data_8RSF
# 
_entry.id   8RSF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8RSF         pdb_00008rsf 10.2210/pdb8rsf/pdb 
WWPDB D_1292135452 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-12-04 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RSF 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-24 
_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                 3 
_pdbx_contact_author.email              ec.schulz@uke.de 
_pdbx_contact_author.name_first         Eike 
_pdbx_contact_author.name_last          Schulz 
_pdbx_contact_author.name_mi            C 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1685-8605 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bosman, R.'      1 0000-0002-9939-602X 
'Prester, A.'     2 0000-0003-2738-7682 
'von Soosten, L.' 3 0000-0001-7568-1013 
'Dibenedetto, S.' 4 ?                   
'Bartels, K.'     5 0000-0002-7980-1913 
'Sung, S.'        6 0000-0001-5820-4696 
'von Stetten, D.' 7 0000-0001-7906-9788 
'Mehrabi, P.'     8 0000-0003-3211-6959 
'Schulz, E.C.'    9 0000-0002-1685-8605 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Kapton-based HARE chips for fixed-target serial crystallography' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Bosman, R.'      1  0000-0001-5820-4696 
primary 'Prester, A.'     2  0000-0003-2738-7682 
primary 'von Soosten, L.' 3  0000-0001-7568-1013 
primary 'Dibenedetto, S.' 4  ?                   
primary 'Bartels, K.'     5  0000-0002-7980-1913 
primary 'Sung, S.'        6  0000-0001-5820-4696 
primary 'von Stetten, D.' 7  0000-0001-7906-9788 
primary 'Mehrabi, P.'     8  0000-0003-3211-6959 
primary 'Blatter, G.'     9  ?                   
primary 'Lu, G.'          10 ?                   
primary 'Bernhard, S.'    11 ?                   
primary 'Osbild, M.'      12 ?                   
primary 'Schulz, E.C.'    13 0000-0002-1685-8605 
# 
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     nat 'Proteinase K' 40364.902 1   3.4.21.64 ? ? ? 
2 non-polymer syn 'NITRATE ION'  62.005    1   ?         ? ? ? 
3 non-polymer syn 'CALCIUM ION'  40.078    1   ?         ? ? ? 
4 water       nat water          18.015    137 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Endopeptidase K,Tritirachium alkaline proteinase' 
# 
_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       
;MRLSVLLSLLPLALGAPAVEQRSEAAPLIEARGEMVANKYIVKFKEGSALSALDAAMEKISGKPDHVYKNVFSGFAATLD
ENMVRVLRAHPDVEYIEQDAVVTINAAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFEGRAQM
VKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNGSGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGG
GYSSSVNSAAARLQSSGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLDIFGPGTDILSTWIGG
STRSISGTSMATPHVAGLAAYLMTLGKTTAASACRYIADTANKGDLSNIPFGTVNLLAYNNYQA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRLSVLLSLLPLALGAPAVEQRSEAAPLIEARGEMVANKYIVKFKEGSALSALDAAMEKISGKPDHVYKNVFSGFAATLD
ENMVRVLRAHPDVEYIEQDAVVTINAAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFEGRAQM
VKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNGSGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGG
GYSSSVNSAAARLQSSGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLDIFGPGTDILSTWIGG
STRSISGTSMATPHVAGLAAYLMTLGKTTAASACRYIADTANKGDLSNIPFGTVNLLAYNNYQA
;
_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 'NITRATE ION' NO3 
3 'CALCIUM ION' CA  
4 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ARG n 
1 3   LEU n 
1 4   SER n 
1 5   VAL n 
1 6   LEU n 
1 7   LEU n 
1 8   SER n 
1 9   LEU n 
1 10  LEU n 
1 11  PRO n 
1 12  LEU n 
1 13  ALA n 
1 14  LEU n 
1 15  GLY n 
1 16  ALA n 
1 17  PRO n 
1 18  ALA n 
1 19  VAL n 
1 20  GLU n 
1 21  GLN n 
1 22  ARG n 
1 23  SER n 
1 24  GLU n 
1 25  ALA n 
1 26  ALA n 
1 27  PRO n 
1 28  LEU n 
1 29  ILE n 
1 30  GLU n 
1 31  ALA n 
1 32  ARG n 
1 33  GLY n 
1 34  GLU n 
1 35  MET n 
1 36  VAL n 
1 37  ALA n 
1 38  ASN n 
1 39  LYS n 
1 40  TYR n 
1 41  ILE n 
1 42  VAL n 
1 43  LYS n 
1 44  PHE n 
1 45  LYS n 
1 46  GLU n 
1 47  GLY n 
1 48  SER n 
1 49  ALA n 
1 50  LEU n 
1 51  SER n 
1 52  ALA n 
1 53  LEU n 
1 54  ASP n 
1 55  ALA n 
1 56  ALA n 
1 57  MET n 
1 58  GLU n 
1 59  LYS n 
1 60  ILE n 
1 61  SER n 
1 62  GLY n 
1 63  LYS n 
1 64  PRO n 
1 65  ASP n 
1 66  HIS n 
1 67  VAL n 
1 68  TYR n 
1 69  LYS n 
1 70  ASN n 
1 71  VAL n 
1 72  PHE n 
1 73  SER n 
1 74  GLY n 
1 75  PHE n 
1 76  ALA n 
1 77  ALA n 
1 78  THR n 
1 79  LEU n 
1 80  ASP n 
1 81  GLU n 
1 82  ASN n 
1 83  MET n 
1 84  VAL n 
1 85  ARG n 
1 86  VAL n 
1 87  LEU n 
1 88  ARG n 
1 89  ALA n 
1 90  HIS n 
1 91  PRO n 
1 92  ASP n 
1 93  VAL n 
1 94  GLU n 
1 95  TYR n 
1 96  ILE n 
1 97  GLU n 
1 98  GLN n 
1 99  ASP n 
1 100 ALA n 
1 101 VAL n 
1 102 VAL n 
1 103 THR n 
1 104 ILE n 
1 105 ASN n 
1 106 ALA n 
1 107 ALA n 
1 108 GLN n 
1 109 THR n 
1 110 ASN n 
1 111 ALA n 
1 112 PRO n 
1 113 TRP n 
1 114 GLY n 
1 115 LEU n 
1 116 ALA n 
1 117 ARG n 
1 118 ILE n 
1 119 SER n 
1 120 SER n 
1 121 THR n 
1 122 SER n 
1 123 PRO n 
1 124 GLY n 
1 125 THR n 
1 126 SER n 
1 127 THR n 
1 128 TYR n 
1 129 TYR n 
1 130 TYR n 
1 131 ASP n 
1 132 GLU n 
1 133 SER n 
1 134 ALA n 
1 135 GLY n 
1 136 GLN n 
1 137 GLY n 
1 138 SER n 
1 139 CYS n 
1 140 VAL n 
1 141 TYR n 
1 142 VAL n 
1 143 ILE n 
1 144 ASP n 
1 145 THR n 
1 146 GLY n 
1 147 ILE n 
1 148 GLU n 
1 149 ALA n 
1 150 SER n 
1 151 HIS n 
1 152 PRO n 
1 153 GLU n 
1 154 PHE n 
1 155 GLU n 
1 156 GLY n 
1 157 ARG n 
1 158 ALA n 
1 159 GLN n 
1 160 MET n 
1 161 VAL n 
1 162 LYS n 
1 163 THR n 
1 164 TYR n 
1 165 TYR n 
1 166 TYR n 
1 167 SER n 
1 168 SER n 
1 169 ARG n 
1 170 ASP n 
1 171 GLY n 
1 172 ASN n 
1 173 GLY n 
1 174 HIS n 
1 175 GLY n 
1 176 THR n 
1 177 HIS n 
1 178 CYS n 
1 179 ALA n 
1 180 GLY n 
1 181 THR n 
1 182 VAL n 
1 183 GLY n 
1 184 SER n 
1 185 ARG n 
1 186 THR n 
1 187 TYR n 
1 188 GLY n 
1 189 VAL n 
1 190 ALA n 
1 191 LYS n 
1 192 LYS n 
1 193 THR n 
1 194 GLN n 
1 195 LEU n 
1 196 PHE n 
1 197 GLY n 
1 198 VAL n 
1 199 LYS n 
1 200 VAL n 
1 201 LEU n 
1 202 ASP n 
1 203 ASP n 
1 204 ASN n 
1 205 GLY n 
1 206 SER n 
1 207 GLY n 
1 208 GLN n 
1 209 TYR n 
1 210 SER n 
1 211 THR n 
1 212 ILE n 
1 213 ILE n 
1 214 ALA n 
1 215 GLY n 
1 216 MET n 
1 217 ASP n 
1 218 PHE n 
1 219 VAL n 
1 220 ALA n 
1 221 SER n 
1 222 ASP n 
1 223 LYS n 
1 224 ASN n 
1 225 ASN n 
1 226 ARG n 
1 227 ASN n 
1 228 CYS n 
1 229 PRO n 
1 230 LYS n 
1 231 GLY n 
1 232 VAL n 
1 233 VAL n 
1 234 ALA n 
1 235 SER n 
1 236 LEU n 
1 237 SER n 
1 238 LEU n 
1 239 GLY n 
1 240 GLY n 
1 241 GLY n 
1 242 TYR n 
1 243 SER n 
1 244 SER n 
1 245 SER n 
1 246 VAL n 
1 247 ASN n 
1 248 SER n 
1 249 ALA n 
1 250 ALA n 
1 251 ALA n 
1 252 ARG n 
1 253 LEU n 
1 254 GLN n 
1 255 SER n 
1 256 SER n 
1 257 GLY n 
1 258 VAL n 
1 259 MET n 
1 260 VAL n 
1 261 ALA n 
1 262 VAL n 
1 263 ALA n 
1 264 ALA n 
1 265 GLY n 
1 266 ASN n 
1 267 ASN n 
1 268 ASN n 
1 269 ALA n 
1 270 ASP n 
1 271 ALA n 
1 272 ARG n 
1 273 ASN n 
1 274 TYR n 
1 275 SER n 
1 276 PRO n 
1 277 ALA n 
1 278 SER n 
1 279 GLU n 
1 280 PRO n 
1 281 SER n 
1 282 VAL n 
1 283 CYS n 
1 284 THR n 
1 285 VAL n 
1 286 GLY n 
1 287 ALA n 
1 288 SER n 
1 289 ASP n 
1 290 ARG n 
1 291 TYR n 
1 292 ASP n 
1 293 ARG n 
1 294 ARG n 
1 295 SER n 
1 296 SER n 
1 297 PHE n 
1 298 SER n 
1 299 ASN n 
1 300 TYR n 
1 301 GLY n 
1 302 SER n 
1 303 VAL n 
1 304 LEU n 
1 305 ASP n 
1 306 ILE n 
1 307 PHE n 
1 308 GLY n 
1 309 PRO n 
1 310 GLY n 
1 311 THR n 
1 312 ASP n 
1 313 ILE n 
1 314 LEU n 
1 315 SER n 
1 316 THR n 
1 317 TRP n 
1 318 ILE n 
1 319 GLY n 
1 320 GLY n 
1 321 SER n 
1 322 THR n 
1 323 ARG n 
1 324 SER n 
1 325 ILE n 
1 326 SER n 
1 327 GLY n 
1 328 THR n 
1 329 SER n 
1 330 MET n 
1 331 ALA n 
1 332 THR n 
1 333 PRO n 
1 334 HIS n 
1 335 VAL n 
1 336 ALA n 
1 337 GLY n 
1 338 LEU n 
1 339 ALA n 
1 340 ALA n 
1 341 TYR n 
1 342 LEU n 
1 343 MET n 
1 344 THR n 
1 345 LEU n 
1 346 GLY n 
1 347 LYS n 
1 348 THR n 
1 349 THR n 
1 350 ALA n 
1 351 ALA n 
1 352 SER n 
1 353 ALA n 
1 354 CYS n 
1 355 ARG n 
1 356 TYR n 
1 357 ILE n 
1 358 ALA n 
1 359 ASP n 
1 360 THR n 
1 361 ALA n 
1 362 ASN n 
1 363 LYS n 
1 364 GLY n 
1 365 ASP n 
1 366 LEU n 
1 367 SER n 
1 368 ASN n 
1 369 ILE n 
1 370 PRO n 
1 371 PHE n 
1 372 GLY n 
1 373 THR n 
1 374 VAL n 
1 375 ASN n 
1 376 LEU n 
1 377 LEU n 
1 378 ALA n 
1 379 TYR n 
1 380 ASN n 
1 381 ASN n 
1 382 TYR n 
1 383 GLN n 
1 384 ALA n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           384 
_entity_src_nat.common_name                ? 
