data_9HJV
# 
_entry.id   9HJV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9HJV         pdb_00009hjv 10.2210/pdb9hjv/pdb 
WWPDB D_1292143270 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-21 ? 
2 'Structure model' 1 1 2025-06-18 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HJV 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-02 
_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              christopher.schofield@chem.ox.ac.uk 
_pdbx_contact_author.name_first         Christopher 
_pdbx_contact_author.name_last          Schofield 
_pdbx_contact_author.name_mi            J. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0290-6565 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Beech, M.J.'     1 ? 
'Smith, H.G.'     2 ? 
'Allen, M.D.'     3 ? 
'Farley, A.J.M.'  4 ? 
'Schofield, C.J.' 5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Chem Sci' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-6520 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                9691 
_citation.page_last                 9704 
_citation.title                     
'Binding assays enable discovery of Tet(X) inhibitors that combat tetracycline destructase resistance.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1039/d5sc00964b 
_citation.pdbx_database_id_PubMed   40342919 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Beech, M.J.'     1  ? 
primary 'Toma, E.C.'      2  ? 
primary 'Smith, H.G.'     3  ? 
primary 'Trush, M.M.'     4  ? 
primary 'Ang, J.H.J.'     5  ? 
primary 'Wong, M.Y.'      6  ? 
primary 'Wong, C.H.J.'    7  ? 
primary 'Ali, H.S.'       8  ? 
primary 'Butt, Z.'        9  ? 
primary 'Goel, V.'        10 ? 
primary 'Duarte, F.'      11 ? 
primary 'Farley, A.J.M.'  12 ? 
primary 'Walsh, T.R.'     13 ? 
primary 'Schofield, C.J.' 14 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Flavin-dependent monooxygenase'                                   41668.992 1   1.14.13.- ? ? 
'Residues for which electron density was not observed were not modelled.' 
2 non-polymer syn 'DIHYDROFLAVINE-ADENINE DINUCLEOTIDE'                              787.566   1   ?         ? ? ? 
3 non-polymer syn '2-chloro-10-[3-(4-methylpiperazin-1-yl)propyl]-10H-phenothiazine' 373.943   1   ?         ? ? ? 
4 non-polymer syn 'SULFATE ION'                                                      96.063    3   ?         ? ? ? 
5 water       nat water                                                              18.015    279 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'TetX monooxygenase,TetX' 
# 
_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       
;NLLSDKNVAIIGGGPVGLTMAKLLQQNGIDVSVYERDNDREARIFGGTLDLHKGSGQEAMKKAGLLQTYYDLALPMGVNI
ADEKGNILSTKNVKPENRFDNPEINRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVIIANGGM
SKVRKFVTDTEVEETGTFNIQADIHHPEVNCPGFFQLCNGNRLMAAHQGNLLFANPNNNGALHFGISFKTPDEWKNQTQV
DFQNRNSVVDFLLKEFSDWDERYKELIRVTSSFVGLATRIFPLGKSWKSKRPLPITMIGDAAHLMPPFAGQGVNSGLMDA
LILSDNLTNGKFNSIEEAIENYEQQMFIYGKEAQEESTQNEIEMFKPDFTF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;NLLSDKNVAIIGGGPVGLTMAKLLQQNGIDVSVYERDNDREARIFGGTLDLHKGSGQEAMKKAGLLQTYYDLALPMGVNI
ADEKGNILSTKNVKPENRFDNPEINRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVIIANGGM
SKVRKFVTDTEVEETGTFNIQADIHHPEVNCPGFFQLCNGNRLMAAHQGNLLFANPNNNGALHFGISFKTPDEWKNQTQV
DFQNRNSVVDFLLKEFSDWDERYKELIRVTSSFVGLATRIFPLGKSWKSKRPLPITMIGDAAHLMPPFAGQGVNSGLMDA
LILSDNLTNGKFNSIEEAIENYEQQMFIYGKEAQEESTQNEIEMFKPDFTF
;
_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 'DIHYDROFLAVINE-ADENINE DINUCLEOTIDE'                              FDA 
3 '2-chloro-10-[3-(4-methylpiperazin-1-yl)propyl]-10H-phenothiazine' P77 
4 'SULFATE ION'                                                      SO4 
5 water                                                              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASN n 
1 2   LEU n 
1 3   LEU n 
1 4   SER n 
1 5   ASP n 
1 6   LYS n 
1 7   ASN n 
1 8   VAL n 
1 9   ALA n 
1 10  ILE n 
1 11  ILE n 
1 12  GLY n 
1 13  GLY n 
1 14  GLY n 
1 15  PRO n 
1 16  VAL n 
1 17  GLY n 
1 18  LEU n 
1 19  THR n 
1 20  MET n 
1 21  ALA n 
1 22  LYS n 
1 23  LEU n 
1 24  LEU n 
1 25  GLN n 
1 26  GLN n 
1 27  ASN n 
1 28  GLY n 
1 29  ILE n 
1 30  ASP n 
1 31  VAL n 
1 32  SER n 
1 33  VAL n 
1 34  TYR n 
1 35  GLU n 
1 36  ARG n 
1 37  ASP n 
1 38  ASN n 
1 39  ASP n 
1 40  ARG n 
1 41  GLU n 
1 42  ALA n 
1 43  ARG n 
1 44  ILE n 
1 45  PHE n 
1 46  GLY n 
1 47  GLY n 
1 48  THR n 
1 49  LEU n 
1 50  ASP n 
1 51  LEU n 
1 52  HIS n 
1 53  LYS n 
1 54  GLY n 
1 55  SER n 
1 56  GLY n 
1 57  GLN n 
1 58  GLU n 
1 59  ALA n 
1 60  MET n 
1 61  LYS n 
1 62  LYS n 
1 63  ALA n 
1 64  GLY n 
1 65  LEU n 
1 66  LEU n 
1 67  GLN n 
1 68  THR n 
1 69  TYR n 
1 70  TYR n 
1 71  ASP n 
1 72  LEU n 
1 73  ALA n 
1 74  LEU n 
1 75  PRO n 
1 76  MET n 
1 77  GLY n 
1 78  VAL n 
1 79  ASN n 
1 80  ILE n 
1 81  ALA n 
1 82  ASP n 
1 83  GLU n 
1 84  LYS n 
1 85  GLY n 
1 86  ASN n 
1 87  ILE n 
1 88  LEU n 
1 89  SER n 
1 90  THR n 
1 91  LYS n 
1 92  ASN n 
1 93  VAL n 
1 94  LYS n 
1 95  PRO n 
1 96  GLU n 
1 97  ASN n 
1 98  ARG n 
1 99  PHE n 
1 100 ASP n 
1 101 ASN n 
1 102 PRO n 
1 103 GLU n 
1 104 ILE n 
1 105 ASN n 
1 106 ARG n 
1 107 ASN n 
1 108 ASP n 
1 109 LEU n 
1 110 ARG n 
1 111 ALA n 
1 112 ILE n 
1 113 LEU n 
1 114 LEU n 
1 115 ASN n 
1 116 SER n 
1 117 LEU n 
1 118 GLU n 
1 119 ASN n 
1 120 ASP n 
1 121 THR n 
1 122 VAL n 
1 123 ILE n 
1 124 TRP n 
1 125 ASP n 
1 126 ARG n 
1 127 LYS n 
1 128 LEU n 
1 129 VAL n 
1 130 MET n 
1 131 LEU n 
1 132 GLU n 
1 133 PRO n 
1 134 GLY n 
1 135 LYS n 
1 136 LYS n 
1 137 LYS n 
1 138 TRP n 
1 139 THR n 
1 140 LEU n 
1 141 THR n 
1 142 PHE n 
1 143 GLU n 
1 144 ASN n 
1 145 LYS n 
1 146 PRO n 
1 147 SER n 
1 148 GLU n 
1 149 THR n 
1 150 ALA n 
1 151 ASP n 
1 152 LEU n 
1 153 VAL n 
1 154 ILE n 
1 155 ILE n 
1 156 ALA n 
1 157 ASN n 
1 158 GLY n 
1 159 GLY n 
1 160 MET n 
1 161 SER n 
1 162 LYS n 
1 163 VAL n 
1 164 ARG n 
1 165 LYS n 
1 166 PHE n 
1 167 VAL n 
1 168 THR n 
1 169 ASP n 
1 170 THR n 
1 171 GLU n 
1 172 VAL n 
1 173 GLU n 
1 174 GLU n 
1 175 THR n 
1 176 GLY n 
1 177 THR n 
1 178 PHE n 
1 179 ASN n 
1 180 ILE n 
1 181 GLN n 
1 182 ALA n 
1 183 ASP n 
1 184 ILE n 
1 185 HIS n 
1 186 HIS n 
1 187 PRO n 
1 188 GLU n 
1 189 VAL n 
1 190 ASN n 
1 191 CYS n 
1 192 PRO n 
1 193 GLY n 
1 194 PHE n 
1 195 PHE n 
1 196 GLN n 
1 197 LEU n 
1 198 CYS n 
1 199 ASN n 
1 200 GLY n 
1 201 ASN n 
1 202 ARG n 
1 203 LEU n 
1 204 MET n 
1 205 ALA n 
1 206 ALA n 
1 207 HIS n 
1 208 GLN n 
1 209 GLY n 
1 210 ASN n 
1 211 LEU n 
1 212 LEU n 
1 213 PHE n 
1 214 ALA n 
1 215 ASN n 
1 216 PRO n 
1 217 ASN n 
1 218 ASN n 
1 219 ASN n 
1 220 GLY n 
1 221 ALA n 
1 222 LEU n 
1 223 HIS n 
1 224 PHE n 
1 225 GLY n 
1 226 ILE n 
1 227 SER n 
1 228 PHE n 
1 229 LYS n 
1 230 THR n 
1 231 PRO n 
1 232 ASP n 
1 233 GLU n 
1 234 TRP n 
1 235 LYS n 
1 236 ASN n 
1 237 GLN n 
1 238 THR n 
1 239 GLN n 
1 240 VAL n 
1 241 ASP n 
1 242 PHE n 
1 243 GLN n 
1 244 ASN n 
1 245 ARG n 
1 246 ASN n 
1 247 SER n 
1 248 VAL n 
1 249 VAL n 
1 250 ASP n 
1 251 PHE n 
1 252 LEU n 
1 253 LEU n 
1 254 LYS n 
1 255 GLU n 
1 256 PHE n 
1 257 SER n 
1 258 ASP n 
1 259 TRP n 
1 260 ASP n 
1 261 GLU n 
1 262 ARG n 
1 263 TYR n 
1 264 LYS n 
1 265 GLU n 
1 266 LEU n 
1 267 ILE n 
1 268 ARG n 
1 269 VAL n 
1 270 THR n 
1 271 SER n 
1 272 SER n 
1 273 PHE n 
1 274 VAL n 
1 275 GLY n 
1 276 LEU n 
1 277 ALA n 
1 278 THR n 
1 279 ARG n 
1 280 ILE n 
1 281 PHE n 
1 282 PRO n 
1 283 LEU n 
1 284 GLY n 
1 285 LYS n 
1 286 SER n 
1 287 TRP n 
1 288 LYS n 
1 289 SER n 
1 290 LYS n 
1 291 ARG n 
1 292 PRO n 
1 293 LEU n 
1 294 PRO n 
1 295 ILE n 
1 296 THR n 
1 297 MET n 
1 298 ILE n 
1 299 GLY n 
1 300 ASP n 
1 301 ALA n 
1 302 ALA n 
1 303 HIS n 
1 304 LEU n 
1 305 MET n 
1 306 PRO n 
1 307 PRO n 
1 308 PHE n 
1 309 ALA n 
1 310 GLY n 
1 311 GLN n 
1 312 GLY n 
1 313 VAL n 
1 314 ASN n 
1 315 SER n 
1 316 GLY n 
1 317 LEU n 
1 318 MET n 
1 319 ASP n 
1 320 ALA n 
1 321 LEU n 
1 322 ILE n 
1 323 LEU n 
1 324 SER n 
1 325 ASP n 
1 326 ASN n 
1 327 LEU n 
1 328 THR n 
1 329 ASN n 
1 330 GLY n 
1 331 LYS n 
1 332 PHE n 
1 333 ASN n 
1 334 SER n 
1 335 ILE n 
1 336 GLU n 
1 337 GLU n 
1 338 ALA n 
1 339 ILE n 
1 340 GLU n 
1 341 ASN n 
1 342 TYR n 
1 343 GLU n 
1 344 GLN n 
1 345 GLN n 
1 346 MET n 
1 347 PHE n 
1 348 ILE n 
1 349 TYR n 
1 350 GLY n 
1 351 LYS n 
1 352 GLU n 
1 353 ALA n 
1 354 GLN n 
1 355 GLU n 
1 356 GLU n 
1 357 SER n 
1 358 THR n 
1 359 GLN n 
1 360 ASN n 
1 361 GLU n 
1 362 ILE n 
1 363 GLU n 
1 364 MET n 
1 365 PHE n 
1 366 LYS n 
1 367 PRO n 
1 368 ASP n 
1 369 PHE n 
1 370 THR n 
1 371 PHE 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                   371 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 mtr-1 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              C41 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                            ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                                           ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                         ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                    ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                                           ? 'C3 H7 N O2 S'      121.158 
FDA non-polymer         . 'DIHYDROFLAVINE-ADENINE DINUCLEOTIDE'                              ? 'C27 H35 N9 O15 P2' 787.566 
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 
P77 non-polymer         . '2-chloro-10-[3-(4-methylpiperazin-1-yl)propyl]-10H-phenothiazine' ? 'C20 H24 Cl N3 S'   373.943 
PHE 'L-peptide linking' y PHENYLALANINE                                                      ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                                            ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                                             ? 'C3 H7 N O3'        105.093 
SO4 non-polymer         . 'SULFATE ION'                                                      ? 'O4 S -2'           96.063  
THR 'L-peptide linking' y THREONINE                                                          ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                         ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                                           ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                                             ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ASN 1   12  12  ASN ASN A . n 
A 1 2   LEU 2   13  13  LEU LEU A . n 
A 1 3   LEU 3   14  14  LEU LEU A . n 
A 1 4   SER 4   15  15  SER SER A . n 
A 1 5   ASP 5   16  16  ASP ASP A . n 
A 1 6   LYS 6   17  17  LYS LYS A . n 
A 1 7   ASN 7   18  18  ASN ASN A . n 
A 1 8   VAL 8   19  19  VAL VAL A . n 
A 1 9   ALA 9   20  20  ALA ALA A . n 
A 1 10  ILE 10  21  21  ILE ILE A . n 
A 1 11  ILE 11  22  22  ILE ILE A . n 
A 1 12  GLY 12  23  23  GLY GLY A . n 
A 1 13  GLY 13  24  24  GLY GLY A . n 
A 1 14  GLY 14  25  25  GLY GLY A . n 
A 1 15  PRO 15  26  26  PRO PRO A . n 
A 1 16  VAL 16  27  27  VAL VAL A . n 
A 1 17  GLY 17  28  28  GLY GLY A . n 
A 1 18  LEU 18  29  29  LEU LEU A . n 
A 1 19  THR 19  30  30  THR THR A . n 
A 1 20  MET 20  31  31  MET MET A . n 
A 1 21  ALA 21  32  32  ALA ALA A . n 
A 1 22  LYS 22  33  33  LYS LYS A . n 
A 1 23  LEU 23  34  34  LEU LEU A . n 
A 1 24  LEU 24  35  35  LEU LEU A . n 
A 1 25  GLN 25  36  36  GLN GLN A . n 
A 1 26  GLN 26  37  37  GLN GLN A . n 
A 1 27  ASN 27  38  38  ASN ASN A . n 
A 1 28  GLY 28  39  39  GLY GLY A . n 
A 1 29  ILE 29  40  40  ILE ILE A . n 
A 1 30  ASP 30  41  41  ASP ASP A . n 
A 1 31  VAL 31  42  42  VAL VAL A . n 
A 1 32  SER 32  43  43  SER SER A . n 
A 1 33  VAL 33  44  44  VAL VAL A . n 
A 1 34  TYR 34  45  45  TYR TYR A . n 
A 1 35  GLU 35  46  46  GLU GLU A . n 
A 1 36  ARG 36  47  47  ARG ARG A . n 
A 1 37  ASP 37  48  48  ASP ASP A . n 
A 1 38  ASN 38  49  49  ASN ASN A . n 
A 1 39  ASP 39  50  50  ASP ASP A . n 
A 1 40  ARG 40  51  51  ARG ARG A . n 
A 1 41  GLU 41  52  52  GLU GLU A . n 
A 1 42  ALA 42  53  53  ALA ALA A . n 
A 1 43  ARG 43  54  54  ARG ARG A . n 
A 1 44  ILE 44  55  55  ILE ILE A . n 
A 1 45  PHE 45  56  56  PHE PHE A . n 
A 1 46  GLY 46  57  57  GLY GLY A . n 
A 1 47  GLY 47  58  58  GLY GLY A . n 
A 1 48  THR 48  59  59  THR THR A . n 
A 1 49  LEU 49  60  60  LEU LEU A . n 
A 1 50  ASP 50  61  61  ASP ASP A . n 
A 1 51  LEU 51  62  62  LEU LEU A . n 
A 1 52  HIS 52  63  63  HIS HIS A . n 
A 1 53  LYS 53  64  64  LYS LYS A . n 
A 1 54  GLY 54  65  65  GLY GLY A . n 
A 1 55  SER 55  66  66  SER SER A . n 
A 1 56  GLY 56  67  67  GLY GLY A . n 
A 1 57  GLN 57  68  68  GLN GLN A . n 
A 1 58  GLU 58  69  69  GLU GLU A . n 
A 1 59  ALA 59  70  70  ALA ALA A . n 
A 1 60  MET 60  71  71  MET MET A . n 
A 1 61  LYS 61  72  72  LYS LYS A . n 
A 1 62  LYS 62  73  73  LYS LYS A . n 
A 1 63  ALA 63  74  74  ALA ALA A . n 
A 1 64  GLY 64  75  75  GLY GLY A . n 
A 1 65  LEU 65  76  76  LEU LEU A . n 
A 1 66  LEU 66  77  77  LEU LEU A . n 
A 1 67  GLN 67  78  78  GLN GLN A . n 
A 1 68  THR 68  79  79  THR THR A . n 
A 1 69  TYR 69  80  80  TYR TYR A . n 
A 1 70  TYR 70  81  81  TYR TYR A . n 
A 1 71  ASP 71  82  82  ASP ASP A . n 
A 1 72  LEU 72  83  83  LEU LEU A . n 
A 1 73  ALA 73  84  84  ALA ALA A . n 
A 1 74  LEU 74  85  85  LEU LEU A . n 
A 1 75  PRO 75  86  86  PRO PRO A . n 
A 1 76  MET 76  87  87  MET MET A . n 
A 1 77  GLY 77  88  88  GLY GLY A . n 
A 1 78  VAL 78  89  89  VAL VAL A . n 
A 1 79  ASN 79  90  90  ASN ASN A . n 
A 1 80  ILE 80  91  91  ILE ILE A . n 
A 1 81  ALA 81  92  92  ALA ALA A . n 
A 1 82  ASP 82  93  93  ASP ASP A . n 
A 1 83  GLU 83  94  94  GLU GLU A . n 
A 1 84  LYS 84  95  95  LYS LYS A . n 
A 1 85  GLY 85  96  96  GLY GLY A . n 
A 1 86  ASN 86  97  97  ASN ASN A . n 
A 1 87  ILE 87  98  98  ILE ILE A . n 
A 1 88  LEU 88  99  99  LEU LEU A . n 
A 1 89  SER 89  100 100 SER SER A . n 
A 1 90  THR 90  101 101 THR THR A . n 
A 1 91  LYS 91  102 102 LYS LYS A . n 
A 1 92  ASN 92  103 103 ASN ASN A . n 
A 1 93  VAL 93  104 104 VAL VAL A . n 
A 1 94  LYS 94  105 105 LYS LYS A . n 
A 1 95  PRO 95  106 106 PRO PRO A . n 
A 1 96  GLU 96  107 107 GLU GLU A . n 
A 1 97  ASN 97  108 108 ASN ASN A . n 
A 1 98  ARG 98  109 109 ARG ARG A . n 
A 1 99  PHE 99  110 110 PHE PHE A . n 
A 1 100 ASP 100 111 111 ASP ASP A . n 
A 1 101 ASN 101 112 112 ASN ASN A . n 
A 1 102 PRO 102 113 113 PRO PRO A . n 
A 1 103 GLU 103 114 114 GLU GLU A . n 
A 1 104 ILE 104 115 115 ILE ILE A . n 
A 1 105 ASN 105 116 116 ASN ASN A . n 
A 1 106 ARG 106 117 117 ARG ARG A . n 
A 1 107 ASN 107 118 118 ASN ASN A . n 
A 1 108 ASP 108 119 119 ASP ASP A . n 
A 1 109 LEU 109 120 120 LEU LEU A . n 
A 1 110 ARG 110 121 121 ARG ARG A . n 
A 1 111 ALA 111 122 122 ALA ALA A . n 
A 1 112 ILE 112 123 123 ILE ILE A . n 
A 1 113 LEU 113 124 124 LEU LEU A . n 
A 1 114 LEU 114 125 125 LEU LEU A . n 
A 1 115 ASN 115 126 126 ASN ASN A . n 
A 1 116 SER 116 127 127 SER SER A . n 
A 1 117 LEU 117 128 128 LEU LEU A . n 
A 1 118 GLU 118 129 129 GLU GLU A . n 
A 1 119 ASN 119 130 130 ASN ASN A . n 
A 1 120 ASP 120 131 131 ASP ASP A . n 
A 1 121 THR 121 132 132 THR THR A . n 
A 1 122 VAL 122 133 133 VAL VAL A . n 
A 1 123 ILE 123 134 134 ILE ILE A . n 
A 1 124 TRP 124 135 135 TRP TRP A . n 
A 1 125 ASP 125 136 136 ASP ASP A . n 
A 1 126 ARG 126 137 137 ARG ARG A . n 
A 1 127 LYS 127 138 138 LYS LYS A . n 
A 1 128 LEU 128 139 139 LEU LEU A . n 
A 1 129 VAL 129 140 140 VAL VAL A . n 
A 1 130 MET 130 141 141 MET MET A . n 
A 1 131 LEU 131 142 142 LEU LEU A . n 
A 1 132 GLU 132 143 143 GLU GLU A . n 
A 1 133 PRO 133 144 144 PRO PRO A . n 
A 1 134 GLY 134 145 145 GLY GLY A . n 
A 1 135 LYS 135 146 146 LYS LYS A . n 
A 1 136 LYS 136 147 147 LYS LYS A . n 
A 1 137 LYS 137 148 148 LYS LYS A . n 
A 1 138 TRP 138 149 149 TRP TRP A . n 
A 1 139 THR 139 150 150 THR THR A . n 
A 1 140 LEU 140 151 151 LEU LEU A . n 
A 1 141 THR 141 152 152 THR THR A . n 
A 1 142 PHE 142 153 153 PHE PHE A . n 
A 1 143 GLU 143 154 154 GLU GLU A . n 
A 1 144 ASN 144 155 155 ASN ASN A . n 
A 1 145 LYS 145 156 156 LYS LYS A . n 
A 1 146 PRO 146 157 157 PRO PRO A . n 
A 1 147 SER 147 158 158 SER SER A . n 
A 1 148 GLU 148 159 159 GLU GLU A . n 
A 1 149 THR 149 160 160 THR THR A . n 
A 1 150 ALA 150 161 161 ALA ALA A . n 
A 1 151 ASP 151 162 162 ASP ASP A . n 
A 1 152 LEU 152 163 163 LEU LEU A . n 
A 1 153 VAL 153 164 164 VAL VAL A . n 
A 1 154 ILE 154 165 165 ILE ILE A . n 
A 1 155 ILE 155 166 166 ILE ILE A . n 
A 1 156 ALA 156 167 167 ALA ALA A . n 
A 1 157 ASN 157 168 168 ASN ASN A . n 
A 1 158 GLY 158 169 169 GLY GLY A . n 
A 1 159 GLY 159 170 170 GLY GLY A . n 
A 1 160 MET 160 171 171 MET MET A . n 
A 1 161 SER 161 172 172 SER SER A . n 
A 1 162 LYS 162 173 173 LYS LYS A . n 
A 1 163 VAL 163 174 174 VAL VAL A . n 
A 1 164 ARG 164 175 175 ARG ARG A . n 
A 1 165 LYS 165 176 176 LYS LYS A . n 
A 1 166 PHE 166 177 177 PHE PHE A . n 
A 1 167 VAL 167 178 178 VAL VAL A . n 
A 1 168 THR 168 179 179 THR THR A . n 
A 1 169 ASP 169 180 180 ASP ASP A . n 
A 1 170 THR 170 181 181 THR THR A . n 
A 1 171 GLU 171 182 182 GLU GLU A . n 
A 1 172 VAL 172 183 183 VAL VAL A . n 
A 1 173 GLU 173 184 184 GLU GLU A . n 
A 1 174 GLU 174 185 185 GLU GLU A . n 
A 1 175 THR 175 186 186 THR THR A . n 
A 1 176 GLY 176 187 187 GLY GLY A . n 
A 1 177 THR 177 188 188 THR THR A . n 
A 1 178 PHE 178 189 189 PHE PHE A . n 
A 1 179 ASN 179 190 190 ASN ASN A . n 
A 1 180 ILE 180 191 191 ILE ILE A . n 
A 1 181 GLN 181 192 192 GLN GLN A . n 
A 1 182 ALA 182 193 193 ALA ALA A . n 
A 1 183 ASP 183 194 194 ASP ASP A . n 
A 1 184 ILE 184 195 195 ILE ILE A . n 
A 1 185 HIS 185 196 196 HIS HIS A . n 
A 1 186 HIS 186 197 197 HIS HIS A . n 
A 1 187 PRO 187 198 198 PRO PRO A . n 
A 1 188 GLU 188 199 199 GLU GLU A . n 
A 1 189 VAL 189 200 200 VAL VAL A . n 
A 1 190 ASN 190 201 201 ASN ASN A . n 
A 1 191 CYS 191 202 202 CYS CYS A . n 
A 1 192 PRO 192 203 203 PRO PRO A . n 
A 1 193 GLY 193 204 204 GLY GLY A . n 
A 1 194 PHE 194 205 205 PHE PHE A . n 
A 1 195 PHE 195 206 206 PHE PHE A . n 
A 1 196 GLN 196 207 207 GLN GLN A . n 
A 1 197 LEU 197 208 208 LEU LEU A . n 
A 1 198 CYS 198 209 209 CYS CYS A . n 
A 1 199 ASN 199 210 210 ASN ASN A . n 
A 1 200 GLY 200 211 211 GLY GLY A . n 
A 1 201 ASN 201 212 212 ASN ASN A . n 
A 1 202 ARG 202 213 213 ARG ARG A . n 
A 1 203 LEU 203 214 214 LEU LEU A . n 
A 1 204 MET 204 215 215 MET MET A . n 
A 1 205 ALA 205 216 216 ALA ALA A . n 
A 1 206 ALA 206 217 217 ALA ALA A . n 
A 1 207 HIS 207 218 218 HIS HIS A . n 
A 1 208 GLN 208 219 219 GLN GLN A . n 
A 1 209 GLY 209 220 220 GLY GLY A . n 
A 1 210 ASN 210 221 221 ASN ASN A . n 
A 1 211 LEU 211 222 222 LEU LEU A . n 
A 1 212 LEU 212 223 223 LEU LEU A . n 
A 1 213 PHE 213 224 224 PHE PHE A . n 
A 1 214 ALA 214 225 225 ALA ALA A . n 
A 1 215 ASN 215 226 226 ASN ASN A . n 
A 1 216 PRO 216 227 227 PRO PRO A . n 
A 1 217 ASN 217 228 228 ASN ASN A . n 
A 1 218 ASN 218 229 229 ASN ASN A . n 
A 1 219 ASN 219 230 230 ASN ASN A . n 
A 1 220 GLY 220 231 231 GLY GLY A . n 
A 1 221 ALA 221 232 232 ALA ALA A . n 
A 1 222 LEU 222 233 233 LEU LEU A . n 
A 1 223 HIS 223 234 234 HIS HIS A . n 
A 1 224 PHE 224 235 235 PHE PHE A . n 
A 1 225 GLY 225 236 236 GLY GLY A . n 
A 1 226 ILE 226 237 237 ILE ILE A . n 
A 1 227 SER 227 238 238 SER SER A . n 
A 1 228 PHE 228 239 239 PHE PHE A . n 
A 1 229 LYS 229 240 240 LYS LYS A . n 
A 1 230 THR 230 241 241 THR THR A . n 
A 1 231 PRO 231 242 242 PRO PRO A . n 
A 1 232 ASP 232 243 243 ASP ASP A . n 
A 1 233 GLU 233 244 244 GLU GLU A . n 
A 1 234 TRP 234 245 245 TRP TRP A . n 
A 1 235 LYS 235 246 246 LYS LYS A . n 
A 1 236 ASN 236 247 247 ASN ASN A . n 
A 1 237 GLN 237 248 248 GLN GLN A . n 
A 1 238 THR 238 249 249 THR THR A . n 
A 1 239 GLN 239 250 250 GLN GLN A . n 
A 1 240 VAL 240 251 251 VAL VAL A . n 
A 1 241 ASP 241 252 252 ASP ASP A . n 
A 1 242 PHE 242 253 253 PHE PHE A . n 
A 1 243 GLN 243 254 254 GLN GLN A . n 
A 1 244 ASN 244 255 255 ASN ASN A . n 
A 1 245 ARG 245 256 256 ARG ARG A . n 
A 1 246 ASN 246 257 257 ASN ASN A . n 
A 1 247 SER 247 258 258 SER SER A . n 
A 1 248 VAL 248 259 259 VAL VAL A . n 
A 1 249 VAL 249 260 260 VAL VAL A . n 
A 1 250 ASP 250 261 261 ASP ASP A . n 
A 1 251 PHE 251 262 262 PHE PHE A . n 
A 1 252 LEU 252 263 263 LEU LEU A . n 
A 1 253 LEU 253 264 264 LEU LEU A . n 
A 1 254 LYS 254 265 265 LYS LYS A . n 
A 1 255 GLU 255 266 266 GLU GLU A . n 
A 1 256 PHE 256 267 267 PHE PHE A . n 
A 1 257 SER 257 268 268 SER SER A . n 
A 1 258 ASP 258 269 269 ASP ASP A . n 
A 1 259 TRP 259 270 270 TRP TRP A . n 
A 1 260 ASP 260 271 271 ASP ASP A . n 
A 1 261 GLU 261 272 272 GLU GLU A . n 
A 1 262 ARG 262 273 273 ARG ARG A . n 
A 1 263 TYR 263 274 274 TYR TYR A . n 
A 1 264 LYS 264 275 275 LYS LYS A . n 
A 1 265 GLU 265 276 276 GLU GLU A . n 
A 1 266 LEU 266 277 277 LEU LEU A . n 
A 1 267 ILE 267 278 278 ILE ILE A . n 
A 1 268 ARG 268 279 279 ARG ARG A . n 
A 1 269 VAL 269 280 280 VAL VAL A . n 
A 1 270 THR 270 281 281 THR THR A . n 
A 1 271 SER 271 282 282 SER SER A . n 
A 1 272 SER 272 283 283 SER SER A . n 
A 1 273 PHE 273 284 284 PHE PHE A . n 
A 1 274 VAL 274 285 285 VAL VAL A . n 
A 1 275 GLY 275 286 286 GLY GLY A . n 
A 1 276 LEU 276 287 287 LEU LEU A . n 
A 1 277 ALA 277 288 288 ALA ALA A . n 
A 1 278 THR 278 289 289 THR THR A . n 
A 1 279 ARG 279 290 290 ARG ARG A . n 
A 1 280 ILE 280 291 291 ILE ILE A . n 
A 1 281 PHE 281 292 292 PHE PHE A . n 
A 1 282 PRO 282 293 293 PRO PRO A . n 
A 1 283 LEU 283 294 294 LEU LEU A . n 
A 1 284 GLY 284 295 295 GLY GLY A . n 
A 1 285 LYS 285 296 296 LYS LYS A . n 
A 1 286 SER 286 297 297 SER SER A . n 
A 1 287 TRP 287 298 298 TRP TRP A . n 
A 1 288 LYS 288 299 299 LYS LYS A . n 
A 1 289 SER 289 300 300 SER SER A . n 
A 1 290 LYS 290 301 301 LYS LYS A . n 
A 1 291 ARG 291 302 302 ARG ARG A . n 
A 1 292 PRO 292 303 303 PRO PRO A . n 
A 1 293 LEU 293 304 304 LEU LEU A . n 
A 1 294 PRO 294 305 305 PRO PRO A . n 
A 1 295 ILE 295 306 306 ILE ILE A . n 
A 1 296 THR 296 307 307 THR THR A . n 
A 1 297 MET 297 308 308 MET MET A . n 
A 1 298 ILE 298 309 309 ILE ILE A . n 
A 1 299 GLY 299 310 310 GLY GLY A . n 
A 1 300 ASP 300 311 311 ASP ASP A . n 
A 1 301 ALA 301 312 312 ALA ALA A . n 
A 1 302 ALA 302 313 313 ALA ALA A . n 
A 1 303 HIS 303 314 314 HIS HIS A . n 
A 1 304 LEU 304 315 315 LEU LEU A . n 
A 1 305 MET 305 316 316 MET MET A . n 
A 1 306 PRO 306 317 317 PRO PRO A . n 
A 1 307 PRO 307 318 318 PRO PRO A . n 
A 1 308 PHE 308 319 319 PHE PHE A . n 
A 1 309 ALA 309 320 320 ALA ALA A . n 
A 1 310 GLY 310 321 321 GLY GLY A . n 
A 1 311 GLN 311 322 322 GLN GLN A . n 
A 1 312 GLY 312 323 323 GLY GLY A . n 
A 1 313 VAL 313 324 324 VAL VAL A . n 
A 1 314 ASN 314 325 325 ASN ASN A . n 
A 1 315 SER 315 326 326 SER SER A . n 
A 1 316 GLY 316 327 327 GLY GLY A . n 
A 1 317 LEU 317 328 328 LEU LEU A . n 
A 1 318 MET 318 329 329 MET MET A . n 
A 1 319 ASP 319 330 330 ASP ASP A . n 
A 1 320 ALA 320 331 331 ALA ALA A . n 
A 1 321 LEU 321 332 332 LEU LEU A . n 
A 1 322 ILE 322 333 333 ILE ILE A . n 
A 1 323 LEU 323 334 334 LEU LEU A . n 
A 1 324 SER 324 335 335 SER SER A . n 
A 1 325 ASP 325 336 336 ASP ASP A . n 
A 1 326 ASN 326 337 337 ASN ASN A . n 
A 1 327 LEU 327 338 338 LEU LEU A . n 
A 1 328 THR 328 339 339 THR THR A . n 
A 1 329 ASN 329 340 340 ASN ASN A . n 
A 1 330 GLY 330 341 341 GLY GLY A . n 
A 1 331 LYS 331 342 342 LYS LYS A . n 
A 1 332 PHE 332 343 343 PHE PHE A . n 
A 1 333 ASN 333 344 344 ASN ASN A . n 
A 1 334 SER 334 345 345 SER SER A . n 
A 1 335 ILE 335 346 346 ILE ILE A . n 
A 1 336 GLU 336 347 347 GLU GLU A . n 
A 1 337 GLU 337 348 348 GLU GLU A . n 
A 1 338 ALA 338 349 349 ALA ALA A . n 
A 1 339 ILE 339 350 350 ILE ILE A . n 
A 1 340 GLU 340 351 351 GLU GLU A . n 
A 1 341 ASN 341 352 352 ASN ASN A . n 
A 1 342 TYR 342 353 353 TYR TYR A . n 
A 1 343 GLU 343 354 354 GLU GLU A . n 
A 1 344 GLN 344 355 355 GLN GLN A . n 
A 1 345 GLN 345 356 356 GLN GLN A . n 
A 1 346 MET 346 357 357 MET MET A . n 
A 1 347 PHE 347 358 358 PHE PHE A . n 
A 1 348 ILE 348 359 359 ILE ILE A . n 
A 1 349 TYR 349 360 360 TYR TYR A . n 
A 1 350 GLY 350 361 361 GLY GLY A . n 
A 1 351 LYS 351 362 362 LYS LYS A . n 
A 1 352 GLU 352 363 363 GLU GLU A . n 
A 1 353 ALA 353 364 364 ALA ALA A . n 
A 1 354 GLN 354 365 365 GLN GLN A . n 
A 1 355 GLU 355 366 366 GLU GLU A . n 
A 1 356 GLU 356 367 367 GLU GLU A . n 
A 1 357 SER 357 368 368 SER SER A . n 
A 1 358 THR 358 369 369 THR THR A . n 
A 1 359 GLN 359 370 370 GLN GLN A . n 
A 1 360 ASN 360 371 371 ASN ASN A . n 
A 1 361 GLU 361 372 372 GLU GLU A . n 
A 1 362 ILE 362 373 373 ILE ILE A . n 
A 1 363 GLU 363 374 374 GLU GLU A . n 
A 1 364 MET 364 375 375 MET MET A . n 
A 1 365 PHE 365 376 376 PHE PHE A . n 
A 1 366 LYS 366 377 377 LYS LYS A . n 
A 1 367 PRO 367 378 378 PRO PRO A . n 
A 1 368 ASP 368 379 379 ASP ASP A . n 
A 1 369 PHE 369 380 380 PHE PHE A . n 
A 1 370 THR 370 381 381 THR THR A . n 
A 1 371 PHE 371 382 382 PHE PHE A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        P77 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   P77 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FDA 1   401 401 FDA FDA A . 
C 3 P77 1   402 402 P77 PCL A . 
D 4 SO4 1   403 2   SO4 SO4 A . 
E 4 SO4 1   404 3   SO4 SO4 A . 
F 4 SO4 1   405 5   SO4 SO4 A . 
G 5 HOH 1   501 216 HOH HOH A . 
G 5 HOH 2   502 18  HOH HOH A . 
G 5 HOH 3   503 306 HOH HOH A . 
G 5 HOH 4   504 113 HOH HOH A . 
G 5 HOH 5   505 38  HOH HOH A . 
G 5 HOH 6   506 20  HOH HOH A . 
G 5 HOH 7   507 17  HOH HOH A . 
G 5 HOH 8   508 125 HOH HOH A . 
G 5 HOH 9   509 2   HOH HOH A . 
G 5 HOH 10  510 140 HOH HOH A . 
G 5 HOH 11  511 9   HOH HOH A . 
G 5 HOH 12  512 128 HOH HOH A . 
G 5 HOH 13  513 49  HOH HOH A . 
G 5 HOH 14  514 189 HOH HOH A . 
G 5 HOH 15  515 312 HOH HOH A . 
G 5 HOH 16  516 206 HOH HOH A . 
G 5 HOH 17  517 138 HOH HOH A . 
G 5 HOH 18  518 57  HOH HOH A . 
G 5 HOH 19  519 139 HOH HOH A . 
G 5 HOH 20  520 39  HOH HOH A . 
G 5 HOH 21  521 36  HOH HOH A . 
G 5 HOH 22  522 4   HOH HOH A . 
G 5 HOH 23  523 133 HOH HOH A . 
G 5 HOH 24  524 123 HOH HOH A . 
G 5 HOH 25  525 89  HOH HOH A . 
G 5 HOH 26  526 25  HOH HOH A . 
G 5 HOH 27  527 239 HOH HOH A . 
G 5 HOH 28  528 15  HOH HOH A . 
G 5 HOH 29  529 178 HOH HOH A . 
G 5 HOH 30  530 26  HOH HOH A . 
G 5 HOH 31  531 50  HOH HOH A . 
G 5 HOH 32  532 52  HOH HOH A . 
G 5 HOH 33  533 150 HOH HOH A . 
G 5 HOH 34  534 92  HOH HOH A . 
G 5 HOH 35  535 44  HOH HOH A . 
G 5 HOH 36  536 64  HOH HOH A . 
G 5 HOH 37  537 309 HOH HOH A . 
G 5 HOH 38  538 280 HOH HOH A . 
G 5 HOH 39  539 28  HOH HOH A . 
G 5 HOH 40  540 65  HOH HOH A . 
G 5 HOH 41  541 287 HOH HOH A . 
G 5 HOH 42  542 134 HOH HOH A . 
G 5 HOH 43  543 41  HOH HOH A . 
G 5 HOH 44  544 79  HOH HOH A . 
G 5 HOH 45  545 307 HOH HOH A . 
G 5 HOH 46  546 12  HOH HOH A . 
G 5 HOH 47  547 100 HOH HOH A . 
G 5 HOH 48  548 185 HOH HOH A . 
G 5 HOH 49  549 151 HOH HOH A . 
G 5 HOH 50  550 159 HOH HOH A . 
G 5 HOH 51  551 34  HOH HOH A . 
G 5 HOH 52  552 23  HOH HOH A . 
G 5 HOH 53  553 174 HOH HOH A . 
G 5 HOH 54  554 66  HOH HOH A . 
G 5 HOH 55  555 116 HOH HOH A . 
G 5 HOH 56  556 254 HOH HOH A . 
G 5 HOH 57  557 126 HOH HOH A . 
G 5 HOH 58  558 11  HOH HOH A . 
G 5 HOH 59  559 210 HOH HOH A . 
G 5 HOH 60  560 83  HOH HOH A . 
G 5 HOH 61  561 91  HOH HOH A . 
G 5 HOH 62  562 29  HOH HOH A . 
G 5 HOH 63  563 291 HOH HOH A . 
G 5 HOH 64  564 56  HOH HOH A . 
G 5 HOH 65  565 219 HOH HOH A . 
G 5 HOH 66  566 3   HOH HOH A . 
G 5 HOH 67  567 121 HOH HOH A . 
G 5 HOH 68  568 107 HOH HOH A . 
G 5 HOH 69  569 72  HOH HOH A . 
G 5 HOH 70  570 303 HOH HOH A . 
G 5 HOH 71  571 236 HOH HOH A . 
G 5 HOH 72  572 35  HOH HOH A . 
G 5 HOH 73  573 308 HOH HOH A . 
G 5 HOH 74  574 221 HOH HOH A . 
G 5 HOH 75  575 16  HOH HOH A . 
G 5 HOH 76  576 32  HOH HOH A . 
G 5 HOH 77  577 166 HOH HOH A . 
G 5 HOH 78  578 146 HOH HOH A . 
G 5 HOH 79  579 131 HOH HOH A . 
G 5 HOH 80  580 102 HOH HOH A . 
G 5 HOH 81  581 42  HOH HOH A . 
G 5 HOH 82  582 40  HOH HOH A . 
G 5 HOH 83  583 30  HOH HOH A . 
G 5 HOH 84  584 48  HOH HOH A . 
G 5 HOH 85  585 1   HOH HOH A . 
G 5 HOH 86  586 228 HOH HOH A . 
G 5 HOH 87  587 117 HOH HOH A . 
G 5 HOH 88  588 122 HOH HOH A . 
G 5 HOH 89  589 157 HOH HOH A . 
G 5 HOH 90  590 101 HOH HOH A . 
G 5 HOH 91  591 284 HOH HOH A . 
G 5 HOH 92  592 304 HOH HOH A . 
G 5 HOH 93  593 60  HOH HOH A . 
G 5 HOH 94  594 148 HOH HOH A . 
G 5 HOH 95  595 195 HOH HOH A . 
G 5 HOH 96  596 263 HOH HOH A . 
G 5 HOH 97  597 21  HOH HOH A . 
G 5 HOH 98  598 97  HOH HOH A . 
G 5 HOH 99  599 81  HOH HOH A . 
G 5 HOH 100 600 171 HOH HOH A . 
G 5 HOH 101 601 238 HOH HOH A . 
G 5 HOH 102 602 96  HOH HOH A . 
G 5 HOH 103 603 173 HOH HOH A . 
G 5 HOH 104 604 233 HOH HOH A . 
G 5 HOH 105 605 136 HOH HOH A . 
G 5 HOH 106 606 61  HOH HOH A . 
G 5 HOH 107 607 190 HOH HOH A . 
G 5 HOH 108 608 5   HOH HOH A . 
G 5 HOH 109 609 7   HOH HOH A . 
G 5 HOH 110 610 243 HOH HOH A . 
G 5 HOH 111 611 237 HOH HOH A . 
G 5 HOH 112 612 271 HOH HOH A . 
G 5 HOH 113 613 24  HOH HOH A . 
G 5 HOH 114 614 160 HOH HOH A . 
G 5 HOH 115 615 184 HOH HOH A . 
G 5 HOH 116 616 13  HOH HOH A . 
G 5 HOH 117 617 177 HOH HOH A . 
G 5 HOH 118 618 69  HOH HOH A . 
G 5 HOH 119 619 227 HOH HOH A . 
G 5 HOH 120 620 276 HOH HOH A . 
G 5 HOH 121 621 70  HOH HOH A . 
G 5 HOH 122 622 141 HOH HOH A . 
G 5 HOH 123 623 104 HOH HOH A . 
G 5 HOH 124 624 191 HOH HOH A . 
G 5 HOH 125 625 31  HOH HOH A . 
G 5 HOH 126 626 155 HOH HOH A . 
G 5 HOH 127 627 46  HOH HOH A . 
G 5 HOH 128 628 43  HOH HOH A . 
G 5 HOH 129 629 202 HOH HOH A . 
G 5 HOH 130 630 142 HOH HOH A . 
G 5 HOH 131 631 156 HOH HOH A . 
G 5 HOH 132 632 194 HOH HOH A . 
G 5 HOH 133 633 90  HOH HOH A . 
G 5 HOH 134 634 67  HOH HOH A . 
G 5 HOH 135 635 302 HOH HOH A . 
G 5 HOH 136 636 240 HOH HOH A . 
G 5 HOH 137 637 193 HOH HOH A . 
G 5 HOH 138 638 95  HOH HOH A . 
G 5 HOH 139 639 272 HOH HOH A . 
G 5 HOH 140 640 63  HOH HOH A . 
G 5 HOH 141 641 204 HOH HOH A . 
G 5 HOH 142 642 14  HOH HOH A . 
G 5 HOH 143 643 257 HOH HOH A . 
G 5 HOH 144 644 88  HOH HOH A . 
G 5 HOH 145 645 192 HOH HOH A . 
G 5 HOH 146 646 45  HOH HOH A . 
G 5 HOH 147 647 73  HOH HOH A . 
G 5 HOH 148 648 279 HOH HOH A . 
G 5 HOH 149 649 62  HOH HOH A . 
G 5 HOH 150 650 260 HOH HOH A . 
G 5 HOH 151 651 120 HOH HOH A . 
G 5 HOH 152 652 75  HOH HOH A . 
G 5 HOH 153 653 299 HOH HOH A . 
G 5 HOH 154 654 106 HOH HOH A . 
G 5 HOH 155 655 258 HOH HOH A . 
G 5 HOH 156 656 135 HOH HOH A . 
G 5 HOH 157 657 137 HOH HOH A . 
G 5 HOH 158 658 264 HOH HOH A . 
G 5 HOH 159 659 211 HOH HOH A . 
G 5 HOH 160 660 68  HOH HOH A . 
G 5 HOH 161 661 111 HOH HOH A . 
G 5 HOH 162 662 152 HOH HOH A . 
G 5 HOH 163 663 296 HOH HOH A . 
G 5 HOH 164 664 19  HOH HOH A . 
G 5 HOH 165 665 266 HOH HOH A . 
G 5 HOH 166 666 130 HOH HOH A . 
G 5 HOH 167 667 298 HOH HOH A . 
G 5 HOH 168 668 172 HOH HOH A . 
G 5 HOH 169 669 8   HOH HOH A . 
G 5 HOH 170 670 87  HOH HOH A . 
G 5 HOH 171 671 84  HOH HOH A . 
G 5 HOH 172 672 124 HOH HOH A . 
G 5 HOH 173 673 118 HOH HOH A . 
G 5 HOH 174 674 74  HOH HOH A . 
G 5 HOH 175 675 53  HOH HOH A . 
G 5 HOH 176 676 268 HOH HOH A . 
G 5 HOH 177 677 305 HOH HOH A . 
G 5 HOH 178 678 6   HOH HOH A . 
G 5 HOH 179 679 145 HOH HOH A . 
G 5 HOH 180 680 33  HOH HOH A . 
G 5 HOH 181 681 311 HOH HOH A . 
G 5 HOH 182 682 250 HOH HOH A . 
G 5 HOH 183 683 55  HOH HOH A . 
G 5 HOH 184 684 22  HOH HOH A . 
G 5 HOH 185 685 132 HOH HOH A . 
G 5 HOH 186 686 103 HOH HOH A . 
G 5 HOH 187 687 175 HOH HOH A . 
G 5 HOH 188 688 109 HOH HOH A . 
G 5 HOH 189 689 209 HOH HOH A . 
G 5 HOH 190 690 289 HOH HOH A . 
G 5 HOH 191 691 167 HOH HOH A . 
G 5 HOH 192 692 169 HOH HOH A . 
G 5 HOH 193 693 108 HOH HOH A . 
G 5 HOH 194 694 85  HOH HOH A . 
G 5 HOH 195 695 129 HOH HOH A . 
G 5 HOH 196 696 197 HOH HOH A . 
G 5 HOH 197 697 59  HOH HOH A . 
G 5 HOH 198 698 114 HOH HOH A . 
G 5 HOH 199 699 77  HOH HOH A . 
G 5 HOH 200 700 153 HOH HOH A . 
G 5 HOH 201 701 215 HOH HOH A . 
G 5 HOH 202 702 214 HOH HOH A . 
G 5 HOH 203 703 165 HOH HOH A . 
G 5 HOH 204 704 270 HOH HOH A . 
G 5 HOH 205 705 119 HOH HOH A . 
G 5 HOH 206 706 143 HOH HOH A . 
G 5 HOH 207 707 51  HOH HOH A . 
G 5 HOH 208 708 54  HOH HOH A . 
G 5 HOH 209 709 205 HOH HOH A . 
G 5 HOH 210 710 242 HOH HOH A . 
G 5 HOH 211 711 295 HOH HOH A . 
G 5 HOH 212 712 226 HOH HOH A . 
G 5 HOH 213 713 198 HOH HOH A . 
G 5 HOH 214 714 201 HOH HOH A . 
G 5 HOH 215 715 183 HOH HOH A . 
G 5 HOH 216 716 262 HOH HOH A . 
G 5 HOH 217 717 162 HOH HOH A . 
G 5 HOH 218 718 47  HOH HOH A . 
G 5 HOH 219 719 176 HOH HOH A . 
G 5 HOH 220 720 58  HOH HOH A . 
G 5 HOH 221 721 168 HOH HOH A . 
G 5 HOH 222 722 248 HOH HOH A . 
G 5 HOH 223 723 94  HOH HOH A . 
G 5 HOH 224 724 37  HOH HOH A . 
G 5 HOH 225 725 286 HOH HOH A . 
G 5 HOH 226 726 158 HOH HOH A . 
G 5 HOH 227 727 182 HOH HOH A . 
G 5 HOH 228 728 261 HOH HOH A . 
G 5 HOH 229 729 110 HOH HOH A . 
G 5 HOH 230 730 246 HOH HOH A . 
G 5 HOH 231 731 196 HOH HOH A . 
G 5 HOH 232 732 225 HOH HOH A . 
G 5 HOH 233 733 86  HOH HOH A . 
G 5 HOH 234 734 161 HOH HOH A . 
G 5 HOH 235 735 275 HOH HOH A . 
G 5 HOH 236 736 251 HOH HOH A . 
G 5 HOH 237 737 252 HOH HOH A . 
G 5 HOH 238 738 234 HOH HOH A . 
G 5 HOH 239 739 300 HOH HOH A . 
G 5 HOH 240 740 186 HOH HOH A . 
G 5 HOH 241 741 213 HOH HOH A . 
G 5 HOH 242 742 269 HOH HOH A . 
G 5 HOH 243 743 220 HOH HOH A . 
G 5 HOH 244 744 249 HOH HOH A . 
G 5 HOH 245 745 292 HOH HOH A . 
G 5 HOH 246 746 127 HOH HOH A . 
G 5 HOH 247 747 222 HOH HOH A . 
G 5 HOH 248 748 310 HOH HOH A . 
G 5 HOH 249 749 274 HOH HOH A . 
G 5 HOH 250 750 283 HOH HOH A . 
G 5 HOH 251 751 180 HOH HOH A . 
G 5 HOH 252 752 224 HOH HOH A . 
G 5 HOH 253 753 244 HOH HOH A . 
G 5 HOH 254 754 82  HOH HOH A . 
G 5 HOH 255 755 144 HOH HOH A . 
G 5 HOH 256 756 163 HOH HOH A . 
G 5 HOH 257 757 170 HOH HOH A . 
G 5 HOH 258 758 188 HOH HOH A . 
G 5 HOH 259 759 187 HOH HOH A . 
G 5 HOH 260 760 278 HOH HOH A . 
G 5 HOH 261 761 223 HOH HOH A . 
G 5 HOH 262 762 115 HOH HOH A . 
G 5 HOH 263 763 282 HOH HOH A . 
G 5 HOH 264 764 297 HOH HOH A . 
G 5 HOH 265 765 229 HOH HOH A . 
G 5 HOH 266 766 281 HOH HOH A . 
G 5 HOH 267 767 217 HOH HOH A . 
G 5 HOH 268 768 200 HOH HOH A . 
G 5 HOH 269 769 181 HOH HOH A . 
G 5 HOH 270 770 256 HOH HOH A . 
G 5 HOH 271 771 78  HOH HOH A . 
G 5 HOH 272 772 288 HOH HOH A . 
G 5 HOH 273 773 277 HOH HOH A . 
G 5 HOH 274 774 99  HOH HOH A . 
G 5 HOH 275 775 112 HOH HOH A . 
G 5 HOH 276 776 293 HOH HOH A . 
G 5 HOH 277 777 301 HOH HOH A . 
G 5 HOH 278 778 147 HOH HOH A . 
G 5 HOH 279 779 247 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21.2_5419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HJV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     97.593 
_cell.length_a_esd                 ? 
_cell.length_b                     97.593 
_cell.length_b_esd                 ? 
_cell.length_c                     168.285 
_cell.length_c_esd                 ? 
_cell.volume                       1388076.416 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9HJV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                179 
_symmetry.space_group_name_Hall            'P 65 2 (x,y,z+1/12)' 
_symmetry.space_group_name_H-M             'P 65 2 2' 
_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                   9HJV 
_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             2.78 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.69 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'29 %w/v PEG4000, 0.1 M sodium citrate (pH 6.5), 0.1 M magnesium acetate, 0.1 M ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9763 
_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                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9763 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HJV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.2 
_reflns.d_resolution_low                               84.52 
_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                                     24742 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                22.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.991 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.2 
_reflns_shell.d_res_low                                     2.27 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2107 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.776 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.74 
_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                                 9HJV 
_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                            2.20 
_refine.ls_d_res_low                             75.53 
_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                     24692 
_refine.ls_number_reflns_R_free                  1270 
_refine.ls_number_reflns_R_work                  23422 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.64 
_refine.ls_percent_reflns_R_free                 5.14 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1737 
_refine.ls_R_factor_R_free                       0.2217 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1711 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       '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                 21.2611 
_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                            0.2311 
_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                       2.20 
_refine_hist.d_res_low                        75.53 
_refine_hist.number_atoms_solvent             279 
_refine_hist.number_atoms_total               3301 
_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        2929 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         93 
_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' ? 0.0070  ? 3167 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8806  ? 4304 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0544  ? 456  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0064  ? 561  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 17.7797 ? 1233 ? 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' 2.20 2.29  . . 132 2539 99.33 . . . . 0.2113 . . . . . . . . . . . 0.2899 
'X-RAY DIFFRACTION' 2.29 2.39  . . 137 2524 99.00 . . . . 0.2039 . . . . . . . . . . . 0.2855 
'X-RAY DIFFRACTION' 2.39 2.52  . . 130 2550 99.59 . . . . 0.1884 . . . . . . . . . . . 0.2526 
'X-RAY DIFFRACTION' 2.52 2.68  . . 147 2556 99.78 . . . . 0.1806 . . . . . . . . . . . 0.2238 
'X-RAY DIFFRACTION' 2.68 2.88  . . 139 2573 99.78 . . . . 0.1856 . . . . . . . . . . . 0.2138 
'X-RAY DIFFRACTION' 2.88 3.17  . . 148 2581 99.93 . . . . 0.1835 . . . . . . . . . . . 0.2629 
'X-RAY DIFFRACTION' 3.17 3.63  . . 131 2631 99.96 . . . . 0.1614 . . . . . . . . . . . 0.2480 
'X-RAY DIFFRACTION' 3.63 4.58  . . 146 2637 99.50 . . . . 0.1415 . . . . . . . . . . . 0.1530 
'X-RAY DIFFRACTION' 4.58 75.53 . . 160 2831 99.90 . . . . 0.1671 . . . . . . . . . . . 0.2185 
# 
_struct.entry_id                     9HJV 
_struct.title                        'Crystal structure of flavin-dependent monooxygenase Tet(X4) in complex with prochlorperazine' 
_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        9HJV 
_struct_keywords.text            'Flavin-dependent monooxygenase Tet(X4), OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A3T0V9Y5_ECOLX 
_struct_ref.pdbx_db_accession          A0A3T0V9Y5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NLLSDKNVAIIGGGPVGLTMAKLLQQNGIDVSVYERDNDREARIFGGTLDLHKGSGQEAMKKAGLLQTYYDLALPMGVNI
ADEKGNILSTKNVKPENRFDNPEINRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVIIANGGM
SKVRKFVTDTEVEETGTFNIQADIHHPEVNCPGFFQLCNGNRLMAAHQGNLLFANPNNNGALHFGISFKTPDEWKNQTQV
DFQNRNSVVDFLLKEFSDWDERYKELIRVTSSFVGLATRIFPLGKSWKSKRPLPITMIGDAAHLMPPFAGQGVNSGLMDA
LILSDNLTNGKFNSIEEAIENYEQQMFIYGKEAQEESTQNEIEMFKPDFTF
;
_struct_ref.pdbx_align_begin           9 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9HJV 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 371 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A3T0V9Y5 
_struct_ref_seq.db_align_beg                  9 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  379 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       12 
_struct_ref_seq.pdbx_auth_seq_align_end       382 
# 
_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)' 1920  ? 
1 MORE         -42   ? 
1 'SSA (A^2)'  17100 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 GLY A 14  ? GLN A 26  ? GLY A 25  GLN A 37  1 ? 13 
HELX_P HELX_P2  AA2 SER A 55  ? ALA A 63  ? SER A 66  ALA A 74  1 ? 9  
HELX_P HELX_P3  AA3 LEU A 65  ? ALA A 73  ? LEU A 76  ALA A 84  1 ? 9  
HELX_P HELX_P4  AA4 LYS A 94  ? ARG A 98  ? LYS A 105 ARG A 109 5 ? 5  
HELX_P HELX_P5  AA5 ASN A 105 ? SER A 116 ? ASN A 116 SER A 127 1 ? 12 
HELX_P HELX_P6  AA6 HIS A 186 ? CYS A 191 ? HIS A 197 CYS A 202 1 ? 6  
HELX_P HELX_P7  AA7 CYS A 191 ? ASN A 199 ? CYS A 202 ASN A 210 1 ? 9  
HELX_P HELX_P8  AA8 PRO A 231 ? LYS A 235 ? PRO A 242 LYS A 246 5 ? 5  
HELX_P HELX_P9  AA9 ASN A 244 ? PHE A 256 ? ASN A 255 PHE A 267 1 ? 13 
HELX_P HELX_P10 AB1 ASP A 260 ? THR A 270 ? ASP A 271 THR A 281 1 ? 11 
HELX_P HELX_P11 AB2 GLY A 299 ? LEU A 304 ? GLY A 310 LEU A 315 1 ? 6  
HELX_P HELX_P12 AB3 GLY A 312 ? ASN A 329 ? GLY A 323 ASN A 340 1 ? 18 
HELX_P HELX_P13 AB4 SER A 334 ? PHE A 365 ? SER A 345 PHE A 376 1 ? 32 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 7 ? 
AA4 ? 3 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? 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 VAL A 122 ? ILE A 123 ? VAL A 133 ILE A 134 
AA1 2 ASP A 30  ? TYR A 34  ? ASP A 41  TYR A 45  
AA1 3 ASN A 7   ? ILE A 11  ? ASN A 18  ILE A 22  
AA1 4 LEU A 152 ? ILE A 155 ? LEU A 163 ILE A 166 
AA1 5 ILE A 295 ? MET A 297 ? ILE A 306 MET A 308 
AA2 1 LEU A 49  ? ASP A 50  ? LEU A 60  ASP A 61  
AA2 2 GLU A 103 ? ILE A 104 ? GLU A 114 ILE A 115 
AA3 1 ILE A 87  ? LYS A 91  ? ILE A 98  LYS A 102 
AA3 2 VAL A 78  ? ALA A 81  ? VAL A 89  ALA A 92  
AA3 3 ARG A 202 ? HIS A 207 ? ARG A 213 HIS A 218 
AA3 4 ASN A 210 ? ASN A 218 ? ASN A 221 ASN A 229 
AA3 5 ALA A 221 ? LYS A 229 ? ALA A 232 LYS A 240 
AA3 6 GLU A 173 ? ILE A 184 ? GLU A 184 ILE A 195 
AA3 7 VAL A 274 ? ILE A 280 ? VAL A 285 ILE A 291 
AA4 1 LEU A 128 ? PRO A 133 ? LEU A 139 PRO A 144 
AA4 2 TRP A 138 ? PHE A 142 ? TRP A 149 PHE A 153 
AA4 3 LYS A 145 ? ALA A 150 ? LYS A 156 ALA A 161 
# 
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 O ILE A 123 ? O ILE A 134 N VAL A 33  ? N VAL A 44  
AA1 2 3 O SER A 32  ? O SER A 43  N ILE A 10  ? N ILE A 21  
AA1 3 4 N ALA A 9   ? N ALA A 20  O LEU A 152 ? O LEU A 163 
AA1 4 5 N ILE A 155 ? N ILE A 166 O THR A 296 ? O THR A 307 
AA2 1 2 N LEU A 49  ? N LEU A 60  O ILE A 104 ? O ILE A 115 
AA3 1 2 O LYS A 91  ? O LYS A 102 N VAL A 78  ? N VAL A 89  
AA3 2 3 N ASN A 79  ? N ASN A 90  O ARG A 202 ? O ARG A 213 
AA3 3 4 N ALA A 205 ? N ALA A 216 O LEU A 212 ? O LEU A 223 
AA3 4 5 N ASN A 218 ? N ASN A 229 O ALA A 221 ? O ALA A 232 
AA3 5 6 O PHE A 228 ? O PHE A 239 N PHE A 178 ? N PHE A 189 
AA3 6 7 N GLU A 173 ? N GLU A 184 O ILE A 280 ? O ILE A 291 
AA4 1 2 N VAL A 129 ? N VAL A 140 O THR A 141 ? O THR A 152 
AA4 2 3 N LEU A 140 ? N LEU A 151 O GLU A 148 ? O GLU A 159 
# 
_pdbx_entry_details.entry_id                   9HJV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 66  ? ? -134.38 -94.46 
2 1 ASN A 112 ? ? -166.36 65.24  
3 1 ASN A 228 ? ? -156.03 72.06  
4 1 TRP A 245 ? ? -86.64  40.78  
5 1 ASN A 247 ? ? -140.98 24.41  
6 1 GLN A 250 ? ? 72.50   -42.29 
7 1 HIS A 314 ? ? -157.13 43.03  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z          
2  x-y,x,z+5/6    
3  y,-x+y,z+1/6   
4  -y,x-y,z+2/3   
5  -x+y,-x,z+1/3  
6  x-y,-y,-z      
7  -x,-x+y,-z+1/3 
8  -x,-y,z+1/2    
9  y,x,-z+2/3     
10 -y,-x,-z+1/6   
11 -x+y,y,-z+1/2  
12 x,x-y,-z+5/6   
# 
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 2.1682146382  -34.6655682625 -3.99009994252 0.152590558036 ? 0.00730693536133 ? 0.0369225387757  ? 
0.153525620105 ? -0.00857196728424 ? 0.159742345415 ? 1.8926435896  ? -0.67648138662 ? 1.01363134654 ? 0.981665793838 ? 
-0.44591389902  ? 1.23799659315  ? 0.00166289865881 ? -0.025184986333 ? -0.210645404955 ? 0.0544698350181 ? 0.0345604853724 ? 
0.0344729877686 ? 0.057503094928  ? -0.0242180711323  ? -0.0337548075346 ? 
2 'X-RAY DIFFRACTION' ? refined 8.47080698047 -26.286219973  2.6669865248   0.261810144777 ? 0.0073015449775  ? -0.0193246898753 ? 
0.218248193063 ? -0.00378442485554 ? 0.196914033992 ? 2.07964078973 ? -1.72362407538 ? 1.1079995055  ? 1.93876051176  ? 
-0.841934909903 ? 0.937676642168 ? -0.240915810433  ? -0.159647460738 ? 0.1697678431    ? 0.340769937732  ? 0.0830184856338 ? 
-0.234603685876 ? -0.192923911848 ? -0.00412925339263 ? 0.150259339282   ? 
# 
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 12  ? A 221 A 232 ? ? 
;chain 'A' and (resid   12  through  232 )
;
2 'X-RAY DIFFRACTION' 2 A 222 A 233 ? A 371 A 382 ? ? 
;chain 'A' and (resid  233  through  382 )
;
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
FDA PA     P  N S 88  
FDA O1A    O  N N 89  
FDA O2A    O  N N 90  
FDA O5B    O  N N 91  
FDA C5B    C  N N 92  
FDA C4B    C  N R 93  
FDA O4B    O  N N 94  
FDA C3B    C  N S 95  
FDA O3B    O  N N 96  
FDA C2B    C  N R 97  
FDA O2B    O  N N 98  
FDA C1B    C  N R 99  
FDA N9A    N  Y N 100 
FDA C8A    C  Y N 101 
FDA N7A    N  Y N 102 
FDA C5A    C  Y N 103 
FDA C6A    C  Y N 104 
FDA N6A    N  N N 105 
FDA N1A    N  Y N 106 
FDA C2A    C  Y N 107 
FDA N3A    N  Y N 108 
FDA C4A    C  Y N 109 
FDA N1     N  N N 110 
FDA C2     C  N N 111 
FDA O2     O  N N 112 
FDA N3     N  N N 113 
FDA C4     C  N N 114 
FDA O4     O  N N 115 
FDA C4X    C  N N 116 
FDA N5     N  N N 117 
FDA C5X    C  Y N 118 
FDA C6     C  Y N 119 
FDA C7     C  Y N 120 
FDA C7M    C  N N 121 
FDA C8     C  Y N 122 
FDA C8M    C  N N 123 
FDA C9     C  Y N 124 
FDA C9A    C  Y N 125 
FDA N10    N  N N 126 
FDA C10    C  N N 127 
FDA "C1'"  C  N N 128 
FDA "C2'"  C  N S 129 
FDA "O2'"  O  N N 130 
FDA "C3'"  C  N S 131 
FDA "O3'"  O  N N 132 
FDA "C4'"  C  N R 133 
FDA "O4'"  O  N N 134 
FDA "C5'"  C  N N 135 
FDA "O5'"  O  N N 136 
FDA P      P  N R 137 
FDA O1P    O  N N 138 
FDA O2P    O  N N 139 
FDA O3P    O  N N 140 
FDA HOA2   H  N N 141 
FDA H51A   H  N N 142 
FDA H52A   H  N N 143 
FDA H4B    H  N N 144 
FDA H3B    H  N N 145 
FDA HO3A   H  N N 146 
FDA H2B    H  N N 147 
FDA HO2A   H  N N 148 
FDA H1B    H  N N 149 
FDA H8A    H  N N 150 
FDA H61A   H  N N 151 
FDA H62A   H  N N 152 
FDA H2A    H  N N 153 
FDA HN1    H  N N 154 
FDA HN3    H  N N 155 
FDA HN5    H  N N 156 
FDA H6     H  N N 157 
FDA HM71   H  N N 158 
FDA HM72   H  N N 159 
FDA HM73   H  N N 160 
FDA HM81   H  N N 161 
FDA HM82   H  N N 162 
FDA HM83   H  N N 163 
FDA H9     H  N N 164 
FDA "H1'1" H  N N 165 
FDA "H1'2" H  N N 166 
FDA "H2'"  H  N N 167 
FDA "HO2'" H  N N 168 
FDA "H3'"  H  N N 169 
FDA "HO3'" H  N N 170 
FDA "H4'"  H  N N 171 
FDA "HO4'" H  N N 172 
FDA "H5'1" H  N N 173 
FDA "H5'2" H  N N 174 
FDA HOP2   H  N N 175 
GLN N      N  N N 176 
GLN CA     C  N S 177 
GLN C      C  N N 178 
GLN O      O  N N 179 
GLN CB     C  N N 180 
GLN CG     C  N N 181 
GLN CD     C  N N 182 
GLN OE1    O  N N 183 
GLN NE2    N  N N 184 
GLN OXT    O  N N 185 
GLN H      H  N N 186 
GLN H2     H  N N 187 
GLN HA     H  N N 188 
GLN HB2    H  N N 189 
GLN HB3    H  N N 190 
GLN HG2    H  N N 191 
GLN HG3    H  N N 192 
GLN HE21   H  N N 193 
GLN HE22   H  N N 194 
GLN HXT    H  N N 195 
GLU N      N  N N 196 
GLU CA     C  N S 197 
GLU C      C  N N 198 
GLU O      O  N N 199 
GLU CB     C  N N 200 
GLU CG     C  N N 201 
GLU CD     C  N N 202 
GLU OE1    O  N N 203 
GLU OE2    O  N N 204 
GLU OXT    O  N N 205 
GLU H      H  N N 206 
GLU H2     H  N N 207 
GLU HA     H  N N 208 
GLU HB2    H  N N 209 
GLU HB3    H  N N 210 
GLU HG2    H  N N 211 
GLU HG3    H  N N 212 
GLU HE2    H  N N 213 
GLU HXT    H  N N 214 
GLY N      N  N N 215 
GLY CA     C  N N 216 
GLY C      C  N N 217 
GLY O      O  N N 218 
GLY OXT    O  N N 219 
GLY H      H  N N 220 
GLY H2     H  N N 221 
GLY HA2    H  N N 222 
GLY HA3    H  N N 223 
GLY HXT    H  N N 224 
HIS N      N  N N 225 
HIS CA     C  N S 226 
HIS C      C  N N 227 
HIS O      O  N N 228 
HIS CB     C  N N 229 
HIS CG     C  Y N 230 
HIS ND1    N  Y N 231 
HIS CD2    C  Y N 232 
HIS CE1    C  Y N 233 
HIS NE2    N  Y N 234 
HIS OXT    O  N N 235 
HIS H      H  N N 236 
HIS H2     H  N N 237 
HIS HA     H  N N 238 
HIS HB2    H  N N 239 
HIS HB3    H  N N 240 
HIS HD1    H  N N 241 
HIS HD2    H  N N 242 
HIS HE1    H  N N 243 
HIS HE2    H  N N 244 
HIS HXT    H  N N 245 
HOH O      O  N N 246 
HOH H1     H  N N 247 
HOH H2     H  N N 248 
ILE N      N  N N 249 
ILE CA     C  N S 250 
ILE C      C  N N 251 
ILE O      O  N N 252 
ILE CB     C  N S 253 
ILE CG1    C  N N 254 
ILE CG2    C  N N 255 
ILE CD1    C  N N 256 
ILE OXT    O  N N 257 
ILE H      H  N N 258 
ILE H2     H  N N 259 
ILE HA     H  N N 260 
ILE HB     H  N N 261 
ILE HG12   H  N N 262 
ILE HG13   H  N N 263 
ILE HG21   H  N N 264 
ILE HG22   H  N N 265 
ILE HG23   H  N N 266 
ILE HD11   H  N N 267 
ILE HD12   H  N N 268 
ILE HD13   H  N N 269 
ILE HXT    H  N N 270 
LEU N      N  N N 271 
LEU CA     C  N S 272 
LEU C      C  N N 273 
LEU O      O  N N 274 
LEU CB     C  N N 275 
LEU CG     C  N N 276 
LEU CD1    C  N N 277 
LEU CD2    C  N N 278 
LEU OXT    O  N N 279 
LEU H      H  N N 280 
LEU H2     H  N N 281 
LEU HA     H  N N 282 
LEU HB2    H  N N 283 
LEU HB3    H  N N 284 
LEU HG     H  N N 285 
LEU HD11   H  N N 286 
LEU HD12   H  N N 287 
LEU HD13   H  N N 288 
LEU HD21   H  N N 289 
LEU HD22   H  N N 290 
LEU HD23   H  N N 291 
LEU HXT    H  N N 292 
LYS N      N  N N 293 
LYS CA     C  N S 294 
LYS C      C  N N 295 
LYS O      O  N N 296 
LYS CB     C  N N 297 
LYS CG     C  N N 298 
LYS CD     C  N N 299 
LYS CE     C  N N 300 
LYS NZ     N  N N 301 
LYS OXT    O  N N 302 
LYS H      H  N N 303 
LYS H2     H  N N 304 
LYS HA     H  N N 305 
LYS HB2    H  N N 306 
LYS HB3    H  N N 307 
LYS HG2    H  N N 308 
LYS HG3    H  N N 309 
LYS HD2    H  N N 310 
LYS HD3    H  N N 311 
LYS HE2    H  N N 312 
LYS HE3    H  N N 313 
LYS HZ1    H  N N 314 
LYS HZ2    H  N N 315 
LYS HZ3    H  N N 316 
LYS HXT    H  N N 317 
MET N      N  N N 318 
MET CA     C  N S 319 
MET C      C  N N 320 
MET O      O  N N 321 
MET CB     C  N N 322 
MET CG     C  N N 323 
MET SD     S  N N 324 
MET CE     C  N N 325 
MET OXT    O  N N 326 
MET H      H  N N 327 
MET H2     H  N N 328 
MET HA     H  N N 329 
MET HB2    H  N N 330 
MET HB3    H  N N 331 
MET HG2    H  N N 332 
MET HG3    H  N N 333 
MET HE1    H  N N 334 
MET HE2    H  N N 335 
MET HE3    H  N N 336 
MET HXT    H  N N 337 
P77 S      S  N N 338 
P77 CL     CL N N 339 
P77 C1     C  Y N 340 
P77 N1     N  N N 341 
P77 C2     C  Y N 342 
P77 N2     N  N N 343 
P77 C3     C  Y N 344 
P77 N3     N  N N 345 
P77 C4     C  Y N 346 
P77 C5     C  Y N 347 
P77 C6     C  Y N 348 
P77 C7     C  Y N 349 
P77 C8     C  Y N 350 
P77 C9     C  Y N 351 
P77 C10    C  Y N 352 
P77 C11    C  Y N 353 
P77 C12    C  Y N 354 
P77 C13    C  N N 355 
P77 C14    C  N N 356 
P77 C15    C  N N 357 
P77 C16    C  N N 358 
P77 C17    C  N N 359 
P77 C18    C  N N 360 
P77 C19    C  N N 361 
P77 C20    C  N N 362 
P77 H2     H  N N 363 
P77 H3     H  N N 364 
P77 H6     H  N N 365 
P77 H8     H  N N 366 
P77 H9     H  N N 367 
P77 H10    H  N N 368 
P77 H11    H  N N 369 
P77 H13    H  N N 370 
P77 H13A   H  N N 371 
P77 H14    H  N N 372 
P77 H14A   H  N N 373 
P77 H15    H  N N 374 
P77 H15A   H  N N 375 
P77 H16    H  N N 376 
P77 H16A   H  N N 377 
P77 H17    H  N N 378 
P77 H17A   H  N N 379 
P77 H18    H  N N 380 
P77 H18A   H  N N 381 
P77 H19    H  N N 382 
P77 H19A   H  N N 383 
P77 H20    H  N N 384 
P77 H20A   H  N N 385 
P77 H20B   H  N N 386 
PHE N      N  N N 387 
PHE CA     C  N S 388 
PHE C      C  N N 389 
PHE O      O  N N 390 
PHE CB     C  N N 391 
PHE CG     C  Y N 392 
PHE CD1    C  Y N 393 
PHE CD2    C  Y N 394 
PHE CE1    C  Y N 395 
PHE CE2    C  Y N 396 
PHE CZ     C  Y N 397 
PHE OXT    O  N N 398 
PHE H      H  N N 399 
PHE H2     H  N N 400 
PHE HA     H  N N 401 
PHE HB2    H  N N 402 
PHE HB3    H  N N 403 
PHE HD1    H  N N 404 
PHE HD2    H  N N 405 
PHE HE1    H  N N 406 
PHE HE2    H  N N 407 
PHE HZ     H  N N 408 
PHE HXT    H  N N 409 
PRO N      N  N N 410 
PRO CA     C  N S 411 
PRO C      C  N N 412 
PRO O      O  N N 413 
PRO CB     C  N N 414 
PRO CG     C  N N 415 
PRO CD     C  N N 416 
PRO OXT    O  N N 417 
PRO H      H  N N 418 
PRO HA     H  N N 419 
PRO HB2    H  N N 420 
PRO HB3    H  N N 421 
PRO HG2    H  N N 422 
PRO HG3    H  N N 423 
PRO HD2    H  N N 424 
PRO HD3    H  N N 425 
PRO HXT    H  N N 426 
SER N      N  N N 427 
SER CA     C  N S 428 
SER C      C  N N 429 
SER O      O  N N 430 
SER CB     C  N N 431 
SER OG     O  N N 432 
SER OXT    O  N N 433 
SER H      H  N N 434 
SER H2     H  N N 435 
SER HA     H  N N 436 
SER HB2    H  N N 437 
SER HB3    H  N N 438 
SER HG     H  N N 439 
SER HXT    H  N N 440 
SO4 S      S  N N 441 
SO4 O1     O  N N 442 
SO4 O2     O  N N 443 
SO4 O3     O  N N 444 
SO4 O4     O  N N 445 
THR N      N  N N 446 
THR CA     C  N S 447 
THR C      C  N N 448 
THR O      O  N N 449 
THR CB     C  N R 450 
THR OG1    O  N N 451 
THR CG2    C  N N 452 
THR OXT    O  N N 453 
THR H      H  N N 454 
THR H2     H  N N 455 
THR HA     H  N N 456 
THR HB     H  N N 457 
THR HG1    H  N N 458 
THR HG21   H  N N 459 
THR HG22   H  N N 460 
THR HG23   H  N N 461 
THR HXT    H  N N 462 
TRP N      N  N N 463 
TRP CA     C  N S 464 
TRP C      C  N N 465 
TRP O      O  N N 466 
TRP CB     C  N N 467 
TRP CG     C  Y N 468 
TRP CD1    C  Y N 469 
TRP CD2    C  Y N 470 
TRP NE1    N  Y N 471 
TRP CE2    C  Y N 472 
TRP CE3    C  Y N 473 
TRP CZ2    C  Y N 474 
TRP CZ3    C  Y N 475 
TRP CH2    C  Y N 476 
TRP OXT    O  N N 477 
TRP H      H  N N 478 
TRP H2     H  N N 479 
TRP HA     H  N N 480 
TRP HB2    H  N N 481 
TRP HB3    H  N N 482 
TRP HD1    H  N N 483 
TRP HE1    H  N N 484 
TRP HE3    H  N N 485 
TRP HZ2    H  N N 486 
TRP HZ3    H  N N 487 
TRP HH2    H  N N 488 
TRP HXT    H  N N 489 
TYR N      N  N N 490 
TYR CA     C  N S 491 
TYR C      C  N N 492 
TYR O      O  N N 493 
TYR CB     C  N N 494 
TYR CG     C  Y N 495 
TYR CD1    C  Y N 496 
TYR CD2    C  Y N 497 
TYR CE1    C  Y N 498 
TYR CE2    C  Y N 499 
TYR CZ     C  Y N 500 
TYR OH     O  N N 501 
TYR OXT    O  N N 502 
TYR H      H  N N 503 
TYR H2     H  N N 504 
TYR HA     H  N N 505 
TYR HB2    H  N N 506 
TYR HB3    H  N N 507 
TYR HD1    H  N N 508 
TYR HD2    H  N N 509 
TYR HE1    H  N N 510 
TYR HE2    H  N N 511 
TYR HH     H  N N 512 
TYR HXT    H  N N 513 
VAL N      N  N N 514 
VAL CA     C  N S 515 
VAL C      C  N N 516 
VAL O      O  N N 517 
VAL CB     C  N N 518 
VAL CG1    C  N N 519 
VAL CG2    C  N N 520 
VAL OXT    O  N N 521 
VAL H      H  N N 522 
VAL H2     H  N N 523 
VAL HA     H  N N 524 
VAL HB     H  N N 525 
VAL HG11   H  N N 526 
VAL HG12   H  N N 527 
VAL HG13   H  N N 528 
VAL HG21   H  N N 529 
VAL HG22   H  N N 530 
VAL HG23   H  N N 531 
VAL HXT    H  N N 532 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FDA PA    O1A    doub N N 83  
FDA PA    O2A    sing N N 84  
FDA PA    O5B    sing N N 85  
FDA PA    O3P    sing N N 86  
FDA O2A   HOA2   sing N N 87  
FDA O5B   C5B    sing N N 88  
FDA C5B   C4B    sing N N 89  
FDA C5B   H51A   sing N N 90  
FDA C5B   H52A   sing N N 91  
FDA C4B   O4B    sing N N 92  
FDA C4B   C3B    sing N N 93  
FDA C4B   H4B    sing N N 94  
FDA O4B   C1B    sing N N 95  
FDA C3B   O3B    sing N N 96  
FDA C3B   C2B    sing N N 97  
FDA C3B   H3B    sing N N 98  
FDA O3B   HO3A   sing N N 99  
FDA C2B   O2B    sing N N 100 
FDA C2B   C1B    sing N N 101 
FDA C2B   H2B    sing N N 102 
FDA O2B   HO2A   sing N N 103 
FDA C1B   N9A    sing N N 104 
FDA C1B   H1B    sing N N 105 
FDA N9A   C8A    sing Y N 106 
FDA N9A   C4A    sing Y N 107 
FDA C8A   N7A    doub Y N 108 
FDA C8A   H8A    sing N N 109 
FDA N7A   C5A    sing Y N 110 
FDA C5A   C6A    sing Y N 111 
FDA C5A   C4A    doub Y N 112 
FDA C6A   N6A    sing N N 113 
FDA C6A   N1A    doub Y N 114 
FDA N6A   H61A   sing N N 115 
FDA N6A   H62A   sing N N 116 
FDA N1A   C2A    sing Y N 117 
FDA C2A   N3A    doub Y N 118 
FDA C2A   H2A    sing N N 119 
FDA N3A   C4A    sing Y N 120 
FDA N1    C2     sing N N 121 
FDA N1    C10    sing N N 122 
FDA N1    HN1    sing N N 123 
FDA C2    O2     doub N N 124 
FDA C2    N3     sing N N 125 
FDA N3    C4     sing N N 126 
FDA N3    HN3    sing N N 127 
FDA C4    O4     doub N N 128 
FDA C4    C4X    sing N N 129 
FDA C4X   N5     sing N N 130 
FDA C4X   C10    doub N N 131 
FDA N5    C5X    sing N N 132 
FDA N5    HN5    sing N N 133 
FDA C5X   C6     doub Y N 134 
FDA C5X   C9A    sing Y N 135 
FDA C6    C7     sing Y N 136 
FDA C6    H6     sing N N 137 
FDA C7    C7M    sing N N 138 
FDA C7    C8     doub Y N 139 
FDA C7M   HM71   sing N N 140 
FDA C7M   HM72   sing N N 141 
FDA C7M   HM73   sing N N 142 
FDA C8    C8M    sing N N 143 
FDA C8    C9     sing Y N 144 
FDA C8M   HM81   sing N N 145 
FDA C8M   HM82   sing N N 146 
FDA C8M   HM83   sing N N 147 
FDA C9    C9A    doub Y N 148 
FDA C9    H9     sing N N 149 
FDA C9A   N10    sing N N 150 
FDA N10   C10    sing N N 151 
FDA N10   "C1'"  sing N N 152 
FDA "C1'" "C2'"  sing N N 153 
FDA "C1'" "H1'1" sing N N 154 
FDA "C1'" "H1'2" sing N N 155 
FDA "C2'" "O2'"  sing N N 156 
FDA "C2'" "C3'"  sing N N 157 
FDA "C2'" "H2'"  sing N N 158 
FDA "O2'" "HO2'" sing N N 159 
FDA "C3'" "O3'"  sing N N 160 
FDA "C3'" "C4'"  sing N N 161 
FDA "C3'" "H3'"  sing N N 162 
FDA "O3'" "HO3'" sing N N 163 
FDA "C4'" "O4'"  sing N N 164 
FDA "C4'" "C5'"  sing N N 165 
FDA "C4'" "H4'"  sing N N 166 
FDA "O4'" "HO4'" sing N N 167 
FDA "C5'" "O5'"  sing N N 168 
FDA "C5'" "H5'1" sing N N 169 
FDA "C5'" "H5'2" sing N N 170 
FDA "O5'" P      sing N N 171 
FDA P     O1P    doub N N 172 
FDA P     O2P    sing N N 173 
FDA P     O3P    sing N N 174 
FDA O2P   HOP2   sing N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
HOH O     H1     sing N N 243 
HOH O     H2     sing N N 244 
ILE N     CA     sing N N 245 
ILE N     H      sing N N 246 
ILE N     H2     sing N N 247 
ILE CA    C      sing N N 248 
ILE CA    CB     sing N N 249 
ILE CA    HA     sing N N 250 
ILE C     O      doub N N 251 
ILE C     OXT    sing N N 252 
ILE CB    CG1    sing N N 253 
ILE CB    CG2    sing N N 254 
ILE CB    HB     sing N N 255 
ILE CG1   CD1    sing N N 256 
ILE CG1   HG12   sing N N 257 
ILE CG1   HG13   sing N N 258 
ILE CG2   HG21   sing N N 259 
ILE CG2   HG22   sing N N 260 
ILE CG2   HG23   sing N N 261 
ILE CD1   HD11   sing N N 262 
ILE CD1   HD12   sing N N 263 
ILE CD1   HD13   sing N N 264 
ILE OXT   HXT    sing N N 265 
LEU N     CA     sing N N 266 
LEU N     H      sing N N 267 
LEU N     H2     sing N N 268 
LEU CA    C      sing N N 269 
LEU CA    CB     sing N N 270 
LEU CA    HA     sing N N 271 
LEU C     O      doub N N 272 
LEU C     OXT    sing N N 273 
LEU CB    CG     sing N N 274 
LEU CB    HB2    sing N N 275 
LEU CB    HB3    sing N N 276 
LEU CG    CD1    sing N N 277 
LEU CG    CD2    sing N N 278 
LEU CG    HG     sing N N 279 
LEU CD1   HD11   sing N N 280 
LEU CD1   HD12   sing N N 281 
LEU CD1   HD13   sing N N 282 
LEU CD2   HD21   sing N N 283 
LEU CD2   HD22   sing N N 284 
LEU CD2   HD23   sing N N 285 
LEU OXT   HXT    sing N N 286 
LYS N     CA     sing N N 287 
LYS N     H      sing N N 288 
LYS N     H2     sing N N 289 
LYS CA    C      sing N N 290 
LYS CA    CB     sing N N 291 
LYS CA    HA     sing N N 292 
LYS C     O      doub N N 293 
LYS C     OXT    sing N N 294 
LYS CB    CG     sing N N 295 
LYS CB    HB2    sing N N 296 
LYS CB    HB3    sing N N 297 
LYS CG    CD     sing N N 298 
LYS CG    HG2    sing N N 299 
LYS CG    HG3    sing N N 300 
LYS CD    CE     sing N N 301 
LYS CD    HD2    sing N N 302 
LYS CD    HD3    sing N N 303 
LYS CE    NZ     sing N N 304 
LYS CE    HE2    sing N N 305 
LYS CE    HE3    sing N N 306 
LYS NZ    HZ1    sing N N 307 
LYS NZ    HZ2    sing N N 308 
LYS NZ    HZ3    sing N N 309 
LYS OXT   HXT    sing N N 310 
MET N     CA     sing N N 311 
MET N     H      sing N N 312 
MET N     H2     sing N N 313 
MET CA    C      sing N N 314 
MET CA    CB     sing N N 315 
MET CA    HA     sing N N 316 
MET C     O      doub N N 317 
MET C     OXT    sing N N 318 
MET CB    CG     sing N N 319 
MET CB    HB2    sing N N 320 
MET CB    HB3    sing N N 321 
MET CG    SD     sing N N 322 
MET CG    HG2    sing N N 323 
MET CG    HG3    sing N N 324 
MET SD    CE     sing N N 325 
MET CE    HE1    sing N N 326 
MET CE    HE2    sing N N 327 
MET CE    HE3    sing N N 328 
MET OXT   HXT    sing N N 329 
P77 S     C4     sing N N 330 
P77 S     C7     sing N N 331 
P77 C1    CL     sing N N 332 
P77 C2    C1     doub Y N 333 
P77 C1    C6     sing Y N 334 
P77 C5    N1     sing N N 335 
P77 C12   N1     sing N N 336 
P77 N1    C13    sing N N 337 
P77 C3    C2     sing Y N 338 
P77 C2    H2     sing N N 339 
P77 N2    C19    sing N N 340 
P77 N2    C15    sing N N 341 
P77 N2    C16    sing N N 342 
P77 C3    C4     doub Y N 343 
P77 C3    H3     sing N N 344 
P77 C18   N3     sing N N 345 
P77 C17   N3     sing N N 346 
P77 N3    C20    sing N N 347 
P77 C4    C5     sing Y N 348 
P77 C5    C6     doub Y N 349 
P77 C6    H6     sing N N 350 
P77 C8    C7     doub Y N 351 
P77 C7    C12    sing Y N 352 
P77 C8    C9     sing Y N 353 
P77 C8    H8     sing N N 354 
P77 C9    C10    doub Y N 355 
P77 C9    H9     sing N N 356 
P77 C10   C11    sing Y N 357 
P77 C10   H10    sing N N 358 
P77 C12   C11    doub Y N 359 
P77 C11   H11    sing N N 360 
P77 C13   C14    sing N N 361 
P77 C13   H13    sing N N 362 
P77 C13   H13A   sing N N 363 
P77 C14   C15    sing N N 364 
P77 C14   H14    sing N N 365 
P77 C14   H14A   sing N N 366 
P77 C15   H15    sing N N 367 
P77 C15   H15A   sing N N 368 
P77 C16   C17    sing N N 369 
P77 C16   H16    sing N N 370 
P77 C16   H16A   sing N N 371 
P77 C17   H17    sing N N 372 
P77 C17   H17A   sing N N 373 
P77 C19   C18    sing N N 374 
P77 C18   H18    sing N N 375 
P77 C18   H18A   sing N N 376 
P77 C19   H19    sing N N 377 
P77 C19   H19A   sing N N 378 
P77 C20   H20    sing N N 379 
P77 C20   H20A   sing N N 380 
P77 C20   H20B   sing N N 381 
PHE N     CA     sing N N 382 
PHE N     H      sing N N 383 
PHE N     H2     sing N N 384 
PHE CA    C      sing N N 385 
PHE CA    CB     sing N N 386 
PHE CA    HA     sing N N 387 
PHE C     O      doub N N 388 
PHE C     OXT    sing N N 389 
PHE CB    CG     sing N N 390 
PHE CB    HB2    sing N N 391 
PHE CB    HB3    sing N N 392 
PHE CG    CD1    doub Y N 393 
PHE CG    CD2    sing Y N 394 
PHE CD1   CE1    sing Y N 395 
PHE CD1   HD1    sing N N 396 
PHE CD2   CE2    doub Y N 397 
PHE CD2   HD2    sing N N 398 
PHE CE1   CZ     doub Y N 399 
PHE CE1   HE1    sing N N 400 
PHE CE2   CZ     sing Y N 401 
PHE CE2   HE2    sing N N 402 
PHE CZ    HZ     sing N N 403 
PHE OXT   HXT    sing N N 404 
PRO N     CA     sing N N 405 
PRO N     CD     sing N N 406 
PRO N     H      sing N N 407 
PRO CA    C      sing N N 408 
PRO CA    CB     sing N N 409 
PRO CA    HA     sing N N 410 
PRO C     O      doub N N 411 
PRO C     OXT    sing N N 412 
PRO CB    CG     sing N N 413 
PRO CB    HB2    sing N N 414 
PRO CB    HB3    sing N N 415 
PRO CG    CD     sing N N 416 
PRO CG    HG2    sing N N 417 
PRO CG    HG3    sing N N 418 
PRO CD    HD2    sing N N 419 
PRO CD    HD3    sing N N 420 
PRO OXT   HXT    sing N N 421 
SER N     CA     sing N N 422 
SER N     H      sing N N 423 
SER N     H2     sing N N 424 
SER CA    C      sing N N 425 
SER CA    CB     sing N N 426 
SER CA    HA     sing N N 427 
SER C     O      doub N N 428 
SER C     OXT    sing N N 429 
SER CB    OG     sing N N 430 
SER CB    HB2    sing N N 431 
SER CB    HB3    sing N N 432 
SER OG    HG     sing N N 433 
SER OXT   HXT    sing N N 434 
SO4 S     O1     doub N N 435 
SO4 S     O2     doub N N 436 
SO4 S     O3     sing N N 437 
SO4 S     O4     sing N N 438 
THR N     CA     sing N N 439 
THR N     H      sing N N 440 
THR N     H2     sing N N 441 
THR CA    C      sing N N 442 
THR CA    CB     sing N N 443 
THR CA    HA     sing N N 444 
THR C     O      doub N N 445 
THR C     OXT    sing N N 446 
THR CB    OG1    sing N N 447 
THR CB    CG2    sing N N 448 
THR CB    HB     sing N N 449 
THR OG1   HG1    sing N N 450 
THR CG2   HG21   sing N N 451 
THR CG2   HG22   sing N N 452 
THR CG2   HG23   sing N N 453 
THR OXT   HXT    sing N N 454 
TRP N     CA     sing N N 455 
TRP N     H      sing N N 456 
TRP N     H2     sing N N 457 
TRP CA    C      sing N N 458 
TRP CA    CB     sing N N 459 
TRP CA    HA     sing N N 460 
TRP C     O      doub N N 461 
TRP C     OXT    sing N N 462 
TRP CB    CG     sing N N 463 
TRP CB    HB2    sing N N 464 
TRP CB    HB3    sing N N 465 
TRP CG    CD1    doub Y N 466 
TRP CG    CD2    sing Y N 467 
TRP CD1   NE1    sing Y N 468 
TRP CD1   HD1    sing N N 469 
TRP CD2   CE2    doub Y N 470 
TRP CD2   CE3    sing Y N 471 
TRP NE1   CE2    sing Y N 472 
TRP NE1   HE1    sing N N 473 
TRP CE2   CZ2    sing Y N 474 
TRP CE3   CZ3    doub Y N 475 
TRP CE3   HE3    sing N N 476 
TRP CZ2   CH2    doub Y N 477 
TRP CZ2   HZ2    sing N N 478 
TRP CZ3   CH2    sing Y N 479 
TRP CZ3   HZ3    sing N N 480 
TRP CH2   HH2    sing N N 481 
TRP OXT   HXT    sing N N 482 
TYR N     CA     sing N N 483 
TYR N     H      sing N N 484 
TYR N     H2     sing N N 485 
TYR CA    C      sing N N 486 
TYR CA    CB     sing N N 487 
TYR CA    HA     sing N N 488 
TYR C     O      doub N N 489 
TYR C     OXT    sing N N 490 
TYR CB    CG     sing N N 491 
TYR CB    HB2    sing N N 492 
TYR CB    HB3    sing N N 493 
TYR CG    CD1    doub Y N 494 
TYR CG    CD2    sing Y N 495 
TYR CD1   CE1    sing Y N 496 
TYR CD1   HD1    sing N N 497 
TYR CD2   CE2    doub Y N 498 
TYR CD2   HD2    sing N N 499 
TYR CE1   CZ     doub Y N 500 
TYR CE1   HE1    sing N N 501 
TYR CE2   CZ     sing Y N 502 
TYR CE2   HE2    sing N N 503 
TYR CZ    OH     sing N N 504 
TYR OH    HH     sing N N 505 
TYR OXT   HXT    sing N N 506 
VAL N     CA     sing N N 507 
VAL N     H      sing N N 508 
VAL N     H2     sing N N 509 
VAL CA    C      sing N N 510 
VAL CA    CB     sing N N 511 
VAL CA    HA     sing N N 512 
VAL C     O      doub N N 513 
VAL C     OXT    sing N N 514 
VAL CB    CG1    sing N N 515 
VAL CB    CG2    sing N N 516 
VAL CB    HB     sing N N 517 
VAL CG1   HG11   sing N N 518 
VAL CG1   HG12   sing N N 519 
VAL CG1   HG13   sing N N 520 
VAL CG2   HG21   sing N N 521 
VAL CG2   HG22   sing N N 522 
VAL CG2   HG23   sing N N 523 
VAL OXT   HXT    sing N N 524 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           'Ineos Oxford Institute Core Grant' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 65 2 2' 
_space_group.name_Hall        'P 65 2 (x,y,z+1/12)' 
_space_group.IT_number        179 
_space_group.crystal_system   hexagonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9HJV 
_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]   0.010247 
_atom_sites.fract_transf_matrix[1][2]   0.005916 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011832 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.005942 
_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.
;
? 
