA  . THR A 57  ? 0.4959 0.4305 0.3514 0.0124  -0.0639 0.0340  56  THR A CA  
462  C C   . THR A 57  ? 0.4401 0.3785 0.3007 0.0152  -0.0545 0.0300  56  THR A C   
463  O O   . THR A 57  ? 0.3951 0.3471 0.2732 0.0150  -0.0439 0.0329  56  THR A O   
464  C CB  . THR A 57  ? 0.5051 0.4505 0.3859 0.0033  -0.0669 0.0383  56  THR A CB  
465  O OG1 . THR A 57  ? 0.6019 0.5458 0.4798 0.0014  -0.0743 0.0431  56  THR A OG1 
466  C CG2 . THR A 57  ? 0.4756 0.4173 0.3623 -0.0032 -0.0749 0.0346  56  THR A CG2 
467  N N   . PRO A 58  ? 0.4405 0.3668 0.2864 0.0180  -0.0583 0.0234  57  PRO A N   
468  C CA  . PRO A 58  ? 0.4394 0.3694 0.2906 0.0206  -0.0500 0.0198  57  PRO A CA  
469  C C   . PRO A 58  ? 0.4444 0.3796 0.3152 0.0123  -0.0526 0.0189  57  PRO A C   
470  O O   . PRO A 58  ? 0.4210 0.3530 0.2962 0.0053  -0.0628 0.0195  57  PRO A O   
471  C CB  . PRO A 58  ? 0.4549 0.3680 0.2795 0.0281  -0.0542 0.0132  57  PRO A CB  
472  C CG  . PRO A 58  ? 0.4466 0.3458 0.2588 0.0245  -0.0691 0.0119  57  PRO A CG  
473  C CD  . PRO A 58  ? 0.4383 0.3461 0.2601 0.0200  -0.0705 0.0189  57  PRO A CD  
474  N N   . PHE A 59  ? 0.4040 0.3485 0.2870 0.0132  -0.0430 0.0179  58  PHE A N   
475  C CA  . PHE A 59  ? 0.4033 0.3535 0.3034 0.0063  -0.0444 0.0167  58  PHE A CA  
476  C C   . PHE A 59  ? 0.3727 0.3256 0.2744 0.0103  -0.0361 0.0134  58  PHE A C   
477  O O   . PHE A 59  ? 0.3658 0.3241 0.2664 0.0165  -0.0261 0.0141  58  PHE A O   
478  C CB  . PHE A 59  ? 0.3704 0.3365 0.2952 -0.0007 -0.0416 0.0215  58  PHE A CB  
479  C CG  . PHE A 59  ? 0.3327 0.3119 0.2699 0.0021  -0.0294 0.0244  58  PHE A CG  
480  C CD1 . PHE A 59  ? 0.3126 0.2937 0.2467 0.0053  -0.0265 0.0287  58  PHE A CD1 
481  C CD2 . PHE A 59  ? 0.3066 0.2964 0.2593 0.0010  -0.0214 0.0233  58  PHE A CD2 
482  C CE1 . PHE A 59  ? 0.2873 0.2800 0.2339 0.0072  -0.0160 0.0320  58  PHE A CE1 
483  C CE2 . PHE A 59  ? 0.3074 0.3086 0.2723 0.0030  -0.0111 0.0261  58  PHE A CE2 
484  C CZ  . PHE A 59  ? 0.2771 0.2795 0.2393 0.0060  -0.0085 0.0306  58  PHE A CZ  
485  N N   . ASN A 60  ? 0.3608 0.3101 0.2655 0.0066  -0.0408 0.0103  59  ASN A N   
486  C CA  . ASN A 60  ? 0.3366 0.2880 0.2434 0.0099  -0.0343 0.0071  59  ASN A CA  
487  C C   . ASN A 60  ? 0.3033 0.2730 0.2315 0.0081  -0.0232 0.0099  59  ASN A C   
488  O O   . ASN A 60  ? 0.2714 0.2517 0.2170 0.0013  -0.0233 0.0128  59  ASN A O   
489  C CB  . ASN A 60  ? 0.3453 0.2898 0.2528 0.0050  -0.0427 0.0044  59  ASN A CB  
490  C CG  . ASN A 60  ? 0.3667 0.2909 0.2524 0.0073  -0.0543 0.0008  59  ASN A CG  
491  O OD1 . ASN A 60  ? 0.3718 0.2861 0.2385 0.0152  -0.0542 -0.0015 59  ASN A OD1 
492  N ND2 . ASN A 60  ? 0.3299 0.2478 0.2179 0.0005  -0.0647 0.0003  59  ASN A ND2 
493  N N   . GLN A 61  ? 0.3167 0.2900 0.2435 0.0144  -0.0139 0.0087  60  GLN A N   
494  C CA  . GLN A 61  ? 0.2657 0.2549 0.2117 0.0131  -0.0038 0.0108  60  GLN A CA  
495  C C   . GLN A 61  ? 0.2714 0.2616 0.2187 0.0155  0.0001  0.0076  60  GLN A C   
496  O O   . GLN A 61  ? 0.2703 0.2487 0.2026 0.0197  -0.0039 0.0039  60  GLN A O   
497  C CB  . GLN A 61  ? 0.2391 0.2350 0.1860 0.0180  0.0050  0.0146  60  GLN A CB  
498  C CG  . GLN A 61  ? 0.2963 0.2950 0.2479 0.0147  0.0027  0.0189  60  GLN A CG  
499  C CD  . GLN A 61  ? 0.3058 0.3160 0.2686 0.0165  0.0121  0.0237  60  GLN A CD  
500  O OE1 . GLN A 61  ? 0.3493 0.3584 0.3067 0.0186  0.0123  0.0276  60  GLN A OE1 
501  N NE2 . GLN A 61  ? 0.2977 0.3186 0.2763 0.0153  0.0194  0.0237  60  GLN A NE2 
502  N N   . GLY A 62  ? 0.2447 0.2489 0.2104 0.0130  0.0074  0.0088  61  GLY A N   
503  C CA  . GLY A 62  ? 0.2304 0.2376 0.1984 0.0160  0.0124  0.0067  61  GLY A CA  
504  C C   . GLY A 62  ? 0.2158 0.2177 0.1831 0.0125  0.0059  0.0034  61  GLY A C   
505  O O   . GLY A 62  ? 0.2196 0.2186 0.1889 0.0061  -0.0021 0.0033  61  GLY A O   
506  N N   . SER A 63  ? 0.2093 0.2110 0.1745 0.0171  0.0097  0.0014  62  SER A N   
507  C CA  . SER A 63  ? 0.2368 0.2363 0.2047 0.0137  0.0051  -0.0009 62  SER A CA  
508  C C   . SER A 63  ? 0.2494 0.2321 0.2020 0.0133  -0.0062 -0.0032 62  SER A C   
509  O O   . SER A 63  ? 0.2645 0.2457 0.2218 0.0070  -0.0128 -0.0034 62  SER A O   
510  C CB  . SER A 63  ? 0.2008 0.2034 0.1693 0.0196  0.0116  -0.0022 62  SER A CB  
511  O OG  . SER A 63  ? 0.2664 0.2584 0.2172 0.0292  0.0126  -0.0042 62  SER A OG  
512  N N   . TYR A 64  ? 0.2591 0.2288 0.1933 0.0198  -0.0088 -0.0049 63  TYR A N   
513  C CA  . TYR A 64  ? 0.3007 0.2527 0.2197 0.0193  -0.0207 -0.0075 63  TYR A CA  
514  C C   . TYR A 64  ? 0.3016 0.2534 0.2255 0.0104  -0.0288 -0.0049 63  TYR A C   
515  O O   . TYR A 64  ? 0.3366 0.2772 0.2548 0.0064  -0.0397 -0.0058 63  TYR A O   
516  C CB  . TYR A 64  ? 0.3698 0.3078 0.2663 0.0296  -0.0213 -0.0108 63  TYR A CB  
517  C CG  . TYR A 64  ? 0.4132 0.3525 0.3043 0.0397  -0.0127 -0.0131 63  TYR A CG  
518  C CD1 . TYR A 64  ? 0.4454 0.3950 0.3502 0.0389  -0.0068 -0.0125 63  TYR A CD1 
519  C CD2 . TYR A 64  ? 0.4991 0.4299 0.3710 0.0502  -0.0104 -0.0156 63  TYR A CD2 
520  C CE1 . TYR A 64  ? 0.4466 0.3983 0.3475 0.0482  0.0009  -0.0141 63  TYR A CE1 
521  C CE2 . TYR A 64  ? 0.5241 0.4574 0.3915 0.0600  -0.0022 -0.0173 63  TYR A CE2 
522  C CZ  . TYR A 64  ? 0.5028 0.4467 0.3853 0.0588  0.0034  -0.0164 63  TYR A CZ  
523  O OH  . TYR A 64  ? 0.5172 0.4645 0.3961 0.0686  0.0114  -0.0175 63  TYR A OH  
524  N N   . ALA A 65  ? 0.2511 0.2154 0.1865 0.0071  -0.0239 -0.0014 64  ALA A N   
525  C CA  . ALA A 65  ? 0.2554 0.2232 0.1996 -0.0016 -0.0304 0.0016  64  ALA A CA  
526  C C   . ALA A 65  ? 0.2724 0.2531 0.2356 -0.0095 -0.0299 0.0033  64  ALA A C   
527  O O   . ALA A 65  ? 0.2985 0.2792 0.2665 -0.0168 -0.0378 0.0052  64  ALA A O   
528  C CB  . ALA A 65  ? 0.2325 0.2081 0.1814 -0.0013 -0.0258 0.0046  64  ALA A CB  
529  N N   . MET A 66  ? 0.2741 0.2664 0.2481 -0.0082 -0.0207 0.0029  65  MET A N   
530  C CA  . MET A 66  ? 0.2438 0.2498 0.2354 -0.0150 -0.0192 0.0042  65  MET A CA  
531  C C   . MET A 66  ? 0.2306 0.2326 0.2207 -0.0166 -0.0232 0.0030  65  MET A C   
532  O O   . MET A 66  ? 0.2066 0.2201 0.2100 -0.0223 -0.0222 0.0043  65  MET A O   
533  C CB  . MET A 66  ? 0.2197 0.2407 0.2249 -0.0134 -0.0080 0.0045  65  MET A CB  
534  C CG  . MET A 66  ? 0.2088 0.2355 0.2195 -0.0133 -0.0044 0.0066  65  MET A CG  
535  S SD  . MET A 66  ? 0.2190 0.2622 0.2473 -0.0125 0.0072  0.0071  65  MET A SD  
536  C CE  . MET A 66  ? 0.2373 0.2745 0.2540 -0.0031 0.0138  0.0068  65  MET A CE  
537  N N   . ASN A 67  ? 0.2438 0.2297 0.2176 -0.0116 -0.0279 0.0005  66  ASN A N   
538  C CA  . ASN A 67  ? 0.2487 0.2290 0.2205 -0.0124 -0.0322 -0.0006 66  ASN A CA  
539  C C   . ASN A 67  ? 0.2579 0.2507 0.2405 -0.0107 -0.0232 -0.0010 66  ASN A C   
540  O O   . ASN A 67  ? 0.2144 0.2126 0.2051 -0.0154 -0.0249 0.0001  66  ASN A O   
541  C CB  . ASN A 67  ? 0.2546 0.2352 0.2323 -0.0220 -0.0419 0.0025  66  ASN A CB  
542  C CG  . ASN A 67  ? 0.2586 0.2279 0.2301 -0.0226 -0.0494 0.0018  66  ASN A CG  
543  O OD1 . ASN A 67  ? 0.3097 0.2664 0.2688 -0.0150 -0.0496 -0.0018 66  ASN A OD1 
544  N ND2 . ASN A 67  ? 0.2456 0.2195 0.2259 -0.0314 -0.0558 0.0056  66  ASN A ND2 
545  N N   . THR A 68  ? 0.2287 0.2265 0.2115 -0.0042 -0.0136 -0.0021 67  THR A N   
546  C CA  . THR A 68  ? 0.2497 0.2582 0.2417 -0.0017 -0.0051 -0.0025 67  THR A CA  
547  C C   . THR A 68  ? 0.2396 0.2405 0.2199 0.0086  -0.0008 -0.0048 67  THR A C   
548  O O   . THR A 68  ? 0.2483 0.2589 0.2359 0.0120  0.0076  -0.0046 67  THR A O   
549  C CB  . THR A 68  ? 0.1974 0.2226 0.2047 -0.0042 0.0031  -0.0008 67  THR A CB  
550  O OG1 . THR A 68  ? 0.2118 0.2341 0.2135 -0.0005 0.0057  -0.0002 67  THR A OG1 
551  C CG2 . THR A 68  ? 0.1756 0.2106 0.1958 -0.0135 -0.0002 0.0009  67  THR A CG2 
552  N N   . GLY A 69  ? 0.2402 0.2242 0.2026 0.0138  -0.0066 -0.0071 68  GLY A N   
553  C CA  . GLY A 69  ? 0.2635 0.2409 0.2136 0.0246  -0.0020 -0.0095 68  GLY A CA  
554  C C   . GLY A 69  ? 0.2628 0.2363 0.2113 0.0285  -0.0028 -0.0115 68  GLY A C   
555  O O   . GLY A 69  ? 0.2447 0.2132 0.1950 0.0234  -0.0104 -0.0117 68  GLY A O   
556  N N   . VAL A 70  ? 0.2634 0.2398 0.2089 0.0376  0.0053  -0.0125 69  VAL A N   
557  C CA  . VAL A 70  ? 0.2341 0.2073 0.1779 0.0431  0.0056  -0.0143 69  VAL A CA  
558  C C   . VAL A 70  ? 0.2635 0.2244 0.1884 0.0556  0.0068  -0.0180 69  VAL A C   
559  O O   . VAL A 70  ? 0.2675 0.2287 0.1845 0.0606  0.0113  -0.0180 69  VAL A O   
560  C CB  . VAL A 70  ? 0.2411 0.2328 0.2024 0.0426  0.0150  -0.0116 69  VAL A CB  
561  C CG1 . VAL A 70  ? 0.2230 0.2245 0.2005 0.0313  0.0123  -0.0093 69  VAL A CG1 
562  C CG2 . VAL A 70  ? 0.2308 0.2348 0.1971 0.0456  0.0255  -0.0092 69  VAL A CG2 
563  N N   . LYS A 71  ? 0.2665 0.2164 0.1839 0.0610  0.0025  -0.0212 70  LYS A N   
564  C CA  . LYS A 71  ? 0.3006 0.2406 0.2010 0.0744  0.0048  -0.0252 70  LYS A CA  
565  C C   . LYS A 71  ? 0.3499 0.3069 0.2581 0.0812  0.0183  -0.0227 70  LYS A C   
566  O O   . LYS A 71  ? 0.3486 0.3205 0.2746 0.0771  0.0232  -0.0193 70  LYS A O   
567  C CB  . LYS A 71  ? 0.3384 0.2625 0.2303 0.0788  -0.0033 -0.0293 70  LYS A CB  
568  C CG  . LYS A 71  ? 0.3762 0.2813 0.2589 0.0727  -0.0178 -0.0315 70  LYS A CG  
569  C CD  . LYS A 71  ? 0.3984 0.2867 0.2732 0.0774  -0.0262 -0.0354 70  LYS A CD  
570  C CE  . LYS A 71  ? 0.4712 0.3372 0.3326 0.0738  -0.0410 -0.0383 70  LYS A CE  
571  N NZ  . LYS A 71  ? 0.5644 0.4156 0.4236 0.0745  -0.0508 -0.0402 70  LYS A NZ  
572  N N   . PRO A 72  ? 0.3970 0.3531 0.2927 0.0913  0.0243  -0.0239 71  PRO A N   
573  C CA  . PRO A 72  ? 0.4352 0.4079 0.3385 0.0984  0.0369  -0.0208 71  PRO A CA  
574  C C   . PRO A 72  ? 0.4299 0.4016 0.3341 0.1060  0.0381  -0.0228 71  PRO A C   
575  O O   . PRO A 72  ? 0.4294 0.3840 0.3219 0.1097  0.0296  -0.0278 71  PRO A O   
576  C CB  . PRO A 72  ? 0.4880 0.4573 0.3740 0.1080  0.0414  -0.0218 71  PRO A CB  
577  C CG  . PRO A 72  ? 0.5084 0.4543 0.3732 0.1103  0.0298  -0.0282 71  PRO A CG  
578  C CD  . PRO A 72  ? 0.4164 0.3569 0.2902 0.0969  0.0196  -0.0278 71  PRO A CD  
579  N N   . LEU A 73  ? 0.3741 0.3643 0.2939 0.1069  0.0475  -0.0182 72  LEU A N   
580  C CA  . LEU A 73  ? 0.3782 0.3697 0.3003 0.1125  0.0485  -0.0185 72  LEU A CA  
581  C C   . LEU A 73  ? 0.4406 0.4237 0.3454 0.1222  0.0485  -0.0208 72  LEU A C   
582  O O   . LEU A 73  ? 0.4639 0.4445 0.3581 0.1238  0.0494  -0.0207 72  LEU A O   
583  C CB  . LEU A 73  ? 0.3666 0.3795 0.3109 0.1068  0.0558  -0.0118 72  LEU A CB  
584  C CG  . LEU A 73  ? 0.4292 0.4526 0.3925 0.0970  0.0558  -0.0093 72  LEU A CG  
585  C CD1 . LEU A 73  ? 0.4533 0.4946 0.4356 0.0911  0.0613  -0.0035 72  LEU A CD1 
586  C CD2 . LEU A 73  ? 0.4439 0.4581 0.4057 0.0997  0.0498  -0.0132 72  LEU A CD2 
587  N N   . GLU A 74  ? 0.5486 0.5274 0.4503 0.1291  0.0473  -0.0230 73  GLU A N   
588  C CA  . GLU A 74  ? 0.6154 0.5873 0.5012 0.1392  0.0475  -0.0255 73  GLU A CA  
589  C C   . GLU A 74  ? 0.5900 0.5778 0.4802 0.1394  0.0564  -0.0196 73  GLU A C   
590  O O   . GLU A 74  ? 0.5739 0.5792 0.4821 0.1348  0.0629  -0.0137 73  GLU A O   
591  C CB  . GLU A 74  ? 0.7321 0.7008 0.6181 0.1459  0.0462  -0.0277 73  GLU A CB  
592  C CG  . GLU A 74  ? 0.8638 0.8240 0.7325 0.1573  0.0457  -0.0313 73  GLU A CG  
593  C CD  . GLU A 74  ? 0.9400 0.8964 0.8092 0.1641  0.0439  -0.0338 73  GLU A CD  
594  O OE1 . GLU A 74  ? 0.9346 0.8961 0.8186 0.1599  0.0436  -0.0321 73  GLU A OE1 
595  O OE2 . GLU A 74  ? 0.9875 0.9358 0.8423 0.1740  0.0428  -0.0376 73  GLU A OE2 
596  N N   . GLY A 75  ? 0.6099 0.5907 0.4836 0.1445  0.0558  -0.0213 74  GLY A N   
597  C CA  . GLY A 75  ? 0.5928 0.5870 0.4691 0.1449  0.0633  -0.0156 74  GLY A CA  
598  C C   . GLY A 75  ? 0.6182 0.6180 0.5000 0.1366  0.0648  -0.0118 74  GLY A C   
599  O O   . GLY A 75  ? 0.6491 0.6572 0.5303 0.1374  0.0697  -0.0074 74  GLY A O   
600  N N   . GLY A 76  ? 0.5591 0.5549 0.4466 0.1288  0.0607  -0.0132 75  GLY A N   
601  C CA  . GLY A 76  ? 0.5399 0.5401 0.4322 0.1212  0.0616  -0.0102 75  GLY A CA  
602  C C   . GLY A 76  ? 0.5244 0.5086 0.3958 0.1244  0.0559  -0.0147 75  GLY A C   
603  O O   . GLY A 76  ? 0.5425 0.5106 0.3953 0.1319  0.0500  -0.0208 75  GLY A O   
604  N N   . GLU A 77  ? 0.4946 0.4828 0.3692 0.1182  0.0569  -0.0118 76  GLU A N   
605  C CA  . GLU A 77  ? 0.5399 0.5148 0.3957 0.1200  0.0518  -0.0150 76  GLU A CA  
606  C C   . GLU A 77  ? 0.5062 0.4748 0.3634 0.1122  0.0465  -0.0171 76  GLU A C   
607  O O   . GLU A 77  ? 0.4347 0.4154 0.3108 0.1045  0.0499  -0.0134 76  GLU A O   
608  C CB  . GLU A 77  ? 0.6248 0.6096 0.4801 0.1207  0.0577  -0.0092 76  GLU A CB  
609  C CG  . GLU A 77  ? 0.6942 0.6847 0.5451 0.1290  0.0627  -0.0071 76  GLU A CG  
610  C CD  . GLU A 77  ? 0.7374 0.7369 0.5871 0.1296  0.0678  -0.0012 76  GLU A CD  
611  O OE1 . GLU A 77  ? 0.7253 0.7234 0.5738 0.1246  0.0663  0.0002  76  GLU A OE1 
612  O OE2 . GLU A 77  ? 0.7653 0.7734 0.6152 0.1352  0.0732  0.0022  76  GLU A OE2 
613  N N   . TYR A 78  ? 0.5300 0.4793 0.3671 0.1137  0.0371  -0.0229 77  TYR A N   
614  C CA  . TYR A 78  ? 0.5372 0.4826 0.3814 0.1008  0.0286  -0.0216 77  TYR A CA  
615  C C   . TYR A 78  ? 0.4830 0.4404 0.3336 0.0966  0.0341  -0.0155 77  TYR A C   
616  O O   . TYR A 78  ? 0.4694 0.4317 0.3108 0.1044  0.0413  -0.0134 77  TYR A O   
617  C CB  . TYR A 78  ? 0.6108 0.5331 0.4354 0.1010  0.0151  -0.0278 77  TYR A CB  
618  C CG  . TYR A 78  ? 0.6740 0.5818 0.4928 0.1037  0.0074  -0.0337 77  TYR A CG  
619  C CD1 . TYR A 78  ? 0.7116 0.6097 0.5131 0.1173  0.0086  -0.0392 77  TYR A CD1 
620  C CD2 . TYR A 78  ? 0.7124 0.6163 0.5431 0.0931  -0.0011 -0.0334 77  TYR A CD2 
621  C CE1 . TYR A 78  ? 0.7567 0.6404 0.5533 0.1201  0.0009  -0.0446 77  TYR A CE1 
622  C CE2 . TYR A 78  ? 0.7683 0.6587 0.5944 0.0951  -0.0087 -0.0380 77  TYR A CE2 
623  C CZ  . TYR A 78  ? 0.8221 0.7018 0.6313 0.1086  -0.0080 -0.0436 77  TYR A CZ  
624  O OH  . TYR A 78  ? 0.9019 0.7670 0.7069 0.1109  -0.0161 -0.0481 77  TYR A OH  
625  N N   . ASP A 79  ? 0.4450 0.4072 0.3113 0.0844  0.0305  -0.0124 78  ASP A N   
626  C CA  . ASP A 79  ? 0.4222 0.3966 0.2992 0.0789  0.0352  -0.0063 78  ASP A CA  
627  C C   . ASP A 79  ? 0.4217 0.3861 0.2950 0.0710  0.0245  -0.0071 78  ASP A C   
628  O O   . ASP A 79  ? 0.4037 0.3702 0.2912 0.0611  0.0197  -0.0066 78  ASP A O   
629  C CB  . ASP A 79  ? 0.4421 0.4346 0.3450 0.0722  0.0422  -0.0016 78  ASP A CB  
630  C CG  . ASP A 79  ? 0.4797 0.4842 0.3950 0.0669  0.0468  0.0046  78  ASP A CG  
631  O OD1 . ASP A 79  ? 0.5421 0.5527 0.4528 0.0728  0.0541  0.0085  78  ASP A OD1 
632  O OD2 . ASP A 79  ? 0.3863 0.3946 0.3161 0.0570  0.0433  0.0058  78  ASP A OD2 
633  N N   . ILE A 80  ? 0.4036 0.3580 0.2581 0.0753  0.0209  -0.0082 79  ILE A N   
634  C CA  . ILE A 80  ? 0.4128 0.3566 0.2620 0.0685  0.0098  -0.0090 79  ILE A CA  
635  C C   . ILE A 80  ? 0.3761 0.3319 0.2371 0.0629  0.0136  -0.0025 79  ILE A C   
636  O O   . ILE A 80  ? 0.3876 0.3464 0.2402 0.0683  0.0186  0.0004  79  ILE A O   
637  C CB  . ILE A 80  ? 0.5186 0.4433 0.3402 0.0760  0.0021  -0.0143 79  ILE A CB  
638  C CG1 . ILE A 80  ? 0.5759 0.4864 0.3876 0.0802  -0.0040 -0.0212 79  ILE A CG1 
639  C CG2 . ILE A 80  ? 0.5369 0.4527 0.3536 0.0690  -0.0087 -0.0138 79  ILE A CG2 
640  C CD1 . ILE A 80  ? 0.6368 0.5264 0.4209 0.0878  -0.0129 -0.0276 79  ILE A CD1 
641  N N   . ASP A 81  ? 0.3491 0.3121 0.2297 0.0524  0.0113  0.0000  80  ASP A N   
642  C CA  . ASP A 81  ? 0.3706 0.3455 0.2656 0.0468  0.0148  0.0059  80  ASP A CA  
643  C C   . ASP A 81  ? 0.3848 0.3510 0.2739 0.0416  0.0046  0.0061  80  ASP A C   
644  O O   . ASP A 81  ? 0.3732 0.3326 0.2639 0.0356  -0.0045 0.0036  80  ASP A O   
645  C CB  . ASP A 81  ? 0.3085 0.2974 0.2288 0.0392  0.0190  0.0080  80  ASP A CB  
646  C CG  . ASP A 81  ? 0.3061 0.3045 0.2338 0.0436  0.0285  0.0083  80  ASP A CG  
647  O OD1 . ASP A 81  ? 0.3498 0.3533 0.2733 0.0504  0.0365  0.0111  80  ASP A OD1 
648  O OD2 . ASP A 81  ? 0.3165 0.3178 0.2545 0.0400  0.0279  0.0061  80  ASP A OD2 
649  N N   . VAL A 82  ? 0.3577 0.3249 0.2406 0.0437  0.0059  0.0099  81  VAL A N   
650  C CA  . VAL A 82  ? 0.3498 0.3104 0.2284 0.0388  -0.0034 0.0111  81  VAL A CA  
651  C C   . VAL A 82  ? 0.3607 0.3328 0.2503 0.0367  0.0018  0.0179  81  VAL A C   
652  O O   . VAL A 82  ? 0.3521 0.3326 0.2432 0.0417  0.0114  0.0215  81  VAL A O   
653  C CB  . VAL A 82  ? 0.3988 0.3420 0.2498 0.0450  -0.0113 0.0072  81  VAL A CB  
654  C CG1 . VAL A 82  ? 0.4243 0.3541 0.2647 0.0467  -0.0179 0.0003  81  VAL A CG1 
655  C CG2 . VAL A 82  ? 0.4487 0.3935 0.2849 0.0551  -0.0033 0.0088  81  VAL A CG2 
656  N N   . GLY A 83  ? 0.3554 0.3282 0.2538 0.0294  -0.0048 0.0201  82  GLY A N   
657  C CA  . GLY A 83  ? 0.3388 0.3200 0.2464 0.0273  -0.0021 0.0265  82  GLY A CA  
658  C C   . GLY A 83  ? 0.3752 0.3458 0.2654 0.0284  -0.0107 0.0275  82  GLY A C   
659  O O   . GLY A 83  ? 0.3592 0.3180 0.2389 0.0264  -0.0209 0.0236  82  GLY A O   
660  N N   . ILE A 84  ? 0.3927 0.3674 0.2799 0.0314  -0.0068 0.0330  83  ILE A N   
661  C CA  . ILE A 84  ? 0.4401 0.4064 0.3124 0.0320  -0.0148 0.0350  83  ILE A CA  
662  C C   . ILE A 84  ? 0.4032 0.3799 0.2918 0.0279  -0.0129 0.0426  83  ILE A C   
663  O O   . ILE A 84  ? 0.4100 0.3968 0.3070 0.0302  -0.0034 0.0476  83  ILE A O   
664  C CB  . ILE A 84  ? 0.4338 0.3919 0.2790 0.0417  -0.0134 0.0338  83  ILE A CB  
665  C CG1 . ILE A 84  ? 0.4474 0.4170 0.2957 0.0477  -0.0001 0.0384  83  ILE A CG1 
666  C CG2 . ILE A 84  ? 0.4306 0.3748 0.2577 0.0458  -0.0185 0.0253  83  ILE A CG2 
667  C CD1 . ILE A 84  ? 0.4462 0.4106 0.2685 0.0574  0.0020  0.0391  83  ILE A CD1 
668  N N   . ILE A 85  ? 0.3778 0.3523 0.2720 0.0216  -0.0221 0.0437  84  ILE A N   
669  C CA  . ILE A 85  ? 0.3410 0.3240 0.2505 0.0178  -0.0219 0.0506  84  ILE A CA  
670  C C   . ILE A 85  ? 0.3576 0.3334 0.2481 0.0212  -0.0272 0.0542  84  ILE A C   
671  O O   . ILE A 85  ? 0.3947 0.3603 0.2731 0.0194  -0.0381 0.0520  84  ILE A O   
672  C CB  . ILE A 85  ? 0.3630 0.3496 0.2911 0.0094  -0.0286 0.0501  84  ILE A CB  
673  C CG1 . ILE A 85  ? 0.3532 0.3454 0.2959 0.0064  -0.0247 0.0455  84  ILE A CG1 
674  C CG2 . ILE A 85  ? 0.3675 0.3636 0.3133 0.0065  -0.0273 0.0570  84  ILE A CG2 
675  C CD1 . ILE A 85  ? 0.3170 0.3115 0.2730 -0.0012 -0.0322 0.0442  84  ILE A CD1 
676  N N   . LEU A 86  ? 0.3896 0.3706 0.2769 0.0259  -0.0198 0.0600  85  LEU A N   
677  C CA  . LEU A 86  ? 0.4677 0.4434 0.3370 0.0293  -0.0242 0.0643  85  LEU A CA  
678  C C   . LEU A 86  ? 0.4710 0.4503 0.3543 0.0232  -0.0305 0.0701  85  LEU A C   
679  O O   . LEU A 86  ? 0.4403 0.4296 0.3487 0.0185  -0.0272 0.0731  85  LEU A O   
680  C CB  . LEU A 86  ? 0.5384 0.5201 0.4002 0.0363  -0.0138 0.0697  85  LEU A CB  
681  C CG  . LEU A 86  ? 0.6469 0.6224 0.4846 0.0449  -0.0099 0.0647  85  LEU A CG  
682  C CD1 . LEU A 86  ? 0.6707 0.6491 0.5179 0.0452  -0.0037 0.0589  85  LEU A CD1 
683  C CD2 . LEU A 86  ? 0.6713 0.6529 0.4980 0.0519  -0.0017 0.0716  85  LEU A CD2 
684  N N   . ASN A 87  ? 0.4770 0.4477 0.3435 0.0237  -0.0400 0.0713  86  ASN A N   
685  C CA  . ASN A 87  ? 0.4662 0.4394 0.3436 0.0184  -0.0474 0.0770  86  ASN A CA  
686  C C   . ASN A 87  ? 0.4627 0.4441 0.3451 0.0208  -0.0413 0.0865  86  ASN A C   
687  O O   . ASN A 87  ? 0.4571 0.4349 0.3257 0.0227  -0.0462 0.0914  86  ASN A O   
688  C CB  . ASN A 87  ? 0.5492 0.5095 0.4063 0.0177  -0.0609 0.0746  86  ASN A CB  
689  C CG  . ASN A 87  ? 0.5907 0.5537 0.4601 0.0117  -0.0699 0.0801  86  ASN A CG  
690  O OD1 . ASN A 87  ? 0.5828 0.5561 0.4783 0.0068  -0.0678 0.0830  86  ASN A OD1 
691  N ND2 . ASN A 87  ? 0.6215 0.5752 0.4716 0.0125  -0.0801 0.0814  86  ASN A ND2 
692  N N   . ILE A 88  ? 0.4335 0.4259 0.3360 0.0204  -0.0309 0.0894  87  ILE A N   
693  C CA  . ILE A 88  ? 0.4331 0.4336 0.3428 0.0223  -0.0243 0.0989  87  ILE A CA  
694  C C   . ILE A 88  ? 0.4184 0.4292 0.3599 0.0172  -0.0204 0.1017  87  ILE A C   
695  O O   . ILE A 88  ? 0.4081 0.4214 0.3641 0.0139  -0.0194 0.0958  87  ILE A O   
696  C CB  . ILE A 88  ? 0.4357 0.4389 0.3331 0.0291  -0.0138 0.1005  87  ILE A CB  
697  C CG1 . ILE A 88  ? 0.4368 0.4450 0.3473 0.0287  -0.0055 0.0952  87  ILE A CG1 
698  C CG2 . ILE A 88  ? 0.4995 0.4926 0.3641 0.0354  -0.0171 0.0970  87  ILE A CG2 
699  C CD1 . ILE A 88  ? 0.4699 0.4815 0.3690 0.0354  0.0046  0.0962  87  ILE A CD1 
700  N N   . ALA A 89  ? 0.4178 0.4342 0.3694 0.0170  -0.0186 0.1110  88  ALA A N   
701  C CA  . ALA A 89  ? 0.4066 0.4319 0.3875 0.0133  -0.0146 0.1143  88  ALA A CA  
702  C C   . ALA A 89  ? 0.3937 0.4256 0.3814 0.0157  -0.0032 0.1168  88  ALA A C   
703  O O   . ALA A 89  ? 0.4265 0.4596 0.4020 0.0198  0.0013  0.1232  88  ALA A O   
704  C CB  . ALA A 89  ? 0.4246 0.4519 0.4144 0.0117  -0.0194 0.1234  88  ALA A CB  
705  N N   . LYS A 90  ? 0.3575 0.3944 0.3648 0.0131  0.0013  0.1122  89  LYS A N   
706  C CA  . LYS A 90  ? 0.3969 0.4398 0.4104 0.0149  0.0115  0.1136  89  LYS A CA  
707  C C   . LYS A 90  ? 0.3805 0.4290 0.4044 0.0153  0.0157  0.1248  89  LYS A C   
708  O O   . LYS A 90  ? 0.3579 0.4107 0.3772 0.0184  0.0233  0.1295  89  LYS A O   
709  C CB  . LYS A 90  ? 0.3883 0.4352 0.4214 0.0115  0.0144  0.1063  89  LYS A CB  
710  C CG  . LYS A 90  ? 0.4018 0.4533 0.4618 0.0072  0.0130  0.1079  89  LYS A CG  
711  C CD  . LYS A 90  ? 0.3922 0.4476 0.4681 0.0045  0.0157  0.0996  89  LYS A CD  
712  C CE  . LYS A 90  ? 0.4066 0.4665 0.5085 0.0013  0.0146  0.1003  89  LYS A CE  
713  N NZ  . LYS A 90  ? 0.4259 0.4883 0.5388 0.0018  0.0181  0.1095  89  LYS A NZ  
714  N N   . ASP A 91  ? 0.3792 0.4283 0.4174 0.0123  0.0107  0.1298  90  ASP A N   
715  C CA  . ASP A 91  ? 0.4040 0.4578 0.4537 0.0122  0.0137  0.1411  90  ASP A CA  
716  C C   . ASP A 91  ? 0.4616 0.5144 0.4903 0.0161  0.0136  0.1501  90  ASP A C   
717  O O   . ASP A 91  ? 0.4991 0.5567 0.5340 0.0165  0.0176  0.1606  90  ASP A O   
718  C CB  . ASP A 91  ? 0.4330 0.4870 0.5047 0.0085  0.0079  0.1435  90  ASP A CB  
719  C CG  . ASP A 91  ? 0.4784 0.5351 0.5729 0.0053  0.0092  0.1357  90  ASP A CG  
720  O OD1 . ASP A 91  ? 0.4918 0.5515 0.5898 0.0054  0.0159  0.1317  90  ASP A OD1 
721  O OD2 . ASP A 91  ? 0.5076 0.5639 0.6163 0.0030  0.0036  0.1337  90  ASP A OD2 
722  N N   . ASP A 92  ? 0.4604 0.5069 0.4643 0.0187  0.0088  0.1465  91  ASP A N   
723  C CA  . ASP A 92  ? 0.5017 0.5468 0.4826 0.0230  0.0083  0.1539  91  ASP A CA  
724  C C   . ASP A 92  ? 0.5218 0.5697 0.4849 0.0286  0.0170  0.1538  91  ASP A C   
725  O O   . ASP A 92  ? 0.5832 0.6317 0.5266 0.0330  0.0182  0.1603  91  ASP A O   
726  C CB  . ASP A 92  ? 0.5515 0.5878 0.5131 0.0236  -0.0020 0.1498  91  ASP A CB  
727  C CG  . ASP A 92  ? 0.5714 0.6065 0.5480 0.0191  -0.0107 0.1532  91  ASP A CG  
728  O OD1 . ASP A 92  ? 0.5614 0.6020 0.5607 0.0166  -0.0087 0.1600  91  ASP A OD1 
729  O OD2 . ASP A 92  ? 0.5977 0.6263 0.5639 0.0182  -0.0200 0.1492  91  ASP A OD2 
730  N N   . HIS A 93  ? 0.4651 0.5154 0.4344 0.0288  0.0231  0.1467  92  HIS A N   
731  C CA  . HIS A 93  ? 0.4429 0.4953 0.3941 0.0347  0.0306  0.1452  92  HIS A CA  
732  C C   . HIS A 93  ? 0.4387 0.4991 0.4085 0.0335  0.0396  0.1444  92  HIS A C   
733  O O   . HIS A 93  ? 0.4239 0.4849 0.4157 0.0284  0.0385  0.1400  92  HIS A O   
734  C CB  . HIS A 93  ? 0.4621 0.5048 0.3900 0.0380  0.0261  0.1337  92  HIS A CB  