_entity_src_nat.pdbx_organism_scientific   'Parengyodontium album' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      37998 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
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 
CA  non-polymer         . 'CALCIUM ION'   ? 'Ca 2'           40.078  
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
NO3 non-polymer         . 'NITRATE ION'   ? 'N O3 -1'        62.005  
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -104 ?   ?   ?   A . n 
A 1 2   ARG 2   -103 ?   ?   ?   A . n 
A 1 3   LEU 3   -102 ?   ?   ?   A . n 
A 1 4   SER 4   -101 ?   ?   ?   A . n 
A 1 5   VAL 5   -100 ?   ?   ?   A . n 
A 1 6   LEU 6   -99  ?   ?   ?   A . n 
A 1 7   LEU 7   -98  ?   ?   ?   A . n 
A 1 8   SER 8   -97  ?   ?   ?   A . n 
A 1 9   LEU 9   -96  ?   ?   ?   A . n 
A 1 10  LEU 10  -95  ?   ?   ?   A . n 
A 1 11  PRO 11  -94  ?   ?   ?   A . n 
A 1 12  LEU 12  -93  ?   ?   ?   A . n 
A 1 13  ALA 13  -92  ?   ?   ?   A . n 
A 1 14  LEU 14  -91  ?   ?   ?   A . n 
A 1 15  GLY 15  -90  ?   ?   ?   A . n 
A 1 16  ALA 16  -89  ?   ?   ?   A . n 
A 1 17  PRO 17  -88  ?   ?   ?   A . n 
A 1 18  ALA 18  -87  ?   ?   ?   A . n 
A 1 19  VAL 19  -86  ?   ?   ?   A . n 
A 1 20  GLU 20  -85  ?   ?   ?   A . n 
A 1 21  GLN 21  -84  ?   ?   ?   A . n 
A 1 22  ARG 22  -83  ?   ?   ?   A . n 
A 1 23  SER 23  -82  ?   ?   ?   A . n 
A 1 24  GLU 24  -81  ?   ?   ?   A . n 
A 1 25  ALA 25  -80  ?   ?   ?   A . n 
A 1 26  ALA 26  -79  ?   ?   ?   A . n 
A 1 27  PRO 27  -78  ?   ?   ?   A . n 
A 1 28  LEU 28  -77  ?   ?   ?   A . n 
A 1 29  ILE 29  -76  ?   ?   ?   A . n 
A 1 30  GLU 30  -75  ?   ?   ?   A . n 
A 1 31  ALA 31  -74  ?   ?   ?   A . n 
A 1 32  ARG 32  -73  ?   ?   ?   A . n 
A 1 33  GLY 33  -72  ?   ?   ?   A . n 
A 1 34  GLU 34  -71  ?   ?   ?   A . n 
A 1 35  MET 35  -70  ?   ?   ?   A . n 
A 1 36  VAL 36  -69  ?   ?   ?   A . n 
A 1 37  ALA 37  -68  ?   ?   ?   A . n 
A 1 38  ASN 38  -67  ?   ?   ?   A . n 
A 1 39  LYS 39  -66  ?   ?   ?   A . n 
A 1 40  TYR 40  -65  ?   ?   ?   A . n 
A 1 41  ILE 41  -64  ?   ?   ?   A . n 
A 1 42  VAL 42  -63  ?   ?   ?   A . n 
A 1 43  LYS 43  -62  ?   ?   ?   A . n 
A 1 44  PHE 44  -61  ?   ?   ?   A . n 
A 1 45  LYS 45  -60  ?   ?   ?   A . n 
A 1 46  GLU 46  -59  ?   ?   ?   A . n 
A 1 47  GLY 47  -58  ?   ?   ?   A . n 
A 1 48  SER 48  -57  ?   ?   ?   A . n 
A 1 49  ALA 49  -56  ?   ?   ?   A . n 
A 1 50  LEU 50  -55  ?   ?   ?   A . n 
A 1 51  SER 51  -54  ?   ?   ?   A . n 
A 1 52  ALA 52  -53  ?   ?   ?   A . n 
A 1 53  LEU 53  -52  ?   ?   ?   A . n 
A 1 54  ASP 54  -51  ?   ?   ?   A . n 
A 1 55  ALA 55  -50  ?   ?   ?   A . n 
A 1 56  ALA 56  -49  ?   ?   ?   A . n 
A 1 57  MET 57  -48  ?   ?   ?   A . n 
A 1 58  GLU 58  -47  ?   ?   ?   A . n 
A 1 59  LYS 59  -46  ?   ?   ?   A . n 
A 1 60  ILE 60  -45  ?   ?   ?   A . n 
A 1 61  SER 61  -44  ?   ?   ?   A . n 
A 1 62  GLY 62  -43  ?   ?   ?   A . n 
A 1 63  LYS 63  -42  ?   ?   ?   A . n 
A 1 64  PRO 64  -41  ?   ?   ?   A . n 
A 1 65  ASP 65  -40  ?   ?   ?   A . n 
A 1 66  HIS 66  -39  ?   ?   ?   A . n 
A 1 67  VAL 67  -38  ?   ?   ?   A . n 
A 1 68  TYR 68  -37  ?   ?   ?   A . n 
A 1 69  LYS 69  -36  ?   ?   ?   A . n 
A 1 70  ASN 70  -35  ?   ?   ?   A . n 
A 1 71  VAL 71  -34  ?   ?   ?   A . n 
A 1 72  PHE 72  -33  ?   ?   ?   A . n 
A 1 73  SER 73  -32  ?   ?   ?   A . n 
A 1 74  GLY 74  -31  ?   ?   ?   A . n 
A 1 75  PHE 75  -30  ?   ?   ?   A . n 
A 1 76  ALA 76  -29  ?   ?   ?   A . n 
A 1 77  ALA 77  -28  ?   ?   ?   A . n 
A 1 78  THR 78  -27  ?   ?   ?   A . n 
A 1 79  LEU 79  -26  ?   ?   ?   A . n 
A 1 80  ASP 80  -25  ?   ?   ?   A . n 
A 1 81  GLU 81  -24  ?   ?   ?   A . n 
A 1 82  ASN 82  -23  ?   ?   ?   A . n 
A 1 83  MET 83  -22  ?   ?   ?   A . n 
A 1 84  VAL 84  -21  ?   ?   ?   A . n 
A 1 85  ARG 85  -20  ?   ?   ?   A . n 
A 1 86  VAL 86  -19  ?   ?   ?   A . n 
A 1 87  LEU 87  -18  ?   ?   ?   A . n 
A 1 88  ARG 88  -17  ?   ?   ?   A . n 
A 1 89  ALA 89  -16  ?   ?   ?   A . n 
A 1 90  HIS 90  -15  ?   ?   ?   A . n 
A 1 91  PRO 91  -14  ?   ?   ?   A . n 
A 1 92  ASP 92  -13  ?   ?   ?   A . n 
A 1 93  VAL 93  -12  ?   ?   ?   A . n 
A 1 94  GLU 94  -11  ?   ?   ?   A . n 
A 1 95  TYR 95  -10  ?   ?   ?   A . n 
A 1 96  ILE 96  -9   ?   ?   ?   A . n 
A 1 97  GLU 97  -8   ?   ?   ?   A . n 
A 1 98  GLN 98  -7   ?   ?   ?   A . n 
A 1 99  ASP 99  -6   ?   ?   ?   A . n 
A 1 100 ALA 100 -5   ?   ?   ?   A . n 
A 1 101 VAL 101 -4   ?   ?   ?   A . n 
A 1 102 VAL 102 -3   ?   ?   ?   A . n 
A 1 103 THR 103 -2   ?   ?   ?   A . n 
A 1 104 ILE 104 -1   ?   ?   ?   A . n 
A 1 105 ASN 105 0    ?   ?   ?   A . n 
A 1 106 ALA 106 1    1   ALA ALA A . n 
A 1 107 ALA 107 2    2   ALA ALA A . n 
A 1 108 GLN 108 3    3   GLN GLN A . n 
A 1 109 THR 109 4    4   THR THR A . n 
A 1 110 ASN 110 5    5   ASN ASN A . n 
A 1 111 ALA 111 6    6   ALA ALA A . n 
A 1 112 PRO 112 7    7   PRO PRO A . n 
A 1 113 TRP 113 8    8   TRP TRP A . n 
A 1 114 GLY 114 9    9   GLY GLY A . n 
A 1 115 LEU 115 10   10  LEU LEU A . n 
A 1 116 ALA 116 11   11  ALA ALA A . n 
A 1 117 ARG 117 12   12  ARG ARG A . n 
A 1 118 ILE 118 13   13  ILE ILE A . n 
A 1 119 SER 119 14   14  SER SER A . n 
A 1 120 SER 120 15   15  SER SER A . n 
A 1 121 THR 121 16   16  THR THR A . n 
A 1 122 SER 122 17   17  SER SER A . n 
A 1 123 PRO 123 18   18  PRO PRO A . n 
A 1 124 GLY 124 19   19  GLY GLY A . n 
A 1 125 THR 125 20   20  THR THR A . n 
A 1 126 SER 126 21   21  SER SER A . n 
A 1 127 THR 127 22   22  THR THR A . n 
A 1 128 TYR 128 23   23  TYR TYR A . n 
A 1 129 TYR 129 24   24  TYR TYR A . n 
A 1 130 TYR 130 25   25  TYR TYR A . n 
A 1 131 ASP 131 26   26  ASP ASP A . n 
A 1 132 GLU 132 27   27  GLU GLU A . n 
A 1 133 SER 133 28   28  SER SER A . n 
A 1 134 ALA 134 29   29  ALA ALA A . n 
A 1 135 GLY 135 30   30  GLY GLY A . n 
A 1 136 GLN 136 31   31  GLN GLN A . n 
A 1 137 GLY 137 32   32  GLY GLY A . n 
A 1 138 SER 138 33   33  SER SER A . n 
A 1 139 CYS 139 34   34  CYS CYS A . n 
A 1 140 VAL 140 35   35  VAL VAL A . n 
A 1 141 TYR 141 36   36  TYR TYR A . n 
A 1 142 VAL 142 37   37  VAL VAL A . n 
A 1 143 ILE 143 38   38  ILE ILE A . n 
A 1 144 ASP 144 39   39  ASP ASP A . n 
A 1 145 THR 145 40   40  THR THR A . n 
A 1 146 GLY 146 41   41  GLY GLY A . n 
A 1 147 ILE 147 42   42  ILE ILE A . n 
A 1 148 GLU 148 43   43  GLU GLU A . n 
A 1 149 ALA 149 44   44  ALA ALA A . n 
A 1 150 SER 150 45   45  SER SER A . n 
A 1 151 HIS 151 46   46  HIS HIS A . n 
A 1 152 PRO 152 47   47  PRO PRO A . n 
A 1 153 GLU 153 48   48  GLU GLU A . n 
A 1 154 PHE 154 49   49  PHE PHE A . n 
A 1 155 GLU 155 50   50  GLU GLU A . n 
A 1 156 GLY 156 51   51  GLY GLY A . n 
A 1 157 ARG 157 52   52  ARG ARG A . n 
A 1 158 ALA 158 53   53  ALA ALA A . n 
A 1 159 GLN 159 54   54  GLN GLN A . n 
A 1 160 MET 160 55   55  MET MET A . n 
A 1 161 VAL 161 56   56  VAL VAL A . n 
A 1 162 LYS 162 57   57  LYS LYS A . n 
A 1 163 THR 163 58   58  THR THR A . n 
A 1 164 TYR 164 59   59  TYR TYR A . n 
A 1 165 TYR 165 60   60  TYR TYR A . n 
A 1 166 TYR 166 61   61  TYR TYR A . n 
A 1 167 SER 167 62   62  SER SER A . n 
A 1 168 SER 168 63   63  SER SER A . n 
A 1 169 ARG 169 64   64  ARG ARG A . n 
A 1 170 ASP 170 65   65  ASP ASP A . n 
A 1 171 GLY 171 66   66  GLY GLY A . n 
A 1 172 ASN 172 67   67  ASN ASN A . n 
A 1 173 GLY 173 68   68  GLY GLY A . n 
A 1 174 HIS 174 69   69  HIS HIS A . n 
A 1 175 GLY 175 70   70  GLY GLY A . n 
A 1 176 THR 176 71   71  THR THR A . n 
A 1 177 HIS 177 72   72  HIS HIS A . n 
A 1 178 CYS 178 73   73  CYS CYS A . n 
A 1 179 ALA 179 74   74  ALA ALA A . n 
A 1 180 GLY 180 75   75  GLY GLY A . n 
A 1 181 THR 181 76   76  THR THR A . n 
A 1 182 VAL 182 77   77  VAL VAL A . n 
A 1 183 GLY 183 78   78  GLY GLY A . n 
A 1 184 SER 184 79   79  SER SER A . n 
A 1 185 ARG 185 80   80  ARG ARG A . n 
A 1 186 THR 186 81   81  THR THR A . n 
A 1 187 TYR 187 82   82  TYR TYR A . n 
A 1 188 GLY 188 83   83  GLY GLY A . n 
A 1 189 VAL 189 84   84  VAL VAL A . n 
A 1 190 ALA 190 85   85  ALA ALA A . n 
A 1 191 LYS 191 86   86  LYS LYS A . n 
A 1 192 LYS 192 87   87  LYS LYS A . n 
A 1 193 THR 193 88   88  THR THR A . n 
A 1 194 GLN 194 89   89  GLN GLN A . n 
A 1 195 LEU 195 90   90  LEU LEU A . n 
A 1 196 PHE 196 91   91  PHE PHE A . n 
A 1 197 GLY 197 92   92  GLY GLY A . n 
A 1 198 VAL 198 93   93  VAL VAL A . n 
A 1 199 LYS 199 94   94  LYS LYS A . n 
A 1 200 VAL 200 95   95  VAL VAL A . n 
A 1 201 LEU 201 96   96  LEU LEU A . n 
A 1 202 ASP 202 97   97  ASP ASP A . n 
A 1 203 ASP 203 98   98  ASP ASP A . n 
A 1 204 ASN 204 99   99  ASN ASN A . n 
A 1 205 GLY 205 100  100 GLY GLY A . n 
A 1 206 SER 206 101  101 SER SER A . n 
A 1 207 GLY 207 102  102 GLY GLY A . n 
A 1 208 GLN 208 103  103 GLN GLN A . n 
A 1 209 TYR 209 104  104 TYR TYR A . n 
A 1 210 SER 210 105  105 SER SER A . n 
A 1 211 THR 211 106  106 THR THR A . n 
A 1 212 ILE 212 107  107 ILE ILE A . n 
A 1 213 ILE 213 108  108 ILE ILE A . n 
A 1 214 ALA 214 109  109 ALA ALA A . n 
A 1 215 GLY 215 110  110 GLY GLY A . n 
A 1 216 MET 216 111  111 MET MET A . n 
A 1 217 ASP 217 112  112 ASP ASP A . n 
A 1 218 PHE 218 113  113 PHE PHE A . n 
A 1 219 VAL 219 114  114 VAL VAL A . n 
A 1 220 ALA 220 115  115 ALA ALA A . n 
A 1 221 SER 221 116  116 SER SER A . n 
A 1 222 ASP 222 117  117 ASP ASP A . n 
A 1 223 LYS 223 118  118 LYS LYS A . n 
A 1 224 ASN 224 119  119 ASN ASN A . n 
A 1 225 ASN 225 120  120 ASN ASN A . n 
A 1 226 ARG 226 121  121 ARG ARG A . n 
A 1 227 ASN 227 122  122 ASN ASN A . n 
A 1 228 CYS 228 123  123 CYS CYS A . n 
A 1 229 PRO 229 124  124 PRO PRO A . n 
A 1 230 LYS 230 125  125 LYS LYS A . n 
A 1 231 GLY 231 126  126 GLY GLY A . n 
A 1 232 VAL 232 127  127 VAL VAL A . n 
A 1 233 VAL 233 128  128 VAL VAL A . n 
A 1 234 ALA 234 129  129 ALA ALA A . n 
A 1 235 SER 235 130  130 SER SER A . n 
A 1 236 LEU 236 131  131 LEU LEU A . n 
A 1 237 SER 237 132  132 SER SER A . n 
A 1 238 LEU 238 133  133 LEU LEU A . n 
A 1 239 GLY 239 134  134 GLY GLY A . n 
A 1 240 GLY 240 135  135 GLY GLY A . n 
A 1 241 GLY 241 136  136 GLY GLY A . n 
A 1 242 TYR 242 137  137 TYR TYR A . n 
A 1 243 SER 243 138  138 SER SER A . n 
A 1 244 SER 244 139  139 SER SER A . n 
A 1 245 SER 245 140  140 SER SER A . n 
A 1 246 VAL 246 141  141 VAL VAL A . n 
A 1 247 ASN 247 142  142 ASN ASN A . n 
A 1 248 SER 248 143  143 SER SER A . n 
A 1 249 ALA 249 144  144 ALA ALA A . n 
A 1 250 ALA 250 145  145 ALA ALA A . n 
A 1 251 ALA 251 146  146 ALA ALA A . n 