P  ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . ASN A 1 1   ? -23.94997 -21.42604 -15.13563 1.000 50.76528  ? 12  ASN A N     1 
ATOM   2    C  CA    . ASN A 1 1   ? -22.73621 -21.68251 -14.36382 1.000 53.73559  ? 12  ASN A CA    1 
ATOM   3    C  C     . ASN A 1 1   ? -21.63066 -20.66234 -14.65157 1.000 43.01611  ? 12  ASN A C     1 
ATOM   4    O  O     . ASN A 1 1   ? -21.61109 -20.03569 -15.70988 1.000 43.53498  ? 12  ASN A O     1 
ATOM   5    C  CB    . ASN A 1 1   ? -22.20101 -23.09108 -14.65004 1.000 56.39939  ? 12  ASN A CB    1 
ATOM   6    C  CG    . ASN A 1 1   ? -23.28324 -24.14522 -14.61535 1.000 66.84345  ? 12  ASN A CG    1 
ATOM   7    O  OD1   . ASN A 1 1   ? -23.86171 -24.42326 -13.56479 1.000 76.61516  ? 12  ASN A OD1   1 
ATOM   8    N  ND2   . ASN A 1 1   ? -23.55438 -24.75218 -15.76738 1.000 71.97577  ? 12  ASN A ND2   1 
ATOM   9    N  N     . LEU A 1 2   ? -20.70634 -20.52065 -13.69502 1.000 36.53853  ? 13  LEU A N     1 
ATOM   10   C  CA    . LEU A 1 2   ? -19.53557 -19.66536 -13.88856 1.000 37.09395  ? 13  LEU A CA    1 
ATOM   11   C  C     . LEU A 1 2   ? -18.66540 -20.14788 -15.04427 1.000 32.26437  ? 13  LEU A C     1 
ATOM   12   O  O     . LEU A 1 2   ? -18.08702 -19.33361 -15.77112 1.000 34.73888  ? 13  LEU A O     1 
ATOM   13   C  CB    . LEU A 1 2   ? -18.69523 -19.60684 -12.60561 1.000 24.42815  ? 13  LEU A CB    1 
ATOM   14   C  CG    . LEU A 1 2   ? -19.28124 -18.79649 -11.45454 1.000 32.70447  ? 13  LEU A CG    1 
ATOM   15   C  CD1   . LEU A 1 2   ? -18.28493 -18.70393 -10.30201 1.000 28.93407  ? 13  LEU A CD1   1 
ATOM   16   C  CD2   . LEU A 1 2   ? -19.69113 -17.41682 -11.95751 1.000 30.54094  ? 13  LEU A CD2   1 
ATOM   17   N  N     . LEU A 1 3   ? -18.52663 -21.46195 -15.20741 1.000 25.94953  ? 14  LEU A N     1 
ATOM   18   C  CA    . LEU A 1 3   ? -17.59569 -22.02551 -16.17914 1.000 30.26038  ? 14  LEU A CA    1 
ATOM   19   C  C     . LEU A 1 3   ? -18.26362 -22.64661 -17.40169 1.000 33.22304  ? 14  LEU A C     1 
ATOM   20   O  O     . LEU A 1 3   ? -17.56322 -23.20613 -18.25260 1.000 29.13337  ? 14  LEU A O     1 
ATOM   21   C  CB    . LEU A 1 3   ? -16.69718 -23.06522 -15.49293 1.000 22.21659  ? 14  LEU A CB    1 
ATOM   22   C  CG    . LEU A 1 3   ? -15.69370 -22.37843 -14.56737 1.000 27.13999  ? 14  LEU A CG    1 
ATOM   23   C  CD1   . LEU A 1 3   ? -15.10033 -23.33288 -13.54731 1.000 24.91229  ? 14  LEU A CD1   1 
ATOM   24   C  CD2   . LEU A 1 3   ? -14.60275 -21.72094 -15.40313 1.000 26.46504  ? 14  LEU A CD2   1 
ATOM   25   N  N     . SER A 1 4   ? -19.58439 -22.56506 -17.53288 1.000 35.34963  ? 15  SER A N     1 
ATOM   26   C  CA    . SER A 1 4   ? -20.20700 -23.11809 -18.72852 1.000 36.15692  ? 15  SER A CA    1 
ATOM   27   C  C     . SER A 1 4   ? -19.67150 -22.40211 -19.96889 1.000 34.57267  ? 15  SER A C     1 
ATOM   28   O  O     . SER A 1 4   ? -19.49518 -21.17765 -19.97612 1.000 30.43465  ? 15  SER A O     1 
ATOM   29   C  CB    . SER A 1 4   ? -21.72952 -23.00231 -18.64497 1.000 36.58418  ? 15  SER A CB    1 
ATOM   30   O  OG    . SER A 1 4   ? -22.12909 -21.69566 -18.96872 1.000 31.58437  ? 15  SER A OG    1 
ATOM   31   N  N     . ASP A 1 5   ? -19.36578 -23.18437 -21.00685 1.000 32.31215  ? 16  ASP A N     1 
ATOM   32   C  CA    . ASP A 1 5   ? -18.72514 -22.69554 -22.23245 1.000 38.76411  ? 16  ASP A CA    1 
ATOM   33   C  C     . ASP A 1 5   ? -17.34789 -22.07544 -21.98222 1.000 31.87953  ? 16  ASP A C     1 
ATOM   34   O  O     . ASP A 1 5   ? -16.85495 -21.30269 -22.81403 1.000 30.46244  ? 16  ASP A O     1 
ATOM   35   C  CB    . ASP A 1 5   ? -19.62242 -21.69049 -22.96943 1.000 37.23994  ? 16  ASP A CB    1 
ATOM   36   C  CG    . ASP A 1 5   ? -20.95069 -22.29178 -23.37650 1.000 43.79048  ? 16  ASP A CG    1 
ATOM   37   O  OD1   . ASP A 1 5   ? -20.97871 -23.49202 -23.74091 1.000 47.48677  ? 16  ASP A OD1   1 
ATOM   38   O  OD2   . ASP A 1 5   ? -21.96695 -21.56708 -23.32351 1.000 48.91129  ? 16  ASP A OD2   1 
ATOM   39   N  N     . LYS A 1 6   ? -16.71220 -22.39067 -20.85137 1.000 29.92008  ? 17  LYS A N     1 
ATOM   40   C  CA    . LYS A 1 6   ? -15.37002 -21.91265 -20.54630 1.000 26.17465  ? 17  LYS A CA    1 
ATOM   41   C  C     . LYS A 1 6   ? -14.50404 -23.09993 -20.15986 1.000 27.24880  ? 17  LYS A C     1 
ATOM   42   O  O     . LYS A 1 6   ? -15.00693 -24.16365 -19.79300 1.000 26.92868  ? 17  LYS A O     1 
ATOM   43   C  CB    . LYS A 1 6   ? -15.38720 -20.85995 -19.42418 1.000 24.91532  ? 17  LYS A CB    1 
ATOM   44   C  CG    . LYS A 1 6   ? -16.12495 -19.59129 -19.84083 1.000 30.01061  ? 17  LYS A CG    1 
ATOM   45   C  CD    . LYS A 1 6   ? -16.16891 -18.50081 -18.76377 1.000 33.26151  ? 17  LYS A CD    1 
ATOM   46   C  CE    . LYS A 1 6   ? -16.91327 -17.27682 -19.32322 1.000 27.55556  ? 17  LYS A CE    1 
ATOM   47   N  NZ    . LYS A 1 6   ? -16.92622 -16.10333 -18.41402 1.000 33.97029  ? 17  LYS A NZ    1 
ATOM   48   N  N     . ASN A 1 7   ? -13.19074 -22.93031 -20.25338 1.000 22.52866  ? 18  ASN A N     1 
ATOM   49   C  CA    . ASN A 1 7   ? -12.29241 -24.01281 -19.88206 1.000 24.86684  ? 18  ASN A CA    1 
ATOM   50   C  C     . ASN A 1 7   ? -11.25095 -23.51161 -18.89225 1.000 20.82238  ? 18  ASN A C     1 
ATOM   51   O  O     . ASN A 1 7   ? -10.96228 -22.31736 -18.80235 1.000 22.02018  ? 18  ASN A O     1 
ATOM   52   C  CB    . ASN A 1 7   ? -11.63293 -24.65611 -21.11574 1.000 26.56365  ? 18  ASN A CB    1 
ATOM   53   C  CG    . ASN A 1 7   ? -10.71093 -23.70481 -21.86778 1.000 28.83338  ? 18  ASN A CG    1 
ATOM   54   O  OD1   . ASN A 1 7   ? -11.15621 -22.72463 -22.44674 1.000 33.92862  ? 18  ASN A OD1   1 
ATOM   55   N  ND2   . ASN A 1 7   ? -9.42702  -24.02336 -21.89822 1.000 27.13087  ? 18  ASN A ND2   1 
ATOM   56   N  N     . VAL A 1 8   ? -10.72030 -24.44938 -18.11698 1.000 17.12944  ? 19  VAL A N     1 
ATOM   57   C  CA    . VAL A 1 8   ? -9.78079  -24.16792 -17.04324 1.000 17.43742  ? 19  VAL A CA    1 
ATOM   58   C  C     . VAL A 1 8   ? -8.45172  -24.81193 -17.40630 1.000 17.23790  ? 19  VAL A C     1 
ATOM   59   O  O     . VAL A 1 8   ? -8.41648  -25.93927 -17.90628 1.000 18.80357  ? 19  VAL A O     1 
ATOM   60   C  CB    . VAL A 1 8   ? -10.30267 -24.69746 -15.68981 1.000 20.81480  ? 19  VAL A CB    1 
ATOM   61   C  CG1   . VAL A 1 8   ? -9.30850  -24.39416 -14.54429 1.000 14.11919  ? 19  VAL A CG1   1 
ATOM   62   C  CG2   . VAL A 1 8   ? -11.66535 -24.10418 -15.37207 1.000 17.68654  ? 19  VAL A CG2   1 
ATOM   63   N  N     . ALA A 1 9   ? -7.35992  -24.09691 -17.16980 1.000 16.72712  ? 20  ALA A N     1 
ATOM   64   C  CA    . ALA A 1 9   ? -6.02476  -24.66755 -17.30029 1.000 16.64946  ? 20  ALA A CA    1 
ATOM   65   C  C     . ALA A 1 9   ? -5.37149  -24.70451 -15.92400 1.000 17.60418  ? 20  ALA A C     1 
ATOM   66   O  O     . ALA A 1 9   ? -5.22119  -23.66449 -15.26771 1.000 20.52398  ? 20  ALA A O     1 
ATOM   67   C  CB    . ALA A 1 9   ? -5.17122  -23.87161 -18.28990 1.000 15.35567  ? 20  ALA A CB    1 
ATOM   68   N  N     . ILE A 1 10  ? -5.00752  -25.89837 -15.48098 1.000 17.20960  ? 21  ILE A N     1 
ATOM   69   C  CA    . ILE A 1 10  ? -4.23553  -26.08464 -14.25441 1.000 17.99104  ? 21  ILE A CA    1 
ATOM   70   C  C     . ILE A 1 10  ? -2.77674  -26.28614 -14.63675 1.000 17.86644  ? 21  ILE A C     1 
ATOM   71   O  O     . ILE A 1 10  ? -2.45275  -27.18745 -15.42444 1.000 15.71372  ? 21  ILE A O     1 
ATOM   72   C  CB    . ILE A 1 10  ? -4.75367  -27.28367 -13.43925 1.000 18.35475  ? 21  ILE A CB    1 
ATOM   73   C  CG1   . ILE A 1 10  ? -6.20409  -27.04193 -12.99326 1.000 17.06336  ? 21  ILE A CG1   1 
ATOM   74   C  CG2   . ILE A 1 10  ? -3.82652  -27.56394 -12.21953 1.000 12.37608  ? 21  ILE A CG2   1 
ATOM   75   C  CD1   . ILE A 1 10  ? -6.81535  -28.25994 -12.36691 1.000 14.72053  ? 21  ILE A CD1   1 
ATOM   76   N  N     . ILE A 1 11  ? -1.89281  -25.46879 -14.06671 1.000 17.00329  ? 22  ILE A N     1 
ATOM   77   C  CA    . ILE A 1 11  ? -0.47019  -25.54069 -14.36327 1.000 14.97413  ? 22  ILE A CA    1 
ATOM   78   C  C     . ILE A 1 11  ? 0.18499   -26.41979 -13.30855 1.000 20.59503  ? 22  ILE A C     1 
ATOM   79   O  O     . ILE A 1 11  ? 0.34747   -26.00897 -12.15541 1.000 17.01594  ? 22  ILE A O     1 
ATOM   80   C  CB    . ILE A 1 11  ? 0.17345   -24.15366 -14.40824 1.000 16.76217  ? 22  ILE A CB    1 
ATOM   81   C  CG1   . ILE A 1 11  ? -0.66957  -23.21264 -15.28588 1.000 15.77792  ? 22  ILE A CG1   1 
ATOM   82   C  CG2   . ILE A 1 11  ? 1.61032   -24.27710 -14.95565 1.000 16.00372  ? 22  ILE A CG2   1 
ATOM   83   C  CD1   . ILE A 1 11  ? -0.99853  -23.75388 -16.68844 1.000 14.22062  ? 22  ILE A CD1   1 
ATOM   84   N  N     . GLY A 1 12  ? 0.57438   -27.62651 -13.70171 1.000 16.79735  ? 23  GLY A N     1 
ATOM   85   C  CA    . GLY A 1 12  ? 1.25756   -28.51838 -12.78146 1.000 17.15195  ? 23  GLY A CA    1 
ATOM   86   C  C     . GLY A 1 12  ? 0.39126   -29.69008 -12.37329 1.000 15.47194  ? 23  GLY A C     1 
ATOM   87   O  O     . GLY A 1 12  ? -0.71756  -29.51130 -11.86610 1.000 15.44330  ? 23  GLY A O     1 
ATOM   88   N  N     . GLY A 1 13  ? 0.88694   -30.89851 -12.60235 1.000 19.72319  ? 24  GLY A N     1 
ATOM   89   C  CA    . GLY A 1 13  ? 0.19011   -32.09606 -12.18654 1.000 20.59479  ? 24  GLY A CA    1 
ATOM   90   C  C     . GLY A 1 13  ? 0.78188   -32.74346 -10.94799 1.000 19.83465  ? 24  GLY A C     1 
ATOM   91   O  O     . GLY A 1 13  ? 1.05251   -33.95067 -10.94086 1.000 17.51029  ? 24  GLY A O     1 
ATOM   92   N  N     . GLY A 1 14  ? 1.00882   -31.95912 -9.89790  1.000 17.33582  ? 25  GLY A N     1 
ATOM   93   C  CA    . GLY A 1 14  ? 1.35376   -32.51996 -8.60877  1.000 17.96784  ? 25  GLY A CA    1 
ATOM   94   C  C     . GLY A 1 14  ? 0.10545   -33.06369 -7.93649  1.000 18.14714  ? 25  GLY A C     1 
ATOM   95   O  O     . GLY A 1 14  ? -0.97877  -33.10474 -8.53600  1.000 19.16110  ? 25  GLY A O     1 
ATOM   96   N  N     . PRO A 1 15  ? 0.21957   -33.50316 -6.68670  1.000 19.77274  ? 26  PRO A N     1 
ATOM   97   C  CA    . PRO A 1 15  ? -0.98711  -34.00033 -6.00382  1.000 13.82561  ? 26  PRO A CA    1 
ATOM   98   C  C     . PRO A 1 15  ? -2.04910  -32.92378 -5.85910  1.000 21.21927  ? 26  PRO A C     1 
ATOM   99   O  O     . PRO A 1 15  ? -3.24936  -33.23469 -5.90501  1.000 17.95323  ? 26  PRO A O     1 
ATOM   100  C  CB    . PRO A 1 15  ? -0.45765  -34.48013 -4.63829  1.000 17.19529  ? 26  PRO A CB    1 
ATOM   101  C  CG    . PRO A 1 15  ? 0.84855   -33.73038 -4.43040  1.000 15.42729  ? 26  PRO A CG    1 
ATOM   102  C  CD    . PRO A 1 15  ? 1.42363   -33.56429 -5.83602  1.000 16.09946  ? 26  PRO A CD    1 
ATOM   103  N  N     . VAL A 1 16  ? -1.64521  -31.65873 -5.71357  1.000 15.61496  ? 27  VAL A N     1 
ATOM   104  C  CA    . VAL A 1 16  ? -2.62714  -30.58728 -5.55164  1.000 16.83203  ? 27  VAL A CA    1 
ATOM   105  C  C     . VAL A 1 16  ? -3.30620  -30.26794 -6.88455  1.000 19.55281  ? 27  VAL A C     1 
ATOM   106  O  O     . VAL A 1 16  ? -4.53641  -30.15161 -6.95629  1.000 17.21052  ? 27  VAL A O     1 
ATOM   107  C  CB    . VAL A 1 16  ? -1.96912  -29.34108 -4.93373  1.000 14.53516  ? 27  VAL A CB    1 
ATOM   108  C  CG1   . VAL A 1 16  ? -2.97871  -28.18807 -4.88072  1.000 18.08968  ? 27  VAL A CG1   1 
ATOM   109  C  CG2   . VAL A 1 16  ? -1.45046  -29.64789 -3.51791  1.000 16.98273  ? 27  VAL A CG2   1 
ATOM   110  N  N     . GLY A 1 17  ? -2.52116  -30.12834 -7.96045  1.000 16.53869  ? 28  GLY A N     1 
ATOM   111  C  CA    . GLY A 1 17  ? -3.11052  -29.83865 -9.26537  1.000 16.52050  ? 28  GLY A CA    1 
ATOM   112  C  C     . GLY A 1 17  ? -3.98701  -30.96496 -9.79279  1.000 18.88438  ? 28  GLY A C     1 
ATOM   113  O  O     . GLY A 1 17  ? -5.04876  -30.71964 -10.37994 1.000 18.57933  ? 28  GLY A O     1 
ATOM   114  N  N     . LEU A 1 18  ? -3.56977  -32.21869 -9.57196  1.000 16.42664  ? 29  LEU A N     1 
ATOM   115  C  CA    . LEU A 1 18  ? -4.36788  -33.34950 -10.03805 1.000 17.06368  ? 29  LEU A CA    1 
ATOM   116  C  C     . LEU A 1 18  ? -5.67216  -33.44870 -9.26268  1.000 17.15207  ? 29  LEU A C     1 
ATOM   117  O  O     . LEU A 1 18  ? -6.72143  -33.75906 -9.83490  1.000 15.41272  ? 29  LEU A O     1 
ATOM   118  C  CB    . LEU A 1 18  ? -3.57282  -34.65405 -9.93301  1.000 20.03088  ? 29  LEU A CB    1 
ATOM   119  C  CG    . LEU A 1 18  ? -2.34713  -34.82947 -10.84764 1.000 22.61597  ? 29  LEU A CG    1 
ATOM   120  C  CD1   . LEU A 1 18  ? -1.71689  -36.22824 -10.66416 1.000 15.05805  ? 29  LEU A CD1   1 
ATOM   121  C  CD2   . LEU A 1 18  ? -2.71117  -34.58064 -12.32326 1.000 16.09736  ? 29  LEU A CD2   1 
ATOM   122  N  N     . THR A 1 19  ? -5.63736  -33.14267 -7.96555  1.000 19.16565  ? 30  THR A N     1 
ATOM   123  C  CA    . THR A 1 19  ? -6.87020  -33.15388 -7.19411  1.000 18.08986  ? 30  THR A CA    1 
ATOM   124  C  C     . THR A 1 19  ? -7.79986  -32.03309 -7.63746  1.000 20.33751  ? 30  THR A C     1 
ATOM   125  O  O     . THR A 1 19  ? -9.00556  -32.25522 -7.81953  1.000 21.54985  ? 30  THR A O     1 
ATOM   126  C  CB    . THR A 1 19  ? -6.54984  -33.05316 -5.71321  1.000 20.24939  ? 30  THR A CB    1 
ATOM   127  O  OG1   . THR A 1 19  ? -5.84415  -34.23871 -5.31358  1.000 20.08238  ? 30  THR A OG1   1 
ATOM   128  C  CG2   . THR A 1 19  ? -7.83911  -32.88750 -4.89719  1.000 17.81586  ? 30  THR A CG2   1 
ATOM   129  N  N     . MET A 1 20  ? -7.24620  -30.83353 -7.84877  1.000 20.95979  ? 31  MET A N     1 
ATOM   130  C  CA    . MET A 1 20  ? -8.02185  -29.71871 -8.38341  1.000 21.52022  ? 31  MET A CA    1 
ATOM   131  C  C     . MET A 1 20  ? -8.73214  -30.12160 -9.66482  1.000 17.41056  ? 31  MET A C     1 
ATOM   132  O  O     . MET A 1 20  ? -9.92435  -29.84810 -9.84007  1.000 21.09555  ? 31  MET A O     1 
ATOM   133  C  CB    . MET A 1 20  ? -7.10158  -28.51745 -8.63922  1.000 18.03145  ? 31  MET A CB    1 
ATOM   134  C  CG    . MET A 1 20  ? -7.84209  -27.23482 -9.03776  1.000 14.35870  ? 31  MET A CG    1 
ATOM   135  S  SD    . MET A 1 20  ? -8.67737  -26.45266 -7.64276  1.000 19.40251  ? 31  MET A SD    1 
ATOM   136  C  CE    . MET A 1 20  ? -10.24574 -25.94842 -8.34201  1.000 18.92423  ? 31  MET A CE    1 
ATOM   137  N  N     . ALA A 1 21  ? -8.00402  -30.78130 -10.57001 1.000 19.45244  ? 32  ALA A N     1 
ATOM   138  C  CA    . ALA A 1 21  ? -8.58874  -31.23802 -11.82880 1.000 17.45371  ? 32  ALA A CA    1 
ATOM   139  C  C     . ALA A 1 21  ? -9.74314  -32.19503 -11.59358 1.000 20.74951  ? 32  ALA A C     1 
ATOM   140  O  O     . ALA A 1 21  ? -10.77967 -32.10547 -12.25940 1.000 19.26632  ? 32  ALA A O     1 
ATOM   141  C  CB    . ALA A 1 21  ? -7.51997  -31.92603 -12.68936 1.000 13.43095  ? 32  ALA A CB    1 
ATOM   142  N  N     . LYS A 1 22  ? -9.56937  -33.14665 -10.67583 1.000 19.91661  ? 33  LYS A N     1 
ATOM   143  C  CA    . LYS A 1 22  ? -10.61246 -34.13610 -10.47494 1.000 16.49665  ? 33  LYS A CA    1 
ATOM   144  C  C     . LYS A 1 22  ? -11.87367 -33.48954 -9.91790  1.000 18.78802  ? 33  LYS A C     1 
ATOM   145  O  O     . LYS A 1 22  ? -12.98481 -33.79074 -10.36619 1.000 20.70826  ? 33  LYS A O     1 
ATOM   146  C  CB    . LYS A 1 22  ? -10.09263 -35.23726 -9.54956  1.000 19.70246  ? 33  LYS A CB    1 
ATOM   147  C  CG    . LYS A 1 22  ? -11.14921 -36.20385 -9.04132  1.000 18.28915  ? 33  LYS A CG    1 
ATOM   148  C  CD    . LYS A 1 22  ? -11.70279 -37.07353 -10.15392 1.000 26.21100  ? 33  LYS A CD    1 
ATOM   149  C  CE    . LYS A 1 22  ? -12.83448 -37.96096 -9.61674  1.000 25.80587  ? 33  LYS A CE    1 
ATOM   150  N  NZ    . LYS A 1 22  ? -13.55945 -38.57379 -10.72011 1.000 35.18814  ? 33  LYS A NZ    1 
ATOM   151  N  N     . LEU A 1 23  ? -11.71985 -32.58813 -8.94933  1.000 20.94674  ? 34  LEU A N     1 
ATOM   152  C  CA    . LEU A 1 23  ? -12.88715 -31.96458 -8.34141  1.000 20.58827  ? 34  LEU A CA    1 
ATOM   153  C  C     . LEU A 1 23  ? -13.62819 -31.07108 -9.32282  1.000 21.64672  ? 34  LEU A C     1 
ATOM   154  O  O     . LEU A 1 23  ? -14.85240 -30.96759 -9.24163  1.000 21.53991  ? 34  LEU A O     1 
ATOM   155  C  CB    . LEU A 1 23  ? -12.46990 -31.17426 -7.10600  1.000 18.49623  ? 34  LEU A CB    1 
ATOM   156  C  CG    . LEU A 1 23  ? -11.87294 -32.04025 -5.99559  1.000 22.61120  ? 34  LEU A CG    1 
ATOM   157  C  CD1   . LEU A 1 23  ? -11.37639 -31.17078 -4.85190  1.000 20.14232  ? 34  LEU A CD1   1 
ATOM   158  C  CD2   . LEU A 1 23  ? -12.89604 -33.06960 -5.49214  1.000 22.85110  ? 34  LEU A CD2   1 
ATOM   159  N  N     . LEU A 1 24  ? -12.91559 -30.42273 -10.25444 1.000 20.33438  ? 35  LEU A N     1 
ATOM   160  C  CA    . LEU A 1 24  ? -13.60315 -29.64021 -11.27920 1.000 21.34426  ? 35  LEU A CA    1 
ATOM   161  C  C     . LEU A 1 24  ? -14.23623 -30.55615 -12.31232 1.000 23.97302  ? 35  LEU A C     1 
ATOM   162  O  O     . LEU A 1 24  ? -15.39161 -30.36176 -12.70995 1.000 21.86365  ? 35  LEU A O     1 
ATOM   163  C  CB    . LEU A 1 24  ? -12.63034 -28.67864 -11.97037 1.000 15.25829  ? 35  LEU A CB    1 
ATOM   164  C  CG    . LEU A 1 24  ? -12.02846 -27.51252 -11.20032 1.000 23.71265  ? 35  LEU A CG    1 
ATOM   165  C  CD1   . LEU A 1 24  ? -11.08152 -26.72164 -12.10273 1.000 16.07561  ? 35  LEU A CD1   1 
ATOM   166  C  CD2   . LEU A 1 24  ? -13.12850 -26.60574 -10.65844 1.000 19.19339  ? 35  LEU A CD2   1 
ATOM   167  N  N     . GLN A 1 25  ? -13.47993 -31.56494 -12.76096 1.000 20.64823  ? 36  GLN A N     1 
ATOM   168  C  CA    . GLN A 1 25  ? -13.94524 -32.40221 -13.85539 1.000 23.34635  ? 36  GLN A CA    1 
ATOM   169  C  C     . GLN A 1 25  ? -15.21758 -33.13545 -13.48321 1.000 26.99697  ? 36  GLN A C     1 
ATOM   170  O  O     . GLN A 1 25  ? -16.09689 -33.32053 -14.32827 1.000 25.34850  ? 36  GLN A O     1 
ATOM   171  C  CB    . GLN A 1 25  ? -12.87176 -33.41291 -14.25642 1.000 21.50927  ? 36  GLN A CB    1 
ATOM   172  C  CG    . GLN A 1 25  ? -13.20165 -34.15598 -15.55777 1.000 21.62717  ? 36  GLN A CG    1 
ATOM   173  C  CD    . GLN A 1 25  ? -11.98928 -34.84857 -16.11032 1.000 24.59143  ? 36  GLN A CD    1 
ATOM   174  O  OE1   . GLN A 1 25  ? -11.58791 -35.88597 -15.60254 1.000 25.29298  ? 36  GLN A OE1   1 
ATOM   175  N  NE2   . GLN A 1 25  ? -11.36297 -34.25408 -17.13231 1.000 23.43367  ? 36  GLN A NE2   1 
ATOM   176  N  N     . GLN A 1 26  ? -15.32407 -33.58202 -12.22731 1.000 23.73266  ? 37  GLN A N     1 
ATOM   177  C  CA    . GLN A 1 26  ? -16.48919 -34.35428 -11.83674 1.000 30.67197  ? 37  GLN A CA    1 
ATOM   178  C  C     . GLN A 1 26  ? -17.74192 -33.49854 -11.73554 1.000 27.70048  ? 37  GLN A C     1 
ATOM   179  O  O     . GLN A 1 26  ? -18.83234 -34.05936 -11.63142 1.000 28.31053  ? 37  GLN A O     1 
ATOM   180  C  CB    . GLN A 1 26  ? -16.23401 -35.07808 -10.51088 1.000 28.82102  ? 37  GLN A CB    1 
ATOM   181  C  CG    . GLN A 1 26  ? -16.33311 -34.19566 -9.28484  1.000 28.31480  ? 37  GLN A CG    1 
ATOM   182  C  CD    . GLN A 1 26  ? -15.94764 -34.94398 -8.02546  1.000 27.48145  ? 37  GLN A CD    1 
ATOM   183  O  OE1   . GLN A 1 26  ? -15.36435 -36.02243 -8.09328  1.000 32.23276  ? 37  GLN A OE1   1 
ATOM   184  N  NE2   . GLN A 1 26  ? -16.29370 -34.39165 -6.87039  1.000 30.94243  ? 37  GLN A NE2   1 
ATOM   185  N  N     . ASN A 1 27  ? -17.61618 -32.16850 -11.76921 1.000 26.74863  ? 38  ASN A N     1 
ATOM   186  C  CA    . ASN A 1 27  ? -18.76201 -31.27453 -11.89622 1.000 23.61860  ? 38  ASN A CA    1 
ATOM   187  C  C     . ASN A 1 27  ? -18.96936 -30.79954 -13.32934 1.000 31.02616  ? 38  ASN A C     1 
ATOM   188  O  O     . ASN A 1 27  ? -19.59239 -29.75607 -13.53446 1.000 28.43011  ? 38  ASN A O     1 
ATOM   189  C  CB    . ASN A 1 27  ? -18.61945 -30.05987 -10.97734 1.000 23.10555  ? 38  ASN A CB    1 
ATOM   190  C  CG    . ASN A 1 27  ? -18.69348 -30.42721 -9.50369  1.000 31.04418  ? 38  ASN A CG    1 
ATOM   191  O  OD1   . ASN A 1 27  ? -17.77462 -30.16642 -8.73333  1.000 41.36304  ? 38  ASN A OD1   1 
ATOM   192  N  ND2   . ASN A 1 27  ? -19.77842 -31.04554 -9.11552  1.000 34.54627  ? 38  ASN A ND2   1 
ATOM   193  N  N     . GLY A 1 28  ? -18.43146 -31.51677 -14.32205 1.000 23.74519  ? 39  GLY A N     1 
ATOM   194  C  CA    . GLY A 1 28  ? -18.71782 -31.17725 -15.70277 1.000 27.28090  ? 39  GLY A CA    1 
ATOM   195  C  C     . GLY A 1 28  ? -17.89291 -30.04369 -16.27056 1.000 29.11335  ? 39  GLY A C     1 
ATOM   196  O  O     . GLY A 1 28  ? -18.28164 -29.45369 -17.27958 1.000 34.33387  ? 39  GLY A O     1 
ATOM   197  N  N     . ILE A 1 29  ? -16.75427 -29.73048 -15.67824 1.000 27.13540  ? 40  ILE A N     1 
ATOM   198  C  CA    . ILE A 1 29  ? -15.96460 -28.58439 -16.11208 1.000 23.78127  ? 40  ILE A CA    1 
ATOM   199  C  C     . ILE A 1 29  ? -14.90006 -29.05485 -17.08432 1.000 24.21298  ? 40  ILE A C     1 
ATOM   200  O  O     . ILE A 1 29  ? -14.24461 -30.07541 -16.85942 1.000 24.59220  ? 40  ILE A O     1 
ATOM   201  C  CB    . ILE A 1 29  ? -15.35197 -27.85706 -14.90797 1.000 20.37474  ? 40  ILE A CB    1 
ATOM   202  C  CG1   . ILE A 1 29  ? -16.47728 -27.15340 -14.16647 1.000 27.70862  ? 40  ILE A CG1   1 
ATOM   203  C  CG2   . ILE A 1 29  ? -14.33652 -26.81025 -15.33970 1.000 17.07601  ? 40  ILE A CG2   1 
ATOM   204  C  CD1   . ILE A 1 29  ? -16.02822 -26.61755 -12.90386 1.000 30.46960  ? 40  ILE A CD1   1 
ATOM   205  N  N     . ASP A 1 30  ? -14.76214 -28.32477 -18.18324 1.000 21.25895  ? 41  ASP A N     1 
ATOM   206  C  CA    . ASP A 1 30  ? -13.70360 -28.52699 -19.15883 1.000 23.48009  ? 41  ASP A CA    1 
ATOM   207  C  C     . ASP A 1 30  ? -12.37558 -28.05422 -18.56121 1.000 24.10653  ? 41  ASP A C     1 
ATOM   208  O  O     . ASP A 1 30  ? -12.14276 -26.84780 -18.42686 1.000 19.93101  ? 41  ASP A O     1 
ATOM   209  C  CB    . ASP A 1 30  ? -14.07704 -27.75342 -20.41872 1.000 19.75326  ? 41  ASP A CB    1 
ATOM   210  C  CG    . ASP A 1 30  ? -13.08712 -27.95298 -21.56675 1.000 30.59402  ? 41  ASP A CG    1 
ATOM   211  O  OD1   . ASP A 1 30  ? -12.08890 -28.69096 -21.42397 1.000 22.15181  ? 41  ASP A OD1   1 
ATOM   212  O  OD2   . ASP A 1 30  ? -13.32185 -27.34542 -22.62869 1.000 33.00967  ? 41  ASP A OD2   1 
ATOM   213  N  N     . VAL A 1 31  ? -11.51085 -28.99449 -18.17431 1.000 22.23245  ? 42  VAL A N     1 
ATOM   214  C  CA    . VAL A 1 31  ? -10.26659 -28.67147 -17.47436 1.000 20.23543  ? 42  VAL A CA    1 
ATOM   215  C  C     . VAL A 1 31  ? -9.13673  -29.51002 -18.05517 1.000 23.58955  ? 42  VAL A C     1 
ATOM   216  O  O     . VAL A 1 31  ? -9.31727  -30.69853 -18.35043 1.000 24.78168  ? 42  VAL A O     1 
ATOM   217  C  CB    . VAL A 1 31  ? -10.38773 -28.89610 -15.94087 1.000 25.00975  ? 42  VAL A CB    1 
ATOM   218  C  CG1   . VAL A 1 31  ? -10.85629 -30.32694 -15.61348 1.000 19.46254  ? 42  VAL A CG1   1 
ATOM   219  C  CG2   . VAL A 1 31  ? -9.06037  -28.59208 -15.23569 1.000 15.80660  ? 42  VAL A CG2   1 
ATOM   220  N  N     . SER A 1 32  ? -7.97253  -28.88286 -18.23823 1.000 19.40457  ? 43  SER A N     1 
ATOM   221  C  CA    . SER A 1 32  ? -6.75066  -29.57120 -18.63466 1.000 19.70093  ? 43  SER A CA    1 
ATOM   222  C  C     . SER A 1 32  ? -5.65963  -29.27573 -17.61546 1.000 22.84058  ? 43  SER A C     1 
ATOM   223  O  O     . SER A 1 32  ? -5.63013  -28.19313 -17.01226 1.000 17.86521  ? 43  SER A O     1 
ATOM   224  C  CB    . SER A 1 32  ? -6.25524  -29.13074 -20.02231 1.000 21.85876  ? 43  SER A CB    1 
ATOM   225  O  OG    . SER A 1 32  ? -7.09338  -29.58772 -21.06296 1.000 28.96998  ? 43  SER A OG    1 
ATOM   226  N  N     . VAL A 1 33  ? -4.75569  -30.23658 -17.43554 1.000 18.11671  ? 44  VAL A N     1 
ATOM   227  C  CA    . VAL A 1 33  ? -3.58294  -30.06803 -16.57983 1.000 14.72216  ? 44  VAL A CA    1 
ATOM   228  C  C     . VAL A 1 33  ? -2.35450  -30.12108 -17.46741 1.000 19.67202  ? 44  VAL A C     1 
ATOM   229  O  O     . VAL A 1 33  ? -2.16335  -31.10082 -18.19054 1.000 22.32701  ? 44  VAL A O     1 
ATOM   230  C  CB    . VAL A 1 33  ? -3.48937  -31.16101 -15.50895 1.000 17.49241  ? 44  VAL A CB    1 
ATOM   231  C  CG1   . VAL A 1 33  ? -2.19240  -30.99036 -14.70955 1.000 16.23778  ? 44  VAL A CG1   1 
ATOM   232  C  CG2   . VAL A 1 33  ? -4.70794  -31.15879 -14.60427 1.000 13.20800  ? 44  VAL A CG2   1 
ATOM   233  N  N     . TYR A 1 34  ? -1.51527  -29.09257 -17.41399 1.000 20.85834  ? 45  TYR A N     1 
ATOM   234  C  CA    . TYR A 1 34  ? -0.25380  -29.08934 -18.15937 1.000 18.59602  ? 45  TYR A CA    1 
ATOM   235  C  C     . TYR A 1 34  ? 0.89210   -29.40896 -17.20630 1.000 15.69640  ? 45  TYR A C     1 
ATOM   236  O  O     . TYR A 1 34  ? 1.12232   -28.67554 -16.24460 1.000 17.26887  ? 45  TYR A O     1 
ATOM   237  C  CB    . TYR A 1 34  ? -0.04198  -27.74384 -18.85555 1.000 16.62438  ? 45  TYR A CB    1 
ATOM   238  C  CG    . TYR A 1 34  ? -1.17872  -27.42686 -19.81953 1.000 18.55215  ? 45  TYR A CG    1 
ATOM   239  C  CD1   . TYR A 1 34  ? -1.20982  -27.98995 -21.08955 1.000 18.53202  ? 45  TYR A CD1   1 
ATOM   240  C  CD2   . TYR A 1 34  ? -2.22767  -26.60504 -19.44373 1.000 17.06361  ? 45  TYR A CD2   1 
ATOM   241  C  CE1   . TYR A 1 34  ? -2.23915  -27.72392 -21.97414 1.000 22.98506  ? 45  TYR A CE1   1 
ATOM   242  C  CE2   . TYR A 1 34  ? -3.27693  -26.33178 -20.31762 1.000 22.29402  ? 45  TYR A CE2   1 
ATOM   243  C  CZ    . TYR A 1 34  ? -3.27065  -26.89116 -21.58083 1.000 24.42767  ? 45  TYR A CZ    1 
ATOM   244  O  OH    . TYR A 1 34  ? -4.29167  -26.64013 -22.45062 1.000 22.40300  ? 45  TYR A OH    1 
ATOM   245  N  N     . GLU A 1 35  ? 1.60166   -30.50448 -17.46399 1.000 16.82736  ? 46  GLU A N     1 
ATOM   246  C  CA    . GLU A 1 35  ? 2.62557   -31.00946 -16.55479 1.000 21.08096  ? 46  GLU A CA    1 
ATOM   247  C  C     . GLU A 1 35  ? 3.95810   -31.11592 -17.29112 1.000 20.14894  ? 46  GLU A C     1 
ATOM   248  O  O     . GLU A 1 35  ? 4.01824   -31.68795 -18.38523 1.000 19.20058  ? 46  GLU A O     1 
ATOM   249  C  CB    . GLU A 1 35  ? 2.20355   -32.36884 -15.98248 1.000 20.85312  ? 46  GLU A CB    1 
ATOM   250  C  CG    . GLU A 1 35  ? 3.34999   -33.20475 -15.40269 1.000 19.54912  ? 46  GLU A CG    1 
ATOM   251  C  CD    . GLU A 1 35  ? 3.99807   -32.52086 -14.21327 1.000 18.64412  ? 46  GLU A CD    1 
ATOM   252  O  OE1   . GLU A 1 35  ? 3.25739   -32.03787 -13.33179 1.000 16.94916  ? 46  GLU A OE1   1 
ATOM   253  O  OE2   . GLU A 1 35  ? 5.24284   -32.43981 -14.16756 1.000 20.48675  ? 46  GLU A OE2   1 
ATOM   254  N  N     A ARG A 1 36  ? 5.02237   -30.57562 -16.68513 0.449 20.73656  ? 47  ARG A N     1 
ATOM   255  N  N     B ARG A 1 36  ? 5.02642   -30.57994 -16.68571 0.551 19.81039  ? 47  ARG A N     1 
ATOM   256  C  CA    A ARG A 1 36  ? 6.31650   -30.53706 -17.36702 0.449 22.97483  ? 47  ARG A CA    1 
ATOM   257  C  CA    B ARG A 1 36  ? 6.31203   -30.53962 -17.38585 0.551 23.00629  ? 47  ARG A CA    1 
ATOM   258  C  C     A ARG A 1 36  ? 6.92800   -31.92423 -17.52953 0.449 21.68925  ? 47  ARG A C     1 
ATOM   259  C  C     B ARG A 1 36  ? 6.94235   -31.92202 -17.52301 0.551 21.30953  ? 47  ARG A C     1 
ATOM   260  O  O     A ARG A 1 36  ? 7.68087   -32.14818 -18.48023 0.449 24.06930  ? 47  ARG A O     1 
ATOM   261  O  O     B ARG A 1 36  ? 7.71184   -32.14534 -18.45991 0.551 24.13036  ? 47  ARG A O     1 
ATOM   262  C  CB    A ARG A 1 36  ? 7.29712   -29.62865 -16.62024 0.449 23.10887  ? 47  ARG A CB    1 
ATOM   263  C  CB    B ARG A 1 36  ? 7.28927   -29.58067 -16.69064 0.551 23.07927  ? 47  ARG A CB    1 
ATOM   264  C  CG    A ARG A 1 36  ? 7.74402   -30.17527 -15.27846 0.449 23.77593  ? 47  ARG A CG    1 
ATOM   265  C  CG    B ARG A 1 36  ? 7.83309   -30.04355 -15.35002 0.551 23.82622  ? 47  ARG A CG    1 
ATOM   266  C  CD    A ARG A 1 36  ? 8.86686   -29.34877 -14.67648 0.449 23.84331  ? 47  ARG A CD    1 
ATOM   267  C  CD    B ARG A 1 36  ? 8.67705   -28.94621 -14.69348 0.551 23.99911  ? 47  ARG A CD    1 
ATOM   268  N  NE    A ARG A 1 36  ? 9.13402   -29.74275 -13.29760 0.449 23.79315  ? 47  ARG A NE    1 
ATOM   269  N  NE    B ARG A 1 36  ? 10.00152  -28.79841 -15.28935 0.551 26.09906  ? 47  ARG A NE    1 
ATOM   270  C  CZ    A ARG A 1 36  ? 9.75845   -28.98148 -12.40875 0.449 26.69608  ? 47  ARG A CZ    1 
ATOM   271  C  CZ    B ARG A 1 36  ? 10.80703  -27.75712 -15.09672 0.551 31.98690  ? 47  ARG A CZ    1 
ATOM   272  N  NH1   A ARG A 1 36  ? 10.21167  -27.77870 -12.72512 0.449 21.43060  ? 47  ARG A NH1   1 
ATOM   273  N  NH1   B ARG A 1 36  ? 10.44230  -26.72231 -14.35433 0.551 24.40983  ? 47  ARG A NH1   1 
ATOM   274  N  NH2   A ARG A 1 36  ? 9.91958   -29.43248 -11.16849 0.449 24.41821  ? 47  ARG A NH2   1 
ATOM   275  N  NH2   B ARG A 1 36  ? 12.00576  -27.74683 -15.67585 0.551 31.49689  ? 47  ARG A NH2   1 
ATOM   276  N  N     . ASP A 1 37  ? 6.63272   -32.85441 -16.62088 1.000 24.21878  ? 48  ASP A N     1 
ATOM   277  C  CA    . ASP A 1 37  ? 7.15746   -34.21656 -16.73106 1.000 23.77920  ? 48  ASP A CA    1 
ATOM   278  C  C     . ASP A 1 37  ? 6.85178   -34.80967 -18.09784 1.000 24.48282  ? 48  ASP A C     1 
ATOM   279  O  O     . ASP A 1 37  ? 5.73969   -34.66372 -18.61646 1.000 26.00096  ? 48  ASP A O     1 
ATOM   280  C  CB    . ASP A 1 37  ? 6.54028   -35.13259 -15.67183 1.000 25.29563  ? 48  ASP A CB    1 
ATOM   281  C  CG    . ASP A 1 37  ? 7.05154   -34.86830 -14.27397 1.000 28.41306  ? 48  ASP A CG    1 
ATOM   282  O  OD1   . ASP A 1 37  ? 8.13352   -34.25095 -14.12070 1.000 29.57676  ? 48  ASP A OD1   1 
ATOM   283  O  OD2   . ASP A 1 37  ? 6.35180   -35.29852 -13.32206 1.000 30.39144  ? 48  ASP A OD2   1 
ATOM   284  N  N     . ASN A 1 38  ? 7.84210   -35.50419 -18.66674 1.000 23.76514  ? 49  ASN A N     1 
ATOM   285  C  CA    . ASN A 1 38  ? 7.70208   -36.04156 -20.01719 1.000 37.55187  ? 49  ASN A CA    1 
ATOM   286  C  C     . ASN A 1 38  ? 6.59561   -37.09231 -20.12577 1.000 36.16041  ? 49  ASN A C     1 
ATOM   287  O  O     . ASN A 1 38  ? 5.95574   -37.18974 -21.17699 1.000 41.34076  ? 49  ASN A O     1 
ATOM   288  C  CB    . ASN A 1 38  ? 9.03281   -36.63033 -20.49925 1.000 36.12736  ? 49  ASN A CB    1 
ATOM   289  C  CG    . ASN A 1 38  ? 8.96014   -37.11740 -21.94323 1.000 52.07355  ? 49  ASN A CG    1 
ATOM   290  O  OD1   . ASN A 1 38  ? 9.19507   -36.35451 -22.88062 1.000 56.11093  ? 49  ASN A OD1   1 
ATOM   291  N  ND2   . ASN A 1 38  ? 8.61948   -38.39041 -22.12663 1.000 59.28013  ? 49  ASN A ND2   1 
ATOM   292  N  N     . ASP A 1 39  ? 6.35982   -37.89440 -19.08248 1.000 40.11051  ? 50  ASP A N     1 
ATOM   293  C  CA    . ASP A 1 39  ? 5.25899   -38.86075 -19.11051 1.000 39.43671  ? 50  ASP A CA    1 
ATOM   294  C  C     . ASP A 1 39  ? 4.97615   -39.34774 -17.69865 1.000 34.78660  ? 50  ASP A C     1 
ATOM   295  O  O     . ASP A 1 39  ? 5.72087   -39.05917 -16.75989 1.000 36.54492  ? 50  ASP A O     1 
ATOM   296  C  CB    . ASP A 1 39  ? 5.54925   -40.05624 -20.03304 1.000 45.58053  ? 50  ASP A CB    1 
ATOM   297  C  CG    . ASP A 1 39  ? 6.77306   -40.85820 -19.60279 1.000 43.61784  ? 50  ASP A CG    1 
ATOM   298  O  OD1   . ASP A 1 39  ? 6.85291   -41.28926 -18.43092 1.000 43.46406  ? 50  ASP A OD1   1 
ATOM   299  O  OD2   . ASP A 1 39  ? 7.65342   -41.07314 -20.45851 1.000 57.12731  ? 50  ASP A OD2   1 
ATOM   300  N  N     . ARG A 1 40  ? 3.90628   -40.13978 -17.56953 1.000 38.58200  ? 51  ARG A N     1 
ATOM   301  C  CA    . ARG A 1 40  ? 3.39136   -40.48688 -16.24776 1.000 37.34297  ? 51  ARG A CA    1 
ATOM   302  C  C     . ARG A 1 40  ? 4.25687   -41.48560 -15.50628 1.000 41.57391  ? 51  ARG A C     1 
ATOM   303  O  O     . ARG A 1 40  ? 4.05352   -41.65729 -14.30020 1.000 46.75572  ? 51  ARG A O     1 
ATOM   304  C  CB    . ARG A 1 40  ? 1.96556   -41.03856 -16.33846 1.000 47.39888  ? 51  ARG A CB    1 
ATOM   305  C  CG    . ARG A 1 40  ? 1.84541   -42.49118 -16.75603 1.000 46.25391  ? 51  ARG A CG    1 
ATOM   306  C  CD    . ARG A 1 40  ? 0.38763   -42.93257 -16.68296 1.000 59.26184  ? 51  ARG A CD    1 
ATOM   307  N  NE    . ARG A 1 40  ? 0.00429   -43.42221 -15.35967 1.000 59.92272  ? 51  ARG A NE    1 
ATOM   308  C  CZ    . ARG A 1 40  ? -1.24958  -43.60258 -14.95963 1.000 52.39199  ? 51  ARG A CZ    1 
ATOM   309  N  NH1   . ARG A 1 40  ? -2.27841  -43.27916 -15.73303 1.000 43.37836  ? 51  ARG A NH1   1 
ATOM   310  N  NH2   . ARG A 1 40  ? -1.47814  -44.12426 -13.75628 1.000 48.13672  ? 51  ARG A NH2   1 
ATOM   311  N  N     . GLU A 1 41  ? 5.19956   -42.14610 -16.18313 1.000 39.78445  ? 52  GLU A N     1 
ATOM   312  C  CA    . GLU A 1 41  ? 6.09830   -43.08737 -15.52484 1.000 41.41246  ? 52  GLU A CA    1 
ATOM   313  C  C     . GLU A 1 41  ? 7.29406   -42.40676 -14.87364 1.000 38.44129  ? 52  GLU A C     1 
ATOM   314  O  O     . GLU A 1 41  ? 8.11973   -43.09449 -14.26885 1.000 40.01885  ? 52  GLU A O     1 
ATOM   315  C  CB    . GLU A 1 41  ? 6.59635   -44.14392 -16.52326 1.000 54.13404  ? 52  GLU A CB    1 
ATOM   316  C  CG    . GLU A 1 41  ? 5.50462   -44.79516 -17.38569 1.000 52.88065  ? 52  GLU A CG    1 
ATOM   317  C  CD    . GLU A 1 41  ? 4.50312   -45.62272 -16.58480 1.000 64.98850  ? 52  GLU A CD    1 
ATOM   318  O  OE1   . GLU A 1 41  ? 4.78595   -45.95952 -15.41182 1.000 67.25975  ? 52  GLU A OE1   1 
ATOM   319  O  OE2   . GLU A 1 41  ? 3.42201   -45.93738 -17.13493 1.000 74.55375  ? 52  GLU A OE2   1 
ATOM   320  N  N     . ALA A 1 42  ? 7.41830   -41.08824 -14.99546 1.000 38.05219  ? 53  ALA A N     1 
ATOM   321  C  CA    . ALA A 1 42  ? 8.46408   -40.35030 -14.29728 1.000 46.58429  ? 53  ALA A CA    1 
ATOM   322  C  C     . ALA A 1 42  ? 8.42032   -40.63675 -12.79916 1.000 40.93725  ? 53  ALA A C     1 
ATOM   323  O  O     . ALA A 1 42  ? 7.39121   -40.44378 -12.15360 1.000 38.03415  ? 53  ALA A O     1 
ATOM   324  C  CB    . ALA A 1 42  ? 8.28865   -38.84965 -14.55985 1.000 37.09879  ? 53  ALA A CB    1 
ATOM   325  N  N     . ARG A 1 43  ? 9.53179   -41.11381 -12.24900 1.000 32.57158  ? 54  ARG A N     1 
ATOM   326  C  CA    . ARG A 1 43  ? 9.59904   -41.37602 -10.81869 1.000 36.27816  ? 54  ARG A CA    1 
ATOM   327  C  C     . ARG A 1 43  ? 9.56899   -40.06536 -10.04111 1.000 35.82265  ? 54  ARG A C     1 
ATOM   328  O  O     . ARG A 1 43  ? 10.20823  -39.08393 -10.42347 1.000 33.13402  ? 54  ARG A O     1 
ATOM   329  C  CB    . ARG A 1 43  ? 10.87328  -42.15146 -10.48303 1.000 44.24487  ? 54  ARG A CB    1 
ATOM   330  C  CG    . ARG A 1 43  ? 10.73267  -43.16065 -9.35603  1.000 49.07878  ? 54  ARG A CG    1 
ATOM   331  C  CD    . ARG A 1 43  ? 9.71693   -44.23703 -9.71693  1.000 60.86104  ? 54  ARG A CD    1 
ATOM   332  N  NE    . ARG A 1 43  ? 9.15926   -44.87558 -8.52912  1.000 70.58702  ? 54  ARG A NE    1 
ATOM   333  C  CZ    . ARG A 1 43  ? 7.97328   -45.46967 -8.48299  1.000 65.81778  ? 54  ARG A CZ    1 
ATOM   334  N  NH1   . ARG A 1 43  ? 7.18540   -45.53051 -9.55016  1.000 56.39685  ? 54  ARG A NH1   1 
ATOM   335  N  NH2   . ARG A 1 43  ? 7.55981   -45.99978 -7.33479  1.000 56.43668  ? 54  ARG A NH2   1 
ATOM   336  N  N     . ILE A 1 44  ? 8.81020   -40.03893 -8.95404  1.000 32.51236  ? 55  ILE A N     1 
ATOM   337  C  CA    . ILE A 1 44  ? 8.77240   -38.88607 -8.06150  1.000 26.85777  ? 55  ILE A CA    1 
ATOM   338  C  C     . ILE A 1 44  ? 9.65275   -39.20230 -6.86514  1.000 33.93825  ? 55  ILE A C     1 
ATOM   339  O  O     . ILE A 1 44  ? 9.35245   -40.12183 -6.09314  1.000 30.11244  ? 55  ILE A O     1 
ATOM   340  C  CB    . ILE A 1 44  ? 7.34623   -38.55520 -7.60277  1.000 24.03207  ? 55  ILE A CB    1 
ATOM   341  C  CG1   . ILE A 1 44  ? 6.43504   -38.26501 -8.79086  1.000 27.08553  ? 55  ILE A CG1   1 
ATOM   342  C  CG2   . ILE A 1 44  ? 7.37422   -37.38713 -6.61682  1.000 24.31779  ? 55  ILE A CG2   1 
ATOM   343  C  CD1   . ILE A 1 44  ? 4.97608   -38.34523 -8.44555  1.000 21.18880  ? 55  ILE A CD1   1 
ATOM   344  N  N     . PHE A 1 45  ? 10.73348  -38.44347 -6.71702  1.000 29.73223  ? 56  PHE A N     1 
ATOM   345  C  CA    . PHE A 1 45  ? 11.64469  -38.60717 -5.59503  1.000 35.39575  ? 56  PHE A CA    1 
ATOM   346  C  C     . PHE A 1 45  ? 11.03400  -37.99705 -4.33666  1.000 29.82637  ? 56  PHE A C     1 
ATOM   347  O  O     . PHE A 1 45  ? 10.36458  -36.96303 -4.39669  1.000 28.54731  ? 56  PHE A O     1 
ATOM   348  C  CB    . PHE A 1 45  ? 12.98687  -37.94293 -5.92526  1.000 28.54095  ? 56  PHE A CB    1 
ATOM   349  C  CG    . PHE A 1 45  ? 13.99914  -38.00241 -4.81178  1.000 29.64807  ? 56  PHE A CG    1 
ATOM   350  C  CD1   . PHE A 1 45  ? 14.76589  -39.13905 -4.61463  1.000 26.82035  ? 56  PHE A CD1   1 
ATOM   351  C  CD2   . PHE A 1 45  ? 14.19893  -36.91127 -3.98039  1.000 31.46168  ? 56  PHE A CD2   1 
ATOM   352  C  CE1   . PHE A 1 45  ? 15.69814  -39.19787 -3.59939  1.000 31.33241  ? 56  PHE A CE1   1 
ATOM   353  C  CE2   . PHE A 1 45  ? 15.13022  -36.96070 -2.95885  1.000 28.50140  ? 56  PHE A CE2   1 
ATOM   354  C  CZ    . PHE A 1 45  ? 15.88425  -38.10069 -2.76746  1.000 26.50437  ? 56  PHE A CZ    1 
ATOM   355  N  N     . GLY A 1 46  ? 11.26102  -38.64589 -3.19324  1.000 28.90111  ? 57  GLY A N     1 
ATOM   356  C  CA    . GLY A 1 46  ? 10.79936  -38.09924 -1.92585  1.000 25.03861  ? 57  GLY A CA    1 
ATOM   357  C  C     . GLY A 1 46  ? 10.19660  -39.11658 -0.98324  1.000 24.41648  ? 57  GLY A C     1 
ATOM   358  O  O     . GLY A 1 46  ? 10.01679  -40.27887 -1.35492  1.000 23.25293  ? 57  GLY A O     1 
ATOM   359  N  N     . GLY A 1 47  ? 9.88047   -38.69788 0.23807   1.000 26.78031  ? 58  GLY A N     1 
ATOM   360  C  CA    . GLY A 1 47  ? 9.21516   -39.56924 1.18177   1.000 26.18578  ? 58  GLY A CA    1 
ATOM   361  C  C     . GLY A 1 47  ? 7.73736   -39.74457 0.84871   1.000 29.32030  ? 58  GLY A C     1 
ATOM   362  O  O     . GLY A 1 47  ? 7.24709   -39.38168 -0.22147  1.000 25.53297  ? 58  GLY A O     1 
ATOM   363  N  N     . THR A 1 48  ? 7.01984   -40.32552 1.80372   1.000 22.67195  ? 59  THR A N     1 
ATOM   364  C  CA    . THR A 1 48  ? 5.59626   -40.53624 1.64462   1.000 21.88493  ? 59  THR A CA    1 
ATOM   365  C  C     . THR A 1 48  ? 4.81070   -39.28057 2.03855   1.000 26.40364  ? 59  THR A C     1 
ATOM   366  O  O     . THR A 1 48  ? 5.34510   -38.33858 2.63090   1.000 20.33611  ? 59  THR A O     1 
ATOM   367  C  CB    . THR A 1 48  ? 5.15215   -41.71161 2.49778   1.000 28.68265  ? 59  THR A CB    1 
ATOM   368  O  OG1   . THR A 1 48  ? 5.57880   -41.47034 3.83937   1.000 24.30284  ? 59  THR A OG1   1 
ATOM   369  C  CG2   . THR A 1 48  ? 5.76687   -43.02472 1.97518   1.000 19.64634  ? 59  THR A CG2   1 
ATOM   370  N  N     . LEU A 1 49  ? 3.51802   -39.28472 1.69801   1.000 21.46965  ? 60  LEU A N     1 
ATOM   371  C  CA    . LEU A 1 49  ? 2.55573   -38.27262 2.12867   1.000 23.77546  ? 60  LEU A CA    1 
ATOM   372  C  C     . LEU A 1 49  ? 1.46427   -38.91782 2.97328   1.000 23.59107  ? 60  LEU A C     1 
ATOM   373  O  O     . LEU A 1 49  ? 1.03391   -40.04487 2.70802   1.000 26.44297  ? 60  LEU A O     1 
ATOM   374  C  CB    . LEU A 1 49  ? 1.89955   -37.55507 0.93276   1.000 18.19469  ? 60  LEU A CB    1 
ATOM   375  C  CG    . LEU A 1 49  ? 2.82255   -36.68301 0.08010   1.000 20.25977  ? 60  LEU A CG    1 
ATOM   376  C  CD1   . LEU A 1 49  ? 2.12486   -36.21932 -1.20838  1.000 15.18859  ? 60  LEU A CD1   1 
ATOM   377  C  CD2   . LEU A 1 49  ? 3.27922   -35.51891 0.89924   1.000 18.80017  ? 60  LEU A CD2   1 
ATOM   378  N  N     . ASP A 1 50  ? 1.01694   -38.19841 3.99193   1.000 26.98360  ? 61  ASP A N     1 
ATOM   379  C  CA    . ASP A 1 50  ? -0.10426  -38.61353 4.81779   1.000 29.60764  ? 61  ASP A CA    1 
ATOM   380  C  C     . ASP A 1 50  ? -1.19724  -37.56125 4.69582   1.000 29.70969  ? 61  ASP A C     1 
ATOM   381  O  O     . ASP A 1 50  ? -0.92154  -36.36291 4.80490   1.000 32.41351  ? 61  ASP A O     1 
ATOM   382  C  CB    . ASP A 1 50  ? 0.32034   -38.79071 6.27685   1.000 29.35815  ? 61  ASP A CB    1 
ATOM   383  C  CG    . ASP A 1 50  ? 0.84358   -37.50884 6.88547   1.000 39.97128  ? 61  ASP A CG    1 
ATOM   384  O  OD1   . ASP A 1 50  ? 1.66838   -36.83652 6.22422   1.000 45.92985  ? 61  ASP A OD1   1 
ATOM   385  O  OD2   . ASP A 1 50  ? 0.42290   -37.15956 8.01064   1.000 39.59180  ? 61  ASP A OD2   1 
ATOM   386  N  N     . LEU A 1 51  ? -2.42489  -38.00219 4.44610   1.000 23.91419  ? 62  LEU A N     1 
ATOM   387  C  CA    . LEU A 1 51  ? -3.55879  -37.10024 4.28771   1.000 28.00409  ? 62  LEU A CA    1 
ATOM   388  C  C     . LEU A 1 51  ? -4.37905  -37.06868 5.57502   1.000 25.79688  ? 62  LEU A C     1 
ATOM   389  O  O     . LEU A 1 51  ? -4.64840  -38.11299 6.17045   1.000 27.34728  ? 62  LEU A O     1 
ATOM   390  C  CB    . LEU A 1 51  ? -4.42859  -37.53315 3.10495   1.000 27.38229  ? 62  LEU A CB    1 
ATOM   391  C  CG    . LEU A 1 51  ? -3.65672  -37.75690 1.79391   1.000 30.27148  ? 62  LEU A CG    1 
ATOM   392  C  CD1   . LEU A 1 51  ? -4.59433  -38.07571 0.63113   1.000 31.65487  ? 62  LEU A CD1   1 
ATOM   393  C  CD2   . LEU A 1 51  ? -2.79198  -36.57059 1.43913   1.000 24.68263  ? 62  LEU A CD2   1 
ATOM   394  N  N     . HIS A 1 52  ? -4.77027  -35.87110 6.00000   1.000 22.98427  ? 63  HIS A N     1 
ATOM   395  C  CA    . HIS A 1 52  ? -5.39276  -35.65350 7.29944   1.000 27.83912  ? 63  HIS A CA    1 
ATOM   396  C  C     . HIS A 1 52  ? -6.91159  -35.57607 7.17951   1.000 30.29144  ? 63  HIS A C     1 
ATOM   397  O  O     . HIS A 1 52  ? -7.45370  -35.12578 6.16754   1.000 29.78525  ? 63  HIS A O     1 
ATOM   398  C  CB    . HIS A 1 52  ? -4.87216  -34.36293 7.94819   1.000 25.44084  ? 63  HIS A CB    1 
ATOM   399  C  CG    . HIS A 1 52  ? -3.38732  -34.34213 8.16304   1.000 39.42657  ? 63  HIS A CG    1 
ATOM   400  N  ND1   . HIS A 1 52  ? -2.66453  -33.16885 8.25540   1.000 40.79110  ? 63  HIS A ND1   1 
ATOM   401  C  CD2   . HIS A 1 52  ? -2.48924  -35.34867 8.30458   1.000 33.04335  ? 63  HIS A CD2   1 
ATOM   402  C  CE1   . HIS A 1 52  ? -1.38645  -33.45364 8.44059   1.000 41.56363  ? 63  HIS A CE1   1 
ATOM   403  N  NE2   . HIS A 1 52  ? -1.25199  -34.76864 8.47062   1.000 42.43558  ? 63  HIS A NE2   1 
ATOM   404  N  N     . LYS A 1 53  ? -7.59700  -36.01780 8.23000   1.000 33.30231  ? 64  LYS A N     1 
ATOM   405  C  CA    . LYS A 1 53  ? -9.03694  -35.82453 8.29321   1.000 34.87383  ? 64  LYS A CA    1 
ATOM   406  C  C     . LYS A 1 53  ? -9.34664  -34.33705 8.34228   1.000 37.37262  ? 64  LYS A C     1 
ATOM   407  O  O     . LYS A 1 53  ? -8.63587  -33.56260 8.98588   1.000 41.80881  ? 64  LYS A O     1 
ATOM   408  C  CB    . LYS A 1 53  ? -9.61843  -36.53994 9.50922   1.000 39.69166  ? 64  LYS A CB    1 
ATOM   409  C  CG    . LYS A 1 53  ? -9.54812  -38.06141 9.38046   1.000 44.55196  ? 64  LYS A CG    1 
ATOM   410  C  CD    . LYS A 1 53  ? -10.34803 -38.78532 10.44808  1.000 46.88074  ? 64  LYS A CD    1 
ATOM   411  C  CE    . LYS A 1 53  ? -10.28060 -40.28494 10.21717  1.000 41.23857  ? 64  LYS A CE    1 
ATOM   412  N  NZ    . LYS A 1 53  ? -10.18260 -41.05068 11.49764  1.000 58.54133  ? 64  LYS A NZ    1 
ATOM   413  N  N     . GLY A 1 54  ? -10.39447 -33.93181 7.62607   1.000 37.15979  ? 65  GLY A N     1 
ATOM   414  C  CA    . GLY A 1 54  ? -10.77100 -32.53960 7.53821   1.000 31.23247  ? 65  GLY A CA    1 
ATOM   415  C  C     . GLY A 1 54  ? -10.07542 -31.75456 6.44265   1.000 34.58091  ? 65  GLY A C     1 
ATOM   416  O  O     . GLY A 1 54  ? -10.52889 -30.65673 6.10527   1.000 39.92540  ? 65  GLY A O     1 
ATOM   417  N  N     . SER A 1 55  ? -9.00009  -32.28210 5.86144   1.000 28.19857  ? 66  SER A N     1 
ATOM   418  C  CA    . SER A 1 55  ? -8.30899  -31.54360 4.82002   1.000 30.33133  ? 66  SER A CA    1 
ATOM   419  C  C     . SER A 1 55  ? -7.99919  -32.45992 3.65072   1.000 29.79579  ? 66  SER A C     1 
ATOM   420  O  O     . SER A 1 55  ? -8.84862  -32.63171 2.77012   1.000 28.48835  ? 66  SER A O     1 
ATOM   421  C  CB    . SER A 1 55  ? -7.04162  -30.87829 5.36902   1.000 24.31896  ? 66  SER A CB    1 
ATOM   422  O  OG    . SER A 1 55  ? -6.23124  -31.81301 6.03969   1.000 31.60144  ? 66  SER A OG    1 
ATOM   423  N  N     . GLY A 1 56  ? -6.79528  -33.04157 3.61991   1.000 22.72339  ? 67  GLY A N     1 
ATOM   424  C  CA    . GLY A 1 56  ? -6.44682  -33.92877 2.51919   1.000 23.71244  ? 67  GLY A CA    1 
ATOM   425  C  C     . GLY A 1 56  ? -7.44211  -35.06053 2.32950   1.000 26.95958  ? 67  GLY A C     1 
ATOM   426  O  O     . GLY A 1 56  ? -7.84222  -35.36937 1.20626   1.000 26.00565  ? 67  GLY A O     1 
ATOM   427  N  N     . GLN A 1 57  ? -7.87304  -35.68241 3.42456   1.000 20.94354  ? 68  GLN A N     1 
ATOM   428  C  CA    . GLN A 1 57  ? -8.81880  -36.77603 3.28242   1.000 27.60549  ? 68  GLN A CA    1 
ATOM   429  C  C     . GLN A 1 57  ? -10.18310 -36.27617 2.85141   1.000 28.22426  ? 68  GLN A C     1 
ATOM   430  O  O     . GLN A 1 57  ? -10.93448 -37.02781 2.23231   1.000 27.11779  ? 68  GLN A O     1 
ATOM   431  C  CB    . GLN A 1 57  ? -8.94563  -37.55443 4.58436   1.000 24.02345  ? 68  GLN A CB    1 
ATOM   432  C  CG    . GLN A 1 57  ? -7.68423  -38.29695 4.99826   1.000 25.58638  ? 68  GLN A CG    1 
ATOM   433  C  CD    . GLN A 1 57  ? -7.94247  -39.26977 6.13878   1.000 27.05226  ? 68  GLN A CD    1 
ATOM   434  O  OE1   . GLN A 1 57  ? -9.05067  -39.78040 6.28590   1.000 27.05457  ? 68  GLN A OE1   1 
ATOM   435  N  NE2   . GLN A 1 57  ? -6.92890  -39.51059 6.95973   1.000 21.47355  ? 68  GLN A NE2   1 
ATOM   436  N  N     . GLU A 1 58  ? -10.53267 -35.02832 3.18377   1.000 24.89924  ? 69  GLU A N     1 
ATOM   437  C  CA    . GLU A 1 58  ? -11.83912 -34.51224 2.78281   1.000 23.88563  ? 69  GLU A CA    1 
ATOM   438  C  C     . GLU A 1 58  ? -11.87413 -34.23448 1.29173   1.000 27.40811  ? 69  GLU A C     1 
ATOM   439  O  O     . GLU A 1 58  ? -12.92254 -34.38877 0.65210   1.000 25.65627  ? 69  GLU A O     1 
ATOM   440  C  CB    . GLU A 1 58  ? -12.17302 -33.24719 3.56599   1.000 25.35183  ? 69  GLU A CB    1 
ATOM   441  C  CG    . GLU A 1 58  ? -13.61560 -32.84696 3.48806   1.000 37.32458  ? 69  GLU A CG    1 
ATOM   442  C  CD    . GLU A 1 58  ? -14.52296 -33.80577 4.23353   1.000 34.64462  ? 69  GLU A CD    1 
ATOM   443  O  OE1   . GLU A 1 58  ? -14.01675 -34.60264 5.05284   1.000 34.30815  ? 69  GLU A OE1   1 
ATOM   444  O  OE2   . GLU A 1 58  ? -15.74481 -33.75934 3.98904   1.000 42.93152  ? 69  GLU A OE2   1 
ATOM   445  N  N     . ALA A 1 59  ? -10.72982 -33.84757 0.71986   1.000 21.85676  ? 70  ALA A N     1 
ATOM   446  C  CA    . ALA A 1 59  ? -10.64335 -33.71207 -0.72462  1.000 25.75078  ? 70  ALA A CA    1 
ATOM   447  C  C     . ALA A 1 59  ? -10.80037 -35.06338 -1.40717  1.000 28.48590  ? 70  ALA A C     1 
ATOM   448  O  O     . ALA A 1 59  ? -11.49747 -35.16594 -2.42152  1.000 26.39570  ? 70  ALA A O     1 
ATOM   449  C  CB    . ALA A 1 59  ? -9.31559  -33.05911 -1.11437  1.000 21.76086  ? 70  ALA A CB    1 
ATOM   450  N  N     . MET A 1 60  ? -10.15050 -36.10776 -0.87548  1.000 23.77339  ? 71  MET A N     1 
ATOM   451  C  CA    . MET A 1 60  ? -10.30927 -37.44792 -1.44546  1.000 28.13805  ? 71  MET A CA    1 
ATOM   452  C  C     . MET A 1 60  ? -11.74443 -37.93949 -1.31626  1.000 25.53046  ? 71  MET A C     1 
ATOM   453  O  O     . MET A 1 60  ? -12.29099 -38.52573 -2.25626  1.000 27.25753  ? 71  MET A O     1 
ATOM   454  C  CB    . MET A 1 60  ? -9.34570  -38.43749 -0.77738  1.000 24.38473  ? 71  MET A CB    1 
ATOM   455  C  CG    . MET A 1 60  ? -7.84587  -38.14918 -1.02410  1.000 25.30591  ? 71  MET A CG    1 
ATOM   456  S  SD    . MET A 1 60  ? -7.36541  -38.04387 -2.77215  1.000 27.24257  ? 71  MET A SD    1 
ATOM   457  C  CE    . MET A 1 60  ? -7.51896  -36.30639 -3.14161  1.000 34.22403  ? 71  MET A CE    1 
ATOM   458  N  N     A LYS A 1 61  ? -12.36748 -37.70565 -0.15951  0.493 23.43607  ? 72  LYS A N     1 
ATOM   459  N  N     B LYS A 1 61  ? -12.36414 -37.72140 -0.15396  0.507 23.52524  ? 72  LYS A N     1 
ATOM   460  C  CA    A LYS A 1 61  ? -13.75904 -38.09418 0.04279   0.493 26.14827  ? 72  LYS A CA    1 
ATOM   461  C  CA    B LYS A 1 61  ? -13.76337 -38.08906 0.03747   0.507 26.14593  ? 72  LYS A CA    1 
ATOM   462  C  C     A LYS A 1 61  ? -14.66498 -37.44525 -0.99876  0.493 26.27526  ? 72  LYS A C     1 
ATOM   463  C  C     B LYS A 1 61  ? -14.64891 -37.44844 -1.02202  0.507 26.26872  ? 72  LYS A C     1 
ATOM   464  O  O     A LYS A 1 61  ? -15.48270 -38.11928 -1.63481  0.493 27.06550  ? 72  LYS A O     1 
ATOM   465  O  O     B LYS A 1 61  ? -15.44034 -38.12791 -1.68512  0.507 27.04352  ? 72  LYS A O     1 
ATOM   466  C  CB    A LYS A 1 61  ? -14.18992 -37.71735 1.46367   0.493 26.54205  ? 72  LYS A CB    1 
ATOM   467  C  CB    B LYS A 1 61  ? -14.21601 -37.67748 1.44000   0.507 26.55559  ? 72  LYS A CB    1 
ATOM   468  C  CG    A LYS A 1 61  ? -15.38040 -38.49254 2.03261   0.493 27.81051  ? 72  LYS A CG    1 
ATOM   469  C  CG    B LYS A 1 61  ? -15.71388 -37.80942 1.71112   0.507 25.92808  ? 72  LYS A CG    1 
ATOM   470  C  CD    A LYS A 1 61  ? -15.44582 -38.34487 3.56539   0.493 28.26008  ? 72  LYS A CD    1 
ATOM   471  C  CD    B LYS A 1 61  ? -16.01107 -37.53938 3.19566   0.507 28.40714  ? 72  LYS A CD    1 
ATOM   472  C  CE    A LYS A 1 61  ? -16.68381 -39.02279 4.17392   0.493 36.98120  ? 72  LYS A CE    1 
ATOM   473  C  CE    B LYS A 1 61  ? -17.45475 -37.87875 3.56724   0.507 32.73975  ? 72  LYS A CE    1 
ATOM   474  N  NZ    A LYS A 1 61  ? -16.70112 -40.52495 4.09295   0.493 27.54097  ? 72  LYS A NZ    1 
ATOM   475  N  NZ    B LYS A 1 61  ? -17.67657 -37.84390 5.04597   0.507 37.33289  ? 72  LYS A NZ    1 
ATOM   476  N  N     . LYS A 1 62  ? -14.50913 -36.13425 -1.20771  1.000 26.02667  ? 73  LYS A N     1 
ATOM   477  C  CA    . LYS A 1 62  ? -15.33097 -35.42457 -2.18483  1.000 26.58510  ? 73  LYS A CA    1 
ATOM   478  C  C     . LYS A 1 62  ? -15.15284 -35.99668 -3.58867  1.000 26.73961  ? 73  LYS A C     1 
ATOM   479  O  O     . LYS A 1 62  ? -16.08690 -35.96553 -4.40227  1.000 21.35573  ? 73  LYS A O     1 
ATOM   480  C  CB    . LYS A 1 62  ? -14.96469 -33.93183 -2.15524  1.000 28.06410  ? 73  LYS A CB    1 
ATOM   481  C  CG    . LYS A 1 62  ? -15.84391 -33.00915 -2.99856  1.000 35.50240  ? 73  LYS A CG    1 
ATOM   482  C  CD    . LYS A 1 62  ? -17.16002 -32.68236 -2.31076  1.000 45.69499  ? 73  LYS A CD    1 
ATOM   483  C  CE    . LYS A 1 62  ? -18.06527 -31.82900 -3.20745  1.000 44.66146  ? 73  LYS A CE    1 
ATOM   484  N  NZ    . LYS A 1 62  ? -19.49660 -31.91908 -2.74296  1.000 53.34527  ? 73  LYS A NZ    1 
ATOM   485  N  N     . ALA A 1 63  ? -13.96718 -36.52678 -3.88392  1.000 21.02629  ? 74  ALA A N     1 
ATOM   486  C  CA    . ALA A 1 63  ? -13.64298 -37.05965 -5.19654  1.000 22.02091  ? 74  ALA A CA    1 
ATOM   487  C  C     . ALA A 1 63  ? -14.02782 -38.52222 -5.36003  1.000 24.48247  ? 74  ALA A C     1 
ATOM   488  O  O     . ALA A 1 63  ? -13.80796 -39.08100 -6.43817  1.000 27.09367  ? 74  ALA A O     1 
ATOM   489  C  CB    . ALA A 1 63  ? -12.14163 -36.89371 -5.47012  1.000 22.01332  ? 74  ALA A CB    1 
ATOM   490  N  N     . GLY A 1 64  ? -14.57897 -39.15794 -4.32461  1.000 24.80600  ? 75  GLY A N     1 
ATOM   491  C  CA    . GLY A 1 64  ? -14.84927 -40.58387 -4.37743  1.000 27.89447  ? 75  GLY A CA    1 
ATOM   492  C  C     . GLY A 1 64  ? -13.61507 -41.45064 -4.30655  1.000 28.37771  ? 75  GLY A C     1 
ATOM   493  O  O     . GLY A 1 64  ? -13.65337 -42.61324 -4.72063  1.000 30.99505  ? 75  GLY A O     1 
ATOM   494  N  N     . LEU A 1 65  ? -12.51824 -40.92242 -3.77832  1.000 25.00256  ? 76  LEU A N     1 
ATOM   495  C  CA    . LEU A 1 65  ? -11.24790 -41.62906 -3.79020  1.000 30.49788  ? 76  LEU A CA    1 
ATOM   496  C  C     . LEU A 1 65  ? -10.74420 -41.98059 -2.40291  1.000 27.83083  ? 76  LEU A C     1 
ATOM   497  O  O     . LEU A 1 65  ? -9.61600  -42.46985 -2.28693  1.000 29.93141  ? 76  LEU A O     1 
ATOM   498  C  CB    . LEU A 1 65  ? -10.17649 -40.79207 -4.51973  1.000 22.30483  ? 76  LEU A CB    1 
ATOM   499  C  CG    . LEU A 1 65  ? -10.49917 -40.50671 -5.99698  1.000 25.98040  ? 76  LEU A CG    1 
ATOM   500  C  CD1   . LEU A 1 65  ? -9.54326  -39.48166 -6.58501  1.000 24.87505  ? 76  LEU A CD1   1 
ATOM   501  C  CD2   . LEU A 1 65  ? -10.51111 -41.79306 -6.83395  1.000 27.44620  ? 76  LEU A CD2   1 
ATOM   502  N  N     . LEU A 1 66  ? -11.52936 -41.73707 -1.34991  1.000 28.84743  ? 77  LEU A N     1 
ATOM   503  C  CA    . LEU A 1 66  ? -11.01377 -41.93800 0.00154   1.000 29.85813  ? 77  LEU A CA    1 
ATOM   504  C  C     . LEU A 1 66  ? -10.64451 -43.40150 0.24851   1.000 29.48681  ? 77  LEU A C     1 
ATOM   505  O  O     . LEU A 1 66  ? -9.61892  -43.69298 0.87687   1.000 30.10228  ? 77  LEU A O     1 
ATOM   506  C  CB    . LEU A 1 66  ? -12.02887 -41.45588 1.04243   1.000 26.92728  ? 77  LEU A CB    1 
ATOM   507  C  CG    . LEU A 1 66  ? -11.45412 -41.51495 2.46864   1.000 25.99513  ? 77  LEU A CG    1 
ATOM   508  C  CD1   . LEU A 1 66  ? -10.10374 -40.76877 2.50346   1.000 23.22867  ? 77  LEU A CD1   1 
ATOM   509  C  CD2   . LEU A 1 66  ? -12.43179 -40.98305 3.54512   1.000 23.89214  ? 77  LEU A CD2   1 
ATOM   510  N  N     . GLN A 1 67  ? -11.46969 -44.33812 -0.22327  1.000 27.27600  ? 78  GLN A N     1 
ATOM   511  C  CA    . GLN A 1 67  ? -11.12295 -45.74258 -0.04207  1.000 28.06544  ? 78  GLN A CA    1 
ATOM   512  C  C     . GLN A 1 67  ? -9.90807  -46.11213 -0.88193  1.000 31.23932  ? 78  GLN A C     1 
ATOM   513  O  O     . GLN A 1 67  ? -9.04178  -46.86754 -0.42653  1.000 31.77625  ? 78  GLN A O     1 
ATOM   514  C  CB    . GLN A 1 67  ? -12.30422 -46.64230 -0.38813  1.000 28.16642  ? 78  GLN A CB    1 
ATOM   515  C  CG    . GLN A 1 67  ? -12.10957 -48.08633 0.09711   1.000 28.91877  ? 78  GLN A CG    1 
ATOM   516  C  CD    . GLN A 1 67  ? -12.05085 -48.18459 1.61464   1.000 34.70943  ? 78  GLN A CD    1 
ATOM   517  O  OE1   . GLN A 1 67  ? -12.90321 -47.63075 2.30349   1.000 37.50247  ? 78  GLN A OE1   1 
ATOM   518  N  NE2   . GLN A 1 67  ? -11.03661 -48.87830 2.14283   1.000 29.22413  ? 78  GLN A NE2   1 
ATOM   519  N  N     . THR A 1 68  ? -9.81828  -45.57377 -2.10411  1.000 28.88231  ? 79  THR A N     1 
ATOM   520  C  CA    . THR A 1 68  ? -8.65993  -45.84432 -2.94938  1.000 27.91316  ? 79  THR A CA    1 
ATOM   521  C  C     . THR A 1 68  ? -7.37603  -45.47244 -2.21909  1.000 32.48713  ? 79  THR A C     1 
ATOM   522  O  O     . THR A 1 68  ? -6.41401  -46.24933 -2.19320  1.000 33.61735  ? 79  THR A O     1 
ATOM   523  C  CB    . THR A 1 68  ? -8.78063  -45.07836 -4.27056  1.000 28.73811  ? 79  THR A CB    1 
ATOM   524  O  OG1   . THR A 1 68  ? -10.12700 -45.15859 -4.74522  1.000 30.88939  ? 79  THR A OG1   1 
ATOM   525  C  CG2   . THR A 1 68  ? -7.84272  -45.66947 -5.34170  1.000 31.40763  ? 79  THR A CG2   1 
ATOM   526  N  N     . TYR A 1 69  ? -7.36578  -44.29280 -1.58971  1.000 27.89960  ? 80  TYR A N     1 
ATOM   527  C  CA    . TYR A 1 69  ? -6.22951  -43.85914 -0.78180  1.000 25.94045  ? 80  TYR A CA    1 
ATOM   528  C  C     . TYR A 1 69  ? -5.95912  -44.81637 0.37451   1.000 26.72826  ? 80  TYR A C     1 
ATOM   529  O  O     . TYR A 1 69  ? -4.81415  -45.20918 0.60381   1.000 29.16857  ? 80  TYR A O     1 
ATOM   530  C  CB    . TYR A 1 69  ? -6.48574  -42.44096 -0.26391  1.000 25.11774  ? 80  TYR A CB    1 
ATOM   531  C  CG    . TYR A 1 69  ? -5.65842  -42.02260 0.94314   1.000 24.38414  ? 80  TYR A CG    1 
ATOM   532  C  CD1   . TYR A 1 69  ? -4.27736  -41.83042 0.84992   1.000 25.56818  ? 80  TYR A CD1   1 
ATOM   533  C  CD2   . TYR A 1 69  ? -6.27353  -41.78267 2.17181   1.000 29.65882  ? 80  TYR A CD2   1 
ATOM   534  C  CE1   . TYR A 1 69  ? -3.52902  -41.42346 1.96444   1.000 27.54989  ? 80  TYR A CE1   1 
ATOM   535  C  CE2   . TYR A 1 69  ? -5.54852  -41.38277 3.28305   1.000 22.75224  ? 80  TYR A CE2   1 
ATOM   536  C  CZ    . TYR A 1 69  ? -4.17912  -41.20621 3.17685   1.000 31.75451  ? 80  TYR A CZ    1 
ATOM   537  O  OH    . TYR A 1 69  ? -3.47335  -40.81183 4.28999   1.000 31.08272  ? 80  TYR A OH    1 
ATOM   538  N  N     . TYR A 1 70  ? -6.99896  -45.19841 1.12529   1.000 28.69734  ? 81  TYR A N     1 
ATOM   539  C  CA    . TYR A 1 70  ? -6.78238  -46.09085 2.26349   1.000 28.94115  ? 81  TYR A CA    1 
ATOM   540  C  C     . TYR A 1 70  ? -6.17911  -47.42496 1.82126   1.000 33.90060  ? 81  TYR A C     1 
ATOM   541  O  O     . TYR A 1 70  ? -5.35893  -48.01174 2.53956   1.000 28.90987  ? 81  TYR A O     1 
ATOM   542  C  CB    . TYR A 1 70  ? -8.08806  -46.35862 3.01253   1.000 25.50032  ? 81  TYR A CB    1 
ATOM   543  C  CG    . TYR A 1 70  ? -8.64627  -45.24182 3.86767   1.000 28.71143  ? 81  TYR A CG    1 
ATOM   544  C  CD1   . TYR A 1 70  ? -7.83318  -44.23719 4.37472   1.000 29.25189  ? 81  TYR A CD1   1 
ATOM   545  C  CD2   . TYR A 1 70  ? -10.00094 -45.21334 4.18140   1.000 30.33279  ? 81  TYR A CD2   1 
ATOM   546  C  CE1   . TYR A 1 70  ? -8.36369  -43.21758 5.15800   1.000 31.77024  ? 81  TYR A CE1   1 
ATOM   547  C  CE2   . TYR A 1 70  ? -10.54341 -44.20832 4.96392   1.000 28.30723  ? 81  TYR A CE2   1 
ATOM   548  C  CZ    . TYR A 1 70  ? -9.72454  -43.20958 5.44473   1.000 34.58747  ? 81  TYR A CZ    1 
ATOM   549  O  OH    . TYR A 1 70  ? -10.26980 -42.20908 6.21838   1.000 29.22283  ? 81  TYR A OH    1 
ATOM   550  N  N     . ASP A 1 71  ? -6.58799  -47.92875 0.65140   1.000 28.28489  ? 82  ASP A N     1 
ATOM   551  C  CA    . ASP A 1 71  ? -6.14690  -49.25367 0.21416   1.000 31.52019  ? 82  ASP A CA    1 
ATOM   552  C  C     . ASP A 1 71  ? -4.66691  -49.26805 -0.15387  1.000 28.70630  ? 82  ASP A C     1 
ATOM   553  O  O     . ASP A 1 71  ? -4.03386  -50.32522 -0.11850  1.000 33.23158  ? 82  ASP A O     1 
ATOM   554  C  CB    . ASP A 1 71  ? -6.97791  -49.72863 -0.97810  1.000 27.73443  ? 82  ASP A CB    1 
ATOM   555  C  CG    . ASP A 1 71  ? -8.42772  -50.02299 -0.61941  1.000 35.50739  ? 82  ASP A CG    1 
ATOM   556  O  OD1   . ASP A 1 71  ? -8.75383  -50.24624 0.56834   1.000 34.67107  ? 82  ASP A OD1   1 
ATOM   557  O  OD2   . ASP A 1 71  ? -9.25339  -50.04646 -1.55106  1.000 40.36331  ? 82  ASP A OD2   1 
ATOM   558  N  N     . LEU A 1 72  ? -4.10955  -48.12011 -0.53058  1.000 32.77078  ? 83  LEU A N     1 
ATOM   559  C  CA    . LEU A 1 72  ? -2.70480  -48.00525 -0.89876  1.000 29.17990  ? 83  LEU A CA    1 
ATOM   560  C  C     . LEU A 1 72  ? -1.85454  -47.37467 0.18826   1.000 33.22977  ? 83  LEU A C     1 
ATOM   561  O  O     . LEU A 1 72  ? -0.62970  -47.31966 0.03674   1.000 31.44465  ? 83  LEU A O     1 
ATOM   562  C  CB    . LEU A 1 72  ? -2.55725  -47.17019 -2.17902  1.000 28.08568  ? 83  LEU A CB    1 
ATOM   563  C  CG    . LEU A 1 72  ? -2.93534  -47.93618 -3.43803  1.000 34.36223  ? 83  LEU A CG    1 
ATOM   564  C  CD1   . LEU A 1 72  ? -2.87382  -47.02646 -4.63928  1.000 31.00931  ? 83  LEU A CD1   1 
ATOM   565  C  CD2   . LEU A 1 72  ? -1.99906  -49.13924 -3.61404  1.000 32.32297  ? 83  LEU A CD2   1 
ATOM   566  N  N     . ALA A 1 73  ? -2.46163  -46.87929 1.25939   1.000 25.07851  ? 84  ALA A N     1 
ATOM   567  C  CA    . ALA A 1 73  ? -1.71049  -46.19681 2.29324   1.000 27.00750  ? 84  ALA A CA    1 
ATOM   568  C  C     . ALA A 1 73  ? -1.38984  -47.16787 3.41977   1.000 31.43644  ? 84  ALA A C     1 
ATOM   569  O  O     . ALA A 1 73  ? -1.96941  -48.24485 3.53143   1.000 32.16822  ? 84  ALA A O     1 
ATOM   570  C  CB    . ALA A 1 73  ? -2.47512  -44.98246 2.82459   1.000 26.35460  ? 84  ALA A CB    1 
ATOM   571  N  N     . LEU A 1 74  ? -0.46816  -46.75580 4.27120   1.000 26.92727  ? 85  LEU A N     1 
ATOM   572  C  CA    . LEU A 1 74  ? 0.04313   -47.59353 5.34276   1.000 38.26853  ? 85  LEU A CA    1 
ATOM   573  C  C     . LEU A 1 74  ? 0.11813   -46.77738 6.62363   1.000 31.66638  ? 85  LEU A C     1 
ATOM   574  O  O     . LEU A 1 74  ? 0.87045   -45.79886 6.68776   1.000 31.05903  ? 85  LEU A O     1 
ATOM   575  C  CB    . LEU A 1 74  ? 1.42650   -48.14222 4.96914   1.000 31.69476  ? 85  LEU A CB    1 
ATOM   576  C  CG    . LEU A 1 74  ? 1.99712   -49.27199 5.81162   1.000 43.80952  ? 85  LEU A CG    1 
ATOM   577  C  CD1   . LEU A 1 74  ? 0.91471   -50.30609 6.12359   1.000 42.45145  ? 85  LEU A CD1   1 
ATOM   578  C  CD2   . LEU A 1 74  ? 3.15525   -49.91799 5.07649   1.000 46.16057  ? 85  LEU A CD2   1 
ATOM   579  N  N     . PRO A 1 75  ? -0.64084  -47.11997 7.65659   1.000 29.86814  ? 86  PRO A N     1 
ATOM   580  C  CA    . PRO A 1 75  ? -0.39628  -46.49302 8.95520   1.000 31.89627  ? 86  PRO A CA    1 
ATOM   581  C  C     . PRO A 1 75  ? 0.95647   -46.95195 9.48090   1.000 32.43180  ? 86  PRO A C     1 
ATOM   582  O  O     . PRO A 1 75  ? 1.31755   -48.12472 9.37820   1.000 36.23507  ? 86  PRO A O     1 
ATOM   583  C  CB    . PRO A 1 75  ? -1.55465  -47.00025 9.81883   1.000 37.84059  ? 86  PRO A CB    1 
ATOM   584  C  CG    . PRO A 1 75  ? -1.91432  -48.30692 9.20039   1.000 38.11244  ? 86  PRO A CG    1 
ATOM   585  C  CD    . PRO A 1 75  ? -1.68234  -48.15763 7.72630   1.000 32.25450  ? 86  PRO A CD    1 
ATOM   586  N  N     A MET A 1 76  ? 1.71834   -46.01628 10.02858  0.464 31.89108  ? 87  MET A N     1 
ATOM   587  N  N     B MET A 1 76  ? 1.71444   -46.00622 10.02727  0.536 31.86421  ? 87  MET A N     1 
ATOM   588  C  CA    A MET A 1 76  ? 3.03556   -46.35911 10.53408  0.464 34.84617  ? 87  MET A CA    1 
ATOM   589  C  CA    B MET A 1 76  ? 3.06168   -46.27519 10.50399  0.536 34.85457  ? 87  MET A CA    1 
ATOM   590  C  C     A MET A 1 76  ? 3.30474   -45.62801 11.83542  0.464 35.57651  ? 87  MET A C     1 
ATOM   591  C  C     B MET A 1 76  ? 3.26817   -45.62075 11.85955  0.536 35.56670  ? 87  MET A C     1 
ATOM   592  O  O     A MET A 1 76  ? 2.94993   -44.45621 11.99086  0.464 37.00511  ? 87  MET A O     1 
ATOM   593  O  O     B MET A 1 76  ? 2.84484   -44.48169 12.07515  0.536 36.99636  ? 87  MET A O     1 
ATOM   594  C  CB    A MET A 1 76  ? 4.12734   -46.04489 9.50473   0.464 36.00824  ? 87  MET A CB    1 
ATOM   595  C  CB    B MET A 1 76  ? 4.11849   -45.75213 9.52012   0.536 35.83889  ? 87  MET A CB    1 
ATOM   596  C  CG    A MET A 1 76  ? 4.13974   -47.02955 8.34989   0.464 32.48212  ? 87  MET A CG    1 
ATOM   597  C  CG    B MET A 1 76  ? 3.93581   -46.21151 8.08419   0.536 32.69582  ? 87  MET A CG    1 
ATOM   598  S  SD    A MET A 1 76  ? 5.48926   -46.77357 7.20605   0.464 43.13930  ? 87  MET A SD    1 
ATOM   599  S  SD    B MET A 1 76  ? 5.28410   -45.62428 7.04897   0.536 36.46230  ? 87  MET A SD    1 
ATOM   600  C  CE    A MET A 1 76  ? 6.89771   -47.27774 8.18852   0.464 28.41910  ? 87  MET A CE    1 
ATOM   601  C  CE    B MET A 1 76  ? 6.67739   -46.27308 7.98333   0.536 33.20876  ? 87  MET A CE    1 
ATOM   602  N  N     . GLY A 1 77  ? 3.92454   -46.34203 12.76798  1.000 34.45556  ? 88  GLY A N     1 
ATOM   603  C  CA    . GLY A 1 77  ? 4.30669   -45.77725 14.03720  1.000 39.29196  ? 88  GLY A CA    1 
ATOM   604  C  C     . GLY A 1 77  ? 5.55396   -44.92181 13.92851  1.000 41.48391  ? 88  GLY A C     1 
ATOM   605  O  O     . GLY A 1 77  ? 6.11110   -44.69743 12.85409  1.000 38.06688  ? 88  GLY A O     1 
ATOM   606  N  N     . VAL A 1 78  ? 6.00309   -44.43570 15.08293  1.000 38.11374  ? 89  VAL A N     1 
ATOM   607  C  CA    . VAL A 1 78  ? 7.10907   -43.49029 15.14980  1.000 35.48457  ? 89  VAL A CA    1 
ATOM   608  C  C     . VAL A 1 78  ? 7.99933   -43.84791 16.33029  1.000 39.26954  ? 89  VAL A C     1 
ATOM   609  O  O     . VAL A 1 78  ? 7.51864   -43.99737 17.45798  1.000 39.27276  ? 89  VAL A O     1 
ATOM   610  C  CB    . VAL A 1 78  ? 6.61924   -42.03726 15.28362  1.000 39.11611  ? 89  VAL A CB    1 
ATOM   611  C  CG1   . VAL A 1 78  ? 7.80696   -41.11313 15.40045  1.000 38.19839  ? 89  VAL A CG1   1 
ATOM   612  C  CG2   . VAL A 1 78  ? 5.78398   -41.64766 14.09685  1.000 46.78829  ? 89  VAL A CG2   1 
ATOM   613  N  N     . ASN A 1 79  ? 9.29345   -43.98980 16.07069  1.000 38.52681  ? 90  ASN A N     1 
ATOM   614  C  CA    . ASN A 1 79  ? 10.29565  -44.14390 17.11170  1.000 34.15472  ? 90  ASN A CA    1 
ATOM   615  C  C     . ASN A 1 79  ? 11.17131  -42.90813 17.13238  1.000 35.49795  ? 90  ASN A C     1 
ATOM   616  O  O     . ASN A 1 79  ? 11.61396  -42.43655 16.08018  1.000 29.81831  ? 90  ASN A O     1 
ATOM   617  C  CB    . ASN A 1 79  ? 11.17131  -45.37349 16.89096  1.000 33.11722  ? 90  ASN A CB    1 
ATOM   618  C  CG    . ASN A 1 79  ? 10.40793  -46.65789 17.02659  1.000 37.53367  ? 90  ASN A CG    1 
ATOM   619  O  OD1   . ASN A 1 79  ? 9.27256   -46.66822 17.50779  1.000 40.28065  ? 90  ASN A OD1   1 
ATOM   620  N  ND2   . ASN A 1 79  ? 11.02924  -47.76334 16.60863  1.000 38.71286  ? 90  ASN A ND2   1 
ATOM   621  N  N     . ILE A 1 80  ? 11.40137  -42.38303 18.32414  1.000 35.84069  ? 91  ILE A N     1 
ATOM   622  C  CA    . ILE A 1 80  ? 12.42608  -41.38089 18.55750  1.000 34.94271  ? 91  ILE A CA    1 
ATOM   623  C  C     . ILE A 1 80  ? 13.64829  -42.10120 19.10443  1.000 33.78680  ? 91  ILE A C     1 
ATOM   624  O  O     . ILE A 1 80  ? 13.54125  -42.86635 20.07041  1.000 37.27681  ? 91  ILE A O     1 
ATOM   625  C  CB    . ILE A 1 80  ? 11.92525  -40.29764 19.52697  1.000 41.22185  ? 91  ILE A CB    1 
ATOM   626  C  CG1   . ILE A 1 80  ? 10.62978  -39.69395 18.98868  1.000 36.28764  ? 91  ILE A CG1   1 
ATOM   627  C  CG2   . ILE A 1 80  ? 12.97601  -39.20626 19.72263  1.000 34.97432  ? 91  ILE A CG2   1 
ATOM   628  C  CD1   . ILE A 1 80  ? 9.87636   -38.89540 20.01469  1.000 42.76904  ? 91  ILE A CD1   1 
ATOM   629  N  N     . ALA A 1 81  ? 14.79832  -41.88820 18.47221  1.000 30.48290  ? 92  ALA A N     1 
ATOM   630  C  CA    . ALA A 1 81  ? 16.06529  -42.44402 18.92485  1.000 30.98539  ? 92  ALA A CA    1 
ATOM   631  C  C     . ALA A 1 81  ? 17.05004  -41.31541 19.19477  1.000 33.92181  ? 92  ALA A C     1 
ATOM   632  O  O     . ALA A 1 81  ? 16.89826  -40.20345 18.67714  1.000 33.99173  ? 92  ALA A O     1 
ATOM   633  C  CB    . ALA A 1 81  ? 16.65849  -43.40760 17.88781  1.000 27.17082  ? 92  ALA A CB    1 
ATOM   634  N  N     . ASP A 1 82  ? 18.07304  -41.60749 20.00558  1.000 30.41930  ? 93  ASP A N     1 
ATOM   635  C  CA    . ASP A 1 82  ? 19.17945  -40.67932 20.19047  1.000 37.58363  ? 93  ASP A CA    1 
ATOM   636  C  C     . ASP A 1 82  ? 20.32757  -41.06364 19.24504  1.000 30.84970  ? 93  ASP A C     1 
ATOM   637  O  O     . ASP A 1 82  ? 20.27731  -42.07493 18.54706  1.000 30.29944  ? 93  ASP A O     1 
ATOM   638  C  CB    . ASP A 1 82  ? 19.60920  -40.61286 21.66601  1.000 32.93319  ? 93  ASP A CB    1 
ATOM   639  C  CG    . ASP A 1 82  ? 20.29184  -41.89171 22.16501  1.000 38.82747  ? 93  ASP A CG    1 
ATOM   640  O  OD1   . ASP A 1 82  ? 20.59122  -42.79614 21.35339  1.000 36.86460  ? 93  ASP A OD1   1 
ATOM   641  O  OD2   . ASP A 1 82  ? 20.54103  -41.99392 23.39325  1.000 41.35065  ? 93  ASP A OD2   1 
ATOM   642  N  N     . GLU A 1 83  ? 21.38035  -40.24495 19.23406  1.000 31.61879  ? 94  GLU A N     1 
ATOM   643  C  CA    . GLU A 1 83  ? 22.50309  -40.43936 18.32264  1.000 31.44399  ? 94  GLU A CA    1 
ATOM   644  C  C     . GLU A 1 83  ? 23.29165  -41.71695 18.59953  1.000 35.59820  ? 94  GLU A C     1 
ATOM   645  O  O     . GLU A 1 83  ? 24.09602  -42.11694 17.75227  1.000 35.65188  ? 94  GLU A O     1 
ATOM   646  C  CB    . GLU A 1 83  ? 23.44028  -39.22358 18.37794  1.000 28.80964  ? 94  GLU A CB    1 
ATOM   647  C  CG    . GLU A 1 83  ? 24.41859  -39.20759 19.56825  1.000 34.40276  ? 94  GLU A CG    1 
ATOM   648  C  CD    . GLU A 1 83  ? 23.77798  -38.77433 20.88184  1.000 35.20698  ? 94  GLU A CD    1 
ATOM   649  O  OE1   . GLU A 1 83  ? 22.58767  -38.39888 20.87837  1.000 41.58072  ? 94  GLU A OE1   1 
ATOM   650  O  OE2   . GLU A 1 83  ? 24.47152  -38.80399 21.92088  1.000 39.74485  ? 94  GLU A OE2   1 
ATOM   651  N  N     . LYS A 1 84  ? 23.09917  -42.36014 19.74866  1.000 29.49975  ? 95  LYS A N     1 
ATOM   652  C  CA    . LYS A 1 84  ? 23.73526  -43.63923 20.03733  1.000 33.99009  ? 95  LYS A CA    1 
ATOM   653  C  C     . LYS A 1 84  ? 22.85396  -44.81964 19.66433  1.000 33.61214  ? 95  LYS A C     1 
ATOM   654  O  O     . LYS A 1 84  ? 23.21183  -45.96107 19.96393  1.000 37.96074  ? 95  LYS A O     1 
ATOM   655  C  CB    . LYS A 1 84  ? 24.11442  -43.73341 21.52077  1.000 31.04303  ? 95  LYS A CB    1 
ATOM   656  C  CG    . LYS A 1 84  ? 24.63810  -42.43177 22.10297  1.000 40.69086  ? 95  LYS A CG    1 
ATOM   657  C  CD    . LYS A 1 84  ? 25.04704  -42.59071 23.55952  1.000 42.00368  ? 95  LYS A CD    1 
ATOM   658  C  CE    . LYS A 1 84  ? 25.13049  -41.23728 24.24939  1.000 47.54011  ? 95  LYS A CE    1 
ATOM   659  N  NZ    . LYS A 1 84  ? 25.73696  -41.34694 25.61098  1.000 58.66938  ? 95  LYS A NZ    1 
ATOM   660  N  N     . GLY A 1 85  ? 21.70759  -44.57511 19.03836  1.000 32.70500  ? 96  GLY A N     1 
ATOM   661  C  CA    . GLY A 1 85  ? 20.82722  -45.66245 18.67841  1.000 35.27096  ? 96  GLY A CA    1 
ATOM   662  C  C     . GLY A 1 85  ? 19.91089  -46.15250 19.77915  1.000 37.44645  ? 96  GLY A C     1 
ATOM   663  O  O     . GLY A 1 85  ? 19.22037  -47.15676 19.58392  1.000 40.10698  ? 96  GLY A O     1 
ATOM   664  N  N     . ASN A 1 86  ? 19.87804  -45.48757 20.92802  1.000 37.73481  ? 97  ASN A N     1 
ATOM   665  C  CA    . ASN A 1 86  ? 18.90478  -45.83488 21.95399  1.000 38.03546  ? 97  ASN A CA    1 
ATOM   666  C  C     . ASN A 1 86  ? 17.51562  -45.39011 21.52331  1.000 36.94736  ? 97  ASN A C     1 
ATOM   667  O  O     . ASN A 1 86  ? 17.33122  -44.25891 21.06811  1.000 32.40285  ? 97  ASN A O     1 
ATOM   668  C  CB    . ASN A 1 86  ? 19.26928  -45.17221 23.27624  1.000 35.26886  ? 97  ASN A CB    1 
ATOM   669  C  CG    . ASN A 1 86  ? 20.62023  -45.59116 23.77451  1.000 39.32067  ? 97  ASN A CG    1 
ATOM   670  O  OD1   . ASN A 1 86  ? 20.91932  -46.78503 23.87609  1.000 40.92050  ? 97  ASN A OD1   1 
ATOM   671  N  ND2   . ASN A 1 86  ? 21.45731  -44.61028 24.08723  1.000 44.80938  ? 97  ASN A ND2   1 
ATOM   672  N  N     . ILE A 1 87  ? 16.53582  -46.27726 21.66961  1.000 38.12010  ? 98  ILE A N     1 
ATOM   673  C  CA    . ILE A 1 87  ? 15.14745  -45.92546 21.39402  1.000 39.65620  ? 98  ILE A CA    1 
ATOM   674  C  C     . ILE A 1 87  ? 14.60446  -45.18944 22.61644  1.000 37.82973  ? 98  ILE A C     1 
ATOM   675  O  O     . ILE A 1 87  ? 14.45027  -45.77745 23.68833  1.000 40.15766  ? 98  ILE A O     1 
ATOM   676  C  CB    . ILE A 1 87  ? 14.30235  -47.16114 21.06791  1.000 37.49228  ? 98  ILE A CB    1 
ATOM   677  C  CG1   . ILE A 1 87  ? 14.76007  -47.79654 19.75827  1.000 40.76179  ? 98  ILE A CG1   1 
ATOM   678  C  CG2   . ILE A 1 87  ? 12.83359  -46.76548 20.96620  1.000 38.06971  ? 98  ILE A CG2   1 
ATOM   679  C  CD1   . ILE A 1 87  ? 14.41222  -46.96198 18.53281  1.000 36.04336  ? 98  ILE A CD1   1 
ATOM   680  N  N     . LEU A 1 88  ? 14.33382  -43.89615 22.46130  1.000 36.27120  ? 99  LEU A N     1 
ATOM   681  C  CA    . LEU A 1 88  ? 13.78973  -43.09118 23.54733  1.000 42.36665  ? 99  LEU A CA    1 
ATOM   682  C  C     . LEU A 1 88  ? 12.27219  -43.17143 23.64297  1.000 43.27538  ? 99  LEU A C     1 
ATOM   683  O  O     . LEU A 1 88  ? 11.72633  -43.00269 24.73685  1.000 49.26409  ? 99  LEU A O     1 
ATOM   684  C  CB    . LEU A 1 88  ? 14.20108  -41.62461 23.38193  1.000 42.84420  ? 99  LEU A CB    1 
ATOM   685  C  CG    . LEU A 1 88  ? 15.69927  -41.33701 23.25723  1.000 41.90308  ? 99  LEU A CG    1 
ATOM   686  C  CD1   . LEU A 1 88  ? 15.96374  -39.83329 23.24716  1.000 34.07750  ? 99  LEU A CD1   1 
ATOM   687  C  CD2   . LEU A 1 88  ? 16.47806  -42.03379 24.36867  1.000 36.24528  ? 99  LEU A CD2   1 
ATOM   688  N  N     . SER A 1 89  ? 11.57927  -43.43436 22.53396  1.000 42.85760  ? 100 SER A N     1 
ATOM   689  C  CA    . SER A 1 89  ? 10.12112  -43.41842 22.51578  1.000 41.67861  ? 100 SER A CA    1 
ATOM   690  C  C     . SER A 1 89  ? 9.62825   -44.27268 21.35792  1.000 42.99653  ? 100 SER A C     1 
ATOM   691  O  O     . SER A 1 89  ? 10.15051  -44.15592 20.24793  1.000 41.55020  ? 100 SER A O     1 
ATOM   692  C  CB    . SER A 1 89  ? 9.60854   -41.98120 22.37847  1.000 42.30039  ? 100 SER A CB    1 
ATOM   693  O  OG    . SER A 1 89  ? 8.24000   -41.95442 22.04209  1.000 47.80818  ? 100 SER A OG    1 
ATOM   694  N  N     . THR A 1 90  ? 8.62612   -45.11858 21.61129  1.000 39.43551  ? 101 THR A N     1 
ATOM   695  C  CA    . THR A 1 90  ? 8.00376   -45.93722 20.57197  1.000 46.39305  ? 101 THR A CA    1 
ATOM   696  C  C     . THR A 1 90  ? 6.49653   -45.72889 20.61450  1.000 52.74922  ? 101 THR A C     1 
ATOM   697  O  O     . THR A 1 90  ? 5.85479   -46.05583 21.61745  1.000 52.57156  ? 101 THR A O     1 
ATOM   698  C  CB    . THR A 1 90  ? 8.32509   -47.42568 20.75071  1.000 47.17973  ? 101 THR A CB    1 
ATOM   699  O  OG1   . THR A 1 90  ? 9.72714   -47.64442 20.58359  1.000 51.97272  ? 101 THR A OG1   1 
ATOM   700  C  CG2   . THR A 1 90  ? 7.56778   -48.26775 19.72495  1.000 45.96192  ? 101 THR A CG2   1 
ATOM   701  N  N     . LYS A 1 91  ? 5.93042   -45.19578 19.53267  1.000 44.06901  ? 102 LYS A N     1 
ATOM   702  C  CA    . LYS A 1 91  ? 4.48555   -45.00015 19.41714  1.000 44.41661  ? 102 LYS A CA    1 
ATOM   703  C  C     . LYS A 1 91  ? 4.01746   -45.75387 18.18028  1.000 51.56922  ? 102 LYS A C     1 
ATOM   704  O  O     . LYS A 1 91  ? 4.23595   -45.30539 17.04924  1.000 46.42135  ? 102 LYS A O     1 
ATOM   705  C  CB    . LYS A 1 91  ? 4.11088   -43.51976 19.33050  1.000 46.79841  ? 102 LYS A CB    1 
ATOM   706  C  CG    . LYS A 1 91  ? 4.57174   -42.66403 20.51084  1.000 61.61861  ? 102 LYS A CG    1 
ATOM   707  C  CD    . LYS A 1 91  ? 4.20844   -43.28292 21.86501  1.000 65.84966  ? 102 LYS A CD    1 
ATOM   708  C  CE    . LYS A 1 91  ? 2.69650   -43.43352 22.05978  1.000 73.72330  ? 102 LYS A CE    1 
ATOM   709  N  NZ    . LYS A 1 91  ? 2.33983   -44.75895 22.67590  1.000 61.55721  ? 102 LYS A NZ    1 
ATOM   710  N  N     . ASN A 1 92  ? 3.38445   -46.89903 18.39128  1.000 43.47411  ? 103 ASN A N     1 
ATOM   711  C  CA    . ASN A 1 92  ? 2.76419   -47.62111 17.29473  1.000 48.61730  ? 103 ASN A CA    1 
ATOM   712  C  C     . ASN A 1 92  ? 1.36641   -47.06907 17.04574  1.000 48.22678  ? 103 ASN A C     1 
ATOM   713  O  O     . ASN A 1 92  ? 0.80935   -46.34286 17.87054  1.000 42.42099  ? 103 ASN A O     1 
ATOM   714  C  CB    . ASN A 1 92  ? 2.71365   -49.11113 17.60425  1.000 44.64368  ? 103 ASN A CB    1 
ATOM   715  C  CG    . ASN A 1 92  ? 4.08882   -49.69929 17.80507  1.000 50.01275  ? 103 ASN A CG    1 
ATOM   716  O  OD1   . ASN A 1 92  ? 4.99394   -49.47598 17.00124  1.000 46.62368  ? 103 ASN A OD1   1 
ATOM   717  N  ND2   . ASN A 1 92  ? 4.26246   -50.44069 18.89139  1.000 42.40097  ? 103 ASN A ND2   1 
ATOM   718  N  N     . VAL A 1 93  ? 0.81172   -47.39038 15.87948  1.000 49.54558  ? 104 VAL A N     1 
ATOM   719  C  CA    . VAL A 1 93  ? -0.52162  -46.90662 15.53030  1.000 46.68881  ? 104 VAL A CA    1 
ATOM   720  C  C     . VAL A 1 93  ? -1.55069  -47.80365 16.20346  1.000 52.24654  ? 104 VAL A C     1 
ATOM   721  O  O     . VAL A 1 93  ? -1.56981  -49.02030 15.98425  1.000 47.33101  ? 104 VAL A O     1 
ATOM   722  C  CB    . VAL A 1 93  ? -0.73609  -46.86744 14.01006  1.000 47.42959  ? 104 VAL A CB    1 
ATOM   723  C  CG1   . VAL A 1 93  ? -2.15497  -46.38535 13.68904  1.000 45.17915  ? 104 VAL A CG1   1 
ATOM   724  C  CG2   . VAL A 1 93  ? 0.27455   -45.95617 13.34839  1.000 44.32809  ? 104 VAL A CG2   1 
ATOM   725  N  N     . LYS A 1 94  ? -2.39551  -47.20710 17.03860  1.000 51.98825  ? 105 LYS A N     1 
ATOM   726  C  CA    . LYS A 1 94  ? -3.48851  -47.95716 17.63121  1.000 44.65111  ? 105 LYS A CA    1 
ATOM   727  C  C     . LYS A 1 94  ? -4.56131  -48.18931 16.56951  1.000 46.79848  ? 105 LYS A C     1 
ATOM   728  O  O     . LYS A 1 94  ? -4.77938  -47.32339 15.71247  1.000 42.19860  ? 105 LYS A O     1 
ATOM   729  C  CB    . LYS A 1 94  ? -4.06635  -47.19945 18.83041  1.000 54.55413  ? 105 LYS A CB    1 
ATOM   730  C  CG    . LYS A 1 94  ? -3.04307  -46.87187 19.92536  1.000 55.48034  ? 105 LYS A CG    1 
ATOM   731  C  CD    . LYS A 1 94  ? -3.40556  -45.59384 20.69118  1.000 68.21608  ? 105 LYS A CD    1 
ATOM   732  C  CE    . LYS A 1 94  ? -3.91532  -45.88205 22.10286  1.000 72.90736  ? 105 LYS A CE    1 
ATOM   733  N  NZ    . LYS A 1 94  ? -2.87225  -46.52011 22.96232  1.000 76.72628  ? 105 LYS A NZ    1 
ATOM   734  N  N     . PRO A 1 95  ? -5.24113  -49.34115 16.58983  1.000 42.19940  ? 106 PRO A N     1 
ATOM   735  C  CA    . PRO A 1 95  ? -6.16479  -49.65402 15.48397  1.000 38.63865  ? 106 PRO A CA    1 
ATOM   736  C  C     . PRO A 1 95  ? -7.22820  -48.59148 15.25290  1.000 41.51490  ? 106 PRO A C     1 
ATOM   737  O  O     . PRO A 1 95  ? -7.59687  -48.34515 14.09691  1.000 40.56888  ? 106 PRO A O     1 
ATOM   738  C  CB    . PRO A 1 95  ? -6.77780  -51.00304 15.90097  1.000 37.80314  ? 106 PRO A CB    1 
ATOM   739  C  CG    . PRO A 1 95  ? -6.51117  -51.12283 17.36090  1.000 40.22341  ? 106 PRO A CG    1 
ATOM   740  C  CD    . PRO A 1 95  ? -5.22007  -50.40058 17.61063  1.000 37.66344  ? 106 PRO A CD    1 
ATOM   741  N  N     . GLU A 1 96  ? -7.71129  -47.93393 16.31088  1.000 37.35422  ? 107 GLU A N     1 
ATOM   742  C  CA    . GLU A 1 96  ? -8.73858  -46.90650 16.16606  1.000 46.64067  ? 107 GLU A CA    1 
ATOM   743  C  C     . GLU A 1 96  ? -8.21998  -45.62745 15.51081  1.000 42.98217  ? 107 GLU A C     1 
ATOM   744  O  O     . GLU A 1 96  ? -9.02736  -44.75143 15.18227  1.000 43.43211  ? 107 GLU A O     1 
ATOM   745  C  CB    . GLU A 1 96  ? -9.35734  -46.57638 17.53193  1.000 45.14016  ? 107 GLU A CB    1 
ATOM   746  C  CG    . GLU A 1 96  ? -8.39637  -45.94792 18.54082  1.000 46.57063  ? 107 GLU A CG    1 
ATOM   747  C  CD    . GLU A 1 96  ? -7.73500  -46.96587 19.46569  1.000 54.91608  ? 107 GLU A CD    1 
ATOM   748  O  OE1   . GLU A 1 96  ? -7.51660  -48.12736 19.05157  1.000 48.85290  ? 107 GLU A OE1   1 
ATOM   749  O  OE2   . GLU A 1 96  ? -7.43051  -46.59489 20.61893  1.000 61.79405  ? 107 GLU A OE2   1 
ATOM   750  N  N     . ASN A 1 97  ? -6.90825  -45.50030 15.31912  1.000 37.14844  ? 108 ASN A N     1 
ATOM   751  C  CA    . ASN A 1 97  ? -6.29998  -44.35138 14.66301  1.000 37.87559  ? 108 ASN A CA    1 
ATOM   752  C  C     . ASN A 1 97  ? -5.66684  -44.72052 13.32644  1.000 39.63527  ? 108 ASN A C     1 
ATOM   753  O  O     . ASN A 1 97  ? -4.89685  -43.92981 12.76467  1.000 38.40398  ? 108 ASN A O     1 
ATOM   754  C  CB    . ASN A 1 97  ? -5.25605  -43.72470 15.59063  1.000 44.01381  ? 108 ASN A CB    1 
ATOM   755  C  CG    . ASN A 1 97  ? -5.85467  -43.25891 16.90894  1.000 42.26312  ? 108 ASN A CG    1 
ATOM   756  O  OD1   . ASN A 1 97  ? -6.98495  -42.77639 16.95101  1.000 45.87343  ? 108 ASN A OD1   1 
ATOM   757  N  ND2   . ASN A 1 97  ? -5.09882  -43.41093 17.99071  1.000 49.79200  ? 108 ASN A ND2   1 
ATOM   758  N  N     . ARG A 1 98  ? -5.96751  -45.90569 12.80383  1.000 35.36519  ? 109 ARG A N     1 
ATOM   759  C  CA    . ARG A 1 98  ? -5.34355  -46.35684 11.57094  1.000 41.09376  ? 109 ARG A CA    1 
ATOM   760  C  C     . ARG A 1 98  ? -5.79272  -45.56280 10.34526  1.000 39.28971  ? 109 ARG A C     1 
ATOM   761  O  O     . ARG A 1 98  ? -5.14324  -45.66305 9.29846   1.000 40.43343  ? 109 ARG A O     1 
ATOM   762  C  CB    . ARG A 1 98  ? -5.62938  -47.84333 11.37464  1.000 35.47128  ? 109 ARG A CB    1 
ATOM   763  C  CG    . ARG A 1 98  ? -7.05008  -48.15805 10.96930  1.000 37.62994  ? 109 ARG A CG    1 
ATOM   764  C  CD    . ARG A 1 98  ? -7.30634  -49.66161 11.06189  1.000 42.23667  ? 109 ARG A CD    1 
ATOM   765  N  NE    . ARG A 1 98  ? -8.62329  -50.03239 10.55132  1.000 39.45355  ? 109 ARG A NE    1 
ATOM   766  C  CZ    . ARG A 1 98  ? -9.73862  -49.98207 11.26336  1.000 44.18892  ? 109 ARG A CZ    1 
ATOM   767  N  NH1   . ARG A 1 98  ? -9.73899  -49.56140 12.51815  1.000 47.02555  ? 109 ARG A NH1   1 
ATOM   768  N  NH2   . ARG A 1 98  ? -10.88035 -50.36745 10.70586  1.000 46.41342  ? 109 ARG A NH2   1 
ATOM   769  N  N     . PHE A 1 99  ? -6.87504  -44.78760 10.44032  1.000 34.64177  ? 110 PHE A N     1 
ATOM   770  C  CA    . PHE A 1 99  ? -7.32758  -43.93033 9.35038   1.000 35.65914  ? 110 PHE A CA    1 
ATOM   771  C  C     . PHE A 1 99  ? -6.94865  -42.46625 9.54346   1.000 33.22350  ? 110 PHE A C     1 
ATOM   772  O  O     . PHE A 1 99  ? -7.32821  -41.63359 8.71600   1.000 33.00351  ? 110 PHE A O     1 
ATOM   773  C  CB    . PHE A 1 99  ? -8.85276  -44.03413 9.17699   1.000 37.68365  ? 110 PHE A CB    1 
ATOM   774  C  CG    . PHE A 1 99  ? -9.32550  -45.37688 8.66669   1.000 40.04730  ? 110 PHE A CG    1 
ATOM   775  C  CD1   . PHE A 1 99  ? -8.63533  -46.04216 7.66322   1.000 43.50555  ? 110 PHE A CD1   1 
ATOM   776  C  CD2   . PHE A 1 99  ? -10.46758 -45.97163 9.19313   1.000 45.57013  ? 110 PHE A CD2   1 
ATOM   777  C  CE1   . PHE A 1 99  ? -9.07986  -47.28558 7.19628   1.000 44.42438  ? 110 PHE A CE1   1 
ATOM   778  C  CE2   . PHE A 1 99  ? -10.91878 -47.21616 8.72991   1.000 45.06186  ? 110 PHE A CE2   1 
ATOM   779  C  CZ    . PHE A 1 99  ? -10.22851 -47.86663 7.73040   1.000 41.73449  ? 110 PHE A CZ    1 
ATOM   780  N  N     . ASP A 1 100 ? -6.21146  -42.12898 10.60690  1.000 35.16200  ? 111 ASP A N     1 
ATOM   781  C  CA    . ASP A 1 100 ? -5.93209  -40.72428 10.91059  1.000 34.24506  ? 111 ASP A CA    1 
ATOM   782  C  C     . ASP A 1 100 ? -5.05053  -40.07913 9.84910   1.000 38.34817  ? 111 ASP A C     1 
ATOM   783  O  O     . ASP A 1 100 ? -5.33994  -38.97182 9.38552   1.000 35.91946  ? 111 ASP A O     1 
ATOM   784  C  CB    . ASP A 1 100 ? -5.27714  -40.59876 12.28487  1.000 39.01833  ? 111 ASP A CB    1 
ATOM   785  C  CG    . ASP A 1 100 ? -6.26219  -40.81217 13.42349  1.000 43.51356  ? 111 ASP A CG    1 
ATOM   786  O  OD1   . ASP A 1 100 ? -7.47231  -40.96368 13.14866  1.000 39.22350  ? 111 ASP A OD1   1 
ATOM   787  O  OD2   . ASP A 1 100 ? -5.81451  -40.83218 14.59088  1.000 46.52758  ? 111 ASP A OD2   1 
ATOM   788  N  N     . ASN A 1 101 ? -3.95001  -40.74114 9.47271   1.000 38.35669  ? 112 ASN A N     1 
ATOM   789  C  CA    . ASN A 1 101 ? -3.04015  -40.22388 8.45209   1.000 33.52791  ? 112 ASN A CA    1 
ATOM   790  C  C     . ASN A 1 101 ? -2.07930  -41.31588 7.98980   1.000 35.41814  ? 112 ASN A C     1 
ATOM   791  O  O     . ASN A 1 101 ? -0.86344  -41.21144 8.20125   1.000 35.66747  ? 112 ASN A O     1 
ATOM   792  C  CB    . ASN A 1 101 ? -2.26123  -38.99598 8.96111   1.000 36.63141  ? 112 ASN A CB    1 
ATOM   793  C  CG    . ASN A 1 101 ? -1.48504  -39.25952 10.26261  1.000 37.96842  ? 112 ASN A CG    1 
ATOM   794  O  OD1   . ASN A 1 101 ? -1.98676  -39.88372 11.18796  1.000 41.94976  ? 112 ASN A OD1   1 
ATOM   795  N  ND2   . ASN A 1 101 ? -0.25958  -38.74926 10.33159  1.000 46.41806  ? 112 ASN A ND2   1 
ATOM   796  N  N     . PRO A 1 102 ? -2.57528  -42.37184 7.34929   1.000 32.10526  ? 113 PRO A N     1 
ATOM   797  C  CA    . PRO A 1 102 ? -1.66598  -43.40375 6.84891   1.000 28.63250  ? 113 PRO A CA    1 
ATOM   798  C  C     . PRO A 1 102 ? -0.82825  -42.86632 5.69420   1.000 33.51941  ? 113 PRO A C     1 
ATOM   799  O  O     . PRO A 1 102 ? -1.26242  -42.00637 4.92261   1.000 26.98615  ? 113 PRO A O     1 
ATOM   800  C  CB    . PRO A 1 102 ? -2.60839  -44.52977 6.40213   1.000 29.17981  ? 113 PRO A CB    1 
ATOM   801  C  CG    . PRO A 1 102 ? -3.89190  -43.82292 6.04979   1.000 35.47335  ? 113 PRO A CG    1 
ATOM   802  C  CD    . PRO A 1 102 ? -3.98094  -42.62775 6.97228   1.000 29.47156  ? 113 PRO A CD    1 
ATOM   803  N  N     . GLU A 1 103 ? 0.40504   -43.36445 5.61417   1.000 27.05293  ? 114 GLU A N     1 
ATOM   804  C  CA    . GLU A 1 103 ? 1.38611   -42.90007 4.63934   1.000 28.86921  ? 114 GLU A CA    1 
ATOM   805  C  C     . GLU A 1 103 ? 1.15565   -43.54942 3.28053   1.000 27.00279  ? 114 GLU A C     1 
ATOM   806  O  O     . GLU A 1 103 ? 0.92357   -44.75495 3.18672   1.000 25.70015  ? 114 GLU A O     1 
ATOM   807  C  CB    . GLU A 1 103 ? 2.80261   -43.23816 5.11760   1.000 28.58212  ? 114 GLU A CB    1 
ATOM   808  C  CG    . GLU A 1 103 ? 3.14577   -42.74434 6.51061   1.000 33.25552  ? 114 GLU A CG    1 
ATOM   809  C  CD    . GLU A 1 103 ? 3.28247   -41.24059 6.56613   1.000 37.97466  ? 114 GLU A CD    1 
ATOM   810  O  OE1   . GLU A 1 103 ? 3.66502   -40.63661 5.53813   1.000 39.25687  ? 114 GLU A OE1   1 
ATOM   811  O  OE2   . GLU A 1 103 ? 3.01074   -40.65725 7.63489   1.000 47.90117  ? 114 GLU A OE2   1 
ATOM   812  N  N     . ILE A 1 104 ? 1.26539   -42.75656 2.21762   1.000 27.00720  ? 115 ILE A N     1 
ATOM   813  C  CA    . ILE A 1 104 ? 1.12057   -43.26491 0.85855   1.000 25.91138  ? 115 ILE A CA    1 
ATOM   814  C  C     . ILE A 1 104 ? 2.30697   -42.79486 0.02690   1.000 23.65832  ? 115 ILE A C     1 
ATOM   815  O  O     . ILE A 1 104 ? 2.76270   -41.65573 0.16124   1.000 19.94469  ? 115 ILE A O     1 
ATOM   816  C  CB    . ILE A 1 104 ? -0.21957  -42.83220 0.21394   1.000 18.73509  ? 115 ILE A CB    1 
ATOM   817  C  CG1   . ILE A 1 104 ? -0.41765  -43.51060 -1.13898  1.000 20.49131  ? 115 ILE A CG1   1 
ATOM   818  C  CG2   . ILE A 1 104 ? -0.30080  -41.31176 0.05153   1.000 17.34216  ? 115 ILE A CG2   1 
ATOM   819  C  CD1   . ILE A 1 104 ? -1.87004  -43.35815 -1.67948  1.000 24.03537  ? 115 ILE A CD1   1 
ATOM   820  N  N     . ASN A 1 105 ? 2.82883   -43.69899 -0.79782  1.000 23.23500  ? 116 ASN A N     1 
ATOM   821  C  CA    . ASN A 1 105 ? 3.87459   -43.36599 -1.75252  1.000 25.89336  ? 116 ASN A CA    1 
ATOM   822  C  C     . ASN A 1 105 ? 3.37517   -42.32241 -2.75919  1.000 26.12099  ? 116 ASN A C     1 
ATOM   823  O  O     . ASN A 1 105 ? 2.20950   -42.33736 -3.17095  1.000 26.69287  ? 116 ASN A O     1 
ATOM   824  C  CB    . ASN A 1 105 ? 4.32686   -44.65294 -2.46283  1.000 20.79678  ? 116 ASN A CB    1 
ATOM   825  C  CG    . ASN A 1 105 ? 5.32520   -44.38879 -3.59120  1.000 27.80141  ? 116 ASN A CG    1 
ATOM   826  O  OD1   . ASN A 1 105 ? 4.93440   -44.17025 -4.73303  1.000 23.43314  ? 116 ASN A OD1   1 
ATOM   827  N  ND2   . ASN A 1 105 ? 6.61548   -44.43278 -3.27167  1.000 22.45580  ? 116 ASN A ND2   1 
ATOM   828  N  N     . ARG A 1 106 ? 4.26905   -41.40920 -3.15443  1.000 19.77503  ? 117 ARG A N     1 
ATOM   829  C  CA    . ARG A 1 106 ? 3.87298   -40.28620 -4.00075  1.000 21.99054  ? 117 ARG A CA    1 
ATOM   830  C  C     . ARG A 1 106 ? 3.51774   -40.73110 -5.41256  1.000 23.78485  ? 117 ARG A C     1 
ATOM   831  O  O     . ARG A 1 106 ? 2.64509   -40.12841 -6.04900  1.000 21.75928  ? 117 ARG A O     1 
ATOM   832  C  CB    . ARG A 1 106 ? 4.98727   -39.23809 -4.05765  1.000 20.12119  ? 117 ARG A CB    1 
ATOM   833  C  CG    . ARG A 1 106 ? 5.15591   -38.39608 -2.77406  1.000 22.65454  ? 117 ARG A CG    1 
ATOM   834  C  CD    . ARG A 1 106 ? 6.46605   -37.58668 -2.84924  1.000 22.05317  ? 117 ARG A CD    1 
ATOM   835  N  NE    . ARG A 1 106 ? 6.75274   -36.85283 -1.62470  1.000 20.73314  ? 117 ARG A NE    1 
ATOM   836  C  CZ    . ARG A 1 106 ? 6.33012   -35.61982 -1.36495  1.000 22.19668  ? 117 ARG A CZ    1 
ATOM   837  N  NH1   . ARG A 1 106 ? 5.55437   -34.95558 -2.21341  1.000 19.85299  ? 117 ARG A NH1   1 
ATOM   838  N  NH2   . ARG A 1 106 ? 6.70591   -35.03154 -0.23356  1.000 16.77559  ? 117 ARG A NH2   1 
ATOM   839  N  N     . ASN A 1 107 ? 4.18629   -41.76168 -5.93211  1.000 21.87353  ? 118 ASN A N     1 
ATOM   840  C  CA    . ASN A 1 107 ? 3.78550   -42.28442 -7.22954  1.000 22.82825  ? 118 ASN A CA    1 
ATOM   841  C  C     . ASN A 1 107 ? 2.43268   -42.99397 -7.13689  1.000 22.53245  ? 118 ASN A C     1 
ATOM   842  O  O     . ASN A 1 107 ? 1.62569   -42.92307 -8.06665  1.000 23.44872  ? 118 ASN A O     1 
ATOM   843  C  CB    . ASN A 1 107 ? 4.87326   -43.21151 -7.78308  1.000 26.38849  ? 118 ASN A CB    1 
ATOM   844  C  CG    . ASN A 1 107 ? 6.14145   -42.45309 -8.17817  1.000 30.17706  ? 118 ASN A CG    1 
ATOM   845  O  OD1   . ASN A 1 107 ? 6.26394   -41.97885 -9.30475  1.000 35.74170  ? 118 ASN A OD1   1 
ATOM   846  N  ND2   . ASN A 1 107 ? 7.08117   -42.34224 -7.25115  1.000 31.75031  ? 118 ASN A ND2   1 
ATOM   847  N  N     . ASP A 1 108 ? 2.15624   -43.67061 -6.02052  1.000 21.31258  ? 119 ASP A N     1 
ATOM   848  C  CA    . ASP A 1 108 ? 0.84297   -44.28915 -5.85038  1.000 21.48998  ? 119 ASP A CA    1 
ATOM   849  C  C     . ASP A 1 108 ? -0.25670  -43.23568 -5.83034  1.000 23.88344  ? 119 ASP A C     1 
ATOM   850  O  O     . ASP A 1 108 ? -1.28831  -43.39179 -6.49630  1.000 25.11294  ? 119 ASP A O     1 
ATOM   851  C  CB    . ASP A 1 108 ? 0.80646   -45.13436 -4.57488  1.000 19.58917  ? 119 ASP A CB    1 
ATOM   852  C  CG    . ASP A 1 108 ? 1.59024   -46.43873 -4.71353  1.000 23.22940  ? 119 ASP A CG    1 
ATOM   853  O  OD1   . ASP A 1 108 ? 1.74438   -46.93017 -5.85377  1.000 31.30551  ? 119 ASP A OD1   1 
ATOM   854  O  OD2   . ASP A 1 108 ? 2.03813   -46.97548 -3.68402  1.000 26.52247  ? 119 ASP A OD2   1 
ATOM   855  N  N     . LEU A 1 109 ? -0.03965  -42.14266 -5.09310  1.000 24.67170  ? 120 LEU A N     1 
ATOM   856  C  CA    . LEU A 1 109 ? -1.02694  -41.06474 -5.03029  1.000 26.63396  ? 120 LEU A CA    1 
ATOM   857  C  C     . LEU A 1 109 ? -1.25274  -40.42420 -6.40148  1.000 26.85991  ? 120 LEU A C     1 