735  C CG  . HIS A 93  ? 0.5169 0.5504 0.4273 0.0383  0.0157  0.1330  92  HIS A CG  
736  N ND1 . HIS A 93  ? 0.5725 0.6049 0.4603 0.0433  0.0148  0.1392  92  HIS A ND1 
737  C CD2 . HIS A 93  ? 0.5198 0.5456 0.4322 0.0342  0.0054  0.1273  92  HIS A CD2 
738  C CE1 . HIS A 93  ? 0.5819 0.6053 0.4583 0.0420  0.0040  0.1368  92  HIS A CE1 
739  N NE2 . HIS A 93  ? 0.5636 0.5831 0.4551 0.0364  -0.0019 0.1299  92  HIS A NE2 
740  N N   . ASP A 94  ? 0.4275 0.4945 0.3879 0.0385  0.0483  0.1486  93  ASP A N   
741  C CA  . ASP A 94  ? 0.4527 0.5277 0.4278 0.0382  0.0568  0.1476  93  ASP A CA  
742  C C   . ASP A 94  ? 0.4426 0.5133 0.4075 0.0408  0.0577  0.1356  93  ASP A C   
743  O O   . ASP A 94  ? 0.4486 0.5128 0.3881 0.0463  0.0556  0.1305  93  ASP A O   
744  C CB  . ASP A 94  ? 0.5133 0.5971 0.4859 0.0418  0.0634  0.1525  93  ASP A CB  
745  C CG  . ASP A 94  ? 0.5500 0.6423 0.5392 0.0412  0.0705  0.1510  93  ASP A CG  
746  O OD1 . ASP A 94  ? 0.5718 0.6689 0.5862 0.0358  0.0709  0.1550  93  ASP A OD1 
747  O OD2 . ASP A 94  ? 0.5547 0.6483 0.5320 0.0463  0.0749  0.1453  93  ASP A OD2 
748  N N   . PRO A 95  ? 0.4299 0.5032 0.4139 0.0371  0.0600  0.1303  94  PRO A N   
749  C CA  . PRO A 95  ? 0.4486 0.5175 0.4241 0.0392  0.0600  0.1187  94  PRO A CA  
750  C C   . PRO A 95  ? 0.4726 0.5436 0.4270 0.0474  0.0666  0.1183  94  PRO A C   
751  O O   . PRO A 95  ? 0.4756 0.5381 0.4097 0.0517  0.0635  0.1099  94  PRO A O   
752  C CB  . PRO A 95  ? 0.4716 0.5460 0.4734 0.0338  0.0630  0.1160  94  PRO A CB  
753  C CG  . PRO A 95  ? 0.4723 0.5501 0.4958 0.0282  0.0611  0.1232  94  PRO A CG  
754  C CD  . PRO A 95  ? 0.4451 0.5251 0.4589 0.0310  0.0622  0.1345  94  PRO A CD  
755  N N   . VAL A 96  ? 0.4702 0.5517 0.4313 0.0494  0.0740  0.1251  95  VAL A N   
756  C CA  . VAL A 96  ? 0.4782 0.5622 0.4233 0.0570  0.0787  0.1221  95  VAL A CA  
757  C C   . VAL A 96  ? 0.5072 0.5847 0.4246 0.0628  0.0755  0.1222  95  VAL A C   
758  O O   . VAL A 96  ? 0.5209 0.5942 0.4181 0.0697  0.0763  0.1156  95  VAL A O   
759  C CB  . VAL A 96  ? 0.4658 0.5620 0.4278 0.0566  0.0847  0.1283  95  VAL A CB  
760  C CG1 . VAL A 96  ? 0.4221 0.5219 0.3691 0.0646  0.0896  0.1258  95  VAL A CG1 
761  C CG2 . VAL A 96  ? 0.4720 0.5724 0.4602 0.0506  0.0859  0.1265  95  VAL A CG2 
762  N N   . GLU A 97  ? 0.5036 0.5792 0.4200 0.0601  0.0709  0.1288  96  GLU A N   
763  C CA  . GLU A 97  ? 0.5093 0.5776 0.3992 0.0648  0.0662  0.1281  96  GLU A CA  
764  C C   . GLU A 97  ? 0.4765 0.5308 0.3456 0.0673  0.0592  0.1182  96  GLU A C   
765  O O   . GLU A 97  ? 0.5064 0.5543 0.3513 0.0739  0.0576  0.1121  96  GLU A O   
766  C CB  . GLU A 97  ? 0.5305 0.5992 0.4264 0.0603  0.0615  0.1372  96  GLU A CB  
767  C CG  . GLU A 97  ? 0.6081 0.6669 0.4787 0.0631  0.0537  0.1358  96  GLU A CG  
768  C CD  . GLU A 97  ? 0.6970 0.7540 0.5768 0.0572  0.0468  0.1433  96  GLU A CD  
769  O OE1 . GLU A 97  ? 0.7082 0.7722 0.6141 0.0515  0.0488  0.1501  96  GLU A OE1 
770  O OE2 . GLU A 97  ? 0.7397 0.7878 0.6015 0.0582  0.0386  0.1420  96  GLU A OE2 
771  N N   . VAL A 98  ? 0.4378 0.4870 0.3178 0.0617  0.0540  0.1154  97  VAL A N   
772  C CA  . VAL A 98  ? 0.4563 0.4914 0.3225 0.0617  0.0448  0.1037  97  VAL A CA  
773  C C   . VAL A 98  ? 0.4936 0.5263 0.3498 0.0673  0.0488  0.0949  97  VAL A C   
774  O O   . VAL A 98  ? 0.5248 0.5463 0.3569 0.0726  0.0440  0.0872  97  VAL A O   
775  C CB  . VAL A 98  ? 0.4327 0.4644 0.3205 0.0523  0.0373  0.1005  97  VAL A CB  
776  C CG1 . VAL A 98  ? 0.4115 0.4299 0.2873 0.0514  0.0276  0.0896  97  VAL A CG1 
777  C CG2 . VAL A 98  ? 0.4245 0.4585 0.3220 0.0478  0.0332  0.1093  97  VAL A CG2 
778  N N   . LYS A 99  ? 0.4813 0.5238 0.3560 0.0661  0.0571  0.0957  98  LYS A N   
779  C CA  . LYS A 99  ? 0.4968 0.5383 0.3628 0.0719  0.0615  0.0885  98  LYS A CA  
780  C C   . LYS A 99  ? 0.5236 0.5659 0.3692 0.0812  0.0654  0.0879  98  LYS A C   
781  O O   . LYS A 99  ? 0.5196 0.5546 0.3494 0.0872  0.0645  0.0790  98  LYS A O   
782  C CB  . LYS A 99  ? 0.4907 0.5437 0.3822 0.0684  0.0693  0.0902  98  LYS A CB  
783  C CG  . LYS A 99  ? 0.4465 0.4954 0.3566 0.0601  0.0635  0.0835  98  LYS A CG  
784  C CD  . LYS A 99  ? 0.4427 0.5014 0.3734 0.0580  0.0706  0.0832  98  LYS A CD  
785  C CE  . LYS A 99  ? 0.4721 0.5442 0.4240 0.0547  0.0773  0.0939  98  LYS A CE  
786  N NZ  . LYS A 99  ? 0.4458 0.5258 0.4193 0.0514  0.0817  0.0921  98  LYS A NZ  
787  N N   . LYS A 100 ? 0.5111 0.5614 0.3589 0.0817  0.0686  0.0960  99  LYS A N   
788  C CA  . LYS A 100 ? 0.4971 0.5485 0.3273 0.0898  0.0713  0.0947  99  LYS A CA  
789  C C   . LYS A 100 ? 0.4973 0.5339 0.2994 0.0936  0.0626  0.0884  99  LYS A C   
790  O O   . LYS A 100 ? 0.5058 0.5376 0.2897 0.1013  0.0628  0.0817  99  LYS A O   
791  C CB  . LYS A 100 ? 0.4974 0.5619 0.3378 0.0889  0.0767  0.1057  99  LYS A CB  
792  C CG  . LYS A 100 ? 0.5176 0.5851 0.3404 0.0974  0.0802  0.1054  99  LYS A CG  
793  C CD  . LYS A 100 ? 0.5523 0.6332 0.3854 0.0960  0.0851  0.1171  99  LYS A CD  
794  C CE  . LYS A 100 ? 0.6083 0.6929 0.4231 0.1048  0.0887  0.1170  99  LYS A CE  
795  N NZ  . LYS A 100 ? 0.6630 0.7495 0.4750 0.1116  0.0935  0.1102  99  LYS A NZ  
796  N N   . TRP A 101 ? 0.5464 0.5756 0.3459 0.0884  0.0542  0.0904  100 TRP A N   
797  C CA  . TRP A 101 ? 0.5772 0.5902 0.3520 0.0906  0.0436  0.0829  100 TRP A CA  
798  C C   . TRP A 101 ? 0.5803 0.5825 0.3441 0.0946  0.0410  0.0709  100 TRP A C   
799  O O   . TRP A 101 ? 0.5938 0.5873 0.3369 0.1012  0.0382  0.0634  100 TRP A O   
800  C CB  . TRP A 101 ? 0.6085 0.6148 0.3873 0.0832  0.0338  0.0858  100 TRP A CB  
801  C CG  . TRP A 101 ? 0.6326 0.6460 0.4207 0.0788  0.0335  0.0969  100 TRP A CG  
802  C CD1 . TRP A 101 ? 0.6493 0.6724 0.4376 0.0809  0.0395  0.1042  100 TRP A CD1 
803  C CD2 . TRP A 101 ? 0.6404 0.6519 0.4400 0.0716  0.0262  0.1022  100 TRP A CD2 
804  N NE1 . TRP A 101 ? 0.6394 0.6658 0.4383 0.0752  0.0362  0.1136  100 TRP A NE1 
805  C CE2 . TRP A 101 ? 0.6344 0.6539 0.4410 0.0695  0.0281  0.1124  100 TRP A CE2 
806  C CE3 . TRP A 101 ? 0.6345 0.6384 0.4457 0.0645  0.0173  0.0966  100 TRP A CE3 
807  C CZ2 . TRP A 101 ? 0.6389 0.6589 0.4589 0.0630  0.0220  0.1197  100 TRP A CZ2 
808  C CZ3 . TRP A 101 ? 0.6374 0.6426 0.4649 0.0570  0.0114  0.1020  100 TRP A CZ3 
809  C CH2 . TRP A 101 ? 0.6347 0.6476 0.4659 0.0568  0.0137  0.1137  100 TRP A CH2 
810  N N   . ILE A 102 ? 0.5505 0.5531 0.3287 0.0907  0.0417  0.0691  101 ILE A N   
811  C CA  . ILE A 102 ? 0.5463 0.5376 0.3152 0.0935  0.0379  0.0580  101 ILE A CA  
812  C C   . ILE A 102 ? 0.5819 0.5773 0.3463 0.1018  0.0457  0.0536  101 ILE A C   
813  O O   . ILE A 102 ? 0.5910 0.5745 0.3380 0.1075  0.0412  0.0442  101 ILE A O   
814  C CB  . ILE A 102 ? 0.4634 0.4559 0.2542 0.0856  0.0366  0.0567  101 ILE A CB  
815  C CG1 . ILE A 102 ? 0.4477 0.4364 0.2502 0.0756  0.0270  0.0587  101 ILE A CG1 
816  C CG2 . ILE A 102 ? 0.4539 0.4351 0.2370 0.0878  0.0325  0.0455  101 ILE A CG2 
817  C CD1 . ILE A 102 ? 0.4117 0.3837 0.1922 0.0761  0.0141  0.0531  101 ILE A CD1 
818  N N   . ARG A 103 ? 0.6099 0.6219 0.3911 0.1025  0.0566  0.0606  102 ARG A N   
819  C CA  . ARG A 103 ? 0.6465 0.6640 0.4263 0.1101  0.0638  0.0577  102 ARG A CA  
820  C C   . ARG A 103 ? 0.6584 0.6715 0.4157 0.1184  0.0626  0.0551  102 ARG A C   
821  O O   . ARG A 103 ? 0.6404 0.6474 0.3855 0.1259  0.0624  0.0473  102 ARG A O   
822  C CB  . ARG A 103 ? 0.6862 0.7227 0.4903 0.1079  0.0741  0.0668  102 ARG A CB  
823  C CG  . ARG A 103 ? 0.7497 0.7930 0.5568 0.1145  0.0808  0.0644  102 ARG A CG  
824  C CD  . ARG A 103 ? 0.8010 0.8613 0.6208 0.1154  0.0890  0.0743  102 ARG A CD  
825  N NE  . ARG A 103 ? 0.8447 0.9054 0.6475 0.1202  0.0889  0.0773  102 ARG A NE  
826  C CZ  . ARG A 103 ? 0.9320 0.9906 0.7169 0.1297  0.0902  0.0732  102 ARG A CZ  
827  N NH1 . ARG A 103 ? 0.9515 1.0073 0.7335 0.1354  0.0914  0.0661  102 ARG A NH1 
828  N NH2 . ARG A 103 ? 0.9876 1.0473 0.7577 0.1334  0.0900  0.0762  102 ARG A NH2 
829  N N   . ASP A 104 ? 0.6851 0.7015 0.4373 0.1172  0.0618  0.0617  103 ASP A N   
830  C CA  . ASP A 104 ? 0.7140 0.7262 0.4440 0.1245  0.0602  0.0593  103 ASP A CA  
831  C C   . ASP A 104 ? 0.7175 0.7093 0.4251 0.1268  0.0490  0.0482  103 ASP A C   
832  O O   . ASP A 104 ? 0.7328 0.7183 0.4219 0.1350  0.0477  0.0420  103 ASP A O   
833  C CB  . ASP A 104 ? 0.7002 0.7198 0.4303 0.1215  0.0608  0.0693  103 ASP A CB  
834  C CG  . ASP A 104 ? 0.6907 0.7302 0.4415 0.1201  0.0716  0.0805  103 ASP A CG  
835  O OD1 . ASP A 104 ? 0.6679 0.7158 0.4328 0.1217  0.0784  0.0805  103 ASP A OD1 
836  O OD2 . ASP A 104 ? 0.6924 0.7387 0.4459 0.1172  0.0724  0.0896  103 ASP A OD2 
837  N N   . ALA A 105 ? 0.6934 0.6747 0.4032 0.1196  0.0402  0.0457  104 ALA A N   
838  C CA  . ALA A 105 ? 0.6960 0.6574 0.3875 0.1206  0.0282  0.0350  104 ALA A CA  
839  C C   . ALA A 105 ? 0.6930 0.6476 0.3791 0.1275  0.0292  0.0254  104 ALA A C   
840  O O   . ALA A 105 ? 0.6903 0.6310 0.3575 0.1330  0.0227  0.0169  104 ALA A O   
841  C CB  . ALA A 105 ? 0.6594 0.6131 0.3584 0.1109  0.0190  0.0351  104 ALA A CB  
842  N N   . LEU A 106 ? 0.6824 0.6464 0.3858 0.1272  0.0371  0.0269  105 LEU A N   
843  C CA  . LEU A 106 ? 0.7118 0.6707 0.4134 0.1331  0.0383  0.0190  105 LEU A CA  
844  C C   . LEU A 106 ? 0.7662 0.7377 0.4691 0.1420  0.0489  0.0213  105 LEU A C   
845  O O   . LEU A 106 ? 0.7658 0.7388 0.4743 0.1460  0.0525  0.0177  105 LEU A O   
846  C CB  . LEU A 106 ? 0.6662 0.6274 0.3862 0.1269  0.0393  0.0189  105 LEU A CB  
847  C CG  . LEU A 106 ? 0.6828 0.6310 0.4021 0.1186  0.0283  0.0156  105 LEU A CG  
848  C CD1 . LEU A 106 ? 0.6474 0.6033 0.3876 0.1123  0.0321  0.0183  105 LEU A CD1 
849  C CD2 . LEU A 106 ? 0.7050 0.6326 0.4066 0.1217  0.0172  0.0045  105 LEU A CD2 
850  N N   . LYS A 107 ? 0.8298 0.8106 0.5278 0.1449  0.0535  0.0275  106 LYS A N   
851  C CA  . LYS A 107 ? 0.9159 0.9116 0.6182 0.1522  0.0640  0.0317  106 LYS A CA  
852  C C   . LYS A 107 ? 0.9972 0.9848 0.6855 0.1626  0.0633  0.0226  106 LYS A C   
853  O O   . LYS A 107 ? 0.9811 0.9786 0.6788 0.1672  0.0707  0.0240  106 LYS A O   
854  C CB  . LYS A 107 ? 0.9441 0.9490 0.6401 0.1536  0.0674  0.0394  106 LYS A CB  
855  C CG  . LYS A 107 ? 0.9639 0.9897 0.6737 0.1563  0.0791  0.0487  106 LYS A CG  
856  C CD  . LYS A 107 ? 0.9896 1.0241 0.6942 0.1561  0.0815  0.0572  106 LYS A CD  
857  C CE  . LYS A 107 ? 0.9891 1.0445 0.7084 0.1582  0.0925  0.0673  106 LYS A CE  
858  N NZ  . LYS A 107 ? 0.9887 1.0526 0.7027 0.1579  0.0946  0.0760  106 LYS A NZ  
859  N N   . ASP A 108 ? 1.0773 1.0464 0.7439 0.1662  0.0537  0.0135  107 ASP A N   
860  C CA  . ASP A 108 ? 1.1253 1.0848 0.7764 0.1768  0.0518  0.0047  107 ASP A CA  
861  C C   . ASP A 108 ? 1.0637 1.0048 0.7120 0.1755  0.0426  -0.0050 107 ASP A C   
862  O O   . ASP A 108 ? 1.0719 0.9978 0.7029 0.1824  0.0361  -0.0139 107 ASP A O   
863  C CB  . ASP A 108 ? 1.2381 1.1904 0.8654 0.1833  0.0479  0.0017  107 ASP A CB  
864  C CG  . ASP A 108 ? 1.3177 1.2878 0.9466 0.1844  0.0564  0.0117  107 ASP A CG  
865  O OD1 . ASP A 108 ? 1.3336 1.3219 0.9778 0.1859  0.0671  0.0189  107 ASP A OD1 
866  O OD2 . ASP A 108 ? 1.3554 1.3215 0.9711 0.1831  0.0520  0.0127  107 ASP A OD2 
867  N N   . TYR A 109 ? 1.0030 0.9453 0.6684 0.1667  0.0418  -0.0033 108 TYR A N   
868  C CA  . TYR A 109 ? 0.9465 0.8731 0.6117 0.1642  0.0334  -0.0113 108 TYR A CA  
869  C C   . TYR A 109 ? 0.9124 0.8480 0.5935 0.1661  0.0406  -0.0106 108 TYR A C   
870  O O   . TYR A 109 ? 0.8896 0.8418 0.5907 0.1610  0.0487  -0.0029 108 TYR A O   
871  C CB  . TYR A 109 ? 0.9006 0.8211 0.5723 0.1525  0.0260  -0.0102 108 TYR A CB  
872  C CG  . TYR A 109 ? 0.8887 0.7918 0.5590 0.1490  0.0157  -0.0182 108 TYR A CG  
873  C CD1 . TYR A 109 ? 0.8866 0.7689 0.5398 0.1492  0.0027  -0.0258 108 TYR A CD1 
874  C CD2 . TYR A 109 ? 0.8974 0.8051 0.5845 0.1449  0.0185  -0.0177 108 TYR A CD2 
875  C CE1 . TYR A 109 ? 0.8915 0.7580 0.5450 0.1452  -0.0074 -0.0322 108 TYR A CE1 
876  C CE2 . TYR A 109 ? 0.8968 0.7890 0.5829 0.1413  0.0089  -0.0244 108 TYR A CE2 
877  C CZ  . TYR A 109 ? 0.9098 0.7814 0.5795 0.1413  -0.0042 -0.0314 108 TYR A CZ  
878  O OH  . TYR A 109 ? 0.9078 0.7642 0.5782 0.1368  -0.0145 -0.0371 108 TYR A OH  
879  N N   . GLY A 110 ? 0.9054 0.8302 0.5781 0.1732  0.0372  -0.0183 109 GLY A N   
880  C CA  . GLY A 110 ? 0.8965 0.8281 0.5831 0.1749  0.0424  -0.0183 109 GLY A CA  
881  C C   . GLY A 110 ? 0.8968 0.8507 0.5961 0.1784  0.0553  -0.0100 109 GLY A C   
882  O O   . GLY A 110 ? 0.9173 0.8788 0.6087 0.1843  0.0600  -0.0068 109 GLY A O   
883  N N   . ASN A 111 ? 0.9165 0.8816 0.6366 0.1743  0.0607  -0.0063 110 ASN A N   
884  C CA  . ASN A 111 ? 0.9275 0.9137 0.6628 0.1759  0.0719  0.0020  110 ASN A CA  
885  C C   . ASN A 111 ? 0.9074 0.9086 0.6538 0.1696  0.0776  0.0118  110 ASN A C   
886  O O   . ASN A 111 ? 0.9394 0.9582 0.6997 0.1699  0.0861  0.0196  110 ASN A O   
887  C CB  . ASN A 111 ? 0.9681 0.9608 0.7230 0.1722  0.0747  0.0029  110 ASN A CB  
888  C CG  . ASN A 111 ? 1.0398 1.0179 0.7853 0.1777  0.0688  -0.0062 110 ASN A CG  
889  O OD1 . ASN A 111 ? 1.0804 1.0396 0.8086 0.1799  0.0596  -0.0140 110 ASN A OD1 
890  N ND2 . ASN A 111 ? 1.0409 1.0274 0.7983 0.1797  0.0734  -0.0049 110 ASN A ND2 
891  N N   . GLY A 112 ? 0.8578 0.8522 0.5990 0.1638  0.0726  0.0120  111 GLY A N   
892  C CA  . GLY A 112 ? 0.8329 0.8399 0.5837 0.1578  0.0770  0.0213  111 GLY A CA  
893  C C   . GLY A 112 ? 0.8024 0.8084 0.5666 0.1465  0.0741  0.0234  111 GLY A C   
894  O O   . GLY A 112 ? 0.8017 0.7974 0.5672 0.1431  0.0685  0.0176  111 GLY A O   
895  N N   . ALA A 113 ? 0.7351 0.7523 0.5094 0.1408  0.0778  0.0322  112 ALA A N   
896  C CA  . ALA A 113 ? 0.6744 0.6929 0.4626 0.1303  0.0759  0.0357  112 ALA A CA  
897  C C   . ALA A 113 ? 0.6596 0.6968 0.4688 0.1255  0.0837  0.0470  112 ALA A C   
898  O O   . ALA A 113 ? 0.6887 0.7347 0.4953 0.1295  0.0884  0.0526  112 ALA A O   
899  C CB  . ALA A 113 ? 0.6412 0.6464 0.4135 0.1275  0.0673  0.0333  112 ALA A CB  
900  N N   . GLU A 114 ? 0.5917 0.6344 0.4217 0.1166  0.0846  0.0504  113 GLU A N   
901  C CA  . GLU A 114 ? 0.5623 0.6212 0.4147 0.1112  0.0908  0.0605  113 GLU A CA  
902  C C   . GLU A 114 ? 0.5082 0.5680 0.3758 0.1011  0.0886  0.0638  113 GLU A C   
903  O O   . GLU A 114 ? 0.5046 0.5559 0.3720 0.0976  0.0841  0.0582  113 GLU A O   
904  C CB  . GLU A 114 ? 0.5995 0.6687 0.4683 0.1118  0.0961  0.0617  113 GLU A CB  
905  C CG  . GLU A 114 ? 0.6532 0.7184 0.5324 0.1076  0.0938  0.0560  113 GLU A CG  
906  C CD  . GLU A 114 ? 0.7250 0.7993 0.6177 0.1086  0.0979  0.0571  113 GLU A CD  
907  O OE1 . GLU A 114 ? 0.7792 0.8590 0.6658 0.1157  0.1018  0.0593  113 GLU A OE1 
908  O OE2 . GLU A 114 ? 0.7407 0.8169 0.6499 0.1022  0.0971  0.0559  113 GLU A OE2 
909  N N   . ILE A 115 ? 0.4813 0.5516 0.3625 0.0966  0.0918  0.0732  114 ILE A N   
910  C CA  . ILE A 115 ? 0.5125 0.5852 0.4110 0.0872  0.0902  0.0777  114 ILE A CA  
911  C C   . ILE A 115 ? 0.4999 0.5809 0.4240 0.0814  0.0929  0.0786  114 ILE A C   
912  O O   . ILE A 115 ? 0.5056 0.5965 0.4408 0.0820  0.0971  0.0831  114 ILE A O   
913  C CB  . ILE A 115 ? 0.5340 0.6130 0.4357 0.0850  0.0914  0.0874  114 ILE A CB  
914  C CG1 . ILE A 115 ? 0.5766 0.6471 0.4518 0.0907  0.0879  0.0862  114 ILE A CG1 
915  C CG2 . ILE A 115 ? 0.5500 0.6307 0.4706 0.0755  0.0892  0.0919  114 ILE A CG2 
916  C CD1 . ILE A 115 ? 0.5844 0.6622 0.4607 0.0901  0.0897  0.0959  114 ILE A CD1 
917  N N   . ARG A 116 ? 0.4671 0.5440 0.4001 0.0757  0.0898  0.0742  115 ARG A N   
918  C CA  . ARG A 116 ? 0.4500 0.5330 0.4071 0.0689  0.0906  0.0741  115 ARG A CA  
919  C C   . ARG A 116 ? 0.4372 0.5216 0.4106 0.0603  0.0882  0.0774  115 ARG A C   
920  O O   . ARG A 116 ? 0.5024 0.5818 0.4674 0.0595  0.0857  0.0786  115 ARG A O   
921  C CB  . ARG A 116 ? 0.4696 0.5471 0.4245 0.0697  0.0887  0.0652  115 ARG A CB  
922  C CG  . ARG A 116 ? 0.5266 0.6006 0.4636 0.0790  0.0901  0.0611  115 ARG A CG  
923  C CD  . ARG A 116 ? 0.5744 0.6412 0.5076 0.0799  0.0873  0.0525  115 ARG A CD  
924  N NE  . ARG A 116 ? 0.6244 0.6972 0.5799 0.0727  0.0873  0.0521  115 ARG A NE  
925  C CZ  . ARG A 116 ? 0.6393 0.7079 0.5973 0.0709  0.0847  0.0457  115 ARG A CZ  
926  N NH1 . ARG A 116 ? 0.6508 0.7087 0.5906 0.0760  0.0818  0.0393  115 ARG A NH1 
927  N NH2 . ARG A 116 ? 0.6011 0.6752 0.5787 0.0639  0.0841  0.0454  115 ARG A NH2 
928  N N   . ARG A 117 ? 0.4167 0.5071 0.4129 0.0538  0.0882  0.0787  116 ARG A N   
929  C CA  . ARG A 117 ? 0.4504 0.5423 0.4642 0.0459  0.0857  0.0820  116 ARG A CA  
930  C C   . ARG A 117 ? 0.3998 0.4856 0.4107 0.0431  0.0821  0.0784  116 ARG A C   
931  O O   . ARG A 117 ? 0.3699 0.4560 0.3878 0.0391  0.0803  0.0828  116 ARG A O   
932  C CB  . ARG A 117 ? 0.5155 0.6108 0.5501 0.0397  0.0843  0.0800  116 ARG A CB  
933  C CG  . ARG A 117 ? 0.6078 0.7098 0.6480 0.0412  0.0874  0.0853  116 ARG A CG  
934  C CD  . ARG A 117 ? 0.6740 0.7775 0.7319 0.0349  0.0850  0.0827  116 ARG A CD  
935  N NE  . ARG A 117 ? 0.7335 0.8431 0.7943 0.0369  0.0881  0.0864  116 ARG A NE  
936  C CZ  . ARG A 117 ? 0.7782 0.8938 0.8478 0.0361  0.0897  0.0945  116 ARG A CZ  
937  N NH1 . ARG A 117 ? 0.7739 0.8895 0.8502 0.0333  0.0883  0.0998  116 ARG A NH1 
938  N NH2 . ARG A 117 ? 0.8112 0.9332 0.8835 0.0381  0.0925  0.0979  116 ARG A NH2 
939  N N   . SER A 118 ? 0.3720 0.4525 0.3730 0.0451  0.0809  0.0711  117 SER A N   
940  C CA  . SER A 118 ? 0.3602 0.4345 0.3600 0.0414  0.0759  0.0669  117 SER A CA  
941  C C   . SER A 118 ? 0.3404 0.4018 0.3148 0.0458  0.0697  0.0617  117 SER A C   
942  O O   . SER A 118 ? 0.3503 0.4034 0.3234 0.0415  0.0614  0.0567  117 SER A O   
943  C CB  . SER A 118 ? 0.4122 0.4880 0.4257 0.0367  0.0745  0.0603  117 SER A CB  
944  O OG  . SER A 118 ? 0.4429 0.5239 0.4775 0.0310  0.0740  0.0609  117 SER A OG  
945  N N   . CYS A 119 ? 0.3571 0.4167 0.3114 0.0544  0.0731  0.0627  118 CYS A N   
946  C CA  . CYS A 119 ? 0.3377 0.3832 0.2675 0.0587  0.0661  0.0562  118 CYS A CA  
947  C C   . CYS A 119 ? 0.4155 0.4606 0.3233 0.0688  0.0708  0.0590  118 CYS A C   
948  O O   . CYS A 119 ? 0.4707 0.5274 0.3836 0.0717  0.0793  0.0665  118 CYS A O   
949  C CB  . CYS A 119 ? 0.3350 0.3735 0.2623 0.0585  0.0623  0.0470  118 CYS A CB  
950  S SG  . CYS A 119 ? 0.4054 0.4506 0.3310 0.0663  0.0715  0.0455  118 CYS A SG  
951  N N   . VAL A 120 ? 0.4096 0.4412 0.2933 0.0737  0.0644  0.0528  119 VAL A N   
952  C CA  . VAL A 120 ? 0.4694 0.4984 0.3287 0.0849  0.0682  0.0522  119 VAL A CA  
953  C C   . VAL A 120 ? 0.4865 0.5063 0.3353 0.0896  0.0657  0.0424  119 VAL A C   
954  O O   . VAL A 120 ? 0.4944 0.5009 0.3386 0.0859  0.0558  0.0352  119 VAL A O   
955  C CB  . VAL A 120 ? 0.4895 0.5090 0.3270 0.0877  0.0620  0.0528  119 VAL A CB  
956  C CG1 . VAL A 120 ? 0.4635 0.4775 0.2789 0.0979  0.0626  0.0481  119 VAL A CG1 
957  C CG2 . VAL A 120 ? 0.5039 0.5336 0.3515 0.0840  0.0651  0.0636  119 VAL A CG2 
958  N N   . THR A 121 ? 0.4190 0.4450 0.2711 0.0950  0.0717  0.0415  120 THR A N   
959  C CA  . THR A 121 ? 0.4328 0.4507 0.2775 0.0996  0.0695  0.0329  120 THR A CA  
960  C C   . THR A 121 ? 0.5086 0.5186 0.3315 0.1095  0.0679  0.0288  120 THR A C   
961  O O   . THR A 121 ? 0.4721 0.4911 0.2955 0.1136  0.0734  0.0337  120 THR A O   
962  C CB  . THR A 121 ? 0.4455 0.4753 0.3126 0.0975  0.0754  0.0343  120 THR A CB  
963  O OG1 . THR A 121 ? 0.4536 0.4888 0.3404 0.0883  0.0755  0.0361  120 THR A OG1 
964  C CG2 . THR A 121 ? 0.4332 0.4549 0.2917 0.1033  0.0732  0.0264  120 THR A CG2 
965  N N   . VAL A 122 ? 0.5587 0.5515 0.3626 0.1130  0.0598  0.0198  121 VAL A N   
966  C CA  . VAL A 122 ? 0.6272 0.6105 0.4109 0.1226  0.0572  0.0142  121 VAL A CA  
967  C C   . VAL A 122 ? 0.6333 0.6117 0.4179 0.1266  0.0565  0.0077  121 VAL A C   
968  O O   . VAL A 122 ? 0.5786 0.5518 0.3694 0.1219  0.0528  0.0042  121 VAL A O   
969  C CB  . VAL A 122 ? 0.6948 0.6601 0.4555 0.1234  0.0465  0.0090  121 VAL A CB  
970  C CG1 . VAL A 122 ? 0.7049 0.6564 0.4634 0.1172  0.0366  0.0034  121 VAL A CG1 
971  C CG2 . VAL A 122 ? 0.7547 0.7101 0.4955 0.1335  0.0437  0.0028  121 VAL A CG2 
972  N N   . PHE A 123 ? 0.6976 0.6784 0.4764 0.1354  0.0602  0.0067  122 PHE A N   
973  C CA  . PHE A 123 ? 0.6931 0.6719 0.4748 0.1397  0.0607  0.0022  122 PHE A CA  
974  C C   . PHE A 123 ? 0.7127 0.6727 0.4712 0.1480  0.0528  -0.0070 122 PHE A C   
975  O O   . PHE A 123 ? 0.7264 0.6800 0.4677 0.1531  0.0502  -0.0086 122 PHE A O   
976  C CB  . PHE A 123 ? 0.6527 0.6494 0.4477 0.1431  0.0706  0.0085  122 PHE A CB  
977  C CG  . PHE A 123 ? 0.6256 0.6394 0.4455 0.1343  0.0770  0.0171  122 PHE A CG  
978  C CD1 . PHE A 123 ? 0.6433 0.6623 0.4816 0.1286  0.0781  0.0172  122 PHE A CD1 
979  C CD2 . PHE A 123 ? 0.6030 0.6272 0.4282 0.1314  0.0811  0.0249  122 PHE A CD2 
980  C CE1 . PHE A 123 ? 0.6356 0.6690 0.4971 0.1201  0.0827  0.0244  122 PHE A CE1 
981  C CE2 . PHE A 123 ? 0.6050 0.6434 0.4538 0.1230  0.0858  0.0325  122 PHE A CE2 
982  C CZ  . PHE A 123 ? 0.6162 0.6588 0.4830 0.1173  0.0864  0.0319  122 PHE A CZ  
983  N N   . LYS A 124 ? 0.7374 0.6885 0.4963 0.1491  0.0487  -0.0130 123 LYS A N   
984  C CA  . LYS A 124 ? 0.7856 0.7169 0.5251 0.1557  0.0395  -0.0220 123 LYS A CA  
985  C C   . LYS A 124 ? 0.7812 0.7127 0.5278 0.1591  0.0408  -0.0248 123 LYS A C   
986  O O   . LYS A 124 ? 0.7328 0.6755 0.4987 0.1533  0.0454  -0.0211 123 LYS A O   
987  C CB  . LYS A 124 ? 0.8187 0.7313 0.5488 0.1494  0.0273  -0.0274 123 LYS A CB  
988  C CG  . LYS A 124 ? 0.8786 0.7716 0.5853 0.1546  0.0172  -0.0342 123 LYS A CG  
989  C CD  . LYS A 124 ? 0.8915 0.7909 0.5886 0.1588  0.0214  -0.0307 123 LYS A CD  
990  C CE  . LYS A 124 ? 0.9708 0.8558 0.6461 0.1687  0.0156  -0.0374 123 LYS A CE  
991  N NZ  . LYS A 124 ? 1.0238 0.8852 0.6858 0.1657  0.0007  -0.0448 123 LYS A NZ  
992  N N   . PRO A 125 ? 0.8172 0.7369 0.5490 0.1683  0.0366  -0.0310 124 PRO A N   
993  C CA  . PRO A 125 ? 0.7956 0.7152 0.5339 0.1717  0.0373  -0.0335 124 PRO A CA  
994  C C   . PRO A 125 ? 0.7611 0.6750 0.5102 0.1632  0.0321  -0.0354 124 PRO A C   
995  O O   . PRO A 125 ? 0.8186 0.7136 0.5576 0.1608  0.0209  -0.0415 124 PRO A O   
996  C CB  . PRO A 125 ? 0.8545 0.7566 0.5713 0.1819  0.0301  -0.0414 124 PRO A CB  
997  C CG  . PRO A 125 ? 0.9031 0.7922 0.6030 0.1812  0.0227  -0.0442 124 PRO A CG  
998  C CD  . PRO A 125 ? 0.8604 0.7664 0.5692 0.1761  0.0308  -0.0362 124 PRO A CD  
999  N N   . GLY A 126 ? 0.6537 0.5841 0.4240 0.1581  0.0396  -0.0300 125 GLY A N   
1000 C CA  . GLY A 126 ? 0.6520 0.5796 0.4340 0.1507  0.0361  -0.0314 125 GLY A CA  
1001 C C   . GLY A 126 ? 0.6370 0.5683 0.4284 0.1400  0.0355  -0.0284 125 GLY A C   
1002 O O   . GLY A 126 ? 0.6267 0.5575 0.4290 0.1337  0.0332  -0.0293 125 GLY A O   
1003 N N   . TYR A 127 ? 0.6637 0.5991 0.4515 0.1380  0.0374  -0.0250 126 TYR A N   
1004 C CA  . TYR A 127 ? 0.6348 0.5742 0.4317 0.1280  0.0370  -0.0220 126 TYR A CA  
1005 C C   . TYR A 127 ? 0.5867 0.5365 0.3839 0.1269  0.0425  -0.0158 126 TYR A C   
1006 O O   . TYR A 127 ? 0.5686 0.5172 0.3536 0.1337  0.0436  -0.0155 126 TYR A O   
1007 C CB  . TYR A 127 ? 0.6879 0.6067 0.4721 0.1237  0.0242  -0.0285 126 TYR A CB  
1008 C CG  . TYR A 127 ? 0.7475 0.6503 0.5098 0.1270  0.0157  -0.0323 126 TYR A CG  
1009 C CD1 . TYR A 127 ? 0.7904 0.6785 0.5373 0.1350  0.0096  -0.0383 126 TYR A CD1 
