data_8YSD
# 
_entry.id   8YSD 
# 
_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   8YSD         pdb_00008ysd 10.2210/pdb8ysd/pdb 
WWPDB D_1300046288 ?            ?                   
# 
_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                        8YSD 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-22 
_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 must be annotated as Met0' 
2 non-polymer nat "ADENOSINE-5'-TRIPHOSPHATE" 507.181   2   ? ? ? ?                                             
3 non-polymer syn 'MAGNESIUM ION'             24.305    2   ? ? ? ?                                             
4 water       nat water                       18.015    358 ? ? ? ?                                             
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        DwCdnB 
# 
_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 'MAGNESIUM ION'             MG  
4 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 
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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ATP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ATP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ATP 1   401 401 ATP ATP A . 
C 2 ATP 1   402 402 ATP ATP A . 
D 3 MG  1   403 501 MG  MG  A . 
E 3 MG  1   404 502 MG  MG  A . 
F 4 HOH 1   501 99  HOH HOH A . 
F 4 HOH 2   502 68  HOH HOH A . 
F 4 HOH 3   503 213 HOH HOH A . 
F 4 HOH 4   504 147 HOH HOH A . 
F 4 HOH 5   505 256 HOH HOH A . 
F 4 HOH 6   506 229 HOH HOH A . 
F 4 HOH 7   507 80  HOH HOH A . 
F 4 HOH 8   508 351 HOH HOH A . 
F 4 HOH 9   509 74  HOH HOH A . 
F 4 HOH 10  510 216 HOH HOH A . 
F 4 HOH 11  511 161 HOH HOH A . 
F 4 HOH 12  512 244 HOH HOH A . 
F 4 HOH 13  513 75  HOH HOH A . 
F 4 HOH 14  514 367 HOH HOH A . 
F 4 HOH 15  515 287 HOH HOH A . 
F 4 HOH 16  516 186 HOH HOH A . 
F 4 HOH 17  517 271 HOH HOH A . 
F 4 HOH 18  518 134 HOH HOH A . 
F 4 HOH 19  519 321 HOH HOH A . 
F 4 HOH 20  520 193 HOH HOH A . 
F 4 HOH 21  521 312 HOH HOH A . 
F 4 HOH 22  522 188 HOH HOH A . 
F 4 HOH 23  523 235 HOH HOH A . 
F 4 HOH 24  524 173 HOH HOH A . 
F 4 HOH 25  525 86  HOH HOH A . 
F 4 HOH 26  526 7   HOH HOH A . 
F 4 HOH 27  527 275 HOH HOH A . 
F 4 HOH 28  528 123 HOH HOH A . 
F 4 HOH 29  529 41  HOH HOH A . 
F 4 HOH 30  530 163 HOH HOH A . 
F 4 HOH 31  531 71  HOH HOH A . 
F 4 HOH 32  532 341 HOH HOH A . 
F 4 HOH 33  533 169 HOH HOH A . 
F 4 HOH 34  534 61  HOH HOH A . 
F 4 HOH 35  535 13  HOH HOH A . 
F 4 HOH 36  536 81  HOH HOH A . 
F 4 HOH 37  537 34  HOH HOH A . 
F 4 HOH 38  538 199 HOH HOH A . 
F 4 HOH 39  539 153 HOH HOH A . 
F 4 HOH 40  540 60  HOH HOH A . 
F 4 HOH 41  541 70  HOH HOH A . 
F 4 HOH 42  542 33  HOH HOH A . 
F 4 HOH 43  543 185 HOH HOH A . 
F 4 HOH 44  544 177 HOH HOH A . 
F 4 HOH 45  545 314 HOH HOH A . 
F 4 HOH 46  546 355 HOH HOH A . 
F 4 HOH 47  547 290 HOH HOH A . 
F 4 HOH 48  548 270 HOH HOH A . 
F 4 HOH 49  549 101 HOH HOH A . 
F 4 HOH 50  550 310 HOH HOH A . 
F 4 HOH 51  551 38  HOH HOH A . 
F 4 HOH 52  552 176 HOH HOH A . 
F 4 HOH 53  553 251 HOH HOH A . 
F 4 HOH 54  554 9   HOH HOH A . 
F 4 HOH 55  555 98  HOH HOH A . 
F 4 HOH 56  556 46  HOH HOH A . 
F 4 HOH 57  557 1   HOH HOH A . 
F 4 HOH 58  558 184 HOH HOH A . 
F 4 HOH 59  559 240 HOH HOH A . 
F 4 HOH 60  560 43  HOH HOH A . 
F 4 HOH 61  561 149 HOH HOH A . 
F 4 HOH 62  562 48  HOH HOH A . 
F 4 HOH 63  563 356 HOH HOH A . 
F 4 HOH 64  564 225 HOH HOH A . 
F 4 HOH 65  565 200 HOH HOH A . 
F 4 HOH 66  566 82  HOH HOH A . 
F 4 HOH 67  567 202 HOH HOH A . 
F 4 HOH 68  568 201 HOH HOH A . 
F 4 HOH 69  569 250 HOH HOH A . 
F 4 HOH 70  570 138 HOH HOH A . 
F 4 HOH 71  571 303 HOH HOH A . 
F 4 HOH 72  572 291 HOH HOH A . 
F 4 HOH 73  573 278 HOH HOH A . 
F 4 HOH 74  574 85  HOH HOH A . 
F 4 HOH 75  575 3   HOH HOH A . 
F 4 HOH 76  576 100 HOH HOH A . 
F 4 HOH 77  577 357 HOH HOH A . 
F 4 HOH 78  578 264 HOH HOH A . 
F 4 HOH 79  579 8   HOH HOH A . 
F 4 HOH 80  580 52  HOH HOH A . 
F 4 HOH 81  581 92  HOH HOH A . 
F 4 HOH 82  582 196 HOH HOH A . 
F 4 HOH 83  583 59  HOH HOH A . 
F 4 HOH 84  584 111 HOH HOH A . 
F 4 HOH 85  585 364 HOH HOH A . 
F 4 HOH 86  586 118 HOH HOH A . 
F 4 HOH 87  587 172 HOH HOH A . 
F 4 HOH 88  588 79  HOH HOH A . 
F 4 HOH 89  589 272 HOH HOH A . 
F 4 HOH 90  590 217 HOH HOH A . 
F 4 HOH 91  591 54  HOH HOH A . 
F 4 HOH 92  592 53  HOH HOH A . 
F 4 HOH 93  593 67  HOH HOH A . 
F 4 HOH 94  594 299 HOH HOH A . 
F 4 HOH 95  595 212 HOH HOH A . 
F 4 HOH 96  596 306 HOH HOH A . 
F 4 HOH 97  597 93  HOH HOH A . 
F 4 HOH 98  598 262 HOH HOH A . 
F 4 HOH 99  599 145 HOH HOH A . 
F 4 HOH 100 600 4   HOH HOH A . 
F 4 HOH 101 601 207 HOH HOH A . 
F 4 HOH 102 602 94  HOH HOH A . 
F 4 HOH 103 603 36  HOH HOH A . 
F 4 HOH 104 604 29  HOH HOH A . 
F 4 HOH 105 605 137 HOH HOH A . 
F 4 HOH 106 606 181 HOH HOH A . 
F 4 HOH 107 607 14  HOH HOH A . 
F 4 HOH 108 608 337 HOH HOH A . 
F 4 HOH 109 609 44  HOH HOH A . 
F 4 HOH 110 610 241 HOH HOH A . 
F 4 HOH 111 611 156 HOH HOH A . 
F 4 HOH 112 612 143 HOH HOH A . 
F 4 HOH 113 613 97  HOH HOH A . 
F 4 HOH 114 614 226 HOH HOH A . 
F 4 HOH 115 615 11  HOH HOH A . 
F 4 HOH 116 616 180 HOH HOH A . 
F 4 HOH 117 617 6   HOH HOH A . 
F 4 HOH 118 618 168 HOH HOH A . 
F 4 HOH 119 619 249 HOH HOH A . 
F 4 HOH 120 620 159 HOH HOH A . 
F 4 HOH 121 621 224 HOH HOH A . 
F 4 HOH 122 622 26  HOH HOH A . 
F 4 HOH 123 623 62  HOH HOH A . 
F 4 HOH 124 624 120 HOH HOH A . 
F 4 HOH 125 625 65  HOH HOH A . 
F 4 HOH 126 626 130 HOH HOH A . 
F 4 HOH 127 627 96  HOH HOH A . 
F 4 HOH 128 628 194 HOH HOH A . 
F 4 HOH 129 629 211 HOH HOH A . 
F 4 HOH 130 630 95  HOH HOH A . 
F 4 HOH 131 631 206 HOH HOH A . 
F 4 HOH 132 632 21  HOH HOH A . 
F 4 HOH 133 633 2   HOH HOH A . 
F 4 HOH 134 634 233 HOH HOH A . 
F 4 HOH 135 635 116 HOH HOH A . 
F 4 HOH 136 636 51  HOH HOH A . 
F 4 HOH 137 637 5   HOH HOH A . 
F 4 HOH 138 638 27  HOH HOH A . 
F 4 HOH 139 639 227 HOH HOH A . 
F 4 HOH 140 640 69  HOH HOH A . 
F 4 HOH 141 641 66  HOH HOH A . 
F 4 HOH 142 642 148 HOH HOH A . 
F 4 HOH 143 643 252 HOH HOH A . 
F 4 HOH 144 644 288 HOH HOH A . 
F 4 HOH 145 645 16  HOH HOH A . 
F 4 HOH 146 646 165 HOH HOH A . 
F 4 HOH 147 647 335 HOH HOH A . 
F 4 HOH 148 648 10  HOH HOH A . 
F 4 HOH 149 649 232 HOH HOH A . 
F 4 HOH 150 650 73  HOH HOH A . 
F 4 HOH 151 651 64  HOH HOH A . 
F 4 HOH 152 652 30  HOH HOH A . 
F 4 HOH 153 653 115 HOH HOH A . 
F 4 HOH 154 654 113 HOH HOH A . 
F 4 HOH 155 655 363 HOH HOH A . 
F 4 HOH 156 656 39  HOH HOH A . 
F 4 HOH 157 657 307 HOH HOH A . 
F 4 HOH 158 658 220 HOH HOH A . 
F 4 HOH 159 659 282 HOH HOH A . 
F 4 HOH 160 660 105 HOH HOH A . 
F 4 HOH 161 661 28  HOH HOH A . 
F 4 HOH 162 662 12  HOH HOH A . 
F 4 HOH 163 663 18  HOH HOH A . 
F 4 HOH 164 664 103 HOH HOH A . 
F 4 HOH 165 665 32  HOH HOH A . 
F 4 HOH 166 666 76  HOH HOH A . 
F 4 HOH 167 667 133 HOH HOH A . 
F 4 HOH 168 668 257 HOH HOH A . 
F 4 HOH 169 669 263 HOH HOH A . 
F 4 HOH 170 670 309 HOH HOH A . 
F 4 HOH 171 671 106 HOH HOH A . 
F 4 HOH 172 672 90  HOH HOH A . 
F 4 HOH 173 673 318 HOH HOH A . 
F 4 HOH 174 674 274 HOH HOH A . 
F 4 HOH 175 675 47  HOH HOH A . 
F 4 HOH 176 676 210 HOH HOH A . 
F 4 HOH 177 677 167 HOH HOH A . 
F 4 HOH 178 678 88  HOH HOH A . 
F 4 HOH 179 679 87  HOH HOH A . 
F 4 HOH 180 680 144 HOH HOH A . 
F 4 HOH 181 681 35  HOH HOH A . 
F 4 HOH 182 682 84  HOH HOH A . 
F 4 HOH 183 683 258 HOH HOH A . 
F 4 HOH 184 684 222 HOH HOH A . 
F 4 HOH 185 685 117 HOH HOH A . 
F 4 HOH 186 686 261 HOH HOH A . 
F 4 HOH 187 687 135 HOH HOH A . 
F 4 HOH 188 688 195 HOH HOH A . 
F 4 HOH 189 689 37  HOH HOH A . 
F 4 HOH 190 690 234 HOH HOH A . 
F 4 HOH 191 691 55  HOH HOH A . 
F 4 HOH 192 692 102 HOH HOH A . 
F 4 HOH 193 693 283 HOH HOH A . 
F 4 HOH 194 694 302 HOH HOH A . 
F 4 HOH 195 695 203 HOH HOH A . 
F 4 HOH 196 696 40  HOH HOH A . 
F 4 HOH 197 697 236 HOH HOH A . 
F 4 HOH 198 698 108 HOH HOH A . 
F 4 HOH 199 699 313 HOH HOH A . 
F 4 HOH 200 700 20  HOH HOH A . 
F 4 HOH 201 701 219 HOH HOH A . 
F 4 HOH 202 702 31  HOH HOH A . 
F 4 HOH 203 703 119 HOH HOH A . 
F 4 HOH 204 704 49  HOH HOH A . 
F 4 HOH 205 705 50  HOH HOH A . 
F 4 HOH 206 706 77  HOH HOH A . 
F 4 HOH 207 707 56  HOH HOH A . 
F 4 HOH 208 708 42  HOH HOH A . 
F 4 HOH 209 709 218 HOH HOH A . 
F 4 HOH 210 710 19  HOH HOH A . 
F 4 HOH 211 711 164 HOH HOH A . 
F 4 HOH 212 712 183 HOH HOH A . 
F 4 HOH 213 713 17  HOH HOH A . 
F 4 HOH 214 714 237 HOH HOH A . 
F 4 HOH 215 715 361 HOH HOH A . 
F 4 HOH 216 716 126 HOH HOH A . 
F 4 HOH 217 717 346 HOH HOH A . 
F 4 HOH 218 718 174 HOH HOH A . 
F 4 HOH 219 719 204 HOH HOH A . 
F 4 HOH 220 720 141 HOH HOH A . 
F 4 HOH 221 721 247 HOH HOH A . 
F 4 HOH 222 722 253 HOH HOH A . 
F 4 HOH 223 723 191 HOH HOH A . 
F 4 HOH 224 724 122 HOH HOH A . 
F 4 HOH 225 725 308 HOH HOH A . 
F 4 HOH 226 726 45  HOH HOH A . 
F 4 HOH 227 727 325 HOH HOH A . 
F 4 HOH 228 728 215 HOH HOH A . 
F 4 HOH 229 729 209 HOH HOH A . 
F 4 HOH 230 730 345 HOH HOH A . 
F 4 HOH 231 731 265 HOH HOH A . 
F 4 HOH 232 732 197 HOH HOH A . 
F 4 HOH 233 733 22  HOH HOH A . 
F 4 HOH 234 734 170 HOH HOH A . 
F 4 HOH 235 735 178 HOH HOH A . 
F 4 HOH 236 736 276 HOH HOH A . 
F 4 HOH 237 737 91  HOH HOH A . 
F 4 HOH 238 738 24  HOH HOH A . 
F 4 HOH 239 739 315 HOH HOH A . 
F 4 HOH 240 740 89  HOH HOH A . 
F 4 HOH 241 741 353 HOH HOH A . 
F 4 HOH 242 742 342 HOH HOH A . 
F 4 HOH 243 743 350 HOH HOH A . 
F 4 HOH 244 744 132 HOH HOH A . 
F 4 HOH 245 745 136 HOH HOH A . 
F 4 HOH 246 746 127 HOH HOH A . 
F 4 HOH 247 747 15  HOH HOH A . 
F 4 HOH 248 748 254 HOH HOH A . 
F 4 HOH 249 749 23  HOH HOH A . 
F 4 HOH 250 750 157 HOH HOH A . 
F 4 HOH 251 751 324 HOH HOH A . 
F 4 HOH 252 752 112 HOH HOH A . 
F 4 HOH 253 753 338 HOH HOH A . 
F 4 HOH 254 754 336 HOH HOH A . 
F 4 HOH 255 755 160 HOH HOH A . 
F 4 HOH 256 756 246 HOH HOH A . 
F 4 HOH 257 757 366 HOH HOH A . 
F 4 HOH 258 758 267 HOH HOH A . 
F 4 HOH 259 759 187 HOH HOH A . 
F 4 HOH 260 760 269 HOH HOH A . 
F 4 HOH 261 761 266 HOH HOH A . 
F 4 HOH 262 762 158 HOH HOH A . 
F 4 HOH 263 763 228 HOH HOH A . 
F 4 HOH 264 764 107 HOH HOH A . 
F 4 HOH 265 765 339 HOH HOH A . 
F 4 HOH 266 766 273 HOH HOH A . 
F 4 HOH 267 767 72  HOH HOH A . 
F 4 HOH 268 768 230 HOH HOH A . 
F 4 HOH 269 769 162 HOH HOH A . 
F 4 HOH 270 770 139 HOH HOH A . 
F 4 HOH 271 771 245 HOH HOH A . 
F 4 HOH 272 772 78  HOH HOH A . 
F 4 HOH 273 773 322 HOH HOH A . 
F 4 HOH 274 774 347 HOH HOH A . 
F 4 HOH 275 775 304 HOH HOH A . 
F 4 HOH 276 776 301 HOH HOH A . 
F 4 HOH 277 777 286 HOH HOH A . 
F 4 HOH 278 778 58  HOH HOH A . 
F 4 HOH 279 779 243 HOH HOH A . 
F 4 HOH 280 780 358 HOH HOH A . 
F 4 HOH 281 781 154 HOH HOH A . 
F 4 HOH 282 782 131 HOH HOH A . 
F 4 HOH 283 783 316 HOH HOH A . 
F 4 HOH 284 784 110 HOH HOH A . 
F 4 HOH 285 785 359 HOH HOH A . 
F 4 HOH 286 786 332 HOH HOH A . 
F 4 HOH 287 787 326 HOH HOH A . 
F 4 HOH 288 788 317 HOH HOH A . 
F 4 HOH 289 789 360 HOH HOH A . 
F 4 HOH 290 790 57  HOH HOH A . 
F 4 HOH 291 791 189 HOH HOH A . 
F 4 HOH 292 792 121 HOH HOH A . 
F 4 HOH 293 793 248 HOH HOH A . 
F 4 HOH 294 794 295 HOH HOH A . 
F 4 HOH 295 795 152 HOH HOH A . 
F 4 HOH 296 796 182 HOH HOH A . 
F 4 HOH 297 797 289 HOH HOH A . 
F 4 HOH 298 798 284 HOH HOH A . 
F 4 HOH 299 799 129 HOH HOH A . 
F 4 HOH 300 800 238 HOH HOH A . 
F 4 HOH 301 801 231 HOH HOH A . 
F 4 HOH 302 802 255 HOH HOH A . 
F 4 HOH 303 803 223 HOH HOH A . 
F 4 HOH 304 804 260 HOH HOH A . 
F 4 HOH 305 805 239 HOH HOH A . 
F 4 HOH 306 806 340 HOH HOH A . 
F 4 HOH 307 807 343 HOH HOH A . 
F 4 HOH 308 808 297 HOH HOH A . 
F 4 HOH 309 809 293 HOH HOH A . 
F 4 HOH 310 810 208 HOH HOH A . 
F 4 HOH 311 811 298 HOH HOH A . 
F 4 HOH 312 812 205 HOH HOH A . 
F 4 HOH 313 813 352 HOH HOH A . 
F 4 HOH 314 814 281 HOH HOH A . 
F 4 HOH 315 815 128 HOH HOH A . 
F 4 HOH 316 816 146 HOH HOH A . 
F 4 HOH 317 817 104 HOH HOH A . 
F 4 HOH 318 818 179 HOH HOH A . 
F 4 HOH 319 819 292 HOH HOH A . 
F 4 HOH 320 820 124 HOH HOH A . 
F 4 HOH 321 821 280 HOH HOH A . 
F 4 HOH 322 822 25  HOH HOH A . 
F 4 HOH 323 823 166 HOH HOH A . 
F 4 HOH 324 824 63  HOH HOH A . 
F 4 HOH 325 825 242 HOH HOH A . 
F 4 HOH 326 826 362 HOH HOH A . 
F 4 HOH 327 827 279 HOH HOH A . 
F 4 HOH 328 828 311 HOH HOH A . 
F 4 HOH 329 829 285 HOH HOH A . 
F 4 HOH 330 830 305 HOH HOH A . 
F 4 HOH 331 831 190 HOH HOH A . 
F 4 HOH 332 832 300 HOH HOH A . 
F 4 HOH 333 833 221 HOH HOH A . 
F 4 HOH 334 834 296 HOH HOH A . 
F 4 HOH 335 835 320 HOH HOH A . 
F 4 HOH 336 836 344 HOH HOH A . 
F 4 HOH 337 837 114 HOH HOH A . 
F 4 HOH 338 838 319 HOH HOH A . 
F 4 HOH 339 839 349 HOH HOH A . 
F 4 HOH 340 840 83  HOH HOH A . 
F 4 HOH 341 841 151 HOH HOH A . 
F 4 HOH 342 842 142 HOH HOH A . 
F 4 HOH 343 843 354 HOH HOH A . 
F 4 HOH 344 844 175 HOH HOH A . 
F 4 HOH 345 845 365 HOH HOH A . 
F 4 HOH 346 846 277 HOH HOH A . 
F 4 HOH 347 847 171 HOH HOH A . 
F 4 HOH 348 848 109 HOH HOH A . 
F 4 HOH 349 849 259 HOH HOH A . 
F 4 HOH 350 850 198 HOH HOH A . 
F 4 HOH 351 851 140 HOH HOH A . 
F 4 HOH 352 852 214 HOH HOH A . 
F 4 HOH 353 853 192 HOH HOH A . 
F 4 HOH 354 854 348 HOH HOH A . 
F 4 HOH 355 855 155 HOH HOH A . 
F 4 HOH 356 856 268 HOH HOH A . 
F 4 HOH 357 857 294 HOH HOH A . 
F 4 HOH 358 858 368 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                  99.96 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   105.81 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  99.54 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YSD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     35.387 
_cell.length_a_esd                 ? 
_cell.length_b                     46.809 
_cell.length_b_esd                 ? 
_cell.length_c                     59.976 
_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                         8YSD 
_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                   8YSD 
_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             2.34 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.44 
_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 Bis-Tris pH 6.5, 25 % w/v PEG 3350' 
_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   0.99984 
_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        0.99984 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'TPS 05A' 
_diffrn_source.pdbx_synchrotron_site       NSRRC 
# 
_reflns.B_iso_Wilson_estimate                          11.54 
_reflns.entry_id                                       8YSD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.61 
_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                                     44348 
_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                           96.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.146 
_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                              0.142 
_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                                    1.61 
_reflns_shell.d_res_low                                     1.67 
_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                             4353 
_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                               4.4 
_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                                  0.984 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          95.1 
_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                                 8YSD 
_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                            1.61 
_refine.ls_d_res_low                             28.08 
_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                     43824 
_refine.ls_number_reflns_R_free                  1980 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.13 
_refine.ls_percent_reflns_R_free                 4.52 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1890 
_refine.ls_R_factor_R_free                       0.2139 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1878 
_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               'FREE R-VALUE' 
_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.details                          ? 
_refine_hist.d_res_high                       1.61 
_refine_hist.d_res_low                        28.08 
_refine_hist.number_atoms_solvent             358 
_refine_hist.number_atoms_total               3076 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2654 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         64 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_struct.entry_id                     8YSD 
_struct.title                        
'Crystal structure of the Deinococcus wulumuqiensis CD-NTase DwCdnB in complex with ATP (form 2)' 
_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        8YSD 
_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 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
# 
_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              8YSD 
_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             8YSD 
_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       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 GLY A 62  ? ASN A 67  ? GLY A 61  ASN A 66  1 ? 6  
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 GLY A 154 ? ARG A 158 ? GLY A 153 ARG A 157 5 ? 5  
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 PRO A 207 ? PHE A 220 ? PRO A 206 PHE A 219 1 ? 14 
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 ? ALA A 305 ? THR A 283 ALA A 304 1 ? 22 
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 ? ? ? ? ? ? ? 2.033 ? ? 
metalc2  metalc ? ? A ASP 79  OD1 ? ? ? 1_555 E MG  . MG ? ? A ASP 78  A MG  404 1_555 ? ? ? ? ? ? ? 2.620 ? ? 
metalc3  metalc ? ? A ASP 79  OD2 ? ? ? 1_555 E MG  . MG ? ? A ASP 78  A MG  404 1_555 ? ? ? ? ? ? ? 2.259 ? ? 
metalc4  metalc ? ? A ASP 81  OD2 ? ? ? 1_555 D MG  . MG ? ? A ASP 80  A MG  403 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
metalc5  metalc ? ? A ASP 81  OD1 ? ? ? 1_555 E MG  . MG ? ? A ASP 80  A MG  404 1_555 ? ? ? ? ? ? ? 2.128 ? ? 
metalc6  metalc ? ? A ASP 130 OD2 ? ? ? 1_555 E MG  . MG ? ? A ASP 129 A MG  404 1_555 ? ? ? ? ? ? ? 2.148 ? ? 
metalc7  metalc ? ? B ATP .   O2G ? ? ? 1_555 D MG  . MG ? ? A ATP 401 A MG  403 1_555 ? ? ? ? ? ? ? 1.995 ? ? 
metalc8  metalc ? ? B ATP .   O2B ? ? ? 1_555 D MG  . MG ? ? A ATP 401 A MG  403 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc9  metalc ? ? B ATP .   O2A ? ? ? 1_555 D MG  . MG ? ? A ATP 401 A MG  403 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
metalc10 metalc ? ? B ATP .   O2A ? ? ? 1_555 E MG  . MG ? ? A ATP 401 A MG  404 1_555 ? ? ? ? ? ? ? 2.361 ? ? 
metalc11 metalc ? ? D MG  .   MG  ? ? ? 1_555 F HOH . O  ? ? A MG  403 A HOH 579 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc12 metalc ? ? E MG  .   MG  ? ? ? 1_555 F HOH . O  ? ? A MG  404 A HOH 601 1_555 ? ? ? ? ? ? ? 1.925 ? ? 
metalc13 metalc ? ? E MG  .   MG  ? ? ? 1_555 F HOH . O  ? ? A MG  404 A HOH 666 1_555 ? ? ? ? ? ? ? 2.081 ? ? 
# 
_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 89.9  ? 
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 98.7  ? 
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_555 170.9 ? 
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_555 170.2 ? 
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 86.4  ? 
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 84.6  ? 
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 82.7  ? 
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 86.6  ? 
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 91.4  ? 
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 88.1  ? 
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 92.8  ? 
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 84.3  ? 
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 98.2  ? 
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 95.8  ? 
15 O2A ? B ATP .   ? A ATP 401 ? 1_555 MG ? D MG . ? A MG 403 ? 1_555 O   ? F HOH .   ? A HOH 579 ? 1_555 169.9 ? 
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 52.8  ? 
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 99.6  ? 
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 85.8  ? 
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 61.3  ? 
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_555 113.5 ? 
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 97.5  ? 
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_555 123.8 ? 
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 73.0  ? 
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 89.2  ? 
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_555 170.9 ? 
26 OD1 ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O   ? F HOH .   ? A HOH 601 ? 1_555 145.6 ? 
27 OD2 ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O   ? F HOH .   ? A HOH 601 ? 1_555 161.5 ? 
28 OD1 ? A ASP 81  ? A ASP 80  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O   ? F HOH .   ? A HOH 601 ? 1_555 87.8  ? 
29 OD2 ? A ASP 130 ? A ASP 129 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O   ? F HOH .   ? A HOH 601 ? 1_555 84.5  ? 
30 O2A ? B ATP .   ? A ATP 401 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O   ? F HOH .   ? A HOH 601 ? 1_555 89.6  ? 
31 OD1 ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O   ? F HOH .   ? A HOH 666 ? 1_555 73.5  ? 
32 OD2 ? A ASP 79  ? A ASP 78  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O   ? F HOH .   ? A HOH 666 ? 1_555 85.1  ? 
33 OD1 ? A ASP 81  ? A ASP 80  ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O   ? F HOH .   ? A HOH 666 ? 1_555 170.8 ? 
34 OD2 ? A ASP 130 ? A ASP 129 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O   ? F HOH .   ? A HOH 666 ? 1_555 84.7  ? 
35 O2A ? B ATP .   ? A ATP 401 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O   ? F HOH .   ? A HOH 666 ? 1_555 89.7  ? 
36 O   ? F HOH .   ? A HOH 601 ? 1_555 MG ? E MG . ? A MG 404 ? 1_555 O   ? F HOH .   ? A HOH 666 ? 1_555 101.3 ? 
# 
_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       3.71 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
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 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? 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 ALA A 113 ? ARG A 116 ? ALA A 112 ARG A 115 
AA2 1 PHE A 56  ? ASN A 60  ? PHE A 55  ASN A 59  
AA2 2 TYR A 78  ? LEU A 86  ? TYR A 77  LEU A 85  
AA2 3 TYR A 127 ? ALA A 135 ? TYR A 126 ALA A 134 
AA2 4 CYS A 145 ? LYS A 148 ? CYS A 144 LYS A 147 
AA2 5 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 HIS A 253 ? ASP A 257 ? HIS A 252 ASP A 256 
AA4 2 ARG A 262 ? ARG A 266 ? ARG A 261 ARG A 265 
# 
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 VAL A 82  ? N VAL A 81  O ALA A 132 ? O ALA A 131 
AA1 3 4 O LEU A 131 ? O LEU A 130 N VAL A 120 ? N VAL A 119 
AA1 4 5 O THR A 121 ? O THR A 120 N GLU A 114 ? N GLU A 113 
AA2 1 2 N PHE A 59  ? N PHE A 58  O GLY A 83  ? O GLY A 82  
AA2 2 3 N VAL A 82  ? N VAL A 81  O ALA A 132 ? O ALA A 131 
AA2 3 4 N VAL A 133 ? N VAL A 132 O ALA A 147 ? O ALA A 146 
AA2 4 5 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                   8YSD 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 708 ? ? O  A HOH 781 ? ? 1.99 
2  1 O  A HOH 631 ? ? O  A HOH 832 ? ? 2.07 
3  1 O  A HOH 781 ? ? O  A HOH 816 ? ? 2.10 
4  1 O  A HOH 773 ? ? O  A HOH 783 ? ? 2.12 
5  1 O  A HOH 712 ? ? O  A HOH 779 ? ? 2.12 
6  1 O  A HOH 563 ? ? O  A HOH 785 ? ? 2.12 
7  1 O  A HOH 832 ? ? O  A HOH 854 ? ? 2.12 
8  1 O  A HOH 839 ? ? O  A HOH 854 ? ? 2.15 
9  1 OG A SER 117 ? ? NZ A LYS 147 ? ? 2.18 
10 1 O  A HOH 629 ? ? O  A HOH 734 ? ? 2.19 
11 1 O  A HOH 720 ? ? O  A HOH 798 ? ? 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     504 
_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     786 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_455 
_pdbx_validate_symm_contact.dist              2.09 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 170 ? ? CZ A ARG 170 ? ? NH2 A ARG 170 ? ? 116.96 120.30 -3.34 0.50 N 
2 1 NE A ARG 237 ? ? CZ A ARG 237 ? ? NH1 A ARG 237 ? ? 123.39 120.30 3.09  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU A 105 ? ? -103.44 41.97 
2 1 ASN A 110 ? ? -88.77  30.16 
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
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 
VAL N      N  N N 420 
VAL CA     C  N S 421 
VAL C      C  N N 422 
VAL O      O  N N 423 
VAL CB     C  N N 424 
VAL CG1    C  N N 425 
VAL CG2    C  N N 426 
VAL OXT    O  N N 427 
VAL H      H  N N 428 
VAL H2     H  N N 429 
VAL HA     H  N N 430 
VAL HB     H  N N 431 
VAL HG11   H  N N 432 
VAL HG12   H  N N 433 
VAL HG13   H  N N 434 
VAL HG21   H  N N 435 
VAL HG22   H  N N 436 
VAL HG23   H  N N 437 
VAL HXT    H  N N 438 
# 
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 
VAL N     CA     sing N N 407 
VAL N     H      sing N N 408 
VAL N     H2     sing N N 409 
VAL CA    C      sing N N 410 
VAL CA    CB     sing N N 411 
VAL CA    HA     sing N N 412 
VAL C     O      doub N N 413 
VAL C     OXT    sing N N 414 
VAL CB    CG1    sing N N 415 
VAL CB    CG2    sing N N 416 
VAL CB    HB     sing N N 417 
VAL CG1   HG11   sing N N 418 
VAL CG1   HG12   sing N N 419 
VAL CG1   HG13   sing N N 420 
VAL CG2   HG21   sing N N 421 
VAL CG2   HG22   sing N N 422 
VAL CG2   HG23   sing N N 423 
VAL OXT   HXT    sing N N 424 
# 
_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' 
# 
_space_group.name_H-M_alt     'P 1' 
_space_group.name_Hall        'P 1' 
_space_group.IT_number        1 
_space_group.crystal_system   triclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8YSD 
_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]   0.028259 
_atom_sites.fract_transf_matrix[1][2]   0.004749 
_atom_sites.fract_transf_matrix[1][3]   0.009344 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021663 
_atom_sites.fract_transf_matrix[2][3]   0.005117 
_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]   0.017806 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153 2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . MET A 1 1   ? 3.109   26.842  41.598  1.00 29.61 ?  0   MET A N     1 
ATOM   2    C  CA    . MET A 1 1   ? 2.516   25.748  40.807  1.00 31.75 ?  0   MET A CA    1 
ATOM   3    C  C     . MET A 1 1   ? 3.183   25.678  39.429  1.00 27.57 ?  0   MET A C     1 
ATOM   4    O  O     . MET A 1 1   ? 3.697   26.686  38.928  1.00 28.21 ?  0   MET A O     1 
ATOM   5    C  CB    . MET A 1 1   ? 0.990   25.918  40.672  1.00 33.12 ?  0   MET A CB    1 
ATOM   6    C  CG    . MET A 1 1   ? 0.521   26.466  39.334  1.00 34.52 ?  0   MET A CG    1 
ATOM   7    S  SD    . MET A 1 1   ? -1.261  26.764  39.186  1.00 35.75 ?  0   MET A SD    1 
ATOM   8    C  CE    . MET A 1 1   ? -1.251  27.716  37.658  1.00 36.72 ?  0   MET A CE    1 
ATOM   9    N  N     . MET A 1 2   ? 3.178   24.488  38.830  1.00 29.36 ?  1   MET A N     1 
ATOM   10   C  CA    . MET A 1 2   ? 3.815   24.305  37.530  1.00 30.17 ?  1   MET A CA    1 
ATOM   11   C  C     . MET A 1 2   ? 3.086   25.111  36.461  1.00 28.23 ?  1   MET A C     1 
ATOM   12   O  O     . MET A 1 2   ? 1.869   25.313  36.526  1.00 27.71 ?  1   MET A O     1 
ATOM   13   C  CB    . MET A 1 2   ? 3.850   22.816  37.162  1.00 31.78 ?  1   MET A CB    1 
ATOM   14   C  CG    . MET A 1 2   ? 4.738   21.982  38.093  1.00 34.79 ?  1   MET A CG    1 
ATOM   15   S  SD    . MET A 1 2   ? 6.361   22.756  38.325  1.00 39.15 ?  1   MET A SD    1 
ATOM   16   C  CE    . MET A 1 2   ? 7.208   21.501  39.293  1.00 37.58 ?  1   MET A CE    1 
ATOM   17   N  N     . ALA A 1 3   ? 3.853   25.618  35.493  1.00 25.66 ?  2   ALA A N     1 
ATOM   18   C  CA    . ALA A 1 3   ? 3.277   26.448  34.449  1.00 23.63 ?  2   ALA A CA    1 
ATOM   19   C  C     . ALA A 1 3   ? 2.319   25.619  33.603  1.00 23.56 ?  2   ALA A C     1 
ATOM   20   O  O     . ALA A 1 3   ? 2.682   24.515  33.154  1.00 21.71 ?  2   ALA A O     1 
ATOM   21   C  CB    . ALA A 1 3   ? 4.359   27.061  33.559  1.00 24.07 ?  2   ALA A CB    1 
ATOM   22   N  N     . PRO A 1 4   ? 1.087   26.075  33.405  1.00 21.53 ?  3   PRO A N     1 
ATOM   23   C  CA    . PRO A 1 4   ? 0.199   25.408  32.457  1.00 19.90 ?  3   PRO A CA    1 
ATOM   24   C  C     . PRO A 1 4   ? 0.587   25.763  31.031  1.00 19.19 ?  3   PRO A C     1 
ATOM   25   O  O     . PRO A 1 4   ? 1.259   26.760  30.768  1.00 20.13 ?  3   PRO A O     1 
ATOM   26   C  CB    . PRO A 1 4   ? -1.184  25.970  32.798  1.00 21.21 ?  3   PRO A CB    1 
ATOM   27   C  CG    . PRO A 1 4   ? -0.901  27.391  33.291  1.00 21.82 ?  3   PRO A CG    1 
ATOM   28   C  CD    . PRO A 1 4   ? 0.472   27.293  33.999  1.00 21.25 ?  3   PRO A CD    1 
ATOM   29   N  N     . VAL A 1 5   ? 0.109   24.947  30.081  1.00 15.46 ?  4   VAL A N     1 
ATOM   30   C  CA    . VAL A 1 5   ? 0.422   25.243  28.687  1.00 13.31 ?  4   VAL A CA    1 
ATOM   31   C  C     . VAL A 1 5   ? -0.829  25.296  27.807  1.00 12.52 ?  4   VAL A C     1 
ATOM   32   O  O     . VAL A 1 5   ? -0.720  25.296  26.568  1.00 11.09 ?  4   VAL A O     1 
ATOM   33   C  CB    . VAL A 1 5   ? 1.422   24.207  28.106  1.00 12.19 ?  4   VAL A CB    1 
ATOM   34   C  CG1   . VAL A 1 5   ? 2.861   24.401  28.720  1.00 15.82 ?  4   VAL A CG1   1 
ATOM   35   C  CG2   . VAL A 1 5   ? 0.944   22.831  28.340  1.00 10.69 ?  4   VAL A CG2   1 
ATOM   36   N  N     . GLN A 1 6   ? -2.023  25.357  28.404  1.00 10.01 ?  5   GLN A N     1 
ATOM   37   C  CA    . GLN A 1 6   ? -3.236  25.266  27.568  1.00 8.97  ?  5   GLN A CA    1 
ATOM   38   C  C     . GLN A 1 6   ? -3.373  26.454  26.612  1.00 9.36  ?  5   GLN A C     1 
ATOM   39   O  O     . GLN A 1 6   ? -3.726  26.278  25.432  1.00 10.39 ?  5   GLN A O     1 
ATOM   40   C  CB    . GLN A 1 6   ? -4.494  25.136  28.441  1.00 9.10  ?  5   GLN A CB    1 
ATOM   41   C  CG    . GLN A 1 6   ? -5.819  25.002  27.678  1.00 9.68  ?  5   GLN A CG    1 
ATOM   42   C  CD    . GLN A 1 6   ? -5.945  23.713  26.860  1.00 9.59  ?  5   GLN A CD    1 
ATOM   43   O  OE1   . GLN A 1 6   ? -5.130  22.792  26.988  1.00 9.67  ?  5   GLN A OE1   1 
ATOM   44   N  NE2   . GLN A 1 6   ? -6.997  23.633  26.043  1.00 10.47 ?  5   GLN A NE2   1 
ATOM   45   N  N     . LYS A 1 7   ? -3.112  27.673  27.090  1.00 11.65 ?  6   LYS A N     1 
ATOM   46   C  CA    . LYS A 1 7   ? -3.223  28.830  26.207  1.00 13.58 ?  6   LYS A CA    1 
ATOM   47   C  C     . LYS A 1 7   ? -2.265  28.700  25.033  1.00 11.18 ?  6   LYS A C     1 
ATOM   48   O  O     . LYS A 1 7   ? -2.597  29.080  23.894  1.00 11.38 ?  6   LYS A O     1 
ATOM   49   C  CB    . LYS A 1 7   ? -2.931  30.115  26.978  1.00 20.73 ?  6   LYS A CB    1 
ATOM   50   C  CG    . LYS A 1 7   ? -4.131  30.596  27.758  1.00 28.80 ?  6   LYS A CG    1 
ATOM   51   C  CD    . LYS A 1 7   ? -3.776  31.156  29.136  1.00 37.23 ?  6   LYS A CD    1 
ATOM   52   C  CE    . LYS A 1 7   ? -2.992  32.456  29.077  1.00 41.51 ?  6   LYS A CE    1 
ATOM   53   N  NZ    . LYS A 1 7   ? -2.775  32.994  30.471  1.00 43.98 1  6   LYS A NZ    1 
ATOM   54   N  N     . GLN A 1 8   ? -1.071  28.146  25.288  1.00 10.81 ?  7   GLN A N     1 
ATOM   55   C  CA    . GLN A 1 8   ? -0.115  28.008  24.194  1.00 12.46 ?  7   GLN A CA    1 
ATOM   56   C  C     . GLN A 1 8   ? -0.566  26.939  23.215  1.00 9.66  ?  7   GLN A C     1 
ATOM   57   O  O     . GLN A 1 8   ? -0.362  27.086  22.004  1.00 9.77  ?  7   GLN A O     1 
ATOM   58   C  CB    . GLN A 1 8   ? 1.277   27.679  24.746  1.00 14.51 ?  7   GLN A CB    1 
ATOM   59   C  CG    . GLN A 1 8   ? 2.027   29.001  25.108  1.00 17.53 ?  7   GLN A CG    1 
ATOM   60   C  CD    . GLN A 1 8   ? 1.414   29.675  26.255  1.00 19.66 ?  7   GLN A CD    1 
ATOM   61   O  OE1   . GLN A 1 8   ? 1.297   30.926  26.288  1.00 23.49 ?  7   GLN A OE1   1 
ATOM   62   N  NE2   . GLN A 1 8   ? 0.993   28.886  27.230  1.00 14.68 ?  7   GLN A NE2   1 
ATOM   63   N  N     . PHE A 1 9   ? -1.160  25.835  23.717  1.00 9.35  ?  8   PHE A N     1 
ATOM   64   C  CA    . PHE A 1 9   ? -1.688  24.844  22.785  1.00 7.23  ?  8   PHE A CA    1 
ATOM   65   C  C     . PHE A 1 9   ? -2.787  25.461  21.925  1.00 6.79  ?  8   PHE A C     1 
ATOM   66   O  O     . PHE A 1 9   ? -2.816  25.234  20.721  1.00 7.58  ?  8   PHE A O     1 
ATOM   67   C  CB    . PHE A 1 9   ? -2.201  23.585  23.516  1.00 7.53  ?  8   PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 9   ? -1.179  22.492  23.585  1.00 7.53  ?  8   PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 9   ? -0.870  21.741  22.453  1.00 9.14  ?  8   PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 9   ? -0.512  22.234  24.788  1.00 9.69  ?  8   PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 9   ? 0.084   20.705  22.531  1.00 8.01  ?  8   PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 9   ? 0.438   21.228  24.863  1.00 10.30 ?  8   PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 9   ? 0.750   20.496  23.745  1.00 8.14  ?  8   PHE A CZ    1 
ATOM   74   N  N     . ARG A 1 10  ? -3.688  26.262  22.525  1.00 7.91  ?  9   ARG A N     1 
ATOM   75   C  CA    . ARG A 1 10  ? -4.751  26.820  21.691  1.00 8.29  ?  9   ARG A CA    1 
ATOM   76   C  C     . ARG A 1 10  ? -4.215  27.840  20.684  1.00 6.43  ?  9   ARG A C     1 
ATOM   77   O  O     . ARG A 1 10  ? -4.685  27.903  19.547  1.00 8.04  ?  9   ARG A O     1 
ATOM   78   C  CB    . ARG A 1 10  ? -5.836  27.454  22.573  1.00 8.59  ?  9   ARG A CB    1 
ATOM   79   C  CG    . ARG A 1 10  ? -6.505  26.498  23.527  1.00 10.38 ?  9   ARG A CG    1 
ATOM   80   C  CD    . ARG A 1 10  ? -7.385  25.489  22.785  1.00 10.42 ?  9   ARG A CD    1 
ATOM   81   N  NE    . ARG A 1 10  ? -8.368  26.021  21.824  1.00 12.43 ?  9   ARG A NE    1 
ATOM   82   C  CZ    . ARG A 1 10  ? -9.661  26.218  22.112  1.00 14.25 ?  9   ARG A CZ    1 
ATOM   83   N  NH1   . ARG A 1 10  ? -10.124 25.951  23.326  1.00 13.88 1  9   ARG A NH1   1 
ATOM   84   N  NH2   . ARG A 1 10  ? -10.491 26.641  21.169  1.00 16.17 ?  9   ARG A NH2   1 
ATOM   85   N  N     . GLU A 1 11  ? -3.178  28.599  21.051  1.00 7.52  ?  10  GLU A N     1 
ATOM   86   C  CA    . GLU A 1 11  ? -2.521  29.463  20.073  1.00 8.34  ?  10  GLU A CA    1 
ATOM   87   C  C     . GLU A 1 11  ? -1.879  28.653  18.941  1.00 5.65  ?  10  GLU A C     1 
ATOM   88   O  O     . GLU A 1 11  ? -2.049  28.949  17.749  1.00 8.76  ?  10  GLU A O     1 
ATOM   89   C  CB    . GLU A 1 11  ? -1.499  30.330  20.791  1.00 9.25  ?  10  GLU A CB    1 
ATOM   90   C  CG    . GLU A 1 11  ? -0.669  31.230  19.887  1.00 10.68 ?  10  GLU A CG    1 
ATOM   91   C  CD    . GLU A 1 11  ? -1.473  32.202  18.992  1.00 14.11 ?  10  GLU A CD    1 
ATOM   92   O  OE1   . GLU A 1 11  ? -2.605  32.634  19.350  1.00 16.46 ?  10  GLU A OE1   1 
ATOM   93   O  OE2   . GLU A 1 11  ? -0.978  32.493  17.904  1.00 14.25 -1 10  GLU A OE2   1 
ATOM   94   N  N     . PHE A 1 12  ? -1.146  27.605  19.308  1.00 9.05  ?  11  PHE A N     1 
ATOM   95   C  CA    . PHE A 1 12  ? -0.576  26.698  18.323  1.00 8.51  ?  11  PHE A CA    1 
ATOM   96   C  C     . PHE A 1 12  ? -1.650  26.161  17.384  1.00 7.67  ?  11  PHE A C     1 
ATOM   97   O  O     . PHE A 1 12  ? -1.481  26.143  16.165  1.00 6.83  ?  11  PHE A O     1 
ATOM   98   C  CB    . PHE A 1 12  ? 0.125   25.566  19.075  1.00 7.70  ?  11  PHE A CB    1 
ATOM   99   C  CG    . PHE A 1 12  ? 0.786   24.538  18.185  1.00 6.28  ?  11  PHE A CG    1 
ATOM   100  C  CD1   . PHE A 1 12  ? 1.647   24.924  17.150  1.00 8.62  ?  11  PHE A CD1   1 
ATOM   101  C  CD2   . PHE A 1 12  ? 0.567   23.186  18.419  1.00 8.39  ?  11  PHE A CD2   1 
ATOM   102  C  CE1   . PHE A 1 12  ? 2.265   23.988  16.358  1.00 8.94  ?  11  PHE A CE1   1 
ATOM   103  C  CE2   . PHE A 1 12  ? 1.245   22.219  17.654  1.00 7.04  ?  11  PHE A CE2   1 
ATOM   104  C  CZ    . PHE A 1 12  ? 2.081   22.625  16.625  1.00 6.85  ?  11  PHE A CZ    1 
ATOM   105  N  N     . HIS A 1 13  ? -2.786  25.726  17.944  1.00 6.28  ?  12  HIS A N     1 
ATOM   106  C  CA    . HIS A 1 13  ? -3.848  25.229  17.085  1.00 7.41  ?  12  HIS A CA    1 
ATOM   107  C  C     . HIS A 1 13  ? -4.330  26.295  16.102  1.00 6.80  ?  12  HIS A C     1 
ATOM   108  O  O     . HIS A 1 13  ? -4.541  26.004  14.914  1.00 8.96  ?  12  HIS A O     1 
ATOM   109  C  CB    . HIS A 1 13  ? -5.026  24.702  17.925  1.00 7.11  ?  12  HIS A CB    1 
ATOM   110  C  CG    . HIS A 1 13  ? -6.123  24.161  17.073  1.00 8.18  ?  12  HIS A CG    1 
ATOM   111  N  ND1   . HIS A 1 13  ? -7.362  24.765  16.952  1.00 8.01  ?  12  HIS A ND1   1 
ATOM   112  C  CD2   . HIS A 1 13  ? -6.146  23.097  16.232  1.00 7.85  ?  12  HIS A CD2   1 
ATOM   113  C  CE1   . HIS A 1 13  ? -8.089  24.086  16.085  1.00 8.13  ?  12  HIS A CE1   1 
ATOM   114  N  NE2   . HIS A 1 13  ? -7.393  23.038  15.684  1.00 9.08  ?  12  HIS A NE2   1 
ATOM   115  N  N     . ASP A 1 14  ? -4.476  27.547  16.569  1.00 9.49  ?  13  ASP A N     1 
ATOM   116  C  CA    . ASP A 1 14  ? -4.899  28.630  15.687  1.00 10.43 ?  13  ASP A CA    1 
ATOM   117  C  C     . ASP A 1 14  ? -3.923  28.842  14.539  1.00 8.32  ?  13  ASP A C     1 
ATOM   118  O  O     . ASP A 1 14  ? -4.356  29.144  13.414  1.00 10.46 ?  13  ASP A O     1 
ATOM   119  C  CB    . ASP A 1 14  ? -5.065  29.922  16.495  1.00 11.82 ?  13  ASP A CB    1 
ATOM   120  C  CG    . ASP A 1 14  ? -6.306  29.890  17.390  1.00 16.73 ?  13  ASP A CG    1 
ATOM   121  O  OD1   . ASP A 1 14  ? -7.206  29.068  17.119  1.00 16.59 ?  13  ASP A OD1   1 
ATOM   122  O  OD2   . ASP A 1 14  ? -6.366  30.666  18.377  1.00 21.74 -1 13  ASP A OD2   1 
ATOM   123  N  N     . ARG A 1 15  ? -2.627  28.614  14.792  1.00 7.61  ?  14  ARG A N     1 
ATOM   124  C  CA    . ARG A 1 15  ? -1.599  28.771  13.756  1.00 7.62  ?  14  ARG A CA    1 
ATOM   125  C  C     . ARG A 1 15  ? -1.622  27.647  12.738  1.00 7.47  ?  14  ARG A C     1 
ATOM   126  O  O     . ARG A 1 15  ? -1.329  27.870  11.555  1.00 9.08  ?  14  ARG A O     1 
ATOM   127  C  CB    . ARG A 1 15  ? -0.218  28.873  14.395  1.00 7.38  ?  14  ARG A CB    1 
ATOM   128  C  CG    . ARG A 1 15  ? -0.158  30.017  15.427  1.00 8.30  ?  14  ARG A CG    1 
ATOM   129  C  CD    . ARG A 1 15  ? 1.201   30.026  16.095  1.00 7.84  ?  14  ARG A CD    1 
ATOM   130  N  NE    . ARG A 1 15  ? 1.337   31.178  16.992  1.00 7.83  ?  14  ARG A NE    1 
ATOM   131  C  CZ    . ARG A 1 15  ? 2.475   31.543  17.579  1.00 11.32 ?  14  ARG A CZ    1 
ATOM   132  N  NH1   . ARG A 1 15  ? 3.603   30.821  17.428  1.00 10.14 1  14  ARG A NH1   1 
ATOM   133  N  NH2   . ARG A 1 15  ? 2.496   32.628  18.339  1.00 14.25 ?  14  ARG A NH2   1 
ATOM   134  N  N     . ILE A 1 16  ? -1.907  26.406  13.180  1.00 6.38  ?  15  ILE A N     1 
ATOM   135  C  CA    . ILE A 1 16  ? -1.783  25.280  12.258  1.00 5.03  ?  15  ILE A CA    1 
ATOM   136  C  C     . ILE A 1 16  ? -3.083  24.888  11.549  1.00 6.03  ?  15  ILE A C     1 
ATOM   137  O  O     . ILE A 1 16  ? -3.022  24.197  10.524  1.00 6.51  ?  15  ILE A O     1 
ATOM   138  C  CB    . ILE A 1 16  ? -1.203  24.041  12.989  1.00 6.14  ?  15  ILE A CB    1 
ATOM   139  C  CG1   . ILE A 1 16  ? -2.218  23.474  13.987  1.00 5.90  ?  15  ILE A CG1   1 
ATOM   140  C  CG2   . ILE A 1 16  ? 0.071   24.409  13.740  1.00 5.01  ?  15  ILE A CG2   1 
ATOM   141  C  CD1   . ILE A 1 16  ? -1.692  22.165  14.600  1.00 7.54  ?  15  ILE A CD1   1 
ATOM   142  N  N     . LYS A 1 17  ? -4.250  25.308  12.033  1.00 5.70  ?  16  LYS A N     1 
ATOM   143  C  CA    . LYS A 1 17  ? -5.494  24.842  11.431  1.00 8.54  ?  16  LYS A CA    1 
ATOM   144  C  C     . LYS A 1 17  ? -5.682  25.399  10.032  1.00 8.45  ?  16  LYS A C     1 
ATOM   145  O  O     . LYS A 1 17  ? -5.353  26.556  9.753   1.00 10.38 ?  16  LYS A O     1 
ATOM   146  C  CB    . LYS A 1 17  ? -6.688  25.241  12.297  1.00 12.22 ?  16  LYS A CB    1 
ATOM   147  C  CG    . LYS A 1 17  ? -6.829  26.703  12.575  1.00 15.68 ?  16  LYS A CG    1 
ATOM   148  C  CD    . LYS A 1 17  ? -7.856  26.954  13.677  1.00 18.87 ?  16  LYS A CD    1 
ATOM   149  C  CE    . LYS A 1 17  ? -8.225  28.452  13.728  1.00 18.69 ?  16  LYS A CE    1 
ATOM   150  N  NZ    . LYS A 1 17  ? -9.117  28.733  14.899  1.00 21.99 1  16  LYS A NZ    1 
ATOM   151  N  N     . LEU A 1 18  ? -6.233  24.575  9.147   1.00 9.64  ?  17  LEU A N     1 
ATOM   152  C  CA    . LEU A 1 18  ? -6.637  24.997  7.809   1.00 11.84 ?  17  LEU A CA    1 
ATOM   153  C  C     . LEU A 1 18  ? -8.124  24.712  7.663   1.00 13.15 ?  17  LEU A C     1 
ATOM   154  O  O     . LEU A 1 18  ? -8.558  23.567  7.863   1.00 16.60 ?  17  LEU A O     1 
ATOM   155  C  CB    . LEU A 1 18  ? -5.862  24.258  6.712   1.00 14.88 ?  17  LEU A CB    1 
ATOM   156  C  CG    . LEU A 1 18  ? -6.278  24.703  5.331   1.00 15.77 ?  17  LEU A CG    1 
ATOM   157  C  CD1   . LEU A 1 18  ? -5.952  26.159  5.137   1.00 17.72 ?  17  LEU A CD1   1 
ATOM   158  C  CD2   . LEU A 1 18  ? -5.565  23.812  4.381   1.00 21.21 ?  17  LEU A CD2   1 
ATOM   159  N  N     . ALA A 1 19  ? -8.905  25.750  7.355   1.00 11.59 ?  18  ALA A N     1 
ATOM   160  C  CA    . ALA A 1 19  ? -10.356 25.592  7.385   1.00 12.04 ?  18  ALA A CA    1 
ATOM   161  C  C     . ALA A 1 19  ? -10.831 24.525  6.402   1.00 12.39 ?  18  ALA A C     1 
ATOM   162  O  O     . ALA A 1 19  ? -10.263 24.324  5.301   1.00 13.19 ?  18  ALA A O     1 
ATOM   163  C  CB    . ALA A 1 19  ? -11.042 26.931  7.080   1.00 14.68 ?  18  ALA A CB    1 
ATOM   164  N  N     . GLN A 1 20  ? -11.867 23.810  6.818   1.00 13.10 ?  19  GLN A N     1 
ATOM   165  C  CA    . GLN A 1 20  ? -12.441 22.732  6.021   1.00 13.94 ?  19  GLN A CA    1 
ATOM   166  C  C     . GLN A 1 20  ? -13.131 23.281  4.763   1.00 13.42 ?  19  GLN A C     1 
ATOM   167  O  O     . GLN A 1 20  ? -13.390 24.480  4.638   1.00 13.11 ?  19  GLN A O     1 
ATOM   168  C  CB    . GLN A 1 20  ? -13.467 21.975  6.853   1.00 12.57 ?  19  GLN A CB    1 
ATOM   169  C  CG    . GLN A 1 20  ? -14.633 22.893  7.241   1.00 12.72 ?  19  GLN A CG    1 
ATOM   170  C  CD    . GLN A 1 20  ? -15.672 22.193  8.067   1.00 13.94 ?  19  GLN A CD    1 
ATOM   171  O  OE1   . GLN A 1 20  ? -16.052 21.067  7.774   1.00 17.63 ?  19  GLN A OE1   1 
ATOM   172  N  NE2   . GLN A 1 20  ? -16.126 22.852  9.132   1.00 16.19 ?  19  GLN A NE2   1 
ATOM   173  N  N     . TYR A 1 21  ? -13.475 22.363  3.842   1.00 13.68 ?  20  TYR A N     1 
ATOM   174  C  CA    . TYR A 1 21  ? -14.095 22.781  2.572   1.00 12.30 ?  20  TYR A CA    1 
ATOM   175  C  C     . TYR A 1 21  ? -15.272 23.733  2.779   1.00 16.81 ?  20  TYR A C     1 
ATOM   176  O  O     . TYR A 1 21  ? -15.348 24.778  2.118   1.00 18.42 ?  20  TYR A O     1 
ATOM   177  C  CB    . TYR A 1 21  ? -14.583 21.568  1.795   1.00 11.08 ?  20  TYR A CB    1 
ATOM   178  C  CG    . TYR A 1 21  ? -13.547 20.707  1.135   1.00 11.95 ?  20  TYR A CG    1 
ATOM   179  C  CD1   . TYR A 1 21  ? -12.683 21.213  0.178   1.00 12.81 ?  20  TYR A CD1   1 
ATOM   180  C  CD2   . TYR A 1 21  ? -13.480 19.339  1.405   1.00 12.65 ?  20  TYR A CD2   1 
ATOM   181  C  CE1   . TYR A 1 21  ? -11.768 20.398  -0.477  1.00 14.29 ?  20  TYR A CE1   1 
ATOM   182  C  CE2   . TYR A 1 21  ? -12.543 18.527  0.787   1.00 13.78 ?  20  TYR A CE2   1 
ATOM   183  C  CZ    . TYR A 1 21  ? -11.695 19.060  -0.176  1.00 15.33 ?  20  TYR A CZ    1 
ATOM   184  O  OH    . TYR A 1 21  ? -10.791 18.239  -0.804  1.00 15.85 ?  20  TYR A OH    1 
ATOM   185  N  N     . ASP A 1 22  ? -16.199 23.387  3.689   1.00 19.14 ?  21  ASP A N     1 
ATOM   186  C  CA    . ASP A 1 22  ? -17.414 24.189  3.859   1.00 23.46 ?  21  ASP A CA    1 
ATOM   187  C  C     . ASP A 1 22  ? -17.114 25.612  4.309   1.00 23.60 ?  21  ASP A C     1 
ATOM   188  O  O     . ASP A 1 22  ? -17.975 26.486  4.156   1.00 25.28 ?  21  ASP A O     1 
ATOM   189  C  CB    . ASP A 1 22  ? -18.367 23.561  4.876   1.00 27.41 ?  21  ASP A CB    1 
ATOM   190  C  CG    . ASP A 1 22  ? -18.990 22.275  4.394   1.00 30.89 ?  21  ASP A CG    1 
ATOM   191  O  OD1   . ASP A 1 22  ? -18.982 22.008  3.175   1.00 32.93 ?  21  ASP A OD1   1 
ATOM   192  O  OD2   . ASP A 1 22  ? -19.499 21.526  5.261   1.00 33.97 -1 21  ASP A OD2   1 
ATOM   193  N  N     . GLU A 1 23  ? -15.912 25.866  4.839   1.00 20.26 ?  22  GLU A N     1 
ATOM   194  C  CA    . GLU A 1 23  ? -15.527 27.180  5.345   1.00 22.03 ?  22  GLU A CA    1 
ATOM   195  C  C     . GLU A 1 23  ? -14.348 27.777  4.594   1.00 19.88 ?  22  GLU A C     1 
ATOM   196  O  O     . GLU A 1 23  ? -13.729 28.734  5.085   1.00 21.55 ?  22  GLU A O     1 
ATOM   197  C  CB    . GLU A 1 23  ? -15.168 27.094  6.833   1.00 22.06 ?  22  GLU A CB    1 
ATOM   198  C  CG    . GLU A 1 23  ? -16.269 26.576  7.727   1.00 26.29 ?  22  GLU A CG    1 
ATOM   199  C  CD    . GLU A 1 23  ? -15.827 26.496  9.169   1.00 29.33 ?  22  GLU A CD    1 
ATOM   200  O  OE1   . GLU A 1 23  ? -15.798 27.553  9.824   1.00 32.68 ?  22  GLU A OE1   1 
ATOM   201  O  OE2   . GLU A 1 23  ? -15.484 25.393  9.658   1.00 31.11 -1 22  GLU A OE2   1 
ATOM   202  N  N     . ASN A 1 24  ? -13.981 27.215  3.452   1.00 18.36 ?  23  ASN A N     1 
ATOM   203  C  CA    . ASN A 1 24  ? -12.741 27.572  2.777   1.00 19.19 ?  23  ASN A CA    1 
ATOM   204  C  C     . ASN A 1 24  ? -13.058 27.687  1.286   1.00 21.39 ?  23  ASN A C     1 
ATOM   205  O  O     . ASN A 1 24  ? -13.056 26.701  0.547   1.00 21.04 ?  23  ASN A O     1 
ATOM   206  C  CB    . ASN A 1 24  ? -11.637 26.547  3.073   1.00 18.52 ?  23  ASN A CB    1 
ATOM   207  C  CG    . ASN A 1 24  ? -10.281 27.047  2.711   1.00 18.71 ?  23  ASN A CG    1 
ATOM   208  O  OD1   . ASN A 1 24  ? -10.142 27.831  1.783   1.00 21.74 ?  23  ASN A OD1   1 
ATOM   209  N  ND2   . ASN A 1 24  ? -9.261  26.613  3.447   1.00 16.71 ?  23  ASN A ND2   1 
ATOM   210  N  N     . GLN A 1 25  ? -13.321 28.915  0.840   1.00 23.16 ?  24  GLN A N     1 
ATOM   211  C  CA    . GLN A 1 25  ? -13.657 29.117  -0.567  1.00 25.09 ?  24  GLN A CA    1 
ATOM   212  C  C     . GLN A 1 25  ? -12.485 28.788  -1.480  1.00 22.60 ?  24  GLN A C     1 
ATOM   213  O  O     . GLN A 1 25  ? -12.671 28.248  -2.584  1.00 22.49 ?  24  GLN A O     1 
ATOM   214  C  CB    . GLN A 1 25  ? -14.110 30.555  -0.795  1.00 30.42 ?  24  GLN A CB    1 
ATOM   215  C  CG    . GLN A 1 25  ? -14.441 30.823  -2.246  1.00 35.29 ?  24  GLN A CG    1 
ATOM   216  C  CD    . GLN A 1 25  ? -15.894 31.096  -2.431  1.00 40.30 ?  24  GLN A CD    1 
ATOM   217  O  OE1   . GLN A 1 25  ? -16.365 32.206  -2.158  1.00 42.25 ?  24  GLN A OE1   1 
ATOM   218  N  NE2   . GLN A 1 25  ? -16.633 30.086  -2.885  1.00 42.12 ?  24  GLN A NE2   1 
ATOM   219  N  N     . THR A 1 26  ? -11.268 29.135  -1.067  1.00 22.74 ?  25  THR A N     1 
ATOM   220  C  CA    . THR A 1 26  ? -10.102 28.821  -1.884  1.00 23.08 ?  25  THR A CA    1 
ATOM   221  C  C     . THR A 1 26  ? -10.022 27.326  -2.184  1.00 22.86 ?  25  THR A C     1 
ATOM   222  O  O     . THR A 1 26  ? -9.822  26.915  -3.335  1.00 23.86 ?  25  THR A O     1 
ATOM   223  C  CB    . THR A 1 26  ? -8.848  29.298  -1.171  1.00 26.59 ?  25  THR A CB    1 
ATOM   224  O  OG1   . THR A 1 26  ? -8.926  30.715  -1.002  1.00 28.54 ?  25  THR A OG1   1 
ATOM   225  C  CG2   . THR A 1 26  ? -7.617  28.943  -1.953  1.00 26.56 ?  25  THR A CG2   1 
ATOM   226  N  N     . LEU A 1 27  ? -10.161 26.488  -1.153  1.00 22.02 ?  26  LEU A N     1 
ATOM   227  C  CA    . LEU A 1 27  ? -10.089 25.056  -1.404  1.00 18.79 ?  26  LEU A CA    1 
ATOM   228  C  C     . LEU A 1 27  ? -11.239 24.585  -2.283  1.00 18.90 ?  26  LEU A C     1 
ATOM   229  O  O     . LEU A 1 27  ? -11.047 23.716  -3.142  1.00 18.24 ?  26  LEU A O     1 
ATOM   230  C  CB    . LEU A 1 27  ? -10.088 24.273  -0.090  1.00 16.73 ?  26  LEU A CB    1 
ATOM   231  C  CG    . LEU A 1 27  ? -8.848  24.486  0.761   1.00 17.29 ?  26  LEU A CG    1 
ATOM   232  C  CD1   . LEU A 1 27  ? -9.029  23.598  2.011   1.00 14.97 ?  26  LEU A CD1   1 
ATOM   233  C  CD2   . LEU A 1 27  ? -7.576  24.090  0.070   1.00 17.91 ?  26  LEU A CD2   1 
ATOM   234  N  N     . ARG A 1 28  ? -12.447 25.097  -2.042  1.00 18.12 ?  27  ARG A N     1 
ATOM   235  C  CA    . ARG A 1 28  ? -13.575 24.695  -2.876  1.00 19.71 ?  27  ARG A CA    1 
ATOM   236  C  C     . ARG A 1 28  ? -13.319 25.049  -4.337  1.00 22.29 ?  27  ARG A C     1 
ATOM   237  O  O     . ARG A 1 28  ? -13.609 24.249  -5.233  1.00 24.04 ?  27  ARG A O     1 
ATOM   238  C  CB    . ARG A 1 28  ? -14.869 25.354  -2.402  1.00 21.29 ?  27  ARG A CB    1 
ATOM   239  C  CG    . ARG A 1 28  ? -15.385 24.909  -1.043  1.00 22.52 ?  27  ARG A CG    1 
ATOM   240  C  CD    . ARG A 1 28  ? -16.861 25.247  -0.864  1.00 23.07 ?  27  ARG A CD    1 
ATOM   241  N  NE    . ARG A 1 28  ? -17.123 26.684  -0.929  1.00 26.53 ?  27  ARG A NE    1 
ATOM   242  C  CZ    . ARG A 1 28  ? -17.016 27.528  0.101   1.00 27.94 ?  27  ARG A CZ    1 
ATOM   243  N  NH1   . ARG A 1 28  ? -16.637 27.094  1.295   1.00 26.15 1  27  ARG A NH1   1 
ATOM   244  N  NH2   . ARG A 1 28  ? -17.288 28.820  -0.065  1.00 28.48 ?  27  ARG A NH2   1 
ATOM   245  N  N     . ASP A 1 29  ? -12.756 26.239  -4.594  1.00 23.45 ?  28  ASP A N     1 
ATOM   246  C  CA    . ASP A 1 29  ? -12.510 26.658  -5.980  1.00 24.14 ?  28  ASP A CA    1 
ATOM   247  C  C     . ASP A 1 29  ? -11.411 25.829  -6.627  1.00 24.03 ?  28  ASP A C     1 
ATOM   248  O  O     . ASP A 1 29  ? -11.523 25.461  -7.801  1.00 23.27 ?  28  ASP A O     1 
ATOM   249  C  CB    . ASP A 1 29  ? -12.145 28.149  -6.051  1.00 26.59 ?  28  ASP A CB    1 
ATOM   250  C  CG    . ASP A 1 29  ? -13.292 29.065  -5.648  1.00 28.24 ?  28  ASP A CG    1 
ATOM   251  O  OD1   . ASP A 1 29  ? -14.457 28.633  -5.649  1.00 28.58 ?  28  ASP A OD1   1 
ATOM   252  O  OD2   . ASP A 1 29  ? -13.028 30.253  -5.340  1.00 30.47 -1 28  ASP A OD2   1 
ATOM   253  N  N     . GLU A 1 30  ? -10.341 25.503  -5.882  1.00 21.71 ?  29  GLU A N     1 
ATOM   254  C  CA    . GLU A 1 30  ? -9.289  24.657  -6.450  1.00 21.18 ?  29  GLU A CA    1 
ATOM   255  C  C     . GLU A 1 30  ? -9.810  23.241  -6.735  1.00 22.83 ?  29  GLU A C     1 
ATOM   256  O  O     . GLU A 1 30  ? -9.522  22.648  -7.794  1.00 22.77 ?  29  GLU A O     1 
ATOM   257  C  CB    . GLU A 1 30  ? -8.079  24.637  -5.500  1.00 22.56 ?  29  GLU A CB    1 
ATOM   258  C  CG    . GLU A 1 30  ? -7.467  26.015  -5.339  1.00 23.87 ?  29  GLU A CG    1 
ATOM   259  C  CD    . GLU A 1 30  ? -6.464  26.114  -4.218  1.00 26.85 ?  29  GLU A CD    1 
ATOM   260  O  OE1   . GLU A 1 30  ? -6.462  25.219  -3.341  1.00 25.65 ?  29  GLU A OE1   1 
ATOM   261  O  OE2   . GLU A 1 30  ? -5.691  27.098  -4.211  1.00 27.57 -1 29  GLU A OE2   1 
ATOM   262  N  N     . ARG A 1 31  ? -10.606 22.695  -5.806  1.00 21.43 ?  30  ARG A N     1 
ATOM   263  C  CA    . ARG A 1 31  ? -11.259 21.413  -6.032  1.00 21.06 ?  30  ARG A CA    1 
ATOM   264  C  C     . ARG A 1 31  ? -12.113 21.469  -7.298  1.00 22.89 ?  30  ARG A C     1 
ATOM   265  O  O     . ARG A 1 31  ? -11.946 20.656  -8.212  1.00 25.68 ?  30  ARG A O     1 
ATOM   266  C  CB    . ARG A 1 31  ? -12.117 21.045  -4.818  1.00 21.95 ?  30  ARG A CB    1 
ATOM   267  C  CG    . ARG A 1 31  ? -12.924 19.741  -4.946  1.00 19.56 ?  30  ARG A CG    1 
ATOM   268  C  CD    . ARG A 1 31  ? -14.162 19.775  -4.064  1.00 19.25 ?  30  ARG A CD    1 
ATOM   269  N  NE    . ARG A 1 31  ? -15.093 20.871  -4.377  1.00 21.05 ?  30  ARG A NE    1 
ATOM   270  C  CZ    . ARG A 1 31  ? -15.911 21.425  -3.487  1.00 21.12 ?  30  ARG A CZ    1 
ATOM   271  N  NH1   . ARG A 1 31  ? -15.898 20.987  -2.228  1.00 22.36 1  30  ARG A NH1   1 
ATOM   272  N  NH2   . ARG A 1 31  ? -16.722 22.421  -3.836  1.00 22.35 ?  30  ARG A NH2   1 
ATOM   273  N  N     . ASP A 1 32  ? -13.011 22.451  -7.373  1.00 24.11 ?  31  ASP A N     1 
ATOM   274  C  CA    . ASP A 1 32  ? -13.920 22.547  -8.505  1.00 23.46 ?  31  ASP A CA    1 
ATOM   275  C  C     . ASP A 1 32  ? -13.184 22.799  -9.807  1.00 24.12 ?  31  ASP A C     1 
ATOM   276  O  O     . ASP A 1 32  ? -13.641 22.345  -10.853 1.00 25.15 ?  31  ASP A O     1 
ATOM   277  C  CB    . ASP A 1 32  ? -14.948 23.643  -8.262  1.00 24.18 ?  31  ASP A CB    1 
ATOM   278  C  CG    . ASP A 1 32  ? -15.902 23.293  -7.153  1.00 24.92 ?  31  ASP A CG    1 
ATOM   279  O  OD1   . ASP A 1 32  ? -15.894 22.119  -6.717  1.00 26.98 ?  31  ASP A OD1   1 
ATOM   280  O  OD2   . ASP A 1 32  ? -16.661 24.177  -6.733  1.00 26.84 -1 31  ASP A OD2   1 
ATOM   281  N  N     . ALA A 1 33  ? -12.070 23.530  -9.780  1.00 23.32 ?  32  ALA A N     1 
ATOM   282  C  CA    . ALA A 1 33  ? -11.270 23.705  -10.991 1.00 24.84 ?  32  ALA A CA    1 
ATOM   283  C  C     . ALA A 1 33  ? -10.772 22.362  -11.507 1.00 27.81 ?  32  ALA A C     1 
ATOM   284  O  O     . ALA A 1 33  ? -10.853 22.077  -12.711 1.00 29.77 ?  32  ALA A O     1 
ATOM   285  C  CB    . ALA A 1 33  ? -10.098 24.658  -10.740 1.00 22.32 ?  32  ALA A CB    1 
ATOM   286  N  N     . VAL A 1 34  ? -10.276 21.504  -10.612 1.00 27.75 ?  33  VAL A N     1 
ATOM   287  C  CA    . VAL A 1 34  ? -9.851  20.182  -11.073 1.00 26.80 ?  33  VAL A CA    1 
ATOM   288  C  C     . VAL A 1 34  ? -11.046 19.384  -11.603 1.00 27.16 ?  33  VAL A C     1 
ATOM   289  O  O     . VAL A 1 34  ? -10.941 18.674  -12.619 1.00 28.40 ?  33  VAL A O     1 
ATOM   290  C  CB    . VAL A 1 34  ? -9.082  19.444  -9.962  1.00 29.66 ?  33  VAL A CB    1 
ATOM   291  C  CG1   . VAL A 1 34  ? -8.820  18.006  -10.343 1.00 28.87 ?  33  VAL A CG1   1 
ATOM   292  C  CG2   . VAL A 1 34  ? -7.765  20.143  -9.709  1.00 29.01 ?  33  VAL A CG2   1 
ATOM   293  N  N     . LEU A 1 35  ? -12.207 19.516  -10.957 1.00 25.74 ?  34  LEU A N     1 
ATOM   294  C  CA    . LEU A 1 35  ? -13.385 18.749  -11.388 1.00 24.40 ?  34  LEU A CA    1 
ATOM   295  C  C     . LEU A 1 35  ? -13.903 19.225  -12.755 1.00 26.33 ?  34  LEU A C     1 
ATOM   296  O  O     . LEU A 1 35  ? -14.282 18.410  -13.616 1.00 27.77 ?  34  LEU A O     1 
ATOM   297  C  CB    . LEU A 1 35  ? -14.486 18.841  -10.330 1.00 24.73 ?  34  LEU A CB    1 
ATOM   298  C  CG    . LEU A 1 35  ? -14.181 18.239  -8.935  1.00 22.71 ?  34  LEU A CG    1 
ATOM   299  C  CD1   . LEU A 1 35  ? -15.266 18.594  -7.940  1.00 23.26 ?  34  LEU A CD1   1 
ATOM   300  C  CD2   . LEU A 1 35  ? -13.983 16.700  -8.974  1.00 22.57 ?  34  LEU A CD2   1 
ATOM   301  N  N     . THR A 1 36  ? -13.934 20.539  -12.973 1.00 28.27 ?  35  THR A N     1 
ATOM   302  C  CA    . THR A 1 36  ? -14.334 21.053  -14.280 1.00 28.62 ?  35  THR A CA    1 
ATOM   303  C  C     . THR A 1 36  ? -13.342 20.630  -15.349 1.00 29.03 ?  35  THR A C     1 
ATOM   304  O  O     . THR A 1 36  ? -13.735 20.332  -16.494 1.00 30.09 ?  35  THR A O     1 
ATOM   305  C  CB    . THR A 1 36  ? -14.453 22.574  -14.260 1.00 30.95 ?  35  THR A CB    1 
ATOM   306  O  OG1   . THR A 1 36  ? -13.188 23.150  -13.918 1.00 36.01 ?  35  THR A OG1   1 
ATOM   307  C  CG2   . THR A 1 36  ? -15.504 23.022  -13.281 1.00 28.58 ?  35  THR A CG2   1 
ATOM   308  N  N     . ALA A 1 37  ? -12.049 20.615  -15.005 1.00 27.53 ?  36  ALA A N     1 
ATOM   309  C  CA    . ALA A 1 37  ? -11.063 20.183  -15.983 1.00 27.20 ?  36  ALA A CA    1 
ATOM   310  C  C     . ALA A 1 37  ? -11.302 18.737  -16.371 1.00 28.83 ?  36  ALA A C     1 
ATOM   311  O  O     . ALA A 1 37  ? -11.195 18.385  -17.553 1.00 28.98 ?  36  ALA A O     1 
ATOM   312  C  CB    . ALA A 1 37  ? -9.643  20.381  -15.455 1.00 25.99 ?  36  ALA A CB    1 
ATOM   313  N  N     . VAL A 1 38  ? -11.647 17.881  -15.403 1.00 28.44 ?  37  VAL A N     1 
ATOM   314  C  CA    . VAL A 1 38  ? -11.864 16.484  -15.782 1.00 30.79 ?  37  VAL A CA    1 
ATOM   315  C  C     . VAL A 1 38  ? -13.103 16.358  -16.673 1.00 31.46 ?  37  VAL A C     1 
ATOM   316  O  O     . VAL A 1 38  ? -13.098 15.589  -17.642 1.00 33.04 ?  37  VAL A O     1 
ATOM   317  C  CB    . VAL A 1 38  ? -11.934 15.535  -14.564 1.00 30.40 ?  37  VAL A CB    1 
ATOM   318  C  CG1   . VAL A 1 38  ? -10.701 15.623  -13.692 1.00 30.15 ?  37  VAL A CG1   1 
ATOM   319  C  CG2   . VAL A 1 38  ? -13.107 15.799  -13.729 1.00 31.22 ?  37  VAL A CG2   1 
ATOM   320  N  N     . ARG A 1 39  ? -14.161 17.140  -16.414 1.00 31.86 ?  38  ARG A N     1 
ATOM   321  C  CA    . ARG A 1 39  ? -15.329 17.054  -17.303 1.00 33.51 ?  38  ARG A CA    1 
ATOM   322  C  C     . ARG A 1 39  ? -14.979 17.450  -18.746 1.00 35.61 ?  38  ARG A C     1 
ATOM   323  O  O     . ARG A 1 39  ? -15.317 16.734  -19.706 1.00 34.25 ?  38  ARG A O     1 
ATOM   324  C  CB    . ARG A 1 39  ? -16.480 17.906  -16.769 1.00 34.22 ?  38  ARG A CB    1 
ATOM   325  C  CG    . ARG A 1 39  ? -16.999 17.381  -15.443 1.00 37.63 ?  38  ARG A CG    1 
ATOM   326  C  CD    . ARG A 1 39  ? -18.449 17.743  -15.193 1.00 40.13 ?  38  ARG A CD    1 
ATOM   327  N  NE    . ARG A 1 39  ? -18.980 16.984  -14.068 1.00 43.28 ?  38  ARG A NE    1 
ATOM   328  C  CZ    . ARG A 1 39  ? -18.933 17.393  -12.806 1.00 46.21 ?  38  ARG A CZ    1 
ATOM   329  N  NH1   . ARG A 1 39  ? -19.448 16.629  -11.845 1.00 46.91 1  38  ARG A NH1   1 
ATOM   330  N  NH2   . ARG A 1 39  ? -18.372 18.564  -12.503 1.00 46.59 ?  38  ARG A NH2   1 
ATOM   331  N  N     . GLU A 1 40  ? -14.285 18.578  -18.925 1.00 41.27 ?  39  GLU A N     1 
ATOM   332  C  CA    . GLU A 1 40  ? -13.912 18.983  -20.287 1.00 48.59 ?  39  GLU A CA    1 
ATOM   333  C  C     . GLU A 1 40  ? -12.954 17.980  -20.938 1.00 48.23 ?  39  GLU A C     1 
ATOM   334  O  O     . GLU A 1 40  ? -13.120 17.581  -22.113 1.00 51.15 ?  39  GLU A O     1 
ATOM   335  C  CB    . GLU A 1 40  ? -13.281 20.370  -20.263 1.00 57.24 ?  39  GLU A CB    1 
ATOM   336  C  CG    . GLU A 1 40  ? -14.171 21.457  -19.734 1.00 64.95 ?  39  GLU A CG    1 
ATOM   337  C  CD    . GLU A 1 40  ? -13.371 22.699  -19.390 1.00 72.92 ?  39  GLU A CD    1 
ATOM   338  O  OE1   . GLU A 1 40  ? -12.143 22.562  -19.167 1.00 77.53 ?  39  GLU A OE1   1 
ATOM   339  O  OE2   . GLU A 1 40  ? -13.958 23.806  -19.348 1.00 77.05 -1 39  GLU A OE2   1 
ATOM   340  N  N     . GLY A 1 41  ? -11.925 17.580  -20.196 1.00 46.99 ?  40  GLY A N     1 
ATOM   341  C  CA    . GLY A 1 41  ? -10.961 16.641  -20.724 1.00 45.73 ?  40  GLY A CA    1 
ATOM   342  C  C     . GLY A 1 41  ? -11.585 15.321  -21.106 1.00 44.10 ?  40  GLY A C     1 
ATOM   343  O  O     . GLY A 1 41  ? -11.155 14.689  -22.067 1.00 44.27 ?  40  GLY A O     1 
ATOM   344  N  N     . LEU A 1 42  ? -12.618 14.893  -20.376 1.00 40.98 ?  41  LEU A N     1 
ATOM   345  C  CA    . LEU A 1 42  ? -13.296 13.656  -20.736 1.00 38.18 ?  41  LEU A CA    1 
ATOM   346  C  C     . LEU A 1 42  ? -14.090 13.826  -22.019 1.00 38.17 ?  41  LEU A C     1 
ATOM   347  O  O     . LEU A 1 42  ? -14.186 12.886  -22.821 1.00 34.78 ?  41  LEU A O     1 
ATOM   348  C  CB    . LEU A 1 42  ? -14.210 13.204  -19.603 1.00 37.03 ?  41  LEU A CB    1 
ATOM   349  C  CG    . LEU A 1 42  ? -13.583 12.489  -18.413 1.00 37.03 ?  41  LEU A CG    1 
ATOM   350  C  CD1   . LEU A 1 42  ? -14.654 12.237  -17.351 1.00 36.85 ?  41  LEU A CD1   1 
ATOM   351  C  CD2   . LEU A 1 42  ? -12.961 11.186  -18.844 1.00 36.27 ?  41  LEU A CD2   1 
ATOM   352  N  N     . LYS A 1 43  ? -14.700 15.001  -22.219 1.00 39.19 ?  42  LYS A N     1 
ATOM   353  C  CA    . LYS A 1 43  ? -15.320 15.248  -23.519 1.00 42.27 ?  42  LYS A CA    1 
ATOM   354  C  C     . LYS A 1 43  ? -14.335 14.930  -24.630 1.00 47.79 ?  42  LYS A C     1 
ATOM   355  O  O     . LYS A 1 43  ? -14.636 14.163  -25.562 1.00 47.96 ?  42  LYS A O     1 
ATOM   356  C  CB    . LYS A 1 43  ? -15.806 16.694  -23.637 1.00 39.94 ?  42  LYS A CB    1 
ATOM   357  C  CG    . LYS A 1 43  ? -17.200 16.884  -23.105 1.00 39.13 ?  42  LYS A CG    1 
ATOM   358  C  CD    . LYS A 1 43  ? -17.709 18.290  -23.335 1.00 39.37 ?  42  LYS A CD    1 
ATOM   359  C  CE    . LYS A 1 43  ? -17.061 19.274  -22.392 1.00 38.49 ?  42  LYS A CE    1 
ATOM   360  N  NZ    . LYS A 1 43  ? -17.940 20.466  -22.177 1.00 38.92 1  42  LYS A NZ    1 
ATOM   361  N  N     . LYS A 1 44  ? -13.119 15.472  -24.508 1.00 55.28 ?  43  LYS A N     1 
ATOM   362  C  CA    . LYS A 1 44  ? -12.154 15.252  -25.586 1.00 56.73 ?  43  LYS A CA    1 
ATOM   363  C  C     . LYS A 1 44  ? -11.666 13.798  -25.624 1.00 53.74 ?  43  LYS A C     1 
ATOM   364  O  O     . LYS A 1 44  ? -11.505 13.223  -26.708 1.00 53.70 ?  43  LYS A O     1 
ATOM   365  C  CB    . LYS A 1 44  ? -10.991 16.243  -25.480 1.00 63.92 ?  43  LYS A CB    1 
ATOM   366  C  CG    . LYS A 1 44  ? -9.864  15.880  -24.527 1.00 67.80 ?  43  LYS A CG    1 
ATOM   367  C  CD    . LYS A 1 44  ? -8.843  17.013  -24.421 1.00 71.26 ?  43  LYS A CD    1 
ATOM   368  C  CE    . LYS A 1 44  ? -9.516  18.378  -24.216 1.00 72.76 ?  43  LYS A CE    1 
ATOM   369  N  NZ    . LYS A 1 44  ? -9.669  19.155  -25.483 1.00 73.29 1  43  LYS A NZ    1 
ATOM   370  N  N     . VAL A 1 45  ? -11.459 13.173  -24.463 1.00 49.23 ?  44  VAL A N     1 
ATOM   371  C  CA    . VAL A 1 45  ? -10.921 11.815  -24.446 1.00 44.44 ?  44  VAL A CA    1 
ATOM   372  C  C     . VAL A 1 45  ? -11.885 10.851  -25.117 1.00 43.88 ?  44  VAL A C     1 
ATOM   373  O  O     . VAL A 1 45  ? -11.470 9.961   -25.867 1.00 42.68 ?  44  VAL A O     1 
ATOM   374  C  CB    . VAL A 1 45  ? -10.599 11.372  -23.004 1.00 40.91 ?  44  VAL A CB    1 
ATOM   375  C  CG1   . VAL A 1 45  ? -10.353 9.873   -22.938 1.00 38.99 ?  44  VAL A CG1   1 
ATOM   376  C  CG2   . VAL A 1 45  ? -9.395  12.135  -22.459 1.00 39.63 ?  44  VAL A CG2   1 
ATOM   377  N  N     . PHE A 1 46  ? -13.188 11.021  -24.882 1.00 43.71 ?  45  PHE A N     1 
ATOM   378  C  CA    . PHE A 1 46  ? -14.128 10.010  -25.343 1.00 44.24 ?  45  PHE A CA    1 
ATOM   379  C  C     . PHE A 1 46  ? -14.722 10.299  -26.712 1.00 47.52 ?  45  PHE A C     1 
ATOM   380  O  O     . PHE A 1 46  ? -15.150 9.352   -27.385 1.00 46.90 ?  45  PHE A O     1 
ATOM   381  C  CB    . PHE A 1 46  ? -15.244 9.810   -24.316 1.00 40.87 ?  45  PHE A CB    1 
ATOM   382  C  CG    . PHE A 1 46  ? -14.913 8.767   -23.289 1.00 38.62 ?  45  PHE A CG    1 
ATOM   383  C  CD1   . PHE A 1 46  ? -13.961 9.018   -22.311 1.00 37.56 ?  45  PHE A CD1   1 
ATOM   384  C  CD2   . PHE A 1 46  ? -15.533 7.532   -23.313 1.00 37.78 ?  45  PHE A CD2   1 
ATOM   385  C  CE1   . PHE A 1 46  ? -13.645 8.057   -21.378 1.00 36.04 ?  45  PHE A CE1   1 
ATOM   386  C  CE2   . PHE A 1 46  ? -15.223 6.571   -22.382 1.00 35.91 ?  45  PHE A CE2   1 
ATOM   387  C  CZ    . PHE A 1 46  ? -14.277 6.835   -21.407 1.00 36.80 ?  45  PHE A CZ    1 
ATOM   388  N  N     . ALA A 1 47  ? -14.746 11.562  -27.162 1.00 51.55 ?  46  ALA A N     1 
ATOM   389  C  CA    . ALA A 1 47  ? -15.009 11.783  -28.582 1.00 56.98 ?  46  ALA A CA    1 
ATOM   390  C  C     . ALA A 1 47  ? -13.993 11.042  -29.447 1.00 62.40 ?  46  ALA A C     1 
ATOM   391  O  O     . ALA A 1 47  ? -14.294 10.669  -30.590 1.00 62.37 ?  46  ALA A O     1 
ATOM   392  C  CB    . ALA A 1 47  ? -14.996 13.278  -28.901 1.00 57.34 ?  46  ALA A CB    1 
ATOM   393  N  N     . ASP A 1 48  ? -12.798 10.800  -28.905 1.00 67.60 ?  47  ASP A N     1 
ATOM   394  C  CA    . ASP A 1 48  ? -11.707 10.115  -29.580 1.00 72.51 ?  47  ASP A CA    1 
ATOM   395  C  C     . ASP A 1 48  ? -11.846 8.597   -29.575 1.00 71.76 ?  47  ASP A C     1 
ATOM   396  O  O     . ASP A 1 48  ? -11.055 7.916   -30.239 1.00 72.77 ?  47  ASP A O     1 
ATOM   397  C  CB    . ASP A 1 48  ? -10.389 10.499  -28.917 1.00 78.32 ?  47  ASP A CB    1 
ATOM   398  C  CG    . ASP A 1 48  ? -9.383  11.014  -29.899 1.00 83.08 ?  47  ASP A CG    1 
ATOM   399  O  OD1   . ASP A 1 48  ? -9.669  10.967  -31.117 1.00 84.72 ?  47  ASP A OD1   1 
ATOM   400  O  OD2   . ASP A 1 48  ? -8.308  11.467  -29.451 1.00 84.70 -1 47  ASP A OD2   1 
ATOM   401  N  N     . ARG A 1 49  ? -12.809 8.050   -28.840 1.00 68.79 ?  48  ARG A N     1 
ATOM   402  C  CA    . ARG A 1 49  ? -13.030 6.615   -28.808 1.00 64.54 ?  48  ARG A CA    1 
ATOM   403  C  C     . ARG A 1 49  ? -14.357 6.210   -29.431 1.00 57.47 ?  48  ARG A C     1 
ATOM   404  O  O     . ARG A 1 49  ? -14.689 5.019   -29.425 1.00 56.06 ?  48  ARG A O     1 
ATOM   405  C  CB    . ARG A 1 49  ? -12.961 6.106   -27.361 1.00 66.99 ?  48  ARG A CB    1 
ATOM   406  C  CG    . ARG A 1 49  ? -11.683 6.489   -26.636 1.00 68.69 ?  48  ARG A CG    1 
ATOM   407  C  CD    . ARG A 1 49  ? -11.871 6.474   -25.120 1.00 69.61 ?  48  ARG A CD    1 
ATOM   408  N  NE    . ARG A 1 49  ? -11.719 5.145   -24.521 1.00 69.58 ?  48  ARG A NE    1 
ATOM   409  C  CZ    . ARG A 1 49  ? -10.579 4.676   -24.011 1.00 68.88 ?  48  ARG A CZ    1 
ATOM   410  N  NH1   . ARG A 1 49  ? -9.473  5.418   -24.026 1.00 68.41 1  48  ARG A NH1   1 
ATOM   411  N  NH2   . ARG A 1 49  ? -10.546 3.460   -23.484 1.00 68.56 ?  48  ARG A NH2   1 
ATOM   412  N  N     . GLY A 1 50  ? -15.122 7.160   -29.967 1.00 51.54 ?  49  GLY A N     1 
ATOM   413  C  CA    . GLY A 1 50  ? -16.436 6.863   -30.505 1.00 46.58 ?  49  GLY A CA    1 
ATOM   414  C  C     . GLY A 1 50  ? -17.494 6.579   -29.465 1.00 43.06 ?  49  GLY A C     1 
ATOM   415  O  O     . GLY A 1 50  ? -18.560 6.049   -29.806 1.00 41.35 ?  49  GLY A O     1 
ATOM   416  N  N     . GLU A 1 51  ? -17.236 6.921   -28.197 1.00 40.16 ?  50  GLU A N     1 
ATOM   417  C  CA    . GLU A 1 51  ? -18.139 6.610   -27.100 1.00 40.24 ?  50  GLU A CA    1 
ATOM   418  C  C     . GLU A 1 51  ? -18.576 7.892   -26.398 1.00 33.58 ?  50  GLU A C     1 
ATOM   419  O  O     . GLU A 1 51  ? -17.844 8.882   -26.378 1.00 28.45 ?  50  GLU A O     1 
ATOM   420  C  CB    . GLU A 1 51  ? -17.465 5.665   -26.090 1.00 45.42 ?  50  GLU A CB    1 
ATOM   421  C  CG    . GLU A 1 51  ? -16.717 4.508   -26.735 1.00 51.11 ?  50  GLU A CG    1 
ATOM   422  C  CD    . GLU A 1 51  ? -15.907 3.705   -25.735 1.00 55.52 ?  50  GLU A CD    1 
ATOM   423  O  OE1   . GLU A 1 51  ? -16.284 2.548   -25.461 1.00 57.38 ?  50  GLU A OE1   1 
ATOM   424  O  OE2   . GLU A 1 51  ? -14.897 4.230   -25.220 1.00 57.22 -1 50  GLU A OE2   1 
ATOM   425  N  N     . ALA A 1 52  ? -19.774 7.862   -25.815 1.00 32.43 ?  51  ALA A N     1 
ATOM   426  C  CA    . ALA A 1 52  ? -20.206 8.955   -24.965 1.00 32.11 ?  51  ALA A CA    1 
ATOM   427  C  C     . ALA A 1 52  ? -19.317 9.033   -23.726 1.00 33.29 ?  51  ALA A C     1 
ATOM   428  O  O     . ALA A 1 52  ? -18.939 8.010   -23.140 1.00 31.31 ?  51  ALA A O     1 
ATOM   429  C  CB    . ALA A 1 52  ? -21.667 8.770   -24.552 1.00 34.40 ?  51  ALA A CB    1 
ATOM   430  N  N     . ALA A 1 53  ? -18.962 10.255  -23.343 1.00 31.65 ?  52  ALA A N     1 
ATOM   431  C  CA    . ALA A 1 53  ? -18.155 10.430  -22.149 1.00 33.57 ?  52  ALA A CA    1 
ATOM   432  C  C     . ALA A 1 53  ? -18.941 9.954   -20.929 1.00 32.80 ?  52  ALA A C     1 
ATOM   433  O  O     . ALA A 1 53  ? -20.161 10.161  -20.859 1.00 29.44 ?  52  ALA A O     1 
ATOM   434  C  CB    . ALA A 1 53  ? -17.754 11.895  -21.972 1.00 32.10 ?  52  ALA A CB    1 
ATOM   435  N  N     . PRO A 1 54  ? -18.285 9.311   -19.962 1.00 34.61 ?  53  PRO A N     1 
ATOM   436  C  CA    . PRO A 1 54  ? -18.967 8.981   -18.705 1.00 36.53 ?  53  PRO A CA    1 
ATOM   437  C  C     . PRO A 1 54  ? -19.176 10.216  -17.843 1.00 35.66 ?  53  PRO A C     1 
ATOM   438  O  O     . PRO A 1 54  ? -18.425 11.196  -17.907 1.00 37.26 ?  53  PRO A O     1 
ATOM   439  C  CB    . PRO A 1 54  ? -18.008 7.998   -18.030 1.00 36.44 ?  53  PRO A CB    1 
ATOM   440  C  CG    . PRO A 1 54  ? -16.651 8.419   -18.541 1.00 36.50 ?  53  PRO A CG    1 
ATOM   441  C  CD    . PRO A 1 54  ? -16.857 8.940   -19.939 1.00 35.46 ?  53  PRO A CD    1 
