data_9HK5
# 
_entry.id   9HK5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9HK5         pdb_00009hk5 10.2210/pdb9hk5/pdb 
WWPDB D_1292143584 ?            ?                   
# 
_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       2025-05-07 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9HK5 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              karsten.niefind@uni-koeln.de 
_pdbx_contact_author.name_first         Karsten 
_pdbx_contact_author.name_last          Niefind 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0183-6315 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Werner, C.'  1 0000-0001-5263-4994 
'Niefind, K.' 2 0000-0002-0183-6315 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? GE ? ? primary Biol.Chem.   ?      ?    1431-6730 ? ? ?   ? ? ?  
;A CK2 alpha ' mutant indicating why CK2 alpha and CK2 alpha ', the isoforms of the catalytic subunit of human protein kinase CK2, deviate in affinity to CK2 beta.
;
2025 ? 10.1515/hsz-2024-0157     40223482 ? ? 
? ? ? ? ? ? ? UK ? ? 1       'J Mol Biol' JMOBAK 0070 1089-8638 ? ? 407 ? 1 12 
;Structure of the human protein kinase CK2 catalytic subunit CK2alpha' and interaction thermodynamics with the regulatory subunit CK2beta
;
2011 ? 10.1016/j.jmb.2011.01.020 21241709 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Werner, C.'       1  0000-0001-5263-4994 
primary 'Eimermacher, S.'  2  0000-0002-2311-3644 
primary 'Harasimowicz, H.' 3  0009-0007-5720-3078 
primary 'Fischer, D.'      4  ?                   
primary 'Pietsch, M.'      5  0000-0002-8110-2265 
primary 'Niefind, K.'      6  0000-0002-0183-6315 
1       'Bischoff, N.'     7  ?                   
1       'Olsen, B.'        8  ?                   
1       'Raaf, J.'         9  ?                   
1       'Bretner, M.'      10 ?                   
1       'Issinger, O.G.'   11 ?                   
1       'Niefind, K.'      12 ?                   
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 
;Casein kinase II subunit alpha'
;
42907.965 1   2.7.11.1 'P32V, V83I, T101I, C336S' ? ? 
2 non-polymer syn 1,2-ETHANEDIOL                                                          62.068    2   ?        ? ? ? 
3 non-polymer syn '5-[(3-chlorophenyl)amino]benzo[c][2,6]naphthyridine-8-carboxylic acid' 349.770   1   ?        ? ? ? 
4 water       nat water                                                                   18.015    337 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;CK II alpha'
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGSSHHHHHHSQDPMPGPAAGSRARVYAEVNSLRSREYWDYEAHVVSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERV
VVKILKPVKKKKIKREIKILENLRGGTNIIKLIDIVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALD
YCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASM
IFRREPFFHGQDNYDQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLL
RYDHQQRLTAKEAMEHPYFYPVVKEQSQPSADNAVLSSGLTAAR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSQDPMPGPAAGSRARVYAEVNSLRSREYWDYEAHVVSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERV
VVKILKPVKKKKIKREIKILENLRGGTNIIKLIDIVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALD
YCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASM
IFRREPFFHGQDNYDQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLL
RYDHQQRLTAKEAMEHPYFYPVVKEQSQPSADNAVLSSGLTAAR
;
_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 1,2-ETHANEDIOL                                                          EDO 
3 '5-[(3-chlorophenyl)amino]benzo[c][2,6]naphthyridine-8-carboxylic acid' 3NG 
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   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  GLN n 
1 13  ASP n 
1 14  PRO n 
1 15  MET n 
1 16  PRO n 
1 17  GLY n 
1 18  PRO n 
1 19  ALA n 
1 20  ALA n 
1 21  GLY n 
1 22  SER n 
1 23  ARG n 
1 24  ALA n 
1 25  ARG n 
1 26  VAL n 
1 27  TYR n 
1 28  ALA n 
1 29  GLU n 
1 30  VAL n 
1 31  ASN n 
1 32  SER n 
1 33  LEU n 
1 34  ARG n 
1 35  SER n 
1 36  ARG n 
1 37  GLU n 
1 38  TYR n 
1 39  TRP n 
1 40  ASP n 
1 41  TYR n 
1 42  GLU n 
1 43  ALA n 
1 44  HIS n 
1 45  VAL n 
1 46  VAL n 
1 47  SER n 
1 48  TRP n 
1 49  GLY n 
1 50  ASN n 
1 51  GLN n 
1 52  ASP n 
1 53  ASP n 
1 54  TYR n 
1 55  GLN n 
1 56  LEU n 
1 57  VAL n 
1 58  ARG n 
1 59  LYS n 
1 60  LEU n 
1 61  GLY n 
1 62  ARG n 
1 63  GLY n 
1 64  LYS n 
1 65  TYR n 
1 66  SER n 
1 67  GLU n 
1 68  VAL n 
1 69  PHE n 
1 70  GLU n 
1 71  ALA n 
1 72  ILE n 
1 73  ASN n 
1 74  ILE n 
1 75  THR n 
1 76  ASN n 
1 77  ASN n 
1 78  GLU n 
1 79  ARG n 
1 80  VAL n 
1 81  VAL n 
1 82  VAL n 
1 83  LYS n 
1 84  ILE n 
1 85  LEU n 
1 86  LYS n 
1 87  PRO n 
1 88  VAL n 
1 89  LYS n 
1 90  LYS n 
1 91  LYS n 
1 92  LYS n 
1 93  ILE n 
1 94  LYS n 
1 95  ARG n 
1 96  GLU n 
1 97  ILE n 
1 98  LYS n 
1 99  ILE n 
1 100 LEU n 
1 101 GLU n 
1 102 ASN n 
1 103 LEU n 
1 104 ARG n 
1 105 GLY n 
1 106 GLY n 
1 107 THR n 
1 108 ASN n 
1 109 ILE n 
1 110 ILE n 
1 111 LYS n 
1 112 LEU n 
1 113 ILE n 
1 114 ASP n 
1 115 ILE n 
1 116 VAL n 
1 117 LYS n 
1 118 ASP n 
1 119 PRO n 
1 120 VAL n 
1 121 SER n 
1 122 LYS n 
1 123 THR n 
1 124 PRO n 
1 125 ALA n 
1 126 LEU n 
1 127 VAL n 
1 128 PHE n 
1 129 GLU n 
1 130 TYR n 
1 131 ILE n 
1 132 ASN n 
1 133 ASN n 
1 134 THR n 
1 135 ASP n 
1 136 PHE n 
1 137 LYS n 
1 138 GLN n 
1 139 LEU n 
1 140 TYR n 
1 141 GLN n 
1 142 ILE n 
1 143 LEU n 
1 144 THR n 
1 145 ASP n 
1 146 PHE n 
1 147 ASP n 
1 148 ILE n 
1 149 ARG n 
1 150 PHE n 
1 151 TYR n 
1 152 MET n 
1 153 TYR n 
1 154 GLU n 
1 155 LEU n 
1 156 LEU n 
1 157 LYS n 
1 158 ALA n 
1 159 LEU n 
1 160 ASP n 
1 161 TYR n 
1 162 CYS n 
1 163 HIS n 
1 164 SER n 
1 165 LYS n 
1 166 GLY n 
1 167 ILE n 
1 168 MET n 
1 169 HIS n 
1 170 ARG n 
1 171 ASP n 
1 172 VAL n 
1 173 LYS n 
1 174 PRO n 
1 175 HIS n 
1 176 ASN n 
1 177 VAL n 
1 178 MET n 
1 179 ILE n 
1 180 ASP n 
1 181 HIS n 
1 182 GLN n 
1 183 GLN n 
1 184 LYS n 
1 185 LYS n 
1 186 LEU n 
1 187 ARG n 
1 188 LEU n 
1 189 ILE n 
1 190 ASP n 
1 191 TRP n 
1 192 GLY n 
1 193 LEU n 
1 194 ALA n 
1 195 GLU n 
1 196 PHE n 
1 197 TYR n 
1 198 HIS n 
1 199 PRO n 
1 200 ALA n 
1 201 GLN n 
1 202 GLU n 
1 203 TYR n 
1 204 ASN n 
1 205 VAL n 
1 206 ARG n 
1 207 VAL n 
1 208 ALA n 
1 209 SER n 
1 210 ARG n 
1 211 TYR n 
1 212 PHE n 
1 213 LYS n 
1 214 GLY n 
1 215 PRO n 
1 216 GLU n 
1 217 LEU n 
1 218 LEU n 
1 219 VAL n 
1 220 ASP n 
1 221 TYR n 
1 222 GLN n 
1 223 MET n 
1 224 TYR n 
1 225 ASP n 
1 226 TYR n 
1 227 SER n 
1 228 LEU n 
1 229 ASP n 
1 230 MET n 
1 231 TRP n 
1 232 SER n 
1 233 LEU n 
1 234 GLY n 
1 235 CYS n 
1 236 MET n 
1 237 LEU n 
1 238 ALA n 
1 239 SER n 
1 240 MET n 
1 241 ILE n 
1 242 PHE n 
1 243 ARG n 
1 244 ARG n 
1 245 GLU n 
1 246 PRO n 
1 247 PHE n 
1 248 PHE n 
1 249 HIS n 
1 250 GLY n 
1 251 GLN n 
1 252 ASP n 
1 253 ASN n 
1 254 TYR n 
1 255 ASP n 
1 256 GLN n 
1 257 LEU n 
1 258 VAL n 
1 259 ARG n 
1 260 ILE n 
1 261 ALA n 
1 262 LYS n 
1 263 VAL n 
1 264 LEU n 
1 265 GLY n 
1 266 THR n 
1 267 GLU n 
1 268 GLU n 
1 269 LEU n 
1 270 TYR n 
1 271 GLY n 
1 272 TYR n 
1 273 LEU n 
1 274 LYS n 
1 275 LYS n 
1 276 TYR n 
1 277 HIS n 
1 278 ILE n 
1 279 ASP n 
1 280 LEU n 
1 281 ASP n 
1 282 PRO n 
1 283 HIS n 
1 284 PHE n 
1 285 ASN n 
1 286 ASP n 
1 287 ILE n 
1 288 LEU n 
1 289 GLY n 
1 290 GLN n 
1 291 HIS n 
1 292 SER n 
1 293 ARG n 
1 294 LYS n 
1 295 ARG n 
1 296 TRP n 
1 297 GLU n 
1 298 ASN n 
1 299 PHE n 
1 300 ILE n 
1 301 HIS n 
1 302 SER n 
1 303 GLU n 
1 304 ASN n 
1 305 ARG n 
1 306 HIS n 
1 307 LEU n 
1 308 VAL n 
1 309 SER n 
1 310 PRO n 
1 311 GLU n 
1 312 ALA n 
1 313 LEU n 
1 314 ASP n 
1 315 LEU n 
1 316 LEU n 
1 317 ASP n 
1 318 LYS n 
1 319 LEU n 
1 320 LEU n 
1 321 ARG n 
1 322 TYR n 
1 323 ASP n 
1 324 HIS n 
1 325 GLN n 
1 326 GLN n 
1 327 ARG n 
1 328 LEU n 
1 329 THR n 
1 330 ALA n 
1 331 LYS n 
1 332 GLU n 
1 333 ALA n 
1 334 MET n 
1 335 GLU n 
1 336 HIS n 
1 337 PRO n 
1 338 TYR n 
1 339 PHE n 
1 340 TYR n 
1 341 PRO n 
1 342 VAL n 
1 343 VAL n 
1 344 LYS n 
1 345 GLU n 
1 346 GLN n 
1 347 SER n 
1 348 GLN n 
1 349 PRO n 
1 350 SER n 
1 351 ALA n 
1 352 ASP n 
1 353 ASN n 
1 354 ALA n 
1 355 VAL n 
1 356 LEU n 
1 357 SER n 
1 358 SER n 
1 359 GLY n 
1 360 LEU n 
1 361 THR n 
1 362 ALA n 
1 363 ALA n 
1 364 ARG 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                   364 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CSNK2A2, CK2A2' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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 
3NG non-polymer         . '5-[(3-chlorophenyl)amino]benzo[c][2,6]naphthyridine-8-carboxylic acid' ?                 
'C19 H12 Cl N3 O2' 349.770 
ALA 'L-peptide linking' y ALANINE                                                                 ?                 'C3 H7 N O2' 
89.093  
ARG 'L-peptide linking' y ARGININE                                                                ?                 
'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                              ?                 'C4 H8 N2 O3' 
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                         ?                 'C4 H7 N O4' 
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                ?                 'C3 H7 N O2 S' 
121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                                          'ETHYLENE GLYCOL' 'C2 H6 O2' 
62.068  
GLN 'L-peptide linking' y GLUTAMINE                                                               ?                 'C5 H10 N2 O3' 
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                         ?                 'C5 H9 N O4' 
147.129 
GLY 'peptide linking'   y GLYCINE                                                                 ?                 'C2 H5 N O2' 
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                               ?                 
'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                                                                   ?                 'H2 O' 18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                              ?                 'C6 H13 N O2' 
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                 ?                 'C6 H13 N O2' 
131.173 
LYS 'L-peptide linking' y LYSINE                                                                  ?                 
'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                                                              ?                 
'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                           ?                 'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                                 ?                 'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                                  ?                 'C3 H7 N O3' 
105.093 
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   -13 ?   ?   ?   A . n 
A 1 2   GLY 2   -12 ?   ?   ?   A . n 
A 1 3   SER 3   -11 ?   ?   ?   A . n 
A 1 4   SER 4   -10 ?   ?   ?   A . n 
A 1 5   HIS 5   -9  ?   ?   ?   A . n 
A 1 6   HIS 6   -8  ?   ?   ?   A . n 
A 1 7   HIS 7   -7  ?   ?   ?   A . n 
A 1 8   HIS 8   -6  ?   ?   ?   A . n 
A 1 9   HIS 9   -5  ?   ?   ?   A . n 
A 1 10  HIS 10  -4  ?   ?   ?   A . n 
A 1 11  SER 11  -3  ?   ?   ?   A . n 
A 1 12  GLN 12  -2  ?   ?   ?   A . n 
A 1 13  ASP 13  -1  ?   ?   ?   A . n 
A 1 14  PRO 14  0   ?   ?   ?   A . n 
A 1 15  MET 15  1   ?   ?   ?   A . n 
A 1 16  PRO 16  2   ?   ?   ?   A . n 
A 1 17  GLY 17  3   ?   ?   ?   A . n 
A 1 18  PRO 18  4   ?   ?   ?   A . n 
A 1 19  ALA 19  5   ?   ?   ?   A . n 
A 1 20  ALA 20  6   ?   ?   ?   A . n 
A 1 21  GLY 21  7   7   GLY GLY A . n 
A 1 22  SER 22  8   8   SER SER A . n 
A 1 23  ARG 23  9   9   ARG ARG A . n 
A 1 24  ALA 24  10  10  ALA ALA A . n 
A 1 25  ARG 25  11  11  ARG ARG A . n 
A 1 26  VAL 26  12  12  VAL VAL A . n 
A 1 27  TYR 27  13  13  TYR TYR A . n 
A 1 28  ALA 28  14  14  ALA ALA A . n 
A 1 29  GLU 29  15  15  GLU GLU A . n 
A 1 30  VAL 30  16  16  VAL VAL A . n 
A 1 31  ASN 31  17  17  ASN ASN A . n 
A 1 32  SER 32  18  18  SER SER A . n 
A 1 33  LEU 33  19  19  LEU LEU A . n 
A 1 34  ARG 34  20  20  ARG ARG A . n 
A 1 35  SER 35  21  21  SER SER A . n 
A 1 36  ARG 36  22  22  ARG ARG A . n 
A 1 37  GLU 37  23  23  GLU GLU A . n 
A 1 38  TYR 38  24  24  TYR TYR A . n 
A 1 39  TRP 39  25  25  TRP TRP A . n 
A 1 40  ASP 40  26  26  ASP ASP A . n 
A 1 41  TYR 41  27  27  TYR TYR A . n 
A 1 42  GLU 42  28  28  GLU GLU A . n 
A 1 43  ALA 43  29  29  ALA ALA A . n 
A 1 44  HIS 44  30  30  HIS HIS A . n 
A 1 45  VAL 45  31  31  VAL VAL A . n 
A 1 46  VAL 46  32  32  VAL VAL A . n 
A 1 47  SER 47  33  33  SER SER A . n 
A 1 48  TRP 48  34  34  TRP TRP A . n 
A 1 49  GLY 49  35  35  GLY GLY A . n 
A 1 50  ASN 50  36  36  ASN ASN A . n 
A 1 51  GLN 51  37  37  GLN GLN A . n 
A 1 52  ASP 52  38  38  ASP ASP A . n 
A 1 53  ASP 53  39  39  ASP ASP A . n 
A 1 54  TYR 54  40  40  TYR TYR A . n 
A 1 55  GLN 55  41  41  GLN GLN A . n 
A 1 56  LEU 56  42  42  LEU LEU A . n 
A 1 57  VAL 57  43  43  VAL VAL A . n 
A 1 58  ARG 58  44  44  ARG ARG A . n 
A 1 59  LYS 59  45  45  LYS LYS A . n 
A 1 60  LEU 60  46  46  LEU LEU A . n 
A 1 61  GLY 61  47  47  GLY GLY A . n 
A 1 62  ARG 62  48  48  ARG ARG A . n 
A 1 63  GLY 63  49  49  GLY GLY A . n 
A 1 64  LYS 64  50  50  LYS LYS A . n 
A 1 65  TYR 65  51  51  TYR TYR A . n 
A 1 66  SER 66  52  52  SER SER A . n 
A 1 67  GLU 67  53  53  GLU GLU A . n 
A 1 68  VAL 68  54  54  VAL VAL A . n 
A 1 69  PHE 69  55  55  PHE PHE A . n 
A 1 70  GLU 70  56  56  GLU GLU A . n 
A 1 71  ALA 71  57  57  ALA ALA A . n 
A 1 72  ILE 72  58  58  ILE ILE A . n 
A 1 73  ASN 73  59  59  ASN ASN A . n 
A 1 74  ILE 74  60  60  ILE ILE A . n 
A 1 75  THR 75  61  61  THR THR A . n 
A 1 76  ASN 76  62  62  ASN ASN A . n 
A 1 77  ASN 77  63  63  ASN ASN A . n 
A 1 78  GLU 78  64  64  GLU GLU A . n 
A 1 79  ARG 79  65  65  ARG ARG A . n 
A 1 80  VAL 80  66  66  VAL VAL A . n 
A 1 81  VAL 81  67  67  VAL VAL A . n 
A 1 82  VAL 82  68  68  VAL VAL A . n 
A 1 83  LYS 83  69  69  LYS LYS A . n 
A 1 84  ILE 84  70  70  ILE ILE A . n 
A 1 85  LEU 85  71  71  LEU LEU A . n 
A 1 86  LYS 86  72  72  LYS LYS A . n 
A 1 87  PRO 87  73  73  PRO PRO A . n 
A 1 88  VAL 88  74  74  VAL VAL A . n 
A 1 89  LYS 89  75  75  LYS LYS A . n 
A 1 90  LYS 90  76  76  LYS LYS A . n 
A 1 91  LYS 91  77  77  LYS LYS A . n 
A 1 92  LYS 92  78  78  LYS LYS A . n 
A 1 93  ILE 93  79  79  ILE ILE A . n 
A 1 94  LYS 94  80  80  LYS LYS A . n 
A 1 95  ARG 95  81  81  ARG ARG A . n 
A 1 96  GLU 96  82  82  GLU GLU A . n 
A 1 97  ILE 97  83  83  ILE ILE A . n 
A 1 98  LYS 98  84  84  LYS LYS A . n 
A 1 99  ILE 99  85  85  ILE ILE A . n 
A 1 100 LEU 100 86  86  LEU LEU A . n 
A 1 101 GLU 101 87  87  GLU GLU A . n 
A 1 102 ASN 102 88  88  ASN ASN A . n 
A 1 103 LEU 103 89  89  LEU LEU A . n 
A 1 104 ARG 104 90  90  ARG ARG A . n 
A 1 105 GLY 105 91  91  GLY GLY A . n 
A 1 106 GLY 106 92  92  GLY GLY A . n 
A 1 107 THR 107 93  93  THR THR A . n 
A 1 108 ASN 108 94  94  ASN ASN A . n 
A 1 109 ILE 109 95  95  ILE ILE A . n 
A 1 110 ILE 110 96  96  ILE ILE A . n 
A 1 111 LYS 111 97  97  LYS LYS A . n 
A 1 112 LEU 112 98  98  LEU LEU A . n 
A 1 113 ILE 113 99  99  ILE ILE A . n 
A 1 114 ASP 114 100 100 ASP ASP A . n 
A 1 115 ILE 115 101 101 ILE ILE A . n 
A 1 116 VAL 116 102 102 VAL VAL A . n 
A 1 117 LYS 117 103 103 LYS LYS A . n 
A 1 118 ASP 118 104 104 ASP ASP A . n 
A 1 119 PRO 119 105 105 PRO PRO A . n 
A 1 120 VAL 120 106 106 VAL VAL A . n 
A 1 121 SER 121 107 107 SER SER A . n 
A 1 122 LYS 122 108 108 LYS LYS A . n 
A 1 123 THR 123 109 109 THR THR A . n 
A 1 124 PRO 124 110 110 PRO PRO A . n 
A 1 125 ALA 125 111 111 ALA ALA A . n 
A 1 126 LEU 126 112 112 LEU LEU A . n 
A 1 127 VAL 127 113 113 VAL VAL A . n 
A 1 128 PHE 128 114 114 PHE PHE A . n 
A 1 129 GLU 129 115 115 GLU GLU A . n 
A 1 130 TYR 130 116 116 TYR TYR A . n 
A 1 131 ILE 131 117 117 ILE ILE A . n 
A 1 132 ASN 132 118 118 ASN ASN A . n 
A 1 133 ASN 133 119 119 ASN ASN A . n 
A 1 134 THR 134 120 120 THR THR A . n 
A 1 135 ASP 135 121 121 ASP ASP A . n 
A 1 136 PHE 136 122 122 PHE PHE A . n 
A 1 137 LYS 137 123 123 LYS LYS A . n 
A 1 138 GLN 138 124 124 GLN GLN A . n 
A 1 139 LEU 139 125 125 LEU LEU A . n 
A 1 140 TYR 140 126 126 TYR TYR A . n 
A 1 141 GLN 141 127 127 GLN GLN A . n 
A 1 142 ILE 142 128 128 ILE ILE A . n 
A 1 143 LEU 143 129 129 LEU LEU A . n 
A 1 144 THR 144 130 130 THR THR A . n 
A 1 145 ASP 145 131 131 ASP ASP A . n 
A 1 146 PHE 146 132 132 PHE PHE A . n 
A 1 147 ASP 147 133 133 ASP ASP A . n 
A 1 148 ILE 148 134 134 ILE ILE A . n 
A 1 149 ARG 149 135 135 ARG ARG A . n 
A 1 150 PHE 150 136 136 PHE PHE A . n 
A 1 151 TYR 151 137 137 TYR TYR A . n 
A 1 152 MET 152 138 138 MET MET A . n 
A 1 153 TYR 153 139 139 TYR TYR A . n 
A 1 154 GLU 154 140 140 GLU GLU A . n 
A 1 155 LEU 155 141 141 LEU LEU A . n 
A 1 156 LEU 156 142 142 LEU LEU A . n 
A 1 157 LYS 157 143 143 LYS LYS A . n 
A 1 158 ALA 158 144 144 ALA ALA A . n 
A 1 159 LEU 159 145 145 LEU LEU A . n 
A 1 160 ASP 160 146 146 ASP ASP A . n 
A 1 161 TYR 161 147 147 TYR TYR A . n 
A 1 162 CYS 162 148 148 CYS CYS A . n 
A 1 163 HIS 163 149 149 HIS HIS A . n 
A 1 164 SER 164 150 150 SER SER A . n 
A 1 165 LYS 165 151 151 LYS LYS A . n 
A 1 166 GLY 166 152 152 GLY GLY A . n 
A 1 167 ILE 167 153 153 ILE ILE A . n 
A 1 168 MET 168 154 154 MET MET A . n 
A 1 169 HIS 169 155 155 HIS HIS A . n 
A 1 170 ARG 170 156 156 ARG ARG A . n 
A 1 171 ASP 171 157 157 ASP ASP A . n 
A 1 172 VAL 172 158 158 VAL VAL A . n 
A 1 173 LYS 173 159 159 LYS LYS A . n 
A 1 174 PRO 174 160 160 PRO PRO A . n 
A 1 175 HIS 175 161 161 HIS HIS A . n 
A 1 176 ASN 176 162 162 ASN ASN A . n 
A 1 177 VAL 177 163 163 VAL VAL A . n 
A 1 178 MET 178 164 164 MET MET A . n 
A 1 179 ILE 179 165 165 ILE ILE A . n 
A 1 180 ASP 180 166 166 ASP ASP A . n 
A 1 181 HIS 181 167 167 HIS HIS A . n 
A 1 182 GLN 182 168 168 GLN GLN A . n 
A 1 183 GLN 183 169 169 GLN GLN A . n 
A 1 184 LYS 184 170 170 LYS LYS A . n 
A 1 185 LYS 185 171 171 LYS LYS A . n 
A 1 186 LEU 186 172 172 LEU LEU A . n 
A 1 187 ARG 187 173 173 ARG ARG A . n 
A 1 188 LEU 188 174 174 LEU LEU A . n 
A 1 189 ILE 189 175 175 ILE ILE A . n 
A 1 190 ASP 190 176 176 ASP ASP A . n 
A 1 191 TRP 191 177 177 TRP TRP A . n 
A 1 192 GLY 192 178 178 GLY GLY A . n 
A 1 193 LEU 193 179 179 LEU LEU A . n 
A 1 194 ALA 194 180 180 ALA ALA A . n 
A 1 195 GLU 195 181 181 GLU GLU A . n 
A 1 196 PHE 196 182 182 PHE PHE A . n 
A 1 197 TYR 197 183 183 TYR TYR A . n 
A 1 198 HIS 198 184 184 HIS HIS A . n 
A 1 199 PRO 199 185 185 PRO PRO A . n 
A 1 200 ALA 200 186 186 ALA ALA A . n 
A 1 201 GLN 201 187 187 GLN GLN A . n 
A 1 202 GLU 202 188 188 GLU GLU A . n 
A 1 203 TYR 203 189 189 TYR TYR A . n 
A 1 204 ASN 204 190 190 ASN ASN A . n 
A 1 205 VAL 205 191 191 VAL VAL A . n 
A 1 206 ARG 206 192 192 ARG ARG A . n 
A 1 207 VAL 207 193 193 VAL VAL A . n 
A 1 208 ALA 208 194 194 ALA ALA A . n 
A 1 209 SER 209 195 195 SER SER A . n 
A 1 210 ARG 210 196 196 ARG ARG A . n 
A 1 211 TYR 211 197 197 TYR TYR A . n 
A 1 212 PHE 212 198 198 PHE PHE A . n 
A 1 213 LYS 213 199 199 LYS LYS A . n 
A 1 214 GLY 214 200 200 GLY GLY A . n 
A 1 215 PRO 215 201 201 PRO PRO A . n 
A 1 216 GLU 216 202 202 GLU GLU A . n 
A 1 217 LEU 217 203 203 LEU LEU A . n 
A 1 218 LEU 218 204 204 LEU LEU A . n 
A 1 219 VAL 219 205 205 VAL VAL A . n 
A 1 220 ASP 220 206 206 ASP ASP A . n 
A 1 221 TYR 221 207 207 TYR TYR A . n 
A 1 222 GLN 222 208 208 GLN GLN A . n 
A 1 223 MET 223 209 209 MET MET A . n 
A 1 224 TYR 224 210 210 TYR TYR A . n 
A 1 225 ASP 225 211 211 ASP ASP A . n 
A 1 226 TYR 226 212 212 TYR TYR A . n 
A 1 227 SER 227 213 213 SER SER A . n 
A 1 228 LEU 228 214 214 LEU LEU A . n 
A 1 229 ASP 229 215 215 ASP ASP A . n 
A 1 230 MET 230 216 216 MET MET A . n 
A 1 231 TRP 231 217 217 TRP TRP A . n 
A 1 232 SER 232 218 218 SER SER A . n 
A 1 233 LEU 233 219 219 LEU LEU A . n 
A 1 234 GLY 234 220 220 GLY GLY A . n 
A 1 235 CYS 235 221 221 CYS CYS A . n 
A 1 236 MET 236 222 222 MET MET A . n 
A 1 237 LEU 237 223 223 LEU LEU A . n 
A 1 238 ALA 238 224 224 ALA ALA A . n 
A 1 239 SER 239 225 225 SER SER A . n 
A 1 240 MET 240 226 226 MET MET A . n 
A 1 241 ILE 241 227 227 ILE ILE A . n 
A 1 242 PHE 242 228 228 PHE PHE A . n 
A 1 243 ARG 243 229 229 ARG ARG A . n 
A 1 244 ARG 244 230 230 ARG ARG A . n 
A 1 245 GLU 245 231 231 GLU GLU A . n 
A 1 246 PRO 246 232 232 PRO PRO A . n 
A 1 247 PHE 247 233 233 PHE PHE A . n 
A 1 248 PHE 248 234 234 PHE PHE A . n 
A 1 249 HIS 249 235 235 HIS HIS A . n 
A 1 250 GLY 250 236 236 GLY GLY A . n 
A 1 251 GLN 251 237 237 GLN GLN A . n 
A 1 252 ASP 252 238 238 ASP ASP A . n 
A 1 253 ASN 253 239 239 ASN ASN A . n 
A 1 254 TYR 254 240 240 TYR TYR A . n 
A 1 255 ASP 255 241 241 ASP ASP A . n 
A 1 256 GLN 256 242 242 GLN GLN A . n 
A 1 257 LEU 257 243 243 LEU LEU A . n 
A 1 258 VAL 258 244 244 VAL VAL A . n 
A 1 259 ARG 259 245 245 ARG ARG A . n 
A 1 260 ILE 260 246 246 ILE ILE A . n 
A 1 261 ALA 261 247 247 ALA ALA A . n 
A 1 262 LYS 262 248 248 LYS LYS A . n 
A 1 263 VAL 263 249 249 VAL VAL A . n 
A 1 264 LEU 264 250 250 LEU LEU A . n 
A 1 265 GLY 265 251 251 GLY GLY A . n 
A 1 266 THR 266 252 252 THR THR A . n 
A 1 267 GLU 267 253 253 GLU GLU A . n 
A 1 268 GLU 268 254 254 GLU GLU A . n 
A 1 269 LEU 269 255 255 LEU LEU A . n 
A 1 270 TYR 270 256 256 TYR TYR A . n 
A 1 271 GLY 271 257 257 GLY GLY A . n 
A 1 272 TYR 272 258 258 TYR TYR A . n 
A 1 273 LEU 273 259 259 LEU LEU A . n 
A 1 274 LYS 274 260 260 LYS LYS A . n 
A 1 275 LYS 275 261 261 LYS LYS A . n 
A 1 276 TYR 276 262 262 TYR TYR A . n 
A 1 277 HIS 277 263 263 HIS HIS A . n 
A 1 278 ILE 278 264 264 ILE ILE A . n 
A 1 279 ASP 279 265 265 ASP ASP A . n 
A 1 280 LEU 280 266 266 LEU LEU A . n 
A 1 281 ASP 281 267 267 ASP ASP A . n 
A 1 282 PRO 282 268 268 PRO PRO A . n 
A 1 283 HIS 283 269 269 HIS HIS A . n 
A 1 284 PHE 284 270 270 PHE PHE A . n 
A 1 285 ASN 285 271 271 ASN ASN A . n 
A 1 286 ASP 286 272 272 ASP ASP A . n 
A 1 287 ILE 287 273 273 ILE ILE A . n 
A 1 288 LEU 288 274 274 LEU LEU A . n 
A 1 289 GLY 289 275 275 GLY GLY A . n 
A 1 290 GLN 290 276 276 GLN GLN A . n 
A 1 291 HIS 291 277 277 HIS HIS A . n 
A 1 292 SER 292 278 278 SER SER A . n 
A 1 293 ARG 293 279 279 ARG ARG A . n 
A 1 294 LYS 294 280 280 LYS LYS A . n 
A 1 295 ARG 295 281 281 ARG ARG A . n 
A 1 296 TRP 296 282 282 TRP TRP A . n 
A 1 297 GLU 297 283 283 GLU GLU A . n 
A 1 298 ASN 298 284 284 ASN ASN A . n 
A 1 299 PHE 299 285 285 PHE PHE A . n 
A 1 300 ILE 300 286 286 ILE ILE A . n 
A 1 301 HIS 301 287 287 HIS HIS A . n 
A 1 302 SER 302 288 288 SER SER A . n 
A 1 303 GLU 303 289 289 GLU GLU A . n 
A 1 304 ASN 304 290 290 ASN ASN A . n 
A 1 305 ARG 305 291 291 ARG ARG A . n 
A 1 306 HIS 306 292 292 HIS HIS A . n 
A 1 307 LEU 307 293 293 LEU LEU A . n 
A 1 308 VAL 308 294 294 VAL VAL A . n 
A 1 309 SER 309 295 295 SER SER A . n 
A 1 310 PRO 310 296 296 PRO PRO A . n 
A 1 311 GLU 311 297 297 GLU GLU A . n 
A 1 312 ALA 312 298 298 ALA ALA A . n 
A 1 313 LEU 313 299 299 LEU LEU A . n 
A 1 314 ASP 314 300 300 ASP ASP A . n 
A 1 315 LEU 315 301 301 LEU LEU A . n 
A 1 316 LEU 316 302 302 LEU LEU A . n 
A 1 317 ASP 317 303 303 ASP ASP A . n 
A 1 318 LYS 318 304 304 LYS LYS A . n 
A 1 319 LEU 319 305 305 LEU LEU A . n 
A 1 320 LEU 320 306 306 LEU LEU A . n 
A 1 321 ARG 321 307 307 ARG ARG A . n 
A 1 322 TYR 322 308 308 TYR TYR A . n 
A 1 323 ASP 323 309 309 ASP ASP A . n 
A 1 324 HIS 324 310 310 HIS HIS A . n 
A 1 325 GLN 325 311 311 GLN GLN A . n 
A 1 326 GLN 326 312 312 GLN GLN A . n 
A 1 327 ARG 327 313 313 ARG ARG A . n 
A 1 328 LEU 328 314 314 LEU LEU A . n 
A 1 329 THR 329 315 315 THR THR A . n 
A 1 330 ALA 330 316 316 ALA ALA A . n 
A 1 331 LYS 331 317 317 LYS LYS A . n 
A 1 332 GLU 332 318 318 GLU GLU A . n 
A 1 333 ALA 333 319 319 ALA ALA A . n 
A 1 334 MET 334 320 320 MET MET A . n 
A 1 335 GLU 335 321 321 GLU GLU A . n 
A 1 336 HIS 336 322 322 HIS HIS A . n 
A 1 337 PRO 337 323 323 PRO PRO A . n 
A 1 338 TYR 338 324 324 TYR TYR A . n 
A 1 339 PHE 339 325 325 PHE PHE A . n 
A 1 340 TYR 340 326 326 TYR TYR A . n 
A 1 341 PRO 341 327 327 PRO PRO A . n 
A 1 342 VAL 342 328 328 VAL VAL A . n 
A 1 343 VAL 343 329 329 VAL VAL A . n 
A 1 344 LYS 344 330 330 LYS LYS A . n 
A 1 345 GLU 345 331 331 GLU GLU A . n 
A 1 346 GLN 346 332 332 GLN GLN A . n 
A 1 347 SER 347 333 333 SER SER A . n 
A 1 348 GLN 348 334 334 GLN GLN A . n 
A 1 349 PRO 349 335 ?   ?   ?   A . n 
A 1 350 SER 350 336 ?   ?   ?   A . n 
A 1 351 ALA 351 337 ?   ?   ?   A . n 
A 1 352 ASP 352 338 ?   ?   ?   A . n 
A 1 353 ASN 353 339 ?   ?   ?   A . n 
A 1 354 ALA 354 340 ?   ?   ?   A . n 
A 1 355 VAL 355 341 ?   ?   ?   A . n 
A 1 356 LEU 356 342 ?   ?   ?   A . n 
A 1 357 SER 357 343 ?   ?   ?   A . n 
A 1 358 SER 358 344 ?   ?   ?   A . n 
A 1 359 GLY 359 345 ?   ?   ?   A . n 
A 1 360 LEU 360 346 ?   ?   ?   A . n 
A 1 361 THR 361 347 ?   ?   ?   A . n 
A 1 362 ALA 362 348 ?   ?   ?   A . n 
A 1 363 ALA 363 349 ?   ?   ?   A . n 
A 1 364 ARG 364 350 ?   ?   ?   A . n 
# 
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 EDO 1   401 401  EDO EDO A . 
C 3 3NG 1   402 1    3NG 3NG A . 
D 2 EDO 1   403 2    EDO EDO A . 
E 4 HOH 1   501 296  HOH HOH A . 
E 4 HOH 2   502 279  HOH HOH A . 
E 4 HOH 3   503 2054 HOH HOH A . 
E 4 HOH 4   504 714  HOH HOH A . 
E 4 HOH 5   505 58   HOH HOH A . 
E 4 HOH 6   506 1040 HOH HOH A . 
E 4 HOH 7   507 1859 HOH HOH A . 
E 4 HOH 8   508 229  HOH HOH A . 
E 4 HOH 9   509 84   HOH HOH A . 
E 4 HOH 10  510 150  HOH HOH A . 
E 4 HOH 11  511 433  HOH HOH A . 
E 4 HOH 12  512 310  HOH HOH A . 
E 4 HOH 13  513 211  HOH HOH A . 
E 4 HOH 14  514 1064 HOH HOH A . 
E 4 HOH 15  515 341  HOH HOH A . 
E 4 HOH 16  516 716  HOH HOH A . 
E 4 HOH 17  517 1690 HOH HOH A . 
E 4 HOH 18  518 367  HOH HOH A . 
E 4 HOH 19  519 377  HOH HOH A . 
E 4 HOH 20  520 118  HOH HOH A . 
E 4 HOH 21  521 509  HOH HOH A . 
E 4 HOH 22  522 526  HOH HOH A . 
E 4 HOH 23  523 1939 HOH HOH A . 
E 4 HOH 24  524 50   HOH HOH A . 
E 4 HOH 25  525 91   HOH HOH A . 
E 4 HOH 26  526 542  HOH HOH A . 
E 4 HOH 27  527 123  HOH HOH A . 
E 4 HOH 28  528 1892 HOH HOH A . 
E 4 HOH 29  529 1075 HOH HOH A . 
E 4 HOH 30  530 134  HOH HOH A . 
E 4 HOH 31  531 88   HOH HOH A . 
E 4 HOH 32  532 313  HOH HOH A . 
E 4 HOH 33  533 30   HOH HOH A . 
E 4 HOH 34  534 375  HOH HOH A . 
E 4 HOH 35  535 125  HOH HOH A . 
E 4 HOH 36  536 176  HOH HOH A . 
E 4 HOH 37  537 76   HOH HOH A . 
E 4 HOH 38  538 173  HOH HOH A . 
E 4 HOH 39  539 1994 HOH HOH A . 
E 4 HOH 40  540 147  HOH HOH A . 
E 4 HOH 41  541 1527 HOH HOH A . 
E 4 HOH 42  542 144  HOH HOH A . 
E 4 HOH 43  543 143  HOH HOH A . 
E 4 HOH 44  544 163  HOH HOH A . 
E 4 HOH 45  545 269  HOH HOH A . 
E 4 HOH 46  546 105  HOH HOH A . 
E 4 HOH 47  547 319  HOH HOH A . 
E 4 HOH 48  548 2080 HOH HOH A . 
E 4 HOH 49  549 1863 HOH HOH A . 
E 4 HOH 50  550 89   HOH HOH A . 
E 4 HOH 51  551 36   HOH HOH A . 
E 4 HOH 52  552 508  HOH HOH A . 
E 4 HOH 53  553 225  HOH HOH A . 
E 4 HOH 54  554 1062 HOH HOH A . 
E 4 HOH 55  555 161  HOH HOH A . 
E 4 HOH 56  556 79   HOH HOH A . 
E 4 HOH 57  557 142  HOH HOH A . 
E 4 HOH 58  558 101  HOH HOH A . 
E 4 HOH 59  559 62   HOH HOH A . 
E 4 HOH 60  560 115  HOH HOH A . 
E 4 HOH 61  561 167  HOH HOH A . 
E 4 HOH 62  562 442  HOH HOH A . 
E 4 HOH 63  563 175  HOH HOH A . 
E 4 HOH 64  564 120  HOH HOH A . 
E 4 HOH 65  565 72   HOH HOH A . 
E 4 HOH 66  566 1091 HOH HOH A . 
E 4 HOH 67  567 265  HOH HOH A . 
E 4 HOH 68  568 386  HOH HOH A . 
E 4 HOH 69  569 25   HOH HOH A . 
E 4 HOH 70  570 216  HOH HOH A . 
E 4 HOH 71  571 86   HOH HOH A . 
E 4 HOH 72  572 33   HOH HOH A . 
E 4 HOH 73  573 102  HOH HOH A . 
E 4 HOH 74  574 2414 HOH HOH A . 
E 4 HOH 75  575 1827 HOH HOH A . 
E 4 HOH 76  576 325  HOH HOH A . 
E 4 HOH 77  577 235  HOH HOH A . 
E 4 HOH 78  578 106  HOH HOH A . 
E 4 HOH 79  579 2116 HOH HOH A . 
E 4 HOH 80  580 214  HOH HOH A . 
E 4 HOH 81  581 191  HOH HOH A . 
E 4 HOH 82  582 20   HOH HOH A . 
E 4 HOH 83  583 511  HOH HOH A . 
E 4 HOH 84  584 1971 HOH HOH A . 
E 4 HOH 85  585 316  HOH HOH A . 
E 4 HOH 86  586 57   HOH HOH A . 
E 4 HOH 87  587 13   HOH HOH A . 
E 4 HOH 88  588 69   HOH HOH A . 
E 4 HOH 89  589 66   HOH HOH A . 
E 4 HOH 90  590 1947 HOH HOH A . 
E 4 HOH 91  591 3    HOH HOH A . 
E 4 HOH 92  592 42   HOH HOH A . 
E 4 HOH 93  593 198  HOH HOH A . 
E 4 HOH 94  594 81   HOH HOH A . 
E 4 HOH 95  595 505  HOH HOH A . 
E 4 HOH 96  596 49   HOH HOH A . 
E 4 HOH 97  597 571  HOH HOH A . 
E 4 HOH 98  598 51   HOH HOH A . 
E 4 HOH 99  599 199  HOH HOH A . 
E 4 HOH 100 600 1844 HOH HOH A . 
E 4 HOH 101 601 153  HOH HOH A . 
E 4 HOH 102 602 261  HOH HOH A . 
E 4 HOH 103 603 1905 HOH HOH A . 
E 4 HOH 104 604 821  HOH HOH A . 
E 4 HOH 105 605 74   HOH HOH A . 
E 4 HOH 106 606 264  HOH HOH A . 
E 4 HOH 107 607 26   HOH HOH A . 
E 4 HOH 108 608 159  HOH HOH A . 
E 4 HOH 109 609 160  HOH HOH A . 
E 4 HOH 110 610 2320 HOH HOH A . 
E 4 HOH 111 611 93   HOH HOH A . 
E 4 HOH 112 612 236  HOH HOH A . 
E 4 HOH 113 613 380  HOH HOH A . 
E 4 HOH 114 614 133  HOH HOH A . 
E 4 HOH 115 615 1874 HOH HOH A . 
E 4 HOH 116 616 8    HOH HOH A . 
E 4 HOH 117 617 166  HOH HOH A . 
E 4 HOH 118 618 171  HOH HOH A . 
E 4 HOH 119 619 46   HOH HOH A . 
E 4 HOH 120 620 41   HOH HOH A . 
E 4 HOH 121 621 83   HOH HOH A . 
E 4 HOH 122 622 1922 HOH HOH A . 
E 4 HOH 123 623 14   HOH HOH A . 
E 4 HOH 124 624 668  HOH HOH A . 
E 4 HOH 125 625 2037 HOH HOH A . 
E 4 HOH 126 626 416  HOH HOH A . 
E 4 HOH 127 627 891  HOH HOH A . 
E 4 HOH 128 628 121  HOH HOH A . 
E 4 HOH 129 629 112  HOH HOH A . 
E 4 HOH 130 630 249  HOH HOH A . 
E 4 HOH 131 631 1931 HOH HOH A . 
E 4 HOH 132 632 2118 HOH HOH A . 
E 4 HOH 133 633 80   HOH HOH A . 
E 4 HOH 134 634 285  HOH HOH A . 
E 4 HOH 135 635 128  HOH HOH A . 
E 4 HOH 136 636 11   HOH HOH A . 
E 4 HOH 137 637 427  HOH HOH A . 
E 4 HOH 138 638 9    HOH HOH A . 
E 4 HOH 139 639 190  HOH HOH A . 
E 4 HOH 140 640 15   HOH HOH A . 
E 4 HOH 141 641 98   HOH HOH A . 
E 4 HOH 142 642 21   HOH HOH A . 
E 4 HOH 143 643 16   HOH HOH A . 
E 4 HOH 144 644 289  HOH HOH A . 
E 4 HOH 145 645 382  HOH HOH A . 
E 4 HOH 146 646 212  HOH HOH A . 
E 4 HOH 147 647 64   HOH HOH A . 
E 4 HOH 148 648 204  HOH HOH A . 
E 4 HOH 149 649 836  HOH HOH A . 
E 4 HOH 150 650 260  HOH HOH A . 
E 4 HOH 151 651 472  HOH HOH A . 
E 4 HOH 152 652 28   HOH HOH A . 
E 4 HOH 153 653 24   HOH HOH A . 
E 4 HOH 154 654 40   HOH HOH A . 
E 4 HOH 155 655 276  HOH HOH A . 
E 4 HOH 156 656 616  HOH HOH A . 
E 4 HOH 157 657 87   HOH HOH A . 
E 4 HOH 158 658 1846 HOH HOH A . 
E 4 HOH 159 659 90   HOH HOH A . 
E 4 HOH 160 660 1526 HOH HOH A . 
E 4 HOH 161 661 1168 HOH HOH A . 
E 4 HOH 162 662 68   HOH HOH A . 
E 4 HOH 163 663 137  HOH HOH A . 
E 4 HOH 164 664 43   HOH HOH A . 
E 4 HOH 165 665 1852 HOH HOH A . 
E 4 HOH 166 666 185  HOH HOH A . 
E 4 HOH 167 667 1910 HOH HOH A . 
E 4 HOH 168 668 828  HOH HOH A . 
E 4 HOH 169 669 599  HOH HOH A . 
E 4 HOH 170 670 1535 HOH HOH A . 
E 4 HOH 171 671 22   HOH HOH A . 
E 4 HOH 172 672 194  HOH HOH A . 
E 4 HOH 173 673 59   HOH HOH A . 
E 4 HOH 174 674 524  HOH HOH A . 
E 4 HOH 175 675 162  HOH HOH A . 
E 4 HOH 176 676 2112 HOH HOH A . 
E 4 HOH 177 677 2117 HOH HOH A . 
E 4 HOH 178 678 38   HOH HOH A . 
E 4 HOH 179 679 1079 HOH HOH A . 
E 4 HOH 180 680 491  HOH HOH A . 
E 4 HOH 181 681 97   HOH HOH A . 
E 4 HOH 182 682 37   HOH HOH A . 
E 4 HOH 183 683 94   HOH HOH A . 
E 4 HOH 184 684 1015 HOH HOH A . 
E 4 HOH 185 685 1124 HOH HOH A . 
E 4 HOH 186 686 205  HOH HOH A . 
E 4 HOH 187 687 244  HOH HOH A . 
E 4 HOH 188 688 157  HOH HOH A . 
E 4 HOH 189 689 96   HOH HOH A . 
E 4 HOH 190 690 368  HOH HOH A . 
E 4 HOH 191 691 183  HOH HOH A . 
E 4 HOH 192 692 303  HOH HOH A . 
E 4 HOH 193 693 61   HOH HOH A . 
E 4 HOH 194 694 1026 HOH HOH A . 
E 4 HOH 195 695 1900 HOH HOH A . 
E 4 HOH 196 696 140  HOH HOH A . 
E 4 HOH 197 697 1964 HOH HOH A . 
E 4 HOH 198 698 4    HOH HOH A . 
E 4 HOH 199 699 75   HOH HOH A . 
E 4 HOH 200 700 1004 HOH HOH A . 
E 4 HOH 201 701 447  HOH HOH A . 
E 4 HOH 202 702 1854 HOH HOH A . 
E 4 HOH 203 703 1986 HOH HOH A . 
E 4 HOH 204 704 71   HOH HOH A . 
E 4 HOH 205 705 2732 HOH HOH A . 
E 4 HOH 206 706 1936 HOH HOH A . 
E 4 HOH 207 707 1925 HOH HOH A . 
E 4 HOH 208 708 122  HOH HOH A . 
E 4 HOH 209 709 23   HOH HOH A . 
E 4 HOH 210 710 1924 HOH HOH A . 
E 4 HOH 211 711 328  HOH HOH A . 
E 4 HOH 212 712 294  HOH HOH A . 
E 4 HOH 213 713 195  HOH HOH A . 
E 4 HOH 214 714 116  HOH HOH A . 
E 4 HOH 215 715 284  HOH HOH A . 
E 4 HOH 216 716 2254 HOH HOH A . 
E 4 HOH 217 717 720  HOH HOH A . 
E 4 HOH 218 718 148  HOH HOH A . 
E 4 HOH 219 719 56   HOH HOH A . 
E 4 HOH 220 720 362  HOH HOH A . 
E 4 HOH 221 721 271  HOH HOH A . 
E 4 HOH 222 722 207  HOH HOH A . 
E 4 HOH 223 723 135  HOH HOH A . 
E 4 HOH 224 724 241  HOH HOH A . 
E 4 HOH 225 725 2371 HOH HOH A . 
E 4 HOH 226 726 2730 HOH HOH A . 
E 4 HOH 227 727 35   HOH HOH A . 
E 4 HOH 228 728 165  HOH HOH A . 
E 4 HOH 229 729 32   HOH HOH A . 
E 4 HOH 230 730 2232 HOH HOH A . 
E 4 HOH 231 731 85   HOH HOH A . 
E 4 HOH 232 732 131  HOH HOH A . 
E 4 HOH 233 733 286  HOH HOH A . 
E 4 HOH 234 734 139  HOH HOH A . 
E 4 HOH 235 735 2733 HOH HOH A . 
E 4 HOH 236 736 203  HOH HOH A . 
E 4 HOH 237 737 220  HOH HOH A . 
E 4 HOH 238 738 1966 HOH HOH A . 
E 4 HOH 239 739 45   HOH HOH A . 
E 4 HOH 240 740 252  HOH HOH A . 
E 4 HOH 241 741 2172 HOH HOH A . 
E 4 HOH 242 742 52   HOH HOH A . 
E 4 HOH 243 743 2154 HOH HOH A . 
E 4 HOH 244 744 29   HOH HOH A . 
E 4 HOH 245 745 78   HOH HOH A . 
E 4 HOH 246 746 2573 HOH HOH A . 
E 4 HOH 247 747 237  HOH HOH A . 
E 4 HOH 248 748 6    HOH HOH A . 
E 4 HOH 249 749 136  HOH HOH A . 
E 4 HOH 250 750 2145 HOH HOH A . 
E 4 HOH 251 751 411  HOH HOH A . 
E 4 HOH 252 752 1983 HOH HOH A . 
E 4 HOH 253 753 129  HOH HOH A . 
E 4 HOH 254 754 501  HOH HOH A . 
E 4 HOH 255 755 2728 HOH HOH A . 
E 4 HOH 256 756 67   HOH HOH A . 
E 4 HOH 257 757 103  HOH HOH A . 
E 4 HOH 258 758 48   HOH HOH A . 
E 4 HOH 259 759 2650 HOH HOH A . 
E 4 HOH 260 760 53   HOH HOH A . 
E 4 HOH 261 761 297  HOH HOH A . 
E 4 HOH 262 762 233  HOH HOH A . 
E 4 HOH 263 763 31   HOH HOH A . 
E 4 HOH 264 764 2610 HOH HOH A . 
E 4 HOH 265 765 299  HOH HOH A . 
E 4 HOH 266 766 19   HOH HOH A . 
E 4 HOH 267 767 374  HOH HOH A . 
E 4 HOH 268 768 1580 HOH HOH A . 
E 4 HOH 269 769 2156 HOH HOH A . 
E 4 HOH 270 770 34   HOH HOH A . 
E 4 HOH 271 771 381  HOH HOH A . 
E 4 HOH 272 772 2661 HOH HOH A . 
E 4 HOH 273 773 435  HOH HOH A . 
E 4 HOH 274 774 2735 HOH HOH A . 
E 4 HOH 275 775 798  HOH HOH A . 
E 4 HOH 276 776 1904 HOH HOH A . 
E 4 HOH 277 777 2103 HOH HOH A . 
E 4 HOH 278 778 1896 HOH HOH A . 
E 4 HOH 279 779 1401 HOH HOH A . 
E 4 HOH 280 780 2731 HOH HOH A . 
E 4 HOH 281 781 454  HOH HOH A . 
E 4 HOH 282 782 780  HOH HOH A . 
E 4 HOH 283 783 315  HOH HOH A . 
E 4 HOH 284 784 1582 HOH HOH A . 
E 4 HOH 285 785 686  HOH HOH A . 
E 4 HOH 286 786 179  HOH HOH A . 
E 4 HOH 287 787 1510 HOH HOH A . 
E 4 HOH 288 788 1937 HOH HOH A . 
E 4 HOH 289 789 1871 HOH HOH A . 
E 4 HOH 290 790 1926 HOH HOH A . 
E 4 HOH 291 791 2676 HOH HOH A . 
E 4 HOH 292 792 590  HOH HOH A . 
E 4 HOH 293 793 681  HOH HOH A . 
E 4 HOH 294 794 55   HOH HOH A . 
E 4 HOH 295 795 1036 HOH HOH A . 
E 4 HOH 296 796 1869 HOH HOH A . 
E 4 HOH 297 797 317  HOH HOH A . 
E 4 HOH 298 798 518  HOH HOH A . 
E 4 HOH 299 799 274  HOH HOH A . 
E 4 HOH 300 800 1890 HOH HOH A . 
E 4 HOH 301 801 460  HOH HOH A . 
E 4 HOH 302 802 1938 HOH HOH A . 
E 4 HOH 303 803 1911 HOH HOH A . 
E 4 HOH 304 804 27   HOH HOH A . 
E 4 HOH 305 805 351  HOH HOH A . 
E 4 HOH 306 806 282  HOH HOH A . 
E 4 HOH 307 807 520  HOH HOH A . 
E 4 HOH 308 808 1894 HOH HOH A . 
E 4 HOH 309 809 841  HOH HOH A . 
E 4 HOH 310 810 765  HOH HOH A . 
E 4 HOH 311 811 2204 HOH HOH A . 
E 4 HOH 312 812 777  HOH HOH A . 
E 4 HOH 313 813 192  HOH HOH A . 
E 4 HOH 314 814 1647 HOH HOH A . 
E 4 HOH 315 815 292  HOH HOH A . 
E 4 HOH 316 816 2355 HOH HOH A . 
E 4 HOH 317 817 1979 HOH HOH A . 
E 4 HOH 318 818 141  HOH HOH A . 
E 4 HOH 319 819 2729 HOH HOH A . 
E 4 HOH 320 820 1566 HOH HOH A . 
E 4 HOH 321 821 329  HOH HOH A . 
E 4 HOH 322 822 476  HOH HOH A . 
E 4 HOH 323 823 70   HOH HOH A . 
E 4 HOH 324 824 2703 HOH HOH A . 
E 4 HOH 325 825 1273 HOH HOH A . 
E 4 HOH 326 826 576  HOH HOH A . 
E 4 HOH 327 827 450  HOH HOH A . 
E 4 HOH 328 828 452  HOH HOH A . 
E 4 HOH 329 829 470  HOH HOH A . 
E 4 HOH 330 830 436  HOH HOH A . 
E 4 HOH 331 831 2657 HOH HOH A . 
E 4 HOH 332 832 2734 HOH HOH A . 
E 4 HOH 333 833 488  HOH HOH A . 
E 4 HOH 334 834 1891 HOH HOH A . 
E 4 HOH 335 835 1164 HOH HOH A . 
E 4 HOH 336 836 1258 HOH HOH A . 
E 4 HOH 337 837 168  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .         1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .         2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .         3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21_5207 4 
# 
_cell.angle_alpha                  111.757 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.221 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  91.546 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HK5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.788 
_cell.length_a_esd                 ? 
_cell.length_b                     47.804 
_cell.length_b_esd                 ? 
_cell.length_c                     50.579 
_cell.length_c_esd                 ? 
_cell.volume                       105019.019 
_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                         9HK5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            'P 1' 
_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                   9HK5 
_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             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.75 
_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              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;protein stock solution: 5 mg/ml protein, 500 mM NaCl, 25 mM Tris/HCl, pH 8.5;
protein/inhibitor mixture: 19 mikroliter protein stock solution plus 1 mikroliter 20 mM CX-4945 in DMSO;
reservoir: 900 mM LiCL, 28 % (w/v) PEG 6000, 250 mM Tris/HCl, pH 8.5; crystallization drop: 2 mikroliter reservoir + 4 mikroliter protein/inhibitor mixture; initial crystals were optimized by micro seeding
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2024-11-28 
_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   0.873128 
_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                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.873128 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          9.63 
_reflns.entry_id                                       9HK5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.491 
_reflns.d_resolution_low                               46.971 
_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                                     44234 
_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                           88.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.129 
_reflns.pdbx_Rpim_I_all                                0.076 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.992 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.104 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.104 
_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                                    1.491 
_reflns_shell.d_res_low                                     1.672 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2189 
_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                               3.0 
_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                               0.944 
_reflns_shell.pdbx_Rpim_I_all                               0.533 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.447 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          11.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.775 
_reflns_shell.pdbx_Rsym_value                               0.775 
_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                               16.80 
_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                                 9HK5 
_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                            1.491 
_refine.ls_d_res_low                             46.97 
_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                     44234 
_refine.ls_number_reflns_R_free                  1091 
_refine.ls_number_reflns_R_work                  43143 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    66.72 
_refine.ls_percent_reflns_R_free                 2.47 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1748 
_refine.ls_R_factor_R_free                       0.2038 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1741 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.96 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 23.1756 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.1324 
_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                       1.491 
_refine_hist.d_res_low                        46.97 
_refine_hist.number_atoms_solvent             337 
_refine_hist.number_atoms_total               3140 
_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        2770 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0063  ? 2909 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7935  ? 3928 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0856  ? 403  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0077  ? 502  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.3186 ? 1102 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.491 1.56  . . 3   100  1.25  . . . . 0.2077 . . . . . . . . . . . 0.3892 
'X-RAY DIFFRACTION' 1.56  1.64  . . 26  1159 14.33 . . . . 0.2453 . . . . . . . . . . . 0.2515 
'X-RAY DIFFRACTION' 1.64  1.74  . . 103 3873 47.92 . . . . 0.2487 . . . . . . . . . . . 0.2820 
'X-RAY DIFFRACTION' 1.74  1.88  . . 171 6477 80.26 . . . . 0.2241 . . . . . . . . . . . 0.2440 
'X-RAY DIFFRACTION' 1.88  2.07  . . 195 7648 95.11 . . . . 0.1991 . . . . . . . . . . . 0.2375 
'X-RAY DIFFRACTION' 2.07  2.37  . . 200 7936 97.69 . . . . 0.1746 . . . . . . . . . . . 0.2113 
'X-RAY DIFFRACTION' 2.37  2.98  . . 193 7964 98.38 . . . . 0.1714 . . . . . . . . . . . 0.2000 
'X-RAY DIFFRACTION' 2.98  46.97 . . 200 7986 98.83 . . . . 0.1419 . . . . . . . . . . . 0.1640 
# 
_struct.entry_id                     9HK5 
_struct.title                        
;Structure of a mutant of human protein kinase CK2alpha' that equals its isoenzyme CK2alpha in affinity to the regulatory subunit CK2beta
;
_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        9HK5 
_struct_keywords.text            
;human protein kinase CK2 human casein kinase 2 isoenzymes CK2alpha and CK2alpha' CK2alpha/CK2beta interaction, TRANSFERASE
;
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 2 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CSK22_HUMAN 
_struct_ref.pdbx_db_accession          P19784 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIK
REVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKP
HNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRREPFFHGQDNY
DQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAM
EHPYFYPVVKEQSQPCADNAVLSSGLTAAR
;
_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              9HK5 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 15 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 364 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P19784 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  350 
_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       350 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9HK5 MET A 1   ? UNP P19784 ?   ?   'initiating methionine' -13 1  
1 9HK5 GLY A 2   ? UNP P19784 ?   ?   'expression tag'        -12 2  
1 9HK5 SER A 3   ? UNP P19784 ?   ?   'expression tag'        -11 3  
1 9HK5 SER A 4   ? UNP P19784 ?   ?   'expression tag'        -10 4  
1 9HK5 HIS A 5   ? UNP P19784 ?   ?   'expression tag'        -9  5  
1 9HK5 HIS A 6   ? UNP P19784 ?   ?   'expression tag'        -8  6  
1 9HK5 HIS A 7   ? UNP P19784 ?   ?   'expression tag'        -7  7  
1 9HK5 HIS A 8   ? UNP P19784 ?   ?   'expression tag'        -6  8  
1 9HK5 HIS A 9   ? UNP P19784 ?   ?   'expression tag'        -5  9  
1 9HK5 HIS A 10  ? UNP P19784 ?   ?   'expression tag'        -4  10 
1 9HK5 SER A 11  ? UNP P19784 ?   ?   'expression tag'        -3  11 
1 9HK5 GLN A 12  ? UNP P19784 ?   ?   'expression tag'        -2  12 
1 9HK5 ASP A 13  ? UNP P19784 ?   ?   'expression tag'        -1  13 
1 9HK5 PRO A 14  ? UNP P19784 ?   ?   'expression tag'        0   14 
1 9HK5 VAL A 46  ? UNP P19784 PRO 32  'engineered mutation'   32  15 
1 9HK5 ILE A 97  ? UNP P19784 VAL 83  'engineered mutation'   83  16 
1 9HK5 ILE A 115 ? UNP P19784 THR 101 'engineered mutation'   101 17 
1 9HK5 SER A 350 ? UNP P19784 CYS 336 'engineered mutation'   336 18 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 220   ? 
1 MORE         3     ? 
1 'SSA (A^2)'  15730 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 35  ? ASP A 40  ? SER A 21  ASP A 26  1 ? 6  
HELX_P HELX_P2  AA2 TYR A 41  ? HIS A 44  ? TYR A 27  HIS A 30  5 ? 4  
HELX_P HELX_P3  AA3 ASN A 50  ? ASP A 52  ? ASN A 36  ASP A 38  5 ? 3  
HELX_P HELX_P4  AA4 LYS A 89  ? LEU A 103 ? LYS A 75  LEU A 89  1 ? 15 
HELX_P HELX_P5  AA5 ASP A 135 ? TYR A 140 ? ASP A 121 TYR A 126 1 ? 6  
HELX_P HELX_P6  AA6 THR A 144 ? LYS A 165 ? THR A 130 LYS A 151 1 ? 22 
HELX_P HELX_P7  AA7 LYS A 173 ? HIS A 175 ? LYS A 159 HIS A 161 5 ? 3  
HELX_P HELX_P8  AA8 SER A 209 ? LYS A 213 ? SER A 195 LYS A 199 5 ? 5  
HELX_P HELX_P9  AA9 GLY A 214 ? VAL A 219 ? GLY A 200 VAL A 205 1 ? 6  
HELX_P HELX_P10 AB1 TYR A 226 ? ARG A 243 ? TYR A 212 ARG A 229 1 ? 18 
HELX_P HELX_P11 AB2 ASP A 252 ? GLY A 265 ? ASP A 238 GLY A 251 1 ? 14 
HELX_P HELX_P12 AB3 GLY A 265 ? HIS A 277 ? GLY A 251 HIS A 263 1 ? 13 
HELX_P HELX_P13 AB4 ASP A 281 ? ILE A 287 ? ASP A 267 ILE A 273 5 ? 7  
HELX_P HELX_P14 AB5 ARG A 295 ? ILE A 300 ? ARG A 281 ILE A 286 5 ? 6  
HELX_P HELX_P15 AB6 ASN A 304 ? VAL A 308 ? ASN A 290 VAL A 294 5 ? 5  
HELX_P HELX_P16 AB7 SER A 309 ? LEU A 320 ? SER A 295 LEU A 306 1 ? 12 
HELX_P HELX_P17 AB8 ASP A 323 ? ARG A 327 ? ASP A 309 ARG A 313 5 ? 5  
HELX_P HELX_P18 AB9 THR A 329 ? GLU A 335 ? THR A 315 GLU A 321 1 ? 7  
HELX_P HELX_P19 AC1 HIS A 336 ? TYR A 338 ? HIS A 322 TYR A 324 5 ? 3  
HELX_P HELX_P20 AC2 PHE A 339 ? GLN A 346 ? PHE A 325 GLN A 332 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LYS 86  A . ? LYS 72  A PRO 87  A ? PRO 73  A 1 4.94  
2 GLU 245 A . ? GLU 231 A PRO 246 A ? PRO 232 A 1 -7.20 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 54  ? ARG A 62  ? TYR A 40  ARG A 48  
AA1 2 SER A 66  ? ASN A 73  ? SER A 52  ASN A 59  
AA1 3 ARG A 79  ? LEU A 85  ? ARG A 65  LEU A 71  
AA1 4 PRO A 124 ? GLU A 129 ? PRO A 110 GLU A 115 
AA1 5 LEU A 112 ? LYS A 117 ? LEU A 98  LYS A 103 
AA2 1 ILE A 167 ? MET A 168 ? ILE A 153 MET A 154 
AA2 2 GLU A 195 ? PHE A 196 ? GLU A 181 PHE A 182 
AA3 1 VAL A 177 ? ASP A 180 ? VAL A 163 ASP A 166 
AA3 2 LYS A 185 ? LEU A 188 ? LYS A 171 LEU A 174 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 57  ? N VAL A 43  O GLU A 70  ? O GLU A 56  
AA1 2 3 N PHE A 69  ? N PHE A 55  O VAL A 82  ? O VAL A 68  
AA1 3 4 N LYS A 83  ? N LYS A 69  O LEU A 126 ? O LEU A 112 
AA1 4 5 O ALA A 125 ? O ALA A 111 N VAL A 116 ? N VAL A 102 
AA2 1 2 N MET A 168 ? N MET A 154 O GLU A 195 ? O GLU A 181 
AA3 1 2 N ASP A 180 ? N ASP A 166 O LYS A 185 ? O LYS A 171 
# 
_pdbx_entry_details.entry_id                   9HK5 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 72  ? ? -172.14 119.35 
2 1 ASP A 157 ? ? -144.09 40.86  
3 1 ASP A 176 ? ? 53.64   80.01  
4 1 ALA A 194 ? ? 62.78   157.39 
5 1 MET A 209 ? ? -93.41  53.66  
6 1 HIS A 235 ? ? -108.19 74.42  
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 62.9091190014 41.55687347   0.232137754921 0.0719121683975  ? -0.00168432141769  ? 
0.00725932927691   ? 0.071570845358   ? 0.000934331468872 ? 0.128442621801    ? 0.115648712012 ? 0.0897952463832  ? 
-0.0561174130298 ? 0.0690140956982 ? -0.0312746125717 ? 0.171858161667 ? -0.0279033848547 ? 0.0205905244722   ? -0.0736260239821 ? 
-0.0282002862662  ? 0.042155431669   ? 0.0472670161258 ? 0.0376358593816  ? -0.0138662438093 ? 0.00677361233069 ? 
2 'X-RAY DIFFRACTION' ? refined 50.326419236  25.0957923716 8.54775330715  0.0967492670151  ? -0.000692094590455 ? 
-0.00720033688269  ? 0.0466184610976  ? 0.00254790310096  ? 0.0488214124504   ? 0.638640868302 ? 0.167917967768   ? 
-0.370746247475  ? 0.623782973398  ? -0.504452784424  ? 0.51745319991  ? -0.0082724894982 ? 0.082190592873    ? 0.0544300486203  ? 
-0.0030107919691  ? 0.085756051099   ? 0.0752903534403 ? 0.117183927427   ? -0.0651429750128 ? 0.0827940174146  ? 
3 'X-RAY DIFFRACTION' ? refined 45.5434799059 38.4273664759 11.7591751835  0.0466907182812  ? 0.000523061879707  ? 
-0.00763468334634  ? 0.0300266040905  ? -0.00523857210793 ? 0.0460657604522   ? 0.452163829225 ? -0.233151056453  ? 
-0.100944096842  ? 0.410301628546  ? 0.0589481599603  ? 0.308970499856 ? -0.039165593013  ? 0.00507596926413  ? -0.0834648536519 ? 
0.080790438976    ? 0.0177278742515  ? 0.0510081257447 ? 0.12487789881    ? -0.0355040860887 ? -0.0164163007543 ? 
4 'X-RAY DIFFRACTION' ? refined 44.8218208273 43.5164893929 0.351796585968 0.032999460541   ? -0.00678797035019  ? 
0.00158283941299   ? 0.0354936699042  ? 0.0045323087201   ? 0.0304261180005   ? 0.261317056849 ? -0.0663871596277 ? 0.116044653273 
? 0.201205191159  ? 0.0106605363879  ? 0.143042068109 ? -0.0159136397255 ? 0.0158473634403   ? -0.0267891942988 ? 
-0.00356298131606 ? 0.00712197867545 ? 0.013263336085  ? 0.0270152961524  ? 0.00545537580182 ? -0.187582489076  ? 
5 'X-RAY DIFFRACTION' ? refined 32.2524089443 53.2380409648 -7.23382168403 0.00287022297186 ? -0.00735645398088  ? 
-0.00499301301704  ? 0.0842061763138  ? 0.0287316804172   ? -0.00278766036204 ? 0.452915606867 ? -0.0129349947508 ? 
-0.250892717499  ? 0.472785442674  ? 0.0477802369014  ? 0.227394856115 ? 0.0758935259184  ? 0.329953346045    ? 0.0928569915756  ? 
-0.227644744218   ? -0.0552616626267 ? 0.180507952416  ? -0.0720317820191 ? -0.267933623137  ? -0.28760008391   ? 
6 'X-RAY DIFFRACTION' ? refined 43.6856473659 57.7304670958 8.26535397727  0.0628779906839  ? -0.0186573150597   ? 
-0.000731155349181 ? 0.00760838894145 ? -0.00445320949245 ? 0.0481305568529   ? 0.301961671107 ? 0.0840816858529  ? 
-0.0100869851656 ? 0.517085905281  ? 0.0349365422307  ? 0.15873900773  ? 0.0526527569467  ? -0.00112931807859 ? 0.134769310315   ? 
0.130178313162    ? 0.0134489236898  ? -0.141442770577 ? -0.084138155263  ? 0.0117182721183  ? 0.0246512300114  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 7   ? A 30  A 36  ? ? 
;chain 'A' and (resid 7 through 36 )
;
2 'X-RAY DIFFRACTION' 2 A 31  A 37  ? A 82  A 88  ? ? 
;chain 'A' and (resid 37 through 88 )
;
3 'X-RAY DIFFRACTION' 3 A 83  A 89  ? A 144 A 150 ? ? 
;chain 'A' and (resid 89 through 150 )
;
4 'X-RAY DIFFRACTION' 4 A 145 A 151 ? A 222 A 228 ? ? 
;chain 'A' and (resid 151 through 228 )
;
5 'X-RAY DIFFRACTION' 5 A 223 A 229 ? A 299 A 305 ? ? 
;chain 'A' and (resid 229 through 305 )
;
6 'X-RAY DIFFRACTION' 6 A 300 A 306 ? A 328 A 334 ? ? 
;chain 'A' and (resid 306 through 334 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 836 ? 5.90 . 
2 1 O ? A HOH 837 ? 6.12 . 
# 
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 MET -13 ? A MET 1   
2  1 Y 1 A GLY -12 ? A GLY 2   
3  1 Y 1 A SER -11 ? A SER 3   
4  1 Y 1 A SER -10 ? A SER 4   
5  1 Y 1 A HIS -9  ? A HIS 5   
6  1 Y 1 A HIS -8  ? A HIS 6   
7  1 Y 1 A HIS -7  ? A HIS 7   
8  1 Y 1 A HIS -6  ? A HIS 8   
9  1 Y 1 A HIS -5  ? A HIS 9   
10 1 Y 1 A HIS -4  ? A HIS 10  
11 1 Y 1 A SER -3  ? A SER 11  
12 1 Y 1 A GLN -2  ? A GLN 12  
13 1 Y 1 A ASP -1  ? A ASP 13  
14 1 Y 1 A PRO 0   ? A PRO 14  
15 1 Y 1 A MET 1   ? A MET 15  
16 1 Y 1 A PRO 2   ? A PRO 16  
17 1 Y 1 A GLY 3   ? A GLY 17  
18 1 Y 1 A PRO 4   ? A PRO 18  
19 1 Y 1 A ALA 5   ? A ALA 19  
20 1 Y 1 A ALA 6   ? A ALA 20  
21 1 Y 1 A PRO 335 ? A PRO 349 
22 1 Y 1 A SER 336 ? A SER 350 
23 1 Y 1 A ALA 337 ? A ALA 351 
24 1 Y 1 A ASP 338 ? A ASP 352 
25 1 Y 1 A ASN 339 ? A ASN 353 
26 1 Y 1 A ALA 340 ? A ALA 354 
27 1 Y 1 A VAL 341 ? A VAL 355 
28 1 Y 1 A LEU 342 ? A LEU 356 
29 1 Y 1 A SER 343 ? A SER 357 
30 1 Y 1 A SER 344 ? A SER 358 
31 1 Y 1 A GLY 345 ? A GLY 359 
32 1 Y 1 A LEU 346 ? A LEU 360 
33 1 Y 1 A THR 347 ? A THR 361 
34 1 Y 1 A ALA 348 ? A ALA 362 
35 1 Y 1 A ALA 349 ? A ALA 363 
36 1 Y 1 A ARG 350 ? A ARG 364 
# 
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 
3NG C1   C  Y N 1   
3NG C2   C  Y N 2   
3NG C3   C  Y N 3   
3NG C4   C  Y N 4   
3NG C5   C  Y N 5   
3NG C6   C  Y N 6   
3NG C7   C  Y N 7   
3NG C8   C  Y N 8   
3NG N9   N  Y N 9   
3NG C10  C  Y N 10  
3NG C11  C  Y N 11  
3NG N12  N  Y N 12  
3NG C13  C  Y N 13  
3NG C14  C  Y N 14  
3NG N15  N  N N 15  
3NG C16  C  Y N 16  
3NG C17  C  Y N 17  
3NG C18  C  Y N 18  
3NG C19  C  Y N 19  
3NG C20  C  Y N 20  
3NG C21  C  Y N 21  
3NG CL22 CL N N 22  
3NG C23  C  N N 23  
3NG O24  O  N N 24  
3NG O25  O  N N 25  
3NG H3   H  N N 26  
3NG H4   H  N N 27  
3NG H6   H  N N 28  
3NG H11  H  N N 29  
3NG H13  H  N N 30  
3NG H14  H  N N 31  
3NG HN15 H  N N 32  
3NG H17  H  N N 33  
3NG H19  H  N N 34  
3NG H20  H  N N 35  
3NG H21  H  N N 36  
3NG HO25 H  N N 37  
ALA N    N  N N 38  
ALA CA   C  N S 39  
ALA C    C  N N 40  
ALA O    O  N N 41  
ALA CB   C  N N 42  
ALA OXT  O  N N 43  
ALA H    H  N N 44  
ALA H2   H  N N 45  
ALA HA   H  N N 46  
ALA HB1  H  N N 47  
ALA HB2  H  N N 48  
ALA HB3  H  N N 49  
ALA HXT  H  N N 50  
ARG N    N  N N 51  
ARG CA   C  N S 52  
ARG C    C  N N 53  
ARG O    O  N N 54  
ARG CB   C  N N 55  
ARG CG   C  N N 56  
ARG CD   C  N N 57  
ARG NE   N  N N 58  
ARG CZ   C  N N 59  
ARG NH1  N  N N 60  
ARG NH2  N  N N 61  
ARG OXT  O  N N 62  
ARG H    H  N N 63  
ARG H2   H  N N 64  
ARG HA   H  N N 65  
ARG HB2  H  N N 66  
ARG HB3  H  N N 67  
ARG HG2  H  N N 68  
ARG HG3  H  N N 69  
ARG HD2  H  N N 70  
ARG HD3  H  N N 71  
ARG HE   H  N N 72  
ARG HH11 H  N N 73  
ARG HH12 H  N N 74  
ARG HH21 H  N N 75  
ARG HH22 H  N N 76  
ARG HXT  H  N N 77  
ASN N    N  N N 78  
ASN CA   C  N S 79  
ASN C    C  N N 80  
ASN O    O  N N 81  
ASN CB   C  N N 82  
ASN CG   C  N N 83  
ASN OD1  O  N N 84  
ASN ND2  N  N N 85  
ASN OXT  O  N N 86  
ASN H    H  N N 87  
ASN H2   H  N N 88  
ASN HA   H  N N 89  
ASN HB2  H  N N 90  
ASN HB3  H  N N 91  
ASN HD21 H  N N 92  
ASN HD22 H  N N 93  
ASN HXT  H  N N 94  
ASP N    N  N N 95  
ASP CA   C  N S 96  
ASP C    C  N N 97  
ASP O    O  N N 98  
ASP CB   C  N N 99  
ASP CG   C  N N 100 
ASP OD1  O  N N 101 
ASP OD2  O  N N 102 
ASP OXT  O  N N 103 
ASP H    H  N N 104 
ASP H2   H  N N 105 
ASP HA   H  N N 106 
ASP HB2  H  N N 107 
ASP HB3  H  N N 108 
ASP HD2  H  N N 109 
ASP HXT  H  N N 110 
CYS N    N  N N 111 
CYS CA   C  N R 112 
CYS C    C  N N 113 
CYS O    O  N N 114 
CYS CB   C  N N 115 
CYS SG   S  N N 116 
CYS OXT  O  N N 117 
CYS H    H  N N 118 
CYS H2   H  N N 119 
CYS HA   H  N N 120 
CYS HB2  H  N N 121 
CYS HB3  H  N N 122 
CYS HG   H  N N 123 
CYS HXT  H  N N 124 
EDO C1   C  N N 125 
EDO O1   O  N N 126 
EDO C2   C  N N 127 
EDO O2   O  N N 128 
EDO H11  H  N N 129 
EDO H12  H  N N 130 
EDO HO1  H  N N 131 
EDO H21  H  N N 132 
EDO H22  H  N N 133 
EDO HO2  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 
PHE N    N  N N 297 
PHE CA   C  N S 298 
PHE C    C  N N 299 
PHE O    O  N N 300 
PHE CB   C  N N 301 
PHE CG   C  Y N 302 
PHE CD1  C  Y N 303 
PHE CD2  C  Y N 304 
PHE CE1  C  Y N 305 
PHE CE2  C  Y N 306 
PHE CZ   C  Y N 307 
PHE OXT  O  N N 308 
PHE H    H  N N 309 
PHE H2   H  N N 310 
PHE HA   H  N N 311 
PHE HB2  H  N N 312 
PHE HB3  H  N N 313 
PHE HD1  H  N N 314 
PHE HD2  H  N N 315 
PHE HE1  H  N N 316 
PHE HE2  H  N N 317 
PHE HZ   H  N N 318 
PHE HXT  H  N N 319 
PRO N    N  N N 320 
PRO CA   C  N S 321 
PRO C    C  N N 322 
PRO O    O  N N 323 
PRO CB   C  N N 324 
PRO CG   C  N N 325 
PRO CD   C  N N 326 
PRO OXT  O  N N 327 
PRO H    H  N N 328 
PRO HA   H  N N 329 
PRO HB2  H  N N 330 
PRO HB3  H  N N 331 
PRO HG2  H  N N 332 
PRO HG3  H  N N 333 
PRO HD2  H  N N 334 
PRO HD3  H  N N 335 
PRO HXT  H  N N 336 
SER N    N  N N 337 
SER CA   C  N S 338 
SER C    C  N N 339 
SER O    O  N N 340 
SER CB   C  N N 341 
SER OG   O  N N 342 
SER OXT  O  N N 343 
SER H    H  N N 344 
SER H2   H  N N 345 
SER HA   H  N N 346 
SER HB2  H  N N 347 
SER HB3  H  N N 348 
SER HG   H  N N 349 
SER HXT  H  N N 350 
THR N    N  N N 351 
THR CA   C  N S 352 
THR C    C  N N 353 
THR O    O  N N 354 
THR CB   C  N R 355 
THR OG1  O  N N 356 
THR CG2  C  N N 357 
THR OXT  O  N N 358 
THR H    H  N N 359 
THR H2   H  N N 360 
THR HA   H  N N 361 
THR HB   H  N N 362 
THR HG1  H  N N 363 
THR HG21 H  N N 364 
THR HG22 H  N N 365 
THR HG23 H  N N 366 
THR HXT  H  N N 367 
TRP N    N  N N 368 
TRP CA   C  N S 369 
TRP C    C  N N 370 
TRP O    O  N N 371 
TRP CB   C  N N 372 
TRP CG   C  Y N 373 
TRP CD1  C  Y N 374 
TRP CD2  C  Y N 375 
TRP NE1  N  Y N 376 
TRP CE2  C  Y N 377 
TRP CE3  C  Y N 378 
TRP CZ2  C  Y N 379 
TRP CZ3  C  Y N 380 
TRP CH2  C  Y N 381 
TRP OXT  O  N N 382 
TRP H    H  N N 383 
TRP H2   H  N N 384 
TRP HA   H  N N 385 
TRP HB2  H  N N 386 
TRP HB3  H  N N 387 
TRP HD1  H  N N 388 
TRP HE1  H  N N 389 
TRP HE3  H  N N 390 
TRP HZ2  H  N N 391 
TRP HZ3  H  N N 392 
TRP HH2  H  N N 393 
TRP HXT  H  N N 394 
TYR N    N  N N 395 
TYR CA   C  N S 396 
TYR C    C  N N 397 
TYR O    O  N N 398 
TYR CB   C  N N 399 
TYR CG   C  Y N 400 
TYR CD1  C  Y N 401 
TYR CD2  C  Y N 402 
TYR CE1  C  Y N 403 
TYR CE2  C  Y N 404 
TYR CZ   C  Y N 405 
TYR OH   O  N N 406 
TYR OXT  O  N N 407 
TYR H    H  N N 408 
TYR H2   H  N N 409 
TYR HA   H  N N 410 
TYR HB2  H  N N 411 
TYR HB3  H  N N 412 
TYR HD1  H  N N 413 
TYR HD2  H  N N 414 
TYR HE1  H  N N 415 
TYR HE2  H  N N 416 
TYR HH   H  N N 417 
TYR HXT  H  N N 418 
VAL N    N  N N 419 
VAL CA   C  N S 420 
VAL C    C  N N 421 
VAL O    O  N N 422 
VAL CB   C  N N 423 
VAL CG1  C  N N 424 
VAL CG2  C  N N 425 
VAL OXT  O  N N 426 
VAL H    H  N N 427 
VAL H2   H  N N 428 
VAL HA   H  N N 429 
VAL HB   H  N N 430 
VAL HG11 H  N N 431 
VAL HG12 H  N N 432 
VAL HG13 H  N N 433 
VAL HG21 H  N N 434 
VAL HG22 H  N N 435 
VAL HG23 H  N N 436 
VAL HXT  H  N N 437 
# 
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 
3NG C1  C2   doub Y N 1   
3NG C1  N9   sing Y N 2   
3NG C1  C6   sing Y N 3   
3NG C2  C3   sing Y N 4   
3NG C8  C2   sing Y N 5   
3NG C3  C4   doub Y N 6   
3NG C3  H3   sing N N 7   
3NG C4  C5   sing Y N 8   
3NG C4  H4   sing N N 9   
3NG C5  C6   doub Y N 10  
3NG C5  C23  sing N N 11  
3NG C6  H6   sing N N 12  
3NG C14 C7   sing Y N 13  
3NG C10 C7   sing Y N 14  
3NG C7  C8   doub Y N 15  
3NG C8  C13  sing Y N 16  
3NG C10 N9   doub Y N 17  
3NG N15 C10  sing N N 18  
3NG C14 C11  doub Y N 19  
3NG C11 N12  sing Y N 20  
3NG C11 H11  sing N N 21  
3NG N12 C13  doub Y N 22  
3NG C13 H13  sing N N 23  
3NG C14 H14  sing N N 24  
3NG C16 N15  sing N N 25  
3NG N15 HN15 sing N N 26  
3NG C21 C16  doub Y N 27  
3NG C16 C17  sing Y N 28  
3NG C18 C17  doub Y N 29  
3NG C17 H17  sing N N 30  
3NG C19 C18  sing Y N 31  
3NG C18 CL22 sing N N 32  
3NG C20 C19  doub Y N 33  
3NG C19 H19  sing N N 34  
3NG C20 C21  sing Y N 35  
3NG C20 H20  sing N N 36  
3NG C21 H21  sing N N 37  
3NG O24 C23  doub N N 38  
3NG C23 O25  sing N N 39  
3NG O25 HO25 sing N N 40  
ALA N   CA   sing N N 41  
ALA N   H    sing N N 42  
ALA N   H2   sing N N 43  
ALA CA  C    sing N N 44  
ALA CA  CB   sing N N 45  
ALA CA  HA   sing N N 46  
ALA C   O    doub N N 47  
ALA C   OXT  sing N N 48  
ALA CB  HB1  sing N N 49  
ALA CB  HB2  sing N N 50  
ALA CB  HB3  sing N N 51  
ALA OXT HXT  sing N N 52  
ARG N   CA   sing N N 53  
ARG N   H    sing N N 54  
ARG N   H2   sing N N 55  
ARG CA  C    sing N N 56  
ARG CA  CB   sing N N 57  
ARG CA  HA   sing N N 58  
ARG C   O    doub N N 59  
ARG C   OXT  sing N N 60  
ARG CB  CG   sing N N 61  
ARG CB  HB2  sing N N 62  
ARG CB  HB3  sing N N 63  
ARG CG  CD   sing N N 64  
ARG CG  HG2  sing N N 65  
ARG CG  HG3  sing N N 66  
ARG CD  NE   sing N N 67  
ARG CD  HD2  sing N N 68  
ARG CD  HD3  sing N N 69  
ARG NE  CZ   sing N N 70  
ARG NE  HE   sing N N 71  
ARG CZ  NH1  sing N N 72  
ARG CZ  NH2  doub N N 73  
ARG NH1 HH11 sing N N 74  
ARG NH1 HH12 sing N N 75  
ARG NH2 HH21 sing N N 76  
ARG NH2 HH22 sing N N 77  
ARG OXT HXT  sing N N 78  
ASN N   CA   sing N N 79  
ASN N   H    sing N N 80  
ASN N   H2   sing N N 81  
ASN CA  C    sing N N 82  
ASN CA  CB   sing N N 83  
ASN CA  HA   sing N N 84  
ASN C   O    doub N N 85  
ASN C   OXT  sing N N 86  
ASN CB  CG   sing N N 87  
ASN CB  HB2  sing N N 88  
ASN CB  HB3  sing N N 89  
ASN CG  OD1  doub N N 90  
ASN CG  ND2  sing N N 91  
ASN ND2 HD21 sing N N 92  
ASN ND2 HD22 sing N N 93  
ASN OXT HXT  sing N N 94  
ASP N   CA   sing N N 95  
ASP N   H    sing N N 96  
ASP N   H2   sing N N 97  
ASP CA  C    sing N N 98  
ASP CA  CB   sing N N 99  
ASP CA  HA   sing N N 100 
ASP C   O    doub N N 101 
ASP C   OXT  sing N N 102 
ASP CB  CG   sing N N 103 
ASP CB  HB2  sing N N 104 
ASP CB  HB3  sing N N 105 
ASP CG  OD1  doub N N 106 
ASP CG  OD2  sing N N 107 
ASP OD2 HD2  sing N N 108 
ASP OXT HXT  sing N N 109 
CYS N   CA   sing N N 110 
CYS N   H    sing N N 111 
CYS N   H2   sing N N 112 
CYS CA  C    sing N N 113 
CYS CA  CB   sing N N 114 
CYS CA  HA   sing N N 115 
CYS C   O    doub N N 116 
CYS C   OXT  sing N N 117 
CYS CB  SG   sing N N 118 
CYS CB  HB2  sing N N 119 
CYS CB  HB3  sing N N 120 
CYS SG  HG   sing N N 121 
CYS OXT HXT  sing N N 122 
EDO C1  O1   sing N N 123 
EDO C1  C2   sing N N 124 
EDO C1  H11  sing N N 125 
EDO C1  H12  sing N N 126 
EDO O1  HO1  sing N N 127 
EDO C2  O2   sing N N 128 
EDO C2  H21  sing N N 129 
EDO C2  H22  sing N N 130 
EDO O2  HO2  sing N N 131 
GLN N   CA   sing N N 132 
GLN N   H    sing N N 133 
GLN N   H2   sing N N 134 
GLN CA  C    sing N N 135 
GLN CA  CB   sing N N 136 
GLN CA  HA   sing N N 137 
GLN C   O    doub N N 138 
GLN C   OXT  sing N N 139 
GLN CB  CG   sing N N 140 
GLN CB  HB2  sing N N 141 
GLN CB  HB3  sing N N 142 
GLN CG  CD   sing N N 143 
GLN CG  HG2  sing N N 144 
GLN CG  HG3  sing N N 145 
GLN CD  OE1  doub N N 146 
GLN CD  NE2  sing N N 147 
GLN NE2 HE21 sing N N 148 
GLN NE2 HE22 sing N N 149 
GLN OXT HXT  sing N N 150 
GLU N   CA   sing N N 151 
GLU N   H    sing N N 152 
GLU N   H2   sing N N 153 
GLU CA  C    sing N N 154 
GLU CA  CB   sing N N 155 
GLU CA  HA   sing N N 156 
GLU C   O    doub N N 157 
GLU C   OXT  sing N N 158 
GLU CB  CG   sing N N 159 
GLU CB  HB2  sing N N 160 
GLU CB  HB3  sing N N 161 
GLU CG  CD   sing N N 162 
GLU CG  HG2  sing N N 163 
GLU CG  HG3  sing N N 164 
GLU CD  OE1  doub N N 165 
GLU CD  OE2  sing N N 166 
GLU OE2 HE2  sing N N 167 
GLU OXT HXT  sing N N 168 
GLY N   CA   sing N N 169 
GLY N   H    sing N N 170 
GLY N   H2   sing N N 171 
GLY CA  C    sing N N 172 
GLY CA  HA2  sing N N 173 
GLY CA  HA3  sing N N 174 
GLY C   O    doub N N 175 
GLY C   OXT  sing N N 176 
GLY OXT HXT  sing N N 177 
HIS N   CA   sing N N 178 
HIS N   H    sing N N 179 
HIS N   H2   sing N N 180 
HIS CA  C    sing N N 181 
HIS CA  CB   sing N N 182 
HIS CA  HA   sing N N 183 
HIS C   O    doub N N 184 
HIS C   OXT  sing N N 185 
HIS CB  CG   sing N N 186 
HIS CB  HB2  sing N N 187 
HIS CB  HB3  sing N N 188 
HIS CG  ND1  sing Y N 189 
HIS CG  CD2  doub Y N 190 
HIS ND1 CE1  doub Y N 191 
HIS ND1 HD1  sing N N 192 
HIS CD2 NE2  sing Y N 193 
HIS CD2 HD2  sing N N 194 
HIS CE1 NE2  sing Y N 195 
HIS CE1 HE1  sing N N 196 
HIS NE2 HE2  sing N N 197 
HIS OXT HXT  sing N N 198 
HOH O   H1   sing N N 199 
HOH O   H2   sing N N 200 
ILE N   CA   sing N N 201 
ILE N   H    sing N N 202 
ILE N   H2   sing N N 203 
ILE CA  C    sing N N 204 
ILE CA  CB   sing N N 205 
ILE CA  HA   sing N N 206 
ILE C   O    doub N N 207 
ILE C   OXT  sing N N 208 
ILE CB  CG1  sing N N 209 
ILE CB  CG2  sing N N 210 
ILE CB  HB   sing N N 211 
ILE CG1 CD1  sing N N 212 
ILE CG1 HG12 sing N N 213 
ILE CG1 HG13 sing N N 214 
ILE CG2 HG21 sing N N 215 
ILE CG2 HG22 sing N N 216 
ILE CG2 HG23 sing N N 217 
ILE CD1 HD11 sing N N 218 
ILE CD1 HD12 sing N N 219 
ILE CD1 HD13 sing N N 220 
ILE OXT HXT  sing N N 221 
LEU N   CA   sing N N 222 
LEU N   H    sing N N 223 
LEU N   H2   sing N N 224 
LEU CA  C    sing N N 225 
LEU CA  CB   sing N N 226 
LEU CA  HA   sing N N 227 
LEU C   O    doub N N 228 
LEU C   OXT  sing N N 229 
LEU CB  CG   sing N N 230 
LEU CB  HB2  sing N N 231 
LEU CB  HB3  sing N N 232 
LEU CG  CD1  sing N N 233 
LEU CG  CD2  sing N N 234 
LEU CG  HG   sing N N 235 
LEU CD1 HD11 sing N N 236 
LEU CD1 HD12 sing N N 237 
LEU CD1 HD13 sing N N 238 
LEU CD2 HD21 sing N N 239 
LEU CD2 HD22 sing N N 240 
LEU CD2 HD23 sing N N 241 
LEU OXT HXT  sing N N 242 
LYS N   CA   sing N N 243 
LYS N   H    sing N N 244 
LYS N   H2   sing N N 245 
LYS CA  C    sing N N 246 
LYS CA  CB   sing N N 247 
LYS CA  HA   sing N N 248 
LYS C   O    doub N N 249 
LYS C   OXT  sing N N 250 
LYS CB  CG   sing N N 251 
LYS CB  HB2  sing N N 252 
LYS CB  HB3  sing N N 253 
LYS CG  CD   sing N N 254 
LYS CG  HG2  sing N N 255 
LYS CG  HG3  sing N N 256 
LYS CD  CE   sing N N 257 
LYS CD  HD2  sing N N 258 
LYS CD  HD3  sing N N 259 
LYS CE  NZ   sing N N 260 
LYS CE  HE2  sing N N 261 
LYS CE  HE3  sing N N 262 
LYS NZ  HZ1  sing N N 263 
LYS NZ  HZ2  sing N N 264 
LYS NZ  HZ3  sing N N 265 
LYS OXT HXT  sing N N 266 
MET N   CA   sing N N 267 
MET N   H    sing N N 268 
MET N   H2   sing N N 269 
MET CA  C    sing N N 270 
MET CA  CB   sing N N 271 
MET CA  HA   sing N N 272 
MET C   O    doub N N 273 
MET C   OXT  sing N N 274 
MET CB  CG   sing N N 275 
MET CB  HB2  sing N N 276 
MET CB  HB3  sing N N 277 
MET CG  SD   sing N N 278 
MET CG  HG2  sing N N 279 
MET CG  HG3  sing N N 280 
MET SD  CE   sing N N 281 
MET CE  HE1  sing N N 282 
MET CE  HE2  sing N N 283 
MET CE  HE3  sing N N 284 
MET OXT HXT  sing N N 285 
PHE N   CA   sing N N 286 
PHE N   H    sing N N 287 
PHE N   H2   sing N N 288 
PHE CA  C    sing N N 289 
PHE CA  CB   sing N N 290 
PHE CA  HA   sing N N 291 
PHE C   O    doub N N 292 
PHE C   OXT  sing N N 293 
PHE CB  CG   sing N N 294 
PHE CB  HB2  sing N N 295 
PHE CB  HB3  sing N N 296 
PHE CG  CD1  doub Y N 297 
PHE CG  CD2  sing Y N 298 
PHE CD1 CE1  sing Y N 299 
PHE CD1 HD1  sing N N 300 
PHE CD2 CE2  doub Y N 301 
PHE CD2 HD2  sing N N 302 
PHE CE1 CZ   doub Y N 303 
PHE CE1 HE1  sing N N 304 
PHE CE2 CZ   sing Y N 305 
PHE CE2 HE2  sing N N 306 
PHE CZ  HZ   sing N N 307 
PHE OXT HXT  sing N N 308 
PRO N   CA   sing N N 309 
PRO N   CD   sing N N 310 
PRO N   H    sing N N 311 
PRO CA  C    sing N N 312 
PRO CA  CB   sing N N 313 
PRO CA  HA   sing N N 314 
PRO C   O    doub N N 315 
PRO C   OXT  sing N N 316 
PRO CB  CG   sing N N 317 
PRO CB  HB2  sing N N 318 
PRO CB  HB3  sing N N 319 
PRO CG  CD   sing N N 320 
PRO CG  HG2  sing N N 321 
PRO CG  HG3  sing N N 322 
PRO CD  HD2  sing N N 323 
PRO CD  HD3  sing N N 324 
PRO OXT HXT  sing N N 325 
SER N   CA   sing N N 326 
SER N   H    sing N N 327 
SER N   H2   sing N N 328 
SER CA  C    sing N N 329 
SER CA  CB   sing N N 330 
SER CA  HA   sing N N 331 
SER C   O    doub N N 332 
SER C   OXT  sing N N 333 
SER CB  OG   sing N N 334 
SER CB  HB2  sing N N 335 
SER CB  HB3  sing N N 336 
SER OG  HG   sing N N 337 
SER OXT HXT  sing N N 338 
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   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           'NI 643/11-1' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3OFM 
_pdbx_initial_refinement_model.details          ? 
# 
_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                    9HK5 
_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]   0.021373 
_atom_sites.fract_transf_matrix[1][2]   0.000577 
_atom_sites.fract_transf_matrix[1][3]   0.000319 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020926 
_atom_sites.fract_transf_matrix[2][3]   0.008358 
_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]   0.021290 
_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.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 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.
;
? 