ATOM   858  O  O     . LEU A 1 109 ? -2.39982  -40.17150 -6.79949  1.000 31.75395  ? 120 LEU A O     1 
ATOM   859  C  CB    . LEU A 1 109 ? -0.58241  -40.01148 -4.01288  1.000 19.90969  ? 120 LEU A CB    1 
ATOM   860  C  CG    . LEU A 1 109 ? -1.58339  -38.87438 -3.78870  1.000 26.60307  ? 120 LEU A CG    1 
ATOM   861  C  CD1   . LEU A 1 109 ? -2.88664  -39.43681 -3.24785  1.000 20.33309  ? 120 LEU A CD1   1 
ATOM   862  C  CD2   . LEU A 1 109 ? -0.99821  -37.83439 -2.84293  1.000 20.51760  ? 120 LEU A CD2   1 
ATOM   863  N  N     . ARG A 1 110 ? -0.17527  -40.14795 -7.13814  1.000 24.04947  ? 121 ARG A N     1 
ATOM   864  C  CA    . ARG A 1 110 ? -0.33265  -39.65724 -8.50762  1.000 23.64149  ? 121 ARG A CA    1 
ATOM   865  C  C     . ARG A 1 110 ? -1.17337  -40.61716 -9.34243  1.000 24.71117  ? 121 ARG A C     1 
ATOM   866  O  O     . ARG A 1 110 ? -2.09925  -40.18986 -10.04404 1.000 25.15254  ? 121 ARG A O     1 
ATOM   867  C  CB    . ARG A 1 110 ? 1.03864   -39.44344 -9.15669  1.000 20.43923  ? 121 ARG A CB    1 
ATOM   868  C  CG    . ARG A 1 110 ? 0.96120   -39.13737 -10.64303 1.000 23.44520  ? 121 ARG A CG    1 
ATOM   869  C  CD    . ARG A 1 110 ? 2.31784   -38.77084 -11.23976 1.000 24.53908  ? 121 ARG A CD    1 
ATOM   870  N  NE    . ARG A 1 110 ? 2.44765   -37.32363 -11.40423 1.000 30.23383  ? 121 ARG A NE    1 
ATOM   871  C  CZ    . ARG A 1 110 ? 3.47154   -36.71877 -11.99391 1.000 31.67027  ? 121 ARG A CZ    1 
ATOM   872  N  NH1   . ARG A 1 110 ? 4.49437   -37.40740 -12.48144 1.000 26.34313  ? 121 ARG A NH1   1 
ATOM   873  N  NH2   . ARG A 1 110 ? 3.45943   -35.39196 -12.11434 1.000 25.76423  ? 121 ARG A NH2   1 
ATOM   874  N  N     . ALA A 1 111 ? -0.89054  -41.92152 -9.24708  1.000 19.19774  ? 122 ALA A N     1 
ATOM   875  C  CA    . ALA A 1 111 ? -1.62846  -42.91029 -10.03323 1.000 27.70679  ? 122 ALA A CA    1 
ATOM   876  C  C     . ALA A 1 111 ? -3.11356  -42.93664 -9.67437  1.000 23.49259  ? 122 ALA A C     1 
ATOM   877  O  O     . ALA A 1 111 ? -3.96378  -43.12330 -10.55147 1.000 26.03498  ? 122 ALA A O     1 
ATOM   878  C  CB    . ALA A 1 111 ? -1.01366  -44.30368 -9.84768  1.000 22.91869  ? 122 ALA A CB    1 
ATOM   879  N  N     . ILE A 1 112 ? -3.44289  -42.79233 -8.38858  1.000 26.26209  ? 123 ILE A N     1 
ATOM   880  C  CA    . ILE A 1 112 ? -4.84587  -42.73531 -7.97295  1.000 28.63668  ? 123 ILE A CA    1 
ATOM   881  C  C     . ILE A 1 112 ? -5.54257  -41.55954 -8.64517  1.000 24.01211  ? 123 ILE A C     1 
ATOM   882  O  O     . ILE A 1 112 ? -6.64777  -41.68973 -9.18754  1.000 24.98628  ? 123 ILE A O     1 
ATOM   883  C  CB    . ILE A 1 112 ? -4.95199  -42.62607 -6.44115  1.000 27.95084  ? 123 ILE A CB    1 
ATOM   884  C  CG1   . ILE A 1 112 ? -4.55799  -43.93116 -5.75321  1.000 30.90271  ? 123 ILE A CG1   1 
ATOM   885  C  CG2   . ILE A 1 112 ? -6.35559  -42.24096 -6.02926  1.000 31.72901  ? 123 ILE A CG2   1 
ATOM   886  C  CD1   . ILE A 1 112 ? -4.53560  -43.76781 -4.23442  1.000 31.99998  ? 123 ILE A CD1   1 
ATOM   887  N  N     . LEU A 1 113 ? -4.89149  -40.39515 -8.62586  1.000 21.43226  ? 124 LEU A N     1 
ATOM   888  C  CA    . LEU A 1 113 ? -5.49974  -39.18859 -9.17289  1.000 24.18390  ? 124 LEU A CA    1 
ATOM   889  C  C     . LEU A 1 113 ? -5.60061  -39.25594 -10.69033 1.000 22.88127  ? 124 LEU A C     1 
ATOM   890  O  O     . LEU A 1 113 ? -6.65180  -38.93698 -11.25095 1.000 23.42410  ? 124 LEU A O     1 
ATOM   891  C  CB    . LEU A 1 113 ? -4.70694  -37.96683 -8.71643  1.000 17.57831  ? 124 LEU A CB    1 
ATOM   892  C  CG    . LEU A 1 113 ? -4.77668  -37.83434 -7.17948  1.000 27.66693  ? 124 LEU A CG    1 
ATOM   893  C  CD1   . LEU A 1 113 ? -3.71825  -36.89982 -6.62866  1.000 21.03966  ? 124 LEU A CD1   1 
ATOM   894  C  CD2   . LEU A 1 113 ? -6.15169  -37.35497 -6.74228  1.000 24.16460  ? 124 LEU A CD2   1 
ATOM   895  N  N     . LEU A 1 114 ? -4.53111  -39.69570 -11.36817 1.000 20.68423  ? 125 LEU A N     1 
ATOM   896  C  CA    . LEU A 1 114 ? -4.58002  -39.85480 -12.82102 1.000 24.57973  ? 125 LEU A CA    1 
ATOM   897  C  C     . LEU A 1 114 ? -5.66076  -40.84336 -13.23133 1.000 27.21302  ? 125 LEU A C     1 
ATOM   898  O  O     . LEU A 1 114 ? -6.41419  -40.58913 -14.17641 1.000 28.30039  ? 125 LEU A O     1 
ATOM   899  C  CB    . LEU A 1 114 ? -3.22542  -40.32144 -13.36877 1.000 25.32722  ? 125 LEU A CB    1 
ATOM   900  C  CG    . LEU A 1 114 ? -1.99839  -39.42140 -13.20201 1.000 32.34307  ? 125 LEU A CG    1 
ATOM   901  C  CD1   . LEU A 1 114 ? -0.74593  -40.12949 -13.70748 1.000 33.93287  ? 125 LEU A CD1   1 
ATOM   902  C  CD2   . LEU A 1 114 ? -2.19656  -38.10380 -13.92899 1.000 26.72345  ? 125 LEU A CD2   1 
ATOM   903  N  N     . ASN A 1 115 ? -5.72884  -41.99835 -12.55421 1.000 23.67873  ? 126 ASN A N     1 
ATOM   904  C  CA    . ASN A 1 115 ? -6.71669  -43.00657 -12.93034 1.000 25.17183  ? 126 ASN A CA    1 
ATOM   905  C  C     . ASN A 1 115 ? -8.13755  -42.47921 -12.78068 1.000 29.79151  ? 126 ASN A C     1 
ATOM   906  O  O     . ASN A 1 115 ? -9.04474  -42.92624 -13.48949 1.000 28.68120  ? 126 ASN A O     1 
ATOM   907  C  CB    . ASN A 1 115 ? -6.54953  -44.27731 -12.08935 1.000 27.74825  ? 126 ASN A CB    1 
ATOM   908  C  CG    . ASN A 1 115 ? -5.30844  -45.07100 -12.46162 1.000 35.21383  ? 126 ASN A CG    1 
ATOM   909  O  OD1   . ASN A 1 115 ? -4.67472  -44.81421 -13.48475 1.000 43.07111  ? 126 ASN A OD1   1 
ATOM   910  N  ND2   . ASN A 1 115 ? -4.95903  -46.04674 -11.63083 1.000 33.52689  ? 126 ASN A ND2   1 
ATOM   911  N  N     . SER A 1 116 ? -8.35265  -41.53683 -11.86468 1.000 22.49578  ? 127 SER A N     1 
ATOM   912  C  CA    . SER A 1 116 ? -9.68037  -40.97254 -11.67715 1.000 25.56146  ? 127 SER A CA    1 
ATOM   913  C  C     . SER A 1 116 ? -10.02277 -39.89943 -12.70486 1.000 24.05608  ? 127 SER A C     1 
ATOM   914  O  O     . SER A 1 116 ? -11.15858 -39.42768 -12.71933 1.000 26.45286  ? 127 SER A O     1 
ATOM   915  C  CB    . SER A 1 116 ? -9.79154  -40.37072 -10.28251 1.000 21.94942  ? 127 SER A CB    1 
ATOM   916  O  OG    . SER A 1 116 ? -9.10744  -39.13315 -10.26553 1.000 24.35647  ? 127 SER A OG    1 
ATOM   917  N  N     . LEU A 1 117 ? -9.08170  -39.48806 -13.54868 1.000 28.55012  ? 128 LEU A N     1 
ATOM   918  C  CA    . LEU A 1 117 ? -9.33162  -38.42753 -14.51612 1.000 26.67815  ? 128 LEU A CA    1 
ATOM   919  C  C     . LEU A 1 117 ? -9.70174  -39.02461 -15.86814 1.000 32.58887  ? 128 LEU A C     1 
ATOM   920  O  O     . LEU A 1 117 ? -9.27449  -40.12932 -16.21186 1.000 29.01094  ? 128 LEU A O     1 
ATOM   921  C  CB    . LEU A 1 117 ? -8.10184  -37.52902 -14.67370 1.000 24.64496  ? 128 LEU A CB    1 
ATOM   922  C  CG    . LEU A 1 117 ? -7.69608  -36.69920 -13.45405 1.000 22.31746  ? 128 LEU A CG    1 
ATOM   923  C  CD1   . LEU A 1 117 ? -6.47676  -35.88313 -13.79997 1.000 18.91592  ? 128 LEU A CD1   1 
ATOM   924  C  CD2   . LEU A 1 117 ? -8.84493  -35.78306 -13.04059 1.000 20.15968  ? 128 LEU A CD2   1 
ATOM   925  N  N     A GLU A 1 118 ? -10.50862 -38.29030 -16.63300 0.561 28.97357  ? 129 GLU A N     1 
ATOM   926  N  N     B GLU A 1 118 ? -10.50877 -38.28369 -16.62904 0.439 28.98442  ? 129 GLU A N     1 
ATOM   927  C  CA    A GLU A 1 118 ? -10.80226 -38.72401 -17.99051 0.561 30.79693  ? 129 GLU A CA    1 
ATOM   928  C  CA    B GLU A 1 118 ? -10.78162 -38.66716 -18.00617 0.439 30.78957  ? 129 GLU A CA    1 
ATOM   929  C  C     A GLU A 1 118 ? -9.51897  -38.72681 -18.81056 0.561 30.07242  ? 129 GLU A C     1 
ATOM   930  C  C     B GLU A 1 118 ? -9.47614  -38.76305 -18.78081 0.439 30.09579  ? 129 GLU A C     1 
ATOM   931  O  O     A GLU A 1 118 ? -8.57683  -37.98183 -18.52964 0.561 32.65146  ? 129 GLU A O     1 
ATOM   932  O  O     B GLU A 1 118 ? -8.48311  -38.10935 -18.44841 0.439 32.66941  ? 129 GLU A O     1 
ATOM   933  C  CB    A GLU A 1 118 ? -11.84961 -37.81539 -18.64069 0.561 32.11500  ? 129 GLU A CB    1 
ATOM   934  C  CB    B GLU A 1 118 ? -11.70640 -37.65354 -18.68436 0.439 32.05105  ? 129 GLU A CB    1 
ATOM   935  C  CG    A GLU A 1 118 ? -13.21582 -37.82420 -17.95276 0.561 36.11997  ? 129 GLU A CG    1 
ATOM   936  C  CG    B GLU A 1 118 ? -13.16638 -37.73643 -18.27574 0.439 35.95686  ? 129 GLU A CG    1 
ATOM   937  C  CD    A GLU A 1 118 ? -13.98731 -39.11302 -18.16618 0.561 34.29784  ? 129 GLU A CD    1 
ATOM   938  C  CD    B GLU A 1 118 ? -13.99351 -36.61131 -18.87285 0.439 35.03320  ? 129 GLU A CD    1 
ATOM   939  O  OE1   A GLU A 1 118 ? -13.93609 -39.66171 -19.28594 0.561 38.21162  ? 129 GLU A OE1   1 
ATOM   940  O  OE1   B GLU A 1 118 ? -13.64170 -36.12397 -19.96853 0.439 35.07086  ? 129 GLU A OE1   1 
ATOM   941  O  OE2   A GLU A 1 118 ? -14.64641 -39.57895 -17.21087 0.561 39.33363  ? 129 GLU A OE2   1 
ATOM   942  O  OE2   B GLU A 1 118 ? -14.98377 -36.20191 -18.23759 0.439 33.34730  ? 129 GLU A OE2   1 
ATOM   943  N  N     . ASN A 1 119 ? -9.47659  -39.59207 -19.82155 1.000 32.79263  ? 130 ASN A N     1 
ATOM   944  C  CA    . ASN A 1 119 ? -8.28460  -39.71737 -20.64729 1.000 27.64840  ? 130 ASN A CA    1 
ATOM   945  C  C     . ASN A 1 119 ? -7.92402  -38.36352 -21.25060 1.000 29.88404  ? 130 ASN A C     1 
ATOM   946  O  O     . ASN A 1 119 ? -8.80216  -37.56212 -21.58330 1.000 32.20006  ? 130 ASN A O     1 
ATOM   947  C  CB    . ASN A 1 119 ? -8.50751  -40.75025 -21.74772 1.000 38.87340  ? 130 ASN A CB    1 
ATOM   948  C  CG    . ASN A 1 119 ? -8.61665  -42.17487 -21.21226 1.000 38.93345  ? 130 ASN A CG    1 
ATOM   949  O  OD1   . ASN A 1 119 ? -8.12552  -42.49724 -20.12245 1.000 36.52583  ? 130 ASN A OD1   1 
ATOM   950  N  ND2   . ASN A 1 119 ? -9.23486  -43.04215 -22.00083 1.000 36.50706  ? 130 ASN A ND2   1 
ATOM   951  N  N     . ASP A 1 120 ? -6.62167  -38.08345 -21.32129 1.000 26.99687  ? 131 ASP A N     1 
ATOM   952  C  CA    . ASP A 1 120 ? -6.09901  -36.85820 -21.93008 1.000 33.42925  ? 131 ASP A CA    1 
ATOM   953  C  C     . ASP A 1 120 ? -6.48323  -35.60368 -21.14835 1.000 31.23344  ? 131 ASP A C     1 
ATOM   954  O  O     . ASP A 1 120 ? -6.58031  -34.51666 -21.72036 1.000 33.79099  ? 131 ASP A O     1 
ATOM   955  C  CB    . ASP A 1 120 ? -6.54723  -36.72803 -23.38951 1.000 32.86043  ? 131 ASP A CB    1 
ATOM   956  C  CG    . ASP A 1 120 ? -6.05220  -37.87544 -24.25055 1.000 44.89905  ? 131 ASP A CG    1 
ATOM   957  O  OD1   . ASP A 1 120 ? -4.87649  -38.28603 -24.06790 1.000 45.70481  ? 131 ASP A OD1   1 
ATOM   958  O  OD2   . ASP A 1 120 ? -6.83861  -38.36851 -25.09228 1.000 43.68275  ? 131 ASP A OD2   1 
ATOM   959  N  N     . THR A 1 121 ? -6.73057  -35.73425 -19.84645 1.000 22.45339  ? 132 THR A N     1 
ATOM   960  C  CA    . THR A 1 121 ? -6.90225  -34.53971 -19.03194 1.000 24.67967  ? 132 THR A CA    1 
ATOM   961  C  C     . THR A 1 121 ? -5.55886  -33.87198 -18.78745 1.000 25.77803  ? 132 THR A C     1 
ATOM   962  O  O     . THR A 1 121 ? -5.43796  -32.64828 -18.90124 1.000 23.19148  ? 132 THR A O     1 
ATOM   963  C  CB    . THR A 1 121 ? -7.57523  -34.88635 -17.69982 1.000 22.40567  ? 132 THR A CB    1 
ATOM   964  O  OG1   . THR A 1 121 ? -8.86451  -35.45518 -17.95158 1.000 23.62798  ? 132 THR A OG1   1 
ATOM   965  C  CG2   . THR A 1 121 ? -7.74459  -33.64360 -16.83773 1.000 17.83460  ? 132 THR A CG2   1 
ATOM   966  N  N     . VAL A 1 122 ? -4.54541  -34.66865 -18.46782 1.000 23.61825  ? 133 VAL A N     1 
ATOM   967  C  CA    . VAL A 1 122 ? -3.17956  -34.19576 -18.28465 1.000 23.15572  ? 133 VAL A CA    1 
ATOM   968  C  C     . VAL A 1 122 ? -2.47775  -34.19629 -19.63708 1.000 24.40792  ? 133 VAL A C     1 
ATOM   969  O  O     . VAL A 1 122 ? -2.50783  -35.20026 -20.35049 1.000 26.50533  ? 133 VAL A O     1 
ATOM   970  C  CB    . VAL A 1 122 ? -2.43401  -35.08177 -17.26838 1.000 26.20723  ? 133 VAL A CB    1 
ATOM   971  C  CG1   . VAL A 1 122 ? -1.01500  -34.57379 -17.03213 1.000 20.31380  ? 133 VAL A CG1   1 
ATOM   972  C  CG2   . VAL A 1 122 ? -3.21103  -35.13618 -15.93431 1.000 20.42827  ? 133 VAL A CG2   1 
ATOM   973  N  N     . ILE A 1 123 ? -1.86752  -33.06648 -20.00405 1.000 19.24336  ? 134 ILE A N     1 
ATOM   974  C  CA    . ILE A 1 123 ? -1.01674  -32.96545 -21.19014 1.000 20.31318  ? 134 ILE A CA    1 
ATOM   975  C  C     . ILE A 1 123 ? 0.42400   -32.97248 -20.70380 1.000 22.66462  ? 134 ILE A C     1 
ATOM   976  O  O     . ILE A 1 123 ? 0.87666   -32.01311 -20.06815 1.000 23.48450  ? 134 ILE A O     1 
ATOM   977  C  CB    . ILE A 1 123 ? -1.30027  -31.70014 -22.01431 1.000 24.40513  ? 134 ILE A CB    1 
ATOM   978  C  CG1   . ILE A 1 123 ? -2.79216  -31.34614 -22.01025 1.000 21.47472  ? 134 ILE A CG1   1 
ATOM   979  C  CG2   . ILE A 1 123 ? -0.75769  -31.87533 -23.46068 1.000 18.17200  ? 134 ILE A CG2   1 
ATOM   980  C  CD1   . ILE A 1 123 ? -3.63554  -32.32144 -22.78144 1.000 24.84845  ? 134 ILE A CD1   1 
ATOM   981  N  N     . TRP A 1 124 ? 1.13882   -34.05308 -20.98245 1.000 21.86771  ? 135 TRP A N     1 
ATOM   982  C  CA    . TRP A 1 124 ? 2.50374   -34.23443 -20.50829 1.000 26.06817  ? 135 TRP A CA    1 
ATOM   983  C  C     . TRP A 1 124 ? 3.48994   -33.44709 -21.37079 1.000 31.04110  ? 135 TRP A C     1 
ATOM   984  O  O     . TRP A 1 124 ? 3.17063   -33.00589 -22.48197 1.000 26.34812  ? 135 TRP A O     1 
ATOM   985  C  CB    . TRP A 1 124 ? 2.85535   -35.72431 -20.50852 1.000 27.11739  ? 135 TRP A CB    1 
ATOM   986  C  CG    . TRP A 1 124 ? 1.92119   -36.49564 -19.61146 1.000 31.13992  ? 135 TRP A CG    1 
ATOM   987  C  CD1   . TRP A 1 124 ? 0.73204   -37.08727 -19.95821 1.000 27.06033  ? 135 TRP A CD1   1 
ATOM   988  C  CD2   . TRP A 1 124 ? 2.08583   -36.71728 -18.20898 1.000 25.61351  ? 135 TRP A CD2   1 
ATOM   989  N  NE1   . TRP A 1 124 ? 0.15253   -37.66252 -18.85344 1.000 26.97561  ? 135 TRP A NE1   1 
ATOM   990  C  CE2   . TRP A 1 124 ? 0.96395   -37.44751 -17.76645 1.000 24.86598  ? 135 TRP A CE2   1 
ATOM   991  C  CE3   . TRP A 1 124 ? 3.07953   -36.36721 -17.28249 1.000 28.34931  ? 135 TRP A CE3   1 
ATOM   992  C  CZ2   . TRP A 1 124 ? 0.80943   -37.83812 -16.44279 1.000 26.86937  ? 135 TRP A CZ2   1 
ATOM   993  C  CZ3   . TRP A 1 124 ? 2.92803   -36.75838 -15.96578 1.000 26.84652  ? 135 TRP A CZ3   1 
ATOM   994  C  CH2   . TRP A 1 124 ? 1.79960   -37.48799 -15.55778 1.000 29.10459  ? 135 TRP A CH2   1 
ATOM   995  N  N     . ASP A 1 125 ? 4.70443   -33.26780 -20.83858 1.000 25.26665  ? 136 ASP A N     1 
ATOM   996  C  CA    . ASP A 1 125 ? 5.77308   -32.56206 -21.55172 1.000 26.58158  ? 136 ASP A CA    1 
ATOM   997  C  C     . ASP A 1 125 ? 5.31679   -31.15441 -21.93824 1.000 24.42146  ? 136 ASP A C     1 
ATOM   998  O  O     . ASP A 1 125 ? 5.48168   -30.70688 -23.07729 1.000 22.83850  ? 136 ASP A O     1 
ATOM   999  C  CB    . ASP A 1 125 ? 6.23269   -33.35332 -22.78317 1.000 28.42365  ? 136 ASP A CB    1 
ATOM   1000 C  CG    . ASP A 1 125 ? 7.52272   -32.80679 -23.38552 1.000 33.24219  ? 136 ASP A CG    1 
ATOM   1001 O  OD1   . ASP A 1 125 ? 8.16464   -31.95595 -22.73623 1.000 34.68189  ? 136 ASP A OD1   1 
ATOM   1002 O  OD2   . ASP A 1 125 ? 7.89179   -33.21787 -24.50679 1.000 34.80817  ? 136 ASP A OD2   1 
ATOM   1003 N  N     . ARG A 1 126 ? 4.68121   -30.47400 -20.98043 1.000 23.48456  ? 137 ARG A N     1 
ATOM   1004 C  CA    . ARG A 1 126 ? 4.18014   -29.11558 -21.16004 1.000 23.94043  ? 137 ARG A CA    1 
ATOM   1005 C  C     . ARG A 1 126 ? 4.73613   -28.28889 -20.00931 1.000 21.68669  ? 137 ARG A C     1 
ATOM   1006 O  O     . ARG A 1 126 ? 4.16348   -28.27849 -18.91831 1.000 25.72758  ? 137 ARG A O     1 
ATOM   1007 C  CB    . ARG A 1 126 ? 2.65630   -29.09088 -21.19505 1.000 25.30721  ? 137 ARG A CB    1 
ATOM   1008 C  CG    . ARG A 1 126 ? 2.05188   -29.64538 -22.48934 1.000 24.95194  ? 137 ARG A CG    1 
ATOM   1009 C  CD    . ARG A 1 126 ? 2.47894   -28.80823 -23.69310 1.000 24.10425  ? 137 ARG A CD    1 
ATOM   1010 N  NE    . ARG A 1 126 ? 1.89456   -29.29567 -24.93669 1.000 27.14826  ? 137 ARG A NE    1 
ATOM   1011 C  CZ    . ARG A 1 126 ? 2.35653   -30.33512 -25.62094 1.000 33.90500  ? 137 ARG A CZ    1 
ATOM   1012 N  NH1   . ARG A 1 126 ? 3.41401   -31.02476 -25.21046 1.000 27.98767  ? 137 ARG A NH1   1 
ATOM   1013 N  NH2   . ARG A 1 126 ? 1.74713   -30.68906 -26.74759 1.000 30.96578  ? 137 ARG A NH2   1 
ATOM   1014 N  N     . LYS A 1 127 ? 5.86682   -27.62740 -20.23934 1.000 22.10385  ? 138 LYS A N     1 
ATOM   1015 C  CA    . LYS A 1 127 ? 6.45182   -26.71070 -19.26111 1.000 23.72293  ? 138 LYS A CA    1 
ATOM   1016 C  C     . LYS A 1 127 ? 5.98051   -25.30063 -19.61004 1.000 24.79672  ? 138 LYS A C     1 
ATOM   1017 O  O     . LYS A 1 127 ? 6.41007   -24.72488 -20.61944 1.000 24.14602  ? 138 LYS A O     1 
ATOM   1018 C  CB    . LYS A 1 127 ? 7.97751   -26.79871 -19.26286 1.000 24.21212  ? 138 LYS A CB    1 
ATOM   1019 C  CG    . LYS A 1 127 ? 8.66522   -25.88729 -18.22442 1.000 25.34672  ? 138 LYS A CG    1 
ATOM   1020 C  CD    . LYS A 1 127 ? 10.11526  -25.68942 -18.57708 1.000 30.83107  ? 138 LYS A CD    1 
ATOM   1021 C  CE    . LYS A 1 127 ? 10.98009  -25.17115 -17.41508 1.000 49.55538  ? 138 LYS A CE    1 
ATOM   1022 N  NZ    . LYS A 1 127 ? 10.76240  -23.72947 -17.01980 1.000 52.15197  ? 138 LYS A NZ    1 
ATOM   1023 N  N     . LEU A 1 128 ? 5.07068   -24.76379 -18.80450 1.000 20.03618  ? 139 LEU A N     1 
ATOM   1024 C  CA    . LEU A 1 128 ? 4.60885   -23.39964 -19.02569 1.000 26.27423  ? 139 LEU A CA    1 
ATOM   1025 C  C     . LEU A 1 128 ? 5.72871   -22.40254 -18.72255 1.000 26.02533  ? 139 LEU A C     1 
ATOM   1026 O  O     . LEU A 1 128 ? 6.35094   -22.44367 -17.64711 1.000 22.07748  ? 139 LEU A O     1 
ATOM   1027 C  CB    . LEU A 1 128 ? 3.38997   -23.11326 -18.15238 1.000 20.03341  ? 139 LEU A CB    1 
ATOM   1028 C  CG    . LEU A 1 128 ? 2.79655   -21.72363 -18.36436 1.000 24.88379  ? 139 LEU A CG    1 
ATOM   1029 C  CD1   . LEU A 1 128 ? 1.92951   -21.70624 -19.63365 1.000 20.41969  ? 139 LEU A CD1   1 
ATOM   1030 C  CD2   . LEU A 1 128 ? 2.00468   -21.27940 -17.14517 1.000 17.89729  ? 139 LEU A CD2   1 
ATOM   1031 N  N     . VAL A 1 129 ? 6.01642   -21.53054 -19.68530 1.000 23.76109  ? 140 VAL A N     1 
ATOM   1032 C  CA    . VAL A 1 129 ? 7.01154   -20.48687 -19.48582 1.000 28.04256  ? 140 VAL A CA    1 
ATOM   1033 C  C     . VAL A 1 129 ? 6.40932   -19.08249 -19.43494 1.000 22.96595  ? 140 VAL A C     1 
ATOM   1034 O  O     . VAL A 1 129 ? 7.02239   -18.19341 -18.82540 1.000 24.86246  ? 140 VAL A O     1 
ATOM   1035 C  CB    . VAL A 1 129 ? 8.14167   -20.55335 -20.53940 1.000 30.66018  ? 140 VAL A CB    1 
ATOM   1036 C  CG1   . VAL A 1 129 ? 8.75857   -21.93897 -20.56402 1.000 27.67395  ? 140 VAL A CG1   1 
ATOM   1037 C  CG2   . VAL A 1 129 ? 7.65436   -20.16486 -21.92007 1.000 27.34874  ? 140 VAL A CG2   1 
ATOM   1038 N  N     . MET A 1 130 ? 5.23008   -18.85151 -20.00902 1.000 22.79824  ? 141 MET A N     1 
ATOM   1039 C  CA    . MET A 1 130 ? 4.69091   -17.49717 -19.94937 1.000 25.09615  ? 141 MET A CA    1 
ATOM   1040 C  C     . MET A 1 130 ? 3.17437   -17.50423 -20.09419 1.000 26.28425  ? 141 MET A C     1 
ATOM   1041 O  O     . MET A 1 130 ? 2.60053   -18.36207 -20.77350 1.000 25.94591  ? 141 MET A O     1 
ATOM   1042 C  CB    . MET A 1 130 ? 5.30375   -16.60469 -21.03334 1.000 31.83144  ? 141 MET A CB    1 
ATOM   1043 C  CG    . MET A 1 130 ? 4.28859   -15.63062 -21.59901 1.000 41.95680  ? 141 MET A CG    1 
ATOM   1044 S  SD    . MET A 1 130 ? 4.87114   -14.76946 -23.01647 1.000 61.41486  ? 141 MET A SD    1 
ATOM   1045 C  CE    . MET A 1 130 ? 6.17631   -13.95380 -22.16087 1.000 55.19527  ? 141 MET A CE    1 
ATOM   1046 N  N     . LEU A 1 131 ? 2.53871   -16.52597 -19.45085 1.000 24.34985  ? 142 LEU A N     1 
ATOM   1047 C  CA    . LEU A 1 131 ? 1.11362   -16.27292 -19.57559 1.000 24.90097  ? 142 LEU A CA    1 
ATOM   1048 C  C     . LEU A 1 131 ? 0.90054   -14.91386 -20.21618 1.000 24.55014  ? 142 LEU A C     1 
ATOM   1049 O  O     . LEU A 1 131 ? 1.66622   -13.97984 -19.98483 1.000 31.78698  ? 142 LEU A O     1 
ATOM   1050 C  CB    . LEU A 1 131 ? 0.41764   -16.29803 -18.21811 1.000 21.83205  ? 142 LEU A CB    1 
ATOM   1051 C  CG    . LEU A 1 131 ? 0.36887   -17.67403 -17.57822 1.000 23.76499  ? 142 LEU A CG    1 
ATOM   1052 C  CD1   . LEU A 1 131 ? 0.02173   -17.55203 -16.10680 1.000 27.79689  ? 142 LEU A CD1   1 
ATOM   1053 C  CD2   . LEU A 1 131 ? -0.64684  -18.53983 -18.29957 1.000 23.43463  ? 142 LEU A CD2   1 
ATOM   1054 N  N     . GLU A 1 132 ? -0.14527  -14.80728 -21.01490 1.000 27.30804  ? 143 GLU A N     1 
ATOM   1055 C  CA    . GLU A 1 132 ? -0.50979  -13.50957 -21.54929 1.000 27.12438  ? 143 GLU A CA    1 
ATOM   1056 C  C     . GLU A 1 132 ? -2.02622  -13.35771 -21.54032 1.000 29.75068  ? 143 GLU A C     1 
ATOM   1057 O  O     . GLU A 1 132 ? -2.73564  -14.16609 -22.15423 1.000 27.36785  ? 143 GLU A O     1 
ATOM   1058 C  CB    . GLU A 1 132 ? 0.05116   -13.32644 -22.96191 1.000 32.16170  ? 143 GLU A CB    1 
ATOM   1059 C  CG    . GLU A 1 132 ? -0.34570  -11.99084 -23.59843 1.000 35.97993  ? 143 GLU A CG    1 
ATOM   1060 C  CD    . GLU A 1 132 ? 0.43072   -11.67677 -24.87869 1.000 50.98968  ? 143 GLU A CD    1 
ATOM   1061 O  OE1   . GLU A 1 132 ? 1.39264   -12.41005 -25.20607 1.000 54.72392  ? 143 GLU A OE1   1 
ATOM   1062 O  OE2   . GLU A 1 132 ? 0.07808   -10.68679 -25.55715 1.000 56.23407  ? 143 GLU A OE2   1 
ATOM   1063 N  N     . PRO A 1 133 ? -2.55920  -12.33673 -20.86238 1.000 32.44482  ? 144 PRO A N     1 
ATOM   1064 C  CA    . PRO A 1 133 ? -4.01654  -12.13231 -20.84468 1.000 28.49108  ? 144 PRO A CA    1 
ATOM   1065 C  C     . PRO A 1 133 ? -4.49732  -11.51215 -22.15126 1.000 28.24034  ? 144 PRO A C     1 
ATOM   1066 O  O     . PRO A 1 133 ? -3.94519  -10.51825 -22.61644 1.000 29.83616  ? 144 PRO A O     1 
ATOM   1067 C  CB    . PRO A 1 133 ? -4.22290  -11.17395 -19.66691 1.000 31.55093  ? 144 PRO A CB    1 
ATOM   1068 C  CG    . PRO A 1 133 ? -2.92240  -10.32581 -19.66369 1.000 24.15320  ? 144 PRO A CG    1 
ATOM   1069 C  CD    . PRO A 1 133 ? -1.83416  -11.30786 -20.08180 1.000 30.95076  ? 144 PRO A CD    1 
ATOM   1070 N  N     . GLY A 1 134 ? -5.53153  -12.10490 -22.74295 1.000 26.49679  ? 145 GLY A N     1 
ATOM   1071 C  CA    . GLY A 1 134 ? -6.18824  -11.54986 -23.90633 1.000 27.56478  ? 145 GLY A CA    1 
ATOM   1072 C  C     . GLY A 1 134 ? -7.43137  -10.77196 -23.52675 1.000 28.86519  ? 145 GLY A C     1 
ATOM   1073 O  O     . GLY A 1 134 ? -7.62652  -10.38840 -22.36533 1.000 28.48562  ? 145 GLY A O     1 
ATOM   1074 N  N     . LYS A 1 135 ? -8.29256  -10.54545 -24.52491 1.000 25.80834  ? 146 LYS A N     1 
ATOM   1075 C  CA    . LYS A 1 135 ? -9.57879  -9.89803  -24.26685 1.000 29.64945  ? 146 LYS A CA    1 
ATOM   1076 C  C     . LYS A 1 135 ? -10.39223 -10.69228 -23.26009 1.000 31.73915  ? 146 LYS A C     1 
ATOM   1077 O  O     . LYS A 1 135 ? -10.93754 -10.13044 -22.30417 1.000 34.86876  ? 146 LYS A O     1 
ATOM   1078 C  CB    . LYS A 1 135 ? -10.37463 -9.73901  -25.56496 1.000 27.34868  ? 146 LYS A CB    1 
ATOM   1079 C  CG    . LYS A 1 135 ? -9.74333  -8.80272  -26.59486 1.000 32.46095  ? 146 LYS A CG    1 
ATOM   1080 C  CD    . LYS A 1 135 ? -10.64734 -8.69630  -27.84104 1.000 27.68675  ? 146 LYS A CD    1 
ATOM   1081 C  CE    . LYS A 1 135 ? -9.84734  -8.25544  -29.06946 1.000 46.42322  ? 146 LYS A CE    1 
ATOM   1082 N  NZ    . LYS A 1 135 ? -8.81115  -9.27078  -29.46095 1.000 42.28423  ? 146 LYS A NZ    1 
ATOM   1083 N  N     . LYS A 1 136 ? -10.48871 -12.00792 -23.46098 1.000 29.13050  ? 147 LYS A N     1 
ATOM   1084 C  CA    . LYS A 1 136 ? -11.20563 -12.87801 -22.53356 1.000 24.04905  ? 147 LYS A CA    1 
ATOM   1085 C  C     . LYS A 1 136 ? -10.43789 -14.12710 -22.12781 1.000 27.35997  ? 147 LYS A C     1 
ATOM   1086 O  O     . LYS A 1 136 ? -10.73828 -14.68610 -21.06965 1.000 29.26084  ? 147 LYS A O     1 
ATOM   1087 C  CB    . LYS A 1 136 ? -12.56284 -13.30254 -23.12228 1.000 26.06316  ? 147 LYS A CB    1 
ATOM   1088 C  CG    . LYS A 1 136 ? -13.46882 -12.13352 -23.52542 1.000 34.29593  ? 147 LYS A CG    1 
ATOM   1089 C  CD    . LYS A 1 136 ? -14.92089 -12.58191 -23.76498 1.000 41.70590  ? 147 LYS A CD    1 
ATOM   1090 C  CE    . LYS A 1 136 ? -15.85040 -11.36292 -23.95936 1.000 53.41201  ? 147 LYS A CE    1 
ATOM   1091 N  NZ    . LYS A 1 136 ? -17.30038 -11.71461 -24.18355 1.000 45.30266  ? 147 LYS A NZ    1 
ATOM   1092 N  N     . LYS A 1 137 ? -9.45085  -14.57336 -22.89566 1.000 26.29180  ? 148 LYS A N     1 
ATOM   1093 C  CA    . LYS A 1 137 ? -8.74862  -15.80759 -22.58886 1.000 22.56089  ? 148 LYS A CA    1 
ATOM   1094 C  C     . LYS A 1 137 ? -7.27822  -15.53297 -22.31331 1.000 21.75753  ? 148 LYS A C     1 
ATOM   1095 O  O     . LYS A 1 137 ? -6.67831  -14.64390 -22.92022 1.000 21.06837  ? 148 LYS A O     1 
ATOM   1096 C  CB    . LYS A 1 137 ? -8.89798  -16.81640 -23.74363 1.000 25.52054  ? 148 LYS A CB    1 
ATOM   1097 C  CG    . LYS A 1 137 ? -10.22698 -17.57364 -23.71194 1.000 30.57654  ? 148 LYS A CG    1 
ATOM   1098 C  CD    . LYS A 1 137 ? -10.39459 -18.46366 -24.92775 1.000 33.17699  ? 148 LYS A CD    1 
ATOM   1099 C  CE    . LYS A 1 137 ? -11.73585 -19.18602 -24.90511 1.000 34.90915  ? 148 LYS A CE    1 
ATOM   1100 N  NZ    . LYS A 1 137 ? -11.76687 -20.27060 -23.88679 1.000 36.07055  ? 148 LYS A NZ    1 
ATOM   1101 N  N     . TRP A 1 138 ? -6.70772  -16.29322 -21.38284 1.000 20.10453  ? 149 TRP A N     1 
ATOM   1102 C  CA    . TRP A 1 138 ? -5.25627  -16.37076 -21.26631 1.000 23.59681  ? 149 TRP A CA    1 
ATOM   1103 C  C     . TRP A 1 138 ? -4.66757  -17.11411 -22.45724 1.000 19.06564  ? 149 TRP A C     1 
ATOM   1104 O  O     . TRP A 1 138 ? -5.24406  -18.08813 -22.93351 1.000 19.29927  ? 149 TRP A O     1 
ATOM   1105 C  CB    . TRP A 1 138 ? -4.86649  -17.11412 -19.98993 1.000 19.07961  ? 149 TRP A CB    1 
ATOM   1106 C  CG    . TRP A 1 138 ? -5.21155  -16.41921 -18.72533 1.000 21.57854  ? 149 TRP A CG    1 
ATOM   1107 C  CD1   . TRP A 1 138 ? -6.33964  -16.59030 -17.97727 1.000 18.46321  ? 149 TRP A CD1   1 
ATOM   1108 C  CD2   . TRP A 1 138 ? -4.40951  -15.45716 -18.03336 1.000 20.69306  ? 149 TRP A CD2   1 
ATOM   1109 N  NE1   . TRP A 1 138 ? -6.29784  -15.78718 -16.87343 1.000 20.03349  ? 149 TRP A NE1   1 
ATOM   1110 C  CE2   . TRP A 1 138 ? -5.11919  -15.08271 -16.87658 1.000 20.35266  ? 149 TRP A CE2   1 
ATOM   1111 C  CE3   . TRP A 1 138 ? -3.16089  -14.86924 -18.28371 1.000 28.10375  ? 149 TRP A CE3   1 
ATOM   1112 C  CZ2   . TRP A 1 138 ? -4.62949  -14.14806 -15.97085 1.000 17.43944  ? 149 TRP A CZ2   1 
ATOM   1113 C  CZ3   . TRP A 1 138 ? -2.67050  -13.92938 -17.37223 1.000 23.38378  ? 149 TRP A CZ3   1 
ATOM   1114 C  CH2   . TRP A 1 138 ? -3.41178  -13.58049 -16.23190 1.000 19.08749  ? 149 TRP A CH2   1 
ATOM   1115 N  N     . THR A 1 139 ? -3.50897  -16.67333 -22.93077 1.000 22.61384  ? 150 THR A N     1 
ATOM   1116 C  CA    . THR A 1 139 ? -2.69527  -17.49017 -23.82158 1.000 21.73620  ? 150 THR A CA    1 
ATOM   1117 C  C     . THR A 1 139 ? -1.52185  -18.05344 -23.02936 1.000 27.02284  ? 150 THR A C     1 
ATOM   1118 O  O     . THR A 1 139 ? -0.79910  -17.31252 -22.34456 1.000 23.52136  ? 150 THR A O     1 
ATOM   1119 C  CB    . THR A 1 139 ? -2.20661  -16.70394 -25.04237 1.000 27.63558  ? 150 THR A CB    1 
ATOM   1120 O  OG1   . THR A 1 139 ? -3.30754  -16.47844 -25.92701 1.000 28.98182  ? 150 THR A OG1   1 
ATOM   1121 C  CG2   . THR A 1 139 ? -1.13770  -17.48919 -25.81135 1.000 26.31351  ? 150 THR A CG2   1 
ATOM   1122 N  N     . LEU A 1 140 ? -1.36819  -19.36727 -23.09913 1.000 22.13549  ? 151 LEU A N     1 
ATOM   1123 C  CA    . LEU A 1 140 ? -0.36698  -20.10884 -22.35902 1.000 21.99707  ? 151 LEU A CA    1 
ATOM   1124 C  C     . LEU A 1 140 ? 0.75627   -20.46915 -23.31498 1.000 24.90039  ? 151 LEU A C     1 
ATOM   1125 O  O     . LEU A 1 140 ? 0.50089   -21.05524 -24.36588 1.000 25.18100  ? 151 LEU A O     1 
ATOM   1126 C  CB    . LEU A 1 140 ? -0.97855  -21.38052 -21.77463 1.000 19.41614  ? 151 LEU A CB    1 
ATOM   1127 C  CG    . LEU A 1 140 ? -1.86494  -21.29922 -20.54222 1.000 23.18183  ? 151 LEU A CG    1 
ATOM   1128 C  CD1   . LEU A 1 140 ? -3.09190  -20.42913 -20.74951 1.000 22.04479  ? 151 LEU A CD1   1 
ATOM   1129 C  CD2   . LEU A 1 140 ? -2.26846  -22.71381 -20.18139 1.000 23.31265  ? 151 LEU A CD2   1 
ATOM   1130 N  N     . THR A 1 141 ? 1.98529   -20.10982 -22.96326 1.000 23.61978  ? 152 THR A N     1 
ATOM   1131 C  CA    . THR A 1 141 ? 3.15380   -20.37567 -23.79527 1.000 25.30270  ? 152 THR A CA    1 
ATOM   1132 C  C     . THR A 1 141 ? 3.97774   -21.47756 -23.14952 1.000 28.69422  ? 152 THR A C     1 
ATOM   1133 O  O     . THR A 1 141 ? 4.40885   -21.34415 -21.99829 1.000 25.66535  ? 152 THR A O     1 
ATOM   1134 C  CB    . THR A 1 141 ? 4.00455   -19.11928 -23.97855 1.000 28.95972  ? 152 THR A CB    1 
ATOM   1135 O  OG1   . THR A 1 141 ? 3.23822   -18.10986 -24.64775 1.000 26.42033  ? 152 THR A OG1   1 
ATOM   1136 C  CG2   . THR A 1 141 ? 5.23926   -19.43227 -24.80714 1.000 24.12674  ? 152 THR A CG2   1 
ATOM   1137 N  N     . PHE A 1 142 ? 4.20024   -22.55970 -23.88605 1.000 29.42908  ? 153 PHE A N     1 
ATOM   1138 C  CA    . PHE A 1 142 ? 4.95954   -23.68920 -23.38027 1.000 20.52630  ? 153 PHE A CA    1 
ATOM   1139 C  C     . PHE A 1 142 ? 6.29269   -23.78709 -24.09894 1.000 28.00227  ? 153 PHE A C     1 
ATOM   1140 O  O     . PHE A 1 142 ? 6.47679   -23.25683 -25.19455 1.000 30.65475  ? 153 PHE A O     1 
ATOM   1141 C  CB    . PHE A 1 142 ? 4.17865   -24.98757 -23.54811 1.000 23.18032  ? 153 PHE A CB    1 
ATOM   1142 C  CG    . PHE A 1 142 ? 2.86092   -24.97705 -22.86080 1.000 22.99023  ? 153 PHE A CG    1 
ATOM   1143 C  CD1   . PHE A 1 142 ? 2.77336   -25.25661 -21.49982 1.000 21.67901  ? 153 PHE A CD1   1 
ATOM   1144 C  CD2   . PHE A 1 142 ? 1.70809   -24.67362 -23.56341 1.000 21.80290  ? 153 PHE A CD2   1 
ATOM   1145 C  CE1   . PHE A 1 142 ? 1.54943   -25.24896 -20.85166 1.000 22.09564  ? 153 PHE A CE1   1 
ATOM   1146 C  CE2   . PHE A 1 142 ? 0.47673   -24.67094 -22.93088 1.000 23.30106  ? 153 PHE A CE2   1 
ATOM   1147 C  CZ    . PHE A 1 142 ? 0.39560   -24.95537 -21.56506 1.000 23.63116  ? 153 PHE A CZ    1 
ATOM   1148 N  N     . GLU A 1 143 ? 7.23055   -24.46548 -23.45782 1.000 24.63824  ? 154 GLU A N     1 
ATOM   1149 C  CA    . GLU A 1 143 ? 8.56759   -24.62839 -24.01612 1.000 23.18430  ? 154 GLU A CA    1 
ATOM   1150 C  C     . GLU A 1 143 ? 8.52948   -25.55068 -25.23656 1.000 26.71449  ? 154 GLU A C     1 
ATOM   1151 O  O     . GLU A 1 143 ? 8.27187   -26.75235 -25.11451 1.000 28.59030  ? 154 GLU A O     1 
ATOM   1152 C  CB    . GLU A 1 143 ? 9.48750   -25.16998 -22.93011 1.000 25.33187  ? 154 GLU A CB    1 
ATOM   1153 C  CG    . GLU A 1 143 ? 10.91780  -25.31376 -23.33899 1.000 36.39812  ? 154 GLU A CG    1 
ATOM   1154 C  CD    . GLU A 1 143 ? 11.78306  -25.78267 -22.18709 1.000 40.83906  ? 154 GLU A CD    1 
ATOM   1155 O  OE1   . GLU A 1 143 ? 11.77086  -25.12595 -21.12344 1.000 46.48240  ? 154 GLU A OE1   1 
ATOM   1156 O  OE2   . GLU A 1 143 ? 12.45789  -26.81592 -22.34685 1.000 54.97997  ? 154 GLU A OE2   1 
ATOM   1157 N  N     . ASN A 1 144 ? 8.76356   -24.97514 -26.41732 1.000 27.43373  ? 155 ASN A N     1 
ATOM   1158 C  CA    . ASN A 1 144 ? 8.92431   -25.68503 -27.68569 1.000 25.73865  ? 155 ASN A CA    1 
ATOM   1159 C  C     . ASN A 1 144 ? 7.67569   -26.48098 -28.09215 1.000 26.06919  ? 155 ASN A C     1 
ATOM   1160 O  O     . ASN A 1 144 ? 7.75347   -27.38060 -28.93631 1.000 27.98867  ? 155 ASN A O     1 
ATOM   1161 C  CB    . ASN A 1 144 ? 10.18018  -26.57773 -27.65825 1.000 28.97299  ? 155 ASN A CB    1 
ATOM   1162 C  CG    . ASN A 1 144 ? 11.48302  -25.75642 -27.52088 1.000 33.79042  ? 155 ASN A CG    1 
ATOM   1163 O  OD1   . ASN A 1 144 ? 11.47663  -24.65548 -26.98711 1.000 37.29585  ? 155 ASN A OD1   1 
ATOM   1164 N  ND2   . ASN A 1 144 ? 12.58888  -26.29122 -28.01628 1.000 33.22836  ? 155 ASN A ND2   1 
ATOM   1165 N  N     . LYS A 1 145 ? 6.51183   -26.12355 -27.56071 1.000 24.66322  ? 156 LYS A N     1 
ATOM   1166 C  CA    . LYS A 1 145 ? 5.23371   -26.75717 -27.84616 1.000 23.54047  ? 156 LYS A CA    1 
ATOM   1167 C  C     . LYS A 1 145 ? 4.22639   -25.67186 -28.18722 1.000 29.78847  ? 156 LYS A C     1 
ATOM   1168 O  O     . LYS A 1 145 ? 4.39968   -24.51472 -27.79324 1.000 26.07910  ? 156 LYS A O     1 
ATOM   1169 C  CB    . LYS A 1 145 ? 4.73197   -27.57914 -26.64655 1.000 24.34069  ? 156 LYS A CB    1 
ATOM   1170 C  CG    . LYS A 1 145 ? 5.70654   -28.66009 -26.16397 1.000 28.65358  ? 156 LYS A CG    1 
ATOM   1171 C  CD    . LYS A 1 145 ? 5.74225   -29.82622 -27.13755 1.000 30.82182  ? 156 LYS A CD    1 
ATOM   1172 C  CE    . LYS A 1 145 ? 6.79540   -30.85128 -26.73063 1.000 38.17723  ? 156 LYS A CE    1 
ATOM   1173 N  NZ    . LYS A 1 145 ? 8.13281   -30.51403 -27.31608 1.000 49.86193  ? 156 LYS A NZ    1 
ATOM   1174 N  N     . PRO A 1 146 ? 3.15858   -26.00588 -28.91742 1.000 24.97959  ? 157 PRO A N     1 
ATOM   1175 C  CA    . PRO A 1 146 ? 2.21367   -24.96328 -29.32687 1.000 27.49217  ? 157 PRO A CA    1 
ATOM   1176 C  C     . PRO A 1 146 ? 1.42795   -24.43161 -28.14090 1.000 22.83041  ? 157 PRO A C     1 
ATOM   1177 O  O     . PRO A 1 146 ? 1.26934   -25.09716 -27.11469 1.000 23.40274  ? 157 PRO A O     1 
ATOM   1178 C  CB    . PRO A 1 146 ? 1.30234   -25.66624 -30.34044 1.000 30.46470  ? 157 PRO A CB    1 
ATOM   1179 C  CG    . PRO A 1 146 ? 1.44803   -27.12291 -30.07314 1.000 30.26327  ? 157 PRO A CG    1 
ATOM   1180 C  CD    . PRO A 1 146 ? 2.79740   -27.33681 -29.45001 1.000 29.55651  ? 157 PRO A CD    1 
ATOM   1181 N  N     . SER A 1 147 ? 0.94880   -23.20139 -28.29581 1.000 25.96455  ? 158 SER A N     1 
ATOM   1182 C  CA    . SER A 1 147 ? 0.28700   -22.48107 -27.22082 1.000 24.98503  ? 158 SER A CA    1 
ATOM   1183 C  C     . SER A 1 147 ? -1.12859  -22.99920 -27.02020 1.000 26.72636  ? 158 SER A C     1 
ATOM   1184 O  O     . SER A 1 147 ? -1.70085  -23.68119 -27.87877 1.000 22.46089  ? 158 SER A O     1 
ATOM   1185 C  CB    . SER A 1 147 ? 0.25558   -20.98254 -27.52238 1.000 23.60945  ? 158 SER A CB    1 
ATOM   1186 O  OG    . SER A 1 147 ? -0.50836  -20.72140 -28.68616 1.000 27.52104  ? 158 SER A OG    1 
ATOM   1187 N  N     . GLU A 1 148 ? -1.69649  -22.66151 -25.86281 1.000 22.75123  ? 159 GLU A N     1 
ATOM   1188 C  CA    . GLU A 1 148 ? -3.06006  -23.03822 -25.52454 1.000 23.51033  ? 159 GLU A CA    1 
ATOM   1189 C  C     . GLU A 1 148 ? -3.74832  -21.83265 -24.89836 1.000 26.11331  ? 159 GLU A C     1 
ATOM   1190 O  O     . GLU A 1 148 ? -3.09333  -20.86381 -24.51378 1.000 24.42302  ? 159 GLU A O     1 
ATOM   1191 C  CB    . GLU A 1 148 ? -3.08847  -24.24404 -24.57417 1.000 23.52715  ? 159 GLU A CB    1 
ATOM   1192 C  CG    . GLU A 1 148 ? -2.30997  -25.46981 -25.05942 1.000 24.50751  ? 159 GLU A CG    1 
ATOM   1193 C  CD    . GLU A 1 148 ? -3.08502  -26.33542 -26.04577 1.000 28.88186  ? 159 GLU A CD    1 
ATOM   1194 O  OE1   . GLU A 1 148 ? -4.24485  -25.99513 -26.37378 1.000 28.34542  ? 159 GLU A OE1   1 
ATOM   1195 O  OE2   . GLU A 1 148 ? -2.52758  -27.36444 -26.49459 1.000 31.37656  ? 159 GLU A OE2   1 
ATOM   1196 N  N     . THR A 1 149 ? -5.08185  -21.87527 -24.82565 1.000 22.57809  ? 160 THR A N     1 
ATOM   1197 C  CA    . THR A 1 149 ? -5.85363  -20.79632 -24.21027 1.000 25.73334  ? 160 THR A CA    1 
ATOM   1198 C  C     . THR A 1 149 ? -6.75819  -21.34771 -23.11131 1.000 25.58921  ? 160 THR A C     1 
ATOM   1199 O  O     . THR A 1 149 ? -7.10535  -22.53518 -23.09984 1.000 23.83363  ? 160 THR A O     1 
ATOM   1200 C  CB    . THR A 1 149 ? -6.71113  -20.02597 -25.22543 1.000 26.05332  ? 160 THR A CB    1 
ATOM   1201 O  OG1   . THR A 1 149 ? -7.64972  -20.91546 -25.83450 1.000 30.45977  ? 160 THR A OG1   1 
ATOM   1202 C  CG2   . THR A 1 149 ? -5.83957  -19.36783 -26.31943 1.000 24.06104  ? 160 THR A CG2   1 
ATOM   1203 N  N     . ALA A 1 150 ? -7.13600  -20.46577 -22.18303 1.000 21.27851  ? 161 ALA A N     1 
ATOM   1204 C  CA    . ALA A 1 150 ? -8.01872  -20.84606 -21.08816 1.000 23.96603  ? 161 ALA A CA    1 
ATOM   1205 C  C     . ALA A 1 150 ? -8.68093  -19.60846 -20.49637 1.000 17.11723  ? 161 ALA A C     1 
ATOM   1206 O  O     . ALA A 1 150 ? -8.06581  -18.54587 -20.39945 1.000 19.64804  ? 161 ALA A O     1 
ATOM   1207 C  CB    . ALA A 1 150 ? -7.25250  -21.60056 -19.99306 1.000 20.19691  ? 161 ALA A CB    1 
ATOM   1208 N  N     . ASP A 1 151 ? -9.93860  -19.77022 -20.08273 1.000 20.00910  ? 162 ASP A N     1 
ATOM   1209 C  CA    . ASP A 1 151 ? -10.65817 -18.68558 -19.40951 1.000 23.72224  ? 162 ASP A CA    1 
ATOM   1210 C  C     . ASP A 1 151 ? -10.16321 -18.47993 -17.98701 1.000 25.55358  ? 162 ASP A C     1 
ATOM   1211 O  O     . ASP A 1 151 ? -10.26251 -17.36775 -17.44904 1.000 19.95759  ? 162 ASP A O     1 
ATOM   1212 C  CB    . ASP A 1 151 ? -12.15390 -18.98112 -19.38732 1.000 19.61541  ? 162 ASP A CB    1 
ATOM   1213 C  CG    . ASP A 1 151 ? -12.74088 -19.03424 -20.76474 1.000 23.94237  ? 162 ASP A CG    1 
ATOM   1214 O  OD1   . ASP A 1 151 ? -13.04712 -17.96141 -21.30565 1.000 23.38332  ? 162 ASP A OD1   1 
ATOM   1215 O  OD2   . ASP A 1 151 ? -12.86582 -20.14544 -21.31845 1.000 24.78574  ? 162 ASP A OD2   1 
ATOM   1216 N  N     . LEU A 1 152 ? -9.64754  -19.54103 -17.36492 1.000 19.40305  ? 163 LEU A N     1 
ATOM   1217 C  CA    . LEU A 1 152 ? -9.20040  -19.50559 -15.98675 1.000 19.01498  ? 163 LEU A CA    1 
ATOM   1218 C  C     . LEU A 1 152 ? -7.90671  -20.29135 -15.89817 1.000 19.63212  ? 163 LEU A C     1 
ATOM   1219 O  O     . LEU A 1 152 ? -7.82635  -21.41681 -16.39992 1.000 16.31876  ? 163 LEU A O     1 
ATOM   1220 C  CB    . LEU A 1 152 ? -10.26402 -20.09538 -15.04086 1.000 16.62543  ? 163 LEU A CB    1 
ATOM   1221 C  CG    . LEU A 1 152 ? -9.82905  -20.39384 -13.60675 1.000 17.29312  ? 163 LEU A CG    1 
ATOM   1222 C  CD1   . LEU A 1 152 ? -9.44940  -19.11296 -12.86756 1.000 16.89450  ? 163 LEU A CD1   1 
ATOM   1223 C  CD2   . LEU A 1 152 ? -10.92425 -21.13682 -12.84329 1.000 14.50068  ? 163 LEU A CD2   1 
ATOM   1224 N  N     . VAL A 1 153 ? -6.89651  -19.69436 -15.27100 1.000 19.43298  ? 164 VAL A N     1 
ATOM   1225 C  CA    . VAL A 1 153 ? -5.60663  -20.33800 -15.06044 1.000 15.66436  ? 164 VAL A CA    1 
ATOM   1226 C  C     . VAL A 1 153 ? -5.41720  -20.53170 -13.56095 1.000 19.52768  ? 164 VAL A C     1 
ATOM   1227 O  O     . VAL A 1 153 ? -5.61786  -19.59815 -12.77264 1.000 17.80840  ? 164 VAL A O     1 
ATOM   1228 C  CB    . VAL A 1 153 ? -4.46082  -19.51276 -15.66912 1.000 19.48550  ? 164 VAL A CB    1 
ATOM   1229 C  CG1   . VAL A 1 153 ? -3.11676  -20.10274 -15.25210 1.000 14.61642  ? 164 VAL A CG1   1 
ATOM   1230 C  CG2   . VAL A 1 153 ? -4.58444  -19.47838 -17.20313 1.000 17.46806  ? 164 VAL A CG2   1 
ATOM   1231 N  N     . ILE A 1 154 ? -5.05700  -21.74566 -13.16673 1.000 19.79124  ? 165 ILE A N     1 
ATOM   1232 C  CA    . ILE A 1 154 ? -4.82965  -22.08486 -11.77048 1.000 17.89244  ? 165 ILE A CA    1 
ATOM   1233 C  C     . ILE A 1 154 ? -3.38683  -22.55347 -11.66739 1.000 20.88383  ? 165 ILE A C     1 
ATOM   1234 O  O     . ILE A 1 154 ? -3.02692  -23.61038 -12.20508 1.000 16.42659  ? 165 ILE A O     1 
ATOM   1235 C  CB    . ILE A 1 154 ? -5.80379  -23.15557 -11.26592 1.000 17.57051  ? 165 ILE A CB    1 
ATOM   1236 C  CG1   . ILE A 1 154 ? -7.25277  -22.65211 -11.35160 1.000 18.79120  ? 165 ILE A CG1   1 
ATOM   1237 C  CG2   . ILE A 1 154 ? -5.44272  -23.56599 -9.84811  1.000 15.47573  ? 165 ILE A CG2   1 
ATOM   1238 C  CD1   . ILE A 1 154 ? -8.31045  -23.66393 -10.90723 1.000 14.46043  ? 165 ILE A CD1   1 
ATOM   1239 N  N     . ILE A 1 155 ? -2.55874  -21.76231 -10.99012 1.000 18.70867  ? 166 ILE A N     1 
ATOM   1240 C  CA    . ILE A 1 155 ? -1.13619  -22.06254 -10.84848 1.000 17.39365  ? 166 ILE A CA    1 
ATOM   1241 C  C     . ILE A 1 155 ? -0.98014  -23.11250 -9.74737  1.000 18.25016  ? 166 ILE A C     1 
ATOM   1242 O  O     . ILE A 1 155 ? -1.21815  -22.82784 -8.57334  1.000 21.10836  ? 166 ILE A O     1 
ATOM   1243 C  CB    . ILE A 1 155 ? -0.32515  -20.80432 -10.51796 1.000 14.72962  ? 166 ILE A CB    1 
ATOM   1244 C  CG1   . ILE A 1 155 ? -0.49650  -19.71932 -11.59598 1.000 17.96149  ? 166 ILE A CG1   1 
ATOM   1245 C  CG2   . ILE A 1 155 ? 1.14554   -21.15566 -10.25617 1.000 19.28043  ? 166 ILE A CG2   1 
ATOM   1246 C  CD1   . ILE A 1 155 ? -0.16419  -20.16385 -13.01278 1.000 20.93244  ? 166 ILE A CD1   1 
ATOM   1247 N  N     . ALA A 1 156 ? -0.53765  -24.32051 -10.11708 1.000 18.43275  ? 167 ALA A N     1 
ATOM   1248 C  CA    . ALA A 1 156 ? -0.33767  -25.39832 -9.15541  1.000 18.55443  ? 167 ALA A CA    1 
ATOM   1249 C  C     . ALA A 1 156 ? 1.01059   -26.07042 -9.36331  1.000 19.63439  ? 167 ALA A C     1 
ATOM   1250 O  O     . ALA A 1 156 ? 1.14470   -27.27700 -9.18340  1.000 16.95731  ? 167 ALA A O     1 
ATOM   1251 C  CB    . ALA A 1 156 ? -1.46402  -26.42254 -9.25779  1.000 14.78793  ? 167 ALA A CB    1 
ATOM   1252 N  N     . ASN A 1 157 ? 2.01931   -25.32349 -9.78843  1.000 18.64341  ? 168 ASN A N     1 
ATOM   1253 C  CA    . ASN A 1 157 ? 3.24354   -25.96237 -10.24083 1.000 18.28773  ? 168 ASN A CA    1 
ATOM   1254 C  C     . ASN A 1 157 ? 4.36597   -25.82706 -9.21704  1.000 18.60939  ? 168 ASN A C     1 
ATOM   1255 O  O     . ASN A 1 157 ? 5.53759   -25.75611 -9.57727  1.000 19.72788  ? 168 ASN A O     1 
ATOM   1256 C  CB    . ASN A 1 157 ? 3.65239   -25.45160 -11.62664 1.000 15.06991  ? 168 ASN A CB    1 
ATOM   1257 C  CG    . ASN A 1 157 ? 4.14439   -24.01932 -11.62414 1.000 20.81927  ? 168 ASN A CG    1 
ATOM   1258 O  OD1   . ASN A 1 157 ? 3.49060   -23.13811 -11.08544 1.000 18.70570  ? 168 ASN A OD1   1 
ATOM   1259 N  ND2   . ASN A 1 157 ? 5.31065   -23.78048 -12.24720 1.000 17.26931  ? 168 ASN A ND2   1 
ATOM   1260 N  N     . GLY A 1 158 ? 4.01750   -25.82483 -7.93067  1.000 17.91714  ? 169 GLY A N     1 
ATOM   1261 C  CA    . GLY A 1 158 ? 4.99582   -26.05408 -6.88879  1.000 18.82450  ? 169 GLY A CA    1 
ATOM   1262 C  C     . GLY A 1 158 ? 5.64333   -24.79116 -6.36695  1.000 23.56664  ? 169 GLY A C     1 
ATOM   1263 O  O     . GLY A 1 158 ? 5.39628   -23.66657 -6.82582  1.000 17.96953  ? 169 GLY A O     1 
ATOM   1264 N  N     . GLY A 1 159 ? 6.53901   -25.00927 -5.39657  1.000 15.91132  ? 170 GLY A N     1 
ATOM   1265 C  CA    . GLY A 1 159 ? 7.05769   -23.91126 -4.60779  1.000 16.23382  ? 170 GLY A CA    1 
ATOM   1266 C  C     . GLY A 1 159 ? 7.97605   -22.98463 -5.37259  1.000 25.46060  ? 170 GLY A C     1 
ATOM   1267 O  O     . GLY A 1 159 ? 8.08789   -21.80094 -5.02962  1.000 20.63671  ? 170 GLY A O     1 
ATOM   1268 N  N     . MET A 1 160 ? 8.63977   -23.49055 -6.41679  1.000 20.81726  ? 171 MET A N     1 
ATOM   1269 C  CA    . MET A 1 160 ? 9.56719   -22.67238 -7.18849  1.000 23.54804  ? 171 MET A CA    1 
ATOM   1270 C  C     . MET A 1 160 ? 8.93158   -22.06836 -8.43726  1.000 22.48172  ? 171 MET A C     1 
ATOM   1271 O  O     . MET A 1 160 ? 9.65722   -21.70619 -9.36683  1.000 30.59574  ? 171 MET A O     1 
ATOM   1272 C  CB    . MET A 1 160 ? 10.81042  -23.48091 -7.57622  1.000 21.89271  ? 171 MET A CB    1 
ATOM   1273 C  CG    . MET A 1 160 ? 11.66126  -23.97843 -6.39060  1.000 29.48709  ? 171 MET A CG    1 
ATOM   1274 S  SD    . MET A 1 160 ? 12.10379  -22.65215 -5.24600  1.000 41.41144  ? 171 MET A SD    1 
ATOM   1275 C  CE    . MET A 1 160 ? 13.52846  -21.91711 -6.05178  1.000 25.74839  ? 171 MET A CE    1 
ATOM   1276 N  N     . SER A 1 161 ? 7.60432   -21.94147 -8.47597  1.000 22.27698  ? 172 SER A N     1 
ATOM   1277 C  CA    . SER A 1 161 ? 6.91008   -21.45997 -9.67234  1.000 18.11515  ? 172 SER A CA    1 
ATOM   1278 C  C     . SER A 1 161 ? 7.45047   -20.10608 -10.10913 1.000 22.63764  ? 172 SER A C     1 
ATOM   1279 O  O     . SER A 1 161 ? 7.64487   -19.21277 -9.28223  1.000 26.23236  ? 172 SER A O     1 
ATOM   1280 C  CB    . SER A 1 161 ? 5.41057   -21.33981 -9.39661  1.000 17.72624  ? 172 SER A CB    1 
ATOM   1281 O  OG    . SER A 1 161 ? 4.74756   -20.79788 -10.52402 1.000 16.55303  ? 172 SER A OG    1 
ATOM   1282 N  N     . LYS A 1 162 ? 7.69147   -19.95026 -11.41483 1.000 18.50104  ? 173 LYS A N     1 
ATOM   1283 C  CA    . LYS A 1 162 ? 8.09890   -18.65988 -11.96509 1.000 22.87255  ? 173 LYS A CA    1 
ATOM   1284 C  C     . LYS A 1 162 ? 6.96013   -17.92814 -12.66697 1.000 26.15678  ? 173 LYS A C     1 
ATOM   1285 O  O     . LYS A 1 162 ? 7.18435   -16.85228 -13.23798 1.000 26.18503  ? 173 LYS A O     1 
ATOM   1286 C  CB    . LYS A 1 162 ? 9.26905   -18.83900 -12.93809 1.000 25.06911  ? 173 LYS A CB    1 
ATOM   1287 C  CG    . LYS A 1 162 ? 10.51048  -19.52719 -12.33469 1.000 29.61485  ? 173 LYS A CG    1 
ATOM   1288 C  CD    . LYS A 1 162 ? 11.60703  -19.59760 -13.40249 1.000 40.80684  ? 173 LYS A CD    1 
ATOM   1289 C  CE    . LYS A 1 162 ? 12.40615  -20.89548 -13.33089 1.000 59.89153  ? 173 LYS A CE    1 
ATOM   1290 N  NZ    . LYS A 1 162 ? 12.86900  -21.39532 -14.67406 1.000 69.54670  ? 173 LYS A NZ    1 
ATOM   1291 N  N     . VAL A 1 163 ? 5.74478   -18.46998 -12.62262 1.000 20.35855  ? 174 VAL A N     1 
ATOM   1292 C  CA    . VAL A 1 163 ? 4.62072   -17.87377 -13.33057 1.000 22.45180  ? 174 VAL A CA    1 
ATOM   1293 C  C     . VAL A 1 163 ? 3.58036   -17.34204 -12.34581 1.000 26.63823  ? 174 VAL A C     1 
ATOM   1294 O  O     . VAL A 1 163 ? 2.37284   -17.57460 -12.50654 1.000 24.80349  ? 174 VAL A O     1 
ATOM   1295 C  CB    . VAL A 1 163 ? 4.01312   -18.89389 -14.30654 1.000 23.59121  ? 174 VAL A CB    1 
ATOM   1296 C  CG1   . VAL A 1 163 ? 4.96706   -19.12117 -15.47147 1.000 23.52074  ? 174 VAL A CG1   1 
ATOM   1297 C  CG2   . VAL A 1 163 ? 3.73059   -20.19842 -13.58362 1.000 15.00923  ? 174 VAL A CG2   1 
ATOM   1298 N  N     . ARG A 1 164 ? 4.03905   -16.60329 -11.32878 1.000 26.16707  ? 175 ARG A N     1 
ATOM   1299 C  CA    . ARG A 1 164 ? 3.16256   -16.09072 -10.28706 1.000 25.25165  ? 175 ARG A CA    1 
ATOM   1300 C  C     . ARG A 1 164 ? 2.85609   -14.60670 -10.40964 1.000 26.99452  ? 175 ARG A C     1 
ATOM   1301 O  O     . ARG A 1 164 ? 1.94731   -14.13350 -9.71648  1.000 20.74040  ? 175 ARG A O     1 
ATOM   1302 C  CB    . ARG A 1 164 ? 3.77447   -16.32334 -8.89951  1.000 25.95967  ? 175 ARG A CB    1 
ATOM   1303 C  CG    . ARG A 1 164 ? 3.97005   -17.77976 -8.48819  1.000 24.33463  ? 175 ARG A CG    1 
ATOM   1304 C  CD    . ARG A 1 164 ? 5.02917   -17.79315 -7.42234  1.000 28.04923  ? 175 ARG A CD    1 
ATOM   1305 N  NE    . ARG A 1 164 ? 4.87180   -18.83236 -6.41559  1.000 26.79649  ? 175 ARG A NE    1 
ATOM   1306 C  CZ    . ARG A 1 164 ? 5.89219   -19.47708 -5.86953  1.000 25.63654  ? 175 ARG A CZ    1 
ATOM   1307 N  NH1   . ARG A 1 164 ? 7.13117   -19.30297 -6.30965  1.000 27.07505  ? 175 ARG A NH1   1 
ATOM   1308 N  NH2   . ARG A 1 164 ? 5.67029   -20.29930 -4.84645  1.000 24.34440  ? 175 ARG A NH2   1 
ATOM   1309 N  N     . LYS A 1 165 ? 3.58287   -13.86679 -11.25818 1.000 25.23370  ? 176 LYS A N     1 
ATOM   1310 C  CA    . LYS A 1 165 ? 3.61132   -12.40475 -11.15057 1.000 28.96452  ? 176 LYS A CA    1 
ATOM   1311 C  C     . LYS A 1 165 ? 2.24783   -11.77379 -11.40294 1.000 28.54358  ? 176 LYS A C     1 
ATOM   1312 O  O     . LYS A 1 165 ? 1.96426   -10.69333 -10.87424 1.000 28.67138  ? 176 LYS A O     1 
ATOM   1313 C  CB    . LYS A 1 165 ? 4.64860   -11.80990 -12.11033 1.000 30.94113  ? 176 LYS A CB    1 
ATOM   1314 C  CG    . LYS A 1 165 ? 6.10779   -11.91672 -11.61417 1.000 42.95205  ? 176 LYS A CG    1 
ATOM   1315 C  CD    . LYS A 1 165 ? 6.26821   -11.30256 -10.21498 1.000 46.02364  ? 176 LYS A CD    1 
ATOM   1316 C  CE    . LYS A 1 165 ? 7.69595   -11.39220 -9.66466  1.000 39.71513  ? 176 LYS A CE    1 
ATOM   1317 N  NZ    . LYS A 1 165 ? 8.22534   -12.77927 -9.60397  1.000 45.01865  ? 176 LYS A NZ    1 
ATOM   1318 N  N     . PHE A 1 166 ? 1.38620   -12.41667 -12.19329 1.000 22.85772  ? 177 PHE A N     1 
ATOM   1319 C  CA    . PHE A 1 166 ? 0.05089   -11.84670 -12.33504 1.000 25.03348  ? 177 PHE A CA    1 
ATOM   1320 C  C     . PHE A 1 166 ? -0.75701  -11.93737 -11.04772 1.000 28.46077  ? 177 PHE A C     1 
ATOM   1321 O  O     . PHE A 1 166 ? -1.77521  -11.24931 -10.92457 1.000 24.44700  ? 177 PHE A O     1 
ATOM   1322 C  CB    . PHE A 1 166 ? -0.70563  -12.51064 -13.49668 1.000 26.33856  ? 177 PHE A CB    1 
ATOM   1323 C  CG    . PHE A 1 166 ? -0.31129  -11.97070 -14.84832 1.000 26.91105  ? 177 PHE A CG    1 
ATOM   1324 C  CD1   . PHE A 1 166 ? -0.60955  -10.66222 -15.19538 1.000 26.53059  ? 177 PHE A CD1   1 
ATOM   1325 C  CD2   . PHE A 1 166 ? 0.38915   -12.76074 -15.75362 1.000 26.88177  ? 177 PHE A CD2   1 
ATOM   1326 C  CE1   . PHE A 1 166 ? -0.23566  -10.14465 -16.43958 1.000 29.02882  ? 177 PHE A CE1   1 
ATOM   1327 C  CE2   . PHE A 1 166 ? 0.76597   -12.25966 -16.98928 1.000 25.44855  ? 177 PHE A CE2   1 
ATOM   1328 C  CZ    . PHE A 1 166 ? 0.46526   -10.94885 -17.33122 1.000 24.05055  ? 177 PHE A CZ    1 
ATOM   1329 N  N     . VAL A 1 167 ? -0.30977  -12.72782 -10.07759 1.000 25.06293  ? 178 VAL A N     1 
ATOM   1330 C  CA    . VAL A 1 167 ? -1.00234  -12.87069 -8.80361  1.000 23.58224  ? 178 VAL A CA    1 
ATOM   1331 C  C     . VAL A 1 167 ? -0.30492  -12.10289 -7.68394  1.000 24.85872  ? 178 VAL A C     1 
ATOM   1332 O  O     . VAL A 1 167 ? -0.96756  -11.46813 -6.86292  1.000 27.05819  ? 178 VAL A O     1 
ATOM   1333 C  CB    . VAL A 1 167 ? -1.14876  -14.37087 -8.46062  1.000 24.82303  ? 178 VAL A CB    1 
ATOM   1334 C  CG1   . VAL A 1 167 ? -1.60344  -14.56707 -7.03616  1.000 22.21846  ? 178 VAL A CG1   1 
ATOM   1335 C  CG2   . VAL A 1 167 ? -2.14004  -15.01740 -9.41366  1.000 18.57543  ? 178 VAL A CG2   1 
ATOM   1336 N  N     . THR A 1 168 ? 1.02541   -12.13421 -7.62480  1.000 26.46206  ? 179 THR A N     1 
ATOM   1337 C  CA    . THR A 1 168 ? 1.73167   -11.48020 -6.52611  1.000 26.03739  ? 179 THR A CA    1 
ATOM   1338 C  C     . THR A 1 168 ? 3.18180   -11.25743 -6.92534  1.000 29.04525  ? 179 THR A C     1 
ATOM   1339 O  O     . THR A 1 168 ? 3.73330   -11.99946 -7.73639  1.000 24.60019  ? 179 THR A O     1 
ATOM   1340 C  CB    . THR A 1 168 ? 1.67043   -12.31063 -5.23431  1.000 29.20123  ? 179 THR A CB    1 
ATOM   1341 O  OG1   . THR A 1 168 ? 2.49286   -11.70231 -4.23100  1.000 25.67867  ? 179 THR A OG1   1 
ATOM   1342 C  CG2   . THR A 1 168 ? 2.16002   -13.76419 -5.47717  1.000 22.31139  ? 179 THR A CG2   1 
ATOM   1343 N  N     . ASP A 1 169 ? 3.79079   -10.23098 -6.34138  1.000 29.98487  ? 180 ASP A N     1 
ATOM   1344 C  CA    . ASP A 1 169 ? 5.21692   -9.97842  -6.49524  1.000 30.85768  ? 180 ASP A CA    1 
ATOM   1345 C  C     . ASP A 1 169 ? 6.05676   -10.64356 -5.41334  1.000 32.42781  ? 180 ASP A C     1 
ATOM   1346 O  O     . ASP A 1 169 ? 7.28312   -10.47791 -5.41905  1.000 31.87492  ? 180 ASP A O     1 
ATOM   1347 C  CB    . ASP A 1 169 ? 5.49986   -8.46822  -6.48380  1.000 27.52085  ? 180 ASP A CB    1 
ATOM   1348 C  CG    . ASP A 1 169 ? 4.87247   -7.74664  -7.66292  1.000 35.69403  ? 180 ASP A CG    1 
ATOM   1349 O  OD1   . ASP A 1 169 ? 4.86917   -8.30904  -8.77719  1.000 37.40660  ? 180 ASP A OD1   1 
ATOM   1350 O  OD2   . ASP A 1 169 ? 4.37939   -6.61854  -7.46751  1.000 42.21429  ? 180 ASP A OD2   1 
ATOM   1351 N  N     . THR A 1 170 ? 5.42412   -11.35254 -4.47619  1.000 32.78808  ? 181 THR A N     1 
ATOM   1352 C  CA    . THR A 1 170 ? 6.14370   -12.04984 -3.41434  1.000 30.68134  ? 181 THR A CA    1 
ATOM   1353 C  C     . THR A 1 170 ? 7.14760   -13.02689 -4.01249  1.000 30.32847  ? 181 THR A C     1 
ATOM   1354 O  O     . THR A 1 170 ? 6.87657   -13.67533 -5.02333  1.000 27.97938  ? 181 THR A O     1 
ATOM   1355 C  CB    . THR A 1 170 ? 5.14333   -12.79126 -2.51290  1.000 32.96051  ? 181 THR A CB    1 
ATOM   1356 O  OG1   . THR A 1 170 ? 4.26438   -11.84110 -1.88901  1.000 33.23694  ? 181 THR A OG1   1 
ATOM   1357 C  CG2   . THR A 1 170 ? 5.85819   -13.62066 -1.43034  1.000 29.63346  ? 181 THR A CG2   1 
ATOM   1358 N  N     . GLU A 1 171 ? 8.32111   -13.11375 -3.39266  1.000 30.78683  ? 182 GLU A N     1 
ATOM   1359 C  CA    . GLU A 1 171 ? 9.39846   -13.98497 -3.83734  1.000 33.67970  ? 182 GLU A CA    1 
ATOM   1360 C  C     . GLU A 1 171 ? 9.61141   -15.11602 -2.84059  1.000 29.88325  ? 182 GLU A C     1 
ATOM   1361 O  O     . GLU A 1 171 ? 9.45284   -14.94142 -1.63230  1.000 29.29583  ? 182 GLU A O     1 
ATOM   1362 C  CB    . GLU A 1 171 ? 10.70970  -13.20984 -4.00234  1.000 35.03759  ? 182 GLU A CB    1 
ATOM   1363 C  CG    . GLU A 1 171 ? 10.68110  -12.12126 -5.08057  1.000 44.67487  ? 182 GLU A CG    1 
ATOM   1364 C  CD    . GLU A 1 171 ? 10.49976  -12.68660 -6.47670  1.000 48.74277  ? 182 GLU A CD    1 
ATOM   1365 O  OE1   . GLU A 1 171 ? 9.74312   -12.08690 -7.26772  1.000 57.07351  ? 182 GLU A OE1   1 
ATOM   1366 O  OE2   . GLU A 1 171 ? 11.10960  -13.73505 -6.78158  1.000 50.53765  ? 182 GLU A OE2   1 
ATOM   1367 N  N     . VAL A 1 172 ? 9.97539   -16.28411 -3.35956  1.000 24.65292  ? 183 VAL A N     1 
ATOM   1368 C  CA    . VAL A 1 172 ? 10.34529  -17.38460 -2.48485  1.000 32.59672  ? 183 VAL A CA    1 
ATOM   1369 C  C     . VAL A 1 172 ? 11.61868  -17.00349 -1.71771  1.000 35.66275  ? 183 VAL A C     1 
ATOM   1370 O  O     . VAL A 1 172 ? 12.47559  -16.26110 -2.22076  1.000 33.70507  ? 183 VAL A O     1 
ATOM   1371 C  CB    . VAL A 1 172 ? 10.52227  -18.66656 -3.31753  1.000 34.30811  ? 183 VAL A CB    1 
ATOM   1372 C  CG1   . VAL A 1 172 ? 11.75035  -18.54645 -4.20828  1.000 33.97456  ? 183 VAL A CG1   1 
ATOM   1373 C  CG2   . VAL A 1 172 ? 10.59141  -19.89068 -2.42995  1.000 33.81791  ? 183 VAL A CG2   1 
ATOM   1374 N  N     . GLU A 1 173 ? 11.71940  -17.47091 -0.46608  1.000 30.33930  ? 184 GLU A N     1 
ATOM   1375 C  CA    . GLU A 1 173 ? 12.83690  -17.14937 0.41781   1.000 29.58347  ? 184 GLU A CA    1 
ATOM   1376 C  C     . GLU A 1 173 ? 13.45637  -18.42335 0.97230   1.000 31.90920  ? 184 GLU A C     1 
ATOM   1377 O  O     . GLU A 1 173 ? 12.75535  -19.38866 1.26399   1.000 30.51765  ? 184 GLU A O     1 
ATOM   1378 C  CB    . GLU A 1 173 ? 12.41655  -16.29445 1.62838   1.000 28.26972  ? 184 GLU A CB    1 
ATOM   1379 C  CG    . GLU A 1 173 ? 11.73055  -14.98867 1.31944   1.000 37.46597  ? 184 GLU A CG    1 
ATOM   1380 C  CD    . GLU A 1 173 ? 11.28106  -14.26369 2.58324   1.000 41.39387  ? 184 GLU A CD    1 
ATOM   1381 O  OE1   . GLU A 1 173 ? 11.37320  -14.85987 3.68052   1.000 35.68724  ? 184 GLU A OE1   1 
ATOM   1382 O  OE2   . GLU A 1 173 ? 10.83423  -13.09649 2.48606   1.000 45.98527  ? 184 GLU A OE2   1 
ATOM   1383 N  N     . GLU A 1 174 ? 14.76917  -18.39396 1.18099   1.000 29.55587  ? 185 GLU A N     1 
ATOM   1384 C  CA    . GLU A 1 174 ? 15.44123  -19.45017 1.92365   1.000 32.90421  ? 185 GLU A CA    1 
ATOM   1385 C  C     . GLU A 1 174 ? 15.29005  -19.20365 3.42372   1.000 28.78992  ? 185 GLU A C     1 
ATOM   1386 O  O     . GLU A 1 174 ? 15.46606  -18.08308 3.89138   1.000 32.19714  ? 185 GLU A O     1 
ATOM   1387 C  CB    . GLU A 1 174 ? 16.91576  -19.49989 1.52446   1.000 31.82006  ? 185 GLU A CB    1 
ATOM   1388 C  CG    . GLU A 1 174 ? 17.08969  -19.85745 0.05476   1.000 37.92122  ? 185 GLU A CG    1 
ATOM   1389 C  CD    . GLU A 1 174 ? 18.53906  -19.91244 -0.38053  1.000 47.18553  ? 185 GLU A CD    1 
ATOM   1390 O  OE1   . GLU A 1 174 ? 19.42789  -19.55403 0.42362   1.000 54.33258  ? 185 GLU A OE1   1 
ATOM   1391 O  OE2   . GLU A 1 174 ? 18.78510  -20.31291 -1.53765  1.000 53.46517  ? 185 GLU A OE2   1 
ATOM   1392 N  N     . THR A 1 175 ? 14.95228  -20.24036 4.18205   1.000 31.96245  ? 186 THR A N     1 
ATOM   1393 C  CA    . THR A 1 175 ? 14.77430  -20.04776 5.61540   1.000 26.20219  ? 186 THR A CA    1 
ATOM   1394 C  C     . THR A 1 175 ? 16.06327  -20.20056 6.40891   1.000 28.82707  ? 186 THR A C     1 
ATOM   1395 O  O     . THR A 1 175 ? 16.11905  -19.75501 7.55657   1.000 30.41036  ? 186 THR A O     1 
ATOM   1396 C  CB    . THR A 1 175 ? 13.75804  -21.03759 6.18144   1.000 29.71285  ? 186 THR A CB    1 
ATOM   1397 O  OG1   . THR A 1 175 ? 14.28852  -22.36352 6.07503   1.000 28.26387  ? 186 THR A OG1   1 
ATOM   1398 C  CG2   . THR A 1 175 ? 12.44092  -20.94379 5.44361   1.000 26.93640  ? 186 THR A CG2   1 
ATOM   1399 N  N     . GLY A 1 176 ? 17.09421  -20.82297 5.84443   1.000 32.79296  ? 187 GLY A N     1 
ATOM   1400 C  CA    . GLY A 1 176 ? 18.34602  -21.01193 6.55235   1.000 26.92717  ? 187 GLY A CA    1 
ATOM   1401 C  C     . GLY A 1 176 ? 18.63922  -22.43365 6.99602   1.000 32.14578  ? 187 GLY A C     1 
ATOM   1402 O  O     . GLY A 1 176 ? 19.68818  -22.66028 7.61320   1.000 30.32806  ? 187 GLY A O     1 
ATOM   1403 N  N     . THR A 1 177 ? 17.76274  -23.39635 6.71709   1.000 30.47447  ? 188 THR A N     1 
ATOM   1404 C  CA    . THR A 1 177 ? 18.06943  -24.79942 6.95063   1.000 23.88786  ? 188 THR A CA    1 
ATOM   1405 C  C     . THR A 1 177 ? 18.23140  -25.52302 5.61775   1.000 25.81125  ? 188 THR A C     1 
ATOM   1406 O  O     . THR A 1 177 ? 17.79996  -25.04984 4.56509   1.000 29.62392  ? 188 THR A O     1 
ATOM   1407 C  CB    . THR A 1 177 ? 16.98975  -25.47978 7.81055   1.000 28.31933  ? 188 THR A CB    1 
ATOM   1408 O  OG1   . THR A 1 177 ? 15.73668  -25.50298 7.12099   1.000 29.16623  ? 188 THR A OG1   1 
ATOM   1409 C  CG2   . THR A 1 177 ? 16.80610  -24.74982 9.12576   1.000 28.21066  ? 188 THR A CG2   1 
ATOM   1410 N  N     . PHE A 1 178 ? 18.86915  -26.68312 5.66463   1.000 24.95147  ? 189 PHE A N     1 
ATOM   1411 C  CA    . PHE A 1 178 ? 19.21667  -27.40216 4.45159   1.000 25.88857  ? 189 PHE A CA    1 
ATOM   1412 C  C     . PHE A 1 178 ? 18.93200  -28.87995 4.67009   1.000 27.60098  ? 189 PHE A C     1 
ATOM   1413 O  O     . PHE A 1 178 ? 19.05344  -29.38897 5.78751   1.000 26.97961  ? 189 PHE A O     1 
ATOM   1414 C  CB    . PHE A 1 178 ? 20.69217  -27.15811 4.08026   1.000 29.44678  ? 189 PHE A CB    1 
ATOM   1415 C  CG    . PHE A 1 178 ? 21.02716  -27.47684 2.65455   1.000 30.62610  ? 189 PHE A CG    1 
ATOM   1416 C  CD1   . PHE A 1 178 ? 21.38667  -28.76922 2.28131   1.000 31.34292  ? 189 PHE A CD1   1 
ATOM   1417 C  CD2   . PHE A 1 178 ? 21.01084  -26.47610 1.68393   1.000 30.97004  ? 189 PHE A CD2   1 
ATOM   1418 C  CE1   . PHE A 1 178 ? 21.70228  -29.07020 0.94998   1.000 27.13476  ? 189 PHE A CE1   1 
ATOM   1419 C  CE2   . PHE A 1 178 ? 21.32755  -26.76025 0.36207   1.000 31.01140  ? 189 PHE A CE2   1 
ATOM   1420 C  CZ    . PHE A 1 178 ? 21.67448  -28.05890 -0.00731  1.000 34.15425  ? 189 PHE A CZ    1 
ATOM   1421 N  N     . ASN A 1 179 ? 18.54689  -29.56484 3.59464   1.000 26.49330  ? 190 ASN A N     1 
ATOM   1422 C  CA    . ASN A 1 179 ? 18.12370  -30.95787 3.65598   1.000 24.98717  ? 190 ASN A CA    1 
ATOM   1423 C  C     . ASN A 1 179 ? 18.87096  -31.78037 2.62656   1.000 29.35547  ? 190 ASN A C     1 
ATOM   1424 O  O     . ASN A 1 179 ? 18.98500  -31.37827 1.46452   1.000 28.21148  ? 190 ASN A O     1 
ATOM   1425 C  CB    . ASN A 1 179 ? 16.62745  -31.08470 3.41435   1.000 24.22767  ? 190 ASN A CB    1 
ATOM   1426 C  CG    . ASN A 1 179 ? 15.85125  -30.06940 4.18824   1.000 27.63997  ? 190 ASN A CG    1 
ATOM   1427 O  OD1   . ASN A 1 179 ? 15.65066  -30.22785 5.38697   1.000 28.61206  ? 190 ASN A OD1   1 
ATOM   1428 N  ND2   . ASN A 1 179 ? 15.43482  -28.99409 3.52048   1.000 25.92483  ? 190 ASN A ND2   1 
ATOM   1429 N  N     . ILE A 1 180 ? 19.37423  -32.92546 3.06247   1.000 22.25685  ? 191 ILE A N     1 
ATOM   1430 C  CA    . ILE A 1 180 ? 19.96030  -33.93089 2.19220   1.000 26.33284  ? 191 ILE A CA    1 
ATOM   1431 C  C     . ILE A 1 180 ? 19.11505  -35.18380 2.32850   1.000 26.25804  ? 191 ILE A C     1 
ATOM   1432 O  O     . ILE A 1 180 ? 18.84906  -35.63582 3.44743   1.000 27.96442  ? 191 ILE A O     1 
ATOM   1433 C  CB    . ILE A 1 180 ? 21.42746  -34.21236 2.55672   1.000 24.24702  ? 191 ILE A CB    1 
ATOM   1434 C  CG1   . ILE A 1 180 ? 22.25088  -32.92354 2.42446   1.000 26.69120  ? 191 ILE A CG1   1 
ATOM   1435 C  CG2   . ILE A 1 180 ? 21.98451  -35.33824 1.69863   1.000 25.69764  ? 191 ILE A CG2   1 
ATOM   1436 C  CD1   . ILE A 1 180 ? 23.70416  -33.07045 2.86327   1.000 27.61073  ? 191 ILE A CD1   1 
ATOM   1437 N  N     . GLN A 1 181 ? 18.68391  -35.72902 1.19918   1.000 29.69153  ? 192 GLN A N     1 
ATOM   1438 C  CA    . GLN A 1 181 ? 17.77650  -36.86326 1.16621   1.000 24.31563  ? 192 GLN A CA    1 
ATOM   1439 C  C     . GLN A 1 181 ? 18.36132  -37.96316 0.30411   1.000 24.99314  ? 192 GLN A C     1 
ATOM   1440 O  O     . GLN A 1 181 ? 19.19720  -37.71289 -0.57124  1.000 24.62363  ? 192 GLN A O     1 
ATOM   1441 C  CB    . GLN A 1 181 ? 16.42236  -36.46692 0.59824   1.000 26.29039  ? 192 GLN A CB    1 
ATOM   1442 C  CG    . GLN A 1 181 ? 15.66326  -35.51030 1.46826   1.000 30.84052  ? 192 GLN A CG    1 
ATOM   1443 C  CD    . GLN A 1 181 ? 14.36266  -35.11421 0.82052   1.000 33.10828  ? 192 GLN A CD    1 
ATOM   1444 O  OE1   . GLN A 1 181 ? 14.26497  -34.04583 0.22048   1.000 34.55378  ? 192 GLN A OE1   1 
ATOM   1445 N  NE2   . GLN A 1 181 ? 13.35445  -35.98496 0.91586   1.000 27.46666  ? 192 GLN A NE2   1 
ATOM   1446 N  N     . ALA A 1 182 ? 17.87036  -39.17981 0.52180   1.000 21.35400  ? 193 ALA A N     1 
ATOM   1447 C  CA    . ALA A 1 182 ? 18.36499  -40.31316 -0.24041  1.000 26.84177  ? 193 ALA A CA    1 
ATOM   1448 C  C     . ALA A 1 182 ? 17.41484  -41.48991 -0.08475  1.000 27.82127  ? 193 ALA A C     1 
ATOM   1449 O  O     . ALA A 1 182 ? 16.58495  -41.53169 0.82751   1.000 25.00238  ? 193 ALA A O     1 
ATOM   1450 C  CB    . ALA A 1 182 ? 19.78423  -40.70341 0.19931   1.000 21.46714  ? 193 ALA A CB    1 
ATOM   1451 N  N     . ASP A 1 183 ? 17.54829  -42.44084 -1.00218  1.000 27.33272  ? 194 ASP A N     1 
ATOM   1452 C  CA    . ASP A 1 183 ? 16.85971  -43.72252 -0.92883  1.000 31.97018  ? 194 ASP A CA    1 
ATOM   1453 C  C     . ASP A 1 183 ? 17.88183  -44.84151 -0.81881  1.000 27.48919  ? 194 ASP A C     1 
ATOM   1454 O  O     . ASP A 1 183 ? 18.93589  -44.80156 -1.45797  1.000 30.44984  ? 194 ASP A O     1 
ATOM   1455 C  CB    . ASP A 1 183 ? 15.98096  -43.97307 -2.15740  1.000 24.28829  ? 194 ASP A CB    1 
ATOM   1456 C  CG    . ASP A 1 183 ? 14.78394  -43.03493 -2.22257  1.000 29.56923  ? 194 ASP A CG    1 
ATOM   1457 O  OD1   . ASP A 1 183 ? 14.13804  -42.81524 -1.17982  1.000 30.92305  ? 194 ASP A OD1   1 
ATOM   1458 O  OD2   . ASP A 1 183 ? 14.48837  -42.51336 -3.31583  1.000 33.72605  ? 194 ASP A OD2   1 
ATOM   1459 N  N     . ILE A 1 184 ? 17.55909  -45.83928 -0.01238  1.000 24.54387  ? 195 ILE A N     1 
ATOM   1460 C  CA    . ILE A 1 184 ? 18.30690  -47.08028 0.03641   1.000 28.25219  ? 195 ILE A CA    1 
ATOM   1461 C  C     . ILE A 1 184 ? 17.36638  -48.19800 -0.37388  1.000 30.12293  ? 195 ILE A C     1 
ATOM   1462 O  O     . ILE A 1 184 ? 16.32650  -48.40770 0.26177   1.000 29.48937  ? 195 ILE A O     1 
ATOM   1463 C  CB    . ILE A 1 184 ? 18.89460  -47.33988 1.42633   1.000 27.87508  ? 195 ILE A CB    1 
ATOM   1464 C  CG1   . ILE A 1 184 ? 19.90107  -46.23297 1.75562   1.000 28.26216  ? 195 ILE A CG1   1 
ATOM   1465 C  CG2   . ILE A 1 184 ? 19.53146  -48.73590 1.45953   1.000 24.95549  ? 195 ILE A CG2   1 
ATOM   1466 C  CD1   . ILE A 1 184 ? 20.66922  -46.47958 2.99715   1.000 29.72509  ? 195 ILE A CD1   1 
ATOM   1467 N  N     . HIS A 1 185 ? 17.73110  -48.91556 -1.42473  1.000 31.88413  ? 196 HIS A N     1 
ATOM   1468 C  CA    . HIS A 1 185 ? 16.94962  -50.04937 -1.87565  1.000 30.72567  ? 196 HIS A CA    1 
ATOM   1469 C  C     . HIS A 1 185 ? 17.38466  -51.28867 -1.10624  1.000 32.27772  ? 196 HIS A C     1 
ATOM   1470 O  O     . HIS A 1 185 ? 18.54457  -51.41381 -0.70449  1.000 36.34276  ? 196 HIS A O     1 
ATOM   1471 C  CB    . HIS A 1 185 ? 17.10851  -50.20855 -3.38789  1.000 38.27522  ? 196 HIS A CB    1 
ATOM   1472 C  CG    . HIS A 1 185 ? 16.87681  -48.92638 -4.12938  1.000 52.14792  ? 196 HIS A CG    1 
ATOM   1473 N  ND1   . HIS A 1 185 ? 15.66975  -48.25872 -4.09212  1.000 51.43964  ? 196 HIS A ND1   1 
ATOM   1474 C  CD2   . HIS A 1 185 ? 17.71132  -48.15057 -4.86322  1.000 54.25153  ? 196 HIS A CD2   1 
ATOM   1475 C  CE1   . HIS A 1 185 ? 15.75992  -47.14429 -4.79609  1.000 46.75726  ? 196 HIS A CE1   1 
ATOM   1476 N  NE2   . HIS A 1 185 ? 16.98872  -47.05393 -5.27399  1.000 58.20624  ? 196 HIS A NE2   1 
ATOM   1477 N  N     . HIS A 1 186 ? 16.43043  -52.17873 -0.85798  1.000 34.75513  ? 197 HIS A N     1 
ATOM   1478 C  CA    . HIS A 1 186 ? 16.63618  -53.35584 -0.01937  1.000 36.36021  ? 197 HIS A CA    1 
ATOM   1479 C  C     . HIS A 1 186 ? 17.38142  -53.01155 1.27403   1.000 35.26838  ? 197 HIS A C     1 
ATOM   1480 O  O     . HIS A 1 186 ? 18.48878  -53.51105 1.51200   1.000 37.04863  ? 197 HIS A O     1 
ATOM   1481 C  CB    . HIS A 1 186 ? 17.36755  -54.44089 -0.79634  1.000 41.71821  ? 197 HIS A CB    1 
ATOM   1482 C  CG    . HIS A 1 186 ? 16.67026  -54.84590 -2.05840  1.000 50.12345  ? 197 HIS A CG    1 
ATOM   1483 N  ND1   . HIS A 1 186 ? 17.14934  -54.52552 -3.31066  1.000 54.44360  ? 197 HIS A ND1   1 
ATOM   1484 C  CD2   . HIS A 1 186 ? 15.51811  -55.52936 -2.25923  1.000 54.38240  ? 197 HIS A CD2   1 
ATOM   1485 C  CE1   . HIS A 1 186 ? 16.32731  -55.00190 -4.22915  1.000 61.17620  ? 197 HIS A CE1   1 
ATOM   1486 N  NE2   . HIS A 1 186 ? 15.32985  -55.61597 -3.61746  1.000 64.28142  ? 197 HIS A NE2   1 
ATOM   1487 N  N     . PRO A 1 187 ? 16.81437  -52.15109 2.12141   1.000 32.54111  ? 198 PRO A N     1 
ATOM   1488 C  CA    . PRO A 1 187 ? 17.54986  -51.73382 3.32820   1.000 31.19632  ? 198 PRO A CA    1 
ATOM   1489 C  C     . PRO A 1 187 ? 17.78274  -52.86560 4.31177   1.000 36.31386  ? 198 PRO A C     1 
ATOM   1490 O  O     . PRO A 1 187 ? 18.78083  -52.83955 5.04425   1.000 34.82955  ? 198 PRO A O     1 
ATOM   1491 C  CB    . PRO A 1 187 ? 16.65629  -50.64099 3.92614   1.000 29.04179  ? 198 PRO A CB    1 
ATOM   1492 C  CG    . PRO A 1 187 ? 15.26487  -50.94986 3.37791   1.000 35.21702  ? 198 PRO A CG    1 
ATOM   1493 C  CD    . PRO A 1 187 ? 15.48935  -51.50467 2.00910   1.000 32.37945  ? 198 PRO A CD    1 
ATOM   1494 N  N     . GLU A 1 188 ? 16.90084  -53.86785 4.34176   1.000 32.00028  ? 199 GLU A N     1 
ATOM   1495 C  CA    . GLU A 1 188 ? 17.10937  -55.00784 5.22228   1.000 35.54421  ? 199 GLU A CA    1 
ATOM   1496 C  C     . GLU A 1 188 ? 18.43310  -55.70763 4.93079   1.000 38.25703  ? 199 GLU A C     1 
ATOM   1497 O  O     . GLU A 1 188 ? 18.99283  -56.35765 5.82024   1.000 40.50892  ? 199 GLU A O     1 
ATOM   1498 C  CB    . GLU A 1 188 ? 15.92717  -55.97700 5.09598   1.000 37.64576  ? 199 GLU A CB    1 
ATOM   1499 C  CG    . GLU A 1 188 ? 15.90643  -56.82163 3.81956   1.000 40.48107  ? 199 GLU A CG    1 
ATOM   1500 C  CD    . GLU A 1 188 ? 15.51755  -56.03532 2.56125   1.000 55.19522  ? 199 GLU A CD    1 
ATOM   1501 O  OE1   . GLU A 1 188 ? 14.91672  -54.93777 2.67321   1.000 41.87437  ? 199 GLU A OE1   1 
ATOM   1502 O  OE2   . GLU A 1 188 ? 15.81242  -56.53253 1.44872   1.000 58.36328  ? 199 GLU A OE2   1 
ATOM   1503 N  N     . VAL A 1 189 ? 18.95513  -55.55833 3.71660   1.000 38.70696  ? 200 VAL A N     1 
ATOM   1504 C  CA    . VAL A 1 189 ? 20.25468  -56.09421 3.34055   1.000 37.08690  ? 200 VAL A CA    1 
ATOM   1505 C  C     . VAL A 1 189 ? 21.33858  -55.02291 3.37598   1.000 38.12345  ? 200 VAL A C     1 
ATOM   1506 O  O     . VAL A 1 189 ? 22.44468  -55.27848 3.84898   1.000 39.86138  ? 200 VAL A O     1 
ATOM   1507 C  CB    . VAL A 1 189 ? 20.16862  -56.74342 1.94177   1.000 38.79725  ? 200 VAL A CB    1 
ATOM   1508 C  CG1   . VAL A 1 189 ? 21.53349  -57.24371 1.50425   1.000 43.65391  ? 200 VAL A CG1   1 
ATOM   1509 C  CG2   . VAL A 1 189 ? 19.13935  -57.87054 1.93234   1.000 42.62682  ? 200 VAL A CG2   1 
ATOM   1510 N  N     . ASN A 1 190 ? 21.03683  -53.81216 2.89643   1.000 35.62584  ? 201 ASN A N     1 
ATOM   1511 C  CA    . ASN A 1 190 ? 22.07595  -52.81339 2.65508   1.000 38.08741  ? 201 ASN A CA    1 
ATOM   1512 C  C     . ASN A 1 190 ? 22.35721  -51.91136 3.84736   1.000 32.27257  ? 201 ASN A C     1 
ATOM   1513 O  O     . ASN A 1 190 ? 23.49368  -51.45516 3.99514   1.000 33.91264  ? 201 ASN A O     1 
ATOM   1514 C  CB    . ASN A 1 190 ? 21.71904  -51.96514 1.43248   1.000 38.46998  ? 201 ASN A CB    1 
ATOM   1515 C  CG    . ASN A 1 190 ? 22.00360  -52.69318 0.13220   1.000 41.11950  ? 201 ASN A CG    1 
ATOM   1516 O  OD1   . ASN A 1 190 ? 23.03148  -53.35201 -0.00609  1.000 38.76933  ? 201 ASN A OD1   1 
ATOM   1517 N  ND2   . ASN A 1 190 ? 21.08862  -52.59458 -0.81406  1.000 41.33017  ? 201 ASN A ND2   1 
ATOM   1518 N  N     . CYS A 1 191 ? 21.37339  -51.64383 4.70821   1.000 35.80463  ? 202 CYS A N     1 
ATOM   1519 C  CA    . CYS A 1 191 ? 21.62054  -51.01118 6.00864   1.000 33.78398  ? 202 CYS A CA    1 
ATOM   1520 C  C     . CYS A 1 191 ? 20.89126  -51.77364 7.11124   1.000 33.56478  ? 202 CYS A C     1 
ATOM   1521 O  O     . CYS A 1 191 ? 20.01751  -51.22662 7.78808   1.000 29.81506  ? 202 CYS A O     1 
ATOM   1522 C  CB    . CYS A 1 191 ? 21.21526  -49.53773 5.99370   1.000 27.02472  ? 202 CYS A CB    1 
ATOM   1523 S  SG    . CYS A 1 191 ? 19.53900  -49.21757 5.46577   1.000 28.92818  ? 202 CYS A SG    1 
ATOM   1524 N  N     . PRO A 1 192 ? 21.27523  -53.03759 7.35429   1.000 32.77488  ? 203 PRO A N     1 
ATOM   1525 C  CA    . PRO A 1 192 ? 20.48116  -53.88544 8.26593   1.000 33.26068  ? 203 PRO A CA    1 
ATOM   1526 C  C     . PRO A 1 192 ? 20.34304  -53.33807 9.67890   1.000 35.33136  ? 203 PRO A C     1 
ATOM   1527 O  O     . PRO A 1 192 ? 19.24673  -53.40080 10.25242  1.000 33.40901  ? 203 PRO A O     1 
ATOM   1528 C  CB    . PRO A 1 192 ? 21.23608  -55.23123 8.24421   1.000 33.53377  ? 203 PRO A CB    1 
ATOM   1529 C  CG    . PRO A 1 192 ? 22.59458  -54.92651 7.69430   1.000 36.63836  ? 203 PRO A CG    1 
ATOM   1530 C  CD    . PRO A 1 192 ? 22.40329  -53.77087 6.75406   1.000 33.31195  ? 203 PRO A CD    1 
ATOM   1531 N  N     . GLY A 1 193 ? 21.41653  -52.79677 10.25569  1.000 31.24485  ? 204 GLY A N     1 
ATOM   1532 C  CA    . GLY A 1 193 ? 21.33431  -52.29678 11.61984  1.000 28.40205  ? 204 GLY A CA    1 
ATOM   1533 C  C     . GLY A 1 193 ? 20.35396  -51.15015 11.76812  1.000 34.50023  ? 204 GLY A C     1 
ATOM   1534 O  O     . GLY A 1 193 ? 19.55036  -51.11683 12.70508  1.000 34.01661  ? 204 GLY A O     1 
ATOM   1535 N  N     . PHE A 1 194 ? 20.40799  -50.18611 10.84793  1.000 32.68256  ? 205 PHE A N     1 
ATOM   1536 C  CA    . PHE A 1 194 ? 19.48693  -49.05913 10.93823  1.000 28.40970  ? 205 PHE A CA    1 
ATOM   1537 C  C     . PHE A 1 194 ? 18.07057  -49.49848 10.60710  1.000 31.24261  ? 205 PHE A C     1 
ATOM   1538 O  O     . PHE A 1 194 ? 17.10357  -49.00584 11.19727  1.000 30.20563  ? 205 PHE A O     1 
ATOM   1539 C  CB    . PHE A 1 194 ? 19.92465  -47.91894 10.01634  1.000 26.49228  ? 205 PHE A CB    1 
ATOM   1540 C  CG    . PHE A 1 194 ? 19.03953  -46.71685 10.10474  1.000 28.76275  ? 205 PHE A CG    1 
ATOM   1541 C  CD1   . PHE A 1 194 ? 19.14908  -45.83760 11.17353  1.000 29.55626  ? 205 PHE A CD1   1 
ATOM   1542 C  CD2   . PHE A 1 194 ? 18.06104  -46.48677 9.14710   1.000 30.69007  ? 205 PHE A CD2   1 
ATOM   1543 C  CE1   . PHE A 1 194 ? 18.31430  -44.73096 11.27308  1.000 24.14739  ? 205 PHE A CE1   1 
ATOM   1544 C  CE2   . PHE A 1 194 ? 17.22531  -45.38620 9.23579   1.000 30.00341  ? 205 PHE A CE2   1 
ATOM   1545 C  CZ    . PHE A 1 194 ? 17.35237  -44.50648 10.29129  1.000 27.06963  ? 205 PHE A CZ    1 
ATOM   1546 N  N     . PHE A 1 195 ? 17.93276  -50.42810 9.66584   1.000 35.99373  ? 206 PHE A N     1 
ATOM   1547 C  CA    . PHE A 1 195 ? 16.61982  -50.97428 9.35234   1.000 33.98708  ? 206 PHE A CA    1 
ATOM   1548 C  C     . PHE A 1 195 ? 16.00250  -51.63840 10.58100  1.000 33.89422  ? 206 PHE A C     1 
ATOM   1549 O  O     . PHE A 1 195 ? 14.82342  -51.43149 10.89257  1.000 32.37627  ? 206 PHE A O     1 
ATOM   1550 C  CB    . PHE A 1 195 ? 16.74504  -51.96372 8.19227   1.000 30.10178  ? 206 PHE A CB    1 
ATOM   1551 C  CG    . PHE A 1 195 ? 15.43530  -52.54698 7.75363   1.000 35.90453  ? 206 PHE A CG    1 
ATOM   1552 C  CD1   . PHE A 1 195 ? 14.57448  -51.81557 6.93960   1.000 30.94209  ? 206 PHE A CD1   1 
ATOM   1553 C  CD2   . PHE A 1 195 ? 15.06696  -53.82628 8.14818   1.000 31.83156  ? 206 PHE A CD2   1 
ATOM   1554 C  CE1   . PHE A 1 195 ? 13.36018  -52.34545 6.53116   1.000 33.10326  ? 206 PHE A CE1   1 
ATOM   1555 C  CE2   . PHE A 1 195 ? 13.85748  -54.36654 7.74550   1.000 34.17570  ? 206 PHE A CE2   1 
ATOM   1556 C  CZ    . PHE A 1 195 ? 13.00052  -53.62501 6.93317   1.000 32.40899  ? 206 PHE A CZ    1 
ATOM   1557 N  N     . GLN A 1 196 ? 16.79577  -52.43135 11.30492  1.000 33.82579  ? 207 GLN A N     1 
ATOM   1558 C  CA    . GLN A 1 196 ? 16.29185  -53.06029 12.51966  1.000 33.88626  ? 207 GLN A CA    1 
ATOM   1559 C  C     . GLN A 1 196 ? 15.96702  -52.02053 13.58571  1.000 34.21423  ? 207 GLN A C     1 
ATOM   1560 O  O     . GLN A 1 196 ? 14.98618  -52.16294 14.32765  1.000 39.05215  ? 207 GLN A O     1 
ATOM   1561 C  CB    . GLN A 1 196 ? 17.30145  -54.08155 13.02628  1.000 37.86242  ? 207 GLN A CB    1 
ATOM   1562 C  CG    . GLN A 1 196 ? 17.40171  -55.29434 12.10959  1.000 42.47753  ? 207 GLN A CG    1 
ATOM   1563 C  CD    . GLN A 1 196 ? 18.69924  -56.06473 12.29392  1.000 49.24184  ? 207 GLN A CD    1 
ATOM   1564 O  OE1   . GLN A 1 196 ? 19.32083  -56.01575 13.35690  1.000 55.96627  ? 207 GLN A OE1   1 
ATOM   1565 N  NE2   . GLN A 1 196 ? 19.11663  -56.77610 11.25313  1.000 42.90003  ? 207 GLN A NE2   1 
ATOM   1566 N  N     . LEU A 1 197 ? 16.75584  -50.94818 13.65299  1.000 36.19050  ? 208 LEU A N     1 
ATOM   1567 C  CA    . LEU A 1 197 ? 16.45788  -49.87722 14.59614  1.000 34.05546  ? 208 LEU A CA    1 
ATOM   1568 C  C     . LEU A 1 197 ? 15.08249  -49.28009 14.33479  1.000 31.72098  ? 208 LEU A C     1 
ATOM   1569 O  O     . LEU A 1 197 ? 14.31905  -49.01937 15.27432  1.000 31.81716  ? 208 LEU A O     1 
ATOM   1570 C  CB    . LEU A 1 197 ? 17.52874  -48.79513 14.51639  1.000 33.77060  ? 208 LEU A CB    1 
ATOM   1571 C  CG    . LEU A 1 197 ? 17.48990  -47.73004 15.60779  1.000 37.69207  ? 208 LEU A CG    1 
ATOM   1572 C  CD1   . LEU A 1 197 ? 17.72983  -48.36970 16.98238  1.000 33.84022  ? 208 LEU A CD1   1 
ATOM   1573 C  CD2   . LEU A 1 197 ? 18.53654  -46.66509 15.32022  1.000 33.83142  ? 208 LEU A CD2   1 
ATOM   1574 N  N     . CYS A 1 198 ? 14.74512  -49.05263 13.06701  1.000 29.72356  ? 209 CYS A N     1 
ATOM   1575 C  CA    . CYS A 1 198 ? 13.42181  -48.51806 12.75771  1.000 33.70845  ? 209 CYS A CA    1 
ATOM   1576 C  C     . CYS A 1 198 ? 12.33580  -49.50007 13.18506  1.000 37.03153  ? 209 CYS A C     1 
ATOM   1577 O  O     . CYS A 1 198 ? 11.35010  -49.11549 13.82786  1.000 39.97703  ? 209 CYS A O     1 
ATOM   1578 C  CB    . CYS A 1 198 ? 13.31214  -48.19347 11.26466  1.000 29.86894  ? 209 CYS A CB    1 
ATOM   1579 S  SG    . CYS A 1 198 ? 14.39927  -46.85912 10.66950  1.000 31.84089  ? 209 CYS A SG    1 
ATOM   1580 N  N     . ASN A 1 199 ? 12.51193  -50.78024 12.84733  1.000 37.57537  ? 210 ASN A N     1 
ATOM   1581 C  CA    . ASN A 1 199 ? 11.62642  -51.84900 13.30727  1.000 39.11035  ? 210 ASN A CA    1 
ATOM   1582 C  C     . ASN A 1 199 ? 10.18445  -51.58022 12.88142  1.000 37.89738  ? 210 ASN A C     1 
ATOM   1583 O  O     . ASN A 1 199 ? 9.25937   -51.57614 13.69233  1.000 37.13876  ? 210 ASN A O     1 
ATOM   1584 C  CB    . ASN A 1 199 ? 11.73184  -52.02807 14.82391  1.000 40.95196  ? 210 ASN A CB    1 
ATOM   1585 C  CG    . ASN A 1 199 ? 11.12057  -53.32585 15.29979  1.000 46.49109  ? 210 ASN A CG    1 
ATOM   1586 O  OD1   . ASN A 1 199 ? 11.05800  -54.30205 14.55321  1.000 49.12832  ? 210 ASN A OD1   1 
ATOM   1587 N  ND2   . ASN A 1 199 ? 10.65966  -53.34382 16.54865  1.000 42.21433  ? 210 ASN A ND2   1 
ATOM   1588 N  N     . GLY A 1 200 ? 10.00550  -51.32867 11.58806  1.000 35.33460  ? 211 GLY A N     1 
ATOM   1589 C  CA    . GLY A 1 200 ? 8.69754   -51.08071 11.02697  1.000 32.76724  ? 211 GLY A CA    1 
ATOM   1590 C  C     . GLY A 1 200 ? 8.15449   -49.68495 11.23047  1.000 36.28992  ? 211 GLY A C     1 
ATOM   1591 O  O     . GLY A 1 200 ? 7.15452   -49.33272 10.58990  1.000 35.11626  ? 211 GLY A O     1 
ATOM   1592 N  N     . ASN A 1 201 ? 8.77166   -48.87206 12.08618  1.000 34.15418  ? 212 ASN A N     1 
ATOM   1593 C  CA    . ASN A 1 201 ? 8.28140   -47.52847 12.35560  1.000 32.95388  ? 212 ASN A CA    1 
ATOM   1594 C  C     . ASN A 1 201 ? 9.12739   -46.48666 11.64107  1.000 28.16856  ? 212 ASN A C     1 
ATOM   1595 O  O     . ASN A 1 201 ? 10.30586  -46.70904 11.36532  1.000 30.76020  ? 212 ASN A O     1 
ATOM   1596 C  CB    . ASN A 1 201 ? 8.27798   -47.23369 13.85907  1.000 31.58568  ? 212 ASN A CB    1 
ATOM   1597 C  CG    . ASN A 1 201 ? 7.13197   -47.92272 14.58948  1.000 39.37263  ? 212 ASN A CG    1 
ATOM   1598 O  OD1   . ASN A 1 201 ? 6.18619   -48.41875 13.97044  1.000 34.03627  ? 212 ASN A OD1   1 
ATOM   1599 N  ND2   . ASN A 1 201 ? 7.21190   -47.94808 15.91290  1.000 37.22193  ? 212 ASN A ND2   1 
ATOM   1600 N  N     . ARG A 1 202 ? 8.51904   -45.33572 11.35296  1.000 29.71553  ? 213 ARG A N     1 
ATOM   1601 C  CA    . ARG A 1 202 ? 9.31775   -44.15738 11.04393  1.000 31.94801  ? 213 ARG A CA    1 
ATOM   1602 C  C     . ARG A 1 202 ? 10.21834  -43.82935 12.23161  1.000 30.16151  ? 213 ARG A C     1 
ATOM   1603 O  O     . ARG A 1 202 ? 9.91782   -44.16675 13.37897  1.000 30.72290  ? 213 ARG A O     1 
ATOM   1604 C  CB    . ARG A 1 202 ? 8.41879   -42.96577 10.70039  1.000 28.71932  ? 213 ARG A CB    1 
ATOM   1605 C  CG    . ARG A 1 202 ? 8.01278   -42.93828 9.24028   1.000 35.58429  ? 213 ARG A CG    1 
ATOM   1606 C  CD    . ARG A 1 202 ? 6.89716   -41.94458 8.93872   1.000 42.84455  ? 213 ARG A CD    1 
ATOM   1607 N  NE    . ARG A 1 202 ? 5.69759   -42.23675 9.70681   1.000 51.89632  ? 213 ARG A NE    1 
ATOM   1608 C  CZ    . ARG A 1 202 ? 5.19360   -41.44708 10.64415  1.000 54.33719  ? 213 ARG A CZ    1 
ATOM   1609 N  NH1   . ARG A 1 202 ? 5.75310   -40.28417 10.94385  1.000 52.88448  ? 213 ARG A NH1   1 
ATOM   1610 N  NH2   . ARG A 1 202 ? 4.09401   -41.82953 11.28862  1.000 49.64554  ? 213 ARG A NH2   1 
ATOM   1611 N  N     . LEU A 1 203 ? 11.34507  -43.18621 11.95388  1.000 28.32839  ? 214 LEU A N     1 
ATOM   1612 C  CA    . LEU A 1 203 ? 12.31713  -42.86817 12.99252  1.000 26.76952  ? 214 LEU A CA    1 
ATOM   1613 C  C     . LEU A 1 203 ? 12.75549  -41.41285 12.87611  1.000 30.79863  ? 214 LEU A C     1 
ATOM   1614 O  O     . LEU A 1 203 ? 12.94993  -40.89380 11.77188  1.000 30.19083  ? 214 LEU A O     1 
ATOM   1615 C  CB    . LEU A 1 203 ? 13.54442  -43.80358 12.91318  1.000 24.44328  ? 214 LEU A CB    1 
ATOM   1616 C  CG    . LEU A 1 203 ? 14.63717  -43.60932 13.98229  1.000 27.10001  ? 214 LEU A CG    1 
ATOM   1617 C  CD1   . LEU A 1 203 ? 15.22313  -44.95621 14.37472  1.000 28.01504  ? 214 LEU A CD1   1 
ATOM   1618 C  CD2   . LEU A 1 203 ? 15.75064  -42.66769 13.51478  1.000 26.25737  ? 214 LEU A CD2   1 
ATOM   1619 N  N     . MET A 1 204 ? 12.91060  -40.75751 14.01929  1.000 26.97055  ? 215 MET A N     1 
ATOM   1620 C  CA    . MET A 1 204 ? 13.45580  -39.41038 14.07743  1.000 31.92199  ? 215 MET A CA    1 
ATOM   1621 C  C     . MET A 1 204 ? 14.49728  -39.35188 15.18218  1.000 31.72631  ? 215 MET A C     1 
ATOM   1622 O  O     . MET A 1 204 ? 14.34929  -40.00382 16.21865  1.000 29.20569  ? 215 MET A O     1 
ATOM   1623 C  CB    . MET A 1 204 ? 12.36830  -38.37362 14.33509  1.000 31.08571  ? 215 MET A CB    1 
ATOM   1624 C  CG    . MET A 1 204 ? 11.28409  -38.37705 13.29428  1.000 42.00202  ? 215 MET A CG    1 
ATOM   1625 S  SD    . MET A 1 204 ? 10.06259  -37.12167 13.66070  1.000 43.29474  ? 215 MET A SD    1 
ATOM   1626 C  CE    . MET A 1 204 ? 9.23811   -37.85665 15.06659  1.000 27.65564  ? 215 MET A CE    1 
ATOM   1627 N  N     . ALA A 1 205 ? 15.54647  -38.57207 14.95180  1.000 25.98082  ? 216 ALA A N     1 
ATOM   1628 C  CA    . ALA A 1 205 ? 16.61978  -38.40448 15.91987  1.000 27.66951  ? 216 ALA A CA    1 
ATOM   1629 C  C     . ALA A 1 205 ? 17.22865  -37.02641 15.72107  1.000 29.34403  ? 216 ALA A C     1 
ATOM   1630 O  O     . ALA A 1 205 ? 17.30099  -36.52660 14.59418  1.000 31.02071  ? 216 ALA A O     1 
ATOM   1631 C  CB    . ALA A 1 205 ? 17.70175  -39.48781 15.76917  1.000 23.22155  ? 216 ALA A CB    1 
ATOM   1632 N  N     . ALA A 1 206 ? 17.67033  -36.41755 16.82170  1.000 30.79815  ? 217 ALA A N     1 
ATOM   1633 C  CA    . ALA A 1 206 ? 18.27126  -35.09087 16.78869  1.000 30.57577  ? 217 ALA A CA    1 
ATOM   1634 C  C     . ALA A 1 206 ? 19.45225  -35.04351 17.74639  1.000 30.52437  ? 217 ALA A C     1 
ATOM   1635 O  O     . ALA A 1 206 ? 19.35623  -35.53674 18.87083  1.000 35.78477  ? 217 ALA A O     1 
ATOM   1636 C  CB    . ALA A 1 206 ? 17.24574  -34.01222 17.15916  1.000 36.77812  ? 217 ALA A CB    1 
ATOM   1637 N  N     . HIS A 1 207 ? 20.55816  -34.44525 17.30454  1.000 29.98311  ? 218 HIS A N     1 
ATOM   1638 C  CA    . HIS A 1 207 ? 21.76177  -34.33571 18.12800  1.000 30.59030  ? 218 HIS A CA    1 
ATOM   1639 C  C     . HIS A 1 207 ? 22.60045  -33.18809 17.59781  1.000 34.69099  ? 218 HIS A C     1 
ATOM   1640 O  O     . HIS A 1 207 ? 23.04710  -33.24080 16.44738  1.000 30.70629  ? 218 HIS A O     1 
ATOM   1641 C  CB    . HIS A 1 207 ? 22.57020  -35.63935 18.09679  1.000 31.32438  ? 218 HIS A CB    1 
ATOM   1642 C  CG    . HIS A 1 207 ? 23.81566  -35.60910 18.92737  1.000 31.24057  ? 218 HIS A CG    1 
ATOM   1643 N  ND1   . HIS A 1 207 ? 23.79370  -35.47539 20.29950  1.000 39.17371  ? 218 HIS A ND1   1 
ATOM   1644 C  CD2   . HIS A 1 207 ? 25.12167  -35.73055 18.58313  1.000 35.42951  ? 218 HIS A CD2   1 
ATOM   1645 C  CE1   . HIS A 1 207 ? 25.03172  -35.50927 20.76424  1.000 36.81478  ? 218 HIS A CE1   1 
ATOM   1646 N  NE2   . HIS A 1 207 ? 25.85572  -35.66230 19.74287  1.000 36.55496  ? 218 HIS A NE2   1 
ATOM   1647 N  N     . GLN A 1 208 ? 22.80369  -32.15917 18.42485  1.000 35.32371  ? 219 GLN A N     1 
ATOM   1648 C  CA    . GLN A 1 208 ? 23.73024  -31.06101 18.13124  1.000 32.30934  ? 219 GLN A CA    1 
ATOM   1649 C  C     . GLN A 1 208 ? 23.43334  -30.40449 16.78363  1.000 35.11093  ? 219 GLN A C     1 
ATOM   1650 O  O     . GLN A 1 208 ? 24.33384  -30.12064 15.99270  1.000 39.93891  ? 219 GLN A O     1 
ATOM   1651 C  CB    . GLN A 1 208 ? 25.18178  -31.54165 18.20129  1.000 37.91154  ? 219 GLN A CB    1 
ATOM   1652 C  CG    . GLN A 1 208 ? 25.59108  -31.98765 19.60095  1.000 40.02861  ? 219 GLN A CG    1 
ATOM   1653 C  CD    . GLN A 1 208 ? 27.01896  -32.50138 19.67859  1.000 51.92757  ? 219 GLN A CD    1 
ATOM   1654 O  OE1   . GLN A 1 208 ? 27.63067  -32.84329 18.66303  1.000 62.17232  ? 219 GLN A OE1   1 
ATOM   1655 N  NE2   . GLN A 1 208 ? 27.55766  -32.56060 20.89284  1.000 43.88020  ? 219 GLN A NE2   1 
ATOM   1656 N  N     . GLY A 1 209 ? 22.15157  -30.14978 16.52924  1.000 36.51240  ? 220 GLY A N     1 
ATOM   1657 C  CA    . GLY A 1 209 ? 21.75740  -29.37235 15.37891  1.000 35.29265  ? 220 GLY A CA    1 
ATOM   1658 C  C     . GLY A 1 209 ? 21.58022  -30.16508 14.10666  1.000 38.76099  ? 220 GLY A C     1 
ATOM   1659 O  O     . GLY A 1 209 ? 21.20177  -29.58717 13.08124  1.000 31.27397  ? 220 GLY A O     1 
ATOM   1660 N  N     . ASN A 1 210 ? 21.85008  -31.46258 14.12892  1.000 34.85385  ? 221 ASN A N     1 
ATOM   1661 C  CA    . ASN A 1 210 ? 21.59616  -32.32860 12.98629  1.000 30.24311  ? 221 ASN A CA    1 
ATOM   1662 C  C     . ASN A 1 210 ? 20.35917  -33.15878 13.28375  1.000 29.31154  ? 221 ASN A C     1 
ATOM   1663 O  O     . ASN A 1 210 ? 20.24465  -33.74782 14.36233  1.000 33.74546  ? 221 ASN A O     1 
ATOM   1664 C  CB    . ASN A 1 210 ? 22.80371  -33.22633 12.69816  1.000 31.80410  ? 221 ASN A CB    1 
ATOM   1665 C  CG    . ASN A 1 210 ? 23.94987  -32.46129 12.06744  1.000 37.80034  ? 221 ASN A CG    1 
ATOM   1666 O  OD1   . ASN A 1 210 ? 23.73077  -31.58272 11.23591  1.000 32.50730  ? 221 ASN A OD1   1 
ATOM   1667 N  ND2   . ASN A 1 210 ? 25.17449  -32.76985 12.47563  1.000 37.46817  ? 221 ASN A ND2   1 
ATOM   1668 N  N     . LEU A 1 211 ? 19.42442  -33.17206 12.34628  1.000 29.01638  ? 222 LEU A N     1 
ATOM   1669 C  CA    . LEU A 1 211 ? 18.21803  -33.97559 12.44431  1.000 30.65198  ? 222 LEU A CA    1 
ATOM   1670 C  C     . LEU A 1 211 ? 18.27346  -35.07676 11.40067  1.000 27.32137  ? 222 LEU A C     1 
ATOM   1671 O  O     . LEU A 1 211 ? 18.75916  -34.85947 10.28731  1.000 26.73152  ? 222 LEU A O     1 
ATOM   1672 C  CB    . LEU A 1 211 ? 16.95913  -33.12626 12.22663  1.000 29.07563  ? 222 LEU A CB    1 
ATOM   1673 C  CG    . LEU A 1 211 ? 16.37596  -32.33717 13.39743  1.000 36.17473  ? 222 LEU A CG    1 
ATOM   1674 C  CD1   . LEU A 1 211 ? 17.46396  -31.68303 14.25123  1.000 34.24371  ? 222 LEU A CD1   1 
ATOM   1675 C  CD2   . LEU A 1 211 ? 15.42363  -31.28101 12.84147  1.000 40.92957  ? 222 LEU A CD2   1 
ATOM   1676 N  N     . LEU A 1 212 ? 17.77023  -36.24913 11.76697  1.000 23.85306  ? 223 LEU A N     1 
ATOM   1677 C  CA    . LEU A 1 212 ? 17.61721  -37.37316 10.85535  1.000 27.07119  ? 223 LEU A CA    1 
ATOM   1678 C  C     . LEU A 1 212 ? 16.18422  -37.87674 10.91598  1.000 28.33155  ? 223 LEU A C     1 
ATOM   1679 O  O     . LEU A 1 212 ? 15.68568  -38.20071 11.99918  1.000 28.20688  ? 223 LEU A O     1 
ATOM   1680 C  CB    . LEU A 1 212 ? 18.57108  -38.52217 11.20400  1.000 25.15608  ? 223 LEU A CB    1 
ATOM   1681 C  CG    . LEU A 1 212 ? 18.49891  -39.70804 10.23254  1.000 30.04223  ? 223 LEU A CG    1 
ATOM   1682 C  CD1   . LEU A 1 212 ? 19.85019  -39.95390 9.60742   1.000 27.44394  ? 223 LEU A CD1   1 
ATOM   1683 C  CD2   . LEU A 1 212 ? 18.01133  -40.97527 10.92913  1.000 33.82127  ? 223 LEU A CD2   1 
ATOM   1684 N  N     . PHE A 1 213 ? 15.53742  -37.95726 9.75425   1.000 24.62268  ? 224 PHE A N     1 
ATOM   1685 C  CA    . PHE A 1 213 ? 14.23920  -38.59981 9.59989   1.000 27.50076  ? 224 PHE A CA    1 
ATOM   1686 C  C     . PHE A 1 213 ? 14.39956  -39.79688 8.67617   1.000 27.80324  ? 224 PHE A C     1 
ATOM   1687 O  O     . PHE A 1 213 ? 15.21039  -39.76997 7.74389   1.000 30.74475  ? 224 PHE A O     1 
ATOM   1688 C  CB    . PHE A 1 213 ? 13.18209  -37.66010 8.98887   1.000 30.12242  ? 224 PHE A CB    1 
ATOM   1689 C  CG    . PHE A 1 213 ? 13.08122  -36.31084 9.65260   1.000 36.62135  ? 224 PHE A CG    1 
ATOM   1690 C  CD1   . PHE A 1 213 ? 13.91018  -35.26937 9.26677   1.000 35.18537  ? 224 PHE A CD1   1 
ATOM   1691 C  CD2   . PHE A 1 213 ? 12.12162  -36.06830 10.62221  1.000 39.80572  ? 224 PHE A CD2   1 
ATOM   1692 C  CE1   . PHE A 1 213 ? 13.80874  -34.03082 9.85654   1.000 34.69499  ? 224 PHE A CE1   1 
ATOM   1693 C  CE2   . PHE A 1 213 ? 12.01604  -34.82223 11.21068  1.000 36.39472  ? 224 PHE A CE2   1 
ATOM   1694 C  CZ    . PHE A 1 213 ? 12.86420  -33.80967 10.82881  1.000 38.54875  ? 224 PHE A CZ    1 
ATOM   1695 N  N     . ALA A 1 214 ? 13.60937  -40.84124 8.91036   1.000 23.40923  ? 225 ALA A N     1 
ATOM   1696 C  CA    . ALA A 1 214 ? 13.67840  -42.00945 8.04596   1.000 25.54225  ? 225 ALA A CA    1 
ATOM   1697 C  C     . ALA A 1 214 ? 12.34040  -42.73032 8.00917   1.000 27.19670  ? 225 ALA A C     1 
ATOM   1698 O  O     . ALA A 1 214 ? 11.63758  -42.82720 9.01907   1.000 29.36985  ? 225 ALA A O     1 
ATOM   1699 C  CB    . ALA A 1 214 ? 14.78328  -42.97528 8.49444   1.000 21.54782  ? 225 ALA A CB    1 
ATOM   1700 N  N     . ASN A 1 215 ? 12.00487  -43.23521 6.83400   1.000 27.17193  ? 226 ASN A N     1 
ATOM   1701 C  CA    . ASN A 1 215 ? 10.86469  -44.12545 6.63810   1.000 26.39211  ? 226 ASN A CA    1 
ATOM   1702 C  C     . ASN A 1 215 ? 11.40847  -45.44254 6.11354   1.000 24.91989  ? 226 ASN A C     1 
ATOM   1703 O  O     . ASN A 1 215 ? 11.82423  -45.51066 4.94378   1.000 27.10286  ? 226 ASN A O     1 
ATOM   1704 C  CB    . ASN A 1 215 ? 9.87377   -43.51125 5.65439   1.000 22.35640  ? 226 ASN A CB    1 
ATOM   1705 C  CG    . ASN A 1 215 ? 8.65070   -44.38457 5.40920   1.000 24.94809  ? 226 ASN A CG    1 
ATOM   1706 O  OD1   . ASN A 1 215 ? 8.66273   -45.59973 5.63109   1.000 22.76632  ? 226 ASN A OD1   1 
ATOM   1707 N  ND2   . ASN A 1 215 ? 7.58628   -43.75810 4.92833   1.000 22.63503  ? 226 ASN A ND2   1 
ATOM   1708 N  N     . PRO A 1 216 ? 11.41525  -46.51596 6.90591   1.000 26.07202  ? 227 PRO A N     1 
ATOM   1709 C  CA    . PRO A 1 216 ? 12.07840  -47.75227 6.46681   1.000 26.14608  ? 227 PRO A CA    1 
ATOM   1710 C  C     . PRO A 1 216 ? 11.33146  -48.51646 5.38444   1.000 29.03603  ? 227 PRO A C     1 
ATOM   1711 O  O     . PRO A 1 216 ? 11.81246  -49.57124 4.96407   1.000 30.36593  ? 227 PRO A O     1 
ATOM   1712 C  CB    . PRO A 1 216 ? 12.15211  -48.57424 7.76027   1.000 24.67699  ? 227 PRO A CB    1 
ATOM   1713 C  CG    . PRO A 1 216 ? 10.90675  -48.17695 8.48623   1.000 26.15747  ? 227 PRO A CG    1 
ATOM   1714 C  CD    . PRO A 1 216 ? 10.74241  -46.68969 8.20629   1.000 25.07149  ? 227 PRO A CD    1 