ATOM   442  N  N     . THR A 1 55  ? -20.233 10.174  -17.053 1.00 34.74 ?  54  THR A N     1 
ATOM   443  C  CA    . THR A 1 55  ? -20.501 11.212  -16.075 1.00 33.65 ?  54  THR A CA    1 
ATOM   444  C  C     . THR A 1 55  ? -19.993 10.744  -14.720 1.00 29.93 ?  54  THR A C     1 
ATOM   445  O  O     . THR A 1 55  ? -19.751 9.558   -14.500 1.00 28.15 ?  54  THR A O     1 
ATOM   446  C  CB    . THR A 1 55  ? -21.991 11.522  -15.996 1.00 35.83 ?  54  THR A CB    1 
ATOM   447  O  OG1   . THR A 1 55  ? -22.710 10.291  -15.903 1.00 37.17 ?  54  THR A OG1   1 
ATOM   448  C  CG2   . THR A 1 55  ? -22.453 12.302  -17.224 1.00 37.41 ?  54  THR A CG2   1 
ATOM   449  N  N     . PHE A 1 56  ? -19.799 11.701  -13.823 1.00 27.61 ?  55  PHE A N     1 
ATOM   450  C  CA    . PHE A 1 56  ? -19.388 11.360  -12.477 1.00 26.13 ?  55  PHE A CA    1 
ATOM   451  C  C     . PHE A 1 56  ? -20.066 12.307  -11.504 1.00 25.48 ?  55  PHE A C     1 
ATOM   452  O  O     . PHE A 1 56  ? -20.429 13.439  -11.854 1.00 23.67 ?  55  PHE A O     1 
ATOM   453  C  CB    . PHE A 1 56  ? -17.863 11.407  -12.319 1.00 24.16 ?  55  PHE A CB    1 
ATOM   454  C  CG    . PHE A 1 56  ? -17.272 12.770  -12.456 1.00 25.85 ?  55  PHE A CG    1 
ATOM   455  C  CD1   . PHE A 1 56  ? -17.167 13.599  -11.357 1.00 25.83 ?  55  PHE A CD1   1 
ATOM   456  C  CD2   . PHE A 1 56  ? -16.775 13.213  -13.668 1.00 26.28 ?  55  PHE A CD2   1 
ATOM   457  C  CE1   . PHE A 1 56  ? -16.620 14.852  -11.470 1.00 25.94 ?  55  PHE A CE1   1 
ATOM   458  C  CE2   . PHE A 1 56  ? -16.229 14.470  -13.788 1.00 27.18 ?  55  PHE A CE2   1 
ATOM   459  C  CZ    . PHE A 1 56  ? -16.141 15.289  -12.690 1.00 26.72 ?  55  PHE A CZ    1 
ATOM   460  N  N     . THR A 1 57  ? -20.234 11.811  -10.278 1.00 25.70 ?  56  THR A N     1 
ATOM   461  C  CA    . THR A 1 57  ? -20.641 12.593  -9.118  1.00 24.69 ?  56  THR A CA    1 
ATOM   462  C  C     . THR A 1 57  ? -19.456 12.741  -8.173  1.00 21.91 ?  56  THR A C     1 
ATOM   463  O  O     . THR A 1 57  ? -18.896 11.719  -7.762  1.00 22.05 ?  56  THR A O     1 
ATOM   464  C  CB    . THR A 1 57  ? -21.787 11.901  -8.372  1.00 27.67 ?  56  THR A CB    1 
ATOM   465  O  OG1   . THR A 1 57  ? -22.837 11.578  -9.285  1.00 29.88 ?  56  THR A OG1   1 
ATOM   466  C  CG2   . THR A 1 57  ? -22.332 12.806  -7.285  1.00 29.69 ?  56  THR A CG2   1 
ATOM   467  N  N     . PRO A 1 58  ? -19.078 13.952  -7.776  1.00 20.92 ?  57  PRO A N     1 
ATOM   468  C  CA    . PRO A 1 58  ? -17.979 14.113  -6.817  1.00 17.69 ?  57  PRO A CA    1 
ATOM   469  C  C     . PRO A 1 58  ? -18.486 14.183  -5.380  1.00 17.19 ?  57  PRO A C     1 
ATOM   470  O  O     . PRO A 1 58  ? -19.649 14.498  -5.117  1.00 15.74 ?  57  PRO A O     1 
ATOM   471  C  CB    . PRO A 1 58  ? -17.354 15.440  -7.251  1.00 20.68 ?  57  PRO A CB    1 
ATOM   472  C  CG    . PRO A 1 58  ? -18.552 16.249  -7.760  1.00 21.60 ?  57  PRO A CG    1 
ATOM   473  C  CD    . PRO A 1 58  ? -19.594 15.251  -8.244  1.00 22.84 ?  57  PRO A CD    1 
ATOM   474  N  N     . PHE A 1 59  ? -17.583 13.878  -4.450  1.00 16.95 ?  58  PHE A N     1 
ATOM   475  C  CA    . PHE A 1 59  ? -17.865 14.099  -3.032  1.00 15.07 ?  58  PHE A CA    1 
ATOM   476  C  C     . PHE A 1 59  ? -16.560 14.421  -2.300  1.00 15.33 ?  58  PHE A C     1 
ATOM   477  O  O     . PHE A 1 59  ? -15.469 14.023  -2.716  1.00 14.63 ?  58  PHE A O     1 
ATOM   478  C  CB    . PHE A 1 59  ? -18.601 12.901  -2.393  1.00 13.68 ?  58  PHE A CB    1 
ATOM   479  C  CG    . PHE A 1 59  ? -17.820 11.609  -2.388  1.00 14.78 ?  58  PHE A CG    1 
ATOM   480  C  CD1   . PHE A 1 59  ? -17.798 10.773  -3.499  1.00 15.47 ?  58  PHE A CD1   1 
ATOM   481  C  CD2   . PHE A 1 59  ? -17.112 11.215  -1.264  1.00 15.25 ?  58  PHE A CD2   1 
ATOM   482  C  CE1   . PHE A 1 59  ? -17.088 9.575   -3.479  1.00 15.68 ?  58  PHE A CE1   1 
ATOM   483  C  CE2   . PHE A 1 59  ? -16.386 10.039  -1.239  1.00 14.39 ?  58  PHE A CE2   1 
ATOM   484  C  CZ    . PHE A 1 59  ? -16.372 9.207   -2.367  1.00 15.35 ?  58  PHE A CZ    1 
ATOM   485  N  N     . ASN A 1 60  ? -16.680 15.193  -1.226  1.00 13.55 ?  59  ASN A N     1 
ATOM   486  C  CA    . ASN A 1 60  ? -15.487 15.616  -0.487  1.00 10.84 ?  59  ASN A CA    1 
ATOM   487  C  C     . ASN A 1 60  ? -14.926 14.458  0.330   1.00 10.85 ?  59  ASN A C     1 
ATOM   488  O  O     . ASN A 1 60  ? -15.676 13.660  0.888   1.00 11.76 ?  59  ASN A O     1 
ATOM   489  C  CB    . ASN A 1 60  ? -15.848 16.773  0.434   1.00 13.13 ?  59  ASN A CB    1 
ATOM   490  C  CG    . ASN A 1 60  ? -16.227 18.027  -0.317  1.00 16.60 ?  59  ASN A CG    1 
ATOM   491  O  OD1   . ASN A 1 60  ? -15.872 18.193  -1.481  1.00 19.86 ?  59  ASN A OD1   1 
ATOM   492  N  ND2   . ASN A 1 60  ? -16.917 18.940  0.361   1.00 20.06 ?  59  ASN A ND2   1 
ATOM   493  N  N     . GLN A 1 61  ? -13.597 14.370  0.411   1.00 10.91 ?  60  GLN A N     1 
ATOM   494  C  CA    . GLN A 1 61  ? -12.932 13.346  1.209   1.00 11.37 ?  60  GLN A CA    1 
ATOM   495  C  C     . GLN A 1 61  ? -11.838 13.969  2.069   1.00 8.44  ?  60  GLN A C     1 
ATOM   496  O  O     . GLN A 1 61  ? -11.497 15.152  1.919   1.00 9.25  ?  60  GLN A O     1 
ATOM   497  C  CB    . GLN A 1 61  ? -12.293 12.251  0.335   1.00 14.64 ?  60  GLN A CB    1 
ATOM   498  C  CG    . GLN A 1 61  ? -13.310 11.344  -0.286  1.00 17.04 ?  60  GLN A CG    1 
ATOM   499  C  CD    . GLN A 1 61  ? -12.751 10.014  -0.717  1.00 17.84 ?  60  GLN A CD    1 
ATOM   500  O  OE1   . GLN A 1 61  ? -12.839 9.656   -1.889  1.00 23.25 ?  60  GLN A OE1   1 
ATOM   501  N  NE2   . GLN A 1 61  ? -12.250 9.242   0.225   1.00 16.16 ?  60  GLN A NE2   1 
ATOM   502  N  N     . GLY A 1 62  ? -11.270 13.132  2.969   1.00 8.62  ?  61  GLY A N     1 
ATOM   503  C  CA    . GLY A 1 62  ? -10.055 13.479  3.660   1.00 7.06  ?  61  GLY A CA    1 
ATOM   504  C  C     . GLY A 1 62  ? -10.249 14.566  4.714   1.00 9.18  ?  61  GLY A C     1 
ATOM   505  O  O     . GLY A 1 62  ? -11.368 14.907  5.149   1.00 9.62  ?  61  GLY A O     1 
ATOM   506  N  N     . SER A 1 63  ? -9.111  15.118  5.106   1.00 8.11  ?  62  SER A N     1 
ATOM   507  C  CA    . SER A 1 63  ? -9.107  16.012  6.251   1.00 8.09  ?  62  SER A CA    1 
ATOM   508  C  C     . SER A 1 63  ? -9.905  17.299  6.000   1.00 11.66 ?  62  SER A C     1 
ATOM   509  O  O     . SER A 1 63  ? -10.461 17.867  6.945   1.00 9.82  ?  62  SER A O     1 
ATOM   510  C  CB    . SER A 1 63  ? -7.658  16.300  6.616   1.00 9.69  ?  62  SER A CB    1 
ATOM   511  O  OG    . SER A 1 63  ? -7.097  17.162  5.641   1.00 10.22 ?  62  SER A OG    1 
ATOM   512  N  N     . TYR A 1 64  ? -9.977  17.788  4.751   1.00 10.34 ?  63  TYR A N     1 
ATOM   513  C  CA    . TYR A 1 64  ? -10.751 18.989  4.501   1.00 11.56 ?  63  TYR A CA    1 
ATOM   514  C  C     . TYR A 1 64  ? -12.246 18.705  4.482   1.00 11.82 ?  63  TYR A C     1 
ATOM   515  O  O     . TYR A 1 64  ? -13.037 19.644  4.569   1.00 14.28 ?  63  TYR A O     1 
ATOM   516  C  CB    . TYR A 1 64  ? -10.249 19.643  3.201   1.00 14.69 ?  63  TYR A CB    1 
ATOM   517  C  CG    . TYR A 1 64  ? -8.776  19.942  3.263   1.00 22.10 ?  63  TYR A CG    1 
ATOM   518  C  CD1   . TYR A 1 64  ? -8.194  20.398  4.448   1.00 30.02 ?  63  TYR A CD1   1 
ATOM   519  C  CD2   . TYR A 1 64  ? -7.968  19.764  2.170   1.00 27.59 ?  63  TYR A CD2   1 
ATOM   520  C  CE1   . TYR A 1 64  ? -6.831  20.658  4.522   1.00 32.17 ?  63  TYR A CE1   1 
ATOM   521  C  CE2   . TYR A 1 64  ? -6.608  20.036  2.234   1.00 32.31 ?  63  TYR A CE2   1 
ATOM   522  C  CZ    . TYR A 1 64  ? -6.054  20.466  3.407   1.00 36.21 ?  63  TYR A CZ    1 
ATOM   523  O  OH    . TYR A 1 64  ? -4.707  20.724  3.450   1.00 46.20 ?  63  TYR A OH    1 
ATOM   524  N  N     . ALA A 1 65  ? -12.652 17.430  4.429   1.00 9.97  ?  64  ALA A N     1 
ATOM   525  C  CA    . ALA A 1 65  ? -14.047 17.070  4.641   1.00 11.78 ?  64  ALA A CA    1 
ATOM   526  C  C     . ALA A 1 65  ? -14.346 16.849  6.118   1.00 11.01 ?  64  ALA A C     1 
ATOM   527  O  O     . ALA A 1 65  ? -15.456 17.134  6.587   1.00 14.92 ?  64  ALA A O     1 
ATOM   528  C  CB    . ALA A 1 65  ? -14.403 15.808  3.861   1.00 11.72 ?  64  ALA A CB    1 
ATOM   529  N  N     . MET A 1 66  ? -13.378 16.321  6.840   1.00 8.61  ?  65  MET A N     1 
ATOM   530  C  CA    . MET A 1 66  ? -13.567 15.932  8.223   1.00 9.23  ?  65  MET A CA    1 
ATOM   531  C  C     . MET A 1 66  ? -13.188 17.047  9.192   1.00 10.02 ?  65  MET A C     1 
ATOM   532  O  O     . MET A 1 66  ? -13.232 16.838  10.412  1.00 8.47  ?  65  MET A O     1 
ATOM   533  C  CB    . MET A 1 66  ? -12.749 14.669  8.528   1.00 8.35  ?  65  MET A CB    1 
ATOM   534  C  CG    . MET A 1 66  ? -13.135 13.451  7.688   1.00 10.93 ?  65  MET A CG    1 
ATOM   535  S  SD    . MET A 1 66  ? -12.369 11.920  8.151   1.00 10.98 ?  65  MET A SD    1 
ATOM   536  C  CE    . MET A 1 66  ? -10.675 12.149  7.552   1.00 13.79 ?  65  MET A CE    1 
ATOM   537  N  N     . ASN A 1 67  ? -12.712 18.199  8.690   1.00 10.12 ?  66  ASN A N     1 
ATOM   538  C  CA    . ASN A 1 67  ? -12.319 19.301  9.569   1.00 7.87  ?  66  ASN A CA    1 
ATOM   539  C  C     . ASN A 1 67  ? -11.142 18.900  10.473  1.00 10.02 ?  66  ASN A C     1 
ATOM   540  O  O     . ASN A 1 67  ? -11.078 19.250  11.656  1.00 10.64 ?  66  ASN A O     1 
ATOM   541  C  CB    . ASN A 1 67  ? -13.522 19.815  10.384  1.00 8.39  ?  66  ASN A CB    1 
ATOM   542  C  CG    . ASN A 1 67  ? -13.286 21.196  10.940  1.00 10.43 ?  66  ASN A CG    1 
ATOM   543  O  OD1   . ASN A 1 67  ? -12.398 21.914  10.493  1.00 11.47 ?  66  ASN A OD1   1 
ATOM   544  N  ND2   . ASN A 1 67  ? -14.083 21.579  11.895  1.00 11.73 ?  66  ASN A ND2   1 
ATOM   545  N  N     . THR A 1 68  ? -10.193 18.161  9.892   1.00 9.91  ?  67  THR A N     1 
ATOM   546  C  CA    . THR A 1 68  ? -8.953  17.826  10.577  1.00 8.04  ?  67  THR A CA    1 
ATOM   547  C  C     . THR A 1 68  ? -7.717  18.309  9.808   1.00 10.44 ?  67  THR A C     1 
ATOM   548  O  O     . THR A 1 68  ? -6.603  17.797  10.004  1.00 9.88  ?  67  THR A O     1 
ATOM   549  C  CB    . THR A 1 68  ? -8.858  16.326  10.758  1.00 7.96  ?  67  THR A CB    1 
ATOM   550  O  OG1   . THR A 1 68  ? -8.987  15.729  9.471   1.00 8.28  ?  67  THR A OG1   1 
ATOM   551  C  CG2   . THR A 1 68  ? -9.981  15.822  11.671  1.00 10.91 ?  67  THR A CG2   1 
ATOM   552  N  N     . GLY A 1 69  ? -7.873  19.345  8.989   1.00 11.10 ?  68  GLY A N     1 
ATOM   553  C  CA    . GLY A 1 69  ? -6.792  19.790  8.132   1.00 9.55  ?  68  GLY A CA    1 
ATOM   554  C  C     . GLY A 1 69  ? -5.812  20.751  8.779   1.00 8.34  ?  68  GLY A C     1 
ATOM   555  O  O     . GLY A 1 69  ? -6.173  21.561  9.651   1.00 8.70  ?  68  GLY A O     1 
ATOM   556  N  N     . VAL A 1 70  ? -4.559  20.626  8.351   1.00 7.26  ?  69  VAL A N     1 
ATOM   557  C  CA    . VAL A 1 70  ? -3.502  21.529  8.810   1.00 8.17  ?  69  VAL A CA    1 
ATOM   558  C  C     . VAL A 1 70  ? -2.824  22.226  7.620   1.00 7.91  ?  69  VAL A C     1 
ATOM   559  O  O     . VAL A 1 70  ? -2.749  21.719  6.491   1.00 12.87 ?  69  VAL A O     1 
ATOM   560  C  CB    . VAL A 1 70  ? -2.425  20.810  9.662   1.00 11.00 ?  69  VAL A CB    1 
ATOM   561  C  CG1   . VAL A 1 70  ? -3.003  20.308  11.015  1.00 10.03 ?  69  VAL A CG1   1 
ATOM   562  C  CG2   . VAL A 1 70  ? -1.751  19.670  8.866   1.00 9.55  ?  69  VAL A CG2   1 
ATOM   563  N  N     . LYS A 1 71  ? -2.300  23.412  7.923   1.00 9.80  ?  70  LYS A N     1 
ATOM   564  C  CA    . LYS A 1 71  ? -1.458  24.092  6.969   1.00 9.21  ?  70  LYS A CA    1 
ATOM   565  C  C     . LYS A 1 71  ? -0.114  23.380  6.867   1.00 9.80  ?  70  LYS A C     1 
ATOM   566  O  O     . LYS A 1 71  ? 0.464   22.978  7.887   1.00 10.76 ?  70  LYS A O     1 
ATOM   567  C  CB    . LYS A 1 71  ? -1.254  25.536  7.405   1.00 9.71  ?  70  LYS A CB    1 
ATOM   568  C  CG    . LYS A 1 71  ? -2.527  26.397  7.323   1.00 9.10  ?  70  LYS A CG    1 
ATOM   569  C  CD    . LYS A 1 71  ? -2.312  27.729  8.061   1.00 12.00 ?  70  LYS A CD    1 
ATOM   570  C  CE    . LYS A 1 71  ? -3.440  28.711  7.686   1.00 14.41 ?  70  LYS A CE    1 
ATOM   571  N  NZ    . LYS A 1 71  ? -3.320  30.007  8.387   1.00 13.90 1  70  LYS A NZ    1 
ATOM   572  N  N     . PRO A 1 72  ? 0.427   23.247  5.667   1.00 10.18 ?  71  PRO A N     1 
ATOM   573  C  CA    . PRO A 1 72  ? 1.779   22.701  5.512   1.00 11.31 ?  71  PRO A CA    1 
ATOM   574  C  C     . PRO A 1 72  ? 2.846   23.669  5.982   1.00 11.55 ?  71  PRO A C     1 
ATOM   575  O  O     . PRO A 1 72  ? 2.654   24.896  6.021   1.00 13.31 ?  71  PRO A O     1 
ATOM   576  C  CB    . PRO A 1 72  ? 1.908   22.473  3.999   1.00 12.22 ?  71  PRO A CB    1 
ATOM   577  C  CG    . PRO A 1 72  ? 0.968   23.512  3.418   1.00 13.98 ?  71  PRO A CG    1 
ATOM   578  C  CD    . PRO A 1 72  ? -0.158  23.733  4.400   1.00 12.84 ?  71  PRO A CD    1 
ATOM   579  N  N     . LEU A 1 73  ? 3.977   23.107  6.373   1.00 13.56 ?  72  LEU A N     1 
ATOM   580  C  CA    . LEU A 1 73  ? 5.155   23.917  6.642   1.00 15.26 ?  72  LEU A CA    1 
ATOM   581  C  C     . LEU A 1 73  ? 5.660   24.531  5.341   1.00 15.91 ?  72  LEU A C     1 
ATOM   582  O  O     . LEU A 1 73  ? 5.306   24.093  4.240   1.00 15.64 ?  72  LEU A O     1 
ATOM   583  C  CB    . LEU A 1 73  ? 6.248   23.081  7.289   1.00 16.63 ?  72  LEU A CB    1 
ATOM   584  C  CG    . LEU A 1 73  ? 5.834   22.588  8.677   1.00 17.26 ?  72  LEU A CG    1 
ATOM   585  C  CD1   . LEU A 1 73  ? 6.870   21.579  9.169   1.00 19.29 ?  72  LEU A CD1   1 
ATOM   586  C  CD2   . LEU A 1 73  ? 5.744   23.764  9.624   1.00 16.21 ?  72  LEU A CD2   1 
ATOM   587  N  N     . GLU A 1 74  ? 6.558   25.516  5.462   1.00 20.90 ?  73  GLU A N     1 
ATOM   588  C  CA    . GLU A 1 74  ? 7.097   26.134  4.249   1.00 28.34 ?  73  GLU A CA    1 
ATOM   589  C  C     . GLU A 1 74  ? 7.695   25.074  3.334   1.00 25.84 ?  73  GLU A C     1 
ATOM   590  O  O     . GLU A 1 74  ? 8.434   24.190  3.780   1.00 26.16 ?  73  GLU A O     1 
ATOM   591  C  CB    . GLU A 1 74  ? 8.148   27.197  4.587   1.00 36.35 ?  73  GLU A CB    1 
ATOM   592  C  CG    . GLU A 1 74  ? 8.771   27.847  3.346   1.00 44.96 ?  73  GLU A CG    1 
ATOM   593  C  CD    . GLU A 1 74  ? 9.911   28.795  3.679   1.00 53.86 ?  73  GLU A CD    1 
ATOM   594  O  OE1   . GLU A 1 74  ? 10.151  29.056  4.882   1.00 58.50 ?  73  GLU A OE1   1 
ATOM   595  O  OE2   . GLU A 1 74  ? 10.574  29.279  2.733   1.00 59.17 -1 73  GLU A OE2   1 
ATOM   596  N  N     . GLY A 1 75  ? 7.352   25.144  2.047   1.00 25.66 ?  74  GLY A N     1 
ATOM   597  C  CA    . GLY A 1 75  ? 7.798   24.163  1.079   1.00 25.02 ?  74  GLY A CA    1 
ATOM   598  C  C     . GLY A 1 75  ? 6.906   22.942  0.941   1.00 25.32 ?  74  GLY A C     1 
ATOM   599  O  O     . GLY A 1 75  ? 6.960   22.266  -0.097  1.00 26.27 ?  74  GLY A O     1 
ATOM   600  N  N     . GLY A 1 76  ? 6.076   22.639  1.961   1.00 23.48 ?  75  GLY A N     1 
ATOM   601  C  CA    . GLY A 1 76  ? 5.147   21.533  1.858   1.00 21.20 ?  75  GLY A CA    1 
ATOM   602  C  C     . GLY A 1 76  ? 3.932   21.883  1.031   1.00 22.52 ?  75  GLY A C     1 
ATOM   603  O  O     . GLY A 1 76  ? 3.689   23.027  0.668   1.00 25.64 ?  75  GLY A O     1 
ATOM   604  N  N     . GLU A 1 77  ? 3.113   20.872  0.752   1.00 19.95 ?  76  GLU A N     1 
ATOM   605  C  CA    . GLU A 1 77  ? 1.924   21.055  -0.071  1.00 20.39 ?  76  GLU A CA    1 
ATOM   606  C  C     . GLU A 1 77  ? 0.662   20.702  0.708   1.00 20.50 ?  76  GLU A C     1 
ATOM   607  O  O     . GLU A 1 77  ? 0.687   19.814  1.559   1.00 22.36 ?  76  GLU A O     1 
ATOM   608  C  CB    . GLU A 1 77  ? 1.956   20.177  -1.317  1.00 24.02 ?  76  GLU A CB    1 
ATOM   609  C  CG    . GLU A 1 77  ? 3.101   20.466  -2.250  1.00 30.62 ?  76  GLU A CG    1 
ATOM   610  C  CD    . GLU A 1 77  ? 2.970   19.698  -3.552  1.00 38.00 ?  76  GLU A CD    1 
ATOM   611  O  OE1   . GLU A 1 77  ? 2.591   18.509  -3.514  1.00 39.36 ?  76  GLU A OE1   1 
ATOM   612  O  OE2   . GLU A 1 77  ? 3.235   20.289  -4.620  1.00 44.38 -1 76  GLU A OE2   1 
ATOM   613  N  N     . TYR A 1 78  ? -0.425  21.401  0.368   1.00 21.52 ?  77  TYR A N     1 
ATOM   614  C  CA    . TYR A 1 78  ? -1.796  21.061  0.717   1.00 22.94 ?  77  TYR A CA    1 
ATOM   615  C  C     . TYR A 1 78  ? -2.247  19.856  -0.081  1.00 18.84 ?  77  TYR A C     1 
ATOM   616  O  O     . TYR A 1 78  ? -1.768  19.584  -1.183  1.00 19.13 ?  77  TYR A O     1 
ATOM   617  C  CB    . TYR A 1 78  ? -2.785  22.176  0.350   1.00 33.67 ?  77  TYR A CB    1 
ATOM   618  C  CG    . TYR A 1 78  ? -2.570  23.517  0.967   1.00 42.26 ?  77  TYR A CG    1 
ATOM   619  C  CD1   . TYR A 1 78  ? -1.884  24.513  0.299   1.00 47.27 ?  77  TYR A CD1   1 
ATOM   620  C  CD2   . TYR A 1 78  ? -3.101  23.804  2.204   1.00 47.80 ?  77  TYR A CD2   1 
ATOM   621  C  CE1   . TYR A 1 78  ? -1.702  25.761  0.880   1.00 51.39 ?  77  TYR A CE1   1 
ATOM   622  C  CE2   . TYR A 1 78  ? -2.932  25.044  2.795   1.00 51.93 ?  77  TYR A CE2   1 
ATOM   623  C  CZ    . TYR A 1 78  ? -2.235  26.017  2.136   1.00 54.55 ?  77  TYR A CZ    1 
ATOM   624  O  OH    . TYR A 1 78  ? -2.092  27.238  2.755   1.00 59.33 ?  77  TYR A OH    1 
ATOM   625  N  N     . ASP A 1 79  ? -3.269  19.201  0.443   1.00 14.12 ?  78  ASP A N     1 
ATOM   626  C  CA    . ASP A 1 79  ? -3.717  17.927  -0.074  1.00 16.22 ?  78  ASP A CA    1 
ATOM   627  C  C     . ASP A 1 79  ? -5.236  17.946  -0.211  1.00 14.68 ?  78  ASP A C     1 
ATOM   628  O  O     . ASP A 1 79  ? -5.928  17.697  0.768   1.00 14.05 ?  78  ASP A O     1 
ATOM   629  C  CB    . ASP A 1 79  ? -3.276  16.870  0.925   1.00 24.33 ?  78  ASP A CB    1 
ATOM   630  C  CG    . ASP A 1 79  ? -3.700  15.552  0.528   1.00 23.05 ?  78  ASP A CG    1 
ATOM   631  O  OD1   . ASP A 1 79  ? -3.343  15.198  -0.601  1.00 29.67 ?  78  ASP A OD1   1 
ATOM   632  O  OD2   . ASP A 1 79  ? -4.418  14.900  1.287   1.00 14.27 -1 78  ASP A OD2   1 
ATOM   633  N  N     . ILE A 1 80  ? -5.788  18.211  -1.399  1.00 12.85 ?  79  ILE A N     1 
ATOM   634  C  CA    . ILE A 1 80  ? -7.235  18.312  -1.580  1.00 15.05 ?  79  ILE A CA    1 
ATOM   635  C  C     . ILE A 1 80  ? -7.714  16.919  -1.979  1.00 15.66 ?  79  ILE A C     1 
ATOM   636  O  O     . ILE A 1 80  ? -7.396  16.453  -3.067  1.00 17.45 ?  79  ILE A O     1 
ATOM   637  C  CB    . ILE A 1 80  ? -7.577  19.353  -2.657  1.00 19.18 ?  79  ILE A CB    1 
ATOM   638  C  CG1   . ILE A 1 80  ? -7.321  20.766  -2.163  1.00 22.56 ?  79  ILE A CG1   1 
ATOM   639  C  CG2   . ILE A 1 80  ? -9.018  19.256  -3.107  1.00 20.09 ?  79  ILE A CG2   1 
ATOM   640  C  CD1   . ILE A 1 80  ? -7.563  21.820  -3.245  1.00 22.37 ?  79  ILE A CD1   1 
ATOM   641  N  N     . ASP A 1 81  ? -8.459  16.241  -1.102  1.00 11.48 ?  80  ASP A N     1 
ATOM   642  C  CA    . ASP A 1 81  ? -8.920  14.883  -1.364  1.00 12.74 ?  80  ASP A CA    1 
ATOM   643  C  C     . ASP A 1 81  ? -10.360 14.933  -1.845  1.00 13.32 ?  80  ASP A C     1 
ATOM   644  O  O     . ASP A 1 81  ? -11.205 15.566  -1.204  1.00 13.33 ?  80  ASP A O     1 
ATOM   645  C  CB    . ASP A 1 81  ? -8.844  14.027  -0.092  1.00 14.02 ?  80  ASP A CB    1 
ATOM   646  C  CG    . ASP A 1 81  ? -7.442  13.936  0.461   1.00 14.06 ?  80  ASP A CG    1 
ATOM   647  O  OD1   . ASP A 1 81  ? -6.549  13.502  -0.275  1.00 15.54 ?  80  ASP A OD1   1 
ATOM   648  O  OD2   . ASP A 1 81  ? -7.230  14.297  1.651   1.00 12.04 -1 80  ASP A OD2   1 
ATOM   649  N  N     . VAL A 1 82  ? -10.653 14.250  -2.962  1.00 13.62 ?  81  VAL A N     1 
ATOM   650  C  CA    . VAL A 1 82  ? -12.012 14.222  -3.478  1.00 16.53 ?  81  VAL A CA    1 
ATOM   651  C  C     . VAL A 1 82  ? -12.282 12.840  -4.053  1.00 16.04 ?  81  VAL A C     1 
ATOM   652  O  O     . VAL A 1 82  ? -11.358 12.141  -4.467  1.00 17.76 ?  81  VAL A O     1 
ATOM   653  C  CB    . VAL A 1 82  ? -12.212 15.337  -4.536  1.00 21.55 ?  81  VAL A CB    1 
ATOM   654  C  CG1   . VAL A 1 82  ? -11.259 15.119  -5.639  1.00 24.79 ?  81  VAL A CG1   1 
ATOM   655  C  CG2   . VAL A 1 82  ? -13.636 15.364  -5.083  1.00 23.51 ?  81  VAL A CG2   1 
ATOM   656  N  N     . GLY A 1 83  ? -13.541 12.417  -4.011  1.00 17.89 ?  82  GLY A N     1 
ATOM   657  C  CA    . GLY A 1 83  ? -13.976 11.178  -4.637  1.00 18.59 ?  82  GLY A CA    1 
ATOM   658  C  C     . GLY A 1 83  ? -14.812 11.518  -5.861  1.00 15.74 ?  82  GLY A C     1 
ATOM   659  O  O     . GLY A 1 83  ? -15.531 12.511  -5.872  1.00 17.69 ?  82  GLY A O     1 
ATOM   660  N  N     . ILE A 1 84  ? -14.676 10.720  -6.911  1.00 18.68 ?  83  ILE A N     1 
ATOM   661  C  CA    . ILE A 1 84  ? -15.562 10.855  -8.055  1.00 20.34 ?  83  ILE A CA    1 
ATOM   662  C  C     . ILE A 1 84  ? -16.119 9.483   -8.366  1.00 17.86 ?  83  ILE A C     1 
ATOM   663  O  O     . ILE A 1 84  ? -15.369 8.506   -8.463  1.00 18.39 ?  83  ILE A O     1 
ATOM   664  C  CB    . ILE A 1 84  ? -14.868 11.466  -9.288  1.00 21.64 ?  83  ILE A CB    1 
ATOM   665  C  CG1   . ILE A 1 84  ? -13.606 10.704  -9.676  1.00 21.63 ?  83  ILE A CG1   1 
ATOM   666  C  CG2   . ILE A 1 84  ? -14.533 12.936  -9.025  1.00 21.92 ?  83  ILE A CG2   1 
ATOM   667  C  CD1   . ILE A 1 84  ? -12.999 11.254  -10.995 1.00 22.30 ?  83  ILE A CD1   1 
ATOM   668  N  N     . ILE A 1 85  ? -17.431 9.412   -8.507  1.00 20.79 ?  84  ILE A N     1 
ATOM   669  C  CA    . ILE A 1 85  ? -18.141 8.170   -8.740  1.00 21.89 ?  84  ILE A CA    1 
ATOM   670  C  C     . ILE A 1 85  ? -18.584 8.179   -10.200 1.00 21.89 ?  84  ILE A C     1 
ATOM   671  O  O     . ILE A 1 85  ? -19.495 8.934   -10.573 1.00 23.67 ?  84  ILE A O     1 
ATOM   672  C  CB    . ILE A 1 85  ? -19.344 8.029   -7.806  1.00 19.91 ?  84  ILE A CB    1 
ATOM   673  C  CG1   . ILE A 1 85  ? -18.906 8.236   -6.350  1.00 20.35 ?  84  ILE A CG1   1 
ATOM   674  C  CG2   . ILE A 1 85  ? -19.959 6.683   -8.012  1.00 20.30 ?  84  ILE A CG2   1 
ATOM   675  C  CD1   . ILE A 1 85  ? -20.067 8.144   -5.371  1.00 21.12 ?  84  ILE A CD1   1 
ATOM   676  N  N     . LEU A 1 86  ? -17.921 7.375   -11.018 1.00 24.48 ?  85  LEU A N     1 
ATOM   677  C  CA    . LEU A 1 86  ? -18.239 7.312   -12.439 1.00 27.65 ?  85  LEU A CA    1 
ATOM   678  C  C     . LEU A 1 86  ? -19.457 6.432   -12.687 1.00 29.14 ?  85  LEU A C     1 
ATOM   679  O  O     . LEU A 1 86  ? -19.682 5.427   -11.995 1.00 26.55 ?  85  LEU A O     1 
ATOM   680  C  CB    . LEU A 1 86  ? -17.056 6.773   -13.242 1.00 28.94 ?  85  LEU A CB    1 
ATOM   681  C  CG    . LEU A 1 86  ? -15.930 7.761   -13.539 1.00 30.89 ?  85  LEU A CG    1 
ATOM   682  C  CD1   . LEU A 1 86  ? -14.833 7.045   -14.252 1.00 31.59 ?  85  LEU A CD1   1 
ATOM   683  C  CD2   . LEU A 1 86  ? -16.434 8.900   -14.390 1.00 32.04 ?  85  LEU A CD2   1 
ATOM   684  N  N     . ASN A 1 87  ? -20.227 6.814   -13.715 1.00 31.08 ?  86  ASN A N     1 
ATOM   685  C  CA    . ASN A 1 87  ? -21.462 6.125   -14.099 1.00 35.31 ?  86  ASN A CA    1 
ATOM   686  C  C     . ASN A 1 87  ? -21.131 4.881   -14.930 1.00 32.57 ?  86  ASN A C     1 
ATOM   687  O  O     . ASN A 1 87  ? -21.521 4.736   -16.095 1.00 30.08 ?  86  ASN A O     1 
ATOM   688  C  CB    . ASN A 1 87  ? -22.363 7.090   -14.858 1.00 43.88 ?  86  ASN A CB    1 
ATOM   689  C  CG    . ASN A 1 87  ? -23.720 6.505   -15.173 1.00 51.79 ?  86  ASN A CG    1 
ATOM   690  O  OD1   . ASN A 1 87  ? -24.240 5.664   -14.436 1.00 55.09 ?  86  ASN A OD1   1 
ATOM   691  N  ND2   . ASN A 1 87  ? -24.309 6.951   -16.280 1.00 57.99 ?  86  ASN A ND2   1 
ATOM   692  N  N     . ILE A 1 88  ? -20.382 3.967   -14.297 1.00 28.30 ?  87  ILE A N     1 
ATOM   693  C  CA    . ILE A 1 88  ? -19.831 2.798   -14.971 1.00 27.14 ?  87  ILE A CA    1 
ATOM   694  C  C     . ILE A 1 88  ? -19.963 1.569   -14.084 1.00 26.24 ?  87  ILE A C     1 
ATOM   695  O  O     . ILE A 1 88  ? -20.053 1.656   -12.858 1.00 26.79 ?  87  ILE A O     1 
ATOM   696  C  CB    . ILE A 1 88  ? -18.353 2.974   -15.377 1.00 25.45 ?  87  ILE A CB    1 
ATOM   697  C  CG1   . ILE A 1 88  ? -17.482 3.177   -14.130 1.00 26.16 ?  87  ILE A CG1   1 
ATOM   698  C  CG2   . ILE A 1 88  ? -18.216 4.111   -16.389 1.00 26.00 ?  87  ILE A CG2   1 
ATOM   699  C  CD1   . ILE A 1 88  ? -15.990 3.084   -14.419 1.00 25.05 ?  87  ILE A CD1   1 
ATOM   700  N  N     . ALA A 1 89  ? -19.984 0.410   -14.730 1.00 25.58 ?  88  ALA A N     1 
ATOM   701  C  CA    . ALA A 1 89  ? -20.053 -0.867  -14.038 1.00 20.88 ?  88  ALA A CA    1 
ATOM   702  C  C     . ALA A 1 89  ? -18.641 -1.371  -13.794 1.00 25.11 ?  88  ALA A C     1 
ATOM   703  O  O     . ALA A 1 89  ? -17.831 -1.429  -14.723 1.00 24.37 ?  88  ALA A O     1 
ATOM   704  C  CB    . ALA A 1 89  ? -20.835 -1.883  -14.877 1.00 25.18 ?  88  ALA A CB    1 
ATOM   705  N  N     . LYS A 1 90  ? -18.344 -1.747  -12.548 1.00 24.38 ?  89  LYS A N     1 
ATOM   706  C  CA    . LYS A 1 90  ? -16.969 -2.110  -12.237 1.00 24.44 ?  89  LYS A CA    1 
ATOM   707  C  C     . LYS A 1 90  ? -16.550 -3.388  -12.950 1.00 26.99 ?  89  LYS A C     1 
ATOM   708  O  O     . LYS A 1 90  ? -15.380 -3.529  -13.311 1.00 27.20 ?  89  LYS A O     1 
ATOM   709  C  CB    . LYS A 1 90  ? -16.786 -2.246  -10.726 1.00 25.05 ?  89  LYS A CB    1 
ATOM   710  C  CG    . LYS A 1 90  ? -17.470 -3.434  -10.123 1.00 24.94 ?  89  LYS A CG    1 
ATOM   711  C  CD    . LYS A 1 90  ? -17.221 -3.481  -8.652  1.00 24.19 ?  89  LYS A CD    1 
ATOM   712  C  CE    . LYS A 1 90  ? -17.887 -4.680  -8.011  1.00 24.14 ?  89  LYS A CE    1 
ATOM   713  N  NZ    . LYS A 1 90  ? -17.464 -5.964  -8.634  1.00 26.38 1  89  LYS A NZ    1 
ATOM   714  N  N     . ASP A 1 91  ? -17.482 -4.314  -13.190 1.00 28.29 ?  90  ASP A N     1 
ATOM   715  C  CA    . ASP A 1 91  ? -17.093 -5.572  -13.820 1.00 30.20 ?  90  ASP A CA    1 
ATOM   716  C  C     . ASP A 1 91  ? -16.725 -5.408  -15.279 1.00 28.50 ?  90  ASP A C     1 
ATOM   717  O  O     . ASP A 1 91  ? -16.115 -6.316  -15.851 1.00 26.47 ?  90  ASP A O     1 
ATOM   718  C  CB    . ASP A 1 91  ? -18.219 -6.599  -13.715 1.00 34.59 ?  90  ASP A CB    1 
ATOM   719  C  CG    . ASP A 1 91  ? -18.360 -7.174  -12.335 1.00 38.07 ?  90  ASP A CG    1 
ATOM   720  O  OD1   . ASP A 1 91  ? -17.521 -6.863  -11.464 1.00 39.66 ?  90  ASP A OD1   1 
ATOM   721  O  OD2   . ASP A 1 91  ? -19.329 -7.935  -12.126 1.00 39.59 -1 90  ASP A OD2   1 
ATOM   722  N  N     . ASP A 1 92  ? -17.073 -4.285  -15.891 1.00 29.72 ?  91  ASP A N     1 
ATOM   723  C  CA    . ASP A 1 92  ? -16.824 -4.080  -17.304 1.00 30.44 ?  91  ASP A CA    1 
ATOM   724  C  C     . ASP A 1 92  ? -15.558 -3.289  -17.590 1.00 28.02 ?  91  ASP A C     1 
ATOM   725  O  O     . ASP A 1 92  ? -15.251 -3.052  -18.766 1.00 25.98 ?  91  ASP A O     1 
ATOM   726  C  CB    . ASP A 1 92  ? -18.027 -3.388  -17.944 1.00 33.73 ?  91  ASP A CB    1 
ATOM   727  C  CG    . ASP A 1 92  ? -19.288 -4.234  -17.863 1.00 36.50 ?  91  ASP A CG    1 
ATOM   728  O  OD1   . ASP A 1 92  ? -19.191 -5.478  -17.720 1.00 37.83 ?  91  ASP A OD1   1 
ATOM   729  O  OD2   . ASP A 1 92  ? -20.377 -3.649  -17.941 1.00 37.98 -1 91  ASP A OD2   1 
ATOM   730  N  N     . HIS A 1 93  ? -14.810 -2.868  -16.563 1.00 26.62 ?  92  HIS A N     1 
ATOM   731  C  CA    . HIS A 1 93  ? -13.620 -2.070  -16.809 1.00 27.58 ?  92  HIS A CA    1 
ATOM   732  C  C     . HIS A 1 93  ? -12.482 -2.502  -15.897 1.00 26.86 ?  92  HIS A C     1 
ATOM   733  O  O     . HIS A 1 93  ? -12.701 -2.986  -14.783 1.00 27.43 ?  92  HIS A O     1 
ATOM   734  C  CB    . HIS A 1 93  ? -13.918 -0.583  -16.641 1.00 27.39 ?  92  HIS A CB    1 
ATOM   735  C  CG    . HIS A 1 93  ? -14.993 -0.077  -17.554 1.00 29.79 ?  92  HIS A CG    1 
ATOM   736  N  ND1   . HIS A 1 93  ? -14.735 0.369   -18.832 1.00 29.59 ?  92  HIS A ND1   1 
ATOM   737  C  CD2   . HIS A 1 93  ? -16.332 0.042   -17.379 1.00 30.10 ?  92  HIS A CD2   1 
ATOM   738  C  CE1   . HIS A 1 93  ? -15.865 0.760   -19.398 1.00 30.59 ?  92  HIS A CE1   1 
ATOM   739  N  NE2   . HIS A 1 93  ? -16.850 0.572   -18.537 1.00 30.07 ?  92  HIS A NE2   1 
ATOM   740  N  N     . ASP A 1 94  ? -11.253 -2.360  -16.411 1.00 24.94 ?  93  ASP A N     1 
ATOM   741  C  CA    . ASP A 1 94  ? -10.070 -2.447  -15.555 1.00 26.02 ?  93  ASP A CA    1 
ATOM   742  C  C     . ASP A 1 94  ? -9.913  -1.148  -14.770 1.00 23.63 ?  93  ASP A C     1 
ATOM   743  O  O     . ASP A 1 94  ? -10.019 -0.063  -15.355 1.00 24.37 ?  93  ASP A O     1 
ATOM   744  C  CB    . ASP A 1 94  ? -8.812  -2.719  -16.387 1.00 27.12 ?  93  ASP A CB    1 
ATOM   745  C  CG    . ASP A 1 94  ? -7.530  -2.668  -15.555 1.00 30.22 ?  93  ASP A CG    1 
ATOM   746  O  OD1   . ASP A 1 94  ? -7.206  -3.663  -14.867 1.00 31.11 ?  93  ASP A OD1   1 
ATOM   747  O  OD2   . ASP A 1 94  ? -6.853  -1.619  -15.589 1.00 31.13 -1 93  ASP A OD2   1 
ATOM   748  N  N     . PRO A 1 95  ? -9.666  -1.213  -13.458 1.00 27.17 ?  94  PRO A N     1 
ATOM   749  C  CA    . PRO A 1 95  ? -9.495  0.030   -12.655 1.00 25.34 ?  94  PRO A CA    1 
ATOM   750  C  C     . PRO A 1 95  ? -8.431  0.995   -13.162 1.00 25.78 ?  94  PRO A C     1 
ATOM   751  O  O     . PRO A 1 95  ? -8.628  2.228   -13.127 1.00 22.48 ?  94  PRO A O     1 
ATOM   752  C  CB    . PRO A 1 95  ? -9.088  -0.494  -11.276 1.00 29.83 ?  94  PRO A CB    1 
ATOM   753  C  CG    . PRO A 1 95  ? -9.426  -1.893  -11.231 1.00 28.89 ?  94  PRO A CG    1 
ATOM   754  C  CD    . PRO A 1 95  ? -9.609  -2.427  -12.632 1.00 25.34 ?  94  PRO A CD    1 
ATOM   755  N  N     . VAL A 1 96  ? -7.277  0.461   -13.591 1.00 25.93 ?  95  VAL A N     1 
ATOM   756  C  CA    . VAL A 1 96  ? -6.206  1.313   -14.090 1.00 25.49 ?  95  VAL A CA    1 
ATOM   757  C  C     . VAL A 1 96  ? -6.649  2.038   -15.354 1.00 26.72 ?  95  VAL A C     1 
ATOM   758  O  O     . VAL A 1 96  ? -6.363  3.229   -15.526 1.00 24.94 ?  95  VAL A O     1 
ATOM   759  C  CB    . VAL A 1 96  ? -4.926  0.483   -14.308 1.00 29.07 ?  95  VAL A CB    1 
ATOM   760  C  CG1   . VAL A 1 96  ? -3.789  1.348   -14.848 1.00 30.29 ?  95  VAL A CG1   1 
ATOM   761  C  CG2   . VAL A 1 96  ? -4.512  -0.192  -13.011 1.00 28.85 ?  95  VAL A CG2   1 
ATOM   762  N  N     . GLU A 1 97  ? -7.398  1.351   -16.241 1.00 25.17 ?  96  GLU A N     1 
ATOM   763  C  CA    . GLU A 1 97  ? -7.871  2.011   -17.459 1.00 28.03 ?  96  GLU A CA    1 
ATOM   764  C  C     . GLU A 1 97  ? -8.790  3.189   -17.144 1.00 24.89 ?  96  GLU A C     1 
ATOM   765  O  O     . GLU A 1 97  ? -8.684  4.256   -17.762 1.00 27.59 ?  96  GLU A O     1 
ATOM   766  C  CB    . GLU A 1 97  ? -8.580  0.998   -18.370 1.00 28.46 ?  96  GLU A CB    1 
ATOM   767  C  CG    . GLU A 1 97  ? -7.632  0.016   -19.048 1.00 32.18 ?  96  GLU A CG    1 
ATOM   768  C  CD    . GLU A 1 97  ? -6.615  0.723   -19.923 1.00 35.87 ?  96  GLU A CD    1 
ATOM   769  O  OE1   . GLU A 1 97  ? -5.410  0.397   -19.840 1.00 37.70 ?  96  GLU A OE1   1 
ATOM   770  O  OE2   . GLU A 1 97  ? -7.029  1.622   -20.695 1.00 37.26 -1 96  GLU A OE2   1 
ATOM   771  N  N     . VAL A 1 98  ? -9.702  3.020   -16.185 1.00 24.60 ?  97  VAL A N     1 
ATOM   772  C  CA    . VAL A 1 98  ? -10.587 4.112   -15.785 1.00 24.41 ?  97  VAL A CA    1 
ATOM   773  C  C     . VAL A 1 98  ? -9.771  5.281   -15.230 1.00 23.82 ?  97  VAL A C     1 
ATOM   774  O  O     . VAL A 1 98  ? -9.977  6.460   -15.598 1.00 25.34 ?  97  VAL A O     1 
ATOM   775  C  CB    . VAL A 1 98  ? -11.618 3.572   -14.775 1.00 23.21 ?  97  VAL A CB    1 
ATOM   776  C  CG1   . VAL A 1 98  ? -12.405 4.685   -14.155 1.00 21.26 ?  97  VAL A CG1   1 
ATOM   777  C  CG2   . VAL A 1 98  ? -12.547 2.603   -15.487 1.00 21.05 ?  97  VAL A CG2   1 
ATOM   778  N  N     . LYS A 1 99  ? -8.783  4.974   -14.400 1.00 25.03 ?  98  LYS A N     1 
ATOM   779  C  CA    . LYS A 1 99  ? -7.896  6.045   -13.954 1.00 26.59 ?  98  LYS A CA    1 
ATOM   780  C  C     . LYS A 1 99  ? -7.106  6.659   -15.106 1.00 27.32 ?  98  LYS A C     1 
ATOM   781  O  O     . LYS A 1 99  ? -6.730  7.831   -15.030 1.00 27.51 ?  98  LYS A O     1 
ATOM   782  C  CB    . LYS A 1 99  ? -6.987  5.532   -12.842 1.00 26.84 ?  98  LYS A CB    1 
ATOM   783  C  CG    . LYS A 1 99  ? -7.718  5.592   -11.489 1.00 26.97 ?  98  LYS A CG    1 
ATOM   784  C  CD    . LYS A 1 99  ? -6.846  5.252   -10.312 1.00 26.37 ?  98  LYS A CD    1 
ATOM   785  C  CE    . LYS A 1 99  ? -6.533  3.769   -10.304 1.00 25.92 ?  98  LYS A CE    1 
ATOM   786  N  NZ    . LYS A 1 99  ? -5.580  3.466   -9.222  1.00 22.37 1  98  LYS A NZ    1 
ATOM   787  N  N     . LYS A 1 100 ? -6.889  5.908   -16.200 1.00 26.72 ?  99  LYS A N     1 
ATOM   788  C  CA    . LYS A 1 100 ? -6.251  6.495   -17.377 1.00 27.15 ?  99  LYS A CA    1 
ATOM   789  C  C     . LYS A 1 100 ? -7.164  7.523   -18.011 1.00 27.81 ?  99  LYS A C     1 
ATOM   790  O  O     . LYS A 1 100 ? -6.697  8.553   -18.507 1.00 29.82 ?  99  LYS A O     1 
ATOM   791  C  CB    . LYS A 1 100 ? -5.884  5.420   -18.398 1.00 30.01 ?  99  LYS A CB    1 
ATOM   792  C  CG    . LYS A 1 100 ? -4.692  4.579   -18.019 1.00 30.44 ?  99  LYS A CG    1 
ATOM   793  C  CD    . LYS A 1 100 ? -4.201  3.829   -19.260 1.00 34.81 ?  99  LYS A CD    1 
ATOM   794  C  CE    . LYS A 1 100 ? -3.170  2.793   -18.904 1.00 37.45 ?  99  LYS A CE    1 
ATOM   795  N  NZ    . LYS A 1 100 ? -3.804  1.697   -18.125 1.00 38.77 1  99  LYS A NZ    1 
ATOM   796  N  N     . TRP A 1 101 ? -8.463  7.240   -18.046 1.00 27.27 ?  100 TRP A N     1 
ATOM   797  C  CA    . TRP A 1 101 ? -9.380  8.241   -18.577 1.00 29.20 ?  100 TRP A CA    1 
ATOM   798  C  C     . TRP A 1 101 ? -9.207  9.540   -17.820 1.00 28.81 ?  100 TRP A C     1 
ATOM   799  O  O     . TRP A 1 101 ? -9.138  10.627  -18.412 1.00 30.89 ?  100 TRP A O     1 
ATOM   800  C  CB    . TRP A 1 101 ? -10.839 7.803   -18.450 1.00 29.98 ?  100 TRP A CB    1 
ATOM   801  C  CG    . TRP A 1 101 ? -11.186 6.474   -18.992 1.00 31.03 ?  100 TRP A CG    1 
ATOM   802  C  CD1   . TRP A 1 101 ? -10.490 5.736   -19.917 1.00 30.96 ?  100 TRP A CD1   1 
ATOM   803  C  CD2   . TRP A 1 101 ? -12.326 5.699   -18.626 1.00 29.82 ?  100 TRP A CD2   1 
ATOM   804  N  NE1   . TRP A 1 101 ? -11.143 4.547   -20.144 1.00 30.87 ?  100 TRP A NE1   1 
ATOM   805  C  CE2   . TRP A 1 101 ? -12.271 4.500   -19.364 1.00 30.45 ?  100 TRP A CE2   1 
ATOM   806  C  CE3   . TRP A 1 101 ? -13.398 5.907   -17.751 1.00 29.69 ?  100 TRP A CE3   1 
ATOM   807  C  CZ2   . TRP A 1 101 ? -13.248 3.514   -19.253 1.00 28.79 ?  100 TRP A CZ2   1 
ATOM   808  C  CZ3   . TRP A 1 101 ? -14.359 4.931   -17.636 1.00 28.95 ?  100 TRP A CZ3   1 
ATOM   809  C  CH2   . TRP A 1 101 ? -14.279 3.743   -18.382 1.00 29.04 ?  100 TRP A CH2   1 
ATOM   810  N  N     . ILE A 1 102 ? -9.165  9.436   -16.493 1.00 29.39 ?  101 ILE A N     1 
ATOM   811  C  CA    . ILE A 1 102 ? -9.121  10.645  -15.673 1.00 28.55 ?  101 ILE A CA    1 
ATOM   812  C  C     . ILE A 1 102 ? -7.789  11.372  -15.859 1.00 32.69 ?  101 ILE A C     1 
ATOM   813  O  O     . ILE A 1 102 ? -7.748  12.600  -16.031 1.00 30.99 ?  101 ILE A O     1 
ATOM   814  C  CB    . ILE A 1 102 ? -9.377  10.299  -14.197 1.00 27.48 ?  101 ILE A CB    1 
ATOM   815  C  CG1   . ILE A 1 102 ? -10.721 9.559   -14.034 1.00 23.81 ?  101 ILE A CG1   1 
ATOM   816  C  CG2   . ILE A 1 102 ? -9.266  11.556  -13.316 1.00 25.05 ?  101 ILE A CG2   1 
ATOM   817  C  CD1   . ILE A 1 102 ? -11.916 10.260  -14.624 1.00 25.19 ?  101 ILE A CD1   1 
ATOM   818  N  N     . ARG A 1 103 ? -6.684  10.627  -15.844 1.00 33.95 ?  102 ARG A N     1 
ATOM   819  C  CA    . ARG A 1 103 ? -5.378  11.239  -16.090 1.00 38.48 ?  102 ARG A CA    1 
ATOM   820  C  C     . ARG A 1 103 ? -5.322  11.945  -17.443 1.00 39.00 ?  102 ARG A C     1 
ATOM   821  O  O     . ARG A 1 103 ? -4.885  13.099  -17.532 1.00 38.86 ?  102 ARG A O     1 
ATOM   822  C  CB    . ARG A 1 103 ? -4.273  10.195  -16.008 1.00 40.27 ?  102 ARG A CB    1 
ATOM   823  C  CG    . ARG A 1 103 ? -2.897  10.817  -16.185 1.00 43.51 ?  102 ARG A CG    1 
ATOM   824  C  CD    . ARG A 1 103 ? -1.885  9.791   -16.627 1.00 46.53 ?  102 ARG A CD    1 
ATOM   825  N  NE    . ARG A 1 103 ? -2.250  9.230   -17.920 1.00 48.31 ?  102 ARG A NE    1 
ATOM   826  C  CZ    . ARG A 1 103 ? -1.897  8.017   -18.324 1.00 50.36 ?  102 ARG A CZ    1 
ATOM   827  N  NH1   . ARG A 1 103 ? -1.178  7.233   -17.528 1.00 50.55 1  102 ARG A NH1   1 
ATOM   828  N  NH2   . ARG A 1 103 ? -2.275  7.589   -19.517 1.00 50.74 ?  102 ARG A NH2   1 
ATOM   829  N  N     . ASP A 1 104 ? -5.740  11.259  -18.515 1.00 37.73 ?  103 ASP A N     1 
ATOM   830  C  CA    . ASP A 1 104 ? -5.715  11.856  -19.846 1.00 38.12 ?  103 ASP A CA    1 
ATOM   831  C  C     . ASP A 1 104 ? -6.571  13.108  -19.911 1.00 37.14 ?  103 ASP A C     1 
ATOM   832  O  O     . ASP A 1 104 ? -6.226  14.068  -20.616 1.00 35.87 ?  103 ASP A O     1 
ATOM   833  C  CB    . ASP A 1 104 ? -6.196  10.843  -20.890 1.00 39.61 ?  103 ASP A CB    1 
ATOM   834  C  CG    . ASP A 1 104 ? -5.285  9.629   -20.997 1.00 41.57 ?  103 ASP A CG    1 
ATOM   835  O  OD1   . ASP A 1 104 ? -4.186  9.643   -20.394 1.00 42.29 ?  103 ASP A OD1   1 
ATOM   836  O  OD2   . ASP A 1 104 ? -5.678  8.660   -21.686 1.00 42.63 -1 103 ASP A OD2   1 
ATOM   837  N  N     . ALA A 1 105 ? -7.714  13.108  -19.208 1.00 35.63 ?  104 ALA A N     1 
ATOM   838  C  CA    . ALA A 1 105 ? -8.539  14.314  -19.173 1.00 35.31 ?  104 ALA A CA    1 
ATOM   839  C  C     . ALA A 1 105 ? -7.797  15.473  -18.518 1.00 37.17 ?  104 ALA A C     1 
ATOM   840  O  O     . ALA A 1 105 ? -8.030  16.641  -18.862 1.00 36.14 ?  104 ALA A O     1 
ATOM   841  C  CB    . ALA A 1 105 ? -9.844  14.035  -18.432 1.00 33.64 ?  104 ALA A CB    1 
ATOM   842  N  N     . LEU A 1 106 ? -6.908  15.164  -17.577 1.00 39.85 ?  105 LEU A N     1 
ATOM   843  C  CA    . LEU A 1 106 ? -6.061  16.135  -16.890 1.00 44.21 ?  105 LEU A CA    1 
ATOM   844  C  C     . LEU A 1 106 ? -4.638  16.099  -17.421 1.00 55.34 ?  105 LEU A C     1 
ATOM   845  O  O     . LEU A 1 106 ? -3.679  16.125  -16.644 1.00 57.07 ?  105 LEU A O     1 
ATOM   846  C  CB    . LEU A 1 106 ? -6.065  15.875  -15.388 1.00 38.06 ?  105 LEU A CB    1 
ATOM   847  C  CG    . LEU A 1 106 ? -7.377  15.995  -14.614 1.00 32.28 ?  105 LEU A CG    1 
ATOM   848  C  CD1   . LEU A 1 106 ? -7.228  15.321  -13.271 1.00 30.08 ?  105 LEU A CD1   1 
ATOM   849  C  CD2   . LEU A 1 106 ? -7.750  17.455  -14.436 1.00 30.91 ?  105 LEU A CD2   1 
ATOM   850  N  N     . LYS A 1 107 ? -4.469  15.995  -18.740 1.00 64.17 ?  106 LYS A N     1 
ATOM   851  C  CA    . LYS A 1 107 ? -3.124  16.005  -19.308 1.00 71.96 ?  106 LYS A CA    1 
ATOM   852  C  C     . LYS A 1 107 ? -2.525  17.400  -19.224 1.00 75.66 ?  106 LYS A C     1 
ATOM   853  O  O     . LYS A 1 107 ? -1.498  17.617  -18.568 1.00 75.95 ?  106 LYS A O     1 
ATOM   854  C  CB    . LYS A 1 107 ? -3.149  15.509  -20.760 1.00 74.86 ?  106 LYS A CB    1 
ATOM   855  C  CG    . LYS A 1 107 ? -2.889  14.012  -20.915 1.00 77.37 ?  106 LYS A CG    1 
ATOM   856  C  CD    . LYS A 1 107 ? -2.970  13.551  -22.371 1.00 79.67 ?  106 LYS A CD    1 
ATOM   857  C  CE    . LYS A 1 107 ? -1.719  13.919  -23.162 1.00 81.17 ?  106 LYS A CE    1 
ATOM   858  N  NZ    . LYS A 1 107 ? -1.685  13.248  -24.494 1.00 81.70 1  106 LYS A NZ    1 
ATOM   859  N  N     . ASP A 1 108 ? -3.179  18.367  -19.861 1.00 78.63 ?  107 ASP A N     1 
ATOM   860  C  CA    . ASP A 1 108 ? -2.695  19.735  -19.931 1.00 81.27 ?  107 ASP A CA    1 
ATOM   861  C  C     . ASP A 1 108 ? -3.221  20.607  -18.793 1.00 76.48 ?  107 ASP A C     1 
ATOM   862  O  O     . ASP A 1 108 ? -3.219  21.838  -18.913 1.00 77.49 ?  107 ASP A O     1 
ATOM   863  C  CB    . ASP A 1 108 ? -3.056  20.341  -21.291 1.00 88.14 ?  107 ASP A CB    1 
ATOM   864  C  CG    . ASP A 1 108 ? -2.511  19.523  -22.456 1.00 93.11 ?  107 ASP A CG    1 
ATOM   865  O  OD1   . ASP A 1 108 ? -1.561  18.736  -22.249 1.00 94.97 ?  107 ASP A OD1   1 
ATOM   866  O  OD2   . ASP A 1 108 ? -3.032  19.666  -23.580 1.00 94.83 -1 107 ASP A OD2   1 
ATOM   867  N  N     . TYR A 1 109 ? -3.670  20.002  -17.697 1.00 69.16 ?  108 TYR A N     1 
ATOM   868  C  CA    . TYR A 1 109 ? -4.103  20.745  -16.523 1.00 61.02 ?  108 TYR A CA    1 
ATOM   869  C  C     . TYR A 1 109 ? -2.950  20.845  -15.540 1.00 61.10 ?  108 TYR A C     1 
ATOM   870  O  O     . TYR A 1 109 ? -2.378  19.821  -15.147 1.00 60.16 ?  108 TYR A O     1 
ATOM   871  C  CB    . TYR A 1 109 ? -5.299  20.090  -15.831 1.00 52.28 ?  108 TYR A CB    1 
ATOM   872  C  CG    . TYR A 1 109 ? -5.776  20.906  -14.650 1.00 44.40 ?  108 TYR A CG    1 
ATOM   873  C  CD1   . TYR A 1 109 ? -6.633  21.976  -14.834 1.00 41.18 ?  108 TYR A CD1   1 
ATOM   874  C  CD2   . TYR A 1 109 ? -5.342  20.632  -13.360 1.00 41.55 ?  108 TYR A CD2   1 
ATOM   875  C  CE1   . TYR A 1 109 ? -7.066  22.741  -13.770 1.00 39.47 ?  108 TYR A CE1   1 
ATOM   876  C  CE2   . TYR A 1 109 ? -5.761  21.400  -12.284 1.00 38.94 ?  108 TYR A CE2   1 
ATOM   877  C  CZ    . TYR A 1 109 ? -6.627  22.453  -12.494 1.00 38.39 ?  108 TYR A CZ    1 
ATOM   878  O  OH    . TYR A 1 109 ? -7.078  23.228  -11.444 1.00 36.93 ?  108 TYR A OH    1 
ATOM   879  N  N     . GLY A 1 110 ? -2.638  22.072  -15.127 1.00 62.97 ?  109 GLY A N     1 
ATOM   880  C  CA    . GLY A 1 110 ? -1.558  22.285  -14.177 1.00 65.73 ?  109 GLY A CA    1 
ATOM   881  C  C     . GLY A 1 110 ? -0.305  21.539  -14.583 1.00 69.44 ?  109 GLY A C     1 
ATOM   882  O  O     . GLY A 1 110 ? 0.089   21.528  -15.756 1.00 69.59 ?  109 GLY A O     1 
ATOM   883  N  N     . ASN A 1 111 ? 0.322   20.876  -13.608 1.00 72.28 ?  110 ASN A N     1 
ATOM   884  C  CA    . ASN A 1 111 ? 1.543   20.114  -13.836 1.00 75.22 ?  110 ASN A CA    1 
ATOM   885  C  C     . ASN A 1 111 ? 1.269   18.677  -14.240 1.00 76.52 ?  110 ASN A C     1 
ATOM   886  O  O     . ASN A 1 111 ? 2.075   17.786  -13.931 1.00 76.84 ?  110 ASN A O     1 
ATOM   887  C  CB    . ASN A 1 111 ? 2.427   20.149  -12.592 1.00 75.40 ?  110 ASN A CB    1 
ATOM   888  C  CG    . ASN A 1 111 ? 2.822   21.549  -12.208 1.00 75.70 ?  110 ASN A CG    1 
ATOM   889  O  OD1   . ASN A 1 111 ? 2.271   22.523  -12.722 1.00 75.88 ?  110 ASN A OD1   1 
ATOM   890  N  ND2   . ASN A 1 111 ? 3.778   21.665  -11.295 1.00 75.92 ?  110 ASN A ND2   1 
ATOM   891  N  N     . GLY A 1 112 ? 0.148   18.425  -14.916 1.00 79.89 ?  111 GLY A N     1 
ATOM   892  C  CA    . GLY A 1 112 ? -0.198  17.088  -15.355 1.00 77.32 ?  111 GLY A CA    1 
ATOM   893  C  C     . GLY A 1 112 ? -0.567  16.146  -14.225 1.00 72.48 ?  111 GLY A C     1 
ATOM   894  O  O     . GLY A 1 112 ? -0.117  16.307  -13.084 1.00 73.59 ?  111 GLY A O     1 
ATOM   895  N  N     . ALA A 1 113 ? -1.383  15.148  -14.540 1.00 65.48 ?  112 ALA A N     1 
ATOM   896  C  CA    . ALA A 1 113 ? -1.831  14.176  -13.556 1.00 57.40 ?  112 ALA A CA    1 
ATOM   897  C  C     . ALA A 1 113 ? -0.854  13.009  -13.462 1.00 48.97 ?  112 ALA A C     1 
ATOM   898  O  O     . ALA A 1 113 ? 0.079   12.873  -14.250 1.00 47.57 ?  112 ALA A O     1 
ATOM   899  C  CB    . ALA A 1 113 ? -3.231  13.665  -13.901 1.00 57.18 ?  112 ALA A CB    1 
ATOM   900  N  N     . GLU A 1 114 ? -1.091  12.156  -12.477 1.00 42.92 ?  113 GLU A N     1 
ATOM   901  C  CA    . GLU A 1 114 ? -0.266  10.986  -12.220 1.00 38.84 ?  113 GLU A CA    1 
ATOM   902  C  C     . GLU A 1 114 ? -1.140  9.911   -11.597 1.00 33.83 ?  113 GLU A C     1 
ATOM   903  O  O     . GLU A 1 114 ? -1.872  10.181  -10.636 1.00 33.23 ?  113 GLU A O     1 
ATOM   904  C  CB    . GLU A 1 114 ? 0.890   11.338  -11.286 1.00 40.71 ?  113 GLU A CB    1 
ATOM   905  C  CG    . GLU A 1 114 ? 1.800   10.182  -10.925 1.00 44.11 ?  113 GLU A CG    1 
ATOM   906  C  CD    . GLU A 1 114 ? 2.990   10.639  -10.097 1.00 47.93 ?  113 GLU A CD    1 
ATOM   907  O  OE1   . GLU A 1 114 ? 3.200   10.088  -8.988  1.00 49.31 ?  113 GLU A OE1   1 
ATOM   908  O  OE2   . GLU A 1 114 ? 3.699   11.562  -10.559 1.00 49.15 -1 113 GLU A OE2   1 
ATOM   909  N  N     . ILE A 1 115 ? -1.074  8.700   -12.133 1.00 29.26 ?  114 ILE A N     1 
ATOM   910  C  CA    . ILE A 1 115 ? -1.920  7.609   -11.659 1.00 27.65 ?  114 ILE A CA    1 
ATOM   911  C  C     . ILE A 1 115 ? -1.183  6.954   -10.502 1.00 27.37 ?  114 ILE A C     1 
ATOM   912  O  O     . ILE A 1 115 ? -0.093  6.409   -10.678 1.00 27.59 ?  114 ILE A O     1 
ATOM   913  C  CB    . ILE A 1 115 ? -2.238  6.598   -12.771 1.00 25.95 ?  114 ILE A CB    1 
ATOM   914  C  CG1   . ILE A 1 115 ? -3.135  7.240   -13.830 1.00 26.64 ?  114 ILE A CG1   1 
ATOM   915  C  CG2   . ILE A 1 115 ? -2.902  5.373   -12.211 1.00 27.07 ?  114 ILE A CG2   1 
ATOM   916  C  CD1   . ILE A 1 115 ? -3.564  6.285   -14.950 1.00 25.48 ?  114 ILE A CD1   1 
ATOM   917  N  N     . ARG A 1 116 ? -1.734  7.075   -9.301  1.00 26.87 ?  115 ARG A N     1 
ATOM   918  C  CA    . ARG A 1 116 ? -1.204  6.412   -8.125  1.00 29.11 ?  115 ARG A CA    1 
ATOM   919  C  C     . ARG A 1 116 ? -2.141  5.288   -7.728  1.00 27.18 ?  115 ARG A C     1 
ATOM   920  O  O     . ARG A 1 116 ? -3.314  5.242   -8.121  1.00 30.81 ?  115 ARG A O     1 
ATOM   921  C  CB    . ARG A 1 116 ? -1.032  7.397   -6.951  1.00 34.68 ?  115 ARG A CB    1 
ATOM   922  C  CG    . ARG A 1 116 ? -0.179  8.614   -7.274  1.00 39.90 ?  115 ARG A CG    1 
ATOM   923  C  CD    . ARG A 1 116 ? 0.546   9.162   -6.046  1.00 45.89 ?  115 ARG A CD    1 
ATOM   924  N  NE    . ARG A 1 116 ? -0.338  9.905   -5.154  1.00 52.16 ?  115 ARG A NE    1 
ATOM   925  C  CZ    . ARG A 1 116 ? 0.070   10.862  -4.325  1.00 55.68 ?  115 ARG A CZ    1 
ATOM   926  N  NH1   . ARG A 1 116 ? 1.352   11.196  -4.289  1.00 57.68 1  115 ARG A NH1   1 
ATOM   927  N  NH2   . ARG A 1 116 ? -0.800  11.492  -3.544  1.00 57.11 ?  115 ARG A NH2   1 
ATOM   928  N  N     . ARG A 1 117 ? -1.633  4.421   -6.862  1.00 23.20 ?  116 ARG A N     1 
ATOM   929  C  CA    . ARG A 1 117 ? -2.321  3.170   -6.590  1.00 21.08 ?  116 ARG A CA    1 
ATOM   930  C  C     . ARG A 1 117 ? -3.778  3.334   -6.176  1.00 22.71 ?  116 ARG A C     1 
ATOM   931  O  O     . ARG A 1 117 ? -4.615  2.468   -6.477  1.00 22.01 ?  116 ARG A O     1 
ATOM   932  C  CB    . ARG A 1 117 ? -1.583  2.396   -5.508  1.00 19.53 ?  116 ARG A CB    1 
ATOM   933  C  CG    . ARG A 1 117 ? -2.275  1.076   -5.205  1.00 23.86 ?  116 ARG A CG    1 
ATOM   934  C  CD    . ARG A 1 117 ? -1.593  0.245   -4.106  1.00 27.41 ?  116 ARG A CD    1 
ATOM   935  N  NE    . ARG A 1 117 ? -0.193  0.020   -4.450  1.00 32.84 ?  116 ARG A NE    1 
ATOM   936  C  CZ    . ARG A 1 117 ? 0.240   -0.931  -5.281  1.00 37.11 ?  116 ARG A CZ    1 
ATOM   937  N  NH1   . ARG A 1 117 ? -0.612  -1.777  -5.855  1.00 37.40 1  116 ARG A NH1   1 
ATOM   938  N  NH2   . ARG A 1 117 ? 1.535   -1.037  -5.541  1.00 38.78 ?  116 ARG A NH2   1 
ATOM   939  N  N     . SER A 1 118 ? -4.099  4.402   -5.442  1.00 21.54 ?  117 SER A N     1 
ATOM   940  C  CA    . SER A 1 118 ? -5.443  4.573   -4.935  1.00 18.86 ?  117 SER A CA    1 
ATOM   941  C  C     . SER A 1 118 ? -6.112  5.841   -5.426  1.00 18.41 ?  117 SER A C     1 
ATOM   942  O  O     . SER A 1 118 ? -7.245  6.107   -4.994  1.00 21.44 ?  117 SER A O     1 
ATOM   943  C  CB    . SER A 1 118 ? -5.442  4.552   -3.397  1.00 25.77 ?  117 SER A CB    1 
ATOM   944  O  OG    . SER A 1 118 ? -5.190  3.260   -2.854  1.00 29.49 ?  117 SER A OG    1 
ATOM   945  N  N     . CYS A 1 119 ? -5.483  6.609   -6.315  1.00 18.47 ?  118 CYS A N     1 
ATOM   946  C  CA    . CYS A 1 119 ? -6.088  7.863   -6.760  1.00 21.43 ?  118 CYS A CA    1 
ATOM   947  C  C     . CYS A 1 119 ? -5.341  8.348   -7.997  1.00 20.01 ?  118 CYS A C     1 
ATOM   948  O  O     . CYS A 1 119 ? -4.273  7.845   -8.332  1.00 23.68 ?  118 CYS A O     1 
ATOM   949  C  CB    . CYS A 1 119 ? -6.056  8.921   -5.630  1.00 18.49 ?  118 CYS A CB    1 
ATOM   950  S  SG    . CYS A 1 119 ? -4.361  9.443   -5.045  1.00 21.87 ?  118 CYS A SG    1 
ATOM   951  N  N     . VAL A 1 120 ? -5.925  9.312   -8.688  1.00 24.33 ?  119 VAL A N     1 
ATOM   952  C  CA    . VAL A 1 120 ? -5.199  10.128  -9.652  1.00 25.83 ?  119 VAL A CA    1 
ATOM   953  C  C     . VAL A 1 120 ? -4.838  11.430  -8.953  1.00 25.29 ?  119 VAL A C     1 
ATOM   954  O  O     . VAL A 1 120 ? -5.709  12.085  -8.380  1.00 25.34 ?  119 VAL A O     1 
ATOM   955  C  CB    . VAL A 1 120 ? -6.041  10.384  -10.912 1.00 29.82 ?  119 VAL A CB    1 
ATOM   956  C  CG1   . VAL A 1 120 ? -5.290  11.275  -11.889 1.00 32.76 ?  119 VAL A CG1   1 
ATOM   957  C  CG2   . VAL A 1 120 ? -6.448  9.062   -11.550 1.00 30.64 ?  119 VAL A CG2   1 
ATOM   958  N  N     . THR A 1 121 ? -3.568  11.808  -8.981  1.00 24.69 ?  120 THR A N     1 
ATOM   959  C  CA    . THR A 1 121 ? -3.102  13.007  -8.293  1.00 24.99 ?  120 THR A CA    1 
ATOM   960  C  C     . THR A 1 121 ? -2.682  14.038  -9.324  1.00 25.26 ?  120 THR A C     1 
ATOM   961  O  O     . THR A 1 121 ? -1.888  13.730  -10.216 1.00 27.70 ?  120 THR A O     1 
ATOM   962  C  CB    . THR A 1 121 ? -1.924  12.691  -7.364  1.00 26.22 ?  120 THR A CB    1 
ATOM   963  O  OG1   . THR A 1 121 ? -2.348  11.776  -6.352  1.00 27.68 ?  120 THR A OG1   1 
ATOM   964  C  CG2   . THR A 1 121 ? -1.424  13.944  -6.686  1.00 24.83 ?  120 THR A CG2   1 
ATOM   965  N  N     . VAL A 1 122 ? -3.219  15.240  -9.228  1.00 26.69 ?  121 VAL A N     1 
ATOM   966  C  CA    . VAL A 1 122 ? -2.820  16.321  -10.122 1.00 29.58 ?  121 VAL A CA    1 
ATOM   967  C  C     . VAL A 1 122 ? -2.098  17.383  -9.298  1.00 29.13 ?  121 VAL A C     1 
ATOM   968  O  O     . VAL A 1 122 ? -2.534  17.753  -8.201  1.00 25.39 ?  121 VAL A O     1 
ATOM   969  C  CB    . VAL A 1 122 ? -4.018  16.885  -10.922 1.00 33.64 ?  121 VAL A CB    1 
ATOM   970  C  CG1   . VAL A 1 122 ? -5.074  17.474  -10.025 1.00 35.03 ?  121 VAL A CG1   1 
ATOM   971  C  CG2   . VAL A 1 122 ? -3.554  17.900  -11.964 1.00 35.02 ?  121 VAL A CG2   1 
ATOM   972  N  N     . PHE A 1 123 ? -0.958  17.835  -9.808  1.00 30.66 ?  122 PHE A N     1 
ATOM   973  C  CA    . PHE A 1 123 ? -0.073  18.731  -9.078  1.00 31.59 ?  122 PHE A CA    1 
ATOM   974  C  C     . PHE A 1 123 ? -0.217  20.159  -9.582  1.00 36.11 ?  122 PHE A C     1 
ATOM   975  O  O     . PHE A 1 123 ? -0.270  20.398  -10.793 1.00 32.87 ?  122 PHE A O     1 
ATOM   976  C  CB    . PHE A 1 123 ? 1.371   18.265  -9.218  1.00 32.51 ?  122 PHE A CB    1 
ATOM   977  C  CG    . PHE A 1 123 ? 1.589   16.873  -8.747  1.00 34.21 ?  122 PHE A CG    1 
ATOM   978  C  CD1   . PHE A 1 123 ? 1.914   16.620  -7.432  1.00 35.15 ?  122 PHE A CD1   1 
ATOM   979  C  CD2   . PHE A 1 123 ? 1.453   15.803  -9.617  1.00 36.24 ?  122 PHE A CD2   1 
ATOM   980  C  CE1   . PHE A 1 123 ? 2.123   15.336  -6.989  1.00 35.81 ?  122 PHE A CE1   1 
ATOM   981  C  CE2   . PHE A 1 123 ? 1.654   14.512  -9.176  1.00 36.45 ?  122 PHE A CE2   1 
ATOM   982  C  CZ    . PHE A 1 123 ? 1.990   14.284  -7.855  1.00 36.11 ?  122 PHE A CZ    1 
ATOM   983  N  N     . LYS A 1 124 ? -0.285  21.104  -8.655  1.00 38.25 ?  123 LYS A N     1 
ATOM   984  C  CA    . LYS A 1 124 ? -0.372  22.516  -8.971  1.00 43.55 ?  123 LYS A CA    1 
ATOM   985  C  C     . LYS A 1 124 ? 0.485   23.249  -7.957  1.00 43.62 ?  123 LYS A C     1 
ATOM   986  O  O     . LYS A 1 124 ? 0.877   22.668  -6.935  1.00 44.66 ?  123 LYS A O     1 
ATOM   987  C  CB    . LYS A 1 124 ? -1.825  23.021  -8.954  1.00 46.32 ?  123 LYS A CB    1 
ATOM   988  C  CG    . LYS A 1 124 ? -2.621  22.603  -10.206 1.00 49.94 ?  123 LYS A CG    1 
ATOM   989  C  CD    . LYS A 1 124 ? -3.528  23.716  -10.733 1.00 53.19 ?  123 LYS A CD    1 
ATOM   990  C  CE    . LYS A 1 124 ? -2.732  24.924  -11.229 1.00 56.03 ?  123 LYS A CE    1 
ATOM   991  N  NZ    . LYS A 1 124 ? -3.610  26.007  -11.779 1.00 56.75 1  123 LYS A NZ    1 
ATOM   992  N  N     . PRO A 1 125 ? 0.842   24.512  -8.231  1.00 44.93 ?  124 PRO A N     1 
ATOM   993  C  CA    . PRO A 1 125 ? 1.730   25.237  -7.316  1.00 42.96 ?  124 PRO A CA    1 
ATOM   994  C  C     . PRO A 1 125 ? 1.230   25.226  -5.888  1.00 37.63 ?  124 PRO A C     1 
ATOM   995  O  O     . PRO A 1 125 ? 0.192   25.814  -5.581  1.00 37.12 ?  124 PRO A O     1 
ATOM   996  C  CB    . PRO A 1 125 ? 1.743   26.659  -7.892  1.00 46.95 ?  124 PRO A CB    1 
ATOM   997  C  CG    . PRO A 1 125 ? 1.538   26.455  -9.346  1.00 50.65 ?  124 PRO A CG    1 
ATOM   998  C  CD    . PRO A 1 125 ? 0.594   25.279  -9.467  1.00 49.63 ?  124 PRO A CD    1 
ATOM   999  N  N     . GLY A 1 126 ? 1.953   24.532  -5.017  1.00 32.82 ?  125 GLY A N     1 
ATOM   1000 C  CA    . GLY A 1 126 ? 1.650   24.569  -3.601  1.00 28.62 ?  125 GLY A CA    1 
ATOM   1001 C  C     . GLY A 1 126 ? 0.592   23.600  -3.122  1.00 25.89 ?  125 GLY A C     1 
ATOM   1002 O  O     . GLY A 1 126 ? 0.274   23.612  -1.920  1.00 23.45 ?  125 GLY A O     1 
ATOM   1003 N  N     . TYR A 1 127 ? 0.040   22.757  -3.994  1.00 23.94 ?  126 TYR A N     1 
ATOM   1004 C  CA    . TYR A 1 127 ? -0.935  21.770  -3.526  1.00 23.88 ?  126 TYR A CA    1 
ATOM   1005 C  C     . TYR A 1 127 ? -1.138  20.702  -4.588  1.00 22.89 ?  126 TYR A C     1 
ATOM   1006 O  O     . TYR A 1 127 ? -0.819  20.892  -5.767  1.00 23.95 ?  126 TYR A O     1 
ATOM   1007 C  CB    . TYR A 1 127 ? -2.281  22.418  -3.166  1.00 26.55 ?  126 TYR A CB    1 
ATOM   1008 C  CG    . TYR A 1 127 ? -3.050  22.934  -4.374  1.00 31.29 ?  126 TYR A CG    1 
ATOM   1009 C  CD1   . TYR A 1 127 ? -2.833  24.226  -4.861  1.00 32.44 ?  126 TYR A CD1   1 
ATOM   1010 C  CD2   . TYR A 1 127 ? -3.983  22.132  -5.027  1.00 32.11 ?  126 TYR A CD2   1 
ATOM   1011 C  CE1   . TYR A 1 127 ? -3.533  24.709  -5.967  1.00 34.16 ?  126 TYR A CE1   1 
ATOM   1012 C  CE2   . TYR A 1 127 ? -4.691  22.604  -6.136  1.00 34.69 ?  126 TYR A CE2   1 
ATOM   1013 C  CZ    . TYR A 1 127 ? -4.461  23.887  -6.601  1.00 36.04 ?  126 TYR A CZ    1 
ATOM   1014 O  OH    . TYR A 1 127 ? -5.160  24.356  -7.694  1.00 37.55 ?  126 TYR A OH    1 
ATOM   1015 N  N     . HIS A 1 128 ? -1.676  19.566  -4.156  1.00 19.45 ?  127 HIS A N     1 
ATOM   1016 C  CA    . HIS A 1 128 ? -2.065  18.549  -5.113  1.00 21.54 ?  127 HIS A CA    1 
ATOM   1017 C  C     . HIS A 1 128 ? -3.486  18.136  -4.799  1.00 18.87 ?  127 HIS A C     1 
ATOM   1018 O  O     . HIS A 1 128 ? -4.004  18.365  -3.698  1.00 19.06 ?  127 HIS A O     1 
ATOM   1019 C  CB    . HIS A 1 128 ? -1.128  17.330  -5.134  1.00 22.61 ?  127 HIS A CB    1 
ATOM   1020 C  CG    . HIS A 1 128 ? -0.927  16.681  -3.800  1.00 27.01 ?  127 HIS A CG    1 
ATOM   1021 N  ND1   . HIS A 1 128 ? 0.032   17.100  -2.900  1.00 27.77 ?  127 HIS A ND1   1 
ATOM   1022 C  CD2   . HIS A 1 128 ? -1.549  15.625  -3.222  1.00 26.67 ?  127 HIS A CD2   1 
ATOM   1023 C  CE1   . HIS A 1 128 ? -0.012  16.334  -1.826  1.00 27.00 ?  127 HIS A CE1   1 
ATOM   1024 N  NE2   . HIS A 1 128 ? -0.966  15.436  -1.993  1.00 27.07 ?  127 HIS A NE2   1 
ATOM   1025 N  N     . VAL A 1 129 ? -4.116  17.546  -5.805  1.00 18.89 ?  128 VAL A N     1 
ATOM   1026 C  CA    . VAL A 1 129 ? -5.487  17.090  -5.698  1.00 18.55 ?  128 VAL A CA    1 
ATOM   1027 C  C     . VAL A 1 129 ? -5.472  15.586  -5.889  1.00 19.17 ?  128 VAL A C     1 
ATOM   1028 O  O     . VAL A 1 129 ? -5.018  15.098  -6.935  1.00 21.01 ?  128 VAL A O     1 
ATOM   1029 C  CB    . VAL A 1 129 ? -6.391  17.763  -6.731  1.00 18.99 ?  128 VAL A CB    1 
ATOM   1030 C  CG1   . VAL A 1 129 ? -7.768  17.123  -6.665  1.00 18.44 ?  128 VAL A CG1   1 
ATOM   1031 C  CG2   . VAL A 1 129 ? -6.382  19.293  -6.546  1.00 20.45 ?  128 VAL A CG2   1 
ATOM   1032 N  N     . ASP A 1 130 ? -5.947  14.856  -4.872  1.00 16.04 ?  129 ASP A N     1 
ATOM   1033 C  CA    . ASP A 1 130 ? -5.981  13.392  -4.847  1.00 15.87 ?  129 ASP A CA    1 
ATOM   1034 C  C     . ASP A 1 130 ? -7.418  12.982  -5.184  1.00 16.98 ?  129 ASP A C     1 
ATOM   1035 O  O     . ASP A 1 130 ? -8.311  13.063  -4.341  1.00 14.51 ?  129 ASP A O     1 
ATOM   1036 C  CB    . ASP A 1 130 ? -5.575  12.837  -3.480  1.00 19.34 ?  129 ASP A CB    1 
ATOM   1037 C  CG    . ASP A 1 130 ? -4.117  13.133  -3.109  1.00 22.32 ?  129 ASP A CG    1 
ATOM   1038 O  OD1   . ASP A 1 130 ? -3.308  13.350  -4.027  1.00 22.01 ?  129 ASP A OD1   1 
ATOM   1039 O  OD2   . ASP A 1 130 ? -3.796  13.154  -1.898  1.00 23.60 -1 129 ASP A OD2   1 
ATOM   1040 N  N     . LEU A 1 131 ? -7.649  12.510  -6.419  1.00 18.88 ?  130 LEU A N     1 
ATOM   1041 C  CA    . LEU A 1 131 ? -8.974  12.110  -6.873  1.00 23.86 ?  130 LEU A CA    1 
ATOM   1042 C  C     . LEU A 1 131 ? -9.072  10.604  -6.725  1.00 20.09 ?  130 LEU A C     1 
ATOM   1043 O  O     . LEU A 1 131 ? -8.439  9.870   -7.473  1.00 23.71 ?  130 LEU A O     1 
ATOM   1044 C  CB    . LEU A 1 131 ? -9.193  12.501  -8.332  1.00 29.63 ?  130 LEU A CB    1 
ATOM   1045 C  CG    . LEU A 1 131 ? -9.020  13.949  -8.761  1.00 35.95 ?  130 LEU A CG    1 
ATOM   1046 C  CD1   . LEU A 1 131 ? -8.226  13.990  -10.040 1.00 42.01 ?  130 LEU A CD1   1 
ATOM   1047 C  CD2   . LEU A 1 131 ? -10.364 14.617  -8.972  1.00 38.17 ?  130 LEU A CD2   1 
ATOM   1048 N  N     . ALA A 1 132 ? -9.856  10.145  -5.773  1.00 19.34 ?  131 ALA A N     1 
ATOM   1049 C  CA    . ALA A 1 132 ? -10.138 8.732   -5.640  1.00 18.43 ?  131 ALA A CA    1 
ATOM   1050 C  C     . ALA A 1 132 ? -11.280 8.402   -6.610  1.00 17.74 ?  131 ALA A C     1 
ATOM   1051 O  O     . ALA A 1 132 ? -12.264 9.143   -6.692  1.00 18.37 ?  131 ALA A O     1 
ATOM   1052 C  CB    . ALA A 1 132 ? -10.528 8.397   -4.206  1.00 20.04 ?  131 ALA A CB    1 
ATOM   1053 N  N     . VAL A 1 133 ? -11.135 7.322   -7.375  1.00 19.94 ?  132 VAL A N     1 
ATOM   1054 C  CA    . VAL A 1 133 ? -12.033 7.034   -8.490  1.00 19.02 ?  132 VAL A CA    1 
ATOM   1055 C  C     . VAL A 1 133 ? -12.838 5.789   -8.149  1.00 16.28 ?  132 VAL A C     1 
ATOM   1056 O  O     . VAL A 1 133 ? -12.266 4.753   -7.801  1.00 16.60 ?  132 VAL A O     1 
ATOM   1057 C  CB    . VAL A 1 133 ? -11.240 6.858   -9.799  1.00 18.25 ?  132 VAL A CB    1 
ATOM   1058 C  CG1   . VAL A 1 133 ? -12.160 6.367   -10.928 1.00 17.71 ?  132 VAL A CG1   1 
ATOM   1059 C  CG2   . VAL A 1 133 ? -10.573 8.180   -10.174 1.00 18.65 ?  132 VAL A CG2   1 
ATOM   1060 N  N     . TYR A 1 134 ? -14.177 5.889   -8.247  1.00 17.14 ?  133 TYR A N     1 
ATOM   1061 C  CA    . TYR A 1 134 ? -15.060 4.802   -7.859  1.00 16.09 ?  133 TYR A CA    1 
ATOM   1062 C  C     . TYR A 1 134 ? -15.992 4.454   -9.011  1.00 16.68 ?  133 TYR A C     1 
ATOM   1063 O  O     . TYR A 1 134 ? -16.321 5.311   -9.841  1.00 21.09 ?  133 TYR A O     1 
ATOM   1064 C  CB    . TYR A 1 134 ? -15.941 5.173   -6.665  1.00 16.37 ?  133 TYR A CB    1 
ATOM   1065 C  CG    . TYR A 1 134 ? -15.176 5.629   -5.448  1.00 15.61 ?  133 TYR A CG    1 
ATOM   1066 C  CD1   . TYR A 1 134 ? -14.718 6.921   -5.361  1.00 15.01 ?  133 TYR A CD1   1 
ATOM   1067 C  CD2   . TYR A 1 134 ? -14.924 4.758   -4.403  1.00 13.72 ?  133 TYR A CD2   1 
ATOM   1068 C  CE1   . TYR A 1 134 ? -14.025 7.361   -4.238  1.00 18.48 ?  133 TYR A CE1   1 
ATOM   1069 C  CE2   . TYR A 1 134 ? -14.220 5.211   -3.243  1.00 17.97 ?  133 TYR A CE2   1 
ATOM   1070 C  CZ    . TYR A 1 134 ? -13.787 6.502   -3.205  1.00 16.29 ?  133 TYR A CZ    1 
ATOM   1071 O  OH    . TYR A 1 134 ? -13.074 6.968   -2.088  1.00 18.75 ?  133 TYR A OH    1 
ATOM   1072 N  N     . ALA A 1 135 ? -16.445 3.207   -9.020  1.00 17.71 ?  134 ALA A N     1 
ATOM   1073 C  CA    . ALA A 1 135 ? -17.510 2.779   -9.929  1.00 18.06 ?  134 ALA A CA    1 
ATOM   1074 C  C     . ALA A 1 135 ? -18.865 2.996   -9.282  1.00 19.35 ?  134 ALA A C     1 
ATOM   1075 O  O     . ALA A 1 135 ? -18.981 3.080   -8.062  1.00 20.05 ?  134 ALA A O     1 
ATOM   1076 C  CB    . ALA A 1 135 ? -17.351 1.309   -10.298 1.00 19.80 ?  134 ALA A CB    1 
ATOM   1077 N  N     . ASP A 1 136 ? -19.896 3.066   -10.119 1.00 20.98 ?  135 ASP A N     1 
ATOM   1078 C  CA    . ASP A 1 136 ? -21.257 3.326   -9.652  1.00 23.04 ?  135 ASP A CA    1 
ATOM   1079 C  C     . ASP A 1 136 ? -21.817 2.122   -8.895  1.00 22.82 ?  135 ASP A C     1 
ATOM   1080 O  O     . ASP A 1 136 ? -21.888 1.028   -9.464  1.00 23.01 ?  135 ASP A O     1 
ATOM   1081 C  CB    . ASP A 1 136 ? -22.158 3.652   -10.840 1.00 27.35 ?  135 ASP A CB    1 
ATOM   1082 C  CG    . ASP A 1 136 ? -23.508 4.227   -10.415 1.00 31.13 ?  135 ASP A CG    1 
ATOM   1083 O  OD1   . ASP A 1 136 ? -23.992 3.928   -9.311  1.00 32.11 ?  135 ASP A OD1   1 
ATOM   1084 O  OD2   . ASP A 1 136 ? -24.093 4.999   -11.199 1.00 34.84 -1 135 ASP A OD2   1 
ATOM   1085 N  N     . PRO A 1 137 ? -22.245 2.274   -7.635  1.00 18.75 ?  136 PRO A N     1 
ATOM   1086 C  CA    . PRO A 1 137 ? -22.831 1.122   -6.938  1.00 19.73 ?  136 PRO A CA    1 
ATOM   1087 C  C     . PRO A 1 137 ? -24.049 0.549   -7.652  1.00 23.92 ?  136 PRO A C     1 
ATOM   1088 O  O     . PRO A 1 137 ? -24.263 -0.668  -7.617  1.00 26.33 ?  136 PRO A O     1 
ATOM   1089 C  CB    . PRO A 1 137 ? -23.205 1.701   -5.558  1.00 20.60 ?  136 PRO A CB    1 
ATOM   1090 C  CG    . PRO A 1 137 ? -22.295 2.831   -5.371  1.00 18.54 ?  136 PRO A CG    1 
ATOM   1091 C  CD    . PRO A 1 137 ? -22.039 3.420   -6.730  1.00 19.31 ?  136 PRO A CD    1 
ATOM   1092 N  N     . GLU A 1 138 ? -24.858 1.402   -8.284  1.00 27.38 ?  137 GLU A N     1 
ATOM   1093 C  CA    . GLU A 1 138 ? -26.075 0.925   -8.931  1.00 32.69 ?  137 GLU A CA    1 
ATOM   1094 C  C     . GLU A 1 138 ? -25.742 -0.037  -10.063 1.00 29.72 ?  137 GLU A C     1 
ATOM   1095 O  O     . GLU A 1 138 ? -26.371 -1.087  -10.204 1.00 30.64 ?  137 GLU A O     1 
ATOM   1096 C  CB    . GLU A 1 138 ? -26.883 2.113   -9.453  1.00 40.33 ?  137 GLU A CB    1 
ATOM   1097 C  CG    . GLU A 1 138 ? -28.375 1.885   -9.454  1.00 48.63 ?  137 GLU A CG    1 
ATOM   1098 C  CD    . GLU A 1 138 ? -28.908 1.602   -8.064  1.00 53.83 ?  137 GLU A CD    1 
ATOM   1099 O  OE1   . GLU A 1 138 ? -28.416 2.236   -7.110  1.00 55.40 ?  137 GLU A OE1   1 
ATOM   1100 O  OE2   . GLU A 1 138 ? -29.805 0.739   -7.927  1.00 56.06 -1 137 GLU A OE2   1 
ATOM   1101 N  N     . LEU A 1 139 ? -24.738 0.296   -10.861 1.00 26.42 ?  138 LEU A N     1 
ATOM   1102 C  CA    . LEU A 1 139 ? -24.335 -0.541  -11.981 1.00 25.93 ?  138 LEU A CA    1 
ATOM   1103 C  C     . LEU A 1 139 ? -23.393 -1.656  -11.566 1.00 27.29 ?  138 LEU A C     1 
ATOM   1104 O  O     . LEU A 1 139 ? -23.103 -2.534  -12.380 1.00 29.02 ?  138 LEU A O     1 
ATOM   1105 C  CB    . LEU A 1 139 ? -23.659 0.323   -13.054 1.00 25.88 ?  138 LEU A CB    1 
ATOM   1106 C  CG    . LEU A 1 139 ? -24.424 1.582   -13.479 1.00 24.83 ?  138 LEU A CG    1 
ATOM   1107 C  CD1   . LEU A 1 139 ? -23.572 2.442   -14.398 1.00 24.95 ?  138 LEU A CD1   1 
ATOM   1108 C  CD2   . LEU A 1 139 ? -25.724 1.219   -14.183 1.00 25.70 ?  138 LEU A CD2   1 
ATOM   1109 N  N     . SER A 1 140 ? -22.879 -1.630  -10.333 1.00 26.84 ?  139 SER A N     1 
ATOM   1110 C  CA    . SER A 1 140 ? -21.861 -2.582  -9.915  1.00 27.55 ?  139 SER A CA    1 
ATOM   1111 C  C     . SER A 1 140 ? -22.375 -3.580  -8.884  1.00 31.39 ?  139 SER A C     1 
ATOM   1112 O  O     . SER A 1 140 ? -21.580 -4.282  -8.259  1.00 37.03 ?  139 SER A O     1 
ATOM   1113 C  CB    . SER A 1 140 ? -20.637 -1.848  -9.371  1.00 22.68 ?  139 SER A CB    1 
ATOM   1114 O  OG    . SER A 1 140 ? -20.198 -0.882  -10.317 1.00 21.77 ?  139 SER A OG    1 
ATOM   1115 N  N     . GLY A 1 141 ? -23.686 -3.679  -8.705  1.00 32.48 ?  140 GLY A N     1 
ATOM   1116 C  CA    . GLY A 1 141 ? -24.212 -4.675  -7.800  1.00 33.35 ?  140 GLY A CA    1 
ATOM   1117 C  C     . GLY A 1 141 ? -24.440 -4.184  -6.392  1.00 34.02 ?  140 GLY A C     1 
ATOM   1118 O  O     . GLY A 1 141 ? -24.560 -5.007  -5.476  1.00 35.96 ?  140 GLY A O     1 
ATOM   1119 N  N     . GLY A 1 142 ? -24.478 -2.873  -6.185  1.00 32.64 ?  141 GLY A N     1 
ATOM   1120 C  CA    . GLY A 1 142 ? -24.871 -2.301  -4.918  1.00 30.20 ?  141 GLY A CA    1 
ATOM   1121 C  C     . GLY A 1 142 ? -23.733 -1.835  -4.034  1.00 31.21 ?  141 GLY A C     1 
ATOM   1122 O  O     . GLY A 1 142 ? -23.988 -1.172  -3.022  1.00 30.29 ?  141 GLY A O     1 
ATOM   1123 N  N     . THR A 1 143 ? -22.494 -2.147  -4.374  1.00 29.35 ?  142 THR A N     1 
ATOM   1124 C  CA    . THR A 1 143 ? -21.388 -1.820  -3.494  1.00 31.96 ?  142 THR A CA    1 
ATOM   1125 C  C     . THR A 1 143 ? -20.540 -0.709  -4.110  1.00 26.00 ?  142 THR A C     1 
ATOM   1126 O  O     . THR A 1 143 ? -20.489 -0.547  -5.331  1.00 25.79 ?  142 THR A O     1 
ATOM   1127 C  CB    . THR A 1 143 ? -20.573 -3.082  -3.202  1.00 39.27 ?  142 THR A CB    1 
ATOM   1128 O  OG1   . THR A 1 143 ? -19.800 -2.880  -2.019  1.00 49.65 ?  142 THR A OG1   1 
ATOM   1129 C  CG2   . THR A 1 143 ? -19.660 -3.412  -4.346  1.00 39.36 ?  142 THR A CG2   1 
ATOM   1130 N  N     . LEU A 1 144 ? -19.928 0.108   -3.250  1.00 22.33 ?  143 LEU A N     1 
ATOM   1131 C  CA    . LEU A 1 144 ? -19.082 1.213   -3.682  1.00 20.50 ?  143 LEU A CA    1 
ATOM   1132 C  C     . LEU A 1 144 ? -17.632 0.752   -3.637  1.00 19.81 ?  143 LEU A C     1 
ATOM   1133 O  O     . LEU A 1 144 ? -17.130 0.392   -2.563  1.00 20.12 ?  143 LEU A O     1 
ATOM   1134 C  CB    . LEU A 1 144 ? -19.255 2.443   -2.794  1.00 19.99 ?  143 LEU A CB    1 
ATOM   1135 C  CG    . LEU A 1 144 ? -18.379 3.620   -3.193  1.00 21.87 ?  143 LEU A CG    1 
ATOM   1136 C  CD1   . LEU A 1 144 ? -18.836 4.293   -4.487  1.00 19.40 ?  143 LEU A CD1   1 
ATOM   1137 C  CD2   . LEU A 1 144 ? -18.319 4.645   -2.051  1.00 21.62 ?  143 LEU A CD2   1 
ATOM   1138 N  N     . CYS A 1 145 ? -16.970 0.759   -4.801  1.00 16.99 ?  144 CYS A N     1 
ATOM   1139 C  CA    . CYS A 1 145 ? -15.616 0.232   -4.934  1.00 14.96 ?  144 CYS A CA    1 
ATOM   1140 C  C     . CYS A 1 145 ? -14.694 1.266   -5.551  1.00 15.17 ?  144 CYS A C     1 
ATOM   1141 O  O     . CYS A 1 145 ? -15.055 1.920   -6.539  1.00 17.82 ?  144 CYS A O     1 
ATOM   1142 C  CB    . CYS A 1 145 ? -15.596 -1.014  -5.826  1.00 19.00 ?  144 CYS A CB    1 
ATOM   1143 S  SG    . CYS A 1 145 ? -16.506 -2.341  -5.137  1.00 21.14 ?  144 CYS A SG    1 
ATOM   1144 N  N     . ILE A 1 146 ? -13.451 1.375   -4.989  1.00 18.06 ?  145 ILE A N     1 
ATOM   1145 C  CA    . ILE A 1 146 ? -12.430 2.308   -5.453  1.00 15.16 ?  145 ILE A CA    1 
ATOM   1146 C  C     . ILE A 1 146 ? -11.477 1.585   -6.410  1.00 16.33 ?  145 ILE A C     1 
ATOM   1147 O  O     . ILE A 1 146 ? -11.233 0.389   -6.272  1.00 16.01 ?  145 ILE A O     1 
ATOM   1148 C  CB    . ILE A 1 146 ? -11.679 2.926   -4.233  1.00 16.47 ?  145 ILE A CB    1 
ATOM   1149 C  CG1   . ILE A 1 146 ? -10.701 4.018   -4.649  1.00 16.26 ?  145 ILE A CG1   1 
ATOM   1150 C  CG2   . ILE A 1 146 ? -10.950 1.850   -3.468  1.00 15.98 ?  145 ILE A CG2   1 
ATOM   1151 C  CD1   . ILE A 1 146 ? -10.086 4.798   -3.423  1.00 16.90 ?  145 ILE A CD1   1 
ATOM   1152 N  N     . ALA A 1 147 ? -10.978 2.325   -7.411  1.00 18.34 ?  146 ALA A N     1 
ATOM   1153 C  CA    . ALA A 1 147 ? -10.065 1.803   -8.444  1.00 17.26 ?  146 ALA A CA    1 
ATOM   1154 C  C     . ALA A 1 147 ? -8.665  1.674   -7.859  1.00 20.24 ?  146 ALA A C     1 
ATOM   1155 O  O     . ALA A 1 147 ? -7.951  2.674   -7.733  1.00 20.47 ?  146 ALA A O     1 
ATOM   1156 C  CB    . ALA A 1 147 ? -10.052 2.732   -9.646  1.00 20.99 ?  146 ALA A CB    1 
ATOM   1157 N  N     . LYS A 1 148 ? -8.253  0.441   -7.531  1.00 22.17 ?  147 LYS A N     1 
ATOM   1158 C  CA    . LYS A 1 148 ? -6.920  0.128   -7.012  1.00 23.05 ?  147 LYS A CA    1 
ATOM   1159 C  C     . LYS A 1 148 ? -6.004  -0.391  -8.117  1.00 24.12 ?  147 LYS A C     1 
ATOM   1160 O  O     . LYS A 1 148 ? -6.390  -1.291  -8.874  1.00 26.36 ?  147 LYS A O     1 
ATOM   1161 C  CB    . LYS A 1 148 ? -7.017  -0.942  -5.929  1.00 23.67 ?  147 LYS A CB    1 