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    . GLY A 1 21  ? 56.58101 55.96710 -15.60520 1.000 40.60933 ? 7   GLY A N    1 
ATOM   2    C  CA   . GLY A 1 21  ? 55.63448 55.02459 -15.03086 1.000 32.91073 ? 7   GLY A CA   1 
ATOM   3    C  C    . GLY A 1 21  ? 55.28381 55.30688 -13.57871 1.000 30.63251 ? 7   GLY A C    1 
ATOM   4    O  O    . GLY A 1 21  ? 55.94971 56.10235 -12.90975 1.000 32.64820 ? 7   GLY A O    1 
ATOM   5    N  N    . SER A 1 22  ? 54.24085 54.64036 -13.08878 1.000 17.48505 ? 8   SER A N    1 
ATOM   6    C  CA   . SER A 1 22  ? 53.76396 54.86735 -11.72958 1.000 17.41559 ? 8   SER A CA   1 
ATOM   7    C  C    . SER A 1 22  ? 54.74792 54.32164 -10.69309 1.000 16.78635 ? 8   SER A C    1 
ATOM   8    O  O    . SER A 1 22  ? 55.39396 53.28773 -10.89347 1.000 16.99968 ? 8   SER A O    1 
ATOM   9    C  CB   . SER A 1 22  ? 52.39952 54.20375 -11.54470 1.000 17.34396 ? 8   SER A CB   1 
ATOM   10   O  OG   . SER A 1 22  ? 51.97024 54.25805 -10.20319 1.000 17.67154 ? 8   SER A OG   1 
ATOM   11   N  N    . ARG A 1 23  ? 54.84735 55.03253 -9.56677  1.000 20.58736 ? 9   ARG A N    1 
ATOM   12   C  CA   . ARG A 1 23  ? 55.64456 54.61066 -8.42286  1.000 14.56854 ? 9   ARG A CA   1 
ATOM   13   C  C    . ARG A 1 23  ? 54.86574 54.87674 -7.14768  1.000 16.25237 ? 9   ARG A C    1 
ATOM   14   O  O    . ARG A 1 23  ? 54.06933 55.81625 -7.07178  1.000 15.20258 ? 9   ARG A O    1 
ATOM   15   C  CB   . ARG A 1 23  ? 56.93912 55.42186 -8.27818  1.000 17.04682 ? 9   ARG A CB   1 
ATOM   16   C  CG   . ARG A 1 23  ? 57.87646 55.35346 -9.44108  1.000 35.42764 ? 9   ARG A CG   1 
ATOM   17   C  CD   . ARG A 1 23  ? 59.03899 56.29870 -9.20105  1.000 51.36043 ? 9   ARG A CD   1 
ATOM   18   N  NE   . ARG A 1 23  ? 59.68029 56.06821 -7.91069  1.000 36.83465 ? 9   ARG A NE   1 
ATOM   19   C  CZ   . ARG A 1 23  ? 60.80397 55.38213 -7.74420  1.000 33.63432 ? 9   ARG A CZ   1 
ATOM   20   N  NH1  . ARG A 1 23  ? 61.43442 54.82403 -8.76718  1.000 30.93875 ? 9   ARG A NH1  1 
ATOM   21   N  NH2  . ARG A 1 23  ? 61.31542 55.26421 -6.52347  1.000 34.93344 ? 9   ARG A NH2  1 
ATOM   22   N  N    . ALA A 1 24  ? 55.12372 54.04577 -6.14068  1.000 10.39241 ? 10  ALA A N    1 
ATOM   23   C  CA   . ALA A 1 24  ? 54.60583 54.29214 -4.80334  1.000 12.44232 ? 10  ALA A CA   1 
ATOM   24   C  C    . ALA A 1 24  ? 55.13214 55.62108 -4.25953  1.000 12.73209 ? 10  ALA A C    1 
ATOM   25   O  O    . ALA A 1 24  ? 56.31128 55.96303 -4.42653  1.000 13.28511 ? 10  ALA A O    1 
ATOM   26   C  CB   . ALA A 1 24  ? 55.04736 53.15319 -3.89055  1.000 9.54387  ? 10  ALA A CB   1 
ATOM   27   N  N    . ARG A 1 25  ? 54.24171 56.37012 -3.60320  1.000 11.97574 ? 11  ARG A N    1 
ATOM   28   C  CA   . ARG A 1 25  ? 54.60123 57.63038 -2.95606  1.000 12.25098 ? 11  ARG A CA   1 
ATOM   29   C  C    . ARG A 1 25  ? 55.40767 57.41461 -1.68436  1.000 12.28490 ? 11  ARG A C    1 
ATOM   30   O  O    . ARG A 1 25  ? 56.03094 58.36635 -1.18777  1.000 14.70021 ? 11  ARG A O    1 
ATOM   31   C  CB   . ARG A 1 25  ? 53.33852 58.40387 -2.53701  1.000 14.56256 ? 11  ARG A CB   1 
ATOM   32   C  CG   . ARG A 1 25  ? 52.55186 59.04583 -3.64667  1.000 16.85061 ? 11  ARG A CG   1 
ATOM   33   C  CD   . ARG A 1 25  ? 51.68546 60.19707 -3.11118  1.000 15.06271 ? 11  ARG A CD   1 
ATOM   34   N  NE   . ARG A 1 25  ? 50.49538 59.74960 -2.39149  1.000 12.39532 ? 11  ARG A NE   1 
ATOM   35   C  CZ   . ARG A 1 25  ? 50.29445 59.91188 -1.09032  1.000 14.75729 ? 11  ARG A CZ   1 
ATOM   36   N  NH1  . ARG A 1 25  ? 51.20906 60.47715 -0.31504  1.000 12.29982 ? 11  ARG A NH1  1 
ATOM   37   N  NH2  . ARG A 1 25  ? 49.14065 59.51319 -0.55640  1.000 8.47020  ? 11  ARG A NH2  1 
ATOM   38   N  N    . VAL A 1 26  ? 55.38181 56.20420 -1.12854  1.000 8.85229  ? 12  VAL A N    1 
ATOM   39   C  CA   . VAL A 1 26  ? 56.07440 55.87641 0.11324   1.000 7.62985  ? 12  VAL A CA   1 
ATOM   40   C  C    . VAL A 1 26  ? 56.73904 54.51572 -0.05782  1.000 10.67197 ? 12  VAL A C    1 
ATOM   41   O  O    . VAL A 1 26  ? 56.26660 53.66783 -0.82149  1.000 10.89300 ? 12  VAL A O    1 
ATOM   42   C  CB   . VAL A 1 26  ? 55.14260 55.86987 1.34800   1.000 10.06851 ? 12  VAL A CB   1 
ATOM   43   C  CG1  . VAL A 1 26  ? 54.64266 57.27702 1.66939   1.000 9.34624  ? 12  VAL A CG1  1 
ATOM   44   C  CG2  . VAL A 1 26  ? 53.97322 54.91175 1.15223   1.000 11.63459 ? 12  VAL A CG2  1 
ATOM   45   N  N    . TYR A 1 27  ? 57.86057 54.32576 0.64206   1.000 10.84389 ? 13  TYR A N    1 
ATOM   46   C  CA   . TYR A 1 27  ? 58.54581 53.03371 0.72136   1.000 7.82298  ? 13  TYR A CA   1 
ATOM   47   C  C    . TYR A 1 27  ? 58.93559 52.49395 -0.65411  1.000 8.45853  ? 13  TYR A C    1 
ATOM   48   O  O    . TYR A 1 27  ? 59.05563 51.28046 -0.85146  1.000 11.65668 ? 13  TYR A O    1 
ATOM   49   C  CB   . TYR A 1 27  ? 57.74205 52.00550 1.52952   1.000 7.54971  ? 13  TYR A CB   1 
ATOM   50   C  CG   . TYR A 1 27  ? 57.19879 52.51598 2.86380   1.000 11.83104 ? 13  TYR A CG   1 
ATOM   51   C  CD1  . TYR A 1 27  ? 58.04489 53.01854 3.85939   1.000 19.18331 ? 13  TYR A CD1  1 
ATOM   52   C  CD2  . TYR A 1 27  ? 55.84539 52.45240 3.13804   1.000 12.70800 ? 13  TYR A CD2  1 
ATOM   53   C  CE1  . TYR A 1 27  ? 57.52400 53.46341 5.09643   1.000 10.55930 ? 13  TYR A CE1  1 
ATOM   54   C  CE2  . TYR A 1 27  ? 55.32608 52.88775 4.35103   1.000 18.92571 ? 13  TYR A CE2  1 
ATOM   55   C  CZ   . TYR A 1 27  ? 56.16218 53.39415 5.32168   1.000 19.57863 ? 13  TYR A CZ   1 
ATOM   56   O  OH   . TYR A 1 27  ? 55.61252 53.82809 6.52090   1.000 23.13934 ? 13  TYR A OH   1 
ATOM   57   N  N    . ALA A 1 28  ? 59.14861 53.38947 -1.62157  1.000 11.08747 ? 14  ALA A N    1 
ATOM   58   C  CA   . ALA A 1 28  ? 59.44883 52.93709 -2.97402  1.000 10.31186 ? 14  ALA A CA   1 
ATOM   59   C  C    . ALA A 1 28  ? 60.82015 52.28398 -3.05899  1.000 17.44017 ? 14  ALA A C    1 
ATOM   60   O  O    . ALA A 1 28  ? 61.01659 51.36319 -3.85579  1.000 19.38045 ? 14  ALA A O    1 
ATOM   61   C  CB   . ALA A 1 28  ? 59.34206 54.10098 -3.96071  1.000 12.89236 ? 14  ALA A CB   1 
ATOM   62   N  N    . GLU A 1 29  ? 61.76617 52.71687 -2.23503  1.000 13.37521 ? 15  GLU A N    1 
ATOM   63   C  CA   . GLU A 1 29  ? 63.14053 52.24884 -2.32987  1.000 13.66048 ? 15  GLU A CA   1 
ATOM   64   C  C    . GLU A 1 29  ? 63.55074 51.32436 -1.19267  1.000 14.06237 ? 15  GLU A C    1 
ATOM   65   O  O    . GLU A 1 29  ? 64.72631 50.96525 -1.10888  1.000 18.30526 ? 15  GLU A O    1 
ATOM   66   C  CB   . GLU A 1 29  ? 64.09112 53.44595 -2.40622  1.000 20.32784 ? 15  GLU A CB   1 
ATOM   67   C  CG   . GLU A 1 29  ? 63.76592 54.41655 -3.53743  1.000 26.78023 ? 15  GLU A CG   1 
ATOM   68   C  CD   . GLU A 1 29  ? 64.02951 53.83331 -4.92753  1.000 51.85953 ? 15  GLU A CD   1 
ATOM   69   O  OE1  . GLU A 1 29  ? 64.60002 52.72372 -5.02849  1.000 62.73395 ? 15  GLU A OE1  1 
ATOM   70   O  OE2  . GLU A 1 29  ? 63.66607 54.48942 -5.92871  1.000 56.42444 ? 15  GLU A OE2  1 
ATOM   71   N  N    . VAL A 1 30  ? 62.62286 50.91012 -0.32727  1.000 12.27679 ? 16  VAL A N    1 
ATOM   72   C  CA   . VAL A 1 30  ? 63.03263 50.21053 0.88742   1.000 12.81875 ? 16  VAL A CA   1 
ATOM   73   C  C    . VAL A 1 30  ? 63.75167 48.91027 0.56280   1.000 14.53442 ? 16  VAL A C    1 
ATOM   74   O  O    . VAL A 1 30  ? 64.74015 48.56393 1.21232   1.000 14.75658 ? 16  VAL A O    1 
ATOM   75   C  CB   . VAL A 1 30  ? 61.85419 49.99572 1.85502   1.000 25.75513 ? 16  VAL A CB   1 
ATOM   76   C  CG1  . VAL A 1 30  ? 61.45732 51.30309 2.51818   1.000 33.08943 ? 16  VAL A CG1  1 
ATOM   77   C  CG2  . VAL A 1 30  ? 60.70405 49.38469 1.13935   1.000 20.53590 ? 16  VAL A CG2  1 
ATOM   78   N  N    . ASN A 1 31  ? 63.29324 48.18257 -0.45600  1.000 11.82407 ? 17  ASN A N    1 
ATOM   79   C  CA   . ASN A 1 31  ? 63.91954 46.89922 -0.75633  1.000 6.74338  ? 17  ASN A CA   1 
ATOM   80   C  C    . ASN A 1 31  ? 65.30280 47.06960 -1.38165  1.000 7.98003  ? 17  ASN A C    1 
ATOM   81   O  O    . ASN A 1 31  ? 66.24632 46.36346 -1.00947  1.000 9.49962  ? 17  ASN A O    1 
ATOM   82   C  CB   . ASN A 1 31  ? 62.98931 46.04404 -1.60359  1.000 7.92551  ? 17  ASN A CB   1 
ATOM   83   C  CG   . ASN A 1 31  ? 61.82028 45.52990 -0.79621  1.000 12.12892 ? 17  ASN A CG   1 
ATOM   84   O  OD1  . ASN A 1 31  ? 61.97773 45.26959 0.38852   1.000 18.39331 ? 17  ASN A OD1  1 
ATOM   85   N  ND2  . ASN A 1 31  ? 60.64461 45.40368 -1.40782  1.000 8.20977  ? 17  ASN A ND2  1 
ATOM   86   N  N    . SER A 1 32  ? 65.45409 48.00297 -2.32011  1.000 9.63936  ? 18  SER A N    1 
ATOM   87   C  CA   . SER A 1 32  ? 66.76656 48.22560 -2.92893  1.000 8.17355  ? 18  SER A CA   1 
ATOM   88   C  C    . SER A 1 32  ? 67.80623 48.72302 -1.92767  1.000 9.86544  ? 18  SER A C    1 
ATOM   89   O  O    . SER A 1 32  ? 69.01187 48.52842 -2.14980  1.000 11.55278 ? 18  SER A O    1 
ATOM   90   C  CB   . SER A 1 32  ? 66.64188 49.18248 -4.11746  1.000 15.03924 ? 18  SER A CB   1 
ATOM   91   O  OG   . SER A 1 32  ? 66.26287 50.47736 -3.68955  1.000 25.60565 ? 18  SER A OG   1 
ATOM   92   N  N    . LEU A 1 33  ? 67.37615 49.35972 -0.83664  1.000 8.98223  ? 19  LEU A N    1 
ATOM   93   C  CA   . LEU A 1 33  ? 68.29944 49.84655 0.18065   1.000 7.91825  ? 19  LEU A CA   1 
ATOM   94   C  C    . LEU A 1 33  ? 68.67510 48.78094 1.19957   1.000 11.65851 ? 19  LEU A C    1 
ATOM   95   O  O    . LEU A 1 33  ? 69.56254 49.02718 2.02689   1.000 10.78286 ? 19  LEU A O    1 
ATOM   96   C  CB   . LEU A 1 33  ? 67.71559 51.07321 0.90082   1.000 7.20569  ? 19  LEU A CB   1 
ATOM   97   C  CG   . LEU A 1 33  ? 67.50760 52.31584 0.01433   1.000 11.80891 ? 19  LEU A CG   1 
ATOM   98   C  CD1  . LEU A 1 33  ? 66.97766 53.47233 0.83717   1.000 13.33327 ? 19  LEU A CD1  1 
ATOM   99   C  CD2  . LEU A 1 33  ? 68.79100 52.70390 -0.71469  1.000 10.30249 ? 19  LEU A CD2  1 
ATOM   100  N  N    . ARG A 1 34  ? 68.04854 47.61135 1.15055   1.000 9.83969  ? 20  ARG A N    1 
ATOM   101  C  CA   . ARG A 1 34  ? 68.37186 46.50950 2.04667   1.000 8.18928  ? 20  ARG A CA   1 
ATOM   102  C  C    . ARG A 1 34  ? 69.25345 45.48693 1.33918   1.000 9.60521  ? 20  ARG A C    1 
ATOM   103  O  O    . ARG A 1 34  ? 69.40074 45.49695 0.11410   1.000 11.99634 ? 20  ARG A O    1 
ATOM   104  C  CB   . ARG A 1 34  ? 67.08894 45.83363 2.54450   1.000 9.46007  ? 20  ARG A CB   1 
ATOM   105  C  CG   . ARG A 1 34  ? 66.21028 46.74436 3.44100   1.000 10.59941 ? 20  ARG A CG   1 
ATOM   106  C  CD   . ARG A 1 34  ? 64.93796 46.02995 3.88030   1.000 13.83259 ? 20  ARG A CD   1 
ATOM   107  N  NE   . ARG A 1 34  ? 64.11297 46.87175 4.73939   1.000 18.81411 ? 20  ARG A NE   1 
ATOM   108  C  CZ   . ARG A 1 34  ? 62.88174 47.28027 4.44673   1.000 27.95974 ? 20  ARG A CZ   1 
ATOM   109  N  NH1  . ARG A 1 34  ? 62.28231 46.93666 3.31408   1.000 23.28326 ? 20  ARG A NH1  1 
ATOM   110  N  NH2  . ARG A 1 34  ? 62.22879 48.04680 5.31688   1.000 23.60899 ? 20  ARG A NH2  1 
ATOM   111  N  N    . SER A 1 35  ? 69.86520 44.60676 2.13648   1.000 8.12826  ? 21  SER A N    1 
ATOM   112  C  CA   . SER A 1 35  ? 70.62787 43.49572 1.57390   1.000 8.93463  ? 21  SER A CA   1 
ATOM   113  C  C    . SER A 1 35  ? 69.76184 42.69762 0.60440   1.000 9.40118  ? 21  SER A C    1 
ATOM   114  O  O    . SER A 1 35  ? 68.56490 42.51304 0.82606   1.000 9.92878  ? 21  SER A O    1 
ATOM   115  C  CB   . SER A 1 35  ? 71.07972 42.57023 2.70050   1.000 10.28945 ? 21  SER A CB   1 
ATOM   116  O  OG   . SER A 1 35  ? 71.78145 43.28570 3.70532   1.000 8.44958  ? 21  SER A OG   1 
ATOM   117  N  N    . ARG A 1 36  ? 70.38429 42.19114 -0.46096  1.000 10.58753 ? 22  ARG A N    1 
ATOM   118  C  CA   . ARG A 1 36  ? 69.64494 41.36795 -1.41301  1.000 9.42843  ? 22  ARG A CA   1 
ATOM   119  C  C    . ARG A 1 36  ? 68.93362 40.19893 -0.73031  1.000 10.22196 ? 22  ARG A C    1 
ATOM   120  O  O    . ARG A 1 36  ? 67.80412 39.85049 -1.09199  1.000 8.51206  ? 22  ARG A O    1 
ATOM   121  C  CB   . ARG A 1 36  ? 70.58066 40.88070 -2.51783  1.000 9.13926  ? 22  ARG A CB   1 
ATOM   122  C  CG   . ARG A 1 36  ? 69.89482 39.92982 -3.46565  1.000 9.15792  ? 22  ARG A CG   1 
ATOM   123  C  CD   . ARG A 1 36  ? 70.82517 39.50566 -4.55710  1.000 11.35175 ? 22  ARG A CD   1 
ATOM   124  N  NE   . ARG A 1 36  ? 70.21724 38.48399 -5.39368  1.000 19.71107 ? 22  ARG A NE   1 
ATOM   125  C  CZ   . ARG A 1 36  ? 70.70172 38.12053 -6.57032  1.000 47.82799 ? 22  ARG A CZ   1 
ATOM   126  N  NH1  . ARG A 1 36  ? 71.80979 38.65851 -7.05190  1.000 37.58059 ? 22  ARG A NH1  1 
ATOM   127  N  NH2  . ARG A 1 36  ? 70.05778 37.19939 -7.28189  1.000 48.74231 ? 22  ARG A NH2  1 
ATOM   128  N  N    . GLU A 1 37  ? 69.55797 39.59750 0.28539   1.000 7.71945  ? 23  GLU A N    1 
ATOM   129  C  CA   . GLU A 1 37  ? 68.92846 38.44799 0.92931   1.000 8.28481  ? 23  GLU A CA   1 
ATOM   130  C  C    . GLU A 1 37  ? 67.58576 38.78752 1.55885   1.000 8.93348  ? 23  GLU A C    1 
ATOM   131  O  O    . GLU A 1 37  ? 66.77701 37.87904 1.77493   1.000 9.40337  ? 23  GLU A O    1 
ATOM   132  C  CB   . GLU A 1 37  ? 69.85147 37.80710 1.96857   1.000 15.72788 ? 23  GLU A CB   1 
ATOM   133  C  CG   . GLU A 1 37  ? 70.12788 38.68233 3.16895   1.000 25.67114 ? 23  GLU A CG   1 
ATOM   134  C  CD   . GLU A 1 37  ? 70.84854 37.93193 4.27472   1.000 60.93902 ? 23  GLU A CD   1 
ATOM   135  O  OE1  . GLU A 1 37  ? 70.91239 36.68191 4.20592   1.000 42.27923 ? 23  GLU A OE1  1 
ATOM   136  O  OE2  . GLU A 1 37  ? 71.35228 38.59352 5.21025   1.000 69.49641 ? 23  GLU A OE2  1 
ATOM   137  N  N    . TYR A 1 38  ? 67.32634 40.06788 1.82975   1.000 8.29438  ? 24  TYR A N    1 
ATOM   138  C  CA   . TYR A 1 38  ? 66.04463 40.47496 2.39597   1.000 10.48483 ? 24  TYR A CA   1 
ATOM   139  C  C    . TYR A 1 38  ? 64.88531 40.12600 1.46674   1.000 7.37714  ? 24  TYR A C    1 
ATOM   140  O  O    . TYR A 1 38  ? 63.85219 39.61547 1.91407   1.000 9.25801  ? 24  TYR A O    1 
ATOM   141  C  CB   . TYR A 1 38  ? 66.04950 41.97561 2.69388   1.000 8.28311  ? 24  TYR A CB   1 
ATOM   142  C  CG   . TYR A 1 38  ? 64.75106 42.45347 3.28995   1.000 7.29036  ? 24  TYR A CG   1 
ATOM   143  C  CD1  . TYR A 1 38  ? 64.52279 42.35610 4.66501   1.000 7.84967  ? 24  TYR A CD1  1 
ATOM   144  C  CD2  . TYR A 1 38  ? 63.74137 42.99294 2.48887   1.000 8.43483  ? 24  TYR A CD2  1 
ATOM   145  C  CE1  . TYR A 1 38  ? 63.33090 42.77010 5.22767   1.000 9.03321  ? 24  TYR A CE1  1 
ATOM   146  C  CE2  . TYR A 1 38  ? 62.52387 43.42666 3.05454   1.000 7.97978  ? 24  TYR A CE2  1 
ATOM   147  C  CZ   . TYR A 1 38  ? 62.33172 43.30501 4.42126   1.000 11.28742 ? 24  TYR A CZ   1 
ATOM   148  O  OH   . TYR A 1 38  ? 61.14611 43.72761 4.98791   1.000 11.06916 ? 24  TYR A OH   1 
ATOM   149  N  N    . TRP A 1 39  ? 65.03397 40.40756 0.16894   1.000 8.96485  ? 25  TRP A N    1 
ATOM   150  C  CA   . TRP A 1 39  ? 63.95251 40.25153 -0.79995  1.000 7.75584  ? 25  TRP A CA   1 
ATOM   151  C  C    . TRP A 1 39  ? 64.14879 39.08269 -1.76044  1.000 11.73256 ? 25  TRP A C    1 
ATOM   152  O  O    . TRP A 1 39  ? 63.20184 38.71991 -2.46866  1.000 11.06659 ? 25  TRP A O    1 
ATOM   153  C  CB   . TRP A 1 39  ? 63.72445 41.56127 -1.58942  1.000 8.42018  ? 25  TRP A CB   1 
ATOM   154  C  CG   . TRP A 1 39  ? 64.97327 42.18803 -2.17531  1.000 7.67953  ? 25  TRP A CG   1 
ATOM   155  C  CD1  . TRP A 1 39  ? 65.68632 43.23518 -1.65770  1.000 8.27964  ? 25  TRP A CD1  1 
ATOM   156  C  CD2  . TRP A 1 39  ? 65.64021 41.80636 -3.37694  1.000 11.23219 ? 25  TRP A CD2  1 
ATOM   157  N  NE1  . TRP A 1 39  ? 66.75650 43.51811 -2.45859  1.000 8.96405  ? 25  TRP A NE1  1 
ATOM   158  C  CE2  . TRP A 1 39  ? 66.75747 42.65370 -3.52124  1.000 7.57799  ? 25  TRP A CE2  1 
ATOM   159  C  CE3  . TRP A 1 39  ? 65.40659 40.82276 -4.34382  1.000 11.53602 ? 25  TRP A CE3  1 
ATOM   160  C  CZ2  . TRP A 1 39  ? 67.62765 42.56484 -4.60384  1.000 11.64276 ? 25  TRP A CZ2  1 
ATOM   161  C  CZ3  . TRP A 1 39  ? 66.28319 40.72631 -5.41641  1.000 14.75801 ? 25  TRP A CZ3  1 
ATOM   162  C  CH2  . TRP A 1 39  ? 67.37867 41.59301 -5.53597  1.000 15.82801 ? 25  TRP A CH2  1 
ATOM   163  N  N    . ASP A 1 40  ? 65.33572 38.47624 -1.79044  1.000 9.16181  ? 26  ASP A N    1 
ATOM   164  C  CA   . ASP A 1 40  ? 65.63781 37.37916 -2.71702  1.000 14.58807 ? 26  ASP A CA   1 
ATOM   165  C  C    . ASP A 1 40  ? 65.17298 36.06271 -2.09219  1.000 9.35794  ? 26  ASP A C    1 
ATOM   166  O  O    . ASP A 1 40  ? 65.96543 35.22123 -1.66046  1.000 14.80538 ? 26  ASP A O    1 
ATOM   167  C  CB   . ASP A 1 40  ? 67.12827 37.36893 -3.04049  1.000 11.81526 ? 26  ASP A CB   1 
ATOM   168  C  CG   . ASP A 1 40  ? 67.50366 36.36015 -4.12321  1.000 18.36690 ? 26  ASP A CG   1 
ATOM   169  O  OD1  . ASP A 1 40  ? 66.60849 35.73321 -4.71839  1.000 16.97971 ? 26  ASP A OD1  1 
ATOM   170  O  OD2  . ASP A 1 40  ? 68.71985 36.18892 -4.37742  1.000 16.87769 ? 26  ASP A OD2  1 
ATOM   171  N  N    . TYR A 1 41  ? 63.84309 35.90978 -2.03237  1.000 9.61281  ? 27  TYR A N    1 
ATOM   172  C  CA   . TYR A 1 41  ? 63.25794 34.78593 -1.30294  1.000 10.36836 ? 27  TYR A CA   1 
ATOM   173  C  C    . TYR A 1 41  ? 63.63422 33.43274 -1.90616  1.000 13.57591 ? 27  TYR A C    1 
ATOM   174  O  O    . TYR A 1 41  ? 63.64966 32.42272 -1.19418  1.000 11.49974 ? 27  TYR A O    1 
ATOM   175  C  CB   . TYR A 1 41  ? 61.74003 34.94457 -1.19849  1.000 8.49414  ? 27  TYR A CB   1 
ATOM   176  C  CG   . TYR A 1 41  ? 61.03887 35.05163 -2.53792  1.000 9.34191  ? 27  TYR A CG   1 
ATOM   177  C  CD1  . TYR A 1 41  ? 60.67659 33.90792 -3.24432  1.000 12.74114 ? 27  TYR A CD1  1 
ATOM   178  C  CD2  . TYR A 1 41  ? 60.74998 36.29254 -3.09757  1.000 11.24896 ? 27  TYR A CD2  1 
ATOM   179  C  CE1  . TYR A 1 41  ? 60.03825 33.99895 -4.46301  1.000 11.58189 ? 27  TYR A CE1  1 
ATOM   180  C  CE2  . TYR A 1 41  ? 60.11638 36.39342 -4.31556  1.000 16.25359 ? 27  TYR A CE2  1 
ATOM   181  C  CZ   . TYR A 1 41  ? 59.76936 35.23821 -4.99687  1.000 16.58418 ? 27  TYR A CZ   1 
ATOM   182  O  OH   . TYR A 1 41  ? 59.13133 35.31594 -6.20996  1.000 19.16557 ? 27  TYR A OH   1 
ATOM   183  N  N    . GLU A 1 42  ? 63.92851 33.37896 -3.20615  1.000 13.00358 ? 28  GLU A N    1 
ATOM   184  C  CA   . GLU A 1 42  ? 64.30671 32.10144 -3.80993  1.000 15.86974 ? 28  GLU A CA   1 
ATOM   185  C  C    . GLU A 1 42  ? 65.59649 31.54334 -3.22201  1.000 19.82298 ? 28  GLU A C    1 
ATOM   186  O  O    . GLU A 1 42  ? 65.79593 30.32410 -3.23765  1.000 18.32614 ? 28  GLU A O    1 
ATOM   187  C  CB   . GLU A 1 42  ? 64.41851 32.22769 -5.33398  1.000 16.85236 ? 28  GLU A CB   1 
ATOM   188  C  CG   . GLU A 1 42  ? 63.11346 32.59132 -6.01152  1.000 20.69438 ? 28  GLU A CG   1 
ATOM   189  C  CD   . GLU A 1 42  ? 63.27974 32.85605 -7.49819  1.000 56.94831 ? 28  GLU A CD   1 
ATOM   190  O  OE1  . GLU A 1 42  ? 63.39435 31.87289 -8.26308  1.000 39.41765 ? 28  GLU A OE1  1 
ATOM   191  O  OE2  . GLU A 1 42  ? 63.30630 34.04541 -7.89692  1.000 39.82555 ? 28  GLU A OE2  1 
ATOM   192  N  N    . ALA A 1 43  ? 66.45833 32.40099 -2.68105  1.000 12.92239 ? 29  ALA A N    1 
ATOM   193  C  CA   . ALA A 1 43  ? 67.71962 31.99136 -2.07716  1.000 16.88246 ? 29  ALA A CA   1 
ATOM   194  C  C    . ALA A 1 43  ? 67.59584 31.66224 -0.59451  1.000 11.79256 ? 29  ALA A C    1 
ATOM   195  O  O    . ALA A 1 43  ? 68.60125 31.32932 0.04076   1.000 15.97347 ? 29  ALA A O    1 
ATOM   196  C  CB   . ALA A 1 43  ? 68.75105 33.10544 -2.25088  1.000 18.76009 ? 29  ALA A CB   1 
ATOM   197  N  N    . HIS A 1 44  ? 66.39791 31.75604 -0.02569  1.000 13.64336 ? 30  HIS A N    1 
ATOM   198  C  CA   . HIS A 1 44  ? 66.23302 31.60972 1.41527   1.000 14.80040 ? 30  HIS A CA   1 
ATOM   199  C  C    . HIS A 1 44  ? 66.37634 30.14967 1.83918   1.000 16.25400 ? 30  HIS A C    1 
ATOM   200  O  O    . HIS A 1 44  ? 65.87167 29.24114 1.17827   1.000 18.00606 ? 30  HIS A O    1 
ATOM   201  C  CB   . HIS A 1 44  ? 64.84778 32.12550 1.79598   1.000 13.53001 ? 30  HIS A CB   1 
ATOM   202  C  CG   . HIS A 1 44  ? 64.52126 31.98752 3.24813   1.000 17.35842 ? 30  HIS A CG   1 
ATOM   203  N  ND1  . HIS A 1 44  ? 65.25332 32.60374 4.23999   1.000 13.79169 ? 30  HIS A ND1  1 
ATOM   204  C  CD2  . HIS A 1 44  ? 63.53025 31.31132 3.87478   1.000 15.44327 ? 30  HIS A CD2  1 
ATOM   205  C  CE1  . HIS A 1 44  ? 64.72542 32.31413 5.41587   1.000 13.56257 ? 30  HIS A CE1  1 
ATOM   206  N  NE2  . HIS A 1 44  ? 63.68321 31.52752 5.22131   1.000 17.03505 ? 30  HIS A NE2  1 
ATOM   207  N  N    . VAL A 1 45  ? 67.06473 29.92498 2.95587   1.000 23.21855 ? 31  VAL A N    1 
ATOM   208  C  CA   . VAL A 1 45  ? 67.25408 28.59221 3.52180   1.000 21.32895 ? 31  VAL A CA   1 
ATOM   209  C  C    . VAL A 1 45  ? 66.35799 28.47122 4.74760   1.000 13.68051 ? 31  VAL A C    1 
ATOM   210  O  O    . VAL A 1 45  ? 66.50994 29.23275 5.71400   1.000 19.10684 ? 31  VAL A O    1 
ATOM   211  C  CB   . VAL A 1 45  ? 68.72434 28.33769 3.88484   1.000 25.45134 ? 31  VAL A CB   1 
ATOM   212  C  CG1  . VAL A 1 45  ? 68.88155 26.96554 4.54964   1.000 22.65020 ? 31  VAL A CG1  1 
ATOM   213  C  CG2  . VAL A 1 45  ? 69.59588 28.43883 2.64228   1.000 22.43693 ? 31  VAL A CG2  1 
ATOM   214  N  N    . VAL A 1 46  ? 65.43273 27.51323 4.70785   1.000 16.60858 ? 32  VAL A N    1 
ATOM   215  C  CA   . VAL A 1 46  ? 64.41400 27.36245 5.74494   1.000 16.59816 ? 32  VAL A CA   1 
ATOM   216  C  C    . VAL A 1 46  ? 64.99116 26.59114 6.92314   1.000 15.53770 ? 32  VAL A C    1 
ATOM   217  O  O    . VAL A 1 46  ? 65.76819 25.64516 6.74931   1.000 22.95724 ? 32  VAL A O    1 
ATOM   218  C  CB   . VAL A 1 46  ? 63.16942 26.65440 5.17081   1.000 19.07989 ? 32  VAL A CB   1 
ATOM   219  C  CG1  . VAL A 1 46  ? 62.12906 26.39368 6.26285   1.000 18.15981 ? 32  VAL A CG1  1 
ATOM   220  C  CG2  . VAL A 1 46  ? 62.56291 27.46782 4.03836   1.000 19.15193 ? 32  VAL A CG2  1 
ATOM   221  N  N    . SER A 1 47  ? 64.61954 27.00133 8.13242   1.000 19.36171 ? 33  SER A N    1 
ATOM   222  C  CA   . SER A 1 47  ? 64.93717 26.26463 9.34791   1.000 28.21694 ? 33  SER A CA   1 
ATOM   223  C  C    . SER A 1 47  ? 63.68720 25.51143 9.78624   1.000 20.62588 ? 33  SER A C    1 
ATOM   224  O  O    . SER A 1 47  ? 62.62904 26.11822 9.99436   1.000 21.62532 ? 33  SER A O    1 
ATOM   225  C  CB   . SER A 1 47  ? 65.40422 27.20975 10.45321  1.000 28.16134 ? 33  SER A CB   1 
ATOM   226  O  OG   . SER A 1 47  ? 66.64131 27.80948 10.10928  1.000 39.51441 ? 33  SER A OG   1 
ATOM   227  N  N    . TRP A 1 48  ? 63.81756 24.20104 9.94130   1.000 21.09443 ? 34  TRP A N    1 
ATOM   228  C  CA   . TRP A 1 48  ? 62.67735 23.32292 10.14310  1.000 16.02663 ? 34  TRP A CA   1 
ATOM   229  C  C    . TRP A 1 48  ? 62.55046 22.92936 11.60712  1.000 24.82230 ? 34  TRP A C    1 
ATOM   230  O  O    . TRP A 1 48  ? 63.54618 22.60252 12.25937  1.000 21.48405 ? 34  TRP A O    1 
ATOM   231  C  CB   . TRP A 1 48  ? 62.84348 22.06669 9.29460   1.000 14.31724 ? 34  TRP A CB   1 
ATOM   232  C  CG   . TRP A 1 48  ? 62.97941 22.37290 7.83431   1.000 17.36940 ? 34  TRP A CG   1 
ATOM   233  C  CD1  . TRP A 1 48  ? 64.13908 22.45176 7.11376   1.000 20.72284 ? 34  TRP A CD1  1 
ATOM   234  C  CD2  . TRP A 1 48  ? 61.91546 22.65051 6.91502   1.000 14.35350 ? 34  TRP A CD2  1 
ATOM   235  N  NE1  . TRP A 1 48  ? 63.86060 22.75195 5.80338   1.000 19.47702 ? 34  TRP A NE1  1 
ATOM   236  C  CE2  . TRP A 1 48  ? 62.50442 22.88107 5.65355   1.000 17.73470 ? 34  TRP A CE2  1 
ATOM   237  C  CE3  . TRP A 1 48  ? 60.52338 22.72036 7.03504   1.000 13.54404 ? 34  TRP A CE3  1 
ATOM   238  C  CZ2  . TRP A 1 48  ? 61.75057 23.18407 4.52053   1.000 14.86737 ? 34  TRP A CZ2  1 
ATOM   239  C  CZ3  . TRP A 1 48  ? 59.77142 23.02611 5.90599   1.000 16.64496 ? 34  TRP A CZ3  1 
ATOM   240  C  CH2  . TRP A 1 48  ? 60.38942 23.25829 4.66668   1.000 17.17255 ? 34  TRP A CH2  1 
ATOM   241  N  N    . GLY A 1 49  ? 61.31873 22.96782 12.11652  1.000 11.50601 ? 35  GLY A N    1 
ATOM   242  C  CA   . GLY A 1 49  ? 61.00328 22.46196 13.43711  1.000 13.17055 ? 35  GLY A CA   1 
ATOM   243  C  C    . GLY A 1 49  ? 60.69928 20.97300 13.42082  1.000 18.61434 ? 35  GLY A C    1 
ATOM   244  O  O    . GLY A 1 49  ? 61.02095 20.25084 12.47176  1.000 18.19067 ? 35  GLY A O    1 
ATOM   245  N  N    . ASN A 1 50  ? 60.05702 20.51284 14.49630  1.000 15.36908 ? 36  ASN A N    1 
ATOM   246  C  CA   . ASN A 1 50  ? 59.73120 19.10037 14.68780  1.000 19.45650 ? 36  ASN A CA   1 
ATOM   247  C  C    . ASN A 1 50  ? 58.24658 18.88376 14.40178  1.000 14.97377 ? 36  ASN A C    1 
ATOM   248  O  O    . ASN A 1 50  ? 57.38189 19.32049 15.17226  1.000 12.16620 ? 36  ASN A O    1 
ATOM   249  C  CB   . ASN A 1 50  ? 60.08918 18.65894 16.10637  1.000 15.00982 ? 36  ASN A CB   1 
ATOM   250  C  CG   . ASN A 1 50  ? 59.67775 17.22562 16.39778  1.000 28.36494 ? 36  ASN A CG   1 
ATOM   251  O  OD1  . ASN A 1 50  ? 59.43628 16.42700 15.48652  1.000 30.30680 ? 36  ASN A OD1  1 
ATOM   252  N  ND2  . ASN A 1 50  ? 59.59651 16.89154 17.68025  1.000 41.79435 ? 36  ASN A ND2  1 
ATOM   253  N  N    . GLN A 1 51  ? 57.95955 18.17216 13.30978  1.000 14.41151 ? 37  GLN A N    1 
ATOM   254  C  CA   . GLN A 1 51  ? 56.58177 17.99333 12.87269  1.000 13.46390 ? 37  GLN A CA   1 
ATOM   255  C  C    . GLN A 1 51  ? 55.73867 17.29216 13.92925  1.000 14.28184 ? 37  GLN A C    1 
ATOM   256  O  O    . GLN A 1 51  ? 54.55257 17.60390 14.07953  1.000 15.08128 ? 37  GLN A O    1 
ATOM   257  C  CB   . GLN A 1 51  ? 56.55048 17.19529 11.56913  1.000 17.76312 ? 37  GLN A CB   1 
ATOM   258  C  CG   . GLN A 1 51  ? 55.16322 17.07978 10.98973  1.000 15.29812 ? 37  GLN A CG   1 
ATOM   259  C  CD   . GLN A 1 51  ? 55.01154 15.92475 10.01541  1.000 24.77320 ? 37  GLN A CD   1 
ATOM   260  O  OE1  . GLN A 1 51  ? 55.68003 14.88644 10.13863  1.000 20.59425 ? 37  GLN A OE1  1 
ATOM   261  N  NE2  . GLN A 1 51  ? 54.12114 16.09625 9.03949   1.000 13.69609 ? 37  GLN A NE2  1 
ATOM   262  N  N    . ASP A 1 52  ? 56.33515 16.37231 14.69009  1.000 12.29671 ? 38  ASP A N    1 
ATOM   263  C  CA   . ASP A 1 52  ? 55.57376 15.60311 15.67001  1.000 10.46489 ? 38  ASP A CA   1 
ATOM   264  C  C    . ASP A 1 52  ? 55.14294 16.42098 16.88103  1.000 18.37564 ? 38  ASP A C    1 
ATOM   265  O  O    . ASP A 1 52  ? 54.39496 15.89404 17.71359  1.000 15.96788 ? 38  ASP A O    1 
ATOM   266  C  CB   . ASP A 1 52  ? 56.36113 14.36663 16.13072  1.000 13.60628 ? 38  ASP A CB   1 
ATOM   267  C  CG   . ASP A 1 52  ? 56.46337 13.30036 15.05106  1.000 25.84411 ? 38  ASP A CG   1 
ATOM   268  O  OD1  . ASP A 1 52  ? 55.67674 13.34969 14.07763  1.000 21.65053 ? 38  ASP A OD1  1 
ATOM   269  O  OD2  . ASP A 1 52  ? 57.33701 12.41627 15.17428  1.000 29.36917 ? 38  ASP A OD2  1 
ATOM   270  N  N    . ASP A 1 53  ? 55.59468 17.67701 17.01223  1.000 11.07631 ? 39  ASP A N    1 
ATOM   271  C  CA   . ASP A 1 53  ? 55.08668 18.54431 18.07289  1.000 10.57135 ? 39  ASP A CA   1 
ATOM   272  C  C    . ASP A 1 53  ? 53.61651 18.90917 17.88821  1.000 13.12978 ? 39  ASP A C    1 
ATOM   273  O  O    . ASP A 1 53  ? 52.99249 19.39218 18.83934  1.000 11.66625 ? 39  ASP A O    1 
ATOM   274  C  CB   . ASP A 1 53  ? 55.87858 19.85963 18.14246  1.000 14.41435 ? 39  ASP A CB   1 
ATOM   275  C  CG   . ASP A 1 53  ? 57.31912 19.67362 18.62552  1.000 19.52303 ? 39  ASP A CG   1 
ATOM   276  O  OD1  . ASP A 1 53  ? 57.69344 18.54628 19.00178  1.000 18.81248 ? 39  ASP A OD1  1 
ATOM   277  O  OD2  . ASP A 1 53  ? 58.07957 20.67126 18.62752  1.000 20.64028 ? 39  ASP A OD2  1 
ATOM   278  N  N    . TYR A 1 54  ? 53.04642 18.71335 16.70042  1.000 8.39504  ? 40  TYR A N    1 
ATOM   279  C  CA   . TYR A 1 54  ? 51.73238 19.26532 16.37920  1.000 10.31336 ? 40  TYR A CA   1 
ATOM   280  C  C    . TYR A 1 54  ? 50.75078 18.16256 16.01795  1.000 12.56422 ? 40  TYR A C    1 
ATOM   281  O  O    . TYR A 1 54  ? 51.04405 17.32178 15.16054  1.000 16.63168 ? 40  TYR A O    1 
ATOM   282  C  CB   . TYR A 1 54  ? 51.85087 20.30334 15.26326  1.000 10.91019 ? 40  TYR A CB   1 
ATOM   283  C  CG   . TYR A 1 54  ? 52.85195 21.35249 15.65310  1.000 6.19968  ? 40  TYR A CG   1 
ATOM   284  C  CD1  . TYR A 1 54  ? 52.55561 22.28176 16.64075  1.000 8.95464  ? 40  TYR A CD1  1 
ATOM   285  C  CD2  . TYR A 1 54  ? 54.12508 21.35914 15.10269  1.000 14.58081 ? 40  TYR A CD2  1 
ATOM   286  C  CE1  . TYR A 1 54  ? 53.48439 23.22436 17.02987  1.000 14.56595 ? 40  TYR A CE1  1 
ATOM   287  C  CE2  . TYR A 1 54  ? 55.06281 22.29214 15.48871  1.000 11.59244 ? 40  TYR A CE2  1 
ATOM   288  C  CZ   . TYR A 1 54  ? 54.73971 23.22050 16.45869  1.000 15.39381 ? 40  TYR A CZ   1 
ATOM   289  O  OH   . TYR A 1 54  ? 55.68218 24.14946 16.84860  1.000 14.05533 ? 40  TYR A OH   1 
ATOM   290  N  N    . GLN A 1 55  ? 49.58265 18.18335 16.65953  1.000 7.64436  ? 41  GLN A N    1 
ATOM   291  C  CA   . GLN A 1 55  ? 48.54183 17.18412 16.45199  1.000 10.12201 ? 41  GLN A CA   1 
ATOM   292  C  C    . GLN A 1 55  ? 47.31989 17.87784 15.86176  1.000 11.22361 ? 41  GLN A C    1 
ATOM   293  O  O    . GLN A 1 55  ? 46.78884 18.81803 16.46075  1.000 10.01234 ? 41  GLN A O    1 
ATOM   294  C  CB   . GLN A 1 55  ? 48.17855 16.52408 17.78525  1.000 12.22377 ? 41  GLN A CB   1 
ATOM   295  C  CG   . GLN A 1 55  ? 46.89363 15.71559 17.74126  1.000 12.61075 ? 41  GLN A CG   1 
ATOM   296  C  CD   . GLN A 1 55  ? 47.01834 14.48398 16.85745  1.000 21.33847 ? 41  GLN A CD   1 
ATOM   297  O  OE1  . GLN A 1 55  ? 47.95984 13.70148 16.99634  1.000 20.67712 ? 41  GLN A OE1  1 
ATOM   298  N  NE2  . GLN A 1 55  ? 46.07083 14.31081 15.93388  1.000 13.39055 ? 41  GLN A NE2  1 
ATOM   299  N  N    . LEU A 1 56  ? 46.86444 17.41220 14.70369  1.000 10.45588 ? 42  LEU A N    1 
ATOM   300  C  CA   . LEU A 1 56  ? 45.71807 18.03535 14.05453  1.000 10.84168 ? 42  LEU A CA   1 
ATOM   301  C  C    . LEU A 1 56  ? 44.42590 17.65883 14.77573  1.000 10.24854 ? 42  LEU A C    1 
ATOM   302  O  O    . LEU A 1 56  ? 44.20041 16.49255 15.10839  1.000 10.46912 ? 42  LEU A O    1 
ATOM   303  C  CB   . LEU A 1 56  ? 45.63048 17.60132 12.58745  1.000 8.34056  ? 42  LEU A CB   1 
ATOM   304  C  CG   . LEU A 1 56  ? 46.83051 17.90879 11.69352  1.000 6.62774  ? 42  LEU A CG   1 
ATOM   305  C  CD1  . LEU A 1 56  ? 46.49518 17.63908 10.23510  1.000 7.18274  ? 42  LEU A CD1  1 
ATOM   306  C  CD2  . LEU A 1 56  ? 47.32210 19.34521 11.89420  1.000 9.08807  ? 42  LEU A CD2  1 
ATOM   307  N  N    . VAL A 1 57  ? 43.55757 18.65200 14.98275  1.000 10.75947 ? 43  VAL A N    1 
ATOM   308  C  CA   . VAL A 1 57  ? 42.31896 18.48138 15.73449  1.000 9.42882  ? 43  VAL A CA   1 
ATOM   309  C  C    . VAL A 1 57  ? 41.08238 18.60147 14.83939  1.000 12.72370 ? 43  VAL A C    1 
ATOM   310  O  O    . VAL A 1 57  ? 40.15125 17.80061 14.94162  1.000 13.70892 ? 43  VAL A O    1 
ATOM   311  C  CB   . VAL A 1 57  ? 42.25635 19.47034 16.92057  1.000 12.85521 ? 43  VAL A CB   1 
ATOM   312  C  CG1  . VAL A 1 57  ? 40.88762 19.45580 17.55347  1.000 21.36032 ? 43  VAL A CG1  1 
ATOM   313  C  CG2  . VAL A 1 57  ? 43.31673 19.11274 17.94140  1.000 16.34614 ? 43  VAL A CG2  1 
ATOM   314  N  N    . ARG A 1 58  ? 41.05252 19.60350 13.96392  1.000 12.93322 ? 44  ARG A N    1 
ATOM   315  C  CA   . ARG A 1 58  ? 39.84657 19.90737 13.20393  1.000 11.11563 ? 44  ARG A CA   1 
ATOM   316  C  C    . ARG A 1 58  ? 40.23648 20.68766 11.95886  1.000 9.70604  ? 44  ARG A C    1 
ATOM   317  O  O    . ARG A 1 58  ? 41.06007 21.59990 12.02485  1.000 13.53361 ? 44  ARG A O    1 
ATOM   318  C  CB   . ARG A 1 58  ? 38.89958 20.75206 14.06835  1.000 17.09365 ? 44  ARG A CB   1 
ATOM   319  C  CG   . ARG A 1 58  ? 37.61788 21.20645 13.38952  1.000 33.04169 ? 44  ARG A CG   1 
ATOM   320  C  CD   . ARG A 1 58  ? 36.69045 21.88273 14.40009  1.000 29.05120 ? 44  ARG A CD   1 
ATOM   321  N  NE   . ARG A 1 58  ? 37.34112 23.00021 15.07289  1.000 44.02720 ? 44  ARG A NE   1 
ATOM   322  C  CZ   . ARG A 1 58  ? 37.18292 24.27434 14.73594  1.000 62.30018 ? 44  ARG A CZ   1 
ATOM   323  N  NH1  . ARG A 1 58  ? 36.36673 24.63479 13.75743  1.000 47.13737 ? 44  ARG A NH1  1 
ATOM   324  N  NH2  . ARG A 1 58  ? 37.86124 25.21102 15.39668  1.000 48.77032 ? 44  ARG A NH2  1 
ATOM   325  N  N    . LYS A 1 59  ? 39.63377 20.33542 10.82911  1.000 14.89707 ? 45  LYS A N    1 
ATOM   326  C  CA   . LYS A 1 59  ? 39.85939 21.07265 9.59616   1.000 12.55969 ? 45  LYS A CA   1 
ATOM   327  C  C    . LYS A 1 59  ? 39.05448 22.37113 9.62059   1.000 13.02992 ? 45  LYS A C    1 
ATOM   328  O  O    . LYS A 1 59  ? 37.85019 22.36410 9.90386   1.000 15.96133 ? 45  LYS A O    1 
ATOM   329  C  CB   . LYS A 1 59  ? 39.46909 20.20441 8.40046   1.000 14.43827 ? 45  LYS A CB   1 
ATOM   330  C  CG   . LYS A 1 59  ? 39.64351 20.85616 7.04074   1.000 23.51269 ? 45  LYS A CG   1 
ATOM   331  C  CD   . LYS A 1 59  ? 39.42043 19.82697 5.93072   1.000 26.29764 ? 45  LYS A CD   1 
ATOM   332  C  CE   . LYS A 1 59  ? 39.65693 20.41597 4.54981   1.000 33.41596 ? 45  LYS A CE   1 
ATOM   333  N  NZ   . LYS A 1 59  ? 39.51736 19.39054 3.46773   1.000 25.99875 ? 45  LYS A NZ   1 
ATOM   334  N  N    . LEU A 1 60  ? 39.72881 23.48941 9.35610   1.000 11.28841 ? 46  LEU A N    1 
ATOM   335  C  CA   . LEU A 1 60  ? 39.05809 24.78534 9.30518   1.000 11.66064 ? 46  LEU A CA   1 
ATOM   336  C  C    . LEU A 1 60  ? 38.60116 25.13128 7.89834   1.000 22.46213 ? 46  LEU A C    1 
ATOM   337  O  O    . LEU A 1 60  ? 37.51035 25.68249 7.71312   1.000 25.18997 ? 46  LEU A O    1 
ATOM   338  C  CB   . LEU A 1 60  ? 39.98491 25.88778 9.83043   1.000 16.21229 ? 46  LEU A CB   1 
ATOM   339  C  CG   . LEU A 1 60  ? 40.45364 25.74591 11.27674  1.000 20.51696 ? 46  LEU A CG   1 
ATOM   340  C  CD1  . LEU A 1 60  ? 41.40411 26.87128 11.64926  1.000 22.86626 ? 46  LEU A CD1  1 
ATOM   341  C  CD2  . LEU A 1 60  ? 39.27141 25.70215 12.22931  1.000 32.66459 ? 46  LEU A CD2  1 
ATOM   342  N  N    . GLY A 1 61  ? 39.41307 24.81657 6.90093   1.000 19.29414 ? 47  GLY A N    1 
ATOM   343  C  CA   . GLY A 1 61  ? 39.07591 25.18847 5.54446   1.000 26.78908 ? 47  GLY A CA   1 
ATOM   344  C  C    . GLY A 1 61  ? 40.18727 24.80079 4.59971   1.000 25.35332 ? 47  GLY A C    1 
ATOM   345  O  O    . GLY A 1 61  ? 41.16246 24.15276 4.98681   1.000 18.42828 ? 47  GLY A O    1 
ATOM   346  N  N    . ARG A 1 62  ? 40.02110 25.21435 3.34505   1.000 20.02318 ? 48  ARG A N    1 
ATOM   347  C  CA   . ARG A 1 62  ? 40.91015 24.81207 2.26759   1.000 23.01379 ? 48  ARG A CA   1 
ATOM   348  C  C    . ARG A 1 62  ? 41.02531 25.95744 1.27919   1.000 35.82740 ? 48  ARG A C    1 
ATOM   349  O  O    . ARG A 1 62  ? 40.01459 26.54774 0.88577   1.000 37.12609 ? 48  ARG A O    1 
ATOM   350  C  CB   . ARG A 1 62  ? 40.35405 23.58217 1.54223   1.000 34.51775 ? 48  ARG A CB   1 
ATOM   351  C  CG   . ARG A 1 62  ? 40.89323 23.40866 0.13206   1.000 47.96235 ? 48  ARG A CG   1 
ATOM   352  C  CD   . ARG A 1 62  ? 40.18130 22.29091 -0.60756  1.000 53.70416 ? 48  ARG A CD   1 
ATOM   353  N  NE   . ARG A 1 62  ? 40.25347 21.03178 0.12349   1.000 64.91511 ? 48  ARG A NE   1 
ATOM   354  C  CZ   . ARG A 1 62  ? 39.71336 19.89170 -0.28729  1.000 77.06456 ? 48  ARG A CZ   1 
ATOM   355  N  NH1  . ARG A 1 62  ? 39.06021 19.80982 -1.43710  1.000 62.02216 ? 48  ARG A NH1  1 
ATOM   356  N  NH2  . ARG A 1 62  ? 39.83122 18.80604 0.47480   1.000 40.70283 ? 48  ARG A NH2  1 
ATOM   357  N  N    . GLY A 1 63  ? 42.25808 26.26687 0.88349   1.000 42.79099 ? 49  GLY A N    1 
ATOM   358  C  CA   . GLY A 1 63  ? 42.50969 27.17012 -0.21341  1.000 33.53853 ? 49  GLY A CA   1 
ATOM   359  C  C    . GLY A 1 63  ? 42.93640 26.40771 -1.45812  1.000 40.54612 ? 49  GLY A C    1 
ATOM   360  O  O    . GLY A 1 63  ? 42.98523 25.17877 -1.48957  1.000 23.49225 ? 49  GLY A O    1 
ATOM   361  N  N    . LYS A 1 64  ? 43.26090 27.17856 -2.49835  1.000 30.61686 ? 50  LYS A N    1 
ATOM   362  C  CA   . LYS A 1 64  ? 43.66747 26.57725 -3.76389  1.000 37.89817 ? 50  LYS A CA   1 
ATOM   363  C  C    . LYS A 1 64  ? 44.94645 25.76344 -3.60863  1.000 31.90906 ? 50  LYS A C    1 
ATOM   364  O  O    . LYS A 1 64  ? 45.08208 24.69140 -4.21083  1.000 36.60868 ? 50  LYS A O    1 
ATOM   365  C  CB   . LYS A 1 64  ? 43.82671 27.66055 -4.83374  1.000 36.26590 ? 50  LYS A CB   1 
ATOM   366  C  CG   . LYS A 1 64  ? 44.53500 27.20047 -6.09668  1.000 46.44856 ? 50  LYS A CG   1 
ATOM   367  C  CD   . LYS A 1 64  ? 43.65197 27.31058 -7.33343  1.000 60.05940 ? 50  LYS A CD   1 
ATOM   368  C  CE   . LYS A 1 64  ? 42.63277 26.18273 -7.39957  1.000 63.16822 ? 50  LYS A CE   1 
ATOM   369  N  NZ   . LYS A 1 64  ? 41.93060 26.15032 -8.71440  1.000 68.16826 ? 50  LYS A NZ   1 
ATOM   370  N  N    . TYR A 1 65  ? 45.88647 26.24076 -2.78599  1.000 25.83337 ? 51  TYR A N    1 
ATOM   371  C  CA   . TYR A 1 65  ? 47.17879 25.58020 -2.61987  1.000 28.17355 ? 51  TYR A CA   1 
ATOM   372  C  C    . TYR A 1 65  ? 47.47671 25.20377 -1.16817  1.000 29.47679 ? 51  TYR A C    1 
ATOM   373  O  O    . TYR A 1 65  ? 48.63584 24.94183 -0.83072  1.000 28.09916 ? 51  TYR A O    1 
ATOM   374  C  CB   . TYR A 1 65  ? 48.31589 26.43204 -3.19652  1.000 30.41219 ? 51  TYR A CB   1 
ATOM   375  C  CG   . TYR A 1 65  ? 48.09946 26.87058 -4.63192  1.000 46.48492 ? 51  TYR A CG   1 
ATOM   376  C  CD1  . TYR A 1 65  ? 48.03231 25.93817 -5.66436  1.000 41.86769 ? 51  TYR A CD1  1 
ATOM   377  C  CD2  . TYR A 1 65  ? 47.97140 28.21821 -4.95619  1.000 36.00447 ? 51  TYR A CD2  1 
ATOM   378  C  CE1  . TYR A 1 65  ? 47.83549 26.33545 -6.98468  1.000 43.92411 ? 51  TYR A CE1  1 
ATOM   379  C  CE2  . TYR A 1 65  ? 47.77348 28.62543 -6.27352  1.000 44.07712 ? 51  TYR A CE2  1 
ATOM   380  C  CZ   . TYR A 1 65  ? 47.70775 27.67941 -7.28205  1.000 45.55817 ? 51  TYR A CZ   1 
ATOM   381  O  OH   . TYR A 1 65  ? 47.51130 28.07791 -8.58802  1.000 56.72249 ? 51  TYR A OH   1 
ATOM   382  N  N    . SER A 1 66  ? 46.46633 25.15649 -0.30092  1.000 19.98823 ? 52  SER A N    1 
ATOM   383  C  CA   . SER A 1 66  ? 46.72238 24.89166 1.11040   1.000 13.82289 ? 52  SER A CA   1 
ATOM   384  C  C    . SER A 1 66  ? 45.44340 24.42004 1.78482   1.000 19.30605 ? 52  SER A C    1 
ATOM   385  O  O    . SER A 1 66  ? 44.33889 24.56662 1.25273   1.000 22.36922 ? 52  SER A O    1 
ATOM   386  C  CB   . SER A 1 66  ? 47.25529 26.13585 1.82268   1.000 22.32483 ? 52  SER A CB   1 
ATOM   387  O  OG   . SER A 1 66  ? 46.30319 27.18435 1.78198   1.000 24.96364 ? 52  SER A OG   1 
ATOM   388  N  N    . GLU A 1 67  ? 45.61656 23.83880 2.96852   1.000 14.65997 ? 53  GLU A N    1 
ATOM   389  C  CA   . GLU A 1 67  ? 44.51392 23.45944 3.84003   1.000 16.63359 ? 53  GLU A CA   1 
ATOM   390  C  C    . GLU A 1 67  ? 44.91651 23.79231 5.26485   1.000 15.39198 ? 53  GLU A C    1 
ATOM   391  O  O    . GLU A 1 67  ? 46.07437 23.60530 5.64362   1.000 14.27206 ? 53  GLU A O    1 
ATOM   392  C  CB   . GLU A 1 67  ? 44.20436 21.96936 3.74620   1.000 16.61197 ? 53  GLU A CB   1 
ATOM   393  C  CG   . GLU A 1 67  ? 43.43831 21.58425 2.49009   1.000 28.83900 ? 53  GLU A CG   1 
ATOM   394  C  CD   . GLU A 1 67  ? 43.02761 20.12321 2.47395   1.000 41.94000 ? 53  GLU A CD   1 
ATOM   395  O  OE1  . GLU A 1 67  ? 43.03075 19.48637 3.55376   1.000 20.77486 ? 53  GLU A OE1  1 
ATOM   396  O  OE2  . GLU A 1 67  ? 42.71075 19.61349 1.37698   1.000 48.77241 ? 53  GLU A OE2  1 
ATOM   397  N  N    . VAL A 1 68  ? 43.95149 24.25355 6.05292   1.000 10.82146 ? 54  VAL A N    1 
ATOM   398  C  CA   . VAL A 1 68  ? 44.19766 24.85764 7.35401   1.000 11.25799 ? 54  VAL A CA   1 
ATOM   399  C  C    . VAL A 1 68  ? 43.47949 24.04925 8.43047   1.000 9.75635  ? 54  VAL A C    1 
ATOM   400  O  O    . VAL A 1 68  ? 42.29191 23.73360 8.28676   1.000 12.40213 ? 54  VAL A O    1 
ATOM   401  C  CB   . VAL A 1 68  ? 43.72611 26.32081 7.35000   1.000 13.56307 ? 54  VAL A CB   1 
ATOM   402  C  CG1  . VAL A 1 68  ? 43.95573 26.95572 8.69218   1.000 15.99044 ? 54  VAL A CG1  1 
ATOM   403  C  CG2  . VAL A 1 68  ? 44.46302 27.09753 6.26556   1.000 19.61985 ? 54  VAL A CG2  1 
ATOM   404  N  N    . PHE A 1 69  ? 44.19349 23.73289 9.51535   1.000 8.21688  ? 55  PHE A N    1 
ATOM   405  C  CA   . PHE A 1 69  ? 43.66129 22.93447 10.61385  1.000 12.25955 ? 55  PHE A CA   1 
ATOM   406  C  C    . PHE A 1 69  ? 43.86545 23.63478 11.95217  1.000 12.47832 ? 55  PHE A C    1 
ATOM   407  O  O    . PHE A 1 69  ? 44.89758 24.26515 12.18349  1.000 11.07084 ? 55  PHE A O    1 
ATOM   408  C  CB   . PHE A 1 69  ? 44.38239 21.57201 10.68582  1.000 10.03310 ? 55  PHE A CB   1 
ATOM   409  C  CG   . PHE A 1 69  ? 44.24791 20.73807 9.44019   1.000 11.18058 ? 55  PHE A CG   1 
ATOM   410  C  CD1  . PHE A 1 69  ? 45.10371 20.92481 8.35497   1.000 12.76066 ? 55  PHE A CD1  1 
ATOM   411  C  CD2  . PHE A 1 69  ? 43.27367 19.74826 9.35739   1.000 8.77952  ? 55  PHE A CD2  1 
ATOM   412  C  CE1  . PHE A 1 69  ? 44.98253 20.14270 7.21302   1.000 9.93311  ? 55  PHE A CE1  1 
ATOM   413  C  CE2  . PHE A 1 69  ? 43.15215 18.96268 8.22634   1.000 10.56275 ? 55  PHE A CE2  1 
ATOM   414  C  CZ   . PHE A 1 69  ? 43.99492 19.16505 7.14282   1.000 10.06884 ? 55  PHE A CZ   1 
ATOM   415  N  N    . GLU A 1 70  ? 42.88933 23.51049 12.84953  1.000 8.21821  ? 56  GLU A N    1 
ATOM   416  C  CA   . GLU A 1 70  ? 43.18756 23.69657 14.26187  1.000 6.63886  ? 56  GLU A CA   1 
ATOM   417  C  C    . GLU A 1 70  ? 44.02304 22.51602 14.73645  1.000 9.22816  ? 56  GLU A C    1 
ATOM   418  O  O    . GLU A 1 70  ? 43.80362 21.36966 14.32542  1.000 10.68162 ? 56  GLU A O    1 
ATOM   419  C  CB   . GLU A 1 70  ? 41.89438 23.78081 15.08064  1.000 14.06474 ? 56  GLU A CB   1 
ATOM   420  C  CG   . GLU A 1 70  ? 42.10600 23.92865 16.59235  1.000 19.94303 ? 56  GLU A CG   1 
ATOM   421  C  CD   . GLU A 1 70  ? 40.81001 23.79122 17.39152  1.000 28.12216 ? 56  GLU A CD   1 
ATOM   422  O  OE1  . GLU A 1 70  ? 39.73128 24.03213 16.81525  1.000 32.77586 ? 56  GLU A OE1  1 
ATOM   423  O  OE2  . GLU A 1 70  ? 40.87245 23.43435 18.59380  1.000 27.81071 ? 56  GLU A OE2  1 
ATOM   424  N  N    . ALA A 1 71  ? 45.01154 22.80094 15.57645  1.000 11.79405 ? 57  ALA A N    1 
ATOM   425  C  CA   . ALA A 1 71  ? 45.88970 21.76295 16.07542  1.000 7.61330  ? 57  ALA A CA   1 
ATOM   426  C  C    . ALA A 1 71  ? 46.28665 22.09475 17.50425  1.000 7.65306  ? 57  ALA A C    1 
ATOM   427  O  O    . ALA A 1 71  ? 46.00456 23.17973 18.02168  1.000 11.47914 ? 57  ALA A O    1 
ATOM   428  C  CB   . ALA A 1 71  ? 47.12636 21.60516 15.18866  1.000 12.03361 ? 57  ALA A CB   1 
ATOM   429  N  N    . ILE A 1 72  ? 46.96364 21.14688 18.13476  1.000 9.09812  ? 58  ILE A N    1 
ATOM   430  C  CA   . ILE A 1 72  ? 47.51163 21.32873 19.47313  1.000 11.21603 ? 58  ILE A CA   1 
ATOM   431  C  C    . ILE A 1 72  ? 49.01780 21.13063 19.40719  1.000 12.56352 ? 58  ILE A C    1 
ATOM   432  O  O    . ILE A 1 72  ? 49.50028 20.15567 18.81342  1.000 9.83651  ? 58  ILE A O    1 
ATOM   433  C  CB   . ILE A 1 72  ? 46.88533 20.34872 20.48153  1.000 13.17227 ? 58  ILE A CB   1 
ATOM   434  C  CG1  . ILE A 1 72  ? 45.38219 20.59229 20.60634  1.000 21.55757 ? 58  ILE A CG1  1 
ATOM   435  C  CG2  . ILE A 1 72  ? 47.54892 20.47372 21.84484  1.000 14.68916 ? 58  ILE A CG2  1 
ATOM   436  C  CD1  . ILE A 1 72  ? 45.02601 21.95061 21.15587  1.000 29.99615 ? 58  ILE A CD1  1 
ATOM   437  N  N    . ASN A 1 73  ? 49.75503 22.05026 20.01972  1.000 9.84014  ? 59  ASN A N    1 
ATOM   438  C  CA   . ASN A 1 73  ? 51.18549 21.88008 20.22335  1.000 11.20898 ? 59  ASN A CA   1 
ATOM   439  C  C    . ASN A 1 73  ? 51.34490 20.99315 21.45276  1.000 14.12275 ? 59  ASN A C    1 
ATOM   440  O  O    . ASN A 1 73  ? 51.09473 21.43476 22.57943  1.000 13.73655 ? 59  ASN A O    1 
ATOM   441  C  CB   . ASN A 1 73  ? 51.82391 23.25623 20.41840  1.000 12.84612 ? 59  ASN A CB   1 
ATOM   442  C  CG   . ASN A 1 73  ? 53.32902 23.19480 20.64063  1.000 17.23523 ? 59  ASN A CG   1 
ATOM   443  O  OD1  . ASN A 1 73  ? 53.88905 22.13292 20.90974  1.000 16.73866 ? 59  ASN A OD1  1 
ATOM   444  N  ND2  . ASN A 1 73  ? 53.98981 24.35741 20.55714  1.000 16.65557 ? 59  ASN A ND2  1 
ATOM   445  N  N    . ILE A 1 74  ? 51.74023 19.73195 21.24838  1.000 14.16486 ? 60  ILE A N    1 
ATOM   446  C  CA   . ILE A 1 74  ? 51.75908 18.79409 22.36530  1.000 16.42970 ? 60  ILE A CA   1 
ATOM   447  C  C    . ILE A 1 74  ? 52.84477 19.09930 23.38646  1.000 19.56212 ? 60  ILE A C    1 
ATOM   448  O  O    . ILE A 1 74  ? 52.77532 18.59029 24.50976  1.000 19.42610 ? 60  ILE A O    1 
ATOM   449  C  CB   . ILE A 1 74  ? 51.71213 17.31061 21.93145  1.000 20.15910 ? 60  ILE A CB   1 
ATOM   450  C  CG1  . ILE A 1 74  ? 53.03858 16.87298 21.31171  1.000 21.05178 ? 60  ILE A CG1  1 
ATOM   451  C  CG2  . ILE A 1 74  ? 50.55285 17.06396 20.96902  1.000 15.86608 ? 60  ILE A CG2  1 
ATOM   452  C  CD1  . ILE A 1 74  ? 53.10665 15.37437 21.04913  1.000 22.33164 ? 60  ILE A CD1  1 
ATOM   453  N  N    . THR A 1 75  ? 53.82259 19.94694 23.04928  1.000 16.75055 ? 61  THR A N    1 
ATOM   454  C  CA   . THR A 1 75  ? 54.86236 20.29122 24.01737  1.000 16.90559 ? 61  THR A CA   1 
ATOM   455  C  C    . THR A 1 75  ? 54.37537 21.26445 25.09402  1.000 20.34739 ? 61  THR A C    1 
ATOM   456  O  O    . THR A 1 75  ? 54.90860 21.26062 26.20932  1.000 20.92337 ? 61  THR A O    1 
ATOM   457  C  CB   . THR A 1 75  ? 56.11159 20.83563 23.31046  1.000 13.94390 ? 61  THR A CB   1 
ATOM   458  O  OG1  . THR A 1 75  ? 55.83948 22.13238 22.77292  1.000 19.44965 ? 61  THR A OG1  1 
ATOM   459  C  CG2  . THR A 1 75  ? 56.54317 19.91786 22.19170  1.000 19.29558 ? 61  THR A CG2  1 
ATOM   460  N  N    . ASN A 1 76  ? 53.37589 22.09914 24.80091  1.000 14.01728 ? 62  ASN A N    1 
ATOM   461  C  CA   . ASN A 1 76  ? 52.88213 23.06825 25.77118  1.000 14.83791 ? 62  ASN A CA   1 
ATOM   462  C  C    . ASN A 1 76  ? 51.36313 23.07341 25.89541  1.000 15.90508 ? 62  ASN A C    1 
ATOM   463  O  O    . ASN A 1 76  ? 50.81530 23.94373 26.58528  1.000 15.43052 ? 62  ASN A O    1 
ATOM   464  C  CB   . ASN A 1 76  ? 53.39243 24.48039 25.45264  1.000 16.36775 ? 62  ASN A CB   1 
ATOM   465  C  CG   . ASN A 1 76  ? 52.96300 24.95729 24.08480  1.000 16.17973 ? 62  ASN A CG   1 
ATOM   466  O  OD1  . ASN A 1 76  ? 52.07135 24.37803 23.46900  1.000 14.25138 ? 62  ASN A OD1  1 
ATOM   467  N  ND2  . ASN A 1 76  ? 53.59275 26.01884 23.60192  1.000 17.89095 ? 62  ASN A ND2  1 
ATOM   468  N  N    A ASN A 1 77  ? 50.66432 22.14389 25.23498  0.521 16.17117 ? 63  ASN A N    1 
ATOM   469  N  N    B ASN A 1 77  ? 50.67868 22.12938 25.25379  0.479 16.16610 ? 63  ASN A N    1 
ATOM   470  C  CA   A ASN A 1 77  ? 49.20345 22.00260 25.25095  0.521 16.49107 ? 63  ASN A CA   1 
ATOM   471  C  CA   B ASN A 1 77  ? 49.22438 22.04333 25.31341  0.479 16.49164 ? 63  ASN A CA   1 
ATOM   472  C  C    A ASN A 1 77  ? 48.45824 23.13352 24.54564  0.521 15.99573 ? 63  ASN A C    1 
ATOM   473  C  C    B ASN A 1 77  ? 48.55724 23.33512 24.84261  0.479 15.55580 ? 63  ASN A C    1 
ATOM   474  O  O    A ASN A 1 77  ? 47.22120 23.16898 24.57236  0.521 13.96328 ? 63  ASN A O    1 
ATOM   475  O  O    B ASN A 1 77  ? 47.49801 23.71494 25.34750  0.479 17.86709 ? 63  ASN A O    1 
ATOM   476  C  CB   A ASN A 1 77  ? 48.63539 21.76847 26.65765  0.521 15.70022 ? 63  ASN A CB   1 
ATOM   477  C  CB   B ASN A 1 77  ? 48.73849 21.64023 26.71183  0.479 15.59331 ? 63  ASN A CB   1 
ATOM   478  C  CG   A ASN A 1 77  ? 49.01545 20.42146 27.21250  0.521 16.62347 ? 63  ASN A CG   1 
ATOM   479  C  CG   B ASN A 1 77  ? 47.40492 20.93406 26.68086  0.479 16.77241 ? 63  ASN A CG   1 
ATOM   480  O  OD1  A ASN A 1 77  ? 49.58201 20.31720 28.30177  0.521 29.12743 ? 63  ASN A OD1  1 
ATOM   481  O  OD1  B ASN A 1 77  ? 47.12846 20.15823 25.77131  0.479 16.55219 ? 63  ASN A OD1  1 
ATOM   482  N  ND2  A ASN A 1 77  ? 48.71912 19.37283 26.45666  0.521 24.85296 ? 63  ASN A ND2  1 
ATOM   483  N  ND2  B ASN A 1 77  ? 46.56605 21.20085 27.67347  0.479 17.33980 ? 63  ASN A ND2  1 
ATOM   484  N  N    . GLU A 1 78  ? 49.16690 24.03815 23.88839  1.000 13.46690 ? 64  GLU A N    1 
ATOM   485  C  CA   . GLU A 1 78  ? 48.55577 25.24347 23.34574  1.000 12.28929 ? 64  GLU A CA   1 
ATOM   486  C  C    . GLU A 1 78  ? 47.93828 24.98978 21.98401  1.000 11.64943 ? 64  GLU A C    1 
ATOM   487  O  O    . GLU A 1 78  ? 48.48680 24.24256 21.16618  1.000 9.77758  ? 64  GLU A O    1 
ATOM   488  C  CB   . GLU A 1 78  ? 49.56042 26.38995 23.27163  1.000 17.90801 ? 64  GLU A CB   1 
ATOM   489  C  CG   . GLU A 1 78  ? 50.01405 26.81433 24.65247  1.000 24.22584 ? 64  GLU A CG   1 
ATOM   490  C  CD   . GLU A 1 78  ? 50.71601 28.14243 24.65469  1.000 23.30628 ? 64  GLU A CD   1 
ATOM   491  O  OE1  . GLU A 1 78  ? 50.71991 28.82224 23.60174  1.000 20.11027 ? 64  GLU A OE1  1 
ATOM   492  O  OE2  . GLU A 1 78  ? 51.26333 28.50335 25.71624  1.000 24.84826 ? 64  GLU A OE2  1 
ATOM   493  N  N    . ARG A 1 79  ? 46.77120 25.59417 21.77524  1.000 11.15931 ? 65  ARG A N    1 
ATOM   494  C  CA   . ARG A 1 79  ? 46.09599 25.54266 20.48934  1.000 12.90778 ? 65  ARG A CA   1 
ATOM   495  C  C    . ARG A 1 79  ? 46.85245 26.39317 19.47339  1.000 11.86829 ? 65  ARG A C    1 
ATOM   496  O  O    . ARG A 1 79  ? 47.32271 27.49272 19.78413  1.000 14.68174 ? 65  ARG A O    1 
ATOM   497  C  CB   . ARG A 1 79  ? 44.66560 26.06007 20.65346  1.000 14.98770 ? 65  ARG A CB   1 
ATOM   498  C  CG   . ARG A 1 79  ? 43.71037 25.71242 19.51494  1.000 21.81983 ? 65  ARG A CG   1 
ATOM   499  C  CD   . ARG A 1 79  ? 42.27219 26.08903 19.87728  1.000 19.11818 ? 65  ARG A CD   1 
ATOM   500  N  NE   . ARG A 1 79  ? 42.01510 25.83684 21.28860  1.000 28.46001 ? 65  ARG A NE   1 
ATOM   501  C  CZ   . ARG A 1 79  ? 41.41413 24.75543 21.76366  1.000 35.84762 ? 65  ARG A CZ   1 
ATOM   502  N  NH1  . ARG A 1 79  ? 40.90391 23.83803 20.95849  1.000 33.36180 ? 65  ARG A NH1  1 
ATOM   503  N  NH2  . ARG A 1 79  ? 41.32740 24.58810 23.08053  1.000 35.63096 ? 65  ARG A NH2  1 
ATOM   504  N  N    . VAL A 1 80  ? 46.99712 25.85795 18.26369  1.000 11.29348 ? 66  VAL A N    1 
ATOM   505  C  CA   . VAL A 1 80  ? 47.66413 26.51976 17.14976  1.000 9.03406  ? 66  VAL A CA   1 
ATOM   506  C  C    . VAL A 1 80  ? 46.87647 26.23323 15.87801  1.000 9.86051  ? 66  VAL A C    1 
ATOM   507  O  O    . VAL A 1 80  ? 45.86945 25.51405 15.88011  1.000 10.06190 ? 66  VAL A O    1 
ATOM   508  C  CB   . VAL A 1 80  ? 49.13044 26.06681 16.96397  1.000 10.22029 ? 66  VAL A CB   1 
ATOM   509  C  CG1  . VAL A 1 80  ? 49.98651 26.36601 18.20938  1.000 11.96120 ? 66  VAL A CG1  1 
ATOM   510  C  CG2  . VAL A 1 80  ? 49.18863 24.58943 16.57272  1.000 8.76041  ? 66  VAL A CG2  1 
ATOM   511  N  N    . VAL A 1 81  ? 47.35915 26.78471 14.77587  1.000 10.17253 ? 67  VAL A N    1 
ATOM   512  C  CA   . VAL A 1 81  ? 46.78324 26.55428 13.46025  1.000 9.52931  ? 67  VAL A CA   1 
ATOM   513  C  C    . VAL A 1 81  ? 47.88662 26.02068 12.56319  1.000 10.39095 ? 67  VAL A C    1 
ATOM   514  O  O    . VAL A 1 81  ? 48.99161 26.57014 12.54317  1.000 12.17089 ? 67  VAL A O    1 
ATOM   515  C  CB   . VAL A 1 81  ? 46.17282 27.84804 12.88603  1.000 10.93149 ? 67  VAL A CB   1 
ATOM   516  C  CG1  . VAL A 1 81  ? 45.88225 27.69222 11.42734  1.000 15.23461 ? 67  VAL A CG1  1 
ATOM   517  C  CG2  . VAL A 1 81  ? 44.88490 28.18626 13.63572  1.000 14.16047 ? 67  VAL A CG2  1 
ATOM   518  N  N    . VAL A 1 82  ? 47.60120 24.93909 11.84025  1.000 6.91319  ? 68  VAL A N    1 
ATOM   519  C  CA   . VAL A 1 82  ? 48.57089 24.34395 10.92621  1.000 6.62332  ? 68  VAL A CA   1 
ATOM   520  C  C    . VAL A 1 82  ? 48.06221 24.49954 9.50324   1.000 7.18998  ? 68  VAL A C    1 
ATOM   521  O  O    . VAL A 1 82  ? 46.94648 24.07620 9.18431   1.000 9.35412  ? 68  VAL A O    1 
ATOM   522  C  CB   . VAL A 1 82  ? 48.85685 22.87062 11.26160  1.000 10.41021 ? 68  VAL A CB   1 
ATOM   523  C  CG1  . VAL A 1 82  ? 49.77926 22.26940 10.22212  1.000 8.12574  ? 68  VAL A CG1  1 
ATOM   524  C  CG2  . VAL A 1 82  ? 49.48064 22.77036 12.65106  1.000 8.56596  ? 68  VAL A CG2  1 
ATOM   525  N  N    . LYS A 1 83  ? 48.88991 25.08232 8.64423   1.000 5.84636  ? 69  LYS A N    1 
ATOM   526  C  CA   . LYS A 1 83  ? 48.54474 25.30153 7.24432   1.000 5.69481  ? 69  LYS A CA   1 
ATOM   527  C  C    . LYS A 1 83  ? 49.44564 24.39838 6.41175   1.000 8.70859  ? 69  LYS A C    1 
ATOM   528  O  O    . LYS A 1 83  ? 50.63911 24.67558 6.26602   1.000 7.87291  ? 69  LYS A O    1 
ATOM   529  C  CB   . LYS A 1 83  ? 48.76959 26.76699 6.89133   1.000 7.25931  ? 69  LYS A CB   1 
ATOM   530  C  CG   . LYS A 1 83  ? 48.42213 27.16305 5.48128   1.000 9.61164  ? 69  LYS A CG   1 
ATOM   531  C  CD   . LYS A 1 83  ? 48.96178 28.58507 5.26461   1.000 16.02585 ? 69  LYS A CD   1 
ATOM   532  C  CE   . LYS A 1 83  ? 48.38593 29.22252 4.05457   1.000 19.77705 ? 69  LYS A CE   1 
ATOM   533  N  NZ   . LYS A 1 83  ? 48.68144 30.67538 4.09926   1.000 9.69338  ? 69  LYS A NZ   1 
ATOM   534  N  N    . ILE A 1 84  ? 48.87975 23.32919 5.86260   1.000 8.00651  ? 70  ILE A N    1 
ATOM   535  C  CA   . ILE A 1 84  ? 49.64021 22.38667 5.04647   1.000 8.23412  ? 70  ILE A CA   1 
ATOM   536  C  C    . ILE A 1 84  ? 49.64757 22.89906 3.60877   1.000 11.80424 ? 70  ILE A C    1 
ATOM   537  O  O    . ILE A 1 84  ? 48.58963 23.13481 3.01347   1.000 14.96809 ? 70  ILE A O    1 
ATOM   538  C  CB   . ILE A 1 84  ? 49.05295 20.96898 5.14259   1.000 11.35183 ? 70  ILE A CB   1 
ATOM   539  C  CG1  . ILE A 1 84  ? 49.06347 20.48237 6.59854   1.000 11.45214 ? 70  ILE A CG1  1 
ATOM   540  C  CG2  . ILE A 1 84  ? 49.82832 20.00819 4.24608   1.000 12.61218 ? 70  ILE A CG2  1 
ATOM   541  C  CD1  . ILE A 1 84  ? 48.41597 19.11043 6.79133   1.000 12.73889 ? 70  ILE A CD1  1 
ATOM   542  N  N    . LEU A 1 85  ? 50.83775 23.07214 3.04389   1.000 11.97472 ? 71  LEU A N    1 
ATOM   543  C  CA   . LEU A 1 85  ? 50.99364 23.65632 1.71606   1.000 12.36771 ? 71  LEU A CA   1 
ATOM   544  C  C    . LEU A 1 85  ? 51.13564 22.53577 0.68710   1.000 23.12675 ? 71  LEU A C    1 
ATOM   545  O  O    . LEU A 1 85  ? 52.09989 21.76535 0.72616   1.000 25.78058 ? 71  LEU A O    1 
ATOM   546  C  CB   . LEU A 1 85  ? 52.20488 24.58667 1.69645   1.000 12.68785 ? 71  LEU A CB   1 
ATOM   547  C  CG   . LEU A 1 85  ? 52.16807 25.64051 2.81401   1.000 20.12622 ? 71  LEU A CG   1 
ATOM   548  C  CD1  . LEU A 1 85  ? 53.54583 26.24497 3.06946   1.000 16.22166 ? 71  LEU A CD1  1 
ATOM   549  C  CD2  . LEU A 1 85  ? 51.15699 26.73165 2.48641   1.000 15.49299 ? 71  LEU A CD2  1 
ATOM   550  N  N    . LYS A 1 86  ? 50.16711 22.43970 -0.21601  1.000 32.40547 ? 72  LYS A N    1 
ATOM   551  C  CA   . LYS A 1 86  ? 50.05394 21.36636 -1.19752  1.000 37.19878 ? 72  LYS A CA   1 
ATOM   552  C  C    . LYS A 1 86  ? 48.92328 21.76976 -2.13725  1.000 39.45610 ? 72  LYS A C    1 
ATOM   553  O  O    . LYS A 1 86  ? 47.78477 21.93814 -1.68112  1.000 60.81580 ? 72  LYS A O    1 
ATOM   554  C  CB   . LYS A 1 86  ? 49.74767 20.01952 -0.51814  1.000 37.62009 ? 72  LYS A CB   1 
ATOM   555  C  CG   . LYS A 1 86  ? 49.92188 18.77543 -1.41972  1.000 66.43082 ? 72  LYS A CG   1 
ATOM   556  C  CD   . LYS A 1 86  ? 49.34554 17.48185 -0.79370  1.000 62.56045 ? 72  LYS A CD   1 
ATOM   557  C  CE   . LYS A 1 86  ? 49.58584 16.24641 -1.69385  1.000 59.62322 ? 72  LYS A CE   1 
ATOM   558  N  NZ   . LYS A 1 86  ? 48.76599 15.01622 -1.35781  1.000 35.55007 ? 72  LYS A NZ   1 
ATOM   559  N  N    . PRO A 1 87  ? 49.17106 21.94286 -3.44689  1.000 46.70347 ? 73  PRO A N    1 
ATOM   560  C  CA   . PRO A 1 87  ? 50.40854 21.71100 -4.21850  1.000 73.28966 ? 73  PRO A CA   1 
ATOM   561  C  C    . PRO A 1 87  ? 51.66559 22.36857 -3.66242  1.000 63.02719 ? 73  PRO A C    1 
ATOM   562  O  O    . PRO A 1 87  ? 51.62677 23.47034 -3.11731  1.000 41.12646 ? 73  PRO A O    1 
ATOM   563  C  CB   . PRO A 1 87  ? 50.05883 22.27713 -5.60484  1.000 70.20242 ? 73  PRO A CB   1 
ATOM   564  C  CG   . PRO A 1 87  ? 48.57942 22.07938 -5.71627  1.000 67.57085 ? 73  PRO A CG   1 
ATOM   565  C  CD   . PRO A 1 87  ? 48.05976 22.35242 -4.32705  1.000 57.99820 ? 73  PRO A CD   1 
ATOM   566  N  N    . VAL A 1 88  ? 52.79794 21.67862 -3.77348  1.000 53.82512 ? 74  VAL A N    1 
ATOM   567  C  CA   . VAL A 1 88  ? 54.06240 22.21141 -3.28576  1.000 69.99623 ? 74  VAL A CA   1 
ATOM   568  C  C    . VAL A 1 88  ? 54.68225 23.09305 -4.36757  1.000 66.49470 ? 74  VAL A C    1 
ATOM   569  O  O    . VAL A 1 88  ? 55.66025 22.71262 -5.02249  1.000 62.64917 ? 74  VAL A O    1 
ATOM   570  C  CB   . VAL A 1 88  ? 54.99272 21.08394 -2.79488  1.000 57.81783 ? 74  VAL A CB   1 
ATOM   571  C  CG1  . VAL A 1 88  ? 56.26148 21.65107 -2.15790  1.000 54.13620 ? 74  VAL A CG1  1 
ATOM   572  C  CG2  . VAL A 1 88  ? 54.25028 20.19733 -1.79531  1.000 33.77220 ? 74  VAL A CG2  1 
ATOM   573  N  N    . LYS A 1 89  ? 54.08309 24.26583 -4.57909  1.000 52.41438 ? 75  LYS A N    1 
ATOM   574  C  CA   . LYS A 1 89  ? 54.63302 25.31137 -5.43915  1.000 24.82607 ? 75  LYS A CA   1 
ATOM   575  C  C    . LYS A 1 89  ? 55.84205 25.89551 -4.72189  1.000 33.29376 ? 75  LYS A C    1 
ATOM   576  O  O    . LYS A 1 89  ? 55.70583 26.77446 -3.86726  1.000 29.72888 ? 75  LYS A O    1 
ATOM   577  C  CB   . LYS A 1 89  ? 53.57759 26.39164 -5.64903  1.000 52.50788 ? 75  LYS A CB   1 
ATOM   578  C  CG   . LYS A 1 89  ? 52.15533 25.87220 -5.85575  1.000 47.41124 ? 75  LYS A CG   1 
ATOM   579  C  CD   . LYS A 1 89  ? 51.94653 25.39358 -7.27986  1.000 48.91682 ? 75  LYS A CD   1 
ATOM   580  C  CE   . LYS A 1 89  ? 52.23487 26.50620 -8.28344  1.000 51.39634 ? 75  LYS A CE   1 
ATOM   581  N  NZ   . LYS A 1 89  ? 51.29698 27.65606 -8.13893  1.000 47.44185 ? 75  LYS A NZ   1 
ATOM   582  N  N    . LYS A 1 90  ? 57.03583 25.41285 -5.07415  1.000 28.65126 ? 76  LYS A N    1 
ATOM   583  C  CA   . LYS A 1 90  ? 58.20798 25.63889 -4.23197  1.000 33.19307 ? 76  LYS A CA   1 
ATOM   584  C  C    . LYS A 1 90  ? 58.56318 27.11779 -4.13923  1.000 27.93607 ? 76  LYS A C    1 
ATOM   585  O  O    . LYS A 1 90  ? 59.00754 27.59616 -3.08628  1.000 19.00846 ? 76  LYS A O    1 
ATOM   586  C  CB   . LYS A 1 90  ? 59.39055 24.82999 -4.76328  1.000 27.24326 ? 76  LYS A CB   1 
ATOM   587  C  CG   . LYS A 1 90  ? 59.46090 23.40278 -4.23875  1.000 59.23598 ? 76  LYS A CG   1 
ATOM   588  C  CD   . LYS A 1 90  ? 60.78061 22.74383 -4.62832  1.000 73.59414 ? 76  LYS A CD   1 
ATOM   589  C  CE   . LYS A 1 90  ? 61.24815 21.74079 -3.57540  1.000 68.75454 ? 76  LYS A CE   1 
ATOM   590  N  NZ   . LYS A 1 90  ? 60.29535 20.61136 -3.40535  1.000 70.35453 ? 76  LYS A NZ   1 
ATOM   591  N  N    . LYS A 1 91  ? 58.38016 27.85838 -5.23275  1.000 21.09532 ? 77  LYS A N    1 
ATOM   592  C  CA   . LYS A 1 91  ? 58.75468 29.26824 -5.23352  1.000 17.86510 ? 77  LYS A CA   1 
ATOM   593  C  C    . LYS A 1 91  ? 57.76689 30.09754 -4.41804  1.000 19.89942 ? 77  LYS A C    1 
ATOM   594  O  O    . LYS A 1 91  ? 58.16375 30.99258 -3.66187  1.000 18.03577 ? 77  LYS A O    1 
ATOM   595  C  CB   . LYS A 1 91  ? 58.84406 29.76106 -6.67915  1.000 28.12625 ? 77  LYS A CB   1 
ATOM   596  C  CG   . LYS A 1 91  ? 59.34085 31.18016 -6.83853  1.000 33.63937 ? 77  LYS A CG   1 
ATOM   597  C  CD   . LYS A 1 91  ? 59.42413 31.56107 -8.31249  1.000 42.30858 ? 77  LYS A CD   1 
ATOM   598  C  CE   . LYS A 1 91  ? 59.51907 33.06557 -8.49301  1.000 31.06910 ? 77  LYS A CE   1 
ATOM   599  N  NZ   . LYS A 1 91  ? 59.32031 33.44726 -9.92259  1.000 38.81520 ? 77  LYS A NZ   1 
ATOM   600  N  N    . LYS A 1 92  ? 56.47781 29.79955 -4.54749  1.000 18.50501 ? 78  LYS A N    1 
ATOM   601  C  CA   . LYS A 1 92  ? 55.46074 30.48526 -3.75866  1.000 17.60592 ? 78  LYS A CA   1 
ATOM   602  C  C    . LYS A 1 92  ? 55.63323 30.20221 -2.27108  1.000 15.04640 ? 78  LYS A C    1 
ATOM   603  O  O    . LYS A 1 92  ? 55.32846 31.06048 -1.43370  1.000 15.21659 ? 78  LYS A O    1 
ATOM   604  C  CB   . LYS A 1 92  ? 54.08487 30.02704 -4.25227  1.000 22.86131 ? 78  LYS A CB   1 
ATOM   605  C  CG   . LYS A 1 92  ? 52.91534 30.94921 -3.94244  1.000 35.55541 ? 78  LYS A CG   1 
ATOM   606  C  CD   . LYS A 1 92  ? 51.63005 30.44773 -4.60595  1.000 38.19937 ? 78  LYS A CD   1 
ATOM   607  C  CE   . LYS A 1 92  ? 50.39847 31.19112 -4.09375  1.000 33.39907 ? 78  LYS A CE   1 
ATOM   608  N  NZ   . LYS A 1 92  ? 50.22651 31.01971 -2.61738  1.000 29.63885 ? 78  LYS A NZ   1 
ATOM   609  N  N    . ILE A 1 93  ? 56.12932 29.01191 -1.92454  1.000 14.50652 ? 79  ILE A N    1 
ATOM   610  C  CA   . ILE A 1 93  ? 56.29399 28.63833 -0.52191  1.000 11.01434 ? 79  ILE A CA   1 
ATOM   611  C  C    . ILE A 1 93  ? 57.42696 29.42996 0.12234   1.000 9.91373  ? 79  ILE A C    1 
ATOM   612  O  O    . ILE A 1 93  ? 57.27893 29.97891 1.22104   1.000 9.87767  ? 79  ILE A O    1 
ATOM   613  C  CB   . ILE A 1 93  ? 56.50690 27.11877 -0.41299  1.000 14.42078 ? 79  ILE A CB   1 
ATOM   614  C  CG1  . ILE A 1 93  ? 55.18643 26.39711 -0.69004  1.000 14.66062 ? 79  ILE A CG1  1 
ATOM   615  C  CG2  . ILE A 1 93  ? 57.08379 26.75010 0.94658   1.000 11.08159 ? 79  ILE A CG2  1 
ATOM   616  C  CD1  . ILE A 1 93  ? 55.34663 24.90934 -0.90549  1.000 19.87359 ? 79  ILE A CD1  1 
ATOM   617  N  N    . LYS A 1 94  ? 58.57491 29.50390 -0.55175  1.000 11.52756 ? 80  LYS A N    1 
ATOM   618  C  CA   . LYS A 1 94  ? 59.68047 30.29115 -0.02064  1.000 10.21896 ? 80  LYS A CA   1 
ATOM   619  C  C    . LYS A 1 94  ? 59.31990 31.75892 0.07135   1.000 8.09856  ? 80  LYS A C    1 
ATOM   620  O  O    . LYS A 1 94  ? 59.77381 32.44198 0.98889   1.000 8.20573  ? 80  LYS A O    1 
ATOM   621  C  CB   . LYS A 1 94  ? 60.92438 30.10512 -0.88107  1.000 15.17142 ? 80  LYS A CB   1 
ATOM   622  C  CG   . LYS A 1 94  ? 61.30323 28.64298 -1.05141  1.000 24.61880 ? 80  LYS A CG   1 
ATOM   623  C  CD   . LYS A 1 94  ? 62.59762 28.49709 -1.81365  1.000 29.76272 ? 80  LYS A CD   1 
ATOM   624  C  CE   . LYS A 1 94  ? 63.73418 28.93790 -0.94809  1.000 30.34651 ? 80  LYS A CE   1 
ATOM   625  N  NZ   . LYS A 1 94  ? 63.74843 28.14515 0.31076   1.000 40.45262 ? 80  LYS A NZ   1 
ATOM   626  N  N    . ARG A 1 95  ? 58.51266 32.26176 -0.86915  1.000 9.37678  ? 81  ARG A N    1 
ATOM   627  C  CA   . ARG A 1 95  ? 58.10183 33.66126 -0.82190  1.000 7.37119  ? 81  ARG A CA   1 
ATOM   628  C  C    . ARG A 1 95  ? 57.29386 33.94350 0.43567   1.000 7.51411  ? 81  ARG A C    1 
ATOM   629  O  O    . ARG A 1 95  ? 57.55990 34.91486 1.15465   1.000 8.48197  ? 81  ARG A O    1 
ATOM   630  C  CB   . ARG A 1 95  ? 57.28773 34.01252 -2.07175  1.000 12.11359 ? 81  ARG A CB   1 
ATOM   631  C  CG   . ARG A 1 95  ? 56.99623 35.51135 -2.25347  1.000 10.20320 ? 81  ARG A CG   1 
ATOM   632  C  CD   . ARG A 1 95  ? 56.15283 35.76115 -3.51447  1.000 8.89339  ? 81  ARG A CD   1 
ATOM   633  N  NE   . ARG A 1 95  ? 54.77753 35.28950 -3.36230  1.000 13.42798 ? 81  ARG A NE   1 
ATOM   634  C  CZ   . ARG A 1 95  ? 53.85411 35.34596 -4.31505  1.000 14.83855 ? 81  ARG A CZ   1 
ATOM   635  N  NH1  . ARG A 1 95  ? 54.14328 35.77417 -5.53559  1.000 12.75712 ? 81  ARG A NH1  1 
ATOM   636  N  NH2  . ARG A 1 95  ? 52.61183 34.96109 -4.03818  1.000 13.00978 ? 81  ARG A NH2  1 
ATOM   637  N  N    . GLU A 1 96  ? 56.30456 33.08520 0.72847   1.000 5.61699  ? 82  GLU A N    1 
ATOM   638  C  CA   . GLU A 1 96  ? 55.47654 33.29301 1.91121   1.000 7.57442  ? 82  GLU A CA   1 
ATOM   639  C  C    . GLU A 1 96  ? 56.30849 33.17698 3.17901   1.000 8.45406  ? 82  GLU A C    1 
ATOM   640  O  O    . GLU A 1 96  ? 56.17017 33.99894 4.09452   1.000 7.83967  ? 82  GLU A O    1 
ATOM   641  C  CB   . GLU A 1 96  ? 54.29743 32.31093 1.92523   1.000 8.34053  ? 82  GLU A CB   1 
ATOM   642  C  CG   . GLU A 1 96  ? 53.38763 32.49264 3.15118   1.000 6.31874  ? 82  GLU A CG   1 
ATOM   643  C  CD   . GLU A 1 96  ? 52.11305 31.65040 3.10008   1.000 11.81314 ? 82  GLU A CD   1 
ATOM   644  O  OE1  . GLU A 1 96  ? 51.91459 30.91998 2.10905   1.000 10.95000 ? 82  GLU A OE1  1 
ATOM   645  O  OE2  . GLU A 1 96  ? 51.30482 31.72417 4.05630   1.000 13.49505 ? 82  GLU A OE2  1 
ATOM   646  N  N    . ILE A 1 97  ? 57.20737 32.18686 3.22975   1.000 10.43022 ? 83  ILE A N    1 
ATOM   647  C  CA   . ILE A 1 97  ? 58.04728 31.97712 4.41143   1.000 8.66454  ? 83  ILE A CA   1 
ATOM   648  C  C    . ILE A 1 97  ? 58.95655 33.17759 4.65273   1.000 7.86076  ? 83  ILE A C    1 
ATOM   649  O  O    . ILE A 1 97  ? 59.09732 33.64827 5.78672   1.000 7.15751  ? 83  ILE A O    1 
ATOM   650  C  CB   . ILE A 1 97  ? 58.85337 30.66782 4.28409   1.000 6.50115  ? 83  ILE A CB   1 
ATOM   651  C  CG1  . ILE A 1 97  ? 57.93953 29.44364 4.45548   1.000 7.89513  ? 83  ILE A CG1  1 
ATOM   652  C  CG2  . ILE A 1 97  ? 60.01299 30.64932 5.27288   1.000 9.75703  ? 83  ILE A CG2  1 
ATOM   653  C  CD1  . ILE A 1 97  ? 58.61769 28.10799 4.12059   1.000 11.54017 ? 83  ILE A CD1  1 
ATOM   654  N  N    . LYS A 1 98  ? 59.59879 33.68209 3.59571   1.000 6.76129  ? 84  LYS A N    1 
ATOM   655  C  CA   . LYS A 1 98  ? 60.52290 34.80569 3.76507   1.000 6.50251  ? 84  LYS A CA   1 
ATOM   656  C  C    . LYS A 1 98  ? 59.78062 36.07462 4.15555   1.000 6.51641  ? 84  LYS A C    1 
ATOM   657  O  O    . LYS A 1 98  ? 60.25644 36.85517 4.98785   1.000 9.27945  ? 84  LYS A O    1 
ATOM   658  C  CB   . LYS A 1 98  ? 61.32401 35.02801 2.48120   1.000 6.79249  ? 84  LYS A CB   1 
ATOM   659  C  CG   . LYS A 1 98  ? 62.36854 36.15400 2.58920   1.000 10.25086 ? 84  LYS A CG   1 
ATOM   660  C  CD   . LYS A 1 98  ? 63.34113 35.85409 3.72477   1.000 13.59173 ? 84  LYS A CD   1 
ATOM   661  C  CE   . LYS A 1 98  ? 64.49465 36.83972 3.75974   1.000 14.53340 ? 84  LYS A CE   1 
ATOM   662  N  NZ   . LYS A 1 98  ? 65.41948 36.49517 4.86465   1.000 18.81453 ? 84  LYS A NZ   1 
ATOM   663  N  N    . ILE A 1 99  ? 58.60656 36.29508 3.56772   1.000 7.47898  ? 85  ILE A N    1 
ATOM   664  C  CA   . ILE A 1 99  ? 57.80023 37.45498 3.92302   1.000 6.62367  ? 85  ILE A CA   1 
ATOM   665  C  C    . ILE A 1 99  ? 57.40656 37.39791 5.39494   1.000 8.41894  ? 85  ILE A C    1 
ATOM   666  O  O    . ILE A 1 99  ? 57.51533 38.39440 6.12039   1.000 7.72776  ? 85  ILE A O    1 
ATOM   667  C  CB   . ILE A 1 99  ? 56.58668 37.55538 2.97803   1.000 6.97067  ? 85  ILE A CB   1 
ATOM   668  C  CG1  . ILE A 1 99  ? 57.05485 38.09997 1.62912   1.000 6.19874  ? 85  ILE A CG1  1 
ATOM   669  C  CG2  . ILE A 1 99  ? 55.45275 38.39039 3.58670   1.000 5.27835  ? 85  ILE A CG2  1 
ATOM   670  C  CD1  . ILE A 1 99  ? 55.94730 38.16651 0.58324   1.000 6.91591  ? 85  ILE A CD1  1 
ATOM   671  N  N    . LEU A 1 100 ? 56.99001 36.22340 5.87153   1.000 6.50885  ? 86  LEU A N    1 
ATOM   672  C  CA   . LEU A 1 100 ? 56.64654 36.09374 7.28653   1.000 6.35495  ? 86  LEU A CA   1 
ATOM   673  C  C    . LEU A 1 100 ? 57.85929 36.34427 8.18373   1.000 10.84367 ? 86  LEU A C    1 
ATOM   674  O  O    . LEU A 1 100 ? 57.74612 37.01381 9.21935   1.000 11.19826 ? 86  LEU A O    1 
ATOM   675  C  CB   . LEU A 1 100 ? 56.02509 34.72317 7.54550   1.000 6.53507  ? 86  LEU A CB   1 
ATOM   676  C  CG   . LEU A 1 100 ? 54.58622 34.56811 7.04131   1.000 6.91581  ? 86  LEU A CG   1 
ATOM   677  C  CD1  . LEU A 1 100 ? 54.16397 33.09861 7.03481   1.000 9.48929  ? 86  LEU A CD1  1 
ATOM   678  C  CD2  . LEU A 1 100 ? 53.63743 35.41695 7.87402   1.000 10.82595 ? 86  LEU A CD2  1 
ATOM   679  N  N    . GLU A 1 101 ? 59.03199 35.83339 7.80227   1.000 10.76253 ? 87  GLU A N    1 
ATOM   680  C  CA   . GLU A 1 101 ? 60.24701 36.13960 8.55898   1.000 13.35239 ? 87  GLU A CA   1 
ATOM   681  C  C    . GLU A 1 101 ? 60.51456 37.64423 8.59998   1.000 8.53512  ? 87  GLU A C    1 
ATOM   682  O  O    . GLU A 1 101 ? 60.81325 38.20192 9.66003   1.000 9.69692  ? 87  GLU A O    1 
ATOM   683  C  CB   . GLU A 1 101 ? 61.45072 35.38152 7.98833   1.000 16.33242 ? 87  GLU A CB   1 
ATOM   684  C  CG   . GLU A 1 101 ? 62.80428 35.86077 8.53132   1.000 17.60464 ? 87  GLU A CG   1 
ATOM   685  C  CD   . GLU A 1 101 ? 63.99042 35.10849 7.93896   1.000 25.96122 ? 87  GLU A CD   1 
ATOM   686  O  OE1  . GLU A 1 101 ? 64.15050 33.90491 8.23513   1.000 29.59708 ? 87  GLU A OE1  1 
ATOM   687  O  OE2  . GLU A 1 101 ? 64.75624 35.72321 7.17005   1.000 29.36127 ? 87  GLU A OE2  1 
ATOM   688  N  N    . ASN A 1 102 ? 60.42244 38.32087 7.45210   1.000 8.05433  ? 88  ASN A N    1 
ATOM   689  C  CA   . ASN A 1 102 ? 60.67152 39.76090 7.43167   1.000 10.25717 ? 88  ASN A CA   1 
ATOM   690  C  C    . ASN A 1 102 ? 59.68327 40.53553 8.29320   1.000 8.42208  ? 88  ASN A C    1 
ATOM   691  O  O    . ASN A 1 102 ? 59.99192 41.64650 8.74337   1.000 11.54544 ? 88  ASN A O    1 
ATOM   692  C  CB   . ASN A 1 102 ? 60.62534 40.28461 5.99418   1.000 7.87077  ? 88  ASN A CB   1 
ATOM   693  C  CG   . ASN A 1 102 ? 61.80051 39.81746 5.18075   1.000 11.04097 ? 88  ASN A CG   1 
ATOM   694  O  OD1  . ASN A 1 102 ? 62.77890 39.31186 5.72870   1.000 11.29710 ? 88  ASN A OD1  1 
ATOM   695  N  ND2  . ASN A 1 102 ? 61.72556 39.99112 3.86752   1.000 8.93122  ? 88  ASN A ND2  1 
ATOM   696  N  N    . LEU A 1 103 ? 58.48970 39.98914 8.51121   1.000 6.73864  ? 89  LEU A N    1 
ATOM   697  C  CA   . LEU A 1 103 ? 57.42825 40.68127 9.23002   1.000 6.00351  ? 89  LEU A CA   1 
ATOM   698  C  C    . LEU A 1 103 ? 57.35498 40.28079 10.69323  1.000 10.32011 ? 89  LEU A C    1 
ATOM   699  O  O    . LEU A 1 103 ? 56.44082 40.72344 11.39640  1.000 13.74344 ? 89  LEU A O    1 
ATOM   700  C  CB   . LEU A 1 103 ? 56.07775 40.39826 8.56732   1.000 8.25971  ? 89  LEU A CB   1 
ATOM   701  C  CG   . LEU A 1 103 ? 55.89633 40.93043 7.14756   1.000 7.71908  ? 89  LEU A CG   1 
ATOM   702  C  CD1  . LEU A 1 103 ? 54.54474 40.49147 6.57161   1.000 10.92383 ? 89  LEU A CD1  1 
ATOM   703  C  CD2  . LEU A 1 103 ? 56.03112 42.44690 7.14748   1.000 9.80384  ? 89  LEU A CD2  1 
ATOM   704  N  N    . ARG A 1 104 ? 58.29129 39.46107 11.16485  1.000 7.89810  ? 90  ARG A N    1 
ATOM   705  C  CA   . ARG A 1 104 ? 58.21181 38.91387 12.51347  1.000 10.50743 ? 90  ARG A CA   1 
ATOM   706  C  C    . ARG A 1 104 ? 58.14820 40.02663 13.55390  1.000 10.46738 ? 90  ARG A C    1 
ATOM   707  O  O    . ARG A 1 104 ? 58.91040 40.99932 13.49928  1.000 16.03548 ? 90  ARG A O    1 
ATOM   708  C  CB   . ARG A 1 104 ? 59.43704 38.03473 12.76333  1.000 18.33274 ? 90  ARG A CB   1 
ATOM   709  C  CG   . ARG A 1 104 ? 59.41980 37.29922 14.08278  1.000 33.07425 ? 90  ARG A CG   1 
ATOM   710  C  CD   . ARG A 1 104 ? 60.78863 36.70336 14.39073  1.000 49.55760 ? 90  ARG A CD   1 
ATOM   711  N  NE   . ARG A 1 104 ? 60.85758 36.17275 15.74794  1.000 69.11987 ? 90  ARG A NE   1 
ATOM   712  C  CZ   . ARG A 1 104 ? 61.97522 36.05676 16.45289  1.000 60.04658 ? 90  ARG A CZ   1 
ATOM   713  N  NH1  . ARG A 1 104 ? 63.14553 36.43569 15.96263  1.000 50.59050 ? 90  ARG A NH1  1 
ATOM   714  N  NH2  . ARG A 1 104 ? 61.91611 35.55568 17.68376  1.000 67.50167 ? 90  ARG A NH2  1 
ATOM   715  N  N    . GLY A 1 105 ? 57.24358 39.87223 14.51743  1.000 10.66717 ? 91  GLY A N    1 
ATOM   716  C  CA   . GLY A 1 105 ? 57.04458 40.88129 15.53139  1.000 17.01704 ? 91  GLY A CA   1 
ATOM   717  C  C    . GLY A 1 105 ? 56.25932 42.09811 15.08966  1.000 14.24510 ? 91  GLY A C    1 
ATOM   718  O  O    . GLY A 1 105 ? 56.03628 42.99916 15.90901  1.000 15.22892 ? 91  GLY A O    1 
ATOM   719  N  N    . GLY A 1 106 ? 55.82196 42.15655 13.83517  1.000 15.60601 ? 92  GLY A N    1 
ATOM   720  C  CA   . GLY A 1 106 ? 55.04190 43.29602 13.38463  1.000 13.98776 ? 92  GLY A CA   1 
ATOM   721  C  C    . GLY A 1 106 ? 53.67830 43.34886 14.05624  1.000 8.90224  ? 92  GLY A C    1 
ATOM   722  O  O    . GLY A 1 106 ? 53.05294 42.32282 14.33062  1.000 10.51032 ? 92  GLY A O    1 
ATOM   723  N  N    . THR A 1 107 ? 53.21593 44.57279 14.31072  1.000 11.99344 ? 93  THR A N    1 
ATOM   724  C  CA   . THR A 1 107 ? 51.97152 44.79778 15.03121  1.000 11.17546 ? 93  THR A CA   1 
ATOM   725  C  C    . THR A 1 107 ? 50.78261 44.26748 14.24232  1.000 11.98249 ? 93  THR A C    1 
ATOM   726  O  O    . THR A 1 107 ? 50.54222 44.68034 13.10292  1.000 9.24012  ? 93  THR A O    1 
ATOM   727  C  CB   . THR A 1 107 ? 51.78690 46.29516 15.26474  1.000 14.77197 ? 93  THR A CB   1 
ATOM   728  O  OG1  . THR A 1 107 ? 52.95114 46.82006 15.91789  1.000 20.45159 ? 93  THR A OG1  1 
ATOM   729  C  CG2  . THR A 1 107 ? 50.57527 46.53467 16.13562  1.000 15.41435 ? 93  THR A CG2  1 
ATOM   730  N  N    . ASN A 1 108 ? 50.02271 43.37917 14.86951  1.000 9.66645  ? 94  ASN A N    1 
ATOM   731  C  CA   . ASN A 1 108 ? 48.80356 42.78088 14.33556  1.000 6.57107  ? 94  ASN A CA   1 
ATOM   732  C  C    . ASN A 1 108 ? 49.01843 41.89030 13.12232  1.000 7.23301  ? 94  ASN A C    1 
ATOM   733  O  O    . ASN A 1 108 ? 48.04710 41.54874 12.42514  1.000 9.57172  ? 94  ASN A O    1 
ATOM   734  C  CB   . ASN A 1 108 ? 47.69944 43.81822 14.11298  1.000 8.71017  ? 94  ASN A CB   1 
ATOM   735  C  CG   . ASN A 1 108 ? 47.28338 44.45478 15.41064  1.000 10.16535 ? 94  ASN A CG   1 
ATOM   736  O  OD1  . ASN A 1 108 ? 47.44732 43.84818 16.47454  1.000 11.89927 ? 94  ASN A OD1  1 
ATOM   737  N  ND2  . ASN A 1 108 ? 46.78909 45.68097 15.35145  1.000 11.69460 ? 94  ASN A ND2  1 
ATOM   738  N  N    . ILE A 1 109 ? 50.23600 41.49664 12.84540  1.000 7.97767  ? 95  ILE A N    1 
ATOM   739  C  CA   . ILE A 1 109 ? 50.48832 40.49071 11.82291  1.000 7.50063  ? 95  ILE A CA   1 
ATOM   740  C  C    . ILE A 1 109 ? 50.47478 39.12247 12.49224  1.000 8.91301  ? 95  ILE A C    1 
ATOM   741  O  O    . ILE A 1 109 ? 51.03529 38.94658 13.57453  1.000 9.02852  ? 95  ILE A O    1 
ATOM   742  C  CB   . ILE A 1 109 ? 51.81345 40.79392 11.09420  1.000 8.83552  ? 95  ILE A CB   1 
ATOM   743  C  CG1  . ILE A 1 109 ? 51.62276 42.09959 10.29493  1.000 14.32386 ? 95  ILE A CG1  1 
ATOM   744  C  CG2  . ILE A 1 109 ? 52.23957 39.61210 10.18617  1.000 8.00542  ? 95  ILE A CG2  1 
ATOM   745  C  CD1  . ILE A 1 109 ? 52.77983 42.51576 9.48151   1.000 18.53945 ? 95  ILE A CD1  1 
ATOM   746  N  N    . ILE A 1 110 ? 49.80407 38.15367 11.86288  1.000 6.32246  ? 96  ILE A N    1 
ATOM   747  C  CA   . ILE A 1 110 ? 49.69284 36.82275 12.44947  1.000 6.39923  ? 96  ILE A CA   1 
ATOM   748  C  C    . ILE A 1 110 ? 51.07911 36.28342 12.78616  1.000 8.66217  ? 96  ILE A C    1 
ATOM   749  O  O    . ILE A 1 110 ? 52.02147 36.41645 11.99866  1.000 11.43851 ? 96  ILE A O    1 
ATOM   750  C  CB   . ILE A 1 110 ? 48.90947 35.89424 11.50388  1.000 6.76569  ? 96  ILE A CB   1 
ATOM   751  C  CG1  . ILE A 1 110 ? 48.51371 34.60847 12.23929  1.000 7.00650  ? 96  ILE A CG1  1 
ATOM   752  C  CG2  . ILE A 1 110 ? 49.72746 35.57132 10.23339  1.000 6.62100  ? 96  ILE A CG2  1 
ATOM   753  C  CD1  . ILE A 1 110 ? 47.43522 34.82517 13.30241  1.000 7.02014  ? 96  ILE A CD1  1 
ATOM   754  N  N    . LYS A 1 111 ? 51.21645 35.71013 13.98252  1.000 9.14197  ? 97  LYS A N    1 
ATOM   755  C  CA   . LYS A 1 111 ? 52.50891 35.22359 14.45003  1.000 11.89501 ? 97  LYS A CA   1 
ATOM   756  C  C    . LYS A 1 111 ? 52.76842 33.83325 13.88594  1.000 12.11724 ? 97  LYS A C    1 
ATOM   757  O  O    . LYS A 1 111 ? 51.95113 32.92026 14.06566  1.000 10.10574 ? 97  LYS A O    1 
ATOM   758  C  CB   . LYS A 1 111 ? 52.55725 35.17111 15.97579  1.000 18.33540 ? 97  LYS A CB   1 
ATOM   759  C  CG   . LYS A 1 111 ? 53.88675 34.62446 16.49947  1.000 23.42978 ? 97  LYS A CG   1 
ATOM   760  C  CD   . LYS A 1 111 ? 54.05759 34.79010 18.00176  1.000 22.42502 ? 97  LYS A CD   1 
ATOM   761  C  CE   . LYS A 1 111 ? 52.95879 34.10943 18.78744  1.000 33.15470 ? 97  LYS A CE   1 
ATOM   762  N  NZ   . LYS A 1 111 ? 53.26029 34.10072 20.24900  1.000 58.93745 ? 97  LYS A NZ   1 
ATOM   763  N  N    . LEU A 1 112 ? 53.88862 33.67750 13.19128  1.000 7.65627  ? 98  LEU A N    1 
ATOM   764  C  CA   . LEU A 1 112 ? 54.34354 32.36477 12.74315  1.000 11.31311 ? 98  LEU A CA   1 
ATOM   765  C  C    . LEU A 1 112 ? 55.14478 31.71774 13.86938  1.000 9.50694  ? 98  LEU A C    1 
ATOM   766  O  O    . LEU A 1 112 ? 56.19400 32.23655 14.27157  1.000 16.10823 ? 98  LEU A O    1 
ATOM   767  C  CB   . LEU A 1 112 ? 55.17591 32.48076 11.46628  1.000 13.27036 ? 98  LEU A CB   1 
ATOM   768  C  CG   . LEU A 1 112 ? 55.78546 31.20602 10.86800  1.000 10.59637 ? 98  LEU A CG   1 
ATOM   769  C  CD1  . LEU A 1 112 ? 54.71338 30.33933 10.22596  1.000 6.71595  ? 98  LEU A CD1  1 
ATOM   770  C  CD2  . LEU A 1 112 ? 56.87393 31.51907 9.83572   1.000 8.91184  ? 98  LEU A CD2  1 
ATOM   771  N  N    . ILE A 1 113 ? 54.64677 30.59116 14.37249  1.000 10.98519 ? 99  ILE A N    1 
ATOM   772  C  CA   . ILE A 1 113 ? 55.25887 29.87147 15.48977  1.000 10.81729 ? 99  ILE A CA   1 
ATOM   773  C  C    . ILE A 1 113 ? 56.31893 28.88339 15.00866  1.000 8.86506  ? 99  ILE A C    1 
ATOM   774  O  O    . ILE A 1 113 ? 57.33889 28.68546 15.67118  1.000 11.62076 ? 99  ILE A O    1 
ATOM   775  C  CB   . ILE A 1 113 ? 54.13577 29.15483 16.27869  1.000 13.51937 ? 99  ILE A CB   1 
ATOM   776  C  CG1  . ILE A 1 113 ? 53.26377 30.15572 17.02783  1.000 16.02799 ? 99  ILE A CG1  1 
ATOM   777  C  CG2  . ILE A 1 113 ? 54.69384 28.05833 17.21998  1.000 15.84000 ? 99  ILE A CG2  1 
ATOM   778  C  CD1  . ILE A 1 113 ? 52.08235 29.50968 17.72153  1.000 14.38888 ? 99  ILE A CD1  1 
ATOM   779  N  N    . ASP A 1 114 ? 56.10862 28.24105 13.86221  1.000 8.01757  ? 100 ASP A N    1 
ATOM   780  C  CA   . ASP A 1 114 ? 56.98294 27.14654 13.45712  1.000 8.37355  ? 100 ASP A CA   1 
ATOM   781  C  C    . ASP A 1 114 ? 56.81727 26.89634 11.96768  1.000 9.33352  ? 100 ASP A C    1 
ATOM   782  O  O    . ASP A 1 114 ? 55.85042 27.34360 11.34139  1.000 10.08033 ? 100 ASP A O    1 
ATOM   783  C  CB   . ASP A 1 114 ? 56.68237 25.86425 14.25611  1.000 10.73285 ? 100 ASP A CB   1 
ATOM   784  C  CG   . ASP A 1 114 ? 57.93512 25.04389 14.56849  1.000 13.49942 ? 100 ASP A CG   1 
ATOM   785  O  OD1  . ASP A 1 114 ? 58.98141 25.23665 13.91094  1.000 12.86630 ? 100 ASP A OD1  1 
ATOM   786  O  OD2  . ASP A 1 114 ? 57.87330 24.18437 15.47630  1.000 13.25664 ? 100 ASP A OD2  1 
ATOM   787  N  N    . ILE A 1 115 ? 57.78806 26.17506 11.41309  1.000 8.71621  ? 101 ILE A N    1 
ATOM   788  C  CA   . ILE A 1 115 ? 57.77388 25.70152 10.03320  1.000 10.17511 ? 101 ILE A CA   1 
ATOM   789  C  C    . ILE A 1 115 ? 58.24626 24.25709 10.08664  1.000 10.40583 ? 101 ILE A C    1 
ATOM   790  O  O    . ILE A 1 115 ? 59.35309 23.98382 10.56630  1.000 11.33060 ? 101 ILE A O    1 
ATOM   791  C  CB   . ILE A 1 115 ? 58.70761 26.52469 9.12538   1.000 8.94270  ? 101 ILE A CB   1 
ATOM   792  C  CG1  . ILE A 1 115 ? 58.37627 28.01017 9.18397   1.000 9.11105  ? 101 ILE A CG1  1 
ATOM   793  C  CG2  . ILE A 1 115 ? 58.62333 26.04174 7.68233   1.000 12.06282 ? 101 ILE A CG2  1 
ATOM   794  C  CD1  . ILE A 1 115 ? 59.37373 28.85789 8.42405   1.000 14.32209 ? 101 ILE A CD1  1 
ATOM   795  N  N    . VAL A 1 116 ? 57.40705 23.32309 9.63491   1.000 9.83826  ? 102 VAL A N    1 
ATOM   796  C  CA   . VAL A 1 116 ? 57.71539 21.90286 9.75014   1.000 9.75365  ? 102 VAL A CA   1 
ATOM   797  C  C    . VAL A 1 116 ? 57.47787 21.20581 8.41610   1.000 9.11911  ? 102 VAL A C    1 
ATOM   798  O  O    . VAL A 1 116 ? 56.86752 21.75148 7.49622   1.000 9.42362  ? 102 VAL A O    1 
ATOM   799  C  CB   . VAL A 1 116 ? 56.91273 21.22201 10.87697  1.000 7.85522  ? 102 VAL A CB   1 
ATOM   800  C  CG1  . VAL A 1 116 ? 57.19872 21.91473 12.20883  1.000 11.71145 ? 102 VAL A CG1  1 
ATOM   801  C  CG2  . VAL A 1 116 ? 55.42099 21.25955 10.54660  1.000 8.43955  ? 102 VAL A CG2  1 
ATOM   802  N  N    . LYS A 1 117 ? 57.96842 19.97330 8.32088   1.000 11.90875 ? 103 LYS A N    1 
ATOM   803  C  CA   . LYS A 1 117 ? 57.65069 19.15827 7.16177   1.000 10.28057 ? 103 LYS A CA   1 
ATOM   804  C  C    . LYS A 1 117 ? 57.60228 17.68827 7.55141   1.000 12.52374 ? 103 LYS A C    1 
ATOM   805  O  O    . LYS A 1 117 ? 58.18629 17.26055 8.55437   1.000 11.86271 ? 103 LYS A O    1 
ATOM   806  C  CB   . LYS A 1 117 ? 58.63598 19.38588 6.00583   1.000 13.63367 ? 103 LYS A CB   1 
ATOM   807  C  CG   . LYS A 1 117 ? 60.06386 19.01090 6.32187   1.000 16.36219 ? 103 LYS A CG   1 
ATOM   808  C  CD   . LYS A 1 117 ? 61.00185 19.37577 5.16916   1.000 18.44709 ? 103 LYS A CD   1 
ATOM   809  C  CE   . LYS A 1 117 ? 62.46048 19.16480 5.58442   1.000 29.64290 ? 103 LYS A CE   1 
ATOM   810  N  NZ   . LYS A 1 117 ? 63.43300 19.48912 4.49462   1.000 30.02378 ? 103 LYS A NZ   1 
ATOM   811  N  N    . ASP A 1 118 ? 56.87974 16.92301 6.74936   1.000 11.53840 ? 104 ASP A N    1 
ATOM   812  C  CA   . ASP A 1 118 ? 56.89617 15.48013 6.86120   1.000 12.07311 ? 104 ASP A CA   1 
ATOM   813  C  C    . ASP A 1 118 ? 58.29709 15.00786 6.48864   1.000 12.96069 ? 104 ASP A C    1 
ATOM   814  O  O    . ASP A 1 118 ? 58.76124 15.29981 5.38418   1.000 12.15085 ? 104 ASP A O    1 
ATOM   815  C  CB   . ASP A 1 118 ? 55.84868 14.92989 5.88728   1.000 15.12055 ? 104 ASP A CB   1 
ATOM   816  C  CG   . ASP A 1 118 ? 55.69995 13.41615 5.94884   1.000 21.47378 ? 104 ASP A CG   1 
ATOM   817  O  OD1  . ASP A 1 118 ? 56.71886 12.69808 5.98740   1.000 19.32490 ? 104 ASP A OD1  1 
ATOM   818  O  OD2  . ASP A 1 118 ? 54.54139 12.93638 5.94227   1.000 19.17323 ? 104 ASP A OD2  1 
ATOM   819  N  N    . PRO A 1 119 ? 59.00734 14.30365 7.37124   1.000 14.71419 ? 105 PRO A N    1 
ATOM   820  C  CA   . PRO A 1 119 ? 60.38635 13.89458 7.04907   1.000 17.06235 ? 105 PRO A CA   1 
ATOM   821  C  C    . PRO A 1 119 ? 60.47877 12.95051 5.87413   1.000 21.29083 ? 105 PRO A C    1 