1010 C CD2 . TYR A 127 ? 0.7527 0.6551 0.5104 0.1218  0.0132  -0.0297 126 TYR A CD2 
1011 C CE1 . TYR A 127 ? 0.8006 0.6743 0.5287 0.1378  0.0015  -0.0418 126 TYR A CE1 
1012 C CE2 . TYR A 127 ? 0.7737 0.6620 0.5128 0.1241  0.0049  -0.0329 126 TYR A CE2 
1013 C CZ  . TYR A 127 ? 0.8062 0.6802 0.5308 0.1320  -0.0009 -0.0391 126 TYR A CZ  
1014 O OH  . TYR A 127 ? 0.8350 0.6951 0.5419 0.1342  -0.0092 -0.0423 126 TYR A OH  
1015 N N   . HIS A 128 ? 0.5638 0.5238 0.3752 0.1184  0.0456  -0.0107 127 HIS A N   
1016 C CA  . HIS A 128 ? 0.5831 0.5517 0.3958 0.1159  0.0495  -0.0044 127 HIS A CA  
1017 C C   . HIS A 128 ? 0.5356 0.4983 0.3484 0.1070  0.0429  -0.0045 127 HIS A C   
1018 O O   . HIS A 128 ? 0.4823 0.4439 0.3099 0.0982  0.0379  -0.0058 127 HIS A O   
1019 C CB  . HIS A 128 ? 0.5983 0.5890 0.4342 0.1130  0.0604  0.0044  127 HIS A CB  
1020 C CG  . HIS A 128 ? 0.5734 0.5736 0.4319 0.1048  0.0628  0.0064  127 HIS A CG  
1021 N ND1 . HIS A 128 ? 0.5462 0.5518 0.4169 0.1050  0.0651  0.0056  127 HIS A ND1 
1022 C CD2 . HIS A 128 ? 0.5477 0.5531 0.4190 0.0960  0.0629  0.0092  127 HIS A CD2 
1023 C CE1 . HIS A 128 ? 0.5240 0.5376 0.4141 0.0965  0.0662  0.0076  127 HIS A CE1 
1024 N NE2 . HIS A 128 ? 0.5241 0.5380 0.4154 0.0911  0.0652  0.0096  127 HIS A NE2 
1025 N N   . VAL A 129 ? 0.5487 0.5089 0.3517 0.1063  0.0406  -0.0019 128 VAL A N   
1026 C CA  . VAL A 129 ? 0.5015 0.4582 0.3123 0.0950  0.0323  -0.0001 128 VAL A CA  
1027 C C   . VAL A 129 ? 0.4509 0.4250 0.2790 0.0901  0.0401  0.0091  128 VAL A C   
1028 O O   . VAL A 129 ? 0.4821 0.4628 0.3024 0.0962  0.0469  0.0137  128 VAL A O   
1029 C CB  . VAL A 129 ? 0.5071 0.4460 0.2940 0.0971  0.0215  -0.0043 128 VAL A CB  
1030 C CG1 . VAL A 129 ? 0.5051 0.4422 0.3021 0.0853  0.0130  -0.0016 128 VAL A CG1 
1031 C CG2 . VAL A 129 ? 0.5469 0.4672 0.3166 0.1024  0.0131  -0.0136 128 VAL A CG2 
1032 N N   . ASP A 130 ? 0.4351 0.4166 0.2866 0.0794  0.0391  0.0118  129 ASP A N   
1033 C CA  . ASP A 130 ? 0.4026 0.3988 0.2728 0.0735  0.0449  0.0198  129 ASP A CA  
1034 C C   . ASP A 130 ? 0.4021 0.3924 0.2731 0.0660  0.0360  0.0209  129 ASP A C   
1035 O O   . ASP A 130 ? 0.3644 0.3503 0.2440 0.0582  0.0284  0.0180  129 ASP A O   
1036 C CB  . ASP A 130 ? 0.3940 0.4028 0.2899 0.0675  0.0500  0.0215  129 ASP A CB  
1037 C CG  . ASP A 130 ? 0.4199 0.4362 0.3172 0.0746  0.0588  0.0214  129 ASP A CG  
1038 O OD1 . ASP A 130 ? 0.4339 0.4499 0.3153 0.0844  0.0637  0.0222  129 ASP A OD1 
1039 O OD2 . ASP A 130 ? 0.4109 0.4339 0.3249 0.0706  0.0608  0.0206  129 ASP A OD2 
1040 N N   . LEU A 131 ? 0.4015 0.3925 0.2636 0.0684  0.0369  0.0256  130 LEU A N   
1041 C CA  . LEU A 131 ? 0.4283 0.4149 0.2910 0.0621  0.0289  0.0277  130 LEU A CA  
1042 C C   . LEU A 131 ? 0.3865 0.3877 0.2722 0.0561  0.0345  0.0355  130 LEU A C   
1043 O O   . LEU A 131 ? 0.4259 0.4355 0.3118 0.0597  0.0419  0.0421  130 LEU A O   
1044 C CB  . LEU A 131 ? 0.4952 0.4722 0.3323 0.0686  0.0252  0.0278  130 LEU A CB  
1045 C CG  . LEU A 131 ? 0.5727 0.5339 0.3837 0.0764  0.0196  0.0196  130 LEU A CG  
1046 C CD1 . LEU A 131 ? 0.6201 0.5859 0.4188 0.0879  0.0297  0.0197  130 LEU A CD1 
1047 C CD2 . LEU A 131 ? 0.6317 0.5792 0.4229 0.0767  0.0089  0.0180  130 LEU A CD2 
1048 N N   . ALA A 132 ? 0.3365 0.3408 0.2418 0.0471  0.0310  0.0349  131 ALA A N   
1049 C CA  . ALA A 132 ? 0.3078 0.3227 0.2336 0.0411  0.0335  0.0412  131 ALA A CA  
1050 C C   . ALA A 132 ? 0.3366 0.3460 0.2543 0.0397  0.0269  0.0444  131 ALA A C   
1051 O O   . ALA A 132 ? 0.3295 0.3274 0.2341 0.0388  0.0175  0.0404  131 ALA A O   
1052 C CB  . ALA A 132 ? 0.2653 0.2850 0.2128 0.0329  0.0316  0.0387  131 ALA A CB  
1053 N N   . VAL A 133 ? 0.3376 0.3551 0.2632 0.0395  0.0315  0.0521  132 VAL A N   
1054 C CA  . VAL A 133 ? 0.3323 0.3457 0.2485 0.0396  0.0265  0.0566  132 VAL A CA  
1055 C C   . VAL A 133 ? 0.3534 0.3734 0.2923 0.0321  0.0246  0.0610  132 VAL A C   
1056 O O   . VAL A 133 ? 0.3720 0.4026 0.3299 0.0302  0.0315  0.0654  132 VAL A O   
1057 C CB  . VAL A 133 ? 0.3599 0.3769 0.2631 0.0470  0.0333  0.0629  132 VAL A CB  
1058 C CG1 . VAL A 133 ? 0.3823 0.3950 0.2748 0.0471  0.0277  0.0678  132 VAL A CG1 
1059 C CG2 . VAL A 133 ? 0.3808 0.3921 0.2620 0.0556  0.0360  0.0578  132 VAL A CG2 
1060 N N   . TYR A 134 ? 0.3090 0.3227 0.2464 0.0278  0.0150  0.0598  133 TYR A N   
1061 C CA  . TYR A 134 ? 0.2988 0.3183 0.2575 0.0212  0.0124  0.0629  133 TYR A CA  
1062 C C   . TYR A 134 ? 0.3092 0.3250 0.2610 0.0208  0.0062  0.0682  133 TYR A C   
1063 O O   . TYR A 134 ? 0.3337 0.3402 0.2632 0.0242  0.0008  0.0674  133 TYR A O   
1064 C CB  . TYR A 134 ? 0.2798 0.2981 0.2488 0.0152  0.0065  0.0567  133 TYR A CB  
1065 C CG  . TYR A 134 ? 0.2497 0.2704 0.2234 0.0152  0.0109  0.0509  133 TYR A CG  
1066 C CD1 . TYR A 134 ? 0.2533 0.2652 0.2089 0.0186  0.0089  0.0455  133 TYR A CD1 
1067 C CD2 . TYR A 134 ? 0.2573 0.2884 0.2532 0.0118  0.0166  0.0508  133 TYR A CD2 
1068 C CE1 . TYR A 134 ? 0.2841 0.2982 0.2443 0.0186  0.0125  0.0407  133 TYR A CE1 
1069 C CE2 . TYR A 134 ? 0.2724 0.3059 0.2723 0.0117  0.0201  0.0458  133 TYR A CE2 
1070 C CZ  . TYR A 134 ? 0.2997 0.3250 0.2820 0.0150  0.0182  0.0411  133 TYR A CZ  
1071 O OH  . TYR A 134 ? 0.2920 0.3197 0.2786 0.0149  0.0214  0.0366  133 TYR A OH  
1072 N N   . ALA A 135 ? 0.3496 0.3724 0.3206 0.0169  0.0063  0.0735  134 ALA A N   
1073 C CA  . ALA A 135 ? 0.2982 0.3184 0.2666 0.0156  -0.0005 0.0787  134 ALA A CA  
1074 C C   . ALA A 135 ? 0.3585 0.3761 0.3341 0.0099  -0.0099 0.0749  134 ALA A C   
1075 O O   . ALA A 135 ? 0.3636 0.3843 0.3515 0.0064  -0.0097 0.0696  134 ALA A O   
1076 C CB  . ALA A 135 ? 0.2954 0.3241 0.2814 0.0146  0.0041  0.0871  134 ALA A CB  
1077 N N   . ASP A 136 ? 0.3983 0.4111 0.3660 0.0091  -0.0182 0.0781  135 ASP A N   
1078 C CA  . ASP A 136 ? 0.3955 0.4066 0.3697 0.0037  -0.0278 0.0758  135 ASP A CA  
1079 C C   . ASP A 136 ? 0.3513 0.3731 0.3537 -0.0006 -0.0260 0.0779  135 ASP A C   
1080 O O   . ASP A 136 ? 0.3622 0.3884 0.3742 0.0000  -0.0241 0.0844  135 ASP A O   
1081 C CB  . ASP A 136 ? 0.4523 0.4558 0.4108 0.0040  -0.0374 0.0794  135 ASP A CB  
1082 C CG  . ASP A 136 ? 0.4746 0.4751 0.4361 -0.0015 -0.0485 0.0769  135 ASP A CG  
1083 O OD1 . ASP A 136 ? 0.4676 0.4756 0.4494 -0.0061 -0.0484 0.0749  135 ASP A OD1 
1084 O OD2 . ASP A 136 ? 0.5140 0.5052 0.4575 -0.0012 -0.0577 0.0772  135 ASP A OD2 
1085 N N   . PRO A 137 ? 0.3342 0.3604 0.3503 -0.0047 -0.0267 0.0727  136 PRO A N   
1086 C CA  . PRO A 137 ? 0.3571 0.3936 0.3991 -0.0079 -0.0253 0.0740  136 PRO A CA  
1087 C C   . PRO A 137 ? 0.4481 0.4859 0.4966 -0.0097 -0.0326 0.0795  136 PRO A C   
1088 O O   . PRO A 137 ? 0.4584 0.5031 0.5254 -0.0099 -0.0301 0.0830  136 PRO A O   
1089 C CB  . PRO A 137 ? 0.3632 0.4034 0.4131 -0.0116 -0.0263 0.0672  136 PRO A CB  
1090 C CG  . PRO A 137 ? 0.3589 0.3917 0.3904 -0.0095 -0.0244 0.0626  136 PRO A CG  
1091 C CD  . PRO A 137 ? 0.3413 0.3637 0.3499 -0.0059 -0.0282 0.0655  136 PRO A CD  
1092 N N   . GLU A 138 ? 0.5245 0.5553 0.5584 -0.0109 -0.0419 0.0802  137 GLU A N   
1093 C CA  . GLU A 138 ? 0.5789 0.6113 0.6189 -0.0128 -0.0496 0.0858  137 GLU A CA  
1094 C C   . GLU A 138 ? 0.5491 0.5812 0.5886 -0.0094 -0.0472 0.0933  137 GLU A C   
1095 O O   . GLU A 138 ? 0.5812 0.6180 0.6346 -0.0105 -0.0503 0.0985  137 GLU A O   
1096 C CB  . GLU A 138 ? 0.6718 0.6954 0.6938 -0.0148 -0.0608 0.0854  137 GLU A CB  
1097 C CG  . GLU A 138 ? 0.7670 0.7904 0.7900 -0.0190 -0.0649 0.0793  137 GLU A CG  
1098 C CD  . GLU A 138 ? 0.8395 0.8748 0.8870 -0.0236 -0.0670 0.0800  137 GLU A CD  
1099 O OE1 . GLU A 138 ? 0.8754 0.9161 0.9347 -0.0239 -0.0696 0.0855  137 GLU A OE1 
1100 O OE2 . GLU A 138 ? 0.8631 0.9030 0.9180 -0.0265 -0.0658 0.0753  137 GLU A OE2 
1101 N N   . LEU A 139 ? 0.4841 0.5114 0.5082 -0.0052 -0.0416 0.0945  138 LEU A N   
1102 C CA  . LEU A 139 ? 0.4736 0.5010 0.4953 -0.0020 -0.0389 0.1025  138 LEU A CA  
1103 C C   . LEU A 139 ? 0.4311 0.4653 0.4684 -0.0006 -0.0284 0.1043  138 LEU A C   
1104 O O   . LEU A 139 ? 0.4570 0.4922 0.4943 0.0018  -0.0253 0.1118  138 LEU A O   
1105 C CB  . LEU A 139 ? 0.4492 0.4676 0.4418 0.0020  -0.0401 0.1038  138 LEU A CB  
1106 C CG  . LEU A 139 ? 0.4180 0.4276 0.3924 0.0008  -0.0515 0.1015  138 LEU A CG  
1107 C CD1 . LEU A 139 ? 0.3892 0.3892 0.3333 0.0059  -0.0517 0.1006  138 LEU A CD1 
1108 C CD2 . LEU A 139 ? 0.4173 0.4285 0.3992 -0.0018 -0.0599 0.1082  138 LEU A CD2 
1109 N N   . SER A 140 ? 0.3809 0.4198 0.4317 -0.0021 -0.0233 0.0981  139 SER A N   
1110 C CA  . SER A 140 ? 0.3934 0.4378 0.4576 -0.0010 -0.0139 0.0988  139 SER A CA  
1111 C C   . SER A 140 ? 0.4449 0.4968 0.5355 -0.0039 -0.0127 0.0955  139 SER A C   
1112 O O   . SER A 140 ? 0.4952 0.5512 0.5964 -0.0039 -0.0059 0.0921  139 SER A O   
1113 C CB  . SER A 140 ? 0.3533 0.3960 0.4052 0.0012  -0.0075 0.0939  139 SER A CB  
1114 O OG  . SER A 140 ? 0.3534 0.3889 0.3796 0.0047  -0.0090 0.0957  139 SER A OG  
1115 N N   . GLY A 141 ? 0.4388 0.4929 0.5398 -0.0060 -0.0193 0.0964  140 GLY A N   
1116 C CA  . GLY A 141 ? 0.4261 0.4878 0.5517 -0.0077 -0.0182 0.0935  140 GLY A CA  
1117 C C   . GLY A 141 ? 0.4373 0.5033 0.5675 -0.0100 -0.0179 0.0847  140 GLY A C   
1118 O O   . GLY A 141 ? 0.4448 0.5177 0.5939 -0.0107 -0.0149 0.0809  140 GLY A O   
1119 N N   . GLY A 142 ? 0.4312 0.4930 0.5442 -0.0112 -0.0211 0.0814  141 GLY A N   
1120 C CA  . GLY A 142 ? 0.4014 0.4674 0.5181 -0.0140 -0.0217 0.0743  141 GLY A CA  
1121 C C   . GLY A 142 ? 0.3915 0.4582 0.5062 -0.0135 -0.0145 0.0686  141 GLY A C   
1122 O O   . GLY A 142 ? 0.3746 0.4450 0.4918 -0.0159 -0.0148 0.0629  141 GLY A O   
1123 N N   . THR A 143 ? 0.4082 0.4722 0.5187 -0.0107 -0.0082 0.0704  142 THR A N   
1124 C CA  . THR A 143 ? 0.4231 0.4882 0.5326 -0.0100 -0.0013 0.0657  142 THR A CA  
1125 C C   . THR A 143 ? 0.3724 0.4296 0.4585 -0.0077 -0.0007 0.0657  142 THR A C   
1126 O O   . THR A 143 ? 0.3837 0.4352 0.4565 -0.0052 -0.0022 0.0710  142 THR A O   
1127 C CB  . THR A 143 ? 0.4763 0.5455 0.6007 -0.0087 0.0056  0.0677  142 THR A CB  
1128 O OG1 . THR A 143 ? 0.5720 0.6430 0.6959 -0.0083 0.0119  0.0632  142 THR A OG1 
1129 C CG2 . THR A 143 ? 0.4917 0.5568 0.6098 -0.0060 0.0066  0.0760  142 THR A CG2 
1130 N N   . LEU A 144 ? 0.3151 0.3720 0.3958 -0.0082 0.0013  0.0598  143 LEU A N   
1131 C CA  . LEU A 144 ? 0.2808 0.3304 0.3406 -0.0051 0.0027  0.0588  143 LEU A CA  
1132 C C   . LEU A 144 ? 0.2647 0.3173 0.3273 -0.0020 0.0119  0.0602  143 LEU A C   
1133 O O   . LEU A 144 ? 0.2453 0.3039 0.3207 -0.0033 0.0166  0.0568  143 LEU A O   
1134 C CB  . LEU A 144 ? 0.2847 0.3319 0.3378 -0.0071 -0.0002 0.0521  143 LEU A CB  
1135 C CG  . LEU A 144 ? 0.3067 0.3448 0.3374 -0.0033 0.0000  0.0501  143 LEU A CG  
1136 C CD1 . LEU A 144 ? 0.3065 0.3352 0.3182 -0.0010 -0.0062 0.0533  143 LEU A CD1 
1137 C CD2 . LEU A 144 ? 0.3299 0.3661 0.3573 -0.0057 -0.0029 0.0438  143 LEU A CD2 
1138 N N   . CYS A 145 ? 0.2677 0.3167 0.3180 0.0020  0.0142  0.0656  144 CYS A N   
1139 C CA  . CYS A 145 ? 0.2440 0.2972 0.2980 0.0048  0.0228  0.0689  144 CYS A CA  
1140 C C   . CYS A 145 ? 0.2550 0.3035 0.2873 0.0099  0.0257  0.0686  144 CYS A C   
1141 O O   . CYS A 145 ? 0.3039 0.3451 0.3169 0.0127  0.0215  0.0699  144 CYS A O   
1142 C CB  . CYS A 145 ? 0.2789 0.3350 0.3420 0.0052  0.0244  0.0775  144 CYS A CB  
1143 S SG  . CYS A 145 ? 0.2905 0.3525 0.3817 0.0004  0.0222  0.0775  144 CYS A SG  
1144 N N   . ILE A 146 ? 0.2135 0.2661 0.2489 0.0114  0.0326  0.0667  145 ILE A N   
1145 C CA  . ILE A 146 ? 0.2530 0.3032 0.2708 0.0171  0.0370  0.0664  145 ILE A CA  
1146 C C   . ILE A 146 ? 0.2837 0.3396 0.3027 0.0204  0.0440  0.0751  145 ILE A C   
1147 O O   . ILE A 146 ? 0.3081 0.3709 0.3464 0.0175  0.0470  0.0799  145 ILE A O   
1148 C CB  . ILE A 146 ? 0.2561 0.3089 0.2781 0.0168  0.0405  0.0600  145 ILE A CB  
1149 C CG1 . ILE A 146 ? 0.2259 0.2749 0.2280 0.0234  0.0438  0.0585  145 ILE A CG1 
1150 C CG2 . ILE A 146 ? 0.2420 0.3051 0.2866 0.0141  0.0468  0.0619  145 ILE A CG2 
1151 C CD1 . ILE A 146 ? 0.2786 0.3278 0.2819 0.0233  0.0451  0.0516  145 ILE A CD1 
1152 N N   . ALA A 147 ? 0.2817 0.3345 0.2799 0.0266  0.0463  0.0773  146 ALA A N   
1153 C CA  . ALA A 147 ? 0.3749 0.4339 0.3715 0.0304  0.0530  0.0865  146 ALA A CA  
1154 C C   . ALA A 147 ? 0.3748 0.4426 0.3796 0.0323  0.0621  0.0873  146 ALA A C   
1155 O O   . ALA A 147 ? 0.3392 0.4055 0.3305 0.0372  0.0648  0.0830  146 ALA A O   
1156 C CB  . ALA A 147 ? 0.4227 0.4755 0.3922 0.0368  0.0516  0.0883  146 ALA A CB  
1157 N N   . LYS A 148 ? 0.3410 0.4176 0.3682 0.0284  0.0663  0.0928  147 LYS A N   
1158 C CA  . LYS A 148 ? 0.3579 0.4437 0.3970 0.0288  0.0740  0.0943  147 LYS A CA  
1159 C C   . LYS A 148 ? 0.3912 0.4821 0.4302 0.0316  0.0775  0.1023  147 LYS A C   
1160 O O   . LYS A 148 ? 0.3687 0.4608 0.4120 0.0300  0.0763  0.1100  147 LYS A O   
1161 C CB  . LYS A 148 ? 0.4643 0.5518 0.5282 0.0218  0.0711  0.0902  147 LYS A CB  
1162 C CG  . LYS A 148 ? 0.5224 0.6091 0.5898 0.0207  0.0705  0.0806  147 LYS A CG  
1163 C CD  . LYS A 148 ? 0.5246 0.6080 0.5851 0.0203  0.0685  0.0745  147 LYS A CD  
1164 C CE  . LYS A 148 ? 0.5982 0.6808 0.6615 0.0191  0.0674  0.0655  147 LYS A CE  
1165 N NZ  . LYS A 148 ? 0.6541 0.7368 0.7342 0.0136  0.0641  0.0614  147 LYS A NZ  
1166 N N   . GLY A 149 ? 0.4110 0.5051 0.4462 0.0354  0.0810  0.1004  148 GLY A N   
1167 C CA  . GLY A 149 ? 0.4819 0.5822 0.5180 0.0380  0.0842  0.1077  148 GLY A CA  
1168 C C   . GLY A 149 ? 0.5040 0.6050 0.5177 0.0463  0.0879  0.1083  148 GLY A C   
1169 O O   . GLY A 149 ? 0.4686 0.5632 0.4622 0.0505  0.0869  0.1047  148 GLY A O   
1170 N N   . LYS A 150 ? 0.5672 0.6754 0.5836 0.0490  0.0915  0.1126  149 LYS A N   
1171 C CA  . LYS A 150 ? 0.6247 0.7351 0.6218 0.0573  0.0953  0.1136  149 LYS A CA  
1172 C C   . LYS A 150 ? 0.6313 0.7502 0.6327 0.0579  0.0978  0.1241  149 LYS A C   
1173 O O   . LYS A 150 ? 0.6056 0.7277 0.6247 0.0520  0.0963  0.1302  149 LYS A O   
1174 C CB  . LYS A 150 ? 0.6591 0.7710 0.6546 0.0608  0.0977  0.1077  149 LYS A CB  
1175 C CG  . LYS A 150 ? 0.6816 0.7985 0.6995 0.0551  0.0976  0.1084  149 LYS A CG  
1176 C CD  . LYS A 150 ? 0.6945 0.8142 0.7100 0.0590  0.1002  0.1047  149 LYS A CD  
1177 C CE  . LYS A 150 ? 0.6869 0.7986 0.6911 0.0614  0.0985  0.0946  149 LYS A CE  
1178 N NZ  . LYS A 150 ? 0.6903 0.8046 0.6962 0.0637  0.1002  0.0912  149 LYS A NZ  
1179 N N   . GLU A 151 ? 0.7033 0.8257 0.6884 0.0654  0.1014  0.1260  150 GLU A N   
1180 C CA  . GLU A 151 ? 0.8150 0.9471 0.8040 0.0665  0.1044  0.1362  150 GLU A CA  
1181 C C   . GLU A 151 ? 0.8919 1.0327 0.9035 0.0625  0.1061  0.1409  150 GLU A C   
1182 O O   . GLU A 151 ? 0.8969 1.0433 0.9227 0.0583  0.1057  0.1496  150 GLU A O   
1183 C CB  . GLU A 151 ? 0.8226 0.9575 0.7898 0.0758  0.1082  0.1363  150 GLU A CB  
1184 C CG  . GLU A 151 ? 0.8333 0.9578 0.7748 0.0806  0.1055  0.1304  150 GLU A CG  
1185 C CD  . GLU A 151 ? 0.8531 0.9695 0.7816 0.0853  0.1048  0.1190  150 GLU A CD  
1186 O OE1 . GLU A 151 ? 0.8450 0.9590 0.7860 0.0812  0.1036  0.1143  150 GLU A OE1 
1187 O OE2 . GLU A 151 ? 0.8704 0.9824 0.7761 0.0932  0.1051  0.1147  150 GLU A OE2 
1188 N N   . ASN A 152 ? 0.9934 1.1347 1.0081 0.0636  0.1074  0.1351  151 ASN A N   
1189 C CA  . ASN A 152 ? 1.0664 1.2144 1.1008 0.0596  0.1081  0.1387  151 ASN A CA  
1190 C C   . ASN A 152 ? 1.0851 1.2288 1.1392 0.0506  0.1033  0.1377  151 ASN A C   
1191 O O   . ASN A 152 ? 1.0798 1.2283 1.1510 0.0464  0.1028  0.1426  151 ASN A O   
1192 C CB  . ASN A 152 ? 1.1283 1.2770 1.1590 0.0632  0.1102  0.1323  151 ASN A CB  
1193 C CG  . ASN A 152 ? 1.1874 1.3439 1.2357 0.0600  0.1112  0.1368  151 ASN A CG  
1194 O OD1 . ASN A 152 ? 1.2256 1.3900 1.2841 0.0583  0.1124  0.1464  151 ASN A OD1 
1195 N ND2 . ASN A 152 ? 1.1973 1.3515 1.2490 0.0591  0.1104  0.1300  151 ASN A ND2 
1196 N N   . SER A 153 ? 1.0925 1.2270 1.1444 0.0478  0.0995  0.1316  152 SER A N   
1197 C CA  . SER A 153 ? 1.0681 1.1980 1.1379 0.0398  0.0947  0.1294  152 SER A CA  
1198 C C   . SER A 153 ? 1.0605 1.1941 1.1452 0.0357  0.0932  0.1389  152 SER A C   
1199 O O   . SER A 153 ? 1.0256 1.1583 1.1279 0.0300  0.0902  0.1389  152 SER A O   
1200 C CB  . SER A 153 ? 1.0419 1.1628 1.1058 0.0382  0.0913  0.1221  152 SER A CB  
1201 N N   . GLY A 154 ? 1.0935 1.2308 1.1707 0.0385  0.0949  0.1467  153 GLY A N   
1202 C CA  . GLY A 154 ? 1.1218 1.2633 1.2128 0.0349  0.0935  0.1567  153 GLY A CA  
1203 C C   . GLY A 154 ? 1.1426 1.2785 1.2356 0.0317  0.0895  0.1586  153 GLY A C   
1204 O O   . GLY A 154 ? 1.1430 1.2775 1.2201 0.0351  0.0901  0.1601  153 GLY A O   
1205 N N   . ASP A 155 ? 1.1621 1.2940 1.2741 0.0255  0.0848  0.1583  154 ASP A N   
1206 C CA  . ASP A 155 ? 1.1795 1.3065 1.2973 0.0221  0.0804  0.1611  154 ASP A CA  
1207 C C   . ASP A 155 ? 1.1704 1.2892 1.3005 0.0173  0.0756  0.1527  154 ASP A C   
1208 O O   . ASP A 155 ? 1.1513 1.2644 1.2797 0.0160  0.0725  0.1502  154 ASP A O   
1209 C CB  . ASP A 155 ? 1.1959 1.3281 1.3269 0.0199  0.0792  0.1725  154 ASP A CB  
1210 C CG  . ASP A 155 ? 1.2067 1.3341 1.3436 0.0168  0.0744  0.1762  154 ASP A CG  
1211 O OD1 . ASP A 155 ? 1.2078 1.3294 1.3337 0.0176  0.0729  0.1720  154 ASP A OD1 
1212 O OD2 . ASP A 155 ? 1.2140 1.3430 1.3667 0.0135  0.0716  0.1836  154 ASP A OD2 
1213 N N   . GLU A 156 ? 1.1978 1.3159 1.3396 0.0148  0.0747  0.1482  155 GLU A N   
1214 C CA  . GLU A 156 ? 1.2106 1.3209 1.3636 0.0104  0.0699  0.1395  155 GLU A CA  
1215 C C   . GLU A 156 ? 1.1842 1.2902 1.3259 0.0115  0.0703  0.1285  155 GLU A C   
1216 O O   . GLU A 156 ? 1.1775 1.2774 1.3235 0.0088  0.0665  0.1220  155 GLU A O   
1217 C CB  . GLU A 156 ? 1.2495 1.3599 1.4173 0.0073  0.0683  0.1386  155 GLU A CB  
1218 C CG  . GLU A 156 ? 1.2681 1.3704 1.4477 0.0031  0.0631  0.1301  155 GLU A CG  
1219 C CD  . GLU A 156 ? 1.2847 1.3867 1.4751 0.0005  0.0618  0.1282  155 GLU A CD  
1220 O OE1 . GLU A 156 ? 1.2884 1.3947 1.4728 0.0019  0.0650  0.1275  155 GLU A OE1 
1221 O OE2 . GLU A 156 ? 1.2844 1.3818 1.4894 -0.0028 0.0574  0.1276  155 GLU A OE2 
1222 N N   . HIS A 157 ? 1.1543 1.2636 1.2818 0.0155  0.0745  0.1263  156 HIS A N   
1223 C CA  . HIS A 157 ? 1.0894 1.1948 1.2063 0.0167  0.0747  0.1162  156 HIS A CA  
1224 C C   . HIS A 157 ? 0.9726 1.0770 1.0724 0.0205  0.0763  0.1167  156 HIS A C   
1225 O O   . HIS A 157 ? 0.9780 1.0810 1.0644 0.0237  0.0780  0.1107  156 HIS A O   
1226 C CB  . HIS A 157 ? 1.1561 1.2646 1.2681 0.0189  0.0777  0.1129  156 HIS A CB  
1227 C CG  . HIS A 157 ? 1.2158 1.3250 1.3427 0.0151  0.0760  0.1125  156 HIS A CG  
1228 N ND1 . HIS A 157 ? 1.2261 1.3311 1.3681 0.0100  0.0714  0.1112  156 HIS A ND1 
1229 C CD2 . HIS A 157 ? 1.2368 1.3504 1.3655 0.0158  0.0780  0.1132  156 HIS A CD2 
1230 C CE1 . HIS A 157 ? 1.2290 1.3353 1.3805 0.0077  0.0706  0.1111  156 HIS A CE1 
1231 N NE2 . HIS A 157 ? 1.2317 1.3435 1.3758 0.0109  0.0746  0.1126  156 HIS A NE2 
1232 N N   . ARG A 158 ? 0.8315 0.9358 0.9308 0.0203  0.0752  0.1237  157 ARG A N   
1233 C CA  . ARG A 158 ? 0.7133 0.8157 0.7939 0.0239  0.0760  0.1255  157 ARG A CA  
1234 C C   . ARG A 158 ? 0.5919 0.6894 0.6793 0.0198  0.0711  0.1261  157 ARG A C   
1235 O O   . ARG A 158 ? 0.6061 0.7042 0.7046 0.0173  0.0687  0.1330  157 ARG A O   
1236 C CB  . ARG A 158 ? 0.7123 0.8196 0.7815 0.0284  0.0792  0.1348  157 ARG A CB  
1237 C CG  . ARG A 158 ? 0.7286 0.8321 0.7758 0.0323  0.0786  0.1368  157 ARG A CG  
1238 C CD  . ARG A 158 ? 0.7507 0.8592 0.7888 0.0360  0.0808  0.1458  157 ARG A CD  
1239 N NE  . ARG A 158 ? 0.7431 0.8592 0.7793 0.0400  0.0862  0.1464  157 ARG A NE  
1240 C CZ  . ARG A 158 ? 0.7442 0.8661 0.7693 0.0447  0.0894  0.1526  157 ARG A CZ  
1241 N NH1 . ARG A 158 ? 0.7330 0.8623 0.7582 0.0483  0.0942  0.1532  157 ARG A NH1 
1242 N NH2 . ARG A 158 ? 0.7595 0.8797 0.7733 0.0459  0.0875  0.1581  157 ARG A NH2 
1243 N N   . LEU A 159 ? 0.4467 0.5396 0.5283 0.0191  0.0693  0.1194  158 LEU A N   
1244 C CA  . LEU A 159 ? 0.4079 0.4969 0.4993 0.0146  0.0641  0.1192  158 LEU A CA  
1245 C C   . LEU A 159 ? 0.3715 0.4533 0.4477 0.0156  0.0593  0.1098  158 LEU A C   
1246 O O   . LEU A 159 ? 0.3464 0.4269 0.4090 0.0188  0.0614  0.1039  158 LEU A O   
1247 C CB  . LEU A 159 ? 0.4090 0.4977 0.5241 0.0097  0.0609  0.1135  158 LEU A CB  
1248 C CG  . LEU A 159 ? 0.4234 0.5110 0.5406 0.0087  0.0608  0.1020  158 LEU A CG  
1249 C CD1 . LEU A 159 ? 0.4627 0.5468 0.5956 0.0043  0.0554  0.0947  158 LEU A CD1 
1250 C CD2 . LEU A 159 ? 0.3835 0.4735 0.5018 0.0101  0.0638  0.1013  158 LEU A CD2 
1251 N N   . TRP A 160 ? 0.3771 0.4535 0.4564 0.0129  0.0520  0.1079  159 TRP A N   
1252 C CA  . TRP A 160 ? 0.3838 0.4537 0.4545 0.0121  0.0457  0.0985  159 TRP A CA  
1253 C C   . TRP A 160 ? 0.3709 0.4434 0.4616 0.0076  0.0449  0.0913  159 TRP A C   
1254 O O   . TRP A 160 ? 0.4085 0.4825 0.5173 0.0042  0.0424  0.0926  159 TRP A O   
1255 C CB  . TRP A 160 ? 0.3353 0.3995 0.3992 0.0117  0.0381  0.1008  159 TRP A CB  
1256 C CG  . TRP A 160 ? 0.3406 0.4012 0.3811 0.0164  0.0377  0.1062  159 TRP A CG  
1257 C CD1 . TRP A 160 ? 0.3774 0.4401 0.4159 0.0180  0.0391  0.1167  159 TRP A CD1 
1258 C CD2 . TRP A 160 ? 0.3354 0.3892 0.3507 0.0204  0.0353  0.1013  159 TRP A CD2 
1259 N NE1 . TRP A 160 ? 0.4072 0.4657 0.4198 0.0230  0.0382  0.1183  159 TRP A NE1 
1260 C CE2 . TRP A 160 ? 0.4053 0.4576 0.4032 0.0247  0.0356  0.1085  159 TRP A CE2 
1261 C CE3 . TRP A 160 ? 0.3474 0.3959 0.3529 0.0207  0.0327  0.0915  159 TRP A CE3 
1262 C CZ2 . TRP A 160 ? 0.4174 0.4626 0.3879 0.0298  0.0332  0.1054  159 TRP A CZ2 
1263 C CZ3 . TRP A 160 ? 0.3774 0.4181 0.3569 0.0254  0.0299  0.0887  159 TRP A CZ3 
1264 C CH2 . TRP A 160 ? 0.4087 0.4476 0.3706 0.0301  0.0301  0.0952  159 TRP A CH2 
1265 N N   . GLN A 161 ? 0.3223 0.3953 0.4096 0.0078  0.0467  0.0838  160 GLN A N   
1266 C CA  . GLN A 161 ? 0.2724 0.3491 0.3773 0.0039  0.0467  0.0771  160 GLN A CA  
1267 C C   . GLN A 161 ? 0.2559 0.3287 0.3568 0.0018  0.0403  0.0693  160 GLN A C   
1268 O O   . GLN A 161 ? 0.2650 0.3327 0.3479 0.0037  0.0378  0.0662  160 GLN A O   
1269 C CB  . GLN A 161 ? 0.2881 0.3693 0.3946 0.0048  0.0530  0.0745  160 GLN A CB  
1270 C CG  . GLN A 161 ? 0.3389 0.4189 0.4576 0.0013  0.0499  0.0654  160 GLN A CG  
1271 C CD  . GLN A 161 ? 0.4021 0.4814 0.5155 0.0022  0.0520  0.0600  160 GLN A CD  
1272 O OE1 . GLN A 161 ? 0.3962 0.4766 0.4981 0.0049  0.0550  0.0597  160 GLN A OE1 
1273 N NE2 . GLN A 161 ? 0.4224 0.5001 0.5438 0.0000  0.0503  0.0562  160 GLN A NE2 
1274 N N   . ILE A 162 ? 0.2298 0.3055 0.3481 -0.0019 0.0375  0.0662  161 ILE A N   
1275 C CA  . ILE A 162 ? 0.2114 0.2861 0.3287 -0.0042 0.0320  0.0594  161 ILE A CA  
1276 C C   . ILE A 162 ? 0.2110 0.2859 0.3205 -0.0042 0.0337  0.0530  161 ILE A C   
1277 O O   . ILE A 162 ? 0.2380 0.3170 0.3535 -0.0040 0.0390  0.0514  161 ILE A O   
1278 C CB  . ILE A 162 ? 0.2597 0.3395 0.3983 -0.0073 0.0302  0.0568  161 ILE A CB  
1279 C CG1 . ILE A 162 ? 0.2962 0.3771 0.4343 -0.0097 0.0251  0.0507  161 ILE A CG1 
1280 C CG2 . ILE A 162 ? 0.2571 0.3346 0.3993 -0.0072 0.0326  0.0508  161 ILE A CG2 
1281 C CD1 . ILE A 162 ? 0.3913 0.4728 0.5407 -0.0108 0.0213  0.0473  161 ILE A CD1 
1282 N N   . SER A 163 ? 0.1985 0.2687 0.2947 -0.0045 0.0285  0.0497  162 SER A N   
1283 C CA  . SER A 163 ? 0.2426 0.3108 0.3281 -0.0040 0.0289  0.0446  162 SER A CA  