ATOM   1162 C  CG    . LYS A 1 148 ? -7.774  -0.505  -4.669  1.00 28.92 ?  147 LYS A CG    1 
ATOM   1163 C  CD    . LYS A 1 148 ? -7.047  0.627   -3.988  1.00 32.11 ?  147 LYS A CD    1 
ATOM   1164 C  CE    . LYS A 1 148 ? -6.579  0.224   -2.606  1.00 34.80 ?  147 LYS A CE    1 
ATOM   1165 N  NZ    . LYS A 1 148 ? -5.845  1.366   -1.998  1.00 33.39 1  147 LYS A NZ    1 
ATOM   1166 N  N     . GLY A 1 149 ? -4.777  0.139   -8.154  1.00 24.17 ?  148 GLY A N     1 
ATOM   1167 C  CA    . GLY A 1 149 ? -3.680  -0.335  -8.991  1.00 21.51 ?  148 GLY A CA    1 
ATOM   1168 C  C     . GLY A 1 149 ? -3.076  0.778   -9.809  1.00 26.48 ?  148 GLY A C     1 
ATOM   1169 O  O     . GLY A 1 149 ? -3.761  1.763   -10.099 1.00 26.01 ?  148 GLY A O     1 
ATOM   1170 N  N     . LYS A 1 150 ? -1.806  0.641   -10.223 1.00 29.96 ?  149 LYS A N     1 
ATOM   1171 C  CA    . LYS A 1 150 ? -1.195  1.619   -11.123 1.00 34.81 ?  149 LYS A CA    1 
ATOM   1172 C  C     . LYS A 1 150 ? -0.725  0.921   -12.390 1.00 34.24 ?  149 LYS A C     1 
ATOM   1173 O  O     . LYS A 1 150 ? -0.827  -0.292  -12.511 1.00 32.21 ?  149 LYS A O     1 
ATOM   1174 C  CB    . LYS A 1 150 ? -0.043  2.372   -10.451 1.00 39.06 ?  149 LYS A CB    1 
ATOM   1175 C  CG    . LYS A 1 150 ? 0.687   1.627   -9.362  1.00 43.37 ?  149 LYS A CG    1 
ATOM   1176 C  CD    . LYS A 1 150 ? 1.633   2.588   -8.664  1.00 45.28 ?  149 LYS A CD    1 
ATOM   1177 C  CE    . LYS A 1 150 ? 2.624   1.865   -7.805  1.00 47.21 ?  149 LYS A CE    1 
ATOM   1178 N  NZ    . LYS A 1 150 ? 3.398   2.835   -6.988  1.00 47.46 1  149 LYS A NZ    1 
ATOM   1179 N  N     . GLU A 1 151 ? -0.229  1.715   -13.344 1.00 40.09 ?  150 GLU A N     1 
ATOM   1180 C  CA    . GLU A 1 151 ? 0.200   1.148   -14.622 1.00 45.35 ?  150 GLU A CA    1 
ATOM   1181 C  C     . GLU A 1 151 ? 1.293   0.111   -14.431 1.00 46.85 ?  150 GLU A C     1 
ATOM   1182 O  O     . GLU A 1 151 ? 1.461   -0.764  -15.285 1.00 47.07 ?  150 GLU A O     1 
ATOM   1183 C  CB    . GLU A 1 151 ? 0.683   2.247   -15.567 1.00 49.99 ?  150 GLU A CB    1 
ATOM   1184 C  CG    . GLU A 1 151 ? 0.073   3.601   -15.294 1.00 54.51 ?  150 GLU A CG    1 
ATOM   1185 C  CD    . GLU A 1 151 ? 0.077   4.500   -16.513 1.00 58.71 ?  150 GLU A CD    1 
ATOM   1186 O  OE1   . GLU A 1 151 ? -0.096  3.980   -17.639 1.00 61.22 ?  150 GLU A OE1   1 
ATOM   1187 O  OE2   . GLU A 1 151 ? 0.243   5.727   -16.345 1.00 59.33 -1 150 GLU A OE2   1 
ATOM   1188 N  N     . ASN A 1 152 ? 2.016   0.193   -13.312 1.00 48.59 ?  151 ASN A N     1 
ATOM   1189 C  CA    . ASN A 1 152 ? 3.028   -0.775  -12.916 1.00 51.11 ?  151 ASN A CA    1 
ATOM   1190 C  C     . ASN A 1 152 ? 2.434   -2.127  -12.540 1.00 44.33 ?  151 ASN A C     1 
ATOM   1191 O  O     . ASN A 1 152 ? 3.125   -3.139  -12.644 1.00 42.60 ?  151 ASN A O     1 
ATOM   1192 C  CB    . ASN A 1 152 ? 3.812   -0.201  -11.724 1.00 60.65 ?  151 ASN A CB    1 
ATOM   1193 C  CG    . ASN A 1 152 ? 5.236   -0.720  -11.639 1.00 69.46 ?  151 ASN A CG    1 
ATOM   1194 O  OD1   . ASN A 1 152 ? 6.105   -0.319  -12.418 1.00 76.68 ?  151 ASN A OD1   1 
ATOM   1195 N  ND2   . ASN A 1 152 ? 5.491   -1.593  -10.669 1.00 71.75 ?  151 ASN A ND2   1 
ATOM   1196 N  N     . SER A 1 153 ? 1.178   -2.169  -12.111 1.00 39.33 ?  152 SER A N     1 
ATOM   1197 C  CA    . SER A 1 153 ? 0.647   -3.319  -11.388 1.00 36.04 ?  152 SER A CA    1 
ATOM   1198 C  C     . SER A 1 153 ? 0.360   -4.503  -12.297 1.00 37.32 ?  152 SER A C     1 
ATOM   1199 O  O     . SER A 1 153 ? -0.122  -4.337  -13.420 1.00 36.12 ?  152 SER A O     1 
ATOM   1200 C  CB    . SER A 1 153 ? -0.649  -2.936  -10.670 1.00 34.00 ?  152 SER A CB    1 
ATOM   1201 N  N     . GLY A 1 154 ? 0.614   -5.705  -11.780 1.00 38.32 ?  153 GLY A N     1 
ATOM   1202 C  CA    . GLY A 1 154 ? 0.132   -6.920  -12.397 1.00 40.98 ?  153 GLY A CA    1 
ATOM   1203 C  C     . GLY A 1 154 ? -1.328  -7.169  -12.076 1.00 43.71 ?  153 GLY A C     1 
ATOM   1204 O  O     . GLY A 1 154 ? -1.984  -6.401  -11.370 1.00 42.49 ?  153 GLY A O     1 
ATOM   1205 N  N     . ASP A 1 155 ? -1.844  -8.284  -12.603 1.00 46.76 ?  154 ASP A N     1 
ATOM   1206 C  CA    . ASP A 1 155 ? -3.266  -8.579  -12.450 1.00 50.38 ?  154 ASP A CA    1 
ATOM   1207 C  C     . ASP A 1 155 ? -3.642  -8.815  -10.995 1.00 53.43 ?  154 ASP A C     1 
ATOM   1208 O  O     . ASP A 1 155 ? -4.790  -8.581  -10.603 1.00 53.31 ?  154 ASP A O     1 
ATOM   1209 C  CB    . ASP A 1 155 ? -3.654  -9.797  -13.285 1.00 50.91 ?  154 ASP A CB    1 
ATOM   1210 C  CG    . ASP A 1 155 ? -5.112  -10.154 -13.131 1.00 50.95 ?  154 ASP A CG    1 
ATOM   1211 O  OD1   . ASP A 1 155 ? -5.975  -9.348  -13.546 1.00 51.25 ?  154 ASP A OD1   1 
ATOM   1212 O  OD2   . ASP A 1 155 ? -5.396  -11.232 -12.573 1.00 51.32 -1 154 ASP A OD2   1 
ATOM   1213 N  N     . GLU A 1 156 ? -2.693  -9.290  -10.193 1.00 56.80 ?  155 GLU A N     1 
ATOM   1214 C  CA    . GLU A 1 156 ? -2.942  -9.521  -8.777  1.00 59.63 ?  155 GLU A CA    1 
ATOM   1215 C  C     . GLU A 1 156 ? -3.338  -8.236  -8.064  1.00 56.90 ?  155 GLU A C     1 
ATOM   1216 O  O     . GLU A 1 156 ? -4.105  -8.279  -7.100  1.00 55.72 ?  155 GLU A O     1 
ATOM   1217 C  CB    . GLU A 1 156 ? -1.682  -10.134 -8.155  1.00 65.57 ?  155 GLU A CB    1 
ATOM   1218 C  CG    . GLU A 1 156 ? -1.723  -10.453 -6.675  1.00 70.70 ?  155 GLU A CG    1 
ATOM   1219 C  CD    . GLU A 1 156 ? -0.329  -10.731 -6.129  1.00 74.29 ?  155 GLU A CD    1 
ATOM   1220 O  OE1   . GLU A 1 156 ? -0.144  -10.722 -4.891  1.00 75.38 ?  155 GLU A OE1   1 
ATOM   1221 O  OE2   . GLU A 1 156 ? 0.585   -10.948 -6.952  1.00 75.40 -1 155 GLU A OE2   1 
ATOM   1222 N  N     . HIS A 1 157 ? -2.857  -7.084  -8.541  1.00 55.67 ?  156 HIS A N     1 
ATOM   1223 C  CA    . HIS A 1 157 ? -2.966  -5.818  -7.824  1.00 54.68 ?  156 HIS A CA    1 
ATOM   1224 C  C     . HIS A 1 157 ? -3.879  -4.808  -8.506  1.00 49.05 ?  156 HIS A C     1 
ATOM   1225 O  O     . HIS A 1 157 ? -3.861  -3.626  -8.143  1.00 50.91 ?  156 HIS A O     1 
ATOM   1226 C  CB    . HIS A 1 157 ? -1.578  -5.208  -7.634  1.00 58.23 ?  156 HIS A CB    1 
ATOM   1227 C  CG    . HIS A 1 157 ? -0.724  -5.963  -6.668  1.00 61.72 ?  156 HIS A CG    1 
ATOM   1228 N  ND1   . HIS A 1 157 ? -1.232  -6.546  -5.527  1.00 62.39 ?  156 HIS A ND1   1 
ATOM   1229 C  CD2   . HIS A 1 157 ? 0.600   -6.241  -6.677  1.00 62.55 ?  156 HIS A CD2   1 
ATOM   1230 C  CE1   . HIS A 1 157 ? -0.256  -7.145  -4.871  1.00 62.83 ?  156 HIS A CE1   1 
ATOM   1231 N  NE2   . HIS A 1 157 ? 0.866   -6.976  -5.549  1.00 62.90 ?  156 HIS A NE2   1 
ATOM   1232 N  N     . ARG A 1 158 ? -4.665  -5.231  -9.483  1.00 42.28 ?  157 ARG A N     1 
ATOM   1233 C  CA    . ARG A 1 158 ? -5.628  -4.364  -10.144 1.00 34.85 ?  157 ARG A CA    1 
ATOM   1234 C  C     . ARG A 1 158 ? -6.994  -4.808  -9.665  1.00 31.44 ?  157 ARG A C     1 
ATOM   1235 O  O     . ARG A 1 158 ? -7.445  -5.897  -10.016 1.00 30.85 ?  157 ARG A O     1 
ATOM   1236 C  CB    . ARG A 1 158 ? -5.513  -4.470  -11.661 1.00 33.01 ?  157 ARG A CB    1 
ATOM   1237 C  CG    . ARG A 1 158 ? -4.194  -3.996  -12.177 1.00 30.68 ?  157 ARG A CG    1 
ATOM   1238 C  CD    . ARG A 1 158 ? -3.876  -4.617  -13.504 1.00 31.55 ?  157 ARG A CD    1 
ATOM   1239 N  NE    . ARG A 1 158 ? -4.185  -3.722  -14.603 1.00 32.72 ?  157 ARG A NE    1 
ATOM   1240 C  CZ    . ARG A 1 158 ? -3.274  -3.042  -15.284 1.00 34.00 ?  157 ARG A CZ    1 
ATOM   1241 N  NH1   . ARG A 1 158 ? -3.647  -2.259  -16.283 1.00 35.89 1  157 ARG A NH1   1 
ATOM   1242 N  NH2   . ARG A 1 158 ? -1.997  -3.153  -14.974 1.00 34.53 ?  157 ARG A NH2   1 
ATOM   1243 N  N     . LEU A 1 159 ? -7.652  -4.000  -8.841  1.00 28.68 ?  158 LEU A N     1 
ATOM   1244 C  CA    . LEU A 1 159 ? -8.954  -4.458  -8.383  1.00 29.20 ?  158 LEU A CA    1 
ATOM   1245 C  C     . LEU A 1 159 ? -9.849  -3.276  -8.049  1.00 26.69 ?  158 LEU A C     1 
ATOM   1246 O  O     . LEU A 1 159 ? -9.419  -2.120  -8.027  1.00 27.03 ?  158 LEU A O     1 
ATOM   1247 C  CB    . LEU A 1 159 ? -8.843  -5.417  -7.188  1.00 32.33 ?  158 LEU A CB    1 
ATOM   1248 C  CG    . LEU A 1 159 ? -8.106  -5.006  -5.921  1.00 34.19 ?  158 LEU A CG    1 
ATOM   1249 C  CD1   . LEU A 1 159 ? -8.771  -5.656  -4.727  1.00 35.08 ?  158 LEU A CD1   1 
ATOM   1250 C  CD2   . LEU A 1 159 ? -6.664  -5.438  -6.001  1.00 34.85 ?  158 LEU A CD2   1 
ATOM   1251 N  N     . TRP A 1 160 ? -11.124 -3.593  -7.913  1.00 24.68 ?  159 TRP A N     1 
ATOM   1252 C  CA    . TRP A 1 160 ? -12.176 -2.679  -7.493  1.00 24.04 ?  159 TRP A CA    1 
ATOM   1253 C  C     . TRP A 1 160 ? -12.468 -3.061  -6.053  1.00 25.56 ?  159 TRP A C     1 
ATOM   1254 O  O     . TRP A 1 160 ? -13.143 -4.060  -5.795  1.00 29.26 ?  159 TRP A O     1 
ATOM   1255 C  CB    . TRP A 1 160 ? -13.423 -2.824  -8.365  1.00 18.88 ?  159 TRP A CB    1 
ATOM   1256 C  CG    . TRP A 1 160 ? -13.282 -2.254  -9.742  1.00 21.15 ?  159 TRP A CG    1 
ATOM   1257 C  CD1   . TRP A 1 160 ? -13.121 -2.951  -10.910 1.00 20.78 ?  159 TRP A CD1   1 
ATOM   1258 C  CD2   . TRP A 1 160 ? -13.308 -0.866  -10.101 1.00 22.51 ?  159 TRP A CD2   1 
ATOM   1259 N  NE1   . TRP A 1 160 ? -13.042 -2.085  -11.968 1.00 23.44 ?  159 TRP A NE1   1 
ATOM   1260 C  CE2   . TRP A 1 160 ? -13.155 -0.800  -11.503 1.00 20.04 ?  159 TRP A CE2   1 
ATOM   1261 C  CE3   . TRP A 1 160 ? -13.433 0.331   -9.371  1.00 16.55 ?  159 TRP A CE3   1 
ATOM   1262 C  CZ2   . TRP A 1 160 ? -13.128 0.412   -12.193 1.00 21.58 ?  159 TRP A CZ2   1 
ATOM   1263 C  CZ3   . TRP A 1 160 ? -13.409 1.532   -10.059 1.00 19.42 ?  159 TRP A CZ3   1 
ATOM   1264 C  CH2   . TRP A 1 160 ? -13.254 1.566   -11.462 1.00 19.47 ?  159 TRP A CH2   1 
ATOM   1265 N  N     . GLN A 1 161 ? -11.965 -2.273  -5.112  1.00 24.88 ?  160 GLN A N     1 
ATOM   1266 C  CA    . GLN A 1 161 ? -12.030 -2.675  -3.715  1.00 24.08 ?  160 GLN A CA    1 
ATOM   1267 C  C     . GLN A 1 161 ? -13.140 -1.942  -2.976  1.00 20.30 ?  160 GLN A C     1 
ATOM   1268 O  O     . GLN A 1 161 ? -13.306 -0.728  -3.144  1.00 20.71 ?  160 GLN A O     1 
ATOM   1269 C  CB    . GLN A 1 161 ? -10.709 -2.407  -3.005  1.00 26.57 ?  160 GLN A CB    1 
ATOM   1270 C  CG    . GLN A 1 161 ? -10.680 -2.948  -1.602  1.00 28.23 ?  160 GLN A CG    1 
ATOM   1271 C  CD    . GLN A 1 161 ? -9.360  -2.653  -0.934  1.00 32.51 ?  160 GLN A CD    1 
ATOM   1272 O  OE1   . GLN A 1 161 ? -9.002  -1.493  -0.725  1.00 32.12 ?  160 GLN A OE1   1 
ATOM   1273 N  NE2   . GLN A 1 161 ? -8.598  -3.703  -0.644  1.00 35.67 ?  160 GLN A NE2   1 
ATOM   1274 N  N     . ILE A 1 162 ? -13.889 -2.696  -2.176  1.00 19.43 ?  161 ILE A N     1 
ATOM   1275 C  CA    . ILE A 1 162 ? -15.016 -2.115  -1.468  1.00 21.02 ?  161 ILE A CA    1 
ATOM   1276 C  C     . ILE A 1 162 ? -14.495 -1.049  -0.522  1.00 19.62 ?  161 ILE A C     1 
ATOM   1277 O  O     . ILE A 1 162 ? -13.444 -1.212  0.114   1.00 19.50 ?  161 ILE A O     1 
ATOM   1278 C  CB    . ILE A 1 162 ? -15.829 -3.181  -0.711  1.00 26.00 ?  161 ILE A CB    1 
ATOM   1279 C  CG1   . ILE A 1 162 ? -17.076 -2.531  -0.111  1.00 27.76 ?  161 ILE A CG1   1 
ATOM   1280 C  CG2   . ILE A 1 162 ? -15.004 -3.868  0.364   1.00 26.22 ?  161 ILE A CG2   1 
ATOM   1281 C  CD1   . ILE A 1 162 ? -18.002 -3.461  0.571   1.00 30.23 ?  161 ILE A CD1   1 
ATOM   1282 N  N     . SER A 1 163 ? -15.232 0.056   -0.431  1.00 19.45 ?  162 SER A N     1 
ATOM   1283 C  CA    . SER A 1 163 ? -14.740 1.247   0.248   1.00 18.51 ?  162 SER A CA    1 
ATOM   1284 C  C     . SER A 1 163 ? -15.935 1.940   0.897   1.00 17.43 ?  162 SER A C     1 
ATOM   1285 O  O     . SER A 1 163 ? -17.065 1.854   0.408   1.00 17.21 ?  162 SER A O     1 
ATOM   1286 C  CB    . SER A 1 163 ? -14.006 2.131   -0.761  1.00 29.05 ?  162 SER A CB    1 
ATOM   1287 O  OG    . SER A 1 163 ? -13.478 3.305   -0.164  1.00 40.03 ?  162 SER A OG    1 
ATOM   1288 N  N     . ASP A 1 164 ? -15.711 2.601   2.038   1.00 15.10 ?  163 ASP A N     1 
ATOM   1289 C  CA    . ASP A 1 164 ? -16.806 3.298   2.716   1.00 12.64 ?  163 ASP A CA    1 
ATOM   1290 C  C     . ASP A 1 164 ? -16.292 4.635   3.236   1.00 13.77 ?  163 ASP A C     1 
ATOM   1291 O  O     . ASP A 1 164 ? -16.257 4.867   4.448   1.00 14.71 ?  163 ASP A O     1 
ATOM   1292 C  CB    . ASP A 1 164 ? -17.379 2.437   3.848   1.00 13.98 ?  163 ASP A CB    1 
ATOM   1293 C  CG    . ASP A 1 164 ? -18.645 3.039   4.497   1.00 14.10 ?  163 ASP A CG    1 
ATOM   1294 O  OD1   . ASP A 1 164 ? -19.224 4.001   3.946   1.00 15.91 ?  163 ASP A OD1   1 
ATOM   1295 O  OD2   . ASP A 1 164 ? -19.042 2.535   5.569   1.00 15.66 -1 163 ASP A OD2   1 
ATOM   1296 N  N     . PRO A 1 165 ? -15.879 5.545   2.341   1.00 16.30 ?  164 PRO A N     1 
ATOM   1297 C  CA    . PRO A 1 165 ? -15.348 6.827   2.836   1.00 15.53 ?  164 PRO A CA    1 
ATOM   1298 C  C     . PRO A 1 165 ? -16.397 7.649   3.567   1.00 16.94 ?  164 PRO A C     1 
ATOM   1299 O  O     . PRO A 1 165 ? -16.064 8.319   4.563   1.00 16.04 ?  164 PRO A O     1 
ATOM   1300 C  CB    . PRO A 1 165 ? -14.849 7.524   1.556   1.00 19.13 ?  164 PRO A CB    1 
ATOM   1301 C  CG    . PRO A 1 165 ? -15.642 6.877   0.465   1.00 20.09 ?  164 PRO A CG    1 
ATOM   1302 C  CD    . PRO A 1 165 ? -15.764 5.448   0.875   1.00 18.91 ?  164 PRO A CD    1 
ATOM   1303 N  N     . GLN A 1 166 ? -17.667 7.563   3.174   1.00 18.40 ?  165 GLN A N     1 
ATOM   1304 C  CA    . GLN A 1 166 ? -18.642 8.367   3.902   1.00 23.28 ?  165 GLN A CA    1 
ATOM   1305 C  C     . GLN A 1 166 ? -18.957 7.788   5.287   1.00 19.39 ?  165 GLN A C     1 
ATOM   1306 O  O     . GLN A 1 166 ? -19.106 8.558   6.250   1.00 18.22 ?  165 GLN A O     1 
ATOM   1307 C  CB    . GLN A 1 166 ? -19.898 8.573   3.031   1.00 33.05 ?  165 GLN A CB    1 
ATOM   1308 C  CG    . GLN A 1 166 ? -19.766 9.896   2.229   1.00 42.34 ?  165 GLN A CG    1 
ATOM   1309 C  CD    . GLN A 1 166 ? -20.474 9.915   0.880   1.00 49.86 ?  165 GLN A CD    1 
ATOM   1310 O  OE1   . GLN A 1 166 ? -20.588 8.895   0.194   1.00 54.64 ?  165 GLN A OE1   1 
ATOM   1311 N  NE2   . GLN A 1 166 ? -20.942 11.096  0.488   1.00 52.12 ?  165 GLN A NE2   1 
ATOM   1312 N  N     . GLY A 1 167 ? -18.998 6.464   5.444   1.00 16.55 ?  166 GLY A N     1 
ATOM   1313 C  CA    . GLY A 1 167 ? -19.084 5.895   6.782   1.00 13.95 ?  166 GLY A CA    1 
ATOM   1314 C  C     . GLY A 1 167 ? -17.890 6.270   7.653   1.00 12.61 ?  166 GLY A C     1 
ATOM   1315 O  O     . GLY A 1 167 ? -18.049 6.571   8.837   1.00 13.70 ?  166 GLY A O     1 
ATOM   1316 N  N     . PHE A 1 168 ? -16.676 6.289   7.073   1.00 12.11 ?  167 PHE A N     1 
ATOM   1317 C  CA    . PHE A 1 168 ? -15.520 6.702   7.868   1.00 10.17 ?  167 PHE A CA    1 
ATOM   1318 C  C     . PHE A 1 168 ? -15.654 8.157   8.300   1.00 10.49 ?  167 PHE A C     1 
ATOM   1319 O  O     . PHE A 1 168 ? -15.435 8.502   9.472   1.00 10.07 ?  167 PHE A O     1 
ATOM   1320 C  CB    . PHE A 1 168 ? -14.204 6.474   7.097   1.00 12.04 ?  167 PHE A CB    1 
ATOM   1321 C  CG    . PHE A 1 168 ? -12.990 6.894   7.867   1.00 11.61 ?  167 PHE A CG    1 
ATOM   1322 C  CD1   . PHE A 1 168 ? -12.692 6.320   9.080   1.00 9.35  ?  167 PHE A CD1   1 
ATOM   1323 C  CD2   . PHE A 1 168 ? -12.154 7.884   7.381   1.00 12.42 ?  167 PHE A CD2   1 
ATOM   1324 C  CE1   . PHE A 1 168 ? -11.581 6.729   9.839   1.00 10.61 ?  167 PHE A CE1   1 
ATOM   1325 C  CE2   . PHE A 1 168 ? -11.045 8.293   8.108   1.00 13.28 ?  167 PHE A CE2   1 
ATOM   1326 C  CZ    . PHE A 1 168 ? -10.745 7.723   9.333   1.00 10.97 ?  167 PHE A CZ    1 
ATOM   1327 N  N     . GLN A 1 169 ? -16.023 9.030   7.356   1.00 12.54 ?  168 GLN A N     1 
ATOM   1328 C  CA    . GLN A 1 169 ? -16.148 10.440  7.697   1.00 11.02 ?  168 GLN A CA    1 
ATOM   1329 C  C     . GLN A 1 169 ? -17.198 10.637  8.781   1.00 10.23 ?  168 GLN A C     1 
ATOM   1330 O  O     . GLN A 1 169 ? -17.027 11.460  9.697   1.00 10.09 ?  168 GLN A O     1 
ATOM   1331 C  CB    . GLN A 1 169 ? -16.510 11.224  6.443   1.00 11.57 ?  168 GLN A CB    1 
ATOM   1332 C  CG    . GLN A 1 169 ? -15.361 11.189  5.453   1.00 17.10 ?  168 GLN A CG    1 
ATOM   1333 C  CD    . GLN A 1 169 ? -15.734 11.771  4.092   1.00 21.70 ?  168 GLN A CD    1 
ATOM   1334 O  OE1   . GLN A 1 169 ? -15.090 11.455  3.089   1.00 26.78 ?  168 GLN A OE1   1 
ATOM   1335 N  NE2   . GLN A 1 169 ? -16.766 12.607  4.057   1.00 23.65 ?  168 GLN A NE2   1 
ATOM   1336 N  N     . ASP A 1 170 ? -18.326 9.933   8.648   1.00 10.31 ?  169 ASP A N     1 
ATOM   1337 C  CA    . ASP A 1 170 ? -19.378 9.991   9.656   1.00 9.67  ?  169 ASP A CA    1 
ATOM   1338 C  C     . ASP A 1 170 ? -18.865 9.547   11.020  1.00 10.65 ?  169 ASP A C     1 
ATOM   1339 O  O     . ASP A 1 170 ? -19.241 10.108  12.052  1.00 10.88 ?  169 ASP A O     1 
ATOM   1340 C  CB    . ASP A 1 170 ? -20.555 9.125   9.221   1.00 11.82 ?  169 ASP A CB    1 
ATOM   1341 C  CG    . ASP A 1 170 ? -21.666 9.130   10.243  1.00 17.10 ?  169 ASP A CG    1 
ATOM   1342 O  OD1   . ASP A 1 170 ? -21.993 10.234  10.748  1.00 15.98 ?  169 ASP A OD1   1 
ATOM   1343 O  OD2   . ASP A 1 170 ? -22.169 8.035   10.595  1.00 20.30 -1 169 ASP A OD2   1 
ATOM   1344 N  N     . ARG A 1 171 ? -18.027 8.498   11.045  1.00 10.41 ?  170 ARG A N     1 
ATOM   1345 C  CA    . ARG A 1 171 ? -17.559 8.035   12.349  1.00 10.68 ?  170 ARG A CA    1 
ATOM   1346 C  C     . ARG A 1 171 ? -16.643 9.060   13.017  1.00 9.47  ?  170 ARG A C     1 
ATOM   1347 O  O     . ARG A 1 171 ? -16.664 9.244   14.244  1.00 9.97  ?  170 ARG A O     1 
ATOM   1348 C  CB    . ARG A 1 171 ? -16.837 6.697   12.155  1.00 11.96 ?  170 ARG A CB    1 
ATOM   1349 C  CG    . ARG A 1 171 ? -17.764 5.574   11.708  1.00 19.75 ?  170 ARG A CG    1 
ATOM   1350 C  CD    . ARG A 1 171 ? -17.626 4.300   12.507  1.00 21.23 ?  170 ARG A CD    1 
ATOM   1351 N  NE    . ARG A 1 171 ? -18.784 3.483   12.184  1.00 21.58 ?  170 ARG A NE    1 
ATOM   1352 C  CZ    . ARG A 1 171 ? -19.456 2.716   13.024  1.00 22.39 ?  170 ARG A CZ    1 
ATOM   1353 N  NH1   . ARG A 1 171 ? -19.067 2.568   14.303  1.00 22.79 1  170 ARG A NH1   1 
ATOM   1354 N  NH2   . ARG A 1 171 ? -20.533 2.090   12.543  1.00 18.27 ?  170 ARG A NH2   1 
ATOM   1355 N  N     . ILE A 1 172 ? -15.779 9.690   12.233  1.00 7.96  ?  171 ILE A N     1 
ATOM   1356 C  CA    . ILE A 1 172 ? -14.925 10.724  12.802  1.00 7.33  ?  171 ILE A CA    1 
ATOM   1357 C  C     . ILE A 1 172 ? -15.771 11.887  13.292  1.00 9.16  ?  171 ILE A C     1 
ATOM   1358 O  O     . ILE A 1 172 ? -15.525 12.440  14.367  1.00 9.49  ?  171 ILE A O     1 
ATOM   1359 C  CB    . ILE A 1 172 ? -13.876 11.162  11.758  1.00 6.35  ?  171 ILE A CB    1 
ATOM   1360 C  CG1   . ILE A 1 172 ? -12.977 9.965   11.365  1.00 8.45  ?  171 ILE A CG1   1 
ATOM   1361 C  CG2   . ILE A 1 172 ? -13.056 12.312  12.293  1.00 6.59  ?  171 ILE A CG2   1 
ATOM   1362 C  CD1   . ILE A 1 172 ? -12.231 9.347   12.562  1.00 8.74  ?  171 ILE A CD1   1 
ATOM   1363 N  N     . ALA A 1 173 ? -16.795 12.271  12.507  1.00 8.34  ?  172 ALA A N     1 
ATOM   1364 C  CA    . ALA A 1 173 ? -17.607 13.422  12.906  1.00 8.53  ?  172 ALA A CA    1 
ATOM   1365 C  C     . ALA A 1 173 ? -18.479 13.119  14.111  1.00 9.19  ?  172 ALA A C     1 
ATOM   1366 O  O     . ALA A 1 173 ? -18.822 14.026  14.879  1.00 10.03 ?  172 ALA A O     1 
ATOM   1367 C  CB    . ALA A 1 173 ? -18.532 13.848  11.772  1.00 10.00 ?  172 ALA A CB    1 
ATOM   1368 N  N     . SER A 1 174 ? -18.889 11.864  14.258  1.00 10.15 ?  173 SER A N     1 
ATOM   1369 C  CA    . SER A 1 174 ? -19.901 11.488  15.253  1.00 10.99 ?  173 SER A CA    1 
ATOM   1370 C  C     . SER A 1 174 ? -19.336 10.932  16.558  1.00 10.79 ?  173 SER A C     1 
ATOM   1371 O  O     . SER A 1 174 ? -20.105 10.751  17.507  1.00 10.64 ?  173 SER A O     1 
ATOM   1372 C  CB    . SER A 1 174 ? -20.823 10.446  14.655  1.00 11.64 ?  173 SER A CB    1 
ATOM   1373 O  OG    . SER A 1 174 ? -21.382 10.928  13.437  1.00 13.10 ?  173 SER A OG    1 
ATOM   1374 N  N     . LYS A 1 175 ? -18.022 10.700  16.653  1.00 11.67 ?  174 LYS A N     1 
ATOM   1375 C  CA    . LYS A 1 175 ? -17.481 10.081  17.864  1.00 10.11 ?  174 LYS A CA    1 
ATOM   1376 C  C     . LYS A 1 175 ? -17.772 10.923  19.106  1.00 9.45  ?  174 LYS A C     1 
ATOM   1377 O  O     . LYS A 1 175 ? -18.117 10.387  20.176  1.00 13.20 ?  174 LYS A O     1 
ATOM   1378 C  CB    . LYS A 1 175 ? -15.967 9.857   17.693  1.00 8.32  ?  174 LYS A CB    1 
ATOM   1379 C  CG    . LYS A 1 175 ? -15.278 9.292   18.954  1.00 10.35 ?  174 LYS A CG    1 
ATOM   1380 C  CD    . LYS A 1 175 ? -13.793 9.142   18.695  1.00 10.95 ?  174 LYS A CD    1 
ATOM   1381 C  CE    . LYS A 1 175 ? -13.037 8.740   19.977  1.00 12.27 ?  174 LYS A CE    1 
ATOM   1382 N  NZ    . LYS A 1 175 ? -13.587 7.365   20.417  1.00 15.52 1  174 LYS A NZ    1 
ATOM   1383 N  N     . LEU A 1 176 ? -17.642 12.253  18.989  1.00 6.36  ?  175 LEU A N     1 
ATOM   1384 C  CA    . LEU A 1 176 ? -17.846 13.187  20.071  1.00 7.61  ?  175 LEU A CA    1 
ATOM   1385 C  C     . LEU A 1 176 ? -18.672 14.336  19.518  1.00 8.58  ?  175 LEU A C     1 
ATOM   1386 O  O     . LEU A 1 176 ? -18.929 14.390  18.309  1.00 8.96  ?  175 LEU A O     1 
ATOM   1387 C  CB    . LEU A 1 176 ? -16.514 13.685  20.635  1.00 10.56 ?  175 LEU A CB    1 
ATOM   1388 C  CG    . LEU A 1 176 ? -15.677 12.552  21.259  1.00 8.90  ?  175 LEU A CG    1 
ATOM   1389 C  CD1   . LEU A 1 176 ? -14.241 13.036  21.370  1.00 10.66 ?  175 LEU A CD1   1 
ATOM   1390 C  CD2   . LEU A 1 176 ? -16.242 12.168  22.646  1.00 9.59  ?  175 LEU A CD2   1 
ATOM   1391 N  N     . SER A 1 177 ? -19.072 15.253  20.395  1.00 9.30  ?  176 SER A N     1 
ATOM   1392 C  CA    . SER A 1 177 ? -19.777 16.454  19.961  1.00 10.21 ?  176 SER A CA    1 
ATOM   1393 C  C     . SER A 1 177 ? -19.209 17.679  20.661  1.00 8.74  ?  176 SER A C     1 
ATOM   1394 O  O     . SER A 1 177 ? -18.423 17.590  21.624  1.00 8.70  ?  176 SER A O     1 
ATOM   1395 C  CB    . SER A 1 177 ? -21.292 16.348  20.207  1.00 12.00 ?  176 SER A CB    1 
ATOM   1396 O  OG    . SER A 1 177 ? -21.542 16.413  21.588  1.00 13.90 ?  176 SER A OG    1 
ATOM   1397 N  N     . GLY A 1 178 ? -19.617 18.847  20.166  1.00 10.10 ?  177 GLY A N     1 
ATOM   1398 C  CA    . GLY A 1 178 ? -19.288 20.067  20.882  1.00 8.76  ?  177 GLY A CA    1 
ATOM   1399 C  C     . GLY A 1 178 ? -17.815 20.227  21.205  1.00 9.21  ?  177 GLY A C     1 
ATOM   1400 O  O     . GLY A 1 178 ? -16.931 19.928  20.394  1.00 10.33 ?  177 GLY A O     1 
ATOM   1401 N  N     . ASP A 1 179 ? -17.543 20.809  22.365  1.00 9.32  ?  178 ASP A N     1 
ATOM   1402 C  CA    . ASP A 1 179 ? -16.147 21.107  22.674  1.00 9.81  ?  178 ASP A CA    1 
ATOM   1403 C  C     . ASP A 1 179 ? -15.313 19.837  22.886  1.00 8.86  ?  178 ASP A C     1 
ATOM   1404 O  O     . ASP A 1 179 ? -14.080 19.885  22.731  1.00 8.56  ?  178 ASP A O     1 
ATOM   1405 C  CB    . ASP A 1 179 ? -16.092 21.993  23.930  1.00 10.41 ?  178 ASP A CB    1 
ATOM   1406 C  CG    . ASP A 1 179 ? -16.612 23.394  23.687  1.00 13.31 ?  178 ASP A CG    1 
ATOM   1407 O  OD1   . ASP A 1 179 ? -16.667 23.898  22.556  1.00 15.48 ?  178 ASP A OD1   1 
ATOM   1408 O  OD2   . ASP A 1 179 ? -16.964 24.033  24.707  1.00 17.70 -1 178 ASP A OD2   1 
ATOM   1409 N  N     . ASP A 1 180 ? -15.944 18.694  23.216  1.00 8.10  ?  179 ASP A N     1 
ATOM   1410 C  CA    . ASP A 1 180 ? -15.211 17.426  23.291  1.00 7.55  ?  179 ASP A CA    1 
ATOM   1411 C  C     . ASP A 1 180 ? -14.652 17.064  21.921  1.00 6.10  ?  179 ASP A C     1 
ATOM   1412 O  O     . ASP A 1 180 ? -13.452 16.717  21.772  1.00 5.89  ?  179 ASP A O     1 
ATOM   1413 C  CB    . ASP A 1 180 ? -16.137 16.306  23.758  1.00 9.60  ?  179 ASP A CB    1 
ATOM   1414 C  CG    . ASP A 1 180 ? -16.409 16.308  25.240  1.00 14.80 ?  179 ASP A CG    1 
ATOM   1415 O  OD1   . ASP A 1 180 ? -15.878 17.147  26.001  1.00 11.29 ?  179 ASP A OD1   1 
ATOM   1416 O  OD2   . ASP A 1 180 ? -17.147 15.356  25.625  1.00 18.82 -1 179 ASP A OD2   1 
ATOM   1417 N  N     . ALA A 1 181 ? -15.516 17.157  20.910  1.00 6.00  ?  180 ALA A N     1 
ATOM   1418 C  CA    . ALA A 1 181 ? -15.076 16.897  19.540  1.00 6.17  ?  180 ALA A CA    1 
ATOM   1419 C  C     . ALA A 1 181 ? -14.068 17.928  19.073  1.00 5.04  ?  180 ALA A C     1 
ATOM   1420 O  O     . ALA A 1 181 ? -13.136 17.588  18.323  1.00 6.00  ?  180 ALA A O     1 
ATOM   1421 C  CB    . ALA A 1 181 ? -16.285 16.879  18.592  1.00 6.56  ?  180 ALA A CB    1 
ATOM   1422 N  N     . ALA A 1 182 ? -14.203 19.185  19.527  1.00 5.40  ?  181 ALA A N     1 
ATOM   1423 C  CA    . ALA A 1 182 ? -13.177 20.166  19.156  1.00 4.37  ?  181 ALA A CA    1 
ATOM   1424 C  C     . ALA A 1 182 ? -11.802 19.777  19.684  1.00 4.84  ?  181 ALA A C     1 
ATOM   1425 O  O     . ALA A 1 182 ? -10.798 19.885  18.966  1.00 5.58  ?  181 ALA A O     1 
ATOM   1426 C  CB    . ALA A 1 182 ? -13.590 21.542  19.679  1.00 6.95  ?  181 ALA A CB    1 
ATOM   1427 N  N     . GLN A 1 183 ? -11.737 19.250  20.919  1.00 4.62  ?  182 GLN A N     1 
ATOM   1428 C  CA    . GLN A 1 183 ? -10.432 18.834  21.457  1.00 4.85  ?  182 GLN A CA    1 
ATOM   1429 C  C     . GLN A 1 183 ? -9.858  17.622  20.712  1.00 5.59  ?  182 GLN A C     1 
ATOM   1430 O  O     . GLN A 1 183 ? -8.650  17.570  20.443  1.00 5.60  ?  182 GLN A O     1 
ATOM   1431 C  CB    . GLN A 1 183 ? -10.529 18.474  22.942  1.00 5.33  ?  182 GLN A CB    1 
ATOM   1432 C  CG    . GLN A 1 183 ? -9.097  18.260  23.536  1.00 5.61  ?  182 GLN A CG    1 
ATOM   1433 C  CD    . GLN A 1 183 ? -9.115  17.808  24.991  1.00 5.82  ?  182 GLN A CD    1 
ATOM   1434 O  OE1   . GLN A 1 183 ? -9.841  16.891  25.333  1.00 7.80  ?  182 GLN A OE1   1 
ATOM   1435 N  NE2   . GLN A 1 183 ? -8.321  18.467  25.862  1.00 6.36  ?  182 GLN A NE2   1 
ATOM   1436 N  N     . PHE A 1 184 ? -10.718 16.653  20.364  1.00 5.11  ?  183 PHE A N     1 
ATOM   1437 C  CA    . PHE A 1 184 ? -10.350 15.535  19.483  1.00 4.67  ?  183 PHE A CA    1 
ATOM   1438 C  C     . PHE A 1 184 ? -9.716  16.043  18.179  1.00 5.16  ?  183 PHE A C     1 
ATOM   1439 O  O     . PHE A 1 184 ? -8.616  15.608  17.789  1.00 5.55  ?  183 PHE A O     1 
ATOM   1440 C  CB    . PHE A 1 184 ? -11.638 14.739  19.242  1.00 6.15  ?  183 PHE A CB    1 
ATOM   1441 C  CG    . PHE A 1 184 ? -11.620 13.659  18.172  1.00 5.23  ?  183 PHE A CG    1 
ATOM   1442 C  CD1   . PHE A 1 184 ? -10.893 12.474  18.330  1.00 4.69  ?  183 PHE A CD1   1 
ATOM   1443 C  CD2   . PHE A 1 184 ? -12.469 13.761  17.109  1.00 5.81  ?  183 PHE A CD2   1 
ATOM   1444 C  CE1   . PHE A 1 184 ? -10.971 11.458  17.376  1.00 5.69  ?  183 PHE A CE1   1 
ATOM   1445 C  CE2   . PHE A 1 184 ? -12.546 12.772  16.129  1.00 7.48  ?  183 PHE A CE2   1 
ATOM   1446 C  CZ    . PHE A 1 184 ? -11.800 11.573  16.299  1.00 5.87  ?  183 PHE A CZ    1 
ATOM   1447 N  N     . ARG A 1 185 ? -10.385 16.992  17.527  1.00 5.82  ?  184 ARG A N     1 
ATOM   1448 C  CA    . ARG A 1 185 ? -9.846  17.498  16.258  1.00 6.68  ?  184 ARG A CA    1 
ATOM   1449 C  C     . ARG A 1 185 ? -8.551  18.267  16.474  1.00 5.29  ?  184 ARG A C     1 
ATOM   1450 O  O     . ARG A 1 185 ? -7.618  18.148  15.666  1.00 6.13  ?  184 ARG A O     1 
ATOM   1451 C  CB    . ARG A 1 185 ? -10.856 18.389  15.548  1.00 6.48  ?  184 ARG A CB    1 
ATOM   1452 C  CG    . ARG A 1 185 ? -12.052 17.601  15.029  1.00 8.23  ?  184 ARG A CG    1 
ATOM   1453 C  CD    . ARG A 1 185 ? -13.001 18.429  14.141  1.00 9.08  ?  184 ARG A CD    1 
ATOM   1454 N  NE    . ARG A 1 185 ? -13.449 19.646  14.788  1.00 11.30 ?  184 ARG A NE    1 
ATOM   1455 C  CZ    . ARG A 1 185 ? -14.561 19.733  15.525  1.00 15.50 ?  184 ARG A CZ    1 
ATOM   1456 N  NH1   . ARG A 1 185 ? -15.339 18.676  15.673  1.00 15.72 1  184 ARG A NH1   1 
ATOM   1457 N  NH2   . ARG A 1 185 ? -14.897 20.884  16.083  1.00 17.13 ?  184 ARG A NH2   1 
ATOM   1458 N  N     . ARG A 1 186 ? -8.479  19.065  17.557  1.00 5.97  ?  185 ARG A N     1 
ATOM   1459 C  CA    . ARG A 1 186 ? -7.236  19.758  17.861  1.00 4.88  ?  185 ARG A CA    1 
ATOM   1460 C  C     . ARG A 1 186 ? -6.100  18.756  17.989  1.00 3.02  ?  185 ARG A C     1 
ATOM   1461 O  O     . ARG A 1 186 ? -4.996  19.003  17.469  1.00 4.42  ?  185 ARG A O     1 
ATOM   1462 C  CB    . ARG A 1 186 ? -7.315  20.602  19.147  1.00 4.29  ?  185 ARG A CB    1 
ATOM   1463 C  CG    . ARG A 1 186 ? -8.239  21.841  19.015  1.00 4.77  ?  185 ARG A CG    1 
ATOM   1464 C  CD    . ARG A 1 186 ? -7.923  22.909  20.080  1.00 5.11  ?  185 ARG A CD    1 
ATOM   1465 N  NE    . ARG A 1 186 ? -8.147  22.433  21.438  1.00 6.43  ?  185 ARG A NE    1 
ATOM   1466 C  CZ    . ARG A 1 186 ? -9.351  22.353  22.016  1.00 7.23  ?  185 ARG A CZ    1 
ATOM   1467 N  NH1   . ARG A 1 186 ? -10.439 22.727  21.337  1.00 8.07  1  185 ARG A NH1   1 
ATOM   1468 N  NH2   . ARG A 1 186 ? -9.445  21.897  23.249  1.00 7.51  ?  185 ARG A NH2   1 
ATOM   1469 N  N     . CYS A 1 187 ? -6.335  17.632  18.664  1.00 5.06  ?  186 CYS A N     1 
ATOM   1470 C  CA    . CYS A 1 187 ? -5.222  16.723  18.925  1.00 5.33  ?  186 CYS A CA    1 
ATOM   1471 C  C     . CYS A 1 187 ? -4.788  16.011  17.657  1.00 4.06  ?  186 CYS A C     1 
ATOM   1472 O  O     . CYS A 1 187 ? -3.583  15.757  17.460  1.00 5.12  ?  186 CYS A O     1 
ATOM   1473 C  CB    . CYS A 1 187 ? -5.589  15.727  20.031  1.00 6.27  ?  186 CYS A CB    1 
ATOM   1474 S  SG    . CYS A 1 187 ? -5.617  16.619  21.678  1.00 9.92  ?  186 CYS A SG    1 
ATOM   1475 N  N     . ILE A 1 188 ? -5.734  15.697  16.780  1.00 4.23  ?  187 ILE A N     1 
ATOM   1476 C  CA    . ILE A 1 188 ? -5.350  15.172  15.471  1.00 3.75  ?  187 ILE A CA    1 
ATOM   1477 C  C     . ILE A 1 188 ? -4.461  16.180  14.744  1.00 3.56  ?  187 ILE A C     1 
ATOM   1478 O  O     . ILE A 1 188 ? -3.413  15.839  14.181  1.00 4.83  ?  187 ILE A O     1 
ATOM   1479 C  CB    . ILE A 1 188 ? -6.607  14.834  14.669  1.00 4.55  ?  187 ILE A CB    1 
ATOM   1480 C  CG1   . ILE A 1 188 ? -7.304  13.615  15.308  1.00 5.06  ?  187 ILE A CG1   1 
ATOM   1481 C  CG2   . ILE A 1 188 ? -6.257  14.507  13.184  1.00 4.77  ?  187 ILE A CG2   1 
ATOM   1482 C  CD1   . ILE A 1 188 ? -8.759  13.430  14.767  1.00 6.60  ?  187 ILE A CD1   1 
ATOM   1483 N  N     . ARG A 1 189 ? -4.877  17.443  14.747  1.00 4.11  ?  188 ARG A N     1 
ATOM   1484 C  CA    . ARG A 1 189 ? -4.058  18.463  14.077  1.00 5.71  ?  188 ARG A CA    1 
ATOM   1485 C  C     . ARG A 1 189 ? -2.672  18.592  14.708  1.00 4.17  ?  188 ARG A C     1 
ATOM   1486 O  O     . ARG A 1 189 ? -1.668  18.692  13.997  1.00 4.90  ?  188 ARG A O     1 
ATOM   1487 C  CB    . ARG A 1 189 ? -4.779  19.812  14.074  1.00 4.80  ?  188 ARG A CB    1 
ATOM   1488 C  CG    . ARG A 1 189 ? -6.001  19.862  13.191  1.00 4.98  ?  188 ARG A CG    1 
ATOM   1489 C  CD    . ARG A 1 189 ? -6.397  21.304  13.060  1.00 4.89  ?  188 ARG A CD    1 
ATOM   1490 N  NE    . ARG A 1 189 ? -7.463  21.465  12.082  1.00 8.32  ?  188 ARG A NE    1 
ATOM   1491 C  CZ    . ARG A 1 189 ? -8.746  21.608  12.393  1.00 10.44 ?  188 ARG A CZ    1 
ATOM   1492 N  NH1   . ARG A 1 189 ? -9.130  21.626  13.663  1.00 12.54 1  188 ARG A NH1   1 
ATOM   1493 N  NH2   . ARG A 1 189 ? -9.634  21.771  11.397  1.00 13.99 ?  188 ARG A NH2   1 
ATOM   1494 N  N     . TYR A 1 190 ? -2.582  18.623  16.052  1.00 5.59  ?  189 TYR A N     1 
ATOM   1495 C  CA    . TYR A 1 190 ? -1.262  18.735  16.678  1.00 3.91  ?  189 TYR A CA    1 
ATOM   1496 C  C     . TYR A 1 190 ? -0.358  17.624  16.212  1.00 5.01  ?  189 TYR A C     1 
ATOM   1497 O  O     . TYR A 1 190 ? 0.826   17.862  15.919  1.00 5.20  ?  189 TYR A O     1 
ATOM   1498 C  CB    . TYR A 1 190 ? -1.368  18.647  18.190  1.00 3.99  ?  189 TYR A CB    1 
ATOM   1499 C  CG    . TYR A 1 190 ? -2.216  19.677  18.864  1.00 4.23  ?  189 TYR A CG    1 
ATOM   1500 C  CD1   . TYR A 1 190 ? -2.178  20.996  18.481  1.00 4.36  ?  189 TYR A CD1   1 
ATOM   1501 C  CD2   . TYR A 1 190 ? -2.976  19.317  19.969  1.00 3.09  ?  189 TYR A CD2   1 
ATOM   1502 C  CE1   . TYR A 1 190 ? -2.940  21.965  19.142  1.00 5.02  ?  189 TYR A CE1   1 
ATOM   1503 C  CE2   . TYR A 1 190 ? -3.781  20.294  20.642  1.00 5.00  ?  189 TYR A CE2   1 
ATOM   1504 C  CZ    . TYR A 1 190 ? -3.749  21.611  20.206  1.00 6.05  ?  189 TYR A CZ    1 
ATOM   1505 O  OH    . TYR A 1 190 ? -4.508  22.587  20.862  1.00 7.30  ?  189 TYR A OH    1 
ATOM   1506 N  N     . LEU A 1 191 ? -0.904  16.383  16.138  1.00 5.33  ?  190 LEU A N     1 
ATOM   1507 C  CA    . LEU A 1 191 ? -0.031  15.285  15.739  1.00 4.98  ?  190 LEU A CA    1 
ATOM   1508 C  C     . LEU A 1 191 ? 0.298   15.318  14.258  1.00 4.98  ?  190 LEU A C     1 
ATOM   1509 O  O     . LEU A 1 191 ? 1.346   14.814  13.885  1.00 5.15  ?  190 LEU A O     1 
ATOM   1510 C  CB    . LEU A 1 191 ? -0.645  13.926  16.110  1.00 5.67  ?  190 LEU A CB    1 
ATOM   1511 C  CG    . LEU A 1 191 ? -0.694  13.929  17.637  1.00 8.55  ?  190 LEU A CG    1 
ATOM   1512 C  CD1   . LEU A 1 191 ? -1.490  12.726  18.138  1.00 14.07 ?  190 LEU A CD1   1 
ATOM   1513 C  CD2   . LEU A 1 191 ? 0.705   13.939  18.276  1.00 9.74  ?  190 LEU A CD2   1 
ATOM   1514 N  N     . LYS A 1 192 ? -0.543  15.940  13.413  1.00 3.40  ?  191 LYS A N     1 
ATOM   1515 C  CA    . LYS A 1 192 ? -0.167  16.084  12.008  1.00 5.02  ?  191 LYS A CA    1 
ATOM   1516 C  C     . LYS A 1 192 ? 0.973   17.080  11.877  1.00 4.10  ?  191 LYS A C     1 
ATOM   1517 O  O     . LYS A 1 192 ? 1.885   16.872  11.079  1.00 5.23  ?  191 LYS A O     1 
ATOM   1518 C  CB    . LYS A 1 192 ? -1.387  16.529  11.185  1.00 5.12  ?  191 LYS A CB    1 
ATOM   1519 C  CG    . LYS A 1 192 ? -2.366  15.355  10.954  1.00 5.39  ?  191 LYS A CG    1 
ATOM   1520 C  CD    . LYS A 1 192 ? -3.554  15.822  10.159  1.00 5.62  ?  191 LYS A CD    1 
ATOM   1521 C  CE    . LYS A 1 192 ? -4.500  14.692  9.746   1.00 7.01  ?  191 LYS A CE    1 
ATOM   1522 N  NZ    . LYS A 1 192 ? -5.627  15.256  8.905   1.00 10.46 1  191 LYS A NZ    1 
ATOM   1523 N  N     . ARG A 1 193 ? 0.960   18.156  12.679  1.00 5.54  ?  192 ARG A N     1 
ATOM   1524 C  CA    . ARG A 1 193 ? 2.102   19.069  12.630  1.00 5.36  ?  192 ARG A CA    1 
ATOM   1525 C  C     . ARG A 1 193 ? 3.375   18.390  13.144  1.00 4.54  ?  192 ARG A C     1 
ATOM   1526 O  O     . ARG A 1 193 ? 4.463   18.565  12.575  1.00 4.56  ?  192 ARG A O     1 
ATOM   1527 C  CB    . ARG A 1 193 ? 1.801   20.351  13.402  1.00 4.75  ?  192 ARG A CB    1 
ATOM   1528 C  CG    . ARG A 1 193 ? 3.038   21.291  13.510  1.00 5.56  ?  192 ARG A CG    1 
ATOM   1529 C  CD    . ARG A 1 193 ? 3.689   21.612  12.107  1.00 5.92  ?  192 ARG A CD    1 
ATOM   1530 N  NE    . ARG A 1 193 ? 2.798   22.299  11.143  1.00 6.44  ?  192 ARG A NE    1 
ATOM   1531 C  CZ    . ARG A 1 193 ? 2.592   23.625  11.155  1.00 6.92  ?  192 ARG A CZ    1 
ATOM   1532 N  NH1   . ARG A 1 193 ? 3.154   24.403  12.101  1.00 6.40  1  192 ARG A NH1   1 
ATOM   1533 N  NH2   . ARG A 1 193 ? 1.728   24.128  10.264  1.00 7.39  ?  192 ARG A NH2   1 
ATOM   1534 N  N     . TRP A 1 194 ? 3.263   17.583  14.210  1.00 4.98  ?  193 TRP A N     1 
ATOM   1535 C  CA    . TRP A 1 194 ? 4.398   16.777  14.678  1.00 4.41  ?  193 TRP A CA    1 
ATOM   1536 C  C     . TRP A 1 194 ? 4.917   15.868  13.576  1.00 3.76  ?  193 TRP A C     1 
ATOM   1537 O  O     . TRP A 1 194 ? 6.144   15.762  13.371  1.00 5.32  ?  193 TRP A O     1 
ATOM   1538 C  CB    . TRP A 1 194 ? 3.951   15.947  15.892  1.00 4.18  ?  193 TRP A CB    1 
ATOM   1539 C  CG    . TRP A 1 194 ? 4.918   14.856  16.299  1.00 2.74  ?  193 TRP A CG    1 
ATOM   1540 C  CD1   . TRP A 1 194 ? 6.131   15.004  16.931  1.00 5.05  ?  193 TRP A CD1   1 
ATOM   1541 C  CD2   . TRP A 1 194 ? 4.702   13.429  16.172  1.00 4.87  ?  193 TRP A CD2   1 
ATOM   1542 N  NE1   . TRP A 1 194 ? 6.680   13.758  17.182  1.00 5.80  ?  193 TRP A NE1   1 
ATOM   1543 C  CE2   . TRP A 1 194 ? 5.818   12.793  16.723  1.00 3.75  ?  193 TRP A CE2   1 
ATOM   1544 C  CE3   . TRP A 1 194 ? 3.671   12.651  15.631  1.00 6.21  ?  193 TRP A CE3   1 
ATOM   1545 C  CZ2   . TRP A 1 194 ? 5.948   11.372  16.772  1.00 5.44  ?  193 TRP A CZ2   1 
ATOM   1546 C  CZ3   . TRP A 1 194 ? 3.779   11.247  15.707  1.00 6.04  ?  193 TRP A CZ3   1 
ATOM   1547 C  CH2   . TRP A 1 194 ? 4.926   10.645  16.266  1.00 5.40  ?  193 TRP A CH2   1 
ATOM   1548 N  N     . ARG A 1 195 ? 4.006   15.215  12.844  1.00 3.94  ?  194 ARG A N     1 
ATOM   1549 C  CA    . ARG A 1 195 ? 4.395   14.449  11.665  1.00 6.10  ?  194 ARG A CA    1 
ATOM   1550 C  C     . ARG A 1 195 ? 5.214   15.298  10.712  1.00 5.51  ?  194 ARG A C     1 
ATOM   1551 O  O     . ARG A 1 195 ? 6.288   14.880  10.245  1.00 7.02  ?  194 ARG A O     1 
ATOM   1552 C  CB    . ARG A 1 195 ? 3.141   13.939  10.948  1.00 7.53  ?  194 ARG A CB    1 
ATOM   1553 C  CG    . ARG A 1 195 ? 3.388   13.220  9.603   1.00 9.37  ?  194 ARG A CG    1 
ATOM   1554 C  CD    . ARG A 1 195 ? 2.118   13.275  8.693   1.00 12.59 ?  194 ARG A CD    1 
ATOM   1555 N  NE    . ARG A 1 195 ? 1.686   14.637  8.416   1.00 10.56 ?  194 ARG A NE    1 
ATOM   1556 C  CZ    . ARG A 1 195 ? 0.490   14.973  7.928   1.00 11.18 ?  194 ARG A CZ    1 
ATOM   1557 N  NH1   . ARG A 1 195 ? -0.434  14.041  7.689   1.00 12.05 1  194 ARG A NH1   1 
ATOM   1558 N  NH2   . ARG A 1 195 ? 0.180   16.255  7.722   1.00 11.92 ?  194 ARG A NH2   1 
ATOM   1559 N  N     . ASP A 1 196 ? 4.700   16.485  10.365  1.00 6.20  ?  195 ASP A N     1 
ATOM   1560 C  CA    . ASP A 1 196 ? 5.385   17.271  9.343   1.00 6.27  ?  195 ASP A CA    1 
ATOM   1561 C  C     . ASP A 1 196 ? 6.732   17.806  9.828   1.00 8.36  ?  195 ASP A C     1 
ATOM   1562 O  O     . ASP A 1 196 ? 7.669   18.021  9.008   1.00 9.03  ?  195 ASP A O     1 
ATOM   1563 C  CB    . ASP A 1 196 ? 4.492   18.414  8.903   1.00 5.29  ?  195 ASP A CB    1 
ATOM   1564 C  CG    . ASP A 1 196 ? 3.270   17.909  8.114   1.00 9.37  ?  195 ASP A CG    1 
ATOM   1565 O  OD1   . ASP A 1 196 ? 3.347   16.778  7.548   1.00 10.07 ?  195 ASP A OD1   1 
ATOM   1566 O  OD2   . ASP A 1 196 ? 2.232   18.610  8.058   1.00 12.85 -1 195 ASP A OD2   1 
ATOM   1567 N  N     . PHE A 1 197 ? 6.863   18.021  11.140  1.00 5.31  ?  196 PHE A N     1 
ATOM   1568 C  CA    . PHE A 1 197 ? 8.102   18.579  11.673  1.00 7.20  ?  196 PHE A CA    1 
ATOM   1569 C  C     . PHE A 1 197 ? 9.175   17.520  11.873  1.00 8.59  ?  196 PHE A C     1 
ATOM   1570 O  O     . PHE A 1 197 ? 10.363  17.770  11.591  1.00 8.05  ?  196 PHE A O     1 
ATOM   1571 C  CB    . PHE A 1 197 ? 7.807   19.292  12.992  1.00 8.15  ?  196 PHE A CB    1 
ATOM   1572 C  CG    . PHE A 1 197 ? 9.016   19.940  13.601  1.00 7.65  ?  196 PHE A CG    1 
ATOM   1573 C  CD1   . PHE A 1 197 ? 9.719   20.943  12.891  1.00 8.65  ?  196 PHE A CD1   1 
ATOM   1574 C  CD2   . PHE A 1 197 ? 9.475   19.540  14.864  1.00 7.92  ?  196 PHE A CD2   1 
ATOM   1575 C  CE1   . PHE A 1 197 ? 10.866  21.534  13.514  1.00 9.54  ?  196 PHE A CE1   1 
ATOM   1576 C  CE2   . PHE A 1 197 ? 10.589  20.107  15.466  1.00 7.73  ?  196 PHE A CE2   1 
ATOM   1577 C  CZ    . PHE A 1 197 ? 11.303  21.111  14.777  1.00 10.54 ?  196 PHE A CZ    1 
ATOM   1578 N  N     . ARG A 1 198 ? 8.791   16.334  12.346  1.00 5.42  ?  197 ARG A N     1 
ATOM   1579 C  CA    . ARG A 1 198 ? 9.791   15.343  12.696  1.00 6.57  ?  197 ARG A CA    1 
ATOM   1580 C  C     . ARG A 1 198 ? 9.907   14.187  11.721  1.00 6.30  ?  197 ARG A C     1 
ATOM   1581 O  O     . ARG A 1 198 ? 10.785  13.350  11.911  1.00 9.11  ?  197 ARG A O     1 
ATOM   1582 C  CB    . ARG A 1 198 ? 9.472   14.769  14.074  1.00 6.82  ?  197 ARG A CB    1 
ATOM   1583 C  CG    . ARG A 1 198 ? 9.504   15.783  15.210  1.00 10.42 ?  197 ARG A CG    1 
ATOM   1584 C  CD    . ARG A 1 198 ? 10.326  15.218  16.306  1.00 16.08 ?  197 ARG A CD    1 
ATOM   1585 N  NE    . ARG A 1 198 ? 11.790  15.251  16.114  1.00 11.11 ?  197 ARG A NE    1 
ATOM   1586 C  CZ    . ARG A 1 198 ? 12.592  14.521  16.900  1.00 19.32 ?  197 ARG A CZ    1 
ATOM   1587 N  NH1   . ARG A 1 198 ? 12.024  13.708  17.814  1.00 19.94 1  197 ARG A NH1   1 
ATOM   1588 N  NH2   . ARG A 1 198 ? 13.929  14.561  16.788  1.00 14.44 ?  197 ARG A NH2   1 
ATOM   1589 N  N     . PHE A 1 199 ? 9.028   14.063  10.736  1.00 5.68  ?  198 PHE A N     1 
ATOM   1590 C  CA    . PHE A 1 199 ? 9.175   13.012  9.729   1.00 9.56  ?  198 PHE A CA    1 
ATOM   1591 C  C     . PHE A 1 199 ? 9.457   13.666  8.373   1.00 21.52 ?  198 PHE A C     1 
ATOM   1592 O  O     . PHE A 1 199 ? 9.177   14.847  8.170   1.00 22.94 ?  198 PHE A O     1 
ATOM   1593 C  CB    . PHE A 1 199 ? 7.927   12.131  9.708   1.00 11.20 ?  198 PHE A CB    1 
ATOM   1594 C  CG    . PHE A 1 199 ? 7.676   11.375  11.027  1.00 8.39  ?  198 PHE A CG    1 
ATOM   1595 C  CD1   . PHE A 1 199 ? 7.216   12.038  12.144  1.00 5.32  ?  198 PHE A CD1   1 
ATOM   1596 C  CD2   . PHE A 1 199 ? 7.894   9.991   11.137  1.00 8.71  ?  198 PHE A CD2   1 
ATOM   1597 C  CE1   . PHE A 1 199 ? 6.964   11.414  13.345  1.00 7.21  ?  198 PHE A CE1   1 
ATOM   1598 C  CE2   . PHE A 1 199 ? 7.633   9.326   12.350  1.00 9.99  ?  198 PHE A CE2   1 
ATOM   1599 C  CZ    . PHE A 1 199 ? 7.181   10.014  13.465  1.00 9.27  ?  198 PHE A CZ    1 
ATOM   1600 N  N     . SER A 1 200 ? 10.097  12.939  7.468   1.00 34.58 ?  199 SER A N     1 
ATOM   1601 C  CA    . SER A 1 200 ? 10.522  13.609  6.236   1.00 47.03 ?  199 SER A CA    1 
ATOM   1602 C  C     . SER A 1 200 ? 9.348   13.850  5.286   1.00 56.92 ?  199 SER A C     1 
ATOM   1603 O  O     . SER A 1 200 ? 8.293   13.212  5.376   1.00 57.79 ?  199 SER A O     1 
ATOM   1604 C  CB    . SER A 1 200 ? 11.604  12.806  5.516   1.00 49.70 ?  199 SER A CB    1 
ATOM   1605 O  OG    . SER A 1 200 ? 12.819  12.852  6.235   1.00 51.31 ?  199 SER A OG    1 
ATOM   1606 N  N     . SER A 1 201 ? 9.558   14.797  4.342   1.00 64.45 ?  200 SER A N     1 
ATOM   1607 C  CA    . SER A 1 201 ? 8.578   15.194  3.323   1.00 70.94 ?  200 SER A CA    1 
ATOM   1608 C  C     . SER A 1 201 ? 8.440   14.195  2.222   1.00 74.76 ?  200 SER A C     1 
ATOM   1609 O  O     . SER A 1 201 ? 7.824   14.526  1.198   1.00 75.43 ?  200 SER A O     1 
ATOM   1610 C  CB    . SER A 1 201 ? 8.946   16.551  2.730   1.00 74.11 ?  200 SER A CB    1 
ATOM   1611 O  OG    . SER A 1 201 ? 8.150   17.577  3.294   1.00 75.97 ?  200 SER A OG    1 
ATOM   1612 N  N     . ASP A 1 202 ? 9.014   13.006  2.393   1.00 77.36 ?  201 ASP A N     1 
ATOM   1613 C  CA    . ASP A 1 202 ? 8.737   11.877  1.526   1.00 79.17 ?  201 ASP A CA    1 
ATOM   1614 C  C     . ASP A 1 202 ? 7.557   11.084  2.096   1.00 79.29 ?  201 ASP A C     1 
ATOM   1615 O  O     . ASP A 1 202 ? 7.032   11.381  3.175   1.00 79.63 ?  201 ASP A O     1 
ATOM   1616 C  CB    . ASP A 1 202 ? 9.989   11.009  1.350   1.00 80.71 ?  201 ASP A CB    1 
ATOM   1617 C  CG    . ASP A 1 202 ? 10.486  10.387  2.662   1.00 81.70 ?  201 ASP A CG    1 
ATOM   1618 O  OD1   . ASP A 1 202 ? 9.934   10.692  3.740   1.00 81.96 ?  201 ASP A OD1   1 
ATOM   1619 O  OD2   . ASP A 1 202 ? 11.443  9.581   2.610   1.00 82.15 -1 201 ASP A OD2   1 
ATOM   1620 N  N     . GLY A 1 203 ? 7.141   10.056  1.369   1.00 78.38 ?  202 GLY A N     1 
ATOM   1621 C  CA    . GLY A 1 203 ? 5.968   9.286   1.711   1.00 76.06 ?  202 GLY A CA    1 
ATOM   1622 C  C     . GLY A 1 203 ? 6.149   8.198   2.749   1.00 74.16 ?  202 GLY A C     1 
ATOM   1623 O  O     . GLY A 1 203 ? 5.192   7.457   3.002   1.00 74.98 ?  202 GLY A O     1 
ATOM   1624 N  N     . ASN A 1 204 ? 7.332   8.058   3.362   1.00 70.02 ?  203 ASN A N     1 
ATOM   1625 C  CA    . ASN A 1 204 ? 7.452   7.095   4.456   1.00 65.31 ?  203 ASN A CA    1 
ATOM   1626 C  C     . ASN A 1 204 ? 6.492   7.441   5.588   1.00 58.58 ?  203 ASN A C     1 
ATOM   1627 O  O     . ASN A 1 204 ? 5.958   6.541   6.249   1.00 57.73 ?  203 ASN A O     1 
ATOM   1628 C  CB    . ASN A 1 204 ? 8.907   7.014   4.951   1.00 66.53 ?  203 ASN A CB    1 
ATOM   1629 C  CG    . ASN A 1 204 ? 9.176   7.829   6.230   1.00 67.63 ?  203 ASN A CG    1 
ATOM   1630 O  OD1   . ASN A 1 204 ? 8.823   9.011   6.339   1.00 67.80 ?  203 ASN A OD1   1 
ATOM   1631 N  ND2   . ASN A 1 204 ? 9.839   7.192   7.192   1.00 67.95 ?  203 ASN A ND2   1 
ATOM   1632 N  N     . ALA A 1 205 ? 6.240   8.736   5.803   1.00 52.30 ?  204 ALA A N     1 
ATOM   1633 C  CA    . ALA A 1 205 ? 5.263   9.213   6.770   1.00 46.90 ?  204 ALA A CA    1 
ATOM   1634 C  C     . ALA A 1 205 ? 3.907   9.508   6.136   1.00 42.24 ?  204 ALA A C     1 
ATOM   1635 O  O     . ALA A 1 205 ? 3.044   10.082  6.803   1.00 41.24 ?  204 ALA A O     1 
ATOM   1636 C  CB    . ALA A 1 205 ? 5.786   10.463  7.474   1.00 44.68 ?  204 ALA A CB    1 
ATOM   1637 N  N     . ALA A 1 206 ? 3.711   9.132   4.869   1.00 40.26 ?  205 ALA A N     1 
ATOM   1638 C  CA    . ALA A 1 206 ? 2.413   9.329   4.225   1.00 39.58 ?  205 ALA A CA    1 
ATOM   1639 C  C     . ALA A 1 206 ? 1.246   8.671   4.962   1.00 37.35 ?  205 ALA A C     1 
ATOM   1640 O  O     . ALA A 1 206 ? 0.175   9.297   5.035   1.00 37.85 ?  205 ALA A O     1 
ATOM   1641 C  CB    . ALA A 1 206 ? 2.472   8.837   2.773   1.00 40.67 ?  205 ALA A CB    1 
ATOM   1642 N  N     . PRO A 1 207 ? 1.351   7.451   5.502   1.00 32.90 ?  206 PRO A N     1 
ATOM   1643 C  CA    . PRO A 1 207 ? 0.208   6.918   6.254   1.00 27.92 ?  206 PRO A CA    1 
ATOM   1644 C  C     . PRO A 1 207 ? 0.011   7.539   7.631   1.00 20.26 ?  206 PRO A C     1 
ATOM   1645 O  O     . PRO A 1 207 ? -0.975  7.183   8.287   1.00 19.12 ?  206 PRO A O     1 
ATOM   1646 C  CB    . PRO A 1 207 ? 0.510   5.411   6.365   1.00 31.63 ?  206 PRO A CB    1 
ATOM   1647 C  CG    . PRO A 1 207 ? 1.949   5.257   6.038   1.00 33.22 ?  206 PRO A CG    1 
ATOM   1648 C  CD    . PRO A 1 207 ? 2.336   6.401   5.172   1.00 33.66 ?  206 PRO A CD    1 
ATOM   1649 N  N     . LEU A 1 208 ? 0.888   8.432   8.115   1.00 13.30 ?  207 LEU A N     1 
ATOM   1650 C  CA    . LEU A 1 208 ? 0.679   8.955   9.458   1.00 13.95 ?  207 LEU A CA    1 
ATOM   1651 C  C     . LEU A 1 208 ? -0.631  9.763   9.560   1.00 14.82 ?  207 LEU A C     1 
ATOM   1652 O  O     . LEU A 1 208 ? -1.311  9.706   10.593  1.00 14.85 ?  207 LEU A O     1 
ATOM   1653 C  CB    . LEU A 1 208 ? 1.863   9.802   9.910   1.00 17.41 ?  207 LEU A CB    1 
ATOM   1654 C  CG    . LEU A 1 208 ? 3.031   8.986   10.512  1.00 24.41 ?  207 LEU A CG    1 
ATOM   1655 C  CD1   . LEU A 1 208 ? 4.180   9.887   11.007  1.00 25.06 ?  207 LEU A CD1   1 
ATOM   1656 C  CD2   . LEU A 1 208 ? 2.577   8.155   11.658  1.00 23.42 ?  207 LEU A CD2   1 
ATOM   1657 N  N     . GLY A 1 209 ? -0.997  10.532  8.511   1.00 10.91 ?  208 GLY A N     1 
ATOM   1658 C  CA    . GLY A 1 209 ? -2.185  11.378  8.588   1.00 11.41 ?  208 GLY A CA    1 
ATOM   1659 C  C     . GLY A 1 209 ? -3.466  10.593  8.890   1.00 13.17 ?  208 GLY A C     1 
ATOM   1660 O  O     . GLY A 1 209 ? -4.111  10.741  9.956   1.00 10.73 ?  208 GLY A O     1 
ATOM   1661 N  N     . ILE A 1 210 ? -3.816  9.728   7.943   1.00 13.14 ?  209 ILE A N     1 
ATOM   1662 C  CA    . ILE A 1 210 ? -4.965  8.844   8.129   1.00 14.05 ?  209 ILE A CA    1 
ATOM   1663 C  C     . ILE A 1 210 ? -4.727  7.903   9.307   1.00 12.33 ?  209 ILE A C     1 
ATOM   1664 O  O     . ILE A 1 210 ? -5.653  7.637   10.099  1.00 13.08 ?  209 ILE A O     1 
ATOM   1665 C  CB    . ILE A 1 210 ? -5.272  8.074   6.830   1.00 18.63 ?  209 ILE A CB    1 
ATOM   1666 C  CG1   . ILE A 1 210 ? -6.452  7.139   7.030   1.00 18.60 ?  209 ILE A CG1   1 
ATOM   1667 C  CG2   . ILE A 1 210 ? -4.079  7.217   6.410   1.00 18.85 ?  209 ILE A CG2   1 
ATOM   1668 C  CD1   . ILE A 1 210 ? -7.697  7.828   7.455   1.00 19.24 ?  209 ILE A CD1   1 
ATOM   1669 N  N     . GLY A 1 211 ? -3.482  7.452   9.500   1.00 9.38  ?  210 GLY A N     1 
ATOM   1670 C  CA    . GLY A 1 211 ? -3.212  6.551   10.610  1.00 9.66  ?  210 GLY A CA    1 
ATOM   1671 C  C     . GLY A 1 211 ? -3.487  7.220   11.944  1.00 11.19 ?  210 GLY A C     1 
ATOM   1672 O  O     . GLY A 1 211 ? -4.144  6.645   12.830  1.00 9.04  ?  210 GLY A O     1 
ATOM   1673 N  N     . LEU A 1 212 ? -3.031  8.478   12.084  1.00 8.00  ?  211 LEU A N     1 
ATOM   1674 C  CA    . LEU A 1 212 ? -3.255  9.104   13.381  1.00 6.14  ?  211 LEU A CA    1 
ATOM   1675 C  C     . LEU A 1 212 ? -4.725  9.444   13.549  1.00 6.51  ?  211 LEU A C     1 
ATOM   1676 O  O     . LEU A 1 212 ? -5.234  9.397   14.679  1.00 7.03  ?  211 LEU A O     1 
ATOM   1677 C  CB    . LEU A 1 212 ? -2.411  10.369  13.570  1.00 10.06 ?  211 LEU A CB    1 
ATOM   1678 C  CG    . LEU A 1 212 ? -0.890  10.137  13.602  1.00 11.24 ?  211 LEU A CG    1 
ATOM   1679 C  CD1   . LEU A 1 212 ? -0.251  11.464  13.117  1.00 15.33 ?  211 LEU A CD1   1 
ATOM   1680 C  CD2   . LEU A 1 212 ? -0.465  9.811   15.006  1.00 14.33 ?  211 LEU A CD2   1 
ATOM   1681 N  N     . THR A 1 213 ? -5.442  9.682   12.437  1.00 6.89  ?  212 THR A N     1 
ATOM   1682 C  CA    . THR A 1 213 ? -6.873  9.961   12.563  1.00 5.70  ?  212 THR A CA    1 
ATOM   1683 C  C     . THR A 1 213 ? -7.607  8.725   13.020  1.00 5.73  ?  212 THR A C     1 
ATOM   1684 O  O     . THR A 1 213 ? -8.448  8.793   13.940  1.00 5.94  ?  212 THR A O     1 
ATOM   1685 C  CB    . THR A 1 213 ? -7.421  10.473  11.226  1.00 6.91  ?  212 THR A CB    1 
ATOM   1686 O  OG1   . THR A 1 213 ? -6.662  11.632  10.855  1.00 5.66  ?  212 THR A OG1   1 
ATOM   1687 C  CG2   . THR A 1 213 ? -8.932  10.852  11.277  1.00 6.89  ?  212 THR A CG2   1 
ATOM   1688 N  N     . ALA A 1 214 ? -7.270  7.579   12.413  1.00 6.10  ?  213 ALA A N     1 
ATOM   1689 C  CA    . ALA A 1 214 ? -7.935  6.344   12.823  1.00 7.03  ?  213 ALA A CA    1 
ATOM   1690 C  C     . ALA A 1 214 ? -7.485  5.947   14.223  1.00 7.53  ?  213 ALA A C     1 
ATOM   1691 O  O     . ALA A 1 214 ? -8.315  5.517   15.037  1.00 8.14  ?  213 ALA A O     1 
ATOM   1692 C  CB    . ALA A 1 214 ? -7.674  5.222   11.806  1.00 7.65  ?  213 ALA A CB    1 
ATOM   1693 N  N     . ALA A 1 215 ? -6.223  6.234   14.565  1.00 6.80  ?  214 ALA A N     1 
ATOM   1694 C  CA    . ALA A 1 215 ? -5.786  5.915   15.921  1.00 8.07  ?  214 ALA A CA    1 
ATOM   1695 C  C     . ALA A 1 215 ? -6.598  6.718   16.915  1.00 7.12  ?  214 ALA A C     1 
ATOM   1696 O  O     . ALA A 1 215 ? -7.015  6.205   17.955  1.00 7.26  ?  214 ALA A O     1 
ATOM   1697 C  CB    . ALA A 1 215 ? -4.295  6.226   16.077  1.00 9.10  ?  214 ALA A CB    1 
ATOM   1698 N  N     . ALA A 1 216 ? -6.847  7.985   16.599  1.00 7.95  ?  215 ALA A N     1 
ATOM   1699 C  CA    . ALA A 1 216 ? -7.600  8.823   17.523  1.00 7.44  ?  215 ALA A CA    1 
ATOM   1700 C  C     . ALA A 1 216 ? -9.029  8.339   17.626  1.00 7.69  ?  215 ALA A C     1 
ATOM   1701 O  O     . ALA A 1 216 ? -9.598  8.303   18.730  1.00 8.40  ?  215 ALA A O     1 
ATOM   1702 C  CB    . ALA A 1 216 ? -7.586  10.292  17.056  1.00 7.50  ?  215 ALA A CB    1 
ATOM   1703 N  N     . TYR A 1 217 ? -9.601  7.890   16.503  1.00 7.20  ?  216 TYR A N     1 
ATOM   1704 C  CA    . TYR A 1 217 ? -10.935 7.300   16.585  1.00 5.83  ?  216 TYR A CA    1 
ATOM   1705 C  C     . TYR A 1 217 ? -10.975 6.153   17.595  1.00 5.66  ?  216 TYR A C     1 
ATOM   1706 O  O     . TYR A 1 217 ? -11.918 6.063   18.403  1.00 7.59  ?  216 TYR A O     1 
ATOM   1707 C  CB    . TYR A 1 217 ? -11.380 6.791   15.216  1.00 4.80  ?  216 TYR A CB    1 
ATOM   1708 C  CG    . TYR A 1 217 ? -12.667 6.008   15.297  1.00 8.29  ?  216 TYR A CG    1 
ATOM   1709 C  CD1   . TYR A 1 217 ? -13.897 6.666   15.229  1.00 10.48 ?  216 TYR A CD1   1 
ATOM   1710 C  CD2   . TYR A 1 217 ? -12.654 4.607   15.400  1.00 11.15 ?  216 TYR A CD2   1 
ATOM   1711 C  CE1   . TYR A 1 217 ? -15.078 5.962   15.275  1.00 12.54 ?  216 TYR A CE1   1 
ATOM   1712 C  CE2   . TYR A 1 217 ? -13.854 3.884   15.452  1.00 11.86 ?  216 TYR A CE2   1 
ATOM   1713 C  CZ    . TYR A 1 217 ? -15.052 4.578   15.407  1.00 15.02 ?  216 TYR A CZ    1 
ATOM   1714 O  OH    . TYR A 1 217 ? -16.230 3.883   15.468  1.00 15.81 ?  216 TYR A OH    1 
ATOM   1715 N  N     . TRP A 1 218 ? -9.966  5.289   17.597  1.00 5.58  ?  217 TRP A N     1 
ATOM   1716 C  CA    . TRP A 1 218 ? -10.054 4.172   18.542  1.00 7.61  ?  217 TRP A CA    1 
ATOM   1717 C  C     . TRP A 1 218 ? -9.694  4.597   19.955  1.00 9.41  ?  217 TRP A C     1 
ATOM   1718 O  O     . TRP A 1 218 ? -10.303 4.101   20.910  1.00 11.67 ?  217 TRP A O     1 
ATOM   1719 C  CB    . TRP A 1 218 ? -9.129  3.036   18.121  1.00 9.26  ?  217 TRP A CB    1 
ATOM   1720 C  CG    . TRP A 1 218 ? -9.546  2.398   16.882  1.00 8.51  ?  217 TRP A CG    1 
ATOM   1721 C  CD1   . TRP A 1 218 ? -8.871  2.413   15.709  1.00 8.50  ?  217 TRP A CD1   1 
ATOM   1722 C  CD2   . TRP A 1 218 ? -10.718 1.605   16.670  1.00 10.04 ?  217 TRP A CD2   1 
ATOM   1723 N  NE1   . TRP A 1 218 ? -9.575  1.715   14.751  1.00 12.44 ?  217 TRP A NE1   1 
ATOM   1724 C  CE2   . TRP A 1 218 ? -10.698 1.191   15.324  1.00 12.01 ?  217 TRP A CE2   1 
ATOM   1725 C  CE3   . TRP A 1 218 ? -11.797 1.216   17.487  1.00 13.52 ?  217 TRP A CE3   1 
ATOM   1726 C  CZ2   . TRP A 1 218 ? -11.698 0.402   14.768  1.00 13.11 ?  217 TRP A CZ2   1 
ATOM   1727 C  CZ3   . TRP A 1 218 ? -12.816 0.435   16.918  1.00 13.77 ?  217 TRP A CZ3   1 
ATOM   1728 C  CH2   . TRP A 1 218 ? -12.750 0.048   15.571  1.00 15.16 ?  217 TRP A CH2   1 
ATOM   1729 N  N     . TRP A 1 219 ? -8.749  5.537   20.124  1.00 8.14  ?  218 TRP A N     1 
ATOM   1730 C  CA    . TRP A 1 219 ? -8.067  5.631   21.420  1.00 8.38  ?  218 TRP A CA    1 
ATOM   1731 C  C     . TRP A 1 219 ? -8.078  7.006   22.054  1.00 10.95 ?  218 TRP A C     1 
ATOM   1732 O  O     . TRP A 1 219 ? -7.664  7.134   23.223  1.00 11.03 ?  218 TRP A O     1 
ATOM   1733 C  CB    . TRP A 1 219 ? -6.595  5.202   21.292  1.00 9.84  ?  218 TRP A CB    1 
ATOM   1734 C  CG    . TRP A 1 219 ? -6.433  3.763   20.947  1.00 9.56  ?  218 TRP A CG    1 
ATOM   1735 C  CD1   . TRP A 1 219 ? -7.085  2.702   21.550  1.00 12.84 ?  218 TRP A CD1   1 
ATOM   1736 C  CD2   . TRP A 1 219 ? -5.588  3.192   19.946  1.00 9.48  ?  218 TRP A CD2   1 
ATOM   1737 N  NE1   . TRP A 1 219 ? -6.678  1.508   20.970  1.00 11.49 ?  218 TRP A NE1   1 
ATOM   1738 C  CE2   . TRP A 1 219 ? -5.752  1.778   20.003  1.00 11.55 ?  218 TRP A CE2   1 
ATOM   1739 C  CE3   . TRP A 1 219 ? -4.691  3.720   19.028  1.00 10.82 ?  218 TRP A CE3   1 
ATOM   1740 C  CZ2   . TRP A 1 219 ? -5.077  0.913   19.161  1.00 13.42 ?  218 TRP A CZ2   1 
ATOM   1741 C  CZ3   . TRP A 1 219 ? -4.011  2.851   18.191  1.00 14.11 ?  218 TRP A CZ3   1 
ATOM   1742 C  CH2   . TRP A 1 219 ? -4.202  1.466   18.264  1.00 13.40 ?  218 TRP A CH2   1 
ATOM   1743 N  N     . PHE A 1 220 ? -8.485  8.056   21.336  1.00 8.06  ?  219 PHE A N     1 
ATOM   1744 C  CA    . PHE A 1 220 ? -8.498  9.360   21.979  1.00 10.15 ?  219 PHE A CA    1 
ATOM   1745 C  C     . PHE A 1 220 ? -9.534  9.422   23.089  1.00 9.71  ?  219 PHE A C     1 
ATOM   1746 O  O     . PHE A 1 220 ? -10.636 8.888   22.963  1.00 12.26 ?  219 PHE A O     1 
ATOM   1747 C  CB    . PHE A 1 220 ? -8.817  10.446  20.959  1.00 9.32  ?  219 PHE A CB    1 
ATOM   1748 C  CG    . PHE A 1 220 ? -8.969  11.809  21.575  1.00 6.29  ?  219 PHE A CG    1 
ATOM   1749 C  CD1   . PHE A 1 220 ? -7.845  12.587  21.833  1.00 7.78  ?  219 PHE A CD1   1 
ATOM   1750 C  CD2   . PHE A 1 220 ? -10.218 12.296  21.904  1.00 6.92  ?  219 PHE A CD2   1 
ATOM   1751 C  CE1   . PHE A 1 220 ? -7.978  13.836  22.438  1.00 6.92  ?  219 PHE A CE1   1 
ATOM   1752 C  CE2   . PHE A 1 220 ? -10.348 13.574  22.499  1.00 7.35  ?  219 PHE A CE2   1 
ATOM   1753 C  CZ    . PHE A 1 220 ? -9.236  14.298  22.752  1.00 7.36  ?  219 PHE A CZ    1 
ATOM   1754 N  N     . GLN A 1 221 ? -9.170  10.093  24.175  1.00 7.33  ?  220 GLN A N     1 
ATOM   1755 C  CA    . GLN A 1 221 ? -10.097 10.392  25.258  1.00 9.20  ?  220 GLN A CA    1 
ATOM   1756 C  C     . GLN A 1 221 ? -9.980  11.850  25.624  1.00 9.91  ?  220 GLN A C     1 
ATOM   1757 O  O     . GLN A 1 221 ? -8.872  12.391  25.728  1.00 11.23 ?  220 GLN A O     1 
ATOM   1758 C  CB    . GLN A 1 221 ? -9.811  9.537   26.505  1.00 12.06 ?  220 GLN A CB    1 
ATOM   1759 C  CG    . GLN A 1 221 ? -9.789  8.066   26.274  1.00 15.15 ?  220 GLN A CG    1 
ATOM   1760 C  CD    . GLN A 1 221 ? -11.156 7.448   26.065  1.00 19.14 ?  220 GLN A CD    1 
ATOM   1761 O  OE1   . GLN A 1 221 ? -11.258 6.351   25.529  1.00 22.77 ?  220 GLN A OE1   1 
ATOM   1762 N  NE2   . GLN A 1 221 ? -12.202 8.134   26.480  1.00 21.25 ?  220 GLN A NE2   1 
ATOM   1763 N  N     . VAL A 1 222 ? -11.132 12.497  25.820  1.00 8.37  ?  221 VAL A N     1 
ATOM   1764 C  CA    . VAL A 1 222 ? -11.143 13.878  26.276  1.00 8.87  ?  221 VAL A CA    1 
ATOM   1765 C  C     . VAL A 1 222 ? -10.393 14.031  27.592  1.00 8.56  ?  221 VAL A C     1 
ATOM   1766 O  O     . VAL A 1 222 ? -10.394 13.143  28.457  1.00 14.09 ?  221 VAL A O     1 
ATOM   1767 C  CB    . VAL A 1 222 ? -12.607 14.343  26.398  1.00 11.13 ?  221 VAL A CB    1 
ATOM   1768 C  CG1   . VAL A 1 222 ? -12.749 15.710  27.035  1.00 11.75 ?  221 VAL A CG1   1 
ATOM   1769 C  CG2   . VAL A 1 222 ? -13.245 14.363  25.027  1.00 11.87 ?  221 VAL A CG2   1 
ATOM   1770 N  N     . SER A 1 223 ? -9.732  15.166  27.743  1.00 7.40  ?  222 SER A N     1 
ATOM   1771 C  CA    . SER A 1 223 ? -9.239  15.567  29.068  1.00 7.46  ?  222 SER A CA    1 
ATOM   1772 C  C     . SER A 1 223 ? -9.803  16.942  29.379  1.00 9.13  ?  222 SER A C     1 
ATOM   1773 O  O     . SER A 1 223 ? -9.387  17.936  28.794  1.00 9.46  ?  222 SER A O     1 
ATOM   1774 C  CB    . SER A 1 223 ? -7.714  15.587  29.128  1.00 10.42 ?  222 SER A CB    1 
ATOM   1775 O  OG    . SER A 1 223 ? -7.263  15.977  30.456  1.00 9.15  ?  222 SER A OG    1 
ATOM   1776 N  N     . LYS A 1 224 ? -10.699 17.002  30.364  1.00 12.56 ?  223 LYS A N     1 
ATOM   1777 C  CA    . LYS A 1 224 ? -11.219 18.269  30.844  1.00 14.56 ?  223 LYS A CA    1 
ATOM   1778 C  C     . LYS A 1 224 ? -11.520 18.126  32.324  1.00 17.36 ?  223 LYS A C     1 
ATOM   1779 O  O     . LYS A 1 224 ? -11.641 17.022  32.858  1.00 15.96 ?  223 LYS A O     1 
ATOM   1780 C  CB    . LYS A 1 224 ? -12.495 18.690  30.098  1.00 13.01 ?  223 LYS A CB    1 
ATOM   1781 C  CG    . LYS A 1 224 ? -13.630 17.674  30.255  1.00 14.22 ?  223 LYS A CG    1 
ATOM   1782 C  CD    . LYS A 1 224 ? -14.804 17.956  29.304  1.00 16.69 ?  223 LYS A CD    1 
ATOM   1783 C  CE    . LYS A 1 224 ? -15.900 16.942  29.551  1.00 14.11 ?  223 LYS A CE    1 
ATOM   1784 N  NZ    . LYS A 1 224 ? -17.072 17.031  28.607  1.00 14.71 1  223 LYS A NZ    1 
ATOM   1785 N  N     . ARG A 1 225 ? -11.660 19.259  32.971  1.00 18.51 ?  224 ARG A N     1 
ATOM   1786 C  CA    . ARG A 1 225 ? -12.091 19.302  34.363  1.00 22.39 ?  224 ARG A CA    1 
ATOM   1787 C  C     . ARG A 1 225 ? -13.390 20.080  34.451  1.00 21.19 ?  224 ARG A C     1 
ATOM   1788 O  O     . ARG A 1 225 ? -13.551 21.103  33.771  1.00 20.07 ?  224 ARG A O     1 
ATOM   1789 C  CB    . ARG A 1 225 ? -11.034 19.979  35.224  1.00 27.62 ?  224 ARG A CB    1 
ATOM   1790 C  CG    . ARG A 1 225 ? -9.700  19.293  35.274  1.00 35.22 ?  224 ARG A CG    1 
ATOM   1791 C  CD    . ARG A 1 225 ? -8.837  20.035  36.279  1.00 42.10 ?  224 ARG A CD    1 
ATOM   1792 N  NE    . ARG A 1 225 ? -7.410  19.779  36.104  1.00 49.10 ?  224 ARG A NE    1 
ATOM   1793 C  CZ    . ARG A 1 225 ? -6.703  18.935  36.850  1.00 53.87 ?  224 ARG A CZ    1 
ATOM   1794 N  NH1   . ARG A 1 225 ? -7.294  18.257  37.831  1.00 55.43 1  224 ARG A NH1   1 
ATOM   1795 N  NH2   . ARG A 1 225 ? -5.406  18.770  36.615  1.00 55.06 ?  224 ARG A NH2   1 
ATOM   1796 N  N     . THR A 1 226 ? -14.290 19.635  35.336  1.00 23.54 ?  225 THR A N     1 
ATOM   1797 C  CA    . THR A 1 226 ? -15.562 20.311  35.573  1.00 24.14 ?  225 THR A CA    1 
ATOM   1798 C  C     . THR A 1 226 ? -15.610 20.727  37.032  1.00 23.46 ?  225 THR A C     1 
ATOM   1799 O  O     . THR A 1 226 ? -15.429 19.889  37.929  1.00 25.80 ?  225 THR A O     1 
ATOM   1800 C  CB    . THR A 1 226 ? -16.744 19.405  35.241  1.00 28.10 ?  225 THR A CB    1 
ATOM   1801 O  OG1   . THR A 1 226 ? -16.624 18.972  33.877  1.00 29.20 ?  225 THR A OG1   1 
ATOM   1802 C  CG2   . THR A 1 226 ? -18.062 20.158  35.433  1.00 28.05 ?  225 THR A CG2   1 
ATOM   1803 N  N     . ASP A 1 227 ? -15.791 22.000  37.272  1.00 22.92 ?  226 ASP A N     1 
ATOM   1804 C  CA    . ASP A 1 227 ? -15.790 22.446  38.662  1.00 25.65 ?  226 ASP A CA    1 
ATOM   1805 C  C     . ASP A 1 227 ? -17.057 21.928  39.329  1.00 26.19 ?  226 ASP A C     1 
ATOM   1806 O  O     . ASP A 1 227 ? -18.158 22.149  38.802  1.00 25.56 ?  226 ASP A O     1 
ATOM   1807 C  CB    . ASP A 1 227 ? -15.702 23.954  38.733  1.00 27.25 ?  226 ASP A CB    1 
ATOM   1808 C  CG    . ASP A 1 227 ? -15.577 24.452  40.130  1.00 34.80 ?  226 ASP A CG    1 
ATOM   1809 O  OD1   . ASP A 1 227 ? -16.576 24.370  40.889  1.00 34.34 ?  226 ASP A OD1   1 
ATOM   1810 O  OD2   . ASP A 1 227 ? -14.469 24.903  40.473  1.00 40.70 -1 226 ASP A OD2   1 
ATOM   1811 N  N     . PRO A 1 228 ? -16.950 21.217  40.461  1.00 30.30 ?  227 PRO A N     1 
ATOM   1812 C  CA    . PRO A 1 228 ? -18.148 20.638  41.093  1.00 30.89 ?  227 PRO A CA    1 
ATOM   1813 C  C     . PRO A 1 228 ? -19.154 21.662  41.597  1.00 31.80 ?  227 PRO A C     1 
ATOM   1814 O  O     . PRO A 1 228 ? -20.284 21.269  41.916  1.00 34.07 ?  227 PRO A O     1 
ATOM   1815 C  CB    . PRO A 1 228 ? -17.570 19.823  42.262  1.00 32.39 ?  227 PRO A CB    1 
ATOM   1816 C  CG    . PRO A 1 228 ? -16.238 20.445  42.541  1.00 32.14 ?  227 PRO A CG    1 
ATOM   1817 C  CD    . PRO A 1 228 ? -15.718 20.865  41.195  1.00 30.06 ?  227 PRO A CD    1 
ATOM   1818 N  N     . VAL A 1 229 ? -18.798 22.943  41.695  1.00 29.57 ?  228 VAL A N     1 
ATOM   1819 C  CA    . VAL A 1 229 ? -19.707 23.976  42.186  1.00 27.62 ?  228 VAL A CA    1 
ATOM   1820 C  C     . VAL A 1 229 ? -20.187 24.869  41.055  1.00 26.58 ?  228 VAL A C     1 
ATOM   1821 O  O     . VAL A 1 229 ? -21.397 25.020  40.837  1.00 27.28 ?  228 VAL A O     1 
ATOM   1822 C  CB    . VAL A 1 229 ? -19.060 24.810  43.319  1.00 29.50 ?  228 VAL A CB    1 
ATOM   1823 C  CG1   . VAL A 1 229 ? -20.024 25.905  43.779  1.00 28.46 ?  228 VAL A CG1   1 
ATOM   1824 C  CG2   . VAL A 1 229 ? -18.626 23.921  44.472  1.00 28.85 ?  228 VAL A CG2   1 
ATOM   1825 N  N     . SER A 1 230 ? -19.257 25.469  40.310  1.00 24.30 ?  229 SER A N     1 
ATOM   1826 C  CA    . SER A 1 230 ? -19.645 26.385  39.248  1.00 22.90 ?  229 SER A CA    1 
ATOM   1827 C  C     . SER A 1 230 ? -20.024 25.672  37.966  1.00 21.88 ?  229 SER A C     1 
ATOM   1828 O  O     . SER A 1 230 ? -20.597 26.318  37.077  1.00 22.05 ?  229 SER A O     1 
ATOM   1829 C  CB    . SER A 1 230 ? -18.519 27.369  38.934  1.00 24.13 ?  229 SER A CB    1 
ATOM   1830 O  OG    . SER A 1 230 ? -17.450 26.687  38.301  1.00 25.91 ?  229 SER A OG    1 
ATOM   1831 N  N     . GLN A 1 231 ? -19.692 24.386  37.847  1.00 19.44 ?  230 GLN A N     1 
ATOM   1832 C  CA    . GLN A 1 231 ? -19.854 23.602  36.615  1.00 20.60 ?  230 GLN A CA    1 
ATOM   1833 C  C     . GLN A 1 231 ? -19.025 24.133  35.438  1.00 20.99 ?  230 GLN A C     1 
ATOM   1834 O  O     . GLN A 1 231 ? -19.254 23.727  34.291  1.00 19.43 ?  230 GLN A O     1 
ATOM   1835 C  CB    . GLN A 1 231 ? -21.331 23.509  36.195  1.00 22.62 ?  230 GLN A CB    1 
ATOM   1836 C  CG    . GLN A 1 231 ? -22.247 22.874  37.257  1.00 24.72 ?  230 GLN A CG    1 
ATOM   1837 C  CD    . GLN A 1 231 ? -23.709 22.989  36.849  1.00 24.44 ?  230 GLN A CD    1 
ATOM   1838 O  OE1   . GLN A 1 231 ? -24.046 23.752  35.938  1.00 25.45 ?  230 GLN A OE1   1 
ATOM   1839 N  NE2   . GLN A 1 231 ? -24.576 22.232  37.509  1.00 26.63 ?  230 GLN A NE2   1 
ATOM   1840 N  N     . ASN A 1 232 ? -18.078 25.024  35.692  1.00 17.82 ?  231 ASN A N     1 
ATOM   1841 C  CA    . ASN A 1 232 ? -17.211 25.578  34.656  1.00 20.81 ?  231 ASN A CA    1 
ATOM   1842 C  C     . ASN A 1 232 ? -16.238 24.512  34.152  1.00 18.93 ?  231 ASN A C     1 
ATOM   1843 O  O     . ASN A 1 232 ? -15.625 23.801  34.955  1.00 19.96 ?  231 ASN A O     1 
ATOM   1844 C  CB    . ASN A 1 232 ? -16.432 26.764  35.226  1.00 23.86 ?  231 ASN A CB    1 
ATOM   1845 C  CG    . ASN A 1 232 ? -15.590 27.443  34.183  1.00 29.71 ?  231 ASN A CG    1 
ATOM   1846 O  OD1   . ASN A 1 232 ? -16.110 27.952  33.192  1.00 37.17 ?  231 ASN A OD1   1 
ATOM   1847 N  ND2   . ASN A 1 232 ? -14.274 27.453  34.389  1.00 30.56 ?  231 ASN A ND2   1 
ATOM   1848 N  N     . VAL A 1 233 ? -16.070 24.428  32.824  1.00 15.81 ?  232 VAL A N     1 
ATOM   1849 C  CA    . VAL A 1 233 ? -15.293 23.372  32.176  1.00 15.84 ?  232 VAL A CA    1 
ATOM   1850 C  C     . VAL A 1 233 ? -14.013 23.958  31.584  1.00 13.93 ?  232 VAL A C     1 
ATOM   1851 O  O     . VAL A 1 233 ? -14.054 24.967  30.871  1.00 16.15 ?  232 VAL A O     1 
ATOM   1852 C  CB    . VAL A 1 233 ? -16.130 22.669  31.094  1.00 18.24 ?  232 VAL A CB    1 
ATOM   1853 C  CG1   . VAL A 1 233 ? -15.271 21.682  30.317  1.00 17.77 ?  232 VAL A CG1   1 
ATOM   1854 C  CG2   . VAL A 1 233 ? -17.319 21.916  31.745  1.00 17.94 ?  232 VAL A CG2   1 
ATOM   1855 N  N     . THR A 1 234 ? -12.866 23.327  31.886  1.00 13.62 ?  233 THR A N     1 
ATOM   1856 C  CA    . THR A 1 234 ? -11.608 23.689  31.230  1.00 15.24 ?  233 THR A CA    1 
ATOM   1857 C  C     . THR A 1 234 ? -10.993 22.453  30.570  1.00 13.85 ?  233 THR A C     1 
ATOM   1858 O  O     . THR A 1 234 ? -11.070 21.347  31.099  1.00 15.60 ?  233 THR A O     1 
ATOM   1859 C  CB    . THR A 1 234 ? -10.590 24.333  32.197  1.00 19.51 ?  233 THR A CB    1 
ATOM   1860 O  OG1   . THR A 1 234 ? -10.356 23.461  33.295  1.00 23.86 ?  233 THR A OG1   1 
ATOM   1861 C  CG2   . THR A 1 234 ? -11.143 25.669  32.746  1.00 19.59 ?  233 THR A CG2   1 
ATOM   1862 N  N     . TYR A 1 235 ? -10.383 22.650  29.412  1.00 13.11 ?  234 TYR A N     1 
ATOM   1863 C  CA    . TYR A 1 235 ? -9.778  21.528  28.699  1.00 8.69  ?  234 TYR A CA    1 
ATOM   1864 C  C     . TYR A 1 235 ? -8.270  21.520  28.909  1.00 8.96  ?  234 TYR A C     1 
ATOM   1865 O  O     . TYR A 1 235 ? -7.655  22.555  29.174  1.00 11.53 ?  234 TYR A O     1 
ATOM   1866 C  CB    . TYR A 1 235 ? -10.127 21.574  27.200  1.00 8.33  ?  234 TYR A CB    1 
ATOM   1867 C  CG    . TYR A 1 235 ? -11.557 21.130  26.946  1.00 9.62  ?  234 TYR A CG    1 
ATOM   1868 C  CD1   . TYR A 1 235 ? -12.640 22.013  27.090  1.00 11.57 ?  234 TYR A CD1   1 
ATOM   1869 C  CD2   . TYR A 1 235 ? -11.819 19.830  26.556  1.00 8.66  ?  234 TYR A CD2   1 
ATOM   1870 C  CE1   . TYR A 1 235 ? -13.951 21.553  26.901  1.00 11.99 ?  234 TYR A CE1   1 
ATOM   1871 C  CE2   . TYR A 1 235 ? -13.137 19.368  26.330  1.00 9.71  ?  234 TYR A CE2   1 
ATOM   1872 C  CZ    . TYR A 1 235 ? -14.176 20.266  26.498  1.00 13.17 ?  234 TYR A CZ    1 
ATOM   1873 O  OH    . TYR A 1 235 ? -15.451 19.803  26.309  1.00 12.04 ?  234 TYR A OH    1 
ATOM   1874 N  N     . ASP A 1 236 ? -7.697  20.303  28.873  1.00 7.97  ?  235 ASP A N     1 
ATOM   1875 C  CA    . ASP A 1 236 ? -6.263  20.068  29.084  1.00 6.98  ?  235 ASP A CA    1 
ATOM   1876 C  C     . ASP A 1 236 ? -5.712  19.285  27.872  1.00 6.91  ?  235 ASP A C     1 
ATOM   1877 O  O     . ASP A 1 236 ? -5.648  18.055  27.911  1.00 7.37  ?  235 ASP A O     1 
ATOM   1878 C  CB    . ASP A 1 236 ? -6.034  19.260  30.369  1.00 9.87  ?  235 ASP A CB    1 
ATOM   1879 C  CG    . ASP A 1 236 ? -4.589  19.282  30.811  1.00 13.83 ?  235 ASP A CG    1 
ATOM   1880 O  OD1   . ASP A 1 236 ? -3.699  19.509  29.961  1.00 10.94 ?  235 ASP A OD1   1 