ATOM   822  O  O    . PRO A 1 119 ? 61.54907 12.85532 5.25643   1.000 18.90003 ? 105 PRO A O    1 
ATOM   823  C  CB   . PRO A 1 119 ? 60.87101 13.20604 8.33287   1.000 16.18552 ? 105 PRO A CB   1 
ATOM   824  C  CG   . PRO A 1 119 ? 59.86975 13.53604 9.38432   1.000 31.26211 ? 105 PRO A CG   1 
ATOM   825  C  CD   . PRO A 1 119 ? 58.57595 13.84645 8.70269   1.000 21.06364 ? 105 PRO A CD   1 
ATOM   826  N  N    . VAL A 1 120 ? 59.40249 12.24052 5.55010   1.000 15.90715 ? 106 VAL A N    1 
ATOM   827  C  CA   . VAL A 1 120 ? 59.43464 11.26484 4.47178   1.000 12.39674 ? 106 VAL A CA   1 
ATOM   828  C  C    . VAL A 1 120 ? 58.96897 11.87866 3.16108   1.000 17.87290 ? 106 VAL A C    1 
ATOM   829  O  O    . VAL A 1 120 ? 59.66513 11.80779 2.14645   1.000 15.19901 ? 106 VAL A O    1 
ATOM   830  C  CB   . VAL A 1 120 ? 58.59830 10.02642 4.85195   1.000 14.29500 ? 106 VAL A CB   1 
ATOM   831  C  CG1  . VAL A 1 120 ? 58.77800 8.94706  3.80829   1.000 13.03175 ? 106 VAL A CG1  1 
ATOM   832  C  CG2  . VAL A 1 120 ? 58.98185 9.51006  6.23784   1.000 19.49265 ? 106 VAL A CG2  1 
ATOM   833  N  N    . SER A 1 121 ? 57.79119 12.50210 3.15985   1.000 13.01516 ? 107 SER A N    1 
ATOM   834  C  CA   . SER A 1 121 ? 57.23507 13.05754 1.93110   1.000 16.21774 ? 107 SER A CA   1 
ATOM   835  C  C    . SER A 1 121 ? 57.75921 14.45022 1.62467   1.000 13.82138 ? 107 SER A C    1 
ATOM   836  O  O    . SER A 1 121 ? 57.66033 14.89069 0.47671   1.000 19.62372 ? 107 SER A O    1 
ATOM   837  C  CB   . SER A 1 121 ? 55.71521 13.14218 2.03069   1.000 14.14209 ? 107 SER A CB   1 
ATOM   838  O  OG   . SER A 1 121 ? 55.35242 14.20545 2.89511   1.000 14.75898 ? 107 SER A OG   1 
ATOM   839  N  N    . LYS A 1 122 ? 58.28147 15.15731 2.62428   1.000 12.82590 ? 108 LYS A N    1 
ATOM   840  C  CA   . LYS A 1 122 ? 58.81012 16.51414 2.51662   1.000 15.29959 ? 108 LYS A CA   1 
ATOM   841  C  C    . LYS A 1 122 ? 57.73725 17.58216 2.35315   1.000 16.41965 ? 108 LYS A C    1 
ATOM   842  O  O    . LYS A 1 122 ? 58.07221 18.73553 2.09188   1.000 16.96166 ? 108 LYS A O    1 
ATOM   843  C  CB   . LYS A 1 122 ? 59.89357 16.66261 1.43950   1.000 17.55873 ? 108 LYS A CB   1 
ATOM   844  C  CG   . LYS A 1 122 ? 60.93827 15.56073 1.45574   1.000 18.18184 ? 108 LYS A CG   1 
ATOM   845  C  CD   . LYS A 1 122 ? 61.63916 15.49215 2.79887   1.000 18.54728 ? 108 LYS A CD   1 
ATOM   846  C  CE   . LYS A 1 122 ? 62.73458 14.43699 2.78323   1.000 24.21214 ? 108 LYS A CE   1 
ATOM   847  N  NZ   . LYS A 1 122 ? 63.47333 14.39032 4.07124   1.000 30.38505 ? 108 LYS A NZ   1 
ATOM   848  N  N    . THR A 1 123 ? 56.46551 17.24059 2.51173   1.000 13.10379 ? 109 THR A N    1 
ATOM   849  C  CA   . THR A 1 123 ? 55.41456 18.24447 2.41020   1.000 12.12100 ? 109 THR A CA   1 
ATOM   850  C  C    . THR A 1 123 ? 55.54411 19.23069 3.56219   1.000 11.09316 ? 109 THR A C    1 
ATOM   851  O  O    . THR A 1 123 ? 55.58877 18.80905 4.72333   1.000 13.39819 ? 109 THR A O    1 
ATOM   852  C  CB   . THR A 1 123 ? 54.04848 17.57770 2.48554   1.000 14.24362 ? 109 THR A CB   1 
ATOM   853  O  OG1  . THR A 1 123 ? 53.91060 16.65356 1.40022   1.000 19.19694 ? 109 THR A OG1  1 
ATOM   854  C  CG2  . THR A 1 123 ? 52.93740 18.63808 2.40766   1.000 18.17901 ? 109 THR A CG2  1 
ATOM   855  N  N    . PRO A 1 124 ? 55.60449 20.53240 3.29012   1.000 12.98811 ? 110 PRO A N    1 
ATOM   856  C  CA   . PRO A 1 124 ? 55.80250 21.51819 4.35217   1.000 8.84413  ? 110 PRO A CA   1 
ATOM   857  C  C    . PRO A 1 124 ? 54.48549 22.06092 4.89640   1.000 7.45571  ? 110 PRO A C    1 
ATOM   858  O  O    . PRO A 1 124 ? 53.44547 22.03987 4.23702   1.000 10.56483 ? 110 PRO A O    1 
ATOM   859  C  CB   . PRO A 1 124 ? 56.57504 22.62668 3.62419   1.000 11.01531 ? 110 PRO A CB   1 
ATOM   860  C  CG   . PRO A 1 124 ? 56.03798 22.58081 2.23782   1.000 12.68351 ? 110 PRO A CG   1 
ATOM   861  C  CD   . PRO A 1 124 ? 55.74426 21.13355 1.94917   1.000 13.98179 ? 110 PRO A CD   1 
ATOM   862  N  N    . ALA A 1 125 ? 54.55384 22.54397 6.13289   1.000 8.31868  ? 111 ALA A N    1 
ATOM   863  C  CA   . ALA A 1 125 ? 53.41815 23.17430 6.79627   1.000 10.94843 ? 111 ALA A CA   1 
ATOM   864  C  C    . ALA A 1 125 ? 53.89280 24.35461 7.64089   1.000 9.43466  ? 111 ALA A C    1 
ATOM   865  O  O    . ALA A 1 125 ? 54.99334 24.33971 8.20638   1.000 10.80947 ? 111 ALA A O    1 
ATOM   866  C  CB   . ALA A 1 125 ? 52.63912 22.18085 7.67644   1.000 12.84765 ? 111 ALA A CB   1 
ATOM   867  N  N    . LEU A 1 126 ? 53.04996 25.38569 7.71712   1.000 6.29460  ? 112 LEU A N    1 
ATOM   868  C  CA   . LEU A 1 126 ? 53.30052 26.54611 8.55810   1.000 8.03819  ? 112 LEU A CA   1 
ATOM   869  C  C    . LEU A 1 126 ? 52.43374 26.42769 9.80263   1.000 10.71380 ? 112 LEU A C    1 
ATOM   870  O  O    . LEU A 1 126 ? 51.31332 25.92612 9.72884   1.000 9.80658  ? 112 LEU A O    1 
ATOM   871  C  CB   . LEU A 1 126 ? 52.92315 27.82748 7.81323   1.000 7.65294  ? 112 LEU A CB   1 
ATOM   872  C  CG   . LEU A 1 126 ? 53.63462 27.97280 6.45460   1.000 6.65868  ? 112 LEU A CG   1 
ATOM   873  C  CD1  . LEU A 1 126 ? 53.27465 29.28166 5.76243   1.000 7.78563  ? 112 LEU A CD1  1 
ATOM   874  C  CD2  . LEU A 1 126 ? 55.14705 27.84524 6.60947   1.000 10.68217 ? 112 LEU A CD2  1 
ATOM   875  N  N    . VAL A 1 127 ? 52.95875 26.87070 10.94438  1.000 8.84888  ? 113 VAL A N    1 
ATOM   876  C  CA   . VAL A 1 127 ? 52.24546 26.82070 12.21912  1.000 8.12964  ? 113 VAL A CA   1 
ATOM   877  C  C    . VAL A 1 127 ? 52.10653 28.24593 12.73808  1.000 9.49780  ? 113 VAL A C    1 
ATOM   878  O  O    . VAL A 1 127 ? 53.11012 28.95383 12.89877  1.000 9.84324  ? 113 VAL A O    1 
ATOM   879  C  CB   . VAL A 1 127 ? 52.96489 25.93596 13.24860  1.000 8.23033  ? 113 VAL A CB   1 
ATOM   880  C  CG1  . VAL A 1 127 ? 52.10094 25.80130 14.50106  1.000 10.37291 ? 113 VAL A CG1  1 
ATOM   881  C  CG2  . VAL A 1 127 ? 53.30755 24.55705 12.66480  1.000 9.75311  ? 113 VAL A CG2  1 
ATOM   882  N  N    . PHE A 1 128 ? 50.86964 28.66678 12.99949  1.000 9.15266  ? 114 PHE A N    1 
ATOM   883  C  CA   . PHE A 1 128 ? 50.55247 30.02759 13.41804  1.000 9.63092  ? 114 PHE A CA   1 
ATOM   884  C  C    . PHE A 1 128 ? 49.83918 30.02113 14.76310  1.000 8.33087  ? 114 PHE A C    1 
ATOM   885  O  O    . PHE A 1 128 ? 49.27387 29.01055 15.18480  1.000 9.43293  ? 114 PHE A O    1 
ATOM   886  C  CB   . PHE A 1 128 ? 49.58360 30.69020 12.43086  1.000 6.32772  ? 114 PHE A CB   1 
ATOM   887  C  CG   . PHE A 1 128 ? 50.11144 30.80890 11.03168  1.000 6.09585  ? 114 PHE A CG   1 
ATOM   888  C  CD1  . PHE A 1 128 ? 50.92706 31.87389 10.67307  1.000 6.22980  ? 114 PHE A CD1  1 
ATOM   889  C  CD2  . PHE A 1 128 ? 49.77102 29.87299 10.07109  1.000 8.31920  ? 114 PHE A CD2  1 
ATOM   890  C  CE1  . PHE A 1 128 ? 51.40122 31.99613 9.37072   1.000 7.11785  ? 114 PHE A CE1  1 
ATOM   891  C  CE2  . PHE A 1 128 ? 50.24078 29.98460 8.78128   1.000 11.29769 ? 114 PHE A CE2  1 
ATOM   892  C  CZ   . PHE A 1 128 ? 51.04831 31.05529 8.43082   1.000 7.19776  ? 114 PHE A CZ   1 
ATOM   893  N  N    . GLU A 1 129 ? 49.82279 31.18337 15.41454  1.000 11.78902 ? 115 GLU A N    1 
ATOM   894  C  CA   . GLU A 1 129 ? 49.02896 31.33905 16.62616  1.000 13.47499 ? 115 GLU A CA   1 
ATOM   895  C  C    . GLU A 1 129 ? 47.54230 31.21024 16.30256  1.000 10.81584 ? 115 GLU A C    1 
ATOM   896  O  O    . GLU A 1 129 ? 47.10495 31.46534 15.17546  1.000 11.68690 ? 115 GLU A O    1 
ATOM   897  C  CB   . GLU A 1 129 ? 49.29756 32.70488 17.25341  1.000 15.02094 ? 115 GLU A CB   1 
ATOM   898  C  CG   . GLU A 1 129 ? 48.86519 33.83680 16.37269  1.000 9.83990  ? 115 GLU A CG   1 
ATOM   899  C  CD   . GLU A 1 129 ? 49.15674 35.20181 16.96067  1.000 16.58705 ? 115 GLU A CD   1 
ATOM   900  O  OE1  . GLU A 1 129 ? 49.29120 35.31410 18.19973  1.000 17.70095 ? 115 GLU A OE1  1 
ATOM   901  O  OE2  . GLU A 1 129 ? 49.25845 36.15931 16.17533  1.000 13.15475 ? 115 GLU A OE2  1 
ATOM   902  N  N    . TYR A 1 130 ? 46.76369 30.77340 17.29915  1.000 10.49474 ? 116 TYR A N    1 
ATOM   903  C  CA   . TYR A 1 130 ? 45.32577 30.58167 17.15312  1.000 13.27770 ? 116 TYR A CA   1 
ATOM   904  C  C    . TYR A 1 130 ? 44.60957 31.82999 17.65346  1.000 16.79023 ? 116 TYR A C    1 
ATOM   905  O  O    . TYR A 1 130 ? 44.84443 32.27424 18.78002  1.000 15.93036 ? 116 TYR A O    1 
ATOM   906  C  CB   . TYR A 1 130 ? 44.83374 29.35803 17.93888  1.000 15.52999 ? 116 TYR A CB   1 
ATOM   907  C  CG   . TYR A 1 130 ? 43.37272 28.99628 17.67366  1.000 17.95367 ? 116 TYR A CG   1 
ATOM   908  C  CD1  . TYR A 1 130 ? 42.33909 29.55934 18.41999  1.000 20.98036 ? 116 TYR A CD1  1 
ATOM   909  C  CD2  . TYR A 1 130 ? 43.03395 28.09784 16.66326  1.000 22.36897 ? 116 TYR A CD2  1 
ATOM   910  C  CE1  . TYR A 1 130 ? 41.00492 29.23807 18.16138  1.000 23.57752 ? 116 TYR A CE1  1 
ATOM   911  C  CE2  . TYR A 1 130 ? 41.70838 27.76758 16.39593  1.000 22.11830 ? 116 TYR A CE2  1 
ATOM   912  C  CZ   . TYR A 1 130 ? 40.69841 28.33811 17.14714  1.000 30.08966 ? 116 TYR A CZ   1 
ATOM   913  O  OH   . TYR A 1 130 ? 39.39091 27.99643 16.87366  1.000 25.27210 ? 116 TYR A OH   1 
ATOM   914  N  N    . ILE A 1 131 ? 43.74546 32.39216 16.81398  1.000 11.71472 ? 117 ILE A N    1 
ATOM   915  C  CA   . ILE A 1 131 ? 42.91836 33.54051 17.17316  1.000 12.43703 ? 117 ILE A CA   1 
ATOM   916  C  C    . ILE A 1 131 ? 41.47133 33.07047 17.24411  1.000 12.35841 ? 117 ILE A C    1 
ATOM   917  O  O    . ILE A 1 131 ? 40.96778 32.45899 16.29949  1.000 14.38836 ? 117 ILE A O    1 
ATOM   918  C  CB   . ILE A 1 131 ? 43.07238 34.67683 16.14659  1.000 13.53674 ? 117 ILE A CB   1 
ATOM   919  C  CG1  . ILE A 1 131 ? 44.54942 35.02920 15.95596  1.000 17.73480 ? 117 ILE A CG1  1 
ATOM   920  C  CG2  . ILE A 1 131 ? 42.25066 35.88593 16.56376  1.000 13.04625 ? 117 ILE A CG2  1 
ATOM   921  C  CD1  . ILE A 1 131 ? 45.26352 35.45593 17.22740  1.000 18.53527 ? 117 ILE A CD1  1 
ATOM   922  N  N    . ASN A 1 132 ? 40.80207 33.35097 18.36555  1.000 11.19845 ? 118 ASN A N    1 
ATOM   923  C  CA   . ASN A 1 132 ? 39.40709 32.94961 18.55667  1.000 11.87906 ? 118 ASN A CA   1 
ATOM   924  C  C    . ASN A 1 132 ? 38.53678 33.97518 17.83315  1.000 17.29771 ? 118 ASN A C    1 
ATOM   925  O  O    . ASN A 1 132 ? 37.98706 34.90929 18.41978  1.000 20.44098 ? 118 ASN A O    1 
ATOM   926  C  CB   . ASN A 1 132 ? 39.08760 32.84945 20.04931  1.000 12.99308 ? 118 ASN A CB   1 
ATOM   927  C  CG   . ASN A 1 132 ? 37.69477 32.29779 20.32815  1.000 15.45846 ? 118 ASN A CG   1 
ATOM   928  O  OD1  . ASN A 1 132 ? 37.04443 31.71864 19.45198  1.000 21.57274 ? 118 ASN A OD1  1 
ATOM   929  N  ND2  . ASN A 1 132 ? 37.23412 32.46945 21.56526  1.000 25.48202 ? 118 ASN A ND2  1 
ATOM   930  N  N    . ASN A 1 133 ? 38.39881 33.76309 16.52651  1.000 16.64111 ? 119 ASN A N    1 
ATOM   931  C  CA   . ASN A 1 133 ? 37.78436 34.71328 15.60619  1.000 17.75617 ? 119 ASN A CA   1 
ATOM   932  C  C    . ASN A 1 133 ? 36.26584 34.71688 15.72647  1.000 17.83883 ? 119 ASN A C    1 
ATOM   933  O  O    . ASN A 1 133 ? 35.63442 33.67085 15.90283  1.000 17.51517 ? 119 ASN A O    1 
ATOM   934  C  CB   . ASN A 1 133 ? 38.14546 34.27766 14.18550  1.000 23.69343 ? 119 ASN A CB   1 
ATOM   935  C  CG   . ASN A 1 133 ? 37.46576 35.09889 13.11244  1.000 33.71316 ? 119 ASN A CG   1 
ATOM   936  O  OD1  . ASN A 1 133 ? 37.71467 36.30149 12.96752  1.000 35.22297 ? 119 ASN A OD1  1 
ATOM   937  N  ND2  . ASN A 1 133 ? 36.62639 34.44172 12.32255  1.000 20.27093 ? 119 ASN A ND2  1 
ATOM   938  N  N    . THR A 1 134 ? 35.67989 35.90199 15.60568  1.000 14.55239 ? 120 THR A N    1 
ATOM   939  C  CA   . THR A 1 134 ? 34.23965 36.05201 15.44506  1.000 16.64005 ? 120 THR A CA   1 
ATOM   940  C  C    . THR A 1 134 ? 33.95977 36.18735 13.95228  1.000 19.81491 ? 120 THR A C    1 
ATOM   941  O  O    . THR A 1 134 ? 34.53057 37.06511 13.28815  1.000 20.46660 ? 120 THR A O    1 
ATOM   942  C  CB   . THR A 1 134 ? 33.73690 37.29376 16.18546  1.000 31.49690 ? 120 THR A CB   1 
ATOM   943  O  OG1  . THR A 1 134 ? 34.12212 37.23788 17.56708  1.000 35.87219 ? 120 THR A OG1  1 
ATOM   944  C  CG2  . THR A 1 134 ? 32.22738 37.39071 16.08712  1.000 34.23859 ? 120 THR A CG2  1 
ATOM   945  N  N    . ASP A 1 135 ? 33.09602 35.31674 13.43382  1.000 18.21781 ? 121 ASP A N    1 
ATOM   946  C  CA   . ASP A 1 135 ? 32.74352 35.32219 12.01991  1.000 24.99830 ? 121 ASP A CA   1 
ATOM   947  C  C    . ASP A 1 135 ? 32.27049 36.70605 11.59557  1.000 18.27535 ? 121 ASP A C    1 
ATOM   948  O  O    . ASP A 1 135 ? 31.35789 37.28008 12.19984  1.000 17.64183 ? 121 ASP A O    1 
ATOM   949  C  CB   . ASP A 1 135 ? 31.62917 34.29866 11.79307  1.000 34.54268 ? 121 ASP A CB   1 
ATOM   950  C  CG   . ASP A 1 135 ? 31.29768 34.11136 10.32987  1.000 55.37889 ? 121 ASP A CG   1 
ATOM   951  O  OD1  . ASP A 1 135 ? 32.21408 33.75913 9.55511   1.000 64.10427 ? 121 ASP A OD1  1 
ATOM   952  O  OD2  . ASP A 1 135 ? 30.11915 34.30842 9.95881   1.000 66.12541 ? 121 ASP A OD2  1 
ATOM   953  N  N    . PHE A 1 136 ? 32.89348 37.23905 10.54417  1.000 20.34038 ? 122 PHE A N    1 
ATOM   954  C  CA   . PHE A 1 136 ? 32.63925 38.62792 10.17662  1.000 18.59572 ? 122 PHE A CA   1 
ATOM   955  C  C    . PHE A 1 136 ? 31.19561 38.85755 9.73982   1.000 18.81207 ? 122 PHE A C    1 
ATOM   956  O  O    . PHE A 1 136 ? 30.65818 39.94837 9.95112   1.000 18.06096 ? 122 PHE A O    1 
ATOM   957  C  CB   . PHE A 1 136 ? 33.65335 39.11331 9.12904   1.000 22.23835 ? 122 PHE A CB   1 
ATOM   958  C  CG   . PHE A 1 136 ? 33.49194 38.48211 7.76920   1.000 20.75760 ? 122 PHE A CG   1 
ATOM   959  C  CD1  . PHE A 1 136 ? 32.66482 39.06626 6.81241   1.000 26.51819 ? 122 PHE A CD1  1 
ATOM   960  C  CD2  . PHE A 1 136 ? 34.17841 37.31515 7.43940   1.000 17.64708 ? 122 PHE A CD2  1 
ATOM   961  C  CE1  . PHE A 1 136 ? 32.51346 38.49563 5.55265   1.000 23.61448 ? 122 PHE A CE1  1 
ATOM   962  C  CE2  . PHE A 1 136 ? 34.04431 36.74739 6.17495   1.000 17.86408 ? 122 PHE A CE2  1 
ATOM   963  C  CZ   . PHE A 1 136 ? 33.20762 37.33643 5.23522   1.000 20.41334 ? 122 PHE A CZ   1 
ATOM   964  N  N    . LYS A 1 137 ? 30.54728 37.85053 9.14596   1.000 15.73505 ? 123 LYS A N    1 
ATOM   965  C  CA   . LYS A 1 137 ? 29.15015 38.01352 8.75141   1.000 24.58145 ? 123 LYS A CA   1 
ATOM   966  C  C    . LYS A 1 137 ? 28.27379 38.36712 9.94936   1.000 28.93233 ? 123 LYS A C    1 
ATOM   967  O  O    . LYS A 1 137 ? 27.39990 39.23675 9.85607   1.000 32.26523 ? 123 LYS A O    1 
ATOM   968  C  CB   . LYS A 1 137 ? 28.64559 36.75056 8.05260   1.000 30.93785 ? 123 LYS A CB   1 
ATOM   969  C  CG   . LYS A 1 137 ? 29.00281 36.67405 6.57740   1.000 33.53650 ? 123 LYS A CG   1 
ATOM   970  C  CD   . LYS A 1 137 ? 28.37374 37.83423 5.82278   1.000 34.67135 ? 123 LYS A CD   1 
ATOM   971  C  CE   . LYS A 1 137 ? 28.57568 37.72140 4.32268   1.000 37.74666 ? 123 LYS A CE   1 
ATOM   972  N  NZ   . LYS A 1 137 ? 27.92529 38.86665 3.61928   1.000 38.13838 ? 123 LYS A NZ   1 
ATOM   973  N  N    . GLN A 1 138 ? 28.51049 37.72164 11.08899  1.000 24.30670 ? 124 GLN A N    1 
ATOM   974  C  CA   . GLN A 1 138 ? 27.79439 38.07181 12.31007  1.000 19.26793 ? 124 GLN A CA   1 
ATOM   975  C  C    . GLN A 1 138 ? 28.34029 39.35394 12.93195  1.000 31.47807 ? 124 GLN A C    1 
ATOM   976  O  O    . GLN A 1 138 ? 27.56653 40.22848 13.33651  1.000 32.83678 ? 124 GLN A O    1 
ATOM   977  C  CB   . GLN A 1 138 ? 27.90893 36.92677 13.31794  1.000 32.57658 ? 124 GLN A CB   1 
ATOM   978  C  CG   . GLN A 1 138 ? 27.77861 35.53723 12.70904  1.000 43.26459 ? 124 GLN A CG   1 
ATOM   979  C  CD   . GLN A 1 138 ? 26.47410 35.34679 11.96162  1.000 50.06862 ? 124 GLN A CD   1 
ATOM   980  O  OE1  . GLN A 1 138 ? 26.45985 34.85474 10.83039  1.000 52.69314 ? 124 GLN A OE1  1 
ATOM   981  N  NE2  . GLN A 1 138 ? 25.36700 35.73199 12.59143  1.000 64.71365 ? 124 GLN A NE2  1 
ATOM   982  N  N    . LEU A 1 139 ? 29.66841 39.48681 12.99315  1.000 21.72304 ? 125 LEU A N    1 
ATOM   983  C  CA   . LEU A 1 139 ? 30.29350 40.60572 13.69330  1.000 17.26514 ? 125 LEU A CA   1 
ATOM   984  C  C    . LEU A 1 139 ? 29.91341 41.94362 13.07348  1.000 19.31466 ? 125 LEU A C    1 
ATOM   985  O  O    . LEU A 1 139 ? 29.54558 42.88410 13.78621  1.000 20.43863 ? 125 LEU A O    1 
ATOM   986  C  CB   . LEU A 1 139 ? 31.80993 40.43418 13.65534  1.000 20.22343 ? 125 LEU A CB   1 
ATOM   987  C  CG   . LEU A 1 139 ? 32.69023 41.46728 14.35344  1.000 23.49669 ? 125 LEU A CG   1 
ATOM   988  C  CD1  . LEU A 1 139 ? 32.56131 41.34699 15.85016  1.000 22.87658 ? 125 LEU A CD1  1 
ATOM   989  C  CD2  . LEU A 1 139 ? 34.13193 41.26633 13.93869  1.000 19.80144 ? 125 LEU A CD2  1 
ATOM   990  N  N    . TYR A 1 140 ? 30.00455 42.05207 11.74117  1.000 19.50017 ? 126 TYR A N    1 
ATOM   991  C  CA   . TYR A 1 140 ? 29.89003 43.35768 11.09402  1.000 21.20888 ? 126 TYR A CA   1 
ATOM   992  C  C    . TYR A 1 140 ? 28.51851 43.97989 11.27919  1.000 34.54982 ? 126 TYR A C    1 
ATOM   993  O  O    . TYR A 1 140 ? 28.35655 45.17779 11.02947  1.000 37.65147 ? 126 TYR A O    1 
ATOM   994  C  CB   . TYR A 1 140 ? 30.22294 43.29021 9.59991   1.000 14.99522 ? 126 TYR A CB   1 
ATOM   995  C  CG   . TYR A 1 140 ? 31.70079 43.10543 9.26853   1.000 21.47257 ? 126 TYR A CG   1 
ATOM   996  C  CD1  . TYR A 1 140 ? 32.60095 42.62503 10.21734  1.000 18.73561 ? 126 TYR A CD1  1 
ATOM   997  C  CD2  . TYR A 1 140 ? 32.19473 43.41537 8.00085   1.000 15.48301 ? 126 TYR A CD2  1 
ATOM   998  C  CE1  . TYR A 1 140 ? 33.94303 42.44928 9.90965   1.000 24.74740 ? 126 TYR A CE1  1 
ATOM   999  C  CE2  . TYR A 1 140 ? 33.53137 43.24817 7.69381   1.000 19.12046 ? 126 TYR A CE2  1 
ATOM   1000 C  CZ   . TYR A 1 140 ? 34.39971 42.76314 8.64992   1.000 16.33879 ? 126 TYR A CZ   1 
ATOM   1001 O  OH   . TYR A 1 140 ? 35.74373 42.59741 8.34552   1.000 21.31174 ? 126 TYR A OH   1 
ATOM   1002 N  N    . GLN A 1 141 ? 27.53237 43.20204 11.70658  1.000 23.18668 ? 127 GLN A N    1 
ATOM   1003 C  CA   . GLN A 1 141 ? 26.19388 43.72547 11.90920  1.000 28.81577 ? 127 GLN A CA   1 
ATOM   1004 C  C    . GLN A 1 141 ? 25.97870 44.28293 13.30960  1.000 22.40973 ? 127 GLN A C    1 
ATOM   1005 O  O    . GLN A 1 141 ? 24.93337 44.88834 13.55802  1.000 27.24972 ? 127 GLN A O    1 
ATOM   1006 C  CB   . GLN A 1 141 ? 25.15218 42.63676 11.59211  1.000 25.59857 ? 127 GLN A CB   1 
ATOM   1007 C  CG   . GLN A 1 141 ? 24.01051 43.09698 10.68203  1.000 50.17531 ? 127 GLN A CG   1 
ATOM   1008 C  CD   . GLN A 1 141 ? 24.47257 43.54453 9.29472   1.000 46.11512 ? 127 GLN A CD   1 
ATOM   1009 O  OE1  . GLN A 1 141 ? 25.50802 43.10458 8.78997   1.000 61.83685 ? 127 GLN A OE1  1 
ATOM   1010 N  NE2  . GLN A 1 141 ? 23.69591 44.42553 8.67424   1.000 28.76142 ? 127 GLN A NE2  1 
ATOM   1011 N  N    . ILE A 1 142 ? 26.93215 44.10967 14.22694  1.000 20.10279 ? 128 ILE A N    1 
ATOM   1012 C  CA   . ILE A 1 142 ? 26.73802 44.53934 15.61054  1.000 22.78132 ? 128 ILE A CA   1 
ATOM   1013 C  C    . ILE A 1 142 ? 27.88281 45.41115 16.13243  1.000 15.20376 ? 128 ILE A C    1 
ATOM   1014 O  O    . ILE A 1 142 ? 27.97441 45.66980 17.33935  1.000 20.42820 ? 128 ILE A O    1 
ATOM   1015 C  CB   . ILE A 1 142 ? 26.48624 43.33624 16.53508  1.000 28.73089 ? 128 ILE A CB   1 
ATOM   1016 C  CG1  . ILE A 1 142 ? 27.75859 42.49822 16.67959  1.000 24.54999 ? 128 ILE A CG1  1 
ATOM   1017 C  CG2  . ILE A 1 142 ? 25.33352 42.49244 16.00339  1.000 24.06018 ? 128 ILE A CG2  1 
ATOM   1018 C  CD1  . ILE A 1 142 ? 28.26036 42.39249 18.11010  1.000 32.72800 ? 128 ILE A CD1  1 
ATOM   1019 N  N    . LEU A 1 143 ? 28.75693 45.87074 15.24338  1.000 20.03819 ? 129 LEU A N    1 
ATOM   1020 C  CA   . LEU A 1 143 ? 29.83085 46.76095 15.66404  1.000 12.09931 ? 129 LEU A CA   1 
ATOM   1021 C  C    . LEU A 1 143 ? 29.26927 48.14503 15.95426  1.000 16.46411 ? 129 LEU A C    1 
ATOM   1022 O  O    . LEU A 1 143 ? 28.36852 48.61973 15.25915  1.000 17.35693 ? 129 LEU A O    1 
ATOM   1023 C  CB   . LEU A 1 143 ? 30.87718 46.87044 14.55690  1.000 13.66861 ? 129 LEU A CB   1 
ATOM   1024 C  CG   . LEU A 1 143 ? 31.60079 45.57217 14.22747  1.000 15.13369 ? 129 LEU A CG   1 
ATOM   1025 C  CD1  . LEU A 1 143 ? 32.25916 45.67342 12.88420  1.000 16.08377 ? 129 LEU A CD1  1 
ATOM   1026 C  CD2  . LEU A 1 143 ? 32.62987 45.25976 15.30190  1.000 14.05254 ? 129 LEU A CD2  1 
ATOM   1027 N  N    . THR A 1 144 ? 29.79707 48.78810 16.99429  1.000 13.15246 ? 130 THR A N    1 
ATOM   1028 C  CA   . THR A 1 144 ? 29.47947 50.17816 17.26919  1.000 10.50162 ? 130 THR A CA   1 
ATOM   1029 C  C    . THR A 1 144 ? 30.38712 51.08714 16.43740  1.000 10.91207 ? 130 THR A C    1 
ATOM   1030 O  O    . THR A 1 144 ? 31.34440 50.64035 15.80898  1.000 9.27949  ? 130 THR A O    1 
ATOM   1031 C  CB   . THR A 1 144 ? 29.73756 50.49181 18.73940  1.000 13.32867 ? 130 THR A CB   1 
ATOM   1032 O  OG1  . THR A 1 144 ? 31.14906 50.41574 18.98603  1.000 11.76090 ? 130 THR A OG1  1 
ATOM   1033 C  CG2  . THR A 1 144 ? 29.01372 49.49214 19.63354  1.000 13.97586 ? 130 THR A CG2  1 
ATOM   1034 N  N    . ASP A 1 145 ? 30.07622 52.38569 16.45138  1.000 7.69702  ? 131 ASP A N    1 
ATOM   1035 C  CA   . ASP A 1 145 ? 30.91610 53.38033 15.77885  1.000 8.15275  ? 131 ASP A CA   1 
ATOM   1036 C  C    . ASP A 1 145 ? 32.35263 53.32184 16.28848  1.000 9.98271  ? 131 ASP A C    1 
ATOM   1037 O  O    . ASP A 1 145 ? 33.30976 53.30800 15.50071  1.000 10.21229 ? 131 ASP A O    1 
ATOM   1038 C  CB   . ASP A 1 145 ? 30.30458 54.77431 15.98280  1.000 8.85156  ? 131 ASP A CB   1 
ATOM   1039 C  CG   . ASP A 1 145 ? 31.18485 55.91562 15.45058  1.000 14.12911 ? 131 ASP A CG   1 
ATOM   1040 O  OD1  . ASP A 1 145 ? 31.83761 55.76488 14.40368  1.000 10.52704 ? 131 ASP A OD1  1 
ATOM   1041 O  OD2  . ASP A 1 145 ? 31.19790 56.99790 16.07228  1.000 16.61504 ? 131 ASP A OD2  1 
ATOM   1042 N  N    . PHE A 1 146 ? 32.52555 53.27327 17.61088  1.000 8.02263  ? 132 PHE A N    1 
ATOM   1043 C  CA   . PHE A 1 146 ? 33.87066 53.15951 18.16289  1.000 8.09252  ? 132 PHE A CA   1 
ATOM   1044 C  C    . PHE A 1 146 ? 34.55901 51.86323 17.73355  1.000 8.90279  ? 132 PHE A C    1 
ATOM   1045 O  O    . PHE A 1 146 ? 35.74583 51.88564 17.38650  1.000 8.67324  ? 132 PHE A O    1 
ATOM   1046 C  CB   . PHE A 1 146 ? 33.86743 53.29285 19.69004  1.000 9.85730  ? 132 PHE A CB   1 
ATOM   1047 C  CG   . PHE A 1 146 ? 35.24517 53.25877 20.28035  1.000 8.72235  ? 132 PHE A CG   1 
ATOM   1048 C  CD1  . PHE A 1 146 ? 35.99245 54.42160 20.38406  1.000 14.30990 ? 132 PHE A CD1  1 
ATOM   1049 C  CD2  . PHE A 1 146 ? 35.81676 52.05702 20.67169  1.000 12.09318 ? 132 PHE A CD2  1 
ATOM   1050 C  CE1  . PHE A 1 146 ? 37.27738 54.39511 20.90243  1.000 18.48294 ? 132 PHE A CE1  1 
ATOM   1051 C  CE2  . PHE A 1 146 ? 37.09715 52.01396 21.18221  1.000 12.49970 ? 132 PHE A CE2  1 
ATOM   1052 C  CZ   . PHE A 1 146 ? 37.83491 53.18913 21.30109  1.000 17.85569 ? 132 PHE A CZ   1 
ATOM   1053 N  N    . ASP A 1 147 ? 33.84147 50.72219 17.77215  1.000 7.97114  ? 133 ASP A N    1 
ATOM   1054 C  CA   . ASP A 1 147 ? 34.41965 49.44289 17.34285  1.000 6.53004  ? 133 ASP A CA   1 
ATOM   1055 C  C    . ASP A 1 147 ? 35.00851 49.54049 15.94086  1.000 7.50419  ? 133 ASP A C    1 
ATOM   1056 O  O    . ASP A 1 147 ? 36.08880 49.00021 15.67036  1.000 9.45265  ? 133 ASP A O    1 
ATOM   1057 C  CB   . ASP A 1 147 ? 33.34203 48.34353 17.27456  1.000 7.60494  ? 133 ASP A CB   1 
ATOM   1058 C  CG   . ASP A 1 147 ? 32.88672 47.82051 18.62503  1.000 18.12251 ? 133 ASP A CG   1 
ATOM   1059 O  OD1  . ASP A 1 147 ? 33.67579 47.78587 19.59359  1.000 17.34116 ? 133 ASP A OD1  1 
ATOM   1060 O  OD2  . ASP A 1 147 ? 31.70938 47.39284 18.68449  1.000 17.54166 ? 133 ASP A OD2  1 
ATOM   1061 N  N    . ILE A 1 148 ? 34.27533 50.16385 15.01609  1.000 6.65937  ? 134 ILE A N    1 
ATOM   1062 C  CA   . ILE A 1 148 ? 34.75526 50.26183 13.63735  1.000 5.83130  ? 134 ILE A CA   1 
ATOM   1063 C  C    . ILE A 1 148 ? 36.04434 51.06628 13.58103  1.000 6.81352  ? 134 ILE A C    1 
ATOM   1064 O  O    . ILE A 1 148 ? 37.01867 50.66608 12.93604  1.000 8.69868  ? 134 ILE A O    1 
ATOM   1065 C  CB   . ILE A 1 148 ? 33.67446 50.86077 12.72710  1.000 7.24928  ? 134 ILE A CB   1 
ATOM   1066 C  CG1  . ILE A 1 148 ? 32.45109 49.94784 12.69817  1.000 4.79754  ? 134 ILE A CG1  1 
ATOM   1067 C  CG2  . ILE A 1 148 ? 34.22558 51.06776 11.30533  1.000 9.99370  ? 134 ILE A CG2  1 
ATOM   1068 C  CD1  . ILE A 1 148 ? 31.29239 50.55644 11.93213  1.000 10.54153 ? 134 ILE A CD1  1 
ATOM   1069 N  N    . ARG A 1 149 ? 36.05557 52.22977 14.23231  1.000 7.00834  ? 135 ARG A N    1 
ATOM   1070 C  CA   . ARG A 1 149 ? 37.27711 53.02886 14.28623  1.000 5.47038  ? 135 ARG A CA   1 
ATOM   1071 C  C    . ARG A 1 149 ? 38.42135 52.22331 14.88796  1.000 8.38511  ? 135 ARG A C    1 
ATOM   1072 O  O    . ARG A 1 149 ? 39.53864 52.23258 14.36666  1.000 7.36598  ? 135 ARG A O    1 
ATOM   1073 C  CB   . ARG A 1 149 ? 37.02421 54.28972 15.11006  1.000 5.89886  ? 135 ARG A CB   1 
ATOM   1074 C  CG   . ARG A 1 149 ? 35.98853 55.21591 14.49746  1.000 8.77286  ? 135 ARG A CG   1 
ATOM   1075 C  CD   . ARG A 1 149 ? 35.59018 56.32121 15.46768  1.000 7.58689  ? 135 ARG A CD   1 
ATOM   1076 N  NE   . ARG A 1 149 ? 34.35721 57.00733 15.08971  1.000 8.93537  ? 135 ARG A NE   1 
ATOM   1077 C  CZ   . ARG A 1 149 ? 34.25597 58.30951 14.85556  1.000 11.07157 ? 135 ARG A CZ   1 
ATOM   1078 N  NH1  . ARG A 1 149 ? 35.32641 59.08593 14.77035  1.000 9.64697  ? 135 ARG A NH1  1 
ATOM   1079 N  NH2  . ARG A 1 149 ? 33.04663 58.84909 14.71990  1.000 12.10152 ? 135 ARG A NH2  1 
ATOM   1080 N  N    . PHE A 1 150 ? 38.14421 51.49312 15.97229  1.000 7.93314  ? 136 PHE A N    1 
ATOM   1081 C  CA   . PHE A 1 150 ? 39.18238 50.74464 16.67027  1.000 7.40451  ? 136 PHE A CA   1 
ATOM   1082 C  C    . PHE A 1 150 ? 39.77926 49.65279 15.79023  1.000 8.42953  ? 136 PHE A C    1 
ATOM   1083 O  O    . PHE A 1 150 ? 41.00279 49.51321 15.69162  1.000 8.31505  ? 136 PHE A O    1 
ATOM   1084 C  CB   . PHE A 1 150 ? 38.58522 50.14358 17.94235  1.000 9.46340  ? 136 PHE A CB   1 
ATOM   1085 C  CG   . PHE A 1 150 ? 39.54345 49.27663 18.71186  1.000 10.29871 ? 136 PHE A CG   1 
ATOM   1086 C  CD1  . PHE A 1 150 ? 39.64019 47.91653 18.44149  1.000 9.37927  ? 136 PHE A CD1  1 
ATOM   1087 C  CD2  . PHE A 1 150 ? 40.33415 49.81965 19.70539  1.000 13.06325 ? 136 PHE A CD2  1 
ATOM   1088 C  CE1  . PHE A 1 150 ? 40.52708 47.12297 19.13467  1.000 13.70990 ? 136 PHE A CE1  1 
ATOM   1089 C  CE2  . PHE A 1 150 ? 41.21894 49.02623 20.41048  1.000 14.11241 ? 136 PHE A CE2  1 
ATOM   1090 C  CZ   . PHE A 1 150 ? 41.31191 47.67616 20.12150  1.000 16.31809 ? 136 PHE A CZ   1 
ATOM   1091 N  N    . TYR A 1 151 ? 38.93261 48.83080 15.17493  1.000 8.49433  ? 137 TYR A N    1 
ATOM   1092 C  CA   . TYR A 1 151 ? 39.46209 47.71009 14.41001  1.000 8.98667  ? 137 TYR A CA   1 
ATOM   1093 C  C    . TYR A 1 151 ? 40.13203 48.18749 13.12682  1.000 9.99856  ? 137 TYR A C    1 
ATOM   1094 O  O    . TYR A 1 151 ? 41.16625 47.63617 12.71910  1.000 7.51973  ? 137 TYR A O    1 
ATOM   1095 C  CB   . TYR A 1 151 ? 38.35753 46.69968 14.12761  1.000 6.41697  ? 137 TYR A CB   1 
ATOM   1096 C  CG   . TYR A 1 151 ? 37.93964 45.89350 15.33619  1.000 8.19981  ? 137 TYR A CG   1 
ATOM   1097 C  CD1  . TYR A 1 151 ? 38.88605 45.23829 16.12000  1.000 12.39981 ? 137 TYR A CD1  1 
ATOM   1098 C  CD2  . TYR A 1 151 ? 36.60613 45.78521 15.69085  1.000 8.87942  ? 137 TYR A CD2  1 
ATOM   1099 C  CE1  . TYR A 1 151 ? 38.50727 44.49831 17.22508  1.000 9.31296  ? 137 TYR A CE1  1 
ATOM   1100 C  CE2  . TYR A 1 151 ? 36.21252 45.04571 16.79666  1.000 10.56414 ? 137 TYR A CE2  1 
ATOM   1101 C  CZ   . TYR A 1 151 ? 37.17462 44.40375 17.55530  1.000 12.09413 ? 137 TYR A CZ   1 
ATOM   1102 O  OH   . TYR A 1 151 ? 36.79617 43.65599 18.64580  1.000 15.13552 ? 137 TYR A OH   1 
ATOM   1103 N  N    . MET A 1 152 ? 39.56304 49.21193 12.47773  1.000 6.52932  ? 138 MET A N    1 
ATOM   1104 C  CA   . MET A 1 152 ? 40.21405 49.77783 11.29674  1.000 6.98395  ? 138 MET A CA   1 
ATOM   1105 C  C    . MET A 1 152 ? 41.58437 50.34938 11.65246  1.000 6.56861  ? 138 MET A C    1 
ATOM   1106 O  O    . MET A 1 152 ? 42.54472 50.21983 10.87972  1.000 5.96712  ? 138 MET A O    1 
ATOM   1107 C  CB   . MET A 1 152 ? 39.32494 50.84461 10.64848  1.000 9.77728  ? 138 MET A CB   1 
ATOM   1108 C  CG   . MET A 1 152 ? 38.13244 50.31680 9.85065   1.000 12.20216 ? 138 MET A CG   1 
ATOM   1109 S  SD   . MET A 1 152 ? 38.69115 49.55376 8.31660   1.000 18.90871 ? 138 MET A SD   1 
ATOM   1110 C  CE   . MET A 1 152 ? 38.45175 47.82821 8.69679   1.000 12.52799 ? 138 MET A CE   1 
ATOM   1111 N  N    . TYR A 1 153 ? 41.69836 50.98335 12.82115  1.000 5.40558  ? 139 TYR A N    1 
ATOM   1112 C  CA   . TYR A 1 153 ? 43.00011 51.46855 13.27036  1.000 9.49963  ? 139 TYR A CA   1 
ATOM   1113 C  C    . TYR A 1 153 ? 43.97803 50.31333 13.45986  1.000 8.76075  ? 139 TYR A C    1 
ATOM   1114 O  O    . TYR A 1 153 ? 45.13575 50.39121 13.02625  1.000 6.77791  ? 139 TYR A O    1 
ATOM   1115 C  CB   . TYR A 1 153 ? 42.82256 52.25054 14.56991  1.000 7.85729  ? 139 TYR A CB   1 
ATOM   1116 C  CG   . TYR A 1 153 ? 43.98586 53.14678 14.91804  1.000 6.03859  ? 139 TYR A CG   1 
ATOM   1117 C  CD1  . TYR A 1 153 ? 44.32356 54.22034 14.10615  1.000 7.98097  ? 139 TYR A CD1  1 
ATOM   1118 C  CD2  . TYR A 1 153 ? 44.72288 52.93737 16.06727  1.000 10.70803 ? 139 TYR A CD2  1 
ATOM   1119 C  CE1  . TYR A 1 153 ? 45.37747 55.05271 14.42616  1.000 9.93055  ? 139 TYR A CE1  1 
ATOM   1120 C  CE2  . TYR A 1 153 ? 45.78190 53.76811 16.39677  1.000 12.18218 ? 139 TYR A CE2  1 
ATOM   1121 C  CZ   . TYR A 1 153 ? 46.09805 54.82113 15.57642  1.000 13.60827 ? 139 TYR A CZ   1 
ATOM   1122 O  OH   . TYR A 1 153 ? 47.15128 55.64448 15.90759  1.000 16.03839 ? 139 TYR A OH   1 
ATOM   1123 N  N    . GLU A 1 154 ? 43.51346 49.20943 14.05759  1.000 8.36329  ? 140 GLU A N    1 
ATOM   1124 C  CA   . GLU A 1 154 ? 44.38771 48.05629 14.26333  1.000 8.22603  ? 140 GLU A CA   1 
ATOM   1125 C  C    . GLU A 1 154 ? 44.80684 47.43684 12.93306  1.000 7.45460  ? 140 GLU A C    1 
ATOM   1126 O  O    . GLU A 1 154 ? 45.94732 46.99611 12.78218  1.000 8.27854  ? 140 GLU A O    1 
ATOM   1127 C  CB   . GLU A 1 154 ? 43.69656 47.00667 15.14079  1.000 9.25227  ? 140 GLU A CB   1 
ATOM   1128 C  CG   . GLU A 1 154 ? 43.41061 47.47587 16.56931  1.000 9.29064  ? 140 GLU A CG   1 
ATOM   1129 C  CD   . GLU A 1 154 ? 44.68278 47.68009 17.37693  1.000 12.92042 ? 140 GLU A CD   1 
ATOM   1130 O  OE1  . GLU A 1 154 ? 45.44479 46.70687 17.52385  1.000 25.40169 ? 140 GLU A OE1  1 
ATOM   1131 O  OE2  . GLU A 1 154 ? 44.92843 48.80138 17.87109  1.000 16.21358 ? 140 GLU A OE2  1 
ATOM   1132 N  N    . LEU A 1 155 ? 43.89689 47.38031 11.96077  1.000 8.54003  ? 141 LEU A N    1 
ATOM   1133 C  CA   . LEU A 1 155 ? 44.27551 46.85684 10.65036  1.000 7.43518  ? 141 LEU A CA   1 
ATOM   1134 C  C    . LEU A 1 155 ? 45.30217 47.75909 9.96930   1.000 5.19425  ? 141 LEU A C    1 
ATOM   1135 O  O    . LEU A 1 155 ? 46.24199 47.27435 9.32788   1.000 6.86919  ? 141 LEU A O    1 
ATOM   1136 C  CB   . LEU A 1 155 ? 43.02958 46.69529 9.78735   1.000 5.38105  ? 141 LEU A CB   1 
ATOM   1137 C  CG   . LEU A 1 155 ? 43.25852 46.19440 8.35698   1.000 7.18955  ? 141 LEU A CG   1 
ATOM   1138 C  CD1  . LEU A 1 155 ? 43.97625 44.84678 8.35249   1.000 6.82418  ? 141 LEU A CD1  1 
ATOM   1139 C  CD2  . LEU A 1 155 ? 41.91624 46.07697 7.63091   1.000 7.37684  ? 141 LEU A CD2  1 
ATOM   1140 N  N    . LEU A 1 156 ? 45.13847 49.07150 10.10674  1.000 3.32480  ? 142 LEU A N    1 
ATOM   1141 C  CA   . LEU A 1 156 ? 46.08028 50.00296 9.49468   1.000 8.36396  ? 142 LEU A CA   1 
ATOM   1142 C  C    . LEU A 1 156 ? 47.47570 49.84140 10.07560  1.000 9.27869  ? 142 LEU A C    1 
ATOM   1143 O  O    . LEU A 1 156 ? 48.47425 50.00974 9.36406   1.000 8.06759  ? 142 LEU A O    1 
ATOM   1144 C  CB   . LEU A 1 156 ? 45.58390 51.43497 9.67577   1.000 7.43086  ? 142 LEU A CB   1 
ATOM   1145 C  CG   . LEU A 1 156 ? 44.47635 51.85313 8.70694   1.000 8.43872  ? 142 LEU A CG   1 
ATOM   1146 C  CD1  . LEU A 1 156 ? 43.79231 53.12971 9.19629   1.000 8.23751  ? 142 LEU A CD1  1 
ATOM   1147 C  CD2  . LEU A 1 156 ? 45.01107 52.06588 7.29020   1.000 8.21535  ? 142 LEU A CD2  1 
ATOM   1148 N  N    . LYS A 1 157 ? 47.57347 49.53363 11.37039  1.000 8.45735  ? 143 LYS A N    1 
ATOM   1149 C  CA   . LYS A 1 157 ? 48.89110 49.29189 11.94191  1.000 7.47400  ? 143 LYS A CA   1 
ATOM   1150 C  C    . LYS A 1 157 ? 49.59533 48.15664 11.20423  1.000 7.66149  ? 143 LYS A C    1 
ATOM   1151 O  O    . LYS A 1 157 ? 50.79189 48.24930 10.89791  1.000 8.71685  ? 143 LYS A O    1 
ATOM   1152 C  CB   . LYS A 1 157 ? 48.78358 48.97123 13.43374  1.000 8.96160  ? 143 LYS A CB   1 
ATOM   1153 C  CG   . LYS A 1 157 ? 48.30838 50.13101 14.31899  1.000 9.99280  ? 143 LYS A CG   1 
ATOM   1154 C  CD   . LYS A 1 157 ? 48.24596 49.65900 15.76968  1.000 16.25154 ? 143 LYS A CD   1 
ATOM   1155 C  CE   . LYS A 1 157 ? 47.64456 50.72567 16.67488  1.000 17.76873 ? 143 LYS A CE   1 
ATOM   1156 N  NZ   . LYS A 1 157 ? 47.29981 50.18965 18.03149  1.000 14.54948 ? 143 LYS A NZ   1 
ATOM   1157 N  N    . ALA A 1 158 ? 48.86273 47.08743 10.88471  1.000 4.85734  ? 144 ALA A N    1 
ATOM   1158 C  CA   . ALA A 1 158 ? 49.49166 45.94613 10.23129  1.000 3.90637  ? 144 ALA A CA   1 
ATOM   1159 C  C    . ALA A 1 158 ? 49.90882 46.29534 8.81299   1.000 5.74152  ? 144 ALA A C    1 
ATOM   1160 O  O    . ALA A 1 158 ? 50.97412 45.86246 8.34502   1.000 5.69134  ? 144 ALA A O    1 
ATOM   1161 C  CB   . ALA A 1 158 ? 48.52861 44.75428 10.22554  1.000 6.19214  ? 144 ALA A CB   1 
ATOM   1162 N  N    . LEU A 1 159 ? 49.07581 47.06461 8.10626   1.000 5.27168  ? 145 LEU A N    1 
ATOM   1163 C  CA   . LEU A 1 159 ? 49.39631 47.44228 6.73368   1.000 3.28111  ? 145 LEU A CA   1 
ATOM   1164 C  C    . LEU A 1 159 ? 50.53726 48.45023 6.68224   1.000 5.59551  ? 145 LEU A C    1 
ATOM   1165 O  O    . LEU A 1 159 ? 51.42569 48.33443 5.82870   1.000 6.84335  ? 145 LEU A O    1 
ATOM   1166 C  CB   . LEU A 1 159 ? 48.15326 47.99860 6.03448   1.000 6.38956  ? 145 LEU A CB   1 
ATOM   1167 C  CG   . LEU A 1 159 ? 47.04596 46.98238 5.74873   1.000 7.05424  ? 145 LEU A CG   1 
ATOM   1168 C  CD1  . LEU A 1 159 ? 45.88506 47.67876 5.08662   1.000 12.81337 ? 145 LEU A CD1  1 
ATOM   1169 C  CD2  . LEU A 1 159 ? 47.55449 45.84846 4.87503   1.000 7.88447  ? 145 LEU A CD2  1 
ATOM   1170 N  N    . ASP A 1 160 ? 50.52114 49.46551 7.55477   1.000 7.54588  ? 146 ASP A N    1 
ATOM   1171 C  CA   . ASP A 1 160 ? 51.66008 50.37759 7.58774   1.000 7.75332  ? 146 ASP A CA   1 
ATOM   1172 C  C    . ASP A 1 160 ? 52.94052 49.61375 7.87930   1.000 9.30496  ? 146 ASP A C    1 
ATOM   1173 O  O    . ASP A 1 160 ? 53.97371 49.86462 7.24977   1.000 8.47835  ? 146 ASP A O    1 
ATOM   1174 C  CB   . ASP A 1 160 ? 51.46804 51.51263 8.59786   1.000 6.99640  ? 146 ASP A CB   1 
ATOM   1175 C  CG   . ASP A 1 160 ? 52.66210 52.46771 8.60942   1.000 12.78101 ? 146 ASP A CG   1 
ATOM   1176 O  OD1  . ASP A 1 160 ? 52.94310 53.09759 7.56174   1.000 12.59822 ? 146 ASP A OD1  1 
ATOM   1177 O  OD2  . ASP A 1 160 ? 53.33988 52.56102 9.65006   1.000 19.72085 ? 146 ASP A OD2  1 
ATOM   1178 N  N    . TYR A 1 161 ? 52.87658 48.63609 8.78962   1.000 6.21806  ? 147 TYR A N    1 
ATOM   1179 C  CA   . TYR A 1 161 ? 54.05977 47.83734 9.08386   1.000 6.29514  ? 147 TYR A CA   1 
ATOM   1180 C  C    . TYR A 1 161 ? 54.54247 47.08267 7.85219   1.000 7.00072  ? 147 TYR A C    1 
ATOM   1181 O  O    . TYR A 1 161 ? 55.71350 47.18564 7.46919   1.000 6.23694  ? 147 TYR A O    1 
ATOM   1182 C  CB   . TYR A 1 161 ? 53.81628 46.86592 10.23739  1.000 6.64342  ? 147 TYR A CB   1 
ATOM   1183 C  CG   . TYR A 1 161 ? 55.11905 46.25901 10.70449  1.000 5.97667  ? 147 TYR A CG   1 
ATOM   1184 C  CD1  . TYR A 1 161 ? 55.98098 46.99911 11.49855  1.000 15.07790 ? 147 TYR A CD1  1 
ATOM   1185 C  CD2  . TYR A 1 161 ? 55.51088 44.97678 10.32421  1.000 9.38454  ? 147 TYR A CD2  1 
ATOM   1186 C  CE1  . TYR A 1 161 ? 57.17765 46.49337 11.92532  1.000 16.37920 ? 147 TYR A CE1  1 
ATOM   1187 C  CE2  . TYR A 1 161 ? 56.73824 44.45850 10.74691  1.000 15.96017 ? 147 TYR A CE2  1 
ATOM   1188 C  CZ   . TYR A 1 161 ? 57.55717 45.23384 11.55579  1.000 18.01478 ? 147 TYR A CZ   1 
ATOM   1189 O  OH   . TYR A 1 161 ? 58.77348 44.79321 12.01498  1.000 20.89972 ? 147 TYR A OH   1 
ATOM   1190 N  N    . CYS A 1 162 ? 53.65605 46.32575 7.20371   1.000 4.51698  ? 148 CYS A N    1 
ATOM   1191 C  CA   . CYS A 1 162 ? 54.13482 45.52848 6.07791   1.000 7.55064  ? 148 CYS A CA   1 
ATOM   1192 C  C    . CYS A 1 162 ? 54.58322 46.40715 4.90748   1.000 6.36910  ? 148 CYS A C    1 
ATOM   1193 O  O    . CYS A 1 162 ? 55.61259 46.12440 4.28034   1.000 6.45244  ? 148 CYS A O    1 
ATOM   1194 C  CB   . CYS A 1 162 ? 53.14020 44.42771 5.68284   1.000 7.51079  ? 148 CYS A CB   1 
ATOM   1195 S  SG   . CYS A 1 162 ? 51.66619 44.91969 4.79683   1.000 9.82117  ? 148 CYS A SG   1 
ATOM   1196 N  N    . HIS A 1 163 ? 53.85760 47.49571 4.61695   1.000 7.18650  ? 149 HIS A N    1 
ATOM   1197 C  CA   . HIS A 1 163 ? 54.30660 48.38914 3.54824   1.000 6.17277  ? 149 HIS A CA   1 
ATOM   1198 C  C    . HIS A 1 163 ? 55.68056 48.98298 3.87096   1.000 5.50138  ? 149 HIS A C    1 
ATOM   1199 O  O    . HIS A 1 163 ? 56.53114 49.12579 2.97918   1.000 5.75757  ? 149 HIS A O    1 
ATOM   1200 C  CB   . HIS A 1 163 ? 53.28288 49.50472 3.30733   1.000 6.61821  ? 149 HIS A CB   1 
ATOM   1201 C  CG   . HIS A 1 163 ? 51.93275 49.01459 2.86815   1.000 5.98060  ? 149 HIS A CG   1 
ATOM   1202 N  ND1  . HIS A 1 163 ? 50.81233 49.82119 2.86903   1.000 4.53214  ? 149 HIS A ND1  1 
ATOM   1203 C  CD2  . HIS A 1 163 ? 51.52654 47.80723 2.40060   1.000 5.47600  ? 149 HIS A CD2  1 
ATOM   1204 C  CE1  . HIS A 1 163 ? 49.77191 49.12775 2.44207   1.000 5.90654  ? 149 HIS A CE1  1 
ATOM   1205 N  NE2  . HIS A 1 163 ? 50.18057 47.90638 2.13307   1.000 4.79561  ? 149 HIS A NE2  1 
ATOM   1206 N  N    . SER A 1 164 ? 55.91488 49.33900 5.14047   1.000 5.14689  ? 150 SER A N    1 
ATOM   1207 C  CA   . SER A 1 164 ? 57.21310 49.88259 5.53187   1.000 5.36175  ? 150 SER A CA   1 
ATOM   1208 C  C    . SER A 1 164 ? 58.31559 48.84223 5.41456   1.000 9.38914  ? 150 SER A C    1 
ATOM   1209 O  O    . SER A 1 164 ? 59.48547 49.20981 5.29363   1.000 7.27991  ? 150 SER A O    1 
ATOM   1210 C  CB   . SER A 1 164 ? 57.15481 50.43817 6.95824   1.000 8.73905  ? 150 SER A CB   1 
ATOM   1211 O  OG   . SER A 1 164 ? 57.24076 49.40121 7.92672   1.000 7.82471  ? 150 SER A OG   1 
ATOM   1212 N  N    . LYS A 1 165 ? 57.96138 47.56200 5.44806   1.000 6.69289  ? 151 LYS A N    1 
ATOM   1213 C  CA   . LYS A 1 165 ? 58.87810 46.45117 5.20955   1.000 5.57069  ? 151 LYS A CA   1 
ATOM   1214 C  C    . LYS A 1 165 ? 58.97441 46.07024 3.72741   1.000 4.84932  ? 151 LYS A C    1 
ATOM   1215 O  O    . LYS A 1 165 ? 59.57859 45.04015 3.40008   1.000 7.82334  ? 151 LYS A O    1 
ATOM   1216 C  CB   . LYS A 1 165 ? 58.46750 45.25733 6.07490   1.000 6.40343  ? 151 LYS A CB   1 
ATOM   1217 C  CG   . LYS A 1 165 ? 58.77573 45.44391 7.56121   1.000 7.97459  ? 151 LYS A CG   1 
ATOM   1218 C  CD   . LYS A 1 165 ? 60.28624 45.52882 7.77211   1.000 18.60154 ? 151 LYS A CD   1 
ATOM   1219 C  CE   . LYS A 1 165 ? 60.65111 45.47191 9.23735   1.000 28.61657 ? 151 LYS A CE   1 
ATOM   1220 N  NZ   . LYS A 1 165 ? 62.13203 45.47475 9.40496   1.000 34.23702 ? 151 LYS A NZ   1 
ATOM   1221 N  N    . GLY A 1 166 ? 58.41588 46.88689 2.83053   1.000 3.68502  ? 152 GLY A N    1 
ATOM   1222 C  CA   . GLY A 1 166 ? 58.52222 46.63339 1.40304   1.000 3.87368  ? 152 GLY A CA   1 
ATOM   1223 C  C    . GLY A 1 166 ? 57.63133 45.53987 0.86235   1.000 6.19932  ? 152 GLY A C    1 
ATOM   1224 O  O    . GLY A 1 166 ? 57.94856 44.94894 -0.18035  1.000 6.60228  ? 152 GLY A O    1 
ATOM   1225 N  N    . ILE A 1 167 ? 56.50769 45.26520 1.52061   1.000 5.86000  ? 153 ILE A N    1 
ATOM   1226 C  CA   . ILE A 1 167 ? 55.64854 44.13467 1.18461   1.000 4.16242  ? 153 ILE A CA   1 
ATOM   1227 C  C    . ILE A 1 167 ? 54.21304 44.62148 0.99518   1.000 8.10485  ? 153 ILE A C    1 
ATOM   1228 O  O    . ILE A 1 167 ? 53.70599 45.41412 1.80342   1.000 7.71929  ? 153 ILE A O    1 
ATOM   1229 C  CB   . ILE A 1 167 ? 55.74336 43.05199 2.28181   1.000 4.95815  ? 153 ILE A CB   1 
ATOM   1230 C  CG1  . ILE A 1 167 ? 57.12526 42.38254 2.20796   1.000 7.93418  ? 153 ILE A CG1  1 
ATOM   1231 C  CG2  . ILE A 1 167 ? 54.63195 42.00998 2.13447   1.000 7.07784  ? 153 ILE A CG2  1 
ATOM   1232 C  CD1  . ILE A 1 167 ? 57.62381 41.82113 3.54701   1.000 11.38229 ? 153 ILE A CD1  1 
ATOM   1233 N  N    . MET A 1 168 ? 53.57683 44.16998 -0.09226  1.000 7.57134  ? 154 MET A N    1 
ATOM   1234 C  CA   . MET A 1 168 ? 52.15851 44.38139 -0.35673  1.000 7.09704  ? 154 MET A CA   1 
ATOM   1235 C  C    . MET A 1 168 ? 51.44220 43.08910 0.01454   1.000 5.96870  ? 154 MET A C    1 
ATOM   1236 O  O    . MET A 1 168 ? 51.87727 42.00931 -0.39812  1.000 6.00231  ? 154 MET A O    1 
ATOM   1237 C  CB   . MET A 1 168 ? 51.91052 44.59205 -1.85526  1.000 7.96870  ? 154 MET A CB   1 
ATOM   1238 C  CG   . MET A 1 168 ? 52.75282 45.61397 -2.57425  1.000 11.96356 ? 154 MET A CG   1 
ATOM   1239 S  SD   . MET A 1 168 ? 52.37752 45.59263 -4.34627  1.000 12.75325 ? 154 MET A SD   1 
ATOM   1240 C  CE   . MET A 1 168 ? 53.60253 44.42797 -4.96138  1.000 11.25815 ? 154 MET A CE   1 
ATOM   1241 N  N    . HIS A 1 169 ? 50.32900 43.19664 0.74816   1.000 5.49505  ? 155 HIS A N    1 
ATOM   1242 C  CA   . HIS A 1 169 ? 49.58889 41.98952 1.13402   1.000 4.19251  ? 155 HIS A CA   1 
ATOM   1243 C  C    . HIS A 1 169 ? 48.83455 41.38071 -0.05702  1.000 6.90530  ? 155 HIS A C    1 
ATOM   1244 O  O    . HIS A 1 169 ? 48.93036 40.17417 -0.31964  1.000 5.24657  ? 155 HIS A O    1 
ATOM   1245 C  CB   . HIS A 1 169 ? 48.65457 42.30123 2.30466   1.000 4.50358  ? 155 HIS A CB   1 
ATOM   1246 C  CG   . HIS A 1 169 ? 47.94684 41.09628 2.84665   1.000 5.31791  ? 155 HIS A CG   1 
ATOM   1247 N  ND1  . HIS A 1 169 ? 46.82797 40.55855 2.24838   1.000 7.66586  ? 155 HIS A ND1  1 
ATOM   1248 C  CD2  . HIS A 1 169 ? 48.19984 40.32866 3.93459   1.000 6.04218  ? 155 HIS A CD2  1 
ATOM   1249 C  CE1  . HIS A 1 169 ? 46.42636 39.50772 2.93729   1.000 6.97669  ? 155 HIS A CE1  1 
ATOM   1250 N  NE2  . HIS A 1 169 ? 47.24056 39.34734 3.96626   1.000 7.76994  ? 155 HIS A NE2  1 
ATOM   1251 N  N    . ARG A 1 170 ? 48.08716 42.20075 -0.79628  1.000 4.47233  ? 156 ARG A N    1 
ATOM   1252 C  CA   . ARG A 1 170 ? 47.39677 41.84248 -2.03463  1.000 5.90583  ? 156 ARG A CA   1 
ATOM   1253 C  C    . ARG A 1 170 ? 46.16391 40.95491 -1.83593  1.000 6.96934  ? 156 ARG A C    1 
ATOM   1254 O  O    . ARG A 1 170 ? 45.56258 40.53837 -2.82382  1.000 9.27082  ? 156 ARG A O    1 
ATOM   1255 C  CB   . ARG A 1 170 ? 48.32754 41.24963 -3.11029  1.000 5.81112  ? 156 ARG A CB   1 
ATOM   1256 C  CG   . ARG A 1 170 ? 49.53294 42.14365 -3.42570  1.000 6.02079  ? 156 ARG A CG   1 
ATOM   1257 C  CD   . ARG A 1 170 ? 50.19165 41.76337 -4.73857  1.000 3.14772  ? 156 ARG A CD   1 
ATOM   1258 N  NE   . ARG A 1 170 ? 50.61667 40.36833 -4.75559  1.000 5.25591  ? 156 ARG A NE   1 
ATOM   1259 C  CZ   . ARG A 1 170 ? 51.19145 39.79088 -5.79801  1.000 6.91156  ? 156 ARG A CZ   1 
ATOM   1260 N  NH1  . ARG A 1 170 ? 51.34874 40.43781 -6.94250  1.000 10.80869 ? 156 ARG A NH1  1 
ATOM   1261 N  NH2  . ARG A 1 170 ? 51.61362 38.53041 -5.69331  1.000 10.03372 ? 156 ARG A NH2  1 
ATOM   1262 N  N    . ASP A 1 171 ? 45.76314 40.65233 -0.60419  1.000 5.02369  ? 157 ASP A N    1 
ATOM   1263 C  CA   . ASP A 1 171 ? 44.54966 39.86502 -0.39463  1.000 6.18986  ? 157 ASP A CA   1 
ATOM   1264 C  C    . ASP A 1 171 ? 43.81158 40.34001 0.85082   1.000 9.54542  ? 157 ASP A C    1 
ATOM   1265 O  O    . ASP A 1 171 ? 43.29966 39.53465 1.63620   1.000 10.40545 ? 157 ASP A O    1 
ATOM   1266 C  CB   . ASP A 1 171 ? 44.87802 38.37352 -0.33046  1.000 4.99145  ? 157 ASP A CB   1 
ATOM   1267 C  CG   . ASP A 1 171 ? 43.66466 37.49277 -0.53337  1.000 15.16064 ? 157 ASP A CG   1 
ATOM   1268 O  OD1  . ASP A 1 171 ? 42.65589 37.97888 -1.07773  1.000 11.72661 ? 157 ASP A OD1  1 
ATOM   1269 O  OD2  . ASP A 1 171 ? 43.72513 36.30679 -0.14746  1.000 12.23078 ? 157 ASP A OD2  1 
ATOM   1270 N  N    . VAL A 1 172 ? 43.74862 41.65848 1.05326   1.000 4.20802  ? 158 VAL A N    1 
ATOM   1271 C  CA   . VAL A 1 172 ? 42.99416 42.20336 2.18007   1.000 4.08876  ? 158 VAL A CA   1 
ATOM   1272 C  C    . VAL A 1 172 ? 41.49692 42.00694 1.94269   1.000 8.73697  ? 158 VAL A C    1 
ATOM   1273 O  O    . VAL A 1 172 ? 40.95467 42.39677 0.89781   1.000 5.88538  ? 158 VAL A O    1 
ATOM   1274 C  CB   . VAL A 1 172 ? 43.35955 43.67780 2.40838   1.000 7.71308  ? 158 VAL A CB   1 
ATOM   1275 C  CG1  . VAL A 1 172 ? 42.44775 44.31181 3.48494   1.000 7.29614  ? 158 VAL A CG1  1 
ATOM   1276 C  CG2  . VAL A 1 172 ? 44.81794 43.80200 2.81467   1.000 9.23521  ? 158 VAL A CG2  1 
ATOM   1277 N  N    . LYS A 1 173 ? 40.82228 41.40597 2.91711   1.000 7.17832  ? 159 LYS A N    1 
ATOM   1278 C  CA   . LYS A 1 173 ? 39.39496 41.11044 2.85532   1.000 6.29561  ? 159 LYS A CA   1 
ATOM   1279 C  C    . LYS A 1 173 ? 38.96946 40.60386 4.23198   1.000 6.93506  ? 159 LYS A C    1 
ATOM   1280 O  O    . LYS A 1 173 ? 39.81845 40.16233 5.01203   1.000 7.67250  ? 159 LYS A O    1 
ATOM   1281 C  CB   . LYS A 1 173 ? 39.08387 40.05587 1.77617   1.000 6.93658  ? 159 LYS A CB   1 
ATOM   1282 C  CG   . LYS A 1 173 ? 39.76082 38.71466 1.99290   1.000 9.53743  ? 159 LYS A CG   1 
ATOM   1283 C  CD   . LYS A 1 173 ? 39.37411 37.68798 0.91533   1.000 8.91050  ? 159 LYS A CD   1 
ATOM   1284 C  CE   . LYS A 1 173 ? 40.05305 36.33841 1.17019   1.000 10.71433 ? 159 LYS A CE   1 
ATOM   1285 N  NZ   . LYS A 1 173 ? 39.69593 35.31263 0.12452   1.000 11.46747 ? 159 LYS A NZ   1 
ATOM   1286 N  N    . PRO A 1 174 ? 37.67108 40.66442 4.55453   1.000 6.22601  ? 160 PRO A N    1 
ATOM   1287 C  CA   . PRO A 1 174 ? 37.23712 40.23837 5.89554   1.000 6.95259  ? 160 PRO A CA   1 
ATOM   1288 C  C    . PRO A 1 174 ? 37.72792 38.86169 6.31355   1.000 7.16143  ? 160 PRO A C    1 
ATOM   1289 O  O    . PRO A 1 174 ? 38.13346 38.68601 7.47325   1.000 8.50040  ? 160 PRO A O    1 
ATOM   1290 C  CB   . PRO A 1 174 ? 35.70633 40.32070 5.80687   1.000 9.10753  ? 160 PRO A CB   1 
ATOM   1291 C  CG   . PRO A 1 174 ? 35.47712 41.39556 4.77906   1.000 7.31995  ? 160 PRO A CG   1 
ATOM   1292 C  CD   . PRO A 1 174 ? 36.54858 41.20641 3.76715   1.000 7.00490  ? 160 PRO A CD   1 
ATOM   1293 N  N    . HIS A 1 175 ? 37.72063 37.88370 5.40540   1.000 6.98939  ? 161 HIS A N    1 
ATOM   1294 C  CA   . HIS A 1 175 ? 38.18000 36.54815 5.77119   1.000 9.95278  ? 161 HIS A CA   1 
ATOM   1295 C  C    . HIS A 1 175 ? 39.62043 36.55124 6.26424   1.000 13.82745 ? 161 HIS A C    1 
ATOM   1296 O  O    . HIS A 1 175 ? 39.97325 35.74204 7.12585   1.000 16.11964 ? 161 HIS A O    1 
ATOM   1297 C  CB   . HIS A 1 175 ? 38.04513 35.57603 4.60674   1.000 10.14012 ? 161 HIS A CB   1 
ATOM   1298 C  CG   . HIS A 1 175 ? 38.56634 34.21547 4.92778   1.000 26.05888 ? 161 HIS A CG   1 
ATOM   1299 N  ND1  . HIS A 1 175 ? 37.78854 33.24243 5.51793   1.000 27.48722 ? 161 HIS A ND1  1 
ATOM   1300 C  CD2  . HIS A 1 175 ? 39.80201 33.67930 4.78987   1.000 29.94785 ? 161 HIS A CD2  1 
ATOM   1301 C  CE1  . HIS A 1 175 ? 38.51655 32.15610 5.70422   1.000 39.94485 ? 161 HIS A CE1  1 
ATOM   1302 N  NE2  . HIS A 1 175 ? 39.74256 32.39577 5.27417   1.000 38.21715 ? 161 HIS A NE2  1 
ATOM   1303 N  N    . ASN A 1 176 ? 40.46724 37.43983 5.73630   1.000 8.83106  ? 162 ASN A N    1 
ATOM   1304 C  CA   . ASN A 1 176 ? 41.87132 37.49909 6.13214   1.000 8.30965  ? 162 ASN A CA   1 
ATOM   1305 C  C    . ASN A 1 176 ? 42.14025 38.48194 7.26157   1.000 9.15766  ? 162 ASN A C    1 
ATOM   1306 O  O    . ASN A 1 176 ? 43.31092 38.73197 7.58302   1.000 8.98792  ? 162 ASN A O    1 
ATOM   1307 C  CB   . ASN A 1 176 ? 42.76151 37.81157 4.92501   1.000 7.02184  ? 162 ASN A CB   1 
ATOM   1308 C  CG   . ASN A 1 176 ? 42.84735 36.65043 3.96656   1.000 11.27442 ? 162 ASN A CG   1 
ATOM   1309 O  OD1  . ASN A 1 176 ? 42.59673 35.49187 4.34488   1.000 8.70976  ? 162 ASN A OD1  1 
ATOM   1310 N  ND2  . ASN A 1 176 ? 43.17839 36.94074 2.71902   1.000 7.53140  ? 162 ASN A ND2  1 
ATOM   1311 N  N    . VAL A 1 177 ? 41.09631 39.05382 7.85208   1.000 9.46795  ? 163 VAL A N    1 
ATOM   1312 C  CA   . VAL A 1 177 ? 41.22141 39.96351 8.98919   1.000 9.45650  ? 163 VAL A CA   1 
ATOM   1313 C  C    . VAL A 1 177 ? 40.50321 39.29487 10.15729  1.000 13.69722 ? 163 VAL A C    1 
ATOM   1314 O  O    . VAL A 1 177 ? 39.28175 39.41934 10.31651  1.000 13.09171 ? 163 VAL A O    1 
ATOM   1315 C  CB   . VAL A 1 177 ? 40.65818 41.35768 8.68850   1.000 8.05088  ? 163 VAL A CB   1 
ATOM   1316 C  CG1  . VAL A 1 177 ? 40.72378 42.22623 9.91595   1.000 9.90532  ? 163 VAL A CG1  1 
ATOM   1317 C  CG2  . VAL A 1 177 ? 41.42595 42.01008 7.53963   1.000 9.92066  ? 163 VAL A CG2  1 
ATOM   1318 N  N    A MET A 1 178 ? 41.25287 38.52696 10.94530  0.419 7.98621  ? 164 MET A N    1 
ATOM   1319 N  N    B MET A 1 178 ? 41.25765 38.60213 11.00555  0.581 7.89904  ? 164 MET A N    1 
ATOM   1320 C  CA   A MET A 1 178 ? 40.68706 37.83473 12.09102  0.419 8.94471  ? 164 MET A CA   1 
ATOM   1321 C  CA   B MET A 1 178 ? 40.67106 37.82076 12.08498  0.581 8.91032  ? 164 MET A CA   1 
ATOM   1322 C  C    A MET A 1 178 ? 40.44830 38.84201 13.20447  0.419 8.71040  ? 164 MET A C    1 
ATOM   1323 C  C    B MET A 1 178 ? 40.51113 38.68938 13.32128  0.581 8.71875  ? 164 MET A C    1 
ATOM   1324 O  O    A MET A 1 178 ? 41.27850 39.71853 13.45297  0.419 10.07173 ? 164 MET A O    1 
ATOM   1325 O  O    B MET A 1 178 ? 41.48185 39.28738 13.79148  0.581 8.51832  ? 164 MET A O    1 
ATOM   1326 C  CB   A MET A 1 178 ? 41.64432 36.73867 12.57099  0.419 10.11997 ? 164 MET A CB   1 
ATOM   1327 C  CB   B MET A 1 178 ? 41.56580 36.62863 12.40199  0.581 9.94072  ? 164 MET A CB   1 
ATOM   1328 C  CG   A MET A 1 178 ? 41.83711 35.58574 11.58366  0.419 14.04233 ? 164 MET A CG   1 
ATOM   1329 C  CG   B MET A 1 178 ? 41.67266 35.66383 11.25462  0.581 14.46340 ? 164 MET A CG   1 
ATOM   1330 S  SD   A MET A 1 178 ? 40.28103 34.75038 11.20880  0.419 13.20458 ? 164 MET A SD   1 
ATOM   1331 S  SD   B MET A 1 178 ? 42.23205 34.07174 11.83643  0.581 16.55248 ? 164 MET A SD   1 
ATOM   1332 C  CE   A MET A 1 178 ? 40.78738 33.39555 10.16767  0.419 23.67704 ? 164 MET A CE   1 
ATOM   1333 C  CE   B MET A 1 178 ? 41.27059 33.89284 13.30305  0.581 26.22652 ? 164 MET A CE   1 
ATOM   1334 N  N    . ILE A 1 179 ? 39.29224 38.73927 13.85690  1.000 9.45203  ? 165 ILE A N    1 
ATOM   1335 C  CA   . ILE A 1 179 ? 38.94918 39.63312 14.95811  1.000 7.97560  ? 165 ILE A CA   1 
ATOM   1336 C  C    . ILE A 1 179 ? 38.36585 38.81958 16.10135  1.000 10.36294 ? 165 ILE A C    1 
ATOM   1337 O  O    . ILE A 1 179 ? 37.29395 38.22175 15.95920  1.000 13.38400 ? 165 ILE A O    1 
ATOM   1338 C  CB   . ILE A 1 179 ? 37.98007 40.74644 14.52691  1.000 9.19453  ? 165 ILE A CB   1 
ATOM   1339 C  CG1  . ILE A 1 179 ? 38.63294 41.66175 13.48635  1.000 9.41565  ? 165 ILE A CG1  1 
ATOM   1340 C  CG2  . ILE A 1 179 ? 37.52126 41.54706 15.74395  1.000 10.58608 ? 165 ILE A CG2  1 
ATOM   1341 C  CD1  . ILE A 1 179 ? 37.71235 42.75989 12.97938  1.000 13.02922 ? 165 ILE A CD1  1 
ATOM   1342 N  N    . ASP A 1 180 ? 39.07481 38.80096 17.22735  1.000 6.08291  ? 166 ASP A N    1 
ATOM   1343 C  CA   . ASP A 1 180 ? 38.57630 38.27729 18.49719  1.000 8.79384  ? 166 ASP A CA   1 
ATOM   1344 C  C    . ASP A 1 180 ? 37.89563 39.46184 19.17079  1.000 9.75038  ? 166 ASP A C    1 
ATOM   1345 O  O    . ASP A 1 180 ? 38.55918 40.34252 19.72082  1.000 11.36767 ? 166 ASP A O    1 
ATOM   1346 C  CB   . ASP A 1 180 ? 39.74853 37.74731 19.32108  1.000 13.23722 ? 166 ASP A CB   1 
ATOM   1347 C  CG   . ASP A 1 180 ? 39.34343 37.23854 20.71544  1.000 16.73214 ? 166 ASP A CG   1 
ATOM   1348 O  OD1  . ASP A 1 180 ? 38.25407 37.58237 21.22221  1.000 16.84140 ? 166 ASP A OD1  1 
ATOM   1349 O  OD2  . ASP A 1 180 ? 40.13822 36.48840 21.32746  1.000 16.41153 ? 166 ASP A OD2  1 
ATOM   1350 N  N    . HIS A 1 181 ? 36.56734 39.50008 19.09914  1.000 10.28195 ? 167 HIS A N    1 
ATOM   1351 C  CA   . HIS A 1 181 ? 35.79125 40.62006 19.61854  1.000 11.47858 ? 167 HIS A CA   1 
ATOM   1352 C  C    . HIS A 1 181 ? 35.65120 40.57770 21.13248  1.000 13.64725 ? 167 HIS A C    1 
ATOM   1353 O  O    . HIS A 1 181 ? 35.18732 41.55810 21.73022  1.000 17.99235 ? 167 HIS A O    1 
ATOM   1354 C  CB   . HIS A 1 181 ? 34.40164 40.62175 18.95633  1.000 12.97230 ? 167 HIS A CB   1 
ATOM   1355 C  CG   . HIS A 1 181 ? 33.61875 41.88653 19.16249  1.000 14.14202 ? 167 HIS A CG   1 
ATOM   1356 N  ND1  . HIS A 1 181 ? 34.16601 43.14218 18.99429  1.000 14.56775 ? 167 HIS A ND1  1 
ATOM   1357 C  CD2  . HIS A 1 181 ? 32.31789 42.08503 19.48941  1.000 15.88104 ? 167 HIS A CD2  1 
ATOM   1358 C  CE1  . HIS A 1 181 ? 33.24131 44.05896 19.22543  1.000 12.57134 ? 167 HIS A CE1  1 
ATOM   1359 N  NE2  . HIS A 1 181 ? 32.11060 43.44428 19.52965  1.000 16.18636 ? 167 HIS A NE2  1 
ATOM   1360 N  N    . GLN A 1 182 ? 36.04340 39.47221 21.76344  1.000 15.94707 ? 168 GLN A N    1 
ATOM   1361 C  CA   . GLN A 1 182 ? 36.03104 39.38905 23.21890  1.000 13.95563 ? 168 GLN A CA   1 
ATOM   1362 C  C    . GLN A 1 182 ? 37.23409 40.10666 23.80789  1.000 12.87148 ? 168 GLN A C    1 
ATOM   1363 O  O    . GLN A 1 182 ? 37.09010 40.94252 24.70961  1.000 11.98653 ? 168 GLN A O    1 
ATOM   1364 C  CB   . GLN A 1 182 ? 36.01910 37.92266 23.66551  1.000 12.73803 ? 168 GLN A CB   1 
ATOM   1365 C  CG   . GLN A 1 182 ? 34.67944 37.21543 23.45761  1.000 22.24311 ? 168 GLN A CG   1 
ATOM   1366 C  CD   . GLN A 1 182 ? 34.27644 37.14356 21.99457  1.000 24.45459 ? 168 GLN A CD   1 
ATOM   1367 O  OE1  . GLN A 1 182 ? 35.00400 36.58991 21.16165  1.000 43.59786 ? 168 GLN A OE1  1 
ATOM   1368 N  NE2  . GLN A 1 182 ? 33.12512 37.72979 21.66680  1.000 33.53931 ? 168 GLN A NE2  1 
ATOM   1369 N  N    . GLN A 1 183 ? 38.42651 39.80320 23.29171  1.000 9.61593  ? 169 GLN A N    1 
ATOM   1370 C  CA   . GLN A 1 183 ? 39.67234 40.39062 23.76063  1.000 13.71654 ? 169 GLN A CA   1 
ATOM   1371 C  C    . GLN A 1 183 ? 40.11463 41.59616 22.94304  1.000 10.90076 ? 169 GLN A C    1 
ATOM   1372 O  O    . GLN A 1 183 ? 41.17520 42.16724 23.23322  1.000 13.96663 ? 169 GLN A O    1 
ATOM   1373 C  CB   . GLN A 1 183 ? 40.78610 39.32852 23.80585  1.000 11.77541 ? 169 GLN A CB   1 
ATOM   1374 C  CG   . GLN A 1 183 ? 40.61119 38.28395 24.92348  1.000 10.84643 ? 169 GLN A CG   1 
ATOM   1375 C  CD   . GLN A 1 183 ? 41.76677 37.28746 25.01531  1.000 13.88267 ? 169 GLN A CD   1 
ATOM   1376 O  OE1  . GLN A 1 183 ? 41.55632 36.07219 25.04611  1.000 19.66294 ? 169 GLN A OE1  1 
ATOM   1377 N  NE2  . GLN A 1 183 ? 42.98333 37.79401 25.06693  1.000 14.90915 ? 169 GLN A NE2  1 
ATOM   1378 N  N    . LYS A 1 184 ? 39.33965 41.98741 21.92935  1.000 12.98108 ? 170 LYS A N    1 
ATOM   1379 C  CA   . LYS A 1 184 ? 39.67404 43.11152 21.05635  1.000 14.76777 ? 170 LYS A CA   1 
ATOM   1380 C  C    . LYS A 1 184 ? 41.05806 42.92311 20.42916  1.000 14.31106 ? 170 LYS A C    1 
ATOM   1381 O  O    . LYS A 1 184 ? 41.94782 43.77179 20.54015  1.000 15.82636 ? 170 LYS A O    1 
ATOM   1382 C  CB   . LYS A 1 184 ? 39.54362 44.45714 21.77966  1.000 15.25464 ? 170 LYS A CB   1 
ATOM   1383 C  CG   . LYS A 1 184 ? 38.21488 44.65578 22.50373  1.000 26.98470 ? 170 LYS A CG   1 
ATOM   1384 C  CD   . LYS A 1 184 ? 37.05299 44.75642 21.53259  1.000 23.72609 ? 170 LYS A CD   1 
ATOM   1385 C  CE   . LYS A 1 184 ? 35.74747 45.17198 22.21257  1.000 21.65708 ? 170 LYS A CE   1 
ATOM   1386 N  NZ   . LYS A 1 184 ? 34.89898 44.01884 22.63002  1.000 20.16308 ? 170 LYS A NZ   1 
ATOM   1387 N  N    A LYS A 1 185 ? 41.21987 41.79745 19.73305  0.549 12.64497 ? 171 LYS A N    1 
ATOM   1388 N  N    B LYS A 1 185 ? 41.24639 41.76421 19.81014  0.451 12.70175 ? 171 LYS A N    1 
ATOM   1389 C  CA   A LYS A 1 185 ? 42.49695 41.43300 19.12828  0.549 11.06162 ? 171 LYS A CA   1 
ATOM   1390 C  CA   B LYS A 1 185 ? 42.47377 41.43618 19.10771  0.451 11.09056 ? 171 LYS A CA   1 
ATOM   1391 C  C    A LYS A 1 185 ? 42.30591 41.13306 17.64889  0.549 11.45853 ? 171 LYS A C    1 
ATOM   1392 C  C    B LYS A 1 185 ? 42.17305 41.35108 17.61991  0.451 10.96923 ? 171 LYS A C    1 
ATOM   1393 O  O    A LYS A 1 185 ? 41.42699 40.34507 17.28228  0.549 10.62975 ? 171 LYS A O    1 
ATOM   1394 O  O    B LYS A 1 185 ? 41.07673 40.95761 17.21461  0.451 11.73363 ? 171 LYS A O    1 
ATOM   1395 C  CB   A LYS A 1 185 ? 43.10467 40.21182 19.81714  0.549 11.07390 ? 171 LYS A CB   1 
ATOM   1396 C  CB   B LYS A 1 185 ? 43.04087 40.09274 19.57913  0.451 10.65843 ? 171 LYS A CB   1 
ATOM   1397 C  CG   A LYS A 1 185 ? 44.24321 39.60091 19.03842  0.549 10.23021 ? 171 LYS A CG   1 
ATOM   1398 C  CG   B LYS A 1 185 ? 43.24127 39.98471 21.08213  0.451 16.26270 ? 171 LYS A CG   1 
ATOM   1399 C  CD   A LYS A 1 185 ? 45.15160 38.78748 19.92707  0.549 21.61133 ? 171 LYS A CD   1 
ATOM   1400 C  CD   B LYS A 1 185 ? 44.00056 38.71813 21.44837  0.451 15.39911 ? 171 LYS A CD   1 
ATOM   1401 C  CE   A LYS A 1 185 ? 44.42153 37.62074 20.54031  0.549 15.40847 ? 171 LYS A CE   1 
ATOM   1402 C  CE   B LYS A 1 185 ? 45.42160 38.76211 20.90136  0.451 20.89889 ? 171 LYS A CE   1 
ATOM   1403 N  NZ   A LYS A 1 185 ? 45.31928 36.84513 21.43150  0.549 27.65004 ? 171 LYS A NZ   1 
ATOM   1404 N  NZ   B LYS A 1 185 ? 46.24377 37.57439 21.26708  0.451 20.77613 ? 171 LYS A NZ   1 
ATOM   1405 N  N    . LEU A 1 186 ? 43.15386 41.72999 16.81031  1.000 9.08316  ? 172 LEU A N    1 
ATOM   1406 C  CA   . LEU A 1 186 ? 43.03829 41.64102 15.35938  1.000 8.38490  ? 172 LEU A CA   1 
ATOM   1407 C  C    . LEU A 1 186 ? 44.34302 41.11779 14.76935  1.000 7.86404  ? 172 LEU A C    1 
ATOM   1408 O  O    . LEU A 1 186 ? 45.43189 41.55456 15.16136  1.000 9.53255  ? 172 LEU A O    1 
ATOM   1409 C  CB   . LEU A 1 186 ? 42.70386 43.02296 14.76175  1.000 8.62358  ? 172 LEU A CB   1 
ATOM   1410 C  CG   . LEU A 1 186 ? 42.54120 43.16876 13.23994  1.000 7.59750  ? 172 LEU A CG   1 
ATOM   1411 C  CD1  . LEU A 1 186 ? 41.53383 44.28199 12.88821  1.000 11.09605 ? 172 LEU A CD1  1 
ATOM   1412 C  CD2  . LEU A 1 186 ? 43.87548 43.43715 12.54901  1.000 5.09984  ? 172 LEU A CD2  1 
ATOM   1413 N  N    . ARG A 1 187 ? 44.23352 40.20564 13.79932  1.000 5.85714  ? 173 ARG A N    1 
ATOM   1414 C  CA   . ARG A 1 187 ? 45.41118 39.71644 13.08985  1.000 8.52646  ? 173 ARG A CA   1 
ATOM   1415 C  C    . ARG A 1 187 ? 45.12623 39.67894 11.59912  1.000 8.45635  ? 173 ARG A C    1 
ATOM   1416 O  O    . ARG A 1 187 ? 44.08336 39.17085 11.17976  1.000 11.04505 ? 173 ARG A O    1 
ATOM   1417 C  CB   . ARG A 1 187 ? 45.78354 38.30870 13.56076  1.000 6.27201  ? 173 ARG A CB   1 
ATOM   1418 C  CG   . ARG A 1 187 ? 46.27665 38.24708 15.00012  1.000 7.73973  ? 173 ARG A CG   1 
ATOM   1419 C  CD   . ARG A 1 187 ? 47.58311 39.01766 15.17297  1.000 6.10506  ? 173 ARG A CD   1 
ATOM   1420 N  NE   . ARG A 1 187 ? 48.12801 38.81323 16.51166  1.000 10.93619 ? 173 ARG A NE   1 
ATOM   1421 C  CZ   . ARG A 1 187 ? 47.90086 39.61908 17.54058  1.000 17.79786 ? 173 ARG A CZ   1 
ATOM   1422 N  NH1  . ARG A 1 187 ? 47.13927 40.69483 17.42007  1.000 11.92430 ? 173 ARG A NH1  1 
ATOM   1423 N  NH2  . ARG A 1 187 ? 48.44745 39.33696 18.71887  1.000 14.74466 ? 173 ARG A NH2  1 
ATOM   1424 N  N    . LEU A 1 188 ? 46.05874 40.20446 10.81076  1.000 4.34989  ? 174 LEU A N    1 
ATOM   1425 C  CA   . LEU A 1 188 ? 46.03386 40.07280 9.35913   1.000 5.44476  ? 174 LEU A CA   1 
ATOM   1426 C  C    . LEU A 1 188 ? 46.73646 38.77294 8.99404   1.000 4.45039  ? 174 LEU A C    1 
ATOM   1427 O  O    . LEU A 1 188 ? 47.92070 38.59063 9.31286   1.000 5.88848  ? 174 LEU A O    1 
ATOM   1428 C  CB   . LEU A 1 188 ? 46.76528 41.25717 8.72849   1.000 5.68702  ? 174 LEU A CB   1 
ATOM   1429 C  CG   . LEU A 1 188 ? 46.84766 41.34298 7.20439   1.000 6.95633  ? 174 LEU A CG   1 
ATOM   1430 C  CD1  . LEU A 1 188 ? 45.46789 41.17723 6.56332   1.000 8.63026  ? 174 LEU A CD1  1 
ATOM   1431 C  CD2  . LEU A 1 188 ? 47.50440 42.67296 6.78326   1.000 9.37519  ? 174 LEU A CD2  1 
ATOM   1432 N  N    . ILE A 1 189 ? 46.00219 37.86219 8.34862   1.000 7.28939  ? 175 ILE A N    1 
ATOM   1433 C  CA   . ILE A 1 189 ? 46.49127 36.51802 8.04472   1.000 6.02865  ? 175 ILE A CA   1 
ATOM   1434 C  C    . ILE A 1 189 ? 46.63012 36.29098 6.54334   1.000 6.96201  ? 175 ILE A C    1 
ATOM   1435 O  O    . ILE A 1 189 ? 46.30438 37.16393 5.73508   1.000 7.84492  ? 175 ILE A O    1 
ATOM   1436 C  CB   . ILE A 1 189 ? 45.55680 35.45168 8.65255   1.000 8.64318  ? 175 ILE A CB   1 
ATOM   1437 C  CG1  . ILE A 1 189 ? 44.18909 35.48503 7.96279   1.000 5.43257  ? 175 ILE A CG1  1 
ATOM   1438 C  CG2  . ILE A 1 189 ? 45.39166 35.65967 10.15532  1.000 7.84553  ? 175 ILE A CG2  1 
ATOM   1439 C  CD1  . ILE A 1 189 ? 43.42564 34.15791 8.05048   1.000 5.84816  ? 175 ILE A CD1  1 
ATOM   1440 N  N    . ASP A 1 190 ? 47.05990 35.07536 6.17869   1.000 6.13252  ? 176 ASP A N    1 
ATOM   1441 C  CA   . ASP A 1 190 ? 47.20805 34.56220 4.81813   1.000 7.38698  ? 176 ASP A CA   1 
ATOM   1442 C  C    . ASP A 1 190 ? 48.05215 35.44160 3.91465   1.000 6.65580  ? 176 ASP A C    1 
ATOM   1443 O  O    . ASP A 1 190 ? 47.54076 36.17707 3.05340   1.000 8.45357  ? 176 ASP A O    1 
ATOM   1444 C  CB   . ASP A 1 190 ? 45.89160 34.16909 4.15184   1.000 6.02595  ? 176 ASP A CB   1 
ATOM   1445 C  CG   . ASP A 1 190 ? 46.11345 33.22146 2.97332   1.000 18.28316 ? 176 ASP A CG   1 
ATOM   1446 O  OD1  . ASP A 1 190 ? 47.29126 32.96770 2.63863   1.000 11.01419 ? 176 ASP A OD1  1 
ATOM   1447 O  OD2  . ASP A 1 190 ? 45.12590 32.71634 2.39528   1.000 17.38738 ? 176 ASP A OD2  1 
ATOM   1448 N  N    . TRP A 1 191 ? 49.36016 35.29739 4.07793   1.000 7.13064  ? 177 TRP A N    1 
ATOM   1449 C  CA   . TRP A 1 191 ? 50.36879 36.02986 3.33751   1.000 5.11481  ? 177 TRP A CA   1 
ATOM   1450 C  C    . TRP A 1 191 ? 50.82173 35.28036 2.08763   1.000 4.85597  ? 177 TRP A C    1 
ATOM   1451 O  O    . TRP A 1 191 ? 51.89698 35.56371 1.54121   1.000 8.32196  ? 177 TRP A O    1 
ATOM   1452 C  CB   . TRP A 1 191 ? 51.52086 36.38351 4.29216   1.000 9.13579  ? 177 TRP A CB   1 
ATOM   1453 C  CG   . TRP A 1 191 ? 51.03073 37.31956 5.39622   1.000 7.86402  ? 177 TRP A CG   1 
ATOM   1454 C  CD1  . TRP A 1 191 ? 50.38288 36.96556 6.55732   1.000 7.39643  ? 177 TRP A CD1  1 
ATOM   1455 C  CD2  . TRP A 1 191 ? 51.08960 38.75286 5.39457   1.000 6.85092  ? 177 TRP A CD2  1 
ATOM   1456 N  NE1  . TRP A 1 191 ? 50.06262 38.09226 7.28095   1.000 6.42577  ? 177 TRP A NE1  1 
ATOM   1457 C  CE2  . TRP A 1 191 ? 50.48115 39.19922 6.58557   1.000 3.77384  ? 177 TRP A CE2  1 
ATOM   1458 C  CE3  . TRP A 1 191 ? 51.61953 39.70520 4.50256   1.000 4.50639  ? 177 TRP A CE3  1 
ATOM   1459 C  CZ2  . TRP A 1 191 ? 50.38152 40.55032 6.91081   1.000 6.47546  ? 177 TRP A CZ2  1 
ATOM   1460 C  CZ3  . TRP A 1 191 ? 51.52323 41.04812 4.82002   1.000 5.42831  ? 177 TRP A CZ3  1 
ATOM   1461 C  CH2  . TRP A 1 191 ? 50.90041 41.46274 6.01749   1.000 6.42022  ? 177 TRP A CH2  1 
ATOM   1462 N  N    . GLY A 1 192 ? 50.00165 34.34063 1.60827   1.000 5.17216  ? 178 GLY A N    1 
ATOM   1463 C  CA   . GLY A 1 192 ? 50.38159 33.53446 0.46229   1.000 8.16298  ? 178 GLY A CA   1 
ATOM   1464 C  C    . GLY A 1 192 ? 50.32118 34.26277 -0.86725  1.000 8.57295  ? 178 GLY A C    1 
ATOM   1465 O  O    . GLY A 1 192 ? 50.91263 33.79226 -1.84277  1.000 12.42293 ? 178 GLY A O    1 
ATOM   1466 N  N    . LEU A 1 193 ? 49.62586 35.39701 -0.93636  1.000 6.72043  ? 179 LEU A N    1 
ATOM   1467 C  CA   . LEU A 1 193 ? 49.64307 36.22664 -2.13667  1.000 10.82093 ? 179 LEU A CA   1 
ATOM   1468 C  C    . LEU A 1 193 ? 50.53884 37.45157 -2.00548  1.000 7.10320  ? 179 LEU A C    1 
ATOM   1469 O  O    . LEU A 1 193 ? 50.65805 38.21909 -2.96525  1.000 6.06177  ? 179 LEU A O    1 
ATOM   1470 C  CB   . LEU A 1 193 ? 48.22738 36.67236 -2.53049  1.000 11.84820 ? 179 LEU A CB   1 
ATOM   1471 C  CG   . LEU A 1 193 ? 47.26314 35.60446 -3.06776  1.000 17.76534 ? 179 LEU A CG   1 
ATOM   1472 C  CD1  . LEU A 1 193 ? 45.95069 36.24279 -3.52311  1.000 13.07553 ? 179 LEU A CD1  1 
ATOM   1473 C  CD2  . LEU A 1 193 ? 47.88821 34.78970 -4.19582  1.000 23.12894 ? 179 LEU A CD2  1 
ATOM   1474 N  N    . ALA A 1 194 ? 51.15917 37.66169 -0.85021  1.000 4.59733  ? 180 ALA A N    1 
ATOM   1475 C  CA   . ALA A 1 194 ? 51.95601 38.86321 -0.63321  1.000 4.11707  ? 180 ALA A CA   1 
ATOM   1476 C  C    . ALA A 1 194 ? 53.20633 38.86350 -1.51594  1.000 7.63103  ? 180 ALA A C    1 
ATOM   1477 O  O    . ALA A 1 194 ? 53.69196 37.82491 -1.95870  1.000 6.69401  ? 180 ALA A O    1 
ATOM   1478 C  CB   . ALA A 1 194 ? 52.32659 38.98914 0.84867   1.000 6.16620  ? 180 ALA A CB   1 
ATOM   1479 N  N    . GLU A 1 195 ? 53.73448 40.05645 -1.76930  1.000 7.94274  ? 181 GLU A N    1 
ATOM   1480 C  CA   . GLU A 1 195 ? 54.84436 40.19857 -2.70066  1.000 5.68973  ? 181 GLU A CA   1 
ATOM   1481 C  C    . GLU A 1 195 ? 55.68408 41.40396 -2.29543  1.000 6.42711  ? 181 GLU A C    1 
ATOM   1482 O  O    . GLU A 1 195 ? 55.19140 42.33018 -1.64609  1.000 8.03598  ? 181 GLU A O    1 
ATOM   1483 C  CB   . GLU A 1 195 ? 54.30605 40.34980 -4.13583  1.000 11.79496 ? 181 GLU A CB   1 
ATOM   1484 C  CG   . GLU A 1 195 ? 55.31282 40.44128 -5.28084  1.000 17.82757 ? 181 GLU A CG   1 
ATOM   1485 C  CD   . GLU A 1 195 ? 56.35235 39.33070 -5.30275  1.000 14.32009 ? 181 GLU A CD   1 
ATOM   1486 O  OE1  . GLU A 1 195 ? 57.27820 39.37333 -4.47637  1.000 13.68404 ? 181 GLU A OE1  1 
ATOM   1487 O  OE2  . GLU A 1 195 ? 56.26706 38.42745 -6.16685  1.000 26.92163 ? 181 GLU A OE2  1 
ATOM   1488 N  N    . PHE A 1 196 ? 56.96181 41.37372 -2.67378  1.000 4.66997  ? 182 PHE A N    1 
ATOM   1489 C  CA   . PHE A 1 196 ? 57.85446 42.50864 -2.44740  1.000 6.42706  ? 182 PHE A CA   1 
ATOM   1490 C  C    . PHE A 1 196 ? 57.61136 43.58267 -3.49769  1.000 8.17931  ? 182 PHE A C    1 
ATOM   1491 O  O    . PHE A 1 196 ? 57.51414 43.29157 -4.69528  1.000 10.59838 ? 182 PHE A O    1 
ATOM   1492 C  CB   . PHE A 1 196 ? 59.31890 42.05622 -2.53323  1.000 8.29022  ? 182 PHE A CB   1 
ATOM   1493 C  CG   . PHE A 1 196 ? 59.73539 41.12666 -1.42630  1.000 6.72946  ? 182 PHE A CG   1 
ATOM   1494 C  CD1  . PHE A 1 196 ? 59.57922 39.75671 -1.56003  1.000 9.26899  ? 182 PHE A CD1  1 
ATOM   1495 C  CD2  . PHE A 1 196 ? 60.26402 41.62616 -0.24438  1.000 7.93928  ? 182 PHE A CD2  1 
ATOM   1496 C  CE1  . PHE A 1 196 ? 59.95405 38.89765 -0.54901  1.000 11.76647 ? 182 PHE A CE1  1 
ATOM   1497 C  CE2  . PHE A 1 196 ? 60.64436 40.76460 0.78449   1.000 11.87957 ? 182 PHE A CE2  1 
ATOM   1498 C  CZ   . PHE A 1 196 ? 60.48360 39.39809 0.63007   1.000 7.54275  ? 182 PHE A CZ   1 
ATOM   1499 N  N    . TYR A 1 197 ? 57.54883 44.83392 -3.05766  1.000 8.30324  ? 183 TYR A N    1 
ATOM   1500 C  CA   . TYR A 1 197 ? 57.39788 45.94857 -3.98357  1.000 6.34635  ? 183 TYR A CA   1 
ATOM   1501 C  C    . TYR A 1 197 ? 58.76291 46.40677 -4.49856  1.000 8.01318  ? 183 TYR A C    1 
ATOM   1502 O  O    . TYR A 1 197 ? 59.64922 46.75442 -3.71092  1.000 8.33999  ? 183 TYR A O    1 
ATOM   1503 C  CB   . TYR A 1 197 ? 56.65561 47.12420 -3.34589  1.000 6.69812  ? 183 TYR A CB   1 
ATOM   1504 C  CG   . TYR A 1 197 ? 56.60619 48.28362 -4.29862  1.000 6.18978  ? 183 TYR A CG   1 
ATOM   1505 C  CD1  . TYR A 1 197 ? 55.78078 48.25253 -5.41654  1.000 5.81324  ? 183 TYR A CD1  1 
ATOM   1506 C  CD2  . TYR A 1 197 ? 57.43457 49.38269 -4.12700  1.000 10.63104 ? 183 TYR A CD2  1 
ATOM   1507 C  CE1  . TYR A 1 197 ? 55.76092 49.28395 -6.31041  1.000 11.14821 ? 183 TYR A CE1  1 
ATOM   1508 C  CE2  . TYR A 1 197 ? 57.41090 50.43297 -5.01723  1.000 10.70334 ? 183 TYR A CE2  1 
ATOM   1509 C  CZ   . TYR A 1 197 ? 56.57463 50.37586 -6.10799  1.000 13.25014 ? 183 TYR A CZ   1 
ATOM   1510 O  OH   . TYR A 1 197 ? 56.55424 51.41493 -6.99252  1.000 10.78370 ? 183 TYR A OH   1 
ATOM   1511 N  N    . HIS A 1 198 ? 58.91190 46.42338 -5.82484  1.000 7.98058  ? 184 HIS A N    1 
ATOM   1512 C  CA   . HIS A 1 198 ? 60.07730 46.97012 -6.49898  1.000 7.93239  ? 184 HIS A CA   1 
ATOM   1513 C  C    . HIS A 1 198 ? 59.59125 48.00058 -7.51068  1.000 9.72821  ? 184 HIS A C    1 
ATOM   1514 O  O    . HIS A 1 198 ? 58.72246 47.68426 -8.34014  1.000 11.61854 ? 184 HIS A O    1 
ATOM   1515 C  CB   . HIS A 1 198 ? 60.84476 45.84852 -7.20154  1.000 11.12001 ? 184 HIS A CB   1 
ATOM   1516 C  CG   . HIS A 1 198 ? 61.37665 44.80722 -6.26457  1.000 11.13770 ? 184 HIS A CG   1 
ATOM   1517 N  ND1  . HIS A 1 198 ? 62.47812 45.02090 -5.46409  1.000 16.35039 ? 184 HIS A ND1  1 
ATOM   1518 C  CD2  . HIS A 1 198 ? 60.94977 43.55221 -5.98888  1.000 12.20397 ? 184 HIS A CD2  1 
ATOM   1519 C  CE1  . HIS A 1 198 ? 62.71393 43.93764 -4.74529  1.000 11.72340 ? 184 HIS A CE1  1 
ATOM   1520 N  NE2  . HIS A 1 198 ? 61.79925 43.03293 -5.04234  1.000 12.13381 ? 184 HIS A NE2  1 
ATOM   1521 N  N    . PRO A 1 199 ? 60.13877 49.21994 -7.50482  1.000 11.26026 ? 185 PRO A N    1 
ATOM   1522 C  CA   . PRO A 1 199 ? 59.63432 50.26690 -8.40557  1.000 10.91808 ? 185 PRO A CA   1 
ATOM   1523 C  C    . PRO A 1 199 ? 59.72390 49.84746 -9.86457  1.000 9.56264  ? 185 PRO A C    1 
ATOM   1524 O  O    . PRO A 1 199 ? 60.71416 49.25439 -10.29909 1.000 12.90959 ? 185 PRO A O    1 
ATOM   1525 C  CB   . PRO A 1 199 ? 60.57269 51.45320 -8.14008  1.000 17.68039 ? 185 PRO A CB   1 
ATOM   1526 C  CG   . PRO A 1 199 ? 61.21257 51.18317 -6.87833  1.000 22.47100 ? 185 PRO A CG   1 
ATOM   1527 C  CD   . PRO A 1 199 ? 61.26064 49.69478 -6.68439  1.000 15.75793 ? 185 PRO A CD   1 
ATOM   1528 N  N    . ALA A 1 200 ? 58.67989 50.17661 -10.61946 1.000 12.60370 ? 186 ALA A N    1 
ATOM   1529 C  CA   . ALA A 1 200 ? 58.54816 49.90296 -12.04716 1.000 13.88472 ? 186 ALA A CA   1 
ATOM   1530 C  C    . ALA A 1 200 ? 58.31287 48.43123 -12.37898 1.000 16.73471 ? 186 ALA A C    1 
ATOM   1531 O  O    . ALA A 1 200 ? 58.20657 48.09003 -13.56238 1.000 18.22598 ? 186 ALA A O    1 
ATOM   1532 C  CB   . ALA A 1 200 ? 59.71092 50.46312 -12.88045 1.000 11.72406 ? 186 ALA A CB   1 
ATOM   1533 N  N    . GLN A 1 201 ? 58.21856 47.54750 -11.39102 1.000 12.60709 ? 187 GLN A N    1 
ATOM   1534 C  CA   . GLN A 1 201 ? 57.95511 46.14704 -11.68181 1.000 12.75287 ? 187 GLN A CA   1 
ATOM   1535 C  C    . GLN A 1 201 ? 56.48975 45.95392 -12.04595 1.000 12.00082 ? 187 GLN A C    1 
ATOM   1536 O  O    . GLN A 1 201 ? 55.59760 46.55734 -11.44282 1.000 14.43674 ? 187 GLN A O    1 
ATOM   1537 C  CB   . GLN A 1 201 ? 58.30789 45.28398 -10.46885 1.000 15.43983 ? 187 GLN A CB   1 
ATOM   1538 C  CG   . GLN A 1 201 ? 58.23415 43.77922 -10.72591 1.000 16.55058 ? 187 GLN A CG   1 
ATOM   1539 C  CD   . GLN A 1 201 ? 59.02176 42.98763 -9.69417  1.000 25.55488 ? 187 GLN A CD   1 
ATOM   1540 O  OE1  . GLN A 1 201 ? 60.16588 43.32763 -9.37595  1.000 26.76384 ? 187 GLN A OE1  1 
ATOM   1541 N  NE2  . GLN A 1 201 ? 58.40858 41.93693 -9.15576  1.000 25.32534 ? 187 GLN A NE2  1 
ATOM   1542 N  N    . GLU A 1 202 ? 56.23706 45.12020 -13.05252 1.000 11.73794 ? 188 GLU A N    1 
ATOM   1543 C  CA   . GLU A 1 202 ? 54.87289 44.81203 -13.45408 1.000 10.34638 ? 188 GLU A CA   1 
ATOM   1544 C  C    . GLU A 1 202 ? 54.42848 43.53299 -12.76118 1.000 14.87071 ? 188 GLU A C    1 
ATOM   1545 O  O    . GLU A 1 202 ? 55.10444 42.50468 -12.84986 1.000 14.70070 ? 188 GLU A O    1 
ATOM   1546 C  CB   . GLU A 1 202 ? 54.75872 44.69255 -14.97742 1.000 15.57206 ? 188 GLU A CB   1 
ATOM   1547 C  CG   . GLU A 1 202 ? 54.89147 46.04525 -15.67186 1.000 16.49949 ? 188 GLU A CG   1 
ATOM   1548 C  CD   . GLU A 1 202 ? 54.31421 46.06274 -17.07061 1.000 33.74600 ? 188 GLU A CD   1 
ATOM   1549 O  OE1  . GLU A 1 202 ? 53.92468 44.98369 -17.57330 1.000 35.27511 ? 188 GLU A OE1  1 
ATOM   1550 O  OE2  . GLU A 1 202 ? 54.24127 47.16387 -17.66398 1.000 22.97630 ? 188 GLU A OE2  1 
ATOM   1551 N  N    . TYR A 1 203 ? 53.29983 43.59944 -12.06757 1.000 9.25093  ? 189 TYR A N    1 
ATOM   1552 C  CA   . TYR A 1 203 ? 52.83740 42.49242 -11.24551 1.000 6.54758  ? 189 TYR A CA   1 
ATOM   1553 C  C    . TYR A 1 203 ? 51.58983 41.86190 -11.84846 1.000 15.37987 ? 189 TYR A C    1 
ATOM   1554 O  O    . TYR A 1 203 ? 50.86870 42.48435 -12.63332 1.000 11.76621 ? 189 TYR A O    1 
ATOM   1555 C  CB   . TYR A 1 203 ? 52.53060 42.97496 -9.82322  1.000 7.87522  ? 189 TYR A CB   1 
ATOM   1556 C  CG   . TYR A 1 203 ? 53.76461 43.39288 -9.06499  1.000 10.35320 ? 189 TYR A CG   1 
ATOM   1557 C  CD1  . TYR A 1 203 ? 54.50560 42.46486 -8.33708  1.000 11.39208 ? 189 TYR A CD1  1 
ATOM   1558 C  CD2  . TYR A 1 203 ? 54.19615 44.71299 -9.07302  1.000 8.32068  ? 189 TYR A CD2  1 
ATOM   1559 C  CE1  . TYR A 1 203 ? 55.64022 42.84648 -7.64112  1.000 7.03502  ? 189 TYR A CE1  1 
ATOM   1560 C  CE2  . TYR A 1 203 ? 55.32636 45.09795 -8.37534  1.000 8.20554  ? 189 TYR A CE2  1 
ATOM   1561 C  CZ   . TYR A 1 203 ? 56.04006 44.16054 -7.66522  1.000 9.37757  ? 189 TYR A CZ   1 
ATOM   1562 O  OH   . TYR A 1 203 ? 57.16181 44.53702 -6.97367  1.000 10.23175 ? 189 TYR A OH   1 
ATOM   1563 N  N    . ASN A 1 204 ? 51.34051 40.61093 -11.46089 1.000 12.75951 ? 190 ASN A N    1 
ATOM   1564 C  CA   . ASN A 1 204 ? 50.15613 39.89559 -11.92498 1.000 12.21194 ? 190 ASN A CA   1 
ATOM   1565 C  C    . ASN A 1 204 ? 48.91035 40.50787 -11.30054 1.000 12.02362 ? 190 ASN A C    1 
ATOM   1566 O  O    . ASN A 1 204 ? 48.86504 40.73840 -10.09217 1.000 13.75123 ? 190 ASN A O    1 
ATOM   1567 C  CB   . ASN A 1 204 ? 50.26834 38.42362 -11.52702 1.000 17.69463 ? 190 ASN A CB   1 
ATOM   1568 C  CG   . ASN A 1 204 ? 49.29995 37.53317 -12.28333 1.000 18.65364 ? 190 ASN A CG   1 
ATOM   1569 O  OD1  . ASN A 1 204 ? 48.13562 37.87553 -12.47887 1.000 18.07879 ? 190 ASN A OD1  1 
ATOM   1570 N  ND2  . ASN A 1 204 ? 49.78311 36.37569 -12.71346 1.000 23.92801 ? 190 ASN A ND2  1 
ATOM   1571 N  N    . VAL A 1 205 ? 47.89653 40.79617 -12.12668 1.000 8.78105  ? 191 VAL A N    1 
ATOM   1572 C  CA   . VAL A 1 205 ? 46.67839 41.41745 -11.61100 1.000 9.12781  ? 191 VAL A CA   1 
ATOM   1573 C  C    . VAL A 1 205 ? 45.67986 40.39053 -11.09079 1.000 9.49428  ? 191 VAL A C    1 
ATOM   1574 O  O    . VAL A 1 205 ? 44.62198 40.77541 -10.58003 1.000 10.34157 ? 191 VAL A O    1 
ATOM   1575 C  CB   . VAL A 1 205 ? 46.02035 42.35826 -12.64416 1.000 7.30176  ? 191 VAL A CB   1 
ATOM   1576 C  CG1  . VAL A 1 205 ? 46.99439 43.46423 -13.06188 1.000 11.16850 ? 191 VAL A CG1  1 
ATOM   1577 C  CG2  . VAL A 1 205 ? 45.52572 41.55626 -13.84707 1.000 11.86456 ? 191 VAL A CG2  1 
ATOM   1578 N  N    . ARG A 1 206 ? 45.97967 39.09462 -11.20867 1.000 10.80078 ? 192 ARG A N    1 
ATOM   1579 C  CA   . ARG A 1 206 ? 45.10340 38.04128 -10.68714 1.000 12.38955 ? 192 ARG A CA   1 
ATOM   1580 C  C    . ARG A 1 206 ? 45.41627 37.81115 -9.20688  1.000 15.23869 ? 192 ARG A C    1 
ATOM   1581 O  O    . ARG A 1 206 ? 45.90607 36.76225 -8.78365  1.000 15.62715 ? 192 ARG A O    1 
ATOM   1582 C  CB   . ARG A 1 206 ? 45.24995 36.76455 -11.50177 1.000 21.10021 ? 192 ARG A CB   1 
ATOM   1583 C  CG   . ARG A 1 206 ? 44.92465 36.93791 -12.97946 1.000 29.10745 ? 192 ARG A CG   1 
ATOM   1584 C  CD   . ARG A 1 206 ? 45.08382 35.63326 -13.75839 1.000 45.42564 ? 192 ARG A CD   1 
ATOM   1585 N  NE   . ARG A 1 206 ? 44.16519 34.60008 -13.29135 1.000 76.94713 ? 192 ARG A NE   1 
ATOM   1586 C  CZ   . ARG A 1 206 ? 42.88208 34.52512 -13.62206 1.000 64.28253 ? 192 ARG A CZ   1 
ATOM   1587 N  NH1  . ARG A 1 206 ? 42.31750 35.42135 -14.41698 1.000 46.45694 ? 192 ARG A NH1  1 
ATOM   1588 N  NH2  . ARG A 1 206 ? 42.14534 33.52858 -13.13836 1.000 60.41543 ? 192 ARG A NH2  1 
ATOM   1589 N  N    . VAL A 1 207 ? 45.13462 38.84614 -8.41733  1.000 12.79660 ? 193 VAL A N    1 
ATOM   1590 C  CA   . VAL A 1 207 ? 45.29880 38.83661 -6.97186  1.000 12.13173 ? 193 VAL A CA   1 
ATOM   1591 C  C    . VAL A 1 207 ? 44.04145 39.45488 -6.36996  1.000 13.29512 ? 193 VAL A C    1 
ATOM   1592 O  O    . VAL A 1 207 ? 43.22263 40.04916 -7.07386  1.000 11.41459 ? 193 VAL A O    1 
ATOM   1593 C  CB   . VAL A 1 207 ? 46.57017 39.58710 -6.51213  1.000 11.14168 ? 193 VAL A CB   1 
ATOM   1594 C  CG1  . VAL A 1 207 ? 47.82322 38.95502 -7.11951  1.000 13.95031 ? 193 VAL A CG1  1 
ATOM   1595 C  CG2  . VAL A 1 207 ? 46.48714 41.05494 -6.88046  1.000 10.91941 ? 193 VAL A CG2  1 
ATOM   1596 N  N    . ALA A 1 208 ? 43.89298 39.29076 -5.04755  1.000 16.83839 ? 194 ALA A N    1 
ATOM   1597 C  CA   . ALA A 1 208 ? 42.72652 39.73005 -4.27901  1.000 13.42935 ? 194 ALA A CA   1 
ATOM   1598 C  C    . ALA A 1 208 ? 41.41201 39.05243 -4.67447  1.000 13.98374 ? 194 ALA A C    1 
ATOM   1599 O  O    . ALA A 1 208 ? 41.26315 38.53456 -5.78435  1.000 18.50573 ? 194 ALA A O    1 
ATOM   1600 C  CB   . ALA A 1 208 ? 42.57428 41.26029 -4.28171  1.000 13.08512 ? 194 ALA A CB   1 
ATOM   1601 N  N    . SER A 1 209 ? 40.45406 39.04521 -3.75892  1.000 14.52033 ? 195 SER A N    1 
ATOM   1602 C  CA   . SER A 1 209 ? 39.11306 38.55993 -4.04821  1.000 15.58641 ? 195 SER A CA   1 
ATOM   1603 C  C    . SER A 1 209 ? 38.37286 39.59750 -4.88072  1.000 12.19518 ? 195 SER A C    1 
ATOM   1604 O  O    . SER A 1 209 ? 38.60538 40.80040 -4.73766  1.000 9.81018  ? 195 SER A O    1 
ATOM   1605 C  CB   . SER A 1 209 ? 38.34427 38.35726 -2.74028  1.000 19.97208 ? 195 SER A CB   1 
ATOM   1606 O  OG   . SER A 1 209 ? 36.94651 38.62220 -2.90504  1.000 22.76050 ? 195 SER A OG   1 
ATOM   1607 N  N    . ARG A 1 210 ? 37.46402 39.11811 -5.73910  1.000 12.80686 ? 196 ARG A N    1 
ATOM   1608 C  CA   . ARG A 1 210 ? 36.73401 39.99580 -6.65526  1.000 11.32408 ? 196 ARG A CA   1 
ATOM   1609 C  C    . ARG A 1 210 ? 36.25177 41.28254 -5.99254  1.000 9.01266  ? 196 ARG A C    1 
ATOM   1610 O  O    . ARG A 1 210 ? 36.49944 42.38416 -6.49919  1.000 8.76299  ? 196 ARG A O    1 
ATOM   1611 C  CB   . ARG A 1 210 ? 35.53805 39.25413 -7.25650  1.000 11.81175 ? 196 ARG A CB   1 
ATOM   1612 C  CG   . ARG A 1 210 ? 34.73444 40.11211 -8.24480  1.000 7.98825  ? 196 ARG A CG   1 
ATOM   1613 C  CD   . ARG A 1 210 ? 33.51865 39.35947 -8.70044  1.000 11.88636 ? 196 ARG A CD   1 
ATOM   1614 N  NE   . ARG A 1 210 ? 33.89576 38.02070 -9.12894  1.000 23.77431 ? 196 ARG A NE   1 
ATOM   1615 C  CZ   . ARG A 1 210 ? 33.13963 36.94482 -8.97257  1.000 26.73128 ? 196 ARG A CZ   1 
ATOM   1616 N  NH1  . ARG A 1 210 ? 31.96430 37.00791 -8.36341  1.000 30.94935 ? 196 ARG A NH1  1 
ATOM   1617 N  NH2  . ARG A 1 210 ? 33.57464 35.77575 -9.43371  1.000 32.85991 ? 196 ARG A NH2  1 
ATOM   1618 N  N    . TYR A 1 211 ? 35.58317 41.16400 -4.83645  1.000 7.32637  ? 197 TYR A N    1 
ATOM   1619 C  CA   . TYR A 1 211 ? 34.92517 42.32222 -4.24431  1.000 7.29130  ? 197 TYR A CA   1 
ATOM   1620 C  C    . TYR A 1 211 ? 35.91323 43.35124 -3.73418  1.000 7.00490  ? 197 TYR A C    1 
ATOM   1621 O  O    . TYR A 1 211 ? 35.52608 44.49688 -3.49671  1.000 7.29334  ? 197 TYR A O    1 
ATOM   1622 C  CB   . TYR A 1 211 ? 34.02538 41.88788 -3.09120  1.000 7.93701  ? 197 TYR A CB   1 
ATOM   1623 C  CG   . TYR A 1 211 ? 33.11891 40.75699 -3.48369  1.000 9.64202  ? 197 TYR A CG   1 
ATOM   1624 C  CD1  . TYR A 1 211 ? 32.44760 40.78143 -4.69728  1.000 9.16543  ? 197 TYR A CD1  1 
ATOM   1625 C  CD2  . TYR A 1 211 ? 32.94674 39.65651 -2.64928  1.000 10.10490 ? 197 TYR A CD2  1 
ATOM   1626 C  CE1  . TYR A 1 211 ? 31.61538 39.73729 -5.06817  1.000 12.20208 ? 197 TYR A CE1  1 
ATOM   1627 C  CE2  . TYR A 1 211 ? 32.11643 38.61728 -3.01305  1.000 15.82766 ? 197 TYR A CE2  1 
ATOM   1628 C  CZ   . TYR A 1 211 ? 31.45580 38.66676 -4.22606  1.000 14.52424 ? 197 TYR A CZ   1 
ATOM   1629 O  OH   . TYR A 1 211 ? 30.62841 37.63266 -4.60958  1.000 19.54763 ? 197 TYR A OH   1 
ATOM   1630 N  N    . PHE A 1 212 ? 37.17690 42.97012 -3.56917  1.000 6.19164  ? 198 PHE A N    1 
ATOM   1631 C  CA   . PHE A 1 212 ? 38.18564 43.82905 -2.97245  1.000 4.78372  ? 198 PHE A CA   1 
ATOM   1632 C  C    . PHE A 1 212 ? 39.27352 44.22209 -3.95922  1.000 5.39484  ? 198 PHE A C    1 
ATOM   1633 O  O    . PHE A 1 212 ? 40.23489 44.90183 -3.57348  1.000 7.90735  ? 198 PHE A O    1 
ATOM   1634 C  CB   . PHE A 1 212 ? 38.72128 43.17011 -1.69751  1.000 9.72252  ? 198 PHE A CB   1 
ATOM   1635 C  CG   . PHE A 1 212 ? 37.63125 42.90237 -0.71392  1.000 7.34927  ? 198 PHE A CG   1 
ATOM   1636 C  CD1  . PHE A 1 212 ? 36.90613 41.71768 -0.76958  1.000 9.43545  ? 198 PHE A CD1  1 
ATOM   1637 C  CD2  . PHE A 1 212 ? 37.25522 43.87969 0.19553   1.000 8.66285  ? 198 PHE A CD2  1 
ATOM   1638 C  CE1  . PHE A 1 212 ? 35.84915 41.50168 0.09836   1.000 12.69667 ? 198 PHE A CE1  1 
ATOM   1639 C  CE2  . PHE A 1 212 ? 36.20331 43.67504 1.06345   1.000 9.64712  ? 198 PHE A CE2  1 
ATOM   1640 C  CZ   . PHE A 1 212 ? 35.49063 42.48945 1.00571   1.000 10.59331 ? 198 PHE A CZ   1 
ATOM   1641 N  N    . LYS A 1 213 ? 39.12531 43.83335 -5.22784  1.000 8.72099  ? 199 LYS A N    1 