A 1 252 ARG 252 147  147 ARG ARG A . n 
A 1 253 LEU 253 148  148 LEU LEU A . n 
A 1 254 GLN 254 149  149 GLN GLN A . n 
A 1 255 SER 255 150  150 SER SER A . n 
A 1 256 SER 256 151  151 SER SER A . n 
A 1 257 GLY 257 152  152 GLY GLY A . n 
A 1 258 VAL 258 153  153 VAL VAL A . n 
A 1 259 MET 259 154  154 MET MET A . n 
A 1 260 VAL 260 155  155 VAL VAL A . n 
A 1 261 ALA 261 156  156 ALA ALA A . n 
A 1 262 VAL 262 157  157 VAL VAL A . n 
A 1 263 ALA 263 158  158 ALA ALA A . n 
A 1 264 ALA 264 159  159 ALA ALA A . n 
A 1 265 GLY 265 160  160 GLY GLY A . n 
A 1 266 ASN 266 161  161 ASN ASN A . n 
A 1 267 ASN 267 162  162 ASN ASN A . n 
A 1 268 ASN 268 163  163 ASN ASN A . n 
A 1 269 ALA 269 164  164 ALA ALA A . n 
A 1 270 ASP 270 165  165 ASP ASP A . n 
A 1 271 ALA 271 166  166 ALA ALA A . n 
A 1 272 ARG 272 167  167 ARG ARG A . n 
A 1 273 ASN 273 168  168 ASN ASN A . n 
A 1 274 TYR 274 169  169 TYR TYR A . n 
A 1 275 SER 275 170  170 SER SER A . n 
A 1 276 PRO 276 171  171 PRO PRO A . n 
A 1 277 ALA 277 172  172 ALA ALA A . n 
A 1 278 SER 278 173  173 SER SER A . n 
A 1 279 GLU 279 174  174 GLU GLU A . n 
A 1 280 PRO 280 175  175 PRO PRO A . n 
A 1 281 SER 281 176  176 SER SER A . n 
A 1 282 VAL 282 177  177 VAL VAL A . n 
A 1 283 CYS 283 178  178 CYS CYS A . n 
A 1 284 THR 284 179  179 THR THR A . n 
A 1 285 VAL 285 180  180 VAL VAL A . n 
A 1 286 GLY 286 181  181 GLY GLY A . n 
A 1 287 ALA 287 182  182 ALA ALA A . n 
A 1 288 SER 288 183  183 SER SER A . n 
A 1 289 ASP 289 184  184 ASP ASP A . n 
A 1 290 ARG 290 185  185 ARG ARG A . n 
A 1 291 TYR 291 186  186 TYR TYR A . n 
A 1 292 ASP 292 187  187 ASP ASP A . n 
A 1 293 ARG 293 188  188 ARG ARG A . n 
A 1 294 ARG 294 189  189 ARG ARG A . n 
A 1 295 SER 295 190  190 SER SER A . n 
A 1 296 SER 296 191  191 SER SER A . n 
A 1 297 PHE 297 192  192 PHE PHE A . n 
A 1 298 SER 298 193  193 SER SER A . n 
A 1 299 ASN 299 194  194 ASN ASN A . n 
A 1 300 TYR 300 195  195 TYR TYR A . n 
A 1 301 GLY 301 196  196 GLY GLY A . n 
A 1 302 SER 302 197  197 SER SER A . n 
A 1 303 VAL 303 198  198 VAL VAL A . n 
A 1 304 LEU 304 199  199 LEU LEU A . n 
A 1 305 ASP 305 200  200 ASP ASP A . n 
A 1 306 ILE 306 201  201 ILE ILE A . n 
A 1 307 PHE 307 202  202 PHE PHE A . n 
A 1 308 GLY 308 203  203 GLY GLY A . n 
A 1 309 PRO 309 204  204 PRO PRO A . n 
A 1 310 GLY 310 205  205 GLY GLY A . n 
A 1 311 THR 311 206  206 THR THR A . n 
A 1 312 ASP 312 207  207 ASP ASP A . n 
A 1 313 ILE 313 208  208 ILE ILE A . n 
A 1 314 LEU 314 209  209 LEU LEU A . n 
A 1 315 SER 315 210  210 SER SER A . n 
A 1 316 THR 316 211  211 THR THR A . n 
A 1 317 TRP 317 212  212 TRP TRP A . n 
A 1 318 ILE 318 213  213 ILE ILE A . n 
A 1 319 GLY 319 214  214 GLY GLY A . n 
A 1 320 GLY 320 215  215 GLY GLY A . n 
A 1 321 SER 321 216  216 SER SER A . n 
A 1 322 THR 322 217  217 THR THR A . n 
A 1 323 ARG 323 218  218 ARG ARG A . n 
A 1 324 SER 324 219  219 SER SER A . n 
A 1 325 ILE 325 220  220 ILE ILE A . n 
A 1 326 SER 326 221  221 SER SER A . n 
A 1 327 GLY 327 222  222 GLY GLY A . n 
A 1 328 THR 328 223  223 THR THR A . n 
A 1 329 SER 329 224  224 SER SER A . n 
A 1 330 MET 330 225  225 MET MET A . n 
A 1 331 ALA 331 226  226 ALA ALA A . n 
A 1 332 THR 332 227  227 THR THR A . n 
A 1 333 PRO 333 228  228 PRO PRO A . n 
A 1 334 HIS 334 229  229 HIS HIS A . n 
A 1 335 VAL 335 230  230 VAL VAL A . n 
A 1 336 ALA 336 231  231 ALA ALA A . n 
A 1 337 GLY 337 232  232 GLY GLY A . n 
A 1 338 LEU 338 233  233 LEU LEU A . n 
A 1 339 ALA 339 234  234 ALA ALA A . n 
A 1 340 ALA 340 235  235 ALA ALA A . n 
A 1 341 TYR 341 236  236 TYR TYR A . n 
A 1 342 LEU 342 237  237 LEU LEU A . n 
A 1 343 MET 343 238  238 MET MET A . n 
A 1 344 THR 344 239  239 THR THR A . n 
A 1 345 LEU 345 240  240 LEU LEU A . n 
A 1 346 GLY 346 241  241 GLY GLY A . n 
A 1 347 LYS 347 242  242 LYS LYS A . n 
A 1 348 THR 348 243  243 THR THR A . n 
A 1 349 THR 349 244  244 THR THR A . n 
A 1 350 ALA 350 245  245 ALA ALA A . n 
A 1 351 ALA 351 246  246 ALA ALA A . n 
A 1 352 SER 352 247  247 SER SER A . n 
A 1 353 ALA 353 248  248 ALA ALA A . n 
A 1 354 CYS 354 249  249 CYS CYS A . n 
A 1 355 ARG 355 250  250 ARG ARG A . n 
A 1 356 TYR 356 251  251 TYR TYR A . n 
A 1 357 ILE 357 252  252 ILE ILE A . n 
A 1 358 ALA 358 253  253 ALA ALA A . n 
A 1 359 ASP 359 254  254 ASP ASP A . n 
A 1 360 THR 360 255  255 THR THR A . n 
A 1 361 ALA 361 256  256 ALA ALA A . n 
A 1 362 ASN 362 257  257 ASN ASN A . n 
A 1 363 LYS 363 258  258 LYS LYS A . n 
A 1 364 GLY 364 259  259 GLY GLY A . n 
A 1 365 ASP 365 260  260 ASP ASP A . n 
A 1 366 LEU 366 261  261 LEU LEU A . n 
A 1 367 SER 367 262  262 SER SER A . n 
A 1 368 ASN 368 263  263 ASN ASN A . n 
A 1 369 ILE 369 264  264 ILE ILE A . n 
A 1 370 PRO 370 265  265 PRO PRO A . n 
A 1 371 PHE 371 266  266 PHE PHE A . n 
A 1 372 GLY 372 267  267 GLY GLY A . n 
A 1 373 THR 373 268  268 THR THR A . n 
A 1 374 VAL 374 269  269 VAL VAL A . n 
A 1 375 ASN 375 270  270 ASN ASN A . n 
A 1 376 LEU 376 271  271 LEU LEU A . n 
A 1 377 LEU 377 272  272 LEU LEU A . n 
A 1 378 ALA 378 273  273 ALA ALA A . n 
A 1 379 TYR 379 274  274 TYR TYR A . n 
A 1 380 ASN 380 275  275 ASN ASN A . n 
A 1 381 ASN 381 276  276 ASN ASN A . n 
A 1 382 TYR 382 277  277 TYR TYR A . n 
A 1 383 GLN 383 278  278 GLN GLN A . n 
A 1 384 ALA 384 279  279 ALA ALA A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NO3 1   301 301 NO3 NO3 A . 
C 3 CA  1   302 1   CA  CA  A . 
D 4 HOH 1   401 77  HOH HOH A . 
D 4 HOH 2   402 107 HOH HOH A . 
D 4 HOH 3   403 78  HOH HOH A . 
D 4 HOH 4   404 50  HOH HOH A . 
D 4 HOH 5   405 68  HOH HOH A . 
D 4 HOH 6   406 91  HOH HOH A . 
D 4 HOH 7   407 1   HOH HOH A . 
D 4 HOH 8   408 138 HOH HOH A . 
D 4 HOH 9   409 97  HOH HOH A . 
D 4 HOH 10  410 92  HOH HOH A . 
D 4 HOH 11  411 57  HOH HOH A . 
D 4 HOH 12  412 89  HOH HOH A . 
D 4 HOH 13  413 81  HOH HOH A . 
D 4 HOH 14  414 44  HOH HOH A . 
D 4 HOH 15  415 47  HOH HOH A . 
D 4 HOH 16  416 9   HOH HOH A . 
D 4 HOH 17  417 122 HOH HOH A . 
D 4 HOH 18  418 51  HOH HOH A . 
D 4 HOH 19  419 56  HOH HOH A . 
D 4 HOH 20  420 132 HOH HOH A . 
D 4 HOH 21  421 21  HOH HOH A . 
D 4 HOH 22  422 37  HOH HOH A . 
D 4 HOH 23  423 60  HOH HOH A . 
D 4 HOH 24  424 35  HOH HOH A . 
D 4 HOH 25  425 110 HOH HOH A . 
D 4 HOH 26  426 2   HOH HOH A . 
D 4 HOH 27  427 42  HOH HOH A . 
D 4 HOH 28  428 12  HOH HOH A . 
D 4 HOH 29  429 53  HOH HOH A . 
D 4 HOH 30  430 27  HOH HOH A . 
D 4 HOH 31  431 61  HOH HOH A . 
D 4 HOH 32  432 36  HOH HOH A . 
D 4 HOH 33  433 79  HOH HOH A . 
D 4 HOH 34  434 95  HOH HOH A . 
D 4 HOH 35  435 101 HOH HOH A . 
D 4 HOH 36  436 100 HOH HOH A . 
D 4 HOH 37  437 85  HOH HOH A . 
D 4 HOH 38  438 4   HOH HOH A . 
D 4 HOH 39  439 14  HOH HOH A . 
D 4 HOH 40  440 108 HOH HOH A . 
D 4 HOH 41  441 17  HOH HOH A . 
D 4 HOH 42  442 118 HOH HOH A . 
D 4 HOH 43  443 5   HOH HOH A . 
D 4 HOH 44  444 75  HOH HOH A . 
D 4 HOH 45  445 43  HOH HOH A . 
D 4 HOH 46  446 6   HOH HOH A . 
D 4 HOH 47  447 29  HOH HOH A . 
D 4 HOH 48  448 124 HOH HOH A . 
D 4 HOH 49  449 133 HOH HOH A . 
D 4 HOH 50  450 66  HOH HOH A . 
D 4 HOH 51  451 48  HOH HOH A . 
D 4 HOH 52  452 25  HOH HOH A . 
D 4 HOH 53  453 99  HOH HOH A . 
D 4 HOH 54  454 3   HOH HOH A . 
D 4 HOH 55  455 94  HOH HOH A . 
D 4 HOH 56  456 23  HOH HOH A . 
D 4 HOH 57  457 113 HOH HOH A . 
D 4 HOH 58  458 86  HOH HOH A . 
D 4 HOH 59  459 125 HOH HOH A . 
D 4 HOH 60  460 38  HOH HOH A . 
D 4 HOH 61  461 19  HOH HOH A . 
D 4 HOH 62  462 55  HOH HOH A . 
D 4 HOH 63  463 114 HOH HOH A . 
D 4 HOH 64  464 28  HOH HOH A . 
D 4 HOH 65  465 65  HOH HOH A . 
D 4 HOH 66  466 7   HOH HOH A . 
D 4 HOH 67  467 41  HOH HOH A . 
D 4 HOH 68  468 45  HOH HOH A . 
D 4 HOH 69  469 11  HOH HOH A . 
D 4 HOH 70  470 16  HOH HOH A . 
D 4 HOH 71  471 26  HOH HOH A . 
D 4 HOH 72  472 136 HOH HOH A . 
D 4 HOH 73  473 33  HOH HOH A . 
D 4 HOH 74  474 15  HOH HOH A . 
D 4 HOH 75  475 87  HOH HOH A . 
D 4 HOH 76  476 34  HOH HOH A . 
D 4 HOH 77  477 20  HOH HOH A . 
D 4 HOH 78  478 32  HOH HOH A . 
D 4 HOH 79  479 88  HOH HOH A . 
D 4 HOH 80  480 134 HOH HOH A . 
D 4 HOH 81  481 84  HOH HOH A . 
D 4 HOH 82  482 117 HOH HOH A . 
D 4 HOH 83  483 62  HOH HOH A . 
D 4 HOH 84  484 116 HOH HOH A . 
D 4 HOH 85  485 137 HOH HOH A . 
D 4 HOH 86  486 46  HOH HOH A . 
D 4 HOH 87  487 119 HOH HOH A . 
D 4 HOH 88  488 109 HOH HOH A . 
D 4 HOH 89  489 123 HOH HOH A . 
D 4 HOH 90  490 30  HOH HOH A . 
D 4 HOH 91  491 73  HOH HOH A . 
D 4 HOH 92  492 59  HOH HOH A . 
D 4 HOH 93  493 76  HOH HOH A . 
D 4 HOH 94  494 128 HOH HOH A . 
D 4 HOH 95  495 18  HOH HOH A . 
D 4 HOH 96  496 71  HOH HOH A . 
D 4 HOH 97  497 70  HOH HOH A . 
D 4 HOH 98  498 98  HOH HOH A . 
D 4 HOH 99  499 129 HOH HOH A . 
D 4 HOH 100 500 69  HOH HOH A . 
D 4 HOH 101 501 8   HOH HOH A . 
D 4 HOH 102 502 63  HOH HOH A . 
D 4 HOH 103 503 115 HOH HOH A . 
D 4 HOH 104 504 10  HOH HOH A . 
D 4 HOH 105 505 80  HOH HOH A . 
D 4 HOH 106 506 104 HOH HOH A . 
D 4 HOH 107 507 22  HOH HOH A . 
D 4 HOH 108 508 130 HOH HOH A . 
D 4 HOH 109 509 83  HOH HOH A . 
D 4 HOH 110 510 49  HOH HOH A . 
D 4 HOH 111 511 13  HOH HOH A . 
D 4 HOH 112 512 111 HOH HOH A . 
D 4 HOH 113 513 58  HOH HOH A . 
D 4 HOH 114 514 82  HOH HOH A . 
D 4 HOH 115 515 93  HOH HOH A . 
D 4 HOH 116 516 39  HOH HOH A . 
D 4 HOH 117 517 24  HOH HOH A . 
D 4 HOH 118 518 31  HOH HOH A . 
D 4 HOH 119 519 106 HOH HOH A . 
D 4 HOH 120 520 72  HOH HOH A . 
D 4 HOH 121 521 112 HOH HOH A . 
D 4 HOH 122 522 54  HOH HOH A . 
D 4 HOH 123 523 52  HOH HOH A . 
D 4 HOH 124 524 105 HOH HOH A . 
D 4 HOH 125 525 127 HOH HOH A . 
D 4 HOH 126 526 139 HOH HOH A . 
D 4 HOH 127 527 102 HOH HOH A . 
D 4 HOH 128 528 40  HOH HOH A . 
D 4 HOH 129 529 131 HOH HOH A . 
D 4 HOH 130 530 135 HOH HOH A . 
D 4 HOH 131 531 96  HOH HOH A . 
D 4 HOH 132 532 90  HOH HOH A . 
D 4 HOH 133 533 67  HOH HOH A . 
D 4 HOH 134 534 121 HOH HOH A . 
D 4 HOH 135 535 120 HOH HOH A . 
D 4 HOH 136 536 126 HOH HOH A . 
D 4 HOH 137 537 64  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   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? 0.10.2      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? 0.10.2      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 2.8.3       4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RSF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     68.500 
_cell.length_a_esd                 ? 
_cell.length_b                     68.500 
_cell.length_b_esd                 ? 
_cell.length_c                     108.750 
_cell.length_c_esd                 ? 