ATOM   1881 O  OD2   . ASP A 1 236 ? -4.348  19.087  32.027  1.00 15.14 -1 235 ASP A OD2   1 
ATOM   1882 N  N     . ASP A 1 237 ? -5.358  20.010  26.811  1.00 7.72  ?  236 ASP A N     1 
ATOM   1883 C  CA    . ASP A 1 237 ? -4.869  19.360  25.581  1.00 6.21  ?  236 ASP A CA    1 
ATOM   1884 C  C     . ASP A 1 237 ? -3.556  18.641  25.809  1.00 5.16  ?  236 ASP A C     1 
ATOM   1885 O  O     . ASP A 1 237 ? -3.332  17.595  25.216  1.00 6.15  ?  236 ASP A O     1 
ATOM   1886 C  CB    . ASP A 1 237 ? -4.674  20.395  24.475  1.00 6.96  ?  236 ASP A CB    1 
ATOM   1887 C  CG    . ASP A 1 237 ? -5.972  20.973  23.952  1.00 8.61  ?  236 ASP A CG    1 
ATOM   1888 O  OD1   . ASP A 1 237 ? -7.044  20.764  24.585  1.00 6.29  ?  236 ASP A OD1   1 
ATOM   1889 O  OD2   . ASP A 1 237 ? -5.885  21.675  22.913  1.00 7.91  -1 236 ASP A OD2   1 
ATOM   1890 N  N     . ARG A 1 238 ? -2.677  19.192  26.654  1.00 6.87  ?  237 ARG A N     1 
ATOM   1891 C  CA    . ARG A 1 238 ? -1.420  18.514  26.934  1.00 4.97  ?  237 ARG A CA    1 
ATOM   1892 C  C     . ARG A 1 238 ? -1.672  17.143  27.539  1.00 5.87  ?  237 ARG A C     1 
ATOM   1893 O  O     . ARG A 1 238 ? -1.087  16.130  27.113  1.00 7.83  ?  237 ARG A O     1 
ATOM   1894 C  CB    . ARG A 1 238 ? -0.554  19.359  27.861  1.00 5.88  ?  237 ARG A CB    1 
ATOM   1895 C  CG    . ARG A 1 238 ? 0.882   18.812  27.991  1.00 8.71  ?  237 ARG A CG    1 
ATOM   1896 C  CD    . ARG A 1 238 ? 1.519   19.146  29.367  1.00 10.56 ?  237 ARG A CD    1 
ATOM   1897 N  NE    . ARG A 1 238 ? 0.653   18.614  30.414  1.00 9.13  ?  237 ARG A NE    1 
ATOM   1898 C  CZ    . ARG A 1 238 ? 0.519   17.334  30.730  1.00 9.61  ?  237 ARG A CZ    1 
ATOM   1899 N  NH1   . ARG A 1 238 ? 1.279   16.364  30.210  1.00 9.97  1  237 ARG A NH1   1 
ATOM   1900 N  NH2   . ARG A 1 238 ? -0.384  17.015  31.642  1.00 13.16 ?  237 ARG A NH2   1 
ATOM   1901 N  N     . ASP A 1 239 ? -2.587  17.068  28.519  1.00 7.78  ?  238 ASP A N     1 
ATOM   1902 C  CA    . ASP A 1 239 ? -2.920  15.786  29.121  1.00 7.65  ?  238 ASP A CA    1 
ATOM   1903 C  C     . ASP A 1 239 ? -3.641  14.867  28.131  1.00 7.92  ?  238 ASP A C     1 
ATOM   1904 O  O     . ASP A 1 239 ? -3.398  13.661  28.112  1.00 6.97  ?  238 ASP A O     1 
ATOM   1905 C  CB    . ASP A 1 239 ? -3.752  16.021  30.389  1.00 7.89  ?  238 ASP A CB    1 
ATOM   1906 C  CG    . ASP A 1 239 ? -4.096  14.732  31.090  1.00 12.07 ?  238 ASP A CG    1 
ATOM   1907 O  OD1   . ASP A 1 239 ? -3.169  14.006  31.528  1.00 14.71 ?  238 ASP A OD1   1 
ATOM   1908 O  OD2   . ASP A 1 239 ? -5.295  14.393  31.193  1.00 14.16 -1 238 ASP A OD2   1 
ATOM   1909 N  N     . ALA A 1 240 ? -4.558  15.403  27.335  1.00 8.06  ?  239 ALA A N     1 
ATOM   1910 C  CA    . ALA A 1 240 ? -5.224  14.548  26.340  1.00 8.42  ?  239 ALA A CA    1 
ATOM   1911 C  C     . ALA A 1 240 ? -4.199  13.921  25.378  1.00 7.66  ?  239 ALA A C     1 
ATOM   1912 O  O     . ALA A 1 240 ? -4.279  12.721  25.044  1.00 6.66  ?  239 ALA A O     1 
ATOM   1913 C  CB    . ALA A 1 240 ? -6.273  15.378  25.599  1.00 8.42  ?  239 ALA A CB    1 
ATOM   1914 N  N     . LEU A 1 241 ? -3.219  14.716  24.949  1.00 7.93  ?  240 LEU A N     1 
ATOM   1915 C  CA    . LEU A 1 241 ? -2.136  14.187  24.120  1.00 8.32  ?  240 LEU A CA    1 
ATOM   1916 C  C     . LEU A 1 241 ? -1.320  13.150  24.871  1.00 8.77  ?  240 LEU A C     1 
ATOM   1917 O  O     . LEU A 1 241 ? -0.967  12.113  24.321  1.00 7.90  ?  240 LEU A O     1 
ATOM   1918 C  CB    . LEU A 1 241 ? -1.227  15.312  23.663  1.00 6.41  ?  240 LEU A CB    1 
ATOM   1919 C  CG    . LEU A 1 241 ? -1.787  16.184  22.546  1.00 8.54  ?  240 LEU A CG    1 
ATOM   1920 C  CD1   . LEU A 1 241 ? -0.878  17.395  22.399  1.00 10.84 ?  240 LEU A CD1   1 
ATOM   1921 C  CD2   . LEU A 1 241 ? -1.963  15.394  21.223  1.00 7.94  ?  240 LEU A CD2   1 
ATOM   1922 N  N     . GLU A 1 242 ? -0.963  13.432  26.127  1.00 6.25  ?  241 GLU A N     1 
ATOM   1923 C  CA    . GLU A 1 242 ? -0.176  12.457  26.869  1.00 7.82  ?  241 GLU A CA    1 
ATOM   1924 C  C     . GLU A 1 242 ? -0.898  11.123  26.953  1.00 8.97  ?  241 GLU A C     1 
ATOM   1925 O  O     . GLU A 1 242 ? -0.309  10.055  26.709  1.00 9.88  ?  241 GLU A O     1 
ATOM   1926 C  CB    . GLU A 1 242 ? 0.160   13.017  28.260  1.00 9.06  ?  241 GLU A CB    1 
ATOM   1927 C  CG    . GLU A 1 242 ? 1.075   12.081  29.049  1.00 10.83 ?  241 GLU A CG    1 
ATOM   1928 C  CD    . GLU A 1 242 ? 1.117   12.459  30.530  1.00 16.50 ?  241 GLU A CD    1 
ATOM   1929 O  OE1   . GLU A 1 242 ? 1.039   13.663  30.844  1.00 16.72 ?  241 GLU A OE1   1 
ATOM   1930 O  OE2   . GLU A 1 242 ? 1.222   11.529  31.347  1.00 20.23 -1 241 GLU A OE2   1 
ATOM   1931 N  N     . GLN A 1 243 ? -2.188  11.144  27.317  1.00 9.74  ?  242 GLN A N     1 
ATOM   1932 C  CA    . GLN A 1 243 ? -2.901  9.878   27.439  1.00 9.50  ?  242 GLN A CA    1 
ATOM   1933 C  C     . GLN A 1 243 ? -3.005  9.160   26.098  1.00 10.41 ?  242 GLN A C     1 
ATOM   1934 O  O     . GLN A 1 243 ? -2.846  7.950   26.008  1.00 10.15 ?  242 GLN A O     1 
ATOM   1935 C  CB    . GLN A 1 243 ? -4.286  10.125  28.000  1.00 10.43 ?  242 GLN A CB    1 
ATOM   1936 C  CG    . GLN A 1 243 ? -4.214  10.848  29.345  1.00 10.88 ?  242 GLN A CG    1 
ATOM   1937 C  CD    . GLN A 1 243 ? -3.238  10.205  30.364  1.00 16.31 ?  242 GLN A CD    1 
ATOM   1938 O  OE1   . GLN A 1 243 ? -3.116  8.975   30.461  1.00 19.59 ?  242 GLN A OE1   1 
ATOM   1939 N  NE2   . GLN A 1 243 ? -2.552  11.050  31.129  1.00 18.48 ?  242 GLN A NE2   1 
ATOM   1940 N  N     . PHE A 1 244 ? -3.273  9.903   25.040  1.00 7.81  ?  243 PHE A N     1 
ATOM   1941 C  CA    . PHE A 1 244 ? -3.432  9.305   23.715  1.00 6.74  ?  243 PHE A CA    1 
ATOM   1942 C  C     . PHE A 1 244 ? -2.114  8.727   23.201  1.00 9.02  ?  243 PHE A C     1 
ATOM   1943 O  O     . PHE A 1 244 ? -2.090  7.617   22.672  1.00 6.68  ?  243 PHE A O     1 
ATOM   1944 C  CB    . PHE A 1 244 ? -3.957  10.414  22.773  1.00 5.85  ?  243 PHE A CB    1 
ATOM   1945 C  CG    . PHE A 1 244 ? -4.106  10.014  21.315  1.00 7.60  ?  243 PHE A CG    1 
ATOM   1946 C  CD1   . PHE A 1 244 ? -4.500  8.744   20.950  1.00 6.81  ?  243 PHE A CD1   1 
ATOM   1947 C  CD2   . PHE A 1 244 ? -3.904  10.980  20.309  1.00 9.71  ?  243 PHE A CD2   1 
ATOM   1948 C  CE1   . PHE A 1 244 ? -4.622  8.370   19.635  1.00 7.95  ?  243 PHE A CE1   1 
ATOM   1949 C  CE2   . PHE A 1 244 ? -4.029  10.638  18.921  1.00 8.89  ?  243 PHE A CE2   1 
ATOM   1950 C  CZ    . PHE A 1 244 ? -4.358  9.317   18.601  1.00 7.40  ?  243 PHE A CZ    1 
ATOM   1951 N  N     . VAL A 1 245 ? -1.013  9.473   23.340  1.00 7.18  ?  244 VAL A N     1 
ATOM   1952 C  CA    . VAL A 1 245 ? 0.289   8.967   22.894  1.00 6.20  ?  244 VAL A CA    1 
ATOM   1953 C  C     . VAL A 1 245 ? 0.675   7.727   23.687  1.00 8.41  ?  244 VAL A C     1 
ATOM   1954 O  O     . VAL A 1 245 ? 1.183   6.752   23.130  1.00 8.50  ?  244 VAL A O     1 
ATOM   1955 C  CB    . VAL A 1 245 ? 1.348   10.087  22.963  1.00 8.01  ?  244 VAL A CB    1 
ATOM   1956 C  CG1   . VAL A 1 245 ? 2.786   9.540   22.740  1.00 8.47  ?  244 VAL A CG1   1 
ATOM   1957 C  CG2   . VAL A 1 245 ? 1.037   11.132  21.876  1.00 6.61  ?  244 VAL A CG2   1 
ATOM   1958 N  N     . GLN A 1 246 ? 0.458   7.749   25.006  1.00 7.79  ?  245 GLN A N     1 
ATOM   1959 C  CA    . GLN A 1 246 ? 0.772   6.570   25.793  1.00 8.83  ?  245 GLN A CA    1 
ATOM   1960 C  C     . GLN A 1 246 ? -0.065  5.372   25.354  1.00 8.77  ?  245 GLN A C     1 
ATOM   1961 O  O     . GLN A 1 246 ? 0.456   4.253   25.246  1.00 9.05  ?  245 GLN A O     1 
ATOM   1962 C  CB    . GLN A 1 246 ? 0.525   6.861   27.259  1.00 9.92  ?  245 GLN A CB    1 
ATOM   1963 C  CG    . GLN A 1 246 ? 0.841   5.638   28.127  1.00 11.08 ?  245 GLN A CG    1 
ATOM   1964 C  CD    . GLN A 1 246 ? 2.316   5.265   28.125  1.00 15.90 ?  245 GLN A CD    1 
ATOM   1965 O  OE1   . GLN A 1 246 ? 3.108   5.896   28.811  1.00 19.11 ?  245 GLN A OE1   1 
ATOM   1966 N  NE2   . GLN A 1 246 ? 2.691   4.236   27.336  1.00 14.33 ?  245 GLN A NE2   1 
ATOM   1967 N  N     . THR A 1 247 ? -1.337  5.590   25.031  1.00 7.79  ?  246 THR A N     1 
ATOM   1968 C  CA    . THR A 1 247 ? -2.179  4.481   24.586  1.00 8.87  ?  246 THR A CA    1 
ATOM   1969 C  C     . THR A 1 247 ? -1.706  3.925   23.235  1.00 10.18 ?  246 THR A C     1 
ATOM   1970 O  O     . THR A 1 247 ? -1.676  2.696   23.015  1.00 9.51  ?  246 THR A O     1 
ATOM   1971 C  CB    . THR A 1 247 ? -3.630  4.946   24.554  1.00 9.11  ?  246 THR A CB    1 
ATOM   1972 O  OG1   . THR A 1 247 ? -3.994  5.266   25.910  1.00 10.15 ?  246 THR A OG1   1 
ATOM   1973 C  CG2   . THR A 1 247 ? -4.527  3.861   24.015  1.00 9.30  ?  246 THR A CG2   1 
ATOM   1974 N  N     . MET A 1 248 ? -1.317  4.815   22.318  1.00 8.94  ?  247 MET A N     1 
ATOM   1975 C  CA    . MET A 1 248 ? -0.729  4.328   21.070  1.00 8.91  ?  247 MET A CA    1 
ATOM   1976 C  C     . MET A 1 248 ? 0.500   3.480   21.350  1.00 8.09  ?  247 MET A C     1 
ATOM   1977 O  O     . MET A 1 248 ? 0.644   2.373   20.813  1.00 8.72  ?  247 MET A O     1 
ATOM   1978 C  CB    . MET A 1 248 ? -0.389  5.517   20.146  1.00 9.10  ?  247 MET A CB    1 
ATOM   1979 C  CG    . MET A 1 248 ? -1.624  6.020   19.453  1.00 8.66  ?  247 MET A CG    1 
ATOM   1980 S  SD    . MET A 1 248 ? -1.188  7.204   18.142  1.00 9.40  ?  247 MET A SD    1 
ATOM   1981 C  CE    . MET A 1 248 ? -0.646  8.578   19.112  1.00 9.96  ?  247 MET A CE    1 
ATOM   1982 N  N     . LEU A 1 249 ? 1.399   3.989   22.200  1.00 8.51  ?  248 LEU A N     1 
ATOM   1983 C  CA    . LEU A 1 249 ? 2.602   3.221   22.543  1.00 10.45 ?  248 LEU A CA    1 
ATOM   1984 C  C     . LEU A 1 249 ? 2.239   1.867   23.145  1.00 13.89 ?  248 LEU A C     1 
ATOM   1985 O  O     . LEU A 1 249 ? 2.829   0.839   22.776  1.00 14.16 ?  248 LEU A O     1 
ATOM   1986 C  CB    . LEU A 1 249 ? 3.455   4.044   23.495  1.00 8.15  ?  248 LEU A CB    1 
ATOM   1987 C  CG    . LEU A 1 249 ? 4.162   5.149   22.734  1.00 8.44  ?  248 LEU A CG    1 
ATOM   1988 C  CD1   . LEU A 1 249 ? 4.686   6.134   23.722  1.00 9.67  ?  248 LEU A CD1   1 
ATOM   1989 C  CD2   . LEU A 1 249 ? 5.327   4.534   21.900  1.00 10.44 ?  248 LEU A CD2   1 
ATOM   1990 N  N     . ASP A 1 250 ? 1.221   1.835   24.015  1.00 11.11 ?  249 ASP A N     1 
ATOM   1991 C  CA    . ASP A 1 250 ? 0.829   0.550   24.609  1.00 12.35 ?  249 ASP A CA    1 
ATOM   1992 C  C     . ASP A 1 250 ? 0.379   -0.454  23.567  1.00 13.66 ?  249 ASP A C     1 
ATOM   1993 O  O     . ASP A 1 250 ? 0.365   -1.657  23.849  1.00 18.06 ?  249 ASP A O     1 
ATOM   1994 C  CB    . ASP A 1 250 ? -0.299  0.711   25.635  1.00 16.56 ?  249 ASP A CB    1 
ATOM   1995 C  CG    . ASP A 1 250 ? 0.090   1.540   26.825  1.00 19.98 ?  249 ASP A CG    1 
ATOM   1996 O  OD1   . ASP A 1 250 ? 1.294   1.714   27.098  1.00 19.93 ?  249 ASP A OD1   1 
ATOM   1997 O  OD2   . ASP A 1 250 ? -0.848  2.037   27.477  1.00 23.03 -1 249 ASP A OD2   1 
ATOM   1998 N  N     . ASN A 1 251 ? -0.060  -0.008  22.387  1.00 10.24 ?  250 ASN A N     1 
ATOM   1999 C  CA    . ASN A 1 251 ? -0.599  -0.938  21.419  1.00 10.03 ?  250 ASN A CA    1 
ATOM   2000 C  C     . ASN A 1 251 ? 0.422   -1.409  20.380  1.00 10.94 ?  250 ASN A C     1 
ATOM   2001 O  O     . ASN A 1 251 ? 0.057   -2.175  19.488  1.00 14.15 ?  250 ASN A O     1 
ATOM   2002 C  CB    . ASN A 1 251 ? -1.818  -0.326  20.734  1.00 12.33 ?  250 ASN A CB    1 
ATOM   2003 C  CG    . ASN A 1 251 ? -3.063  -0.448  21.577  1.00 13.89 ?  250 ASN A CG    1 
ATOM   2004 O  OD1   . ASN A 1 251 ? -3.763  -1.486  21.543  1.00 15.04 ?  250 ASN A OD1   1 
ATOM   2005 N  ND2   . ASN A 1 251 ? -3.337  0.576   22.375  1.00 12.52 ?  250 ASN A ND2   1 
ATOM   2006 N  N     . PHE A 1 252 ? 1.671   -0.944  20.444  1.00 11.06 ?  251 PHE A N     1 
ATOM   2007 C  CA    . PHE A 1 252 ? 2.699   -1.545  19.596  1.00 12.38 ?  251 PHE A CA    1 
ATOM   2008 C  C     . PHE A 1 252 ? 2.930   -2.978  20.028  1.00 14.67 ?  251 PHE A C     1 
ATOM   2009 O  O     . PHE A 1 252 ? 2.840   -3.321  21.217  1.00 16.74 ?  251 PHE A O     1 
ATOM   2010 C  CB    . PHE A 1 252 ? 4.011   -0.783  19.662  1.00 12.62 ?  251 PHE A CB    1 
ATOM   2011 C  CG    . PHE A 1 252 ? 4.045   0.454   18.807  1.00 11.29 ?  251 PHE A CG    1 
ATOM   2012 C  CD1   . PHE A 1 252 ? 3.378   1.592   19.212  1.00 10.02 ?  251 PHE A CD1   1 
ATOM   2013 C  CD2   . PHE A 1 252 ? 4.803   0.503   17.635  1.00 11.86 ?  251 PHE A CD2   1 
ATOM   2014 C  CE1   . PHE A 1 252 ? 3.443   2.773   18.427  1.00 9.22  ?  251 PHE A CE1   1 
ATOM   2015 C  CE2   . PHE A 1 252 ? 4.864   1.668   16.864  1.00 11.10 ?  251 PHE A CE2   1 
ATOM   2016 C  CZ    . PHE A 1 252 ? 4.190   2.796   17.266  1.00 10.77 ?  251 PHE A CZ    1 
ATOM   2017 N  N     . HIS A 1 253 ? 3.221   -3.817  19.049  1.00 10.60 ?  252 HIS A N     1 
ATOM   2018 C  CA    . HIS A 1 253 ? 3.412   -5.241  19.291  1.00 13.41 ?  252 HIS A CA    1 
ATOM   2019 C  C     . HIS A 1 253 ? 4.682   -5.644  18.570  1.00 12.36 ?  252 HIS A C     1 
ATOM   2020 O  O     . HIS A 1 253 ? 4.823   -5.390  17.376  1.00 10.99 ?  252 HIS A O     1 
ATOM   2021 C  CB    . HIS A 1 253 ? 2.201   -6.034  18.788  1.00 15.25 ?  252 HIS A CB    1 
ATOM   2022 C  CG    . HIS A 1 253 ? 2.394   -7.520  18.779  1.00 24.24 ?  252 HIS A CG    1 
ATOM   2023 N  ND1   . HIS A 1 253 ? 2.178   -8.308  19.893  1.00 26.52 ?  252 HIS A ND1   1 
ATOM   2024 C  CD2   . HIS A 1 253 ? 2.757   -8.367  17.784  1.00 25.33 ?  252 HIS A CD2   1 
ATOM   2025 C  CE1   . HIS A 1 253 ? 2.421   -9.573  19.589  1.00 25.11 ?  252 HIS A CE1   1 
ATOM   2026 N  NE2   . HIS A 1 253 ? 2.773   -9.636  18.315  1.00 26.83 ?  252 HIS A NE2   1 
ATOM   2027 N  N     . ASP A 1 254 ? 5.583   -6.330  19.290  1.00 12.18 ?  253 ASP A N     1 
ATOM   2028 C  CA    . ASP A 1 254 ? 6.795   -6.809  18.658  1.00 14.11 ?  253 ASP A CA    1 
ATOM   2029 C  C     . ASP A 1 254 ? 6.432   -7.951  17.708  1.00 13.52 ?  253 ASP A C     1 
ATOM   2030 O  O     . ASP A 1 254 ? 5.832   -8.946  18.133  1.00 18.51 ?  253 ASP A O     1 
ATOM   2031 C  CB    . ASP A 1 254 ? 7.775   -7.267  19.733  1.00 17.49 ?  253 ASP A CB    1 
ATOM   2032 C  CG    . ASP A 1 254 ? 8.530   -6.116  20.385  1.00 23.57 ?  253 ASP A CG    1 
ATOM   2033 O  OD1   . ASP A 1 254 ? 8.502   -4.962  19.886  1.00 22.59 ?  253 ASP A OD1   1 
ATOM   2034 O  OD2   . ASP A 1 254 ? 9.198   -6.381  21.407  1.00 26.59 -1 253 ASP A OD2   1 
ATOM   2035 N  N     . THR A 1 255 ? 6.817   -7.825  16.439  1.00 10.21 ?  254 THR A N     1 
ATOM   2036 C  CA    . THR A 1 255 ? 6.324   -8.643  15.332  1.00 10.55 ?  254 THR A CA    1 
ATOM   2037 C  C     . THR A 1 255 ? 7.519   -9.216  14.572  1.00 10.99 ?  254 THR A C     1 
ATOM   2038 O  O     . THR A 1 255 ? 8.337   -8.476  14.006  1.00 10.86 ?  254 THR A O     1 
ATOM   2039 C  CB    . THR A 1 255 ? 5.441   -7.821  14.383  1.00 14.21 ?  254 THR A CB    1 
ATOM   2040 O  OG1   . THR A 1 255 ? 4.412   -7.207  15.147  1.00 12.71 ?  254 THR A OG1   1 
ATOM   2041 C  CG2   . THR A 1 255 ? 4.834   -8.683  13.284  1.00 14.81 ?  254 THR A CG2   1 
ATOM   2042 N  N     . TRP A 1 256 ? 7.636   -10.544 14.582  1.00 9.05  ?  255 TRP A N     1 
ATOM   2043 C  CA    . TRP A 1 256 ? 8.776   -11.188 13.967  1.00 9.29  ?  255 TRP A CA    1 
ATOM   2044 C  C     . TRP A 1 256 ? 8.662   -11.132 12.464  1.00 10.96 ?  255 TRP A C     1 
ATOM   2045 O  O     . TRP A 1 256 ? 7.596   -11.368 11.893  1.00 13.29 ?  255 TRP A O     1 
ATOM   2046 C  CB    . TRP A 1 256 ? 8.834   -12.652 14.472  1.00 9.65  ?  255 TRP A CB    1 
ATOM   2047 C  CG    . TRP A 1 256 ? 9.965   -13.469 13.946  1.00 9.02  ?  255 TRP A CG    1 
ATOM   2048 C  CD1   . TRP A 1 256 ? 9.945   -14.334 12.872  1.00 12.93 ?  255 TRP A CD1   1 
ATOM   2049 C  CD2   . TRP A 1 256 ? 11.317  -13.423 14.404  1.00 10.24 ?  255 TRP A CD2   1 
ATOM   2050 N  NE1   . TRP A 1 256 ? 11.203  -14.860 12.675  1.00 13.10 ?  255 TRP A NE1   1 
ATOM   2051 C  CE2   . TRP A 1 256 ? 12.060  -14.334 13.613  1.00 11.69 ?  255 TRP A CE2   1 
ATOM   2052 C  CE3   . TRP A 1 256 ? 11.955  -12.768 15.463  1.00 12.79 ?  255 TRP A CE3   1 
ATOM   2053 C  CZ2   . TRP A 1 256 ? 13.417  -14.592 13.840  1.00 13.14 ?  255 TRP A CZ2   1 
ATOM   2054 C  CZ3   . TRP A 1 256 ? 13.301  -13.010 15.676  1.00 13.72 ?  255 TRP A CZ3   1 
ATOM   2055 C  CH2   . TRP A 1 256 ? 14.019  -13.918 14.859  1.00 13.77 ?  255 TRP A CH2   1 
ATOM   2056 N  N     . ASP A 1 257 ? 9.789   -10.853 11.814  1.00 10.80 ?  256 ASP A N     1 
ATOM   2057 C  CA    . ASP A 1 257 ? 9.889   -10.856 10.371  1.00 11.78 ?  256 ASP A CA    1 
ATOM   2058 C  C     . ASP A 1 257 ? 10.851  -11.976 10.005  1.00 13.96 ?  256 ASP A C     1 
ATOM   2059 O  O     . ASP A 1 257 ? 12.042  -11.913 10.352  1.00 13.01 ?  256 ASP A O     1 
ATOM   2060 C  CB    . ASP A 1 257 ? 10.383  -9.491  9.876   1.00 15.16 ?  256 ASP A CB    1 
ATOM   2061 C  CG    . ASP A 1 257 ? 10.408  -9.406  8.389   1.00 18.99 ?  256 ASP A CG    1 
ATOM   2062 O  OD1   . ASP A 1 257 ? 11.430  -9.750  7.763   1.00 22.76 ?  256 ASP A OD1   1 
ATOM   2063 O  OD2   . ASP A 1 257 ? 9.352   -9.060  7.823   1.00 24.08 -1 256 ASP A OD2   1 
ATOM   2064 N  N     . SER A 1 258 ? 10.308  -13.032 9.375   1.00 11.20 ?  257 SER A N     1 
ATOM   2065 C  CA    . SER A 1 258 ? 11.139  -14.175 9.015   1.00 11.39 ?  257 SER A CA    1 
ATOM   2066 C  C     . SER A 1 258 ? 12.188  -13.826 7.958   1.00 14.87 ?  257 SER A C     1 
ATOM   2067 O  O     . SER A 1 258 ? 13.283  -14.401 7.980   1.00 16.61 ?  257 SER A O     1 
ATOM   2068 C  CB    . SER A 1 258 ? 10.232  -15.332 8.550   1.00 12.46 ?  257 SER A CB    1 
ATOM   2069 O  OG    . SER A 1 258 ? 9.486   -15.841 9.666   1.00 11.85 ?  257 SER A OG    1 
ATOM   2070 N  N     . LYS A 1 259 ? 11.879  -12.930 7.019   1.00 17.33 ?  258 LYS A N     1 
ATOM   2071 C  CA    . LYS A 1 259 ? 12.891  -12.558 6.031   1.00 22.77 ?  258 LYS A CA    1 
ATOM   2072 C  C     . LYS A 1 259 ? 14.125  -11.972 6.712   1.00 20.42 ?  258 LYS A C     1 
ATOM   2073 O  O     . LYS A 1 259 ? 15.253  -12.372 6.416   1.00 22.00 ?  258 LYS A O     1 
ATOM   2074 C  CB    . LYS A 1 259 ? 12.298  -11.575 5.018   1.00 30.60 ?  258 LYS A CB    1 
ATOM   2075 C  CG    . LYS A 1 259 ? 13.345  -10.925 4.139   1.00 39.91 ?  258 LYS A CG    1 
ATOM   2076 C  CD    . LYS A 1 259 ? 14.152  -11.967 3.353   1.00 47.88 ?  258 LYS A CD    1 
ATOM   2077 C  CE    . LYS A 1 259 ? 15.496  -11.388 2.901   1.00 54.90 ?  258 LYS A CE    1 
ATOM   2078 N  NZ    . LYS A 1 259 ? 16.162  -12.267 1.912   1.00 57.93 1  258 LYS A NZ    1 
ATOM   2079 N  N     . ASP A 1 260 ? 13.934  -11.011 7.628   1.00 18.98 ?  259 ASP A N     1 
ATOM   2080 C  CA    . ASP A 1 260 ? 15.030  -10.319 8.301   1.00 17.22 ?  259 ASP A CA    1 
ATOM   2081 C  C     . ASP A 1 260 ? 15.512  -11.020 9.561   1.00 16.51 ?  259 ASP A C     1 
ATOM   2082 O  O     . ASP A 1 260 ? 16.500  -10.582 10.176  1.00 17.08 ?  259 ASP A O     1 
ATOM   2083 C  CB    . ASP A 1 260 ? 14.608  -8.880  8.684   1.00 18.27 ?  259 ASP A CB    1 
ATOM   2084 C  CG    . ASP A 1 260 ? 14.304  -8.014  7.470   1.00 21.69 ?  259 ASP A CG    1 
ATOM   2085 O  OD1   . ASP A 1 260 ? 14.541  -8.454  6.323   1.00 21.66 ?  259 ASP A OD1   1 
ATOM   2086 O  OD2   . ASP A 1 260 ? 13.805  -6.884  7.665   1.00 22.58 -1 259 ASP A OD2   1 
ATOM   2087 N  N     . GLN A 1 261 ? 14.835  -12.088 9.984   1.00 15.24 ?  260 GLN A N     1 
ATOM   2088 C  CA    . GLN A 1 261 ? 15.180  -12.787 11.210  1.00 13.42 ?  260 GLN A CA    1 
ATOM   2089 C  C     . GLN A 1 261 ? 15.331  -11.826 12.370  1.00 14.36 ?  260 GLN A C     1 
ATOM   2090 O  O     . GLN A 1 261 ? 16.310  -11.875 13.122  1.00 14.99 ?  260 GLN A O     1 
ATOM   2091 C  CB    . GLN A 1 261 ? 16.446  -13.641 11.029  1.00 13.92 ?  260 GLN A CB    1 
ATOM   2092 C  CG    . GLN A 1 261 ? 16.208  -14.776 10.058  1.00 14.68 ?  260 GLN A CG    1 
ATOM   2093 C  CD    . GLN A 1 261 ? 15.341  -15.888 10.691  1.00 13.40 ?  260 GLN A CD    1 
ATOM   2094 O  OE1   . GLN A 1 261 ? 15.748  -16.503 11.670  1.00 18.44 ?  260 GLN A OE1   1 
ATOM   2095 N  NE2   . GLN A 1 261 ? 14.141  -16.087 10.162  1.00 13.36 ?  260 GLN A NE2   1 
ATOM   2096 N  N     . ARG A 1 262 ? 14.314  -10.965 12.546  1.00 11.78 ?  261 ARG A N     1 
ATOM   2097 C  CA    . ARG A 1 262 ? 14.304  -10.116 13.741  1.00 12.90 ?  261 ARG A CA    1 
ATOM   2098 C  C     . ARG A 1 262 ? 12.888  -9.613  13.918  1.00 11.83 ?  261 ARG A C     1 
ATOM   2099 O  O     . ARG A 1 262 ? 12.078  -9.723  12.994  1.00 11.80 ?  261 ARG A O     1 
ATOM   2100 C  CB    . ARG A 1 262 ? 15.282  -8.918  13.638  1.00 16.14 ?  261 ARG A CB    1 
ATOM   2101 C  CG    . ARG A 1 262 ? 15.049  -8.031  12.478  1.00 14.60 ?  261 ARG A CG    1 
ATOM   2102 C  CD    . ARG A 1 262 ? 15.721  -6.624  12.744  1.00 15.00 ?  261 ARG A CD    1 
ATOM   2103 N  NE    . ARG A 1 262 ? 14.976  -5.912  13.775  1.00 17.37 ?  261 ARG A NE    1 
ATOM   2104 C  CZ    . ARG A 1 262 ? 15.219  -4.655  14.161  1.00 16.86 ?  261 ARG A CZ    1 
ATOM   2105 N  NH1   . ARG A 1 262 ? 16.239  -3.984  13.628  1.00 19.45 1  261 ARG A NH1   1 
ATOM   2106 N  NH2   . ARG A 1 262 ? 14.464  -4.087  15.091  1.00 14.79 ?  261 ARG A NH2   1 
ATOM   2107 N  N     . SER A 1 263 ? 12.598  -9.047  15.106  1.00 14.13 ?  262 SER A N     1 
ATOM   2108 C  CA    . SER A 1 263 ? 11.301  -8.412  15.368  1.00 12.24 ?  262 SER A CA    1 
ATOM   2109 C  C     . SER A 1 263 ? 11.374  -6.920  15.128  1.00 13.15 ?  262 SER A C     1 
ATOM   2110 O  O     . SER A 1 263 ? 12.417  -6.302  15.327  1.00 14.01 ?  262 SER A O     1 
ATOM   2111 C  CB    . SER A 1 263 ? 10.813  -8.567  16.797  1.00 16.06 ?  262 SER A CB    1 
ATOM   2112 O  OG    . SER A 1 263 ? 10.837  -9.923  17.185  1.00 24.92 ?  262 SER A OG    1 
ATOM   2113 N  N     . TYR A 1 264 ? 10.231  -6.363  14.750  1.00 9.59  ?  263 TYR A N     1 
ATOM   2114 C  CA    . TYR A 1 264 ? 10.041  -4.919  14.669  1.00 10.20 ?  263 TYR A CA    1 
ATOM   2115 C  C     . TYR A 1 264 ? 8.792   -4.571  15.468  1.00 9.80  ?  263 TYR A C     1 
ATOM   2116 O  O     . TYR A 1 264 ? 7.829   -5.330  15.460  1.00 10.74 ?  263 TYR A O     1 
ATOM   2117 C  CB    . TYR A 1 264 ? 9.844   -4.460  13.216  1.00 9.57  ?  263 TYR A CB    1 
ATOM   2118 C  CG    . TYR A 1 264 ? 11.003  -4.721  12.284  1.00 11.82 ?  263 TYR A CG    1 
ATOM   2119 C  CD1   . TYR A 1 264 ? 12.134  -3.910  12.294  1.00 13.04 ?  263 TYR A CD1   1 
ATOM   2120 C  CD2   . TYR A 1 264 ? 10.957  -5.764  11.349  1.00 10.33 ?  263 TYR A CD2   1 
ATOM   2121 C  CE1   . TYR A 1 264 ? 13.192  -4.154  11.435  1.00 14.04 ?  263 TYR A CE1   1 
ATOM   2122 C  CE2   . TYR A 1 264 ? 12.011  -5.997  10.467  1.00 11.77 ?  263 TYR A CE2   1 
ATOM   2123 C  CZ    . TYR A 1 264 ? 13.138  -5.174  10.521  1.00 13.33 ?  263 TYR A CZ    1 
ATOM   2124 O  OH    . TYR A 1 264 ? 14.184  -5.402  9.634   1.00 15.58 ?  263 TYR A OH    1 
ATOM   2125 N  N     . PRO A 1 265 ? 8.757   -3.411  16.131  1.00 8.31  ?  264 PRO A N     1 
ATOM   2126 C  CA    . PRO A 1 265 ? 7.557   -3.012  16.880  1.00 9.92  ?  264 PRO A CA    1 
ATOM   2127 C  C     . PRO A 1 265 ? 6.559   -2.411  15.912  1.00 13.76 ?  264 PRO A C     1 
ATOM   2128 O  O     . PRO A 1 265 ? 6.889   -1.444  15.234  1.00 18.18 ?  264 PRO A O     1 
ATOM   2129 C  CB    . PRO A 1 265 ? 8.080   -1.950  17.850  1.00 14.04 ?  264 PRO A CB    1 
ATOM   2130 C  CG    . PRO A 1 265 ? 9.274   -1.385  17.185  1.00 15.77 ?  264 PRO A CG    1 
ATOM   2131 C  CD    . PRO A 1 265 ? 9.850   -2.427  16.226  1.00 12.77 ?  264 PRO A CD    1 
ATOM   2132 N  N     . ARG A 1 266 ? 5.343   -2.952  15.863  1.00 8.54  ?  265 ARG A N     1 
ATOM   2133 C  CA    . ARG A 1 266 ? 4.378   -2.513  14.865  1.00 9.96  ?  265 ARG A CA    1 
ATOM   2134 C  C     . ARG A 1 266 ? 3.088   -2.084  15.548  1.00 10.60 ?  265 ARG A C     1 
ATOM   2135 O  O     . ARG A 1 266 ? 2.589   -2.721  16.494  1.00 10.35 ?  265 ARG A O     1 
ATOM   2136 C  CB    . ARG A 1 266 ? 4.047   -3.583  13.810  1.00 9.81  ?  265 ARG A CB    1 
ATOM   2137 C  CG    . ARG A 1 266 ? 5.194   -4.047  12.864  1.00 12.49 ?  265 ARG A CG    1 
ATOM   2138 C  CD    . ARG A 1 266 ? 4.643   -4.722  11.591  1.00 14.82 ?  265 ARG A CD    1 
ATOM   2139 N  NE    . ARG A 1 266 ? 3.802   -3.785  10.854  1.00 13.05 ?  265 ARG A NE    1 
ATOM   2140 C  CZ    . ARG A 1 266 ? 4.238   -2.958  9.911   1.00 10.65 ?  265 ARG A CZ    1 
ATOM   2141 N  NH1   . ARG A 1 266 ? 5.526   -2.996  9.525   1.00 8.85  1  265 ARG A NH1   1 
ATOM   2142 N  NH2   . ARG A 1 266 ? 3.384   -2.094  9.356   1.00 10.24 ?  265 ARG A NH2   1 
ATOM   2143 N  N     . LEU A 1 267 ? 2.537   -0.987  15.066  1.00 7.93  ?  266 LEU A N     1 
ATOM   2144 C  CA    . LEU A 1 267 ? 1.221   -0.544  15.480  1.00 6.53  ?  266 LEU A CA    1 
ATOM   2145 C  C     . LEU A 1 267 ? 0.254   -0.828  14.344  1.00 9.87  ?  266 LEU A C     1 
ATOM   2146 O  O     . LEU A 1 267 ? 0.420   -0.290  13.244  1.00 10.66 ?  266 LEU A O     1 
ATOM   2147 C  CB    . LEU A 1 267 ? 1.242   0.950   15.790  1.00 6.05  ?  266 LEU A CB    1 
ATOM   2148 C  CG    . LEU A 1 267 ? -0.063  1.556   16.223  1.00 6.79  ?  266 LEU A CG    1 
ATOM   2149 C  CD1   . LEU A 1 267 ? -0.427  1.068   17.616  1.00 9.68  ?  266 LEU A CD1   1 
ATOM   2150 C  CD2   . LEU A 1 267 ? 0.121   3.082   16.280  1.00 8.81  ?  266 LEU A CD2   1 
ATOM   2151 N  N     . THR A 1 268 ? -0.750  -1.688  14.595  1.00 8.48  ?  267 THR A N     1 
ATOM   2152 C  CA    . THR A 1 268 ? -1.801  -1.968  13.623  1.00 8.30  ?  267 THR A CA    1 
ATOM   2153 C  C     . THR A 1 268 ? -3.029  -1.137  13.982  1.00 9.97  ?  267 THR A C     1 
ATOM   2154 O  O     . THR A 1 268 ? -3.450  -1.143  15.147  1.00 13.35 ?  267 THR A O     1 
ATOM   2155 C  CB    . THR A 1 268 ? -2.163  -3.457  13.669  1.00 13.29 ?  267 THR A CB    1 
ATOM   2156 O  OG1   . THR A 1 268 ? -0.989  -4.229  13.438  1.00 15.65 ?  267 THR A OG1   1 
ATOM   2157 C  CG2   . THR A 1 268 ? -3.223  -3.779  12.622  1.00 15.59 ?  267 THR A CG2   1 
ATOM   2158 N  N     . VAL A 1 269 ? -3.557  -0.359  13.025  1.00 9.41  ?  268 VAL A N     1 
ATOM   2159 C  CA    . VAL A 1 269 ? -4.739  0.464   13.290  1.00 11.10 ?  268 VAL A CA    1 
ATOM   2160 C  C     . VAL A 1 269 ? -5.754  0.157   12.193  1.00 9.95  ?  268 VAL A C     1 
ATOM   2161 O  O     . VAL A 1 269 ? -5.585  0.591   11.050  1.00 12.42 ?  268 VAL A O     1 
ATOM   2162 C  CB    . VAL A 1 269 ? -4.413  1.953   13.354  1.00 14.24 ?  268 VAL A CB    1 
ATOM   2163 C  CG1   . VAL A 1 269 ? -5.726  2.754   13.544  1.00 17.62 ?  268 VAL A CG1   1 
ATOM   2164 C  CG2   . VAL A 1 269 ? -3.443  2.252   14.516  1.00 15.16 ?  268 VAL A CG2   1 
ATOM   2165 N  N     . GLU A 1 270 ? -6.786  -0.622  12.534  1.00 11.72 ?  269 GLU A N     1 
ATOM   2166 C  CA    . GLU A 1 270 ? -7.809  -0.984  11.556  1.00 15.17 ?  269 GLU A CA    1 
ATOM   2167 C  C     . GLU A 1 270 ? -8.708  0.197   11.241  1.00 12.10 ?  269 GLU A C     1 
ATOM   2168 O  O     . GLU A 1 270 ? -9.168  0.891   12.152  1.00 12.23 ?  269 GLU A O     1 
ATOM   2169 C  CB    . GLU A 1 270 ? -8.677  -2.120  12.082  1.00 22.46 ?  269 GLU A CB    1 
ATOM   2170 C  CG    . GLU A 1 270 ? -8.062  -3.499  11.959  1.00 30.19 ?  269 GLU A CG    1 
ATOM   2171 C  CD    . GLU A 1 270 ? -9.040  -4.581  12.363  1.00 39.26 ?  269 GLU A CD    1 
ATOM   2172 O  OE1   . GLU A 1 270 ? -8.651  -5.770  12.312  1.00 44.36 ?  269 GLU A OE1   1 
ATOM   2173 O  OE2   . GLU A 1 270 ? -10.201 -4.237  12.723  1.00 37.69 -1 269 GLU A OE2   1 
ATOM   2174 N  N     . LEU A 1 271 ? -8.997  0.384   9.968   1.00 10.26 ?  270 LEU A N     1 
ATOM   2175 C  CA    . LEU A 1 271 ? -10.073 1.311   9.600   1.00 9.52  ?  270 LEU A CA    1 
ATOM   2176 C  C     . LEU A 1 271 ? -11.364 0.820   10.247  1.00 11.55 ?  270 LEU A C     1 
ATOM   2177 O  O     . LEU A 1 271 ? -11.638 -0.380  10.212  1.00 13.90 ?  270 LEU A O     1 
ATOM   2178 C  CB    . LEU A 1 271 ? -10.241 1.338   8.089   1.00 10.83 ?  270 LEU A CB    1 
ATOM   2179 C  CG    . LEU A 1 271 ? -10.946 2.564   7.522   1.00 11.71 ?  270 LEU A CG    1 
ATOM   2180 C  CD1   . LEU A 1 271 ? -10.072 3.795   7.607   1.00 12.57 ?  270 LEU A CD1   1 
ATOM   2181 C  CD2   . LEU A 1 271 ? -11.280 2.308   6.049   1.00 14.20 ?  270 LEU A CD2   1 
ATOM   2182 N  N     . PRO A 1 272 ? -12.200 1.701   10.803  1.00 8.89  ?  271 PRO A N     1 
ATOM   2183 C  CA    . PRO A 1 272 ? -13.422 1.254   11.479  1.00 11.34 ?  271 PRO A CA    1 
ATOM   2184 C  C     . PRO A 1 272 ? -14.595 0.975   10.551  1.00 11.85 ?  271 PRO A C     1 
ATOM   2185 O  O     . PRO A 1 272 ? -15.692 0.737   11.059  1.00 12.29 ?  271 PRO A O     1 
ATOM   2186 C  CB    . PRO A 1 272 ? -13.753 2.453   12.399  1.00 11.29 ?  271 PRO A CB    1 
ATOM   2187 C  CG    . PRO A 1 272 ? -13.329 3.633   11.601  1.00 8.50  ?  271 PRO A CG    1 
ATOM   2188 C  CD    . PRO A 1 272 ? -11.977 3.143   11.018  1.00 8.54  ?  271 PRO A CD    1 
ATOM   2189 N  N     . VAL A 1 273 ? -14.404 1.063   9.234   1.00 12.27 ?  272 VAL A N     1 
ATOM   2190 C  CA    . VAL A 1 273 ? -15.431 0.807   8.217   1.00 12.76 ?  272 VAL A CA    1 
ATOM   2191 C  C     . VAL A 1 273 ? -14.763 -0.023  7.126   1.00 17.50 ?  272 VAL A C     1 
ATOM   2192 O  O     . VAL A 1 273 ? -13.549 -0.255  7.160   1.00 16.65 ?  272 VAL A O     1 
ATOM   2193 C  CB    . VAL A 1 273 ? -16.015 2.097   7.587   1.00 10.69 ?  272 VAL A CB    1 
ATOM   2194 C  CG1   . VAL A 1 273 ? -16.739 2.915   8.637   1.00 10.57 ?  272 VAL A CG1   1 
ATOM   2195 C  CG2   . VAL A 1 273 ? -14.941 2.889   6.885   1.00 11.28 ?  272 VAL A CG2   1 
ATOM   2196 N  N     . GLN A 1 274 ? -15.544 -0.414  6.120   1.00 18.72 ?  273 GLN A N     1 
ATOM   2197 C  CA    . GLN A 1 274 ? -14.976 -1.171  5.005   1.00 21.24 ?  273 GLN A CA    1 
ATOM   2198 C  C     . GLN A 1 274 ? -13.831 -0.414  4.339   1.00 17.35 ?  273 GLN A C     1 
ATOM   2199 O  O     . GLN A 1 274 ? -13.955 0.794   4.052   1.00 20.26 ?  273 GLN A O     1 
ATOM   2200 C  CB    . GLN A 1 274 ? -16.057 -1.474  3.959   1.00 28.12 ?  273 GLN A CB    1 
ATOM   2201 C  CG    . GLN A 1 274 ? -17.048 -2.518  4.416   1.00 34.59 ?  273 GLN A CG    1 
ATOM   2202 C  CD    . GLN A 1 274 ? -16.514 -3.937  4.264   1.00 41.63 ?  273 GLN A CD    1 
ATOM   2203 O  OE1   . GLN A 1 274 ? -15.429 -4.151  3.712   1.00 42.90 ?  273 GLN A OE1   1 
ATOM   2204 N  NE2   . GLN A 1 274 ? -17.276 -4.916  4.756   1.00 44.39 ?  273 GLN A NE2   1 
ATOM   2205 N  N     . PRO A 1 275 ? -12.723 -1.116  3.955   1.00 19.94 ?  274 PRO A N     1 
ATOM   2206 C  CA    . PRO A 1 275 ? -12.475 -2.556  4.020   1.00 22.51 ?  274 PRO A CA    1 
ATOM   2207 C  C     . PRO A 1 275 ? -11.784 -3.064  5.291   1.00 23.90 ?  274 PRO A C     1 
ATOM   2208 O  O     . PRO A 1 275 ? -11.206 -4.154  5.274   1.00 25.44 ?  274 PRO A O     1 
ATOM   2209 C  CB    . PRO A 1 275 ? -11.550 -2.785  2.817   1.00 22.28 ?  274 PRO A CB    1 
ATOM   2210 C  CG    . PRO A 1 275 ? -10.752 -1.526  2.733   1.00 22.86 ?  274 PRO A CG    1 
ATOM   2211 C  CD    . PRO A 1 275 ? -11.694 -0.409  3.170   1.00 21.19 ?  274 PRO A CD    1 
ATOM   2212 N  N     . TYR A 1 276 ? -11.811 -2.271  6.367   1.00 20.37 ?  275 TYR A N     1 
ATOM   2213 C  CA    . TYR A 1 276 ? -11.248 -2.654  7.665   1.00 17.01 ?  275 TYR A CA    1 
ATOM   2214 C  C     . TYR A 1 276 ? -9.735  -2.948  7.615   1.00 17.60 ?  275 TYR A C     1 
ATOM   2215 O  O     . TYR A 1 276 ? -9.213  -3.674  8.460   1.00 18.20 ?  275 TYR A O     1 
ATOM   2216 C  CB    . TYR A 1 276 ? -12.007 -3.831  8.267   1.00 23.23 ?  275 TYR A CB    1 
ATOM   2217 C  CG    . TYR A 1 276 ? -13.511 -3.576  8.364   1.00 25.90 ?  275 TYR A CG    1 
ATOM   2218 C  CD1   . TYR A 1 276 ? -14.041 -2.810  9.406   1.00 25.90 ?  275 TYR A CD1   1 
ATOM   2219 C  CD2   . TYR A 1 276 ? -14.385 -4.092  7.415   1.00 27.23 ?  275 TYR A CD2   1 
ATOM   2220 C  CE1   . TYR A 1 276 ? -15.422 -2.563  9.499   1.00 27.84 ?  275 TYR A CE1   1 
ATOM   2221 C  CE2   . TYR A 1 276 ? -15.779 -3.857  7.504   1.00 27.91 ?  275 TYR A CE2   1 
ATOM   2222 C  CZ    . TYR A 1 276 ? -16.277 -3.090  8.542   1.00 27.99 ?  275 TYR A CZ    1 
ATOM   2223 O  OH    . TYR A 1 276 ? -17.637 -2.852  8.617   1.00 29.00 ?  275 TYR A OH    1 
ATOM   2224 N  N     . ASN A 1 277 ? -9.032  -2.364  6.649   1.00 17.33 ?  276 ASN A N     1 
ATOM   2225 C  CA    . ASN A 1 277 ? -7.599  -2.614  6.457   1.00 13.99 ?  276 ASN A CA    1 
ATOM   2226 C  C     . ASN A 1 277 ? -6.785  -1.904  7.533   1.00 14.17 ?  276 ASN A C     1 
ATOM   2227 O  O     . ASN A 1 277 ? -7.210  -0.885  8.076   1.00 13.36 ?  276 ASN A O     1 
ATOM   2228 C  CB    . ASN A 1 277 ? -7.174  -2.119  5.078   1.00 15.69 ?  276 ASN A CB    1 
ATOM   2229 C  CG    . ASN A 1 277 ? -7.392  -0.621  4.911   1.00 17.79 ?  276 ASN A CG    1 
ATOM   2230 O  OD1   . ASN A 1 277 ? -8.537  -0.134  4.919   1.00 19.90 ?  276 ASN A OD1   1 
ATOM   2231 N  ND2   . ASN A 1 277 ? -6.300  0.122   4.766   1.00 21.10 ?  276 ASN A ND2   1 
ATOM   2232 N  N     . ASP A 1 278 ? -5.600  -2.448  7.843   1.00 11.54 ?  277 ASP A N     1 
ATOM   2233 C  CA    . ASP A 1 278 ? -4.661  -1.770  8.751   1.00 9.94  ?  277 ASP A CA    1 
ATOM   2234 C  C     . ASP A 1 278 ? -4.104  -0.557  8.012   1.00 11.63 ?  277 ASP A C     1 
ATOM   2235 O  O     . ASP A 1 278 ? -3.406  -0.692  7.006   1.00 11.73 ?  277 ASP A O     1 
ATOM   2236 C  CB    . ASP A 1 278 ? -3.550  -2.753  9.164   1.00 11.61 ?  277 ASP A CB    1 
ATOM   2237 C  CG    . ASP A 1 278 ? -2.363  -2.082  9.876   1.00 13.57 ?  277 ASP A CG    1 
ATOM   2238 O  OD1   . ASP A 1 278 ? -2.495  -0.946  10.341  1.00 10.89 ?  277 ASP A OD1   1 
ATOM   2239 O  OD2   . ASP A 1 278 ? -1.277  -2.718  9.936   1.00 13.30 -1 277 ASP A OD2   1 
ATOM   2240 N  N     . VAL A 1 279 ? -4.454  0.652   8.455   1.00 10.73 ?  278 VAL A N     1 
ATOM   2241 C  CA    . VAL A 1 279 ? -4.031  1.808   7.700   1.00 11.87 ?  278 VAL A CA    1 
ATOM   2242 C  C     . VAL A 1 279 ? -2.533  2.057   7.800   1.00 13.68 ?  278 VAL A C     1 
ATOM   2243 O  O     . VAL A 1 279 ? -2.005  2.871   7.039   1.00 14.49 ?  278 VAL A O     1 
ATOM   2244 C  CB    . VAL A 1 279 ? -4.822  3.047   8.157   1.00 14.31 ?  278 VAL A CB    1 
ATOM   2245 C  CG1   . VAL A 1 279 ? -6.324  2.840   7.863   1.00 16.09 ?  278 VAL A CG1   1 
ATOM   2246 C  CG2   . VAL A 1 279 ? -4.583  3.302   9.616   1.00 14.42 ?  278 VAL A CG2   1 
ATOM   2247 N  N     . PHE A 1 280 ? -1.831  1.356   8.686   1.00 10.96 ?  279 PHE A N     1 
ATOM   2248 C  CA    . PHE A 1 280 ? -0.373  1.485   8.768   1.00 8.90  ?  279 PHE A CA    1 
ATOM   2249 C  C     . PHE A 1 280 ? 0.362   0.363   8.060   1.00 11.41 ?  279 PHE A C     1 
ATOM   2250 O  O     . PHE A 1 280 ? 1.592   0.281   8.169   1.00 11.97 ?  279 PHE A O     1 
ATOM   2251 C  CB    . PHE A 1 280 ? 0.092   1.532   10.235  1.00 9.95  ?  279 PHE A CB    1 
ATOM   2252 C  CG    . PHE A 1 280 ? -0.042  2.879   10.910  1.00 11.88 ?  279 PHE A CG    1 
ATOM   2253 C  CD1   . PHE A 1 280 ? 0.673   3.974   10.461  1.00 16.92 ?  279 PHE A CD1   1 
ATOM   2254 C  CD2   . PHE A 1 280 ? -0.848  3.017   12.022  1.00 13.60 ?  279 PHE A CD2   1 
ATOM   2255 C  CE1   . PHE A 1 280 ? 0.558   5.178   11.117  1.00 16.56 ?  279 PHE A CE1   1 
ATOM   2256 C  CE2   . PHE A 1 280 ? -0.968  4.248   12.678  1.00 14.60 ?  279 PHE A CE2   1 
ATOM   2257 C  CZ    . PHE A 1 280 ? -0.258  5.299   12.217  1.00 14.62 ?  279 PHE A CZ    1 
ATOM   2258 N  N     . GLU A 1 281 ? -0.333  -0.445  7.248   1.00 14.39 ?  280 GLU A N     1 
ATOM   2259 C  CA    . GLU A 1 281 ? 0.293   -1.663  6.745   1.00 16.73 ?  280 GLU A CA    1 
ATOM   2260 C  C     . GLU A 1 281 ? 1.507   -1.377  5.862   1.00 16.36 ?  280 GLU A C     1 
ATOM   2261 O  O     . GLU A 1 281 ? 2.427   -2.215  5.792   1.00 18.54 ?  280 GLU A O     1 
ATOM   2262 C  CB    . GLU A 1 281 ? -0.739  -2.484  5.993   1.00 20.81 ?  280 GLU A CB    1 
ATOM   2263 C  CG    . GLU A 1 281 ? -1.418  -1.769  4.860   1.00 29.67 ?  280 GLU A CG    1 
ATOM   2264 C  CD    . GLU A 1 281 ? -2.657  -2.534  4.344   1.00 37.70 ?  280 GLU A CD    1 
ATOM   2265 O  OE1   . GLU A 1 281 ? -2.677  -3.783  4.457   1.00 41.13 ?  280 GLU A OE1   1 
ATOM   2266 O  OE2   . GLU A 1 281 ? -3.610  -1.886  3.838   1.00 38.97 -1 280 GLU A OE2   1 
ATOM   2267 N  N     . LYS A 1 282 ? 1.537   -0.234  5.178   1.00 18.78 ?  281 LYS A N     1 
ATOM   2268 C  CA    . LYS A 1 282 ? 2.636   -0.027  4.235   1.00 21.09 ?  281 LYS A CA    1 
ATOM   2269 C  C     . LYS A 1 282 ? 3.919   0.432   4.915   1.00 17.30 ?  281 LYS A C     1 
ATOM   2270 O  O     . LYS A 1 282 ? 5.004   0.339   4.311   1.00 18.70 ?  281 LYS A O     1 
ATOM   2271 C  CB    . LYS A 1 282 ? 2.219   0.971   3.156   1.00 32.51 ?  281 LYS A CB    1 
ATOM   2272 C  CG    . LYS A 1 282 ? 1.096   0.427   2.284   1.00 41.67 ?  281 LYS A CG    1 
ATOM   2273 C  CD    . LYS A 1 282 ? 1.324   -1.049  1.928   1.00 49.55 ?  281 LYS A CD    1 
ATOM   2274 C  CE    . LYS A 1 282 ? 2.207   -1.205  0.687   1.00 55.77 ?  281 LYS A CE    1 
ATOM   2275 N  NZ    . LYS A 1 282 ? 2.719   -2.596  0.539   1.00 58.64 1  281 LYS A NZ    1 
ATOM   2276 N  N     . MET A 1 283 ? 3.841   0.876   6.150   1.00 13.43 ?  282 MET A N     1 
ATOM   2277 C  CA    . MET A 1 283 ? 5.059   1.255   6.849   1.00 11.69 ?  282 MET A CA    1 
ATOM   2278 C  C     . MET A 1 283 ? 5.929   0.037   7.077   1.00 9.00  ?  282 MET A C     1 
ATOM   2279 O  O     . MET A 1 283 ? 5.460   -1.012  7.537   1.00 12.83 ?  282 MET A O     1 
ATOM   2280 C  CB    . MET A 1 283 ? 4.717   1.944   8.166   1.00 14.75 ?  282 MET A CB    1 
ATOM   2281 C  CG    . MET A 1 283 ? 4.187   3.332   7.946   1.00 23.10 ?  282 MET A CG    1 
ATOM   2282 S  SD    . MET A 1 283 ? 3.980   4.238   9.493   1.00 23.90 ?  282 MET A SD    1 
ATOM   2283 C  CE    . MET A 1 283 ? 5.443   3.658   10.408  1.00 4.63  ?  282 MET A CE    1 
ATOM   2284 N  N     . THR A 1 284 ? 7.215   0.166   6.769   1.00 9.42  ?  283 THR A N     1 
ATOM   2285 C  CA    . THR A 1 284 ? 8.132   -0.930  6.986   1.00 9.53  ?  283 THR A CA    1 
ATOM   2286 C  C     . THR A 1 284 ? 8.429   -1.112  8.473   1.00 10.96 ?  283 THR A C     1 
ATOM   2287 O  O     . THR A 1 284 ? 8.133   -0.248  9.314   1.00 9.46  ?  283 THR A O     1 
ATOM   2288 C  CB    . THR A 1 284 ? 9.450   -0.681  6.246   1.00 12.56 ?  283 THR A CB    1 
ATOM   2289 O  OG1   . THR A 1 284 ? 10.131  0.410   6.884   1.00 12.34 ?  283 THR A OG1   1 
ATOM   2290 C  CG2   . THR A 1 284 ? 9.193   -0.322  4.792   1.00 13.71 ?  283 THR A CG2   1 
ATOM   2291 N  N     . GLY A 1 285 ? 8.964   -2.282  8.820   1.00 10.77 ?  284 GLY A N     1 
ATOM   2292 C  CA    . GLY A 1 285 ? 9.350   -2.502  10.211  1.00 9.45  ?  284 GLY A CA    1 
ATOM   2293 C  C     . GLY A 1 285 ? 10.326  -1.454  10.735  1.00 9.11  ?  284 GLY A C     1 
ATOM   2294 O  O     . GLY A 1 285 ? 10.200  -0.995  11.877  1.00 8.26  ?  284 GLY A O     1 
ATOM   2295 N  N     . MET A 1 286 ? 11.332  -1.093  9.921   1.00 9.03  ?  285 MET A N     1 
ATOM   2296 C  CA    . MET A 1 286 ? 12.310  -0.108  10.397  1.00 8.62  ?  285 MET A CA    1 
ATOM   2297 C  C     . MET A 1 286 ? 11.656  1.250   10.586  1.00 9.23  ?  285 MET A C     1 
ATOM   2298 O  O     . MET A 1 286 ? 11.967  1.978   11.550  1.00 8.62  ?  285 MET A O     1 
ATOM   2299 C  CB    . MET A 1 286 ? 13.487  -0.006  9.419   1.00 10.54 ?  285 MET A CB    1 
ATOM   2300 C  CG    . MET A 1 286 ? 14.413  -1.240  9.481   1.00 13.08 ?  285 MET A CG    1 
ATOM   2301 S  SD    . MET A 1 286 ? 15.287  -1.249  11.037  1.00 14.24 ?  285 MET A SD    1 
ATOM   2302 C  CE    . MET A 1 286 ? 16.566  -0.049  10.569  1.00 14.04 ?  285 MET A CE    1 
ATOM   2303 N  N     . GLN A 1 287 ? 10.707  1.594   9.709   1.00 7.85  ?  286 GLN A N     1 
ATOM   2304 C  CA    . GLN A 1 287 ? 9.969   2.849   9.889   1.00 5.89  ?  286 GLN A CA    1 
ATOM   2305 C  C     . GLN A 1 287 ? 9.077   2.809   11.108  1.00 7.72  ?  286 GLN A C     1 
ATOM   2306 O  O     . GLN A 1 287 ? 8.914   3.823   11.802  1.00 8.46  ?  286 GLN A O     1 
ATOM   2307 C  CB    . GLN A 1 287 ? 9.124   3.121   8.650   1.00 5.72  ?  286 GLN A CB    1 
ATOM   2308 C  CG    . GLN A 1 287 ? 9.995   3.505   7.444   1.00 9.30  ?  286 GLN A CG    1 
ATOM   2309 C  CD    . GLN A 1 287 ? 9.258   3.394   6.141   1.00 12.15 ?  286 GLN A CD    1 
ATOM   2310 O  OE1   . GLN A 1 287 ? 8.144   2.909   6.072   1.00 11.33 ?  286 GLN A OE1   1 
ATOM   2311 N  NE2   . GLN A 1 287 ? 9.900   3.880   5.060   1.00 15.55 ?  286 GLN A NE2   1 
ATOM   2312 N  N     . MET A 1 288 ? 8.443   1.661   11.364  1.00 8.17  ?  287 MET A N     1 
ATOM   2313 C  CA    . MET A 1 288 ? 7.690   1.507   12.612  1.00 6.77  ?  287 MET A CA    1 
ATOM   2314 C  C     . MET A 1 288 ? 8.576   1.684   13.833  1.00 7.45  ?  287 MET A C     1 
ATOM   2315 O  O     . MET A 1 288 ? 8.151   2.270   14.829  1.00 8.70  ?  287 MET A O     1 
ATOM   2316 C  CB    . MET A 1 288 ? 7.009   0.141   12.620  1.00 9.14  ?  287 MET A CB    1 
ATOM   2317 C  CG    . MET A 1 288 ? 5.712   0.188   11.851  1.00 9.02  ?  287 MET A CG    1 
ATOM   2318 S  SD    . MET A 1 288 ? 4.475   0.891   12.941  1.00 10.12 ?  287 MET A SD    1 
ATOM   2319 C  CE    . MET A 1 288 ? 3.189   1.055   11.727  1.00 10.93 ?  287 MET A CE    1 
ATOM   2320 N  N     . GLU A 1 289 ? 9.774   1.118   13.811  1.00 8.55  ?  288 GLU A N     1 
ATOM   2321 C  CA    . GLU A 1 289 ? 10.665  1.245   14.955  1.00 9.41  ?  288 GLU A CA    1 
ATOM   2322 C  C     . GLU A 1 289 ? 10.994  2.709   15.197  1.00 7.75  ?  288 GLU A C     1 
ATOM   2323 O  O     . GLU A 1 289 ? 10.971  3.201   16.339  1.00 8.65  ?  288 GLU A O     1 
ATOM   2324 C  CB    . GLU A 1 289 ? 11.945  0.428   14.701  1.00 10.18 ?  288 GLU A CB    1 
ATOM   2325 C  CG    . GLU A 1 289 ? 12.951  0.484   15.777  1.00 11.55 ?  288 GLU A CG    1 
ATOM   2326 C  CD    . GLU A 1 289 ? 14.177  -0.332  15.418  1.00 16.61 ?  288 GLU A CD    1 
ATOM   2327 O  OE1   . GLU A 1 289 ? 15.013  0.128   14.609  1.00 15.58 ?  288 GLU A OE1   1 
ATOM   2328 O  OE2   . GLU A 1 289 ? 14.306  -1.456  15.951  1.00 19.63 -1 288 GLU A OE2   1 
ATOM   2329 N  N     . SER A 1 290 ? 11.244  3.447   14.110  1.00 6.57  ?  289 SER A N     1 
ATOM   2330 C  CA    . SER A 1 290 ? 11.555  4.864   14.278  1.00 7.09  ?  289 SER A CA    1 
ATOM   2331 C  C     . SER A 1 290 ? 10.323  5.631   14.752  1.00 7.79  ?  289 SER A C     1 
ATOM   2332 O  O     . SER A 1 290 ? 10.415  6.516   15.617  1.00 9.16  ?  289 SER A O     1 
ATOM   2333 C  CB    . SER A 1 290 ? 12.115  5.422   12.966  1.00 10.32 ?  289 SER A CB    1 
ATOM   2334 O  OG    . SER A 1 290 ? 12.555  6.782   13.165  1.00 14.56 ?  289 SER A OG    1 
ATOM   2335 N  N     . PHE A 1 291 ? 9.164   5.302   14.205  1.00 7.58  ?  290 PHE A N     1 
ATOM   2336 C  CA    . PHE A 1 291 ? 7.915   5.925   14.643  1.00 7.00  ?  290 PHE A CA    1 
ATOM   2337 C  C     . PHE A 1 291 ? 7.717   5.723   16.139  1.00 8.16  ?  290 PHE A C     1 
ATOM   2338 O  O     . PHE A 1 291 ? 7.395   6.670   16.864  1.00 8.23  ?  290 PHE A O     1 
ATOM   2339 C  CB    . PHE A 1 291 ? 6.797   5.342   13.760  1.00 6.75  ?  290 PHE A CB    1 
ATOM   2340 C  CG    . PHE A 1 291 ? 5.371   5.694   14.139  1.00 6.06  ?  290 PHE A CG    1 
ATOM   2341 C  CD1   . PHE A 1 291 ? 5.011   6.921   14.654  1.00 6.14  ?  290 PHE A CD1   1 
ATOM   2342 C  CD2   . PHE A 1 291 ? 4.362   4.773   13.863  1.00 8.57  ?  290 PHE A CD2   1 
ATOM   2343 C  CE1   . PHE A 1 291 ? 3.674   7.186   14.924  1.00 7.51  ?  290 PHE A CE1   1 
ATOM   2344 C  CE2   . PHE A 1 291 ? 3.018   5.038   14.152  1.00 10.80 ?  290 PHE A CE2   1 
ATOM   2345 C  CZ    . PHE A 1 291 ? 2.677   6.268   14.670  1.00 9.24  ?  290 PHE A CZ    1 
ATOM   2346 N  N     . LYS A 1 292 ? 7.909   4.491   16.622  1.00 7.56  ?  291 LYS A N     1 
ATOM   2347 C  CA    . LYS A 1 292 ? 7.747   4.231   18.045  1.00 8.48  ?  291 LYS A CA    1 
ATOM   2348 C  C     . LYS A 1 292 ? 8.719   5.077   18.866  1.00 8.06  ?  291 LYS A C     1 
ATOM   2349 O  O     . LYS A 1 292 ? 8.318   5.682   19.864  1.00 7.97  ?  291 LYS A O     1 
ATOM   2350 C  CB    . LYS A 1 292 ? 7.947   2.737   18.318  1.00 8.49  ?  291 LYS A CB    1 
ATOM   2351 C  CG    . LYS A 1 292 ? 7.653   2.365   19.755  1.00 9.47  ?  291 LYS A CG    1 
ATOM   2352 C  CD    . LYS A 1 292 ? 8.039   0.875   20.016  1.00 10.48 ?  291 LYS A CD    1 
ATOM   2353 C  CE    . LYS A 1 292 ? 7.559   0.564   21.410  1.00 14.26 ?  291 LYS A CE    1 
ATOM   2354 N  NZ    . LYS A 1 292 ? 7.999   -0.836  21.840  1.00 17.91 1  291 LYS A NZ    1 
ATOM   2355 N  N     . SER A 1 293 ? 9.994   5.145   18.443  1.00 7.61  ?  292 SER A N     1 
ATOM   2356 C  CA    . SER A 1 293 ? 10.985  5.914   19.190  1.00 6.83  ?  292 SER A CA    1 
ATOM   2357 C  C     . SER A 1 293 ? 10.593  7.388   19.266  1.00 8.06  ?  292 SER A C     1 
ATOM   2358 O  O     . SER A 1 293 ? 10.727  8.041   20.312  1.00 9.91  ?  292 SER A O     1 
ATOM   2359 C  CB    . SER A 1 293 ? 12.336  5.782   18.486  1.00 11.74 ?  292 SER A CB    1 
ATOM   2360 O  OG    . SER A 1 293 ? 13.367  6.346   19.283  1.00 19.67 ?  292 SER A OG    1 
ATOM   2361 N  N     . LYS A 1 294 ? 10.117  7.933   18.141  1.00 7.27  ?  293 LYS A N     1 
ATOM   2362 C  CA    . LYS A 1 294 ? 9.748   9.336   18.132  1.00 7.68  ?  293 LYS A CA    1 
ATOM   2363 C  C     . LYS A 1 294 ? 8.481   9.593   18.946  1.00 7.06  ?  293 LYS A C     1 
ATOM   2364 O  O     . LYS A 1 294 ? 8.372   10.636  19.604  1.00 7.47  ?  293 LYS A O     1 
ATOM   2365 C  CB    . LYS A 1 294 ? 9.602   9.841   16.684  1.00 9.48  ?  293 LYS A CB    1 
ATOM   2366 C  CG    . LYS A 1 294 ? 10.926  10.498  16.221  1.00 15.52 ?  293 LYS A CG    1 
ATOM   2367 C  CD    . LYS A 1 294 ? 10.871  11.077  14.786  1.00 18.16 ?  293 LYS A CD    1 
ATOM   2368 C  CE    . LYS A 1 294 ? 10.841  9.980   13.808  1.00 16.02 ?  293 LYS A CE    1 
ATOM   2369 N  NZ    . LYS A 1 294 ? 11.058  10.531  12.395  1.00 12.86 1  293 LYS A NZ    1 
ATOM   2370 N  N     . LEU A 1 295 ? 7.537   8.656   18.943  1.00 7.53  ?  294 LEU A N     1 
ATOM   2371 C  CA    . LEU A 1 295 ? 6.374   8.817   19.802  1.00 8.21  ?  294 LEU A CA    1 
ATOM   2372 C  C     . LEU A 1 295 ? 6.788   8.792   21.263  1.00 7.27  ?  294 LEU A C     1 
ATOM   2373 O  O     . LEU A 1 295 ? 6.264   9.544   22.086  1.00 6.36  ?  294 LEU A O     1 
ATOM   2374 C  CB    . LEU A 1 295 ? 5.380   7.691   19.533  1.00 10.86 ?  294 LEU A CB    1 
ATOM   2375 C  CG    . LEU A 1 295 ? 4.284   7.738   18.495  1.00 13.94 ?  294 LEU A CG    1 
ATOM   2376 C  CD1   . LEU A 1 295 ? 3.539   6.416   18.574  1.00 15.49 ?  294 LEU A CD1   1 
ATOM   2377 C  CD2   . LEU A 1 295 ? 3.338   8.850   18.796  1.00 11.12 ?  294 LEU A CD2   1 
ATOM   2378 N  N     . GLN A 1 296 ? 7.742   7.923   21.604  1.00 8.05  ?  295 GLN A N     1 
ATOM   2379 C  CA    . GLN A 1 296 ? 8.205   7.897   22.983  1.00 7.51  ?  295 GLN A CA    1 
ATOM   2380 C  C     . GLN A 1 296 ? 8.872   9.210   23.368  1.00 8.69  ?  295 GLN A C     1 
ATOM   2381 O  O     . GLN A 1 296 ? 8.675   9.711   24.488  1.00 10.38 ?  295 GLN A O     1 
ATOM   2382 C  CB    . GLN A 1 296 ? 9.158   6.713   23.199  1.00 9.58  ?  295 GLN A CB    1 
ATOM   2383 C  CG    . GLN A 1 296 ? 9.612   6.560   24.651  1.00 14.80 ?  295 GLN A CG    1 
ATOM   2384 C  CD    . GLN A 1 296 ? 8.466   6.259   25.605  1.00 21.48 ?  295 GLN A CD    1 
ATOM   2385 O  OE1   . GLN A 1 296 ? 7.772   5.248   25.455  1.00 22.33 ?  295 GLN A OE1   1 
ATOM   2386 N  NE2   . GLN A 1 296 ? 8.272   7.135   26.610  1.00 22.68 ?  295 GLN A NE2   1 
ATOM   2387 N  N     . ALA A 1 297 ? 9.666   9.792   22.459  1.00 8.97  ?  296 ALA A N     1 
ATOM   2388 C  CA    . ALA A 1 297 ? 10.281  11.089  22.759  1.00 7.20  ?  296 ALA A CA    1 
ATOM   2389 C  C     . ALA A 1 297 ? 9.224   12.178  22.937  1.00 7.13  ?  296 ALA A C     1 
ATOM   2390 O  O     . ALA A 1 297 ? 9.353   13.046  23.820  1.00 6.89  ?  296 ALA A O     1 
ATOM   2391 C  CB    . ALA A 1 297 ? 11.268  11.465  21.646  1.00 6.55  ?  296 ALA A CB    1 
ATOM   2392 N  N     . LEU A 1 298 ? 8.181   12.148  22.095  1.00 6.44  ?  297 LEU A N     1 
ATOM   2393 C  CA    . LEU A 1 298 ? 7.080   13.097  22.242  1.00 4.84  ?  297 LEU A CA    1 
ATOM   2394 C  C     . LEU A 1 298 ? 6.405   12.912  23.598  1.00 5.95  ?  297 LEU A C     1 
ATOM   2395 O  O     . LEU A 1 298 ? 6.127   13.890  24.293  1.00 6.79  ?  297 LEU A O     1 
ATOM   2396 C  CB    . LEU A 1 298 ? 6.093   12.912  21.089  1.00 6.32  ?  297 LEU A CB    1 
ATOM   2397 C  CG    . LEU A 1 298 ? 4.772   13.670  21.264  1.00 5.70  ?  297 LEU A CG    1 
ATOM   2398 C  CD1   . LEU A 1 298 ? 5.040   15.180  21.299  1.00 8.03  ?  297 LEU A CD1   1 
ATOM   2399 C  CD2   . LEU A 1 298 ? 3.859   13.317  20.164  1.00 7.44  ?  297 LEU A CD2   1 
ATOM   2400 N  N     . LEU A 1 299 ? 6.142   11.662  23.977  1.00 6.02  ?  298 LEU A N     1 
ATOM   2401 C  CA    . LEU A 1 299 ? 5.515   11.408  25.278  1.00 7.08  ?  298 LEU A CA    1 
ATOM   2402 C  C     . LEU A 1 299 ? 6.355   11.973  26.423  1.00 8.74  ?  298 LEU A C     1 
ATOM   2403 O  O     . LEU A 1 299 ? 5.814   12.604  27.347  1.00 8.59  ?  298 LEU A O     1 
ATOM   2404 C  CB    . LEU A 1 299 ? 5.297   9.916   25.434  1.00 7.01  ?  298 LEU A CB    1 
ATOM   2405 C  CG    . LEU A 1 299 ? 4.645   9.530   26.769  1.00 7.57  ?  298 LEU A CG    1 
ATOM   2406 C  CD1   . LEU A 1 299 ? 3.277   10.171  26.922  1.00 8.43  ?  298 LEU A CD1   1 
ATOM   2407 C  CD2   . LEU A 1 299 ? 4.530   8.017   26.783  1.00 13.44 ?  298 LEU A CD2   1 
ATOM   2408 N  N     . ASN A 1 300 ? 7.670   11.731  26.383  1.00 8.78  ?  299 ASN A N     1 
ATOM   2409 C  CA    . ASN A 1 300 ? 8.560   12.240  27.423  1.00 9.13  ?  299 ASN A CA    1 
ATOM   2410 C  C     . ASN A 1 300 ? 8.502   13.761  27.475  1.00 9.69  ?  299 ASN A C     1 
ATOM   2411 O  O     . ASN A 1 300 ? 8.542   14.369  28.560  1.00 11.05 ?  299 ASN A O     1 
ATOM   2412 C  CB    . ASN A 1 300 ? 9.989   11.748  27.143  1.00 10.99 ?  299 ASN A CB    1 
ATOM   2413 C  CG    . ASN A 1 300 ? 10.125  10.228  27.291  1.00 13.30 ?  299 ASN A CG    1 
ATOM   2414 O  OD1   . ASN A 1 300 ? 9.274   9.566   27.864  1.00 17.79 ?  299 ASN A OD1   1 
ATOM   2415 N  ND2   . ASN A 1 300 ? 11.207  9.681   26.750  1.00 18.55 ?  299 ASN A ND2   1 
ATOM   2416 N  N     . ALA A 1 301 ? 8.423   14.399  26.314  1.00 7.93  ?  300 ALA A N     1 
ATOM   2417 C  CA    . ALA A 1 301 ? 8.315   15.853  26.299  1.00 7.88  ?  300 ALA A CA    1 
ATOM   2418 C  C     . ALA A 1 301 ? 6.989   16.330  26.876  1.00 9.85  ?  300 ALA A C     1 
ATOM   2419 O  O     . ALA A 1 301 ? 6.938   17.379  27.521  1.00 9.30  ?  300 ALA A O     1 
ATOM   2420 C  CB    . ALA A 1 301 ? 8.443   16.381  24.865  1.00 8.65  ?  300 ALA A CB    1 
ATOM   2421 N  N     . LEU A 1 302 ? 5.895   15.644  26.542  1.00 7.80  ?  301 LEU A N     1 
ATOM   2422 C  CA    . LEU A 1 302 ? 4.592   16.034  27.084  1.00 6.94  ?  301 LEU A CA    1 
ATOM   2423 C  C     . LEU A 1 302 ? 4.616   15.962  28.613  1.00 8.95  ?  301 LEU A C     1 
ATOM   2424 O  O     . LEU A 1 302 ? 4.028   16.820  29.303  1.00 9.80  ?  301 LEU A O     1 
ATOM   2425 C  CB    . LEU A 1 302 ? 3.496   15.135  26.519  1.00 6.04  ?  301 LEU A CB    1 
ATOM   2426 C  CG    . LEU A 1 302 ? 3.204   15.357  25.015  1.00 5.72  ?  301 LEU A CG    1 
ATOM   2427 C  CD1   . LEU A 1 302 ? 2.366   14.151  24.451  1.00 7.01  ?  301 LEU A CD1   1 
ATOM   2428 C  CD2   . LEU A 1 302 ? 2.460   16.692  24.823  1.00 7.54  ?  301 LEU A CD2   1 
ATOM   2429 N  N     . LYS A 1 303 ? 5.327   14.959  29.144  1.00 10.79 ?  302 LYS A N     1 
ATOM   2430 C  CA    . LYS A 1 303 ? 5.423   14.825  30.608  1.00 12.60 ?  302 LYS A CA    1 
ATOM   2431 C  C     . LYS A 1 303 ? 6.309   15.906  31.200  1.00 16.35 ?  302 LYS A C     1 
ATOM   2432 O  O     . LYS A 1 303 ? 5.985   16.502  32.244  1.00 13.97 ?  302 LYS A O     1 
ATOM   2433 C  CB    . LYS A 1 303 ? 5.940   13.435  30.984  1.00 13.57 ?  302 LYS A CB    1 
ATOM   2434 C  CG    . LYS A 1 303 ? 4.948   12.342  30.762  1.00 16.38 ?  302 LYS A CG    1 
ATOM   2435 C  CD    . LYS A 1 303 ? 5.527   10.982  31.013  1.00 21.28 ?  302 LYS A CD    1 
ATOM   2436 C  CE    . LYS A 1 303 ? 4.399   9.962   31.021  1.00 26.31 ?  302 LYS A CE    1 
ATOM   2437 N  NZ    . LYS A 1 303 ? 4.621   8.839   31.983  1.00 30.73 1  302 LYS A NZ    1 
ATOM   2438 N  N     . THR A 1 304 ? 7.422   16.203  30.536  1.00 14.98 ?  303 THR A N     1 
ATOM   2439 C  CA    . THR A 1 304 ? 8.292   17.275  30.999  1.00 14.89 ?  303 THR A CA    1 
ATOM   2440 C  C     . THR A 1 304 ? 7.563   18.611  31.021  1.00 17.90 ?  303 THR A C     1 
ATOM   2441 O  O     . THR A 1 304 ? 7.730   19.408  31.961  1.00 16.24 ?  303 THR A O     1 
ATOM   2442 C  CB    . THR A 1 304 ? 9.518   17.354  30.090  1.00 18.64 ?  303 THR A CB    1 
ATOM   2443 O  OG1   . THR A 1 304 ? 10.249  16.146  30.224  1.00 20.17 ?  303 THR A OG1   1 
ATOM   2444 C  CG2   . THR A 1 304 ? 10.382  18.523  30.458  1.00 20.63 ?  303 THR A CG2   1 
ATOM   2445 N  N     . ALA A 1 305 ? 6.772   18.895  29.982  1.00 14.53 ?  304 ALA A N     1 
ATOM   2446 C  CA    . ALA A 1 305 ? 6.000   20.131  29.909  1.00 15.89 ?  304 ALA A CA    1 
ATOM   2447 C  C     . ALA A 1 305 ? 4.924   20.215  30.975  1.00 17.04 ?  304 ALA A C     1 
ATOM   2448 O  O     . ALA A 1 305 ? 4.303   21.281  31.110  1.00 21.38 ?  304 ALA A O     1 
ATOM   2449 C  CB    . ALA A 1 305 ? 5.322   20.252  28.550  1.00 15.75 ?  304 ALA A CB    1 
ATOM   2450 N  N     . LYS A 1 306 ? 4.632   19.122  31.674  1.00 14.36 ?  305 LYS A N     1 
ATOM   2451 C  CA    . LYS A 1 306 ? 3.712   19.279  32.802  1.00 15.73 ?  305 LYS A CA    1 
ATOM   2452 C  C     . LYS A 1 306 ? 4.378   19.903  34.015  1.00 21.47 ?  305 LYS A C     1 
ATOM   2453 O  O     . LYS A 1 306 ? 3.702   20.561  34.819  1.00 26.35 ?  305 LYS A O     1 
ATOM   2454 C  CB    . LYS A 1 306 ? 3.147   17.939  33.190  1.00 14.46 ?  305 LYS A CB    1 
ATOM   2455 C  CG    . LYS A 1 306 ? 1.974   18.011  34.111  1.00 16.07 ?  305 LYS A CG    1 
ATOM   2456 C  CD    . LYS A 1 306 ? 1.546   16.584  34.407  1.00 17.80 ?  305 LYS A CD    1 
ATOM   2457 C  CE    . LYS A 1 306 ? 0.256   16.555  35.225  1.00 20.00 ?  305 LYS A CE    1 
ATOM   2458 N  NZ    . LYS A 1 306 ? -0.221  15.144  35.303  1.00 20.79 1  305 LYS A NZ    1 
ATOM   2459 N  N     . SER A 1 307 ? 5.692   19.729  34.158  1.00 19.08 ?  306 SER A N     1 
ATOM   2460 C  CA    . SER A 1 307 ? 6.358   19.929  35.437  1.00 20.35 ?  306 SER A CA    1 
ATOM   2461 C  C     . SER A 1 307 ? 7.436   21.000  35.393  1.00 20.30 ?  306 SER A C     1 
ATOM   2462 O  O     . SER A 1 307 ? 8.383   20.956  36.180  1.00 24.85 ?  306 SER A O     1 
ATOM   2463 C  CB    . SER A 1 307 ? 6.954   18.612  35.891  1.00 19.97 ?  306 SER A CB    1 
ATOM   2464 O  OG    . SER A 1 307 ? 7.830   18.140  34.887  1.00 23.27 ?  306 SER A OG    1 
ATOM   2465 N  N     . ARG A 1 308 ? 7.322   21.984  34.522  1.00 20.03 ?  307 ARG A N     1 
ATOM   2466 C  CA    . ARG A 1 308 ? 8.284   23.073  34.509  1.00 18.42 ?  307 ARG A CA    1 
ATOM   2467 C  C     . ARG A 1 308 ? 7.745   24.226  35.341  1.00 22.80 ?  307 ARG A C     1 
ATOM   2468 O  O     . ARG A 1 308 ? 6.550   24.534  35.292  1.00 22.19 ?  307 ARG A O     1 
ATOM   2469 C  CB    . ARG A 1 308 ? 8.582   23.577  33.101  1.00 18.46 ?  307 ARG A CB    1 
ATOM   2470 C  CG    . ARG A 1 308 ? 9.139   22.529  32.148  1.00 17.80 ?  307 ARG A CG    1 
ATOM   2471 C  CD    . ARG A 1 308 ? 10.419  21.945  32.636  1.00 18.72 ?  307 ARG A CD    1 
ATOM   2472 N  NE    . ARG A 1 308 ? 10.174  20.752  33.441  1.00 22.78 ?  307 ARG A NE    1 
ATOM   2473 C  CZ    . ARG A 1 308 ? 11.116  20.148  34.144  1.00 25.98 ?  307 ARG A CZ    1 
ATOM   2474 N  NH1   . ARG A 1 308 ? 12.356  20.641  34.148  1.00 29.83 1  307 ARG A NH1   1 
ATOM   2475 N  NH2   . ARG A 1 308 ? 10.818  19.081  34.849  1.00 26.57 ?  307 ARG A NH2   1 
ATOM   2476 N  N     . LEU A 1 309 ? 8.644   24.871  36.091  1.00 22.08 ?  308 LEU A N     1 
ATOM   2477 C  CA    . LEU A 1 309 ? 8.279   26.109  36.773  1.00 23.15 ?  308 LEU A CA    1 
ATOM   2478 C  C     . LEU A 1 309 ? 8.030   27.235  35.801  1.00 22.19 ?  308 LEU A C     1 
ATOM   2479 O  O     . LEU A 1 309 ? 7.105   28.029  35.990  1.00 24.14 ?  308 LEU A O     1 
ATOM   2480 C  CB    . LEU A 1 309 ? 9.391   26.531  37.742  1.00 25.20 ?  308 LEU A CB    1 
ATOM   2481 C  CG    . LEU A 1 309 ? 9.617   25.549  38.877  1.00 27.64 ?  308 LEU A CG    1 
ATOM   2482 C  CD1   . LEU A 1 309 ? 10.971  25.839  39.547  1.00 27.79 ?  308 LEU A CD1   1 
ATOM   2483 C  CD2   . LEU A 1 309 ? 8.467   25.592  39.886  1.00 29.29 ?  308 LEU A CD2   1 
ATOM   2484 N  N     . GLU A 1 310 ? 8.875   27.355  34.797  1.00 22.40 ?  309 GLU A N     1 
ATOM   2485 C  CA    . GLU A 1 310 ? 8.863   28.477  33.882  1.00 24.85 ?  309 GLU A CA    1 
ATOM   2486 C  C     . GLU A 1 310 ? 8.112   28.077  32.623  1.00 21.84 ?  309 GLU A C     1 
ATOM   2487 O  O     . GLU A 1 310 ? 8.376   27.003  32.054  1.00 18.22 ?  309 GLU A O     1 
ATOM   2488 C  CB    . GLU A 1 310 ? 10.285  28.911  33.526  1.00 34.24 ?  309 GLU A CB    1 
ATOM   2489 C  CG    . GLU A 1 310 ? 10.954  29.744  34.615  1.00 43.20 ?  309 GLU A CG    1 
ATOM   2490 C  CD    . GLU A 1 310 ? 10.981  31.232  34.281  1.00 52.40 ?  309 GLU A CD    1 
ATOM   2491 O  OE1   . GLU A 1 310 ? 11.810  31.961  34.877  1.00 58.94 ?  309 GLU A OE1   1 
ATOM   2492 O  OE2   . GLU A 1 310 ? 10.190  31.672  33.413  1.00 54.59 -1 309 GLU A OE2   1 
ATOM   2493 N  N     . LEU A 1 311 ? 7.211   28.961  32.180  1.00 19.54 ?  310 LEU A N     1 
ATOM   2494 C  CA    . LEU A 1 311 ? 6.421   28.682  30.985  1.00 18.92 ?  310 LEU A CA    1 
ATOM   2495 C  C     . LEU A 1 311 ? 7.322   28.531  29.770  1.00 19.01 ?  310 LEU A C     1 
ATOM   2496 O  O     . LEU A 1 311 ? 7.102   27.646  28.930  1.00 16.28 ?  310 LEU A O     1 
ATOM   2497 C  CB    . LEU A 1 311 ? 5.390   29.794  30.776  1.00 18.52 ?  310 LEU A CB    1 
ATOM   2498 C  CG    . LEU A 1 311 ? 4.436   29.686  29.584  1.00 18.88 ?  310 LEU A CG    1 
ATOM   2499 C  CD1   . LEU A 1 311 ? 3.575   28.470  29.721  1.00 16.12 ?  310 LEU A CD1   1 
ATOM   2500 C  CD2   . LEU A 1 311 ? 3.580   30.933  29.604  1.00 18.03 ?  310 LEU A CD2   1 
ATOM   2501 N  N     . HIS A 1 312 ? 8.357   29.370  29.678  1.00 18.49 ?  311 HIS A N     1 
ATOM   2502 C  CA    . HIS A 1 312 ? 9.372   29.225  28.638  1.00 16.95 ?  311 HIS A CA    1 
ATOM   2503 C  C     . HIS A 1 312 ? 9.877   27.792  28.536  1.00 16.20 ?  311 HIS A C     1 
ATOM   2504 O  O     . HIS A 1 312 ? 9.983   27.253  27.426  1.00 14.97 ?  311 HIS A O     1 
ATOM   2505 C  CB    . HIS A 1 312 ? 10.563  30.155  28.902  1.00 19.92 ?  311 HIS A CB    1 
ATOM   2506 C  CG    . HIS A 1 312 ? 11.671  30.004  27.899  1.00 17.19 ?  311 HIS A CG    1 
ATOM   2507 N  ND1   . HIS A 1 312 ? 11.700  30.704  26.714  1.00 20.97 ?  311 HIS A ND1   1 
ATOM   2508 C  CD2   . HIS A 1 312 ? 12.768  29.213  27.895  1.00 20.51 ?  311 HIS A CD2   1 
ATOM   2509 C  CE1   . HIS A 1 312 ? 12.769  30.352  26.023  1.00 21.66 ?  311 HIS A CE1   1 
ATOM   2510 N  NE2   . HIS A 1 312 ? 13.432  29.446  26.717  1.00 19.88 ?  311 HIS A NE2   1 
ATOM   2511 N  N     . ASP A 1 313 ? 10.212  27.163  29.671  1.00 14.44 ?  312 ASP A N     1 
ATOM   2512 C  CA    . ASP A 1 313 ? 10.805  25.821  29.622  1.00 15.13 ?  312 ASP A CA    1 
ATOM   2513 C  C     . ASP A 1 313 ? 9.779   24.769  29.179  1.00 15.56 ?  312 ASP A C     1 
ATOM   2514 O  O     . ASP A 1 313 ? 10.104  23.857  28.389  1.00 15.18 ?  312 ASP A O     1 
ATOM   2515 C  CB    . ASP A 1 313 ? 11.397  25.411  30.967  1.00 17.18 ?  312 ASP A CB    1 
ATOM   2516 C  CG    . ASP A 1 313 ? 12.640  26.222  31.357  1.00 20.72 ?  312 ASP A CG    1 
ATOM   2517 O  OD1   . ASP A 1 313 ? 13.358  26.749  30.491  1.00 22.23 ?  312 ASP A OD1   1 
ATOM   2518 O  OD2   . ASP A 1 313 ? 12.894  26.308  32.558  1.00 23.37 -1 312 ASP A OD2   1 
ATOM   2519 N  N     . ALA A 1 314 ? 8.548   24.860  29.699  1.00 14.14 ?  313 ALA A N     1 
ATOM   2520 C  CA    . ALA A 1 314 ? 7.494   23.920  29.292  1.00 13.27 ?  313 ALA A CA    1 
ATOM   2521 C  C     . ALA A 1 314 ? 7.257   24.023  27.794  1.00 14.00 ?  313 ALA A C     1 
ATOM   2522 O  O     . ALA A 1 314 ? 7.168   23.005  27.071  1.00 12.32 ?  313 ALA A O     1 
ATOM   2523 C  CB    . ALA A 1 314 ? 6.201   24.257  30.053  1.00 14.46 ?  313 ALA A CB    1 
ATOM   2524 N  N     . CYS A 1 315 ? 7.218   25.258  27.300  1.00 11.48 ?  314 CYS A N     1 
ATOM   2525 C  CA    . CYS A 1 315 ? 6.916   25.464  25.890  1.00 8.98  ?  314 CYS A CA    1 
ATOM   2526 C  C     . CYS A 1 315 ? 8.080   25.031  25.014  1.00 10.15 ?  314 CYS A C     1 
ATOM   2527 O  O     . CYS A 1 315 ? 7.875   24.534  23.906  1.00 9.68  ?  314 CYS A O     1 
ATOM   2528 C  CB    . CYS A 1 315 ? 6.592   26.928  25.632  1.00 9.06  ?  314 CYS A CB    1 
ATOM   2529 S  SG    . CYS A 1 315 ? 4.936   27.354  26.340  1.00 12.51 ?  314 CYS A SG    1 
ATOM   2530 N  N     . LYS A 1 316 ? 9.310   25.313  25.441  1.00 10.82 ?  315 LYS A N     1 
ATOM   2531 C  CA    . LYS A 1 316 ? 10.471  24.855  24.687  1.00 10.62 ?  315 LYS A CA    1 
ATOM   2532 C  C     . LYS A 1 316 ? 10.440  23.341  24.531  1.00 9.07  ?  315 LYS A C     1 
ATOM   2533 O  O     . LYS A 1 316 ? 10.680  22.820  23.418  1.00 10.05 ?  315 LYS A O     1 
ATOM   2534 C  CB    . LYS A 1 316 ? 11.748  25.299  25.421  1.00 14.20 ?  315 LYS A CB    1 
ATOM   2535 C  CG    . LYS A 1 316 ? 13.015  24.954  24.619  1.00 22.25 ?  315 LYS A CG    1 
ATOM   2536 C  CD    . LYS A 1 316 ? 12.968  25.686  23.271  1.00 28.58 ?  315 LYS A CD    1 
ATOM   2537 C  CE    . LYS A 1 316 ? 14.328  25.755  22.561  1.00 36.55 ?  315 LYS A CE    1 
ATOM   2538 N  NZ    . LYS A 1 316 ? 14.782  24.459  21.992  1.00 35.88 1  315 LYS A NZ    1 
ATOM   2539 N  N     . ALA A 1 317 ? 10.131  22.622  25.610  1.00 10.51 ?  316 ALA A N     1 
ATOM   2540 C  CA    . ALA A 1 317 ? 10.078  21.158  25.504  1.00 9.72  ?  316 ALA A CA    1 
ATOM   2541 C  C     . ALA A 1 317 ? 9.055   20.736  24.449  1.00 9.82  ?  316 ALA A C     1 
ATOM   2542 O  O     . ALA A 1 317 ? 9.268   19.782  23.686  1.00 13.47 ?  316 ALA A O     1 
ATOM   2543 C  CB    . ALA A 1 317 ? 9.744   20.527  26.860  1.00 12.80 ?  316 ALA A CB    1 
ATOM   2544 N  N     . LEU A 1 318 ? 7.935   21.440  24.379  1.00 8.66  ?  317 LEU A N     1 
ATOM   2545 C  CA    . LEU A 1 318 ? 6.935   21.072  23.375  1.00 8.24  ?  317 LEU A CA    1 
ATOM   2546 C  C     . LEU A 1 318 ? 7.378   21.444  21.959  1.00 7.26  ?  317 LEU A C     1 
ATOM   2547 O  O     . LEU A 1 318 ? 7.141   20.685  21.012  1.00 6.34  ?  317 LEU A O     1 
ATOM   2548 C  CB    . LEU A 1 318 ? 5.616   21.742  23.766  1.00 8.65  ?  317 LEU A CB    1 
ATOM   2549 C  CG    . LEU A 1 318 ? 5.048   21.178  25.059  1.00 10.86 ?  317 LEU A CG    1 
ATOM   2550 C  CD1   . LEU A 1 318 ? 3.892   22.046  25.660  1.00 11.40 ?  317 LEU A CD1   1 
ATOM   2551 C  CD2   . LEU A 1 318 ? 4.605   19.682  24.927  1.00 9.23  ?  317 LEU A CD2   1 
ATOM   2552 N  N     . ALA A 1 319 ? 7.971   22.645  21.782  1.00 7.50  ?  318 ALA A N     1 
ATOM   2553 C  CA    . ALA A 1 319 ? 8.406   23.094  20.470  1.00 8.79  ?  318 ALA A CA    1 
ATOM   2554 C  C     . ALA A 1 319 ? 9.508   22.222  19.894  1.00 7.49  ?  318 ALA A C     1 
ATOM   2555 O  O     . ALA A 1 319 ? 9.619   22.132  18.660  1.00 8.26  ?  318 ALA A O     1 
ATOM   2556 C  CB    . ALA A 1 319 ? 8.853   24.560  20.554  1.00 9.58  ?  318 ALA A CB    1 
ATOM   2557 N  N     . ASP A 1 320 ? 10.244  21.515  20.742  1.00 7.17  ?  319 ASP A N     1 
ATOM   2558 C  CA    . ASP A 1 320 ? 11.238  20.585  20.216  1.00 8.40  ?  319 ASP A CA    1 
ATOM   2559 C  C     . ASP A 1 320 ? 10.602  19.471  19.380  1.00 7.69  ?  319 ASP A C     1 
ATOM   2560 O  O     . ASP A 1 320 ? 11.294  18.847  18.543  1.00 7.28  ?  319 ASP A O     1 
ATOM   2561 C  CB    . ASP A 1 320 ? 12.049  19.981  21.360  1.00 8.28  ?  319 ASP A CB    1 
ATOM   2562 C  CG    . ASP A 1 320 ? 12.988  20.971  21.979  1.00 12.00 ?  319 ASP A CG    1 
ATOM   2563 O  OD1   . ASP A 1 320 ? 13.266  22.000  21.340  1.00 11.97 ?  319 ASP A OD1   1 
ATOM   2564 O  OD2   . ASP A 1 320 ? 13.422  20.724  23.084  1.00 13.36 -1 319 ASP A OD2   1 
ATOM   2565 N  N     . HIS A 1 321 ? 9.299   19.200  19.587  1.00 6.97  ?  320 HIS A N     1 
ATOM   2566 C  CA    . HIS A 1 321 ? 8.583   18.155  18.849  1.00 6.18  ?  320 HIS A CA    1 
ATOM   2567 C  C     . HIS A 1 321 ? 7.503   18.679  17.947  1.00 5.24  ?  320 HIS A C     1 
ATOM   2568 O  O     . HIS A 1 321 ? 7.216   18.036  16.931  1.00 7.08  ?  320 HIS A O     1 
ATOM   2569 C  CB    . HIS A 1 321 ? 7.961   17.143  19.838  1.00 6.90  ?  320 HIS A CB    1 
ATOM   2570 C  CG    . HIS A 1 321 ? 8.986   16.539  20.698  1.00 7.30  ?  320 HIS A CG    1 
ATOM   2571 N  ND1   . HIS A 1 321 ? 9.634   15.380  20.352  1.00 7.09  ?  320 HIS A ND1   1 
ATOM   2572 C  CD2   . HIS A 1 321 ? 9.602   17.001  21.806  1.00 7.67  ?  320 HIS A CD2   1 
ATOM   2573 C  CE1   . HIS A 1 321 ? 10.547  15.104  21.257  1.00 8.78  ?  320 HIS A CE1   1 
ATOM   2574 N  NE2   . HIS A 1 321 ? 10.587  16.096  22.124  1.00 7.16  ?  320 HIS A NE2   1 
ATOM   2575 N  N     . PHE A 1 322 ? 6.925   19.857  18.253  1.00 4.62  ?  321 PHE A N     1 
ATOM   2576 C  CA    . PHE A 1 322 ? 5.872   20.444  17.429  1.00 6.43  ?  321 PHE A CA    1 
ATOM   2577 C  C     . PHE A 1 322 ? 6.368   21.517  16.467  1.00 6.81  ?  321 PHE A C     1 
ATOM   2578 O  O     . PHE A 1 322 ? 5.595   21.923  15.602  1.00 6.45  ?  321 PHE A O     1 
ATOM   2579 C  CB    . PHE A 1 322 ? 4.739   21.003  18.334  1.00 6.20  ?  321 PHE A CB    1 
ATOM   2580 C  CG    . PHE A 1 322 ? 3.935   19.903  19.022  1.00 5.33  ?  321 PHE A CG    1 
ATOM   2581 C  CD1   . PHE A 1 322 ? 3.149   19.073  18.253  1.00 6.37  ?  321 PHE A CD1   1 
ATOM   2582 C  CD2   . PHE A 1 322 ? 3.986   19.726  20.391  1.00 8.74  ?  321 PHE A CD2   1 
ATOM   2583 C  CE1   . PHE A 1 322 ? 2.418   18.033  18.846  1.00 5.98  ?  321 PHE A CE1   1 
ATOM   2584 C  CE2   . PHE A 1 322 ? 3.264   18.709  21.009  1.00 8.91  ?  321 PHE A CE2   1 
ATOM   2585 C  CZ    . PHE A 1 322 ? 2.466   17.846  20.232  1.00 7.40  ?  321 PHE A CZ    1 
ATOM   2586 N  N     . GLY A 1 323 ? 7.634   21.977  16.596  1.00 7.39  ?  322 GLY A N     1 
ATOM   2587 C  CA    . GLY A 1 323 ? 8.231   22.874  15.622  1.00 7.60  ?  322 GLY A CA    1 
ATOM   2588 C  C     . GLY A 1 323 ? 8.094   24.335  16.003  1.00 8.96  ?  322 GLY A C     1 
ATOM   2589 O  O     . GLY A 1 323 ? 7.646   24.687  17.095  1.00 8.43  ?  322 GLY A O     1 
ATOM   2590 N  N     . SER A 1 324 ? 8.573   25.174  15.090  1.00 13.20 ?  323 SER A N     1 
ATOM   2591 C  CA    . SER A 1 324 ? 8.814   26.578  15.410  1.00 15.72 ?  323 SER A CA    1 
ATOM   2592 C  C     . SER A 1 324 ? 7.552   27.419  15.378  1.00 13.38 ?  323 SER A C     1 
ATOM   2593 O  O     . SER A 1 324 ? 7.616   28.590  15.808  1.00 13.35 ?  323 SER A O     1 
ATOM   2594 C  CB    . SER A 1 324 ? 9.876   27.168  14.480  1.00 19.67 ?  323 SER A CB    1 
ATOM   2595 O  OG    . SER A 1 324 ? 9.533   26.924  13.146  1.00 25.52 ?  323 SER A OG    1 
ATOM   2596 N  N     . GLU A 1 325 ? 6.406   26.848  15.015  1.00 9.99  ?  324 GLU A N     1 
ATOM   2597 C  CA    . GLU A 1 325 ? 5.166   27.588  15.296  1.00 10.01 ?  324 GLU A CA    1 
ATOM   2598 C  C     . GLU A 1 325 ? 4.557   27.289  16.662  1.00 9.60  ?  324 GLU A C     1 
ATOM   2599 O  O     . GLU A 1 325 ? 3.533   27.889  17.015  1.00 9.01  ?  324 GLU A O     1 