ATOM   1642 C  CA   . LYS A 1 213 ? 40.08436 44.20594 -6.26255  1.000 6.72129  ? 199 LYS A CA   1 
ATOM   1643 C  C    . LYS A 1 213 ? 40.00483 45.69604 -6.54338  1.000 6.25299  ? 199 LYS A C    1 
ATOM   1644 O  O    . LYS A 1 213 ? 38.92537 46.23685 -6.78642  1.000 8.75369  ? 199 LYS A O    1 
ATOM   1645 C  CB   . LYS A 1 213 ? 39.79293 43.44762 -7.55545  1.000 5.97900  ? 199 LYS A CB   1 
ATOM   1646 C  CG   . LYS A 1 213 ? 40.19219 42.00348 -7.52337  1.000 7.94305  ? 199 LYS A CG   1 
ATOM   1647 C  CD   . LYS A 1 213 ? 39.76902 41.33773 -8.80490  1.000 12.04257 ? 199 LYS A CD   1 
ATOM   1648 C  CE   . LYS A 1 213 ? 39.83872 39.82062 -8.69066  1.000 12.73539 ? 199 LYS A CE   1 
ATOM   1649 N  NZ   . LYS A 1 213 ? 41.20400 39.29782 -8.93041  1.000 18.41061 ? 199 LYS A NZ   1 
ATOM   1650 N  N    . GLY A 1 214 ? 41.15522 46.35759 -6.53245  1.000 6.32066  ? 200 GLY A N    1 
ATOM   1651 C  CA   . GLY A 1 214 ? 41.21248 47.75310 -6.88496  1.000 9.92573  ? 200 GLY A CA   1 
ATOM   1652 C  C    . GLY A 1 214 ? 40.98523 47.92021 -8.36921  1.000 9.33345  ? 200 GLY A C    1 
ATOM   1653 O  O    . GLY A 1 214 ? 41.23775 47.00567 -9.16722  1.000 7.64670  ? 200 GLY A O    1 
ATOM   1654 N  N    . PRO A 1 215 ? 40.48248 49.08744 -8.77095  1.000 6.15679  ? 201 PRO A N    1 
ATOM   1655 C  CA   . PRO A 1 215 ? 40.26349 49.33062 -10.21235 1.000 10.95806 ? 201 PRO A CA   1 
ATOM   1656 C  C    . PRO A 1 215 ? 41.49387 49.10142 -11.08184 1.000 10.64195 ? 201 PRO A C    1 
ATOM   1657 O  O    . PRO A 1 215 ? 41.34218 48.65718 -12.22781 1.000 11.58462 ? 201 PRO A O    1 
ATOM   1658 C  CB   . PRO A 1 215 ? 39.76079 50.78312 -10.27243 1.000 9.30094  ? 201 PRO A CB   1 
ATOM   1659 C  CG   . PRO A 1 215 ? 39.97386 51.34617 -8.89044  1.000 15.31473 ? 201 PRO A CG   1 
ATOM   1660 C  CD   . PRO A 1 215 ? 40.02081 50.20305 -7.93076  1.000 7.96723  ? 201 PRO A CD   1 
ATOM   1661 N  N    . GLU A 1 216 ? 42.70189 49.37620 -10.57783 1.000 8.29106  ? 202 GLU A N    1 
ATOM   1662 C  CA   . GLU A 1 216 ? 43.91505 49.06261 -11.33154 1.000 10.58162 ? 202 GLU A CA   1 
ATOM   1663 C  C    . GLU A 1 216 ? 43.97184 47.58518 -11.75538 1.000 12.45859 ? 202 GLU A C    1 
ATOM   1664 O  O    . GLU A 1 216 ? 44.33220 47.27111 -12.89674 1.000 8.02913  ? 202 GLU A O    1 
ATOM   1665 C  CB   . GLU A 1 216 ? 45.15996 49.50437 -10.54270 1.000 7.83200  ? 202 GLU A CB   1 
ATOM   1666 C  CG   . GLU A 1 216 ? 45.36366 48.82976 -9.18145  1.000 9.05330  ? 202 GLU A CG   1 
ATOM   1667 C  CD   . GLU A 1 216 ? 44.76281 49.62000 -8.01504  1.000 13.12236 ? 202 GLU A CD   1 
ATOM   1668 O  OE1  . GLU A 1 216 ? 43.60480 50.04898 -8.11941  1.000 10.10058 ? 202 GLU A OE1  1 
ATOM   1669 O  OE2  . GLU A 1 216 ? 45.45464 49.80973 -6.98909  1.000 10.52370 ? 202 GLU A OE2  1 
ATOM   1670 N  N    . LEU A 1 217 ? 43.59295 46.66219 -10.86571 1.000 8.22067  ? 203 LEU A N    1 
ATOM   1671 C  CA   . LEU A 1 217 ? 43.55217 45.25067 -11.25398 1.000 10.45511 ? 203 LEU A CA   1 
ATOM   1672 C  C    . LEU A 1 217 ? 42.48374 44.99364 -12.30954 1.000 8.93151  ? 203 LEU A C    1 
ATOM   1673 O  O    . LEU A 1 217 ? 42.69282 44.20603 -13.24241 1.000 9.52133  ? 203 LEU A O    1 
ATOM   1674 C  CB   . LEU A 1 217 ? 43.28506 44.36208 -10.03452 1.000 7.82532  ? 203 LEU A CB   1 
ATOM   1675 C  CG   . LEU A 1 217 ? 44.21058 44.52256 -8.83211  1.000 11.35822 ? 203 LEU A CG   1 
ATOM   1676 C  CD1  . LEU A 1 217 ? 43.82841 43.50714 -7.75906  1.000 11.18989 ? 203 LEU A CD1  1 
ATOM   1677 C  CD2  . LEU A 1 217 ? 45.67726 44.35855 -9.21954  1.000 8.09616  ? 203 LEU A CD2  1 
ATOM   1678 N  N    . LEU A 1 218 ? 41.32304 45.63582 -12.16819 1.000 7.46093  ? 204 LEU A N    1 
ATOM   1679 C  CA   . LEU A 1 218 ? 40.19443 45.34490 -13.03939 1.000 8.64095  ? 204 LEU A CA   1 
ATOM   1680 C  C    . LEU A 1 218 ? 40.41214 45.85619 -14.45778 1.000 11.29514 ? 204 LEU A C    1 
ATOM   1681 O  O    . LEU A 1 218 ? 39.78410 45.33953 -15.39408 1.000 10.82430 ? 204 LEU A O    1 
ATOM   1682 C  CB   . LEU A 1 218 ? 38.91467 45.90841 -12.42038 1.000 10.05686 ? 204 LEU A CB   1 
ATOM   1683 C  CG   . LEU A 1 218 ? 38.62577 45.33129 -11.02648 1.000 9.17898  ? 204 LEU A CG   1 
ATOM   1684 C  CD1  . LEU A 1 218 ? 37.50917 46.09186 -10.35015 1.000 6.77915  ? 204 LEU A CD1  1 
ATOM   1685 C  CD2  . LEU A 1 218 ? 38.27179 43.84890 -11.12892 1.000 9.03099  ? 204 LEU A CD2  1 
ATOM   1686 N  N    . VAL A 1 219 ? 41.30215 46.83709 -14.63416 1.000 11.82143 ? 205 VAL A N    1 
ATOM   1687 C  CA   . VAL A 1 219 ? 41.65246 47.36016 -15.95078 1.000 6.65163  ? 205 VAL A CA   1 
ATOM   1688 C  C    . VAL A 1 219 ? 43.00538 46.84014 -16.43197 1.000 10.98286 ? 205 VAL A C    1 
ATOM   1689 O  O    . VAL A 1 219 ? 43.54471 47.34571 -17.42431 1.000 11.48899 ? 205 VAL A O    1 
ATOM   1690 C  CB   . VAL A 1 219 ? 41.58410 48.89955 -15.99087 1.000 8.63046  ? 205 VAL A CB   1 
ATOM   1691 C  CG1  . VAL A 1 219 ? 40.19150 49.35937 -15.63613 1.000 10.12987 ? 205 VAL A CG1  1 
ATOM   1692 C  CG2  . VAL A 1 219 ? 42.64697 49.53246 -15.06393 1.000 8.10247  ? 205 VAL A CG2  1 
ATOM   1693 N  N    . ASP A 1 220 ? 43.57817 45.85362 -15.73589 1.000 9.27583  ? 206 ASP A N    1 
ATOM   1694 C  CA   . ASP A 1 220 ? 44.80879 45.18128 -16.17116 1.000 10.56227 ? 206 ASP A CA   1 
ATOM   1695 C  C    . ASP A 1 220 ? 46.02765 46.10655 -16.14254 1.000 11.67569 ? 206 ASP A C    1 
ATOM   1696 O  O    . ASP A 1 220 ? 46.90820 46.02243 -16.99585 1.000 13.09354 ? 206 ASP A O    1 
ATOM   1697 C  CB   . ASP A 1 220 ? 44.64396 44.49145 -17.53181 1.000 13.24148 ? 206 ASP A CB   1 
ATOM   1698 C  CG   . ASP A 1 220 ? 43.97925 43.13089 -17.41884 1.000 16.04578 ? 206 ASP A CG   1 
ATOM   1699 O  OD1  . ASP A 1 220 ? 44.66778 42.16164 -17.04415 1.000 25.81346 ? 206 ASP A OD1  1 
ATOM   1700 O  OD2  . ASP A 1 220 ? 42.76699 43.03015 -17.68186 1.000 23.59737 ? 206 ASP A OD2  1 
ATOM   1701 N  N    . TYR A 1 221 ? 46.08355 46.98539 -15.14987 1.000 9.11300  ? 207 TYR A N    1 
ATOM   1702 C  CA   . TYR A 1 221 ? 47.23423 47.86272 -14.95314 1.000 7.75685  ? 207 TYR A CA   1 
ATOM   1703 C  C    . TYR A 1 221 ? 48.19547 47.19069 -13.97828 1.000 9.65450  ? 207 TYR A C    1 
ATOM   1704 O  O    . TYR A 1 221 ? 47.89105 47.04915 -12.79181 1.000 7.11067  ? 207 TYR A O    1 
ATOM   1705 C  CB   . TYR A 1 221 ? 46.79353 49.22420 -14.43225 1.000 6.47849  ? 207 TYR A CB   1 
ATOM   1706 C  CG   . TYR A 1 221 ? 47.96446 50.18187 -14.27755 1.000 9.73391  ? 207 TYR A CG   1 
ATOM   1707 C  CD1  . TYR A 1 221 ? 48.64023 50.65349 -15.38774 1.000 16.02855 ? 207 TYR A CD1  1 
ATOM   1708 C  CD2  . TYR A 1 221 ? 48.39829 50.59973 -13.02029 1.000 15.24419 ? 207 TYR A CD2  1 
ATOM   1709 C  CE1  . TYR A 1 221 ? 49.70796 51.52643 -15.26304 1.000 16.71033 ? 207 TYR A CE1  1 
ATOM   1710 C  CE2  . TYR A 1 221 ? 49.47519 51.47527 -12.88887 1.000 15.71863 ? 207 TYR A CE2  1 
ATOM   1711 C  CZ   . TYR A 1 221 ? 50.11887 51.92983 -14.02034 1.000 17.82764 ? 207 TYR A CZ   1 
ATOM   1712 O  OH   . TYR A 1 221 ? 51.18357 52.79753 -13.93223 1.000 25.97268 ? 207 TYR A OH   1 
ATOM   1713 N  N    . GLN A 1 222 ? 49.36674 46.79733 -14.47766 1.000 10.84041 ? 208 GLN A N    1 
ATOM   1714 C  CA   . GLN A 1 222 ? 50.27725 45.93433 -13.73951 1.000 9.39198  ? 208 GLN A CA   1 
ATOM   1715 C  C    . GLN A 1 222 ? 51.26549 46.67923 -12.85793 1.000 12.28834 ? 208 GLN A C    1 
ATOM   1716 O  O    . GLN A 1 222 ? 51.90505 46.04927 -12.01074 1.000 10.55294 ? 208 GLN A O    1 
ATOM   1717 C  CB   . GLN A 1 222 ? 51.06099 45.05885 -14.71095 1.000 7.27353  ? 208 GLN A CB   1 
ATOM   1718 C  CG   . GLN A 1 222 ? 50.14698 44.15603 -15.50442 1.000 10.99902 ? 208 GLN A CG   1 
ATOM   1719 C  CD   . GLN A 1 222 ? 50.90180 43.12213 -16.28834 1.000 19.02656 ? 208 GLN A CD   1 
ATOM   1720 O  OE1  . GLN A 1 222 ? 50.92094 43.15286 -17.51176 1.000 17.32188 ? 208 GLN A OE1  1 
ATOM   1721 N  NE2  . GLN A 1 222 ? 51.52358 42.19303 -15.58950 1.000 17.37931 ? 208 GLN A NE2  1 
ATOM   1722 N  N    . MET A 1 223 ? 51.41500 47.98513 -13.02668 1.000 11.19527 ? 209 MET A N    1 
ATOM   1723 C  CA   . MET A 1 223 ? 52.42348 48.71327 -12.26204 1.000 9.33927  ? 209 MET A CA   1 
ATOM   1724 C  C    . MET A 1 223 ? 51.83209 49.30344 -10.98444 1.000 10.08222 ? 209 MET A C    1 
ATOM   1725 O  O    . MET A 1 223 ? 51.93779 50.49306 -10.71054 1.000 11.09027 ? 209 MET A O    1 
ATOM   1726 C  CB   . MET A 1 223 ? 53.07207 49.77702 -13.13919 1.000 10.21803 ? 209 MET A CB   1 
ATOM   1727 C  CG   . MET A 1 223 ? 54.44847 50.20684 -12.65935 1.000 13.64582 ? 209 MET A CG   1 
ATOM   1728 S  SD   . MET A 1 223 ? 55.30006 51.25080 -13.84848 1.000 22.01167 ? 209 MET A SD   1 
ATOM   1729 C  CE   . MET A 1 223 ? 55.50995 50.09539 -15.19735 1.000 17.89643 ? 209 MET A CE   1 
ATOM   1730 N  N    . TYR A 1 224 ? 51.19551 48.44472 -10.18863 1.000 8.14267  ? 210 TYR A N    1 
ATOM   1731 C  CA   . TYR A 1 224 ? 50.53153 48.84927 -8.95561  1.000 7.18847  ? 210 TYR A CA   1 
ATOM   1732 C  C    . TYR A 1 224 ? 51.49132 48.72677 -7.76632  1.000 8.28936  ? 210 TYR A C    1 
ATOM   1733 O  O    . TYR A 1 224 ? 52.64460 48.30551 -7.90852  1.000 8.91462  ? 210 TYR A O    1 
ATOM   1734 C  CB   . TYR A 1 224 ? 49.21096 48.08171 -8.78264  1.000 4.18141  ? 210 TYR A CB   1 
ATOM   1735 C  CG   . TYR A 1 224 ? 49.33454 46.56569 -8.62794  1.000 8.56187  ? 210 TYR A CG   1 
ATOM   1736 C  CD1  . TYR A 1 224 ? 49.67750 45.99815 -7.40391  1.000 6.18395  ? 210 TYR A CD1  1 
ATOM   1737 C  CD2  . TYR A 1 224 ? 49.09594 45.70427 -9.70257  1.000 6.11422  ? 210 TYR A CD2  1 
ATOM   1738 C  CE1  . TYR A 1 224 ? 49.78922 44.60094 -7.25473  1.000 7.54667  ? 210 TYR A CE1  1 
ATOM   1739 C  CE2  . TYR A 1 224 ? 49.19117 44.30208 -9.55819  1.000 6.10349  ? 210 TYR A CE2  1 
ATOM   1740 C  CZ   . TYR A 1 224 ? 49.53901 43.77123 -8.32712  1.000 7.05749  ? 210 TYR A CZ   1 
ATOM   1741 O  OH   . TYR A 1 224 ? 49.64687 42.40923 -8.16079  1.000 7.62074  ? 210 TYR A OH   1 
ATOM   1742 N  N    . ASP A 1 225 ? 51.01994 49.10278 -6.57922  1.000 7.09617  ? 211 ASP A N    1 
ATOM   1743 C  CA   . ASP A 1 225 ? 51.88262 49.15125 -5.39892  1.000 5.77443  ? 211 ASP A CA   1 
ATOM   1744 C  C    . ASP A 1 225 ? 51.04332 48.92980 -4.14074  1.000 8.19659  ? 211 ASP A C    1 
ATOM   1745 O  O    . ASP A 1 225 ? 49.90704 48.44574 -4.20890  1.000 6.93396  ? 211 ASP A O    1 
ATOM   1746 C  CB   . ASP A 1 225 ? 52.69337 50.46382 -5.37892  1.000 8.71273  ? 211 ASP A CB   1 
ATOM   1747 C  CG   . ASP A 1 225 ? 51.80702 51.70642 -5.39188  1.000 7.72490  ? 211 ASP A CG   1 
ATOM   1748 O  OD1  . ASP A 1 225 ? 51.08591 51.93749 -4.40697  1.000 10.15946 ? 211 ASP A OD1  1 
ATOM   1749 O  OD2  . ASP A 1 225 ? 51.83270 52.45793 -6.38621  1.000 10.61359 ? 211 ASP A OD2  1 
ATOM   1750 N  N    . TYR A 1 226 ? 51.61990 49.29634 -2.98562  1.000 9.13584  ? 212 TYR A N    1 
ATOM   1751 C  CA   . TYR A 1 226 ? 50.96833 49.14587 -1.68745  1.000 7.53110  ? 212 TYR A CA   1 
ATOM   1752 C  C    . TYR A 1 226 ? 49.57092 49.73890 -1.66832  1.000 7.81798  ? 212 TYR A C    1 
ATOM   1753 O  O    . TYR A 1 226 ? 48.71334 49.28502 -0.89394  1.000 7.39097  ? 212 TYR A O    1 
ATOM   1754 C  CB   . TYR A 1 226 ? 51.77269 49.88497 -0.61989  1.000 2.85687  ? 212 TYR A CB   1 
ATOM   1755 C  CG   . TYR A 1 226 ? 53.27308 49.64125 -0.64246  1.000 7.38215  ? 212 TYR A CG   1 
ATOM   1756 C  CD1  . TYR A 1 226 ? 53.80886 48.40573 -0.27797  1.000 5.42794  ? 212 TYR A CD1  1 
ATOM   1757 C  CD2  . TYR A 1 226 ? 54.14701 50.66521 -0.97839  1.000 6.88805  ? 212 TYR A CD2  1 
ATOM   1758 C  CE1  . TYR A 1 226 ? 55.18930 48.18848 -0.27992  1.000 4.80889  ? 212 TYR A CE1  1 
ATOM   1759 C  CE2  . TYR A 1 226 ? 55.52718 50.46940 -0.98183  1.000 5.52875  ? 212 TYR A CE2  1 
ATOM   1760 C  CZ   . TYR A 1 226 ? 56.04110 49.23565 -0.62674  1.000 8.18785  ? 212 TYR A CZ   1 
ATOM   1761 O  OH   . TYR A 1 226 ? 57.41360 49.06591 -0.62681  1.000 7.12979  ? 212 TYR A OH   1 
ATOM   1762 N  N    . SER A 1 227 ? 49.32904 50.77300 -2.48897  1.000 4.82422  ? 213 SER A N    1 
ATOM   1763 C  CA   . SER A 1 227 ? 48.02684 51.42701 -2.49201  1.000 7.30369  ? 213 SER A CA   1 
ATOM   1764 C  C    . SER A 1 227 ? 46.89745 50.48627 -2.91260  1.000 7.55669  ? 213 SER A C    1 
ATOM   1765 O  O    . SER A 1 227 ? 45.72906 50.80169 -2.67683  1.000 5.19601  ? 213 SER A O    1 
ATOM   1766 C  CB   . SER A 1 227 ? 48.08324 52.67567 -3.36350  1.000 9.13158  ? 213 SER A CB   1 
ATOM   1767 O  OG   . SER A 1 227 ? 48.46493 52.33527 -4.68644  1.000 9.83533  ? 213 SER A OG   1 
ATOM   1768 N  N    . LEU A 1 228 ? 47.20849 49.33010 -3.50349  1.000 7.56964  ? 214 LEU A N    1 
ATOM   1769 C  CA   . LEU A 1 228 ? 46.17102 48.33610 -3.75678  1.000 5.67006  ? 214 LEU A CA   1 
ATOM   1770 C  C    . LEU A 1 228 ? 45.51555 47.88530 -2.45414  1.000 6.22985  ? 214 LEU A C    1 
ATOM   1771 O  O    . LEU A 1 228 ? 44.28822 47.70441 -2.39165  1.000 6.85411  ? 214 LEU A O    1 
ATOM   1772 C  CB   . LEU A 1 228 ? 46.79523 47.14592 -4.48896  1.000 7.98568  ? 214 LEU A CB   1 
ATOM   1773 C  CG   . LEU A 1 228 ? 45.94922 45.88548 -4.52389  1.000 13.17698 ? 214 LEU A CG   1 
ATOM   1774 C  CD1  . LEU A 1 228 ? 44.65936 46.12113 -5.33704  1.000 14.16110 ? 214 LEU A CD1  1 
ATOM   1775 C  CD2  . LEU A 1 228 ? 46.76201 44.70210 -5.06752  1.000 5.22469  ? 214 LEU A CD2  1 
ATOM   1776 N  N    . ASP A 1 229 ? 46.31789 47.72289 -1.39360  1.000 4.88444  ? 215 ASP A N    1 
ATOM   1777 C  CA   . ASP A 1 229 ? 45.78671 47.30321 -0.10016  1.000 7.19157  ? 215 ASP A CA   1 
ATOM   1778 C  C    . ASP A 1 229 ? 44.86185 48.35926 0.49805   1.000 6.54538  ? 215 ASP A C    1 
ATOM   1779 O  O    . ASP A 1 229 ? 43.92659 48.01987 1.23946   1.000 6.95670  ? 215 ASP A O    1 
ATOM   1780 C  CB   . ASP A 1 229 ? 46.93334 47.01569 0.87792   1.000 4.45548  ? 215 ASP A CB   1 
ATOM   1781 C  CG   . ASP A 1 229 ? 47.75314 45.77613 0.49996   1.000 7.88388  ? 215 ASP A CG   1 
ATOM   1782 O  OD1  . ASP A 1 229 ? 47.23732 44.85128 -0.17518  1.000 8.20834  ? 215 ASP A OD1  1 
ATOM   1783 O  OD2  . ASP A 1 229 ? 48.91386 45.71975 0.92864   1.000 7.78958  ? 215 ASP A OD2  1 
ATOM   1784 N  N    . MET A 1 230 ? 45.11241 49.63765 0.19841   1.000 6.60630  ? 216 MET A N    1 
ATOM   1785 C  CA   . MET A 1 230 ? 44.28624 50.70647 0.75379   1.000 7.97411  ? 216 MET A CA   1 
ATOM   1786 C  C    . MET A 1 230 ? 42.92493 50.77398 0.07848   1.000 6.52210  ? 216 MET A C    1 
ATOM   1787 O  O    . MET A 1 230 ? 41.93673 51.15954 0.72586   1.000 7.32597  ? 216 MET A O    1 
ATOM   1788 C  CB   . MET A 1 230 ? 45.01794 52.05036 0.68616   1.000 6.61383  ? 216 MET A CB   1 
ATOM   1789 C  CG   . MET A 1 230 ? 46.34430 52.06648 1.41564   1.000 7.06454  ? 216 MET A CG   1 
ATOM   1790 S  SD   . MET A 1 230 ? 46.15793 51.58689 3.13864   1.000 9.89160  ? 216 MET A SD   1 
ATOM   1791 C  CE   . MET A 1 230 ? 45.10786 52.90144 3.71085   1.000 6.88594  ? 216 MET A CE   1 
ATOM   1792 N  N    . TRP A 1 231 ? 42.83403 50.38856 -1.20187  1.000 5.34088  ? 217 TRP A N    1 
ATOM   1793 C  CA   . TRP A 1 231 ? 41.51638 50.23479 -1.82076  1.000 6.10850  ? 217 TRP A CA   1 
ATOM   1794 C  C    . TRP A 1 231 ? 40.72218 49.13696 -1.12852  1.000 6.58076  ? 217 TRP A C    1 
ATOM   1795 O  O    . TRP A 1 231 ? 39.54291 49.31860 -0.79131  1.000 6.96355  ? 217 TRP A O    1 
ATOM   1796 C  CB   . TRP A 1 231 ? 41.62542 49.91334 -3.32031  1.000 6.90680  ? 217 TRP A CB   1 
ATOM   1797 C  CG   . TRP A 1 231 ? 40.24851 49.61591 -3.91277  1.000 8.78364  ? 217 TRP A CG   1 
ATOM   1798 C  CD1  . TRP A 1 231 ? 39.58842 48.40208 -3.92858  1.000 7.76672  ? 217 TRP A CD1  1 
ATOM   1799 C  CD2  . TRP A 1 231 ? 39.35661 50.55737 -4.52537  1.000 6.18107  ? 217 TRP A CD2  1 
ATOM   1800 N  NE1  . TRP A 1 231 ? 38.34790 48.54283 -4.51483  1.000 5.19888  ? 217 TRP A NE1  1 
ATOM   1801 C  CE2  . TRP A 1 231 ? 38.17989 49.85417 -4.88323  1.000 5.44172  ? 217 TRP A CE2  1 
ATOM   1802 C  CE3  . TRP A 1 231 ? 39.43694 51.93204 -4.80436  1.000 10.37883 ? 217 TRP A CE3  1 
ATOM   1803 C  CZ2  . TRP A 1 231 ? 37.09759 50.47604 -5.53415  1.000 9.54085  ? 217 TRP A CZ2  1 
ATOM   1804 C  CZ3  . TRP A 1 231 ? 38.36180 52.55038 -5.44363  1.000 9.20770  ? 217 TRP A CZ3  1 
ATOM   1805 C  CH2  . TRP A 1 231 ? 37.20194 51.82207 -5.79322  1.000 8.67016  ? 217 TRP A CH2  1 
ATOM   1806 N  N    . SER A 1 232 ? 41.36247 47.98509 -0.90086  1.000 7.02147  ? 218 SER A N    1 
ATOM   1807 C  CA   . SER A 1 232 ? 40.69041 46.88128 -0.22858  1.000 8.01399  ? 218 SER A CA   1 
ATOM   1808 C  C    . SER A 1 232 ? 40.25073 47.28882 1.16574   1.000 9.41990  ? 218 SER A C    1 
ATOM   1809 O  O    . SER A 1 232 ? 39.14881 46.94285 1.60341   1.000 7.67907  ? 218 SER A O    1 
ATOM   1810 C  CB   . SER A 1 232 ? 41.62509 45.66947 -0.13979  1.000 8.21099  ? 218 SER A CB   1 
ATOM   1811 O  OG   . SER A 1 232 ? 42.14618 45.30047 -1.40183  1.000 5.98974  ? 218 SER A OG   1 
ATOM   1812 N  N    . LEU A 1 233 ? 41.10577 48.02299 1.88211   1.000 4.92829  ? 219 LEU A N    1 
ATOM   1813 C  CA   . LEU A 1 233 ? 40.72153 48.49188 3.20635   1.000 7.55166  ? 219 LEU A CA   1 
ATOM   1814 C  C    . LEU A 1 233 ? 39.52982 49.44135 3.11872   1.000 8.20334  ? 219 LEU A C    1 
ATOM   1815 O  O    . LEU A 1 233 ? 38.61441 49.36905 3.94800   1.000 8.00046  ? 219 LEU A O    1 
ATOM   1816 C  CB   . LEU A 1 233 ? 41.92317 49.13495 3.90876   1.000 8.82284  ? 219 LEU A CB   1 
ATOM   1817 C  CG   . LEU A 1 233 ? 41.57587 49.59867 5.32882   1.000 12.20311 ? 219 LEU A CG   1 
ATOM   1818 C  CD1  . LEU A 1 233 ? 42.73025 49.36886 6.27956   1.000 17.38436 ? 219 LEU A CD1  1 
ATOM   1819 C  CD2  . LEU A 1 233 ? 41.17762 51.07079 5.32974   1.000 10.76603 ? 219 LEU A CD2  1 
ATOM   1820 N  N    . GLY A 1 234 ? 39.52122 50.33249 2.11865   1.000 8.23795  ? 220 GLY A N    1 
ATOM   1821 C  CA   . GLY A 1 234 ? 38.37447 51.21586 1.93086   1.000 6.61725  ? 220 GLY A CA   1 
ATOM   1822 C  C    . GLY A 1 234 ? 37.08946 50.45282 1.67133   1.000 9.04452  ? 220 GLY A C    1 
ATOM   1823 O  O    . GLY A 1 234 ? 36.01790 50.82669 2.15873   1.000 8.08674  ? 220 GLY A O    1 
ATOM   1824 N  N    . CYS A 1 235 ? 37.18107 49.36894 0.90485   1.000 3.56787  ? 221 CYS A N    1 
ATOM   1825 C  CA   . CYS A 1 235 ? 36.02186 48.50293 0.69411   1.000 10.18143 ? 221 CYS A CA   1 
ATOM   1826 C  C    . CYS A 1 235 ? 35.48410 47.95906 2.01231   1.000 10.38567 ? 221 CYS A C    1 
ATOM   1827 O  O    . CYS A 1 235 ? 34.25958 47.89214 2.22349   1.000 9.63217  ? 221 CYS A O    1 
ATOM   1828 C  CB   . CYS A 1 235 ? 36.42262 47.35238 -0.21823  1.000 6.68076  ? 221 CYS A CB   1 
ATOM   1829 S  SG   . CYS A 1 235 ? 36.58840 47.84818 -1.94043  1.000 8.15317  ? 221 CYS A SG   1 
ATOM   1830 N  N    . MET A 1 236 ? 36.38306 47.54844 2.90438   1.000 6.97200  ? 222 MET A N    1 
ATOM   1831 C  CA   . MET A 1 236 ? 35.95632 47.02897 4.19732   1.000 9.22211  ? 222 MET A CA   1 
ATOM   1832 C  C    . MET A 1 236 ? 35.33600 48.12016 5.05026   1.000 8.93238  ? 222 MET A C    1 
ATOM   1833 O  O    . MET A 1 236 ? 34.30332 47.89753 5.70192   1.000 7.94969  ? 222 MET A O    1 
ATOM   1834 C  CB   . MET A 1 236 ? 37.13617 46.38541 4.91648   1.000 6.50166  ? 222 MET A CB   1 
ATOM   1835 C  CG   . MET A 1 236 ? 37.64349 45.11311 4.24184   1.000 7.29823  ? 222 MET A CG   1 
ATOM   1836 S  SD   . MET A 1 236 ? 39.00924 44.29756 5.12164   1.000 14.00950 ? 222 MET A SD   1 
ATOM   1837 C  CE   . MET A 1 236 ? 38.25936 44.01471 6.71979   1.000 6.14089  ? 222 MET A CE   1 
ATOM   1838 N  N    . LEU A 1 237 ? 35.95503 49.30090 5.06868   1.000 6.95452  ? 223 LEU A N    1 
ATOM   1839 C  CA   . LEU A 1 237 ? 35.39493 50.42048 5.82135   1.000 7.51959  ? 223 LEU A CA   1 
ATOM   1840 C  C    . LEU A 1 237 ? 33.98086 50.74166 5.35747   1.000 8.63658  ? 223 LEU A C    1 
ATOM   1841 O  O    . LEU A 1 237 ? 33.06993 50.92914 6.17830   1.000 6.66523  ? 223 LEU A O    1 
ATOM   1842 C  CB   . LEU A 1 237 ? 36.29432 51.64320 5.67090   1.000 6.40105  ? 223 LEU A CB   1 
ATOM   1843 C  CG   . LEU A 1 237 ? 35.76558 52.90626 6.35880   1.000 5.80076  ? 223 LEU A CG   1 
ATOM   1844 C  CD1  . LEU A 1 237 ? 35.67408 52.71868 7.87314   1.000 5.86930  ? 223 LEU A CD1  1 
ATOM   1845 C  CD2  . LEU A 1 237 ? 36.64196 54.09814 5.98565   1.000 7.56166  ? 223 LEU A CD2  1 
ATOM   1846 N  N    . ALA A 1 238 ? 33.77790 50.81063 4.03550   1.000 8.52293  ? 224 ALA A N    1 
ATOM   1847 C  CA   . ALA A 1 238 ? 32.44340 51.07465 3.50704   1.000 7.07399  ? 224 ALA A CA   1 
ATOM   1848 C  C    . ALA A 1 238 ? 31.44092 50.01958 3.96231   1.000 7.99210  ? 224 ALA A C    1 
ATOM   1849 O  O    . ALA A 1 238 ? 30.32003 50.35500 4.35607   1.000 6.53703  ? 224 ALA A O    1 
ATOM   1850 C  CB   . ALA A 1 238 ? 32.47708 51.14126 1.97931   1.000 8.33204  ? 224 ALA A CB   1 
ATOM   1851 N  N    . SER A 1 239 ? 31.83140 48.74204 3.93727   1.000 6.80212  ? 225 SER A N    1 
ATOM   1852 C  CA   . SER A 1 239 ? 30.90520 47.68719 4.33726   1.000 4.84436  ? 225 SER A CA   1 
ATOM   1853 C  C    . SER A 1 239 ? 30.55887 47.78494 5.81765   1.000 9.70400  ? 225 SER A C    1 
ATOM   1854 O  O    . SER A 1 239 ? 29.42765 47.47436 6.21404   1.000 8.70080  ? 225 SER A O    1 
ATOM   1855 C  CB   . SER A 1 239 ? 31.50029 46.31801 4.01000   1.000 8.47074  ? 225 SER A CB   1 
ATOM   1856 O  OG   . SER A 1 239 ? 32.54372 45.99918 4.90769   1.000 12.17417 ? 225 SER A OG   1 
ATOM   1857 N  N    . MET A 1 240 ? 31.49784 48.23793 6.64925   1.000 6.98145  ? 226 MET A N    1 
ATOM   1858 C  CA   . MET A 1 240 ? 31.20250 48.32124 8.07770   1.000 12.56661 ? 226 MET A CA   1 
ATOM   1859 C  C    . MET A 1 240 ? 30.31656 49.52391 8.41095   1.000 10.34599 ? 226 MET A C    1 
ATOM   1860 O  O    . MET A 1 240 ? 29.33412 49.39039 9.15831   1.000 8.12332  ? 226 MET A O    1 
ATOM   1861 C  CB   . MET A 1 240 ? 32.50056 48.34827 8.88622   1.000 9.10914  ? 226 MET A CB   1 
ATOM   1862 C  CG   . MET A 1 240 ? 33.25790 47.03053 8.89014   1.000 10.89681 ? 226 MET A CG   1 
ATOM   1863 S  SD   . MET A 1 240 ? 34.91286 47.25812 9.59583   1.000 19.07092 ? 226 MET A SD   1 
ATOM   1864 C  CE   . MET A 1 240 ? 34.57258 47.50264 11.31158  1.000 34.35803 ? 226 MET A CE   1 
ATOM   1865 N  N    . ILE A 1 241 ? 30.63823 50.70395 7.87044   1.000 6.40740  ? 227 ILE A N    1 
ATOM   1866 C  CA   . ILE A 1 241 ? 29.85447 51.88716 8.23719   1.000 8.40741  ? 227 ILE A CA   1 
ATOM   1867 C  C    . ILE A 1 241 ? 28.48383 51.89955 7.56290   1.000 7.18259  ? 227 ILE A C    1 
ATOM   1868 O  O    . ILE A 1 241 ? 27.53475 52.48287 8.10618   1.000 8.53308  ? 227 ILE A O    1 
ATOM   1869 C  CB   . ILE A 1 241 ? 30.59183 53.22898 8.02188   1.000 6.29261  ? 227 ILE A CB   1 
ATOM   1870 C  CG1  . ILE A 1 241 ? 30.73849 53.54091 6.52565   1.000 7.09886  ? 227 ILE A CG1  1 
ATOM   1871 C  CG2  . ILE A 1 241 ? 31.91826 53.25954 8.74201   1.000 8.02031  ? 227 ILE A CG2  1 
ATOM   1872 C  CD1  . ILE A 1 241 ? 31.46023 54.86717 6.22583   1.000 5.96044  ? 227 ILE A CD1  1 
ATOM   1873 N  N    . PHE A 1 242 ? 28.35089 51.29698 6.37768   1.000 5.46229  ? 228 PHE A N    1 
ATOM   1874 C  CA   . PHE A 1 242 ? 27.07933 51.29433 5.65789   1.000 9.52463  ? 228 PHE A CA   1 
ATOM   1875 C  C    . PHE A 1 242 ? 26.28845 49.99990 5.82955   1.000 9.03095  ? 228 PHE A C    1 
ATOM   1876 O  O    . PHE A 1 242 ? 25.08317 49.97971 5.54491   1.000 9.04621  ? 228 PHE A O    1 
ATOM   1877 C  CB   . PHE A 1 242 ? 27.29649 51.55881 4.15522   1.000 6.35847  ? 228 PHE A CB   1 
ATOM   1878 C  CG   . PHE A 1 242 ? 27.83693 52.94020 3.83503   1.000 6.77417  ? 228 PHE A CG   1 
ATOM   1879 C  CD1  . PHE A 1 242 ? 27.31107 54.07466 4.43633   1.000 8.65556  ? 228 PHE A CD1  1 
ATOM   1880 C  CD2  . PHE A 1 242 ? 28.87258 53.09517 2.92798   1.000 8.10554  ? 228 PHE A CD2  1 
ATOM   1881 C  CE1  . PHE A 1 242 ? 27.81856 55.33503 4.13025   1.000 9.63154  ? 228 PHE A CE1  1 
ATOM   1882 C  CE2  . PHE A 1 242 ? 29.37366 54.33763 2.62386   1.000 8.01043  ? 228 PHE A CE2  1 
ATOM   1883 C  CZ   . PHE A 1 242 ? 28.84756 55.46121 3.22066   1.000 8.27360  ? 228 PHE A CZ   1 
ATOM   1884 N  N    . ARG A 1 243 ? 26.93108 48.92928 6.29171   1.000 11.46401 ? 229 ARG A N    1 
ATOM   1885 C  CA   . ARG A 1 243 ? 26.29349 47.63516 6.52671   1.000 10.12346 ? 229 ARG A CA   1 
ATOM   1886 C  C    . ARG A 1 243 ? 25.87160 46.92033 5.25182   1.000 15.47234 ? 229 ARG A C    1 
ATOM   1887 O  O    . ARG A 1 243 ? 25.02454 46.02280 5.29798   1.000 20.31186 ? 229 ARG A O    1 
ATOM   1888 C  CB   . ARG A 1 243 ? 25.13329 47.71641 7.51797   1.000 13.10480 ? 229 ARG A CB   1 
ATOM   1889 C  CG   . ARG A 1 243 ? 25.57368 48.09322 8.88405   1.000 15.02636 ? 229 ARG A CG   1 
ATOM   1890 C  CD   . ARG A 1 243 ? 24.46051 47.84926 9.86881   1.000 31.74811 ? 229 ARG A CD   1 
ATOM   1891 N  NE   . ARG A 1 243 ? 24.97943 47.78824 11.22582  1.000 40.01744 ? 229 ARG A NE   1 
ATOM   1892 C  CZ   . ARG A 1 243 ? 24.22414 47.82722 12.31133  1.000 32.66952 ? 229 ARG A CZ   1 
ATOM   1893 N  NH1  . ARG A 1 243 ? 22.90676 47.92010 12.22998  1.000 29.48503 ? 229 ARG A NH1  1 
ATOM   1894 N  NH2  . ARG A 1 243 ? 24.80686 47.78720 13.50637  1.000 37.00072 ? 229 ARG A NH2  1 
ATOM   1895 N  N    . ARG A 1 244 ? 26.43745 47.29176 4.10847   1.000 7.35563  ? 230 ARG A N    1 
ATOM   1896 C  CA   . ARG A 1 244 ? 26.29599 46.52078 2.88135   1.000 8.71648  ? 230 ARG A CA   1 
ATOM   1897 C  C    . ARG A 1 244 ? 27.60966 45.77404 2.68543   1.000 10.34584 ? 230 ARG A C    1 
ATOM   1898 O  O    . ARG A 1 244 ? 28.63761 46.39537 2.40084   1.000 6.92085  ? 230 ARG A O    1 
ATOM   1899 C  CB   . ARG A 1 244 ? 26.00911 47.43894 1.69809   1.000 9.76696  ? 230 ARG A CB   1 
ATOM   1900 C  CG   . ARG A 1 244 ? 25.73404 46.70029 0.39534   1.000 8.51620  ? 230 ARG A CG   1 
ATOM   1901 C  CD   . ARG A 1 244 ? 25.19228 47.65657 -0.67298  1.000 8.54357  ? 230 ARG A CD   1 
ATOM   1902 N  NE   . ARG A 1 244 ? 26.25603 48.36887 -1.38383  1.000 11.09836 ? 230 ARG A NE   1 
ATOM   1903 C  CZ   . ARG A 1 244 ? 26.03929 49.24173 -2.36019  1.000 8.93574  ? 230 ARG A CZ   1 
ATOM   1904 N  NH1  . ARG A 1 244 ? 24.80968 49.59118 -2.71105  1.000 10.21910 ? 230 ARG A NH1  1 
ATOM   1905 N  NH2  . ARG A 1 244 ? 27.07873 49.75158 -3.02174  1.000 9.67907  ? 230 ARG A NH2  1 
ATOM   1906 N  N    . GLU A 1 245 ? 27.57377 44.45000 2.85627   1.000 8.12281  ? 231 GLU A N    1 
ATOM   1907 C  CA   . GLU A 1 245 ? 28.76943 43.60076 2.79546   1.000 10.23869 ? 231 GLU A CA   1 
ATOM   1908 C  C    . GLU A 1 245 ? 28.52601 42.46793 1.80750   1.000 8.37403  ? 231 GLU A C    1 
ATOM   1909 O  O    . GLU A 1 245 ? 27.54176 41.71571 1.95865   1.000 8.79175  ? 231 GLU A O    1 
ATOM   1910 C  CB   . GLU A 1 245 ? 29.09680 43.03695 4.18710   1.000 14.63745 ? 231 GLU A CB   1 
ATOM   1911 C  CG   . GLU A 1 245 ? 30.57319 42.65656 4.39874   1.000 17.87144 ? 231 GLU A CG   1 
ATOM   1912 C  CD   . GLU A 1 245 ? 31.01310 41.43598 3.59723   1.000 21.02766 ? 231 GLU A CD   1 
ATOM   1913 O  OE1  . GLU A 1 245 ? 30.22920 40.46723 3.50607   1.000 16.09398 ? 231 GLU A OE1  1 
ATOM   1914 O  OE2  . GLU A 1 245 ? 32.14478 41.44159 3.05946   1.000 17.21273 ? 231 GLU A OE2  1 
ATOM   1915 N  N    . PRO A 1 246 ? 29.36351 42.30638 0.78491   1.000 8.19973  ? 232 PRO A N    1 
ATOM   1916 C  CA   . PRO A 1 246 ? 30.46018 43.19785 0.38490   1.000 8.94164  ? 232 PRO A CA   1 
ATOM   1917 C  C    . PRO A 1 246 ? 29.88653 44.49590 -0.17002  1.000 10.76369 ? 232 PRO A C    1 
ATOM   1918 O  O    . PRO A 1 246 ? 28.72225 44.54805 -0.59385  1.000 9.90110  ? 232 PRO A O    1 
ATOM   1919 C  CB   . PRO A 1 246 ? 31.18734 42.38553 -0.69516  1.000 9.92374  ? 232 PRO A CB   1 
ATOM   1920 C  CG   . PRO A 1 246 ? 30.12457 41.48880 -1.26041  1.000 13.30546 ? 232 PRO A CG   1 
ATOM   1921 C  CD   . PRO A 1 246 ? 29.27514 41.12225 -0.08650  1.000 12.93540 ? 232 PRO A CD   1 
ATOM   1922 N  N    . PHE A 1 247 ? 30.66840 45.57546 -0.15781  1.000 6.97128  ? 233 PHE A N    1 
ATOM   1923 C  CA   . PHE A 1 247 ? 30.12125 46.85973 -0.57644  1.000 7.97148  ? 233 PHE A CA   1 
ATOM   1924 C  C    . PHE A 1 247 ? 29.90111 46.92054 -2.08450  1.000 7.20665  ? 233 PHE A C    1 
ATOM   1925 O  O    . PHE A 1 247 ? 28.85384 47.39595 -2.53432  1.000 7.11394  ? 233 PHE A O    1 
ATOM   1926 C  CB   . PHE A 1 247 ? 30.97780 48.03141 -0.07613  1.000 6.54458  ? 233 PHE A CB   1 
ATOM   1927 C  CG   . PHE A 1 247 ? 30.36041 49.37451 -0.36392  1.000 9.63395  ? 233 PHE A CG   1 
ATOM   1928 C  CD1  . PHE A 1 247 ? 29.24978 49.79570 0.35901   1.000 9.27671  ? 233 PHE A CD1  1 
ATOM   1929 C  CD2  . PHE A 1 247 ? 30.85337 50.19010 -1.38491  1.000 8.70387  ? 233 PHE A CD2  1 
ATOM   1930 C  CE1  . PHE A 1 247 ? 28.64630 51.02011 0.09270   1.000 8.54922  ? 233 PHE A CE1  1 
ATOM   1931 C  CE2  . PHE A 1 247 ? 30.25464 51.42098 -1.66291  1.000 10.19961 ? 233 PHE A CE2  1 
ATOM   1932 C  CZ   . PHE A 1 247 ? 29.14805 51.83998 -0.91985  1.000 9.18255  ? 233 PHE A CZ   1 
ATOM   1933 N  N    . PHE A 1 248 ? 30.87674 46.45944 -2.87975  1.000 5.19602  ? 234 PHE A N    1 
ATOM   1934 C  CA   . PHE A 1 248 ? 30.80685 46.42154 -4.34756  1.000 6.20747  ? 234 PHE A CA   1 
ATOM   1935 C  C    . PHE A 1 248 ? 30.69118 44.94931 -4.72744  1.000 8.70630  ? 234 PHE A C    1 
ATOM   1936 O  O    . PHE A 1 248 ? 31.69029 44.22870 -4.73033  1.000 8.94685  ? 234 PHE A O    1 
ATOM   1937 C  CB   . PHE A 1 248 ? 32.07759 46.99359 -4.97342  1.000 7.87988  ? 234 PHE A CB   1 
ATOM   1938 C  CG   . PHE A 1 248 ? 32.28654 48.48232 -4.75498  1.000 13.47835 ? 234 PHE A CG   1 
ATOM   1939 C  CD1  . PHE A 1 248 ? 31.40864 49.41258 -5.28895  1.000 8.34022  ? 234 PHE A CD1  1 
ATOM   1940 C  CD2  . PHE A 1 248 ? 33.41693 48.94403 -4.08752  1.000 9.32311  ? 234 PHE A CD2  1 
ATOM   1941 C  CE1  . PHE A 1 248 ? 31.63564 50.78916 -5.11409  1.000 7.38631  ? 234 PHE A CE1  1 
ATOM   1942 C  CE2  . PHE A 1 248 ? 33.64262 50.30904 -3.90508  1.000 9.19511  ? 234 PHE A CE2  1 
ATOM   1943 C  CZ   . PHE A 1 248 ? 32.75027 51.22936 -4.42395  1.000 9.82467  ? 234 PHE A CZ   1 
ATOM   1944 N  N    . HIS A 1 249 ? 29.48714 44.50698 -5.07611  1.000 7.09232  ? 235 HIS A N    1 
ATOM   1945 C  CA   . HIS A 1 249 ? 29.19028 43.08326 -5.22880  1.000 9.04986  ? 235 HIS A CA   1 
ATOM   1946 C  C    . HIS A 1 249 ? 29.01586 42.73235 -6.70522  1.000 11.12555 ? 235 HIS A C    1 
ATOM   1947 O  O    . HIS A 1 249 ? 27.90889 42.47672 -7.18284  1.000 13.61140 ? 235 HIS A O    1 
ATOM   1948 C  CB   . HIS A 1 249 ? 27.93418 42.74221 -4.39516  1.000 13.07616 ? 235 HIS A CB   1 
ATOM   1949 C  CG   . HIS A 1 249 ? 27.75284 41.28248 -4.11910  1.000 12.65737 ? 235 HIS A CG   1 
ATOM   1950 N  ND1  . HIS A 1 249 ? 27.24991 40.81635 -2.92275  1.000 11.46858 ? 235 HIS A ND1  1 
ATOM   1951 C  CD2  . HIS A 1 249 ? 27.98060 40.18863 -4.88310  1.000 15.97336 ? 235 HIS A CD2  1 
ATOM   1952 C  CE1  . HIS A 1 249 ? 27.19112 39.49748 -2.95510  1.000 12.62770 ? 235 HIS A CE1  1 
ATOM   1953 N  NE2  . HIS A 1 249 ? 27.62063 39.09100 -4.13686  1.000 12.63171 ? 235 HIS A NE2  1 
ATOM   1954 N  N    . GLY A 1 250 ? 30.13544 42.67914 -7.42495  1.000 10.85654 ? 236 GLY A N    1 
ATOM   1955 C  CA   . GLY A 1 250 ? 30.09528 42.32542 -8.83395  1.000 12.95099 ? 236 GLY A CA   1 
ATOM   1956 C  C    . GLY A 1 250 ? 29.87032 40.83948 -9.05813  1.000 15.76294 ? 236 GLY A C    1 
ATOM   1957 O  O    . GLY A 1 250 ? 30.19709 39.99896 -8.22274  1.000 14.53665 ? 236 GLY A O    1 
ATOM   1958 N  N    . GLN A 1 251 ? 29.29078 40.52224 -10.21690 1.000 13.71933 ? 237 GLN A N    1 
ATOM   1959 C  CA   . GLN A 1 251 ? 29.02027 39.13694 -10.59416 1.000 19.56736 ? 237 GLN A CA   1 
ATOM   1960 C  C    . GLN A 1 251 ? 30.22353 38.45773 -11.22824 1.000 24.82455 ? 237 GLN A C    1 
ATOM   1961 O  O    . GLN A 1 251 ? 30.29252 37.22090 -11.24877 1.000 21.42757 ? 237 GLN A O    1 
ATOM   1962 C  CB   . GLN A 1 251 ? 27.85011 39.08564 -11.57835 1.000 24.62901 ? 237 GLN A CB   1 
ATOM   1963 C  CG   . GLN A 1 251 ? 26.50344 39.32826 -10.94529 1.000 41.21239 ? 237 GLN A CG   1 
ATOM   1964 C  CD   . GLN A 1 251 ? 26.22907 38.35567 -9.81900  1.000 50.54445 ? 237 GLN A CD   1 
ATOM   1965 O  OE1  . GLN A 1 251 ? 26.59693 38.60366 -8.66710  1.000 49.25452 ? 237 GLN A OE1  1 
ATOM   1966 N  NE2  . GLN A 1 251 ? 25.58675 37.23534 -10.14368 1.000 46.21591 ? 237 GLN A NE2  1 
ATOM   1967 N  N    . ASP A 1 252 ? 31.15299 39.24667 -11.75001 1.000 18.20317 ? 238 ASP A N    1 
ATOM   1968 C  CA   . ASP A 1 252 ? 32.39722 38.80228 -12.35992 1.000 16.35321 ? 238 ASP A CA   1 
ATOM   1969 C  C    . ASP A 1 252 ? 33.30945 40.01876 -12.38012 1.000 15.71932 ? 238 ASP A C    1 
ATOM   1970 O  O    . ASP A 1 252 ? 32.92550 41.09857 -11.92388 1.000 12.36256 ? 238 ASP A O    1 
ATOM   1971 C  CB   . ASP A 1 252 ? 32.15276 38.23957 -13.76284 1.000 20.11305 ? 238 ASP A CB   1 
ATOM   1972 C  CG   . ASP A 1 252 ? 31.31524 39.16658 -14.62307 1.000 23.39975 ? 238 ASP A CG   1 
ATOM   1973 O  OD1  . ASP A 1 252 ? 31.73605 40.32208 -14.83652 1.000 25.68955 ? 238 ASP A OD1  1 
ATOM   1974 O  OD2  . ASP A 1 252 ? 30.23692 38.74477 -15.09488 1.000 29.38054 ? 238 ASP A OD2  1 
ATOM   1975 N  N    . ASN A 1 253 ? 34.52128 39.84477 -12.91438 1.000 13.66884 ? 239 ASN A N    1 
ATOM   1976 C  CA   . ASN A 1 253 ? 35.49501 40.93557 -12.88935 1.000 12.71407 ? 239 ASN A CA   1 
ATOM   1977 C  C    . ASN A 1 253 ? 35.05170 42.13065 -13.72517 1.000 16.00003 ? 239 ASN A C    1 
ATOM   1978 O  O    . ASN A 1 253 ? 35.36424 43.27606 -13.37628 1.000 18.68048 ? 239 ASN A O    1 
ATOM   1979 C  CB   . ASN A 1 253 ? 36.86805 40.45104 -13.34531 1.000 14.80474 ? 239 ASN A CB   1 
ATOM   1980 C  CG   . ASN A 1 253 ? 37.55887 39.57223 -12.30809 1.000 19.22919 ? 239 ASN A CG   1 
ATOM   1981 O  OD1  . ASN A 1 253 ? 37.11873 39.47097 -11.16163 1.000 16.32115 ? 239 ASN A OD1  1 
ATOM   1982 N  ND2  . ASN A 1 253 ? 38.66093 38.94369 -12.70883 1.000 25.27227 ? 239 ASN A ND2  1 
ATOM   1983 N  N    . TYR A 1 254 ? 34.36231 41.89288 -14.84531 1.000 12.83087 ? 240 TYR A N    1 
ATOM   1984 C  CA   . TYR A 1 254 ? 33.83541 43.00404 -15.63173 1.000 16.91602 ? 240 TYR A CA   1 
ATOM   1985 C  C    . TYR A 1 254 ? 32.77385 43.75790 -14.85181 1.000 13.18482 ? 240 TYR A C    1 
ATOM   1986 O  O    . TYR A 1 254 ? 32.84257 44.98756 -14.70518 1.000 13.10578 ? 240 TYR A O    1 
ATOM   1987 C  CB   . TYR A 1 254 ? 33.24086 42.48834 -16.93913 1.000 14.29587 ? 240 TYR A CB   1 
ATOM   1988 C  CG   . TYR A 1 254 ? 34.24298 41.92557 -17.92024 1.000 17.79224 ? 240 TYR A CG   1 
ATOM   1989 C  CD1  . TYR A 1 254 ? 35.11664 42.75969 -18.60247 1.000 17.93254 ? 240 TYR A CD1  1 
ATOM   1990 C  CD2  . TYR A 1 254 ? 34.28648 40.56434 -18.19647 1.000 24.13615 ? 240 TYR A CD2  1 
ATOM   1991 C  CE1  . TYR A 1 254 ? 36.02916 42.24999 -19.52270 1.000 24.99778 ? 240 TYR A CE1  1 
ATOM   1992 C  CE2  . TYR A 1 254 ? 35.19755 40.04421 -19.11528 1.000 25.53689 ? 240 TYR A CE2  1 
ATOM   1993 C  CZ   . TYR A 1 254 ? 36.06283 40.89232 -19.76952 1.000 30.69299 ? 240 TYR A CZ   1 
ATOM   1994 O  OH   . TYR A 1 254 ? 36.96228 40.38357 -20.67778 1.000 32.92154 ? 240 TYR A OH   1 
ATOM   1995 N  N    . ASP A 1 255 ? 31.78244 43.02892 -14.33531 1.000 11.93866 ? 241 ASP A N    1 
ATOM   1996 C  CA   . ASP A 1 255 ? 30.71714 43.66365 -13.57372 1.000 11.66305 ? 241 ASP A CA   1 
ATOM   1997 C  C    . ASP A 1 255 ? 31.25366 44.35309 -12.32374 1.000 11.51997 ? 241 ASP A C    1 
ATOM   1998 O  O    . ASP A 1 255 ? 30.64804 45.31616 -11.84091 1.000 11.16560 ? 241 ASP A O    1 
ATOM   1999 C  CB   . ASP A 1 255 ? 29.64775 42.62613 -13.22364 1.000 11.82496 ? 241 ASP A CB   1 
ATOM   2000 C  CG   . ASP A 1 255 ? 28.44116 43.23834 -12.56439 1.000 15.99150 ? 241 ASP A CG   1 
ATOM   2001 O  OD1  . ASP A 1 255 ? 27.84175 44.16980 -13.15235 1.000 16.27308 ? 241 ASP A OD1  1 
ATOM   2002 O  OD2  . ASP A 1 255 ? 28.08451 42.78138 -11.46242 1.000 17.23088 ? 241 ASP A OD2  1 
ATOM   2003 N  N    . GLN A 1 256 ? 32.38159 43.87798 -11.78880 1.000 12.43916 ? 242 GLN A N    1 
ATOM   2004 C  CA   . GLN A 1 256 ? 32.96680 44.50775 -10.60815 1.000 11.40663 ? 242 GLN A CA   1 
ATOM   2005 C  C    . GLN A 1 256 ? 33.35163 45.95794 -10.88635 1.000 9.40157  ? 242 GLN A C    1 
ATOM   2006 O  O    . GLN A 1 256 ? 33.06920 46.85018 -10.07727 1.000 8.80222  ? 242 GLN A O    1 
ATOM   2007 C  CB   . GLN A 1 256 ? 34.17001 43.69220 -10.13111 1.000 9.41142  ? 242 GLN A CB   1 
ATOM   2008 C  CG   . GLN A 1 256 ? 34.77576 44.15141 -8.81625  1.000 9.34570  ? 242 GLN A CG   1 
ATOM   2009 C  CD   . GLN A 1 256 ? 33.85323 43.96614 -7.63561  1.000 5.72622  ? 242 GLN A CD   1 
ATOM   2010 O  OE1  . GLN A 1 256 ? 33.02464 43.05405 -7.60395  1.000 10.25581 ? 242 GLN A OE1  1 
ATOM   2011 N  NE2  . GLN A 1 256 ? 33.99887 44.83039 -6.63717  1.000 10.34347 ? 242 GLN A NE2  1 
ATOM   2012 N  N    . LEU A 1 257 ? 33.98172 46.21728 -12.03443 1.000 9.50084  ? 243 LEU A N    1 
ATOM   2013 C  CA   . LEU A 1 257 ? 34.31584 47.59226 -12.39765 1.000 8.05442  ? 243 LEU A CA   1 
ATOM   2014 C  C    . LEU A 1 257 ? 33.06350 48.41643 -12.68669 1.000 8.25665  ? 243 LEU A C    1 
ATOM   2015 O  O    . LEU A 1 257 ? 33.01625 49.61167 -12.36554 1.000 10.78371 ? 243 LEU A O    1 
ATOM   2016 C  CB   . LEU A 1 257 ? 35.25277 47.60552 -13.60840 1.000 10.16927 ? 243 LEU A CB   1 
ATOM   2017 C  CG   . LEU A 1 257 ? 35.79831 48.99086 -13.96672 1.000 10.38855 ? 243 LEU A CG   1 
ATOM   2018 C  CD1  . LEU A 1 257 ? 36.62972 49.55924 -12.81777 1.000 11.78547 ? 243 LEU A CD1  1 
ATOM   2019 C  CD2  . LEU A 1 257 ? 36.60340 48.92189 -15.25522 1.000 12.45475 ? 243 LEU A CD2  1 
ATOM   2020 N  N    . VAL A 1 258 ? 32.04324 47.80999 -13.30228 1.000 9.76246  ? 244 VAL A N    1 
ATOM   2021 C  CA   . VAL A 1 258 ? 30.79309 48.53585 -13.52847 1.000 9.19016  ? 244 VAL A CA   1 
ATOM   2022 C  C    . VAL A 1 258 ? 30.18870 49.00387 -12.20562 1.000 13.74142 ? 244 VAL A C    1 
ATOM   2023 O  O    . VAL A 1 258 ? 29.75138 50.15834 -12.08313 1.000 11.36396 ? 244 VAL A O    1 
ATOM   2024 C  CB   . VAL A 1 258 ? 29.79974 47.69245 -14.34828 1.000 13.79626 ? 244 VAL A CB   1 
ATOM   2025 C  CG1  . VAL A 1 258 ? 28.51936 48.47443 -14.57914 1.000 14.38098 ? 244 VAL A CG1  1 
ATOM   2026 C  CG2  . VAL A 1 258 ? 30.42230 47.27818 -15.68120 1.000 11.19245 ? 244 VAL A CG2  1 
ATOM   2027 N  N    . ARG A 1 259 ? 30.16981 48.12282 -11.19012 1.000 7.84559  ? 245 ARG A N    1 
ATOM   2028 C  CA   . ARG A 1 259 ? 29.61617 48.48851 -9.88329  1.000 8.87833  ? 245 ARG A CA   1 
ATOM   2029 C  C    . ARG A 1 259 ? 30.39441 49.63540 -9.25707  1.000 11.43196 ? 245 ARG A C    1 
ATOM   2030 O  O    . ARG A 1 259 ? 29.82126 50.47890 -8.55705  1.000 11.97886 ? 245 ARG A O    1 
ATOM   2031 C  CB   . ARG A 1 259 ? 29.65978 47.29915 -8.91704  1.000 12.06995 ? 245 ARG A CB   1 
ATOM   2032 C  CG   . ARG A 1 259 ? 28.92082 46.04078 -9.33502  1.000 18.36605 ? 245 ARG A CG   1 
ATOM   2033 C  CD   . ARG A 1 259 ? 27.45960 46.26607 -9.44063  1.000 16.62303 ? 245 ARG A CD   1 
ATOM   2034 N  NE   . ARG A 1 259 ? 26.76096 45.03453 -9.79362  1.000 20.26475 ? 245 ARG A NE   1 
ATOM   2035 C  CZ   . ARG A 1 259 ? 25.80478 44.48315 -9.06125  1.000 25.12131 ? 245 ARG A CZ   1 
ATOM   2036 N  NH1  . ARG A 1 259 ? 25.43033 45.01281 -7.90608  1.000 28.59682 ? 245 ARG A NH1  1 
ATOM   2037 N  NH2  . ARG A 1 259 ? 25.19395 43.38457 -9.50888  1.000 23.25841 ? 245 ARG A NH2  1 
ATOM   2038 N  N    . ILE A 1 260 ? 31.71395 49.64830 -9.44822  1.000 9.20409  ? 246 ILE A N    1 
ATOM   2039 C  CA   . ILE A 1 260 ? 32.52299 50.74460 -8.93132  1.000 7.24207  ? 246 ILE A CA   1 
ATOM   2040 C  C    . ILE A 1 260 ? 32.20374 52.03457 -9.67538  1.000 12.79979 ? 246 ILE A C    1 
ATOM   2041 O  O    . ILE A 1 260 ? 32.02306 53.10025 -9.06780  1.000 11.38389 ? 246 ILE A O    1 
ATOM   2042 C  CB   . ILE A 1 260 ? 34.01448 50.38344 -9.00726  1.000 9.50675  ? 246 ILE A CB   1 
ATOM   2043 C  CG1  . ILE A 1 260 ? 34.31573 49.21588 -8.06361  1.000 9.27669  ? 246 ILE A CG1  1 
ATOM   2044 C  CG2  . ILE A 1 260 ? 34.86426 51.60435 -8.68066  1.000 9.20621  ? 246 ILE A CG2  1 
ATOM   2045 C  CD1  . ILE A 1 260 ? 35.66920 48.55877 -8.30412  1.000 8.40863  ? 246 ILE A CD1  1 
ATOM   2046 N  N    . ALA A 1 261 ? 32.12050 51.95162 -11.00468 1.000 10.34065 ? 247 ALA A N    1 
ATOM   2047 C  CA   . ALA A 1 261 ? 31.91262 53.14330 -11.81705 1.000 12.24296 ? 247 ALA A CA   1 
ATOM   2048 C  C    . ALA A 1 261 ? 30.54625 53.77133 -11.57702 1.000 11.83059 ? 247 ALA A C    1 
ATOM   2049 O  O    . ALA A 1 261 ? 30.40155 54.98765 -11.73519 1.000 12.53152 ? 247 ALA A O    1 
ATOM   2050 C  CB   . ALA A 1 261 ? 32.09013 52.80801 -13.29572 1.000 11.07824 ? 247 ALA A CB   1 
ATOM   2051 N  N    . LYS A 1 262 ? 29.53718 52.97475 -11.20337 1.000 12.03250 ? 248 LYS A N    1 
ATOM   2052 C  CA   . LYS A 1 262 ? 28.23709 53.55064 -10.86103 1.000 14.89365 ? 248 LYS A CA   1 
ATOM   2053 C  C    . LYS A 1 262 ? 28.29760 54.42786 -9.61724  1.000 13.35326 ? 248 LYS A C    1 
ATOM   2054 O  O    . LYS A 1 262 ? 27.37019 55.20890 -9.37843  1.000 16.60832 ? 248 LYS A O    1 
ATOM   2055 C  CB   . LYS A 1 262 ? 27.18413 52.45119 -10.68004 1.000 15.68843 ? 248 LYS A CB   1 
ATOM   2056 C  CG   . LYS A 1 262 ? 26.80034 51.79194 -11.98121 1.000 23.67292 ? 248 LYS A CG   1 
ATOM   2057 C  CD   . LYS A 1 262 ? 25.74885 50.70071 -11.79423 1.000 25.81543 ? 248 LYS A CD   1 
ATOM   2058 C  CE   . LYS A 1 262 ? 25.28709 50.18067 -13.14757 1.000 22.17293 ? 248 LYS A CE   1 
ATOM   2059 N  NZ   . LYS A 1 262 ? 24.27893 49.09365 -12.98821 1.000 45.16654 ? 248 LYS A NZ   1 
ATOM   2060 N  N    . VAL A 1 263 ? 29.35288 54.31070 -8.82135  1.000 10.03730 ? 249 VAL A N    1 
ATOM   2061 C  CA   . VAL A 1 263 ? 29.53363 55.12242 -7.63074  1.000 11.60377 ? 249 VAL A CA   1 
ATOM   2062 C  C    . VAL A 1 263 ? 30.55385 56.23049 -7.85788  1.000 10.75660 ? 249 VAL A C    1 
ATOM   2063 O  O    . VAL A 1 263 ? 30.26321 57.40417 -7.62485  1.000 11.20926 ? 249 VAL A O    1 
ATOM   2064 C  CB   . VAL A 1 263 ? 29.89422 54.23302 -6.41943  1.000 8.80289  ? 249 VAL A CB   1 
ATOM   2065 C  CG1  . VAL A 1 263 ? 30.05964 55.07803 -5.17414  1.000 9.48580  ? 249 VAL A CG1  1 
ATOM   2066 C  CG2  . VAL A 1 263 ? 28.81001 53.17964 -6.20432  1.000 8.75444  ? 249 VAL A CG2  1 
ATOM   2067 N  N    . LEU A 1 264 ? 31.75032 55.87999 -8.35142  1.000 6.97000  ? 250 LEU A N    1 
ATOM   2068 C  CA   . LEU A 1 264 ? 32.81510 56.86387 -8.52874  1.000 5.36446  ? 250 LEU A CA   1 
ATOM   2069 C  C    . LEU A 1 264 ? 32.69611 57.67106 -9.82078  1.000 7.84900  ? 250 LEU A C    1 
ATOM   2070 O  O    . LEU A 1 264 ? 33.35975 58.70926 -9.95234  1.000 11.07771 ? 250 LEU A O    1 
ATOM   2071 C  CB   . LEU A 1 264 ? 34.18452 56.17880 -8.45877  1.000 8.43443  ? 250 LEU A CB   1 
ATOM   2072 C  CG   . LEU A 1 264 ? 34.77190 55.86234 -7.08129  1.000 8.77083  ? 250 LEU A CG   1 
ATOM   2073 C  CD1  . LEU A 1 264 ? 33.88717 54.96830 -6.24351  1.000 15.00834 ? 250 LEU A CD1  1 
ATOM   2074 C  CD2  . LEU A 1 264 ? 36.14659 55.21775 -7.25332  1.000 5.47757  ? 250 LEU A CD2  1 
ATOM   2075 N  N    . GLY A 1 265 ? 31.89213 57.21465 -10.77684 1.000 12.81584 ? 251 GLY A N    1 
ATOM   2076 C  CA   . GLY A 1 265 ? 31.64759 57.95463 -12.00305 1.000 13.23812 ? 251 GLY A CA   1 
ATOM   2077 C  C    . GLY A 1 265 ? 32.43448 57.46104 -13.19901 1.000 11.74092 ? 251 GLY A C    1 
ATOM   2078 O  O    . GLY A 1 265 ? 33.58482 57.04811 -13.05324 1.000 13.26378 ? 251 GLY A O    1 
ATOM   2079 N  N    . THR A 1 266 ? 31.83523 57.50378 -14.39249 1.000 11.05399 ? 252 THR A N    1 
ATOM   2080 C  CA   . THR A 1 266 ? 32.53752 57.01670 -15.58258 1.000 13.65233 ? 252 THR A CA   1 
ATOM   2081 C  C    . THR A 1 266 ? 33.52038 58.03782 -16.15244 1.000 16.60420 ? 252 THR A C    1 
ATOM   2082 O  O    . THR A 1 266 ? 34.60229 57.66053 -16.61741 1.000 12.54575 ? 252 THR A O    1 
ATOM   2083 C  CB   . THR A 1 266 ? 31.53927 56.57433 -16.64795 1.000 15.44626 ? 252 THR A CB   1 
ATOM   2084 O  OG1  . THR A 1 266 ? 30.52455 57.57775 -16.78365 1.000 13.86692 ? 252 THR A OG1  1 
ATOM   2085 C  CG2  . THR A 1 266 ? 30.89757 55.27020 -16.24086 1.000 13.14339 ? 252 THR A CG2  1 
ATOM   2086 N  N    . GLU A 1 267 ? 33.17537 59.32847 -16.15768 1.000 14.14696 ? 253 GLU A N    1 
ATOM   2087 C  CA   . GLU A 1 267 ? 34.14236 60.30379 -16.65681 1.000 15.90085 ? 253 GLU A CA   1 
ATOM   2088 C  C    . GLU A 1 267 ? 35.37968 60.31055 -15.78171 1.000 14.07172 ? 253 GLU A C    1 
ATOM   2089 O  O    . GLU A 1 267 ? 36.50223 60.46549 -16.27124 1.000 14.28909 ? 253 GLU A O    1 
ATOM   2090 C  CB   . GLU A 1 267 ? 33.52718 61.70039 -16.74631 1.000 13.70320 ? 253 GLU A CB   1 
ATOM   2091 C  CG   . GLU A 1 267 ? 32.52451 61.85402 -17.89385 1.000 19.62683 ? 253 GLU A CG   1 
ATOM   2092 C  CD   . GLU A 1 267 ? 33.13489 61.60078 -19.27766 1.000 21.04915 ? 253 GLU A CD   1 
ATOM   2093 O  OE1  . GLU A 1 267 ? 34.07693 62.32012 -19.68423 1.000 24.09016 ? 253 GLU A OE1  1 
ATOM   2094 O  OE2  . GLU A 1 267 ? 32.66400 60.66921 -19.96590 1.000 36.80418 ? 253 GLU A OE2  1 
ATOM   2095 N  N    . GLU A 1 268 ? 35.18656 60.10646 -14.48077 1.000 12.44819 ? 254 GLU A N    1 
ATOM   2096 C  CA   . GLU A 1 268 ? 36.30379 60.02759 -13.55624 1.000 11.14102 ? 254 GLU A CA   1 
ATOM   2097 C  C    . GLU A 1 268 ? 37.16706 58.80985 -13.84647 1.000 11.59412 ? 254 GLU A C    1 
ATOM   2098 O  O    . GLU A 1 268 ? 38.40051 58.88013 -13.75729 1.000 12.44724 ? 254 GLU A O    1 
ATOM   2099 C  CB   . GLU A 1 268 ? 35.75071 60.00763 -12.12952 1.000 10.94149 ? 254 GLU A CB   1 
ATOM   2100 C  CG   . GLU A 1 268 ? 35.10048 61.35324 -11.67760 1.000 14.39729 ? 254 GLU A CG   1 
ATOM   2101 C  CD   . GLU A 1 268 ? 33.68644 61.60863 -12.20542 1.000 20.17318 ? 254 GLU A CD   1 
ATOM   2102 O  OE1  . GLU A 1 268 ? 33.05004 60.69073 -12.76938 1.000 15.16674 ? 254 GLU A OE1  1 
ATOM   2103 O  OE2  . GLU A 1 268 ? 33.19294 62.75378 -12.03998 1.000 17.47454 ? 254 GLU A OE2  1 
ATOM   2104 N  N    . LEU A 1 269 ? 36.53820 57.68670 -14.20424 1.000 11.73357 ? 255 LEU A N    1 
ATOM   2105 C  CA   . LEU A 1 269 ? 37.29446 56.50896 -14.62378 1.000 9.80678  ? 255 LEU A CA   1 
ATOM   2106 C  C    . LEU A 1 269 ? 38.15996 56.80960 -15.84111 1.000 9.83377  ? 255 LEU A C    1 
ATOM   2107 O  O    . LEU A 1 269 ? 39.34635 56.47159 -15.86986 1.000 9.52673  ? 255 LEU A O    1 
ATOM   2108 C  CB   . LEU A 1 269 ? 36.33831 55.35103 -14.92549 1.000 11.10319 ? 255 LEU A CB   1 
ATOM   2109 C  CG   . LEU A 1 269 ? 36.93083 54.09549 -15.58996 1.000 9.63324  ? 255 LEU A CG   1 
ATOM   2110 C  CD1  . LEU A 1 269 ? 37.99159 53.43278 -14.70637 1.000 10.46665 ? 255 LEU A CD1  1 
ATOM   2111 C  CD2  . LEU A 1 269 ? 35.82639 53.10996 -15.92467 1.000 11.97733 ? 255 LEU A CD2  1 
ATOM   2112 N  N    . TYR A 1 270 ? 37.57794 57.42766 -16.87391 1.000 9.68816  ? 256 TYR A N    1 
ATOM   2113 C  CA   . TYR A 1 270 ? 38.34745 57.68496 -18.08829 1.000 8.20530  ? 256 TYR A CA   1 
ATOM   2114 C  C    . TYR A 1 270 ? 39.49475 58.65453 -17.83390 1.000 11.19614 ? 256 TYR A C    1 
ATOM   2115 O  O    . TYR A 1 270 ? 40.55572 58.53394 -18.45492 1.000 14.54667 ? 256 TYR A O    1 
ATOM   2116 C  CB   . TYR A 1 270 ? 37.43355 58.21777 -19.19279 1.000 10.87828 ? 256 TYR A CB   1 
ATOM   2117 C  CG   . TYR A 1 270 ? 36.24040 57.33699 -19.50148 1.000 10.64453 ? 256 TYR A CG   1 
ATOM   2118 C  CD1  . TYR A 1 270 ? 36.34367 55.94585 -19.51198 1.000 11.65004 ? 256 TYR A CD1  1 
ATOM   2119 C  CD2  . TYR A 1 270 ? 35.00608 57.90476 -19.78355 1.000 10.60457 ? 256 TYR A CD2  1 
ATOM   2120 C  CE1  . TYR A 1 270 ? 35.23434 55.15064 -19.81022 1.000 12.54697 ? 256 TYR A CE1  1 
ATOM   2121 C  CE2  . TYR A 1 270 ? 33.90416 57.13147 -20.07048 1.000 11.95561 ? 256 TYR A CE2  1 
ATOM   2122 C  CZ   . TYR A 1 270 ? 34.01854 55.76042 -20.08845 1.000 12.26053 ? 256 TYR A CZ   1 
ATOM   2123 O  OH   . TYR A 1 270 ? 32.89598 55.02103 -20.37489 1.000 20.59724 ? 256 TYR A OH   1 
ATOM   2124 N  N    . GLY A 1 271 ? 39.31332 59.61371 -16.92358 1.000 12.33295 ? 257 GLY A N    1 
ATOM   2125 C  CA   . GLY A 1 271 ? 40.41003 60.50578 -16.58775 1.000 11.73244 ? 257 GLY A CA   1 
ATOM   2126 C  C    . GLY A 1 271 ? 41.57035 59.77663 -15.93503 1.000 12.90913 ? 257 GLY A C    1 
ATOM   2127 O  O    . GLY A 1 271 ? 42.73673 60.08359 -16.19607 1.000 10.87022 ? 257 GLY A O    1 
ATOM   2128 N  N    . TYR A 1 272 ? 41.26243 58.79604 -15.08586 1.000 9.29888  ? 258 TYR A N    1 
ATOM   2129 C  CA   . TYR A 1 272 ? 42.29422 57.96608 -14.47251 1.000 9.68589  ? 258 TYR A CA   1 
ATOM   2130 C  C    . TYR A 1 272 ? 43.02423 57.13824 -15.51709 1.000 8.77262  ? 258 TYR A C    1 
ATOM   2131 O  O    . TYR A 1 272 ? 44.25938 57.08816 -15.53415 1.000 10.64800 ? 258 TYR A O    1 
ATOM   2132 C  CB   . TYR A 1 272 ? 41.63244 57.05746 -13.43746 1.000 9.57572  ? 258 TYR A CB   1 
ATOM   2133 C  CG   . TYR A 1 272 ? 42.48953 55.91398 -12.92288 1.000 8.51013  ? 258 TYR A CG   1 
ATOM   2134 C  CD1  . TYR A 1 272 ? 43.67351 56.16267 -12.24796 1.000 9.17152  ? 258 TYR A CD1  1 
ATOM   2135 C  CD2  . TYR A 1 272 ? 42.08423 54.58676 -13.07487 1.000 9.96650  ? 258 TYR A CD2  1 
ATOM   2136 C  CE1  . TYR A 1 272 ? 44.43723 55.12842 -11.74128 1.000 8.72276  ? 258 TYR A CE1  1 
ATOM   2137 C  CE2  . TYR A 1 272 ? 42.85314 53.54232 -12.58408 1.000 11.54974 ? 258 TYR A CE2  1 
ATOM   2138 C  CZ   . TYR A 1 272 ? 44.03529 53.82659 -11.92787 1.000 10.65731 ? 258 TYR A CZ   1 
ATOM   2139 O  OH   . TYR A 1 272 ? 44.79395 52.80062 -11.41891 1.000 12.29983 ? 258 TYR A OH   1 
ATOM   2140 N  N    . LEU A 1 273 ? 42.27418 56.47875 -16.40071 1.000 10.21539 ? 259 LEU A N    1 
ATOM   2141 C  CA   . LEU A 1 273 ? 42.89676 55.71669 -17.47957 1.000 9.11269  ? 259 LEU A CA   1 
ATOM   2142 C  C    . LEU A 1 273 ? 43.80245 56.60005 -18.32766 1.000 10.90005 ? 259 LEU A C    1 
ATOM   2143 O  O    . LEU A 1 273 ? 44.89799 56.18685 -18.72070 1.000 11.83651 ? 259 LEU A O    1 
ATOM   2144 C  CB   . LEU A 1 273 ? 41.82162 55.09073 -18.36303 1.000 13.42960 ? 259 LEU A CB   1 
ATOM   2145 C  CG   . LEU A 1 273 ? 40.81890 54.13354 -17.71447 1.000 10.40076 ? 259 LEU A CG   1 
ATOM   2146 C  CD1  . LEU A 1 273 ? 39.81086 53.65593 -18.75564 1.000 13.39966 ? 259 LEU A CD1  1 
ATOM   2147 C  CD2  . LEU A 1 273 ? 41.50496 52.94941 -17.02616 1.000 13.35970 ? 259 LEU A CD2  1 
ATOM   2148 N  N    . LYS A 1 274 ? 43.35784 57.81492 -18.63103 1.000 9.20204  ? 260 LYS A N    1 
ATOM   2149 C  CA   . LYS A 1 274 ? 44.16826 58.69457 -19.46533 1.000 12.59555 ? 260 LYS A CA   1 
ATOM   2150 C  C    . LYS A 1 274 ? 45.45238 59.08948 -18.75277 1.000 14.85911 ? 260 LYS A C    1 
ATOM   2151 O  O    . LYS A 1 274 ? 46.51907 59.14847 -19.37295 1.000 14.31367 ? 260 LYS A O    1 
ATOM   2152 C  CB   . LYS A 1 274 ? 43.36175 59.92976 -19.87569 1.000 13.65833 ? 260 LYS A CB   1 
ATOM   2153 C  CG   . LYS A 1 274 ? 44.18996 60.98944 -20.62175 1.000 17.04563 ? 260 LYS A CG   1 
ATOM   2154 C  CD   . LYS A 1 274 ? 43.34015 62.19313 -20.98023 1.000 16.19393 ? 260 LYS A CD   1 
ATOM   2155 C  CE   . LYS A 1 274 ? 44.18145 63.36035 -21.48376 1.000 22.49462 ? 260 LYS A CE   1 
ATOM   2156 N  NZ   . LYS A 1 274 ? 44.87134 63.06987 -22.78404 1.000 28.48000 ? 260 LYS A NZ   1 
ATOM   2157 N  N    . LYS A 1 275 ? 45.37363 59.34562 -17.44217 1.000 9.08677  ? 261 LYS A N    1 
ATOM   2158 C  CA   . LYS A 1 275 ? 46.55668 59.79243 -16.71371 1.000 12.96101 ? 261 LYS A CA   1 
ATOM   2159 C  C    . LYS A 1 275 ? 47.66445 58.75024 -16.75293 1.000 13.84399 ? 261 LYS A C    1 
ATOM   2160 O  O    . LYS A 1 275 ? 48.84198 59.09830 -16.87738 1.000 12.34877 ? 261 LYS A O    1 
ATOM   2161 C  CB   . LYS A 1 275 ? 46.19627 60.14671 -15.27148 1.000 13.29985 ? 261 LYS A CB   1 
ATOM   2162 C  CG   . LYS A 1 275 ? 47.39617 60.55463 -14.41603 1.000 10.97215 ? 261 LYS A CG   1 
ATOM   2163 C  CD   . LYS A 1 275 ? 46.96894 60.93574 -12.99643 1.000 12.73350 ? 261 LYS A CD   1 
ATOM   2164 C  CE   . LYS A 1 275 ? 48.18096 61.23630 -12.13586 1.000 10.86744 ? 261 LYS A CE   1 
ATOM   2165 N  NZ   . LYS A 1 275 ? 47.80429 61.50850 -10.71175 1.000 14.12492 ? 261 LYS A NZ   1 
ATOM   2166 N  N    . TYR A 1 276 ? 47.31406 57.46942 -16.66488 1.000 12.20816 ? 262 TYR A N    1 
ATOM   2167 C  CA   . TYR A 1 276 ? 48.31258 56.40827 -16.62568 1.000 11.92214 ? 262 TYR A CA   1 
ATOM   2168 C  C    . TYR A 1 276 ? 48.45305 55.66587 -17.94745 1.000 12.75286 ? 262 TYR A C    1 
ATOM   2169 O  O    . TYR A 1 276 ? 49.13798 54.64080 -17.99992 1.000 14.04807 ? 262 TYR A O    1 
ATOM   2170 C  CB   . TYR A 1 276 ? 48.06607 55.45597 -15.44075 1.000 12.94477 ? 262 TYR A CB   1 
ATOM   2171 C  CG   . TYR A 1 276 ? 48.17238 56.16404 -14.10403 1.000 13.52645 ? 262 TYR A CG   1 
ATOM   2172 C  CD1  . TYR A 1 276 ? 49.39264 56.28290 -13.44780 1.000 14.48019 ? 262 TYR A CD1  1 
ATOM   2173 C  CD2  . TYR A 1 276 ? 47.06083 56.74352 -13.52098 1.000 8.51716  ? 262 TYR A CD2  1 
ATOM   2174 C  CE1  . TYR A 1 276 ? 49.49567 56.95508 -12.23089 1.000 9.38437  ? 262 TYR A CE1  1 
ATOM   2175 C  CE2  . TYR A 1 276 ? 47.14976 57.41512 -12.31203 1.000 15.99587 ? 262 TYR A CE2  1 
ATOM   2176 C  CZ   . TYR A 1 276 ? 48.37202 57.51406 -11.67705 1.000 14.04190 ? 262 TYR A CZ   1 
ATOM   2177 O  OH   . TYR A 1 276 ? 48.45630 58.19071 -10.48911 1.000 15.66738 ? 262 TYR A OH   1 
ATOM   2178 N  N    . HIS A 1 277 ? 47.84123 56.17251 -19.01712 1.000 12.82034 ? 263 HIS A N    1 
ATOM   2179 C  CA   . HIS A 1 277 ? 47.94005 55.56359 -20.34247 1.000 11.69173 ? 263 HIS A CA   1 
ATOM   2180 C  C    . HIS A 1 277 ? 47.45029 54.11340 -20.34430 1.000 14.94578 ? 263 HIS A C    1 
ATOM   2181 O  O    . HIS A 1 277 ? 48.02312 53.24365 -21.00517 1.000 16.21513 ? 263 HIS A O    1 
ATOM   2182 C  CB   . HIS A 1 277 ? 49.35242 55.70110 -20.92291 1.000 20.05403 ? 263 HIS A CB   1 
ATOM   2183 C  CG   . HIS A 1 277 ? 49.87889 57.10097 -20.86495 1.000 17.40098 ? 263 HIS A CG   1 
ATOM   2184 N  ND1  . HIS A 1 277 ? 49.67795 58.01560 -21.87604 1.000 35.29091 ? 263 HIS A ND1  1 
ATOM   2185 C  CD2  . HIS A 1 277 ? 50.55462 57.75825 -19.89268 1.000 28.90632 ? 263 HIS A CD2  1 
ATOM   2186 C  CE1  . HIS A 1 277 ? 50.23037 59.16791 -21.54072 1.000 29.47015 ? 263 HIS A CE1  1 
ATOM   2187 N  NE2  . HIS A 1 277 ? 50.76564 59.03900 -20.34025 1.000 23.34540 ? 263 HIS A NE2  1 
ATOM   2188 N  N    . ILE A 1 278 ? 46.37078 53.85104 -19.60352 1.000 14.22488 ? 264 ILE A N    1 
ATOM   2189 C  CA   . ILE A 1 278 ? 45.83601 52.49964 -19.45039 1.000 14.73419 ? 264 ILE A CA   1 
ATOM   2190 C  C    . ILE A 1 278 ? 44.84933 52.20744 -20.57200 1.000 15.53930 ? 264 ILE A C    1 
ATOM   2191 O  O    . ILE A 1 278 ? 43.91372 52.98091 -20.81024 1.000 13.87193 ? 264 ILE A O    1 
ATOM   2192 C  CB   . ILE A 1 278 ? 45.16225 52.32484 -18.08020 1.000 15.66014 ? 264 ILE A CB   1 
ATOM   2193 C  CG1  . ILE A 1 278 ? 46.14718 52.58001 -16.94335 1.000 10.52911 ? 264 ILE A CG1  1 
ATOM   2194 C  CG2  . ILE A 1 278 ? 44.57104 50.92334 -17.95832 1.000 13.55793 ? 264 ILE A CG2  1 
ATOM   2195 C  CD1  . ILE A 1 278 ? 45.47414 52.69170 -15.58517 1.000 11.58808 ? 264 ILE A CD1  1 
ATOM   2196 N  N    . ASP A 1 279 ? 45.04995 51.08101 -21.25395 1.000 15.36035 ? 265 ASP A N    1 
ATOM   2197 C  CA   . ASP A 1 279 ? 44.10199 50.61749 -22.25346 1.000 14.10254 ? 265 ASP A CA   1 
ATOM   2198 C  C    . ASP A 1 279 ? 42.94101 49.91578 -21.57012 1.000 15.72366 ? 265 ASP A C    1 
ATOM   2199 O  O    . ASP A 1 279 ? 43.13631 49.13368 -20.63478 1.000 19.48466 ? 265 ASP A O    1 
ATOM   2200 C  CB   . ASP A 1 279 ? 44.78367 49.63833 -23.20567 1.000 19.35211 ? 265 ASP A CB   1 
ATOM   2201 C  CG   . ASP A 1 279 ? 45.80901 50.31278 -24.08404 1.000 37.94258 ? 265 ASP A CG   1 
ATOM   2202 O  OD1  . ASP A 1 279 ? 45.68236 51.54327 -24.29674 1.000 24.66863 ? 265 ASP A OD1  1 
ATOM   2203 O  OD2  . ASP A 1 279 ? 46.73588 49.61507 -24.56061 1.000 36.43292 ? 265 ASP A OD2  1 
ATOM   2204 N  N    . LEU A 1 280 ? 41.72930 50.20543 -22.03679 1.000 16.75658 ? 266 LEU A N    1 
ATOM   2205 C  CA   . LEU A 1 280 ? 40.51546 49.62399 -21.48079 1.000 16.62095 ? 266 LEU A CA   1 
ATOM   2206 C  C    . LEU A 1 280 ? 40.00599 48.54357 -22.42248 1.000 17.31308 ? 266 LEU A C    1 
ATOM   2207 O  O    . LEU A 1 280 ? 39.84027 48.79181 -23.62083 1.000 15.57477 ? 266 LEU A O    1 
ATOM   2208 C  CB   . LEU A 1 280 ? 39.44681 50.70164 -21.30583 1.000 17.90902 ? 266 LEU A CB   1 
ATOM   2209 C  CG   . LEU A 1 280 ? 38.16032 50.27961 -20.60000 1.000 16.83137 ? 266 LEU A CG   1 
ATOM   2210 C  CD1  . LEU A 1 280 ? 38.40690 49.94228 -19.12648 1.000 13.03608 ? 266 LEU A CD1  1 
ATOM   2211 C  CD2  . LEU A 1 280 ? 37.13917 51.37846 -20.72040 1.000 21.63316 ? 266 LEU A CD2  1 
ATOM   2212 N  N    . ASP A 1 281 ? 39.79950 47.34183 -21.88686 1.000 15.30983 ? 267 ASP A N    1 
ATOM   2213 C  CA   . ASP A 1 281 ? 39.22804 46.23326 -22.64066 1.000 14.33084 ? 267 ASP A CA   1 
ATOM   2214 C  C    . ASP A 1 281 ? 37.94103 46.69854 -23.32525 1.000 17.33567 ? 267 ASP A C    1 
ATOM   2215 O  O    . ASP A 1 281 ? 37.04512 47.22692 -22.64925 1.000 14.22206 ? 267 ASP A O    1 
ATOM   2216 C  CB   . ASP A 1 281 ? 38.92805 45.11197 -21.64499 1.000 13.75743 ? 267 ASP A CB   1 
ATOM   2217 C  CG   . ASP A 1 281 ? 38.42683 43.81797 -22.30920 1.000 17.84037 ? 267 ASP A CG   1 
ATOM   2218 O  OD1  . ASP A 1 281 ? 37.81716 43.86229 -23.39596 1.000 15.54151 ? 267 ASP A OD1  1 
ATOM   2219 O  OD2  . ASP A 1 281 ? 38.62380 42.74133 -21.71181 1.000 16.55084 ? 267 ASP A OD2  1 
ATOM   2220 N  N    . PRO A 1 282 ? 37.82478 46.55911 -24.64946 1.000 18.20366 ? 268 PRO A N    1 
ATOM   2221 C  CA   . PRO A 1 282 ? 36.64393 47.10466 -25.34242 1.000 18.48253 ? 268 PRO A CA   1 
ATOM   2222 C  C    . PRO A 1 282 ? 35.33378 46.45375 -24.93915 1.000 18.78048 ? 268 PRO A C    1 
ATOM   2223 O  O    . PRO A 1 282 ? 34.26887 47.02603 -25.20726 1.000 19.88468 ? 268 PRO A O    1 
ATOM   2224 C  CB   . PRO A 1 282 ? 36.96368 46.89186 -26.82966 1.000 16.45806 ? 268 PRO A CB   1 
ATOM   2225 C  CG   . PRO A 1 282 ? 37.97368 45.77410 -26.84509 1.000 21.54541 ? 268 PRO A CG   1 
ATOM   2226 C  CD   . PRO A 1 282 ? 38.78437 45.94326 -25.58170 1.000 21.70364 ? 268 PRO A CD   1 
ATOM   2227 N  N    . HIS A 1 283 ? 35.36488 45.28515 -24.29775 1.000 16.22385 ? 269 HIS A N    1 
ATOM   2228 C  CA   . HIS A 1 283 ? 34.12116 44.71169 -23.78928 1.000 16.67241 ? 269 HIS A CA   1 
ATOM   2229 C  C    . HIS A 1 283 ? 33.42349 45.64798 -22.80810 1.000 20.32863 ? 269 HIS A C    1 
ATOM   2230 O  O    . HIS A 1 283 ? 32.19292 45.59609 -22.66331 1.000 17.02025 ? 269 HIS A O    1 
ATOM   2231 C  CB   . HIS A 1 283 ? 34.38691 43.35934 -23.13670 1.000 19.42459 ? 269 HIS A CB   1 
ATOM   2232 C  CG   . HIS A 1 283 ? 33.17302 42.76046 -22.49686 1.000 23.35372 ? 269 HIS A CG   1 
ATOM   2233 N  ND1  . HIS A 1 283 ? 32.05956 42.38661 -23.21889 1.000 28.76745 ? 269 HIS A ND1  1 
ATOM   2234 C  CD2  . HIS A 1 283 ? 32.88470 42.50341 -21.19961 1.000 23.80059 ? 269 HIS A CD2  1 
ATOM   2235 C  CE1  . HIS A 1 283 ? 31.14266 41.91257 -22.39481 1.000 32.99640 ? 269 HIS A CE1  1 
ATOM   2236 N  NE2  . HIS A 1 283 ? 31.61813 41.97374 -21.16313 1.000 30.34216 ? 269 HIS A NE2  1 
ATOM   2237 N  N    . PHE A 1 284 ? 34.18655 46.51272 -22.13494 1.000 13.70834 ? 270 PHE A N    1 
ATOM   2238 C  CA   . PHE A 1 284 ? 33.60438 47.47287 -21.20028 1.000 15.53879 ? 270 PHE A CA   1 
ATOM   2239 C  C    . PHE A 1 284 ? 32.72846 48.51173 -21.89311 1.000 16.73104 ? 270 PHE A C    1 
ATOM   2240 O  O    . PHE A 1 284 ? 31.84320 49.08879 -21.25059 1.000 19.05800 ? 270 PHE A O    1 
ATOM   2241 C  CB   . PHE A 1 284 ? 34.70006 48.18348 -20.40179 1.000 16.71600 ? 270 PHE A CB   1 
ATOM   2242 C  CG   . PHE A 1 284 ? 35.27140 47.35827 -19.27024 1.000 14.45345 ? 270 PHE A CG   1 
ATOM   2243 C  CD1  . PHE A 1 284 ? 34.51144 47.07817 -18.14546 1.000 13.22908 ? 270 PHE A CD1  1 
ATOM   2244 C  CD2  . PHE A 1 284 ? 36.57076 46.87817 -19.33240 1.000 16.10932 ? 270 PHE A CD2  1 
ATOM   2245 C  CE1  . PHE A 1 284 ? 35.03083 46.32081 -17.10502 1.000 12.85790 ? 270 PHE A CE1  1 
ATOM   2246 C  CE2  . PHE A 1 284 ? 37.10680 46.11940 -18.29605 1.000 14.28923 ? 270 PHE A CE2  1 
ATOM   2247 C  CZ   . PHE A 1 284 ? 36.33354 45.84338 -17.17390 1.000 12.62293 ? 270 PHE A CZ   1 
ATOM   2248 N  N    . ASN A 1 285 ? 32.97639 48.79703 -23.17648 1.000 19.27516 ? 271 ASN A N    1 
ATOM   2249 C  CA   . ASN A 1 285 ? 32.24393 49.86957 -23.84613 1.000 19.40038 ? 271 ASN A CA   1 
ATOM   2250 C  C    . ASN A 1 285 ? 30.73935 49.64489 -23.79692 1.000 29.84972 ? 271 ASN A C    1 
ATOM   2251 O  O    . ASN A 1 285 ? 29.97096 50.60886 -23.70227 1.000 35.47053 ? 271 ASN A O    1 
ATOM   2252 C  CB   . ASN A 1 285 ? 32.68266 49.99720 -25.30692 1.000 25.04059 ? 271 ASN A CB   1 
ATOM   2253 C  CG   . ASN A 1 285 ? 34.17567 50.22106 -25.46112 1.000 18.37264 ? 271 ASN A CG   1 
ATOM   2254 O  OD1  . ASN A 1 285 ? 34.85705 50.65710 -24.53245 1.000 24.62606 ? 271 ASN A OD1  1 
ATOM   2255 N  ND2  . ASN A 1 285 ? 34.69204 49.92399 -26.65318 1.000 28.63560 ? 271 ASN A ND2  1 
ATOM   2256 N  N    . ASP A 1 286 ? 30.30412 48.38876 -23.85326 1.000 27.20879 ? 272 ASP A N    1 
ATOM   2257 C  CA   . ASP A 1 286 ? 28.89172 48.04557 -23.89896 1.000 27.02220 ? 272 ASP A CA   1 
ATOM   2258 C  C    . ASP A 1 286 ? 28.25813 47.86906 -22.52297 1.000 24.21191 ? 272 ASP A C    1 
ATOM   2259 O  O    . ASP A 1 286 ? 27.03962 47.67734 -22.44131 1.000 27.59463 ? 272 ASP A O    1 
ATOM   2260 C  CB   . ASP A 1 286 ? 28.70661 46.75007 -24.69564 1.000 36.89465 ? 272 ASP A CB   1 
ATOM   2261 C  CG   . ASP A 1 286 ? 29.32005 46.82567 -26.08143 1.000 62.74331 ? 272 ASP A CG   1 
ATOM   2262 O  OD1  . ASP A 1 286 ? 29.21419 47.89328 -26.72413 1.000 56.65531 ? 272 ASP A OD1  1 
ATOM   2263 O  OD2  . ASP A 1 286 ? 29.90950 45.81682 -26.52573 1.000 74.63541 ? 272 ASP A OD2  1 
ATOM   2264 N  N    . ILE A 1 287 ? 29.03145 47.91646 -21.44341 1.000 19.36419 ? 273 ILE A N    1 
ATOM   2265 C  CA   . ILE A 1 287 ? 28.47621 47.64920 -20.12315 1.000 18.61297 ? 273 ILE A CA   1 
ATOM   2266 C  C    . ILE A 1 287 ? 28.66885 48.78162 -19.12225 1.000 16.72126 ? 273 ILE A C    1 
ATOM   2267 O  O    . ILE A 1 287 ? 27.92040 48.83794 -18.13181 1.000 16.73003 ? 273 ILE A O    1 
ATOM   2268 C  CB   . ILE A 1 287 ? 28.96211 46.30355 -19.54679 1.000 18.90131 ? 273 ILE A CB   1 
ATOM   2269 C  CG1  . ILE A 1 287 ? 30.48368 46.25845 -19.45870 1.000 18.96010 ? 273 ILE A CG1  1 
ATOM   2270 C  CG2  . ILE A 1 287 ? 28.47002 45.15358 -20.42250 1.000 19.39896 ? 273 ILE A CG2  1 
ATOM   2271 C  CD1  . ILE A 1 287 ? 30.98485 45.00349 -18.80250 1.000 17.02676 ? 273 ILE A CD1  1 
ATOM   2272 N  N    . LEU A 1 288 ? 29.60634 49.70783 -19.34602 1.000 15.27747 ? 274 LEU A N    1 
ATOM   2273 C  CA   . LEU A 1 288 ? 29.87362 50.75480 -18.36260 1.000 17.18244 ? 274 LEU A CA   1 
ATOM   2274 C  C    . LEU A 1 288 ? 28.76668 51.80321 -18.29378 1.000 21.25258 ? 274 LEU A C    1 
ATOM   2275 O  O    . LEU A 1 288 ? 28.56255 52.40410 -17.23207 1.000 18.15441 ? 274 LEU A O    1 
ATOM   2276 C  CB   . LEU A 1 288 ? 31.20395 51.44303 -18.67145 1.000 17.54689 ? 274 LEU A CB   1 
ATOM   2277 C  CG   . LEU A 1 288 ? 32.48696 50.82133 -18.13393 1.000 18.28735 ? 274 LEU A CG   1 
ATOM   2278 C  CD1  . LEU A 1 288 ? 33.70276 51.51169 -18.75350 1.000 15.17927 ? 274 LEU A CD1  1 
ATOM   2279 C  CD2  . LEU A 1 288 ? 32.51722 50.90360 -16.60464 1.000 18.07151 ? 274 LEU A CD2  1 
ATOM   2280 N  N    . GLY A 1 289 ? 28.07151 52.06799 -19.40433 1.000 19.20762 ? 275 GLY A N    1 
ATOM   2281 C  CA   . GLY A 1 289 ? 27.06968 53.12462 -19.35719 1.000 17.10816 ? 275 GLY A CA   1 
ATOM   2282 C  C    . GLY A 1 289 ? 27.69883 54.49504 -19.10886 1.000 17.36243 ? 275 GLY A C    1 
ATOM   2283 O  O    . GLY A 1 289 ? 28.87591 54.73552 -19.37604 1.000 19.88852 ? 275 GLY A O    1 
ATOM   2284 N  N    . GLN A 1 290 ? 26.87558 55.40118 -18.58416 1.000 17.14312 ? 276 GLN A N    1 
ATOM   2285 C  CA   . GLN A 1 290 ? 27.28933 56.75386 -18.21860 1.000 16.08438 ? 276 GLN A CA   1 
ATOM   2286 C  C    . GLN A 1 290 ? 26.73478 57.02950 -16.83178 1.000 17.99078 ? 276 GLN A C    1 
ATOM   2287 O  O    . GLN A 1 290 ? 25.52101 56.94436 -16.62469 1.000 19.94382 ? 276 GLN A O    1 
ATOM   2288 C  CB   . GLN A 1 290 ? 26.73198 57.78240 -19.21099 1.000 20.39371 ? 276 GLN A CB   1 
ATOM   2289 C  CG   . GLN A 1 290 ? 27.27134 57.63412 -20.63073 1.000 21.76788 ? 276 GLN A CG   1 
ATOM   2290 C  CD   . GLN A 1 290 ? 26.64307 58.61154 -21.61693 1.000 44.39760 ? 276 GLN A CD   1 
ATOM   2291 O  OE1  . GLN A 1 290 ? 27.07847 59.75582 -21.73805 1.000 53.79082 ? 276 GLN A OE1  1 
ATOM   2292 N  NE2  . GLN A 1 290 ? 25.62026 58.15702 -22.33206 1.000 55.64317 ? 276 GLN A NE2  1 
ATOM   2293 N  N    . HIS A 1 291 ? 27.61138 57.33489 -15.87796 1.000 18.38295 ? 277 HIS A N    1 
ATOM   2294 C  CA   . HIS A 1 291 ? 27.18951 57.51278 -14.49163 1.000 18.07469 ? 277 HIS A CA   1 
ATOM   2295 C  C    . HIS A 1 291 ? 27.95165 58.67029 -13.86992 1.000 15.88208 ? 277 HIS A C    1 
ATOM   2296 O  O    . HIS A 1 291 ? 29.17421 58.74785 -13.99461 1.000 13.89656 ? 277 HIS A O    1 
ATOM   2297 C  CB   . HIS A 1 291 ? 27.46111 56.24566 -13.67139 1.000 17.62172 ? 277 HIS A CB   1 
ATOM   2298 C  CG   . HIS A 1 291 ? 26.84915 55.00781 -14.25119 1.000 14.87347 ? 277 HIS A CG   1 
ATOM   2299 N  ND1  . HIS A 1 291 ? 25.53643 54.65419 -14.02719 1.000 16.91405 ? 277 HIS A ND1  1 
ATOM   2300 C  CD2  . HIS A 1 291 ? 27.37182 54.03562 -15.03388 1.000 15.88243 ? 277 HIS A CD2  1 
ATOM   2301 C  CE1  . HIS A 1 291 ? 25.27186 53.52642 -14.65874 1.000 17.63534 ? 277 HIS A CE1  1 
ATOM   2302 N  NE2  . HIS A 1 291 ? 26.37049 53.12704 -15.27440 1.000 20.85367 ? 277 HIS A NE2  1 
ATOM   2303 N  N    A SER A 1 292 ? 27.23698 59.56751 -13.19950 0.470 18.16280 ? 278 SER A N    1 
ATOM   2304 N  N    B SER A 1 292 ? 27.22645 59.56165 -13.20158 0.530 18.17495 ? 278 SER A N    1 
ATOM   2305 C  CA   A SER A 1 292 ? 27.89618 60.65565 -12.49621 0.470 15.84570 ? 278 SER A CA   1 
ATOM   2306 C  CA   B SER A 1 292 ? 27.86039 60.63340 -12.45640 0.530 15.87444 ? 278 SER A CA   1 
ATOM   2307 C  C    A SER A 1 292 ? 28.42752 60.16208 -11.15397 0.470 15.53786 ? 278 SER A C    1 
ATOM   2308 C  C    B SER A 1 292 ? 28.51243 60.07812 -11.19352 0.530 15.53459 ? 278 SER A C    1 
ATOM   2309 O  O    A SER A 1 292 ? 27.92274 59.19050 -10.58335 0.470 15.76548 ? 278 SER A O    1 
ATOM   2310 O  O    B SER A 1 292 ? 28.17132 58.99556 -10.71004 0.530 16.13966 ? 278 SER A O    1 
ATOM   2311 C  CB   A SER A 1 292 ? 26.91953 61.81175 -12.26984 0.470 16.41819 ? 278 SER A CB   1 
ATOM   2312 C  CB   B SER A 1 292 ? 26.81437 61.66845 -12.04330 0.530 16.09436 ? 278 SER A CB   1 
ATOM   2313 O  OG   A SER A 1 292 ? 26.27414 62.18334 -13.47787 0.470 15.91335 ? 278 SER A OG   1 
ATOM   2314 O  OG   B SER A 1 292 ? 25.84219 61.08449 -11.18864 0.530 21.80243 ? 278 SER A OG   1 
ATOM   2315 N  N    . ARG A 1 293 ? 29.46671 60.83533 -10.65967 1.000 13.79704 ? 279 ARG A N    1 
ATOM   2316 C  CA   . ARG A 1 293 ? 30.00670 60.51837 -9.34001  1.000 11.73991 ? 279 ARG A CA   1 
ATOM   2317 C  C    . ARG A 1 293 ? 28.93682 60.76675 -8.28415  1.000 24.67389 ? 279 ARG A C    1 
ATOM   2318 O  O    . ARG A 1 293 ? 28.25980 61.79781 -8.30655  1.000 17.38972 ? 279 ARG A O    1 
ATOM   2319 C  CB   . ARG A 1 293 ? 31.23157 61.38154 -9.02780  1.000 14.25816 ? 279 ARG A CB   1 
ATOM   2320 C  CG   . ARG A 1 293 ? 31.77729 61.14081 -7.61191  1.000 20.24654 ? 279 ARG A CG   1 
ATOM   2321 C  CD   . ARG A 1 293 ? 32.55823 62.32495 -7.05729  1.000 42.95517 ? 279 ARG A CD   1 
ATOM   2322 N  NE   . ARG A 1 293 ? 32.95247 62.11725 -5.66491  1.000 32.16231 ? 279 ARG A NE   1 
ATOM   2323 C  CZ   . ARG A 1 293 ? 32.28630 62.56891 -4.60788  1.000 31.53504 ? 279 ARG A CZ   1 
ATOM   2324 N  NH1  . ARG A 1 293 ? 31.18078 63.28693 -4.73563  1.000 24.31144 ? 279 ARG A NH1  1 
ATOM   2325 N  NH2  . ARG A 1 293 ? 32.74260 62.29567 -3.38924  1.000 25.08063 ? 279 ARG A NH2  1 
ATOM   2326 N  N    . LYS A 1 294 ? 28.78223 59.81823 -7.36456  1.000 11.79105 ? 280 LYS A N    1 
ATOM   2327 C  CA   . LYS A 1 294 ? 27.75510 59.87065 -6.33649  1.000 9.77736  ? 280 LYS A CA   1 
ATOM   2328 C  C    . LYS A 1 294 ? 28.33528 60.39377 -5.02675  1.000 17.37244 ? 280 LYS A C    1 
ATOM   2329 O  O    . LYS A 1 294 ? 29.51027 60.18206 -4.71985  1.000 15.30798 ? 280 LYS A O    1 
ATOM   2330 C  CB   . LYS A 1 294 ? 27.16751 58.47913 -6.09344  1.000 9.91917  ? 280 LYS A CB   1 
ATOM   2331 C  CG   . LYS A 1 294 ? 26.58947 57.78983 -7.33191  1.000 16.47829 ? 280 LYS A CG   1 
ATOM   2332 C  CD   . LYS A 1 294 ? 25.54167 58.65854 -7.99515  1.000 18.40885 ? 280 LYS A CD   1 
ATOM   2333 C  CE   . LYS A 1 294 ? 24.77947 57.90177 -9.06198  1.000 13.88181 ? 280 LYS A CE   1 
ATOM   2334 N  NZ   . LYS A 1 294 ? 25.68319 57.43166 -10.13614 1.000 17.95799 ? 280 LYS A NZ   1 
ATOM   2335 N  N    . ARG A 1 295 ? 27.50242 61.09680 -4.26040  1.000 12.59586 ? 281 ARG A N    1 
ATOM   2336 C  CA   . ARG A 1 295 ? 27.89712 61.52461 -2.92732  1.000 15.52423 ? 281 ARG A CA   1 
ATOM   2337 C  C    . ARG A 1 295 ? 27.80535 60.34290 -1.97433  1.000 11.25166 ? 281 ARG A C    1 
ATOM   2338 O  O    . ARG A 1 295 ? 26.84493 59.56940 -2.01952  1.000 12.35186 ? 281 ARG A O    1 
ATOM   2339 C  CB   . ARG A 1 295 ? 26.98739 62.65974 -2.44950  1.000 11.96119 ? 281 ARG A CB   1 
ATOM   2340 C  CG   . ARG A 1 295 ? 27.07495 63.88879 -3.34114  1.000 18.27812 ? 281 ARG A CG   1 
ATOM   2341 C  CD   . ARG A 1 295 ? 26.19595 65.02788 -2.84199  1.000 24.73341 ? 281 ARG A CD   1 
ATOM   2342 N  NE   . ARG A 1 295 ? 26.52110 65.41444 -1.47368  1.000 36.36679 ? 281 ARG A NE   1 
ATOM   2343 C  CZ   . ARG A 1 295 ? 25.71182 65.25112 -0.43406  1.000 42.38890 ? 281 ARG A CZ   1 
ATOM   2344 N  NH1  . ARG A 1 295 ? 24.49624 64.74268 -0.57263  1.000 26.24429 ? 281 ARG A NH1  1 
ATOM   2345 N  NH2  . ARG A 1 295 ? 26.12922 65.61347 0.77484   1.000 43.54481 ? 281 ARG A NH2  1 
ATOM   2346 N  N    . TRP A 1 296 ? 28.81891 60.18947 -1.11699  1.000 12.89504 ? 282 TRP A N    1 
ATOM   2347 C  CA   . TRP A 1 296 ? 28.81850 59.05547 -0.19758  1.000 12.99355 ? 282 TRP A CA   1 
ATOM   2348 C  C    . TRP A 1 296 ? 27.64384 59.09199 0.76477   1.000 12.12910 ? 282 TRP A C    1 
ATOM   2349 O  O    . TRP A 1 296 ? 27.24734 58.03996 1.27782   1.000 11.72661 ? 282 TRP A O    1 
ATOM   2350 C  CB   . TRP A 1 296 ? 30.13212 58.97229 0.57103   1.000 14.05690 ? 282 TRP A CB   1 
ATOM   2351 C  CG   . TRP A 1 296 ? 31.28610 58.69245 -0.31653  1.000 8.17843  ? 282 TRP A CG   1 
ATOM   2352 C  CD1  . TRP A 1 296 ? 32.22834 59.58202 -0.73243  1.000 12.19953 ? 282 TRP A CD1  1 
ATOM   2353 C  CD2  . TRP A 1 296 ? 31.62033 57.43232 -0.92587  1.000 8.71200  ? 282 TRP A CD2  1 
ATOM   2354 N  NE1  . TRP A 1 296 ? 33.14097 58.95131 -1.54860  1.000 10.61470 ? 282 TRP A NE1  1 
ATOM   2355 C  CE2  . TRP A 1 296 ? 32.79189 57.63342 -1.67880  1.000 10.20252 ? 282 TRP A CE2  1 
ATOM   2356 C  CE3  . TRP A 1 296 ? 31.05316 56.14903 -0.88350  1.000 9.07944  ? 282 TRP A CE3  1 
ATOM   2357 C  CZ2  . TRP A 1 296 ? 33.40339 56.60700 -2.41501  1.000 8.69429  ? 282 TRP A CZ2  1 
ATOM   2358 C  CZ3  . TRP A 1 296 ? 31.66601 55.12431 -1.61087  1.000 11.04399 ? 282 TRP A CZ3  1 
ATOM   2359 C  CH2  . TRP A 1 296 ? 32.83149 55.36723 -2.36639  1.000 8.77365  ? 282 TRP A CH2  1 
ATOM   2360 N  N    . GLU A 1 297 ? 27.07203 60.27500 1.00682   1.000 13.32499 ? 283 GLU A N    1 
ATOM   2361 C  CA   . GLU A 1 297 ? 25.86796 60.39303 1.81994   1.000 13.14020 ? 283 GLU A CA   1 
ATOM   2362 C  C    . GLU A 1 297 ? 24.68752 59.61157 1.25167   1.000 13.37871 ? 283 GLU A C    1 
ATOM   2363 O  O    . GLU A 1 297 ? 23.76066 59.29235 2.00454   1.000 15.51512 ? 283 GLU A O    1 
ATOM   2364 C  CB   . GLU A 1 297 ? 25.48067 61.87124 1.96785   1.000 14.49262 ? 283 GLU A CB   1 
ATOM   2365 C  CG   . GLU A 1 297 ? 26.42712 62.69744 2.84942   1.000 18.02402 ? 283 GLU A CG   1 
ATOM   2366 C  CD   . GLU A 1 297 ? 27.67933 63.21737 2.13375   1.000 36.13563 ? 283 GLU A CD   1 
ATOM   2367 O  OE1  . GLU A 1 297 ? 27.93216 62.85044 0.96247   1.000 22.78849 ? 283 GLU A OE1  1 
ATOM   2368 O  OE2  . GLU A 1 297 ? 28.42364 64.01031 2.75868   1.000 26.60144 ? 283 GLU A OE2  1 
ATOM   2369 N  N    . ASN A 1 298 ? 24.69229 59.29723 -0.04940  1.000 11.13057 ? 284 ASN A N    1 
ATOM   2370 C  CA   . ASN A 1 298 ? 23.59581 58.53492 -0.64776  1.000 11.67368 ? 284 ASN A CA   1 
ATOM   2371 C  C    . ASN A 1 298 ? 23.44066 57.14384 -0.04197  1.000 12.89538 ? 284 ASN A C    1 
ATOM   2372 O  O    . ASN A 1 298 ? 22.37781 56.52542 -0.19668  1.000 13.87945 ? 284 ASN A O    1 
ATOM   2373 C  CB   . ASN A 1 298 ? 23.80300 58.37975 -2.15624  1.000 15.48831 ? 284 ASN A CB   1 
ATOM   2374 C  CG   . ASN A 1 298 ? 23.73105 59.69073 -2.89085  1.000 22.83623 ? 284 ASN A CG   1 
ATOM   2375 O  OD1  . ASN A 1 298 ? 23.49182 60.73794 -2.28705  1.000 22.06584 ? 284 ASN A OD1  1 
ATOM   2376 N  ND2  . ASN A 1 298 ? 23.95880 59.65004 -4.20455  1.000 19.93330 ? 284 ASN A ND2  1 
ATOM   2377 N  N    . PHE A 1 299 ? 24.46261 56.62990 0.63515   1.000 10.79055 ? 285 PHE A N    1 
ATOM   2378 C  CA   . PHE A 1 299 ? 24.38555 55.28827 1.20079   1.000 11.44712 ? 285 PHE A CA   1 
ATOM   2379 C  C    . PHE A 1 299 ? 23.87299 55.25971 2.63548   1.000 11.00601 ? 285 PHE A C    1 
ATOM   2380 O  O    . PHE A 1 299 ? 23.68681 54.16803 3.18160   1.000 10.00214 ? 285 PHE A O    1 
ATOM   2381 C  CB   . PHE A 1 299 ? 25.73698 54.57417 1.07957   1.000 12.36494 ? 285 PHE A CB   1 
ATOM   2382 C  CG   . PHE A 1 299 ? 26.18403 54.39978 -0.33699  1.000 6.63634  ? 285 PHE A CG   1 
ATOM   2383 C  CD1  . PHE A 1 299 ? 25.69076 53.36858 -1.11276  1.000 14.24607 ? 285 PHE A CD1  1 
ATOM   2384 C  CD2  . PHE A 1 299 ? 27.08210 55.29913 -0.90666  1.000 12.27916 ? 285 PHE A CD2  1 
ATOM   2385 C  CE1  . PHE A 1 299 ? 26.09167 53.21905 -2.42044  1.000 13.55629 ? 285 PHE A CE1  1 
ATOM   2386 C  CE2  . PHE A 1 299 ? 27.49060 55.15695 -2.22312  1.000 14.28712 ? 285 PHE A CE2  1 
ATOM   2387 C  CZ   . PHE A 1 299 ? 26.99407 54.11104 -2.97971  1.000 14.73870 ? 285 PHE A CZ   1 
ATOM   2388 N  N    . ILE A 1 300 ? 23.62483 56.42428 3.24051   1.000 11.52267 ? 286 ILE A N    1 
ATOM   2389 C  CA   . ILE A 1 300 ? 23.13446 56.50799 4.61092   1.000 11.29194 ? 286 ILE A CA   1 
ATOM   2390 C  C    . ILE A 1 300 ? 21.65155 56.18270 4.63469   1.000 15.68506 ? 286 ILE A C    1 
ATOM   2391 O  O    . ILE A 1 300 ? 20.88195 56.67137 3.80021   1.000 16.88211 ? 286 ILE A O    1 
ATOM   2392 C  CB   . ILE A 1 300 ? 23.38231 57.91606 5.17871   1.000 16.71703 ? 286 ILE A CB   1 
ATOM   2393 C  CG1  . ILE A 1 300 ? 24.88277 58.22689 5.22802   1.000 10.90837 ? 286 ILE A CG1  1 
ATOM   2394 C  CG2  . ILE A 1 300 ? 22.74255 58.05758 6.56275   1.000 14.34235 ? 286 ILE A CG2  1 
ATOM   2395 C  CD1  . ILE A 1 300 ? 25.19122 59.67166 5.53014   1.000 12.46222 ? 286 ILE A CD1  1 
ATOM   2396 N  N    . HIS A 1 301 ? 21.23403 55.37113 5.60391   1.000 7.02961  ? 287 HIS A N    1 
ATOM   2397 C  CA   . HIS A 1 301 ? 19.80974 55.20129 5.87520   1.000 12.17621 ? 287 HIS A CA   1 
ATOM   2398 C  C    . HIS A 1 301 ? 19.62741 54.92872 7.36438   1.000 12.74966 ? 287 HIS A C    1 
ATOM   2399 O  O    . HIS A 1 301 ? 20.59455 54.90611 8.13003   1.000 11.28870 ? 287 HIS A O    1 
ATOM   2400 C  CB   . HIS A 1 301 ? 19.15330 54.19344 4.92156   1.000 12.41203 ? 287 HIS A CB   1 
ATOM   2401 C  CG   . HIS A 1 301 ? 19.51937 52.76707 5.17870   1.000 18.95311 ? 287 HIS A CG   1 
ATOM   2402 N  ND1  . HIS A 1 301 ? 20.71034 52.21303 4.75999   1.000 20.07249 ? 287 HIS A ND1  1 
ATOM   2403 C  CD2  . HIS A 1 301 ? 18.82991 51.76588 5.77478   1.000 31.40549 ? 287 HIS A CD2  1 
ATOM   2404 C  CE1  . HIS A 1 301 ? 20.75106 50.94038 5.11223   1.000 13.83108 ? 287 HIS A CE1  1 
ATOM   2405 N  NE2  . HIS A 1 301 ? 19.62113 50.64378 5.72722   1.000 37.84475 ? 287 HIS A NE2  1 
ATOM   2406 N  N    . SER A 1 302 ? 18.37188 54.73627 7.78699   1.000 14.44999 ? 288 SER A N    1 
ATOM   2407 C  CA   . SER A 1 302 ? 18.10596 54.70039 9.22470   1.000 12.74153 ? 288 SER A CA   1 
ATOM   2408 C  C    . SER A 1 302 ? 18.85201 53.57334 9.93767   1.000 14.45078 ? 288 SER A C    1 
ATOM   2409 O  O    . SER A 1 302 ? 19.19054 53.71045 11.11778  1.000 19.06693 ? 288 SER A O    1 
ATOM   2410 C  CB   . SER A 1 302 ? 16.60710 54.63144 9.49832   1.000 13.37776 ? 288 SER A CB   1 
ATOM   2411 O  OG   . SER A 1 302 ? 16.05007 53.43435 8.98975   1.000 21.70878 ? 288 SER A OG   1 
ATOM   2412 N  N    . GLU A 1 303 ? 19.13021 52.46393 9.24591   1.000 12.76191 ? 289 GLU A N    1 
ATOM   2413 C  CA   . GLU A 1 303 ? 19.78832 51.32734 9.87766   1.000 17.83804 ? 289 GLU A CA   1 
ATOM   2414 C  C    . GLU A 1 303 ? 21.29622 51.51245 10.06088  1.000 15.66543 ? 289 GLU A C    1 
ATOM   2415 O  O    . GLU A 1 303 ? 21.88887 50.82008 10.89737  1.000 24.80184 ? 289 GLU A O    1 
ATOM   2416 C  CB   . GLU A 1 303 ? 19.49292 50.04281 9.09313   1.000 19.35332 ? 289 GLU A CB   1 
ATOM   2417 C  CG   . GLU A 1 303 ? 18.01873 49.64497 9.12522   1.000 30.59464 ? 289 GLU A CG   1 
ATOM   2418 C  CD   . GLU A 1 303 ? 17.64061 48.61979 8.06275   1.000 49.68583 ? 289 GLU A CD   1 
ATOM   2419 O  OE1  . GLU A 1 303 ? 18.36026 48.49797 7.04113   1.000 37.85399 ? 289 GLU A OE1  1 
ATOM   2420 O  OE2  . GLU A 1 303 ? 16.60755 47.93777 8.24668   1.000 28.79915 ? 289 GLU A OE2  1 
ATOM   2421 N  N    . ASN A 1 304 ? 21.93634 52.41673 9.31473   1.000 11.09964 ? 290 ASN A N    1 
ATOM   2422 C  CA   . ASN A 1 304 ? 23.36845 52.63291 9.46950   1.000 10.00686 ? 290 ASN A CA   1 
ATOM   2423 C  C    . ASN A 1 304 ? 23.74881 54.03879 9.91766   1.000 12.18491 ? 290 ASN A C    1 
ATOM   2424 O  O    . ASN A 1 304 ? 24.94345 54.31255 10.07328  1.000 10.79542 ? 290 ASN A O    1 
ATOM   2425 C  CB   . ASN A 1 304 ? 24.13467 52.23424 8.19239   1.000 8.03297  ? 290 ASN A CB   1 
ATOM   2426 C  CG   . ASN A 1 304 ? 23.77477 53.10216 6.99094   1.000 9.86200  ? 290 ASN A CG   1 
ATOM   2427 O  OD1  . ASN A 1 304 ? 23.37816 54.25983 7.14231   1.000 10.40207 ? 290 ASN A OD1  1 
ATOM   2428 N  ND2  . ASN A 1 304 ? 23.92060 52.54514 5.78567   1.000 9.37502  ? 290 ASN A ND2  1 
ATOM   2429 N  N    . ARG A 1 305 ? 22.77384 54.92518 10.15632  1.000 9.50571  ? 291 ARG A N    1 
ATOM   2430 C  CA   . ARG A 1 305 ? 23.06354 56.33878 10.40691  1.000 9.33471  ? 291 ARG A CA   1 
ATOM   2431 C  C    . ARG A 1 305 ? 24.00650 56.53038 11.59521  1.000 12.85387 ? 291 ARG A C    1 
ATOM   2432 O  O    . ARG A 1 305 ? 24.89193 57.39897 11.56277  1.000 12.99625 ? 291 ARG A O    1 
ATOM   2433 C  CB   . ARG A 1 305 ? 21.74738 57.09508 10.63430  1.000 11.89812 ? 291 ARG A CB   1 
ATOM   2434 C  CG   . ARG A 1 305 ? 21.92411 58.59431 10.83926  1.000 31.49977 ? 291 ARG A CG   1 
ATOM   2435 C  CD   . ARG A 1 305 ? 20.56837 59.27884 10.90485  1.000 46.35141 ? 291 ARG A CD   1 
ATOM   2436 N  NE   . ARG A 1 305 ? 19.64583 58.69991 9.93438   1.000 55.18654 ? 291 ARG A NE   1 
ATOM   2437 C  CZ   . ARG A 1 305 ? 19.53643 59.09048 8.67068   1.000 46.85366 ? 291 ARG A CZ   1 
ATOM   2438 N  NH1  . ARG A 1 305 ? 20.24449 60.10672 8.19511   1.000 39.60735 ? 291 ARG A NH1  1 
ATOM   2439 N  NH2  . ARG A 1 305 ? 18.70028 58.44125 7.86184   1.000 26.03137 ? 291 ARG A NH2  1 
ATOM   2440 N  N    . HIS A 1 306 ? 23.83575 55.72693 12.65266  1.000 13.61609 ? 292 HIS A N    1 
ATOM   2441 C  CA   . HIS A 1 306 ? 24.65265 55.86360 13.85554  1.000 12.54764 ? 292 HIS A CA   1 
ATOM   2442 C  C    . HIS A 1 306 ? 26.12227 55.52139 13.63353  1.000 17.56023 ? 292 HIS A C    1 
ATOM   2443 O  O    . HIS A 1 306 ? 26.95007 55.81188 14.51208  1.000 13.98541 ? 292 HIS A O    1 
ATOM   2444 C  CB   . HIS A 1 306 ? 24.08020 55.00306 14.99226  1.000 10.93181 ? 292 HIS A CB   1 
ATOM   2445 C  CG   . HIS A 1 306 ? 24.13678 53.52698 14.73520  1.000 10.70548 ? 292 HIS A CG   1 
ATOM   2446 N  ND1  . HIS A 1 306 ? 23.36389 52.90245 13.77988  1.000 16.56100 ? 292 HIS A ND1  1 
ATOM   2447 C  CD2  . HIS A 1 306 ? 24.86601 52.54748 15.32516  1.000 13.00585 ? 292 HIS A CD2  1 
ATOM   2448 C  CE1  . HIS A 1 306 ? 23.62394 51.60583 13.78095  1.000 17.78399 ? 292 HIS A CE1  1 
ATOM   2449 N  NE2  . HIS A 1 306 ? 24.52759 51.36345 14.71424  1.000 13.65101 ? 292 HIS A NE2  1 
ATOM   2450 N  N    . LEU A 1 307 ? 26.46200 54.89504 12.50799  1.000 11.54224 ? 293 LEU A N    1 
ATOM   2451 C  CA   . LEU A 1 307 ? 27.83306 54.52743 12.20642  1.000 9.85648  ? 293 LEU A CA   1 
ATOM   2452 C  C    . LEU A 1 307 ? 28.53067 55.51232 11.27899  1.000 13.76295 ? 293 LEU A C    1 
ATOM   2453 O  O    . LEU A 1 307 ? 29.75203 55.41389 11.09971  1.000 10.36875 ? 293 LEU A O    1 
ATOM   2454 C  CB   . LEU A 1 307 ? 27.86391 53.13578 11.57667  1.000 6.55570  ? 293 LEU A CB   1 
ATOM   2455 C  CG   . LEU A 1 307 ? 27.21458 52.02522 12.40039  1.000 9.24491  ? 293 LEU A CG   1 
ATOM   2456 C  CD1  . LEU A 1 307 ? 27.20273 50.73450 11.60357  1.000 11.72228 ? 293 LEU A CD1  1 
ATOM   2457 C  CD2  . LEU A 1 307 ? 27.97143 51.84605 13.70222  1.000 13.15457 ? 293 LEU A CD2  1 
ATOM   2458 N  N    . VAL A 1 308 ? 27.79752 56.44990 10.69151  1.000 13.40430 ? 294 VAL A N    1 
ATOM   2459 C  CA   . VAL A 1 308 ? 28.32364 57.34359 9.67341   1.000 11.44173 ? 294 VAL A CA   1 
ATOM   2460 C  C    . VAL A 1 308 ? 28.46918 58.73366 10.27288  1.000 12.77334 ? 294 VAL A C    1 
ATOM   2461 O  O    . VAL A 1 308 ? 27.61419 59.19243 11.03761  1.000 15.85052 ? 294 VAL A O    1 
ATOM   2462 C  CB   . VAL A 1 308 ? 27.43509 57.35382 8.41406   1.000 9.16208  ? 294 VAL A CB   1 