1284 C C   . SER A 163 ? 0.2323 0.2991 0.3160 -0.0074 0.0220  0.0402  162 SER A C   
1285 O O   . SER A 163 ? 0.2391 0.3044 0.3233 -0.0090 0.0164  0.0420  162 SER A O   
1286 C CB  . SER A 163 ? 0.3004 0.3614 0.3648 0.0009  0.0302  0.0470  162 SER A CB  
1287 O OG  . SER A 163 ? 0.3784 0.4369 0.4331 0.0022  0.0310  0.0421  162 SER A OG  
1288 N N   . ASP A 164 ? 0.1975 0.2655 0.2799 -0.0088 0.0223  0.0350  163 ASP A N   
1289 C CA  . ASP A 164 ? 0.2089 0.2769 0.2906 -0.0127 0.0158  0.0316  163 ASP A CA  
1290 C C   . ASP A 164 ? 0.2012 0.2648 0.2711 -0.0124 0.0149  0.0278  163 ASP A C   
1291 O O   . ASP A 164 ? 0.2036 0.2729 0.2811 -0.0154 0.0152  0.0241  163 ASP A O   
1292 C CB  . ASP A 164 ? 0.1985 0.2771 0.3002 -0.0165 0.0166  0.0291  163 ASP A CB  
1293 C CG  . ASP A 164 ? 0.2364 0.3172 0.3393 -0.0205 0.0099  0.0275  163 ASP A CG  
1294 O OD1 . ASP A 164 ? 0.2209 0.2941 0.3105 -0.0210 0.0036  0.0291  163 ASP A OD1 
1295 O OD2 . ASP A 164 ? 0.2280 0.3155 0.3408 -0.0226 0.0104  0.0235  163 ASP A OD2 
1296 N N   . PRO A 165 ? 0.2729 0.2814 0.3007 0.0009  -0.0299 0.0277  164 PRO A N   
1297 C CA  . PRO A 165 ? 0.2925 0.3025 0.3129 -0.0010 -0.0267 0.0227  164 PRO A CA  
1298 C C   . PRO A 165 ? 0.2744 0.2886 0.2980 -0.0008 -0.0275 0.0182  164 PRO A C   
1299 O O   . PRO A 165 ? 0.2417 0.2565 0.2646 -0.0017 -0.0242 0.0135  164 PRO A O   
1300 C CB  . PRO A 165 ? 0.2773 0.2873 0.2852 -0.0031 -0.0277 0.0256  164 PRO A CB  
1301 C CG  . PRO A 165 ? 0.2587 0.2696 0.2670 -0.0023 -0.0330 0.0315  164 PRO A CG  
1302 C CD  . PRO A 165 ? 0.2723 0.2803 0.2924 0.0000  -0.0335 0.0341  164 PRO A CD  
1303 N N   . GLN A 166 ? 0.2480 0.2655 0.2754 0.0001  -0.0319 0.0197  165 GLN A N   
1304 C CA  . GLN A 166 ? 0.2962 0.3181 0.3277 0.0000  -0.0324 0.0155  165 GLN A CA  
1305 C C   . GLN A 166 ? 0.2659 0.2888 0.3085 0.0015  -0.0296 0.0121  165 GLN A C   
1306 O O   . GLN A 166 ? 0.2638 0.2893 0.3076 0.0006  -0.0273 0.0078  165 GLN A O   
1307 C CB  . GLN A 166 ? 0.3496 0.3752 0.3826 0.0003  -0.0381 0.0179  165 GLN A CB  
1308 C CG  . GLN A 166 ? 0.4175 0.4431 0.4380 -0.0016 -0.0406 0.0200  165 GLN A CG  
1309 C CD  . GLN A 166 ? 0.4812 0.5114 0.5021 -0.0018 -0.0462 0.0206  165 GLN A CD  
1310 O OE1 . GLN A 166 ? 0.5504 0.5823 0.5780 -0.0001 -0.0506 0.0241  165 GLN A OE1 
1311 N NE2 . GLN A 166 ? 0.4438 0.4761 0.4585 -0.0040 -0.0464 0.0171  165 GLN A NE2 
1312 N N   . GLY A 167 ? 0.2473 0.2680 0.2978 0.0036  -0.0296 0.0139  166 GLY A N   
1313 C CA  . GLY A 167 ? 0.1806 0.2022 0.2407 0.0049  -0.0263 0.0096  166 GLY A CA  
1314 C C   . GLY A 167 ? 0.1698 0.1895 0.2246 0.0034  -0.0213 0.0060  166 GLY A C   
1315 O O   . GLY A 167 ? 0.1861 0.2086 0.2439 0.0030  -0.0185 0.0014  166 GLY A O   
1316 N N   . PHE A 168 ? 0.1540 0.1695 0.2009 0.0023  -0.0203 0.0080  167 PHE A N   
1317 C CA  . PHE A 168 ? 0.1789 0.1929 0.2210 0.0009  -0.0162 0.0047  167 PHE A CA  
1318 C C   . PHE A 168 ? 0.1613 0.1780 0.1976 -0.0010 -0.0155 0.0020  167 PHE A C   
1319 O O   . PHE A 168 ? 0.1801 0.1979 0.2170 -0.0017 -0.0127 -0.0018 167 PHE A O   
1320 C CB  . PHE A 168 ? 0.2215 0.2310 0.2568 -0.0001 -0.0153 0.0076  167 PHE A CB  
1321 C CG  . PHE A 168 ? 0.2251 0.2333 0.2566 -0.0013 -0.0116 0.0043  167 PHE A CG  
1322 C CD1 . PHE A 168 ? 0.2207 0.2286 0.2580 -0.0007 -0.0091 0.0007  167 PHE A CD1 
1323 C CD2 . PHE A 168 ? 0.2410 0.2485 0.2634 -0.0031 -0.0109 0.0043  167 PHE A CD2 
1324 C CE1 . PHE A 168 ? 0.2345 0.2416 0.2683 -0.0019 -0.0064 -0.0022 167 PHE A CE1 
1325 C CE2 . PHE A 168 ? 0.2536 0.2601 0.2737 -0.0041 -0.0080 0.0013  167 PHE A CE2 
1326 C CZ  . PHE A 168 ? 0.2396 0.2458 0.2652 -0.0035 -0.0060 -0.0016 167 PHE A CZ  
1327 N N   . GLN A 169 ? 0.1649 0.1827 0.1957 -0.0020 -0.0182 0.0038  168 GLN A N   
1328 C CA  . GLN A 169 ? 0.2174 0.2373 0.2438 -0.0038 -0.0179 0.0012  168 GLN A CA  
1329 C C   . GLN A 169 ? 0.2175 0.2416 0.2510 -0.0038 -0.0174 -0.0015 168 GLN A C   
1330 O O   . GLN A 169 ? 0.2003 0.2254 0.2323 -0.0052 -0.0152 -0.0042 168 GLN A O   
1331 C CB  . GLN A 169 ? 0.2592 0.2798 0.2794 -0.0048 -0.0213 0.0031  168 GLN A CB  
1332 C CG  . GLN A 169 ? 0.2679 0.2852 0.2795 -0.0055 -0.0209 0.0051  168 GLN A CG  
1333 C CD  . GLN A 169 ? 0.3371 0.3557 0.3430 -0.0061 -0.0247 0.0077  168 GLN A CD  
1334 O OE1 . GLN A 169 ? 0.3702 0.3870 0.3711 -0.0061 -0.0252 0.0111  168 GLN A OE1 
1335 N NE2 . GLN A 169 ? 0.3394 0.3612 0.3456 -0.0068 -0.0274 0.0061  168 GLN A NE2 
1336 N N   . ASP A 170 ? 0.1969 0.2237 0.2386 -0.0021 -0.0194 -0.0006 169 ASP A N   
1337 C CA  . ASP A 170 ? 0.1888 0.2204 0.2386 -0.0020 -0.0183 -0.0035 169 ASP A CA  
1338 C C   . ASP A 170 ? 0.1949 0.2265 0.2469 -0.0019 -0.0138 -0.0068 169 ASP A C   
1339 O O   . ASP A 170 ? 0.1747 0.2096 0.2277 -0.0033 -0.0115 -0.0095 169 ASP A O   
1340 C CB  . ASP A 170 ? 0.2016 0.2360 0.2612 0.0003  -0.0212 -0.0021 169 ASP A CB  
1341 C CG  . ASP A 170 ? 0.2946 0.3349 0.3640 0.0005  -0.0196 -0.0055 169 ASP A CG  
1342 O OD1 . ASP A 170 ? 0.2799 0.3235 0.3477 -0.0017 -0.0188 -0.0071 169 ASP A OD1 
1343 O OD2 . ASP A 170 ? 0.3451 0.3869 0.4242 0.0028  -0.0191 -0.0066 169 ASP A OD2 
1344 N N   . ARG A 171 ? 0.1650 0.1930 0.2177 -0.0005 -0.0126 -0.0065 170 ARG A N   
1345 C CA  . ARG A 171 ? 0.2080 0.2360 0.2623 -0.0006 -0.0087 -0.0101 170 ARG A CA  
1346 C C   . ARG A 171 ? 0.2016 0.2288 0.2474 -0.0029 -0.0067 -0.0114 170 ARG A C   
1347 O O   . ARG A 171 ? 0.1743 0.2041 0.2205 -0.0039 -0.0040 -0.0144 170 ARG A O   
1348 C CB  . ARG A 171 ? 0.2176 0.2413 0.2744 0.0011  -0.0083 -0.0095 170 ARG A CB  
1349 C CG  . ARG A 171 ? 0.3090 0.3334 0.3767 0.0037  -0.0100 -0.0088 170 ARG A CG  
1350 C CD  . ARG A 171 ? 0.3413 0.3684 0.4178 0.0049  -0.0070 -0.0140 170 ARG A CD  
1351 N NE  . ARG A 171 ? 0.3749 0.4044 0.4634 0.0075  -0.0087 -0.0142 170 ARG A NE  
1352 C CZ  . ARG A 171 ? 0.3703 0.4024 0.4690 0.0091  -0.0064 -0.0189 170 ARG A CZ  
1353 N NH1 . ARG A 171 ? 0.3262 0.3589 0.4233 0.0083  -0.0025 -0.0238 170 ARG A NH1 
1354 N NH2 . ARG A 171 ? 0.3126 0.3470 0.4235 0.0116  -0.0083 -0.0190 170 ARG A NH2 
1355 N N   . ILE A 172 ? 0.1913 0.2150 0.2294 -0.0039 -0.0080 -0.0091 171 ILE A N   
1356 C CA  . ILE A 172 ? 0.1672 0.1897 0.1985 -0.0059 -0.0066 -0.0102 171 ILE A CA  
1357 C C   . ILE A 172 ? 0.2387 0.2647 0.2696 -0.0077 -0.0068 -0.0109 171 ILE A C   
1358 O O   . ILE A 172 ? 0.2412 0.2680 0.2699 -0.0092 -0.0049 -0.0123 171 ILE A O   
1359 C CB  . ILE A 172 ? 0.1582 0.1767 0.1827 -0.0063 -0.0076 -0.0082 171 ILE A CB  
1360 C CG1 . ILE A 172 ? 0.1719 0.1871 0.1973 -0.0050 -0.0068 -0.0073 171 ILE A CG1 
1361 C CG2 . ILE A 172 ? 0.1946 0.2118 0.2136 -0.0081 -0.0066 -0.0095 171 ILE A CG2 
1362 C CD1 . ILE A 172 ? 0.1371 0.1519 0.1645 -0.0049 -0.0042 -0.0100 171 ILE A CD1 
1363 N N   . ALA A 173 ? 0.2234 0.2515 0.2566 -0.0077 -0.0092 -0.0096 172 ALA A N   
1364 C CA  . ALA A 173 ? 0.2297 0.2611 0.2637 -0.0097 -0.0095 -0.0102 172 ALA A CA  
1365 C C   . ALA A 173 ? 0.2097 0.2461 0.2499 -0.0101 -0.0070 -0.0122 172 ALA A C   
1366 O O   . ALA A 173 ? 0.2414 0.2802 0.2810 -0.0123 -0.0057 -0.0128 172 ALA A O   
1367 C CB  . ALA A 173 ? 0.2361 0.2689 0.2715 -0.0097 -0.0132 -0.0088 172 ALA A CB  
1368 N N   . SER A 174 ? 0.2101 0.2483 0.2565 -0.0080 -0.0060 -0.0134 173 SER A N   
1369 C CA  . SER A 174 ? 0.1886 0.2327 0.2423 -0.0081 -0.0035 -0.0160 173 SER A CA  
1370 C C   . SER A 174 ? 0.2081 0.2533 0.2606 -0.0084 0.0005  -0.0189 173 SER A C   
1371 O O   . SER A 174 ? 0.2468 0.2975 0.3037 -0.0092 0.0033  -0.0214 173 SER A O   
1372 C CB  . SER A 174 ? 0.2203 0.2668 0.2838 -0.0053 -0.0051 -0.0163 173 SER A CB  
1373 O OG  . SER A 174 ? 0.2461 0.2925 0.3106 -0.0052 -0.0092 -0.0135 173 SER A OG  
1374 N N   . LYS A 175 ? 0.1864 0.2269 0.2332 -0.0081 0.0008  -0.0189 174 LYS A N   
1375 C CA  . LYS A 175 ? 0.1931 0.2348 0.2390 -0.0082 0.0041  -0.0221 174 LYS A CA  
1376 C C   . LYS A 175 ? 0.2291 0.2751 0.2717 -0.0111 0.0065  -0.0230 174 LYS A C   
1377 O O   . LYS A 175 ? 0.2432 0.2938 0.2879 -0.0115 0.0097  -0.0264 174 LYS A O   
1378 C CB  . LYS A 175 ? 0.2180 0.2539 0.2579 -0.0079 0.0035  -0.0215 174 LYS A CB  
1379 C CG  . LYS A 175 ? 0.2154 0.2525 0.2540 -0.0082 0.0062  -0.0251 174 LYS A CG  
1380 C CD  . LYS A 175 ? 0.2452 0.2770 0.2786 -0.0080 0.0053  -0.0243 174 LYS A CD  
1381 C CE  . LYS A 175 ? 0.2468 0.2801 0.2775 -0.0088 0.0072  -0.0277 174 LYS A CE  
1382 N NZ  . LYS A 175 ? 0.2689 0.3047 0.3063 -0.0073 0.0092  -0.0323 174 LYS A NZ  
1383 N N   . LEU A 176 ? 0.2013 0.2459 0.2388 -0.0133 0.0051  -0.0200 175 LEU A N   
1384 C CA  . LEU A 176 ? 0.2282 0.2760 0.2622 -0.0165 0.0069  -0.0194 175 LEU A CA  
1385 C C   . LEU A 176 ? 0.2064 0.2545 0.2418 -0.0181 0.0050  -0.0167 175 LEU A C   
1386 O O   . LEU A 176 ? 0.2033 0.2494 0.2414 -0.0167 0.0022  -0.0157 175 LEU A O   
1387 C CB  . LEU A 176 ? 0.2040 0.2480 0.2295 -0.0177 0.0068  -0.0184 175 LEU A CB  
1388 C CG  . LEU A 176 ? 0.1822 0.2259 0.2059 -0.0164 0.0083  -0.0214 175 LEU A CG  
1389 C CD1 . LEU A 176 ? 0.1601 0.1985 0.1769 -0.0168 0.0065  -0.0198 175 LEU A CD1 
1390 C CD2 . LEU A 176 ? 0.1795 0.2297 0.2028 -0.0180 0.0119  -0.0241 175 LEU A CD2 
1391 N N   . SER A 177 ? 0.1631 0.2138 0.1965 -0.0213 0.0064  -0.0154 176 SER A N   
1392 C CA  . SER A 177 ? 0.2006 0.2514 0.2360 -0.0233 0.0045  -0.0130 176 SER A CA  
1393 C C   . SER A 177 ? 0.1988 0.2469 0.2281 -0.0263 0.0043  -0.0101 176 SER A C   
1394 O O   . SER A 177 ? 0.1647 0.2124 0.1885 -0.0272 0.0059  -0.0098 176 SER A O   
1395 C CB  . SER A 177 ? 0.2119 0.2701 0.2553 -0.0244 0.0065  -0.0141 176 SER A CB  
1396 O OG  . SER A 177 ? 0.2301 0.2934 0.2722 -0.0269 0.0106  -0.0146 176 SER A OG  
1397 N N   . GLY A 178 ? 0.1755 0.2216 0.2061 -0.0280 0.0019  -0.0080 177 GLY A N   
1398 C CA  . GLY A 178 ? 0.1992 0.2429 0.2263 -0.0312 0.0015  -0.0049 177 GLY A CA  
1399 C C   . GLY A 178 ? 0.2034 0.2413 0.2236 -0.0306 0.0002  -0.0038 177 GLY A C   
1400 O O   . GLY A 178 ? 0.1812 0.2148 0.1997 -0.0279 -0.0017 -0.0050 177 GLY A O   
1401 N N   . ASP A 179 ? 0.2203 0.2582 0.2364 -0.0332 0.0013  -0.0011 178 ASP A N   
1402 C CA  . ASP A 179 ? 0.2451 0.2778 0.2555 -0.0327 -0.0004 0.0003  178 ASP A CA  
1403 C C   . ASP A 179 ? 0.2233 0.2567 0.2302 -0.0302 0.0008  -0.0024 178 ASP A C   
1404 O O   . ASP A 179 ? 0.1997 0.2285 0.2036 -0.0287 -0.0011 -0.0024 178 ASP A O   
1405 C CB  . ASP A 179 ? 0.2074 0.2400 0.2145 -0.0363 -0.0002 0.0046  178 ASP A CB  
1406 C CG  . ASP A 179 ? 0.2908 0.3213 0.3021 -0.0390 -0.0019 0.0076  178 ASP A CG  
1407 O OD1 . ASP A 179 ? 0.2899 0.3174 0.3055 -0.0377 -0.0041 0.0060  178 ASP A OD1 
1408 O OD2 . ASP A 179 ? 0.3056 0.3373 0.3158 -0.0426 -0.0011 0.0116  178 ASP A OD2 
1409 N N   . ASP A 180 ? 0.2282 0.2673 0.2365 -0.0296 0.0038  -0.0051 179 ASP A N   
1410 C CA  . ASP A 180 ? 0.2282 0.2675 0.2350 -0.0269 0.0047  -0.0084 179 ASP A CA  
1411 C C   . ASP A 180 ? 0.1962 0.2308 0.2053 -0.0238 0.0024  -0.0097 179 ASP A C   
1412 O O   . ASP A 180 ? 0.1816 0.2127 0.1881 -0.0222 0.0014  -0.0105 179 ASP A O   
1413 C CB  . ASP A 180 ? 0.2412 0.2873 0.2511 -0.0266 0.0083  -0.0117 179 ASP A CB  
1414 C CG  . ASP A 180 ? 0.2865 0.3382 0.2926 -0.0297 0.0113  -0.0112 179 ASP A CG  
1415 O OD1 . ASP A 180 ? 0.2646 0.3146 0.2649 -0.0321 0.0103  -0.0076 179 ASP A OD1 
1416 O OD2 . ASP A 180 ? 0.2738 0.3320 0.2831 -0.0297 0.0148  -0.0144 179 ASP A OD2 
1417 N N   . ALA A 181 ? 0.1746 0.2097 0.1887 -0.0231 0.0017  -0.0100 180 ALA A N   
1418 C CA  . ALA A 181 ? 0.2163 0.2475 0.2317 -0.0205 -0.0004 -0.0107 180 ALA A CA  
1419 C C   . ALA A 181 ? 0.1936 0.2191 0.2054 -0.0208 -0.0029 -0.0091 180 ALA A C   
1420 O O   . ALA A 181 ? 0.1767 0.1988 0.1873 -0.0188 -0.0039 -0.0099 180 ALA A O   
1421 C CB  . ALA A 181 ? 0.2011 0.2346 0.2220 -0.0201 -0.0013 -0.0109 180 ALA A CB  
1422 N N   . ALA A 182 ? 0.2135 0.2380 0.2243 -0.0232 -0.0038 -0.0069 181 ALA A N   
1423 C CA  . ALA A 182 ? 0.2404 0.2595 0.2491 -0.0233 -0.0062 -0.0058 181 ALA A CA  
1424 C C   . ALA A 182 ? 0.2261 0.2431 0.2312 -0.0221 -0.0061 -0.0062 181 ALA A C   
1425 O O   . ALA A 182 ? 0.1999 0.2132 0.2045 -0.0205 -0.0073 -0.0072 181 ALA A O   
1426 C CB  . ALA A 182 ? 0.2084 0.2266 0.2176 -0.0263 -0.0072 -0.0030 181 ALA A CB  
1427 N N   . GLN A 183 ? 0.1358 0.1556 0.1386 -0.0230 -0.0045 -0.0058 182 GLN A N   
1428 C CA  . GLN A 183 ? 0.1923 0.2105 0.1921 -0.0220 -0.0049 -0.0064 182 GLN A CA  
1429 C C   . GLN A 183 ? 0.2098 0.2275 0.2110 -0.0193 -0.0042 -0.0095 182 GLN A C   
1430 O O   . GLN A 183 ? 0.1810 0.1957 0.1817 -0.0180 -0.0052 -0.0101 182 GLN A O   
1431 C CB  . GLN A 183 ? 0.1830 0.2051 0.1793 -0.0237 -0.0036 -0.0058 182 GLN A CB  
1432 C CG  . GLN A 183 ? 0.1957 0.2161 0.1887 -0.0231 -0.0050 -0.0060 182 GLN A CG  
1433 C CD  . GLN A 183 ? 0.2256 0.2505 0.2140 -0.0248 -0.0038 -0.0059 182 GLN A CD  
1434 O OE1 . GLN A 183 ? 0.2056 0.2353 0.1940 -0.0249 -0.0009 -0.0085 182 GLN A OE1 
1435 N NE2 . GLN A 183 ? 0.2265 0.2501 0.2110 -0.0261 -0.0062 -0.0030 182 GLN A NE2 
1436 N N   . PHE A 184 ? 0.1947 0.2155 0.1984 -0.0185 -0.0023 -0.0111 183 PHE A N   
1437 C CA  . PHE A 184 ? 0.2065 0.2264 0.2125 -0.0161 -0.0018 -0.0133 183 PHE A CA  
1438 C C   . PHE A 184 ? 0.2240 0.2396 0.2299 -0.0150 -0.0035 -0.0127 183 PHE A C   
1439 O O   . PHE A 184 ? 0.1758 0.1890 0.1813 -0.0138 -0.0035 -0.0135 183 PHE A O   
1440 C CB  . PHE A 184 ? 0.2033 0.2269 0.2133 -0.0155 -0.0004 -0.0143 183 PHE A CB  
1441 C CG  . PHE A 184 ? 0.2321 0.2545 0.2454 -0.0132 -0.0002 -0.0155 183 PHE A CG  
1442 C CD1 . PHE A 184 ? 0.2031 0.2250 0.2175 -0.0119 0.0008  -0.0175 183 PHE A CD1 
1443 C CD2 . PHE A 184 ? 0.1729 0.1953 0.1889 -0.0124 -0.0013 -0.0144 183 PHE A CD2 
1444 C CE1 . PHE A 184 ? 0.1690 0.1895 0.1873 -0.0099 0.0009  -0.0180 183 PHE A CE1 
1445 C CE2 . PHE A 184 ? 0.1809 0.2022 0.2000 -0.0104 -0.0015 -0.0146 183 PHE A CE2 
1446 C CZ  . PHE A 184 ? 0.1799 0.2001 0.2003 -0.0092 -0.0003 -0.0161 183 PHE A CZ  
1447 N N   . ARG A 185 ? 0.1717 0.1866 0.1780 -0.0157 -0.0047 -0.0115 184 ARG A N   
1448 C CA  . ARG A 185 ? 0.1784 0.1900 0.1841 -0.0149 -0.0060 -0.0116 184 ARG A CA  
1449 C C   . ARG A 185 ? 0.1765 0.1848 0.1806 -0.0150 -0.0069 -0.0117 184 ARG A C   
1450 O O   . ARG A 185 ? 0.1712 0.1774 0.1750 -0.0138 -0.0068 -0.0127 184 ARG A O   
1451 C CB  . ARG A 185 ? 0.1580 0.1701 0.1647 -0.0158 -0.0075 -0.0110 184 ARG A CB  
1452 C CG  . ARG A 185 ? 0.2033 0.2187 0.2126 -0.0152 -0.0072 -0.0109 184 ARG A CG  
1453 C CD  . ARG A 185 ? 0.2001 0.2160 0.2103 -0.0161 -0.0093 -0.0106 184 ARG A CD  
1454 N NE  . ARG A 185 ? 0.2115 0.2277 0.2229 -0.0184 -0.0099 -0.0100 184 ARG A NE  
1455 C CZ  . ARG A 185 ? 0.2240 0.2439 0.2385 -0.0198 -0.0092 -0.0092 184 ARG A CZ  
1456 N NH1 . ARG A 185 ? 0.2412 0.2651 0.2586 -0.0189 -0.0079 -0.0096 184 ARG A NH1 
1457 N NH2 . ARG A 185 ? 0.2790 0.2987 0.2946 -0.0222 -0.0097 -0.0081 184 ARG A NH2 
1458 N N   . ARG A 186 ? 0.1539 0.1620 0.1576 -0.0164 -0.0077 -0.0105 185 ARG A N   
1459 C CA  . ARG A 186 ? 0.1644 0.1694 0.1678 -0.0163 -0.0091 -0.0104 185 ARG A CA  
1460 C C   . ARG A 186 ? 0.2185 0.2234 0.2216 -0.0148 -0.0083 -0.0118 185 ARG A C   
1461 O O   . ARG A 186 ? 0.1928 0.1954 0.1970 -0.0138 -0.0088 -0.0128 185 ARG A O   
1462 C CB  . ARG A 186 ? 0.1820 0.1868 0.1847 -0.0182 -0.0105 -0.0079 185 ARG A CB  
1463 C CG  . ARG A 186 ? 0.1406 0.1444 0.1449 -0.0199 -0.0117 -0.0062 185 ARG A CG  
1464 C CD  . ARG A 186 ? 0.1853 0.1870 0.1896 -0.0216 -0.0137 -0.0032 185 ARG A CD  
1465 N NE  . ARG A 186 ? 0.2089 0.2138 0.2099 -0.0231 -0.0130 -0.0009 185 ARG A NE  
1466 C CZ  . ARG A 186 ? 0.2161 0.2245 0.2161 -0.0253 -0.0115 0.0008  185 ARG A CZ  
1467 N NH1 . ARG A 186 ? 0.2041 0.2130 0.2070 -0.0262 -0.0111 0.0006  185 ARG A NH1 
1468 N NH2 . ARG A 186 ? 0.1620 0.1739 0.1583 -0.0268 -0.0104 0.0024  185 ARG A NH2 
1469 N N   . CYS A 187 ? 0.2192 0.2269 0.2217 -0.0148 -0.0069 -0.0122 186 CYS A N   
1470 C CA  . CYS A 187 ? 0.2126 0.2203 0.2155 -0.0137 -0.0064 -0.0138 186 CYS A CA  
1471 C C   . CYS A 187 ? 0.2167 0.2233 0.2216 -0.0122 -0.0051 -0.0152 186 CYS A C   
1472 O O   . CYS A 187 ? 0.2054 0.2107 0.2117 -0.0114 -0.0050 -0.0163 186 CYS A O   
1473 C CB  . CYS A 187 ? 0.2162 0.2274 0.2181 -0.0142 -0.0053 -0.0147 186 CYS A CB  
1474 S SG  . CYS A 187 ? 0.2705 0.2832 0.2687 -0.0163 -0.0069 -0.0127 186 CYS A SG  
1475 N N   . ILE A 188 ? 0.1851 0.1922 0.1903 -0.0119 -0.0042 -0.0149 187 ILE A N   
1476 C CA  . ILE A 188 ? 0.1617 0.1675 0.1677 -0.0108 -0.0033 -0.0152 187 ILE A CA  
1477 C C   . ILE A 188 ? 0.1798 0.1834 0.1851 -0.0108 -0.0038 -0.0156 187 ILE A C   
1478 O O   . ILE A 188 ? 0.1712 0.1739 0.1775 -0.0102 -0.0028 -0.0164 187 ILE A O   
1479 C CB  . ILE A 188 ? 0.1550 0.1620 0.1612 -0.0106 -0.0031 -0.0142 187 ILE A CB  
1480 C CG1 . ILE A 188 ? 0.1871 0.1963 0.1959 -0.0102 -0.0022 -0.0146 187 ILE A CG1 
1481 C CG2 . ILE A 188 ? 0.1296 0.1351 0.1350 -0.0100 -0.0027 -0.0136 187 ILE A CG2 
1482 C CD1 . ILE A 188 ? 0.1967 0.2077 0.2072 -0.0098 -0.0026 -0.0135 187 ILE A CD1 
1483 N N   . ARG A 189 ? 0.1724 0.1753 0.1768 -0.0116 -0.0053 -0.0152 188 ARG A N   
1484 C CA  . ARG A 189 ? 0.1794 0.1803 0.1840 -0.0114 -0.0058 -0.0164 188 ARG A CA  
1485 C C   . ARG A 189 ? 0.1613 0.1612 0.1684 -0.0109 -0.0060 -0.0174 188 ARG A C   
1486 O O   . ARG A 189 ? 0.1871 0.1863 0.1956 -0.0102 -0.0050 -0.0191 188 ARG A O   
1487 C CB  . ARG A 189 ? 0.1680 0.1679 0.1725 -0.0123 -0.0076 -0.0162 188 ARG A CB  
1488 C CG  . ARG A 189 ? 0.1889 0.1899 0.1917 -0.0128 -0.0078 -0.0160 188 ARG A CG  
1489 C CD  . ARG A 189 ? 0.2403 0.2399 0.2440 -0.0139 -0.0098 -0.0165 188 ARG A CD  
1490 N NE  . ARG A 189 ? 0.2735 0.2742 0.2757 -0.0144 -0.0104 -0.0172 188 ARG A NE  
1491 C CZ  . ARG A 189 ? 0.3264 0.3285 0.3293 -0.0155 -0.0116 -0.0160 188 ARG A CZ  
1492 N NH1 . ARG A 189 ? 0.3315 0.3343 0.3363 -0.0165 -0.0118 -0.0140 188 ARG A NH1 
1493 N NH2 . ARG A 189 ? 0.3383 0.3417 0.3401 -0.0159 -0.0126 -0.0169 188 ARG A NH2 
1494 N N   . TYR A 190 ? 0.1831 0.1833 0.1907 -0.0113 -0.0073 -0.0165 189 TYR A N   
1495 C CA  . TYR A 190 ? 0.1945 0.1942 0.2047 -0.0108 -0.0083 -0.0172 189 TYR A CA  
1496 C C   . TYR A 190 ? 0.1937 0.1942 0.2057 -0.0099 -0.0063 -0.0189 189 TYR A C   
1497 O O   . TYR A 190 ? 0.2077 0.2077 0.2231 -0.0092 -0.0062 -0.0204 189 TYR A O   
1498 C CB  . TYR A 190 ? 0.1631 0.1639 0.1721 -0.0116 -0.0101 -0.0156 189 TYR A CB  
1499 C CG  . TYR A 190 ? 0.1851 0.1853 0.1924 -0.0130 -0.0120 -0.0131 189 TYR A CG  
1500 C CD1 . TYR A 190 ? 0.1739 0.1712 0.1830 -0.0131 -0.0135 -0.0126 189 TYR A CD1 
1501 C CD2 . TYR A 190 ? 0.1996 0.2020 0.2036 -0.0143 -0.0122 -0.0113 189 TYR A CD2 
1502 C CE1 . TYR A 190 ? 0.1974 0.1938 0.2059 -0.0147 -0.0153 -0.0099 189 TYR A CE1 
1503 C CE2 . TYR A 190 ? 0.1955 0.1976 0.1981 -0.0160 -0.0136 -0.0085 189 TYR A CE2 
1504 C CZ  . TYR A 190 ? 0.2162 0.2151 0.2212 -0.0163 -0.0153 -0.0075 189 TYR A CZ  
1505 O OH  . TYR A 190 ? 0.1891 0.1873 0.1934 -0.0183 -0.0167 -0.0042 189 TYR A OH  
1506 N N   . LEU A 191 ? 0.2134 0.2152 0.2242 -0.0099 -0.0047 -0.0187 190 LEU A N   
1507 C CA  . LEU A 191 ? 0.2011 0.2033 0.2144 -0.0094 -0.0029 -0.0199 190 LEU A CA  
1508 C C   . LEU A 191 ? 0.1713 0.1728 0.1849 -0.0092 -0.0009 -0.0201 190 LEU A C   
1509 O O   . LEU A 191 ? 0.1728 0.1744 0.1893 -0.0090 0.0007  -0.0212 190 LEU A O   
1510 C CB  . LEU A 191 ? 0.2245 0.2279 0.2376 -0.0095 -0.0020 -0.0197 190 LEU A CB  
1511 C CG  . LEU A 191 ? 0.3181 0.3232 0.3310 -0.0099 -0.0034 -0.0205 190 LEU A CG  
1512 C CD1 . LEU A 191 ? 0.3192 0.3255 0.3334 -0.0097 -0.0020 -0.0216 190 LEU A CD1 
1513 C CD2 . LEU A 191 ? 0.3389 0.3440 0.3541 -0.0098 -0.0048 -0.0217 190 LEU A CD2 
1514 N N   . LYS A 192 ? 0.1687 0.1698 0.1792 -0.0094 -0.0008 -0.0193 191 LYS A N   
1515 C CA  . LYS A 192 ? 0.1826 0.1836 0.1920 -0.0094 0.0011  -0.0198 191 LYS A CA  
1516 C C   . LYS A 192 ? 0.1855 0.1863 0.1976 -0.0091 0.0013  -0.0223 191 LYS A C   
1517 O O   . LYS A 192 ? 0.1675 0.1690 0.1809 -0.0091 0.0037  -0.0235 191 LYS A O   
1518 C CB  . LYS A 192 ? 0.1793 0.1804 0.1844 -0.0098 0.0005  -0.0188 191 LYS A CB  
1519 C CG  . LYS A 192 ? 0.2144 0.2161 0.2180 -0.0099 0.0008  -0.0164 191 LYS A CG  
1520 C CD  . LYS A 192 ? 0.2140 0.2162 0.2138 -0.0102 -0.0003 -0.0154 191 LYS A CD  
1521 C CE  . LYS A 192 ? 0.2333 0.2362 0.2326 -0.0100 -0.0004 -0.0128 191 LYS A CE  
1522 N NZ  . LYS A 192 ? 0.2526 0.2565 0.2488 -0.0103 -0.0022 -0.0119 191 LYS A NZ  
1523 N N   . ARG A 193 ? 0.1890 0.1888 0.2026 -0.0089 -0.0012 -0.0229 192 ARG A N   
1524 C CA  . ARG A 193 ? 0.1839 0.1833 0.2018 -0.0083 -0.0014 -0.0255 192 ARG A CA  
1525 C C   . ARG A 193 ? 0.1986 0.1989 0.2215 -0.0077 -0.0010 -0.0263 192 ARG A C   
1526 O O   . ARG A 193 ? 0.1744 0.1756 0.2015 -0.0073 0.0006  -0.0287 192 ARG A O   
1527 C CB  . ARG A 193 ? 0.1915 0.1890 0.2108 -0.0081 -0.0046 -0.0254 192 ARG A CB  
1528 C CG  . ARG A 193 ? 0.2061 0.2027 0.2317 -0.0071 -0.0054 -0.0280 192 ARG A CG  
1529 C CD  . ARG A 193 ? 0.2189 0.2169 0.2459 -0.0067 -0.0022 -0.0317 192 ARG A CD  
1530 N NE  . ARG A 193 ? 0.1932 0.1907 0.2160 -0.0073 -0.0016 -0.0329 192 ARG A NE  
1531 C CZ  . ARG A 193 ? 0.2529 0.2486 0.2783 -0.0070 -0.0032 -0.0352 192 ARG A CZ  
1532 N NH1 . ARG A 193 ? 0.2368 0.2306 0.2693 -0.0060 -0.0056 -0.0361 192 ARG A NH1 
1533 N NH2 . ARG A 193 ? 0.2658 0.2615 0.2870 -0.0078 -0.0027 -0.0366 192 ARG A NH2 
1534 N N   . TRP A 194 ? 0.1998 0.2004 0.2227 -0.0079 -0.0024 -0.0248 193 TRP A N   
1535 C CA  . TRP A 194 ? 0.1757 0.1776 0.2032 -0.0077 -0.0022 -0.0258 193 TRP A CA  
1536 C C   . TRP A 194 ? 0.2057 0.2087 0.2346 -0.0080 0.0016  -0.0266 193 TRP A C   
1537 O O   . TRP A 194 ? 0.1829 0.1872 0.2173 -0.0078 0.0028  -0.0285 193 TRP A O   
1538 C CB  . TRP A 194 ? 0.1803 0.1826 0.2062 -0.0081 -0.0040 -0.0245 193 TRP A CB  
1539 C CG  . TRP A 194 ? 0.1421 0.1459 0.1723 -0.0081 -0.0036 -0.0259 193 TRP A CG  
1540 C CD1 . TRP A 194 ? 0.1521 0.1570 0.1877 -0.0077 -0.0054 -0.0275 193 TRP A CD1 
1541 C CD2 . TRP A 194 ? 0.1395 0.1439 0.1699 -0.0086 -0.0017 -0.0260 193 TRP A CD2 
1542 N NE1 . TRP A 194 ? 0.1781 0.1844 0.2170 -0.0081 -0.0046 -0.0288 193 TRP A NE1 
1543 C CE2 . TRP A 194 ? 0.1778 0.1835 0.2137 -0.0086 -0.0023 -0.0280 193 TRP A CE2 
1544 C CE3 . TRP A 194 ? 0.1995 0.2032 0.2268 -0.0089 0.0002  -0.0247 193 TRP A CE3 
1545 C CZ2 . TRP A 194 ? 0.1855 0.1916 0.2239 -0.0092 -0.0009 -0.0289 193 TRP A CZ2 
1546 C CZ3 . TRP A 194 ? 0.1673 0.1712 0.1975 -0.0092 0.0015  -0.0253 193 TRP A CZ3 
1547 C CH2 . TRP A 194 ? 0.1732 0.1781 0.2089 -0.0094 0.0011  -0.0275 193 TRP A CH2 
1548 N N   . ARG A 195 ? 0.1925 0.1953 0.2170 -0.0086 0.0034  -0.0249 194 ARG A N   
1549 C CA  . ARG A 195 ? 0.2143 0.2178 0.2392 -0.0093 0.0069  -0.0245 194 ARG A CA  
1550 C C   . ARG A 195 ? 0.1808 0.1855 0.2066 -0.0094 0.0093  -0.0265 194 ARG A C   
1551 O O   . ARG A 195 ? 0.1897 0.1960 0.2195 -0.0098 0.0120  -0.0275 194 ARG A O   
1552 C CB  . ARG A 195 ? 0.2302 0.2328 0.2496 -0.0098 0.0076  -0.0217 194 ARG A CB  
1553 C CG  . ARG A 195 ? 0.2777 0.2809 0.2957 -0.0107 0.0110  -0.0203 194 ARG A CG  
1554 C CD  . ARG A 195 ? 0.3288 0.3316 0.3402 -0.0110 0.0108  -0.0178 194 ARG A CD  
1555 N NE  . ARG A 195 ? 0.4087 0.4119 0.4164 -0.0108 0.0097  -0.0194 194 ARG A NE  
1556 C CZ  . ARG A 195 ? 0.4543 0.4575 0.4567 -0.0110 0.0085  -0.0181 194 ARG A CZ  
1557 N NH1 . ARG A 195 ? 0.4597 0.4625 0.4597 -0.0112 0.0082  -0.0147 194 ARG A NH1 