ATOM   2600 C  CB    . GLU A 1 325 ? 4.149   27.348  14.194  1.00 7.19  ?  324 GLU A CB    1 
ATOM   2601 C  CG    . GLU A 1 325 ? 4.692   27.857  12.885  1.00 9.12  ?  324 GLU A CG    1 
ATOM   2602 C  CD    . GLU A 1 325 ? 3.626   27.990  11.829  1.00 12.22 ?  324 GLU A CD    1 
ATOM   2603 O  OE1   . GLU A 1 325 ? 2.677   27.189  11.819  1.00 10.87 ?  324 GLU A OE1   1 
ATOM   2604 O  OE2   . GLU A 1 325 ? 3.740   28.928  11.012  1.00 11.29 -1 324 GLU A OE2   1 
ATOM   2605 N  N     . PHE A 1 326 ? 5.132   26.399  17.461  1.00 8.60  ?  325 PHE A N     1 
ATOM   2606 C  CA    . PHE A 1 326 ? 4.644   26.260  18.826  1.00 8.31  ?  325 PHE A CA    1 
ATOM   2607 C  C     . PHE A 1 326 ? 5.131   27.460  19.610  1.00 8.23  ?  325 PHE A C     1 
ATOM   2608 O  O     . PHE A 1 326 ? 6.329   27.724  19.615  1.00 11.65 ?  325 PHE A O     1 
ATOM   2609 C  CB    . PHE A 1 326 ? 5.116   24.953  19.514  1.00 8.01  ?  325 PHE A CB    1 
ATOM   2610 C  CG    . PHE A 1 326 ? 4.344   24.678  20.743  1.00 8.12  ?  325 PHE A CG    1 
ATOM   2611 C  CD1   . PHE A 1 326 ? 4.648   25.336  21.932  1.00 9.45  ?  325 PHE A CD1   1 
ATOM   2612 C  CD2   . PHE A 1 326 ? 3.190   23.916  20.669  1.00 8.91  ?  325 PHE A CD2   1 
ATOM   2613 C  CE1   . PHE A 1 326 ? 3.876   25.130  23.112  1.00 11.01 ?  325 PHE A CE1   1 
ATOM   2614 C  CE2   . PHE A 1 326 ? 2.407   23.713  21.794  1.00 9.59  ?  325 PHE A CE2   1 
ATOM   2615 C  CZ    . PHE A 1 326 ? 2.736   24.331  23.042  1.00 11.38 ?  325 PHE A CZ    1 
ATOM   2616 N  N     . PRO A 1 327 ? 4.260   28.234  20.244  1.00 9.28  ?  326 PRO A N     1 
ATOM   2617 C  CA    . PRO A 1 327 ? 4.733   29.494  20.841  1.00 10.22 ?  326 PRO A CA    1 
ATOM   2618 C  C     . PRO A 1 327 ? 5.605   29.244  22.067  1.00 11.59 ?  326 PRO A C     1 
ATOM   2619 O  O     . PRO A 1 327 ? 5.286   28.423  22.929  1.00 12.18 ?  326 PRO A O     1 
ATOM   2620 C  CB    . PRO A 1 327 ? 3.427   30.233  21.187  1.00 12.54 ?  326 PRO A CB    1 
ATOM   2621 C  CG    . PRO A 1 327 ? 2.339   29.182  21.241  1.00 12.23 ?  326 PRO A CG    1 
ATOM   2622 C  CD    . PRO A 1 327 ? 2.797   28.069  20.304  1.00 9.28  ?  326 PRO A CD    1 
ATOM   2623 N  N     . VAL A 1 328 ? 6.746   29.924  22.129  1.00 12.82 ?  327 VAL A N     1 
ATOM   2624 C  CA    . VAL A 1 328 ? 7.645   29.825  23.269  1.00 12.41 ?  327 VAL A CA    1 
ATOM   2625 C  C     . VAL A 1 328 ? 7.877   31.228  23.808  1.00 17.50 ?  327 VAL A C     1 
ATOM   2626 O  O     . VAL A 1 328 ? 8.670   31.989  23.258  1.00 18.64 ?  327 VAL A O     1 
ATOM   2627 C  CB    . VAL A 1 328 ? 8.982   29.163  22.883  1.00 16.11 ?  327 VAL A CB    1 
ATOM   2628 C  CG1   . VAL A 1 328 ? 9.827   29.012  24.110  1.00 15.60 ?  327 VAL A CG1   1 
ATOM   2629 C  CG2   . VAL A 1 328 ? 8.749   27.772  22.250  1.00 17.59 ?  327 VAL A CG2   1 
ATOM   2630 N  N     . PRO A 1 329 ? 7.208   31.590  24.894  1.00 20.48 ?  328 PRO A N     1 
ATOM   2631 C  CA    . PRO A 1 329 ? 7.412   32.919  25.490  1.00 21.27 ?  328 PRO A CA    1 
ATOM   2632 C  C     . PRO A 1 329 ? 8.855   33.101  25.917  1.00 25.99 ?  328 PRO A C     1 
ATOM   2633 O  O     . PRO A 1 329 ? 9.536   32.144  26.299  1.00 24.11 ?  328 PRO A O     1 
ATOM   2634 C  CB    . PRO A 1 329 ? 6.493   32.902  26.711  1.00 20.63 ?  328 PRO A CB    1 
ATOM   2635 C  CG    . PRO A 1 329 ? 5.470   31.827  26.418  1.00 22.91 ?  328 PRO A CG    1 
ATOM   2636 C  CD    . PRO A 1 329 ? 6.295   30.765  25.699  1.00 19.92 ?  328 PRO A CD    1 
ATOM   2637 N  N     . GLU A 1 330 ? 9.308   34.354  25.869  1.00 32.71 ?  329 GLU A N     1 
ATOM   2638 C  CA    . GLU A 1 330 ? 10.611  34.703  26.420  1.00 40.03 ?  329 GLU A CA    1 
ATOM   2639 C  C     . GLU A 1 330 ? 10.640  34.497  27.929  1.00 40.33 ?  329 GLU A C     1 
ATOM   2640 O  O     . GLU A 1 330 ? 9.621   34.591  28.616  1.00 39.14 ?  329 GLU A O     1 
ATOM   2641 C  CB    . GLU A 1 330 ? 10.960  36.155  26.102  1.00 47.81 ?  329 GLU A CB    1 
ATOM   2642 C  CG    . GLU A 1 330 ? 10.797  36.524  24.646  1.00 55.25 ?  329 GLU A CG    1 
ATOM   2643 C  CD    . GLU A 1 330 ? 11.679  35.697  23.743  1.00 61.98 ?  329 GLU A CD    1 
ATOM   2644 O  OE1   . GLU A 1 330 ? 12.749  35.245  24.213  1.00 64.30 ?  329 GLU A OE1   1 
ATOM   2645 O  OE2   . GLU A 1 330 ? 11.300  35.494  22.564  1.00 65.50 -1 329 GLU A OE2   1 
ATOM   2646 N  N     . LYS A 1 331 ? 11.832  34.218  28.437  1.00 43.57 ?  330 LYS A N     1 
ATOM   2647 C  CA    . LYS A 1 331 ? 12.068  34.112  29.873  1.00 46.71 ?  330 LYS A CA    1 
ATOM   2648 C  C     . LYS A 1 331 ? 12.152  35.498  30.523  1.00 45.64 ?  330 LYS A C     1 
ATOM   2649 O  O     . LYS A 1 331 ? 11.314  35.874  31.353  1.00 45.10 ?  330 LYS A O     1 
ATOM   2650 C  CB    . LYS A 1 331 ? 13.356  33.330  30.132  1.00 50.86 ?  330 LYS A CB    1 
ATOM   2651 C  CG    . LYS A 1 331 ? 13.475  32.780  31.540  1.00 55.09 ?  330 LYS A CG    1 
ATOM   2652 C  CD    . LYS A 1 331 ? 12.911  31.371  31.624  1.00 58.57 ?  330 LYS A CD    1 
ATOM   2653 C  CE    . LYS A 1 331 ? 14.017  30.326  31.634  1.00 61.13 ?  330 LYS A CE    1 
ATOM   2654 N  NZ    . LYS A 1 331 ? 14.938  30.518  32.792  1.00 62.02 1  330 LYS A NZ    1 
HETATM 2655 P  PG    . ATP B 2 .   ? -4.066  14.421  5.803   1.00 11.32 ?  401 ATP A PG    1 
HETATM 2656 O  O1G   . ATP B 2 .   ? -2.806  13.808  6.283   1.00 14.77 ?  401 ATP A O1G   1 
HETATM 2657 O  O2G   . ATP B 2 .   ? -4.168  14.450  4.300   1.00 11.38 -1 401 ATP A O2G   1 
HETATM 2658 O  O3G   . ATP B 2 .   ? -4.452  15.701  6.478   1.00 9.97  ?  401 ATP A O3G   1 
HETATM 2659 P  PB    . ATP B 2 .   ? -6.303  12.731  5.386   1.00 10.61 ?  401 ATP A PB    1 
HETATM 2660 O  O1B   . ATP B 2 .   ? -7.392  12.104  6.225   1.00 10.85 -1 401 ATP A O1B   1 
HETATM 2661 O  O2B   . ATP B 2 .   ? -6.769  13.711  4.353   1.00 9.36  ?  401 ATP A O2B   1 
HETATM 2662 O  O3B   . ATP B 2 .   ? -5.160  13.326  6.319   1.00 10.64 ?  401 ATP A O3B   1 
HETATM 2663 P  PA    . ATP B 2 .   ? -5.152  11.193  3.114   1.00 11.80 ?  401 ATP A PA    1 
HETATM 2664 O  O1A   . ATP B 2 .   ? -3.926  10.318  3.156   1.00 12.06 -1 401 ATP A O1A   1 
HETATM 2665 O  O2A   . ATP B 2 .   ? -5.123  12.460  2.340   1.00 10.53 ?  401 ATP A O2A   1 
HETATM 2666 O  O3A   . ATP B 2 .   ? -5.611  11.473  4.653   1.00 11.73 ?  401 ATP A O3A   1 
HETATM 2667 O  "O5'" . ATP B 2 .   ? -6.336  10.271  2.521   1.00 11.76 ?  401 ATP A "O5'" 1 
HETATM 2668 C  "C5'" . ATP B 2 .   ? -7.593  10.829  2.136   1.00 9.96  ?  401 ATP A "C5'" 1 
HETATM 2669 C  "C4'" . ATP B 2 .   ? -8.696  9.879   2.637   1.00 10.94 ?  401 ATP A "C4'" 1 
HETATM 2670 O  "O4'" . ATP B 2 .   ? -8.500  8.637   1.955   1.00 12.06 ?  401 ATP A "O4'" 1 
HETATM 2671 C  "C3'" . ATP B 2 .   ? -8.629  9.481   4.097   1.00 10.78 ?  401 ATP A "C3'" 1 
HETATM 2672 O  "O3'" . ATP B 2 .   ? -9.298  10.408  4.975   1.00 11.42 ?  401 ATP A "O3'" 1 
HETATM 2673 C  "C2'" . ATP B 2 .   ? -9.344  8.138   4.114   1.00 11.28 ?  401 ATP A "C2'" 1 
HETATM 2674 O  "O2'" . ATP B 2 .   ? -10.766 8.330   3.993   1.00 13.74 ?  401 ATP A "O2'" 1 
HETATM 2675 C  "C1'" . ATP B 2 .   ? -8.835  7.537   2.812   1.00 10.97 ?  401 ATP A "C1'" 1 
HETATM 2676 N  N9    . ATP B 2 .   ? -7.621  6.761   3.052   1.00 12.43 ?  401 ATP A N9    1 
HETATM 2677 C  C8    . ATP B 2 .   ? -6.348  7.175   2.827   1.00 14.21 ?  401 ATP A C8    1 
HETATM 2678 N  N7    . ATP B 2 .   ? -5.460  6.210   3.111   1.00 15.26 ?  401 ATP A N7    1 
HETATM 2679 C  C5    . ATP B 2 .   ? -6.147  5.142   3.513   1.00 15.03 ?  401 ATP A C5    1 
HETATM 2680 C  C6    . ATP B 2 .   ? -5.785  3.788   3.957   1.00 17.48 ?  401 ATP A C6    1 
HETATM 2681 N  N6    . ATP B 2 .   ? -4.499  3.363   4.027   1.00 19.34 ?  401 ATP A N6    1 
HETATM 2682 N  N1    . ATP B 2 .   ? -6.817  2.995   4.258   1.00 17.47 ?  401 ATP A N1    1 
HETATM 2683 C  C2    . ATP B 2 .   ? -8.102  3.395   4.167   1.00 17.06 ?  401 ATP A C2    1 
HETATM 2684 N  N3    . ATP B 2 .   ? -8.503  4.610   3.790   1.00 15.68 ?  401 ATP A N3    1 
HETATM 2685 C  C4    . ATP B 2 .   ? -7.566  5.501   3.453   1.00 12.26 ?  401 ATP A C4    1 
HETATM 2686 P  PG    . ATP C 2 .   ? 2.518   2.368   -3.129  1.00 74.70 ?  402 ATP A PG    1 
HETATM 2687 O  O1G   . ATP C 2 .   ? 3.154   3.344   -2.159  1.00 75.10 ?  402 ATP A O1G   1 
HETATM 2688 O  O2G   . ATP C 2 .   ? 1.758   1.252   -2.447  1.00 75.07 -1 402 ATP A O2G   1 
HETATM 2689 O  O3G   . ATP C 2 .   ? 3.412   1.895   -4.254  1.00 75.14 ?  402 ATP A O3G   1 
HETATM 2690 P  PB    . ATP C 2 .   ? 1.236   4.804   -3.822  1.00 67.00 ?  402 ATP A PB    1 
HETATM 2691 O  O1B   . ATP C 2 .   ? 2.603   5.445   -3.769  1.00 67.80 -1 402 ATP A O1B   1 
HETATM 2692 O  O2B   . ATP C 2 .   ? 0.284   5.245   -4.902  1.00 67.59 ?  402 ATP A O2B   1 
HETATM 2693 O  O3B   . ATP C 2 .   ? 1.341   3.202   -3.848  1.00 71.52 ?  402 ATP A O3B   1 
HETATM 2694 P  PA    . ATP C 2 .   ? -0.944  4.549   -1.960  1.00 62.61 ?  402 ATP A PA    1 
HETATM 2695 O  O1A   . ATP C 2 .   ? -0.981  4.481   -0.452  1.00 63.06 -1 402 ATP A O1A   1 
HETATM 2696 O  O2A   . ATP C 2 .   ? -1.398  3.344   -2.727  1.00 62.76 ?  402 ATP A O2A   1 
HETATM 2697 O  O3A   . ATP C 2 .   ? 0.549   5.017   -2.379  1.00 65.92 ?  402 ATP A O3A   1 
HETATM 2698 O  "O5'" . ATP C 2 .   ? -1.800  5.813   -2.457  1.00 57.53 ?  402 ATP A "O5'" 1 
HETATM 2699 C  "C5'" . ATP C 2 .   ? -1.196  7.103   -2.383  1.00 52.44 ?  402 ATP A "C5'" 1 
HETATM 2700 C  "C4'" . ATP C 2 .   ? -2.181  8.136   -1.850  1.00 47.10 ?  402 ATP A "C4'" 1 
HETATM 2701 O  "O4'" . ATP C 2 .   ? -3.504  7.592   -1.917  1.00 42.15 ?  402 ATP A "O4'" 1 
HETATM 2702 C  "C3'" . ATP C 2 .   ? -1.867  8.461   -0.386  1.00 45.72 ?  402 ATP A "C3'" 1 
HETATM 2703 O  "O3'" . ATP C 2 .   ? -2.118  9.848   -0.126  1.00 47.62 ?  402 ATP A "O3'" 1 
HETATM 2704 C  "C2'" . ATP C 2 .   ? -2.881  7.669   0.398   1.00 42.37 ?  402 ATP A "C2'" 1 
HETATM 2705 O  "O2'" . ATP C 2 .   ? -3.242  8.321   1.624   1.00 41.65 ?  402 ATP A "O2'" 1 
HETATM 2706 C  "C1'" . ATP C 2 .   ? -4.045  7.566   -0.590  1.00 39.06 ?  402 ATP A "C1'" 1 
HETATM 2707 N  N9    . ATP C 2 .   ? -4.848  6.360   -0.272  1.00 30.31 ?  402 ATP A N9    1 
HETATM 2708 C  C8    . ATP C 2 .   ? -4.407  5.169   0.178   1.00 25.62 ?  402 ATP A C8    1 
HETATM 2709 N  N7    . ATP C 2 .   ? -5.434  4.318   0.392   1.00 27.84 ?  402 ATP A N7    1 
HETATM 2710 C  C5    . ATP C 2 .   ? -6.558  4.974   0.081   1.00 24.05 ?  402 ATP A C5    1 
HETATM 2711 C  C6    . ATP C 2 .   ? -7.985  4.661   0.087   1.00 21.49 ?  402 ATP A C6    1 
HETATM 2712 N  N6    . ATP C 2 .   ? -8.421  3.438   0.474   1.00 21.66 ?  402 ATP A N6    1 
HETATM 2713 N  N1    . ATP C 2 .   ? -8.810  5.649   -0.278  1.00 21.83 ?  402 ATP A N1    1 
HETATM 2714 C  C2    . ATP C 2 .   ? -8.405  6.870   -0.674  1.00 22.66 ?  402 ATP A C2    1 
HETATM 2715 N  N3    . ATP C 2 .   ? -7.110  7.211   -0.718  1.00 21.94 ?  402 ATP A N3    1 
HETATM 2716 C  C4    . ATP C 2 .   ? -6.169  6.326   -0.343  1.00 25.87 ?  402 ATP A C4    1 
HETATM 2717 MG MG    . MG  D 3 .   ? -5.584  14.461  2.894   1.00 9.60  ?  403 MG  A MG    1 
HETATM 2718 MG MG    . MG  E 3 .   ? -4.525  12.972  0.114   1.00 14.97 ?  404 MG  A MG    1 
HETATM 2719 O  O     . HOH F 4 .   ? 17.912  -16.685 12.329  1.00 31.93 ?  501 HOH A O     1 
HETATM 2720 O  O     . HOH F 4 .   ? -24.078 25.626  34.610  1.00 21.52 ?  502 HOH A O     1 
HETATM 2721 O  O     . HOH F 4 .   ? 2.322   7.629   30.141  1.00 40.93 ?  503 HOH A O     1 
HETATM 2722 O  O     . HOH F 4 .   ? -20.290 3.827   10.406  1.00 27.08 ?  504 HOH A O     1 
HETATM 2723 O  O     . HOH F 4 .   ? -20.153 19.952  2.754   1.00 46.31 ?  505 HOH A O     1 
HETATM 2724 O  O     . HOH F 4 .   ? -3.430  18.653  3.604   1.00 24.45 ?  506 HOH A O     1 
HETATM 2725 O  O     . HOH F 4 .   ? -7.075  23.332  -9.000  1.00 26.26 ?  507 HOH A O     1 
HETATM 2726 O  O     . HOH F 4 .   ? -6.245  -6.245  12.501  1.00 38.82 ?  508 HOH A O     1 
HETATM 2727 O  O     . HOH F 4 .   ? -1.805  16.865  6.365   1.00 30.29 ?  509 HOH A O     1 
HETATM 2728 O  O     . HOH F 4 .   ? -21.594 14.210  22.747  1.00 26.68 ?  510 HOH A O     1 
HETATM 2729 O  O     . HOH F 4 .   ? 9.738   23.793  5.904   1.00 30.14 ?  511 HOH A O     1 
HETATM 2730 O  O     . HOH F 4 .   ? -0.904  7.836   30.925  1.00 38.91 ?  512 HOH A O     1 
HETATM 2731 O  O     . HOH F 4 .   ? 13.953  8.319   17.807  1.00 18.86 ?  513 HOH A O     1 
HETATM 2732 O  O     . HOH F 4 .   ? 8.942   31.848  31.212  1.00 24.71 ?  514 HOH A O     1 
HETATM 2733 O  O     . HOH F 4 .   ? -17.884 14.385  5.479   1.00 34.35 ?  515 HOH A O     1 
HETATM 2734 O  O     . HOH F 4 .   ? 5.046   28.923  37.177  1.00 25.46 ?  516 HOH A O     1 
HETATM 2735 O  O     . HOH F 4 .   ? -19.017 22.881  -2.841  1.00 35.84 ?  517 HOH A O     1 
HETATM 2736 O  O     . HOH F 4 .   ? -5.978  18.292  33.814  1.00 24.84 ?  518 HOH A O     1 
HETATM 2737 O  O     . HOH F 4 .   ? 5.784   26.634  0.698   1.00 43.78 ?  519 HOH A O     1 
HETATM 2738 O  O     . HOH F 4 .   ? -10.477 8.629   -32.628 1.00 40.35 ?  520 HOH A O     1 
HETATM 2739 O  O     . HOH F 4 .   ? 4.024   23.038  -5.264  1.00 38.82 ?  521 HOH A O     1 
HETATM 2740 O  O     . HOH F 4 .   ? -15.494 7.248   22.142  1.00 36.86 ?  522 HOH A O     1 
HETATM 2741 O  O     . HOH F 4 .   ? -13.098 3.122   -23.436 1.00 31.37 ?  523 HOH A O     1 
HETATM 2742 O  O     . HOH F 4 .   ? -5.155  31.601  7.537   1.00 34.10 ?  524 HOH A O     1 
HETATM 2743 O  O     . HOH F 4 .   ? 8.670   -10.928 18.150  1.00 20.84 ?  525 HOH A O     1 
HETATM 2744 O  O     . HOH F 4 .   ? 1.514   20.789  9.232   1.00 11.58 ?  526 HOH A O     1 
HETATM 2745 O  O     . HOH F 4 .   ? -7.037  12.521  31.516  1.00 29.84 ?  527 HOH A O     1 
HETATM 2746 O  O     . HOH F 4 .   ? -18.372 16.568  15.003  1.00 22.16 ?  528 HOH A O     1 
HETATM 2747 O  O     . HOH F 4 .   ? 0.217   11.642  6.122   1.00 19.34 ?  529 HOH A O     1 
HETATM 2748 O  O     . HOH F 4 .   ? -6.931  9.700   -1.398  1.00 24.76 ?  530 HOH A O     1 
HETATM 2749 O  O     . HOH F 4 .   ? -2.587  10.290  5.374   1.00 27.07 ?  531 HOH A O     1 
HETATM 2750 O  O     . HOH F 4 .   ? -9.920  21.499  8.636   1.00 19.78 ?  532 HOH A O     1 
HETATM 2751 O  O     . HOH F 4 .   ? -16.213 1.324   15.894  1.00 19.85 ?  533 HOH A O     1 
HETATM 2752 O  O     . HOH F 4 .   ? -24.751 8.086   10.848  1.00 18.33 ?  534 HOH A O     1 
HETATM 2753 O  O     . HOH F 4 .   ? 0.993   -1.932  10.925  1.00 12.39 ?  535 HOH A O     1 
HETATM 2754 O  O     . HOH F 4 .   ? 5.631   -10.814 19.928  1.00 25.25 ?  536 HOH A O     1 
HETATM 2755 O  O     . HOH F 4 .   ? -4.467  18.302  6.325   1.00 15.33 ?  537 HOH A O     1 
HETATM 2756 O  O     . HOH F 4 .   ? -6.223  23.397  31.185  1.00 23.75 ?  538 HOH A O     1 
HETATM 2757 O  O     . HOH F 4 .   ? -1.931  18.999  33.025  1.00 26.40 ?  539 HOH A O     1 
HETATM 2758 O  O     . HOH F 4 .   ? -1.040  -5.140  8.969   1.00 23.96 ?  540 HOH A O     1 
HETATM 2759 O  O     . HOH F 4 .   ? 17.034  -1.534  14.468  1.00 16.64 ?  541 HOH A O     1 
HETATM 2760 O  O     . HOH F 4 .   ? -0.835  14.379  32.675  1.00 19.32 ?  542 HOH A O     1 
HETATM 2761 O  O     . HOH F 4 .   ? -4.349  33.742  17.717  1.00 33.31 ?  543 HOH A O     1 
HETATM 2762 O  O     . HOH F 4 .   ? 5.062   -0.378  23.487  1.00 30.97 ?  544 HOH A O     1 
HETATM 2763 O  O     . HOH F 4 .   ? -22.388 11.941  -1.554  1.00 50.31 ?  545 HOH A O     1 
HETATM 2764 O  O     . HOH F 4 .   ? -12.647 26.212  39.079  1.00 33.66 ?  546 HOH A O     1 
HETATM 2765 O  O     . HOH F 4 .   ? -17.132 13.665  -26.286 1.00 28.09 ?  547 HOH A O     1 
HETATM 2766 O  O     . HOH F 4 .   ? -19.462 1.074   1.215   1.00 25.89 ?  548 HOH A O     1 
HETATM 2767 O  O     . HOH F 4 .   ? 0.076   29.113  29.703  1.00 25.91 ?  549 HOH A O     1 
HETATM 2768 O  O     . HOH F 4 .   ? -2.872  -0.590  -19.079 1.00 44.56 ?  550 HOH A O     1 
HETATM 2769 O  O     . HOH F 4 .   ? -4.466  28.880  10.667  1.00 13.07 ?  551 HOH A O     1 
HETATM 2770 O  O     . HOH F 4 .   ? -16.179 26.622  -5.526  1.00 31.60 ?  552 HOH A O     1 
HETATM 2771 O  O     . HOH F 4 .   ? 5.751   5.914   29.093  1.00 34.98 ?  553 HOH A O     1 
HETATM 2772 O  O     . HOH F 4 .   ? 13.873  19.303  18.070  1.00 13.38 ?  554 HOH A O     1 
HETATM 2773 O  O     . HOH F 4 .   ? -8.916  0.991   2.537   1.00 32.94 ?  555 HOH A O     1 
HETATM 2774 O  O     . HOH F 4 .   ? 15.653  21.941  23.876  1.00 20.53 ?  556 HOH A O     1 
HETATM 2775 O  O     . HOH F 4 .   ? -6.558  11.194  25.178  1.00 10.21 ?  557 HOH A O     1 
HETATM 2776 O  O     . HOH F 4 .   ? -3.335  -3.790  20.278  1.00 31.36 ?  558 HOH A O     1 
HETATM 2777 O  O     . HOH F 4 .   ? -0.504  10.345  32.994  1.00 39.64 ?  559 HOH A O     1 
HETATM 2778 O  O     . HOH F 4 .   ? -11.584 6.461   22.411  1.00 16.65 ?  560 HOH A O     1 
HETATM 2779 O  O     . HOH F 4 .   ? 12.895  -10.732 18.673  1.00 29.21 ?  561 HOH A O     1 
HETATM 2780 O  O     . HOH F 4 .   ? -1.098  -2.926  17.205  1.00 18.26 ?  562 HOH A O     1 
HETATM 2781 O  O     . HOH F 4 .   ? 4.770   -3.793  -14.640 1.00 48.79 ?  563 HOH A O     1 
HETATM 2782 O  O     . HOH F 4 .   ? -21.155 18.173  23.562  1.00 26.67 ?  564 HOH A O     1 
HETATM 2783 O  O     . HOH F 4 .   ? -4.361  25.512  -1.712  1.00 28.17 ?  565 HOH A O     1 
HETATM 2784 O  O     . HOH F 4 .   ? -3.391  0.776   3.989   1.00 33.28 ?  566 HOH A O     1 
HETATM 2785 O  O     . HOH F 4 .   ? 1.236   21.487  34.335  1.00 34.99 ?  567 HOH A O     1 
HETATM 2786 O  O     . HOH F 4 .   ? 12.434  1.041   5.668   1.00 19.83 ?  568 HOH A O     1 
HETATM 2787 O  O     . HOH F 4 .   ? -4.680  -2.140  17.309  1.00 43.18 ?  569 HOH A O     1 
HETATM 2788 O  O     . HOH F 4 .   ? 17.137  -11.762 15.669  1.00 41.51 ?  570 HOH A O     1 
HETATM 2789 O  O     . HOH F 4 .   ? -11.033 24.446  -14.853 1.00 27.21 ?  571 HOH A O     1 
HETATM 2790 O  O     . HOH F 4 .   ? 2.452   15.892  5.179   1.00 42.68 ?  572 HOH A O     1 
HETATM 2791 O  O     . HOH F 4 .   ? -18.752 3.420   -29.281 1.00 58.57 ?  573 HOH A O     1 
HETATM 2792 O  O     . HOH F 4 .   ? 5.059   22.847  33.163  1.00 24.08 ?  574 HOH A O     1 
HETATM 2793 O  O     . HOH F 4 .   ? 0.753   26.845  9.970   1.00 8.95  ?  575 HOH A O     1 
HETATM 2794 O  O     . HOH F 4 .   ? 1.050   19.147  5.701   1.00 21.46 ?  576 HOH A O     1 
HETATM 2795 O  O     . HOH F 4 .   ? -15.279 24.630  43.233  1.00 36.64 ?  577 HOH A O     1 
HETATM 2796 O  O     . HOH F 4 .   ? 1.825   -6.937  22.184  1.00 46.58 ?  578 HOH A O     1 
HETATM 2797 O  O     . HOH F 4 .   ? -6.188  16.385  3.106   1.00 10.13 ?  579 HOH A O     1 
HETATM 2798 O  O     . HOH F 4 .   ? -16.028 -0.385  13.487  1.00 18.19 ?  580 HOH A O     1 
HETATM 2799 O  O     . HOH F 4 .   ? 11.780  13.938  24.588  1.00 20.58 ?  581 HOH A O     1 
HETATM 2800 O  O     . HOH F 4 .   ? -6.623  30.629  21.062  1.00 25.48 ?  582 HOH A O     1 
HETATM 2801 O  O     . HOH F 4 .   ? 13.238  13.669  12.988  1.00 18.06 ?  583 HOH A O     1 
HETATM 2802 O  O     . HOH F 4 .   ? -18.689 0.511   -7.040  1.00 23.31 ?  584 HOH A O     1 
HETATM 2803 O  O     . HOH F 4 .   ? -11.173 1.591   21.393  1.00 35.88 ?  585 HOH A O     1 
HETATM 2804 O  O     . HOH F 4 .   ? -11.010 2.629   0.705   1.00 22.59 ?  586 HOH A O     1 
HETATM 2805 O  O     . HOH F 4 .   ? -21.518 3.021   6.566   1.00 20.62 ?  587 HOH A O     1 
HETATM 2806 O  O     . HOH F 4 .   ? -16.942 23.574  27.385  1.00 23.12 ?  588 HOH A O     1 
HETATM 2807 O  O     . HOH F 4 .   ? -15.203 16.658  33.777  1.00 30.57 ?  589 HOH A O     1 
HETATM 2808 O  O     . HOH F 4 .   ? -18.352 19.263  29.495  1.00 23.89 ?  590 HOH A O     1 
HETATM 2809 O  O     . HOH F 4 .   ? -15.092 15.455  11.843  1.00 12.18 ?  591 HOH A O     1 
HETATM 2810 O  O     . HOH F 4 .   ? 6.833   -15.774 10.311  1.00 15.67 ?  592 HOH A O     1 
HETATM 2811 O  O     . HOH F 4 .   ? 11.527  23.717  17.513  1.00 16.88 ?  593 HOH A O     1 
HETATM 2812 O  O     . HOH F 4 .   ? -18.776 18.783  32.203  1.00 45.33 ?  594 HOH A O     1 
HETATM 2813 O  O     . HOH F 4 .   ? 0.880   4.564   -12.446 1.00 30.11 ?  595 HOH A O     1 
HETATM 2814 O  O     . HOH F 4 .   ? 11.389  25.035  12.451  1.00 35.13 ?  596 HOH A O     1 
HETATM 2815 O  O     . HOH F 4 .   ? -15.852 13.933  9.630   1.00 12.93 ?  597 HOH A O     1 
HETATM 2816 O  O     . HOH F 4 .   ? -0.108  23.497  35.977  1.00 30.27 ?  598 HOH A O     1 
HETATM 2817 O  O     . HOH F 4 .   ? 6.512   30.224  17.713  1.00 17.63 ?  599 HOH A O     1 
HETATM 2818 O  O     . HOH F 4 .   ? 5.494   24.116  13.958  1.00 8.42  ?  600 HOH A O     1 
HETATM 2819 O  O     . HOH F 4 .   ? -4.974  11.174  -0.407  1.00 18.35 ?  601 HOH A O     1 
HETATM 2820 O  O     . HOH F 4 .   ? 13.002  8.120   21.847  1.00 19.48 ?  602 HOH A O     1 
HETATM 2821 O  O     . HOH F 4 .   ? -2.858  21.762  28.135  1.00 16.05 ?  603 HOH A O     1 
HETATM 2822 O  O     . HOH F 4 .   ? -1.732  13.806  3.206   1.00 19.87 ?  604 HOH A O     1 
HETATM 2823 O  O     . HOH F 4 .   ? -17.660 26.027  31.254  1.00 21.00 ?  605 HOH A O     1 
HETATM 2824 O  O     . HOH F 4 .   ? -10.668 30.769  1.128   1.00 43.06 ?  606 HOH A O     1 
HETATM 2825 O  O     . HOH F 4 .   ? -7.559  13.261  8.821   1.00 9.57  ?  607 HOH A O     1 
HETATM 2826 O  O     . HOH F 4 .   ? -21.941 12.704  9.526   1.00 29.11 ?  608 HOH A O     1 
HETATM 2827 O  O     . HOH F 4 .   ? -12.326 10.439  3.142   1.00 15.78 ?  609 HOH A O     1 
HETATM 2828 O  O     . HOH F 4 .   ? 2.800   -4.632  7.072   1.00 27.83 ?  610 HOH A O     1 
HETATM 2829 O  O     . HOH F 4 .   ? -19.944 22.581  7.774   1.00 39.94 ?  611 HOH A O     1 
HETATM 2830 O  O     . HOH F 4 .   ? -12.130 -2.285  12.410  1.00 19.30 ?  612 HOH A O     1 
HETATM 2831 O  O     . HOH F 4 .   ? -4.464  31.047  23.366  1.00 18.15 ?  613 HOH A O     1 
HETATM 2832 O  O     . HOH F 4 .   ? -0.496  1.829   4.971   1.00 27.38 ?  614 HOH A O     1 
HETATM 2833 O  O     . HOH F 4 .   ? 2.006   27.128  7.517   1.00 12.67 ?  615 HOH A O     1 
HETATM 2834 O  O     . HOH F 4 .   ? 0.487   -4.882  15.683  1.00 20.82 ?  616 HOH A O     1 
HETATM 2835 O  O     . HOH F 4 .   ? -6.221  8.428   25.196  1.00 12.55 ?  617 HOH A O     1 
HETATM 2836 O  O     . HOH F 4 .   ? 5.012   -6.661  21.978  1.00 24.82 ?  618 HOH A O     1 
HETATM 2837 O  O     . HOH F 4 .   ? -16.532 30.028  8.824   1.00 44.87 ?  619 HOH A O     1 
HETATM 2838 O  O     . HOH F 4 .   ? 3.917   25.586  1.705   1.00 41.39 ?  620 HOH A O     1 
HETATM 2839 O  O     . HOH F 4 .   ? 4.997   15.021  34.370  1.00 26.40 ?  621 HOH A O     1 
HETATM 2840 O  O     . HOH F 4 .   ? -12.606 24.504  9.491   1.00 13.50 ?  622 HOH A O     1 
HETATM 2841 O  O     . HOH F 4 .   ? 1.793   -6.680  14.356  1.00 21.71 ?  623 HOH A O     1 
HETATM 2842 O  O     . HOH F 4 .   ? 7.614   26.927  11.126  1.00 26.26 ?  624 HOH A O     1 
HETATM 2843 O  O     . HOH F 4 .   ? 8.727   3.148   23.888  1.00 20.25 ?  625 HOH A O     1 
HETATM 2844 O  O     . HOH F 4 .   ? -11.537 5.991   0.202   1.00 23.15 ?  626 HOH A O     1 
HETATM 2845 O  O     . HOH F 4 .   ? 4.906   33.163  19.647  1.00 21.96 ?  627 HOH A O     1 
HETATM 2846 O  O     . HOH F 4 .   ? -18.382 13.568  1.577   1.00 26.96 ?  628 HOH A O     1 
HETATM 2847 O  O     . HOH F 4 .   ? 10.473  -5.559  17.997  1.00 32.34 ?  629 HOH A O     1 
HETATM 2848 O  O     . HOH F 4 .   ? -1.328  19.873  4.944   1.00 28.45 ?  630 HOH A O     1 
HETATM 2849 O  O     . HOH F 4 .   ? -7.149  -1.741  15.073  1.00 25.02 ?  631 HOH A O     1 
HETATM 2850 O  O     . HOH F 4 .   ? 5.688   -12.135 15.816  1.00 14.21 ?  632 HOH A O     1 
HETATM 2851 O  O     . HOH F 4 .   ? 9.079   13.231  18.642  1.00 7.11  ?  633 HOH A O     1 
HETATM 2852 O  O     . HOH F 4 .   ? 14.404  4.168   20.716  1.00 35.33 ?  634 HOH A O     1 
HETATM 2853 O  O     . HOH F 4 .   ? 11.720  1.846   18.680  1.00 22.70 ?  635 HOH A O     1 
HETATM 2854 O  O     . HOH F 4 .   ? 8.961   27.768  18.641  1.00 19.44 ?  636 HOH A O     1 
HETATM 2855 O  O     . HOH F 4 .   ? -13.558 11.088  25.653  1.00 13.56 ?  637 HOH A O     1 
HETATM 2856 O  O     . HOH F 4 .   ? 8.670   6.412   10.732  1.00 13.81 ?  638 HOH A O     1 
HETATM 2857 O  O     . HOH F 4 .   ? 3.107   26.678  3.888   1.00 26.09 ?  639 HOH A O     1 
HETATM 2858 O  O     . HOH F 4 .   ? -2.390  27.809  29.809  1.00 21.27 ?  640 HOH A O     1 
HETATM 2859 O  O     . HOH F 4 .   ? -13.306 9.731   23.271  1.00 16.74 ?  641 HOH A O     1 
HETATM 2860 O  O     . HOH F 4 .   ? -13.882 31.028  2.619   1.00 28.94 ?  642 HOH A O     1 
HETATM 2861 O  O     . HOH F 4 .   ? 10.268  19.014  8.550   1.00 53.12 ?  643 HOH A O     1 
HETATM 2862 O  O     . HOH F 4 .   ? -16.740 18.385  8.765   1.00 29.35 ?  644 HOH A O     1 
HETATM 2863 O  O     . HOH F 4 .   ? -18.252 7.474   15.762  1.00 15.44 ?  645 HOH A O     1 
HETATM 2864 O  O     . HOH F 4 .   ? 12.703  22.761  28.310  1.00 20.05 ?  646 HOH A O     1 
HETATM 2865 O  O     . HOH F 4 .   ? -20.328 11.082  5.915   1.00 29.64 ?  647 HOH A O     1 
HETATM 2866 O  O     . HOH F 4 .   ? -16.382 13.738  16.725  1.00 8.35  ?  648 HOH A O     1 
HETATM 2867 O  O     . HOH F 4 .   ? -20.207 20.236  38.443  1.00 33.38 ?  649 HOH A O     1 
HETATM 2868 O  O     . HOH F 4 .   ? -10.678 25.216  28.264  1.00 21.79 ?  650 HOH A O     1 
HETATM 2869 O  O     . HOH F 4 .   ? 6.561   -2.934  20.602  1.00 16.51 ?  651 HOH A O     1 
HETATM 2870 O  O     . HOH F 4 .   ? -7.402  27.007  19.354  1.00 13.16 ?  652 HOH A O     1 
HETATM 2871 O  O     . HOH F 4 .   ? -12.262 11.177  29.267  1.00 30.24 ?  653 HOH A O     1 
HETATM 2872 O  O     . HOH F 4 .   ? -18.969 5.859   1.326   1.00 21.75 ?  654 HOH A O     1 
HETATM 2873 O  O     . HOH F 4 .   ? -19.453 25.314  25.152  1.00 40.05 ?  655 HOH A O     1 
HETATM 2874 O  O     . HOH F 4 .   ? -1.036  30.961  7.004   1.00 14.76 ?  656 HOH A O     1 
HETATM 2875 O  O     . HOH F 4 .   ? -12.998 27.040  -9.637  1.00 30.26 ?  657 HOH A O     1 
HETATM 2876 O  O     . HOH F 4 .   ? 15.608  27.126  32.670  1.00 34.23 ?  658 HOH A O     1 
HETATM 2877 O  O     . HOH F 4 .   ? 9.054   28.906  7.497   1.00 34.05 ?  659 HOH A O     1 
HETATM 2878 O  O     . HOH F 4 .   ? 13.038  -2.197  18.383  1.00 29.38 ?  660 HOH A O     1 
HETATM 2879 O  O     . HOH F 4 .   ? -9.091  16.664  1.994   1.00 11.32 ?  661 HOH A O     1 
HETATM 2880 O  O     . HOH F 4 .   ? -8.950  25.700  26.078  1.00 13.33 ?  662 HOH A O     1 
HETATM 2881 O  O     . HOH F 4 .   ? -12.294 22.043  23.383  1.00 10.34 ?  663 HOH A O     1 
HETATM 2882 O  O     . HOH F 4 .   ? -0.092  20.993  31.788  1.00 20.42 ?  664 HOH A O     1 
HETATM 2883 O  O     . HOH F 4 .   ? 7.602   -7.315  11.513  1.00 14.76 ?  665 HOH A O     1 
HETATM 2884 O  O     . HOH F 4 .   ? -2.517  12.761  0.617   1.00 18.43 ?  666 HOH A O     1 
HETATM 2885 O  O     . HOH F 4 .   ? -8.860  5.603   -7.285  1.00 21.15 ?  667 HOH A O     1 
HETATM 2886 O  O     . HOH F 4 .   ? 6.221   6.489   32.186  1.00 46.35 ?  668 HOH A O     1 
HETATM 2887 O  O     . HOH F 4 .   ? 7.540   36.377  24.914  1.00 37.67 ?  669 HOH A O     1 
HETATM 2888 O  O     . HOH F 4 .   ? 7.050   -8.787  9.485   1.00 39.45 ?  670 HOH A O     1 
HETATM 2889 O  O     . HOH F 4 .   ? 9.770   13.038  30.768  1.00 29.75 ?  671 HOH A O     1 
HETATM 2890 O  O     . HOH F 4 .   ? 6.908   27.049  7.846   1.00 22.73 ?  672 HOH A O     1 
HETATM 2891 O  O     . HOH F 4 .   ? 6.103   -2.078  3.255   1.00 47.03 ?  673 HOH A O     1 
HETATM 2892 O  O     . HOH F 4 .   ? -23.090 0.630   -0.993  1.00 34.76 ?  674 HOH A O     1 
HETATM 2893 O  O     . HOH F 4 .   ? -14.776 5.384   18.734  1.00 22.44 ?  675 HOH A O     1 
HETATM 2894 O  O     . HOH F 4 .   ? 13.791  12.476  19.697  1.00 23.91 ?  676 HOH A O     1 
HETATM 2895 O  O     . HOH F 4 .   ? -8.754  30.174  19.878  1.00 36.39 ?  677 HOH A O     1 
HETATM 2896 O  O     . HOH F 4 .   ? -6.619  -1.409  21.769  1.00 31.32 ?  678 HOH A O     1 
HETATM 2897 O  O     . HOH F 4 .   ? -19.339 16.014  -0.526  1.00 24.96 ?  679 HOH A O     1 
HETATM 2898 O  O     . HOH F 4 .   ? -18.054 15.875  -19.808 1.00 38.09 ?  680 HOH A O     1 
HETATM 2899 O  O     . HOH F 4 .   ? -11.025 21.950  16.984  1.00 12.70 ?  681 HOH A O     1 
HETATM 2900 O  O     . HOH F 4 .   ? -4.880  -4.677  6.182   1.00 23.00 ?  682 HOH A O     1 
HETATM 2901 O  O     . HOH F 4 .   ? 6.352   31.195  33.771  1.00 26.83 ?  683 HOH A O     1 
HETATM 2902 O  O     . HOH F 4 .   ? 13.875  19.201  36.119  1.00 33.00 ?  684 HOH A O     1 
HETATM 2903 O  O     . HOH F 4 .   ? 6.048   -13.794 11.849  1.00 23.60 ?  685 HOH A O     1 
HETATM 2904 O  O     . HOH F 4 .   ? 1.046   25.953  -0.432  1.00 41.08 ?  686 HOH A O     1 
HETATM 2905 O  O     . HOH F 4 .   ? 5.383   16.171  5.598   1.00 31.60 ?  687 HOH A O     1 
HETATM 2906 O  O     . HOH F 4 .   ? -12.791 23.630  35.476  1.00 24.22 ?  688 HOH A O     1 
HETATM 2907 O  O     . HOH F 4 .   ? -16.250 20.739  4.911   1.00 20.46 ?  689 HOH A O     1 
HETATM 2908 O  O     . HOH F 4 .   ? -20.201 -4.524  -12.233 1.00 25.90 ?  690 HOH A O     1 
HETATM 2909 O  O     . HOH F 4 .   ? 9.299   -4.334  6.812   1.00 24.32 ?  691 HOH A O     1 
HETATM 2910 O  O     . HOH F 4 .   ? -20.674 10.561  21.517  1.00 22.83 ?  692 HOH A O     1 
HETATM 2911 O  O     . HOH F 4 .   ? -9.266  15.745  33.907  1.00 35.17 ?  693 HOH A O     1 
HETATM 2912 O  O     . HOH F 4 .   ? -17.905 27.120  -3.684  1.00 38.81 ?  694 HOH A O     1 
HETATM 2913 O  O     . HOH F 4 .   ? 7.618   -12.991 8.298   1.00 15.79 ?  695 HOH A O     1 
HETATM 2914 O  O     . HOH F 4 .   ? -15.104 15.903  14.845  1.00 19.67 ?  696 HOH A O     1 
HETATM 2915 O  O     . HOH F 4 .   ? 15.328  -15.245 5.997   1.00 33.31 ?  697 HOH A O     1 
HETATM 2916 O  O     . HOH F 4 .   ? -18.106 7.483   20.299  1.00 33.89 ?  698 HOH A O     1 
HETATM 2917 O  O     . HOH F 4 .   ? 10.683  -6.857  6.456   1.00 45.18 ?  699 HOH A O     1 
HETATM 2918 O  O     . HOH F 4 .   ? 7.785   24.520  12.359  1.00 16.51 ?  700 HOH A O     1 
HETATM 2919 O  O     . HOH F 4 .   ? 1.304   -5.047  11.682  1.00 21.44 ?  701 HOH A O     1 
HETATM 2920 O  O     . HOH F 4 .   ? -1.772  22.758  30.521  1.00 16.98 ?  702 HOH A O     1 
HETATM 2921 O  O     . HOH F 4 .   ? 13.835  22.656  18.548  1.00 22.99 ?  703 HOH A O     1 
HETATM 2922 O  O     . HOH F 4 .   ? -17.647 20.047  17.556  1.00 14.13 ?  704 HOH A O     1 
HETATM 2923 O  O     . HOH F 4 .   ? -8.479  4.899   24.933  1.00 17.68 ?  705 HOH A O     1 
HETATM 2924 O  O     . HOH F 4 .   ? -8.167  17.758  32.604  1.00 21.96 ?  706 HOH A O     1 
HETATM 2925 O  O     . HOH F 4 .   ? 7.534   -5.112  9.844   1.00 15.89 ?  707 HOH A O     1 
HETATM 2926 O  O     . HOH F 4 .   ? -11.903 22.218  14.432  1.00 15.41 ?  708 HOH A O     1 
HETATM 2927 O  O     . HOH F 4 .   ? 12.533  5.168   5.270   1.00 33.06 ?  709 HOH A O     1 
HETATM 2928 O  O     . HOH F 4 .   ? -16.430 19.940  12.581  1.00 15.61 ?  710 HOH A O     1 
HETATM 2929 O  O     . HOH F 4 .   ? 9.711   30.659  15.840  1.00 30.87 ?  711 HOH A O     1 
HETATM 2930 O  O     . HOH F 4 .   ? 11.462  18.014  24.554  1.00 32.40 ?  712 HOH A O     1 
HETATM 2931 O  O     . HOH F 4 .   ? 4.325   20.269  5.646   1.00 15.95 ?  713 HOH A O     1 
HETATM 2932 O  O     . HOH F 4 .   ? -8.620  20.484  32.505  1.00 29.29 ?  714 HOH A O     1 
HETATM 2933 O  O     . HOH F 4 .   ? -17.518 23.122  19.834  1.00 40.21 ?  715 HOH A O     1 
HETATM 2934 O  O     . HOH F 4 .   ? -17.742 20.719  27.937  1.00 29.82 ?  716 HOH A O     1 
HETATM 2935 O  O     . HOH F 4 .   ? -18.291 11.419  -27.840 1.00 38.08 ?  717 HOH A O     1 
HETATM 2936 O  O     . HOH F 4 .   ? 0.852   8.442   -14.369 1.00 35.73 ?  718 HOH A O     1 
HETATM 2937 O  O     . HOH F 4 .   ? -18.493 -0.280  6.413   1.00 19.39 ?  719 HOH A O     1 
HETATM 2938 O  O     . HOH F 4 .   ? -6.858  27.776  2.153   1.00 35.19 ?  720 HOH A O     1 
HETATM 2939 O  O     . HOH F 4 .   ? -11.601 5.570   3.295   1.00 27.34 ?  721 HOH A O     1 
HETATM 2940 O  O     . HOH F 4 .   ? -19.913 14.443  -15.287 1.00 27.00 ?  722 HOH A O     1 
HETATM 2941 O  O     . HOH F 4 .   ? 13.928  17.335  15.718  1.00 24.10 ?  723 HOH A O     1 
HETATM 2942 O  O     . HOH F 4 .   ? -18.065 21.379  10.842  1.00 25.48 ?  724 HOH A O     1 
HETATM 2943 O  O     . HOH F 4 .   ? -17.188 18.554  3.306   1.00 29.22 ?  725 HOH A O     1 
HETATM 2944 O  O     . HOH F 4 .   ? -7.751  28.493  7.151   1.00 18.65 ?  726 HOH A O     1 
HETATM 2945 O  O     . HOH F 4 .   ? 10.856  10.258  8.542   1.00 20.40 ?  727 HOH A O     1 
HETATM 2946 O  O     . HOH F 4 .   ? -17.801 21.817  -0.071  1.00 26.34 ?  728 HOH A O     1 
HETATM 2947 O  O     . HOH F 4 .   ? 5.638   3.527   26.681  1.00 22.61 ?  729 HOH A O     1 
HETATM 2948 O  O     . HOH F 4 .   ? -10.138 31.089  -5.270  1.00 41.71 ?  730 HOH A O     1 
HETATM 2949 O  O     . HOH F 4 .   ? -16.955 29.540  3.019   1.00 37.23 ?  731 HOH A O     1 
HETATM 2950 O  O     . HOH F 4 .   ? 13.333  37.817  32.455  1.00 55.54 ?  732 HOH A O     1 
HETATM 2951 O  O     . HOH F 4 .   ? 12.036  -2.581  7.396   1.00 15.17 ?  733 HOH A O     1 
HETATM 2952 O  O     . HOH F 4 .   ? 12.466  -4.658  17.853  1.00 32.49 ?  734 HOH A O     1 
HETATM 2953 O  O     . HOH F 4 .   ? 14.651  -9.007  17.323  1.00 29.67 ?  735 HOH A O     1 
HETATM 2954 O  O     . HOH F 4 .   ? -20.831 -0.436  -0.404  1.00 29.73 ?  736 HOH A O     1 
HETATM 2955 O  O     . HOH F 4 .   ? -13.084 26.660  22.747  1.00 31.96 ?  737 HOH A O     1 
HETATM 2956 O  O     . HOH F 4 .   ? -18.603 18.603  24.687  1.00 19.14 ?  738 HOH A O     1 
HETATM 2957 O  O     . HOH F 4 .   ? -22.385 8.233   -11.221 1.00 52.31 ?  739 HOH A O     1 
HETATM 2958 O  O     . HOH F 4 .   ? -5.314  0.295   24.672  1.00 22.19 ?  740 HOH A O     1 
HETATM 2959 O  O     . HOH F 4 .   ? -15.122 -6.357  -5.528  1.00 53.72 ?  741 HOH A O     1 
HETATM 2960 O  O     . HOH F 4 .   ? -20.678 26.071  2.819   1.00 37.71 ?  742 HOH A O     1 
HETATM 2961 O  O     . HOH F 4 .   ? -12.748 -5.876  12.348  1.00 42.73 ?  743 HOH A O     1 
HETATM 2962 O  O     . HOH F 4 .   ? 14.553  6.894   15.470  1.00 22.47 ?  744 HOH A O     1 
HETATM 2963 O  O     . HOH F 4 .   ? 3.822   -3.510  3.243   1.00 42.59 ?  745 HOH A O     1 
HETATM 2964 O  O     . HOH F 4 .   ? -11.760 14.305  31.349  1.00 21.55 ?  746 HOH A O     1 
HETATM 2965 O  O     . HOH F 4 .   ? -19.018 14.328  23.317  1.00 11.82 ?  747 HOH A O     1 
HETATM 2966 O  O     . HOH F 4 .   ? 2.899   19.079  3.550   1.00 31.05 ?  748 HOH A O     1 
HETATM 2967 O  O     . HOH F 4 .   ? -10.902 24.237  18.702  1.00 11.31 ?  749 HOH A O     1 
HETATM 2968 O  O     . HOH F 4 .   ? 13.713  21.203  26.107  1.00 27.36 ?  750 HOH A O     1 
HETATM 2969 O  O     . HOH F 4 .   ? 11.217  17.061  7.530   1.00 43.01 ?  751 HOH A O     1 
HETATM 2970 O  O     . HOH F 4 .   ? -20.854 4.205   16.211  1.00 19.39 ?  752 HOH A O     1 
HETATM 2971 O  O     . HOH F 4 .   ? -12.357 -0.103  -20.756 1.00 38.05 ?  753 HOH A O     1 
HETATM 2972 O  O     . HOH F 4 .   ? 15.390  12.987  7.953   1.00 35.49 ?  754 HOH A O     1 
HETATM 2973 O  O     . HOH F 4 .   ? -19.860 0.690   -17.824 1.00 25.21 ?  755 HOH A O     1 
HETATM 2974 O  O     . HOH F 4 .   ? 9.057   -11.783 6.375   1.00 29.70 ?  756 HOH A O     1 
HETATM 2975 O  O     . HOH F 4 .   ? 2.405   13.328  33.618  1.00 32.49 ?  757 HOH A O     1 
HETATM 2976 O  O     . HOH F 4 .   ? -13.515 9.093   -33.164 1.00 35.53 ?  758 HOH A O     1 
HETATM 2977 O  O     . HOH F 4 .   ? 1.474   -2.779  -8.135  1.00 39.89 ?  759 HOH A O     1 
HETATM 2978 O  O     . HOH F 4 .   ? -3.688  0.873   26.881  1.00 37.13 ?  760 HOH A O     1 
HETATM 2979 O  O     . HOH F 4 .   ? 3.165   -11.324 15.711  1.00 36.32 ?  761 HOH A O     1 
HETATM 2980 O  O     . HOH F 4 .   ? 15.968  -1.848  18.572  1.00 47.27 ?  762 HOH A O     1 
HETATM 2981 O  O     . HOH F 4 .   ? 12.907  18.400  13.299  1.00 22.45 ?  763 HOH A O     1 
HETATM 2982 O  O     . HOH F 4 .   ? 7.524   31.714  19.681  1.00 25.47 ?  764 HOH A O     1 
HETATM 2983 O  O     . HOH F 4 .   ? -10.956 -1.921  -19.499 1.00 34.78 ?  765 HOH A O     1 
HETATM 2984 O  O     . HOH F 4 .   ? 12.032  15.708  9.903   1.00 33.88 ?  766 HOH A O     1 
HETATM 2985 O  O     . HOH F 4 .   ? 13.323  11.514  25.297  1.00 20.17 ?  767 HOH A O     1 
HETATM 2986 O  O     . HOH F 4 .   ? 4.501   27.823  8.134   1.00 32.51 ?  768 HOH A O     1 
HETATM 2987 O  O     . HOH F 4 .   ? 2.896   18.011  -16.992 1.00 47.60 ?  769 HOH A O     1 
HETATM 2988 O  O     . HOH F 4 .   ? -9.383  11.031  -2.133  1.00 22.20 ?  770 HOH A O     1 
HETATM 2989 O  O     . HOH F 4 .   ? -14.688 24.749  12.701  1.00 32.56 ?  771 HOH A O     1 
HETATM 2990 O  O     . HOH F 4 .   ? -11.452 26.560  15.289  1.00 33.34 ?  772 HOH A O     1 
HETATM 2991 O  O     . HOH F 4 .   ? 0.162   33.487  24.680  1.00 39.12 ?  773 HOH A O     1 
HETATM 2992 O  O     . HOH F 4 .   ? -2.735  -3.331  23.989  1.00 48.96 ?  774 HOH A O     1 
HETATM 2993 O  O     . HOH F 4 .   ? -22.561 20.468  39.731  1.00 40.10 ?  775 HOH A O     1 
HETATM 2994 O  O     . HOH F 4 .   ? -23.370 9.893   -12.730 1.00 35.34 ?  776 HOH A O     1 
HETATM 2995 O  O     . HOH F 4 .   ? -18.916 24.470  8.425   1.00 39.42 ?  777 HOH A O     1 
HETATM 2996 O  O     . HOH F 4 .   ? -10.038 26.493  17.836  1.00 16.40 ?  778 HOH A O     1 
HETATM 2997 O  O     . HOH F 4 .   ? 12.419  16.156  24.898  1.00 34.86 ?  779 HOH A O     1 
HETATM 2998 O  O     . HOH F 4 .   ? -26.508 3.631   -4.740  1.00 46.01 ?  780 HOH A O     1 
HETATM 2999 O  O     . HOH F 4 .   ? -13.103 23.791  14.219  1.00 27.32 ?  781 HOH A O     1 
HETATM 3000 O  O     . HOH F 4 .   ? 11.658  15.223  27.304  1.00 30.68 ?  782 HOH A O     1 
HETATM 3001 O  O     . HOH F 4 .   ? 0.419   31.989  23.205  1.00 39.41 ?  783 HOH A O     1 
HETATM 3002 O  O     . HOH F 4 .   ? -3.110  32.246  13.981  1.00 28.79 ?  784 HOH A O     1 
HETATM 3003 O  O     . HOH F 4 .   ? 3.300   -3.489  -16.139 1.00 48.89 ?  785 HOH A O     1 
HETATM 3004 O  O     . HOH F 4 .   ? 13.492  3.750   9.074   1.00 27.35 ?  786 HOH A O     1 
HETATM 3005 O  O     . HOH F 4 .   ? 12.373  9.302   6.164   1.00 53.06 ?  787 HOH A O     1 
HETATM 3006 O  O     . HOH F 4 .   ? -21.845 -2.682  0.769   1.00 46.67 ?  788 HOH A O     1 
HETATM 3007 O  O     . HOH F 4 .   ? -6.108  -1.539  1.211   1.00 50.03 ?  789 HOH A O     1 
HETATM 3008 O  O     . HOH F 4 .   ? -17.401 6.015   17.979  1.00 18.37 ?  790 HOH A O     1 
HETATM 3009 O  O     . HOH F 4 .   ? -2.650  -6.086  7.105   1.00 37.01 ?  791 HOH A O     1 
HETATM 3010 O  O     . HOH F 4 .   ? 12.148  6.149   2.376   1.00 48.98 ?  792 HOH A O     1 
HETATM 3011 O  O     . HOH F 4 .   ? 10.468  -15.404 4.938   1.00 32.03 ?  793 HOH A O     1 
HETATM 3012 O  O     . HOH F 4 .   ? -19.872 17.580  26.529  1.00 46.65 ?  794 HOH A O     1 
HETATM 3013 O  O     . HOH F 4 .   ? -19.036 18.084  16.729  1.00 25.80 ?  795 HOH A O     1 
HETATM 3014 O  O     . HOH F 4 .   ? -13.177 24.493  24.498  1.00 29.94 ?  796 HOH A O     1 
HETATM 3015 O  O     . HOH F 4 .   ? 14.467  -6.358  18.269  1.00 42.98 ?  797 HOH A O     1 
HETATM 3016 O  O     . HOH F 4 .   ? -7.103  29.953  2.017   1.00 36.26 ?  798 HOH A O     1 
HETATM 3017 O  O     . HOH F 4 .   ? -17.961 15.183  8.346   1.00 30.22 ?  799 HOH A O     1 
HETATM 3018 O  O     . HOH F 4 .   ? -10.170 25.398  11.371  1.00 30.77 ?  800 HOH A O     1 
HETATM 3019 O  O     . HOH F 4 .   ? -14.892 -6.191  -20.639 1.00 31.65 ?  801 HOH A O     1 
HETATM 3020 O  O     . HOH F 4 .   ? -16.657 23.973  15.013  1.00 49.77 ?  802 HOH A O     1 
HETATM 3021 O  O     . HOH F 4 .   ? -6.546  7.232   27.773  1.00 24.25 ?  803 HOH A O     1 
HETATM 3022 O  O     . HOH F 4 .   ? -1.914  1.242   2.380   1.00 49.83 ?  804 HOH A O     1 
HETATM 3023 O  O     . HOH F 4 .   ? 15.900  20.778  25.898  1.00 37.22 ?  805 HOH A O     1 
HETATM 3024 O  O     . HOH F 4 .   ? 4.256   33.114  23.084  1.00 40.21 ?  806 HOH A O     1 
HETATM 3025 O  O     . HOH F 4 .   ? 11.060  26.021  0.867   1.00 40.16 ?  807 HOH A O     1 
HETATM 3026 O  O     . HOH F 4 .   ? 12.562  -16.963 5.287   1.00 42.12 ?  808 HOH A O     1 
HETATM 3027 O  O     . HOH F 4 .   ? 6.703   1.225   24.776  1.00 35.28 ?  809 HOH A O     1 
HETATM 3028 O  O     . HOH F 4 .   ? 11.592  17.560  26.945  1.00 29.44 ?  810 HOH A O     1 
HETATM 3029 O  O     . HOH F 4 .   ? 2.607   29.235  36.271  1.00 32.56 ?  811 HOH A O     1 
HETATM 3030 O  O     . HOH F 4 .   ? -17.103 17.197  12.542  1.00 21.04 ?  812 HOH A O     1 
HETATM 3031 O  O     . HOH F 4 .   ? -5.238  -5.667  10.410  1.00 31.53 ?  813 HOH A O     1 
HETATM 3032 O  O     . HOH F 4 .   ? 14.003  16.428  12.139  1.00 38.27 ?  814 HOH A O     1 
HETATM 3033 O  O     . HOH F 4 .   ? -8.660  29.916  22.446  1.00 33.32 ?  815 HOH A O     1 
HETATM 3034 O  O     . HOH F 4 .   ? -11.506 24.772  13.281  1.00 30.69 ?  816 HOH A O     1 
HETATM 3035 O  O     . HOH F 4 .   ? -5.141  27.670  0.263   1.00 36.79 ?  817 HOH A O     1 
HETATM 3036 O  O     . HOH F 4 .   ? 9.304   25.127  8.298   1.00 32.47 ?  818 HOH A O     1 
HETATM 3037 O  O     . HOH F 4 .   ? 1.327   35.517  20.803  1.00 31.54 ?  819 HOH A O     1 
HETATM 3038 O  O     . HOH F 4 .   ? 12.546  24.472  15.004  1.00 26.17 ?  820 HOH A O     1 
HETATM 3039 O  O     . HOH F 4 .   ? -13.581 25.142  19.015  1.00 28.31 ?  821 HOH A O     1 
HETATM 3040 O  O     . HOH F 4 .   ? 8.495   -17.140 5.931   1.00 17.86 ?  822 HOH A O     1 
HETATM 3041 O  O     . HOH F 4 .   ? 9.785   23.732  10.616  1.00 22.36 ?  823 HOH A O     1 
HETATM 3042 O  O     . HOH F 4 .   ? -7.129  28.306  26.689  1.00 22.02 ?  824 HOH A O     1 
HETATM 3043 O  O     . HOH F 4 .   ? 16.772  25.247  28.803  1.00 30.69 ?  825 HOH A O     1 
HETATM 3044 O  O     . HOH F 4 .   ? 15.464  26.222  18.337  1.00 41.89 ?  826 HOH A O     1 
HETATM 3045 O  O     . HOH F 4 .   ? -6.453  28.614  29.314  1.00 37.26 ?  827 HOH A O     1 
HETATM 3046 O  O     . HOH F 4 .   ? 12.604  -8.712  20.716  1.00 40.42 ?  828 HOH A O     1 
HETATM 3047 O  O     . HOH F 4 .   ? -19.763 -1.024  3.548   1.00 37.42 ?  829 HOH A O     1 
HETATM 3048 O  O     . HOH F 4 .   ? -19.584 28.803  8.642   1.00 49.03 ?  830 HOH A O     1 
HETATM 3049 O  O     . HOH F 4 .   ? -19.850 11.820  23.700  1.00 34.26 ?  831 HOH A O     1 
HETATM 3050 O  O     . HOH F 4 .   ? -7.861  -1.377  16.982  1.00 30.54 ?  832 HOH A O     1 
HETATM 3051 O  O     . HOH F 4 .   ? -16.020 11.420  26.486  1.00 29.41 ?  833 HOH A O     1 
HETATM 3052 O  O     . HOH F 4 .   ? 11.803  -0.294  20.133  1.00 36.52 ?  834 HOH A O     1 
HETATM 3053 O  O     . HOH F 4 .   ? -2.220  24.360  36.104  1.00 54.20 ?  835 HOH A O     1 
HETATM 3054 O  O     . HOH F 4 .   ? 11.483  31.521  8.077   1.00 39.51 ?  836 HOH A O     1 
HETATM 3055 O  O     . HOH F 4 .   ? -14.488 -2.592  13.416  1.00 22.94 ?  837 HOH A O     1 
HETATM 3056 O  O     . HOH F 4 .   ? 7.443   -3.701  4.841   1.00 40.44 ?  838 HOH A O     1 
HETATM 3057 O  O     . HOH F 4 .   ? -9.875  -2.430  16.606  1.00 34.67 ?  839 HOH A O     1 
HETATM 3058 O  O     . HOH F 4 .   ? -13.155 25.700  26.727  1.00 27.61 ?  840 HOH A O     1 
HETATM 3059 O  O     . HOH F 4 .   ? -14.671 3.060   19.800  1.00 35.40 ?  841 HOH A O     1 
HETATM 3060 O  O     . HOH F 4 .   ? -3.863  23.745  31.985  1.00 25.09 ?  842 HOH A O     1 
HETATM 3061 O  O     . HOH F 4 .   ? -23.915 -1.403  -16.738 1.00 36.72 ?  843 HOH A O     1 
HETATM 3062 O  O     . HOH F 4 .   ? -21.121 -1.440  6.277   1.00 40.23 ?  844 HOH A O     1 
HETATM 3063 O  O     . HOH F 4 .   ? 3.627   -10.340 10.119  1.00 37.55 ?  845 HOH A O     1 
HETATM 3064 O  O     . HOH F 4 .   ? 4.329   16.108  36.778  1.00 28.33 ?  846 HOH A O     1 
HETATM 3065 O  O     . HOH F 4 .   ? 10.920  21.689  9.464   1.00 32.57 ?  847 HOH A O     1 
HETATM 3066 O  O     . HOH F 4 .   ? 11.382  26.482  18.897  1.00 24.58 ?  848 HOH A O     1 
HETATM 3067 O  O     . HOH F 4 .   ? 6.748   35.997  22.413  1.00 37.17 ?  849 HOH A O     1 
HETATM 3068 O  O     . HOH F 4 .   ? -4.141  28.497  31.444  1.00 34.48 ?  850 HOH A O     1 
HETATM 3069 O  O     . HOH F 4 .   ? -6.846  30.283  25.128  1.00 30.01 ?  851 HOH A O     1 
HETATM 3070 O  O     . HOH F 4 .   ? -7.723  9.143   29.452  1.00 23.08 ?  852 HOH A O     1 
HETATM 3071 O  O     . HOH F 4 .   ? -17.952 10.608  25.290  1.00 31.92 ?  853 HOH A O     1 
HETATM 3072 O  O     . HOH F 4 .   ? -9.110  -2.026  18.572  1.00 33.61 ?  854 HOH A O     1 
HETATM 3073 O  O     . HOH F 4 .   ? -4.326  26.428  32.663  1.00 45.98 ?  855 HOH A O     1 
HETATM 3074 O  O     . HOH F 4 .   ? -19.721 15.250  -21.912 1.00 35.35 ?  856 HOH A O     1 
HETATM 3075 O  O     . HOH F 4 .   ? 20.715  -3.498  16.027  1.00 36.01 ?  857 HOH A O     1 
HETATM 3076 O  O     . HOH F 4 .   ? 16.878  35.567  30.186  1.00 45.79 ?  858 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   ? 0.3839 0.3660 0.3752 0.0184  -0.0235 -0.0159 0   MET A N   
2    C CA  . MET A 1   ? 0.4114 0.3931 0.4019 0.0186  -0.0236 -0.0156 0   MET A CA  
3    C C   . MET A 1   ? 0.3588 0.3397 0.3489 0.0185  -0.0240 -0.0153 0   MET A C   
4    O O   . MET A 1   ? 0.3671 0.3474 0.3573 0.0184  -0.0245 -0.0154 0   MET A O   
5    C CB  . MET A 1   ? 0.4290 0.4103 0.4191 0.0190  -0.0242 -0.0158 0   MET A CB  
6    C CG  . MET A 1   ? 0.4475 0.4274 0.4368 0.0192  -0.0252 -0.0157 0   MET A CG  
7    S SD  . MET A 1   ? 0.4634 0.4428 0.4523 0.0196  -0.0260 -0.0159 0   MET A SD  
8    C CE  . MET A 1   ? 0.4764 0.4542 0.4647 0.0196  -0.0271 -0.0158 0   MET A CE  
9    N N   . MET A 2   ? 0.3818 0.3625 0.3712 0.0186  -0.0238 -0.0150 1   MET A N   
10   C CA  . MET A 2   ? 0.3926 0.3723 0.3814 0.0185  -0.0242 -0.0148 1   MET A CA  
11   C C   . MET A 2   ? 0.3687 0.3472 0.3568 0.0186  -0.0253 -0.0148 1   MET A C   
12   O O   . MET A 2   ? 0.3623 0.3404 0.3501 0.0189  -0.0257 -0.0150 1   MET A O   
13   C CB  . MET A 2   ? 0.4132 0.3929 0.4013 0.0186  -0.0239 -0.0145 1   MET A CB  
14   C CG  . MET A 2   ? 0.4507 0.4317 0.4395 0.0184  -0.0229 -0.0144 1   MET A CG  
15   S SD  . MET A 2   ? 0.5055 0.4869 0.4952 0.0181  -0.0225 -0.0143 1   MET A SD  
16   C CE  . MET A 2   ? 0.4850 0.4676 0.4753 0.0180  -0.0215 -0.0141 1   MET A CE  
17   N N   . ALA A 3   ? 0.3365 0.3141 0.3244 0.0184  -0.0257 -0.0146 2   ALA A N   
18   C CA  . ALA A 3   ? 0.3113 0.2879 0.2986 0.0184  -0.0267 -0.0145 2   ALA A CA  
19   C C   . ALA A 3   ? 0.3105 0.2880 0.2969 0.0176  -0.0266 -0.0135 2   ALA A C   
20   O O   . ALA A 3   ? 0.2871 0.2648 0.2729 0.0173  -0.0262 -0.0132 2   ALA A O   
21   C CB  . ALA A 3   ? 0.3172 0.2929 0.3044 0.0182  -0.0273 -0.0144 2   ALA A CB  
22   N N   . PRO A 4   ? 0.2846 0.2626 0.2708 0.0174  -0.0269 -0.0131 3   PRO A N   
23   C CA  . PRO A 4   ? 0.2640 0.2429 0.2493 0.0166  -0.0269 -0.0122 3   PRO A CA  
24   C C   . PRO A 4   ? 0.2552 0.2341 0.2399 0.0157  -0.0272 -0.0114 3   PRO A C   
25   O O   . PRO A 4   ? 0.2672 0.2453 0.2522 0.0159  -0.0277 -0.0116 3   PRO A O   
26   C CB  . PRO A 4   ? 0.2804 0.2597 0.2659 0.0167  -0.0272 -0.0121 3   PRO A CB  
27   C CG  . PRO A 4   ? 0.2879 0.2667 0.2744 0.0171  -0.0276 -0.0126 3   PRO A CG  
28   C CD  . PRO A 4   ? 0.2808 0.2587 0.2678 0.0177  -0.0273 -0.0135 3   PRO A CD  
29   N N   . VAL A 5   ? 0.2081 0.1876 0.1916 0.0149  -0.0271 -0.0107 4   VAL A N   
30   C CA  . VAL A 5   ? 0.1812 0.1605 0.1639 0.0142  -0.0276 -0.0101 4   VAL A CA  
31   C C   . VAL A 5   ? 0.1711 0.1513 0.1531 0.0134  -0.0277 -0.0092 4   VAL A C   
32   O O   . VAL A 5   ? 0.1534 0.1335 0.1345 0.0126  -0.0280 -0.0086 4   VAL A O   
33   C CB  . VAL A 5   ? 0.1676 0.1463 0.1493 0.0138  -0.0272 -0.0101 4   VAL A CB  
34   C CG1 . VAL A 5   ? 0.2136 0.1912 0.1960 0.0146  -0.0273 -0.0109 4   VAL A CG1 
35   C CG2 . VAL A 5   ? 0.1484 0.1281 0.1297 0.0135  -0.0265 -0.0100 4   VAL A CG2 
36   N N   . GLN A 6   ? 0.1390 0.1200 0.1215 0.0136  -0.0277 -0.0092 5   GLN A N   
37   C CA  . GLN A 6   ? 0.1258 0.1076 0.1075 0.0129  -0.0279 -0.0084 5   GLN A CA  
38   C C   . GLN A 6   ? 0.1307 0.1126 0.1124 0.0125  -0.0285 -0.0078 5   GLN A C   
39   O O   . GLN A 6   ? 0.1438 0.1262 0.1247 0.0116  -0.0286 -0.0070 5   GLN A O   
40   C CB  . GLN A 6   ? 0.1270 0.1094 0.1092 0.0133  -0.0279 -0.0086 5   GLN A CB  
41   C CG  . GLN A 6   ? 0.1344 0.1176 0.1159 0.0127  -0.0281 -0.0079 5   GLN A CG  
42   C CD  . GLN A 6   ? 0.1335 0.1172 0.1138 0.0119  -0.0278 -0.0075 5   GLN A CD  
43   O OE1 . GLN A 6   ? 0.1347 0.1181 0.1146 0.0119  -0.0273 -0.0078 5   GLN A OE1 
44   N NE2 . GLN A 6   ? 0.1445 0.1291 0.1242 0.0113  -0.0280 -0.0068 5   GLN A NE2 
45   N N   . LYS A 7   ? 0.1594 0.1409 0.1422 0.0130  -0.0289 -0.0080 6   LYS A N   
46   C CA  . LYS A 7   ? 0.1840 0.1652 0.1668 0.0128  -0.0296 -0.0074 6   LYS A CA  
47   C C   . LYS A 7   ? 0.1543 0.1346 0.1360 0.0123  -0.0299 -0.0072 6   LYS A C   
48   O O   . LYS A 7   ? 0.1570 0.1374 0.1380 0.0117  -0.0304 -0.0065 6   LYS A O   
49   C CB  . LYS A 7   ? 0.2744 0.2550 0.2584 0.0135  -0.0300 -0.0079 6   LYS A CB  
50   C CG  . LYS A 7   ? 0.3759 0.3574 0.3608 0.0138  -0.0300 -0.0079 6   LYS A CG  
51   C CD  . LYS A 7   ? 0.4826 0.4634 0.4686 0.0147  -0.0300 -0.0089 6   LYS A CD  
52   C CE  . LYS A 7   ? 0.5367 0.5169 0.5235 0.0149  -0.0304 -0.0090 6   LYS A CE  
53   N NZ  . LYS A 7   ? 0.5678 0.5475 0.5557 0.0157  -0.0304 -0.0100 6   LYS A NZ  
54   N N   . GLN A 8   ? 0.1499 0.1293 0.1314 0.0125  -0.0297 -0.0078 7   GLN A N   
55   C CA  . GLN A 8   ? 0.1715 0.1500 0.1520 0.0120  -0.0299 -0.0076 7   GLN A CA  
56   C C   . GLN A 8   ? 0.1363 0.1154 0.1153 0.0111  -0.0296 -0.0070 7   GLN A C   
57   O O   . GLN A 8   ? 0.1382 0.1170 0.1162 0.0104  -0.0300 -0.0064 7   GLN A O   
58   C CB  . GLN A 8   ? 0.1977 0.1752 0.1785 0.0125  -0.0297 -0.0083 7   GLN A CB  
59   C CG  . GLN A 8   ? 0.2360 0.2124 0.2178 0.0132  -0.0303 -0.0088 7   GLN A CG  
60   C CD  . GLN A 8   ? 0.2623 0.2392 0.2455 0.0139  -0.0303 -0.0091 7   GLN A CD  
61   O OE1 . GLN A 8   ? 0.3107 0.2874 0.2946 0.0141  -0.0309 -0.0091 7   GLN A OE1 
62   N NE2 . GLN A 8   ? 0.1988 0.1764 0.1823 0.0142  -0.0297 -0.0095 7   GLN A NE2 
63   N N   . PHE A 9   ? 0.1321 0.1122 0.1111 0.0110  -0.0289 -0.0071 8   PHE A N   
64   C CA  . PHE A 9   ? 0.1054 0.0863 0.0831 0.0101  -0.0286 -0.0065 8   PHE A CA  
65   C C   . PHE A 9   ? 0.0997 0.0813 0.0771 0.0095  -0.0290 -0.0057 8   PHE A C   
66   O O   . PHE A 9   ? 0.1101 0.0917 0.0862 0.0088  -0.0292 -0.0052 8   PHE A O   
67   C CB  . PHE A 9   ? 0.1088 0.0907 0.0865 0.0100  -0.0278 -0.0068 8   PHE A CB  
68   C CG  . PHE A 9   ? 0.1091 0.0905 0.0863 0.0099  -0.0272 -0.0072 8   PHE A CG  
69   C CD1 . PHE A 9   ? 0.1300 0.1114 0.1058 0.0090  -0.0270 -0.0068 8   PHE A CD1 
70   C CD2 . PHE A 9   ? 0.1363 0.1173 0.1144 0.0107  -0.0269 -0.0079 8   PHE A CD2 
71   C CE1 . PHE A 9   ? 0.1160 0.0970 0.0913 0.0089  -0.0265 -0.0072 8   PHE A CE1 
72   C CE2 . PHE A 9   ? 0.1445 0.1250 0.1220 0.0106  -0.0263 -0.0083 8   PHE A CE2 
73   C CZ  . PHE A 9   ? 0.1175 0.0980 0.0937 0.0097  -0.0261 -0.0079 8   PHE A CZ  
74   N N   . ARG A 10  ? 0.1133 0.0955 0.0917 0.0100  -0.0293 -0.0057 9   ARG A N   
75   C CA  . ARG A 10  ? 0.1179 0.1009 0.0960 0.0095  -0.0297 -0.0049 9   ARG A CA  
76   C C   . ARG A 10  ? 0.0949 0.0770 0.0726 0.0093  -0.0304 -0.0045 9   ARG A C   
77   O O   . ARG A 10  ? 0.1154 0.0978 0.0922 0.0087  -0.0307 -0.0038 9   ARG A O   
78   C CB  . ARG A 10  ? 0.1210 0.1049 0.1003 0.0100  -0.0297 -0.0049 9   ARG A CB  
79   C CG  . ARG A 10  ? 0.1435 0.1278 0.1230 0.0103  -0.0293 -0.0053 9   ARG A CG  
80   C CD  . ARG A 10  ? 0.1441 0.1293 0.1225 0.0096  -0.0291 -0.0049 9   ARG A CD  
81   N NE  . ARG A 10  ? 0.1695 0.1554 0.1474 0.0091  -0.0295 -0.0041 9   ARG A NE  
82   C CZ  . ARG A 10  ? 0.1922 0.1788 0.1705 0.0092  -0.0298 -0.0039 9   ARG A CZ  
83   N NH1 . ARG A 10  ? 0.1872 0.1738 0.1662 0.0099  -0.0296 -0.0044 9   ARG A NH1 
84   N NH2 . ARG A 10  ? 0.2164 0.2037 0.1943 0.0088  -0.0301 -0.0032 9   ARG A NH2 
85   N N   . GLU A 11  ? 0.1089 0.0897 0.0872 0.0099  -0.0308 -0.0049 10  GLU A N   
86   C CA  . GLU A 11  ? 0.1198 0.0996 0.0977 0.0097  -0.0315 -0.0045 10  GLU A CA  
87   C C   . GLU A 11  ? 0.0864 0.0656 0.0627 0.0089  -0.0313 -0.0043 10  GLU A C   
88   O O   . GLU A 11  ? 0.1262 0.1052 0.1015 0.0083  -0.0317 -0.0036 10  GLU A O   
89   C CB  . GLU A 11  ? 0.1313 0.1099 0.1102 0.0104  -0.0318 -0.0051 10  GLU A CB  
90   C CG  . GLU A 11  ? 0.1500 0.1274 0.1286 0.0103  -0.0325 -0.0048 10  GLU A CG  
91   C CD  . GLU A 11  ? 0.1934 0.1711 0.1718 0.0099  -0.0331 -0.0040 10  GLU A CD  
92   O OE1 . GLU A 11  ? 0.2225 0.2013 0.2017 0.0101  -0.0331 -0.0037 10  GLU A OE1 
93   O OE2 . GLU A 11  ? 0.1956 0.1725 0.1732 0.0095  -0.0336 -0.0035 10  GLU A OE2 
94   N N   . PHE A 12  ? 0.1296 0.1085 0.1055 0.0089  -0.0308 -0.0048 11  PHE A N   
95   C CA  . PHE A 12  ? 0.1234 0.1020 0.0978 0.0081  -0.0305 -0.0046 11  PHE A CA  
96   C C   . PHE A 12  ? 0.1128 0.0924 0.0861 0.0072  -0.0303 -0.0040 11  PHE A C   
97   O O   . PHE A 12  ? 0.1027 0.0819 0.0748 0.0065  -0.0305 -0.0035 11  PHE A O   
98   C CB  . PHE A 12  ? 0.1133 0.0918 0.0877 0.0083  -0.0298 -0.0054 11  PHE A CB  
99   C CG  . PHE A 12  ? 0.0959 0.0739 0.0687 0.0075  -0.0294 -0.0053 11  PHE A CG  
100  C CD1 . PHE A 12  ? 0.1263 0.1031 0.0981 0.0070  -0.0298 -0.0050 11  PHE A CD1 
101  C CD2 . PHE A 12  ? 0.1225 0.1014 0.0950 0.0072  -0.0285 -0.0055 11  PHE A CD2 
102  C CE1 . PHE A 12  ? 0.1310 0.1074 0.1014 0.0063  -0.0294 -0.0050 11  PHE A CE1 
103  C CE2 . PHE A 12  ? 0.1059 0.0844 0.0770 0.0064  -0.0281 -0.0055 11  PHE A CE2 
104  C CZ  . PHE A 12  ? 0.1043 0.0816 0.0744 0.0060  -0.0285 -0.0052 11  PHE A CZ  
105  N N   . HIS A 13  ? 0.0945 0.0756 0.0684 0.0073  -0.0299 -0.0039 12  HIS A N   
106  C CA  . HIS A 13  ? 0.1088 0.0910 0.0817 0.0066  -0.0298 -0.0033 12  HIS A CA  
107  C C   . HIS A 13  ? 0.1012 0.0833 0.0739 0.0063  -0.0305 -0.0026 12  HIS A C   
108  O O   . HIS A 13  ? 0.1289 0.1111 0.1003 0.0055  -0.0306 -0.0020 12  HIS A O   
109  C CB  . HIS A 13  ? 0.1042 0.0879 0.0779 0.0068  -0.0293 -0.0034 12  HIS A CB  
110  C CG  . HIS A 13  ? 0.1177 0.1026 0.0906 0.0060  -0.0292 -0.0028 12  HIS A CG  
111  N ND1 . HIS A 13  ? 0.1151 0.1010 0.0884 0.0060  -0.0295 -0.0023 12  HIS A ND1 
112  C CD2 . HIS A 13  ? 0.1138 0.0991 0.0854 0.0052  -0.0287 -0.0026 12  HIS A CD2 
113  C CE1 . HIS A 13  ? 0.1165 0.1034 0.0889 0.0053  -0.0292 -0.0019 12  HIS A CE1 
114  N NE2 . HIS A 13  ? 0.1290 0.1156 0.1004 0.0048  -0.0288 -0.0021 12  HIS A NE2 
115  N N   . ASP A 14  ? 0.1350 0.1169 0.1088 0.0069  -0.0311 -0.0025 13  ASP A N   
116  C CA  . ASP A 14  ? 0.1470 0.1287 0.1206 0.0068  -0.0318 -0.0018 13  ASP A CA  
117  C C   . ASP A 14  ? 0.1211 0.1015 0.0936 0.0063  -0.0322 -0.0015 13  ASP A C   
118  O O   . ASP A 14  ? 0.1484 0.1289 0.1200 0.0057  -0.0325 -0.0008 13  ASP A O   
119  C CB  . ASP A 14  ? 0.1641 0.1457 0.1393 0.0076  -0.0323 -0.0019 13  ASP A CB  
120  C CG  . ASP A 14  ? 0.2255 0.2085 0.2017 0.0079  -0.0320 -0.0020 13  ASP A CG  
121  O OD1 . ASP A 14  ? 0.2235 0.2077 0.1991 0.0075  -0.0316 -0.0017 13  ASP A OD1 
122  O OD2 . ASP A 14  ? 0.2885 0.2714 0.2660 0.0086  -0.0321 -0.0023 13  ASP A OD2 
123  N N   . ARG A 15  ? 0.1125 0.0917 0.0848 0.0064  -0.0321 -0.0021 14  ARG A N   
124  C CA  . ARG A 15  ? 0.1136 0.0913 0.0847 0.0059  -0.0324 -0.0018 14  ARG A CA  
125  C C   . ARG A 15  ? 0.1122 0.0901 0.0816 0.0050  -0.0319 -0.0016 14  ARG A C   
126  O O   . ARG A 15  ? 0.1333 0.1104 0.1014 0.0043  -0.0323 -0.0010 14  ARG A O   
127  C CB  . ARG A 15  ? 0.1109 0.0872 0.0824 0.0064  -0.0324 -0.0025 14  ARG A CB  
128  C CG  . ARG A 15  ? 0.1219 0.0981 0.0952 0.0074  -0.0329 -0.0029 14  ARG A CG  
129  C CD  . ARG A 15  ? 0.1164 0.0913 0.0901 0.0079  -0.0329 -0.0036 14  ARG A CD  
130  N NE  . ARG A 15  ? 0.1158 0.0905 0.0912 0.0088  -0.0333 -0.0040 14  ARG A NE  
131  C CZ  . ARG A 15  ? 0.1601 0.1337 0.1363 0.0094  -0.0335 -0.0046 14  ARG A CZ  
132  N NH1 . ARG A 15  ? 0.1457 0.1184 0.1211 0.0092  -0.0332 -0.0050 14  ARG A NH1 
133  N NH2 . ARG A 15  ? 0.1968 0.1702 0.1745 0.0101  -0.0339 -0.0049 14  ARG A NH2 
134  N N   . ILE A 16  ? 0.0981 0.0769 0.0674 0.0048  -0.0312 -0.0019 15  ILE A N   
135  C CA  . ILE A 16  ? 0.0814 0.0604 0.0491 0.0039  -0.0306 -0.0018 15  ILE A CA  
136  C C   . ILE A 16  ? 0.0939 0.0743 0.0610 0.0034  -0.0305 -0.0012 15  ILE A C   
137  O O   . ILE A 16  ? 0.1005 0.0808 0.0662 0.0026  -0.0302 -0.0009 15  ILE A O   
138  C CB  . ILE A 16  ? 0.0955 0.0746 0.0632 0.0040  -0.0298 -0.0025 15  ILE A CB  
139  C CG1 . ILE A 16  ? 0.0915 0.0722 0.0603 0.0044  -0.0293 -0.0027 15  ILE A CG1 
140  C CG2 . ILE A 16  ? 0.0814 0.0592 0.0498 0.0046  -0.0300 -0.0031 15  ILE A CG2 
141  C CD1 . ILE A 16  ? 0.1123 0.0932 0.0810 0.0043  -0.0285 -0.0034 15  ILE A CD1 
142  N N   . LYS A 17  ? 0.0889 0.0705 0.0571 0.0038  -0.0306 -0.0010 16  LYS A N   
143  C CA  . LYS A 17  ? 0.1246 0.1076 0.0923 0.0033  -0.0304 -0.0005 16  LYS A CA  
144  C C   . LYS A 17  ? 0.1240 0.1065 0.0905 0.0027  -0.0309 0.0002  16  LYS A C   
145  O O   . LYS A 17  ? 0.1487 0.1303 0.1154 0.0029  -0.0316 0.0005  16  LYS A O   
146  C CB  . LYS A 17  ? 0.1704 0.1547 0.1394 0.0038  -0.0305 -0.0005 16  LYS A CB  
147  C CG  . LYS A 17  ? 0.2140 0.1979 0.1840 0.0044  -0.0312 -0.0003 16  LYS A CG  
148  C CD  . LYS A 17  ? 0.2534 0.2385 0.2249 0.0050  -0.0311 -0.0004 16  LYS A CD  
149  C CE  . LYS A 17  ? 0.2509 0.2359 0.2233 0.0055  -0.0319 -0.0001 16  LYS A CE  
150  N NZ  . LYS A 17  ? 0.2919 0.2779 0.2657 0.0061  -0.0318 -0.0003 16  LYS A NZ  
151  N N   . LEU A 18  ? 0.1391 0.1224 0.1046 0.0020  -0.0306 0.0005  17  LEU A N   
152  C CA  . LEU A 18  ? 0.1674 0.1506 0.1318 0.0014  -0.0310 0.0013  17  LEU A CA  
153  C C   . LEU A 18  ? 0.1834 0.1684 0.1480 0.0013  -0.0308 0.0016  17  LEU A C   
154  O O   . LEU A 18  ? 0.2267 0.2128 0.1912 0.0011  -0.0301 0.0013  17  LEU A O   
155  C CB  . LEU A 18  ? 0.2067 0.1890 0.1695 0.0006  -0.0307 0.0014  17  LEU A CB  
156  C CG  . LEU A 18  ? 0.2185 0.2006 0.1801 0.0000  -0.0311 0.0021  17  LEU A CG  
157  C CD1 . LEU A 18  ? 0.2435 0.2244 0.2054 0.0003  -0.0319 0.0026  17  LEU A CD1 
158  C CD2 . LEU A 18  ? 0.2881 0.2695 0.2481 -0.0008 -0.0306 0.0022  17  LEU A CD2 
159  N N   . ALA A 19  ? 0.1633 0.1486 0.1283 0.0015  -0.0314 0.0021  18  ALA A N   
160  C CA  . ALA A 19  ? 0.1684 0.1554 0.1338 0.0016  -0.0313 0.0023  18  ALA A CA  
161  C C   . ALA A 19  ? 0.1729 0.1607 0.1371 0.0009  -0.0309 0.0025  18  ALA A C   
162  O O   . ALA A 19  ? 0.1838 0.1706 0.1466 0.0003  -0.0309 0.0028  18  ALA A O   
163  C CB  . ALA A 19  ? 0.2016 0.1887 0.1675 0.0019  -0.0321 0.0030  18  ALA A CB  
164  N N   . GLN A 20  ? 0.1813 0.1707 0.1459 0.0009  -0.0304 0.0023  19  GLN A N   
165  C CA  . GLN A 20  ? 0.1919 0.1822 0.1555 0.0004  -0.0300 0.0024  19  GLN A CA  
166  C C   . GLN A 20  ? 0.1856 0.1760 0.1484 0.0000  -0.0304 0.0031  19  GLN A C   
167  O O   . GLN A 20  ? 0.1816 0.1717 0.1448 0.0003  -0.0311 0.0036  19  GLN A O   
168  C CB  . GLN A 20  ? 0.1738 0.1655 0.1382 0.0006  -0.0296 0.0021  19  GLN A CB  
169  C CG  . GLN A 20  ? 0.1752 0.1676 0.1405 0.0010  -0.0302 0.0024  19  GLN A CG  
170  C CD  . GLN A 20  ? 0.1903 0.1835 0.1560 0.0012  -0.0301 0.0021  19  GLN A CD  
171  O OE1 . GLN A 20  ? 0.2371 0.2308 0.2021 0.0008  -0.0297 0.0020  19  GLN A OE1 
172  N NE2 . GLN A 20  ? 0.2183 0.2118 0.1853 0.0019  -0.0304 0.0020  19  GLN A NE2 
173  N N   . TYR A 21  ? 0.1890 0.1799 0.1508 -0.0005 -0.0301 0.0032  20  TYR A N   
174  C CA  . TYR A 21  ? 0.1719 0.1628 0.1327 -0.0009 -0.0305 0.0039  20  TYR A CA  
175  C C   . TYR A 21  ? 0.2284 0.2203 0.1901 -0.0004 -0.0310 0.0043  20  TYR A C   
176  O O   . TYR A 21  ? 0.2491 0.2404 0.2106 -0.0004 -0.0316 0.0049  20  TYR A O   
177  C CB  . TYR A 21  ? 0.1565 0.1481 0.1163 -0.0014 -0.0299 0.0038  20  TYR A CB  
178  C CG  . TYR A 21  ? 0.1683 0.1589 0.1269 -0.0020 -0.0295 0.0037  20  TYR A CG  
179  C CD1 . TYR A 21  ? 0.1801 0.1691 0.1376 -0.0025 -0.0298 0.0041  20  TYR A CD1 
180  C CD2 . TYR A 21  ? 0.1769 0.1682 0.1354 -0.0022 -0.0287 0.0031  20  TYR A CD2 
181  C CE1 . TYR A 21  ? 0.1996 0.1876 0.1559 -0.0031 -0.0294 0.0039  20  TYR A CE1 
182  C CE2 . TYR A 21  ? 0.1919 0.1823 0.1493 -0.0028 -0.0283 0.0029  20  TYR A CE2 
183  C CZ  . TYR A 21  ? 0.2125 0.2013 0.1688 -0.0033 -0.0286 0.0034  20  TYR A CZ  
184  O OH  . TYR A 21  ? 0.2198 0.2076 0.1749 -0.0039 -0.0281 0.0032  20  TYR A OH  
185  N N   . ASP A 22  ? 0.2572 0.2502 0.2198 -0.0001 -0.0309 0.0040  21  ASP A N   
186  C CA  . ASP A 22  ? 0.3115 0.3053 0.2748 0.0003  -0.0315 0.0043  21  ASP A CA  
187  C C   . ASP A 22  ? 0.3130 0.3064 0.2773 0.0008  -0.0319 0.0046  21  ASP A C   
188  O O   . ASP A 22  ? 0.3340 0.3278 0.2987 0.0011  -0.0325 0.0050  21  ASP A O   
189  C CB  . ASP A 22  ? 0.3609 0.3556 0.3249 0.0006  -0.0313 0.0039  21  ASP A CB  
190  C CG  . ASP A 22  ? 0.4051 0.4004 0.3682 0.0001  -0.0310 0.0038  21  ASP A CG  
191  O OD1 . ASP A 22  ? 0.4314 0.4266 0.3933 -0.0004 -0.0309 0.0041  21  ASP A OD1 
192  O OD2 . ASP A 22  ? 0.4438 0.4397 0.4073 0.0003  -0.0307 0.0034  21  ASP A OD2 
193  N N   . GLU A 23  ? 0.2708 0.2632 0.2356 0.0010  -0.0318 0.0043  22  GLU A N   
194  C CA  . GLU A 23  ? 0.2933 0.2849 0.2590 0.0015  -0.0324 0.0044  22  GLU A CA  
195  C C   . GLU A 23  ? 0.2670 0.2567 0.2317 0.0013  -0.0328 0.0047  22  GLU A C   
196  O O   . GLU A 23  ? 0.2882 0.2769 0.2536 0.0017  -0.0332 0.0047  22  GLU A O   
197  C CB  . GLU A 23  ? 0.2932 0.2848 0.2601 0.0021  -0.0321 0.0038  22  GLU A CB  
198  C CG  . GLU A 23  ? 0.3461 0.3389 0.3138 0.0023  -0.0320 0.0035  22  GLU A CG  
199  C CD  . GLU A 23  ? 0.3844 0.3769 0.3532 0.0029  -0.0318 0.0029  22  GLU A CD  
200  O OE1 . GLU A 23  ? 0.4266 0.4188 0.3965 0.0034  -0.0322 0.0029  22  GLU A OE1 
201  O OE2 . GLU A 23  ? 0.4070 0.3995 0.3756 0.0027  -0.0313 0.0024  22  GLU A OE2 
202  N N   . ASN A 24  ? 0.2485 0.2376 0.2117 0.0006  -0.0327 0.0049  23  ASN A N   
203  C CA  . ASN A 24  ? 0.2598 0.2471 0.2222 0.0002  -0.0330 0.0052  23  ASN A CA  
204  C C   . ASN A 24  ? 0.2882 0.2752 0.2492 -0.0004 -0.0332 0.0058  23  ASN A C   
205  O O   . ASN A 24  ? 0.2841 0.2713 0.2439 -0.0010 -0.0328 0.0058  23  ASN A O   
206  C CB  . ASN A 24  ? 0.2518 0.2383 0.2136 0.0000  -0.0324 0.0046  23  ASN A CB  
207  C CG  . ASN A 24  ? 0.2550 0.2396 0.2162 -0.0003 -0.0327 0.0047  23  ASN A CG  
208  O OD1 . ASN A 24  ? 0.2939 0.2776 0.2544 -0.0005 -0.0332 0.0053  23  ASN A OD1 
209  N ND2 . ASN A 24  ? 0.2299 0.2138 0.1913 -0.0001 -0.0323 0.0040  23  ASN A ND2 
210  N N   . GLN A 25  ? 0.3108 0.2974 0.2718 -0.0002 -0.0339 0.0065  24  GLN A N   
211  C CA  . GLN A 25  ? 0.3357 0.3220 0.2955 -0.0008 -0.0342 0.0072  24  GLN A CA  
212  C C   . GLN A 25  ? 0.3052 0.2899 0.2634 -0.0015 -0.0341 0.0073  24  GLN A C   
213  O O   . GLN A 25  ? 0.3043 0.2890 0.2612 -0.0022 -0.0339 0.0076  24  GLN A O   
214  C CB  . GLN A 25  ? 0.4032 0.3893 0.3635 -0.0005 -0.0349 0.0078  24  GLN A CB  
215  C CG  . GLN A 25  ? 0.4654 0.4511 0.4243 -0.0010 -0.0352 0.0085  24  GLN A CG  
216  C CD  . GLN A 25  ? 0.5281 0.5154 0.4875 -0.0008 -0.0354 0.0089  24  GLN A CD  
217  O OE1 . GLN A 25  ? 0.5525 0.5400 0.5128 -0.0003 -0.0360 0.0092  24  GLN A OE1 
218  N NE2 . GLN A 25  ? 0.5511 0.5395 0.5099 -0.0011 -0.0350 0.0088  24  GLN A NE2 
219  N N   . THR A 26  ? 0.3074 0.2907 0.2658 -0.0014 -0.0342 0.0071  25  THR A N   
220  C CA  . THR A 26  ? 0.3128 0.2945 0.2697 -0.0021 -0.0341 0.0072  25  THR A CA  
221  C C   . THR A 26  ? 0.3101 0.2922 0.2661 -0.0027 -0.0333 0.0068  25  THR A C   
222  O O   . THR A 26  ? 0.3235 0.3051 0.2780 -0.0034 -0.0331 0.0072  25  THR A O   
223  C CB  . THR A 26  ? 0.3575 0.3379 0.3150 -0.0018 -0.0342 0.0069  25  THR A CB  
224  O OG1 . THR A 26  ? 0.3821 0.3620 0.3404 -0.0014 -0.0350 0.0073  25  THR A OG1 
225  C CG2 . THR A 26  ? 0.3581 0.3368 0.3141 -0.0026 -0.0341 0.0070  25  THR A CG2 
226  N N   . LEU A 27  ? 0.2989 0.2820 0.2557 -0.0023 -0.0327 0.0061  26  LEU A N   
227  C CA  . LEU A 27  ? 0.2581 0.2417 0.2141 -0.0028 -0.0319 0.0057  26  LEU A CA  
228  C C   . LEU A 27  ? 0.2594 0.2441 0.2148 -0.0032 -0.0318 0.0060  26  LEU A C   
229  O O   . LEU A 27  ? 0.2515 0.2360 0.2056 -0.0038 -0.0314 0.0061  26  LEU A O   
230  C CB  . LEU A 27  ? 0.2314 0.2159 0.1885 -0.0024 -0.0314 0.0049  26  LEU A CB  
231  C CG  . LEU A 27  ? 0.2386 0.2220 0.1963 -0.0021 -0.0314 0.0044  26  LEU A CG  
232  C CD1 . LEU A 27  ? 0.2085 0.1930 0.1672 -0.0016 -0.0308 0.0037  26  LEU A CD1 
233  C CD2 . LEU A 27  ? 0.2474 0.2292 0.2037 -0.0027 -0.0312 0.0044  26  LEU A CD2 
234  N N   . ARG A 28  ? 0.2487 0.2347 0.2050 -0.0027 -0.0321 0.0062  27  ARG A N   
235  C CA  . ARG A 28  ? 0.2687 0.2558 0.2244 -0.0030 -0.0320 0.0066  27  ARG A CA  
236  C C   . ARG A 28  ? 0.3023 0.2883 0.2565 -0.0036 -0.0323 0.0073  27  ARG A C   
237  O O   . ARG A 28  ? 0.3247 0.3109 0.2778 -0.0042 -0.0320 0.0073  27  ARG A O   
238  C CB  . ARG A 28  ? 0.2879 0.2764 0.2448 -0.0023 -0.0324 0.0067  27  ARG A CB  
239  C CG  . ARG A 28  ? 0.3025 0.2924 0.2609 -0.0017 -0.0321 0.0061  27  ARG A CG  
240  C CD  . ARG A 28  ? 0.3087 0.3002 0.2678 -0.0013 -0.0323 0.0063  27  ARG A CD  
241  N NE  . ARG A 28  ? 0.3524 0.3436 0.3121 -0.0010 -0.0331 0.0068  27  ARG A NE  
242  C CZ  . ARG A 28  ? 0.3698 0.3609 0.3308 -0.0003 -0.0333 0.0067  27  ARG A CZ  
243  N NH1 . ARG A 28  ? 0.3468 0.3382 0.3087 0.0000  -0.0330 0.0061  27  ARG A NH1 
244  N NH2 . ARG A 28  ? 0.3767 0.3675 0.3381 0.0000  -0.0340 0.0072  27  ARG A NH2 
245  N N   . ASP A 29  ? 0.3174 0.3021 0.2715 -0.0036 -0.0330 0.0078  28  ASP A N   
246  C CA  . ASP A 29  ? 0.3270 0.3106 0.2797 -0.0043 -0.0333 0.0085  28  ASP A CA  
247  C C   . ASP A 29  ? 0.3265 0.3089 0.2777 -0.0050 -0.0328 0.0084  28  ASP A C   
248  O O   . ASP A 29  ? 0.3173 0.2995 0.2673 -0.0057 -0.0326 0.0087  28  ASP A O   
249  C CB  . ASP A 29  ? 0.3583 0.3408 0.3112 -0.0040 -0.0340 0.0090  28  ASP A CB  
250  C CG  . ASP A 29  ? 0.3784 0.3620 0.3325 -0.0033 -0.0346 0.0093  28  ASP A CG  
251  O OD1 . ASP A 29  ? 0.3821 0.3673 0.3366 -0.0032 -0.0344 0.0092  28  ASP A OD1 
252  O OD2 . ASP A 29  ? 0.4066 0.3896 0.3615 -0.0029 -0.0352 0.0096  28  ASP A OD2 
253  N N   . GLU A 30  ? 0.2973 0.2789 0.2488 -0.0050 -0.0325 0.0078  29  GLU A N   
254  C CA  . GLU A 30  ? 0.2913 0.2719 0.2416 -0.0057 -0.0319 0.0076  29  GLU A CA  
255  C C   . GLU A 30  ? 0.3121 0.2937 0.2618 -0.0060 -0.0312 0.0073  29  GLU A C   
256  O O   . GLU A 30  ? 0.3118 0.2930 0.2602 -0.0068 -0.0308 0.0075  29  GLU A O   
257  C CB  . GLU A 30  ? 0.3089 0.2885 0.2596 -0.0055 -0.0318 0.0071  29  GLU A CB  
258  C CG  . GLU A 30  ? 0.3258 0.3042 0.2769 -0.0052 -0.0325 0.0075  29  GLU A CG  
259  C CD  . GLU A 30  ? 0.3635 0.3411 0.3154 -0.0048 -0.0325 0.0069  29  GLU A CD  
260  O OE1 . GLU A 30  ? 0.3479 0.3264 0.3005 -0.0045 -0.0319 0.0062  29  GLU A OE1 
261  O OE2 . GLU A 30  ? 0.3731 0.3493 0.3250 -0.0047 -0.0330 0.0071  29  GLU A OE2 
262  N N   . ARG A 31  ? 0.2933 0.2766 0.2443 -0.0055 -0.0309 0.0068  30  ARG A N   
263  C CA  . ARG A 31  ? 0.2883 0.2727 0.2390 -0.0057 -0.0303 0.0064  30  ARG A CA  
264  C C   . ARG A 31  ? 0.3118 0.2966 0.2615 -0.0061 -0.0305 0.0070  30  ARG A C   
265  O O   . ARG A 31  ? 0.3476 0.3321 0.2961 -0.0068 -0.0300 0.0071  30  ARG A O   
266  C CB  . ARG A 31  ? 0.2986 0.2848 0.2508 -0.0050 -0.0301 0.0059  30  ARG A CB  
267  C CG  . ARG A 31  ? 0.2678 0.2554 0.2199 -0.0051 -0.0295 0.0055  30  ARG A CG  
268  C CD  . ARG A 31  ? 0.2629 0.2522 0.2163 -0.0044 -0.0296 0.0053  30  ARG A CD  