_cell.volume                       510282.188 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8RSF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            'P 4nw 2abw' 
_symmetry.space_group_name_H-M             'P 43 21 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                   8RSF 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_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          'BATCH MODE' 
_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    
;Microcrystals were obtained by mixing proteinase K solution (60mg/ml) with precipitant solution 1M NaNO3, 0.1M sodium 
citrate pH 6.5, in a 5:1 ratio and left overnight at room temperature.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-04 
_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   0.976 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          10.37 
_reflns.entry_id                                       8RSF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.66 
_reflns.d_resolution_low                               57.96 
_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                                     32794 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                889.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.29 
_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                                   0.998 
_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                                    1.66 
_reflns_shell.d_res_low                                     1.73 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           11.34 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2605 
_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                                  0.993 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  0.0946 
_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                               12.37 
_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                                 8RSF 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.66 
_refine.ls_d_res_low                             57.96 
_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                     31322 
_refine.ls_number_reflns_R_free                  1552 
_refine.ls_number_reflns_R_work                  29770 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1342 
_refine.ls_R_factor_R_free                       0.1579 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1330 
_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                          1.36 
_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                 12.7743 
_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                            0.1106 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.66 
_refine_hist.d_res_low                        57.96 
_refine_hist.number_atoms_solvent             137 
_refine_hist.number_atoms_total               2174 
_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        2032 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         5 
_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' ? 0.0116 ? 2251 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0985 ? 3087 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0780 ? 337  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0112 ? 420  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 5.7968 ? 350  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.66 1.71  . . 149 2655 99.96  . . . . 0.1315 . . . . . . . . . . . 0.1652 
'X-RAY DIFFRACTION' 1.71 1.77  . . 120 2656 99.93  . . . . 0.1128 . . . . . . . . . . . 0.1476 
'X-RAY DIFFRACTION' 1.77 1.85  . . 134 2680 99.96  . . . . 0.1198 . . . . . . . . . . . 0.1480 
'X-RAY DIFFRACTION' 1.85 1.93  . . 133 2639 100.00 . . . . 0.1260 . . . . . . . . . . . 0.1606 
'X-RAY DIFFRACTION' 1.93 2.03  . . 148 2672 99.93  . . . . 0.1303 . . . . . . . . . . . 0.1627 
'X-RAY DIFFRACTION' 2.03 2.16  . . 158 2662 99.96  . . . . 0.1295 . . . . . . . . . . . 0.1451 
'X-RAY DIFFRACTION' 2.16 2.33  . . 136 2687 100.00 . . . . 0.1351 . . . . . . . . . . . 0.1796 
'X-RAY DIFFRACTION' 2.33 2.56  . . 138 2711 100.00 . . . . 0.1528 . . . . . . . . . . . 0.1726 
'X-RAY DIFFRACTION' 2.56 2.93  . . 143 2726 100.00 . . . . 0.1501 . . . . . . . . . . . 0.1871 
'X-RAY DIFFRACTION' 2.93 3.69  . . 132 2771 100.00 . . . . 0.1372 . . . . . . . . . . . 0.1422 
'X-RAY DIFFRACTION' 3.69 57.96 . . 161 2911 99.84  . . . . 0.1217 . . . . . . . . . . . 0.1420 
# 
_struct.entry_id                     8RSF 
_struct.title                        'Proteinase K measured via serial crystallography from a kapton HARE-chip (50 micron)' 
_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        8RSF 
_struct_keywords.text            'Proteianse K, Serine Protease, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PRTK_PARAQ 
_struct_ref.pdbx_db_accession          P06873 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MRLSVLLSLLPLALGAPAVEQRSEAAPLIEARGEMVANKYIVKFKEGSALSALDAAMEKISGKPDHVYKNVFSGFAATLD
ENMVRVLRAHPDVEYIEQDAVVTINAAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFEGRAQM
VKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNGSGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGG
GYSSSVNSAAARLQSSGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLDIFGPGTSILSTWIGG
STRSISGTSMATPHVAGLAAYLMTLGKTTAASACRYIADTANKGDLSNIPFGTVNLLAYNNYQA
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8RSF 
_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                 384 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P06873 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  384 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       -104 
_struct_ref_seq.pdbx_auth_seq_align_end       279 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             8RSF 
_struct_ref_seq_dif.mon_id                       ASP 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      312 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P06873 
_struct_ref_seq_dif.db_mon_id                    SER 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          312 
_struct_ref_seq_dif.details                      conflict 
_struct_ref_seq_dif.pdbx_auth_seq_num            207 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 280   ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  10450 ? 
# 
_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 
# 
_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 PRO A 112 ? SER A 119 ? PRO A 7   SER A 14  1 ? 8  
HELX_P HELX_P2 AA2 HIS A 151 ? GLU A 155 ? HIS A 46  GLU A 50  5 ? 5  
HELX_P HELX_P3 AA3 GLY A 173 ? SER A 184 ? GLY A 68  SER A 79  1 ? 12 
HELX_P HELX_P4 AA4 GLN A 208 ? LYS A 223 ? GLN A 103 LYS A 118 1 ? 16 
HELX_P HELX_P5 AA5 ASN A 224 ? ARG A 226 ? ASN A 119 ARG A 121 5 ? 3  
HELX_P HELX_P6 AA6 SER A 243 ? SER A 256 ? SER A 138 SER A 151 1 ? 14 
HELX_P HELX_P7 AA7 ASP A 270 ? ARG A 272 ? ASP A 165 ARG A 167 5 ? 3  
HELX_P HELX_P8 AA8 GLY A 327 ? LEU A 345 ? GLY A 222 LEU A 240 1 ? 19 
HELX_P HELX_P9 AA9 SER A 352 ? THR A 360 ? SER A 247 THR A 255 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 139 SG  ? ? ? 1_555 A CYS 228 SG ? ? A CYS 34  A CYS 123 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
disulf2 disulf ? ? A CYS 283 SG  ? ? ? 1_555 A CYS 354 SG ? ? A CYS 178 A CYS 249 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc1 metalc ? ? A PRO 280 O   ? ? ? 1_555 C CA  .   CA ? ? A PRO 175 A CA  302 1_555 ? ? ? ? ? ? ? 2.398 ? ? 
metalc2 metalc ? ? A VAL 282 O   ? ? ? 1_555 C CA  .   CA ? ? A VAL 177 A CA  302 1_555 ? ? ? ? ? ? ? 2.437 ? ? 
metalc3 metalc ? ? A ASP 305 OD1 ? ? ? 1_555 C CA  .   CA ? ? A ASP 200 A CA  302 1_555 ? ? ? ? ? ? ? 2.739 ? ? 
metalc4 metalc ? ? A ASP 305 OD2 ? ? ? 1_555 C CA  .   CA ? ? A ASP 200 A CA  302 1_555 ? ? ? ? ? ? ? 2.436 ? ? 
metalc5 metalc ? ? C CA  .   CA  ? ? ? 1_555 D HOH .   O  ? ? A CA  302 A HOH 438 1_555 ? ? ? ? ? ? ? 2.470 ? ? 
metalc6 metalc ? ? C CA  .   CA  ? ? ? 1_555 D HOH .   O  ? ? A CA  302 A HOH 439 1_555 ? ? ? ? ? ? ? 2.497 ? ? 
metalc7 metalc ? ? C CA  .   CA  ? ? ? 1_555 D HOH .   O  ? ? A CA  302 A HOH 474 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc8 metalc ? ? C CA  .   CA  ? ? ? 1_555 D HOH .   O  ? ? A CA  302 A HOH 511 1_555 ? ? ? ? ? ? ? 2.561 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A PRO 280 ? A PRO 175 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? A VAL 282 ? A VAL 177 ? 1_555 86.2  ? 
2  O   ? A PRO 280 ? A PRO 175 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD1 ? A ASP 305 ? A ASP 200 ? 1_555 151.6 ? 
3  O   ? A VAL 282 ? A VAL 177 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD1 ? A ASP 305 ? A ASP 200 ? 1_555 114.6 ? 
4  O   ? A PRO 280 ? A PRO 175 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD2 ? A ASP 305 ? A ASP 200 ? 1_555 158.8 ? 
5  O   ? A VAL 282 ? A VAL 177 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD2 ? A ASP 305 ? A ASP 200 ? 1_555 81.2  ? 
6  OD1 ? A ASP 305 ? A ASP 200 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD2 ? A ASP 305 ? A ASP 200 ? 1_555 49.3  ? 
7  O   ? A PRO 280 ? A PRO 175 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 438 ? 1_555 80.3  ? 
8  O   ? A VAL 282 ? A VAL 177 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 438 ? 1_555 74.0  ? 
9  OD1 ? A ASP 305 ? A ASP 200 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 438 ? 1_555 122.6 ? 
10 OD2 ? A ASP 305 ? A ASP 200 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 438 ? 1_555 79.9  ? 
11 O   ? A PRO 280 ? A PRO 175 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 439 ? 1_555 95.0  ? 
12 O   ? A VAL 282 ? A VAL 177 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 439 ? 1_555 146.4 ? 
13 OD1 ? A ASP 305 ? A ASP 200 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 439 ? 1_555 78.4  ? 
14 OD2 ? A ASP 305 ? A ASP 200 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 439 ? 1_555 86.4  ? 
15 O   ? D HOH .   ? A HOH 438 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 439 ? 1_555 73.1  ? 
16 O   ? A PRO 280 ? A PRO 175 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 474 ? 1_555 90.7  ? 
17 O   ? A VAL 282 ? A VAL 177 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 474 ? 1_555 72.3  ? 
18 OD1 ? A ASP 305 ? A ASP 200 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 474 ? 1_555 78.6  ? 
19 OD2 ? A ASP 305 ? A ASP 200 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 474 ? 1_555 101.5 ? 
20 O   ? D HOH .   ? A HOH 438 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 474 ? 1_555 145.6 ? 
21 O   ? D HOH .   ? A HOH 439 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 474 ? 1_555 141.1 ? 
22 O   ? A PRO 280 ? A PRO 175 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 511 ? 1_555 74.5  ? 
23 O   ? A VAL 282 ? A VAL 177 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 511 ? 1_555 138.5 ? 
24 OD1 ? A ASP 305 ? A ASP 200 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 511 ? 1_555 77.2  ? 
25 OD2 ? A ASP 305 ? A ASP 200 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 511 ? 1_555 125.7 ? 
26 O   ? D HOH .   ? A HOH 438 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 511 ? 1_555 135.3 ? 
27 O   ? D HOH .   ? A HOH 439 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 511 ? 1_555 73.0  ? 
28 O   ? D HOH .   ? A HOH 474 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? D HOH .   ? A HOH 511 ? 1_555 71.6  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 139 ? CYS A 228 ? CYS A 34  ? 1_555 CYS A 123 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 283 ? CYS A 354 ? CYS A 178 ? 1_555 CYS A 249 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           275 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            170 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    276 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     171 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.09 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 107 ? GLN A 108 ? ALA A 2   GLN A 3   
AA1 2 TYR A 128 ? TYR A 129 ? TYR A 23  TYR A 24  
AA2 1 ALA A 158 ? THR A 163 ? ALA A 53  THR A 58  
AA2 2 GLN A 194 ? LYS A 199 ? GLN A 89  LYS A 94  
AA2 3 SER A 138 ? ASP A 144 ? SER A 33  ASP A 39  
AA2 4 GLY A 231 ? LEU A 236 ? GLY A 126 LEU A 131 
AA2 5 MET A 259 ? ALA A 263 ? MET A 154 ALA A 158 
AA2 6 CYS A 283 ? SER A 288 ? CYS A 178 SER A 183 
AA2 7 ILE A 306 ? PRO A 309 ? ILE A 201 PRO A 204 
AA3 1 GLY A 240 ? GLY A 241 ? GLY A 135 GLY A 136 
AA3 2 TYR A 274 ? SER A 275 ? TYR A 169 SER A 170 
AA4 1 ILE A 313 ? TRP A 317 ? ILE A 208 TRP A 212 
AA4 2 SER A 321 ? ILE A 325 ? SER A 216 ILE A 220 
AA5 1 ASN A 362 ? LYS A 363 ? ASN A 257 LYS A 258 
AA5 2 LEU A 376 ? LEU A 377 ? LEU A 271 LEU A 272 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 108 ? N GLN A 3   O TYR A 128 ? O TYR A 23  
AA2 1 2 N GLN A 159 ? N GLN A 54  O GLY A 197 ? O GLY A 92  
AA2 2 3 O PHE A 196 ? O PHE A 91  N VAL A 142 ? N VAL A 37  
AA2 3 4 N TYR A 141 ? N TYR A 36  O VAL A 233 ? O VAL A 128 
AA2 4 5 N ALA A 234 ? N ALA A 129 O MET A 259 ? O MET A 154 
AA2 5 6 N VAL A 262 ? N VAL A 157 O CYS A 283 ? O CYS A 178 
AA2 6 7 N GLY A 286 ? N GLY A 181 O ILE A 306 ? O ILE A 201 
AA3 1 2 N GLY A 240 ? N GLY A 135 O SER A 275 ? O SER A 170 
AA4 1 2 N ILE A 313 ? N ILE A 208 O ILE A 325 ? O ILE A 220 
AA5 1 2 N ASN A 362 ? N ASN A 257 O LEU A 377 ? O LEU A 272 
# 
_pdbx_entry_details.entry_id                   8RSF 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ASP A 39  ? ? -167.68 -146.99 
2 1 TYR A 60  ? ? -128.08 -168.53 
3 1 ASP A 207 ? B 62.13   61.53   
4 1 SER A 216 ? A -109.89 -169.77 
5 1 ASN A 270 ? ? -113.25 78.82   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     452 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+3/4  
3 y+1/2,-x+1/2,z+1/4  
4 x+1/2,-y+1/2,-z+1/4 
5 -x+1/2,y+1/2,-z+3/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-z+1/2        