ATOM   1715 N  N     . ASN A 1 217 ? 10.17392  -48.03964 4.91515   1.000 29.42736  ? 228 ASN A N     1 
ATOM   1716 C  CA    . ASN A 1 217 ? 9.40217   -48.83475 3.96766   1.000 25.27851  ? 228 ASN A CA    1 
ATOM   1717 C  C     . ASN A 1 217 ? 8.49006   -47.93811 3.12899   1.000 30.25756  ? 228 ASN A C     1 
ATOM   1718 O  O     . ASN A 1 217 ? 7.26719   -47.92903 3.27231   1.000 26.62971  ? 228 ASN A O     1 
ATOM   1719 C  CB    . ASN A 1 217 ? 8.58011   -49.91066 4.67386   1.000 25.88998  ? 228 ASN A CB    1 
ATOM   1720 C  CG    . ASN A 1 217 ? 7.74307   -50.71497 3.69474   1.000 38.56966  ? 228 ASN A CG    1 
ATOM   1721 O  OD1   . ASN A 1 217 ? 8.06124   -50.77986 2.49550   1.000 33.87560  ? 228 ASN A OD1   1 
ATOM   1722 N  ND2   . ASN A 1 217 ? 6.66045   -51.30146 4.18288   1.000 31.14149  ? 228 ASN A ND2   1 
ATOM   1723 N  N     . ASN A 1 218 ? 9.09077   -47.17979 2.21464   1.000 30.19719  ? 229 ASN A N     1 
ATOM   1724 C  CA    . ASN A 1 218 ? 8.34846   -46.46182 1.18478   1.000 25.31470  ? 229 ASN A CA    1 
ATOM   1725 C  C     . ASN A 1 218 ? 8.32834   -47.37314 -0.03237  1.000 26.68440  ? 229 ASN A C     1 
ATOM   1726 O  O     . ASN A 1 218 ? 9.22519   -47.33540 -0.87106  1.000 28.42385  ? 229 ASN A O     1 
ATOM   1727 C  CB    . ASN A 1 218 ? 8.99146   -45.11318 0.88363   1.000 19.36939  ? 229 ASN A CB    1 
ATOM   1728 C  CG    . ASN A 1 218 ? 8.20415   -44.31225 -0.13491  1.000 25.50368  ? 229 ASN A CG    1 
ATOM   1729 O  OD1   . ASN A 1 218 ? 7.12405   -44.72104 -0.53457  1.000 26.26111  ? 229 ASN A OD1   1 
ATOM   1730 N  ND2   . ASN A 1 218 ? 8.73935   -43.16968 -0.55610  1.000 26.34948  ? 229 ASN A ND2   1 
ATOM   1731 N  N     . ASN A 1 219 ? 7.29196   -48.21075 -0.11829  1.000 28.15619  ? 230 ASN A N     1 
ATOM   1732 C  CA    . ASN A 1 219 ? 7.15343   -49.23896 -1.15699  1.000 28.62685  ? 230 ASN A CA    1 
ATOM   1733 C  C     . ASN A 1 219 ? 8.43552   -50.05761 -1.31701  1.000 29.09399  ? 230 ASN A C     1 
ATOM   1734 O  O     . ASN A 1 219 ? 8.92620   -50.29455 -2.42200  1.000 30.57229  ? 230 ASN A O     1 
ATOM   1735 C  CB    . ASN A 1 219 ? 6.71945   -48.62287 -2.49042  1.000 33.64599  ? 230 ASN A CB    1 
ATOM   1736 C  CG    . ASN A 1 219 ? 5.24364   -48.20593 -2.49441  1.000 32.37782  ? 230 ASN A CG    1 
ATOM   1737 O  OD1   . ASN A 1 219 ? 4.58311   -48.16251 -1.44658  1.000 27.65096  ? 230 ASN A OD1   1 
ATOM   1738 N  ND2   . ASN A 1 219 ? 4.73219   -47.88587 -3.67709  1.000 27.16140  ? 230 ASN A ND2   1 
ATOM   1739 N  N     . GLY A 1 220 ? 8.97915   -50.49554 -0.19011  1.000 31.65410  ? 231 GLY A N     1 
ATOM   1740 C  CA    . GLY A 1 220 ? 10.11971  -51.38593 -0.17152  1.000 29.88923  ? 231 GLY A CA    1 
ATOM   1741 C  C     . GLY A 1 220 ? 11.45832  -50.69079 -0.01344  1.000 32.86870  ? 231 GLY A C     1 
ATOM   1742 O  O     . GLY A 1 220 ? 12.41721  -51.32616 0.42670   1.000 34.63528  ? 231 GLY A O     1 
ATOM   1743 N  N     . ALA A 1 221 ? 11.54808  -49.41265 -0.36468  1.000 32.85846  ? 232 ALA A N     1 
ATOM   1744 C  CA    . ALA A 1 221 ? 12.76832  -48.64359 -0.18674  1.000 29.38833  ? 232 ALA A CA    1 
ATOM   1745 C  C     . ALA A 1 221 ? 12.74507  -47.94106 1.16547   1.000 30.36732  ? 232 ALA A C     1 
ATOM   1746 O  O     . ALA A 1 221 ? 11.68398  -47.68707 1.74189   1.000 27.27939  ? 232 ALA A O     1 
ATOM   1747 C  CB    . ALA A 1 221 ? 12.92709  -47.61468 -1.31337  1.000 26.93522  ? 232 ALA A CB    1 
ATOM   1748 N  N     . LEU A 1 222 ? 13.93268  -47.61584 1.66614   1.000 23.17562  ? 233 LEU A N     1 
ATOM   1749 C  CA    . LEU A 1 222 ? 14.06465  -46.77743 2.84696   1.000 23.53020  ? 233 LEU A CA    1 
ATOM   1750 C  C     . LEU A 1 222 ? 14.40982  -45.35964 2.41242   1.000 29.29490  ? 233 LEU A C     1 
ATOM   1751 O  O     . LEU A 1 222 ? 15.39714  -45.14287 1.70407   1.000 25.12789  ? 233 LEU A O     1 
ATOM   1752 C  CB    . LEU A 1 222 ? 15.13186  -47.32149 3.79691   1.000 26.99776  ? 233 LEU A CB    1 
ATOM   1753 C  CG    . LEU A 1 222 ? 15.32670  -46.58924 5.12569   1.000 27.50254  ? 233 LEU A CG    1 
ATOM   1754 C  CD1   . LEU A 1 222 ? 15.70463  -47.59799 6.20565   1.000 26.03572  ? 233 LEU A CD1   1 
ATOM   1755 C  CD2   . LEU A 1 222 ? 16.40553  -45.52478 5.00310   1.000 25.61588  ? 233 LEU A CD2   1 
ATOM   1756 N  N     . HIS A 1 223 ? 13.60917  -44.39799 2.84625   1.000 22.93103  ? 234 HIS A N     1 
ATOM   1757 C  CA    . HIS A 1 223 ? 13.85906  -43.00227 2.54470   1.000 25.66420  ? 234 HIS A CA    1 
ATOM   1758 C  C     . HIS A 1 223 ? 14.31305  -42.29590 3.80856   1.000 24.54865  ? 234 HIS A C     1 
ATOM   1759 O  O     . HIS A 1 223 ? 13.73433  -42.49765 4.87885   1.000 24.91567  ? 234 HIS A O     1 
ATOM   1760 C  CB    . HIS A 1 223 ? 12.60522  -42.31889 1.99005   1.000 23.09765  ? 234 HIS A CB    1 
ATOM   1761 C  CG    . HIS A 1 223 ? 12.84715  -40.91699 1.54297   1.000 25.35377  ? 234 HIS A CG    1 
ATOM   1762 N  ND1   . HIS A 1 223 ? 13.40362  -40.61346 0.31872   1.000 25.05024  ? 234 HIS A ND1   1 
ATOM   1763 C  CD2   . HIS A 1 223 ? 12.62268  -39.73227 2.16035   1.000 29.81282  ? 234 HIS A CD2   1 
ATOM   1764 C  CE1   . HIS A 1 223 ? 13.50853  -39.30086 0.19881   1.000 28.02581  ? 234 HIS A CE1   1 
ATOM   1765 N  NE2   . HIS A 1 223 ? 13.03540  -38.74333 1.30077   1.000 24.95270  ? 234 HIS A NE2   1 
ATOM   1766 N  N     . PHE A 1 224 ? 15.34859  -41.47606 3.69372   1.000 24.15253  ? 235 PHE A N     1 
ATOM   1767 C  CA    . PHE A 1 224 ? 15.81446  -40.75039 4.86041   1.000 28.61316  ? 235 PHE A CA    1 
ATOM   1768 C  C     . PHE A 1 224 ? 16.22143  -39.33560 4.46741   1.000 25.19344  ? 235 PHE A C     1 
ATOM   1769 O  O     . PHE A 1 224 ? 16.49586  -39.03889 3.29889   1.000 25.24657  ? 235 PHE A O     1 
ATOM   1770 C  CB    . PHE A 1 224 ? 16.95401  -41.49940 5.58191   1.000 25.40172  ? 235 PHE A CB    1 
ATOM   1771 C  CG    . PHE A 1 224 ? 18.28042  -41.46808 4.87754   1.000 24.89024  ? 235 PHE A CG    1 
ATOM   1772 C  CD1   . PHE A 1 224 ? 18.63543  -42.47123 3.97548   1.000 23.68811  ? 235 PHE A CD1   1 
ATOM   1773 C  CD2   . PHE A 1 224 ? 19.20413  -40.46602 5.16012   1.000 26.42232  ? 235 PHE A CD2   1 
ATOM   1774 C  CE1   . PHE A 1 224 ? 19.88259  -42.45738 3.34855   1.000 25.69196  ? 235 PHE A CE1   1 
ATOM   1775 C  CE2   . PHE A 1 224 ? 20.45789  -40.44418 4.53312   1.000 28.35018  ? 235 PHE A CE2   1 
ATOM   1776 C  CZ    . PHE A 1 224 ? 20.79672  -41.44169 3.62839   1.000 30.80152  ? 235 PHE A CZ    1 
ATOM   1777 N  N     . GLY A 1 225 ? 16.20842  -38.46280 5.46777   1.000 23.26391  ? 236 GLY A N     1 
ATOM   1778 C  CA    . GLY A 1 225 ? 16.59771  -37.07518 5.31881   1.000 21.52145  ? 236 GLY A CA    1 
ATOM   1779 C  C     . GLY A 1 225 ? 17.44529  -36.62302 6.49425   1.000 22.84408  ? 236 GLY A C     1 
ATOM   1780 O  O     . GLY A 1 225 ? 17.18088  -36.99532 7.63995   1.000 25.59673  ? 236 GLY A O     1 
ATOM   1781 N  N     . ILE A 1 226 ? 18.48603  -35.84679 6.20285   1.000 21.85862  ? 237 ILE A N     1 
ATOM   1782 C  CA    . ILE A 1 226 ? 19.34649  -35.22983 7.20034   1.000 20.62194  ? 237 ILE A CA    1 
ATOM   1783 C  C     . ILE A 1 226 ? 19.25094  -33.71481 7.02027   1.000 26.62547  ? 237 ILE A C     1 
ATOM   1784 O  O     . ILE A 1 226 ? 19.43266  -33.20883 5.90785   1.000 25.51984  ? 237 ILE A O     1 
ATOM   1785 C  CB    . ILE A 1 226 ? 20.79379  -35.73634 7.05907   1.000 23.06892  ? 237 ILE A CB    1 
ATOM   1786 C  CG1   . ILE A 1 226 ? 20.85437  -37.22955 7.42065   1.000 25.87111  ? 237 ILE A CG1   1 
ATOM   1787 C  CG2   . ILE A 1 226 ? 21.75170  -34.90084 7.88925   1.000 22.87508  ? 237 ILE A CG2   1 
ATOM   1788 C  CD1   . ILE A 1 226 ? 22.20519  -37.86266 7.25675   1.000 21.20186  ? 237 ILE A CD1   1 
ATOM   1789 N  N     . SER A 1 227 ? 18.96399  -32.99730 8.11036   1.000 24.80521  ? 238 SER A N     1 
ATOM   1790 C  CA    . SER A 1 227 ? 18.63687  -31.57532 8.08238   1.000 25.44130  ? 238 SER A CA    1 
ATOM   1791 C  C     . SER A 1 227 ? 19.46077  -30.81391 9.11249   1.000 30.11526  ? 238 SER A C     1 
ATOM   1792 O  O     . SER A 1 227 ? 19.70730  -31.31176 10.21275  1.000 29.39145  ? 238 SER A O     1 
ATOM   1793 C  CB    . SER A 1 227 ? 17.14527  -31.34669 8.36225   1.000 29.63103  ? 238 SER A CB    1 
ATOM   1794 O  OG    . SER A 1 227 ? 16.34859  -31.94635 7.35922   1.000 27.58137  ? 238 SER A OG    1 
ATOM   1795 N  N     . PHE A 1 228 ? 19.87437  -29.59798 8.75609   1.000 27.51908  ? 239 PHE A N     1 
ATOM   1796 C  CA    . PHE A 1 228 ? 20.75372  -28.80790 9.60563   1.000 28.37128  ? 239 PHE A CA    1 
ATOM   1797 C  C     . PHE A 1 228 ? 20.67609  -27.35989 9.15133   1.000 27.89287  ? 239 PHE A C     1 
ATOM   1798 O  O     . PHE A 1 228 ? 20.20715  -27.06814 8.05165   1.000 28.08974  ? 239 PHE A O     1 
ATOM   1799 C  CB    . PHE A 1 228 ? 22.19936  -29.32290 9.52966   1.000 29.97648  ? 239 PHE A CB    1 
ATOM   1800 C  CG    . PHE A 1 228 ? 22.64530  -29.63765 8.12483   1.000 32.36120  ? 239 PHE A CG    1 
ATOM   1801 C  CD1   . PHE A 1 228 ? 23.18145  -28.64929 7.31004   1.000 27.96720  ? 239 PHE A CD1   1 
ATOM   1802 C  CD2   . PHE A 1 228 ? 22.48399  -30.90941 7.60487   1.000 29.56895  ? 239 PHE A CD2   1 
ATOM   1803 C  CE1   . PHE A 1 228 ? 23.56664  -28.93251 6.01938   1.000 28.86996  ? 239 PHE A CE1   1 
ATOM   1804 C  CE2   . PHE A 1 228 ? 22.86703  -31.20270 6.30209   1.000 27.24905  ? 239 PHE A CE2   1 
ATOM   1805 C  CZ    . PHE A 1 228 ? 23.40480  -30.21424 5.51112   1.000 30.74445  ? 239 PHE A CZ    1 
ATOM   1806 N  N     . LYS A 1 229 ? 21.13679  -26.45314 10.01053  1.000 30.02667  ? 240 LYS A N     1 
ATOM   1807 C  CA    . LYS A 1 229 ? 21.31390  -25.06832 9.59104   1.000 36.19945  ? 240 LYS A CA    1 
ATOM   1808 C  C     . LYS A 1 229 ? 22.31286  -24.99961 8.44174   1.000 34.98367  ? 240 LYS A C     1 
ATOM   1809 O  O     . LYS A 1 229 ? 23.32320  -25.70182 8.43354   1.000 34.62714  ? 240 LYS A O     1 
ATOM   1810 C  CB    . LYS A 1 229 ? 21.79826  -24.20758 10.76077  1.000 38.76365  ? 240 LYS A CB    1 
ATOM   1811 C  CG    . LYS A 1 229 ? 20.73644  -23.94084 11.82232  1.000 45.98996  ? 240 LYS A CG    1 
ATOM   1812 C  CD    . LYS A 1 229 ? 21.25663  -22.99147 12.89651  1.000 50.12573  ? 240 LYS A CD    1 
ATOM   1813 C  CE    . LYS A 1 229 ? 20.15181  -22.56658 13.86074  1.000 56.97563  ? 240 LYS A CE    1 
ATOM   1814 N  NZ    . LYS A 1 229 ? 20.58522  -21.49522 14.82311  1.000 59.03614  ? 240 LYS A NZ    1 
ATOM   1815 N  N     . THR A 1 230 ? 22.02094  -24.16802 7.46052   1.000 37.21719  ? 241 THR A N     1 
ATOM   1816 C  CA    . THR A 1 230 ? 22.89805  -24.05931 6.30831   1.000 35.53047  ? 241 THR A CA    1 
ATOM   1817 C  C     . THR A 1 230 ? 24.25666  -23.51683 6.74293   1.000 42.71095  ? 241 THR A C     1 
ATOM   1818 O  O     . THR A 1 230 ? 24.32836  -22.37423 7.22509   1.000 45.68663  ? 241 THR A O     1 
ATOM   1819 C  CB    . THR A 1 230 ? 22.27119  -23.15380 5.25937   1.000 36.86356  ? 241 THR A CB    1 
ATOM   1820 O  OG1   . THR A 1 230 ? 21.01102  -23.70526 4.86410   1.000 38.96123  ? 241 THR A OG1   1 
ATOM   1821 C  CG2   . THR A 1 230 ? 23.17293  -23.04883 4.03972   1.000 37.95423  ? 241 THR A CG2   1 
ATOM   1822 N  N     . PRO A 1 231 ? 25.34202  -24.28781 6.60423   1.000 41.57025  ? 242 PRO A N     1 
ATOM   1823 C  CA    . PRO A 1 231 ? 26.65312  -23.82356 7.08719   1.000 45.93527  ? 242 PRO A CA    1 
ATOM   1824 C  C     . PRO A 1 231 ? 27.03395  -22.46777 6.50581   1.000 52.64951  ? 242 PRO A C     1 
ATOM   1825 O  O     . PRO A 1 231 ? 26.72483  -22.15280 5.35571   1.000 58.19880  ? 242 PRO A O     1 
ATOM   1826 C  CB    . PRO A 1 231 ? 27.61259  -24.92089 6.61622   1.000 43.03168  ? 242 PRO A CB    1 
ATOM   1827 C  CG    . PRO A 1 231 ? 26.75217  -26.13970 6.46799   1.000 38.86011  ? 242 PRO A CG    1 
ATOM   1828 C  CD    . PRO A 1 231 ? 25.41118  -25.63798 6.01368   1.000 37.29856  ? 242 PRO A CD    1 
ATOM   1829 N  N     . ASP A 1 232 ? 27.71854  -21.66218 7.32045   1.000 56.24289  ? 243 ASP A N     1 
ATOM   1830 C  CA    . ASP A 1 232 ? 28.09876  -20.31780 6.88976   1.000 73.42451  ? 243 ASP A CA    1 
ATOM   1831 C  C     . ASP A 1 232 ? 29.05803  -20.34792 5.70844   1.000 68.63133  ? 243 ASP A C     1 
ATOM   1832 O  O     . ASP A 1 232 ? 29.03820  -19.43727 4.87517   1.000 68.74347  ? 243 ASP A O     1 
ATOM   1833 C  CB    . ASP A 1 232 ? 28.71861  -19.55188 8.05698   1.000 77.71394  ? 243 ASP A CB    1 
ATOM   1834 C  CG    . ASP A 1 232 ? 27.71323  -19.24254 9.14099   1.000 87.63073  ? 243 ASP A CG    1 
ATOM   1835 O  OD1   . ASP A 1 232 ? 26.83752  -18.37655 8.90983   1.000 88.85956  ? 243 ASP A OD1   1 
ATOM   1836 O  OD2   . ASP A 1 232 ? 27.79012  -19.88574 10.21244  1.000 88.82736  ? 243 ASP A OD2   1 
ATOM   1837 N  N     . GLU A 1 233 ? 29.89181  -21.38652 5.60945   1.000 69.59156  ? 244 GLU A N     1 
ATOM   1838 C  CA    . GLU A 1 233 ? 30.77433  -21.52597 4.45605   1.000 71.84873  ? 244 GLU A CA    1 
ATOM   1839 C  C     . GLU A 1 233 ? 30.00012  -21.63716 3.14619   1.000 72.38190  ? 244 GLU A C     1 
ATOM   1840 O  O     . GLU A 1 233 ? 30.55665  -21.34676 2.08060   1.000 76.69736  ? 244 GLU A O     1 
ATOM   1841 C  CB    . GLU A 1 233 ? 31.67943  -22.74615 4.63163   1.000 73.97666  ? 244 GLU A CB    1 
ATOM   1842 C  CG    . GLU A 1 233 ? 32.54047  -22.72372 5.88657   1.000 74.96303  ? 244 GLU A CG    1 
ATOM   1843 C  CD    . GLU A 1 233 ? 31.91400  -23.47659 7.05044   1.000 78.47743  ? 244 GLU A CD    1 
ATOM   1844 O  OE1   . GLU A 1 233 ? 30.66814  -23.57439 7.10229   1.000 66.44615  ? 244 GLU A OE1   1 
ATOM   1845 O  OE2   . GLU A 1 233 ? 32.67222  -23.97636 7.91288   1.000 75.56434  ? 244 GLU A OE2   1 
ATOM   1846 N  N     . TRP A 1 234 ? 28.72847  -22.02988 3.20283   1.000 66.91359  ? 245 TRP A N     1 
ATOM   1847 C  CA    . TRP A 1 234 ? 27.89331  -22.20222 2.01446   1.000 74.76635  ? 245 TRP A CA    1 
ATOM   1848 C  C     . TRP A 1 234 ? 27.20600  -20.91538 1.57301   1.000 82.33485  ? 245 TRP A C     1 
ATOM   1849 O  O     . TRP A 1 234 ? 26.03262  -20.95939 1.18911   1.000 82.19225  ? 245 TRP A O     1 
ATOM   1850 C  CB    . TRP A 1 234 ? 26.84764  -23.28442 2.26085   1.000 60.57255  ? 245 TRP A CB    1 
ATOM   1851 C  CG    . TRP A 1 234 ? 27.36312  -24.66077 2.51949   1.000 54.91186  ? 245 TRP A CG    1 
ATOM   1852 C  CD1   . TRP A 1 234 ? 28.64149  -25.02638 2.79708   1.000 58.66015  ? 245 TRP A CD1   1 
ATOM   1853 C  CD2   . TRP A 1 234 ? 26.58743  -25.86482 2.53300   1.000 50.71954  ? 245 TRP A CD2   1 
ATOM   1854 N  NE1   . TRP A 1 234 ? 28.71491  -26.38396 2.98107   1.000 53.67321  ? 245 TRP A NE1   1 
ATOM   1855 C  CE2   . TRP A 1 234 ? 27.46551  -26.92289 2.82663   1.000 49.51676  ? 245 TRP A CE2   1 
ATOM   1856 C  CE3   . TRP A 1 234 ? 25.23393  -26.14780 2.32226   1.000 40.85446  ? 245 TRP A CE3   1 
ATOM   1857 C  CZ2   . TRP A 1 234 ? 27.03751  -28.24737 2.91687   1.000 38.36378  ? 245 TRP A CZ2   1 
ATOM   1858 C  CZ3   . TRP A 1 234 ? 24.80549  -27.46304 2.41181   1.000 43.91743  ? 245 TRP A CZ3   1 
ATOM   1859 C  CH2   . TRP A 1 234 ? 25.70854  -28.49888 2.70554   1.000 40.67510  ? 245 TRP A CH2   1 
ATOM   1860 N  N     . LYS A 1 235 ? 27.86781  -19.75503 1.60364   1.000 92.30176  ? 246 LYS A N     1 
ATOM   1861 C  CA    . LYS A 1 235 ? 27.26677  -18.62312 0.89941   1.000 94.12802  ? 246 LYS A CA    1 
ATOM   1862 C  C     . LYS A 1 235 ? 27.34809  -18.78547 -0.61342  1.000 104.05424 ? 246 LYS A C     1 
ATOM   1863 O  O     . LYS A 1 235 ? 26.91197  -17.89163 -1.34631  1.000 102.66138 ? 246 LYS A O     1 
ATOM   1864 C  CB    . LYS A 1 235 ? 27.91318  -17.30716 1.33640   1.000 88.25947  ? 246 LYS A CB    1 
ATOM   1865 C  CG    . LYS A 1 235 ? 27.37497  -16.77912 2.66693   1.000 93.00562  ? 246 LYS A CG    1 
ATOM   1866 C  CD    . LYS A 1 235 ? 28.16360  -15.56592 3.18040   1.000 99.27507  ? 246 LYS A CD    1 
ATOM   1867 C  CE    . LYS A 1 235 ? 27.74305  -14.24838 2.51542   1.000 99.23294  ? 246 LYS A CE    1 
ATOM   1868 N  NZ    . LYS A 1 235 ? 26.45537  -13.68267 3.03085   1.000 86.96210  ? 246 LYS A NZ    1 
ATOM   1869 N  N     . ASN A 1 236 ? 27.90194  -19.91243 -1.08006  1.000 126.88641 ? 247 ASN A N     1 
ATOM   1870 C  CA    . ASN A 1 236 ? 27.85437  -20.35167 -2.46828  1.000 119.91506 ? 247 ASN A CA    1 
ATOM   1871 C  C     . ASN A 1 236 ? 27.65773  -21.86328 -2.55615  1.000 121.33264 ? 247 ASN A C     1 
ATOM   1872 O  O     . ASN A 1 236 ? 28.03844  -22.48197 -3.55624  1.000 129.53267 ? 247 ASN A O     1 
ATOM   1873 C  CB    . ASN A 1 236 ? 29.12360  -19.95030 -3.21893  1.000 127.04699 ? 247 ASN A CB    1 
ATOM   1874 C  CG    . ASN A 1 236 ? 28.86869  -18.88599 -4.26051  1.000 141.90027 ? 247 ASN A CG    1 
ATOM   1875 O  OD1   . ASN A 1 236 ? 27.83749  -18.21213 -4.23579  1.000 141.65840 ? 247 ASN A OD1   1 
ATOM   1876 N  ND2   . ASN A 1 236 ? 29.80796  -18.72778 -5.18748  1.000 142.68552 ? 247 ASN A ND2   1 
ATOM   1877 N  N     . GLN A 1 237 ? 27.07519  -22.46884 -1.51258  1.000 105.10174 ? 248 GLN A N     1 
ATOM   1878 C  CA    . GLN A 1 237 ? 26.86201  -23.92181 -1.42664  1.000 93.39171  ? 248 GLN A CA    1 
ATOM   1879 C  C     . GLN A 1 237 ? 28.16272  -24.69040 -1.65507  1.000 97.79633  ? 248 GLN A C     1 
ATOM   1880 O  O     . GLN A 1 237 ? 28.15678  -25.81211 -2.16829  1.000 88.27364  ? 248 GLN A O     1 
ATOM   1881 C  CB    . GLN A 1 237 ? 25.77378  -24.38147 -2.40543  1.000 93.39321  ? 248 GLN A CB    1 
ATOM   1882 C  CG    . GLN A 1 237 ? 25.03812  -25.66863 -2.01609  1.000 73.99527  ? 248 GLN A CG    1 
ATOM   1883 C  CD    . GLN A 1 237 ? 23.76373  -25.89175 -2.83977  1.000 86.69950  ? 248 GLN A CD    1 
ATOM   1884 O  OE1   . GLN A 1 237 ? 23.60016  -26.92632 -3.49341  1.000 82.47730  ? 248 GLN A OE1   1 
ATOM   1885 N  NE2   . GLN A 1 237 ? 22.85611  -24.91815 -2.80548  1.000 88.39960  ? 248 GLN A NE2   1 
ATOM   1886 N  N     . THR A 1 238 ? 29.28687  -24.09015 -1.25789  1.000 107.45113 ? 249 THR A N     1 
ATOM   1887 C  CA    . THR A 1 238 ? 30.60007  -24.62987 -1.58278  1.000 111.13799 ? 249 THR A CA    1 
ATOM   1888 C  C     . THR A 1 238 ? 30.82025  -25.97848 -0.89815  1.000 105.22471 ? 249 THR A C     1 
ATOM   1889 O  O     . THR A 1 238 ? 30.00102  -26.45208 -0.10583  1.000 91.86539  ? 249 THR A O     1 
ATOM   1890 C  CB    . THR A 1 238 ? 31.71531  -23.66140 -1.16904  1.000 108.87206 ? 249 THR A CB    1 
ATOM   1891 O  OG1   . THR A 1 238 ? 32.00263  -23.81808 0.22645   1.000 104.82709 ? 249 THR A OG1   1 
ATOM   1892 C  CG2   . THR A 1 238 ? 31.31765  -22.21516 -1.43723  1.000 106.11516 ? 249 THR A CG2   1 
ATOM   1893 N  N     . GLN A 1 239 ? 31.95143  -26.59786 -1.24783  1.000 116.35446 ? 250 GLN A N     1 
ATOM   1894 C  CA    . GLN A 1 239 ? 32.47958  -27.81460 -0.63540  1.000 121.59180 ? 250 GLN A CA    1 
ATOM   1895 C  C     . GLN A 1 239 ? 31.69882  -29.07368 -0.99625  1.000 112.14949 ? 250 GLN A C     1 
ATOM   1896 O  O     . GLN A 1 239 ? 32.31083  -30.11470 -1.26294  1.000 105.33590 ? 250 GLN A O     1 
ATOM   1897 C  CB    . GLN A 1 239 ? 32.55828  -27.66416 0.88671   1.000 127.05281 ? 250 GLN A CB    1 
ATOM   1898 C  CG    . GLN A 1 239 ? 33.89604  -27.12460 1.36419   1.000 132.85313 ? 250 GLN A CG    1 
ATOM   1899 C  CD    . GLN A 1 239 ? 33.75746  -26.14275 2.50758   1.000 137.02933 ? 250 GLN A CD    1 
ATOM   1900 O  OE1   . GLN A 1 239 ? 32.83548  -26.23922 3.31805   1.000 138.57590 ? 250 GLN A OE1   1 
ATOM   1901 N  NE2   . GLN A 1 239 ? 34.67070  -25.18055 2.57217   1.000 130.18478 ? 250 GLN A NE2   1 
ATOM   1902 N  N     . VAL A 1 240 ? 30.36855  -29.01410 -1.00956  1.000 82.63292  ? 251 VAL A N     1 
ATOM   1903 C  CA    . VAL A 1 240 ? 29.55577  -30.20295 -1.23425  1.000 59.86024  ? 251 VAL A CA    1 
ATOM   1904 C  C     . VAL A 1 240 ? 28.95515  -30.13424 -2.62962  1.000 51.23688  ? 251 VAL A C     1 
ATOM   1905 O  O     . VAL A 1 240 ? 28.04009  -29.34416 -2.90145  1.000 44.51777  ? 251 VAL A O     1 
ATOM   1906 C  CB    . VAL A 1 240 ? 28.47422  -30.38383 -0.16864  1.000 47.48085  ? 251 VAL A CB    1 
ATOM   1907 C  CG1   . VAL A 1 240 ? 27.65755  -31.59992 -0.50806  1.000 38.98881  ? 251 VAL A CG1   1 
ATOM   1908 C  CG2   . VAL A 1 240 ? 29.11933  -30.56855 1.19189   1.000 45.47012  ? 251 VAL A CG2   1 
ATOM   1909 N  N     . ASP A 1 241 ? 29.48326  -30.98318 -3.50547  1.000 38.80346  ? 252 ASP A N     1 
ATOM   1910 C  CA    . ASP A 1 241 ? 28.94581  -31.21898 -4.83866  1.000 40.73481  ? 252 ASP A CA    1 
ATOM   1911 C  C     . ASP A 1 241 ? 28.03425  -32.43977 -4.73619  1.000 40.50303  ? 252 ASP A C     1 
ATOM   1912 O  O     . ASP A 1 241 ? 28.49318  -33.54305 -4.42308  1.000 35.65691  ? 252 ASP A O     1 
ATOM   1913 C  CB    . ASP A 1 241 ? 30.10125  -31.42090 -5.81900  1.000 37.14624  ? 252 ASP A CB    1 
ATOM   1914 C  CG    . ASP A 1 241 ? 29.67090  -31.97170 -7.15855  1.000 35.06859  ? 252 ASP A CG    1 
ATOM   1915 O  OD1   . ASP A 1 241 ? 28.48233  -31.86649 -7.52510  1.000 44.23263  ? 252 ASP A OD1   1 
ATOM   1916 O  OD2   . ASP A 1 241 ? 30.55599  -32.50869 -7.85907  1.000 42.26082  ? 252 ASP A OD2   1 
ATOM   1917 N  N     . PHE A 1 242 ? 26.73853  -32.24779 -4.95910  1.000 35.59805  ? 253 PHE A N     1 
ATOM   1918 C  CA    . PHE A 1 242 ? 25.83631  -33.36834 -4.73665  1.000 33.34551  ? 253 PHE A CA    1 
ATOM   1919 C  C     . PHE A 1 242 ? 25.83913  -34.36215 -5.88069  1.000 33.58674  ? 253 PHE A C     1 
ATOM   1920 O  O     . PHE A 1 242 ? 25.20467  -35.41110 -5.75958  1.000 38.26798  ? 253 PHE A O     1 
ATOM   1921 C  CB    . PHE A 1 242 ? 24.42714  -32.85220 -4.44235  1.000 36.64363  ? 253 PHE A CB    1 
ATOM   1922 C  CG    . PHE A 1 242 ? 24.31438  -32.27729 -3.07058  1.000 35.38372  ? 253 PHE A CG    1 
ATOM   1923 C  CD1   . PHE A 1 242 ? 24.12462  -33.10804 -1.98025  1.000 30.45890  ? 253 PHE A CD1   1 
ATOM   1924 C  CD2   . PHE A 1 242 ? 24.49265  -30.92539 -2.85734  1.000 35.78184  ? 253 PHE A CD2   1 
ATOM   1925 C  CE1   . PHE A 1 242 ? 24.06596  -32.59674 -0.71036  1.000 36.42076  ? 253 PHE A CE1   1 
ATOM   1926 C  CE2   . PHE A 1 242 ? 24.43521  -30.40531 -1.58530  1.000 35.55990  ? 253 PHE A CE2   1 
ATOM   1927 C  CZ    . PHE A 1 242 ? 24.22635  -31.24348 -0.50977  1.000 35.27916  ? 253 PHE A CZ    1 
ATOM   1928 N  N     . GLN A 1 243 ? 26.55359  -34.06417 -6.96558  1.000 33.93600  ? 254 GLN A N     1 
ATOM   1929 C  CA    . GLN A 1 243 ? 26.85630  -35.02551 -8.01854  1.000 42.43624  ? 254 GLN A CA    1 
ATOM   1930 C  C     . GLN A 1 243 ? 27.96722  -35.99809 -7.63921  1.000 42.11863  ? 254 GLN A C     1 
ATOM   1931 O  O     . GLN A 1 243 ? 28.16402  -36.99583 -8.33985  1.000 42.22495  ? 254 GLN A O     1 
ATOM   1932 C  CB    . GLN A 1 243 ? 27.27238  -34.28791 -9.29680  1.000 42.10594  ? 254 GLN A CB    1 
ATOM   1933 C  CG    . GLN A 1 243 ? 26.29491  -33.22381 -9.74625  1.000 48.29185  ? 254 GLN A CG    1 
ATOM   1934 C  CD    . GLN A 1 243 ? 24.93763  -33.80565 -10.04429 1.000 58.29888  ? 254 GLN A CD    1 
ATOM   1935 O  OE1   . GLN A 1 243 ? 23.94193  -33.45145 -9.40832  1.000 64.18930  ? 254 GLN A OE1   1 
ATOM   1936 N  NE2   . GLN A 1 243 ? 24.88731  -34.72014 -11.00974 1.000 61.62143  ? 254 GLN A NE2   1 
ATOM   1937 N  N     . ASN A 1 244 ? 28.70233  -35.72718 -6.56498  1.000 37.54514  ? 255 ASN A N     1 
ATOM   1938 C  CA    . ASN A 1 244 ? 29.87903  -36.50398 -6.17000  1.000 35.82282  ? 255 ASN A CA    1 
ATOM   1939 C  C     . ASN A 1 244 ? 29.56213  -37.14542 -4.82342  1.000 32.99937  ? 255 ASN A C     1 
ATOM   1940 O  O     . ASN A 1 244 ? 29.61620  -36.47092 -3.79075  1.000 31.92620  ? 255 ASN A O     1 
ATOM   1941 C  CB    . ASN A 1 244 ? 31.09633  -35.58345 -6.09375  1.000 35.84031  ? 255 ASN A CB    1 
ATOM   1942 C  CG    . ASN A 1 244 ? 32.37573  -36.30740 -5.73325  1.000 34.39747  ? 255 ASN A CG    1 
ATOM   1943 O  OD1   . ASN A 1 244 ? 32.36903  -37.45902 -5.29030  1.000 33.45429  ? 255 ASN A OD1   1 
ATOM   1944 N  ND2   . ASN A 1 244 ? 33.49232  -35.61690 -5.91014  1.000 34.98811  ? 255 ASN A ND2   1 
ATOM   1945 N  N     . ARG A 1 245 ? 29.20892  -38.43777 -4.82621  1.000 31.76318  ? 256 ARG A N     1 
ATOM   1946 C  CA    . ARG A 1 245 ? 28.79894  -39.06098 -3.57438  1.000 28.77658  ? 256 ARG A CA    1 
ATOM   1947 C  C     . ARG A 1 245 ? 29.92020  -39.01591 -2.54238  1.000 31.74223  ? 256 ARG A C     1 
ATOM   1948 O  O     . ARG A 1 245 ? 29.64638  -38.87075 -1.34906  1.000 25.96554  ? 256 ARG A O     1 
ATOM   1949 C  CB    . ARG A 1 245 ? 28.32185  -40.50758 -3.79989  1.000 28.96475  ? 256 ARG A CB    1 
ATOM   1950 C  CG    . ARG A 1 245 ? 29.41833  -41.51310 -4.10612  1.000 39.07720  ? 256 ARG A CG    1 
ATOM   1951 C  CD    . ARG A 1 245 ? 28.91691  -42.96945 -4.07020  1.000 37.74373  ? 256 ARG A CD    1 
ATOM   1952 N  NE    . ARG A 1 245 ? 28.26968  -43.30662 -2.80593  1.000 35.34706  ? 256 ARG A NE    1 
ATOM   1953 C  CZ    . ARG A 1 245 ? 28.91192  -43.72771 -1.72353  1.000 31.23454  ? 256 ARG A CZ    1 
ATOM   1954 N  NH1   . ARG A 1 245 ? 30.22320  -43.89395 -1.71985  1.000 30.53196  ? 256 ARG A NH1   1 
ATOM   1955 N  NH2   . ARG A 1 245 ? 28.22185  -43.97783 -0.61174  1.000 28.62984  ? 256 ARG A NH2   1 
ATOM   1956 N  N     . ASN A 1 246 ? 31.18660  -39.10090 -2.97899  1.000 31.06225  ? 257 ASN A N     1 
ATOM   1957 C  CA    . ASN A 1 246 ? 32.30010  -39.07044 -2.02959  1.000 32.28223  ? 257 ASN A CA    1 
ATOM   1958 C  C     . ASN A 1 246 ? 32.36437  -37.73963 -1.28679  1.000 32.43554  ? 257 ASN A C     1 
ATOM   1959 O  O     . ASN A 1 246 ? 32.63467  -37.70429 -0.08206  1.000 34.60644  ? 257 ASN A O     1 
ATOM   1960 C  CB    . ASN A 1 246 ? 33.62279  -39.33540 -2.75138  1.000 30.52345  ? 257 ASN A CB    1 
ATOM   1961 C  CG    . ASN A 1 246 ? 33.64867  -40.68014 -3.42510  1.000 30.45545  ? 257 ASN A CG    1 
ATOM   1962 O  OD1   . ASN A 1 246 ? 33.15399  -41.66280 -2.88222  1.000 34.81687  ? 257 ASN A OD1   1 
ATOM   1963 N  ND2   . ASN A 1 246 ? 34.20267  -40.72830 -4.63082  1.000 36.61378  ? 257 ASN A ND2   1 
ATOM   1964 N  N     . SER A 1 247 ? 32.12626  -36.63444 -1.99176  1.000 35.43939  ? 258 SER A N     1 
ATOM   1965 C  CA    . SER A 1 247 ? 32.08099  -35.33153 -1.33497  1.000 35.07132  ? 258 SER A CA    1 
ATOM   1966 C  C     . SER A 1 247 ? 30.97942  -35.28426 -0.27884  1.000 32.52282  ? 258 SER A C     1 
ATOM   1967 O  O     . SER A 1 247 ? 31.19746  -34.79866 0.83867   1.000 35.97738  ? 258 SER A O     1 
ATOM   1968 C  CB    . SER A 1 247 ? 31.88961  -34.23595 -2.38882  1.000 33.45939  ? 258 SER A CB    1 
ATOM   1969 O  OG    . SER A 1 247 ? 31.50087  -33.00994 -1.80389  1.000 50.74120  ? 258 SER A OG    1 
ATOM   1970 N  N     . VAL A 1 248 ? 29.79770  -35.81055 -0.60545  1.000 27.39628  ? 259 VAL A N     1 
ATOM   1971 C  CA    . VAL A 1 248 ? 28.67759  -35.77361 0.33003   1.000 27.63689  ? 259 VAL A CA    1 
ATOM   1972 C  C     . VAL A 1 248 ? 28.91818  -36.71803 1.50288   1.000 28.55502  ? 259 VAL A C     1 
ATOM   1973 O  O     . VAL A 1 248 ? 28.66877  -36.35976 2.65930   1.000 25.16169  ? 259 VAL A O     1 
ATOM   1974 C  CB    . VAL A 1 248 ? 27.36703  -36.10588 -0.39659  1.000 28.73925  ? 259 VAL A CB    1 
ATOM   1975 C  CG1   . VAL A 1 248 ? 26.17833  -35.94247 0.55968   1.000 26.58786  ? 259 VAL A CG1   1 
ATOM   1976 C  CG2   . VAL A 1 248 ? 27.21458  -35.22664 -1.62789  1.000 28.22756  ? 259 VAL A CG2   1 
ATOM   1977 N  N     . VAL A 1 249 ? 29.38187  -37.94325 1.22234   1.000 26.35870  ? 260 VAL A N     1 
ATOM   1978 C  CA    . VAL A 1 249 ? 29.69308  -38.89924 2.28466   1.000 25.16776  ? 260 VAL A CA    1 
ATOM   1979 C  C     . VAL A 1 249 ? 30.69636  -38.29222 3.25379   1.000 26.16517  ? 260 VAL A C     1 
ATOM   1980 O  O     . VAL A 1 249 ? 30.55534  -38.40631 4.47579   1.000 28.30401  ? 260 VAL A O     1 
ATOM   1981 C  CB    . VAL A 1 249 ? 30.21648  -40.22145 1.68035   1.000 25.33505  ? 260 VAL A CB    1 
ATOM   1982 C  CG1   . VAL A 1 249 ? 30.82073  -41.12572 2.75431   1.000 25.45797  ? 260 VAL A CG1   1 
ATOM   1983 C  CG2   . VAL A 1 249 ? 29.10126  -40.95478 0.93923   1.000 25.54471  ? 260 VAL A CG2   1 
ATOM   1984 N  N     . ASP A 1 250 ? 31.71053  -37.61320 2.72253   1.000 28.01699  ? 261 ASP A N     1 
ATOM   1985 C  CA    . ASP A 1 250 ? 32.73976  -37.04236 3.57977   1.000 29.89885  ? 261 ASP A CA    1 
ATOM   1986 C  C     . ASP A 1 250 ? 32.16704  -35.96139 4.48680   1.000 34.73945  ? 261 ASP A C     1 
ATOM   1987 O  O     . ASP A 1 250 ? 32.49410  -35.90102 5.67814   1.000 29.04680  ? 261 ASP A O     1 
ATOM   1988 C  CB    . ASP A 1 250 ? 33.85808  -36.46693 2.72924   1.000 30.20439  ? 261 ASP A CB    1 
ATOM   1989 C  CG    . ASP A 1 250 ? 35.04001  -36.06089 3.55467   1.000 35.07343  ? 261 ASP A CG    1 
ATOM   1990 O  OD1   . ASP A 1 250 ? 35.73391  -36.96515 4.05869   1.000 33.91215  ? 261 ASP A OD1   1 
ATOM   1991 O  OD2   . ASP A 1 250 ? 35.26324  -34.84601 3.71052   1.000 41.67456  ? 261 ASP A OD2   1 
ATOM   1992 N  N     . PHE A 1 251 ? 31.32284  -35.08826 3.92991   1.000 30.85712  ? 262 PHE A N     1 
ATOM   1993 C  CA    . PHE A 1 251 ? 30.68332  -34.04334 4.72350   1.000 31.90539  ? 262 PHE A CA    1 
ATOM   1994 C  C     . PHE A 1 251 ? 29.78369  -34.63163 5.81018   1.000 27.70785  ? 262 PHE A C     1 
ATOM   1995 O  O     . PHE A 1 251 ? 29.82126  -34.18944 6.96293   1.000 30.91227  ? 262 PHE A O     1 
ATOM   1996 C  CB    . PHE A 1 251 ? 29.88488  -33.12256 3.80442   1.000 30.69176  ? 262 PHE A CB    1 
ATOM   1997 C  CG    . PHE A 1 251 ? 28.94821  -32.19825 4.52893   1.000 31.15798  ? 262 PHE A CG    1 
ATOM   1998 C  CD1   . PHE A 1 251 ? 29.41585  -31.02811 5.10564   1.000 38.16665  ? 262 PHE A CD1   1 
ATOM   1999 C  CD2   . PHE A 1 251 ? 27.59742  -32.48828 4.61536   1.000 32.20550  ? 262 PHE A CD2   1 
ATOM   2000 C  CE1   . PHE A 1 251 ? 28.54912  -30.16563 5.76811   1.000 41.05905  ? 262 PHE A CE1   1 
ATOM   2001 C  CE2   . PHE A 1 251 ? 26.72388  -31.63730 5.27426   1.000 31.62712  ? 262 PHE A CE2   1 
ATOM   2002 C  CZ    . PHE A 1 251 ? 27.19913  -30.47683 5.85666   1.000 33.60478  ? 262 PHE A CZ    1 
ATOM   2003 N  N     . LEU A 1 252 ? 28.97830  -35.63388 5.46893   1.000 26.66542  ? 263 LEU A N     1 
ATOM   2004 C  CA    . LEU A 1 252 ? 28.03834  -36.17415 6.44753   1.000 25.66811  ? 263 LEU A CA    1 
ATOM   2005 C  C     . LEU A 1 252 ? 28.74885  -36.98407 7.52880   1.000 27.99323  ? 263 LEU A C     1 
ATOM   2006 O  O     . LEU A 1 252 ? 28.35017  -36.94380 8.69677   1.000 29.26019  ? 263 LEU A O     1 
ATOM   2007 C  CB    . LEU A 1 252 ? 26.98147  -37.01727 5.74386   1.000 25.94068  ? 263 LEU A CB    1 
ATOM   2008 C  CG    . LEU A 1 252 ? 25.92180  -36.22991 4.97662   1.000 29.83280  ? 263 LEU A CG    1 
ATOM   2009 C  CD1   . LEU A 1 252 ? 25.02286  -37.18807 4.21695   1.000 27.95867  ? 263 LEU A CD1   1 
ATOM   2010 C  CD2   . LEU A 1 252 ? 25.09857  -35.34508 5.91572   1.000 23.17883  ? 263 LEU A CD2   1 
ATOM   2011 N  N     . LEU A 1 253 ? 29.80265  -37.72228 7.17163   1.000 31.30966  ? 264 LEU A N     1 
ATOM   2012 C  CA    . LEU A 1 253 ? 30.51320  -38.50016 8.18804   1.000 32.82911  ? 264 LEU A CA    1 
ATOM   2013 C  C     . LEU A 1 253 ? 31.16359  -37.59586 9.22204   1.000 29.62434  ? 264 LEU A C     1 
ATOM   2014 O  O     . LEU A 1 253 ? 31.30401  -37.98434 10.38782  1.000 33.87593  ? 264 LEU A O     1 
ATOM   2015 C  CB    . LEU A 1 253 ? 31.56271  -39.40998 7.54356   1.000 26.74963  ? 264 LEU A CB    1 
ATOM   2016 C  CG    . LEU A 1 253 ? 30.94712  -40.60206 6.80505   1.000 30.34382  ? 264 LEU A CG    1 
ATOM   2017 C  CD1   . LEU A 1 253 ? 32.02147  -41.56903 6.31501   1.000 26.21618  ? 264 LEU A CD1   1 
ATOM   2018 C  CD2   . LEU A 1 253 ? 29.95979  -41.30339 7.72326   1.000 25.51101  ? 264 LEU A CD2   1 
ATOM   2019 N  N     . LYS A 1 254 ? 31.56432  -36.39054 8.82031   1.000 29.36429  ? 265 LYS A N     1 
ATOM   2020 C  CA    . LYS A 1 254 ? 32.10203  -35.43797 9.78876   1.000 35.39592  ? 265 LYS A CA    1 
ATOM   2021 C  C     . LYS A 1 254 ? 30.99683  -34.88502 10.68462  1.000 29.66090  ? 265 LYS A C     1 
ATOM   2022 O  O     . LYS A 1 254 ? 31.15429  -34.81542 11.90738  1.000 36.81303  ? 265 LYS A O     1 
ATOM   2023 C  CB    . LYS A 1 254 ? 32.84107  -34.31316 9.06398   1.000 31.13216  ? 265 LYS A CB    1 
ATOM   2024 C  CG    . LYS A 1 254 ? 34.25186  -34.68526 8.66092   1.000 41.93987  ? 265 LYS A CG    1 
ATOM   2025 C  CD    . LYS A 1 254 ? 34.76703  -33.81517 7.50601   1.000 49.84380  ? 265 LYS A CD    1 
ATOM   2026 C  CE    . LYS A 1 254 ? 36.20320  -34.20313 7.14307   1.000 49.99818  ? 265 LYS A CE    1 
ATOM   2027 N  NZ    . LYS A 1 254 ? 36.68730  -33.52259 5.90365   1.000 48.73543  ? 265 LYS A NZ    1 
ATOM   2028 N  N     . GLU A 1 255 ? 29.85717  -34.51736 10.09306  1.000 33.34655  ? 266 GLU A N     1 
ATOM   2029 C  CA    . GLU A 1 255 ? 28.73778  -34.01393 10.88445  1.000 32.74335  ? 266 GLU A CA    1 
ATOM   2030 C  C     . GLU A 1 255 ? 28.19773  -35.06881 11.84184  1.000 32.22487  ? 266 GLU A C     1 
ATOM   2031 O  O     . GLU A 1 255 ? 27.71374  -34.73440 12.92673  1.000 34.97933  ? 266 GLU A O     1 
ATOM   2032 C  CB    . GLU A 1 255 ? 27.61560  -33.52437 9.96107   1.000 31.15181  ? 266 GLU A CB    1 
ATOM   2033 C  CG    . GLU A 1 255 ? 27.90613  -32.23279 9.22205   1.000 34.83050  ? 266 GLU A CG    1 
ATOM   2034 C  CD    . GLU A 1 255 ? 28.25370  -31.09172 10.16421  1.000 45.20040  ? 266 GLU A CD    1 
ATOM   2035 O  OE1   . GLU A 1 255 ? 27.71913  -31.07335 11.30277  1.000 41.38846  ? 266 GLU A OE1   1 
ATOM   2036 O  OE2   . GLU A 1 255 ? 29.07851  -30.23321 9.77320   1.000 41.46072  ? 266 GLU A OE2   1 
ATOM   2037 N  N     . PHE A 1 256 ? 28.25590  -36.34258 11.45429  1.000 33.42971  ? 267 PHE A N     1 
ATOM   2038 C  CA    . PHE A 1 256 ? 27.70691  -37.42902 12.24973  1.000 27.42418  ? 267 PHE A CA    1 
ATOM   2039 C  C     . PHE A 1 256 ? 28.78594  -38.21605 12.98218  1.000 33.24434  ? 267 PHE A C     1 
ATOM   2040 O  O     . PHE A 1 256 ? 28.57001  -39.38210 13.31718  1.000 31.58199  ? 267 PHE A O     1 
ATOM   2041 C  CB    . PHE A 1 256 ? 26.87631  -38.34694 11.35809  1.000 33.41205  ? 267 PHE A CB    1 
ATOM   2042 C  CG    . PHE A 1 256 ? 25.47688  -37.85956 11.15190  1.000 31.72637  ? 267 PHE A CG    1 
ATOM   2043 C  CD1   . PHE A 1 256 ? 25.23551  -36.65281 10.51204  1.000 28.64404  ? 267 PHE A CD1   1 
ATOM   2044 C  CD2   . PHE A 1 256 ? 24.40201  -38.58909 11.62311  1.000 31.20030  ? 267 PHE A CD2   1 
ATOM   2045 C  CE1   . PHE A 1 256 ? 23.94633  -36.19218 10.34141  1.000 31.78034  ? 267 PHE A CE1   1 
ATOM   2046 C  CE2   . PHE A 1 256 ? 23.10277  -38.12014 11.45979  1.000 30.07033  ? 267 PHE A CE2   1 
ATOM   2047 C  CZ    . PHE A 1 256 ? 22.87983  -36.92632 10.82526  1.000 23.43142  ? 267 PHE A CZ    1 
ATOM   2048 N  N     . SER A 1 257 ? 29.93499  -37.58662 13.26036  1.000 28.62106  ? 268 SER A N     1 
ATOM   2049 C  CA    . SER A 1 257 ? 31.08508  -38.31990 13.77950  1.000 32.74472  ? 268 SER A CA    1 
ATOM   2050 C  C     . SER A 1 257 ? 30.79000  -38.99996 15.10855  1.000 31.01511  ? 268 SER A C     1 
ATOM   2051 O  O     . SER A 1 257 ? 31.33231  -40.07005 15.38339  1.000 29.71406  ? 268 SER A O     1 
ATOM   2052 C  CB    . SER A 1 257 ? 32.28603  -37.38724 13.93329  1.000 32.59895  ? 268 SER A CB    1 
ATOM   2053 O  OG    . SER A 1 257 ? 31.93470  -36.29057 14.74856  1.000 39.33926  ? 268 SER A OG    1 
ATOM   2054 N  N     . ASP A 1 258 ? 29.94036  -38.42203 15.95141  1.000 33.04698  ? 269 ASP A N     1 
ATOM   2055 C  CA    . ASP A 1 258 ? 29.66445  -39.08128 17.22137  1.000 41.53726  ? 269 ASP A CA    1 
ATOM   2056 C  C     . ASP A 1 258 ? 28.33114  -39.82752 17.22170  1.000 38.49238  ? 269 ASP A C     1 
ATOM   2057 O  O     . ASP A 1 258 ? 27.81618  -40.15657 18.29284  1.000 38.13807  ? 269 ASP A O     1 
ATOM   2058 C  CB    . ASP A 1 258 ? 29.75852  -38.08467 18.38359  1.000 43.99320  ? 269 ASP A CB    1 
ATOM   2059 C  CG    . ASP A 1 258 ? 28.80216  -36.92809 18.25299  1.000 50.76829  ? 269 ASP A CG    1 
ATOM   2060 O  OD1   . ASP A 1 258 ? 28.92218  -35.99442 19.08228  1.000 54.75264  ? 269 ASP A OD1   1 
ATOM   2061 O  OD2   . ASP A 1 258 ? 27.93091  -36.94511 17.34584  1.000 56.74485  ? 269 ASP A OD2   1 
ATOM   2062 N  N     . TRP A 1 259 ? 27.78928  -40.13805 16.04629  1.000 29.37263  ? 270 TRP A N     1 
ATOM   2063 C  CA    . TRP A 1 259 ? 26.59953  -40.96960 15.95736  1.000 32.28684  ? 270 TRP A CA    1 
ATOM   2064 C  C     . TRP A 1 259 ? 26.97339  -42.44590 15.84206  1.000 32.26947  ? 270 TRP A C     1 
ATOM   2065 O  O     . TRP A 1 259 ? 28.05252  -42.81415 15.37358  1.000 32.94139  ? 270 TRP A O     1 
ATOM   2066 C  CB    . TRP A 1 259 ? 25.73601  -40.57253 14.76113  1.000 26.12190  ? 270 TRP A CB    1 
ATOM   2067 C  CG    . TRP A 1 259 ? 25.07814  -39.23777 14.87586  1.000 33.95319  ? 270 TRP A CG    1 
ATOM   2068 C  CD1   . TRP A 1 259 ? 25.68545  -38.03592 15.08871  1.000 31.30586  ? 270 TRP A CD1   1 
ATOM   2069 C  CD2   . TRP A 1 259 ? 23.67595  -38.96579 14.76349  1.000 28.40681  ? 270 TRP A CD2   1 
ATOM   2070 N  NE1   . TRP A 1 259 ? 24.74875  -37.03060 15.10336  1.000 30.87963  ? 270 TRP A NE1   1 
ATOM   2071 C  CE2   . TRP A 1 259 ? 23.50876  -37.57443 14.90038  1.000 30.56362  ? 270 TRP A CE2   1 
ATOM   2072 C  CE3   . TRP A 1 259 ? 22.54920  -39.76292 14.53206  1.000 30.78154  ? 270 TRP A CE3   1 
ATOM   2073 C  CZ2   . TRP A 1 259 ? 22.25383  -36.95784 14.83690  1.000 31.38114  ? 270 TRP A CZ2   1 
ATOM   2074 C  CZ3   . TRP A 1 259 ? 21.30347  -39.15199 14.46601  1.000 29.93439  ? 270 TRP A CZ3   1 
ATOM   2075 C  CH2   . TRP A 1 259 ? 21.16683  -37.76080 14.62166  1.000 31.57807  ? 270 TRP A CH2   1 
ATOM   2076 N  N     . ASP A 1 260 ? 26.04526  -43.28754 16.27378  1.000 30.62341  ? 271 ASP A N     1 
ATOM   2077 C  CA    . ASP A 1 260 ? 26.21579  -44.72924 16.24555  1.000 27.60926  ? 271 ASP A CA    1 
ATOM   2078 C  C     . ASP A 1 260 ? 26.46959  -45.21060 14.81449  1.000 30.16960  ? 271 ASP A C     1 
ATOM   2079 O  O     . ASP A 1 260 ? 25.96558  -44.63661 13.84610  1.000 28.03506  ? 271 ASP A O     1 
ATOM   2080 C  CB    . ASP A 1 260 ? 24.96278  -45.37103 16.85150  1.000 28.94304  ? 271 ASP A CB    1 
ATOM   2081 C  CG    . ASP A 1 260 ? 25.03006  -46.87212 16.90916  1.000 30.21949  ? 271 ASP A CG    1 
ATOM   2082 O  OD1   . ASP A 1 260 ? 24.71076  -47.51890 15.89205  1.000 26.09016  ? 271 ASP A OD1   1 
ATOM   2083 O  OD2   . ASP A 1 260 ? 25.39007  -47.40056 17.97668  1.000 38.94728  ? 271 ASP A OD2   1 
ATOM   2084 N  N     . GLU A 1 261 ? 27.26825  -46.28162 14.69038  1.000 25.67576  ? 272 GLU A N     1 
ATOM   2085 C  CA    . GLU A 1 261 ? 27.65769  -46.79739 13.37680  1.000 25.38654  ? 272 GLU A CA    1 
ATOM   2086 C  C     . GLU A 1 261 ? 26.46049  -47.19045 12.52413  1.000 26.90922  ? 272 GLU A C     1 
ATOM   2087 O  O     . GLU A 1 261 ? 26.55496  -47.17357 11.29451  1.000 27.03043  ? 272 GLU A O     1 
ATOM   2088 C  CB    . GLU A 1 261 ? 28.59442  -47.99855 13.52048  1.000 25.41842  ? 272 GLU A CB    1 
ATOM   2089 C  CG    . GLU A 1 261 ? 29.95597  -47.62463 14.06313  1.000 29.22468  ? 272 GLU A CG    1 
ATOM   2090 C  CD    . GLU A 1 261 ? 30.81725  -46.89661 13.03428  1.000 29.48674  ? 272 GLU A CD    1 
ATOM   2091 O  OE1   . GLU A 1 261 ? 30.44286  -46.85954 11.83732  1.000 31.44555  ? 272 GLU A OE1   1 
ATOM   2092 O  OE2   . GLU A 1 261 ? 31.87787  -46.36603 13.42082  1.000 36.75619  ? 272 GLU A OE2   1 
ATOM   2093 N  N     . ARG A 1 262 ? 25.33624  -47.55995 13.13791  1.000 27.40575  ? 273 ARG A N     1 
ATOM   2094 C  CA    . ARG A 1 262 ? 24.15480  -47.85973 12.33211  1.000 25.45950  ? 273 ARG A CA    1 
ATOM   2095 C  C     . ARG A 1 262 ? 23.75894  -46.66551 11.47365  1.000 26.54792  ? 273 ARG A C     1 
ATOM   2096 O  O     . ARG A 1 262 ? 23.39168  -46.82890 10.30257  1.000 28.61227  ? 273 ARG A O     1 
ATOM   2097 C  CB    . ARG A 1 262 ? 23.00003  -48.29223 13.22776  1.000 25.90522  ? 273 ARG A CB    1 
ATOM   2098 C  CG    . ARG A 1 262 ? 23.12134  -49.72058 13.70680  1.000 27.82339  ? 273 ARG A CG    1 
ATOM   2099 C  CD    . ARG A 1 262 ? 22.17491  -49.98093 14.85480  1.000 30.39202  ? 273 ARG A CD    1 
ATOM   2100 N  NE    . ARG A 1 262 ? 22.64077  -49.35659 16.08385  1.000 28.74016  ? 273 ARG A NE    1 
ATOM   2101 C  CZ    . ARG A 1 262 ? 22.12356  -49.59372 17.27852  1.000 37.29479  ? 273 ARG A CZ    1 
ATOM   2102 N  NH1   . ARG A 1 262 ? 21.08102  -50.39351 17.42662  1.000 36.46135  ? 273 ARG A NH1   1 
ATOM   2103 N  NH2   . ARG A 1 262 ? 22.67221  -49.02129 18.35080  1.000 35.16368  ? 273 ARG A NH2   1 
ATOM   2104 N  N     . TYR A 1 263 ? 23.84838  -45.45269 12.02706  1.000 27.16682  ? 274 TYR A N     1 
ATOM   2105 C  CA    . TYR A 1 263 ? 23.58440  -44.26175 11.21981  1.000 25.86781  ? 274 TYR A CA    1 
ATOM   2106 C  C     . TYR A 1 263 ? 24.69678  -44.02707 10.20344  1.000 23.39785  ? 274 TYR A C     1 
ATOM   2107 O  O     . TYR A 1 263 ? 24.43500  -43.62862 9.06529   1.000 22.44074  ? 274 TYR A O     1 
ATOM   2108 C  CB    . TYR A 1 263 ? 23.44518  -43.03237 12.11079  1.000 26.99895  ? 274 TYR A CB    1 
ATOM   2109 C  CG    . TYR A 1 263 ? 22.36338  -43.08920 13.17073  1.000 27.06618  ? 274 TYR A CG    1 
ATOM   2110 C  CD1   . TYR A 1 263 ? 21.03679  -42.87901 12.84178  1.000 23.13507  ? 274 TYR A CD1   1 
ATOM   2111 C  CD2   . TYR A 1 263 ? 22.68410  -43.30303 14.50388  1.000 25.28795  ? 274 TYR A CD2   1 
ATOM   2112 C  CE1   . TYR A 1 263 ? 20.04417  -42.90829 13.80427  1.000 28.09985  ? 274 TYR A CE1   1 
ATOM   2113 C  CE2   . TYR A 1 263 ? 21.70479  -43.33096 15.48247  1.000 30.97247  ? 274 TYR A CE2   1 
ATOM   2114 C  CZ    . TYR A 1 263 ? 20.37692  -43.13379 15.12201  1.000 34.58101  ? 274 TYR A CZ    1 
ATOM   2115 O  OH    . TYR A 1 263 ? 19.37949  -43.16143 16.07546  1.000 30.86287  ? 274 TYR A OH    1 
ATOM   2116 N  N     . LYS A 1 264 ? 25.95092  -44.23454 10.60858  1.000 29.02960  ? 275 LYS A N     1 
ATOM   2117 C  CA    . LYS A 1 264 ? 27.07069  -43.98937 9.70189   1.000 25.94529  ? 275 LYS A CA    1 
ATOM   2118 C  C     . LYS A 1 264 ? 27.03595  -44.94050 8.51345   1.000 24.37061  ? 275 LYS A C     1 
ATOM   2119 O  O     . LYS A 1 264 ? 27.37057  -44.55014 7.38919   1.000 27.99354  ? 275 LYS A O     1 
ATOM   2120 C  CB    . LYS A 1 264 ? 28.39366  -44.12080 10.45530  1.000 25.43271  ? 275 LYS A CB    1 
ATOM   2121 C  CG    . LYS A 1 264 ? 28.62367  -43.05835 11.51548  1.000 26.68056  ? 275 LYS A CG    1 
ATOM   2122 C  CD    . LYS A 1 264 ? 30.06611  -43.09508 11.99354  1.000 26.88964  ? 275 LYS A CD    1 
ATOM   2123 C  CE    . LYS A 1 264 ? 30.32184  -42.03957 13.07881  1.000 31.63260  ? 275 LYS A CE    1 
ATOM   2124 N  NZ    . LYS A 1 264 ? 31.78043  -41.85473 13.33123  1.000 33.79890  ? 275 LYS A NZ    1 
ATOM   2125 N  N     . GLU A 1 265 ? 26.62757  -46.19468 8.74652   1.000 26.94128  ? 276 GLU A N     1 
ATOM   2126 C  CA    . GLU A 1 265 ? 26.46231  -47.15627 7.66030   1.000 28.41263  ? 276 GLU A CA    1 
ATOM   2127 C  C     . GLU A 1 265 ? 25.45848  -46.64653 6.63705   1.000 26.42641  ? 276 GLU A C     1 
ATOM   2128 O  O     . GLU A 1 265 ? 25.66209  -46.78442 5.42077   1.000 30.40014  ? 276 GLU A O     1 
ATOM   2129 C  CB    . GLU A 1 265 ? 26.02045  -48.51418 8.23014   1.000 29.68665  ? 276 GLU A CB    1 
ATOM   2130 C  CG    . GLU A 1 265 ? 25.77474  -49.61331 7.17421   1.000 34.17723  ? 276 GLU A CG    1 
ATOM   2131 C  CD    . GLU A 1 265 ? 25.53377  -51.01001 7.78297   1.000 45.69051  ? 276 GLU A CD    1 
ATOM   2132 O  OE1   . GLU A 1 265 ? 24.57425  -51.17659 8.58228   1.000 37.77832  ? 276 GLU A OE1   1 
ATOM   2133 O  OE2   . GLU A 1 265 ? 26.31308  -51.94393 7.45796   1.000 46.35522  ? 276 GLU A OE2   1 
ATOM   2134 N  N     . LEU A 1 266 ? 24.37337  -46.04427 7.11969   1.000 25.27577  ? 277 LEU A N     1 
ATOM   2135 C  CA    . LEU A 1 266 ? 23.37605  -45.44082 6.24778   1.000 26.09493  ? 277 LEU A CA    1 
ATOM   2136 C  C     . LEU A 1 266 ? 24.01918  -44.46452 5.26846   1.000 24.85097  ? 277 LEU A C     1 
ATOM   2137 O  O     . LEU A 1 266 ? 23.79254  -44.53336 4.05566   1.000 24.11230  ? 277 LEU A O     1 
ATOM   2138 C  CB    . LEU A 1 266 ? 22.33716  -44.74013 7.11921   1.000 28.34653  ? 277 LEU A CB    1 
ATOM   2139 C  CG    . LEU A 1 266 ? 20.93921  -44.43537 6.62215   1.000 38.75043  ? 277 LEU A CG    1 
ATOM   2140 C  CD1   . LEU A 1 266 ? 20.25539  -45.73878 6.29925   1.000 34.80502  ? 277 LEU A CD1   1 
ATOM   2141 C  CD2   . LEU A 1 266 ? 20.19091  -43.68786 7.73554   1.000 31.53123  ? 277 LEU A CD2   1 
ATOM   2142 N  N     . ILE A 1 267 ? 24.83738  -43.54855 5.78665   1.000 25.74669  ? 278 ILE A N     1 
ATOM   2143 C  CA    . ILE A 1 267 ? 25.55258  -42.60048 4.93406   1.000 23.23359  ? 278 ILE A CA    1 
ATOM   2144 C  C     . ILE A 1 267 ? 26.50279  -43.33012 3.98388   1.000 28.78106  ? 278 ILE A C     1 
ATOM   2145 O  O     . ILE A 1 267 ? 26.60322  -42.98542 2.79832   1.000 30.09692  ? 278 ILE A O     1 
ATOM   2146 C  CB    . ILE A 1 267 ? 26.29165  -41.58782 5.82600   1.000 31.69036  ? 278 ILE A CB    1 
ATOM   2147 C  CG1   . ILE A 1 267 ? 25.27071  -40.75138 6.59277   1.000 22.69598  ? 278 ILE A CG1   1 
ATOM   2148 C  CG2   . ILE A 1 267 ? 27.27217  -40.72425 5.02387   1.000 26.26037  ? 278 ILE A CG2   1 
ATOM   2149 C  CD1   . ILE A 1 267 ? 25.81421  -40.17092 7.88203   1.000 24.28733  ? 278 ILE A CD1   1 
ATOM   2150 N  N     . ARG A 1 268 ? 27.19446  -44.36630 4.48167   1.000 24.41818  ? 279 ARG A N     1 
ATOM   2151 C  CA    . ARG A 1 268 ? 28.26166  -45.00599 3.71048   1.000 27.03523  ? 279 ARG A CA    1 
ATOM   2152 C  C     . ARG A 1 268 ? 27.72510  -45.79615 2.51854   1.000 27.85424  ? 279 ARG A C     1 
ATOM   2153 O  O     . ARG A 1 268 ? 28.40964  -45.89198 1.49760   1.000 27.75555  ? 279 ARG A O     1 
ATOM   2154 C  CB    . ARG A 1 268 ? 29.11111  -45.92021 4.61554   1.000 23.56686  ? 279 ARG A CB    1 
ATOM   2155 C  CG    . ARG A 1 268 ? 30.22232  -45.18618 5.40723   1.000 28.06484  ? 279 ARG A CG    1 
ATOM   2156 C  CD    . ARG A 1 268 ? 31.12511  -46.13712 6.19156   1.000 26.46874  ? 279 ARG A CD    1 
ATOM   2157 N  NE    . ARG A 1 268 ? 30.37604  -47.04203 7.05690   1.000 29.71401  ? 279 ARG A NE    1 
ATOM   2158 C  CZ    . ARG A 1 268 ? 30.33851  -46.97511 8.38361   1.000 31.62152  ? 279 ARG A CZ    1 
ATOM   2159 N  NH1   . ARG A 1 268 ? 31.03824  -46.06976 9.05821   1.000 33.51124  ? 279 ARG A NH1   1 
ATOM   2160 N  NH2   . ARG A 1 268 ? 29.58821  -47.84585 9.05492   1.000 27.23939  ? 279 ARG A NH2   1 
ATOM   2161 N  N     . VAL A 1 269 ? 26.50612  -46.34347 2.60345   1.000 25.06027  ? 280 VAL A N     1 
ATOM   2162 C  CA    . VAL A 1 269 ? 25.99703  -47.21403 1.54221   1.000 27.39395  ? 280 VAL A CA    1 
ATOM   2163 C  C     . VAL A 1 269 ? 25.07398  -46.50571 0.56058   1.000 26.56176  ? 280 VAL A C     1 
ATOM   2164 O  O     . VAL A 1 269 ? 24.66096  -47.12325 -0.43303  1.000 33.44427  ? 280 VAL A O     1 
ATOM   2165 C  CB    . VAL A 1 269 ? 25.25546  -48.43750 2.12108   1.000 28.96253  ? 280 VAL A CB    1 
ATOM   2166 C  CG1   . VAL A 1 269 ? 26.16483  -49.21428 3.05057   1.000 27.21714  ? 280 VAL A CG1   1 
ATOM   2167 C  CG2   . VAL A 1 269 ? 23.96608  -47.98765 2.82330   1.000 26.12699  ? 280 VAL A CG2   1 
ATOM   2168 N  N     . THR A 1 270 ? 24.73470  -45.24682 0.80104   1.000 25.77988  ? 281 THR A N     1 
ATOM   2169 C  CA    . THR A 1 270 ? 23.84879  -44.51449 -0.09109  1.000 25.07080  ? 281 THR A CA    1 
ATOM   2170 C  C     . THR A 1 270 ? 24.50886  -44.29541 -1.44415  1.000 27.85086  ? 281 THR A C     1 
ATOM   2171 O  O     . THR A 1 270 ? 25.63850  -43.81169 -1.51803  1.000 26.27402  ? 281 THR A O     1 
ATOM   2172 C  CB    . THR A 1 270 ? 23.49100  -43.16791 0.53493   1.000 28.36217  ? 281 THR A CB    1 
ATOM   2173 O  OG1   . THR A 1 270 ? 22.69740  -43.37996 1.71202   1.000 31.60018  ? 281 THR A OG1   1 
ATOM   2174 C  CG2   . THR A 1 270 ? 22.75075  -42.31406 -0.45297  1.000 25.76062  ? 281 THR A CG2   1 
ATOM   2175 N  N     . SER A 1 271 ? 23.80012  -44.62105 -2.52671  1.000 22.42510  ? 282 SER A N     1 
ATOM   2176 C  CA    . SER A 1 271 ? 24.44555  -44.48903 -3.82628  1.000 29.29776  ? 282 SER A CA    1 
ATOM   2177 C  C     . SER A 1 271 ? 24.43268  -43.05140 -4.33508  1.000 28.83364  ? 282 SER A C     1 
ATOM   2178 O  O     . SER A 1 271 ? 25.39436  -42.63069 -4.98240  1.000 35.95428  ? 282 SER A O     1 
ATOM   2179 C  CB    . SER A 1 271 ? 23.80343  -45.43679 -4.84151  1.000 34.17295  ? 282 SER A CB    1 
ATOM   2180 O  OG    . SER A 1 271 ? 22.39396  -45.36290 -4.78839  1.000 46.73510  ? 282 SER A OG    1 
ATOM   2181 N  N     . SER A 1 272 ? 23.38747  -42.27589 -4.04302  1.000 29.55296  ? 283 SER A N     1 
ATOM   2182 C  CA    . SER A 1 272 ? 23.36776  -40.87537 -4.44256  1.000 28.21485  ? 283 SER A CA    1 
ATOM   2183 C  C     . SER A 1 272 ? 22.48586  -40.07967 -3.48744  1.000 29.79452  ? 283 SER A C     1 
ATOM   2184 O  O     . SER A 1 272 ? 21.53326  -40.61320 -2.90884  1.000 32.18485  ? 283 SER A O     1 
ATOM   2185 C  CB    . SER A 1 272 ? 22.88953  -40.71096 -5.88926  1.000 34.08632  ? 283 SER A CB    1 
ATOM   2186 O  OG    . SER A 1 272 ? 21.59755  -41.25516 -6.05967  1.000 39.54727  ? 283 SER A OG    1 
ATOM   2187 N  N     . PHE A 1 273 ? 22.82886  -38.79812 -3.31614  1.000 25.62557  ? 284 PHE A N     1 
ATOM   2188 C  CA    . PHE A 1 273 ? 22.14565  -37.89188 -2.39958  1.000 27.85424  ? 284 PHE A CA    1 
ATOM   2189 C  C     . PHE A 1 273 ? 21.54343  -36.71788 -3.16657  1.000 29.63569  ? 284 PHE A C     1 
ATOM   2190 O  O     . PHE A 1 273 ? 22.06817  -36.29395 -4.19883  1.000 27.44191  ? 284 PHE A O     1 
ATOM   2191 C  CB    . PHE A 1 273 ? 23.09548  -37.31809 -1.32785  1.000 25.01170  ? 284 PHE A CB    1 
ATOM   2192 C  CG    . PHE A 1 273 ? 23.84404  -38.35981 -0.51297  1.000 25.80322  ? 284 PHE A CG    1 
ATOM   2193 C  CD1   . PHE A 1 273 ? 24.95843  -38.99717 -1.02350  1.000 22.46558  ? 284 PHE A CD1   1 
ATOM   2194 C  CD2   . PHE A 1 273 ? 23.46110  -38.64690 0.78923   1.000 26.31627  ? 284 PHE A CD2   1 
ATOM   2195 C  CE1   . PHE A 1 273 ? 25.66206  -39.94167 -0.26232  1.000 26.50547  ? 284 PHE A CE1   1 
ATOM   2196 C  CE2   . PHE A 1 273 ? 24.16811  -39.58582 1.56197   1.000 29.45751  ? 284 PHE A CE2   1 
ATOM   2197 C  CZ    . PHE A 1 273 ? 25.26958  -40.22820 1.03687   1.000 21.77977  ? 284 PHE A CZ    1 
ATOM   2198 N  N     . VAL A 1 274 ? 20.46357  -36.15840 -2.62964  1.000 30.85521  ? 285 VAL A N     1 
ATOM   2199 C  CA    . VAL A 1 274 ? 19.83315  -34.96160 -3.18218  1.000 28.91297  ? 285 VAL A CA    1 
ATOM   2200 C  C     . VAL A 1 274 ? 19.85128  -33.88808 -2.10684  1.000 30.84604  ? 285 VAL A C     1 
ATOM   2201 O  O     . VAL A 1 274 ? 19.28680  -34.08481 -1.02153  1.000 29.35329  ? 285 VAL A O     1 
ATOM   2202 C  CB    . VAL A 1 274 ? 18.39450  -35.22916 -3.64907  1.000 31.53069  ? 285 VAL A CB    1 
ATOM   2203 C  CG1   . VAL A 1 274 ? 17.72366  -33.92104 -4.07246  1.000 29.88987  ? 285 VAL A CG1   1 
ATOM   2204 C  CG2   . VAL A 1 274 ? 18.37827  -36.23655 -4.78175  1.000 25.38300  ? 285 VAL A CG2   1 
ATOM   2205 N  N     . GLY A 1 275 ? 20.50559  -32.76167 -2.39966  1.000 24.28536  ? 286 GLY A N     1 
ATOM   2206 C  CA    . GLY A 1 275 ? 20.46256  -31.61092 -1.52054  1.000 25.75430  ? 286 GLY A CA    1 
ATOM   2207 C  C     . GLY A 1 275 ? 19.34432  -30.63754 -1.88744  1.000 30.65762  ? 286 GLY A C     1 
ATOM   2208 O  O     . GLY A 1 275 ? 18.97130  -30.49974 -3.05039  1.000 29.26075  ? 286 GLY A O     1 
ATOM   2209 N  N     . LEU A 1 276 ? 18.82083  -29.94098 -0.87564  1.000 29.17040  ? 287 LEU A N     1 
ATOM   2210 C  CA    . LEU A 1 276 ? 17.68654  -29.03163 -1.07077  1.000 31.22053  ? 287 LEU A CA    1 
ATOM   2211 C  C     . LEU A 1 276 ? 17.65071  -28.00165 0.05078   1.000 27.65660  ? 287 LEU A C     1 
ATOM   2212 O  O     . LEU A 1 276 ? 17.50157  -28.36352 1.22693   1.000 24.90459  ? 287 LEU A O     1 
ATOM   2213 C  CB    . LEU A 1 276 ? 16.36930  -29.81720 -1.11651  1.000 32.03598  ? 287 LEU A CB    1 
ATOM   2214 C  CG    . LEU A 1 276 ? 15.09330  -28.96510 -1.05507  1.000 44.37487  ? 287 LEU A CG    1 
ATOM   2215 C  CD1   . LEU A 1 276 ? 14.57587  -28.56193 -2.44497  1.000 23.99828  ? 287 LEU A CD1   1 
ATOM   2216 C  CD2   . LEU A 1 276 ? 14.01936  -29.67503 -0.24240  1.000 39.61428  ? 287 LEU A CD2   1 
ATOM   2217 N  N     . ALA A 1 277 ? 17.77281  -26.72519 -0.30232  1.000 28.23879  ? 288 ALA A N     1 
ATOM   2218 C  CA    . ALA A 1 277 ? 17.59558  -25.66590 0.68169   1.000 28.92154  ? 288 ALA A CA    1 
ATOM   2219 C  C     . ALA A 1 277 ? 16.12247  -25.54332 1.06513   1.000 31.99695  ? 288 ALA A C     1 
ATOM   2220 O  O     . ALA A 1 277 ? 15.23589  -25.59406 0.20846   1.000 30.33381  ? 288 ALA A O     1 
ATOM   2221 C  CB    . ALA A 1 277 ? 18.10647  -24.33414 0.13500   1.000 27.59526  ? 288 ALA A CB    1 
ATOM   2222 N  N     . THR A 1 278 ? 15.86227  -25.40034 2.36305   1.000 25.83247  ? 289 THR A N     1 
ATOM   2223 C  CA    . THR A 1 278 ? 14.50589  -25.14759 2.81559   1.000 27.58498  ? 289 THR A CA    1 
ATOM   2224 C  C     . THR A 1 278 ? 14.05353  -23.75932 2.38483   1.000 26.55231  ? 289 THR A C     1 
ATOM   2225 O  O     . THR A 1 278 ? 14.78555  -22.77564 2.52503   1.000 26.07786  ? 289 THR A O     1 
ATOM   2226 C  CB    . THR A 1 278 ? 14.40829  -25.27002 4.32915   1.000 28.89328  ? 289 THR A CB    1 
ATOM   2227 O  OG1   . THR A 1 278 ? 14.97091  -26.52193 4.74882   1.000 27.87783  ? 289 THR A OG1   1 
ATOM   2228 C  CG2   . THR A 1 278 ? 12.94656  -25.19935 4.76405   1.000 21.77414  ? 289 THR A CG2   1 
ATOM   2229 N  N     . ARG A 1 279 ? 12.83503  -23.67879 1.85954   1.000 26.25140  ? 290 ARG A N     1 
ATOM   2230 C  CA    . ARG A 1 279 ? 12.30384  -22.41744 1.36843   1.000 25.17255  ? 290 ARG A CA    1 
ATOM   2231 C  C     . ARG A 1 279 ? 10.88039  -22.20886 1.85661   1.000 25.35219  ? 290 ARG A C     1 
ATOM   2232 O  O     . ARG A 1 279 ? 10.17715  -23.14910 2.24839   1.000 25.36140  ? 290 ARG A O     1 
ATOM   2233 C  CB    . ARG A 1 279 ? 12.35832  -22.35598 -0.16287  1.000 26.35486  ? 290 ARG A CB    1 
ATOM   2234 C  CG    . ARG A 1 279 ? 13.78609  -22.30271 -0.68961  1.000 26.10765  ? 290 ARG A CG    1 
ATOM   2235 C  CD    . ARG A 1 279 ? 13.81674  -22.18788 -2.20527  1.000 29.78209  ? 290 ARG A CD    1 
ATOM   2236 N  NE    . ARG A 1 279 ? 15.17776  -21.98165 -2.68371  1.000 34.33888  ? 290 ARG A NE    1 
ATOM   2237 C  CZ    . ARG A 1 279 ? 15.99151  -22.96234 -3.04815  1.000 34.98027  ? 290 ARG A CZ    1 
ATOM   2238 N  NH1   . ARG A 1 279 ? 15.58199  -24.22366 -3.07778  1.000 25.79968  ? 290 ARG A NH1   1 
ATOM   2239 N  NH2   . ARG A 1 279 ? 17.24507  -22.67152 -3.38585  1.000 27.84170  ? 290 ARG A NH2   1 
ATOM   2240 N  N     . ILE A 1 280 ? 10.46926  -20.94556 1.83569   1.000 25.54365  ? 291 ILE A N     1 
ATOM   2241 C  CA    . ILE A 1 280 ? 9.11657   -20.54933 2.19587   1.000 23.30858  ? 291 ILE A CA    1 
ATOM   2242 C  C     . ILE A 1 280 ? 8.64706   -19.50291 1.19125   1.000 26.00661  ? 291 ILE A C     1 
ATOM   2243 O  O     . ILE A 1 280 ? 9.43150   -18.65683 0.74552   1.000 22.31754  ? 291 ILE A O     1 
ATOM   2244 C  CB    . ILE A 1 280 ? 9.05964   -20.02422 3.64759   1.000 21.82599  ? 291 ILE A CB    1 
ATOM   2245 C  CG1   . ILE A 1 280 ? 7.62233   -19.66793 4.05063   1.000 22.55175  ? 291 ILE A CG1   1 
ATOM   2246 C  CG2   . ILE A 1 280 ? 9.99618   -18.84094 3.83601   1.000 23.57979  ? 291 ILE A CG2   1 
ATOM   2247 C  CD1   . ILE A 1 280 ? 7.47016   -19.31859 5.55049   1.000 27.62987  ? 291 ILE A CD1   1 
ATOM   2248 N  N     . PHE A 1 281 ? 7.37619   -19.59392 0.79664   1.000 23.64806  ? 292 PHE A N     1 
ATOM   2249 C  CA    . PHE A 1 281 ? 6.73139   -18.55465 -0.00088  1.000 22.65819  ? 292 PHE A CA    1 
ATOM   2250 C  C     . PHE A 1 281 ? 5.79255   -17.78354 0.91891   1.000 23.95201  ? 292 PHE A C     1 
ATOM   2251 O  O     . PHE A 1 281 ? 4.63049   -18.17222 1.10030   1.000 22.65437  ? 292 PHE A O     1 
ATOM   2252 C  CB    . PHE A 1 281 ? 5.98346   -19.16515 -1.18248  1.000 24.27666  ? 292 PHE A CB    1 
ATOM   2253 C  CG    . PHE A 1 281 ? 5.49626   -18.15229 -2.16651  1.000 29.17619  ? 292 PHE A CG    1 
ATOM   2254 C  CD1   . PHE A 1 281 ? 6.37956   -17.55042 -3.05511  1.000 24.73980  ? 292 PHE A CD1   1 
ATOM   2255 C  CD2   . PHE A 1 281 ? 4.16168   -17.79266 -2.20379  1.000 21.26850  ? 292 PHE A CD2   1 
ATOM   2256 C  CE1   . PHE A 1 281 ? 5.93633   -16.60181 -3.95139  1.000 25.10555  ? 292 PHE A CE1   1 
ATOM   2257 C  CE2   . PHE A 1 281 ? 3.71677   -16.83888 -3.10615  1.000 24.90671  ? 292 PHE A CE2   1 
ATOM   2258 C  CZ    . PHE A 1 281 ? 4.60641   -16.25079 -3.97716  1.000 27.84737  ? 292 PHE A CZ    1 
ATOM   2259 N  N     . PRO A 1 282 ? 6.25989   -16.70533 1.54063   1.000 21.80709  ? 293 PRO A N     1 
ATOM   2260 C  CA    . PRO A 1 282 ? 5.57110   -16.20154 2.73824   1.000 23.94068  ? 293 PRO A CA    1 
ATOM   2261 C  C     . PRO A 1 282 ? 4.23897   -15.55624 2.38878   1.000 28.66157  ? 293 PRO A C     1 
ATOM   2262 O  O     . PRO A 1 282 ? 4.15161   -14.74749 1.46388   1.000 29.55182  ? 293 PRO A O     1 
ATOM   2263 C  CB    . PRO A 1 282 ? 6.56642   -15.18745 3.32033   1.000 31.67837  ? 293 PRO A CB    1 
ATOM   2264 C  CG    . PRO A 1 282 ? 7.34630   -14.68848 2.09334   1.000 35.54855  ? 293 PRO A CG    1 
ATOM   2265 C  CD    . PRO A 1 282 ? 7.43665   -15.89226 1.17226   1.000 31.44665  ? 293 PRO A CD    1 
ATOM   2266 N  N     . LEU A 1 283 ? 3.19540   -15.93712 3.12918   1.000 26.01878  ? 294 LEU A N     1 
ATOM   2267 C  CA    . LEU A 1 283 ? 1.89992   -15.26933 3.04203   1.000 29.87470  ? 294 LEU A CA    1 
ATOM   2268 C  C     . LEU A 1 283 ? 1.89791   -14.05628 3.96407   1.000 34.42644  ? 294 LEU A C     1 
ATOM   2269 O  O     . LEU A 1 283 ? 2.02109   -14.20109 5.18588   1.000 33.49573  ? 294 LEU A O     1 
ATOM   2270 C  CB    . LEU A 1 283 ? 0.76557   -16.21788 3.42697   1.000 32.26491  ? 294 LEU A CB    1 
ATOM   2271 C  CG    . LEU A 1 283 ? 0.41764   -17.38654 2.50224   1.000 32.46952  ? 294 LEU A CG    1 
ATOM   2272 C  CD1   . LEU A 1 283 ? -0.49755  -18.32937 3.24057   1.000 20.87573  ? 294 LEU A CD1   1 
ATOM   2273 C  CD2   . LEU A 1 283 ? -0.25078  -16.86675 1.24381   1.000 26.87912  ? 294 LEU A CD2   1 
ATOM   2274 N  N     . GLY A 1 284 ? 1.74007   -12.86662 3.38759   1.000 39.71813  ? 295 GLY A N     1 
ATOM   2275 C  CA    . GLY A 1 284 ? 1.74273   -11.65151 4.17782   1.000 36.42127  ? 295 GLY A CA    1 
ATOM   2276 C  C     . GLY A 1 284 ? 0.60028   -10.73332 3.80237   1.000 43.53133  ? 295 GLY A C     1 
ATOM   2277 O  O     . GLY A 1 284 ? -0.56232  -11.02236 4.09934   1.000 40.24835  ? 295 GLY A O     1 
ATOM   2278 N  N     . LYS A 1 285 ? 0.92411   -9.62200  3.14811   1.000 42.20896  ? 296 LYS A N     1 
ATOM   2279 C  CA    . LYS A 1 285 ? -0.10166  -8.74746  2.60576   1.000 50.05282  ? 296 LYS A CA    1 
ATOM   2280 C  C     . LYS A 1 285 ? -0.88469  -9.47272  1.51365   1.000 47.64473  ? 296 LYS A C     1 
ATOM   2281 O  O     . LYS A 1 285 ? -0.42713  -10.46109 0.92780   1.000 46.69993  ? 296 LYS A O     1 
ATOM   2282 C  CB    . LYS A 1 285 ? 0.52197   -7.46776  2.03995   1.000 50.27239  ? 296 LYS A CB    1 
ATOM   2283 C  CG    . LYS A 1 285 ? 1.48918   -6.75442  2.99381   1.000 54.82773  ? 296 LYS A CG    1 
ATOM   2284 C  CD    . LYS A 1 285 ? 2.25929   -5.64386  2.27460   1.000 58.29919  ? 296 LYS A CD    1 
ATOM   2285 C  CE    . LYS A 1 285 ? 3.69347   -5.53711  2.79048   1.000 68.60696  ? 296 LYS A CE    1 
ATOM   2286 N  NZ    . LYS A 1 285 ? 4.53901   -4.62630  1.95800   1.000 69.32069  ? 296 LYS A NZ    1 
ATOM   2287 N  N     A SER A 1 286 ? -2.07813  -8.96198  1.23727   0.463 44.40142  ? 297 SER A N     1 
ATOM   2288 N  N     B SER A 1 286 ? -2.08724  -8.96975  1.24527   0.537 44.39563  ? 297 SER A N     1 
ATOM   2289 C  CA    A SER A 1 286 ? -2.92430  -9.55863  0.22149   0.463 44.95581  ? 297 SER A CA    1 
ATOM   2290 C  CA    B SER A 1 286 ? -2.93988  -9.56770  0.22926   0.537 44.97858  ? 297 SER A CA    1 
ATOM   2291 C  C     A SER A 1 286 ? -2.20184  -9.62958  -1.11891  0.463 41.46322  ? 297 SER A C     1 
ATOM   2292 C  C     B SER A 1 286 ? -2.22845  -9.61281  -1.12083  0.537 41.48205  ? 297 SER A C     1 
ATOM   2293 O  O     A SER A 1 286 ? -1.26409  -8.87796  -1.40177  0.463 38.72741  ? 297 SER A O     1 
ATOM   2294 O  O     B SER A 1 286 ? -1.30900  -8.83610  -1.40694  0.537 38.71093  ? 297 SER A O     1 
ATOM   2295 C  CB    A SER A 1 286 ? -4.20903  -8.75168  0.05697   0.463 43.64487  ? 297 SER A CB    1 
ATOM   2296 C  CB    B SER A 1 286 ? -4.25573  -8.79148  0.09920   0.537 43.67359  ? 297 SER A CB    1 
ATOM   2297 O  OG    A SER A 1 286 ? -3.90282  -7.48895  -0.50317  0.463 38.44536  ? 297 SER A OG    1 
ATOM   2298 O  OG    B SER A 1 286 ? -5.17941  -9.14029  1.12214   0.537 46.01795  ? 297 SER A OG    1 
ATOM   2299 N  N     . TRP A 1 287 ? -2.66410  -10.55156 -1.95175  1.000 38.61465  ? 298 TRP A N     1 
ATOM   2300 C  CA    . TRP A 1 287 ? -2.17985  -10.65155 -3.31240  1.000 32.02421  ? 298 TRP A CA    1 
ATOM   2301 C  C     . TRP A 1 287 ? -2.74890  -9.49744  -4.14530  1.000 31.96113  ? 298 TRP A C     1 
ATOM   2302 O  O     . TRP A 1 287 ? -3.55141  -8.68691  -3.66729  1.000 28.52490  ? 298 TRP A O     1 
ATOM   2303 C  CB    . TRP A 1 287 ? -2.56269  -12.00926 -3.87144  1.000 28.53056  ? 298 TRP A CB    1 
ATOM   2304 C  CG    . TRP A 1 287 ? -1.71997  -13.09196 -3.32516  1.000 30.06559  ? 298 TRP A CG    1 
ATOM   2305 C  CD1   . TRP A 1 287 ? -0.54952  -12.95070 -2.61842  1.000 30.49649  ? 298 TRP A CD1   1 
ATOM   2306 C  CD2   . TRP A 1 287 ? -1.95165  -14.49751 -3.44587  1.000 23.02981  ? 298 TRP A CD2   1 
ATOM   2307 N  NE1   . TRP A 1 287 ? -0.03989  -14.18673 -2.30145  1.000 26.83881  ? 298 TRP A NE1   1 
ATOM   2308 C  CE2   . TRP A 1 287 ? -0.87789  -15.15362 -2.79611  1.000 27.06206  ? 298 TRP A CE2   1 
ATOM   2309 C  CE3   . TRP A 1 287 ? -2.96243  -15.26843 -4.04037  1.000 20.94892  ? 298 TRP A CE3   1 
ATOM   2310 C  CZ2   . TRP A 1 287 ? -0.78385  -16.54855 -2.72591  1.000 23.28920  ? 298 TRP A CZ2   1 
ATOM   2311 C  CZ3   . TRP A 1 287 ? -2.86679  -16.64854 -3.97911  1.000 23.62553  ? 298 TRP A CZ3   1 
ATOM   2312 C  CH2   . TRP A 1 287 ? -1.78246  -17.27828 -3.32368  1.000 20.98522  ? 298 TRP A CH2   1 
ATOM   2313 N  N     . LYS A 1 288 ? -2.33985  -9.42351  -5.41034  1.000 30.68421  ? 299 LYS A N     1 
ATOM   2314 C  CA    . LYS A 1 288 ? -2.79885  -8.34168  -6.27384  1.000 30.24872  ? 299 LYS A CA    1 
ATOM   2315 C  C     . LYS A 1 288 ? -4.29481  -8.44539  -6.52427  1.000 25.20304  ? 299 LYS A C     1 
ATOM   2316 O  O     . LYS A 1 288 ? -4.82405  -9.51985  -6.82261  1.000 27.50335  ? 299 LYS A O     1 
ATOM   2317 C  CB    . LYS A 1 288 ? -2.06439  -8.36128  -7.60773  1.000 28.35119  ? 299 LYS A CB    1 
ATOM   2318 C  CG    . LYS A 1 288 ? -0.57117  -8.29617  -7.48974  1.000 28.84296  ? 299 LYS A CG    1 
ATOM   2319 C  CD    . LYS A 1 288 ? 0.06461   -8.25316  -8.86279  1.000 26.28215  ? 299 LYS A CD    1 
ATOM   2320 C  CE    . LYS A 1 288 ? 1.55770   -8.02693  -8.75880  1.000 30.17808  ? 299 LYS A CE    1 
ATOM   2321 N  NZ    . LYS A 1 288 ? 2.23276   -8.03695  -10.09911 1.000 28.49115  ? 299 LYS A NZ    1 
ATOM   2322 N  N     . SER A 1 289 ? -4.98036  -7.31964  -6.41349  1.000 29.96123  ? 300 SER A N     1 
ATOM   2323 C  CA    . SER A 1 289 ? -6.38641  -7.24172  -6.78326  1.000 40.92676  ? 300 SER A CA    1 
ATOM   2324 C  C     . SER A 1 289 ? -6.53332  -6.73763  -8.21723  1.000 32.93400  ? 300 SER A C     1 
ATOM   2325 O  O     . SER A 1 289 ? -5.59364  -6.20752  -8.81940  1.000 37.53525  ? 300 SER A O     1 
ATOM   2326 C  CB    . SER A 1 289 ? -7.14563  -6.32438  -5.82481  1.000 38.32882  ? 300 SER A CB    1 
ATOM   2327 O  OG    . SER A 1 289 ? -6.70823  -4.99636  -5.99637  1.000 35.57134  ? 300 SER A OG    1 
ATOM   2328 N  N     A LYS A 1 290 ? -7.73898  -6.91286  -8.76204  0.192 36.40405  ? 301 LYS A N     1 
ATOM   2329 N  N     B LYS A 1 290 ? -7.74520  -6.89824  -8.74730  0.808 36.47930  ? 301 LYS A N     1 
ATOM   2330 C  CA    A LYS A 1 290 ? -8.08735  -6.43304  -10.10304 0.192 36.55350  ? 301 LYS A CA    1 
ATOM   2331 C  CA    B LYS A 1 290 ? -8.11507  -6.45914  -10.09555 0.808 36.56112  ? 301 LYS A CA    1 
ATOM   2332 C  C     A LYS A 1 290 ? -7.13032  -6.98296  -11.16240 0.192 36.26384  ? 301 LYS A C     1 
ATOM   2333 C  C     B LYS A 1 290 ? -7.12090  -6.97922  -11.13994 0.808 36.33625  ? 301 LYS A C     1 
ATOM   2334 O  O     A LYS A 1 290 ? -6.56503  -6.24040  -11.96754 0.192 37.14175  ? 301 LYS A O     1 
ATOM   2335 O  O     B LYS A 1 290 ? -6.51987  -6.21957  -11.90042 0.808 37.25930  ? 301 LYS A O     1 
ATOM   2336 C  CB    A LYS A 1 290 ? -8.12532  -4.90224  -10.14771 0.192 38.83200  ? 301 LYS A CB    1 
ATOM   2337 C  CB    B LYS A 1 290 ? -8.23321  -4.93068  -10.16794 0.808 38.86666  ? 301 LYS A CB    1 
ATOM   2338 C  CG    A LYS A 1 290 ? -8.96878  -4.26090  -9.06078  0.192 39.22267  ? 301 LYS A CG    1 
ATOM   2339 C  CG    B LYS A 1 290 ? -8.97734  -4.25919  -9.00512  0.808 39.27862  ? 301 LYS A CG    1 
ATOM   2340 C  CD    A LYS A 1 290 ? -10.38188 -4.80614  -9.07611  0.192 39.71076  ? 301 LYS A CD    1 
ATOM   2341 C  CD    B LYS A 1 290 ? -10.44664 -4.65880  -8.93571  0.808 39.99560  ? 301 LYS A CD    1 
ATOM   2342 C  CE    A LYS A 1 290 ? -11.24746 -4.11130  -8.04306  0.192 41.37170  ? 301 LYS A CE    1 
ATOM   2343 C  CE    B LYS A 1 290 ? -11.15664 -3.94551  -7.77470  0.808 42.55024  ? 301 LYS A CE    1 
ATOM   2344 N  NZ    A LYS A 1 290 ? -12.63330 -4.63830  -8.07758  0.192 39.60739  ? 301 LYS A NZ    1 
ATOM   2345 N  NZ    B LYS A 1 290 ? -10.96341 -2.46145  -7.79120  0.808 36.07701  ? 301 LYS A NZ    1 
ATOM   2346 N  N     . ARG A 1 291 ? -6.94881  -8.30069  -11.15578 1.000 32.29702  ? 302 ARG A N     1 
ATOM   2347 C  CA    . ARG A 1 291 ? -6.08451  -8.93468  -12.14183 1.000 31.00572  ? 302 ARG A CA    1 
ATOM   2348 C  C     . ARG A 1 291 ? -6.72901  -8.86384  -13.53350 1.000 27.48370  ? 302 ARG A C     1 
ATOM   2349 O  O     . ARG A 1 291 ? -7.95392  -8.80148  -13.65522 1.000 22.92179  ? 302 ARG A O     1 
ATOM   2350 C  CB    . ARG A 1 291 ? -5.81086  -10.38921 -11.73403 1.000 22.80502  ? 302 ARG A CB    1 
ATOM   2351 C  CG    . ARG A 1 291 ? -5.09249  -10.49475 -10.38548 1.000 23.93069  ? 302 ARG A CG    1 
ATOM   2352 C  CD    . ARG A 1 291 ? -5.14920  -11.88515 -9.73059  1.000 22.95897  ? 302 ARG A CD    1 
ATOM   2353 N  NE    . ARG A 1 291 ? -4.87904  -11.77898 -8.29538  1.000 24.50678  ? 302 ARG A NE    1 
ATOM   2354 C  CZ    . ARG A 1 291 ? -5.17924  -12.69845 -7.38605  1.000 22.28609  ? 302 ARG A CZ    1 
ATOM   2355 N  NH1   . ARG A 1 291 ? -5.65590  -13.88377 -7.73005  1.000 18.51557  ? 302 ARG A NH1   1 
ATOM   2356 N  NH2   . ARG A 1 291 ? -5.02618  -12.40953 -6.09508  1.000 20.04178  ? 302 ARG A NH2   1 
ATOM   2357 N  N     . PRO A 1 292 ? -5.93016  -8.88915  -14.60384 1.000 23.13146  ? 303 PRO A N     1 
ATOM   2358 C  CA    . PRO A 1 292 ? -6.51400  -8.66074  -15.94351 1.000 28.53320  ? 303 PRO A CA    1 
ATOM   2359 C  C     . PRO A 1 292 ? -7.49670  -9.74060  -16.38758 1.000 30.49367  ? 303 PRO A C     1 
ATOM   2360 O  O     . PRO A 1 292 ? -8.45370  -9.43511  -17.10583 1.000 30.82437  ? 303 PRO A O     1 
ATOM   2361 C  CB    . PRO A 1 292 ? -5.28407  -8.59448  -16.86417 1.000 26.74386  ? 303 PRO A CB    1 
ATOM   2362 C  CG    . PRO A 1 292 ? -4.17724  -9.19745  -16.11605 1.000 30.85289  ? 303 PRO A CG    1 
ATOM   2363 C  CD    . PRO A 1 292 ? -4.46898  -9.05198  -14.64661 1.000 27.49689  ? 303 PRO A CD    1 
ATOM   2364 N  N     . LEU A 1 293 ? -7.29004  -10.98499 -15.98407 1.000 27.47290  ? 304 LEU A N     1 
ATOM   2365 C  CA    . LEU A 1 293 ? -8.20091  -12.09243 -16.22258 1.000 26.34007  ? 304 LEU A CA    1 
ATOM   2366 C  C     . LEU A 1 293 ? -8.13804  -12.99221 -14.99867 1.000 24.08169  ? 304 LEU A C     1 
ATOM   2367 O  O     . LEU A 1 293 ? -7.19264  -12.90182 -14.21048 1.000 19.22014  ? 304 LEU A O     1 
ATOM   2368 C  CB    . LEU A 1 293 ? -7.82324  -12.87829 -17.48803 1.000 23.47195  ? 304 LEU A CB    1 
ATOM   2369 C  CG    . LEU A 1 293 ? -8.02717  -12.23297 -18.86067 1.000 21.65515  ? 304 LEU A CG    1 
ATOM   2370 C  CD1   . LEU A 1 293 ? -7.51511  -13.18429 -19.93816 1.000 25.54308  ? 304 LEU A CD1   1 
ATOM   2371 C  CD2   . LEU A 1 293 ? -9.49043  -11.88350 -19.08603 1.000 24.87182  ? 304 LEU A CD2   1 
ATOM   2372 N  N     . PRO A 1 294 ? -9.12829  -13.86098 -14.80595 1.000 24.65722  ? 305 PRO A N     1 
ATOM   2373 C  CA    . PRO A 1 294 ? -9.15862  -14.68187 -13.58127 1.000 23.77227  ? 305 PRO A CA    1 
ATOM   2374 C  C     . PRO A 1 294 ? -7.96066  -15.61994 -13.48277 1.000 23.63637  ? 305 PRO A C     1 
ATOM   2375 O  O     . PRO A 1 294 ? -7.65911  -16.37918 -14.40954 1.000 18.94693  ? 305 PRO A O     1 
ATOM   2376 C  CB    . PRO A 1 294 ? -10.46987 -15.46871 -13.71580 1.000 24.64360  ? 305 PRO A CB    1 
ATOM   2377 C  CG    . PRO A 1 294 ? -11.32809 -14.63424 -14.68519 1.000 24.33090  ? 305 PRO A CG    1 
ATOM   2378 C  CD    . PRO A 1 294 ? -10.33286 -14.05963 -15.64381 1.000 25.34876  ? 305 PRO A CD    1 
ATOM   2379 N  N     . ILE A 1 295 ? -7.29414  -15.58240 -12.33132 1.000 18.49217  ? 306 ILE A N     1 
ATOM   2380 C  CA    . ILE A 1 295 ? -6.13305  -16.42876 -12.09453 1.000 21.36375  ? 306 ILE A CA    1 
ATOM   2381 C  C     . ILE A 1 295 ? -5.91234  -16.51223 -10.59644 1.000 17.30984  ? 306 ILE A C     1 
ATOM   2382 O  O     . ILE A 1 295 ? -6.16505  -15.54777 -9.86729  1.000 19.07984  ? 306 ILE A O     1 
ATOM   2383 C  CB    . ILE A 1 295 ? -4.88932  -15.87304 -12.83647 1.000 22.41335  ? 306 ILE A CB    1 
ATOM   2384 C  CG1   . ILE A 1 295 ? -3.65550  -16.76141 -12.60378 1.000 19.27371  ? 306 ILE A CG1   1 
ATOM   2385 C  CG2   . ILE A 1 295 ? -4.63767  -14.43002 -12.43311 1.000 16.74112  ? 306 ILE A CG2   1 
ATOM   2386 C  CD1   . ILE A 1 295 ? -2.52140  -16.48088 -13.55768 1.000 17.80682  ? 306 ILE A CD1   1 
ATOM   2387 N  N     . THR A 1 296 ? -5.43678  -17.67502 -10.13140 1.000 16.32216  ? 307 THR A N     1 
ATOM   2388 C  CA    . THR A 1 296 ? -5.09547  -17.86920 -8.72705  1.000 15.63951  ? 307 THR A CA    1 
ATOM   2389 C  C     . THR A 1 296 ? -4.03962  -18.97443 -8.61552  1.000 19.67000  ? 307 THR A C     1 
ATOM   2390 O  O     . THR A 1 296 ? -3.56893  -19.52128 -9.61681  1.000 19.26475  ? 307 THR A O     1 
ATOM   2391 C  CB    . THR A 1 296 ? -6.34776  -18.19281 -7.88451  1.000 20.76344  ? 307 THR A CB    1 
ATOM   2392 O  OG1   . THR A 1 296 ? -6.01379  -18.20483 -6.48771  1.000 21.44304  ? 307 THR A OG1   1 
ATOM   2393 C  CG2   . THR A 1 296 ? -6.92552  -19.54063 -8.26481  1.000 15.52504  ? 307 THR A CG2   1 
ATOM   2394 N  N     . MET A 1 297 ? -3.64527  -19.28029 -7.37883  1.000 15.51782  ? 308 MET A N     1 
ATOM   2395 C  CA    . MET A 1 297 ? -2.61076  -20.26912 -7.10278  1.000 20.64722  ? 308 MET A CA    1 
ATOM   2396 C  C     . MET A 1 297 ? -3.04621  -21.14695 -5.94336  1.000 16.85977  ? 308 MET A C     1 
ATOM   2397 O  O     . MET A 1 297 ? -3.72758  -20.68657 -5.02738  1.000 18.61517  ? 308 MET A O     1 
ATOM   2398 C  CB    . MET A 1 297 ? -1.27997  -19.59599 -6.76381  1.000 16.57767  ? 308 MET A CB    1 
ATOM   2399 C  CG    . MET A 1 297 ? -1.04161  -18.32975 -7.57759  1.000 20.06222  ? 308 MET A CG    1 
ATOM   2400 S  SD    . MET A 1 297 ? 0.67656   -17.78551 -7.55931  1.000 24.65515  ? 308 MET A SD    1 
ATOM   2401 C  CE    . MET A 1 297 ? 0.82929   -17.20507 -5.85610  1.000 17.20134  ? 308 MET A CE    1 
ATOM   2402 N  N     . ILE A 1 298 ? -2.62438  -22.41362 -5.97523  1.000 18.73159  ? 309 ILE A N     1 
ATOM   2403 C  CA    . ILE A 1 298 ? -2.96391  -23.38442 -4.93770  1.000 18.22340  ? 309 ILE A CA    1 
ATOM   2404 C  C     . ILE A 1 298 ? -1.72297  -24.20721 -4.59709  1.000 20.47650  ? 309 ILE A C     1 
ATOM   2405 O  O     . ILE A 1 298 ? -0.77574  -24.29740 -5.38030  1.000 18.12319  ? 309 ILE A O     1 
ATOM   2406 C  CB    . ILE A 1 298 ? -4.11616  -24.31996 -5.38207  1.000 15.42819  ? 309 ILE A CB    1 
ATOM   2407 C  CG1   . ILE A 1 298 ? -3.74203  -25.00489 -6.68966  1.000 19.35270  ? 309 ILE A CG1   1 
ATOM   2408 C  CG2   . ILE A 1 298 ? -5.38962  -23.53957 -5.59339  1.000 15.60320  ? 309 ILE A CG2   1 
ATOM   2409 C  CD1   . ILE A 1 298 ? -4.79557  -26.00943 -7.19786  1.000 17.90787  ? 309 ILE A CD1   1 
ATOM   2410 N  N     . GLY A 1 299 ? -1.74758  -24.84497 -3.41699  1.000 19.48203  ? 310 GLY A N     1 
ATOM   2411 C  CA    . GLY A 1 299 ? -0.64741  -25.73326 -3.07446  1.000 15.49032  ? 310 GLY A CA    1 
ATOM   2412 C  C     . GLY A 1 299 ? 0.62426   -24.96221 -2.75627  1.000 19.63965  ? 310 GLY A C     1 
ATOM   2413 O  O     . GLY A 1 299 ? 0.58773   -23.80400 -2.32017  1.000 19.01186  ? 310 GLY A O     1 
ATOM   2414 N  N     . ASP A 1 300 ? 1.77477   -25.61242 -2.99163  1.000 19.17503  ? 311 ASP A N     1 
ATOM   2415 C  CA    . ASP A 1 300 ? 3.05843   -24.97353 -2.68939  1.000 20.20926  ? 311 ASP A CA    1 
ATOM   2416 C  C     . ASP A 1 300 ? 3.26542   -23.69911 -3.49291  1.000 20.09401  ? 311 ASP A C     1 
ATOM   2417 O  O     . ASP A 1 300 ? 3.96489   -22.79401 -3.03442  1.000 20.12356  ? 311 ASP A O     1 
ATOM   2418 C  CB    . ASP A 1 300 ? 4.21598   -25.92824 -2.95230  1.000 16.39377  ? 311 ASP A CB    1 
ATOM   2419 C  CG    . ASP A 1 300 ? 4.42805   -26.92630 -1.81916  1.000 23.21454  ? 311 ASP A CG    1 
ATOM   2420 O  OD1   . ASP A 1 300 ? 3.60045   -27.01769 -0.86943  1.000 21.74244  ? 311 ASP A OD1   1 
ATOM   2421 O  OD2   . ASP A 1 300 ? 5.44204   -27.63094 -1.89573  1.000 21.31678  ? 311 ASP A OD2   1 
ATOM   2422 N  N     . ALA A 1 301 ? 2.68515   -23.60968 -4.69495  1.000 18.19260  ? 312 ALA A N     1 
ATOM   2423 C  CA    . ALA A 1 301 ? 2.78194   -22.35766 -5.44474  1.000 19.90956  ? 312 ALA A CA    1 
ATOM   2424 C  C     . ALA A 1 301 ? 2.21683   -21.18990 -4.64689  1.000 19.75780  ? 312 ALA A C     1 
ATOM   2425 O  O     . ALA A 1 301 ? 2.69189   -20.05832 -4.78428  1.000 21.06149  ? 312 ALA A O     1 
ATOM   2426 C  CB    . ALA A 1 301 ? 2.05293   -22.47528 -6.78124  1.000 17.97842  ? 312 ALA A CB    1 
ATOM   2427 N  N     . ALA A 1 302 ? 1.22371   -21.45314 -3.79591  1.000 16.00663  ? 313 ALA A N     1 
ATOM   2428 C  CA    . ALA A 1 302 ? 0.54685   -20.44766 -2.97939  1.000 18.33683  ? 313 ALA A CA    1 
ATOM   2429 C  C     . ALA A 1 302 ? 1.20696   -20.24069 -1.61209  1.000 20.87922  ? 313 ALA A C     1 
ATOM   2430 O  O     . ALA A 1 302 ? 1.25252   -19.10736 -1.12142  1.000 21.38411  ? 313 ALA A O     1 
ATOM   2431 C  CB    . ALA A 1 302 ? -0.92291  -20.84065 -2.78318  1.000 16.30698  ? 313 ALA A CB    1 
ATOM   2432 N  N     . HIS A 1 303 ? 1.71545   -21.30122 -0.97178  1.000 17.31613  ? 314 HIS A N     1 
ATOM   2433 C  CA    . HIS A 1 303 ? 2.17156   -21.16649 0.40835   1.000 20.47293  ? 314 HIS A CA    1 
ATOM   2434 C  C     . HIS A 1 303 ? 3.19279   -22.23459 0.79936   1.000 24.58077  ? 314 HIS A C     1 
ATOM   2435 O  O     . HIS A 1 303 ? 3.10102   -22.82067 1.88648   1.000 25.05258  ? 314 HIS A O     1 
ATOM   2436 C  CB    . HIS A 1 303 ? 0.96441   -21.23492 1.33457   1.000 18.14039  ? 314 HIS A CB    1 
ATOM   2437 C  CG    . HIS A 1 303 ? 0.05529   -22.37170 1.00188   1.000 21.93299  ? 314 HIS A CG    1 
ATOM   2438 N  ND1   . HIS A 1 303 ? 0.44325   -23.69057 1.12710   1.000 18.83478  ? 314 HIS A ND1   1 
ATOM   2439 C  CD2   . HIS A 1 303 ? -1.20316  -22.39435 0.50793   1.000 18.91173  ? 314 HIS A CD2   1 
ATOM   2440 C  CE1   . HIS A 1 303 ? -0.54162  -24.47580 0.72902   1.000 20.68069  ? 314 HIS A CE1   1 
ATOM   2441 N  NE2   . HIS A 1 303 ? -1.55379  -23.71484 0.35258   1.000 18.97257  ? 314 HIS A NE2   1 
ATOM   2442 N  N     . LEU A 1 304 ? 4.14558   -22.51416 -0.08553  1.000 17.92702  ? 315 LEU A N     1 
ATOM   2443 C  CA    . LEU A 1 304 ? 5.31322   -23.31217 0.26927   1.000 21.73497  ? 315 LEU A CA    1 
ATOM   2444 C  C     . LEU A 1 304 ? 5.83028   -22.93981 1.65200   1.000 23.24670  ? 315 LEU A C     1 
ATOM   2445 O  O     . LEU A 1 304 ? 5.97784   -21.75506 1.97109   1.000 23.95609  ? 315 LEU A O     1 
ATOM   2446 C  CB    . LEU A 1 304 ? 6.41838   -23.08145 -0.76219  1.000 18.18379  ? 315 LEU A CB    1 
ATOM   2447 C  CG    . LEU A 1 304 ? 7.76874   -23.71601 -0.43293  1.000 24.31346  ? 315 LEU A CG    1 
ATOM   2448 C  CD1   . LEU A 1 304 ? 7.69885   -25.22074 -0.73565  1.000 20.99162  ? 315 LEU A CD1   1 
ATOM   2449 C  CD2   . LEU A 1 304 ? 8.89003   -23.04234 -1.21082  1.000 18.02845  ? 315 LEU A CD2   1 
ATOM   2450 N  N     . MET A 1 305 ? 6.12634   -23.94851 2.46681   1.000 21.23208  ? 316 MET A N     1 
ATOM   2451 C  CA    . MET A 1 305 ? 6.59873   -23.70186 3.82378   1.000 20.95236  ? 316 MET A CA    1 
ATOM   2452 C  C     . MET A 1 305 ? 7.47478   -24.87105 4.25247   1.000 22.54970  ? 316 MET A C     1 
ATOM   2453 O  O     . MET A 1 305 ? 7.43490   -25.93683 3.62430   1.000 21.42232  ? 316 MET A O     1 
ATOM   2454 C  CB    . MET A 1 305 ? 5.41638   -23.51213 4.78795   1.000 20.85474  ? 316 MET A CB    1 
ATOM   2455 C  CG    . MET A 1 305 ? 4.50929   -24.73532 4.97525   1.000 22.36899  ? 316 MET A CG    1 
ATOM   2456 S  SD    . MET A 1 305 ? 3.02141   -24.33354 5.95922   1.000 28.71297  ? 316 MET A SD    1 
ATOM   2457 C  CE    . MET A 1 305 ? 1.85975   -23.82066 4.66647   1.000 24.73410  ? 316 MET A CE    1 
ATOM   2458 N  N     . PRO A 1 306 ? 8.27898   -24.70959 5.30856   1.000 27.09878  ? 317 PRO A N     1 
ATOM   2459 C  CA    . PRO A 1 306 ? 9.15231   -25.81137 5.73661   1.000 21.65926  ? 317 PRO A CA    1 
ATOM   2460 C  C     . PRO A 1 306 ? 8.33621   -27.03619 6.10643   1.000 26.99241  ? 317 PRO A C     1 
ATOM   2461 O  O     . PRO A 1 306 ? 7.20030   -26.91464 6.59755   1.000 23.95166  ? 317 PRO A O     1 
ATOM   2462 C  CB    . PRO A 1 306 ? 9.88096   -25.23359 6.95716   1.000 24.05733  ? 317 PRO A CB    1 
ATOM   2463 C  CG    . PRO A 1 306 ? 9.81283   -23.74155 6.77955   1.000 28.36419  ? 317 PRO A CG    1 
ATOM   2464 C  CD    . PRO A 1 306 ? 8.48663   -23.48897 6.12464   1.000 25.79270  ? 317 PRO A CD    1 
ATOM   2465 N  N     . PRO A 1 307 ? 8.87600   -28.23880 5.89064   1.000 28.44153  ? 318 PRO A N     1 
ATOM   2466 C  CA    . PRO A 1 307 ? 8.08959   -29.47245 6.08230   1.000 31.96822  ? 318 PRO A CA    1 
ATOM   2467 C  C     . PRO A 1 307 ? 8.25329   -30.21122 7.41037   1.000 34.27370  ? 318 PRO A C     1 
ATOM   2468 O  O     . PRO A 1 307 ? 7.62699   -31.26845 7.56495   1.000 33.18657  ? 318 PRO A O     1 
ATOM   2469 C  CB    . PRO A 1 307 ? 8.61597   -30.35105 4.93903   1.000 27.55673  ? 318 PRO A CB    1 
ATOM   2470 C  CG    . PRO A 1 307 ? 10.05412  -30.01970 4.88121   1.000 27.19516  ? 318 PRO A CG    1 
ATOM   2471 C  CD    . PRO A 1 307 ? 10.13778  -28.52089 5.17947   1.000 26.06477  ? 318 PRO A CD    1 
ATOM   2472 N  N     . PHE A 1 308 ? 9.02928   -29.69517 8.36980   1.000 30.66079  ? 319 PHE A N     1 
ATOM   2473 C  CA    . PHE A 1 308 ? 9.49319   -30.52316 9.49164   1.000 36.12915  ? 319 PHE A CA    1 
ATOM   2474 C  C     . PHE A 1 308 ? 8.40365   -30.88632 10.50060  1.000 41.34733  ? 319 PHE A C     1 
ATOM   2475 O  O     . PHE A 1 308 ? 8.56187   -31.88302 11.21279  1.000 40.01358  ? 319 PHE A O     1 
ATOM   2476 C  CB    . PHE A 1 308 ? 10.63672  -29.82998 10.23739  1.000 29.31093  ? 319 PHE A CB    1 
ATOM   2477 C  CG    . PHE A 1 308 ? 11.74243  -29.39140 9.34910   1.000 26.10010  ? 319 PHE A CG    1 
ATOM   2478 C  CD1   . PHE A 1 308 ? 12.58174  -30.31868 8.75994   1.000 31.00709  ? 319 PHE A CD1   1 
ATOM   2479 C  CD2   . PHE A 1 308 ? 11.92667  -28.04923 9.07297   1.000 27.18581  ? 319 PHE A CD2   1 
ATOM   2480 C  CE1   . PHE A 1 308 ? 13.59925  -29.91273 7.90653   1.000 31.67296  ? 319 PHE A CE1   1 
ATOM   2481 C  CE2   . PHE A 1 308 ? 12.94568  -27.63359 8.23293   1.000 28.14234  ? 319 PHE A CE2   1 
ATOM   2482 C  CZ    . PHE A 1 308 ? 13.78085  -28.57008 7.64461   1.000 32.01117  ? 319 PHE A CZ    1 
ATOM   2483 N  N     . ALA A 1 309 ? 7.32012   -30.11453 10.59759  1.000 32.48104  ? 320 ALA A N     1 
ATOM   2484 C  CA    . ALA A 1 309 ? 6.23832   -30.42710 11.52674  1.000 41.36077  ? 320 ALA A CA    1 
ATOM   2485 C  C     . ALA A 1 309 ? 5.00476   -30.99604 10.82781  1.000 44.07075  ? 320 ALA A C     1 
ATOM   2486 O  O     . ALA A 1 309 ? 3.92252   -31.02970 11.42223  1.000 40.40203  ? 320 ALA A O     1 
ATOM   2487 C  CB    . ALA A 1 309 ? 5.85290   -29.19393 12.34509  1.000 41.72808  ? 320 ALA A CB    1 
ATOM   2488 N  N     . GLY A 1 310 ? 5.14409   -31.44643 9.58338   1.000 39.68069  ? 321 GLY A N     1 
ATOM   2489 C  CA    . GLY A 1 310 ? 4.05359   -32.09644 8.88179   1.000 41.47509  ? 321 GLY A CA    1 
ATOM   2490 C  C     . GLY A 1 310 ? 3.11906   -31.18228 8.12057   1.000 42.62769  ? 321 GLY A C     1 
ATOM   2491 O  O     . GLY A 1 310 ? 2.08302   -31.65226 7.62449   1.000 35.40246  ? 321 GLY A O     1 
ATOM   2492 N  N     . GLN A 1 311 ? 3.42544   -29.89221 8.03221   1.000 37.91028  ? 322 GLN A N     1 
ATOM   2493 C  CA    . GLN A 1 311 ? 2.67684   -29.03054 7.13277   1.000 33.87937  ? 322 GLN A CA    1 
ATOM   2494 C  C     . GLN A 1 311 ? 3.14440   -29.26899 5.70479   1.000 31.73859  ? 322 GLN A C     1 
ATOM   2495 O  O     . GLN A 1 311 ? 4.31666   -29.57650 5.45548   1.000 27.51260  ? 322 GLN A O     1 
ATOM   2496 C  CB    . GLN A 1 311 ? 2.84315   -27.55601 7.50759   1.000 33.04164  ? 322 GLN A CB    1 
ATOM   2497 C  CG    . GLN A 1 311 ? 2.14981   -27.14088 8.81722   1.000 36.73444  ? 322 GLN A CG    1 
ATOM   2498 C  CD    . GLN A 1 311 ? 2.85529   -27.65553 10.06897  1.000 44.93953  ? 322 GLN A CD    1 
ATOM   2499 O  OE1   . GLN A 1 311 ? 4.07904   -27.61381 10.17226  1.000 41.08961  ? 322 GLN A OE1   1 
ATOM   2500 N  NE2   . GLN A 1 311 ? 2.07464   -28.14137 11.02929  1.000 54.71568  ? 322 GLN A NE2   1 
ATOM   2501 N  N     . GLY A 1 312 ? 2.21709   -29.13870 4.76221   1.000 26.83406  ? 323 GLY A N     1 
ATOM   2502 C  CA    . GLY A 1 312 ? 2.58831   -29.31199 3.37127   1.000 27.71785  ? 323 GLY A CA    1 
ATOM   2503 C  C     . GLY A 1 312 ? 1.43923   -29.56371 2.41981   1.000 25.81461  ? 323 GLY A C     1 
ATOM   2504 O  O     . GLY A 1 312 ? 0.80268   -28.61571 1.94266   1.000 22.25690  ? 323 GLY A O     1 
ATOM   2505 N  N     . VAL A 1 313 ? 1.17716   -30.83874 2.12051   1.000 20.92590  ? 324 VAL A N     1 
ATOM   2506 C  CA    . VAL A 1 313 ? 0.23600   -31.14763 1.05596   1.000 22.37093  ? 324 VAL A CA    1 
ATOM   2507 C  C     . VAL A 1 313 ? -1.20356  -30.92473 1.50706   1.000 22.05224  ? 324 VAL A C     1 
ATOM   2508 O  O     . VAL A 1 313 ? -2.06708  -30.59381 0.68873   1.000 20.41591  ? 324 VAL A O     1 
ATOM   2509 C  CB    . VAL A 1 313 ? 0.44524   -32.58354 0.54423   1.000 26.21980  ? 324 VAL A CB    1 
ATOM   2510 C  CG1   . VAL A 1 313 ? -0.24087  -33.60937 1.46142   1.000 23.47581  ? 324 VAL A CG1   1 
ATOM   2511 C  CG2   . VAL A 1 313 ? -0.07387  -32.70416 -0.87701  1.000 18.34284  ? 324 VAL A CG2   1 
ATOM   2512 N  N     . ASN A 1 314 ? -1.48289  -31.06090 2.80196   1.000 23.83620  ? 325 ASN A N     1 
ATOM   2513 C  CA    . ASN A 1 314 ? -2.87035  -31.05269 3.24375   1.000 25.55238  ? 325 ASN A CA    1 
ATOM   2514 C  C     . ASN A 1 314 ? -3.49272  -29.67552 3.10371   1.000 21.28356  ? 325 ASN A C     1 
ATOM   2515 O  O     . ASN A 1 314 ? -4.67395  -29.56272 2.76700   1.000 21.63609  ? 325 ASN A O     1 
ATOM   2516 C  CB    . ASN A 1 314 ? -2.96183  -31.56764 4.67321   1.000 23.74105  ? 325 ASN A CB    1 
ATOM   2517 C  CG    . ASN A 1 314 ? -2.95315  -33.06040 4.71691   1.000 27.58848  ? 325 ASN A CG    1 
ATOM   2518 O  OD1   . ASN A 1 314 ? -3.97146  -33.68949 4.43763   1.000 25.70032  ? 325 ASN A OD1   1 
ATOM   2519 N  ND2   . ASN A 1 314 ? -1.79569  -33.65131 5.02632   1.000 24.46185  ? 325 ASN A ND2   1 
ATOM   2520 N  N     A SER A 1 315 ? -2.71903  -28.61494 3.33542   0.649 23.24034  ? 326 SER A N     1 
ATOM   2521 N  N     B SER A 1 315 ? -2.71677  -28.62010 3.37029   0.351 23.34115  ? 326 SER A N     1 
ATOM   2522 C  CA    A SER A 1 315 ? -3.24742  -27.28025 3.08279   0.649 22.90391  ? 326 SER A CA    1 
ATOM   2523 C  CA    B SER A 1 315 ? -3.17917  -27.26754 3.07820   0.351 22.94808  ? 326 SER A CA    1 
ATOM   2524 C  C     A SER A 1 315 ? -3.43072  -27.02728 1.58749   0.649 23.64329  ? 326 SER A C     1 
ATOM   2525 C  C     B SER A 1 315 ? -3.47484  -27.10499 1.59386   0.351 23.53790  ? 326 SER A C     1 
ATOM   2526 O  O     A SER A 1 315 ? -4.32150  -26.26383 1.19708   0.649 20.65052  ? 326 SER A O     1 
ATOM   2527 O  O     B SER A 1 315 ? -4.47666  -26.48649 1.21534   0.351 20.88340  ? 326 SER A O     1 
ATOM   2528 C  CB    A SER A 1 315 ? -2.34161  -26.22068 3.70725   0.649 22.58739  ? 326 SER A CB    1 
ATOM   2529 C  CB    B SER A 1 315 ? -2.13767  -26.23899 3.52074   0.351 22.88171  ? 326 SER A CB    1 
ATOM   2530 O  OG    A SER A 1 315 ? -1.05757  -26.22637 3.11991   0.649 24.19018  ? 326 SER A OG    1 
ATOM   2531 O  OG    B SER A 1 315 ? -2.02385  -26.17828 4.92778   0.351 25.47985  ? 326 SER A OG    1 
ATOM   2532 N  N     . GLY A 1 316 ? -2.61049  -27.65381 0.73783   1.000 19.40671  ? 327 GLY A N     1 
ATOM   2533 C  CA    . GLY A 1 316 ? -2.83553  -27.54200 -0.69170  1.000 16.76957  ? 327 GLY A CA    1 
ATOM   2534 C  C     . GLY A 1 316 ? -4.08726  -28.27589 -1.13992  1.000 19.28793  ? 327 GLY A C     1 
ATOM   2535 O  O     . GLY A 1 316 ? -4.85479  -27.76757 -1.96378  1.000 19.98509  ? 327 GLY A O     1 
ATOM   2536 N  N     . LEU A 1 317 ? -4.32493  -29.47167 -0.59061  1.000 17.93534  ? 328 LEU A N     1 
ATOM   2537 C  CA    . LEU A 1 317 ? -5.55988  -30.18421 -0.90776  1.000 23.64016  ? 328 LEU A CA    1 
ATOM   2538 C  C     . LEU A 1 317 ? -6.78082  -29.44306 -0.38154  1.000 22.89457  ? 328 LEU A C     1 
ATOM   2539 O  O     . LEU A 1 317 ? -7.85573  -29.51924 -0.98228  1.000 21.03989  ? 328 LEU A O     1 
ATOM   2540 C  CB    . LEU A 1 317 ? -5.50921  -31.60262 -0.35016  1.000 21.32962  ? 328 LEU A CB    1 
ATOM   2541 C  CG    . LEU A 1 317 ? -4.36552  -32.42966 -0.95704  1.000 28.48378  ? 328 LEU A CG    1 
ATOM   2542 C  CD1   . LEU A 1 317 ? -4.28448  -33.80117 -0.30587  1.000 20.29247  ? 328 LEU A CD1   1 
ATOM   2543 C  CD2   . LEU A 1 317 ? -4.49577  -32.55679 -2.48281  1.000 17.97900  ? 328 LEU A CD2   1 
ATOM   2544 N  N     . MET A 1 318 ? -6.63178  -28.71780 0.72597   1.000 23.06395  ? 329 MET A N     1 
ATOM   2545 C  CA    . MET A 1 318 ? -7.70784  -27.84964 1.19378   1.000 21.84438  ? 329 MET A CA    1 
ATOM   2546 C  C     . MET A 1 318 ? -7.98515  -26.72536 0.19763   1.000 21.03593  ? 329 MET A C     1 
ATOM   2547 O  O     . MET A 1 318 ? -9.14076  -26.35116 -0.02654  1.000 19.59069  ? 329 MET A O     1 
ATOM   2548 C  CB    . MET A 1 318 ? -7.33855  -27.26269 2.54825   1.000 21.23732  ? 329 MET A CB    1 
ATOM   2549 C  CG    . MET A 1 318 ? -8.40611  -26.35395 3.07103   1.000 35.05362  ? 329 MET A CG    1 
ATOM   2550 S  SD    . MET A 1 318 ? -9.75884  -27.33864 3.74933   1.000 49.43215  ? 329 MET A SD    1 
ATOM   2551 C  CE    . MET A 1 318 ? -9.28684  -27.23749 5.47324   1.000 56.68964  ? 329 MET A CE    1 
ATOM   2552 N  N     . ASP A 1 319 ? -6.92921  -26.15613 -0.38965  1.000 22.00007  ? 330 ASP A N     1 
ATOM   2553 C  CA    . ASP A 1 319 ? -7.10544  -25.15617 -1.43846  1.000 17.67664  ? 330 ASP A CA    1 
ATOM   2554 C  C     . ASP A 1 319 ? -7.98801  -25.69359 -2.55409  1.000 21.07906  ? 330 ASP A C     1 
ATOM   2555 O  O     . ASP A 1 319 ? -8.93258  -25.02891 -2.99601  1.000 24.19619  ? 330 ASP A O     1 
ATOM   2556 C  CB    . ASP A 1 319 ? -5.74354  -24.75266 -2.01961  1.000 16.88947  ? 330 ASP A CB    1 
ATOM   2557 C  CG    . ASP A 1 319 ? -4.78756  -24.16609 -0.97789  1.000 21.33929  ? 330 ASP A CG    1 
ATOM   2558 O  OD1   . ASP A 1 319 ? -5.21806  -23.74238 0.12789   1.000 18.59006  ? 330 ASP A OD1   1 
ATOM   2559 O  OD2   . ASP A 1 319 ? -3.57785  -24.11890 -1.28532  1.000 20.27064  ? 330 ASP A OD2   1 
ATOM   2560 N  N     . ALA A 1 320 ? -7.66463  -26.89395 -3.04500  1.000 18.85835  ? 331 ALA A N     1 
ATOM   2561 C  CA    . ALA A 1 320 ? -8.38085  -27.45858 -4.18319  1.000 21.98181  ? 331 ALA A CA    1 
ATOM   2562 C  C     . ALA A 1 320 ? -9.83587  -27.70643 -3.83240  1.000 21.01720  ? 331 ALA A C     1 
ATOM   2563 O  O     . ALA A 1 320 ? -10.73338 -27.48439 -4.65246  1.000 18.94232  ? 331 ALA A O     1 
ATOM   2564 C  CB    . ALA A 1 320 ? -7.71574  -28.76958 -4.62262  1.000 19.61024  ? 331 ALA A CB    1 
ATOM   2565 N  N     . LEU A 1 321 ? -10.08426 -28.16131 -2.60792  1.000 19.77317  ? 332 LEU A N     1 
ATOM   2566 C  CA    . LEU A 1 321 ? -11.44676 -28.42441 -2.17868  1.000 21.25177  ? 332 LEU A CA    1 
ATOM   2567 C  C     . LEU A 1 321 ? -12.25438 -27.13269 -2.12217  1.000 22.61601  ? 332 LEU A C     1 
ATOM   2568 O  O     . LEU A 1 321 ? -13.36822 -27.05552 -2.65605  1.000 22.18086  ? 332 LEU A O     1 
ATOM   2569 C  CB    . LEU A 1 321 ? -11.40591 -29.11984 -0.82182  1.000 25.20937  ? 332 LEU A CB    1 
ATOM   2570 C  CG    . LEU A 1 321 ? -12.71460 -29.46804 -0.12517  1.000 31.88512  ? 332 LEU A CG    1 
ATOM   2571 C  CD1   . LEU A 1 321 ? -13.55699 -30.38326 -0.97661  1.000 27.70905  ? 332 LEU A CD1   1 
ATOM   2572 C  CD2   . LEU A 1 321 ? -12.37093 -30.12837 1.19545   1.000 31.64435  ? 332 LEU A CD2   1 