269  N NE  . ARG A 31  ? 0.2855 0.2752 0.2392 -0.0041 -0.0303 0.0059  30  ARG A NE  
270  C CZ  . ARG A 31  ? 0.2855 0.2763 0.2405 -0.0034 -0.0305 0.0058  30  ARG A CZ  
271  N NH1 . ARG A 31  ? 0.3006 0.2921 0.2567 -0.0030 -0.0302 0.0052  30  ARG A NH1 
272  N NH2 . ARG A 31  ? 0.3009 0.2920 0.2561 -0.0032 -0.0312 0.0064  30  ARG A NH2 
273  N N   . ASP A 32  ? 0.3268 0.3121 0.2770 -0.0057 -0.0311 0.0075  31  ASP A N   
274  C CA  . ASP A 32  ? 0.3187 0.3044 0.2681 -0.0060 -0.0313 0.0081  31  ASP A CA  
275  C C   . ASP A 32  ? 0.3281 0.3123 0.2759 -0.0068 -0.0314 0.0086  31  ASP A C   
276  O O   . ASP A 32  ? 0.3414 0.3258 0.2882 -0.0073 -0.0313 0.0089  31  ASP A O   
277  C CB  . ASP A 32  ? 0.3273 0.3139 0.2777 -0.0054 -0.0320 0.0084  31  ASP A CB  
278  C CG  . ASP A 32  ? 0.3356 0.3239 0.2873 -0.0047 -0.0318 0.0079  31  ASP A CG  
279  O OD1 . ASP A 32  ? 0.3614 0.3503 0.3133 -0.0048 -0.0312 0.0073  31  ASP A OD1 
280  O OD2 . ASP A 32  ? 0.3594 0.3483 0.3121 -0.0042 -0.0323 0.0081  31  ASP A OD2 
281  N N   . ALA A 33  ? 0.3186 0.3012 0.2661 -0.0070 -0.0317 0.0089  32  ALA A N   
282  C CA  . ALA A 33  ? 0.3389 0.3201 0.2849 -0.0078 -0.0317 0.0094  32  ALA A CA  
283  C C   . ALA A 33  ? 0.3770 0.3579 0.3219 -0.0085 -0.0309 0.0090  32  ALA A C   
284  O O   . ALA A 33  ? 0.4023 0.3829 0.3460 -0.0091 -0.0308 0.0094  32  ALA A O   
285  C CB  . ALA A 33  ? 0.3075 0.2871 0.2535 -0.0078 -0.0321 0.0096  32  ALA A CB  
286  N N   . VAL A 34  ? 0.3759 0.3570 0.3214 -0.0083 -0.0304 0.0083  33  VAL A N   
287  C CA  . VAL A 34  ? 0.3642 0.3453 0.3088 -0.0089 -0.0296 0.0079  33  VAL A CA  
288  C C   . VAL A 34  ? 0.3683 0.3507 0.3128 -0.0090 -0.0293 0.0079  33  VAL A C   
289  O O   . VAL A 34  ? 0.3846 0.3667 0.3279 -0.0097 -0.0289 0.0080  33  VAL A O   
290  C CB  . VAL A 34  ? 0.4002 0.3812 0.3455 -0.0087 -0.0290 0.0071  33  VAL A CB  
291  C CG1 . VAL A 34  ? 0.3904 0.3716 0.3350 -0.0092 -0.0282 0.0067  33  VAL A CG1 
292  C CG2 . VAL A 34  ? 0.3926 0.3720 0.3377 -0.0088 -0.0292 0.0072  33  VAL A CG2 
293  N N   . LEU A 35  ? 0.3495 0.3334 0.2951 -0.0083 -0.0296 0.0078  34  LEU A N   
294  C CA  . LEU A 35  ? 0.3322 0.3174 0.2777 -0.0083 -0.0293 0.0077  34  LEU A CA  
295  C C   . LEU A 35  ? 0.3571 0.3420 0.3014 -0.0088 -0.0297 0.0084  34  LEU A C   
296  O O   . LEU A 35  ? 0.3755 0.3607 0.3190 -0.0092 -0.0294 0.0085  34  LEU A O   
297  C CB  . LEU A 35  ? 0.3353 0.3221 0.2822 -0.0075 -0.0295 0.0074  34  LEU A CB  
298  C CG  . LEU A 35  ? 0.3091 0.2965 0.2572 -0.0070 -0.0291 0.0066  34  LEU A CG  
299  C CD1 . LEU A 35  ? 0.3151 0.3041 0.2647 -0.0061 -0.0294 0.0064  34  LEU A CD1 
300  C CD2 . LEU A 35  ? 0.3073 0.2952 0.2552 -0.0073 -0.0282 0.0060  34  LEU A CD2 
301  N N   . THR A 36  ? 0.3818 0.3662 0.3262 -0.0087 -0.0304 0.0091  35  THR A N   
302  C CA  . THR A 36  ? 0.3867 0.3707 0.3300 -0.0091 -0.0308 0.0098  35  THR A CA  
303  C C   . THR A 36  ? 0.3929 0.3755 0.3346 -0.0100 -0.0304 0.0100  35  THR A C   
304  O O   . THR A 36  ? 0.4067 0.3894 0.3474 -0.0106 -0.0304 0.0104  35  THR A O   
305  C CB  . THR A 36  ? 0.4163 0.3999 0.3599 -0.0088 -0.0316 0.0104  35  THR A CB  
306  O OG1 . THR A 36  ? 0.4808 0.4629 0.4244 -0.0089 -0.0317 0.0105  35  THR A OG1 
307  C CG2 . THR A 36  ? 0.3852 0.3702 0.3304 -0.0079 -0.0320 0.0103  35  THR A CG2 
308  N N   . ALA A 37  ? 0.3743 0.3557 0.3159 -0.0103 -0.0302 0.0099  36  ALA A N   
309  C CA  . ALA A 37  ? 0.3711 0.3512 0.3111 -0.0112 -0.0298 0.0100  36  ALA A CA  
310  C C   . ALA A 37  ? 0.3917 0.3725 0.3313 -0.0115 -0.0290 0.0096  36  ALA A C   
311  O O   . ALA A 37  ? 0.3941 0.3744 0.3325 -0.0123 -0.0288 0.0099  36  ALA A O   
312  C CB  . ALA A 37  ? 0.3562 0.3349 0.2962 -0.0113 -0.0296 0.0098  36  ALA A CB  
313  N N   . VAL A 38  ? 0.3860 0.3679 0.3267 -0.0111 -0.0286 0.0089  37  VAL A N   
314  C CA  . VAL A 38  ? 0.4157 0.3982 0.3560 -0.0114 -0.0279 0.0085  37  VAL A CA  
315  C C   . VAL A 38  ? 0.4240 0.4074 0.3638 -0.0115 -0.0281 0.0088  37  VAL A C   
316  O O   . VAL A 38  ? 0.4445 0.4277 0.3833 -0.0121 -0.0277 0.0089  37  VAL A O   
317  C CB  . VAL A 38  ? 0.4100 0.3935 0.3515 -0.0109 -0.0274 0.0076  37  VAL A CB  
318  C CG1 . VAL A 38  ? 0.4071 0.3897 0.3489 -0.0108 -0.0272 0.0072  37  VAL A CG1 
319  C CG2 . VAL A 38  ? 0.4195 0.4045 0.3622 -0.0101 -0.0278 0.0074  37  VAL A CG2 
320  N N   . ARG A 39  ? 0.4285 0.4128 0.3690 -0.0109 -0.0288 0.0091  38  ARG A N   
321  C CA  . ARG A 39  ? 0.4493 0.4344 0.3894 -0.0110 -0.0290 0.0094  38  ARG A CA  
322  C C   . ARG A 39  ? 0.4768 0.4608 0.4154 -0.0118 -0.0291 0.0101  38  ARG A C   
323  O O   . ARG A 39  ? 0.4599 0.4440 0.3975 -0.0123 -0.0289 0.0102  38  ARG A O   
324  C CB  . ARG A 39  ? 0.4577 0.4438 0.3988 -0.0102 -0.0296 0.0096  38  ARG A CB  
325  C CG  . ARG A 39  ? 0.4999 0.4874 0.4425 -0.0095 -0.0294 0.0089  38  ARG A CG  
326  C CD  . ARG A 39  ? 0.5308 0.5197 0.4741 -0.0089 -0.0299 0.0089  38  ARG A CD  
327  N NE  . ARG A 39  ? 0.5701 0.5600 0.5144 -0.0084 -0.0297 0.0083  38  ARG A NE  
328  C CZ  . ARG A 39  ? 0.6066 0.5969 0.5522 -0.0078 -0.0298 0.0079  38  ARG A CZ  
329  N NH1 . ARG A 39  ? 0.6149 0.6060 0.5613 -0.0075 -0.0296 0.0074  38  ARG A NH1 
330  N NH2 . ARG A 39  ? 0.6113 0.6012 0.5575 -0.0074 -0.0301 0.0082  38  ARG A NH2 
331  N N   . GLU A 40  ? 0.5490 0.5318 0.4872 -0.0119 -0.0296 0.0107  39  GLU A N   
332  C CA  . GLU A 40  ? 0.6425 0.6242 0.5793 -0.0127 -0.0297 0.0114  39  GLU A CA  
333  C C   . GLU A 40  ? 0.6387 0.6195 0.5743 -0.0135 -0.0290 0.0112  39  GLU A C   
334  O O   . GLU A 40  ? 0.6761 0.6568 0.6107 -0.0141 -0.0288 0.0114  39  GLU A O   
335  C CB  . GLU A 40  ? 0.7526 0.7331 0.6892 -0.0126 -0.0303 0.0119  39  GLU A CB  
336  C CG  . GLU A 40  ? 0.8495 0.8308 0.7873 -0.0118 -0.0310 0.0122  39  GLU A CG  
337  C CD  . GLU A 40  ? 0.9509 0.9310 0.8888 -0.0117 -0.0315 0.0126  39  GLU A CD  
338  O OE1 . GLU A 40  ? 1.0098 0.9887 0.9474 -0.0120 -0.0312 0.0124  39  GLU A OE1 
339  O OE2 . GLU A 40  ? 1.0030 0.9833 0.9413 -0.0113 -0.0322 0.0131  39  GLU A OE2 
340  N N   . GLY A 41  ? 0.6231 0.6034 0.5591 -0.0135 -0.0285 0.0107  40  GLY A N   
341  C CA  . GLY A 41  ? 0.6076 0.5871 0.5427 -0.0143 -0.0278 0.0104  40  GLY A CA  
342  C C   . GLY A 41  ? 0.5869 0.5672 0.5217 -0.0145 -0.0272 0.0100  40  GLY A C   
343  O O   . GLY A 41  ? 0.5895 0.5693 0.5233 -0.0152 -0.0268 0.0101  40  GLY A O   
344  N N   . LEU A 42  ? 0.5464 0.5282 0.4823 -0.0138 -0.0273 0.0096  41  LEU A N   
345  C CA  . LEU A 42  ? 0.5108 0.4935 0.4466 -0.0140 -0.0268 0.0093  41  LEU A CA  
346  C C   . LEU A 42  ? 0.5109 0.4938 0.4457 -0.0143 -0.0271 0.0098  41  LEU A C   
347  O O   . LEU A 42  ? 0.4681 0.4511 0.4022 -0.0149 -0.0267 0.0098  41  LEU A O   
348  C CB  . LEU A 42  ? 0.4952 0.4794 0.4324 -0.0132 -0.0268 0.0087  41  LEU A CB  
349  C CG  . LEU A 42  ? 0.4948 0.4793 0.4330 -0.0128 -0.0263 0.0079  41  LEU A CG  
350  C CD1 . LEU A 42  ? 0.4916 0.4775 0.4310 -0.0121 -0.0264 0.0075  41  LEU A CD1 
351  C CD2 . LEU A 42  ? 0.4855 0.4696 0.4230 -0.0134 -0.0255 0.0076  41  LEU A CD2 
352  N N   . LYS A 43  ? 0.5237 0.5068 0.4586 -0.0141 -0.0278 0.0104  42  LYS A N   
353  C CA  . LYS A 43  ? 0.5631 0.5461 0.4969 -0.0145 -0.0281 0.0110  42  LYS A CA  
354  C C   . LYS A 43  ? 0.6338 0.6156 0.5662 -0.0154 -0.0277 0.0113  42  LYS A C   
355  O O   . LYS A 43  ? 0.6362 0.6182 0.5678 -0.0159 -0.0274 0.0113  42  LYS A O   
356  C CB  . LYS A 43  ? 0.5335 0.5165 0.4675 -0.0141 -0.0290 0.0117  42  LYS A CB  
357  C CG  . LYS A 43  ? 0.5225 0.5070 0.4575 -0.0133 -0.0294 0.0116  42  LYS A CG  
358  C CD  . LYS A 43  ? 0.5254 0.5098 0.4605 -0.0130 -0.0302 0.0123  42  LYS A CD  
359  C CE  . LYS A 43  ? 0.5142 0.4981 0.4500 -0.0126 -0.0306 0.0123  42  LYS A CE  
360  N NZ  . LYS A 43  ? 0.5193 0.5037 0.4558 -0.0120 -0.0314 0.0128  42  LYS A NZ  
361  N N   . LYS A 44  ? 0.7293 0.7097 0.6614 -0.0157 -0.0277 0.0115  43  LYS A N   
362  C CA  . LYS A 44  ? 0.7485 0.7277 0.6792 -0.0166 -0.0273 0.0117  43  LYS A CA  
363  C C   . LYS A 44  ? 0.7107 0.6900 0.6412 -0.0170 -0.0264 0.0111  43  LYS A C   
364  O O   . LYS A 44  ? 0.7106 0.6896 0.6401 -0.0177 -0.0260 0.0113  43  LYS A O   
365  C CB  . LYS A 44  ? 0.8402 0.8180 0.7706 -0.0168 -0.0275 0.0121  43  LYS A CB  
366  C CG  . LYS A 44  ? 0.8894 0.8666 0.8203 -0.0168 -0.0270 0.0115  43  LYS A CG  
367  C CD  . LYS A 44  ? 0.9338 0.9095 0.8643 -0.0169 -0.0273 0.0119  43  LYS A CD  
368  C CE  . LYS A 44  ? 0.9525 0.9285 0.8836 -0.0163 -0.0282 0.0125  43  LYS A CE  
369  N NZ  . LYS A 44  ? 0.9598 0.9351 0.8897 -0.0168 -0.0286 0.0134  43  LYS A NZ  
370  N N   . VAL A 45  ? 0.6531 0.6328 0.5846 -0.0166 -0.0261 0.0104  44  VAL A N   
371  C CA  . VAL A 45  ? 0.5925 0.5722 0.5239 -0.0170 -0.0252 0.0098  44  VAL A CA  
372  C C   . VAL A 45  ? 0.5851 0.5658 0.5163 -0.0171 -0.0250 0.0097  44  VAL A C   
373  O O   . VAL A 45  ? 0.5703 0.5506 0.5007 -0.0178 -0.0244 0.0096  44  VAL A O   
374  C CB  . VAL A 45  ? 0.5472 0.5273 0.4799 -0.0164 -0.0249 0.0091  44  VAL A CB  
375  C CG1 . VAL A 45  ? 0.5228 0.5032 0.4556 -0.0166 -0.0241 0.0084  44  VAL A CG1 
376  C CG2 . VAL A 45  ? 0.5314 0.5102 0.4641 -0.0164 -0.0250 0.0091  44  VAL A CG2 
377  N N   . PHE A 46  ? 0.5823 0.5642 0.5142 -0.0165 -0.0255 0.0097  45  PHE A N   
378  C CA  . PHE A 46  ? 0.5888 0.5716 0.5205 -0.0167 -0.0253 0.0095  45  PHE A CA  
379  C C   . PHE A 46  ? 0.6307 0.6135 0.5613 -0.0171 -0.0256 0.0101  45  PHE A C   
380  O O   . PHE A 46  ? 0.6231 0.6059 0.5529 -0.0177 -0.0253 0.0101  45  PHE A O   
381  C CB  . PHE A 46  ? 0.5455 0.5294 0.4782 -0.0161 -0.0256 0.0092  45  PHE A CB  
382  C CG  . PHE A 46  ? 0.5166 0.5007 0.4500 -0.0160 -0.0251 0.0085  45  PHE A CG  
383  C CD1 . PHE A 46  ? 0.5031 0.4868 0.4373 -0.0156 -0.0248 0.0081  45  PHE A CD1 
384  C CD2 . PHE A 46  ? 0.5058 0.4904 0.4391 -0.0163 -0.0248 0.0081  45  PHE A CD2 
385  C CE1 . PHE A 46  ? 0.4835 0.4674 0.4183 -0.0155 -0.0244 0.0075  45  PHE A CE1 
386  C CE2 . PHE A 46  ? 0.4820 0.4666 0.4159 -0.0162 -0.0243 0.0075  45  PHE A CE2 
387  C CZ  . PHE A 46  ? 0.4931 0.4774 0.4277 -0.0158 -0.0241 0.0072  45  PHE A CZ  
388  N N   . ALA A 47  ? 0.6821 0.6644 0.6123 -0.0171 -0.0262 0.0108  46  ALA A N   
389  C CA  . ALA A 47  ? 0.7513 0.7333 0.6802 -0.0176 -0.0263 0.0114  46  ALA A CA  
390  C C   . ALA A 47  ? 0.8207 0.8017 0.7485 -0.0185 -0.0257 0.0114  46  ALA A C   
391  O O   . ALA A 47  ? 0.8207 0.8017 0.7475 -0.0190 -0.0256 0.0116  46  ALA A O   
392  C CB  . ALA A 47  ? 0.7563 0.7377 0.6848 -0.0175 -0.0271 0.0122  46  ALA A CB  
393  N N   . ASP A 48  ? 0.8868 0.8670 0.8147 -0.0187 -0.0252 0.0110  47  ASP A N   
394  C CA  . ASP A 48  ? 0.9496 0.9288 0.8766 -0.0195 -0.0245 0.0110  47  ASP A CA  
395  C C   . ASP A 48  ? 0.9399 0.9197 0.8671 -0.0197 -0.0238 0.0103  47  ASP A C   
396  O O   . ASP A 48  ? 0.9532 0.9322 0.8796 -0.0204 -0.0233 0.0102  47  ASP A O   
397  C CB  . ASP A 48  ? 1.0236 1.0016 0.9507 -0.0196 -0.0243 0.0108  47  ASP A CB  
398  C CG  . ASP A 48  ? 1.0847 1.0613 1.0105 -0.0204 -0.0242 0.0114  47  ASP A CG  
399  O OD1 . ASP A 48  ? 1.1059 1.0824 1.0307 -0.0209 -0.0243 0.0118  47  ASP A OD1 
400  O OD2 . ASP A 48  ? 1.1056 1.0811 1.0314 -0.0205 -0.0241 0.0113  47  ASP A OD2 
401  N N   . ARG A 49  ? 0.9016 0.8825 0.8296 -0.0192 -0.0239 0.0099  48  ARG A N   
402  C CA  . ARG A 49  ? 0.8478 0.8289 0.7757 -0.0197 -0.0235 0.0094  48  ARG A CA  
403  C C   . ARG A 49  ? 0.7580 0.7399 0.6855 -0.0199 -0.0238 0.0096  48  ARG A C   
404  O O   . ARG A 49  ? 0.7401 0.7223 0.6675 -0.0203 -0.0234 0.0092  48  ARG A O   
405  C CB  . ARG A 49  ? 0.8782 0.8597 0.8073 -0.0192 -0.0233 0.0088  48  ARG A CB  
406  C CG  . ARG A 49  ? 0.8997 0.8806 0.8294 -0.0189 -0.0230 0.0086  48  ARG A CG  
407  C CD  . ARG A 49  ? 0.9107 0.8922 0.8418 -0.0182 -0.0230 0.0081  48  ARG A CD  
408  N NE  . ARG A 49  ? 0.9102 0.8918 0.8416 -0.0184 -0.0225 0.0074  48  ARG A NE  
409  C CZ  . ARG A 49  ? 0.9015 0.8825 0.8331 -0.0184 -0.0219 0.0070  48  ARG A CZ  
410  N NH1 . ARG A 49  ? 0.8958 0.8760 0.8274 -0.0184 -0.0218 0.0072  48  ARG A NH1 
411  N NH2 . ARG A 49  ? 0.8973 0.8785 0.8293 -0.0186 -0.0214 0.0065  48  ARG A NH2 
412  N N   . GLY A 50  ? 0.6829 0.6651 0.6101 -0.0197 -0.0244 0.0102  49  GLY A N   
413  C CA  . GLY A 50  ? 0.6199 0.6029 0.5468 -0.0198 -0.0248 0.0103  49  GLY A CA  
414  C C   . GLY A 50  ? 0.5747 0.5587 0.5026 -0.0192 -0.0251 0.0100  49  GLY A C   
415  O O   . GLY A 50  ? 0.5529 0.5376 0.4807 -0.0194 -0.0253 0.0099  49  GLY A O   
416  N N   . GLU A 51  ? 0.5376 0.5218 0.4666 -0.0185 -0.0252 0.0096  50  GLU A N   
417  C CA  . GLU A 51  ? 0.5379 0.5231 0.4680 -0.0180 -0.0254 0.0092  50  GLU A CA  
418  C C   . GLU A 51  ? 0.4531 0.4387 0.3841 -0.0171 -0.0260 0.0095  50  GLU A C   
419  O O   . GLU A 51  ? 0.3883 0.3733 0.3193 -0.0169 -0.0262 0.0097  50  GLU A O   
420  C CB  . GLU A 51  ? 0.6033 0.5883 0.5341 -0.0180 -0.0247 0.0086  50  GLU A CB  
421  C CG  . GLU A 51  ? 0.6758 0.6602 0.6059 -0.0188 -0.0240 0.0083  50  GLU A CG  
422  C CD  . GLU A 51  ? 0.7315 0.7157 0.6622 -0.0187 -0.0234 0.0077  50  GLU A CD  
423  O OE1 . GLU A 51  ? 0.7549 0.7395 0.6858 -0.0190 -0.0230 0.0073  50  GLU A OE1 
424  O OE2 . GLU A 51  ? 0.7532 0.7368 0.6842 -0.0185 -0.0232 0.0076  50  GLU A OE2 
425  N N   . ALA A 52  ? 0.4380 0.4247 0.3697 -0.0166 -0.0264 0.0093  51  ALA A N   
426  C CA  . ALA A 52  ? 0.4334 0.4205 0.3661 -0.0158 -0.0270 0.0094  51  ALA A CA  
427  C C   . ALA A 52  ? 0.4480 0.4350 0.3817 -0.0153 -0.0267 0.0090  51  ALA A C   
428  O O   . ALA A 52  ? 0.4230 0.4099 0.3569 -0.0155 -0.0262 0.0084  51  ALA A O   
429  C CB  . ALA A 52  ? 0.4618 0.4501 0.3951 -0.0154 -0.0275 0.0093  51  ALA A CB  
430  N N   . ALA A 53  ? 0.4272 0.4140 0.3614 -0.0148 -0.0271 0.0092  52  ALA A N   
431  C CA  . ALA A 53  ? 0.4512 0.4378 0.3864 -0.0143 -0.0269 0.0088  52  ALA A CA  
432  C C   . ALA A 53  ? 0.4408 0.4284 0.3771 -0.0138 -0.0269 0.0083  52  ALA A C   
433  O O   . ALA A 53  ? 0.3979 0.3863 0.3345 -0.0135 -0.0274 0.0084  52  ALA A O   
434  C CB  . ALA A 53  ? 0.4326 0.4190 0.3682 -0.0138 -0.0273 0.0093  52  ALA A CB  
435  N N   . PRO A 54  ? 0.4635 0.4510 0.4005 -0.0136 -0.0265 0.0077  53  PRO A N   
436  C CA  . PRO A 54  ? 0.4872 0.4755 0.4252 -0.0130 -0.0265 0.0073  53  PRO A CA  
437  C C   . PRO A 54  ? 0.4757 0.4645 0.4148 -0.0122 -0.0271 0.0074  53  PRO A C   
438  O O   . PRO A 54  ? 0.4960 0.4843 0.4352 -0.0120 -0.0272 0.0076  53  PRO A O   
439  C CB  . PRO A 54  ? 0.4860 0.4740 0.4244 -0.0132 -0.0258 0.0067  53  PRO A CB  
440  C CG  . PRO A 54  ? 0.4874 0.4742 0.4252 -0.0135 -0.0255 0.0069  53  PRO A CG  
441  C CD  . PRO A 54  ? 0.4746 0.4612 0.4113 -0.0140 -0.0258 0.0075  53  PRO A CD  
442  N N   . THR A 55  ? 0.4634 0.4532 0.4034 -0.0117 -0.0274 0.0071  54  THR A N   
443  C CA  . THR A 55  ? 0.4491 0.4394 0.3902 -0.0109 -0.0279 0.0072  54  THR A CA  
444  C C   . THR A 55  ? 0.4015 0.3920 0.3437 -0.0104 -0.0275 0.0065  54  THR A C   
445  O O   . THR A 55  ? 0.3790 0.3694 0.3210 -0.0107 -0.0269 0.0060  54  THR A O   
446  C CB  . THR A 55  ? 0.4761 0.4675 0.4176 -0.0105 -0.0285 0.0073  54  THR A CB  
447  O OG1 . THR A 55  ? 0.4930 0.4850 0.4344 -0.0107 -0.0282 0.0069  54  THR A OG1 
448  C CG2 . THR A 55  ? 0.4965 0.4877 0.4372 -0.0107 -0.0290 0.0080  54  THR A CG2 
449  N N   . PHE A 56  ? 0.3717 0.3624 0.3149 -0.0098 -0.0278 0.0065  55  PHE A N   
450  C CA  . PHE A 56  ? 0.3526 0.3435 0.2968 -0.0093 -0.0275 0.0059  55  PHE A CA  
451  C C   . PHE A 56  ? 0.3436 0.3354 0.2891 -0.0085 -0.0281 0.0059  55  PHE A C   
452  O O   . PHE A 56  ? 0.3207 0.3125 0.2662 -0.0083 -0.0286 0.0064  55  PHE A O   
453  C CB  . PHE A 56  ? 0.3280 0.3179 0.2721 -0.0095 -0.0271 0.0057  55  PHE A CB  
454  C CG  . PHE A 56  ? 0.3495 0.3389 0.2938 -0.0092 -0.0274 0.0062  55  PHE A CG  
455  C CD1 . PHE A 56  ? 0.3487 0.3385 0.2942 -0.0085 -0.0277 0.0060  55  PHE A CD1 
456  C CD2 . PHE A 56  ? 0.3556 0.3442 0.2989 -0.0097 -0.0275 0.0067  55  PHE A CD2 
457  C CE1 . PHE A 56  ? 0.3502 0.3395 0.2959 -0.0083 -0.0281 0.0064  55  PHE A CE1 
458  C CE2 . PHE A 56  ? 0.3671 0.3553 0.3105 -0.0095 -0.0278 0.0071  55  PHE A CE2 
459  C CZ  . PHE A 56  ? 0.3607 0.3493 0.3054 -0.0088 -0.0281 0.0070  55  PHE A CZ  
460  N N   . THR A 57  ? 0.3459 0.3383 0.2923 -0.0081 -0.0279 0.0053  56  THR A N   
461  C CA  . THR A 57  ? 0.3324 0.3255 0.2801 -0.0073 -0.0282 0.0052  56  THR A CA  
462  C C   . THR A 57  ? 0.2971 0.2897 0.2455 -0.0070 -0.0279 0.0049  56  THR A C   
463  O O   . THR A 57  ? 0.2989 0.2914 0.2474 -0.0072 -0.0273 0.0044  56  THR A O   
464  C CB  . THR A 57  ? 0.3695 0.3637 0.3179 -0.0070 -0.0283 0.0048  56  THR A CB  
465  O OG1 . THR A 57  ? 0.3977 0.3923 0.3453 -0.0073 -0.0285 0.0051  56  THR A OG1 
466  C CG2 . THR A 57  ? 0.3945 0.3895 0.3442 -0.0062 -0.0287 0.0048  56  THR A CG2 
467  N N   . PRO A 58  ? 0.2844 0.2769 0.2335 -0.0066 -0.0283 0.0051  57  PRO A N   
468  C CA  . PRO A 58  ? 0.2434 0.2355 0.1933 -0.0063 -0.0280 0.0047  57  PRO A CA  
469  C C   . PRO A 58  ? 0.2362 0.2293 0.1875 -0.0056 -0.0281 0.0043  57  PRO A C   
470  O O   . PRO A 58  ? 0.2174 0.2113 0.1692 -0.0052 -0.0285 0.0044  57  PRO A O   
471  C CB  . PRO A 58  ? 0.2815 0.2730 0.2314 -0.0062 -0.0284 0.0052  57  PRO A CB  
472  C CG  . PRO A 58  ? 0.2930 0.2850 0.2428 -0.0060 -0.0291 0.0058  57  PRO A CG  
473  C CD  . PRO A 58  ? 0.3086 0.3012 0.2578 -0.0063 -0.0290 0.0057  57  PRO A CD  
474  N N   . PHE A 59  ? 0.2331 0.2258 0.1849 -0.0054 -0.0277 0.0038  58  PHE A N   
475  C CA  . PHE A 59  ? 0.2086 0.2021 0.1619 -0.0047 -0.0278 0.0034  58  PHE A CA  
476  C C   . PHE A 59  ? 0.2119 0.2047 0.1657 -0.0045 -0.0276 0.0032  58  PHE A C   
477  O O   . PHE A 59  ? 0.2036 0.1956 0.1568 -0.0049 -0.0271 0.0031  58  PHE A O   
478  C CB  . PHE A 59  ? 0.1907 0.1850 0.1441 -0.0047 -0.0275 0.0029  58  PHE A CB  
479  C CG  . PHE A 59  ? 0.2049 0.1987 0.1578 -0.0051 -0.0267 0.0025  58  PHE A CG  
480  C CD1 . PHE A 59  ? 0.2142 0.2076 0.1659 -0.0057 -0.0265 0.0026  58  PHE A CD1 
481  C CD2 . PHE A 59  ? 0.2106 0.2044 0.1643 -0.0048 -0.0263 0.0019  58  PHE A CD2 
482  C CE1 . PHE A 59  ? 0.2171 0.2101 0.1684 -0.0061 -0.0258 0.0021  58  PHE A CE1 
483  C CE2 . PHE A 59  ? 0.2001 0.1934 0.1533 -0.0051 -0.0257 0.0015  58  PHE A CE2 
484  C CZ  . PHE A 59  ? 0.2128 0.2057 0.1648 -0.0058 -0.0254 0.0016  58  PHE A CZ  
485  N N   . ASN A 60  ? 0.1888 0.1821 0.1439 -0.0039 -0.0279 0.0031  59  ASN A N   
486  C CA  . ASN A 60  ? 0.1546 0.1472 0.1102 -0.0036 -0.0277 0.0028  59  ASN A CA  
487  C C   . ASN A 60  ? 0.1547 0.1472 0.1105 -0.0037 -0.0271 0.0021  59  ASN A C   
488  O O   . ASN A 60  ? 0.1658 0.1591 0.1219 -0.0036 -0.0269 0.0018  59  ASN A O   
489  C CB  . ASN A 60  ? 0.1830 0.1760 0.1399 -0.0030 -0.0282 0.0029  59  ASN A CB  
490  C CG  . ASN A 60  ? 0.2270 0.2199 0.1838 -0.0029 -0.0289 0.0036  59  ASN A CG  
491  O OD1 . ASN A 60  ? 0.2688 0.2611 0.2246 -0.0033 -0.0289 0.0040  59  ASN A OD1 
492  N ND2 . ASN A 60  ? 0.2702 0.2637 0.2281 -0.0024 -0.0294 0.0038  59  ASN A ND2 
493  N N   . GLN A 61  ? 0.1557 0.1473 0.1114 -0.0038 -0.0267 0.0019  60  GLN A N   
494  C CA  . GLN A 61  ? 0.1615 0.1530 0.1175 -0.0038 -0.0261 0.0013  60  GLN A CA  
495  C C   . GLN A 61  ? 0.1244 0.1153 0.0812 -0.0034 -0.0260 0.0010  60  GLN A C   
496  O O   . GLN A 61  ? 0.1346 0.1252 0.0917 -0.0032 -0.0265 0.0014  60  GLN A O   
497  C CB  . GLN A 61  ? 0.2035 0.1945 0.1583 -0.0044 -0.0255 0.0011  60  GLN A CB  
498  C CG  . GLN A 61  ? 0.2340 0.2255 0.1881 -0.0048 -0.0254 0.0012  60  GLN A CG  
499  C CD  . GLN A 61  ? 0.2445 0.2355 0.1977 -0.0053 -0.0247 0.0009  60  GLN A CD  
500  O OE1 . GLN A 61  ? 0.3135 0.3042 0.2656 -0.0059 -0.0246 0.0012  60  GLN A OE1 
501  N NE2 . GLN A 61  ? 0.2231 0.2141 0.1768 -0.0052 -0.0242 0.0003  60  GLN A NE2 
502  N N   . GLY A 62  ? 0.1265 0.1174 0.0837 -0.0033 -0.0255 0.0004  61  GLY A N   
503  C CA  . GLY A 62  ? 0.1068 0.0970 0.0645 -0.0031 -0.0254 0.0001  61  GLY A CA  
504  C C   . GLY A 62  ? 0.1332 0.1236 0.0922 -0.0024 -0.0258 0.0001  61  GLY A C   
505  O O   . GLY A 62  ? 0.1382 0.1294 0.0978 -0.0020 -0.0262 0.0003  61  GLY A O   
506  N N   . SER A 63  ? 0.1197 0.1093 0.0792 -0.0022 -0.0258 0.0000  62  SER A N   
507  C CA  . SER A 63  ? 0.1191 0.1087 0.0798 -0.0015 -0.0262 -0.0001 62  SER A CA  
508  C C   . SER A 63  ? 0.1640 0.1540 0.1252 -0.0012 -0.0269 0.0004  62  SER A C   
509  O O   . SER A 63  ? 0.1402 0.1306 0.1025 -0.0007 -0.0273 0.0004  62  SER A O   
510  C CB  . SER A 63  ? 0.1396 0.1280 0.1005 -0.0014 -0.0261 -0.0004 62  SER A CB  
511  O OG  . SER A 63  ? 0.1472 0.1342 0.1071 -0.0017 -0.0266 0.0000  62  SER A OG  
512  N N   . TYR A 64  ? 0.1477 0.1372 0.1079 -0.0016 -0.0273 0.0010  63  TYR A N   
513  C CA  . TYR A 64  ? 0.1630 0.1527 0.1235 -0.0014 -0.0280 0.0016  63  TYR A CA  
514  C C   . TYR A 64  ? 0.1657 0.1569 0.1265 -0.0013 -0.0281 0.0017  63  TYR A C   
515  O O   . TYR A 64  ? 0.1966 0.1881 0.1579 -0.0010 -0.0286 0.0021  63  TYR A O   
516  C CB  . TYR A 64  ? 0.2036 0.1919 0.1628 -0.0018 -0.0285 0.0021  63  TYR A CB  
517  C CG  . TYR A 64  ? 0.2981 0.2846 0.2570 -0.0019 -0.0286 0.0020  63  TYR A CG  
518  C CD1 . TYR A 64  ? 0.3982 0.3843 0.3582 -0.0013 -0.0287 0.0016  63  TYR A CD1 
519  C CD2 . TYR A 64  ? 0.3685 0.3538 0.3260 -0.0026 -0.0285 0.0022  63  TYR A CD2 
520  C CE1 . TYR A 64  ? 0.4261 0.4106 0.3858 -0.0014 -0.0288 0.0014  63  TYR A CE1 
521  C CE2 . TYR A 64  ? 0.4291 0.4126 0.3861 -0.0027 -0.0286 0.0021  63  TYR A CE2 
522  C CZ  . TYR A 64  ? 0.4782 0.4614 0.4363 -0.0021 -0.0287 0.0016  63  TYR A CZ  
523  O OH  . TYR A 64  ? 0.6054 0.5869 0.5631 -0.0021 -0.0288 0.0015  63  TYR A OH  
524  N N   . ALA A 65  ? 0.1424 0.1340 0.1026 -0.0016 -0.0276 0.0014  64  ALA A N   
525  C CA  . ALA A 65  ? 0.1649 0.1575 0.1253 -0.0015 -0.0278 0.0015  64  ALA A CA  
526  C C   . ALA A 65  ? 0.1546 0.1477 0.1162 -0.0010 -0.0277 0.0010  64  ALA A C   
527  O O   . ALA A 65  ? 0.2036 0.1976 0.1659 -0.0007 -0.0280 0.0011  64  ALA A O   
528  C CB  . ALA A 65  ? 0.1643 0.1573 0.1236 -0.0021 -0.0273 0.0014  64  ALA A CB  
529  N N   . MET A 66  ? 0.1242 0.1169 0.0861 -0.0009 -0.0272 0.0005  65  MET A N   
530  C CA  . MET A 66  ? 0.1317 0.1246 0.0945 -0.0004 -0.0270 0.0000  65  MET A CA  
531  C C   . MET A 66  ? 0.1414 0.1339 0.1054 0.0002  -0.0274 0.0000  65  MET A C   
532  O O   . MET A 66  ? 0.1214 0.1140 0.0863 0.0006  -0.0272 -0.0005 65  MET A O   
533  C CB  . MET A 66  ? 0.1207 0.1133 0.0832 -0.0007 -0.0263 -0.0005 65  MET A CB  
534  C CG  . MET A 66  ? 0.1536 0.1466 0.1150 -0.0013 -0.0259 -0.0006 65  MET A CG  
535  S SD  . MET A 66  ? 0.1545 0.1473 0.1155 -0.0015 -0.0250 -0.0012 65  MET A SD  
536  C CE  . MET A 66  ? 0.1906 0.1821 0.1511 -0.0018 -0.0248 -0.0013 65  MET A CE  
537  N N   . ASN A 67  ? 0.1029 0.1738 0.1079 -0.0306 0.0125  -0.0428 66  ASN A N   
538  C CA  . ASN A 67  ? 0.0757 0.1443 0.0790 -0.0307 0.0123  -0.0412 66  ASN A CA  
539  C C   . ASN A 67  ? 0.1027 0.1708 0.1072 -0.0306 0.0128  -0.0412 66  ASN A C   
540  O O   . ASN A 67  ? 0.1116 0.1774 0.1155 -0.0302 0.0126  -0.0401 66  ASN A O   
541  C CB  . ASN A 67  ? 0.0835 0.1496 0.0855 -0.0301 0.0115  -0.0398 66  ASN A CB  
542  C CG  . ASN A 67  ? 0.1108 0.1748 0.1105 -0.0305 0.0111  -0.0380 66  ASN A CG  
543  O OD1 . ASN A 67  ? 0.1242 0.1887 0.1230 -0.0313 0.0114  -0.0378 66  ASN A OD1 
544  N ND2 . ASN A 67  ? 0.1284 0.1900 0.1272 -0.0299 0.0106  -0.0369 66  ASN A ND2 
545  N N   . THR A 68  ? 0.1001 0.1703 0.1062 -0.0309 0.0135  -0.0426 67  THR A N   
546  C CA  . THR A 68  ? 0.0761 0.1462 0.0833 -0.0309 0.0140  -0.0427 67  THR A CA  
547  C C   . THR A 68  ? 0.1061 0.1776 0.1128 -0.0319 0.0145  -0.0430 67  THR A C   
548  O O   . THR A 68  ? 0.0983 0.1706 0.1063 -0.0320 0.0151  -0.0436 67  THR A O   
549  C CB  . THR A 68  ? 0.0738 0.1451 0.0837 -0.0302 0.0145  -0.0442 67  THR A CB  
550  O OG1 . THR A 68  ? 0.0766 0.1504 0.0874 -0.0305 0.0148  -0.0457 67  THR A OG1 
551  C CG2 . THR A 68  ? 0.1115 0.1811 0.1219 -0.0292 0.0140  -0.0439 67  THR A CG2 
552  N N   . GLY A 69  ? 0.1151 0.1869 0.1199 -0.0327 0.0142  -0.0424 68  GLY A N   
553  C CA  . GLY A 69  ? 0.0950 0.1683 0.0994 -0.0336 0.0146  -0.0427 68  GLY A CA  
554  C C   . GLY A 69  ? 0.0806 0.1525 0.0838 -0.0341 0.0147  -0.0414 68  GLY A C   
555  O O   . GLY A 69  ? 0.0865 0.1560 0.0882 -0.0339 0.0142  -0.0399 68  GLY A O   
556  N N   . VAL A 70  ? 0.0662 0.1397 0.0701 -0.0348 0.0153  -0.0421 69  VAL A N   
557  C CA  . VAL A 70  ? 0.0785 0.1509 0.0812 -0.0354 0.0155  -0.0410 69  VAL A CA  
558  C C   . VAL A 70  ? 0.0749 0.1489 0.0766 -0.0365 0.0156  -0.0412 69  VAL A C   
559  O O   . VAL A 70  ? 0.1366 0.2131 0.1393 -0.0368 0.0159  -0.0425 69  VAL A O   
560  C CB  . VAL A 70  ? 0.1137 0.1861 0.1181 -0.0351 0.0161  -0.0415 69  VAL A CB  
561  C CG1 . VAL A 70  ? 0.1019 0.1722 0.1069 -0.0340 0.0159  -0.0410 69  VAL A CG1 
562  C CG2 . VAL A 70  ? 0.0937 0.1689 0.1002 -0.0352 0.0168  -0.0433 69  VAL A CG2 
563  N N   . LYS A 71  ? 0.0999 0.1726 0.0999 -0.0371 0.0155  -0.0398 70  LYS A N   
564  C CA  . LYS A 71  ? 0.0922 0.1663 0.0914 -0.0382 0.0157  -0.0399 70  LYS A CA  
565  C C   . LYS A 71  ? 0.0986 0.1743 0.0994 -0.0385 0.0165  -0.0410 70  LYS A C   
566  O O   . LYS A 71  ? 0.1108 0.1857 0.1126 -0.0381 0.0168  -0.0409 70  LYS A O   
567  C CB  . LYS A 71  ? 0.1001 0.1721 0.0969 -0.0387 0.0153  -0.0381 70  LYS A CB  
568  C CG  . LYS A 71  ? 0.0935 0.1639 0.0884 -0.0385 0.0145  -0.0370 70  LYS A CG  
569  C CD  . LYS A 71  ? 0.1317 0.1996 0.1246 -0.0389 0.0141  -0.0352 70  LYS A CD  
570  C CE  . LYS A 71  ? 0.1633 0.2301 0.1541 -0.0389 0.0133  -0.0342 70  LYS A CE  
571  N NZ  . LYS A 71  ? 0.1584 0.2227 0.1472 -0.0392 0.0129  -0.0324 70  LYS A NZ  
572  N N   . PRO A 72  ? 0.1025 0.1807 0.1038 -0.0392 0.0168  -0.0421 71  PRO A N   
573  C CA  . PRO A 72  ? 0.1157 0.1956 0.1184 -0.0395 0.0176  -0.0430 71  PRO A CA  
574  C C   . PRO A 72  ? 0.1195 0.1982 0.1210 -0.0402 0.0176  -0.0419 71  PRO A C   
575  O O   . PRO A 72  ? 0.1430 0.2204 0.1425 -0.0407 0.0172  -0.0405 71  PRO A O   
576  C CB  . PRO A 72  ? 0.1261 0.2088 0.1293 -0.0402 0.0178  -0.0443 71  PRO A CB  
577  C CG  . PRO A 72  ? 0.1494 0.2314 0.1505 -0.0405 0.0171  -0.0434 71  PRO A CG  
578  C CD  . PRO A 72  ? 0.1361 0.2155 0.1363 -0.0397 0.0165  -0.0423 71  PRO A CD  
579  N N   . LEU A 73  ? 0.1449 0.2230 0.1472 -0.0398 0.0178  -0.0422 72  LEU A N   
580  C CA  . LEU A 73  ? 0.1671 0.2442 0.1683 -0.0404 0.0178  -0.0413 72  LEU A CA  
581  C C   . LEU A 73  ? 0.1750 0.2542 0.1755 -0.0415 0.0180  -0.0417 72  LEU A C   
582  O O   . LEU A 73  ? 0.1705 0.2520 0.1717 -0.0418 0.0182  -0.0429 72  LEU A O   
583  C CB  . LEU A 73  ? 0.1844 0.2607 0.1868 -0.0397 0.0181  -0.0418 72  LEU A CB  
584  C CG  . LEU A 73  ? 0.1930 0.2671 0.1959 -0.0386 0.0179  -0.0413 72  LEU A CG  
585  C CD1 . LEU A 73  ? 0.2183 0.2920 0.2227 -0.0378 0.0181  -0.0420 72  LEU A CD1 
586  C CD2 . LEU A 73  ? 0.1810 0.2526 0.1821 -0.0387 0.0175  -0.0394 72  LEU A CD2 
587  N N   . GLU A 74  ? 0.2390 0.3172 0.2380 -0.0422 0.0179  -0.0407 73  GLU A N   
588  C CA  . GLU A 74  ? 0.3328 0.4129 0.3312 -0.0434 0.0181  -0.0410 73  GLU A CA  
589  C C   . GLU A 74  ? 0.2998 0.3823 0.2998 -0.0433 0.0185  -0.0428 73  GLU A C   
590  O O   . GLU A 74  ? 0.3035 0.3856 0.3048 -0.0426 0.0187  -0.0434 73  GLU A O   
591  C CB  . GLU A 74  ? 0.4351 0.5138 0.4320 -0.0440 0.0180  -0.0399 73  GLU A CB  
592  C CG  . GLU A 74  ? 0.5439 0.6245 0.5400 -0.0452 0.0182  -0.0402 73  GLU A CG  
593  C CD  . GLU A 74  ? 0.6575 0.7368 0.6523 -0.0458 0.0181  -0.0391 73  GLU A CD  
594  O OE1 . GLU A 74  ? 0.7172 0.7940 0.7115 -0.0453 0.0179  -0.0380 73  GLU A OE1 
595  O OE2 . GLU A 74  ? 0.7244 0.8052 0.7187 -0.0467 0.0182  -0.0394 73  GLU A OE2 
596  N N   . GLY A 75  ? 0.2966 0.3816 0.2967 -0.0439 0.0186  -0.0436 74  GLY A N   
597  C CA  . GLY A 75  ? 0.2872 0.3745 0.2888 -0.0439 0.0190  -0.0453 74  GLY A CA  
598  C C   . GLY A 75  ? 0.2902 0.3784 0.2934 -0.0431 0.0191  -0.0465 74  GLY A C   
599  O O   . GLY A 75  ? 0.3011 0.3917 0.3054 -0.0432 0.0193  -0.0479 74  GLY A O   
600  N N   . GLY A 76  ? 0.2673 0.3539 0.2709 -0.0422 0.0189  -0.0460 75  GLY A N   
601  C CA  . GLY A 76  ? 0.2377 0.3251 0.2428 -0.0414 0.0189  -0.0470 75  GLY A CA  
602  C C   . GLY A 76  ? 0.2541 0.3429 0.2587 -0.0418 0.0188  -0.0472 75  GLY A C   
603  O O   . GLY A 76  ? 0.2942 0.3830 0.2971 -0.0426 0.0186  -0.0463 75  GLY A O   
604  N N   . GLU A 77  ? 0.2206 0.3106 0.2267 -0.0412 0.0188  -0.0483 76  GLU A N   
605  C CA  . GLU A 77  ? 0.2261 0.3170 0.2317 -0.0413 0.0185  -0.0485 76  GLU A CA  
606  C C   . GLU A 77  ? 0.2280 0.3171 0.2336 -0.0403 0.0181  -0.0481 76  GLU A C   
607  O O   . GLU A 77  ? 0.2512 0.3398 0.2584 -0.0395 0.0183  -0.0485 76  GLU A O   
608  C CB  . GLU A 77  ? 0.2706 0.3645 0.2777 -0.0415 0.0189  -0.0503 76  GLU A CB  
609  C CG  . GLU A 77  ? 0.3535 0.4493 0.3605 -0.0424 0.0193  -0.0508 76  GLU A CG  
610  C CD  . GLU A 77  ? 0.4457 0.5442 0.4539 -0.0426 0.0195  -0.0524 76  GLU A CD  
611  O OE1 . GLU A 77  ? 0.4622 0.5612 0.4721 -0.0418 0.0196  -0.0535 76  GLU A OE1 
612  O OE2 . GLU A 77  ? 0.5264 0.6263 0.5337 -0.0434 0.0195  -0.0526 76  GLU A OE2 
613  N N   . TYR A 78  ? 0.2418 0.3301 0.2458 -0.0403 0.0174  -0.0474 77  TYR A N   
614  C CA  . TYR A 78  ? 0.2601 0.3474 0.2641 -0.0394 0.0170  -0.0472 77  TYR A CA  
615  C C   . TYR A 78  ? 0.2067 0.2963 0.2126 -0.0391 0.0172  -0.0489 77  TYR A C   
616  O O   . TYR A 78  ? 0.2095 0.3014 0.2160 -0.0396 0.0176  -0.0500 77  TYR A O   
617  C CB  . TYR A 78  ? 0.3972 0.4833 0.3988 -0.0396 0.0162  -0.0461 77  TYR A CB  
618  C CG  . TYR A 78  ? 0.5074 0.5912 0.5069 -0.0400 0.0159  -0.0443 77  TYR A CG  
619  C CD1 . TYR A 78  ? 0.5713 0.6555 0.5693 -0.0410 0.0159  -0.0438 77  TYR A CD1 
620  C CD2 . TYR A 78  ? 0.5788 0.6600 0.5776 -0.0394 0.0155  -0.0431 77  TYR A CD2 
621  C CE1 . TYR A 78  ? 0.6249 0.7070 0.6209 -0.0413 0.0155  -0.0422 77  TYR A CE1 
622  C CE2 . TYR A 78  ? 0.6324 0.7114 0.6292 -0.0397 0.0151  -0.0414 77  TYR A CE2 
623  C CZ  . TYR A 78  ? 0.6659 0.7454 0.6614 -0.0407 0.0151  -0.0410 77  TYR A CZ  
624  O OH  . TYR A 78  ? 0.7278 0.8051 0.7213 -0.0410 0.0147  -0.0393 77  TYR A OH  
625  N N   . ASP A 79  ? 0.1470 0.2357 0.1537 -0.0382 0.0170  -0.0491 78  ASP A N   
626  C CA  . ASP A 79  ? 0.1723 0.2629 0.1810 -0.0377 0.0172  -0.0507 78  ASP A CA  
627  C C   . ASP A 79  ? 0.1533 0.2432 0.1613 -0.0371 0.0166  -0.0504 78  ASP A C   
628  O O   . ASP A 79  ? 0.1458 0.2339 0.1540 -0.0364 0.0163  -0.0499 78  ASP A O   
629  C CB  . ASP A 79  ? 0.2745 0.3647 0.2853 -0.0370 0.0176  -0.0512 78  ASP A CB  
630  C CG  . ASP A 79  ? 0.2570 0.3489 0.2699 -0.0364 0.0179  -0.0528 78  ASP A CG  
631  O OD1 . ASP A 79  ? 0.3397 0.4340 0.3534 -0.0369 0.0182  -0.0540 78  ASP A OD1 
632  O OD2 . ASP A 79  ? 0.1459 0.2367 0.1597 -0.0355 0.0177  -0.0529 78  ASP A OD2 
633  N N   . ILE A 80  ? 0.1298 0.2211 0.1371 -0.0375 0.0164  -0.0508 79  ILE A N   
634  C CA  . ILE A 80  ? 0.1583 0.2489 0.1648 -0.0371 0.0158  -0.0505 79  ILE A CA  
635  C C   . ILE A 80  ? 0.1646 0.2571 0.1734 -0.0366 0.0160  -0.0522 79  ILE A C   
636  O O   . ILE A 80  ? 0.1861 0.2810 0.1958 -0.0370 0.0164  -0.0534 79  ILE A O   
637  C CB  . ILE A 80  ? 0.2110 0.3022 0.2155 -0.0378 0.0154  -0.0501 79  ILE A CB  
638  C CG1 . ILE A 80  ? 0.2553 0.3444 0.2574 -0.0382 0.0151  -0.0483 79  ILE A CG1 
639  C CG2 . ILE A 80  ? 0.2226 0.3139 0.2267 -0.0374 0.0149  -0.0502 79  ILE A CG2 
640  C CD1 . ILE A 80  ? 0.2534 0.3430 0.2535 -0.0389 0.0147  -0.0479 79  ILE A CD1 
641  N N   . ASP A 81  ? 0.1118 0.2030 0.1215 -0.0356 0.0159  -0.0522 80  ASP A N   
642  C CA  . ASP A 81  ? 0.1264 0.2192 0.1384 -0.0351 0.0161  -0.0537 80  ASP A CA  
643  C C   . ASP A 81  ? 0.1341 0.2268 0.1454 -0.0348 0.0156  -0.0537 80  ASP A C   
644  O O   . ASP A 81  ? 0.1353 0.2260 0.1452 -0.0344 0.0150  -0.0524 80  ASP A O   
645  C CB  . ASP A 81  ? 0.1426 0.2341 0.1562 -0.0342 0.0163  -0.0538 80  ASP A CB  
646  C CG  . ASP A 81  ? 0.1428 0.2342 0.1572 -0.0344 0.0168  -0.0538 80  ASP A CG  
647  O OD1 . ASP A 81  ? 0.1605 0.2541 0.1760 -0.0349 0.0174  -0.0549 80  ASP A OD1 
648  O OD2 . ASP A 81  ? 0.1181 0.2073 0.1319 -0.0341 0.0167  -0.0527 80  ASP A OD2 
649  N N   . VAL A 82  ? 0.1367 0.2318 0.1490 -0.0349 0.0158  -0.0550 81  VAL A N   
650  C CA  . VAL A 82  ? 0.1737 0.2690 0.1855 -0.0346 0.0153  -0.0551 81  VAL A CA  
651  C C   . VAL A 82  ? 0.1660 0.2633 0.1801 -0.0343 0.0156  -0.0569 81  VAL A C   
652  O O   . VAL A 82  ? 0.1866 0.2858 0.2024 -0.0345 0.0162  -0.0581 81  VAL A O   
653  C CB  . VAL A 82  ? 0.2377 0.3336 0.2474 -0.0354 0.0150  -0.0546 81  VAL A CB  
654  C CG1 . VAL A 82  ? 0.2778 0.3761 0.2882 -0.0361 0.0155  -0.0557 81  VAL A CG1 
655  C CG2 . VAL A 82  ? 0.2627 0.3588 0.2718 -0.0351 0.0144  -0.0547 81  VAL A CG2 
656  N N   . GLY A 83  ? 0.1893 0.2865 0.2038 -0.0337 0.0152  -0.0571 82  GLY A N   
657  C CA  . GLY A 83  ? 0.1969 0.2960 0.2134 -0.0333 0.0155  -0.0587 82  GLY A CA  
658  C C   . GLY A 83  ? 0.1607 0.2611 0.1762 -0.0337 0.0152  -0.0590 82  GLY A C   
659  O O   . GLY A 83  ? 0.1865 0.2857 0.1999 -0.0338 0.0146  -0.0578 82  GLY A O   
660  N N   . ILE A 84  ? 0.1967 0.2996 0.2136 -0.0339 0.0156  -0.0605 83  ILE A N   
661  C CA  . ILE A 84  ? 0.2175 0.3217 0.2337 -0.0341 0.0153  -0.0610 83  ILE A CA  
662  C C   . ILE A 84  ? 0.1848 0.2906 0.2033 -0.0336 0.0155  -0.0625 83  ILE A C   
663  O O   . ILE A 84  ? 0.1903 0.2975 0.2108 -0.0336 0.0161  -0.0637 83  ILE A O   
664  C CB  . ILE A 84  ? 0.2337 0.3397 0.2490 -0.0351 0.0155  -0.0612 83  ILE A CB  
665  C CG1 . ILE A 84  ? 0.2323 0.3403 0.2494 -0.0354 0.0162  -0.0626 83  ILE A CG1 
666  C CG2 . ILE A 84  ? 0.2386 0.3430 0.2514 -0.0356 0.0152  -0.0596 83  ILE A CG2 
667  C CD1 . ILE A 84  ? 0.2404 0.3503 0.2566 -0.0363 0.0164  -0.0629 83  ILE A CD1 
668  N N   . ILE A 85  ? 0.2222 0.3276 0.2402 -0.0332 0.0150  -0.0624 84  ILE A N   
669  C CA  . ILE A 85  ? 0.2350 0.3416 0.2550 -0.0327 0.0151  -0.0637 84  ILE A CA  
670  C C   . ILE A 85  ? 0.2343 0.3432 0.2540 -0.0331 0.0151  -0.0646 84  ILE A C   
671  O O   . ILE A 85  ? 0.2577 0.3661 0.2756 -0.0332 0.0146  -0.0638 84  ILE A O   
672  C CB  . ILE A 85  ? 0.2106 0.3153 0.2304 -0.0319 0.0146  -0.0630 84  ILE A CB  
673  C CG1 . ILE A 85  ? 0.2171 0.3194 0.2369 -0.0315 0.0146  -0.0620 84  ILE A CG1 
674  C CG2 . ILE A 85  ? 0.2145 0.3204 0.2365 -0.0313 0.0148  -0.0645 84  ILE A CG2 
675  C CD1 . ILE A 85  ? 0.2275 0.3278 0.2471 -0.0307 0.0141  -0.0612 84  ILE A CD1 
676  N N   . LEU A 86  ? 0.2659 0.3771 0.2873 -0.0334 0.0157  -0.0661 85  LEU A N   
677  C CA  . LEU A 86  ? 0.3053 0.4187 0.3265 -0.0339 0.0157  -0.0670 85  LEU A CA  
678  C C   . LEU A 86  ? 0.3235 0.4377 0.3458 -0.0333 0.0155  -0.0678 85  LEU A C   
679  O O   . LEU A 86  ? 0.2903 0.4041 0.3144 -0.0327 0.0157  -0.0684 85  LEU A O   
680  C CB  . LEU A 86  ? 0.3205 0.4362 0.3431 -0.0344 0.0164  -0.0683 85  LEU A CB  
681  C CG  . LEU A 86  ? 0.3456 0.4615 0.3668 -0.0352 0.0165  -0.0677 85  LEU A CG  
682  C CD1 . LEU A 86  ? 0.3531 0.4713 0.3760 -0.0356 0.0172  -0.0691 85  LEU A CD1 
683  C CD2 . LEU A 86  ? 0.3608 0.4769 0.3797 -0.0358 0.0161  -0.0669 85  LEU A CD2 
684  N N   . ASN A 87  ? 0.3482 0.4634 0.3694 -0.0336 0.0152  -0.0679 86  ASN A N   
685  C CA  . ASN A 87  ? 0.4013 0.5172 0.4232 -0.0332 0.0150  -0.0687 86  ASN A CA  
686  C C   . ASN A 87  ? 0.3649 0.4834 0.3892 -0.0332 0.0156  -0.0706 86  ASN A C   
687  O O   . ASN A 87  ? 0.3327 0.4531 0.3570 -0.0335 0.0156  -0.0714 86  ASN A O   
688  C CB  . ASN A 87  ? 0.5105 0.6264 0.5303 -0.0335 0.0145  -0.0680 86  ASN A CB  
689  C CG  . ASN A 87  ? 0.6104 0.7269 0.6307 -0.0330 0.0142  -0.0685 86  ASN A CG  
690  O OD1 . ASN A 87  ? 0.6519 0.7677 0.6735 -0.0323 0.0142  -0.0688 86  ASN A OD1 
691  N ND2 . ASN A 87  ? 0.6888 0.8065 0.7080 -0.0334 0.0140  -0.0687 86  ASN A ND2 
692  N N   . ILE A 88  ? 0.3102 0.4287 0.3364 -0.0329 0.0160  -0.0713 87  ILE A N   
693  C CA  . ILE A 88  ? 0.2939 0.4147 0.3224 -0.0330 0.0166  -0.0730 87  ILE A CA  
694  C C   . ILE A 88  ? 0.2820 0.4023 0.3128 -0.0322 0.0168  -0.0737 87  ILE A C   
695  O O   . ILE A 88  ? 0.2897 0.4079 0.3204 -0.0317 0.0166  -0.0728 87  ILE A O   
696  C CB  . ILE A 88  ? 0.2721 0.3940 0.3008 -0.0337 0.0171  -0.0734 87  ILE A CB  
697  C CG1 . ILE A 88  ? 0.2816 0.4017 0.3105 -0.0335 0.0173  -0.0726 87  ILE A CG1 
698  C CG2 . ILE A 88  ? 0.2795 0.4022 0.3061 -0.0345 0.0170  -0.0729 87  ILE A CG2 
699  C CD1 . ILE A 88  ? 0.2669 0.3882 0.2965 -0.0340 0.0179  -0.0732 87  ILE A CD1 
700  N N   . ALA A 89  ? 0.2723 0.3945 0.3050 -0.0321 0.0172  -0.0754 88  ALA A N   
701  C CA  . ALA A 89  ? 0.2121 0.3341 0.2472 -0.0314 0.0174  -0.0762 88  ALA A CA  
702  C C   . ALA A 89  ? 0.2649 0.3876 0.3015 -0.0315 0.0180  -0.0769 88  ALA A C   
703  O O   . ALA A 89  ? 0.2548 0.3794 0.2917 -0.0321 0.0184  -0.0777 88  ALA A O   
704  C CB  . ALA A 89  ? 0.2655 0.3894 0.3020 -0.0312 0.0175  -0.0777 88  ALA A CB  
705  N N   . LYS A 90  ? 0.2560 0.3770 0.2935 -0.0309 0.0181  -0.0765 89  LYS A N   
706  C CA  . LYS A 90  ? 0.2563 0.3773 0.2949 -0.0310 0.0186  -0.0769 89  LYS A CA  
707  C C   . LYS A 90  ? 0.2876 0.4099 0.3279 -0.0309 0.0188  -0.0785 89  LYS A C   
708  O O   . LYS A 90  ? 0.2900 0.4128 0.3306 -0.0312 0.0191  -0.0789 89  LYS A O   
709  C CB  . LYS A 90  ? 0.2649 0.3831 0.3037 -0.0303 0.0184  -0.0760 89  LYS A CB  
710  C CG  . LYS A 90  ? 0.2633 0.3806 0.3037 -0.0294 0.0182  -0.0765 89  LYS A CG  
711  C CD  . LYS A 90  ? 0.2547 0.3692 0.2952 -0.0288 0.0181  -0.0755 89  LYS A CD  
712  C CE  . LYS A 90  ? 0.2539 0.3673 0.2959 -0.0279 0.0179  -0.0760 89  LYS A CE  
713  N NZ  . LYS A 90  ? 0.2813 0.3958 0.3251 -0.0277 0.0181  -0.0775 89  LYS A NZ  
714  N N   . ASP A 91  ? 0.3035 0.4264 0.3451 -0.0304 0.0187  -0.0794 90  ASP A N   
715  C CA  . ASP A 91  ? 0.3267 0.4507 0.3700 -0.0303 0.0189  -0.0808 90  ASP A CA  
716  C C   . ASP A 91  ? 0.3044 0.4310 0.3475 -0.0311 0.0192  -0.0817 90  ASP A C   
717  O O   . ASP A 91  ? 0.2779 0.4055 0.3223 -0.0311 0.0194  -0.0829 90  ASP A O   
718  C CB  . ASP A 91  ? 0.3819 0.5058 0.4265 -0.0296 0.0187  -0.0816 90  ASP A CB  
719  C CG  . ASP A 91  ? 0.4265 0.5480 0.4720 -0.0288 0.0185  -0.0811 90  ASP A CG  
720  O OD1 . ASP A 91  ? 0.4474 0.5671 0.4924 -0.0286 0.0185  -0.0802 90  ASP A OD1 
721  O OD2 . ASP A 91  ? 0.4456 0.5668 0.4920 -0.0282 0.0183  -0.0815 90  ASP A OD2 
722  N N   . ASP A 92  ? 0.3200 0.4478 0.3616 -0.0317 0.0192  -0.0812 91  ASP A N   
723  C CA  . ASP A 92  ? 0.3283 0.4586 0.3696 -0.0325 0.0194  -0.0820 91  ASP A CA  
724  C C   . ASP A 92  ? 0.2978 0.4285 0.3381 -0.0332 0.0196  -0.0816 91  ASP A C   
725  O O   . ASP A 92  ? 0.2714 0.4042 0.3114 -0.0339 0.0198  -0.0823 91  ASP A O   
726  C CB  . ASP A 92  ? 0.3700 0.5013 0.4101 -0.0328 0.0191  -0.0818 91  ASP A CB  
727  C CG  . ASP A 92  ? 0.4048 0.5361 0.4459 -0.0321 0.0189  -0.0824 91  ASP A CG  
728  O OD1 . ASP A 92  ? 0.4210 0.5524 0.4640 -0.0316 0.0191  -0.0834 91  ASP A OD1 
729  O OD2 . ASP A 92  ? 0.4244 0.5549 0.4640 -0.0321 0.0184  -0.0816 91  ASP A OD2 
730  N N   . HIS A 93  ? 0.2810 0.4097 0.3208 -0.0331 0.0196  -0.0806 92  HIS A N   
731  C CA  . HIS A 93  ? 0.2934 0.4224 0.3322 -0.0338 0.0198  -0.0801 92  HIS A CA  
732  C C   . HIS A 93  ? 0.2847 0.4118 0.3241 -0.0334 0.0199  -0.0799 92  HIS A C   
733  O O   . HIS A 93  ? 0.2924 0.4176 0.3324 -0.0326 0.0197  -0.0795 92  HIS A O   
734  C CB  . HIS A 93  ? 0.2918 0.4204 0.3285 -0.0343 0.0197  -0.0788 92  HIS A CB  
735  C CG  . HIS A 93  ? 0.3223 0.4518 0.3577 -0.0345 0.0193  -0.0787 92  HIS A CG  
736  N ND1 . HIS A 93  ? 0.3194 0.4508 0.3540 -0.0353 0.0194  -0.0791 92  HIS A ND1 
737  C CD2 . HIS A 93  ? 0.3269 0.4553 0.3615 -0.0341 0.0188  -0.0782 92  HIS A CD2 
738  C CE1 . HIS A 93  ? 0.3324 0.4639 0.3658 -0.0353 0.0190  -0.0788 92  HIS A CE1 
739  N NE2 . HIS A 93  ? 0.3265 0.4562 0.3598 -0.0346 0.0186  -0.0782 92  HIS A NE2 
740  N N   . ASP A 94  ? 0.2601 0.3880 0.2993 -0.0339 0.0202  -0.0802 93  ASP A N   
741  C CA  . ASP A 94  ? 0.2743 0.4006 0.3137 -0.0337 0.0203  -0.0797 93  ASP A CA  
742  C C   . ASP A 94  ? 0.2451 0.3699 0.2827 -0.0340 0.0202  -0.0781 93  ASP A C   
743  O O   . ASP A 94  ? 0.2547 0.3805 0.2909 -0.0347 0.0202  -0.0776 93  ASP A O   
744  C CB  . ASP A 94  ? 0.2876 0.4154 0.3275 -0.0342 0.0206  -0.0806 93  ASP A CB  
745  C CG  . ASP A 94  ? 0.3274 0.4535 0.3673 -0.0341 0.0207  -0.0800 93  ASP A CG  
746  O OD1 . ASP A 94  ? 0.3386 0.4635 0.3798 -0.0335 0.0207  -0.0803 93  ASP A OD1 
747  O OD2 . ASP A 94  ? 0.3395 0.4655 0.3779 -0.0348 0.0208  -0.0792 93  ASP A OD2 
748  N N   . PRO A 95  ? 0.2907 0.4131 0.3284 -0.0334 0.0200  -0.0772 94  PRO A N   
749  C CA  . PRO A 95  ? 0.2687 0.3894 0.3047 -0.0336 0.0199  -0.0757 94  PRO A CA  
750  C C   . PRO A 95  ? 0.2745 0.3960 0.3092 -0.0345 0.0201  -0.0752 94  PRO A C   
751  O O   . PRO A 95  ? 0.2332 0.3546 0.2662 -0.0351 0.0200  -0.0742 94  PRO A O   
752  C CB  . PRO A 95  ? 0.3262 0.4444 0.3629 -0.0329 0.0198  -0.0751 94  PRO A CB  
753  C CG  . PRO A 95  ? 0.3136 0.4319 0.3522 -0.0321 0.0198  -0.0763 94  PRO A CG  
754  C CD  . PRO A 95  ? 0.2676 0.3884 0.3069 -0.0325 0.0200  -0.0777 94  PRO A CD  
755  N N   . VAL A 96  ? 0.2759 0.3981 0.3114 -0.0347 0.0204  -0.0760 95  VAL A N   
756  C CA  . VAL A 96  ? 0.2703 0.3934 0.3047 -0.0356 0.0206  -0.0757 95  VAL A CA  
757  C C   . VAL A 96  ? 0.2855 0.4108 0.3189 -0.0364 0.0207  -0.0760 95  VAL A C   
758  O O   . VAL A 96  ? 0.2635 0.3889 0.2953 -0.0371 0.0207  -0.0751 95  VAL A O   
759  C CB  . VAL A 96  ? 0.3152 0.4385 0.3507 -0.0355 0.0209  -0.0766 95  VAL A CB  
760  C CG1 . VAL A 96  ? 0.3307 0.4549 0.3651 -0.0364 0.0211  -0.0763 95  VAL A CG1 
761  C CG2 . VAL A 96  ? 0.3129 0.4340 0.3494 -0.0347 0.0208  -0.0763 95  VAL A CG2 
762  N N   . GLU A 97  ? 0.2649 0.3920 0.2993 -0.0363 0.0207  -0.0771 96  GLU A N   
763  C CA  . GLU A 97  ? 0.3008 0.4300 0.3342 -0.0371 0.0208  -0.0774 96  GLU A CA  
764  C C   . GLU A 97  ? 0.2617 0.3904 0.2935 -0.0373 0.0205  -0.0761 96  GLU A C   
765  O O   . GLU A 97  ? 0.2962 0.4257 0.3264 -0.0381 0.0205  -0.0755 96  GLU A O   
766  C CB  . GLU A 97  ? 0.3052 0.4363 0.3400 -0.0369 0.0208  -0.0788 96  GLU A CB  
767  C CG  . GLU A 97  ? 0.3514 0.4837 0.3876 -0.0369 0.0211  -0.0802 96  GLU A CG  
768  C CD  . GLU A 97  ? 0.3980 0.5318 0.4333 -0.0378 0.0213  -0.0803 96  GLU A CD  
769  O OE1 . GLU A 97  ? 0.4210 0.5546 0.4568 -0.0379 0.0215  -0.0805 96  GLU A OE1 
770  O OE2 . GLU A 97  ? 0.4154 0.5506 0.4495 -0.0385 0.0213  -0.0800 96  GLU A OE2 
771  N N   . VAL A 98  ? 0.2585 0.3856 0.2905 -0.0366 0.0202  -0.0755 97  VAL A N   
772  C CA  . VAL A 98  ? 0.2574 0.3828 0.2872 -0.0366 0.0197  -0.0740 97  VAL A CA  
773  C C   . VAL A 98  ? 0.2510 0.3749 0.2791 -0.0371 0.0196  -0.0726 97  VAL A C   
774  O O   . VAL A 98  ? 0.2713 0.3946 0.2971 -0.0376 0.0193  -0.0716 97  VAL A O   
775  C CB  . VAL A 98  ? 0.2426 0.3662 0.2731 -0.0357 0.0194  -0.0738 97  VAL A CB  
776  C CG1 . VAL A 98  ? 0.2195 0.3407 0.2476 -0.0356 0.0187  -0.0720 97  VAL A CG1 
777  C CG2 . VAL A 98  ? 0.2143 0.3394 0.2461 -0.0353 0.0194  -0.0750 97  VAL A CG2 
778  N N   . LYS A 99  ? 0.2662 0.3895 0.2953 -0.0369 0.0200  -0.0726 98  LYS A N   
779  C CA  . LYS A 99  ? 0.2869 0.4090 0.3145 -0.0374 0.0200  -0.0714 98  LYS A CA  
780  C C   . LYS A 99  ? 0.2958 0.4196 0.3225 -0.0384 0.0202  -0.0716 98  LYS A C   
781  O O   . LYS A 99  ? 0.2992 0.4222 0.3240 -0.0389 0.0200  -0.0704 98  LYS A O   
782  C CB  . LYS A 99  ? 0.2903 0.4106 0.3188 -0.0369 0.0202  -0.0712 98  LYS A CB  
783  C CG  . LYS A 99  ? 0.2928 0.4108 0.3212 -0.0362 0.0198  -0.0702 98  LYS A CG  
784  C CD  . LYS A 99  ? 0.2858 0.4015 0.3145 -0.0356 0.0199  -0.0697 98  LYS A CD  
785  C CE  . LYS A 99  ? 0.2794 0.3953 0.3103 -0.0349 0.0200  -0.0710 98  LYS A CE  
786  N NZ  . LYS A 99  ? 0.2350 0.3488 0.2663 -0.0345 0.0200  -0.0705 98  LYS A NZ  
787  N N   . LYS A 100 ? 0.2868 0.4133 0.3149 -0.0386 0.0206  -0.0732 99  LYS A N   
788  C CA  . LYS A 100 ? 0.2920 0.4202 0.3192 -0.0396 0.0207  -0.0734 99  LYS A CA  
789  C C   . LYS A 100 ? 0.3014 0.4292 0.3263 -0.0399 0.0202  -0.0726 99  LYS A C   
790  O O   . LYS A 100 ? 0.3274 0.4553 0.3505 -0.0406 0.0201  -0.0719 99  LYS A O   
791  C CB  . LYS A 100 ? 0.3269 0.4574 0.3558 -0.0396 0.0211  -0.0752 99  LYS A CB  
792  C CG  . LYS A 100 ? 0.3322 0.4620 0.3624 -0.0393 0.0213  -0.0757 99  LYS A CG  
793  C CD  . LYS A 100 ? 0.3864 0.5185 0.4176 -0.0396 0.0215  -0.0773 99  LYS A CD  
794  C CE  . LYS A 100 ? 0.4196 0.5511 0.4523 -0.0391 0.0217  -0.0779 99  LYS A CE  
795  N NZ  . LYS A 100 ? 0.4362 0.5664 0.4703 -0.0381 0.0215  -0.0783 99  LYS A NZ  
796  N N   . TRP A 101 ? 0.2946 0.4220 0.3194 -0.0394 0.0198  -0.0726 100 TRP A N   
797  C CA  . TRP A 101 ? 0.3200 0.4469 0.3426 -0.0396 0.0192  -0.0717 100 TRP A CA  
798  C C   . TRP A 101 ? 0.3165 0.4411 0.3369 -0.0398 0.0189  -0.0699 100 TRP A C   
799  O O   . TRP A 101 ? 0.3435 0.4681 0.3620 -0.0404 0.0186  -0.0692 100 TRP A O   
800  C CB  . TRP A 101 ? 0.3300 0.4563 0.3528 -0.0389 0.0188  -0.0718 100 TRP A CB  
801  C CG  . TRP A 101 ? 0.3419 0.4701 0.3669 -0.0385 0.0191  -0.0735 100 TRP A CG  
802  C CD1 . TRP A 101 ? 0.3397 0.4704 0.3663 -0.0389 0.0196  -0.0750 100 TRP A CD1 
803  C CD2 . TRP A 101 ? 0.3264 0.4541 0.3524 -0.0378 0.0188  -0.0738 100 TRP A CD2 
804  N NE1 . TRP A 101 ? 0.3376 0.4694 0.3660 -0.0384 0.0197  -0.0763 100 TRP A NE1 
805  C CE2 . TRP A 101 ? 0.3329 0.4629 0.3610 -0.0377 0.0192  -0.0756 100 TRP A CE2 
806  C CE3 . TRP A 101 ? 0.3258 0.4514 0.3510 -0.0371 0.0183  -0.0728 100 TRP A CE3 
807  C CZ2 . TRP A 101 ? 0.3114 0.4416 0.3409 -0.0370 0.0191  -0.0763 100 TRP A CZ2 
808  C CZ3 . TRP A 101 ? 0.3159 0.4417 0.3425 -0.0365 0.0182  -0.0736 100 TRP A CZ3 
809  C CH2 . TRP A 101 ? 0.3155 0.4436 0.3442 -0.0364 0.0187  -0.0753 100 TRP A CH2 
810  N N   . ILE A 102 ? 0.3245 0.4471 0.3453 -0.0393 0.0188  -0.0692 101 ILE A N   
811  C CA  . ILE A 102 ? 0.3153 0.4354 0.3339 -0.0394 0.0184  -0.0674 101 ILE A CA  
812  C C   . ILE A 102 ? 0.3679 0.4884 0.3858 -0.0402 0.0187  -0.0670 101 ILE A C   
813  O O   . ILE A 102 ? 0.3474 0.4670 0.3630 -0.0407 0.0184  -0.0658 101 ILE A O   
814  C CB  . ILE A 102 ? 0.3024 0.4203 0.3216 -0.0386 0.0183  -0.0667 101 ILE A CB  
815  C CG1 . ILE A 102 ? 0.2557 0.3733 0.2757 -0.0378 0.0180  -0.0671 101 ILE A CG1 
816  C CG2 . ILE A 102 ? 0.2732 0.3885 0.2903 -0.0387 0.0179  -0.0649 101 ILE A CG2 
817  C CD1 . ILE A 102 ? 0.2738 0.3912 0.2921 -0.0378 0.0174  -0.0665 101 ILE A CD1 
818  N N   . ARG A 103 ? 0.3829 0.5046 0.4025 -0.0403 0.0193  -0.0680 102 ARG A N   
819  C CA  . ARG A 103 ? 0.4402 0.5625 0.4593 -0.0411 0.0197  -0.0678 102 ARG A CA  
820  C C   . ARG A 103 ? 0.4467 0.5705 0.4644 -0.0419 0.0196  -0.0679 102 ARG A C   
821  O O   . ARG A 103 ? 0.4458 0.5689 0.4616 -0.0425 0.0194  -0.0669 102 ARG A O   
822  C CB  . ARG A 103 ? 0.4616 0.5854 0.4830 -0.0411 0.0204  -0.0691 102 ARG A CB  
823  C CG  . ARG A 103 ? 0.5026 0.6269 0.5235 -0.0419 0.0207  -0.0688 102 ARG A CG  
824  C CD  . ARG A 103 ? 0.5396 0.6658 0.5625 -0.0420 0.0213  -0.0703 102 ARG A CD  
825  N NE  . ARG A 103 ? 0.5610 0.6898 0.5849 -0.0422 0.0214  -0.0717 102 ARG A NE  
826  C CZ  . ARG A 103 ? 0.5861 0.7157 0.6116 -0.0418 0.0216  -0.0731 102 ARG A CZ  
827  N NH1 . ARG A 103 ? 0.5886 0.7169 0.6152 -0.0412 0.0217  -0.0733 102 ARG A NH1 
828  N NH2 . ARG A 103 ? 0.5899 0.7219 0.6161 -0.0420 0.0217  -0.0743 102 ARG A NH2 
829  N N   . ASP A 104 ? 0.4296 0.5556 0.4483 -0.0419 0.0197  -0.0692 103 ASP A N   
830  C CA  . ASP A 104 ? 0.4344 0.5620 0.4520 -0.0427 0.0196  -0.0695 103 ASP A CA  
831  C C   . ASP A 104 ? 0.4234 0.5494 0.4383 -0.0428 0.0190  -0.0680 103 ASP A C   
832  O O   . ASP A 104 ? 0.4078 0.5342 0.4210 -0.0436 0.0189  -0.0675 103 ASP A O   
833  C CB  . ASP A 104 ? 0.4520 0.5819 0.4710 -0.0426 0.0198  -0.0711 103 ASP A CB  
834  C CG  . ASP A 104 ? 0.4753 0.6071 0.4970 -0.0425 0.0205  -0.0726 103 ASP A CG  
835  O OD1 . ASP A 104 ? 0.4844 0.6158 0.5065 -0.0427 0.0208  -0.0725 103 ASP A OD1 
836  O OD2 . ASP A 104 ? 0.4876 0.6212 0.5108 -0.0423 0.0206  -0.0740 103 ASP A OD2 
837  N N   . ALA A 105 ? 0.4050 0.5293 0.4195 -0.0421 0.0185  -0.0673 104 ALA A N   
838  C CA  . ALA A 105 ? 0.4023 0.5249 0.4143 -0.0422 0.0179  -0.0659 104 ALA A CA  
839  C C   . ALA A 105 ? 0.4271 0.5479 0.4373 -0.0426 0.0178  -0.0644 104 ALA A C   
840  O O   . ALA A 105 ? 0.4151 0.5351 0.4231 -0.0431 0.0174  -0.0633 104 ALA A O   
841  C CB  . ALA A 105 ? 0.3817 0.5027 0.3937 -0.0413 0.0174  -0.0654 104 ALA A CB  
842  N N   . LEU A 106 ? 0.4610 0.5810 0.4722 -0.0425 0.0181  -0.0643 105 LEU A N   
843  C CA  . LEU A 106 ? 0.5171 0.6355 0.5270 -0.0429 0.0181  -0.0630 105 LEU A CA  
844  C C   . LEU A 106 ? 0.6573 0.7775 0.6679 -0.0437 0.0187  -0.0637 105 LEU A C   
845  O O   . LEU A 106 ? 0.6793 0.7987 0.6903 -0.0438 0.0189  -0.0633 105 LEU A O   
846  C CB  . LEU A 106 ? 0.4398 0.5560 0.4502 -0.0422 0.0180  -0.0623 105 LEU A CB  
847  C CG  . LEU A 106 ? 0.3675 0.4816 0.3772 -0.0415 0.0175  -0.0614 105 LEU A CG  
848  C CD1 . LEU A 106 ? 0.3397 0.4524 0.3508 -0.0408 0.0176  -0.0613 105 LEU A CD1 
849  C CD2 . LEU A 106 ? 0.3518 0.4640 0.3588 -0.0417 0.0169  -0.0597 105 LEU A CD2 
850  N N   . LYS A 107 ? 0.7684 0.8909 0.7791 -0.0442 0.0188  -0.0647 106 LYS A N   
851  C CA  . LYS A 107 ? 0.8662 0.9904 0.8774 -0.0450 0.0194  -0.0653 106 LYS A CA  
852  C C   . LYS A 107 ? 0.9143 1.0373 0.9233 -0.0457 0.0192  -0.0639 106 LYS A C   
853  O O   . LYS A 107 ? 0.9181 1.0404 0.9272 -0.0459 0.0194  -0.0635 106 LYS A O   
854  C CB  . LYS A 107 ? 0.9018 1.0287 0.9137 -0.0453 0.0196  -0.0668 106 LYS A CB  
855  C CG  . LYS A 107 ? 0.9320 1.0608 0.9467 -0.0450 0.0201  -0.0685 106 LYS A CG  
856  C CD  . LYS A 107 ? 0.9600 1.0916 0.9754 -0.0453 0.0203  -0.0699 106 LYS A CD  
857  C CE  . LYS A 107 ? 0.9785 1.1117 0.9937 -0.0462 0.0207  -0.0703 106 LYS A CE  
858  N NZ  . LYS A 107 ? 0.9840 1.1200 1.0003 -0.0465 0.0210  -0.0718 106 LYS A NZ  
859  N N   . ASP A 108 ? 0.9527 1.0752 0.9595 -0.0460 0.0187  -0.0632 107 ASP A N   
860  C CA  . ASP A 108 ? 0.9873 1.1088 0.9919 -0.0467 0.0185  -0.0619 107 ASP A CA  
861  C C   . ASP A 108 ? 0.9281 1.0466 0.9310 -0.0463 0.0180  -0.0601 107 ASP A C   
862  O O   . ASP A 108 ? 0.9421 1.0594 0.9428 -0.0468 0.0176  -0.0589 107 ASP A O   
863  C CB  . ASP A 108 ? 1.0743 1.1971 1.0776 -0.0472 0.0183  -0.0621 107 ASP A CB  
864  C CG  . ASP A 108 ? 1.1357 1.2616 1.1405 -0.0476 0.0188  -0.0638 107 ASP A CG  
865  O OD1 . ASP A 108 ? 1.1582 1.2852 1.1649 -0.0477 0.0193  -0.0647 107 ASP A OD1 
866  O OD2 . ASP A 108 ? 1.1572 1.2845 1.1615 -0.0479 0.0186  -0.0642 107 ASP A OD2 
867  N N   . TYR A 109 ? 0.8356 0.9527 0.8395 -0.0455 0.0179  -0.0600 108 TYR A N   
868  C CA  . TYR A 109 ? 0.7339 0.8481 0.7364 -0.0452 0.0174  -0.0583 108 TYR A CA  
869  C C   . TYR A 109 ? 0.7351 0.8483 0.7381 -0.0453 0.0178  -0.0578 108 TYR A C   
870  O O   . TYR A 109 ? 0.7222 0.8362 0.7273 -0.0451 0.0182  -0.0588 108 TYR A O   
871  C CB  . TYR A 109 ? 0.6234 0.7365 0.6266 -0.0442 0.0171  -0.0583 108 TYR A CB  
872  C CG  . TYR A 109 ? 0.5250 0.6351 0.5267 -0.0438 0.0166  -0.0566 108 TYR A CG  
873  C CD1 . TYR A 109 ? 0.4855 0.5943 0.4850 -0.0439 0.0160  -0.0554 108 TYR A CD1 
874  C CD2 . TYR A 109 ? 0.4892 0.5977 0.4917 -0.0434 0.0168  -0.0561 108 TYR A CD2 
875  C CE1 . TYR A 109 ? 0.4652 0.5712 0.4632 -0.0435 0.0155  -0.0539 108 TYR A CE1 
876  C CE2 . TYR A 109 ? 0.4576 0.5634 0.4587 -0.0431 0.0163  -0.0546 108 TYR A CE2 
877  C CZ  . TYR A 109 ? 0.4518 0.5563 0.4506 -0.0431 0.0157  -0.0534 108 TYR A CZ  
878  O OH  . TYR A 109 ? 0.4347 0.5364 0.4321 -0.0428 0.0152  -0.0518 108 TYR A OH  
879  N N   . GLY A 110 ? 0.7600 0.8714 0.7610 -0.0457 0.0175  -0.0563 109 GLY A N   
880  C CA  . GLY A 110 ? 0.7954 0.9057 0.7965 -0.0459 0.0177  -0.0557 109 GLY A CA  
881  C C   . GLY A 110 ? 0.8410 0.9535 0.8439 -0.0464 0.0184  -0.0570 109 GLY A C   
882  O O   . GLY A 110 ? 0.8421 0.9568 0.8451 -0.0470 0.0187  -0.0579 109 GLY A O   
883  N N   . ASN A 111 ? 0.8766 0.9886 0.8810 -0.0460 0.0188  -0.0572 110 ASN A N   
884  C CA  . ASN A 111 ? 0.9125 1.0265 0.9188 -0.0463 0.0195  -0.0584 110 ASN A CA  
885  C C   . ASN A 111 ? 0.9276 1.0435 0.9363 -0.0458 0.0198  -0.0601 110 ASN A C   
886  O O   . ASN A 111 ? 0.9307 1.0476 0.9414 -0.0457 0.0204  -0.0610 110 ASN A O   
887  C CB  . ASN A 111 ? 0.9153 1.0278 0.9220 -0.0462 0.0197  -0.0578 110 ASN A CB  
888  C CG  . ASN A 111 ? 0.9204 1.0311 0.9249 -0.0468 0.0194  -0.0561 110 ASN A CG  
889  O OD1 . ASN A 111 ? 0.9235 1.0336 0.9260 -0.0472 0.0190  -0.0553 110 ASN A OD1 
890  N ND2 . ASN A 111 ? 0.9234 1.0330 0.9281 -0.0469 0.0197  -0.0556 110 ASN A ND2 
891  N N   . GLY A 112 ? 0.9701 1.0867 0.9787 -0.0455 0.0196  -0.0606 111 GLY A N   
892  C CA  . GLY A 112 ? 0.9362 1.0547 0.9471 -0.0450 0.0198  -0.0622 111 GLY A CA  
893  C C   . GLY A 112 ? 0.8748 0.9921 0.8872 -0.0441 0.0199  -0.0624 111 GLY A C   
894  O O   . GLY A 112 ? 0.8893 1.0049 0.9017 -0.0439 0.0200  -0.0616 111 GLY A O   
895  N N   . ALA A 113 ? 0.7853 0.9036 0.7991 -0.0435 0.0199  -0.0635 112 ALA A N   
896  C CA  . ALA A 113 ? 0.6827 0.8001 0.6981 -0.0425 0.0200  -0.0638 112 ALA A CA  
897  C C   . ALA A 113 ? 0.5746 0.6936 0.5926 -0.0424 0.0207  -0.0652 112 ALA A C   
898  O O   . ALA A 113 ? 0.5560 0.6770 0.5746 -0.0430 0.0211  -0.0660 112 ALA A O   
899  C CB  . ALA A 113 ? 0.6798 0.7974 0.6955 -0.0419 0.0196  -0.0643 112 ALA A CB  
900  N N   . GLU A 114 ? 0.4978 0.6158 0.5173 -0.0415 0.0207  -0.0654 113 GLU A N   
901  C CA  . GLU A 114 ? 0.4457 0.5633 0.4667 -0.0409 0.0209  -0.0663 113 GLU A CA  
902  C C   . GLU A 114 ? 0.3820 0.4988 0.4045 -0.0399 0.0207  -0.0668 113 GLU A C   
903  O O   . GLU A 114 ? 0.3752 0.4903 0.3973 -0.0394 0.0205  -0.0658 113 GLU A O   
904  C CB  . GLU A 114 ? 0.4701 0.5859 0.4907 -0.0409 0.0210  -0.0654 113 GLU A CB  
905  C CG  . GLU A 114 ? 0.5128 0.6281 0.5350 -0.0403 0.0211  -0.0662 113 GLU A CG  
906  C CD  . GLU A 114 ? 0.5620 0.6756 0.5836 -0.0404 0.0212  -0.0653 113 GLU A CD  
907  O OE1 . GLU A 114 ? 0.5799 0.6916 0.6022 -0.0396 0.0211  -0.0651 113 GLU A OE1 
908  O OE2 . GLU A 114 ? 0.5777 0.6919 0.5980 -0.0413 0.0213  -0.0649 113 GLU A OE2 
909  N N   . ILE A 115 ? 0.3232 0.4412 0.3474 -0.0395 0.0209  -0.0682 114 ILE A N   
910  C CA  . ILE A 115 ? 0.3025 0.4199 0.3282 -0.0385 0.0208  -0.0688 114 ILE A CA  
911  C C   . ILE A 115 ? 0.2993 0.4147 0.3260 -0.0377 0.0208  -0.0686 114 ILE A C   
912  O O   . ILE A 115 ? 0.3017 0.4174 0.3292 -0.0378 0.0210  -0.0693 114 ILE A O   
913  C CB  . ILE A 115 ? 0.2797 0.3994 0.3069 -0.0384 0.0209  -0.0704 114 ILE A CB  
914  C CG1 . ILE A 115 ? 0.2881 0.4096 0.3144 -0.0390 0.0209  -0.0706 114 ILE A CG1 
915  C CG2 . ILE A 115 ? 0.2936 0.4125 0.3225 -0.0374 0.0208  -0.0711 114 ILE A CG2 
916  C CD1 . ILE A 115 ? 0.2722 0.3960 0.2998 -0.0390 0.0210  -0.0722 114 ILE A CD1 
917  N N   . ARG A 116 ? 0.2938 0.4069 0.3202 -0.0371 0.0205  -0.0677 115 ARG A N   
918  C CA  . ARG A 116 ? 0.3226 0.4337 0.3499 -0.0363 0.0205  -0.0674 115 ARG A CA  
919  C C   . ARG A 116 ? 0.2977 0.4083 0.3265 -0.0354 0.0203  -0.0681 115 ARG A C   
920  O O   . ARG A 116 ? 0.3434 0.4548 0.3723 -0.0353 0.0202  -0.0683 115 ARG A O   
921  C CB  . ARG A 116 ? 0.3943 0.5031 0.4202 -0.0363 0.0203  -0.0658 115 ARG A CB  
922  C CG  . ARG A 116 ? 0.4609 0.5700 0.4851 -0.0373 0.0204  -0.0650 115 ARG A CG  
923  C CD  . ARG A 116 ? 0.5378 0.6445 0.5612 -0.0372 0.0204  -0.0637 115 ARG A CD  
924  N NE  . ARG A 116 ? 0.6183 0.7232 0.6405 -0.0370 0.0201  -0.0624 115 ARG A NE  
925  C CZ  . ARG A 116 ? 0.6639 0.7670 0.6847 -0.0372 0.0199  -0.0610 115 ARG A CZ  
926  N NH1 . ARG A 116 ? 0.6895 0.7924 0.7099 -0.0376 0.0201  -0.0607 115 ARG A NH1 
927  N NH2 . ARG A 116 ? 0.6828 0.7844 0.7027 -0.0370 0.0197  -0.0598 115 ARG A NH2 
928  N N   . ARG A 117 ? 0.2475 0.3566 0.2775 -0.0346 0.0203  -0.0682 116 ARG A N   
929  C CA  . ARG A 117 ? 0.2201 0.3289 0.2518 -0.0337 0.0202  -0.0691 116 ARG A CA  
930  C C   . ARG A 117 ? 0.2411 0.3493 0.2726 -0.0333 0.0199  -0.0686 116 ARG A C   
931  O O   . ARG A 117 ? 0.2316 0.3405 0.2643 -0.0329 0.0198  -0.0695 116 ARG A O   
932  C CB  . ARG A 117 ? 0.2007 0.3077 0.2336 -0.0330 0.0202  -0.0690 116 ARG A CB  
933  C CG  . ARG A 117 ? 0.2550 0.3617 0.2897 -0.0321 0.0201  -0.0699 116 ARG A CG  
934  C CD  . ARG A 117 ? 0.3003 0.4050 0.3361 -0.0313 0.0201  -0.0698 116 ARG A CD  
935  N NE  . ARG A 117 ? 0.3687 0.4741 0.4049 -0.0316 0.0204  -0.0703 116 ARG A NE  
936  C CZ  . ARG A 117 ? 0.4218 0.5288 0.4594 -0.0316 0.0206  -0.0716 116 ARG A CZ  
937  N NH1 . ARG A 117 ? 0.4247 0.5328 0.4634 -0.0314 0.0205  -0.0727 116 ARG A NH1 
938  N NH2 . ARG A 117 ? 0.4427 0.5502 0.4805 -0.0320 0.0208  -0.0720 116 ARG A NH2 
939  N N   . SER A 118 ? 0.2272 0.3339 0.2572 -0.0335 0.0197  -0.0672 117 SER A N   
940  C CA  . SER A 118 ? 0.1937 0.2996 0.2234 -0.0330 0.0194  -0.0666 117 SER A CA  
941  C C   . SER A 118 ? 0.1883 0.2949 0.2161 -0.0338 0.0193  -0.0658 117 SER A C   
942  O O   . SER A 118 ? 0.2271 0.3330 0.2545 -0.0335 0.0190  -0.0653 117 SER A O   
943  C CB  . SER A 118 ? 0.2822 0.3853 0.3118 -0.0323 0.0192  -0.0656 117 SER A CB  
944  O OG  . SER A 118 ? 0.3289 0.4311 0.3603 -0.0315 0.0192  -0.0663 117 SER A OG  
945  N N   . CYS A 119 ? 0.1890 0.2971 0.2158 -0.0347 0.0195  -0.0658 118 CYS A N   
946  C CA  . CYS A 119 ? 0.2268 0.3356 0.2518 -0.0355 0.0194  -0.0650 118 CYS A CA  
947  C C   . CYS A 119 ? 0.2084 0.3192 0.2328 -0.0365 0.0197  -0.0655 118 CYS A C   
948  O O   . CYS A 119 ? 0.2544 0.3659 0.2796 -0.0366 0.0199  -0.0662 118 CYS A O   
949  C CB  . CYS A 119 ? 0.1908 0.2973 0.2143 -0.0355 0.0192  -0.0633 118 CYS A CB  
950  S SG  . CYS A 119 ? 0.2344 0.3395 0.2571 -0.0359 0.0194  -0.0625 118 CYS A SG  
951  N N   . VAL A 120 ? 0.2633 0.3749 0.2861 -0.0371 0.0195  -0.0650 119 VAL A N   
952  C CA  . VAL A 120 ? 0.2823 0.3952 0.3039 -0.0381 0.0196  -0.0649 119 VAL A CA  
953  C C   . VAL A 120 ? 0.2769 0.3877 0.2964 -0.0384 0.0193  -0.0631 119 VAL A C   
954  O O   . VAL A 120 ? 0.2788 0.3875 0.2967 -0.0381 0.0188  -0.0619 119 VAL A O   
955  C CB  . VAL A 120 ? 0.3327 0.4470 0.3534 -0.0384 0.0193  -0.0652 119 VAL A CB  
956  C CG1 . VAL A 120 ? 0.3699 0.4854 0.3893 -0.0394 0.0194  -0.0651 119 VAL A CG1 
957  C CG2 . VAL A 120 ? 0.3417 0.4579 0.3646 -0.0380 0.0196  -0.0670 119 VAL A CG2 
958  N N   . THR A 121 ? 0.2692 0.3804 0.2885 -0.0391 0.0197  -0.0630 120 THR A N   
959  C CA  . THR A 121 ? 0.2743 0.3835 0.2917 -0.0394 0.0195  -0.0614 120 THR A CA  
960  C C   . THR A 121 ? 0.2781 0.3882 0.2937 -0.0404 0.0194  -0.0610 120 THR A C   
961  O O   . THR A 121 ? 0.3079 0.4203 0.3244 -0.0410 0.0199  -0.0621 120 THR A O   
962  C CB  . THR A 121 ? 0.2899 0.3983 0.3082 -0.0393 0.0199  -0.0613 120 THR A CB  
963  O OG1 . THR A 121 ? 0.3084 0.4152 0.3280 -0.0382 0.0197  -0.0614 120 THR A OG1 
964  C CG2 . THR A 121 ? 0.2734 0.3801 0.2899 -0.0397 0.0198  -0.0597 120 THR A CG2 
965  N N   . VAL A 122 ? 0.2975 0.4060 0.3107 -0.0406 0.0189  -0.0596 121 VAL A N   
966  C CA  . VAL A 122 ? 0.3344 0.4435 0.3458 -0.0416 0.0188  -0.0591 121 VAL A CA  
967  C C   . VAL A 122 ? 0.3299 0.4370 0.3397 -0.0420 0.0187  -0.0576 121 VAL A C   
968  O O   . VAL A 122 ? 0.2837 0.3884 0.2928 -0.0415 0.0183  -0.0564 121 VAL A O   
969  C CB  . VAL A 122 ? 0.3864 0.4955 0.3962 -0.0417 0.0182  -0.0588 121 VAL A CB  
970  C CG1 . VAL A 122 ? 0.4054 0.5119 0.4138 -0.0411 0.0176  -0.0574 121 VAL A CG1 
971  C CG2 . VAL A 122 ? 0.4041 0.5143 0.4123 -0.0426 0.0181  -0.0585 121 VAL A CG2 
972  N N   . PHE A 123 ? 0.3491 0.4573 0.3586 -0.0428 0.0190  -0.0577 122 PHE A N   
973  C CA  . PHE A 123 ? 0.3617 0.4684 0.3701 -0.0432 0.0190  -0.0564 122 PHE A CA  
974  C C   . PHE A 123 ? 0.4201 0.5261 0.4259 -0.0439 0.0186  -0.0552 122 PHE A C   
975  O O   . PHE A 123 ? 0.3787 0.4863 0.3839 -0.0445 0.0186  -0.0558 122 PHE A O   
976  C CB  . PHE A 123 ? 0.3724 0.4807 0.3822 -0.0437 0.0197  -0.0573 122 PHE A CB  
977  C CG  . PHE A 123 ? 0.3927 0.5018 0.4052 -0.0430 0.0202  -0.0585 122 PHE A CG  
978  C CD1 . PHE A 123 ? 0.4052 0.5122 0.4181 -0.0424 0.0202  -0.0580 122 PHE A CD1 
979  C CD2 . PHE A 123 ? 0.4171 0.5285 0.4313 -0.0429 0.0205  -0.0602 122 PHE A CD2 
980  C CE1 . PHE A 123 ? 0.4131 0.5198 0.4278 -0.0414 0.0203  -0.0589 122 PHE A CE1 
981  C CE2 . PHE A 123 ? 0.4193 0.5303 0.4353 -0.0419 0.0206  -0.0611 122 PHE A CE2 
982  C CZ  . PHE A 123 ? 0.4158 0.5243 0.4320 -0.0412 0.0205  -0.0604 122 PHE A CZ  
983  N N   . LYS A 124 ? 0.4486 0.5521 0.4528 -0.0439 0.0182  -0.0536 123 LYS A N   
984  C CA  . LYS A 124 ? 0.5169 0.6193 0.5185 -0.0445 0.0177  -0.0523 123 LYS A CA  
985  C C   . LYS A 124 ? 0.5187 0.6192 0.5195 -0.0448 0.0178  -0.0511 123 LYS A C   
986  O O   . LYS A 124 ? 0.5318 0.6315 0.5337 -0.0443 0.0180  -0.0511 123 LYS A O   
987  C CB  . LYS A 124 ? 0.5530 0.6539 0.5531 -0.0441 0.0170  -0.0515 123 LYS A CB  
988  C CG  . LYS A 124 ? 0.5980 0.7010 0.5984 -0.0441 0.0170  -0.0526 123 LYS A CG  
989  C CD  . LYS A 124 ? 0.6403 0.7423 0.6383 -0.0443 0.0163  -0.0516 123 LYS A CD  
990  C CE  . LYS A 124 ? 0.6769 0.7789 0.6731 -0.0452 0.0163  -0.0508 123 LYS A CE  
991  N NZ  . LYS A 124 ? 0.6870 0.7881 0.6809 -0.0454 0.0157  -0.0499 123 LYS A NZ  
992  N N   . PRO A 125 ? 0.5362 0.6360 0.5349 -0.0456 0.0175  -0.0500 124 PRO A N   
993  C CA  . PRO A 125 ? 0.5121 0.6101 0.5099 -0.0459 0.0176  -0.0488 124 PRO A CA  
994  C C   . PRO A 125 ? 0.4456 0.5410 0.4433 -0.0451 0.0173  -0.0478 124 PRO A C   
995  O O   . PRO A 125 ? 0.4401 0.5338 0.4364 -0.0447 0.0167  -0.0468 124 PRO A O   
996  C CB  . PRO A 125 ? 0.5637 0.6612 0.5591 -0.0467 0.0172  -0.0477 124 PRO A CB  
997  C CG  . PRO A 125 ? 0.6096 0.7095 0.6052 -0.0470 0.0173  -0.0489 124 PRO A CG  
998  C CD  . PRO A 125 ? 0.5960 0.6967 0.5931 -0.0462 0.0173  -0.0500 124 PRO A CD  
999  N N   . GLY A 126 ? 0.3841 0.4794 0.3834 -0.0448 0.0177  -0.0481 125 GLY A N   
1000 C CA  . GLY A 126 ? 0.3319 0.4246 0.3311 -0.0441 0.0175  -0.0471 125 GLY A CA  
1001 C C   . GLY A 126 ? 0.2970 0.3894 0.2975 -0.0431 0.0174  -0.0475 125 GLY A C   
1002 O O   . GLY A 126 ? 0.2668 0.3570 0.2672 -0.0424 0.0172  -0.0467 125 GLY A O   
1003 N N   . TYR A 127 ? 0.2712 0.3655 0.2728 -0.0428 0.0175  -0.0489 126 TYR A N   
1004 C CA  . TYR A 127 ? 0.2701 0.3641 0.2730 -0.0418 0.0174  -0.0494 126 TYR A CA  
1005 C C   . TYR A 127 ? 0.2562 0.3529 0.2609 -0.0417 0.0177  -0.0512 126 TYR A C   
1006 O O   . TYR A 127 ? 0.2690 0.3676 0.2734 -0.0424 0.0179  -0.0518 126 TYR A O   
1007 C CB  . TYR A 127 ? 0.3052 0.3972 0.3065 -0.0414 0.0166  -0.0482 126 TYR A CB  
1008 C CG  . TYR A 127 ? 0.3653 0.4582 0.3653 -0.0417 0.0163  -0.0483 126 TYR A CG  
1009 C CD1 . TYR A 127 ? 0.3807 0.4731 0.3786 -0.0425 0.0160  -0.0473 126 TYR A CD1 
1010 C CD2 . TYR A 127 ? 0.3750 0.4692 0.3760 -0.0413 0.0162  -0.0494 126 TYR A CD2 
1011 C CE1 . TYR A 127 ? 0.4027 0.4960 0.3993 -0.0428 0.0157  -0.0474 126 TYR A CE1 
1012 C CE2 . TYR A 127 ? 0.4078 0.5029 0.4076 -0.0416 0.0159  -0.0495 126 TYR A CE2 
1013 C CZ  . TYR A 127 ? 0.4257 0.5204 0.4234 -0.0423 0.0156  -0.0485 126 TYR A CZ  
1014 O OH  . TYR A 127 ? 0.4450 0.5405 0.4414 -0.0426 0.0153  -0.0486 126 TYR A OH  
1015 N N   . HIS A 128 ? 0.2119 0.3088 0.2184 -0.0409 0.0178  -0.0520 127 HIS A N   
1016 C CA  . HIS A 128 ? 0.2370 0.3362 0.2451 -0.0407 0.0180  -0.0536 127 HIS A CA  
1017 C C   . HIS A 128 ? 0.2036 0.3018 0.2118 -0.0398 0.0176  -0.0536 127 HIS A C   
1018 O O   . HIS A 128 ? 0.2069 0.3028 0.2145 -0.0393 0.0172  -0.0525 127 HIS A O   
1019 C CB  . HIS A 128 ? 0.2492 0.3502 0.2598 -0.0406 0.0188  -0.0551 127 HIS A CB  
1020 C CG  . HIS A 128 ? 0.3049 0.4045 0.3168 -0.0398 0.0190  -0.0550 127 HIS A CG  
1021 N ND1 . HIS A 128 ? 0.3151 0.4134 0.3267 -0.0400 0.0191  -0.0542 127 HIS A ND1 
1022 C CD2 . HIS A 128 ? 0.3002 0.3995 0.3138 -0.0389 0.0190  -0.0556 127 HIS A CD2 
1023 C CE1 . HIS A 128 ? 0.3054 0.4023 0.3182 -0.0391 0.0192  -0.0542 127 HIS A CE1 
1024 N NE2 . HIS A 128 ? 0.3056 0.4032 0.3197 -0.0385 0.0191  -0.0551 127 HIS A NE2 
1025 N N   . VAL A 129 ? 0.2029 0.3030 0.2118 -0.0398 0.0176  -0.0547 128 VAL A N   
1026 C CA  . VAL A 129 ? 0.1987 0.2983 0.2079 -0.0390 0.0172  -0.0549 128 VAL A CA  
1027 C C   . VAL A 129 ? 0.2051 0.3065 0.2169 -0.0385 0.0176  -0.0566 128 VAL A C   
1028 O O   . VAL A 129 ? 0.2272 0.3311 0.2401 -0.0390 0.0180  -0.0579 128 VAL A O   
1029 C CB  . VAL A 129 ? 0.2046 0.3048 0.2122 -0.0393 0.0167  -0.0546 128 VAL A CB  
1030 C CG1 . VAL A 129 ? 0.1975 0.2974 0.2056 -0.0385 0.0164  -0.0550 128 VAL A CG1 
1031 C CG2 . VAL A 129 ? 0.2246 0.3229 0.2295 -0.0398 0.0162  -0.0529 128 VAL A CG2 
1032 N N   . ASP A 130 ? 0.1654 0.2656 0.1784 -0.0376 0.0176  -0.0566 129 ASP A N   
1033 C CA  . ASP A 130 ? 0.1619 0.2634 0.1775 -0.0370 0.0180  -0.0581 129 ASP A CA  
1034 C C   . ASP A 130 ? 0.1760 0.2776 0.1918 -0.0365 0.0176  -0.0585 129 ASP A C   
1035 O O   . ASP A 130 ? 0.1455 0.2452 0.1608 -0.0359 0.0171  -0.0577 129 ASP A O   
1036 C CB  . ASP A 130 ? 0.2060 0.3060 0.2229 -0.0364 0.0182  -0.0579 129 ASP A CB  
1037 C CG  . ASP A 130 ? 0.2438 0.3437 0.2607 -0.0369 0.0187  -0.0577 129 ASP A CG  
1038 O OD1 . ASP A 130 ? 0.2393 0.3410 0.2561 -0.0376 0.0190  -0.0582 129 ASP A OD1 
1039 O OD2 . ASP A 130 ? 0.2605 0.3587 0.2777 -0.0365 0.0187  -0.0569 129 ASP A OD2 
1040 N N   . LEU A 131 ? 0.1989 0.3029 0.2154 -0.0368 0.0177  -0.0597 130 LEU A N   
1041 C CA  . LEU A 131 ? 0.2619 0.3663 0.2785 -0.0363 0.0174  -0.0602 130 LEU A CA  
1042 C C   . LEU A 131 ? 0.2129 0.3184 0.2322 -0.0357 0.0178  -0.0617 130 LEU A C   
1043 O O   . LEU A 131 ? 0.2574 0.3651 0.2783 -0.0359 0.0183  -0.0631 130 LEU A O   
1044 C CB  . LEU A 131 ? 0.3346 0.4409 0.3503 -0.0370 0.0173  -0.0607 130 LEU A CB  
1045 C CG  . LEU A 131 ? 0.4156 0.5214 0.4288 -0.0378 0.0170  -0.0595 130 LEU A CG  
1046 C CD1 . LEU A 131 ? 0.4915 0.5997 0.5049 -0.0386 0.0174  -0.0604 130 LEU A CD1 
1047 C CD2 . LEU A 131 ? 0.4446 0.5494 0.4561 -0.0376 0.0163  -0.0586 130 LEU A CD2 
1048 N N   . ALA A 132 ? 0.2036 0.3076 0.2235 -0.0348 0.0175  -0.0614 131 ALA A N   
1049 C CA  . ALA A 132 ? 0.1910 0.2959 0.2134 -0.0341 0.0178  -0.0627 131 ALA A CA  
1050 C C   . ALA A 132 ? 0.1818 0.2880 0.2043 -0.0341 0.0175  -0.0635 131 ALA A C   
1051 O O   . ALA A 132 ? 0.1907 0.2958 0.2114 -0.0341 0.0169  -0.0626 131 ALA A O   
1052 C CB  . ALA A 132 ? 0.2120 0.3146 0.2350 -0.0333 0.0176  -0.0621 131 ALA A CB  
1053 N N   . VAL A 133 ? 0.2083 0.3167 0.2327 -0.0340 0.0179  -0.0651 132 VAL A N   
1054 C CA  . VAL A 133 ? 0.1960 0.3061 0.2205 -0.0341 0.0178  -0.0660 132 VAL A CA  
1055 C C   . VAL A 133 ? 0.1607 0.2709 0.1872 -0.0333 0.0178  -0.0669 132 VAL A C   
1056 O O   . VAL A 133 ? 0.1637 0.2745 0.1924 -0.0329 0.0183  -0.0679 132 VAL A O   
1057 C CB  . VAL A 133 ? 0.1852 0.2981 0.2103 -0.0349 0.0182  -0.0672 132 VAL A CB  
1058 C CG1 . VAL A 133 ? 0.1776 0.2923 0.2031 -0.0349 0.0181  -0.0682 132 VAL A CG1 
1059 C CG2 . VAL A 133 ? 0.1910 0.3036 0.2139 -0.0357 0.0181  -0.0662 132 VAL A CG2 
1060 N N   . TYR A 134 ? 0.1720 0.2816 0.1978 -0.0329 0.0173  -0.0666 133 TYR A N   
1061 C CA  . TYR A 134 ? 0.1582 0.2677 0.1856 -0.0321 0.0172  -0.0673 133 TYR A CA  
1062 C C   . TYR A 134 ? 0.1649 0.2762 0.1925 -0.0322 0.0170  -0.0682 133 TYR A C   
1063 O O   . TYR A 134 ? 0.2212 0.3330 0.2470 -0.0328 0.0167  -0.0678 133 TYR A O   