ATOM   2463 C  CG1  . VAL A 1 308 ? 28.05878 58.21750 7.32646   1.000 10.81545 ? 294 VAL A CG1  1 
ATOM   2464 C  CG2  . VAL A 1 308 ? 27.20880 55.93502 7.90441   1.000 9.78807  ? 294 VAL A CG2  1 
ATOM   2465 N  N    . SER A 1 309 ? 29.55769 59.39769 9.92427   1.000 8.88961  ? 295 SER A N    1 
ATOM   2466 C  CA   . SER A 1 309 ? 29.85664 60.73306 10.40785  1.000 10.58034 ? 295 SER A CA   1 
ATOM   2467 C  C    . SER A 1 309 ? 30.55570 61.47632 9.28585   1.000 11.95965 ? 295 SER A C    1 
ATOM   2468 O  O    . SER A 1 309 ? 31.02083 60.85542 8.32099   1.000 9.14199  ? 295 SER A O    1 
ATOM   2469 C  CB   . SER A 1 309 ? 30.77159 60.66475 11.63432  1.000 14.29977 ? 295 SER A CB   1 
ATOM   2470 O  OG   . SER A 1 309 ? 31.92400 59.90488 11.34136  1.000 12.41301 ? 295 SER A OG   1 
ATOM   2471 N  N    . PRO A 1 310 ? 30.63269 62.80414 9.36774   1.000 13.25667 ? 296 PRO A N    1 
ATOM   2472 C  CA   . PRO A 1 310 ? 31.45452 63.53890 8.39405   1.000 13.61575 ? 296 PRO A CA   1 
ATOM   2473 C  C    . PRO A 1 310 ? 32.87559 63.01145 8.30383   1.000 11.88729 ? 296 PRO A C    1 
ATOM   2474 O  O    . PRO A 1 310 ? 33.41700 62.88672 7.19785   1.000 12.63884 ? 296 PRO A O    1 
ATOM   2475 C  CB   . PRO A 1 310 ? 31.39299 64.98139 8.91730   1.000 14.43444 ? 296 PRO A CB   1 
ATOM   2476 C  CG   . PRO A 1 310 ? 30.06520 65.05095 9.61955   1.000 14.28352 ? 296 PRO A CG   1 
ATOM   2477 C  CD   . PRO A 1 310 ? 29.87629 63.71002 10.25669  1.000 13.78149 ? 296 PRO A CD   1 
ATOM   2478 N  N    . GLU A 1 311 ? 33.47493 62.66431 9.44776   1.000 11.27811 ? 297 GLU A N    1 
ATOM   2479 C  CA   . GLU A 1 311 ? 34.83781 62.14259 9.47481   1.000 10.37149 ? 297 GLU A CA   1 
ATOM   2480 C  C    . GLU A 1 311 ? 34.94634 60.81492 8.73157   1.000 8.21778  ? 297 GLU A C    1 
ATOM   2481 O  O    . GLU A 1 311 ? 35.89555 60.60198 7.96623   1.000 9.63491  ? 297 GLU A O    1 
ATOM   2482 C  CB   . GLU A 1 311 ? 35.27108 61.94651 10.92545  1.000 15.27141 ? 297 GLU A CB   1 
ATOM   2483 C  CG   . GLU A 1 311 ? 35.42396 63.21775 11.69907  1.000 34.35673 ? 297 GLU A CG   1 
ATOM   2484 C  CD   . GLU A 1 311 ? 34.10071 63.84530 12.11525  1.000 40.73575 ? 297 GLU A CD   1 
ATOM   2485 O  OE1  . GLU A 1 311 ? 33.06606 63.13547 12.13754  1.000 14.47924 ? 297 GLU A OE1  1 
ATOM   2486 O  OE2  . GLU A 1 311 ? 34.10307 65.05959 12.41782  1.000 50.85370 ? 297 GLU A OE2  1 
ATOM   2487 N  N    . ALA A 1 312 ? 33.98453 59.90709 8.94574   1.000 8.12989  ? 298 ALA A N    1 
ATOM   2488 C  CA   . ALA A 1 312 ? 34.01014 58.61553 8.26492   1.000 5.99185  ? 298 ALA A CA   1 
ATOM   2489 C  C    . ALA A 1 312 ? 33.91811 58.78714 6.75782   1.000 5.40234  ? 298 ALA A C    1 
ATOM   2490 O  O    . ALA A 1 312 ? 34.65129 58.13252 6.00773   1.000 9.12374  ? 298 ALA A O    1 
ATOM   2491 C  CB   . ALA A 1 312 ? 32.85458 57.74331 8.75845   1.000 5.25114  ? 298 ALA A CB   1 
ATOM   2492 N  N    . LEU A 1 313 ? 33.02836 59.67429 6.29627   1.000 8.36025  ? 299 LEU A N    1 
ATOM   2493 C  CA   . LEU A 1 313 ? 32.81863 59.85729 4.86199   1.000 8.74758  ? 299 LEU A CA   1 
ATOM   2494 C  C    . LEU A 1 313 ? 34.01482 60.52983 4.21115   1.000 8.32888  ? 299 LEU A C    1 
ATOM   2495 O  O    . LEU A 1 313 ? 34.38167 60.19335 3.07670   1.000 9.33041  ? 299 LEU A O    1 
ATOM   2496 C  CB   . LEU A 1 313 ? 31.55796 60.68444 4.62552   1.000 9.85866  ? 299 LEU A CB   1 
ATOM   2497 C  CG   . LEU A 1 313 ? 30.22706 60.01735 4.98337   1.000 12.55104 ? 299 LEU A CG   1 
ATOM   2498 C  CD1  . LEU A 1 313 ? 29.08755 60.90908 4.53560   1.000 15.22747 ? 299 LEU A CD1  1 
ATOM   2499 C  CD2  . LEU A 1 313 ? 30.11710 58.62446 4.34665   1.000 14.87063 ? 299 LEU A CD2  1 
ATOM   2500 N  N    . ASP A 1 314 ? 34.63704 61.47872 4.91330   1.000 10.43900 ? 300 ASP A N    1 
ATOM   2501 C  CA   . ASP A 1 314 ? 35.85082 62.11352 4.40557   1.000 10.44459 ? 300 ASP A CA   1 
ATOM   2502 C  C    . ASP A 1 314 ? 36.97647 61.10536 4.21873   1.000 7.82723  ? 300 ASP A C    1 
ATOM   2503 O  O    . ASP A 1 314 ? 37.65639 61.10721 3.18749   1.000 8.83973  ? 300 ASP A O    1 
ATOM   2504 C  CB   . ASP A 1 314 ? 36.30561 63.22655 5.34559   1.000 8.60736  ? 300 ASP A CB   1 
ATOM   2505 C  CG   . ASP A 1 314 ? 37.48592 63.99139 4.78528   1.000 17.04813 ? 300 ASP A CG   1 
ATOM   2506 O  OD1  . ASP A 1 314 ? 37.30691 64.67801 3.75068   1.000 15.16156 ? 300 ASP A OD1  1 
ATOM   2507 O  OD2  . ASP A 1 314 ? 38.59744 63.88804 5.35014   1.000 13.48741 ? 300 ASP A OD2  1 
ATOM   2508 N  N    . LEU A 1 315 ? 37.22223 60.27140 5.23054   1.000 6.67709  ? 301 LEU A N    1 
ATOM   2509 C  CA   . LEU A 1 315 ? 38.22936 59.22257 5.10284   1.000 6.21495  ? 301 LEU A CA   1 
ATOM   2510 C  C    . LEU A 1 315 ? 37.89478 58.27834 3.95156   1.000 7.69520  ? 301 LEU A C    1 
ATOM   2511 O  O    . LEU A 1 315 ? 38.74759 57.98907 3.10143   1.000 8.77917  ? 301 LEU A O    1 
ATOM   2512 C  CB   . LEU A 1 315 ? 38.35108 58.44983 6.42257   1.000 7.03265  ? 301 LEU A CB   1 
ATOM   2513 C  CG   . LEU A 1 315 ? 39.27360 57.21317 6.42431   1.000 7.80840  ? 301 LEU A CG   1 
ATOM   2514 C  CD1  . LEU A 1 315 ? 40.69343 57.63161 6.08502   1.000 6.67727  ? 301 LEU A CD1  1 
ATOM   2515 C  CD2  . LEU A 1 315 ? 39.25499 56.44316 7.74015   1.000 9.68282  ? 301 LEU A CD2  1 
ATOM   2516 N  N    . LEU A 1 316 ? 36.65466 57.77350 3.91471   1.000 6.85042  ? 302 LEU A N    1 
ATOM   2517 C  CA   . LEU A 1 316 ? 36.27990 56.82610 2.86586   1.000 6.88425  ? 302 LEU A CA   1 
ATOM   2518 C  C    . LEU A 1 316 ? 36.50701 57.41829 1.48053   1.000 7.96145  ? 302 LEU A C    1 
ATOM   2519 O  O    . LEU A 1 316 ? 36.98999 56.73145 0.56782   1.000 8.61440  ? 302 LEU A O    1 
ATOM   2520 C  CB   . LEU A 1 316 ? 34.81477 56.41553 3.04375   1.000 5.62296  ? 302 LEU A CB   1 
ATOM   2521 C  CG   . LEU A 1 316 ? 34.35313 55.28843 2.13031   1.000 8.04167  ? 302 LEU A CG   1 
ATOM   2522 C  CD1  . LEU A 1 316 ? 35.16030 54.00976 2.38297   1.000 9.28710  ? 302 LEU A CD1  1 
ATOM   2523 C  CD2  . LEU A 1 316 ? 32.86057 55.03114 2.31409   1.000 4.77230  ? 302 LEU A CD2  1 
ATOM   2524 N  N    . ASP A 1 317 ? 36.16171 58.69519 1.30456   1.000 7.35460  ? 303 ASP A N    1 
ATOM   2525 C  CA   . ASP A 1 317 ? 36.32765 59.34489 0.00889   1.000 9.28994  ? 303 ASP A CA   1 
ATOM   2526 C  C    . ASP A 1 317 ? 37.79329 59.42711 -0.40199  1.000 7.60216  ? 303 ASP A C    1 
ATOM   2527 O  O    . ASP A 1 317 ? 38.09849 59.44242 -1.60109  1.000 10.74971 ? 303 ASP A O    1 
ATOM   2528 C  CB   . ASP A 1 317 ? 35.71612 60.74112 0.07326   1.000 8.58991  ? 303 ASP A CB   1 
ATOM   2529 C  CG   . ASP A 1 317 ? 35.81673 61.48514 -1.22873  1.000 19.11257 ? 303 ASP A CG   1 
ATOM   2530 O  OD1  . ASP A 1 317 ? 35.23272 61.02695 -2.22305  1.000 10.60921 ? 303 ASP A OD1  1 
ATOM   2531 O  OD2  . ASP A 1 317 ? 36.47475 62.54091 -1.25049  1.000 23.88990 ? 303 ASP A OD2  1 
ATOM   2532 N  N    . LYS A 1 318 ? 38.70456 59.48246 0.57256   1.000 5.89619  ? 304 LYS A N    1 
ATOM   2533 C  CA   . LYS A 1 318 ? 40.13657 59.55896 0.32316   1.000 7.13333  ? 304 LYS A CA   1 
ATOM   2534 C  C    . LYS A 1 318 ? 40.78548 58.19180 0.13143   1.000 6.56509  ? 304 LYS A C    1 
ATOM   2535 O  O    . LYS A 1 318 ? 41.96082 58.12026 -0.24347  1.000 11.04317 ? 304 LYS A O    1 
ATOM   2536 C  CB   . LYS A 1 318 ? 40.80989 60.33630 1.46180   1.000 8.08034  ? 304 LYS A CB   1 
ATOM   2537 C  CG   . LYS A 1 318 ? 40.45921 61.83272 1.47363   1.000 9.90409  ? 304 LYS A CG   1 
ATOM   2538 C  CD   . LYS A 1 318 ? 41.02362 62.54364 2.70555   1.000 13.87489 ? 304 LYS A CD   1 
ATOM   2539 C  CE   . LYS A 1 318 ? 40.73417 64.04172 2.65595   1.000 10.07619 ? 304 LYS A CE   1 
ATOM   2540 N  NZ   . LYS A 1 318 ? 40.84197 64.65519 4.00908   1.000 16.76488 ? 304 LYS A NZ   1 
ATOM   2541 N  N    . LEU A 1 319 ? 40.04775 57.10890 0.35177   1.000 7.90862  ? 305 LEU A N    1 
ATOM   2542 C  CA   . LEU A 1 319 ? 40.52495 55.74931 0.12639   1.000 8.01966  ? 305 LEU A CA   1 
ATOM   2543 C  C    . LEU A 1 319 ? 39.97550 55.15201 -1.16321  1.000 8.73094  ? 305 LEU A C    1 
ATOM   2544 O  O    . LEU A 1 319 ? 40.73771 54.61785 -1.97407  1.000 8.75582  ? 305 LEU A O    1 
ATOM   2545 C  CB   . LEU A 1 319 ? 40.10526 54.85997 1.30832   1.000 8.92325  ? 305 LEU A CB   1 
ATOM   2546 C  CG   . LEU A 1 319 ? 40.72479 55.17256 2.67426   1.000 11.46931 ? 305 LEU A CG   1 
ATOM   2547 C  CD1  . LEU A 1 319 ? 40.10082 54.32120 3.76616   1.000 7.58861  ? 305 LEU A CD1  1 
ATOM   2548 C  CD2  . LEU A 1 319 ? 42.23535 54.96396 2.63768   1.000 10.98807 ? 305 LEU A CD2  1 
ATOM   2549 N  N    . LEU A 1 320 ? 38.65718 55.23028 -1.35551  1.000 8.15911  ? 306 LEU A N    1 
ATOM   2550 C  CA   . LEU A 1 320 ? 37.98793 54.69030 -2.54109  1.000 4.97513  ? 306 LEU A CA   1 
ATOM   2551 C  C    . LEU A 1 320 ? 38.02836 55.72941 -3.66354  1.000 9.86907  ? 306 LEU A C    1 
ATOM   2552 O  O    . LEU A 1 320 ? 37.04081 56.39657 -3.98820  1.000 12.13454 ? 306 LEU A O    1 
ATOM   2553 C  CB   . LEU A 1 320 ? 36.56408 54.26500 -2.19777  1.000 9.24068  ? 306 LEU A CB   1 
ATOM   2554 C  CG   . LEU A 1 320 ? 36.47911 53.09215 -1.22565  1.000 6.71038  ? 306 LEU A CG   1 
ATOM   2555 C  CD1  . LEU A 1 320 ? 35.03139 52.62315 -1.06439  1.000 10.42048 ? 306 LEU A CD1  1 
ATOM   2556 C  CD2  . LEU A 1 320 ? 37.35344 51.95210 -1.70474  1.000 6.79658  ? 306 LEU A CD2  1 
ATOM   2557 N  N    . ARG A 1 321 ? 39.22069 55.85762 -4.24225  1.000 7.02066  ? 307 ARG A N    1 
ATOM   2558 C  CA   . ARG A 1 321 ? 39.52054 56.71673 -5.37695  1.000 8.54355  ? 307 ARG A CA   1 
ATOM   2559 C  C    . ARG A 1 321 ? 40.14913 55.87370 -6.47418  1.000 7.01929  ? 307 ARG A C    1 
ATOM   2560 O  O    . ARG A 1 321 ? 40.92616 54.96416 -6.18530  1.000 10.25636 ? 307 ARG A O    1 
ATOM   2561 C  CB   . ARG A 1 321 ? 40.58434 57.74353 -4.98599  1.000 12.57289 ? 307 ARG A CB   1 
ATOM   2562 C  CG   . ARG A 1 321 ? 40.16457 58.74298 -3.96605  1.000 21.43517 ? 307 ARG A CG   1 
ATOM   2563 C  CD   . ARG A 1 321 ? 41.24892 59.77488 -3.81099  1.000 19.58907 ? 307 ARG A CD   1 
ATOM   2564 N  NE   . ARG A 1 321 ? 40.75972 60.95550 -3.11129  1.000 37.80365 ? 307 ARG A NE   1 
ATOM   2565 C  CZ   . ARG A 1 321 ? 41.46174 62.06885 -2.96228  1.000 38.81980 ? 307 ARG A CZ   1 
ATOM   2566 N  NH1  . ARG A 1 321 ? 42.67060 62.19605 -3.48821  1.000 30.71282 ? 307 ARG A NH1  1 
ATOM   2567 N  NH2  . ARG A 1 321 ? 40.94091 63.07654 -2.26578  1.000 42.17642 ? 307 ARG A NH2  1 
ATOM   2568 N  N    . TYR A 1 322 ? 39.84818 56.19800 -7.73864  1.000 6.95845  ? 308 TYR A N    1 
ATOM   2569 C  CA   . TYR A 1 322 ? 40.47115 55.46903 -8.84039  1.000 6.23612  ? 308 TYR A CA   1 
ATOM   2570 C  C    . TYR A 1 322 ? 41.98818 55.61746 -8.80456  1.000 10.33969 ? 308 TYR A C    1 
ATOM   2571 O  O    . TYR A 1 322 ? 42.72789 54.63941 -8.98767  1.000 10.10332 ? 308 TYR A O    1 
ATOM   2572 C  CB   . TYR A 1 322 ? 39.98976 56.00543 -10.18991 1.000 7.01392  ? 308 TYR A CB   1 
ATOM   2573 C  CG   . TYR A 1 322 ? 38.57224 55.68494 -10.57930 1.000 9.07528  ? 308 TYR A CG   1 
ATOM   2574 C  CD1  . TYR A 1 322 ? 38.14241 54.36714 -10.74043 1.000 7.93773  ? 308 TYR A CD1  1 
ATOM   2575 C  CD2  . TYR A 1 322 ? 37.66901 56.70823 -10.84219 1.000 6.98289  ? 308 TYR A CD2  1 
ATOM   2576 C  CE1  . TYR A 1 322 ? 36.83121 54.08279 -11.11816 1.000 10.34594 ? 308 TYR A CE1  1 
ATOM   2577 C  CE2  . TYR A 1 322 ? 36.37075 56.43481 -11.21210 1.000 7.62990  ? 308 TYR A CE2  1 
ATOM   2578 C  CZ   . TYR A 1 322 ? 35.95015 55.12785 -11.35452 1.000 9.63701  ? 308 TYR A CZ   1 
ATOM   2579 O  OH   . TYR A 1 322 ? 34.65256 54.85295 -11.72663 1.000 11.17645 ? 308 TYR A OH   1 
ATOM   2580 N  N    . ASP A 1 323 ? 42.46624 56.85218 -8.64521  1.000 9.11741  ? 309 ASP A N    1 
ATOM   2581 C  CA   . ASP A 1 323 ? 43.88981 57.15770 -8.76008  1.000 6.58897  ? 309 ASP A CA   1 
ATOM   2582 C  C    . ASP A 1 323 ? 44.62919 56.58550 -7.55803  1.000 5.00195  ? 309 ASP A C    1 
ATOM   2583 O  O    . ASP A 1 323 ? 44.62606 57.17480 -6.47031  1.000 7.71117  ? 309 ASP A O    1 
ATOM   2584 C  CB   . ASP A 1 323 ? 44.10161 58.66000 -8.87595  1.000 11.93532 ? 309 ASP A CB   1 
ATOM   2585 C  CG   . ASP A 1 323 ? 45.52304 59.01985 -9.27252  1.000 13.06537 ? 309 ASP A CG   1 
ATOM   2586 O  OD1  . ASP A 1 323 ? 46.45321 58.20810 -9.03829  1.000 15.32033 ? 309 ASP A OD1  1 
ATOM   2587 O  OD2  . ASP A 1 323 ? 45.70756 60.11602 -9.83593  1.000 14.26506 ? 309 ASP A OD2  1 
ATOM   2588 N  N    . HIS A 1 324 ? 45.27884 55.43115 -7.76876  1.000 9.22568  ? 310 HIS A N    1 
ATOM   2589 C  CA   . HIS A 1 324 ? 45.93834 54.71350 -6.68064  1.000 7.75123  ? 310 HIS A CA   1 
ATOM   2590 C  C    . HIS A 1 324 ? 46.99687 55.57301 -6.01090  1.000 9.72922  ? 310 HIS A C    1 
ATOM   2591 O  O    . HIS A 1 324 ? 47.20035 55.47305 -4.79375  1.000 10.45014 ? 310 HIS A O    1 
ATOM   2592 C  CB   . HIS A 1 324 ? 46.55931 53.41309 -7.20776  1.000 9.26001  ? 310 HIS A CB   1 
ATOM   2593 C  CG   . HIS A 1 324 ? 47.47884 53.61394 -8.37704  1.000 13.20663 ? 310 HIS A CG   1 
ATOM   2594 N  ND1  . HIS A 1 324 ? 47.02557 53.68793 -9.67506  1.000 16.26505 ? 310 HIS A ND1  1 
ATOM   2595 C  CD2  . HIS A 1 324 ? 48.82240 53.78495 -8.43873  1.000 13.54077 ? 310 HIS A CD2  1 
ATOM   2596 C  CE1  . HIS A 1 324 ? 48.04803 53.88809 -10.48722 1.000 13.65430 ? 310 HIS A CE1  1 
ATOM   2597 N  NE2  . HIS A 1 324 ? 49.15026 53.94857 -9.76119  1.000 15.22112 ? 310 HIS A NE2  1 
ATOM   2598 N  N    . GLN A 1 325 ? 47.64835 56.44633 -6.78092  1.000 9.14298  ? 311 GLN A N    1 
ATOM   2599 C  CA   . GLN A 1 325 ? 48.68188 57.32882 -6.25404  1.000 13.72956 ? 311 GLN A CA   1 
ATOM   2600 C  C    . GLN A 1 325 ? 48.12253 58.41305 -5.32840  1.000 11.53196 ? 311 GLN A C    1 
ATOM   2601 O  O    . GLN A 1 325 ? 48.85491 58.92002 -4.47270  1.000 16.44415 ? 311 GLN A O    1 
ATOM   2602 C  CB   . GLN A 1 325 ? 49.46473 57.93457 -7.42364  1.000 13.98262 ? 311 GLN A CB   1 
ATOM   2603 C  CG   . GLN A 1 325 ? 50.86367 58.39131 -7.06405  1.000 27.01205 ? 311 GLN A CG   1 
ATOM   2604 C  CD   . GLN A 1 325 ? 51.01621 59.89877 -7.11596  1.000 35.96596 ? 311 GLN A CD   1 
ATOM   2605 O  OE1  . GLN A 1 325 ? 50.05459 60.62524 -7.37024  1.000 39.16703 ? 311 GLN A OE1  1 
ATOM   2606 N  NE2  . GLN A 1 325 ? 52.23378 60.37805 -6.87641  1.000 26.33870 ? 311 GLN A NE2  1 
ATOM   2607 N  N    . GLN A 1 326 ? 46.84473 58.76313 -5.45776  1.000 7.97060  ? 312 GLN A N    1 
ATOM   2608 C  CA   . GLN A 1 326 ? 46.22879 59.78297 -4.61845  1.000 13.50717 ? 312 GLN A CA   1 
ATOM   2609 C  C    . GLN A 1 326 ? 45.54059 59.22534 -3.37649  1.000 12.00475 ? 312 GLN A C    1 
ATOM   2610 O  O    . GLN A 1 326 ? 45.17120 60.00855 -2.49865  1.000 10.74965 ? 312 GLN A O    1 
ATOM   2611 C  CB   . GLN A 1 326 ? 45.23430 60.61843 -5.44013  1.000 13.57334 ? 312 GLN A CB   1 
ATOM   2612 C  CG   . GLN A 1 326 ? 45.91670 61.51858 -6.47197  1.000 23.74475 ? 312 GLN A CG   1 
ATOM   2613 C  CD   . GLN A 1 326 ? 46.80721 62.57407 -5.81388  1.000 29.63293 ? 312 GLN A CD   1 
ATOM   2614 O  OE1  . GLN A 1 326 ? 46.31265 63.57497 -5.28605  1.000 39.05938 ? 312 GLN A OE1  1 
ATOM   2615 N  NE2  . GLN A 1 326 ? 48.12228 62.34800 -5.83415  1.000 32.08836 ? 312 GLN A NE2  1 
ATOM   2616 N  N    . ARG A 1 327 ? 45.33990 57.91132 -3.28865  1.000 6.65323  ? 313 ARG A N    1 
ATOM   2617 C  CA   . ARG A 1 327 ? 44.78673 57.31568 -2.07920  1.000 5.84763  ? 313 ARG A CA   1 
ATOM   2618 C  C    . ARG A 1 327 ? 45.70178 57.59429 -0.89712  1.000 6.62074  ? 313 ARG A C    1 
ATOM   2619 O  O    . ARG A 1 327 ? 46.92229 57.71201 -1.04447  1.000 6.71096  ? 313 ARG A O    1 
ATOM   2620 C  CB   . ARG A 1 327 ? 44.66236 55.80274 -2.24660  1.000 7.97379  ? 313 ARG A CB   1 
ATOM   2621 C  CG   . ARG A 1 327 ? 43.66174 55.36939 -3.30491  1.000 9.64397  ? 313 ARG A CG   1 
ATOM   2622 C  CD   . ARG A 1 327 ? 43.63100 53.84361 -3.48993  1.000 6.67721  ? 313 ARG A CD   1 
ATOM   2623 N  NE   . ARG A 1 327 ? 43.06021 53.52600 -4.79312  1.000 6.72144  ? 313 ARG A NE   1 
ATOM   2624 C  CZ   . ARG A 1 327 ? 43.43487 52.49954 -5.54320  1.000 9.74223  ? 313 ARG A CZ   1 
ATOM   2625 N  NH1  . ARG A 1 327 ? 44.30645 51.60891 -5.10495  1.000 7.42163  ? 313 ARG A NH1  1 
ATOM   2626 N  NH2  . ARG A 1 327 ? 42.96123 52.39274 -6.78345  1.000 8.91182  ? 313 ARG A NH2  1 
ATOM   2627 N  N    . LEU A 1 328 ? 45.10096 57.73618 0.28433   1.000 8.95032  ? 314 LEU A N    1 
ATOM   2628 C  CA   . LEU A 1 328 ? 45.90303 57.87776 1.49205   1.000 10.42138 ? 314 LEU A CA   1 
ATOM   2629 C  C    . LEU A 1 328 ? 46.77697 56.64642 1.67149   1.000 5.48214  ? 314 LEU A C    1 
ATOM   2630 O  O    . LEU A 1 328 ? 46.36823 55.52821 1.35718   1.000 7.59777  ? 314 LEU A O    1 
ATOM   2631 C  CB   . LEU A 1 328 ? 44.99793 58.00611 2.71478   1.000 8.08175  ? 314 LEU A CB   1 
ATOM   2632 C  CG   . LEU A 1 328 ? 44.02930 59.18840 2.81025   1.000 8.24486  ? 314 LEU A CG   1 
ATOM   2633 C  CD1  . LEU A 1 328 ? 43.40954 59.23691 4.20113   1.000 7.79006  ? 314 LEU A CD1  1 
ATOM   2634 C  CD2  . LEU A 1 328 ? 44.72189 60.49188 2.48573   1.000 15.50483 ? 314 LEU A CD2  1 
ATOM   2635 N  N    . THR A 1 329 ? 48.00175 56.86270 2.12848   1.000 6.07182  ? 315 THR A N    1 
ATOM   2636 C  CA   . THR A 1 329 ? 48.82172 55.77871 2.64037   1.000 8.32993  ? 315 THR A CA   1 
ATOM   2637 C  C    . THR A 1 329 ? 48.25321 55.29429 3.97533   1.000 9.96257  ? 315 THR A C    1 
ATOM   2638 O  O    . THR A 1 329 ? 47.41998 55.95648 4.60122   1.000 7.35780  ? 315 THR A O    1 
ATOM   2639 C  CB   . THR A 1 329 ? 50.26013 56.27330 2.85207   1.000 6.70748  ? 315 THR A CB   1 
ATOM   2640 O  OG1  . THR A 1 329 ? 50.28731 57.22597 3.92738   1.000 8.60319  ? 315 THR A OG1  1 
ATOM   2641 C  CG2  . THR A 1 329 ? 50.79708 56.94468 1.58294   1.000 7.90719  ? 315 THR A CG2  1 
ATOM   2642 N  N    . ALA A 1 330 ? 48.70171 54.11321 4.41276   1.000 5.36122  ? 316 ALA A N    1 
ATOM   2643 C  CA   . ALA A 1 330 ? 48.26096 53.60964 5.71348   1.000 7.94235  ? 316 ALA A CA   1 
ATOM   2644 C  C    . ALA A 1 330 ? 48.60008 54.58727 6.84048   1.000 7.31570  ? 316 ALA A C    1 
ATOM   2645 O  O    . ALA A 1 330 ? 47.77953 54.81951 7.73992   1.000 8.23719  ? 316 ALA A O    1 
ATOM   2646 C  CB   . ALA A 1 330 ? 48.85320 52.22076 5.97620   1.000 4.70215  ? 316 ALA A CB   1 
ATOM   2647 N  N    . LYS A 1 331 ? 49.80283 55.17236 6.80883   1.000 6.48310  ? 317 LYS A N    1 
ATOM   2648 C  CA   . LYS A 1 331 ? 50.19523 56.14799 7.83060   1.000 6.81470  ? 317 LYS A CA   1 
ATOM   2649 C  C    . LYS A 1 331 ? 49.29471 57.38078 7.79651   1.000 9.00723  ? 317 LYS A C    1 
ATOM   2650 O  O    . LYS A 1 331 ? 48.82544 57.84976 8.84246   1.000 7.12031  ? 317 LYS A O    1 
ATOM   2651 C  CB   . LYS A 1 331 ? 51.65656 56.54686 7.62028   1.000 8.01891  ? 317 LYS A CB   1 
ATOM   2652 C  CG   . LYS A 1 331 ? 52.22064 57.51199 8.66170   1.000 10.50901 ? 317 LYS A CG   1 
ATOM   2653 C  CD   . LYS A 1 331 ? 53.74642 57.66618 8.48582   1.000 16.22053 ? 317 LYS A CD   1 
ATOM   2654 C  CE   . LYS A 1 331 ? 54.37464 58.51715 9.60038   1.000 18.19491 ? 317 LYS A CE   1 
ATOM   2655 N  NZ   . LYS A 1 331 ? 53.81116 59.90022 9.58598   1.000 41.73804 ? 317 LYS A NZ   1 
ATOM   2656 N  N    . GLU A 1 332 ? 49.04424 57.91799 6.59521   1.000 8.12298  ? 318 GLU A N    1 
ATOM   2657 C  CA   . GLU A 1 332 ? 48.16612 59.07882 6.44544   1.000 6.68204  ? 318 GLU A CA   1 
ATOM   2658 C  C    . GLU A 1 332 ? 46.75475 58.76340 6.91047   1.000 8.38280  ? 318 GLU A C    1 
ATOM   2659 O  O    . GLU A 1 332 ? 46.09205 59.61077 7.52318   1.000 8.08201  ? 318 GLU A O    1 
ATOM   2660 C  CB   . GLU A 1 332 ? 48.12589 59.52832 4.97737   1.000 8.30757  ? 318 GLU A CB   1 
ATOM   2661 C  CG   . GLU A 1 332 ? 49.36801 60.26421 4.50416   1.000 8.13723  ? 318 GLU A CG   1 
ATOM   2662 C  CD   . GLU A 1 332 ? 49.42110 60.42382 2.99130   1.000 10.59276 ? 318 GLU A CD   1 
ATOM   2663 O  OE1  . GLU A 1 332 ? 48.58963 59.83452 2.29446   1.000 8.81747  ? 318 GLU A OE1  1 
ATOM   2664 O  OE2  . GLU A 1 332 ? 50.30189 61.13961 2.49707   1.000 15.50572 ? 318 GLU A OE2  1 
ATOM   2665 N  N    . ALA A 1 333 ? 46.27259 57.55082 6.62623   1.000 6.31042  ? 319 ALA A N    1 
ATOM   2666 C  CA   . ALA A 1 333 ? 44.94545 57.17150 7.09313   1.000 6.14722  ? 319 ALA A CA   1 
ATOM   2667 C  C    . ALA A 1 333 ? 44.89371 57.14120 8.61876   1.000 6.45290  ? 319 ALA A C    1 
ATOM   2668 O  O    . ALA A 1 333 ? 43.94065 57.64342 9.21768   1.000 6.68862  ? 319 ALA A O    1 
ATOM   2669 C  CB   . ALA A 1 333 ? 44.52120 55.84233 6.46213   1.000 5.81152  ? 319 ALA A CB   1 
ATOM   2670 N  N    . MET A 1 334 ? 45.93750 56.60498 9.26617   1.000 5.40533  ? 320 MET A N    1 
ATOM   2671 C  CA   . MET A 1 334 ? 45.95906 56.53989 10.73183  1.000 7.27193  ? 320 MET A CA   1 
ATOM   2672 C  C    . MET A 1 334 ? 45.94052 57.92189 11.37763  1.000 10.07631 ? 320 MET A C    1 
ATOM   2673 O  O    . MET A 1 334 ? 45.52906 58.06396 12.53935  1.000 11.49630 ? 320 MET A O    1 
ATOM   2674 C  CB   . MET A 1 334 ? 47.18887 55.76900 11.21846  1.000 6.20024  ? 320 MET A CB   1 
ATOM   2675 C  CG   . MET A 1 334 ? 47.17347 54.27054 10.90313  1.000 7.80405  ? 320 MET A CG   1 
ATOM   2676 S  SD   . MET A 1 334 ? 48.67380 53.43327 11.47874  1.000 16.40466 ? 320 MET A SD   1 
ATOM   2677 C  CE   . MET A 1 334 ? 48.57922 53.64532 13.25201  1.000 16.45586 ? 320 MET A CE   1 
ATOM   2678 N  N    . GLU A 1 335 ? 46.42787 58.93681 10.67435  1.000 6.71075  ? 321 GLU A N    1 
ATOM   2679 C  CA   . GLU A 1 335 ? 46.43674 60.30578 11.18054  1.000 7.39877  ? 321 GLU A CA   1 
ATOM   2680 C  C    . GLU A 1 335 ? 45.10760 61.02500 10.98362  1.000 6.73335  ? 321 GLU A C    1 
ATOM   2681 O  O    . GLU A 1 335 ? 44.92974 62.13369 11.50178  1.000 8.85349  ? 321 GLU A O    1 
ATOM   2682 C  CB   . GLU A 1 335 ? 47.59856 61.07576 10.54494  1.000 11.55086 ? 321 GLU A CB   1 
ATOM   2683 C  CG   . GLU A 1 335 ? 48.95163 60.59542 11.05632  1.000 12.31689 ? 321 GLU A CG   1 
ATOM   2684 C  CD   . GLU A 1 335 ? 50.11434 60.87731 10.11522  1.000 27.51840 ? 321 GLU A CD   1 
ATOM   2685 O  OE1  . GLU A 1 335 ? 49.88825 61.36815 8.98694   1.000 26.63219 ? 321 GLU A OE1  1 
ATOM   2686 O  OE2  . GLU A 1 335 ? 51.27195 60.59489 10.50486  1.000 25.79513 ? 321 GLU A OE2  1 
ATOM   2687 N  N    . HIS A 1 336 ? 44.16190 60.41384 10.28324  1.000 7.17957  ? 322 HIS A N    1 
ATOM   2688 C  CA   . HIS A 1 336 ? 42.90751 61.08336 9.98134   1.000 10.19123 ? 322 HIS A CA   1 
ATOM   2689 C  C    . HIS A 1 336 ? 42.08323 61.29126 11.25691  1.000 9.34978  ? 322 HIS A C    1 
ATOM   2690 O  O    . HIS A 1 336 ? 42.11046 60.45885 12.16929  1.000 10.47550 ? 322 HIS A O    1 
ATOM   2691 C  CB   . HIS A 1 336 ? 42.10970 60.23390 8.99370   1.000 7.55468  ? 322 HIS A CB   1 
ATOM   2692 C  CG   . HIS A 1 336 ? 40.95120 60.94999 8.37121   1.000 7.35115  ? 322 HIS A CG   1 
ATOM   2693 N  ND1  . HIS A 1 336 ? 39.72287 61.04902 8.98920   1.000 9.28809  ? 322 HIS A ND1  1 
ATOM   2694 C  CD2  . HIS A 1 336 ? 40.83560 61.60485 7.19105   1.000 10.63301 ? 322 HIS A CD2  1 
ATOM   2695 C  CE1  . HIS A 1 336 ? 38.90176 61.74444 8.22066   1.000 12.90027 ? 322 HIS A CE1  1 
ATOM   2696 N  NE2  . HIS A 1 336 ? 39.55151 62.09290 7.12417   1.000 9.15604  ? 322 HIS A NE2  1 
ATOM   2697 N  N    . PRO A 1 337 ? 41.34140 62.40027 11.33887  1.000 7.66001  ? 323 PRO A N    1 
ATOM   2698 C  CA   . PRO A 1 337 ? 40.46310 62.65134 12.50576  1.000 8.51225  ? 323 PRO A CA   1 
ATOM   2699 C  C    . PRO A 1 337 ? 39.46822 61.54779 12.84764  1.000 10.99759 ? 323 PRO A C    1 
ATOM   2700 O  O    . PRO A 1 337 ? 39.01680 61.47629 14.00017  1.000 8.03255  ? 323 PRO A O    1 
ATOM   2701 C  CB   . PRO A 1 337 ? 39.70836 63.91874 12.09380  1.000 12.59663 ? 323 PRO A CB   1 
ATOM   2702 C  CG   . PRO A 1 337 ? 40.57598 64.58345 11.10307  1.000 11.87136 ? 323 PRO A CG   1 
ATOM   2703 C  CD   . PRO A 1 337 ? 41.37249 63.53638 10.40304  1.000 6.95437  ? 323 PRO A CD   1 
ATOM   2704 N  N    . TYR A 1 338 ? 39.06535 60.71951 11.88276  1.000 8.21748  ? 324 TYR A N    1 
ATOM   2705 C  CA   . TYR A 1 338 ? 38.20370 59.58037 12.19845  1.000 8.06613  ? 324 TYR A CA   1 
ATOM   2706 C  C    . TYR A 1 338 ? 38.77268 58.72576 13.32969  1.000 9.23614  ? 324 TYR A C    1 
ATOM   2707 O  O    . TYR A 1 338 ? 38.01434 58.12382 14.09081  1.000 9.13032  ? 324 TYR A O    1 
ATOM   2708 C  CB   . TYR A 1 338 ? 38.02176 58.73439 10.93997  1.000 6.63506  ? 324 TYR A CB   1 
ATOM   2709 C  CG   . TYR A 1 338 ? 37.11146 57.50750 11.04618  1.000 6.00720  ? 324 TYR A CG   1 
ATOM   2710 C  CD1  . TYR A 1 338 ? 35.73996 57.64037 11.25355  1.000 7.81487  ? 324 TYR A CD1  1 
ATOM   2711 C  CD2  . TYR A 1 338 ? 37.62078 56.22403 10.86209  1.000 6.36104  ? 324 TYR A CD2  1 
ATOM   2712 C  CE1  . TYR A 1 338 ? 34.91215 56.53787 11.31247  1.000 6.26452  ? 324 TYR A CE1  1 
ATOM   2713 C  CE2  . TYR A 1 338 ? 36.78307 55.09021 10.91798  1.000 4.43030  ? 324 TYR A CE2  1 
ATOM   2714 C  CZ   . TYR A 1 338 ? 35.43633 55.26281 11.13926  1.000 8.99414  ? 324 TYR A CZ   1 
ATOM   2715 O  OH   . TYR A 1 338 ? 34.61528 54.17260 11.19523  1.000 7.68203  ? 324 TYR A OH   1 
ATOM   2716 N  N    . PHE A 1 339 ? 40.09529 58.64821 13.45724  1.000 7.92571  ? 325 PHE A N    1 
ATOM   2717 C  CA   . PHE A 1 339 ? 40.69461 57.80061 14.47772  1.000 7.19746  ? 325 PHE A CA   1 
ATOM   2718 C  C    . PHE A 1 339 ? 41.03557 58.53385 15.77197  1.000 7.88768  ? 325 PHE A C    1 
ATOM   2719 O  O    . PHE A 1 339 ? 41.47416 57.88466 16.73277  1.000 10.55279 ? 325 PHE A O    1 
ATOM   2720 C  CB   . PHE A 1 339 ? 41.91734 57.07259 13.91366  1.000 4.23090  ? 325 PHE A CB   1 
ATOM   2721 C  CG   . PHE A 1 339 ? 41.58017 56.17983 12.75687  1.000 6.13181  ? 325 PHE A CG   1 
ATOM   2722 C  CD1  . PHE A 1 339 ? 40.79927 55.05127 12.95109  1.000 5.85515  ? 325 PHE A CD1  1 
ATOM   2723 C  CD2  . PHE A 1 339 ? 42.00614 56.48112 11.47654  1.000 5.74166  ? 325 PHE A CD2  1 
ATOM   2724 C  CE1  . PHE A 1 339 ? 40.45473 54.23256 11.90041  1.000 7.62997  ? 325 PHE A CE1  1 
ATOM   2725 C  CE2  . PHE A 1 339 ? 41.67885 55.65118 10.42039  1.000 4.89249  ? 325 PHE A CE2  1 
ATOM   2726 C  CZ   . PHE A 1 339 ? 40.89619 54.52886 10.63013  1.000 5.37302  ? 325 PHE A CZ   1 
ATOM   2727 N  N    . TYR A 1 340 ? 40.80504 59.84430 15.84785  1.000 9.52787  ? 326 TYR A N    1 
ATOM   2728 C  CA   . TYR A 1 340 ? 41.08718 60.56002 17.09084  1.000 6.04411  ? 326 TYR A CA   1 
ATOM   2729 C  C    . TYR A 1 340 ? 40.47898 59.92015 18.33841  1.000 9.61404  ? 326 TYR A C    1 
ATOM   2730 O  O    . TYR A 1 340 ? 41.20021 59.80790 19.34173  1.000 12.38989 ? 326 TYR A O    1 
ATOM   2731 C  CB   . TYR A 1 340 ? 40.75912 62.05734 16.97969  1.000 8.83562  ? 326 TYR A CB   1 
ATOM   2732 C  CG   . TYR A 1 340 ? 41.02461 62.80610 18.26724  1.000 13.04031 ? 326 TYR A CG   1 
ATOM   2733 C  CD1  . TYR A 1 340 ? 42.31332 62.91402 18.77003  1.000 16.35945 ? 326 TYR A CD1  1 
ATOM   2734 C  CD2  . TYR A 1 340 ? 39.98792 63.38679 18.98591  1.000 15.01571 ? 326 TYR A CD2  1 
ATOM   2735 C  CE1  . TYR A 1 340 ? 42.56429 63.58825 19.95774  1.000 17.24307 ? 326 TYR A CE1  1 
ATOM   2736 C  CE2  . TYR A 1 340 ? 40.22446 64.06350 20.16577  1.000 15.47407 ? 326 TYR A CE2  1 
ATOM   2737 C  CZ   . TYR A 1 340 ? 41.51222 64.16331 20.64404  1.000 25.63143 ? 326 TYR A CZ   1 
ATOM   2738 O  OH   . TYR A 1 340 ? 41.75013 64.84207 21.81656  1.000 34.25819 ? 326 TYR A OH   1 
ATOM   2739 N  N    . PRO A 1 341 ? 39.21297 59.46898 18.35688  1.000 10.81994 ? 327 PRO A N    1 
ATOM   2740 C  CA   . PRO A 1 341 ? 38.69749 58.81250 19.57775  1.000 8.90752  ? 327 PRO A CA   1 
ATOM   2741 C  C    . PRO A 1 341 ? 39.47859 57.57441 19.97321  1.000 12.27678 ? 327 PRO A C    1 
ATOM   2742 O  O    . PRO A 1 341 ? 39.59343 57.27563 21.17040  1.000 15.63902 ? 327 PRO A O    1 
ATOM   2743 C  CB   . PRO A 1 341 ? 37.25224 58.45540 19.20813  1.000 12.51554 ? 327 PRO A CB   1 
ATOM   2744 C  CG   . PRO A 1 341 ? 36.90635 59.34049 18.09248  1.000 15.87906 ? 327 PRO A CG   1 
ATOM   2745 C  CD   . PRO A 1 341 ? 38.17514 59.57241 17.32209  1.000 10.07476 ? 327 PRO A CD   1 
ATOM   2746 N  N    . VAL A 1 342 ? 40.02267 56.85026 18.99528  1.000 9.72048  ? 328 VAL A N    1 
ATOM   2747 C  CA   . VAL A 1 342 ? 40.83161 55.67471 19.29023  1.000 8.07501  ? 328 VAL A CA   1 
ATOM   2748 C  C    . VAL A 1 342 ? 42.17054 56.09305 19.87338  1.000 14.09539 ? 328 VAL A C    1 
ATOM   2749 O  O    . VAL A 1 342 ? 42.62387 55.54810 20.88515  1.000 20.53470 ? 328 VAL A O    1 
ATOM   2750 C  CB   . VAL A 1 342 ? 41.01665 54.82819 18.01644  1.000 7.64096  ? 328 VAL A CB   1 
ATOM   2751 C  CG1  . VAL A 1 342 ? 41.91486 53.64287 18.31340  1.000 14.05033 ? 328 VAL A CG1  1 
ATOM   2752 C  CG2  . VAL A 1 342 ? 39.66506 54.35481 17.48824  1.000 11.89499 ? 328 VAL A CG2  1 
ATOM   2753 N  N    . VAL A 1 343 ? 42.81958 57.07048 19.23652  1.000 12.34180 ? 329 VAL A N    1 
ATOM   2754 C  CA   . VAL A 1 343 ? 44.09709 57.58633 19.71844  1.000 14.24195 ? 329 VAL A CA   1 
ATOM   2755 C  C    . VAL A 1 343 ? 43.95253 58.14902 21.12560  1.000 22.79758 ? 329 VAL A C    1 
ATOM   2756 O  O    . VAL A 1 343 ? 44.79469 57.90402 22.00045  1.000 27.32426 ? 329 VAL A O    1 
ATOM   2757 C  CB   . VAL A 1 343 ? 44.62985 58.64092 18.73418  1.000 16.66535 ? 329 VAL A CB   1 
ATOM   2758 C  CG1  . VAL A 1 343 ? 45.80311 59.38895 19.34467  1.000 23.11306 ? 329 VAL A CG1  1 
ATOM   2759 C  CG2  . VAL A 1 343 ? 45.03236 57.98758 17.43333  1.000 14.64507 ? 329 VAL A CG2  1 
ATOM   2760 N  N    . LYS A 1 344 ? 42.88613 58.91365 21.36651  1.000 17.10693 ? 330 LYS A N    1 
ATOM   2761 C  CA   . LYS A 1 344 ? 42.68668 59.51582 22.67876  1.000 20.43459 ? 330 LYS A CA   1 
ATOM   2762 C  C    . LYS A 1 344 ? 42.40484 58.46664 23.74696  1.000 35.51416 ? 330 LYS A C    1 
ATOM   2763 O  O    . LYS A 1 344 ? 42.78239 58.65017 24.90858  1.000 36.87245 ? 330 LYS A O    1 
ATOM   2764 C  CB   . LYS A 1 344 ? 41.56377 60.55133 22.60854  1.000 22.85136 ? 330 LYS A CB   1 
ATOM   2765 C  CG   . LYS A 1 344 ? 41.29514 61.26766 23.92260  1.000 39.69339 ? 330 LYS A CG   1 
ATOM   2766 C  CD   . LYS A 1 344 ? 40.37848 62.46749 23.72720  1.000 47.49706 ? 330 LYS A CD   1 
ATOM   2767 C  CE   . LYS A 1 344 ? 39.08037 62.07456 23.03869  1.000 44.97115 ? 330 LYS A CE   1 
ATOM   2768 N  NZ   . LYS A 1 344 ? 38.16862 63.24298 22.87992  1.000 59.88616 ? 330 LYS A NZ   1 
ATOM   2769 N  N    . GLU A 1 345 ? 41.75474 57.36315 23.37727  1.000 31.61184 ? 331 GLU A N    1 
ATOM   2770 C  CA   . GLU A 1 345 ? 41.48886 56.29032 24.32696  1.000 25.17089 ? 331 GLU A CA   1 
ATOM   2771 C  C    . GLU A 1 345 ? 42.71891 55.42014 24.56544  1.000 37.41133 ? 331 GLU A C    1 
ATOM   2772 O  O    . GLU A 1 345 ? 42.92439 54.94158 25.68587  1.000 40.39579 ? 331 GLU A O    1 
ATOM   2773 C  CB   . GLU A 1 345 ? 40.30710 55.44983 23.83346  1.000 31.53320 ? 331 GLU A CB   1 
ATOM   2774 C  CG   . GLU A 1 345 ? 39.82581 54.38194 24.80022  1.000 40.88595 ? 331 GLU A CG   1 
ATOM   2775 C  CD   . GLU A 1 345 ? 38.97241 54.94641 25.91925  1.000 49.00189 ? 331 GLU A CD   1 
ATOM   2776 O  OE1  . GLU A 1 345 ? 38.65495 56.15725 25.88101  1.000 47.16994 ? 331 GLU A OE1  1 
ATOM   2777 O  OE2  . GLU A 1 345 ? 38.61907 54.17411 26.83590  1.000 48.12814 ? 331 GLU A OE2  1 
ATOM   2778 N  N    . GLN A 1 346 ? 43.55083 55.21161 23.53712  1.000 36.36844 ? 332 GLN A N    1 
ATOM   2779 C  CA   . GLN A 1 346 ? 44.81719 54.48170 23.66933  1.000 39.55659 ? 332 GLN A CA   1 
ATOM   2780 C  C    . GLN A 1 346 ? 45.88987 55.27975 24.41189  1.000 52.87559 ? 332 GLN A C    1 
ATOM   2781 O  O    . GLN A 1 346 ? 47.05114 54.84798 24.43132  1.000 47.51643 ? 332 GLN A O    1 
ATOM   2782 C  CB   . GLN A 1 346 ? 45.32784 53.98715 22.30686  1.000 46.42527 ? 332 GLN A CB   1 
ATOM   2783 C  CG   . GLN A 1 346 ? 44.98104 52.51751 22.02068  1.000 60.66183 ? 332 GLN A CG   1 
ATOM   2784 C  CD   . GLN A 1 346 ? 44.95925 52.14745 20.53127  1.000 60.41927 ? 332 GLN A CD   1 
ATOM   2785 O  OE1  . GLN A 1 346 ? 45.92712 52.39783 19.78975  1.000 22.28495 ? 332 GLN A OE1  1 
ATOM   2786 N  NE2  . GLN A 1 346 ? 43.84874 51.52304 20.09283  1.000 18.19720 ? 332 GLN A NE2  1 
ATOM   2787 N  N    . SER A 1 347 ? 45.49941 56.41606 25.00146  1.000 61.15532 ? 333 SER A N    1 
ATOM   2788 C  CA   . SER A 1 347 ? 46.37727 57.22066 25.83923  1.000 59.95275 ? 333 SER A CA   1 
ATOM   2789 C  C    . SER A 1 347 ? 45.73540 57.62387 27.16094  1.000 65.04282 ? 333 SER A C    1 
ATOM   2790 O  O    . SER A 1 347 ? 46.34525 58.38847 27.91683  1.000 75.41799 ? 333 SER A O    1 
ATOM   2791 C  CB   . SER A 1 347 ? 46.84848 58.47876 25.09122  1.000 53.36386 ? 333 SER A CB   1 
ATOM   2792 O  OG   . SER A 1 347 ? 47.52912 58.13644 23.89476  1.000 60.37541 ? 333 SER A OG   1 
ATOM   2793 N  N    . GLN A 1 348 ? 44.52718 57.14730 27.45274  1.000 71.22068 ? 334 GLN A N    1 
ATOM   2794 C  CA   . GLN A 1 348 ? 43.87563 57.38297 28.73816  1.000 67.82778 ? 334 GLN A CA   1 
ATOM   2795 C  C    . GLN A 1 348 ? 43.95853 56.12891 29.60144  1.000 71.27027 ? 334 GLN A C    1 
ATOM   2796 O  O    . GLN A 1 348 ? 44.37335 56.18470 30.75871  1.000 79.15881 ? 334 GLN A O    1 
ATOM   2797 C  CB   . GLN A 1 348 ? 42.40902 57.77519 28.54077  1.000 55.93965 ? 334 GLN A CB   1 
ATOM   2798 C  CG   . GLN A 1 348 ? 42.20360 59.17955 27.99893  1.000 73.74974 ? 334 GLN A CG   1 
ATOM   2799 C  CD   . GLN A 1 348 ? 42.50518 60.25412 29.02637  1.000 85.62902 ? 334 GLN A CD   1 
ATOM   2800 O  OE1  . GLN A 1 348 ? 43.31156 61.15139 28.78309  1.000 86.14247 ? 334 GLN A OE1  1 
ATOM   2801 N  NE2  . GLN A 1 348 ? 41.84915 60.17298 30.18013  1.000 84.98491 ? 334 GLN A NE2  1 
HETATM 2802 C  C1   . EDO B 2 .   ? 36.53478 35.35781 -5.27616  1.000 40.07516 ? 401 EDO A C1   1 
HETATM 2803 O  O1   . EDO B 2 .   ? 37.22238 36.11467 -6.25302  1.000 29.83791 ? 401 EDO A O1   1 
HETATM 2804 C  C2   . EDO B 2 .   ? 35.52426 36.20463 -4.54283  1.000 29.28725 ? 401 EDO A C2   1 
HETATM 2805 O  O2   . EDO B 2 .   ? 34.25002 36.07177 -5.13864  1.000 30.53331 ? 401 EDO A O2   1 
HETATM 2806 C  C1   . 3NG C 3 .   ? 44.18593 30.98116 9.35513   1.000 10.28366 ? 402 3NG A C1   1 
HETATM 2807 C  C2   . 3NG C 3 .   ? 44.66876 31.29559 10.63379  1.000 10.17233 ? 402 3NG A C2   1 
HETATM 2808 C  C3   . 3NG C 3 .   ? 45.98412 31.76969 10.76057  1.000 12.04429 ? 402 3NG A C3   1 
HETATM 2809 C  C4   . 3NG C 3 .   ? 46.77342 31.92144 9.66903   1.000 8.39053  ? 402 3NG A C4   1 
HETATM 2810 C  C5   . 3NG C 3 .   ? 46.30696 31.61272 8.38077   1.000 10.17150 ? 402 3NG A C5   1 
HETATM 2811 C  C6   . 3NG C 3 .   ? 45.01746 31.14386 8.23180   1.000 12.91343 ? 402 3NG A C6   1 
HETATM 2812 C  C7   . 3NG C 3 .   ? 42.47855 30.62264 11.51702  1.000 22.11588 ? 402 3NG A C7   1 
HETATM 2813 C  C8   . 3NG C 3 .   ? 43.78058 31.10300 11.75078  1.000 17.08920 ? 402 3NG A C8   1 
HETATM 2814 N  N9   . 3NG C 3 .   ? 42.92001 30.52136 9.14036   1.000 17.66367 ? 402 3NG A N9   1 
HETATM 2815 C  C10  . 3NG C 3 .   ? 42.10052 30.33685 10.12687  1.000 17.78389 ? 402 3NG A C10  1 
HETATM 2816 C  C11  . 3NG C 3 .   ? 42.11556 30.75363 13.89331  1.000 17.16449 ? 402 3NG A C11  1 
HETATM 2817 N  N12  . 3NG C 3 .   ? 43.35308 31.22435 14.12204  1.000 25.92532 ? 402 3NG A N12  1 
HETATM 2818 C  C13  . 3NG C 3 .   ? 44.15310 31.39478 13.08789  1.000 25.49241 ? 402 3NG A C13  1 
HETATM 2819 C  C14  . 3NG C 3 .   ? 41.64017 30.45216 12.63210  1.000 23.84539 ? 402 3NG A C14  1 
HETATM 2820 N  N15  . 3NG C 3 .   ? 40.82336 29.87331 9.91068   1.000 26.45320 ? 402 3NG A N15  1 
HETATM 2821 C  C16  . 3NG C 3 .   ? 40.07921 29.49116 8.78554   1.000 21.33217 ? 402 3NG A C16  1 
HETATM 2822 C  C17  . 3NG C 3 .   ? 40.78620 29.08451 7.63783   1.000 28.15383 ? 402 3NG A C17  1 
HETATM 2823 C  C18  . 3NG C 3 .   ? 40.11642 28.68545 6.49434   1.000 42.12534 ? 402 3NG A C18  1 
HETATM 2824 C  C19  . 3NG C 3 .   ? 38.72832 28.66538 6.43703   1.000 31.82511 ? 402 3NG A C19  1 
HETATM 2825 C  C20  . 3NG C 3 .   ? 38.03717 29.06127 7.57512   1.000 36.82736 ? 402 3NG A C20  1 
HETATM 2826 C  C21  . 3NG C 3 .   ? 38.68319 29.46851 8.73965   1.000 30.50702 ? 402 3NG A C21  1 
HETATM 2827 CL CL22 . 3NG C 3 .   ? 41.04824 28.20164 5.10043   1.000 45.58776 ? 402 3NG A CL22 1 
HETATM 2828 C  C23  . 3NG C 3 .   ? 47.22514 31.83824 7.18605   1.000 8.42740  ? 402 3NG A C23  1 
HETATM 2829 O  O24  . 3NG C 3 .   ? 46.91205 31.27805 6.12530   1.000 9.94260  ? 402 3NG A O24  1 
HETATM 2830 O  O25  . 3NG C 3 .   ? 48.16588 32.63353 7.38882   1.000 12.01954 ? 402 3NG A O25  1 
HETATM 2831 C  C1   . EDO D 2 .   ? 50.19196 66.68949 9.79154   1.000 6.36260  ? 403 EDO A C1   1 
HETATM 2832 O  O1   . EDO D 2 .   ? 51.47597 66.36298 9.28037   1.000 18.33100 ? 403 EDO A O1   1 
HETATM 2833 C  C2   . EDO D 2 .   ? 49.34080 65.46222 9.96973   1.000 16.45760 ? 403 EDO A C2   1 
HETATM 2834 O  O2   . EDO D 2 .   ? 49.76759 64.73963 11.10226  1.000 48.98470 ? 403 EDO A O2   1 
HETATM 2835 O  O    . HOH E 4 .   ? 44.19454 53.30918 -24.61281 1.000 32.15853 ? 501 HOH A O    1 
HETATM 2836 O  O    . HOH E 4 .   ? 58.76256 48.53090 -15.83343 1.000 26.80949 ? 502 HOH A O    1 
HETATM 2837 O  O    . HOH E 4 .   ? 70.24853 34.64226 -5.48211  1.000 39.70571 ? 503 HOH A O    1 
HETATM 2838 O  O    . HOH E 4 .   ? 42.584   27.525   22.967    1.000 36.43089 ? 504 HOH A O    1 
HETATM 2839 O  O    . HOH E 4 .   ? 60.27556 19.51439 10.25385  1.000 14.72135 ? 505 HOH A O    1 
HETATM 2840 O  O    . HOH E 4 .   ? 51.56389 25.57276 -1.81625  1.000 35.50041 ? 506 HOH A O    1 
HETATM 2841 O  O    . HOH E 4 .   ? 42.74566 33.22185 2.85653   1.000 17.71876 ? 507 HOH A O    1 
HETATM 2842 O  O    . HOH E 4 .   ? 36.43625 37.29518 -10.16947 1.000 28.75634 ? 508 HOH A O    1 
HETATM 2843 O  O    . HOH E 4 .   ? 36.25646 58.77444 -3.93630  1.000 15.04671 ? 509 HOH A O    1 
HETATM 2844 O  O    . HOH E 4 .   ? 27.20774 47.29756 12.96462  1.000 31.51037 ? 510 HOH A O    1 
HETATM 2845 O  O    . HOH E 4 .   ? 47.78703 31.50501 -2.25013  1.000 27.72759 ? 511 HOH A O    1 
HETATM 2846 O  O    . HOH E 4 .   ? 62.01990 44.46959 -10.64574 1.000 28.71836 ? 512 HOH A O    1 
HETATM 2847 O  O    . HOH E 4 .   ? 35.10282 61.42888 -21.82122 1.000 28.25735 ? 513 HOH A O    1 
HETATM 2848 O  O    . HOH E 4 .   ? 68.77468 35.74880 5.19660   1.000 43.26022 ? 514 HOH A O    1 
HETATM 2849 O  O    . HOH E 4 .   ? 48.75319 43.67995 18.65423  1.000 32.05085 ? 515 HOH A O    1 
HETATM 2850 O  O    . HOH E 4 .   ? 28.06994 51.31557 -21.84445 1.000 34.77657 ? 516 HOH A O    1 
HETATM 2851 O  O    . HOH E 4 .   ? 43.343   32.136   20.841    1.000 41.14622 ? 517 HOH A O    1 
HETATM 2852 O  O    . HOH E 4 .   ? 47.75082 53.11976 -23.54435 1.000 27.65809 ? 518 HOH A O    1 
HETATM 2853 O  O    . HOH E 4 .   ? 53.75402 33.02030 -1.90348  1.000 31.49413 ? 519 HOH A O    1 
HETATM 2854 O  O    . HOH E 4 .   ? 59.35034 39.67544 -5.95793  1.000 21.14487 ? 520 HOH A O    1 
HETATM 2855 O  O    . HOH E 4 .   ? 60.32351 40.34105 -8.52153  1.000 39.56525 ? 521 HOH A O    1 
HETATM 2856 O  O    . HOH E 4 .   ? 72.915   40.648   5.247     1.000 35.54717 ? 522 HOH A O    1 
HETATM 2857 O  O    . HOH E 4 .   ? 54.08078 47.12696 -20.24487 1.000 34.09237 ? 523 HOH A O    1 
HETATM 2858 O  O    . HOH E 4 .   ? 44.84458 30.51041 4.77239   1.000 15.37859 ? 524 HOH A O    1 
HETATM 2859 O  O    . HOH E 4 .   ? 63.68457 47.30663 -5.28769  1.000 18.89716 ? 525 HOH A O    1 
HETATM 2860 O  O    . HOH E 4 .   ? 47.33795 51.26112 -26.47022 1.000 40.57139 ? 526 HOH A O    1 
HETATM 2861 O  O    . HOH E 4 .   ? 24.78499 47.55730 -15.01430 1.000 25.47665 ? 527 HOH A O    1 
HETATM 2862 O  O    . HOH E 4 .   ? 51.48502 30.85184 26.79310  1.000 27.95331 ? 528 HOH A O    1 
HETATM 2863 O  O    . HOH E 4 .   ? 43.82263 22.72551 -1.31618  1.000 34.94824 ? 529 HOH A O    1 
HETATM 2864 O  O    . HOH E 4 .   ? 40.71010 36.27490 -2.06602  1.000 21.68513 ? 530 HOH A O    1 
HETATM 2865 O  O    . HOH E 4 .   ? 36.85596 40.63674 9.64541   1.000 19.01660 ? 531 HOH A O    1 
HETATM 2866 O  O    . HOH E 4 .   ? 24.55233 47.61956 -10.86019 1.000 31.68137 ? 532 HOH A O    1 
HETATM 2867 O  O    . HOH E 4 .   ? 55.99597 50.93544 -9.48954  1.000 11.22415 ? 533 HOH A O    1 
HETATM 2868 O  O    . HOH E 4 .   ? 36.25859 47.45509 19.62147  1.000 27.14038 ? 534 HOH A O    1 
HETATM 2869 O  O    . HOH E 4 .   ? 52.79728 30.02727 -0.17286  1.000 18.87677 ? 535 HOH A O    1 
HETATM 2870 O  O    . HOH E 4 .   ? 62.78541 47.95777 -9.39243  1.000 25.23699 ? 536 HOH A O    1 
HETATM 2871 O  O    . HOH E 4 .   ? 51.78232 62.39057 4.23987   1.000 23.69107 ? 537 HOH A O    1 
HETATM 2872 O  O    . HOH E 4 .   ? 48.81093 63.30694 7.61293   1.000 26.14377 ? 538 HOH A O    1 
HETATM 2873 O  O    . HOH E 4 .   ? 30.33565 45.63538 20.04043  1.000 33.02414 ? 539 HOH A O    1 
HETATM 2874 O  O    . HOH E 4 .   ? 58.40203 57.47743 -4.01852  1.000 23.44407 ? 540 HOH A O    1 
HETATM 2875 O  O    . HOH E 4 .   ? 45.55298 21.04510 -0.65365  1.000 34.99135 ? 541 HOH A O    1 
HETATM 2876 O  O    . HOH E 4 .   ? 30.03621 41.33504 -19.17501 1.000 23.08424 ? 542 HOH A O    1 
HETATM 2877 O  O    . HOH E 4 .   ? 44.19345 27.95949 3.13422   1.000 29.98895 ? 543 HOH A O    1 
HETATM 2878 O  O    . HOH E 4 .   ? 42.11737 40.67963 -11.37612 1.000 23.67184 ? 544 HOH A O    1 
HETATM 2879 O  O    . HOH E 4 .   ? 28.15247 40.31840 -15.41107 1.000 28.78193 ? 545 HOH A O    1 
HETATM 2880 O  O    . HOH E 4 .   ? 42.98623 50.66481 17.75977  1.000 16.89842 ? 546 HOH A O    1 
HETATM 2881 O  O    . HOH E 4 .   ? 66.09385 30.21577 8.12085   1.000 30.52556 ? 547 HOH A O    1 
HETATM 2882 O  O    . HOH E 4 .   ? 47.28741 34.55019 -9.14831  1.000 35.42173 ? 548 HOH A O    1 
HETATM 2883 O  O    . HOH E 4 .   ? 50.86783 29.07026 20.98167  1.000 24.56500 ? 549 HOH A O    1 
HETATM 2884 O  O    . HOH E 4 .   ? 26.83271 56.01806 17.14191  1.000 20.08518 ? 550 HOH A O    1 
HETATM 2885 O  O    . HOH E 4 .   ? 52.93104 52.24443 -8.78975  1.000 14.24222 ? 551 HOH A O    1 
HETATM 2886 O  O    . HOH E 4 .   ? 52.26421 48.66339 -16.74645 1.000 29.34429 ? 552 HOH A O    1 
HETATM 2887 O  O    . HOH E 4 .   ? 30.58749 56.48222 -20.38673 1.000 33.89196 ? 553 HOH A O    1 
HETATM 2888 O  O    . HOH E 4 .   ? 43.52700 64.49442 -24.56762 1.000 39.43928 ? 554 HOH A O    1 
HETATM 2889 O  O    . HOH E 4 .   ? 40.63233 44.59322 -17.91108 1.000 18.48739 ? 555 HOH A O    1 
HETATM 2890 O  O    . HOH E 4 .   ? 48.44408 29.89792 19.68249  1.000 18.32522 ? 556 HOH A O    1 
HETATM 2891 O  O    . HOH E 4 .   ? 39.44975 61.03148 -12.59988 1.000 18.77095 ? 557 HOH A O    1 
HETATM 2892 O  O    . HOH E 4 .   ? 59.89380 42.42595 11.47877  1.000 20.76657 ? 558 HOH A O    1 
HETATM 2893 O  O    . HOH E 4 .   ? 42.13535 35.06442 20.28880  1.000 16.72637 ? 559 HOH A O    1 
HETATM 2894 O  O    . HOH E 4 .   ? 67.19142 34.28110 3.50963   1.000 21.58402 ? 560 HOH A O    1 
HETATM 2895 O  O    . HOH E 4 .   ? 45.21063 36.58842 24.23052  1.000 28.01197 ? 561 HOH A O    1 
HETATM 2896 O  O    . HOH E 4 .   ? 14.74479 49.43139 9.43822   1.000 36.52447 ? 562 HOH A O    1 
HETATM 2897 O  O    . HOH E 4 .   ? 47.63768 57.83812 14.46633  1.000 17.75182 ? 563 HOH A O    1 
HETATM 2898 O  O    . HOH E 4 .   ? 51.31222 55.03154 -5.90469  1.000 16.87823 ? 564 HOH A O    1 
HETATM 2899 O  O    . HOH E 4 .   ? 59.34727 22.31262 16.68301  1.000 16.17910 ? 565 HOH A O    1 
HETATM 2900 O  O    . HOH E 4 .   ? 34.65910 52.85574 -23.02370 1.000 31.65099 ? 566 HOH A O    1 
HETATM 2901 O  O    . HOH E 4 .   ? 66.05304 24.30281 4.45370   1.000 30.58597 ? 567 HOH A O    1 
HETATM 2902 O  O    . HOH E 4 .   ? 37.81285 58.25135 22.91136  1.000 25.47904 ? 568 HOH A O    1 
HETATM 2903 O  O    . HOH E 4 .   ? 31.40241 57.39245 12.11665  1.000 11.11637 ? 569 HOH A O    1 
HETATM 2904 O  O    . HOH E 4 .   ? 49.79329 61.49488 -17.61875 1.000 27.69249 ? 570 HOH A O    1 
HETATM 2905 O  O    . HOH E 4 .   ? 43.14612 60.67791 -0.86903  1.000 16.71855 ? 571 HOH A O    1 
HETATM 2906 O  O    . HOH E 4 .   ? 69.57191 48.73891 4.69615   1.000 15.55108 ? 572 HOH A O    1 
HETATM 2907 O  O    . HOH E 4 .   ? 30.73253 58.96633 -19.20535 1.000 17.44423 ? 573 HOH A O    1 
HETATM 2908 O  O    . HOH E 4 .   ? 64.44079 28.42873 -4.57193  1.000 40.98734 ? 574 HOH A O    1 
HETATM 2909 O  O    . HOH E 4 .   ? 61.48399 26.47292 12.40091  1.000 32.92379 ? 575 HOH A O    1 
HETATM 2910 O  O    . HOH E 4 .   ? 37.74330 16.93151 14.11820  1.000 32.32037 ? 576 HOH A O    1 
HETATM 2911 O  O    . HOH E 4 .   ? 15.63397 51.77308 11.06511  1.000 33.90360 ? 577 HOH A O    1 
HETATM 2912 O  O    . HOH E 4 .   ? 57.07318 13.13827 11.78200  1.000 22.44031 ? 578 HOH A O    1 
HETATM 2913 O  O    . HOH E 4 .   ? 50.81357 52.51597 2.96717   1.000 6.90798  ? 579 HOH A O    1 
HETATM 2914 O  O    . HOH E 4 .   ? 25.40203 41.50226 -6.98471  1.000 27.76654 ? 580 HOH A O    1 
HETATM 2915 O  O    . HOH E 4 .   ? 29.18532 37.47298 -6.88269  1.000 34.44248 ? 581 HOH A O    1 
HETATM 2916 O  O    . HOH E 4 .   ? 32.13047 54.13862 12.27083  1.000 10.72442 ? 582 HOH A O    1 
HETATM 2917 O  O    . HOH E 4 .   ? 42.10640 31.13815 5.62082   1.000 36.75606 ? 583 HOH A O    1 
HETATM 2918 O  O    . HOH E 4 .   ? 53.17335 29.94733 23.73638  1.000 34.36421 ? 584 HOH A O    1 
HETATM 2919 O  O    . HOH E 4 .   ? 42.89970 33.85035 -0.91551  1.000 31.69364 ? 585 HOH A O    1 
HETATM 2920 O  O    . HOH E 4 .   ? 33.17423 39.41142 1.59892   1.000 17.86659 ? 586 HOH A O    1 
HETATM 2921 O  O    . HOH E 4 .   ? 69.18004 45.33498 -2.57691  1.000 10.27909 ? 587 HOH A O    1 
HETATM 2922 O  O    . HOH E 4 .   ? 50.66457 37.58459 18.74524  1.000 17.40319 ? 588 HOH A O    1 
HETATM 2923 O  O    . HOH E 4 .   ? 27.01931 46.21648 -4.14125  1.000 15.57204 ? 589 HOH A O    1 
HETATM 2924 O  O    . HOH E 4 .   ? 36.95306 62.39841 20.60934  1.000 30.73572 ? 590 HOH A O    1 
HETATM 2925 O  O    . HOH E 4 .   ? 54.73594 48.52148 -9.78433  1.000 9.03999  ? 591 HOH A O    1 
HETATM 2926 O  O    . HOH E 4 .   ? 63.98116 35.59941 -5.38328  1.000 14.44852 ? 592 HOH A O    1 
HETATM 2927 O  O    . HOH E 4 .   ? 25.42374 62.35457 -8.82434  1.000 29.69240 ? 593 HOH A O    1 
HETATM 2928 O  O    . HOH E 4 .   ? 66.75872 35.26559 1.02343   1.000 15.51010 ? 594 HOH A O    1 
HETATM 2929 O  O    . HOH E 4 .   ? 47.67249 46.38208 19.05376  1.000 28.40116 ? 595 HOH A O    1 
HETATM 2930 O  O    . HOH E 4 .   ? 45.27989 47.82964 -19.46658 1.000 16.23045 ? 596 HOH A O    1 
HETATM 2931 O  O    . HOH E 4 .   ? 49.861   63.450   1.120     1.000 32.95193 ? 597 HOH A O    1 
HETATM 2932 O  O    . HOH E 4 .   ? 31.00277 60.64220 -14.70104 1.000 13.13902 ? 598 HOH A O    1 
HETATM 2933 O  O    . HOH E 4 .   ? 43.46686 62.53765 -17.14056 1.000 22.31325 ? 599 HOH A O    1 
HETATM 2934 O  O    . HOH E 4 .   ? 50.34178 33.51743 5.99599   1.000 7.73794  ? 600 HOH A O    1 
HETATM 2935 O  O    . HOH E 4 .   ? 21.01167 54.16057 13.19338  1.000 20.64657 ? 601 HOH A O    1 
HETATM 2936 O  O    . HOH E 4 .   ? 62.49679 42.72644 8.95843   1.000 22.14403 ? 602 HOH A O    1 
HETATM 2937 O  O    . HOH E 4 .   ? 59.95455 18.62427 20.54194  1.000 33.04839 ? 603 HOH A O    1 
HETATM 2938 O  O    . HOH E 4 .   ? 61.93538 47.04221 -11.35236 1.000 35.45572 ? 604 HOH A O    1 
HETATM 2939 O  O    . HOH E 4 .   ? 51.028   26.895   27.919    1.000 19.46959 ? 605 HOH A O    1 
HETATM 2940 O  O    . HOH E 4 .   ? 45.72530 19.10963 3.22308   1.000 33.37305 ? 606 HOH A O    1 
HETATM 2941 O  O    . HOH E 4 .   ? 35.33966 59.59957 -8.27860  1.000 13.77517 ? 607 HOH A O    1 
HETATM 2942 O  O    . HOH E 4 .   ? 39.14674 35.08203 23.46436  1.000 21.11315 ? 608 HOH A O    1 
HETATM 2943 O  O    . HOH E 4 .   ? 28.19487 44.46436 -15.86032 1.000 19.24447 ? 609 HOH A O    1 
HETATM 2944 O  O    . HOH E 4 .   ? 49.94979 52.13993 -18.79872 1.000 33.31385 ? 610 HOH A O    1 
HETATM 2945 O  O    . HOH E 4 .   ? 27.51840 49.77248 -7.23319  1.000 20.55386 ? 611 HOH A O    1 
HETATM 2946 O  O    . HOH E 4 .   ? 37.30045 63.96180 0.95641   1.000 26.07156 ? 612 HOH A O    1 
HETATM 2947 O  O    . HOH E 4 .   ? 27.61133 41.65582 7.76393   1.000 33.94039 ? 613 HOH A O    1 
HETATM 2948 O  O    . HOH E 4 .   ? 52.43824 13.99504 17.33623  1.000 23.98470 ? 614 HOH A O    1 
HETATM 2949 O  O    . HOH E 4 .   ? 20.91182 59.04935 2.41045   1.000 24.20106 ? 615 HOH A O    1 
HETATM 2950 O  O    . HOH E 4 .   ? 46.77795 62.89704 13.40449  1.000 7.88945  ? 616 HOH A O    1 
HETATM 2951 O  O    . HOH E 4 .   ? 47.52181 20.97108 1.67031   1.000 30.50289 ? 617 HOH A O    1 
HETATM 2952 O  O    . HOH E 4 .   ? 41.14601 46.83217 -19.52947 1.000 18.31449 ? 618 HOH A O    1 
HETATM 2953 O  O    . HOH E 4 .   ? 52.711   58.489   4.343     1.000 11.93525 ? 619 HOH A O    1 
HETATM 2954 O  O    . HOH E 4 .   ? 44.10344 59.97825 14.02464  1.000 11.04489 ? 620 HOH A O    1 
HETATM 2955 O  O    . HOH E 4 .   ? 52.53073 49.90970 12.26386  1.000 14.08406 ? 621 HOH A O    1 
HETATM 2956 O  O    . HOH E 4 .   ? 65.34858 12.41033 3.60497   1.000 33.08877 ? 622 HOH A O    1 
HETATM 2957 O  O    . HOH E 4 .   ? 51.96680 54.06167 5.15672   1.000 7.86678  ? 623 HOH A O    1 
HETATM 2958 O  O    . HOH E 4 .   ? 24.16408 55.99024 -12.02302 1.000 22.60031 ? 624 HOH A O    1 
HETATM 2959 O  O    . HOH E 4 .   ? 44.010   45.209   19.363    1.000 34.64347 ? 625 HOH A O    1 
HETATM 2960 O  O    . HOH E 4 .   ? 29.31382 57.62183 18.01522  1.000 22.52723 ? 626 HOH A O    1 
HETATM 2961 O  O    . HOH E 4 .   ? 52.16673 21.05322 29.01023  1.000 34.91355 ? 627 HOH A O    1 
HETATM 2962 O  O    . HOH E 4 .   ? 46.81732 58.75920 -22.11039 1.000 21.26646 ? 628 HOH A O    1 
HETATM 2963 O  O    . HOH E 4 .   ? 41.41098 52.10173 -24.04909 1.000 20.09927 ? 629 HOH A O    1 
HETATM 2964 O  O    . HOH E 4 .   ? 60.03987 20.67159 1.71709   1.000 28.95673 ? 630 HOH A O    1 
HETATM 2965 O  O    . HOH E 4 .   ? 63.77370 53.34649 -9.11993  1.000 39.14349 ? 631 HOH A O    1 
HETATM 2966 O  O    . HOH E 4 .   ? 48.69334 56.15729 -2.53906  1.000 8.42634  ? 632 HOH A O    1 
HETATM 2967 O  O    . HOH E 4 .   ? 50.04317 13.59081 18.84896  1.000 18.90567 ? 633 HOH A O    1 
HETATM 2968 O  O    . HOH E 4 .   ? 53.10509 62.40583 -1.01874  1.000 25.53905 ? 634 HOH A O    1 
HETATM 2969 O  O    . HOH E 4 .   ? 39.48647 42.47509 -19.06535 1.000 24.75954 ? 635 HOH A O    1 
HETATM 2970 O  O    . HOH E 4 .   ? 48.19911 50.22734 -6.64760  1.000 7.79433  ? 636 HOH A O    1 
HETATM 2971 O  O    . HOH E 4 .   ? 41.36576 41.74615 -13.39584 1.000 27.04552 ? 637 HOH A O    1 
HETATM 2972 O  O    . HOH E 4 .   ? 53.70539 35.29832 -0.58053  1.000 9.22704  ? 638 HOH A O    1 
HETATM 2973 O  O    . HOH E 4 .   ? 57.90915 53.27841 -12.12583 1.000 29.75806 ? 639 HOH A O    1 
HETATM 2974 O  O    . HOH E 4 .   ? 47.95698 54.25670 -0.56873  1.000 11.05879 ? 640 HOH A O    1 
HETATM 2975 O  O    . HOH E 4 .   ? 31.78363 58.57571 -5.05246  1.000 17.41382 ? 641 HOH A O    1 
HETATM 2976 O  O    . HOH E 4 .   ? 48.73946 37.54477 0.91914   1.000 9.65113  ? 642 HOH A O    1 
HETATM 2977 O  O    . HOH E 4 .   ? 36.48564 46.41134 -5.31039  1.000 9.45786  ? 643 HOH A O    1 
HETATM 2978 O  O    . HOH E 4 .   ? 44.26365 31.02843 0.32322   1.000 39.88362 ? 644 HOH A O    1 
HETATM 2979 O  O    . HOH E 4 .   ? 50.16242 33.85234 20.43496  1.000 31.47961 ? 645 HOH A O    1 
HETATM 2980 O  O    . HOH E 4 .   ? 49.139   31.144   23.522    1.000 33.26978 ? 646 HOH A O    1 
HETATM 2981 O  O    . HOH E 4 .   ? 34.24081 59.62102 -5.58138  1.000 14.82892 ? 647 HOH A O    1 
HETATM 2982 O  O    . HOH E 4 .   ? 32.52108 64.63848 5.18612   1.000 24.37733 ? 648 HOH A O    1 
HETATM 2983 O  O    . HOH E 4 .   ? 22.26196 48.33809 14.94198  1.000 35.33192 ? 649 HOH A O    1 
HETATM 2984 O  O    . HOH E 4 .   ? 25.95835 46.20342 -12.63418 1.000 28.28844 ? 650 HOH A O    1 
HETATM 2985 O  O    . HOH E 4 .   ? 52.60967 31.39308 20.70942  1.000 35.90533 ? 651 HOH A O    1 
HETATM 2986 O  O    . HOH E 4 .   ? 61.76610 40.05324 -4.50525  1.000 11.41143 ? 652 HOH A O    1 
HETATM 2987 O  O    . HOH E 4 .   ? 41.08111 40.32901 -1.24175  1.000 10.41614 ? 653 HOH A O    1 
HETATM 2988 O  O    . HOH E 4 .   ? 25.73469 39.99542 0.60614   1.000 9.99206  ? 654 HOH A O    1 
HETATM 2989 O  O    . HOH E 4 .   ? 41.97443 36.64472 -9.59730  1.000 22.50461 ? 655 HOH A O    1 
HETATM 2990 O  O    . HOH E 4 .   ? 67.84297 33.73012 -6.31779  1.000 31.36580 ? 656 HOH A O    1 
HETATM 2991 O  O    . HOH E 4 .   ? 37.839   18.128   10.898    1.000 20.63320 ? 657 HOH A O    1 
HETATM 2992 O  O    . HOH E 4 .   ? 33.28337 45.46078 1.09578   1.000 7.51777  ? 658 HOH A O    1 
HETATM 2993 O  O    . HOH E 4 .   ? 30.22330 63.19038 -12.08129 1.000 17.91561 ? 659 HOH A O    1 
HETATM 2994 O  O    . HOH E 4 .   ? 57.655   13.325   -1.908    1.000 29.84593 ? 660 HOH A O    1 
HETATM 2995 O  O    . HOH E 4 .   ? 58.32331 30.57848 17.56608  1.000 34.49982 ? 661 HOH A O    1 
HETATM 2996 O  O    . HOH E 4 .   ? 49.55676 29.85230 0.90515   1.000 21.56159 ? 662 HOH A O    1 
HETATM 2997 O  O    . HOH E 4 .   ? 60.83470 48.94335 -2.31278  1.000 17.11146 ? 663 HOH A O    1 
HETATM 2998 O  O    . HOH E 4 .   ? 33.52043 43.94937 3.17014   1.000 11.07847 ? 664 HOH A O    1 
HETATM 2999 O  O    . HOH E 4 .   ? 45.14605 43.45331 18.13291  1.000 15.32010 ? 665 HOH A O    1 
HETATM 3000 O  O    . HOH E 4 .   ? 46.14382 28.54769 -1.10351  1.000 21.42179 ? 666 HOH A O    1 
HETATM 3001 O  O    . HOH E 4 .   ? 44.63385 49.31880 21.74980  1.000 34.40962 ? 667 HOH A O    1 
HETATM 3002 O  O    . HOH E 4 .   ? 56.82022 48.38865 -17.94596 1.000 39.56770 ? 668 HOH A O    1 
HETATM 3003 O  O    . HOH E 4 .   ? 56.95549 23.49176 19.33609  1.000 31.11743 ? 669 HOH A O    1 
HETATM 3004 O  O    . HOH E 4 .   ? 67.10772 34.19015 7.77184   1.000 38.20996 ? 670 HOH A O    1 
HETATM 3005 O  O    . HOH E 4 .   ? 51.90478 53.38979 -2.06881  1.000 9.57902  ? 671 HOH A O    1 
HETATM 3006 O  O    . HOH E 4 .   ? 26.32762 46.68292 -17.09707 1.000 24.48512 ? 672 HOH A O    1 
HETATM 3007 O  O    . HOH E 4 .   ? 47.53589 42.00898 -17.15276 1.000 15.39028 ? 673 HOH A O    1 
HETATM 3008 O  O    . HOH E 4 .   ? 30.62819 38.90644 -17.93916 1.000 35.57032 ? 674 HOH A O    1 
HETATM 3009 O  O    . HOH E 4 .   ? 58.41378 44.08164 -14.62381 1.000 21.86024 ? 675 HOH A O    1 
HETATM 3010 O  O    . HOH E 4 .   ? 34.71463 64.39721 -5.54055  1.000 39.19419 ? 676 HOH A O    1 
HETATM 3011 O  O    . HOH E 4 .   ? 44.63112 43.89911 -0.96371  1.000 6.35969  ? 677 HOH A O    1 
HETATM 3012 O  O    . HOH E 4 .   ? 46.40376 35.32866 0.29840   1.000 11.27307 ? 678 HOH A O    1 
HETATM 3013 O  O    . HOH E 4 .   ? 46.09755 27.55702 23.78445  1.000 29.94680 ? 679 HOH A O    1 
HETATM 3014 O  O    . HOH E 4 .   ? 56.38262 40.75463 -10.84421 1.000 33.55618 ? 680 HOH A O    1 
HETATM 3015 O  O    . HOH E 4 .   ? 71.18397 51.41512 2.19111   1.000 15.10076 ? 681 HOH A O    1 
HETATM 3016 O  O    . HOH E 4 .   ? 33.45382 45.55929 -1.77587  1.000 8.47451  ? 682 HOH A O    1 
HETATM 3017 O  O    . HOH E 4 .   ? 46.39336 62.45055 7.03833   1.000 17.06002 ? 683 HOH A O    1 
HETATM 3018 O  O    . HOH E 4 .   ? 36.43884 34.79333 23.10192  1.000 25.88379 ? 684 HOH A O    1 
HETATM 3019 O  O    . HOH E 4 .   ? 36.27396 27.01707 9.96819   1.000 33.74593 ? 685 HOH A O    1 
HETATM 3020 O  O    . HOH E 4 .   ? 37.16486 62.23925 -18.47141 1.000 23.97922 ? 686 HOH A O    1 
HETATM 3021 O  O    . HOH E 4 .   ? 61.42251 25.51127 15.46113  1.000 30.58967 ? 687 HOH A O    1 
HETATM 3022 O  O    . HOH E 4 .   ? 22.486   44.638   5.002     1.000 24.64116 ? 688 HOH A O    1 
HETATM 3023 O  O    . HOH E 4 .   ? 54.62546 58.66807 -6.95078  1.000 19.32461 ? 689 HOH A O    1 
HETATM 3024 O  O    . HOH E 4 .   ? 47.00448 30.43902 1.22186   1.000 27.99755 ? 690 HOH A O    1 
HETATM 3025 O  O    . HOH E 4 .   ? 37.48926 41.78464 -25.41313 1.000 26.97197 ? 691 HOH A O    1 
HETATM 3026 O  O    . HOH E 4 .   ? 63.69527 19.23949 11.87231  1.000 31.75524 ? 692 HOH A O    1 
HETATM 3027 O  O    . HOH E 4 .   ? 48.31752 44.20137 -18.79769 1.000 13.84270 ? 693 HOH A O    1 
HETATM 3028 O  O    . HOH E 4 .   ? 27.01407 36.27146 -4.62617  1.000 28.85165 ? 694 HOH A O    1 
HETATM 3029 O  O    . HOH E 4 .   ? 41.23079 33.02433 1.10765   1.000 30.21153 ? 695 HOH A O    1 
HETATM 3030 O  O    . HOH E 4 .   ? 60.01783 32.60405 8.36057   1.000 24.34003 ? 696 HOH A O    1 
HETATM 3031 O  O    . HOH E 4 .   ? 51.48007 39.00268 16.46658  1.000 33.22029 ? 697 HOH A O    1 
HETATM 3032 O  O    . HOH E 4 .   ? 26.25334 43.08559 -1.36306  1.000 9.46817  ? 698 HOH A O    1 
HETATM 3033 O  O    . HOH E 4 .   ? 35.42472 37.66388 -0.59310  1.000 14.85703 ? 699 HOH A O    1 
HETATM 3034 O  O    . HOH E 4 .   ? 36.14458 26.77238 5.35566   1.000 42.06150 ? 700 HOH A O    1 
HETATM 3035 O  O    . HOH E 4 .   ? 59.22974 49.47728 10.09973  1.000 31.71273 ? 701 HOH A O    1 
HETATM 3036 O  O    . HOH E 4 .   ? 52.96156 27.11858 20.64252  1.000 20.12806 ? 702 HOH A O    1 
HETATM 3037 O  O    . HOH E 4 .   ? 58.19940 34.39792 14.35753  1.000 39.55399 ? 703 HOH A O    1 
HETATM 3038 O  O    . HOH E 4 .   ? 53.12195 18.73376 6.34477   1.000 14.38422 ? 704 HOH A O    1 
HETATM 3039 O  O    . HOH E 4 .   ? 40.44951 36.86948 -11.59904 1.000 30.55122 ? 705 HOH A O    1 
HETATM 3040 O  O    . HOH E 4 .   ? 57.93999 26.64581 -7.90250  1.000 31.65174 ? 706 HOH A O    1 
HETATM 3041 O  O    . HOH E 4 .   ? 25.12707 60.42238 12.09147  1.000 31.86554 ? 707 HOH A O    1 
HETATM 3042 O  O    . HOH E 4 .   ? 25.95288 50.54040 -16.67564 1.000 22.08530 ? 708 HOH A O    1 
HETATM 3043 O  O    . HOH E 4 .   ? 50.05214 47.36499 -17.31742 1.000 15.27692 ? 709 HOH A O    1 
HETATM 3044 O  O    . HOH E 4 .   ? 47.391   66.227   -4.445    1.000 40.10757 ? 710 HOH A O    1 
HETATM 3045 O  O    . HOH E 4 .   ? 24.30269 59.06005 -12.86646 1.000 28.74783 ? 711 HOH A O    1 
HETATM 3046 O  O    . HOH E 4 .   ? 47.71027 49.78488 -20.85408 1.000 28.72797 ? 712 HOH A O    1 
HETATM 3047 O  O    . HOH E 4 .   ? 59.92321 54.03583 -11.21998 1.000 33.41226 ? 713 HOH A O    1 
HETATM 3048 O  O    . HOH E 4 .   ? 41.75826 52.67590 21.89081  1.000 22.85081 ? 714 HOH A O    1 
HETATM 3049 O  O    . HOH E 4 .   ? 67.76063 53.00130 -4.28487  1.000 34.02003 ? 715 HOH A O    1 
HETATM 3050 O  O    . HOH E 4 .   ? 43.43147 60.95721 -11.60206 1.000 40.73818 ? 716 HOH A O    1 
HETATM 3051 O  O    . HOH E 4 .   ? 57.04308 17.39122 -1.06891  1.000 40.22077 ? 717 HOH A O    1 
HETATM 3052 O  O    . HOH E 4 .   ? 16.12958 55.69309 6.03115   1.000 23.52020 ? 718 HOH A O    1 
HETATM 3053 O  O    . HOH E 4 .   ? 30.42682 53.96457 19.64656  1.000 12.40218 ? 719 HOH A O    1 
HETATM 3054 O  O    . HOH E 4 .   ? 26.81774 47.21309 -6.39879  1.000 34.24775 ? 720 HOH A O    1 
HETATM 3055 O  O    . HOH E 4 .   ? 22.99133 61.20955 8.83269   1.000 28.18134 ? 721 HOH A O    1 
HETATM 3056 O  O    . HOH E 4 .   ? 55.81879 50.91483 10.21789  1.000 24.63176 ? 722 HOH A O    1 
HETATM 3057 O  O    . HOH E 4 .   ? 63.02628 49.06887 -3.79256  1.000 22.43970 ? 723 HOH A O    1 
HETATM 3058 O  O    . HOH E 4 .   ? 51.02343 42.07054 17.42531  1.000 23.05793 ? 724 HOH A O    1 
HETATM 3059 O  O    . HOH E 4 .   ? 44.48606 64.25181 23.00594  1.000 35.89562 ? 725 HOH A O    1 
HETATM 3060 O  O    . HOH E 4 .   ? 43.36189 63.59170 5.34327   1.000 20.82096 ? 726 HOH A O    1 
HETATM 3061 O  O    . HOH E 4 .   ? 27.60385 53.25461 18.00028  1.000 12.20913 ? 727 HOH A O    1 
HETATM 3062 O  O    . HOH E 4 .   ? 30.66971 62.72096 -1.20012  1.000 24.13725 ? 728 HOH A O    1 
HETATM 3063 O  O    . HOH E 4 .   ? 52.96064 39.24373 -9.23654  1.000 15.15705 ? 729 HOH A O    1 
HETATM 3064 O  O    . HOH E 4 .   ? 69.33964 33.99164 1.33241   1.000 36.37989 ? 730 HOH A O    1 
HETATM 3065 O  O    . HOH E 4 .   ? 61.93964 54.19956 0.43442   1.000 16.57135 ? 731 HOH A O    1 
HETATM 3066 O  O    . HOH E 4 .   ? 35.52827 37.13714 -13.93825 1.000 26.08043 ? 732 HOH A O    1 
HETATM 3067 O  O    . HOH E 4 .   ? 31.69405 34.73829 -12.38023 1.000 42.55653 ? 733 HOH A O    1 
HETATM 3068 O  O    . HOH E 4 .   ? 53.80385 57.90229 -9.85815  1.000 25.63071 ? 734 HOH A O    1 
HETATM 3069 O  O    . HOH E 4 .   ? 69.02482 32.01818 4.05930   1.000 29.15506 ? 735 HOH A O    1 
HETATM 3070 O  O    . HOH E 4 .   ? 50.88399 33.94201 -6.37992  1.000 25.28232 ? 736 HOH A O    1 
HETATM 3071 O  O    . HOH E 4 .   ? 38.58883 30.32348 11.99591  1.000 25.57749 ? 737 HOH A O    1 
HETATM 3072 O  O    . HOH E 4 .   ? 37.12311 26.16560 2.83769   1.000 33.71804 ? 738 HOH A O    1 
HETATM 3073 O  O    . HOH E 4 .   ? 59.38269 56.47690 -1.51401  1.000 14.03700 ? 739 HOH A O    1 
HETATM 3074 O  O    . HOH E 4 .   ? 66.63795 22.92122 9.84434   1.000 26.14339 ? 740 HOH A O    1 
HETATM 3075 O  O    . HOH E 4 .   ? 31.39916 33.66415 15.43351  1.000 32.48575 ? 741 HOH A O    1 
HETATM 3076 O  O    . HOH E 4 .   ? 51.21796 55.68866 -3.48191  1.000 10.04070 ? 742 HOH A O    1 
HETATM 3077 O  O    . HOH E 4 .   ? 30.61996 35.19378 -2.69270  1.000 47.61724 ? 743 HOH A O    1 
HETATM 3078 O  O    . HOH E 4 .   ? 48.55912 40.29106 -15.11879 1.000 14.70250 ? 744 HOH A O    1 
HETATM 3079 O  O    . HOH E 4 .   ? 53.96354 55.97614 4.99539   1.000 17.08542 ? 745 HOH A O    1 
HETATM 3080 O  O    . HOH E 4 .   ? 53.27979 45.49594 18.71373  1.000 36.04109 ? 746 HOH A O    1 
HETATM 3081 O  O    . HOH E 4 .   ? 51.38373 28.38011 -1.44268  1.000 29.78088 ? 747 HOH A O    1 
HETATM 3082 O  O    . HOH E 4 .   ? 37.97824 58.68559 -7.89563  1.000 8.01365  ? 748 HOH A O    1 
HETATM 3083 O  O    . HOH E 4 .   ? 23.14558 51.26234 -4.75328  1.000 21.35919 ? 749 HOH A O    1 
HETATM 3084 O  O    . HOH E 4 .   ? 55.85560 10.26111 13.46718  1.000 36.69158 ? 750 HOH A O    1 
HETATM 3085 O  O    . HOH E 4 .   ? 67.07204 39.06297 5.54265   1.000 26.48989 ? 751 HOH A O    1 
HETATM 3086 O  O    . HOH E 4 .   ? 57.46923 33.89252 16.60338  1.000 41.35983 ? 752 HOH A O    1 
HETATM 3087 O  O    . HOH E 4 .   ? 60.34804 16.59126 12.03530  1.000 22.47985 ? 753 HOH A O    1 
HETATM 3088 O  O    . HOH E 4 .   ? 46.33147 32.90904 -0.51182  1.000 33.13128 ? 754 HOH A O    1 
HETATM 3089 O  O    . HOH E 4 .   ? 36.02964 37.81325 2.71071   1.000 5.07789  ? 755 HOH A O    1 
HETATM 3090 O  O    . HOH E 4 .   ? 24.22073 43.09562 -5.65737  1.000 18.02772 ? 756 HOH A O    1 
HETATM 3091 O  O    . HOH E 4 .   ? 65.30593 25.43820 2.26586   1.000 20.21664 ? 757 HOH A O    1 
HETATM 3092 O  O    . HOH E 4 .   ? 51.87276 36.39360 -8.07628  1.000 14.25848 ? 758 HOH A O    1 
HETATM 3093 O  O    . HOH E 4 .   ? 44.02180 23.41535 24.71634  1.000 36.12717 ? 759 HOH A O    1 
HETATM 3094 O  O    . HOH E 4 .   ? 24.98612 60.20418 9.47259   1.000 17.05380 ? 760 HOH A O    1 
HETATM 3095 O  O    . HOH E 4 .   ? 46.92794 38.01244 -15.47076 1.000 28.48336 ? 761 HOH A O    1 
HETATM 3096 O  O    . HOH E 4 .   ? 38.53112 30.68948 15.12924  1.000 33.64755 ? 762 HOH A O    1 
HETATM 3097 O  O    . HOH E 4 .   ? 24.89955 62.29048 -5.81564  1.000 11.78421 ? 763 HOH A O    1 
HETATM 3098 O  O    . HOH E 4 .   ? 22.16100 42.20761 -9.36566  1.000 39.13999 ? 764 HOH A O    1 
HETATM 3099 O  O    . HOH E 4 .   ? 22.26830 44.23513 -7.74865  1.000 28.20656 ? 765 HOH A O    1 
HETATM 3100 O  O    . HOH E 4 .   ? 25.68698 51.32615 -5.52040  1.000 11.11498 ? 766 HOH A O    1 
HETATM 3101 O  O    . HOH E 4 .   ? 43.15600 30.44482 -2.34077  1.000 33.49515 ? 767 HOH A O    1 
HETATM 3102 O  O    . HOH E 4 .   ? 68.19573 31.87435 6.69263   1.000 45.78335 ? 768 HOH A O    1 
HETATM 3103 O  O    . HOH E 4 .   ? 46.79884 65.72671 -22.59084 1.000 36.32094 ? 769 HOH A O    1 
HETATM 3104 O  O    . HOH E 4 .   ? 40.70194 59.64030 -8.57931  1.000 13.82249 ? 770 HOH A O    1 
HETATM 3105 O  O    . HOH E 4 .   ? 37.66416 64.74508 8.44606   1.000 26.15358 ? 771 HOH A O    1 
HETATM 3106 O  O    . HOH E 4 .   ? 52.33439 61.70974 -19.06256 1.000 37.37749 ? 772 HOH A O    1 
HETATM 3107 O  O    . HOH E 4 .   ? 51.54635 13.99002 15.16593  1.000 27.27378 ? 773 HOH A O    1 
HETATM 3108 O  O    . HOH E 4 .   ? 63.01900 24.90167 0.86716   1.000 38.22004 ? 774 HOH A O    1 
HETATM 3109 O  O    . HOH E 4 .   ? 53.34171 42.87417 17.99396  1.000 32.42036 ? 775 HOH A O    1 
HETATM 3110 O  O    . HOH E 4 .   ? 51.29893 18.77784 -4.95940  1.000 40.06003 ? 776 HOH A O    1 
HETATM 3111 O  O    . HOH E 4 .   ? 29.82152 65.48624 5.57835   1.000 44.22562 ? 777 HOH A O    1 
HETATM 3112 O  O    . HOH E 4 .   ? 58.41649 52.99174 -15.31548 1.000 30.47286 ? 778 HOH A O    1 
HETATM 3113 O  O    . HOH E 4 .   ? 44.866   47.038   21.022    1.000 41.17960 ? 779 HOH A O    1 
HETATM 3114 O  O    . HOH E 4 .   ? 43.60721 63.55091 0.05017   1.000 28.05955 ? 780 HOH A O    1 
HETATM 3115 O  O    . HOH E 4 .   ? 48.553   64.175   3.205     1.000 31.62662 ? 781 HOH A O    1 
HETATM 3116 O  O    . HOH E 4 .   ? 41.88072 29.46198 2.52966   1.000 33.27846 ? 782 HOH A O    1 
HETATM 3117 O  O    . HOH E 4 .   ? 42.922   26.832   25.433    1.000 33.66615 ? 783 HOH A O    1 
HETATM 3118 O  O    . HOH E 4 .   ? 48.907   60.343   21.359    1.000 34.01894 ? 784 HOH A O    1 
HETATM 3119 O  O    . HOH E 4 .   ? 68.70544 30.86908 -5.34638  1.000 28.58359 ? 785 HOH A O    1 
HETATM 3120 O  O    . HOH E 4 .   ? 48.15568 49.01588 -18.64363 1.000 25.65339 ? 786 HOH A O    1 
HETATM 3121 O  O    . HOH E 4 .   ? 66.09032 45.33164 -6.18377  1.000 41.18608 ? 787 HOH A O    1 
HETATM 3122 O  O    . HOH E 4 .   ? 31.07397 56.41045 19.73840  1.000 34.21737 ? 788 HOH A O    1 
HETATM 3123 O  O    . HOH E 4 .   ? 59.35559 14.11958 12.50783  1.000 27.91577 ? 789 HOH A O    1 
HETATM 3124 O  O    . HOH E 4 .   ? 52.69734 51.64822 -17.17205 1.000 28.88431 ? 790 HOH A O    1 
HETATM 3125 O  O    . HOH E 4 .   ? 47.52304 49.10297 21.62021  1.000 43.47539 ? 791 HOH A O    1 
HETATM 3126 O  O    . HOH E 4 .   ? 62.50067 16.86861 13.22510  1.000 33.38351 ? 792 HOH A O    1 
HETATM 3127 O  O    . HOH E 4 .   ? 22.48642 58.64519 14.64260  1.000 24.86998 ? 793 HOH A O    1 
HETATM 3128 O  O    . HOH E 4 .   ? 71.845   44.500   -3.133    1.000 10.75385 ? 794 HOH A O    1 
HETATM 3129 O  O    . HOH E 4 .   ? 46.157   27.246   26.110    1.000 22.84907 ? 795 HOH A O    1 
HETATM 3130 O  O    . HOH E 4 .   ? 23.47684 48.53238 -6.17229  1.000 26.22295 ? 796 HOH A O    1 
HETATM 3131 O  O    . HOH E 4 .   ? 63.25892 38.21608 -6.29255  1.000 29.63908 ? 797 HOH A O    1 
HETATM 3132 O  O    . HOH E 4 .   ? 38.02249 61.02457 -5.83125  1.000 27.80542 ? 798 HOH A O    1 
HETATM 3133 O  O    . HOH E 4 .   ? 44.53362 64.17409 2.94613   1.000 30.20725 ? 799 HOH A O    1 
HETATM 3134 O  O    . HOH E 4 .   ? 69.10653 46.51040 -5.47863  1.000 28.01287 ? 800 HOH A O    1 
HETATM 3135 O  O    . HOH E 4 .   ? 59.57647 33.92178 11.16678  1.000 26.08040 ? 801 HOH A O    1 
HETATM 3136 O  O    . HOH E 4 .   ? 29.30319 36.68998 -1.04646  1.000 35.01362 ? 802 HOH A O    1 
HETATM 3137 O  O    . HOH E 4 .   ? 35.06847 63.98309 -8.76892  1.000 39.42138 ? 803 HOH A O    1 
HETATM 3138 O  O    . HOH E 4 .   ? 50.47405 53.36898 0.29559   1.000 9.51294  ? 804 HOH A O    1 
HETATM 3139 O  O    . HOH E 4 .   ? 63.509   53.771   2.293     1.000 28.84876 ? 805 HOH A O    1 
HETATM 3140 O  O    . HOH E 4 .   ? 68.45161 41.29583 5.56185   1.000 26.81943 ? 806 HOH A O    1 
HETATM 3141 O  O    . HOH E 4 .   ? 20.44987 56.65199 14.53971  1.000 35.54041 ? 807 HOH A O    1 
HETATM 3142 O  O    . HOH E 4 .   ? 41.16469 60.14341 -11.17654 1.000 31.51071 ? 808 HOH A O    1 
HETATM 3143 O  O    . HOH E 4 .   ? 61.87484 22.70703 17.29243  1.000 35.19703 ? 809 HOH A O    1 
HETATM 3144 O  O    . HOH E 4 .   ? 65.48501 37.94769 -7.86318  1.000 38.77055 ? 810 HOH A O    1 
HETATM 3145 O  O    . HOH E 4 .   ? 68.195   50.727   -7.207    1.000 41.94993 ? 811 HOH A O    1 
HETATM 3146 O  O    . HOH E 4 .   ? 37.11197 48.47744 21.64810  1.000 38.03205 ? 812 HOH A O    1 
HETATM 3147 O  O    . HOH E 4 .   ? 45.97027 63.36323 -17.87810 1.000 21.61293 ? 813 HOH A O    1 
HETATM 3148 O  O    . HOH E 4 .   ? 57.98014 44.74670 -16.89779 1.000 38.67487 ? 814 HOH A O    1 
HETATM 3149 O  O    . HOH E 4 .   ? 56.63026 36.77105 17.17170  1.000 33.19707 ? 815 HOH A O    1 
HETATM 3150 O  O    . HOH E 4 .   ? 56.99196 59.67435 -6.14341  1.000 34.57152 ? 816 HOH A O    1 
HETATM 3151 O  O    . HOH E 4 .   ? 24.99452 49.25018 -8.86679  1.000 32.67684 ? 817 HOH A O    1 
HETATM 3152 O  O    . HOH E 4 .   ? 40.39976 62.91109 -14.10624 1.000 35.00350 ? 818 HOH A O    1 
HETATM 3153 O  O    . HOH E 4 .   ? 44.10705 63.72235 7.52981   1.000 17.31432 ? 819 HOH A O    1 
HETATM 3154 O  O    . HOH E 4 .   ? 58.24195 52.62346 10.62065  1.000 33.40325 ? 820 HOH A O    1 
HETATM 3155 O  O    . HOH E 4 .   ? 28.46351 42.30521 -17.04029 1.000 24.29924 ? 821 HOH A O    1 
HETATM 3156 O  O    . HOH E 4 .   ? 46.72099 63.24535 4.25084   1.000 34.71171 ? 822 HOH A O    1 
HETATM 3157 O  O    . HOH E 4 .   ? 51.48660 16.59857 5.51229   1.000 18.39786 ? 823 HOH A O    1 
HETATM 3158 O  O    . HOH E 4 .   ? 51.51124 46.05507 20.04538  1.000 37.19721 ? 824 HOH A O    1 
HETATM 3159 O  O    . HOH E 4 .   ? 25.10198 45.33869 -18.93634 1.000 39.77804 ? 825 HOH A O    1 
HETATM 3160 O  O    . HOH E 4 .   ? 41.38837 64.04369 -18.07664 1.000 34.36045 ? 826 HOH A O    1 
HETATM 3161 O  O    . HOH E 4 .   ? 36.64751 62.14461 -8.38811  1.000 34.05058 ? 827 HOH A O    1 
HETATM 3162 O  O    . HOH E 4 .   ? 40.48513 51.47973 23.59969  1.000 34.37155 ? 828 HOH A O    1 
HETATM 3163 O  O    . HOH E 4 .   ? 24.54131 56.21932 18.45516  1.000 28.88500 ? 829 HOH A O    1 
HETATM 3164 O  O    . HOH E 4 .   ? 38.28235 62.33366 -10.49146 1.000 31.44697 ? 830 HOH A O    1 
HETATM 3165 O  O    . HOH E 4 .   ? 58.63967 49.65848 12.88608  1.000 34.99577 ? 831 HOH A O    1 
HETATM 3166 O  O    . HOH E 4 .   ? 59.73491 23.27511 0.95870   1.000 33.56098 ? 832 HOH A O    1 
HETATM 3167 O  O    . HOH E 4 .   ? 14.54866 54.90009 4.38210   1.000 37.24863 ? 833 HOH A O    1 
HETATM 3168 O  O    . HOH E 4 .   ? 61.91230 12.80632 12.11479  1.000 32.22810 ? 834 HOH A O    1 
HETATM 3169 O  O    . HOH E 4 .   ? 42.27947 66.62666 -19.12684 1.000 44.53863 ? 835 HOH A O    1 
HETATM 3170 O  O    . HOH E 4 .   ? 25.74779 42.99728 -19.08057 1.000 30.47928 ? 836 HOH A O    1 
HETATM 3171 O  O    . HOH E 4 .   ? 39.30477 48.97735 23.30548  1.000 28.20540 ? 837 HOH A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLY A 21  ? 0.49611 0.51612 0.53074 -0.02086 -0.01628 0.00471  7   GLY A N   
2    C CA  . GLY A 21  ? 0.39679 0.41790 0.43576 -0.02065 -0.01604 0.00578  7   GLY A CA  
3    C C   . GLY A 21  ? 0.36717 0.38799 0.40874 -0.01774 -0.01434 0.00755  7   GLY A C   
4    O O   . GLY A 21  ? 0.39380 0.41313 0.43355 -0.01583 -0.01304 0.00755  7   GLY A O   
5    N N   . SER A 22  ? 0.19879 0.22105 0.24451 -0.01754 -0.01430 0.00901  8   SER A N   
6    C CA  . SER A 22  ? 0.19696 0.21926 0.24549 -0.01496 -0.01275 0.01083  8   SER A CA  
7    C C   . SER A 22  ? 0.19010 0.20994 0.23777 -0.01359 -0.01072 0.00928  8   SER A C   
8    O O   . SER A 22  ? 0.19351 0.21212 0.24029 -0.01472 -0.01055 0.00718  8   SER A O   
9    C CB  . SER A 22  ? 0.19371 0.21840 0.24688 -0.01540 -0.01332 0.01265  8   SER A CB  
10   O OG  . SER A 22  ? 0.19695 0.22161 0.25289 -0.01308 -0.01170 0.01417  8   SER A OG  
11   N N   . ARG A 23  ? 0.23838 0.25752 0.28633 -0.01113 -0.00914 0.01041  9   ARG A N   
12   C CA  . ARG A 23  ? 0.16292 0.18015 0.21047 -0.00963 -0.00716 0.00948  9   ARG A CA  
13   C C   . ARG A 23  ? 0.18298 0.20084 0.23369 -0.00753 -0.00584 0.01169  9   ARG A C   
14   O O   . ARG A 23  ? 0.16886 0.18798 0.22079 -0.00667 -0.00604 0.01371  9   ARG A O   
15   C CB  . ARG A 23  ? 0.19636 0.21168 0.23966 -0.00877 -0.00622 0.00816  9   ARG A CB  
16   C CG  . ARG A 23  ? 0.43064 0.44519 0.47026 -0.01059 -0.00724 0.00588  9   ARG A CG  
17   C CD  . ARG A 23  ? 0.63430 0.64726 0.66990 -0.00961 -0.00625 0.00494  9   ARG A CD  
18   N NE  . ARG A 23  ? 0.45072 0.46246 0.48637 -0.00784 -0.00424 0.00465  9   ARG A NE  
19   C CZ  . ARG A 23  ? 0.41115 0.42168 0.44511 -0.00797 -0.00348 0.00261  9   ARG A CZ  
20   N NH1 . ARG A 23  ? 0.37774 0.38793 0.40986 -0.00972 -0.00440 0.00051  9   ARG A NH1 
21   N NH2 . ARG A 23  ? 0.42782 0.43754 0.46195 -0.00630 -0.00170 0.00270  9   ARG A NH2 
22   N N   . ALA A 24  ? 0.10864 0.12558 0.16064 -0.00670 -0.00443 0.01130  10  ALA A N   
23   C CA  . ALA A 24  ? 0.13371 0.15091 0.18813 -0.00467 -0.00287 0.01308  10  ALA A CA  
24   C C   . ALA A 24  ? 0.13855 0.15475 0.19047 -0.00296 -0.00166 0.01350  10  ALA A C   
25   O O   . ALA A 24  ? 0.14735 0.16195 0.19547 -0.00299 -0.00129 0.01187  10  ALA A O   
26   C CB  . ALA A 24  ? 0.09705 0.11311 0.15246 -0.00427 -0.00160 0.01226  10  ALA A CB  
27   N N   . ARG A 25  ? 0.12793 0.14510 0.18199 -0.00151 -0.00098 0.01568  11  ARG A N   
28   C CA  . ARG A 25  ? 0.13247 0.14854 0.18447 0.00019  0.00044  0.01626  11  ARG A CA  
29   C C   . ARG A 25  ? 0.13376 0.14827 0.18474 0.00139  0.00251  0.01559  11  ARG A C   
30   O O   . ARG A 25  ? 0.16570 0.17889 0.21395 0.00244  0.00377  0.01546  11  ARG A O   
31   C CB  . ARG A 25  ? 0.16025 0.17777 0.21529 0.00150  0.00080  0.01885  11  ARG A CB  
32   C CG  . ARG A 25  ? 0.18847 0.20757 0.24420 0.00085  -0.00095 0.02004  11  ARG A CG  
33   C CD  . ARG A 25  ? 0.16505 0.18478 0.22249 0.00272  -0.00003 0.02238  11  ARG A CD  
34   N NE  . ARG A 25  ? 0.12899 0.15072 0.19126 0.00350  0.00047  0.02422  11  ARG A NE  
35   C CZ  . ARG A 25  ? 0.15859 0.17987 0.22225 0.00518  0.00254  0.02504  11  ARG A CZ  
36   N NH1 . ARG A 25  ? 0.12929 0.14817 0.18987 0.00624  0.00435  0.02418  11  ARG A NH1 
37   N NH2 . ARG A 25  ? 0.07676 0.10016 0.14492 0.00572  0.00281  0.02676  11  ARG A NH2 
38   N N   . VAL A 26  ? 0.08952 0.10420 0.14262 0.00122  0.00290  0.01527  12  VAL A N   
39   C CA  . VAL A 26  ? 0.07461 0.08813 0.12717 0.00229  0.00476  0.01486  12  VAL A CA  
40   C C   . VAL A 26  ? 0.11335 0.12628 0.16586 0.00128  0.00439  0.01320  12  VAL A C   
41   O O   . VAL A 26  ? 0.11533 0.12896 0.16960 -0.00007 0.00301  0.01291  12  VAL A O   
42   C CB  . VAL A 26  ? 0.10407 0.11844 0.16005 0.00364  0.00613  0.01683  12  VAL A CB  
43   C CG1 . VAL A 26  ? 0.09497 0.10950 0.15065 0.00492  0.00696  0.01832  12  VAL A CG1 
44   C CG2 . VAL A 26  ? 0.12188 0.13799 0.18219 0.00290  0.00513  0.01786  12  VAL A CG2 
45   N N   . TYR A 27  ? 0.11667 0.12829 0.16706 0.00189  0.00566  0.01212  13  TYR A N   
46   C CA  . TYR A 27  ? 0.07859 0.08949 0.12916 0.00136  0.00571  0.01076  13  TYR A CA  
47   C C   . TYR A 27  ? 0.08716 0.09776 0.13647 -0.00035 0.00409  0.00897  13  TYR A C   
48   O O   . TYR A 27  ? 0.12739 0.13759 0.17792 -0.00112 0.00375  0.00810  13  TYR A O   
49   C CB  . TYR A 27  ? 0.07362 0.08507 0.12817 0.00165  0.00619  0.01196  13  TYR A CB  
50   C CG  . TYR A 27  ? 0.12714 0.13911 0.18327 0.00317  0.00776  0.01383  13  TYR A CG  
51   C CD1 . TYR A 27  ? 0.22124 0.23243 0.27520 0.00435  0.00941  0.01373  13  TYR A CD1 
52   C CD2 . TYR A 27  ? 0.13656 0.14993 0.19636 0.00332  0.00764  0.01565  13  TYR A CD2 
53   C CE1 . TYR A 27  ? 0.11141 0.12305 0.16675 0.00558  0.01095  0.01538  13  TYR A CE1 
54   C CE2 . TYR A 27  ? 0.21463 0.22851 0.27595 0.00465  0.00917  0.01728  13  TYR A CE2 
55   C CZ  . TYR A 27  ? 0.22398 0.23690 0.28302 0.00574  0.01084  0.01711  13  TYR A CZ  
56   O OH  . TYR A 27  ? 0.26843 0.28184 0.32891 0.00691  0.01243  0.01867  13  TYR A OH  
57   N N   . ALA A 28  ? 0.12130 0.13195 0.16803 -0.00101 0.00313  0.00837  14  ALA A N   
58   C CA  . ALA A 28  ? 0.11195 0.12245 0.15740 -0.00283 0.00156  0.00669  14  ALA A CA  
59   C C   . ALA A 28  ? 0.20348 0.21263 0.24653 -0.00307 0.00203  0.00447  14  ALA A C   
60   O O   . ALA A 28  ? 0.22814 0.23693 0.27130 -0.00443 0.00118  0.00304  14  ALA A O   
61   C CB  . ALA A 28  ? 0.14524 0.15618 0.18842 -0.00350 0.00042  0.00671  14  ALA A CB  
62   N N   . GLU A 29  ? 0.15292 0.16140 0.19388 -0.00181 0.00344  0.00418  15  GLU A N   
63   C CA  . GLU A 29  ? 0.15767 0.16520 0.19616 -0.00191 0.00391  0.00216  15  GLU A CA  
64   C C   . GLU A 29  ? 0.16239 0.16948 0.20244 -0.00078 0.00528  0.00234  15  GLU A C   
65   O O   . GLU A 29  ? 0.21693 0.22344 0.25515 -0.00056 0.00586  0.00092  15  GLU A O   
66   C CB  . GLU A 29  ? 0.24359 0.25085 0.27792 -0.00162 0.00432  0.00145  15  GLU A CB  
67   C CG  . GLU A 29  ? 0.32585 0.33338 0.35830 -0.00272 0.00297  0.00131  15  GLU A CG  
68   C CD  . GLU A 29  ? 0.64382 0.65126 0.67534 -0.00460 0.00146  -0.00054 15  GLU A CD  
69   O OE1 . GLU A 29  ? 0.78157 0.78851 0.81353 -0.00496 0.00162  -0.00195 15  GLU A OE1 
70   O OE2 . GLU A 29  ? 0.70192 0.70973 0.73222 -0.00573 0.00015  -0.00056 15  GLU A OE2 
71   N N   . VAL A 30  ? 0.13852 0.14599 0.18196 -0.00007 0.00580  0.00409  16  VAL A N   
72   C CA  . VAL A 30  ? 0.14510 0.15222 0.18974 0.00113  0.00722  0.00455  16  VAL A CA  
73   C C   . VAL A 30  ? 0.16705 0.17322 0.21198 0.00068  0.00712  0.00300  16  VAL A C   
74   O O   . VAL A 30  ? 0.17028 0.17607 0.21433 0.00158  0.00817  0.00253  16  VAL A O   
75   C CB  . VAL A 30  ? 0.30753 0.31527 0.35578 0.00183  0.00778  0.00672  16  VAL A CB  
76   C CG1 . VAL A 30  ? 0.40040 0.40885 0.44799 0.00276  0.00855  0.00819  16  VAL A CG1 
77   C CG2 . VAL A 30  ? 0.24036 0.24847 0.29144 0.00065  0.00651  0.00712  16  VAL A CG2 
78   N N   . ASN A 31  ? 0.13246 0.13825 0.17855 -0.00074 0.00591  0.00216  17  ASN A N   
79   C CA  . ASN A 31  ? 0.06839 0.07295 0.11488 -0.00115 0.00598  0.00067  17  ASN A CA  
80   C C   . ASN A 31  ? 0.08535 0.08945 0.12841 -0.00132 0.00602  -0.00148 17  ASN A C   
81   O O   . ASN A 31  ? 0.10491 0.10831 0.14772 -0.00059 0.00690  -0.00229 17  ASN A O   
82   C CB  . ASN A 31  ? 0.08276 0.08693 0.13144 -0.00276 0.00483  0.00039  17  ASN A CB  
83   C CG  . ASN A 31  ? 0.13466 0.13916 0.18703 -0.00244 0.00510  0.00237  17  ASN A CG  
84   O OD1 . ASN A 31  ? 0.21367 0.21801 0.26719 -0.00103 0.00633  0.00343  17  ASN A OD1 
85   N ND2 . ASN A 31  ? 0.08419 0.08934 0.13840 -0.00379 0.00396  0.00296  17  ASN A ND2 
86   N N   . SER A 32  ? 0.10709 0.11165 0.14751 -0.00227 0.00511  -0.00235 18  SER A N   
87   C CA  . SER A 32  ? 0.08975 0.09404 0.12676 -0.00255 0.00516  -0.00442 18  SER A CA  
88   C C   . SER A 32  ? 0.11164 0.11634 0.14686 -0.00097 0.00652  -0.00420 18  SER A C   
89   O O   . SER A 32  ? 0.13375 0.13828 0.16692 -0.00086 0.00691  -0.00581 18  SER A O   
90   C CB  . SER A 32  ? 0.17740 0.18214 0.21188 -0.00399 0.00385  -0.00522 18  SER A CB  
91   O OG  . SER A 32  ? 0.31127 0.31684 0.34478 -0.00338 0.00394  -0.00373 18  SER A OG  
92   N N   . LEU A 33  ? 0.10001 0.10535 0.13592 0.00016  0.00730  -0.00228 19  LEU A N   
93   C CA  . LEU A 33  ? 0.08695 0.09280 0.12112 0.00147  0.00864  -0.00194 19  LEU A CA  
94   C C   . LEU A 33  ? 0.13367 0.13936 0.16994 0.00266  0.00974  -0.00139 19  LEU A C   
95   O O   . LEU A 33  ? 0.12284 0.12916 0.15770 0.00366  0.01083  -0.00120 19  LEU A O   
96   C CB  . LEU A 33  ? 0.07790 0.08438 0.11151 0.00205  0.00913  -0.00022 19  LEU A CB  
97   C CG  . LEU A 33  ? 0.13703 0.14360 0.16805 0.00113  0.00824  -0.00060 19  LEU A CG  
98   C CD1 . LEU A 33  ? 0.15638 0.16327 0.18695 0.00192  0.00903  0.00113  19  LEU A CD1 
99   C CD2 . LEU A 33  ? 0.11928 0.12581 0.14636 0.00050  0.00805  -0.00264 19  LEU A CD2 
100  N N   . ARG A 34  ? 0.10984 0.11474 0.14929 0.00249  0.00949  -0.00112 20  ARG A N   
101  C CA  . ARG A 34  ? 0.08836 0.09286 0.12993 0.00357  0.01046  -0.00056 20  ARG A CA  
102  C C   . ARG A 34  ? 0.10670 0.11022 0.14803 0.00331  0.01036  -0.00248 20  ARG A C   
103  O O   . ARG A 34  ? 0.13760 0.14063 0.17758 0.00206  0.00944  -0.00423 20  ARG A O   
104  C CB  . ARG A 34  ? 0.10336 0.10740 0.14867 0.00358  0.01041  0.00110  20  ARG A CB  
105  C CG  . ARG A 34  ? 0.11721 0.12229 0.16323 0.00410  0.01082  0.00319  20  ARG A CG  
106  C CD  . ARG A 34  ? 0.15698 0.16180 0.20679 0.00400  0.01075  0.00474  20  ARG A CD  
107  N NE  . ARG A 34  ? 0.21945 0.22532 0.27007 0.00455  0.01127  0.00666  20  ARG A NE  
108  C CZ  . ARG A 34  ? 0.33460 0.34099 0.38675 0.00395  0.01058  0.00758  20  ARG A CZ  
109  N NH1 . ARG A 34  ? 0.27518 0.28128 0.32820 0.00263  0.00923  0.00687  20  ARG A NH1 
110  N NH2 . ARG A 34  ? 0.27896 0.28626 0.33182 0.00465  0.01131  0.00929  20  ARG A NH2 
111  N N   . SER A 35  ? 0.08766 0.09091 0.13027 0.00452  0.01136  -0.00211 21  SER A N   
112  C CA  . SER A 35  ? 0.09814 0.10022 0.14111 0.00452  0.01148  -0.00374 21  SER A CA  
113  C C   . SER A 35  ? 0.10404 0.10445 0.14872 0.00310  0.01057  -0.00456 21  SER A C   
114  O O   . SER A 35  ? 0.11008 0.11016 0.15701 0.00265  0.01021  -0.00324 21  SER A O   
115  C CB  . SER A 35  ? 0.11471 0.11657 0.15967 0.00611  0.01266  -0.00262 21  SER A CB  
116  O OG  . SER A 35  ? 0.09129 0.09493 0.13483 0.00728  0.01350  -0.00160 21  SER A OG  
117  N N   . ARG A 36  ? 0.11974 0.11917 0.16337 0.00233  0.01027  -0.00676 22  ARG A N   
118  C CA  . ARG A 36  ? 0.10517 0.10291 0.15016 0.00078  0.00952  -0.00774 22  ARG A CA  
119  C C   . ARG A 36  ? 0.11454 0.11083 0.16302 0.00120  0.01002  -0.00644 22  ARG A C   
120  O O   . ARG A 36  ? 0.09258 0.08814 0.14270 -0.00009 0.00931  -0.00609 22  ARG A O   
121  C CB  . ARG A 36  ? 0.10239 0.09913 0.14573 0.00006  0.00948  -0.01039 22  ARG A CB  
122  C CG  . ARG A 36  ? 0.10286 0.09763 0.14747 -0.00165 0.00890  -0.01154 22  ARG A CG  