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         50.9340577314 
_pdbx_refine_tls.origin_y         46.8708273934 
_pdbx_refine_tls.origin_z         27.569437944 
_pdbx_refine_tls.T[1][1]          0.0597950533278 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.00146226594054 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0069990483633 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.042555364575 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.000251770173413 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0503795581491 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.778932882329 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.174555618262 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.00472429735265 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.87681878493 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0550529262532 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.524742812856 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.00463650195456 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0250414575749 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.00110108542503 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0396978824633 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0023861271351 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0532090562032 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0182691140077 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.00953878603178 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.00294236264812 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   D 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    C 
_pdbx_refine_tls_group.end_auth_seq_id     139 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       537 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.56 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -104 ? A MET 1   
2   1 Y 1 A ARG -103 ? A ARG 2   
3   1 Y 1 A LEU -102 ? A LEU 3   
4   1 Y 1 A SER -101 ? A SER 4   
5   1 Y 1 A VAL -100 ? A VAL 5   
6   1 Y 1 A LEU -99  ? A LEU 6   
7   1 Y 1 A LEU -98  ? A LEU 7   
8   1 Y 1 A SER -97  ? A SER 8   
9   1 Y 1 A LEU -96  ? A LEU 9   
10  1 Y 1 A LEU -95  ? A LEU 10  
11  1 Y 1 A PRO -94  ? A PRO 11  
12  1 Y 1 A LEU -93  ? A LEU 12  
13  1 Y 1 A ALA -92  ? A ALA 13  
14  1 Y 1 A LEU -91  ? A LEU 14  
15  1 Y 1 A GLY -90  ? A GLY 15  
16  1 Y 1 A ALA -89  ? A ALA 16  
17  1 Y 1 A PRO -88  ? A PRO 17  
18  1 Y 1 A ALA -87  ? A ALA 18  
19  1 Y 1 A VAL -86  ? A VAL 19  
20  1 Y 1 A GLU -85  ? A GLU 20  
21  1 Y 1 A GLN -84  ? A GLN 21  
22  1 Y 1 A ARG -83  ? A ARG 22  
23  1 Y 1 A SER -82  ? A SER 23  
24  1 Y 1 A GLU -81  ? A GLU 24  
25  1 Y 1 A ALA -80  ? A ALA 25  
26  1 Y 1 A ALA -79  ? A ALA 26  
27  1 Y 1 A PRO -78  ? A PRO 27  
28  1 Y 1 A LEU -77  ? A LEU 28  
29  1 Y 1 A ILE -76  ? A ILE 29  
30  1 Y 1 A GLU -75  ? A GLU 30  
31  1 Y 1 A ALA -74  ? A ALA 31  
32  1 Y 1 A ARG -73  ? A ARG 32  
33  1 Y 1 A GLY -72  ? A GLY 33  
34  1 Y 1 A GLU -71  ? A GLU 34  
35  1 Y 1 A MET -70  ? A MET 35  
36  1 Y 1 A VAL -69  ? A VAL 36  
37  1 Y 1 A ALA -68  ? A ALA 37  
38  1 Y 1 A ASN -67  ? A ASN 38  
39  1 Y 1 A LYS -66  ? A LYS 39  
40  1 Y 1 A TYR -65  ? A TYR 40  
41  1 Y 1 A ILE -64  ? A ILE 41  
42  1 Y 1 A VAL -63  ? A VAL 42  
43  1 Y 1 A LYS -62  ? A LYS 43  
44  1 Y 1 A PHE -61  ? A PHE 44  
45  1 Y 1 A LYS -60  ? A LYS 45  
46  1 Y 1 A GLU -59  ? A GLU 46  
47  1 Y 1 A GLY -58  ? A GLY 47  
48  1 Y 1 A SER -57  ? A SER 48  
49  1 Y 1 A ALA -56  ? A ALA 49  
50  1 Y 1 A LEU -55  ? A LEU 50  
51  1 Y 1 A SER -54  ? A SER 51  
52  1 Y 1 A ALA -53  ? A ALA 52  
53  1 Y 1 A LEU -52  ? A LEU 53  
54  1 Y 1 A ASP -51  ? A ASP 54  
55  1 Y 1 A ALA -50  ? A ALA 55  
56  1 Y 1 A ALA -49  ? A ALA 56  
57  1 Y 1 A MET -48  ? A MET 57  
58  1 Y 1 A GLU -47  ? A GLU 58  
59  1 Y 1 A LYS -46  ? A LYS 59  
60  1 Y 1 A ILE -45  ? A ILE 60  
61  1 Y 1 A SER -44  ? A SER 61  
62  1 Y 1 A GLY -43  ? A GLY 62  
63  1 Y 1 A LYS -42  ? A LYS 63  
64  1 Y 1 A PRO -41  ? A PRO 64  
65  1 Y 1 A ASP -40  ? A ASP 65  
66  1 Y 1 A HIS -39  ? A HIS 66  
67  1 Y 1 A VAL -38  ? A VAL 67  
68  1 Y 1 A TYR -37  ? A TYR 68  
69  1 Y 1 A LYS -36  ? A LYS 69  
70  1 Y 1 A ASN -35  ? A ASN 70  
71  1 Y 1 A VAL -34  ? A VAL 71  
72  1 Y 1 A PHE -33  ? A PHE 72  
73  1 Y 1 A SER -32  ? A SER 73  
74  1 Y 1 A GLY -31  ? A GLY 74  
75  1 Y 1 A PHE -30  ? A PHE 75  
76  1 Y 1 A ALA -29  ? A ALA 76  
77  1 Y 1 A ALA -28  ? A ALA 77  
78  1 Y 1 A THR -27  ? A THR 78  
79  1 Y 1 A LEU -26  ? A LEU 79  
80  1 Y 1 A ASP -25  ? A ASP 80  
81  1 Y 1 A GLU -24  ? A GLU 81  
82  1 Y 1 A ASN -23  ? A ASN 82  
83  1 Y 1 A MET -22  ? A MET 83  
84  1 Y 1 A VAL -21  ? A VAL 84  
85  1 Y 1 A ARG -20  ? A ARG 85  
86  1 Y 1 A VAL -19  ? A VAL 86  
87  1 Y 1 A LEU -18  ? A LEU 87  
88  1 Y 1 A ARG -17  ? A ARG 88  
89  1 Y 1 A ALA -16  ? A ALA 89  
90  1 Y 1 A HIS -15  ? A HIS 90  
91  1 Y 1 A PRO -14  ? A PRO 91  
92  1 Y 1 A ASP -13  ? A ASP 92  
93  1 Y 1 A VAL -12  ? A VAL 93  
94  1 Y 1 A GLU -11  ? A GLU 94  
95  1 Y 1 A TYR -10  ? A TYR 95  
96  1 Y 1 A ILE -9   ? A ILE 96  
97  1 Y 1 A GLU -8   ? A GLU 97  
98  1 Y 1 A GLN -7   ? A GLN 98  
99  1 Y 1 A ASP -6   ? A ASP 99  
100 1 Y 1 A ALA -5   ? A ALA 100 
101 1 Y 1 A VAL -4   ? A VAL 101 
102 1 Y 1 A VAL -3   ? A VAL 102 
103 1 Y 1 A THR -2   ? A THR 103 
104 1 Y 1 A ILE -1   ? A ILE 104 
105 1 Y 1 A ASN 0    ? A ASN 105 
# 
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  
CA  CA   CA N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
NO3 N    N  N N 251 
NO3 O1   O  N N 252 
NO3 O2   O  N N 253 
NO3 O3   O  N N 254 
PHE N    N  N N 255 
PHE CA   C  N S 256 
PHE C    C  N N 257 
PHE O    O  N N 258 
PHE CB   C  N N 259 
PHE CG   C  Y N 260 
PHE CD1  C  Y N 261 
PHE CD2  C  Y N 262 
PHE CE1  C  Y N 263 
PHE CE2  C  Y N 264 
PHE CZ   C  Y N 265 
PHE OXT  O  N N 266 
PHE H    H  N N 267 
PHE H2   H  N N 268 
PHE HA   H  N N 269 
PHE HB2  H  N N 270 
PHE HB3  H  N N 271 
PHE HD1  H  N N 272 
PHE HD2  H  N N 273 
PHE HE1  H  N N 274 
PHE HE2  H  N N 275 
PHE HZ   H  N N 276 
PHE HXT  H  N N 277 
PRO N    N  N N 278 
PRO CA   C  N S 279 
PRO C    C  N N 280 
PRO O    O  N N 281 
PRO CB   C  N N 282 
PRO CG   C  N N 283 
PRO CD   C  N N 284 
PRO OXT  O  N N 285 
PRO H    H  N N 286 
PRO HA   H  N N 287 
PRO HB2  H  N N 288 
PRO HB3  H  N N 289 
PRO HG2  H  N N 290 
PRO HG3  H  N N 291 
PRO HD2  H  N N 292 
PRO HD3  H  N N 293 
PRO HXT  H  N N 294 
SER N    N  N N 295 
SER CA   C  N S 296 
SER C    C  N N 297 
SER O    O  N N 298 
SER CB   C  N N 299 
SER OG   O  N N 300 
SER OXT  O  N N 301 
SER H    H  N N 302 
SER H2   H  N N 303 
SER HA   H  N N 304 
SER HB2  H  N N 305 
SER HB3  H  N N 306 
SER HG   H  N N 307 
SER HXT  H  N N 308 
THR N    N  N N 309 
THR CA   C  N S 310 
THR C    C  N N 311 
THR O    O  N N 312 
THR CB   C  N R 313 
THR OG1  O  N N 314 
THR CG2  C  N N 315 
THR OXT  O  N N 316 
THR H    H  N N 317 
THR H2   H  N N 318 
THR HA   H  N N 319 
THR HB   H  N N 320 
THR HG1  H  N N 321 
THR HG21 H  N N 322 
THR HG22 H  N N 323 
THR HG23 H  N N 324 
THR HXT  H  N N 325 
TRP N    N  N N 326 
TRP CA   C  N S 327 
TRP C    C  N N 328 
TRP O    O  N N 329 
TRP CB   C  N N 330 
TRP CG   C  Y N 331 
TRP CD1  C  Y N 332 
TRP CD2  C  Y N 333 
TRP NE1  N  Y N 334 
TRP CE2  C  Y N 335 
TRP CE3  C  Y N 336 
TRP CZ2  C  Y N 337 
TRP CZ3  C  Y N 338 
TRP CH2  C  Y N 339 
TRP OXT  O  N N 340 
TRP H    H  N N 341 
TRP H2   H  N N 342 
TRP HA   H  N N 343 
TRP HB2  H  N N 344 
TRP HB3  H  N N 345 
TRP HD1  H  N N 346 
TRP HE1  H  N N 347 
TRP HE3  H  N N 348 
TRP HZ2  H  N N 349 
TRP HZ3  H  N N 350 
TRP HH2  H  N N 351 
TRP HXT  H  N N 352 
TYR N    N  N N 353 
TYR CA   C  N S 354 
TYR C    C  N N 355 
TYR O    O  N N 356 
TYR CB   C  N N 357 
TYR CG   C  Y N 358 
TYR CD1  C  Y N 359 
TYR CD2  C  Y N 360 
TYR CE1  C  Y N 361 
TYR CE2  C  Y N 362 
TYR CZ   C  Y N 363 
TYR OH   O  N N 364 
TYR OXT  O  N N 365 
TYR H    H  N N 366 
TYR H2   H  N N 367 
TYR HA   H  N N 368 
TYR HB2  H  N N 369 
TYR HB3  H  N N 370 
TYR HD1  H  N N 371 
TYR HD2  H  N N 372 
TYR HE1  H  N N 373 
TYR HE2  H  N N 374 
TYR HH   H  N N 375 
TYR HXT  H  N N 376 
VAL N    N  N N 377 
VAL CA   C  N S 378 
VAL C    C  N N 379 
VAL O    O  N N 380 
VAL CB   C  N N 381 
VAL CG1  C  N N 382 
VAL CG2  C  N N 383 
VAL OXT  O  N N 384 
VAL H    H  N N 385 
VAL H2   H  N N 386 
VAL HA   H  N N 387 
VAL HB   H  N N 388 
VAL HG11 H  N N 389 
VAL HG12 H  N N 390 
VAL HG13 H  N N 391 
VAL HG21 H  N N 392 
VAL HG22 H  N N 393 
VAL HG23 H  N N 394 
VAL HXT  H  N N 395 
# 
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  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
NO3 N   O1   doub N N 237 
NO3 N   O2   sing N N 238 
NO3 N   O3   sing N N 239 
PHE N   CA   sing N N 240 
PHE N   H    sing N N 241 
PHE N   H2   sing N N 242 
PHE CA  C    sing N N 243 
PHE CA  CB   sing N N 244 
PHE CA  HA   sing N N 245 
PHE C   O    doub N N 246 
PHE C   OXT  sing N N 247 
PHE CB  CG   sing N N 248 
PHE CB  HB2  sing N N 249 
PHE CB  HB3  sing N N 250 
PHE CG  CD1  doub Y N 251 
PHE CG  CD2  sing Y N 252 
PHE CD1 CE1  sing Y N 253 
PHE CD1 HD1  sing N N 254 
PHE CD2 CE2  doub Y N 255 
PHE CD2 HD2  sing N N 256 
PHE CE1 CZ   doub Y N 257 
PHE CE1 HE1  sing N N 258 
PHE CE2 CZ   sing Y N 259 
PHE CE2 HE2  sing N N 260 
PHE CZ  HZ   sing N N 261 
PHE OXT HXT  sing N N 262 
PRO N   CA   sing N N 263 
PRO N   CD   sing N N 264 
PRO N   H    sing N N 265 
PRO CA  C    sing N N 266 
PRO CA  CB   sing N N 267 
PRO CA  HA   sing N N 268 
PRO C   O    doub N N 269 
PRO C   OXT  sing N N 270 
PRO CB  CG   sing N N 271 
PRO CB  HB2  sing N N 272 
PRO CB  HB3  sing N N 273 
PRO CG  CD   sing N N 274 
PRO CG  HG2  sing N N 275 
PRO CG  HG3  sing N N 276 
PRO CD  HD2  sing N N 277 
PRO CD  HD3  sing N N 278 
PRO OXT HXT  sing N N 279 
SER N   CA   sing N N 280 
SER N   H    sing N N 281 
SER N   H2   sing N N 282 
SER CA  C    sing N N 283 
SER CA  CB   sing N N 284 
SER CA  HA   sing N N 285 
SER C   O    doub N N 286 
SER C   OXT  sing N N 287 
SER CB  OG   sing N N 288 
SER CB  HB2  sing N N 289 
SER CB  HB3  sing N N 290 
SER OG  HG   sing N N 291 
SER OXT HXT  sing N N 292 
THR N   CA   sing N N 293 
THR N   H    sing N N 294 
THR N   H2   sing N N 295 
THR CA  C    sing N N 296 
THR CA  CB   sing N N 297 
THR CA  HA   sing N N 298 
THR C   O    doub N N 299 
THR C   OXT  sing N N 300 
THR CB  OG1  sing N N 301 
THR CB  CG2  sing N N 302 
THR CB  HB   sing N N 303 
THR OG1 HG1  sing N N 304 
THR CG2 HG21 sing N N 305 
THR CG2 HG22 sing N N 306 
THR CG2 HG23 sing N N 307 
THR OXT HXT  sing N N 308 
TRP N   CA   sing N N 309 
TRP N   H    sing N N 310 
TRP N   H2   sing N N 311 
TRP CA  C    sing N N 312 
TRP CA  CB   sing N N 313 
TRP CA  HA   sing N N 314 
TRP C   O    doub N N 315 
TRP C   OXT  sing N N 316 
TRP CB  CG   sing N N 317 
TRP CB  HB2  sing N N 318 
TRP CB  HB3  sing N N 319 
TRP CG  CD1  doub Y N 320 
TRP CG  CD2  sing Y N 321 
TRP CD1 NE1  sing Y N 322 
TRP CD1 HD1  sing N N 323 
TRP CD2 CE2  doub Y N 324 
TRP CD2 CE3  sing Y N 325 
TRP NE1 CE2  sing Y N 326 
TRP NE1 HE1  sing N N 327 
TRP CE2 CZ2  sing Y N 328 
TRP CE3 CZ3  doub Y N 329 
TRP CE3 HE3  sing N N 330 
TRP CZ2 CH2  doub Y N 331 
TRP CZ2 HZ2  sing N N 332 
TRP CZ3 CH2  sing Y N 333 
TRP CZ3 HZ3  sing N N 334 
TRP CH2 HH2  sing N N 335 
TRP OXT HXT  sing N N 336 
TYR N   CA   sing N N 337 
TYR N   H    sing N N 338 
TYR N   H2   sing N N 339 
TYR CA  C    sing N N 340 
TYR CA  CB   sing N N 341 
TYR CA  HA   sing N N 342 
TYR C   O    doub N N 343 
TYR C   OXT  sing N N 344 
TYR CB  CG   sing N N 345 
TYR CB  HB2  sing N N 346 
TYR CB  HB3  sing N N 347 
TYR CG  CD1  doub Y N 348 
TYR CG  CD2  sing Y N 349 
TYR CD1 CE1  sing Y N 350 
TYR CD1 HD1  sing N N 351 
TYR CD2 CE2  doub Y N 352 
TYR CD2 HD2  sing N N 353 
TYR CE1 CZ   doub Y N 354 
TYR CE1 HE1  sing N N 355 
TYR CE2 CZ   sing Y N 356 
TYR CE2 HE2  sing N N 357 
TYR CZ  OH   sing N N 358 
TYR OH  HH   sing N N 359 
TYR OXT HXT  sing N N 360 
VAL N   CA   sing N N 361 
VAL N   H    sing N N 362 
VAL N   H2   sing N N 363 
VAL CA  C    sing N N 364 
VAL CA  CB   sing N N 365 
VAL CA  HA   sing N N 366 
VAL C   O    doub N N 367 
VAL C   OXT  sing N N 368 
VAL CB  CG1  sing N N 369 
VAL CB  CG2  sing N N 370 
VAL CB  HB   sing N N 371 
VAL CG1 HG11 sing N N 372 
VAL CG1 HG12 sing N N 373 
VAL CG1 HG13 sing N N 374 
VAL CG2 HG21 sing N N 375 
VAL CG2 HG22 sing N N 376 
VAL CG2 HG23 sing N N 377 
VAL OXT HXT  sing N N 378 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'German Research Foundation (DFG)'                        Germany 458246365 1 
'German Research Foundation (DFG)'                        Germany 451079909 2 
'German Federal Ministry for Economic Affairs and Energy' Germany 01KI2114  3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1IC6 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.method        'fixed target' 
# 
_pdbx_serial_crystallography_sample_delivery_fixed_target.diffrn_id                       1 
_pdbx_serial_crystallography_sample_delivery_fixed_target.description                     ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_holding                  'HARE-Chip , Kapton (50um)' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.support_base                    ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_unit_size                ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.crystals_per_unit               ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_solvent                  ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_dehydration_prevention   ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.motion_control                  ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.velocity_horizontal             ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.velocity_vertical               ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.details                         ? 