1064 C CB  . TYR A 134 ? 0.1629 0.2697 0.1893 -0.0315 0.0166  -0.0660 133 TYR A CB  
1065 C CG  . TYR A 134 ? 0.1542 0.2589 0.1802 -0.0313 0.0167  -0.0649 133 TYR A CG  
1066 C CD1 . TYR A 134 ? 0.1476 0.2513 0.1715 -0.0319 0.0165  -0.0635 133 TYR A CD1 
1067 C CD2 . TYR A 134 ? 0.1299 0.2338 0.1577 -0.0306 0.0169  -0.0652 133 TYR A CD2 
1068 C CE1 . TYR A 134 ? 0.1923 0.2941 0.2157 -0.0318 0.0165  -0.0625 133 TYR A CE1 
1069 C CE2 . TYR A 134 ? 0.1845 0.2863 0.2118 -0.0305 0.0170  -0.0641 133 TYR A CE2 
1070 C CZ  . TYR A 134 ? 0.1643 0.2652 0.1894 -0.0311 0.0168  -0.0628 133 TYR A CZ  
1071 O OH  . TYR A 134 ? 0.1963 0.2953 0.2209 -0.0310 0.0168  -0.0617 133 TYR A OH  
1072 N N   . ALA A 135 ? 0.1770 0.2891 0.2066 -0.0316 0.0172  -0.0695 134 ALA A N   
1073 C CA  . ALA A 135 ? 0.1810 0.2944 0.2109 -0.0316 0.0170  -0.0703 134 ALA A CA  
1074 C C   . ALA A 135 ? 0.1981 0.3098 0.2272 -0.0310 0.0164  -0.0694 134 ALA A C   
1075 O O   . ALA A 135 ? 0.2078 0.3173 0.2368 -0.0305 0.0162  -0.0685 134 ALA A O   
1076 C CB  . ALA A 135 ? 0.2015 0.3168 0.2341 -0.0313 0.0175  -0.0721 134 ALA A CB  
1077 N N   . ASP A 136 ? 0.2187 0.3313 0.2472 -0.0311 0.0160  -0.0696 135 ASP A N   
1078 C CA  . ASP A 136 ? 0.2457 0.3567 0.2731 -0.0306 0.0154  -0.0688 135 ASP A CA  
1079 C C   . ASP A 136 ? 0.2423 0.3528 0.2719 -0.0297 0.0155  -0.0695 135 ASP A C   
1080 O O   . ASP A 136 ? 0.2436 0.3558 0.2750 -0.0296 0.0158  -0.0710 135 ASP A O   
1081 C CB  . ASP A 136 ? 0.3001 0.4124 0.3265 -0.0309 0.0151  -0.0690 135 ASP A CB  
1082 C CG  . ASP A 136 ? 0.3491 0.4598 0.3740 -0.0305 0.0144  -0.0679 135 ASP A CG  
1083 O OD1 . ASP A 136 ? 0.3620 0.4709 0.3874 -0.0298 0.0142  -0.0674 135 ASP A OD1 
1084 O OD2 . ASP A 136 ? 0.3965 0.5076 0.4197 -0.0309 0.0141  -0.0675 135 ASP A OD2 
1085 N N   . PRO A 137 ? 0.1918 0.2999 0.2210 -0.0291 0.0151  -0.0684 136 PRO A N   
1086 C CA  . PRO A 137 ? 0.2037 0.3113 0.2348 -0.0283 0.0152  -0.0691 136 PRO A CA  
1087 C C   . PRO A 137 ? 0.2561 0.3649 0.2877 -0.0281 0.0149  -0.0699 136 PRO A C   
1088 O O   . PRO A 137 ? 0.2857 0.3953 0.3195 -0.0276 0.0152  -0.0711 136 PRO A O   
1089 C CB  . PRO A 137 ? 0.2159 0.3207 0.2460 -0.0278 0.0147  -0.0675 136 PRO A CB  
1090 C CG  . PRO A 137 ? 0.1908 0.2946 0.2192 -0.0283 0.0147  -0.0664 136 PRO A CG  
1091 C CD  . PRO A 137 ? 0.2002 0.3060 0.2275 -0.0291 0.0148  -0.0667 136 PRO A CD  
1092 N N   . GLU A 138 ? 0.3006 0.4095 0.3303 -0.0284 0.0145  -0.0692 137 GLU A N   
1093 C CA  . GLU A 138 ? 0.3673 0.4772 0.3974 -0.0282 0.0142  -0.0699 137 GLU A CA  
1094 C C   . GLU A 138 ? 0.3282 0.4409 0.3600 -0.0285 0.0147  -0.0717 137 GLU A C   
1095 O O   . GLU A 138 ? 0.3391 0.4525 0.3725 -0.0280 0.0148  -0.0728 137 GLU A O   
1096 C CB  . GLU A 138 ? 0.4651 0.5747 0.4926 -0.0285 0.0136  -0.0689 137 GLU A CB  
1097 C CG  . GLU A 138 ? 0.5704 0.6796 0.5977 -0.0281 0.0131  -0.0688 137 GLU A CG  
1098 C CD  . GLU A 138 ? 0.6368 0.7437 0.6646 -0.0273 0.0129  -0.0681 137 GLU A CD  
1099 O OE1 . GLU A 138 ? 0.6577 0.7627 0.6846 -0.0272 0.0128  -0.0669 137 GLU A OE1 
1100 O OE2 . GLU A 138 ? 0.6647 0.7718 0.6937 -0.0267 0.0128  -0.0688 137 GLU A OE2 
1101 N N   . LEU A 139 ? 0.2861 0.4002 0.3176 -0.0292 0.0151  -0.0721 138 LEU A N   
1102 C CA  . LEU A 139 ? 0.2785 0.3952 0.3115 -0.0295 0.0156  -0.0737 138 LEU A CA  
1103 C C   . LEU A 139 ? 0.2947 0.4120 0.3302 -0.0292 0.0162  -0.0748 138 LEU A C   
1104 O O   . LEU A 139 ? 0.3154 0.4347 0.3524 -0.0294 0.0166  -0.0763 138 LEU A O   
1105 C CB  . LEU A 139 ? 0.2779 0.3959 0.3095 -0.0304 0.0157  -0.0737 138 LEU A CB  
1106 C CG  . LEU A 139 ? 0.2657 0.3832 0.2947 -0.0307 0.0151  -0.0725 138 LEU A CG  
1107 C CD1 . LEU A 139 ? 0.2672 0.3858 0.2949 -0.0316 0.0153  -0.0723 138 LEU A CD1 
1108 C CD2 . LEU A 139 ? 0.2763 0.3948 0.3054 -0.0305 0.0148  -0.0731 138 LEU A CD2 
1109 N N   . SER A 140 ? 0.2895 0.4049 0.3253 -0.0288 0.0162  -0.0741 139 SER A N   
1110 C CA  . SER A 140 ? 0.2977 0.4135 0.3356 -0.0286 0.0168  -0.0750 139 SER A CA  
1111 C C   . SER A 140 ? 0.3461 0.4607 0.3858 -0.0277 0.0168  -0.0753 139 SER A C   
1112 O O   . SER A 140 ? 0.4171 0.5315 0.4584 -0.0274 0.0172  -0.0758 139 SER A O   
1113 C CB  . SER A 140 ? 0.2366 0.3514 0.2737 -0.0289 0.0170  -0.0742 139 SER A CB  
1114 O OG  . SER A 140 ? 0.2253 0.3412 0.2608 -0.0298 0.0170  -0.0738 139 SER A OG  
1115 N N   . GLY A 141 ? 0.3603 0.4742 0.3996 -0.0273 0.0163  -0.0750 140 GLY A N   
1116 C CA  . GLY A 141 ? 0.3710 0.4840 0.4121 -0.0264 0.0163  -0.0754 140 GLY A CA  
1117 C C   . GLY A 141 ? 0.3807 0.4909 0.4210 -0.0259 0.0159  -0.0739 140 GLY A C   
1118 O O   . GLY A 141 ? 0.4052 0.5144 0.4470 -0.0252 0.0160  -0.0741 140 GLY A O   
1119 N N   . GLY A 142 ? 0.3645 0.4733 0.4023 -0.0262 0.0155  -0.0724 141 GLY A N   
1120 C CA  . GLY A 142 ? 0.3349 0.4410 0.3717 -0.0258 0.0151  -0.0709 141 GLY A CA  
1121 C C   . GLY A 142 ? 0.3482 0.4530 0.3847 -0.0258 0.0153  -0.0701 141 GLY A C   
1122 O O   . GLY A 142 ? 0.3377 0.4401 0.3730 -0.0255 0.0149  -0.0687 141 GLY A O   
1123 N N   . THR A 143 ? 0.3238 0.4299 0.3614 -0.0262 0.0159  -0.0709 142 THR A N   
1124 C CA  . THR A 143 ? 0.3573 0.4621 0.3948 -0.0262 0.0161  -0.0702 142 THR A CA  
1125 C C   . THR A 143 ? 0.2822 0.3875 0.3179 -0.0270 0.0162  -0.0696 142 THR A C   
1126 O O   . THR A 143 ? 0.2791 0.3863 0.3144 -0.0276 0.0163  -0.0702 142 THR A O   
1127 C CB  . THR A 143 ? 0.4490 0.5541 0.4889 -0.0258 0.0166  -0.0713 142 THR A CB  
1128 O OG1 . THR A 143 ? 0.5813 0.6841 0.6209 -0.0254 0.0165  -0.0703 142 THR A OG1 
1129 C CG2 . THR A 143 ? 0.4494 0.5565 0.4897 -0.0263 0.0169  -0.0724 142 THR A CG2 
1130 N N   . LEU A 144 ? 0.2368 0.3403 0.2713 -0.0271 0.0161  -0.0683 143 LEU A N   
1131 C CA  . LEU A 144 ? 0.2142 0.3179 0.2469 -0.0279 0.0162  -0.0676 143 LEU A CA  
1132 C C   . LEU A 144 ? 0.2047 0.3093 0.2389 -0.0281 0.0169  -0.0683 143 LEU A C   
1133 O O   . LEU A 144 ? 0.2086 0.3120 0.2438 -0.0276 0.0171  -0.0681 143 LEU A O   
1134 C CB  . LEU A 144 ? 0.2093 0.3104 0.2398 -0.0279 0.0157  -0.0657 143 LEU A CB  
1135 C CG  . LEU A 144 ? 0.2337 0.3350 0.2624 -0.0287 0.0158  -0.0649 143 LEU A CG  
1136 C CD1 . LEU A 144 ? 0.2025 0.3051 0.2296 -0.0294 0.0155  -0.0649 143 LEU A CD1 
1137 C CD2 . LEU A 144 ? 0.2320 0.3305 0.2589 -0.0286 0.0154  -0.0631 143 LEU A CD2 
1138 N N   . CYS A 145 ? 0.1681 0.2749 0.2024 -0.0288 0.0173  -0.0692 144 CYS A N   
1139 C CA  . CYS A 145 ? 0.1419 0.2493 0.1773 -0.0290 0.0177  -0.0699 144 CYS A CA  
1140 C C   . CYS A 145 ? 0.1447 0.2530 0.1787 -0.0299 0.0179  -0.0695 144 CYS A C   
1141 O O   . CYS A 145 ? 0.1782 0.2879 0.2110 -0.0305 0.0178  -0.0695 144 CYS A O   
1142 C CB  . CYS A 145 ? 0.1920 0.3010 0.2291 -0.0288 0.0179  -0.0716 144 CYS A CB  
1143 S SG  . CYS A 145 ? 0.2188 0.3268 0.2577 -0.0278 0.0176  -0.0721 144 CYS A SG  
1144 N N   . ILE A 146 ? 0.1817 0.2889 0.2156 -0.0299 0.0181  -0.0691 145 ILE A N   
1145 C CA  . ILE A 146 ? 0.1452 0.2530 0.1778 -0.0308 0.0183  -0.0686 145 ILE A CA  
1146 C C   . ILE A 146 ? 0.1591 0.2685 0.1927 -0.0311 0.0186  -0.0699 145 ILE A C   
1147 O O   . ILE A 146 ? 0.1546 0.2639 0.1899 -0.0305 0.0187  -0.0709 145 ILE A O   
1148 C CB  . ILE A 146 ? 0.1629 0.2683 0.1947 -0.0307 0.0183  -0.0673 145 ILE A CB  
1149 C CG1 . ILE A 146 ? 0.1605 0.2665 0.1908 -0.0316 0.0185  -0.0667 145 ILE A CG1 
1150 C CG2 . ILE A 146 ? 0.1567 0.2607 0.1900 -0.0299 0.0183  -0.0677 145 ILE A CG2 
1151 C CD1 . ILE A 146 ? 0.1698 0.2734 0.1990 -0.0315 0.0184  -0.0652 145 ILE A CD1 
1152 N N   . ALA A 147 ? 0.1844 0.2955 0.2170 -0.0320 0.0188  -0.0700 146 ALA A N   
1153 C CA  . ALA A 147 ? 0.1698 0.2828 0.2033 -0.0324 0.0192  -0.0712 146 ALA A CA  
1154 C C   . ALA A 147 ? 0.2078 0.3196 0.2415 -0.0324 0.0193  -0.0710 146 ALA A C   
1155 O O   . ALA A 147 ? 0.2113 0.3227 0.2436 -0.0329 0.0194  -0.0701 146 ALA A O   
1156 C CB  . ALA A 147 ? 0.2167 0.3318 0.2489 -0.0334 0.0193  -0.0713 146 ALA A CB  
1157 N N   . LYS A 148 ? 0.2319 0.3432 0.2673 -0.0317 0.0194  -0.0718 147 LYS A N   
1158 C CA  . LYS A 148 ? 0.2433 0.3535 0.2791 -0.0316 0.0196  -0.0717 147 LYS A CA  
1159 C C   . LYS A 148 ? 0.2559 0.3682 0.2925 -0.0321 0.0199  -0.0730 147 LYS A C   
1160 O O   . LYS A 148 ? 0.2833 0.3970 0.3212 -0.0319 0.0200  -0.0742 147 LYS A O   
1161 C CB  . LYS A 148 ? 0.2512 0.3596 0.2886 -0.0306 0.0194  -0.0718 147 LYS A CB  
1162 C CG  . LYS A 148 ? 0.3187 0.4249 0.3554 -0.0300 0.0191  -0.0706 147 LYS A CG  
1163 C CD  . LYS A 148 ? 0.3601 0.4648 0.3952 -0.0304 0.0191  -0.0692 147 LYS A CD  
1164 C CE  . LYS A 148 ? 0.3948 0.4971 0.4305 -0.0296 0.0190  -0.0686 147 LYS A CE  
1165 N NZ  . LYS A 148 ? 0.3779 0.4789 0.4120 -0.0300 0.0190  -0.0672 147 LYS A NZ  
1166 N N   . GLY A 149 ? 0.2568 0.3690 0.2927 -0.0325 0.0201  -0.0726 148 GLY A N   
1167 C CA  . GLY A 149 ? 0.2222 0.3360 0.2589 -0.0329 0.0204  -0.0736 148 GLY A CA  
1168 C C   . GLY A 149 ? 0.2853 0.4003 0.3204 -0.0340 0.0206  -0.0733 148 GLY A C   
1169 O O   . GLY A 149 ? 0.2796 0.3951 0.3134 -0.0344 0.0205  -0.0727 148 GLY A O   
1170 N N   . LYS A 150 ? 0.3291 0.4449 0.3645 -0.0343 0.0209  -0.0738 149 LYS A N   
1171 C CA  . LYS A 150 ? 0.3904 0.5077 0.4245 -0.0353 0.0211  -0.0736 149 LYS A CA  
1172 C C   . LYS A 150 ? 0.3821 0.5017 0.4172 -0.0357 0.0213  -0.0751 149 LYS A C   
1173 O O   . LYS A 150 ? 0.3557 0.4757 0.3925 -0.0351 0.0214  -0.0762 149 LYS A O   
1174 C CB  . LYS A 150 ? 0.4451 0.5610 0.4781 -0.0356 0.0211  -0.0726 149 LYS A CB  
1175 C CG  . LYS A 150 ? 0.4999 0.6139 0.5340 -0.0349 0.0211  -0.0725 149 LYS A CG  
1176 C CD  . LYS A 150 ? 0.5250 0.6376 0.5578 -0.0352 0.0212  -0.0712 149 LYS A CD  
1177 C CE  . LYS A 150 ? 0.5496 0.6608 0.5834 -0.0346 0.0212  -0.0713 149 LYS A CE  
1178 N NZ  . LYS A 150 ? 0.5537 0.6633 0.5862 -0.0349 0.0212  -0.0699 149 LYS A NZ  
1179 N N   . GLU A 151 ? 0.4560 0.5773 0.4901 -0.0366 0.0215  -0.0751 150 GLU A N   
1180 C CA  . GLU A 151 ? 0.5215 0.6452 0.5564 -0.0370 0.0218  -0.0765 150 GLU A CA  
1181 C C   . GLU A 151 ? 0.5400 0.6635 0.5764 -0.0366 0.0219  -0.0773 150 GLU A C   
1182 O O   . GLU A 151 ? 0.5419 0.6670 0.5795 -0.0366 0.0221  -0.0787 150 GLU A O   
1183 C CB  . GLU A 151 ? 0.5802 0.7055 0.6136 -0.0381 0.0219  -0.0763 150 GLU A CB  
1184 C CG  . GLU A 151 ? 0.6383 0.7629 0.6698 -0.0385 0.0217  -0.0749 150 GLU A CG  
1185 C CD  . GLU A 151 ? 0.6912 0.8179 0.7215 -0.0395 0.0219  -0.0750 150 GLU A CD  
1186 O OE1 . GLU A 151 ? 0.7220 0.8509 0.7531 -0.0397 0.0220  -0.0762 150 GLU A OE1 
1187 O OE2 . GLU A 151 ? 0.6998 0.8260 0.7284 -0.0401 0.0218  -0.0738 150 GLU A OE2 
1188 N N   . ASN A 152 ? 0.5629 0.6843 0.5991 -0.0363 0.0219  -0.0765 151 ASN A N   
1189 C CA  . ASN A 152 ? 0.5945 0.7153 0.6322 -0.0358 0.0220  -0.0771 151 ASN A CA  
1190 C C   . ASN A 152 ? 0.5081 0.6284 0.5476 -0.0349 0.0219  -0.0779 151 ASN A C   
1191 O O   . ASN A 152 ? 0.4857 0.6063 0.5266 -0.0346 0.0221  -0.0788 151 ASN A O   
1192 C CB  . ASN A 152 ? 0.7163 0.8349 0.7532 -0.0357 0.0220  -0.0758 151 ASN A CB  
1193 C CG  . ASN A 152 ? 0.8277 0.9462 0.8653 -0.0357 0.0222  -0.0762 151 ASN A CG  
1194 O OD1 . ASN A 152 ? 0.9188 1.0388 0.9559 -0.0364 0.0224  -0.0765 151 ASN A OD1 
1195 N ND2 . ASN A 152 ? 0.8568 0.9737 0.8956 -0.0349 0.0221  -0.0763 151 ASN A ND2 
1196 N N   . SER A 153 ? 0.4452 0.5647 0.4846 -0.0345 0.0217  -0.0775 152 SER A N   
1197 C CA  . SER A 153 ? 0.4033 0.5216 0.4443 -0.0335 0.0215  -0.0779 152 SER A CA  
1198 C C   . SER A 153 ? 0.4184 0.5385 0.4611 -0.0333 0.0216  -0.0795 152 SER A C   
1199 O O   . SER A 153 ? 0.4027 0.5248 0.4451 -0.0338 0.0217  -0.0802 152 SER A O   
1200 C CB  . SER A 153 ? 0.3782 0.4951 0.4186 -0.0331 0.0212  -0.0771 152 SER A CB  
1201 N N   . GLY A 154 ? 0.4308 0.5501 0.4751 -0.0326 0.0216  -0.0801 153 GLY A N   
1202 C CA  . GLY A 154 ? 0.4635 0.5840 0.5095 -0.0323 0.0216  -0.0815 153 GLY A CA  
1203 C C   . GLY A 154 ? 0.4982 0.6181 0.5445 -0.0318 0.0213  -0.0814 153 GLY A C   
1204 O O   . GLY A 154 ? 0.4836 0.6022 0.5288 -0.0317 0.0211  -0.0803 153 GLY A O   
1205 N N   . ASP A 155 ? 0.5360 0.6570 0.5838 -0.0315 0.0213  -0.0826 154 ASP A N   
1206 C CA  . ASP A 155 ? 0.5818 0.7025 0.6299 -0.0310 0.0211  -0.0827 154 ASP A CA  
1207 C C   . ASP A 155 ? 0.6212 0.7393 0.6696 -0.0302 0.0208  -0.0818 154 ASP A C   
1208 O O   . ASP A 155 ? 0.6201 0.7374 0.6681 -0.0299 0.0206  -0.0813 154 ASP A O   
1209 C CB  . ASP A 155 ? 0.5874 0.7097 0.6372 -0.0308 0.0212  -0.0842 154 ASP A CB  
1210 C CG  . ASP A 155 ? 0.5879 0.7100 0.6381 -0.0304 0.0209  -0.0844 154 ASP A CG  
1211 O OD1 . ASP A 155 ? 0.5918 0.7146 0.6408 -0.0307 0.0208  -0.0840 154 ASP A OD1 
1212 O OD2 . ASP A 155 ? 0.5924 0.7135 0.6440 -0.0297 0.0208  -0.0848 154 ASP A OD2 
1213 N N   . GLU A 156 ? 0.6642 0.7808 0.7132 -0.0298 0.0209  -0.0816 155 GLU A N   
1214 C CA  . GLU A 156 ? 0.7007 0.8149 0.7501 -0.0290 0.0206  -0.0808 155 GLU A CA  
1215 C C   . GLU A 156 ? 0.6672 0.7800 0.7148 -0.0291 0.0204  -0.0792 155 GLU A C   
1216 O O   . GLU A 156 ? 0.6527 0.7638 0.7004 -0.0285 0.0202  -0.0785 155 GLU A O   
1217 C CB  . GLU A 156 ? 0.7760 0.8892 0.8263 -0.0287 0.0207  -0.0808 155 GLU A CB  
1218 C CG  . GLU A 156 ? 0.8416 0.9521 0.8924 -0.0279 0.0205  -0.0800 155 GLU A CG  
1219 C CD  . GLU A 156 ? 0.8873 0.9969 0.9385 -0.0278 0.0206  -0.0798 155 GLU A CD  
1220 O OE1 . GLU A 156 ? 0.9019 1.0093 0.9531 -0.0273 0.0205  -0.0789 155 GLU A OE1 
1221 O OE2 . GLU A 156 ? 0.9008 1.0119 0.9523 -0.0282 0.0209  -0.0806 155 GLU A OE2 
1222 N N   . HIS A 157 ? 0.6518 0.7654 0.6979 -0.0299 0.0206  -0.0787 156 HIS A N   
1223 C CA  . HIS A 157 ? 0.6404 0.7526 0.6847 -0.0301 0.0205  -0.0772 156 HIS A CA  
1224 C C   . HIS A 157 ? 0.5692 0.6824 0.6120 -0.0307 0.0204  -0.0769 156 HIS A C   
1225 O O   . HIS A 157 ? 0.5936 0.7061 0.6348 -0.0310 0.0203  -0.0757 156 HIS A O   
1226 C CB  . HIS A 157 ? 0.6857 0.7974 0.7292 -0.0305 0.0206  -0.0767 156 HIS A CB  
1227 C CG  . HIS A 157 ? 0.7302 0.8403 0.7748 -0.0299 0.0207  -0.0766 156 HIS A CG  
1228 N ND1 . HIS A 157 ? 0.7390 0.8471 0.7844 -0.0290 0.0204  -0.0762 156 HIS A ND1 
1229 C CD2 . HIS A 157 ? 0.7404 0.8506 0.7855 -0.0300 0.0209  -0.0768 156 HIS A CD2 
1230 C CE1 . HIS A 157 ? 0.7446 0.8516 0.7909 -0.0286 0.0205  -0.0762 156 HIS A CE1 
1231 N NE2 . HIS A 157 ? 0.7452 0.8534 0.7913 -0.0292 0.0207  -0.0766 156 HIS A NE2 
1232 N N   . ARG A 158 ? 0.4826 0.5977 0.5260 -0.0308 0.0204  -0.0779 157 ARG A N   
1233 C CA  . ARG A 158 ? 0.3886 0.5048 0.4307 -0.0313 0.0203  -0.0776 157 ARG A CA  
1234 C C   . ARG A 158 ? 0.3454 0.4609 0.3882 -0.0306 0.0200  -0.0776 157 ARG A C   
1235 O O   . ARG A 158 ? 0.3372 0.4534 0.3814 -0.0303 0.0200  -0.0787 157 ARG A O   
1236 C CB  . ARG A 158 ? 0.3642 0.4833 0.4066 -0.0320 0.0206  -0.0788 157 ARG A CB  
1237 C CG  . ARG A 158 ? 0.3347 0.4546 0.3764 -0.0327 0.0208  -0.0788 157 ARG A CG  
1238 C CD  . ARG A 158 ? 0.3446 0.4670 0.3873 -0.0331 0.0211  -0.0803 157 ARG A CD  
1239 N NE  . ARG A 158 ? 0.3592 0.4835 0.4006 -0.0339 0.0212  -0.0803 157 ARG A NE  
1240 C CZ  . ARG A 158 ? 0.3753 0.5007 0.4159 -0.0347 0.0214  -0.0803 157 ARG A CZ  
1241 N NH1 . ARG A 158 ? 0.3991 0.5262 0.4385 -0.0354 0.0215  -0.0803 157 ARG A NH1 
1242 N NH2 . ARG A 158 ? 0.3821 0.5070 0.4229 -0.0347 0.0216  -0.0802 157 ARG A NH2 
1243 N N   . LEU A 159 ? 0.3114 0.4253 0.3530 -0.0305 0.0198  -0.0763 158 LEU A N   
1244 C CA  . LEU A 159 ? 0.3181 0.4313 0.3602 -0.0298 0.0195  -0.0763 158 LEU A CA  
1245 C C   . LEU A 159 ? 0.2870 0.3997 0.3275 -0.0300 0.0193  -0.0751 158 LEU A C   
1246 O O   . LEU A 159 ? 0.2918 0.4043 0.3308 -0.0306 0.0193  -0.0742 158 LEU A O   
1247 C CB  . LEU A 159 ? 0.3579 0.4690 0.4014 -0.0289 0.0194  -0.0763 158 LEU A CB  
1248 C CG  . LEU A 159 ? 0.3824 0.4912 0.4254 -0.0286 0.0193  -0.0750 158 LEU A CG  
1249 C CD1 . LEU A 159 ? 0.3941 0.5008 0.4380 -0.0277 0.0190  -0.0747 158 LEU A CD1 
1250 C CD2 . LEU A 159 ? 0.3905 0.4994 0.4342 -0.0287 0.0196  -0.0755 158 LEU A CD2 
1251 N N   . TRP A 160 ? 0.2614 0.3739 0.3023 -0.0296 0.0190  -0.0753 159 TRP A N   
1252 C CA  . TRP A 160 ? 0.2540 0.3658 0.2936 -0.0296 0.0188  -0.0742 159 TRP A CA  
1253 C C   . TRP A 160 ? 0.2740 0.3832 0.3141 -0.0287 0.0185  -0.0735 159 TRP A C   
1254 O O   . TRP A 160 ? 0.3205 0.4294 0.3620 -0.0280 0.0184  -0.0741 159 TRP A O   
1255 C CB  . TRP A 160 ? 0.1880 0.3016 0.2278 -0.0297 0.0187  -0.0749 159 TRP A CB  
1256 C CG  . TRP A 160 ? 0.2162 0.3321 0.2551 -0.0306 0.0189  -0.0754 159 TRP A CG  
1257 C CD1 . TRP A 160 ? 0.2105 0.3286 0.2504 -0.0308 0.0191  -0.0768 159 TRP A CD1 
1258 C CD2 . TRP A 160 ? 0.2339 0.3505 0.2710 -0.0313 0.0189  -0.0745 159 TRP A CD2 
1259 N NE1 . TRP A 160 ? 0.2439 0.3639 0.2827 -0.0317 0.0193  -0.0768 159 TRP A NE1 
1260 C CE2 . TRP A 160 ? 0.2018 0.3210 0.2388 -0.0320 0.0191  -0.0754 159 TRP A CE2 
1261 C CE3 . TRP A 160 ? 0.1594 0.2746 0.1948 -0.0315 0.0187  -0.0730 159 TRP A CE3 
1262 C CZ2 . TRP A 160 ? 0.2215 0.3418 0.2568 -0.0329 0.0192  -0.0749 159 TRP A CZ2 
1263 C CZ3 . TRP A 160 ? 0.1959 0.3123 0.2297 -0.0324 0.0188  -0.0724 159 TRP A CZ3 
1264 C CH2 . TRP A 160 ? 0.1957 0.3146 0.2294 -0.0330 0.0190  -0.0734 159 TRP A CH2 
1265 N N   . GLN A 161 ? 0.2663 0.3737 0.3053 -0.0287 0.0185  -0.0722 160 GLN A N   
1266 C CA  . GLN A 161 ? 0.2567 0.3617 0.2964 -0.0278 0.0182  -0.0715 160 GLN A CA  
1267 C C   . GLN A 161 ? 0.2097 0.3134 0.2482 -0.0276 0.0179  -0.0704 160 GLN A C   
1268 O O   . GLN A 161 ? 0.2154 0.3193 0.2522 -0.0282 0.0179  -0.0695 160 GLN A O   
1269 C CB  . GLN A 161 ? 0.2889 0.3925 0.3282 -0.0279 0.0184  -0.0708 160 GLN A CB  
1270 C CG  . GLN A 161 ? 0.3105 0.4115 0.3506 -0.0270 0.0182  -0.0703 160 GLN A CG  
1271 C CD  . GLN A 161 ? 0.3653 0.4650 0.4050 -0.0270 0.0183  -0.0696 160 GLN A CD  
1272 O OE1 . GLN A 161 ? 0.3610 0.4603 0.3991 -0.0275 0.0183  -0.0686 160 GLN A OE1 
1273 N NE2 . GLN A 161 ? 0.4049 0.5042 0.4462 -0.0266 0.0184  -0.0702 160 GLN A NE2 
1274 N N   . ILE A 162 ? 0.1988 0.3012 0.2384 -0.0267 0.0177  -0.0704 161 ILE A N   
1275 C CA  . ILE A 162 ? 0.2196 0.3208 0.2584 -0.0264 0.0173  -0.0694 161 ILE A CA  
1276 C C   . ILE A 162 ? 0.2029 0.3023 0.2402 -0.0266 0.0173  -0.0679 161 ILE A C   
1277 O O   . ILE A 162 ? 0.2017 0.2998 0.2393 -0.0264 0.0174  -0.0676 161 ILE A O   
1278 C CB  . ILE A 162 ? 0.2825 0.3825 0.3228 -0.0255 0.0171  -0.0697 161 ILE A CB  
1279 C CG1 . ILE A 162 ? 0.3055 0.4045 0.3448 -0.0252 0.0167  -0.0688 161 ILE A CG1 
1280 C CG2 . ILE A 162 ? 0.2856 0.3836 0.3269 -0.0249 0.0171  -0.0695 161 ILE A CG2 
1281 C CD1 . ILE A 162 ? 0.3367 0.4346 0.3773 -0.0244 0.0165  -0.0690 161 ILE A CD1 
1282 N N   . SER A 163 ? 0.2013 0.3006 0.2371 -0.0268 0.0171  -0.0670 162 SER A N   
1283 C CA  . SER A 163 ? 0.1905 0.2883 0.2245 -0.0272 0.0171  -0.0655 162 SER A CA  
1284 C C   . SER A 163 ? 0.1774 0.2742 0.2105 -0.0269 0.0167  -0.0645 162 SER A C   
1285 O O   . SER A 163 ? 0.1746 0.2719 0.2074 -0.0268 0.0164  -0.0647 162 SER A O   
1286 C CB  . SER A 163 ? 0.3237 0.4233 0.3566 -0.0282 0.0173  -0.0655 162 SER A CB  
1287 O OG  . SER A 163 ? 0.4638 0.5621 0.4950 -0.0286 0.0173  -0.0641 162 SER A OG  
1288 N N   . ASP A 164 ? 0.1491 0.2436 0.1812 -0.0267 0.0165  -0.0631 163 ASP A N   
1289 C CA  . ASP A 164 ? 0.1192 0.2116 0.1496 -0.0264 0.0158  -0.0617 163 ASP A CA  
1290 C C   . ASP A 164 ? 0.1348 0.2254 0.1629 -0.0268 0.0156  -0.0601 163 ASP A C   
1291 O O   . ASP A 164 ? 0.1475 0.2359 0.1754 -0.0263 0.0154  -0.0590 163 ASP A O   
1292 C CB  . ASP A 164 ? 0.1361 0.2270 0.1681 -0.0254 0.0157  -0.0618 163 ASP A CB  
1293 C CG  . ASP A 164 ? 0.1389 0.2277 0.1693 -0.0250 0.0149  -0.0604 163 ASP A CG  
1294 O OD1 . ASP A 164 ? 0.1626 0.2512 0.1909 -0.0254 0.0145  -0.0597 163 ASP A OD1 
1295 O OD2 . ASP A 164 ? 0.1588 0.2460 0.1901 -0.0242 0.0148  -0.0602 163 ASP A OD2 
1296 N N   . PRO A 165 ? 0.1672 0.2587 0.1937 -0.0276 0.0156  -0.0598 164 PRO A N   
1297 C CA  . PRO A 165 ? 0.1586 0.2484 0.1830 -0.0280 0.0154  -0.0582 164 PRO A CA  
1298 C C   . PRO A 165 ? 0.1779 0.2653 0.2005 -0.0277 0.0147  -0.0566 164 PRO A C   
1299 O O   . PRO A 165 ? 0.1676 0.2529 0.1891 -0.0276 0.0145  -0.0554 164 PRO A O   
1300 C CB  . PRO A 165 ? 0.2040 0.2956 0.2272 -0.0290 0.0156  -0.0584 164 PRO A CB  
1301 C CG  . PRO A 165 ? 0.2153 0.3089 0.2393 -0.0290 0.0155  -0.0596 164 PRO A CG  
1302 C CD  . PRO A 165 ? 0.1993 0.2934 0.2259 -0.0283 0.0158  -0.0609 164 PRO A CD  
1303 N N   . GLN A 166 ? 0.1964 0.2840 0.2186 -0.0275 0.0142  -0.0567 165 GLN A N   
1304 C CA  . GLN A 166 ? 0.2596 0.3448 0.2800 -0.0272 0.0135  -0.0552 165 GLN A CA  
1305 C C   . GLN A 166 ? 0.2106 0.2939 0.2321 -0.0262 0.0134  -0.0549 165 GLN A C   
1306 O O   . GLN A 166 ? 0.1972 0.2781 0.2172 -0.0260 0.0129  -0.0534 165 GLN A O   
1307 C CB  . GLN A 166 ? 0.3834 0.4694 0.4029 -0.0273 0.0130  -0.0553 165 GLN A CB  
1308 C CG  . GLN A 166 ? 0.5018 0.5880 0.5189 -0.0281 0.0128  -0.0545 165 GLN A CG  
1309 C CD  . GLN A 166 ? 0.5965 0.6847 0.6132 -0.0285 0.0127  -0.0552 165 GLN A CD  
1310 O OE1 . GLN A 166 ? 0.6559 0.7460 0.6743 -0.0284 0.0130  -0.0567 165 GLN A OE1 
1311 N NE2 . GLN A 166 ? 0.6262 0.7137 0.6405 -0.0289 0.0122  -0.0541 165 GLN A NE2 
1312 N N   . GLY A 167 ? 0.1736 0.2577 0.1975 -0.0257 0.0137  -0.0561 166 GLY A N   
1313 C CA  . GLY A 167 ? 0.1408 0.2232 0.1659 -0.0248 0.0137  -0.0558 166 GLY A CA  
1314 C C   . GLY A 167 ? 0.1244 0.2054 0.1492 -0.0249 0.0139  -0.0551 166 GLY A C   
1315 O O   . GLY A 167 ? 0.1392 0.2180 0.1636 -0.0244 0.0136  -0.0540 166 GLY A O   
1316 N N   . PHE A 168 ? 0.1174 0.2000 0.1427 -0.0255 0.0145  -0.0557 167 PHE A N   
1317 C CA  . PHE A 168 ? 0.0933 0.1747 0.1183 -0.0256 0.0148  -0.0550 167 PHE A CA  
1318 C C   . PHE A 168 ? 0.0990 0.1784 0.1212 -0.0259 0.0142  -0.0532 167 PHE A C   
1319 O O   . PHE A 168 ? 0.0945 0.1717 0.1163 -0.0256 0.0141  -0.0521 167 PHE A O   
1320 C CB  . PHE A 168 ? 0.1160 0.1996 0.1419 -0.0263 0.0155  -0.0560 167 PHE A CB  
1321 C CG  . PHE A 168 ? 0.1111 0.1936 0.1366 -0.0264 0.0158  -0.0553 167 PHE A CG  
1322 C CD1 . PHE A 168 ? 0.0825 0.1636 0.1093 -0.0257 0.0159  -0.0552 167 PHE A CD1 
1323 C CD2 . PHE A 168 ? 0.1217 0.2045 0.1457 -0.0273 0.0159  -0.0548 167 PHE A CD2 
1324 C CE1 . PHE A 168 ? 0.0990 0.1788 0.1254 -0.0258 0.0161  -0.0544 167 PHE A CE1 
1325 C CE2 . PHE A 168 ? 0.1330 0.2148 0.1567 -0.0274 0.0162  -0.0541 167 PHE A CE2 
1326 C CZ  . PHE A 168 ? 0.1039 0.1842 0.1287 -0.0267 0.0163  -0.0540 167 PHE A CZ  
1327 N N   . GLN A 169 ? 0.1253 0.2054 0.1458 -0.0266 0.0140  -0.0528 168 GLN A N   
1328 C CA  . GLN A 169 ? 0.1076 0.1857 0.1253 -0.0270 0.0135  -0.0510 168 GLN A CA  
1329 C C   . GLN A 169 ? 0.0986 0.1743 0.1157 -0.0262 0.0128  -0.0499 168 GLN A C   
1330 O O   . GLN A 169 ? 0.0981 0.1716 0.1138 -0.0262 0.0125  -0.0485 168 GLN A O   
1331 C CB  . GLN A 169 ? 0.1148 0.1941 0.1309 -0.0277 0.0132  -0.0510 168 GLN A CB  
1332 C CG  . GLN A 169 ? 0.1838 0.2654 0.2004 -0.0285 0.0138  -0.0519 168 GLN A CG  
1333 C CD  . GLN A 169 ? 0.2420 0.3251 0.2572 -0.0292 0.0137  -0.0521 168 GLN A CD  
1334 O OE1 . GLN A 169 ? 0.3053 0.3908 0.3214 -0.0297 0.0142  -0.0532 168 GLN A OE1 
1335 N NE2 . GLN A 169 ? 0.2677 0.3497 0.2811 -0.0292 0.0130  -0.0510 168 GLN A NE2 
1336 N N   . ASP A 170 ? 0.0993 0.1753 0.1173 -0.0257 0.0126  -0.0505 169 ASP A N   
1337 C CA  . ASP A 170 ? 0.0920 0.1659 0.1096 -0.0249 0.0120  -0.0496 169 ASP A CA  
1338 C C   . ASP A 170 ? 0.1046 0.1767 0.1233 -0.0243 0.0121  -0.0492 169 ASP A C   
1339 O O   . ASP A 170 ? 0.1087 0.1785 0.1263 -0.0239 0.0116  -0.0479 169 ASP A O   
1340 C CB  . ASP A 170 ? 0.1186 0.1934 0.1373 -0.0245 0.0118  -0.0505 169 ASP A CB  
1341 C CG  . ASP A 170 ? 0.1862 0.2589 0.2047 -0.0237 0.0112  -0.0496 169 ASP A CG  
1342 O OD1 . ASP A 170 ? 0.1733 0.2441 0.1897 -0.0238 0.0106  -0.0481 169 ASP A OD1 
1343 O OD2 . ASP A 170 ? 0.2260 0.2989 0.2464 -0.0230 0.0112  -0.0505 169 ASP A OD2 
1344 N N   . ARG A 171 ? 0.1004 0.1738 0.1214 -0.0241 0.0128  -0.0505 170 ARG A N   
1345 C CA  . ARG A 171 ? 0.1039 0.1758 0.1260 -0.0235 0.0129  -0.0502 170 ARG A CA  
1346 C C   . ARG A 171 ? 0.0896 0.1599 0.1102 -0.0238 0.0129  -0.0489 170 ARG A C   
1347 O O   . ARG A 171 ? 0.0968 0.1648 0.1171 -0.0233 0.0127  -0.0479 170 ARG A O   
1348 C CB  . ARG A 171 ? 0.1186 0.1923 0.1435 -0.0232 0.0136  -0.0519 170 ARG A CB  
1349 C CG  . ARG A 171 ? 0.2163 0.2912 0.2429 -0.0228 0.0136  -0.0532 170 ARG A CG  
1350 C CD  . ARG A 171 ? 0.2342 0.3090 0.2634 -0.0219 0.0139  -0.0540 170 ARG A CD  
1351 N NE  . ARG A 171 ? 0.2381 0.3136 0.2684 -0.0214 0.0137  -0.0549 170 ARG A NE  
1352 C CZ  . ARG A 171 ? 0.2482 0.3227 0.2799 -0.0206 0.0135  -0.0550 170 ARG A CZ  
1353 N NH1 . ARG A 171 ? 0.2537 0.3263 0.2859 -0.0200 0.0136  -0.0543 170 ARG A NH1 
1354 N NH2 . ARG A 171 ? 0.1955 0.2708 0.2279 -0.0203 0.0133  -0.0557 170 ARG A NH2 
1355 N N   . ILE A 172 ? 0.0705 0.1419 0.0901 -0.0247 0.0132  -0.0489 171 ILE A N   
1356 C CA  . ILE A 172 ? 0.0636 0.1335 0.0816 -0.0250 0.0132  -0.0476 171 ILE A CA  
1357 C C   . ILE A 172 ? 0.0883 0.1559 0.1039 -0.0250 0.0124  -0.0459 171 ILE A C   
1358 O O   . ILE A 172 ? 0.0934 0.1589 0.1081 -0.0248 0.0122  -0.0446 171 ILE A O   
1359 C CB  . ILE A 172 ? 0.0507 0.1225 0.0682 -0.0260 0.0137  -0.0481 171 ILE A CB  
1360 C CG1 . ILE A 172 ? 0.0757 0.1496 0.0957 -0.0260 0.0145  -0.0498 171 ILE A CG1 
1361 C CG2 . ILE A 172 ? 0.0549 0.1251 0.0706 -0.0265 0.0136  -0.0467 171 ILE A CG2 
1362 C CD1 . ILE A 172 ? 0.0792 0.1520 0.1007 -0.0254 0.0148  -0.0498 171 ILE A CD1 
1363 N N   . ALA A 173 ? 0.0781 0.1463 0.0926 -0.0252 0.0120  -0.0458 172 ALA A N   
1364 C CA  . ALA A 173 ? 0.0820 0.1480 0.0941 -0.0252 0.0113  -0.0441 172 ALA A CA  
1365 C C   . ALA A 173 ? 0.0909 0.1549 0.1034 -0.0243 0.0108  -0.0435 172 ALA A C   
1366 O O   . ALA A 173 ? 0.1029 0.1646 0.1137 -0.0242 0.0103  -0.0420 172 ALA A O   
1367 C CB  . ALA A 173 ? 0.1006 0.1677 0.1115 -0.0256 0.0109  -0.0443 172 ALA A CB  
1368 N N   . SER A 174 ? 0.1021 0.1667 0.1167 -0.0236 0.0110  -0.0446 173 SER A N   
1369 C CA  . SER A 174 ? 0.1132 0.1761 0.1283 -0.0228 0.0105  -0.0442 173 SER A CA  
1370 C C   . SER A 174 ? 0.1107 0.1721 0.1271 -0.0221 0.0107  -0.0440 173 SER A C   
1371 O O   . SER A 174 ? 0.1093 0.1690 0.1259 -0.0214 0.0102  -0.0434 173 SER A O   
1372 C CB  . SER A 174 ? 0.1204 0.1849 0.1371 -0.0224 0.0105  -0.0455 173 SER A CB  
1373 O OG  . SER A 174 ? 0.1388 0.2047 0.1543 -0.0230 0.0103  -0.0457 173 SER A OG  
1374 N N   . LYS A 175 ? 0.1213 0.1834 0.1386 -0.0223 0.0113  -0.0445 174 LYS A N   
1375 C CA  . LYS A 175 ? 0.1015 0.1623 0.1202 -0.0216 0.0115  -0.0444 174 LYS A CA  
1376 C C   . LYS A 175 ? 0.0947 0.1526 0.1119 -0.0213 0.0109  -0.0426 174 LYS A C   
1377 O O   . LYS A 175 ? 0.1423 0.1987 0.1605 -0.0204 0.0108  -0.0424 174 LYS A O   
1378 C CB  . LYS A 175 ? 0.0781 0.1401 0.0978 -0.0220 0.0123  -0.0451 174 LYS A CB  
1379 C CG  . LYS A 175 ? 0.1039 0.1646 0.1250 -0.0214 0.0125  -0.0450 174 LYS A CG  
1380 C CD  . LYS A 175 ? 0.1108 0.1728 0.1326 -0.0218 0.0133  -0.0456 174 LYS A CD  
1381 C CE  . LYS A 175 ? 0.1276 0.1882 0.1506 -0.0212 0.0135  -0.0454 174 LYS A CE  
1382 N NZ  . LYS A 175 ? 0.1678 0.2287 0.1934 -0.0202 0.0136  -0.0464 174 LYS A NZ  
1383 N N   . LEU A 176 ? 0.0567 0.1136 0.0714 -0.0219 0.0106  -0.0413 175 LEU A N   
1384 C CA  . LEU A 176 ? 0.0740 0.1282 0.0870 -0.0217 0.0101  -0.0396 175 LEU A CA  
1385 C C   . LEU A 176 ? 0.0872 0.1409 0.0977 -0.0222 0.0095  -0.0385 175 LEU A C   
1386 O O   . LEU A 176 ? 0.0916 0.1471 0.1018 -0.0227 0.0096  -0.0393 175 LEU A O   
1387 C CB  . LEU A 176 ? 0.1118 0.1651 0.1242 -0.0220 0.0104  -0.0389 175 LEU A CB  
1388 C CG  . LEU A 176 ? 0.0899 0.1436 0.1048 -0.0215 0.0110  -0.0399 175 LEU A CG  
1389 C CD1 . LEU A 176 ? 0.1122 0.1660 0.1267 -0.0220 0.0115  -0.0396 175 LEU A CD1 
1390 C CD2 . LEU A 176 ? 0.0991 0.1506 0.1146 -0.0204 0.0107  -0.0392 175 LEU A CD2 
1391 N N   . SER A 177 ? 0.0978 0.1490 0.1066 -0.0220 0.0089  -0.0369 176 SER A N   
1392 C CA  . SER A 177 ? 0.1104 0.1609 0.1167 -0.0224 0.0083  -0.0358 176 SER A CA  
1393 C C   . SER A 177 ? 0.0932 0.1416 0.0975 -0.0227 0.0081  -0.0341 176 SER A C   
1394 O O   . SER A 177 ? 0.0928 0.1400 0.0976 -0.0225 0.0083  -0.0337 176 SER A O   
1395 C CB  . SER A 177 ? 0.1334 0.1830 0.1395 -0.0218 0.0076  -0.0354 176 SER A CB  
1396 O OG  . SER A 177 ? 0.1584 0.2055 0.1643 -0.0211 0.0072  -0.0344 176 SER A OG  
1397 N N   . GLY A 178 ? 0.1389 0.1246 0.1204 0.0095  -0.0015 -0.0002 177 GLY A N   
1398 C CA  . GLY A 178 ? 0.1223 0.1076 0.1029 0.0100  -0.0028 -0.0014 177 GLY A CA  
1399 C C   . GLY A 178 ? 0.1274 0.1130 0.1097 0.0099  -0.0034 -0.0004 177 GLY A C   
1400 O O   . GLY A 178 ? 0.1411 0.1266 0.1248 0.0091  -0.0033 0.0004  177 GLY A O   
1401 N N   . ASP A 179 ? 0.1285 0.1147 0.1109 0.0107  -0.0042 -0.0005 178 ASP A N   
1402 C CA  . ASP A 179 ? 0.1342 0.1206 0.1180 0.0106  -0.0050 0.0002  178 ASP A CA  
1403 C C   . ASP A 179 ? 0.1208 0.1084 0.1074 0.0102  -0.0043 0.0028  178 ASP A C   
1404 O O   . ASP A 179 ? 0.1165 0.1040 0.1047 0.0099  -0.0046 0.0036  178 ASP A O   
1405 C CB  . ASP A 179 ? 0.1419 0.1288 0.1250 0.0116  -0.0059 -0.0005 178 ASP A CB  
1406 C CG  . ASP A 179 ? 0.1798 0.1651 0.1607 0.0119  -0.0067 -0.0033 178 ASP A CG  
1407 O OD1 . ASP A 179 ? 0.2071 0.1923 0.1889 0.0105  -0.0066 -0.0036 178 ASP A OD1 
1408 O OD2 . ASP A 179 ? 0.2355 0.2213 0.2159 0.0130  -0.0071 -0.0040 178 ASP A OD2 
1409 N N   . ASP A 180 ? 0.1107 0.0992 0.0979 0.0103  -0.0035 0.0040  179 ASP A N   
1410 C CA  . ASP A 180 ? 0.1026 0.0918 0.0923 0.0099  -0.0030 0.0062  179 ASP A CA  
1411 C C   . ASP A 180 ? 0.0843 0.0724 0.0751 0.0090  -0.0024 0.0063  179 ASP A C   
1412 O O   . ASP A 180 ? 0.0809 0.0689 0.0738 0.0087  -0.0025 0.0073  179 ASP A O   
1413 C CB  . ASP A 180 ? 0.1284 0.1184 0.1179 0.0101  -0.0022 0.0070  179 ASP A CB  
1414 C CG  . ASP A 180 ? 0.1940 0.1855 0.1829 0.0109  -0.0028 0.0077  179 ASP A CG  
1415 O OD1 . ASP A 180 ? 0.1494 0.1415 0.1382 0.0113  -0.0039 0.0075  179 ASP A OD1 
1416 O OD2 . ASP A 180 ? 0.2445 0.2370 0.2334 0.0110  -0.0022 0.0085  179 ASP A OD2 
1417 N N   . ALA A 181 ? 0.0837 0.0710 0.0731 0.0087  -0.0017 0.0051  180 ALA A N   
1418 C CA  . ALA A 181 ? 0.0858 0.0725 0.0762 0.0079  -0.0011 0.0050  180 ALA A CA  
1419 C C   . ALA A 181 ? 0.0714 0.0577 0.0622 0.0076  -0.0019 0.0044  180 ALA A C   
1420 O O   . ALA A 181 ? 0.0830 0.0691 0.0758 0.0071  -0.0016 0.0051  180 ALA A O   
1421 C CB  . ALA A 181 ? 0.0915 0.0778 0.0800 0.0077  -0.0004 0.0038  180 ALA A CB  
1422 N N   . ALA A 182 ? 0.0768 0.0627 0.0657 0.0080  -0.0030 0.0031  181 ALA A N   
1423 C CA  . ALA A 182 ? 0.0638 0.0492 0.0530 0.0077  -0.0039 0.0025  181 ALA A CA  
1424 C C   . ALA A 182 ? 0.0686 0.0547 0.0607 0.0078  -0.0039 0.0042  181 ALA A C   
1425 O O   . ALA A 182 ? 0.0774 0.0634 0.0712 0.0074  -0.0038 0.0045  181 ALA A O   
1426 C CB  . ALA A 182 ? 0.0976 0.0824 0.0841 0.0081  -0.0052 0.0005  181 ALA A CB  
1427 N N   . GLN A 183 ? 0.0652 0.0521 0.0582 0.0084  -0.0040 0.0054  182 GLN A N   
1428 C CA  . GLN A 183 ? 0.0670 0.0546 0.0628 0.0084  -0.0042 0.0071  182 GLN A CA  
1429 C C   . GLN A 183 ? 0.0757 0.0629 0.0739 0.0077  -0.0037 0.0083  182 GLN A C   
1430 O O   . GLN A 183 ? 0.0753 0.0623 0.0752 0.0072  -0.0041 0.0086  182 GLN A O   
1431 C CB  . GLN A 183 ? 0.0727 0.0613 0.0686 0.0090  -0.0048 0.0082  182 GLN A CB  
1432 C CG  . GLN A 183 ? 0.0752 0.0643 0.0736 0.0089  -0.0055 0.0098  182 GLN A CG  
1433 C CD  . GLN A 183 ? 0.0777 0.0675 0.0758 0.0094  -0.0064 0.0107  182 GLN A CD  
1434 O OE1 . GLN A 183 ? 0.1032 0.0929 0.1001 0.0096  -0.0061 0.0110  182 GLN A OE1 
1435 N NE2 . GLN A 183 ? 0.0839 0.0748 0.0828 0.0098  -0.0071 0.0112  182 GLN A NE2 
1436 N N   . PHE A 184 ? 0.0700 0.0568 0.0671 0.0075  -0.0030 0.0082  183 PHE A N   
1437 C CA  . PHE A 184 ? 0.0647 0.0506 0.0621 0.0071  -0.0021 0.0085  183 PHE A CA  
1438 C C   . PHE A 184 ? 0.0709 0.0562 0.0690 0.0066  -0.0022 0.0078  183 PHE A C   
1439 O O   . PHE A 184 ? 0.0758 0.0604 0.0744 0.0065  -0.0019 0.0081  183 PHE A O   
1440 C CB  . PHE A 184 ? 0.0836 0.0699 0.0799 0.0072  -0.0008 0.0084  183 PHE A CB  
1441 C CG  . PHE A 184 ? 0.0719 0.0581 0.0687 0.0069  0.0009  0.0086  183 PHE A CG  
1442 C CD1 . PHE A 184 ? 0.0645 0.0510 0.0627 0.0071  0.0020  0.0098  183 PHE A CD1 
1443 C CD2 . PHE A 184 ? 0.0795 0.0656 0.0755 0.0066  0.0016  0.0076  183 PHE A CD2 
1444 C CE1 . PHE A 184 ? 0.0767 0.0636 0.0759 0.0069  0.0038  0.0099  183 PHE A CE1 
1445 C CE2 . PHE A 184 ? 0.1004 0.0867 0.0970 0.0064  0.0033  0.0078  183 PHE A CE2 
1446 C CZ  . PHE A 184 ? 0.0793 0.0661 0.0777 0.0066  0.0044  0.0090  183 PHE A CZ  
1447 N N   . ARG A 185 ? 0.0792 0.0650 0.0770 0.0063  -0.0020 0.0068  184 ARG A N   
1448 C CA  . ARG A 185 ? 0.0899 0.0755 0.0885 0.0058  -0.0019 0.0062  184 ARG A CA  
1449 C C   . ARG A 185 ? 0.0714 0.0576 0.0719 0.0058  -0.0025 0.0065  184 ARG A C   
1450 O O   . ARG A 185 ? 0.0819 0.0677 0.0833 0.0052  -0.0028 0.0063  184 ARG A O   
1451 C CB  . ARG A 185 ? 0.0881 0.0738 0.0845 0.0057  -0.0016 0.0048  184 ARG A CB  
1452 C CG  . ARG A 185 ? 0.1108 0.0963 0.1057 0.0056  -0.0007 0.0045  184 ARG A CG  
1453 C CD  . ARG A 185 ? 0.1224 0.1077 0.1148 0.0053  -0.0007 0.0031  184 ARG A CD  
1454 N NE  . ARG A 185 ? 0.1514 0.1365 0.1413 0.0056  -0.0020 0.0019  184 ARG A NE  
1455 C CZ  . ARG A 185 ? 0.2055 0.1904 0.1932 0.0060  -0.0022 0.0012  184 ARG A CZ  
1456 N NH1 . ARG A 185 ? 0.2081 0.1932 0.1958 0.0062  -0.0011 0.0018  184 ARG A NH1 
1457 N NH2 . ARG A 185 ? 0.2271 0.2115 0.2124 0.0062  -0.0036 -0.0002 184 ARG A NH2 
1458 N N   . ARG A 186 ? 0.0802 0.0666 0.0799 0.0066  -0.0027 0.0067  185 ARG A N   
1459 C CA  . ARG A 186 ? 0.0663 0.0526 0.0664 0.0070  -0.0029 0.0069  185 ARG A CA  
1460 C C   . ARG A 186 ? 0.0413 0.0289 0.0445 0.0066  -0.0020 0.0083  185 ARG A C   
1461 O O   . ARG A 186 ? 0.0617 0.0464 0.0599 0.0080  -0.0010 0.0075  185 ARG A O   
1462 C CB  . ARG A 186 ? 0.0595 0.0458 0.0577 0.0076  -0.0042 0.0062  185 ARG A CB  
1463 C CG  . ARG A 186 ? 0.0671 0.0524 0.0618 0.0074  -0.0056 0.0038  185 ARG A CG  
1464 C CD  . ARG A 186 ? 0.0719 0.0569 0.0653 0.0078  -0.0071 0.0028  185 ARG A CD  
1465 N NE  . ARG A 186 ? 0.0882 0.0741 0.0819 0.0086  -0.0070 0.0039  185 ARG A NE  
1466 C CZ  . ARG A 186 ? 0.0989 0.0849 0.0908 0.0091  -0.0071 0.0033  185 ARG A CZ  
1467 N NH1 . ARG A 186 ? 0.1106 0.0957 0.1003 0.0088  -0.0072 0.0016  185 ARG A NH1 
1468 N NH2 . ARG A 186 ? 0.1018 0.0890 0.0943 0.0098  -0.0071 0.0045  185 ARG A NH2 
1469 N N   . CYS A 187 ? 0.0697 0.0538 0.0690 0.0065  -0.0049 0.0074  186 CYS A N   
1470 C CA  . CYS A 187 ? 0.0738 0.0567 0.0722 0.0075  -0.0038 0.0085  186 CYS A CA  
1471 C C   . CYS A 187 ? 0.0570 0.0402 0.0571 0.0070  -0.0022 0.0089  186 CYS A C   
1472 O O   . CYS A 187 ? 0.0697 0.0533 0.0715 0.0070  -0.0016 0.0096  186 CYS A O   
1473 C CB  . CYS A 187 ? 0.0851 0.0688 0.0841 0.0079  -0.0034 0.0099  186 CYS A CB  
1474 S SG  . CYS A 187 ? 0.1317 0.1157 0.1296 0.0085  -0.0053 0.0096  186 CYS A SG  
1475 N N   . ILE A 188 ? 0.0591 0.0426 0.0592 0.0065  -0.0015 0.0085  187 ILE A N   
1476 C CA  . ILE A 188 ? 0.0523 0.0364 0.0539 0.0060  0.0000  0.0086  187 ILE A CA  
1477 C C   . ILE A 188 ? 0.0502 0.0336 0.0516 0.0059  -0.0008 0.0079  187 ILE A C   
1478 O O   . ILE A 188 ? 0.0654 0.0494 0.0688 0.0057  0.0001  0.0084  187 ILE A O   
1479 C CB  . ILE A 188 ? 0.0624 0.0469 0.0635 0.0057  0.0008  0.0081  187 ILE A CB  
1480 C CG1 . ILE A 188 ? 0.0685 0.0538 0.0700 0.0060  0.0020  0.0089  187 ILE A CG1 
1481 C CG2 . ILE A 188 ? 0.0647 0.0497 0.0670 0.0053  0.0021  0.0079  187 ILE A CG2 
1482 C CD1 . ILE A 188 ? 0.0884 0.0739 0.0887 0.0058  0.0027  0.0083  187 ILE A CD1 
1483 N N   . ARG A 189 ? 0.0582 0.0405 0.0573 0.0060  -0.0023 0.0067  188 ARG A N   
1484 C CA  . ARG A 189 ? 0.0788 0.0609 0.0773 0.0060  -0.0022 0.0060  188 ARG A CA  
1485 C C   . ARG A 189 ? 0.0589 0.0408 0.0586 0.0065  -0.0022 0.0069  188 ARG A C   
1486 O O   . ARG A 189 ? 0.0674 0.0498 0.0690 0.0061  -0.0020 0.0070  188 ARG A O   
1487 C CB  . ARG A 189 ? 0.0664 0.0505 0.0654 0.0063  -0.0006 0.0059  188 ARG A CB  
1488 C CG  . ARG A 189 ? 0.0673 0.0532 0.0687 0.0053  -0.0004 0.0056  188 ARG A CG  
1489 C CD  . ARG A 189 ? 0.0670 0.0522 0.0665 0.0051  -0.0023 0.0042  188 ARG A CD  
1490 N NE  . ARG A 189 ? 0.1107 0.0961 0.1091 0.0046  -0.0024 0.0033  188 ARG A NE  
1491 C CZ  . ARG A 189 ? 0.1385 0.1238 0.1346 0.0046  -0.0030 0.0025  188 ARG A CZ  
1492 N NH1 . ARG A 189 ? 0.1654 0.1505 0.1604 0.0050  -0.0036 0.0024  188 ARG A NH1 
1493 N NH2 . ARG A 189 ? 0.1838 0.1692 0.1785 0.0042  -0.0029 0.0018  188 ARG A NH2 
1494 N N   . TYR A 190 ? 0.0770 0.0590 0.0762 0.0072  -0.0026 0.0073  189 TYR A N   
1495 C CA  . TYR A 190 ? 0.0551 0.0374 0.0560 0.0074  -0.0029 0.0081  189 TYR A CA  
1496 C C   . TYR A 190 ? 0.0676 0.0509 0.0717 0.0067  -0.0022 0.0091  189 TYR A C   
1497 O O   . TYR A 190 ? 0.0694 0.0531 0.0752 0.0065  -0.0022 0.0094  189 TYR A O   
1498 C CB  . TYR A 190 ? 0.0564 0.0388 0.0565 0.0083  -0.0034 0.0087  189 TYR A CB  
1499 C CG  . TYR A 190 ? 0.0593 0.0429 0.0584 0.0088  -0.0032 0.0083  189 TYR A CG  
1500 C CD1 . TYR A 190 ? 0.0602 0.0447 0.0609 0.0083  -0.0038 0.0078  189 TYR A CD1 
1501 C CD2 . TYR A 190 ? 0.0451 0.0293 0.0432 0.0095  -0.0031 0.0087  189 TYR A CD2 
1502 C CE1 . TYR A 190 ? 0.0683 0.0536 0.0687 0.0080  -0.0052 0.0069  189 TYR A CE1 
1503 C CE2 . TYR A 190 ? 0.0677 0.0543 0.0681 0.0092  -0.0036 0.0090  189 TYR A CE2 
1504 C CZ  . TYR A 190 ? 0.0812 0.0672 0.0813 0.0085  -0.0052 0.0074  189 TYR A CZ  
1505 O OH  . TYR A 190 ? 0.0977 0.0836 0.0961 0.0084  -0.0068 0.0059  189 TYR A OH  
1506 N N   . LEU A 191 ? 0.0711 0.0551 0.0762 0.0065  -0.0012 0.0098  190 LEU A N   
1507 C CA  . LEU A 191 ? 0.0651 0.0506 0.0735 0.0062  0.0002  0.0109  190 LEU A CA  
1508 C C   . LEU A 191 ? 0.0646 0.0504 0.0742 0.0056  0.0010  0.0105  190 LEU A C   
1509 O O   . LEU A 191 ? 0.0656 0.0523 0.0778 0.0055  0.0019  0.0112  190 LEU A O   
1510 C CB  . LEU A 191 ? 0.0733 0.0597 0.0826 0.0063  0.0015  0.0119  190 LEU A CB  
1511 C CG  . LEU A 191 ? 0.1101 0.0964 0.1186 0.0068  0.0007  0.0126  190 LEU A CG  
1512 C CD1 . LEU A 191 ? 0.1795 0.1667 0.1885 0.0070  0.0017  0.0134  190 LEU A CD1 
1513 C CD2 . LEU A 191 ? 0.1242 0.1111 0.1346 0.0070  0.0004  0.0136  190 LEU A CD2 
1514 N N   . LYS A 192 ? 0.0455 0.0305 0.0532 0.0054  0.0007  0.0093  191 LYS A N   
1515 C CA  . LYS A 192 ? 0.0654 0.0509 0.0742 0.0050  0.0014  0.0089  191 LYS A CA  
1516 C C   . LYS A 192 ? 0.0538 0.0390 0.0630 0.0049  0.0005  0.0087  191 LYS A C   
1517 O O   . LYS A 192 ? 0.0671 0.0531 0.0785 0.0046  0.0012  0.0089  191 LYS A O   
1518 C CB  . LYS A 192 ? 0.0677 0.0526 0.0743 0.0047  0.0012  0.0078  191 LYS A CB  
1519 C CG  . LYS A 192 ? 0.0707 0.0563 0.0777 0.0047  0.0027  0.0081  191 LYS A CG  
1520 C CD  . LYS A 192 ? 0.0744 0.0596 0.0795 0.0044  0.0024  0.0071  191 LYS A CD  
1521 C CE  . LYS A 192 ? 0.0916 0.0776 0.0970 0.0044  0.0041  0.0073  191 LYS A CE  
1522 N NZ  . LYS A 192 ? 0.1361 0.1218 0.1397 0.0041  0.0039  0.0063  191 LYS A NZ  
1523 N N   . ARG A 193 ? 0.0729 0.0572 0.0803 0.0052  -0.0009 0.0082  192 ARG A N   
1524 C CA  . ARG A 193 ? 0.0704 0.0548 0.0786 0.0051  -0.0017 0.0080  192 ARG A CA  
1525 C C   . ARG A 193 ? 0.0588 0.0440 0.0698 0.0051  -0.0013 0.0092  192 ARG A C   
1526 O O   . ARG A 193 ? 0.0581 0.0440 0.0712 0.0048  -0.0012 0.0094  192 ARG A O   
1527 C CB  . ARG A 193 ? 0.0634 0.0472 0.0697 0.0055  -0.0029 0.0073  192 ARG A CB  
1528 C CG  . ARG A 193 ? 0.0731 0.0573 0.0808 0.0053  -0.0038 0.0073  192 ARG A CG  
1529 C CD  . ARG A 193 ? 0.0769 0.0617 0.0862 0.0047  -0.0036 0.0069  192 ARG A CD  
1530 N NE  . ARG A 193 ? 0.0840 0.0687 0.0919 0.0044  -0.0037 0.0059  192 ARG A NE  
1531 C CZ  . ARG A 193 ? 0.0901 0.0752 0.0976 0.0041  -0.0050 0.0049  192 ARG A CZ  
1532 N NH1 . ARG A 193 ? 0.0833 0.0685 0.0912 0.0041  -0.0064 0.0047  192 ARG A NH1 
1533 N NH2 . ARG A 193 ? 0.0963 0.0816 0.1029 0.0038  -0.0051 0.0041  192 ARG A NH2 
1534 N N   . TRP A 194 ? 0.0641 0.0496 0.0754 0.0055  -0.0011 0.0101  193 TRP A N   
1535 C CA  . TRP A 194 ? 0.0557 0.0422 0.0698 0.0055  -0.0005 0.0115  193 TRP A CA  
1536 C C   . TRP A 194 ? 0.0461 0.0337 0.0629 0.0052  0.0011  0.0120  193 TRP A C   
1537 O O   . TRP A 194 ? 0.0648 0.0532 0.0841 0.0050  0.0014  0.0126  193 TRP A O   
1538 C CB  . TRP A 194 ? 0.0528 0.0395 0.0666 0.0060  -0.0003 0.0124  193 TRP A CB  
1539 C CG  . TRP A 194 ? 0.0331 0.0212 0.0500 0.0060  0.0007  0.0140  193 TRP A CG  
1540 C CD1 . TRP A 194 ? 0.0616 0.0501 0.0801 0.0061  0.0002  0.0148  193 TRP A CD1 
1541 C CD2 . TRP A 194 ? 0.0591 0.0482 0.0778 0.0060  0.0023  0.0149  193 TRP A CD2 
1542 N NE1 . TRP A 194 ? 0.0697 0.0596 0.0909 0.0061  0.0014  0.0162  193 TRP A NE1 
1543 C CE2 . TRP A 194 ? 0.0436 0.0338 0.0649 0.0061  0.0027  0.0163  193 TRP A CE2 
1544 C CE3 . TRP A 194 ? 0.0761 0.0654 0.0944 0.0060  0.0035  0.0148  193 TRP A CE3 
1545 C CZ2 . TRP A 194 ? 0.0638 0.0554 0.0875 0.0063  0.0044  0.0176  193 TRP A CZ2 
1546 C CZ3 . TRP A 194 ? 0.0728 0.0634 0.0934 0.0062  0.0051  0.0159  193 TRP A CZ3 
1547 C CH2 . TRP A 194 ? 0.0635 0.0552 0.0867 0.0063  0.0055  0.0173  193 TRP A CH2 
1548 N N   . ARG A 195 ? 0.0485 0.0363 0.0649 0.0051  0.0022  0.0117  194 ARG A N   
1549 C CA  . ARG A 195 ? 0.0747 0.0635 0.0935 0.0048  0.0038  0.0120  194 ARG A CA  
1550 C C   . ARG A 195 ? 0.0671 0.0559 0.0865 0.0045  0.0034  0.0114  194 ARG A C   
1551 O O   . ARG A 195 ? 0.0850 0.0748 0.1071 0.0044  0.0042  0.0120  194 ARG A O   
1552 C CB  . ARG A 195 ? 0.0932 0.0820 0.1108 0.0048  0.0048  0.0115  194 ARG A CB  
1553 C CG  . ARG A 195 ? 0.1156 0.1053 0.1351 0.0047  0.0065  0.0115  194 ARG A CG  
1554 C CD  . ARG A 195 ? 0.1572 0.1465 0.1748 0.0045  0.0069  0.0105  194 ARG A CD  
1555 N NE  . ARG A 195 ? 0.1326 0.1209 0.1479 0.0042  0.0054  0.0094  194 ARG A NE  
1556 C CZ  . ARG A 195 ? 0.1413 0.1290 0.1543 0.0041  0.0052  0.0085  194 ARG A CZ  
1557 N NH1 . ARG A 195 ? 0.1523 0.1404 0.1651 0.0042  0.0065  0.0086  194 ARG A NH1 
1558 N NH2 . ARG A 195 ? 0.1516 0.1385 0.1627 0.0039  0.0037  0.0076  194 ARG A NH2 
1559 N N   . ASP A 196 ? 0.0769 0.0648 0.0940 0.0043  0.0022  0.0102  195 ASP A N   
1560 C CA  . ASP A 196 ? 0.0775 0.0655 0.0953 0.0040  0.0019  0.0097  195 ASP A CA  
1561 C C   . ASP A 196 ? 0.1034 0.0917 0.1227 0.0039  0.0011  0.0101  195 ASP A C   
1562 O O   . ASP A 196 ? 0.1110 0.0999 0.1322 0.0037  0.0013  0.0101  195 ASP A O   
1563 C CB  . ASP A 196 ? 0.0663 0.0533 0.0813 0.0038  0.0008  0.0084  195 ASP A CB  
1564 C CG  . ASP A 196 ? 0.1184 0.1054 0.1322 0.0038  0.0018  0.0080  195 ASP A CG  
1565 O OD1 . ASP A 196 ? 0.1264 0.1143 0.1420 0.0038  0.0034  0.0085  195 ASP A OD1 
1566 O OD2 . ASP A 196 ? 0.1637 0.1498 0.1749 0.0038  0.0009  0.0071  195 ASP A OD2 
1567 N N   . PHE A 197 ? 0.0651 0.0529 0.0838 0.0042  0.0001  0.0105  196 PHE A N   
1568 C CA  . PHE A 197 ? 0.0885 0.0765 0.1086 0.0042  -0.0007 0.0108  196 PHE A CA  
1569 C C   . PHE A 197 ? 0.1047 0.0939 0.1279 0.0042  0.0003  0.0122  196 PHE A C   
1570 O O   . PHE A 197 ? 0.0969 0.0867 0.1222 0.0040  0.0002  0.0125  196 PHE A O   
1571 C CB  . PHE A 197 ? 0.1015 0.0887 0.1196 0.0045  -0.0022 0.0106  196 PHE A CB  
1572 C CG  . PHE A 197 ? 0.0946 0.0820 0.1139 0.0045  -0.0032 0.0109  196 PHE A CG  
1573 C CD1 . PHE A 197 ? 0.1070 0.0945 0.1270 0.0041  -0.0039 0.0103  196 PHE A CD1 
1574 C CD2 . PHE A 197 ? 0.0978 0.0853 0.1177 0.0048  -0.0034 0.0119  196 PHE A CD2 
1575 C CE1 . PHE A 197 ? 0.1178 0.1055 0.1391 0.0040  -0.0049 0.0106  196 PHE A CE1 
1576 C CE2 . PHE A 197 ? 0.0949 0.0827 0.1160 0.0048  -0.0043 0.0123  196 PHE A CE2 
1577 C CZ  . PHE A 197 ? 0.1303 0.1181 0.1520 0.0044  -0.0051 0.0116  196 PHE A CZ  
1578 N N   . ARG A 198 ? 0.0641 0.0538 0.0879 0.0045  0.0014  0.0131  197 ARG A N   
1579 C CA  . ARG A 198 ? 0.0773 0.0682 0.1041 0.0046  0.0023  0.0145  197 ARG A CA  
1580 C C   . ARG A 198 ? 0.0728 0.0648 0.1018 0.0046  0.0043  0.0149  197 ARG A C   
1581 O O   . ARG A 198 ? 0.1071 0.1001 0.1388 0.0047  0.0052  0.0161  197 ARG A O   
1582 C CB  . ARG A 198 ? 0.0807 0.0715 0.1070 0.0050  0.0022  0.0154  197 ARG A CB  
1583 C CG  . ARG A 198 ? 0.1271 0.1171 0.1516 0.0052  0.0004  0.0151  197 ARG A CG  
1584 C CD  . ARG A 198 ? 0.1980 0.1887 0.2242 0.0054  0.0004  0.0165  197 ARG A CD  
1585 N NE  . ARG A 198 ? 0.1339 0.1254 0.1629 0.0052  0.0005  0.0172  197 ARG A NE  
1586 C CZ  . ARG A 198 ? 0.2367 0.2293 0.2679 0.0054  0.0008  0.0187  197 ARG A CZ  
1587 N NH1 . ARG A 198 ? 0.2446 0.2375 0.2754 0.0057  0.0012  0.0195  197 ARG A NH1 
1588 N NH2 . ARG A 198 ? 0.1738 0.1672 0.2076 0.0052  0.0009  0.0193  197 ARG A NH2 
1589 N N   . PHE A 199 ? 0.0653 0.0571 0.0933 0.0045  0.0050  0.0141  198 PHE A N   
1590 C CA  . PHE A 199 ? 0.1135 0.1062 0.1435 0.0046  0.0070  0.0145  198 PHE A CA  
1591 C C   . PHE A 199 ? 0.2649 0.2576 0.2950 0.0043  0.0071  0.0136  198 PHE A C   
1592 O O   . PHE A 199 ? 0.2839 0.2757 0.3121 0.0040  0.0057  0.0126  198 PHE A O   
1593 C CB  . PHE A 199 ? 0.1347 0.1273 0.1635 0.0048  0.0080  0.0144  198 PHE A CB  
1594 C CG  . PHE A 199 ? 0.0990 0.0918 0.1280 0.0052  0.0081  0.0154  198 PHE A CG  
1595 C CD1 . PHE A 199 ? 0.0611 0.0531 0.0880 0.0052  0.0065  0.0153  198 PHE A CD1 
1596 C CD2 . PHE A 199 ? 0.1019 0.0957 0.1332 0.0055  0.0097  0.0165  198 PHE A CD2 
1597 C CE1 . PHE A 199 ? 0.0850 0.0772 0.1119 0.0055  0.0065  0.0162  198 PHE A CE1 
1598 C CE2 . PHE A 199 ? 0.1180 0.1121 0.1494 0.0058  0.0097  0.0175  198 PHE A CE2 
1599 C CZ  . PHE A 199 ? 0.1099 0.1032 0.1391 0.0058  0.0081  0.0174  198 PHE A CZ  
1600 N N   . SER A 200 ? 0.4292 0.4228 0.4618 0.0043  0.0086  0.0140  199 SER A N   
1601 C CA  . SER A 200 ? 0.5868 0.5805 0.6197 0.0041  0.0086  0.0133  199 SER A CA  
1602 C C   . SER A 200 ? 0.7129 0.7061 0.7437 0.0039  0.0089  0.0122  199 SER A C   
1603 O O   . SER A 200 ? 0.7244 0.7174 0.7539 0.0041  0.0096  0.0121  199 SER A O   
1604 C CB  . SER A 200 ? 0.6192 0.6141 0.6553 0.0042  0.0102  0.0140  199 SER A CB  
1605 O OG  . SER A 200 ? 0.6386 0.6341 0.6768 0.0042  0.0097  0.0149  199 SER A OG  
1606 N N   . SER A 201 ? 0.8085 0.8015 0.8387 0.0036  0.0084  0.0114  200 SER A N   
1607 C CA  . SER A 201 ? 0.8914 0.8840 0.9198 0.0035  0.0085  0.0104  200 SER A CA  
1608 C C   . SER A 201 ? 0.9393 0.9326 0.9688 0.0036  0.0106  0.0104  200 SER A C   
1609 O O   . SER A 201 ? 0.9482 0.9413 0.9764 0.0035  0.0108  0.0096  200 SER A O   
1610 C CB  . SER A 201 ? 0.9319 0.9242 0.9596 0.0031  0.0071  0.0096  200 SER A CB  
1611 O OG  . SER A 201 ? 0.9568 0.9480 0.9816 0.0029  0.0054  0.0089  200 SER A OG  
1612 N N   . ASP A 202 ? 0.9712 0.9652 1.0030 0.0040  0.0121  0.0113  201 ASP A N   
1613 C CA  . ASP A 202 ? 0.9935 0.9881 1.0263 0.0043  0.0142  0.0114  201 ASP A CA  
1614 C C   . ASP A 202 ? 0.9957 0.9898 1.0271 0.0045  0.0148  0.0115  201 ASP A C   
1615 O O   . ASP A 202 ? 1.0007 0.9943 1.0306 0.0045  0.0135  0.0115  201 ASP A O   
1616 C CB  . ASP A 202 ? 1.0117 1.0072 1.0478 0.0046  0.0156  0.0123  201 ASP A CB  
1617 C CG  . ASP A 202 ? 1.0236 1.0194 1.0612 0.0048  0.0155  0.0134  201 ASP A CG  
1618 O OD1 . ASP A 202 ? 1.0276 1.0229 1.0636 0.0048  0.0142  0.0135  201 ASP A OD1 
1619 O OD2 . ASP A 202 ? 1.0280 1.0247 1.0684 0.0051  0.0166  0.0143  201 ASP A OD2 
1620 N N   . GLY A 203 ? 0.9839 0.9783 1.0158 0.0048  0.0167  0.0114  202 GLY A N   
1621 C CA  . GLY A 203 ? 0.9550 0.9492 0.9856 0.0051  0.0173  0.0114  202 GLY A CA  
1622 C C   . GLY A 203 ? 0.9304 0.9249 0.9625 0.0055  0.0180  0.0124  202 GLY A C   
1623 O O   . GLY A 203 ? 0.9411 0.9354 0.9723 0.0058  0.0187  0.0124  202 GLY A O   
1624 N N   . ASN A 204 ? 0.8771 0.8721 0.9114 0.0056  0.0177  0.0134  203 ASN A N   
1625 C CA  . ASN A 204 ? 0.8169 0.8123 0.8525 0.0060  0.0181  0.0144  203 ASN A CA  
1626 C C   . ASN A 204 ? 0.7325 0.7273 0.7658 0.0059  0.0168  0.0144  203 ASN A C   
1627 O O   . ASN A 204 ? 0.7218 0.7167 0.7551 0.0063  0.0174  0.0149  203 ASN A O   
1628 C CB  . ASN A 204 ? 0.8311 0.8273 0.8695 0.0061  0.0180  0.0155  203 ASN A CB  
1629 C CG  . ASN A 204 ? 0.8453 0.8413 0.8830 0.0058  0.0160  0.0159  203 ASN A CG  
1630 O OD1 . ASN A 204 ? 0.8484 0.8437 0.8839 0.0054  0.0144  0.0151  203 ASN A OD1 
1631 N ND2 . ASN A 204 ? 0.8485 0.8451 0.8881 0.0061  0.0161  0.0171  203 ASN A ND2 
1632 N N   . ALA A 205 ? 0.6540 0.6481 0.6852 0.0055  0.0150  0.0137  204 ALA A N   
1633 C CA  . ALA A 205 ? 0.5866 0.5799 0.6153 0.0054  0.0136  0.0134  204 ALA A CA  
1634 C C   . ALA A 205 ? 0.5288 0.5214 0.5548 0.0052  0.0136  0.0123  204 ALA A C   
1635 O O   . ALA A 205 ? 0.5171 0.5090 0.5408 0.0051  0.0123  0.0119  204 ALA A O   
1636 C CB  . ALA A 205 ? 0.5589 0.5518 0.5868 0.0051  0.0115  0.0133  204 ALA A CB  
1637 N N   . ALA A 206 ? 0.5036 0.4964 0.5299 0.0052  0.0150  0.0118  205 ALA A N   
1638 C CA  . ALA A 206 ? 0.4959 0.4882 0.5199 0.0051  0.0152  0.0109  205 ALA A CA  
1639 C C   . ALA A 206 ? 0.4682 0.4602 0.4908 0.0053  0.0154  0.0110  205 ALA A C   
1640 O O   . ALA A 206 ? 0.4756 0.4669 0.4957 0.0051  0.0145  0.0102  205 ALA A O   
1641 C CB  . ALA A 206 ? 0.5093 0.5020 0.5341 0.0052  0.0169  0.0104  205 ALA A CB  
1642 N N   . PRO A 207 ? 0.4112 0.4036 0.4354 0.0058  0.0165  0.0118  206 PRO A N   
1643 C CA  . PRO A 207 ? 0.3487 0.3408 0.3715 0.0060  0.0166  0.0119  206 PRO A CA  
1644 C C   . PRO A 207 ? 0.2522 0.2439 0.2737 0.0059  0.0148  0.0122  206 PRO A C   
1645 O O   . PRO A 207 ? 0.2383 0.2298 0.2585 0.0061  0.0147  0.0123  206 PRO A O   
1646 C CB  . PRO A 207 ? 0.3946 0.3874 0.4197 0.0066  0.0184  0.0128  206 PRO A CB  
1647 C CG  . PRO A 207 ? 0.4136 0.4071 0.4414 0.0067  0.0189  0.0135  206 PRO A CG  
1648 C CD  . PRO A 207 ? 0.4195 0.4127 0.4467 0.0062  0.0181  0.0126  206 PRO A CD  
1649 N N   . LEU A 208 ? 0.1640 0.1556 0.1858 0.0057  0.0134  0.0124  207 LEU A N   
1650 C CA  . LEU A 208 ? 0.1727 0.1639 0.1933 0.0057  0.0118  0.0127  207 LEU A CA  
1651 C C   . LEU A 208 ? 0.1852 0.1755 0.2026 0.0054  0.0107  0.0117  207 LEU A C   
1652 O O   . LEU A 208 ? 0.1861 0.1760 0.2022 0.0056  0.0100  0.0119  207 LEU A O   
1653 C CB  . LEU A 208 ? 0.2164 0.2076 0.2377 0.0055  0.0105  0.0130  207 LEU A CB  
1654 C CG  . LEU A 208 ? 0.3037 0.2959 0.3280 0.0058  0.0111  0.0144  207 LEU A CG  
1655 C CD1 . LEU A 208 ? 0.3117 0.3038 0.3366 0.0056  0.0097  0.0146  207 LEU A CD1 
1656 C CD2 . LEU A 208 ? 0.2910 0.2835 0.3154 0.0062  0.0113  0.0153  207 LEU A CD2 
1657 N N   . GLY A 209 ? 0.1363 0.1261 0.1523 0.0051  0.0104  0.0106  208 GLY A N   
1658 C CA  . GLY A 209 ? 0.1439 0.1328 0.1570 0.0049  0.0093  0.0097  208 GLY A CA  
1659 C C   . GLY A 209 ? 0.1664 0.1554 0.1785 0.0051  0.0100  0.0097  208 GLY A C   
1660 O O   . GLY A 209 ? 0.1362 0.1246 0.1468 0.0052  0.0091  0.0098  208 GLY A O   
1661 N N   . ILE A 210 ? 0.1657 0.1551 0.1784 0.0052  0.0118  0.0096  209 ILE A N   
1662 C CA  . ILE A 210 ? 0.1775 0.1669 0.1894 0.0055  0.0127  0.0096  209 ILE A CA  
1663 C C   . ILE A 210 ? 0.1552 0.1450 0.1684 0.0059  0.0130  0.0107  209 ILE A C   
1664 O O   . ILE A 210 ? 0.1651 0.1547 0.1771 0.0061  0.0128  0.0108  209 ILE A O   
1665 C CB  . ILE A 210 ? 0.2352 0.2249 0.2476 0.0056  0.0146  0.0092  209 ILE A CB  
1666 C CG1 . ILE A 210 ? 0.2352 0.2248 0.2468 0.0059  0.0156  0.0091  209 ILE A CG1 
1667 C CG2 . ILE A 210 ? 0.2368 0.2272 0.2521 0.0058  0.0160  0.0099  209 ILE A CG2 
1668 C CD1 . ILE A 210 ? 0.2444 0.2334 0.2533 0.0057  0.0145  0.0085  209 ILE A CD1 
1669 N N   . GLY A 211 ? 0.1168 0.1072 0.1325 0.0061  0.0135  0.0116  210 GLY A N   
1670 C CA  . GLY A 211 ? 0.1197 0.1107 0.1368 0.0065  0.0138  0.0128  210 GLY A CA  
1671 C C   . GLY A 211 ? 0.1397 0.1302 0.1553 0.0065  0.0120  0.0131  210 GLY A C   
1672 O O   . GLY A 211 ? 0.1126 0.1033 0.1278 0.0068  0.0121  0.0136  210 GLY A O   
1673 N N   . LEU A 212 ? 0.0998 0.0897 0.1144 0.0061  0.0105  0.0126  211 LEU A N   
1674 C CA  . LEU A 212 ? 0.0769 0.0664 0.0900 0.0062  0.0089  0.0128  211 LEU A CA  
1675 C C   . LEU A 212 ? 0.0827 0.0716 0.0932 0.0062  0.0083  0.0120  211 LEU A C   
1676 O O   . LEU A 212 ? 0.0896 0.0784 0.0992 0.0064  0.0077  0.0124  211 LEU A O   
1677 C CB  . LEU A 212 ? 0.1269 0.1158 0.1395 0.0060  0.0072  0.0125  211 LEU A CB  
1678 C CG  . LEU A 212 ? 0.1407 0.1303 0.1560 0.0060  0.0075  0.0134  211 LEU A CG  
1679 C CD1 . LEU A 212 ? 0.1929 0.1818 0.2076 0.0057  0.0062  0.0125  211 LEU A CD1 
1680 C CD2 . LEU A 212 ? 0.1795 0.1695 0.1955 0.0064  0.0070  0.0145  211 LEU A CD2 
1681 N N   . THR A 213 ? 0.0879 0.0764 0.0973 0.0059  0.0088  0.0110  212 THR A N   
1682 C CA  . THR A 213 ? 0.0738 0.0619 0.0809 0.0059  0.0083  0.0102  212 THR A CA  
1683 C C   . THR A 213 ? 0.0739 0.0625 0.0814 0.0063  0.0095  0.0109  212 THR A C   
1684 O O   . THR A 213 ? 0.0771 0.0655 0.0831 0.0064  0.0089  0.0109  212 THR A O   
1685 C CB  . THR A 213 ? 0.0897 0.0774 0.0956 0.0055  0.0086  0.0091  212 THR A CB  
1686 O OG1 . THR A 213 ? 0.0740 0.0612 0.0797 0.0052  0.0074  0.0086  212 THR A OG1 
1687 C CG2 . THR A 213 ? 0.0904 0.0777 0.0939 0.0054  0.0082  0.0082  212 THR A CG2 
1688 N N   . ALA A 214 ? 0.0777 0.0669 0.0871 0.0065  0.0113  0.0114  213 ALA A N   
1689 C CA  . ALA A 214 ? 0.0892 0.0788 0.0991 0.0069  0.0124  0.0120  213 ALA A CA  
1690 C C   . ALA A 214 ? 0.0950 0.0852 0.1059 0.0072  0.0119  0.0133  213 ALA A C   
1691 O O   . ALA A 214 ? 0.1029 0.0933 0.1130 0.0075  0.0118  0.0137  213 ALA A O   
1692 C CB  . ALA A 214 ? 0.0962 0.0863 0.1080 0.0071  0.0143  0.0121  213 ALA A CB  
1693 N N   . ALA A 215 ? 0.0852 0.0757 0.0975 0.0072  0.0114  0.0139  214 ALA A N   
1694 C CA  . ALA A 215 ? 0.1008 0.0919 0.1139 0.0075  0.0108  0.0152  214 ALA A CA  
1695 C C   . ALA A 215 ? 0.0897 0.0803 0.1004 0.0075  0.0093  0.0149  214 ALA A C   
1696 O O   . ALA A 215 ? 0.0915 0.0825 0.1020 0.0078  0.0092  0.0158  214 ALA A O   
1697 C CB  . ALA A 215 ? 0.1132 0.1046 0.1281 0.0074  0.0104  0.0158  214 ALA A CB  
1698 N N   . ALA A 216 ? 0.1013 0.0909 0.1100 0.0072  0.0081  0.0137  215 ALA A N   
1699 C CA  . ALA A 216 ? 0.0958 0.0848 0.1021 0.0072  0.0066  0.0134  215 ALA A CA  
1700 C C   . ALA A 216 ? 0.0993 0.0884 0.1043 0.0074  0.0071  0.0131  215 ALA A C   
1701 O O   . ALA A 216 ? 0.1086 0.0980 0.1127 0.0077  0.0065  0.0136  215 ALA A O   
1702 C CB  . ALA A 216 ? 0.0975 0.0853 0.1020 0.0069  0.0051  0.0120  215 ALA A CB  
1703 N N   . TYR A 217 ? 0.0931 0.0822 0.0983 0.0072  0.0083  0.0125  216 TYR A N   
1704 C CA  . TYR A 217 ? 0.0760 0.0652 0.0802 0.0074  0.0090  0.0123  216 TYR A CA  
1705 C C   . TYR A 217 ? 0.0732 0.0633 0.0785 0.0079  0.0096  0.0137  216 TYR A C   
1706 O O   . TYR A 217 ? 0.0980 0.0883 0.1021 0.0081  0.0092  0.0139  216 TYR A O   
1707 C CB  . TYR A 217 ? 0.0629 0.0520 0.0673 0.0072  0.0104  0.0116  216 TYR A CB  
1708 C CG  . TYR A 217 ? 0.1074 0.0966 0.1110 0.0075  0.0112  0.0115  216 TYR A CG  
1709 C CD1 . TYR A 217 ? 0.1361 0.1248 0.1374 0.0074  0.0106  0.0104  216 TYR A CD1 
1710 C CD2 . TYR A 217 ? 0.1429 0.1326 0.1482 0.0079  0.0125  0.0124  216 TYR A CD2 
1711 C CE1 . TYR A 217 ? 0.1624 0.1511 0.1630 0.0076  0.0114  0.0103  216 TYR A CE1 
1712 C CE2 . TYR A 217 ? 0.1520 0.1418 0.1566 0.0081  0.0132  0.0123  216 TYR A CE2 
1713 C CZ  . TYR A 217 ? 0.1930 0.1823 0.1953 0.0080  0.0126  0.0112  216 TYR A CZ  
1714 O OH  . TYR A 217 ? 0.2034 0.1925 0.2050 0.0082  0.0132  0.0111  216 TYR A OH  
1715 N N   . TRP A 218 ? 0.0712 0.0620 0.0790 0.0080  0.0104  0.0147  217 TRP A N   
1716 C CA  . TRP A 218 ? 0.0961 0.0880 0.1051 0.0085  0.0110  0.0161  217 TRP A CA  
1717 C C   . TRP A 218 ? 0.1188 0.1112 0.1275 0.0086  0.0097  0.0171  217 TRP A C   
1718 O O   . TRP A 218 ? 0.1474 0.1405 0.1557 0.0090  0.0096  0.0178  217 TRP A O   
1719 C CB  . TRP A 218 ? 0.1159 0.1084 0.1278 0.0087  0.0124  0.0170  217 TRP A CB  
1720 C CG  . TRP A 218 ? 0.1063 0.0984 0.1186 0.0087  0.0138  0.0163  217 TRP A CG  
1721 C CD1 . TRP A 218 ? 0.1059 0.0977 0.1192 0.0085  0.0146  0.0158  217 TRP A CD1 
1722 C CD2 . TRP A 218 ? 0.1260 0.1179 0.1376 0.0089  0.0146  0.0161  217 TRP A CD2 
1723 N NE1 . TRP A 218 ? 0.1560 0.1475 0.1693 0.0086  0.0159  0.0151  217 TRP A NE1 
1724 C CE2 . TRP A 218 ? 0.1508 0.1423 0.1631 0.0088  0.0159  0.0153  217 TRP A CE2 
1725 C CE3 . TRP A 218 ? 0.1703 0.1625 0.1809 0.0091  0.0144  0.0165  217 TRP A CE3 
1726 C CZ2 . TRP A 218 ? 0.1651 0.1561 0.1769 0.0090  0.0170  0.0149  217 TRP A CZ2 
1727 C CZ3 . TRP A 218 ? 0.1737 0.1654 0.1839 0.0093  0.0154  0.0160  217 TRP A CZ3 
1728 C CH2 . TRP A 218 ? 0.1914 0.1825 0.2021 0.0092  0.0167  0.0152  217 TRP A CH2 
1729 N N   . TRP A 219 ? 0.1028 0.0949 0.1114 0.0085  0.0086  0.0169  218 TRP A N   
1730 C CA  . TRP A 219 ? 0.1055 0.0983 0.1146 0.0087  0.0077  0.0181  218 TRP A CA  
1731 C C   . TRP A 219 ? 0.1390 0.1311 0.1459 0.0087  0.0059  0.0175  218 TRP A C   
1732 O O   . TRP A 219 ? 0.1398 0.1325 0.1467 0.0090  0.0051  0.0184  218 TRP A O   
1733 C CB  . TRP A 219 ? 0.1229 0.1163 0.1346 0.0087  0.0083  0.0190  218 TRP A CB  
1734 C CG  . TRP A 219 ? 0.1183 0.1126 0.1325 0.0089  0.0100  0.0200  218 TRP A CG  
1735 C CD1 . TRP A 219 ? 0.1594 0.1546 0.1740 0.0093  0.0106  0.0209  218 TRP A CD1 
1736 C CD2 . TRP A 219 ? 0.1164 0.1108 0.1329 0.0088  0.0112  0.0200  218 TRP A CD2 
1737 N NE1 . TRP A 219 ? 0.1412 0.1369 0.1584 0.0094  0.0122  0.0215  218 TRP A NE1 
1738 C CE2 . TRP A 219 ? 0.1418 0.1371 0.1601 0.0092  0.0125  0.0210  218 TRP A CE2 
1739 C CE3 . TRP A 219 ? 0.1334 0.1273 0.1506 0.0085  0.0112  0.0194  218 TRP A CE3 
1740 C CZ2 . TRP A 219 ? 0.1646 0.1601 0.1853 0.0093  0.0140  0.0213  218 TRP A CZ2 
1741 C CZ3 . TRP A 219 ? 0.1740 0.1683 0.1937 0.0086  0.0127  0.0197  218 TRP A CZ3 
1742 C CH2 . TRP A 219 ? 0.1642 0.1593 0.1856 0.0090  0.0141  0.0207  218 TRP A CH2 
1743 N N   . PHE A 220 ? 0.1034 0.0942 0.1086 0.0084  0.0052  0.0159  219 PHE A N   
1744 C CA  . PHE A 220 ? 0.1308 0.1209 0.1340 0.0085  0.0034  0.0153  219 PHE A CA  
1745 C C   . PHE A 220 ? 0.1256 0.1163 0.1272 0.0090  0.0027  0.0155  219 PHE A C   
1746 O O   . PHE A 220 ? 0.1579 0.1489 0.1589 0.0090  0.0035  0.0154  219 PHE A O   
1747 C CB  . PHE A 220 ? 0.1212 0.1099 0.1230 0.0081  0.0027  0.0136  219 PHE A CB  
1748 C CG  . PHE A 220 ? 0.0838 0.0716 0.0836 0.0083  0.0008  0.0128  219 PHE A CG  
1749 C CD1 . PHE A 220 ? 0.1028 0.0901 0.1028 0.0084  -0.0004 0.0127  219 PHE A CD1 
1750 C CD2 . PHE A 220 ? 0.0923 0.0802 0.0904 0.0084  0.0001  0.0121  219 PHE A CD2 
1751 C CE1 . PHE A 220 ? 0.0926 0.0792 0.0911 0.0086  -0.0023 0.0119  219 PHE A CE1 
1752 C CE2 . PHE A 220 ? 0.0983 0.0858 0.0953 0.0086  -0.0017 0.0114  219 PHE A CE2 
1753 C CZ  . PHE A 220 ? 0.0984 0.0854 0.0958 0.0087  -0.0029 0.0113  219 PHE A CZ  
1754 N N   . GLN A 221 ? 0.0956 0.0864 0.0964 0.0093  0.0013  0.0158  220 GLN A N   
1755 C CA  . GLN A 221 ? 0.1197 0.1112 0.1188 0.0098  0.0005  0.0158  220 GLN A CA  
1756 C C   . GLN A 221 ? 0.1294 0.1201 0.1270 0.0100  -0.0014 0.0148  220 GLN A C   
1757 O O   . GLN A 221 ? 0.1461 0.1362 0.1442 0.0100  -0.0022 0.0147  220 GLN A O   
1758 C CB  . GLN A 221 ? 0.1550 0.1482 0.1550 0.0102  0.0007  0.0175  220 GLN A CB  
1759 C CG  . GLN A 221 ? 0.1931 0.1874 0.1951 0.0101  0.0025  0.0187  220 GLN A CG  
1760 C CD  . GLN A 221 ? 0.2437 0.2384 0.2451 0.0101  0.0033  0.0185  220 GLN A CD  
1761 O OE1 . GLN A 221 ? 0.2890 0.2840 0.2919 0.0099  0.0047  0.0191  220 GLN A OE1 
1762 N NE2 . GLN A 221 ? 0.2712 0.2659 0.2704 0.0103  0.0025  0.0178  220 GLN A NE2 
1763 N N   . VAL A 222 ? 0.1104 0.1012 0.1065 0.0101  -0.0021 0.0139  221 VAL A N   
1764 C CA  . VAL A 222 ? 0.1170 0.1077 0.1122 0.0102  -0.0038 0.0130  221 VAL A CA  
1765 C C   . VAL A 222 ? 0.1128 0.1044 0.1081 0.0108  -0.0048 0.0138  221 VAL A C   
1766 O O   . VAL A 222 ? 0.1824 0.1753 0.1778 0.0112  -0.0043 0.0151  221 VAL A O   
1767 C CB  . VAL A 222 ? 0.1458 0.1373 0.1396 0.0104  -0.0037 0.0121  221 VAL A CB  
1768 C CG1 . VAL A 222 ? 0.1536 0.1459 0.1468 0.0107  -0.0050 0.0113  221 VAL A CG1 
1769 C CG2 . VAL A 222 ? 0.1556 0.1461 0.1492 0.0098  -0.0028 0.0111  221 VAL A CG2 
1770 N N   . SER A 223 ? 0.0982 0.0894 0.0937 0.0108  -0.0063 0.0132  222 SER A N   
1771 C CA  . SER A 223 ? 0.0986 0.0910 0.0940 0.0114  -0.0075 0.0138  222 SER A CA  
1772 C C   . SER A 223 ? 0.1195 0.1130 0.1146 0.0114  -0.0084 0.0129  222 SER A C   
1773 O O   . SER A 223 ? 0.1234 0.1167 0.1195 0.0111  -0.0086 0.0122  222 SER A O   
1774 C CB  . SER A 223 ? 0.1362 0.1275 0.1323 0.0115  -0.0081 0.0142  222 SER A CB  
1775 O OG  . SER A 223 ? 0.1197 0.1122 0.1156 0.0121  -0.0093 0.0147  222 SER A OG  
1776 N N   . LYS A 224 ? 0.1627 0.1580 0.1565 0.0120  -0.0085 0.0128  223 LYS A N   
1777 C CA  . LYS A 224 ? 0.1879 0.1845 0.1806 0.0125  -0.0090 0.0117  223 LYS A CA  
1778 C C   . LYS A 224 ? 0.2231 0.2218 0.2148 0.0132  -0.0096 0.0122  223 LYS A C   
1779 O O   . LYS A 224 ? 0.2051 0.2045 0.1968 0.0133  -0.0093 0.0134  223 LYS A O   
1780 C CB  . LYS A 224 ? 0.1690 0.1653 0.1602 0.0127  -0.0081 0.0100  223 LYS A CB  
1781 C CG  . LYS A 224 ? 0.1844 0.1813 0.1747 0.0127  -0.0073 0.0105  223 LYS A CG  
1782 C CD  . LYS A 224 ? 0.2164 0.2123 0.2054 0.0127  -0.0064 0.0089  223 LYS A CD  
1783 C CE  . LYS A 224 ? 0.1836 0.1805 0.1720 0.0128  -0.0055 0.0095  223 LYS A CE  
1784 N NZ  . LYS A 224 ? 0.1918 0.1878 0.1791 0.0128  -0.0046 0.0082  223 LYS A NZ  
1785 N N   . ARG A 225 ? 0.2375 0.2374 0.2283 0.0138  -0.0103 0.0112  224 ARG A N   
1786 C CA  . ARG A 225 ? 0.2863 0.2885 0.2760 0.0144  -0.0109 0.0114  224 ARG A CA  
1787 C C   . ARG A 225 ? 0.2714 0.2744 0.2593 0.0151  -0.0106 0.0095  224 ARG A C   
1788 O O   . ARG A 225 ? 0.2578 0.2596 0.2451 0.0153  -0.0105 0.0077  224 ARG A O   
1789 C CB  . ARG A 225 ? 0.3520 0.3551 0.3423 0.0147  -0.0122 0.0116  224 ARG A CB  
1790 C CG  . ARG A 225 ? 0.4480 0.4502 0.4400 0.0142  -0.0127 0.0133  224 ARG A CG  
1791 C CD  . ARG A 225 ? 0.5346 0.5381 0.5270 0.0145  -0.0140 0.0135  224 ARG A CD  
1792 N NE  . ARG A 225 ? 0.6231 0.6253 0.6173 0.0141  -0.0147 0.0146  224 ARG A NE  
1793 C CZ  . ARG A 225 ? 0.6836 0.6857 0.6777 0.0143  -0.0152 0.0157  224 ARG A CZ  
1794 N NH1 . ARG A 225 ? 0.7030 0.7070 0.6960 0.0149  -0.0149 0.0163  224 ARG A NH1 
1795 N NH2 . ARG A 225 ? 0.6988 0.6992 0.6941 0.0143  -0.0157 0.0162  224 ARG A NH2 
1796 N N   . THR A 226 ? 0.3009 0.3059 0.2877 0.0155  -0.0104 0.0097  225 THR A N   
1797 C CA  . THR A 226 ? 0.3086 0.3147 0.2938 0.0162  -0.0102 0.0080  225 THR A CA  
1798 C C   . THR A 226 ? 0.2993 0.3080 0.2839 0.0169  -0.0110 0.0080  225 THR A C   
1799 O O   . THR A 226 ? 0.3283 0.3387 0.3131 0.0168  -0.0112 0.0095  225 THR A O   
1800 C CB  . THR A 226 ? 0.3588 0.3652 0.3436 0.0161  -0.0091 0.0083  225 THR A CB  
1801 O OG1 . THR A 226 ? 0.3734 0.3773 0.3589 0.0154  -0.0083 0.0084  225 THR A OG1 
1802 C CG2 . THR A 226 ? 0.3583 0.3656 0.3417 0.0169  -0.0088 0.0064  225 THR A CG2 
1803 N N   . ASP A 227 ? 0.2927 0.3016 0.2764 0.0176  -0.0115 0.0061  226 ASP A N   
1804 C CA  . ASP A 227 ? 0.3266 0.3381 0.3098 0.0183  -0.0123 0.0060  226 ASP A CA  
1805 C C   . ASP A 227 ? 0.3329 0.3468 0.3152 0.0186  -0.0118 0.0060  226 ASP A C   
1806 O O   . ASP A 227 ? 0.3253 0.3388 0.3070 0.0190  -0.0110 0.0048  226 ASP A O   
1807 C CB  . ASP A 227 ? 0.3472 0.3583 0.3298 0.0190  -0.0130 0.0039  226 ASP A CB  
1808 C CG  . ASP A 227 ? 0.4421 0.4558 0.4242 0.0196  -0.0138 0.0037  226 ASP A CG  
1809 O OD1 . ASP A 227 ? 0.4359 0.4518 0.4172 0.0202  -0.0136 0.0033  226 ASP A OD1 
1810 O OD2 . ASP A 227 ? 0.5167 0.5303 0.4993 0.0196  -0.0148 0.0040  226 ASP A OD2 
1811 N N   . PRO A 228 ? 0.3842 0.4004 0.3665 0.0186  -0.0120 0.0074  227 PRO A N   
1812 C CA  . PRO A 228 ? 0.3911 0.4097 0.3727 0.0189  -0.0114 0.0076  227 PRO A CA  
1813 C C   . PRO A 228 ? 0.4024 0.4227 0.3830 0.0198  -0.0115 0.0056  227 PRO A C   
1814 O O   . PRO A 228 ? 0.4308 0.4528 0.4109 0.0201  -0.0108 0.0055  227 PRO A O   
1815 C CB  . PRO A 228 ? 0.4093 0.4301 0.3912 0.0187  -0.0118 0.0095  227 PRO A CB  
1816 C CG  . PRO A 228 ? 0.4062 0.4263 0.3886 0.0187  -0.0130 0.0096  227 PRO A CG  
1817 C CD  . PRO A 228 ? 0.3807 0.3976 0.3638 0.0183  -0.0129 0.0090  227 PRO A CD  
1818 N N   . VAL A 229 ? 0.3745 0.3943 0.3548 0.0204  -0.0122 0.0041  228 VAL A N   
1819 C CA  . VAL A 229 ? 0.3495 0.3709 0.3291 0.0214  -0.0123 0.0021  228 VAL A CA  
1820 C C   . VAL A 229 ? 0.3372 0.3561 0.3167 0.0219  -0.0119 0.0002  228 VAL A C   
1821 O O   . VAL A 229 ? 0.3460 0.3654 0.3252 0.0224  -0.0113 -0.0008 228 VAL A O   
1822 C CB  . VAL A 229 ? 0.3729 0.3958 0.3521 0.0219  -0.0134 0.0017  228 VAL A CB  
1823 C CG1 . VAL A 229 ? 0.3594 0.3838 0.3380 0.0231  -0.0134 -0.0004 228 VAL A CG1 
1824 C CG2 . VAL A 229 ? 0.3638 0.3892 0.3431 0.0216  -0.0138 0.0036  228 VAL A CG2 
1825 N N   . SER A 230 ? 0.3090 0.3253 0.2889 0.0217  -0.0123 -0.0003 229 SER A N   
1826 C CA  . SER A 230 ? 0.2922 0.3059 0.2719 0.0222  -0.0120 -0.0022 229 SER A CA  
1827 C C   . SER A 230 ? 0.2800 0.2915 0.2600 0.0215  -0.0110 -0.0019 229 SER A C   
1828 O O   . SER A 230 ? 0.2828 0.2924 0.2627 0.0220  -0.0106 -0.0035 229 SER A O   
1829 C CB  . SER A 230 ? 0.3084 0.3200 0.2883 0.0223  -0.0128 -0.0031 229 SER A CB  
1830 O OG  . SER A 230 ? 0.3313 0.3412 0.3119 0.0212  -0.0128 -0.0016 229 SER A OG  
1831 N N   . GLN A 231 ? 0.2488 0.2605 0.2292 0.0206  -0.0107 0.0002  230 GLN A N   
1832 C CA  . GLN A 231 ? 0.2642 0.2737 0.2450 0.0198  -0.0098 0.0008  230 GLN A CA  
1833 C C   . GLN A 231 ? 0.2701 0.2764 0.2512 0.0194  -0.0099 0.0001  230 GLN A C   
1834 O O   . GLN A 231 ? 0.2510 0.2552 0.2322 0.0189  -0.0092 0.0000  230 GLN A O   
1835 C CB  . GLN A 231 ? 0.2897 0.2995 0.2701 0.0202  -0.0089 -0.0001 230 GLN A CB  
1836 C CG  . GLN A 231 ? 0.3153 0.3284 0.2955 0.0204  -0.0087 0.0006  230 GLN A CG  
1837 C CD  . GLN A 231 ? 0.3117 0.3252 0.2917 0.0209  -0.0079 -0.0005 230 GLN A CD  
1838 O OE1 . GLN A 231 ? 0.3252 0.3366 0.3052 0.0213  -0.0078 -0.0020 230 GLN A OE1 
1839 N NE2 . GLN A 231 ? 0.3387 0.3547 0.3186 0.0209  -0.0075 0.0004  230 GLN A NE2 
1840 N N   . ASN A 232 ? 0.2300 0.2357 0.2112 0.0197  -0.0108 -0.0006 231 ASN A N   
1841 C CA  . ASN A 232 ? 0.2688 0.2714 0.2503 0.0193  -0.0110 -0.0013 231 ASN A CA  
1842 C C   . ASN A 232 ? 0.2449 0.2468 0.2275 0.0181  -0.0108 0.0008  231 ASN A C   
1843 O O   . ASN A 232 ? 0.2571 0.2607 0.2405 0.0178  -0.0112 0.0027  231 ASN A O   
1844 C CB  . ASN A 232 ? 0.3075 0.3101 0.2888 0.0199  -0.0120 -0.0024 231 ASN A CB  
1845 C CG  . ASN A 232 ? 0.3826 0.3820 0.3641 0.0196  -0.0123 -0.0034 231 ASN A CG  
1846 O OD1 . ASN A 232 ? 0.4781 0.4751 0.4590 0.0198  -0.0119 -0.0050 231 ASN A OD1 
1847 N ND2 . ASN A 232 ? 0.3931 0.3924 0.3754 0.0191  -0.0130 -0.0024 231 ASN A ND2 
1848 N N   . VAL A 233 ? 0.2063 0.2055 0.1890 0.0175  -0.0103 0.0004  232 VAL A N   
1849 C CA  . VAL A 233 ? 0.2065 0.2049 0.1905 0.0164  -0.0099 0.0023  232 VAL A CA  
1850 C C   . VAL A 233 ? 0.1826 0.1792 0.1673 0.0160  -0.0104 0.0020  232 VAL A C   
1851 O O   . VAL A 233 ? 0.2118 0.2062 0.1956 0.0162  -0.0106 -0.0001 232 VAL A O   
1852 C CB  . VAL A 233 ? 0.2373 0.2345 0.2211 0.0159  -0.0088 0.0022  232 VAL A CB  
1853 C CG1 . VAL A 233 ? 0.2312 0.2274 0.2166 0.0148  -0.0083 0.0040  232 VAL A CG1 
1854 C CG2 . VAL A 233 ? 0.2331 0.2323 0.2164 0.0162  -0.0082 0.0028  232 VAL A CG2 
1855 N N   . THR A 234 ? 0.1780 0.1753 0.1644 0.0154  -0.0107 0.0041  233 THR A N   
1856 C CA  . THR A 234 ? 0.1985 0.1943 0.1861 0.0149  -0.0111 0.0041  233 THR A CA  
1857 C C   . THR A 234 ? 0.1803 0.1758 0.1699 0.0139  -0.0104 0.0063  233 THR A C   
1858 O O   . THR A 234 ? 0.2018 0.1986 0.1923 0.0137  -0.0102 0.0082  233 THR A O   
1859 C CB  . THR A 234 ? 0.2521 0.2490 0.2402 0.0153  -0.0122 0.0044  233 THR A CB  