123  C CD  . ARG A 36  ? 0.13159 0.12535 0.17438 -0.00242 0.00899  -0.01426 22  ARG A CD  
124  N NE  . ARG A 36  ? 0.23778 0.22938 0.28177 -0.00410 0.00866  -0.01543 22  ARG A NE  
125  C CZ  . ARG A 36  ? 0.59477 0.58529 0.63718 -0.00547 0.00851  -0.01795 22  ARG A CZ  
126  N NH1 . ARG A 36  ? 0.46557 0.45702 0.50530 -0.00529 0.00865  -0.01955 22  ARG A NH1 
127  N NH2 . ARG A 36  ? 0.60668 0.59518 0.65013 -0.00719 0.00826  -0.01893 22  ARG A NH2 
128  N N   . GLU A 37  ? 0.08255 0.07856 0.13220 0.00295  0.01122  -0.00559 23  GLU A N   
129  C CA  . GLU A 37  ? 0.08917 0.08360 0.14201 0.00333  0.01173  -0.00436 23  GLU A CA  
130  C C   . GLU A 37  ? 0.09653 0.09169 0.15120 0.00297  0.01134  -0.00223 23  GLU A C   
131  O O   . GLU A 37  ? 0.10210 0.09588 0.15930 0.00257  0.01140  -0.00146 23  GLU A O   
132  C CB  . GLU A 37  ? 0.18321 0.17741 0.23697 0.00537  0.01306  -0.00355 23  GLU A CB  
133  C CG  . GLU A 37  ? 0.30857 0.30505 0.36177 0.00675  0.01358  -0.00170 23  GLU A CG  
134  C CD  . GLU A 37  ? 0.75483 0.75118 0.80940 0.00860  0.01479  -0.00050 23  GLU A CD  
135  O OE1 . GLU A 37  ? 0.51857 0.51280 0.57505 0.00889  0.01522  -0.00076 23  GLU A OE1 
136  O OE2 . GLU A 37  ? 0.86283 0.86118 0.91653 0.00972  0.01533  0.00073  23  GLU A OE2 
137  N N   . TYR A 38  ? 0.08817 0.08539 0.14158 0.00306  0.01099  -0.00132 24  TYR A N   
138  C CA  . TYR A 38  ? 0.11504 0.11313 0.17020 0.00278  0.01069  0.00066  24  TYR A CA  
139  C C   . TYR A 38  ? 0.07548 0.07286 0.13196 0.00089  0.00955  0.00028  24  TYR A C   
140  O O   . TYR A 38  ? 0.09851 0.09561 0.15764 0.00058  0.00953  0.00167  24  TYR A O   
141  C CB  . TYR A 38  ? 0.08710 0.08728 0.14033 0.00316  0.01059  0.00140  24  TYR A CB  
142  C CG  . TYR A 38  ? 0.07358 0.07475 0.12867 0.00304  0.01043  0.00343  24  TYR A CG  
143  C CD1 . TYR A 38  ? 0.07996 0.08162 0.13668 0.00426  0.01147  0.00540  24  TYR A CD1 
144  C CD2 . TYR A 38  ? 0.08781 0.08955 0.14313 0.00169  0.00926  0.00345  24  TYR A CD2 
145  C CE1 . TYR A 38  ? 0.09402 0.09664 0.15256 0.00416  0.01144  0.00721  24  TYR A CE1 
146  C CE2 . TYR A 38  ? 0.08101 0.08386 0.13832 0.00171  0.00919  0.00541  24  TYR A CE2 
147  C CZ  . TYR A 38  ? 0.12224 0.12547 0.18115 0.00295  0.01033  0.00721  24  TYR A CZ  
148  O OH  . TYR A 38  ? 0.11843 0.12281 0.17934 0.00298  0.01037  0.00906  24  TYR A OH  
149  N N   . TRP A 39  ? 0.09625 0.09351 0.15086 -0.00052 0.00858  -0.00157 25  TRP A N   
150  C CA  . TRP A 39  ? 0.08072 0.07780 0.13617 -0.00255 0.00733  -0.00193 25  TRP A CA  
151  C C   . TRP A 39  ? 0.13177 0.12669 0.18732 -0.00391 0.00714  -0.00391 25  TRP A C   
152  O O   . TRP A 39  ? 0.12311 0.11770 0.17967 -0.00576 0.00622  -0.00412 25  TRP A O   
153  C CB  . TRP A 39  ? 0.08926 0.08808 0.14259 -0.00345 0.00619  -0.00224 25  TRP A CB  
154  C CG  . TRP A 39  ? 0.08097 0.07996 0.13085 -0.00327 0.00620  -0.00403 25  TRP A CG  
155  C CD1 . TRP A 39  ? 0.08885 0.08906 0.13668 -0.00200 0.00669  -0.00366 25  TRP A CD1 
156  C CD2 . TRP A 39  ? 0.12693 0.12489 0.17495 -0.00453 0.00574  -0.00648 25  TRP A CD2 
157  N NE1 . TRP A 39  ? 0.09855 0.09863 0.14340 -0.00238 0.00653  -0.00569 25  TRP A NE1 
158  C CE2 . TRP A 39  ? 0.08141 0.08015 0.12636 -0.00388 0.00597  -0.00746 25  TRP A CE2 
159  C CE3 . TRP A 39  ? 0.13112 0.12753 0.17967 -0.00624 0.00525  -0.00801 25  TRP A CE3 
160  C CZ2 . TRP A 39  ? 0.13390 0.13207 0.17641 -0.00484 0.00567  -0.00988 25  TRP A CZ2 
161  C CZ3 . TRP A 39  ? 0.17299 0.16869 0.21906 -0.00720 0.00503  -0.01047 25  TRP A CZ3 
162  C CH2 . TRP A 39  ? 0.18720 0.18385 0.23035 -0.00646 0.00523  -0.01138 25  TRP A CH2 
163  N N   . ASP A 40  ? 0.10002 0.09350 0.15459 -0.00309 0.00803  -0.00533 26  ASP A N   
164  C CA  . ASP A 40  ? 0.16956 0.16072 0.22400 -0.00428 0.00808  -0.00743 26  ASP A CA  
165  C C   . ASP A 40  ? 0.10306 0.09212 0.16038 -0.00403 0.00886  -0.00659 26  ASP A C   
166  O O   . ASP A 40  ? 0.17244 0.15981 0.23029 -0.00276 0.01003  -0.00694 26  ASP A O   
167  C CB  . ASP A 40  ? 0.13536 0.12604 0.18752 -0.00340 0.00877  -0.00932 26  ASP A CB  
168  C CG  . ASP A 40  ? 0.21930 0.20760 0.27095 -0.00471 0.00889  -0.01179 26  ASP A CG  
169  O OD1 . ASP A 40  ? 0.20181 0.18883 0.25451 -0.00658 0.00834  -0.01218 26  ASP A OD1 
170  O OD2 . ASP A 40  ? 0.20113 0.18887 0.25128 -0.00392 0.00963  -0.01339 26  ASP A OD2 
171  N N   . TYR A 41  ? 0.10555 0.09487 0.16482 -0.00527 0.00819  -0.00533 27  TYR A N   
172  C CA  . TYR A 41  ? 0.11476 0.10237 0.17681 -0.00508 0.00888  -0.00415 27  TYR A CA  
173  C C   . TYR A 41  ? 0.15643 0.14075 0.21864 -0.00589 0.00948  -0.00600 27  TYR A C   
174  O O   . TYR A 41  ? 0.13019 0.11252 0.19423 -0.00507 0.01049  -0.00528 27  TYR A O   
175  C CB  . TYR A 41  ? 0.08997 0.07881 0.15396 -0.00644 0.00798  -0.00254 27  TYR A CB  
176  C CG  . TYR A 41  ? 0.10084 0.09003 0.16408 -0.00908 0.00660  -0.00379 27  TYR A CG  
177  C CD1 . TYR A 41  ? 0.14447 0.13136 0.20828 -0.01101 0.00652  -0.00505 27  TYR A CD1 
178  C CD2 . TYR A 41  ? 0.12459 0.11636 0.18646 -0.00971 0.00540  -0.00368 27  TYR A CD2 
179  C CE1 . TYR A 41  ? 0.12988 0.11729 0.19289 -0.01361 0.00523  -0.00616 27  TYR A CE1 
180  C CE2 . TYR A 41  ? 0.18802 0.18033 0.24921 -0.01217 0.00406  -0.00467 27  TYR A CE2 
181  C CZ  . TYR A 41  ? 0.19272 0.18295 0.25445 -0.01418 0.00396  -0.00592 27  TYR A CZ  
182  O OH  . TYR A 41  ? 0.22543 0.21637 0.28640 -0.01684 0.00260  -0.00689 27  TYR A OH  
183  N N   . GLU A 42  ? 0.15007 0.13365 0.21036 -0.00753 0.00894  -0.00836 28  GLU A N   
184  C CA  . GLU A 42  ? 0.18749 0.16771 0.24778 -0.00835 0.00968  -0.01029 28  GLU A CA  
185  C C   . GLU A 42  ? 0.23810 0.21671 0.29837 -0.00599 0.01123  -0.01069 28  GLU A C   
186  O O   . GLU A 42  ? 0.21985 0.19535 0.28111 -0.00595 0.01224  -0.01142 28  GLU A O   
187  C CB  . GLU A 42  ? 0.20081 0.18073 0.25878 -0.01067 0.00885  -0.01285 28  GLU A CB  
188  C CG  . GLU A 42  ? 0.24893 0.23029 0.30708 -0.01327 0.00729  -0.01249 28  GLU A CG  
189  C CD  . GLU A 42  ? 0.70889 0.69040 0.76448 -0.01559 0.00636  -0.01488 28  GLU A CD  
190  O OE1 . GLU A 42  ? 0.48791 0.46677 0.54301 -0.01719 0.00678  -0.01687 28  GLU A OE1 
191  O OE2 . GLU A 42  ? 0.49169 0.47585 0.54565 -0.01585 0.00527  -0.01479 28  GLU A OE2 
192  N N   . ALA A 43  ? 0.15036 0.13103 0.20959 -0.00402 0.01147  -0.01014 29  ALA A N   
193  C CA  . ALA A 43  ? 0.20079 0.18064 0.26003 -0.00167 0.01284  -0.01028 29  ALA A CA  
194  C C   . ALA A 43  ? 0.13553 0.11544 0.19709 0.00029  0.01366  -0.00769 29  ALA A C   
195  O O   . ALA A 43  ? 0.18851 0.16807 0.25034 0.00237  0.01476  -0.00739 29  ALA A O   
196  C CB  . ALA A 43  ? 0.22459 0.20689 0.28132 -0.00073 0.01267  -0.01101 29  ALA A CB  
197  N N   . HIS A 44  ? 0.15819 0.13874 0.22145 -0.00033 0.01315  -0.00577 30  HIS A N   
198  C CA  . HIS A 44  ? 0.17201 0.15308 0.23726 0.00139  0.01384  -0.00320 30  HIS A CA  
199  C C   . HIS A 44  ? 0.19085 0.16867 0.25806 0.00206  0.01499  -0.00292 30  HIS A C   
200  O O   . HIS A 44  ? 0.21372 0.18887 0.28156 0.00050  0.01500  -0.00400 30  HIS A O   
201  C CB  . HIS A 44  ? 0.15496 0.13766 0.22146 0.00033  0.01298  -0.00140 30  HIS A CB  
202  C CG  . HIS A 44  ? 0.20256 0.18586 0.27112 0.00175  0.01364  0.00122  30  HIS A CG  
203  N ND1 . HIS A 44  ? 0.15693 0.14208 0.22502 0.00377  0.01424  0.00249  30  HIS A ND1 
204  C CD2 . HIS A 44  ? 0.17782 0.16019 0.24877 0.00128  0.01380  0.00281  30  HIS A CD2 
205  C CE1 . HIS A 44  ? 0.15329 0.13862 0.22341 0.00448  0.01474  0.00475  30  HIS A CE1 
206  N NE2 . HIS A 44  ? 0.19724 0.18087 0.26915 0.00304  0.01449  0.00499  30  HIS A NE2 
207  N N   . VAL A 45  ? 0.27870 0.25670 0.34680 0.00432  0.01599  -0.00142 31  VAL A N   
208  C CA  . VAL A 45  ? 0.25510 0.23014 0.32517 0.00530  0.01714  -0.00074 31  VAL A CA  
209  C C   . VAL A 45  ? 0.15733 0.13293 0.22954 0.00560  0.01721  0.00203  31  VAL A C   
210  O O   . VAL A 45  ? 0.22515 0.20345 0.29737 0.00687  0.01725  0.00381  31  VAL A O   
211  C CB  . VAL A 45  ? 0.30748 0.28238 0.37718 0.00769  0.01824  -0.00093 31  VAL A CB  
212  C CG1 . VAL A 45  ? 0.27228 0.24410 0.34422 0.00887  0.01944  0.00011  31  VAL A CG1 
213  C CG2 . VAL A 45  ? 0.27016 0.24456 0.33778 0.00730  0.01824  -0.00379 31  VAL A CG2 
214  N N   . VAL A 46  ? 0.19470 0.16776 0.26859 0.00432  0.01729  0.00234  32  VAL A N   
215  C CA  . VAL A 46  ? 0.19374 0.16726 0.26966 0.00416  0.01726  0.00481  32  VAL A CA  
216  C C   . VAL A 46  ? 0.18022 0.15251 0.25763 0.00623  0.01846  0.00659  32  VAL A C   
217  O O   . VAL A 46  ? 0.27505 0.24454 0.35268 0.00713  0.01937  0.00579  32  VAL A O   
218  C CB  . VAL A 46  ? 0.22551 0.19695 0.30249 0.00170  0.01681  0.00436  32  VAL A CB  
219  C CG1 . VAL A 46  ? 0.21299 0.18480 0.29220 0.00150  0.01688  0.00690  32  VAL A CG1 
220  C CG2 . VAL A 46  ? 0.22632 0.19944 0.30192 -0.00039 0.01549  0.00287  32  VAL A CG2 
221  N N   . SER A 47  ? 0.22760 0.20201 0.30605 0.00701  0.01852  0.00905  33  SER A N   
222  C CA  . SER A 47  ? 0.33954 0.31299 0.41959 0.00865  0.01951  0.01114  33  SER A CA  
223  C C   . SER A 47  ? 0.24327 0.21504 0.32537 0.00733  0.01952  0.01250  33  SER A C   
224  O O   . SER A 47  ? 0.25512 0.22888 0.33767 0.00610  0.01882  0.01337  33  SER A O   
225  C CB  . SER A 47  ? 0.33777 0.31479 0.41744 0.01026  0.01965  0.01299  33  SER A CB  
226  O OG  . SER A 47  ? 0.48171 0.46019 0.55947 0.01151  0.01975  0.01181  33  SER A OG  
227  N N   . TRP A 48  ? 0.25001 0.21813 0.33335 0.00763  0.02036  0.01273  34  TRP A N   
228  C CA  . TRP A 48  ? 0.18603 0.15184 0.27107 0.00607  0.02041  0.01358  34  TRP A CA  
229  C C   . TRP A 48  ? 0.29681 0.26277 0.38355 0.00725  0.02106  0.01645  34  TRP A C   
230  O O   . TRP A 48  ? 0.25461 0.22013 0.34156 0.00935  0.02187  0.01740  34  TRP A O   
231  C CB  . TRP A 48  ? 0.16592 0.12704 0.25103 0.00535  0.02101  0.01182  34  TRP A CB  
232  C CG  . TRP A 48  ? 0.20528 0.16607 0.28861 0.00399  0.02044  0.00892  34  TRP A CG  
233  C CD1 . TRP A 48  ? 0.24843 0.20866 0.33028 0.00502  0.02078  0.00698  34  TRP A CD1 
234  C CD2 . TRP A 48  ? 0.16710 0.12833 0.24994 0.00128  0.01940  0.00766  34  TRP A CD2 
235  N NE1 . TRP A 48  ? 0.23319 0.19331 0.31354 0.00303  0.02004  0.00455  34  TRP A NE1 
236  C CE2 . TRP A 48  ? 0.21071 0.17149 0.29164 0.00071  0.01915  0.00497  34  TRP A CE2 
237  C CE3 . TRP A 48  ? 0.15620 0.11834 0.24008 -0.00077 0.01866  0.00861  34  TRP A CE3 
238  C CZ2 . TRP A 48  ? 0.17458 0.13579 0.25452 -0.00187 0.01812  0.00327  34  TRP A CZ2 
239  C CZ3 . TRP A 48  ? 0.19555 0.15828 0.27860 -0.00325 0.01763  0.00697  34  TRP A CZ3 
240  C CH2 . TRP A 48  ? 0.20305 0.16532 0.28411 -0.00380 0.01734  0.00436  34  TRP A CH2 
241  N N   . GLY A 49  ? 0.12748 0.09425 0.21544 0.00585  0.02069  0.01788  35  GLY A N   
242  C CA  . GLY A 49  ? 0.14808 0.11461 0.23773 0.00646  0.02128  0.02052  35  GLY A CA  
243  C C   . GLY A 49  ? 0.21815 0.18006 0.30905 0.00579  0.02195  0.02070  35  GLY A C   
244  O O   . GLY A 49  ? 0.21407 0.17264 0.30445 0.00536  0.02223  0.01877  35  GLY A O   
245  N N   . ASN A 50  ? 0.17662 0.13826 0.26908 0.00560  0.02228  0.02302  36  ASN A N   
246  C CA  . ASN A 50  ? 0.22944 0.18669 0.32312 0.00500  0.02300  0.02362  36  ASN A CA  
247  C C   . ASN A 50  ? 0.17256 0.12939 0.26699 0.00219  0.02244  0.02350  36  ASN A C   
248  O O   . ASN A 50  ? 0.13580 0.09528 0.23118 0.00150  0.02209  0.02522  36  ASN A O   
249  C CB  . ASN A 50  ? 0.17278 0.12988 0.26764 0.00670  0.02377  0.02643  36  ASN A CB  
250  C CG  . ASN A 50  ? 0.34303 0.29556 0.43915 0.00603  0.02451  0.02733  36  ASN A CG  
251  O OD1 . ASN A 50  ? 0.36895 0.31770 0.46487 0.00473  0.02471  0.02560  36  ASN A OD1 
252  N ND2 . ASN A 50  ? 0.51264 0.46541 0.60994 0.00681  0.02496  0.03004  36  ASN A ND2 
253  N N   . GLN A 51  ? 0.23606 0.15454 0.15698 0.01860  -0.00403 -0.00824 37  GLN A N   
254  C CA  . GLN A 51  ? 0.22465 0.14189 0.14503 0.01502  -0.00395 -0.00852 37  GLN A CA  
255  C C   . GLN A 51  ? 0.23706 0.15081 0.15477 0.01448  -0.00360 -0.00784 37  GLN A C   
256  O O   . GLN A 51  ? 0.24708 0.16082 0.16512 0.01210  -0.00406 -0.00781 37  GLN A O   
257  C CB  . GLN A 51  ? 0.28104 0.19493 0.19895 0.01350  -0.00270 -0.00901 37  GLN A CB  
258  C CG  . GLN A 51  ? 0.25094 0.16314 0.16718 0.00929  -0.00334 -0.00943 37  GLN A CG  
259  C CD  . GLN A 51  ? 0.37431 0.28108 0.28588 0.00707  -0.00196 -0.01017 37  GLN A CD  
260  O OE1 . GLN A 51  ? 0.32358 0.22614 0.23277 0.00884  0.00024  -0.01013 37  GLN A OE1 
261  N NE2 . GLN A 51  ? 0.23480 0.14116 0.14443 0.00294  -0.00313 -0.01082 37  GLN A NE2 
262  N N   . ASP A 52  ? 0.21406 0.12429 0.12886 0.01702  -0.00258 -0.00703 38  ASP A N   
263  C CA  . ASP A 52  ? 0.19321 0.09938 0.10503 0.01684  -0.00189 -0.00616 38  ASP A CA  
264  C C   . ASP A 52  ? 0.29271 0.20087 0.20462 0.01722  -0.00294 -0.00601 38  ASP A C   
265  O O   . ASP A 52  ? 0.26425 0.16891 0.17354 0.01708  -0.00219 -0.00517 38  ASP A O   
266  C CB  . ASP A 52  ? 0.23556 0.13704 0.14438 0.01992  0.00001  -0.00488 38  ASP A CB  
267  C CG  . ASP A 52  ? 0.39222 0.28975 0.29999 0.01884  0.00231  -0.00519 38  ASP A CG  
268  O OD1 . ASP A 52  ? 0.33926 0.23640 0.24696 0.01514  0.00197  -0.00648 38  ASP A OD1 
269  O OD2 . ASP A 52  ? 0.43820 0.33269 0.34501 0.02174  0.00466  -0.00400 38  ASP A OD2 
270  N N   . ASP A 53  ? 0.19768 0.11088 0.11229 0.01759  -0.00425 -0.00686 39  ASP A N   
271  C CA  . ASP A 53  ? 0.19075 0.10569 0.10522 0.01715  -0.00452 -0.00721 39  ASP A CA  
272  C C   . ASP A 53  ? 0.22276 0.13723 0.13888 0.01450  -0.00358 -0.00704 39  ASP A C   
273  O O   . ASP A 53  ? 0.20479 0.11868 0.11979 0.01438  -0.00265 -0.00701 39  ASP A O   
274  C CB  . ASP A 53  ? 0.23664 0.15691 0.15413 0.01733  -0.00572 -0.00845 39  ASP A CB  
275  C CG  . ASP A 53  ? 0.30234 0.22278 0.21667 0.02005  -0.00717 -0.00859 39  ASP A CG  
276  O OD1 . ASP A 53  ? 0.29498 0.21314 0.20667 0.02200  -0.00686 -0.00672 39  ASP A OD1 
277  O OD2 . ASP A 53  ? 0.31446 0.23898 0.23080 0.01991  -0.00854 -0.00967 39  ASP A OD2 
278  N N   . TYR A 54  ? 0.16241 0.07635 0.08022 0.01242  -0.00365 -0.00694 40  TYR A N   
279  C CA  . TYR A 54  ? 0.18657 0.09955 0.10573 0.01002  -0.00321 -0.00657 40  TYR A CA  
280  C C   . TYR A 54  ? 0.21684 0.12607 0.13447 0.00752  -0.00311 -0.00511 40  TYR A C   
281  O O   . TYR A 54  ? 0.27037 0.17636 0.18520 0.00650  -0.00371 -0.00593 40  TYR A O   
282  C CB  . TYR A 54  ? 0.19124 0.10863 0.11466 0.00890  -0.00396 -0.00708 40  TYR A CB  
283  C CG  . TYR A 54  ? 0.12930 0.05095 0.05531 0.01088  -0.00397 -0.00827 40  TYR A CG  
284  C CD1 . TYR A 54  ? 0.16364 0.08594 0.09066 0.01132  -0.00258 -0.00856 40  TYR A CD1 
285  C CD2 . TYR A 54  ? 0.23398 0.15865 0.16137 0.01208  -0.00505 -0.00891 40  TYR A CD2 
286  C CE1 . TYR A 54  ? 0.23275 0.15879 0.16190 0.01216  -0.00275 -0.00985 40  TYR A CE1 
287  C CE2 . TYR A 54  ? 0.19410 0.12242 0.12394 0.01332  -0.00542 -0.00982 40  TYR A CE2 
288  C CZ  . TYR A 54  ? 0.24175 0.17080 0.17234 0.01302  -0.00449 -0.01045 40  TYR A CZ  
289  O OH  . TYR A 54  ? 0.22329 0.15522 0.15553 0.01345  -0.00500 -0.01178 40  TYR A OH  
290  N N   . GLN A 55  ? 0.15377 0.06336 0.07332 0.00632  -0.00205 -0.00285 41  GLN A N   
291  C CA  . GLN A 55  ? 0.18630 0.09297 0.10532 0.00344  -0.00208 -0.00089 41  GLN A CA  
292  C C   . GLN A 55  ? 0.19659 0.10827 0.12158 0.00014  -0.00244 0.00190  41  GLN A C   
293  O O   . GLN A 55  ? 0.17852 0.09387 0.10804 0.00113  -0.00076 0.00375  41  GLN A O   
294  C CB  . GLN A 55  ? 0.21458 0.11812 0.13174 0.00505  -0.00034 0.00061  41  GLN A CB  
295  C CG  . GLN A 55  ? 0.21967 0.12131 0.13817 0.00190  -0.00006 0.00348  41  GLN A CG  
296  C CD  . GLN A 55  ? 0.33329 0.22949 0.24799 -0.00077 -0.00124 0.00232  41  GLN A CD  
297  O OE1 . GLN A 55  ? 0.32816 0.21927 0.23821 0.00142  -0.00059 0.00044  41  GLN A OE1 
298  N NE2 . GLN A 55  ? 0.23168 0.12884 0.14826 -0.00574 -0.00276 0.00367  41  GLN A NE2 
299  N N   . LEU A 56  ? 0.18688 0.09866 0.11174 -0.00392 -0.00436 0.00249  42  LEU A N   
300  C CA  . LEU A 56  ? 0.18755 0.10564 0.11875 -0.00750 -0.00527 0.00617  42  LEU A CA  
301  C C   . LEU A 56  ? 0.17872 0.09725 0.11343 -0.00902 -0.00419 0.01030  42  LEU A C   
302  O O   . LEU A 56  ? 0.18454 0.09773 0.11551 -0.01019 -0.00428 0.01017  42  LEU A O   
303  C CB  . LEU A 56  ? 0.15655 0.07499 0.08536 -0.01224 -0.00820 0.00567  42  LEU A CB  
304  C CG  . LEU A 56  ? 0.13618 0.05420 0.06144 -0.01107 -0.00903 0.00209  42  LEU A CG  
305  C CD1 . LEU A 56  ? 0.14354 0.06293 0.06644 -0.01647 -0.01172 0.00231  42  LEU A CD1 
306  C CD2 . LEU A 56  ? 0.16355 0.08738 0.09437 -0.00746 -0.00790 0.00234  42  LEU A CD2 
307  N N   . VAL A 57  ? 0.18045 0.10533 0.12303 -0.00892 -0.00274 0.01443  43  VAL A N   
308  C CA  . VAL A 57  ? 0.16154 0.08775 0.10896 -0.00957 -0.00086 0.01922  43  VAL A CA  
309  C C   . VAL A 57  ? 0.19842 0.13178 0.15324 -0.01459 -0.00276 0.02492  43  VAL A C   
310  O O   . VAL A 57  ? 0.21041 0.14366 0.16681 -0.01783 -0.00357 0.02827  43  VAL A O   
311  C CB  . VAL A 57  ? 0.20368 0.13056 0.15420 -0.00489 0.00361  0.02010  43  VAL A CB  
312  C CG1 . VAL A 57  ? 0.30851 0.23768 0.26540 -0.00537 0.00629  0.02601  43  VAL A CG1 
313  C CG2 . VAL A 57  ? 0.25276 0.17304 0.19528 -0.00107 0.00478  0.01539  43  VAL A CG2 
314  N N   . ARG A 58  ? 0.19707 0.13733 0.15700 -0.01547 -0.00360 0.02663  44  ARG A N   
315  C CA  . ARG A 58  ? 0.16818 0.11736 0.13681 -0.01984 -0.00518 0.03348  44  ARG A CA  
316  C C   . ARG A 58  ? 0.14769 0.10293 0.11816 -0.02136 -0.00744 0.03352  44  ARG A C   
317  O O   . ARG A 58  ? 0.19611 0.15126 0.16685 -0.01731 -0.00544 0.03088  44  ARG A O   
318  C CB  . ARG A 58  ? 0.23904 0.19273 0.21771 -0.01692 -0.00053 0.03953  44  ARG A CB  
319  C CG  . ARG A 58  ? 0.43356 0.39811 0.42377 -0.02057 -0.00136 0.04833  44  ARG A CG  
320  C CD  . ARG A 58  ? 0.37901 0.34682 0.37799 -0.01618 0.00455  0.05189  44  ARG A CD  
321  N NE  . ARG A 58  ? 0.56975 0.53428 0.56881 -0.01057 0.00955  0.04952  44  ARG A NE  
322  C CZ  . ARG A 58  ? 0.79644 0.76745 0.80324 -0.00853 0.01197  0.05116  44  ARG A CZ  
323  N NH1 . ARG A 58  ? 0.59773 0.57970 0.61358 -0.01097 0.00995  0.05581  44  ARG A NH1 
324  N NH2 . ARG A 58  ? 0.62696 0.59349 0.63260 -0.00394 0.01654  0.04802  44  ARG A NH2 
325  N N   . LYS A 59  ? 0.21124 0.17194 0.18284 -0.02754 -0.01170 0.03670  45  LYS A N   
326  C CA  . LYS A 59  ? 0.17852 0.14638 0.15231 -0.02948 -0.01401 0.03794  45  LYS A CA  
327  C C   . LYS A 59  ? 0.17641 0.15483 0.16385 -0.02779 -0.01141 0.04574  45  LYS A C   
328  O O   . LYS A 59  ? 0.20888 0.19289 0.20468 -0.02952 -0.01074 0.05279  45  LYS A O   
329  C CB  . LYS A 59  ? 0.20326 0.17316 0.17217 -0.03740 -0.01960 0.03866  45  LYS A CB  
330  C CG  . LYS A 59  ? 0.31521 0.29304 0.28513 -0.04029 -0.02253 0.04034  45  LYS A CG  
331  C CD  . LYS A 59  ? 0.35371 0.33067 0.31481 -0.04863 -0.02799 0.03911  45  LYS A CD  
332  C CE  . LYS A 59  ? 0.44165 0.42614 0.40186 -0.05175 -0.03102 0.04043  45  LYS A CE  
333  N NZ  . LYS A 59  ? 0.35224 0.33429 0.30130 -0.06037 -0.03609 0.03814  45  LYS A NZ  
334  N N   . LEU A 60  ? 0.15254 0.13347 0.14290 -0.02412 -0.00940 0.04482  46  LEU A N   
335  C CA  . LEU A 60  ? 0.14971 0.13999 0.15335 -0.02209 -0.00609 0.05221  46  LEU A CA  
336  C C   . LEU A 60  ? 0.28075 0.28283 0.28988 -0.02628 -0.00992 0.05697  46  LEU A C   
337  O O   . LEU A 60  ? 0.30792 0.32053 0.32865 -0.02587 -0.00902 0.06227  46  LEU A O   
338  C CB  . LEU A 60  ? 0.20826 0.19479 0.21294 -0.01571 -0.00120 0.04841  46  LEU A CB  
339  C CG  . LEU A 60  ? 0.26799 0.24413 0.26743 -0.01110 0.00290  0.04300  46  LEU A CG  
340  C CD1 . LEU A 60  ? 0.29866 0.27166 0.29849 -0.00620 0.00688  0.03910  46  LEU A CD1 
341  C CD2 . LEU A 60  ? 0.41953 0.39623 0.42534 -0.01021 0.00671  0.04844  46  LEU A CD2 
342  N N   . GLY A 61  ? 0.24391 0.24470 0.24448 -0.02947 -0.01413 0.05359  47  GLY A N   
343  C CA  . GLY A 61  ? 0.33382 0.34573 0.33831 -0.03377 -0.01786 0.05851  47  GLY A CA  
344  C C   . GLY A 61  ? 0.32110 0.32867 0.31354 -0.03580 -0.02127 0.05204  47  GLY A C   
345  O O   . GLY A 61  ? 0.24074 0.23692 0.22253 -0.03376 -0.02076 0.04363  47  GLY A O   
346  N N   . ARG A 62  ? 0.24960 0.26692 0.24427 -0.03953 -0.02447 0.05634  48  ARG A N   
347  C CA  . ARG A 62  ? 0.29233 0.30676 0.27533 -0.04231 -0.02784 0.05094  48  ARG A CA  
348  C C   . ARG A 62  ? 0.44854 0.47412 0.43862 -0.04178 -0.02805 0.05606  48  ARG A C   
349  O O   . ARG A 62  ? 0.45674 0.49520 0.45868 -0.04356 -0.02886 0.06400  48  ARG A O   
350  C CB  . ARG A 62  ? 0.44147 0.45525 0.41480 -0.05113 -0.03355 0.05053  48  ARG A CB  
351  C CG  . ARG A 62  ? 0.61459 0.62973 0.57803 -0.05565 -0.03728 0.04817  48  ARG A CG  
352  C CD  . ARG A 62  ? 0.69040 0.70562 0.64449 -0.06560 -0.04297 0.04848  48  ARG A CD  
353  N NE  . ARG A 62  ? 0.83989 0.84168 0.78490 -0.06673 -0.04251 0.04207  48  ARG A NE  
354  C CZ  . ARG A 62  ? 0.99814 0.99617 0.93379 -0.07511 -0.04655 0.04064  48  ARG A CZ  
355  N NH1 . ARG A 62  ? 0.80500 0.81077 0.74079 -0.08224 -0.04957 0.04404  48  ARG A NH1 
356  N NH2 . ARG A 62  ? 0.54416 0.52943 0.47293 -0.07505 -0.04514 0.03502  48  ARG A NH2 
357  N N   . GLY A 63  ? 0.54006 0.56128 0.52453 -0.03844 -0.02688 0.05048  49  GLY A N   
358  C CA  . GLY A 63  ? 0.41835 0.44905 0.40690 -0.03854 -0.02758 0.05438  49  GLY A CA  
359  C C   . GLY A 63  ? 0.51220 0.54142 0.48695 -0.04421 -0.03219 0.05081  49  GLY A C   
360  O O   . GLY A 63  ? 0.30329 0.32379 0.26552 -0.04837 -0.03463 0.04540  49  GLY A O   
361  N N   . LYS A 64  ? 0.38281 0.42010 0.36039 -0.04401 -0.03254 0.05342  50  LYS A N   
362  C CA  . LYS A 64  ? 0.47935 0.51517 0.44544 -0.04864 -0.03530 0.04915  50  LYS A CA  
363  C C   . LYS A 64  ? 0.41372 0.43432 0.36435 -0.04651 -0.03421 0.03943  50  LYS A C   
364  O O   . LYS A 64  ? 0.47967 0.49306 0.41822 -0.05090 -0.03562 0.03395  50  LYS A O   
365  C CB  . LYS A 64  ? 0.45233 0.49945 0.42615 -0.04757 -0.03464 0.05353  50  LYS A CB  
366  C CG  . LYS A 64  ? 0.58653 0.63027 0.54803 -0.05038 -0.03588 0.04859  50  LYS A CG  
367  C CD  . LYS A 64  ? 0.75405 0.80931 0.71863 -0.05697 -0.03872 0.05382  50  LYS A CD  
368  C CE  . LYS A 64  ? 0.79596 0.84937 0.75477 -0.06507 -0.04219 0.05367  50  LYS A CE  
369  N NZ  . LYS A 64  ? 0.85629 0.91906 0.81473 -0.07234 -0.04503 0.05786  50  LYS A NZ  
370  N N   . TYR A 65  ? 0.33781 0.35262 0.29112 -0.03911 -0.03024 0.03631  51  TYR A N   
371  C CA  . TYR A 65  ? 0.37561 0.37717 0.31769 -0.03584 -0.02815 0.02736  51  TYR A CA  
372  C C   . TYR A 65  ? 0.39497 0.38690 0.33812 -0.03126 -0.02525 0.02295  51  TYR A C   
373  O O   . TYR A 65  ? 0.38223 0.36522 0.32020 -0.02686 -0.02278 0.01699  51  TYR A O   
374  C CB  . TYR A 65  ? 0.40272 0.40623 0.34657 -0.03105 -0.02580 0.02654  51  TYR A CB  
375  C CG  . TYR A 65  ? 0.60330 0.61681 0.54611 -0.03499 -0.02830 0.03122  51  TYR A CG  
376  C CD1 . TYR A 65  ? 0.54970 0.55980 0.48128 -0.04023 -0.03008 0.02770  51  TYR A CD1 
377  C CD2 . TYR A 65  ? 0.46212 0.48774 0.41814 -0.03241 -0.02727 0.03808  51  TYR A CD2 
378  C CE1 . TYR A 65  ? 0.57248 0.59124 0.50520 -0.04307 -0.03124 0.03083  51  TYR A CE1 
379  C CE2 . TYR A 65  ? 0.56077 0.59571 0.51825 -0.03519 -0.02860 0.04168  51  TYR A CE2 
380  C CZ  . TYR A 65  ? 0.58466 0.61614 0.53021 -0.04058 -0.03072 0.03786  51  TYR A CZ  
381  O OH  . TYR A 65  ? 0.72269 0.76299 0.66951 -0.04339 -0.03182 0.04117  51  TYR A OH  
382  N N   . SER A 66  ? 0.27191 0.26585 0.22170 -0.03220 -0.02544 0.02621  52  SER A N   
383  C CA  . SER A 66  ? 0.19620 0.18186 0.14715 -0.02774 -0.02253 0.02258  52  SER A CA  
384  C C   . SER A 66  ? 0.26414 0.25099 0.21841 -0.03100 -0.02366 0.02601  52  SER A C   
385  O O   . SER A 66  ? 0.29828 0.29429 0.25735 -0.03588 -0.02630 0.03241  52  SER A O   
386  C CB  . SER A 66  ? 0.29961 0.28764 0.26099 -0.02102 -0.01861 0.02341  52  SER A CB  
387  O OG  . SER A 66  ? 0.32516 0.32399 0.29935 -0.02125 -0.01789 0.03101  52  SER A OG  
388  N N   . GLU A 67  ? 0.20902 0.18704 0.16095 -0.02827 -0.02166 0.02218  53  GLU A N   
389  C CA  . GLU A 67  ? 0.23259 0.21081 0.18860 -0.02987 -0.02163 0.02525  53  GLU A CA  
390  C C   . GLU A 67  ? 0.21738 0.19039 0.17706 -0.02350 -0.01742 0.02299  53  GLU A C   
391  O O   . GLU A 67  ? 0.20762 0.17308 0.16157 -0.01967 -0.01589 0.01714  53  GLU A O   
392  C CB  . GLU A 67  ? 0.23832 0.20909 0.18378 -0.03506 -0.02426 0.02225  53  GLU A CB  
393  C CG  . GLU A 67  ? 0.39242 0.36892 0.33441 -0.04322 -0.02893 0.02545  53  GLU A CG  
394  C CD  . GLU A 67  ? 0.56445 0.53276 0.49631 -0.04907 -0.03124 0.02246  53  GLU A CD  
395  O OE1 . GLU A 67  ? 0.29934 0.25982 0.23020 -0.04668 -0.02915 0.02000  53  GLU A OE1 
396  O OE2 . GLU A 67  ? 0.65305 0.62252 0.57755 -0.05631 -0.03503 0.02254  53  GLU A OE2 
397  N N   . VAL A 68  ? 0.15506 0.13215 0.12395 -0.02263 -0.01549 0.02792  54  VAL A N   
398  C CA  . VAL A 68  ? 0.16029 0.13391 0.13355 -0.01692 -0.01097 0.02673  54  VAL A CA  
399  C C   . VAL A 68  ? 0.14330 0.11214 0.11526 -0.01735 -0.01010 0.02708  54  VAL A C   
400  O O   . VAL A 68  ? 0.17387 0.14740 0.14996 -0.02119 -0.01146 0.03245  54  VAL A O   
401  C CB  . VAL A 68  ? 0.18243 0.16450 0.16840 -0.01461 -0.00781 0.03254  54  VAL A CB  
402  C CG1 . VAL A 68  ? 0.21383 0.19096 0.20277 -0.00939 -0.00270 0.03070  54  VAL A CG1 
403  C CG2 . VAL A 68  ? 0.25700 0.24394 0.24453 -0.01411 -0.00861 0.03247  54  VAL A CG2 
404  N N   . PHE A 69  ? 0.12841 0.08868 0.09512 -0.01350 -0.00791 0.02194  55  PHE A N   
405  C CA  . PHE A 69  ? 0.18208 0.13710 0.14664 -0.01326 -0.00674 0.02184  55  PHE A CA  
406  C C   . PHE A 69  ? 0.18502 0.13705 0.15205 -0.00812 -0.00212 0.02082  55  PHE A C   
407  O O   . PHE A 69  ? 0.16849 0.11833 0.13382 -0.00479 -0.00073 0.01697  55  PHE A O   
408  C CB  . PHE A 69  ? 0.16060 0.10674 0.11388 -0.01408 -0.00875 0.01628  55  PHE A CB  
409  C CG  . PHE A 69  ? 0.17684 0.12304 0.12493 -0.01956 -0.01270 0.01593  55  PHE A CG  
410  C CD1 . PHE A 69  ? 0.19799 0.14474 0.14212 -0.02011 -0.01430 0.01325  55  PHE A CD1 
411  C CD2 . PHE A 69  ? 0.14730 0.09247 0.09381 -0.02448 -0.01467 0.01814  55  PHE A CD2 
412  C CE1 . PHE A 69  ? 0.16473 0.11040 0.10229 -0.02555 -0.01753 0.01241  55  PHE A CE1 
413  C CE2 . PHE A 69  ? 0.17235 0.11644 0.11255 -0.03038 -0.01826 0.01717  55  PHE A CE2 
414  C CZ  . PHE A 69  ? 0.16776 0.11188 0.10293 -0.03102 -0.01961 0.01417  55  PHE A CZ  
415  N N   . GLU A 70  ? 0.13001 0.08169 0.10056 -0.00776 0.00035  0.02423  56  GLU A N   
416  C CA  . GLU A 70  ? 0.11284 0.05854 0.08087 -0.00358 0.00427  0.02162  56  GLU A CA  
417  C C   . GLU A 70  ? 0.15167 0.08970 0.10926 -0.00309 0.00233  0.01631  56  GLU A C   
418  O O   . GLU A 70  ? 0.17190 0.10817 0.12579 -0.00610 -0.00056 0.01635  56  GLU A O   
419  C CB  . GLU A 70  ? 0.20448 0.15142 0.17850 -0.00321 0.00787  0.02701  56  GLU A CB  
420  C CG  . GLU A 70  ? 0.28249 0.22273 0.25252 0.00077  0.01229  0.02440  56  GLU A CG  
421  C CD  . GLU A 70  ? 0.38434 0.32496 0.35922 0.00115  0.01603  0.02984  56  GLU A CD  
422  O OE1 . GLU A 70  ? 0.43783 0.38533 0.42218 -0.00082 0.01641  0.03656  56  GLU A OE1 
423  O OE2 . GLU A 70  ? 0.38421 0.31880 0.35366 0.00341  0.01859  0.02791  56  GLU A OE2 
424  N N   . ALA A 71  ? 0.18723 0.12074 0.14015 0.00048  0.00398  0.01191  57  ALA A N   
425  C CA  . ALA A 71  ? 0.13928 0.06657 0.08342 0.00153  0.00248  0.00778  57  ALA A CA  
426  C C   . ALA A 71  ? 0.14210 0.06572 0.08296 0.00491  0.00539  0.00576  57  ALA A C   
427  O O   . ALA A 71  ? 0.18902 0.11380 0.13333 0.00628  0.00870  0.00648  57  ALA A O   
428  C CB  . ALA A 71  ? 0.19674 0.12347 0.13701 0.00156  -0.00035 0.00408  57  ALA A CB  
429  N N   . ILE A 72  ? 0.16431 0.08327 0.09811 0.00611  0.00436  0.00331  58  ILE A N   
430  C CA  . ILE A 72  ? 0.19376 0.10968 0.12272 0.00879  0.00617  0.00124  58  ILE A CA  
431  C C   . ILE A 72  ? 0.21277 0.12773 0.13687 0.01014  0.00369  -0.00240 58  ILE A C   
432  O O   . ILE A 72  ? 0.17942 0.09300 0.10132 0.00985  0.00143  -0.00286 58  ILE A O   
433  C CB  . ILE A 72  ? 0.22080 0.13319 0.14650 0.00931  0.00751  0.00310  58  ILE A CB  
434  C CG1 . ILE A 72  ? 0.32455 0.23845 0.25608 0.00821  0.01037  0.00748  58  ILE A CG1 
435  C CG2 . ILE A 72  ? 0.24303 0.15275 0.16234 0.01174  0.00886  0.00100  58  ILE A CG2 
436  C CD1 . ILE A 72  ? 0.43012 0.34501 0.36459 0.00957  0.01452  0.00789  58  ILE A CD1 
437  N N   . ASN A 73  ? 0.17865 0.09409 0.10114 0.01145  0.00440  -0.00478 59  ASN A N   
438  C CA  . ASN A 73  ? 0.19742 0.11282 0.11564 0.01273  0.00207  -0.00736 59  ASN A CA  
439  C C   . ASN A 73  ? 0.23731 0.14992 0.14936 0.01400  0.00219  -0.00690 59  ASN A C   
440  O O   . ASN A 73  ? 0.23387 0.14533 0.14273 0.01426  0.00413  -0.00727 59  ASN A O   
441  C CB  . ASN A 73  ? 0.21663 0.13487 0.13660 0.01258  0.00251  -0.00952 59  ASN A CB  
442  C CG  . ASN A 73  ? 0.27136 0.19310 0.19040 0.01307  -0.00034 -0.01076 59  ASN A CG  
443  O OD1 . ASN A 73  ? 0.26661 0.18735 0.18203 0.01427  -0.00202 -0.01006 59  ASN A OD1 
444  N ND2 . ASN A 73  ? 0.26192 0.18695 0.18397 0.01227  -0.00056 -0.01246 59  ASN A ND2 
445  N N   . ILE A 74  ? 0.23901 0.15012 0.14907 0.01482  0.00060  -0.00590 60  ILE A N   
446  C CA  . ILE A 74  ? 0.27006 0.17886 0.17533 0.01620  0.00108  -0.00441 60  ILE A CA  
447  C C   . ILE A 74  ? 0.31063 0.22134 0.21130 0.01742  -0.00008 -0.00542 60  ILE A C   
448  O O   . ILE A 74  ? 0.31073 0.22047 0.20690 0.01831  0.00053  -0.00400 60  ILE A O   
449  C CB  . ILE A 74  ? 0.31847 0.22412 0.22336 0.01671  0.00070  -0.00255 60  ILE A CB  
450  C CG1 . ILE A 74  ? 0.32976 0.23586 0.23426 0.01817  -0.00110 -0.00326 60  ILE A CG1 
451  C CG2 . ILE A 74  ? 0.26342 0.16742 0.17200 0.01425  0.00136  -0.00165 60  ILE A CG2 
452  C CD1 . ILE A 74  ? 0.34794 0.24940 0.25116 0.01911  -0.00036 -0.00153 60  ILE A CD1 
453  N N   . THR A 75  ? 0.27361 0.18750 0.17533 0.01712  -0.00187 -0.00754 61  THR A N   
454  C CA  . THR A 75  ? 0.27542 0.19275 0.17416 0.01716  -0.00360 -0.00803 61  THR A CA  
455  C C   . THR A 75  ? 0.31949 0.23722 0.21639 0.01527  -0.00181 -0.00940 61  THR A C   
456  O O   . THR A 75  ? 0.32776 0.24721 0.22002 0.01480  -0.00280 -0.00939 61  THR A O   
457  C CB  . THR A 75  ? 0.23531 0.15692 0.13758 0.01702  -0.00618 -0.00916 61  THR A CB  
458  O OG1 . THR A 75  ? 0.30258 0.22616 0.21026 0.01502  -0.00523 -0.01118 61  THR A OG1 
459  C CG2 . THR A 75  ? 0.30287 0.22329 0.20698 0.01902  -0.00696 -0.00790 61  THR A CG2 
460  N N   . ASN A 76  ? 0.23880 0.15492 0.13887 0.01413  0.00106  -0.01036 62  ASN A N   
461  C CA  . ASN A 76  ? 0.25027 0.16532 0.14819 0.01263  0.00386  -0.01180 62  ASN A CA  
462  C C   . ASN A 76  ? 0.26558 0.17569 0.16305 0.01323  0.00834  -0.01055 62  ASN A C   
463  O O   . ASN A 76  ? 0.26065 0.16879 0.15685 0.01236  0.01188  -0.01153 62  ASN A O   
464  C CB  . ASN A 76  ? 0.26732 0.18520 0.16938 0.01063  0.00390  -0.01444 62  ASN A CB  
465  C CG  . ASN A 76  ? 0.26229 0.18078 0.17169 0.01086  0.00483  -0.01414 62  ASN A CG  
466  O OD1 . ASN A 76  ? 0.23806 0.15438 0.14906 0.01195  0.00598  -0.01219 62  ASN A OD1 
467  N ND2 . ASN A 76  ? 0.28159 0.20299 0.19519 0.00961  0.00432  -0.01600 62  ASN A ND2 
468  N N   A ASN A 77  ? 0.26957 0.17704 0.16783 0.01459  0.00869  -0.00841 63  ASN A N   
469  N N   B ASN A 77  ? 0.26954 0.17702 0.16768 0.01461  0.00865  -0.00841 63  ASN A N   
470  C CA  A ASN A 77  ? 0.27334 0.17854 0.17470 0.01480  0.01242  -0.00566 63  ASN A CA  
471  C CA  B ASN A 77  ? 0.27350 0.17861 0.17450 0.01481  0.01251  -0.00580 63  ASN A CA  
472  C C   A ASN A 77  ? 0.26451 0.17039 0.17287 0.01398  0.01530  -0.00544 63  ASN A C   
473  C C   B ASN A 77  ? 0.25975 0.16491 0.16639 0.01403  0.01587  -0.00618 63  ASN A C   
474  O O   A ASN A 77  ? 0.23767 0.14277 0.15010 0.01412  0.01874  -0.00232 63  ASN A O   
475  O O   B ASN A 77  ? 0.28944 0.19230 0.19713 0.01439  0.02052  -0.00446 63  ASN A O   
476  C CB  A ASN A 77  ? 0.26654 0.16839 0.16161 0.01563  0.01561  -0.00465 63  ASN A CB  
477  C CB  B ASN A 77  ? 0.26538 0.16730 0.15979 0.01572  0.01519  -0.00464 63  ASN A CB  
478  C CG  A ASN A 77  ? 0.27973 0.18156 0.17033 0.01677  0.01332  -0.00286 63  ASN A CG  
479  C CG  B ASN A 77  ? 0.27937 0.18007 0.17783 0.01629  0.01774  -0.00041 63  ASN A CG  
480  O OD1 A ASN A 77  ? 0.44081 0.34217 0.32373 0.01717  0.01294  -0.00366 63  ASN A OD1 
481  O OD1 B ASN A 77  ? 0.27435 0.17650 0.17806 0.01582  0.01574  0.00173  63  ASN A OD1 
482  N ND2 A ASN A 77  ? 0.38226 0.28457 0.27747 0.01705  0.01185  -0.00027 63  ASN A ND2 
483  N ND2 B ASN A 77  ? 0.28843 0.18620 0.18420 0.01702  0.02235  0.00084  63  ASN A ND2 
484  N N   . GLU A 78  ? 0.23100 0.13885 0.14183 0.01324  0.01411  -0.00792 64  GLU A N   
485  C CA  . GLU A 78  ? 0.21365 0.12214 0.13115 0.01276  0.01746  -0.00751 64  GLU A CA  
486  C C   . GLU A 78  ? 0.20122 0.11386 0.12754 0.01217  0.01619  -0.00408 64  GLU A C   
487  O O   . GLU A 78  ? 0.17664 0.09153 0.10333 0.01167  0.01195  -0.00417 64  GLU A O   
488  C CB  . GLU A 78  ? 0.28392 0.19441 0.20209 0.01172  0.01677  -0.01093 64  GLU A CB  
489  C CG  . GLU A 78  ? 0.36619 0.27570 0.27858 0.01071  0.01768  -0.01321 64  GLU A CG  
490  C CD  . GLU A 78  ? 0.35299 0.26453 0.26802 0.00893  0.01803  -0.01600 64  GLU A CD  
491  O OE1 . GLU A 78  ? 0.30954 0.22308 0.23147 0.00894  0.01848  -0.01578 64  GLU A OE1 
492  O OE2 . GLU A 78  ? 0.37443 0.28534 0.28436 0.00738  0.01787  -0.01840 64  GLU A OE2 
493  N N   . ARG A 79  ? 0.19245 0.10598 0.12557 0.01212  0.02017  -0.00072 65  ARG A N   
494  C CA  . ARG A 79  ? 0.20992 0.12861 0.15191 0.01093  0.01899  0.00324  65  ARG A CA  
495  C C   . ARG A 79  ? 0.19430 0.11643 0.14021 0.01044  0.01736  0.00159  65  ARG A C   
496  O O   . ARG A 79  ? 0.23043 0.15107 0.17634 0.01115  0.01985  -0.00090 65  ARG A O   
497  C CB  . ARG A 79  ? 0.23350 0.15323 0.18274 0.01127  0.02414  0.00832  65  ARG A CB  
498  C CG  . ARG A 79  ? 0.31496 0.24100 0.27309 0.00935  0.02241  0.01402  65  ARG A CG  
499  C CD  . ARG A 79  ? 0.27773 0.20524 0.24344 0.01000  0.02772  0.02017  65  ARG A CD  
500  N NE  . ARG A 79  ? 0.40011 0.32141 0.35983 0.01193  0.03161  0.01924  65  ARG A NE  
501  C CZ  . ARG A 79  ? 0.49464 0.41493 0.45247 0.01158  0.03098  0.02161  65  ARG A CZ  
502  N NH1 . ARG A 79  ? 0.46036 0.38503 0.42221 0.00896  0.02687  0.02516  65  ARG A NH1 
503  N NH2 . ARG A 79  ? 0.49601 0.41051 0.44729 0.01358  0.03461  0.02033  65  ARG A NH2 
504  N N   . VAL A 80  ? 0.18477 0.11098 0.13335 0.00902  0.01329  0.00279  66  VAL A N   
505  C CA  . VAL A 80  ? 0.15353 0.08370 0.10602 0.00855  0.01147  0.00197  66  VAL A CA  
506  C C   . VAL A 80  ? 0.16008 0.09583 0.11874 0.00639  0.00961  0.00640  66  VAL A C   
507  O O   . VAL A 80  ? 0.16199 0.09846 0.12186 0.00492  0.00938  0.00988  66  VAL A O   
508  C CB  . VAL A 80  ? 0.17101 0.09993 0.11739 0.00896  0.00758  -0.00240 66  VAL A CB  
509  C CG1 . VAL A 80  ? 0.19649 0.12129 0.13669 0.01032  0.00851  -0.00633 66  VAL A CG1 
510  C CG2 . VAL A 80  ? 0.15431 0.08216 0.09639 0.00805  0.00414  -0.00210 66  VAL A CG2 
511  N N   . VAL A 81  ? 0.16139 0.10141 0.12372 0.00584  0.00801  0.00644  67  VAL A N   
512  C CA  . VAL A 81  ? 0.14976 0.09570 0.11661 0.00323  0.00554  0.01030  67  VAL A CA  
513  C C   . VAL A 81  ? 0.16252 0.10814 0.12415 0.00258  0.00156  0.00696  67  VAL A C   
514  O O   . VAL A 81  ? 0.18565 0.13054 0.14626 0.00446  0.00162  0.00375  67  VAL A O   
515  C CB  . VAL A 81  ? 0.16183 0.11428 0.13924 0.00332  0.00825  0.01491  67  VAL A CB  
516  C CG1 . VAL A 81  ? 0.21280 0.17233 0.19371 0.00041  0.00484  0.01843  67  VAL A CG1 
517  C CG2 . VAL A 81  ? 0.20055 0.15356 0.18392 0.00385  0.01266  0.01963  67  VAL A CG2 
518  N N   . VAL A 82  ? 0.11963 0.06530 0.07774 -0.00023 -0.00159 0.00769  68  VAL A N   
519  C CA  . VAL A 82  ? 0.11835 0.06259 0.07072 -0.00089 -0.00451 0.00467  68  VAL A CA  
520  C C   . VAL A 82  ? 0.12247 0.07285 0.07787 -0.00430 -0.00657 0.00787  68  VAL A C   
521  O O   . VAL A 82  ? 0.14851 0.10149 0.10541 -0.00788 -0.00781 0.01149  68  VAL A O   
522  C CB  . VAL A 82  ? 0.17159 0.10875 0.11520 -0.00137 -0.00589 0.00190  68  VAL A CB  
523  C CG1 . VAL A 82  ? 0.14530 0.08027 0.08317 -0.00199 -0.00785 -0.00079 68  VAL A CG1 
524  C CG2 . VAL A 82  ? 0.15079 0.08322 0.09146 0.00211  -0.00418 -0.00071 68  VAL A CG2 
525  N N   . LYS A 83  ? 0.10429 0.05740 0.06045 -0.00347 -0.00714 0.00684  69  LYS A N   
526  C CA  . LYS A 83  ? 0.09955 0.05902 0.05780 -0.00660 -0.00915 0.00986  69  LYS A CA  
527  C C   . LYS A 83  ? 0.14239 0.09735 0.09115 -0.00758 -0.01122 0.00594  69  LYS A C   
528  O O   . LYS A 83  ? 0.13286 0.08616 0.08011 -0.00452 -0.01047 0.00303  69  LYS A O   
529  C CB  . LYS A 83  ? 0.11415 0.08036 0.08131 -0.00451 -0.00736 0.01229  69  LYS A CB  
530  C CG  . LYS A 83  ? 0.14010 0.11444 0.11065 -0.00731 -0.00918 0.01639  69  LYS A CG  
531  C CD  . LYS A 83  ? 0.21689 0.19616 0.19586 -0.00410 -0.00670 0.01784  69  LYS A CD  
532  C CE  . LYS A 83  ? 0.25891 0.24816 0.24436 -0.00636 -0.00767 0.02380  69  LYS A CE  
533  N NZ  . LYS A 83  ? 0.12629 0.11991 0.12211 -0.00290 -0.00413 0.02612  69  LYS A NZ  
534  N N   . ILE A 84  ? 0.13638 0.08902 0.07881 -0.01197 -0.01347 0.00600  70  ILE A N   
535  C CA  . ILE A 84  ? 0.14468 0.09130 0.07688 -0.01328 -0.01454 0.00208  70  ILE A CA  
536  C C   . ILE A 84  ? 0.18775 0.14068 0.12008 -0.01591 -0.01615 0.00399  70  ILE A C   
537  O O   . ILE A 84  ? 0.22442 0.18436 0.15994 -0.02036 -0.01829 0.00840  70  ILE A O   
538  C CB  . ILE A 84  ? 0.18917 0.12875 0.11339 -0.01725 -0.01572 0.00063  70  ILE A CB  
539  C CG1 . ILE A 84  ? 0.19220 0.12617 0.11676 -0.01423 -0.01390 -0.00066 70  ILE A CG1 
540  C CG2 . ILE A 84  ? 0.21146 0.14334 0.12441 -0.01870 -0.01578 -0.00364 70  ILE A CG2 
541  C CD1 . ILE A 84  ? 0.21296 0.14002 0.13104 -0.01795 -0.01465 -0.00153 70  ILE A CD1 
542  N N   . LEU A 85  ? 0.19157 0.14269 0.12073 -0.01319 -0.01512 0.00126  71  LEU A N   
543  C CA  . LEU A 85  ? 0.19444 0.15169 0.12379 -0.01482 -0.01613 0.00310  71  LEU A CA  
544  C C   . LEU A 85  ? 0.33709 0.28810 0.25352 -0.01898 -0.01728 0.00013  71  LEU A C   
545  O O   . LEU A 85  ? 0.37640 0.31812 0.28502 -0.01670 -0.01528 -0.00448 71  LEU A O   
546  C CB  . LEU A 85  ? 0.19624 0.15544 0.13039 -0.00934 -0.01392 0.00229  71  LEU A CB  
547  C CG  . LEU A 85  ? 0.28553 0.24849 0.23068 -0.00558 -0.01225 0.00400  71  LEU A CG  
548  C CD1 . LEU A 85  ? 0.23555 0.19745 0.18334 -0.00049 -0.01023 0.00173  71  LEU A CD1 
549  C CD2 . LEU A 85  ? 0.22009 0.19328 0.17530 -0.00728 -0.01260 0.00991  71  LEU A CD2 
550  N N   . LYS A 86  ? 0.45371 0.40970 0.36785 -0.02526 -0.02028 0.00302  72  LYS A N   
551  C CA  . LYS A 86  ? 0.52040 0.47070 0.42229 -0.03071 -0.02147 0.00024  72  LYS A CA  
552  C C   . LYS A 86  ? 0.54443 0.50558 0.44914 -0.03712 -0.02520 0.00551  72  LYS A C   
553  O O   . LYS A 86  ? 0.81129 0.77820 0.72123 -0.04046 -0.02792 0.01010  72  LYS A O   
554  C CB  . LYS A 86  ? 0.53044 0.47107 0.42788 -0.03216 -0.02052 -0.00305 72  LYS A CB  
555  C CG  . LYS A 86  ? 0.90044 0.83396 0.78967 -0.03525 -0.01899 -0.00661 72  LYS A CG  
556  C CD  . LYS A 86  ? 0.85536 0.78073 0.74092 -0.03792 -0.01855 -0.00828 72  LYS A CD  
557  C CE  . LYS A 86  ? 0.82378 0.74111 0.70053 -0.04080 -0.01646 -0.01167 72  LYS A CE  
558  N NZ  . LYS A 86  ? 0.52253 0.43325 0.39496 -0.04543 -0.01674 -0.01242 72  LYS A NZ  
559  N N   . PRO A 87  ? 0.63579 0.60077 0.53795 -0.03891 -0.02538 0.00572  73  PRO A N   
560  C CA  . PRO A 87  ? 0.97661 0.93584 0.87223 -0.03583 -0.02228 0.00130  73  PRO A CA  
561  C C   . PRO A 87  ? 0.84659 0.80350 0.74466 -0.02828 -0.01934 -0.00013 73  PRO A C   
562  O O   . PRO A 87  ? 0.56409 0.52780 0.47073 -0.02546 -0.01995 0.00363  73  PRO A O   
563  C CB  . PRO A 87  ? 0.93420 0.90306 0.83010 -0.03966 -0.02434 0.00482  73  PRO A CB  
564  C CG  . PRO A 87  ? 0.89783 0.87306 0.79650 -0.04672 -0.02825 0.00893  73  PRO A CG  
565  C CD  . PRO A 87  ? 0.77365 0.75021 0.67981 -0.04500 -0.02900 0.01144  73  PRO A CD  
566  N N   . VAL A 88  ? 0.73503 0.68264 0.62744 -0.02466 -0.01564 -0.00504 74  VAL A N   
567  C CA  . VAL A 88  ? 0.93985 0.88507 0.83463 -0.01766 -0.01279 -0.00624 74  VAL A CA  
568  C C   . VAL A 88  ? 0.89372 0.84462 0.78816 -0.01636 -0.01230 -0.00438 74  VAL A C   
569  O O   . VAL A 88  ? 0.84827 0.79435 0.73777 -0.01407 -0.00920 -0.00702 74  VAL A O   
570  C CB  . VAL A 88  ? 0.79037 0.72463 0.68181 -0.01398 -0.00888 -0.01075 74  VAL A CB  
571  C CG1 . VAL A 88  ? 0.74280 0.67579 0.63834 -0.00681 -0.00638 -0.01120 74  VAL A CG1 
572  C CG2 . VAL A 88  ? 0.48723 0.41689 0.37907 -0.01580 -0.00951 -0.01164 74  VAL A CG2 
573  N N   . LYS A 89  ? 0.70870 0.67132 0.61148 -0.01747 -0.01477 0.00100  75  LYS A N   
574  C CA  . LYS A 89  ? 0.35493 0.32567 0.26269 -0.01515 -0.01394 0.00413  75  LYS A CA  
575  C C   . LYS A 89  ? 0.45980 0.42929 0.37592 -0.00754 -0.01062 0.00308  75  LYS A C   
576  O O   . LYS A 89  ? 0.40871 0.38366 0.33719 -0.00485 -0.01065 0.00549  75  LYS A O   
577  C CB  . LYS A 89  ? 0.69724 0.68179 0.61603 -0.01767 -0.01675 0.01100  75  LYS A CB  
578  C CG  . LYS A 89  ? 0.63298 0.62053 0.54791 -0.02523 -0.02081 0.01332  75  LYS A CG  
579  C CD  . LYS A 89  ? 0.65440 0.64324 0.56097 -0.03008 -0.02197 0.01276  75  LYS A CD  
580  C CE  . LYS A 89  ? 0.68066 0.68009 0.59207 -0.02887 -0.02189 0.01761  75  LYS A CE  
581  N NZ  . LYS A 89  ? 0.62096 0.63465 0.54697 -0.02961 -0.02395 0.02582  75  LYS A NZ  
582  N N   . LYS A 90  ? 0.40571 0.36788 0.31503 -0.00426 -0.00753 -0.00033 76  LYS A N   
583  C CA  . LYS A 90  ? 0.46203 0.42138 0.37777 0.00231  -0.00476 -0.00173 76  LYS A CA  
584  C C   . LYS A 90  ? 0.38736 0.35689 0.31720 0.00573  -0.00455 0.00222  76  LYS A C   
585  O O   . LYS A 90  ? 0.27117 0.24132 0.20974 0.00927  -0.00394 0.00208  76  LYS A O   
586  C CB  . LYS A 90  ? 0.39280 0.34316 0.29916 0.00516  -0.00105 -0.00498 76  LYS A CB  
587  C CG  . LYS A 90  ? 0.80546 0.74338 0.70186 0.00466  0.00043  -0.00938 76  LYS A CG  
588  C CD  . LYS A 90  ? 0.99182 0.92167 0.88275 0.00899  0.00531  -0.01149 76  LYS A CD  
589  C CE  . LYS A 90  ? 0.93222 0.85502 0.82512 0.01153  0.00719  -0.01325 76  LYS A CE  
590  N NZ  . LYS A 90  ? 0.95523 0.87359 0.84433 0.00641  0.00609  -0.01503 76  LYS A NZ  
591  N N   . LYS A 91  ? 0.29737 0.27483 0.22933 0.00444  -0.00496 0.00584  77  LYS A N   
592  C CA  . LYS A 91  ? 0.24886 0.23547 0.19446 0.00776  -0.00414 0.00980  77  LYS A CA  
593  C C   . LYS A 91  ? 0.26881 0.26174 0.22555 0.00662  -0.00568 0.01283  77  LYS A C   
594  O O   . LYS A 91  ? 0.24081 0.23611 0.20835 0.00993  -0.00438 0.01361  77  LYS A O   
595  C CB  . LYS A 91  ? 0.37703 0.37029 0.32136 0.00687  -0.00376 0.01328  77  LYS A CB  
596  C CG  . LYS A 91  ? 0.43922 0.44150 0.39742 0.01054  -0.00228 0.01762  77  LYS A CG  
597  C CD  . LYS A 91  ? 0.54762 0.55644 0.50347 0.00967  -0.00182 0.02136  77  LYS A CD  
598  C CE  . LYS A 91  ? 0.39650 0.41615 0.36784 0.01221  -0.00075 0.02710  77  LYS A CE  
599  N NZ  . LYS A 91  ? 0.49254 0.52035 0.46191 0.01054  -0.00090 0.03191  77  LYS A NZ  
600  N N   . LYS A 92  ? 0.25123 0.24654 0.20533 0.00175  -0.00819 0.01462  78  LYS A N   
601  C CA  . LYS A 92  ? 0.23463 0.23526 0.19906 0.00083  -0.00895 0.01794  78  LYS A CA  
602  C C   . LYS A 92  ? 0.20413 0.19759 0.16998 0.00302  -0.00811 0.01411  78  LYS A C   
603  O O   . LYS A 92  ? 0.20196 0.19825 0.17795 0.00454  -0.00697 0.01584  78  LYS A O   
604  C CB  . LYS A 92  ? 0.30125 0.30579 0.26159 -0.00519 -0.01206 0.02097  78  LYS A CB  
605  C CG  . LYS A 92  ? 0.45471 0.46869 0.42755 -0.00638 -0.01246 0.02732  78  LYS A CG  
606  C CD  . LYS A 92  ? 0.48773 0.50718 0.45648 -0.01289 -0.01613 0.03130  78  LYS A CD  
607  C CE  . LYS A 92  ? 0.41979 0.44771 0.40150 -0.01376 -0.01609 0.03799  78  LYS A CE  
608  N NZ  . LYS A 92  ? 0.37356 0.39437 0.35821 -0.01147 -0.01426 0.03493  78  LYS A NZ  
609  N N   . ILE A 93  ? 0.20390 0.18780 0.15948 0.00322  -0.00824 0.00906  79  ILE A N   
610  C CA  . ILE A 93  ? 0.16167 0.13919 0.11764 0.00506  -0.00772 0.00581  79  ILE A CA  
611  C C   . ILE A 93  ? 0.14519 0.12295 0.10854 0.00977  -0.00577 0.00486  79  ILE A C   
612  O O   . ILE A 93  ? 0.14259 0.12046 0.11226 0.01083  -0.00524 0.00465  79  ILE A O   
613  C CB  . ILE A 93  ? 0.21227 0.17993 0.15572 0.00402  -0.00807 0.00151  79  ILE A CB  
614  C CG1 . ILE A 93  ? 0.21749 0.18456 0.15499 -0.00154 -0.01038 0.00230  79  ILE A CG1 
615  C CG2 . ILE A 93  ? 0.17185 0.13342 0.11579 0.00713  -0.00713 -0.00154 79  ILE A CG2 
616  C CD1 . ILE A 93  ? 0.29135 0.24828 0.21548 -0.00348 -0.01033 -0.00183 79  ILE A CD1 
617  N N   . LYS A 94  ? 0.16598 0.14368 0.12834 0.01235  -0.00458 0.00433  80  LYS A N   
618  C CA  . LYS A 94  ? 0.14640 0.12538 0.11649 0.01621  -0.00316 0.00401  80  LYS A CA  
619  C C   . LYS A 94  ? 0.11312 0.09943 0.09516 0.01634  -0.00242 0.00728  80  LYS A C   
620  O O   . LYS A 94  ? 0.11239 0.09848 0.10091 0.01796  -0.00160 0.00638  80  LYS A O   
621  C CB  . LYS A 94  ? 0.21011 0.18853 0.17781 0.01898  -0.00173 0.00384  80  LYS A CB  
622  C CG  . LYS A 94  ? 0.33652 0.30656 0.29232 0.01922  -0.00123 0.00083  80  LYS A CG  
623  C CD  . LYS A 94  ? 0.40250 0.37153 0.35681 0.02272  0.00119  0.00109  80  LYS A CD  
624  C CE  . LYS A 94  ? 0.40682 0.37703 0.36918 0.02647  0.00174  0.00127  80  LYS A CE  
625  N NZ  . LYS A 94  ? 0.53768 0.50225 0.49709 0.02661  0.00085  -0.00120 80  LYS A NZ  
626  N N   . ARG A 95  ? 0.12616 0.11895 0.11117 0.01443  -0.00251 0.01131  81  ARG A N   
627  C CA  . ARG A 95  ? 0.09435 0.09404 0.09168 0.01484  -0.00097 0.01524  81  ARG A CA  
628  C C   . ARG A 95  ? 0.09556 0.09310 0.09683 0.01401  -0.00037 0.01467  81  ARG A C   
629  O O   . ARG A 95  ? 0.10515 0.10270 0.11442 0.01556  0.00175  0.01445  81  ARG A O   
630  C CB  . ARG A 95  ? 0.15094 0.15883 0.15049 0.01276  -0.00137 0.02067  81  ARG A CB  
631  C CG  . ARG A 95  ? 0.11940 0.13531 0.13296 0.01392  0.00105  0.02594  81  ARG A CG  
632  C CD  . ARG A 95  ? 0.09900 0.12433 0.11457 0.01165  0.00021  0.03234  81  ARG A CD  
633  N NE  . ARG A 95  ? 0.15654 0.18362 0.17004 0.00791  -0.00168 0.03463  81  ARG A NE  
634  C CZ  . ARG A 95  ? 0.17119 0.20694 0.18567 0.00477  -0.00335 0.04058  81  ARG A CZ  
635  N NH1 . ARG A 95  ? 0.14192 0.18501 0.15779 0.00482  -0.00347 0.04451  81  ARG A NH1 
636  N NH2 . ARG A 95  ? 0.14749 0.18516 0.16167 0.00133  -0.00506 0.04308  81  ARG A NH2 
637  N N   . GLU A 96  ? 0.07437 0.06943 0.06962 0.01137  -0.00195 0.01426  82  GLU A N   
638  C CA  . GLU A 96  ? 0.09883 0.09165 0.09732 0.01076  -0.00094 0.01408  82  GLU A CA  
639  C C   . GLU A 96  ? 0.11306 0.09878 0.10938 0.01266  -0.00035 0.00903  82  GLU A C   
640  O O   . GLU A 96  ? 0.10373 0.08832 0.10582 0.01334  0.00188  0.00865  82  GLU A O   
641  C CB  . GLU A 96  ? 0.11084 0.10272 0.10334 0.00744  -0.00295 0.01501  82  GLU A CB  
642  C CG  . GLU A 96  ? 0.08483 0.07443 0.08082 0.00711  -0.00140 0.01537  82  GLU A CG  
643  C CD  . GLU A 96  ? 0.15538 0.14569 0.14778 0.00364  -0.00327 0.01765  82  GLU A CD  
644  O OE1 . GLU A 96  ? 0.14573 0.13806 0.13227 0.00084  -0.00611 0.01861  82  GLU A OE1 
645  O OE2 . GLU A 96  ? 0.17630 0.16495 0.17150 0.00346  -0.00177 0.01852  82  GLU A OE2 
646  N N   . ILE A 97  ? 0.14247 0.12338 0.13045 0.01346  -0.00206 0.00540  83  ILE A N   
647  C CA  . ILE A 97  ? 0.12269 0.09813 0.10840 0.01501  -0.00212 0.00142  83  ILE A CA  
648  C C   . ILE A 97  ? 0.10913 0.08680 0.10275 0.01671  -0.00067 0.00123  83  ILE A C   
649  O O   . ILE A 97  ? 0.10053 0.07548 0.09594 0.01661  0.00009  -0.00084 83  ILE A O   
650  C CB  . ILE A 97  ? 0.09989 0.07069 0.07643 0.01594  -0.00373 -0.00113 83  ILE A CB  
651  C CG1 . ILE A 97  ? 0.12179 0.08811 0.09008 0.01383  -0.00487 -0.00198 83  ILE A CG1 
652  C CG2 . ILE A 97  ? 0.14205 0.11006 0.11861 0.01796  -0.00397 -0.00371 83  ILE A CG2 
653  C CD1 . ILE A 97  ? 0.17284 0.13372 0.13192 0.01463  -0.00546 -0.00409 83  ILE A CD1 
654  N N   . LYS A 98  ? 0.09221 0.07454 0.09015 0.01796  -0.00021 0.00330  84  LYS A N   
655  C CA  . LYS A 98  ? 0.08553 0.07004 0.09150 0.01932  0.00110  0.00330  84  LYS A CA  
656  C C   . LYS A 98  ? 0.08235 0.06839 0.09685 0.01840  0.00387  0.00480  84  LYS A C   
657  O O   . LYS A 98  ? 0.11675 0.10067 0.13515 0.01825  0.00510  0.00281  84  LYS A O   
658  C CB  . LYS A 98  ? 0.08656 0.07595 0.09557 0.02109  0.00135  0.00578  84  LYS A CB  
659  C CG  . LYS A 98  ? 0.12651 0.11848 0.14450 0.02239  0.00257  0.00616  84  LYS A CG  
660  C CD  . LYS A 98  ? 0.17100 0.15895 0.18647 0.02249  0.00097  0.00258  84  LYS A CD  
661  C CE  . LYS A 98  ? 0.17916 0.17005 0.20299 0.02315  0.00146  0.00310  84  LYS A CE  
662  N NZ  . LYS A 98  ? 0.23519 0.22338 0.25630 0.02256  -0.00082 0.00030  84  LYS A NZ  
663  N N   . ILE A 99  ? 0.09237 0.08196 0.10984 0.01755  0.00512  0.00856  85  ILE A N   
664  C CA  . ILE A 99  ? 0.07820 0.06899 0.10448 0.01717  0.00875  0.01088  85  ILE A CA  
665  C C   . ILE A 99  ? 0.10435 0.08812 0.12741 0.01617  0.00985  0.00729  85  ILE A C   
666  O O   . ILE A 99  ? 0.09492 0.07582 0.12288 0.01610  0.01300  0.00598  85  ILE A O   
667  C CB  . ILE A 99  ? 0.07909 0.07638 0.10939 0.01645  0.00948  0.01681  85  ILE A CB  
668  C CG1 . ILE A 99  ? 0.06493 0.06965 0.10094 0.01757  0.00967  0.02080  85  ILE A CG1 
669  C CG2 . ILE A 99  ? 0.05516 0.05238 0.09301 0.01612  0.01356  0.01960  85  ILE A CG2 
670  C CD1 . ILE A 99  ? 0.07016 0.08295 0.10966 0.01641  0.00960  0.02737  85  ILE A CD1 
671  N N   . LEU A 100 ? 0.08430 0.06456 0.09845 0.01525  0.00753  0.00540  86  LEU A N   
672  C CA  . LEU A 100 ? 0.08589 0.05956 0.09601 0.01442  0.00854  0.00209  86  LEU A CA  
673  C C   . LEU A 100 ? 0.14499 0.11439 0.15263 0.01443  0.00789  -0.00263 86  LEU A C   
674  O O   . LEU A 100 ? 0.15083 0.11568 0.15898 0.01350  0.01038  -0.00496 86  LEU A O   
675  C CB  . LEU A 100 ? 0.09188 0.06313 0.09330 0.01353  0.00604  0.00145  86  LEU A CB  
676  C CG  . LEU A 100 ? 0.09465 0.06941 0.09870 0.01244  0.00691  0.00611  86  LEU A CG  
677  C CD1 . LEU A 100 ? 0.13092 0.10363 0.12600 0.01107  0.00368  0.00538  86  LEU A CD1 
678  C CD2 . LEU A 100 ? 0.14288 0.11587 0.15258 0.01243  0.01140  0.00762  86  LEU A CD2 
679  N N   . GLU A 101 ? 0.14441 0.11523 0.14929 0.01524  0.00473  -0.00383 87  GLU A N   
680  C CA  . GLU A 101 ? 0.17816 0.14689 0.18228 0.01487  0.00360  -0.00715 87  GLU A CA  
681  C C   . GLU A 101 ? 0.11407 0.08342 0.12680 0.01419  0.00663  -0.00712 87  GLU A C   
682  O O   . GLU A 101 ? 0.13062 0.09560 0.14222 0.01232  0.00745  -0.01045 87  GLU A O   
683  C CB  . GLU A 101 ? 0.21578 0.18717 0.21760 0.01639  0.00033  -0.00696 87  GLU A CB  
684  C CG  . GLU A 101 ? 0.23103 0.20289 0.23497 0.01592  -0.00109 -0.00877 87  GLU A CG  
685  C CD  . GLU A 101 ? 0.33609 0.31116 0.33916 0.01802  -0.00362 -0.00744 87  GLU A CD  
686  O OE1 . GLU A 101 ? 0.38514 0.35824 0.38117 0.01886  -0.00551 -0.00798 87  GLU A OE1 
687  O OE2 . GLU A 101 ? 0.37546 0.35483 0.38531 0.01908  -0.00320 -0.00550 87  GLU A OE2 
688  N N   . ASN A 102 ? 0.10350 0.07799 0.12454 0.01542  0.00846  -0.00337 88  ASN A N   
689  C CA  . ASN A 102 ? 0.12825 0.10306 0.15841 0.01495  0.01192  -0.00292 88  ASN A CA  
690  C C   . ASN A 102 ? 0.10629 0.07563 0.13808 0.01362  0.01658  -0.00394 88  ASN A C   
691  O O   . ASN A 102 ? 0.14544 0.11147 0.18177 0.01234  0.01972  -0.00568 88  ASN A O   
692  C CB  . ASN A 102 ? 0.09266 0.07466 0.13173 0.01688  0.01336  0.00225  88  ASN A CB  
693  C CG  . ASN A 102 ? 0.13150 0.11795 0.17006 0.01832  0.01009  0.00299  88  ASN A CG  
694  O OD1 . ASN A 102 ? 0.13697 0.12147 0.17080 0.01792  0.00716  -0.00002 88  ASN A OD1 
695  N ND2 . ASN A 102 ? 0.10097 0.09377 0.14460 0.02006  0.01078  0.00751  88  ASN A ND2 
696  N N   . LEU A 103 ? 0.08503 0.08134 0.08967 0.01533  -0.01626 -0.00765 89  LEU A N   
697  C CA  . LEU A 103 ? 0.07591 0.07209 0.08011 0.01429  -0.01618 -0.00736 89  LEU A CA  
698  C C   . LEU A 103 ? 0.13274 0.12569 0.13369 0.01546  -0.01711 -0.00724 89  LEU A C   
699  O O   . LEU A 103 ? 0.17660 0.16898 0.17662 0.01500  -0.01713 -0.00696 89  LEU A O   
700  C CB  . LEU A 103 ? 0.10465 0.10042 0.10876 0.01367  -0.01625 -0.00767 89  LEU A CB  
701  C CG  . LEU A 103 ? 0.09567 0.09509 0.10253 0.01258  -0.01524 -0.00771 89  LEU A CG  
702  C CD1 . LEU A 103 ? 0.13630 0.13556 0.14320 0.01222  -0.01585 -0.00854 89  LEU A CD1 
703  C CD2 . LEU A 103 ? 0.12026 0.12294 0.12930 0.01109  -0.01373 -0.00642 89  LEU A CD2 
704  N N   . ARG A 104 ? 0.10340 0.09429 0.10240 0.01716  -0.01777 -0.00729 90  ARG A N   
705  C CA  . ARG A 104 ? 0.13901 0.12629 0.13394 0.01875  -0.01846 -0.00687 90  ARG A CA  
706  C C   . ARG A 104 ? 0.13793 0.12672 0.13306 0.01840  -0.01869 -0.00702 90  ARG A C   
707  O O   . ARG A 104 ? 0.20636 0.19836 0.20456 0.01767  -0.01867 -0.00757 90  ARG A O   
708  C CB  . ARG A 104 ? 0.23910 0.22488 0.23258 0.02069  -0.01900 -0.00689 90  ARG A CB  
709  C CG  . ARG A 104 ? 0.42886 0.41040 0.41741 0.02277  -0.01946 -0.00618 90  ARG A CG  
710  C CD  . ARG A 104 ? 0.63795 0.61918 0.62583 0.02476  -0.02019 -0.00636 90  ARG A CD  
711  N NE  . ARG A 104 ? 0.88853 0.86619 0.87152 0.02701  -0.02069 -0.00568 90  ARG A NE  
712  C CZ  . ARG A 104 ? 0.77374 0.75188 0.75588 0.02895  -0.02182 -0.00610 90  ARG A CZ  
713  N NH1 . ARG A 104 ? 0.65135 0.63329 0.63757 0.02879  -0.02253 -0.00714 90  ARG A NH1 
714  N NH2 . ARG A 104 ? 0.87105 0.84568 0.84803 0.03126  -0.02217 -0.00538 90  ARG A NH2 
715  N N   . GLY A 105 ? 0.14256 0.12856 0.13419 0.01908  -0.01882 -0.00645 91  GLY A N   
716  C CA  . GLY A 105 ? 0.22274 0.20980 0.21403 0.01907  -0.01910 -0.00676 91  GLY A CA  
717  C C   . GLY A 105 ? 0.18545 0.17561 0.18019 0.01694  -0.01835 -0.00692 91  GLY A C   
718  O O   . GLY A 105 ? 0.19772 0.18860 0.19230 0.01696  -0.01853 -0.00728 91  GLY A O   
719  N N   . GLY A 106 ? 0.20116 0.19305 0.19875 0.01534  -0.01752 -0.00671 92  GLY A N   
720  C CA  . GLY A 106 ? 0.17870 0.17350 0.17927 0.01348  -0.01656 -0.00655 92  GLY A CA  
721  C C   . GLY A 106 ? 0.11538 0.10886 0.11401 0.01362  -0.01664 -0.00607 92  GLY A C   
722  O O   . GLY A 106 ? 0.13796 0.12801 0.13338 0.01469  -0.01712 -0.00549 92  GLY A O   
723  N N   . THR A 107 ? 0.15317 0.14893 0.15359 0.01265  -0.01606 -0.00608 93  THR A N   
724  C CA  . THR A 107 ? 0.14357 0.13865 0.14240 0.01294  -0.01613 -0.00563 93  THR A CA  
725  C C   . THR A 107 ? 0.15342 0.14877 0.15308 0.01212  -0.01595 -0.00500 93  THR A C   
726  O O   . THR A 107 ? 0.11641 0.11500 0.11967 0.01040  -0.01511 -0.00503 93  THR A O   
727  C CB  . THR A 107 ? 0.18741 0.18521 0.18865 0.01197  -0.01548 -0.00591 93  THR A CB  
728  O OG1 . THR A 107 ? 0.25951 0.25699 0.26056 0.01271  -0.01609 -0.00689 93  THR A OG1 
729  C CG2 . THR A 107 ? 0.19638 0.19361 0.19569 0.01267  -0.01567 -0.00558 93  THR A CG2 
730  N N   . ASN A 108 ? 0.12666 0.11811 0.12251 0.01352  -0.01662 -0.00420 94  ASN A N   
731  C CA  . ASN A 108 ? 0.08752 0.07829 0.08386 0.01183  -0.01555 -0.00366 94  ASN A CA  
732  C C   . ASN A 108 ? 0.09542 0.08595 0.09345 0.01054  -0.01533 -0.00429 94  ASN A C   
733  O O   . ASN A 108 ? 0.12403 0.11573 0.12392 0.00784  -0.01379 -0.00459 94  ASN A O   
734  C CB  . ASN A 108 ? 0.11178 0.10743 0.11174 0.00990  -0.01471 -0.00374 94  ASN A CB  
735  C CG  . ASN A 108 ? 0.13141 0.12614 0.12868 0.01107  -0.01426 -0.00313 94  ASN A CG  
736  O OD1 . ASN A 108 ? 0.15682 0.14662 0.14868 0.01270  -0.01370 -0.00231 94  ASN A OD1 
737  N ND2 . ASN A 108 ? 0.14817 0.14739 0.14878 0.01065  -0.01450 -0.00349 94  ASN A ND2 
738  N N   . ILE A 109 ? 0.10542 0.09470 0.10300 0.01245  -0.01686 -0.00474 95  ILE A N   
739  C CA  . ILE A 109 ? 0.09966 0.08760 0.09773 0.01168  -0.01647 -0.00544 95  ILE A CA  
740  C C   . ILE A 109 ? 0.12169 0.10224 0.11472 0.01219  -0.01508 -0.00466 95  ILE A C   
741  O O   . ILE A 109 ? 0.12572 0.10257 0.11475 0.01473  -0.01557 -0.00366 95  ILE A O   
742  C CB  . ILE A 109 ? 0.11483 0.10572 0.11516 0.01273  -0.01753 -0.00624 95  ILE A CB  
743  C CG1 . ILE A 109 ? 0.18094 0.17789 0.18542 0.01062  -0.01621 -0.00637 95  ILE A CG1 
744  C CG2 . ILE A 109 ? 0.10528 0.09360 0.10529 0.01357  -0.01808 -0.00704 95  ILE A CG2 
745  C CD1 . ILE A 109 ? 0.23307 0.23221 0.23913 0.01031  -0.01515 -0.00643 95  ILE A CD1 
746  N N   . ILE A 110 ? 0.08958 0.06786 0.08279 0.00986  -0.01333 -0.00515 96  ILE A N   
747  C CA  . ILE A 110 ? 0.09452 0.06517 0.08346 0.01000  -0.01149 -0.00426 96  ILE A CA  
748  C C   . ILE A 110 ? 0.12556 0.09235 0.11122 0.01364  -0.01288 -0.00386 96  ILE A C   
749  O O   . ILE A 110 ? 0.15911 0.12858 0.14692 0.01491  -0.01470 -0.00505 96  ILE A O   
750  C CB  . ILE A 110 ? 0.09893 0.06826 0.08987 0.00681  -0.00982 -0.00559 96  ILE A CB  
751  C CG1 . ILE A 110 ? 0.10597 0.06702 0.09322 0.00627  -0.00716 -0.00434 96  ILE A CG1 
752  C CG2 . ILE A 110 ? 0.09594 0.06688 0.08875 0.00740  -0.01135 -0.00754 96  ILE A CG2 
753  C CD1 . ILE A 110 ? 0.10698 0.06677 0.09298 0.00498  -0.00481 -0.00248 96  ILE A CD1 
754  N N   . LYS A 111 ? 0.13540 0.09615 0.11580 0.01563  -0.01198 -0.00204 97  LYS A N   
755  C CA  . LYS A 111 ? 0.17202 0.13054 0.14940 0.01899  -0.01314 -0.00150 97  LYS A CA  
756  C C   . LYS A 111 ? 0.17684 0.13028 0.15328 0.01879  -0.01183 -0.00172 97  LYS A C   
757  O O   . LYS A 111 ? 0.15442 0.10104 0.12851 0.01752  -0.00934 -0.00090 97  LYS A O   
758  C CB  . LYS A 111 ? 0.25610 0.21213 0.22844 0.02085  -0.01237 0.00047  97  LYS A CB  
759  C CG  . LYS A 111 ? 0.32127 0.27743 0.29153 0.02321  -0.01313 0.00066  97  LYS A CG  
760  C CD  . LYS A 111 ? 0.31047 0.26559 0.27599 0.02537  -0.01306 0.00189  97  LYS A CD  
761  C CE  . LYS A 111 ? 0.45039 0.39851 0.41083 0.02548  -0.01012 0.00435  97  LYS A CE  
762  N NZ  . LYS A 111 ? 0.77918 0.72602 0.73415 0.02822  -0.00996 0.00555  97  LYS A NZ  
763  N N   . LEU A 112 ? 0.11852 0.07530 0.09708 0.01972  -0.01316 -0.00285 98  LEU A N   
764  C CA  . LEU A 112 ? 0.16663 0.11906 0.14415 0.02013  -0.01209 -0.00307 98  LEU A CA  
765  C C   . LEU A 112 ? 0.14600 0.09568 0.11954 0.02266  -0.01172 -0.00127 98  LEU A C   
766  O O   . LEU A 112 ? 0.22802 0.18219 0.20183 0.02439  -0.01347 -0.00136 98  LEU A O   
767  C CB  . LEU A 112 ? 0.18860 0.14574 0.16987 0.02024  -0.01348 -0.00500 98  LEU A CB  
768  C CG  . LEU A 112 ? 0.15614 0.10971 0.13677 0.02095  -0.01261 -0.00559 98  LEU A CG  
769  C CD1 . LEU A 112 ? 0.10881 0.05691 0.08945 0.01855  -0.01072 -0.00682 98  LEU A CD1 
770  C CD2 . LEU A 112 ? 0.13186 0.09112 0.11563 0.02183  -0.01409 -0.00700 98  LEU A CD2 
771  N N   . ILE A 113 ? 0.16831 0.11063 0.13845 0.02264  -0.00934 0.00018  99  ILE A N   
772  C CA  . ILE A 113 ? 0.16877 0.10768 0.13456 0.02522  -0.00873 0.00213  99  ILE A CA  
773  C C   . ILE A 113 ? 0.14435 0.08197 0.11051 0.02669  -0.00895 0.00164  99  ILE A C   
774  O O   . ILE A 113 ? 0.17969 0.11806 0.14379 0.02934  -0.00994 0.00234  99  ILE A O   
775  C CB  . ILE A 113 ? 0.20669 0.13820 0.16878 0.02437  -0.00556 0.00432  99  ILE A CB  
776  C CG1 . ILE A 113 ? 0.23846 0.17139 0.19914 0.02376  -0.00529 0.00525  99  ILE A CG1 
777  C CG2 . ILE A 113 ? 0.23929 0.16575 0.19680 0.02696  -0.00432 0.00642  99  ILE A CG2 
778  C CD1 . ILE A 113 ? 0.22102 0.14709 0.17861 0.02245  -0.00157 0.00755  99  ILE A CD1 
779  N N   . ASP A 114 ? 0.13341 0.06907 0.10215 0.02508  -0.00807 0.00021  100 ASP A N   
780  C CA  . ASP A 114 ? 0.13877 0.07194 0.10745 0.02653  -0.00776 -0.00011 100 ASP A CA  
781  C C   . ASP A 114 ? 0.14948 0.08326 0.12189 0.02464  -0.00757 -0.00267 100 ASP A C   
782  O O   . ASP A 114 ? 0.15797 0.09258 0.13246 0.02195  -0.00726 -0.00407 100 ASP A O   
783  C CB  . ASP A 114 ? 0.17259 0.09763 0.13758 0.02722  -0.00527 0.00196  100 ASP A CB  
784  C CG  . ASP A 114 ? 0.20871 0.13239 0.17182 0.03042  -0.00577 0.00271  100 ASP A CG  
785  O OD1 . ASP A 114 ? 0.19842 0.12663 0.16381 0.03160  -0.00759 0.00125  100 ASP A OD1 
786  O OD2 . ASP A 114 ? 0.20881 0.12677 0.16811 0.03182  -0.00417 0.00487  100 ASP A OD2 
787  N N   . ILE A 115 ? 0.14157 0.07502 0.11459 0.02619  -0.00781 -0.00343 101 ILE A N   
788  C CA  . ILE A 115 ? 0.15923 0.09246 0.13492 0.02499  -0.00742 -0.00596 101 ILE A CA  
789  C C   . ILE A 115 ? 0.16462 0.09178 0.13897 0.02636  -0.00594 -0.00563 101 ILE A C   
790  O O   . ILE A 115 ? 0.17664 0.10430 0.14957 0.02926  -0.00668 -0.00439 101 ILE A O   
791  C CB  . ILE A 115 ? 0.14022 0.08101 0.11855 0.02597  -0.00955 -0.00742 101 ILE A CB  
792  C CG1 . ILE A 115 ? 0.13969 0.08680 0.11969 0.02496  -0.01115 -0.00745 101 ILE A CG1 
793  C CG2 . ILE A 115 ? 0.17916 0.11971 0.15946 0.02495  -0.00904 -0.01014 101 ILE A CG2 
794  C CD1 . ILE A 115 ? 0.20220 0.15679 0.18519 0.02590  -0.01296 -0.00840 101 ILE A CD1 
795  N N   . VAL A 116 ? 0.15907 0.08053 0.13420 0.02417  -0.00389 -0.00686 102 VAL A N   
796  C CA  . VAL A 116 ? 0.16050 0.07539 0.13471 0.02521  -0.00230 -0.00650 102 VAL A CA  
797  C C   . VAL A 116 ? 0.15204 0.06530 0.12914 0.02345  -0.00149 -0.00993 102 VAL A C   
798  O O   . VAL A 116 ? 0.15407 0.07058 0.13340 0.02105  -0.00188 -0.01249 102 VAL A O   
799  C CB  . VAL A 116 ? 0.13953 0.04747 0.11146 0.02445  -0.00019 -0.00406 102 VAL A CB  
800  C CG1 . VAL A 116 ? 0.18897 0.09879 0.15722 0.02660  -0.00098 -0.00090 102 VAL A CG1 
801  C CG2 . VAL A 116 ? 0.14684 0.05270 0.12112 0.02017  0.00128  -0.00546 102 VAL A CG2 
802  N N   . LYS A 117 ? 0.18914 0.09734 0.16600 0.02477  -0.00044 -0.01012 103 LYS A N   
803  C CA  . LYS A 117 ? 0.16847 0.07412 0.14803 0.02299  0.00053  -0.01362 103 LYS A CA  
804  C C   . LYS A 117 ? 0.19971 0.09706 0.17907 0.02336  0.00227  -0.01304 103 LYS A C   
805  O O   . LYS A 117 ? 0.19335 0.08755 0.16983 0.02599  0.00258  -0.00989 103 LYS A O   
806  C CB  . LYS A 117 ? 0.20908 0.11966 0.18928 0.02470  -0.00067 -0.01583 103 LYS A CB  
807  C CG  . LYS A 117 ? 0.24414 0.15486 0.22270 0.02874  -0.00129 -0.01409 103 LYS A CG  
808  C CD  . LYS A 117 ? 0.26838 0.18470 0.24783 0.03030  -0.00248 -0.01606 103 LYS A CD  
809  C CE  . LYS A 117 ? 0.41010 0.32769 0.38851 0.03423  -0.00331 -0.01416 103 LYS A CE  
810  N NZ  . LYS A 117 ? 0.41270 0.33573 0.39233 0.03586  -0.00427 -0.01581 103 LYS A NZ  
811  N N   . ASP A 118 ? 0.18735 0.08127 0.16978 0.02069  0.00322  -0.01627 104 ASP A N   
812  C CA  . ASP A 118 ? 0.19657 0.08270 0.17946 0.02101  0.00448  -0.01649 104 ASP A CA  
813  C C   . ASP A 118 ? 0.20807 0.09453 0.18985 0.02481  0.00416  -0.01669 104 ASP A C   
814  O O   . ASP A 118 ? 0.19591 0.08687 0.17890 0.02516  0.00350  -0.01955 104 ASP A O   
815  C CB  . ASP A 118 ? 0.23445 0.11849 0.22157 0.01721  0.00462  -0.02089 104 ASP A CB  
816  C CG  . ASP A 118 ? 0.31764 0.19292 0.30535 0.01705  0.00550  -0.02148 104 ASP A CG  
817  O OD1 . ASP A 118 ? 0.29178 0.16428 0.27820 0.02022  0.00598  -0.02079 104 ASP A OD1 
818  O OD2 . ASP A 118 ? 0.28952 0.16041 0.27857 0.01364  0.00564  -0.02259 104 ASP A OD2 
819  N N   . PRO A 119 ? 0.23267 0.11466 0.21174 0.02781  0.00468  -0.01363 105 PRO A N   
820  C CA  . PRO A 119 ? 0.26245 0.14525 0.24059 0.03158  0.00418  -0.01373 105 PRO A CA  
821  C C   . PRO A 119 ? 0.31603 0.19598 0.29695 0.03111  0.00485  -0.01768 105 PRO A C   
822  O O   . PRO A 119 ? 0.28498 0.16745 0.26568 0.03372  0.00439  -0.01870 105 PRO A O   
823  C CB  . PRO A 119 ? 0.25430 0.13176 0.22892 0.03443  0.00484  -0.00969 105 PRO A CB  
824  C CG  . PRO A 119 ? 0.44653 0.32193 0.41936 0.03255  0.00561  -0.00701 105 PRO A CG  
825  C CD  . PRO A 119 ? 0.31600 0.19202 0.29230 0.02798  0.00595  -0.00984 105 PRO A CD  
826  N N   . VAL A 120 ? 0.24865 0.12351 0.23224 0.02790  0.00576  -0.02008 106 VAL A N   
827  C CA  . VAL A 120 ? 0.20429 0.07601 0.19072 0.02742  0.00618  -0.02432 106 VAL A CA  
828  C C   . VAL A 120 ? 0.27081 0.14833 0.25995 0.02484  0.00579  -0.02893 106 VAL A C   
829  O O   . VAL A 120 ? 0.23610 0.11621 0.22518 0.02616  0.00607  -0.03152 106 VAL A O   
830  C CB  . VAL A 120 ? 0.23110 0.09341 0.21863 0.02563  0.00690  -0.02456 106 VAL A CB  
831  C CG1 . VAL A 120 ? 0.21544 0.07405 0.20565 0.02578  0.00687  -0.02900 106 VAL A CG1 
832  C CG2 . VAL A 120 ? 0.30017 0.15670 0.28376 0.02809  0.00809  -0.01930 106 VAL A CG2 
833  N N   . SER A 121 ? 0.20800 0.08765 0.19887 0.02121  0.00531  -0.02987 107 SER A N   
834  C CA  . SER A 121 ? 0.24608 0.13108 0.23904 0.01847  0.00538  -0.03431 107 SER A CA  
835  C C   . SER A 121 ? 0.21430 0.10721 0.20364 0.01955  0.00494  -0.03299 107 SER A C   
836  O O   . SER A 121 ? 0.28695 0.18380 0.27486 0.01849  0.00499  -0.03592 107 SER A O   
837  C CB  . SER A 121 ? 0.21887 0.10404 0.21442 0.01417  0.00404  -0.03549 107 SER A CB  
838  O OG  . SER A 121 ? 0.22623 0.11398 0.22056 0.01360  0.00373  -0.03223 107 SER A OG  
839  N N   . LYS A 122 ? 0.20173 0.09682 0.18878 0.02174  0.00393  -0.02858 108 LYS A N   
840  C CA  . LYS A 122 ? 0.23131 0.13407 0.21593 0.02314  0.00232  -0.02701 108 LYS A CA  
841  C C   . LYS A 122 ? 0.24389 0.15098 0.22900 0.01991  0.00169  -0.02776 108 LYS A C   
842  O O   . LYS A 122 ? 0.24897 0.16274 0.23275 0.02084  -0.00004 -0.02704 108 LYS A O   
843  C CB  . LYS A 122 ? 0.25899 0.16592 0.24224 0.02574  0.00152  -0.02853 108 LYS A CB  
844  C CG  . LYS A 122 ? 0.26836 0.17111 0.25135 0.02885  0.00229  -0.02831 108 LYS A CG  
845  C CD  . LYS A 122 ? 0.27387 0.17509 0.25576 0.03153  0.00186  -0.02395 108 LYS A CD  
846  C CE  . LYS A 122 ? 0.34699 0.24453 0.32843 0.03488  0.00243  -0.02368 108 LYS A CE  
847  N NZ  . LYS A 122 ? 0.42607 0.32267 0.40575 0.03771  0.00183  -0.01949 108 LYS A NZ  
848  N N   . THR A 123 ? 0.20216 0.10594 0.18979 0.01620  0.00280  -0.02920 109 THR A N   
849  C CA  . THR A 123 ? 0.18822 0.09607 0.17626 0.01305  0.00231  -0.02982 109 THR A CA  
850  C C   . THR A 123 ? 0.17477 0.08522 0.16150 0.01433  0.00117  -0.02560 109 THR A C   
851  O O   . THR A 123 ? 0.20552 0.11161 0.19195 0.01527  0.00171  -0.02258 109 THR A O   
852  C CB  . THR A 123 ? 0.21493 0.11925 0.20701 0.00884  0.00345  -0.03187 109 THR A CB  
853  O OG1 . THR A 123 ? 0.27845 0.18064 0.27031 0.00733  0.00481  -0.03554 109 THR A OG1 
854  C CG2 . THR A 123 ? 0.26351 0.17224 0.25498 0.00538  0.00328  -0.03206 109 THR A CG2 
855  N N   . PRO A 124 ? 0.19689 0.11422 0.18238 0.01455  -0.00060 -0.02521 110 PRO A N   
856  C CA  . PRO A 124 ? 0.14389 0.06398 0.12817 0.01590  -0.00172 -0.02155 110 PRO A CA  
857  C C   . PRO A 124 ? 0.12594 0.04597 0.11137 0.01261  -0.00134 -0.02113 110 PRO A C   
858  O O   . PRO A 124 ? 0.16451 0.08499 0.15192 0.00913  -0.00087 -0.02397 110 PRO A O   
859  C CB  . PRO A 124 ? 0.16890 0.09696 0.15267 0.01783  -0.00407 -0.02185 110 PRO A CB  
860  C CG  . PRO A 124 ? 0.18894 0.11928 0.17370 0.01581  -0.00433 -0.02575 110 PRO A CG  
861  C CD  . PRO A 124 ? 0.20760 0.13098 0.19266 0.01448  -0.00215 -0.02795 110 PRO A CD  
862  N N   . ALA A 125 ? 0.13752 0.05716 0.12140 0.01378  -0.00151 -0.01754 111 ALA A N   
863  C CA  . ALA A 125 ? 0.17061 0.09037 0.15501 0.01123  -0.00116 -0.01650 111 ALA A CA  
864  C C   . ALA A 125 ? 0.15083 0.07472 0.13293 0.01350  -0.00268 -0.01350 111 ALA A C   
865  O O   . ALA A 125 ? 0.16881 0.09314 0.14876 0.01690  -0.00338 -0.01134 111 ALA A O   
866  C CB  . ALA A 125 ? 0.19701 0.10936 0.18179 0.00958  0.00104  -0.01502 111 ALA A CB  
867  N N   . LEU A 126 ? 0.10962 0.03696 0.09258 0.01149  -0.00336 -0.01365 112 LEU A N   
868  C CA  . LEU A 126 ? 0.13098 0.06208 0.11235 0.01320  -0.00475 -0.01117 112 LEU A CA  
869  C C   . LEU A 126 ? 0.16704 0.09343 0.14661 0.01205  -0.00284 -0.00864 112 LEU A C   
870  O O   . LEU A 126 ? 0.15627 0.07899 0.13735 0.00869  -0.00091 -0.00945 112 LEU A O   
871  C CB  . LEU A 126 ? 0.12291 0.06118 0.10669 0.01193  -0.00683 -0.01295 112 LEU A CB  
872  C CG  . LEU A 126 ? 0.10798 0.05138 0.09364 0.01284  -0.00844 -0.01544 112 LEU A CG  
873  C CD1 . LEU A 126 ? 0.11878 0.06989 0.10715 0.01193  -0.01046 -0.01679 112 LEU A CD1 
874  C CD2 . LEU A 126 ? 0.15896 0.10356 0.14335 0.01663  -0.00919 -0.01397 112 LEU A CD2 
875  N N   . VAL A 127 ? 0.14426 0.07119 0.12076 0.01476  -0.00332 -0.00564 113 VAL A N   
876  C CA  . VAL A 127 ? 0.13742 0.06032 0.11114 0.01440  -0.00141 -0.00280 113 VAL A CA  
877  C C   . VAL A 127 ? 0.15329 0.08130 0.12628 0.01506  -0.00304 -0.00194 113 VAL A C   
878  O O   . VAL A 127 ? 0.15609 0.08925 0.12866 0.01779  -0.00547 -0.00169 113 VAL A O   
879  C CB  . VAL A 127 ? 0.14147 0.05994 0.11130 0.01738  -0.00041 -0.00004 113 VAL A CB  
880  C CG1 . VAL A 127 ? 0.17115 0.08521 0.13777 0.01685  0.00211  0.00292  113 VAL A CG1 
881  C CG2 . VAL A 127 ? 0.16195 0.07578 0.13284 0.01730  0.00073  -0.00105 113 VAL A CG2 
882  N N   . PHE A 128 ? 0.14919 0.07606 0.12251 0.01235  -0.00160 -0.00161 114 PHE A N   
883  C CA  . PHE A 128 ? 0.15387 0.08517 0.12689 0.01262  -0.00297 -0.00107 114 PHE A CA  
884  C C   . PHE A 128 ? 0.13992 0.06737 0.10925 0.01271  -0.00042 0.00201  114 PHE A C   
885  O O   . PHE A 128 ? 0.15624 0.07778 0.12439 0.01138  0.00284  0.00347  114 PHE A O   
886  C CB  . PHE A 128 ? 0.10763 0.04610 0.08670 0.00838  -0.00324 -0.00349 114 PHE A CB  
887  C CG  . PHE A 128 ? 0.10195 0.04510 0.08456 0.00812  -0.00548 -0.00651 114 PHE A CG  
888  C CD1 . PHE A 128 ? 0.10093 0.05088 0.08490 0.01020  -0.00835 -0.00705 114 PHE A CD1 
889  C CD2 . PHE A 128 ? 0.13021 0.07098 0.11490 0.00579  -0.00458 -0.00887 114 PHE A CD2 
890  C CE1 . PHE A 128 ? 0.10973 0.06403 0.09669 0.01016  -0.00997 -0.00949 114 PHE A CE1 
891  C CE2 . PHE A 128 ? 0.16562 0.11078 0.15286 0.00591  -0.00654 -0.01167 114 PHE A CE2 
892  C CZ  . PHE A 128 ? 0.11110 0.06309 0.09929 0.00817  -0.00907 -0.01176 114 PHE A CZ  
893  N N   . GLU A 129 ? 0.18231 0.11478 0.15084 0.01395  -0.00177 0.00288  115 GLU A N   
894  C CA  . GLU A 129 ? 0.20558 0.13563 0.17078 0.01393  0.00071  0.00554  115 GLU A CA  
895  C C   . GLU A 129 ? 0.17017 0.10107 0.13971 0.00891  0.00376  0.00511  115 GLU A C   
896  O O   . GLU A 129 ? 0.17750 0.11360 0.15295 0.00568  0.00289  0.00241  115 GLU A O   
897  C CB  . GLU A 129 ? 0.22351 0.15955 0.18767 0.01612  -0.00171 0.00577  115 GLU A CB  
898  C CG  . GLU A 129 ? 0.15282 0.09771 0.12334 0.01337  -0.00339 0.00339  115 GLU A CG  
899  C CD  . GLU A 129 ? 0.23661 0.18696 0.20666 0.01544  -0.00573 0.00339  115 GLU A CD  
900  O OE1 . GLU A 129 ? 0.25346 0.20098 0.21812 0.01825  -0.00540 0.00526  115 GLU A OE1 
901  O OE2 . GLU A 129 ? 0.18917 0.14649 0.16416 0.01438  -0.00787 0.00146  115 GLU A OE2 
902  N N   . TYR A 130 ? 0.16881 0.09457 0.13538 0.00842  0.00747  0.00785  116 TYR A N   
903  C CA  . TYR A 130 ? 0.20243 0.12865 0.17341 0.00373  0.01085  0.00777  116 TYR A CA  
904  C C   . TYR A 130 ? 0.24439 0.17715 0.21641 0.00324  0.01081  0.00824  116 TYR A C   
905  O O   . TYR A 130 ? 0.23572 0.16731 0.20225 0.00649  0.01103  0.01056  116 TYR A O   
906  C CB  . TYR A 130 ? 0.23517 0.15184 0.20305 0.00324  0.01563  0.01074  116 TYR A CB  
907  C CG  . TYR A 130 ? 0.26377 0.18069 0.23770 -0.00214 0.01934  0.01028  116 TYR A CG  
908  C CD1 . TYR A 130 ? 0.30107 0.22045 0.27563 -0.00343 0.02198  0.01206  116 TYR A CD1 
909  C CD2 . TYR A 130 ? 0.31851 0.23351 0.29789 -0.00587 0.02008  0.00777  116 TYR A CD2 
910  C CE1 . TYR A 130 ? 0.33148 0.25181 0.31255 -0.00843 0.02534  0.01149  116 TYR A CE1 
911  C CE2 . TYR A 130 ? 0.31276 0.22895 0.29869 -0.01091 0.02302  0.00685  116 TYR A CE2 
912  C CZ  . TYR A 130 ? 0.41255 0.33121 0.39951 -0.01227 0.02580  0.00882  116 TYR A CZ  
913  O OH  . TYR A 130 ? 0.34814 0.26960 0.34249 -0.01706 0.02827  0.00769  116 TYR A OH  
914  N N   . ILE A 131 ? 0.17554 0.11519 0.15438 -0.00055 0.01040  0.00593  117 ILE A N   
915  C CA  . ILE A 131 ? 0.18190 0.12791 0.16273 -0.00142 0.01068  0.00618  117 ILE A CA  
916  C C   . ILE A 131 ? 0.17971 0.12512 0.16473 -0.00564 0.01481  0.00668  117 ILE A C   
917  O O   . ILE A 131 ? 0.20336 0.14937 0.19395 -0.00929 0.01528  0.00454  117 ILE A O   
918  C CB  . ILE A 131 ? 0.19117 0.14631 0.17685 -0.00202 0.00685  0.00330  117 ILE A CB  
919  C CG1 . ILE A 131 ? 0.24514 0.20078 0.22793 0.00171  0.00305  0.00265  117 ILE A CG1 
920  C CG2 . ILE A 131 ? 0.18232 0.14355 0.16983 -0.00251 0.00717  0.00368  117 ILE A CG2 
921  C CD1 . ILE A 131 ? 0.25823 0.21145 0.23458 0.00602  0.00240  0.00477  117 ILE A CD1 
922  N N   . ASN A 132 ? 0.16618 0.11058 0.14872 -0.00509 0.01782  0.00933  118 ASN A N   
923  C CA  . ASN A 132 ? 0.17345 0.11755 0.16035 -0.00898 0.02225  0.01016  118 ASN A CA  
924  C C   . ASN A 132 ? 0.23635 0.19040 0.23049 -0.01172 0.02077  0.00767  118 ASN A C   
925  O O   . ASN A 132 ? 0.27480 0.23304 0.26883 -0.01105 0.02148  0.00862  118 ASN A O   
926  C CB  . ASN A 132 ? 0.19124 0.13034 0.17210 -0.00682 0.02633  0.01424  118 ASN A CB  
927  C CG  . ASN A 132 ? 0.22136 0.15920 0.20679 -0.01078 0.03170  0.01562  118 ASN A CG  
928  O OD1 . ASN A 132 ? 0.29590 0.23491 0.28886 -0.01527 0.03254  0.01352  118 ASN A OD1 
929  N ND2 . ASN A 132 ? 0.35055 0.28610 0.33155 -0.00904 0.03543  0.01905  118 ASN A ND2 
930  N N   . ASN A 133 ? 0.22474 0.18247 0.22508 -0.01466 0.01872  0.00437  119 ASN A N   
931  C CA  . ASN A 133 ? 0.23346 0.20090 0.24029 -0.01663 0.01635  0.00165  119 ASN A CA  
932  C C   . ASN A 133 ? 0.23124 0.20222 0.24433 -0.02039 0.01959  0.00165  119 ASN A C   
933  O O   . ASN A 133 ? 0.22779 0.19435 0.24335 -0.02325 0.02313  0.00215  119 ASN A O   
934  C CB  . ASN A 133 ? 0.30680 0.27608 0.31736 -0.01825 0.01339  -0.00182 119 ASN A CB  
935  C CG  . ASN A 133 ? 0.42823 0.40730 0.44542 -0.02026 0.01099  -0.00469 119 ASN A CG  
936  O OD1 . ASN A 133 ? 0.44556 0.43040 0.46235 -0.01821 0.00853  -0.00476 119 ASN A OD1 
937  N ND2 . ASN A 133 ? 0.25527 0.23620 0.27873 -0.02417 0.01157  -0.00720 119 ASN A ND2 
938  N N   . THR A 134 ? 0.18587 0.16496 0.20209 -0.02040 0.01844  0.00102  120 THR A N   
939  C CA  . THR A 134 ? 0.20794 0.19267 0.23163 -0.02397 0.02058  0.00023  120 THR A CA  
940  C C   . THR A 134 ? 0.24352 0.23536 0.27400 -0.02634 0.01717  -0.00372 120 THR A C   
941  O O   . THR A 134 ? 0.25044 0.24706 0.28014 -0.02429 0.01328  -0.00500 120 THR A O   
942  C CB  . THR A 134 ? 0.39470 0.38431 0.41773 -0.02217 0.02132  0.00183  120 THR A CB  
943  O OG1 . THR A 134 ? 0.45480 0.43794 0.47024 -0.01920 0.02397  0.00528  120 THR A OG1 
944  C CG2 . THR A 134 ? 0.42480 0.42027 0.45585 -0.02571 0.02389  0.00121  120 THR A CG2 
945  N N   . ASP A 135 ? 0.22090 0.21332 0.25797 -0.03053 0.01867  -0.00566 121 ASP A N   
946  C CA  . ASP A 135 ? 0.30270 0.30189 0.34524 -0.03217 0.01504  -0.00951 121 ASP A CA  
947  C C   . ASP A 135 ? 0.21351 0.22247 0.25839 -0.03080 0.01245  -0.01009 121 ASP A C   
948  O O   . ASP A 135 ? 0.20360 0.21611 0.25059 -0.03092 0.01430  -0.00862 121 ASP A O   
949  C CB  . ASP A 135 ? 0.42206 0.42124 0.46916 -0.03493 0.01635  -0.01048 121 ASP A CB  
950  C CG  . ASP A 135 ? 0.68298 0.68769 0.73348 -0.03560 0.01233  -0.01408 121 ASP A CG  
951  O OD1 . ASP A 135 ? 0.79500 0.79763 0.84304 -0.03475 0.00982  -0.01587 121 ASP A OD1 
952  O OD2 . ASP A 135 ? 0.81546 0.82632 0.87069 -0.03674 0.01177  -0.01500 121 ASP A OD2 
953  N N   . PHE A 136 ? 0.23863 0.25159 0.28262 -0.02904 0.00823  -0.01195 122 PHE A N   
954  C CA  . PHE A 136 ? 0.21373 0.23447 0.25835 -0.02680 0.00583  -0.01172 122 PHE A CA  
955  C C   . PHE A 136 ? 0.21304 0.23979 0.26195 -0.02758 0.00543  -0.01208 122 PHE A C   
956  O O   . PHE A 136 ? 0.20166 0.23318 0.25139 -0.02611 0.00524  -0.01083 122 PHE A O   
957  C CB  . PHE A 136 ? 0.26015 0.28284 0.30196 -0.02424 0.00182  -0.01289 122 PHE A CB  
958  C CG  . PHE A 136 ? 0.24074 0.26476 0.28319 -0.02457 -0.00063 -0.01513 122 PHE A CG  
959  C CD1 . PHE A 136 ? 0.31114 0.34120 0.35523 -0.02366 -0.00263 -0.01555 122 PHE A CD1 
960  C CD2 . PHE A 136 ? 0.20358 0.22228 0.24465 -0.02560 -0.00079 -0.01678 122 PHE A CD2 
961  C CE1 . PHE A 136 ? 0.27383 0.30510 0.31832 -0.02392 -0.00466 -0.01774 122 PHE A CE1 
962  C CE2 . PHE A 136 ? 0.20570 0.22584 0.24722 -0.02577 -0.00295 -0.01907 122 PHE A CE2 
963  C CZ  . PHE A 136 ? 0.23525 0.26185 0.27851 -0.02499 -0.00484 -0.01962 122 PHE A CZ  
964  N N   . LYS A 137 ? 0.17322 0.19960 0.22504 -0.02981 0.00531  -0.01385 123 LYS A N   
965  C CA  . LYS A 137 ? 0.28184 0.31387 0.33828 -0.03078 0.00494  -0.01441 123 LYS A CA  
966  C C   . LYS A 137 ? 0.33584 0.36884 0.39461 -0.03157 0.00837  -0.01219 123 LYS A C   
967  O O   . LYS A 137 ? 0.37537 0.41417 0.43640 -0.03067 0.00774  -0.01159 123 LYS A O   
968  C CB  . LYS A 137 ? 0.36167 0.39255 0.42128 -0.03343 0.00461  -0.01694 123 LYS A CB  
969  C CG  . LYS A 137 ? 0.39424 0.42736 0.45264 -0.03228 0.00071  -0.01943 123 LYS A CG  
970  C CD  . LYS A 137 ? 0.40598 0.44628 0.46510 -0.03018 -0.00176 -0.01924 123 LYS A CD  
971  C CE  . LYS A 137 ? 0.44459 0.48711 0.50251 -0.02904 -0.00511 -0.02157 123 LYS A CE  
972  N NZ  . LYS A 137 ? 0.44735 0.49600 0.50573 -0.02688 -0.00705 -0.02099 123 LYS A NZ  
973  N N   . GLN A 138 ? 0.27964 0.30654 0.33737 -0.03291 0.01226  -0.01066 124 GLN A N   
974  C CA  . GLN A 138 ? 0.21540 0.24253 0.27416 -0.03316 0.01605  -0.00814 124 GLN A CA  
975  C C   . GLN A 138 ? 0.37074 0.39931 0.42597 -0.03024 0.01615  -0.00631 124 GLN A C   
976  O O   . GLN A 138 ? 0.38590 0.41909 0.44266 -0.02926 0.01689  -0.00514 124 GLN A O   
977  C CB  . GLN A 138 ? 0.38708 0.40603 0.44465 -0.03501 0.02059  -0.00651 124 GLN A CB  
978  C CG  . GLN A 138 ? 0.52282 0.53824 0.58280 -0.03763 0.02040  -0.00847 124 GLN A CG  
979  C CD  . GLN A 138 ? 0.60474 0.62638 0.67126 -0.03961 0.01906  -0.01054 124 GLN A CD  
980  O OE1 . GLN A 138 ? 0.63686 0.65997 0.70527 -0.04050 0.01607  -0.01344 124 GLN A OE1 
981  N NE2 . GLN A 138 ? 0.78788 0.81319 0.85775 -0.04018 0.02134  -0.00910 124 GLN A NE2 
982  N N   . LEU A 139 ? 0.24995 0.27474 0.30069 -0.02879 0.01533  -0.00620 125 LEU A N   
983  C CA  . LEU A 139 ? 0.19439 0.21973 0.24188 -0.02621 0.01583  -0.00463 125 LEU A CA  
984  C C   . LEU A 139 ? 0.21727 0.25042 0.26618 -0.02391 0.01251  -0.00511 125 LEU A C   
985  O O   . LEU A 139 ? 0.23073 0.26637 0.27947 -0.02235 0.01387  -0.00365 125 LEU A O   
986  C CB  . LEU A 139 ? 0.23604 0.25541 0.27694 -0.02402 0.01391  -0.00440 125 LEU A CB  
987  C CG  . LEU A 139 ? 0.28025 0.29799 0.31453 -0.01972 0.01277  -0.00251 125 LEU A CG  
988  C CD1 . LEU A 139 ? 0.27577 0.28810 0.30534 -0.01847 0.01660  0.00040  125 LEU A CD1 
989  C CD2 . LEU A 139 ? 0.23650 0.25007 0.26580 -0.01768 0.00973  -0.00298 125 LEU A CD2 
990  N N   . TYR A 140 ? 0.21838 0.25459 0.26795 -0.02327 0.00839  -0.00682 126 TYR A N   
991  C CA  . TYR A 140 ? 0.23850 0.27966 0.28767 -0.02036 0.00541  -0.00645 126 TYR A CA  
992  C C   . TYR A 140 ? 0.40480 0.45053 0.45741 -0.02021 0.00630  -0.00547 126 TYR A C   
993  O O   . TYR A 140 ? 0.44328 0.49182 0.49548 -0.01763 0.00480  -0.00456 126 TYR A O   
994  C CB  . TYR A 140 ? 0.15978 0.20192 0.20805 -0.01946 0.00166  -0.00785 126 TYR A CB  
995  C CG  . TYR A 140 ? 0.24431 0.28298 0.28857 -0.01833 0.00005  -0.00844 126 TYR A CG  
996  C CD1 . TYR A 140 ? 0.21164 0.24602 0.25421 -0.01912 0.00186  -0.00839 126 TYR A CD1 
997  C CD2 . TYR A 140 ? 0.16891 0.20831 0.21106 -0.01644 -0.00294 -0.00890 126 TYR A CD2 
998  C CE1 . TYR A 140 ? 0.28979 0.32130 0.32919 -0.01803 0.00017  -0.00906 126 TYR A CE1 
999  C CE2 . TYR A 140 ? 0.21713 0.25359 0.25577 -0.01528 -0.00423 -0.00925 126 TYR A CE2 
1000 C CZ  . TYR A 140 ? 0.18349 0.21634 0.22097 -0.01603 -0.00296 -0.00946 126 TYR A CZ  
1001 O OH  . TYR A 140 ? 0.24842 0.27856 0.28277 -0.01470 -0.00449 -0.00991 126 TYR A OH  
1002 N N   . GLN A 141 ? 0.25963 0.30564 0.31572 -0.02284 0.00883  -0.00553 127 GLN A N   
1003 C CA  . GLN A 141 ? 0.32809 0.37883 0.38795 -0.02284 0.00979  -0.00465 127 GLN A CA  
1004 C C   . GLN A 141 ? 0.24732 0.29780 0.30634 -0.02203 0.01336  -0.00260 127 GLN A C   
1005 O O   . GLN A 141 ? 0.30633 0.36097 0.36807 -0.02149 0.01421  -0.00166 127 GLN A O   
1006 C CB  . GLN A 141 ? 0.28535 0.33727 0.35001 -0.02607 0.01061  -0.00588 127 GLN A CB  
1007 C CG  . GLN A 141 ? 0.59317 0.65126 0.66200 -0.02578 0.00839  -0.00653 127 GLN A CG  
1008 C CD  . GLN A 141 ? 0.54195 0.60128 0.60893 -0.02382 0.00419  -0.00773 127 GLN A CD  
1009 O OE1 . GLN A 141 ? 0.74330 0.79926 0.80697 -0.02365 0.00271  -0.00880 127 GLN A OE1 
1010 N NE2 . GLN A 141 ? 0.31997 0.38389 0.38895 -0.02223 0.00252  -0.00742 127 GLN A NE2 
1011 N N   . ILE A 142 ? 0.22103 0.26664 0.27614 -0.02172 0.01562  -0.00187 128 ILE A N   
1012 C CA  . ILE A 142 ? 0.25593 0.30039 0.30927 -0.02074 0.01961  0.00007  128 ILE A CA  
1013 C C   . ILE A 142 ? 0.16213 0.20470 0.21084 -0.01787 0.01950  0.00054  128 ILE A C   
1014 O O   . ILE A 142 ? 0.23019 0.27007 0.27592 -0.01655 0.02315  0.00216  128 ILE A O   
1015 C CB  . ILE A 142 ? 0.33330 0.37224 0.38610 -0.02307 0.02425  0.00129  128 ILE A CB  