ATOM   2573 N  N     . ILE A 1 322 ? -11.69249 -26.09577 -1.49735  1.000 22.93566  ? 333 ILE A N     1 
ATOM   2574 C  CA    . ILE A 1 322 ? -12.41745 -24.83743 -1.33998  1.000 22.76742  ? 333 ILE A CA    1 
ATOM   2575 C  C     . ILE A 1 322 ? -12.62174 -24.16866 -2.68985  1.000 20.53187  ? 333 ILE A C     1 
ATOM   2576 O  O     . ILE A 1 322 ? -13.73412 -23.74109 -3.03167  1.000 20.74195  ? 333 ILE A O     1 
ATOM   2577 C  CB    . ILE A 1 322 ? -11.67285 -23.91309 -0.36311  1.000 21.30222  ? 333 ILE A CB    1 
ATOM   2578 C  CG1   . ILE A 1 322 ? -11.72807 -24.49840 1.06525   1.000 23.74622  ? 333 ILE A CG1   1 
ATOM   2579 C  CG2   . ILE A 1 322 ? -12.24303 -22.51305 -0.44412  1.000 20.53035  ? 333 ILE A CG2   1 
ATOM   2580 C  CD1   . ILE A 1 322 ? -10.94243 -23.69954 2.12541   1.000 21.77313  ? 333 ILE A CD1   1 
ATOM   2581 N  N     . LEU A 1 323 ? -11.55398 -24.08543 -3.48522  1.000 19.21524  ? 334 LEU A N     1 
ATOM   2582 C  CA    . LEU A 1 323 ? -11.63096 -23.37717 -4.75953  1.000 20.14318  ? 334 LEU A CA    1 
ATOM   2583 C  C     . LEU A 1 323 ? -12.58473 -24.07760 -5.71645  1.000 20.61613  ? 334 LEU A C     1 
ATOM   2584 O  O     . LEU A 1 323 ? -13.40860 -23.43071 -6.37502  1.000 20.48008  ? 334 LEU A O     1 
ATOM   2585 C  CB    . LEU A 1 323 ? -10.23067 -23.25406 -5.37798  1.000 17.35886  ? 334 LEU A CB    1 
ATOM   2586 C  CG    . LEU A 1 323 ? -10.14233 -22.54684 -6.73703  1.000 18.92348  ? 334 LEU A CG    1 
ATOM   2587 C  CD1   . LEU A 1 323 ? -10.72023 -21.13564 -6.66802  1.000 16.74172  ? 334 LEU A CD1   1 
ATOM   2588 C  CD2   . LEU A 1 323 ? -8.67495  -22.53030 -7.21594  1.000 17.66568  ? 334 LEU A CD2   1 
ATOM   2589 N  N     . SER A 1 324 ? -12.49860 -25.41000 -5.80053  1.000 20.66568  ? 335 SER A N     1 
ATOM   2590 C  CA    . SER A 1 324 ? -13.39707 -26.13064 -6.69916  1.000 21.79767  ? 335 SER A CA    1 
ATOM   2591 C  C     . SER A 1 324 ? -14.84647 -25.95653 -6.27236  1.000 23.54205  ? 335 SER A C     1 
ATOM   2592 O  O     . SER A 1 324 ? -15.72612 -25.76508 -7.11703  1.000 24.75141  ? 335 SER A O     1 
ATOM   2593 C  CB    . SER A 1 324 ? -13.03018 -27.61336 -6.76871  1.000 19.59433  ? 335 SER A CB    1 
ATOM   2594 O  OG    . SER A 1 324 ? -13.26379 -28.28074 -5.53300  1.000 23.08192  ? 335 SER A OG    1 
ATOM   2595 N  N     . ASP A 1 325 ? -15.11724 -26.00722 -4.96525  1.000 24.48997  ? 336 ASP A N     1 
ATOM   2596 C  CA    . ASP A 1 325 ? -16.48644 -25.79417 -4.51045  1.000 24.73611  ? 336 ASP A CA    1 
ATOM   2597 C  C     . ASP A 1 325 ? -16.98058 -24.39210 -4.85612  1.000 23.13438  ? 336 ASP A C     1 
ATOM   2598 O  O     . ASP A 1 325 ? -18.12123 -24.22727 -5.30363  1.000 27.24907  ? 336 ASP A O     1 
ATOM   2599 C  CB    . ASP A 1 325 ? -16.61956 -26.03293 -3.00752  1.000 23.19276  ? 336 ASP A CB    1 
ATOM   2600 C  CG    . ASP A 1 325 ? -18.06168 -25.84759 -2.54373  1.000 37.00736  ? 336 ASP A CG    1 
ATOM   2601 O  OD1   . ASP A 1 325 ? -18.92231 -26.62146 -3.01156  1.000 43.87364  ? 336 ASP A OD1   1 
ATOM   2602 O  OD2   . ASP A 1 325 ? -18.35655 -24.90486 -1.77684  1.000 36.66285  ? 336 ASP A OD2   1 
ATOM   2603 N  N     . ASN A 1 326 ? -16.14042 -23.36743 -4.65678  1.000 21.95974  ? 337 ASN A N     1 
ATOM   2604 C  CA    . ASN A 1 326 ? -16.55364 -22.00643 -4.98990  1.000 23.59462  ? 337 ASN A CA    1 
ATOM   2605 C  C     . ASN A 1 326 ? -16.83602 -21.85487 -6.47970  1.000 23.25568  ? 337 ASN A C     1 
ATOM   2606 O  O     . ASN A 1 326 ? -17.73919 -21.10680 -6.86686  1.000 21.42121  ? 337 ASN A O     1 
ATOM   2607 C  CB    . ASN A 1 326 ? -15.48117 -20.99844 -4.56750  1.000 24.81303  ? 337 ASN A CB    1 
ATOM   2608 C  CG    . ASN A 1 326 ? -15.45770 -20.75145 -3.06643  1.000 26.90525  ? 337 ASN A CG    1 
ATOM   2609 O  OD1   . ASN A 1 326 ? -16.28280 -21.28487 -2.31873  1.000 26.08078  ? 337 ASN A OD1   1 
ATOM   2610 N  ND2   . ASN A 1 326 ? -14.50840 -19.93221 -2.62005  1.000 22.17505  ? 337 ASN A ND2   1 
ATOM   2611 N  N     . LEU A 1 327 ? -16.06230 -22.53741 -7.32684  1.000 21.44775  ? 338 LEU A N     1 
ATOM   2612 C  CA    . LEU A 1 327 ? -16.23641 -22.42538 -8.77247  1.000 25.08820  ? 338 LEU A CA    1 
ATOM   2613 C  C     . LEU A 1 327 ? -17.48953 -23.14207 -9.26125  1.000 26.36276  ? 338 LEU A C     1 
ATOM   2614 O  O     . LEU A 1 327 ? -17.94040 -22.87890 -10.38269 1.000 21.73378  ? 338 LEU A O     1 
ATOM   2615 C  CB    . LEU A 1 327 ? -14.99376 -22.97086 -9.51195  1.000 18.50845  ? 338 LEU A CB    1 
ATOM   2616 C  CG    . LEU A 1 327 ? -13.75887 -22.06633 -9.39335  1.000 20.84395  ? 338 LEU A CG    1 
ATOM   2617 C  CD1   . LEU A 1 327 ? -12.46740 -22.70866 -9.91536  1.000 20.97091  ? 338 LEU A CD1   1 
ATOM   2618 C  CD2   . LEU A 1 327 ? -13.97788 -20.69751 -10.05313 1.000 18.56898  ? 338 LEU A CD2   1 
ATOM   2619 N  N     . THR A 1 328 ? -18.06198 -24.03587 -8.45412  1.000 24.64230  ? 339 THR A N     1 
ATOM   2620 C  CA    . THR A 1 328 ? -19.13645 -24.90290 -8.91673  1.000 23.65782  ? 339 THR A CA    1 
ATOM   2621 C  C     . THR A 1 328 ? -20.40599 -24.87363 -8.07394  1.000 29.57043  ? 339 THR A C     1 
ATOM   2622 O  O     . THR A 1 328 ? -21.40391 -25.46990 -8.49919  1.000 24.70606  ? 339 THR A O     1 
ATOM   2623 C  CB    . THR A 1 328 ? -18.64781 -26.36121 -8.99372  1.000 29.65240  ? 339 THR A CB    1 
ATOM   2624 O  OG1   . THR A 1 328 ? -18.26451 -26.82110 -7.69080  1.000 29.80910  ? 339 THR A OG1   1 
ATOM   2625 C  CG2   . THR A 1 328 ? -17.45239 -26.45725 -9.89491  1.000 23.53039  ? 339 THR A CG2   1 
ATOM   2626 N  N     . ASN A 1 329 ? -20.41947 -24.21664 -6.90981  1.000 23.83428  ? 340 ASN A N     1 
ATOM   2627 C  CA    . ASN A 1 329 ? -21.64549 -24.25754 -6.11415  1.000 31.91363  ? 340 ASN A CA    1 
ATOM   2628 C  C     . ASN A 1 329 ? -22.69760 -23.26366 -6.59636  1.000 25.42816  ? 340 ASN A C     1 
ATOM   2629 O  O     . ASN A 1 329 ? -23.83848 -23.33279 -6.13344  1.000 31.24841  ? 340 ASN A O     1 
ATOM   2630 C  CB    . ASN A 1 329 ? -21.35325 -24.03845 -4.61171  1.000 29.06263  ? 340 ASN A CB    1 
ATOM   2631 C  CG    . ASN A 1 329 ? -20.67656 -22.68272 -4.30487  1.000 31.36076  ? 340 ASN A CG    1 
ATOM   2632 O  OD1   . ASN A 1 329 ? -20.68995 -21.75426 -5.12226  1.000 24.40026  ? 340 ASN A OD1   1 
ATOM   2633 N  ND2   . ASN A 1 329 ? -20.09031 -22.57529 -3.10591  1.000 27.33214  ? 340 ASN A ND2   1 
ATOM   2634 N  N     . GLY A 1 330 ? -22.35506 -22.36817 -7.52188  1.000 30.80212  ? 341 GLY A N     1 
ATOM   2635 C  CA    . GLY A 1 330 ? -23.31478 -21.41390 -8.05553  1.000 29.72416  ? 341 GLY A CA    1 
ATOM   2636 C  C     . GLY A 1 330 ? -23.70460 -20.27933 -7.12954  1.000 30.94200  ? 341 GLY A C     1 
ATOM   2637 O  O     . GLY A 1 330 ? -24.71090 -19.61129 -7.38592  1.000 29.44029  ? 341 GLY A O     1 
ATOM   2638 N  N     . LYS A 1 331 ? -22.94830 -20.04076 -6.05406  1.000 26.59028  ? 342 LYS A N     1 
ATOM   2639 C  CA    . LYS A 1 331 ? -23.25796 -18.94468 -5.13957  1.000 30.81832  ? 342 LYS A CA    1 
ATOM   2640 C  C     . LYS A 1 331 ? -22.56788 -17.64157 -5.51368  1.000 28.24919  ? 342 LYS A C     1 
ATOM   2641 O  O     . LYS A 1 331 ? -22.94777 -16.58676 -5.00364  1.000 34.27374  ? 342 LYS A O     1 
ATOM   2642 C  CB    . LYS A 1 331 ? -22.86359 -19.30910 -3.69827  1.000 25.98282  ? 342 LYS A CB    1 
ATOM   2643 C  CG    . LYS A 1 331 ? -23.60223 -20.51433 -3.11602  1.000 30.65065  ? 342 LYS A CG    1 
ATOM   2644 C  CD    . LYS A 1 331 ? -25.10352 -20.26022 -3.02981  1.000 35.04702  ? 342 LYS A CD    1 
ATOM   2645 C  CE    . LYS A 1 331 ? -25.81005 -21.42846 -2.35842  1.000 42.68423  ? 342 LYS A CE    1 
ATOM   2646 N  NZ    . LYS A 1 331 ? -27.23664 -21.51973 -2.75746  1.000 45.38209  ? 342 LYS A NZ    1 
ATOM   2647 N  N     . PHE A 1 332 ? -21.56784 -17.68056 -6.37687  1.000 22.97905  ? 343 PHE A N     1 
ATOM   2648 C  CA    . PHE A 1 332 ? -20.78029 -16.50144 -6.68555  1.000 28.90333  ? 343 PHE A CA    1 
ATOM   2649 C  C     . PHE A 1 332 ? -21.18118 -15.93162 -8.03827  1.000 30.93777  ? 343 PHE A C     1 
ATOM   2650 O  O     . PHE A 1 332 ? -21.54948 -16.67014 -8.95240  1.000 33.31897  ? 343 PHE A O     1 
ATOM   2651 C  CB    . PHE A 1 332 ? -19.28832 -16.84685 -6.64998  1.000 26.05250  ? 343 PHE A CB    1 
ATOM   2652 C  CG    . PHE A 1 332 ? -18.78952 -17.15845 -5.26783  1.000 22.31850  ? 343 PHE A CG    1 
ATOM   2653 C  CD1   . PHE A 1 332 ? -18.52956 -16.14069 -4.37114  1.000 21.41661  ? 343 PHE A CD1   1 
ATOM   2654 C  CD2   . PHE A 1 332 ? -18.62545 -18.47513 -4.84823  1.000 24.77386  ? 343 PHE A CD2   1 
ATOM   2655 C  CE1   . PHE A 1 332 ? -18.08052 -16.43420 -3.07834  1.000 21.98840  ? 343 PHE A CE1   1 
ATOM   2656 C  CE2   . PHE A 1 332 ? -18.18845 -18.77438 -3.56769  1.000 21.88106  ? 343 PHE A CE2   1 
ATOM   2657 C  CZ    . PHE A 1 332 ? -17.91635 -17.75954 -2.68402  1.000 22.32227  ? 343 PHE A CZ    1 
ATOM   2658 N  N     . ASN A 1 333 ? -21.12809 -14.59891 -8.14363  1.000 31.68363  ? 344 ASN A N     1 
ATOM   2659 C  CA    . ASN A 1 333 ? -21.52806 -13.89232 -9.35748  1.000 28.50930  ? 344 ASN A CA    1 
ATOM   2660 C  C     . ASN A 1 333 ? -20.44647 -13.88206 -10.42739 1.000 36.07054  ? 344 ASN A C     1 
ATOM   2661 O  O     . ASN A 1 333 ? -20.74674 -13.62651 -11.59786 1.000 34.81581  ? 344 ASN A O     1 
ATOM   2662 C  CB    . ASN A 1 333 ? -21.90064 -12.44059 -9.04421  1.000 35.91166  ? 344 ASN A CB    1 
ATOM   2663 C  CG    . ASN A 1 333 ? -23.23315 -12.31855 -8.33059  1.000 54.55175  ? 344 ASN A CG    1 
ATOM   2664 O  OD1   . ASN A 1 333 ? -24.13112 -13.14193 -8.52382  1.000 50.07386  ? 344 ASN A OD1   1 
ATOM   2665 N  ND2   . ASN A 1 333 ? -23.36811 -11.28682 -7.49489  1.000 54.10646  ? 344 ASN A ND2   1 
ATOM   2666 N  N     . SER A 1 334 ? -19.19616 -14.12394 -10.06604 1.000 29.44822  ? 345 SER A N     1 
ATOM   2667 C  CA    . SER A 1 334 ? -18.15848 -14.16106 -11.08016 1.000 28.79333  ? 345 SER A CA    1 
ATOM   2668 C  C     . SER A 1 334 ? -17.07064 -15.11454 -10.63308 1.000 26.14537  ? 345 SER A C     1 
ATOM   2669 O  O     . SER A 1 334 ? -16.97516 -15.48045 -9.45695  1.000 25.52321  ? 345 SER A O     1 
ATOM   2670 C  CB    . SER A 1 334 ? -17.56894 -12.77745 -11.33071 1.000 23.06184  ? 345 SER A CB    1 
ATOM   2671 O  OG    . SER A 1 334 ? -16.89064 -12.34275 -10.17035 1.000 25.91026  ? 345 SER A OG    1 
ATOM   2672 N  N     . ILE A 1 335 ? -16.23696 -15.50231 -11.59618 1.000 28.84692  ? 346 ILE A N     1 
ATOM   2673 C  CA    . ILE A 1 335 ? -15.06782 -16.30686 -11.27229 1.000 25.20375  ? 346 ILE A CA    1 
ATOM   2674 C  C     . ILE A 1 335 ? -14.14872 -15.54621 -10.31993 1.000 22.80652  ? 346 ILE A C     1 
ATOM   2675 O  O     . ILE A 1 335 ? -13.57389 -16.12962 -9.39193  1.000 21.91124  ? 346 ILE A O     1 
ATOM   2676 C  CB    . ILE A 1 335 ? -14.35838 -16.72272 -12.57038 1.000 22.73851  ? 346 ILE A CB    1 
ATOM   2677 C  CG1   . ILE A 1 335 ? -15.29686 -17.62721 -13.39477 1.000 25.40873  ? 346 ILE A CG1   1 
ATOM   2678 C  CG2   . ILE A 1 335 ? -13.01862 -17.37989 -12.25558 1.000 19.57800  ? 346 ILE A CG2   1 
ATOM   2679 C  CD1   . ILE A 1 335 ? -14.86125 -17.87079 -14.84704 1.000 19.38272  ? 346 ILE A CD1   1 
ATOM   2680 N  N     A GLU A 1 336 ? -14.00811 -14.23459 -10.52037 0.666 20.99399  ? 347 GLU A N     1 
ATOM   2681 N  N     B GLU A 1 336 ? -14.02026 -14.22991 -10.52955 0.334 20.82236  ? 347 GLU A N     1 
ATOM   2682 C  CA    A GLU A 1 336 ? -13.13869 -13.44372 -9.65521  0.666 25.22831  ? 347 GLU A CA    1 
ATOM   2683 C  CA    B GLU A 1 336 ? -13.17101 -13.38796 -9.68984  0.334 25.21211  ? 347 GLU A CA    1 
ATOM   2684 C  C     A GLU A 1 336 ? -13.58549 -13.52027 -8.20310  0.666 25.52005  ? 347 GLU A C     1 
ATOM   2685 C  C     B GLU A 1 336 ? -13.58935 -13.46052 -8.22620  0.334 25.47859  ? 347 GLU A C     1 
ATOM   2686 O  O     A GLU A 1 336 ? -12.75281 -13.62737 -7.29468  0.666 24.34532  ? 347 GLU A O     1 
ATOM   2687 O  O     B GLU A 1 336 ? -12.73859 -13.50760 -7.32994  0.334 24.36611  ? 347 GLU A O     1 
ATOM   2688 C  CB    A GLU A 1 336 ? -13.10685 -11.98935 -10.12042 0.666 26.26946  ? 347 GLU A CB    1 
ATOM   2689 C  CB    B GLU A 1 336 ? -13.22770 -11.94050 -10.19400 0.334 26.29472  ? 347 GLU A CB    1 
ATOM   2690 C  CG    A GLU A 1 336 ? -12.24984 -11.75211 -11.34752 0.666 27.77178  ? 347 GLU A CG    1 
ATOM   2691 C  CG    B GLU A 1 336 ? -12.16762 -10.99831 -9.62931  0.334 27.46669  ? 347 GLU A CG    1 
ATOM   2692 C  CD    A GLU A 1 336 ? -12.99134 -11.96236 -12.66292 0.666 26.37728  ? 347 GLU A CD    1 
ATOM   2693 C  CD    B GLU A 1 336 ? -12.38733 -9.53742  -10.03033 0.334 32.12964  ? 347 GLU A CD    1 
ATOM   2694 O  OE1   A GLU A 1 336 ? -14.10150 -12.54737 -12.67491 0.666 22.94568  ? 347 GLU A OE1   1 
ATOM   2695 O  OE1   B GLU A 1 336 ? -13.43014 -9.23724  -10.65656 0.334 33.24859  ? 347 GLU A OE1   1 
ATOM   2696 O  OE2   A GLU A 1 336 ? -12.45125 -11.52039 -13.69557 0.666 27.67352  ? 347 GLU A OE2   1 
ATOM   2697 O  OE2   B GLU A 1 336 ? -11.51948 -8.68573  -9.71272  0.334 31.68151  ? 347 GLU A OE2   1 
ATOM   2698 N  N     . GLU A 1 337 ? -14.89781 -13.47848 -7.96621  1.000 21.41818  ? 348 GLU A N     1 
ATOM   2699 C  CA    . GLU A 1 337 ? -15.39830 -13.47985 -6.59413  1.000 26.89656  ? 348 GLU A CA    1 
ATOM   2700 C  C     . GLU A 1 337 ? -15.27962 -14.85463 -5.95320  1.000 25.34790  ? 348 GLU A C     1 
ATOM   2701 O  O     . GLU A 1 337 ? -15.03603 -14.95608 -4.74263  1.000 25.57335  ? 348 GLU A O     1 
ATOM   2702 C  CB    . GLU A 1 337 ? -16.85030 -12.98805 -6.56552  1.000 26.74281  ? 348 GLU A CB    1 
ATOM   2703 C  CG    . GLU A 1 337 ? -16.95271 -11.47435 -6.64014  1.000 34.06180  ? 348 GLU A CG    1 
ATOM   2704 C  CD    . GLU A 1 337 ? -18.29118 -10.98467 -7.17825  1.000 39.37036  ? 348 GLU A CD    1 
ATOM   2705 O  OE1   . GLU A 1 337 ? -18.65224 -11.37211 -8.30515  1.000 46.22041  ? 348 GLU A OE1   1 
ATOM   2706 O  OE2   . GLU A 1 337 ? -18.97839 -10.21245 -6.48077  1.000 45.94040  ? 348 GLU A OE2   1 
ATOM   2707 N  N     . ALA A 1 338 ? -15.47152 -15.92009 -6.73978  1.000 21.31374  ? 349 ALA A N     1 
ATOM   2708 C  CA    . ALA A 1 338 ? -15.17931 -17.25727 -6.23630  1.000 23.85201  ? 349 ALA A CA    1 
ATOM   2709 C  C     . ALA A 1 338 ? -13.71040 -17.38291 -5.84501  1.000 22.89429  ? 349 ALA A C     1 
ATOM   2710 O  O     . ALA A 1 338 ? -13.38918 -17.97779 -4.80887  1.000 18.57728  ? 349 ALA A O     1 
ATOM   2711 C  CB    . ALA A 1 338 ? -15.54044 -18.31077 -7.28655  1.000 18.72942  ? 349 ALA A CB    1 
ATOM   2712 N  N     . ILE A 1 339 ? -12.80770 -16.82705 -6.67180  1.000 22.64328  ? 350 ILE A N     1 
ATOM   2713 C  CA    . ILE A 1 339 ? -11.37007 -16.84524 -6.37667  1.000 21.41277  ? 350 ILE A CA    1 
ATOM   2714 C  C     . ILE A 1 339 ? -11.08481 -16.06619 -5.10195  1.000 22.43727  ? 350 ILE A C     1 
ATOM   2715 O  O     . ILE A 1 339 ? -10.41329 -16.55831 -4.18613  1.000 23.93170  ? 350 ILE A O     1 
ATOM   2716 C  CB    . ILE A 1 339 ? -10.56710 -16.27459 -7.56430  1.000 18.69561  ? 350 ILE A CB    1 
ATOM   2717 C  CG1   . ILE A 1 339 ? -10.48024 -17.28844 -8.70687  1.000 18.41806  ? 350 ILE A CG1   1 
ATOM   2718 C  CG2   . ILE A 1 339 ? -9.18662  -15.77731 -7.10674  1.000 20.51205  ? 350 ILE A CG2   1 
ATOM   2719 C  CD1   . ILE A 1 339 ? -9.91385  -16.71050 -10.00312 1.000 22.23704  ? 350 ILE A CD1   1 
ATOM   2720 N  N     . GLU A 1 340 ? -11.58498 -14.83037 -5.03410  1.000 21.13435  ? 351 GLU A N     1 
ATOM   2721 C  CA    . GLU A 1 340 ? -11.38710 -13.98549 -3.85678  1.000 21.73616  ? 351 GLU A CA    1 
ATOM   2722 C  C     . GLU A 1 340 ? -11.78508 -14.69834 -2.57365  1.000 24.93271  ? 351 GLU A C     1 
ATOM   2723 O  O     . GLU A 1 340 ? -11.06729 -14.63282 -1.57605  1.000 26.74499  ? 351 GLU A O     1 
ATOM   2724 C  CB    . GLU A 1 340 ? -12.18783 -12.69056 -3.99835  1.000 26.08249  ? 351 GLU A CB    1 
ATOM   2725 C  CG    . GLU A 1 340 ? -12.20162 -11.78658 -2.75174  1.000 30.93953  ? 351 GLU A CG    1 
ATOM   2726 C  CD    . GLU A 1 340 ? -10.86241 -11.11114 -2.50215  1.000 42.57654  ? 351 GLU A CD    1 
ATOM   2727 O  OE1   . GLU A 1 340 ? -9.93596  -11.31218 -3.31631  1.000 43.97415  ? 351 GLU A OE1   1 
ATOM   2728 O  OE2   . GLU A 1 340 ? -10.73020 -10.37322 -1.50155  1.000 50.78458  ? 351 GLU A OE2   1 
ATOM   2729 N  N     . ASN A 1 341 ? -12.92829 -15.38718 -2.58229  1.000 24.68357  ? 352 ASN A N     1 
ATOM   2730 C  CA    . ASN A 1 341 ? -13.37383 -16.09401 -1.38671  1.000 20.69763  ? 352 ASN A CA    1 
ATOM   2731 C  C     . ASN A 1 341 ? -12.42067 -17.23467 -1.01933  1.000 20.33955  ? 352 ASN A C     1 
ATOM   2732 O  O     . ASN A 1 341 ? -12.11932 -17.44517 0.16398   1.000 25.47840  ? 352 ASN A O     1 
ATOM   2733 C  CB    . ASN A 1 341 ? -14.78847 -16.61610 -1.59609  1.000 21.12837  ? 352 ASN A CB    1 
ATOM   2734 C  CG    . ASN A 1 341 ? -15.33606 -17.28429 -0.35674  1.000 27.31613  ? 352 ASN A CG    1 
ATOM   2735 O  OD1   . ASN A 1 341 ? -15.20161 -18.49545 -0.17695  1.000 24.24839  ? 352 ASN A OD1   1 
ATOM   2736 N  ND2   . ASN A 1 341 ? -15.91914 -16.48771 0.52666   1.000 23.49149  ? 352 ASN A ND2   1 
ATOM   2737 N  N     . TYR A 1 342 ? -11.92991 -17.97410 -2.01717  1.000 20.78655  ? 353 TYR A N     1 
ATOM   2738 C  CA    . TYR A 1 342 ? -10.90595 -18.98632 -1.75972  1.000 19.21201  ? 353 TYR A CA    1 
ATOM   2739 C  C     . TYR A 1 342 ? -9.65798  -18.35761 -1.14536  1.000 23.77011  ? 353 TYR A C     1 
ATOM   2740 O  O     . TYR A 1 342 ? -9.16298  -18.81859 -0.10853  1.000 22.29632  ? 353 TYR A O     1 
ATOM   2741 C  CB    . TYR A 1 342 ? -10.54474 -19.73401 -3.04879  1.000 19.62210  ? 353 TYR A CB    1 
ATOM   2742 C  CG    . TYR A 1 342 ? -9.11193  -20.23220 -3.03628  1.000 21.67606  ? 353 TYR A CG    1 
ATOM   2743 C  CD1   . TYR A 1 342 ? -8.69026  -21.14315 -2.07057  1.000 19.84153  ? 353 TYR A CD1   1 
ATOM   2744 C  CD2   . TYR A 1 342 ? -8.18057  -19.78508 -3.97011  1.000 18.52522  ? 353 TYR A CD2   1 
ATOM   2745 C  CE1   . TYR A 1 342 ? -7.39942  -21.57790 -2.02038  1.000 19.30226  ? 353 TYR A CE1   1 
ATOM   2746 C  CE2   . TYR A 1 342 ? -6.86131  -20.22778 -3.92637  1.000 21.35932  ? 353 TYR A CE2   1 
ATOM   2747 C  CZ    . TYR A 1 342 ? -6.48700  -21.12279 -2.93730  1.000 18.19598  ? 353 TYR A CZ    1 
ATOM   2748 O  OH    . TYR A 1 342 ? -5.20624  -21.58768 -2.84396  1.000 19.77448  ? 353 TYR A OH    1 
ATOM   2749 N  N     . GLU A 1 343 ? -9.12193  -17.30934 -1.78032  1.000 22.56384  ? 354 GLU A N     1 
ATOM   2750 C  CA    . GLU A 1 343 ? -7.87205  -16.73571 -1.29439  1.000 23.63450  ? 354 GLU A CA    1 
ATOM   2751 C  C     . GLU A 1 343 ? -8.02567  -16.18853 0.11840   1.000 25.04823  ? 354 GLU A C     1 
ATOM   2752 O  O     . GLU A 1 343 ? -7.11798  -16.33414 0.94138   1.000 20.84693  ? 354 GLU A O     1 
ATOM   2753 C  CB    . GLU A 1 343 ? -7.36379  -15.66297 -2.25722  1.000 18.77981  ? 354 GLU A CB    1 
ATOM   2754 C  CG    . GLU A 1 343 ? -6.94785  -16.26542 -3.61742  1.000 23.43702  ? 354 GLU A CG    1 
ATOM   2755 C  CD    . GLU A 1 343 ? -6.47448  -15.23123 -4.62579  1.000 22.99428  ? 354 GLU A CD    1 
ATOM   2756 O  OE1   . GLU A 1 343 ? -6.58033  -14.02206 -4.33604  1.000 25.65170  ? 354 GLU A OE1   1 
ATOM   2757 O  OE2   . GLU A 1 343 ? -5.99491  -15.63011 -5.71610  1.000 21.03409  ? 354 GLU A OE2   1 
ATOM   2758 N  N     . GLN A 1 344 ? -9.17866  -15.58799 0.43261   1.000 28.47473  ? 355 GLN A N     1 
ATOM   2759 C  CA    . GLN A 1 344 ? -9.37963  -15.06161 1.78142   1.000 24.51679  ? 355 GLN A CA    1 
ATOM   2760 C  C     . GLN A 1 344 ? -9.32408  -16.16931 2.82879   1.000 26.06739  ? 355 GLN A C     1 
ATOM   2761 O  O     . GLN A 1 344 ? -8.72488  -15.99199 3.89331   1.000 26.14992  ? 355 GLN A O     1 
ATOM   2762 C  CB    . GLN A 1 344 ? -10.70869 -14.30738 1.86776   1.000 36.92396  ? 355 GLN A CB    1 
ATOM   2763 C  CG    . GLN A 1 344 ? -10.77706 -12.99840 1.04899   1.000 38.46896  ? 355 GLN A CG    1 
ATOM   2764 C  CD    . GLN A 1 344 ? -9.89997  -11.87201 1.61415   1.000 46.97190  ? 355 GLN A CD    1 
ATOM   2765 O  OE1   . GLN A 1 344 ? -8.79898  -12.10447 2.11481   1.000 44.09252  ? 355 GLN A OE1   1 
ATOM   2766 N  NE2   . GLN A 1 344 ? -10.39736 -10.64072 1.52550   1.000 56.08052  ? 355 GLN A NE2   1 
ATOM   2767 N  N     . GLN A 1 345 ? -9.94756  -17.31745 2.55539   1.000 25.23014  ? 356 GLN A N     1 
ATOM   2768 C  CA    . GLN A 1 345 ? -9.88248  -18.41761 3.51474   1.000 30.43159  ? 356 GLN A CA    1 
ATOM   2769 C  C     . GLN A 1 345 ? -8.46676  -18.95792 3.62111   1.000 26.87641  ? 356 GLN A C     1 
ATOM   2770 O  O     . GLN A 1 345 ? -7.97310  -19.20598 4.72608   1.000 26.20594  ? 356 GLN A O     1 
ATOM   2771 C  CB    . GLN A 1 345 ? -10.83780 -19.54486 3.12271   1.000 22.67335  ? 356 GLN A CB    1 
ATOM   2772 C  CG    . GLN A 1 345 ? -12.30434 -19.16202 3.15761   1.000 25.84445  ? 356 GLN A CG    1 
ATOM   2773 C  CD    . GLN A 1 345 ? -13.20616 -20.31824 2.77964   1.000 28.71944  ? 356 GLN A CD    1 
ATOM   2774 O  OE1   . GLN A 1 345 ? -13.22391 -21.34507 3.45108   1.000 35.37214  ? 356 GLN A OE1   1 
ATOM   2775 N  NE2   . GLN A 1 345 ? -13.94819 -20.16434 1.69170   1.000 23.69666  ? 356 GLN A NE2   1 
ATOM   2776 N  N     . MET A 1 346 ? -7.79833  -19.12024 2.48135   1.000 22.64944  ? 357 MET A N     1 
ATOM   2777 C  CA    . MET A 1 346 ? -6.48138  -19.74341 2.45319   1.000 23.43694  ? 357 MET A CA    1 
ATOM   2778 C  C     . MET A 1 346 ? -5.46015  -18.89268 3.18132   1.000 30.28047  ? 357 MET A C     1 
ATOM   2779 O  O     . MET A 1 346 ? -4.52772  -19.42774 3.79138   1.000 26.19015  ? 357 MET A O     1 
ATOM   2780 C  CB    . MET A 1 346 ? -6.04775  -19.99255 0.99792   1.000 19.06875  ? 357 MET A CB    1 
ATOM   2781 C  CG    . MET A 1 346 ? -4.62113  -20.51576 0.83079   1.000 20.97128  ? 357 MET A CG    1 
ATOM   2782 S  SD    . MET A 1 346 ? -3.36906  -19.21881 0.72505   1.000 23.98216  ? 357 MET A SD    1 
ATOM   2783 C  CE    . MET A 1 346 ? -3.88431  -18.39188 -0.78323  1.000 21.91512  ? 357 MET A CE    1 
ATOM   2784 N  N     . PHE A 1 347 ? -5.60185  -17.56912 3.12584   1.000 24.09512  ? 358 PHE A N     1 
ATOM   2785 C  CA    . PHE A 1 347 ? -4.66905  -16.74152 3.87813   1.000 31.06985  ? 358 PHE A CA    1 
ATOM   2786 C  C     . PHE A 1 347 ? -4.78261  -16.99667 5.38195   1.000 34.20076  ? 358 PHE A C     1 
ATOM   2787 O  O     . PHE A 1 347 ? -3.78781  -16.87482 6.10475   1.000 33.58216  ? 358 PHE A O     1 
ATOM   2788 C  CB    . PHE A 1 347 ? -4.88827  -15.26401 3.54753   1.000 29.61401  ? 358 PHE A CB    1 
ATOM   2789 C  CG    . PHE A 1 347 ? -3.97377  -14.74247 2.47111   1.000 37.80368  ? 358 PHE A CG    1 
ATOM   2790 C  CD1   . PHE A 1 347 ? -4.04257  -15.24528 1.18052   1.000 26.60131  ? 358 PHE A CD1   1 
ATOM   2791 C  CD2   . PHE A 1 347 ? -3.03853  -13.74573 2.75638   1.000 39.16450  ? 358 PHE A CD2   1 
ATOM   2792 C  CE1   . PHE A 1 347 ? -3.19889  -14.77154 0.18808   1.000 30.46780  ? 358 PHE A CE1   1 
ATOM   2793 C  CE2   . PHE A 1 347 ? -2.18651  -13.26483 1.77038   1.000 38.48182  ? 358 PHE A CE2   1 
ATOM   2794 C  CZ    . PHE A 1 347 ? -2.26752  -13.77701 0.48240   1.000 40.27237  ? 358 PHE A CZ    1 
ATOM   2795 N  N     . ILE A 1 348 ? -5.96301  -17.38130 5.87665   1.000 32.61713  ? 359 ILE A N     1 
ATOM   2796 C  CA    . ILE A 1 348 ? -6.10237  -17.61211 7.31421   1.000 28.60575  ? 359 ILE A CA    1 
ATOM   2797 C  C     . ILE A 1 348 ? -5.40107  -18.90327 7.71904   1.000 31.29860  ? 359 ILE A C     1 
ATOM   2798 O  O     . ILE A 1 348 ? -4.41378  -18.86882 8.45791   1.000 36.57804  ? 359 ILE A O     1 
ATOM   2799 C  CB    . ILE A 1 348 ? -7.57695  -17.61069 7.74125   1.000 32.85761  ? 359 ILE A CB    1 
ATOM   2800 C  CG1   . ILE A 1 348 ? -8.20311  -16.26179 7.40049   1.000 32.12235  ? 359 ILE A CG1   1 
ATOM   2801 C  CG2   . ILE A 1 348 ? -7.68832  -17.87073 9.25788   1.000 29.12949  ? 359 ILE A CG2   1 
ATOM   2802 C  CD1   . ILE A 1 348 ? -9.66717  -16.21158 7.62302   1.000 32.96667  ? 359 ILE A CD1   1 
ATOM   2803 N  N     . TYR A 1 349 ? -5.88236  -20.05824 7.23791   1.000 27.79735  ? 360 TYR A N     1 
ATOM   2804 C  CA    . TYR A 1 349 ? -5.22065  -21.31650 7.60566   1.000 27.63418  ? 360 TYR A CA    1 
ATOM   2805 C  C     . TYR A 1 349 ? -3.82233  -21.44605 7.00464   1.000 30.41396  ? 360 TYR A C     1 
ATOM   2806 O  O     . TYR A 1 349 ? -2.98941  -22.16832 7.55659   1.000 31.07041  ? 360 TYR A O     1 
ATOM   2807 C  CB    . TYR A 1 349 ? -6.07610  -22.53556 7.21472   1.000 26.51638  ? 360 TYR A CB    1 
ATOM   2808 C  CG    . TYR A 1 349 ? -6.37591  -22.73367 5.72008   1.000 24.80739  ? 360 TYR A CG    1 
ATOM   2809 C  CD1   . TYR A 1 349 ? -5.41786  -23.24911 4.86016   1.000 23.41842  ? 360 TYR A CD1   1 
ATOM   2810 C  CD2   . TYR A 1 349 ? -7.64198  -22.45448 5.19719   1.000 27.32660  ? 360 TYR A CD2   1 
ATOM   2811 C  CE1   . TYR A 1 349 ? -5.68582  -23.44872 3.50202   1.000 23.63232  ? 360 TYR A CE1   1 
ATOM   2812 C  CE2   . TYR A 1 349 ? -7.93807  -22.65597 3.83823   1.000 21.60031  ? 360 TYR A CE2   1 
ATOM   2813 C  CZ    . TYR A 1 349 ? -6.95966  -23.14718 2.99967   1.000 23.93430  ? 360 TYR A CZ    1 
ATOM   2814 O  OH    . TYR A 1 349 ? -7.23281  -23.33739 1.66105   1.000 19.52630  ? 360 TYR A OH    1 
ATOM   2815 N  N     . GLY A 1 350 ? -3.54114  -20.77855 5.88355   1.000 30.23433  ? 361 GLY A N     1 
ATOM   2816 C  CA    . GLY A 1 350 ? -2.19111  -20.82224 5.33388   1.000 25.80984  ? 361 GLY A CA    1 
ATOM   2817 C  C     . GLY A 1 350 ? -1.19833  -20.07565 6.20065   1.000 29.13463  ? 361 GLY A C     1 
ATOM   2818 O  O     . GLY A 1 350 ? -0.09454  -20.56540 6.45280   1.000 27.79747  ? 361 GLY A O     1 
ATOM   2819 N  N     . LYS A 1 351 ? -1.58732  -18.89249 6.69548   1.000 27.86754  ? 362 LYS A N     1 
ATOM   2820 C  CA    . LYS A 1 351 ? -0.70722  -18.13937 7.58451   1.000 31.60390  ? 362 LYS A CA    1 
ATOM   2821 C  C     . LYS A 1 351 ? -0.49374  -18.86663 8.90094   1.000 33.98771  ? 362 LYS A C     1 
ATOM   2822 O  O     . LYS A 1 351 ? 0.60052   -18.81858 9.46530   1.000 33.81088  ? 362 LYS A O     1 
ATOM   2823 C  CB    . LYS A 1 351 ? -1.27107  -16.74652 7.86826   1.000 34.62030  ? 362 LYS A CB    1 
ATOM   2824 C  CG    . LYS A 1 351 ? -0.91079  -15.68794 6.84945   1.000 39.73924  ? 362 LYS A CG    1 
ATOM   2825 C  CD    . LYS A 1 351 ? -1.28513  -14.29262 7.35969   1.000 35.27015  ? 362 LYS A CD    1 
ATOM   2826 C  CE    . LYS A 1 351 ? -1.55354  -13.37047 6.18493   1.000 38.44799  ? 362 LYS A CE    1 
ATOM   2827 N  NZ    . LYS A 1 351 ? -1.68054  -11.95800 6.59974   1.000 48.00467  ? 362 LYS A NZ    1 
ATOM   2828 N  N     . GLU A 1 352 ? -1.53769  -19.50887 9.42792   1.000 34.87574  ? 363 GLU A N     1 
ATOM   2829 C  CA    . GLU A 1 352 ? -1.37374  -20.27193 10.65725  1.000 35.66649  ? 363 GLU A CA    1 
ATOM   2830 C  C     . GLU A 1 352 ? -0.42464  -21.43016 10.43885  1.000 32.98293  ? 363 GLU A C     1 
ATOM   2831 O  O     . GLU A 1 352 ? 0.48428   -21.66272 11.24149  1.000 36.70020  ? 363 GLU A O     1 
ATOM   2832 C  CB    . GLU A 1 352 ? -2.72786  -20.76105 11.15380  1.000 32.58201  ? 363 GLU A CB    1 
ATOM   2833 C  CG    . GLU A 1 352 ? -3.71309  -19.63415 11.15468  1.000 50.62322  ? 363 GLU A CG    1 
ATOM   2834 C  CD    . GLU A 1 352 ? -4.84110  -19.78915 12.13876  1.000 63.63728  ? 363 GLU A CD    1 
ATOM   2835 O  OE1   . GLU A 1 352 ? -5.53258  -18.77406 12.38937  1.000 73.09595  ? 363 GLU A OE1   1 
ATOM   2836 O  OE2   . GLU A 1 352 ? -5.03161  -20.91189 12.65570  1.000 77.93567  ? 363 GLU A OE2   1 
ATOM   2837 N  N     . ALA A 1 353 ? -0.60872  -22.15985 9.33867   1.000 29.06378  ? 364 ALA A N     1 
ATOM   2838 C  CA    . ALA A 1 353 ? 0.28871   -23.26782 9.05668   1.000 26.89407  ? 364 ALA A CA    1 
ATOM   2839 C  C     . ALA A 1 353 ? 1.71905   -22.77337 8.88555   1.000 27.38413  ? 364 ALA A C     1 
ATOM   2840 O  O     . ALA A 1 353 ? 2.66220   -23.39645 9.38666   1.000 28.96642  ? 364 ALA A O     1 
ATOM   2841 C  CB    . ALA A 1 353 ? -0.19231  -24.03684 7.82507   1.000 26.96095  ? 364 ALA A CB    1 
ATOM   2842 N  N     . GLN A 1 354 ? 1.90005   -21.63113 8.22134   1.000 27.39631  ? 365 GLN A N     1 
ATOM   2843 C  CA    . GLN A 1 354 ? 3.24815   -21.10559 8.03095   1.000 25.37850  ? 365 GLN A CA    1 
ATOM   2844 C  C     . GLN A 1 354 ? 3.86602   -20.67036 9.34888   1.000 33.52366  ? 365 GLN A C     1 
ATOM   2845 O  O     . GLN A 1 354 ? 5.04007   -20.95385 9.60898   1.000 32.05745  ? 365 GLN A O     1 
ATOM   2846 C  CB    . GLN A 1 354 ? 3.24335   -19.94959 7.02954   1.000 23.08955  ? 365 GLN A CB    1 
ATOM   2847 C  CG    . GLN A 1 354 ? 3.06321   -20.41894 5.59928   1.000 21.58118  ? 365 GLN A CG    1 
ATOM   2848 C  CD    . GLN A 1 354 ? 3.41910   -19.35497 4.57632   1.000 23.86673  ? 365 GLN A CD    1 
ATOM   2849 O  OE1   . GLN A 1 354 ? 3.37145   -18.16787 4.86647   1.000 29.34395  ? 365 GLN A OE1   1 
ATOM   2850 N  NE2   . GLN A 1 354 ? 3.78009   -19.78151 3.37099   1.000 20.32386  ? 365 GLN A NE2   1 
ATOM   2851 N  N     . GLU A 1 355 ? 3.09695   -19.98835 10.19579  1.000 31.28287  ? 366 GLU A N     1 
ATOM   2852 C  CA    . GLU A 1 355 ? 3.62765   -19.57614 11.48869  1.000 33.84110  ? 366 GLU A CA    1 
ATOM   2853 C  C     . GLU A 1 355 ? 4.07528   -20.78559 12.29513  1.000 36.84844  ? 366 GLU A C     1 
ATOM   2854 O  O     . GLU A 1 355 ? 5.17523   -20.79790 12.85895  1.000 37.65349  ? 366 GLU A O     1 
ATOM   2855 C  CB    . GLU A 1 355 ? 2.58031   -18.77089 12.25609  1.000 34.53139  ? 366 GLU A CB    1 
ATOM   2856 C  CG    . GLU A 1 355 ? 2.28371   -17.40938 11.64483  1.000 50.19996  ? 366 GLU A CG    1 
ATOM   2857 C  CD    . GLU A 1 355 ? 1.08929   -16.72435 12.30162  1.000 58.02546  ? 366 GLU A CD    1 
ATOM   2858 O  OE1   . GLU A 1 355 ? 0.10200   -16.39799 11.60136  1.000 62.48431  ? 366 GLU A OE1   1 
ATOM   2859 O  OE2   . GLU A 1 355 ? 1.14147   -16.52540 13.53431  1.000 67.28503  ? 366 GLU A OE2   1 
ATOM   2860 N  N     . GLU A 1 356 ? 3.24255   -21.82891 12.33238  1.000 31.78916  ? 367 GLU A N     1 
ATOM   2861 C  CA    . GLU A 1 356 ? 3.59716   -23.03012 13.07773  1.000 33.85160  ? 367 GLU A CA    1 
ATOM   2862 C  C     . GLU A 1 356 ? 4.82407   -23.71470 12.48421  1.000 34.86504  ? 367 GLU A C     1 
ATOM   2863 O  O     . GLU A 1 356 ? 5.71726   -24.14880 13.21684  1.000 36.49845  ? 367 GLU A O     1 
ATOM   2864 C  CB    . GLU A 1 356 ? 2.41442   -23.99380 13.11039  1.000 38.07669  ? 367 GLU A CB    1 
ATOM   2865 C  CG    . GLU A 1 356 ? 2.72834   -25.29553 13.83098  1.000 53.22897  ? 367 GLU A CG    1 
ATOM   2866 C  CD    . GLU A 1 356 ? 1.53198   -26.22656 13.89842  1.000 74.17422  ? 367 GLU A CD    1 
ATOM   2867 O  OE1   . GLU A 1 356 ? 0.39233   -25.74843 13.67319  1.000 74.86417  ? 367 GLU A OE1   1 
ATOM   2868 O  OE2   . GLU A 1 356 ? 1.73609   -27.43497 14.17445  1.000 71.98024  ? 367 GLU A OE2   1 
ATOM   2869 N  N     A SER A 1 357 ? 4.88566   -23.82958 11.15616  0.649 34.30199  ? 368 SER A N     1 
ATOM   2870 N  N     B SER A 1 357 ? 4.88073   -23.82772 11.15834  0.351 34.27035  ? 368 SER A N     1 
ATOM   2871 C  CA    A SER A 1 357 ? 6.03795   -24.48018 10.53971  0.649 32.73744  ? 368 SER A CA    1 
ATOM   2872 C  CA    B SER A 1 357 ? 6.03120   -24.46618 10.53174  0.351 32.73386  ? 368 SER A CA    1 
ATOM   2873 C  C     A SER A 1 357 ? 7.31340   -23.67339 10.77308  0.649 31.52403  ? 368 SER A C     1 
ATOM   2874 C  C     B SER A 1 357 ? 7.30758   -23.67109 10.78245  0.351 31.55048  ? 368 SER A C     1 
ATOM   2875 O  O     A SER A 1 357 ? 8.37954   -24.24548 11.02654  0.649 31.28882  ? 368 SER A O     1 
ATOM   2876 O  O     B SER A 1 357 ? 8.37068   -24.24873 11.03810  0.351 31.32969  ? 368 SER A O     1 
ATOM   2877 C  CB    A SER A 1 357 ? 5.78399   -24.69919 9.04533   0.649 28.54585  ? 368 SER A CB    1 
ATOM   2878 C  CB    B SER A 1 357 ? 5.78117   -24.63361 9.03616   0.351 28.60201  ? 368 SER A CB    1 
ATOM   2879 O  OG    A SER A 1 357 ? 5.92632   -23.49105 8.32383   0.649 30.65143  ? 368 SER A OG    1 
ATOM   2880 O  OG    B SER A 1 357 ? 6.97608   -25.01250 8.39073   0.351 31.04722  ? 368 SER A OG    1 
ATOM   2881 N  N     . THR A 1 358 ? 7.21992   -22.34309 10.72510  1.000 28.83510  ? 369 THR A N     1 
ATOM   2882 C  CA    . THR A 1 358 ? 8.39567   -21.51692 10.96355  1.000 30.30783  ? 369 THR A CA    1 
ATOM   2883 C  C     . THR A 1 358 ? 8.82629   -21.56902 12.42649  1.000 36.64900  ? 369 THR A C     1 
ATOM   2884 O  O     . THR A 1 358 ? 10.02450  -21.67430 12.72146  1.000 37.40476  ? 369 THR A O     1 
ATOM   2885 C  CB    . THR A 1 358 ? 8.11012   -20.08331 10.52776  1.000 29.74354  ? 369 THR A CB    1 
ATOM   2886 O  OG1   . THR A 1 358 ? 7.99032   -20.05903 9.10550   1.000 32.38122  ? 369 THR A OG1   1 
ATOM   2887 C  CG2   . THR A 1 358 ? 9.23162   -19.14644 10.94459  1.000 28.63749  ? 369 THR A CG2   1 
ATOM   2888 N  N     . GLN A 1 359 ? 7.87005   -21.50896 13.35713  1.000 33.06555  ? 370 GLN A N     1 
ATOM   2889 C  CA    . GLN A 1 359 ? 8.22101   -21.62193 14.76971  1.000 40.28371  ? 370 GLN A CA    1 
ATOM   2890 C  C     . GLN A 1 359 ? 8.82343   -22.98273 15.06301  1.000 37.31683  ? 370 GLN A C     1 
ATOM   2891 O  O     . GLN A 1 359 ? 9.85880   -23.09149 15.72964  1.000 38.60964  ? 370 GLN A O     1 
ATOM   2892 C  CB    . GLN A 1 359 ? 6.99798   -21.38337 15.65257  1.000 36.91660  ? 370 GLN A CB    1 
ATOM   2893 C  CG    . GLN A 1 359 ? 6.89243   -19.95452 16.13681  1.000 59.38880  ? 370 GLN A CG    1 
ATOM   2894 C  CD    . GLN A 1 359 ? 8.25718   -19.30213 16.35337  1.000 56.39800  ? 370 GLN A CD    1 
ATOM   2895 O  OE1   . GLN A 1 359 ? 9.02324   -19.70394 17.22958  1.000 53.98195  ? 370 GLN A OE1   1 
ATOM   2896 N  NE2   . GLN A 1 359 ? 8.56180   -18.28820 15.54344  1.000 60.94577  ? 370 GLN A NE2   1 
ATOM   2897 N  N     . ASN A 1 360 ? 8.18793   -24.03425 14.55593  1.000 35.55912  ? 371 ASN A N     1 
ATOM   2898 C  CA    . ASN A 1 360 ? 8.72950   -25.37191 14.71951  1.000 35.39577  ? 371 ASN A CA    1 
ATOM   2899 C  C     . ASN A 1 360 ? 10.15544  -25.46527 14.18838  1.000 35.92170  ? 371 ASN A C     1 
ATOM   2900 O  O     . ASN A 1 360 ? 11.02690  -26.05942 14.83655  1.000 33.88902  ? 371 ASN A O     1 
ATOM   2901 C  CB    . ASN A 1 360 ? 7.82557   -26.37759 14.01928  1.000 33.74382  ? 371 ASN A CB    1 
ATOM   2902 C  CG    . ASN A 1 360 ? 8.30237   -27.77129 14.19892  1.000 45.27237  ? 371 ASN A CG    1 
ATOM   2903 O  OD1   . ASN A 1 360 ? 9.16325   -28.22959 13.45758  1.000 55.57442  ? 371 ASN A OD1   1 
ATOM   2904 N  ND2   . ASN A 1 360 ? 7.76909   -28.46305 15.20196  1.000 51.80449  ? 371 ASN A ND2   1 
ATOM   2905 N  N     . GLU A 1 361 ? 10.41346  -24.87713 13.01530  1.000 30.82605  ? 372 GLU A N     1 
ATOM   2906 C  CA    . GLU A 1 361 ? 11.75803  -24.90737 12.44646  1.000 33.14767  ? 372 GLU A CA    1 
ATOM   2907 C  C     . GLU A 1 361 ? 12.76958  -24.26652 13.39277  1.000 38.00822  ? 372 GLU A C     1 
ATOM   2908 O  O     . GLU A 1 361 ? 13.83484  -24.83379 13.66378  1.000 35.75578  ? 372 GLU A O     1 
ATOM   2909 C  CB    . GLU A 1 361 ? 11.75895  -24.20144 11.09230  1.000 32.77896  ? 372 GLU A CB    1 
ATOM   2910 C  CG    . GLU A 1 361 ? 13.08829  -24.27489 10.34503  1.000 36.01450  ? 372 GLU A CG    1 
ATOM   2911 C  CD    . GLU A 1 361 ? 13.03678  -23.55318 9.00717   1.000 33.11763  ? 372 GLU A CD    1 
ATOM   2912 O  OE1   . GLU A 1 361 ? 12.24967  -22.59903 8.87464   1.000 35.43864  ? 372 GLU A OE1   1 
ATOM   2913 O  OE2   . GLU A 1 361 ? 13.76829  -23.94738 8.08161   1.000 32.51999  ? 372 GLU A OE2   1 
ATOM   2914 N  N     . ILE A 1 362 ? 12.44016  -23.08201 13.91346  1.000 33.19351  ? 373 ILE A N     1 
ATOM   2915 C  CA    . ILE A 1 362 ? 13.29966  -22.40324 14.88049  1.000 41.10733  ? 373 ILE A CA    1 
ATOM   2916 C  C     . ILE A 1 362 ? 13.63398  -23.32487 16.04602  1.000 38.71132  ? 373 ILE A C     1 
ATOM   2917 O  O     . ILE A 1 362 ? 14.79110  -23.41337 16.48051  1.000 37.15218  ? 373 ILE A O     1 
ATOM   2918 C  CB    . ILE A 1 362 ? 12.61868  -21.10982 15.36225  1.000 34.24111  ? 373 ILE A CB    1 
ATOM   2919 C  CG1   . ILE A 1 362 ? 12.67055  -20.05097 14.26266  1.000 43.24785  ? 373 ILE A CG1   1 
ATOM   2920 C  CG2   . ILE A 1 362 ? 13.24869  -20.60168 16.64428  1.000 39.65808  ? 373 ILE A CG2   1 
ATOM   2921 C  CD1   . ILE A 1 362 ? 11.78879  -18.84310 14.53468  1.000 36.10155  ? 373 ILE A CD1   1 
ATOM   2922 N  N     . GLU A 1 363 ? 12.62592  -24.03022 16.56366  1.000 36.58456  ? 374 GLU A N     1 
ATOM   2923 C  CA    . GLU A 1 363 ? 12.82054  -24.83762 17.76039  1.000 34.39948  ? 374 GLU A CA    1 
ATOM   2924 C  C     . GLU A 1 363 ? 13.64421  -26.08167 17.47256  1.000 38.24528  ? 374 GLU A C     1 
ATOM   2925 O  O     . GLU A 1 363 ? 14.56244  -26.40549 18.23488  1.000 37.15530  ? 374 GLU A O     1 
ATOM   2926 C  CB    . GLU A 1 363 ? 11.46969  -25.20365 18.36685  1.000 37.73186  ? 374 GLU A CB    1 
ATOM   2927 C  CG    . GLU A 1 363 ? 11.03266  -24.17815 19.39319  1.000 52.00187  ? 374 GLU A CG    1 
ATOM   2928 C  CD    . GLU A 1 363 ? 9.57102   -23.81153 19.27637  1.000 65.69107  ? 374 GLU A CD    1 
ATOM   2929 O  OE1   . GLU A 1 363 ? 8.75434   -24.73381 19.05592  1.000 72.75799  ? 374 GLU A OE1   1 
ATOM   2930 O  OE2   . GLU A 1 363 ? 9.24071   -22.60627 19.39583  1.000 69.94946  ? 374 GLU A OE2   1 
ATOM   2931 N  N     . MET A 1 364 ? 13.36115  -26.76949 16.35893  1.000 32.94212  ? 375 MET A N     1 
ATOM   2932 C  CA    . MET A 1 364 ? 13.99202  -28.05805 16.10491  1.000 40.42944  ? 375 MET A CA    1 
ATOM   2933 C  C     . MET A 1 364 ? 15.47157  -27.94829 15.77827  1.000 40.63002  ? 375 MET A C     1 
ATOM   2934 O  O     . MET A 1 364 ? 16.16783  -28.96646 15.80174  1.000 36.93671  ? 375 MET A O     1 
ATOM   2935 C  CB    . MET A 1 364 ? 13.28291  -28.78193 14.96755  1.000 36.03049  ? 375 MET A CB    1 
ATOM   2936 C  CG    . MET A 1 364 ? 11.91390  -29.26813 15.35254  1.000 42.11917  ? 375 MET A CG    1 
ATOM   2937 S  SD    . MET A 1 364 ? 11.17268  -30.37152 14.14381  1.000 56.15423  ? 375 MET A SD    1 
ATOM   2938 C  CE    . MET A 1 364 ? 9.89546   -31.09502 15.19475  1.000 48.23749  ? 375 MET A CE    1 
ATOM   2939 N  N     . PHE A 1 365 ? 15.96586  -26.75410 15.46291  1.000 40.83889  ? 376 PHE A N     1 
ATOM   2940 C  CA    . PHE A 1 365 ? 17.35645  -26.57979 15.06940  1.000 39.05629  ? 376 PHE A CA    1 
ATOM   2941 C  C     . PHE A 1 365 ? 18.15186  -25.76499 16.07112  1.000 43.99205  ? 376 PHE A C     1 
ATOM   2942 O  O     . PHE A 1 365 ? 19.28242  -25.36414 15.77131  1.000 49.76912  ? 376 PHE A O     1 
ATOM   2943 C  CB    . PHE A 1 365 ? 17.43571  -25.95831 13.68037  1.000 31.72253  ? 376 PHE A CB    1 
ATOM   2944 C  CG    . PHE A 1 365 ? 17.00598  -26.89302 12.61496  1.000 35.18011  ? 376 PHE A CG    1 
ATOM   2945 C  CD1   . PHE A 1 365 ? 17.85849  -27.90420 12.19153  1.000 32.79175  ? 376 PHE A CD1   1 
ATOM   2946 C  CD2   . PHE A 1 365 ? 15.73112  -26.81480 12.08090  1.000 26.38084  ? 376 PHE A CD2   1 
ATOM   2947 C  CE1   . PHE A 1 365 ? 17.46185  -28.80630 11.21903  1.000 33.39485  ? 376 PHE A CE1   1 
ATOM   2948 C  CE2   . PHE A 1 365 ? 15.31941  -27.71509 11.11435  1.000 34.28500  ? 376 PHE A CE2   1 
ATOM   2949 C  CZ    . PHE A 1 365 ? 16.19132  -28.71490 10.67698  1.000 33.41747  ? 376 PHE A CZ    1 
ATOM   2950 N  N     . LYS A 1 366 ? 17.59092  -25.50788 17.24388  1.000 43.30217  ? 377 LYS A N     1 
ATOM   2951 C  CA    . LYS A 1 366 ? 18.40108  -25.03318 18.35061  1.000 46.39370  ? 377 LYS A CA    1 
ATOM   2952 C  C     . LYS A 1 366 ? 19.39069  -26.12755 18.74819  1.000 51.67058  ? 377 LYS A C     1 
ATOM   2953 O  O     . LYS A 1 366 ? 19.03721  -27.31414 18.74583  1.000 53.63708  ? 377 LYS A O     1 
ATOM   2954 C  CB    . LYS A 1 366 ? 17.51218  -24.64858 19.52935  1.000 43.78012  ? 377 LYS A CB    1 
ATOM   2955 C  CG    . LYS A 1 366 ? 16.74094  -23.38003 19.29629  1.000 43.05960  ? 377 LYS A CG    1 
ATOM   2956 C  CD    . LYS A 1 366 ? 15.79683  -23.08926 20.44427  1.000 54.48285  ? 377 LYS A CD    1 
ATOM   2957 C  CE    . LYS A 1 366 ? 15.56617  -21.58887 20.57608  1.000 52.48414  ? 377 LYS A CE    1 
ATOM   2958 N  NZ    . LYS A 1 366 ? 16.03563  -20.84655 19.36259  1.000 54.59573  ? 377 LYS A NZ    1 
ATOM   2959 N  N     . PRO A 1 367 ? 20.63541  -25.77180 19.07838  1.000 63.05090  ? 378 PRO A N     1 
ATOM   2960 C  CA    . PRO A 1 367 ? 21.68038  -26.80473 19.23511  1.000 55.83624  ? 378 PRO A CA    1 
ATOM   2961 C  C     . PRO A 1 367 ? 21.33626  -27.88574 20.24701  1.000 55.11250  ? 378 PRO A C     1 
ATOM   2962 O  O     . PRO A 1 367 ? 21.78960  -29.03007 20.10488  1.000 52.72082  ? 378 PRO A O     1 
ATOM   2963 C  CB    . PRO A 1 367 ? 22.90932  -25.99294 19.67795  1.000 62.07698  ? 378 PRO A CB    1 
ATOM   2964 C  CG    . PRO A 1 367 ? 22.62393  -24.57266 19.24323  1.000 60.96006  ? 378 PRO A CG    1 
ATOM   2965 C  CD    . PRO A 1 367 ? 21.13797  -24.41209 19.35341  1.000 58.65463  ? 378 PRO A CD    1 
ATOM   2966 N  N     . ASP A 1 368 ? 20.53986  -27.56014 21.26322  1.000 51.83445  ? 379 ASP A N     1 
ATOM   2967 C  CA    . ASP A 1 368 ? 20.18760  -28.49307 22.32537  1.000 58.04133  ? 379 ASP A CA    1 
ATOM   2968 C  C     . ASP A 1 368 ? 18.77301  -29.05897 22.18111  1.000 60.46752  ? 379 ASP A C     1 
ATOM   2969 O  O     . ASP A 1 368 ? 18.15795  -29.45300 23.18071  1.000 56.27132  ? 379 ASP A O     1 
ATOM   2970 C  CB    . ASP A 1 368 ? 20.35634  -27.81097 23.68438  1.000 69.84023  ? 379 ASP A CB    1 
ATOM   2971 C  CG    . ASP A 1 368 ? 19.67132  -26.44509 23.75072  1.000 81.57891  ? 379 ASP A CG    1 
ATOM   2972 O  OD1   . ASP A 1 368 ? 18.96928  -26.05798 22.78489  1.000 65.56294  ? 379 ASP A OD1   1 
ATOM   2973 O  OD2   . ASP A 1 368 ? 19.84092  -25.75483 24.78229  1.000 85.32845  ? 379 ASP A OD2   1 
ATOM   2974 N  N     . PHE A 1 369 ? 18.24323  -29.12386 20.96004  1.000 60.30790  ? 380 PHE A N     1 
ATOM   2975 C  CA    . PHE A 1 369 ? 16.88723  -29.62963 20.77819  1.000 54.33912  ? 380 PHE A CA    1 
ATOM   2976 C  C     . PHE A 1 369 ? 16.83957  -31.14488 20.93458  1.000 52.04949  ? 380 PHE A C     1 
ATOM   2977 O  O     . PHE A 1 369 ? 17.73283  -31.86602 20.47915  1.000 47.75362  ? 380 PHE A O     1 
ATOM   2978 C  CB    . PHE A 1 369 ? 16.33803  -29.24265 19.40770  1.000 43.32211  ? 380 PHE A CB    1 
ATOM   2979 C  CG    . PHE A 1 369 ? 15.05757  -29.95310 19.03982  1.000 42.60835  ? 380 PHE A CG    1 
ATOM   2980 C  CD1   . PHE A 1 369 ? 13.83219  -29.49257 19.50518  1.000 44.62966  ? 380 PHE A CD1   1 
ATOM   2981 C  CD2   . PHE A 1 369 ? 15.07577  -31.06687 18.20947  1.000 39.10573  ? 380 PHE A CD2   1 
ATOM   2982 C  CE1   . PHE A 1 369 ? 12.65116  -30.13415 19.16047  1.000 44.66885  ? 380 PHE A CE1   1 
ATOM   2983 C  CE2   . PHE A 1 369 ? 13.89874  -31.71631 17.86376  1.000 41.80578  ? 380 PHE A CE2   1 
ATOM   2984 C  CZ    . PHE A 1 369 ? 12.68429  -31.24899 18.33778  1.000 36.69090  ? 380 PHE A CZ    1 
ATOM   2985 N  N     . THR A 1 370 ? 15.78305  -31.61551 21.59861  1.000 58.26947  ? 381 THR A N     1 
ATOM   2986 C  CA    . THR A 1 370 ? 15.40813  -33.02038 21.63594  1.000 62.00607  ? 381 THR A CA    1 
ATOM   2987 C  C     . THR A 1 370 ? 13.91346  -33.13124 21.36889  1.000 59.67954  ? 381 THR A C     1 
ATOM   2988 O  O     . THR A 1 370 ? 13.12890  -32.26201 21.76803  1.000 59.64233  ? 381 THR A O     1 
ATOM   2989 C  CB    . THR A 1 370 ? 15.72808  -33.68916 22.99135  1.000 65.81139  ? 381 THR A CB    1 
ATOM   2990 O  OG1   . THR A 1 370 ? 14.75312  -33.29105 23.96971  1.000 58.04132  ? 381 THR A OG1   1 
ATOM   2991 C  CG2   . THR A 1 370 ? 17.11914  -33.30520 23.46880  1.000 61.45146  ? 381 THR A CG2   1 
ATOM   2992 N  N     . PHE A 1 371 ? 13.52861  -34.20249 20.68157  1.000 54.76843  ? 382 PHE A N     1 
ATOM   2993 C  CA    . PHE A 1 371 ? 12.12212  -34.48378 20.40685  1.000 57.42275  ? 382 PHE A CA    1 
ATOM   2994 C  C     . PHE A 1 371 ? 11.35967  -34.77607 21.70193  1.000 62.08779  ? 382 PHE A C     1 
ATOM   2995 O  O     . PHE A 1 371 ? 10.14009  -34.60752 21.77212  1.000 70.08421  ? 382 PHE A O     1 
ATOM   2996 C  CB    . PHE A 1 371 ? 11.98613  -35.66705 19.43617  1.000 48.55838  ? 382 PHE A CB    1 
ATOM   2997 C  CG    . PHE A 1 371 ? 12.35493  -35.34348 18.00887  1.000 46.23950  ? 382 PHE A CG    1 
ATOM   2998 C  CD1   . PHE A 1 371 ? 11.43682  -34.74186 17.16236  1.000 45.20447  ? 382 PHE A CD1   1 
ATOM   2999 C  CD2   . PHE A 1 371 ? 13.61397  -35.66198 17.50811  1.000 44.00417  ? 382 PHE A CD2   1 
ATOM   3000 C  CE1   . PHE A 1 371 ? 11.76742  -34.44310 15.83931  1.000 39.60712  ? 382 PHE A CE1   1 
ATOM   3001 C  CE2   . PHE A 1 371 ? 13.95422  -35.37178 16.18971  1.000 37.57335  ? 382 PHE A CE2   1 
ATOM   3002 C  CZ    . PHE A 1 371 ? 13.02560  -34.75622 15.34933  1.000 36.78976  ? 382 PHE A CZ    1 
HETATM 3003 P  PA    . FDA B 2 .   ? 4.45208   -30.22041 -6.25496  1.000 17.81039  ? 401 FDA A PA    1 
HETATM 3004 O  O1A   . FDA B 2 .   ? 4.26587   -31.54334 -5.58813  1.000 16.63712  ? 401 FDA A O1A   1 
HETATM 3005 O  O2A   . FDA B 2 .   ? 5.78518   -29.55437 -6.22374  1.000 19.95943  ? 401 FDA A O2A   1 
HETATM 3006 O  O5B   . FDA B 2 .   ? 3.83500   -30.29008 -7.77685  1.000 21.61137  ? 401 FDA A O5B   1 
HETATM 3007 C  C5B   . FDA B 2 .   ? 4.20765   -29.32325 -8.74703  1.000 22.79873  ? 401 FDA A C5B   1 
HETATM 3008 C  C4B   . FDA B 2 .   ? 4.03577   -29.98059 -10.11029 1.000 17.53360  ? 401 FDA A C4B   1 
HETATM 3009 O  O4B   . FDA B 2 .   ? 4.18661   -29.02379 -11.15893 1.000 16.10480  ? 401 FDA A O4B   1 
HETATM 3010 C  C3B   . FDA B 2 .   ? 5.09712   -31.05953 -10.36258 1.000 20.50225  ? 401 FDA A C3B   1 
HETATM 3011 O  O3B   . FDA B 2 .   ? 4.46341   -32.20538 -10.88814 1.000 17.81674  ? 401 FDA A O3B   1 
HETATM 3012 C  C2B   . FDA B 2 .   ? 6.04680   -30.37497 -11.37645 1.000 17.88926  ? 401 FDA A C2B   1 
HETATM 3013 O  O2B   . FDA B 2 .   ? 6.66217   -31.24167 -12.27164 1.000 17.29699  ? 401 FDA A O2B   1 
HETATM 3014 C  C1B   . FDA B 2 .   ? 5.08722   -29.46422 -12.14836 1.000 17.29246  ? 401 FDA A C1B   1 
HETATM 3015 N  N9A   . FDA B 2 .   ? 5.64946   -28.27556 -12.77552 1.000 20.35341  ? 401 FDA A N9A   1 
HETATM 3016 C  C8A   . FDA B 2 .   ? 6.62806   -27.44761 -12.26894 1.000 18.77787  ? 401 FDA A C8A   1 
HETATM 3017 N  N7A   . FDA B 2 .   ? 6.88157   -26.41881 -13.04222 1.000 21.02635  ? 401 FDA A N7A   1 
HETATM 3018 C  C5A   . FDA B 2 .   ? 6.03724   -26.55674 -14.11874 1.000 18.33077  ? 401 FDA A C5A   1 
HETATM 3019 C  C6A   . FDA B 2 .   ? 5.81693   -25.79262 -15.29042 1.000 16.04235  ? 401 FDA A C6A   1 
HETATM 3020 N  N6A   . FDA B 2 .   ? 6.50110   -24.68816 -15.58544 1.000 18.30697  ? 401 FDA A N6A   1 
HETATM 3021 N  N1A   . FDA B 2 .   ? 4.87049   -26.19715 -16.14837 1.000 18.57944  ? 401 FDA A N1A   1 
HETATM 3022 C  C2A   . FDA B 2 .   ? 4.19093   -27.31464 -15.88537 1.000 20.07401  ? 401 FDA A C2A   1 
HETATM 3023 N  N3A   . FDA B 2 .   ? 4.31606   -28.10831 -14.82756 1.000 18.46536  ? 401 FDA A N3A   1 
HETATM 3024 C  C4A   . FDA B 2 .   ? 5.25053   -27.69814 -13.96590 1.000 17.19629  ? 401 FDA A C4A   1 
HETATM 3025 N  N1    . FDA B 2 .   ? 4.12370   -32.61893 2.97440   1.000 21.17768  ? 401 FDA A N1    1 
HETATM 3026 C  C2    . FDA B 2 .   ? 3.21946   -33.32685 3.67679   1.000 30.37320  ? 401 FDA A C2    1 
HETATM 3027 O  O2    . FDA B 2 .   ? 2.03515   -33.05458 3.61530   1.000 29.88704  ? 401 FDA A O2    1 
HETATM 3028 N  N3    . FDA B 2 .   ? 3.77863   -34.33818 4.42757   1.000 34.16345  ? 401 FDA A N3    1 
HETATM 3029 C  C4    . FDA B 2 .   ? 5.13151   -34.65139 4.49906   1.000 33.27133  ? 401 FDA A C4    1 
HETATM 3030 O  O4    . FDA B 2 .   ? 5.54412   -35.56054 5.18677   1.000 40.82287  ? 401 FDA A O4    1 
HETATM 3031 C  C4X   . FDA B 2 .   ? 5.98906   -33.83137 3.70706   1.000 30.20907  ? 401 FDA A C4X   1 
HETATM 3032 N  N5    . FDA B 2 .   ? 7.35547   -34.08811 3.73238   1.000 24.86264  ? 401 FDA A N5    1 
HETATM 3033 C  C5X   . FDA B 2 .   ? 8.16744   -33.27502 2.96968   1.000 26.76395  ? 401 FDA A C5X   1 
HETATM 3034 C  C6    . FDA B 2 .   ? 9.53521   -33.48193 2.96328   1.000 29.08033  ? 401 FDA A C6    1 
HETATM 3035 C  C7    . FDA B 2 .   ? 10.38623  -32.68998 2.20771   1.000 31.54256  ? 401 FDA A C7    1 
HETATM 3036 C  C7M   . FDA B 2 .   ? 11.86856  -32.94954 2.23624   1.000 36.27873  ? 401 FDA A C7M   1 
HETATM 3037 C  C8    . FDA B 2 .   ? 9.84437   -31.65829 1.43142   1.000 28.27642  ? 401 FDA A C8    1 
HETATM 3038 C  C8M   . FDA B 2 .   ? 10.71984  -30.77073 0.58899   1.000 24.42834  ? 401 FDA A C8M   1 
HETATM 3039 C  C9    . FDA B 2 .   ? 8.46527   -31.45641 1.44152   1.000 25.34215  ? 401 FDA A C9    1 
HETATM 3040 C  C9A   . FDA B 2 .   ? 7.62535   -32.24779 2.19055   1.000 24.49718  ? 401 FDA A C9A   1 
HETATM 3041 N  N10   . FDA B 2 .   ? 6.23688   -31.99800 2.18565   1.000 22.50711  ? 401 FDA A N10   1 
HETATM 3042 C  C10   . FDA B 2 .   ? 5.46656   -32.83407 2.96000   1.000 25.24727  ? 401 FDA A C10   1 
HETATM 3043 C  "C1'" . FDA B 2 .   ? 5.64630   -30.94246 1.36141   1.000 24.73695  ? 401 FDA A "C1'" 1 
HETATM 3044 C  "C2'" . FDA B 2 .   ? 4.76933   -31.51487 0.21926   1.000 27.76943  ? 401 FDA A "C2'" 1 
HETATM 3045 O  "O2'" . FDA B 2 .   ? 5.33094   -32.63158 -0.40604  1.000 21.50589  ? 401 FDA A "O2'" 1 
HETATM 3046 C  "C3'" . FDA B 2 .   ? 4.27817   -30.42058 -0.73522  1.000 21.69471  ? 401 FDA A "C3'" 1 
HETATM 3047 O  "O3'" . FDA B 2 .   ? 3.39533   -29.62674 0.01466   1.000 20.51463  ? 401 FDA A "O3'" 1 
HETATM 3048 C  "C4'" . FDA B 2 .   ? 3.53088   -30.95804 -1.96309  1.000 20.26858  ? 401 FDA A "C4'" 1 
HETATM 3049 O  "O4'" . FDA B 2 .   ? 4.36608   -31.66423 -2.86032  1.000 19.38967  ? 401 FDA A "O4'" 1 
HETATM 3050 C  "C5'" . FDA B 2 .   ? 2.81552   -29.78515 -2.64599  1.000 17.46084  ? 401 FDA A "C5'" 1 
HETATM 3051 O  "O5'" . FDA B 2 .   ? 2.26054   -30.30749 -3.82513  1.000 19.16721  ? 401 FDA A "O5'" 1 
HETATM 3052 P  P     . FDA B 2 .   ? 1.91504   -29.32055 -5.08305  1.000 15.67224  ? 401 FDA A P     1 
HETATM 3053 O  O1P   . FDA B 2 .   ? 1.08951   -30.16699 -6.00024  1.000 15.30427  ? 401 FDA A O1P   1 
HETATM 3054 O  O2P   . FDA B 2 .   ? 1.44773   -27.96385 -4.64621  1.000 15.19983  ? 401 FDA A O2P   1 
HETATM 3055 O  O3P   . FDA B 2 .   ? 3.40711   -29.10138 -5.69640  1.000 18.53741  ? 401 FDA A O3P   1 
HETATM 3056 S  S     . P77 C 3 .   ? 12.61870  -36.60802 4.40908   0.769 45.61191  ? 402 P77 A S     1 
HETATM 3057 CL CL    . P77 C 3 .   ? 9.40651   -39.95693 8.39907   0.769 56.18369  ? 402 P77 A CL    1 
HETATM 3058 C  C1    . P77 C 3 .   ? 10.32624  -38.96942 7.23862   0.769 37.63709  ? 402 P77 A C1    1 
HETATM 3059 N  N1    . P77 C 3 .   ? 10.62875  -35.22772 6.54897   0.769 35.49359  ? 402 P77 A N1    1 
HETATM 3060 C  C2    . P77 C 3 .   ? 11.16462  -39.63058 6.34876   0.769 39.91835  ? 402 P77 A C2    1 
HETATM 3061 N  N2    . P77 C 3 .   ? 6.42453   -35.36665 8.58821   0.769 55.99605  ? 402 P77 A N2    1 
HETATM 3062 C  C3    . P77 C 3 .   ? 11.81173  -38.78602 5.53511   0.769 39.37676  ? 402 P77 A C3    1 
HETATM 3063 N  N3    . P77 C 3 .   ? 4.12222   -36.89529 8.88238   0.769 58.92155  ? 402 P77 A N3    1 
HETATM 3064 C  C4    . P77 C 3 .   ? 11.63165  -37.45120 5.59832   0.769 40.48397  ? 402 P77 A C4    1 
HETATM 3065 C  C5    . P77 C 3 .   ? 10.80310  -36.74388 6.47736   0.769 38.53704  ? 402 P77 A C5    1 
HETATM 3066 C  C6    . P77 C 3 .   ? 10.10670  -37.59536 7.36107   0.769 42.52718  ? 402 P77 A C6    1 
HETATM 3067 C  C7    . P77 C 3 .   ? 12.87011  -35.09226 5.17415   0.769 36.57392  ? 402 P77 A C7    1 
HETATM 3068 C  C8    . P77 C 3 .   ? 14.04927  -34.52200 4.76637   0.769 35.85716  ? 402 P77 A C8    1 
HETATM 3069 C  C9    . P77 C 3 .   ? 14.36589  -33.31721 5.29500   0.769 39.53839  ? 402 P77 A C9    1 
HETATM 3070 C  C10   . P77 C 3 .   ? 13.49595  -32.71504 6.21604   0.769 34.87797  ? 402 P77 A C10   1 
HETATM 3071 C  C11   . P77 C 3 .   ? 12.28615  -33.33860 6.61231   0.769 37.72272  ? 402 P77 A C11   1 
HETATM 3072 C  C12   . P77 C 3 .   ? 11.94947  -34.57052 6.08256   0.769 38.76944  ? 402 P77 A C12   1 
HETATM 3073 C  C13   . P77 C 3 .   ? 9.92329   -34.60281 7.67306   0.769 41.48924  ? 402 P77 A C13   1 
HETATM 3074 C  C14   . P77 C 3 .   ? 8.38451   -34.67913 7.43155   0.769 46.93098  ? 402 P77 A C14   1 
HETATM 3075 C  C15   . P77 C 3 .   ? 7.63966   -34.84221 8.84480   0.769 49.17456  ? 402 P77 A C15   1 
HETATM 3076 C  C16   . P77 C 3 .   ? 6.53557   -36.65168 8.45390   0.769 56.86113  ? 402 P77 A C16   1 
HETATM 3077 C  C17   . P77 C 3 .   ? 5.26647   -37.49452 8.53915   0.769 54.75809  ? 402 P77 A C17   1 
HETATM 3078 C  C18   . P77 C 3 .   ? 4.29343   -35.88982 9.69823   0.769 56.45270  ? 402 P77 A C18   1 
HETATM 3079 C  C19   . P77 C 3 .   ? 5.56782   -35.09398 9.55670   0.769 54.83060  ? 402 P77 A C19   1 
HETATM 3080 C  C20   . P77 C 3 .   ? 3.28052   -37.77792 9.40390   0.769 55.32782  ? 402 P77 A C20   1 
HETATM 3081 S  S     . SO4 D 4 .   ? 3.42097   -33.99854 -27.43637 0.577 57.41541  ? 403 SO4 A S     1 
HETATM 3082 O  O1    . SO4 D 4 .   ? 3.15115   -34.33706 -28.86857 0.577 44.46553  ? 403 SO4 A O1    1 
HETATM 3083 O  O2    . SO4 D 4 .   ? 2.19357   -33.29902 -26.94711 0.577 54.83287  ? 403 SO4 A O2    1 
HETATM 3084 O  O3    . SO4 D 4 .   ? 3.64092   -35.25208 -26.63144 0.577 45.84276  ? 403 SO4 A O3    1 
HETATM 3085 O  O4    . SO4 D 4 .   ? 4.62404   -33.10499 -27.30201 0.577 38.49358  ? 403 SO4 A O4    1 
HETATM 3086 S  S     . SO4 E 4 .   ? -0.95296  -28.63741 6.60271   1.000 59.81403  ? 404 SO4 A S     1 
HETATM 3087 O  O1    . SO4 E 4 .   ? -0.37473  -28.31622 5.24878   1.000 29.55399  ? 404 SO4 A O1    1 
HETATM 3088 O  O2    . SO4 E 4 .   ? -2.45116  -28.72502 6.51863   1.000 58.06799  ? 404 SO4 A O2    1 
HETATM 3089 O  O3    . SO4 E 4 .   ? -0.37318  -29.93489 7.10027   1.000 44.00537  ? 404 SO4 A O3    1 
HETATM 3090 O  O4    . SO4 E 4 .   ? -0.66802  -27.53434 7.58835   1.000 56.66442  ? 404 SO4 A O4    1 
HETATM 3091 S  S     . SO4 F 4 .   ? -12.40613 -47.11918 14.05477  1.000 126.28827 ? 405 SO4 A S     1 
HETATM 3092 O  O1    . SO4 F 4 .   ? -11.66447 -45.81251 14.12353  1.000 95.84614  ? 405 SO4 A O1    1 
HETATM 3093 O  O2    . SO4 F 4 .   ? -12.50517 -47.56668 12.62253  1.000 111.08937 ? 405 SO4 A O2    1 
HETATM 3094 O  O3    . SO4 F 4 .   ? -11.69826 -48.16508 14.87807  1.000 87.44083  ? 405 SO4 A O3    1 
HETATM 3095 O  O4    . SO4 F 4 .   ? -13.78778 -46.91905 14.60231  1.000 123.54540 ? 405 SO4 A O4    1 
HETATM 3096 O  O     . HOH G 5 .   ? -12.34073 -10.73232 -16.13498 1.000 43.57333  ? 501 HOH A O     1 
HETATM 3097 O  O     . HOH G 5 .   ? -6.03734  -24.87354 -21.78941 1.000 20.76169  ? 502 HOH A O     1 
HETATM 3098 O  O     . HOH G 5 .   ? 6.05492   -28.28039 8.66000   1.000 40.03275  ? 503 HOH A O     1 
HETATM 3099 O  O     . HOH G 5 .   ? -9.87821  -21.96744 -25.00721 1.000 35.47029  ? 504 HOH A O     1 
HETATM 3100 O  O     . HOH G 5 .   ? 21.96235  -27.14038 12.64026  1.000 30.22521  ? 505 HOH A O     1 
HETATM 3101 O  O     . HOH G 5 .   ? 3.42559   -22.43660 -26.56518 1.000 22.87997  ? 506 HOH A O     1 
HETATM 3102 O  O     . HOH G 5 .   ? 4.80513   -40.13854 -12.29441 1.000 35.38412  ? 507 HOH A O     1 
HETATM 3103 O  O     . HOH G 5 .   ? 9.10904   -41.19634 -3.72284  1.000 29.49009  ? 508 HOH A O     1 
HETATM 3104 O  O     . HOH G 5 .   ? 0.30276   -29.68607 -8.44758  1.000 15.15953  ? 509 HOH A O     1 
HETATM 3105 O  O     . HOH G 5 .   ? -13.59044 -15.67388 -20.15765 1.000 29.25047  ? 510 HOH A O     1 
HETATM 3106 O  O     . HOH G 5 .   ? 7.56485   -28.60148 -0.71081  1.000 24.37369  ? 511 HOH A O     1 
HETATM 3107 O  O     . HOH G 5 .   ? 38.04372  -36.50590 5.20440   1.000 37.15385  ? 512 HOH A O     1 
HETATM 3108 O  O     . HOH G 5 .   ? -7.63214  -32.05249 -21.84232 1.000 30.78078  ? 513 HOH A O     1 
HETATM 3109 O  O     . HOH G 5 .   ? 1.60024   -34.46856 7.39320   1.000 40.04150  ? 514 HOH A O     1 
HETATM 3110 O  O     . HOH G 5 .   ? 15.18665  -36.25231 20.84951  1.000 51.43110  ? 515 HOH A O     1 
HETATM 3111 O  O     . HOH G 5 .   ? 5.63049   -32.03008 6.01137   1.000 40.20855  ? 516 HOH A O     1 
HETATM 3112 O  O     . HOH G 5 .   ? 10.28855  -20.70351 7.95832   1.000 31.82942  ? 517 HOH A O     1 
HETATM 3113 O  O     . HOH G 5 .   ? 16.88467  -37.65589 19.40845  1.000 33.31085  ? 518 HOH A O     1 
HETATM 3114 O  O     . HOH G 5 .   ? -16.89248 -35.06647 -16.78869 1.000 43.05700  ? 519 HOH A O     1 
HETATM 3115 O  O     . HOH G 5 .   ? -9.47319  -28.36120 -21.74139 1.000 30.03075  ? 520 HOH A O     1 
HETATM 3116 O  O     . HOH G 5 .   ? -18.12217 -16.68218 -15.97299 1.000 30.55490  ? 521 HOH A O     1 
HETATM 3117 O  O     . HOH G 5 .   ? 6.93782   -41.32873 -2.01223  1.000 24.42767  ? 522 HOH A O     1 
HETATM 3118 O  O     . HOH G 5 .   ? 7.74083   -42.11600 19.43015  1.000 40.77578  ? 523 HOH A O     1 
HETATM 3119 O  O     . HOH G 5 .   ? -11.51904 -15.20164 -18.57442 1.000 29.34033  ? 524 HOH A O     1 
HETATM 3120 O  O     . HOH G 5 .   ? 7.69002   -29.14675 -8.04336  1.000 31.34970  ? 525 HOH A O     1 
HETATM 3121 O  O     . HOH G 5 .   ? 1.35913   -15.21585 -13.22535 1.000 27.89240  ? 526 HOH A O     1 
HETATM 3122 O  O     . HOH G 5 .   ? -25.53522 -16.47048 -4.36055  1.000 43.05120  ? 527 HOH A O     1 
HETATM 3123 O  O     . HOH G 5 .   ? 17.23030  -22.56766 3.57858   1.000 29.95882  ? 528 HOH A O     1 
HETATM 3124 O  O     . HOH G 5 .   ? 18.74704  -49.70399 20.24311  1.000 40.63182  ? 529 HOH A O     1 
HETATM 3125 O  O     . HOH G 5 .   ? -8.33014  -26.15503 -20.57233 1.000 25.62011  ? 530 HOH A O     1 
HETATM 3126 O  O     . HOH G 5 .   ? -6.14616  -24.12507 -26.13852 1.000 33.91084  ? 531 HOH A O     1 
HETATM 3127 O  O     . HOH G 5 .   ? -6.04671  -36.67117 10.55965  1.000 30.05737  ? 532 HOH A O     1 
HETATM 3128 O  O     . HOH G 5 .   ? -8.73883  -49.43378 -4.10950  1.000 35.40502  ? 533 HOH A O     1 
HETATM 3129 O  O     . HOH G 5 .   ? 2.33871   -11.40709 -20.32729 1.000 36.35750  ? 534 HOH A O     1 
HETATM 3130 O  O     . HOH G 5 .   ? -12.64580 -47.93435 4.95656   1.000 32.95152  ? 535 HOH A O     1 
HETATM 3131 O  O     . HOH G 5 .   ? 6.02516   -13.38355 -7.56379  1.000 30.44630  ? 536 HOH A O     1 
HETATM 3132 O  O     . HOH G 5 .   ? -12.19798 -21.68517 5.90686   1.000 40.51453  ? 537 HOH A O     1 
HETATM 3133 O  O     . HOH G 5 .   ? -4.12542  -30.30456 7.90351   1.000 37.68711  ? 538 HOH A O     1 
HETATM 3134 O  O     . HOH G 5 .   ? 22.57434  -49.54223 9.32192   1.000 28.03565  ? 539 HOH A O     1 
HETATM 3135 O  O     . HOH G 5 .   ? 1.80923   -34.33951 -24.49816 1.000 36.95101  ? 540 HOH A O     1 
HETATM 3136 O  O     . HOH G 5 .   ? 7.41014   -35.69712 -25.42905 1.000 53.37595  ? 541 HOH A O     1 
HETATM 3137 O  O     . HOH G 5 .   ? -8.73160  -12.38205 -5.47052  1.000 30.05287  ? 542 HOH A O     1 
HETATM 3138 O  O     . HOH G 5 .   ? 2.53216   -42.72449 -10.59148 1.000 31.65389  ? 543 HOH A O     1 
HETATM 3139 O  O     . HOH G 5 .   ? 1.20962   -15.05599 -25.65663 1.000 39.33843  ? 544 HOH A O     1 
HETATM 3140 O  O     . HOH G 5 .   ? 18.75411  -29.26571 16.48094  1.000 47.27705  ? 545 HOH A O     1 
HETATM 3141 O  O     . HOH G 5 .   ? 5.10201   -33.90575 -6.56804  1.000 20.67912  ? 546 HOH A O     1 
HETATM 3142 O  O     . HOH G 5 .   ? 20.16390  -22.06554 2.90525   1.000 37.05287  ? 547 HOH A O     1 
HETATM 3143 O  O     . HOH G 5 .   ? 6.54451   -48.05792 -5.92594  1.000 48.17928  ? 548 HOH A O     1 
HETATM 3144 O  O     . HOH G 5 .   ? 32.64812  -32.58958 1.35767   1.000 40.46530  ? 549 HOH A O     1 
HETATM 3145 O  O     . HOH G 5 .   ? 33.22033  -44.24113 12.45196  1.000 39.55372  ? 550 HOH A O     1 
HETATM 3146 O  O     . HOH G 5 .   ? 35.73717  -39.52109 3.20457   1.000 28.54891  ? 551 HOH A O     1 
HETATM 3147 O  O     . HOH G 5 .   ? 0.28637   -27.50908 -26.41970 1.000 24.23164  ? 552 HOH A O     1 
HETATM 3148 O  O     . HOH G 5 .   ? -26.48651 -22.82178 -6.19339  1.000 35.25357  ? 553 HOH A O     1 
HETATM 3149 O  O     . HOH G 5 .   ? 25.23892  -34.08921 15.11643  1.000 32.01471  ? 554 HOH A O     1 
HETATM 3150 O  O     . HOH G 5 .   ? 8.44515   -30.42076 -20.41086 1.000 30.61925  ? 555 HOH A O     1 
HETATM 3151 O  O     . HOH G 5 .   ? 26.74274  -45.97801 19.83203  1.000 45.30062  ? 556 HOH A O     1 
HETATM 3152 O  O     . HOH G 5 .   ? 25.43237  -29.51321 10.89127  1.000 37.42867  ? 557 HOH A O     1 
HETATM 3153 O  O     . HOH G 5 .   ? 0.25983   -31.67199 5.13045   1.000 29.67470  ? 558 HOH A O     1 
HETATM 3154 O  O     . HOH G 5 .   ? 16.27381  -25.89593 22.87734  1.000 56.12181  ? 559 HOH A O     1 
HETATM 3155 O  O     . HOH G 5 .   ? 10.16230  -12.68311 -0.09823  1.000 42.26978  ? 560 HOH A O     1 
HETATM 3156 O  O     . HOH G 5 .   ? -5.02135  -14.57364 -25.05728 1.000 33.69714  ? 561 HOH A O     1 
HETATM 3157 O  O     . HOH G 5 .   ? 1.58609   -16.42747 -23.26625 1.000 29.05943  ? 562 HOH A O     1 
HETATM 3158 O  O     . HOH G 5 .   ? 21.74901  -36.77552 -6.84578  1.000 45.79664  ? 563 HOH A O     1 
HETATM 3159 O  O     . HOH G 5 .   ? -17.52814 -39.76284 -0.95412  1.000 29.33210  ? 564 HOH A O     1 
HETATM 3160 O  O     . HOH G 5 .   ? -19.82952 -19.02819 -18.35227 1.000 46.26839  ? 565 HOH A O     1 
HETATM 3161 O  O     . HOH G 5 .   ? 6.61798   -27.69665 -4.42727  1.000 17.37266  ? 566 HOH A O     1 
HETATM 3162 O  O     . HOH G 5 .   ? 16.05142  -42.97268 -5.49034  1.000 40.08302  ? 567 HOH A O     1 
HETATM 3163 O  O     . HOH G 5 .   ? -3.18380  -20.26952 -28.46902 1.000 29.91461  ? 568 HOH A O     1 
HETATM 3164 O  O     . HOH G 5 .   ? -12.22442 -36.11882 6.43622   1.000 37.57203  ? 569 HOH A O     1 
HETATM 3165 O  O     . HOH G 5 .   ? -7.18242  -13.83011 4.53622   1.000 42.96623  ? 570 HOH A O     1 
HETATM 3166 O  O     . HOH G 5 .   ? -5.10917  -4.05315  -11.00816 1.000 44.54568  ? 571 HOH A O     1 
HETATM 3167 O  O     . HOH G 5 .   ? -3.66907  -17.57284 -28.40883 1.000 26.42814  ? 572 HOH A O     1 
HETATM 3168 O  O     . HOH G 5 .   ? -14.48030 -36.98490 -12.74938 1.000 39.74655  ? 573 HOH A O     1 
HETATM 3169 O  O     . HOH G 5 .   ? -20.09763 -27.32712 -5.71985  1.000 39.33188  ? 574 HOH A O     1 
HETATM 3170 O  O     . HOH G 5 .   ? 4.65937   -26.70032 1.63924   1.000 19.59565  ? 575 HOH A O     1 
HETATM 3171 O  O     . HOH G 5 .   ? -16.45295 -26.07818 -18.46510 1.000 28.11476  ? 576 HOH A O     1 
HETATM 3172 O  O     . HOH G 5 .   ? 4.61862   -49.00647 11.58788  1.000 38.98225  ? 577 HOH A O     1 
HETATM 3173 O  O     . HOH G 5 .   ? 4.22991   -37.94782 5.55732   1.000 35.34251  ? 578 HOH A O     1 
HETATM 3174 O  O     . HOH G 5 .   ? 21.34758  -45.89269 -2.21348  1.000 30.39821  ? 579 HOH A O     1 
HETATM 3175 O  O     . HOH G 5 .   ? 5.53775   -14.64788 -13.33120 1.000 27.71807  ? 580 HOH A O     1 
HETATM 3176 O  O     . HOH G 5 .   ? 10.52467  -25.85306 1.86309   1.000 26.83193  ? 581 HOH A O     1 
HETATM 3177 O  O     . HOH G 5 .   ? 25.17823  -37.96666 -4.73171  1.000 29.24487  ? 582 HOH A O     1 
HETATM 3178 O  O     . HOH G 5 .   ? 8.10083   -21.30029 -15.85201 1.000 20.77718  ? 583 HOH A O     1 
HETATM 3179 O  O     . HOH G 5 .   ? 6.66291   -17.68847 8.64688   1.000 33.49198  ? 584 HOH A O     1 
HETATM 3180 O  O     . HOH G 5 .   ? 1.41923   -25.69677 -6.28480  1.000 16.73906  ? 585 HOH A O     1 
HETATM 3181 O  O     . HOH G 5 .   ? 11.96270  -41.44011 -3.62093  1.000 38.76884  ? 586 HOH A O     1 
HETATM 3182 O  O     . HOH G 5 .   ? 11.42662  -43.41190 -1.15364  1.000 32.53980  ? 587 HOH A O     1 
HETATM 3183 O  O     . HOH G 5 .   ? 27.74490  -34.09961 16.20007  1.000 40.60417  ? 588 HOH A O     1 
HETATM 3184 O  O     . HOH G 5 .   ? 12.56373  -20.73663 10.89868  1.000 40.96805  ? 589 HOH A O     1 
HETATM 3185 O  O     . HOH G 5 .   ? 28.39676  -47.38356 16.96749  1.000 34.47253  ? 590 HOH A O     1 
HETATM 3186 O  O     . HOH G 5 .   ? 1.04557   -42.49080 9.75104   1.000 48.00569  ? 591 HOH A O     1 
HETATM 3187 O  O     . HOH G 5 .   ? -12.93879 -9.18903  -0.31376  1.000 36.38523  ? 592 HOH A O     1 
HETATM 3188 O  O     . HOH G 5 .   ? 21.94187  -25.74914 15.08530  1.000 43.20522  ? 593 HOH A O     1 
HETATM 3189 O  O     . HOH G 5 .   ? -5.42971  -43.86516 -15.98169 1.000 40.44495  ? 594 HOH A O     1 
HETATM 3190 O  O     . HOH G 5 .   ? -11.10935 -8.63150  -17.01743 1.000 39.72579  ? 595 HOH A O     1 
HETATM 3191 O  O     . HOH G 5 .   ? -14.79792 -13.47581 -15.19671 1.000 37.11375  ? 596 HOH A O     1 
HETATM 3192 O  O     . HOH G 5 .   ? 6.80483   -27.85911 -23.02709 1.000 26.02646  ? 597 HOH A O     1 
HETATM 3193 O  O     . HOH G 5 .   ? 32.73551  -40.25299 11.12387  1.000 36.24656  ? 598 HOH A O     1 
HETATM 3194 O  O     . HOH G 5 .   ? -15.77471 -37.39162 -15.84600 1.000 40.69657  ? 599 HOH A O     1 
HETATM 3195 O  O     . HOH G 5 .   ? 32.50956  -36.61423 17.45926  1.000 53.00390  ? 600 HOH A O     1 
HETATM 3196 O  O     . HOH G 5 .   ? 13.63590  -50.03366 -4.81337  1.000 53.52473  ? 601 HOH A O     1 
HETATM 3197 O  O     . HOH G 5 .   ? 8.13295   -25.36550 -8.61717  1.000 27.77744  ? 602 HOH A O     1 
HETATM 3198 O  O     . HOH G 5 .   ? 16.82587  -32.99115 -0.16033  1.000 36.58588  ? 603 HOH A O     1 
HETATM 3199 O  O     . HOH G 5 .   ? 11.53025  -22.83713 -11.10827 1.000 36.59229  ? 604 HOH A O     1 
HETATM 3200 O  O     . HOH G 5 .   ? -19.95635 -25.84804 -20.39274 1.000 40.29289  ? 605 HOH A O     1 
HETATM 3201 O  O     . HOH G 5 .   ? 18.96570  -41.60847 -3.42636  1.000 27.30510  ? 606 HOH A O     1 
HETATM 3202 O  O     . HOH G 5 .   ? 19.41760  -37.41312 20.95083  1.000 38.30836  ? 607 HOH A O     1 
HETATM 3203 O  O     . HOH G 5 .   ? 0.68436   -27.34409 -0.55218  1.000 19.61050  ? 608 HOH A O     1 
HETATM 3204 O  O     . HOH G 5 .   ? 5.95068   -28.46574 3.46215   1.000 23.49762  ? 609 HOH A O     1 
HETATM 3205 O  O     . HOH G 5 .   ? 7.09799   -51.15555 17.79553  1.000 49.17200  ? 610 HOH A O     1 
HETATM 3206 O  O     . HOH G 5 .   ? 9.52460   -55.07068 12.33004  1.000 50.53238  ? 611 HOH A O     1 
HETATM 3207 O  O     . HOH G 5 .   ? -9.50185  -10.94056 -12.69871 1.000 38.30136  ? 612 HOH A O     1 
HETATM 3208 O  O     . HOH G 5 .   ? -2.19687  -8.78357  -12.20271 1.000 27.14135  ? 613 HOH A O     1 
HETATM 3209 O  O     . HOH G 5 .   ? 1.11772   -5.89780  -11.53959 1.000 41.17774  ? 614 HOH A O     1 
HETATM 3210 O  O     . HOH G 5 .   ? 7.68680   -31.19699 -4.96554  1.000 35.08826  ? 615 HOH A O     1 
HETATM 3211 O  O     . HOH G 5 .   ? 2.00433   -25.85269 2.01840   1.000 22.89868  ? 616 HOH A O     1 
HETATM 3212 O  O     . HOH G 5 .   ? 9.45907   -14.98898 5.73670   1.000 40.45510  ? 617 HOH A O     1 
HETATM 3213 O  O     . HOH G 5 .   ? -18.74446 -35.20820 -3.87766  1.000 33.62604  ? 618 HOH A O     1 
HETATM 3214 O  O     . HOH G 5 .   ? 28.80701  -49.28784 6.41031   1.000 35.05695  ? 619 HOH A O     1 
HETATM 3215 O  O     . HOH G 5 .   ? -12.61228 -10.36139 -20.05166 1.000 41.85092  ? 620 HOH A O     1 
HETATM 3216 O  O     . HOH G 5 .   ? 19.73288  -52.14112 15.32257  1.000 31.29838  ? 621 HOH A O     1 
HETATM 3217 O  O     . HOH G 5 .   ? 8.92359   -26.90326 10.26580  1.000 34.91176  ? 622 HOH A O     1 
HETATM 3218 O  O     . HOH G 5 .   ? -11.56628 -51.65388 -1.44955  1.000 47.74618  ? 623 HOH A O     1 
HETATM 3219 O  O     . HOH G 5 .   ? 8.88064   -32.89704 -11.72853 1.000 38.96516  ? 624 HOH A O     1 
HETATM 3220 O  O     . HOH G 5 .   ? -8.25030  -43.98199 -8.80858  1.000 26.21308  ? 625 HOH A O     1 
HETATM 3221 O  O     . HOH G 5 .   ? -15.73524 -29.45650 -4.84089  1.000 35.64421  ? 626 HOH A O     1 
HETATM 3222 O  O     . HOH G 5 .   ? 2.45957   -14.27873 -0.99005  1.000 32.81755  ? 627 HOH A O     1 
HETATM 3223 O  O     . HOH G 5 .   ? -2.53895  -36.07704 -23.03517 1.000 29.09477  ? 628 HOH A O     1 
HETATM 3224 O  O     . HOH G 5 .   ? -6.27170  -39.92689 -16.92350 1.000 38.67019  ? 629 HOH A O     1 
HETATM 3225 O  O     . HOH G 5 .   ? 14.24701  -50.94098 17.35264  1.000 38.48743  ? 630 HOH A O     1 
HETATM 3226 O  O     . HOH G 5 .   ? 4.78436   -12.03940 2.01225   1.000 38.16519  ? 631 HOH A O     1 
HETATM 3227 O  O     . HOH G 5 .   ? 21.19934  -43.83881 -7.15580  1.000 39.13014  ? 632 HOH A O     1 
HETATM 3228 O  O     . HOH G 5 .   ? -4.62034  -47.08870 5.11627   1.000 36.38081  ? 633 HOH A O     1 
HETATM 3229 O  O     . HOH G 5 .   ? 12.26374  -51.59397 9.68115   1.000 33.42713  ? 634 HOH A O     1 
HETATM 3230 O  O     . HOH G 5 .   ? -9.34035  -13.52475 -25.56714 1.000 21.86653  ? 635 HOH A O     1 
HETATM 3231 O  O     . HOH G 5 .   ? 1.69904   -12.32697 0.59858   1.000 43.03670  ? 636 HOH A O     1 
HETATM 3232 O  O     . HOH G 5 .   ? -12.611   -43.034   7.604     1.000 45.30381  ? 637 HOH A O     1 
HETATM 3233 O  O     . HOH G 5 .   ? 3.067     -17.856   -27.477   1.000 37.88862  ? 638 HOH A O     1 
HETATM 3234 O  O     . HOH G 5 .   ? 10.63138  -30.47814 -28.68552 1.000 57.10988  ? 639 HOH A O     1 
HETATM 3235 O  O     . HOH G 5 .   ? -9.82663  -32.55353 -20.45429 1.000 26.82644  ? 640 HOH A O     1 
HETATM 3236 O  O     . HOH G 5 .   ? -20.59395 -21.91910 -9.97652  1.000 29.79805  ? 641 HOH A O     1 
HETATM 3237 O  O     . HOH G 5 .   ? -12.65076 -31.95947 -18.29111 1.000 22.88875  ? 642 HOH A O     1 
HETATM 3238 O  O     . HOH G 5 .   ? -0.16402  -47.39936 -7.92513  1.000 42.98618  ? 643 HOH A O     1 
HETATM 3239 O  O     . HOH G 5 .   ? -10.06376 -12.66117 -7.86450  1.000 29.49127  ? 644 HOH A O     1 
HETATM 3240 O  O     . HOH G 5 .   ? -8.74953  -43.97224 12.44654  1.000 44.60669  ? 645 HOH A O     1 
HETATM 3241 O  O     . HOH G 5 .   ? -16.19110 -12.99829 -3.00682  1.000 28.29296  ? 646 HOH A O     1 
HETATM 3242 O  O     . HOH G 5 .   ? 6.82979   -34.67610 -10.56791 1.000 34.17889  ? 647 HOH A O     1 
HETATM 3243 O  O     . HOH G 5 .   ? -8.86170  -8.78436  -4.13434  1.000 43.22268  ? 648 HOH A O     1 
HETATM 3244 O  O     . HOH G 5 .   ? -10.27010 -35.17403 -20.98074 1.000 35.50900  ? 649 HOH A O     1 
HETATM 3245 O  O     . HOH G 5 .   ? 0.534     -18.130   -29.338   1.000 45.13871  ? 650 HOH A O     1 
HETATM 3246 O  O     . HOH G 5 .   ? 8.93636   -14.58023 -11.71948 1.000 34.98654  ? 651 HOH A O     1 
HETATM 3247 O  O     . HOH G 5 .   ? -3.34062  -10.32107 3.44443   1.000 47.39451  ? 652 HOH A O     1 
HETATM 3248 O  O     . HOH G 5 .   ? 9.48830   -47.55011 -5.88015  1.000 73.12514  ? 653 HOH A O     1 
HETATM 3249 O  O     . HOH G 5 .   ? 7.65181   -36.84194 1.80138   1.000 27.92565  ? 654 HOH A O     1 
HETATM 3250 O  O     . HOH G 5 .   ? -17.634   -41.618   6.582     1.000 52.04022  ? 655 HOH A O     1 
HETATM 3251 O  O     . HOH G 5 .   ? -11.76267 -41.27760 -20.26350 1.000 35.51323  ? 656 HOH A O     1 
HETATM 3252 O  O     . HOH G 5 .   ? -3.03524  -38.00821 -19.98512 1.000 29.54881  ? 657 HOH A O     1 
HETATM 3253 O  O     . HOH G 5 .   ? -8.27344  -44.45487 -15.80729 1.000 44.81901  ? 658 HOH A O     1 
HETATM 3254 O  O     . HOH G 5 .   ? -5.78005  -28.59943 -23.95061 1.000 39.80052  ? 659 HOH A O     1 
HETATM 3255 O  O     . HOH G 5 .   ? -13.70562 -44.20590 -7.12564  1.000 29.82029  ? 660 HOH A O     1 
HETATM 3256 O  O     . HOH G 5 .   ? 9.06467   -19.06118 -16.97254 1.000 26.18486  ? 661 HOH A O     1 
HETATM 3257 O  O     . HOH G 5 .   ? 11.81844  -41.20458 -14.01977 1.000 42.10228  ? 662 HOH A O     1 
HETATM 3258 O  O     . HOH G 5 .   ? 30.54587  -44.15309 15.97891  1.000 44.45929  ? 663 HOH A O     1 
HETATM 3259 O  O     . HOH G 5 .   ? 2.03144   -35.83531 -8.95589  1.000 24.74860  ? 664 HOH A O     1 
HETATM 3260 O  O     . HOH G 5 .   ? -6.00130  -11.37782 2.76812   1.000 52.18414  ? 665 HOH A O     1 
HETATM 3261 O  O     . HOH G 5 .   ? 35.12206  -38.93639 -6.72433  1.000 35.43136  ? 666 HOH A O     1 
HETATM 3262 O  O     . HOH G 5 .   ? -0.98350  -6.03060  -0.71539  1.000 49.56628  ? 667 HOH A O     1 
HETATM 3263 O  O     . HOH G 5 .   ? -15.39990 -25.43536 -23.33088 1.000 40.62996  ? 668 HOH A O     1 
HETATM 3264 O  O     . HOH G 5 .   ? 7.47916   -22.13033 -13.33498 1.000 19.50557  ? 669 HOH A O     1 
HETATM 3265 O  O     . HOH G 5 .   ? 6.78673   -15.93662 -10.48946 1.000 31.26217  ? 670 HOH A O     1 
HETATM 3266 O  O     . HOH G 5 .   ? 11.16778  -36.07321 -8.37621  1.000 37.22601  ? 671 HOH A O     1 
HETATM 3267 O  O     . HOH G 5 .   ? -4.62219  -40.17021 -20.83528 1.000 37.16607  ? 672 HOH A O     1 
HETATM 3268 O  O     . HOH G 5 .   ? 20.47006  -48.58389 -2.44148  1.000 37.95947  ? 673 HOH A O     1 
HETATM 3269 O  O     . HOH G 5 .   ? 19.78879  -31.31900 17.83742  1.000 37.23310  ? 674 HOH A O     1 
HETATM 3270 O  O     . HOH G 5 .   ? -3.45032  -6.70830  -10.77968 1.000 30.95137  ? 675 HOH A O     1 
HETATM 3271 O  O     . HOH G 5 .   ? 2.04504   -37.26118 -5.71830  1.000 19.43973  ? 676 HOH A O     1 
HETATM 3272 O  O     . HOH G 5 .   ? 4.19146   -14.81415 -17.71028 1.000 32.15775  ? 677 HOH A O     1 
HETATM 3273 O  O     . HOH G 5 .   ? 4.21819   -35.84030 -4.69273  1.000 20.62091  ? 678 HOH A O     1 
HETATM 3274 O  O     . HOH G 5 .   ? 9.09882   -10.81255 -1.70352  1.000 37.43327  ? 679 HOH A O     1 
HETATM 3275 O  O     . HOH G 5 .   ? 0.19328   -35.97945 -23.02675 1.000 26.81682  ? 680 HOH A O     1 
HETATM 3276 O  O     . HOH G 5 .   ? 10.14925  -18.91118 -7.72419  1.000 36.34750  ? 681 HOH A O     1 
HETATM 3277 O  O     . HOH G 5 .   ? -11.88371 -38.90728 6.33794   1.000 36.64807  ? 682 HOH A O     1 
HETATM 3278 O  O     . HOH G 5 .   ? 4.53086   -34.57443 -9.10649  1.000 27.34663  ? 683 HOH A O     1 
HETATM 3279 O  O     . HOH G 5 .   ? 8.83159   -27.82119 1.80980   1.000 24.87666  ? 684 HOH A O     1 
HETATM 3280 O  O     . HOH G 5 .   ? -6.23940  -48.37133 -4.25949  1.000 39.99716  ? 685 HOH A O     1 
HETATM 3281 O  O     . HOH G 5 .   ? 33.330    -44.241   8.598     1.000 31.35172  ? 686 HOH A O     1 
HETATM 3282 O  O     . HOH G 5 .   ? 0.63269   -46.03563 -12.91860 1.000 50.89708  ? 687 HOH A O     1 
HETATM 3283 O  O     . HOH G 5 .   ? -14.493   -41.465   -1.211    1.000 42.23859  ? 688 HOH A O     1 
HETATM 3284 O  O     . HOH G 5 .   ? 3.20784   -4.51331  -9.22379  1.000 45.53952  ? 689 HOH A O     1 
HETATM 3285 O  O     . HOH G 5 .   ? 23.24622  -37.36670 24.22837  1.000 50.79528  ? 690 HOH A O     1 
HETATM 3286 O  O     . HOH G 5 .   ? -4.14204  -16.56968 10.33881  1.000 38.67117  ? 691 HOH A O     1 
HETATM 3287 O  O     . HOH G 5 .   ? -13.82410 -23.21107 -23.70755 1.000 36.28499  ? 692 HOH A O     1 
HETATM 3288 O  O     . HOH G 5 .   ? 20.95528  -32.26064 -5.31438  1.000 31.31468  ? 693 HOH A O     1 
HETATM 3289 O  O     . HOH G 5 .   ? -8.84371  -10.03859 -9.62088  1.000 37.45897  ? 694 HOH A O     1 
HETATM 3290 O  O     . HOH G 5 .   ? 9.91328   -16.58415 -6.34600  1.000 32.86032  ? 695 HOH A O     1 
HETATM 3291 O  O     . HOH G 5 .   ? -4.83368  -3.39903  -8.07174  1.000 51.51115  ? 696 HOH A O     1 
HETATM 3292 O  O     . HOH G 5 .   ? 1.278     -22.526   -31.212   1.000 30.14662  ? 697 HOH A O     1 
HETATM 3293 O  O     . HOH G 5 .   ? -5.05535  -37.62229 -18.15004 1.000 22.85396  ? 698 HOH A O     1 
HETATM 3294 O  O     . HOH G 5 .   ? 8.69855   -40.50824 4.31367   1.000 27.26766  ? 699 HOH A O     1 
HETATM 3295 O  O     . HOH G 5 .   ? -7.72059  -10.39850 -7.04858  1.000 33.34052  ? 700 HOH A O     1 
HETATM 3296 O  O     . HOH G 5 .   ? 6.98201   -15.42803 -17.55729 1.000 35.86554  ? 701 HOH A O     1 
HETATM 3297 O  O     . HOH G 5 .   ? -3.08899  -43.53150 10.33770  1.000 32.00297  ? 702 HOH A O     1 
HETATM 3298 O  O     . HOH G 5 .   ? 4.57659   -37.37143 -23.88655 1.000 51.59296  ? 703 HOH A O     1 
HETATM 3299 O  O     . HOH G 5 .   ? -22.89125 -20.15837 -11.58577 1.000 40.45997  ? 704 HOH A O     1 
HETATM 3300 O  O     . HOH G 5 .   ? -18.89159 -26.46209 -17.46007 1.000 34.33033  ? 705 HOH A O     1 
HETATM 3301 O  O     . HOH G 5 .   ? 13.71116  -25.03441 -24.93030 1.000 38.80436  ? 706 HOH A O     1 
HETATM 3302 O  O     . HOH G 5 .   ? 10.32073  -35.66275 0.40704   1.000 30.04472  ? 707 HOH A O     1 
HETATM 3303 O  O     . HOH G 5 .   ? -15.64260 -13.52921 -0.29118  1.000 25.55622  ? 708 HOH A O     1 
HETATM 3304 O  O     . HOH G 5 .   ? 7.37857   -31.19448 -2.40442  1.000 27.46818  ? 709 HOH A O     1 
HETATM 3305 O  O     . HOH G 5 .   ? 22.56997  -49.32355 -0.97656  1.000 41.89632  ? 710 HOH A O     1 
HETATM 3306 O  O     . HOH G 5 .   ? 12.00862  -33.54868 -1.82438  1.000 46.92797  ? 711 HOH A O     1 
HETATM 3307 O  O     . HOH G 5 .   ? 9.48279   -50.48784 16.57328  1.000 49.10378  ? 712 HOH A O     1 
HETATM 3308 O  O     . HOH G 5 .   ? -20.53646 -19.78953 -8.38264  1.000 44.71784  ? 713 HOH A O     1 
HETATM 3309 O  O     . HOH G 5 .   ? 15.58297  -18.97383 -3.29151  1.000 43.01799  ? 714 HOH A O     1 
HETATM 3310 O  O     . HOH G 5 .   ? -18.57433 -32.37539 -6.30794  1.000 38.90623  ? 715 HOH A O     1 
HETATM 3311 O  O     . HOH G 5 .   ? -10.19726 -20.07406 6.70089   1.000 35.76057  ? 716 HOH A O     1 
HETATM 3312 O  O     . HOH G 5 .   ? 9.02769   -16.34879 -15.68120 1.000 36.25922  ? 717 HOH A O     1 
HETATM 3313 O  O     . HOH G 5 .   ? -17.10551 -14.57891 -14.42748 1.000 27.00704  ? 718 HOH A O     1 
HETATM 3314 O  O     . HOH G 5 .   ? 16.90271  -49.24228 22.50639  1.000 40.58429  ? 719 HOH A O     1 
HETATM 3315 O  O     . HOH G 5 .   ? 12.27572  -26.27115 -0.45302  1.000 35.92922  ? 720 HOH A O     1 
HETATM 3316 O  O     . HOH G 5 .   ? -11.26448 -42.48232 -15.80555 1.000 39.39437  ? 721 HOH A O     1 
HETATM 3317 O  O     . HOH G 5 .   ? 22.32623  -48.62839 21.80541  1.000 45.54372  ? 722 HOH A O     1 
HETATM 3318 O  O     . HOH G 5 .   ? -14.500   -44.264   -0.949    1.000 32.14841  ? 723 HOH A O     1 
HETATM 3319 O  O     . HOH G 5 .   ? -20.55232 -13.01342 -5.51720  1.000 35.03726  ? 724 HOH A O     1 
HETATM 3320 O  O     . HOH G 5 .   ? 31.17102  -31.46620 7.72508   1.000 41.24605  ? 725 HOH A O     1 
HETATM 3321 O  O     . HOH G 5 .   ? 29.01353  -40.00922 -7.53514  1.000 36.12603  ? 726 HOH A O     1 
HETATM 3322 O  O     . HOH G 5 .   ? 3.36388   -9.56234  1.17065   1.000 49.09420  ? 727 HOH A O     1 
HETATM 3323 O  O     . HOH G 5 .   ? 31.94521  -39.83610 -7.31893  1.000 46.10502  ? 728 HOH A O     1 
HETATM 3324 O  O     . HOH G 5 .   ? -6.83965  -46.32984 -9.08743  1.000 32.55484  ? 729 HOH A O     1 
HETATM 3325 O  O     . HOH G 5 .   ? -17.40352 -36.98601 -20.16396 1.000 47.19182  ? 730 HOH A O     1 
HETATM 3326 O  O     . HOH G 5 .   ? 2.14438   -5.72083  -5.35643  1.000 48.80042  ? 731 HOH A O     1 
HETATM 3327 O  O     . HOH G 5 .   ? -9.366    -19.493   -28.147   1.000 40.92566  ? 732 HOH A O     1 
HETATM 3328 O  O     . HOH G 5 .   ? -8.56682  -13.21507 -10.57148 1.000 26.34534  ? 733 HOH A O     1 
HETATM 3329 O  O     . HOH G 5 .   ? 26.40081  -39.20709 -6.77775  1.000 44.05231  ? 734 HOH A O     1 
HETATM 3330 O  O     . HOH G 5 .   ? -21.65189 -27.33010 -15.13397 1.000 60.93652  ? 735 HOH A O     1 
HETATM 3331 O  O     . HOH G 5 .   ? -9.60418  -41.33006 15.63877  1.000 53.60923  ? 736 HOH A O     1 
HETATM 3332 O  O     . HOH G 5 .   ? 11.33506  -50.39526 18.57823  1.000 56.15598  ? 737 HOH A O     1 
HETATM 3333 O  O     . HOH G 5 .   ? -17.11842 -26.19131 -21.31976 1.000 44.47880  ? 738 HOH A O     1 
HETATM 3334 O  O     . HOH G 5 .   ? 1.63913   -40.77789 -19.94088 1.000 47.81273  ? 739 HOH A O     1 
HETATM 3335 O  O     . HOH G 5 .   ? 34.25455  -43.38125 -6.69505  1.000 45.47926  ? 740 HOH A O     1 
HETATM 3336 O  O     . HOH G 5 .   ? -2.17252  -41.10403 -18.31909 1.000 46.85090  ? 741 HOH A O     1 
HETATM 3337 O  O     . HOH G 5 .   ? -2.74912  -4.76814  -6.48492  1.000 39.53260  ? 742 HOH A O     1 
HETATM 3338 O  O     . HOH G 5 .   ? 10.58562  -45.44162 -3.33378  1.000 42.94005  ? 743 HOH A O     1 
HETATM 3339 O  O     . HOH G 5 .   ? -7.90405  -39.44108 17.05127  1.000 49.08360  ? 744 HOH A O     1 
HETATM 3340 O  O     . HOH G 5 .   ? -20.85600 -37.24740 3.69466   1.000 51.55685  ? 745 HOH A O     1 
HETATM 3341 O  O     . HOH G 5 .   ? 7.40865   -15.70674 -7.83254  1.000 34.15730  ? 746 HOH A O     1 
HETATM 3342 O  O     . HOH G 5 .   ? -0.98222  -40.44314 -20.77305 1.000 52.64179  ? 747 HOH A O     1 
HETATM 3343 O  O     . HOH G 5 .   ? 7.32551   -35.32494 -28.18127 1.000 37.79705  ? 748 HOH A O     1 
HETATM 3344 O  O     . HOH G 5 .   ? 4.31035   -11.92708 -18.53446 1.000 44.39239  ? 749 HOH A O     1 
HETATM 3345 O  O     . HOH G 5 .   ? -5.55264  -12.81650 0.37944   1.000 43.21807  ? 750 HOH A O     1 
HETATM 3346 O  O     . HOH G 5 .   ? 37.790    -30.956   3.377     1.000 52.62279  ? 751 HOH A O     1 
HETATM 3347 O  O     . HOH G 5 .   ? 11.76092  -54.56862 10.71121  1.000 47.80410  ? 752 HOH A O     1 
HETATM 3348 O  O     . HOH G 5 .   ? -10.84300 -43.81680 -10.12549 1.000 43.15926  ? 753 HOH A O     1 
HETATM 3349 O  O     . HOH G 5 .   ? 3.34587   -14.67915 -14.97021 1.000 31.63559  ? 754 HOH A O     1 
HETATM 3350 O  O     . HOH G 5 .   ? 9.07638   -16.57880 7.91007   1.000 40.31866  ? 755 HOH A O     1 
HETATM 3351 O  O     . HOH G 5 .   ? 17.76341  -40.60454 -5.83328  1.000 38.14199  ? 756 HOH A O     1 
HETATM 3352 O  O     . HOH G 5 .   ? 17.60837  -52.73490 17.18767  1.000 38.24246  ? 757 HOH A O     1 
HETATM 3353 O  O     . HOH G 5 .   ? -16.730   -7.833    -24.254   1.000 38.34501  ? 758 HOH A O     1 
HETATM 3354 O  O     . HOH G 5 .   ? -13.75130 -9.91379  -5.99452  1.000 35.50298  ? 759 HOH A O     1 
HETATM 3355 O  O     . HOH G 5 .   ? 2.56713   -9.01717  -14.42623 1.000 33.42154  ? 760 HOH A O     1 
HETATM 3356 O  O     . HOH G 5 .   ? -4.89930  -50.91501 -3.96227  1.000 40.48132  ? 761 HOH A O     1 
HETATM 3357 O  O     . HOH G 5 .   ? 7.71614   -33.57709 -6.05522  1.000 27.77185  ? 762 HOH A O     1 
HETATM 3358 O  O     . HOH G 5 .   ? -5.52410  -8.58964  -26.71259 1.000 40.79371  ? 763 HOH A O     1 
HETATM 3359 O  O     . HOH G 5 .   ? 3.10985   -45.37303 -11.76713 1.000 50.23034  ? 764 HOH A O     1 
HETATM 3360 O  O     . HOH G 5 .   ? -5.28955  -21.85099 -29.04944 1.000 38.08966  ? 765 HOH A O     1 
HETATM 3361 O  O     . HOH G 5 .   ? -8.35956  -27.30833 -24.27081 1.000 40.96788  ? 766 HOH A O     1 
HETATM 3362 O  O     . HOH G 5 .   ? 6.60252   -39.85374 18.80609  1.000 43.98702  ? 767 HOH A O     1 
HETATM 3363 O  O     . HOH G 5 .   ? -0.91144  -50.00444 -7.29856  1.000 49.27790  ? 768 HOH A O     1 
HETATM 3364 O  O     . HOH G 5 .   ? -19.461   -34.649   -17.101   1.000 38.33680  ? 769 HOH A O     1 
HETATM 3365 O  O     . HOH G 5 .   ? -6.563    -14.959   14.122    1.000 44.12310  ? 770 HOH A O     1 
HETATM 3366 O  O     . HOH G 5 .   ? -7.298    -19.875   -30.064   1.000 39.79125  ? 771 HOH A O     1 
HETATM 3367 O  O     . HOH G 5 .   ? 6.40298   -50.60436 -6.73223  1.000 52.70132  ? 772 HOH A O     1 
HETATM 3368 O  O     . HOH G 5 .   ? 35.35847  -36.77822 11.79315  1.000 42.78223  ? 773 HOH A O     1 
HETATM 3369 O  O     . HOH G 5 .   ? 1.92109   -38.29533 -23.04786 1.000 47.87291  ? 774 HOH A O     1 
HETATM 3370 O  O     . HOH G 5 .   ? -14.68948 -42.81988 -9.20543  1.000 35.48424  ? 775 HOH A O     1 
HETATM 3371 O  O     . HOH G 5 .   ? 3.96634   -11.20617 -15.86549 1.000 41.82187  ? 776 HOH A O     1 
HETATM 3372 O  O     . HOH G 5 .   ? -5.37154  -14.15170 9.62605   1.000 40.46000  ? 777 HOH A O     1 
HETATM 3373 O  O     . HOH G 5 .   ? -5.77238  -47.97334 -7.08013  1.000 37.88586  ? 778 HOH A O     1 
HETATM 3374 O  O     . HOH G 5 .   ? -0.03380  -4.33621  -6.36027  1.000 53.25883  ? 779 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   . ASN A 1   ? 0.56452 0.71144 0.65289 0.05119  0.00001  -0.01212 12  ASN A N   
2    C CA  . ASN A 1   ? 0.60938 0.74527 0.68705 0.04928  0.00531  -0.01283 12  ASN A CA  
3    C C   . ASN A 1   ? 0.48680 0.60192 0.54570 0.05176  0.00200  -0.01670 12  ASN A C   
4    O O   . ASN A 1   ? 0.49763 0.60513 0.55137 0.05160  -0.00469 -0.01790 12  ASN A O   
5    C CB  . ASN A 1   ? 0.64224 0.77597 0.72470 0.03802  0.00602  -0.01157 12  ASN A CB  
6    C CG  . ASN A 1   ? 0.76143 0.91311 0.86521 0.03310  0.00605  -0.00678 12  ASN A CG  
7    O OD1 . ASN A 1   ? 0.87627 1.04368 0.99108 0.03531  0.01218  -0.00122 12  ASN A OD1 
8    N ND2 . ASN A 1   ? 0.82481 0.97502 0.93492 0.02647  -0.00139 -0.00843 12  ASN A ND2 
9    N N   . LEU A 2   ? 0.41061 0.51741 0.46027 0.05364  0.00626  -0.01764 13  LEU A N   
10   C CA  . LEU A 2   ? 0.42925 0.51641 0.46375 0.05412  0.00262  -0.01995 13  LEU A CA  
11   C C   . LEU A 2   ? 0.37252 0.45100 0.40238 0.04459  -0.00011 -0.01922 13  LEU A C   
12   O O   . LEU A 2   ? 0.41055 0.47772 0.43165 0.04422  -0.00531 -0.01880 13  LEU A O   
13   C CB  . LEU A 2   ? 0.27333 0.35441 0.30042 0.05709  0.00717  -0.02122 13  LEU A CB  
14   C CG  . LEU A 2   ? 0.37714 0.46299 0.40249 0.06972  0.00833  -0.02380 13  LEU A CG  
15   C CD1 . LEU A 2   ? 0.33567 0.41277 0.35092 0.07258  0.01096  -0.02602 13  LEU A CD1 
16   C CD2 . LEU A 2   ? 0.35376 0.43133 0.37533 0.07727  -0.00009 -0.02661 13  LEU A CD2 
17   N N   . LEU A 3   ? 0.28879 0.37275 0.32442 0.03739  0.00297  -0.01869 14  LEU A N   
18   C CA  . LEU A 3   ? 0.34774 0.42459 0.37742 0.03035  0.00105  -0.01942 14  LEU A CA  
19   C C   . LEU A 3   ? 0.38114 0.46462 0.41656 0.02686  -0.00375 -0.02057 14  LEU A C   
20   O O   . LEU A 3   ? 0.33254 0.41210 0.36229 0.02266  -0.00563 -0.02236 14  LEU A O   
21   C CB  . LEU A 3   ? 0.24677 0.32112 0.27623 0.02579  0.00639  -0.01967 14  LEU A CB  
22   C CG  . LEU A 3   ? 0.31555 0.38012 0.33553 0.02853  0.00914  -0.01923 14  LEU A CG  
23   C CD1 . LEU A 3   ? 0.28662 0.35155 0.30838 0.02604  0.01498  -0.01884 14  LEU A CD1 
24   C CD2 . LEU A 3   ? 0.31425 0.36797 0.32332 0.02649  0.00552  -0.01860 14  LEU A CD2 
25   N N   . SER A 4   ? 0.40089 0.49506 0.44717 0.02926  -0.00632 -0.02003 15  SER A N   
26   C CA  . SER A 4   ? 0.40762 0.50710 0.45908 0.02613  -0.01266 -0.02180 15  SER A CA  
27   C C   . SER A 4   ? 0.39471 0.48680 0.43209 0.02711  -0.01785 -0.02257 15  SER A C   
28   O O   . SER A 4   ? 0.34662 0.43328 0.37648 0.03132  -0.01879 -0.02004 15  SER A O   
29   C CB  . SER A 4   ? 0.40333 0.51669 0.47000 0.02886  -0.01511 -0.02017 15  SER A CB  
30   O OG  . SER A 4   ? 0.34211 0.45442 0.40354 0.03546  -0.01835 -0.01943 15  SER A OG  
31   N N   . ASP A 5   ? 0.36741 0.45930 0.40100 0.02359  -0.02169 -0.02580 16  ASP A N   
32   C CA  . ASP A 5   ? 0.45529 0.54345 0.47412 0.02462  -0.02552 -0.02566 16  ASP A CA  
33   C C   . ASP A 5   ? 0.37509 0.45458 0.38161 0.02444  -0.02091 -0.02203 16  ASP A C   
34   O O   . ASP A 5   ? 0.36129 0.43903 0.35712 0.02563  -0.02333 -0.01825 16  ASP A O   
35   C CB  . ASP A 5   ? 0.43493 0.52677 0.45325 0.02866  -0.03170 -0.02318 16  ASP A CB  
36   C CG  . ASP A 5   ? 0.51042 0.61206 0.54135 0.02858  -0.03759 -0.02651 16  ASP A CG  
37   O OD1 . ASP A 5   ? 0.55522 0.65919 0.58987 0.02514  -0.04022 -0.03156 16  ASP A OD1 
38   O OD2 . ASP A 5   ? 0.57120 0.67793 0.60927 0.03219  -0.04049 -0.02423 16  ASP A OD2 
39   N N   . LYS A 6   ? 0.35109 0.42600 0.35974 0.02270  -0.01475 -0.02205 17  LYS A N   
40   C CA  . LYS A 6   ? 0.30942 0.37648 0.30861 0.02179  -0.01109 -0.01876 17  LYS A CA  
41   C C   . LYS A 6   ? 0.32341 0.38944 0.32248 0.01841  -0.00650 -0.02202 17  LYS A C   
42   O O   . LYS A 6   ? 0.31535 0.38447 0.32335 0.01681  -0.00583 -0.02594 17  LYS A O   
43   C CB  . LYS A 6   ? 0.29521 0.35549 0.29597 0.02455  -0.00959 -0.01566 17  LYS A CB  
44   C CG  . LYS A 6   ? 0.36037 0.41930 0.36060 0.02882  -0.01543 -0.01256 17  LYS A CG  
45   C CD  . LYS A 6   ? 0.40413 0.45453 0.40513 0.03348  -0.01606 -0.01133 17  LYS A CD  
46   C CE  . LYS A 6   ? 0.33273 0.38065 0.33360 0.03821  -0.02350 -0.00858 17  LYS A CE  
47   N NZ  . LYS A 6   ? 0.41773 0.45475 0.41824 0.04416  -0.02676 -0.00848 17  LYS A NZ  
48   N N   . ASN A 7   ? 0.26786 0.32997 0.25816 0.01713  -0.00391 -0.01960 18  ASN A N   
49   C CA  . ASN A 7   ? 0.29795 0.35896 0.28792 0.01482  0.00020  -0.02273 18  ASN A CA  
50   C C   . ASN A 7   ? 0.24975 0.30393 0.23748 0.01372  0.00446  -0.01882 18  ASN A C   
51   O O   . ASN A 7   ? 0.26746 0.31741 0.25179 0.01431  0.00313  -0.01351 18  ASN A O   
52   C CB  . ASN A 7   ? 0.32046 0.38670 0.30214 0.01535  -0.00117 -0.02554 18  ASN A CB  
53   C CG  . ASN A 7   ? 0.35179 0.42087 0.32288 0.01607  -0.00073 -0.01874 18  ASN A CG  
54   O OD1 . ASN A 7   ? 0.41666 0.48741 0.38506 0.01713  -0.00416 -0.01384 18  ASN A OD1 
55   N ND2 . ASN A 7   ? 0.33128 0.40222 0.29735 0.01546  0.00318  -0.01752 18  ASN A ND2 
56   N N   . VAL A 8   ? 0.20266 0.25487 0.19332 0.01206  0.00838  -0.02148 19  VAL A N   
57   C CA  . VAL A 8   ? 0.20905 0.25497 0.19853 0.01118  0.01198  -0.01889 19  VAL A CA  
58   C C   . VAL A 8   ? 0.20765 0.25485 0.19246 0.00949  0.01433  -0.01924 19  VAL A C   
59   O O   . VAL A 8   ? 0.22604 0.27697 0.21144 0.00962  0.01439  -0.02414 19  VAL A O   
60   C CB  . VAL A 8   ? 0.24991 0.29410 0.24686 0.01154  0.01494  -0.02065 19  VAL A CB  
61   C CG1 . VAL A 8   ? 0.16829 0.20578 0.16240 0.01155  0.01783  -0.01868 19  VAL A CG1 
62   C CG2 . VAL A 8   ? 0.20764 0.25458 0.20979 0.01464  0.01330  -0.02023 19  VAL A CG2 
63   N N   . ALA A 9   ? 0.20342 0.24771 0.18442 0.00835  0.01538  -0.01423 20  ALA A N   