1558 N NH2 . ARG A 195 ? 0.4460 0.4495 0.4461 -0.0109 0.0074  -0.0202 194 ARG A NH2 
1559 N N   . ASP A 196 ? 0.1685 0.1727 0.1912 -0.0090 0.0085  -0.0274 195 ASP A N   
1560 C CA  . ASP A 196 ? 0.1829 0.1887 0.2064 -0.0091 0.0110  -0.0302 195 ASP A CA  
1561 C C   . ASP A 196 ? 0.1829 0.1899 0.2148 -0.0082 0.0109  -0.0334 195 ASP A C   
1562 O O   . ASP A 196 ? 0.2061 0.2155 0.2411 -0.0084 0.0142  -0.0358 195 ASP A O   
1563 C CB  . ASP A 196 ? 0.2627 0.2677 0.2818 -0.0089 0.0097  -0.0312 195 ASP A CB  
1564 C CG  . ASP A 196 ? 0.2975 0.3023 0.3088 -0.0099 0.0100  -0.0285 195 ASP A CG  
1565 O OD1 . ASP A 196 ? 0.3204 0.3259 0.3297 -0.0107 0.0119  -0.0260 195 ASP A OD1 
1566 O OD2 . ASP A 196 ? 0.3533 0.3572 0.3613 -0.0098 0.0080  -0.0288 195 ASP A OD2 
1567 N N   . PHE A 197 ? 0.1229 0.1285 0.1585 -0.0072 0.0071  -0.0332 196 PHE A N   
1568 C CA  . PHE A 197 ? 0.1777 0.1843 0.2219 -0.0061 0.0060  -0.0360 196 PHE A CA  
1569 C C   . PHE A 197 ? 0.1950 0.2038 0.2448 -0.0064 0.0075  -0.0364 196 PHE A C   
1570 O O   . PHE A 197 ? 0.1633 0.1746 0.2204 -0.0060 0.0092  -0.0393 196 PHE A O   
1571 C CB  . PHE A 197 ? 0.1424 0.1467 0.1880 -0.0051 0.0008  -0.0349 196 PHE A CB  
1572 C CG  . PHE A 197 ? 0.2107 0.2156 0.2655 -0.0037 -0.0014 -0.0370 196 PHE A CG  
1573 C CD1 . PHE A 197 ? 0.2363 0.2422 0.2972 -0.0027 0.0001  -0.0408 196 PHE A CD1 
1574 C CD2 . PHE A 197 ? 0.1825 0.1875 0.2404 -0.0034 -0.0053 -0.0355 196 PHE A CD2 
1575 C CE1 . PHE A 197 ? 0.2222 0.2288 0.2931 -0.0011 -0.0023 -0.0429 196 PHE A CE1 
1576 C CE2 . PHE A 197 ? 0.1824 0.1881 0.2493 -0.0020 -0.0080 -0.0372 196 PHE A CE2 
1577 C CZ  . PHE A 197 ? 0.2105 0.2169 0.2846 -0.0007 -0.0066 -0.0407 196 PHE A CZ  
1578 N N   . ARG A 198 ? 0.1616 0.1700 0.2092 -0.0073 0.0070  -0.0339 197 ARG A N   
1579 C CA  . ARG A 198 ? 0.1653 0.1755 0.2192 -0.0077 0.0075  -0.0346 197 ARG A CA  
1580 C C   . ARG A 198 ? 0.2231 0.2342 0.2764 -0.0093 0.0120  -0.0336 197 ARG A C   
1581 O O   . ARG A 198 ? 0.2351 0.2476 0.2944 -0.0099 0.0127  -0.0341 197 ARG A O   
1582 C CB  . ARG A 198 ? 0.2065 0.2156 0.2599 -0.0075 0.0034  -0.0334 197 ARG A CB  
1583 C CG  . ARG A 198 ? 0.2280 0.2364 0.2823 -0.0063 -0.0013 -0.0336 197 ARG A CG  
1584 C CD  . ARG A 198 ? 0.3161 0.3258 0.3749 -0.0061 -0.0047 -0.0342 197 ARG A CD  
1585 N NE  . ARG A 198 ? 0.2748 0.2872 0.3434 -0.0058 -0.0040 -0.0369 197 ARG A NE  
1586 C CZ  . ARG A 198 ? 0.3273 0.3417 0.4013 -0.0060 -0.0061 -0.0381 197 ARG A CZ  
1587 N NH1 . ARG A 198 ? 0.3360 0.3500 0.4058 -0.0066 -0.0088 -0.0372 197 ARG A NH1 
1588 N NH2 . ARG A 198 ? 0.2777 0.2950 0.3616 -0.0057 -0.0054 -0.0407 197 ARG A NH2 
1589 N N   . PHE A 199 ? 0.1759 0.1865 0.2226 -0.0101 0.0147  -0.0319 198 PHE A N   
1590 C CA  . PHE A 199 ? 0.2340 0.2453 0.2799 -0.0118 0.0188  -0.0300 198 PHE A CA  
1591 C C   . PHE A 199 ? 0.3877 0.4014 0.4312 -0.0126 0.0231  -0.0309 198 PHE A C   
1592 O O   . PHE A 199 ? 0.4519 0.4657 0.4905 -0.0142 0.0261  -0.0282 198 PHE A O   
1593 C CB  . PHE A 199 ? 0.1850 0.1937 0.2248 -0.0123 0.0180  -0.0262 198 PHE A CB  
1594 C CG  . PHE A 199 ? 0.2247 0.2318 0.2672 -0.0117 0.0147  -0.0261 198 PHE A CG  
1595 C CD1 . PHE A 199 ? 0.1916 0.1979 0.2324 -0.0105 0.0108  -0.0270 198 PHE A CD1 
1596 C CD2 . PHE A 199 ? 0.2371 0.2436 0.2837 -0.0127 0.0157  -0.0251 198 PHE A CD2 
1597 C CE1 . PHE A 199 ? 0.2351 0.2408 0.2774 -0.0102 0.0081  -0.0272 198 PHE A CE1 
1598 C CE2 . PHE A 199 ? 0.2269 0.2324 0.2758 -0.0123 0.0129  -0.0259 198 PHE A CE2 
1599 C CZ  . PHE A 199 ? 0.2447 0.2502 0.2910 -0.0111 0.0092  -0.0271 198 PHE A CZ  
1600 N N   . SER A 200 ? 0.4737 0.4892 0.5207 -0.0116 0.0232  -0.0348 199 SER A N   
1601 C CA  . SER A 200 ? 0.5640 0.5824 0.6092 -0.0122 0.0274  -0.0371 199 SER A CA  
1602 C C   . SER A 200 ? 0.6211 0.6436 0.6721 -0.0138 0.0325  -0.0382 199 SER A C   
1603 O O   . SER A 200 ? 0.6433 0.6686 0.6903 -0.0152 0.0371  -0.0387 199 SER A O   
1604 C CB  . SER A 200 ? 0.5661 0.5848 0.6145 -0.0103 0.0255  -0.0415 199 SER A CB  
1605 O OG  . SER A 200 ? 0.5597 0.5796 0.6189 -0.0090 0.0239  -0.0441 199 SER A OG  
1606 N N   . SER A 201 ? 0.5991 0.6223 0.6592 -0.0138 0.0319  -0.0386 200 SER A N   
1607 C CA  . SER A 201 ? 0.5950 0.6223 0.6618 -0.0157 0.0370  -0.0395 200 SER A CA  
1608 C C   . SER A 201 ? 0.5922 0.6190 0.6533 -0.0184 0.0406  -0.0346 200 SER A C   
1609 O O   . SER A 201 ? 0.6021 0.6326 0.6654 -0.0206 0.0460  -0.0346 200 SER A O   
1610 C CB  . SER A 201 ? 0.5449 0.5732 0.6236 -0.0152 0.0348  -0.0411 200 SER A CB  
1611 O OG  . SER A 201 ? 0.5444 0.5732 0.6292 -0.0126 0.0311  -0.0450 200 SER A OG  
1612 N N   . ASP A 202 ? 0.5653 0.5877 0.6198 -0.0185 0.0377  -0.0303 201 ASP A N   
1613 C CA  . ASP A 202 ? 0.5785 0.5996 0.6286 -0.0208 0.0401  -0.0250 201 ASP A CA  
1614 C C   . ASP A 202 ? 0.6098 0.6269 0.6500 -0.0199 0.0368  -0.0217 201 ASP A C   
1615 O O   . ASP A 202 ? 0.5865 0.6001 0.6277 -0.0190 0.0330  -0.0201 201 ASP A O   
1616 C CB  . ASP A 202 ? 0.5890 0.6090 0.6479 -0.0219 0.0400  -0.0236 201 ASP A CB  
1617 C CG  . ASP A 202 ? 0.6415 0.6602 0.6980 -0.0247 0.0432  -0.0180 201 ASP A CG  
1618 O OD1 . ASP A 202 ? 0.6543 0.6734 0.7015 -0.0258 0.0454  -0.0148 201 ASP A OD1 
1619 O OD2 . ASP A 202 ? 0.6692 0.6866 0.7334 -0.0258 0.0433  -0.0166 201 ASP A OD2 
1620 N N   . GLY A 203 ? 0.6596 0.6778 0.6907 -0.0203 0.0381  -0.0211 202 GLY A N   
1621 C CA  . GLY A 203 ? 0.6842 0.6994 0.7065 -0.0195 0.0348  -0.0182 202 GLY A CA  
1622 C C   . GLY A 203 ? 0.6955 0.7075 0.7163 -0.0205 0.0339  -0.0124 202 GLY A C   
1623 O O   . GLY A 203 ? 0.6642 0.6732 0.6820 -0.0192 0.0301  -0.0106 202 GLY A O   
1624 N N   . ASN A 204 ? 0.7320 0.7446 0.7556 -0.0228 0.0375  -0.0093 203 ASN A N   
1625 C CA  . ASN A 204 ? 0.7507 0.7596 0.7748 -0.0236 0.0365  -0.0037 203 ASN A CA  
1626 C C   . ASN A 204 ? 0.6762 0.6820 0.7085 -0.0220 0.0330  -0.0051 203 ASN A C   
1627 O O   . ASN A 204 ? 0.6679 0.6701 0.6999 -0.0214 0.0303  -0.0020 203 ASN A O   
1628 C CB  . ASN A 204 ? 0.8659 0.8761 0.8922 -0.0268 0.0413  0.0002  203 ASN A CB  
1629 C CG  . ASN A 204 ? 0.9400 0.9459 0.9665 -0.0279 0.0402  0.0070  203 ASN A CG  
1630 O OD1 . ASN A 204 ? 0.9659 0.9693 1.0017 -0.0283 0.0399  0.0077  203 ASN A OD1 
1631 N ND2 . ASN A 204 ? 0.9604 0.9654 0.9774 -0.0282 0.0392  0.0118  203 ASN A ND2 
1632 N N   . ALA A 205 ? 0.5973 0.6046 0.6369 -0.0212 0.0327  -0.0100 204 ALA A N   
1633 C CA  . ALA A 205 ? 0.5349 0.5401 0.5814 -0.0199 0.0293  -0.0121 204 ALA A CA  
1634 C C   . ALA A 205 ? 0.5026 0.5063 0.5447 -0.0175 0.0249  -0.0138 204 ALA A C   
1635 O O   . ALA A 205 ? 0.4862 0.4883 0.5321 -0.0165 0.0220  -0.0152 204 ALA A O   
1636 C CB  . ALA A 205 ? 0.4622 0.4700 0.5178 -0.0200 0.0300  -0.0166 204 ALA A CB  
1637 N N   . ALA A 206 ? 0.4839 0.4885 0.5182 -0.0167 0.0244  -0.0138 205 ALA A N   
1638 C CA  . ALA A 206 ? 0.4656 0.4695 0.4968 -0.0148 0.0205  -0.0157 205 ALA A CA  
1639 C C   . ALA A 206 ? 0.4958 0.4970 0.5248 -0.0141 0.0181  -0.0130 205 ALA A C   
1640 O O   . ALA A 206 ? 0.5455 0.5455 0.5716 -0.0149 0.0190  -0.0090 205 ALA A O   
1641 C CB  . ALA A 206 ? 0.4582 0.4636 0.4829 -0.0144 0.0207  -0.0168 205 ALA A CB  
1642 N N   . PRO A 207 ? 0.4148 0.4153 0.4452 -0.0128 0.0150  -0.0150 206 PRO A N   
1643 C CA  . PRO A 207 ? 0.3771 0.3759 0.4059 -0.0120 0.0130  -0.0132 206 PRO A CA  
1644 C C   . PRO A 207 ? 0.4028 0.4018 0.4242 -0.0116 0.0120  -0.0114 206 PRO A C   
1645 O O   . PRO A 207 ? 0.4098 0.4099 0.4281 -0.0111 0.0108  -0.0134 206 PRO A O   
1646 C CB  . PRO A 207 ? 0.3757 0.3749 0.4073 -0.0110 0.0106  -0.0166 206 PRO A CB  
1647 C CG  . PRO A 207 ? 0.3876 0.3885 0.4190 -0.0109 0.0102  -0.0192 206 PRO A CG  
1648 C CD  . PRO A 207 ? 0.3571 0.3588 0.3904 -0.0120 0.0132  -0.0189 206 PRO A CD  
1649 N N   . LEU A 208 ? 0.3404 0.3383 0.3595 -0.0118 0.0121  -0.0076 207 LEU A N   
1650 C CA  . LEU A 208 ? 0.4317 0.4303 0.4439 -0.0117 0.0110  -0.0058 207 LEU A CA  
1651 C C   . LEU A 208 ? 0.3704 0.3696 0.3815 -0.0105 0.0082  -0.0079 207 LEU A C   
1652 O O   . LEU A 208 ? 0.3810 0.3798 0.3960 -0.0097 0.0071  -0.0094 207 LEU A O   
1653 C CB  . LEU A 208 ? 0.5416 0.5388 0.5527 -0.0120 0.0106  -0.0009 207 LEU A CB  
1654 C CG  . LEU A 208 ? 0.5885 0.5853 0.5990 -0.0137 0.0135  0.0024  207 LEU A CG  
1655 C CD1 . LEU A 208 ? 0.6490 0.6437 0.6593 -0.0139 0.0124  0.0081  207 LEU A CD1 
1656 C CD2 . LEU A 208 ? 0.5342 0.5336 0.5375 -0.0149 0.0154  0.0016  207 LEU A CD2 
1657 N N   . GLY A 209 ? 0.2822 0.2825 0.2878 -0.0106 0.0073  -0.0082 208 GLY A N   
1658 C CA  . GLY A 209 ? 0.2724 0.2733 0.2770 -0.0099 0.0048  -0.0094 208 GLY A CA  
1659 C C   . GLY A 209 ? 0.1988 0.1995 0.2052 -0.0091 0.0032  -0.0073 208 GLY A C   
1660 O O   . GLY A 209 ? 0.2530 0.2544 0.2614 -0.0085 0.0019  -0.0087 208 GLY A O   
1661 N N   . ILE A 210 ? 0.2681 0.2681 0.2740 -0.0092 0.0032  -0.0038 209 ILE A N   
1662 C CA  . ILE A 210 ? 0.2611 0.2608 0.2704 -0.0081 0.0015  -0.0018 209 ILE A CA  
1663 C C   . ILE A 210 ? 0.2507 0.2495 0.2671 -0.0074 0.0022  -0.0037 209 ILE A C   
1664 O O   . ILE A 210 ? 0.2904 0.2900 0.3104 -0.0064 0.0011  -0.0048 209 ILE A O   
1665 C CB  . ILE A 210 ? 0.2765 0.2752 0.2842 -0.0084 0.0010  0.0030  209 ILE A CB  
1666 C CG1 . ILE A 210 ? 0.3170 0.3150 0.3307 -0.0069 -0.0010 0.0050  209 ILE A CG1 
1667 C CG2 . ILE A 210 ? 0.2877 0.2846 0.2960 -0.0095 0.0036  0.0047  209 ILE A CG2 
1668 C CD1 . ILE A 210 ? 0.3237 0.3241 0.3374 -0.0060 -0.0035 0.0041  209 ILE A CD1 
1669 N N   . GLY A 211 ? 0.2336 0.2310 0.2524 -0.0080 0.0042  -0.0045 210 GLY A N   
1670 C CA  . GLY A 211 ? 0.2500 0.2468 0.2754 -0.0075 0.0047  -0.0072 210 GLY A CA  
1671 C C   . GLY A 211 ? 0.2458 0.2447 0.2707 -0.0072 0.0040  -0.0111 210 GLY A C   
1672 O O   . GLY A 211 ? 0.2011 0.2008 0.2298 -0.0064 0.0036  -0.0132 210 GLY A O   
1673 N N   . LEU A 212 ? 0.2114 0.2114 0.2318 -0.0078 0.0039  -0.0123 211 LEU A N   
1674 C CA  . LEU A 212 ? 0.2253 0.2271 0.2447 -0.0078 0.0029  -0.0150 211 LEU A CA  
1675 C C   . LEU A 212 ? 0.1927 0.1962 0.2109 -0.0074 0.0017  -0.0145 211 LEU A C   
1676 O O   . LEU A 212 ? 0.1848 0.1901 0.2038 -0.0074 0.0015  -0.0165 211 LEU A O   
1677 C CB  . LEU A 212 ? 0.2527 0.2547 0.2688 -0.0085 0.0027  -0.0157 211 LEU A CB  
1678 C CG  . LEU A 212 ? 0.2961 0.2972 0.3143 -0.0088 0.0040  -0.0166 211 LEU A CG  
1679 C CD1 . LEU A 212 ? 0.3072 0.3086 0.3229 -0.0092 0.0038  -0.0174 211 LEU A CD1 
1680 C CD2 . LEU A 212 ? 0.3023 0.3040 0.3247 -0.0088 0.0038  -0.0192 211 LEU A CD2 
1681 N N   . THR A 213 ? 0.1610 0.1644 0.1771 -0.0073 0.0010  -0.0120 212 THR A N   
1682 C CA  . THR A 213 ? 0.1670 0.1724 0.1830 -0.0070 -0.0003 -0.0115 212 THR A CA  
1683 C C   . THR A 213 ? 0.1959 0.2022 0.2178 -0.0059 0.0000  -0.0122 212 THR A C   
1684 O O   . THR A 213 ? 0.1799 0.1889 0.2034 -0.0058 0.0000  -0.0140 212 THR A O   
1685 C CB  . THR A 213 ? 0.1827 0.1879 0.1954 -0.0072 -0.0016 -0.0088 212 THR A CB  
1686 O OG1 . THR A 213 ? 0.2083 0.2127 0.2162 -0.0081 -0.0014 -0.0091 212 THR A OG1 
1687 C CG2 . THR A 213 ? 0.1767 0.1843 0.1900 -0.0070 -0.0032 -0.0085 212 THR A CG2 
1688 N N   . ALA A 214 ? 0.2054 0.2096 0.2311 -0.0052 0.0004  -0.0108 213 ALA A N   
1689 C CA  . ALA A 214 ? 0.2168 0.2213 0.2497 -0.0039 0.0006  -0.0120 213 ALA A CA  
1690 C C   . ALA A 214 ? 0.1753 0.1810 0.2106 -0.0040 0.0020  -0.0166 213 ALA A C   
1691 O O   . ALA A 214 ? 0.1874 0.1957 0.2266 -0.0033 0.0024  -0.0193 213 ALA A O   
1692 C CB  . ALA A 214 ? 0.1917 0.1928 0.2286 -0.0032 0.0004  -0.0090 213 ALA A CB  
1693 N N   . ALA A 215 ? 0.1616 0.1661 0.1947 -0.0049 0.0027  -0.0177 214 ALA A N   
1694 C CA  . ALA A 215 ? 0.1837 0.1899 0.2180 -0.0053 0.0034  -0.0221 214 ALA A CA  
1695 C C   . ALA A 215 ? 0.2260 0.2360 0.2564 -0.0059 0.0032  -0.0236 214 ALA A C   
1696 O O   . ALA A 215 ? 0.2006 0.2134 0.2329 -0.0058 0.0040  -0.0271 214 ALA A O   
1697 C CB  . ALA A 215 ? 0.1813 0.1860 0.2139 -0.0062 0.0036  -0.0227 214 ALA A CB  
1698 N N   . ALA A 216 ? 0.1955 0.2059 0.2206 -0.0066 0.0023  -0.0212 215 ALA A N   
1699 C CA  . ALA A 216 ? 0.1710 0.1846 0.1929 -0.0076 0.0022  -0.0218 215 ALA A CA  
1700 C C   . ALA A 216 ? 0.1658 0.1824 0.1916 -0.0069 0.0028  -0.0226 215 ALA A C   
1701 O O   . ALA A 216 ? 0.2166 0.2370 0.2422 -0.0076 0.0039  -0.0249 215 ALA A O   
1702 C CB  . ALA A 216 ? 0.1575 0.1703 0.1745 -0.0085 0.0009  -0.0191 215 ALA A CB  
1703 N N   . TYR A 217 ? 0.1668 0.1822 0.1963 -0.0057 0.0022  -0.0206 216 TYR A N   
1704 C CA  . TYR A 217 ? 0.1869 0.2052 0.2221 -0.0046 0.0026  -0.0216 216 TYR A CA  
1705 C C   . TYR A 217 ? 0.1876 0.2079 0.2279 -0.0039 0.0045  -0.0262 216 TYR A C   
1706 O O   . TYR A 217 ? 0.1713 0.1962 0.2139 -0.0040 0.0059  -0.0289 216 TYR A O   
1707 C CB  . TYR A 217 ? 0.2052 0.2213 0.2445 -0.0031 0.0010  -0.0185 216 TYR A CB  
1708 C CG  . TYR A 217 ? 0.1982 0.2171 0.2456 -0.0015 0.0010  -0.0198 216 TYR A CG  
1709 C CD1 . TYR A 217 ? 0.2080 0.2308 0.2565 -0.0017 0.0004  -0.0193 216 TYR A CD1 
1710 C CD2 . TYR A 217 ? 0.2306 0.2484 0.2860 0.0002  0.0017  -0.0219 216 TYR A CD2 
1711 C CE1 . TYR A 217 ? 0.2196 0.2455 0.2770 -0.0001 0.0005  -0.0208 216 TYR A CE1 
1712 C CE2 . TYR A 217 ? 0.2286 0.2491 0.2930 0.0019  0.0018  -0.0236 216 TYR A CE2 
1713 C CZ  . TYR A 217 ? 0.2374 0.2622 0.3028 0.0018  0.0012  -0.0230 216 TYR A CZ  
1714 O OH  . TYR A 217 ? 0.2592 0.2872 0.3349 0.0038  0.0013  -0.0251 216 TYR A OH  
1715 N N   . TRP A 218 ? 0.1539 0.1712 0.1964 -0.0034 0.0048  -0.0275 217 TRP A N   
1716 C CA  . TRP A 218 ? 0.2268 0.2459 0.2749 -0.0027 0.0064  -0.0327 217 TRP A CA  
1717 C C   . TRP A 218 ? 0.2296 0.2524 0.2724 -0.0043 0.0076  -0.0364 217 TRP A C   
1718 O O   . TRP A 218 ? 0.2251 0.2520 0.2706 -0.0042 0.0094  -0.0410 217 TRP A O   
1719 C CB  . TRP A 218 ? 0.2057 0.2202 0.2589 -0.0018 0.0061  -0.0331 217 TRP A CB  
1720 C CG  . TRP A 218 ? 0.2076 0.2186 0.2672 -0.0002 0.0049  -0.0296 217 TRP A CG  
1721 C CD1 . TRP A 218 ? 0.1744 0.1811 0.2328 -0.0003 0.0037  -0.0246 217 TRP A CD1 
1722 C CD2 . TRP A 218 ? 0.2144 0.2264 0.2830 0.0018  0.0048  -0.0305 217 TRP A CD2 
1723 N NE1 . TRP A 218 ? 0.1879 0.1925 0.2529 0.0013  0.0025  -0.0218 217 TRP A NE1 
1724 C CE2 . TRP A 218 ? 0.1880 0.1955 0.2600 0.0028  0.0029  -0.0253 217 TRP A CE2 
1725 C CE3 . TRP A 218 ? 0.2681 0.2847 0.3424 0.0028  0.0062  -0.0353 217 TRP A CE3 
1726 C CZ2 . TRP A 218 ? 0.2160 0.2230 0.2974 0.0049  0.0017  -0.0243 217 TRP A CZ2 
1727 C CZ3 . TRP A 218 ? 0.2865 0.3028 0.3711 0.0051  0.0054  -0.0350 217 TRP A CZ3 
1728 C CH2 . TRP A 218 ? 0.2638 0.2751 0.3521 0.0062  0.0028  -0.0293 217 TRP A CH2 
1729 N N   . TRP A 219 ? 0.2123 0.2340 0.2477 -0.0059 0.0066  -0.0345 218 TRP A N   
1730 C CA  . TRP A 219 ? 0.1747 0.1989 0.2056 -0.0073 0.0070  -0.0376 218 TRP A CA  
1731 C C   . TRP A 219 ? 0.2080 0.2343 0.2306 -0.0093 0.0064  -0.0353 218 TRP A C   
1732 O O   . TRP A 219 ? 0.2433 0.2724 0.2616 -0.0106 0.0065  -0.0375 218 TRP A O   
1733 C CB  . TRP A 219 ? 0.2072 0.2278 0.2388 -0.0072 0.0060  -0.0384 218 TRP A CB  
1734 C CG  . TRP A 219 ? 0.2125 0.2311 0.2528 -0.0057 0.0067  -0.0412 218 TRP A CG  
1735 C CD1 . TRP A 219 ? 0.2573 0.2784 0.3034 -0.0049 0.0082  -0.0461 218 TRP A CD1 
1736 C CD2 . TRP A 219 ? 0.1900 0.2036 0.2349 -0.0051 0.0061  -0.0393 218 TRP A CD2 
1737 N NE1 . TRP A 219 ? 0.2302 0.2475 0.2848 -0.0036 0.0082  -0.0472 218 TRP A NE1 
1738 C CE2 . TRP A 219 ? 0.2234 0.2361 0.2771 -0.0038 0.0069  -0.0428 218 TRP A CE2 
1739 C CE3 . TRP A 219 ? 0.2555 0.2656 0.2983 -0.0055 0.0051  -0.0352 218 TRP A CE3 
1740 C CZ2 . TRP A 219 ? 0.2378 0.2458 0.2982 -0.0033 0.0066  -0.0414 218 TRP A CZ2 
1741 C CZ3 . TRP A 219 ? 0.2803 0.2864 0.3290 -0.0051 0.0053  -0.0341 218 TRP A CZ3 
1742 C CH2 . TRP A 219 ? 0.2419 0.2467 0.2992 -0.0040 0.0059  -0.0368 218 TRP A CH2 
1743 N N   . PHE A 220 ? 0.2014 0.2264 0.2217 -0.0096 0.0054  -0.0310 219 PHE A N   
1744 C CA  . PHE A 220 ? 0.1719 0.1984 0.1856 -0.0116 0.0046  -0.0287 219 PHE A CA  
1745 C C   . PHE A 220 ? 0.1730 0.2052 0.1851 -0.0130 0.0066  -0.0305 219 PHE A C   
1746 O O   . PHE A 220 ? 0.1997 0.2348 0.2164 -0.0123 0.0084  -0.0322 219 PHE A O   
1747 C CB  . PHE A 220 ? 0.1667 0.1907 0.1794 -0.0117 0.0033  -0.0245 219 PHE A CB  
1748 C CG  . PHE A 220 ? 0.1887 0.2139 0.1963 -0.0138 0.0025  -0.0220 219 PHE A CG  
1749 C CD1 . PHE A 220 ? 0.1878 0.2105 0.1914 -0.0146 0.0006  -0.0203 219 PHE A CD1 
1750 C CD2 . PHE A 220 ? 0.1636 0.1926 0.1713 -0.0151 0.0037  -0.0213 219 PHE A CD2 
1751 C CE1 . PHE A 220 ? 0.1934 0.2165 0.1931 -0.0166 -0.0005 -0.0175 219 PHE A CE1 
1752 C CE2 . PHE A 220 ? 0.1993 0.2291 0.2027 -0.0174 0.0030  -0.0185 219 PHE A CE2 
1753 C CZ  . PHE A 220 ? 0.1520 0.1785 0.1514 -0.0181 0.0008  -0.0164 219 PHE A CZ  
1754 N N   . GLN A 221 ? 0.2068 0.2410 0.2124 -0.0150 0.0061  -0.0300 220 GLN A N   
1755 C CA  . GLN A 221 ? 0.1982 0.2382 0.2003 -0.0171 0.0081  -0.0307 220 GLN A CA  
1756 C C   . GLN A 221 ? 0.2086 0.2481 0.2048 -0.0195 0.0066  -0.0256 220 GLN A C   
1757 O O   . GLN A 221 ? 0.2131 0.2492 0.2058 -0.0198 0.0038  -0.0233 220 GLN A O   
1758 C CB  . GLN A 221 ? 0.2618 0.3060 0.2612 -0.0177 0.0094  -0.0353 220 GLN A CB  
1759 C CG  . GLN A 221 ? 0.3571 0.4016 0.3635 -0.0155 0.0109  -0.0410 220 GLN A CG  
1760 C CD  . GLN A 221 ? 0.4779 0.5261 0.4907 -0.0147 0.0139  -0.0434 220 GLN A CD  
1761 O OE1 . GLN A 221 ? 0.5835 0.6305 0.6044 -0.0123 0.0146  -0.0464 220 GLN A OE1 
1762 N NE2 . GLN A 221 ? 0.4670 0.5199 0.4770 -0.0166 0.0157  -0.0418 220 GLN A NE2 
1763 N N   . VAL A 222 ? 0.2484 0.2913 0.2444 -0.0211 0.0082  -0.0239 221 VAL A N   
1764 C CA  . VAL A 222 ? 0.2324 0.2745 0.2236 -0.0237 0.0067  -0.0188 221 VAL A CA  
1765 C C   . VAL A 222 ? 0.2185 0.2626 0.2020 -0.0258 0.0060  -0.0180 221 VAL A C   
1766 O O   . VAL A 222 ? 0.2174 0.2663 0.1984 -0.0262 0.0080  -0.0218 221 VAL A O   
1767 C CB  . VAL A 222 ? 0.2533 0.2993 0.2468 -0.0254 0.0090  -0.0174 221 VAL A CB  
1768 C CG1 . VAL A 222 ? 0.2775 0.3225 0.2666 -0.0285 0.0076  -0.0119 221 VAL A CG1 
1769 C CG2 . VAL A 222 ? 0.2477 0.2915 0.2485 -0.0233 0.0087  -0.0178 221 VAL A CG2 
1770 N N   . SER A 223 ? 0.1987 0.2391 0.1785 -0.0270 0.0029  -0.0132 222 SER A N   
1771 C CA  . SER A 223 ? 0.2263 0.2686 0.1985 -0.0295 0.0015  -0.0108 222 SER A CA  
1772 C C   . SER A 223 ? 0.2214 0.2630 0.1912 -0.0324 0.0007  -0.0046 222 SER A C   
1773 O O   . SER A 223 ? 0.2046 0.2405 0.1773 -0.0319 -0.0021 -0.0012 222 SER A O   
1774 C CB  . SER A 223 ? 0.2169 0.2551 0.1877 -0.0281 -0.0024 -0.0106 222 SER A CB  
1775 O OG  . SER A 223 ? 0.2171 0.2575 0.1804 -0.0304 -0.0043 -0.0079 222 SER A OG  
1776 N N   . LYS A 224 ? 0.2439 0.2914 0.2087 -0.0356 0.0032  -0.0032 223 LYS A N   
1777 C CA  . LYS A 224 ? 0.2437 0.2909 0.2066 -0.0390 0.0028  0.0031  223 LYS A CA  
1778 C C   . LYS A 224 ? 0.2854 0.3390 0.2393 -0.0428 0.0046  0.0051  223 LYS A C   
1779 O O   . LYS A 224 ? 0.3190 0.3786 0.2691 -0.0428 0.0072  0.0004  223 LYS A O   
1780 C CB  . LYS A 224 ? 0.2687 0.3167 0.2385 -0.0393 0.0054  0.0031  223 LYS A CB  
1781 C CG  . LYS A 224 ? 0.2397 0.2953 0.2115 -0.0394 0.0105  -0.0020 223 LYS A CG  
1782 C CD  . LYS A 224 ? 0.2183 0.2744 0.1984 -0.0393 0.0121  -0.0020 223 LYS A CD  
1783 C CE  . LYS A 224 ? 0.2595 0.3232 0.2437 -0.0388 0.0170  -0.0075 223 LYS A CE  
1784 N NZ  . LYS A 224 ? 0.2235 0.2880 0.2165 -0.0384 0.0179  -0.0076 223 LYS A NZ  
1785 N N   . ARG A 225 ? 0.2957 0.3482 0.2464 -0.0462 0.0031  0.0123  224 ARG A N   
1786 C CA  . ARG A 225 ? 0.3697 0.4279 0.3110 -0.0505 0.0045  0.0161  224 ARG A CA  
1787 C C   . ARG A 225 ? 0.3786 0.4385 0.3217 -0.0543 0.0071  0.0211  224 ARG A C   
1788 O O   . ARG A 225 ? 0.3628 0.4165 0.3121 -0.0542 0.0048  0.0249  224 ARG A O   
1789 C CB  . ARG A 225 ? 0.4473 0.5017 0.3819 -0.0514 -0.0010 0.0216  224 ARG A CB  
1790 C CG  . ARG A 225 ? 0.6072 0.6611 0.5394 -0.0484 -0.0037 0.0170  224 ARG A CG  
1791 C CD  . ARG A 225 ? 0.7185 0.7811 0.6414 -0.0502 -0.0009 0.0133  224 ARG A CD  
1792 N NE  . ARG A 225 ? 0.7780 0.8446 0.6905 -0.0551 -0.0011 0.0200  224 ARG A NE  
1793 C CZ  . ARG A 225 ? 0.8038 0.8688 0.7089 -0.0563 -0.0063 0.0251  224 ARG A CZ  
1794 N NH1 . ARG A 225 ? 0.8335 0.8933 0.7413 -0.0530 -0.0116 0.0238  224 ARG A NH1 
1795 N NH2 . ARG A 225 ? 0.7787 0.8476 0.6738 -0.0611 -0.0063 0.0318  224 ARG A NH2 
1796 N N   . THR A 226 ? 0.4222 0.4909 0.3602 -0.0577 0.0121  0.0206  225 THR A N   
1797 C CA  . THR A 226 ? 0.4796 0.5516 0.4188 -0.0621 0.0153  0.0254  225 THR A CA  
1798 C C   . THR A 226 ? 0.5045 0.5792 0.4323 -0.0671 0.0148  0.0327  225 THR A C   
1799 O O   . THR A 226 ? 0.4890 0.5708 0.4075 -0.0684 0.0170  0.0304  225 THR A O   
1800 C CB  . THR A 226 ? 0.5701 0.6509 0.5135 -0.0624 0.0221  0.0192  225 THR A CB  
1801 O OG1 . THR A 226 ? 0.6122 0.6901 0.5655 -0.0575 0.0217  0.0128  225 THR A OG1 
1802 C CG2 . THR A 226 ? 0.5748 0.6589 0.5216 -0.0669 0.0254  0.0239  225 THR A CG2 
1803 N N   . ASP A 227 ? 0.6030 0.6722 0.5317 -0.0698 0.0117  0.0414  226 ASP A N   
1804 C CA  . ASP A 227 ? 0.6670 0.7376 0.5852 -0.0746 0.0102  0.0499  226 ASP A CA  
1805 C C   . ASP A 227 ? 0.6659 0.7476 0.5777 -0.0796 0.0173  0.0502  226 ASP A C   
1806 O O   . ASP A 227 ? 0.6451 0.7304 0.5644 -0.0810 0.0222  0.0486  226 ASP A O   
1807 C CB  . ASP A 227 ? 0.7091 0.7708 0.6321 -0.0765 0.0056  0.0592  226 ASP A CB  
1808 C CG  . ASP A 227 ? 0.7777 0.8387 0.6904 -0.0807 0.0023  0.0691  226 ASP A CG  
1809 O OD1 . ASP A 227 ? 0.8242 0.8924 0.7296 -0.0862 0.0064  0.0734  226 ASP A OD1 
1810 O OD2 . ASP A 227 ? 0.7985 0.8521 0.7105 -0.0787 -0.0045 0.0726  226 ASP A OD2 
1811 N N   . PRO A 228 ? 0.6654 0.7536 0.5639 -0.0826 0.0182  0.0519  227 PRO A N   
1812 C CA  . PRO A 228 ? 0.6645 0.7647 0.5563 -0.0873 0.0258  0.0509  227 PRO A CA  
1813 C C   . PRO A 228 ? 0.6893 0.7906 0.5809 -0.0935 0.0281  0.0604  227 PRO A C   
1814 O O   . PRO A 228 ? 0.6932 0.8049 0.5811 -0.0977 0.0353  0.0596  227 PRO A O   
1815 C CB  . PRO A 228 ? 0.6566 0.7621 0.5330 -0.0886 0.0249  0.0503  227 PRO A CB  
1816 C CG  . PRO A 228 ? 0.6395 0.7349 0.5136 -0.0869 0.0158  0.0568  227 PRO A CG  
1817 C CD  . PRO A 228 ? 0.6487 0.7342 0.5376 -0.0815 0.0124  0.0539  227 PRO A CD  
1818 N N   . VAL A 229 ? 0.6596 0.7510 0.5558 -0.0943 0.0226  0.0692  228 VAL A N   
1819 C CA  . VAL A 229 ? 0.6681 0.7594 0.5654 -0.1004 0.0241  0.0790  228 VAL A CA  
1820 C C   . VAL A 229 ? 0.6510 0.7375 0.5646 -0.0993 0.0247  0.0780  228 VAL A C   
1821 O O   . VAL A 229 ? 0.6423 0.7349 0.5604 -0.1030 0.0306  0.0783  228 VAL A O   
1822 C CB  . VAL A 229 ? 0.6772 0.7609 0.5676 -0.1030 0.0171  0.0910  228 VAL A CB  
1823 C CG1 . VAL A 229 ? 0.6415 0.7247 0.5338 -0.1096 0.0187  0.1016  228 VAL A CG1 
1824 C CG2 . VAL A 229 ? 0.7101 0.7995 0.5836 -0.1044 0.0160  0.0922  228 VAL A CG2 
1825 N N   . SER A 230 ? 0.6398 0.7157 0.5624 -0.0942 0.0188  0.0763  229 SER A N   
1826 C CA  . SER A 230 ? 0.6173 0.6881 0.5547 -0.0931 0.0184  0.0752  229 SER A CA  
1827 C C   . SER A 230 ? 0.5793 0.6533 0.5249 -0.0883 0.0215  0.0640  229 SER A C   
1828 O O   . SER A 230 ? 0.5362 0.6082 0.4935 -0.0878 0.0220  0.0623  229 SER A O   
1829 C CB  . SER A 230 ? 0.6062 0.6638 0.5494 -0.0905 0.0103  0.0794  229 SER A CB  
1830 O OG  . SER A 230 ? 0.5558 0.6095 0.4969 -0.0847 0.0064  0.0739  229 SER A OG  
1831 N N   . GLN A 231 ? 0.5880 0.6668 0.5280 -0.0849 0.0231  0.0565  230 GLN A N   