1016 C CG1 . ILE A 142 ? 0.28427 0.31563 0.33289 -0.02357 0.02501  0.00139  128 ILE A CG1 
1017 C CG2 . ILE A 142 ? 0.27152 0.31282 0.32984 -0.02604 0.02425  0.00043  128 ILE A CG2 
1018 C CD1 . ILE A 142 ? 0.39236 0.41667 0.43448 -0.02181 0.02938  0.00432  128 ILE A CD1 
1019 N N   . LEU A 143 ? 0.22336 0.26693 0.27106 -0.01653 0.01545  -0.00073 129 LEU A N   
1020 C CA  . LEU A 143 ? 0.12502 0.16674 0.16796 -0.01338 0.01432  -0.00036 129 LEU A CA  
1021 C C   . LEU A 143 ? 0.17810 0.22484 0.22262 -0.01108 0.01444  0.00005  129 LEU A C   
1022 O O   . LEU A 143 ? 0.18732 0.23721 0.23495 -0.01068 0.01273  0.00034  129 LEU A O   
1023 C CB  . LEU A 143 ? 0.14513 0.18702 0.18720 -0.01269 0.01003  -0.00176 129 LEU A CB  
1024 C CG  . LEU A 143 ? 0.16625 0.20270 0.20606 -0.01434 0.00950  -0.00233 129 LEU A CG  
1025 C CD1 . LEU A 143 ? 0.17697 0.21604 0.21811 -0.01419 0.00561  -0.00409 129 LEU A CD1 
1026 C CD2 . LEU A 143 ? 0.15800 0.18603 0.18990 -0.01224 0.01035  -0.00067 129 LEU A CD2 
1027 N N   . THR A 144 ? 0.13943 0.18222 0.17808 -0.00803 0.01509  0.00123  130 THR A N   
1028 C CA  . THR A 144 ? 0.10436 0.15087 0.14378 -0.00539 0.01481  0.00133  130 THR A CA  
1029 C C   . THR A 144 ? 0.10915 0.15701 0.14845 -0.00350 0.01065  0.00037  130 THR A C   
1030 O O   . THR A 144 ? 0.08982 0.13524 0.12751 -0.00390 0.00822  -0.00019 130 THR A O   
1031 C CB  . THR A 144 ? 0.14416 0.18542 0.17685 -0.00268 0.01697  0.00259  130 THR A CB  
1032 O OG1 . THR A 144 ? 0.12851 0.16364 0.15471 -0.00083 0.01458  0.00246  130 THR A OG1 
1033 C CG2 . THR A 144 ? 0.15366 0.19222 0.18514 -0.00423 0.02154  0.00410  130 THR A CG2 
1034 N N   . ASP A 145 ? 0.06801 0.11662 0.10781 -0.00124 0.00978  0.00029  131 ASP A N   
1035 C CA  . ASP A 145 ? 0.07506 0.12134 0.11336 0.00065  0.00629  -0.00018 131 ASP A CA  
1036 C C   . ASP A 145 ? 0.10007 0.14463 0.13459 0.00225  0.00514  -0.00030 131 ASP A C   
1037 O O   . ASP A 145 ? 0.10424 0.14611 0.13767 0.00224  0.00241  -0.00067 131 ASP A O   
1038 C CB  . ASP A 145 ? 0.08360 0.13007 0.12265 0.00252  0.00642  -0.00017 131 ASP A CB  
1039 C CG  . ASP A 145 ? 0.15209 0.19522 0.18954 0.00414  0.00369  -0.00032 131 ASP A CG  
1040 O OD1 . ASP A 145 ? 0.10744 0.14817 0.14437 0.00346  0.00162  -0.00026 131 ASP A OD1 
1041 O OD2 . ASP A 145 ? 0.18397 0.22656 0.22076 0.00605  0.00395  -0.00042 131 ASP A OD2 
1042 N N   . PHE A 146 ? 0.07814 0.11886 0.10783 0.00374  0.00689  0.00010  132 PHE A N   
1043 C CA  . PHE A 146 ? 0.08307 0.11761 0.10680 0.00542  0.00517  -0.00020 132 PHE A CA  
1044 C C   . PHE A 146 ? 0.09502 0.12630 0.11694 0.00362  0.00436  -0.00008 132 PHE A C   
1045 O O   . PHE A 146 ? 0.09340 0.12240 0.11374 0.00444  0.00167  -0.00067 132 PHE A O   
1046 C CB  . PHE A 146 ? 0.10888 0.13909 0.12656 0.00768  0.00705  0.00010  132 PHE A CB  
1047 C CG  . PHE A 146 ? 0.09837 0.12293 0.11011 0.00980  0.00480  -0.00056 132 PHE A CG  
1048 C CD1 . PHE A 146 ? 0.16921 0.19360 0.18091 0.01212  0.00222  -0.00197 132 PHE A CD1 
1049 C CD2 . PHE A 146 ? 0.14438 0.16393 0.15117 0.00945  0.00514  0.00013  132 PHE A CD2 
1050 C CE1 . PHE A 146 ? 0.22510 0.24497 0.23220 0.01399  -0.00018 -0.00295 132 PHE A CE1 
1051 C CE2 . PHE A 146 ? 0.15277 0.16774 0.15442 0.01163  0.00276  -0.00059 132 PHE A CE2 
1052 C CZ  . PHE A 146 ? 0.22035 0.23576 0.22232 0.01387  -0.00004 -0.00227 132 PHE A CZ  
1053 N N   . ASP A 147 ? 0.08319 0.11405 0.10563 0.00118  0.00682  0.00063  133 ASP A N   
1054 C CA  . ASP A 147 ? 0.06656 0.09397 0.08758 -0.00061 0.00630  0.00064  133 ASP A CA  
1055 C C   . ASP A 147 ? 0.07677 0.10707 0.10128 -0.00136 0.00309  -0.00051 133 ASP A C   
1056 O O   . ASP A 147 ? 0.10352 0.13023 0.12540 -0.00109 0.00132  -0.00082 133 ASP A O   
1057 C CB  . ASP A 147 ? 0.07903 0.10715 0.10278 -0.00379 0.00937  0.00118  133 ASP A CB  
1058 C CG  . ASP A 147 ? 0.21510 0.23884 0.23464 -0.00343 0.01325  0.00284  133 ASP A CG  
1059 O OD1 . ASP A 147 ? 0.20942 0.22749 0.22197 -0.00088 0.01329  0.00363  133 ASP A OD1 
1060 O OD2 . ASP A 147 ? 0.20561 0.23181 0.22909 -0.00575 0.01636  0.00338  133 ASP A OD2 
1061 N N   . ILE A 148 ? 0.06191 0.09885 0.09227 -0.00216 0.00247  -0.00106 134 ILE A N   
1062 C CA  . ILE A 148 ? 0.04976 0.08914 0.08267 -0.00253 -0.00030 -0.00186 134 ILE A CA  
1063 C C   . ILE A 148 ? 0.06435 0.10028 0.09425 -0.00004 -0.00261 -0.00168 134 ILE A C   
1064 O O   . ILE A 148 ? 0.08972 0.12286 0.11793 -0.00006 -0.00427 -0.00181 134 ILE A O   
1065 C CB  . ILE A 148 ? 0.06693 0.10657 0.10194 -0.00275 -0.00050 -0.00133 134 ILE A CB  
1066 C CG1 . ILE A 148 ? 0.03386 0.07630 0.07213 -0.00524 0.00134  -0.00155 134 ILE A CG1 
1067 C CG2 . ILE A 148 ? 0.10307 0.13986 0.13679 -0.00227 -0.00280 -0.00106 134 ILE A CG2 
1068 C CD1 . ILE A 148 ? 0.10526 0.14919 0.14608 -0.00499 0.00095  -0.00113 134 ILE A CD1 
1069 N N   . ARG A 149 ? 0.06721 0.10268 0.09640 0.00197  -0.00250 -0.00135 135 ARG A N   
1070 C CA  . ARG A 149 ? 0.04995 0.08132 0.07658 0.00372  -0.00429 -0.00120 135 ARG A CA  
1071 C C   . ARG A 149 ? 0.08820 0.11812 0.11228 0.00484  -0.00556 -0.00214 135 ARG A C   
1072 O O   . ARG A 149 ? 0.07722 0.10329 0.09936 0.00479  -0.00694 -0.00181 135 ARG A O   
1073 C CB  . ARG A 149 ? 0.05541 0.08677 0.08195 0.00552  -0.00380 -0.00121 135 ARG A CB  
1074 C CG  . ARG A 149 ? 0.09075 0.12278 0.11980 0.00489  -0.00296 -0.00042 135 ARG A CG  
1075 C CD  . ARG A 149 ? 0.07541 0.10819 0.10467 0.00669  -0.00213 -0.00071 135 ARG A CD  
1076 N NE  . ARG A 149 ? 0.09103 0.12543 0.12304 0.00630  -0.00103 -0.00031 135 ARG A NE  
1077 C CZ  . ARG A 149 ? 0.11820 0.15112 0.15135 0.00699  -0.00128 0.00009  135 ARG A CZ  
1078 N NH1 . ARG A 149 ? 0.10166 0.13134 0.13354 0.00748  -0.00231 0.00072  135 ARG A NH1 
1079 N NH2 . ARG A 149 ? 0.12976 0.16472 0.16531 0.00706  -0.00023 -0.00000 135 ARG A NH2 
1080 N N   . PHE A 150 ? 0.08512 0.11132 0.10499 0.00478  -0.00377 -0.00180 136 PHE A N   
1081 C CA  . PHE A 150 ? 0.08223 0.10251 0.09659 0.00583  -0.00445 -0.00184 136 PHE A CA  
1082 C C   . PHE A 150 ? 0.09558 0.11458 0.11013 0.00435  -0.00539 -0.00193 136 PHE A C   
1083 O O   . PHE A 150 ? 0.09553 0.11207 0.10834 0.00558  -0.00745 -0.00238 136 PHE A O   
1084 C CB  . PHE A 150 ? 0.11115 0.12773 0.12069 0.00615  -0.00172 -0.00093 136 PHE A CB  
1085 C CG  . PHE A 150 ? 0.12594 0.13624 0.12913 0.00756  -0.00215 -0.00061 136 PHE A CG  
1086 C CD1 . PHE A 150 ? 0.11579 0.12300 0.11757 0.00596  -0.00121 0.00012  136 PHE A CD1 
1087 C CD2 . PHE A 150 ? 0.16339 0.17087 0.16208 0.01066  -0.00360 -0.00118 136 PHE A CD2 
1088 C CE1 . PHE A 150 ? 0.17459 0.17591 0.17042 0.00763  -0.00158 0.00063  136 PHE A CE1 
1089 C CE2 . PHE A 150 ? 0.18048 0.18258 0.17315 0.01239  -0.00425 -0.00088 136 PHE A CE2 
1090 C CZ  . PHE A 150 ? 0.20997 0.20893 0.20111 0.01097  -0.00315 0.00023  136 PHE A CZ  
1091 N N   . TYR A 151 ? 0.09512 0.11572 0.11190 0.00176  -0.00388 -0.00173 137 TYR A N   
1092 C CA  . TYR A 151 ? 0.10206 0.12081 0.11858 0.00042  -0.00462 -0.00212 137 TYR A CA  
1093 C C   . TYR A 151 ? 0.11258 0.13491 0.13241 0.00070  -0.00715 -0.00295 137 TYR A C   
1094 O O   . TYR A 151 ? 0.08248 0.10240 0.10083 0.00115  -0.00857 -0.00333 137 TYR A O   
1095 C CB  . TYR A 151 ? 0.06867 0.08802 0.08712 -0.00258 -0.00237 -0.00211 137 TYR A CB  
1096 C CG  . TYR A 151 ? 0.09425 0.10848 0.10882 -0.00293 0.00057  -0.00090 137 TYR A CG  
1097 C CD1 . TYR A 151 ? 0.15167 0.15921 0.16026 -0.00125 0.00056  -0.00014 137 TYR A CD1 
1098 C CD2 . TYR A 151 ? 0.10141 0.11761 0.11836 -0.00473 0.00351  -0.00034 137 TYR A CD2 
1099 C CE1 . TYR A 151 ? 0.11562 0.11816 0.12007 -0.00119 0.00355  0.00139  137 TYR A CE1 
1100 C CE2 . TYR A 151 ? 0.12555 0.13690 0.13894 -0.00497 0.00675  0.00116  137 TYR A CE2 
1101 C CZ  . TYR A 151 ? 0.14946 0.15377 0.15629 -0.00310 0.00681  0.00215  137 TYR A CZ  
1102 O OH  . TYR A 151 ? 0.19107 0.19022 0.19379 -0.00298 0.01029  0.00404  137 TYR A OH  
1103 N N   . MET A 152 ? 0.06561 0.09310 0.08937 0.00063  -0.00743 -0.00288 138 MET A N   
1104 C CA  . MET A 152 ? 0.07283 0.09777 0.09476 0.00068  -0.00780 -0.00132 138 MET A CA  
1105 C C   . MET A 152 ? 0.06954 0.09135 0.08868 0.00220  -0.00830 -0.00090 138 MET A C   
1106 O O   . MET A 152 ? 0.06294 0.08321 0.08057 0.00212  -0.00836 -0.00044 138 MET A O   
1107 C CB  . MET A 152 ? 0.10743 0.13307 0.13100 0.00042  -0.00709 0.00001  138 MET A CB  
1108 C CG  . MET A 152 ? 0.13661 0.16452 0.16249 -0.00091 -0.00675 -0.00048 138 MET A CG  
1109 S SD  . MET A 152 ? 0.22230 0.24920 0.24695 -0.00149 -0.00765 -0.00054 138 MET A SD  
1110 C CE  . MET A 152 ? 0.14065 0.16929 0.16606 -0.00337 -0.00763 -0.00260 138 MET A CE  
1111 N N   . TYR A 153 ? 0.05524 0.07628 0.07387 0.00360  -0.00850 -0.00131 139 TYR A N   
1112 C CA  . TYR A 153 ? 0.10893 0.12678 0.12524 0.00478  -0.00899 -0.00145 139 TYR A CA  
1113 C C   . TYR A 153 ? 0.10110 0.11637 0.11540 0.00544  -0.01017 -0.00234 139 TYR A C   
1114 O O   . TYR A 153 ? 0.07691 0.09043 0.09019 0.00539  -0.01004 -0.00216 139 TYR A O   
1115 C CB  . TYR A 153 ? 0.08848 0.10575 0.10431 0.00636  -0.00935 -0.00219 139 TYR A CB  
1116 C CG  . TYR A 153 ? 0.06673 0.08144 0.08127 0.00698  -0.00963 -0.00255 139 TYR A CG  
1117 C CD1 . TYR A 153 ? 0.09074 0.10582 0.10668 0.00633  -0.00896 -0.00213 139 TYR A CD1 
1118 C CD2 . TYR A 153 ? 0.12761 0.13964 0.13961 0.00869  -0.01098 -0.00398 139 TYR A CD2 
1119 C CE1 . TYR A 153 ? 0.11608 0.12921 0.13202 0.00701  -0.00968 -0.00340 139 TYR A CE1 
1120 C CE2 . TYR A 153 ? 0.14699 0.15725 0.15863 0.00903  -0.01142 -0.00484 139 TYR A CE2 
1121 C CZ  . TYR A 153 ? 0.16404 0.17496 0.17806 0.00810  -0.01082 -0.00469 139 TYR A CZ  
1122 O OH  . TYR A 153 ? 0.19520 0.20442 0.20976 0.00864  -0.01181 -0.00630 139 TYR A OH  
1123 N N   . GLU A 154 ? 0.09623 0.11140 0.11014 0.00620  -0.01135 -0.00322 140 GLU A N   
1124 C CA  . GLU A 154 ? 0.09672 0.10812 0.10772 0.00716  -0.01266 -0.00361 140 GLU A CA  
1125 C C   . GLU A 154 ? 0.08628 0.09827 0.09870 0.00564  -0.01248 -0.00368 140 GLU A C   
1126 O O   . GLU A 154 ? 0.09824 0.10750 0.10881 0.00634  -0.01291 -0.00380 140 GLU A O   
1127 C CB  . GLU A 154 ? 0.11264 0.11973 0.11917 0.00647  -0.01040 -0.00280 140 GLU A CB  
1128 C CG  . GLU A 154 ? 0.11510 0.12005 0.11785 0.00819  -0.00955 -0.00232 140 GLU A CG  
1129 C CD  . GLU A 154 ? 0.16333 0.16521 0.16238 0.01126  -0.01180 -0.00288 140 GLU A CD  
1130 O OE1 . GLU A 154 ? 0.32384 0.32177 0.31954 0.01212  -0.01235 -0.00262 140 GLU A OE1 
1131 O OE2 . GLU A 154 ? 0.20431 0.20774 0.20399 0.01292  -0.01314 -0.00373 140 GLU A OE2 
1132 N N   . LEU A 155 ? 0.09792 0.11339 0.11317 0.00365  -0.01153 -0.00364 141 LEU A N   
1133 C CA  . LEU A 155 ? 0.08379 0.09954 0.09917 0.00263  -0.01117 -0.00366 141 LEU A CA  
1134 C C   . LEU A 155 ? 0.05600 0.07118 0.07018 0.00305  -0.01009 -0.00239 141 LEU A C   
1135 O O   . LEU A 155 ? 0.07785 0.09186 0.09129 0.00334  -0.01023 -0.00259 141 LEU A O   
1136 C CB  . LEU A 155 ? 0.05583 0.07509 0.07354 0.00060  -0.01038 -0.00378 141 LEU A CB  
1137 C CG  . LEU A 155 ? 0.07869 0.09839 0.09609 -0.00013 -0.01027 -0.00388 141 LEU A CG  
1138 C CD1 . LEU A 155 ? 0.07505 0.09230 0.09194 0.00003  -0.01156 -0.00569 141 LEU A CD1 
1139 C CD2 . LEU A 155 ? 0.07944 0.10204 0.09881 -0.00187 -0.00981 -0.00404 141 LEU A CD2 
1140 N N   . LEU A 156 ? 0.03191 0.04795 0.04646 0.00310  -0.00919 -0.00138 142 LEU A N   
1141 C CA  . LEU A 156 ? 0.09582 0.11126 0.11072 0.00377  -0.00899 -0.00149 142 LEU A CA  
1142 C C   . LEU A 156 ? 0.10870 0.12131 0.12254 0.00476  -0.00964 -0.00231 142 LEU A C   
1143 O O   . LEU A 156 ? 0.09335 0.10554 0.10764 0.00504  -0.00966 -0.00252 142 LEU A O   
1144 C CB  . LEU A 156 ? 0.08324 0.09980 0.09930 0.00390  -0.00848 -0.00100 142 LEU A CB  
1145 C CG  . LEU A 156 ? 0.09459 0.11395 0.11210 0.00320  -0.00792 0.00002  142 LEU A CG  
1146 C CD1 . LEU A 156 ? 0.09135 0.11167 0.10997 0.00347  -0.00749 0.00056  142 LEU A CD1 
1147 C CD2 . LEU A 156 ? 0.09127 0.11147 0.10940 0.00330  -0.00778 0.00056  142 LEU A CD2 
1148 N N   . LYS A 157 ? 0.09933 0.11021 0.11180 0.00539  -0.01026 -0.00271 143 LYS A N   
1149 C CA  . LYS A 157 ? 0.08815 0.09640 0.09943 0.00643  -0.01113 -0.00360 143 LYS A CA  
1150 C C   . LYS A 157 ? 0.09095 0.09843 0.10172 0.00650  -0.01137 -0.00373 143 LYS A C   
1151 O O   . LYS A 157 ? 0.10450 0.11108 0.11562 0.00698  -0.01170 -0.00435 143 LYS A O   
1152 C CB  . LYS A 157 ? 0.10831 0.11483 0.11737 0.00745  -0.01191 -0.00382 143 LYS A CB  
1153 C CG  . LYS A 157 ? 0.12114 0.12812 0.13042 0.00780  -0.01188 -0.00404 143 LYS A CG  
1154 C CD  . LYS A 157 ? 0.20229 0.20682 0.20837 0.00979  -0.01336 -0.00497 143 LYS A CD  
1155 C CE  . LYS A 157 ? 0.22138 0.22646 0.22729 0.01053  -0.01348 -0.00548 143 LYS A CE  
1156 N NZ  . LYS A 157 ? 0.18292 0.18563 0.18426 0.01304  -0.01465 -0.00596 143 LYS A NZ  
1157 N N   . ALA A 158 ? 0.05543 0.06335 0.06578 0.00608  -0.01148 -0.00345 144 ALA A N   
1158 C CA  . ALA A 158 ? 0.04395 0.05064 0.05384 0.00648  -0.01215 -0.00407 144 ALA A CA  
1159 C C   . ALA A 158 ? 0.06605 0.07479 0.07731 0.00583  -0.01115 -0.00367 144 ALA A C   
1160 O O   . ALA A 158 ? 0.06577 0.07360 0.07687 0.00649  -0.01144 -0.00411 144 ALA A O   
1161 C CB  . ALA A 158 ? 0.07318 0.07918 0.08291 0.00644  -0.01352 -0.00490 144 ALA A CB  
1162 N N   . LEU A 159 ? 0.05881 0.07009 0.07141 0.00498  -0.01040 -0.00314 145 LEU A N   
1163 C CA  . LEU A 159 ? 0.03265 0.04570 0.04632 0.00493  -0.00992 -0.00286 145 LEU A CA  
1164 C C   . LEU A 159 ? 0.06177 0.07449 0.07635 0.00556  -0.00974 -0.00270 145 LEU A C   
1165 O O   . LEU A 159 ? 0.07721 0.09046 0.09234 0.00598  -0.00966 -0.00260 145 LEU A O   
1166 C CB  . LEU A 159 ? 0.07077 0.08658 0.08542 0.00406  -0.00937 -0.00212 145 LEU A CB  
1167 C CG  . LEU A 159 ? 0.07888 0.09577 0.09337 0.00304  -0.00969 -0.00251 145 LEU A CG  
1168 C CD1 . LEU A 159 ? 0.15056 0.16999 0.16630 0.00235  -0.00936 -0.00191 145 LEU A CD1 
1169 C CD2 . LEU A 159 ? 0.08966 0.10631 0.10360 0.00317  -0.01020 -0.00337 145 LEU A CD2 
1170 N N   . ASP A 160 ? 0.08651 0.09864 0.10156 0.00560  -0.00973 -0.00269 146 ASP A N   
1171 C CA  . ASP A 160 ? 0.08879 0.10056 0.10524 0.00601  -0.00983 -0.00281 146 ASP A CA  
1172 C C   . ASP A 160 ? 0.10918 0.11918 0.12519 0.00668  -0.01063 -0.00373 146 ASP A C   
1173 O O   . ASP A 160 ? 0.09797 0.10869 0.11547 0.00695  -0.01056 -0.00357 146 ASP A O   
1174 C CB  . ASP A 160 ? 0.07923 0.09025 0.09635 0.00598  -0.01003 -0.00314 146 ASP A CB  
1175 C CG  . ASP A 160 ? 0.15188 0.16256 0.17119 0.00622  -0.01035 -0.00350 146 ASP A CG  
1176 O OD1 . ASP A 160 ? 0.14835 0.16085 0.16948 0.00612  -0.00964 -0.00247 146 ASP A OD1 
1177 O OD2 . ASP A 160 ? 0.24038 0.24920 0.25972 0.00662  -0.01139 -0.00479 146 ASP A OD2 
1178 N N   . TYR A 161 ? 0.07140 0.07940 0.08546 0.00707  -0.01137 -0.00448 147 TYR A N   
1179 C CA  . TYR A 161 ? 0.07314 0.07954 0.08650 0.00793  -0.01224 -0.00528 147 TYR A CA  
1180 C C   . TYR A 161 ? 0.08163 0.08901 0.09535 0.00809  -0.01191 -0.00499 147 TYR A C   
1181 O O   . TYR A 161 ? 0.07139 0.07922 0.08637 0.00857  -0.01207 -0.00515 147 TYR A O   
1182 C CB  . TYR A 161 ? 0.07919 0.08330 0.08993 0.00861  -0.01306 -0.00573 147 TYR A CB  
1183 C CG  . TYR A 161 ? 0.07156 0.07406 0.08146 0.00978  -0.01413 -0.00657 147 TYR A CG  
1184 C CD1 . TYR A 161 ? 0.18676 0.18882 0.19731 0.01035  -0.01503 -0.00753 147 TYR A CD1 
1185 C CD2 . TYR A 161 ? 0.11545 0.11700 0.12411 0.01041  -0.01438 -0.00651 147 TYR A CD2 
1186 C CE1 . TYR A 161 ? 0.20375 0.20483 0.21376 0.01152  -0.01616 -0.00838 147 TYR A CE1 
1187 C CE2 . TYR A 161 ? 0.19938 0.19971 0.20731 0.01166  -0.01538 -0.00720 147 TYR A CE2 
1188 C CZ  . TYR A 161 ? 0.22518 0.22548 0.23382 0.01220  -0.01629 -0.00812 147 TYR A CZ  
1189 O OH  . TYR A 161 ? 0.26212 0.26167 0.27031 0.01355  -0.01746 -0.00892 147 TYR A OH  
1190 N N   . CYS A 162 ? 0.05025 0.05825 0.06312 0.00775  -0.01152 -0.00464 148 CYS A N   
1191 C CA  . CYS A 162 ? 0.08838 0.09716 0.10135 0.00816  -0.01142 -0.00468 148 CYS A CA  
1192 C C   . CYS A 162 ? 0.07185 0.08334 0.08681 0.00811  -0.01060 -0.00384 148 CYS A C   
1193 O O   . CYS A 162 ? 0.07246 0.08455 0.08816 0.00885  -0.01057 -0.00380 148 CYS A O   
1194 C CB  . CYS A 162 ? 0.08829 0.09702 0.10007 0.00785  -0.01156 -0.00490 148 CYS A CB  
1195 S SG  . CYS A 162 ? 0.11628 0.12802 0.12887 0.00660  -0.01088 -0.00435 148 CYS A SG  
1196 N N   . HIS A 163 ? 0.08126 0.09454 0.09725 0.00743  -0.00991 -0.00290 149 HIS A N   
1197 C CA  . HIS A 163 ? 0.06687 0.08279 0.08488 0.00763  -0.00909 -0.00157 149 HIS A CA  
1198 C C   . HIS A 163 ? 0.05780 0.07356 0.07767 0.00815  -0.00915 -0.00152 149 HIS A C   
1199 O O   . HIS A 163 ? 0.05985 0.07753 0.08138 0.00880  -0.00856 -0.00059 149 HIS A O   
1200 C CB  . HIS A 163 ? 0.07166 0.08935 0.09045 0.00702  -0.00842 -0.00038 149 HIS A CB  
1201 C CG  . HIS A 163 ? 0.06372 0.08210 0.08141 0.00645  -0.00850 -0.00045 149 HIS A CG  
1202 N ND1 . HIS A 163 ? 0.04483 0.06435 0.06302 0.00585  -0.00819 0.00034  149 HIS A ND1 
1203 C CD2 . HIS A 163 ? 0.05783 0.07607 0.07416 0.00642  -0.00896 -0.00144 149 HIS A CD2 
1204 C CE1 . HIS A 163 ? 0.06235 0.08240 0.07967 0.00540  -0.00854 -0.00026 149 HIS A CE1 
1205 N NE2 . HIS A 163 ? 0.04888 0.06831 0.06502 0.00571  -0.00899 -0.00139 149 HIS A NE2 
1206 N N   . SER A 164 ? 0.05400 0.06766 0.07390 0.00793  -0.00990 -0.00252 150 SER A N   
1207 C CA  . SER A 164 ? 0.05606 0.06948 0.07818 0.00829  -0.01035 -0.00294 150 SER A CA  
1208 C C   . SER A 164 ? 0.10723 0.12027 0.12924 0.00915  -0.01088 -0.00351 150 SER A C   
1209 O O   . SER A 164 ? 0.07935 0.09335 0.10390 0.00959  -0.01097 -0.00347 150 SER A O   
1210 C CB  . SER A 164 ? 0.09957 0.11078 0.12169 0.00799  -0.01137 -0.00420 150 SER A CB  
1211 O OG  . SER A 164 ? 0.08956 0.09849 0.10926 0.00849  -0.01246 -0.00546 150 SER A OG  
1212 N N   . LYS A 165 ? 0.08037 0.08968 0.08424 0.00023  -0.00309 0.00674  151 LYS A N   
1213 C CA  . LYS A 165 ? 0.06586 0.07565 0.07015 0.00092  -0.00233 0.00633  151 LYS A CA  
1214 C C   . LYS A 165 ? 0.05604 0.06752 0.06069 0.00011  -0.00107 0.00620  151 LYS A C   
1215 O O   . LYS A 165 ? 0.09354 0.10538 0.09833 0.00077  -0.00031 0.00562  151 LYS A O   
1216 C CB  . LYS A 165 ? 0.07784 0.08525 0.08021 0.00201  -0.00201 0.00595  151 LYS A CB  
1217 C CG  . LYS A 165 ? 0.09831 0.10444 0.10025 0.00320  -0.00320 0.00602  151 LYS A CG  
1218 C CD  . LYS A 165 ? 0.23180 0.23919 0.23579 0.00395  -0.00398 0.00582  151 LYS A CD  
1219 C CE  . LYS A 165 ? 0.35938 0.36529 0.36262 0.00538  -0.00523 0.00574  151 LYS A CE  
1220 N NZ  . LYS A 165 ? 0.42938 0.43656 0.43490 0.00614  -0.00608 0.00546  151 LYS A NZ  
1221 N N   . GLY A 166 ? 0.04091 0.05345 0.04565 -0.00117 -0.00094 0.00669  152 GLY A N   
1222 C CA  . GLY A 166 ? 0.04268 0.05705 0.04745 -0.00188 0.00018  0.00663  152 GLY A CA  
1223 C C   . GLY A 166 ? 0.07319 0.08634 0.07601 -0.00180 0.00114  0.00587  152 GLY A C   
1224 O O   . GLY A 166 ? 0.07790 0.09239 0.08057 -0.00181 0.00209  0.00537  152 GLY A O   
1225 N N   . ILE A 167 ? 0.07016 0.08092 0.07157 -0.00172 0.00091  0.00574  153 ILE A N   
1226 C CA  . ILE A 167 ? 0.04965 0.05890 0.04960 -0.00164 0.00163  0.00504  153 ILE A CA  
1227 C C   . ILE A 167 ? 0.10017 0.10859 0.09919 -0.00261 0.00145  0.00531  153 ILE A C   
1228 O O   . ILE A 167 ? 0.09549 0.10327 0.09454 -0.00275 0.00073  0.00585  153 ILE A O   
1229 C CB  . ILE A 167 ? 0.06061 0.06768 0.06010 -0.00049 0.00161  0.00470  153 ILE A CB  
1230 C CG1 . ILE A 167 ? 0.09768 0.10562 0.09816 0.00054  0.00182  0.00417  153 ILE A CG1 
1231 C CG2 . ILE A 167 ? 0.08853 0.09360 0.08679 -0.00063 0.00211  0.00426  153 ILE A CG2 
1232 C CD1 . ILE A 167 ? 0.14191 0.14815 0.14241 0.00179  0.00128  0.00423  153 ILE A CD1 
1233 N N   . MET A 168 ? 0.09362 0.10218 0.09187 -0.00317 0.00199  0.00482  154 MET A N   
1234 C CA  . MET A 168 ? 0.08815 0.09585 0.08565 -0.00400 0.00183  0.00486  154 MET A CA  
1235 C C   . MET A 168 ? 0.07478 0.08034 0.07167 -0.00364 0.00222  0.00424  154 MET A C   
1236 O O   . MET A 168 ? 0.07538 0.08058 0.07211 -0.00312 0.00268  0.00345  154 MET A O   
1237 C CB  . MET A 168 ? 0.09889 0.10801 0.09588 -0.00480 0.00204  0.00462  154 MET A CB  
1238 C CG  . MET A 168 ? 0.14850 0.16004 0.14603 -0.00527 0.00194  0.00532  154 MET A CG  
1239 S SD  . MET A 168 ? 0.15843 0.17148 0.15466 -0.00601 0.00234  0.00499  154 MET A SD  
1240 C CE  . MET A 168 ? 0.13911 0.15352 0.13513 -0.00497 0.00346  0.00392  154 MET A CE  
1241 N N   . HIS A 169 ? 0.06928 0.07352 0.06599 -0.00392 0.00201  0.00459  155 HIS A N   
1242 C CA  . HIS A 169 ? 0.05353 0.05579 0.04998 -0.00378 0.00241  0.00430  155 HIS A CA  
1243 C C   . HIS A 169 ? 0.08801 0.09005 0.08431 -0.00445 0.00255  0.00348  155 HIS A C   
1244 O O   . HIS A 169 ? 0.06739 0.06827 0.06368 -0.00412 0.00281  0.00275  155 HIS A O   
1245 C CB  . HIS A 169 ? 0.05779 0.05913 0.05419 -0.00386 0.00232  0.00505  155 HIS A CB  
1246 C CG  . HIS A 169 ? 0.06876 0.06819 0.06511 -0.00381 0.00281  0.00514  155 HIS A CG  
1247 N ND1 . HIS A 169 ? 0.09855 0.09738 0.09533 -0.00465 0.00297  0.00481  155 HIS A ND1 
1248 C CD2 . HIS A 169 ? 0.07852 0.07648 0.07458 -0.00309 0.00309  0.00567  155 HIS A CD2 
1249 C CE1 . HIS A 169 ? 0.09034 0.08743 0.08731 -0.00455 0.00338  0.00518  155 HIS A CE1 
1250 N NE2 . HIS A 169 ? 0.10078 0.09727 0.09718 -0.00360 0.00349  0.00579  155 HIS A NE2 
1251 N N   . ARG A 170 ? 0.05688 0.05994 0.05311 -0.00533 0.00221  0.00350  156 ARG A N   
1252 C CA  . ARG A 170 ? 0.07510 0.07826 0.07103 -0.00595 0.00210  0.00266  156 ARG A CA  
1253 C C   . ARG A 170 ? 0.08898 0.09038 0.08544 -0.00636 0.00209  0.00233  156 ARG A C   
1254 O O   . ARG A 170 ? 0.11821 0.11945 0.11459 -0.00681 0.00181  0.00146  156 ARG A O   
1255 C CB  . ARG A 170 ? 0.07385 0.07780 0.06914 -0.00548 0.00235  0.00169  156 ARG A CB  
1256 C CG  . ARG A 170 ? 0.07584 0.08199 0.07093 -0.00526 0.00249  0.00217  156 ARG A CG  
1257 C CD  . ARG A 170 ? 0.03923 0.04687 0.03350 -0.00497 0.00285  0.00124  156 ARG A CD  
1258 N NE  . ARG A 170 ? 0.06630 0.07283 0.06057 -0.00401 0.00320  0.00001  156 ARG A NE  
1259 C CZ  . ARG A 170 ? 0.08715 0.09476 0.08070 -0.00342 0.00353  -0.00119 156 ARG A CZ  
1260 N NH1 . ARG A 170 ? 0.13610 0.14599 0.12860 -0.00376 0.00369  -0.00121 156 ARG A NH1 
1261 N NH2 . ARG A 170 ? 0.12702 0.13339 0.12082 -0.00239 0.00367  -0.00239 156 ARG A NH2 
1262 N N   . ASP A 171 ? 0.06455 0.06472 0.06161 -0.00623 0.00236  0.00302  157 ASP A N   
1263 C CA  . ASP A 171 ? 0.07950 0.07825 0.07744 -0.00680 0.00243  0.00298  157 ASP A CA  
1264 C C   . ASP A 171 ? 0.12183 0.12056 0.12029 -0.00695 0.00272  0.00410  157 ASP A C   
1265 O O   . ASP A 171 ? 0.13294 0.13039 0.13203 -0.00703 0.00318  0.00464  157 ASP A O   
1266 C CB  . ASP A 171 ? 0.06487 0.06170 0.06308 -0.00640 0.00264  0.00250  157 ASP A CB  
1267 C CG  . ASP A 171 ? 0.19372 0.18914 0.19318 -0.00721 0.00247  0.00222  157 ASP A CG  
1268 O OD1 . ASP A 171 ? 0.14978 0.14599 0.14979 -0.00805 0.00211  0.00199  157 ASP A OD1 
1269 O OD2 . ASP A 171 ? 0.15705 0.15053 0.15714 -0.00703 0.00259  0.00225  157 ASP A OD2 
1270 N N   . VAL A 172 ? 0.05382 0.05401 0.05205 -0.00696 0.00244  0.00450  158 VAL A N   
1271 C CA  . VAL A 172 ? 0.05208 0.05256 0.05071 -0.00692 0.00266  0.00530  158 VAL A CA  
1272 C C   . VAL A 172 ? 0.11049 0.11104 0.11044 -0.00784 0.00270  0.00520  158 VAL A C   
1273 O O   . VAL A 172 ? 0.07400 0.07522 0.07439 -0.00850 0.00206  0.00456  158 VAL A O   
1274 C CB  . VAL A 172 ? 0.09766 0.09953 0.09588 -0.00657 0.00207  0.00552  158 VAL A CB  
1275 C CG1 . VAL A 172 ? 0.09207 0.09446 0.09070 -0.00638 0.00219  0.00602  158 VAL A CG1 
1276 C CG2 . VAL A 172 ? 0.11723 0.11905 0.11461 -0.00568 0.00201  0.00571  158 VAL A CG2 
1277 N N   . LYS A 173 ? 0.09072 0.09068 0.09135 -0.00790 0.00345  0.00592  159 LYS A N   
1278 C CA  . LYS A 173 ? 0.07889 0.07908 0.08124 -0.00881 0.00365  0.00600  159 LYS A CA  
1279 C C   . LYS A 173 ? 0.08697 0.08687 0.08966 -0.00862 0.00475  0.00722  159 LYS A C   
1280 O O   . LYS A 173 ? 0.09704 0.09596 0.09852 -0.00787 0.00520  0.00787  159 LYS A O   
1281 C CB  . LYS A 173 ? 0.08707 0.08609 0.09040 -0.00962 0.00329  0.00523  159 LYS A CB  
1282 C CG  . LYS A 173 ? 0.12076 0.11776 0.12386 -0.00937 0.00365  0.00540  159 LYS A CG  
1283 C CD  . LYS A 173 ? 0.11286 0.10859 0.11711 -0.01008 0.00304  0.00437  159 LYS A CD  
1284 C CE  . LYS A 173 ? 0.13647 0.12993 0.14070 -0.00972 0.00322  0.00447  159 LYS A CE  
1285 N NZ  . LYS A 173 ? 0.14608 0.13810 0.15153 -0.01028 0.00240  0.00324  159 LYS A NZ  
1286 N N   . PRO A 174 ? 0.07712 0.07800 0.08144 -0.00925 0.00520  0.00762  160 PRO A N   
1287 C CA  . PRO A 174 ? 0.08620 0.08724 0.09072 -0.00906 0.00645  0.00899  160 PRO A CA  
1288 C C   . PRO A 174 ? 0.08965 0.08855 0.09390 -0.00913 0.00702  0.00989  160 PRO A C   
1289 O O   . PRO A 174 ? 0.10714 0.10576 0.11007 -0.00837 0.00779  0.01103  160 PRO A O   
1290 C CB  . PRO A 174 ? 0.11217 0.11470 0.11917 -0.01003 0.00679  0.00909  160 PRO A CB  
1291 C CG  . PRO A 174 ? 0.08905 0.09269 0.09639 -0.01015 0.00557  0.00774  160 PRO A CG  
1292 C CD  . PRO A 174 ? 0.08597 0.08816 0.09203 -0.01006 0.00462  0.00690  160 PRO A CD  
1293 N N   . HIS A 175 ? 0.08762 0.08492 0.09302 -0.00992 0.00652  0.00937  161 HIS A N   
1294 C CA  . HIS A 175 ? 0.12593 0.12091 0.13133 -0.00995 0.00683  0.01017  161 HIS A CA  
1295 C C   . HIS A 175 ? 0.17613 0.17014 0.17911 -0.00863 0.00675  0.01031  161 HIS A C   
1296 O O   . HIS A 175 ? 0.20583 0.19837 0.20827 -0.00829 0.00727  0.01152  161 HIS A O   
1297 C CB  . HIS A 175 ? 0.12834 0.12164 0.13530 -0.01078 0.00597  0.00915  161 HIS A CB  
1298 C CG  . HIS A 175 ? 0.33079 0.32142 0.33791 -0.01072 0.00601  0.00981  161 HIS A CG  
1299 N ND1 . HIS A 175 ? 0.34862 0.33814 0.35764 -0.01165 0.00658  0.01125  161 HIS A ND1 
1300 C CD2 . HIS A 175 ? 0.38108 0.36997 0.38684 -0.00980 0.00553  0.00933  161 HIS A CD2 
1301 C CE1 . HIS A 175 ? 0.50735 0.49426 0.51611 -0.01133 0.00630  0.01163  161 HIS A CE1 
1302 N NE2 . HIS A 175 ? 0.48626 0.47278 0.49304 -0.01013 0.00565  0.01039  161 HIS A NE2 
1303 N N   . ASN A 176 ? 0.11303 0.10785 0.11467 -0.00790 0.00606  0.00919  162 ASN A N   
1304 C CA  . ASN A 176 ? 0.10727 0.10144 0.10702 -0.00667 0.00586  0.00920  162 ASN A CA  
1305 C C   . ASN A 176 ? 0.11809 0.11353 0.11633 -0.00571 0.00617  0.00989  162 ASN A C   
1306 O O   . ASN A 176 ? 0.11649 0.11170 0.11331 -0.00465 0.00581  0.00977  162 ASN A O   
1307 C CB  . ASN A 176 ? 0.09101 0.08542 0.09037 -0.00642 0.00497  0.00770  162 ASN A CB  
1308 C CG  . ASN A 176 ? 0.14511 0.13790 0.14537 -0.00684 0.00457  0.00685  162 ASN A CG  
1309 O OD1 . ASN A 176 ? 0.11299 0.10390 0.11404 -0.00708 0.00480  0.00746  162 ASN A OD1 
1310 N ND2 . ASN A 176 ? 0.09751 0.09099 0.09766 -0.00691 0.00392  0.00546  162 ASN A ND2 
1311 N N   . VAL A 177 ? 0.12141 0.11830 0.12003 -0.00596 0.00675  0.01047  163 VAL A N   
1312 C CA  . VAL A 177 ? 0.12134 0.11948 0.11848 -0.00491 0.00701  0.01097  163 VAL A CA  
1313 C C   . VAL A 177 ? 0.17515 0.17316 0.17212 -0.00493 0.00827  0.01256  163 VAL A C   
1314 O O   . VAL A 177 ? 0.16660 0.16597 0.16485 -0.00561 0.00900  0.01297  163 VAL A O   
1315 C CB  . VAL A 177 ? 0.10268 0.10294 0.10028 -0.00493 0.00654  0.01011  163 VAL A CB  
1316 C CG1 . VAL A 177 ? 0.12627 0.12769 0.12239 -0.00370 0.00671  0.01044  163 VAL A CG1 
1317 C CG2 . VAL A 177 ? 0.12632 0.12667 0.12396 -0.00500 0.00534  0.00888  163 VAL A CG2 
1318 N N   A MET A 178 ? 0.10383 0.10025 0.09936 -0.00423 0.00853  0.01356  164 MET A N   
1319 N N   B MET A 178 ? 0.10272 0.09926 0.09815 -0.00416 0.00854  0.01356  164 MET A N   
1320 C CA  A MET A 178 ? 0.11622 0.11239 0.11125 -0.00423 0.00975  0.01539  164 MET A CA  
1321 C CA  B MET A 178 ? 0.11577 0.11194 0.11084 -0.00425 0.00976  0.01541  164 MET A CA  
1322 C C   A MET A 178 ? 0.11315 0.11138 0.10643 -0.00309 0.01026  0.01570  164 MET A C   
1323 C C   B MET A 178 ? 0.11340 0.11138 0.10650 -0.00305 0.01034  0.01592  164 MET A C   
1324 O O   A MET A 178 ? 0.13079 0.12943 0.12245 -0.00185 0.00942  0.01484  164 MET A O   
1325 O O   B MET A 178 ? 0.11155 0.10948 0.10262 -0.00167 0.00962  0.01544  164 MET A O   
1326 C CB  A MET A 178 ? 0.13235 0.12599 0.12617 -0.00370 0.00964  0.01638  164 MET A CB  
1327 C CB  B MET A 178 ? 0.13000 0.12350 0.12420 -0.00392 0.00962  0.01633  164 MET A CB  
1328 C CG  A MET A 178 ? 0.18219 0.17357 0.17779 -0.00466 0.00913  0.01608  164 MET A CG  
1329 C CG  B MET A 178 ? 0.18726 0.17886 0.18342 -0.00495 0.00903  0.01572  164 MET A CG  
1330 S SD  A MET A 178 ? 0.17061 0.16189 0.16922 -0.00660 0.00995  0.01696  164 MET A SD  
1331 S SD  B MET A 178 ? 0.21491 0.20330 0.21071 -0.00482 0.00910  0.01729  164 MET A SD  
1332 C CE  A MET A 178 ? 0.30375 0.29189 0.30398 -0.00725 0.00892  0.01630  164 MET A CE  
1333 C CE  B MET A 178 ? 0.33742 0.32664 0.33243 -0.00499 0.01069  0.01984  164 MET A CE  
1334 N N   . ILE A 179 ? 0.12189 0.12157 0.11568 -0.00350 0.01159  0.01684  165 ILE A N   
1335 C CA  . ILE A 179 ? 0.10302 0.10492 0.09509 -0.00228 0.01222  0.01706  165 ILE A CA  
1336 C C   . ILE A 179 ? 0.13344 0.13563 0.12467 -0.00230 0.01390  0.01929  165 ILE A C   
1337 O O   . ILE A 179 ? 0.17075 0.17360 0.16419 -0.00367 0.01502  0.02032  165 ILE A O   
1338 C CB  . ILE A 179 ? 0.11706 0.12155 0.11074 -0.00252 0.01216  0.01580  165 ILE A CB  
1339 C CG1 . ILE A 179 ? 0.11981 0.12401 0.11393 -0.00239 0.01043  0.01384  165 ILE A CG1 
1340 C CG2 . ILE A 179 ? 0.13445 0.14134 0.12643 -0.00113 0.01295  0.01599  165 ILE A CG2 
1341 C CD1 . ILE A 179 ? 0.16429 0.17069 0.16007 -0.00263 0.01008  0.01262  165 ILE A CD1 
1342 N N   . ASP A 180 ? 0.08043 0.08217 0.06853 -0.00081 0.01402  0.02010  166 ASP A N   
1343 C CA  . ASP A 180 ? 0.11506 0.11757 0.10150 -0.00043 0.01566  0.02227  166 ASP A CA  
1344 C C   . ASP A 180 ? 0.12640 0.13226 0.11181 0.00072  0.01630  0.02155  166 ASP A C   
1345 O O   . ASP A 180 ? 0.14757 0.15389 0.13046 0.00250  0.01543  0.02045  166 ASP A O   
1346 C CB  . ASP A 180 ? 0.17312 0.17343 0.15641 0.00082  0.01518  0.02327  166 ASP A CB  
1347 C CG  . ASP A 180 ? 0.21795 0.21899 0.19880 0.00142  0.01680  0.02571  166 ASP A CG  
1348 O OD1 . ASP A 180 ? 0.21833 0.22223 0.19933 0.00136  0.01835  0.02633  166 ASP A OD1 
1349 O OD2 . ASP A 180 ? 0.21535 0.21418 0.19403 0.00204  0.01654  0.02707  166 ASP A OD2 
1350 N N   . HIS A 181 ? 0.13160 0.13985 0.11922 -0.00026 0.01769  0.02202  167 HIS A N   
1351 C CA  . HIS A 181 ? 0.14573 0.15744 0.13296 0.00081  0.01831  0.02110  167 HIS A CA  
1352 C C   . HIS A 181 ? 0.17376 0.18709 0.15768 0.00230  0.01979  0.02256  167 HIS A C   
1353 O O   . HIS A 181 ? 0.22820 0.24438 0.21104 0.00372  0.02017  0.02157  167 HIS A O   
1354 C CB  . HIS A 181 ? 0.16262 0.17649 0.15378 -0.00079 0.01926  0.02105  167 HIS A CB  
1355 C CG  . HIS A 181 ? 0.17615 0.19344 0.16773 0.00024  0.01945  0.01949  167 HIS A CG  
1356 N ND1 . HIS A 181 ? 0.18188 0.19930 0.17233 0.00168  0.01772  0.01718  167 HIS A ND1 
1357 C CD2 . HIS A 181 ? 0.19645 0.21717 0.18979 0.00003  0.02106  0.01986  167 HIS A CD2 
1358 C CE1 . HIS A 181 ? 0.15524 0.17582 0.14659 0.00242  0.01816  0.01612  167 HIS A CE1 
1359 N NE2 . HIS A 181 ? 0.19971 0.22250 0.19280 0.00149  0.02023  0.01766  167 HIS A NE2 
1360 N N   . GLN A 182 ? 0.20404 0.21563 0.18625 0.00212  0.02055  0.02487  168 GLN A N   
1361 C CA  . GLN A 182 ? 0.17960 0.19216 0.15849 0.00350  0.02134  0.02578  168 GLN A CA  
1362 C C   . GLN A 182 ? 0.16748 0.17919 0.14239 0.00586  0.01992  0.02466  168 GLN A C   
1363 O O   . GLN A 182 ? 0.15634 0.17023 0.12887 0.00770  0.02004  0.02374  168 GLN A O   
1364 C CB  . GLN A 182 ? 0.16486 0.17530 0.14382 0.00222  0.02193  0.02806  168 GLN A CB  
1365 C CG  . GLN A 182 ? 0.28364 0.29538 0.26612 0.00011  0.02345  0.02931  168 GLN A CG  
1366 C CD  . GLN A 182 ? 0.31038 0.32168 0.29711 -0.00166 0.02308  0.02862  168 GLN A CD  
1367 O OE1 . GLN A 182 ? 0.55354 0.56180 0.54118 -0.00243 0.02194  0.02863  168 GLN A OE1 
1368 N NE2 . GLN A 182 ? 0.42351 0.43794 0.41289 -0.00222 0.02396  0.02790  168 GLN A NE2 
1369 N N   . GLN A 183 ? 0.12747 0.13605 0.10184 0.00589  0.01840  0.02450  169 GLN A N   
1370 C CA  . GLN A 183 ? 0.18085 0.18819 0.15212 0.00790  0.01660  0.02321  169 GLN A CA  
1371 C C   . GLN A 183 ? 0.14467 0.15215 0.11736 0.00831  0.01464  0.02028  169 GLN A C   
1372 O O   . GLN A 183 ? 0.18448 0.19098 0.15522 0.00983  0.01292  0.01903  169 GLN A O   
1373 C CB  . GLN A 183 ? 0.15783 0.16162 0.12797 0.00775  0.01579  0.02450  169 GLN A CB  
1374 C CG  . GLN A 183 ? 0.14683 0.15000 0.11529 0.00764  0.01674  0.02661  169 GLN A CG  
1375 C CD  . GLN A 183 ? 0.18684 0.18641 0.15423 0.00768  0.01560  0.02762  169 GLN A CD  
1376 O OE1 . GLN A 183 ? 0.26025 0.25818 0.22867 0.00630  0.01618  0.02946  169 GLN A OE1 
1377 N NE2 . GLN A 183 ? 0.20089 0.19923 0.16636 0.00931  0.01385  0.02640  169 GLN A NE2 
1378 N N   . LYS A 184 ? 0.16948 0.17812 0.14563 0.00695  0.01476  0.01926  170 LYS A N   
1379 C CA  . LYS A 184 ? 0.19154 0.20027 0.16930 0.00708  0.01293  0.01676  170 LYS A CA  
1380 C C   . LYS A 184 ? 0.18668 0.19254 0.16453 0.00695  0.01112  0.01616  170 LYS A C   
1381 O O   . LYS A 184 ? 0.20635 0.21183 0.18315 0.00822  0.00941  0.01467  170 LYS A O   
1382 C CB  . LYS A 184 ? 0.19755 0.20844 0.17362 0.00910  0.01229  0.01507  170 LYS A CB  
1383 C CG  . LYS A 184 ? 0.34513 0.35928 0.32088 0.00956  0.01420  0.01556  170 LYS A CG  
1384 C CD  . LYS A 184 ? 0.30203 0.31771 0.28174 0.00783  0.01494  0.01525  170 LYS A CD  
1385 C CE  . LYS A 184 ? 0.27453 0.29396 0.25437 0.00852  0.01665  0.01528  170 LYS A CE  
1386 N NZ  . LYS A 184 ? 0.25507 0.27567 0.23536 0.00737  0.01920  0.01788  170 LYS A NZ  
1387 N N   A LYS A 185 ? 0.16571 0.16962 0.14512 0.00539  0.01145  0.01725  171 LYS A N   
1388 N N   B LYS A 185 ? 0.16651 0.17038 0.14572 0.00547  0.01149  0.01734  171 LYS A N   
1389 C CA  A LYS A 185 ? 0.14643 0.14780 0.12607 0.00526  0.01001  0.01682  171 LYS A CA  
1390 C CA  B LYS A 185 ? 0.14676 0.14816 0.12647 0.00522  0.01003  0.01681  171 LYS A CA  
1391 C C   A LYS A 185 ? 0.15058 0.15125 0.13354 0.00340  0.00978  0.01624  171 LYS A C   
1392 C C   B LYS A 185 ? 0.14420 0.14529 0.12729 0.00342  0.00976  0.01601  171 LYS A C   
1393 O O   A LYS A 185 ? 0.13953 0.14015 0.12420 0.00196  0.01095  0.01725  171 LYS A O   
1394 O O   B LYS A 185 ? 0.15299 0.15484 0.13800 0.00207  0.01090  0.01660  171 LYS A O   
1395 C CB  A LYS A 185 ? 0.14791 0.14715 0.12569 0.00558  0.01039  0.01866  171 LYS A CB  
1396 C CB  B LYS A 185 ? 0.14250 0.14157 0.12090 0.00520  0.01043  0.01866  171 LYS A CB  
1397 C CG  A LYS A 185 ? 0.13774 0.13445 0.11651 0.00517  0.00917  0.01829  171 LYS A CG  
1398 C CG  B LYS A 185 ? 0.21465 0.21389 0.18937 0.00689  0.01087  0.01988  171 LYS A CG  
1399 C CD  A LYS A 185 ? 0.28337 0.27806 0.25970 0.00625  0.00885  0.01957  171 LYS A CD  
1400 C CD  B LYS A 185 ? 0.20503 0.20154 0.17852 0.00696  0.01079  0.02159  171 LYS A CD  
1401 C CE  A LYS A 185 ? 0.20527 0.19923 0.18095 0.00561  0.01045  0.02205  171 LYS A CE  
1402 C CE  B LYS A 185 ? 0.27521 0.26978 0.24908 0.00746  0.00884  0.02027  171 LYS A CE  
1403 N NZ  A LYS A 185 ? 0.36189 0.35370 0.33499 0.00675  0.00999  0.02342  171 LYS A NZ  
1404 N NZ  B LYS A 185 ? 0.27493 0.26678 0.24769 0.00778  0.00849  0.02170  171 LYS A NZ  
1405 N N   . LEU A 186 ? 0.12038 0.12051 0.10423 0.00343  0.00823  0.01468  172 LEU A N   
1406 C CA  . LEU A 186 ? 0.11075 0.11052 0.09732 0.00191  0.00785  0.01387  172 LEU A CA  
1407 C C   . LEU A 186 ? 0.10476 0.10255 0.09149 0.00192  0.00685  0.01353  172 LEU A C   
1408 O O   . LEU A 186 ? 0.12643 0.12388 0.11188 0.00313  0.00579  0.01302  172 LEU A O   
1409 C CB  . LEU A 186 ? 0.11279 0.11433 0.10054 0.00186  0.00701  0.01228  172 LEU A CB  
1410 C CG  . LEU A 186 ? 0.09897 0.10049 0.08920 0.00042  0.00646  0.01136  172 LEU A CG  
1411 C CD1 . LEU A 186 ? 0.14219 0.14570 0.13371 0.00012  0.00625  0.01046  172 LEU A CD1 
1412 C CD2 . LEU A 186 ? 0.06762 0.06821 0.05794 0.00061  0.00511  0.01050  172 LEU A CD2 
1413 N N   . ARG A 187 ? 0.07915 0.07577 0.06762 0.00063  0.00709  0.01366  173 ARG A N   
1414 C CA  . ARG A 187 ? 0.11333 0.10840 0.10223 0.00067  0.00621  0.01308  173 ARG A CA  
1415 C C   . ARG A 187 ? 0.11164 0.10691 0.10275 -0.00066 0.00600  0.01206  173 ARG A C   
1416 O O   . ARG A 187 ? 0.14400 0.13922 0.13644 -0.00183 0.00670  0.01239  173 ARG A O   
1417 C CB  . ARG A 187 ? 0.08574 0.07855 0.07401 0.00083  0.00658  0.01433  173 ARG A CB  
1418 C CG  . ARG A 187 ? 0.10535 0.09767 0.09105 0.00230  0.00658  0.01540  173 ARG A CG  
1419 C CD  . ARG A 187 ? 0.08488 0.07745 0.06963 0.00366  0.00521  0.01431  173 ARG A CD  
1420 N NE  . ARG A 187 ? 0.14718 0.13896 0.12939 0.00516  0.00499  0.01527  173 ARG A NE  
1421 C CZ  . ARG A 187 ? 0.23434 0.22736 0.21454 0.00625  0.00497  0.01539  173 ARG A CZ  
1422 N NH1 . ARG A 187 ? 0.15912 0.15419 0.13976 0.00604  0.00514  0.01459  173 ARG A NH1 
1423 N NH2 . ARG A 187 ? 0.19681 0.18896 0.17446 0.00769  0.00467  0.01626  173 ARG A NH2 
1424 N N   . LEU A 188 ? 0.05939 0.05497 0.05092 -0.00048 0.00502  0.01089  174 LEU A N   
1425 C CA  . LEU A 188 ? 0.07269 0.06836 0.06582 -0.00151 0.00475  0.00992  174 LEU A CA  
1426 C C   . LEU A 188 ? 0.06063 0.05442 0.05404 -0.00145 0.00474  0.00991  174 LEU A C   
1427 O O   . LEU A 188 ? 0.07928 0.07246 0.07199 -0.00044 0.00426  0.00983  174 LEU A O   
1428 C CB  . LEU A 188 ? 0.07521 0.07230 0.06857 -0.00129 0.00381  0.00889  174 LEU A CB  
1429 C CG  . LEU A 188 ? 0.09069 0.08834 0.08528 -0.00221 0.00350  0.00793  174 LEU A CG  
1430 C CD1 . LEU A 188 ? 0.11149 0.10935 0.10707 -0.00342 0.00392  0.00783  174 LEU A CD1 
1431 C CD2 . LEU A 188 ? 0.12073 0.11997 0.11551 -0.00206 0.00262  0.00736  174 LEU A CD2 
1432 N N   . ILE A 189 ? 0.09651 0.08935 0.09110 -0.00246 0.00513  0.00991  175 ILE A N   
1433 C CA  . ILE A 189 ? 0.08110 0.07182 0.07614 -0.00240 0.00502  0.00985  175 ILE A CA  
1434 C C   . ILE A 189 ? 0.09248 0.08334 0.08870 -0.00296 0.00457  0.00834  175 ILE A C   
1435 O O   . ILE A 189 ? 0.10298 0.09554 0.09955 -0.00351 0.00441  0.00756  175 ILE A O   
1436 C CB  . ILE A 189 ? 0.11460 0.10366 0.11014 -0.00303 0.00569  0.01120  175 ILE A CB  
1437 C CG1 . ILE A 189 ? 0.07315 0.06290 0.07036 -0.00449 0.00604  0.01099  175 ILE A CG1 
1438 C CG2 . ILE A 189 ? 0.10497 0.09415 0.09897 -0.00240 0.00629  0.01282  175 ILE A CG2 
1439 C CD1 . ILE A 189 ? 0.07860 0.06635 0.07726 -0.00541 0.00638  0.01191  175 ILE A CD1 
1440 N N   . ASP A 190 ? 0.08243 0.07139 0.07919 -0.00277 0.00433  0.00795  176 ASP A N   
1441 C CA  . ASP A 190 ? 0.09809 0.08679 0.09579 -0.00306 0.00388  0.00641  176 ASP A CA  
1442 C C   . ASP A 190 ? 0.08827 0.07908 0.08555 -0.00265 0.00358  0.00516  176 ASP A C   
1443 O O   . ASP A 190 ? 0.11045 0.10284 0.10791 -0.00338 0.00352  0.00455  176 ASP A O   
1444 C CB  . ASP A 190 ? 0.08056 0.06881 0.07959 -0.00438 0.00391  0.00614  176 ASP A CB  
1445 C CG  . ASP A 190 ? 0.23591 0.22299 0.23577 -0.00437 0.00326  0.00455  176 ASP A CG  
1446 O OD1 . ASP A 190 ? 0.14405 0.13105 0.14339 -0.00329 0.00294  0.00362  176 ASP A OD1 
1447 O OD2 . ASP A 190 ? 0.22440 0.21070 0.22553 -0.00535 0.00301  0.00414  176 ASP A OD2 
1448 N N   . TRP A 191 ? 0.09442 0.08524 0.09128 -0.00149 0.00335  0.00484  177 TRP A N   
1449 C CA  . TRP A 191 ? 0.06823 0.06118 0.06493 -0.00101 0.00317  0.00390  177 TRP A CA  
1450 C C   . TRP A 191 ? 0.06479 0.05775 0.06196 -0.00073 0.00300  0.00230  177 TRP A C   
1451 O O   . TRP A 191 ? 0.10814 0.10276 0.10530 -0.00004 0.00298  0.00153  177 TRP A O   
1452 C CB  . TRP A 191 ? 0.11917 0.11250 0.11545 0.00012  0.00298  0.00447  177 TRP A CB  
1453 C CG  . TRP A 191 ? 0.10317 0.09690 0.09873 -0.00005 0.00304  0.00573  177 TRP A CG  
1454 C CD1 . TRP A 191 ? 0.09797 0.09017 0.09289 -0.00001 0.00326  0.00693  177 TRP A CD1 
1455 C CD2 . TRP A 191 ? 0.08968 0.08552 0.08510 -0.00028 0.00284  0.00585  177 TRP A CD2 
1456 N NE1 . TRP A 191 ? 0.08551 0.07890 0.07974 -0.00002 0.00325  0.00759  177 TRP A NE1 
1457 C CE2 . TRP A 191 ? 0.05110 0.04655 0.04574 -0.00019 0.00288  0.00688  177 TRP A CE2 
1458 C CE3 . TRP A 191 ? 0.05910 0.05711 0.05501 -0.00054 0.00260  0.00524  177 TRP A CE3 
1459 C CZ2 . TRP A 191 ? 0.08487 0.08186 0.07930 -0.00023 0.00252  0.00707  177 TRP A CZ2 
1460 C CZ3 . TRP A 191 ? 0.07033 0.06972 0.06620 -0.00076 0.00222  0.00568  177 TRP A CZ3 
1461 C CH2 . TRP A 191 ? 0.08333 0.08212 0.07850 -0.00055 0.00209  0.00646  177 TRP A CH2 
1462 N N   . GLY A 192 ? 0.06918 0.06046 0.06688 -0.00125 0.00286  0.00175  178 GLY A N   
1463 C CA  . GLY A 192 ? 0.10703 0.09808 0.10505 -0.00079 0.00254  -0.00000 178 GLY A CA  
1464 C C   . GLY A 192 ? 0.11157 0.10507 0.10909 -0.00118 0.00262  -0.00110 178 GLY A C   
1465 O O   . GLY A 192 ? 0.16018 0.15427 0.15756 -0.00048 0.00250  -0.00265 178 GLY A O   
1466 N N   . LEU A 193 ? 0.08774 0.08271 0.08490 -0.00218 0.00280  -0.00034 179 LEU A N   
1467 C CA  . LEU A 193 ? 0.13909 0.13648 0.13558 -0.00256 0.00283  -0.00103 179 LEU A CA  
1468 C C   . LEU A 193 ? 0.09131 0.09115 0.08743 -0.00238 0.00313  -0.00028 179 LEU A C   
1469 O O   . LEU A 193 ? 0.07759 0.07957 0.07315 -0.00274 0.00320  -0.00052 179 LEU A O   
1470 C CB  . LEU A 193 ? 0.15210 0.14946 0.14861 -0.00384 0.00255  -0.00084 179 LEU A CB  
1471 C CG  . LEU A 193 ? 0.22747 0.22295 0.22458 -0.00425 0.00204  -0.00187 179 LEU A CG  
1472 C CD1 . LEU A 193 ? 0.16783 0.16386 0.16511 -0.00548 0.00169  -0.00171 179 LEU A CD1 
1473 C CD2 . LEU A 193 ? 0.29556 0.29107 0.29216 -0.00340 0.00176  -0.00377 179 LEU A CD2 
1474 N N   . ALA A 194 ? 0.05956 0.05912 0.05601 -0.00186 0.00322  0.00069  180 ALA A N   
1475 C CA  . ALA A 194 ? 0.05274 0.05445 0.04924 -0.00177 0.00327  0.00143  180 ALA A CA  
1476 C C   . ALA A 194 ? 0.09649 0.10034 0.09312 -0.00112 0.00357  0.00063  180 ALA A C   
1477 O O   . ALA A 194 ? 0.08473 0.08819 0.08142 -0.00029 0.00373  -0.00054 180 ALA A O   
1478 C CB  . ALA A 194 ? 0.07893 0.07966 0.07570 -0.00120 0.00310  0.00245  180 ALA A CB  
1479 N N   . GLU A 195 ? 0.09957 0.10581 0.09640 -0.00148 0.00362  0.00129  181 GLU A N   
1480 C CA  . GLU A 195 ? 0.07007 0.07895 0.06716 -0.00108 0.00410  0.00079  181 GLU A CA  
1481 C C   . GLU A 195 ? 0.07841 0.08926 0.07653 -0.00128 0.00397  0.00197  181 GLU A C   
1482 O O   . GLU A 195 ? 0.09889 0.10927 0.09717 -0.00196 0.00341  0.00302  181 GLU A O   
1483 C CB  . GLU A 195 ? 0.14733 0.15752 0.14330 -0.00174 0.00437  0.00021  181 GLU A CB  
1484 C CG  . GLU A 195 ? 0.22277 0.23603 0.21856 -0.00135 0.00509  -0.00033 181 GLU A CG  
1485 C CD  . GLU A 195 ? 0.17806 0.19161 0.17443 0.00015  0.00554  -0.00164 181 GLU A CD  
1486 O OE1 . GLU A 195 ? 0.16944 0.18329 0.16721 0.00077  0.00553  -0.00121 181 GLU A OE1 
1487 O OE2 . GLU A 195 ? 0.33796 0.35148 0.33346 0.00080  0.00578  -0.00321 181 GLU A OE2 
1488 N N   . PHE A 196 ? 0.05510 0.06821 0.05414 -0.00065 0.00443  0.00171  182 PHE A N   
1489 C CA  . PHE A 196 ? 0.07613 0.09145 0.07662 -0.00096 0.00428  0.00282  182 PHE A CA  
1490 C C   . PHE A 196 ? 0.09769 0.11521 0.09787 -0.00222 0.00448  0.00364  182 PHE A C   
1491 O O   . PHE A 196 ? 0.12823 0.14711 0.12735 -0.00234 0.00519  0.00306  182 PHE A O   
1492 C CB  . PHE A 196 ? 0.09857 0.11589 0.10053 0.00013  0.00478  0.00228  182 PHE A CB  
1493 C CG  . PHE A 196 ? 0.07931 0.09456 0.08182 0.00144  0.00435  0.00169  182 PHE A CG  
1494 C CD1 . PHE A 196 ? 0.11229 0.12585 0.11405 0.00241  0.00458  0.00036  182 PHE A CD1 
1495 C CD2 . PHE A 196 ? 0.09437 0.10918 0.09811 0.00172  0.00354  0.00247  182 PHE A CD2 
1496 C CE1 . PHE A 196 ? 0.14446 0.15592 0.14669 0.00359  0.00408  0.00000  182 PHE A CE1 
1497 C CE2 . PHE A 196 ? 0.14486 0.15768 0.14883 0.00299  0.00305  0.00204  182 PHE A CE2 
1498 C CZ  . PHE A 196 ? 0.09076 0.10187 0.09396 0.00389  0.00334  0.00091  182 PHE A CZ  
1499 N N   . TYR A 197 ? 0.09886 0.11672 0.09991 -0.00308 0.00376  0.00498  183 TYR A N   
1500 C CA  . TYR A 197 ? 0.07344 0.09325 0.07445 -0.00434 0.00376  0.00605  183 TYR A CA  
1501 C C   . TYR A 197 ? 0.09286 0.11604 0.09556 -0.00444 0.00434  0.00675  183 TYR A C   
1502 O O   . TYR A 197 ? 0.09613 0.11984 0.10091 -0.00416 0.00391  0.00721  183 TYR A O   
1503 C CB  . TYR A 197 ? 0.07820 0.09673 0.07957 -0.00524 0.00254  0.00715  183 TYR A CB  
1504 C CG  . TYR A 197 ? 0.07107 0.09148 0.07263 -0.00653 0.00237  0.00843  183 TYR A CG  
1505 C CD1 . TYR A 197 ? 0.06682 0.08750 0.06655 -0.00715 0.00269  0.00836  183 TYR A CD1 
1506 C CD2 . TYR A 197 ? 0.12610 0.14807 0.12976 -0.00713 0.00182  0.00976  183 TYR A CD2 
1507 C CE1 . TYR A 197 ? 0.13384 0.15620 0.13354 -0.00830 0.00251  0.00971  183 TYR A CE1 
1508 C CE2 . TYR A 197 ? 0.12638 0.14998 0.13032 -0.00841 0.00163  0.01119  183 TYR A CE2 
1509 C CZ  . TYR A 197 ? 0.15928 0.18307 0.16110 -0.00898 0.00201  0.01122  183 TYR A CZ  
1510 O OH  . TYR A 197 ? 0.12751 0.15282 0.12940 -0.01024 0.00176  0.01281  183 TYR A OH  
1511 N N   . HIS A 198 ? 0.09194 0.11752 0.09377 -0.00483 0.00531  0.00685  184 HIS A N   
1512 C CA  . HIS A 198 ? 0.08958 0.11889 0.09292 -0.00520 0.00609  0.00783  184 HIS A CA  
1513 C C   . HIS A 198 ? 0.11219 0.14284 0.11459 -0.00667 0.00608  0.00931  184 HIS A C   
1514 O O   . HIS A 198 ? 0.13714 0.16729 0.13703 -0.00679 0.00635  0.00877  184 HIS A O   
1515 C CB  . HIS A 198 ? 0.12939 0.16081 0.13231 -0.00398 0.00753  0.00645  184 HIS A CB  
1516 C CG  . HIS A 198 ? 0.12973 0.15979 0.13366 -0.00247 0.00742  0.00504  184 HIS A CG  
1517 N ND1 . HIS A 198 ? 0.19450 0.22557 0.20117 -0.00206 0.00716  0.00544  184 HIS A ND1 
1518 C CD2 . HIS A 198 ? 0.14447 0.17209 0.14714 -0.00129 0.00738  0.00331  184 HIS A CD2 
1519 C CE1 . HIS A 198 ? 0.13642 0.16576 0.14326 -0.00062 0.00699  0.00403  184 HIS A CE1 
1520 N NE2 . HIS A 198 ? 0.14313 0.17029 0.14760 -0.00016 0.00712  0.00279  184 HIS A NE2 
1521 N N   . PRO A 199 ? 0.13037 0.16268 0.13478 -0.00780 0.00567  0.01121  185 PRO A N   
1522 C CA  . PRO A 199 ? 0.12602 0.15922 0.12960 -0.00928 0.00543  0.01289  185 PRO A CA  
1523 C C   . PRO A 199 ? 0.10870 0.14457 0.11006 -0.00925 0.00694  0.01278  185 PRO A C   
1524 O O   . PRO A 199 ? 0.15000 0.18871 0.15179 -0.00851 0.00837  0.01229  185 PRO A O   
1525 C CB  . PRO A 199 ? 0.20998 0.24500 0.21679 -0.01034 0.00491  0.01490  185 PRO A CB  
1526 C CG  . PRO A 199 ? 0.27021 0.30428 0.27931 -0.00946 0.00434  0.01413  185 PRO A CG  
1527 C CD  . PRO A 199 ? 0.18588 0.21926 0.19360 -0.00779 0.00526  0.01194  185 PRO A CD  
1528 N N   . ALA A 200 ? 0.14830 0.18333 0.14725 -0.00996 0.00656  0.01318  186 ALA A N   
1529 C CA  . ALA A 200 ? 0.16471 0.20193 0.16092 -0.00997 0.00769  0.01313  186 ALA A CA  
1530 C C   . ALA A 200 ? 0.20170 0.23844 0.19570 -0.00839 0.00851  0.01054  186 ALA A C   
1531 O O   . ALA A 200 ? 0.22084 0.25936 0.21231 -0.00811 0.00938  0.01010  186 ALA A O   
1532 C CB  . ALA A 200 ? 0.13556 0.17721 0.13269 -0.01060 0.00901  0.01494  186 ALA A CB  
1533 N N   . GLN A 201 ? 0.14996 0.18429 0.14476 -0.00732 0.00816  0.00882  187 GLN A N   
1534 C CA  . GLN A 201 ? 0.15269 0.18616 0.14570 -0.00589 0.00867  0.00639  187 GLN A CA  
1535 C C   . GLN A 201 ? 0.14484 0.17569 0.13544 -0.00617 0.00775  0.00564  187 GLN A C   
1536 O O   . GLN A 201 ? 0.17636 0.20479 0.16737 -0.00703 0.00651  0.00638  187 GLN A O   
1537 C CB  . GLN A 201 ? 0.18679 0.21829 0.18157 -0.00477 0.00845  0.00508  187 GLN A CB  
1538 C CG  . GLN A 201 ? 0.20159 0.23220 0.19506 -0.00320 0.00891  0.00259  187 GLN A CG  
1539 C CD  . GLN A 201 ? 0.31524 0.34498 0.31075 -0.00199 0.00897  0.00164  187 GLN A CD  
1540 O OE1 . GLN A 201 ? 0.32910 0.36106 0.32674 -0.00183 0.00947  0.00238  187 GLN A OE1 
1541 N NE2 . GLN A 201 ? 0.31357 0.34006 0.30861 -0.00118 0.00836  0.00010  187 GLN A NE2 
1542 N N   . GLU A 202 ? 0.14212 0.17359 0.13028 -0.00537 0.00828  0.00407  188 GLU A N   
1543 C CA  . GLU A 202 ? 0.12600 0.15506 0.11205 -0.00552 0.00730  0.00309  188 GLU A CA  
1544 C C   . GLU A 202 ? 0.18417 0.21021 0.17064 -0.00448 0.00686  0.00096  188 GLU A C   
1545 O O   . GLU A 202 ? 0.18182 0.20841 0.16833 -0.00314 0.00758  -0.00065 188 GLU A O   
1546 C CB  . GLU A 202 ? 0.19247 0.22374 0.17546 -0.00527 0.00783  0.00259  188 GLU A CB  
1547 C CG  . GLU A 202 ? 0.20366 0.23731 0.18593 -0.00660 0.00797  0.00509  188 GLU A CG  
1548 C CD  . GLU A 202 ? 0.42290 0.45768 0.40162 -0.00658 0.00792  0.00480  188 GLU A CD  
1549 O OE1 . GLU A 202 ? 0.44313 0.47720 0.41996 -0.00539 0.00787  0.00242  188 GLU A OE1 
1550 O OE2 . GLU A 202 ? 0.28630 0.32255 0.26414 -0.00774 0.00780  0.00698  188 GLU A OE2 
1551 N N   . TYR A 203 ? 0.11389 0.13679 0.10082 -0.00508 0.00568  0.00100  189 TYR A N   
1552 C CA  . TYR A 203 ? 0.08038 0.10027 0.06812 -0.00438 0.00523  -0.00050 189 TYR A CA  
1553 C C   . TYR A 203 ? 0.19337 0.21140 0.17960 -0.00440 0.00441  -0.00191 189 TYR A C   
1554 O O   . TYR A 203 ? 0.14792 0.16643 0.13271 -0.00516 0.00388  -0.00147 189 TYR A O   
1555 C CB  . TYR A 203 ? 0.09720 0.11507 0.08696 -0.00498 0.00461  0.00066  189 TYR A CB  
1556 C CG  . TYR A 203 ? 0.12755 0.14674 0.11909 -0.00474 0.00515  0.00167  189 TYR A CG  
1557 C CD1 . TYR A 203 ? 0.14056 0.15906 0.13322 -0.00359 0.00553  0.00077  189 TYR A CD1 
1558 C CD2 . TYR A 203 ? 0.10095 0.12196 0.09324 -0.00565 0.00510  0.00353  189 TYR A CD2 
1559 C CE1 . TYR A 203 ? 0.08437 0.10412 0.07881 -0.00332 0.00585  0.00161  189 TYR A CE1 
1560 C CE2 . TYR A 203 ? 0.09843 0.12065 0.09269 -0.00546 0.00540  0.00438  189 TYR A CE2 
1561 C CZ  . TYR A 203 ? 0.11312 0.13477 0.10841 -0.00427 0.00577  0.00337  189 TYR A CZ  
1562 O OH  . TYR A 203 ? 0.12285 0.14571 0.12020 -0.00403 0.00591  0.00412  189 TYR A OH  
1563 N N   . ASN A 204 ? 0.16077 0.17654 0.14750 -0.00358 0.00417  -0.00359 190 ASN A N   
1564 C CA  . ASN A 204 ? 0.15480 0.16851 0.14069 -0.00362 0.00322  -0.00504 190 ASN A CA  
1565 C C   . ASN A 204 ? 0.15272 0.16457 0.13954 -0.00489 0.00229  -0.00395 190 ASN A C   
1566 O O   . ASN A 204 ? 0.17442 0.18509 0.16298 -0.00523 0.00231  -0.00291 190 ASN A O   
1567 C CB  . ASN A 204 ? 0.22467 0.23621 0.21144 -0.00252 0.00310  -0.00686 190 ASN A CB  
1568 C CG  . ASN A 204 ? 0.23768 0.24753 0.22355 -0.00230 0.00210  -0.00879 190 ASN A CG  
1569 O OD1 . ASN A 204 ? 0.23078 0.23967 0.21647 -0.00328 0.00121  -0.00853 190 ASN A OD1 
1570 N ND2 . ASN A 204 ? 0.30473 0.31420 0.29023 -0.00094 0.00211  -0.01085 190 ASN A ND2 
1571 N N   . VAL A 205 ? 0.11210 0.12383 0.09771 -0.00551 0.00143  -0.00422 191 VAL A N   
1572 C CA  . VAL A 205 ? 0.11661 0.12692 0.10328 -0.00664 0.00052  -0.00329 191 VAL A CA  
1573 C C   . VAL A 205 ? 0.12170 0.12925 0.10978 -0.00669 -0.00014 -0.00440 191 VAL A C   
1574 O O   . VAL A 205 ? 0.13239 0.13885 0.12169 -0.00756 -0.00078 -0.00375 191 VAL A O   
1575 C CB  . VAL A 205 ? 0.09362 0.10512 0.07869 -0.00738 -0.00025 -0.00277 191 VAL A CB  
1576 C CG1 . VAL A 205 ? 0.14205 0.15623 0.12607 -0.00758 0.00041  -0.00118 191 VAL A CG1 
1577 C CG2 . VAL A 205 ? 0.15208 0.16338 0.13534 -0.00689 -0.00091 -0.00469 191 VAL A CG2 
1578 N N   . ARG A 206 ? 0.13860 0.14504 0.12674 -0.00578 -0.00004 -0.00605 192 ARG A N   
1579 C CA  . ARG A 206 ? 0.15909 0.16275 0.14891 -0.00591 -0.00069 -0.00694 192 ARG A CA  
1580 C C   . ARG A 206 ? 0.19497 0.19733 0.18670 -0.00590 -0.00005 -0.00584 192 ARG A C   
1581 O O   . ARG A 206 ? 0.20013 0.20107 0.19257 -0.00515 0.00017  -0.00655 192 ARG A O   
1582 C CB  . ARG A 206 ? 0.26993 0.27270 0.25908 -0.00493 -0.00115 -0.00924 192 ARG A CB  
1583 C CG  . ARG A 206 ? 0.37167 0.37573 0.35855 -0.00475 -0.00188 -0.01049 192 ARG A CG  
1584 C CD  . ARG A 206 ? 0.57890 0.58199 0.56507 -0.00355 -0.00249 -0.01309 192 ARG A CD  
1585 N NE  . ARG A 206 ? 0.97841 0.97834 0.96689 -0.00390 -0.00357 -0.01399 192 ARG A NE  
1586 C CZ  . ARG A 206 ? 0.81816 0.81691 0.80737 -0.00475 -0.00490 -0.01449 192 ARG A CZ  
1587 N NH1 . ARG A 206 ? 0.59240 0.59269 0.58006 -0.00526 -0.00544 -0.01425 192 ARG A NH1 
1588 N NH2 . ARG A 206 ? 0.76927 0.76524 0.76101 -0.00513 -0.00578 -0.01515 192 ARG A NH2 
1589 N N   . VAL A 207 ? 0.16365 0.16648 0.15609 -0.00666 0.00015  -0.00411 193 VAL A N   
1590 C CA  . VAL A 207 ? 0.15507 0.15689 0.14898 -0.00668 0.00067  -0.00291 193 VAL A CA  
1591 C C   . VAL A 207 ? 0.16958 0.17091 0.16466 -0.00771 0.00028  -0.00193 193 VAL A C   
1592 O O   . VAL A 207 ? 0.14562 0.14765 0.14044 -0.00838 -0.00040 -0.00205 193 VAL A O   
1593 C CB  . VAL A 207 ? 0.14215 0.14556 0.13563 -0.00618 0.00142  -0.00187 193 VAL A CB  
1594 C CG1 . VAL A 207 ? 0.17772 0.18200 0.17034 -0.00509 0.00191  -0.00291 193 VAL A CG1 
1595 C CG2 . VAL A 207 ? 0.13888 0.14425 0.13175 -0.00685 0.00122  -0.00081 193 VAL A CG2 
1596 N N   . ALA A 208 ? 0.21439 0.21463 0.21076 -0.00775 0.00071  -0.00097 194 ALA A N   
1597 C CA  . ALA A 208 ? 0.17089 0.17078 0.16858 -0.00854 0.00058  -0.00007 194 ALA A CA  
1598 C C   . ALA A 208 ? 0.17783 0.17666 0.17682 -0.00930 -0.00003 -0.00078 194 ALA A C   
1599 O O   . ALA A 208 ? 0.23534 0.23390 0.23389 -0.00932 -0.00069 -0.00211 194 ALA A O   
1600 C CB  . ALA A 208 ? 0.16607 0.16772 0.16339 -0.00888 0.00033  0.00080  194 ALA A CB  
1601 N N   . SER A 209 ? 0.18424 0.18257 0.18490 -0.00988 0.00017  0.00005  195 SER A N   
1602 C CA  . SER A 209 ? 0.19735 0.19504 0.19982 -0.01077 -0.00041 -0.00041 195 SER A CA  
1603 C C   . SER A 209 ? 0.15395 0.15315 0.15626 -0.01127 -0.00128 -0.00074 195 SER A C   
1604 O O   . SER A 209 ? 0.12355 0.12417 0.12502 -0.01113 -0.00124 -0.00005 195 SER A O   
1605 C CB  . SER A 209 ? 0.25240 0.24965 0.25680 -0.01123 0.00031  0.00084  195 SER A CB  
1606 O OG  . SER A 209 ? 0.28686 0.28478 0.29316 -0.01216 -0.00017 0.00080  195 SER A OG  
1607 N N   . ARG A 210 ? 0.16153 0.16028 0.16479 -0.01185 -0.00226 -0.00182 196 ARG A N   
1608 C CA  . ARG A 210 ? 0.14241 0.14241 0.14544 -0.01228 -0.00334 -0.00227 196 ARG A CA  
1609 C C   . ARG A 210 ? 0.11244 0.11389 0.11611 -0.01251 -0.00319 -0.00109 196 ARG A C   
1610 O O   . ARG A 210 ? 0.10936 0.11198 0.11162 -0.01236 -0.00370 -0.00089 196 ARG A O   
1611 C CB  . ARG A 210 ? 0.14821 0.14742 0.15316 -0.01300 -0.00442 -0.00337 196 ARG A CB  
1612 C CG  . ARG A 210 ? 0.09947 0.09986 0.10418 -0.01336 -0.00577 -0.00392 196 ARG A CG  
1613 C CD  . ARG A 210 ? 0.14831 0.14794 0.15538 -0.01409 -0.00691 -0.00500 196 ARG A CD  
1614 N NE  . ARG A 210 ? 0.29952 0.29736 0.30644 -0.01385 -0.00720 -0.00625 196 ARG A NE  
1615 C CZ  . ARG A 210 ? 0.33651 0.33293 0.34623 -0.01449 -0.00766 -0.00680 196 ARG A CZ  
1616 N NH1 . ARG A 210 ? 0.38870 0.38554 0.40170 -0.01548 -0.00767 -0.00608 196 ARG A NH1 
1617 N NH2 . ARG A 210 ? 0.41483 0.40945 0.42425 -0.01411 -0.00816 -0.00810 196 ARG A NH2 
1618 N N   . TYR A 211 ? 0.09040 0.09180 0.09617 -0.01282 -0.00249 -0.00026 197 TYR A N   
1619 C CA  . TYR A 211 ? 0.08916 0.09202 0.09586 -0.01293 -0.00249 0.00051  197 TYR A CA  
1620 C C   . TYR A 211 ? 0.08587 0.08946 0.09082 -0.01220 -0.00209 0.00132  197 TYR A C   
1621 O O   . TYR A 211 ? 0.08903 0.09377 0.09432 -0.01213 -0.00249 0.00171  197 TYR A O   
1622 C CB  . TYR A 211 ? 0.09645 0.09942 0.10570 -0.01332 -0.00161 0.00120  197 TYR A CB  
1623 C CG  . TYR A 211 ? 0.11759 0.11969 0.12907 -0.01418 -0.00197 0.00058  197 TYR A CG  
1624 C CD1 . TYR A 211 ? 0.11133 0.11354 0.12338 -0.01466 -0.00344 -0.00061 197 TYR A CD1 
1625 C CD2 . TYR A 211 ? 0.12326 0.12435 0.13633 -0.01452 -0.00098 0.00124  197 TYR A CD2 
1626 C CE1 . TYR A 211 ? 0.14930 0.15063 0.16369 -0.01546 -0.00401 -0.00131 197 TYR A CE1 
1627 C CE2 . TYR A 211 ? 0.19522 0.19540 0.21076 -0.01543 -0.00147 0.00073  197 TYR A CE2 
1628 C CZ  . TYR A 211 ? 0.17842 0.17872 0.19471 -0.01589 -0.00304 -0.00063 197 TYR A CZ  
1629 O OH  . TYR A 211 ? 0.24148 0.24078 0.26046 -0.01680 -0.00377 -0.00128 197 TYR A OH  
1630 N N   . PHE A 212 ? 0.07634 0.07926 0.07965 -0.01162 -0.00144 0.00151  198 PHE A N   
1631 C CA  . PHE A 212 ? 0.05875 0.06225 0.06077 -0.01093 -0.00108 0.00229  198 PHE A CA  
1632 C C   . PHE A 212 ? 0.06701 0.07091 0.06706 -0.01069 -0.00150 0.00207  198 PHE A C   
1633 O O   . PHE A 212 ? 0.09894 0.10336 0.09814 -0.01021 -0.00129 0.00272  198 PHE A O   
1634 C CB  . PHE A 212 ? 0.12153 0.12423 0.12365 -0.01040 0.00010  0.00295  198 PHE A CB  
1635 C CG  . PHE A 212 ? 0.09087 0.09359 0.09478 -0.01067 0.00067  0.00344  198 PHE A CG  
1636 C CD1 . PHE A 212 ? 0.11711 0.11888 0.12252 -0.01129 0.00095  0.00324  198 PHE A CD1 
1637 C CD2 . PHE A 212 ? 0.10699 0.11086 0.11130 -0.01033 0.00083  0.00404  198 PHE A CD2 
1638 C CE1 . PHE A 212 ? 0.15763 0.15980 0.16498 -0.01169 0.00160  0.00389  198 PHE A CE1 
1639 C CE2 . PHE A 212 ? 0.11873 0.12311 0.12471 -0.01053 0.00151  0.00448  198 PHE A CE2 
1640 C CZ  . PHE A 212 ? 0.13043 0.13408 0.13798 -0.01128 0.00198  0.00451  198 PHE A CZ  
1641 N N   . LYS A 213 ? 0.10939 0.11321 0.10876 -0.01100 -0.00212 0.00117  199 LYS A N   
1642 C CA  . LYS A 213 ? 0.08448 0.08907 0.08183 -0.01078 -0.00240 0.00103  199 LYS A CA  
1643 C C   . LYS A 213 ? 0.07826 0.08408 0.07524 -0.01104 -0.00319 0.00185  199 LYS A C   
1644 O O   . LYS A 213 ? 0.10960 0.11562 0.10739 -0.01152 -0.00411 0.00179  199 LYS A O   
1645 C CB  . LYS A 213 ? 0.07546 0.07976 0.07196 -0.01093 -0.00298 -0.00025 199 LYS A CB  
1646 C CG  . LYS A 213 ? 0.10074 0.10378 0.09728 -0.01050 -0.00241 -0.00121 199 LYS A CG  
1647 C CD  . LYS A 213 ? 0.15303 0.15573 0.14881 -0.01057 -0.00328 -0.00272 199 LYS A CD  
1648 C CE  . LYS A 213 ? 0.16213 0.16308 0.15867 -0.01024 -0.00309 -0.00386 199 LYS A CE  
1649 N NZ  . LYS A 213 ? 0.23450 0.23556 0.22945 -0.00925 -0.00240 -0.00438 199 LYS A NZ  
1650 N N   . GLY A 214 ? 0.07920 0.08581 0.07515 -0.01075 -0.00293 0.00263  200 GLY A N   
1651 C CA  . GLY A 214 ? 0.12463 0.13223 0.12028 -0.01108 -0.00381 0.00354  200 GLY A CA  
1652 C C   . GLY A 214 ? 0.11741 0.12564 0.11157 -0.01150 -0.00459 0.00330  200 GLY A C   
1653 O O   . GLY A 214 ? 0.09647 0.10472 0.08935 -0.01132 -0.00424 0.00241  200 GLY A O   
1654 N N   . PRO A 215 ? 0.07701 0.08570 0.07122 -0.01196 -0.00578 0.00401  201 PRO A N   
1655 C CA  . PRO A 215 ? 0.13820 0.14751 0.13065 -0.01234 -0.00664 0.00398  201 PRO A CA  
1656 C C   . PRO A 215 ? 0.13456 0.14501 0.12478 -0.01217 -0.00588 0.00425  201 PRO A C   
1657 O O   . PRO A 215 ? 0.14699 0.15782 0.13535 -0.01214 -0.00613 0.00356  201 PRO A O   
1658 C CB  . PRO A 215 ? 0.11693 0.12645 0.11001 -0.01281 -0.00804 0.00510  201 PRO A CB  
1659 C CG  . PRO A 215 ? 0.19257 0.20176 0.18756 -0.01257 -0.00781 0.00567  201 PRO A CG  
1660 C CD  . PRO A 215 ? 0.09944 0.10801 0.09527 -0.01206 -0.00652 0.00476  201 PRO A CD  
1661 N N   . GLU A 216 ? 0.10451 0.11564 0.09487 -0.01197 -0.00498 0.00516  202 GLU A N   
1662 C CA  . GLU A 216 ? 0.13362 0.14621 0.12223 -0.01172 -0.00401 0.00534  202 GLU A CA  
1663 C C   . GLU A 216 ? 0.15784 0.17015 0.14538 -0.01104 -0.00326 0.00356  202 GLU A C   
1664 O O   . GLU A 216 ? 0.10207 0.11552 0.08747 -0.01081 -0.00303 0.00312  202 GLU A O   
1665 C CB  . GLU A 216 ? 0.09820 0.11153 0.08785 -0.01158 -0.00322 0.00644  202 GLU A CB  
1666 C CG  . GLU A 216 ? 0.11351 0.12569 0.10479 -0.01097 -0.00253 0.00580  202 GLU A CG  
1667 C CD  . GLU A 216 ? 0.16477 0.17589 0.15794 -0.01113 -0.00330 0.00635  202 GLU A CD  
1668 O OE1 . GLU A 216 ? 0.12658 0.13707 0.12012 -0.01151 -0.00432 0.00625  202 GLU A OE1 
1669 O OE2 . GLU A 216 ? 0.13152 0.14253 0.12580 -0.01077 -0.00296 0.00677  202 GLU A OE2 
1670 N N   . LEU A 217 ? 0.10420 0.11497 0.09318 -0.01067 -0.00294 0.00251  203 LEU A N   
1671 C CA  . LEU A 217 ? 0.13294 0.14304 0.12126 -0.01006 -0.00254 0.00077  203 LEU A CA  
1672 C C   . LEU A 217 ? 0.11412 0.12385 0.10139 -0.01029 -0.00365 -0.00030 203 LEU A C   
1673 O O   . LEU A 217 ? 0.12206 0.13208 0.10763 -0.00976 -0.00360 -0.00160 203 LEU A O   
1674 C CB  . LEU A 217 ? 0.09957 0.10788 0.08987 -0.00979 -0.00211 0.00019  203 LEU A CB  
1675 C CG  . LEU A 217 ? 0.14395 0.15228 0.13533 -0.00944 -0.00121 0.00110  203 LEU A CG  
1676 C CD1 . LEU A 217 ? 0.14194 0.14839 0.13484 -0.00916 -0.00085 0.00054  203 LEU A CD1 
1677 C CD2 . LEU A 217 ? 0.10253 0.11229 0.09281 -0.00880 -0.00030 0.00115  203 LEU A CD2 
1678 N N   . LEU A 218 ? 0.09534 0.10447 0.08367 -0.01098 -0.00478 0.00009  204 LEU A N   
1679 C CA  . LEU A 218 ? 0.11062 0.11923 0.09847 -0.01120 -0.00604 -0.00103 204 LEU A CA  
1680 C C   . LEU A 218 ? 0.14474 0.15473 0.12969 -0.01117 -0.00666 -0.00086 204 LEU A C   
1681 O O   . LEU A 218 ? 0.13928 0.14899 0.12301 -0.01101 -0.00759 -0.00220 204 LEU A O   
1682 C CB  . LEU A 218 ? 0.12804 0.13587 0.11821 -0.01186 -0.00703 -0.00066 204 LEU A CB  
1683 C CG  . LEU A 218 ? 0.11641 0.12310 0.10925 -0.01185 -0.00628 -0.00077 204 LEU A CG  
1684 C CD1 . LEU A 218 ? 0.08532 0.09187 0.08038 -0.01237 -0.00699 -0.00020 204 LEU A CD1 
1685 C CD2 . LEU A 218 ? 0.11475 0.12017 0.10822 -0.01165 -0.00617 -0.00237 204 LEU A CD2 
1686 N N   . VAL A 219 ? 0.15128 0.16278 0.13510 -0.01133 -0.00619 0.00078  205 VAL A N   
1687 C CA  . VAL A 219 ? 0.08626 0.09936 0.06711 -0.01134 -0.00651 0.00136  205 VAL A CA  
1688 C C   . VAL A 219 ? 0.14119 0.15598 0.12013 -0.01062 -0.00500 0.00115  205 VAL A C   
1689 O O   . VAL A 219 ? 0.14780 0.16446 0.12426 -0.01063 -0.00481 0.00202  205 VAL A O   
1690 C CB  . VAL A 219 ? 0.11107 0.12480 0.09205 -0.01218 -0.00727 0.00357  205 VAL A CB  
1691 C CG1 . VAL A 219 ? 0.12994 0.14220 0.11274 -0.01267 -0.00887 0.00345  205 VAL A CG1 
1692 C CG2 . VAL A 219 ? 0.10367 0.11805 0.08614 -0.01238 -0.00622 0.00515  205 VAL A CG2 
1693 N N   . ASP A 220 ? 0.11936 0.13363 0.09945 -0.00997 -0.00389 0.00010  206 ASP A N   
1694 C CA  . ASP A 220 ? 0.13564 0.15147 0.11421 -0.00905 -0.00252 -0.00055 206 ASP A CA  
1695 C C   . ASP A 220 ? 0.14905 0.16717 0.12740 -0.00931 -0.00142 0.00148  206 ASP A C   
1696 O O   . ASP A 220 ? 0.16693 0.18733 0.14323 -0.00881 -0.00049 0.00154  206 ASP A O   
1697 C CB  . ASP A 220 ? 0.17033 0.18685 0.14593 -0.00829 -0.00286 -0.00225 206 ASP A CB  
1698 C CG  . ASP A 220 ? 0.20631 0.22069 0.18266 -0.00763 -0.00348 -0.00475 206 ASP A CG  
1699 O OD1 . ASP A 220 ? 0.32991 0.34398 0.30691 -0.00677 -0.00257 -0.00590 206 ASP A OD1 
1700 O OD2 . ASP A 220 ? 0.30236 0.31530 0.27893 -0.00800 -0.00496 -0.00552 206 ASP A OD2 
1701 N N   . TYR A 221 ? 0.11602 0.13365 0.09659 -0.01005 -0.00155 0.00311  207 TYR A N   
1702 C CA  . TYR A 221 ? 0.09803 0.11755 0.07915 -0.01041 -0.00071 0.00504  207 TYR A CA  
1703 C C   . TYR A 221 ? 0.12149 0.14098 0.10436 -0.00971 0.00048  0.00452  207 TYR A C   
1704 O O   . TYR A 221 ? 0.08919 0.10682 0.07417 -0.00971 0.00021  0.00432  207 TYR A O   
1705 C CB  . TYR A 221 ? 0.08155 0.10041 0.06419 -0.01149 -0.00180 0.00695  207 TYR A CB  
1706 C CG  . TYR A 221 ? 0.12189 0.14257 0.10539 -0.01200 -0.00120 0.00903  207 TYR A CG  
1707 C CD1 . TYR A 221 ? 0.20139 0.22456 0.18306 -0.01234 -0.00066 0.01033  207 TYR A CD1 
1708 C CD2 . TYR A 221 ? 0.19100 0.21100 0.17721 -0.01214 -0.00119 0.00970  207 TYR A CD2 
1709 C CE1 . TYR A 221 ? 0.20902 0.23399 0.19191 -0.01297 -0.00012 0.01239  207 TYR A CE1 
1710 C CE2 . TYR A 221 ? 0.19608 0.21771 0.18345 -0.01267 -0.00084 0.01155  207 TYR A CE2 
1711 C CZ  . TYR A 221 ? 0.22246 0.24657 0.20834 -0.01316 -0.00029 0.01294  207 TYR A CZ  
1712 O OH  . TYR A 221 ? 0.32452 0.35042 0.31191 -0.01384 0.00007  0.01495  207 TYR A OH  
1713 N N   . GLN A 222 ? 0.13607 0.15779 0.11803 -0.00906 0.00180  0.00433  208 GLN A N   
1714 C CA  . GLN A 222 ? 0.11725 0.13900 0.10060 -0.00812 0.00285  0.00341  208 GLN A CA  
1715 C C   . GLN A 222 ? 0.15288 0.17556 0.13847 -0.00847 0.00334  0.00505  208 GLN A C   
1716 O O   . GLN A 222 ? 0.13055 0.15277 0.11764 -0.00774 0.00390  0.00439  208 GLN A O   
1717 C CB  . GLN A 222 ? 0.09035 0.11418 0.07183 -0.00701 0.00400  0.00206  208 GLN A CB  
1718 C CG  . GLN A 222 ? 0.13862 0.16126 0.11803 -0.00641 0.00334  -0.00001 208 GLN A CG  
1719 C CD  . GLN A 222 ? 0.24028 0.26457 0.21807 -0.00497 0.00433  -0.00186 208 GLN A CD  
1720 O OE1 . GLN A 222 ? 0.21897 0.24515 0.19403 -0.00463 0.00452  -0.00226 208 GLN A OE1 
1721 N NE2 . GLN A 222 ? 0.21913 0.24272 0.19848 -0.00399 0.00491  -0.00307 208 GLN A NE2 
1722 N N   . MET A 223 ? 0.13852 0.16237 0.12448 -0.00955 0.00297  0.00715  209 MET A N   
1723 C CA  . MET A 223 ? 0.11389 0.13875 0.10221 -0.00990 0.00327  0.00866  209 MET A CA  
1724 C C   . MET A 223 ? 0.12344 0.14582 0.11382 -0.01034 0.00204  0.00914  209 MET A C   
1725 O O   . MET A 223 ? 0.13571 0.15828 0.12739 -0.01122 0.00128  0.01082  209 MET A O   
1726 C CB  . MET A 223 ? 0.12421 0.15187 0.11216 -0.01084 0.00359  0.01078  209 MET A CB  
1727 C CG  . MET A 223 ? 0.16614 0.19583 0.15650 -0.01098 0.00435  0.01202  209 MET A CG  
1728 S SD  . MET A 223 ? 0.27094 0.30449 0.26091 -0.01211 0.00510  0.01460  209 MET A SD  
1729 C CE  . MET A 223 ? 0.21915 0.25516 0.20567 -0.01096 0.00676  0.01301  209 MET A CE  
1730 N N   . TYR A 224 ? 0.09955 0.11959 0.09025 -0.00967 0.00183  0.00762  210 TYR A N   
1731 C CA  . TYR A 224 ? 0.08768 0.10548 0.07997 -0.00985 0.00084  0.00782  210 TYR A CA  
1732 C C   . TYR A 224 ? 0.10104 0.11871 0.09521 -0.00926 0.00120  0.00792  210 TYR A C   
1733 O O   . TYR A 224 ? 0.10833 0.12760 0.10279 -0.00874 0.00216  0.00780  210 TYR A O   
1734 C CB  . TYR A 224 ? 0.05055 0.06612 0.04220 -0.00962 0.00040  0.00643  210 TYR A CB  
1735 C CG  . TYR A 224 ? 0.10644 0.12117 0.09771 -0.00863 0.00122  0.00473  210 TYR A CG  
1736 C CD1 . TYR A 224 ? 0.07630 0.08978 0.06888 -0.00796 0.00154  0.00438  210 TYR A CD1 
1737 C CD2 . TYR A 224 ? 0.07592 0.09093 0.06546 -0.00830 0.00152  0.00345  210 TYR A CD2 
1738 C CE1 . TYR A 224 ? 0.09398 0.10641 0.08635 -0.00709 0.00212  0.00295  210 TYR A CE1 
1739 C CE2 . TYR A 224 ? 0.07618 0.09011 0.06562 -0.00737 0.00202  0.00180  210 TYR A CE2 
1740 C CZ  . TYR A 224 ? 0.08821 0.10079 0.07916 -0.00682 0.00231  0.00166  210 TYR A CZ  
1741 O OH  . TYR A 224 ? 0.09576 0.10703 0.08676 -0.00593 0.00266  0.00020  210 TYR A OH  
1742 N N   . ASP A 225 ? 0.08610 0.10200 0.08152 -0.00923 0.00038  0.00807  211 ASP A N   
1743 C CA  . ASP A 225 ? 0.06889 0.08456 0.06595 -0.00865 0.00041  0.00825  211 ASP A CA  
1744 C C   . ASP A 225 ? 0.10023 0.11354 0.09766 -0.00819 -0.00013 0.00768  211 ASP A C   
1745 O O   . ASP A 225 ? 0.08495 0.09696 0.08155 -0.00823 -0.00018 0.00697  211 ASP A O   
1746 C CB  . ASP A 225 ? 0.10510 0.12223 0.10371 -0.00931 -0.00021 0.00982  211 ASP A CB  
1747 C CG  . ASP A 225 ? 0.09274 0.10909 0.09168 -0.01020 -0.00162 0.01074  211 ASP A CG  
1748 O OD1 . ASP A 225 ? 0.12401 0.13856 0.12345 -0.00990 -0.00246 0.01035  211 ASP A OD1 
1749 O OD2 . ASP A 225 ? 0.12900 0.14659 0.12767 -0.01114 -0.00191 0.01187  211 ASP A OD2 
1750 N N   . TYR A 226 ? 0.11183 0.12474 0.11055 -0.00772 -0.00053 0.00800  212 TYR A N   
1751 C CA  . TYR A 226 ? 0.09208 0.10308 0.09098 -0.00712 -0.00094 0.00758  212 TYR A CA  
1752 C C   . TYR A 226 ? 0.09609 0.10619 0.09476 -0.00763 -0.00170 0.00761  212 TYR A C   
1753 O O   . TYR A 226 ? 0.09122 0.09997 0.08963 -0.00722 -0.00161 0.00707  212 TYR A O   
1754 C CB  . TYR A 226 ? 0.03242 0.04345 0.03267 -0.00666 -0.00171 0.00808  212 TYR A CB  
1755 C CG  . TYR A 226 ? 0.08899 0.10135 0.09015 -0.00626 -0.00128 0.00826  212 TYR A CG  
1756 C CD1 . TYR A 226 ? 0.06451 0.07646 0.06528 -0.00530 -0.00041 0.00750  212 TYR A CD1 
1757 C CD2 . TYR A 226 ? 0.08168 0.09567 0.08437 -0.00685 -0.00187 0.00924  212 TYR A CD2 
1758 C CE1 . TYR A 226 ? 0.05584 0.06917 0.05771 -0.00483 -0.00009 0.00756  212 TYR A CE1 
1759 C CE2 . TYR A 226 ? 0.06352 0.07905 0.06749 -0.00652 -0.00146 0.00943  212 TYR A CE2 
1760 C CZ  . TYR A 226 ? 0.09743 0.11269 0.10098 -0.00545 -0.00057 0.00851  212 TYR A CZ  
1761 O OH  . TYR A 226 ? 0.08295 0.09992 0.08803 -0.00503 -0.00025 0.00861  212 TYR A OH  
1762 N N   . SER A 227 ? 0.05783 0.06875 0.05671 -0.00853 -0.00248 0.00833  213 SER A N   
1763 C CA  . SER A 227 ? 0.08948 0.09963 0.08840 -0.00894 -0.00340 0.00832  213 SER A CA  
1764 C C   . SER A 227 ? 0.09325 0.10271 0.09116 -0.00903 -0.00284 0.00744  213 SER A C   
1765 O O   . SER A 227 ? 0.06348 0.07226 0.06169 -0.00916 -0.00344 0.00720  213 SER A O   
1766 C CB  . SER A 227 ? 0.11219 0.12323 0.11153 -0.00988 -0.00446 0.00940  213 SER A CB  
1767 O OG  . SER A 227 ? 0.12104 0.13337 0.11929 -0.01045 -0.00378 0.00972  213 SER A OG  
1768 N N   . LEU A 228 ? 0.09367 0.10331 0.09063 -0.00889 -0.00180 0.00685  214 LEU A N   
1769 C CA  . LEU A 228 ? 0.07012 0.07882 0.06650 -0.00892 -0.00142 0.00590  214 LEU A CA  
1770 C C   . LEU A 228 ? 0.07743 0.08477 0.07450 -0.00842 -0.00120 0.00557  214 LEU A C   
1771 O O   . LEU A 228 ? 0.08544 0.09216 0.08283 -0.00869 -0.00138 0.00520  214 LEU A O   
1772 C CB  . LEU A 228 ? 0.09969 0.10865 0.09508 -0.00864 -0.00048 0.00516  214 LEU A CB  
1773 C CG  . LEU A 228 ? 0.16597 0.17356 0.16114 -0.00850 -0.00012 0.00406  214 LEU A CG  
1774 C CD1 . LEU A 228 ? 0.17853 0.18603 0.17350 -0.00925 -0.00087 0.00373  214 LEU A CD1 
1775 C CD2 . LEU A 228 ? 0.06549 0.07314 0.05989 -0.00793 0.00067  0.00318  214 LEU A CD2 
1776 N N   . ASP A 229 ? 0.06041 0.06742 0.05775 -0.00767 -0.00084 0.00578  215 ASP A N   
1777 C CA  . ASP A 229 ? 0.08990 0.09579 0.08756 -0.00709 -0.00053 0.00567  215 ASP A CA  
1778 C C   . ASP A 229 ? 0.08146 0.08745 0.07978 -0.00715 -0.00131 0.00589  215 ASP A C   
1779 O O   . ASP A 229 ? 0.08677 0.09221 0.08535 -0.00695 -0.00097 0.00572  215 ASP A O   
1780 C CB  . ASP A 229 ? 0.05539 0.06096 0.05294 -0.00616 -0.00019 0.00589  215 ASP A CB  
1781 C CG  . ASP A 229 ? 0.09907 0.10432 0.09616 -0.00584 0.00063  0.00548  215 ASP A CG  
1782 O OD1 . ASP A 229 ? 0.10346 0.10817 0.10025 -0.00615 0.00108  0.00490  215 ASP A OD1 
1783 O OD2 . ASP A 229 ? 0.09777 0.10324 0.09495 -0.00517 0.00071  0.00565  215 ASP A OD2 
1784 N N   . MET A 230 ? 0.08184 0.08859 0.08058 -0.00741 -0.00237 0.00630  216 MET A N   
1785 C CA  . MET A 230 ? 0.09889 0.10569 0.09840 -0.00729 -0.00334 0.00633  216 MET A CA  
1786 C C   . MET A 230 ? 0.08034 0.08725 0.08022 -0.00795 -0.00363 0.00601  216 MET A C   
1787 O O   . MET A 230 ? 0.09028 0.09719 0.09088 -0.00766 -0.00393 0.00572  216 MET A O   
1788 C CB  . MET A 230 ? 0.08129 0.08857 0.08144 -0.00734 -0.00464 0.00689  216 MET A CB  
1789 C CG  . MET A 230 ? 0.08698 0.09425 0.08719 -0.00667 -0.00459 0.00713  216 MET A CG  
1790 S SD  . MET A 230 ? 0.12321 0.12964 0.12299 -0.00531 -0.00412 0.00662  216 MET A SD  
1791 C CE  . MET A 230 ? 0.08486 0.09133 0.08545 -0.00497 -0.00547 0.00627  216 MET A CE  
1792 N N   . TRP A 231 ? 0.06547 0.07260 0.06485 -0.00873 -0.00355 0.00594  217 TRP A N   
1793 C CA  . TRP A 231 ? 0.07507 0.08220 0.07483 -0.00929 -0.00384 0.00547  217 TRP A CA  
1794 C C   . TRP A 231 ? 0.08108 0.08764 0.08131 -0.00908 -0.00283 0.00495  217 TRP A C   
1795 O O   . TRP A 231 ? 0.08550 0.09225 0.08683 -0.00914 -0.00304 0.00468  217 TRP A O   
1796 C CB  . TRP A 231 ? 0.08540 0.09282 0.08420 -0.01001 -0.00398 0.00537  217 TRP A CB  
1797 C CG  . TRP A 231 ? 0.10906 0.11634 0.10833 -0.01051 -0.00439 0.00471  217 TRP A CG  
1798 C CD1 . TRP A 231 ? 0.09626 0.10297 0.09586 -0.01062 -0.00372 0.00395  217 TRP A CD1 
1799 C CD2 . TRP A 231 ? 0.07580 0.08346 0.07559 -0.01097 -0.00574 0.00478  217 TRP A CD2 
1800 N NE1 . TRP A 231 ? 0.06342 0.07028 0.06383 -0.01114 -0.00455 0.00348  217 TRP A NE1 
1801 C CE2 . TRP A 231 ? 0.06629 0.07374 0.06674 -0.01130 -0.00579 0.00395  217 TRP A CE2 
1802 C CE3 . TRP A 231 ? 0.12879 0.13683 0.12872 -0.01113 -0.00705 0.00549  217 TRP A CE3 
1803 C CZ2 . TRP A 231 ? 0.11786 0.12562 0.11903 -0.01172 -0.00711 0.00373  217 TRP A CZ2 
1804 C CZ3 . TRP A 231 ? 0.11373 0.12189 0.11424 -0.01153 -0.00837 0.00535  217 TRP A CZ3 
1805 C CH2 . TRP A 231 ? 0.10675 0.11483 0.10784 -0.01177 -0.00838 0.00442  217 TRP A CH2 
1806 N N   . SER A 232 ? 0.08709 0.09301 0.08669 -0.00883 -0.00176 0.00485  218 SER A N   
1807 C CA  . SER A 232 ? 0.09971 0.10492 0.09987 -0.00874 -0.00081 0.00463  218 SER A CA  
1808 C C   . SER A 232 ? 0.11725 0.12267 0.11800 -0.00811 -0.00053 0.00498  218 SER A C   
1809 O O   . SER A 232 ? 0.09481 0.10037 0.09659 -0.00828 -0.00009 0.00491  218 SER A O   
1810 C CB  . SER A 232 ? 0.10279 0.10705 0.10215 -0.00843 0.00008  0.00458  218 SER A CB  
1811 O OG  . SER A 232 ? 0.07489 0.07919 0.07350 -0.00875 -0.00011 0.00409  218 SER A OG  
1812 N N   . LEU A 233 ? 0.06050 0.06608 0.06067 -0.00735 -0.00080 0.00532  219 LEU A N   
1813 C CA  . LEU A 233 ? 0.09354 0.09944 0.09395 -0.00653 -0.00067 0.00545  219 LEU A CA  
1814 C C   . LEU A 233 ? 0.10107 0.10793 0.10269 -0.00668 -0.00144 0.00510  219 LEU A C   
1815 O O   . LEU A 233 ? 0.09810 0.10552 0.10036 -0.00631 -0.00088 0.00502  219 LEU A O   
1816 C CB  . LEU A 233 ? 0.10994 0.11574 0.10955 -0.00562 -0.00114 0.00568  219 LEU A CB  
1817 C CG  . LEU A 233 ? 0.15270 0.15881 0.15215 -0.00452 -0.00108 0.00563  219 LEU A CG  
1818 C CD1 . LEU A 233 ? 0.21892 0.22443 0.21717 -0.00352 -0.00089 0.00590  219 LEU A CD1 
1819 C CD2 . LEU A 233 ? 0.13397 0.14084 0.13425 -0.00425 -0.00250 0.00520  219 LEU A CD2 
1820 N N   . GLY A 234 ? 0.10129 0.10844 0.10327 -0.00719 -0.00271 0.00495  220 GLY A N   
1821 C CA  . GLY A 234 ? 0.08008 0.08800 0.08335 -0.00732 -0.00365 0.00456  220 GLY A CA  
1822 C C   . GLY A 234 ? 0.11031 0.11863 0.11472 -0.00790 -0.00302 0.00423  220 GLY A C   
1823 O O   . GLY A 234 ? 0.09742 0.10668 0.10316 -0.00762 -0.00309 0.00389  220 GLY A O   
1824 N N   . CYS A 235 ? 0.04126 0.04896 0.04535 -0.00867 -0.00245 0.00424  221 CYS A N   
1825 C CA  . CYS A 235 ? 0.12450 0.13239 0.12996 -0.00931 -0.00191 0.00394  221 CYS A CA  
1826 C C   . CYS A 235 ? 0.12668 0.13501 0.13293 -0.00887 -0.00056 0.00424  221 CYS A C   
1827 O O   . CYS A 235 ? 0.11618 0.12553 0.12426 -0.00912 -0.00031 0.00406  221 CYS A O   
1828 C CB  . CYS A 235 ? 0.08073 0.08758 0.08553 -0.00999 -0.00160 0.00379  221 CYS A CB  
1829 S SG  . CYS A 235 ? 0.09966 0.10648 0.10364 -0.01063 -0.00306 0.00335  221 CYS A SG  
1830 N N   . MET A 236 ? 0.08409 0.09179 0.08902 -0.00822 0.00034  0.00478  222 MET A N   
1831 C CA  . MET A 236 ? 0.11235 0.12048 0.11757 -0.00773 0.00169  0.00530  222 MET A CA  
1832 C C   . MET A 236 ? 0.10798 0.11769 0.11372 -0.00684 0.00150  0.00507  222 MET A C   
1833 O O   . MET A 236 ? 0.09469 0.10566 0.10170 -0.00678 0.00243  0.00522  222 MET A O   
1834 C CB  . MET A 236 ? 0.07889 0.08584 0.08230 -0.00712 0.00245  0.00593  222 MET A CB  
1835 C CG  . MET A 236 ? 0.08959 0.09498 0.09273 -0.00783 0.00281  0.00608  222 MET A CG  
1836 S SD  . MET A 236 ? 0.17571 0.17963 0.17696 -0.00699 0.00358  0.00680  222 MET A SD  
1837 C CE  . MET A 236 ? 0.07582 0.08038 0.07713 -0.00643 0.00491  0.00779  222 MET A CE  
1838 N N   . LEU A 237 ? 0.08319 0.09294 0.08812 -0.00611 0.00029  0.00468  223 LEU A N   
1839 C CA  . LEU A 237 ? 0.08971 0.10081 0.09518 -0.00508 -0.00021 0.00417  223 LEU A CA  
1840 C C   . LEU A 237 ? 0.10265 0.11512 0.11039 -0.00555 -0.00055 0.00362  223 LEU A C   
1841 O O   . LEU A 237 ? 0.07679 0.09090 0.08556 -0.00491 0.00010  0.00338  223 LEU A O   
1842 C CB  . LEU A 237 ? 0.07599 0.08654 0.08067 -0.00447 -0.00187 0.00381  223 LEU A CB  
1843 C CG  . LEU A 237 ? 0.06780 0.07945 0.07316 -0.00328 -0.00284 0.00301  223 LEU A CG  
1844 C CD1 . LEU A 237 ? 0.06869 0.08120 0.07312 -0.00192 -0.00166 0.00296  223 LEU A CD1 
1845 C CD2 . LEU A 237 ? 0.09049 0.10125 0.09556 -0.00302 -0.00480 0.00276  223 LEU A CD2 
1846 N N   . ALA A 238 ? 0.10110 0.11309 0.10964 -0.00661 -0.00159 0.00339  224 ALA A N   
1847 C CA  . ALA A 238 ? 0.08159 0.09478 0.09241 -0.00708 -0.00213 0.00282  224 ALA A CA  
1848 C C   . ALA A 238 ? 0.09230 0.10660 0.10476 -0.00754 -0.00051 0.00308  224 ALA A C   
1849 O O   . ALA A 238 ? 0.07259 0.08875 0.08704 -0.00724 -0.00031 0.00268  224 ALA A O   
1850 C CB  . ALA A 238 ? 0.09778 0.11007 0.10873 -0.00815 -0.00348 0.00264  224 ALA A CB  
1851 N N   . SER A 239 ? 0.07779 0.09102 0.08964 -0.00824 0.00064  0.00378  225 SER A N   
1852 C CA  . SER A 239 ? 0.05210 0.06617 0.06579 -0.00889 0.00210  0.00426  225 SER A CA  
1853 C C   . SER A 239 ? 0.11308 0.12882 0.12681 -0.00789 0.00359  0.00476  225 SER A C   
1854 O O   . SER A 239 ? 0.09901 0.11659 0.11499 -0.00819 0.00459  0.00497  225 SER A O   
1855 C CB  . SER A 239 ? 0.09890 0.11108 0.11187 -0.00976 0.00277  0.00490  225 SER A CB  
1856 O OG  . SER A 239 ? 0.14686 0.15811 0.15759 -0.00902 0.00369  0.00566  225 SER A OG  
1857 N N   . MET A 240 ? 0.07954 0.09486 0.09086 -0.00667 0.00373  0.00492  226 MET A N   
1858 C CA  . MET A 240 ? 0.14988 0.16685 0.16075 -0.00553 0.00512  0.00533  226 MET A CA  
1859 C C   . MET A 240 ? 0.12053 0.13984 0.13273 -0.00452 0.00458  0.00429  226 MET A C   
1860 O O   . MET A 240 ? 0.09114 0.11279 0.10472 -0.00419 0.00592  0.00447  226 MET A O   
1861 C CB  . MET A 240 ? 0.10755 0.12323 0.11532 -0.00444 0.00530  0.00575  226 MET A CB  
1862 C CG  . MET A 240 ? 0.13123 0.14497 0.13782 -0.00516 0.00620  0.00690  226 MET A CG  
1863 S SD  . MET A 240 ? 0.23643 0.24854 0.23964 -0.00383 0.00579  0.00707  226 MET A SD  
1864 C CE  . MET A 240 ? 0.42990 0.44381 0.43174 -0.00220 0.00707  0.00747  226 MET A CE  
1865 N N   . ILE A 241 ? 0.07091 0.08970 0.08285 -0.00399 0.00263  0.00322  227 ILE A N   
1866 C CA  . ILE A 241 ? 0.09515 0.11593 0.10836 -0.00281 0.00188  0.00207  227 ILE A CA  
1867 C C   . ILE A 241 ? 0.07798 0.10042 0.09450 -0.00362 0.00169  0.00161  227 ILE A C   
1868 O O   . ILE A 241 ? 0.09372 0.11860 0.11190 -0.00268 0.00190  0.00086  227 ILE A O   
1869 C CB  . ILE A 241 ? 0.06910 0.08875 0.08124 -0.00185 -0.00031 0.00112  227 ILE A CB  
1870 C CG1 . ILE A 241 ? 0.07956 0.09769 0.09248 -0.00307 -0.00212 0.00098  227 ILE A CG1 
1871 C CG2 . ILE A 241 ? 0.09241 0.11063 0.10169 -0.00099 -0.00026 0.00147  227 ILE A CG2 
1872 C CD1 . ILE A 241 ? 0.06578 0.08270 0.07799 -0.00240 -0.00437 0.00037  227 ILE A CD1 
1873 N N   . PHE A 242 ? 0.05623 0.07751 0.07380 -0.00522 0.00118  0.00189  228 PHE A N   
1874 C CA  . PHE A 242 ? 0.10613 0.12883 0.12693 -0.00603 0.00070  0.00137  228 PHE A CA  
1875 C C   . PHE A 242 ? 0.09882 0.12265 0.12166 -0.00717 0.00253  0.00221  228 PHE A C   
1876 O O   . PHE A 242 ? 0.09731 0.12303 0.12337 -0.00766 0.00248  0.00180  228 PHE A O   
1877 C CB  . PHE A 242 ? 0.06663 0.08748 0.08748 -0.00699 -0.00137 0.00096  228 PHE A CB  
1878 C CG  . PHE A 242 ? 0.07258 0.09255 0.09226 -0.00611 -0.00343 0.00026  228 PHE A CG  
1879 C CD1 . PHE A 242 ? 0.09555 0.11706 0.11626 -0.00472 -0.00414 -0.00067 228 PHE A CD1 
1880 C CD2 . PHE A 242 ? 0.09088 0.10854 0.10856 -0.00665 -0.00466 0.00056  228 PHE A CD2 
1881 C CE1 . PHE A 242 ? 0.10856 0.12894 0.12846 -0.00400 -0.00625 -0.00123 228 PHE A CE1 
1882 C CE2 . PHE A 242 ? 0.09022 0.10704 0.10710 -0.00605 -0.00655 0.00021  228 PHE A CE2 
1883 C CZ  . PHE A 242 ? 0.09277 0.11077 0.11082 -0.00476 -0.00744 -0.00066 228 PHE A CZ  
1884 N N   . ARG A 243 ? 0.14001 0.14540 0.15017 -0.00368 0.00563  -0.00827 229 ARG A N   
1885 C CA  . ARG A 243 ? 0.12108 0.12918 0.13439 -0.00645 0.00776  -0.01403 229 ARG A CA  
1886 C C   . ARG A 243 ? 0.18930 0.20012 0.19845 -0.00649 0.00667  -0.01438 229 ARG A C   
1887 O O   . ARG A 243 ? 0.24858 0.26299 0.26018 -0.00779 0.00772  -0.01760 229 ARG A O   
1888 C CB  . ARG A 243 ? 0.15719 0.16503 0.17570 -0.00637 0.00886  -0.01586 229 ARG A CB  
1889 C CG  . ARG A 243 ? 0.18523 0.18693 0.19878 -0.00453 0.00664  -0.01110 229 ARG A CG  
1890 C CD  . ARG A 243 ? 0.39590 0.39749 0.41289 -0.00490 0.00766  -0.01274 229 ARG A CD  
1891 N NE  . ARG A 243 ? 0.50128 0.50149 0.51771 -0.00487 0.00820  -0.01179 229 ARG A NE  
1892 C CZ  . ARG A 243 ? 0.40401 0.40672 0.43057 -0.00638 0.01280  -0.01581 229 ARG A CZ  
1893 N NH1 . ARG A 243 ? 0.36284 0.36858 0.38888 -0.00484 0.01104  -0.01318 229 ARG A NH1 
1894 N NH2 . ARG A 243 ? 0.45983 0.46116 0.48487 -0.00644 0.01339  -0.01484 229 ARG A NH2 
1895 N N   . ARG A 244 ? 0.08627 0.10001 0.09321 -0.00748 0.00610  -0.01392 230 ARG A N   
1896 C CA  . ARG A 244 ? 0.10170 0.12246 0.10703 -0.00967 0.00611  -0.01546 230 ARG A CA  
1897 C C   . ARG A 244 ? 0.12418 0.13989 0.12903 -0.00865 0.00461  -0.01041 230 ARG A C   
1898 O O   . ARG A 244 ? 0.08392 0.09545 0.08360 -0.00693 0.00427  -0.00910 230 ARG A O   
1899 C CB  . ARG A 244 ? 0.11132 0.13970 0.12008 -0.01104 0.00365  -0.01211 230 ARG A CB  
1900 C CG  . ARG A 244 ? 0.09281 0.12974 0.10103 -0.01292 0.00298  -0.01303 230 ARG A CG  
1901 C CD  . ARG A 244 ? 0.08833 0.13364 0.10265 -0.01307 -0.00032 -0.00907 230 ARG A CD  
1902 N NE  . ARG A 244 ? 0.12304 0.16689 0.13176 -0.01240 -0.00040 -0.00566 230 ARG A NE  
1903 C CZ  . ARG A 244 ? 0.09229 0.14306 0.10416 -0.01172 -0.00252 -0.00208 230 ARG A CZ  
1904 N NH1 . ARG A 244 ? 0.10262 0.16215 0.12351 -0.01110 -0.00536 -0.00156 230 ARG A NH1 
1905 N NH2 . ARG A 244 ? 0.10428 0.15360 0.10988 -0.01124 -0.00192 0.00100  230 ARG A NH2 
1906 N N   . GLU A 245 ? 0.09452 0.11483 0.09928 -0.01173 0.00737  -0.01612 231 GLU A N   
1907 C CA  . GLU A 245 ? 0.12527 0.13796 0.12579 -0.00858 0.00602  -0.01194 231 GLU A CA  
1908 C C   . GLU A 245 ? 0.09814 0.11711 0.10292 -0.01172 0.00603  -0.01264 231 GLU A C   