64   C CA  . ALA A 9   ? 0.20240 0.24952 0.18069 0.00716  0.01839  -0.01370 20  ALA A CA  
65   C C   . ALA A 9   ? 0.21597 0.25574 0.19717 0.00584  0.02065  -0.01298 20  ALA A C   
66   O O   . ALA A 9   ? 0.25508 0.28836 0.23639 0.00530  0.01876  -0.00907 20  ALA A O   
67   C CB  . ALA A 9   ? 0.18561 0.23928 0.15856 0.00639  0.01764  -0.00660 20  ALA A CB  
68   N N   . ILE A 10  ? 0.21019 0.25006 0.19364 0.00584  0.02354  -0.01715 21  ILE A N   
69   C CA  . ILE A 10  ? 0.22134 0.25567 0.20656 0.00492  0.02573  -0.01633 21  ILE A CA  
70   C C   . ILE A 10  ? 0.21899 0.25773 0.20212 0.00406  0.02735  -0.01418 21  ILE A C   
71   O O   . ILE A 10  ? 0.18992 0.23531 0.17183 0.00566  0.02863  -0.01755 21  ILE A O   
72   C CB  . ILE A 10  ? 0.22497 0.25709 0.21534 0.00530  0.02763  -0.02054 21  ILE A CB  
73   C CG1 . ILE A 10  ? 0.20749 0.23911 0.20173 0.00630  0.02683  -0.02083 21  ILE A CG1 
74   C CG2 . ILE A 10  ? 0.15063 0.17804 0.14156 0.00483  0.02987  -0.01928 21  ILE A CG2 
75   C CD1 . ILE A 10  ? 0.17499 0.20748 0.17683 0.00556  0.02836  -0.02246 21  ILE A CD1 
76   N N   . ILE A 11  ? 0.20909 0.24462 0.19234 0.00217  0.02662  -0.00894 22  ILE A N   
77   C CA  . ILE A 11  ? 0.18113 0.22311 0.16470 0.00087  0.02811  -0.00502 22  ILE A CA  
78   C C   . ILE A 11  ? 0.25278 0.29087 0.23886 0.00128  0.03019  -0.00803 22  ILE A C   
79   O O   . ILE A 11  ? 0.20984 0.23955 0.19714 0.00029  0.02859  -0.00688 22  ILE A O   
80   C CB  . ILE A 11  ? 0.20353 0.24477 0.18858 -0.00260 0.02458  0.00389  22  ILE A CB  
81   C CG1 . ILE A 11  ? 0.19144 0.23363 0.17442 -0.00294 0.02138  0.00741  22  ILE A CG1 
82   C CG2 . ILE A 11  ? 0.18910 0.24252 0.17645 -0.00420 0.02683  0.00990  22  ILE A CG2 
83   C CD1 . ILE A 11  ? 0.16890 0.22383 0.14760 -0.00054 0.02397  0.00615  22  ILE A CD1 
84   N N   . GLY A 12  ? 0.20271 0.24651 0.18900 0.00356  0.03293  -0.01230 23  GLY A N   
85   C CA  . GLY A 12  ? 0.20742 0.24770 0.19657 0.00421  0.03440  -0.01458 23  GLY A CA  
86   C C   . GLY A 12  ? 0.18740 0.22188 0.17858 0.00573  0.03456  -0.02071 23  GLY A C   
87   O O   . GLY A 12  ? 0.18850 0.21760 0.18068 0.00484  0.03372  -0.02097 23  GLY A O   
88   N N   . GLY A 13  ? 0.24009 0.27632 0.23298 0.00826  0.03511  -0.02514 24  GLY A N   
89   C CA  . GLY A 13  ? 0.25187 0.28136 0.24928 0.00876  0.03371  -0.02963 24  GLY A CA  
90   C C   . GLY A 13  ? 0.24299 0.26651 0.24413 0.00827  0.03442  -0.02812 24  GLY A C   
91   O O   . GLY A 13  ? 0.21324 0.23390 0.21817 0.01017  0.03293  -0.03187 24  GLY A O   
92   N N   . GLY A 14  ? 0.21265 0.23359 0.21244 0.00640  0.03567  -0.02303 25  GLY A N   
93   C CA  . GLY A 14  ? 0.22170 0.23715 0.22385 0.00623  0.03607  -0.02100 25  GLY A CA  
94   C C   . GLY A 14  ? 0.22396 0.23554 0.23002 0.00505  0.03609  -0.01971 25  GLY A C   
95   O O   . GLY A 14  ? 0.23554 0.24855 0.24394 0.00417  0.03531  -0.02111 25  GLY A O   
96   N N   . PRO A 15  ? 0.24517 0.25338 0.25272 0.00497  0.03689  -0.01605 26  PRO A N   
97   C CA  . PRO A 15  ? 0.16820 0.17635 0.18077 0.00362  0.03768  -0.01220 26  PRO A CA  
98   C C   . PRO A 15  ? 0.26152 0.27398 0.27073 0.00415  0.03933  -0.01060 26  PRO A C   
99   O O   . PRO A 15  ? 0.21695 0.23294 0.23225 0.00280  0.03975  -0.00851 26  PRO A O   
100  C CB  . PRO A 15  ? 0.21171 0.21759 0.22404 0.00438  0.03872  -0.00729 26  PRO A CB  
101  C CG  . PRO A 15  ? 0.19228 0.19679 0.19710 0.00642  0.03834  -0.00900 26  PRO A CG  
102  C CD  . PRO A 15  ? 0.20012 0.20619 0.20540 0.00616  0.03699  -0.01421 26  PRO A CD  
103  N N   . VAL A 16  ? 0.19340 0.20561 0.19429 0.00620  0.03937  -0.01145 27  VAL A N   
104  C CA  . VAL A 16  ? 0.20912 0.22407 0.20635 0.00822  0.03983  -0.01097 27  VAL A CA  
105  C C   . VAL A 16  ? 0.24199 0.25935 0.24158 0.00673  0.03848  -0.01367 27  VAL A C   
106  O O   . VAL A 16  ? 0.20980 0.23156 0.21257 0.00717  0.03913  -0.01280 27  VAL A O   
107  C CB  . VAL A 16  ? 0.18432 0.19537 0.17258 0.01127  0.03792  -0.01165 27  VAL A CB  
108  C CG1 . VAL A 16  ? 0.23024 0.24256 0.21453 0.01470  0.03695  -0.01265 27  VAL A CG1 
109  C CG2 . VAL A 16  ? 0.21708 0.22658 0.20161 0.01392  0.03868  -0.00941 27  VAL A CG2 
110  N N   . GLY A 17  ? 0.20462 0.22098 0.20280 0.00542  0.03667  -0.01640 28  GLY A N   
111  C CA  . GLY A 17  ? 0.20309 0.22273 0.20189 0.00472  0.03515  -0.01871 28  GLY A CA  
112  C C   . GLY A 17  ? 0.22984 0.25159 0.23609 0.00341  0.03434  -0.02079 28  GLY A C   
113  O O   . GLY A 17  ? 0.22416 0.24913 0.23264 0.00317  0.03301  -0.02157 28  GLY A O   
114  N N   . LEU A 18  ? 0.19792 0.21706 0.20916 0.00252  0.03393  -0.02167 29  LEU A N   
115  C CA  . LEU A 18  ? 0.20314 0.22178 0.22342 0.00079  0.03082  -0.02372 29  LEU A CA  
116  C C   . LEU A 18  ? 0.20049 0.22244 0.22877 -0.00134 0.03181  -0.01822 29  LEU A C   
117  O O   . LEU A 18  ? 0.17508 0.19965 0.21089 -0.00320 0.02885  -0.01888 29  LEU A O   
118  C CB  . LEU A 18  ? 0.24114 0.25421 0.26573 0.00079  0.02863  -0.02587 29  LEU A CB  
119  C CG  . LEU A 18  ? 0.27601 0.28874 0.29455 0.00432  0.02738  -0.03216 29  LEU A CG  
120  C CD1 . LEU A 18  ? 0.18058 0.18677 0.20480 0.00550  0.02409  -0.03505 29  LEU A CD1 
121  C CD2 . LEU A 18  ? 0.19325 0.21033 0.20804 0.00639  0.02464  -0.03808 29  LEU A CD2 
122  N N   . THR A 19  ? 0.22597 0.24960 0.25264 -0.00051 0.03583  -0.01251 30  THR A N   
123  C CA  . THR A 19  ? 0.20756 0.23867 0.24110 -0.00113 0.03808  -0.00615 30  THR A CA  
124  C C   . THR A 19  ? 0.23491 0.27199 0.26583 0.00106  0.03848  -0.00739 30  THR A C   
125  O O   . THR A 19  ? 0.24470 0.28888 0.28521 -0.00057 0.03781  -0.00476 30  THR A O   
126  C CB  . THR A 19  ? 0.23549 0.26878 0.26511 0.00126  0.04243  -0.00036 30  THR A CB  
127  O OG1 . THR A 19  ? 0.23347 0.26162 0.26795 -0.00128 0.04138  0.00208  30  THR A OG1 
128  C CG2 . THR A 19  ? 0.19885 0.24437 0.23370 0.00264  0.04612  0.00684  30  THR A CG2 
129  N N   . MET A 20  ? 0.24759 0.28173 0.26706 0.00444  0.03864  -0.01087 31  MET A N   
130  C CA  . MET A 20  ? 0.25452 0.29203 0.27113 0.00684  0.03762  -0.01246 31  MET A CA  
131  C C   . MET A 20  ? 0.19944 0.23927 0.22281 0.00398  0.03404  -0.01500 31  MET A C   
132  O O   . MET A 20  ? 0.24201 0.28868 0.27085 0.00456  0.03349  -0.01371 31  MET A O   
133  C CB  . MET A 20  ? 0.21621 0.24737 0.22153 0.00920  0.03608  -0.01524 31  MET A CB  
134  C CG  . MET A 20  ? 0.17037 0.20286 0.17233 0.01236  0.03399  -0.01617 31  MET A CG  
135  S SD  . MET A 20  ? 0.23375 0.27038 0.23307 0.01949  0.03607  -0.01461 31  MET A SD  
136  C CE  . MET A 20  ? 0.22299 0.26802 0.22803 0.02169  0.03477  -0.01481 31  MET A CE  
137  N N   . ALA A 21  ? 0.22710 0.26211 0.24990 0.00180  0.03116  -0.01911 32  ALA A N   
138  C CA  . ALA A 21  ? 0.19980 0.23621 0.22715 0.00028  0.02640  -0.02316 32  ALA A CA  
139  C C   . ALA A 21  ? 0.23539 0.27554 0.27745 -0.00306 0.02421  -0.02054 32  ALA A C   
140  O O   . ALA A 21  ? 0.21312 0.25795 0.26097 -0.00384 0.02077  -0.02142 32  ALA A O   
141  C CB  . ALA A 21  ? 0.15188 0.18339 0.17505 0.00054  0.02371  -0.02886 32  ALA A CB  
142  N N   . LYS A 22  ? 0.22288 0.26141 0.27245 -0.00553 0.02540  -0.01643 33  LYS A N   
143  C CA  . LYS A 22  ? 0.17265 0.21500 0.23915 -0.01012 0.02228  -0.01186 33  LYS A CA  
144  C C   . LYS A 22  ? 0.19523 0.25054 0.26809 -0.00968 0.02584  -0.00498 33  LYS A C   
145  O O   . LYS A 22  ? 0.21327 0.27473 0.29882 -0.01266 0.02189  -0.00328 33  LYS A O   
146  C CB  . LYS A 22  ? 0.21242 0.25044 0.28575 -0.01298 0.02276  -0.00691 33  LYS A CB  
147  C CG  . LYS A 22  ? 0.18600 0.22969 0.27921 -0.01882 0.02030  0.00206  33  LYS A CG  
148  C CD  . LYS A 22  ? 0.28406 0.32228 0.38956 -0.02297 0.00986  -0.00277 33  LYS A CD  
149  C CE  . LYS A 22  ? 0.26883 0.31399 0.39769 -0.03024 0.00649  0.00848  33  LYS A CE  
150  N NZ  . LYS A 22  ? 0.38491 0.42575 0.52633 -0.03410 -0.00490 0.00344  33  LYS A NZ  
151  N N   . LEU A 23  ? 0.22383 0.28394 0.28811 -0.00519 0.03263  -0.00152 34  LEU A N   
152  C CA  . LEU A 23  ? 0.21297 0.28722 0.28208 -0.00245 0.03651  0.00435  34  LEU A CA  
153  C C   . LEU A 23  ? 0.22588 0.30314 0.29346 -0.00018 0.03359  -0.00019 34  LEU A C   
154  O O   . LEU A 23  ? 0.21673 0.30667 0.29502 0.00005  0.03399  0.00422  34  LEU A O   
155  C CB  . LEU A 23  ? 0.18935 0.26655 0.24687 0.00402  0.04305  0.00672  34  LEU A CB  
156  C CG  . LEU A 23  ? 0.24097 0.31800 0.30016 0.00245  0.04634  0.01288  34  LEU A CG  
157  C CD1 . LEU A 23  ? 0.21395 0.29263 0.25874 0.01018  0.05138  0.01309  34  LEU A CD1 
158  C CD2 . LEU A 23  ? 0.23329 0.32362 0.31133 -0.00228 0.04760  0.02394  34  LEU A CD2 
159  N N   . LEU A 24  ? 0.21666 0.28403 0.27192 0.00154  0.03065  -0.00784 35  LEU A N   
160  C CA  . LEU A 24  ? 0.22909 0.29887 0.28303 0.00333  0.02699  -0.01135 35  LEU A CA  
161  C C   . LEU A 24  ? 0.25820 0.32908 0.32359 -0.00161 0.02039  -0.01339 35  LEU A C   
162  O O   . LEU A 24  ? 0.22576 0.30513 0.29983 -0.00172 0.01771  -0.01220 35  LEU A O   
163  C CB  . LEU A 24  ? 0.16038 0.22080 0.19857 0.00614  0.02565  -0.01666 35  LEU A CB  
164  C CG  . LEU A 24  ? 0.27253 0.32913 0.29932 0.01112  0.02882  -0.01602 35  LEU A CG  
165  C CD1 . LEU A 24  ? 0.18235 0.23052 0.19793 0.01146  0.02584  -0.01917 35  LEU A CD1 
166  C CD2 . LEU A 24  ? 0.21205 0.27660 0.24062 0.01674  0.03004  -0.01405 35  LEU A CD2 
167  N N   . GLN A 25  ? 0.21896 0.28101 0.28457 -0.00501 0.01676  -0.01717 36  GLN A N   
168  C CA  . GLN A 25  ? 0.25106 0.31114 0.32486 -0.00825 0.00824  -0.02181 36  GLN A CA  
169  C C   . GLN A 25  ? 0.28746 0.35601 0.38229 -0.01325 0.00528  -0.01546 36  GLN A C   
170  O O   . GLN A 25  ? 0.26271 0.33431 0.36612 -0.01505 -0.00187 -0.01777 36  GLN A O   
171  C CB  . GLN A 25  ? 0.23275 0.28151 0.30299 -0.00927 0.00442  -0.02778 36  GLN A CB  
172  C CG  . GLN A 25  ? 0.23435 0.27906 0.30832 -0.00999 -0.00606 -0.03591 36  GLN A CG  
173  C CD  . GLN A 25  ? 0.27832 0.31302 0.34302 -0.00727 -0.00916 -0.04417 36  GLN A CD  
174  O OE1 . GLN A 25  ? 0.28712 0.31483 0.35906 -0.00955 -0.01122 -0.04393 36  GLN A OE1 
175  N NE2 . GLN A 25  ? 0.26888 0.30408 0.31741 -0.00178 -0.00921 -0.05073 36  GLN A NE2 
176  N N   . GLN A 26  ? 0.24136 0.31489 0.34548 -0.01572 0.01028  -0.00656 37  GLN A N   
177  C CA  . GLN A 26  ? 0.31821 0.40214 0.44504 -0.02155 0.00763  0.00222  37  GLN A CA  
178  C C   . GLN A 26  ? 0.27275 0.37363 0.40611 -0.01924 0.01045  0.00714  37  GLN A C   
179  O O   . GLN A 26  ? 0.26973 0.38199 0.42395 -0.02430 0.00727  0.01459  37  GLN A O   
180  C CB  . GLN A 26  ? 0.29108 0.37802 0.42596 -0.02465 0.01270  0.01243  37  GLN A CB  
181  C CG  . GLN A 26  ? 0.28262 0.38251 0.41070 -0.01912 0.02397  0.01967  37  GLN A CG  
182  C CD  . GLN A 26  ? 0.26946 0.37208 0.40263 -0.02144 0.02873  0.02952  37  GLN A CD  
183  O OE1 . GLN A 26  ? 0.33155 0.42274 0.47040 -0.02677 0.02377  0.02966  37  GLN A OE1 
184  N NE2 . GLN A 26  ? 0.30883 0.42705 0.43979 -0.01661 0.03785  0.03776  37  GLN A NE2 
185  N N   . ASN A 27  ? 0.26530 0.36821 0.38281 -0.01176 0.01547  0.00357  38  ASN A N   
186  C CA  . ASN A 27  ? 0.21957 0.33639 0.34144 -0.00791 0.01644  0.00568  38  ASN A CA  
187  C C   . ASN A 27  ? 0.31716 0.42823 0.43347 -0.00681 0.00885  -0.00290 38  ASN A C   
188  O O   . ASN A 27  ? 0.28298 0.40115 0.39608 -0.00156 0.00973  -0.00339 38  ASN A O   
189  C CB  . ASN A 27  ? 0.21550 0.33795 0.32446 0.00088  0.02518  0.00715  38  ASN A CB  
190  C CG  . ASN A 27  ? 0.31037 0.44418 0.42499 0.00176  0.03312  0.01665  38  ASN A CG  
191  O OD1 . ASN A 27  ? 0.44759 0.57524 0.54877 0.00551  0.03805  0.01578  38  ASN A OD1 
192  N ND2 . ASN A 27  ? 0.34200 0.49356 0.47704 -0.00177 0.03403  0.02652  38  ASN A ND2 
193  N N   . GLY A 28  ? 0.22995 0.32850 0.34376 -0.01047 0.00118  -0.00998 39  GLY A N   
194  C CA  . GLY A 28  ? 0.27738 0.37296 0.38621 -0.00900 -0.00656 -0.01746 39  GLY A CA  
195  C C   . GLY A 28  ? 0.31032 0.39889 0.39697 -0.00287 -0.00431 -0.02298 39  GLY A C   
196  O O   . GLY A 28  ? 0.37769 0.46743 0.45941 -0.00036 -0.00909 -0.02663 39  GLY A O   
197  N N   . ILE A 29  ? 0.29179 0.37342 0.36581 -0.00079 0.00206  -0.02285 40  ILE A N   
198  C CA  . ILE A 29  ? 0.25725 0.33323 0.31310 0.00396  0.00391  -0.02559 40  ILE A CA  
199  C C   . ILE A 29  ? 0.26908 0.33661 0.31429 0.00343  0.00058  -0.03179 40  ILE A C   
200  O O   . ILE A 29  ? 0.27498 0.33737 0.32204 0.00099  0.00056  -0.03377 40  ILE A O   
201  C CB  . ILE A 29  ? 0.21704 0.29104 0.26606 0.00695  0.01152  -0.02176 40  ILE A CB  
202  C CG1 . ILE A 29  ? 0.30413 0.38847 0.36020 0.01071  0.01411  -0.01730 40  ILE A CG1 
203  C CG2 . ILE A 29  ? 0.18339 0.24939 0.21602 0.01001  0.01189  -0.02359 40  ILE A CG2 
204  C CD1 . ILE A 29  ? 0.34134 0.42474 0.39162 0.01475  0.02035  -0.01471 40  ILE A CD1 
205  N N   . ASP A 30  ? 0.23535 0.30273 0.26966 0.00641  -0.00247 -0.03447 41  ASP A N   
206  C CA  . ASP A 30  ? 0.26908 0.33252 0.29054 0.00797  -0.00426 -0.03922 41  ASP A CA  
207  C C   . ASP A 30  ? 0.28167 0.34057 0.29370 0.00862  0.00240  -0.03617 41  ASP A C   
208  O O   . ASP A 30  ? 0.23101 0.28959 0.23669 0.01019  0.00481  -0.03164 41  ASP A O   
209  C CB  . ASP A 30  ? 0.22315 0.29093 0.23645 0.01114  -0.00885 -0.04029 41  ASP A CB  
210  C CG  . ASP A 30  ? 0.36503 0.43328 0.36412 0.01417  -0.01058 -0.04454 41  ASP A CG  
211  O OD1 . ASP A 30  ? 0.26027 0.32541 0.25599 0.01434  -0.00838 -0.04754 41  ASP A OD1 
212  O OD2 . ASP A 30  ? 0.39667 0.46990 0.38765 0.01716  -0.01409 -0.04443 41  ASP A OD2 
213  N N   . VAL A 31  ? 0.25923 0.31391 0.27158 0.00735  0.00431  -0.03846 42  VAL A N   
214  C CA  . VAL A 31  ? 0.23733 0.28822 0.24331 0.00746  0.01014  -0.03538 42  VAL A CA  
215  C C   . VAL A 31  ? 0.28217 0.33197 0.28215 0.00882  0.00972  -0.04018 42  VAL A C   
216  O O   . VAL A 31  ? 0.29632 0.34427 0.30101 0.00890  0.00557  -0.04622 42  VAL A O   
217  C CB  . VAL A 31  ? 0.29607 0.34402 0.31016 0.00536  0.01438  -0.03166 42  VAL A CB  
218  C CG1 . VAL A 31  ? 0.22205 0.26916 0.24827 0.00241  0.01217  -0.03365 42  VAL A CG1 
219  C CG2 . VAL A 31  ? 0.18330 0.22672 0.19057 0.00569  0.01904  -0.02929 42  VAL A CG2 
220  N N   . SER A 32  ? 0.23183 0.28317 0.22229 0.01027  0.01323  -0.03738 43  SER A N   
221  C CA  . SER A 32  ? 0.23689 0.28990 0.22176 0.01265  0.01443  -0.04076 43  SER A CA  
222  C C   . SER A 32  ? 0.27765 0.32771 0.26248 0.01091  0.01973  -0.03571 43  SER A C   
223  O O   . SER A 32  ? 0.21532 0.26353 0.19994 0.00890  0.02170  -0.02932 43  SER A O   
224  C CB  . SER A 32  ? 0.26473 0.32753 0.23827 0.01679  0.01372  -0.04097 43  SER A CB  
225  O OG  . SER A 32  ? 0.35450 0.42032 0.32591 0.01991  0.00782  -0.04760 43  SER A OG  
226  N N   . VAL A 33  ? 0.21810 0.26706 0.20320 0.01230  0.02089  -0.03920 44  VAL A N   
227  C CA  . VAL A 33  ? 0.17567 0.22306 0.16064 0.01118  0.02520  -0.03499 44  VAL A CA  
228  C C   . VAL A 33  ? 0.23748 0.29447 0.21550 0.01494  0.02693  -0.03535 44  VAL A C   
229  O O   . VAL A 33  ? 0.27084 0.33111 0.24638 0.01970  0.02507  -0.04270 44  VAL A O   
230  C CB  . VAL A 33  ? 0.21095 0.25046 0.20322 0.01000  0.02542  -0.03740 44  VAL A CB  
231  C CG1 . VAL A 33  ? 0.19565 0.23441 0.18690 0.00954  0.02920  -0.03349 44  VAL A CG1 
232  C CG2 . VAL A 33  ? 0.15592 0.19006 0.15586 0.00670  0.02472  -0.03524 44  VAL A CG2 
233  N N   . TYR A 34  ? 0.25161 0.31376 0.22715 0.01332  0.02986  -0.02738 45  TYR A N   
234  C CA  . TYR A 34  ? 0.22014 0.29527 0.19115 0.01650  0.03264  -0.02502 45  TYR A CA  
235  C C   . TYR A 34  ? 0.18253 0.25573 0.15813 0.01544  0.03531  -0.02317 45  TYR A C   
236  O O   . TYR A 34  ? 0.20319 0.27014 0.18281 0.01066  0.03557  -0.01707 45  TYR A O   
237  C CB  . TYR A 34  ? 0.19311 0.27777 0.16077 0.01455  0.03332  -0.01504 45  TYR A CB  
238  C CG  . TYR A 34  ? 0.21847 0.30536 0.18107 0.01611  0.03025  -0.01663 45  TYR A CG  
239  C CD1 . TYR A 34  ? 0.21695 0.31560 0.17158 0.02259  0.02981  -0.02170 45  TYR A CD1 
240  C CD2 . TYR A 34  ? 0.20182 0.27940 0.16712 0.01231  0.02724  -0.01400 45  TYR A CD2 
241  C CE1 . TYR A 34  ? 0.27431 0.37516 0.22386 0.02436  0.02618  -0.02346 45  TYR A CE1 
242  C CE2 . TYR A 34  ? 0.26854 0.34853 0.23000 0.01395  0.02396  -0.01539 45  TYR A CE2 
243  C CZ  . TYR A 34  ? 0.29435 0.38577 0.24802 0.01952  0.02330  -0.01985 45  TYR A CZ  
244  O OH  . TYR A 34  ? 0.26926 0.36326 0.21869 0.02145  0.01929  -0.02149 45  TYR A OH  
245  N N   . GLU A 35  ? 0.19554 0.27356 0.17026 0.02071  0.03635  -0.02917 46  GLU A N   
246  C CA  . GLU A 35  ? 0.24858 0.32419 0.22821 0.02060  0.03818  -0.02872 46  GLU A CA  
247  C C   . GLU A 35  ? 0.23167 0.32490 0.20900 0.02568  0.04166  -0.02672 46  GLU A C   
248  O O   . GLU A 35  ? 0.21827 0.32187 0.18939 0.03316  0.04178  -0.03272 46  GLU A O   
249  C CB  . GLU A 35  ? 0.24856 0.31200 0.23176 0.02259  0.03535  -0.03772 46  GLU A CB  
250  C CG  . GLU A 35  ? 0.23092 0.29418 0.21768 0.02543  0.03647  -0.03952 46  GLU A CG  
251  C CD  . GLU A 35  ? 0.21902 0.27920 0.21018 0.02001  0.03861  -0.03120 46  GLU A CD  
252  O OE1 . GLU A 35  ? 0.20037 0.25022 0.19341 0.01485  0.03758  -0.02812 46  GLU A OE1 
253  O OE2 . GLU A 35  ? 0.23885 0.30798 0.23157 0.02151  0.04091  -0.02786 46  GLU A OE2 
254  N N   A ARG A 36  ? 0.23591 0.33359 0.21840 0.02231  0.04406  -0.01846 47  ARG A N   
255  N N   B ARG A 36  ? 0.22417 0.32188 0.20666 0.02234  0.04407  -0.01848 47  ARG A N   
256  C CA  A ARG A 36  ? 0.25731 0.37569 0.23993 0.02644  0.04805  -0.01379 47  ARG A CA  
257  C CA  B ARG A 36  ? 0.25769 0.37624 0.24020 0.02652  0.04806  -0.01384 47  ARG A CA  
258  C C   A ARG A 36  ? 0.23998 0.36270 0.22141 0.03562  0.04889  -0.02365 47  ARG A C   
259  C C   B ARG A 36  ? 0.23512 0.35792 0.21663 0.03560  0.04892  -0.02357 47  ARG A C   
260  O O   A ARG A 36  ? 0.26467 0.40738 0.24247 0.04320  0.05219  -0.02386 47  ARG A O   
261  O O   B ARG A 36  ? 0.26532 0.40816 0.24336 0.04314  0.05226  -0.02368 47  ARG A O   
262  C CB  A ARG A 36  ? 0.25509 0.37662 0.24632 0.01962  0.04892  -0.00198 47  ARG A CB  
263  C CB  B ARG A 36  ? 0.25450 0.37691 0.24550 0.01962  0.04901  -0.00159 47  ARG A CB  
264  C CG  A ARG A 36  ? 0.26576 0.37465 0.26296 0.01803  0.04744  -0.00479 47  ARG A CG  
265  C CG  B ARG A 36  ? 0.26561 0.37651 0.26316 0.01767  0.04767  -0.00339 47  ARG A CG  
266  C CD  A ARG A 36  ? 0.26182 0.37628 0.26783 0.01242  0.04719  0.00613  47  ARG A CD  
267  C CD  B ARG A 36  ? 0.26431 0.37724 0.27031 0.01024  0.04637  0.00842  47  ARG A CD  
268  N NE  A ARG A 36  ? 0.26458 0.36471 0.27475 0.01061  0.04464  0.00340  47  ARG A NE  
269  N NE  B ARG A 36  ? 0.28131 0.41720 0.29314 0.01169  0.04981  0.01662  47  ARG A NE  
270  C CZ  A ARG A 36  ? 0.30041 0.39661 0.31731 0.00473  0.04153  0.01050  47  ARG A CZ  
271  C CZ  B ARG A 36  ? 0.35023 0.49356 0.37156 0.00477  0.04826  0.02946  47  ARG A CZ  
272  N NH1 A ARG A 36  ? 0.22918 0.33348 0.25161 -0.00092 0.03981  0.02140  47  ARG A NH1 
273  N NH1 B ARG A 36  ? 0.25834 0.38597 0.28316 -0.00340 0.04227  0.03434  47  ARG A NH1 
274  N NH2 A ARG A 36  ? 0.27531 0.35873 0.29375 0.00446  0.03911  0.00697  47  ARG A NH2 
275  N NH2 B ARG A 36  ? 0.33359 0.50134 0.36181 0.00652  0.05213  0.03774  47  ARG A NH2 
276  N N   . ASP A 37  ? 0.27678 0.38208 0.26135 0.03572  0.04574  -0.03131 48  ASP A N   
277  C CA  . ASP A 37  ? 0.27110 0.37691 0.25549 0.04466  0.04463  -0.04130 48  ASP A CA  
278  C C   . ASP A 37  ? 0.28002 0.39487 0.25535 0.05472  0.04331  -0.05095 48  ASP A C   
279  O O   . ASP A 37  ? 0.30270 0.41201 0.27321 0.05366  0.04035  -0.05424 48  ASP A O   
280  C CB  . ASP A 37  ? 0.29620 0.37949 0.28543 0.04230  0.03979  -0.04737 48  ASP A CB  
281  C CG  . ASP A 37  ? 0.33581 0.41149 0.33226 0.03585  0.04067  -0.04024 48  ASP A CG  
282  O OD1 . ASP A 37  ? 0.34575 0.43312 0.34491 0.03478  0.04398  -0.03290 48  ASP A OD1 
283  O OD2 . ASP A 37  ? 0.36538 0.42416 0.36520 0.03195  0.03761  -0.04157 48  ASP A OD2 
284  N N   . ASN A 38  ? 0.26701 0.39619 0.23977 0.06551  0.04494  -0.05620 49  ASN A N   
285  C CA  . ASN A 38  ? 0.44137 0.58214 0.40329 0.07774  0.04354  -0.06636 49  ASN A CA  
286  C C   . ASN A 38  ? 0.43154 0.55126 0.39113 0.08096  0.03434  -0.08081 49  ASN A C   
287  O O   . ASN A 38  ? 0.49895 0.62258 0.44922 0.08689  0.03117  -0.08793 49  ASN A O   
288  C CB  . ASN A 38  ? 0.41814 0.57557 0.37897 0.08833  0.04556  -0.06819 49  ASN A CB  
289  C CG  . ASN A 38  ? 0.62092 0.78677 0.57086 0.09878  0.04161  -0.07530 49  ASN A CG  
290  O OD1 . ASN A 38  ? 0.66744 0.85251 0.61201 0.09964  0.04532  -0.06704 49  ASN A OD1 
291  N ND2 . ASN A 38  ? 0.71793 0.86927 0.66517 0.10686  0.03314  -0.09035 49  ASN A ND2 
292  N N   . ASP A 39  ? 0.48583 0.58390 0.45429 0.07716  0.02922  -0.08467 50  ASP A N   
293  C CA  . ASP A 39  ? 0.48366 0.56106 0.45369 0.07789  0.01934  -0.09578 50  ASP A CA  
294  C C   . ASP A 39  ? 0.42761 0.48397 0.41015 0.06901  0.01621  -0.09244 50  ASP A C   
295  O O   . ASP A 39  ? 0.44768 0.50535 0.43551 0.06466  0.02112  -0.08408 50  ASP A O   
296  C CB  . ASP A 39  ? 0.56326 0.64169 0.52690 0.09319  0.01239  -0.11212 50  ASP A CB  
297  C CG  . ASP A 39  ? 0.53665 0.61647 0.50417 0.10085  0.01264  -0.11567 50  ASP A CG  
298  O OD1 . ASP A 39  ? 0.53635 0.60018 0.51491 0.09432  0.01059  -0.11234 50  ASP A OD1 
299  O OD2 . ASP A 39  ? 0.70481 0.79986 0.66591 0.10976  0.01357  -0.11665 50  ASP A OD2 
300  N N   . ARG A 40  ? 0.48014 0.51789 0.46791 0.06669  0.00726  -0.09876 51  ARG A N   
301  C CA  . ARG A 40  ? 0.46623 0.48633 0.46630 0.05675  0.00482  -0.09263 51  ARG A CA  
302  C C   . ARG A 40  ? 0.52041 0.53209 0.52712 0.06013  0.00208  -0.09462 51  ARG A C   
303  O O   . ARG A 40  ? 0.58665 0.58732 0.60253 0.05210  0.00196  -0.08687 51  ARG A O   
304  C CB  . ARG A 40  ? 0.59644 0.60146 0.60305 0.05221  -0.00421 -0.09640 51  ARG A CB  
305  C CG  . ARG A 40  ? 0.58512 0.57615 0.59617 0.05926  -0.01670 -0.10932 51  ARG A CG  
306  C CD  . ARG A 40  ? 0.75120 0.72769 0.77278 0.05172  -0.02597 -0.10958 51  ARG A CD  
307  N NE  . ARG A 40  ? 0.75884 0.72213 0.79582 0.04180  -0.02777 -0.09983 51  ARG A NE  
308  C CZ  . ARG A 40  ? 0.66213 0.61712 0.71142 0.03226  -0.03256 -0.09398 51  ARG A CZ  
309  N NH1 . ARG A 40  ? 0.54737 0.50479 0.59602 0.03057  -0.03618 -0.09703 51  ARG A NH1 
310  N NH2 . ARG A 40  ? 0.60674 0.55241 0.66983 0.02438  -0.03374 -0.08395 51  ARG A NH2 
311  N N   . GLU A 41  ? 0.49738 0.51487 0.49938 0.07256  -0.00018 -0.10458 52  GLU A N   
312  C CA  . GLU A 41  ? 0.51835 0.52846 0.52667 0.07712  -0.00319 -0.10692 52  GLU A CA  
313  C C   . GLU A 41  ? 0.47615 0.50008 0.48436 0.07590  0.00659  -0.09728 52  GLU A C   
314  O O   . GLU A 41  ? 0.49579 0.51541 0.50934 0.07957  0.00482  -0.09803 52  GLU A O   
315  C CB  . GLU A 41  ? 0.68107 0.69115 0.68463 0.09296  -0.01102 -0.12330 52  GLU A CB  
316  C CG  . GLU A 41  ? 0.66987 0.66738 0.67197 0.09637  -0.02270 -0.13543 52  GLU A CG  
317  C CD  . GLU A 41  ? 0.82700 0.79831 0.84396 0.08673  -0.03336 -0.13361 52  GLU A CD  
318  O OE1 . GLU A 41  ? 0.85546 0.81730 0.88280 0.08053  -0.03292 -0.12524 52  GLU A OE1 
319  O OE2 . GLU A 41  ? 0.95084 0.91208 0.96979 0.08518  -0.04255 -0.13967 52  GLU A OE2 
320  N N   . ALA A 42  ? 0.46759 0.50738 0.47084 0.07089  0.01562  -0.08821 53  ALA A N   
321  C CA  . ALA A 42  ? 0.57114 0.62228 0.57657 0.06760  0.02319  -0.07782 53  ALA A CA  
322  C C   . ALA A 42  ? 0.50200 0.53722 0.51621 0.05979  0.02142  -0.07125 53  ALA A C   
323  O O   . ALA A 42  ? 0.46841 0.49139 0.48533 0.05089  0.02004  -0.06652 53  ALA A O   
324  C CB  . ALA A 42  ? 0.44800 0.51263 0.44896 0.06073  0.03028  -0.06814 53  ALA A CB  
325  N N   . ARG A 43  ? 0.39401 0.43101 0.41255 0.06390  0.02151  -0.07067 54  ARG A N   
326  C CA  . ARG A 43  ? 0.44299 0.46682 0.46860 0.05746  0.01991  -0.06377 54  ARG A CA  
327  C C   . ARG A 43  ? 0.43599 0.46461 0.46050 0.04777  0.02576  -0.05210 54  ARG A C   
328  O O   . ARG A 43  ? 0.39752 0.44209 0.41933 0.04754  0.03089  -0.04813 54  ARG A O   
329  C CB  . ARG A 43  ? 0.54162 0.56765 0.57183 0.06510  0.01822  -0.06611 54  ARG A CB  
330  C CG  . ARG A 43  ? 0.60680 0.61336 0.64461 0.06292  0.01188  -0.06446 54  ARG A CG  
331  C CD  . ARG A 43  ? 0.76081 0.74986 0.80177 0.06435  0.00313  -0.07201 54  ARG A CD  
332  N NE  . ARG A 43  ? 0.88726 0.85828 0.93645 0.05718  -0.00176 -0.06499 54  ARG A NE  
333  C CZ  . ARG A 43  ? 0.82996 0.78611 0.88471 0.05233  -0.00817 -0.06491 54  ARG A CZ  
334  N NH1 . ARG A 43  ? 0.71172 0.66666 0.76444 0.05393  -0.01153 -0.07293 54  ARG A NH1 
335  N NH2 . ARG A 43  ? 0.71258 0.65608 0.77567 0.04551  -0.01149 -0.05561 54  ARG A NH2 
336  N N   . ILE A 44  ? 0.39769 0.41300 0.42464 0.04010  0.02436  -0.04628 55  ILE A N   
337  C CA  . ILE A 44  ? 0.32606 0.34337 0.35105 0.03270  0.02819  -0.03689 55  ILE A CA  
338  C C   . ILE A 44  ? 0.41565 0.42949 0.44436 0.03271  0.02708  -0.03236 55  ILE A C   
339  O O   . ILE A 44  ? 0.36998 0.37172 0.40243 0.03229  0.02351  -0.03138 55  ILE A O   
340  C CB  . ILE A 44  ? 0.29377 0.30197 0.31737 0.02595  0.02802  -0.03336 55  ILE A CB  
341  C CG1 . ILE A 44  ? 0.33243 0.34377 0.35293 0.02597  0.02825  -0.03792 55  ILE A CG1 
342  C CG2 . ILE A 44  ? 0.29807 0.30767 0.31823 0.02070  0.03085  -0.02546 55  ILE A CG2 
343  C CD1 . ILE A 44  ? 0.26013 0.26250 0.28245 0.02076  0.02672  -0.03580 55  ILE A CD1 
344  N N   . PHE A 45  ? 0.35872 0.38359 0.38737 0.03283  0.02949  -0.02867 56  PHE A N   
345  C CA  . PHE A 45  ? 0.42996 0.45301 0.46190 0.03287  0.02786  -0.02430 56  PHE A CA  
346  C C   . PHE A 45  ? 0.36365 0.37783 0.39179 0.02653  0.02735  -0.01781 56  PHE A C   
347  O O   . PHE A 45  ? 0.34875 0.36375 0.37217 0.02220  0.02910  -0.01572 56  PHE A O   
348  C CB  . PHE A 45  ? 0.33663 0.37615 0.37165 0.03461  0.02976  -0.02200 56  PHE A CB  
349  C CG  . PHE A 45  ? 0.34940 0.38851 0.38858 0.03449  0.02724  -0.01750 56  PHE A CG  
350  C CD1 . PHE A 45  ? 0.31205 0.35051 0.35649 0.04096  0.02487  -0.02030 56  PHE A CD1 
351  C CD2 . PHE A 45  ? 0.37291 0.41177 0.41073 0.02860  0.02609  -0.01111 56  PHE A CD2 
352  C CE1 . PHE A 45  ? 0.36786 0.40641 0.41622 0.04109  0.02207  -0.01600 56  PHE A CE1 
353  C CE2 . PHE A 45  ? 0.33444 0.37282 0.37566 0.02883  0.02261  -0.00754 56  PHE A CE2 
354  C CZ  . PHE A 45  ? 0.30719 0.34609 0.35377 0.03482  0.02095  -0.00954 56  PHE A CZ  
355  N N   . GLY A 46  ? 0.35410 0.36031 0.38371 0.02702  0.02464  -0.01474 57  GLY A N   
356  C CA  . GLY A 46  ? 0.30890 0.30929 0.33316 0.02315  0.02421  -0.00875 57  GLY A CA  
357  C C   . GLY A 46  ? 0.30417 0.29438 0.32917 0.02314  0.02243  -0.00502 57  GLY A C   
358  O O   . GLY A 46  ? 0.28915 0.27401 0.32034 0.02499  0.02045  -0.00708 57  GLY A O   
359  N N   . GLY A 47  ? 0.33696 0.32472 0.35585 0.02149  0.02243  0.00080  58  GLY A N   
360  C CA  . GLY A 47  ? 0.33143 0.31274 0.35077 0.02104  0.02169  0.00708  58  GLY A CA  
361  C C   . GLY A 47  ? 0.37120 0.35079 0.39204 0.01777  0.02406  0.00867  58  GLY A C   
362  O O   . GLY A 47  ? 0.32219 0.30381 0.34414 0.01645  0.02557  0.00349  58  GLY A O   
363  N N   . THR A 48  ? 0.28756 0.26477 0.30910 0.01644  0.02424  0.01705  59  THR A N   
364  C CA  . THR A 48  ? 0.27615 0.25395 0.30143 0.01280  0.02630  0.02096  59  THR A CA  
365  C C   . THR A 48  ? 0.33412 0.31980 0.34930 0.01280  0.03104  0.02230  59  THR A C   
366  O O   . THR A 48  ? 0.25977 0.24838 0.26454 0.01581  0.03160  0.02091  59  THR A O   
367  C CB  . THR A 48  ? 0.36092 0.33534 0.39354 0.01091  0.02449  0.03177  59  THR A CB  
368  O OG1 . THR A 48  ? 0.30709 0.28540 0.33091 0.01366  0.02574  0.03862  59  THR A OG1 
369  C CG2 . THR A 48  ? 0.24609 0.20981 0.29057 0.01117  0.01793  0.02938  59  THR A CG2 
370  N N   . LEU A 49  ? 0.26931 0.25803 0.28841 0.00984  0.03338  0.02459  60  LEU A N   
371  C CA  . LEU A 49  ? 0.29833 0.29551 0.30952 0.01079  0.03786  0.02685  60  LEU A CA  
372  C C   . LEU A 49  ? 0.29219 0.29596 0.30821 0.00919  0.04055  0.03884  60  LEU A C   
373  O O   . LEU A 49  ? 0.32479 0.32555 0.35437 0.00459  0.03841  0.04422  60  LEU A O   
374  C CB  . LEU A 49  ? 0.22684 0.22545 0.23902 0.00913  0.03887  0.01985  60  LEU A CB  
375  C CG  . LEU A 49  ? 0.25557 0.25155 0.26265 0.01046  0.03723  0.01031  60  LEU A CG  
376  C CD1 . LEU A 49  ? 0.19000 0.18750 0.19959 0.00845  0.03778  0.00493  60  LEU A CD1 
377  C CD2 . LEU A 49  ? 0.24041 0.23830 0.23560 0.01413  0.03738  0.00957  60  LEU A CD2 
378  N N   . ASP A 50  ? 0.33546 0.34892 0.34087 0.01338  0.04464  0.04334  61  ASP A N   
379  C CA  . ASP A 50  ? 0.36359 0.38893 0.37244 0.01300  0.04889  0.05600  61  ASP A CA  
380  C C   . ASP A 50  ? 0.36310 0.39912 0.36661 0.01577  0.05344  0.05386  61  ASP A C   
381  O O   . ASP A 50  ? 0.40195 0.43792 0.39169 0.02158  0.05363  0.04545  61  ASP A O   
382  C CB  . ASP A 50  ? 0.36165 0.39272 0.36110 0.01795  0.05024  0.06441  61  ASP A CB  
383  C CG  . ASP A 50  ? 0.50193 0.53489 0.48191 0.02638  0.05052  0.05650  61  ASP A CG  
384  O OD1 . ASP A 50  ? 0.58197 0.60497 0.55819 0.02669  0.04660  0.04476  61  ASP A OD1 
385  O OD2 . ASP A 50  ? 0.49685 0.54182 0.46563 0.03303  0.05407  0.06213  61  ASP A OD2 
386  N N   . LEU A 51  ? 0.28279 0.32737 0.29847 0.01159  0.05603  0.06140  62  LEU A N   
387  C CA  . LEU A 51  ? 0.33155 0.38788 0.34459 0.01436  0.06034  0.06016  62  LEU A CA  
388  C C   . LEU A 51  ? 0.29832 0.37449 0.30735 0.01954  0.06686  0.07258  62  LEU A C   
389  O O   . LEU A 51  ? 0.31221 0.39558 0.33127 0.01585  0.06830  0.08675  62  LEU A O   
390  C CB  . LEU A 51  ? 0.31845 0.37366 0.34830 0.00686  0.05865  0.06005  62  LEU A CB  
391  C CG  . LEU A 51  ? 0.35943 0.39731 0.39344 0.00263  0.05226  0.04867  62  LEU A CG  
392  C CD1 . LEU A 51  ? 0.37239 0.40984 0.42051 -0.00319 0.04975  0.04713  62  LEU A CD1 
393  C CD2 . LEU A 51  ? 0.29586 0.32715 0.31482 0.00762  0.05143  0.03613  62  LEU A CD2 
394  N N   . HIS A 52  ? 0.26441 0.34996 0.25892 0.02868  0.07036  0.06761  63  HIS A N   
395  C CA  . HIS A 52  ? 0.32210 0.42821 0.30745 0.03738  0.07676  0.07680  63  HIS A CA  
396  C C   . HIS A 52  ? 0.34313 0.46929 0.33852 0.03745  0.08272  0.08462  63  HIS A C   
397  O O   . HIS A 52  ? 0.33567 0.45852 0.33751 0.03471  0.08140  0.07764  63  HIS A O   
398  C CB  . HIS A 52  ? 0.30018 0.40460 0.26185 0.04993  0.07565  0.06520  63  HIS A CB  
399  C CG  . HIS A 52  ? 0.48623 0.57330 0.43850 0.05034  0.06932  0.05811  63  HIS A CG  
400  N ND1 . HIS A 52  ? 0.51230 0.58895 0.44862 0.05745  0.06408  0.04433  63  HIS A ND1 
401  C CD2 . HIS A 52  ? 0.40632 0.48485 0.36432 0.04454  0.06657  0.06325  63  HIS A CD2 
402  C CE1 . HIS A 52  ? 0.52732 0.59127 0.46063 0.05551  0.05882  0.04179  63  HIS A CE1 
403  N NE2 . HIS A 52  ? 0.53388 0.59892 0.47956 0.04824  0.06056  0.05273  63  HIS A NE2 
404  N N   . LYS A 53  ? 0.37314 0.52201 0.37019 0.04085  0.08940  0.10016  64  LYS A N   
405  C CA  . LYS A 53  ? 0.38244 0.55473 0.38788 0.04300  0.09555  0.10809  64  LYS A CA  
406  C C   . LYS A 53  ? 0.41931 0.59354 0.40714 0.05554  0.09542  0.09303  64  LYS A C   
407  O O   . LYS A 53  ? 0.48451 0.65284 0.45119 0.06595  0.09340  0.08318  64  LYS A O   
408  C CB  . LYS A 53  ? 0.43566 0.62677 0.44567 0.04439  0.09768  0.12385  64  LYS A CB  
409  C CG  . LYS A 53  ? 0.49059 0.67932 0.52286 0.03060  0.09585  0.14017  64  LYS A CG  
410  C CD  . LYS A 53  ? 0.51005 0.71991 0.55129 0.03084  0.09763  0.15748  64  LYS A CD  
411  C CE  . LYS A 53  ? 0.43260 0.63634 0.49794 0.01637  0.09331  0.17274  64  LYS A CE  
412  N NZ  . LYS A 53  ? 0.64764 0.86331 0.71336 0.01809  0.09384  0.18777  64  LYS A NZ  
413  N N   . GLY A 54  ? 0.41120 0.59207 0.40863 0.05437  0.09618  0.09090  65  GLY A N   
414  C CA  . GLY A 54  ? 0.34071 0.52163 0.32435 0.06540  0.09485  0.07707  65  GLY A CA  
415  C C   . GLY A 54  ? 0.39192 0.55256 0.36944 0.06484  0.09093  0.06180  65  GLY A C   
416  O O   . GLY A 54  ? 0.46217 0.62167 0.43315 0.07174  0.08896  0.05145  65  GLY A O   
417  N N   . SER A 55  ? 0.31725 0.45574 0.29843 0.05500  0.08497  0.05826  66  SER A N   
418  C CA  . SER A 55  ? 0.35323 0.46907 0.33015 0.05253  0.07762  0.04336  66  SER A CA  
419  C C   . SER A 55  ? 0.34518 0.44807 0.33885 0.03867  0.07395  0.04452  66  SER A C   
420  O O   . SER A 55  ? 0.32290 0.42947 0.33006 0.03322  0.07401  0.04599  66  SER A O   
421  C CB  . SER A 55  ? 0.28818 0.38942 0.24640 0.05890  0.07259  0.03363  66  SER A CB  
422  O OG  . SER A 55  ? 0.38119 0.48040 0.33912 0.05588  0.07287  0.04048  66  SER A OG  
423  N N   . GLY A 56  ? 0.26086 0.34900 0.25353 0.03387  0.07011  0.04312  67  GLY A N   
424  C CA  . GLY A 56  ? 0.27271 0.34862 0.27963 0.02293  0.06599  0.04259  67  GLY A CA  
425  C C   . GLY A 56  ? 0.30391 0.38976 0.33067 0.01540  0.06771  0.05438  67  GLY A C   
426  O O   . GLY A 56  ? 0.28941 0.37030 0.32838 0.00879  0.06430  0.05182  67  GLY A O   
427  N N   . GLN A 57  ? 0.22143 0.32215 0.25218 0.01632  0.07237  0.06808  68  GLN A N   
428  C CA  . GLN A 57  ? 0.29519 0.40578 0.34791 0.00783  0.07288  0.08154  68  GLN A CA  
429  C C   . GLN A 57  ? 0.29519 0.42106 0.35614 0.00838  0.07575  0.08318  68  GLN A C   
430  O O   . GLN A 57  ? 0.27346 0.40209 0.35480 -0.00043 0.07304  0.08968  68  GLN A O   
431  C CB  . GLN A 57  ? 0.24379 0.36897 0.30003 0.00819  0.07740  0.09856  68  GLN A CB  
432  C CG  . GLN A 57  ? 0.26978 0.38017 0.32222 0.00615  0.07357  0.09954  68  GLN A CG  
433  C CD  . GLN A 57  ? 0.28080 0.40562 0.34144 0.00413  0.07695  0.11943  68  GLN A CD  
434  O OE1 . GLN A 57  ? 0.26942 0.41144 0.34708 -0.00066 0.07982  0.13419  68  GLN A OE1 
435  N NE2 . GLN A 57  ? 0.21577 0.33503 0.26510 0.00765  0.07644  0.12102  68  GLN A NE2 
436  N N   . GLU A 58  ? 0.25473 0.39038 0.30095 0.01897  0.08019  0.07726  69  GLU A N   
437  C CA  . GLU A 58  ? 0.23409 0.38527 0.28819 0.02067  0.08286  0.07850  69  GLU A CA  
438  C C   . GLU A 58  ? 0.28221 0.41770 0.34146 0.01524  0.07621  0.06689  69  GLU A C   
439  O O   . GLU A 58  ? 0.25199 0.39624 0.32659 0.01087  0.07547  0.07036  69  GLU A O   
440  C CB  . GLU A 58  ? 0.25414 0.41898 0.29014 0.03532  0.08838  0.07411  69  GLU A CB  
441  C CG  . GLU A 58  ? 0.39512 0.58282 0.44023 0.03911  0.09300  0.07908  69  GLU A CG  
442  C CD  . GLU A 58  ? 0.34909 0.55759 0.40965 0.03511  0.09632  0.09695  69  GLU A CD  
443  O OE1 . GLU A 58  ? 0.34488 0.55374 0.40493 0.03281  0.09705  0.10598  69  GLU A OE1 
444  O OE2 . GLU A 58  ? 0.44496 0.66802 0.51822 0.03407  0.09689  0.10183  69  GLU A OE2 
445  N N   . ALA A 59  ? 0.22316 0.33694 0.27036 0.01540  0.07116  0.05396  70  ALA A N   
446  C CA  . ALA A 59  ? 0.27570 0.37555 0.32716 0.01018  0.06494  0.04419  70  ALA A CA  
447  C C   . ALA A 59  ? 0.30566 0.40030 0.37637 -0.00073 0.06002  0.04905  70  ALA A C   
448  O O   . ALA A 59  ? 0.27570 0.37004 0.35718 -0.00512 0.05609  0.04665  70  ALA A O   
449  C CB  . ALA A 59  ? 0.23672 0.31784 0.27225 0.01269  0.06126  0.03184  70  ALA A CB  
450  N N   . MET A 60  ? 0.24625 0.33557 0.32145 -0.00475 0.05890  0.05533  71  MET A N   
451  C CA  . MET A 60  ? 0.29737 0.37979 0.39196 -0.01456 0.05232  0.05991  71  MET A CA  
452  C C   . MET A 60  ? 0.25167 0.35135 0.36702 -0.01986 0.05302  0.07295  71  MET A C   
453  O O   . MET A 60  ? 0.26979 0.36478 0.40109 -0.02693 0.04585  0.07202  71  MET A O   
454  C CB  . MET A 60  ? 0.25247 0.32592 0.34812 -0.01697 0.05057  0.06515  71  MET A CB  
455  C CG  . MET A 60  ? 0.27539 0.33159 0.35453 -0.01301 0.04845  0.05271  71  MET A CG  
456  S SD  . MET A 60  ? 0.30589 0.34553 0.38366 -0.01452 0.04091  0.03622  71  MET A SD  
457  C CE  . MET A 60  ? 0.39803 0.44302 0.45931 -0.00778 0.04531  0.02739  71  MET A CE  
458  N N   A LYS A 61  ? 0.21794 0.33896 0.33356 -0.01604 0.06123  0.08534  72  LYS A N   
459  N N   B LYS A 61  ? 0.21903 0.34001 0.33481 -0.01613 0.06120  0.08547  72  LYS A N   
460  C CA  A LYS A 61  ? 0.23812 0.38069 0.37470 -0.02060 0.06323  0.09997  72  LYS A CA  
461  C CA  B LYS A 61  ? 0.23809 0.38067 0.37466 -0.02058 0.06323  0.09991  72  LYS A CA  
462  C C   A LYS A 61  ? 0.23677 0.38308 0.37849 -0.02057 0.06092  0.09255  72  LYS A C   
463  C C   B LYS A 61  ? 0.23689 0.38267 0.37853 -0.02065 0.06074  0.09225  72  LYS A C   
464  O O   A LYS A 61  ? 0.23861 0.38755 0.40221 -0.02923 0.05498  0.09781  72  LYS A O   
465  O O   B LYS A 61  ? 0.23887 0.38650 0.40215 -0.02935 0.05456  0.09708  72  LYS A O   
466  C CB  A LYS A 61  ? 0.23643 0.40476 0.36729 -0.01299 0.07419  0.11277  72  LYS A CB  
467  C CB  B LYS A 61  ? 0.23658 0.40515 0.36727 -0.01279 0.07424  0.11242  72  LYS A CB  
468  C CG  A LYS A 61  ? 0.23572 0.42986 0.39110 -0.01908 0.07741  0.13457  72  LYS A CG  
469  C CG  B LYS A 61  ? 0.21233 0.40995 0.36287 -0.01488 0.07877  0.12800  72  LYS A CG  
470  C CD  A LYS A 61  ? 0.24086 0.45102 0.38188 -0.00974 0.08444  0.14325  72  LYS A CD  
471  C CD  B LYS A 61  ? 0.24162 0.45851 0.37921 -0.00493 0.08635  0.13667  72  LYS A CD  
472  C CE  A LYS A 61  ? 0.33896 0.56922 0.49694 -0.01308 0.08410  0.16033  72  LYS A CE  
473  C CE  B LYS A 61  ? 0.28390 0.52269 0.43737 -0.00664 0.08674  0.15021  72  LYS A CE  
474  N NZ  A LYS A 61  ? 0.21390 0.43690 0.39563 -0.02676 0.07624  0.17393  72  LYS A NZ  
475  N NZ  B LYS A 61  ? 0.33972 0.59644 0.48232 0.00235  0.09251  0.15999  72  LYS A NZ  
476  N N   . LYS A 62  ? 0.24046 0.38569 0.36274 -0.01105 0.06421  0.08017  73  LYS A N   
477  C CA  . LYS A 62  ? 0.24544 0.39385 0.37083 -0.01001 0.06189  0.07301  73  LYS A CA  
478  C C   . LYS A 62  ? 0.25084 0.38029 0.38485 -0.01829 0.05126  0.06450  73  LYS A C   
479  O O   . LYS A 62  ? 0.17684 0.31131 0.32327 -0.02157 0.04706  0.06377  73  LYS A O   
480  C CB  . LYS A 62  ? 0.27304 0.41853 0.37473 0.00160  0.06546  0.06071  73  LYS A CB  
481  C CG  . LYS A 62  ? 0.36522 0.51587 0.46784 0.00489  0.06395  0.05419  73  LYS A CG  
482  C CD  . LYS A 62  ? 0.48192 0.66079 0.59349 0.01019  0.07063  0.06429  73  LYS A CD  
483  C CE  . LYS A 62  ? 0.46629 0.64992 0.58072 0.01326  0.06809  0.05793  73  LYS A CE  
484  N NZ  . LYS A 62  ? 0.56031 0.77415 0.69242 0.01493  0.07321  0.07055  73  LYS A NZ  
485  N N   . ALA A 63  ? 0.18763 0.29635 0.31492 -0.02076 0.04650  0.05767  74  ALA A N   
486  C CA  . ALA A 63  ? 0.20482 0.29550 0.33637 -0.02594 0.03643  0.04763  74  ALA A CA  
487  C C   . ALA A 63  ? 0.22941 0.31639 0.38442 -0.03592 0.02814  0.05539  74  ALA A C   
488  O O   . ALA A 63  ? 0.26623 0.33779 0.42542 -0.03934 0.01819  0.04627  74  ALA A O   
489  C CB  . ALA A 63  ? 0.21715 0.28920 0.33006 -0.02228 0.03529  0.03604  74  ALA A CB  
490  N N   . GLY A 64  ? 0.22379 0.32453 0.39420 -0.04024 0.03124  0.07217  75  GLY A N   
491  C CA  . GLY A 64  ? 0.25675 0.35194 0.45118 -0.05063 0.02202  0.08138  75  GLY A CA  
492  C C   . GLY A 64  ? 0.27136 0.34529 0.46157 -0.05196 0.01655  0.07738  75  GLY A C   
493  O O   . GLY A 64  ? 0.30298 0.36410 0.51059 -0.05944 0.00503  0.07888  75  GLY A O   
494  N N   . LEU A 65  ? 0.23738 0.30683 0.40577 -0.04459 0.02351  0.07218  76  LEU A N   
495  C CA  . LEU A 65  ? 0.31552 0.36525 0.47802 -0.04427 0.01862  0.06645  76  LEU A CA  
496  C C   . LEU A 65  ? 0.28069 0.33544 0.44132 -0.04374 0.02448  0.07916  76  LEU A C   
497  O O   . LEU A 65  ? 0.31447 0.35418 0.46861 -0.04230 0.02143  0.07474  76  LEU A O   
498  C CB  . LEU A 65  ? 0.22346 0.26155 0.36248 -0.03633 0.01980  0.04826  76  LEU A CB  
499  C CG  . LEU A 65  ? 0.27232 0.30417 0.41065 -0.03593 0.01329  0.03491  76  LEU A CG  
500  C CD1 . LEU A 65  ? 0.26774 0.29425 0.38315 -0.02812 0.01682  0.02105  76  LEU A CD1 
501  C CD2 . LEU A 65  ? 0.29106 0.30726 0.44451 -0.04112 -0.00037 0.03039  76  LEU A CD2 
502  N N   . LEU A 66  ? 0.28460 0.36146 0.45001 -0.04386 0.03292  0.09478  77  LEU A N   
503  C CA  . LEU A 66  ? 0.29708 0.38087 0.45652 -0.04139 0.03941  0.10637  77  LEU A CA  
504  C C   . LEU A 66  ? 0.29081 0.36242 0.46714 -0.04938 0.03098  0.11608  77  LEU A C   
505  O O   . LEU A 66  ? 0.30450 0.36790 0.47135 -0.04656 0.03168  0.11673  77  LEU A O   
506  C CB  . LEU A 66  ? 0.24934 0.36256 0.41121 -0.03890 0.05003  0.12202  77  LEU A CB  
507  C CG  . LEU A 66  ? 0.23822 0.36054 0.38894 -0.03385 0.05750  0.13266  77  LEU A CG  
508  C CD1 . LEU A 66  ? 0.21735 0.32420 0.34104 -0.02483 0.05878  0.11600  77  LEU A CD1 
509  C CD2 . LEU A 66  ? 0.20103 0.35589 0.35087 -0.02853 0.06901  0.14749  77  LEU A CD2 
510  N N   . GLN A 67  ? 0.25478 0.32440 0.45718 -0.05940 0.02182  0.12396  78  GLN A N   
511  C CA  . GLN A 67  ? 0.26382 0.31868 0.48386 -0.06713 0.01143  0.13271  78  GLN A CA  
512  C C   . GLN A 67  ? 0.31680 0.34290 0.52725 -0.06389 0.00203  0.11354  78  GLN A C   
513  O O   . GLN A 67  ? 0.32769 0.34122 0.53844 -0.06402 -0.00199 0.11635  78  GLN A O   
514  C CB  . GLN A 67  ? 0.25336 0.31121 0.50562 -0.07914 0.00157  0.14540  78  GLN A CB  
515  C CG  . GLN A 67  ? 0.26055 0.30671 0.53153 -0.08665 -0.00901 0.15864  78  GLN A CG  
516  C CD  . GLN A 67  ? 0.32987 0.39453 0.59440 -0.08362 0.00073  0.17637  78  GLN A CD  
517  O OE1 . GLN A 67  ? 0.35718 0.44878 0.61896 -0.08086 0.01093  0.18685  78  GLN A OE1 
518  N NE2 . GLN A 67  ? 0.26620 0.31676 0.52743 -0.08297 -0.00285 0.17885  78  GLN A NE2 
519  N N   . THR A 68  ? 0.29297 0.31006 0.49437 -0.06011 -0.00126 0.09437  79  THR A N   
520  C CA  . THR A 68  ? 0.29194 0.28603 0.48260 -0.05517 -0.00881 0.07588  79  THR A CA  
521  C C   . THR A 68  ? 0.35723 0.34955 0.52757 -0.04769 -0.00116 0.07322  79  THR A C   
522  O O   . THR A 68  ? 0.37684 0.35319 0.54727 -0.04633 -0.00753 0.06961  79  THR A O   
523  C CB  . THR A 68  ? 0.30684 0.29807 0.48701 -0.05074 -0.01021 0.05767  79  THR A CB  
524  O OG1 . THR A 68  ? 0.32579 0.32459 0.52328 -0.05725 -0.01471 0.06234  79  THR A OG1 
525  C CG2 . THR A 68  ? 0.34963 0.31856 0.52515 -0.04658 -0.02111 0.03993  79  THR A CG2 
526  N N   . TYR A 69  ? 0.29931 0.30786 0.45288 -0.04241 0.01158  0.07499  80  TYR A N   
527  C CA  . TYR A 69  ? 0.28070 0.28923 0.41570 -0.03561 0.01831  0.07361  80  TYR A CA  
528  C C   . TYR A 69  ? 0.28792 0.29617 0.43146 -0.03868 0.01728  0.08927  80  TYR A C   
529  O O   . TYR A 69  ? 0.32496 0.32123 0.46208 -0.03553 0.01460  0.08547  80  TYR A O   
530  C CB  . TYR A 69  ? 0.27017 0.29608 0.38811 -0.02961 0.03006  0.07353  80  TYR A CB  
531  C CG  . TYR A 69  ? 0.26455 0.29544 0.36650 -0.02349 0.03696  0.07745  80  TYR A CG  
532  C CD1 . TYR A 69  ? 0.28827 0.30682 0.37639 -0.01847 0.03558  0.06666  80  TYR A CD1 
533  C CD2 . TYR A 69  ? 0.32557 0.37540 0.42594 -0.02194 0.04474  0.09187  80  TYR A CD2 
534  C CE1 . TYR A 69  ? 0.31670 0.33954 0.39052 -0.01288 0.04056  0.06982  80  TYR A CE1 
535  C CE2 . TYR A 69  ? 0.24192 0.29651 0.32606 -0.01521 0.05007  0.09448  80  TYR A CE2 
536  C CZ  . TYR A 69  ? 0.36512 0.40510 0.43631 -0.01108 0.04736  0.08318  80  TYR A CZ  
537  O OH  . TYR A 69  ? 0.36031 0.40467 0.41603 -0.00452 0.05129  0.08554  80  TYR A OH  
538  N N   . TYR A 70  ? 0.30291 0.32593 0.46153 -0.04470 0.01951  0.10814  81  TYR A N   
539  C CA  . TYR A 70  ? 0.30256 0.32755 0.46952 -0.04788 0.01890  0.12568  81  TYR A CA  
540  C C   . TYR A 70  ? 0.36856 0.36935 0.55016 -0.05264 0.00497  0.12381  81  TYR A C   
541  O O   . TYR A 70  ? 0.30821 0.30210 0.48814 -0.05147 0.00319  0.12968  81  TYR A O   
542  C CB  . TYR A 70  ? 0.24573 0.29302 0.43015 -0.05456 0.02300  0.14831  81  TYR A CB  
543  C CG  . TYR A 70  ? 0.28189 0.35682 0.45219 -0.04803 0.03740  0.15495  81  TYR A CG  
544  C CD1 . TYR A 70  ? 0.29697 0.37460 0.43988 -0.03701 0.04536  0.14529  81  TYR A CD1 
545  C CD2 . TYR A 70  ? 0.28937 0.38831 0.47483 -0.05242 0.04214  0.17107  81  TYR A CD2 
546  C CE1 . TYR A 70  ? 0.32544 0.42699 0.45469 -0.02942 0.05690  0.14967  81  TYR A CE1 
547  C CE2 . TYR A 70  ? 0.25923 0.38494 0.43137 -0.04449 0.05513  0.17637  81  TYR A CE2 
548  C CZ  . TYR A 70  ? 0.34835 0.47425 0.49156 -0.03245 0.06208  0.16475  81  TYR A CZ  
549  O OH  . TYR A 70  ? 0.27677 0.42774 0.40582 -0.02293 0.07340  0.16814  81  TYR A OH  
550  N N   . ASP A 71  ? 0.29715 0.28449 0.49306 -0.05727 -0.00598 0.11528  82  ASP A N   
551  C CA  . ASP A 71  ? 0.34088 0.30424 0.55251 -0.06108 -0.02138 0.11298  82  ASP A CA  
552  C C   . ASP A 71  ? 0.31665 0.26283 0.51123 -0.05186 -0.02394 0.09526  82  ASP A C   
553  O O   . ASP A 71  ? 0.37700 0.30527 0.58038 -0.05231 -0.03444 0.09532  82  ASP A O   
554  C CB  . ASP A 71  ? 0.29033 0.24352 0.51994 -0.06686 -0.03372 0.10616  82  ASP A CB  
555  C CG  . ASP A 71  ? 0.37563 0.34392 0.62956 -0.07804 -0.03471 0.12636  82  ASP A CG  
556  O OD1 . ASP A 71  ? 0.35722 0.34070 0.61943 -0.08268 -0.02880 0.14848  82  ASP A OD1 
557  O OD2 . ASP A 71  ? 0.43396 0.40021 0.69944 -0.08208 -0.04177 0.12060  82  ASP A OD2 
558  N N   . LEU A 72  ? 0.37388 0.32556 0.54570 -0.04350 -0.01521 0.08056  83  LEU A N   
559  C CA  . LEU A 72  ? 0.33747 0.27759 0.49364 -0.03468 -0.01618 0.06485  83  LEU A CA  
560  C C   . LEU A 72  ? 0.39129 0.34069 0.53060 -0.02950 -0.00599 0.06941  83  LEU A C   
561  O O   . LEU A 72  ? 0.37491 0.31656 0.50328 -0.02275 -0.00674 0.05895  83  LEU A O   
562  C CB  . LEU A 72  ? 0.32791 0.26769 0.47153 -0.02912 -0.01485 0.04552  83  LEU A CB  
563  C CG  . LEU A 72  ? 0.40814 0.33342 0.56405 -0.03046 -0.02789 0.03485  83  LEU A CG  
564  C CD1 . LEU A 72  ? 0.36910 0.29803 0.51108 -0.02473 -0.02512 0.01810  83  LEU A CD1 
565  C CD2 . LEU A 72  ? 0.38699 0.29205 0.54908 -0.02696 -0.03975 0.02876  83  LEU A CD2 
566  N N   . ALA A 73  ? 0.28311 0.24998 0.41978 -0.03163 0.00314  0.08416  84  ALA A N   
567  C CA  . ALA A 73  ? 0.31049 0.28635 0.42933 -0.02564 0.01185  0.08704  84  ALA A CA  
568  C C   . ALA A 73  ? 0.36481 0.33860 0.49103 -0.02778 0.00917  0.10286  84  ALA A C   
569  O O   . ALA A 73  ? 0.36896 0.33803 0.51526 -0.03511 0.00219  0.11513  84  ALA A O   
570  C CB  . ALA A 73  ? 0.29903 0.29573 0.40659 -0.02371 0.02319  0.09153  84  ALA A CB  
571  N N   . LEU A 74  ? 0.31177 0.28924 0.42211 -0.02154 0.01404  0.10323  85  LEU A N   
572  C CA  . LEU A 74  ? 0.45504 0.43015 0.56884 -0.02190 0.01147  0.11679  85  LEU A CA  
573  C C   . LEU A 74  ? 0.37121 0.36460 0.46737 -0.01666 0.02158  0.12514  85  LEU A C   
574  O O   . LEU A 74  ? 0.36921 0.36437 0.44652 -0.00935 0.02563  0.11327  85  LEU A O   
575  C CB  . LEU A 74  ? 0.37855 0.33480 0.49090 -0.01760 0.00354  0.10535  85  LEU A CB  
576  C CG  . LEU A 74  ? 0.53204 0.47993 0.65259 -0.01853 -0.00289 0.11776  85  LEU A CG  
577  C CD1 . LEU A 74  ? 0.50747 0.45526 0.65023 -0.02819 -0.00795 0.13711  85  LEU A CD1 
578  C CD2 . LEU A 74  ? 0.56749 0.49519 0.69121 -0.01424 -0.01261 0.10361  85  LEU A CD2 
579  N N   . PRO A 75  ? 0.34173 0.34987 0.44325 -0.01967 0.02539  0.14543  86  PRO A N   
580  C CA  . PRO A 75  ? 0.36825 0.39271 0.45095 -0.01251 0.03349  0.15276  86  PRO A CA  
581  C C   . PRO A 75  ? 0.38122 0.39377 0.45727 -0.00847 0.02841  0.15143  86  PRO A C   
582  O O   . PRO A 75  ? 0.42905 0.42747 0.52025 -0.01306 0.01986  0.15725  86  PRO A O   
583  C CB  . PRO A 75  ? 0.43327 0.47726 0.52724 -0.01735 0.03787  0.17707  86  PRO A CB  
584  C CG  . PRO A 75  ? 0.43208 0.46213 0.55389 -0.02838 0.02788  0.18526  86  PRO A CG  
585  C CD  . PRO A 75  ? 0.36296 0.37393 0.48863 -0.02952 0.02151  0.16368  86  PRO A CD  
586  N N   A MET A 76  ? 0.38011 0.39746 0.43415 0.00040  0.03248  0.14316  87  MET A N   
587  N N   B MET A 76  ? 0.37977 0.39722 0.43370 0.00044  0.03254  0.14308  87  MET A N   
588  C CA  A MET A 76  ? 0.42304 0.43054 0.47041 0.00472  0.02749  0.14119  87  MET A CA  
589  C CA  B MET A 76  ? 0.42349 0.43103 0.46980 0.00510  0.02771  0.13996  87  MET A CA  
590  C C   A MET A 76  ? 0.43450 0.45699 0.46025 0.01320  0.03307  0.14567  87  MET A C   
591  C C   B MET A 76  ? 0.43420 0.45733 0.45984 0.01321  0.03332  0.14611  87  MET A C   
592  O O   A MET A 76  ? 0.45385 0.48788 0.46429 0.01863  0.03927  0.13887  87  MET A O   
593  O O   B MET A 76  ? 0.45311 0.48893 0.46365 0.01858  0.03985  0.14066  87  MET A O   
594  C CB  A MET A 76  ? 0.44399 0.43517 0.48899 0.00714  0.02244  0.12035  87  MET A CB  
595  C CB  B MET A 76  ? 0.44237 0.43575 0.48360 0.00827  0.02384  0.11833  87  MET A CB  
596  C CG  A MET A 76  ? 0.39830 0.37264 0.46323 0.00130  0.01457  0.11574  87  MET A CG  
597  C CG  B MET A 76  ? 0.40171 0.38169 0.45889 0.00293  0.01883  0.10881  87  MET A CG  
598  S SD  A MET A 76  ? 0.53910 0.49900 0.60100 0.00604  0.00951  0.09339  87  MET A SD  
599  S SD  B MET A 76  ? 0.45546 0.42429 0.50566 0.00810  0.01556  0.08641  87  MET A SD  
600  C CE  A MET A 76  ? 0.35598 0.31091 0.41290 0.01152  0.00483  0.09721  87  MET A CE  
601  C CE  B MET A 76  ? 0.41729 0.37993 0.46456 0.01283  0.01017  0.09058  87  MET A CE  
602  N N   . GLY A 77  ? 0.42106 0.44260 0.44549 0.01494  0.02982  0.15684  88  GLY A N   
603  C CA  . GLY A 77  ? 0.48514 0.51949 0.48828 0.02395  0.03324  0.16077  88  GLY A CA  
604  C C   . GLY A 77  ? 0.52099 0.54637 0.50883 0.03093  0.02967  0.14192  88  GLY A C   
605  O O   . GLY A 77  ? 0.48037 0.49215 0.47385 0.02888  0.02593  0.12653  88  GLY A O   
606  N N   . VAL A 78  ? 0.48176 0.51630 0.45009 0.03960  0.03044  0.14390  89  VAL A N   
607  C CA  . VAL A 78  ? 0.45553 0.48400 0.40872 0.04646  0.02631  0.12731  89  VAL A CA  
608  C C   . VAL A 78  ? 0.50647 0.53640 0.44919 0.05252  0.02179  0.13421  89  VAL A C   
609  O O   . VAL A 78  ? 0.50511 0.54998 0.43709 0.05728  0.02539  0.14799  89  VAL A O   
610  C CB  . VAL A 78  ? 0.50419 0.54255 0.43950 0.05312  0.03072  0.11682  89  VAL A CB  
611  C CG1 . VAL A 78  ? 0.49952 0.53002 0.42183 0.05911  0.02413  0.10123  89  VAL A CG1 
612  C CG2 . VAL A 78  ? 0.59856 0.63518 0.54400 0.04743  0.03459  0.10984  89  VAL A CG2 
613  N N   . ASN A 79  ? 0.50056 0.51683 0.44645 0.05285  0.01403  0.12525  90  ASN A N   
614  C CA  . ASN A 79  ? 0.44874 0.46523 0.38376 0.05933  0.00828  0.12829  90  ASN A CA  
615  C C   . ASN A 79  ? 0.47122 0.48502 0.39252 0.06532  0.00373  0.11087  90  ASN A C   
616  O O   . ASN A 79  ? 0.39954 0.40433 0.32909 0.06181  0.00165  0.09727  90  ASN A O   
617  C CB  . ASN A 79  ? 0.43442 0.43788 0.38601 0.05544  0.00140  0.13319  90  ASN A CB  
618  C CG  . ASN A 79  ? 0.48540 0.48928 0.45143 0.04951  0.00297  0.15212  90  ASN A CG  
619  O OD1 . ASN A 79  ? 0.51681 0.53440 0.47927 0.04868  0.00977  0.16478  90  ASN A OD1 
620  N ND2 . ASN A 79  ? 0.49932 0.48866 0.48293 0.04560  -0.00396 0.15473  90  ASN A ND2 
621  N N   . ILE A 80  ? 0.47959 0.50184 0.38035 0.07444  0.00163  0.11186  91  ILE A N   
622  C CA  . ILE A 80  ? 0.47362 0.49141 0.36263 0.08028  -0.00623 0.09726  91  ILE A CA  
623  C C   . ILE A 80  ? 0.45989 0.47237 0.35148 0.08201  -0.01438 0.10133  91  ILE A C   
624  O O   . ILE A 80  ? 0.50390 0.52285 0.38960 0.08544  -0.01410 0.11558  91  ILE A O   
625  C CB  . ILE A 80  ? 0.55789 0.58692 0.42144 0.09085  -0.00558 0.09335  91  ILE A CB  
626  C CG1 . ILE A 80  ? 0.49356 0.52907 0.35613 0.08963  0.00302  0.09080  91  ILE A CG1 
627  C CG2 . ILE A 80  ? 0.48462 0.50636 0.33788 0.09617  -0.01624 0.07723  91  ILE A CG2 
628  C CD1 . ILE A 80  ? 0.57891 0.62919 0.41693 0.10159  0.00574  0.09043  91  ILE A CD1 
629  N N   . ALA A 81  ? 0.41816 0.42033 0.31972 0.07957  -0.02147 0.09016  92  ALA A N   
630  C CA  . ALA A 81  ? 0.42485 0.42249 0.32996 0.08180  -0.03014 0.09192  92  ALA A CA  
631  C C   . ALA A 81  ? 0.46554 0.46167 0.36166 0.08636  -0.03929 0.07852  92  ALA A C   
632  O O   . ALA A 81  ? 0.46761 0.46255 0.36137 0.08529  -0.03947 0.06685  92  ALA A O   
633  C CB  . ALA A 81  ? 0.37157 0.35972 0.30107 0.07500  -0.03125 0.09215  92  ALA A CB  
634  N N   . ASP A 82  ? 0.42262 0.41823 0.31494 0.09113  -0.04803 0.08071  93  ASP A N   
635  C CA  . ASP A 82  ? 0.51530 0.50830 0.40440 0.09402  -0.05899 0.06875  93  ASP A CA  
636  C C   . ASP A 82  ? 0.42381 0.41136 0.33697 0.08802  -0.06299 0.06491  93  ASP A C   
637  O O   . ASP A 82  ? 0.41232 0.39728 0.34163 0.08356  -0.05799 0.07046  93  ASP A O   
638  C CB  . ASP A 82  ? 0.46169 0.45887 0.33075 0.10389  -0.06735 0.07187  93  ASP A CB  
639  C CG  . ASP A 82  ? 0.53419 0.53120 0.40988 0.10507  -0.07048 0.08383  93  ASP A CG  
640  O OD1 . ASP A 82  ? 0.50383 0.49591 0.40094 0.09871  -0.06794 0.08785  93  ASP A OD1 
641  O OD2 . ASP A 82  ? 0.57029 0.57195 0.42889 0.11337  -0.07630 0.08892  93  ASP A OD2 
642  N N   . GLU A 83  ? 0.43293 0.41948 0.34896 0.08852  -0.07283 0.05533  94  GLU A N   
643  C CA  . GLU A 83  ? 0.42330 0.40897 0.36246 0.08355  -0.07628 0.05157  94  GLU A CA  
644  C C   . GLU A 83  ? 0.47263 0.45819 0.42175 0.08582  -0.07922 0.05960  94  GLU A C   
645  O O   . GLU A 83  ? 0.46627 0.45265 0.43569 0.08290  -0.07990 0.05757  94  GLU A O   
646  C CB  . GLU A 83  ? 0.38907 0.37552 0.33004 0.08313  -0.08738 0.04164  94  GLU A CB  
647  C CG  . GLU A 83  ? 0.46215 0.44937 0.39563 0.08948  -0.10040 0.04226  94  GLU A CG  
648  C CD  . GLU A 83  ? 0.48215 0.46840 0.38716 0.09794  -0.10419 0.04215  94  GLU A CD  
649  O OE1 . GLU A 83  ? 0.56743 0.55343 0.45902 0.09905  -0.09666 0.04125  94  GLU A OE1 
650  O OE2 . GLU A 83  ? 0.54249 0.52947 0.43816 0.10437  -0.11489 0.04276  94  GLU A OE2 
651  N N   . LYS A 84  ? 0.39992 0.38550 0.33543 0.09166  -0.08113 0.06893  95  LYS A N   
652  C CA  . LYS A 84  ? 0.45424 0.43818 0.39905 0.09394  -0.08416 0.07801  95  LYS A CA  
653  C C   . LYS A 84  ? 0.44865 0.42837 0.40009 0.09124  -0.07535 0.08821  95  LYS A C   
654  O O   . LYS A 84  ? 0.50251 0.47883 0.46100 0.09327  -0.07823 0.09734  95  LYS A O   
655  C CB  . LYS A 84  ? 0.42191 0.40833 0.34925 0.10183  -0.09269 0.08406  95  LYS A CB  
656  C CG  . LYS A 84  ? 0.54742 0.53667 0.46198 0.10546  -0.10236 0.07372  95  LYS A CG  
657  C CD  . LYS A 84  ? 0.56925 0.56118 0.46553 0.11449  -0.11175 0.07904  95  LYS A CD  
658  C CE  . LYS A 84  ? 0.64534 0.63863 0.52233 0.11965  -0.12076 0.06817  95  LYS A CE  
659  N NZ  . LYS A 84  ? 0.79103 0.78707 0.65107 0.12925  -0.13235 0.07116  95  LYS A NZ  
660  N N   . GLY A 85  ? 0.43774 0.41696 0.38794 0.08667  -0.06590 0.08722  96  GLY A N   
661  C CA  . GLY A 85  ? 0.46910 0.44383 0.42721 0.08325  -0.05903 0.09704  96  GLY A CA  
662  C C   . GLY A 85  ? 0.50035 0.47841 0.44404 0.08560  -0.05614 0.11228  96  GLY A C   
663  O O   . GLY A 85  ? 0.53236 0.50649 0.48504 0.08200  -0.05214 0.12318  96  GLY A O   
664  N N   . ASN A 86  ? 0.50859 0.49452 0.43064 0.09183  -0.05860 0.11387  97  ASN A N   
665  C CA  . ASN A 86  ? 0.51498 0.50878 0.42142 0.09502  -0.05402 0.12896  97  ASN A CA  
666  C C   . ASN A 86  ? 0.50071 0.49968 0.40344 0.09136  -0.04327 0.12922  97  ASN A C   
667  O O   . ASN A 86  ? 0.44459 0.44475 0.34183 0.09127  -0.04150 0.11565  97  ASN A O   
668  C CB  . ASN A 86  ? 0.48529 0.48765 0.36711 0.10485  -0.05996 0.12849  97  ASN A CB  
669  C CG  . ASN A 86  ? 0.53689 0.53525 0.42187 0.10878  -0.07130 0.12883  97  ASN A CG  
670  O OD1 . ASN A 86  ? 0.55469 0.54872 0.45139 0.10747  -0.07329 0.14066  97  ASN A OD1 
671  N ND2 . ASN A 86  ? 0.60921 0.60836 0.48497 0.11359  -0.07999 0.11588  97  ASN A ND2 
672  N N   . ILE A 87  ? 0.51303 0.51527 0.42009 0.08807  -0.03679 0.14545  98  ILE A N   
673  C CA  . ILE A 87  ? 0.53092 0.54105 0.43478 0.08504  -0.02651 0.14832  98  ILE A CA  
674  C C   . ILE A 87  ? 0.51130 0.53813 0.38793 0.09445  -0.02352 0.15235  98  ILE A C   
675  O O   . ILE A 87  ? 0.54074 0.57723 0.40784 0.09902  -0.02331 0.16851  98  ILE A O   
676  C CB  . ILE A 87  ? 0.49823 0.50639 0.41991 0.07718  -0.02181 0.16510  98  ILE A CB  
677  C CG1 . ILE A 87  ? 0.53701 0.52799 0.48377 0.06970  -0.02538 0.15760  98  ILE A CG1 
678  C CG2 . ILE A 87  ? 0.50294 0.52324 0.42030 0.07484  -0.01125 0.17017  98  ILE A CG2 
679  C CD1 . ILE A 87  ? 0.47653 0.46463 0.42833 0.06567  -0.02093 0.14123  98  ILE A CD1 
680  N N   . LEU A 88  ? 0.49466 0.52519 0.35829 0.09823  -0.02180 0.13759  99  LEU A N   
681  C CA  . LEU A 88  ? 0.57580 0.62184 0.41211 0.10930  -0.01963 0.13795  99  LEU A CA  
682  C C   . LEU A 88  ? 0.58323 0.64484 0.41620 0.10898  -0.00740 0.14958  99  LEU A C   
683  O O   . LEU A 88  ? 0.65988 0.73913 0.47279 0.11833  -0.00376 0.15764  99  LEU A O   
684  C CB  . LEU A 88  ? 0.58750 0.62891 0.41147 0.11457  -0.02547 0.11601  99  LEU A CB  
685  C CG  . LEU A 88  ? 0.57845 0.60669 0.40698 0.11454  -0.03823 0.10364  99  LEU A CG  
686  C CD1 . LEU A 88  ? 0.48478 0.50960 0.30041 0.11987  -0.04514 0.08435  99  LEU A CD1 
687  C CD2 . LEU A 88  ? 0.50858 0.53972 0.32886 0.12068  -0.04522 0.11335  99  LEU A CD2 
688  N N   . SER A 89  ? 0.57286 0.62979 0.42574 0.09865  -0.00111 0.15037  100 SER A N   
689  C CA  . SER A 89  ? 0.55295 0.62527 0.40537 0.09757  0.01009  0.16031  100 SER A CA  
690  C C   . SER A 89  ? 0.56317 0.62647 0.44404 0.08384  0.01360  0.16649  100 SER A C   
691  O O   . SER A 89  ? 0.54582 0.59228 0.44062 0.07755  0.00967  0.15286  100 SER A O   
692  C CB  . SER A 89  ? 0.56429 0.64219 0.40074 0.10442  0.01283  0.14389  100 SER A CB  
693  O OG  . SER A 89  ? 0.62816 0.71858 0.46975 0.10155  0.02344  0.15100  100 SER A OG  
694  N N   . THR A 90  ? 0.51110 0.58643 0.40083 0.07950  0.02041  0.18721  101 THR A N   
695  C CA  . THR A 90  ? 0.59284 0.66015 0.50974 0.06667  0.02259  0.19387  101 THR A CA  
696  C C   . THR A 90  ? 0.66658 0.75358 0.58407 0.06540  0.03326  0.20415  101 THR A C   
697  O O   . THR A 90  ? 0.65892 0.76421 0.57435 0.06675  0.03764  0.21527  101 THR A O   
698  C CB  . THR A 90  ? 0.59943 0.65870 0.53449 0.05989  0.01742  0.21190  101 THR A CB  
699  O OG1 . THR A 90  ? 0.66560 0.70650 0.60263 0.06124  0.00743  0.20121  101 THR A OG1 
700  C CG2 . THR A 90  ? 0.57753 0.62820 0.54061 0.04719  0.01809  0.21879  101 THR A CG2 
701  N N   . LYS A 91  ? 0.55537 0.63765 0.48141 0.06060  0.03626  0.19215  102 LYS A N   
702  C CA  . LYS A 91  ? 0.55243 0.65275 0.48245 0.05858  0.04587  0.20079  102 LYS A CA  
703  C C   . LYS A 91  ? 0.63774 0.72498 0.59668 0.04475  0.04439  0.20294  102 LYS A C   
704  O O   . LYS A 91  ? 0.57567 0.64770 0.54044 0.04145  0.04173  0.18478  102 LYS A O   
705  C CB  . LYS A 91  ? 0.58620 0.69478 0.49715 0.06755  0.05038  0.18357  102 LYS A CB  
706  C CG  . LYS A 91  ? 0.78012 0.89870 0.66241 0.08223  0.04932  0.17604  102 LYS A CG  
707  C CD  . LYS A 91  ? 0.82787 0.96543 0.70869 0.08524  0.05196  0.18966  102 LYS A CD  
708  C CE  . LYS A 91  ? 0.91620 1.07637 0.80858 0.08285  0.06113  0.19957  102 LYS A CE  
709  N NZ  . LYS A 91  ? 0.75298 0.92326 0.66265 0.07567  0.06227  0.22106  102 LYS A NZ  
710  N N   . ASN A 92  ? 0.52699 0.61944 0.50539 0.03638  0.04458  0.22190  103 ASN A N   
711  C CA  . ASN A 92  ? 0.58658 0.66850 0.59216 0.02388  0.04238  0.22603  103 ASN A CA  
712  C C   . ASN A 92  ? 0.57426 0.67454 0.58360 0.02225  0.05067  0.22593  103 ASN A C   
713  O O   . ASN A 92  ? 0.49837 0.62108 0.49235 0.03056  0.05788  0.22557  103 ASN A O   
714  C CB  . ASN A 92  ? 0.53065 0.60741 0.55819 0.01501  0.03581  0.24165  103 ASN A CB  
715  C CG  . ASN A 92  ? 0.60569 0.66333 0.63124 0.01698  0.02672  0.24096  103 ASN A CG  
716  O OD1 . ASN A 92  ? 0.56971 0.60747 0.59430 0.01847  0.02136  0.22680  103 ASN A OD1 
717  N ND2 . ASN A 92  ? 0.50690 0.57161 0.53253 0.01750  0.02465  0.25361  103 ASN A ND2 
718  N N   . VAL A 93  ? 0.58741 0.67758 0.61751 0.01242  0.04872  0.22486  104 VAL A N   
719  C CA  . VAL A 93  ? 0.54376 0.65026 0.57994 0.01030  0.05541  0.22452  104 VAL A CA  
720  C C   . VAL A 93  ? 0.60218 0.72676 0.65619 0.00467  0.05601  0.24231  104 VAL A C   
721  O O   . VAL A 93  ? 0.53602 0.64974 0.61260 -0.00535 0.04829  0.25231  104 VAL A O   
722  C CB  . VAL A 93  ? 0.55383 0.64320 0.60508 0.00226  0.05252  0.21593  104 VAL A CB  
723  C CG1 . VAL A 93  ? 0.51699 0.62446 0.57515 0.00025  0.05884  0.21607  104 VAL A CG1 
724  C CG2 . VAL A 93  ? 0.52552 0.59782 0.56093 0.00849  0.04958  0.18919  104 VAL A CG2 
725  N N   . LYS A 94  ? 0.59289 0.74512 0.63731 0.01190  0.06432  0.24606  105 LYS A N   
726  C CA  . LYS A 94  ? 0.48686 0.66017 0.54951 0.00721  0.06577  0.26395  105 LYS A CA  
727  C C   . LYS A 94  ? 0.50644 0.67888 0.59280 -0.00288 0.06421  0.26538  105 LYS A C   
728  O O   . LYS A 94  ? 0.45157 0.61939 0.53239 -0.00135 0.06687  0.25175  105 LYS A O   
729  C CB  . LYS A 94  ? 0.60776 0.81204 0.65302 0.01978  0.07492  0.26680  105 LYS A CB  
730  C CG  . LYS A 94  ? 0.62738 0.83351 0.64711 0.03122  0.07585  0.26358  105 LYS A CG  
731  C CD  . LYS A 94  ? 0.78963 1.01753 0.78474 0.04704  0.08362  0.25441  105 LYS A CD  
732  C CE  . LYS A 94  ? 0.84009 1.09722 0.83284 0.05402  0.08812  0.26928  105 LYS A CE  
733  N NZ  . LYS A 94  ? 0.89298 1.14440 0.87786 0.05550  0.08420  0.27592  105 LYS A NZ  
734  N N   . PRO A 95  ? 0.43789 0.61440 0.55109 -0.01323 0.05909  0.28154  106 PRO A N   
735  C CA  . PRO A 95  ? 0.38651 0.55801 0.52357 -0.02356 0.05485  0.28179  106 PRO A CA  
736  C C   . PRO A 95  ? 0.41819 0.60948 0.54971 -0.01846 0.06333  0.27625  106 PRO A C   
737  O O   . PRO A 95  ? 0.40703 0.58744 0.54696 -0.02358 0.06107  0.26703  106 PRO A O   
738  C CB  . PRO A 95  ? 0.36423 0.54342 0.52870 -0.03314 0.04826  0.30265  106 PRO A CB  
739  C CG  . PRO A 95  ? 0.39226 0.59096 0.54509 -0.02583 0.05328  0.31477  106 PRO A CG  
740  C CD  . PRO A 95  ? 0.37376 0.55989 0.49739 -0.01598 0.05612  0.30039  106 PRO A CD  
741  N N   . GLU A 96  ? 0.36089 0.58047 0.47792 -0.00762 0.07248  0.28062  107 GLU A N   
742  C CA  . GLU A 96  ? 0.47401 0.71289 0.58523 -0.00107 0.07990  0.27497  107 GLU A CA  
743  C C   . GLU A 96  ? 0.43946 0.66547 0.52820 0.00640  0.08312  0.25253  107 GLU A C   
744  O O   . GLU A 96  ? 0.44274 0.67987 0.52762 0.01106  0.08779  0.24541  107 GLU A O   
745  C CB  . GLU A 96  ? 0.44696 0.71957 0.54859 0.01023  0.08778  0.28525  107 GLU A CB  
746  C CG  . GLU A 96  ? 0.47408 0.74923 0.54616 0.02384  0.09180  0.27783  107 GLU A CG  
747  C CD  . GLU A 96  ? 0.57850 0.85428 0.65378 0.02154  0.08871  0.29223  107 GLU A CD  
748  O OE1 . GLU A 96  ? 0.49959 0.76014 0.59645 0.00837  0.08105  0.30195  107 GLU A OE1 
749  O OE2 . GLU A 96  ? 0.66697 0.95801 0.72291 0.03350  0.09320  0.29322  107 GLU A OE2 
750  N N   . ASN A 97  ? 0.37780 0.58126 0.45241 0.00783  0.08026  0.24191  108 ASN A N   
751  C CA  . ASN A 97  ? 0.39810 0.58806 0.45295 0.01407  0.08216  0.22173  108 ASN A CA  
752  C C   . ASN A 97  ? 0.42626 0.58743 0.49227 0.00380  0.07554  0.21441  108 ASN A C   
753  O O   . ASN A 97  ? 0.42041 0.56753 0.47124 0.00794  0.07611  0.19933  108 ASN A O   
754  C CB  . ASN A 97  ? 0.48536 0.67496 0.51201 0.02654  0.08416  0.21437  108 ASN A CB  
755  C CG  . ASN A 97  ? 0.45808 0.67581 0.47191 0.03872  0.09014  0.21912  108 ASN A CG  
756  O OD1 . ASN A 97  ? 0.49648 0.73306 0.51344 0.04239  0.09467  0.21986  108 ASN A OD1 
757  N ND2 . ASN A 97  ? 0.55710 0.77803 0.55674 0.04561  0.08973  0.22240  108 ASN A ND2 
758  N N   . ARG A 98  ? 0.36637 0.51828 0.45907 -0.00895 0.06838  0.22443  109 ARG A N   
759  C CA  . ARG A 98  ? 0.44452 0.56787 0.54899 -0.01775 0.06037  0.21695  109 ARG A CA  
760  C C   . ARG A 98  ? 0.42267 0.54144 0.52872 -0.01927 0.06218  0.20374  109 ARG A C   
761  O O   . ARG A 98  ? 0.44399 0.53870 0.55360 -0.02291 0.05550  0.19051  109 ARG A O   
762  C CB  . ARG A 98  ? 0.36695 0.48092 0.49988 -0.02982 0.05005  0.22947  109 ARG A CB  
763  C CG  . ARG A 98  ? 0.38287 0.50917 0.53772 -0.03709 0.04851  0.23670  109 ARG A CG  
764  C CD  . ARG A 98  ? 0.43450 0.55426 0.61604 -0.04755 0.03746  0.25107  109 ARG A CD  
765  N NE  . ARG A 98  ? 0.38853 0.51724 0.59328 -0.05536 0.03367  0.25775  109 ARG A NE  
766  C CZ  . ARG A 98  ? 0.43682 0.59431 0.64785 -0.05431 0.03907  0.27169  109 ARG A CZ  
767  N NH1 . ARG A 98  ? 0.47020 0.65103 0.66553 -0.04517 0.04868  0.27953  109 ARG A NH1 
768  N NH2 . ARG A 98  ? 0.45550 0.61881 0.68919 -0.06197 0.03409  0.27776  109 ARG A NH2 
769  N N   . PHE A 99  ? 0.35784 0.49783 0.46055 -0.01505 0.06900  0.20273  110 PHE A N   
770  C CA  . PHE A 99  ? 0.37154 0.50937 0.47397 -0.01523 0.07121  0.18994  110 PHE A CA  
771  C C   . PHE A 99  ? 0.34826 0.49151 0.42256 -0.00228 0.07878  0.17542  110 PHE A C   
772  O O   . PHE A 99  ? 0.34719 0.48824 0.41855 -0.00051 0.07933  0.16153  110 PHE A O   
773  C CB  . PHE A 99  ? 0.38549 0.54126 0.50506 -0.01923 0.07187  0.19721  110 PHE A CB  
774  C CG  . PHE A 99  ? 0.40836 0.55536 0.55789 -0.03281 0.06192  0.20795  110 PHE A CG  
775  C CD1 . PHE A 99  ? 0.45750 0.57664 0.61887 -0.04131 0.05225  0.20176  110 PHE A CD1 
776  C CD2 . PHE A 99  ? 0.46632 0.63265 0.63249 -0.03629 0.06111  0.22372  110 PHE A CD2 
777  C CE1 . PHE A 99  ? 0.46364 0.57235 0.65194 -0.05256 0.04060  0.20932  110 PHE A CE1 
778  C CE2 . PHE A 99  ? 0.45346 0.61088 0.64781 -0.04857 0.05019  0.23332  110 PHE A CE2 
779  C CZ  . PHE A 99  ? 0.41772 0.54547 0.62253 -0.05642 0.03938  0.22521  110 PHE A CZ  
780  N N   . ASP A 100 ? 0.37850 0.52590 0.43160 0.00749  0.08168  0.17493  111 ASP A N   
781  C CA  . ASP A 100 ? 0.37431 0.52628 0.40057 0.02094  0.08628  0.15987  111 ASP A CA  
782  C C   . ASP A 100 ? 0.43739 0.56320 0.45646 0.02089  0.07949  0.13653  111 ASP A C   
783  O O   . ASP A 100 ? 0.40948 0.53602 0.41928 0.02616  0.08104  0.12331  111 ASP A O   
784  C CB  . ASP A 100 ? 0.43907 0.59809 0.44536 0.03117  0.08759  0.16256  111 ASP A CB  
785  C CG  . ASP A 100 ? 0.48668 0.67123 0.49541 0.03575  0.09096  0.17469  111 ASP A CG  
786  O OD1 . ASP A 100 ? 0.42261 0.62034 0.44736 0.03165  0.09279  0.18111  111 ASP A OD1 
787  O OD2 . ASP A 100 ? 0.52693 0.71908 0.52183 0.04377  0.09159  0.17814  111 ASP A OD2 
788  N N   . ASN A 101 ? 0.44345 0.54718 0.46674 0.01559  0.07186  0.13185  112 ASN A N   
789  C CA  . ASN A 101 ? 0.39131 0.47312 0.40948 0.01531  0.06584  0.11190  112 ASN A CA  
790  C C   . ASN A 101 ? 0.41805 0.48000 0.44767 0.00835  0.05791  0.11123  112 ASN A C   
791  O O   . ASN A 101 ? 0.42831 0.47926 0.44763 0.01202  0.05438  0.10387  112 ASN A O   
792  C CB  . ASN A 101 ? 0.43932 0.51960 0.43291 0.02627  0.06638  0.09916  112 ASN A CB  
793  C CG  . ASN A 101 ? 0.45928 0.54290 0.44045 0.03227  0.06620  0.10583  112 ASN A CG  
794  O OD1 . ASN A 101 ? 0.50382 0.60291 0.48716 0.03305  0.07038  0.12235  112 ASN A OD1 
795  N ND2 . ASN A 101 ? 0.57497 0.64533 0.54337 0.03656  0.06110  0.09362  112 ASN A ND2 
796  N N   . PRO A 102 ? 0.37061 0.42722 0.42203 -0.00116 0.05395  0.11817  113 PRO A N   
797  C CA  . PRO A 102 ? 0.32990 0.36620 0.39180 -0.00604 0.04513  0.11537  113 PRO A CA  
798  C C   . PRO A 102 ? 0.39900 0.41965 0.45494 -0.00413 0.04112  0.09491  113 PRO A C   
799  O O   . PRO A 102 ? 0.31677 0.33957 0.36901 -0.00330 0.04326  0.08506  113 PRO A O   
800  C CB  . PRO A 102 ? 0.32890 0.36383 0.41597 -0.01611 0.04072  0.12685  113 PRO A CB  
801  C CG  . PRO A 102 ? 0.40265 0.45281 0.49237 -0.01716 0.04638  0.12752  113 PRO A CG  
802  C CD  . PRO A 102 ? 0.32787 0.39586 0.39605 -0.00743 0.05602  0.12729  113 PRO A CD  
803  N N   . GLU A 103 ? 0.32213 0.32866 0.37710 -0.00290 0.03546  0.08955  114 GLU A N   
804  C CA  . GLU A 103 ? 0.35092 0.34596 0.40002 -0.00011 0.03226  0.07217  114 GLU A CA  
805  C C   . GLU A 103 ? 0.32618 0.31009 0.38971 -0.00473 0.02631  0.06499  114 GLU A C   
806  O O   . GLU A 103 ? 0.30709 0.28316 0.38624 -0.00935 0.02021  0.07146  114 GLU A O   
807  C CB  . GLU A 103 ? 0.35172 0.33870 0.39556 0.00380  0.02854  0.07009  114 GLU A CB  
808  C CG  . GLU A 103 ? 0.41268 0.40889 0.44199 0.00901  0.03230  0.07686  114 GLU A CG  
809  C CD  . GLU A 103 ? 0.47593 0.47861 0.48832 0.01440  0.03630  0.06725  114 GLU A CD  
810  O OE1 . GLU A 103 ? 0.49428 0.49147 0.50584 0.01433  0.03495  0.05464  114 GLU A OE1 
811  O OE2 . GLU A 103 ? 0.60225 0.61566 0.60211 0.01921  0.04018  0.07244  114 GLU A OE2 
812  N N   . ILE A 104 ? 0.32850 0.31103 0.38662 -0.00302 0.02699  0.05140  115 ILE A N   
813  C CA  . ILE A 104 ? 0.31438 0.28750 0.38263 -0.00533 0.02120  0.04234  115 ILE A CA  
814  C C   . ILE A 104 ? 0.29028 0.25877 0.34985 -0.00009 0.02014  0.02796  115 ILE A C   
815  O O   . ILE A 104 ? 0.24534 0.22035 0.29212 0.00316  0.02495  0.02401  115 ILE A O   
816  C CB  . ILE A 104 ? 0.21979 0.19949 0.29257 -0.00908 0.02316  0.04208  115 ILE A CB  
817  C CG1 . ILE A 104 ? 0.24196 0.21109 0.32553 -0.01113 0.01539  0.03302  115 ILE A CG1 
818  C CG2 . ILE A 104 ? 0.20399 0.19317 0.26176 -0.00542 0.02996  0.03570  115 ILE A CG2 
819  C CD1 . ILE A 104 ? 0.28199 0.25689 0.37435 -0.01617 0.01523  0.03529  115 ILE A CD1 
820  N N   . ASN A 105 ? 0.28593 0.24366 0.35324 0.00114  0.01317  0.02073  116 ASN A N   
821  C CA  . ASN A 105 ? 0.32207 0.27869 0.38307 0.00673  0.01241  0.00762  116 ASN A CA  
822  C C   . ASN A 105 ? 0.32466 0.28845 0.37937 0.00667  0.01610  0.00030  116 ASN A C   
823  O O   . ASN A 105 ? 0.33007 0.29441 0.38973 0.00289  0.01546  0.00128  116 ASN A O   
824  C CB  . ASN A 105 ? 0.25830 0.20270 0.32919 0.00958  0.00347  0.00086  116 ASN A CB  
825  C CG  . ASN A 105 ? 0.34827 0.29503 0.41303 0.01683  0.00313  -0.01288 116 ASN A CG  
826  O OD1 . ASN A 105 ? 0.29277 0.24137 0.35620 0.01813  0.00240  -0.02127 116 ASN A OD1 
827  N ND2 . ASN A 105 ? 0.28113 0.22952 0.34256 0.02194  0.00360  -0.01447 116 ASN A ND2 
828  N N   . ARG A 106 ? 0.24549 0.21542 0.29045 0.01055  0.01949  -0.00602 117 ARG A N   
829  C CA  . ARG A 106 ? 0.27326 0.25066 0.31163 0.01027  0.02312  -0.01084 117 ARG A CA  
830  C C   . ARG A 106 ? 0.29540 0.27069 0.33762 0.01171  0.01932  -0.01966 117 ARG A C   
831  O O   . ARG A 106 ? 0.26907 0.24830 0.30939 0.00976  0.02073  -0.02138 117 ARG A O   
832  C CB  . ARG A 106 ? 0.25015 0.23474 0.27963 0.01315  0.02647  -0.01333 117 ARG A CB  
833  C CG  . ARG A 106 ? 0.28358 0.27078 0.30641 0.01204  0.02941  -0.00651 117 ARG A CG  
834  C CD  . ARG A 106 ? 0.27589 0.26815 0.29388 0.01435  0.02988  -0.00886 117 ARG A CD  
835  N NE  . ARG A 106 ? 0.26115 0.25379 0.27282 0.01421  0.03025  -0.00407 117 ARG A NE  
836  C CZ  . ARG A 106 ? 0.28131 0.27616 0.28591 0.01325  0.03142  -0.00332 117 ARG A CZ  
837  N NH1 . ARG A 106 ? 0.25119 0.24846 0.25468 0.01165  0.03300  -0.00578 117 ARG A NH1 
838  N NH2 . ARG A 106 ? 0.21508 0.20908 0.21324 0.01466  0.03000  -0.00064 117 ARG A NH2 
839  N N   . ASN A 107 ? 0.27167 0.24091 0.31851 0.01618  0.01387  -0.02609 118 ASN A N   
840  C CA  . ASN A 107 ? 0.28391 0.25003 0.33343 0.01899  0.00863  -0.03573 118 ASN A CA  
841  C C   . ASN A 107 ? 0.27957 0.23679 0.33977 0.01332  0.00300  -0.03242 118 ASN A C   
842  O O   . ASN A 107 ? 0.29078 0.24827 0.35190 0.01276  0.00026  -0.03770 118 ASN A O   
843  C CB  . ASN A 107 ? 0.32987 0.29199 0.38078 0.02732  0.00340  -0.04482 118 ASN A CB  
844  C CG  . ASN A 107 ? 0.37636 0.35195 0.41828 0.03321  0.00921  -0.04824 118 ASN A CG  
845  O OD1 . ASN A 107 ? 0.44572 0.43082 0.48148 0.03735  0.01105  -0.05485 118 ASN A OD1 
846  N ND2 . ASN A 107 ? 0.39561 0.37323 0.43753 0.03344  0.01177  -0.04275 118 ASN A ND2 
847  N N   . ASP A 108 ? 0.26336 0.21388 0.33254 0.00877  0.00093  -0.02258 119 ASP A N   
848  C CA  . ASP A 108 ? 0.26316 0.20811 0.34524 0.00194  -0.00406 -0.01620 119 ASP A CA  
849  C C   . ASP A 108 ? 0.29077 0.24686 0.36983 -0.00268 0.00237  -0.01137 119 ASP A C   
850  O O   . ASP A 108 ? 0.30431 0.25946 0.39041 -0.00579 -0.00178 -0.01314 119 ASP A O   
851  C CB  . ASP A 108 ? 0.23764 0.17662 0.33003 -0.00234 -0.00633 -0.00348 119 ASP A CB  
852  C CG  . ASP A 108 ? 0.28614 0.21010 0.38637 0.00145  -0.01635 -0.00819 119 ASP A CG  
853  O OD1 . ASP A 108 ? 0.39052 0.30671 0.49223 0.00633  -0.02400 -0.02122 119 ASP A OD1 
854  O OD2 . ASP A 108 ? 0.32779 0.24775 0.43220 0.00041  -0.01713 0.00080  119 ASP A OD2 
855  N N   . LEU A 109 ? 0.30082 0.26709 0.36950 -0.00246 0.01148  -0.00611 120 LEU A N   
856  C CA  . LEU A 109 ? 0.32352 0.30023 0.38822 -0.00509 0.01732  -0.00246 120 LEU A CA  
857  C C   . LEU A 109 ? 0.32727 0.30666 0.38663 -0.00301 0.01667  -0.01271 120 LEU A C   
858  O O   . LEU A 109 ? 0.38663 0.36974 0.45014 -0.00604 0.01613  -0.01180 120 LEU A O   
859  C CB  . LEU A 109 ? 0.23962 0.22417 0.29269 -0.00324 0.02512  0.00258  120 LEU A CB  
860  C CG  . LEU A 109 ? 0.32259 0.31737 0.37084 -0.00423 0.03061  0.00608  120 LEU A CG  
861  C CD1 . LEU A 109 ? 0.23765 0.23701 0.29790 -0.00892 0.03057  0.01623  120 LEU A CD1 
862  C CD2 . LEU A 109 ? 0.24815 0.24782 0.28360 -0.00069 0.03590  0.00825  120 LEU A CD2 
863  N N   . ARG A 110 ? 0.29462 0.27399 0.34516 0.00235  0.01684  -0.02160 121 ARG A N   
864  C CA  . ARG A 110 ? 0.28997 0.27314 0.33516 0.00502  0.01587  -0.03052 121 ARG A CA  
865  C C   . ARG A 110 ? 0.30266 0.27905 0.35720 0.00417  0.00739  -0.03590 121 ARG A C   
866  O O   . ARG A 110 ? 0.30701 0.28714 0.36154 0.00269  0.00644  -0.03798 121 ARG A O   
867  C CB  . ARG A 110 ? 0.25123 0.23778 0.28758 0.01148  0.01711  -0.03767 121 ARG A CB  
868  C CG  . ARG A 110 ? 0.28943 0.28146 0.31992 0.01557  0.01567  -0.04652 121 ARG A CG  
869  C CD  . ARG A 110 ? 0.30319 0.30399 0.32520 0.02196  0.01877  -0.05073 121 ARG A CD  
870  N NE  . ARG A 110 ? 0.37427 0.38576 0.38872 0.02018  0.02492  -0.04616 121 ARG A NE  
871  C CZ  . ARG A 110 ? 0.39074 0.41344 0.39914 0.02385  0.02831  -0.04663 121 ARG A CZ  
872  N NH1 . ARG A 110 ? 0.32198 0.34921 0.32973 0.03074  0.02744  -0.05205 121 ARG A NH1 
873  N NH2 . ARG A 110 ? 0.31494 0.34525 0.31874 0.02083  0.03221  -0.04102 121 ARG A NH2 
874  N N   . ALA A 111 ? 0.23354 0.19892 0.29697 0.00507  -0.00007 -0.03811 122 ALA A N   
875  C CA  . ALA A 111 ? 0.34104 0.29705 0.41464 0.00453  -0.01092 -0.04430 122 ALA A CA  
876  C C   . ALA A 111 ? 0.28318 0.24017 0.36927 -0.00413 -0.01267 -0.03532 122 ALA A C   
877  O O   . ALA A 111 ? 0.31433 0.26940 0.40548 -0.00521 -0.01939 -0.04057 122 ALA A O   
878  C CB  . ALA A 111 ? 0.28228 0.22401 0.36452 0.00708  -0.02001 -0.04748 122 ALA A CB  
879  N N   . ILE A 112 ? 0.31500 0.27625 0.40659 -0.00981 -0.00710 -0.02158 123 ILE A N   
880  C CA  . ILE A 112 ? 0.33902 0.30617 0.44287 -0.01738 -0.00691 -0.01113 123 ILE A CA  
881  C C   . ILE A 112 ? 0.27942 0.25742 0.37552 -0.01657 -0.00235 -0.01454 123 ILE A C   
882  O O   . ILE A 112 ? 0.28799 0.26758 0.39379 -0.02023 -0.00734 -0.01451 123 ILE A O   
883  C CB  . ILE A 112 ? 0.32691 0.30120 0.43390 -0.02109 0.00045  0.00425  123 ILE A CB  
884  C CG1 . ILE A 112 ? 0.36382 0.32743 0.48291 -0.02380 -0.00576 0.01085  123 ILE A CG1 
885  C CG2 . ILE A 112 ? 0.36748 0.35448 0.48360 -0.02671 0.00392  0.01511  123 ILE A CG2 
886  C CD1 . ILE A 112 ? 0.37478 0.34747 0.49361 -0.02594 0.00231  0.02614  123 ILE A CD1 
887  N N   . LEU A 113 ? 0.24989 0.23498 0.32946 -0.01193 0.00617  -0.01717 124 LEU A N   
888  C CA  . LEU A 113 ? 0.28409 0.27873 0.35606 -0.01098 0.01036  -0.01917 124 LEU A CA  
889  C C   . LEU A 113 ? 0.26951 0.26142 0.33846 -0.00805 0.00399  -0.03084 124 LEU A C   
890  O O   . LEU A 113 ? 0.27367 0.27002 0.34631 -0.00999 0.00182  -0.03137 124 LEU A O   
891  C CB  . LEU A 113 ? 0.20351 0.20407 0.26031 -0.00725 0.01905  -0.01827 124 LEU A CB  
892  C CG  . LEU A 113 ? 0.32950 0.33400 0.38772 -0.00892 0.02471  -0.00737 124 LEU A CG  
893  C CD1 . LEU A 113 ? 0.24969 0.25574 0.29398 -0.00487 0.03027  -0.00785 124 LEU A CD1 
894  C CD2 . LEU A 113 ? 0.27986 0.29457 0.34372 -0.01146 0.02775  0.00010  124 LEU A CD2 
895  N N   . LEU A 114 ? 0.24595 0.23188 0.30808 -0.00252 0.00071  -0.04029 125 LEU A N   
896  C CA  . LEU A 114 ? 0.29727 0.28193 0.35472 0.00219  -0.00574 -0.05212 125 LEU A CA  
897  C C   . LEU A 114 ? 0.32838 0.30521 0.40038 -0.00131 -0.01703 -0.05472 125 LEU A C   
898  O O   . LEU A 114 ? 0.34152 0.32119 0.41258 -0.00069 -0.02128 -0.05991 125 LEU A O   
899  C CB  . LEU A 114 ? 0.31076 0.29216 0.35941 0.01025  -0.00741 -0.06154 125 LEU A CB  
900  C CG  . LEU A 114 ? 0.40097 0.39126 0.43666 0.01415  0.00202  -0.05989 125 LEU A CG  
901  C CD1 . LEU A 114 ? 0.42332 0.41192 0.45406 0.02249  -0.00056 -0.06867 125 LEU A CD1 
902  C CD2 . LEU A 114 ? 0.32944 0.33139 0.35454 0.01512  0.00712  -0.05963 125 LEU A CD2 
903  N N   . ASN A 115 ? 0.28230 0.24871 0.36868 -0.00516 -0.02320 -0.05087 126 ASN A N   
904  C CA  . ASN A 115 ? 0.29863 0.25587 0.40192 -0.00951 -0.03619 -0.05255 126 ASN A CA  
905  C C   . ASN A 115 ? 0.35058 0.31739 0.46397 -0.01693 -0.03477 -0.04370 126 ASN A C   
906  O O   . ASN A 115 ? 0.33421 0.29738 0.45816 -0.01947 -0.04527 -0.04752 126 ASN A O   
907  C CB  . ASN A 115 ? 0.33013 0.27470 0.44948 -0.01379 -0.04308 -0.04659 126 ASN A CB  
908  C CG  . ASN A 115 ? 0.43100 0.36313 0.54384 -0.00539 -0.04905 -0.05817 126 ASN A CG  
909  O OD1 . ASN A 115 ? 0.53507 0.46866 0.63278 0.00401  -0.04951 -0.07170 126 ASN A OD1 
910  N ND2 . ASN A 115 ? 0.40941 0.33059 0.53387 -0.00815 -0.05364 -0.05227 126 ASN A ND2 
911  N N   . SER A 116 ? 0.25493 0.23430 0.36551 -0.01971 -0.02268 -0.03242 127 SER A N   
912  C CA  . SER A 116 ? 0.28685 0.27792 0.40646 -0.02507 -0.02027 -0.02400 127 SER A CA  
913  C C   . SER A 116 ? 0.26937 0.26781 0.37684 -0.02090 -0.01849 -0.03155 127 SER A C   
914  O O   . SER A 116 ? 0.29404 0.30205 0.40900 -0.02429 -0.01779 -0.02633 127 SER A O   
915  C CB  . SER A 116 ? 0.23724 0.23970 0.35704 -0.02743 -0.00849 -0.01013 127 SER A CB  
916  O OG  . SER A 116 ? 0.27253 0.28048 0.37243 -0.02134 0.00097  -0.01367 127 SER A OG  
917  N N   . LEU A 117 ? 0.33307 0.32899 0.42271 -0.01352 -0.01753 -0.04249 128 LEU A N   
918  C CA  . LEU A 117 ? 0.31086 0.31450 0.38829 -0.00957 -0.01557 -0.04786 128 LEU A CA  
919  C C   . LEU A 117 ? 0.38719 0.38554 0.46550 -0.00687 -0.02755 -0.05945 128 LEU A C   
920  O O   . LEU A 117 ? 0.34455 0.33175 0.42598 -0.00468 -0.03646 -0.06719 128 LEU A O   
921  C CB  . LEU A 117 ? 0.29044 0.29752 0.34843 -0.00337 -0.00728 -0.05074 128 LEU A CB  
922  C CG  . LEU A 117 ? 0.26064 0.27262 0.31470 -0.00473 0.00338  -0.04121 128 LEU A CG  
923  C CD1 . LEU A 117 ? 0.22217 0.23671 0.25984 0.00051  0.00873  -0.04438 128 LEU A CD1 
924  C CD2 . LEU A 117 ? 0.22903 0.24998 0.28696 -0.00759 0.00726  -0.03384 128 LEU A CD2 
925  N N   A GLU A 118 ? 0.33993 0.34581 0.41512 -0.00622 -0.02870 -0.06123 129 GLU A N   
926  N N   B GLU A 118 ? 0.34006 0.34600 0.41522 -0.00623 -0.02863 -0.06118 129 GLU A N   
927  C CA  A GLU A 118 ? 0.36524 0.36735 0.43755 -0.00205 -0.04010 -0.07331 129 GLU A CA  
928  C CA  B GLU A 118 ? 0.36527 0.36784 0.43676 -0.00183 -0.03966 -0.07330 129 GLU A CA  
929  C C   A GLU A 118 ? 0.36304 0.36378 0.41580 0.00777  -0.03931 -0.08402 129 GLU A C   
930  C C   B GLU A 118 ? 0.36343 0.36379 0.41629 0.00780  -0.03927 -0.08404 129 GLU A C   
931  O O   A GLU A 118 ? 0.39779 0.40449 0.43833 0.01056  -0.02869 -0.08060 129 GLU A O   
932  O O   B GLU A 118 ? 0.39818 0.40368 0.43942 0.01056  -0.02888 -0.08076 129 GLU A O   
933  C CB  A GLU A 118 ? 0.37910 0.39110 0.45003 -0.00257 -0.04063 -0.07233 129 GLU A CB  
934  C CB  B GLU A 118 ? 0.37903 0.39204 0.44673 -0.00159 -0.03911 -0.07252 129 GLU A CB  
935  C CG  A GLU A 118 ? 0.42132 0.43815 0.51292 -0.01120 -0.04194 -0.06205 129 GLU A CG  
936  C CG  B GLU A 118 ? 0.42049 0.43738 0.50833 -0.00950 -0.04298 -0.06475 129 GLU A CG  
937  C CD  A GLU A 118 ? 0.39437 0.40271 0.50608 -0.01625 -0.05653 -0.06468 129 GLU A CD  
938  C CD  B GLU A 118 ? 0.40668 0.43472 0.48970 -0.00823 -0.04129 -0.06354 129 GLU A CD  
939  O OE1 A GLU A 118 ? 0.44799 0.44859 0.55528 -0.01174 -0.06832 -0.07746 129 GLU A OE1 
940  O OE1 B GLU A 118 ? 0.41217 0.44185 0.47852 -0.00155 -0.04276 -0.07156 129 GLU A OE1 
941  O OE2 A GLU A 118 ? 0.45077 0.46067 0.58306 -0.02451 -0.05683 -0.05359 129 GLU A OE2 
942  O OE2 B GLU A 118 ? 0.37828 0.41473 0.47403 -0.01328 -0.03825 -0.05397 129 GLU A OE2 
943  N N   . ASN A 119 ? 0.40063 0.39421 0.45113 0.01350  -0.05128 -0.09705 130 ASN A N   
944  C CA  . ASN A 119 ? 0.34119 0.33604 0.37329 0.02471  -0.05096 -0.10793 130 ASN A CA  
945  C C   . ASN A 119 ? 0.37025 0.38095 0.38426 0.02907  -0.04085 -0.10527 130 ASN A C   
946  O O   . ASN A 119 ? 0.39745 0.41491 0.41109 0.02629  -0.04027 -0.10142 130 ASN A O   
947  C CB  . ASN A 119 ? 0.48671 0.47271 0.51759 0.03192  -0.06685 -0.12381 130 ASN A CB  
948  C CG  . ASN A 119 ? 0.48768 0.45534 0.53628 0.02870  -0.07876 -0.12729 130 ASN A CG  
949  O OD1 . ASN A 119 ? 0.45605 0.41864 0.51313 0.02408  -0.07376 -0.11950 130 ASN A OD1 
950  N ND2 . ASN A 119 ? 0.45867 0.41562 0.51282 0.03149  -0.09576 -0.13916 130 ASN A ND2 
951  N N   . ASP A 120 ? 0.33592 0.35306 0.33678 0.03525  -0.03286 -0.10570 131 ASP A N   
952  C CA  . ASP A 120 ? 0.41748 0.45034 0.40235 0.03927  -0.02386 -0.10171 131 ASP A CA  
953  C C   . ASP A 120 ? 0.38686 0.42431 0.37555 0.03079  -0.01488 -0.08775 131 ASP A C   
954  O O   . ASP A 120 ? 0.41882 0.46660 0.39848 0.03180  -0.01100 -0.08346 131 ASP A O   
955  C CB  . ASP A 120 ? 0.41175 0.45194 0.38486 0.04671  -0.03039 -0.11026 131 ASP A CB  
956  C CG  . ASP A 120 ? 0.56779 0.60493 0.53324 0.05816  -0.03955 -0.12598 131 ASP A CG  
957  O OD1 . ASP A 120 ? 0.57902 0.61771 0.53985 0.06386  -0.03564 -0.12853 131 ASP A OD1 
958  O OD2 . ASP A 120 ? 0.55414 0.58722 0.51839 0.06208  -0.05136 -0.13630 131 ASP A OD2 
959  N N   . THR A 121 ? 0.27379 0.30378 0.27555 0.02311  -0.01219 -0.08056 132 THR A N   
960  C CA  . THR A 121 ? 0.30014 0.33444 0.30313 0.01756  -0.00368 -0.06892 132 THR A CA  
961  C C   . THR A 121 ? 0.31538 0.35518 0.30889 0.01967  0.00476  -0.06435 132 THR A C   
962  O O   . THR A 121 ? 0.28235 0.32912 0.26970 0.01887  0.00963  -0.05779 132 THR A O   
963  C CB  . THR A 121 ? 0.26852 0.29589 0.28690 0.01027  -0.00309 -0.06255 132 THR A CB  
964  O OG1 . THR A 121 ? 0.28105 0.30564 0.31107 0.00725  -0.01122 -0.06480 132 THR A OG1 
965  C CG2 . THR A 121 ? 0.20936 0.24125 0.22703 0.00689  0.00497  -0.05246 132 THR A CG2 
966  N N   . VAL A 122 ? 0.28909 0.32563 0.28267 0.02225  0.00551  -0.06743 133 VAL A N   
967  C CA  . VAL A 122 ? 0.28341 0.32645 0.26995 0.02453  0.01251  -0.06350 133 VAL A CA  
968  C C   . VAL A 122 ? 0.29937 0.35427 0.27374 0.03299  0.01224  -0.06905 133 VAL A C   
969  O O   . VAL A 122 ? 0.32726 0.38060 0.29922 0.03952  0.00606  -0.07977 133 VAL A O   
970  C CB  . VAL A 122 ? 0.32250 0.35767 0.31559 0.02390  0.01331  -0.06383 133 VAL A CB  
971  C CG1 . VAL A 122 ? 0.24711 0.28996 0.23477 0.02582  0.02003  -0.05921 133 VAL A CG1 
972  C CG2 . VAL A 122 ? 0.24861 0.27457 0.25301 0.01630  0.01376  -0.05740 133 VAL A CG2 
973  N N   . ILE A 123 ? 0.23232 0.29963 0.19921 0.03333  0.01822  -0.06150 134 ILE A N   
974  C CA  . ILE A 123 ? 0.24426 0.32783 0.19972 0.04149  0.02021  -0.06334 134 ILE A CA  
975  C C   . ILE A 123 ? 0.27153 0.36169 0.22793 0.04266  0.02627  -0.05880 134 ILE A C   
976  O O   . ILE A 123 ? 0.28006 0.37232 0.23993 0.03647  0.03110  -0.04778 134 ILE A O   
977  C CB  . ILE A 123 ? 0.29451 0.39004 0.24274 0.04056  0.02234  -0.05546 134 ILE A CB  
978  C CG1 . ILE A 123 ? 0.25930 0.34579 0.21085 0.03590  0.01742  -0.05583 134 ILE A CG1 
979  C CG2 . ILE A 123 ? 0.21385 0.32783 0.14877 0.05106  0.02270  -0.05954 134 ILE A CG2 
980  C CD1 . ILE A 123 ? 0.30396 0.38695 0.25322 0.04116  0.00930  -0.06822 134 ILE A CD1 
981  N N   . TRP A 124 ? 0.26134 0.35415 0.21538 0.05092  0.02497  -0.06770 135 TRP A N   
982  C CA  . TRP A 124 ? 0.31157 0.41101 0.26789 0.05307  0.03000  -0.06460 135 TRP A CA  
983  C C   . TRP A 124 ? 0.36884 0.49274 0.31784 0.05739  0.03657  -0.05696 135 TRP A C   
984  O O   . TRP A 124 ? 0.30831 0.44464 0.24816 0.06128  0.03673  -0.05636 135 TRP A O   
985  C CB  . TRP A 124 ? 0.32679 0.41964 0.28391 0.06151  0.02517  -0.07759 135 TRP A CB  
986  C CG  . TRP A 124 ? 0.38211 0.45188 0.34918 0.05573  0.01841  -0.08202 135 TRP A CG  
987  C CD1 . TRP A 124 ? 0.33375 0.39202 0.30240 0.05573  0.00997  -0.09011 135 TRP A CD1 
988  C CD2 . TRP A 124 ? 0.31271 0.37000 0.29049 0.04864  0.01940  -0.07685 135 TRP A CD2 
989  N NE1 . TRP A 124 ? 0.33436 0.37503 0.31556 0.04841  0.00618  -0.08885 135 TRP A NE1 
990  C CE2 . TRP A 124 ? 0.30628 0.34637 0.29214 0.04444  0.01224  -0.08079 135 TRP A CE2 
991  C CE3 . TRP A 124 ? 0.34520 0.40512 0.32683 0.04549  0.02521  -0.06873 135 TRP A CE3 
992  C CZ2 . TRP A 124 ? 0.33235 0.35955 0.32901 0.03768  0.01173  -0.07596 135 TRP A CZ2 
993  C CZ3 . TRP A 124 ? 0.32788 0.37339 0.31877 0.03944  0.02403  -0.06561 135 TRP A CZ3 
994  C CH2 . TRP A 124 ? 0.35930 0.38939 0.35715 0.03579  0.01784  -0.06877 135 TRP A CH2 
995  N N   . ASP A 125 ? 0.29133 0.42340 0.24528 0.05646  0.04184  -0.04991 136 ASP A N   
996  C CA  . ASP A 125 ? 0.30044 0.45844 0.25110 0.05962  0.04847  -0.04006 136 ASP A CA  
997  C C   . ASP A 125 ? 0.27142 0.43558 0.22091 0.05208  0.05003  -0.02725 136 ASP A C   
998  O O   . ASP A 125 ? 0.24719 0.43169 0.18888 0.05673  0.05277  -0.02244 136 ASP A O   
999  C CB  . ASP A 125 ? 0.32161 0.49633 0.26203 0.07376  0.04848  -0.04873 136 ASP A CB  
1000 C CG  . ASP A 125 ? 0.37421 0.57293 0.31591 0.07553  0.05385  -0.03609 136 ASP A CG  
1001 O OD1 . ASP A 125 ? 0.38730 0.59240 0.33806 0.06730  0.05861  -0.02274 136 ASP A OD1 
1002 O OD2 . ASP A 125 ? 0.39208 0.60396 0.32651 0.08519  0.05268  -0.03920 136 ASP A OD2 
1003 N N   . ARG A 126 ? 0.26312 0.40929 0.21990 0.04117  0.04767  -0.02202 137 ARG A N   
1004 C CA  . ARG A 126 ? 0.26846 0.41532 0.22585 0.03362  0.04729  -0.01057 137 ARG A CA  
1005 C C   . ARG A 126 ? 0.23875 0.37821 0.20703 0.02413  0.04763  -0.00012 137 ARG A C   
1006 O O   . ARG A 126 ? 0.29504 0.41462 0.26787 0.01916  0.04450  -0.00314 137 ARG A O   
1007 C CB  . ARG A 126 ? 0.29203 0.42309 0.24644 0.03177  0.04210  -0.01698 137 ARG A CB  
1008 C CG  . ARG A 126 ? 0.28845 0.42784 0.23177 0.04046  0.04001  -0.02573 137 ARG A CG  
1009 C CD  . ARG A 126 ? 0.27250 0.43503 0.20832 0.04329  0.04342  -0.01560 137 ARG A CD  
1010 N NE  . ARG A 126 ? 0.31237 0.48365 0.23549 0.05273  0.04089  -0.02438 137 ARG A NE  
1011 C CZ  . ARG A 126 ? 0.39713 0.57945 0.31165 0.06465  0.04121  -0.03513 137 ARG A CZ  
1012 N NH1 . ARG A 126 ? 0.31964 0.50607 0.23769 0.06861  0.04438  -0.03804 137 ARG A NH1 
1013 N NH2 . ARG A 126 ? 0.36194 0.55002 0.26460 0.07322  0.03705  -0.04347 137 ARG A NH2 
1014 N N   . LYS A 127 ? 0.23686 0.39334 0.20965 0.02211  0.05099  0.01224  138 LYS A N   
1015 C CA  . LYS A 127 ? 0.25579 0.40585 0.23972 0.01278  0.04935  0.02303  138 LYS A CA  
1016 C C   . LYS A 127 ? 0.26918 0.41828 0.25471 0.00586  0.04611  0.03478  138 LYS A C   
1017 O O   . LYS A 127 ? 0.25440 0.42343 0.23961 0.00584  0.04838  0.04599  138 LYS A O   
1018 C CB  . LYS A 127 ? 0.25322 0.42220 0.24453 0.01348  0.05339  0.03089  138 LYS A CB  
1019 C CG  . LYS A 127 ? 0.26566 0.42741 0.26998 0.00359  0.04985  0.04165  138 LYS A CG  
1020 C CD  . LYS A 127 ? 0.32367 0.51046 0.33731 0.00296  0.05361  0.05402  138 LYS A CD  
1021 C CE  . LYS A 127 ? 0.55863 0.73788 0.58636 -0.00524 0.04919  0.06126  138 LYS A CE  
1022 N NZ  . LYS A 127 ? 0.59304 0.75971 0.62878 -0.01617 0.04130  0.07238  138 LYS A NZ  
1023 N N   . LEU A 128 ? 0.21575 0.34276 0.20278 0.00083  0.04071  0.03248  139 LEU A N   
1024 C CA  . LEU A 128 ? 0.29541 0.41806 0.28483 -0.00522 0.03596  0.04270  139 LEU A CA  
1025 C C   . LEU A 128 ? 0.28673 0.41410 0.28801 -0.01279 0.03333  0.05765  139 LEU A C   
1026 O O   . LEU A 128 ? 0.23730 0.35584 0.24571 -0.01579 0.03122  0.05684  139 LEU A O   
1027 C CB  . LEU A 128 ? 0.22480 0.32339 0.21300 -0.00687 0.03064  0.03522  139 LEU A CB  
1028 C CG  . LEU A 128 ? 0.28793 0.37944 0.27810 -0.01155 0.02445  0.04380  139 LEU A CG  
1029 C CD1 . LEU A 128 ? 0.23110 0.33161 0.21314 -0.00795 0.02553  0.04368  139 LEU A CD1 
1030 C CD2 . LEU A 128 ? 0.20664 0.27500 0.19837 -0.01293 0.01863  0.03779  139 LEU A CD2 
1031 N N   . VAL A 129 ? 0.25213 0.39440 0.25628 -0.01604 0.03291  0.07212  140 VAL A N   
1032 C CA  . VAL A 129 ? 0.30012 0.44696 0.31841 -0.02480 0.02869  0.08877  140 VAL A CA  
1033 C C   . VAL A 129 ? 0.23925 0.37090 0.26245 -0.03190 0.01913  0.09766  140 VAL A C   
1034 O O   . VAL A 129 ? 0.26165 0.38521 0.29780 -0.03985 0.01152  0.10727  140 VAL A O   
1035 C CB  . VAL A 129 ? 0.32077 0.50075 0.34343 -0.02427 0.03536  0.10290  140 VAL A CB  
1036 C CG1 . VAL A 129 ? 0.27988 0.47401 0.29759 -0.01553 0.04383  0.09267  140 VAL A CG1 
1037 C CG2 . VAL A 129 ? 0.27580 0.47218 0.29115 -0.02202 0.03777  0.11118  140 VAL A CG2 
1038 N N   . MET A 130 ? 0.24204 0.36805 0.25614 -0.02907 0.01790  0.09418  141 MET A N   
1039 C CA  . MET A 130 ? 0.27442 0.38522 0.29391 -0.03505 0.00788  0.10259  141 MET A CA  
1040 C C   . MET A 130 ? 0.29761 0.39497 0.30611 -0.02988 0.00614  0.09158  141 MET A C   
1041 O O   . MET A 130 ? 0.29370 0.40097 0.29116 -0.02312 0.01272  0.08348  141 MET A O   
1042 C CB  . MET A 130 ? 0.35075 0.48063 0.37807 -0.04098 0.00663  0.12426  141 MET A CB  