1860 O OG1 . THR A 234 ? 0.3060 0.3053 0.2951 0.0152  -0.0125 0.0066  233 THR A OG1 
1861 C CG2 . THR A 234 ? 0.2538 0.2505 0.2399 0.0163  -0.0129 0.0020  233 THR A CG2 
1862 N N   . TYR A 235 ? 0.1714 0.1650 0.1616 0.0134  -0.0101 0.0058  234 TYR A N   
1863 C CA  . TYR A 235 ? 0.1148 0.1082 0.1073 0.0125  -0.0093 0.0077  234 TYR A CA  
1864 C C   . TYR A 235 ? 0.1172 0.1110 0.1120 0.0123  -0.0097 0.0092  234 TYR A C   
1865 O O   . TYR A 235 ? 0.1501 0.1437 0.1443 0.0127  -0.0105 0.0082  234 TYR A O   
1866 C CB  . TYR A 235 ? 0.1110 0.1024 0.1030 0.0119  -0.0084 0.0065  234 TYR A CB  
1867 C CG  . TYR A 235 ? 0.1280 0.1192 0.1184 0.0119  -0.0077 0.0059  234 TYR A CG  
1868 C CD1 . TYR A 235 ? 0.1537 0.1444 0.1416 0.0126  -0.0080 0.0037  234 TYR A CD1 
1869 C CD2 . TYR A 235 ? 0.1152 0.1067 0.1069 0.0114  -0.0068 0.0074  234 TYR A CD2 
1870 C CE1 . TYR A 235 ? 0.1593 0.1502 0.1460 0.0127  -0.0073 0.0033  234 TYR A CE1 
1871 C CE2 . TYR A 235 ? 0.1290 0.1205 0.1194 0.0114  -0.0061 0.0069  234 TYR A CE2 
1872 C CZ  . TYR A 235 ? 0.1738 0.1650 0.1617 0.0121  -0.0063 0.0049  234 TYR A CZ  
1873 O OH  . TYR A 235 ? 0.1598 0.1511 0.1466 0.0122  -0.0056 0.0045  234 TYR A OH  
1874 N N   . ASP A 236 ? 0.1037 0.0979 0.1010 0.0117  -0.0094 0.0114  235 ASP A N   
1875 C CA  . ASP A 236 ? 0.0903 0.0848 0.0900 0.0113  -0.0097 0.0128  235 ASP A CA  
1876 C C   . ASP A 236 ? 0.0893 0.0823 0.0908 0.0101  -0.0089 0.0129  235 ASP A C   
1877 O O   . ASP A 236 ? 0.0970 0.0868 0.0962 0.0101  -0.0099 0.0122  235 ASP A O   
1878 C CB  . ASP A 236 ? 0.1270 0.1215 0.1265 0.0112  -0.0111 0.0136  235 ASP A CB  
1879 C CG  . ASP A 236 ? 0.1771 0.1708 0.1775 0.0110  -0.0122 0.0138  235 ASP A CG  
1880 O OD1 . ASP A 236 ? 0.1402 0.1332 0.1423 0.0103  -0.0118 0.0137  235 ASP A OD1 
1881 O OD2 . ASP A 236 ? 0.1942 0.1880 0.1931 0.0118  -0.0133 0.0141  235 ASP A OD2 
1882 N N   . ASP A 237 ? 0.0997 0.0925 0.1011 0.0106  -0.0076 0.0123  236 ASP A N   
1883 C CA  . ASP A 237 ? 0.0803 0.0725 0.0833 0.0098  -0.0062 0.0125  236 ASP A CA  
1884 C C   . ASP A 237 ? 0.0720 0.0574 0.0666 0.0119  -0.0079 0.0097  236 ASP A C   
1885 O O   . ASP A 237 ? 0.0840 0.0691 0.0806 0.0111  -0.0074 0.0109  236 ASP A O   
1886 C CB  . ASP A 237 ? 0.0910 0.0813 0.0920 0.0104  -0.0058 0.0109  236 ASP A CB  
1887 C CG  . ASP A 237 ? 0.1129 0.1021 0.1120 0.0100  -0.0065 0.0091  236 ASP A CG  
1888 O OD1 . ASP A 237 ? 0.0838 0.0735 0.0817 0.0102  -0.0068 0.0089  236 ASP A OD1 
1889 O OD2 . ASP A 237 ? 0.1050 0.0927 0.1029 0.0095  -0.0067 0.0074  236 ASP A OD2 
1890 N N   . ARG A 238 ? 0.0928 0.0806 0.0877 0.0135  -0.0068 0.0109  237 ARG A N   
1891 C CA  . ARG A 238 ? 0.0687 0.0551 0.0652 0.0129  -0.0082 0.0119  237 ARG A CA  
1892 C C   . ARG A 238 ? 0.0794 0.0662 0.0773 0.0125  -0.0085 0.0136  237 ARG A C   
1893 O O   . ARG A 238 ? 0.1033 0.0907 0.1036 0.0119  -0.0072 0.0149  237 ARG A O   
1894 C CB  . ARG A 238 ? 0.0796 0.0676 0.0761 0.0140  -0.0084 0.0122  237 ARG A CB  
1895 C CG  . ARG A 238 ? 0.1150 0.1024 0.1136 0.0138  -0.0090 0.0136  237 ARG A CG  
1896 C CD  . ARG A 238 ? 0.1380 0.1268 0.1365 0.0146  -0.0101 0.0142  237 ARG A CD  
1897 N NE  . ARG A 238 ? 0.1200 0.1094 0.1177 0.0147  -0.0110 0.0144  237 ARG A NE  
1898 C CZ  . ARG A 238 ? 0.1253 0.1153 0.1245 0.0142  -0.0106 0.0161  237 ARG A CZ  
1899 N NH1 . ARG A 238 ? 0.1288 0.1193 0.1307 0.0133  -0.0092 0.0175  237 ARG A NH1 
1900 N NH2 . ARG A 238 ? 0.1701 0.1612 0.1686 0.0143  -0.0112 0.0165  237 ARG A NH2 
1901 N N   . ASP A 239 ? 0.1035 0.0912 0.1008 0.0126  -0.0093 0.0136  238 ASP A N   
1902 C CA  . ASP A 239 ? 0.1009 0.0902 0.0994 0.0125  -0.0085 0.0154  238 ASP A CA  
1903 C C   . ASP A 239 ? 0.1041 0.0934 0.1033 0.0117  -0.0068 0.0156  238 ASP A C   
1904 O O   . ASP A 239 ? 0.0911 0.0816 0.0922 0.0114  -0.0053 0.0171  238 ASP A O   
1905 C CB  . ASP A 239 ? 0.1039 0.0945 0.1013 0.0129  -0.0097 0.0155  238 ASP A CB  
1906 C CG  . ASP A 239 ? 0.1559 0.1486 0.1541 0.0129  -0.0084 0.0173  238 ASP A CG  
1907 O OD1 . ASP A 239 ? 0.1884 0.1823 0.1882 0.0130  -0.0078 0.0188  238 ASP A OD1 
1908 O OD2 . ASP A 239 ? 0.1823 0.1757 0.1799 0.0127  -0.0080 0.0172  238 ASP A OD2 
1909 N N   . ALA A 240 ? 0.1067 0.0947 0.1047 0.0114  -0.0071 0.0142  239 ALA A N   
1910 C CA  . ALA A 240 ? 0.1110 0.0991 0.1098 0.0107  -0.0054 0.0143  239 ALA A CA  
1911 C C   . ALA A 240 ? 0.1008 0.0888 0.1016 0.0102  -0.0040 0.0149  239 ALA A C   
1912 O O   . ALA A 240 ? 0.0872 0.0761 0.0897 0.0098  -0.0024 0.0159  239 ALA A O   
1913 C CB  . ALA A 240 ? 0.1117 0.0987 0.1093 0.0102  -0.0062 0.0127  239 ALA A CB  
1914 N N   . LEU A 241 ? 0.1045 0.0914 0.1053 0.0102  -0.0046 0.0143  240 LEU A N   
1915 C CA  . LEU A 241 ? 0.1086 0.0958 0.1118 0.0097  -0.0034 0.0149  240 LEU A CA  
1916 C C   . LEU A 241 ? 0.1129 0.1018 0.1185 0.0097  -0.0026 0.0168  240 LEU A C   
1917 O O   . LEU A 241 ? 0.1008 0.0906 0.1088 0.0093  -0.0011 0.0177  240 LEU A O   
1918 C CB  . LEU A 241 ? 0.0849 0.0710 0.0877 0.0098  -0.0042 0.0140  240 LEU A CB  
1919 C CG  . LEU A 241 ? 0.1129 0.0975 0.1140 0.0096  -0.0045 0.0123  240 LEU A CG  
1920 C CD1 . LEU A 241 ? 0.1425 0.1264 0.1429 0.0100  -0.0051 0.0116  240 LEU A CD1 
1921 C CD2 . LEU A 241 ? 0.1047 0.0895 0.1074 0.0086  -0.0030 0.0123  240 LEU A CD2 
1922 N N   . GLU A 242 ? 0.0809 0.0704 0.0861 0.0104  -0.0037 0.0174  241 GLU A N   
1923 C CA  . GLU A 242 ? 0.0995 0.0907 0.1070 0.0104  -0.0030 0.0193  241 GLU A CA  
1924 C C   . GLU A 242 ? 0.1133 0.1058 0.1219 0.0102  -0.0016 0.0204  241 GLU A C   
1925 O O   . GLU A 242 ? 0.1235 0.1171 0.1347 0.0099  -0.0002 0.0216  241 GLU A O   
1926 C CB  . GLU A 242 ? 0.1153 0.1071 0.1218 0.0111  -0.0045 0.0197  241 GLU A CB  
1927 C CG  . GLU A 242 ? 0.1363 0.1300 0.1453 0.0111  -0.0039 0.0217  241 GLU A CG  
1928 C CD  . GLU A 242 ? 0.2082 0.2029 0.2159 0.0119  -0.0052 0.0222  241 GLU A CD  
1929 O OE1 . GLU A 242 ? 0.2120 0.2057 0.2175 0.0124  -0.0068 0.0210  241 GLU A OE1 
1930 O OE2 . GLU A 242 ? 0.2544 0.2510 0.2634 0.0119  -0.0047 0.0239  241 GLU A OE2 
1931 N N   . GLN A 243 ? 0.1236 0.1161 0.1302 0.0104  -0.0018 0.0199  242 GLN A N   
1932 C CA  . GLN A 243 ? 0.1199 0.1138 0.1274 0.0103  -0.0005 0.0210  242 GLN A CA  
1933 C C   . GLN A 243 ? 0.1310 0.1246 0.1401 0.0098  0.0011  0.0207  242 GLN A C   
1934 O O   . GLN A 243 ? 0.1265 0.1213 0.1378 0.0097  0.0025  0.0219  242 GLN A O   
1935 C CB  . GLN A 243 ? 0.1324 0.1263 0.1375 0.0107  -0.0010 0.0204  242 GLN A CB  
1936 C CG  . GLN A 243 ? 0.1384 0.1330 0.1420 0.0113  -0.0027 0.0206  242 GLN A CG  
1937 C CD  . GLN A 243 ? 0.2060 0.2024 0.2115 0.0116  -0.0025 0.0224  242 GLN A CD  
1938 O OE1 . GLN A 243 ? 0.2464 0.2441 0.2538 0.0114  -0.0012 0.0239  242 GLN A OE1 
1939 N NE2 . GLN A 243 ? 0.2337 0.2301 0.2385 0.0120  -0.0040 0.0223  242 GLN A NE2 
1940 N N   . PHE A 244 ? 0.0990 0.0909 0.1069 0.0095  0.0009  0.0192  243 PHE A N   
1941 C CA  . PHE A 244 ? 0.0851 0.0768 0.0943 0.0090  0.0024  0.0188  243 PHE A CA  
1942 C C   . PHE A 244 ? 0.1128 0.1051 0.1249 0.0087  0.0033  0.0196  243 PHE A C   
1943 O O   . PHE A 244 ? 0.0821 0.0753 0.0963 0.0086  0.0049  0.0202  243 PHE A O   
1944 C CB  . PHE A 244 ? 0.0751 0.0651 0.0822 0.0087  0.0016  0.0169  243 PHE A CB  
1945 C CG  . PHE A 244 ? 0.0969 0.0867 0.1050 0.0082  0.0029  0.0163  243 PHE A CG  
1946 C CD1 . PHE A 244 ? 0.0862 0.0769 0.0957 0.0081  0.0046  0.0170  243 PHE A CD1 
1947 C CD2 . PHE A 244 ? 0.1243 0.1129 0.1316 0.0078  0.0024  0.0150  243 PHE A CD2 
1948 C CE1 . PHE A 244 ? 0.1004 0.0909 0.1107 0.0078  0.0058  0.0164  243 PHE A CE1 
1949 C CE2 . PHE A 244 ? 0.1138 0.1023 0.1219 0.0074  0.0036  0.0144  243 PHE A CE2 
1950 C CZ  . PHE A 244 ? 0.0940 0.0836 0.1037 0.0074  0.0053  0.0151  243 PHE A CZ  
1951 N N   . VAL A 245 ? 0.0894 0.0814 0.1019 0.0087  0.0024  0.0196  244 VAL A N   
1952 C CA  . VAL A 245 ? 0.0757 0.0685 0.0913 0.0085  0.0033  0.0204  244 VAL A CA  
1953 C C   . VAL A 245 ? 0.1024 0.0969 0.1203 0.0087  0.0042  0.0223  244 VAL A C   
1954 O O   . VAL A 245 ? 0.1024 0.0978 0.1229 0.0086  0.0056  0.0230  244 VAL A O   
1955 C CB  . VAL A 245 ? 0.0990 0.0910 0.1143 0.0084  0.0020  0.0200  244 VAL A CB  
1956 C CG1 . VAL A 245 ? 0.1034 0.0964 0.1220 0.0082  0.0027  0.0211  244 VAL A CG1 
1957 C CG2 . VAL A 245 ? 0.0823 0.0727 0.0960 0.0081  0.0014  0.0182  244 VAL A CG2 
1958 N N   . GLN A 246 ? 0.0947 0.0898 0.1116 0.0091  0.0033  0.0231  245 GLN A N   
1959 C CA  . GLN A 246 ? 0.1065 0.1035 0.1256 0.0094  0.0041  0.0249  245 GLN A CA  
1960 C C   . GLN A 246 ? 0.1053 0.1028 0.1252 0.0094  0.0057  0.0252  245 GLN A C   
1961 O O   . GLN A 246 ? 0.1075 0.1062 0.1301 0.0094  0.0069  0.0264  245 GLN A O   
1962 C CB  . GLN A 246 ? 0.1206 0.1182 0.1381 0.0098  0.0029  0.0256  245 GLN A CB  
1963 C CG  . GLN A 246 ? 0.1339 0.1336 0.1536 0.0100  0.0037  0.0276  245 GLN A CG  
1964 C CD  . GLN A 246 ? 0.1936 0.1941 0.2163 0.0099  0.0041  0.0287  245 GLN A CD  
1965 O OE1 . GLN A 246 ? 0.2342 0.2350 0.2569 0.0100  0.0030  0.0291  245 GLN A OE1 
1966 N NE2 . GLN A 246 ? 0.1726 0.1737 0.1981 0.0097  0.0057  0.0293  245 GLN A NE2 
1967 N N   . THR A 247 ? 0.0939 0.0906 0.1116 0.0093  0.0056  0.0241  246 THR A N   
1968 C CA  . THR A 247 ? 0.1071 0.1043 0.1254 0.0094  0.0071  0.0243  246 THR A CA  
1969 C C   . THR A 247 ? 0.1232 0.1201 0.1436 0.0092  0.0085  0.0240  246 THR A C   
1970 O O   . THR A 247 ? 0.1137 0.1115 0.1362 0.0093  0.0099  0.0248  246 THR A O   
1971 C CB  . THR A 247 ? 0.1115 0.1079 0.1269 0.0094  0.0066  0.0231  246 THR A CB  
1972 O OG1 . THR A 247 ? 0.1249 0.1219 0.1388 0.0097  0.0055  0.0237  246 THR A OG1 
1973 C CG2 . THR A 247 ? 0.1135 0.1102 0.1295 0.0095  0.0080  0.0232  246 THR A CG2 
1974 N N   . MET A 248 ? 0.1080 0.1038 0.1279 0.0088  0.0081  0.0227  247 MET A N   
1975 C CA  . MET A 248 ? 0.1069 0.1027 0.1288 0.0086  0.0094  0.0225  247 MET A CA  
1976 C C   . MET A 248 ? 0.0950 0.0921 0.1202 0.0088  0.0102  0.0240  247 MET A C   
1977 O O   . MET A 248 ? 0.1020 0.0998 0.1294 0.0090  0.0117  0.0245  247 MET A O   
1978 C CB  . MET A 248 ? 0.1101 0.1047 0.1310 0.0082  0.0087  0.0210  247 MET A CB  
1979 C CG  . MET A 248 ? 0.1058 0.0992 0.1242 0.0080  0.0086  0.0195  247 MET A CG  
1980 S SD  . MET A 248 ? 0.1158 0.1080 0.1335 0.0075  0.0081  0.0180  247 MET A SD  
1981 C CE  . MET A 248 ? 0.1235 0.1150 0.1397 0.0075  0.0059  0.0178  247 MET A CE  
1982 N N   . LEU A 249 ? 0.1000 0.0975 0.1256 0.0088  0.0091  0.0247  248 LEU A N   
1983 C CA  . LEU A 249 ? 0.1231 0.1219 0.1519 0.0090  0.0097  0.0263  248 LEU A CA  
1984 C C   . LEU A 249 ? 0.1658 0.1659 0.1960 0.0094  0.0107  0.0277  248 LEU A C   
1985 O O   . LEU A 249 ? 0.1680 0.1690 0.2011 0.0095  0.0121  0.0285  248 LEU A O   
1986 C CB  . LEU A 249 ? 0.0940 0.0930 0.1225 0.0089  0.0083  0.0268  248 LEU A CB  
1987 C CG  . LEU A 249 ? 0.0982 0.0961 0.1263 0.0085  0.0076  0.0257  248 LEU A CG  
1988 C CD1 . LEU A 249 ? 0.1142 0.1119 0.1413 0.0086  0.0059  0.0258  248 LEU A CD1 
1989 C CD2 . LEU A 249 ? 0.1222 0.1208 0.1538 0.0084  0.0088  0.0262  248 LEU A CD2 
1990 N N   . ASP A 250 ? 0.1312 0.1315 0.1595 0.0095  0.0102  0.0279  249 ASP A N   
1991 C CA  . ASP A 250 ? 0.1460 0.1476 0.1756 0.0099  0.0111  0.0292  249 ASP A CA  
1992 C C   . ASP A 250 ? 0.1623 0.1637 0.1931 0.0101  0.0127  0.0289  249 ASP A C   
1993 O O   . ASP A 250 ? 0.2170 0.2195 0.2497 0.0104  0.0137  0.0301  249 ASP A O   
1994 C CB  . ASP A 250 ? 0.2000 0.2019 0.2272 0.0101  0.0102  0.0294  249 ASP A CB  
1995 C CG  . ASP A 250 ? 0.2435 0.2458 0.2696 0.0101  0.0087  0.0299  249 ASP A CG  
1996 O OD1 . ASP A 250 ? 0.2422 0.2450 0.2699 0.0101  0.0084  0.0306  249 ASP A OD1 
1997 O OD2 . ASP A 250 ? 0.2831 0.2852 0.3066 0.0102  0.0078  0.0295  249 ASP A OD2 
1998 N N   . ASN A 251 ? 0.1198 0.1199 0.1494 0.0098  0.0130  0.0273  250 ASN A N   
1999 C CA  . ASN A 251 ? 0.1170 0.1168 0.1474 0.0100  0.0146  0.0269  250 ASN A CA  
2000 C C   . ASN A 251 ? 0.1275 0.1274 0.1606 0.0101  0.0158  0.0269  250 ASN A C   
2001 O O   . ASN A 251 ? 0.1681 0.1677 0.2018 0.0103  0.0171  0.0265  250 ASN A O   
2002 C CB  . ASN A 251 ? 0.1475 0.1460 0.1751 0.0098  0.0143  0.0252  250 ASN A CB  
2003 C CG  . ASN A 251 ? 0.1679 0.1665 0.1935 0.0099  0.0138  0.0254  250 ASN A CG  
2004 O OD1 . ASN A 251 ? 0.1822 0.1811 0.2082 0.0102  0.0148  0.0257  250 ASN A OD1 
2005 N ND2 . ASN A 251 ? 0.1514 0.1497 0.1747 0.0098  0.0123  0.0251  250 ASN A ND2 
2006 N N   . PHE A 252 ? 0.1284 0.1287 0.1629 0.0099  0.0154  0.0273  251 PHE A N   
2007 C CA  . PHE A 252 ? 0.1441 0.1447 0.1814 0.0100  0.0166  0.0276  251 PHE A CA  
2008 C C   . PHE A 252 ? 0.1719 0.1738 0.2119 0.0105  0.0178  0.0292  251 PHE A C   
2009 O O   . PHE A 252 ? 0.1977 0.2004 0.2378 0.0107  0.0173  0.0304  251 PHE A O   
2010 C CB  . PHE A 252 ? 0.1468 0.1477 0.1852 0.0097  0.0159  0.0278  251 PHE A CB  
2011 C CG  . PHE A 252 ? 0.1309 0.1306 0.1676 0.0092  0.0152  0.0262  251 PHE A CG  
2012 C CD1 . PHE A 252 ? 0.1161 0.1149 0.1497 0.0089  0.0137  0.0253  251 PHE A CD1 
2013 C CD2 . PHE A 252 ? 0.1376 0.1371 0.1758 0.0091  0.0160  0.0257  251 PHE A CD2 
2014 C CE1 . PHE A 252 ? 0.1069 0.1046 0.1390 0.0085  0.0129  0.0239  251 PHE A CE1 
2015 C CE2 . PHE A 252 ? 0.1289 0.1274 0.1655 0.0087  0.0153  0.0243  251 PHE A CE2 
2016 C CZ  . PHE A 252 ? 0.1260 0.1236 0.1596 0.0084  0.0137  0.0234  251 PHE A CZ  
2017 N N   . HIS A 253 ? 0.1197 0.1215 0.1616 0.0108  0.0194  0.0291  252 HIS A N   
2018 C CA  . HIS A 253 ? 0.1542 0.1568 0.1986 0.0113  0.0206  0.0304  252 HIS A CA  
2019 C C   . HIS A 253 ? 0.1397 0.1428 0.1871 0.0115  0.0217  0.0308  252 HIS A C   
2020 O O   . HIS A 253 ? 0.1226 0.1249 0.1699 0.0114  0.0224  0.0296  252 HIS A O   
2021 C CB  . HIS A 253 ? 0.1780 0.1799 0.2214 0.0116  0.0216  0.0299  252 HIS A CB  
2022 C CG  . HIS A 253 ? 0.2908 0.2933 0.3368 0.0122  0.0231  0.0310  252 HIS A CG  
2023 N ND1 . HIS A 253 ? 0.3192 0.3227 0.3660 0.0125  0.0230  0.0325  252 HIS A ND1 
2024 C CD2 . HIS A 253 ? 0.3041 0.3063 0.3520 0.0126  0.0247  0.0309  252 HIS A CD2 
2025 C CE1 . HIS A 253 ? 0.3004 0.3042 0.3496 0.0130  0.0244  0.0333  252 HIS A CE1 
2026 N NE2 . HIS A 253 ? 0.3222 0.3252 0.3721 0.0131  0.0255  0.0323  252 HIS A NE2 
2027 N N   . ASP A 254 ? 0.1361 0.1405 0.1862 0.0118  0.0219  0.0325  253 ASP A N   
2028 C CA  . ASP A 254 ? 0.1593 0.1642 0.2126 0.0120  0.0230  0.0330  253 ASP A CA  
2029 C C   . ASP A 254 ? 0.1516 0.1560 0.2059 0.0124  0.0249  0.0327  253 ASP A C   
2030 O O   . ASP A 254 ? 0.2146 0.2193 0.2693 0.0129  0.0255  0.0335  253 ASP A O   
2031 C CB  . ASP A 254 ? 0.2008 0.2073 0.2566 0.0121  0.0228  0.0350  253 ASP A CB  
2032 C CG  . ASP A 254 ? 0.2778 0.2847 0.3331 0.0116  0.0212  0.0352  253 ASP A CG  
2033 O OD1 . ASP A 254 ? 0.2664 0.2723 0.3198 0.0112  0.0204  0.0338  253 ASP A OD1 
2034 O OD2 . ASP A 254 ? 0.3151 0.3233 0.3721 0.0117  0.0208  0.0368  253 ASP A OD2 
2035 N N   . THR A 255 ? 0.1098 0.1135 0.1646 0.0124  0.0258  0.0317  254 THR A N   
2036 C CA  . THR A 255 ? 0.1143 0.1172 0.1694 0.0128  0.0275  0.0309  254 THR A CA  
2037 C C   . THR A 255 ? 0.1193 0.1218 0.1763 0.0128  0.0284  0.0311  254 THR A C   
2038 O O   . THR A 255 ? 0.1177 0.1201 0.1749 0.0125  0.0280  0.0305  254 THR A O   
2039 C CB  . THR A 255 ? 0.1621 0.1636 0.2141 0.0124  0.0272  0.0289  254 THR A CB  
2040 O OG1 . THR A 255 ? 0.1442 0.1454 0.1934 0.0121  0.0259  0.0286  254 THR A OG1 
2041 C CG2 . THR A 255 ? 0.1707 0.1706 0.2215 0.0125  0.0284  0.0279  254 THR A CG2 
2042 N N   . TRP A 256 ? 0.0943 0.0968 0.1529 0.0133  0.0295  0.0319  255 TRP A N   
2043 C CA  . TRP A 256 ? 0.0967 0.0989 0.1574 0.0134  0.0304  0.0322  255 TRP A CA  
2044 C C   . TRP A 256 ? 0.1190 0.1194 0.1780 0.0132  0.0310  0.0305  255 TRP A C   
2045 O O   . TRP A 256 ? 0.1496 0.1489 0.2065 0.0132  0.0314  0.0294  255 TRP A O   
2046 C CB  . TRP A 256 ? 0.1003 0.1030 0.1632 0.0140  0.0314  0.0337  255 TRP A CB  
2047 C CG  . TRP A 256 ? 0.0917 0.0941 0.1569 0.0142  0.0324  0.0342  255 TRP A CG  
2048 C CD1 . TRP A 256 ? 0.1416 0.1427 0.2068 0.0144  0.0337  0.0335  255 TRP A CD1 
2049 C CD2 . TRP A 256 ? 0.1058 0.1095 0.1737 0.0143  0.0322  0.0355  255 TRP A CD2 
2050 N NE1 . TRP A 256 ? 0.1430 0.1443 0.2107 0.0146  0.0343  0.0343  255 TRP A NE1 
2051 C CE2 . TRP A 256 ? 0.1239 0.1268 0.1933 0.0145  0.0334  0.0356  255 TRP A CE2 
2052 C CE3 . TRP A 256 ? 0.1371 0.1425 0.2063 0.0141  0.0311  0.0366  255 TRP A CE3 
2053 C CZ2 . TRP A 256 ? 0.1410 0.1449 0.2133 0.0146  0.0336  0.0367  255 TRP A CZ2 
2054 C CZ3 . TRP A 256 ? 0.1477 0.1539 0.2196 0.0142  0.0313  0.0378  255 TRP A CZ3 
2055 C CH2 . TRP A 256 ? 0.1481 0.1536 0.2216 0.0145  0.0325  0.0378  255 TRP A CH2 
2056 N N   . ASP A 257 ? 0.1166 0.1170 0.1766 0.0130  0.0311  0.0303  256 ASP A N   
2057 C CA  . ASP A 257 ? 0.1300 0.1289 0.1888 0.0128  0.0317  0.0288  256 ASP A CA  
2058 C C   . ASP A 257 ? 0.1568 0.1555 0.2181 0.0131  0.0330  0.0296  256 ASP A C   
2059 O O   . ASP A 257 ? 0.1437 0.1434 0.2073 0.0132  0.0328  0.0306  256 ASP A O   
2060 C CB  . ASP A 257 ? 0.1731 0.1719 0.2309 0.0122  0.0308  0.0279  256 ASP A CB  
2061 C CG  . ASP A 257 ? 0.2226 0.2200 0.2790 0.0120  0.0313  0.0264  256 ASP A CG  
2062 O OD1 . ASP A 257 ? 0.2699 0.2672 0.3277 0.0120  0.0320  0.0265  256 ASP A OD1 
2063 O OD2 . ASP A 257 ? 0.2882 0.2847 0.3419 0.0117  0.0312  0.0251  256 ASP A OD2 
2064 N N   . SER A 258 ? 0.1224 0.1200 0.1833 0.0134  0.0341  0.0292  257 SER A N   
2065 C CA  . SER A 258 ? 0.1241 0.1214 0.1873 0.0137  0.0354  0.0299  257 SER A CA  
2066 C C   . SER A 258 ? 0.1683 0.1651 0.2318 0.0135  0.0357  0.0293  257 SER A C   
2067 O O   . SER A 258 ? 0.1893 0.1866 0.2554 0.0137  0.0363  0.0302  257 SER A O   
2068 C CB  . SER A 258 ? 0.1382 0.1343 0.2007 0.0140  0.0366  0.0296  257 SER A CB  
2069 O OG  . SER A 258 ? 0.1302 0.1270 0.1931 0.0144  0.0365  0.0307  257 SER A OG  
2070 N N   . LYS A 259 ? 0.2005 0.1965 0.2616 0.0130  0.0352  0.0277  258 LYS A N   
2071 C CA  . LYS A 259 ? 0.2693 0.2649 0.3308 0.0127  0.0354  0.0271  258 LYS A CA  
2072 C C   . LYS A 259 ? 0.2384 0.2355 0.3021 0.0127  0.0347  0.0281  258 LYS A C   
2073 O O   . LYS A 259 ? 0.2576 0.2548 0.3234 0.0128  0.0353  0.0287  258 LYS A O   
2074 C CB  . LYS A 259 ? 0.3698 0.3645 0.4282 0.0122  0.0348  0.0253  258 LYS A CB  
2075 C CG  . LYS A 259 ? 0.4877 0.4824 0.5465 0.0119  0.0347  0.0247  258 LYS A CG  
2076 C CD  . LYS A 259 ? 0.5882 0.5823 0.6487 0.0121  0.0361  0.0250  258 LYS A CD  
2077 C CE  . LYS A 259 ? 0.6766 0.6711 0.7383 0.0119  0.0359  0.0250  258 LYS A CE  
2078 N NZ  . LYS A 259 ? 0.7149 0.7086 0.7777 0.0121  0.0372  0.0249  258 LYS A NZ  
2079 N N   . ASP A 260 ? 0.2200 0.2180 0.2832 0.0125  0.0334  0.0284  259 ASP A N   
2080 C CA  . ASP A 260 ? 0.1966 0.1960 0.2618 0.0124  0.0325  0.0294  259 ASP A CA  
2081 C C   . ASP A 260 ? 0.1863 0.1870 0.2541 0.0128  0.0326  0.0313  259 ASP A C   
2082 O O   . ASP A 260 ? 0.1924 0.1943 0.2621 0.0127  0.0320  0.0322  259 ASP A O   
2083 C CB  . ASP A 260 ? 0.2103 0.2101 0.2736 0.0119  0.0311  0.0287  259 ASP A CB  
2084 C CG  . ASP A 260 ? 0.2548 0.2536 0.3158 0.0115  0.0308  0.0270  259 ASP A CG  
2085 O OD1 . ASP A 260 ? 0.2549 0.2526 0.3155 0.0115  0.0317  0.0262  259 ASP A OD1 
2086 O OD2 . ASP A 260 ? 0.2666 0.2655 0.3258 0.0111  0.0297  0.0263  259 ASP A OD2 
2087 N N   . GLN A 261 ? 0.1700 0.1707 0.2382 0.0132  0.0334  0.0319  260 GLN A N   
2088 C CA  . GLN A 261 ? 0.1458 0.1478 0.2165 0.0137  0.0334  0.0338  260 GLN A CA  
2089 C C   . GLN A 261 ? 0.1570 0.1605 0.2281 0.0134  0.0320  0.0346  260 GLN A C   
2090 O O   . GLN A 261 ? 0.1637 0.1685 0.2372 0.0135  0.0317  0.0360  260 GLN A O   
2091 C CB  . GLN A 261 ? 0.1510 0.1532 0.2247 0.0140  0.0344  0.0348  260 GLN A CB  
2092 C CG  . GLN A 261 ? 0.1611 0.1619 0.2347 0.0143  0.0359  0.0343  260 GLN A CG  
2093 C CD  . GLN A 261 ? 0.1447 0.1456 0.2187 0.0147  0.0366  0.0351  260 GLN A CD  
2094 O OE1 . GLN A 261 ? 0.2074 0.2095 0.2838 0.0151  0.0367  0.0368  260 GLN A OE1 
2095 N NE2 . GLN A 261 ? 0.1455 0.1451 0.2171 0.0147  0.0369  0.0340  260 GLN A NE2 
2096 N N   . ARG A 262 ? 0.1253 0.1286 0.1938 0.0131  0.0311  0.0337  261 ARG A N   
2097 C CA  . ARG A 262 ? 0.1388 0.1436 0.2075 0.0129  0.0297  0.0345  261 ARG A CA  
2098 C C   . ARG A 262 ? 0.1263 0.1307 0.1923 0.0128  0.0292  0.0336  261 ARG A C   
2099 O O   . ARG A 262 ? 0.1272 0.1301 0.1910 0.0127  0.0297  0.0322  261 ARG A O   
2100 C CB  . ARG A 262 ? 0.1796 0.1849 0.2487 0.0125  0.0288  0.0342  261 ARG A CB  
2101 C CG  . ARG A 262 ? 0.1613 0.1653 0.2281 0.0120  0.0286  0.0324  261 ARG A CG  
2102 C CD  . ARG A 262 ? 0.1661 0.1709 0.2330 0.0115  0.0272  0.0323  261 ARG A CD  
2103 N NE  . ARG A 262 ? 0.1962 0.2018 0.2621 0.0114  0.0261  0.0326  261 ARG A NE  
2104 C CZ  . ARG A 262 ? 0.1896 0.1958 0.2551 0.0109  0.0248  0.0324  261 ARG A CZ  
2105 N NH1 . ARG A 262 ? 0.2223 0.2284 0.2885 0.0106  0.0245  0.0321  261 ARG A NH1 
2106 N NH2 . ARG A 262 ? 0.1637 0.1703 0.2280 0.0108  0.0238  0.0327  261 ARG A NH2 
2107 N N   . SER A 263 ? 0.1550 0.1607 0.2210 0.0127  0.0281  0.0344  262 SER A N   
2108 C CA  . SER A 263 ? 0.1321 0.1374 0.1954 0.0125  0.0274  0.0336  262 SER A CA  
2109 C C   . SER A 263 ? 0.1442 0.1495 0.2060 0.0120  0.0263  0.0325  262 SER A C   
2110 O O   . SER A 263 ? 0.1543 0.1604 0.2175 0.0117  0.0257  0.0330  262 SER A O   
2111 C CB  . SER A 263 ? 0.1798 0.1867 0.2437 0.0128  0.0268  0.0350  262 SER A CB  
2112 O OG  . SER A 263 ? 0.2913 0.2985 0.3569 0.0133  0.0278  0.0363  262 SER A OG  
2113 N N   . TYR A 264 ? 0.1004 0.1047 0.1594 0.0118  0.0260  0.0312  263 TYR A N   
2114 C CA  . TYR A 264 ? 0.1090 0.1128 0.1657 0.0112  0.0246  0.0301  263 TYR A CA  
2115 C C   . TYR A 264 ? 0.1051 0.1084 0.1588 0.0110  0.0234  0.0298  263 TYR A C   
2116 O O   . TYR A 264 ? 0.1174 0.1204 0.1704 0.0113  0.0241  0.0297  263 TYR A O   
2117 C CB  . TYR A 264 ? 0.1018 0.1045 0.1572 0.0109  0.0251  0.0284  263 TYR A CB  
2118 C CG  . TYR A 264 ? 0.1300 0.1323 0.1868 0.0109  0.0257  0.0282  263 TYR A CG  
2119 C CD1 . TYR A 264 ? 0.1449 0.1478 0.2029 0.0106  0.0251  0.0284  263 TYR A CD1 
2120 C CD2 . TYR A 264 ? 0.1115 0.1128 0.1683 0.0112  0.0270  0.0277  263 TYR A CD2 
2121 C CE1 . TYR A 264 ? 0.1572 0.1598 0.2166 0.0106  0.0257  0.0283  263 TYR A CE1 
2122 C CE2 . TYR A 264 ? 0.1295 0.1303 0.1874 0.0111  0.0276  0.0276  263 TYR A CE2 
2123 C CZ  . TYR A 264 ? 0.1486 0.1501 0.2078 0.0108  0.0269  0.0279  263 TYR A CZ  
2124 O OH  . TYR A 264 ? 0.1767 0.1779 0.2372 0.0108  0.0276  0.0277  263 TYR A OH  
2125 N N   . PRO A 265 ? 0.0869 0.0901 0.1387 0.0105  0.0217  0.0295  264 PRO A N   
2126 C CA  . PRO A 265 ? 0.1085 0.1111 0.1573 0.0104  0.0205  0.0292  264 PRO A CA  
2127 C C   . PRO A 265 ? 0.1584 0.1597 0.2045 0.0101  0.0205  0.0273  264 PRO A C   
2128 O O   . PRO A 265 ? 0.2150 0.2157 0.2603 0.0097  0.0200  0.0263  264 PRO A O   
2129 C CB  . PRO A 265 ? 0.1609 0.1638 0.2089 0.0100  0.0187  0.0295  264 PRO A CB  
2130 C CG  . PRO A 265 ? 0.1822 0.1852 0.2317 0.0097  0.0187  0.0293  264 PRO A CG  
2131 C CD  . PRO A 265 ? 0.1431 0.1466 0.1955 0.0101  0.0206  0.0296  264 PRO A CD  
2132 N N   . ARG A 266 ? 0.0930 0.0938 0.1376 0.0104  0.0210  0.0270  265 ARG A N   
2133 C CA  . ARG A 266 ? 0.1122 0.1118 0.1545 0.0101  0.0212  0.0253  265 ARG A CA  
2134 C C   . ARG A 266 ? 0.1215 0.1205 0.1607 0.0100  0.0201  0.0248  265 ARG A C   
2135 O O   . ARG A 266 ? 0.1182 0.1176 0.1574 0.0103  0.0200  0.0257  265 ARG A O   
2136 C CB  . ARG A 266 ? 0.1100 0.1093 0.1533 0.0106  0.0231  0.0249  265 ARG A CB  
2137 C CG  . ARG A 266 ? 0.1429 0.1426 0.1889 0.0108  0.0245  0.0251  265 ARG A CG  
2138 C CD  . ARG A 266 ? 0.1732 0.1717 0.2184 0.0109  0.0258  0.0240  265 ARG A CD  
2139 N NE  . ARG A 266 ? 0.1520 0.1495 0.1944 0.0105  0.0253  0.0224  265 ARG A NE  
2140 C CZ  . ARG A 266 ? 0.1220 0.1190 0.1637 0.0100  0.0250  0.0213  265 ARG A CZ  
2141 N NH1 . ARG A 266 ? 0.0984 0.0958 0.1420 0.0100  0.0253  0.0217  265 ARG A NH1 
2142 N NH2 . ARG A 266 ? 0.1179 0.1141 0.1569 0.0097  0.0245  0.0200  265 ARG A NH2 
2143 N N   . LEU A 267 ? 0.0889 0.0869 0.1256 0.0096  0.0193  0.0234  266 LEU A N   
2144 C CA  . LEU A 267 ? 0.0723 0.0697 0.1060 0.0094  0.0184  0.0227  266 LEU A CA  
2145 C C   . LEU A 267 ? 0.1153 0.1118 0.1478 0.0095  0.0194  0.0215  266 LEU A C   
2146 O O   . LEU A 267 ? 0.1256 0.1216 0.1577 0.0092  0.0197  0.0204  266 LEU A O   
2147 C CB  . LEU A 267 ? 0.0672 0.0639 0.0987 0.0089  0.0166  0.0220  266 LEU A CB  
2148 C CG  . LEU A 267 ? 0.0779 0.0739 0.1062 0.0087  0.0156  0.0212  266 LEU A CG  
2149 C CD1 . LEU A 267 ? 0.1143 0.1110 0.1426 0.0090  0.0151  0.0224  266 LEU A CD1 
2150 C CD2 . LEU A 267 ? 0.1044 0.0996 0.1308 0.0082  0.0139  0.0203  266 LEU A CD2 
2151 N N   . THR A 268 ? 0.0980 0.0944 0.1299 0.0098  0.0201  0.0217  267 THR A N   
2152 C CA  . THR A 268 ? 0.0965 0.0920 0.1270 0.0098  0.0210  0.0205  267 THR A CA  
2153 C C   . THR A 268 ? 0.1189 0.1137 0.1462 0.0095  0.0197  0.0196  267 THR A C   
2154 O O   . THR A 268 ? 0.1618 0.1570 0.1884 0.0096  0.0189  0.0203  267 THR A O   
2155 C CB  . THR A 268 ? 0.1591 0.1548 0.1910 0.0104  0.0224  0.0212  267 THR A CB  
2156 O OG1 . THR A 268 ? 0.1878 0.1842 0.2228 0.0107  0.0235  0.0222  267 THR A OG1 
2157 C CG2 . THR A 268 ? 0.1891 0.1838 0.2195 0.0105  0.0234  0.0200  267 THR A CG2 
2158 N N   . VAL A 269 ? 0.1128 0.1067 0.1382 0.0092  0.0196  0.0181  268 VAL A N   
2159 C CA  . VAL A 269 ? 0.1353 0.1286 0.1577 0.0089  0.0185  0.0172  268 VAL A CA  
2160 C C   . VAL A 269 ? 0.1215 0.1140 0.1426 0.0089  0.0195  0.0161  268 VAL A C   
2161 O O   . VAL A 269 ? 0.1530 0.1451 0.1738 0.0087  0.0199  0.0151  268 VAL A O   
2162 C CB  . VAL A 269 ? 0.1757 0.1687 0.1967 0.0084  0.0169  0.0166  268 VAL A CB  
2163 C CG1 . VAL A 269 ? 0.2199 0.2120 0.2376 0.0081  0.0159  0.0156  268 VAL A CG1 
2164 C CG2 . VAL A 269 ? 0.1868 0.1803 0.2088 0.0084  0.0158  0.0177  268 VAL A CG2 
2165 N N   . GLU A 270 ? 0.1442 0.1366 0.1647 0.0092  0.0200  0.0162  269 GLU A N   
2166 C CA  . GLU A 270 ? 0.1886 0.1801 0.2078 0.0093  0.0210  0.0152  269 GLU A CA  
2167 C C   . GLU A 270 ? 0.1508 0.1417 0.1672 0.0088  0.0199  0.0138  269 GLU A C   
2168 O O   . GLU A 270 ? 0.1530 0.1439 0.1679 0.0086  0.0186  0.0139  269 GLU A O   
2169 C CB  . GLU A 270 ? 0.2808 0.2723 0.3001 0.0097  0.0216  0.0157  269 GLU A CB  
2170 C CG  . GLU A 270 ? 0.3778 0.3696 0.3997 0.0102  0.0230  0.0167  269 GLU A CG  
2171 C CD  . GLU A 270 ? 0.4929 0.4844 0.5145 0.0106  0.0236  0.0172  269 GLU A CD  
2172 O OE1 . GLU A 270 ? 0.5567 0.5484 0.5804 0.0111  0.0248  0.0180  269 GLU A OE1 
2173 O OE2 . GLU A 270 ? 0.4738 0.4649 0.4932 0.0105  0.0228  0.0167  269 GLU A OE2 
2174 N N   . LEU A 271 ? 0.1280 0.1183 0.1435 0.0086  0.0207  0.0127  270 LEU A N   
2175 C CA  . LEU A 271 ? 0.1198 0.1095 0.1325 0.0082  0.0200  0.0114  270 LEU A CA  
2176 C C   . LEU A 271 ? 0.1460 0.1355 0.1574 0.0085  0.0199  0.0115  270 LEU A C   
2177 O O   . LEU A 271 ? 0.1755 0.1648 0.1878 0.0089  0.0210  0.0119  270 LEU A O   
2178 C CB  . LEU A 271 ? 0.1370 0.1259 0.1486 0.0078  0.0202  0.0102  270 LEU A CB  
2179 C CG  . LEU A 271 ? 0.1491 0.1376 0.1581 0.0072  0.0191  0.0090  270 LEU A CG  
2180 C CD1 . LEU A 271 ? 0.1597 0.1487 0.1692 0.0070  0.0186  0.0091  270 LEU A CD1 
2181 C CD2 . LEU A 271 ? 0.1813 0.1691 0.1892 0.0067  0.0191  0.0079  270 LEU A CD2 
2182 N N   . PRO A 272 ? 0.1132 0.1024 0.1224 0.0082  0.0186  0.0110  271 PRO A N   
2183 C CA  . PRO A 272 ? 0.1446 0.1336 0.1527 0.0085  0.0184  0.0111  271 PRO A CA  
2184 C C   . PRO A 272 ? 0.1519 0.1400 0.1583 0.0084  0.0192  0.0099  271 PRO A C   
2185 O O   . PRO A 272 ? 0.1579 0.1459 0.1632 0.0086  0.0190  0.0098  271 PRO A O   
2186 C CB  . PRO A 272 ? 0.1445 0.1336 0.1508 0.0082  0.0166  0.0109  271 PRO A CB  
2187 C CG  . PRO A 272 ? 0.1095 0.0983 0.1150 0.0077  0.0161  0.0100  271 PRO A CG  
2188 C CD  . PRO A 272 ? 0.1091 0.0983 0.1170 0.0077  0.0170  0.0106  271 PRO A CD  
2189 N N   . VAL A 273 ? 0.1576 0.1452 0.1635 0.0078  0.0191  0.0090  272 VAL A N   
2190 C CA  . VAL A 273 ? 0.1647 0.1514 0.1688 0.0073  0.0188  0.0078  272 VAL A CA  
2191 C C   . VAL A 273 ? 0.2244 0.2109 0.2296 0.0071  0.0196  0.0078  272 VAL A C   
2192 O O   . VAL A 273 ? 0.2129 0.1997 0.2201 0.0074  0.0202  0.0085  272 VAL A O   
2193 C CB  . VAL A 273 ? 0.1393 0.1259 0.1411 0.0066  0.0175  0.0066  272 VAL A CB  
2194 C CG1 . VAL A 273 ? 0.1381 0.1249 0.1386 0.0067  0.0167  0.0066  272 VAL A CG1 
2195 C CG2 . VAL A 273 ? 0.1465 0.1334 0.1488 0.0063  0.0173  0.0064  272 VAL A CG2 
2196 N N   . GLN A 274 ? 0.2406 0.2264 0.2445 0.0067  0.0195  0.0069  273 GLN A N   
2197 C CA  . GLN A 274 ? 0.2723 0.2577 0.2770 0.0066  0.0202  0.0067  273 GLN A CA  
2198 C C   . GLN A 274 ? 0.2227 0.2086 0.2281 0.0063  0.0200  0.0066  273 GLN A C   
2199 O O   . GLN A 274 ? 0.2598 0.2460 0.2640 0.0059  0.0190  0.0060  273 GLN A O   
2200 C CB  . GLN A 274 ? 0.3602 0.3451 0.3633 0.0061  0.0199  0.0058  273 GLN A CB  
2201 C CG  . GLN A 274 ? 0.4424 0.4266 0.4452 0.0064  0.0204  0.0060  273 GLN A CG  
2202 C CD  . GLN A 274 ? 0.5312 0.5149 0.5356 0.0068  0.0219  0.0066  273 GLN A CD  
2203 O OE1 . GLN A 274 ? 0.5468 0.5306 0.5526 0.0068  0.0225  0.0068  273 GLN A OE1 
2204 N NE2 . GLN A 274 ? 0.5663 0.5495 0.5708 0.0071  0.0225  0.0070  273 GLN A NE2 
2205 N N   . PRO A 275 ? 0.2548 0.2407 0.2621 0.0065  0.0210  0.0071  274 PRO A N   
2206 C CA  . PRO A 275 ? 0.2870 0.2724 0.2957 0.0070  0.0223  0.0078  274 PRO A CA  
2207 C C   . PRO A 275 ? 0.3037 0.2898 0.3147 0.0077  0.0230  0.0092  274 PRO A C   
2208 O O   . PRO A 275 ? 0.3226 0.3085 0.3354 0.0081  0.0240  0.0099  274 PRO A O   
2209 C CB  . PRO A 275 ? 0.2839 0.2693 0.2935 0.0068  0.0228  0.0076  274 PRO A CB  
2210 C CG  . PRO A 275 ? 0.2910 0.2770 0.3007 0.0065  0.0220  0.0074  274 PRO A CG  
2211 C CD  . PRO A 275 ? 0.2705 0.2566 0.2782 0.0063  0.0208  0.0069  274 PRO A CD  
2212 N N   . TYR A 276 ? 0.2587 0.2454 0.2697 0.0079  0.0223  0.0096  275 TYR A N   
2213 C CA  . TYR A 276 ? 0.2152 0.2028 0.2284 0.0085  0.0228  0.0110  275 TYR A CA  
2214 C C   . TYR A 276 ? 0.2216 0.2098 0.2374 0.0088  0.0235  0.0119  275 TYR A C   
2215 O O   . TYR A 276 ? 0.2282 0.2171 0.2462 0.0093  0.0241  0.0132  275 TYR A O   
2216 C CB  . TYR A 276 ? 0.2940 0.2812 0.3075 0.0090  0.0235  0.0116  275 TYR A CB  
2217 C CG  . TYR A 276 ? 0.3288 0.3155 0.3398 0.0088  0.0229  0.0108  275 TYR A CG  
2218 C CD1 . TYR A 276 ? 0.3289 0.3162 0.3392 0.0090  0.0221  0.0111  275 TYR A CD1 
2219 C CD2 . TYR A 276 ? 0.3465 0.3322 0.3560 0.0084  0.0230  0.0099  275 TYR A CD2 
2220 C CE1 . TYR A 276 ? 0.3544 0.3411 0.3624 0.0088  0.0215  0.0103  275 TYR A CE1 
2221 C CE2 . TYR A 276 ? 0.3559 0.3411 0.3633 0.0082  0.0224  0.0092  275 TYR A CE2 
2222 C CZ  . TYR A 276 ? 0.3570 0.3427 0.3636 0.0084  0.0216  0.0094  275 TYR A CZ  
2223 O OH  . TYR A 276 ? 0.3707 0.3559 0.3752 0.0081  0.0209  0.0087  275 TYR A OH  
2224 N N   . ASN A 277 ? 0.2183 0.2064 0.2340 0.0083  0.0232  0.0113  276 ASN A N   
2225 C CA  . ASN A 277 ? 0.1750 0.1636 0.1931 0.0085  0.0238  0.0119  276 ASN A CA  
2226 C C   . ASN A 277 ? 0.1763 0.1660 0.1960 0.0087  0.0234  0.0129  276 ASN A C   
2227 O O   . ASN A 277 ? 0.1663 0.1564 0.1849 0.0086  0.0225  0.0127  276 ASN A O   
2228 C CB  . ASN A 277 ? 0.1969 0.1850 0.2142 0.0079  0.0236  0.0109  276 ASN A CB  
2229 C CG  . ASN A 277 ? 0.2240 0.2123 0.2396 0.0075  0.0225  0.0101  276 ASN A CG  
2230 O OD1 . ASN A 277 ? 0.2515 0.2395 0.2649 0.0072  0.0218  0.0094  276 ASN A OD1 
2231 N ND2 . ASN A 277 ? 0.2654 0.2543 0.2822 0.0074  0.0222  0.0103  276 ASN A ND2 
2232 N N   . ASP A 278 ? 0.1418 0.1323 0.1642 0.0091  0.0240  0.0140  277 ASP A N   
2233 C CA  . ASP A 278 ? 0.1206 0.1123 0.1448 0.0092  0.0235  0.0150  277 ASP A CA  
2234 C C   . ASP A 278 ? 0.1422 0.1338 0.1658 0.0087  0.0229  0.0142  277 ASP A C   
2235 O O   . ASP A 278 ? 0.1434 0.1348 0.1675 0.0085  0.0232  0.0138  277 ASP A O   
2236 C CB  . ASP A 278 ? 0.1404 0.1329 0.1678 0.0096  0.0243  0.0164  277 ASP A CB  
2237 C CG  . ASP A 278 ? 0.1642 0.1579 0.1936 0.0097  0.0239  0.0174  277 ASP A CG  
2238 O OD1 . ASP A 278 ? 0.1307 0.1244 0.1586 0.0093  0.0223  0.0170  277 ASP A OD1 
2239 O OD2 . ASP A 278 ? 0.1598 0.1541 0.1917 0.0099  0.0244  0.0183  277 ASP A OD2 
2240 N N   . VAL A 279 ? 0.1311 0.1231 0.1535 0.0085  0.0219  0.0139  278 VAL A N   
2241 C CA  . VAL A 279 ? 0.1458 0.1376 0.1675 0.0080  0.0213  0.0130  278 VAL A CA  
2242 C C   . VAL A 279 ? 0.1677 0.1602 0.1917 0.0079  0.0210  0.0138  278 VAL A C   
2243 O O   . VAL A 279 ? 0.1781 0.1705 0.2019 0.0076  0.0207  0.0132  278 VAL A O   
2244 C CB  . VAL A 279 ? 0.1779 0.1692 0.1968 0.0075  0.0195  0.0124  278 VAL A CB  
2245 C CG1 . VAL A 279 ? 0.2012 0.1920 0.2180 0.0076  0.0199  0.0115  278 VAL A CG1 
2246 C CG2 . VAL A 279 ? 0.1791 0.1706 0.1981 0.0075  0.0181  0.0133  278 VAL A CG2 
2247 N N   . PHE A 280 ? 0.1324 0.1255 0.1585 0.0083  0.0212  0.0150  279 PHE A N   
2248 C CA  . PHE A 280 ? 0.1053 0.0991 0.1337 0.0082  0.0211  0.0158  279 PHE A CA  
2249 C C   . PHE A 280 ? 0.1362 0.1303 0.1670 0.0086  0.0228  0.0162  279 PHE A C   
2250 O O   . PHE A 280 ? 0.1423 0.1371 0.1755 0.0087  0.0229  0.0170  279 PHE A O   
2251 C CB  . PHE A 280 ? 0.1182 0.1125 0.1473 0.0083  0.0199  0.0170  279 PHE A CB  
2252 C CG  . PHE A 280 ? 0.1435 0.1374 0.1706 0.0078  0.0179  0.0166  279 PHE A CG  
2253 C CD1 . PHE A 280 ? 0.2074 0.2011 0.2343 0.0074  0.0170  0.0161  279 PHE A CD1 
2254 C CD2 . PHE A 280 ? 0.1659 0.1596 0.1914 0.0079  0.0169  0.0169  279 PHE A CD2 
2255 C CE1 . PHE A 280 ? 0.2037 0.1969 0.2287 0.0070  0.0151  0.0158  279 PHE A CE1 
2256 C CE2 . PHE A 280 ? 0.1794 0.1726 0.2029 0.0075  0.0150  0.0165  279 PHE A CE2 
2257 C CZ  . PHE A 280 ? 0.1798 0.1727 0.2031 0.0071  0.0142  0.0160  279 PHE A CZ  
2258 N N   . GLU A 281 ? 0.1747 0.1678 0.2042 0.0086  0.0235  0.0155  280 GLU A N   
2259 C CA  . GLU A 281 ? 0.2039 0.1967 0.2349 0.0089  0.0245  0.0159  280 GLU A CA  
2260 C C   . GLU A 281 ? 0.1989 0.1917 0.2310 0.0086  0.0247  0.0157  280 GLU A C   
2261 O O   . GLU A 281 ? 0.2258 0.2188 0.2600 0.0089  0.0254  0.0165  280 GLU A O   
2262 C CB  . GLU A 281 ? 0.2567 0.2482 0.2858 0.0089  0.0252  0.0151  280 GLU A CB  
2263 C CG  . GLU A 281 ? 0.3700 0.3607 0.3965 0.0083  0.0247  0.0136  280 GLU A CG  
2264 C CD  . GLU A 281 ? 0.4728 0.4624 0.4973 0.0083  0.0251  0.0128  280 GLU A CD  
2265 O OE1 . GLU A 281 ? 0.5160 0.5053 0.5415 0.0087  0.0261  0.0134  280 GLU A OE1 
2266 O OE2 . GLU A 281 ? 0.4898 0.4789 0.5118 0.0079  0.0245  0.0117  280 GLU A OE2 
2267 N N   . LYS A 282 ? 0.2300 0.2226 0.2608 0.0082  0.0240  0.0148  281 LYS A N   
2268 C CA  . LYS A 282 ? 0.2590 0.2516 0.2907 0.0080  0.0242  0.0145  281 LYS A CA  
2269 C C   . LYS A 282 ? 0.2098 0.2035 0.2441 0.0080  0.0238  0.0155  281 LYS A C   
2270 O O   . LYS A 282 ? 0.2270 0.2208 0.2627 0.0080  0.0241  0.0157  281 LYS A O   
2271 C CB  . LYS A 282 ? 0.4045 0.3965 0.4340 0.0074  0.0236  0.0132  281 LYS A CB  
2272 C CG  . LYS A 282 ? 0.5218 0.5126 0.5489 0.0073  0.0239  0.0122  281 LYS A CG  
2273 C CD  . LYS A 282 ? 0.6214 0.6118 0.6496 0.0076  0.0252  0.0126  281 LYS A CD  
2274 C CE  . LYS A 282 ? 0.7000 0.6901 0.7288 0.0075  0.0257  0.0122  281 LYS A CE  
2275 N NZ  . LYS A 282 ? 0.7360 0.7258 0.7664 0.0078  0.0269  0.0128  281 LYS A NZ  
2276 N N   . MET A 283 ? 0.1602 0.1547 0.1952 0.0082  0.0232  0.0163  282 MET A N   
2277 C CA  . MET A 283 ? 0.1370 0.1327 0.1745 0.0082  0.0228  0.0174  282 MET A CA  
2278 C C   . MET A 283 ? 0.1020 0.0981 0.1420 0.0086  0.0237  0.0185  282 MET A C   
2279 O O   . MET A 283 ? 0.1504 0.1464 0.1907 0.0090  0.0243  0.0190  282 MET A O   
2280 C CB  . MET A 283 ? 0.1758 0.1720 0.2127 0.0081  0.0214  0.0179  282 MET A CB  
2281 C CG  . MET A 283 ? 0.2828 0.2781 0.3169 0.0075  0.0199  0.0167  282 MET A CG  
2282 S SD  . MET A 283 ? 0.2935 0.2886 0.3260 0.0073  0.0176  0.0171  282 MET A SD  
2283 C CE  . MET A 283 ? 0.0480 0.0442 0.0838 0.0075  0.0177  0.0188  282 MET A CE  
2284 N N   . THR A 284 ? 0.1065 0.1030 0.1484 0.0086  0.0237  0.0189  283 THR A N   
2285 C CA  . THR A 284 ? 0.1070 0.1039 0.1513 0.0089  0.0246  0.0200  283 THR A CA  
2286 C C   . THR A 284 ? 0.1240 0.1221 0.1703 0.0092  0.0242  0.0215  283 THR A C   
2287 O O   . THR A 284 ? 0.1048 0.1037 0.1508 0.0091  0.0232  0.0217  283 THR A O   
2288 C CB  . THR A 284 ? 0.1449 0.1418 0.1907 0.0088  0.0247  0.0199  283 THR A CB  
2289 O OG1 . THR A 284 ? 0.1414 0.1393 0.1883 0.0085  0.0236  0.0204  283 THR A OG1 
2290 C CG2 . THR A 284 ? 0.1604 0.1563 0.2043 0.0084  0.0249  0.0185  283 THR A CG2 
2291 N N   . GLY A 285 ? 0.1208 0.1193 0.1691 0.0097  0.0251  0.0226  284 GLY A N   
2292 C CA  . GLY A 285 ? 0.1029 0.1028 0.1533 0.0099  0.0247  0.0242  284 GLY A CA  
2293 C C   . GLY A 285 ? 0.0978 0.0987 0.1496 0.0096  0.0237  0.0247  284 GLY A C   
2294 O O   . GLY A 285 ? 0.0870 0.0883 0.1383 0.0095  0.0224  0.0253  284 GLY A O   
2295 N N   . MET A 286 ? 0.0965 0.0973 0.1491 0.0094  0.0237  0.0244  285 MET A N   
2296 C CA  . MET A 286 ? 0.0906 0.0923 0.1447 0.0091  0.0227  0.0249  285 MET A CA  
2297 C C   . MET A 286 ? 0.0997 0.1005 0.1506 0.0085  0.0209  0.0238  285 MET A C   
2298 O O   . MET A 286 ? 0.0921 0.0930 0.1424 0.0082  0.0193  0.0242  285 MET A O   
2299 C CB  . MET A 286 ? 0.1146 0.1160 0.1697 0.0089  0.0230  0.0246  285 MET A CB  
2300 C CG  . MET A 286 ? 0.1459 0.1477 0.2035 0.0093  0.0240  0.0257  285 MET A CG  
2301 S SD  . MET A 286 ? 0.1591 0.1626 0.2195 0.0095  0.0234  0.0277  285 MET A SD  
2302 C CE  . MET A 286 ? 0.1561 0.1599 0.2175 0.0090  0.0225  0.0274  285 MET A CE  
2303 N N   . GLN A 287 ? 0.0832 0.0832 0.1319 0.0084  0.0211  0.0224  286 GLN A N   
2304 C CA  . GLN A 287 ? 0.0598 0.0588 0.1052 0.0078  0.0194  0.0214  286 GLN A CA  
2305 C C   . GLN A 287 ? 0.0836 0.0823 0.1272 0.0079  0.0185  0.0217  286 GLN A C   
2306 O O   . GLN A 287 ? 0.0938 0.0920 0.1356 0.0075  0.0167  0.0215  286 GLN A O   
2307 C CB  . GLN A 287 ? 0.0585 0.0567 0.1021 0.0077  0.0200  0.0199  286 GLN A CB  
2308 C CG  . GLN A 287 ? 0.1033 0.1017 0.1481 0.0075  0.0205  0.0194  286 GLN A CG  
2309 C CD  . GLN A 287 ? 0.1403 0.1379 0.1835 0.0075  0.0214  0.0182  286 GLN A CD  
2310 O OE1 . GLN A 287 ? 0.1307 0.1277 0.1722 0.0076  0.0218  0.0177  286 GLN A OE1 
2311 N NE2 . GLN A 287 ? 0.1834 0.1807 0.2266 0.0072  0.0214  0.0175  286 GLN A NE2 
2312 N N   . MET A 288 ? 0.0892 0.0881 0.1332 0.0084  0.0196  0.0223  287 MET A N   
2313 C CA  . MET A 288 ? 0.0718 0.0707 0.1145 0.0085  0.0187  0.0228  287 MET A CA  
2314 C C   . MET A 288 ? 0.0798 0.0795 0.1238 0.0084  0.0177  0.0241  287 MET A C   
2315 O O   . MET A 288 ? 0.0963 0.0957 0.1385 0.0083  0.0163  0.0242  287 MET A O   
2316 C CB  . MET A 288 ? 0.1015 0.1007 0.1450 0.0090  0.0202  0.0233  287 MET A CB  
2317 C CG  . MET A 288 ? 0.1012 0.0994 0.1422 0.0090  0.0207  0.0220  287 MET A CG  
2318 S SD  . MET A 288 ? 0.1164 0.1139 0.1541 0.0087  0.0190  0.0217  287 MET A SD  
2319 C CE  . MET A 288 ? 0.1279 0.1243 0.1631 0.0086  0.0196  0.0200  287 MET A CE  
2320 N N   . GLU A 289 ? 0.0923 0.0930 0.1394 0.0086  0.0185  0.0252  288 GLU A N   
2321 C CA  . GLU A 289 ? 0.1025 0.1039 0.1509 0.0086  0.0175  0.0265  288 GLU A CA  
2322 C C   . GLU A 289 ? 0.0823 0.0832 0.1291 0.0081  0.0157  0.0258  288 GLU A C   
2323 O O   . GLU A 289 ? 0.0940 0.0948 0.1397 0.0080  0.0143  0.0263  288 GLU A O   
2324 C CB  . GLU A 289 ? 0.1107 0.1133 0.1629 0.0089  0.0187  0.0276  288 GLU A CB  
2325 C CG  . GLU A 289 ? 0.1271 0.1307 0.1811 0.0089  0.0180  0.0290  288 GLU A CG  
2326 C CD  . GLU A 289 ? 0.1896 0.1943 0.2473 0.0092  0.0193  0.0301  288 GLU A CD  
2327 O OE1 . GLU A 289 ? 0.1762 0.1809 0.2350 0.0090  0.0194  0.0296  288 GLU A OE1 
2328 O OE2 . GLU A 289 ? 0.2269 0.2325 0.2865 0.0096  0.0201  0.0314  288 GLU A OE2 
2329 N N   . SER A 290 ? 0.0677 0.0680 0.1141 0.0077  0.0156  0.0247  289 SER A N   
2330 C CA  . SER A 290 ? 0.0751 0.0746 0.1198 0.0072  0.0139  0.0240  289 SER A CA  
2331 C C   . SER A 290 ? 0.0855 0.0838 0.1266 0.0071  0.0126  0.0230  289 SER A C   
2332 O O   . SER A 290 ? 0.1035 0.1014 0.1432 0.0069  0.0109  0.0230  289 SER A O   
2333 C CB  . SER A 290 ? 0.1158 0.1151 0.1611 0.0070  0.0142  0.0230  289 SER A CB  
2334 O OG  . SER A 290 ? 0.1702 0.1688 0.2142 0.0065  0.0124  0.0224  289 SER A OG  
2335 N N   . PHE A 291 ? 0.0835 0.0814 0.1231 0.0072  0.0133  0.0222  290 PHE A N   
2336 C CA  . PHE A 291 ? 0.0776 0.0744 0.1138 0.0070  0.0122  0.0214  290 PHE A CA  
2337 C C   . PHE A 291 ? 0.0925 0.0896 0.1282 0.0073  0.0114  0.0224  290 PHE A C   
2338 O O   . PHE A 291 ? 0.0942 0.0906 0.1277 0.0071  0.0098  0.0220  290 PHE A O   
2339 C CB  . PHE A 291 ? 0.0749 0.0713 0.1101 0.0072  0.0134  0.0206  290 PHE A CB  
2340 C CG  . PHE A 291 ? 0.0676 0.0631 0.0996 0.0071  0.0127  0.0198  290 PHE A CG  
2341 C CD1 . PHE A 291 ? 0.0698 0.0644 0.0993 0.0068  0.0109  0.0191  290 PHE A CD1 
2342 C CD2 . PHE A 291 ? 0.0995 0.0951 0.1312 0.0074  0.0139  0.0197  290 PHE A CD2 
2343 C CE1 . PHE A 291 ? 0.0883 0.0821 0.1150 0.0068  0.0103  0.0184  290 PHE A CE1 
2344 C CE2 . PHE A 291 ? 0.1288 0.1236 0.1577 0.0074  0.0133  0.0190  290 PHE A CE2 
2345 C CZ  . PHE A 291 ? 0.1103 0.1042 0.1367 0.0071  0.0115  0.0184  290 PHE A CZ  
2346 N N   . LYS A 292 ? 0.0837 0.0819 0.1216 0.0077  0.0125  0.0238  291 LYS A N   
2347 C CA  . LYS A 292 ? 0.0953 0.0940 0.1329 0.0079  0.0118  0.0249  291 LYS A CA  
2348 C C   . LYS A 292 ? 0.0899 0.0887 0.1277 0.0077  0.0103  0.0254  291 LYS A C   
2349 O O   . LYS A 292 ? 0.0896 0.0879 0.1252 0.0077  0.0090  0.0254  291 LYS A O   
2350 C CB  . LYS A 292 ? 0.0941 0.0942 0.1344 0.0084  0.0133  0.0264  291 LYS A CB  
2351 C CG  . LYS A 292 ? 0.1064 0.1070 0.1463 0.0086  0.0127  0.0276  291 LYS A CG  
2352 C CD  . LYS A 292 ? 0.1177 0.1198 0.1607 0.0091  0.0141  0.0292  291 LYS A CD  
2353 C CE  . LYS A 292 ? 0.1656 0.1684 0.2079 0.0093  0.0135  0.0303  291 LYS A CE  
2354 N NZ  . LYS A 292 ? 0.2103 0.2146 0.2556 0.0097  0.0147  0.0321  291 LYS A NZ  
2355 N N   . SER A 293 ? 0.0832 0.0825 0.1234 0.0076  0.0106  0.0258  292 SER A N   
2356 C CA  . SER A 293 ? 0.0732 0.0727 0.1137 0.0074  0.0092  0.0263  292 SER A CA  
2357 C C   . SER A 293 ? 0.0903 0.0882 0.1276 0.0071  0.0075  0.0249  292 SER A C   
2358 O O   . SER A 293 ? 0.1143 0.1120 0.1504 0.0071  0.0061  0.0252  292 SER A O   
2359 C CB  . SER A 293 ? 0.1342 0.1343 0.1777 0.0073  0.0099  0.0267  292 SER A CB  
2360 O OG  . SER A 293 ? 0.2342 0.2346 0.2784 0.0072  0.0087  0.0274  292 SER A OG  
2361 N N   . LYS A 294 ? 0.0811 0.0780 0.1171 0.0069  0.0076  0.0234  293 LYS A N   
2362 C CA  . LYS A 294 ? 0.0877 0.0833 0.1208 0.0066  0.0060  0.0221  293 LYS A CA  
2363 C C   . LYS A 294 ? 0.0811 0.0758 0.1112 0.0068  0.0051  0.0217  293 LYS A C   
2364 O O   . LYS A 294 ? 0.0874 0.0812 0.1153 0.0068  0.0035  0.0212  293 LYS A O   
2365 C CB  . LYS A 294 ? 0.1109 0.1058 0.1436 0.0063  0.0063  0.0207  293 LYS A CB  
2366 C CG  . LYS A 294 ? 0.1868 0.1818 0.2211 0.0060  0.0059  0.0206  293 LYS A CG  
2367 C CD  . LYS A 294 ? 0.2205 0.2150 0.2545 0.0056  0.0061  0.0193  293 LYS A CD  
2368 C CE  . LYS A 294 ? 0.1925 0.1879 0.2284 0.0057  0.0080  0.0196  293 LYS A CE  
2369 N NZ  . LYS A 294 ? 0.1525 0.1477 0.1885 0.0054  0.0083  0.0185  293 LYS A NZ  
2370 N N   . LEU A 295 ? 0.0871 0.0821 0.1169 0.0070  0.0062  0.0219  294 LEU A N   
2371 C CA  . LEU A 295 ? 0.0968 0.0913 0.1239 0.0073  0.0054  0.0217  294 LEU A CA  
2372 C C   . LEU A 295 ? 0.0846 0.0797 0.1119 0.0076  0.0045  0.0229  294 LEU A C   
2373 O O   . LEU A 295 ? 0.0742 0.0685 0.0990 0.0078  0.0032  0.0225  294 LEU A O   
2374 C CB  . LEU A 295 ? 0.1301 0.1250 0.1574 0.0074  0.0068  0.0219  294 LEU A CB  
2375 C CG  . LEU A 295 ? 0.1698 0.1640 0.1956 0.0073  0.0074  0.0206  294 LEU A CG  
2376 C CD1 . LEU A 295 ? 0.1890 0.1840 0.2155 0.0076  0.0088  0.0213  294 LEU A CD1 
2377 C CD2 . LEU A 295 ? 0.1357 0.1286 0.1580 0.0072  0.0059  0.0194  294 LEU A CD2 
2378 N N   . GLN A 296 ? 0.0930 0.0895 0.1233 0.0077  0.0053  0.0245  295 GLN A N   
2379 C CA  . GLN A 296 ? 0.0859 0.0832 0.1164 0.0079  0.0045  0.0257  295 GLN A CA  
2380 C C   . GLN A 296 ? 0.1015 0.0979 0.1309 0.0079  0.0028  0.0252  295 GLN A C   
2381 O O   . GLN A 296 ? 0.1235 0.1197 0.1511 0.0082  0.0016  0.0254  295 GLN A O   
2382 C CB  . GLN A 296 ? 0.1103 0.1093 0.1444 0.0080  0.0057  0.0275  295 GLN A CB  
2383 C CG  . GLN A 296 ? 0.1759 0.1759 0.2104 0.0083  0.0049  0.0290  295 GLN A CG  
2384 C CD  . GLN A 296 ? 0.2611 0.2614 0.2937 0.0087  0.0046  0.0293  295 GLN A CD  
2385 O OE1 . GLN A 296 ? 0.2714 0.2723 0.3046 0.0088  0.0058  0.0297  295 GLN A OE1 
2386 N NE2 . GLN A 296 ? 0.2772 0.2771 0.3075 0.0089  0.0030  0.0292  295 GLN A NE2 
2387 N N   . ALA A 297 ? 0.1049 0.1008 0.1351 0.0075  0.0027  0.0245  296 ALA A N   
2388 C CA  . ALA A 297 ? 0.0831 0.0782 0.1122 0.0074  0.0011  0.0239  296 ALA A CA  
2389 C C   . ALA A 297 ? 0.0840 0.0775 0.1093 0.0076  -0.0002 0.0223  296 ALA A C   
2390 O O   . ALA A 297 ? 0.0818 0.0747 0.1055 0.0080  -0.0017 0.0221  296 ALA A O   
2391 C CB  . ALA A 297 ? 0.0743 0.0693 0.1052 0.0070  0.0014  0.0234  296 ALA A CB  
2392 N N   . LEU A 298 ? 0.0761 0.0688 0.1000 0.0075  0.0003  0.0212  297 LEU A N   
2393 C CA  . LEU A 298 ? 0.0574 0.0486 0.0778 0.0077  -0.0008 0.0198  297 LEU A CA  
2394 C C   . LEU A 298 ? 0.0719 0.0634 0.0907 0.0083  -0.0014 0.0204  297 LEU A C   
2395 O O   . LEU A 298 ? 0.0837 0.0743 0.1000 0.0088  -0.0028 0.0197  297 LEU A O   
2396 C CB  . LEU A 298 ? 0.0766 0.0673 0.0962 0.0074  0.0001  0.0188  297 LEU A CB  
2397 C CG  . LEU A 298 ? 0.0704 0.0598 0.0864 0.0077  -0.0009 0.0175  297 LEU A CG  
2398 C CD1 . LEU A 298 ? 0.1010 0.0891 0.1151 0.0079  -0.0024 0.0162  297 LEU A CD1 
2399 C CD2 . LEU A 298 ? 0.0927 0.0817 0.1082 0.0074  0.0001  0.0167  297 LEU A CD2 
2400 N N   . LEU A 299 ? 0.0719 0.0647 0.0920 0.0084  -0.0003 0.0217  298 LEU A N   
2401 C CA  . LEU A 299 ? 0.0856 0.0789 0.1044 0.0089  -0.0008 0.0225  298 LEU A CA  
2402 C C   . LEU A 299 ? 0.1065 0.1003 0.1253 0.0093  -0.0021 0.0231  298 LEU A C   
2403 O O   . LEU A 299 ? 0.1055 0.0989 0.1218 0.0099  -0.0033 0.0227  298 LEU A O   
2404 C CB  . LEU A 299 ? 0.0835 0.0784 0.1044 0.0089  0.0007  0.0239  298 LEU A CB  
2405 C CG  . LEU A 299 ? 0.0907 0.0865 0.1105 0.0094  0.0003  0.0248  298 LEU A CG  
2406 C CD1 . LEU A 299 ? 0.1030 0.0978 0.1195 0.0096  -0.0005 0.0236  298 LEU A CD1 
2407 C CD2 . LEU A 299 ? 0.1637 0.1611 0.1859 0.0093  0.0020  0.0263  298 LEU A CD2 
2408 N N   . ASN A 300 ? 0.1058 0.1004 0.1272 0.0091  -0.0018 0.0241  299 ASN A N   
2409 C CA  . ASN A 300 ? 0.1101 0.1051 0.1317 0.0094  -0.0030 0.0248  299 ASN A CA  
2410 C C   . ASN A 300 ? 0.1186 0.1120 0.1375 0.0097  -0.0046 0.0232  299 ASN A C   
2411 O O   . ASN A 300 ? 0.1363 0.1298 0.1537 0.0104  -0.0059 0.0232  299 ASN A O   
2412 C CB  . ASN A 300 ? 0.1322 0.1282 0.1573 0.0090  -0.0023 0.0260  299 ASN A CB  
2413 C CG  . ASN A 300 ? 0.1599 0.1577 0.1877 0.0089  -0.0007 0.0277  299 ASN A CG  
2414 O OD1 . ASN A 300 ? 0.2168 0.2152 0.2439 0.0091  -0.0004 0.0283  299 ASN A OD1 
2415 N ND2 . ASN A 300 ? 0.2251 0.2237 0.2561 0.0085  0.0002  0.0285  299 ASN A ND2 
2416 N N   . ALA A 301 ? 0.0970 0.0891 0.1153 0.0093  -0.0045 0.0218  300 ALA A N   
2417 C CA  . ALA A 301 ? 0.0975 0.0882 0.1135 0.0097  -0.0060 0.0202  300 ALA A CA  
2418 C C   . ALA A 301 ? 0.1240 0.1140 0.1365 0.0105  -0.0067 0.0192  300 ALA A C   
2419 O O   . ALA A 301 ? 0.1178 0.1074 0.1283 0.0112  -0.0080 0.0185  300 ALA A O   
2420 C CB  . ALA A 301 ? 0.1076 0.0973 0.1238 0.0091  -0.0056 0.0189  300 ALA A CB  
2421 N N   . LEU A 302 ? 0.0982 0.0882 0.1102 0.0103  -0.0059 0.0191  301 LEU A N   
2422 C CA  . LEU A 302 ? 0.0885 0.0779 0.0973 0.0110  -0.0066 0.0182  301 LEU A CA  
2423 C C   . LEU A 302 ? 0.1137 0.1043 0.1219 0.0118  -0.0075 0.0192  301 LEU A C   
2424 O O   . LEU A 302 ? 0.1256 0.1158 0.1311 0.0127  -0.0087 0.0182  301 LEU A O   
2425 C CB  . LEU A 302 ? 0.0771 0.0665 0.0859 0.0106  -0.0054 0.0182  301 LEU A CB  
2426 C CG  . LEU A 302 ? 0.0734 0.0617 0.0822 0.0099  -0.0048 0.0170  301 LEU A CG  
2427 C CD1 . LEU A 302 ? 0.0893 0.0781 0.0989 0.0094  -0.0033 0.0175  301 LEU A CD1 
2428 C CD2 . LEU A 302 ? 0.0980 0.0848 0.1036 0.0105  -0.0058 0.0152  301 LEU A CD2 
2429 N N   . LYS A 303 ? 0.1358 0.1279 0.1464 0.0115  -0.0069 0.0210  302 LYS A N   
2430 C CA  . LYS A 303 ? 0.1584 0.1519 0.1687 0.0121  -0.0077 0.0220  302 LYS A CA  
2431 C C   . LYS A 303 ? 0.2060 0.1994 0.2157 0.0127  -0.0091 0.0217  302 LYS A C   
2432 O O   . LYS A 303 ? 0.1765 0.1703 0.1842 0.0136  -0.0104 0.0213  302 LYS A O   
2433 C CB  . LYS A 303 ? 0.1690 0.1644 0.1821 0.0117  -0.0065 0.0242  302 LYS A CB  
2434 C CG  . LYS A 303 ? 0.2043 0.2003 0.2178 0.0114  -0.0052 0.0247  302 LYS A CG  
2435 C CD  . LYS A 303 ? 0.2646 0.2625 0.2813 0.0111  -0.0039 0.0268  302 LYS A CD  
2436 C CE  . LYS A 303 ? 0.3282 0.3268 0.3447 0.0110  -0.0028 0.0272  302 LYS A CE  
2437 N NZ  . LYS A 303 ? 0.3828 0.3837 0.4012 0.0111  -0.0021 0.0293  302 LYS A NZ  
2438 N N   . THR A 304 ? 0.1883 0.1812 0.1997 0.0123  -0.0089 0.0217  303 THR A N   
2439 C CA  . THR A 304 ? 0.1873 0.1801 0.1982 0.0128  -0.0102 0.0212  303 THR A CA  
2440 C C   . THR A 304 ? 0.2268 0.2186 0.2346 0.0137  -0.0113 0.0193  303 THR A C   
2441 O O   . THR A 304 ? 0.2061 0.1985 0.2125 0.0146  -0.0125 0.0190  303 THR A O   
2442 C CB  . THR A 304 ? 0.2342 0.2266 0.2476 0.0119  -0.0097 0.0215  303 THR A CB  
2443 O OG1 . THR A 304 ? 0.2521 0.2458 0.2685 0.0113  -0.0087 0.0233  303 THR A OG1 
2444 C CG2 . THR A 304 ? 0.2595 0.2517 0.2726 0.0123  -0.0110 0.0209  303 THR A CG2 
2445 N N   . ALA A 305 ? 0.1849 0.1754 0.1916 0.0134  -0.0107 0.0180  304 ALA A N   
2446 C CA  . ALA A 305 ? 0.2032 0.1932 0.2073 0.0143  -0.0112 0.0164  304 ALA A CA  
2447 C C   . ALA A 305 ? 0.2183 0.2092 0.2199 0.0155  -0.0119 0.0161  304 ALA A C   
2448 O O   . ALA A 305 ? 0.2734 0.2654 0.2737 0.0162  -0.0118 0.0152  304 ALA A O   
2449 C CB  . ALA A 305 ? 0.2019 0.1908 0.2058 0.0136  -0.0103 0.0154  304 ALA A CB  
2450 N N   . LYS A 306 ? 0.1841 0.1755 0.1860 0.0153  -0.0120 0.0172  305 LYS A N   
2451 C CA  . LYS A 306 ? 0.2019 0.1941 0.2017 0.0163  -0.0131 0.0168  305 LYS A CA  
2452 C C   . LYS A 306 ? 0.2742 0.2679 0.2736 0.0172  -0.0144 0.0169  305 LYS A C   
2453 O O   . LYS A 306 ? 0.3362 0.3310 0.3339 0.0177  -0.0151 0.0158  305 LYS A O   
2454 C CB  . LYS A 306 ? 0.1852 0.1783 0.1861 0.0155  -0.0126 0.0181  305 LYS A CB  
2455 C CG  . LYS A 306 ? 0.2060 0.1997 0.2050 0.0160  -0.0137 0.0177  305 LYS A CG  
2456 C CD  . LYS A 306 ? 0.2269 0.2221 0.2274 0.0152  -0.0124 0.0195  305 LYS A CD  
2457 C CE  . LYS A 306 ? 0.2549 0.2512 0.2540 0.0154  -0.0132 0.0193  305 LYS A CE  
2458 N NZ  . LYS A 306 ? 0.2640 0.2618 0.2643 0.0149  -0.0115 0.0210  305 LYS A NZ  
2459 N N   . SER A 307 ? 0.2431 0.2373 0.2447 0.0168  -0.0144 0.0182  306 SER A N   
2460 C CA  . SER A 307 ? 0.2586 0.2544 0.2602 0.0174  -0.0156 0.0188  306 SER A CA  
2461 C C   . SER A 307 ? 0.2577 0.2538 0.2597 0.0179  -0.0160 0.0185  306 SER A C   
2462 O O   . SER A 307 ? 0.3146 0.3117 0.3177 0.0180  -0.0167 0.0194  306 SER A O   
2463 C CB  . SER A 307 ? 0.2526 0.2495 0.2568 0.0165  -0.0150 0.0211  306 SER A CB  
2464 O OG  . SER A 307 ? 0.2938 0.2899 0.3005 0.0155  -0.0138 0.0218  306 SER A OG  
2465 N N   . ARG A 308 ? 0.2545 0.2502 0.2562 0.0180  -0.0154 0.0174  307 ARG A N   
2466 C CA  . ARG A 308 ? 0.2335 0.2300 0.2363 0.0180  -0.0158 0.0173  307 ARG A CA  
2467 C C   . ARG A 308 ? 0.2882 0.2876 0.2903 0.0186  -0.0162 0.0168  307 ARG A C   
2468 O O   . ARG A 308 ? 0.2803 0.2810 0.2820 0.0183  -0.0156 0.0165  307 ARG A O   
2469 C CB  . ARG A 308 ? 0.2341 0.2290 0.2384 0.0167  -0.0151 0.0166  307 ARG A CB  
2470 C CG  . ARG A 308 ? 0.2258 0.2188 0.2318 0.0155  -0.0143 0.0172  307 ARG A CG  
2471 C CD  . ARG A 308 ? 0.2367 0.2300 0.2445 0.0152  -0.0147 0.0186  307 ARG A CD  
2472 N NE  . ARG A 308 ? 0.2878 0.2820 0.2958 0.0154  -0.0145 0.0199  307 ARG A NE  
2473 C CZ  . ARG A 308 ? 0.3273 0.3226 0.3371 0.0152  -0.0148 0.0215  307 ARG A CZ  
2474 N NH1 . ARG A 308 ? 0.3756 0.3710 0.3869 0.0149  -0.0152 0.0218  307 ARG A NH1 
2475 N NH2 . ARG A 308 ? 0.3343 0.3308 0.3446 0.0151  -0.0145 0.0228  307 ARG A NH2 
2476 N N   . LEU A 309 ? 0.2786 0.2793 0.2812 0.0189  -0.0173 0.0172  308 LEU A N   
2477 C CA  . LEU A 309 ? 0.2910 0.2945 0.2941 0.0187  -0.0180 0.0170  308 LEU A CA  
2478 C C   . LEU A 309 ? 0.2792 0.2806 0.2831 0.0173  -0.0185 0.0155  308 LEU A C   
2479 O O   . LEU A 309 ? 0.3041 0.3058 0.3075 0.0168  -0.0192 0.0143  308 LEU A O   
2480 C CB  . LEU A 309 ? 0.3164 0.3212 0.3198 0.0193  -0.0192 0.0174  308 LEU A CB  
2481 C CG  . LEU A 309 ? 0.3476 0.3532 0.3494 0.0205  -0.0195 0.0178  308 LEU A CG  
2482 C CD1 . LEU A 309 ? 0.3491 0.3551 0.3516 0.0209  -0.0207 0.0184  308 LEU A CD1 
2483 C CD2 . LEU A 309 ? 0.3680 0.3766 0.3684 0.0209  -0.0193 0.0176  308 LEU A CD2 
2484 N N   . GLU A 310 ? 0.2825 0.2813 0.2873 0.0166  -0.0184 0.0149  309 GLU A N   
2485 C CA  . GLU A 310 ? 0.3144 0.3106 0.3193 0.0154  -0.0191 0.0129  309 GLU A CA  
2486 C C   . GLU A 310 ? 0.2769 0.2712 0.2816 0.0147  -0.0181 0.0121  309 GLU A C   
2487 O O   . GLU A 310 ? 0.2310 0.2249 0.2363 0.0147  -0.0168 0.0132  309 GLU A O   
2488 C CB  . GLU A 310 ? 0.4334 0.4282 0.4395 0.0149  -0.0197 0.0127  309 GLU A CB  
2489 C CG  . GLU A 310 ? 0.5463 0.5425 0.5525 0.0154  -0.0211 0.0127  309 GLU A CG  
2490 C CD  . GLU A 310 ? 0.6637 0.6578 0.6694 0.0147  -0.0224 0.0103  309 GLU A CD  
2491 O OE1 . GLU A 310 ? 0.7463 0.7407 0.7523 0.0148  -0.0235 0.0102  309 GLU A OE1 
2492 O OE2 . GLU A 310 ? 0.6925 0.6845 0.6973 0.0140  -0.0224 0.0086  309 GLU A OE2 
2493 N N   . LEU A 311 ? 0.2487 0.2415 0.2523 0.0141  -0.0187 0.0100  310 LEU A N   
2494 C CA  . LEU A 311 ? 0.2415 0.2327 0.2447 0.0133  -0.0178 0.0092  310 LEU A CA  
2495 C C   . LEU A 311 ? 0.2427 0.2322 0.2473 0.0124  -0.0174 0.0091  310 LEU A C   
2496 O O   . LEU A 311 ? 0.2082 0.1973 0.2132 0.0121  -0.0161 0.0096  310 LEU A O   
2497 C CB  . LEU A 311 ? 0.2376 0.2272 0.2390 0.0130  -0.0188 0.0066  310 LEU A CB  
2498 C CG  . LEU A 311 ? 0.2430 0.2310 0.2435 0.0123  -0.0181 0.0053  310 LEU A CG  
2499 C CD1 . LEU A 311 ? 0.2074 0.1969 0.2080 0.0127  -0.0168 0.0068  310 LEU A CD1 
2500 C CD2 . LEU A 311 ? 0.2335 0.2198 0.2318 0.0122  -0.0193 0.0026  310 LEU A CD2 
2501 N N   . HIS A 312 ? 0.2363 0.2249 0.2415 0.0120  -0.0185 0.0084  311 HIS A N   
2502 C CA  . HIS A 312 ? 0.2165 0.2040 0.2234 0.0111  -0.0182 0.0085  311 HIS A CA  
2503 C C   . HIS A 312 ? 0.2064 0.1947 0.2145 0.0114  -0.0167 0.0106  311 HIS A C   
2504 O O   . HIS A 312 ? 0.1907 0.1783 0.1997 0.0107  -0.0158 0.0107  311 HIS A O   
2505 C CB  . HIS A 312 ? 0.2540 0.2410 0.2617 0.0108  -0.0195 0.0080  311 HIS A CB  
2506 C CG  . HIS A 312 ? 0.2192 0.2053 0.2287 0.0099  -0.0192 0.0083  311 HIS A CG  
2507 N ND1 . HIS A 312 ? 0.2675 0.2521 0.2773 0.0087  -0.0197 0.0067  311 HIS A ND1 
2508 C CD2 . HIS A 312 ? 0.2603 0.2471 0.2717 0.0099  -0.0186 0.0100  311 HIS A CD2 
2509 C CE1 . HIS A 312 ? 0.2755 0.2601 0.2872 0.0081  -0.0193 0.0075  311 HIS A CE1 
2510 N NE2 . HIS A 312 ? 0.2522 0.2381 0.2651 0.0087  -0.0186 0.0094  311 HIS A NE2 
2511 N N   . ASP A 313 ? 0.1835 0.1734 0.1917 0.0125  -0.0166 0.0123  312 ASP A N   
2512 C CA  . ASP A 313 ? 0.1918 0.1820 0.2010 0.0127  -0.0155 0.0139  312 ASP A CA  
2513 C C   . ASP A 313 ? 0.1977 0.1876 0.2060 0.0128  -0.0142 0.0142  312 ASP A C   
2514 O O   . ASP A 313 ? 0.1927 0.1819 0.2022 0.0122  -0.0133 0.0148  312 ASP A O   
2515 C CB  . ASP A 313 ? 0.2174 0.2091 0.2265 0.0137  -0.0160 0.0154  312 ASP A CB  
2516 C CG  . ASP A 313 ? 0.2617 0.2535 0.2719 0.0136  -0.0171 0.0154  312 ASP A CG  
2517 O OD1 . ASP A 313 ? 0.2808 0.2714 0.2923 0.0125  -0.0174 0.0147  312 ASP A OD1 
2518 O OD2 . ASP A 313 ? 0.2949 0.2883 0.3047 0.0145  -0.0178 0.0161  312 ASP A OD2 
2519 N N   . ALA A 314 ? 0.1799 0.1707 0.1865 0.0135  -0.0141 0.0139  313 ALA A N   
2520 C CA  . ALA A 314 ? 0.1693 0.1598 0.1750 0.0137  -0.0129 0.0141  313 ALA A CA  
2521 C C   . ALA A 314 ? 0.1788 0.1678 0.1851 0.0125  -0.0123 0.0131  313 ALA A C   
2522 O O   . ALA A 314 ? 0.1578 0.1460 0.1644 0.0121  -0.0113 0.0135  313 ALA A O   
2523 C CB  . ALA A 314 ? 0.1844 0.1764 0.1885 0.0145  -0.0131 0.0139  313 ALA A CB  
2524 N N   . CYS A 315 ? 0.1472 0.1355 0.1535 0.0117  -0.0132 0.0116  314 CYS A N   
2525 C CA  . CYS A 315 ? 0.1157 0.1029 0.1224 0.0106  -0.0128 0.0104  314 CYS A CA  
2526 C C   . CYS A 315 ? 0.1302 0.1168 0.1388 0.0099  -0.0124 0.0109  314 CYS A C   
2527 O O   . CYS A 315 ? 0.1243 0.1104 0.1333 0.0093  -0.0115 0.0108  314 CYS A O   
2528 C CB  . CYS A 315 ? 0.1173 0.1036 0.1233 0.0099  -0.0143 0.0083  314 CYS A CB  
2529 S SG  . CYS A 315 ? 0.1617 0.1483 0.1653 0.0104  -0.0147 0.0072  314 CYS A SG  
2530 N N   . LYS A 316 ? 0.1382 0.1250 0.1480 0.0099  -0.0131 0.0114  315 LYS A N   
2531 C CA  . LYS A 316 ? 0.1350 0.1216 0.1470 0.0091  -0.0127 0.0121  315 LYS A CA  
2532 C C   . LYS A 316 ? 0.1150 0.1019 0.1278 0.0093  -0.0113 0.0134  315 LYS A C   
2533 O O   . LYS A 316 ? 0.1270 0.1137 0.1411 0.0085  -0.0104 0.0135  315 LYS A O   
2534 C CB  . LYS A 316 ? 0.1798 0.1667 0.1930 0.0092  -0.0136 0.0126  315 LYS A CB  
2535 C CG  . LYS A 316 ? 0.2809 0.2678 0.2967 0.0084  -0.0133 0.0132  315 LYS A CG  
2536 C CD  . LYS A 316 ? 0.3611 0.3474 0.3773 0.0074  -0.0135 0.0118  315 LYS A CD  
2537 C CE  . LYS A 316 ? 0.4612 0.4476 0.4800 0.0066  -0.0135 0.0121  315 LYS A CE  
2538 N NZ  . LYS A 316 ? 0.4519 0.4389 0.4726 0.0063  -0.0121 0.0134  315 LYS A NZ  
2539 N N   . ALA A 317 ? 0.1333 0.1207 0.1452 0.0101  -0.0111 0.0144  316 ALA A N   
2540 C CA  . ALA A 317 ? 0.1229 0.1106 0.1358 0.0100  -0.0100 0.0157  316 ALA A CA  
2541 C C   . ALA A 317 ? 0.1245 0.1117 0.1368 0.0096  -0.0090 0.0150  316 ALA A C   
2542 O O   . ALA A 317 ? 0.1701 0.1575 0.1841 0.0089  -0.0079 0.0156  316 ALA A O   
2543 C CB  . ALA A 317 ? 0.1620 0.1505 0.1740 0.0109  -0.0102 0.0167  316 ALA A CB  
2544 N N   . LEU A 318 ? 0.1108 0.0975 0.1208 0.0099  -0.0092 0.0138  317 LEU A N   
2545 C CA  . LEU A 318 ? 0.1059 0.0920 0.1151 0.0096  -0.0083 0.0131  317 LEU A CA  
2546 C C   . LEU A 318 ? 0.0932 0.0789 0.1037 0.0086  -0.0080 0.0123  317 LEU A C   
2547 O O   . LEU A 318 ? 0.0814 0.0670 0.0926 0.0080  -0.0070 0.0124  317 LEU A O   
2548 C CB  . LEU A 318 ? 0.1119 0.0979 0.1186 0.0102  -0.0086 0.0122  317 LEU A CB  
2549 C CG  . LEU A 318 ? 0.1402 0.1268 0.1455 0.0113  -0.0087 0.0130  317 LEU A CG  
2550 C CD1 . LEU A 318 ? 0.1474 0.1348 0.1509 0.0120  -0.0090 0.0123  317 LEU A CD1 
2551 C CD2 . LEU A 318 ? 0.1197 0.1060 0.1251 0.0111  -0.0078 0.0138  317 LEU A CD2 
2552 N N   . ALA A 319 ? 0.0961 0.0817 0.1070 0.0082  -0.0090 0.0115  318 ALA A N   
2553 C CA  . ALA A 319 ? 0.1121 0.0976 0.1243 0.0073  -0.0090 0.0107  318 ALA A CA  
2554 C C   . ALA A 319 ? 0.0947 0.0806 0.1094 0.0068  -0.0082 0.0118  318 ALA A C   
2555 O O   . ALA A 319 ? 0.1041 0.0901 0.1198 0.0062  -0.0076 0.0114  318 ALA A O   
2556 C CB  . ALA A 319 ? 0.1222 0.1075 0.1343 0.0069  -0.0105 0.0096  318 ALA A CB  
2557 N N   . ASP A 320 ? 0.0899 0.0764 0.1059 0.0071  -0.0081 0.0131  319 ASP A N   
2558 C CA  . ASP A 320 ? 0.1043 0.0917 0.1233 0.0066  -0.0071 0.0143  319 ASP A CA  
2559 C C   . ASP A 320 ? 0.0951 0.0827 0.1145 0.0064  -0.0056 0.0145  319 ASP A C   
2560 O O   . ASP A 320 ? 0.0888 0.0772 0.1107 0.0059  -0.0047 0.0150  319 ASP A O   
2561 C CB  . ASP A 320 ? 0.1021 0.0901 0.1224 0.0069  -0.0072 0.0158  319 ASP A CB  
2562 C CG  . ASP A 320 ? 0.1491 0.1371 0.1696 0.0070  -0.0085 0.0157  319 ASP A CG  
2563 O OD1 . ASP A 320 ? 0.1489 0.1365 0.1694 0.0066  -0.0092 0.0146  319 ASP A OD1 
2564 O OD2 . ASP A 320 ? 0.1661 0.1546 0.1870 0.0075  -0.0089 0.0167  319 ASP A OD2 
2565 N N   . HIS A 321 ? 0.0869 0.0740 0.1041 0.0067  -0.0054 0.0141  320 HIS A N   
2566 C CA  . HIS A 321 ? 0.0766 0.0640 0.0942 0.0065  -0.0040 0.0143  320 HIS A CA  
2567 C C   . HIS A 321 ? 0.0657 0.0522 0.0813 0.0064  -0.0040 0.0129  320 HIS A C   
2568 O O   . HIS A 321 ? 0.0886 0.0754 0.1050 0.0060  -0.0029 0.0128  320 HIS A O   
2569 C CB  . HIS A 321 ? 0.0857 0.0735 0.1029 0.0070  -0.0035 0.0153  320 HIS A CB  
2570 C CG  . HIS A 321 ? 0.0897 0.0786 0.1091 0.0071  -0.0035 0.0169  320 HIS A CG  
2571 N ND1 . HIS A 321 ? 0.0856 0.0757 0.1081 0.0068  -0.0021 0.0181  320 HIS A ND1 
2572 C CD2 . HIS A 321 ? 0.0943 0.0833 0.1136 0.0075  -0.0045 0.0174  320 HIS A CD2 
2573 C CE1 . HIS A 321 ? 0.1061 0.0971 0.1302 0.0069  -0.0023 0.0194  320 HIS A CE1 
2574 N NE2 . HIS A 321 ? 0.0865 0.0768 0.1087 0.0073  -0.0038 0.0189  320 HIS A NE2 
2575 N N   . PHE A 322 ? 0.0590 0.0446 0.0721 0.0066  -0.0051 0.0118  321 PHE A N   
2576 C CA  . PHE A 322 ? 0.0828 0.0678 0.0940 0.0065  -0.0051 0.0105  321 PHE A CA  
2577 C C   . PHE A 322 ? 0.0873 0.0724 0.0992 0.0059  -0.0057 0.0095  321 PHE A C   
2578 O O   . PHE A 322 ? 0.0832 0.0680 0.0939 0.0056  -0.0055 0.0085  321 PHE A O   
2579 C CB  . PHE A 322 ? 0.0808 0.0653 0.0893 0.0072  -0.0057 0.0099  321 PHE A CB  
2580 C CG  . PHE A 322 ? 0.0703 0.0546 0.0778 0.0077  -0.0051 0.0106  321 PHE A CG  
2581 C CD1 . PHE A 322 ? 0.0835 0.0677 0.0908 0.0074  -0.0041 0.0105  321 PHE A CD1 
2582 C CD2 . PHE A 322 ? 0.1134 0.0980 0.1204 0.0084  -0.0056 0.0114  321 PHE A CD2 
2583 C CE1 . PHE A 322 ? 0.0787 0.0630 0.0855 0.0077  -0.0036 0.0112  321 PHE A CE1 
2584 C CE2 . PHE A 322 ? 0.1159 0.1006 0.1222 0.0088  -0.0052 0.0121  321 PHE A CE2 
2585 C CZ  . PHE A 322 ? 0.0967 0.0813 0.1031 0.0083  -0.0042 0.0120  321 PHE A CZ  
2586 N N   . GLY A 323 ? 0.0939 0.0793 0.1075 0.0057  -0.0063 0.0098  322 GLY A N   
2587 C CA  . GLY A 323 ? 0.0961 0.0818 0.1107 0.0050  -0.0069 0.0090  322 GLY A CA  
2588 C C   . GLY A 323 ? 0.1138 0.0992 0.1273 0.0049  -0.0085 0.0078  322 GLY A C   
2589 O O   . GLY A 323 ? 0.1077 0.0928 0.1198 0.0053  -0.0092 0.0076  322 GLY A O   
2590 N N   . SER A 324 ? 0.1671 0.1528 0.1815 0.0042  -0.0092 0.0070  323 SER A N   
2591 C CA  . SER A 324 ? 0.1992 0.1848 0.2132 0.0038  -0.0110 0.0058  323 SER A CA  
2592 C C   . SER A 324 ? 0.1704 0.1557 0.1822 0.0037  -0.0120 0.0044  323 SER A C   
2593 O O   . SER A 324 ? 0.1704 0.1554 0.1815 0.0034  -0.0138 0.0032  323 SER A O   
2594 C CB  . SER A 324 ? 0.2484 0.2345 0.2643 0.0031  -0.0116 0.0056  323 SER A CB  
2595 O OG  . SER A 324 ? 0.3224 0.3089 0.3385 0.0029  -0.0107 0.0054  323 SER A OG  
2596 N N   . GLU A 325 ? 0.1279 0.1131 0.1385 0.0039  -0.0110 0.0043  324 GLU A N   
2597 C CA  . GLU A 325 ? 0.1290 0.1139 0.1373 0.0038  -0.0121 0.0030  324 GLU A CA  
2598 C C   . GLU A 325 ? 0.1245 0.1089 0.1315 0.0045  -0.0120 0.0033  324 GLU A C   
2599 O O   . GLU A 325 ? 0.1178 0.1019 0.1228 0.0045  -0.0129 0.0021  324 GLU A O   
2600 C CB  . GLU A 325 ? 0.0935 0.0787 0.1010 0.0036  -0.0113 0.0026  324 GLU A CB  
2601 C CG  . GLU A 325 ? 0.1174 0.1032 0.1261 0.0029  -0.0116 0.0022  324 GLU A CG  
2602 C CD  . GLU A 325 ? 0.1569 0.1430 0.1644 0.0027  -0.0114 0.0015  324 GLU A CD  
2603 O OE1 . GLU A 325 ? 0.1403 0.1261 0.1468 0.0030  -0.0101 0.0019  324 GLU A OE1 
2604 O OE2 . GLU A 325 ? 0.1450 0.1316 0.1526 0.0022  -0.0125 0.0007  324 GLU A OE2 
2605 N N   . PHE A 326 ? 0.1114 0.0959 0.1193 0.0052  -0.0111 0.0048  325 PHE A N   
2606 C CA  . PHE A 326 ? 0.1083 0.0926 0.1149 0.0059  -0.0113 0.0051  325 PHE A CA  
2607 C C   . PHE A 326 ? 0.1075 0.0914 0.1138 0.0058  -0.0131 0.0041  325 PHE A C   
2608 O O   . PHE A 326 ? 0.1503 0.1344 0.1581 0.0056  -0.0136 0.0045  325 PHE A O   
2609 C CB  . PHE A 326 ? 0.1041 0.0887 0.1116 0.0068  -0.0100 0.0071  325 PHE A CB  
2610 C CG  . PHE A 326 ? 0.1058 0.0906 0.1119 0.0077  -0.0099 0.0075  325 PHE A CG  
2611 C CD1 . PHE A 326 ? 0.1228 0.1078 0.1286 0.0081  -0.0111 0.0074  325 PHE A CD1 
2612 C CD2 . PHE A 326 ? 0.1162 0.1011 0.1212 0.0080  -0.0088 0.0078  325 PHE A CD2 
2613 C CE1 . PHE A 326 ? 0.1428 0.1284 0.1473 0.0090  -0.0111 0.0079  325 PHE A CE1 
2614 C CE2 . PHE A 326 ? 0.1251 0.1105 0.1289 0.0089  -0.0088 0.0082  325 PHE A CE2 
2615 C CZ  . PHE A 326 ? 0.1476 0.1335 0.1513 0.0094  -0.0099 0.0083  325 PHE A CZ  
2616 N N   . PRO A 327 ? 0.1216 0.1051 0.1259 0.0060  -0.0143 0.0028  326 PRO A N   
2617 C CA  . PRO A 327 ? 0.1340 0.1167 0.1377 0.0059  -0.0161 0.0015  326 PRO A CA  
2618 C C   . PRO A 327 ? 0.1509 0.1340 0.1555 0.0067  -0.0161 0.0028  326 PRO A C   
2619 O O   . PRO A 327 ? 0.1581 0.1420 0.1626 0.0076  -0.0152 0.0041  326 PRO A O   
2620 C CB  . PRO A 327 ? 0.1645 0.1465 0.1655 0.0060  -0.0170 -0.0003 326 PRO A CB  
2621 C CG  . PRO A 327 ? 0.1606 0.1431 0.1610 0.0065  -0.0156 0.0005  326 PRO A CG  
2622 C CD  . PRO A 327 ? 0.1223 0.1057 0.1247 0.0062  -0.0140 0.0022  326 PRO A CD  
2623 N N   . VAL A 328 ? 0.1662 0.1491 0.1719 0.0063  -0.0171 0.0026  327 VAL A N   
2624 C CA  . VAL A 328 ? 0.1606 0.1438 0.1670 0.0070  -0.0173 0.0037  327 VAL A CA  
2625 C C   . VAL A 328 ? 0.2258 0.2080 0.2312 0.0069  -0.0191 0.0020  327 VAL A C   
2626 O O   . VAL A 328 ? 0.2402 0.2218 0.2464 0.0062  -0.0200 0.0012  327 VAL A O   
2627 C CB  . VAL A 328 ? 0.2065 0.1903 0.2154 0.0068  -0.0165 0.0053  327 VAL A CB  
2628 C CG1 . VAL A 328 ? 0.1995 0.1839 0.2091 0.0076  -0.0168 0.0066  327 VAL A CG1 
2629 C CG2 . VAL A 328 ? 0.2247 0.2092 0.2345 0.0069  -0.0147 0.0067  327 VAL A CG2 
2630 N N   . PRO A 329 ? 0.2641 0.2462 0.2678 0.0078  -0.0196 0.0015  328 PRO A N   
2631 C CA  . PRO A 329 ? 0.2748 0.2558 0.2775 0.0079  -0.0213 -0.0002 328 PRO A CA  
2632 C C   . PRO A 329 ? 0.3340 0.3152 0.3383 0.0079  -0.0218 0.0007  328 PRO A C   
2633 O O   . PRO A 329 ? 0.3092 0.2918 0.3151 0.0083  -0.0209 0.0029  328 PRO A O   
2634 C CB  . PRO A 329 ? 0.2672 0.2486 0.2681 0.0091  -0.0213 -0.0003 328 PRO A CB  
2635 C CG  . PRO A 329 ? 0.2958 0.2781 0.2964 0.0092  -0.0199 0.0006  328 PRO A CG  
2636 C CD  . PRO A 329 ? 0.2570 0.2401 0.2599 0.0088  -0.0187 0.0025  328 PRO A CD  
2637 N N   . GLU A 330 ? 0.4197 0.3996 0.4237 0.0075  -0.0232 -0.0010 329 GLU A N   
2638 C CA  . GLU A 330 ? 0.5119 0.4919 0.5173 0.0076  -0.0239 -0.0003 329 GLU A CA  
2639 C C   . GLU A 330 ? 0.5154 0.4966 0.5203 0.0090  -0.0239 0.0008  329 GLU A C   
2640 O O   . GLU A 330 ? 0.5008 0.4822 0.5040 0.0098  -0.0239 0.0003  329 GLU A O   
2641 C CB  . GLU A 330 ? 0.6112 0.5894 0.6159 0.0070  -0.0255 -0.0026 329 GLU A CB  
2642 C CG  . GLU A 330 ? 0.7057 0.6831 0.7105 0.0057  -0.0258 -0.0039 329 GLU A CG  
2643 C CD  . GLU A 330 ? 0.7897 0.7683 0.7971 0.0049  -0.0250 -0.0022 329 GLU A CD  
2644 O OE1 . GLU A 330 ? 0.8181 0.7976 0.8273 0.0052  -0.0246 -0.0005 329 GLU A OE1 
2645 O OE2 . GLU A 330 ? 0.8340 0.8130 0.8417 0.0041  -0.0246 -0.0025 329 GLU A OE2 
2646 N N   . LYS A 331 ? 0.5555 0.5378 0.5621 0.0092  -0.0240 0.0024  330 LYS A N   
2647 C CA  . LYS A 331 ? 0.5949 0.5787 0.6013 0.0104  -0.0242 0.0036  330 LYS A CA  
2648 C C   . LYS A 331 ? 0.5820 0.5648 0.5873 0.0107  -0.0258 0.0018  330 LYS A C   
2649 O O   . LYS A 331 ? 0.5756 0.5588 0.5792 0.0116  -0.0261 0.0011  330 LYS A O   
2650 C CB  . LYS A 331 ? 0.6462 0.6315 0.6548 0.0105  -0.0237 0.0059  330 LYS A CB  
2651 C CG  . LYS A 331 ? 0.6990 0.6867 0.7076 0.0118  -0.0236 0.0077  330 LYS A CG  
2652 C CD  . LYS A 331 ? 0.7425 0.7318 0.7512 0.0123  -0.0221 0.0095  330 LYS A CD  
2653 C CE  . LYS A 331 ? 0.7741 0.7642 0.7846 0.0124  -0.0213 0.0116  330 LYS A CE  
2654 N NZ  . LYS A 331 ? 0.7846 0.7763 0.7956 0.0131  -0.0221 0.0126  330 LYS A NZ  
# 