1909 O O   . GLU A 245 ? 0.10450 0.12376 0.10579 -0.01103 0.00744  -0.01638 231 GLU A O   
1910 C CB  . GLU A 245 ? 0.17986 0.19124 0.18506 -0.00929 0.00605  -0.01080 231 GLU A CB  
1911 C CG  . GLU A 245 ? 0.22231 0.23079 0.22593 -0.00867 0.00573  -0.00919 231 GLU A CG  
1912 C CD  . GLU A 245 ? 0.26162 0.27379 0.26355 -0.01219 0.00845  -0.01366 231 GLU A CD  
1913 O OE1 . GLU A 245 ? 0.19811 0.21078 0.20261 -0.01146 0.00710  -0.01204 231 GLU A OE1 
1914 O OE2 . GLU A 245 ? 0.21437 0.22498 0.21466 -0.01184 0.00781  -0.01206 231 GLU A OE2 
1915 N N   . PRO A 246 ? 0.09553 0.11957 0.09645 -0.01513 0.00775  -0.01605 232 PRO A N   
1916 C CA  . PRO A 246 ? 0.10931 0.12413 0.10630 -0.01007 0.00520  -0.01028 232 PRO A CA  
1917 C C   . PRO A 246 ? 0.12970 0.14854 0.13073 -0.01098 0.00393  -0.00856 232 PRO A C   
1918 O O   . PRO A 246 ? 0.11671 0.14085 0.11864 -0.01179 0.00397  -0.00975 232 PRO A O   
1919 C CB  . PRO A 246 ? 0.11899 0.14149 0.11657 -0.01567 0.00672  -0.01309 232 PRO A CB  
1920 C CG  . PRO A 246 ? 0.15987 0.18396 0.16171 -0.01457 0.00564  -0.01198 232 PRO A CG  
1921 C CD  . PRO A 246 ? 0.15390 0.18283 0.15475 -0.01745 0.00862  -0.01833 232 PRO A CD  
1922 N N   . PHE A 247 ? 0.08274 0.10193 0.08020 -0.01195 0.00428  -0.00893 233 PHE A N   
1923 C CA  . PHE A 247 ? 0.09519 0.11278 0.09490 -0.00927 0.00229  -0.00534 233 PHE A CA  
1924 C C   . PHE A 247 ? 0.08583 0.10768 0.08031 -0.00971 0.00192  -0.00504 233 PHE A C   
1925 O O   . PHE A 247 ? 0.08100 0.11298 0.07632 -0.01163 0.00192  -0.00493 233 PHE A O   
1926 C CB  . PHE A 247 ? 0.07901 0.09149 0.07817 -0.00737 0.00168  -0.00361 233 PHE A CB  
1927 C CG  . PHE A 247 ? 0.11738 0.13212 0.11654 -0.00695 0.00074  -0.00185 233 PHE A CG  
1928 C CD1 . PHE A 247 ? 0.11208 0.13110 0.10929 -0.00807 0.00102  -0.00282 233 PHE A CD1 
1929 C CD2 . PHE A 247 ? 0.10645 0.12181 0.10245 -0.00624 -0.00019 0.00053  233 PHE A CD2 
1930 C CE1 . PHE A 247 ? 0.09912 0.12256 0.10315 -0.00758 -0.00000 0.00150  233 PHE A CE1 
1931 C CE2 . PHE A 247 ? 0.12276 0.14408 0.12070 -0.00628 -0.00131 0.00431  233 PHE A CE2 
1932 C CZ  . PHE A 247 ? 0.10691 0.13322 0.10877 -0.00685 -0.00125 0.00595  233 PHE A CZ  
1933 N N   . PHE A 248 ? 0.06070 0.08220 0.05453 -0.01037 0.00192  -0.00476 234 PHE A N   
1934 C CA  . PHE A 248 ? 0.07186 0.09922 0.06477 -0.01161 0.00151  -0.00411 234 PHE A CA  
1935 C C   . PHE A 248 ? 0.09965 0.13222 0.09893 -0.01445 0.00230  -0.00606 234 PHE A C   
1936 O O   . PHE A 248 ? 0.10422 0.13295 0.10277 -0.01487 0.00275  -0.00648 234 PHE A O   
1937 C CB  . PHE A 248 ? 0.09393 0.11881 0.08666 -0.01130 0.00090  -0.00233 234 PHE A CB  
1938 C CG  . PHE A 248 ? 0.16507 0.18825 0.15880 -0.00970 -0.00002 0.00006  234 PHE A CG  
1939 C CD1 . PHE A 248 ? 0.09495 0.12663 0.09531 -0.01007 -0.00063 0.00218  234 PHE A CD1 
1940 C CD2 . PHE A 248 ? 0.11441 0.13102 0.10881 -0.00834 -0.00006 0.00015  234 PHE A CD2 
1941 C CE1 . PHE A 248 ? 0.08563 0.11341 0.08161 -0.00746 -0.00128 0.00509  234 PHE A CE1 
1942 C CE2 . PHE A 248 ? 0.11275 0.12816 0.10847 -0.00682 -0.00074 0.00195  234 PHE A CE2 
1943 C CZ  . PHE A 248 ? 0.11642 0.13933 0.11754 -0.00703 -0.00121 0.00427  234 PHE A CZ  
1944 N N   . HIS A 249 ? 0.07818 0.11871 0.07259 -0.01542 0.00410  -0.00845 235 HIS A N   
1945 C CA  . HIS A 249 ? 0.10154 0.14573 0.09659 -0.01728 0.00540  -0.01182 235 HIS A CA  
1946 C C   . HIS A 249 ? 0.12336 0.18061 0.11874 -0.02062 0.00530  -0.01346 235 HIS A C   
1947 O O   . HIS A 249 ? 0.14931 0.22166 0.14620 -0.02315 0.00510  -0.01716 235 HIS A O   
1948 C CB  . HIS A 249 ? 0.15007 0.19963 0.14713 -0.01832 0.00593  -0.01562 235 HIS A CB  
1949 C CG  . HIS A 249 ? 0.14466 0.19346 0.14281 -0.01910 0.00750  -0.01877 235 HIS A CG  
1950 N ND1 . HIS A 249 ? 0.13044 0.17516 0.13015 -0.01813 0.00830  -0.02045 235 HIS A ND1 
1951 C CD2 . HIS A 249 ? 0.18550 0.23771 0.18371 -0.02090 0.00844  -0.02055 235 HIS A CD2 
1952 C CE1 . HIS A 249 ? 0.14462 0.18994 0.14523 -0.01906 0.00962  -0.02275 235 HIS A CE1 
1953 N NE2 . HIS A 249 ? 0.14344 0.19335 0.14316 -0.02085 0.00978  -0.02305 235 HIS A NE2 
1954 N N   . GLY A 250 ? 0.12186 0.17444 0.11620 -0.02035 0.00533  -0.01123 236 GLY A N   
1955 C CA  . GLY A 250 ? 0.14411 0.20952 0.13845 -0.02381 0.00506  -0.01287 236 GLY A CA  
1956 C C   . GLY A 250 ? 0.17833 0.24753 0.17306 -0.02624 0.00653  -0.01701 236 GLY A C   
1957 O O   . GLY A 250 ? 0.16627 0.22496 0.16109 -0.02468 0.00786  -0.01715 236 GLY A O   
1958 N N   . GLN A 251 ? 0.14732 0.23142 0.14253 -0.02922 0.00529  -0.02014 237 GLN A N   
1959 C CA  . GLN A 251 ? 0.21983 0.30780 0.21584 -0.03159 0.00591  -0.02462 237 GLN A CA  
1960 C C   . GLN A 251 ? 0.28780 0.37340 0.28201 -0.03386 0.00848  -0.02411 237 GLN A C   
1961 O O   . GLN A 251 ? 0.24496 0.32956 0.23963 -0.03538 0.01013  -0.02695 237 GLN A O   
1962 C CB  . GLN A 251 ? 0.28058 0.37724 0.27797 -0.03148 -0.00085 -0.02750 237 GLN A CB  
1963 C CG  . GLN A 251 ? 0.48835 0.58787 0.48966 -0.03004 -0.00364 -0.02909 237 GLN A CG  
1964 C CD  . GLN A 251 ? 0.60679 0.70328 0.61039 -0.03101 0.00092  -0.03223 237 GLN A CD  
1965 O OE1 . GLN A 251 ? 0.59316 0.68250 0.59578 -0.02979 0.00493  -0.03060 237 GLN A OE1 
1966 N NE2 . GLN A 251 ? 0.54942 0.65112 0.55544 -0.03298 0.00020  -0.03698 237 GLN A NE2 
1967 N N   . ASP A 252 ? 0.20565 0.28772 0.19827 -0.03338 0.00743  -0.02032 238 ASP A N   
1968 C CA  . ASP A 252 ? 0.18479 0.26065 0.17591 -0.03448 0.00799  -0.01911 238 ASP A CA  
1969 C C   . ASP A 252 ? 0.17952 0.24774 0.17000 -0.03223 0.00663  -0.01452 238 ASP A C   
1970 O O   . ASP A 252 ? 0.13684 0.20483 0.12805 -0.02999 0.00549  -0.01245 238 ASP A O   
1971 C CB  . ASP A 252 ? 0.22940 0.31634 0.21847 -0.03777 0.00596  -0.02272 238 ASP A CB  
1972 C CG  . ASP A 252 ? 0.27059 0.36208 0.25641 -0.03482 -0.00126 -0.02268 238 ASP A CG  
1973 O OD1 . ASP A 252 ? 0.30126 0.38996 0.28487 -0.03250 -0.00317 -0.01901 238 ASP A OD1 
1974 O OD2 . ASP A 252 ? 0.34435 0.44233 0.32966 -0.03465 -0.00511 -0.02620 238 ASP A OD2 
1975 N N   . ASN A 253 ? 0.15593 0.21820 0.14522 -0.03293 0.00680  -0.01330 239 ASN A N   
1976 C CA  . ASN A 253 ? 0.14648 0.20085 0.13575 -0.03077 0.00560  -0.00978 239 ASN A CA  
1977 C C   . ASN A 253 ? 0.18397 0.25212 0.17183 -0.03285 0.00367  -0.00890 239 ASN A C   
1978 O O   . ASN A 253 ? 0.21919 0.28274 0.20784 -0.03031 0.00256  -0.00605 239 ASN A O   
1979 C CB  . ASN A 253 ? 0.17585 0.22259 0.16407 -0.03134 0.00609  -0.00935 239 ASN A CB  
1980 C CG  . ASN A 253 ? 0.23481 0.26909 0.22671 -0.02796 0.00525  -0.00938 239 ASN A CG  
1981 O OD1 . ASN A 253 ? 0.20245 0.23169 0.18599 -0.02402 0.00591  -0.01051 239 ASN A OD1 
1982 N ND2 . ASN A 253 ? 0.31727 0.34499 0.29798 -0.02647 0.00646  -0.01067 239 ASN A ND2 
1983 N N   . TYR A 254 ? 0.14374 0.21801 0.12577 -0.03181 -0.00029 -0.01125 240 TYR A N   
1984 C CA  . TYR A 254 ? 0.19696 0.27311 0.17266 -0.02716 -0.00566 -0.00966 240 TYR A CA  
1985 C C   . TYR A 254 ? 0.14735 0.22693 0.12668 -0.02474 -0.00668 -0.00837 240 TYR A C   
1986 O O   . TYR A 254 ? 0.14734 0.22477 0.12585 -0.02147 -0.00782 -0.00486 240 TYR A O   
1987 C CB  . TYR A 254 ? 0.16446 0.24583 0.13289 -0.02649 -0.01010 -0.01243 240 TYR A CB  
1988 C CG  . TYR A 254 ? 0.21206 0.28962 0.17434 -0.02798 -0.00977 -0.01349 240 TYR A CG  
1989 C CD1 . TYR A 254 ? 0.21845 0.28972 0.17318 -0.02515 -0.01067 -0.01056 240 TYR A CD1 
1990 C CD2 . TYR A 254 ? 0.29130 0.37123 0.25454 -0.03190 -0.00834 -0.01745 240 TYR A CD2 
1991 C CE1 . TYR A 254 ? 0.31155 0.37862 0.25963 -0.02623 -0.01017 -0.01164 240 TYR A CE1 
1992 C CE2 . TYR A 254 ? 0.31219 0.38852 0.26957 -0.03334 -0.00797 -0.01851 240 TYR A CE2 
1993 C CZ  . TYR A 254 ? 0.38222 0.45204 0.33193 -0.03049 -0.00895 -0.01565 240 TYR A CZ  
1994 O OH  . TYR A 254 ? 0.41403 0.47966 0.35718 -0.03167 -0.00831 -0.01678 240 TYR A OH  
1995 N N   . ASP A 255 ? 0.12874 0.21313 0.11174 -0.02610 -0.00615 -0.01126 241 ASP A N   
1996 C CA  . ASP A 255 ? 0.12331 0.21036 0.10947 -0.02392 -0.00730 -0.01049 241 ASP A CA  
1997 C C   . ASP A 255 ? 0.12217 0.20321 0.11233 -0.02378 -0.00277 -0.00739 241 ASP A C   
1998 O O   . ASP A 255 ? 0.11709 0.19867 0.10848 -0.02114 -0.00413 -0.00532 241 ASP A O   
1999 C CB  . ASP A 255 ? 0.12284 0.21463 0.11182 -0.02555 -0.00740 -0.01482 241 ASP A CB  
2000 C CG  . ASP A 255 ? 0.17360 0.26822 0.16579 -0.02332 -0.00977 -0.01452 241 ASP A CG  
2001 O OD1 . ASP A 255 ? 0.17622 0.27492 0.16715 -0.02027 -0.01501 -0.01252 241 ASP A OD1 
2002 O OD2 . ASP A 255 ? 0.18890 0.28136 0.18443 -0.02434 -0.00648 -0.01616 241 ASP A OD2 
2003 N N   . GLN A 256 ? 0.13525 0.20991 0.12746 -0.02644 0.00225  -0.00686 242 GLN A N   
2004 C CA  . GLN A 256 ? 0.12756 0.18471 0.12113 -0.02236 0.00261  -0.00440 242 GLN A CA  
2005 C C   . GLN A 256 ? 0.10139 0.16018 0.09564 -0.02101 0.00105  -0.00116 242 GLN A C   
2006 O O   . GLN A 256 ? 0.09500 0.14873 0.09071 -0.01815 0.00082  0.00047  242 GLN A O   
2007 C CB  . GLN A 256 ? 0.10727 0.14888 0.10144 -0.02039 0.00398  -0.00436 242 GLN A CB  
2008 C CG  . GLN A 256 ? 0.11230 0.14186 0.10094 -0.01699 0.00210  -0.00462 242 GLN A CG  
2009 C CD  . GLN A 256 ? 0.06640 0.09520 0.05597 -0.01610 0.00247  -0.00553 242 GLN A CD  
2010 O OE1 . GLN A 256 ? 0.11891 0.15434 0.11643 -0.01871 0.00295  -0.00685 242 GLN A OE1 
2011 N NE2 . GLN A 256 ? 0.12323 0.14975 0.12003 -0.01556 0.00187  -0.00405 242 GLN A NE2 
2012 N N   . LEU A 257 ? 0.10036 0.16740 0.09323 -0.02304 0.00005  -0.00012 243 LEU A N   
2013 C CA  . LEU A 257 ? 0.08399 0.14826 0.07378 -0.01877 -0.00252 0.00314  243 LEU A CA  
2014 C C   . LEU A 257 ? 0.08577 0.15557 0.07238 -0.01439 -0.00556 0.00506  243 LEU A C   
2015 O O   . LEU A 257 ? 0.11799 0.18626 0.10548 -0.01109 -0.00568 0.00844  243 LEU A O   
2016 C CB  . LEU A 257 ? 0.11506 0.17471 0.09661 -0.01744 -0.00404 0.00347  243 LEU A CB  
2017 C CG  . LEU A 257 ? 0.12169 0.17539 0.09764 -0.01241 -0.00464 0.00734  243 LEU A CG  
2018 C CD1 . LEU A 257 ? 0.13936 0.18643 0.12200 -0.01287 -0.00256 0.00795  243 LEU A CD1 
2019 C CD2 . LEU A 257 ? 0.15307 0.20167 0.11849 -0.01084 -0.00516 0.00780  243 LEU A CD2 
2020 N N   . VAL A 258 ? 0.10368 0.17997 0.08727 -0.01426 -0.00854 0.00292  244 VAL A N   
2021 C CA  . VAL A 258 ? 0.09489 0.17696 0.07733 -0.01055 -0.01260 0.00457  244 VAL A CA  
2022 C C   . VAL A 258 ? 0.15022 0.23240 0.13949 -0.01048 -0.01054 0.00549  244 VAL A C   
2023 O O   . VAL A 258 ? 0.11957 0.20266 0.10955 -0.00683 -0.01195 0.00914  244 VAL A O   
2024 C CB  . VAL A 258 ? 0.15164 0.24101 0.13155 -0.01107 -0.01705 0.00121  244 VAL A CB  
2025 C CG1 . VAL A 258 ? 0.15673 0.25254 0.13715 -0.00733 -0.02204 0.00316  244 VAL A CG1 
2026 C CG2 . VAL A 258 ? 0.12165 0.21024 0.09337 -0.01109 -0.01895 0.00045  244 VAL A CG2 
2027 N N   . ARG A 259 ? 0.07486 0.15511 0.06813 -0.01423 -0.00671 0.00254  245 ARG A N   
2028 C CA  . ARG A 259 ? 0.08758 0.16552 0.08424 -0.01408 -0.00451 0.00316  245 ARG A CA  
2029 C C   . ARG A 259 ? 0.12110 0.19378 0.11948 -0.01291 -0.00149 0.00728  245 ARG A C   
2030 O O   . ARG A 259 ? 0.12797 0.19959 0.12758 -0.01090 -0.00160 0.00953  245 ARG A O   
2031 C CB  . ARG A 259 ? 0.12965 0.20316 0.12579 -0.01736 -0.00027 -0.00043 245 ARG A CB  
2032 C CG  . ARG A 259 ? 0.20760 0.28615 0.20408 -0.01893 -0.00219 -0.00509 245 ARG A CG  
2033 C CD  . ARG A 259 ? 0.18222 0.26729 0.18209 -0.01716 -0.00748 -0.00627 245 ARG A CD  
2034 N NE  . ARG A 259 ? 0.22626 0.31633 0.22739 -0.01907 -0.00911 -0.01102 245 ARG A NE  
2035 C CZ  . ARG A 259 ? 0.28617 0.37717 0.29116 -0.01973 -0.00936 -0.01410 245 ARG A CZ  
2036 N NH1 . ARG A 259 ? 0.33075 0.41740 0.33839 -0.01867 -0.00831 -0.01310 245 ARG A NH1 
2037 N NH2 . ARG A 259 ? 0.26028 0.35664 0.26680 -0.02152 -0.01092 -0.01840 245 ARG A NH2 
2038 N N   . ILE A 260 ? 0.09593 0.15918 0.09461 -0.01299 -0.00097 0.00707  246 ILE A N   
2039 C CA  . ILE A 260 ? 0.07372 0.12679 0.07465 -0.01027 -0.00099 0.00875  246 ILE A CA  
2040 C C   . ILE A 260 ? 0.13895 0.20610 0.14128 -0.00729 -0.00155 0.01450  246 ILE A C   
2041 O O   . ILE A 260 ? 0.12156 0.18483 0.12615 -0.00435 -0.00101 0.01687  246 ILE A O   
2042 C CB  . ILE A 260 ? 0.10565 0.14912 0.10644 -0.01097 -0.00130 0.00668  246 ILE A CB  
2043 C CG1 . ILE A 260 ? 0.10977 0.13947 0.10323 -0.01073 -0.00105 0.00324  246 ILE A CG1 
2044 C CG2 . ILE A 260 ? 0.10263 0.14260 0.10456 -0.00851 -0.00195 0.00864  246 ILE A CG2 
2045 C CD1 . ILE A 260 ? 0.09817 0.12506 0.09626 -0.01277 -0.00065 0.00163  246 ILE A CD1 
2046 N N   . ALA A 261 ? 0.10980 0.17871 0.10439 -0.00515 -0.00451 0.01506  247 ALA A N   
2047 C CA  . ALA A 261 ? 0.13549 0.20461 0.12508 0.00029  -0.00633 0.01958  247 ALA A CA  
2048 C C   . ALA A 261 ? 0.12746 0.20252 0.11952 0.00292  -0.00827 0.02190  247 ALA A C   
2049 O O   . ALA A 261 ? 0.13657 0.21111 0.12846 0.00721  -0.00804 0.02644  247 ALA A O   
2050 C CB  . ALA A 261 ? 0.12377 0.19332 0.10383 0.00152  -0.00938 0.01947  247 ALA A CB  
2051 N N   . LYS A 262 ? 0.12750 0.20754 0.12214 0.00060  -0.01018 0.01879  248 LYS A N   
2052 C CA  . LYS A 262 ? 0.16087 0.24562 0.15941 0.00302  -0.01271 0.02047  248 LYS A CA  
2053 C C   . LYS A 262 ? 0.14099 0.22145 0.14492 0.00347  -0.00861 0.02313  248 LYS A C   
2054 O O   . LYS A 262 ? 0.18009 0.26320 0.18776 0.00636  -0.01020 0.02572  248 LYS A O   
2055 C CB  . LYS A 262 ? 0.16836 0.25823 0.16950 0.00037  -0.01581 0.01568  248 LYS A CB  
2056 C CG  . LYS A 262 ? 0.26892 0.36487 0.26566 0.00071  -0.02080 0.01363  248 LYS A CG  
2057 C CD  . LYS A 262 ? 0.29294 0.39426 0.29367 -0.00197 -0.02355 0.00856  248 LYS A CD  
2058 C CE  . LYS A 262 ? 0.24594 0.35414 0.24239 -0.00135 -0.02901 0.00690  248 LYS A CE  
2059 N NZ  . LYS A 262 ? 0.53378 0.64747 0.53487 -0.00413 -0.03145 0.00172  248 LYS A NZ  
2060 N N   . VAL A 263 ? 0.10071 0.17480 0.10586 0.00060  -0.00352 0.02247  249 VAL A N   
2061 C CA  . VAL A 263 ? 0.12142 0.18914 0.13033 0.00065  0.00036  0.02454  249 VAL A CA  
2062 C C   . VAL A 263 ? 0.11155 0.17426 0.12289 0.00395  0.00201  0.02642  249 VAL A C   
2063 O O   . VAL A 263 ? 0.11645 0.17893 0.13052 0.00706  0.00373  0.03016  249 VAL A O   
2064 C CB  . VAL A 263 ? 0.09270 0.14354 0.09823 -0.00263 0.00010  0.01810  249 VAL A CB  
2065 C CG1 . VAL A 263 ? 0.10595 0.14352 0.11096 -0.00108 0.00027  0.01781  249 VAL A CG1 
2066 C CG2 . VAL A 263 ? 0.08950 0.14955 0.09358 -0.00515 -0.00126 0.01704  249 VAL A CG2 
2067 N N   . LEU A 264 ? 0.06468 0.12509 0.07505 0.00362  0.00166  0.02459  250 LEU A N   
2068 C CA  . LEU A 264 ? 0.04503 0.10194 0.05686 0.00734  0.00345  0.02688  250 LEU A CA  
2069 C C   . LEU A 264 ? 0.07816 0.13682 0.08324 0.01162  0.00369  0.03155  250 LEU A C   
2070 O O   . LEU A 264 ? 0.12053 0.17467 0.12571 0.01505  0.00631  0.03390  250 LEU A O   
2071 C CB  . LEU A 264 ? 0.08676 0.13672 0.09698 0.00542  0.00249  0.02323  250 LEU A CB  
2072 C CG  . LEU A 264 ? 0.09584 0.13181 0.10560 0.00317  0.00131  0.01770  250 LEU A CG  
2073 C CD1 . LEU A 264 ? 0.17695 0.20818 0.18512 0.00014  -0.00075 0.01336  250 LEU A CD1 
2074 C CD2 . LEU A 264 ? 0.05589 0.08848 0.06376 0.00187  0.00082  0.01579  250 LEU A CD2 
2075 N N   . GLY A 265 ? 0.14158 0.20522 0.14014 0.01178  0.00015  0.03226  251 GLY A N   
2076 C CA  . GLY A 265 ? 0.14886 0.21360 0.14052 0.01626  -0.00160 0.03641  251 GLY A CA  
2077 C C   . GLY A 265 ? 0.13407 0.19564 0.11639 0.01607  -0.00317 0.03554  251 GLY A C   
2078 O O   . GLY A 265 ? 0.15574 0.21093 0.13729 0.01376  -0.00112 0.03298  251 GLY A O   
2079 N N   . THR A 266 ? 0.12642 0.19208 0.10150 0.01853  -0.00713 0.03761  252 THR A N   
2080 C CA  . THR A 266 ? 0.16362 0.22624 0.12887 0.01817  -0.00857 0.03685  252 THR A CA  
2081 C C   . THR A 266 ? 0.20477 0.26051 0.16561 0.02141  -0.00533 0.04064  252 THR A C   
2082 O O   . THR A 266 ? 0.15727 0.20671 0.11270 0.01980  -0.00398 0.03911  252 THR A O   
2083 C CB  . THR A 266 ? 0.18591 0.25593 0.14505 0.01925  -0.01451 0.03694  252 THR A CB  
2084 O OG1 . THR A 266 ? 0.16348 0.23873 0.12467 0.02375  -0.01651 0.04147  252 THR A OG1 
2085 C CG2 . THR A 266 ? 0.15380 0.22924 0.11635 0.01499  -0.01724 0.03153  252 THR A CG2 
2086 N N   . GLU A 267 ? 0.17257 0.22926 0.13569 0.02596  -0.00383 0.04556  253 GLU A N   
2087 C CA  . GLU A 267 ? 0.19799 0.24830 0.15787 0.02905  -0.00007 0.04885  253 GLU A CA  
2088 C C   . GLU A 267 ? 0.17561 0.21838 0.14067 0.02682  0.00470  0.04594  253 GLU A C   
2089 O O   . GLU A 267 ? 0.18198 0.21820 0.14274 0.02711  0.00696  0.04594  253 GLU A O   
2090 C CB  . GLU A 267 ? 0.16843 0.22128 0.13094 0.03444  0.00128  0.05455  253 GLU A CB  
2091 C CG  . GLU A 267 ? 0.24366 0.30276 0.19931 0.03774  -0.00387 0.05822  253 GLU A CG  
2092 C CD  . GLU A 267 ? 0.26652 0.32290 0.21036 0.03841  -0.00553 0.05910  253 GLU A CD  
2093 O OE1 . GLU A 267 ? 0.30809 0.35832 0.24891 0.04055  -0.00154 0.06158  253 GLU A OE1 
2094 O OE2 . GLU A 267 ? 0.46675 0.52728 0.40436 0.03673  -0.01076 0.05708  253 GLU A OE2 
2095 N N   . GLU A 268 ? 0.15164 0.19539 0.12595 0.02456  0.00589  0.04322  254 GLU A N   
2096 C CA  . GLU A 268 ? 0.13547 0.17262 0.11522 0.02253  0.00923  0.03979  254 GLU A CA  
2097 C C   . GLU A 268 ? 0.14452 0.17695 0.11906 0.01824  0.00778  0.03563  254 GLU A C   
2098 O O   . GLU A 268 ? 0.15792 0.18298 0.13204 0.01769  0.01013  0.03400  254 GLU A O   
2099 C CB  . GLU A 268 ? 0.12846 0.16860 0.11866 0.02114  0.00992  0.03787  254 GLU A CB  
2100 C CG  . GLU A 268 ? 0.16908 0.21231 0.16564 0.02521  0.01284  0.04177  254 GLU A CG  
2101 C CD  . GLU A 268 ? 0.24042 0.29118 0.23489 0.02710  0.01025  0.04580  254 GLU A CD  
2102 O OE1 . GLU A 268 ? 0.17732 0.23225 0.16669 0.02532  0.00562  0.04489  254 GLU A OE1 
2103 O OE2 . GLU A 268 ? 0.20443 0.25692 0.20260 0.03061  0.01265  0.04971  254 GLU A OE2 
2104 N N   . LEU A 269 ? 0.14613 0.18283 0.11686 0.01529  0.00406  0.03367  255 LEU A N   
2105 C CA  . LEU A 269 ? 0.12504 0.15745 0.09012 0.01135  0.00305  0.02994  255 LEU A CA  
2106 C C   . LEU A 269 ? 0.13032 0.15734 0.08598 0.01282  0.00397  0.03189  255 LEU A C   
2107 O O   . LEU A 269 ? 0.12956 0.14918 0.08323 0.01060  0.00579  0.02969  255 LEU A O   
2108 C CB  . LEU A 269 ? 0.13980 0.17927 0.10280 0.00885  -0.00083 0.02762  255 LEU A CB  
2109 C CG  . LEU A 269 ? 0.12431 0.16088 0.08084 0.00539  -0.00189 0.02401  255 LEU A CG  
2110 C CD1 . LEU A 269 ? 0.13559 0.16526 0.09683 0.00175  0.00046  0.02016  255 LEU A CD1 
2111 C CD2 . LEU A 269 ? 0.15121 0.19681 0.10707 0.00372  -0.00572 0.02175  255 LEU A CD2 
2112 N N   . TYR A 270 ? 0.12925 0.16000 0.07886 0.01649  0.00254  0.03607  256 TYR A N   
2113 C CA  . TYR A 270 ? 0.11516 0.14133 0.05527 0.01786  0.00330  0.03816  256 TYR A CA  
2114 C C   . TYR A 270 ? 0.15425 0.17361 0.09754 0.01989  0.00809  0.03961  256 TYR A C   
2115 O O   . TYR A 270 ? 0.20042 0.21392 0.13837 0.01907  0.00970  0.03921  256 TYR A O   
2116 C CB  . TYR A 270 ? 0.14939 0.18128 0.08266 0.02189  0.00040  0.04264  256 TYR A CB  
2117 C CG  . TYR A 270 ? 0.14465 0.18449 0.07531 0.02063  -0.00497 0.04095  256 TYR A CG  
2118 C CD1 . TYR A 270 ? 0.15810 0.19790 0.08665 0.01602  -0.00680 0.03578  256 TYR A CD1 
2119 C CD2 . TYR A 270 ? 0.14144 0.18909 0.07240 0.02429  -0.00820 0.04435  256 TYR A CD2 
2120 C CE1 . TYR A 270 ? 0.16716 0.21519 0.09438 0.01514  -0.01167 0.03371  256 TYR A CE1 
2121 C CE2 . TYR A 270 ? 0.15638 0.21203 0.08585 0.02335  -0.01355 0.04241  256 TYR A CE2 
2122 C CZ  . TYR A 270 ? 0.16068 0.21674 0.08843 0.01876  -0.01524 0.03692  256 TYR A CZ  
2123 O OH  . TYR A 270 ? 0.26350 0.32826 0.19085 0.01796  -0.02049 0.03458  256 TYR A OH  
2124 N N   . GLY A 271 ? 0.16535 0.18559 0.11765 0.02267  0.01060  0.04100  257 GLY A N   
2125 C CA  . GLY A 271 ? 0.15847 0.17248 0.11483 0.02499  0.01530  0.04139  257 GLY A CA  
2126 C C   . GLY A 271 ? 0.17454 0.18226 0.13369 0.02115  0.01634  0.03634  257 GLY A C   
2127 O O   . GLY A 271 ? 0.15119 0.15274 0.10910 0.02220  0.01919  0.03595  257 GLY A O   
2128 N N   . TYR A 272 ? 0.12705 0.13625 0.09001 0.01691  0.01402  0.03243  258 TYR A N   
2129 C CA  . TYR A 272 ? 0.13316 0.13672 0.09815 0.01294  0.01421  0.02762  258 TYR A CA  
2130 C C   . TYR A 272 ? 0.12559 0.12585 0.08188 0.00989  0.01354  0.02671  258 TYR A C   
2131 O O   . TYR A 272 ? 0.15108 0.14577 0.10773 0.00951  0.01549  0.02507  258 TYR A O   
2132 C CB  . TYR A 272 ? 0.12923 0.13555 0.09905 0.00914  0.01165  0.02419  258 TYR A CB  
2133 C CG  . TYR A 272 ? 0.11726 0.11867 0.08742 0.00413  0.01082  0.01927  258 TYR A CG  
2134 C CD1 . TYR A 272 ? 0.12592 0.12195 0.10061 0.00501  0.01256  0.01695  258 TYR A CD1 
2135 C CD2 . TYR A 272 ? 0.13694 0.13858 0.10316 -0.00021 0.00869  0.01665  258 TYR A CD2 
2136 C CE1 . TYR A 272 ? 0.12065 0.11392 0.09685 0.00143  0.01135  0.01279  258 TYR A CE1 
2137 C CE2 . TYR A 272 ? 0.15870 0.15447 0.12567 -0.00383 0.00860  0.01202  258 TYR A CE2 
2138 C CZ  . TYR A 272 ? 0.14397 0.14228 0.11868 -0.00385 0.00852  0.01149  258 TYR A CZ  
2139 O OH  . TYR A 272 ? 0.16472 0.15953 0.14309 -0.00355 0.00834  0.00781  258 TYR A OH  
2140 N N   . LEU A 273 ? 0.14530 0.14902 0.09382 0.00821  0.01087  0.02752  259 LEU A N   
2141 C CA  . LEU A 273 ? 0.13543 0.13613 0.07468 0.00541  0.01042  0.02669  259 LEU A CA  
2142 C C   . LEU A 273 ? 0.16032 0.15782 0.09601 0.00882  0.01320  0.02985  259 LEU A C   
2143 O O   . LEU A 273 ? 0.17429 0.16784 0.10761 0.00689  0.01456  0.02841  259 LEU A O   
2144 C CB  . LEU A 273 ? 0.19145 0.19648 0.12234 0.00518  0.00712  0.02722  259 LEU A CB  
2145 C CG  . LEU A 273 ? 0.15033 0.15995 0.08490 0.00349  0.00453  0.02408  259 LEU A CG  
2146 C CD1 . LEU A 273 ? 0.18854 0.20486 0.11572 0.00454  0.00082  0.02471  259 LEU A CD1 
2147 C CD2 . LEU A 273 ? 0.18866 0.19281 0.12614 -0.00027 0.00562  0.01906  259 LEU A CD2 
2148 N N   . LYS A 274 ? 0.13823 0.13757 0.07384 0.01430  0.01438  0.03428  260 LYS A N   
2149 C CA  . LYS A 274 ? 0.18387 0.17919 0.11552 0.01819  0.01757  0.03744  260 LYS A CA  
2150 C C   . LYS A 274 ? 0.21244 0.20104 0.15110 0.01933  0.02156  0.03520  260 LYS A C   
2151 O O   . LYS A 274 ? 0.20854 0.19176 0.14356 0.02004  0.02397  0.03519  260 LYS A O   
2152 C CB  . LYS A 274 ? 0.19653 0.19531 0.12711 0.02395  0.01820  0.04279  260 LYS A CB  
2153 C CG  . LYS A 274 ? 0.24211 0.23603 0.16952 0.02865  0.02236  0.04629  260 LYS A CG  
2154 C CD  . LYS A 274 ? 0.23028 0.22795 0.15706 0.03423  0.02303  0.05180  260 LYS A CD  
2155 C CE  . LYS A 274 ? 0.31227 0.30451 0.23792 0.03922  0.02817  0.05505  260 LYS A CE  
2156 N NZ  . LYS A 274 ? 0.39292 0.38146 0.30773 0.03899  0.02839  0.05638  260 LYS A NZ  
2157 N N   . LYS A 275 ? 0.13613 0.12459 0.08453 0.01978  0.02229  0.03294  261 LYS A N   
2158 C CA  . LYS A 275 ? 0.18543 0.16704 0.13999 0.02167  0.02592  0.03022  261 LYS A CA  
2159 C C   . LYS A 275 ? 0.19888 0.17524 0.15189 0.01806  0.02560  0.02612  261 LYS A C   
2160 O O   . LYS A 275 ? 0.18230 0.15155 0.13534 0.02022  0.02894  0.02491  261 LYS A O   
2161 C CB  . LYS A 275 ? 0.18605 0.16894 0.15035 0.02251  0.02619  0.02798  261 LYS A CB  
2162 C CG  . LYS A 275 ? 0.15706 0.13280 0.12703 0.02453  0.02962  0.02413  261 LYS A CG  
2163 C CD  . LYS A 275 ? 0.17586 0.15347 0.15449 0.02555  0.02982  0.02188  261 LYS A CD  
2164 C CE  . LYS A 275 ? 0.15250 0.12548 0.13493 0.02381  0.03023  0.01710  261 LYS A CE  
2165 N NZ  . LYS A 275 ? 0.19010 0.16774 0.17884 0.01988  0.02638  0.01416  261 LYS A NZ  
2166 N N   . TYR A 276 ? 0.17744 0.15719 0.12922 0.01270  0.02192  0.02389  262 TYR A N   
2167 C CA  . TYR A 276 ? 0.17534 0.15080 0.12685 0.00941  0.02165  0.01996  262 TYR A CA  
2168 C C   . TYR A 276 ? 0.18807 0.16551 0.13097 0.00683  0.02080  0.02134  262 TYR A C   
2169 O O   . TYR A 276 ? 0.20523 0.18049 0.14804 0.00400  0.02044  0.01829  262 TYR A O   
2170 C CB  . TYR A 276 ? 0.18568 0.16272 0.14345 0.00576  0.01896  0.01575  262 TYR A CB  
2171 C CG  . TYR A 276 ? 0.19169 0.16527 0.15699 0.00857  0.02014  0.01345  262 TYR A CG  
2172 C CD1 . TYR A 276 ? 0.20582 0.17054 0.17383 0.01031  0.02239  0.00912  262 TYR A CD1 
2173 C CD2 . TYR A 276 ? 0.12515 0.10430 0.09417 0.00973  0.01925  0.01528  262 TYR A CD2 
2174 C CE1 . TYR A 276 ? 0.13909 0.10380 0.11367 0.01206  0.02270  0.00683  262 TYR A CE1 
2175 C CE2 . TYR A 276 ? 0.21839 0.19522 0.19416 0.01257  0.02063  0.01315  262 TYR A CE2 
2176 C CZ  . TYR A 276 ? 0.19548 0.16462 0.17343 0.01406  0.02270  0.00877  262 TYR A CZ  
2177 O OH  . TYR A 276 ? 0.21184 0.18670 0.19674 0.01185  0.01973  0.00697  262 TYR A OH  
2178 N N   . HIS A 277 ? 0.19030 0.17117 0.12565 0.00827  0.02063  0.02564  263 HIS A N   
2179 C CA  . HIS A 277 ? 0.17860 0.16142 0.10421 0.00615  0.01986  0.02688  263 HIS A CA  
2180 C C   . HIS A 277 ? 0.21779 0.20761 0.14247 0.00009  0.01644  0.02411  263 HIS A C   
2181 O O   . HIS A 277 ? 0.23439 0.22581 0.15591 -0.00184 0.01663  0.02286  263 HIS A O   
2182 C CB  . HIS A 277 ? 0.28790 0.26288 0.21118 0.00812  0.02347  0.02654  263 HIS A CB  
2183 C CG  . HIS A 277 ? 0.25593 0.22437 0.18086 0.01395  0.02742  0.02873  263 HIS A CG  
2184 N ND1 . HIS A 277 ? 0.48477 0.45330 0.40283 0.01772  0.02899  0.03349  263 HIS A ND1 
2185 C CD2 . HIS A 277 ? 0.40112 0.36333 0.33386 0.01683  0.03023  0.02664  263 HIS A CD2 
2186 C CE1 . HIS A 277 ? 0.41149 0.37446 0.33378 0.02264  0.03299  0.03444  263 HIS A CE1 
2187 N NE2 . HIS A 277 ? 0.33222 0.29149 0.26331 0.02209  0.03383  0.03012  263 HIS A NE2 
2188 N N   . ILE A 278 ? 0.20625 0.20031 0.13392 -0.00235 0.01372  0.02302  264 ILE A N   
2189 C CA  . ILE A 278 ? 0.20973 0.20984 0.14026 -0.00715 0.01073  0.01917  264 ILE A CA  
2190 C C   . ILE A 278 ? 0.22841 0.21972 0.14230 -0.00724 0.00933  0.01892  264 ILE A C   
2191 O O   . ILE A 278 ? 0.20837 0.20167 0.11703 -0.00323 0.00819  0.02259  264 ILE A O   
2192 C CB  . ILE A 278 ? 0.21887 0.21844 0.15771 -0.00856 0.00930  0.01650  264 ILE A CB  
2193 C CG1 . ILE A 278 ? 0.14984 0.15028 0.09993 -0.00437 0.01152  0.01658  264 ILE A CG1 
2194 C CG2 . ILE A 278 ? 0.19467 0.18940 0.13107 0.00178  0.01108  0.01423  264 ILE A CG2 
2195 C CD1 . ILE A 278 ? 0.16001 0.16183 0.11845 -0.00443 0.01019  0.01510  264 ILE A CD1 
2196 N N   . ASP A 279 ? 0.23244 0.21365 0.13754 -0.00502 0.01031  0.01570  265 ASP A N   
2197 C CA  . ASP A 279 ? 0.21841 0.20419 0.11322 -0.00144 0.00781  0.01646  265 ASP A CA  
2198 C C   . ASP A 279 ? 0.23373 0.22971 0.13399 -0.00039 0.00482  0.01471  265 ASP A C   
2199 O O   . ASP A 279 ? 0.27603 0.27672 0.18758 -0.00151 0.00544  0.01198  265 ASP A O   
2200 C CB  . ASP A 279 ? 0.28673 0.27214 0.17642 0.00245  0.00928  0.01484  265 ASP A CB  
2201 C CG  . ASP A 279 ? 0.52692 0.50495 0.40978 -0.00849 0.01025  0.01595  265 ASP A CG  
2202 O OD1 . ASP A 279 ? 0.35295 0.34521 0.23914 -0.00937 0.00920  0.02137  265 ASP A OD1 
2203 O OD2 . ASP A 279 ? 0.48868 0.50476 0.39084 0.00541  0.01237  0.01899  265 ASP A OD2 
2204 N N   . LEU A 280 ? 0.24584 0.24897 0.14187 -0.00037 0.00074  0.01621  266 LEU A N   
2205 C CA  . LEU A 280 ? 0.23737 0.25225 0.14190 -0.00136 -0.00278 0.01402  266 LEU A CA  
2206 C C   . LEU A 280 ? 0.24591 0.26699 0.14491 -0.00268 -0.00599 0.01099  266 LEU A C   
2207 O O   . LEU A 280 ? 0.22813 0.24839 0.11525 -0.00104 -0.00796 0.01259  266 LEU A O   
2208 C CB  . LEU A 280 ? 0.25105 0.27192 0.15749 0.00088  -0.00525 0.01764  266 LEU A CB  
2209 C CG  . LEU A 280 ? 0.23055 0.26268 0.14629 -0.00004 -0.00838 0.01572  266 LEU A CG  
2210 C CD1 . LEU A 280 ? 0.17823 0.21013 0.10696 -0.00265 -0.00585 0.01343  266 LEU A CD1 
2211 C CD2 . LEU A 280 ? 0.28947 0.32743 0.20506 0.00352  -0.01097 0.01987  266 LEU A CD2 
2212 N N   . ASP A 281 ? 0.21551 0.24281 0.12339 -0.00645 -0.00644 0.00658  267 ASP A N   
2213 C CA  . ASP A 281 ? 0.20187 0.23603 0.10661 -0.00881 -0.00938 0.00289  267 ASP A CA  
2214 C C   . ASP A 281 ? 0.23964 0.28076 0.13828 -0.00644 -0.01441 0.00427  267 ASP A C   
2215 O O   . ASP A 281 ? 0.19613 0.24285 0.10140 -0.00555 -0.01607 0.00563  267 ASP A O   
2216 C CB  . ASP A 281 ? 0.18794 0.22861 0.10616 -0.01409 -0.00879 -0.00121 267 ASP A CB  
2217 C CG  . ASP A 281 ? 0.23797 0.28525 0.15463 -0.01748 -0.01085 -0.00570 267 ASP A CG  
2218 O OD1 . ASP A 281 ? 0.21111 0.26149 0.11790 -0.01547 -0.01455 -0.00601 267 ASP A OD1 
2219 O OD2 . ASP A 281 ? 0.21794 0.26733 0.14359 -0.02251 -0.00872 -0.00889 267 ASP A OD2 
2220 N N   . PRO A 282 ? 0.25471 0.29591 0.14104 -0.00526 -0.01704 0.00416  268 PRO A N   
2221 C CA  . PRO A 282 ? 0.25777 0.30604 0.13845 -0.00276 -0.02239 0.00611  268 PRO A CA  
2222 C C   . PRO A 282 ? 0.25475 0.31496 0.14386 -0.00467 -0.02631 0.00267  268 PRO A C   
2223 O O   . PRO A 282 ? 0.26683 0.33389 0.15480 -0.00224 -0.03075 0.00464  268 PRO A O   
2224 C CB  . PRO A 282 ? 0.23818 0.28335 0.10380 -0.00196 -0.02402 0.00600  268 PRO A CB  
2225 C CG  . PRO A 282 ? 0.30413 0.34435 0.17015 -0.00506 -0.02037 0.00181  268 PRO A CG  
2226 C CD  . PRO A 282 ? 0.30423 0.33920 0.18121 -0.00593 -0.01530 0.00250  268 PRO A CD  
2227 N N   . HIS A 283 ? 0.21843 0.28154 0.11646 -0.00903 -0.02469 -0.00220 269 HIS A N   
2228 C CA  . HIS A 283 ? 0.21766 0.29127 0.12455 -0.01110 -0.02755 -0.00536 269 HIS A CA  
2229 C C   . HIS A 283 ? 0.26030 0.33688 0.17522 -0.00896 -0.02793 -0.00227 269 HIS A C   
2230 O O   . HIS A 283 ? 0.21406 0.29942 0.13320 -0.00873 -0.03167 -0.00334 269 HIS A O   
2231 C CB  . HIS A 283 ? 0.24905 0.32401 0.16498 -0.01649 -0.02436 -0.01035 269 HIS A CB  
2232 C CG  . HIS A 283 ? 0.29253 0.37689 0.21791 -0.01877 -0.02610 -0.01354 269 HIS A CG  
2233 N ND1 . HIS A 283 ? 0.35930 0.45205 0.28168 -0.01866 -0.03133 -0.01617 269 HIS A ND1 
2234 C CD2 . HIS A 283 ? 0.29355 0.37986 0.23090 -0.02104 -0.02324 -0.01444 269 HIS A CD2 
2235 C CE1 . HIS A 283 ? 0.40735 0.50660 0.33976 -0.02070 -0.03149 -0.01873 269 HIS A CE1 
2236 N NE2 . HIS A 283 ? 0.37218 0.46740 0.31329 -0.02208 -0.02640 -0.01763 269 HIS A NE2 
2237 N N   . PHE A 284 ? 0.17809 0.24743 0.09533 -0.00736 -0.02411 0.00143  270 PHE A N   
2238 C CA  . PHE A 284 ? 0.19813 0.26961 0.12266 -0.00520 -0.02400 0.00456  270 PHE A CA  
2239 C C   . PHE A 284 ? 0.21365 0.28951 0.13255 -0.00057 -0.02853 0.00863  270 PHE A C   
2240 O O   . PHE A 284 ? 0.23914 0.32019 0.16479 0.00105  -0.02993 0.01031  270 PHE A O   
2241 C CB  . PHE A 284 ? 0.21504 0.27735 0.14274 -0.00457 -0.01891 0.00741  270 PHE A CB  
2242 C CG  . PHE A 284 ? 0.18363 0.24397 0.12156 -0.00901 -0.01491 0.00421  270 PHE A CG  
2243 C CD1 . PHE A 284 ? 0.16260 0.22862 0.11142 -0.01116 -0.01446 0.00262  270 PHE A CD1 
2244 C CD2 . PHE A 284 ? 0.20756 0.26028 0.14424 -0.01107 -0.01154 0.00311  270 PHE A CD2 
2245 C CE1 . PHE A 284 ? 0.15542 0.21963 0.11349 -0.01558 -0.01062 0.00025  270 PHE A CE1 
2246 C CE2 . PHE A 284 ? 0.18151 0.23297 0.12845 -0.01554 -0.00826 0.00069  270 PHE A CE2 
2247 C CZ  . PHE A 284 ? 0.15494 0.21214 0.11254 -0.01796 -0.00775 -0.00056 270 PHE A CZ  
2248 N N   . ASN A 285 ? 0.25062 0.32432 0.15742 0.00168  -0.03065 0.01062  271 ASN A N   
2249 C CA  . ASN A 285 ? 0.25263 0.33023 0.15427 0.00630  -0.03461 0.01545  271 ASN A CA  
2250 C C   . ASN A 285 ? 0.37931 0.46870 0.28614 0.00663  -0.04021 0.01383  271 ASN A C   
2251 O O   . ASN A 285 ? 0.44826 0.54198 0.35747 0.01032  -0.04262 0.01789  271 ASN A O   
2252 C CB  . ASN A 285 ? 0.32998 0.40427 0.21717 0.00793  -0.03634 0.01721  271 ASN A CB  
2253 C CG  . ASN A 285 ? 0.25157 0.31366 0.13286 0.00754  -0.03084 0.01876  271 ASN A CG  
2254 O OD1 . ASN A 285 ? 0.33064 0.38674 0.21829 0.00731  -0.02610 0.02009  271 ASN A OD1 
2255 N ND2 . ASN A 285 ? 0.38697 0.44520 0.25586 0.00737  -0.03151 0.01846  271 ASN A ND2 
2256 N N   . ASP A 286 ? 0.34329 0.43796 0.25256 0.00285  -0.04217 0.00795  272 ASP A N   
2257 C CA  . ASP A 286 ? 0.33564 0.44143 0.24965 0.00266  -0.04768 0.00560  272 ASP A CA  
2258 C C   . ASP A 286 ? 0.29427 0.40368 0.22199 0.00087  -0.04612 0.00372  272 ASP A C   
2259 O O   . ASP A 286 ? 0.33243 0.45070 0.26534 0.00088  -0.05045 0.00201  272 ASP A O   
2260 C CB  . ASP A 286 ? 0.46074 0.57054 0.37055 -0.00077 -0.05041 -0.00016 272 ASP A CB  
2261 C CG  . ASP A 286 ? 0.79422 0.90019 0.68955 0.00063  -0.05195 0.00117  272 ASP A CG  
2262 O OD1 . ASP A 286 ? 0.71963 0.82513 0.60787 0.00501  -0.05429 0.00655  272 ASP A OD1 
2263 O OD2 . ASP A 286 ? 0.94715 1.05046 0.83820 -0.00265 -0.05057 -0.00302 272 ASP A OD2 
2264 N N   . ILE A 287 ? 0.23308 0.33591 0.16676 -0.00073 -0.04018 0.00393  273 ILE A N   
2265 C CA  . ILE A 287 ? 0.21863 0.32420 0.16438 -0.00287 -0.03826 0.00186  273 ILE A CA  
2266 C C   . ILE A 287 ? 0.19425 0.29580 0.14528 -0.00049 -0.03502 0.00632  273 ILE A C   
2267 O O   . ILE A 287 ? 0.19022 0.29517 0.15027 -0.00105 -0.03472 0.00563  273 ILE A O   
2268 C CB  . ILE A 287 ? 0.22136 0.32494 0.17186 -0.00830 -0.03419 -0.00352 273 ILE A CB  
2269 C CG1 . ILE A 287 ? 0.22636 0.32021 0.17383 -0.00951 -0.02894 -0.00256 273 ILE A CG1 
2270 C CG2 . ILE A 287 ? 0.22674 0.33620 0.17413 -0.01075 -0.03768 -0.00843 273 ILE A CG2 
2271 C CD1 . ILE A 287 ? 0.20046 0.29254 0.15394 -0.01466 -0.02458 -0.00692 273 ILE A CD1 
2272 N N   . LEU A 288 ? 0.18015 0.27445 0.12587 0.00220  -0.03253 0.01083  274 LEU A N   
2273 C CA  . LEU A 288 ? 0.20386 0.29397 0.15503 0.00413  -0.02888 0.01472  274 LEU A CA  
2274 C C   . LEU A 288 ? 0.25251 0.34835 0.20664 0.00839  -0.03214 0.01871  274 LEU A C   
2275 O O   . LEU A 288 ? 0.21097 0.30606 0.17275 0.00907  -0.02970 0.02041  274 LEU A O   
2276 C CB  . LEU A 288 ? 0.21374 0.29422 0.15874 0.00577  -0.02511 0.01817  274 LEU A CB  
2277 C CG  . LEU A 288 ? 0.22523 0.29774 0.17187 0.00207  -0.02009 0.01558  274 LEU A CG  
2278 C CD1 . LEU A 288 ? 0.19161 0.25479 0.13034 0.00416  -0.01754 0.01885  274 LEU A CD1 
2279 C CD2 . LEU A 288 ? 0.21909 0.29063 0.17691 0.00016  -0.01648 0.01489  274 LEU A CD2 
2280 N N   . GLY A 289 ? 0.22670 0.32809 0.17501 0.01139  -0.03755 0.02050  275 GLY A N   
2281 C CA  . GLY A 289 ? 0.19719 0.30384 0.14900 0.01583  -0.04057 0.02490  275 GLY A CA  
2282 C C   . GLY A 289 ? 0.20273 0.30293 0.15403 0.01966  -0.03645 0.03104  275 GLY A C   
2283 O O   . GLY A 289 ? 0.23930 0.33153 0.18485 0.01973  -0.03257 0.03254  275 GLY A O   
2284 N N   . GLN A 290 ? 0.19650 0.30024 0.15462 0.02285  -0.03720 0.03448  276 GLN A N   
2285 C CA  . GLN A 290 ? 0.18426 0.28284 0.14404 0.02658  -0.03297 0.04022  276 GLN A CA  
2286 C C   . GLN A 290 ? 0.20419 0.30392 0.17545 0.02590  -0.03082 0.03986  276 GLN A C   
2287 O O   . GLN A 290 ? 0.22450 0.33163 0.20164 0.02654  -0.03492 0.03912  276 GLN A O   
2288 C CB  . GLN A 290 ? 0.23911 0.34121 0.19455 0.03235  -0.03637 0.04606  276 GLN A CB  
2289 C CG  . GLN A 290 ? 0.26118 0.36173 0.20417 0.03342  -0.03840 0.04714  276 GLN A CG  
2290 C CD  . GLN A 290 ? 0.54787 0.65259 0.48645 0.03920  -0.04214 0.05307  276 GLN A CD  
2291 O OE1 . GLN A 290 ? 0.66883 0.76897 0.60601 0.04304  -0.03859 0.05858  276 GLN A OE1 
2292 N NE2 . GLN A 290 ? 0.68797 0.80156 0.62465 0.03983  -0.04926 0.05188  276 GLN A NE2 
2293 N N   . HIS A 291 ? 0.21042 0.30288 0.18516 0.02446  -0.02454 0.04010  277 HIS A N   
2294 C CA  . HIS A 291 ? 0.20312 0.29570 0.18794 0.02312  -0.02196 0.03936  277 HIS A CA  
2295 C C   . HIS A 291 ? 0.17679 0.26243 0.16423 0.02502  -0.01569 0.04330  277 HIS A C   
2296 O O   . HIS A 291 ? 0.15510 0.23400 0.13891 0.02427  -0.01183 0.04330  277 HIS A O   
2297 C CB  . HIS A 291 ? 0.19675 0.28816 0.18464 0.01725  -0.02052 0.03326  277 HIS A CB  
2298 C CG  . HIS A 291 ? 0.16059 0.25811 0.14643 0.01472  -0.02556 0.02852  277 HIS A CG  
2299 N ND1 . HIS A 291 ? 0.18196 0.28700 0.17370 0.01441  -0.02981 0.02640  277 HIS A ND1 
2300 C CD2 . HIS A 291 ? 0.17570 0.27279 0.15497 0.01225  -0.02675 0.02522  277 HIS A CD2 
2301 C CE1 . HIS A 291 ? 0.19063 0.29989 0.17954 0.01184  -0.03332 0.02196  277 HIS A CE1 
2302 N NE2 . HIS A 291 ? 0.23556 0.34009 0.21669 0.01047  -0.03143 0.02120  277 HIS A NE2 
2303 N N   A SER A 292 ? 0.20285 0.29003 0.19723 0.02740  -0.01460 0.04632  278 SER A N   
2304 N N   B SER A 292 ? 0.20297 0.29022 0.19737 0.02740  -0.01465 0.04630  278 SER A N   
2305 C CA  A SER A 292 ? 0.17430 0.25532 0.17244 0.02873  -0.00809 0.04946  278 SER A CA  
2306 C CA  B SER A 292 ? 0.17453 0.25569 0.17294 0.02862  -0.00815 0.04934  278 SER A CA  
2307 C C   A SER A 292 ? 0.16991 0.24681 0.17366 0.02394  -0.00375 0.04571  278 SER A C   
2308 C C   B SER A 292 ? 0.17010 0.24678 0.17336 0.02369  -0.00377 0.04539  278 SER A C   
2309 O O   A SER A 292 ? 0.17112 0.25054 0.17736 0.02030  -0.00579 0.04180  278 SER A O   
2310 O O   B SER A 292 ? 0.17654 0.25531 0.18138 0.01973  -0.00573 0.04110  278 SER A O   
2311 C CB  A SER A 292 ? 0.17876 0.26268 0.18238 0.03287  -0.00812 0.05411  278 SER A CB  
2312 C CB  B SER A 292 ? 0.17412 0.25834 0.17905 0.03207  -0.00818 0.05332  278 SER A CB  
2313 O OG  A SER A 292 ? 0.17215 0.26111 0.17137 0.03734  -0.01303 0.05750  278 SER A OG  
2314 O OG  B SER A 292 ? 0.24294 0.33103 0.25443 0.02958  -0.01053 0.05031  278 SER A OG  
2315 N N   . ARG A 293 ? 0.14913 0.21985 0.15524 0.02406  0.00219  0.04661  279 ARG A N   
2316 C CA  . ARG A 293 ? 0.12202 0.18935 0.13469 0.02005  0.00630  0.04327  279 ARG A CA  
2317 C C   . ARG A 293 ? 0.28330 0.35236 0.30184 0.01888  0.00707  0.04425  279 ARG A C   
2318 O O   . ARG A 293 ? 0.18992 0.26014 0.21067 0.02227  0.00758  0.04839  279 ARG A O   
2319 C CB  . ARG A 293 ? 0.15459 0.21631 0.17085 0.02176  0.01154  0.04354  279 ARG A CB  
2320 C CG  . ARG A 293 ? 0.23233 0.28434 0.25260 0.01762  0.01200  0.03727  279 ARG A CG  
2321 C CD  . ARG A 293 ? 0.52252 0.56535 0.54423 0.01905  0.01467  0.03598  279 ARG A CD  
2322 N NE  . ARG A 293 ? 0.38937 0.42156 0.41110 0.01512  0.01260  0.02863  279 ARG A NE  
2323 C CZ  . ARG A 293 ? 0.38188 0.41086 0.40544 0.01361  0.01229  0.02650  279 ARG A CZ  
2324 N NH1 . ARG A 293 ? 0.28782 0.32195 0.31396 0.01481  0.01452  0.03144  279 ARG A NH1 
2325 N NH2 . ARG A 293 ? 0.30069 0.32600 0.32626 0.01460  0.01466  0.03211  279 ARG A NH2 
2326 N N   . LYS A 294 ? 0.11994 0.18795 0.14012 0.01402  0.00708  0.04068  280 LYS A N   
2327 C CA  . LYS A 294 ? 0.09407 0.16044 0.11699 0.01248  0.00665  0.04128  280 LYS A CA  
2328 C C   . LYS A 294 ? 0.19572 0.24567 0.21868 0.01023  0.00842  0.03668  280 LYS A C   
2329 O O   . LYS A 294 ? 0.17408 0.21358 0.19398 0.00805  0.00833  0.02973  280 LYS A O   
2330 C CB  . LYS A 294 ? 0.09605 0.16367 0.11716 0.00922  0.00199  0.03645  280 LYS A CB  
2331 C CG  . LYS A 294 ? 0.17665 0.25327 0.19618 0.01076  -0.00403 0.03417  280 LYS A CG  
2332 C CD  . LYS A 294 ? 0.19786 0.28101 0.22058 0.01588  -0.00765 0.03757  280 LYS A CD  
2333 C CE  . LYS A 294 ? 0.13825 0.22984 0.15935 0.01677  -0.01445 0.03511  280 LYS A CE  
2334 N NZ  . LYS A 294 ? 0.19287 0.28400 0.20545 0.01641  -0.01509 0.03456  280 LYS A NZ  
2335 N N   . ARG A 295 ? 0.13429 0.18318 0.16112 0.01099  0.00941  0.03968  281 ARG A N   
2336 C CA  . ARG A 295 ? 0.17687 0.21108 0.20190 0.00887  0.00971  0.03441  281 ARG A CA  
2337 C C   . ARG A 295 ? 0.12539 0.15389 0.14823 0.00662  0.00664  0.03039  281 ARG A C   
2338 O O   . ARG A 295 ? 0.13516 0.17247 0.16168 0.00620  0.00555  0.03381  281 ARG A O   
2339 C CB  . ARG A 295 ? 0.12889 0.16522 0.16036 0.01090  0.01203  0.03933  281 ARG A CB  
2340 C CG  . ARG A 295 ? 0.20563 0.24845 0.24041 0.01472  0.01546  0.04455  281 ARG A CG  
2341 C CD  . ARG A 295 ? 0.28492 0.32879 0.32604 0.01677  0.01805  0.04947  281 ARG A CD  
2342 N NE  . ARG A 295 ? 0.43711 0.46852 0.47614 0.01356  0.01803  0.04316  281 ARG A NE  
2343 C CZ  . ARG A 295 ? 0.51345 0.54167 0.55547 0.01246  0.01719  0.04289  281 ARG A CZ  
2344 N NH1 . ARG A 295 ? 0.30381 0.34049 0.35286 0.01376  0.01664  0.04868  281 ARG A NH1 
2345 N NH2 . ARG A 295 ? 0.53283 0.55067 0.57100 0.01016  0.01666  0.03698  281 ARG A NH2 
2346 N N   . TRP A 296 ? 0.14657 0.17125 0.17213 0.00622  0.00634  0.02248  282 TRP A N   
2347 C CA  . TRP A 296 ? 0.15012 0.17025 0.17333 0.00430  0.00466  0.01902  282 TRP A CA  
2348 C C   . TRP A 296 ? 0.14048 0.15601 0.16436 0.00436  0.00449  0.02266  282 TRP A C   
2349 O O   . TRP A 296 ? 0.13450 0.15079 0.16027 0.00322  0.00363  0.02213  282 TRP A O   
2350 C CB  . TRP A 296 ? 0.16927 0.17854 0.18628 0.00376  0.00472  0.01682  282 TRP A CB  
2351 C CG  . TRP A 296 ? 0.09276 0.10696 0.11103 0.00416  0.00478  0.01455  282 TRP A CG  
2352 C CD1 . TRP A 296 ? 0.14648 0.15580 0.16124 0.00502  0.00590  0.01675  282 TRP A CD1 
2353 C CD2 . TRP A 296 ? 0.10042 0.11535 0.11525 0.00283  0.00282  0.01302  282 TRP A CD2 
2354 N NE1 . TRP A 296 ? 0.12441 0.13836 0.14054 0.00516  0.00558  0.01411  282 TRP A NE1 
2355 C CE2 . TRP A 296 ? 0.12199 0.13332 0.13233 0.00314  0.00303  0.01396  282 TRP A CE2 
2356 C CE3 . TRP A 296 ? 0.10569 0.12132 0.11797 0.00111  0.00096  0.01175  282 TRP A CE3 
2357 C CZ2 . TRP A 296 ? 0.10336 0.11588 0.11111 0.00206  0.00170  0.01233  282 TRP A CZ2 
2358 C CZ3 . TRP A 296 ? 0.13336 0.14729 0.13897 -0.00027 -0.00018 0.01096  282 TRP A CZ3 
2359 C CH2 . TRP A 296 ? 0.10470 0.11852 0.11014 0.00020  0.00014  0.01077  282 TRP A CH2 
2360 N N   . GLU A 297 ? 0.15449 0.16989 0.18191 0.00544  0.00629  0.02528  283 GLU A N   
2361 C CA  . GLU A 297 ? 0.14926 0.16596 0.18405 0.00549  0.00729  0.02787  283 GLU A CA  
2362 C C   . GLU A 297 ? 0.14609 0.17450 0.18775 0.00502  0.00618  0.03196  283 GLU A C   
2363 O O   . GLU A 297 ? 0.17076 0.20083 0.21792 0.00414  0.00579  0.02828  283 GLU A O   
2364 C CB  . GLU A 297 ? 0.16557 0.18170 0.20338 0.00681  0.00966  0.03049  283 GLU A CB  
2365 C CG  . GLU A 297 ? 0.21456 0.22261 0.24766 0.00647  0.01038  0.02553  283 GLU A CG  
2366 C CD  . GLU A 297 ? 0.43993 0.45642 0.47663 0.00810  0.01231  0.02340  283 GLU A CD  
2367 O OE1 . GLU A 297 ? 0.27044 0.29028 0.30513 0.00845  0.01136  0.02470  283 GLU A OE1 
2368 O OE2 . GLU A 297 ? 0.32026 0.33368 0.35679 0.00784  0.01457  0.02240  283 GLU A OE2 
2369 N N   . ASN A 298 ? 0.11471 0.15344 0.15476 0.00527  0.00465  0.03236  284 ASN A N   
2370 C CA  . ASN A 298 ? 0.11544 0.16719 0.16092 0.00511  0.00132  0.02803  284 ASN A CA  
2371 C C   . ASN A 298 ? 0.13131 0.18200 0.17666 0.00190  -0.00005 0.02066  284 ASN A C   
2372 O O   . ASN A 298 ? 0.13875 0.19809 0.19051 0.00149  -0.00244 0.01647  284 ASN A O   
2373 C CB  . ASN A 298 ? 0.16172 0.22244 0.20433 0.00657  -0.00086 0.02945  284 ASN A CB  
2374 C CG  . ASN A 298 ? 0.25315 0.31754 0.29698 0.01058  0.00033  0.03583  284 ASN A CG  
2375 O OD1 . ASN A 298 ? 0.24350 0.30402 0.29088 0.01194  0.00319  0.03944  284 ASN A OD1 
2376 N ND2 . ASN A 298 ? 0.21519 0.28642 0.25576 0.01267  -0.00168 0.03717  284 ASN A ND2 
2377 N N   . PHE A 299 ? 0.11035 0.15059 0.14905 0.00012  0.00121  0.01876  285 PHE A N   
2378 C CA  . PHE A 299 ? 0.11932 0.15839 0.15723 -0.00257 0.00076  0.01170  285 PHE A CA  
2379 C C   . PHE A 299 ? 0.11455 0.14848 0.15514 -0.00308 0.00227  0.00909  285 PHE A C   
2380 O O   . PHE A 299 ? 0.10214 0.13645 0.14144 -0.00516 0.00243  0.00377  285 PHE A O   
2381 C CB  . PHE A 299 ? 0.13618 0.16839 0.16524 -0.00357 0.00089  0.01026  285 PHE A CB  
2382 C CG  . PHE A 299 ? 0.06314 0.10103 0.08797 -0.00361 -0.00057 0.01267  285 PHE A CG  
2383 C CD1 . PHE A 299 ? 0.15672 0.20241 0.18215 -0.00523 -0.00226 0.00961  285 PHE A CD1 
2384 C CD2 . PHE A 299 ? 0.13705 0.17238 0.15712 -0.00169 -0.00022 0.01838  285 PHE A CD2 
2385 C CE1 . PHE A 299 ? 0.14768 0.19916 0.16824 -0.00525 -0.00335 0.01149  285 PHE A CE1 
2386 C CE2 . PHE A 299 ? 0.16204 0.20338 0.17742 -0.00176 -0.00089 0.02050  285 PHE A CE2 
2387 C CZ  . PHE A 299 ? 0.16491 0.21463 0.18047 -0.00364 -0.00233 0.01673  285 PHE A CZ  
2388 N N   . ILE A 300 ? 0.12169 0.15065 0.16547 -0.00110 0.00359  0.01340  286 ILE A N   
2389 C CA  . ILE A 300 ? 0.12013 0.14218 0.16674 -0.00098 0.00505  0.01183  286 ILE A CA  
2390 C C   . ILE A 300 ? 0.16963 0.20248 0.22385 -0.00209 0.00436  0.00943  286 ILE A C   
2391 O O   . ILE A 300 ? 0.17922 0.22275 0.23948 -0.00103 0.00314  0.01116  286 ILE A O   
2392 C CB  . ILE A 300 ? 0.19149 0.20374 0.23994 0.00167  0.00697  0.01692  286 ILE A CB  
2393 C CG1 . ILE A 300 ? 0.12363 0.12792 0.16292 0.00290  0.00691  0.01615  286 ILE A CG1 
2394 C CG2 . ILE A 300 ? 0.16238 0.16755 0.21502 0.00207  0.00862  0.01480  286 ILE A CG2 
2395 C CD1 . ILE A 300 ? 0.14536 0.14733 0.18081 0.00375  0.00772  0.01602  286 ILE A CD1 
2396 N N   . HIS A 301 ? 0.06096 0.09076 0.11538 -0.00340 0.00493  0.00552  287 HIS A N   
2397 C CA  . HIS A 301 ? 0.12089 0.15858 0.18317 -0.00403 0.00461  0.00404  287 HIS A CA  
2398 C C   . HIS A 301 ? 0.13202 0.15789 0.19452 -0.00394 0.00673  0.00151  287 HIS A C   
2399 O O   . HIS A 301 ? 0.11967 0.13271 0.17653 -0.00274 0.00818  0.00033  287 HIS A O   
2400 C CB  . HIS A 301 ? 0.11815 0.17131 0.18214 -0.00587 0.00204  0.00136  287 HIS A CB  
2401 C CG  . HIS A 301 ? 0.20410 0.25346 0.26257 -0.00814 0.00186  -0.00089 287 HIS A CG  
2402 N ND1 . HIS A 301 ? 0.22237 0.26743 0.27286 -0.00875 0.00161  -0.00073 287 HIS A ND1 
2403 C CD2 . HIS A 301 ? 0.36160 0.40909 0.42257 -0.00929 0.00209  -0.00400 287 HIS A CD2 
2404 C CE1 . HIS A 301 ? 0.14581 0.18550 0.19421 -0.00967 0.00195  -0.00434 287 HIS A CE1 
2405 N NE2 . HIS A 301 ? 0.44745 0.48881 0.50167 -0.01006 0.00241  -0.00688 287 HIS A NE2 
2406 N N   . SER A 302 ? 0.14961 0.18021 0.21922 -0.00455 0.00688  -0.00004 288 SER A N   
2407 C CA  . SER A 302 ? 0.13131 0.15051 0.20230 -0.00388 0.00938  -0.00269 288 SER A CA  
2408 C C   . SER A 302 ? 0.15848 0.16849 0.22210 -0.00379 0.01047  -0.00769 288 SER A C   
2409 O O   . SER A 302 ? 0.22134 0.22026 0.28286 -0.00195 0.01273  -0.00990 288 SER A O   
2410 C CB  . SER A 302 ? 0.13389 0.16024 0.21416 -0.00463 0.00944  -0.00370 288 SER A CB  
2411 O OG  . SER A 302 ? 0.23595 0.27168 0.31721 -0.00655 0.00765  -0.00655 288 SER A OG  
2412 N N   . GLU A 303 ? 0.13674 0.15199 0.19616 -0.00531 0.00906  -0.00963 289 GLU A N   
2413 C CA  . GLU A 303 ? 0.20578 0.21351 0.25848 -0.00471 0.01059  -0.01470 289 GLU A CA  
2414 C C   . GLU A 303 ? 0.18392 0.18483 0.22646 -0.00294 0.01060  -0.01339 289 GLU A C   
2415 O O   . GLU A 303 ? 0.30371 0.30312 0.33553 -0.00253 0.00978  -0.01256 289 GLU A O   
2416 C CB  . GLU A 303 ? 0.22261 0.23840 0.27433 -0.00694 0.00932  -0.01692 289 GLU A CB  
2417 C CG  . GLU A 303 ? 0.35965 0.38309 0.41971 -0.00857 0.00884  -0.01835 289 GLU A CG  
2418 C CD  . GLU A 303 ? 0.59783 0.63118 0.65882 -0.01075 0.00677  -0.01945 289 GLU A CD  
2419 O OE1 . GLU A 303 ? 0.44825 0.48500 0.50503 -0.01131 0.00506  -0.01748 289 GLU A OE1 
2420 O OE2 . GLU A 303 ? 0.33012 0.36760 0.39652 -0.01183 0.00688  -0.02245 289 GLU A OE2 
2421 N N   . ASN A 304 ? 0.12609 0.12623 0.16942 -0.00223 0.00991  -0.01028 290 ASN A N   
2422 C CA  . ASN A 304 ? 0.11719 0.11522 0.14780 -0.00129 0.00832  -0.00742 290 ASN A CA  
2423 C C   . ASN A 304 ? 0.14646 0.14204 0.17447 -0.00100 0.00764  -0.00391 290 ASN A C   
2424 O O   . ASN A 304 ? 0.12763 0.12824 0.15430 -0.00083 0.00826  -0.00291 290 ASN A O   
2425 C CB  . ASN A 304 ? 0.09192 0.09144 0.12185 -0.00176 0.00788  -0.00786 290 ASN A CB  
2426 C CG  . ASN A 304 ? 0.11074 0.11769 0.14628 -0.00298 0.00652  -0.00321 290 ASN A CG  
2427 O OD1 . ASN A 304 ? 0.11624 0.12231 0.15668 -0.00190 0.00690  0.00011  290 ASN A OD1 
2428 N ND2 . ASN A 304 ? 0.10226 0.11843 0.13552 -0.00520 0.00477  -0.00221 290 ASN A ND2 
2429 N N   . ARG A 305 ? 0.10986 0.10565 0.14566 0.00008  0.00895  -0.00282 291 ARG A N   
2430 C CA  . ARG A 305 ? 0.10858 0.10282 0.14328 0.00004  0.00902  0.00015  291 ARG A CA  
2431 C C   . ARG A 305 ? 0.15121 0.15146 0.18572 -0.00026 0.01094  -0.00091 291 ARG A C   
2432 O O   . ARG A 305 ? 0.15363 0.15350 0.18667 0.00009  0.01125  0.00030  291 ARG A O   
2433 C CB  . ARG A 305 ? 0.13760 0.13233 0.18215 0.00107  0.01062  0.00157  291 ARG A CB  
2434 C CG  . ARG A 305 ? 0.38257 0.38447 0.42980 0.00100  0.01210  0.00413  291 ARG A CG  
2435 C CD  . ARG A 305 ? 0.57038 0.56485 0.62590 0.00208  0.01310  0.00690  291 ARG A CD  
2436 N NE  . ARG A 305 ? 0.67651 0.67453 0.74580 0.00182  0.01344  0.00929  291 ARG A NE  
2437 C CZ  . ARG A 305 ? 0.56706 0.57293 0.64023 0.00195  0.01243  0.01402  291 ARG A CZ  
2438 N NH1 . ARG A 305 ? 0.47702 0.47960 0.54828 0.00341  0.01314  0.01912  291 ARG A NH1 
2439 N NH2 . ARG A 305 ? 0.29737 0.31774 0.37396 0.00066  0.01027  0.01259  291 ARG A NH2 
2440 N N   . HIS A 306 ? 0.16434 0.15792 0.19509 -0.00102 0.01058  -0.00328 292 HIS A N   
2441 C CA  . HIS A 306 ? 0.15178 0.14487 0.18011 -0.00137 0.01137  -0.00389 292 HIS A CA  
2442 C C   . HIS A 306 ? 0.21677 0.21045 0.23999 -0.00144 0.01034  -0.00378 292 HIS A C   
2443 O O   . HIS A 306 ? 0.17221 0.16546 0.19371 -0.00160 0.01076  -0.00387 292 HIS A O   
2444 C CB  . HIS A 306 ? 0.12809 0.12758 0.15969 -0.00195 0.01333  -0.00534 292 HIS A CB  
2445 C CG  . HIS A 306 ? 0.12587 0.12600 0.15489 -0.00246 0.01246  -0.00665 292 HIS A CG  
2446 N ND1 . HIS A 306 ? 0.19917 0.20023 0.22984 -0.00251 0.01181  -0.00736 292 HIS A ND1 
2447 C CD2 . HIS A 306 ? 0.15889 0.15340 0.18188 -0.00324 0.01113  -0.00799 292 HIS A CD2 
2448 C CE1 . HIS A 306 ? 0.21538 0.21701 0.24331 -0.00308 0.01149  -0.00859 292 HIS A CE1 
2449 N NE2 . HIS A 306 ? 0.16337 0.16111 0.19420 -0.00453 0.01458  -0.01138 292 HIS A NE2 
2450 N N   . LEU A 307 ? 0.14098 0.13557 0.16200 -0.00135 0.00904  -0.00364 293 LEU A N   
2451 C CA  . LEU A 307 ? 0.11904 0.11816 0.13730 -0.00127 0.00878  -0.00316 293 LEU A CA  
2452 C C   . LEU A 307 ? 0.17052 0.16565 0.18675 -0.00078 0.00762  -0.00196 293 LEU A C   
2453 O O   . LEU A 307 ? 0.12696 0.12566 0.14135 -0.00072 0.00754  -0.00169 293 LEU A O   
2454 C CB  . LEU A 307 ? 0.07949 0.07565 0.09395 -0.00175 0.00708  -0.00430 293 LEU A CB  
2455 C CG  . LEU A 307 ? 0.11328 0.10967 0.12832 -0.00244 0.00765  -0.00583 293 LEU A CG  
2456 C CD1 . LEU A 307 ? 0.14320 0.14408 0.15811 -0.00261 0.00782  -0.00610 293 LEU A CD1 
2457 C CD2 . LEU A 307 ? 0.16340 0.15944 0.17697 -0.00271 0.00800  -0.00586 293 LEU A CD2 
2458 N N   . VAL A 308 ? 0.16495 0.15973 0.18462 -0.00021 0.00811  -0.00059 294 VAL A N   
2459 C CA  . VAL A 308 ? 0.13997 0.13494 0.15983 0.00044  0.00793  0.00127  294 VAL A CA  
2460 C C   . VAL A 308 ? 0.15399 0.15304 0.17830 0.00080  0.01034  0.00217  294 VAL A C   
2461 O O   . VAL A 308 ? 0.19179 0.19080 0.21967 0.00084  0.01163  0.00232  294 VAL A O   
2462 C CB  . VAL A 308 ? 0.11003 0.10575 0.13233 0.00093  0.00731  0.00312  294 VAL A CB  
2463 C CG1 . VAL A 308 ? 0.12840 0.12966 0.15288 0.00152  0.00791  0.00513  294 VAL A CG1 
2464 C CG2 . VAL A 308 ? 0.11849 0.11475 0.13866 0.00044  0.00608  0.00157  294 VAL A CG2 
2465 N N   . SER A 309 ? 0.10539 0.10419 0.12818 0.00108  0.01053  0.00276  295 SER A N   
2466 C CA  . SER A 309 ? 0.12621 0.12456 0.15123 0.00150  0.01240  0.00364  295 SER A CA  
2467 C C   . SER A 309 ? 0.14613 0.13933 0.16895 0.00240  0.01156  0.00573  295 SER A C   
2468 O O   . SER A 309 ? 0.11088 0.10510 0.13138 0.00235  0.01023  0.00568  295 SER A O   
2469 C CB  . SER A 309 ? 0.17452 0.17179 0.19701 0.00091  0.01271  0.00201  295 SER A CB  
2470 O OG  . SER A 309 ? 0.15405 0.14689 0.17070 0.00059  0.01019  0.00125  295 SER A OG  
2471 N N   . PRO A 310 ? 0.15903 0.15766 0.18700 0.00291  0.01475  0.00677  296 PRO A N   
2472 C CA  . PRO A 310 ? 0.16656 0.15901 0.19176 0.00402  0.01403  0.00900  296 PRO A CA  
2473 C C   . PRO A 310 ? 0.14351 0.14143 0.16673 0.00309  0.01430  0.00649  296 PRO A C   
2474 O O   . PRO A 310 ? 0.15576 0.14882 0.17564 0.00374  0.01245  0.00778  296 PRO A O   
2475 C CB  . PRO A 310 ? 0.17638 0.16729 0.20477 0.00481  0.01658  0.01044  296 PRO A CB  
2476 C CG  . PRO A 310 ? 0.17344 0.16418 0.20509 0.00474  0.01714  0.01083  296 PRO A CG  
2477 C CD  . PRO A 310 ? 0.16443 0.16275 0.19646 0.00319  0.01684  0.00744  296 PRO A CD  
2478 N N   . GLU A 311 ? 0.13689 0.13372 0.15790 0.00225  0.01394  0.00451  297 GLU A N   
2479 C CA  . GLU A 311 ? 0.12686 0.12314 0.14406 0.00170  0.01276  0.00320  297 GLU A CA  
2480 C C   . GLU A 311 ? 0.10201 0.09522 0.11501 0.00142  0.00953  0.00269  297 GLU A C   
2481 O O   . GLU A 311 ? 0.12044 0.11399 0.13165 0.00141  0.00886  0.00256  297 GLU A O   
2482 C CB  . GLU A 311 ? 0.18955 0.18515 0.20554 0.00101  0.01278  0.00182  297 GLU A CB  
2483 C CG  . GLU A 311 ? 0.43303 0.42250 0.44986 0.00135  0.01384  0.00241  297 GLU A CG  
2484 C CD  . GLU A 311 ? 0.51029 0.50499 0.53249 0.00161  0.01675  0.00299  297 GLU A CD  
2485 O OE1 . GLU A 311 ? 0.17992 0.16948 0.20075 0.00159  0.01453  0.00309  297 GLU A OE1 
2486 O OE2 . GLU A 311 ? 0.64074 0.62795 0.66352 0.00225  0.01744  0.00416  297 GLU A OE2 
2487 N N   . ALA A 312 ? 0.10072 0.09466 0.11352 0.00107  0.00860  0.00213  298 ALA A N   
2488 C CA  . ALA A 312 ? 0.07406 0.06924 0.08436 0.00070  0.00681  0.00140  298 ALA A CA  
2489 C C   . ALA A 312 ? 0.06625 0.06199 0.07702 0.00124  0.00659  0.00262  298 ALA A C   
2490 O O   . ALA A 312 ? 0.11293 0.11158 0.12215 0.00093  0.00600  0.00189  298 ALA A O   
2491 C CB  . ALA A 312 ? 0.06446 0.05999 0.07507 0.00037  0.00639  0.00079  298 ALA A CB  
2492 N N   . LEU A 313 ? 0.10258 0.09836 0.11672 0.00208  0.00770  0.00473  299 LEU A N   
2493 C CA  . LEU A 313 ? 0.10674 0.10382 0.12181 0.00285  0.00754  0.00687  299 LEU A CA  
2494 C C   . LEU A 313 ? 0.09996 0.10054 0.11596 0.00313  0.00923  0.00685  299 LEU A C   
2495 O O   . LEU A 313 ? 0.11446 0.11229 0.12776 0.00367  0.00766  0.00805  299 LEU A O   
2496 C CB  . LEU A 313 ? 0.11911 0.11718 0.13830 0.00381  0.00855  0.01000  299 LEU A CB  
2497 C CG  . LEU A 313 ? 0.15017 0.15353 0.17318 0.00307  0.00868  0.00917  299 LEU A CG  
2498 C CD1 . LEU A 313 ? 0.18148 0.18758 0.20951 0.00401  0.00974  0.01279  299 LEU A CD1 
2499 C CD2 . LEU A 313 ? 0.18248 0.18213 0.20041 0.00264  0.00582  0.00891  299 LEU A CD2 
2500 N N   . ASP A 314 ? 0.12646 0.12295 0.14722 0.00454  0.01347  0.00923  300 ASP A N   
2501 C CA  . ASP A 314 ? 0.12935 0.12374 0.14376 0.00414  0.01075  0.00776  300 ASP A CA  
2502 C C   . ASP A 314 ? 0.09733 0.09177 0.10829 0.00314  0.00916  0.00554  300 ASP A C   
2503 O O   . ASP A 314 ? 0.11037 0.10493 0.12056 0.00356  0.00923  0.00603  300 ASP A O   
2504 C CB  . ASP A 314 ? 0.10401 0.09746 0.12557 0.00545  0.01733  0.00981  300 ASP A CB  
2505 C CG  . ASP A 314 ? 0.21151 0.20364 0.23260 0.00632  0.01922  0.01067  300 ASP A CG  
2506 O OD1 . ASP A 314 ? 0.18920 0.18086 0.20601 0.00655  0.01531  0.01106  300 ASP A OD1 
2507 O OD2 . ASP A 314 ? 0.16949 0.15985 0.18312 0.00426  0.01381  0.00685  300 ASP A OD2 
2508 N N   . LEU A 315 ? 0.08339 0.07789 0.09242 0.00200  0.00788  0.00345  301 LEU A N   
2509 C CA  . LEU A 315 ? 0.07828 0.07342 0.08445 0.00121  0.00627  0.00194  301 LEU A CA  
2510 C C   . LEU A 315 ? 0.09701 0.09330 0.10207 0.00111  0.00496  0.00181  301 LEU A C   
2511 O O   . LEU A 315 ? 0.11041 0.10839 0.11476 0.00096  0.00498  0.00147  301 LEU A O   
2512 C CB  . LEU A 315 ? 0.08890 0.08454 0.09376 0.00047  0.00526  0.00074  301 LEU A CB  
2513 C CG  . LEU A 315 ? 0.09907 0.09590 0.10171 0.00001  0.00356  0.00001  301 LEU A CG  
2514 C CD1 . LEU A 315 ? 0.08499 0.08133 0.08739 0.00004  0.00393  0.00005  301 LEU A CD1 
2515 C CD2 . LEU A 315 ? 0.12245 0.12077 0.12468 -0.00024 0.00320  -0.00033 301 LEU A CD2 
2516 N N   . LEU A 316 ? 0.08521 0.08388 0.09119 0.00098  0.00484  0.00176  302 LEU A N   
2517 C CA  . LEU A 316 ? 0.08583 0.08512 0.09062 0.00084  0.00353  0.00159  302 LEU A CA  
2518 C C   . LEU A 316 ? 0.09949 0.09790 0.10510 0.00177  0.00391  0.00345  302 LEU A C   
2519 O O   . LEU A 316 ? 0.10806 0.10697 0.11228 0.00153  0.00306  0.00292  302 LEU A O   
2520 C CB  . LEU A 316 ? 0.06916 0.06811 0.07638 0.00117  0.00404  0.00263  302 LEU A CB  
2521 C CG  . LEU A 316 ? 0.10074 0.10021 0.10459 0.00068  0.00171  0.00179  302 LEU A CG  
2522 C CD1 . LEU A 316 ? 0.11749 0.11735 0.11804 0.00002  0.00042  0.00004  302 LEU A CD1 
2523 C CD2 . LEU A 316 ? 0.05796 0.05927 0.06410 0.00072  0.00183  0.00260  302 LEU A CD2 
2524 N N   . ASP A 317 ? 0.08937 0.08908 0.10099 0.00373  0.00774  0.00745  303 ASP A N   
2525 C CA  . ASP A 317 ? 0.11449 0.11441 0.12407 0.00439  0.00654  0.00865  303 ASP A CA  
2526 C C   . ASP A 317 ? 0.09422 0.09248 0.10215 0.00443  0.00707  0.00757  303 ASP A C   
2527 O O   . ASP A 317 ? 0.13377 0.13312 0.14156 0.00540  0.00738  0.00895  303 ASP A O   
2528 C CB  . ASP A 317 ? 0.10445 0.10490 0.11703 0.00595  0.00852  0.01180  303 ASP A CB  
2529 C CG  . ASP A 317 ? 0.23671 0.23929 0.25018 0.00799  0.00982  0.01518  303 ASP A CG  
2530 O OD1 . ASP A 317 ? 0.12511 0.13618 0.14181 0.00846  0.01015  0.01539  303 ASP A OD1 
2531 O OD2 . ASP A 317 ? 0.29520 0.30101 0.31150 0.00845  0.01381  0.01480  303 ASP A OD2 
2532 N N   . LYS A 318 ? 0.07257 0.07138 0.08008 0.00321  0.00801  0.00505  304 LYS A N   
2533 C CA  . LYS A 318 ? 0.09028 0.08514 0.09561 0.00333  0.00759  0.00470  304 LYS A CA  
2534 C C   . LYS A 318 ? 0.08367 0.07910 0.08668 0.00201  0.00561  0.00263  304 LYS A C   
2535 O O   . LYS A 318 ? 0.14033 0.13666 0.14260 0.00171  0.00644  0.00204  304 LYS A O   
2536 C CB  . LYS A 318 ? 0.10266 0.09604 0.10832 0.00310  0.00862  0.00428  304 LYS A CB  
2537 C CG  . LYS A 318 ? 0.12377 0.11979 0.13275 0.00421  0.01231  0.00602  304 LYS A CG  
2538 C CD  . LYS A 318 ? 0.17493 0.16555 0.18670 0.00522  0.01658  0.00740  304 LYS A CD  
2539 C CE  . LYS A 318 ? 0.12741 0.11691 0.13853 0.00571  0.01480  0.00825  304 LYS A CE  
2540 N NZ  . LYS A 318 ? 0.21219 0.20051 0.22429 0.00518  0.01562  0.00756  304 LYS A NZ  
2541 N N   . LEU A 319 ? 0.10048 0.09732 0.10269 0.00120  0.00380  0.00159  305 LEU A N   
2542 C CA  . LEU A 319 ? 0.10182 0.10039 0.10249 0.00030  0.00216  0.00034  305 LEU A CA  
2543 C C   . LEU A 319 ? 0.11092 0.10947 0.11135 0.00036  0.00147  0.00041  305 LEU A C   
2544 O O   . LEU A 319 ? 0.11132 0.11016 0.11120 0.00013  0.00133  0.00012  305 LEU A O   
2545 C CB  . LEU A 319 ? 0.11312 0.11264 0.11329 -0.00001 0.00067  -0.00002 305 LEU A CB  
2546 C CG  . LEU A 319 ? 0.14550 0.14450 0.14578 -0.00006 0.00095  -0.00007 305 LEU A CG  
2547 C CD1 . LEU A 319 ? 0.09615 0.09597 0.09621 -0.00003 0.00018  -0.00004 305 LEU A CD1 
2548 C CD2 . LEU A 319 ? 0.13949 0.13842 0.13959 -0.00012 0.00096  -0.00012 305 LEU A CD2 
2549 N N   . LEU A 320 ? 0.10623 0.10134 0.10244 -0.00191 0.00995  0.01009  306 LEU A N   
2550 C CA  . LEU A 320 ? 0.06463 0.06269 0.06171 -0.00034 0.00986  0.01079  306 LEU A CA  
2551 C C   . LEU A 320 ? 0.12582 0.12416 0.12500 0.00062  0.01172  0.01262  306 LEU A C   
2552 O O   . LEU A 320 ? 0.15435 0.15270 0.15400 0.00230  0.01268  0.01381  306 LEU A O   
2553 C CB  . LEU A 320 ? 0.11878 0.11748 0.11485 0.00114  0.00922  0.01053  306 LEU A CB  
2554 C CG  . LEU A 320 ? 0.08741 0.08603 0.08153 0.00012  0.00739  0.00884  306 LEU A CG  
2555 C CD1 . LEU A 320 ? 0.13405 0.13374 0.12814 0.00166  0.00702  0.00873  306 LEU A CD1 
2556 C CD2 . LEU A 320 ? 0.08771 0.08816 0.08237 -0.00084 0.00618  0.00814  306 LEU A CD2 
2557 N N   . ARG A 321 ? 0.08920 0.08777 0.08979 -0.00060 0.01232  0.01289  307 ARG A N   
2558 C CA  . ARG A 321 ? 0.10779 0.10658 0.11025 -0.00023 0.01411  0.01459  307 ARG A CA  
2559 C C   . ARG A 321 ? 0.08752 0.08881 0.09038 -0.00077 0.01381  0.01470  307 ARG A C   
2560 O O   . ARG A 321 ? 0.12833 0.13029 0.13108 -0.00206 0.01282  0.01329  307 ARG A O   
2561 C CB  . ARG A 321 ? 0.15901 0.15531 0.16339 -0.00166 0.01554  0.01461  307 ARG A CB  
2562 C CG  . ARG A 321 ? 0.27234 0.26556 0.27653 -0.00146 0.01623  0.01451  307 ARG A CG  
2563 C CD  . ARG A 321 ? 0.24881 0.23974 0.25575 -0.00290 0.01764  0.01465  307 ARG A CD  
2564 N NE  . ARG A 321 ? 0.48054 0.46823 0.48759 -0.00250 0.01880  0.01492  307 ARG A NE  
2565 C CZ  . ARG A 321 ? 0.49338 0.47853 0.50306 -0.00351 0.02018  0.01516  307 ARG A CZ  
2566 N NH1 . ARG A 321 ? 0.38953 0.37516 0.40226 -0.00490 0.02071  0.01523  307 ARG A NH1 
2567 N NH2 . ARG A 321 ? 0.53702 0.51899 0.54650 -0.00314 0.02114  0.01522  307 ARG A NH2 
2568 N N   . TYR A 322 ? 0.08620 0.08875 0.08944 0.00009  0.01483  0.01640  308 TYR A N   
2569 C CA  . TYR A 322 ? 0.07640 0.08097 0.07958 -0.00066 0.01493  0.01651  308 TYR A CA  
2570 C C   . TYR A 322 ? 0.12804 0.13186 0.13296 -0.00269 0.01605  0.01580  308 TYR A C   
2571 O O   . TYR A 322 ? 0.12453 0.12977 0.12959 -0.00379 0.01555  0.01459  308 TYR A O   
2572 C CB  . TYR A 322 ? 0.08598 0.09156 0.08895 0.00020  0.01619  0.01867  308 TYR A CB  
2573 C CG  . TYR A 322 ? 0.11171 0.11931 0.11380 0.00207  0.01507  0.01953  308 TYR A CG  
2574 C CD1 . TYR A 322 ? 0.09671 0.10683 0.09806 0.00241  0.01319  0.01858  308 TYR A CD1 
2575 C CD2 . TYR A 322 ? 0.08516 0.09245 0.08770 0.00348  0.01600  0.02141  308 TYR A CD2 
2576 C CE1 . TYR A 322 ? 0.12635 0.13894 0.12781 0.00403  0.01219  0.01939  308 TYR A CE1 
2577 C CE2 . TYR A 322 ? 0.09259 0.10227 0.09504 0.00513  0.01508  0.02225  308 TYR A CE2 
2578 C CZ  . TYR A 322 ? 0.11721 0.12969 0.11926 0.00535  0.01318  0.02123  308 TYR A CZ  
2579 O OH  . TYR A 322 ? 0.13555 0.15090 0.13820 0.00684  0.01232  0.02205  308 TYR A OH  
2580 N N   . ASP A 323 ? 0.11259 0.11439 0.11944 -0.00315 0.01774  0.01659  309 ASP A N   
2581 C CA  . ASP A 323 ? 0.07972 0.08113 0.08950 -0.00496 0.01909  0.01619  309 ASP A CA  
2582 C C   . ASP A 323 ? 0.05923 0.06040 0.07042 -0.00615 0.01769  0.01410  309 ASP A C   
2583 O O   . ASP A 323 ? 0.09401 0.09300 0.10598 -0.00639 0.01734  0.01360  309 ASP A O   
2584 C CB  . ASP A 323 ? 0.14750 0.14659 0.15940 -0.00503 0.02120  0.01761  309 ASP A CB  
2585 C CG  . ASP A 323 ? 0.16062 0.15962 0.17619 -0.00679 0.02293  0.01744  309 ASP A CG  
2586 O OD1 . ASP A 323 ? 0.18811 0.18849 0.20550 -0.00800 0.02228  0.01579  309 ASP A OD1 
2587 O OD2 . ASP A 323 ? 0.17579 0.17342 0.19281 -0.00692 0.02502  0.01898  309 ASP A OD2 
2588 N N   . HIS A 324 ? 0.11185 0.11525 0.12343 -0.00702 0.01690  0.01288  310 HIS A N   
2589 C CA  . HIS A 324 ? 0.09263 0.09626 0.10562 -0.00806 0.01523  0.01100  310 HIS A CA  
2590 C C   . HIS A 324 ? 0.11678 0.11865 0.13424 -0.00933 0.01583  0.01045  310 HIS A C   
2591 O O   . HIS A 324 ? 0.12610 0.12669 0.14427 -0.01004 0.01417  0.00923  310 HIS A O   
2592 C CB  . HIS A 324 ? 0.11058 0.11712 0.12413 -0.00868 0.01469  0.00993  310 HIS A CB  
2593 C CG  . HIS A 324 ? 0.15918 0.16709 0.17552 -0.00941 0.01681  0.01039  310 HIS A CG  
2594 N ND1 . HIS A 324 ? 0.19836 0.20720 0.21244 -0.00898 0.01821  0.01169  310 HIS A ND1 
2595 C CD2 . HIS A 324 ? 0.16157 0.16991 0.18300 -0.01058 0.01783  0.00964  310 HIS A CD2 
2596 C CE1 . HIS A 324 ? 0.16394 0.17384 0.18101 -0.01002 0.02020  0.01185  310 HIS A CE1 
2597 N NE2 . HIS A 324 ? 0.18230 0.19189 0.20414 -0.01088 0.02008  0.01056  310 HIS A NE2 
2598 N N   . GLN A 325 ? 0.10849 0.10996 0.12895 -0.00977 0.01807  0.01128  311 GLN A N   
2599 C CA  . GLN A 325 ? 0.16552 0.16520 0.19095 -0.01102 0.01874  0.01059  311 GLN A CA  
2600 C C   . GLN A 325 ? 0.13905 0.13539 0.16372 -0.01086 0.01855  0.01092  311 GLN A C   
2601 O O   . GLN A 325 ? 0.20075 0.19524 0.22881 -0.01210 0.01794  0.00970  311 GLN A O   
2602 C CB  . GLN A 325 ? 0.16749 0.16768 0.19610 -0.01154 0.02146  0.01150  311 GLN A CB  
2603 C CG  . GLN A 325 ? 0.33055 0.33011 0.36568 -0.01305 0.02197  0.01011  311 GLN A CG  
2604 C CD  . GLN A 325 ? 0.44411 0.44096 0.48148 -0.01344 0.02390  0.01115  311 GLN A CD  
2605 O OE1 . GLN A 325 ? 0.48628 0.48159 0.52030 -0.01247 0.02485  0.01297  311 GLN A OE1 
2606 N NE2 . GLN A 325 ? 0.32034 0.31662 0.36379 -0.01480 0.02444  0.00992  311 GLN A NE2 
2607 N N   . GLN A 326 ? 0.09563 0.09108 0.11614 -0.00938 0.01888  0.01233  312 GLN A N   
2608 C CA  . GLN A 326 ? 0.16711 0.15935 0.18675 -0.00906 0.01897  0.01262  312 GLN A CA  
2609 C C   . GLN A 326 ? 0.14951 0.14075 0.16587 -0.00896 0.01667  0.01150  312 GLN A C   
2610 O O   . GLN A 326 ? 0.13488 0.12302 0.15054 -0.00909 0.01654  0.01131  312 GLN A O   
2611 C CB  . GLN A 326 ? 0.16876 0.16039 0.18657 -0.00737 0.02081  0.01479  312 GLN A CB  
2612 C CG  . GLN A 326 ? 0.29664 0.28798 0.31757 -0.00782 0.02328  0.01615  312 GLN A CG  
2613 C CD  . GLN A 326 ? 0.37072 0.35929 0.39590 -0.00928 0.02409  0.01546  312 GLN A CD  
2614 O OE1 . GLN A 326 ? 0.49111 0.47684 0.51612 -0.00893 0.02462  0.01590  312 GLN A OE1 
2615 N NE2 . GLN A 326 ? 0.40016 0.38954 0.42951 -0.01093 0.02411  0.01421  312 GLN A NE2 
2616 N N   . ARG A 327 ? 0.08171 0.07522 0.09585 -0.00880 0.01494  0.01079  313 ARG A N   
2617 C CA  . ARG A 327 ? 0.07294 0.06533 0.08391 -0.00902 0.01269  0.00978  313 ARG A CA  
2618 C C   . ARG A 327 ? 0.08303 0.07246 0.09607 -0.01102 0.01104  0.00824  313 ARG A C   
2619 O O   . ARG A 327 ? 0.08258 0.07234 0.10007 -0.01227 0.01100  0.00736  313 ARG A O   
2620 C CB  . ARG A 327 ? 0.09951 0.09490 0.10856 -0.00885 0.01111  0.00919  313 ARG A CB  
2621 C CG  . ARG A 327 ? 0.12073 0.11843 0.12727 -0.00696 0.01179  0.01017  313 ARG A CG  
2622 C CD  . ARG A 327 ? 0.08283 0.08310 0.08777 -0.00700 0.01024  0.00922  313 ARG A CD  
2623 N NE  . ARG A 327 ? 0.08304 0.08521 0.08713 -0.00560 0.01096  0.01004  313 ARG A NE  
2624 C CZ  . ARG A 327 ? 0.12052 0.12486 0.12479 -0.00579 0.01070  0.00951  313 ARG A CZ  
2625 N NH1 . ARG A 327 ? 0.09049 0.09569 0.09581 -0.00706 0.00981  0.00802  313 ARG A NH1 
2626 N NH2 . ARG A 327 ? 0.10976 0.11542 0.11342 -0.00474 0.01139  0.01055  313 ARG A NH2 
2627 N N   . LEU A 328 ? 0.11467 0.10084 0.12456 -0.01124 0.00943  0.00773  314 LEU A N   
2628 C CA  . LEU A 328 ? 0.13437 0.11665 0.14495 -0.01308 0.00676  0.00583  314 LEU A CA  
2629 C C   . LEU A 328 ? 0.07096 0.05488 0.08246 -0.01414 0.00445  0.00426  314 LEU A C   
2630 O O   . LEU A 328 ? 0.09745 0.08427 0.10696 -0.01354 0.00397  0.00470  314 LEU A O   
2631 C CB  . LEU A 328 ? 0.10738 0.08569 0.11400 -0.01269 0.00516  0.00544  314 LEU A CB  
2632 C CG  . LEU A 328 ? 0.11062 0.08680 0.11585 -0.01147 0.00751  0.00638  314 LEU A CG  
2633 C CD1 . LEU A 328 ? 0.10724 0.07929 0.10945 -0.01119 0.00603  0.00503  314 LEU A CD1 
2634 C CD2 . LEU A 328 ? 0.20198 0.17633 0.21080 -0.01219 0.00922  0.00637  314 LEU A CD2 
2635 N N   . THR A 329 ? 0.07782 0.06032 0.09256 -0.01553 0.00316  0.00230  315 THR A N   
2636 C CA  . THR A 329 ? 0.10589 0.08944 0.12117 -0.01619 0.00076  0.00015  315 THR A CA  
2637 C C   . THR A 329 ? 0.12997 0.10983 0.13873 -0.01637 -0.00089 -0.00164 315 THR A C   
2638 O O   . THR A 329 ? 0.09978 0.07602 0.10376 -0.01581 -0.00043 -0.00145 315 THR A O   
2639 C CB  . THR A 329 ? 0.08322 0.06684 0.10480 -0.01710 -0.00007 -0.00152 315 THR A CB  
2640 O OG1 . THR A 329 ? 0.10969 0.08818 0.12902 -0.01805 -0.00112 -0.00271 315 THR A OG1 
2641 C CG2 . THR A 329 ? 0.09539 0.08188 0.12317 -0.01692 0.00286  -0.00019 315 THR A CG2 
2642 N N   . ALA A 330 ? 0.07028 0.05279 0.08062 -0.01589 -0.00253 -0.00343 316 ALA A N   
2643 C CA  . ALA A 330 ? 0.10403 0.08550 0.11224 -0.01484 -0.00433 -0.00514 316 ALA A CA  
2644 C C   . ALA A 330 ? 0.09765 0.07502 0.10529 -0.01570 -0.00543 -0.00671 316 ALA A C   
2645 O O   . ALA A 330 ? 0.11105 0.08617 0.11576 -0.01486 -0.00582 -0.00725 316 ALA A O   
2646 C CB  . ALA A 330 ? 0.06154 0.04613 0.07100 -0.01382 -0.00784 -0.00540 316 ALA A CB  
2647 N N   . LYS A 331 ? 0.08619 0.06284 0.09730 -0.01707 -0.00653 -0.00726 317 LYS A N   
2648 C CA  . LYS A 331 ? 0.09184 0.06448 0.10260 -0.01811 -0.00758 -0.00889 317 LYS A CA  
2649 C C   . LYS A 331 ? 0.12240 0.09043 0.12941 -0.01875 -0.00405 -0.00855 317 LYS A C   
2650 O O   . LYS A 331 ? 0.09991 0.06532 0.10531 -0.01843 -0.00399 -0.01011 317 LYS A O   
2651 C CB  . LYS A 331 ? 0.10467 0.07824 0.12177 -0.01909 -0.00927 -0.00937 317 LYS A CB  
2652 C CG  . LYS A 331 ? 0.13743 0.10707 0.15480 -0.02034 -0.01081 -0.01121 317 LYS A CG  
2653 C CD  . LYS A 331 ? 0.20640 0.17812 0.23179 -0.02089 -0.01292 -0.01190 317 LYS A CD  
2654 C CE  . LYS A 331 ? 0.23251 0.20049 0.25832 -0.02218 -0.01510 -0.01392 317 LYS A CE  
2655 N NZ  . LYS A 331 ? 0.53328 0.49657 0.55601 -0.02344 -0.01221 -0.01389 317 LYS A NZ  
2656 N N   . GLU A 332 ? 0.11141 0.07932 0.11790 -0.01875 -0.00236 -0.00579 318 GLU A N   
2657 C CA  . GLU A 332 ? 0.09559 0.05976 0.09853 -0.01815 -0.00174 -0.00372 318 GLU A CA  
2658 C C   . GLU A 332 ? 0.11882 0.08256 0.11713 -0.01582 -0.00421 -0.00206 318 GLU A C   
2659 O O   . GLU A 332 ? 0.11109 0.07608 0.11991 -0.01339 -0.00427 -0.00284 318 GLU A O   
2660 C CB  . GLU A 332 ? 0.11299 0.08037 0.12228 -0.01777 0.00002  -0.00096 318 GLU A CB  
2661 C CG  . GLU A 332 ? 0.10797 0.07687 0.12434 -0.01870 0.00110  -0.00151 318 GLU A CG  
2662 C CD  . GLU A 332 ? 0.13552 0.10945 0.15750 -0.01776 0.00451  0.00068  318 GLU A CD  
2663 O OE1 . GLU A 332 ? 0.11270 0.08949 0.13283 -0.01646 0.00590  0.00241  318 GLU A OE1 
2664 O OE2 . GLU A 332 ? 0.19553 0.17040 0.22322 -0.01835 0.00591  0.00061  318 GLU A OE2 
2665 N N   . ALA A 333 ? 0.08479 0.05818 0.09680 -0.01255 0.00028  -0.00392 319 ALA A N   
2666 C CA  . ALA A 333 ? 0.08602 0.05662 0.09093 -0.01207 -0.00097 -0.00279 319 ALA A CA  
2667 C C   . ALA A 333 ? 0.09267 0.06012 0.09239 -0.01248 -0.00259 -0.00555 319 ALA A C   
2668 O O   . ALA A 333 ? 0.09873 0.06272 0.09269 -0.01203 -0.00225 -0.00518 319 ALA A O   
2669 C CB  . ALA A 333 ? 0.08164 0.05567 0.08350 -0.01147 -0.00078 -0.00149 319 ALA A CB  
2670 N N   . MET A 334 ? 0.07941 0.04714 0.07883 -0.01367 -0.00475 -0.00772 320 MET A N   
2671 C CA  . MET A 334 ? 0.10603 0.07058 0.09968 -0.01399 -0.00770 -0.00914 320 MET A CA  
2672 C C   . MET A 334 ? 0.14268 0.10304 0.13713 -0.01469 -0.00677 -0.01076 320 MET A C   
2673 O O   . MET A 334 ? 0.16383 0.12075 0.15223 -0.01468 -0.00828 -0.01158 320 MET A O   
2674 C CB  . MET A 334 ? 0.09188 0.05754 0.08616 -0.01481 -0.01118 -0.01011 320 MET A CB  
2675 C CG  . MET A 334 ? 0.11154 0.08059 0.10439 -0.01371 -0.01301 -0.00846 320 MET A CG  
2676 S SD  . MET A 334 ? 0.21940 0.18924 0.21466 -0.01402 -0.01750 -0.00909 320 MET A SD  
2677 C CE  . MET A 334 ? 0.22402 0.18844 0.21279 -0.01425 -0.02070 -0.00992 320 MET A CE  
2678 N N   . GLU A 335 ? 0.09766 0.05792 0.09941 -0.01539 -0.00415 -0.01120 321 GLU A N   
2679 C CA  . GLU A 335 ? 0.10689 0.06364 0.11059 -0.01569 -0.00343 -0.01236 321 GLU A CA  
2680 C C   . GLU A 335 ? 0.09990 0.05411 0.10183 -0.01406 -0.00289 -0.01023 321 GLU A C   
2681 O O   . GLU A 335 ? 0.12819 0.07839 0.12982 -0.01420 -0.00293 -0.01103 321 GLU A O   
2682 C CB  . GLU A 335 ? 0.15811 0.11528 0.16549 -0.01744 -0.00030 -0.01271 321 GLU A CB  
2683 C CG  . GLU A 335 ? 0.16968 0.12478 0.17353 -0.02030 -0.00344 -0.01432 321 GLU A CG  
2684 C CD  . GLU A 335 ? 0.36227 0.31645 0.36685 -0.02227 -0.00426 -0.01282 321 GLU A CD  
2685 O OE1 . GLU A 335 ? 0.35147 0.30504 0.35539 -0.02200 -0.00327 -0.00986 321 GLU A OE1 
2686 O OE2 . GLU A 335 ? 0.33869 0.29419 0.34722 -0.02322 -0.00758 -0.01422 321 GLU A OE2 
2687 N N   . HIS A 336 ? 0.10644 0.06227 0.10408 -0.01296 -0.00167 -0.00747 322 HIS A N   
2688 C CA  . HIS A 336 ? 0.14715 0.10039 0.13968 -0.01210 0.00118  -0.00538 322 HIS A CA  
2689 C C   . HIS A 336 ? 0.14037 0.08955 0.12533 -0.01190 0.00162  -0.00705 322 HIS A C   
2690 O O   . HIS A 336 ? 0.15609 0.10536 0.13657 -0.01214 -0.00034 -0.00844 322 HIS A O   
2691 C CB  . HIS A 336 ? 0.11350 0.07025 0.10329 -0.01109 0.00323  -0.00269 322 HIS A CB  
2692 C CG  . HIS A 336 ? 0.11185 0.06808 0.09938 -0.00987 0.00720  -0.00052 322 HIS A CG  
2693 N ND1 . HIS A 336 ? 0.13936 0.09315 0.12039 -0.00890 0.00927  -0.00079 322 HIS A ND1 
2694 C CD2 . HIS A 336 ? 0.15146 0.10985 0.14269 -0.00927 0.00958  0.00185  322 HIS A CD2 
2695 C CE1 . HIS A 336 ? 0.18442 0.13920 0.16654 -0.00751 0.01265  0.00114  322 HIS A CE1 
2696 N NE2 . HIS A 336 ? 0.13400 0.09177 0.12212 -0.00766 0.01277  0.00279  322 HIS A NE2 
2697 N N   . PRO A 337 ? 0.12077 0.06638 0.10390 -0.01146 0.00427  -0.00667 323 PRO A N   
2698 C CA  . PRO A 337 ? 0.13537 0.07686 0.11120 -0.01125 0.00525  -0.00812 323 PRO A CA  
2699 C C   . PRO A 337 ? 0.16926 0.11148 0.13712 -0.01061 0.00595  -0.00732 323 PRO A C   
2700 O O   . PRO A 337 ? 0.13476 0.07395 0.09650 -0.01084 0.00563  -0.00860 323 PRO A O   
2701 C CB  . PRO A 337 ? 0.18769 0.12663 0.16429 -0.01043 0.00910  -0.00703 323 PRO A CB  
2702 C CG  . PRO A 337 ? 0.17541 0.11583 0.15982 -0.01080 0.00879  -0.00586 323 PRO A CG  
2703 C CD  . PRO A 337 ? 0.11042 0.05555 0.09827 -0.01123 0.00649  -0.00494 323 PRO A CD  
2704 N N   . TYR A 338 ? 0.13287 0.07884 0.10051 -0.00982 0.00700  -0.00511 324 TYR A N   
2705 C CA  . TYR A 338 ? 0.13313 0.07982 0.09353 -0.00936 0.00716  -0.00430 324 TYR A CA  
2706 C C   . TYR A 338 ? 0.14908 0.09546 0.10639 -0.01030 0.00325  -0.00551 324 TYR A C   
2707 O O   . TYR A 338 ? 0.15030 0.09529 0.10131 -0.01019 0.00337  -0.00486 324 TYR A O   
2708 C CB  . TYR A 338 ? 0.11279 0.06430 0.07501 -0.00853 0.00783  -0.00234 324 TYR A CB  
2709 C CG  . TYR A 338 ? 0.10669 0.05943 0.06213 -0.00793 0.00802  -0.00153 324 TYR A CG  
2710 C CD1 . TYR A 338 ? 0.13025 0.08286 0.08382 -0.00649 0.01054  -0.00142 324 TYR A CD1 
2711 C CD2 . TYR A 338 ? 0.11020 0.06612 0.06537 -0.00837 0.00508  -0.00096 324 TYR A CD2 
2712 C CE1 . TYR A 338 ? 0.10734 0.06508 0.06561 -0.00521 0.00858  -0.00182 324 TYR A CE1 
2713 C CE2 . TYR A 338 ? 0.08202 0.04424 0.04207 -0.00688 0.00398  -0.00047 324 TYR A CE2 
2714 C CZ  . TYR A 338 ? 0.13942 0.10055 0.10177 -0.00573 0.00545  -0.00134 324 TYR A CZ  
2715 O OH  . TYR A 338 ? 0.12117 0.08481 0.08591 -0.00511 0.00474  -0.00090 324 TYR A OH  
2716 N N   . PHE A 339 ? 0.13016 0.07815 0.09283 -0.01110 0.00000  -0.00694 325 PHE A N   
2717 C CA  . PHE A 339 ? 0.12188 0.06974 0.08184 -0.01175 -0.00351 -0.00778 325 PHE A CA  
2718 C C   . PHE A 339 ? 0.13307 0.07619 0.09044 -0.01274 -0.00476 -0.01012 325 PHE A C   
2719 O O   . PHE A 339 ? 0.16859 0.11021 0.12215 -0.01339 -0.00765 -0.01051 325 PHE A O   
2720 C CB  . PHE A 339 ? 0.08116 0.03292 0.04667 -0.01212 -0.00620 -0.00782 325 PHE A CB  
2721 C CG  . PHE A 339 ? 0.10328 0.05946 0.07024 -0.01125 -0.00529 -0.00564 325 PHE A CG  
2722 C CD1 . PHE A 339 ? 0.10150 0.05817 0.06281 -0.01065 -0.00547 -0.00363 325 PHE A CD1 
2723 C CD2 . PHE A 339 ? 0.09482 0.05425 0.06909 -0.01111 -0.00401 -0.00532 325 PHE A CD2 
2724 C CE1 . PHE A 339 ? 0.12229 0.08281 0.08480 -0.00994 -0.00462 -0.00176 325 PHE A CE1 
2725 C CE2 . PHE A 339 ? 0.08288 0.04573 0.05728 -0.01052 -0.00321 -0.00340 325 PHE A CE2 
2726 C CZ  . PHE A 339 ? 0.09076 0.05437 0.05902 -0.00991 -0.00362 -0.00193 325 PHE A CZ  
2727 N N   . TYR A 340 ? 0.15420 0.09454 0.11327 -0.01280 -0.00268 -0.01147 326 TYR A N   
2728 C CA  . TYR A 340 ? 0.11260 0.04820 0.06885 -0.01380 -0.00377 -0.01396 326 TYR A CA  
2729 C C   . TYR A 340 ? 0.16202 0.09438 0.10888 -0.01408 -0.00452 -0.01373 326 TYR A C   
2730 O O   . TYR A 340 ? 0.19882 0.12870 0.14323 -0.01517 -0.00749 -0.01525 326 TYR A O   
2731 C CB  . TYR A 340 ? 0.14795 0.08065 0.10711 -0.01361 -0.00109 -0.01517 326 TYR A CB  
2732 C CG  . TYR A 340 ? 0.20395 0.13155 0.15997 -0.01470 -0.00215 -0.01803 326 TYR A CG  
2733 C CD1 . TYR A 340 ? 0.24521 0.17225 0.20412 -0.01611 -0.00549 -0.02026 326 TYR A CD1 
2734 C CD2 . TYR A 340 ? 0.23232 0.15571 0.18250 -0.01440 0.00036  -0.01859 326 TYR A CD2 
2735 C CE1 . TYR A 340 ? 0.25909 0.18134 0.21473 -0.01723 -0.00659 -0.02301 326 TYR A CE1 
2736 C CE2 . TYR A 340 ? 0.24083 0.15935 0.18776 -0.01546 -0.00055 -0.02136 326 TYR A CE2 
2737 C CZ  . TYR A 340 ? 0.36882 0.28674 0.31832 -0.01688 -0.00416 -0.02357 326 TYR A CZ  
2738 O OH  . TYR A 340 ? 0.48091 0.39386 0.42688 -0.01803 -0.00517 -0.02647 326 TYR A OH  
2739 N N   . PRO A 341 ? 0.17913 0.11113 0.12085 -0.01327 -0.00201 -0.01175 327 PRO A N   
2740 C CA  . PRO A 341 ? 0.15879 0.08722 0.09243 -0.01378 -0.00268 -0.01127 327 PRO A CA  
2741 C C   . PRO A 341 ? 0.20165 0.13087 0.13394 -0.01430 -0.00667 -0.01032 327 PRO A C   
2742 O O   . PRO A 341 ? 0.24743 0.17263 0.17415 -0.01516 -0.00849 -0.01082 327 PRO A O   
2743 C CB  . PRO A 341 ? 0.20512 0.13413 0.13628 -0.01281 0.00096  -0.00890 327 PRO A CB  
2744 C CG  . PRO A 341 ? 0.24524 0.17656 0.18153 -0.01180 0.00394  -0.00889 327 PRO A CG  
2745 C CD  . PRO A 341 ? 0.16839 0.10274 0.11166 -0.01198 0.00168  -0.00984 327 PRO A CD  
2746 N N   . VAL A 342 ? 0.16599 0.10003 0.10332 -0.01376 -0.00800 -0.00896 328 VAL A N   
2747 C CA  . VAL A 342 ? 0.14492 0.07979 0.08211 -0.01400 -0.01173 -0.00801 328 VAL A CA  
2748 C C   . VAL A 342 ? 0.22095 0.15453 0.16008 -0.01501 -0.01521 -0.01040 328 VAL A C   
2749 O O   . VAL A 342 ? 0.30482 0.23537 0.24003 -0.01565 -0.01822 -0.01047 328 VAL A O   
2750 C CB  . VAL A 342 ? 0.13580 0.07622 0.07830 -0.01307 -0.01179 -0.00609 328 VAL A CB  
2751 C CG1 . VAL A 342 ? 0.21655 0.15756 0.15973 -0.01314 -0.01556 -0.00524 328 VAL A CG1 
2752 C CG2 . VAL A 342 ? 0.18998 0.13129 0.13069 -0.01225 -0.00856 -0.00368 328 VAL A CG2 
2753 N N   . VAL A 343 ? 0.19592 0.13143 0.14158 -0.01528 -0.01477 -0.01235 329 VAL A N   
2754 C CA  . VAL A 343 ? 0.21931 0.15367 0.16814 -0.01648 -0.01769 -0.01483 329 VAL A CA  
2755 C C   . VAL A 343 ? 0.33187 0.26026 0.27408 -0.01749 -0.01854 -0.01663 329 VAL A C   
2756 O O   . VAL A 343 ? 0.39059 0.31669 0.33091 -0.01843 -0.02218 -0.01756 329 VAL A O   
2757 C CB  . VAL A 343 ? 0.24620 0.18309 0.20392 -0.01676 -0.01598 -0.01645 329 VAL A CB  
2758 C CG1 . VAL A 343 ? 0.32753 0.26233 0.28833 -0.01832 -0.01825 -0.01931 329 VAL A CG1 
2759 C CG2 . VAL A 343 ? 0.21657 0.15910 0.18077 -0.01610 -0.01573 -0.01490 329 VAL A CG2 
2760 N N   . LYS A 344 ? 0.26197 0.18753 0.20048 -0.01732 -0.01519 -0.01715 330 LYS A N   
2761 C CA  . LYS A 344 ? 0.30824 0.22792 0.24027 -0.01833 -0.01550 -0.01912 330 LYS A CA  
2762 C C   . LYS A 344 ? 0.50314 0.41954 0.42669 -0.01865 -0.01742 -0.01766 330 LYS A C   
2763 O O   . LYS A 344 ? 0.52352 0.43531 0.44215 -0.01983 -0.01964 -0.01927 330 LYS A O   
2764 C CB  . LYS A 344 ? 0.34004 0.25757 0.27064 -0.01787 -0.01106 -0.01989 330 LYS A CB  
2765 C CG  . LYS A 344 ? 0.55761 0.46893 0.48163 -0.01889 -0.01080 -0.02224 330 LYS A CG  
2766 C CD  . LYS A 344 ? 0.65684 0.56627 0.58156 -0.01831 -0.00642 -0.02338 330 LYS A CD  
2767 C CE  . LYS A 344 ? 0.62450 0.53603 0.54817 -0.01686 -0.00258 -0.02060 330 LYS A CE  
2768 N NZ  . LYS A 344 ? 0.81384 0.72329 0.73828 -0.01615 0.00173  -0.02153 330 LYS A NZ  
2769 N N   . GLU A 345 ? 0.45360 0.37194 0.37556 -0.01773 -0.01659 -0.01463 331 GLU A N   
2770 C CA  . GLU A 345 ? 0.37549 0.29040 0.29050 -0.01809 -0.01822 -0.01299 331 GLU A CA  
2771 C C   . GLU A 345 ? 0.52984 0.44525 0.44638 -0.01839 -0.02311 -0.01250 331 GLU A C   
2772 O O   . GLU A 345 ? 0.57116 0.48194 0.48176 -0.01923 -0.02566 -0.01244 331 GLU A O   
2773 C CB  . GLU A 345 ? 0.45593 0.37237 0.36982 -0.01714 -0.01529 -0.01008 331 GLU A CB  
2774 C CG  . GLU A 345 ? 0.57797 0.49025 0.48525 -0.01769 -0.01607 -0.00848 331 GLU A CG  
2775 C CD  . GLU A 345 ? 0.68524 0.59171 0.58489 -0.01866 -0.01391 -0.00971 331 GLU A CD  
2776 O OE1 . GLU A 345 ? 0.66221 0.56810 0.56193 -0.01869 -0.01145 -0.01167 331 GLU A OE1 
2777 O OE2 . GLU A 345 ? 0.67756 0.57982 0.57127 -0.01943 -0.01455 -0.00885 331 GLU A OE2 
2778 N N   . GLN A 346 ? 0.51223 0.43292 0.43669 -0.01773 -0.02442 -0.01219 332 GLN A N   
2779 C CA  . GLN A 346 ? 0.55137 0.47291 0.47869 -0.01787 -0.02899 -0.01195 332 GLN A CA  
2780 C C   . GLN A 346 ? 0.72077 0.63973 0.64854 -0.01919 -0.03212 -0.01479 332 GLN A C   
2781 O O   . GLN A 346 ? 0.65128 0.57132 0.58280 -0.01933 -0.03595 -0.01489 332 GLN A O   
2782 C CB  . GLN A 346 ? 0.63337 0.56139 0.56919 -0.01677 -0.02897 -0.01081 332 GLN A CB  
2783 C CG  . GLN A 346 ? 0.81350 0.74274 0.74863 -0.01571 -0.02925 -0.00778 332 GLN A CG  
2784 C CD  . GLN A 346 ? 0.80597 0.74156 0.74813 -0.01452 -0.02742 -0.00658 332 GLN A CD  
2785 O OE1 . GLN A 346 ? 0.31934 0.25884 0.26855 -0.01443 -0.02845 -0.00760 332 GLN A OE1 
2786 N NE2 . GLN A 346 ? 0.27152 0.20796 0.21192 -0.01377 -0.02461 -0.00445 332 GLN A NE2 
2787 N N   . SER A 347 ? 0.82794 0.74343 0.75225 -0.02013 -0.03046 -0.01709 333 SER A N   
2788 C CA  . SER A 347 ? 0.81403 0.72617 0.73774 -0.02162 -0.03319 -0.02002 333 SER A CA  
2789 C C   . SER A 347 ? 0.88397 0.78939 0.79798 -0.02266 -0.03278 -0.02125 333 SER A C   
2790 O O   . SER A 347 ? 1.01693 0.91902 0.92959 -0.02402 -0.03475 -0.02398 333 SER A O   
2791 C CB  . SER A 347 ? 0.72697 0.64187 0.65875 -0.02206 -0.03154 -0.02260 333 SER A CB  
2792 O OG  . SER A 347 ? 0.81083 0.73162 0.75154 -0.02139 -0.03184 -0.02165 333 SER A OG  
2793 N N   . GLN A 348 ? 0.96512 0.86839 0.87255 -0.02219 -0.03013 -0.01944 334 GLN A N   
2794 C CA  . GLN A 348 ? 0.92762 0.82424 0.82528 -0.02327 -0.02950 -0.02038 334 GLN A CA  
2795 C C   . GLN A 348 ? 0.97461 0.86758 0.86576 -0.02368 -0.03252 -0.01831 334 GLN A C   
2796 O O   . GLN A 348 ? 1.07836 0.96597 0.96334 -0.02502 -0.03542 -0.01956 334 GLN A O   
2797 C CB  . GLN A 348 ? 0.77816 0.67426 0.67303 -0.02269 -0.02399 -0.01996 334 GLN A CB  
2798 C CG  . GLN A 348 ? 1.00176 0.89921 0.90118 -0.02249 -0.02085 -0.02243 334 GLN A CG  
2799 C CD  . GLN A 348 ? 1.15524 1.04744 1.05083 -0.02394 -0.02157 -0.02601 334 GLN A CD  
2800 O OE1 . GLN A 348 ? 1.15952 1.05268 1.06082 -0.02441 -0.02263 -0.02853 334 GLN A OE1 
2801 N NE2 . GLN A 348 ? 1.15219 1.03859 1.03826 -0.02479 -0.02082 -0.02637 334 GLN A NE2 
# 