1832 C CA  . GLN A 231 ? 0.6058 0.6861 0.5535 -0.0797 0.0248  0.0463  230 GLN A CA  
1833 C C   . GLN A 231 ? 0.5590 0.6287 0.5156 -0.0749 0.0190  0.0449  230 GLN A C   
1834 O O   . GLN A 231 ? 0.5891 0.6588 0.5538 -0.0711 0.0198  0.0380  230 GLN A O   
1835 C CB  . GLN A 231 ? 0.6213 0.7103 0.5766 -0.0814 0.0315  0.0423  230 GLN A CB  
1836 C CG  . GLN A 231 ? 0.6876 0.7889 0.6348 -0.0848 0.0384  0.0402  230 GLN A CG  
1837 C CD  . GLN A 231 ? 0.7326 0.8431 0.6891 -0.0858 0.0452  0.0351  230 GLN A CD  
1838 O OE1 . GLN A 231 ? 0.7137 0.8214 0.6825 -0.0848 0.0444  0.0345  230 GLN A OE1 
1839 N NE2 . GLN A 231 ? 0.7577 0.8796 0.7089 -0.0878 0.0517  0.0309  230 GLN A NE2 
1840 N N   . ASN A 232 ? 0.5095 0.5703 0.4646 -0.0751 0.0131  0.0513  231 ASN A N   
1841 C CA  . ASN A 232 ? 0.4710 0.5220 0.4338 -0.0708 0.0076  0.0498  231 ASN A CA  
1842 C C   . ASN A 232 ? 0.3999 0.4500 0.3604 -0.0654 0.0062  0.0427  231 ASN A C   
1843 O O   . ASN A 232 ? 0.4255 0.4775 0.3771 -0.0651 0.0054  0.0429  231 ASN A O   
1844 C CB  . ASN A 232 ? 0.5321 0.5745 0.4942 -0.0725 0.0019  0.0582  231 ASN A CB  
1845 C CG  . ASN A 232 ? 0.6127 0.6458 0.5857 -0.0700 -0.0023 0.0576  231 ASN A CG  
1846 O OD1 . ASN A 232 ? 0.6429 0.6730 0.6197 -0.0651 -0.0040 0.0514  231 ASN A OD1 
1847 N ND2 . ASN A 232 ? 0.6341 0.6630 0.6125 -0.0736 -0.0038 0.0640  231 ASN A ND2 
1848 N N   . VAL A 233 ? 0.3641 0.4115 0.3328 -0.0612 0.0056  0.0368  232 VAL A N   
1849 C CA  . VAL A 233 ? 0.3413 0.3884 0.3093 -0.0563 0.0051  0.0299  232 VAL A CA  
1850 C C   . VAL A 233 ? 0.3063 0.3441 0.2767 -0.0531 -0.0007 0.0307  232 VAL A C   
1851 O O   . VAL A 233 ? 0.2881 0.3200 0.2654 -0.0527 -0.0032 0.0322  232 VAL A O   
1852 C CB  . VAL A 233 ? 0.3281 0.3790 0.3032 -0.0538 0.0085  0.0230  232 VAL A CB  
1853 C CG1 . VAL A 233 ? 0.3397 0.3885 0.3155 -0.0488 0.0072  0.0168  232 VAL A CG1 
1854 C CG2 . VAL A 233 ? 0.2917 0.3527 0.2650 -0.0565 0.0145  0.0211  232 VAL A CG2 
1855 N N   . THR A 234 ? 0.2893 0.3261 0.2543 -0.0510 -0.0029 0.0292  233 THR A N   
1856 C CA  . THR A 234 ? 0.2998 0.3291 0.2676 -0.0475 -0.0078 0.0287  233 THR A CA  
1857 C C   . THR A 234 ? 0.2607 0.2912 0.2289 -0.0434 -0.0069 0.0215  233 THR A C   
1858 O O   . THR A 234 ? 0.2778 0.3141 0.2409 -0.0434 -0.0044 0.0184  233 THR A O   
1859 C CB  . THR A 234 ? 0.3571 0.3832 0.3194 -0.0488 -0.0122 0.0346  233 THR A CB  
1860 O OG1 . THR A 234 ? 0.3958 0.4285 0.3485 -0.0505 -0.0106 0.0347  233 THR A OG1 
1861 C CG2 . THR A 234 ? 0.4075 0.4300 0.3717 -0.0525 -0.0141 0.0424  233 THR A CG2 
1862 N N   . TYR A 235 ? 0.2461 0.2711 0.2204 -0.0400 -0.0089 0.0188  234 TYR A N   
1863 C CA  . TYR A 235 ? 0.1992 0.2247 0.1747 -0.0363 -0.0082 0.0127  234 TYR A CA  
1864 C C   . TYR A 235 ? 0.2305 0.2527 0.2041 -0.0345 -0.0120 0.0129  234 TYR A C   
1865 O O   . TYR A 235 ? 0.2416 0.2592 0.2155 -0.0351 -0.0158 0.0173  234 TYR A O   
1866 C CB  . TYR A 235 ? 0.2269 0.2496 0.2096 -0.0338 -0.0077 0.0094  234 TYR A CB  
1867 C CG  . TYR A 235 ? 0.2784 0.3061 0.2635 -0.0347 -0.0039 0.0075  234 TYR A CG  
1868 C CD1 . TYR A 235 ? 0.2956 0.3242 0.2829 -0.0376 -0.0031 0.0107  234 TYR A CD1 
1869 C CD2 . TYR A 235 ? 0.2738 0.3054 0.2599 -0.0327 -0.0010 0.0024  234 TYR A CD2 
1870 C CE1 . TYR A 235 ? 0.2927 0.3266 0.2833 -0.0385 0.0003  0.0088  234 TYR A CE1 
1871 C CE2 . TYR A 235 ? 0.2649 0.3014 0.2545 -0.0333 0.0022  0.0005  234 TYR A CE2 
1872 C CZ  . TYR A 235 ? 0.2775 0.3154 0.2693 -0.0361 0.0029  0.0037  234 TYR A CZ  
1873 O OH  . TYR A 235 ? 0.2670 0.3103 0.2633 -0.0367 0.0061  0.0016  234 TYR A OH  
1874 N N   . ASP A 236 ? 0.2196 0.2440 0.1919 -0.0324 -0.0111 0.0080  235 ASP A N   
1875 C CA  . ASP A 236 ? 0.2247 0.2473 0.1955 -0.0308 -0.0144 0.0074  235 ASP A CA  
1876 C C   . ASP A 236 ? 0.2029 0.2234 0.1792 -0.0272 -0.0137 0.0022  235 ASP A C   
1877 O O   . ASP A 236 ? 0.2320 0.2558 0.2078 -0.0262 -0.0117 -0.0023 235 ASP A O   
1878 C CB  . ASP A 236 ? 0.2371 0.2654 0.2001 -0.0325 -0.0139 0.0069  235 ASP A CB  
1879 C CG  . ASP A 236 ? 0.2493 0.2762 0.2104 -0.0314 -0.0183 0.0072  235 ASP A CG  
1880 O OD1 . ASP A 236 ? 0.2509 0.2730 0.2180 -0.0288 -0.0207 0.0061  235 ASP A OD1 
1881 O OD2 . ASP A 236 ? 0.2862 0.3173 0.2400 -0.0333 -0.0193 0.0082  235 ASP A OD2 
1882 N N   . ASP A 237 ? 0.1677 0.1829 0.1497 -0.0256 -0.0154 0.0026  236 ASP A N   
1883 C CA  . ASP A 237 ? 0.1757 0.1891 0.1624 -0.0227 -0.0145 -0.0017 236 ASP A CA  
1884 C C   . ASP A 237 ? 0.2050 0.2187 0.1917 -0.0211 -0.0159 -0.0042 236 ASP A C   
1885 O O   . ASP A 237 ? 0.1976 0.2121 0.1866 -0.0194 -0.0140 -0.0082 236 ASP A O   
1886 C CB  . ASP A 237 ? 0.2081 0.2163 0.1999 -0.0216 -0.0159 -0.0009 236 ASP A CB  
1887 C CG  . ASP A 237 ? 0.2071 0.2152 0.2002 -0.0227 -0.0143 0.0001  236 ASP A CG  
1888 O OD1 . ASP A 237 ? 0.1863 0.1982 0.1767 -0.0247 -0.0124 0.0012  236 ASP A OD1 
1889 O OD2 . ASP A 237 ? 0.1746 0.1793 0.1718 -0.0217 -0.0150 -0.0006 236 ASP A OD2 
1890 N N   . ARG A 238 ? 0.2181 0.2311 0.2029 -0.0218 -0.0195 -0.0016 237 ARG A N   
1891 C CA  . ARG A 238 ? 0.2015 0.2152 0.1869 -0.0204 -0.0213 -0.0041 237 ARG A CA  
1892 C C   . ARG A 238 ? 0.2218 0.2407 0.2034 -0.0209 -0.0189 -0.0078 237 ARG A C   
1893 O O   . ARG A 238 ? 0.1827 0.2021 0.1675 -0.0193 -0.0180 -0.0121 237 ARG A O   
1894 C CB  . ARG A 238 ? 0.1996 0.2123 0.1837 -0.0211 -0.0262 -0.0002 237 ARG A CB  
1895 C CG  . ARG A 238 ? 0.2090 0.2222 0.1957 -0.0195 -0.0289 -0.0028 237 ARG A CG  
1896 C CD  . ARG A 238 ? 0.2276 0.2428 0.2093 -0.0210 -0.0335 0.0005  237 ARG A CD  
1897 N NE  . ARG A 238 ? 0.2688 0.2889 0.2414 -0.0236 -0.0318 0.0011  237 ARG A NE  
1898 C CZ  . ARG A 238 ? 0.2608 0.2855 0.2302 -0.0238 -0.0294 -0.0037 237 ARG A CZ  
1899 N NH1 . ARG A 238 ? 0.1853 0.2099 0.1601 -0.0217 -0.0288 -0.0090 237 ARG A NH1 
1900 N NH2 . ARG A 238 ? 0.2629 0.2925 0.2242 -0.0263 -0.0275 -0.0035 237 ARG A NH2 
1901 N N   . ASP A 239 ? 0.2330 0.2559 0.2083 -0.0233 -0.0177 -0.0064 238 ASP A N   
1902 C CA  . ASP A 239 ? 0.2321 0.2603 0.2041 -0.0238 -0.0151 -0.0108 238 ASP A CA  
1903 C C   . ASP A 239 ? 0.2010 0.2294 0.1779 -0.0222 -0.0109 -0.0150 238 ASP A C   
1904 O O   . ASP A 239 ? 0.2015 0.2319 0.1802 -0.0212 -0.0095 -0.0199 238 ASP A O   
1905 C CB  . ASP A 239 ? 0.2328 0.2660 0.1967 -0.0270 -0.0141 -0.0084 238 ASP A CB  
1906 C CG  . ASP A 239 ? 0.2823 0.3217 0.2430 -0.0275 -0.0110 -0.0139 238 ASP A CG  
1907 O OD1 . ASP A 239 ? 0.2819 0.3228 0.2412 -0.0270 -0.0127 -0.0173 238 ASP A OD1 
1908 O OD2 . ASP A 239 ? 0.2668 0.3096 0.2269 -0.0285 -0.0069 -0.0153 238 ASP A OD2 
1909 N N   . ALA A 240 ? 0.1876 0.2141 0.1671 -0.0222 -0.0093 -0.0130 239 ALA A N   
1910 C CA  . ALA A 240 ? 0.2057 0.2322 0.1901 -0.0206 -0.0061 -0.0163 239 ALA A CA  
1911 C C   . ALA A 240 ? 0.2130 0.2363 0.2027 -0.0181 -0.0067 -0.0189 239 ALA A C   
1912 O O   . ALA A 240 ? 0.1993 0.2237 0.1922 -0.0169 -0.0046 -0.0227 239 ALA A O   
1913 C CB  . ALA A 240 ? 0.2096 0.2345 0.1960 -0.0209 -0.0052 -0.0134 239 ALA A CB  
1914 N N   . LEU A 241 ? 0.1648 0.1841 0.1562 -0.0174 -0.0093 -0.0169 240 LEU A N   
1915 C CA  . LEU A 241 ? 0.1711 0.1878 0.1674 -0.0154 -0.0095 -0.0191 240 LEU A CA  
1916 C C   . LEU A 241 ? 0.1522 0.1710 0.1488 -0.0152 -0.0102 -0.0225 240 LEU A C   
1917 O O   . LEU A 241 ? 0.1841 0.2023 0.1852 -0.0140 -0.0088 -0.0255 240 LEU A O   
1918 C CB  . LEU A 241 ? 0.1908 0.2037 0.1893 -0.0148 -0.0120 -0.0168 240 LEU A CB  
1919 C CG  . LEU A 241 ? 0.3181 0.3278 0.3190 -0.0142 -0.0111 -0.0155 240 LEU A CG  
1920 C CD1 . LEU A 241 ? 0.3373 0.3439 0.3410 -0.0135 -0.0136 -0.0143 240 LEU A CD1 
1921 C CD2 . LEU A 241 ? 0.2858 0.2951 0.2897 -0.0129 -0.0084 -0.0177 240 LEU A CD2 
1922 N N   . GLU A 242 ? 0.1666 0.1879 0.1586 -0.0166 -0.0125 -0.0219 241 GLU A N   
1923 C CA  . GLU A 242 ? 0.2115 0.2355 0.2035 -0.0166 -0.0135 -0.0257 241 GLU A CA  
1924 C C   . GLU A 242 ? 0.2411 0.2679 0.2341 -0.0165 -0.0101 -0.0303 241 GLU A C   
1925 O O   . GLU A 242 ? 0.2305 0.2568 0.2283 -0.0154 -0.0096 -0.0342 241 GLU A O   
1926 C CB  . GLU A 242 ? 0.2291 0.2560 0.2143 -0.0184 -0.0168 -0.0239 241 GLU A CB  
1927 C CG  . GLU A 242 ? 0.2409 0.2708 0.2258 -0.0186 -0.0187 -0.0281 241 GLU A CG  
1928 C CD  . GLU A 242 ? 0.2622 0.2961 0.2385 -0.0207 -0.0218 -0.0264 241 GLU A CD  
1929 O OE1 . GLU A 242 ? 0.2835 0.3164 0.2558 -0.0218 -0.0240 -0.0208 241 GLU A OE1 
1930 O OE2 . GLU A 242 ? 0.3209 0.3590 0.2946 -0.0214 -0.0223 -0.0308 241 GLU A OE2 
1931 N N   . GLN A 243 ? 0.2093 0.2388 0.1986 -0.0175 -0.0077 -0.0300 242 GLN A N   
1932 C CA  . GLN A 243 ? 0.2163 0.2487 0.2079 -0.0171 -0.0044 -0.0348 242 GLN A CA  
1933 C C   . GLN A 243 ? 0.1978 0.2264 0.1973 -0.0150 -0.0027 -0.0359 242 GLN A C   
1934 O O   . GLN A 243 ? 0.1817 0.2106 0.1861 -0.0141 -0.0015 -0.0403 242 GLN A O   
1935 C CB  . GLN A 243 ? 0.2219 0.2582 0.2094 -0.0186 -0.0019 -0.0341 242 GLN A CB  
1936 C CG  . GLN A 243 ? 0.3102 0.3512 0.2889 -0.0212 -0.0028 -0.0327 242 GLN A CG  
1937 C CD  . GLN A 243 ? 0.4362 0.4819 0.4121 -0.0228 0.0008  -0.0327 242 GLN A CD  
1938 O OE1 . GLN A 243 ? 0.5230 0.5705 0.4928 -0.0251 0.0004  -0.0283 242 GLN A OE1 
1939 N NE2 . GLN A 243 ? 0.3934 0.4412 0.3746 -0.0216 0.0043  -0.0374 242 GLN A NE2 
1940 N N   . PHE A 244 ? 0.1863 0.2116 0.1873 -0.0144 -0.0026 -0.0319 243 PHE A N   
1941 C CA  . PHE A 244 ? 0.1705 0.1925 0.1777 -0.0127 -0.0011 -0.0321 243 PHE A CA  
1942 C C   . PHE A 244 ? 0.1985 0.2177 0.2103 -0.0117 -0.0020 -0.0336 243 PHE A C   
1943 O O   . PHE A 244 ? 0.1857 0.2038 0.2032 -0.0107 -0.0005 -0.0358 243 PHE A O   
1944 C CB  . PHE A 244 ? 0.1482 0.1677 0.1546 -0.0126 -0.0014 -0.0277 243 PHE A CB  
1945 C CG  . PHE A 244 ? 0.2011 0.2176 0.2123 -0.0111 -0.0003 -0.0270 243 PHE A CG  
1946 C CD1 . PHE A 244 ? 0.1818 0.1984 0.1980 -0.0100 0.0014  -0.0293 243 PHE A CD1 
1947 C CD2 . PHE A 244 ? 0.2260 0.2395 0.2366 -0.0109 -0.0011 -0.0239 243 PHE A CD2 
1948 C CE1 . PHE A 244 ? 0.2356 0.2492 0.2555 -0.0089 0.0019  -0.0276 243 PHE A CE1 
1949 C CE2 . PHE A 244 ? 0.2447 0.2559 0.2583 -0.0099 -0.0002 -0.0228 243 PHE A CE2 
1950 C CZ  . PHE A 244 ? 0.2349 0.2461 0.2528 -0.0089 0.0012  -0.0242 243 PHE A CZ  
1951 N N   . VAL A 245 ? 0.1878 0.2060 0.1982 -0.0121 -0.0044 -0.0323 244 VAL A N   
1952 C CA  . VAL A 245 ? 0.1610 0.1772 0.1766 -0.0115 -0.0050 -0.0337 244 VAL A CA  
1953 C C   . VAL A 245 ? 0.1721 0.1906 0.1902 -0.0117 -0.0051 -0.0386 244 VAL A C   
1954 O O   . VAL A 245 ? 0.1843 0.2011 0.2088 -0.0111 -0.0041 -0.0407 244 VAL A O   
1955 C CB  . VAL A 245 ? 0.1505 0.1657 0.1650 -0.0117 -0.0078 -0.0316 244 VAL A CB  
1956 C CG1 . VAL A 245 ? 0.1611 0.1760 0.1813 -0.0113 -0.0088 -0.0340 244 VAL A CG1 
1957 C CG2 . VAL A 245 ? 0.1720 0.1844 0.1864 -0.0112 -0.0073 -0.0280 244 VAL A CG2 
1958 N N   . GLN A 246 ? 0.1938 0.2162 0.2068 -0.0128 -0.0062 -0.0405 245 GLN A N   
1959 C CA  . GLN A 246 ? 0.2297 0.2547 0.2446 -0.0131 -0.0063 -0.0461 245 GLN A CA  
1960 C C   . GLN A 246 ? 0.2323 0.2567 0.2527 -0.0122 -0.0031 -0.0491 245 GLN A C   
1961 O O   . GLN A 246 ? 0.1722 0.1959 0.1991 -0.0118 -0.0027 -0.0531 245 GLN A O   
1962 C CB  . GLN A 246 ? 0.2576 0.2876 0.2646 -0.0147 -0.0077 -0.0475 245 GLN A CB  
1963 C CG  . GLN A 246 ? 0.2722 0.3056 0.2804 -0.0152 -0.0080 -0.0542 245 GLN A CG  
1964 C CD  . GLN A 246 ? 0.3478 0.3799 0.3610 -0.0150 -0.0109 -0.0560 245 GLN A CD  
1965 O OE1 . GLN A 246 ? 0.3714 0.4049 0.3808 -0.0158 -0.0145 -0.0545 245 GLN A OE1 
1966 N NE2 . GLN A 246 ? 0.2982 0.3276 0.3206 -0.0141 -0.0094 -0.0589 245 GLN A NE2 
1967 N N   . THR A 247 ? 0.2262 0.2508 0.2453 -0.0118 -0.0009 -0.0472 246 THR A N   
1968 C CA  . THR A 247 ? 0.2358 0.2599 0.2612 -0.0106 0.0016  -0.0499 246 THR A CA  
1969 C C   . THR A 247 ? 0.2000 0.2190 0.2331 -0.0094 0.0020  -0.0482 246 THR A C   
1970 O O   . THR A 247 ? 0.2075 0.2251 0.2480 -0.0087 0.0030  -0.0514 246 THR A O   
1971 C CB  . THR A 247 ? 0.2739 0.3001 0.2968 -0.0105 0.0035  -0.0482 246 THR A CB  
1972 O OG1 . THR A 247 ? 0.2959 0.3275 0.3118 -0.0121 0.0036  -0.0501 246 THR A OG1 
1973 C CG2 . THR A 247 ? 0.2410 0.2668 0.2718 -0.0089 0.0058  -0.0509 246 THR A CG2 
1974 N N   . MET A 248 ? 0.1785 0.1946 0.2099 -0.0093 0.0014  -0.0431 247 MET A N   
1975 C CA  . MET A 248 ? 0.1843 0.1961 0.2216 -0.0087 0.0019  -0.0411 247 MET A CA  
1976 C C   . MET A 248 ? 0.2239 0.2351 0.2667 -0.0091 0.0013  -0.0444 247 MET A C   
1977 O O   . MET A 248 ? 0.2487 0.2573 0.2989 -0.0087 0.0024  -0.0456 247 MET A O   
1978 C CB  . MET A 248 ? 0.2290 0.2389 0.2628 -0.0088 0.0014  -0.0361 247 MET A CB  
1979 C CG  . MET A 248 ? 0.2560 0.2652 0.2869 -0.0083 0.0021  -0.0325 247 MET A CG  
1980 S SD  . MET A 248 ? 0.2761 0.2831 0.3034 -0.0086 0.0016  -0.0280 247 MET A SD  
1981 C CE  . MET A 248 ? 0.3774 0.3811 0.4102 -0.0083 0.0032  -0.0266 247 MET A CE  
1982 N N   . LEU A 249 ? 0.1902 0.2034 0.2300 -0.0100 -0.0008 -0.0459 248 LEU A N   
1983 C CA  . LEU A 249 ? 0.2228 0.2361 0.2681 -0.0106 -0.0018 -0.0495 248 LEU A CA  
1984 C C   . LEU A 249 ? 0.2488 0.2630 0.2990 -0.0105 -0.0012 -0.0551 248 LEU A C   
1985 O O   . LEU A 249 ? 0.2597 0.2719 0.3183 -0.0107 -0.0008 -0.0574 248 LEU A O   
1986 C CB  . LEU A 249 ? 0.2050 0.2213 0.2457 -0.0115 -0.0049 -0.0502 248 LEU A CB  
1987 C CG  . LEU A 249 ? 0.2396 0.2546 0.2792 -0.0114 -0.0060 -0.0460 248 LEU A CG  
1988 C CD1 . LEU A 249 ? 0.1963 0.2142 0.2307 -0.0120 -0.0096 -0.0460 248 LEU A CD1 
1989 C CD2 . LEU A 249 ? 0.2248 0.2376 0.2729 -0.0115 -0.0052 -0.0462 248 LEU A CD2 
1990 N N   . ASP A 250 ? 0.2283 0.2458 0.2741 -0.0104 -0.0008 -0.0578 249 ASP A N   
1991 C CA  . ASP A 250 ? 0.2466 0.2657 0.2973 -0.0102 0.0003  -0.0641 249 ASP A CA  
1992 C C   . ASP A 250 ? 0.2634 0.2781 0.3233 -0.0089 0.0024  -0.0635 249 ASP A C   
1993 O O   . ASP A 250 ? 0.2678 0.2823 0.3352 -0.0086 0.0030  -0.0689 249 ASP A O   
1994 C CB  . ASP A 250 ? 0.2872 0.3112 0.3311 -0.0104 0.0011  -0.0666 249 ASP A CB  
1995 C CG  . ASP A 250 ? 0.3236 0.3523 0.3583 -0.0120 -0.0012 -0.0679 249 ASP A CG  
1996 O OD1 . ASP A 250 ? 0.3398 0.3680 0.3744 -0.0127 -0.0039 -0.0674 249 ASP A OD1 
1997 O OD2 . ASP A 250 ? 0.3495 0.3827 0.3775 -0.0126 -0.0004 -0.0692 249 ASP A OD2 
1998 N N   . ASN A 251 ? 0.2495 0.2610 0.3092 -0.0082 0.0033  -0.0573 250 ASN A N   
1999 C CA  . ASN A 251 ? 0.2202 0.2276 0.2883 -0.0070 0.0047  -0.0557 250 ASN A CA  
2000 C C   . ASN A 251 ? 0.2516 0.2543 0.3259 -0.0075 0.0048  -0.0525 250 ASN A C   
2001 O O   . ASN A 251 ? 0.2295 0.2282 0.3102 -0.0068 0.0057  -0.0497 250 ASN A O   
2002 C CB  . ASN A 251 ? 0.1995 0.2068 0.2641 -0.0059 0.0056  -0.0511 250 ASN A CB  
2003 C CG  . ASN A 251 ? 0.2586 0.2699 0.3224 -0.0052 0.0065  -0.0551 250 ASN A CG  
2004 O OD1 . ASN A 251 ? 0.2539 0.2644 0.3258 -0.0039 0.0075  -0.0579 250 ASN A OD1 
2005 N ND2 . ASN A 251 ? 0.2367 0.2526 0.2915 -0.0060 0.0063  -0.0554 250 ASN A ND2 
2006 N N   . PHE A 252 ? 0.1973 0.2005 0.2704 -0.0088 0.0037  -0.0527 251 PHE A N   
2007 C CA  . PHE A 252 ? 0.2164 0.2160 0.2971 -0.0097 0.0042  -0.0510 251 PHE A CA  
2008 C C   . PHE A 252 ? 0.2513 0.2496 0.3421 -0.0099 0.0041  -0.0567 251 PHE A C   
2009 O O   . PHE A 252 ? 0.2402 0.2418 0.3306 -0.0099 0.0030  -0.0632 251 PHE A O   
2010 C CB  . PHE A 252 ? 0.1831 0.1843 0.2611 -0.0109 0.0032  -0.0503 251 PHE A CB  
2011 C CG  . PHE A 252 ? 0.2001 0.2010 0.2717 -0.0109 0.0038  -0.0444 251 PHE A CG  
2012 C CD1 . PHE A 252 ? 0.1823 0.1855 0.2447 -0.0102 0.0029  -0.0431 251 PHE A CD1 
2013 C CD2 . PHE A 252 ? 0.1937 0.1921 0.2686 -0.0117 0.0054  -0.0404 251 PHE A CD2 
2014 C CE1 . PHE A 252 ? 0.2127 0.2154 0.2699 -0.0102 0.0033  -0.0385 251 PHE A CE1 
2015 C CE2 . PHE A 252 ? 0.2401 0.2386 0.3090 -0.0116 0.0062  -0.0359 251 PHE A CE2 
2016 C CZ  . PHE A 252 ? 0.2575 0.2580 0.3179 -0.0108 0.0050  -0.0353 251 PHE A CZ  
2017 N N   . HIS A 253 ? 0.2117 0.2053 0.3118 -0.0101 0.0053  -0.0543 252 HIS A N   
2018 C CA  . HIS A 253 ? 0.2325 0.2238 0.3441 -0.0105 0.0052  -0.0593 252 HIS A CA  
2019 C C   . HIS A 253 ? 0.2293 0.2174 0.3485 -0.0124 0.0057  -0.0566 252 HIS A C   
2020 O O   . HIS A 253 ? 0.2203 0.2056 0.3387 -0.0129 0.0072  -0.0495 252 HIS A O   
2021 C CB  . HIS A 253 ? 0.2628 0.2508 0.3811 -0.0088 0.0060  -0.0592 252 HIS A CB  
2022 C CG  . HIS A 253 ? 0.3557 0.3474 0.4680 -0.0071 0.0059  -0.0619 252 HIS A CG  
2023 N ND1 . HIS A 253 ? 0.3789 0.3753 0.4893 -0.0069 0.0054  -0.0699 252 HIS A ND1 
2024 C CD2 . HIS A 253 ? 0.3615 0.3533 0.4695 -0.0056 0.0065  -0.0576 252 HIS A CD2 
2025 C CE1 . HIS A 253 ? 0.3855 0.3848 0.4906 -0.0055 0.0061  -0.0703 252 HIS A CE1 
2026 N NE2 . HIS A 253 ? 0.3536 0.3501 0.4578 -0.0046 0.0066  -0.0630 252 HIS A NE2 
2027 N N   . ASP A 254 ? 0.2153 0.2041 0.3416 -0.0137 0.0047  -0.0625 253 ASP A N   
2028 C CA  . ASP A 254 ? 0.2453 0.2311 0.3811 -0.0157 0.0055  -0.0606 253 ASP A CA  
2029 C C   . ASP A 254 ? 0.2336 0.2131 0.3790 -0.0157 0.0070  -0.0566 253 ASP A C   
2030 O O   . ASP A 254 ? 0.2319 0.2092 0.3829 -0.0144 0.0066  -0.0601 253 ASP A O   
2031 C CB  . ASP A 254 ? 0.2602 0.2484 0.4029 -0.0171 0.0036  -0.0685 253 ASP A CB  
2032 C CG  . ASP A 254 ? 0.3349 0.3292 0.4688 -0.0174 0.0014  -0.0711 253 ASP A CG  
2033 O OD1 . ASP A 254 ? 0.3050 0.3009 0.4297 -0.0169 0.0020  -0.0659 253 ASP A OD1 
2034 O OD2 . ASP A 254 ? 0.3774 0.3750 0.5138 -0.0180 -0.0010 -0.0783 253 ASP A OD2 
2035 N N   . THR A 255 ? 0.2241 0.2006 0.3714 -0.0173 0.0089  -0.0492 254 THR A N   
2036 C CA  . THR A 255 ? 0.2078 0.1782 0.3615 -0.0174 0.0103  -0.0429 254 THR A CA  
2037 C C   . THR A 255 ? 0.2169 0.1845 0.3803 -0.0205 0.0119  -0.0400 254 THR A C   
2038 O O   . THR A 255 ? 0.2369 0.2069 0.3962 -0.0222 0.0134  -0.0368 254 THR A O   
2039 C CB  . THR A 255 ? 0.2164 0.1867 0.3594 -0.0164 0.0113  -0.0349 254 THR A CB  
2040 O OG1 . THR A 255 ? 0.2226 0.1963 0.3568 -0.0139 0.0099  -0.0379 254 THR A OG1 
2041 C CG2 . THR A 255 ? 0.2133 0.1774 0.3622 -0.0164 0.0119  -0.0279 254 THR A CG2 
2042 N N   . TRP A 256 ? 0.1822 0.1447 0.3591 -0.0212 0.0115  -0.0415 255 TRP A N   
2043 C CA  . TRP A 256 ? 0.2126 0.1723 0.4007 -0.0244 0.0130  -0.0392 255 TRP A CA  
2044 C C   . TRP A 256 ? 0.2248 0.1817 0.4100 -0.0261 0.0158  -0.0281 255 TRP A C   
2045 O O   . TRP A 256 ? 0.2925 0.2462 0.4736 -0.0247 0.0158  -0.0220 255 TRP A O   
2046 C CB  . TRP A 256 ? 0.2068 0.1610 0.4107 -0.0247 0.0118  -0.0434 255 TRP A CB  
2047 C CG  . TRP A 256 ? 0.2221 0.1729 0.4396 -0.0283 0.0131  -0.0418 255 TRP A CG  
2048 C CD1 . TRP A 256 ? 0.2638 0.2075 0.4914 -0.0301 0.0143  -0.0346 255 TRP A CD1 
2049 C CD2 . TRP A 256 ? 0.2146 0.1689 0.4379 -0.0308 0.0130  -0.0473 255 TRP A CD2 
2050 N NE1 . TRP A 256 ? 0.2557 0.1999 0.4926 -0.0329 0.0154  -0.0348 255 TRP A NE1 
2051 C CE2 . TRP A 256 ? 0.2561 0.2069 0.4909 -0.0333 0.0146  -0.0428 255 TRP A CE2 
2052 C CE3 . TRP A 256 ? 0.2496 0.2111 0.4681 -0.0306 0.0114  -0.0550 255 TRP A CE3 
2053 C CZ2 . TRP A 256 ? 0.2737 0.2282 0.5150 -0.0353 0.0148  -0.0459 255 TRP A CZ2 
2054 C CZ3 . TRP A 256 ? 0.2499 0.2142 0.4761 -0.0329 0.0113  -0.0582 255 TRP A CZ3 
2055 C CH2 . TRP A 256 ? 0.2935 0.2548 0.5307 -0.0350 0.0131  -0.0537 255 TRP A CH2 
2056 N N   . ASP A 257 ? 0.1933 0.1518 0.3805 -0.0293 0.0181  -0.0256 256 ASP A N   
2057 C CA  . ASP A 257 ? 0.2372 0.1933 0.4237 -0.0319 0.0214  -0.0155 256 ASP A CA  
2058 C C   . ASP A 257 ? 0.2161 0.1690 0.4182 -0.0355 0.0229  -0.0149 256 ASP A C   
2059 O O   . ASP A 257 ? 0.2267 0.1832 0.4343 -0.0373 0.0233  -0.0202 256 ASP A O   
2060 C CB  . ASP A 257 ? 0.2768 0.2389 0.4511 -0.0326 0.0238  -0.0128 256 ASP A CB  
2061 C CG  . ASP A 257 ? 0.3589 0.3195 0.5309 -0.0354 0.0276  -0.0026 256 ASP A CG  
2062 O OD1 . ASP A 257 ? 0.3959 0.3568 0.5756 -0.0390 0.0305  -0.0008 256 ASP A OD1 
2063 O OD2 . ASP A 257 ? 0.4472 0.4063 0.6096 -0.0342 0.0277  0.0036  256 ASP A OD2 
2064 N N   . SER A 258 ? 0.2344 0.1801 0.4439 -0.0366 0.0233  -0.0081 257 SER A N   
2065 C CA  . SER A 258 ? 0.2715 0.2127 0.4972 -0.0402 0.0245  -0.0067 257 SER A CA  
2066 C C   . SER A 258 ? 0.2912 0.2355 0.5161 -0.0445 0.0290  -0.0007 257 SER A C   
2067 O O   . SER A 258 ? 0.2951 0.2404 0.5305 -0.0471 0.0300  -0.0031 257 SER A O   
2068 C CB  . SER A 258 ? 0.3016 0.2344 0.5348 -0.0399 0.0233  -0.0002 257 SER A CB  
2069 O OG  . SER A 258 ? 0.3262 0.2574 0.5492 -0.0403 0.0249  0.0109  257 SER A OG  
2070 N N   . LYS A 259 ? 0.3672 0.3142 0.5781 -0.0447 0.0315  0.0065  258 LYS A N   
2071 C CA  . LYS A 259 ? 0.4123 0.3632 0.6216 -0.0487 0.0364  0.0117  258 LYS A CA  
2072 C C   . LYS A 259 ? 0.3757 0.3340 0.5872 -0.0493 0.0371  0.0032  258 LYS A C   
2073 O O   . LYS A 259 ? 0.3753 0.3350 0.5978 -0.0530 0.0396  0.0026  258 LYS A O   
2074 C CB  . LYS A 259 ? 0.5080 0.4613 0.7005 -0.0484 0.0386  0.0195  258 LYS A CB  
2075 C CG  . LYS A 259 ? 0.6133 0.5722 0.8021 -0.0523 0.0442  0.0236  258 LYS A CG  
2076 C CD  . LYS A 259 ? 0.6932 0.6564 0.8638 -0.0510 0.0458  0.0274  258 LYS A CD  
2077 C CE  . LYS A 259 ? 0.7512 0.7217 0.9186 -0.0542 0.0514  0.0282  258 LYS A CE  
2078 N NZ  . LYS A 259 ? 0.7733 0.7490 0.9237 -0.0526 0.0527  0.0291  258 LYS A NZ  
2079 N N   . ASP A 260 ? 0.3287 0.2919 0.5305 -0.0457 0.0347  -0.0033 259 ASP A N   
2080 C CA  . ASP A 260 ? 0.3093 0.2795 0.5127 -0.0458 0.0345  -0.0111 259 ASP A CA  
2081 C C   . ASP A 260 ? 0.3089 0.2784 0.5246 -0.0453 0.0307  -0.0202 259 ASP A C   
2082 O O   . ASP A 260 ? 0.3115 0.2866 0.5308 -0.0458 0.0300  -0.0266 259 ASP A O   
2083 C CB  . ASP A 260 ? 0.3142 0.2896 0.5024 -0.0423 0.0332  -0.0137 259 ASP A CB  
2084 C CG  . ASP A 260 ? 0.4025 0.3797 0.5785 -0.0429 0.0370  -0.0061 259 ASP A CG  
2085 O OD1 . ASP A 260 ? 0.4367 0.4117 0.6152 -0.0461 0.0407  0.0014  259 ASP A OD1 
2086 O OD2 . ASP A 260 ? 0.4256 0.4064 0.5895 -0.0402 0.0361  -0.0076 259 ASP A OD2 
2087 N N   . GLN A 261 ? 0.2973 0.2604 0.5197 -0.0444 0.0282  -0.0214 260 GLN A N   
2088 C CA  . GLN A 261 ? 0.2849 0.2474 0.5185 -0.0439 0.0245  -0.0308 260 GLN A CA  
2089 C C   . GLN A 261 ? 0.2577 0.2263 0.4837 -0.0410 0.0211  -0.0397 260 GLN A C   
2090 O O   . GLN A 261 ? 0.2600 0.2326 0.4921 -0.0414 0.0190  -0.0470 260 GLN A O   
2091 C CB  . GLN A 261 ? 0.3221 0.2862 0.5667 -0.0462 0.0257  -0.0314 260 GLN A CB  
2092 C CG  . GLN A 261 ? 0.3473 0.3050 0.5996 -0.0478 0.0273  -0.0244 260 GLN A CG  
2093 C CD  . GLN A 261 ? 0.3875 0.3398 0.6445 -0.0448 0.0236  -0.0275 260 GLN A CD  
2094 O OE1 . GLN A 261 ? 0.3881 0.3348 0.6426 -0.0439 0.0236  -0.0217 260 GLN A OE1 
2095 N NE2 . GLN A 261 ? 0.3763 0.3309 0.6402 -0.0433 0.0205  -0.0369 260 GLN A NE2 
2096 N N   . ARG A 262 ? 0.2221 0.1919 0.4334 -0.0377 0.0201  -0.0385 261 ARG A N   
2097 C CA  . ARG A 262 ? 0.2455 0.2208 0.4487 -0.0350 0.0167  -0.0460 261 ARG A CA  
2098 C C   . ARG A 262 ? 0.2546 0.2288 0.4449 -0.0315 0.0157  -0.0443 261 ARG A C   
2099 O O   . ARG A 262 ? 0.2836 0.2536 0.4707 -0.0312 0.0175  -0.0371 261 ARG A O   
2100 C CB  . ARG A 262 ? 0.2418 0.2241 0.4401 -0.0356 0.0175  -0.0466 261 ARG A CB  
2101 C CG  . ARG A 262 ? 0.1803 0.1637 0.3683 -0.0356 0.0211  -0.0385 261 ARG A CG  
2102 C CD  . ARG A 262 ? 0.1579 0.1483 0.3388 -0.0346 0.0206  -0.0408 261 ARG A CD  
2103 N NE  . ARG A 262 ? 0.2470 0.2391 0.4164 -0.0312 0.0171  -0.0442 261 ARG A NE  
2104 C CZ  . ARG A 262 ? 0.2758 0.2730 0.4377 -0.0298 0.0158  -0.0459 261 ARG A CZ  
2105 N NH1 . ARG A 262 ? 0.2375 0.2387 0.4026 -0.0311 0.0177  -0.0452 261 ARG A NH1 
2106 N NH2 . ARG A 262 ? 0.2421 0.2403 0.3939 -0.0270 0.0127  -0.0482 261 ARG A NH2 