# 
_space_group.name_H-M_alt     'P 43 21 2' 
_space_group.name_Hall        'P 4nw 2abw' 
_space_group.IT_number        96 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8RSF 
_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]   0.014599 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.014599 
_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]   0.009195 
_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.
;
? 
CA ? ? 16.26893 3.65395 ? ? 3.58509  77.28589 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 106 ? 56.84179 58.13702 9.42687  1.000 15.19085 ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 106 ? 56.52052 59.28502 10.30929 1.000 14.91214 ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 106 ? 57.55949 59.38447 11.41848 1.000 14.46507 ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 106 ? 58.21195 58.40356 11.75408 1.000 13.71065 ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 106 ? 55.12163 59.14679 10.91866 1.000 15.45943 ? 1   ALA A CB  1 
ATOM   6    N  N   . ALA A 1 107 ? 57.72380 60.56737 12.00839 1.000 14.16536 ? 2   ALA A N   1 
ATOM   7    C  CA  . ALA A 1 107 ? 58.70604 60.72659 13.07014 1.000 14.69565 ? 2   ALA A CA  1 
ATOM   8    C  C   . ALA A 1 107 ? 58.11521 61.70857 14.07027 1.000 22.90527 ? 2   ALA A C   1 
ATOM   9    O  O   . ALA A 1 107 ? 57.61890 62.77147 13.67964 1.000 22.88905 ? 2   ALA A O   1 
ATOM   10   C  CB  . ALA A 1 107 ? 60.05147 61.24114 12.54860 1.000 16.90605 ? 2   ALA A CB  1 
ATOM   11   N  N   . GLN A 1 108 ? 58.14547 61.33900 15.34383 1.000 11.53338 ? 3   GLN A N   1 
ATOM   12   C  CA  . GLN A 1 108 ? 57.75611 62.23389 16.42233 1.000 9.20833  ? 3   GLN A CA  1 
ATOM   13   C  C   . GLN A 1 108 ? 59.02557 62.70565 17.11712 1.000 10.71628 ? 3   GLN A C   1 
ATOM   14   O  O   . GLN A 1 108 ? 59.73066 61.89480 17.74182 1.000 10.43151 ? 3   GLN A O   1 
ATOM   15   C  CB  . GLN A 1 108 ? 56.84510 61.48193 17.40481 1.000 8.53405  ? 3   GLN A CB  1 
ATOM   16   C  CG  . GLN A 1 108 ? 56.46079 62.33302 18.58566 1.000 8.86192  ? 3   GLN A CG  1 
ATOM   17   C  CD  . GLN A 1 108 ? 55.71065 61.53219 19.63903 1.000 10.38103 ? 3   GLN A CD  1 
ATOM   18   O  OE1 . GLN A 1 108 ? 55.33390 60.35993 19.41870 1.000 11.15326 ? 3   GLN A OE1 1 
ATOM   19   N  NE2 . GLN A 1 108 ? 55.49959 62.15883 20.80889 1.000 10.61380 ? 3   GLN A NE2 1 
ATOM   20   N  N   . THR A 1 109 ? 59.31884 64.00607 17.02085 1.000 11.95737 ? 4   THR A N   1 
ATOM   21   C  CA  . THR A 1 109 ? 60.51698 64.53800 17.66726 1.000 13.95715 ? 4   THR A CA  1 
ATOM   22   C  C   . THR A 1 109 ? 60.25132 64.78831 19.15958 1.000 11.52625 ? 4   THR A C   1 
ATOM   23   O  O   . THR A 1 109 ? 59.10488 65.00390 19.58362 1.000 14.19866 ? 4   THR A O   1 
ATOM   24   C  CB  . THR A 1 109 ? 60.98846 65.82698 16.97361 1.000 17.32609 ? 4   THR A CB  1 
ATOM   25   O  OG1 . THR A 1 109 ? 59.93391 66.78968 16.98579 1.000 23.95482 ? 4   THR A OG1 1 
ATOM   26   C  CG2 . THR A 1 109 ? 61.36120 65.55192 15.51749 1.000 17.51196 ? 4   THR A CG2 1 
ATOM   27   N  N   . ASN A 1 110 ? 61.32670 64.74270 19.95715 1.000 15.56291 ? 5   ASN A N   1 
ATOM   28   C  CA  . ASN A 1 110 ? 61.25052 64.96989 21.40449 1.000 15.03815 ? 5   ASN A CA  1 
ATOM   29   C  C   . ASN A 1 110 ? 60.19715 64.06186 22.04181 1.000 13.45297 ? 5   ASN A C   1 
ATOM   30   O  O   . ASN A 1 110 ? 59.35552 64.47432 22.85260 1.000 15.72874 ? 5   ASN A O   1 
ATOM   31   C  CB  . ASN A 1 110 ? 60.96350 66.43952 21.70831 1.000 16.89379 ? 5   ASN A CB  1 
ATOM   32   C  CG  . ASN A 1 110 ? 62.12517 67.32173 21.33525 1.000 34.69155 ? 5   ASN A CG  1 
ATOM   33   O  OD1 . ASN A 1 110 ? 63.26351 67.07715 21.74229 1.000 45.43316 ? 5   ASN A OD1 1 
ATOM   34   N  ND2 . ASN A 1 110 ? 61.85354 68.34057 20.53567 1.000 46.46739 ? 5   ASN A ND2 1 
ATOM   35   N  N   . ALA A 1 111 ? 60.23436 62.79739 21.64028 1.000 11.16786 ? 6   ALA A N   1 
ATOM   36   C  CA  . ALA A 1 111 ? 59.27999 61.82933 22.13554 1.000 8.96695  ? 6   ALA A CA  1 
ATOM   37   C  C   . ALA A 1 111 ? 59.67738 61.39419 23.55043 1.000 8.63797  ? 6   ALA A C   1 
ATOM   38   O  O   . ALA A 1 111 ? 60.85058 61.46216 23.91338 1.000 12.99555 ? 6   ALA A O   1 
ATOM   39   C  CB  . ALA A 1 111 ? 59.25739 60.61650 21.20465 1.000 12.36594 ? 6   ALA A CB  1 
ATOM   40   N  N   . PRO A 1 112 ? 58.73244 60.85763 24.33264 1.000 8.78207  ? 7   PRO A N   1 
ATOM   41   C  CA  . PRO A 1 112 ? 59.11622 60.15008 25.56556 1.000 8.12508  ? 7   PRO A CA  1 
ATOM   42   C  C   . PRO A 1 112 ? 60.14635 59.06822 25.26178 1.000 9.06505  ? 7   PRO A C   1 
ATOM   43   O  O   . PRO A 1 112 ? 60.11635 58.41870 24.20621 1.000 10.28766 ? 7   PRO A O   1 
ATOM   44   C  CB  . PRO A 1 112 ? 57.80373 59.51644 26.04909 1.000 11.01776 ? 7   PRO A CB  1 
ATOM   45   C  CG  . PRO A 1 112 ? 56.71080 60.30478 25.38305 1.000 12.96264 ? 7   PRO A CG  1 
ATOM   46   C  CD  . PRO A 1 112 ? 57.28392 60.76394 24.05701 1.000 10.00564 ? 7   PRO A CD  1 
ATOM   47   N  N   . TRP A 1 113 ? 61.07485 58.86926 26.19691 1.000 7.25750  ? 8   TRP A N   1 
ATOM   48   C  CA  . TRP A 1 113 ? 62.22982 58.02064 25.88653 1.000 7.12733  ? 8   TRP A CA  1 
ATOM   49   C  C   . TRP A 1 113 ? 61.83156 56.60759 25.50064 1.000 6.75930  ? 8   TRP A C   1 
ATOM   50   O  O   . TRP A 1 113 ? 62.52805 55.99557 24.68349 1.000 8.04197  ? 8   TRP A O   1 
ATOM   51   C  CB  . TRP A 1 113 ? 63.21282 57.99529 27.07330 1.000 7.94950  ? 8   TRP A CB  1 
ATOM   52   C  CG  . TRP A 1 113 ? 62.83394 57.07699 28.21060 1.000 7.01042  ? 8   TRP A CG  1 
ATOM   53   C  CD1 . TRP A 1 113 ? 62.19560 57.43650 29.38589 1.000 9.76746  ? 8   TRP A CD1 1 
ATOM   54   C  CD2 . TRP A 1 113 ? 63.11439 55.67248 28.32755 1.000 7.21541  ? 8   TRP A CD2 1 
ATOM   55   N  NE1 . TRP A 1 113 ? 62.03154 56.32289 30.19905 1.000 7.75081  ? 8   TRP A NE1 1 
ATOM   56   C  CE2 . TRP A 1 113 ? 62.57567 55.22923 29.56755 1.000 8.05352  ? 8   TRP A CE2 1 
ATOM   57   C  CE3 . TRP A 1 113 ? 63.74593 54.73214 27.49427 1.000 6.88367  ? 8   TRP A CE3 1 
ATOM   58   C  CZ2 . TRP A 1 113 ? 62.65976 53.88834 29.99192 1.000 7.47904  ? 8   TRP A CZ2 1 
ATOM   59   C  CZ3 . TRP A 1 113 ? 63.81294 53.40882 27.89812 1.000 7.28650  ? 8   TRP A CZ3 1 
ATOM   60   C  CH2 . TRP A 1 113 ? 63.27723 52.98725 29.14619 1.000 6.80592  ? 8   TRP A CH2 1 
ATOM   61   N  N   . GLY A 1 114 ? 60.74939 56.07414 26.07630 1.000 7.19906  ? 9   GLY A N   1 
ATOM   62   C  CA  . GLY A 1 114 ? 60.37579 54.69150 25.79490 1.000 7.06760  ? 9   GLY A CA  1 
ATOM   63   C  C   . GLY A 1 114 ? 59.90133 54.49082 24.36607 1.000 6.30022  ? 9   GLY A C   1 
ATOM   64   O  O   . GLY A 1 114 ? 60.17115 53.44045 23.75085 1.000 7.85625  ? 9   GLY A O   1 
ATOM   65   N  N   . LEU A 1 115 ? 59.16655 55.47773 23.82366 1.000 6.63778  ? 10  LEU A N   1 
ATOM   66   C  CA  . LEU A 1 115 ? 58.78030 55.39058 22.41234 1.000 6.63390  ? 10  LEU A CA  1 
ATOM   67   C  C   . LEU A 1 115 ? 60.01805 55.45967 21.50866 1.000 9.26996  ? 10  LEU A C   1 
ATOM   68   O  O   . LEU A 1 115 ? 60.14040 54.69606 20.52968 1.000 10.63131 ? 10  LEU A O   1 
ATOM   69   C  CB  . LEU A 1 115 ? 57.82677 56.52422 22.04016 1.000 8.32195  ? 10  LEU A CB  1 
ATOM   70   C  CG  . LEU A 1 115 ? 56.50568 56.58820 22.82516 1.000 9.71535  ? 10  LEU A CG  1 
ATOM   71   C  CD1 . LEU A 1 115 ? 55.59945 57.65658 22.19458 1.000 9.89469  ? 10  LEU A CD1 1 
ATOM   72   C  CD2 . LEU A 1 115 ? 55.78715 55.23761 22.79359 1.000 10.84173 ? 10  LEU A CD2 1 
ATOM   73   N  N   . ALA A 1 116 ? 60.94279 56.38480 21.80549 1.000 8.41749  ? 11  ALA A N   1 
ATOM   74   C  CA  . ALA A 1 116 ? 62.16310 56.43339 21.01223 1.000 7.42132  ? 11  ALA A CA  1 
ATOM   75   C  C   . ALA A 1 116 ? 62.91668 55.10744 21.09368 1.000 8.72274  ? 11  ALA A C   1 
ATOM   76   O  O   . ALA A 1 116 ? 63.46460 54.62834 20.09370 1.000 10.77651 ? 11  ALA A O   1 
ATOM   77   C  CB  . ALA A 1 116 ? 63.04078 57.59651 21.47318 1.000 9.03015  ? 11  ALA A CB  1 
ATOM   78   N  N   . ARG A 1 117 ? 62.93431 54.48581 22.27576 1.000 7.74591  ? 12  ARG A N   1 
ATOM   79   C  CA  . ARG A 1 117 ? 63.74136 53.27800 22.46801 1.000 7.20827  ? 12  ARG A CA  1 
ATOM   80   C  C   . ARG A 1 117 ? 63.21204 52.11962 21.63291 1.000 10.33437 ? 12  ARG A C   1 
ATOM   81   O  O   . ARG A 1 117 ? 64.01178 51.30990 21.13605 1.000 8.96028  ? 12  ARG A O   1 
ATOM   82   C  CB  . ARG A 1 117 ? 63.76253 52.86152 23.96312 1.000 7.93319  ? 12  ARG A CB  1 
ATOM   83   C  CG  . ARG A 1 117 ? 64.74746 51.70799 24.27285 1.000 8.27581  ? 12  ARG A CG  1 
ATOM   84   C  CD  . ARG A 1 117 ? 66.18910 52.18802 24.08101 1.000 11.33115 ? 12  ARG A CD  1 
ATOM   85   N  NE  . ARG A 1 117 ? 67.17498 51.10577 24.09102 1.000 8.87722  ? 12  ARG A NE  1 
ATOM   86   C  CZ  . ARG A 1 117 ? 67.55152 50.43177 23.00627 1.000 10.86762 ? 12  ARG A CZ  1 
ATOM   87   N  NH1 . ARG A 1 117 ? 66.93162 50.59407 21.84160 1.000 10.46626 ? 12  ARG A NH1 1 
ATOM   88   N  NH2 . ARG A 1 117 ? 68.56567 49.57272 23.09160 1.000 11.78010 ? 12  ARG A NH2 1 
ATOM   89   N  N   . ILE A 1 118 ? 61.88035 51.98245 21.51754 1.000 7.91222  ? 13  ILE A N   1 
ATOM   90   C  CA  . ILE A 1 118 ? 61.33570 50.86416 20.76309 1.000 7.05562  ? 13  ILE A CA  1 
ATOM   91   C  C   . ILE A 1 118 ? 61.48100 51.04511 19.26640 1.000 8.62195  ? 13  ILE A C   1 
ATOM   92   O  O   . ILE A 1 118 ? 61.17075 50.10066 18.53305 1.000 10.27312 ? 13  ILE A O   1 
ATOM   93   C  CB  . ILE A 1 118 ? 59.86960 50.56371 21.10400 1.000 10.04242 ? 13  ILE A CB  1 
ATOM   94   C  CG1 . ILE A 1 118 ? 58.96019 51.71888 20.74632 1.000 15.25192 ? 13  ILE A CG1 1 
ATOM   95   C  CG2 . ILE A 1 118 ? 59.72994 50.10031 22.58826 1.000 15.33100 ? 13  ILE A CG2 1 
ATOM   96   C  CD1 . ILE A 1 118 ? 57.49993 51.24036 20.63633 1.000 25.02119 ? 13  ILE A CD1 1 