1043 C CG  . MET A 130 ? 0.48290 0.60347 0.50780 -0.04238 -0.00022 0.12971  141 MET A CG  
1044 S SD  . MET A 130 ? 0.71844 0.86500 0.75004 -0.04808 -0.00009 0.15584  141 MET A SD  
1045 C CE  . MET A 130 ? 0.63404 0.77486 0.68827 -0.05993 -0.00852 0.17037  141 MET A CE  
1046 N N   . LEU A 131 ? 0.27935 0.35421 0.29162 -0.03263 -0.00374 0.09112  142 LEU A N   
1047 C CA  . LEU A 131 ? 0.29290 0.35555 0.29767 -0.02830 -0.00695 0.08339  142 LEU A CA  
1048 C C   . LEU A 131 ? 0.28780 0.34695 0.29804 -0.03299 -0.01574 0.09768  142 LEU A C   
1049 O O   . LEU A 131 ? 0.37726 0.43114 0.39936 -0.04025 -0.02348 0.11008  142 LEU A O   
1050 C CB  . LEU A 131 ? 0.26215 0.30170 0.26567 -0.02509 -0.01123 0.06923  142 LEU A CB  
1051 C CG  . LEU A 131 ? 0.28784 0.32950 0.28562 -0.02015 -0.00303 0.05530  142 LEU A CG  
1052 C CD1 . LEU A 131 ? 0.34533 0.36712 0.34370 -0.01802 -0.00750 0.04548  142 LEU A CD1 
1053 C CD2 . LEU A 131 ? 0.28401 0.33388 0.27253 -0.01432 0.00303  0.04700  142 LEU A CD2 
1054 N N   . GLU A 132 ? 0.32451 0.38592 0.32714 -0.02908 -0.01562 0.09631  143 GLU A N   
1055 C CA  . GLU A 132 ? 0.32273 0.37770 0.33017 -0.03271 -0.02512 0.10884  143 GLU A CA  
1056 C C   . GLU A 132 ? 0.36269 0.40490 0.36280 -0.02626 -0.02856 0.09794  143 GLU A C   
1057 O O   . GLU A 132 ? 0.33223 0.38533 0.32229 -0.02055 -0.02179 0.09024  143 GLU A O   
1058 C CB  . GLU A 132 ? 0.37815 0.45813 0.38573 -0.03594 -0.02142 0.12670  143 GLU A CB  
1059 C CG  . GLU A 132 ? 0.42665 0.50080 0.43963 -0.04014 -0.03162 0.14191  143 GLU A CG  
1060 C CD  . GLU A 132 ? 0.60688 0.70774 0.62275 -0.04494 -0.02845 0.16412  143 GLU A CD  
1061 O OE1 . GLU A 132 ? 0.64663 0.77104 0.66159 -0.04501 -0.01860 0.16819  143 GLU A OE1 
1062 O OE2 . GLU A 132 ? 0.67267 0.77209 0.69187 -0.04809 -0.03585 0.17816  143 GLU A OE2 
1063 N N   . PRO A 133 ? 0.40263 0.42212 0.40801 -0.02638 -0.03980 0.09663  144 PRO A N   
1064 C CA  . PRO A 133 ? 0.35789 0.36709 0.35756 -0.01938 -0.04320 0.08684  144 PRO A CA  
1065 C C   . PRO A 133 ? 0.35256 0.36976 0.35068 -0.02014 -0.04647 0.09858  144 PRO A C   
1066 O O   . PRO A 133 ? 0.37059 0.38655 0.37649 -0.02650 -0.05386 0.11523  144 PRO A O   
1067 C CB  . PRO A 133 ? 0.40320 0.38638 0.40921 -0.01824 -0.05497 0.08223  144 PRO A CB  
1068 C CG  . PRO A 133 ? 0.30691 0.28592 0.32488 -0.02780 -0.06291 0.09816  144 PRO A CG  
1069 C CD  . PRO A 133 ? 0.38547 0.38761 0.40291 -0.03227 -0.05108 0.10368  144 PRO A CD  
1070 N N   . GLY A 134 ? 0.33074 0.35640 0.31962 -0.01392 -0.04168 0.09066  145 GLY A N   
1071 C CA  . GLY A 134 ? 0.34320 0.37515 0.32899 -0.01292 -0.04548 0.09934  145 GLY A CA  
1072 C C   . GLY A 134 ? 0.36524 0.37859 0.35291 -0.00790 -0.05492 0.09313  145 GLY A C   
1073 O O   . GLY A 134 ? 0.36513 0.35952 0.35767 -0.00575 -0.06035 0.08501  145 GLY A O   
1074 N N   . LYS A 135 ? 0.32586 0.34583 0.30891 -0.00485 -0.05707 0.09650  146 LYS A N   
1075 C CA  . LYS A 135 ? 0.37883 0.38427 0.36344 0.00137  -0.06536 0.08987  146 LYS A CA  
1076 C C   . LYS A 135 ? 0.40728 0.40849 0.39018 0.00833  -0.06061 0.07048  146 LYS A C   
1077 O O   . LYS A 135 ? 0.45098 0.43565 0.43822 0.01304  -0.06679 0.06315  146 LYS A O   
1078 C CB  . LYS A 135 ? 0.34777 0.36457 0.32679 0.00388  -0.06713 0.09577  146 LYS A CB  
1079 C CG  . LYS A 135 ? 0.41022 0.43184 0.39130 -0.00231 -0.07298 0.11739  146 LYS A CG  
1080 C CD  . LYS A 135 ? 0.34834 0.38160 0.32203 0.00169  -0.07487 0.12182  146 LYS A CD  
1081 C CE  . LYS A 135 ? 0.58096 0.63050 0.55241 -0.00415 -0.07516 0.14386  146 LYS A CE  
1082 N NZ  . LYS A 135 ? 0.52319 0.59573 0.48769 -0.00647 -0.06276 0.14576  146 LYS A NZ  
1083 N N   . LYS A 136 ? 0.37109 0.38779 0.34794 0.00958  -0.05012 0.06230  147 LYS A N   
1084 C CA  . LYS A 136 ? 0.30711 0.32251 0.28414 0.01476  -0.04501 0.04635  147 LYS A CA  
1085 C C   . LYS A 136 ? 0.34709 0.37060 0.32187 0.01227  -0.03511 0.04059  147 LYS A C   
1086 O O   . LYS A 136 ? 0.37187 0.39108 0.34883 0.01504  -0.03170 0.03012  147 LYS A O   
1087 C CB  . LYS A 136 ? 0.33044 0.35456 0.30528 0.02019  -0.04468 0.03977  147 LYS A CB  
1088 C CG  . LYS A 136 ? 0.43629 0.45323 0.41357 0.02403  -0.05461 0.04427  147 LYS A CG  
1089 C CD  . LYS A 136 ? 0.52734 0.55194 0.50535 0.03029  -0.05451 0.03541  147 LYS A CD  
1090 C CE  . LYS A 136 ? 0.67727 0.69315 0.65900 0.03557  -0.06489 0.03862  147 LYS A CE  
1091 N NZ  . LYS A 136 ? 0.57071 0.59539 0.55519 0.04190  -0.06555 0.03086  147 LYS A NZ  
1092 N N   . LYS A 137 ? 0.33084 0.36665 0.30148 0.00785  -0.03047 0.04743  148 LYS A N   
1093 C CA  . LYS A 137 ? 0.28169 0.32544 0.25008 0.00669  -0.02170 0.04124  148 LYS A CA  
1094 C C   . LYS A 137 ? 0.27080 0.31398 0.24191 0.00098  -0.02047 0.05009  148 LYS A C   
1095 O O   . LYS A 137 ? 0.26077 0.30605 0.23368 -0.00311 -0.02451 0.06390  148 LYS A O   
1096 C CB  . LYS A 137 ? 0.31593 0.37735 0.27639 0.00874  -0.01689 0.03851  148 LYS A CB  
1097 C CG  . LYS A 137 ? 0.37974 0.44194 0.34009 0.01353  -0.01692 0.02614  148 LYS A CG  
1098 C CD  . LYS A 137 ? 0.41034 0.48771 0.36253 0.01615  -0.01518 0.02281  148 LYS A CD  
1099 C CE  . LYS A 137 ? 0.43134 0.50878 0.38627 0.01973  -0.01720 0.01144  148 LYS A CE  
1100 N NZ  . LYS A 137 ? 0.44536 0.51884 0.40631 0.01911  -0.01291 0.00160  148 LYS A NZ  
1101 N N   . TRP A 138 ? 0.25008 0.29102 0.22278 0.00038  -0.01534 0.04314  149 TRP A N   
1102 C CA  . TRP A 138 ? 0.29198 0.33762 0.26698 -0.00462 -0.01244 0.05038  149 TRP A CA  
1103 C C   . TRP A 138 ? 0.22957 0.29657 0.19826 -0.00444 -0.00586 0.05442  149 TRP A C   
1104 O O   . TRP A 138 ? 0.23204 0.30714 0.19410 0.00025  -0.00191 0.04529  149 TRP A O   
1105 C CB  . TRP A 138 ? 0.23629 0.27507 0.21358 -0.00420 -0.00855 0.04089  149 TRP A CB  
1106 C CG  . TRP A 138 ? 0.27270 0.29269 0.25450 -0.00311 -0.01448 0.03677  149 TRP A CG  
1107 C CD1 . TRP A 138 ? 0.23609 0.24837 0.21705 0.00246  -0.01493 0.02616  149 TRP A CD1 
1108 C CD2 . TRP A 138 ? 0.26362 0.27117 0.25146 -0.00679 -0.02137 0.04283  149 TRP A CD2 
1109 N NE1 . TRP A 138 ? 0.26021 0.25677 0.24420 0.00396  -0.02113 0.02436  149 TRP A NE1 
1110 C CE2 . TRP A 138 ? 0.26450 0.25613 0.25268 -0.00177 -0.02606 0.03373  149 TRP A CE2 
1111 C CE3 . TRP A 138 ? 0.35491 0.36414 0.34876 -0.01371 -0.02467 0.05548  149 TRP A CE3 
1112 C CZ2 . TRP A 138 ? 0.23165 0.20675 0.22422 -0.00251 -0.03499 0.03491  149 TRP A CZ2 
1113 C CZ3 . TRP A 138 ? 0.29853 0.29062 0.29933 -0.01620 -0.03414 0.05793  149 TRP A CZ3 
1114 C CH2 . TRP A 138 ? 0.25064 0.22474 0.24986 -0.01014 -0.03972 0.04669  149 TRP A CH2 
1115 N N   . THR A 139 ? 0.27033 0.34735 0.24155 -0.00904 -0.00519 0.06805  150 THR A N   
1116 C CA  . THR A 139 ? 0.25367 0.35324 0.21897 -0.00743 0.00258  0.07090  150 THR A CA  
1117 C C   . THR A 139 ? 0.31844 0.41950 0.28880 -0.00969 0.00724  0.06948  150 THR A C   
1118 O O   . THR A 139 ? 0.27347 0.36665 0.25358 -0.01578 0.00354  0.07769  150 THR A O   
1119 C CB  . THR A 139 ? 0.32304 0.43964 0.28734 -0.00988 0.00173  0.08890  150 THR A CB  
1120 O OG1 . THR A 139 ? 0.34192 0.46073 0.29852 -0.00588 -0.00135 0.08814  150 THR A OG1 
1121 C CG2 . THR A 139 ? 0.29936 0.44214 0.25829 -0.00727 0.01058  0.09291  150 THR A CG2 
1122 N N   . LEU A 140 ? 0.25570 0.36534 0.22000 -0.00454 0.01402  0.05843  151 LEU A N   
1123 C CA  . LEU A 140 ? 0.25222 0.36332 0.22024 -0.00507 0.01867  0.05467  151 LEU A CA  
1124 C C   . LEU A 140 ? 0.28153 0.41797 0.24661 -0.00311 0.02489  0.06251  151 LEU A C   
1125 O O   . LEU A 140 ? 0.28359 0.43484 0.23834 0.00356  0.02812  0.05885  151 LEU A O   
1126 C CB  . LEU A 140 ? 0.22348 0.32650 0.18775 -0.00006 0.02113  0.03721  151 LEU A CB  
1127 C CG  . LEU A 140 ? 0.27686 0.35862 0.24533 -0.00119 0.01742  0.02904  151 LEU A CG  
1128 C CD1 . LEU A 140 ? 0.26543 0.33884 0.23333 -0.00110 0.01165  0.03008  151 LEU A CD1 
1129 C CD2 . LEU A 140 ? 0.27998 0.35972 0.24607 0.00312  0.02079  0.01519  151 LEU A CD2 
1130 N N   . THR A 141 ? 0.26022 0.40282 0.23440 -0.00818 0.02612  0.07319  152 THR A N   
1131 C CA  . THR A 141 ? 0.27252 0.44270 0.24616 -0.00625 0.03271  0.08279  152 THR A CA  
1132 C C   . THR A 141 ? 0.31398 0.48701 0.28926 -0.00297 0.03789  0.07359  152 THR A C   
1133 O O   . THR A 141 ? 0.27702 0.43626 0.26189 -0.00817 0.03542  0.07312  152 THR A O   
1134 C CB  . THR A 141 ? 0.31182 0.49093 0.29758 -0.01515 0.02994  0.10483  152 THR A CB  
1135 O OG1 . THR A 141 ? 0.28106 0.45749 0.26530 -0.01782 0.02447  0.11424  152 THR A OG1 
1136 C CG2 . THR A 141 ? 0.23935 0.45147 0.22589 -0.01270 0.03801  0.11613  152 THR A CG2 
1137 N N   . PHE A 142 ? 0.32077 0.51116 0.28625 0.00646  0.04416  0.06580  153 PHE A N   
1138 C CA  . PHE A 142 ? 0.20668 0.40019 0.17304 0.01117  0.04854  0.05625  153 PHE A CA  
1139 C C   . PHE A 142 ? 0.29051 0.51499 0.25846 0.01463  0.05534  0.06700  153 PHE A C   
1140 O O   . PHE A 142 ? 0.31796 0.56440 0.28237 0.01610  0.05781  0.07904  153 PHE A O   
1141 C CB  . PHE A 142 ? 0.24630 0.43301 0.20143 0.02057  0.04884  0.03657  153 PHE A CB  
1142 C CG  . PHE A 142 ? 0.25263 0.41305 0.20784 0.01744  0.04301  0.02717  153 PHE A CG  
1143 C CD1 . PHE A 142 ? 0.24025 0.38059 0.20286 0.01344  0.04104  0.02114  153 PHE A CD1 
1144 C CD2 . PHE A 142 ? 0.24085 0.39855 0.18901 0.01890  0.03960  0.02515  153 PHE A CD2 
1145 C CE1 . PHE A 142 ? 0.25217 0.37206 0.21530 0.01133  0.03660  0.01371  153 PHE A CE1 
1146 C CE2 . PHE A 142 ? 0.26640 0.40280 0.21613 0.01646  0.03463  0.01720  153 PHE A CE2 
1147 C CZ  . PHE A 142 ? 0.27403 0.39238 0.23147 0.01276  0.03353  0.01182  153 PHE A CZ  
1148 N N   . GLU A 143 ? 0.24495 0.47238 0.21881 0.01622  0.05839  0.06333  154 GLU A N   
1149 C CA  . GLU A 143 ? 0.21643 0.46963 0.19484 0.02004  0.06311  0.07160  154 GLU A CA  
1150 C C   . GLU A 143 ? 0.26124 0.52742 0.22636 0.03377  0.06488  0.06102  154 GLU A C   
1151 O O   . GLU A 143 ? 0.29026 0.54859 0.24745 0.04238  0.06493  0.04344  154 GLU A O   
1152 C CB  . GLU A 143 ? 0.24153 0.49118 0.22979 0.01867  0.06457  0.06855  154 GLU A CB  
1153 C CG  . GLU A 143 ? 0.37212 0.64293 0.36791 0.02183  0.06697  0.07619  154 GLU A CG  
1154 C CD  . GLU A 143 ? 0.42637 0.69272 0.43261 0.01977  0.06768  0.07380  154 GLU A CD  
1155 O OE1 . GLU A 143 ? 0.49827 0.75247 0.51539 0.00900  0.06489  0.08035  154 GLU A OE1 
1156 O OE2 . GLU A 143 ? 0.60365 0.87824 0.60711 0.02931  0.07031  0.06515  154 GLU A OE2 
1157 N N   . ASN A 144 ? 0.26448 0.55000 0.22787 0.03583  0.06529  0.07202  155 ASN A N   
1158 C CA  . ASN A 144 ? 0.24093 0.54392 0.19310 0.04911  0.06669  0.06540  155 ASN A CA  
1159 C C   . ASN A 144 ? 0.25463 0.54498 0.19090 0.05736  0.06380  0.04698  155 ASN A C   
1160 O O   . ASN A 144 ? 0.27930 0.57846 0.20568 0.06979  0.06336  0.03617  155 ASN A O   
1161 C CB  . ASN A 144 ? 0.27653 0.59248 0.23183 0.05690  0.06966  0.06139  155 ASN A CB  
1162 C CG  . ASN A 144 ? 0.32614 0.66028 0.29746 0.04991  0.07193  0.08128  155 ASN A CG  
1163 O OD1 . ASN A 144 ? 0.36844 0.69723 0.35141 0.03714  0.07015  0.09541  155 ASN A OD1 
1164 N ND2 . ASN A 144 ? 0.31153 0.66707 0.28393 0.05848  0.07485  0.08246  155 ASN A ND2 
1165 N N   . LYS A 145 ? 0.24410 0.51491 0.17809 0.05092  0.06093  0.04381  156 LYS A N   
1166 C CA  . LYS A 145 ? 0.23853 0.49614 0.15976 0.05680  0.05697  0.02763  156 LYS A CA  
1167 C C   . LYS A 145 ? 0.31965 0.57460 0.23758 0.05070  0.05455  0.03649  156 LYS A C   
1168 O O   . LYS A 145 ? 0.26953 0.52478 0.19658 0.04009  0.05518  0.05300  156 LYS A O   
1169 C CB  . LYS A 145 ? 0.25591 0.49036 0.17857 0.05551  0.05520  0.01266  156 LYS A CB  
1170 C CG  . LYS A 145 ? 0.30922 0.54329 0.23620 0.06082  0.05677  0.00423  156 LYS A CG  
1171 C CD  . LYS A 145 ? 0.33831 0.57767 0.25511 0.07460  0.05381  -0.00991 156 LYS A CD  
1172 C CE  . LYS A 145 ? 0.42968 0.67012 0.35075 0.08052  0.05487  -0.01679 156 LYS A CE  
1173 N NZ  . LYS A 145 ? 0.56799 0.83399 0.49254 0.08357  0.05958  -0.00442 156 LYS A NZ  
1174 N N   . PRO A 146 ? 0.26404 0.51542 0.16965 0.05708  0.05055  0.02610  157 PRO A N   
1175 C CA  . PRO A 146 ? 0.29751 0.54777 0.19930 0.05213  0.04776  0.03514  157 PRO A CA  
1176 C C   . PRO A 146 ? 0.24403 0.46949 0.15394 0.04133  0.04414  0.03560  157 PRO A C   
1177 O O   . PRO A 146 ? 0.25567 0.46165 0.17188 0.03947  0.04247  0.02405  157 PRO A O   
1178 C CB  . PRO A 146 ? 0.33973 0.59041 0.22737 0.06275  0.04306  0.02070  157 PRO A CB  
1179 C CG  . PRO A 146 ? 0.34064 0.58314 0.22609 0.07082  0.04157  0.00132  157 PRO A CG  
1180 C CD  . PRO A 146 ? 0.32648 0.57463 0.22190 0.06922  0.04704  0.00624  157 PRO A CD  
1181 N N   . SER A 147 ? 0.28363 0.50579 0.19711 0.03392  0.04091  0.04896  158 SER A N   
1182 C CA  . SER A 147 ? 0.27613 0.47187 0.20132 0.02375  0.03532  0.05058  158 SER A CA  
1183 C C   . SER A 147 ? 0.30576 0.48250 0.22723 0.02623  0.02978  0.03456  158 SER A C   
1184 O O   . SER A 147 ? 0.25329 0.43667 0.16345 0.03440  0.02844  0.02470  158 SER A O   
1185 C CB  . SER A 147 ? 0.25609 0.45429 0.18667 0.01611  0.03227  0.07004  158 SER A CB  
1186 O OG  . SER A 147 ? 0.30613 0.51392 0.22563 0.02078  0.03006  0.07218  158 SER A OG  
1187 N N   . GLU A 148 ? 0.25968 0.41351 0.19125 0.01947  0.02601  0.03217  159 GLU A N   
1188 C CA  . GLU A 148 ? 0.27480 0.41202 0.20647 0.02049  0.02107  0.01970  159 GLU A CA  
1189 C C   . GLU A 148 ? 0.31020 0.43218 0.24981 0.01385  0.01622  0.02674  159 GLU A C   
1190 O O   . GLU A 148 ? 0.28736 0.40719 0.23342 0.00813  0.01583  0.03880  159 GLU A O   
1191 C CB  . GLU A 148 ? 0.27742 0.40326 0.21325 0.02165  0.02218  0.00588  159 GLU A CB  
1192 C CG  . GLU A 148 ? 0.28800 0.42595 0.21722 0.02897  0.02578  -0.00227 159 GLU A CG  
1193 C CD  . GLU A 148 ? 0.34525 0.48749 0.26464 0.03717  0.02189  -0.01454 159 GLU A CD  
1194 O OE1 . GLU A 148 ? 0.34058 0.47749 0.25893 0.03648  0.01669  -0.01602 159 GLU A OE1 
1195 O OE2 . GLU A 148 ? 0.37621 0.52690 0.28906 0.04496  0.02313  -0.02336 159 GLU A OE2 
1196 N N   . THR A 149 ? 0.26876 0.38051 0.20859 0.01510  0.01156  0.01918  160 THR A N   
1197 C CA  . THR A 149 ? 0.31118 0.40861 0.25796 0.01109  0.00656  0.02355  160 THR A CA  
1198 C C   . THR A 149 ? 0.31200 0.39516 0.26511 0.01136  0.00553  0.01206  160 THR A C   
1199 O O   . THR A 149 ? 0.28961 0.37408 0.24188 0.01418  0.00688  0.00137  160 THR A O   
1200 C CB  . THR A 149 ? 0.31534 0.41693 0.25764 0.01273  0.00143  0.02884  160 THR A CB  
1201 O OG1 . THR A 149 ? 0.37158 0.47737 0.30838 0.01809  -0.00007 0.01759  160 THR A OG1 
1202 C CG2 . THR A 149 ? 0.28659 0.40450 0.22312 0.01210  0.00252  0.04348  160 THR A CG2 
1203 N N   . ALA A 150 ? 0.25953 0.32954 0.21942 0.00879  0.00252  0.01482  161 ALA A N   
1204 C CA  . ALA A 150 ? 0.29502 0.35465 0.26093 0.00982  0.00222  0.00604  161 ALA A CA  
1205 C C   . ALA A 150 ? 0.21051 0.25914 0.18074 0.00999  -0.00289 0.00946  161 ALA A C   
1206 O O   . ALA A 150 ? 0.24415 0.28725 0.21513 0.00764  -0.00610 0.01784  161 ALA A O   
1207 C CB  . ALA A 150 ? 0.24763 0.30298 0.21678 0.00834  0.00691  0.00201  161 ALA A CB  
1208 N N   . ASP A 151 ? 0.24678 0.29257 0.22090 0.01311  -0.00428 0.00295  162 ASP A N   
1209 C CA  . ASP A 151 ? 0.29574 0.33188 0.27371 0.01568  -0.00897 0.00392  162 ASP A CA  
1210 C C   . ASP A 151 ? 0.32146 0.34749 0.30196 0.01598  -0.00778 0.00216  162 ASP A C   
1211 O O   . ASP A 151 ? 0.25373 0.26928 0.23529 0.01822  -0.01316 0.00404  162 ASP A O   
1212 C CB  . ASP A 151 ? 0.24096 0.28102 0.22331 0.01977  -0.00998 -0.00209 162 ASP A CB  
1213 C CG  . ASP A 151 ? 0.29381 0.34243 0.27347 0.02026  -0.01320 -0.00082 162 ASP A CG  
1214 O OD1 . ASP A 151 ? 0.28805 0.33423 0.26618 0.02169  -0.01880 0.00466  162 ASP A OD1 
1215 O OD2 . ASP A 151 ? 0.30197 0.35900 0.28077 0.01953  -0.01111 -0.00541 162 ASP A OD2 
1216 N N   . LEU A 152 ? 0.24259 0.27093 0.22371 0.01449  -0.00182 -0.00195 163 LEU A N   
1217 C CA  . LEU A 152 ? 0.23988 0.26031 0.22230 0.01539  -0.00032 -0.00421 163 LEU A CA  
1218 C C   . LEU A 152 ? 0.24743 0.27003 0.22847 0.01112  0.00411  -0.00319 163 LEU A C   
1219 O O   . LEU A 152 ? 0.20274 0.23369 0.18361 0.00981  0.00830  -0.00576 163 LEU A O   
1220 C CB  . LEU A 152 ? 0.20744 0.23045 0.19380 0.01974  0.00288  -0.01066 163 LEU A CB  
1221 C CG  . LEU A 152 ? 0.21734 0.23607 0.20365 0.02136  0.00613  -0.01334 163 LEU A CG  
1222 C CD1 . LEU A 152 ? 0.21752 0.22394 0.20046 0.02486  0.00038  -0.01280 163 LEU A CD1 
1223 C CD2 . LEU A 152 ? 0.17772 0.20425 0.16899 0.02502  0.01055  -0.01713 163 LEU A CD2 
1224 N N   . VAL A 153 ? 0.24768 0.26237 0.22832 0.00942  0.00210  0.00013  164 VAL A N   
1225 C CA  . VAL A 153 ? 0.19925 0.21616 0.17976 0.00580  0.00582  0.00156  164 VAL A CA  
1226 C C   . VAL A 153 ? 0.25054 0.25974 0.23168 0.00785  0.00677  -0.00286 164 VAL A C   
1227 O O   . VAL A 153 ? 0.23231 0.23142 0.21292 0.01081  0.00166  -0.00365 164 VAL A O   
1228 C CB  . VAL A 153 ? 0.24741 0.26440 0.22856 0.00118  0.00228  0.01105  164 VAL A CB  
1229 C CG1 . VAL A 153 ? 0.18434 0.20404 0.16697 -0.00187 0.00577  0.01247  164 VAL A CG1 
1230 C CG2 . VAL A 153 ? 0.21870 0.24741 0.19759 -0.00007 0.00282  0.01635  164 VAL A CG2 
1231 N N   . ILE A 154 ? 0.25219 0.26592 0.23387 0.00719  0.01256  -0.00610 165 ILE A N   
1232 C CA  . ILE A 154 ? 0.22990 0.23850 0.21143 0.00919  0.01419  -0.00938 165 ILE A CA  
1233 C C   . ILE A 154 ? 0.26734 0.27673 0.24942 0.00546  0.01584  -0.00702 165 ILE A C   
1234 O O   . ILE A 154 ? 0.20797 0.22501 0.19116 0.00378  0.02025  -0.00772 165 ILE A O   
1235 C CB  . ILE A 154 ? 0.22339 0.23724 0.20697 0.01177  0.01920  -0.01390 165 ILE A CB  
1236 C CG1 . ILE A 154 ? 0.23780 0.25362 0.22256 0.01582  0.01769  -0.01547 165 ILE A CG1 
1237 C CG2 . ILE A 154 ? 0.19825 0.20892 0.18084 0.01379  0.02147  -0.01550 165 ILE A CG2 
1238 C CD1 . ILE A 154 ? 0.17853 0.20244 0.16846 0.01746  0.02229  -0.01764 165 ILE A CD1 
1239 N N   . ILE A 155 ? 0.24257 0.24390 0.22437 0.00471  0.01133  -0.00468 166 ILE A N   
1240 C CA  . ILE A 155 ? 0.22470 0.22749 0.20869 0.00101  0.01192  -0.00146 166 ILE A CA  
1241 C C   . ILE A 155 ? 0.23613 0.23828 0.21901 0.00327  0.01611  -0.00620 166 ILE A C   
1242 O O   . ILE A 155 ? 0.27578 0.27049 0.25575 0.00687  0.01393  -0.00918 166 ILE A O   
1243 C CB  . ILE A 155 ? 0.19321 0.18700 0.17945 -0.00142 0.00368  0.00340  166 ILE A CB  
1244 C CG1 . ILE A 155 ? 0.23329 0.22711 0.22205 -0.00433 -0.00144 0.01022  166 ILE A CG1 
1245 C CG2 . ILE A 155 ? 0.24847 0.24529 0.23881 -0.00531 0.00411  0.00708  166 ILE A CG2 
1246 C CD1 . ILE A 155 ? 0.26526 0.27439 0.25568 -0.00781 0.00363  0.01616  166 ILE A CD1 
1247 N N   . ALA A 156 ? 0.23519 0.24524 0.21993 0.00192  0.02151  -0.00682 167 ALA A N   
1248 C CA  . ALA A 156 ? 0.23692 0.24625 0.22182 0.00346  0.02496  -0.00993 167 ALA A CA  
1249 C C   . ALA A 156 ? 0.24808 0.26210 0.23584 0.00129  0.02667  -0.00822 167 ALA A C   
1250 O O   . ALA A 156 ? 0.21291 0.22928 0.20211 0.00226  0.03015  -0.01081 167 ALA A O   
1251 C CB  . ALA A 156 ? 0.18759 0.20056 0.17372 0.00512  0.02897  -0.01344 167 ALA A CB  
1252 N N   . ASN A 157 ? 0.23403 0.25038 0.22395 -0.00161 0.02390  -0.00319 168 ASN A N   
1253 C CA  . ASN A 157 ? 0.22523 0.25076 0.21885 -0.00289 0.02646  -0.00091 168 ASN A CA  
1254 C C   . ASN A 157 ? 0.22957 0.25132 0.22618 -0.00415 0.02373  0.00127  168 ASN A C   
1255 O O   . ASN A 157 ? 0.23928 0.26912 0.24116 -0.00645 0.02355  0.00620  168 ASN A O   
1256 C CB  . ASN A 157 ? 0.17999 0.21708 0.17552 -0.00502 0.02683  0.00489  168 ASN A CB  
1257 C CG  . ASN A 157 ? 0.25228 0.28701 0.25175 -0.00956 0.02090  0.01323  168 ASN A CG  
1258 O OD1 . ASN A 157 ? 0.23003 0.25277 0.22793 -0.00992 0.01558  0.01267  168 ASN A OD1 
1259 N ND2 . ASN A 157 ? 0.20120 0.24817 0.20679 -0.01276 0.02121  0.02147  168 ASN A ND2 
1260 N N   . GLY A 158 ? 0.22540 0.23664 0.21873 -0.00210 0.02164  -0.00213 169 GLY A N   
1261 C CA  . GLY A 158 ? 0.23751 0.24552 0.23222 -0.00193 0.01957  -0.00182 169 GLY A CA  
1262 C C   . GLY A 158 ? 0.29925 0.30033 0.29584 -0.00430 0.01126  0.00153  169 GLY A C   
1263 O O   . GLY A 158 ? 0.22904 0.22688 0.22684 -0.00655 0.00641  0.00443  169 GLY A O   
1264 N N   . GLY A 159 ? 0.20289 0.20103 0.20064 -0.00390 0.00842  0.00134  170 GLY A N   
1265 C CA  . GLY A 159 ? 0.21003 0.19822 0.20856 -0.00499 -0.00157 0.00232  170 GLY A CA  
1266 C C   . GLY A 159 ? 0.32198 0.31401 0.33140 -0.01181 -0.00732 0.01053  170 GLY A C   
1267 O O   . GLY A 159 ? 0.26378 0.24513 0.27519 -0.01370 -0.01767 0.01189  170 GLY A O   
1268 N N   . MET A 160 ? 0.25537 0.26314 0.27245 -0.01517 -0.00140 0.01649  171 MET A N   
1269 C CA  . MET A 160 ? 0.28307 0.29937 0.31228 -0.02202 -0.00559 0.02708  171 MET A CA  
1270 C C   . MET A 160 ? 0.26753 0.28927 0.29740 -0.02440 -0.00389 0.03220  171 MET A C   
1271 O O   . MET A 160 ? 0.36237 0.39812 0.40201 -0.02947 -0.00350 0.04277  171 MET A O   
1272 C CB  . MET A 160 ? 0.25318 0.28752 0.29113 -0.02333 -0.00028 0.03215  171 MET A CB  
1273 C CG  . MET A 160 ? 0.35002 0.38039 0.38997 -0.02192 -0.00343 0.02923  171 MET A CG  
1274 S SD  . MET A 160 ? 0.50533 0.51831 0.54981 -0.02602 -0.01927 0.03079  171 MET A SD  
1275 C CE  . MET A 160 ? 0.29444 0.32363 0.36025 -0.03576 -0.02412 0.04644  171 MET A CE  
1276 N N   . SER A 161 ? 0.27116 0.28386 0.29140 -0.02068 -0.00286 0.02593  172 SER A N   
1277 C CA  . SER A 161 ? 0.21689 0.23483 0.23658 -0.02209 -0.00110 0.03008  172 SER A CA  
1278 C C   . SER A 161 ? 0.27104 0.28813 0.30096 -0.02916 -0.01003 0.04157  172 SER A C   
1279 O O   . SER A 161 ? 0.32050 0.32238 0.35383 -0.03116 -0.02096 0.04174  172 SER A O   
1280 C CB  . SER A 161 ? 0.21935 0.22533 0.22884 -0.01705 -0.00121 0.02161  172 SER A CB  
1281 O OG  . SER A 161 ? 0.20318 0.21331 0.21245 -0.01837 -0.00082 0.02579  172 SER A OG  
1282 N N   . LYS A 162 ? 0.21149 0.24503 0.24644 -0.03265 -0.00619 0.05152  173 LYS A N   
1283 C CA  . LYS A 162 ? 0.26289 0.29728 0.30889 -0.04023 -0.01448 0.06517  173 LYS A CA  
1284 C C   . LYS A 162 ? 0.30810 0.33649 0.34924 -0.03972 -0.01682 0.06643  173 LYS A C   
1285 O O   . LYS A 162 ? 0.30526 0.33412 0.35554 -0.04608 -0.02393 0.07894  173 LYS A O   
1286 C CB  . LYS A 162 ? 0.27843 0.33876 0.33532 -0.04499 -0.00917 0.07909  173 LYS A CB  
1287 C CG  . LYS A 162 ? 0.33062 0.39987 0.39473 -0.04554 -0.00709 0.07941  173 LYS A CG  
1288 C CD  . LYS A 162 ? 0.45866 0.55744 0.53437 -0.04936 -0.00138 0.09463  173 LYS A CD  
1289 C CE  . LYS A 162 ? 0.69494 0.81064 0.77003 -0.04387 0.00808  0.09002  173 LYS A CE  
1290 N NZ  . LYS A 162 ? 0.80651 0.95352 0.88243 -0.04076 0.01884  0.09779  173 LYS A NZ  
1291 N N   . VAL A 163 ? 0.24076 0.26363 0.26914 -0.03268 -0.01178 0.05474  174 VAL A N   
1292 C CA  . VAL A 163 ? 0.27011 0.28913 0.29383 -0.03137 -0.01341 0.05536  174 VAL A CA  
1293 C C   . VAL A 163 ? 0.33260 0.32922 0.35031 -0.02668 -0.02062 0.04506  174 VAL A C   
1294 O O   . VAL A 163 ? 0.31292 0.30729 0.32221 -0.02123 -0.01725 0.03771  174 VAL A O   
1295 C CB  . VAL A 163 ? 0.28219 0.31674 0.29742 -0.02679 -0.00215 0.05146  174 VAL A CB  
1296 C CG1 . VAL A 163 ? 0.27180 0.33005 0.29184 -0.02989 0.00350  0.06294  174 VAL A CG1 
1297 C CG2 . VAL A 163 ? 0.17640 0.20935 0.18454 -0.02090 0.00462  0.03829  174 VAL A CG2 
1298 N N   . ARG A 164 ? 0.33039 0.31122 0.35262 -0.02810 -0.03123 0.04436  175 ARG A N   
1299 C CA  . ARG A 164 ? 0.32782 0.28854 0.34308 -0.02152 -0.03860 0.03345  175 ARG A CA  
1300 C C   . ARG A 164 ? 0.35363 0.29839 0.37365 -0.02308 -0.05258 0.03763  175 ARG A C   
1301 O O   . ARG A 164 ? 0.28189 0.21137 0.29478 -0.01553 -0.05844 0.02775  175 ARG A O   
1302 C CB  . ARG A 164 ? 0.34035 0.29188 0.35411 -0.01902 -0.04240 0.02632  175 ARG A CB  
1303 C CG  . ARG A 164 ? 0.31784 0.28070 0.32607 -0.01599 -0.03043 0.02054  175 ARG A CG  
1304 C CD  . ARG A 164 ? 0.36590 0.32259 0.37726 -0.01698 -0.03629 0.01929  175 ARG A CD  
1305 N NE  . ARG A 164 ? 0.35285 0.31009 0.35521 -0.01058 -0.02998 0.00991  175 ARG A NE  
1306 C CZ  . ARG A 164 ? 0.33579 0.29728 0.34100 -0.01208 -0.02864 0.01049  175 ARG A CZ  
1307 N NH1 . ARG A 164 ? 0.34761 0.31612 0.36500 -0.01963 -0.03148 0.01982  175 ARG A NH1 
1308 N NH2 . ARG A 164 ? 0.32288 0.28276 0.31933 -0.00581 -0.02455 0.00255  175 ARG A NH2 
1309 N N   . LYS A 165 ? 0.32594 0.27455 0.35828 -0.03214 -0.05838 0.05245  176 LYS A N   
1310 C CA  . LYS A 165 ? 0.37677 0.30630 0.41745 -0.03531 -0.07547 0.05776  176 LYS A CA  
1311 C C   . LYS A 165 ? 0.37745 0.29593 0.41115 -0.02887 -0.07938 0.05253  176 LYS A C   
1312 O O   . LYS A 165 ? 0.38570 0.28238 0.42130 -0.02625 -0.09436 0.04918  176 LYS A O   
1313 C CB  . LYS A 165 ? 0.39287 0.33237 0.45038 -0.04757 -0.07994 0.07795  176 LYS A CB  
1314 C CG  . LYS A 165 ? 0.53954 0.48309 0.60935 -0.05479 -0.08361 0.08449  176 LYS A CG  
1315 C CD  . LYS A 165 ? 0.58700 0.50425 0.65744 -0.05185 -0.09922 0.07417  176 LYS A CD  
1316 C CE  . LYS A 165 ? 0.50182 0.42205 0.58512 -0.05896 -0.10448 0.07998  176 LYS A CE  
1317 N NZ  . LYS A 165 ? 0.56336 0.50516 0.64198 -0.05740 -0.08817 0.07745  176 LYS A NZ  
1318 N N   . PHE A 166 ? 0.30335 0.23584 0.32929 -0.02558 -0.06735 0.05107  177 PHE A N   
1319 C CA  . PHE A 166 ? 0.33629 0.25882 0.35605 -0.01859 -0.07125 0.04517  177 PHE A CA  
1320 C C   . PHE A 166 ? 0.38754 0.29685 0.39699 -0.00707 -0.07310 0.02796  177 PHE A C   
1321 O O   . PHE A 166 ? 0.34176 0.23977 0.34734 0.00015  -0.07950 0.02209  177 PHE A O   
1322 C CB  . PHE A 166 ? 0.34840 0.28939 0.36296 -0.01778 -0.05909 0.04755  177 PHE A CB  
1323 C CG  . PHE A 166 ? 0.34973 0.30053 0.37224 -0.02605 -0.06091 0.06458  177 PHE A CG  
1324 C CD1 . PHE A 166 ? 0.34736 0.28460 0.37609 -0.02803 -0.07403 0.07223  177 PHE A CD1 
1325 C CD2 . PHE A 166 ? 0.34116 0.31531 0.36491 -0.03117 -0.05000 0.07339  177 PHE A CD2 
1326 C CE1 . PHE A 166 ? 0.37287 0.32067 0.40943 -0.03605 -0.07576 0.09027  177 PHE A CE1 
1327 C CE2 . PHE A 166 ? 0.31675 0.30331 0.34687 -0.03783 -0.05092 0.09025  177 PHE A CE2 
1328 C CZ  . PHE A 166 ? 0.30100 0.27491 0.33791 -0.04091 -0.06359 0.09972  177 PHE A CZ  
1329 N N   . VAL A 167 ? 0.34529 0.25665 0.35033 -0.00455 -0.06809 0.02040  178 VAL A N   
1330 C CA  . VAL A 167 ? 0.33305 0.23549 0.32748 0.00694  -0.06878 0.00544  178 VAL A CA  
1331 C C   . VAL A 167 ? 0.35529 0.23849 0.35074 0.00912  -0.08319 0.00075  178 VAL A C   
1332 O O   . VAL A 167 ? 0.39037 0.25906 0.37866 0.01965  -0.09172 -0.01002 178 VAL A O   
1333 C CB  . VAL A 167 ? 0.34558 0.26449 0.33309 0.00947  -0.05296 0.00013  178 VAL A CB  
1334 C CG1 . VAL A 167 ? 0.31800 0.23073 0.29547 0.02030  -0.05329 -0.01249 178 VAL A CG1 
1335 C CG2 . VAL A 167 ? 0.26224 0.19589 0.24765 0.01008  -0.04198 0.00118  178 VAL A CG2 
1336 N N   . THR A 168 ? 0.37263 0.25587 0.37694 0.00018  -0.08690 0.00816  179 THR A N   
1337 C CA  . THR A 168 ? 0.37292 0.23778 0.37861 0.00205  -0.10168 0.00302  179 THR A CA  
1338 C C   . THR A 168 ? 0.40502 0.27173 0.42684 -0.01145 -0.10769 0.01679  179 THR A C   
1339 O O   . THR A 168 ? 0.34003 0.22673 0.36793 -0.01960 -0.09603 0.02721  179 THR A O   
1340 C CB  . THR A 168 ? 0.41664 0.28338 0.40949 0.01139  -0.09582 -0.00985 179 THR A CB  
1341 O OG1 . THR A 168 ? 0.37724 0.22699 0.37145 0.01270  -0.11101 -0.01443 179 THR A OG1 
1342 C CG2 . THR A 168 ? 0.32198 0.21069 0.31506 0.00620  -0.07861 -0.00535 179 THR A CG2 
1343 N N   . ASP A 169 ? 0.42125 0.26760 0.45044 -0.01312 -0.12663 0.01655  180 ASP A N   
1344 C CA  . ASP A 169 ? 0.42617 0.27357 0.47271 -0.02579 -0.13454 0.02933  180 ASP A CA  
1345 C C   . ASP A 169 ? 0.44663 0.29530 0.49017 -0.02407 -0.13391 0.02258  180 ASP A C   
1346 O O   . ASP A 169 ? 0.43403 0.28436 0.49271 -0.03407 -0.14095 0.03241  180 ASP A O   
1347 C CB  . ASP A 169 ? 0.38752 0.21075 0.44740 -0.03038 -0.15824 0.03446  180 ASP A CB  
1348 C CG  . ASP A 169 ? 0.48902 0.31168 0.55552 -0.03456 -0.16035 0.04527  180 ASP A CG  
1349 O OD1 . ASP A 169 ? 0.50195 0.34780 0.57153 -0.04092 -0.14539 0.05728  180 ASP A OD1 
1350 O OD2 . ASP A 169 ? 0.57910 0.37781 0.64704 -0.03058 -0.17764 0.04121  180 ASP A OD2 
1351 N N   . THR A 170 ? 0.45726 0.30589 0.48264 -0.01171 -0.12637 0.00711  181 THR A N   
1352 C CA  . THR A 170 ? 0.43155 0.28214 0.45206 -0.00894 -0.12506 0.00062  181 THR A CA  
1353 C C   . THR A 170 ? 0.41611 0.28927 0.44697 -0.01933 -0.11259 0.01262  181 THR A C   
1354 O O   . THR A 170 ? 0.37984 0.27138 0.41187 -0.02277 -0.09784 0.01962  181 THR A O   
1355 C CB  . THR A 170 ? 0.46675 0.31957 0.46603 0.00567  -0.11511 -0.01467 181 THR A CB  
1356 O OG1 . THR A 170 ? 0.48005 0.31355 0.46925 0.01734  -0.12727 -0.02666 181 THR A OG1 
1357 C CG2 . THR A 170 ? 0.42529 0.28220 0.41844 0.00879  -0.11235 -0.02015 181 THR A CG2 
1358 N N   . GLU A 171 ? 0.41985 0.29167 0.45824 -0.02352 -0.11950 0.01446  182 GLU A N   
1359 C CA  . GLU A 171 ? 0.44577 0.33884 0.49506 -0.03217 -0.10953 0.02519  182 GLU A CA  
1360 C C   . GLU A 171 ? 0.39974 0.29819 0.43750 -0.02513 -0.10150 0.01560  182 GLU A C   
1361 O O   . GLU A 171 ? 0.40091 0.28446 0.42774 -0.01670 -0.10990 0.00365  182 GLU A O   
1362 C CB  . GLU A 171 ? 0.45634 0.34718 0.52776 -0.04424 -0.12397 0.03807  182 GLU A CB  
1363 C CG  . GLU A 171 ? 0.57401 0.46252 0.66092 -0.05371 -0.13208 0.05218  182 GLU A CG  
1364 C CD  . GLU A 171 ? 0.61606 0.52997 0.70598 -0.05831 -0.11454 0.06408  182 GLU A CD  
1365 O OE1 . GLU A 171 ? 0.72259 0.63359 0.81236 -0.05919 -0.11529 0.06848  182 GLU A OE1 
1366 O OE2 . GLU A 171 ? 0.63060 0.56724 0.72236 -0.06010 -0.10060 0.06839  182 GLU A OE2 
1367 N N   . VAL A 172 ? 0.32561 0.24569 0.36539 -0.02785 -0.08565 0.02091  183 VAL A N   
1368 C CA  . VAL A 172 ? 0.42690 0.35262 0.45901 -0.02278 -0.07896 0.01444  183 VAL A CA  
1369 C C   . VAL A 172 ? 0.46445 0.38383 0.50675 -0.02684 -0.09270 0.01645  183 VAL A C   
1370 O O   . VAL A 172 ? 0.43316 0.35360 0.49388 -0.03687 -0.10216 0.02758  183 VAL A O   
1371 C CB  . VAL A 172 ? 0.44017 0.38899 0.47440 -0.02491 -0.06112 0.01993  183 VAL A CB  
1372 C CG1 . VAL A 172 ? 0.42428 0.38859 0.47801 -0.03543 -0.06152 0.03432  183 VAL A CG1 
1373 C CG2 . VAL A 172 ? 0.43607 0.38867 0.46018 -0.01820 -0.05336 0.01233  183 VAL A CG2 
1374 N N   . GLU A 173 ? 0.40303 0.31591 0.43382 -0.01905 -0.09482 0.00626  184 GLU A N   
1375 C CA  . GLU A 173 ? 0.39371 0.29887 0.43146 -0.02107 -0.10908 0.00571  184 GLU A CA  
1376 C C   . GLU A 173 ? 0.42008 0.33792 0.45441 -0.01844 -0.09980 0.00449  184 GLU A C   
1377 O O   . GLU A 173 ? 0.40569 0.32873 0.42511 -0.01067 -0.08709 -0.00162 184 GLU A O   
1378 C CB  . GLU A 173 ? 0.38949 0.27039 0.41424 -0.01186 -0.12556 -0.00763 184 GLU A CB  
1379 C CG  . GLU A 173 ? 0.51147 0.37495 0.53712 -0.01152 -0.13778 -0.00969 184 GLU A CG  
1380 C CD  . GLU A 173 ? 0.57422 0.41460 0.58396 0.00091  -0.15362 -0.02561 184 GLU A CD  
1381 O OE1 . GLU A 173 ? 0.50665 0.34720 0.50210 0.01001  -0.15242 -0.03479 184 GLU A OE1 
1382 O OE2 . GLU A 173 ? 0.63805 0.46024 0.64894 0.00250  -0.16776 -0.02913 184 GLU A OE2 
1383 N N   . GLU A 174 ? 0.38396 0.30597 0.43306 -0.02488 -0.10761 0.01066  185 GLU A N   
1384 C CA  . GLU A 174 ? 0.42477 0.35490 0.47055 -0.02138 -0.10301 0.00832  185 GLU A CA  
1385 C C   . GLU A 174 ? 0.38399 0.29610 0.41380 -0.01174 -0.11496 -0.00442 185 GLU A C   
1386 O O   . GLU A 174 ? 0.43213 0.32705 0.46416 -0.01205 -0.13314 -0.00815 185 GLU A O   
1387 C CB  . GLU A 174 ? 0.39862 0.34267 0.46773 -0.03162 -0.10670 0.02044  185 GLU A CB  
1388 C CG  . GLU A 174 ? 0.46403 0.43021 0.54659 -0.03880 -0.09315 0.03285  185 GLU A CG  
1389 C CD  . GLU A 174 ? 0.56724 0.55191 0.67369 -0.04793 -0.09537 0.04609  185 GLU A CD  
1390 O OE1 . GLU A 174 ? 0.65679 0.63543 0.77217 -0.05055 -0.10930 0.04654  185 GLU A OE1 
1391 O OE2 . GLU A 174 ? 0.63617 0.64274 0.75252 -0.05191 -0.08335 0.05606  185 GLU A OE2 
1392 N N   . THR A 175 ? 0.42835 0.34423 0.44184 -0.00265 -0.10561 -0.01101 186 THR A N   
1393 C CA  . THR A 175 ? 0.36594 0.26777 0.36186 0.00808  -0.11577 -0.02268 186 THR A CA  
1394 C C   . THR A 175 ? 0.39715 0.29856 0.39958 0.00664  -0.12658 -0.02208 186 THR A C   
1395 O O   . THR A 175 ? 0.42585 0.31342 0.41618 0.01455  -0.14008 -0.03170 186 THR A O   
1396 C CB  . THR A 175 ? 0.41576 0.32272 0.39047 0.01908  -0.10158 -0.02868 186 THR A CB  
1397 O OG1 . THR A 175 ? 0.39068 0.31324 0.36998 0.01676  -0.08939 -0.02248 186 THR A OG1 
1398 C CG2 . THR A 175 ? 0.38197 0.29060 0.35089 0.02082  -0.09103 -0.02935 186 THR A CG2 
1399 N N   . GLY A 176 ? 0.43613 0.35314 0.45671 -0.00211 -0.12138 -0.01162 187 GLY A N   
1400 C CA  . GLY A 176 ? 0.35854 0.27724 0.38733 -0.00375 -0.13131 -0.01018 187 GLY A CA  
1401 C C   . GLY A 176 ? 0.42249 0.35395 0.44495 0.00112  -0.11940 -0.00961 187 GLY A C   
1402 O O   . GLY A 176 ? 0.39655 0.33029 0.42549 0.00045  -0.12738 -0.00840 187 GLY A O   
1403 N N   . THR A 177 ? 0.40251 0.34167 0.41371 0.00580  -0.10189 -0.01010 188 THR A N   
1404 C CA  . THR A 177 ? 0.31579 0.26701 0.32483 0.00892  -0.09072 -0.00763 188 THR A CA  
1405 C C   . THR A 177 ? 0.32968 0.29779 0.35324 0.00261  -0.07653 0.00084  188 THR A C   
1406 O O   . THR A 177 ? 0.37492 0.34585 0.40481 -0.00239 -0.07234 0.00396  188 THR A O   
1407 C CB  . THR A 177 ? 0.38123 0.32822 0.36655 0.01991  -0.08318 -0.01420 188 THR A CB  
1408 O OG1 . THR A 177 ? 0.39375 0.34151 0.37292 0.02069  -0.07210 -0.01488 188 THR A OG1 
1409 C CG2 . THR A 177 ? 0.39031 0.32294 0.35863 0.02851  -0.09683 -0.02342 188 THR A CG2 
1410 N N   . PHE A 178 ? 0.31343 0.29291 0.34170 0.00381  -0.06975 0.00417  189 PHE A N   
1411 C CA  . PHE A 178 ? 0.31499 0.31141 0.35725 -0.00030 -0.05818 0.01092  189 PHE A CA  
1412 C C   . PHE A 178 ? 0.33802 0.33845 0.37225 0.00618  -0.04723 0.00933  189 PHE A C   
1413 O O   . PHE A 178 ? 0.33510 0.32994 0.36006 0.01170  -0.05046 0.00667  189 PHE A O   
1414 C CB  . PHE A 178 ? 0.34823 0.35777 0.41284 -0.00692 -0.06435 0.01873  189 PHE A CB  
1415 C CG  . PHE A 178 ? 0.35158 0.38074 0.43133 -0.01121 -0.05394 0.02621  189 PHE A CG  
1416 C CD1 . PHE A 178 ? 0.35510 0.39783 0.43796 -0.00690 -0.04346 0.02715  189 PHE A CD1 
1417 C CD2 . PHE A 178 ? 0.35046 0.38499 0.44126 -0.01880 -0.05538 0.03246  189 PHE A CD2 
1418 C CE1 . PHE A 178 ? 0.29123 0.35360 0.38616 -0.00865 -0.03404 0.03276  189 PHE A CE1 
1419 C CE2 . PHE A 178 ? 0.33988 0.39532 0.44309 -0.02154 -0.04534 0.03989  189 PHE A CE2 
1420 C CZ  . PHE A 178 ? 0.37442 0.44437 0.47892 -0.01580 -0.03449 0.03936  189 PHE A CZ  
1421 N N   . ASN A 179 ? 0.31969 0.32936 0.35757 0.00568  -0.03521 0.01117  190 ASN A N   
1422 C CA  . ASN A 179 ? 0.30222 0.31330 0.33388 0.01120  -0.02580 0.00956  190 ASN A CA  
1423 C C   . ASN A 179 ? 0.34768 0.37430 0.39339 0.01082  -0.01917 0.01285  190 ASN A C   
1424 O O   . ASN A 179 ? 0.32671 0.36377 0.38142 0.00707  -0.01558 0.01550  190 ASN A O   
1425 C CB  . ASN A 179 ? 0.29899 0.30322 0.31833 0.01300  -0.01847 0.00625  190 ASN A CB  
1426 C CG  . ASN A 179 ? 0.35053 0.34265 0.35701 0.01415  -0.02440 0.00269  190 ASN A CG  
1427 O OD1 . ASN A 179 ? 0.36913 0.35414 0.36385 0.01933  -0.02791 0.00042  190 ASN A OD1 
1428 N ND2 . ASN A 179 ? 0.32887 0.31909 0.33707 0.01020  -0.02615 0.00221  190 ASN A ND2 
1429 N N   . ILE A 180 ? 0.25665 0.28536 0.30365 0.01563  -0.01786 0.01271  191 ILE A N   
1430 C CA  . ILE A 180 ? 0.30044 0.34211 0.35799 0.01843  -0.01156 0.01360  191 ILE A CA  
1431 C C   . ILE A 180 ? 0.30525 0.33841 0.35403 0.02371  -0.00597 0.01007  191 ILE A C   
1432 O O   . ILE A 180 ? 0.33323 0.35579 0.37350 0.02633  -0.00881 0.00998  191 ILE A O   
1433 C CB  . ILE A 180 ? 0.26645 0.31834 0.33649 0.01992  -0.01671 0.01689  191 ILE A CB  
1434 C CG1 . ILE A 180 ? 0.29057 0.35125 0.37233 0.01312  -0.02367 0.02203  191 ILE A CG1 
1435 C CG2 . ILE A 180 ? 0.27719 0.34253 0.35666 0.02538  -0.01019 0.01636  191 ILE A CG2 
1436 C CD1 . ILE A 180 ? 0.29376 0.36555 0.38978 0.01358  -0.03021 0.02621  191 ILE A CD1 
1437 N N   . GLN A 181 ? 0.34634 0.38436 0.39744 0.02524  0.00119  0.00772  192 GLN A N   
1438 C CA  . GLN A 181 ? 0.28330 0.31217 0.32842 0.02899  0.00517  0.00452  192 GLN A CA  
1439 C C   . GLN A 181 ? 0.28618 0.32323 0.34022 0.03475  0.00795  0.00162  192 GLN A C   
1440 O O   . GLN A 181 ? 0.27324 0.32614 0.33620 0.03593  0.00969  0.00168  192 GLN A O   
1441 C CB  . GLN A 181 ? 0.31252 0.33620 0.35020 0.02607  0.00957  0.00244  192 GLN A CB  
1442 C CG  . GLN A 181 ? 0.37660 0.39130 0.40390 0.02264  0.00707  0.00389  192 GLN A CG  
1443 C CD  . GLN A 181 ? 0.40824 0.41983 0.42989 0.02032  0.01151  0.00191  192 GLN A CD  
1444 O OE1 . GLN A 181 ? 0.42508 0.44053 0.44727 0.01684  0.01146  0.00188  192 GLN A OE1 
1445 N NE2 . GLN A 181 ? 0.34035 0.34525 0.35801 0.02187  0.01476  0.00109  192 GLN A NE2 
1446 N N   . ALA A 182 ? 0.24427 0.27098 0.29610 0.03876  0.00807  -0.00065 193 ALA A N   
1447 C CA  . ALA A 182 ? 0.30979 0.34091 0.36917 0.04593  0.00883  -0.00523 193 ALA A CA  
1448 C C   . ALA A 182 ? 0.32849 0.34365 0.38495 0.04803  0.00770  -0.00751 193 ALA A C   
1449 O O   . ALA A 182 ? 0.29888 0.30206 0.34903 0.04410  0.00651  -0.00323 193 ALA A O   
1450 C CB  . ALA A 182 ? 0.23615 0.27524 0.30427 0.05073  0.00504  -0.00359 193 ALA A CB  
1451 N N   . ASP A 183 ? 0.32025 0.33634 0.38193 0.05469  0.00758  -0.01404 194 ASP A N   
1452 C CA  . ASP A 183 ? 0.38394 0.38397 0.44680 0.05742  0.00382  -0.01654 194 ASP A CA  
1453 C C   . ASP A 183 ? 0.32489 0.32373 0.39585 0.06624  -0.00134 -0.01935 194 ASP A C   
1454 O O   . ASP A 183 ? 0.35580 0.36944 0.43171 0.07303  -0.00024 -0.02376 194 ASP A O   
1455 C CB  . ASP A 183 ? 0.28772 0.28563 0.34949 0.05876  0.00540  -0.02397 194 ASP A CB  
1456 C CG  . ASP A 183 ? 0.35754 0.35393 0.41202 0.05031  0.00955  -0.02103 194 ASP A CG  
1457 O OD1 . ASP A 183 ? 0.37867 0.36688 0.42939 0.04426  0.00925  -0.01383 194 ASP A OD1 
1458 O OD2 . ASP A 183 ? 0.40826 0.41279 0.46038 0.05053  0.01315  -0.02576 194 ASP A OD2 
1459 N N   . ILE A 184 ? 0.29241 0.27474 0.36541 0.06639  -0.00704 -0.01597 195 ILE A N   
1460 C CA  . ILE A 184 ? 0.33864 0.31495 0.41986 0.07521  -0.01371 -0.01931 195 ILE A CA  
1461 C C   . ILE A 184 ? 0.36725 0.32550 0.45178 0.07660  -0.01926 -0.02335 195 ILE A C   
1462 O O   . ILE A 184 ? 0.36399 0.30912 0.44736 0.06903  -0.02091 -0.01596 195 ILE A O   
1463 C CB  . ILE A 184 ? 0.33495 0.30654 0.41763 0.07434  -0.01785 -0.01030 195 ILE A CB  
1464 C CG1 . ILE A 184 ? 0.33449 0.32377 0.41558 0.07331  -0.01435 -0.00757 195 ILE A CG1 
1465 C CG2 . ILE A 184 ? 0.29802 0.26014 0.39003 0.08364  -0.02605 -0.01358 195 ILE A CG2 
1466 C CD1 . ILE A 184 ? 0.35323 0.34026 0.43592 0.07433  -0.01933 -0.00059 195 ILE A CD1 
1467 N N   . HIS A 185 ? 0.38794 0.34636 0.47715 0.08665  -0.02273 -0.03483 196 HIS A N   
1468 C CA  . HIS A 185 ? 0.37807 0.31740 0.47197 0.08924  -0.03086 -0.04052 196 HIS A CA  
1469 C C   . HIS A 185 ? 0.40015 0.32325 0.50300 0.09355  -0.04101 -0.03752 196 HIS A C   
1470 O O   . HIS A 185 ? 0.44838 0.37856 0.55392 0.09991  -0.04185 -0.03698 196 HIS A O   
1471 C CB  . HIS A 185 ? 0.47162 0.41827 0.56439 0.09961  -0.03101 -0.05582 196 HIS A CB  
1472 C CG  . HIS A 185 ? 0.64385 0.60949 0.72805 0.09596  -0.02067 -0.05709 196 HIS A CG  
1473 N ND1 . HIS A 185 ? 0.63783 0.59971 0.71693 0.08488  -0.01696 -0.05207 196 HIS A ND1 
1474 C CD2 . HIS A 185 ? 0.66363 0.65317 0.74452 0.10138  -0.01334 -0.06095 196 HIS A CD2 
1475 C CE1 . HIS A 185 ? 0.57456 0.55494 0.64706 0.08390  -0.00857 -0.05366 196 HIS A CE1 
1476 N NE2 . HIS A 185 ? 0.71336 0.71106 0.78715 0.09328  -0.00617 -0.05826 196 HIS A NE2 
1477 N N   . HIS A 186 ? 0.43675 0.33836 0.54542 0.08923  -0.04916 -0.03405 197 HIS A N   
1478 C CA  . HIS A 186 ? 0.45992 0.34332 0.57828 0.09071  -0.05982 -0.02775 197 HIS A CA  
1479 C C   . HIS A 186 ? 0.44440 0.33509 0.56055 0.08811  -0.05656 -0.01551 197 HIS A C   
1480 O O   . HIS A 186 ? 0.46525 0.35656 0.58587 0.09689  -0.06111 -0.01773 197 HIS A O   
1481 C CB  . HIS A 186 ? 0.52817 0.40296 0.65397 0.10539  -0.07010 -0.04193 197 HIS A CB  
1482 C CG  . HIS A 186 ? 0.63711 0.50337 0.76398 0.10973  -0.07538 -0.05561 197 HIS A CG  
1483 N ND1 . HIS A 186 ? 0.68894 0.57006 0.80961 0.12109  -0.07168 -0.07155 197 HIS A ND1 
1484 C CD2 . HIS A 186 ? 0.69577 0.54120 0.82932 0.10425  -0.08456 -0.05527 197 HIS A CD2 
1485 C CE1 . HIS A 186 ? 0.77797 0.64679 0.89966 0.12334  -0.07870 -0.08179 197 HIS A CE1 
1486 N NE2 . HIS A 186 ? 0.82191 0.66822 0.95227 0.11281  -0.08715 -0.07237 197 HIS A NE2 
1487 N N   . PRO A 187 ? 0.41023 0.30715 0.51904 0.07724  -0.04925 -0.00328 198 PRO A N   
1488 C CA  . PRO A 187 ? 0.39198 0.29682 0.49652 0.07592  -0.04680 0.00673  198 PRO A CA  
1489 C C   . PRO A 187 ? 0.45925 0.34912 0.57140 0.07716  -0.05626 0.01643  198 PRO A C   
1490 O O   . PRO A 187 ? 0.43893 0.33420 0.55023 0.08108  -0.05747 0.02011  198 PRO A O   
1491 C CB  . PRO A 187 ? 0.36571 0.27807 0.45967 0.06521  -0.03825 0.01598  198 PRO A CB  
1492 C CG  . PRO A 187 ? 0.44621 0.34860 0.54328 0.05926  -0.03890 0.01623  198 PRO A CG  
1493 C CD  . PRO A 187 ? 0.40963 0.30744 0.51320 0.06697  -0.04343 0.00104  198 PRO A CD  
1494 N N   . GLU A 188 ? 0.40798 0.27913 0.52876 0.07368  -0.06393 0.02138  199 GLU A N   
1495 C CA  . GLU A 188 ? 0.45497 0.31062 0.58492 0.07454  -0.07422 0.03194  199 GLU A CA  
1496 C C   . GLU A 188 ? 0.48828 0.34038 0.62493 0.08766  -0.08202 0.02196  199 GLU A C   
1497 O O   . GLU A 188 ? 0.51760 0.36264 0.65892 0.08999  -0.08873 0.03068  199 GLU A O   
1498 C CB  . GLU A 188 ? 0.48440 0.32007 0.62590 0.06815  -0.08267 0.03825  199 GLU A CB  
1499 C CG  . GLU A 188 ? 0.52188 0.34247 0.67374 0.07557  -0.09274 0.02221  199 GLU A CG  
1500 C CD  . GLU A 188 ? 0.70711 0.53809 0.85196 0.07675  -0.08552 0.00723  199 GLU A CD  
1501 O OE1 . GLU A 188 ? 0.53685 0.38237 0.67182 0.06872  -0.07395 0.01174  199 GLU A OE1 
1502 O OE2 . GLU A 188 ? 0.74807 0.57259 0.89688 0.08669  -0.09203 -0.00938 199 GLU A OE2 
1503 N N   . VAL A 189 ? 0.49168 0.35060 0.62841 0.09696  -0.08086 0.00436  200 VAL A N   
1504 C CA  . VAL A 189 ? 0.46861 0.32965 0.61087 0.11133  -0.08645 -0.00654 200 VAL A CA  
1505 C C   . VAL A 189 ? 0.47539 0.36262 0.61050 0.11504  -0.07661 -0.00945 200 VAL A C   
1506 O O   . VAL A 189 ? 0.49452 0.38653 0.63350 0.12224  -0.07992 -0.00854 200 VAL A O   
1507 C CB  . VAL A 189 ? 0.49114 0.34425 0.63873 0.12163  -0.09268 -0.02449 200 VAL A CB  
1508 C CG1 . VAL A 189 ? 0.54907 0.40915 0.70043 0.13782  -0.09671 -0.03658 200 VAL A CG1 
1509 C CG2 . VAL A 189 ? 0.54579 0.37201 0.70182 0.11644  -0.10447 -0.02131 200 VAL A CG2 
1510 N N   . ASN A 190 ? 0.44111 0.34538 0.56713 0.10976  -0.06534 -0.01210 201 ASN A N   
1511 C CA  . ASN A 190 ? 0.46509 0.39455 0.58751 0.11357  -0.05733 -0.01621 201 ASN A CA  
1512 C C   . ASN A 190 ? 0.39039 0.32923 0.50659 0.10551  -0.05296 -0.00394 201 ASN A C   
1513 O O   . ASN A 190 ? 0.40509 0.36029 0.52315 0.10983  -0.05135 -0.00476 201 ASN A O   
1514 C CB  . ASN A 190 ? 0.46700 0.41060 0.58408 0.11297  -0.04868 -0.02546 201 ASN A CB  
1515 C CG  . ASN A 190 ? 0.49878 0.44277 0.62079 0.12626  -0.05229 -0.04097 201 ASN A CG  
1516 O OD1 . ASN A 190 ? 0.46554 0.41302 0.59450 0.13865  -0.05725 -0.04695 201 ASN A OD1 
1517 N ND2 . ASN A 190 ? 0.50391 0.44455 0.62190 0.12480  -0.05042 -0.04806 201 ASN A ND2 
1518 N N   . CYS A 191 ? 0.44040 0.37047 0.54955 0.09467  -0.05157 0.00728  202 CYS A N   
1519 C CA  . CYS A 191 ? 0.41540 0.35083 0.51740 0.08929  -0.05015 0.01871  202 CYS A CA  
1520 C C   . CYS A 191 ? 0.41858 0.33726 0.51947 0.08456  -0.05539 0.03201  202 CYS A C   
1521 O O   . CYS A 191 ? 0.37415 0.29309 0.46560 0.07626  -0.05111 0.04110  202 CYS A O   
1522 C CB  . CYS A 191 ? 0.32898 0.27772 0.42011 0.08156  -0.04110 0.01937  202 CYS A CB  
1523 S SG  . CYS A 191 ? 0.35736 0.29943 0.44235 0.07297  -0.03534 0.01955  202 CYS A SG  
1524 N N   . PRO A 192 ? 0.40979 0.31497 0.52054 0.09034  -0.06497 0.03430  203 PRO A N   
1525 C CA  . PRO A 192 ? 0.42088 0.30947 0.53340 0.08507  -0.07065 0.04874  203 PRO A CA  
1526 C C   . PRO A 192 ? 0.44881 0.34379 0.54983 0.07943  -0.06773 0.06347  203 PRO A C   
1527 O O   . PRO A 192 ? 0.42734 0.31786 0.52419 0.07174  -0.06580 0.07546  203 PRO A O   
1528 C CB  . PRO A 192 ? 0.42458 0.29905 0.55050 0.09413  -0.08268 0.04718  203 PRO A CB  
1529 C CG  . PRO A 192 ? 0.45849 0.34689 0.58671 0.10464  -0.08199 0.03425  203 PRO A CG  
1530 C CD  . PRO A 192 ? 0.41308 0.31788 0.53474 0.10238  -0.07139 0.02412  203 PRO A CD  
1531 N N   . GLY A 193 ? 0.39491 0.30152 0.49073 0.08357  -0.06767 0.06297  204 GLY A N   
1532 C CA  . GLY A 193 ? 0.36123 0.27355 0.44436 0.08008  -0.06640 0.07547  204 GLY A CA  
1533 C C   . GLY A 193 ? 0.44015 0.36127 0.50943 0.07273  -0.05714 0.07721  204 GLY A C   
1534 O O   . GLY A 193 ? 0.43718 0.35796 0.49734 0.06844  -0.05534 0.08986  204 GLY A O   
1535 N N   . PHE A 194 ? 0.41464 0.34498 0.48217 0.07183  -0.05115 0.06505  205 PHE A N   
1536 C CA  . PHE A 194 ? 0.36229 0.29998 0.41717 0.06564  -0.04322 0.06562  205 PHE A CA  
1537 C C   . PHE A 194 ? 0.40012 0.32991 0.45705 0.05985  -0.03991 0.07048  205 PHE A C   
1538 O O   . PHE A 194 ? 0.38914 0.32280 0.43573 0.05520  -0.03497 0.07811  205 PHE A O   
1539 C CB  . PHE A 194 ? 0.33452 0.28347 0.38860 0.06564  -0.03868 0.05275  205 PHE A CB  
1540 C CG  . PHE A 194 ? 0.36543 0.32050 0.40692 0.06010  -0.03194 0.05251  205 PHE A CG  
1541 C CD1 . PHE A 194 ? 0.37802 0.33916 0.40582 0.05997  -0.03234 0.05631  205 PHE A CD1 
1542 C CD2 . PHE A 194 ? 0.38975 0.34379 0.43254 0.05591  -0.02616 0.04810  205 PHE A CD2 
1543 C CE1 . PHE A 194 ? 0.31198 0.27776 0.32774 0.05640  -0.02714 0.05504  205 PHE A CE1 
1544 C CE2 . PHE A 194 ? 0.38300 0.34240 0.41459 0.05157  -0.02042 0.04783  205 PHE A CE2 
1545 C CZ  . PHE A 194 ? 0.34843 0.31347 0.36663 0.05212  -0.02092 0.05102  205 PHE A CZ  
1546 N N   . PHE A 195 ? 0.45921 0.37853 0.52985 0.06074  -0.04325 0.06586  206 PHE A N   
1547 C CA  . PHE A 195 ? 0.43510 0.34534 0.51091 0.05476  -0.04250 0.07111  206 PHE A CA  
1548 C C   . PHE A 195 ? 0.43575 0.34119 0.51089 0.05094  -0.04506 0.08991  206 PHE A C   
1549 O O   . PHE A 195 ? 0.41671 0.32542 0.48802 0.04450  -0.04012 0.09917  206 PHE A O   
1550 C CB  . PHE A 195 ? 0.38505 0.28255 0.47613 0.05810  -0.04886 0.06172  206 PHE A CB  
1551 C CG  . PHE A 195 ? 0.45954 0.34626 0.55841 0.05169  -0.05027 0.06569  206 PHE A CG  
1552 C CD1 . PHE A 195 ? 0.39601 0.28832 0.49132 0.04734  -0.04347 0.05916  206 PHE A CD1 
1553 C CD2 . PHE A 195 ? 0.40914 0.27997 0.52034 0.04961  -0.05939 0.07665  206 PHE A CD2 
1554 C CE1 . PHE A 195 ? 0.42360 0.30672 0.52746 0.04111  -0.04560 0.06295  206 PHE A CE1 
1555 C CE2 . PHE A 195 ? 0.43882 0.29981 0.55989 0.04265  -0.06210 0.08127  206 PHE A CE2 
1556 C CZ  . PHE A 195 ? 0.41548 0.28303 0.53289 0.03846  -0.05514 0.07408  206 PHE A CZ  
1557 N N   . GLN A 196 ? 0.43553 0.33504 0.51465 0.05518  -0.05259 0.09678  207 GLN A N   
1558 C CA  . GLN A 196 ? 0.43747 0.33444 0.51562 0.05188  -0.05507 0.11668  207 GLN A CA  
1559 C C   . GLN A 196 ? 0.44259 0.35610 0.50129 0.05075  -0.04723 0.12443  207 GLN A C   
1560 O O   . GLN A 196 ? 0.50365 0.42159 0.55857 0.04616  -0.04404 0.14010  207 GLN A O   
1561 C CB  . GLN A 196 ? 0.48848 0.37554 0.57459 0.05754  -0.06548 0.12162  207 GLN A CB  
1562 C CG  . GLN A 196 ? 0.54670 0.41462 0.65264 0.05918  -0.07512 0.11629  207 GLN A CG  
1563 C CD  . GLN A 196 ? 0.63264 0.49238 0.74595 0.06809  -0.08518 0.11360  207 GLN A CD  
1564 O OE1 . GLN A 196 ? 0.71832 0.58359 0.82456 0.07080  -0.08672 0.12250  207 GLN A OE1 
1565 N NE2 . GLN A 196 ? 0.55197 0.39908 0.67896 0.07377  -0.09249 0.10063  207 GLN A NE2 
1566 N N   . LEU A 197 ? 0.46826 0.39190 0.51492 0.05525  -0.04446 0.11358  208 LEU A N   
1567 C CA  . LEU A 197 ? 0.44306 0.38078 0.47012 0.05568  -0.03862 0.11768  208 LEU A CA  
1568 C C   . LEU A 197 ? 0.41308 0.35718 0.43499 0.05015  -0.02988 0.11928  208 LEU A C   
1569 O O   . LEU A 197 ? 0.41503 0.36872 0.42516 0.04957  -0.02547 0.13094  208 LEU A O   
1570 C CB  . LEU A 197 ? 0.43989 0.38479 0.45845 0.06045  -0.03917 0.10391  208 LEU A CB  
1571 C CG  . LEU A 197 ? 0.49260 0.44920 0.49033 0.06320  -0.03703 0.10611  208 LEU A CG  
1572 C CD1 . LEU A 197 ? 0.44584 0.40376 0.43617 0.06716  -0.04170 0.12082  208 LEU A CD1 
1573 C CD2 . LEU A 197 ? 0.44333 0.40457 0.43754 0.06618  -0.03950 0.09168  208 LEU A CD2 
1574 N N   . CYS A 198 ? 0.38623 0.32674 0.41639 0.04692  -0.02720 0.10781  209 CYS A N   
1575 C CA  . CYS A 198 ? 0.43585 0.38221 0.46271 0.04172  -0.01949 0.10917  209 CYS A CA  
1576 C C   . CYS A 198 ? 0.47586 0.42010 0.51107 0.03638  -0.01940 0.12691  209 CYS A C   
1577 O O   . CYS A 198 ? 0.51209 0.46811 0.53874 0.03438  -0.01296 0.13715  209 CYS A O   
1578 C CB  . CYS A 198 ? 0.38587 0.32811 0.42090 0.03953  -0.01778 0.09396  209 CYS A CB  
1579 S SG  . CYS A 198 ? 0.41130 0.36025 0.43826 0.04382  -0.01638 0.07595  209 CYS A SG  
1580 N N   . ASN A 199 ? 0.48165 0.41153 0.53451 0.03439  -0.02714 0.13124  210 ASN A N   
1581 C CA  . ASN A 199 ? 0.49848 0.42438 0.56315 0.02842  -0.02979 0.15051  210 ASN A CA  
1582 C C   . ASN A 199 ? 0.47966 0.41196 0.54831 0.02119  -0.02329 0.15451  210 ASN A C   
1583 O O   . ASN A 199 ? 0.46691 0.41152 0.53268 0.01772  -0.01825 0.17147  210 ASN A O   
1584 C CB  . ASN A 199 ? 0.52198 0.45741 0.57659 0.03063  -0.02935 0.16882  210 ASN A CB  
1585 C CG  . ASN A 199 ? 0.58881 0.51831 0.65933 0.02456  -0.03461 0.19073  210 ASN A CG  
1586 O OD1 . ASN A 199 ? 0.62128 0.53326 0.71212 0.02044  -0.04296 0.19005  210 ASN A OD1 
1587 N ND2 . ASN A 199 ? 0.53264 0.47711 0.59421 0.02432  -0.03042 0.21071  210 ASN A ND2 
1588 N N   . GLY A 200 ? 0.44722 0.37308 0.52226 0.01960  -0.02319 0.13886  211 GLY A N   
1589 C CA  . GLY A 200 ? 0.41137 0.34194 0.49170 0.01300  -0.01827 0.14040  211 GLY A CA  
1590 C C   . GLY A 200 ? 0.45578 0.40452 0.51855 0.01439  -0.00712 0.13672  211 GLY A C   
1591 O O   . GLY A 200 ? 0.43830 0.39111 0.50485 0.00996  -0.00291 0.13442  211 GLY A O   
1592 N N   . ASN A 201 ? 0.43160 0.39054 0.47556 0.02086  -0.00333 0.13537  212 ASN A N   
1593 C CA  . ASN A 201 ? 0.41705 0.39154 0.44351 0.02361  0.00548  0.13105  212 ASN A CA  
1594 C C   . ASN A 201 ? 0.36024 0.33197 0.37806 0.02781  0.00547  0.11079  212 ASN A C   
1595 O O   . ASN A 201 ? 0.39506 0.35802 0.41567 0.03067  -0.00027 0.10273  212 ASN A O   
1596 C CB  . ASN A 201 ? 0.40052 0.38933 0.41026 0.02891  0.00882  0.14325  212 ASN A CB  
1597 C CG  . ASN A 201 ? 0.49346 0.49336 0.50916 0.02472  0.01247  0.16546  212 ASN A CG  
1598 O OD1 . ASN A 201 ? 0.42091 0.41930 0.45301 0.01708  0.01324  0.17121  212 ASN A OD1 
1599 N ND2 . ASN A 201 ? 0.46633 0.47881 0.46912 0.02981  0.01440  0.17871  212 ASN A ND2 
1600 N N   . ARG A 202 ? 0.38013 0.36050 0.38842 0.02826  0.01171  0.10354  213 ARG A N   
1601 C CA  . ARG A 202 ? 0.41194 0.39283 0.40911 0.03261  0.01156  0.08815  213 ARG A CA  
1602 C C   . ARG A 202 ? 0.39276 0.37745 0.37579 0.03923  0.00864  0.08997  213 ARG A C   
1603 O O   . ARG A 202 ? 0.39997 0.39156 0.37580 0.04174  0.00961  0.10272  213 ARG A O   
1604 C CB  . ARG A 202 ? 0.37116 0.36019 0.35986 0.03242  0.01777  0.08203  213 ARG A CB  
1605 C CG  . ARG A 202 ? 0.45601 0.43951 0.45652 0.02728  0.01872  0.07336  213 ARG A CG  
1606 C CD  . ARG A 202 ? 0.54723 0.53899 0.54167 0.02646  0.02482  0.07038  213 ARG A CD  
1607 N NE  . ARG A 202 ? 0.65869 0.66090 0.65224 0.02566  0.02965  0.08402  213 ARG A NE  
1608 C CZ  . ARG A 202 ? 0.69043 0.70539 0.66874 0.03109  0.03417  0.08747  213 ARG A CZ  
1609 N NH1 . ARG A 202 ? 0.67701 0.69293 0.63943 0.03748  0.03305  0.07724  213 ARG A NH1 
1610 N NH2 . ARG A 202 ? 0.62631 0.65401 0.60598 0.03050  0.03933  0.10166  213 ARG A NH2 
1611 N N   . LEU A 203 ? 0.37181 0.35306 0.35148 0.04212  0.00460  0.07792  214 LEU A N   
1612 C CA  . LEU A 203 ? 0.35522 0.33867 0.32323 0.04818  -0.00023 0.07801  214 LEU A CA  
1613 C C   . LEU A 203 ? 0.40897 0.39485 0.36639 0.05093  -0.00176 0.06530  214 LEU A C   
1614 O O   . LEU A 203 ? 0.39978 0.38286 0.36448 0.04767  -0.00141 0.05543  214 LEU A O   
1615 C CB  . LEU A 203 ? 0.32467 0.30018 0.30388 0.04884  -0.00710 0.07844  214 LEU A CB  
1616 C CG  . LEU A 203 ? 0.36096 0.33841 0.33031 0.05491  -0.01347 0.07921  214 LEU A CG  
1617 C CD1 . LEU A 203 ? 0.37134 0.34302 0.35008 0.05585  -0.01844 0.08856  214 LEU A CD1 
1618 C CD2 . LEU A 203 ? 0.35020 0.32738 0.32007 0.05619  -0.01799 0.06578  214 LEU A CD2 
1619 N N   . MET A 204 ? 0.36446 0.35554 0.30476 0.05721  -0.00430 0.06590  215 MET A N   
1620 C CA  . MET A 204 ? 0.43041 0.42130 0.36118 0.06030  -0.00907 0.05416  215 MET A CA  
1621 C C   . MET A 204 ? 0.43101 0.42200 0.35244 0.06639  -0.01746 0.05464  215 MET A C   
1622 O O   . MET A 204 ? 0.40052 0.39561 0.31356 0.07081  -0.01738 0.06457  215 MET A O   
1623 C CB  . MET A 204 ? 0.42285 0.41925 0.33901 0.06359  -0.00520 0.05094  215 MET A CB  
1624 C CG  . MET A 204 ? 0.55790 0.55518 0.48280 0.05792  0.00265  0.05070  215 MET A CG  
1625 S SD  . MET A 204 ? 0.57754 0.58224 0.48522 0.06353  0.00645  0.04641  215 MET A SD  
1626 C CE  . MET A 204 ? 0.37918 0.39736 0.27425 0.07026  0.01172  0.06128  215 MET A CE  
1627 N N   . ALA A 205 ? 0.35869 0.34602 0.28244 0.06633  -0.02512 0.04487  216 ALA A N   
1628 C CA  . ALA A 205 ? 0.38263 0.36952 0.29917 0.07166  -0.03499 0.04373  216 ALA A CA  
1629 C C   . ALA A 205 ? 0.40538 0.38927 0.32029 0.07152  -0.04317 0.03181  216 ALA A C   
1630 O O   . ALA A 205 ? 0.42313 0.40516 0.35036 0.06529  -0.04173 0.02627  216 ALA A O   
1631 C CB  . ALA A 205 ? 0.32192 0.30676 0.25364 0.06979  -0.03830 0.04833  216 ALA A CB  
1632 N N   . ALA A 206 ? 0.42895 0.41233 0.32891 0.07849  -0.05267 0.02836  217 ALA A N   
1633 C CA  . ALA A 206 ? 0.42821 0.40674 0.32679 0.07859  -0.06353 0.01737  217 ALA A CA  
1634 C C   . ALA A 206 ? 0.42928 0.40657 0.32394 0.08323  -0.07649 0.01603  217 ALA A C   
1635 O O   . ALA A 206 ? 0.50012 0.48031 0.37923 0.09113  -0.07784 0.02064  217 ALA A O   
1636 C CB  . ALA A 206 ? 0.51353 0.49043 0.39345 0.08427  -0.06393 0.01051  217 ALA A CB  
1637 N N   . HIS A 207 ? 0.41854 0.39285 0.32783 0.07825  -0.08624 0.01069  218 HIS A N   
1638 C CA  . HIS A 207 ? 0.42667 0.39998 0.33564 0.08157  -0.10019 0.00903  218 HIS A CA  
1639 C C   . HIS A 207 ? 0.47511 0.44456 0.39843 0.07542  -0.11178 0.00165  218 HIS A C   
1640 O O   . HIS A 207 ? 0.41586 0.38923 0.36162 0.06648  -0.10796 0.00382  218 HIS A O   
1641 C CB  . HIS A 207 ? 0.42974 0.40845 0.35199 0.08022  -0.09774 0.01780  218 HIS A CB  
1642 C CG  . HIS A 207 ? 0.42825 0.40721 0.35154 0.08366  -0.11189 0.01694  218 HIS A CG  
1643 N ND1 . HIS A 207 ? 0.53682 0.51382 0.43778 0.09337  -0.12040 0.01558  218 HIS A ND1 
1644 C CD2 . HIS A 207 ? 0.47315 0.45569 0.41732 0.07927  -0.11904 0.01764  218 HIS A CD2 
1645 C CE1 . HIS A 207 ? 0.50436 0.48205 0.41239 0.09433  -0.13302 0.01502  218 HIS A CE1 
1646 N NE2 . HIS A 207 ? 0.49079 0.47223 0.42590 0.08559  -0.13231 0.01657  218 HIS A NE2 
1647 N N   . GLN A 208 ? 0.48970 0.45204 0.40040 0.08049  -0.12641 -0.00665 219 GLN A N   
1648 C CA  . GLN A 208 ? 0.44825 0.40558 0.37378 0.07453  -0.14152 -0.01258 219 GLN A CA  
1649 C C   . GLN A 208 ? 0.47827 0.43514 0.42065 0.06446  -0.13623 -0.01301 219 GLN A C   
1650 O O   . GLN A 208 ? 0.52995 0.49094 0.49661 0.05512  -0.14035 -0.01028 219 GLN A O   
1651 C CB  . GLN A 208 ? 0.51083 0.47439 0.45525 0.07087  -0.14932 -0.00786 219 GLN A CB  
1652 C CG  . GLN A 208 ? 0.54358 0.50620 0.47113 0.08097  -0.15837 -0.00835 219 GLN A CG  
1653 C CD  . GLN A 208 ? 0.68550 0.65501 0.63251 0.07783  -0.16622 -0.00345 219 GLN A CD  
1654 O OE1 . GLN A 208 ? 0.80381 0.78195 0.77650 0.06928  -0.16077 0.00219  219 GLN A OE1 
1655 N NE2 . GLN A 208 ? 0.58859 0.55573 0.52292 0.08576  -0.17919 -0.00570 219 GLN A NE2 
1656 N N   . GLY A 209 ? 0.50143 0.45491 0.43097 0.06670  -0.12701 -0.01562 220 GLY A N   
1657 C CA  . GLY A 209 ? 0.48273 0.43402 0.42422 0.05865  -0.12387 -0.01705 220 GLY A CA  
1658 C C   . GLY A 209 ? 0.51780 0.47914 0.47580 0.05105  -0.10762 -0.00919 220 GLY A C   
1659 O O   . GLY A 209 ? 0.41996 0.38110 0.38721 0.04459  -0.10366 -0.00944 220 GLY A O   
1660 N N   . ASN A 210 ? 0.46431 0.43384 0.42613 0.05217  -0.09910 -0.00254 221 ASN A N   
1661 C CA  . ASN A 210 ? 0.39891 0.37656 0.37363 0.04726  -0.08444 0.00326  221 ASN A CA  
1662 C C   . ASN A 210 ? 0.39280 0.36934 0.35157 0.05262  -0.07273 0.00545  221 ASN A C   
1663 O O   . ASN A 210 ? 0.45383 0.42949 0.39885 0.05966  -0.07380 0.00760  221 ASN A O   
1664 C CB  . ASN A 210 ? 0.40937 0.39659 0.40245 0.04504  -0.08430 0.00886  221 ASN A CB  
1665 C CG  . ASN A 210 ? 0.47605 0.46961 0.49058 0.03777  -0.09257 0.00937  221 ASN A CG  
1666 O OD1 . ASN A 210 ? 0.40640 0.40032 0.42842 0.03160  -0.09219 0.00838  221 ASN A OD1 
1667 N ND2 . ASN A 210 ? 0.46622 0.46575 0.49166 0.03826  -0.10053 0.01201  221 ASN A ND2 
1668 N N   . LEU A 211 ? 0.38801 0.36545 0.34903 0.04915  -0.06218 0.00576  222 LEU A N   
1669 C CA  . LEU A 211 ? 0.41200 0.38990 0.36274 0.05230  -0.05085 0.00923  222 LEU A CA  
1670 C C   . LEU A 211 ? 0.36291 0.34581 0.32937 0.04782  -0.04137 0.01405  222 LEU A C   
1671 O O   . LEU A 211 ? 0.34902 0.33577 0.33088 0.04226  -0.04023 0.01269  222 LEU A O   
1672 C CB  . LEU A 211 ? 0.39666 0.37128 0.33680 0.05285  -0.04706 0.00503  222 LEU A CB  
1673 C CG  . LEU A 211 ? 0.49534 0.46558 0.41356 0.06130  -0.05297 0.00016  222 LEU A CG  
1674 C CD1 . LEU A 211 ? 0.47375 0.43923 0.38813 0.06466  -0.06826 -0.00471 222 LEU A CD1 
1675 C CD2 . LEU A 211 ? 0.55810 0.52472 0.47233 0.06045  -0.05140 -0.00566 222 LEU A CD2 
1676 N N   . LEU A 212 ? 0.32020 0.30338 0.28273 0.05073  -0.03527 0.01994  223 LEU A N   
1677 C CA  . LEU A 212 ? 0.35607 0.34102 0.33149 0.04782  -0.02750 0.02353  223 LEU A CA  
1678 C C   . LEU A 212 ? 0.37510 0.35834 0.34302 0.04818  -0.01924 0.02766  223 LEU A C   
1679 O O   . LEU A 212 ? 0.37764 0.36073 0.33336 0.05245  -0.01900 0.03318  223 LEU A O   
1680 C CB  . LEU A 212 ? 0.32890 0.31463 0.31228 0.05035  -0.03053 0.02816  223 LEU A CB  
1681 C CG  . LEU A 212 ? 0.38618 0.37182 0.38347 0.04878  -0.02472 0.03004  223 LEU A CG  
1682 C CD1 . LEU A 212 ? 0.34616 0.33736 0.35923 0.04913  -0.02822 0.02741  223 LEU A CD1 
1683 C CD2 . LEU A 212 ? 0.43672 0.41736 0.43098 0.05150  -0.02333 0.03827  223 LEU A CD2 
1684 N N   . PHE A 213 ? 0.32541 0.30894 0.30121 0.04382  -0.01269 0.02580  224 PHE A N   
1685 C CA  . PHE A 213 ? 0.36273 0.34525 0.33693 0.04274  -0.00534 0.03036  224 PHE A CA  
1686 C C   . PHE A 213 ? 0.36216 0.34250 0.35174 0.04030  -0.00302 0.03163  224 PHE A C   
1687 O O   . PHE A 213 ? 0.39535 0.37731 0.39550 0.03917  -0.00421 0.02624  224 PHE A O   
1688 C CB  . PHE A 213 ? 0.39696 0.38070 0.36685 0.04028  -0.00075 0.02610  224 PHE A CB  
1689 C CG  . PHE A 213 ? 0.48374 0.46790 0.43981 0.04337  -0.00462 0.02172  224 PHE A CG  
1690 C CD1 . PHE A 213 ? 0.46497 0.44789 0.42402 0.04172  -0.01071 0.01500  224 PHE A CD1 
1691 C CD2 . PHE A 213 ? 0.52839 0.51478 0.46926 0.04827  -0.00265 0.02446  224 PHE A CD2 
1692 C CE1 . PHE A 213 ? 0.46349 0.44393 0.41083 0.04475  -0.01653 0.01008  224 PHE A CE1 
1693 C CE2 . PHE A 213 ? 0.49001 0.47566 0.41717 0.05298  -0.00747 0.01844  224 PHE A CE2 
1694 C CZ  . PHE A 213 ? 0.51773 0.49867 0.44828 0.05110  -0.01524 0.01071  224 PHE A CZ  
1695 N N   . ALA A 214 ? 0.30691 0.28425 0.29828 0.03988  -0.00017 0.03892  225 ALA A N   
1696 C CA  . ALA A 214 ? 0.33071 0.30316 0.33662 0.03828  -0.00002 0.03899  225 ALA A CA  
1697 C C   . ALA A 214 ? 0.35185 0.32110 0.36040 0.03514  0.00364  0.04589  225 ALA A C   
1698 O O   . ALA A 214 ? 0.38104 0.35271 0.38217 0.03533  0.00532  0.05529  225 ALA A O   
1699 C CB  . ALA A 214 ? 0.27912 0.24810 0.29150 0.04185  -0.00585 0.04200  225 ALA A CB  
1700 N N   . ASN A 215 ? 0.34925 0.31436 0.36880 0.03260  0.00447  0.04149  226 ASN A N   
1701 C CA  . ASN A 215 ? 0.33852 0.29860 0.36566 0.02884  0.00542  0.04771  226 ASN A CA  
1702 C C   . ASN A 215 ? 0.31863 0.26845 0.35977 0.03011  -0.00072 0.04628  226 ASN A C   
1703 O O   . ASN A 215 ? 0.34492 0.29279 0.39207 0.03185  -0.00198 0.03552  226 ASN A O   
1704 C CB  . ASN A 215 ? 0.28640 0.24919 0.31386 0.02527  0.01001  0.04214  226 ASN A CB  
1705 C CG  . ASN A 215 ? 0.31746 0.27573 0.35473 0.02058  0.00998  0.04861  226 ASN A CG  
1706 O OD1 . ASN A 215 ? 0.28909 0.23925 0.33667 0.01961  0.00503  0.05516  226 ASN A OD1 
1707 N ND2 . ASN A 215 ? 0.28713 0.25027 0.32262 0.01739  0.01455  0.04709  226 ASN A ND2 
1708 N N   . PRO A 216 ? 0.33356 0.27685 0.38021 0.03007  -0.00515 0.05673  227 PRO A N   
1709 C CA  . PRO A 216 ? 0.33400 0.26558 0.39385 0.03284  -0.01291 0.05422  227 PRO A CA  
1710 C C   . PRO A 216 ? 0.36970 0.29144 0.44210 0.03024  -0.01623 0.05004  227 PRO A C   
1711 O O   . PRO A 216 ? 0.38674 0.29692 0.47010 0.03362  -0.02411 0.04639  227 PRO A O   
1712 C CB  . PRO A 216 ? 0.31624 0.24371 0.37766 0.03262  -0.01697 0.06912  227 PRO A CB  
1713 C CG  . PRO A 216 ? 0.33454 0.26982 0.38950 0.02727  -0.01101 0.08108  227 PRO A CG  
1714 C CD  . PRO A 216 ? 0.32139 0.26822 0.36300 0.02788  -0.00353 0.07211  227 PRO A CD  
1715 N N   . ASN A 217 ? 0.37380 0.29907 0.44523 0.02506  -0.01163 0.04978  228 ASN A N   
1716 C CA  . ASN A 217 ? 0.32045 0.23537 0.40465 0.02222  -0.01658 0.04658  228 ASN A CA  
1717 C C   . ASN A 217 ? 0.38248 0.30473 0.46245 0.01893  -0.01056 0.04035  228 ASN A C   
1718 O O   . ASN A 217 ? 0.33478 0.25876 0.41827 0.01259  -0.00868 0.04821  228 ASN A O   
1719 C CB  . ASN A 217 ? 0.32704 0.23337 0.42329 0.01628  -0.02192 0.06217  228 ASN A CB  
1720 C CG  . ASN A 217 ? 0.48668 0.38085 0.59794 0.01254  -0.02914 0.05872  228 ASN A CG  
1721 O OD1 . ASN A 217 ? 0.42860 0.31721 0.54131 0.01715  -0.03261 0.04285  228 ASN A OD1 
1722 N ND2 . ASN A 217 ? 0.38976 0.28119 0.51228 0.00445  -0.03169 0.07373  228 ASN A ND2 
1723 N N   . ASN A 218 ? 0.38204 0.30992 0.45540 0.02332  -0.00763 0.02686  229 ASN A N   
1724 C CA  . ASN A 218 ? 0.31942 0.25236 0.39006 0.02131  -0.00369 0.01928  229 ASN A CA  
1725 C C   . ASN A 218 ? 0.33698 0.25952 0.41739 0.02430  -0.01111 0.00891  229 ASN A C   
1726 O O   . ASN A 218 ? 0.35907 0.28350 0.43741 0.03136  -0.01215 -0.00285 229 ASN A O   
1727 C CB  . ASN A 218 ? 0.24396 0.18946 0.30253 0.02408  0.00299  0.01233  229 ASN A CB  
1728 C CG  . ASN A 218 ? 0.32092 0.27195 0.37616 0.02188  0.00701  0.00600  229 ASN A CG  
1729 O OD1 . ASN A 218 ? 0.33008 0.27642 0.39129 0.01821  0.00523  0.00688  229 ASN A OD1 
1730 N ND2 . ASN A 218 ? 0.33106 0.29215 0.37795 0.02370  0.01165  0.00047  229 ASN A ND2 
1731 N N   . ASN A 219 ? 0.35528 0.26761 0.44692 0.01932  -0.01692 0.01357  230 ASN A N   
1732 C CA  . ASN A 219 ? 0.36226 0.26084 0.46459 0.02216  -0.02717 0.00393  230 ASN A CA  
1733 C C   . ASN A 219 ? 0.37002 0.26031 0.47510 0.03150  -0.03419 -0.00390 230 ASN A C   
1734 O O   . ASN A 219 ? 0.38970 0.27785 0.49405 0.03971  -0.03809 -0.01875 230 ASN A O   
1735 C CB  . ASN A 219 ? 0.42570 0.32968 0.52301 0.02386  -0.02498 -0.00869 230 ASN A CB  
1736 C CG  . ASN A 219 ? 0.40761 0.31494 0.50766 0.01482  -0.02221 -0.00177 230 ASN A CG  
1737 O OD1 . ASN A 219 ? 0.34566 0.25569 0.44925 0.00768  -0.01935 0.01298  230 ASN A OD1 
1738 N ND2 . ASN A 219 ? 0.34160 0.25073 0.43968 0.01589  -0.02282 -0.01213 230 ASN A ND2 
1739 N N   . GLY A 220 ? 0.40268 0.28956 0.51047 0.03118  -0.03581 0.00630  231 GLY A N   
1740 C CA  . GLY A 220 ? 0.38177 0.25957 0.49432 0.03972  -0.04358 0.00108  231 GLY A CA  
1741 C C   . GLY A 220 ? 0.41837 0.30980 0.52069 0.04685  -0.03710 -0.00350 231 GLY A C   
1742 O O   . GLY A 220 ? 0.44108 0.32778 0.54711 0.05263  -0.04207 -0.00303 231 GLY A O   
1743 N N   . ALA A 221 ? 0.41646 0.32449 0.50752 0.04631  -0.02708 -0.00729 232 ALA A N   
1744 C CA  . ALA A 221 ? 0.37028 0.29256 0.45378 0.05119  -0.02141 -0.00969 232 ALA A CA  
1745 C C   . ALA A 221 ? 0.38292 0.31102 0.45988 0.04516  -0.01636 0.00321  232 ALA A C   
1746 O O   . ALA A 221 ? 0.34500 0.27181 0.41969 0.03769  -0.01374 0.01230  232 ALA A O   
1747 C CB  . ALA A 221 ? 0.33667 0.27382 0.41292 0.05357  -0.01458 -0.01958 232 ALA A CB  
1748 N N   . LEU A 222 ? 0.28420 0.26118 0.33519 0.02412  -0.03090 0.02343  233 LEU A N   
1749 C CA  . LEU A 222 ? 0.28998 0.27269 0.33137 0.01926  -0.02168 0.03123  233 LEU A CA  
1750 C C   . LEU A 222 ? 0.36488 0.35522 0.39297 0.01891  -0.01623 0.02641  233 LEU A C   
1751 O O   . LEU A 222 ? 0.31178 0.30766 0.33531 0.02281  -0.01743 0.02088  233 LEU A O   
1752 C CB  . LEU A 222 ? 0.33490 0.31835 0.37254 0.02048  -0.02253 0.03538  233 LEU A CB  
1753 C CG  . LEU A 222 ? 0.34425 0.33105 0.36968 0.01842  -0.01602 0.04231  233 LEU A CG  
1754 C CD1 . LEU A 222 ? 0.32592 0.30962 0.35370 0.02001  -0.01777 0.05029  233 LEU A CD1 
1755 C CD2 . LEU A 222 ? 0.32228 0.31541 0.33560 0.01895  -0.01529 0.03663  233 LEU A CD2 
1756 N N   . HIS A 223 ? 0.28551 0.27694 0.30883 0.01498  -0.01024 0.02980  234 HIS A N   
1757 C CA  . HIS A 223 ? 0.32178 0.31866 0.33468 0.01386  -0.00641 0.02629  234 HIS A CA  
1758 C C   . HIS A 223 ? 0.31102 0.30868 0.31304 0.01245  -0.00417 0.03034  234 HIS A C   
1759 O O   . HIS A 223 ? 0.31785 0.31230 0.31653 0.01277  -0.00171 0.03662  234 HIS A O   
1760 C CB  . HIS A 223 ? 0.28922 0.28512 0.30326 0.01195  -0.00335 0.02490  234 HIS A CB  
1761 C CG  . HIS A 223 ? 0.31904 0.31975 0.32454 0.01092  -0.00047 0.02150  234 HIS A CG  
1762 N ND1 . HIS A 223 ? 0.31319 0.31936 0.31925 0.01379  -0.00130 0.01670  234 HIS A ND1 
1763 C CD2 . HIS A 223 ? 0.37838 0.37919 0.37518 0.00841  0.00261  0.02298  234 HIS A CD2 
1764 C CE1 . HIS A 223 ? 0.35121 0.36121 0.35243 0.01140  0.00153  0.01694  234 HIS A CE1 
1765 N NE2 . HIS A 223 ? 0.31568 0.32118 0.31123 0.00788  0.00279  0.01958  234 HIS A NE2 
1766 N N   . PHE A 224 ? 0.30606 0.30820 0.30343 0.01217  -0.00577 0.02753  235 PHE A N   
1767 C CA  . PHE A 224 ? 0.36655 0.36672 0.35391 0.01196  -0.00753 0.02924  235 PHE A CA  
1768 C C   . PHE A 224 ? 0.32259 0.32570 0.30894 0.00953  -0.00940 0.02620  235 PHE A C   
1769 O O   . PHE A 224 ? 0.31826 0.32809 0.31291 0.00835  -0.00828 0.02478  235 PHE A O   
1770 C CB  . PHE A 224 ? 0.32588 0.32598 0.31329 0.01414  -0.01216 0.03106  235 PHE A CB  
1771 C CG  . PHE A 224 ? 0.31388 0.32160 0.31024 0.01389  -0.01583 0.02908  235 PHE A CG  
1772 C CD1 . PHE A 224 ? 0.29420 0.30654 0.29930 0.01664  -0.01544 0.02812  235 PHE A CD1 
1773 C CD2 . PHE A 224 ? 0.33202 0.34245 0.32945 0.01218  -0.02074 0.02889  235 PHE A CD2 
1774 C CE1 . PHE A 224 ? 0.31362 0.33594 0.32662 0.01880  -0.01717 0.02818  235 PHE A CE1 
1775 C CE2 . PHE A 224 ? 0.34872 0.36936 0.35910 0.01212  -0.02318 0.03036  235 PHE A CE2 
1776 C CZ  . PHE A 224 ? 0.37504 0.40299 0.39229 0.01603  -0.02004 0.03063  235 PHE A CZ  
1777 N N   . GLY A 225 ? 0.30350 0.30107 0.27935 0.01017  -0.01283 0.02574  236 GLY A N   
1778 C CA  . GLY A 225 ? 0.28124 0.27845 0.25803 0.00771  -0.01793 0.02320  236 GLY A CA  
1779 C C   . GLY A 225 ? 0.30227 0.29305 0.27266 0.01000  -0.02821 0.02178  236 GLY A C   
1780 O O   . GLY A 225 ? 0.34442 0.32833 0.29981 0.01586  -0.02935 0.02167  236 GLY A O   
1781 N N   . ILE A 226 ? 0.28459 0.27812 0.26782 0.00630  -0.03628 0.02170  237 ILE A N   
1782 C CA  . ILE A 226 ? 0.27203 0.25781 0.25370 0.00791  -0.05020 0.01922  237 ILE A CA  
1783 C C   . ILE A 226 ? 0.34812 0.32866 0.33486 0.00495  -0.05838 0.01673  237 ILE A C   
1784 O O   . ILE A 226 ? 0.32496 0.31455 0.33013 -0.00128 -0.05552 0.02099  237 ILE A O   
1785 C CB  . ILE A 226 ? 0.29425 0.28824 0.29403 0.00546  -0.05527 0.02316  237 ILE A CB  
1786 C CG1 . ILE A 226 ? 0.33170 0.32751 0.32377 0.00961  -0.04939 0.02444  237 ILE A CG1 
1787 C CG2 . ILE A 226 ? 0.29250 0.27863 0.29802 0.00551  -0.07278 0.02081  237 ILE A CG2 
1788 C CD1 . ILE A 226 ? 0.26425 0.26886 0.27247 0.00855  -0.05301 0.02810  237 ILE A CD1 
1789 N N   . SER A 227 ? 0.33568 0.30143 0.30538 0.01095  -0.06900 0.01012  238 SER A N   
1790 C CA  . SER A 227 ? 0.34670 0.30337 0.31659 0.01028  -0.07827 0.00579  238 SER A CA  
1791 C C   . SER A 227 ? 0.41111 0.35328 0.37985 0.01442  -0.10023 -0.00043 238 SER A C   
1792 O O   . SER A 227 ? 0.41032 0.34479 0.36163 0.02325  -0.10628 -0.00463 238 SER A O   
1793 C CB  . SER A 227 ? 0.41007 0.36034 0.35544 0.01710  -0.07044 0.00158  238 SER A CB  
1794 O OG  . SER A 227 ? 0.37868 0.34063 0.32865 0.01275  -0.05326 0.00666  238 SER A OG  
1795 N N   . PHE A 228 ? 0.37326 0.31093 0.36140 0.00873  -0.11347 -0.00077 239 PHE A N   
1796 C CA  . PHE A 228 ? 0.38696 0.30953 0.38149 0.01135  -0.13859 -0.00669 239 PHE A CA  
1797 C C   . PHE A 228 ? 0.37752 0.29261 0.38967 0.00596  -0.15111 -0.00742 239 PHE A C   
1798 O O   . PHE A 228 ? 0.37221 0.29810 0.39697 -0.00161 -0.13870 -0.00051 239 PHE A O   
1799 C CB  . PHE A 228 ? 0.39506 0.32689 0.41702 0.00509  -0.14506 0.00029  239 PHE A CB  
1800 C CG  . PHE A 228 ? 0.40702 0.36210 0.46046 -0.00662 -0.13034 0.01437  239 PHE A CG  
1801 C CD1 . PHE A 228 ? 0.33756 0.29910 0.42596 -0.01612 -0.13693 0.02312  239 PHE A CD1 
1802 C CD2 . PHE A 228 ? 0.36852 0.33889 0.41607 -0.00644 -0.11019 0.01941  239 PHE A CD2 
1803 C CE1 . PHE A 228 ? 0.33270 0.31755 0.44667 -0.02343 -0.12176 0.03740  239 PHE A CE1 
1804 C CE2 . PHE A 228 ? 0.32419 0.31538 0.39577 -0.01327 -0.09714 0.03107  239 PHE A CE2 
1805 C CZ  . PHE A 228 ? 0.35517 0.35463 0.45835 -0.02085 -0.10183 0.04043  239 PHE A CZ  
1806 N N   . LYS A 229 ? 0.41089 0.30617 0.42382 0.01081  -0.17732 -0.01615 240 LYS A N   
1807 C CA  . LYS A 229 ? 0.48325 0.37026 0.52190 0.00404  -0.19400 -0.01536 240 LYS A CA  
1808 C C   . LYS A 229 ? 0.44479 0.35198 0.53245 -0.01214 -0.19049 0.00208  240 LYS A C   
1809 O O   . LYS A 229 ? 0.43039 0.34909 0.53620 -0.01591 -0.19003 0.00931  240 LYS A O   
1810 C CB  . LYS A 229 ? 0.52605 0.38627 0.56052 0.01283  -0.22730 -0.02853 240 LYS A CB  
1811 C CG  . LYS A 229 ? 0.64101 0.48018 0.62622 0.03217  -0.23292 -0.04569 240 LYS A CG  
1812 C CD  . LYS A 229 ? 0.70446 0.51470 0.68539 0.04306  -0.26960 -0.06044 240 LYS A CD  
1813 C CE  . LYS A 229 ? 0.81494 0.60466 0.74521 0.06542  -0.27542 -0.07742 240 LYS A CE  
1814 N NZ  . LYS A 229 ? 0.85213 0.61150 0.77947 0.07810  -0.30472 -0.09127 240 LYS A NZ  
1815 N N   . THR A 230 ? 0.46413 0.37714 0.57282 -0.02043 -0.18685 0.01006  241 THR A N   
1816 C CA  . THR A 230 ? 0.42005 0.35537 0.57458 -0.03348 -0.18074 0.02958  241 THR A CA  
1817 C C   . THR A 230 ? 0.49960 0.42982 0.69340 -0.03906 -0.20690 0.03478  241 THR A C   
1818 O O   . THR A 230 ? 0.54045 0.44985 0.74559 -0.03937 -0.23266 0.02872  241 THR A O   
1819 C CB  . THR A 230 ? 0.43074 0.37127 0.59864 -0.03954 -0.17361 0.03735  241 THR A CB  
1820 O OG1 . THR A 230 ? 0.46743 0.41250 0.60042 -0.03418 -0.15067 0.03210  241 THR A OG1 
1821 C CG2 . THR A 230 ? 0.42029 0.38706 0.63474 -0.05049 -0.16492 0.06043  241 THR A CG2 
1822 N N   . PRO A 231 ? 0.47178 0.41939 0.68831 -0.04297 -0.20305 0.04555  242 PRO A N   
1823 C CA  . PRO A 231 ? 0.51522 0.45821 0.77190 -0.04822 -0.22942 0.05083  242 PRO A CA  
1824 C C   . PRO A 231 ? 0.58408 0.52713 0.88924 -0.05906 -0.24491 0.06406  242 PRO A C   
1825 O O   . PRO A 231 ? 0.64310 0.60384 0.96435 -0.06526 -0.22761 0.07870  242 PRO A O   
1826 C CB  . PRO A 231 ? 0.46273 0.43325 0.73902 -0.05157 -0.21365 0.06541  242 PRO A CB  
1827 C CG  . PRO A 231 ? 0.42266 0.40033 0.65352 -0.04357 -0.18666 0.05822  242 PRO A CG  
1828 C CD  . PRO A 231 ? 0.41294 0.38436 0.61987 -0.04184 -0.17587 0.05280  242 PRO A CD  
1829 N N   . ASP A 232 ? 0.63141 0.55104 0.95452 -0.05867 -0.27423 0.05914  243 ASP A N   
1830 C CA  . ASP A 232 ? 0.83995 0.75056 1.19929 -0.06436 -0.28403 0.07174  243 ASP A CA  
1831 C C   . ASP A 232 ? 0.75197 0.69426 1.16145 -0.07499 -0.26812 0.10201  243 ASP A C   
1832 O O   . ASP A 232 ? 0.74255 0.69044 1.17895 -0.08008 -0.26475 0.11804  243 ASP A O   
1833 C CB  . ASP A 232 ? 0.90546 0.78031 1.26701 -0.05733 -0.31423 0.06042  243 ASP A CB  
1834 C CG  . ASP A 232 ? 1.05883 0.90093 1.36981 -0.04297 -0.32911 0.03240  243 ASP A CG  
1835 O OD1 . ASP A 232 ? 1.08117 0.91225 1.38285 -0.04098 -0.33165 0.02801  243 ASP A OD1 
1836 O OD2 . ASP A 232 ? 1.08913 0.91780 1.36811 -0.03217 -0.33679 0.01558  243 ASP A OD2 
1837 N N   . GLU A 233 ? 0.75318 0.71719 1.17379 -0.07646 -0.25737 0.11093  244 GLU A N   
1838 C CA  . GLU A 233 ? 0.75700 0.75385 1.21908 -0.08294 -0.23852 0.14018  244 GLU A CA  
1839 C C   . GLU A 233 ? 0.75515 0.77957 1.21546 -0.08494 -0.21154 0.15255  244 GLU A C   
1840 O O   . GLU A 233 ? 0.79158 0.83885 1.28372 -0.08759 -0.19700 0.17794  244 GLU A O   
1841 C CB  . GLU A 233 ? 0.77635 0.79156 1.24287 -0.08158 -0.23047 0.14440  244 GLU A CB  
1842 C CG  . GLU A 233 ? 0.79637 0.78622 1.26567 -0.07924 -0.25569 0.13340  244 GLU A CG  
1843 C CD  . GLU A 233 ? 0.86308 0.83443 1.28427 -0.07067 -0.26523 0.10515  244 GLU A CD  
1844 O OE1 . GLU A 233 ? 0.72442 0.69058 1.10965 -0.06655 -0.26084 0.09086  244 GLU A OE1 
1845 O OE2 . GLU A 233 ? 0.83011 0.79225 1.24874 -0.06709 -0.27686 0.09815  244 GLU A OE2 
1846 N N   . TRP A 234 ? 0.69918 0.72126 1.12198 -0.08226 -0.20488 0.13572  245 TRP A N   
1847 C CA  . TRP A 234 ? 0.79532 0.83851 1.20694 -0.08157 -0.17769 0.14402  245 TRP A CA  
1848 C C   . TRP A 234 ? 0.89103 0.92424 1.31308 -0.08627 -0.18385 0.14738  245 TRP A C   
1849 O O   . TRP A 234 ? 0.90291 0.93192 1.28810 -0.08138 -0.16891 0.13799  245 TRP A O   
1850 C CB  . TRP A 234 ? 0.63892 0.67462 0.98795 -0.07082 -0.15999 0.12299  245 TRP A CB  
1851 C CG  . TRP A 234 ? 0.56839 0.61529 0.90272 -0.06515 -0.14939 0.12033  245 TRP A CG  
1852 C CD1 . TRP A 234 ? 0.60185 0.65998 0.96699 -0.06766 -0.15728 0.13012  245 TRP A CD1 
1853 C CD2 . TRP A 234 ? 0.53109 0.57829 0.81774 -0.05599 -0.13001 0.10718  245 TRP A CD2 
1854 N NE1 . TRP A 234 ? 0.54574 0.61071 0.88288 -0.06012 -0.14357 0.12313  245 TRP A NE1 
1855 C CE2 . TRP A 234 ? 0.51122 0.56914 0.80105 -0.05314 -0.12729 0.10926  245 TRP A CE2 
1856 C CE3 . TRP A 234 ? 0.42270 0.46216 0.66742 -0.05022 -0.11574 0.09467  245 TRP A CE3 
1857 C CZ2 . TRP A 234 ? 0.38170 0.44158 0.63437 -0.04487 -0.11157 0.09920  245 TRP A CZ2 
1858 C CZ3 . TRP A 234 ? 0.47201 0.51411 0.68255 -0.04253 -0.10047 0.08554  245 TRP A CZ3 
1859 C CH2 . TRP A 234 ? 0.42634 0.47802 0.64111 -0.03999 -0.09882 0.08783  245 TRP A CH2 
1860 N N   . LYS A 235 ? 1.01137 1.03181 1.46386 -0.08868 -0.19932 0.15815  246 LYS A N   
1861 C CA  . LYS A 235 ? 1.03261 1.04969 1.49414 -0.09061 -0.19829 0.16603  246 LYS A CA  
1862 C C   . LYS A 235 ? 1.14081 1.19401 1.61877 -0.09061 -0.16901 0.19152  246 LYS A C   
1863 O O   . LYS A 235 ? 1.11946 1.17464 1.60657 -0.09125 -0.16534 0.20128  246 LYS A O   
1864 C CB  . LYS A 235 ? 0.95597 0.94997 1.44752 -0.09160 -0.22482 0.17127  246 LYS A CB  
1865 C CG  . LYS A 235 ? 1.03861 0.99148 1.50370 -0.08730 -0.25353 0.14306  246 LYS A CG  
1866 C CD  . LYS A 235 ? 1.11519 1.04429 1.61252 -0.08627 -0.28228 0.14816  246 LYS A CD  
1867 C CE  . LYS A 235 ? 1.10906 1.03500 1.62634 -0.08758 -0.28741 0.15891  246 LYS A CE  
1868 N NZ  . LYS A 235 ? 0.97513 0.87416 1.45487 -0.08210 -0.29877 0.13433  246 LYS A NZ  
1869 N N   . ASN A 236 ? 1.42020 1.50153 1.89938 -0.08762 -0.14860 0.20177  247 ASN A N   
1870 C CA  . ASN A 236 ? 1.32009 1.43560 1.80053 -0.08231 -0.11810 0.22104  247 ASN A CA  
1871 C C   . ASN A 236 ? 1.34058 1.47471 1.79480 -0.07685 -0.09921 0.21336  247 ASN A C   
1872 O O   . ASN A 236 ? 1.43423 1.59747 1.88996 -0.06867 -0.07570 0.22939  247 ASN A O   
1873 C CB  . ASN A 236 ? 1.39066 1.52604 1.91050 -0.07958 -0.11256 0.25091  247 ASN A CB  
1874 C CG  . ASN A 236 ? 1.57065 1.71441 2.10650 -0.07772 -0.10603 0.26909  247 ASN A CG  
1875 O OD1 . ASN A 236 ? 1.57713 1.70542 2.09982 -0.08066 -0.11184 0.25810  247 ASN A OD1 
1876 N ND2 . ASN A 236 ? 1.56285 1.73161 2.12694 -0.07187 -0.09409 0.29752  247 ASN A ND2 
1877 N N   . GLN A 237 ? 1.15559 1.26619 1.57161 -0.07525 -0.10827 0.18595  248 GLN A N   
1878 C CA  . GLN A 237 ? 1.01942 1.13469 1.39435 -0.06518 -0.09190 0.17288  248 GLN A CA  
1879 C C   . GLN A 237 ? 1.05731 1.19931 1.45920 -0.06299 -0.08489 0.18942  248 GLN A C   
1880 O O   . GLN A 237 ? 0.93880 1.09684 1.31836 -0.05304 -0.06496 0.18892  248 GLN A O   
1881 C CB  . GLN A 237 ? 1.02917 1.15214 1.36721 -0.05616 -0.06749 0.16866  248 GLN A CB  
1882 C CG  . GLN A 237 ? 0.80380 0.91639 1.09129 -0.04740 -0.05840 0.14644  248 GLN A CG  
1883 C CD  . GLN A 237 ? 0.97618 1.08859 1.22942 -0.04023 -0.04120 0.13903  248 GLN A CD  
1884 O OE1 . GLN A 237 ? 0.92498 1.05028 1.15850 -0.03059 -0.02431 0.13790  248 GLN A OE1 
1885 N NE2 . GLN A 237 ? 1.00520 1.10179 1.25179 -0.04421 -0.04725 0.13321  248 GLN A NE2 
1886 N N   . THR A 238 ? 1.16173 1.30781 1.61312 -0.07175 -0.10292 0.20385  249 THR A N   
1887 C CA  . THR A 238 ? 1.19359 1.36135 1.66780 -0.06769 -0.09440 0.22189  249 THR A CA  
1888 C C   . THR A 238 ? 1.12375 1.29497 1.57934 -0.06331 -0.09396 0.20809  249 THR A C   
1889 O O   . THR A 238 ? 0.97864 1.12341 1.38842 -0.06036 -0.09895 0.18177  249 THR A O   
1890 C CB  . THR A 238 ? 1.15682 1.31117 1.66866 -0.07412 -0.11410 0.23433  249 THR A CB  
1891 O OG1 . THR A 238 ? 1.11508 1.24431 1.62357 -0.07848 -0.13872 0.21573  249 THR A OG1 
1892 C CG2 . THR A 238 ? 1.12185 1.26141 1.64863 -0.07897 -0.12414 0.24069  249 THR A CG2 
1893 N N   . GLN A 239 ? 1.25191 1.44459 1.72444 -0.05827 -0.08394 0.22341  250 GLN A N   
1894 C CA  . GLN A 239 ? 1.31925 1.51745 1.78324 -0.05384 -0.08487 0.21506  250 GLN A CA  
1895 C C   . GLN A 239 ? 1.21671 1.41640 1.62805 -0.04101 -0.06420 0.19992  250 GLN A C   
1896 O O   . GLN A 239 ? 1.12535 1.34333 1.53360 -0.03218 -0.05248 0.20430  250 GLN A O   
1897 C CB  . GLN A 239 ? 1.40031 1.56682 1.86030 -0.06100 -0.11380 0.19537  250 GLN A CB  
1898 C CG  . GLN A 239 ? 1.46466 1.62326 1.95989 -0.06674 -0.12997 0.20625  250 GLN A CG  
1899 C CD  . GLN A 239 ? 1.52939 1.65048 2.02662 -0.07410 -0.16052 0.19143  250 GLN A CD  
1900 O OE1 . GLN A 239 ? 1.56641 1.66642 2.03243 -0.07313 -0.17274 0.16813  250 GLN A OE1 
1901 N NE2 . GLN A 239 ? 1.43407 1.54564 1.96672 -0.07951 -0.17357 0.20527  250 GLN A NE2 
1902 N N   . VAL A 240 ? 0.86329 1.04281 1.23358 -0.03922 -0.06043 0.18206  251 VAL A N   
1903 C CA  . VAL A 240 ? 0.59245 0.76783 0.91414 -0.02820 -0.04493 0.16590  251 VAL A CA  
1904 C C   . VAL A 240 ? 0.48071 0.67321 0.79285 -0.01995 -0.02409 0.17447  251 VAL A C   
1905 O O   . VAL A 240 ? 0.40186 0.58415 0.70546 -0.02323 -0.02402 0.17126  251 VAL A O   
1906 C CB  . VAL A 240 ? 0.46049 0.60174 0.74182 -0.03028 -0.05541 0.13956  251 VAL A CB  
1907 C CG1 . VAL A 240 ? 0.36734 0.50686 0.60720 -0.01991 -0.03971 0.12680  251 VAL A CG1 
1908 C CG2 . VAL A 240 ? 0.43869 0.56427 0.72470 -0.03453 -0.07513 0.13100  251 VAL A CG2 
1909 N N   . ASP A 241 ? 0.31478 0.53297 0.62660 -0.00744 -0.00709 0.18471  252 ASP A N   
1910 C CA  . ASP A 241 ? 0.33995 0.57407 0.63373 0.00590  0.01298  0.18962  252 ASP A CA  
1911 C C   . ASP A 241 ? 0.35880 0.57592 0.60421 0.01481  0.01718  0.16557  252 ASP A C   
1912 O O   . ASP A 241 ? 0.30026 0.51857 0.53596 0.02094  0.01745  0.15933  252 ASP A O   
1913 C CB  . ASP A 241 ? 0.27259 0.54490 0.59390 0.01744  0.02763  0.21522  252 ASP A CB  
1914 C CG  . ASP A 241 ? 0.24960 0.53863 0.54422 0.03735  0.04808  0.21744  252 ASP A CG  
1915 O OD1 . ASP A 241 ? 0.38078 0.65480 0.64506 0.03984  0.05095  0.20419  252 ASP A OD1 
1916 O OD2 . ASP A 241 ? 0.32776 0.64581 0.63215 0.05213  0.06081  0.23288  252 ASP A OD2 
1917 N N   . PHE A 242 ? 0.31145 0.51200 0.52911 0.01496  0.01909  0.15247  253 PHE A N   
1918 C CA  . PHE A 242 ? 0.30208 0.48457 0.48032 0.02104  0.02002  0.13070  253 PHE A CA  
1919 C C   . PHE A 242 ? 0.30592 0.50376 0.46646 0.03971  0.03398  0.13098  253 PHE A C   
1920 O O   . PHE A 242 ? 0.37930 0.56304 0.51167 0.04567  0.03313  0.11408  253 PHE A O   
1921 C CB  . PHE A 242 ? 0.35886 0.51737 0.51606 0.01422  0.01539  0.11635  253 PHE A CB  
1922 C CG  . PHE A 242 ? 0.34838 0.48574 0.51030 0.00040  -0.00049 0.10891  253 PHE A CG  
1923 C CD1 . PHE A 242 ? 0.29783 0.41780 0.44167 -0.00097 -0.00792 0.09437  253 PHE A CD1 
1924 C CD2 . PHE A 242 ? 0.34617 0.48156 0.53181 -0.00961 -0.00909 0.11743  253 PHE A CD2 
1925 C CE1 . PHE A 242 ? 0.37934 0.48058 0.52390 -0.00996 -0.02261 0.08750  253 PHE A CE1 
1926 C CE2 . PHE A 242 ? 0.34978 0.46411 0.53723 -0.01919 -0.02616 0.10887  253 PHE A CE2 
1927 C CZ  . PHE A 242 ? 0.35925 0.45692 0.52428 -0.01831 -0.03249 0.09364  253 PHE A CZ  
1928 N N   . GLN A 243 ? 0.29525 0.52161 0.47255 0.05024  0.04589  0.15044  254 GLN A N   
1929 C CA  . GLN A 243 ? 0.40195 0.64650 0.56393 0.07210  0.05833  0.15271  254 GLN A CA  
1930 C C   . GLN A 243 ? 0.39201 0.64669 0.56161 0.07785  0.05736  0.15496  254 GLN A C   
1931 O O   . GLN A 243 ? 0.39619 0.66057 0.54760 0.09722  0.06466  0.15182  254 GLN A O   
1932 C CB  . GLN A 243 ? 0.38258 0.65739 0.55986 0.08390  0.07309  0.17587  254 GLN A CB  
1933 C CG  . GLN A 243 ? 0.46444 0.73230 0.63812 0.07864  0.07470  0.17698  254 GLN A CG  
1934 C CD  . GLN A 243 ? 0.61232 0.85789 0.74489 0.08559  0.07323  0.15345  254 GLN A CD  
1935 O OE1 . GLN A 243 ? 0.69829 0.91878 0.82183 0.07176  0.06398  0.13943  254 GLN A OE1 
1936 N NE2 . GLN A 243 ? 0.65966 0.91408 0.76759 0.10837  0.08128  0.14889  254 GLN A NE2 
1937 N N   . ASN A 244 ? 0.32641 0.57837 0.52177 0.06293  0.04731  0.15968  255 ASN A N   
1938 C CA  . ASN A 244 ? 0.29620 0.56006 0.50485 0.06700  0.04584  0.16469  255 ASN A CA  
1939 C C   . ASN A 244 ? 0.27505 0.50965 0.46913 0.05600  0.03102  0.14444  255 ASN A C   
1940 O O   . ASN A 244 ? 0.26099 0.48211 0.46994 0.03949  0.01858  0.14338  255 ASN A O   
1941 C CB  . ASN A 244 ? 0.27241 0.56043 0.52892 0.05963  0.04577  0.19041  255 ASN A CB  
1942 C CG  . ASN A 244 ? 0.24284 0.54637 0.51774 0.06398  0.04459  0.19808  255 ASN A CG  
1943 O OD1 . ASN A 244 ? 0.24259 0.53409 0.49442 0.06933  0.04087  0.18204  255 ASN A OD1 
1944 N ND2 . ASN A 244 ? 0.22620 0.55703 0.54615 0.06125  0.04714  0.22408  255 ASN A ND2 
1945 N N   . ARG A 245 ? 0.27273 0.49665 0.43748 0.06628  0.03136  0.12853  256 ARG A N   
1946 C CA  . ARG A 245 ? 0.24873 0.44556 0.39909 0.05672  0.01884  0.11131  256 ARG A CA  
1947 C C   . ARG A 245 ? 0.27734 0.47705 0.45167 0.04799  0.00955  0.11765  256 ARG A C   
1948 O O   . ARG A 245 ? 0.21231 0.39086 0.38340 0.03584  -0.00265 0.10855  256 ARG A O   
1949 C CB  . ARG A 245 ? 0.26446 0.45076 0.38531 0.06943  0.01975  0.09587  256 ARG A CB  
1950 C CG  . ARG A 245 ? 0.38588 0.58861 0.51026 0.08377  0.02300  0.10013  256 ARG A CG  
1951 C CD  . ARG A 245 ? 0.38375 0.56937 0.48097 0.09369  0.01866  0.08259  256 ARG A CD  
1952 N NE  . ARG A 245 ? 0.36510 0.52378 0.45415 0.07968  0.00754  0.07041  256 ARG A NE  
1953 C CZ  . ARG A 245 ? 0.31237 0.46566 0.40874 0.07321  0.00004  0.06998  256 ARG A CZ  
1954 N NH1 . ARG A 245 ? 0.29149 0.46332 0.40526 0.07804  0.00121  0.07995  256 ARG A NH1 
1955 N NH2 . ARG A 245 ? 0.29050 0.42041 0.37689 0.06262  -0.00846 0.06040  256 ARG A NH2 
1956 N N   . ASN A 246 ? 0.25162 0.47809 0.45052 0.05517  0.01487  0.13393  257 ASN A N   
1957 C CA  . ASN A 246 ? 0.25722 0.48721 0.48215 0.04715  0.00470  0.14043  257 ASN A CA  
1958 C C   . ASN A 246 ? 0.25348 0.47541 0.50351 0.02956  -0.00760 0.14604  257 ASN A C   
1959 O O   . ASN A 246 ? 0.28475 0.49058 0.53956 0.01998  -0.02280 0.13938  257 ASN A O   
1960 C CB  . ASN A 246 ? 0.21503 0.47902 0.46570 0.05902  0.01416  0.15973  257 ASN A CB  
1961 C CG  . ASN A 246 ? 0.22083 0.49113 0.44521 0.07898  0.02363  0.15252  257 ASN A CG  
1962 O OD1 . ASN A 246 ? 0.29254 0.54056 0.48978 0.08021  0.01725  0.13378  257 ASN A OD1 
1963 N ND2 . ASN A 246 ? 0.28611 0.58678 0.51827 0.09620  0.03852  0.16792  257 ASN A ND2 
1964 N N   . SER A 247 ? 0.28293 0.51494 0.54866 0.02642  -0.00250 0.15798  258 SER A N   
1965 C CA  . SER A 247 ? 0.27426 0.49527 0.56302 0.01038  -0.01645 0.16170  258 SER A CA  
1966 C C   . SER A 247 ? 0.26415 0.44969 0.52188 0.00257  -0.02864 0.13903  258 SER A C   
1967 O O   . SER A 247 ? 0.31030 0.47939 0.57728 -0.00725 -0.04623 0.13418  258 SER A O   
1968 C CB  . SER A 247 ? 0.24187 0.47944 0.54999 0.00982  -0.00733 0.17848  258 SER A CB  
1969 O OG  . SER A 247 ? 0.46210 0.68229 0.78355 -0.00473 -0.02171 0.17708  258 SER A OG  
1970 N N   . VAL A 248 ? 0.21540 0.38919 0.43634 0.00836  -0.02014 0.12531  259 VAL A N   
1971 C CA  . VAL A 248 ? 0.23788 0.38173 0.43047 0.00259  -0.02886 0.10675  259 VAL A CA  
1972 C C   . VAL A 248 ? 0.25901 0.38835 0.43760 0.00296  -0.03790 0.09549  259 VAL A C   
1973 O O   . VAL A 248 ? 0.22524 0.33426 0.39652 -0.00330 -0.05132 0.08669  259 VAL A O   
1974 C CB  . VAL A 248 ? 0.26381 0.40152 0.42663 0.00858  -0.01738 0.09764  259 VAL A CB  
1975 C CG1 . VAL A 248 ? 0.25404 0.36415 0.39203 0.00268  -0.02506 0.08191  259 VAL A CG1 
1976 C CG2 . VAL A 248 ? 0.24761 0.40166 0.42325 0.01042  -0.00761 0.10984  259 VAL A CG2 
1977 N N   . VAL A 249 ? 0.22996 0.36895 0.40259 0.01204  -0.03099 0.09537  260 VAL A N   
1978 C CA  . VAL A 249 ? 0.22266 0.34961 0.38399 0.01301  -0.03897 0.08660  260 VAL A CA  
1979 C C   . VAL A 249 ? 0.22804 0.35316 0.41295 0.00559  -0.05456 0.09122  260 VAL A C   
1980 O O   . VAL A 249 ? 0.26620 0.37141 0.43782 0.00282  -0.06673 0.08115  260 VAL A O   
1981 C CB  . VAL A 249 ? 0.22166 0.36212 0.37883 0.02471  -0.02999 0.08794  260 VAL A CB  
1982 C CG1 . VAL A 249 ? 0.22749 0.35922 0.38058 0.02527  -0.03905 0.08248  260 VAL A CG1 
1983 C CG2 . VAL A 249 ? 0.23533 0.36980 0.36546 0.03271  -0.02011 0.07885  260 VAL A CG2 
1984 N N   . ASP A 250 ? 0.23234 0.37843 0.45375 0.00319  -0.05515 0.10737  261 ASP A N   
1985 C CA  . ASP A 250 ? 0.24697 0.39188 0.49717 -0.00403 -0.07256 0.11274  261 ASP A CA  
1986 C C   . ASP A 250 ? 0.31791 0.43829 0.56374 -0.01267 -0.08938 0.10389  261 ASP A C   
1987 O O   . ASP A 250 ? 0.25213 0.35566 0.49586 -0.01485 -0.10709 0.09589  261 ASP A O   
1988 C CB  . ASP A 250 ? 0.22561 0.40030 0.52171 -0.00536 -0.06900 0.13521  261 ASP A CB  
1989 C CG  . ASP A 250 ? 0.27515 0.45088 0.60659 -0.01223 -0.08796 0.14205  261 ASP A CG  
1990 O OD1 . ASP A 250 ? 0.26041 0.43786 0.59024 -0.00797 -0.09127 0.13933  261 ASP A OD1 
1991 O OD2 . ASP A 250 ? 0.34947 0.52295 0.71102 -0.02174 -0.10110 0.14966  261 ASP A OD2 
1992 N N   . PHE A 251 ? 0.27048 0.38824 0.51372 -0.01600 -0.08491 0.10480  262 PHE A N   
1993 C CA  . PHE A 251 ? 0.29421 0.38795 0.53009 -0.02209 -0.10058 0.09527  262 PHE A CA  
1994 C C   . PHE A 251 ? 0.26408 0.33228 0.45641 -0.01734 -0.10455 0.07592  262 PHE A C   
1995 O O   . PHE A 251 ? 0.31365 0.36173 0.49915 -0.01797 -0.12303 0.06672  262 PHE A O   
1996 C CB  . PHE A 251 ? 0.27656 0.37399 0.51560 -0.02524 -0.09229 0.10021  262 PHE A CB  
1997 C CG  . PHE A 251 ? 0.29693 0.36830 0.51863 -0.02864 -0.10507 0.08757  262 PHE A CG  
1998 C CD1 . PHE A 251 ? 0.38105 0.44158 0.62753 -0.03529 -0.12709 0.08907  262 PHE A CD1 
1999 C CD2 . PHE A 251 ? 0.32781 0.38565 0.51020 -0.02429 -0.09611 0.07459  262 PHE A CD2 
2000 C CE1 . PHE A 251 ? 0.43227 0.46773 0.66006 -0.03578 -0.14000 0.07611  262 PHE A CE1 
2001 C CE2 . PHE A 251 ? 0.33361 0.36928 0.49880 -0.02525 -0.10671 0.06359  262 PHE A CE2 
2002 C CZ  . PHE A 251 ? 0.35576 0.37969 0.54137 -0.03010 -0.12866 0.06349  262 PHE A CZ  
2003 N N   . LEU A 252 ? 0.26025 0.32912 0.42379 -0.01128 -0.08821 0.07034  263 LEU A N   
2004 C CA  . LEU A 252 ? 0.26720 0.31480 0.39327 -0.00674 -0.08980 0.05587  263 LEU A CA  
2005 C C   . LEU A 252 ? 0.30111 0.34184 0.42067 -0.00273 -0.09928 0.05155  263 LEU A C   
2006 O O   . LEU A 252 ? 0.33126 0.35253 0.42797 0.00086  -0.10912 0.04164  263 LEU A O   
2007 C CB  . LEU A 252 ? 0.27708 0.32753 0.38102 -0.00245 -0.07154 0.05304  263 LEU A CB  
2008 C CG  . LEU A 252 ? 0.32815 0.37798 0.42739 -0.00484 -0.06397 0.05281  263 LEU A CG  
2009 C CD1 . LEU A 252 ? 0.30898 0.36241 0.39091 0.00007  -0.04835 0.05023  263 LEU A CD1 
2010 C CD2 . LEU A 252 ? 0.25637 0.28549 0.33884 -0.00619 -0.07398 0.04391  263 LEU A CD2 
2011 N N   . LEU A 253 ? 0.33157 0.38852 0.46953 -0.00158 -0.09632 0.05916  264 LEU A N   
2012 C CA  . LEU A 253 ? 0.35477 0.40529 0.48730 0.00235  -0.10578 0.05526  264 LEU A CA  
2013 C C   . LEU A 253 ? 0.31460 0.35250 0.45848 -0.00017 -0.12868 0.05227  264 LEU A C   
2014 O O   . LEU A 253 ? 0.37949 0.40231 0.50533 0.00512  -0.13969 0.04399  264 LEU A O   
2015 C CB  . LEU A 253 ? 0.26419 0.33579 0.41638 0.00474  -0.09859 0.06440  264 LEU A CB  
2016 C CG  . LEU A 253 ? 0.31395 0.39149 0.44749 0.01103  -0.08077 0.06287  264 LEU A CG  
2017 C CD1 . LEU A 253 ? 0.25060 0.34638 0.39912 0.01647  -0.07594 0.06975  264 LEU A CD1 
2018 C CD2 . LEU A 253 ? 0.27113 0.32782 0.37035 0.01455  -0.08096 0.05173  264 LEU A CD2 
2019 N N   . LYS A 254 ? 0.29951 0.34252 0.47368 -0.00730 -0.13743 0.05912  265 LYS A N   
2020 C CA  . LYS A 254 ? 0.37701 0.40424 0.56363 -0.00942 -0.16331 0.05465  265 LYS A CA  
2021 C C   . LYS A 254 ? 0.32533 0.32576 0.47588 -0.00435 -0.17202 0.03947  265 LYS A C   
2022 O O   . LYS A 254 ? 0.42796 0.40894 0.56182 0.00229  -0.19005 0.02879  265 LYS A O   