2107 N N   . SER A 263 ? 0.2147 0.1930 0.3976 -0.0291 0.0126  -0.0506 262 SER A N   
2108 C CA  . SER A 263 ? 0.2591 0.2374 0.4298 -0.0260 0.0118  -0.0494 262 SER A CA  
2109 C C   . SER A 263 ? 0.2449 0.2278 0.4027 -0.0252 0.0124  -0.0463 262 SER A C   
2110 O O   . SER A 263 ? 0.1964 0.1837 0.3543 -0.0262 0.0122  -0.0481 262 SER A O   
2111 C CB  . SER A 263 ? 0.3159 0.2959 0.4858 -0.0240 0.0084  -0.0580 262 SER A CB  
2112 O OG  . SER A 263 ? 0.3953 0.3706 0.5767 -0.0242 0.0079  -0.0611 262 SER A OG  
2113 N N   . TYR A 264 ? 0.2163 0.1980 0.3641 -0.0234 0.0131  -0.0416 263 TYR A N   
2114 C CA  . TYR A 264 ? 0.1995 0.1851 0.3346 -0.0221 0.0131  -0.0397 263 TYR A CA  
2115 C C   . TYR A 264 ? 0.2183 0.2046 0.3449 -0.0194 0.0110  -0.0417 263 TYR A C   
2116 O O   . TYR A 264 ? 0.2282 0.2111 0.3569 -0.0183 0.0108  -0.0412 263 TYR A O   
2117 C CB  . TYR A 264 ? 0.2064 0.1908 0.3365 -0.0229 0.0164  -0.0315 263 TYR A CB  
2118 C CG  . TYR A 264 ? 0.2646 0.2492 0.4021 -0.0260 0.0195  -0.0287 263 TYR A CG  
2119 C CD1 . TYR A 264 ? 0.2396 0.2291 0.3769 -0.0268 0.0203  -0.0306 263 TYR A CD1 
2120 C CD2 . TYR A 264 ? 0.2784 0.2583 0.4237 -0.0280 0.0217  -0.0240 263 TYR A CD2 
2121 C CE1 . TYR A 264 ? 0.2560 0.2464 0.4007 -0.0298 0.0236  -0.0283 263 TYR A CE1 
2122 C CE2 . TYR A 264 ? 0.2603 0.2408 0.4123 -0.0312 0.0250  -0.0211 263 TYR A CE2 
2123 C CZ  . TYR A 264 ? 0.2579 0.2440 0.4096 -0.0321 0.0261  -0.0235 263 TYR A CZ  
2124 O OH  . TYR A 264 ? 0.2811 0.2685 0.4403 -0.0354 0.0299  -0.0210 263 TYR A OH  
2125 N N   . PRO A 265 ? 0.2179 0.2085 0.3354 -0.0182 0.0093  -0.0439 264 PRO A N   
2126 C CA  . PRO A 265 ? 0.2473 0.2389 0.3563 -0.0160 0.0078  -0.0451 264 PRO A CA  
2127 C C   . PRO A 265 ? 0.3176 0.3072 0.4199 -0.0151 0.0095  -0.0385 264 PRO A C   
2128 O O   . PRO A 265 ? 0.4325 0.4226 0.5306 -0.0158 0.0110  -0.0341 264 PRO A O   
2129 C CB  . PRO A 265 ? 0.2447 0.2414 0.3468 -0.0157 0.0055  -0.0483 264 PRO A CB  
2130 C CG  . PRO A 265 ? 0.2080 0.2059 0.3121 -0.0170 0.0066  -0.0460 264 PRO A CG  
2131 C CD  . PRO A 265 ? 0.1808 0.1756 0.2957 -0.0189 0.0090  -0.0443 264 PRO A CD  
2132 N N   . ARG A 266 ? 0.2419 0.2295 0.3436 -0.0137 0.0091  -0.0381 265 ARG A N   
2133 C CA  . ARG A 266 ? 0.2085 0.1943 0.3047 -0.0128 0.0100  -0.0320 265 ARG A CA  
2134 C C   . ARG A 266 ? 0.2595 0.2475 0.3493 -0.0108 0.0086  -0.0339 265 ARG A C   
2135 O O   . ARG A 266 ? 0.2160 0.2044 0.3096 -0.0098 0.0077  -0.0389 265 ARG A O   
2136 C CB  . ARG A 266 ? 0.2431 0.2237 0.3471 -0.0130 0.0110  -0.0279 265 ARG A CB  
2137 C CG  . ARG A 266 ? 0.2694 0.2478 0.3787 -0.0155 0.0131  -0.0238 265 ARG A CG  
2138 C CD  . ARG A 266 ? 0.2547 0.2283 0.3664 -0.0157 0.0140  -0.0166 265 ARG A CD  
2139 N NE  . ARG A 266 ? 0.2480 0.2228 0.3489 -0.0148 0.0140  -0.0116 265 ARG A NE  
2140 C CZ  . ARG A 266 ? 0.2193 0.1953 0.3132 -0.0163 0.0159  -0.0069 265 ARG A CZ  
2141 N NH1 . ARG A 266 ? 0.1917 0.1683 0.2889 -0.0187 0.0182  -0.0064 265 ARG A NH1 
2142 N NH2 . ARG A 266 ? 0.2169 0.1941 0.3012 -0.0154 0.0155  -0.0031 265 ARG A NH2 
2143 N N   . LEU A 267 ? 0.2234 0.2128 0.3039 -0.0102 0.0087  -0.0303 266 LEU A N   
2144 C CA  . LEU A 267 ? 0.2332 0.2243 0.3080 -0.0086 0.0078  -0.0306 266 LEU A CA  
2145 C C   . LEU A 267 ? 0.2224 0.2106 0.2981 -0.0078 0.0081  -0.0252 266 LEU A C   
2146 O O   . LEU A 267 ? 0.2312 0.2181 0.3031 -0.0085 0.0089  -0.0198 266 LEU A O   
2147 C CB  . LEU A 267 ? 0.2292 0.2237 0.2942 -0.0087 0.0072  -0.0300 266 LEU A CB  
2148 C CG  . LEU A 267 ? 0.2082 0.2050 0.2672 -0.0075 0.0063  -0.0304 266 LEU A CG  
2149 C CD1 . LEU A 267 ? 0.1649 0.1641 0.2265 -0.0070 0.0057  -0.0362 266 LEU A CD1 
2150 C CD2 . LEU A 267 ? 0.1769 0.1761 0.2276 -0.0080 0.0056  -0.0292 266 LEU A CD2 
2151 N N   . THR A 268 ? 0.1694 0.1567 0.2503 -0.0063 0.0075  -0.0269 267 THR A N   
2152 C CA  . THR A 268 ? 0.2066 0.1916 0.2891 -0.0051 0.0070  -0.0221 267 THR A CA  
2153 C C   . THR A 268 ? 0.2172 0.2058 0.2933 -0.0038 0.0061  -0.0226 267 THR A C   
2154 O O   . THR A 268 ? 0.2526 0.2444 0.3290 -0.0031 0.0061  -0.0280 267 THR A O   
2155 C CB  . THR A 268 ? 0.2357 0.2173 0.3301 -0.0041 0.0066  -0.0237 267 THR A CB  
2156 O OG1 . THR A 268 ? 0.2369 0.2149 0.3381 -0.0056 0.0075  -0.0230 267 THR A OG1 
2157 C CG2 . THR A 268 ? 0.2661 0.2453 0.3628 -0.0026 0.0055  -0.0182 267 THR A CG2 
2158 N N   . VAL A 269 ? 0.2210 0.2094 0.2913 -0.0037 0.0056  -0.0171 268 VAL A N   
2159 C CA  . VAL A 269 ? 0.2061 0.1978 0.2710 -0.0028 0.0046  -0.0172 268 VAL A CA  
2160 C C   . VAL A 269 ? 0.2297 0.2196 0.2967 -0.0016 0.0032  -0.0119 268 VAL A C   
2161 O O   . VAL A 269 ? 0.2045 0.1932 0.2662 -0.0024 0.0027  -0.0066 268 VAL A O   
2162 C CB  . VAL A 269 ? 0.2535 0.2478 0.3083 -0.0039 0.0048  -0.0165 268 VAL A CB  
2163 C CG1 . VAL A 269 ? 0.2703 0.2676 0.3206 -0.0032 0.0037  -0.0160 268 VAL A CG1 
2164 C CG2 . VAL A 269 ? 0.2427 0.2389 0.2960 -0.0048 0.0054  -0.0213 268 VAL A CG2 
2165 N N   . GLU A 270 ? 0.2425 0.2325 0.3173 0.0002  0.0024  -0.0137 269 GLU A N   
2166 C CA  . GLU A 270 ? 0.2767 0.2654 0.3551 0.0016  0.0003  -0.0089 269 GLU A CA  
2167 C C   . GLU A 270 ? 0.2476 0.2399 0.3181 0.0017  -0.0009 -0.0070 269 GLU A C   
2168 O O   . GLU A 270 ? 0.2490 0.2455 0.3163 0.0017  -0.0002 -0.0111 269 GLU A O   
2169 C CB  . GLU A 270 ? 0.3353 0.3238 0.4256 0.0039  -0.0002 -0.0124 269 GLU A CB  
2170 C CG  . GLU A 270 ? 0.4551 0.4398 0.5550 0.0040  0.0007  -0.0151 269 GLU A CG  
2171 C CD  . GLU A 270 ? 0.5361 0.5186 0.6495 0.0064  -0.0006 -0.0158 269 GLU A CD  
2172 O OE1 . GLU A 270 ? 0.5772 0.5544 0.6989 0.0065  -0.0011 -0.0137 269 GLU A OE1 
2173 O OE2 . GLU A 270 ? 0.5466 0.5328 0.6629 0.0083  -0.0011 -0.0185 269 GLU A OE2 
2174 N N   . LEU A 271 ? 0.2151 0.2059 0.2826 0.0016  -0.0028 -0.0007 270 LEU A N   
2175 C CA  . LEU A 271 ? 0.2147 0.2088 0.2775 0.0021  -0.0048 0.0010  270 LEU A CA  
2176 C C   . LEU A 271 ? 0.2071 0.2038 0.2789 0.0043  -0.0058 -0.0021 270 LEU A C   
2177 O O   . LEU A 271 ? 0.1995 0.1939 0.2816 0.0060  -0.0065 -0.0019 270 LEU A O   
2178 C CB  . LEU A 271 ? 0.2073 0.1995 0.2661 0.0017  -0.0072 0.0083  270 LEU A CB  
2179 C CG  . LEU A 271 ? 0.2340 0.2296 0.2842 0.0011  -0.0090 0.0098  270 LEU A CG  
2180 C CD1 . LEU A 271 ? 0.2011 0.1979 0.2413 -0.0010 -0.0069 0.0078  270 LEU A CD1 
2181 C CD2 . LEU A 271 ? 0.2987 0.2929 0.3465 0.0011  -0.0122 0.0169  270 LEU A CD2 
2182 N N   . PRO A 272 ? 0.2201 0.2216 0.2892 0.0043  -0.0056 -0.0050 271 PRO A N   
2183 C CA  . PRO A 272 ? 0.2307 0.2357 0.3089 0.0063  -0.0059 -0.0084 271 PRO A CA  
2184 C C   . PRO A 272 ? 0.2342 0.2396 0.3177 0.0080  -0.0095 -0.0041 271 PRO A C   
2185 O O   . PRO A 272 ? 0.2185 0.2274 0.3106 0.0097  -0.0099 -0.0069 271 PRO A O   
2186 C CB  . PRO A 272 ? 0.1972 0.2074 0.2694 0.0050  -0.0042 -0.0123 271 PRO A CB  
2187 C CG  . PRO A 272 ? 0.2058 0.2151 0.2668 0.0030  -0.0051 -0.0086 271 PRO A CG  
2188 C CD  . PRO A 272 ? 0.1938 0.1979 0.2524 0.0024  -0.0050 -0.0056 271 PRO A CD  
2189 N N   . VAL A 273 ? 0.2010 0.2035 0.2796 0.0075  -0.0121 0.0024  272 VAL A N   
2190 C CA  . VAL A 273 ? 0.1715 0.1739 0.2544 0.0090  -0.0164 0.0075  272 VAL A CA  
2191 C C   . VAL A 273 ? 0.2054 0.2019 0.2886 0.0089  -0.0180 0.0139  272 VAL A C   
2192 O O   . VAL A 273 ? 0.2045 0.1975 0.2846 0.0075  -0.0155 0.0139  272 VAL A O   
2193 C CB  . VAL A 273 ? 0.2458 0.2518 0.3201 0.0079  -0.0187 0.0097  272 VAL A CB  
2194 C CG1 . VAL A 273 ? 0.2874 0.2992 0.3624 0.0076  -0.0169 0.0040  272 VAL A CG1 
2195 C CG2 . VAL A 273 ? 0.2349 0.2390 0.2958 0.0053  -0.0180 0.0125  272 VAL A CG2 
2196 N N   . GLN A 274 ? 0.2002 0.1957 0.2875 0.0103  -0.0223 0.0196  273 GLN A N   
2197 C CA  . GLN A 274 ? 0.2102 0.2002 0.2969 0.0099  -0.0242 0.0270  273 GLN A CA  
2198 C C   . GLN A 274 ? 0.2351 0.2242 0.3071 0.0067  -0.0226 0.0298  273 GLN A C   
2199 O O   . GLN A 274 ? 0.2541 0.2470 0.3161 0.0054  -0.0226 0.0288  273 GLN A O   
2200 C CB  . GLN A 274 ? 0.2347 0.2248 0.3258 0.0116  -0.0300 0.0334  273 GLN A CB  
2201 C CG  . GLN A 274 ? 0.2720 0.2622 0.3801 0.0151  -0.0320 0.0315  273 GLN A CG  
2202 C CD  . GLN A 274 ? 0.3383 0.3219 0.4571 0.0162  -0.0322 0.0341  273 GLN A CD  
2203 O OE1 . GLN A 274 ? 0.3539 0.3329 0.4672 0.0140  -0.0304 0.0373  273 GLN A OE1 
2204 N NE2 . GLN A 274 ? 0.3911 0.3742 0.5262 0.0195  -0.0342 0.0324  273 GLN A NE2 
2205 N N   . PRO A 275 ? 0.2791 0.2634 0.3500 0.0053  -0.0209 0.0332  274 PRO A N   
2206 C CA  . PRO A 275 ? 0.2719 0.2510 0.3550 0.0065  -0.0212 0.0350  274 PRO A CA  
2207 C C   . PRO A 275 ? 0.2998 0.2778 0.3902 0.0068  -0.0171 0.0276  274 PRO A C   
2208 O O   . PRO A 275 ? 0.3080 0.2810 0.4066 0.0068  -0.0166 0.0291  274 PRO A O   
2209 C CB  . PRO A 275 ? 0.2774 0.2524 0.3539 0.0041  -0.0213 0.0430  274 PRO A CB  
2210 C CG  . PRO A 275 ? 0.2573 0.2353 0.3196 0.0013  -0.0181 0.0411  274 PRO A CG  
2211 C CD  . PRO A 275 ? 0.2535 0.2372 0.3112 0.0022  -0.0193 0.0368  274 PRO A CD  
2212 N N   . TYR A 276 ? 0.2196 0.2020 0.3069 0.0067  -0.0146 0.0202  275 TYR A N   
2213 C CA  . TYR A 276 ? 0.2427 0.2250 0.3360 0.0069  -0.0112 0.0127  275 TYR A CA  
2214 C C   . TYR A 276 ? 0.2778 0.2563 0.3689 0.0047  -0.0086 0.0134  275 TYR A C   
2215 O O   . TYR A 276 ? 0.2924 0.2686 0.3921 0.0050  -0.0069 0.0094  275 TYR A O   
2216 C CB  . TYR A 276 ? 0.2464 0.2277 0.3554 0.0098  -0.0122 0.0096  275 TYR A CB  
2217 C CG  . TYR A 276 ? 0.2335 0.2191 0.3471 0.0122  -0.0146 0.0085  275 TYR A CG  
2218 C CD1 . TYR A 276 ? 0.2373 0.2291 0.3469 0.0121  -0.0129 0.0027  275 TYR A CD1 
2219 C CD2 . TYR A 276 ? 0.3024 0.2859 0.4251 0.0144  -0.0187 0.0136  275 TYR A CD2 
2220 C CE1 . TYR A 276 ? 0.2555 0.2519 0.3704 0.0140  -0.0148 0.0015  275 TYR A CE1 
2221 C CE2 . TYR A 276 ? 0.3270 0.3151 0.4554 0.0166  -0.0211 0.0122  275 TYR A CE2 
2222 C CZ  . TYR A 276 ? 0.2937 0.2884 0.4183 0.0164  -0.0189 0.0060  275 TYR A CZ  
2223 O OH  . TYR A 276 ? 0.3394 0.3392 0.4703 0.0183  -0.0208 0.0045  275 TYR A OH  
2224 N N   . ASN A 277 ? 0.2758 0.2539 0.3560 0.0023  -0.0080 0.0180  276 ASN A N   
2225 C CA  . ASN A 277 ? 0.2847 0.2598 0.3632 0.0000  -0.0054 0.0192  276 ASN A CA  
2226 C C   . ASN A 277 ? 0.2717 0.2495 0.3460 -0.0011 -0.0022 0.0122  276 ASN A C   
2227 O O   . ASN A 277 ? 0.2539 0.2360 0.3222 -0.0008 -0.0020 0.0086  276 ASN A O   
2228 C CB  . ASN A 277 ? 0.2470 0.2213 0.3154 -0.0022 -0.0056 0.0267  276 ASN A CB  
2229 C CG  . ASN A 277 ? 0.3136 0.2927 0.3695 -0.0029 -0.0057 0.0258  276 ASN A CG  
2230 O OD1 . ASN A 277 ? 0.2906 0.2727 0.3459 -0.0013 -0.0081 0.0245  276 ASN A OD1 
2231 N ND2 . ASN A 277 ? 0.3125 0.2927 0.3596 -0.0053 -0.0031 0.0258  276 ASN A ND2 
2232 N N   . ASP A 278 ? 0.2520 0.2273 0.3300 -0.0025 0.0001  0.0109  277 ASP A N   
2233 C CA  . ASP A 278 ? 0.2128 0.1905 0.2867 -0.0038 0.0026  0.0055  277 ASP A CA  
2234 C C   . ASP A 278 ? 0.2530 0.2327 0.3151 -0.0057 0.0037  0.0084  277 ASP A C   
2235 O O   . ASP A 278 ? 0.2461 0.2240 0.3060 -0.0075 0.0048  0.0133  277 ASP A O   
2236 C CB  . ASP A 278 ? 0.2317 0.2062 0.3138 -0.0049 0.0044  0.0036  277 ASP A CB  
2237 C CG  . ASP A 278 ? 0.2337 0.2109 0.3123 -0.0064 0.0065  -0.0014 277 ASP A CG  
2238 O OD1 . ASP A 278 ? 0.2138 0.1949 0.2850 -0.0061 0.0065  -0.0046 277 ASP A OD1 
2239 O OD2 . ASP A 278 ? 0.2398 0.2148 0.3234 -0.0079 0.0080  -0.0019 277 ASP A OD2 
2240 N N   . VAL A 279 ? 0.2066 0.1904 0.2614 -0.0054 0.0035  0.0053  278 VAL A N   
2241 C CA  . VAL A 279 ? 0.2609 0.2466 0.3053 -0.0068 0.0042  0.0073  278 VAL A CA  
2242 C C   . VAL A 279 ? 0.2595 0.2452 0.3027 -0.0087 0.0071  0.0058  278 VAL A C   
2243 O O   . VAL A 279 ? 0.2498 0.2367 0.2860 -0.0102 0.0084  0.0080  278 VAL A O   
2244 C CB  . VAL A 279 ? 0.2995 0.2891 0.3381 -0.0060 0.0030  0.0043  278 VAL A CB  
2245 C CG1 . VAL A 279 ? 0.3304 0.3206 0.3705 -0.0044 0.0002  0.0064  278 VAL A CG1 
2246 C CG2 . VAL A 279 ? 0.3431 0.3344 0.3843 -0.0056 0.0037  -0.0020 278 VAL A CG2 
2247 N N   . PHE A 280 ? 0.2477 0.2326 0.2980 -0.0088 0.0081  0.0019  279 PHE A N   
2248 C CA  . PHE A 280 ? 0.2231 0.2083 0.2743 -0.0105 0.0105  0.0002  279 PHE A CA  
2249 C C   . PHE A 280 ? 0.2426 0.2244 0.3003 -0.0121 0.0121  0.0038  279 PHE A C   
2250 O O   . PHE A 280 ? 0.2163 0.1984 0.2770 -0.0136 0.0142  0.0021  279 PHE A O   
2251 C CB  . PHE A 280 ? 0.2516 0.2384 0.3065 -0.0100 0.0103  -0.0065 279 PHE A CB  
2252 C CG  . PHE A 280 ? 0.2863 0.2766 0.3342 -0.0094 0.0095  -0.0096 279 PHE A CG  
2253 C CD1 . PHE A 280 ? 0.3650 0.3570 0.4069 -0.0104 0.0105  -0.0090 279 PHE A CD1 
2254 C CD2 . PHE A 280 ? 0.3288 0.3208 0.3767 -0.0081 0.0079  -0.0131 279 PHE A CD2 
2255 C CE1 . PHE A 280 ? 0.4130 0.4075 0.4497 -0.0099 0.0094  -0.0115 279 PHE A CE1 
2256 C CE2 . PHE A 280 ? 0.3751 0.3700 0.4169 -0.0079 0.0071  -0.0151 279 PHE A CE2 
2257 C CZ  . PHE A 280 ? 0.3898 0.3855 0.4263 -0.0087 0.0076  -0.0142 279 PHE A CZ  
2258 N N   . GLU A 281 ? 0.2486 0.2272 0.3089 -0.0118 0.0110  0.0090  280 GLU A N   
2259 C CA  . GLU A 281 ? 0.2884 0.2629 0.3569 -0.0132 0.0121  0.0125  280 GLU A CA  
2260 C C   . GLU A 281 ? 0.2956 0.2708 0.3605 -0.0162 0.0153  0.0160  280 GLU A C   
2261 O O   . GLU A 281 ? 0.3289 0.3018 0.4013 -0.0180 0.0172  0.0168  280 GLU A O   
2262 C CB  . GLU A 281 ? 0.3176 0.2884 0.3892 -0.0123 0.0097  0.0185  280 GLU A CB  
2263 C CG  . GLU A 281 ? 0.3702 0.3423 0.4313 -0.0126 0.0088  0.0247  280 GLU A CG  
2264 C CD  . GLU A 281 ? 0.4679 0.4374 0.5324 -0.0108 0.0051  0.0295  280 GLU A CD  
2265 O OE1 . GLU A 281 ? 0.4643 0.4295 0.5402 -0.0100 0.0041  0.0301  280 GLU A OE1 
2266 O OE2 . GLU A 281 ? 0.4945 0.4660 0.5510 -0.0102 0.0031  0.0322  280 GLU A OE2 
2267 N N   . LYS A 282 ? 0.2581 0.2365 0.3122 -0.0169 0.0163  0.0176  281 LYS A N   
2268 C CA  . LYS A 282 ? 0.3182 0.2981 0.3687 -0.0198 0.0199  0.0206  281 LYS A CA  
2269 C C   . LYS A 282 ? 0.2821 0.2647 0.3359 -0.0208 0.0225  0.0148  281 LYS A C   
2270 O O   . LYS A 282 ? 0.2731 0.2566 0.3281 -0.0234 0.0260  0.0167  281 LYS A O   
2271 C CB  . LYS A 282 ? 0.3924 0.3753 0.4302 -0.0203 0.0202  0.0235  281 LYS A CB  
2272 C CG  . LYS A 282 ? 0.4985 0.4792 0.5323 -0.0211 0.0189  0.0318  281 LYS A CG  
2273 C CD  . LYS A 282 ? 0.5985 0.5788 0.6294 -0.0185 0.0145  0.0325  281 LYS A CD  
2274 C CE  . LYS A 282 ? 0.6344 0.6129 0.6607 -0.0193 0.0125  0.0411  281 LYS A CE  
2275 N NZ  . LYS A 282 ? 0.6319 0.6118 0.6535 -0.0170 0.0082  0.0413  281 LYS A NZ  
2276 N N   . MET A 283 ? 0.2386 0.2228 0.2941 -0.0189 0.0209  0.0082  282 MET A N   
2277 C CA  . MET A 283 ? 0.2327 0.2195 0.2919 -0.0196 0.0225  0.0030  282 MET A CA  
2278 C C   . MET A 283 ? 0.2329 0.2174 0.3036 -0.0210 0.0236  0.0025  282 MET A C   
2279 O O   . MET A 283 ? 0.2729 0.2540 0.3501 -0.0202 0.0216  0.0023  282 MET A O   
2280 C CB  . MET A 283 ? 0.2737 0.2625 0.3316 -0.0173 0.0199  -0.0031 282 MET A CB  
2281 C CG  . MET A 283 ? 0.3550 0.3463 0.4029 -0.0163 0.0191  -0.0033 282 MET A CG  
2282 S SD  . MET A 283 ? 0.4165 0.4097 0.4634 -0.0141 0.0160  -0.0094 282 MET A SD  
2283 C CE  . MET A 283 ? 0.2839 0.2788 0.3386 -0.0150 0.0169  -0.0140 282 MET A CE  
2284 N N   . THR A 284 ? 0.1905 0.1772 0.2646 -0.0232 0.0267  0.0018  283 THR A N   
2285 C CA  . THR A 284 ? 0.2325 0.2173 0.3183 -0.0249 0.0277  0.0010  283 THR A CA  
2286 C C   . THR A 284 ? 0.2137 0.1992 0.3060 -0.0234 0.0250  -0.0064 283 THR A C   
2287 O O   . THR A 284 ? 0.1916 0.1794 0.2787 -0.0213 0.0227  -0.0104 283 THR A O   
2288 C CB  . THR A 284 ? 0.2553 0.2429 0.3435 -0.0280 0.0321  0.0024  283 THR A CB  
2289 O OG1 . THR A 284 ? 0.2181 0.2107 0.3050 -0.0273 0.0325  -0.0032 283 THR A OG1 
2290 C CG2 . THR A 284 ? 0.2697 0.2576 0.3495 -0.0298 0.0351  0.0095  283 THR A CG2 
2291 N N   . GLY A 285 ? 0.1905 0.1741 0.2941 -0.0247 0.0252  -0.0081 284 GLY A N   
2292 C CA  . GLY A 285 ? 0.2041 0.1888 0.3137 -0.0237 0.0225  -0.0154 284 GLY A CA  
2293 C C   . GLY A 285 ? 0.1947 0.1847 0.3029 -0.0237 0.0225  -0.0199 284 GLY A C   
2294 O O   . GLY A 285 ? 0.2151 0.2073 0.3214 -0.0219 0.0194  -0.0250 284 GLY A O   
2295 N N   . MET A 286 ? 0.1724 0.1648 0.2820 -0.0257 0.0259  -0.0178 285 MET A N   
2296 C CA  . MET A 286 ? 0.1876 0.1852 0.2971 -0.0255 0.0258  -0.0219 285 MET A CA  
2297 C C   . MET A 286 ? 0.1892 0.1887 0.2875 -0.0231 0.0244  -0.0223 285 MET A C   
2298 O O   . MET A 286 ? 0.1772 0.1795 0.2748 -0.0217 0.0217  -0.0267 285 MET A O   
2299 C CB  . MET A 286 ? 0.1792 0.1794 0.2933 -0.0282 0.0305  -0.0196 285 MET A CB  
2300 C CG  . MET A 286 ? 0.2663 0.2659 0.3938 -0.0309 0.0318  -0.0204 285 MET A CG  
2301 S SD  . MET A 286 ? 0.3140 0.3173 0.4506 -0.0301 0.0279  -0.0289 285 MET A SD  
2302 C CE  . MET A 286 ? 0.3859 0.3957 0.5209 -0.0299 0.0301  -0.0302 285 MET A CE  
2303 N N   . GLN A 287 ? 0.1539 0.1520 0.2436 -0.0229 0.0258  -0.0176 286 GLN A N   
2304 C CA  . GLN A 287 ? 0.1964 0.1958 0.2759 -0.0208 0.0242  -0.0180 286 GLN A CA  
2305 C C   . GLN A 287 ? 0.1989 0.1971 0.2763 -0.0186 0.0199  -0.0208 286 GLN A C   
2306 O O   . GLN A 287 ? 0.1811 0.1812 0.2538 -0.0171 0.0178  -0.0233 286 GLN A O   
2307 C CB  . GLN A 287 ? 0.1970 0.1950 0.2681 -0.0212 0.0262  -0.0124 286 GLN A CB  
2308 C CG  . GLN A 287 ? 0.2644 0.2648 0.3346 -0.0234 0.0308  -0.0100 286 GLN A CG  
2309 C CD  . GLN A 287 ? 0.3529 0.3520 0.4148 -0.0243 0.0325  -0.0040 286 GLN A CD  
2310 O OE1 . GLN A 287 ? 0.3085 0.3042 0.3671 -0.0233 0.0302  -0.0011 286 GLN A OE1 
2311 N NE2 . GLN A 287 ? 0.3705 0.3727 0.4288 -0.0262 0.0366  -0.0023 286 GLN A NE2 
2312 N N   . MET A 288 ? 0.1865 0.1815 0.2677 -0.0185 0.0188  -0.0206 287 MET A N   
2313 C CA  . MET A 288 ? 0.1925 0.1872 0.2725 -0.0167 0.0154  -0.0241 287 MET A CA  
2314 C C   . MET A 288 ? 0.1730 0.1707 0.2567 -0.0165 0.0131  -0.0298 287 MET A C   
2315 O O   . MET A 288 ? 0.1815 0.1808 0.2601 -0.0151 0.0104  -0.0323 287 MET A O   
2316 C CB  . MET A 288 ? 0.2023 0.1932 0.2875 -0.0166 0.0150  -0.0234 287 MET A CB  
2317 C CG  . MET A 288 ? 0.2260 0.2145 0.3058 -0.0156 0.0151  -0.0189 287 MET A CG  
2318 S SD  . MET A 288 ? 0.2348 0.2254 0.3068 -0.0132 0.0122  -0.0217 287 MET A SD  
2319 C CE  . MET A 288 ? 0.2676 0.2563 0.3331 -0.0125 0.0126  -0.0154 287 MET A CE  
2320 N N   . GLU A 289 ? 0.1675 0.1659 0.2601 -0.0181 0.0139  -0.0316 288 GLU A N   
2321 C CA  . GLU A 289 ? 0.1572 0.1589 0.2538 -0.0180 0.0113  -0.0368 288 GLU A CA  
2322 C C   . GLU A 289 ? 0.1911 0.1961 0.2820 -0.0170 0.0101  -0.0372 288 GLU A C   
2323 O O   . GLU A 289 ? 0.2031 0.2101 0.2913 -0.0158 0.0066  -0.0402 288 GLU A O   
2324 C CB  . GLU A 289 ? 0.1719 0.1741 0.2800 -0.0201 0.0128  -0.0382 288 GLU A CB  
2325 C CG  . GLU A 289 ? 0.2298 0.2354 0.3436 -0.0202 0.0095  -0.0439 288 GLU A CG  
2326 C CD  . GLU A 289 ? 0.3054 0.3118 0.4318 -0.0226 0.0111  -0.0452 288 GLU A CD  
2327 O OE1 . GLU A 289 ? 0.3456 0.3539 0.4750 -0.0237 0.0141  -0.0431 288 GLU A OE1 
2328 O OE2 . GLU A 289 ? 0.3680 0.3733 0.5016 -0.0235 0.0096  -0.0486 288 GLU A OE2 
2329 N N   . SER A 290 ? 0.1730 0.1785 0.2621 -0.0174 0.0131  -0.0340 289 SER A N   
2330 C CA  . SER A 290 ? 0.2019 0.2101 0.2867 -0.0162 0.0121  -0.0346 289 SER A CA  
2331 C C   . SER A 290 ? 0.1762 0.1833 0.2511 -0.0145 0.0098  -0.0337 289 SER A C   
2332 O O   . SER A 290 ? 0.1792 0.1880 0.2517 -0.0133 0.0067  -0.0354 289 SER A O   
2333 C CB  . SER A 290 ? 0.2109 0.2201 0.2959 -0.0171 0.0164  -0.0322 289 SER A CB  
2334 O OG  . SER A 290 ? 0.3143 0.3261 0.3973 -0.0159 0.0155  -0.0336 289 SER A OG  
2335 N N   . PHE A 291 ? 0.1920 0.1964 0.2616 -0.0143 0.0110  -0.0307 290 PHE A N   
2336 C CA  . PHE A 291 ? 0.2191 0.2227 0.2805 -0.0130 0.0090  -0.0299 290 PHE A CA  
2337 C C   . PHE A 291 ? 0.2028 0.2076 0.2642 -0.0123 0.0054  -0.0333 290 PHE A C   
2338 O O   . PHE A 291 ? 0.1853 0.1913 0.2415 -0.0115 0.0030  -0.0337 290 PHE A O   
2339 C CB  . PHE A 291 ? 0.2224 0.2232 0.2812 -0.0131 0.0107  -0.0265 290 PHE A CB  
2340 C CG  . PHE A 291 ? 0.2251 0.2254 0.2769 -0.0118 0.0090  -0.0257 290 PHE A CG  
2341 C CD1 . PHE A 291 ? 0.1629 0.1647 0.2092 -0.0110 0.0070  -0.0264 290 PHE A CD1 
2342 C CD2 . PHE A 291 ? 0.2634 0.2616 0.3152 -0.0115 0.0093  -0.0240 290 PHE A CD2 
2343 C CE1 . PHE A 291 ? 0.2012 0.2028 0.2418 -0.0102 0.0058  -0.0256 290 PHE A CE1 
2344 C CE2 . PHE A 291 ? 0.2519 0.2502 0.2985 -0.0104 0.0079  -0.0235 290 PHE A CE2 
2345 C CZ  . PHE A 291 ? 0.1729 0.1731 0.2138 -0.0099 0.0063  -0.0243 290 PHE A CZ  
2346 N N   . LYS A 292 ? 0.2020 0.2064 0.2690 -0.0129 0.0051  -0.0357 291 LYS A N   
2347 C CA  . LYS A 292 ? 0.2060 0.2122 0.2723 -0.0125 0.0019  -0.0396 291 LYS A CA  
2348 C C   . LYS A 292 ? 0.1858 0.1951 0.2523 -0.0125 -0.0011 -0.0416 291 LYS A C   
2349 O O   . LYS A 292 ? 0.1751 0.1860 0.2360 -0.0119 -0.0040 -0.0426 291 LYS A O   
2350 C CB  . LYS A 292 ? 0.2114 0.2167 0.2850 -0.0133 0.0021  -0.0427 291 LYS A CB  
2351 C CG  . LYS A 292 ? 0.2386 0.2459 0.3100 -0.0129 -0.0006 -0.0472 291 LYS A CG  
2352 C CD  . LYS A 292 ? 0.2907 0.2972 0.3704 -0.0137 -0.0005 -0.0515 291 LYS A CD  
2353 C CE  . LYS A 292 ? 0.3334 0.3426 0.4098 -0.0134 -0.0029 -0.0567 291 LYS A CE  
2354 N NZ  . LYS A 292 ? 0.3624 0.3713 0.4475 -0.0141 -0.0032 -0.0622 291 LYS A NZ  
2355 N N   . SER A 293 ? 0.1401 0.1503 0.2135 -0.0131 -0.0005 -0.0422 292 SER A N   
2356 C CA  . SER A 293 ? 0.1532 0.1666 0.2286 -0.0128 -0.0039 -0.0441 292 SER A CA  
2357 C C   . SER A 293 ? 0.1798 0.1933 0.2483 -0.0116 -0.0053 -0.0417 292 SER A C   
2358 O O   . SER A 293 ? 0.1923 0.2076 0.2581 -0.0111 -0.0093 -0.0425 292 SER A O   
2359 C CB  . SER A 293 ? 0.2393 0.2540 0.3246 -0.0136 -0.0024 -0.0451 292 SER A CB  
2360 O OG  . SER A 293 ? 0.3769 0.3914 0.4696 -0.0150 -0.0016 -0.0475 292 SER A OG  
2361 N N   . LYS A 294 ? 0.1454 0.1571 0.2111 -0.0113 -0.0023 -0.0387 293 LYS A N   
2362 C CA  . LYS A 294 ? 0.1609 0.1724 0.2211 -0.0102 -0.0036 -0.0368 293 LYS A CA  
2363 C C   . LYS A 294 ? 0.1694 0.1801 0.2211 -0.0099 -0.0056 -0.0356 293 LYS A C   
2364 O O   . LYS A 294 ? 0.1433 0.1545 0.1914 -0.0094 -0.0085 -0.0347 293 LYS A O   
2365 C CB  . LYS A 294 ? 0.1988 0.2091 0.2584 -0.0101 0.0001  -0.0348 293 LYS A CB  
2366 C CG  . LYS A 294 ? 0.2389 0.2512 0.3065 -0.0103 0.0017  -0.0363 293 LYS A CG  
2367 C CD  . LYS A 294 ? 0.2844 0.2963 0.3504 -0.0104 0.0057  -0.0349 293 LYS A CD  
2368 C CE  . LYS A 294 ? 0.2624 0.2737 0.3294 -0.0119 0.0102  -0.0334 293 LYS A CE  
2369 N NZ  . LYS A 294 ? 0.2283 0.2405 0.2940 -0.0124 0.0143  -0.0326 293 LYS A NZ  
2370 N N   . LEU A 295 ? 0.1428 0.1525 0.1922 -0.0103 -0.0040 -0.0355 294 LEU A N   
2371 C CA  . LEU A 295 ? 0.1926 0.2026 0.2351 -0.0102 -0.0054 -0.0352 294 LEU A CA  
2372 C C   . LEU A 295 ? 0.1951 0.2078 0.2364 -0.0105 -0.0092 -0.0374 294 LEU A C   
2373 O O   . LEU A 295 ? 0.1831 0.1967 0.2182 -0.0106 -0.0114 -0.0361 294 LEU A O   
2374 C CB  . LEU A 295 ? 0.2146 0.2234 0.2570 -0.0104 -0.0031 -0.0356 294 LEU A CB  
2375 C CG  . LEU A 295 ? 0.3309 0.3379 0.3691 -0.0100 -0.0011 -0.0325 294 LEU A CG  
2376 C CD1 . LEU A 295 ? 0.3143 0.3206 0.3543 -0.0099 0.0004  -0.0335 294 LEU A CD1 
2377 C CD2 . LEU A 295 ? 0.2421 0.2499 0.2734 -0.0098 -0.0027 -0.0309 294 LEU A CD2 
2378 N N   . GLN A 296 ? 0.1878 0.2019 0.2350 -0.0110 -0.0101 -0.0407 295 GLN A N   
2379 C CA  . GLN A 296 ? 0.2291 0.2463 0.2750 -0.0114 -0.0142 -0.0432 295 GLN A CA  
2380 C C   . GLN A 296 ? 0.1915 0.2096 0.2365 -0.0110 -0.0178 -0.0411 295 GLN A C   