ATOM   97   N  N   . SER A 1 119 ? 61.94860 52.21537 18.77081 1.000 7.66241  ? 14  SER A N   1 
ATOM   98   C  CA  . SER A 1 119 ? 62.20988 52.38632 17.33650 1.000 10.05130 ? 14  SER A CA  1 
ATOM   99   C  C   . SER A 1 119 ? 63.69701 52.59914 17.02641 1.000 12.61217 ? 14  SER A C   1 
ATOM   100  O  O   . SER A 1 119 ? 64.05996 53.08278 15.93275 1.000 14.87484 ? 14  SER A O   1 
ATOM   101  C  CB  . SER A 1 119 ? 61.36116 53.52643 16.77416 1.000 11.33784 ? 14  SER A CB  1 
ATOM   102  O  OG  . SER A 1 119 ? 61.76705 54.81187 17.28121 1.000 12.23642 ? 14  SER A OG  1 
ATOM   103  N  N   . SER A 1 120 ? 64.57950 52.16278 17.92379 1.000 9.24603  ? 15  SER A N   1 
ATOM   104  C  CA  . SER A 1 120 ? 66.01370 52.37990 17.79482 1.000 8.79892  ? 15  SER A CA  1 
ATOM   105  C  C   . SER A 1 120 ? 66.79146 51.12281 18.16256 1.000 10.71747 ? 15  SER A C   1 
ATOM   106  O  O   . SER A 1 120 ? 66.36761 50.34324 19.01332 1.000 11.21452 ? 15  SER A O   1 
ATOM   107  C  CB  . SER A 1 120 ? 66.47325 53.51349 18.71960 1.000 11.79995 ? 15  SER A CB  1 
ATOM   108  O  OG  . SER A 1 120 ? 67.88042 53.74053 18.51769 1.000 15.99179 ? 15  SER A OG  1 
ATOM   109  N  N   . THR A 1 121 ? 67.95734 50.95389 17.54644 1.000 13.92556 ? 16  THR A N   1 
ATOM   110  C  CA  . THR A 1 121 ? 68.83777 49.87800 17.97897 1.000 13.74575 ? 16  THR A CA  1 
ATOM   111  C  C   . THR A 1 121 ? 69.82987 50.32705 19.04802 1.000 18.58410 ? 16  THR A C   1 
ATOM   112  O  O   . THR A 1 121 ? 70.71005 49.54785 19.43550 1.000 27.49658 ? 16  THR A O   1 
ATOM   113  C  CB  . THR A 1 121 ? 69.59798 49.29574 16.79367 1.000 15.53033 ? 16  THR A CB  1 
ATOM   114  O  OG1 . THR A 1 121 ? 70.33180 50.34783 16.17238 1.000 18.81711 ? 16  THR A OG1 1 
ATOM   115  C  CG2 . THR A 1 121 ? 68.62870 48.68806 15.79380 1.000 16.27259 ? 16  THR A CG2 1 
ATOM   116  N  N   . SER A 1 122 ? 69.73882 51.55562 19.52000 1.000 15.58634 ? 17  SER A N   1 
ATOM   117  C  CA  . SER A 1 122 ? 70.65900 52.04355 20.54970 1.000 16.15813 ? 17  SER A CA  1 
ATOM   118  C  C   . SER A 1 122 ? 69.90196 52.93212 21.52613 1.000 16.68487 ? 17  SER A C   1 
ATOM   119  O  O   . SER A 1 122 ? 68.92015 53.58233 21.14265 1.000 14.13139 ? 17  SER A O   1 
ATOM   120  C  CB  . SER A 1 122 ? 71.82795 52.83347 19.95418 1.000 19.32500 ? 17  SER A CB  1 
ATOM   121  O  OG  . SER A 1 122 ? 71.33979 53.94072 19.23902 1.000 28.91794 ? 17  SER A OG  1 
ATOM   122  N  N   . PRO A 1 123 ? 70.31866 52.97931 22.79183 1.000 14.47506 ? 18  PRO A N   1 
ATOM   123  C  CA  . PRO A 1 123 ? 69.67692 53.89199 23.73749 1.000 13.08593 ? 18  PRO A CA  1 
ATOM   124  C  C   . PRO A 1 123 ? 70.12923 55.33002 23.49797 1.000 12.49754 ? 18  PRO A C   1 
ATOM   125  O  O   . PRO A 1 123 ? 71.10069 55.60815 22.77469 1.000 16.54813 ? 18  PRO A O   1 
ATOM   126  C  CB  . PRO A 1 123 ? 70.14541 53.35598 25.10188 1.000 15.89864 ? 18  PRO A CB  1 
ATOM   127  C  CG  . PRO A 1 123 ? 71.51856 52.83052 24.81867 1.000 19.52830 ? 18  PRO A CG  1 
ATOM   128  C  CD  . PRO A 1 123 ? 71.41863 52.22338 23.42244 1.000 21.10363 ? 18  PRO A CD  1 
ATOM   129  N  N   . GLY A 1 124 ? 69.38701 56.25505 24.10341 1.000 13.51053 ? 19  GLY A N   1 
ATOM   130  C  CA  . GLY A 1 124 ? 69.78144 57.64914 24.11315 1.000 14.37735 ? 19  GLY A CA  1 
ATOM   131  C  C   . GLY A 1 124 ? 69.23702 58.50659 22.99554 1.000 19.42043 ? 19  GLY A C   1 
ATOM   132  O  O   . GLY A 1 124 ? 69.62320 59.67389 22.90179 1.000 20.65092 ? 19  GLY A O   1 
ATOM   133  N  N   . THR A 1 125 ? 68.37602 57.97599 22.13495 1.000 15.29889 ? 20  THR A N   1 
ATOM   134  C  CA  . THR A 1 125 ? 67.77537 58.78495 21.07321 1.000 13.22402 ? 20  THR A CA  1 
ATOM   135  C  C   . THR A 1 125 ? 66.46083 59.40645 21.54980 1.000 13.13173 ? 20  THR A C   1 
ATOM   136  O  O   . THR A 1 125 ? 65.89112 59.01333 22.56285 1.000 16.81727 ? 20  THR A O   1 
ATOM   137  C  CB  . THR A 1 125 ? 67.52040 57.95487 19.81046 1.000 18.01458 ? 20  THR A CB  1 
ATOM   138  O  OG1 . THR A 1 125 ? 66.41702 57.06205 20.04470 1.000 17.02461 ? 20  THR A OG1 1 
ATOM   139  C  CG2 . THR A 1 125 ? 68.75940 57.15775 19.40353 1.000 18.25649 ? 20  THR A CG2 1 
ATOM   140  N  N   . SER A 1 126 ? 65.97485 60.40335 20.80951 1.000 15.44610 ? 21  SER A N   1 
ATOM   141  C  CA  . SER A 1 126 ? 64.77169 61.09276 21.25957 1.000 16.78102 ? 21  SER A CA  1 
ATOM   142  C  C   . SER A 1 126 ? 63.68024 61.18190 20.19553 1.000 14.85372 ? 21  SER A C   1 
ATOM   143  O  O   . SER A 1 126 ? 62.69919 61.90137 20.40328 1.000 17.91155 ? 21  SER A O   1 
ATOM   144  C  CB  . SER A 1 126 ? 65.10909 62.50377 21.73747 1.000 20.63656 ? 21  SER A CB  1 
ATOM   145  O  OG  . SER A 1 126 ? 65.71509 63.17253 20.66617 1.000 26.04228 ? 21  SER A OG  1 
ATOM   146  N  N   . THR A 1 127 ? 63.82237 60.49978 19.06054 1.000 11.67691 ? 22  THR A N   1 
ATOM   147  C  CA  . THR A 1 127 ? 62.79580 60.52547 18.02175 1.000 11.15272 ? 22  THR A CA  1 
ATOM   148  C  C   . THR A 1 127 ? 62.13163 59.16316 17.93836 1.000 11.78245 ? 22  THR A C   1 
ATOM   149  O  O   . THR A 1 127 ? 62.82404 58.14003 17.92297 1.000 13.46509 ? 22  THR A O   1 
ATOM   150  C  CB  . THR A 1 127 ? 63.39391 60.88254 16.66382 1.000 11.92291 ? 22  THR A CB  1 
ATOM   151  O  OG1 . THR A 1 127 ? 64.01215 62.18729 16.73539 1.000 17.91557 ? 22  THR A OG1 1 
ATOM   152  C  CG2 . THR A 1 127 ? 62.36107 60.90030 15.58141 1.000 14.76996 ? 22  THR A CG2 1 
ATOM   153  N  N   . TYR A 1 128 ? 60.80603 59.14822 17.86209 1.000 8.44516  ? 23  TYR A N   1 
ATOM   154  C  CA  . TYR A 1 128 ? 60.06263 57.90339 17.65297 1.000 8.03760  ? 23  TYR A CA  1 
ATOM   155  C  C   . TYR A 1 128 ? 59.70318 57.78300 16.17418 1.000 10.61762 ? 23  TYR A C   1 
ATOM   156  O  O   . TYR A 1 128 ? 58.96639 58.61157 15.64707 1.000 10.00237 ? 23  TYR A O   1 
ATOM   157  C  CB  . TYR A 1 128 ? 58.79944 57.88983 18.51374 1.000 7.54624  ? 23  TYR A CB  1 
ATOM   158  C  CG  . TYR A 1 128 ? 57.83701 56.73456 18.29575 1.000 8.20614  ? 23  TYR A CG  1 
ATOM   159  C  CD1 . TYR A 1 128 ? 58.31704 55.44680 18.05689 1.000 8.02453  ? 23  TYR A CD1 1 
ATOM   160  C  CD2 . TYR A 1 128 ? 56.45989 56.93328 18.36451 1.000 9.52506  ? 23  TYR A CD2 1 
ATOM   161  C  CE1 . TYR A 1 128 ? 57.42419 54.37982 17.90269 1.000 7.27781  ? 23  TYR A CE1 1 
ATOM   162  C  CE2 . TYR A 1 128 ? 55.56318 55.87168 18.21433 1.000 6.69537  ? 23  TYR A CE2 1 
ATOM   163  C  CZ  . TYR A 1 128 ? 56.06898 54.59867 17.97500 1.000 9.60324  ? 23  TYR A CZ  1 
ATOM   164  O  OH  . TYR A 1 128 ? 55.20913 53.53863 17.81353 1.000 9.56420  ? 23  TYR A OH  1 
ATOM   165  N  N   A TYR A 1 129 ? 60.23741 56.75933 15.51033 0.581 10.56066 ? 24  TYR A N   1 
ATOM   166  N  N   B TYR A 1 129 ? 60.25010 56.77700 15.49248 0.419 10.55215 ? 24  TYR A N   1 
ATOM   167  C  CA  A TYR A 1 129 ? 60.00645 56.51934 14.09132 0.581 11.22419 ? 24  TYR A CA  1 
ATOM   168  C  CA  B TYR A 1 129 ? 59.96116 56.56366 14.07787 0.419 11.07735 ? 24  TYR A CA  1 
ATOM   169  C  C   A TYR A 1 129 ? 58.95239 55.43062 13.96014 0.581 10.65662 ? 24  TYR A C   1 
ATOM   170  C  C   B TYR A 1 129 ? 58.95102 55.44312 13.95109 0.419 10.67094 ? 24  TYR A C   1 
ATOM   171  O  O   A TYR A 1 129 ? 59.08013 54.38880 14.60219 0.581 12.97196 ? 24  TYR A O   1 
ATOM   172  O  O   B TYR A 1 129 ? 59.12596 54.38655 14.55979 0.419 12.83081 ? 24  TYR A O   1 
ATOM   173  C  CB  A TYR A 1 129 ? 61.31231 56.06959 13.42665 0.581 11.57985 ? 24  TYR A CB  1 
ATOM   174  C  CB  B TYR A 1 129 ? 61.21911 56.18883 13.29960 0.419 12.26947 ? 24  TYR A CB  1 
ATOM   175  C  CG  A TYR A 1 129 ? 62.53617 56.99280 13.59811 0.581 9.81190  ? 24  TYR A CG  1 
ATOM   176  C  CG  B TYR A 1 129 ? 62.19003 57.32466 13.08990 0.419 11.86522 ? 24  TYR A CG  1 
ATOM   177  C  CD1 A TYR A 1 129 ? 62.77648 58.04128 12.71277 0.581 20.72169 ? 24  TYR A CD1 1 
ATOM   178  C  CD1 B TYR A 1 129 ? 61.96871 58.30807 12.11766 0.419 10.79488 ? 24  TYR A CD1 1 
ATOM   179  C  CD2 A TYR A 1 129 ? 63.47937 56.76582 14.60836 0.581 11.40823 ? 24  TYR A CD2 1 
ATOM   180  C  CD2 B TYR A 1 129 ? 63.36008 57.38383 13.82359 0.419 12.56306 ? 24  TYR A CD2 1 
ATOM   181  C  CE1 A TYR A 1 129 ? 63.88868 58.85466 12.84515 0.581 18.01986 ? 24  TYR A CE1 1 
ATOM   182  C  CE1 B TYR A 1 129 ? 62.87353 59.33258 11.93416 0.419 15.45950 ? 24  TYR A CE1 1 
ATOM   183  C  CE2 A TYR A 1 129 ? 64.61540 57.59866 14.74508 0.581 15.83804 ? 24  TYR A CE2 1 
ATOM   184  C  CE2 B TYR A 1 129 ? 64.26657 58.40441 13.64890 0.419 15.76313 ? 24  TYR A CE2 1 
ATOM   185  C  CZ  A TYR A 1 129 ? 64.80722 58.63359 13.86062 0.581 15.46177 ? 24  TYR A CZ  1 
ATOM   186  C  CZ  B TYR A 1 129 ? 64.02405 59.37392 12.70130 0.419 16.90614 ? 24  TYR A CZ  1 
ATOM   187  O  OH  A TYR A 1 129 ? 65.91279 59.47617 13.94473 0.581 17.24028 ? 24  TYR A OH  1 
ATOM   188  O  OH  B TYR A 1 129 ? 64.94103 60.38004 12.52667 0.419 21.60191 ? 24  TYR A OH  1 
ATOM   189  N  N   . TYR A 1 130 ? 57.91682 55.66335 13.14576 1.000 8.87813  ? 25  TYR A N   1 
ATOM   190  C  CA  . TYR A 1 130 ? 56.83841 54.67354 13.03496 1.000 9.83289  ? 25  TYR A CA  1 
ATOM   191  C  C   . TYR A 1 130 ? 56.10268 54.83991 11.71678 1.000 10.97711 ? 25  TYR A C   1 
ATOM   192  O  O   . TYR A 1 130 ? 56.12836 55.90744 11.10743 1.000 11.43926 ? 25  TYR A O   1 
ATOM   193  C  CB  . TYR A 1 130 ? 55.86178 54.80134 14.23632 1.000 10.24834 ? 25  TYR A CB  1 
ATOM   194  C  CG  . TYR A 1 130 ? 55.13193 56.13051 14.30541 1.000 9.98587  ? 25  TYR A CG  1 
ATOM   195  C  CD1 . TYR A 1 130 ? 55.76077 57.25208 14.84565 1.000 9.67145  ? 25  TYR A CD1 1 
ATOM   196  C  CD2 . TYR A 1 130 ? 53.83289 56.28581 13.77860 1.000 8.93555  ? 25  TYR A CD2 1 
ATOM   197  C  CE1 . TYR A 1 130 ? 55.11716 58.48317 14.85700 1.000 10.07001 ? 25  TYR A CE1 1 