2023 C CB  . LYS A 254 ? 0.30242 0.34305 0.53741 -0.01912 -0.17128 0.06845  265 LYS A CB  
2024 C CG  . LYS A 254 ? 0.41779 0.48193 0.69381 -0.02214 -0.17184 0.08369  265 LYS A CG  
2025 C CD  . LYS A 254 ? 0.49398 0.58185 0.81801 -0.03051 -0.16751 0.10401  265 LYS A CD  
2026 C CE  . LYS A 254 ? 0.47269 0.58716 0.83986 -0.03191 -0.16704 0.12167  265 LYS A CE  
2027 N NZ  . LYS A 254 ? 0.43149 0.57540 0.84484 -0.03744 -0.15697 0.14583  265 LYS A NZ  
2028 N N   . GLU A 255 ? 0.37707 0.37671 0.51325 -0.00544 -0.15906 0.03832  266 GLU A N   
2029 C CA  . GLU A 255 ? 0.38867 0.36559 0.48983 0.00101  -0.16473 0.02515  266 GLU A CA  
2030 C C   . GLU A 255 ? 0.39894 0.36556 0.45990 0.01219  -0.15927 0.01663  266 GLU A C   
2031 O O   . GLU A 255 ? 0.44990 0.39668 0.48247 0.02172  -0.17046 0.00585  266 GLU A O   
2032 C CB  . GLU A 255 ? 0.36890 0.35003 0.46470 -0.00256 -0.14957 0.02715  266 GLU A CB  
2033 C CG  . GLU A 255 ? 0.40260 0.38847 0.53233 -0.01177 -0.15743 0.03443  266 GLU A CG  
2034 C CD  . GLU A 255 ? 0.53882 0.50333 0.67526 -0.01080 -0.18632 0.02648  266 GLU A CD  
2035 O OE1 . GLU A 255 ? 0.50958 0.45236 0.61064 -0.00014 -0.19641 0.01196  266 GLU A OE1 
2036 O OE2 . GLU A 255 ? 0.47591 0.44559 0.65382 -0.01947 -0.19967 0.03543  266 GLU A OE2 
2037 N N   . PHE A 256 ? 0.41078 0.39074 0.46866 0.01260  -0.14236 0.02199  267 PHE A N   
2038 C CA  . PHE A 256 ? 0.34818 0.32080 0.37301 0.02203  -0.13514 0.01742  267 PHE A CA  
2039 C C   . PHE A 256 ? 0.42120 0.39329 0.44864 0.02617  -0.14437 0.01742  267 PHE A C   
2040 O O   . PHE A 256 ? 0.40576 0.37847 0.41575 0.03166  -0.13489 0.01815  267 PHE A O   
2041 C CB  . PHE A 256 ? 0.42210 0.40639 0.44101 0.02026  -0.11203 0.02250  267 PHE A CB  
2042 C CG  . PHE A 256 ? 0.40847 0.38715 0.40983 0.02104  -0.10304 0.01974  267 PHE A CG  
2043 C CD1 . PHE A 256 ? 0.36509 0.34448 0.37878 0.01523  -0.10567 0.01966  267 PHE A CD1 
2044 C CD2 . PHE A 256 ? 0.41245 0.38572 0.38730 0.02772  -0.09234 0.01861  267 PHE A CD2 
2045 C CE1 . PHE A 256 ? 0.41201 0.38613 0.40937 0.01646  -0.09787 0.01679  267 PHE A CE1 
2046 C CE2 . PHE A 256 ? 0.40406 0.37348 0.36500 0.02883  -0.08419 0.01709  267 PHE A CE2 
2047 C CZ  . PHE A 256 ? 0.31666 0.28609 0.28754 0.02343  -0.08711 0.01529  267 PHE A CZ  
2048 N N   . SER A 257 ? 0.35540 0.32572 0.40634 0.02359  -0.16403 0.01711  268 SER A N   
2049 C CA  . SER A 257 ? 0.40370 0.37662 0.46383 0.02610  -0.17285 0.01845  268 SER A CA  
2050 C C   . SER A 257 ? 0.39982 0.35645 0.42216 0.03929  -0.17724 0.01034  268 SER A C   
2051 O O   . SER A 257 ? 0.38245 0.34364 0.40291 0.04242  -0.17439 0.01291  268 SER A O   
2052 C CB  . SER A 257 ? 0.39077 0.36259 0.48526 0.02114  -0.19641 0.01947  268 SER A CB  
2053 O OG  . SER A 257 ? 0.48807 0.43769 0.56896 0.02607  -0.21624 0.00866  268 SER A OG  
2054 N N   . ASP A 258 ? 0.44206 0.38048 0.43310 0.04876  -0.18362 0.00139  269 ASP A N   
2055 C CA  . ASP A 258 ? 0.56634 0.49179 0.52010 0.06402  -0.18601 -0.00387 269 ASP A CA  
2056 C C   . ASP A 258 ? 0.53619 0.46428 0.46206 0.06913  -0.16293 0.00025  269 ASP A C   
2057 O O   . ASP A 258 ? 0.54642 0.46422 0.43843 0.08367  -0.16266 -0.00215 269 ASP A O   
2058 C CB  . ASP A 258 ? 0.61166 0.51466 0.54522 0.07667  -0.21096 -0.01640 269 ASP A CB  
2059 C CG  . ASP A 258 ? 0.70409 0.59804 0.62683 0.07829  -0.21278 -0.02206 269 ASP A CG  
2060 O OD1 . ASP A 258 ? 0.76565 0.63997 0.67473 0.08885  -0.23608 -0.03370 269 ASP A OD1 
2061 O OD2 . ASP A 258 ? 0.77474 0.67974 0.70157 0.07031  -0.19268 -0.01590 269 ASP A OD2 
2062 N N   . TRP A 259 ? 0.41092 0.35333 0.35177 0.05848  -0.14406 0.00751  270 TRP A N   
2063 C CA  . TRP A 259 ? 0.45268 0.39869 0.37538 0.06146  -0.12369 0.01301  270 TRP A CA  
2064 C C   . TRP A 259 ? 0.44760 0.40219 0.37631 0.06049  -0.11447 0.02015  270 TRP A C   
2065 O O   . TRP A 259 ? 0.44573 0.40850 0.39740 0.05453  -0.11865 0.02172  270 TRP A O   
2066 C CB  . TRP A 259 ? 0.36786 0.32235 0.30231 0.05190  -0.11032 0.01577  270 TRP A CB  
2067 C CG  . TRP A 259 ? 0.47323 0.41881 0.39803 0.05380  -0.11611 0.00968  270 TRP A CG  
2068 C CD1 . TRP A 259 ? 0.44013 0.37703 0.37232 0.05340  -0.13516 0.00257  270 TRP A CD1 
2069 C CD2 . TRP A 259 ? 0.40900 0.35307 0.31726 0.05654  -0.10394 0.01039  270 TRP A CD2 
2070 N NE1 . TRP A 259 ? 0.44163 0.37068 0.36097 0.05617  -0.13578 -0.00214 270 TRP A NE1 
2071 C CE2 . TRP A 259 ? 0.44104 0.37526 0.34498 0.05829  -0.11589 0.00267  270 TRP A CE2 
2072 C CE3 . TRP A 259 ? 0.43978 0.38997 0.33981 0.05731  -0.08517 0.01740  270 TRP A CE3 
2073 C CZ2 . TRP A 259 ? 0.45772 0.38857 0.34606 0.06185  -0.10844 0.00118  270 TRP A CZ2 
2074 C CZ3 . TRP A 259 ? 0.43400 0.38202 0.32135 0.06006  -0.07765 0.01705  270 TRP A CZ3 
2075 C CH2 . TRP A 259 ? 0.46031 0.39908 0.34043 0.06274  -0.08860 0.00874  270 TRP A CH2 
2076 N N   . ASP A 260 ? 0.43364 0.38685 0.34306 0.06697  -0.10192 0.02560  271 ASP A N   
2077 C CA  . ASP A 260 ? 0.39210 0.35083 0.30610 0.06696  -0.09377 0.03300  271 ASP A CA  
2078 C C   . ASP A 260 ? 0.41088 0.38226 0.35317 0.05512  -0.08633 0.03543  271 ASP A C   
2079 O O   . ASP A 260 ? 0.37872 0.35534 0.33114 0.04819  -0.08053 0.03450  271 ASP A O   
2080 C CB  . ASP A 260 ? 0.41662 0.37276 0.31033 0.07477  -0.08088 0.04111  271 ASP A CB  
2081 C CG  . ASP A 260 ? 0.42949 0.38930 0.32942 0.07501  -0.07379 0.05019  271 ASP A CG  
2082 O OD1 . ASP A 260 ? 0.36851 0.33510 0.28769 0.06632  -0.06541 0.05380  271 ASP A OD1 
2083 O OD2 . ASP A 260 ? 0.54666 0.50150 0.43167 0.08493  -0.07778 0.05342  271 ASP A OD2 
2084 N N   . GLU A 261 ? 0.34877 0.32482 0.30197 0.05470  -0.08697 0.03827  272 GLU A N   
2085 C CA  . GLU A 261 ? 0.33325 0.32121 0.31011 0.04756  -0.08161 0.03957  272 GLU A CA  
2086 C C   . GLU A 261 ? 0.35124 0.34132 0.32986 0.04435  -0.06875 0.04227  272 GLU A C   
2087 O O   . GLU A 261 ? 0.34460 0.34365 0.33879 0.03982  -0.06472 0.04111  272 GLU A O   
2088 C CB  . GLU A 261 ? 0.33038 0.32103 0.31437 0.05044  -0.08464 0.04185  272 GLU A CB  
2089 C CG  . GLU A 261 ? 0.37608 0.36789 0.36644 0.05212  -0.09827 0.03913  272 GLU A CG  
2090 C CD  . GLU A 261 ? 0.36605 0.37165 0.38266 0.04564  -0.10110 0.03847  272 GLU A CD  
2091 O OE1 . GLU A 261 ? 0.38407 0.39928 0.41144 0.04160  -0.09121 0.04005  272 GLU A OE1 
2092 O OE2 . GLU A 261 ? 0.45376 0.46120 0.48161 0.04537  -0.11363 0.03740  272 GLU A OE2 
2093 N N   . ARG A 262 ? 0.36482 0.34763 0.32885 0.04775  -0.06250 0.04675  273 ARG A N   
2094 C CA  . ARG A 262 ? 0.33779 0.32210 0.30745 0.04402  -0.05237 0.04957  273 ARG A CA  
2095 C C   . ARG A 262 ? 0.34889 0.33732 0.32250 0.03875  -0.05001 0.04468  273 ARG A C   
2096 O O   . ARG A 262 ? 0.36939 0.36285 0.35490 0.03475  -0.04509 0.04352  273 ARG A O   
2097 C CB  . ARG A 262 ? 0.34972 0.32788 0.30669 0.04859  -0.04585 0.05812  273 ARG A CB  
2098 C CG  . ARG A 262 ? 0.37364 0.34918 0.33434 0.05195  -0.04553 0.06609  273 ARG A CG  
2099 C CD  . ARG A 262 ? 0.41187 0.38388 0.35901 0.05879  -0.03904 0.07785  273 ARG A CD  
2100 N NE  . ARG A 262 ? 0.40016 0.36858 0.32326 0.06844  -0.04351 0.07669  273 ARG A NE  
2101 C CZ  . ARG A 262 ? 0.51509 0.48140 0.42054 0.07914  -0.03887 0.08711  273 ARG A CZ  
2102 N NH1 . ARG A 262 ? 0.50103 0.47032 0.41402 0.07993  -0.02824 0.10200  273 ARG A NH1 
2103 N NH2 . ARG A 262 ? 0.49798 0.45939 0.37869 0.09042  -0.04573 0.08335  273 ARG A NH2 
2104 N N   . TYR A 263 ? 0.36115 0.34650 0.32456 0.03978  -0.05491 0.04123  274 TYR A N   
2105 C CA  . TYR A 263 ? 0.34153 0.33046 0.31087 0.03444  -0.05412 0.03712  274 TYR A CA  
2106 C C   . TYR A 263 ? 0.29964 0.29933 0.29004 0.02955  -0.05762 0.03538  274 TYR A C   
2107 O O   . TYR A 263 ? 0.28155 0.28864 0.28245 0.02540  -0.05233 0.03503  274 TYR A O   
2108 C CB  . TYR A 263 ? 0.36367 0.34445 0.31771 0.03787  -0.06131 0.03327  274 TYR A CB  
2109 C CG  . TYR A 263 ? 0.37534 0.34776 0.30529 0.04631  -0.05694 0.03597  274 TYR A CG  
2110 C CD1 . TYR A 263 ? 0.32662 0.29986 0.25255 0.04546  -0.04654 0.03867  274 TYR A CD1 
2111 C CD2 . TYR A 263 ? 0.36161 0.32652 0.27270 0.05666  -0.06319 0.03658  274 TYR A CD2 
2112 C CE1 . TYR A 263 ? 0.39767 0.36658 0.30342 0.05464  -0.04090 0.04368  274 TYR A CE1 
2113 C CE2 . TYR A 263 ? 0.44313 0.40307 0.33062 0.06741  -0.05755 0.04115  274 TYR A CE2 
2114 C CZ  . TYR A 263 ? 0.48833 0.45136 0.37423 0.06630  -0.04563 0.04554  274 TYR A CZ  
2115 O OH  . TYR A 263 ? 0.44891 0.41033 0.31341 0.07826  -0.03813 0.05269  274 TYR A OH  
2116 N N   . LYS A 264 ? 0.36794 0.36989 0.36516 0.03107  -0.06628 0.03542  275 LYS A N   
2117 C CA  . LYS A 264 ? 0.31669 0.33216 0.33695 0.02761  -0.06875 0.03679  275 LYS A CA  
2118 C C   . LYS A 264 ? 0.29033 0.31595 0.31969 0.02872  -0.05931 0.03874  275 LYS A C   
2119 O O   . LYS A 264 ? 0.32701 0.36556 0.37106 0.02735  -0.05542 0.04070  275 LYS A O   
2120 C CB  . LYS A 264 ? 0.30762 0.32368 0.33502 0.02963  -0.08050 0.03727  275 LYS A CB  
2121 C CG  . LYS A 264 ? 0.32911 0.33442 0.35021 0.03009  -0.09432 0.03354  275 LYS A CG  
2122 C CD  . LYS A 264 ? 0.32576 0.33400 0.36193 0.03089  -0.10786 0.03429  275 LYS A CD  
2123 C CE  . LYS A 264 ? 0.39259 0.38684 0.42247 0.03299  -0.12599 0.02854  275 LYS A CE  
2124 N NZ  . LYS A 264 ? 0.41055 0.40926 0.46440 0.03156  -0.14163 0.02999  275 LYS A NZ  
2125 N N   . GLU A 265 ? 0.32776 0.34732 0.34857 0.03260  -0.05634 0.03867  276 GLU A N   
2126 C CA  . GLU A 265 ? 0.34259 0.36734 0.36962 0.03558  -0.05056 0.03822  276 GLU A CA  
2127 C C   . GLU A 265 ? 0.31680 0.34344 0.34384 0.03357  -0.04349 0.03645  276 GLU A C   
2128 O O   . GLU A 265 ? 0.36131 0.39762 0.39614 0.03695  -0.03993 0.03540  276 GLU A O   
2129 C CB  . GLU A 265 ? 0.36465 0.37877 0.38454 0.03896  -0.05121 0.03901  276 GLU A CB  
2130 C CG  . GLU A 265 ? 0.41918 0.43397 0.44542 0.04331  -0.04932 0.03668  276 GLU A CG  
2131 C CD  . GLU A 265 ? 0.56910 0.57287 0.59407 0.04615  -0.05292 0.03883  276 GLU A CD  
2132 O OE1 . GLU A 265 ? 0.47396 0.46813 0.49331 0.04346  -0.05133 0.04357  276 GLU A OE1 
2133 O OE2 . GLU A 265 ? 0.57498 0.58057 0.60574 0.05186  -0.05719 0.03695  276 GLU A OE2 
2134 N N   . LEU A 266 ? 0.30848 0.32644 0.32544 0.02981  -0.04141 0.03622  277 LEU A N   
2135 C CA  . LEU A 266 ? 0.31860 0.33760 0.33529 0.02742  -0.03543 0.03450  277 LEU A CA  
2136 C C   . LEU A 266 ? 0.29493 0.32700 0.32229 0.02630  -0.03402 0.03480  277 LEU A C   
2137 O O   . LEU A 266 ? 0.28187 0.32087 0.31342 0.02911  -0.02906 0.03369  277 LEU A O   
2138 C CB  . LEU A 266 ? 0.35438 0.36391 0.35874 0.02439  -0.03421 0.03515  277 LEU A CB  
2139 C CG  . LEU A 266 ? 0.48826 0.49464 0.48944 0.02235  -0.02792 0.03444  277 LEU A CG  
2140 C CD1 . LEU A 266 ? 0.43822 0.44049 0.44372 0.02433  -0.02599 0.03559  277 LEU A CD1 
2141 C CD2 . LEU A 266 ? 0.40398 0.40286 0.39120 0.02198  -0.02733 0.03608  277 LEU A CD2 
2142 N N   . ILE A 267 ? 0.30322 0.33879 0.33625 0.02312  -0.03928 0.03711  278 ILE A N   
2143 C CA  . ILE A 267 ? 0.26116 0.31104 0.31058 0.02131  -0.03846 0.04115  278 ILE A CA  
2144 C C   . ILE A 267 ? 0.32203 0.38778 0.38375 0.02783  -0.03479 0.04478  278 ILE A C   
2145 O O   . ILE A 267 ? 0.33149 0.41071 0.40135 0.03093  -0.02819 0.04832  278 ILE A O   
2146 C CB  . ILE A 267 ? 0.36623 0.41423 0.42363 0.01643  -0.04870 0.04326  278 ILE A CB  
2147 C CG1 . ILE A 267 ? 0.26254 0.29527 0.30453 0.01331  -0.05206 0.03855  278 ILE A CG1 
2148 C CG2 . ILE A 267 ? 0.28313 0.34840 0.36624 0.01388  -0.04934 0.05136  278 ILE A CG2 
2149 C CD1 . ILE A 267 ? 0.28700 0.30957 0.32624 0.01281  -0.06589 0.03637  278 ILE A CD1 
2150 N N   . ARG A 268 ? 0.26711 0.33193 0.32873 0.03185  -0.03862 0.04428  279 ARG A N   
2151 C CA  . ARG A 268 ? 0.29093 0.37190 0.36439 0.03972  -0.03620 0.04809  279 ARG A CA  
2152 C C   . ARG A 268 ? 0.30301 0.38661 0.36871 0.04924  -0.02939 0.04414  279 ARG A C   
2153 O O   . ARG A 268 ? 0.29340 0.39419 0.36699 0.05823  -0.02440 0.04811  279 ARG A O   
2154 C CB  . ARG A 268 ? 0.24783 0.32541 0.32219 0.04192  -0.04324 0.04773  279 ARG A CB  
2155 C CG  . ARG A 268 ? 0.29776 0.38078 0.38779 0.03679  -0.05150 0.05329  279 ARG A CG  
2156 C CD  . ARG A 268 ? 0.27778 0.35890 0.36901 0.04040  -0.05841 0.05293  279 ARG A CD  
2157 N NE  . ARG A 268 ? 0.33227 0.39423 0.40249 0.04144  -0.06086 0.04651  279 ARG A NE  
2158 C CZ  . ARG A 268 ? 0.36416 0.41265 0.42466 0.03890  -0.06895 0.04473  279 ARG A CZ  
2159 N NH1 . ARG A 268 ? 0.38521 0.43414 0.45392 0.03533  -0.07840 0.04619  279 ARG A NH1 
2160 N NH2 . ARG A 268 ? 0.31928 0.35342 0.36227 0.04115  -0.06848 0.04208  279 ARG A NH2 
2161 N N   . VAL A 269 ? 0.27782 0.34525 0.32911 0.04882  -0.02972 0.03698  280 VAL A N   
2162 C CA  . VAL A 269 ? 0.31009 0.37597 0.35479 0.05885  -0.02776 0.03119  280 VAL A CA  
2163 C C   . VAL A 269 ? 0.30043 0.36787 0.34093 0.05959  -0.02230 0.02927  280 VAL A C   
2164 O O   . VAL A 269 ? 0.39017 0.45621 0.42435 0.06984  -0.02218 0.02341  280 VAL A O   
2165 C CB  . VAL A 269 ? 0.33876 0.38571 0.37598 0.05889  -0.03393 0.02541  280 VAL A CB  
2166 C CG1 . VAL A 269 ? 0.31630 0.36137 0.35645 0.05949  -0.03931 0.02746  280 VAL A CG1 
2167 C CG2 . VAL A 269 ? 0.30909 0.34262 0.34100 0.04874  -0.03343 0.02543  280 VAL A CG2 
2168 N N   . THR A 270 ? 0.28917 0.35811 0.33224 0.05026  -0.01934 0.03311  281 THR A N   
2169 C CA  . THR A 270 ? 0.28105 0.35128 0.32024 0.05052  -0.01422 0.03174  281 THR A CA  
2170 C C   . THR A 270 ? 0.30845 0.39793 0.35182 0.06203  -0.00785 0.03574  281 THR A C   
2171 O O   . THR A 270 ? 0.27838 0.38490 0.33501 0.06289  -0.00489 0.04518  281 THR A O   
2172 C CB  . THR A 270 ? 0.32258 0.39040 0.36465 0.03863  -0.01356 0.03549  281 THR A CB  
2173 O OG1 . THR A 270 ? 0.37209 0.42281 0.40577 0.03170  -0.01784 0.03189  281 THR A OG1 
2174 C CG2 . THR A 270 ? 0.28896 0.36071 0.32912 0.03921  -0.00787 0.03554  281 THR A CG2 
2175 N N   . SER A 271 ? 0.24377 0.33147 0.27681 0.07200  -0.00597 0.02961  282 SER A N   
2176 C CA  . SER A 271 ? 0.32433 0.43155 0.35730 0.08718  0.00090  0.03394  282 SER A CA  
2177 C C   . SER A 271 ? 0.31123 0.43236 0.35195 0.08322  0.00924  0.04388  282 SER A C   
2178 O O   . SER A 271 ? 0.39053 0.53423 0.44135 0.09102  0.01670  0.05540  282 SER A O   
2179 C CB  . SER A 271 ? 0.39416 0.49360 0.41065 0.10337  -0.00246 0.02240  282 SER A CB  
2180 O OG  . SER A 271 ? 0.56171 0.64268 0.57133 0.09657  -0.00690 0.01413  282 SER A OG  
2181 N N   . SER A 272 ? 0.32508 0.43446 0.36334 0.07164  0.00839  0.04129  283 SER A N   
2182 C CA  . SER A 272 ? 0.30140 0.42194 0.34869 0.06668  0.01473  0.05086  283 SER A CA  
2183 C C   . SER A 272 ? 0.32675 0.43104 0.37426 0.05020  0.01026  0.04784  283 SER A C   
2184 O O   . SER A 272 ? 0.36689 0.45281 0.40318 0.04618  0.00533  0.03796  283 SER A O   
2185 C CB  . SER A 272 ? 0.37654 0.50520 0.41338 0.08048  0.02153  0.05031  283 SER A CB  
2186 O OG  . SER A 272 ? 0.45780 0.56713 0.47769 0.08226  0.01636  0.03620  283 SER A OG  
2187 N N   . PHE A 273 ? 0.26664 0.37839 0.32863 0.04163  0.01153  0.05749  284 PHE A N   
2188 C CA  . PHE A 273 ? 0.29966 0.39696 0.36171 0.02820  0.00616  0.05496  284 PHE A CA  
2189 C C   . PHE A 273 ? 0.32021 0.42135 0.38446 0.02647  0.01075  0.05894  284 PHE A C   
2190 O O   . PHE A 273 ? 0.28304 0.40232 0.35731 0.03273  0.01773  0.06919  284 PHE A O   
2191 C CB  . PHE A 273 ? 0.25803 0.35576 0.33654 0.01900  -0.00149 0.06106  284 PHE A CB  
2192 C CG  . PHE A 273 ? 0.26896 0.36420 0.34725 0.02051  -0.00658 0.05868  284 PHE A CG  
2193 C CD1 . PHE A 273 ? 0.21754 0.32963 0.30641 0.02845  -0.00328 0.06533  284 PHE A CD1 
2194 C CD2 . PHE A 273 ? 0.28508 0.36226 0.35256 0.01515  -0.01436 0.05098  284 PHE A CD2 
2195 C CE1 . PHE A 273 ? 0.26952 0.37896 0.35860 0.02985  -0.00852 0.06307  284 PHE A CE1 
2196 C CE2 . PHE A 273 ? 0.32578 0.40058 0.39289 0.01692  -0.01922 0.04959  284 PHE A CE2 
2197 C CZ  . PHE A 273 ? 0.21962 0.30986 0.29806 0.02350  -0.01682 0.05515  284 PHE A CZ  
2198 N N   . VAL A 274 ? 0.34392 0.42910 0.39934 0.01875  0.00728  0.05224  285 VAL A N   
2199 C CA  . VAL A 274 ? 0.31842 0.40430 0.37584 0.01564  0.00992  0.05516  285 VAL A CA  
2200 C C   . VAL A 274 ? 0.34380 0.41950 0.40871 0.00430  0.00116  0.05597  285 VAL A C   
2201 O O   . VAL A 274 ? 0.33434 0.39386 0.38708 0.00064  -0.00470 0.04727  285 VAL A O   
2202 C CB  . VAL A 274 ? 0.36118 0.43668 0.40017 0.01897  0.01289  0.04525  285 VAL A CB  
2203 C CG1 . VAL A 274 ? 0.34015 0.41473 0.38080 0.01488  0.01464  0.04781  285 VAL A CG1 
2204 C CG2 . VAL A 274 ? 0.28347 0.36652 0.31446 0.03234  0.01804  0.04266  285 VAL A CG2 
2205 N N   . GLY A 275 ? 0.25070 0.33587 0.33616 0.00012  -0.00046 0.06707  286 GLY A N   
2206 C CA  . GLY A 275 ? 0.27065 0.34388 0.36402 -0.00929 -0.01168 0.06670  286 GLY A CA  
2207 C C   . GLY A 275 ? 0.33774 0.40322 0.42389 -0.01158 -0.01047 0.06385  286 GLY A C   
2208 O O   . GLY A 275 ? 0.31688 0.39233 0.40256 -0.00735 -0.00088 0.06822  286 GLY A O   
2209 N N   . LEU A 276 ? 0.32729 0.37467 0.40638 -0.01667 -0.02089 0.05618  287 LEU A N   
2210 C CA  . LEU A 276 ? 0.35945 0.39738 0.42941 -0.01820 -0.02082 0.05181  287 LEU A CA  
2211 C C   . LEU A 276 ? 0.31983 0.34047 0.39053 -0.02276 -0.03640 0.04681  287 LEU A C   
2212 O O   . LEU A 276 ? 0.29452 0.30215 0.34959 -0.02061 -0.04322 0.03759  287 LEU A O   
2213 C CB  . LEU A 276 ? 0.38060 0.41179 0.42483 -0.01328 -0.01265 0.04140  287 LEU A CB  
2214 C CG  . LEU A 276 ? 0.54471 0.56437 0.57696 -0.01421 -0.01338 0.03525  287 LEU A CG  
2215 C CD1 . LEU A 276 ? 0.28255 0.31115 0.31812 -0.01270 -0.00472 0.03957  287 LEU A CD1 
2216 C CD2 . LEU A 276 ? 0.49544 0.50401 0.50571 -0.01079 -0.01152 0.02531  287 LEU A CD2 
2217 N N   . ALA A 277 ? 0.32171 0.34156 0.40967 -0.02752 -0.04283 0.05288  288 ALA A N   
2218 C CA  . ALA A 277 ? 0.33740 0.33760 0.42389 -0.02992 -0.06002 0.04585  288 ALA A CA  
2219 C C   . ALA A 277 ? 0.39122 0.37724 0.44727 -0.02500 -0.05723 0.03302  288 ALA A C   
2220 O O   . ALA A 277 ? 0.37077 0.36241 0.41937 -0.02380 -0.04496 0.03354  288 ALA A O   
2221 C CB  . ALA A 277 ? 0.30955 0.31218 0.42677 -0.03674 -0.06896 0.05697  288 ALA A CB  
2222 N N   . THR A 278 ? 0.32504 0.29341 0.36307 -0.02058 -0.06868 0.02188  289 THR A N   
2223 C CA  . THR A 278 ? 0.36029 0.31660 0.37121 -0.01422 -0.06657 0.01157  289 THR A CA  
2224 C C   . THR A 278 ? 0.34735 0.29626 0.36525 -0.01673 -0.07343 0.01134  289 THR A C   
2225 O O   . THR A 278 ? 0.33743 0.27895 0.37446 -0.02077 -0.08979 0.01360  289 THR A O   
2226 C CB  . THR A 278 ? 0.38969 0.33028 0.37784 -0.00545 -0.07713 0.00104  289 THR A CB  
2227 O OG1 . THR A 278 ? 0.37571 0.32299 0.36053 -0.00376 -0.07223 0.00272  289 THR A OG1 
2228 C CG2 . THR A 278 ? 0.31151 0.24479 0.27102 0.00345  -0.07048 -0.00677 289 THR A CG2 
2229 N N   . ARG A 279 ? 0.34750 0.29784 0.35210 -0.01449 -0.06215 0.00896  290 ARG A N   
2230 C CA  . ARG A 279 ? 0.33421 0.27818 0.34406 -0.01644 -0.06701 0.00886  290 ARG A CA  
2231 C C   . ARG A 279 ? 0.34918 0.28289 0.33120 -0.00818 -0.06396 -0.00167 290 ARG A C   
2232 O O   . ARG A 279 ? 0.35462 0.29152 0.31748 -0.00228 -0.05318 -0.00529 290 ARG A O   
2233 C CB  . ARG A 279 ? 0.33731 0.29799 0.36606 -0.02260 -0.05501 0.02058  290 ARG A CB  
2234 C CG  . ARG A 279 ? 0.31967 0.29266 0.37965 -0.02936 -0.05815 0.03424  290 ARG A CG  
2235 C CD  . ARG A 279 ? 0.35501 0.34609 0.43049 -0.03180 -0.04512 0.04727  290 ARG A CD  
2236 N NE  . ARG A 279 ? 0.39705 0.40219 0.50548 -0.03701 -0.04764 0.06356  290 ARG A NE  
2237 C CZ  . ARG A 279 ? 0.39696 0.41923 0.51290 -0.03547 -0.03857 0.07126  290 ARG A CZ  
2238 N NH1 . ARG A 279 ? 0.28693 0.31307 0.38027 -0.02936 -0.02730 0.06366  290 ARG A NH1 
2239 N NH2 . ARG A 279 ? 0.29097 0.32697 0.43991 -0.03979 -0.04158 0.08774  290 ARG A NH2 
2240 N N   . ILE A 280 ? 0.35543 0.27729 0.33783 -0.00750 -0.07403 -0.00528 291 ILE A N   
2241 C CA  . ILE A 280 ? 0.33814 0.25115 0.29634 0.00110  -0.07163 -0.01430 291 ILE A CA  
2242 C C   . ILE A 280 ? 0.36868 0.28102 0.33843 -0.00366 -0.07197 -0.01119 291 ILE A C   
2243 O O   . ILE A 280 ? 0.31495 0.22458 0.30844 -0.01088 -0.08301 -0.00513 291 ILE A O   
2244 C CB  . ILE A 280 ? 0.33290 0.22629 0.27010 0.01269  -0.08817 -0.02623 291 ILE A CB  
2245 C CG1 . ILE A 280 ? 0.35315 0.24027 0.26344 0.02446  -0.08347 -0.03433 291 ILE A CG1 
2246 C CG2 . ILE A 280 ? 0.35434 0.23225 0.30933 0.00927  -0.11225 -0.02802 291 ILE A CG2 
2247 C CD1 . ILE A 280 ? 0.43268 0.30253 0.31460 0.04135  -0.09712 -0.04636 291 ILE A CD1 
2248 N N   . PHE A 281 ? 0.34217 0.25826 0.29809 0.00007  -0.05961 -0.01363 292 PHE A N   
2249 C CA  . PHE A 281 ? 0.32890 0.24193 0.29008 -0.00194 -0.06051 -0.01283 292 PHE A CA  
2250 C C   . PHE A 281 ? 0.35836 0.25497 0.29674 0.00894  -0.06894 -0.02469 292 PHE A C   
2251 O O   . PHE A 281 ? 0.34695 0.24717 0.26664 0.01632  -0.05766 -0.02861 292 PHE A O   
2252 C CB  . PHE A 281 ? 0.34365 0.27234 0.30642 -0.00444 -0.04217 -0.00752 292 PHE A CB  
2253 C CG  . PHE A 281 ? 0.40332 0.33106 0.37418 -0.00720 -0.04243 -0.00455 292 PHE A CG  
2254 C CD1 . PHE A 281 ? 0.33742 0.26993 0.33265 -0.01491 -0.04616 0.00644  292 PHE A CD1 
2255 C CD2 . PHE A 281 ? 0.30965 0.23308 0.26538 -0.00155 -0.03851 -0.01105 292 PHE A CD2 
2256 C CE1 . PHE A 281 ? 0.33970 0.27160 0.34260 -0.01681 -0.04617 0.01069  292 PHE A CE1 
2257 C CE2 . PHE A 281 ? 0.35392 0.27577 0.31665 -0.00377 -0.03935 -0.00844 292 PHE A CE2 
2258 C CZ  . PHE A 281 ? 0.38225 0.30793 0.36789 -0.01136 -0.04319 0.00239  292 PHE A CZ  
2259 N N   . PRO A 282 ? 0.33670 0.21515 0.27672 0.01150  -0.08961 -0.03040 293 PRO A N   
2260 C CA  . PRO A 282 ? 0.37880 0.24042 0.29042 0.02685  -0.09965 -0.04394 293 PRO A CA  
2261 C C   . PRO A 282 ? 0.44333 0.30284 0.34284 0.03245  -0.09404 -0.04785 293 PRO A C   
2262 O O   . PRO A 282 ? 0.44964 0.30757 0.36562 0.02485  -0.09696 -0.04399 293 PRO A O   
2263 C CB  . PRO A 282 ? 0.48040 0.32123 0.40200 0.02724  -0.12716 -0.04928 293 PRO A CB  
2264 C CG  . PRO A 282 ? 0.51441 0.36146 0.47481 0.01017  -0.12996 -0.03607 293 PRO A CG  
2265 C CD  . PRO A 282 ? 0.45091 0.32342 0.42050 0.00169  -0.10586 -0.02399 293 PRO A CD  
2266 N N   . LEU A 283 ? 0.41854 0.27968 0.29037 0.04637  -0.08510 -0.05392 294 LEU A N   
2267 C CA  . LEU A 283 ? 0.47321 0.33125 0.33064 0.05512  -0.08158 -0.05886 294 LEU A CA  
2268 C C   . LEU A 283 ? 0.54465 0.37878 0.38461 0.06903  -0.10383 -0.07192 294 LEU A C   
2269 O O   . LEU A 283 ? 0.54337 0.36922 0.36009 0.08417  -0.11109 -0.07974 294 LEU A O   
2270 C CB  . LEU A 283 ? 0.50450 0.37750 0.34392 0.06482  -0.06157 -0.05689 294 LEU A CB  
2271 C CG  . LEU A 283 ? 0.49466 0.38913 0.34991 0.05378  -0.04107 -0.04594 294 LEU A CG  
2272 C CD1 . LEU A 283 ? 0.34872 0.25528 0.18918 0.06473  -0.02614 -0.04302 294 LEU A CD1 
2273 C CD2 . LEU A 283 ? 0.41829 0.31651 0.28648 0.04612  -0.03636 -0.04346 294 LEU A CD2 
2274 N N   . GLY A 284 ? 0.61231 0.43463 0.46216 0.06559  -0.11548 -0.07455 295 GLY A N   
2275 C CA  . GLY A 284 ? 0.58394 0.38061 0.41929 0.07895  -0.14000 -0.08812 295 GLY A CA  
2276 C C   . GLY A 284 ? 0.67859 0.46987 0.50553 0.08524  -0.13966 -0.09269 295 GLY A C   
2277 O O   . GLY A 284 ? 0.64174 0.44200 0.44552 0.09807  -0.12482 -0.09503 295 GLY A O   
2278 N N   . LYS A 285 ? 0.65938 0.43694 0.50742 0.07631  -0.15594 -0.09252 296 LYS A N   
2279 C CA  . LYS A 285 ? 0.76133 0.53460 0.60585 0.07953  -0.15518 -0.09517 296 LYS A CA  
2280 C C   . LYS A 285 ? 0.71961 0.51843 0.57224 0.06981  -0.12725 -0.08347 296 LYS A C   
2281 O O   . LYS A 285 ? 0.69629 0.51332 0.56477 0.05712  -0.11254 -0.07226 296 LYS A O   
2282 C CB  . LYS A 285 ? 0.76140 0.51582 0.63290 0.06955  -0.17838 -0.09417 296 LYS A CB  
2283 C CG  . LYS A 285 ? 0.82764 0.55471 0.70085 0.07581  -0.21088 -0.10467 296 LYS A CG  
2284 C CD  . LYS A 285 ? 0.86194 0.57756 0.77560 0.06089  -0.23101 -0.09627 296 LYS A CD  
2285 C CE  . LYS A 285 ? 0.98650 0.69555 0.92471 0.05554  -0.25129 -0.09225 296 LYS A CE  
2286 N NZ  . LYS A 285 ? 0.98059 0.68666 0.96661 0.03835  -0.26638 -0.07775 296 LYS A NZ  
2287 N N   A SER A 286 ? 0.68221 0.48121 0.52364 0.07703  -0.12165 -0.08698 297 SER A N   
2288 N N   B SER A 286 ? 0.68219 0.48130 0.52334 0.07719  -0.12150 -0.08702 297 SER A N   
2289 C CA  A SER A 286 ? 0.67965 0.50014 0.52832 0.06968  -0.09851 -0.07779 297 SER A CA  
2290 C CA  B SER A 286 ? 0.68000 0.50064 0.52834 0.06987  -0.09829 -0.07784 297 SER A CA  
2291 C C   A SER A 286 ? 0.62215 0.45086 0.50241 0.04969  -0.09509 -0.06498 297 SER A C   
2292 C C   B SER A 286 ? 0.62252 0.45111 0.50249 0.04989  -0.09509 -0.06512 297 SER A C   
2293 O O   A SER A 286 ? 0.58487 0.40202 0.48457 0.04136  -0.11096 -0.06178 297 SER A O   
2294 O O   B SER A 286 ? 0.58496 0.40168 0.48420 0.04170  -0.11115 -0.06207 297 SER A O   
2295 C CB  A SER A 286 ? 0.66869 0.48490 0.50471 0.07965  -0.09754 -0.08367 297 SER A CB  
2296 C CB  B SER A 286 ? 0.66928 0.48608 0.50404 0.08041  -0.09681 -0.08386 297 SER A CB  
2297 O OG  A SER A 286 ? 0.60391 0.40291 0.45392 0.07394  -0.11508 -0.08502 297 SER A OG  
2298 O OG  B SER A 286 ? 0.70684 0.52825 0.51339 0.09952  -0.08890 -0.09032 297 SER A OG  
2299 N N   . TRP A 287 ? 0.57718 0.42664 0.46337 0.04334  -0.07455 -0.05679 298 TRP A N   
2300 C CA  . TRP A 287 ? 0.48228 0.34184 0.39265 0.02893  -0.06865 -0.04488 298 TRP A CA  
2301 C C   . TRP A 287 ? 0.48176 0.33433 0.39829 0.02774  -0.07347 -0.04401 298 TRP A C   
2302 O O   . TRP A 287 ? 0.44721 0.28722 0.34939 0.03758  -0.08111 -0.05347 298 TRP A O   
2303 C CB  . TRP A 287 ? 0.43075 0.31154 0.34175 0.02595  -0.04830 -0.03930 298 TRP A CB  
2304 C CG  . TRP A 287 ? 0.44743 0.33518 0.35974 0.02360  -0.04484 -0.03684 298 TRP A CG  
2305 C CD1 . TRP A 287 ? 0.45439 0.33336 0.37098 0.02176  -0.05718 -0.03718 298 TRP A CD1 
2306 C CD2 . TRP A 287 ? 0.35321 0.25730 0.26452 0.02274  -0.02955 -0.03355 298 TRP A CD2 
2307 N NE1 . TRP A 287 ? 0.40446 0.29428 0.32101 0.01998  -0.04899 -0.03420 298 TRP A NE1 
2308 C CE2 . TRP A 287 ? 0.40326 0.30818 0.31680 0.02047  -0.03221 -0.03183 298 TRP A CE2 
2309 C CE3 . TRP A 287 ? 0.32270 0.23973 0.23354 0.02366  -0.01570 -0.03199 298 TRP A CE3 
2310 C CZ2 . TRP A 287 ? 0.35081 0.26898 0.26510 0.01916  -0.02077 -0.02842 298 TRP A CZ2 
2311 C CZ3 . TRP A 287 ? 0.35154 0.28080 0.26532 0.02205  -0.00596 -0.02866 298 TRP A CZ3 
2312 C CH2 . TRP A 287 ? 0.31756 0.24730 0.23249 0.01986  -0.00816 -0.02681 298 TRP A CH2 
2313 N N   . LYS A 288 ? 0.45587 0.31726 0.39273 0.01721  -0.06860 -0.03208 299 LYS A N   
2314 C CA  . LYS A 288 ? 0.44972 0.30547 0.39412 0.01573  -0.07268 -0.02897 299 LYS A CA  
2315 C C   . LYS A 288 ? 0.38990 0.25031 0.31740 0.02358  -0.06217 -0.03574 299 LYS A C   
2316 O O   . LYS A 288 ? 0.41566 0.29160 0.33774 0.02452  -0.04678 -0.03511 299 LYS A O   
2317 C CB  . LYS A 288 ? 0.41382 0.28188 0.38152 0.00542  -0.06660 -0.01249 299 LYS A CB  
2318 C CG  . LYS A 288 ? 0.41261 0.28049 0.40280 -0.00298 -0.07500 -0.00203 299 LYS A CG  
2319 C CD  . LYS A 288 ? 0.36754 0.25087 0.38019 -0.01022 -0.06659 0.01693  299 LYS A CD  
2320 C CE  . LYS A 288 ? 0.40700 0.29142 0.44821 -0.01878 -0.07578 0.03050  299 LYS A CE  
2321 N NZ  . LYS A 288 ? 0.37166 0.27554 0.43533 -0.02353 -0.06490 0.05237  299 LYS A NZ  
2322 N N   . SER A 289 ? 0.45687 0.30329 0.37824 0.02933  -0.07185 -0.04204 300 SER A N   
2323 C CA  . SER A 289 ? 0.59823 0.44913 0.50767 0.03623  -0.06310 -0.04686 300 SER A CA  
2324 C C   . SER A 289 ? 0.49116 0.34606 0.41412 0.02998  -0.06008 -0.03783 300 SER A C   
2325 O O   . SER A 289 ? 0.54427 0.39640 0.48550 0.02183  -0.06636 -0.02738 300 SER A O   
2326 C CB  . SER A 289 ? 0.57675 0.41107 0.46850 0.04899  -0.07448 -0.05956 300 SER A CB  
2327 O OG  . SER A 289 ? 0.54493 0.36036 0.44625 0.04670  -0.09269 -0.05946 300 SER A OG  
2328 N N   A LYS A 290 ? 0.53520 0.39774 0.45025 0.03470  -0.05026 -0.04069 301 LYS A N   
2329 N N   B LYS A 290 ? 0.53629 0.39857 0.45118 0.03481  -0.05045 -0.04084 301 LYS A N   
2330 C CA  A LYS A 290 ? 0.53335 0.39925 0.45627 0.03201  -0.04723 -0.03395 301 LYS A CA  
2331 C CA  B LYS A 290 ? 0.53347 0.39965 0.45603 0.03218  -0.04693 -0.03417 301 LYS A CA  
2332 C C   A LYS A 290 ? 0.52060 0.39931 0.45795 0.02404  -0.04006 -0.02037 301 LYS A C   
2333 C C   B LYS A 290 ? 0.52159 0.40011 0.45892 0.02402  -0.04023 -0.02046 301 LYS A C   
2334 O O   A LYS A 290 ? 0.52784 0.40490 0.47847 0.01973  -0.04376 -0.00936 301 LYS A O   
2335 O O   B LYS A 290 ? 0.52946 0.40583 0.48039 0.01954  -0.04444 -0.00950 301 LYS A O   
2336 C CB  A LYS A 290 ? 0.56684 0.41478 0.49382 0.03283  -0.06204 -0.03430 301 LYS A CB  
2337 C CB  B LYS A 290 ? 0.56745 0.41600 0.49331 0.03341  -0.06121 -0.03486 301 LYS A CB  
2338 C CG  A LYS A 290 ? 0.58220 0.41561 0.49247 0.04360  -0.07128 -0.04859 301 LYS A CG  
2339 C CG  B LYS A 290 ? 0.58324 0.41627 0.49290 0.04395  -0.07156 -0.04907 301 LYS A CG  
2340 C CD  A LYS A 290 ? 0.58945 0.43378 0.48560 0.05210  -0.05881 -0.05545 301 LYS A CD  
2341 C CD  B LYS A 290 ? 0.59449 0.43631 0.48885 0.05352  -0.06066 -0.05698 301 LYS A CD  
2342 C CE  A LYS A 290 ? 0.62026 0.45271 0.49896 0.06554  -0.06640 -0.06790 301 LYS A CE  
2343 C CE  B LYS A 290 ? 0.63732 0.46562 0.51378 0.06716  -0.06989 -0.06977 301 LYS A CE  
2344 N NZ  A LYS A 290 ? 0.59623 0.44241 0.46626 0.07362  -0.05329 -0.07153 301 LYS A NZ  
2345 N NZ  B LYS A 290 ? 0.56206 0.36803 0.44067 0.06878  -0.08879 -0.07286 301 LYS A NZ  
2346 N N   . ARG A 291 ? 0.46658 0.35887 0.40169 0.02333  -0.02961 -0.02013 302 ARG A N   
2347 C CA  . ARG A 291 ? 0.44252 0.34806 0.38749 0.01911  -0.02213 -0.00858 302 ARG A CA  
2348 C C   . ARG A 291 ? 0.39615 0.30898 0.33913 0.02317  -0.01562 -0.00480 302 ARG A C   
2349 O O   . ARG A 291 ? 0.34211 0.25294 0.27587 0.02841  -0.01452 -0.01331 302 ARG A O   
2350 C CB  . ARG A 291 ? 0.33631 0.25237 0.27781 0.01884  -0.01440 -0.01135 302 ARG A CB  
2351 C CG  . ARG A 291 ? 0.35257 0.26199 0.29469 0.01597  -0.02070 -0.01432 302 ARG A CG  
2352 C CD  . ARG A 291 ? 0.33955 0.25730 0.27549 0.01727  -0.01347 -0.01916 302 ARG A CD  
2353 N NE  . ARG A 291 ? 0.36410 0.27281 0.29424 0.01853  -0.02031 -0.02492 302 ARG A NE  
2354 C CZ  . ARG A 291 ? 0.33742 0.25013 0.25922 0.02215  -0.01562 -0.03003 302 ARG A CZ  
2355 N NH1 . ARG A 291 ? 0.28512 0.21051 0.20788 0.02259  -0.00508 -0.02938 302 ARG A NH1 
2356 N NH2 . ARG A 291 ? 0.31527 0.21846 0.22777 0.02665  -0.02272 -0.03569 302 ARG A NH2 
2357 N N   . PRO A 292 ? 0.33511 0.25748 0.28630 0.02238  -0.01108 0.00848  303 PRO A N   
2358 C CA  . PRO A 292 ? 0.40325 0.33108 0.34980 0.02887  -0.00627 0.01249  303 PRO A CA  
2359 C C   . PRO A 292 ? 0.43033 0.36466 0.36362 0.03618  -0.00030 0.00190  303 PRO A C   
2360 O O   . PRO A 292 ? 0.43724 0.37015 0.36380 0.04217  -0.00039 -0.00169 303 PRO A O   
2361 C CB  . PRO A 292 ? 0.37299 0.31265 0.33051 0.02874  -0.00115 0.03105  303 PRO A CB  
2362 C CG  . PRO A 292 ? 0.42071 0.36434 0.38723 0.02264  -0.00104 0.03441  303 PRO A CG  
2363 C CD  . PRO A 292 ? 0.38339 0.31277 0.34859 0.01715  -0.01013 0.02166  303 PRO A CD  
2364 N N   . LEU A 293 ? 0.39064 0.33119 0.32202 0.03584  0.00334  -0.00299 304 LEU A N   
2365 C CA  . LEU A 293 ? 0.37723 0.32201 0.30156 0.04134  0.00586  -0.01323 304 LEU A CA  
2366 C C   . LEU A 293 ? 0.34757 0.29268 0.27474 0.03671  0.00626  -0.01924 304 LEU A C   
2367 O O   . LEU A 293 ? 0.28499 0.22881 0.21647 0.03098  0.00556  -0.01507 304 LEU A O   
2368 C CB  . LEU A 293 ? 0.33929 0.29405 0.25849 0.04944  0.01008  -0.00960 304 LEU A CB  
2369 C CG  . LEU A 293 ? 0.31789 0.27483 0.23007 0.05851  0.01102  -0.00399 304 LEU A CG  
2370 C CD1 . LEU A 293 ? 0.36663 0.33393 0.26996 0.06975  0.01498  -0.00146 304 LEU A CD1 
2371 C CD2 . LEU A 293 ? 0.36263 0.31236 0.27004 0.06222  0.00640  -0.01417 304 LEU A CD2 
2372 N N   . PRO A 294 ? 0.35433 0.30136 0.28117 0.03928  0.00676  -0.02792 305 PRO A N   
2373 C CA  . PRO A 294 ? 0.34123 0.28978 0.27222 0.03558  0.00813  -0.03131 305 PRO A CA  
2374 C C   . PRO A 294 ? 0.33687 0.29100 0.27021 0.03289  0.01056  -0.02724 305 PRO A C   
2375 O O   . PRO A 294 ? 0.27586 0.23550 0.20854 0.03679  0.01158  -0.02653 305 PRO A O   
2376 C CB  . PRO A 294 ? 0.34950 0.30140 0.28544 0.03928  0.00795  -0.03794 305 PRO A CB  
2377 C CG  . PRO A 294 ? 0.34790 0.29634 0.28022 0.04434  0.00498  -0.04034 305 PRO A CG  
2378 C CD  . PRO A 294 ? 0.36340 0.31108 0.28866 0.04581  0.00509  -0.03404 305 PRO A CD  
2379 N N   . ILE A 295 ? 0.27194 0.22405 0.20663 0.02784  0.01060  -0.02543 306 ILE A N   
2380 C CA  . ILE A 295 ? 0.30565 0.26276 0.24331 0.02486  0.01257  -0.02149 306 ILE A CA  
2381 C C   . ILE A 295 ? 0.25550 0.20912 0.19307 0.02129  0.01171  -0.02295 306 ILE A C   
2382 O O   . ILE A 295 ? 0.28192 0.22760 0.21543 0.02139  0.00802  -0.02485 306 ILE A O   
2383 C CB  . ILE A 295 ? 0.31748 0.27705 0.25707 0.02371  0.01265  -0.01198 306 ILE A CB  
2384 C CG1 . ILE A 295 ? 0.27409 0.24038 0.21784 0.02133  0.01503  -0.00728 306 ILE A CG1 
2385 C CG2 . ILE A 295 ? 0.24769 0.19857 0.18983 0.01984  0.00746  -0.00811 306 ILE A CG2 
2386 C CD1 . ILE A 295 ? 0.25151 0.22564 0.19943 0.02286  0.01763  0.00436  306 ILE A CD1 
2387 N N   . THR A 296 ? 0.24026 0.19910 0.18081 0.01975  0.01429  -0.02249 307 THR A N   
2388 C CA  . THR A 296 ? 0.23301 0.18952 0.17170 0.01794  0.01387  -0.02295 307 THR A CA  
2389 C C   . THR A 296 ? 0.28068 0.24295 0.22374 0.01508  0.01575  -0.01966 307 THR A C   
2390 O O   . THR A 296 ? 0.27248 0.24035 0.21914 0.01539  0.01722  -0.01729 307 THR A O   
2391 C CB  . THR A 296 ? 0.29793 0.25576 0.23523 0.02191  0.01683  -0.02660 307 THR A CB  
2392 O OG1 . THR A 296 ? 0.30948 0.26477 0.24049 0.02336  0.01657  -0.02656 307 THR A OG1 
2393 C CG2 . THR A 296 ? 0.22529 0.19169 0.17290 0.02218  0.02065  -0.02622 307 THR A CG2 
2394 N N   . MET A 297 ? 0.22935 0.19005 0.17020 0.01407  0.01538  -0.01970 308 MET A N   
2395 C CA  . MET A 297 ? 0.29158 0.25676 0.23616 0.01137  0.01651  -0.01670 308 MET A CA  
2396 C C   . MET A 297 ? 0.24335 0.21056 0.18669 0.01324  0.01959  -0.01764 308 MET A C   
2397 O O   . MET A 297 ? 0.26898 0.23294 0.20538 0.01726  0.01988  -0.01941 308 MET A O   
2398 C CB  . MET A 297 ? 0.24130 0.20219 0.18638 0.00775  0.01116  -0.01317 308 MET A CB  
2399 C CG  . MET A 297 ? 0.28551 0.24280 0.23396 0.00620  0.00711  -0.00990 308 MET A CG  
2400 S SD  . MET A 297 ? 0.33984 0.29679 0.30015 0.00039  0.00091  -0.00092 308 MET A SD  
2401 C CE  . MET A 297 ? 0.25255 0.19480 0.20622 0.00063  -0.01005 -0.00743 308 MET A CE  
2402 N N   . ILE A 298 ? 0.26294 0.23606 0.21271 0.01168  0.02200  -0.01554 309 ILE A N   
2403 C CA  . ILE A 298 ? 0.25456 0.23123 0.20661 0.01311  0.02552  -0.01362 309 ILE A CA  
2404 C C   . ILE A 298 ? 0.28205 0.26036 0.23560 0.01038  0.02475  -0.01119 309 ILE A C   
2405 O O   . ILE A 298 ? 0.25109 0.23040 0.20711 0.00785  0.02262  -0.01077 309 ILE A O   
2406 C CB  . ILE A 298 ? 0.21289 0.19545 0.17785 0.01408  0.02833  -0.01275 309 ILE A CB  
2407 C CG1 . ILE A 298 ? 0.25989 0.24352 0.23191 0.01270  0.02497  -0.01502 309 ILE A CG1 
2408 C CG2 . ILE A 298 ? 0.21520 0.19736 0.18028 0.01715  0.02933  -0.01440 309 ILE A CG2 
2409 C CD1 . ILE A 298 ? 0.23549 0.22182 0.22311 0.01388  0.02310  -0.01575 309 ILE A CD1 
2410 N N   . GLY A 299 ? 0.26934 0.24936 0.22153 0.01215  0.02729  -0.00841 310 GLY A N   
2411 C CA  . GLY A 299 ? 0.21750 0.19920 0.17186 0.00983  0.02651  -0.00608 310 GLY A CA  
2412 C C   . GLY A 299 ? 0.27444 0.25068 0.22110 0.00823  0.02104  -0.00717 310 GLY A C   
2413 O O   . GLY A 299 ? 0.27176 0.24102 0.20958 0.01021  0.01692  -0.00969 310 GLY A O   
2414 N N   . ASP A 300 ? 0.26584 0.24491 0.21782 0.00500  0.01961  -0.00515 311 ASP A N   
2415 C CA  . ASP A 300 ? 0.28065 0.25603 0.23118 0.00262  0.01347  -0.00430 311 ASP A CA  
2416 C C   . ASP A 300 ? 0.27906 0.25175 0.23267 0.00036  0.00947  -0.00388 311 ASP A C   
2417 O O   . ASP A 300 ? 0.28149 0.24769 0.23542 -0.00126 0.00171  -0.00349 311 ASP A O   
2418 C CB  . ASP A 300 ? 0.22767 0.20922 0.18600 0.00009  0.01378  -0.00084 311 ASP A CB  
2419 C CG  . ASP A 300 ? 0.31521 0.29660 0.27024 0.00165  0.01452  -0.00027 311 ASP A CG  
2420 O OD1 . ASP A 300 ? 0.30013 0.27876 0.24723 0.00566  0.01659  -0.00103 311 ASP A OD1 
2421 O OD2 . ASP A 300 ? 0.28803 0.27333 0.24858 -0.00010 0.01369  0.00211  311 ASP A OD2 
2422 N N   . ALA A 301 ? 0.25234 0.22933 0.20957 0.00066  0.01334  -0.00351 312 ALA A N   
2423 C CA  . ALA A 301 ? 0.27373 0.24868 0.23406 -0.00078 0.01038  -0.00141 312 ALA A CA  
2424 C C   . ALA A 301 ? 0.27806 0.24162 0.23103 0.00025  0.00431  -0.00562 312 ALA A C   
2425 O O   . ALA A 301 ? 0.29480 0.25282 0.25262 -0.00219 -0.00272 -0.00341 312 ALA A O   
2426 C CB  . ALA A 301 ? 0.24713 0.22755 0.20842 0.00192  0.01547  -0.00151 312 ALA A CB  
2427 N N   . ALA A 302 ? 0.23514 0.19546 0.17758 0.00489  0.00644  -0.01073 313 ALA A N   
2428 C CA  . ALA A 302 ? 0.27179 0.22203 0.20289 0.00983  0.00153  -0.01580 313 ALA A CA  
2429 C C   . ALA A 302 ? 0.30998 0.25151 0.23183 0.01346  -0.00653 -0.01866 313 ALA A C   
2430 O O   . ALA A 302 ? 0.32271 0.25207 0.23772 0.01685  -0.01683 -0.02325 313 ALA A O   
2431 C CB  . ALA A 302 ? 0.24678 0.20103 0.17178 0.01557  0.00941  -0.01780 313 ALA A CB  
2432 N N   . HIS A 303 ? 0.26371 0.20977 0.18446 0.01398  -0.00369 -0.01680 314 HIS A N   
2433 C CA  . HIS A 303 ? 0.31083 0.24837 0.21868 0.02045  -0.01115 -0.02044 314 HIS A CA  
2434 C C   . HIS A 303 ? 0.35975 0.30211 0.27210 0.01766  -0.01039 -0.01689 314 HIS A C   
2435 O O   . HIS A 303 ? 0.36979 0.31199 0.27010 0.02487  -0.00865 -0.01752 314 HIS A O   
2436 C CB  . HIS A 303 ? 0.28720 0.22471 0.17734 0.03233  -0.00564 -0.02306 314 HIS A CB  
2437 C CG  . HIS A 303 ? 0.32819 0.27987 0.22529 0.03158  0.00872  -0.01694 314 HIS A CG  
2438 N ND1 . HIS A 303 ? 0.28358 0.24372 0.18833 0.02849  0.01453  -0.01141 314 HIS A ND1 
2439 C CD2 . HIS A 303 ? 0.28650 0.24459 0.18748 0.03296  0.01658  -0.01522 314 HIS A CD2 
2440 C CE1 . HIS A 303 ? 0.30036 0.27060 0.21481 0.02779  0.02422  -0.00649 314 HIS A CE1 
2441 N NE2 . HIS A 303 ? 0.27943 0.24907 0.19237 0.03037  0.02568  -0.00853 314 HIS A NE2 
2442 N N   . LEU A 304 ? 0.26803 0.21599 0.19713 0.00866  -0.01078 -0.01217 315 LEU A N   
2443 C CA  . LEU A 304 ? 0.31332 0.26446 0.24805 0.00594  -0.01273 -0.00916 315 LEU A CA  
2444 C C   . LEU A 304 ? 0.34036 0.27983 0.26308 0.01193  -0.02407 -0.01400 315 LEU A C   
2445 O O   . LEU A 304 ? 0.35453 0.28159 0.27411 0.01406  -0.03659 -0.01874 315 LEU A O   
2446 C CB  . LEU A 304 ? 0.26002 0.21651 0.21436 -0.00241 -0.01555 -0.00311 315 LEU A CB  
2447 C CG  . LEU A 304 ? 0.33348 0.29359 0.29673 -0.00536 -0.01922 0.00074  315 LEU A CG  
2448 C CD1 . LEU A 304 ? 0.28766 0.25897 0.25096 -0.00484 -0.00804 0.00311  315 LEU A CD1 
2449 C CD2 . LEU A 304 ? 0.24530 0.20959 0.23011 -0.01212 -0.02485 0.00854  315 LEU A CD2 
2450 N N   . MET A 305 ? 0.31616 0.25839 0.23217 0.01554  -0.02130 -0.01316 316 MET A N   
2451 C CA  . MET A 305 ? 0.32137 0.25244 0.22228 0.02398  -0.03222 -0.01835 316 MET A CA  
2452 C C   . MET A 305 ? 0.33864 0.27540 0.24275 0.02261  -0.03030 -0.01454 316 MET A C   
2453 O O   . MET A 305 ? 0.31681 0.26580 0.23134 0.01718  -0.01905 -0.00849 316 MET A O   
2454 C CB  . MET A 305 ? 0.32978 0.25659 0.20602 0.03821  -0.02884 -0.02258 316 MET A CB  
2455 C CG  . MET A 305 ? 0.34566 0.28599 0.21828 0.04191  -0.01173 -0.01564 316 MET A CG  
2456 S SD  . MET A 305 ? 0.43443 0.37436 0.28216 0.05991  -0.00532 -0.01673 316 MET A SD  
2457 C CE  . MET A 305 ? 0.37774 0.32320 0.23885 0.05285  0.00199  -0.01569 316 MET A CE  
2458 N N   . PRO A 306 ? 0.40251 0.32946 0.29766 0.02828  -0.04262 -0.01872 317 PRO A N   
2459 C CA  . PRO A 306 ? 0.33091 0.26296 0.22908 0.02721  -0.04141 -0.01511 317 PRO A CA  
2460 C C   . PRO A 306 ? 0.39850 0.34025 0.28684 0.03258  -0.02598 -0.01015 317 PRO A C   
2461 O O   . PRO A 306 ? 0.36529 0.30694 0.23782 0.04209  -0.01958 -0.01047 317 PRO A O   
2462 C CB  . PRO A 306 ? 0.37090 0.28756 0.25560 0.03610  -0.05930 -0.02261 317 PRO A CB  
2463 C CG  . PRO A 306 ? 0.42921 0.33262 0.31588 0.03624  -0.07367 -0.02922 317 PRO A CG  
2464 C CD  . PRO A 306 ? 0.39613 0.30515 0.27872 0.03651  -0.06081 -0.02794 317 PRO A CD  
2465 N N   . PRO A 307 ? 0.41014 0.36104 0.30948 0.02724  -0.01989 -0.00429 318 PRO A N   
2466 C CA  . PRO A 307 ? 0.45222 0.41268 0.34974 0.03010  -0.00612 0.00250  318 PRO A CA  
2467 C C   . PRO A 307 ? 0.48663 0.44637 0.36925 0.04012  -0.00517 0.00545  318 PRO A C   
2468 O O   . PRO A 307 ? 0.46886 0.43745 0.35463 0.04169  0.00612  0.01371  318 PRO A O   
2469 C CB  . PRO A 307 ? 0.38607 0.35552 0.30545 0.01904  -0.00197 0.00648  318 PRO A CB  
2470 C CG  . PRO A 307 ? 0.38030 0.34647 0.30652 0.01479  -0.01274 0.00417  318 PRO A CG  
2471 C CD  . PRO A 307 ? 0.37200 0.32705 0.29129 0.01714  -0.02423 -0.00201 318 PRO A CD  
2472 N N   . PHE A 308 ? 0.44938 0.39862 0.31697 0.04766  -0.01738 -0.00037 319 PHE A N   
2473 C CA  . PHE A 308 ? 0.52281 0.47177 0.37816 0.05628  -0.01774 0.00260  319 PHE A CA  
2474 C C   . PHE A 308 ? 0.59422 0.54755 0.42924 0.07159  -0.00697 0.00894  319 PHE A C   
2475 O O   . PHE A 308 ? 0.57719 0.53547 0.40768 0.07705  -0.00169 0.01633  319 PHE A O   
2476 C CB  . PHE A 308 ? 0.44467 0.37970 0.28931 0.06158  -0.03641 -0.00651 319 PHE A CB  
2477 C CG  . PHE A 308 ? 0.39692 0.32965 0.26512 0.04758  -0.04720 -0.00967 319 PHE A CG  
2478 C CD1 . PHE A 308 ? 0.44924 0.39119 0.33770 0.03713  -0.04378 -0.00408 319 PHE A CD1 
2479 C CD2 . PHE A 308 ? 0.41286 0.33530 0.28478 0.04555  -0.06047 -0.01680 319 PHE A CD2 
2480 C CE1 . PHE A 308 ? 0.44936 0.39289 0.36118 0.02582  -0.05160 -0.00411 319 PHE A CE1 
2481 C CE2 . PHE A 308 ? 0.41591 0.33915 0.31422 0.03267  -0.06919 -0.01590 319 PHE A CE2 
2482 C CZ  . PHE A 308 ? 0.45431 0.38951 0.37246 0.02326  -0.06368 -0.00877 319 PHE A CZ  
2483 N N   . ALA A 309 ? 0.48596 0.43883 0.30934 0.07959  -0.00305 0.00773  320 ALA A N   
2484 C CA  . ALA A 309 ? 0.60166 0.56235 0.40751 0.09587  0.00928  0.01661  320 ALA A CA  
2485 C C   . ALA A 309 ? 0.62429 0.60011 0.45008 0.08936  0.02587  0.02842  320 ALA A C   
2486 O O   . ALA A 309 ? 0.57806 0.56270 0.39434 0.10205  0.03709  0.03735  320 ALA A O   
2487 C CB  . ALA A 309 ? 0.62006 0.57037 0.39505 0.11463  0.00179  0.00768  320 ALA A CB  
2488 N N   . GLY A 310 ? 0.55822 0.53761 0.41186 0.07130  0.02700  0.02908  321 GLY A N   
2489 C CA  . GLY A 310 ? 0.56956 0.56111 0.44519 0.06469  0.03914  0.03917  321 GLY A CA  
2490 C C   . GLY A 310 ? 0.58290 0.57460 0.46216 0.06241  0.04070  0.03513  321 GLY A C   
2491 O O   . GLY A 310 ? 0.48202 0.48368 0.37942 0.05871  0.04988  0.04364  321 GLY A O   
2492 N N   . GLN A 311 ? 0.53181 0.51233 0.39628 0.06469  0.03090  0.02291  322 GLN A N   
2493 C CA  . GLN A 311 ? 0.47910 0.45866 0.34950 0.06029  0.03105  0.01838  322 GLN A CA  
2494 C C   . GLN A 311 ? 0.44427 0.42389 0.33776 0.04360  0.02791  0.01544  322 GLN A C   
2495 O O   . GLN A 311 ? 0.39003 0.36629 0.28903 0.03687  0.02137  0.01263  322 GLN A O   
2496 C CB  . GLN A 311 ? 0.48018 0.44651 0.32873 0.06870  0.02010  0.00679  322 GLN A CB  
2497 C CG  . GLN A 311 ? 0.53633 0.50232 0.35709 0.08981  0.02312  0.00792  322 GLN A CG  
2498 C CD  . GLN A 311 ? 0.64713 0.61088 0.44949 0.10177  0.02056  0.00969  322 GLN A CD  
2499 O OE1 . GLN A 311 ? 0.60232 0.55567 0.40323 0.09743  0.00791  0.00247  322 GLN A OE1 
2500 N NE2 . GLN A 311 ? 0.77166 0.74640 0.56089 0.11779  0.03292  0.02066  322 GLN A NE2 
2501 N N   . GLY A 312 ? 0.37631 0.36055 0.28271 0.03855  0.03270  0.01650  323 GLY A N   
2502 C CA  . GLY A 312 ? 0.38155 0.36594 0.30566 0.02639  0.02975  0.01328  323 GLY A CA  
2503 C C   . GLY A 312 ? 0.35016 0.34072 0.28996 0.02262  0.03533  0.01592  323 GLY A C   
2504 O O   . GLY A 312 ? 0.30673 0.29519 0.24373 0.02318  0.03488  0.01196  323 GLY A O   
2505 N N   . VAL A 313 ? 0.28019 0.27711 0.23779 0.01893  0.03881  0.02217  324 VAL A N   
2506 C CA  . VAL A 313 ? 0.29139 0.29170 0.26691 0.01474  0.03990  0.02275  324 VAL A CA  
2507 C C   . VAL A 313 ? 0.28381 0.29052 0.26356 0.01981  0.04703  0.02978  324 VAL A C   
2508 O O   . VAL A 313 ? 0.25975 0.26737 0.24859 0.01791  0.04674  0.02776  324 VAL A O   
2509 C CB  . VAL A 313 ? 0.33293 0.33526 0.32804 0.00994  0.03751  0.02573  324 VAL A CB  
2510 C CG1 . VAL A 313 ? 0.29114 0.30058 0.30025 0.01212  0.04310  0.03870  324 VAL A CG1 
2511 C CG2 . VAL A 313 ? 0.22923 0.23005 0.23766 0.00641  0.03289  0.02036  324 VAL A CG2 
2512 N N   . ASN A 314 ? 0.30698 0.31918 0.27950 0.02780  0.05381  0.03868  325 ASN A N   
2513 C CA  . ASN A 314 ? 0.32240 0.34501 0.30346 0.03389  0.06272  0.04937  325 ASN A CA  
2514 C C   . ASN A 314 ? 0.27404 0.29416 0.24047 0.03917  0.06322  0.04280  325 ASN A C   
2515 O O   . ASN A 314 ? 0.27163 0.29874 0.25171 0.03982  0.06753  0.04762  325 ASN A O   
2516 C CB  . ASN A 314 ? 0.29846 0.32989 0.27370 0.04393  0.07143  0.06270  325 ASN A CB  
2517 C CG  . ASN A 314 ? 0.33621 0.37423 0.33779 0.03829  0.07316  0.07477  325 ASN A CG  
2518 O OD1 . ASN A 314 ? 0.29969 0.34688 0.32992 0.03524  0.07673  0.08600  325 ASN A OD1 
2519 N ND2 . ASN A 314 ? 0.30055 0.33327 0.29562 0.03635  0.06907  0.07261  325 ASN A ND2 
2520 N N   A SER A 315 ? 0.31077 0.32036 0.25190 0.04278  0.05742  0.03192  326 SER A N   
2521 N N   B SER A 315 ? 0.31213 0.32182 0.25291 0.04305  0.05755  0.03210  326 SER A N   
2522 C CA  A SER A 315 ? 0.31227 0.31692 0.24105 0.04691  0.05536  0.02441  326 SER A CA  
2523 C CA  B SER A 315 ? 0.31322 0.31728 0.24142 0.04670  0.05490  0.02394  326 SER A CA  
2524 C C   A SER A 315 ? 0.31800 0.31924 0.26109 0.03629  0.05058  0.01798  326 SER A C   
2525 C C   B SER A 315 ? 0.31600 0.31797 0.26036 0.03622  0.05105  0.01868  326 SER A C   
2526 O O   A SER A 315 ? 0.28005 0.28163 0.22295 0.03845  0.05161  0.01581  326 SER A O   
2527 O O   B SER A 315 ? 0.28089 0.28485 0.22774 0.03832  0.05309  0.01797  326 SER A O   
2528 C CB  A SER A 315 ? 0.32150 0.31347 0.22325 0.05327  0.04705  0.01443  326 SER A CB  
2529 C CB  B SER A 315 ? 0.32512 0.31564 0.22864 0.05071  0.04540  0.01311  326 SER A CB  
2530 O OG  A SER A 315 ? 0.34374 0.32712 0.24826 0.04334  0.03775  0.00760  326 SER A OG  
2531 O OG  B SER A 315 ? 0.36491 0.35540 0.24781 0.06460  0.04726  0.01567  326 SER A OG  
2532 N N   . GLY A 316 ? 0.26169 0.26005 0.21563 0.02664  0.04547  0.01497  327 GLY A N   
2533 C CA  . GLY A 316 ? 0.22502 0.22153 0.19063 0.01984  0.04160  0.00986  327 GLY A CA  
2534 C C   . GLY A 316 ? 0.24710 0.25119 0.23456 0.01869  0.04485  0.01561  327 GLY A C   
2535 O O   . GLY A 316 ? 0.25448 0.25794 0.24692 0.01799  0.04335  0.01211  327 GLY A O   
2536 N N   . LEU A 317 ? 0.22240 0.23359 0.22548 0.01848  0.04835  0.02531  328 LEU A N   
2537 C CA  . LEU A 317 ? 0.28310 0.30185 0.31326 0.01698  0.04980  0.03312  328 LEU A CA  
2538 C C   . LEU A 317 ? 0.27102 0.29786 0.30101 0.02364  0.05762  0.03951  328 LEU A C   
2539 O O   . LEU A 317 ? 0.23945 0.27053 0.28944 0.02203  0.05678  0.04212  328 LEU A O   
2540 C CB  . LEU A 317 ? 0.24505 0.26982 0.29555 0.01508  0.05125  0.04460  328 LEU A CB  
2541 C CG  . LEU A 317 ? 0.33784 0.35444 0.38997 0.00955  0.04249  0.03764  328 LEU A CG  
2542 C CD1 . LEU A 317 ? 0.22596 0.24730 0.29776 0.00798  0.04325  0.04931  328 LEU A CD1 
2543 C CD2 . LEU A 317 ? 0.20412 0.21351 0.26549 0.00587  0.03201  0.02705  328 LEU A CD2 
2544 N N   . MET A 318 ? 0.28016 0.30884 0.28732 0.03257  0.06417  0.04152  329 MET A N   
2545 C CA  . MET A 318 ? 0.26452 0.30002 0.26545 0.04192  0.07122  0.04549  329 MET A CA  
2546 C C   . MET A 318 ? 0.25961 0.28656 0.25311 0.03980  0.06523  0.03312  329 MET A C   
2547 O O   . MET A 318 ? 0.23605 0.26928 0.23903 0.04274  0.06850  0.03628  329 MET A O   
2548 C CB  . MET A 318 ? 0.26639 0.30222 0.23831 0.05495  0.07653  0.04688  329 MET A CB  
2549 C CG  . MET A 318 ? 0.44255 0.48530 0.40403 0.06791  0.08362  0.05018  329 MET A CG  
2550 S SD  . MET A 318 ? 0.60662 0.67448 0.59710 0.07454  0.09895  0.07490  329 MET A SD  
2551 C CE  . MET A 318 ? 0.70769 0.78050 0.66576 0.09408  0.10761  0.08177  329 MET A CE  
2552 N N   . ASP A 319 ? 0.28145 0.29512 0.25934 0.03515  0.05679  0.02047  330 ASP A N   
2553 C CA  . ASP A 319 ? 0.23086 0.23676 0.20400 0.03253  0.05101  0.01052  330 ASP A CA  
2554 C C   . ASP A 319 ? 0.26459 0.27444 0.26188 0.02726  0.04908  0.01155  330 ASP A C   
2555 O O   . ASP A 319 ? 0.30280 0.31365 0.30289 0.02938  0.04923  0.00981  330 ASP A O   
2556 C CB  . ASP A 319 ? 0.22869 0.22318 0.18986 0.02703  0.04296  0.00129  330 ASP A CB  
2557 C CG  . ASP A 319 ? 0.29423 0.28219 0.23438 0.03149  0.04091  -0.00110 330 ASP A CG  
2558 O OD1 . ASP A 319 ? 0.26340 0.25253 0.19040 0.04146  0.04439  0.00091  330 ASP A OD1 
2559 O OD2 . ASP A 319 ? 0.28392 0.26553 0.22074 0.02624  0.03492  -0.00502 330 ASP A OD2 
2560 N N   . ALA A 320 ? 0.23045 0.24109 0.24499 0.02116  0.04537  0.01324  331 ALA A N   
2561 C CA  . ALA A 320 ? 0.26260 0.27337 0.29924 0.01733  0.03919  0.01156  331 ALA A CA  
2562 C C   . ALA A 320 ? 0.23901 0.26065 0.29890 0.01945  0.04359  0.02191  331 ALA A C   
2563 O O   . ALA A 320 ? 0.20871 0.23011 0.28091 0.01896  0.03920  0.01914  331 ALA A O   
2564 C CB  . ALA A 320 ? 0.22914 0.23714 0.27882 0.01268  0.03250  0.01092  331 ALA A CB  
2565 N N   . LEU A 321 ? 0.21727 0.24975 0.28427 0.02273  0.05258  0.03521  332 LEU A N   
2566 C CA  . LEU A 321 ? 0.22260 0.26949 0.31538 0.02573  0.05896  0.04938  332 LEU A CA  
2567 C C   . LEU A 321 ? 0.24325 0.29305 0.32301 0.03289  0.06395  0.04708  332 LEU A C   
2568 O O   . LEU A 321 ? 0.22892 0.28405 0.32981 0.03233  0.06240  0.04995  332 LEU A O   
2569 C CB  . LEU A 321 ? 0.26636 0.32600 0.36548 0.03016  0.06960  0.06614  332 LEU A CB  
2570 C CG  . LEU A 321 ? 0.33472 0.41444 0.46233 0.03529  0.07995  0.08684  332 LEU A CG  
2571 C CD1 . LEU A 321 ? 0.26567 0.34844 0.43871 0.02622  0.07107  0.09295  332 LEU A CD1 
2572 C CD2 . LEU A 321 ? 0.32825 0.41922 0.45487 0.04119  0.09080  0.10279  332 LEU A CD2 
2573 N N   . ILE A 322 ? 0.26029 0.30526 0.30590 0.04006  0.06812  0.04106  333 ILE A N   
2574 C CA  . ILE A 322 ? 0.26272 0.30894 0.29339 0.04873  0.07190  0.03817  333 ILE A CA  
2575 C C   . ILE A 322 ? 0.23793 0.27359 0.26859 0.04321  0.06249  0.02551  333 ILE A C   
2576 O O   . ILE A 322 ? 0.23527 0.27620 0.27662 0.04588  0.06355  0.02712  333 ILE A O   
2577 C CB  . ILE A 322 ? 0.25859 0.29828 0.25252 0.05856  0.07446  0.03270  333 ILE A CB  
2578 C CG1 . ILE A 322 ? 0.28602 0.33882 0.27741 0.06879  0.08550  0.04686  333 ILE A CG1 
2579 C CG2 . ILE A 322 ? 0.25631 0.29142 0.23233 0.06665  0.07369  0.02511  333 ILE A CG2 
2580 C CD1 . ILE A 322 ? 0.27649 0.32110 0.22968 0.08112  0.08550  0.04032  333 ILE A CD1 
2581 N N   . LEU A 323 ? 0.22960 0.25156 0.24893 0.03640  0.05367  0.01400  334 LEU A N   
2582 C CA  . LEU A 323 ? 0.24594 0.25831 0.26110 0.03329  0.04571  0.00305  334 LEU A CA  
2583 C C   . LEU A 323 ? 0.24128 0.25748 0.28457 0.02962  0.04061  0.00444  334 LEU A C   
2584 O O   . LEU A 323 ? 0.23898 0.25412 0.28506 0.03138  0.03794  0.00063  334 LEU A O   
2585 C CB  . LEU A 323 ? 0.21976 0.22034 0.21945 0.02837  0.03913  -0.00582 334 LEU A CB  
2586 C CG  . LEU A 323 ? 0.24442 0.23646 0.23813 0.02663  0.03208  -0.01493 334 LEU A CG  
2587 C CD1 . LEU A 323 ? 0.22217 0.21080 0.20313 0.03133  0.03303  -0.01806 334 LEU A CD1 
2588 C CD2 . LEU A 323 ? 0.23495 0.21984 0.21643 0.02312  0.02814  -0.01917 334 LEU A CD2 
2589 N N   . SER A 324 ? 0.23340 0.25289 0.29891 0.02495  0.03745  0.00950  335 SER A N   
2590 C CA  . SER A 324 ? 0.23750 0.25810 0.33261 0.02200  0.02867  0.00984  335 SER A CA  
2591 C C   . SER A 324 ? 0.24776 0.28136 0.36536 0.02500  0.03405  0.02058  335 SER A C   
2592 O O   . SER A 324 ? 0.25882 0.29117 0.39045 0.02492  0.02703  0.01696  335 SER A O   
2593 C CB  . SER A 324 ? 0.20248 0.22260 0.31941 0.01705  0.02212  0.01351  335 SER A CB  
2594 O OG  . SER A 324 ? 0.23671 0.26954 0.37076 0.01671  0.03110  0.02951  335 SER A OG  
2595 N N   . ASP A 325 ? 0.25414 0.30132 0.37504 0.02917  0.04673  0.03453  336 ASP A N   
2596 C CA  . ASP A 325 ? 0.24489 0.30794 0.38702 0.03422  0.05421  0.04728  336 ASP A CA  
2597 C C   . ASP A 325 ? 0.23263 0.29203 0.35434 0.04017  0.05522  0.03832  336 ASP A C   
2598 O O   . ASP A 325 ? 0.27557 0.34121 0.41856 0.04102  0.05319  0.04133  336 ASP A O   
2599 C CB  . ASP A 325 ? 0.21913 0.29917 0.36292 0.04144  0.06965  0.06500  336 ASP A CB  
2600 C CG  . ASP A 325 ? 0.37921 0.47950 0.54740 0.04856  0.07923  0.08123  336 ASP A CG  
2601 O OD1 . ASP A 325 ? 0.44911 0.55736 0.66053 0.04247  0.07392  0.09085  336 ASP A OD1 
2602 O OD2 . ASP A 325 ? 0.37998 0.48763 0.52541 0.06092  0.09049  0.08384  336 ASP A OD2 
2603 N N   . ASN A 326 ? 0.23424 0.28304 0.31709 0.04421  0.05704  0.02762  337 ASN A N   
2604 C CA  . ASN A 326 ? 0.26317 0.30642 0.32689 0.04975  0.05640  0.01889  337 ASN A CA  
2605 C C   . ASN A 326 ? 0.25944 0.29296 0.33120 0.04403  0.04451  0.00844  337 ASN A C   
2606 O O   . ASN A 326 ? 0.23512 0.26984 0.30894 0.04777  0.04366  0.00623  337 ASN A O   
2607 C CB  . ASN A 326 ? 0.29566 0.32646 0.32066 0.05373  0.05674  0.00926  337 ASN A CB  
2608 C CG  . ASN A 326 ? 0.32469 0.36343 0.33416 0.06505  0.06721  0.01673  337 ASN A CG  
2609 O OD1 . ASN A 326 ? 0.30278 0.35905 0.32912 0.07117  0.07702  0.03106  337 ASN A OD1 
2610 N ND2 . ASN A 326 ? 0.27949 0.30559 0.25746 0.06913  0.06447  0.00778  337 ASN A ND2 
2611 N N   . LEU A 327 ? 0.23902 0.26283 0.31306 0.03686  0.03513  0.00164  338 LEU A N   
2612 C CA  . LEU A 327 ? 0.28757 0.30148 0.36419 0.03466  0.02329  -0.00899 338 LEU A CA  
2613 C C   . LEU A 327 ? 0.28948 0.30989 0.40229 0.03344  0.01644  -0.00466 338 LEU A C   
2614 O O   . LEU A 327 ? 0.23252 0.24571 0.34755 0.03441  0.00643  -0.01340 338 LEU A O   
2615 C CB  . LEU A 327 ? 0.21163 0.21442 0.27718 0.03087  0.01569  -0.01712 338 LEU A CB  
2616 C CG  . LEU A 327 ? 0.25474 0.24965 0.28758 0.03150  0.01933  -0.02231 338 LEU A CG  
2617 C CD1 . LEU A 327 ? 0.26119 0.24971 0.28590 0.02868  0.01476  -0.02649 338 LEU A CD1 
2618 C CD2 . LEU A 327 ? 0.23390 0.22203 0.24960 0.03494  0.01769  -0.02900 338 LEU A CD2 
2619 N N   . THR A 328 ? 0.25312 0.28714 0.39603 0.03180  0.02083  0.00955  339 THR A N   
2620 C CA  . THR A 328 ? 0.22465 0.26424 0.41000 0.02880  0.01137  0.01543  339 THR A CA  
2621 C C   . THR A 328 ? 0.28278 0.34275 0.49801 0.03147  0.02115  0.03322  339 THR A C   
2622 O O   . THR A 328 ? 0.20597 0.27140 0.46135 0.02862  0.01220  0.03928  339 THR A O   
2623 C CB  . THR A 328 ? 0.29420 0.33076 0.50170 0.02269  0.00250  0.01825  339 THR A CB  
2624 O OG1 . THR A 328 ? 0.29116 0.33945 0.50201 0.02182  0.01560  0.03270  339 THR A OG1 
2625 C CG2 . THR A 328 ? 0.23196 0.25050 0.41159 0.02235  -0.00711 0.00154  339 THR A CG2 
2626 N N   . ASN A 329 ? 0.21182 0.28355 0.41022 0.03817  0.03821  0.04224  340 ASN A N   
2627 C CA  . ASN A 329 ? 0.29677 0.39122 0.52458 0.04331  0.04908  0.06165  340 ASN A CA  
2628 C C   . ASN A 329 ? 0.21324 0.31040 0.44251 0.04856  0.04821  0.05801  340 ASN A C   
2629 O O   . ASN A 329 ? 0.27011 0.38735 0.52984 0.05277  0.05557  0.07453  340 ASN A O   
2630 C CB  . ASN A 329 ? 0.26216 0.37053 0.47156 0.05250  0.06809  0.07443  340 ASN A CB  
2631 C CG  . ASN A 329 ? 0.31260 0.40980 0.46917 0.06121  0.07323  0.06040  340 ASN A CG  
2632 O OD1 . ASN A 329 ? 0.23506 0.31884 0.37320 0.06121  0.06581  0.04514  340 ASN A OD1 
2633 N ND2 . ASN A 329 ? 0.26760 0.36985 0.40104 0.06935  0.08476  0.06609  340 ASN A ND2 
2634 N N   . GLY A 330 ? 0.29730 0.37617 0.49687 0.04875  0.03973  0.03853  341 GLY A N   
2635 C CA  . GLY A 330 ? 0.28343 0.36290 0.48305 0.05362  0.03757  0.03386  341 GLY A CA  
2636 C C   . GLY A 330 ? 0.30279 0.39228 0.48058 0.06558  0.05247  0.03851  341 GLY A C   
2637 O O   . GLY A 330 ? 0.27932 0.37450 0.46478 0.07080  0.05272  0.03903  341 GLY A O   
2638 N N   . LYS A 331 ? 0.25639 0.34750 0.40642 0.07156  0.06371  0.04118  342 LYS A N   
2639 C CA  . LYS A 331 ? 0.31626 0.41415 0.44055 0.08619  0.07561  0.04325  342 LYS A CA  
2640 C C   . LYS A 331 ? 0.30538 0.38138 0.38658 0.08897  0.06937  0.02381  342 LYS A C   
2641 O O   . LYS A 331 ? 0.38823 0.46546 0.44855 0.10144  0.07457  0.02176  342 LYS A O   
2642 C CB  . LYS A 331 ? 0.25398 0.36462 0.36863 0.09490  0.08970  0.05612  342 LYS A CB  
2643 C CG  . LYS A 331 ? 0.28984 0.42625 0.44849 0.09462  0.09915  0.08045  342 LYS A CG  
2644 C CD  . LYS A 331 ? 0.32868 0.48688 0.51607 0.10277  0.10644  0.09456  342 LYS A CD  
2645 C CE  . LYS A 331 ? 0.39997 0.58665 0.63518 0.10307  0.11715  0.12297  342 LYS A CE  
2646 N NZ  . LYS A 331 ? 0.41254 0.61780 0.69397 0.10287  0.11725  0.13658  342 LYS A NZ  
2647 N N   . PHE A 332 ? 0.24931 0.30593 0.31786 0.07877  0.05819  0.01061  343 PHE A N   
2648 C CA  . PHE A 332 ? 0.34299 0.37996 0.37525 0.08025  0.05241  -0.00439 343 PHE A CA  
2649 C C   . PHE A 332 ? 0.37142 0.39809 0.40598 0.07641  0.04208  -0.01424 343 PHE A C   
2650 O O   . PHE A 332 ? 0.39310 0.42122 0.45165 0.06955  0.03535  -0.01405 343 PHE A O   
2651 C CB  . PHE A 332 ? 0.31648 0.34116 0.33223 0.07318  0.04878  -0.00965 343 PHE A CB  
2652 C CG  . PHE A 332 ? 0.27041 0.30178 0.27581 0.07910  0.05774  -0.00242 343 PHE A CG  
2653 C CD1 . PHE A 332 ? 0.27078 0.29659 0.24636 0.09057  0.06024  -0.00651 343 PHE A CD1 
2654 C CD2 . PHE A 332 ? 0.29102 0.33363 0.31664 0.07468  0.06248  0.00844  343 PHE A CD2 
2655 C CE1 . PHE A 332 ? 0.28036 0.31172 0.24337 0.09875  0.06750  -0.00063 343 PHE A CE1 
2656 C CE2 . PHE A 332 ? 0.25563 0.30512 0.27064 0.08153  0.07122  0.01600  343 PHE A CE2 
2657 C CZ  . PHE A 332 ? 0.27385 0.31794 0.25635 0.09420  0.07391  0.01123  343 PHE A CZ  
2658 N N   . ASN A 333 ? 0.39304 0.40844 0.40235 0.08215  0.03961  -0.02303 344 ASN A N   
2659 C CA  . ASN A 333 ? 0.35653 0.36217 0.36452 0.08052  0.03079  -0.03157 344 ASN A CA  
2660 C C   . ASN A 333 ? 0.46130 0.45113 0.45809 0.07208  0.02166  -0.03986 344 ASN A C   
2661 O O   . ASN A 333 ? 0.44665 0.43031 0.44588 0.07059  0.01418  -0.04531 344 ASN A O   
2662 C CB  . ASN A 333 ? 0.45955 0.45884 0.44609 0.09053  0.03111  -0.03674 344 ASN A CB  
2663 C CG  . ASN A 333 ? 0.68580 0.70228 0.68464 0.10160  0.03950  -0.02898 344 ASN A CG  
2664 O OD1 . ASN A 333 ? 0.61350 0.64566 0.64342 0.09969  0.04226  -0.02027 344 ASN A OD1 
2665 N ND2 . ASN A 333 ? 0.68875 0.70252 0.66453 0.11434  0.04274  -0.03159 344 ASN A ND2 
2666 N N   . SER A 334 ? 0.38362 0.36763 0.36765 0.06797  0.02234  -0.04022 345 SER A N   
2667 C CA  . SER A 334 ? 0.38197 0.35456 0.35749 0.06142  0.01545  -0.04536 345 SER A CA  
2668 C C   . SER A 334 ? 0.34778 0.32193 0.32369 0.05602  0.01773  -0.04211 345 SER A C   
2669 O O   . SER A 334 ? 0.33735 0.31819 0.31422 0.05759  0.02414  -0.03695 345 SER A O   
2670 C CB  . SER A 334 ? 0.32145 0.28008 0.27472 0.06286  0.01148  -0.05039 345 SER A CB  
2671 O OG  . SER A 334 ? 0.36344 0.31810 0.30293 0.06474  0.01380  -0.04968 345 SER A OG  
2672 N N   . ILE A 335 ? 0.38465 0.35310 0.35831 0.05126  0.01268  -0.04482 346 ILE A N   
2673 C CA  . ILE A 335 ? 0.33899 0.30777 0.31087 0.04648  0.01418  -0.04238 346 ILE A CA  
2674 C C   . ILE A 335 ? 0.31620 0.27936 0.27099 0.04634  0.01674  -0.04144 346 ILE A C   
2675 O O   . ILE A 335 ? 0.30386 0.27028 0.25839 0.04487  0.02038  -0.03808 346 ILE A O   
2676 C CB  . ILE A 335 ? 0.31001 0.27430 0.27965 0.04458  0.00847  -0.04547 346 ILE A CB  
2677 C CG1 . ILE A 335 ? 0.33686 0.30461 0.32395 0.04653  0.00257  -0.04830 346 ILE A CG1 
2678 C CG2 . ILE A 335 ? 0.27134 0.23576 0.23677 0.04042  0.01030  -0.04281 346 ILE A CG2 
2679 C CD1 . ILE A 335 ? 0.26482 0.22686 0.24478 0.05004  -0.00491 -0.05367 346 ILE A CD1 
2680 N N   A GLU A 336 ? 0.30088 0.25450 0.24230 0.04832  0.01331  -0.04447 347 GLU A N   
2681 N N   B GLU A 336 ? 0.29869 0.25231 0.24016 0.04836  0.01329  -0.04450 347 GLU A N   
2682 C CA  A GLU A 336 ? 0.36194 0.30712 0.28950 0.04861  0.01160  -0.04476 347 GLU A CA  
2683 C CA  B GLU A 336 ? 0.36190 0.30677 0.28927 0.04876  0.01140  -0.04493 347 GLU A CA  
2684 C C   A GLU A 336 ? 0.36576 0.31494 0.28894 0.05517  0.01598  -0.04421 347 GLU A C   
2685 C C   B GLU A 336 ? 0.36554 0.31422 0.28831 0.05525  0.01569  -0.04442 347 GLU A C   
2686 O O   A GLU A 336 ? 0.35446 0.30081 0.26974 0.05541  0.01575  -0.04355 347 GLU A O   
2687 O O   B GLU A 336 ? 0.35542 0.30060 0.26979 0.05551  0.01505  -0.04399 347 GLU A O   
2688 C CB  A GLU A 336 ? 0.38219 0.31545 0.30048 0.05019  0.00502  -0.04770 347 GLU A CB  
2689 C CB  B GLU A 336 ? 0.38241 0.31574 0.30093 0.05060  0.00497  -0.04796 347 GLU A CB  
2690 C CG  A GLU A 336 ? 0.40207 0.33140 0.32173 0.04480  0.00152  -0.04480 347 GLU A CG  
2691 C CG  B GLU A 336 ? 0.40474 0.32546 0.31341 0.04935  -0.00178 -0.04833 347 GLU A CG  
2692 C CD  A GLU A 336 ? 0.38136 0.31494 0.30591 0.04663  0.00197  -0.04559 347 GLU A CD  
2693 C CD  B GLU A 336 ? 0.46972 0.37801 0.37305 0.05169  -0.00970 -0.05075 347 GLU A CD  
2694 O OE1 A GLU A 336 ? 0.33331 0.27355 0.26498 0.04976  0.00409  -0.04840 347 GLU A OE1 
2695 O OE1 B GLU A 336 ? 0.48290 0.39306 0.38733 0.05530  -0.00859 -0.05275 347 GLU A OE1 
2696 O OE2 A GLU A 336 ? 0.39956 0.33011 0.32179 0.04577  -0.00035 -0.04248 347 GLU A OE2 
2697 O OE2 B GLU A 336 ? 0.46925 0.36526 0.36924 0.04984  -0.01832 -0.05044 347 GLU A OE2 
2698 N N   . GLU A 337 ? 0.30956 0.26644 0.23779 0.06195  0.02020  -0.04366 348 GLU A N   
2699 C CA  . GLU A 337 ? 0.37880 0.34218 0.30097 0.07186  0.02618  -0.04120 348 GLU A CA  
2700 C C   . GLU A 337 ? 0.35078 0.32749 0.28484 0.07016  0.03401  -0.03317 348 GLU A C   
2701 O O   . GLU A 337 ? 0.35625 0.33563 0.27979 0.07727  0.03815  -0.03056 348 GLU A O   
2702 C CB  . GLU A 337 ? 0.37324 0.34359 0.29927 0.08086  0.02959  -0.04075 348 GLU A CB  
2703 C CG  . GLU A 337 ? 0.47684 0.43270 0.38465 0.08718  0.02206  -0.04894 348 GLU A CG  
2704 C CD  . GLU A 337 ? 0.54000 0.50077 0.45513 0.09229  0.02314  -0.04966 348 GLU A CD  
2705 O OE1 . GLU A 337 ? 0.62024 0.58433 0.55159 0.08487  0.02194  -0.04872 348 GLU A OE1 
2706 O OE2 . GLU A 337 ? 0.62698 0.58789 0.53066 0.10510  0.02437  -0.05171 348 GLU A OE2 
2707 N N   . ALA A 338 ? 0.28995 0.27432 0.24555 0.06216  0.03501  -0.02931 349 ALA A N   
2708 C CA  . ALA A 338 ? 0.31435 0.30866 0.28326 0.05873  0.04005  -0.02172 349 ALA A CA  
2709 C C   . ALA A 338 ? 0.30987 0.29578 0.26423 0.05496  0.03766  -0.02395 349 ALA A C   
2710 O O   . ALA A 338 ? 0.25386 0.24548 0.20652 0.05758  0.04285  -0.01855 349 ALA A O   
2711 C CB  . ALA A 338 ? 0.23940 0.23867 0.23356 0.05108  0.03690  -0.01986 349 ALA A CB  
2712 N N   . ILE A 339 ? 0.31385 0.28738 0.25911 0.04934  0.03007  -0.03046 350 ILE A N   
2713 C CA  . ILE A 339 ? 0.30422 0.27029 0.23908 0.04527  0.02681  -0.03161 350 ILE A CA  
2714 C C   . ILE A 339 ? 0.32543 0.28514 0.24194 0.05298  0.02562  -0.03364 350 ILE A C   
2715 O O   . ILE A 339 ? 0.34581 0.30647 0.25701 0.05428  0.02709  -0.03152 350 ILE A O   
2716 C CB  . ILE A 339 ? 0.27372 0.23061 0.20602 0.03916  0.01991  -0.03500 350 ILE A CB  
2717 C CG1 . ILE A 339 ? 0.26403 0.22652 0.20926 0.03426  0.02017  -0.03371 350 ILE A CG1 
2718 C CG2 . ILE A 339 ? 0.30311 0.25091 0.22534 0.03649  0.01489  -0.03539 350 ILE A CG2 
2719 C CD1 . ILE A 339 ? 0.31546 0.27240 0.25705 0.03214  0.01558  -0.03513 350 ILE A CD1 
2720 N N   . GLU A 340 ? 0.31527 0.26709 0.22065 0.05949  0.02149  -0.03869 351 GLU A N   
2721 C CA  . GLU A 340 ? 0.33267 0.27534 0.21786 0.06998  0.01708  -0.04317 351 GLU A CA  
2722 C C   . GLU A 340 ? 0.37123 0.32520 0.25090 0.08046  0.02602  -0.03827 351 GLU A C   
2723 O O   . GLU A 340 ? 0.40123 0.34925 0.26571 0.08648  0.02270  -0.04036 351 GLU A O   
2724 C CB  . GLU A 340 ? 0.39353 0.32808 0.26941 0.07781  0.01211  -0.04915 351 GLU A CB  
2725 C CG  . GLU A 340 ? 0.46643 0.39042 0.31870 0.09310  0.00590  -0.05575 351 GLU A CG  
2726 C CD  . GLU A 340 ? 0.62329 0.52791 0.46652 0.08999  -0.00912 -0.06196 351 GLU A CD  
2727 O OE1 . GLU A 340 ? 0.63732 0.53927 0.49423 0.07557  -0.01257 -0.05904 351 GLU A OE1 
2728 O OE2 . GLU A 340 ? 0.73805 0.63017 0.56137 0.10301  -0.01837 -0.06944 351 GLU A OE2 
2729 N N   . ASN A 341 ? 0.35786 0.32874 0.25127 0.08343  0.03700  -0.03058 352 ASN A N   
2730 C CA  . ASN A 341 ? 0.30308 0.28841 0.19492 0.09424  0.04769  -0.02180 352 ASN A CA  
2731 C C   . ASN A 341 ? 0.29557 0.28434 0.19290 0.08759  0.04990  -0.01657 352 ASN A C   
2732 O O   . ASN A 341 ? 0.36453 0.35582 0.24771 0.09772  0.05333  -0.01366 352 ASN A O   
2733 C CB  . ASN A 341 ? 0.29486 0.29929 0.20864 0.09666  0.05837  -0.01161 352 ASN A CB  
2734 C CG  . ASN A 341 ? 0.36659 0.38945 0.28185 0.10938  0.07138  0.00145  352 ASN A CG  
2735 O OD1 . ASN A 341 ? 0.31773 0.35209 0.25150 0.10367  0.07757  0.01216  352 ASN A OD1 
2736 N ND2 . ASN A 341 ? 0.32405 0.34975 0.21877 0.12823  0.07536  0.00116  352 ASN A ND2 
2737 N N   . TYR A 342 ? 0.29514 0.28371 0.21095 0.07242  0.04751  -0.01573 353 TYR A N   
2738 C CA  . TYR A 342 ? 0.27348 0.26308 0.19341 0.06583  0.04783  -0.01234 353 TYR A CA  
2739 C C   . TYR A 342 ? 0.34349 0.31864 0.24102 0.06812  0.03962  -0.01964 353 TYR A C   
2740 O O   . TYR A 342 ? 0.32720 0.30425 0.21572 0.07363  0.04187  -0.01668 353 TYR A O   
2741 C CB  . TYR A 342 ? 0.27215 0.26161 0.21179 0.05171  0.04451  -0.01261 353 TYR A CB  
2742 C CG  . TYR A 342 ? 0.30132 0.28483 0.23744 0.04481  0.04030  -0.01415 353 TYR A CG  
2743 C CD1 . TYR A 342 ? 0.27602 0.26539 0.21247 0.04659  0.04483  -0.00802 353 TYR A CD1 
2744 C CD2 . TYR A 342 ? 0.26566 0.23922 0.19899 0.03746  0.03252  -0.02011 353 TYR A CD2 
2745 C CE1 . TYR A 342 ? 0.27189 0.25620 0.20531 0.04093  0.04082  -0.00946 353 TYR A CE1 
2746 C CE2 . TYR A 342 ? 0.30310 0.27341 0.23505 0.03204  0.02940  -0.02000 353 TYR A CE2 
2747 C CZ  . TYR A 342 ? 0.26150 0.23665 0.19321 0.03364  0.03314  -0.01548 353 TYR A CZ  
2748 O OH  . TYR A 342 ? 0.28268 0.25512 0.21355 0.02877  0.02999  -0.01531 353 TYR A OH  
2749 N N   . GLU A 343 ? 0.33544 0.29598 0.22590 0.06400  0.02909  -0.02833 354 GLU A N   
2750 C CA  . GLU A 343 ? 0.35850 0.30463 0.23487 0.06407  0.01849  -0.03422 354 GLU A CA  
2751 C C   . GLU A 343 ? 0.38610 0.32673 0.23889 0.08069  0.01593  -0.03813 354 GLU A C   
2752 O O   . GLU A 343 ? 0.33853 0.27300 0.18056 0.08393  0.01067  -0.04006 354 GLU A O   
2753 C CB  . GLU A 343 ? 0.30066 0.23360 0.17929 0.05667  0.00754  -0.03976 354 GLU A CB  
2754 C CG  . GLU A 343 ? 0.35141 0.29013 0.24896 0.04317  0.00993  -0.03539 354 GLU A CG  
2755 C CD  . GLU A 343 ? 0.34769 0.27690 0.24909 0.03714  0.00156  -0.03714 354 GLU A CD  
2756 O OE1 . GLU A 343 ? 0.38833 0.30538 0.28093 0.04173  -0.00708 -0.04201 354 GLU A OE1 
2757 O OE2 . GLU A 343 ? 0.31728 0.25136 0.23056 0.02906  0.00336  -0.03298 354 GLU A OE2 
2758 N N   . GLN A 344 ? 0.43180 0.37500 0.27511 0.09324  0.01939  -0.03944 355 GLN A N   
2759 C CA  . GLN A 344 ? 0.39213 0.33064 0.20876 0.11344  0.01708  -0.04367 355 GLN A CA  
2760 C C   . GLN A 344 ? 0.40876 0.36093 0.22075 0.12159  0.02790  -0.03478 355 GLN A C   
2761 O O   . GLN A 344 ? 0.42003 0.36389 0.20966 0.13390  0.02173  -0.03941 355 GLN A O   
2762 C CB  . GLN A 344 ? 0.55079 0.49305 0.35910 0.12702  0.02110  -0.04504 355 GLN A CB  
2763 C CG  . GLN A 344 ? 0.57636 0.50182 0.38347 0.12311  0.00818  -0.05521 355 GLN A CG  
2764 C CD  . GLN A 344 ? 0.69934 0.59984 0.48553 0.13038  -0.01175 -0.06820 355 GLN A CD  
2765 O OE1 . GLN A 344 ? 0.66718 0.55943 0.44871 0.12838  -0.01965 -0.07045 355 GLN A OE1 
2766 N NE2 . GLN A 344 ? 0.82267 0.71013 0.59800 0.13896  -0.02158 -0.07698 355 GLN A NE2 
2767 N N   . GLN A 345 ? 0.38415 0.35660 0.21787 0.11566  0.04278  -0.02171 356 GLN A N   
2768 C CA  . GLN A 345 ? 0.44552 0.43189 0.27885 0.12233  0.05342  -0.01062 356 GLN A CA  
2769 C C   . GLN A 345 ? 0.40365 0.38111 0.23642 0.11269  0.04608  -0.01343 356 GLN A C   
2770 O O   . GLN A 345 ? 0.40133 0.37792 0.21645 0.12391  0.04604  -0.01251 356 GLN A O   
2771 C CB  . GLN A 345 ? 0.32965 0.33847 0.19336 0.11596  0.06835  0.00520  356 GLN A CB  
2772 C CG  . GLN A 345 ? 0.36372 0.38596 0.23230 0.12674  0.07765  0.01164  356 GLN A CG  
2773 C CD  . GLN A 345 ? 0.38069 0.42470 0.28581 0.11917  0.08984  0.02863  356 GLN A CD  
2774 O OE1 . GLN A 345 ? 0.45667 0.51498 0.37233 0.12175  0.09937  0.04278  356 GLN A OE1 
2775 N NE2 . GLN A 345 ? 0.30938 0.35519 0.23579 0.10980  0.08817  0.02763  356 GLN A NE2 
2776 N N   . MET A 346 ? 0.34620 0.31748 0.19690 0.09364  0.03980  -0.01667 357 MET A N   
2777 C CA  . MET A 346 ? 0.35654 0.32262 0.21134 0.08359  0.03443  -0.01740 357 MET A CA  
2778 C C   . MET A 346 ? 0.45670 0.40482 0.28899 0.09033  0.02016  -0.02775 357 MET A C   
2779 O O   . MET A 346 ? 0.40724 0.35305 0.23481 0.09040  0.01721  -0.02718 357 MET A O   
2780 C CB  . MET A 346 ? 0.29425 0.25899 0.17128 0.06501  0.03132  -0.01820 357 MET A CB  
2781 C CG  . MET A 346 ? 0.31832 0.27819 0.20031 0.05503  0.02540  -0.01898 357 MET A CG  
2782 S SD  . MET A 346 ? 0.36610 0.30638 0.23874 0.05205  0.00808  -0.02886 357 MET A SD  
2783 C CE  . MET A 346 ? 0.33645 0.27483 0.22139 0.04395  0.00644  -0.03060 357 MET A CE  
2784 N N   . PHE A 347 ? 0.38724 0.32128 0.20699 0.09606  0.00935  -0.03758 358 PHE A N   
2785 C CA  . PHE A 347 ? 0.48847 0.40304 0.28901 0.10366  -0.00782 -0.04816 358 PHE A CA  
2786 C C   . PHE A 347 ? 0.53657 0.45239 0.31052 0.12472  -0.00582 -0.04862 358 PHE A C   
2787 O O   . PHE A 347 ? 0.53728 0.44035 0.29833 0.12958  -0.01841 -0.05498 358 PHE A O   
2788 C CB  . PHE A 347 ? 0.47781 0.37565 0.27173 0.10681  -0.02159 -0.05846 358 PHE A CB  
2789 C CG  . PHE A 347 ? 0.57822 0.46564 0.39251 0.08859  -0.03324 -0.06025 358 PHE A CG  
2790 C CD1 . PHE A 347 ? 0.42443 0.32358 0.26273 0.07214  -0.02374 -0.05234 358 PHE A CD1 
2791 C CD2 . PHE A 347 ? 0.60384 0.46995 0.41428 0.08934  -0.05457 -0.06894 358 PHE A CD2 
2792 C CE1 . PHE A 347 ? 0.46960 0.36226 0.32578 0.05796  -0.03230 -0.05131 358 PHE A CE1 
2793 C CE2 . PHE A 347 ? 0.58959 0.44913 0.42341 0.07272  -0.06406 -0.06667 358 PHE A CE2 
2794 C CZ  . PHE A 347 ? 0.60009 0.47427 0.45581 0.05764  -0.05145 -0.05697 358 PHE A CZ  
2795 N N   . ILE A 348 ? 0.51357 0.44574 0.28000 0.13834  0.00995  -0.04070 359 ILE A N   
2796 C CA  . ILE A 348 ? 0.47070 0.40658 0.20960 0.16169  0.01380  -0.03894 359 ILE A CA  
2797 C C   . ILE A 348 ? 0.49916 0.44460 0.24545 0.15632  0.02078  -0.02950 359 ILE A C   
2798 O O   . ILE A 348 ? 0.57563 0.50884 0.30533 0.16250  0.00942  -0.03616 359 ILE A O   
2799 C CB  . ILE A 348 ? 0.52134 0.47514 0.25196 0.17967  0.03023  -0.03004 359 ILE A CB  
2800 C CG1 . ILE A 348 ? 0.51748 0.46029 0.24274 0.18431  0.02040  -0.03991 359 ILE A CG1 
2801 C CG2 . ILE A 348 ? 0.47697 0.43827 0.19154 0.20037  0.03264  -0.02295 359 ILE A CG2 
2802 C CD1 . ILE A 348 ? 0.52032 0.48245 0.24981 0.19574  0.03447  -0.02888 359 ILE A CD1 
2803 N N   . TYR A 349 ? 0.43922 0.40523 0.21172 0.14486  0.03761  -0.01436 360 TYR A N   
2804 C CA  . TYR A 349 ? 0.43153 0.40584 0.21260 0.13955  0.04345  -0.00509 360 TYR A CA  
2805 C C   . TYR A 349 ? 0.46764 0.42834 0.25960 0.12120  0.03016  -0.01282 360 TYR A C   
2806 O O   . TYR A 349 ? 0.47689 0.43753 0.26611 0.12103  0.02905  -0.01030 360 TYR A O   
2807 C CB  . TYR A 349 ? 0.39977 0.39751 0.21023 0.13143  0.06183  0.01306  360 TYR A CB  
2808 C CG  . TYR A 349 ? 0.36666 0.36680 0.20911 0.11006  0.06209  0.01353  360 TYR A CG  
2809 C CD1 . TYR A 349 ? 0.34549 0.33942 0.20489 0.09132  0.05536  0.01011  360 TYR A CD1 
2810 C CD2 . TYR A 349 ? 0.39125 0.40099 0.24605 0.11086  0.06934  0.01799  360 TYR A CD2 
2811 C CE1 . TYR A 349 ? 0.33927 0.33509 0.22356 0.07557  0.05502  0.00988  360 TYR A CE1 
2812 C CE2 . TYR A 349 ? 0.30928 0.32023 0.19120 0.09354  0.06815  0.01753  360 TYR A CE2 
2813 C CZ  . TYR A 349 ? 0.33701 0.34055 0.23183 0.07693  0.06082  0.01307  360 TYR A CZ  
2814 O OH  . TYR A 349 ? 0.27360 0.27766 0.19065 0.06341  0.05884  0.01166  360 TYR A OH  
2815 N N   . GLY A 350 ? 0.46431 0.41504 0.26942 0.10655  0.02086  -0.02062 361 GLY A N   
2816 C CA  . GLY A 350 ? 0.40802 0.34830 0.22434 0.09126  0.00914  -0.02566 361 GLY A CA  
2817 C C   . GLY A 350 ? 0.46316 0.38486 0.25897 0.10016  -0.00848 -0.03645 361 GLY A C   
2818 O O   . GLY A 350 ? 0.44633 0.36454 0.24531 0.09511  -0.01440 -0.03655 361 GLY A O   
2819 N N   . LYS A 351 ? 0.45850 0.36718 0.23315 0.11469  -0.01855 -0.04622 362 LYS A N   
2820 C CA  . LYS A 351 ? 0.51953 0.40739 0.27388 0.12575  -0.03918 -0.05837 362 LYS A CA  
2821 C C   . LYS A 351 ? 0.55617 0.44741 0.28780 0.14261  -0.03598 -0.05644 362 LYS A C   
2822 O O   . LYS A 351 ? 0.56062 0.43874 0.28530 0.14469  -0.05114 -0.06304 362 LYS A O   
2823 C CB  . LYS A 351 ? 0.56975 0.44149 0.30418 0.14069  -0.05209 -0.07036 362 LYS A CB  
2824 C CG  . LYS A 351 ? 0.63295 0.49048 0.38648 0.12591  -0.06693 -0.07643 362 LYS A CG  
2825 C CD  . LYS A 351 ? 0.59081 0.42729 0.32201 0.14327  -0.08505 -0.09056 362 LYS A CD  
2826 C CE  . LYS A 351 ? 0.62619 0.45694 0.37772 0.12973  -0.09014 -0.09149 362 LYS A CE  
2827 N NZ  . LYS A 351 ? 0.76093 0.56698 0.49604 0.14367  -0.11278 -0.10603 362 LYS A NZ  
2828 N N   . GLU A 352 ? 0.56512 0.47424 0.28577 0.15591  -0.01686 -0.04648 363 GLU A N   
2829 C CA  . GLU A 352 ? 0.57997 0.49535 0.27984 0.17288  -0.01115 -0.04135 363 GLU A CA  
2830 C C   . GLU A 352 ? 0.53704 0.45869 0.25747 0.15606  -0.00791 -0.03386 363 GLU A C   
2831 O O   . GLU A 352 ? 0.59150 0.50490 0.29804 0.16310  -0.01723 -0.03777 363 GLU A O   
2832 C CB  . GLU A 352 ? 0.53595 0.47361 0.22841 0.18859  0.01101  -0.02727 363 GLU A CB  
2833 C CG  . GLU A 352 ? 0.76708 0.70207 0.45430 0.19893  0.00813  -0.03198 363 GLU A CG  
2834 C CD  . GLU A 352 ? 0.92800 0.88103 0.60890 0.21979  0.02156  -0.01936 363 GLU A CD  
2835 O OE1 . GLU A 352 ? 1.05272 1.00119 0.72340 0.23311  0.01597  -0.02457 363 GLU A OE1 
2836 O OE2 . GLU A 352 ? 1.10075 1.07247 0.78799 0.22320  0.03702  -0.00347 363 GLU A OE2 
2837 N N   . ALA A 353 ? 0.47208 0.40722 0.22499 0.13479  0.00382  -0.02405 364 ALA A N   
2838 C CA  . ALA A 353 ? 0.43629 0.37685 0.20871 0.11960  0.00617  -0.01775 364 ALA A CA  
2839 C C   . ALA A 353 ? 0.44749 0.37022 0.22276 0.11067  -0.01384 -0.02893 364 ALA A C   
2840 O O   . ALA A 353 ? 0.46861 0.38952 0.24246 0.11013  -0.01806 -0.02816 364 ALA A O   
2841 C CB  . ALA A 353 ? 0.42139 0.37667 0.22633 0.10071  0.01901  -0.00787 364 ALA A CB  
2842 N N   . GLN A 354 ? 0.45009 0.35985 0.23099 0.10419  -0.02688 -0.03827 365 GLN A N   
2843 C CA  . GLN A 354 ? 0.42658 0.32098 0.21671 0.09499  -0.04645 -0.04597 365 GLN A CA  
2844 C C   . GLN A 354 ? 0.54404 0.42157 0.30814 0.11237  -0.06393 -0.05616 365 GLN A C   
2845 O O   . GLN A 354 ? 0.52540 0.39693 0.29571 0.10762  -0.07474 -0.05780 365 GLN A O   
2846 C CB  . GLN A 354 ? 0.39560 0.28091 0.20079 0.08466  -0.05631 -0.05091 365 GLN A CB  
2847 C CG  . GLN A 354 ? 0.36228 0.26221 0.19550 0.06596  -0.04316 -0.04167 365 GLN A CG  
2848 C CD  . GLN A 354 ? 0.38782 0.27969 0.23932 0.05446  -0.05383 -0.04395 365 GLN A CD  
2849 O OE1 . GLN A 354 ? 0.46523 0.34105 0.30865 0.06076  -0.06889 -0.05231 365 GLN A OE1 
2850 N NE2 . GLN A 354 ? 0.33106 0.23401 0.20714 0.03891  -0.04650 -0.03595 365 GLN A NE2 
2851 N N   . GLU A 355 ? 0.52837 0.39791 0.26233 0.13422  -0.06774 -0.06347 366 GLU A N   
2852 C CA  . GLU A 355 ? 0.57661 0.42844 0.28076 0.15505  -0.08606 -0.07497 366 GLU A CA  
2853 C C   . GLU A 355 ? 0.61463 0.47604 0.30940 0.16124  -0.07772 -0.06792 366 GLU A C   
2854 O O   . GLU A 355 ? 0.63063 0.47909 0.32094 0.16362  -0.09472 -0.07470 366 GLU A O   
2855 C CB  . GLU A 355 ? 0.59837 0.44397 0.26970 0.18100  -0.08766 -0.08224 366 GLU A CB  
2856 C CG  . GLU A 355 ? 0.79904 0.63003 0.47830 0.17733  -0.10159 -0.09160 366 GLU A CG  
2857 C CD  . GLU A 355 ? 0.90260 0.73641 0.56569 0.19887  -0.09660 -0.09194 366 GLU A CD  
2858 O OE1 . GLU A 355 ? 0.95480 0.79645 0.62287 0.19528  -0.08611 -0.08886 366 GLU A OE1 
2859 O OE2 . GLU A 355 ? 1.02774 0.85601 0.67278 0.22063  -0.10354 -0.09518 366 GLU A OE2 
2860 N N   . GLU A 356 ? 0.54286 0.42709 0.23789 0.16308  -0.05234 -0.05329 367 GLU A N   
2861 C CA  . GLU A 356 ? 0.56772 0.46238 0.25610 0.16870  -0.04297 -0.04417 367 GLU A CA  
2862 C C   . GLU A 356 ? 0.57102 0.46586 0.28784 0.14625  -0.04767 -0.04175 367 GLU A C   
2863 O O   . GLU A 356 ? 0.59648 0.48590 0.30440 0.15155  -0.05574 -0.04367 367 GLU A O   
2864 C CB  . GLU A 356 ? 0.61172 0.53164 0.30337 0.17244  -0.01545 -0.02627 367 GLU A CB  
2865 C CG  . GLU A 356 ? 0.80044 0.73254 0.48948 0.17707  -0.00460 -0.01394 367 GLU A CG  
2866 C CD  . GLU A 356 ? 1.05435 1.01180 0.75214 0.18073  0.02132  0.00640  367 GLU A CD  
2867 O OE1 . GLU A 356 ? 1.06075 1.02589 0.75785 0.18641  0.03033  0.00975  367 GLU A OE1 
2868 O OE2 . GLU A 356 ? 1.01908 0.98882 0.72702 0.17769  0.03189  0.01983  367 GLU A OE2 
2869 N N   A SER A 357 ? 0.55058 0.45220 0.30054 0.12274  -0.04262 -0.03738 368 SER A N   
2870 N N   B SER A 357 ? 0.55021 0.45184 0.30007 0.12282  -0.04259 -0.03738 368 SER A N   
2871 C CA  A SER A 357 ? 0.52126 0.42516 0.29745 0.10364  -0.04579 -0.03424 368 SER A CA  
2872 C CA  B SER A 357 ? 0.52123 0.42505 0.29746 0.10361  -0.04585 -0.03431 368 SER A CA  
2873 C C   A SER A 357 ? 0.51196 0.39644 0.28937 0.10214  -0.07093 -0.04576 368 SER A C   
2874 C C   B SER A 357 ? 0.51240 0.39684 0.28954 0.10232  -0.07093 -0.04581 368 SER A C   
2875 O O   A SER A 357 ? 0.50696 0.39040 0.29147 0.09772  -0.07708 -0.04483 368 SER A O   
2876 O O   B SER A 357 ? 0.50759 0.39104 0.29175 0.09794  -0.07700 -0.04483 368 SER A O   
2877 C CB  A SER A 357 ? 0.45398 0.36926 0.26137 0.08291  -0.03546 -0.02762 368 SER A CB  
2878 C CB  B SER A 357 ? 0.45498 0.36960 0.26216 0.08300  -0.03610 -0.02809 368 SER A CB  
2879 O OG  A SER A 357 ? 0.48101 0.38582 0.29779 0.07591  -0.04742 -0.03486 368 SER A OG  
2880 O OG  B SER A 357 ? 0.47787 0.39337 0.30841 0.06719  -0.04157 -0.02644 368 SER A OG  
2881 N N   . THR A 358 ? 0.48495 0.35337 0.25728 0.10617  -0.08704 -0.05638 369 THR A N   
2882 C CA  . THR A 358 ? 0.50819 0.35665 0.28672 0.10456  -0.11404 -0.06661 369 THR A CA  
2883 C C   . THR A 358 ? 0.60331 0.43804 0.35114 0.12580  -0.12840 -0.07577 369 THR A C   
2884 O O   . THR A 358 ? 0.61255 0.43876 0.36991 0.12192  -0.14443 -0.07894 369 THR A O   
2885 C CB  . THR A 358 ? 0.50442 0.33804 0.28766 0.10367  -0.12888 -0.07495 369 THR A CB  
2886 O OG1 . THR A 358 ? 0.52307 0.36922 0.33805 0.08272  -0.11772 -0.06557 369 THR A OG1 
2887 C CG2 . THR A 358 ? 0.49603 0.30593 0.28613 0.10481  -0.16079 -0.08598 369 THR A CG2 
2888 N N   . GLN A 359 ? 0.57078 0.40417 0.28139 0.14981  -0.12276 -0.07941 370 GLN A N   
2889 C CA  . GLN A 359 ? 0.67754 0.49926 0.35379 0.17397  -0.13476 -0.08752 370 GLN A CA  
2890 C C   . GLN A 359 ? 0.63378 0.46910 0.31499 0.16948  -0.12324 -0.07707 370 GLN A C   
2891 O O   . GLN A 359 ? 0.65596 0.47941 0.33163 0.17447  -0.14050 -0.08354 370 GLN A O   
2892 C CB  . GLN A 359 ? 0.64212 0.46873 0.29181 0.19897  -0.12196 -0.08648 370 GLN A CB  
2893 C CG  . GLN A 359 ? 0.93572 0.74122 0.57957 0.21300  -0.14211 -0.10008 370 GLN A CG  
2894 C CD  . GLN A 359 ? 0.90164 0.68257 0.55866 0.20874  -0.17285 -0.11235 370 GLN A CD  
2895 O OE1 . GLN A 359 ? 0.87562 0.65036 0.52509 0.21793  -0.18067 -0.11516 370 GLN A OE1 
2896 N NE2 . GLN A 359 ? 0.95613 0.72343 0.63610 0.19445  -0.19030 -0.11838 370 GLN A NE2 
2897 N N   . ASN A 360 ? 0.59943 0.45875 0.29291 0.15993  -0.09562 -0.06105 371 ASN A N   
2898 C CA  . ASN A 360 ? 0.59011 0.46241 0.29236 0.15376  -0.08455 -0.05023 371 ASN A CA  
2899 C C   . ASN A 360 ? 0.58912 0.45531 0.32043 0.13434  -0.09925 -0.05300 371 ASN A C   
2900 O O   . ASN A 360 ? 0.56584 0.42924 0.29254 0.13806  -0.10592 -0.05334 371 ASN A O   
2901 C CB  . ASN A 360 ? 0.55534 0.45184 0.27493 0.14283  -0.05648 -0.03338 371 ASN A CB  
2902 C CG  . ASN A 360 ? 0.69412 0.60286 0.42317 0.13743  -0.04587 -0.02208 371 ASN A CG  
2903 O OD1 . ASN A 360 ? 0.81481 0.72578 0.57098 0.11836  -0.04843 -0.02041 371 ASN A OD1 
2904 N ND2 . ASN A 360 ? 0.78139 0.69880 0.48814 0.15548  -0.03379 -0.01323 371 ASN A ND2 
2905 N N   . GLU A 361 ? 0.51470 0.38000 0.27655 0.11458  -0.10396 -0.05373 372 GLU A N   
2906 C CA  . GLU A 361 ? 0.53453 0.39741 0.32752 0.09685  -0.11639 -0.05343 372 GLU A CA  
2907 C C   . GLU A 361 ? 0.60648 0.44770 0.38996 0.10702  -0.14508 -0.06584 372 GLU A C   
2908 O O   . GLU A 361 ? 0.57469 0.41584 0.36803 0.10305  -0.15230 -0.06449 372 GLU A O   
2909 C CB  . GLU A 361 ? 0.51844 0.38428 0.34273 0.07815  -0.11670 -0.05085 372 GLU A CB  
2910 C CG  . GLU A 361 ? 0.54604 0.41533 0.40701 0.05973  -0.12502 -0.04590 372 GLU A CG  
2911 C CD  . GLU A 361 ? 0.49789 0.37229 0.38814 0.04394  -0.12338 -0.04084 372 GLU A CD  
2912 O OE1 . GLU A 361 ? 0.53263 0.39872 0.41516 0.04790  -0.12692 -0.04596 372 GLU A OE1 
2913 O OE2 . GLU A 361 ? 0.47607 0.36361 0.39593 0.02902  -0.11790 -0.03113 372 GLU A OE2 
2914 N N   . ILE A 362 ? 0.55845 0.38001 0.32274 0.12124  -0.16330 -0.07878 373 ILE A N   
2915 C CA  . ILE A 362 ? 0.67080 0.46779 0.42331 0.13422  -0.19471 -0.09318 373 ILE A CA  
2916 C C   . ILE A 362 ? 0.64973 0.44673 0.37439 0.15104  -0.19391 -0.09430 373 ILE A C   
2917 O O   . ILE A 362 ? 0.63048 0.41743 0.36371 0.15019  -0.21293 -0.09891 373 ILE A O   
2918 C CB  . ILE A 362 ? 0.59768 0.37465 0.32868 0.15176  -0.20949 -0.10665 373 ILE A CB  
2919 C CG1 . ILE A 362 ? 0.70367 0.47407 0.46548 0.13413  -0.22147 -0.10789 373 ILE A CG1 
2920 C CG2 . ILE A 362 ? 0.67669 0.43234 0.39780 0.17048  -0.22917 -0.11776 373 ILE A CG2 
2921 C CD1 . ILE A 362 ? 0.62200 0.37864 0.37106 0.14835  -0.22628 -0.11612 373 ILE A CD1 
2922 N N   . GLU A 363 ? 0.62896 0.43845 0.32264 0.16653  -0.17133 -0.08840 374 GLU A N   
2923 C CA  . GLU A 363 ? 0.60881 0.42003 0.27818 0.18458  -0.16653 -0.08698 374 GLU A CA  
2924 C C   . GLU A 363 ? 0.64718 0.47167 0.33429 0.16977  -0.15925 -0.07638 374 GLU A C   
2925 O O   . GLU A 363 ? 0.63875 0.45475 0.31823 0.17712  -0.17300 -0.08087 374 GLU A O   
2926 C CB  . GLU A 363 ? 0.65561 0.48052 0.29751 0.20384  -0.14134 -0.07922 374 GLU A CB  
2927 C CG  . GLU A 363 ? 0.84817 0.65783 0.46984 0.22862  -0.15044 -0.09066 374 GLU A CG  
2928 C CD  . GLU A 363 ? 1.02162 0.84202 0.63232 0.23821  -0.13273 -0.08559 374 GLU A CD  
2929 O OE1 . GLU A 363 ? 1.10393 0.94771 0.71283 0.23628  -0.10656 -0.06981 374 GLU A OE1 
2930 O OE2 . GLU A 363 ? 1.08183 0.88742 0.68851 0.24747  -0.14548 -0.09641 374 GLU A OE2 
2931 N N   . MET A 364 ? 0.56305 0.40848 0.28013 0.14791  -0.13665 -0.06224 375 MET A N   
2932 C CA  . MET A 364 ? 0.64651 0.50682 0.38281 0.13510  -0.12472 -0.05080 375 MET A CA  
2933 C C   . MET A 364 ? 0.64169 0.49522 0.40685 0.12042  -0.14379 -0.05460 375 MET A C   
2934 O O   . MET A 364 ? 0.58832 0.45074 0.36437 0.11412  -0.13859 -0.04772 375 MET A O   
2935 C CB  . MET A 364 ? 0.57575 0.45765 0.33559 0.11779  -0.09880 -0.03673 375 MET A CB  
2936 C CG  . MET A 364 ? 0.65612 0.54961 0.39461 0.13067  -0.07729 -0.02796 375 MET A CG  
2937 S SD  . MET A 364 ? 0.81591 0.73299 0.58471 0.11133  -0.05045 -0.01131 375 MET A SD  
2938 C CE  . MET A 364 ? 0.72064 0.64962 0.46254 0.13244  -0.03058 0.00136  375 MET A CE  
2939 N N   . PHE A 365 ? 0.64405 0.48300 0.42464 0.11473  -0.16571 -0.06394 376 PHE A N   
2940 C CA  . PHE A 365 ? 0.61104 0.44636 0.42656 0.09950  -0.18344 -0.06429 376 PHE A CA  
2941 C C   . PHE A 365 ? 0.68531 0.49532 0.49088 0.11250  -0.21711 -0.07912 376 PHE A C   
2942 O O   . PHE A 365 ? 0.74910 0.55360 0.58830 0.10011  -0.23656 -0.07975 376 PHE A O   
2943 C CB  . PHE A 365 ? 0.50267 0.34561 0.35703 0.07815  -0.18102 -0.05814 376 PHE A CB  
2944 C CG  . PHE A 365 ? 0.53334 0.40047 0.40287 0.06439  -0.15237 -0.04424 376 PHE A CG  
2945 C CD1 . PHE A 365 ? 0.49099 0.37262 0.38232 0.05326  -0.14460 -0.03494 376 PHE A CD1 
2946 C CD2 . PHE A 365 ? 0.42243 0.29706 0.28285 0.06446  -0.13424 -0.04123 376 PHE A CD2 
2947 C CE1 . PHE A 365 ? 0.48806 0.38967 0.39112 0.04307  -0.12070 -0.02399 376 PHE A CE1 
2948 C CE2 . PHE A 365 ? 0.51132 0.40600 0.38536 0.05325  -0.11071 -0.02988 376 PHE A CE2 
2949 C CZ  . PHE A 365 ? 0.48923 0.39659 0.38389 0.04303  -0.10463 -0.02185 376 PHE A CZ  
2950 N N   . LYS A 366 ? 0.69639 0.49126 0.45764 0.13833  -0.22517 -0.09049 377 LYS A N   
2951 C CA  . LYS A 366 ? 0.74487 0.51789 0.49998 0.15192  -0.24791 -0.10277 377 LYS A CA  
2952 C C   . LYS A 366 ? 0.80819 0.58761 0.56745 0.14992  -0.24870 -0.09824 377 LYS A C   
2953 O O   . LYS A 366 ? 0.83244 0.62951 0.57601 0.15166  -0.22859 -0.08819 377 LYS A O   
2954 C CB  . LYS A 366 ? 0.72953 0.49062 0.44329 0.18041  -0.24356 -0.11192 377 LYS A CB  
2955 C CG  . LYS A 366 ? 0.72470 0.47424 0.43713 0.18484  -0.24915 -0.11898 377 LYS A CG  
2956 C CD  . LYS A 366 ? 0.88536 0.62726 0.55748 0.21515  -0.24253 -0.12594 377 LYS A CD  
2957 C CE  . LYS A 366 ? 0.86693 0.58578 0.54144 0.22422  -0.26183 -0.13832 377 LYS A CE  
2958 N NZ  . LYS A 366 ? 0.88135 0.59604 0.59700 0.19829  -0.27564 -0.13693 377 LYS A NZ  
2959 N N   . PRO A 367 ? 0.94940 0.71465 0.73159 0.14616  -0.27145 -0.10429 378 PRO A N   
2960 C CA  . PRO A 367 ? 0.85114 0.62494 0.64544 0.13993  -0.27280 -0.09851 378 PRO A CA  
2961 C C   . PRO A 367 ? 0.85367 0.63240 0.60795 0.15899  -0.25757 -0.09733 378 PRO A C   
2962 O O   . PRO A 367 ? 0.81666 0.61029 0.57620 0.15251  -0.24897 -0.08768 378 PRO A O   
2963 C CB  . PRO A 367 ? 0.92887 0.68090 0.74888 0.13840  -0.30116 -0.10778 378 PRO A CB  
2964 C CG  . PRO A 367 ? 0.91386 0.65140 0.75094 0.13435  -0.31404 -0.11312 378 PRO A CG  
2965 C CD  . PRO A 367 ? 0.89663 0.63632 0.69566 0.14845  -0.29723 -0.11593 378 PRO A CD  
2966 N N   . ASP A 368 ? 0.82851 0.59619 0.54478 0.18322  -0.25332 -0.10545 379 ASP A N   
2967 C CA  . ASP A 368 ? 0.91734 0.69040 0.59757 0.20359  -0.23815 -0.10273 379 ASP A CA  
2968 C C   . ASP A 368 ? 0.94939 0.74195 0.60615 0.21041  -0.20843 -0.09081 379 ASP A C   
2969 O O   . ASP A 368 ? 0.90564 0.70116 0.53126 0.23225  -0.19498 -0.08883 379 ASP A O   
2970 C CB  . ASP A 368 ? 1.08299 0.83177 0.73885 0.22936  -0.25364 -0.11843 379 ASP A CB  
2971 C CG  . ASP A 368 ? 1.23949 0.97168 0.88845 0.23974  -0.26287 -0.12940 379 ASP A CG  
2972 O OD1 . ASP A 368 ? 1.02985 0.77096 0.69028 0.22724  -0.25478 -0.12427 379 ASP A OD1 
2973 O OD2 . ASP A 368 ? 1.30047 1.00959 0.93204 0.26176  -0.27912 -0.14351 379 ASP A OD2 
2974 N N   . PHE A 369 ? 0.93710 0.74389 0.61043 0.19264  -0.19743 -0.08157 380 PHE A N   
2975 C CA  . PHE A 369 ? 0.86153 0.68616 0.51695 0.19807  -0.16954 -0.06932 380 PHE A CA  
2976 C C   . PHE A 369 ? 0.82822 0.67140 0.47803 0.19815  -0.14934 -0.05311 380 PHE A C   
2977 O O   . PHE A 369 ? 0.76370 0.61261 0.43811 0.18191  -0.15101 -0.04801 380 PHE A O   
2978 C CB  . PHE A 369 ? 0.71172 0.54478 0.38955 0.17855  -0.16286 -0.06464 380 PHE A CB  
2979 C CG  . PHE A 369 ? 0.69651 0.55123 0.37118 0.17715  -0.13053 -0.04909 380 PHE A CG  
2980 C CD1 . PHE A 369 ? 0.73222 0.58722 0.37628 0.19661  -0.12187 -0.04936 380 PHE A CD1 
2981 C CD2 . PHE A 369 ? 0.63571 0.51024 0.33989 0.15704  -0.11020 -0.03418 380 PHE A CD2 
2982 C CE1 . PHE A 369 ? 0.72485 0.60077 0.37159 0.19452  -0.09321 -0.03341 380 PHE A CE1 
2983 C CE2 . PHE A 369 ? 0.66330 0.55600 0.36913 0.15522  -0.08382 -0.02001 380 PHE A CE2 
2984 C CZ  . PHE A 369 ? 0.60695 0.50102 0.28612 0.17308  -0.07512 -0.01879 380 PHE A CZ  
2985 N N   . THR A 370 ? 0.91078 0.76535 0.53785 0.21455  -0.12691 -0.04363 381 THR A N   
2986 C CA  . THR A 370 ? 0.95152 0.82640 0.57802 0.21361  -0.10321 -0.02403 381 THR A CA  
2987 C C   . THR A 370 ? 0.91761 0.80915 0.54079 0.21673  -0.07809 -0.01076 381 THR A C   
2988 O O   . THR A 370 ? 0.92283 0.81096 0.53234 0.23035  -0.07649 -0.01682 381 THR A O   
2989 C CB  . THR A 370 ? 1.00598 0.88085 0.61371 0.23239  -0.10019 -0.02188 381 THR A CB  
2990 O OG1 . THR A 370 ? 0.91485 0.79163 0.49883 0.25631  -0.08964 -0.02206 381 THR A OG1 
2991 C CG2 . THR A 370 ? 0.95741 0.81212 0.56535 0.23388  -0.12751 -0.03857 381 THR A CG2 
2992 N N   . PHE A 371 ? 0.84195 0.75206 0.48694 0.20188  -0.05788 0.00706  382 PHE A N   
2993 C CA  . PHE A 371 ? 0.86823 0.79618 0.51740 0.20280  -0.03352 0.02270  382 PHE A CA  
2994 C C   . PHE A 371 ? 0.93112 0.86873 0.55920 0.22737  -0.01923 0.03220  382 PHE A C   
2995 O O   . PHE A 371 ? 1.02784 0.97807 0.65698 0.23425  -0.00299 0.04101  382 PHE A O   
2996 C CB  . PHE A 371 ? 0.73689 0.68133 0.42678 0.17845  -0.01706 0.03800  382 PHE A CB  
2997 C CG  . PHE A 371 ? 0.69682 0.63873 0.42134 0.15176  -0.02310 0.02981  382 PHE A CG  
2998 C CD1 . PHE A 371 ? 0.67833 0.62459 0.41464 0.14375  -0.01620 0.02957  382 PHE A CD1 
2999 C CD2 . PHE A 371 ? 0.66336 0.60011 0.40848 0.13609  -0.03474 0.02367  382 PHE A CD2 
3000 C CE1 . PHE A 371 ? 0.59799 0.54294 0.36396 0.12147  -0.02088 0.02320  382 PHE A CE1 
3001 C CE2 . PHE A 371 ? 0.57159 0.50875 0.34727 0.11439  -0.03843 0.01843  382 PHE A CE2 
3002 C CZ  . PHE A 371 ? 0.55719 0.49827 0.34239 0.10745  -0.03142 0.01821  382 PHE A CZ  
# 