2381 O O   . GLN A 296 ? 0.1670 0.1871 0.2064 -0.0113 -0.0214 -0.0405 295 GLN A O   
2382 C CB  . GLN A 296 ? 0.1869 0.2054 0.2406 -0.0121 -0.0146 -0.0475 295 GLN A CB  
2383 C CG  . GLN A 296 ? 0.2492 0.2714 0.3013 -0.0128 -0.0191 -0.0507 295 GLN A CG  
2384 C CD  . GLN A 296 ? 0.2727 0.2965 0.3167 -0.0133 -0.0192 -0.0523 295 GLN A CD  
2385 O OE1 . GLN A 296 ? 0.2764 0.2993 0.3217 -0.0134 -0.0163 -0.0547 295 GLN A OE1 
2386 N NE2 . GLN A 296 ? 0.2430 0.2693 0.2789 -0.0136 -0.0226 -0.0509 295 GLN A NE2 
2387 N N   . ALA A 297 ? 0.1855 0.2025 0.2364 -0.0103 -0.0169 -0.0401 296 ALA A N   
2388 C CA  . ALA A 297 ? 0.1954 0.2129 0.2470 -0.0095 -0.0203 -0.0383 296 ALA A CA  
2389 C C   . ALA A 297 ? 0.1763 0.1920 0.2199 -0.0092 -0.0210 -0.0345 296 ALA A C   
2390 O O   . ALA A 297 ? 0.1739 0.1902 0.2148 -0.0091 -0.0252 -0.0326 296 ALA A O   
2391 C CB  . ALA A 297 ? 0.1966 0.2137 0.2569 -0.0087 -0.0183 -0.0387 296 ALA A CB  
2392 N N   . LEU A 298 ? 0.1466 0.1601 0.1865 -0.0093 -0.0172 -0.0332 297 LEU A N   
2393 C CA  . LEU A 298 ? 0.1387 0.1508 0.1716 -0.0093 -0.0176 -0.0299 297 LEU A CA  
2394 C C   . LEU A 298 ? 0.1654 0.1795 0.1914 -0.0104 -0.0199 -0.0294 297 LEU A C   
2395 O O   . LEU A 298 ? 0.1402 0.1541 0.1617 -0.0108 -0.0226 -0.0265 297 LEU A O   
2396 C CB  . LEU A 298 ? 0.1811 0.1911 0.2120 -0.0093 -0.0133 -0.0290 297 LEU A CB  
2397 C CG  . LEU A 298 ? 0.1843 0.1932 0.2086 -0.0096 -0.0133 -0.0261 297 LEU A CG  
2398 C CD1 . LEU A 298 ? 0.1668 0.1742 0.1913 -0.0092 -0.0160 -0.0239 297 LEU A CD1 
2399 C CD2 . LEU A 298 ? 0.1276 0.1349 0.1508 -0.0095 -0.0095 -0.0256 297 LEU A CD2 
2400 N N   . LEU A 299 ? 0.1666 0.1825 0.1916 -0.0111 -0.0187 -0.0323 298 LEU A N   
2401 C CA  . LEU A 299 ? 0.1900 0.2088 0.2081 -0.0123 -0.0203 -0.0328 298 LEU A CA  
2402 C C   . LEU A 299 ? 0.2130 0.2340 0.2296 -0.0127 -0.0255 -0.0321 298 LEU A C   
2403 O O   . LEU A 299 ? 0.1965 0.2189 0.2057 -0.0138 -0.0277 -0.0295 298 LEU A O   
2404 C CB  . LEU A 299 ? 0.2218 0.2423 0.2412 -0.0126 -0.0181 -0.0373 298 LEU A CB  
2405 C CG  . LEU A 299 ? 0.2870 0.3115 0.2993 -0.0140 -0.0194 -0.0390 298 LEU A CG  
2406 C CD1 . LEU A 299 ? 0.2479 0.2725 0.2535 -0.0146 -0.0175 -0.0362 298 LEU A CD1 
2407 C CD2 . LEU A 299 ? 0.4084 0.4347 0.4241 -0.0142 -0.0178 -0.0447 298 LEU A CD2 
2408 N N   . ASN A 300 ? 0.2081 0.2297 0.2317 -0.0121 -0.0276 -0.0342 299 ASN A N   
2409 C CA  . ASN A 300 ? 0.2005 0.2242 0.2238 -0.0123 -0.0332 -0.0334 299 ASN A CA  
2410 C C   . ASN A 300 ? 0.2083 0.2299 0.2299 -0.0118 -0.0360 -0.0281 299 ASN A C   
2411 O O   . ASN A 300 ? 0.2272 0.2503 0.2436 -0.0126 -0.0404 -0.0253 299 ASN A O   
2412 C CB  . ASN A 300 ? 0.2087 0.2335 0.2420 -0.0115 -0.0347 -0.0367 299 ASN A CB  
2413 C CG  . ASN A 300 ? 0.2772 0.3041 0.3129 -0.0123 -0.0329 -0.0420 299 ASN A CG  
2414 O OD1 . ASN A 300 ? 0.3060 0.3342 0.3355 -0.0133 -0.0315 -0.0437 299 ASN A OD1 
2415 N ND2 . ASN A 300 ? 0.3123 0.3397 0.3580 -0.0119 -0.0329 -0.0449 299 ASN A ND2 
2416 N N   . ALA A 301 ? 0.2102 0.2283 0.2361 -0.0107 -0.0334 -0.0266 300 ALA A N   
2417 C CA  . ALA A 301 ? 0.2029 0.2183 0.2283 -0.0102 -0.0359 -0.0221 300 ALA A CA  
2418 C C   . ALA A 301 ? 0.2405 0.2554 0.2563 -0.0117 -0.0356 -0.0184 300 ALA A C   
2419 O O   . ALA A 301 ? 0.2192 0.2334 0.2321 -0.0123 -0.0395 -0.0141 300 ALA A O   
2420 C CB  . ALA A 301 ? 0.2311 0.2434 0.2634 -0.0087 -0.0328 -0.0226 300 ALA A CB  
2421 N N   . LEU A 302 ? 0.1768 0.1921 0.1883 -0.0125 -0.0311 -0.0197 301 LEU A N   
2422 C CA  . LEU A 302 ? 0.1542 0.1700 0.1572 -0.0142 -0.0303 -0.0167 301 LEU A CA  
2423 C C   . LEU A 302 ? 0.2098 0.2294 0.2058 -0.0159 -0.0338 -0.0155 301 LEU A C   
2424 O O   . LEU A 302 ? 0.2227 0.2423 0.2128 -0.0174 -0.0357 -0.0109 301 LEU A O   
2425 C CB  . LEU A 302 ? 0.1335 0.1500 0.1348 -0.0144 -0.0251 -0.0192 301 LEU A CB  
2426 C CG  . LEU A 302 ? 0.2051 0.2181 0.2107 -0.0133 -0.0219 -0.0191 301 LEU A CG  
2427 C CD1 . LEU A 302 ? 0.1802 0.1940 0.1861 -0.0131 -0.0175 -0.0220 301 LEU A CD1 
2428 C CD2 . LEU A 302 ? 0.1914 0.2023 0.1944 -0.0139 -0.0224 -0.0149 301 LEU A CD2 
2429 N N   . LYS A 303 ? 0.2106 0.2336 0.2068 -0.0160 -0.0347 -0.0196 302 LYS A N   
2430 C CA  . LYS A 303 ? 0.2588 0.2861 0.2476 -0.0178 -0.0384 -0.0190 302 LYS A CA  
2431 C C   . LYS A 303 ? 0.2707 0.2971 0.2601 -0.0177 -0.0447 -0.0144 302 LYS A C   
2432 O O   . LYS A 303 ? 0.3002 0.3283 0.2815 -0.0196 -0.0478 -0.0101 302 LYS A O   
2433 C CB  . LYS A 303 ? 0.2773 0.3084 0.2673 -0.0178 -0.0382 -0.0253 302 LYS A CB  
2434 C CG  . LYS A 303 ? 0.2927 0.3257 0.2803 -0.0184 -0.0329 -0.0297 302 LYS A CG  
2435 C CD  . LYS A 303 ? 0.3635 0.3998 0.3536 -0.0185 -0.0335 -0.0363 302 LYS A CD  
2436 C CE  . LYS A 303 ? 0.4329 0.4710 0.4222 -0.0188 -0.0285 -0.0413 302 LYS A CE  
2437 N NZ  . LYS A 303 ? 0.5127 0.5542 0.4920 -0.0207 -0.0268 -0.0400 302 LYS A NZ  
2438 N N   . THR A 304 ? 0.2394 0.2633 0.2387 -0.0156 -0.0468 -0.0150 303 THR A N   
2439 C CA  . THR A 304 ? 0.2724 0.2951 0.2747 -0.0149 -0.0531 -0.0108 303 THR A CA  
2440 C C   . THR A 304 ? 0.3042 0.3233 0.3035 -0.0155 -0.0541 -0.0043 303 THR A C   
2441 O O   . THR A 304 ? 0.3000 0.3190 0.2958 -0.0165 -0.0595 0.0010  303 THR A O   
2442 C CB  . THR A 304 ? 0.2687 0.2896 0.2839 -0.0123 -0.0539 -0.0135 303 THR A CB  
2443 O OG1 . THR A 304 ? 0.3071 0.3315 0.3256 -0.0122 -0.0533 -0.0192 303 THR A OG1 
2444 C CG2 . THR A 304 ? 0.2831 0.3028 0.3035 -0.0112 -0.0606 -0.0095 303 THR A CG2 
2445 N N   . ALA A 305 ? 0.2824 0.2981 0.2833 -0.0152 -0.0492 -0.0043 304 ALA A N   
2446 C CA  . ALA A 305 ? 0.2522 0.2642 0.2515 -0.0159 -0.0497 0.0013  304 ALA A CA  
2447 C C   . ALA A 305 ? 0.3515 0.3658 0.3393 -0.0190 -0.0501 0.0056  304 ALA A C   
2448 O O   . ALA A 305 ? 0.4064 0.4180 0.3926 -0.0202 -0.0519 0.0114  304 ALA A O   
2449 C CB  . ALA A 305 ? 0.2349 0.2438 0.2379 -0.0151 -0.0443 -0.0007 304 ALA A CB  
2450 N N   . LYS A 306 ? 0.2794 0.2989 0.2597 -0.0205 -0.0482 0.0026  305 LYS A N   
2451 C CA  . LYS A 306 ? 0.3170 0.3400 0.2860 -0.0237 -0.0482 0.0062  305 LYS A CA  
2452 C C   . LYS A 306 ? 0.3518 0.3765 0.3159 -0.0250 -0.0550 0.0109  305 LYS A C   
2453 O O   . LYS A 306 ? 0.4320 0.4578 0.3876 -0.0278 -0.0564 0.0168  305 LYS A O   
2454 C CB  . LYS A 306 ? 0.3507 0.3791 0.3139 -0.0248 -0.0435 0.0005  305 LYS A CB  
2455 C CG  . LYS A 306 ? 0.4243 0.4570 0.3760 -0.0282 -0.0416 0.0031  305 LYS A CG  
2456 C CD  . LYS A 306 ? 0.4617 0.5001 0.4094 -0.0288 -0.0369 -0.0038 305 LYS A CD  
2457 C CE  . LYS A 306 ? 0.4994 0.5428 0.4364 -0.0323 -0.0342 -0.0017 305 LYS A CE  
2458 N NZ  . LYS A 306 ? 0.5150 0.5641 0.4492 -0.0327 -0.0292 -0.0092 305 LYS A NZ  
2459 N N   . SER A 307 ? 0.4265 0.4516 0.3961 -0.0231 -0.0595 0.0088  306 SER A N   
2460 C CA  . SER A 307 ? 0.4917 0.5196 0.4563 -0.0243 -0.0665 0.0125  306 SER A CA  
2461 C C   . SER A 307 ? 0.5124 0.5356 0.4847 -0.0226 -0.0731 0.0182  306 SER A C   
2462 O O   . SER A 307 ? 0.5493 0.5744 0.5178 -0.0235 -0.0798 0.0225  306 SER A O   
2463 C CB  . SER A 307 ? 0.5084 0.5414 0.4731 -0.0237 -0.0678 0.0057  306 SER A CB  
2464 O OG  . SER A 307 ? 0.5521 0.5826 0.5300 -0.0205 -0.0684 0.0017  306 SER A OG  
2465 N N   . ARG A 308 ? 0.4921 0.5096 0.4755 -0.0203 -0.0717 0.0181  307 ARG A N   
2466 C CA  . ARG A 308 ? 0.4999 0.5130 0.4929 -0.0182 -0.0778 0.0223  307 ARG A CA  
2467 C C   . ARG A 308 ? 0.5427 0.5530 0.5302 -0.0204 -0.0820 0.0318  307 ARG A C   
2468 O O   . ARG A 308 ? 0.5320 0.5405 0.5146 -0.0225 -0.0781 0.0347  307 ARG A O   
2469 C CB  . ARG A 308 ? 0.4677 0.4758 0.4735 -0.0153 -0.0745 0.0189  307 ARG A CB  
2470 C CG  . ARG A 308 ? 0.5036 0.5140 0.5167 -0.0130 -0.0713 0.0106  307 ARG A CG  
2471 C CD  . ARG A 308 ? 0.5585 0.5725 0.5757 -0.0120 -0.0769 0.0089  307 ARG A CD  
2472 N NE  . ARG A 308 ? 0.5885 0.6084 0.5952 -0.0142 -0.0770 0.0070  307 ARG A NE  
2473 C CZ  . ARG A 308 ? 0.6009 0.6249 0.6071 -0.0143 -0.0827 0.0064  307 ARG A CZ  
2474 N NH1 . ARG A 308 ? 0.6373 0.6603 0.6538 -0.0121 -0.0889 0.0079  307 ARG A NH1 
2475 N NH2 . ARG A 308 ? 0.5788 0.6082 0.5749 -0.0164 -0.0823 0.0038  307 ARG A NH2 
2476 N N   . LEU A 309 ? 0.5843 0.5945 0.5735 -0.0201 -0.0900 0.0368  308 LEU A N   
2477 C CA  . LEU A 309 ? 0.6169 0.6238 0.6021 -0.0221 -0.0950 0.0468  308 LEU A CA  
2478 C C   . LEU A 309 ? 0.5780 0.5769 0.5746 -0.0205 -0.0945 0.0494  308 LEU A C   
2479 O O   . LEU A 309 ? 0.6266 0.6223 0.6193 -0.0229 -0.0941 0.0558  308 LEU A O   
2480 C CB  . LEU A 309 ? 0.6882 0.6967 0.6734 -0.0218 -0.1045 0.0516  308 LEU A CB  
2481 C CG  . LEU A 309 ? 0.7542 0.7606 0.7323 -0.0247 -0.1103 0.0631  308 LEU A CG  
2482 C CD1 . LEU A 309 ? 0.7824 0.7944 0.7416 -0.0296 -0.1072 0.0656  308 LEU A CD1 
2483 C CD2 . LEU A 309 ? 0.7529 0.7594 0.7358 -0.0232 -0.1207 0.0677  308 LEU A CD2 
2484 N N   . GLU A 310 ? 0.4621 0.4583 0.4731 -0.0166 -0.0944 0.0441  309 GLU A N   
2485 C CA  . GLU A 310 ? 0.3843 0.3734 0.4071 -0.0147 -0.0937 0.0448  309 GLU A CA  
2486 C C   . GLU A 310 ? 0.3415 0.3302 0.3646 -0.0145 -0.0849 0.0383  309 GLU A C   
2487 O O   . GLU A 310 ? 0.2955 0.2878 0.3197 -0.0131 -0.0806 0.0307  309 GLU A O   
2488 C CB  . GLU A 310 ? 0.4178 0.4048 0.4567 -0.0105 -0.0984 0.0423  309 GLU A CB  
2489 C CG  . GLU A 310 ? 0.5034 0.4900 0.5446 -0.0101 -0.1083 0.0494  309 GLU A CG  
2490 C CD  . GLU A 310 ? 0.5117 0.4910 0.5573 -0.0107 -0.1129 0.0580  309 GLU A CD  
2491 O OE1 . GLU A 310 ? 0.5159 0.4906 0.5635 -0.0113 -0.1082 0.0579  309 GLU A OE1 
2492 O OE2 . GLU A 310 ? 0.4912 0.4693 0.5389 -0.0105 -0.1214 0.0651  309 GLU A OE2 
2493 N N   . LEU A 311 ? 0.2841 0.2684 0.3066 -0.0160 -0.0824 0.0415  310 LEU A N   
2494 C CA  . LEU A 311 ? 0.2961 0.2794 0.3200 -0.0157 -0.0750 0.0358  310 LEU A CA  
2495 C C   . LEU A 311 ? 0.2590 0.2412 0.2955 -0.0118 -0.0734 0.0284  310 LEU A C   
2496 O O   . LEU A 311 ? 0.2401 0.2244 0.2760 -0.0111 -0.0674 0.0219  310 LEU A O   
2497 C CB  . LEU A 311 ? 0.3435 0.3216 0.3679 -0.0176 -0.0742 0.0405  310 LEU A CB  
2498 C CG  . LEU A 311 ? 0.3656 0.3429 0.3903 -0.0179 -0.0672 0.0356  310 LEU A CG  
2499 C CD1 . LEU A 311 ? 0.3510 0.3340 0.3634 -0.0204 -0.0619 0.0342  310 LEU A CD1 
2500 C CD2 . LEU A 311 ? 0.4225 0.3936 0.4519 -0.0191 -0.0680 0.0399  310 LEU A CD2 
2501 N N   . HIS A 312 ? 0.2776 0.2564 0.3257 -0.0092 -0.0788 0.0294  311 HIS A N   
2502 C CA  . HIS A 312 ? 0.2499 0.2285 0.3106 -0.0055 -0.0772 0.0221  311 HIS A CA  
2503 C C   . HIS A 312 ? 0.2654 0.2502 0.3236 -0.0048 -0.0739 0.0160  311 HIS A C   
2504 O O   . HIS A 312 ? 0.2834 0.2693 0.3451 -0.0036 -0.0683 0.0094  311 HIS A O   
2505 C CB  . HIS A 312 ? 0.2699 0.2454 0.3439 -0.0028 -0.0842 0.0242  311 HIS A CB  
2506 C CG  . HIS A 312 ? 0.3186 0.2957 0.4055 0.0008  -0.0827 0.0165  311 HIS A CG  
2507 N ND1 . HIS A 312 ? 0.3484 0.3224 0.4456 0.0029  -0.0793 0.0114  311 HIS A ND1 
2508 C CD2 . HIS A 312 ? 0.3470 0.3289 0.4381 0.0025  -0.0838 0.0127  311 HIS A CD2 
2509 C CE1 . HIS A 312 ? 0.3091 0.2862 0.4162 0.0056  -0.0781 0.0050  311 HIS A CE1 
2510 N NE2 . HIS A 312 ? 0.3257 0.3075 0.4298 0.0054  -0.0808 0.0058  311 HIS A NE2 
2511 N N   . ASP A 313 ? 0.2314 0.2204 0.2837 -0.0058 -0.0776 0.0182  312 ASP A N   
2512 C CA  . ASP A 313 ? 0.2647 0.2593 0.3163 -0.0052 -0.0754 0.0123  312 ASP A CA  
2513 C C   . ASP A 313 ? 0.2856 0.2827 0.3275 -0.0071 -0.0681 0.0087  312 ASP A C   
2514 O O   . ASP A 313 ? 0.2901 0.2895 0.3352 -0.0060 -0.0635 0.0025  312 ASP A O   
2515 C CB  . ASP A 313 ? 0.2835 0.2820 0.3311 -0.0059 -0.0817 0.0152  312 ASP A CB  
2516 C CG  . ASP A 313 ? 0.3634 0.3598 0.4215 -0.0038 -0.0898 0.0190  312 ASP A CG  
2517 O OD1 . ASP A 313 ? 0.3808 0.3739 0.4524 -0.0010 -0.0898 0.0168  312 ASP A OD1 
2518 O OD2 . ASP A 313 ? 0.3594 0.3577 0.4123 -0.0050 -0.0964 0.0242  312 ASP A OD2 
2519 N N   . ALA A 314 ? 0.2972 0.2942 0.3278 -0.0099 -0.0668 0.0128  313 ALA A N   
2520 C CA  . ALA A 314 ? 0.2966 0.2959 0.3195 -0.0114 -0.0600 0.0094  313 ALA A CA  
2521 C C   . ALA A 314 ? 0.2476 0.2440 0.2765 -0.0099 -0.0547 0.0054  313 ALA A C   
2522 O O   . ALA A 314 ? 0.2194 0.2180 0.2481 -0.0095 -0.0497 0.0002  313 ALA A O   
2523 C CB  . ALA A 314 ? 0.3128 0.3126 0.3241 -0.0147 -0.0596 0.0146  313 ALA A CB  
2524 N N   . CYS A 315 ? 0.2344 0.2259 0.2693 -0.0092 -0.0560 0.0076  314 CYS A N   
2525 C CA  . CYS A 315 ? 0.2301 0.2192 0.2698 -0.0081 -0.0513 0.0035  314 CYS A CA  
2526 C C   . CYS A 315 ? 0.2163 0.2067 0.2653 -0.0054 -0.0496 -0.0025 314 CYS A C   
2527 O O   . CYS A 315 ? 0.1995 0.1907 0.2486 -0.0050 -0.0442 -0.0070 314 CYS A O   
2528 C CB  . CYS A 315 ? 0.2334 0.2170 0.2776 -0.0081 -0.0533 0.0068  314 CYS A CB  
2529 S SG  . CYS A 315 ? 0.2261 0.2086 0.2598 -0.0119 -0.0529 0.0131  314 CYS A SG  
2530 N N   . LYS A 316 ? 0.2023 0.1930 0.2593 -0.0036 -0.0542 -0.0025 315 LYS A N   
2531 C CA  . LYS A 316 ? 0.2243 0.2172 0.2909 -0.0013 -0.0524 -0.0083 315 LYS A CA  
2532 C C   . LYS A 316 ? 0.2094 0.2069 0.2711 -0.0021 -0.0485 -0.0118 315 LYS A C   
2533 O O   . LYS A 316 ? 0.2081 0.2068 0.2732 -0.0014 -0.0435 -0.0166 315 LYS A O   
2534 C CB  . LYS A 316 ? 0.2540 0.2470 0.3305 0.0007  -0.0587 -0.0072 315 LYS A CB  
2535 C CG  . LYS A 316 ? 0.3084 0.3043 0.3967 0.0031  -0.0571 -0.0133 315 LYS A CG  
2536 C CD  . LYS A 316 ? 0.4291 0.4231 0.5238 0.0044  -0.0520 -0.0179 315 LYS A CD  
2537 C CE  . LYS A 316 ? 0.4667 0.4634 0.5755 0.0070  -0.0512 -0.0233 315 LYS A CE  
2538 N NZ  . LYS A 316 ? 0.4473 0.4491 0.5557 0.0064  -0.0467 -0.0275 315 LYS A NZ  
2539 N N   . ALA A 317 ? 0.2278 0.2279 0.2817 -0.0037 -0.0507 -0.0095 316 ALA A N   
2540 C CA  . ALA A 317 ? 0.2195 0.2236 0.2692 -0.0046 -0.0472 -0.0130 316 ALA A CA  
2541 C C   . ALA A 317 ? 0.2105 0.2138 0.2558 -0.0053 -0.0406 -0.0150 316 ALA A C   
2542 O O   . ALA A 317 ? 0.2041 0.2092 0.2515 -0.0051 -0.0365 -0.0191 316 ALA A O   
2543 C CB  . ALA A 317 ? 0.2374 0.2443 0.2777 -0.0066 -0.0503 -0.0104 316 ALA A CB  
2544 N N   . LEU A 318 ? 0.1870 0.1876 0.2267 -0.0064 -0.0397 -0.0120 317 LEU A N   
2545 C CA  . LEU A 318 ? 0.1978 0.1978 0.2337 -0.0070 -0.0341 -0.0138 317 LEU A CA  
2546 C C   . LEU A 318 ? 0.1618 0.1601 0.2048 -0.0054 -0.0310 -0.0171 317 LEU A C   
2547 O O   . LEU A 318 ? 0.1528 0.1522 0.1950 -0.0054 -0.0264 -0.0200 317 LEU A O   
2548 C CB  . LEU A 318 ? 0.1892 0.1874 0.2180 -0.0087 -0.0342 -0.0098 317 LEU A CB  
2549 C CG  . LEU A 318 ? 0.2435 0.2445 0.2639 -0.0107 -0.0357 -0.0073 317 LEU A CG  
2550 C CD1 . LEU A 318 ? 0.2871 0.2868 0.3012 -0.0127 -0.0358 -0.0029 317 LEU A CD1 
2551 C CD2 . LEU A 318 ? 0.2461 0.2505 0.2633 -0.0110 -0.0319 -0.0110 317 LEU A CD2 
2552 N N   . ALA A 319 ? 0.1818 0.1776 0.2317 -0.0040 -0.0336 -0.0167 318 ALA A N   
2553 C CA  . ALA A 319 ? 0.2228 0.2176 0.2795 -0.0026 -0.0306 -0.0206 318 ALA A CA  
2554 C C   . ALA A 319 ? 0.1947 0.1929 0.2565 -0.0017 -0.0276 -0.0249 318 ALA A C   
2555 O O   . ALA A 319 ? 0.1851 0.1839 0.2482 -0.0014 -0.0229 -0.0281 318 ALA A O   
2556 C CB  . ALA A 319 ? 0.2106 0.2022 0.2757 -0.0010 -0.0344 -0.0200 318 ALA A CB  
2557 N N   . ASP A 320 ? 0.1840 0.1847 0.2485 -0.0015 -0.0302 -0.0248 319 ASP A N   
2558 C CA  . ASP A 320 ? 0.2312 0.2355 0.3013 -0.0010 -0.0274 -0.0287 319 ASP A CA  
2559 C C   . ASP A 320 ? 0.2037 0.2090 0.2677 -0.0024 -0.0218 -0.0300 319 ASP A C   
2560 O O   . ASP A 320 ? 0.1794 0.1868 0.2479 -0.0023 -0.0181 -0.0330 319 ASP A O   
2561 C CB  . ASP A 320 ? 0.2208 0.2278 0.2936 -0.0010 -0.0316 -0.0283 319 ASP A CB  
2562 C CG  . ASP A 320 ? 0.2036 0.2102 0.2849 0.0007  -0.0373 -0.0274 319 ASP A CG  
2563 O OD1 . ASP A 320 ? 0.2397 0.2444 0.3279 0.0022  -0.0369 -0.0287 319 ASP A OD1 
2564 O OD2 . ASP A 320 ? 0.2311 0.2392 0.3123 0.0005  -0.0424 -0.0256 319 ASP A OD2 
2565 N N   . HIS A 321 ? 0.1180 0.1219 0.1724 -0.0038 -0.0212 -0.0275 320 HIS A N   
2566 C CA  . HIS A 321 ? 0.1244 0.1290 0.1739 -0.0048 -0.0165 -0.0282 320 HIS A CA  
2567 C C   . HIS A 321 ? 0.1785 0.1809 0.2231 -0.0051 -0.0138 -0.0275 320 HIS A C   
2568 O O   . HIS A 321 ? 0.1863 0.1893 0.2288 -0.0056 -0.0098 -0.0283 320 HIS A O   
2569 C CB  . HIS A 321 ? 0.1676 0.1732 0.2110 -0.0061 -0.0175 -0.0268 320 HIS A CB  
2570 C CG  . HIS A 321 ? 0.1723 0.1806 0.2198 -0.0060 -0.0203 -0.0281 320 HIS A CG  
2571 N ND1 . HIS A 321 ? 0.1822 0.1925 0.2335 -0.0063 -0.0180 -0.0308 320 HIS A ND1 
2572 C CD2 . HIS A 321 ? 0.1958 0.2049 0.2446 -0.0058 -0.0254 -0.0271 320 HIS A CD2 
2573 C CE1 . HIS A 321 ? 0.2046 0.2171 0.2596 -0.0063 -0.0216 -0.0319 320 HIS A CE1 
2574 N NE2 . HIS A 321 ? 0.1770 0.1890 0.2302 -0.0059 -0.0263 -0.0296 320 HIS A NE2 
2575 N N   . PHE A 322 ? 0.1974 0.1974 0.2408 -0.0049 -0.0162 -0.0258 321 PHE A N   
2576 C CA  . PHE A 322 ? 0.1822 0.1804 0.2215 -0.0054 -0.0142 -0.0254 321 PHE A CA  
2577 C C   . PHE A 322 ? 0.2049 0.2021 0.2494 -0.0043 -0.0131 -0.0282 321 PHE A C   
2578 O O   . PHE A 322 ? 0.1939 0.1902 0.2351 -0.0047 -0.0110 -0.0290 321 PHE A O   
2579 C CB  . PHE A 322 ? 0.2146 0.2109 0.2490 -0.0064 -0.0171 -0.0218 321 PHE A CB  
2580 C CG  . PHE A 322 ? 0.2202 0.2181 0.2480 -0.0077 -0.0167 -0.0199 321 PHE A CG  
2581 C CD1 . PHE A 322 ? 0.2279 0.2269 0.2520 -0.0082 -0.0131 -0.0206 321 PHE A CD1 
2582 C CD2 . PHE A 322 ? 0.2294 0.2280 0.2550 -0.0084 -0.0199 -0.0174 321 PHE A CD2 
2583 C CE1 . PHE A 322 ? 0.2241 0.2247 0.2437 -0.0091 -0.0127 -0.0195 321 PHE A CE1 
2584 C CE2 . PHE A 322 ? 0.2675 0.2682 0.2874 -0.0096 -0.0191 -0.0166 321 PHE A CE2 
2585 C CZ  . PHE A 322 ? 0.2588 0.2605 0.2763 -0.0099 -0.0154 -0.0179 321 PHE A CZ  
2586 N N   . GLY A 323 ? 0.1902 0.1877 0.2431 -0.0029 -0.0146 -0.0302 322 GLY A N   
2587 C CA  . GLY A 323 ? 0.1778 0.1750 0.2367 -0.0017 -0.0129 -0.0340 322 GLY A CA  
2588 C C   . GLY A 323 ? 0.2126 0.2062 0.2750 -0.0009 -0.0166 -0.0335 322 GLY A C   
2589 O O   . GLY A 323 ? 0.1857 0.1770 0.2470 -0.0013 -0.0209 -0.0295 322 GLY A O   
2590 N N   . SER A 324 ? 0.1817 0.1749 0.2484 -0.0001 -0.0145 -0.0376 323 SER A N   
2591 C CA  . SER A 324 ? 0.2459 0.2358 0.3202 0.0012  -0.0179 -0.0387 323 SER A CA  
2592 C C   . SER A 324 ? 0.2552 0.2410 0.3247 0.0000  -0.0204 -0.0355 323 SER A C   
2593 O O   . SER A 324 ? 0.2404 0.2224 0.3160 0.0007  -0.0243 -0.0345 323 SER A O   
2594 C CB  . SER A 324 ? 0.3089 0.3002 0.3898 0.0025  -0.0144 -0.0453 323 SER A CB  
2595 O OG  . SER A 324 ? 0.3337 0.3256 0.4071 0.0012  -0.0106 -0.0474 323 SER A OG  
2596 N N   . GLU A 325 ? 0.2331 0.2194 0.2926 -0.0019 -0.0183 -0.0337 324 GLU A N   
2597 C CA  . GLU A 325 ? 0.2453 0.2284 0.3010 -0.0034 -0.0205 -0.0307 324 GLU A CA  
2598 C C   . GLU A 325 ? 0.2361 0.2179 0.2888 -0.0045 -0.0242 -0.0245 324 GLU A C   
2599 O O   . GLU A 325 ? 0.2397 0.2189 0.2902 -0.0059 -0.0262 -0.0214 324 GLU A O   
2600 C CB  . GLU A 325 ? 0.2505 0.2351 0.2977 -0.0049 -0.0171 -0.0315 324 GLU A CB  
2601 C CG  . GLU A 325 ? 0.3609 0.3471 0.4089 -0.0043 -0.0135 -0.0373 324 GLU A CG  
2602 C CD  . GLU A 325 ? 0.4266 0.4096 0.4800 -0.0039 -0.0150 -0.0407 324 GLU A CD  
2603 O OE1 . GLU A 325 ? 0.4505 0.4297 0.5065 -0.0044 -0.0189 -0.0377 324 GLU A OE1 
2604 O OE2 . GLU A 325 ? 0.4346 0.4192 0.4898 -0.0032 -0.0122 -0.0464 324 GLU A OE2 
2605 N N   . PHE A 326 ? 0.2011 0.1851 0.2534 -0.0041 -0.0251 -0.0228 325 PHE A N   
2606 C CA  . PHE A 326 ? 0.2328 0.2162 0.2813 -0.0054 -0.0285 -0.0172 325 PHE A CA  
2607 C C   . PHE A 326 ? 0.2435 0.2233 0.2991 -0.0047 -0.0338 -0.0147 325 PHE A C   
2608 O O   . PHE A 326 ? 0.2098 0.1899 0.2734 -0.0027 -0.0354 -0.0165 325 PHE A O   
2609 C CB  . PHE A 326 ? 0.2301 0.2173 0.2753 -0.0055 -0.0281 -0.0166 325 PHE A CB  
2610 C CG  . PHE A 326 ? 0.2188 0.2067 0.2566 -0.0074 -0.0300 -0.0117 325 PHE A CG  
2611 C CD1 . PHE A 326 ? 0.1940 0.1808 0.2329 -0.0078 -0.0349 -0.0076 325 PHE A CD1 
2612 C CD2 . PHE A 326 ? 0.2253 0.2153 0.2554 -0.0090 -0.0270 -0.0113 325 PHE A CD2 
2613 C CE1 . PHE A 326 ? 0.2445 0.2326 0.2755 -0.0100 -0.0362 -0.0032 325 PHE A CE1 
2614 C CE2 . PHE A 326 ? 0.2115 0.2029 0.2351 -0.0109 -0.0281 -0.0075 325 PHE A CE2 
2615 C CZ  . PHE A 326 ? 0.1965 0.1872 0.2200 -0.0115 -0.0325 -0.0036 325 PHE A CZ  
2616 N N   . PRO A 327 ? 0.2401 0.2167 0.2940 -0.0063 -0.0365 -0.0101 326 PRO A N   
2617 C CA  . PRO A 327 ? 0.2244 0.1967 0.2861 -0.0056 -0.0418 -0.0071 326 PRO A CA  
2618 C C   . PRO A 327 ? 0.1988 0.1726 0.2613 -0.0051 -0.0459 -0.0036 326 PRO A C   
2619 O O   . PRO A 327 ? 0.1642 0.1412 0.2182 -0.0066 -0.0457 -0.0008 326 PRO A O   
2620 C CB  . PRO A 327 ? 0.2207 0.1900 0.2785 -0.0083 -0.0431 -0.0022 326 PRO A CB  
2621 C CG  . PRO A 327 ? 0.2406 0.2123 0.2911 -0.0097 -0.0381 -0.0048 326 PRO A CG  
2622 C CD  . PRO A 327 ? 0.2181 0.1948 0.2639 -0.0089 -0.0349 -0.0074 326 PRO A CD  
2623 N N   . VAL A 328 ? 0.1854 0.1570 0.2584 -0.0029 -0.0497 -0.0041 327 VAL A N   
2624 C CA  . VAL A 328 ? 0.1958 0.1684 0.2711 -0.0022 -0.0548 -0.0005 327 VAL A CA  
2625 C C   . VAL A 328 ? 0.2545 0.2215 0.3368 -0.0020 -0.0610 0.0048  327 VAL A C   
2626 O O   . VAL A 328 ? 0.2437 0.2078 0.3384 0.0006  -0.0632 0.0023  327 VAL A O   
2627 C CB  . VAL A 328 ? 0.2432 0.2191 0.3265 0.0006  -0.0541 -0.0059 327 VAL A CB  
2628 C CG1 . VAL A 328 ? 0.2445 0.2220 0.3297 0.0012  -0.0600 -0.0021 327 VAL A CG1 
2629 C CG2 . VAL A 328 ? 0.2302 0.2109 0.3073 0.0001  -0.0477 -0.0108 327 VAL A CG2 
2630 N N   . PRO A 329 ? 0.2751 0.2405 0.3499 -0.0047 -0.0639 0.0122  328 PRO A N   
2631 C CA  . PRO A 329 ? 0.2950 0.2548 0.3763 -0.0049 -0.0702 0.0185  328 PRO A CA  
2632 C C   . PRO A 329 ? 0.3171 0.2768 0.4074 -0.0022 -0.0762 0.0197  328 PRO A C   
2633 O O   . PRO A 329 ? 0.3084 0.2732 0.3952 -0.0017 -0.0767 0.0188  328 PRO A O   
2634 C CB  . PRO A 329 ? 0.3001 0.2603 0.3689 -0.0089 -0.0713 0.0264  328 PRO A CB  
2635 C CG  . PRO A 329 ? 0.2943 0.2587 0.3528 -0.0106 -0.0644 0.0227  328 PRO A CG  
2636 C CD  . PRO A 329 ? 0.2983 0.2670 0.3590 -0.0080 -0.0611 0.0151  328 PRO A CD  
2637 N N   . GLU A 330 ? 0.3577 0.3117 0.4607 -0.0005 -0.0809 0.0213  329 GLU A N   
2638 C CA  . GLU A 330 ? 0.4360 0.3895 0.5498 0.0024  -0.0873 0.0227  329 GLU A CA  
2639 C C   . GLU A 330 ? 0.4729 0.4275 0.5786 0.0003  -0.0935 0.0321  329 GLU A C   
2640 O O   . GLU A 330 ? 0.4587 0.4117 0.5539 -0.0032 -0.0941 0.0390  329 GLU A O   
2641 C CB  . GLU A 330 ? 0.5017 0.4483 0.6321 0.0048  -0.0910 0.0223  329 GLU A CB  
2642 C CG  . GLU A 330 ? 0.5970 0.5437 0.7379 0.0076  -0.0857 0.0117  329 GLU A CG  
2643 C CD  . GLU A 330 ? 0.7134 0.6582 0.8485 0.0055  -0.0797 0.0086  329 GLU A CD  
2644 O OE1 . GLU A 330 ? 0.7540 0.6980 0.8773 0.0019  -0.0791 0.0143  329 GLU A OE1 
2645 O OE2 . GLU A 330 ? 0.7212 0.6659 0.8637 0.0074  -0.0755 0.0002  329 GLU A OE2 
2646 N N   . LYS A 331 ? 0.5469 0.5046 0.6575 0.0024  -0.0981 0.0321  330 LYS A N   
2647 C CA  . LYS A 331 ? 0.6248 0.5846 0.7268 0.0006  -0.1044 0.0402  330 LYS A CA  
2648 C C   . LYS A 331 ? 0.6471 0.6010 0.7577 0.0012  -0.1134 0.0487  330 LYS A C   
2649 O O   . LYS A 331 ? 0.6440 0.5918 0.7689 0.0035  -0.1149 0.0476  330 LYS A O   
2650 C CB  . LYS A 331 ? 0.6770 0.6439 0.7795 0.0023  -0.1052 0.0358  330 LYS A CB  
2651 C CG  . LYS A 331 ? 0.7207 0.6911 0.8137 0.0004  -0.1117 0.0428  330 LYS A CG  
2652 C CD  . LYS A 331 ? 0.7433 0.7216 0.8319 0.0008  -0.1097 0.0369  330 LYS A CD  
2653 C CE  . LYS A 331 ? 0.7548 0.7347 0.8599 0.0050  -0.1089 0.0288  330 LYS A CE  
2654 N NZ  . LYS A 331 ? 0.7515 0.7388 0.8531 0.0049  -0.1058 0.0226  330 LYS A NZ  
# 