ATOM   198  C  CE2 . TYR A 1 130 ? 53.16333 57.51585 13.81206 1.000 9.69796  ? 25  TYR A CE2 1 
ATOM   199  C  CZ  . TYR A 1 130 ? 53.81525 58.60424 14.38051 1.000 12.74357 ? 25  TYR A CZ  1 
ATOM   200  O  OH  . TYR A 1 130 ? 53.18406 59.83106 14.41606 1.000 18.43505 ? 25  TYR A OH  1 
ATOM   201  N  N   . ASP A 1 131 ? 55.49597 53.75054 11.25478 1.000 8.81228  ? 26  ASP A N   1 
ATOM   202  C  CA  . ASP A 1 131 ? 54.65842 53.81600 10.07162 1.000 10.17637 ? 26  ASP A CA  1 
ATOM   203  C  C   . ASP A 1 131 ? 53.35184 54.56157 10.36081 1.000 9.16193  ? 26  ASP A C   1 
ATOM   204  O  O   . ASP A 1 131 ? 52.68752 54.29997 11.38183 1.000 11.23491 ? 26  ASP A O   1 
ATOM   205  C  CB  . ASP A 1 131 ? 54.33532 52.38881 9.58362  1.000 11.33450 ? 26  ASP A CB  1 
ATOM   206  C  CG  . ASP A 1 131 ? 53.66634 52.38906 8.21936  1.000 14.08331 ? 26  ASP A CG  1 
ATOM   207  O  OD1 . ASP A 1 131 ? 54.40782 52.37327 7.20151  1.000 20.71626 ? 26  ASP A OD1 1 
ATOM   208  O  OD2 . ASP A 1 131 ? 52.41092 52.38897 8.13738  1.000 14.46314 ? 26  ASP A OD2 1 
ATOM   209  N  N   . GLU A 1 132 ? 52.96006 55.42353 9.38660  1.000 12.66288 ? 27  GLU A N   1 
ATOM   210  C  CA  . GLU A 1 132 ? 51.76676 56.27567 9.46576  1.000 12.93290 ? 27  GLU A CA  1 
ATOM   211  C  C   . GLU A 1 132 ? 50.47997 55.50045 9.76849  1.000 12.68989 ? 27  GLU A C   1 
ATOM   212  O  O   . GLU A 1 132 ? 49.51698 56.08763 10.27886 1.000 14.24206 ? 27  GLU A O   1 
ATOM   213  C  CB  . GLU A 1 132 ? 51.51179 57.02658 8.12616  1.000 20.09942 ? 27  GLU A CB  1 
ATOM   214  C  CG  . GLU A 1 132 ? 52.41959 58.17296 7.58994  1.000 43.00160 ? 27  GLU A CG  1 
ATOM   215  C  CD  . GLU A 1 132 ? 53.94746 57.94098 7.58360  1.000 58.39299 ? 27  GLU A CD  1 
ATOM   216  O  OE1 . GLU A 1 132 ? 54.41764 56.78579 7.45434  1.000 26.90427 ? 27  GLU A OE1 1 
ATOM   217  O  OE2 . GLU A 1 132 ? 54.69206 58.94918 7.62996  1.000 38.04900 ? 27  GLU A OE2 1 
ATOM   218  N  N   . SER A 1 133 ? 50.41022 54.20654 9.40987  1.000 12.24441 ? 28  SER A N   1 
ATOM   219  C  CA  . SER A 1 133 ? 49.18590 53.44870 9.66139  1.000 9.68518  ? 28  SER A CA  1 
ATOM   220  C  C   . SER A 1 133 ? 48.85011 53.42748 11.14420 1.000 12.29390 ? 28  SER A C   1 
ATOM   221  O  O   . SER A 1 133 ? 47.66988 53.43774 11.52329 1.000 11.43938 ? 28  SER A O   1 
ATOM   222  C  CB  . SER A 1 133 ? 49.32585 52.02507 9.11081  1.000 10.30358 ? 28  SER A CB  1 
ATOM   223  O  OG  . SER A 1 133 ? 50.46197 51.37399 9.66335  1.000 13.16903 ? 28  SER A OG  1 
ATOM   224  N  N   . ALA A 1 134 ? 49.87896 53.38014 11.99547 1.000 9.70680  ? 29  ALA A N   1 
ATOM   225  C  CA  . ALA A 1 134 ? 49.75660 53.64689 13.43932 1.000 7.53735  ? 29  ALA A CA  1 
ATOM   226  C  C   . ALA A 1 134 ? 48.66900 52.82262 14.14410 1.000 9.17177  ? 29  ALA A C   1 
ATOM   227  O  O   . ALA A 1 134 ? 48.01338 53.29835 15.06209 1.000 10.78808 ? 29  ALA A O   1 
ATOM   228  C  CB  . ALA A 1 134 ? 49.51708 55.14213 13.69551 1.000 11.35156 ? 29  ALA A CB  1 
ATOM   229  N  N   . GLY A 1 135 ? 48.49920 51.54241 13.77338 1.000 7.10352  ? 30  GLY A N   1 
ATOM   230  C  CA  . GLY A 1 135 ? 47.51767 50.75551 14.48447 1.000 7.77542  ? 30  GLY A CA  1 
ATOM   231  C  C   . GLY A 1 135 ? 46.07216 50.97650 14.08836 1.000 8.26277  ? 30  GLY A C   1 
ATOM   232  O  O   . GLY A 1 135 ? 45.18015 50.39955 14.75012 1.000 9.32253  ? 30  GLY A O   1 
ATOM   233  N  N   . GLN A 1 136 ? 45.81193 51.73889 13.02519 1.000 10.26439 ? 31  GLN A N   1 
ATOM   234  C  CA  . GLN A 1 136 ? 44.43741 51.95115 12.57145 1.000 7.94848  ? 31  GLN A CA  1 
ATOM   235  C  C   . GLN A 1 136 ? 43.79739 50.61873 12.21598 1.000 13.08412 ? 31  GLN A C   1 
ATOM   236  O  O   . GLN A 1 136 ? 44.39036 49.82013 11.48912 1.000 14.60565 ? 31  GLN A O   1 
ATOM   237  C  CB  . GLN A 1 136 ? 44.40332 52.86624 11.35537 1.000 12.73211 ? 31  GLN A CB  1 
ATOM   238  C  CG  . GLN A 1 136 ? 43.06784 53.61574 11.26045 1.000 21.23041 ? 31  GLN A CG  1 
ATOM   239  C  CD  . GLN A 1 136 ? 43.03989 54.59178 10.09503 1.000 46.26015 ? 31  GLN A CD  1 
ATOM   240  O  OE1 . GLN A 1 136 ? 44.07927 55.09148 9.66812  1.000 57.58888 ? 31  GLN A OE1 1 
ATOM   241  N  NE2 . GLN A 1 136 ? 41.84556 54.87880 9.58861  1.000 64.45600 ? 31  GLN A NE2 1 
ATOM   242  N  N   . GLY A 1 137 ? 42.56505 50.40860 12.68673 1.000 7.94420  ? 32  GLY A N   1 
ATOM   243  C  CA  . GLY A 1 137 ? 41.85842 49.16343 12.40403 1.000 11.23649 ? 32  GLY A CA  1 
ATOM   244  C  C   . GLY A 1 137 ? 42.04169 48.06822 13.42188 1.000 10.78274 ? 32  GLY A C   1 
ATOM   245  O  O   . GLY A 1 137 ? 41.32645 47.05790 13.35446 1.000 9.93153  ? 32  GLY A O   1 
ATOM   246  N  N   . SER A 1 138 ? 42.95804 48.23082 14.37511 1.000 8.55740  ? 33  SER A N   1 
ATOM   247  C  CA  . SER A 1 138 ? 43.10942 47.31896 15.50240 1.000 6.83841  ? 33  SER A CA  1 
ATOM   248  C  C   . SER A 1 138 ? 42.38861 47.87925 16.73240 1.000 7.77801  ? 33  SER A C   1 
ATOM   249  O  O   . SER A 1 138 ? 41.98319 49.06423 16.78077 1.000 8.91961  ? 33  SER A O   1 
ATOM   250  C  CB  . SER A 1 138 ? 44.58634 47.08552 15.84294 1.000 8.28268  ? 33  SER A CB  1 
ATOM   251  O  OG  . SER A 1 138 ? 45.12819 48.25915 16.41061 1.000 9.76436  ? 33  SER A OG  1 
ATOM   252  N  N   . CYS A 1 139 ? 42.17056 46.99099 17.70577 1.000 5.96828  ? 34  CYS A N   1 
ATOM   253  C  CA  . CYS A 1 139 ? 41.51425 47.36193 18.94607 1.000 6.40937  ? 34  CYS A CA  1 
ATOM   254  C  C   . CYS A 1 139 ? 42.31823 46.86646 20.13420 1.000 6.96740  ? 34  CYS A C   1 
ATOM   255  O  O   . CYS A 1 139 ? 42.78721 45.72475 20.13728 1.000 9.27598  ? 34  CYS A O   1 
ATOM   256  C  CB  . CYS A 1 139 ? 40.11510 46.77781 19.03630 1.000 8.01557  ? 34  CYS A CB  1 
ATOM   257  S  SG  . CYS A 1 139 ? 39.03080 47.33256 17.68999 1.000 10.24961 ? 34  CYS A SG  1 
ATOM   258  N  N   . VAL A 1 140 ? 42.41696 47.69015 21.18200 1.000 5.17065  ? 35  VAL A N   1 
ATOM   259  C  CA  . VAL A 1 140 ? 43.13055 47.26004 22.39355 1.000 5.58570  ? 35  VAL A CA  1 
ATOM   260  C  C   . VAL A 1 140 ? 42.21454 47.45267 23.57960 1.000 6.40877  ? 35  VAL A C   1 
ATOM   261  O  O   . VAL A 1 140 ? 41.78074 48.57822 23.85093 1.000 7.80360  ? 35  VAL A O   1 
ATOM   262  C  CB  . VAL A 1 140 ? 44.44271 48.04019 22.61329 1.000 5.07736  ? 35  VAL A CB  1 
ATOM   263  C  CG1 . VAL A 1 140 ? 45.16209 47.54703 23.87537 1.000 7.00602  ? 35  VAL A CG1 1 
ATOM   264  C  CG2 . VAL A 1 140 ? 45.37535 47.90521 21.36008 1.000 5.52331  ? 35  VAL A CG2 1 
ATOM   265  N  N   . TYR A 1 141 ? 41.97703 46.36363 24.32855 1.000 5.63490  ? 36  TYR A N   1 
ATOM   266  C  CA  . TYR A 1 141 ? 41.24779 46.43576 25.59677 1.000 4.74677  ? 36  TYR A CA  1 
ATOM   267  C  C   . TYR A 1 141 ? 42.23536 46.67788 26.71503 1.000 8.29087  ? 36  TYR A C   1 
ATOM   268  O  O   . TYR A 1 141 ? 43.22243 45.96257 26.83228 1.000 6.93276  ? 36  TYR A O   1 
ATOM   269  C  CB  . TYR A 1 141 ? 40.49702 45.12846 25.85791 1.000 5.23613  ? 36  TYR A CB  1 
ATOM   270  C  CG  . TYR A 1 141 ? 39.28552 44.90289 25.00346 1.000 6.07199  ? 36  TYR A CG  1 
ATOM   271  C  CD1 . TYR A 1 141 ? 39.41041 44.39374 23.68691 1.000 5.73845  ? 36  TYR A CD1 1 
ATOM   272  C  CD2 . TYR A 1 141 ? 38.00640 45.14715 25.51331 1.000 5.39973  ? 36  TYR A CD2 1 
ATOM   273  C  CE1 . TYR A 1 141 ? 38.28317 44.16768 22.89706 1.000 8.10594  ? 36  TYR A CE1 1 
ATOM   274  C  CE2 . TYR A 1 141 ? 36.86334 44.88540 24.74180 1.000 5.74988  ? 36  TYR A CE2 1 
ATOM   275  C  CZ  . TYR A 1 141 ? 37.01556 44.41854 23.42831 1.000 6.62201  ? 36  TYR A CZ  1 
ATOM   276  O  OH  . TYR A 1 141 ? 35.87429 44.15223 22.69041 1.000 9.66982  ? 36  TYR A OH  1 
ATOM   277  N  N   . VAL A 1 142 ? 41.99168 47.69782 27.52744 1.000 4.60276  ? 37  VAL A N   1 
ATOM   278  C  CA  . VAL A 1 142 ? 42.85304 47.99204 28.68266 1.000 4.48747  ? 37  VAL A CA  1 
ATOM   279  C  C   . VAL A 1 142 ? 42.05303 47.59887 29.91426 1.000 5.65965  ? 37  VAL A C   1 
ATOM   280  O  O   . VAL A 1 142 ? 41.02107 48.20131 30.20152 1.000 7.15957  ? 37  VAL A O   1 
ATOM   281  C  CB  . VAL A 1 142 ? 43.26577 49.47785 28.71925 1.000 7.24422  ? 37  VAL A CB  1 
ATOM   282  C  CG1 . VAL A 1 142 ? 44.20776 49.77887 29.91887 1.000 10.74991 ? 37  VAL A CG1 1 
ATOM   283  C  CG2 . VAL A 1 142 ? 43.96107 49.88022 27.43168 1.000 11.54278 ? 37  VAL A CG2 1 
ATOM   284  N  N   . ILE A 1 143 ? 42.48722 46.53658 30.60460 1.000 4.62862  ? 38  ILE A N   1 
ATOM   285  C  CA  . ILE A 1 143 ? 41.74093 45.92759 31.69440 1.000 5.21865  ? 38  ILE A CA  1 
ATOM   286  C  C   . ILE A 1 143 ? 42.40730 46.41220 32.97715 1.000 5.76744  ? 38  ILE A C   1 
ATOM   287  O  O   . ILE A 1 143 ? 43.50842 45.97928 33.30906 1.000 7.00466  ? 38  ILE A O   1 
ATOM   288  C  CB  . ILE A 1 143 ? 41.74752 44.39741 31.54918 1.000 6.52979  ? 38  ILE A CB  1 
ATOM   289  C  CG1 . ILE A 1 143 ? 41.21155 44.01019 30.16254 1.000 10.52671 ? 38  ILE A CG1 1 
ATOM   290  C  CG2 . ILE A 1 143 ? 40.99718 43.69421 32.71165 1.000 8.54405  ? 38  ILE A CG2 1 
ATOM   291  C  CD1 . ILE A 1 143 ? 41.34265 42.47592 29.86414 1.000 12.78804 ? 38  ILE A CD1 1 
ATOM   292  N  N   . ASP A 1 144 ? 41.78304 47.37340 33.66759 1.000 5.02266  ? 39  ASP A N   1 
ATOM   293  C  CA  . ASP A 1 144 ? 42.52950 48.16675 34.65316 1.000 5.10550  ? 39  ASP A CA  1 
ATOM   294  C  C   . ASP A 1 144 ? 41.55721 48.97379 35.51687 1.000 6.48623  ? 39  ASP A C   1 
ATOM   295  O  O   . ASP A 1 144 ? 40.46358 48.47528 35.81240 1.000 6.60167  ? 39  ASP A O   1 
ATOM   296  C  CB  . ASP A 1 144 ? 43.54891 49.06029 33.91177 1.000 5.76433  ? 39  ASP A CB  1 
ATOM   297  C  CG  . ASP A 1 144 ? 44.76131 49.37154 34.71797 1.000 8.77490  ? 39  ASP A CG  1 
ATOM   298  O  OD1 . ASP A 1 144 ? 44.62958 50.11879 35.71310 1.000 7.51195  ? 39  ASP A OD1 1 
ATOM   299  O  OD2 . ASP A 1 144 ? 45.87711 48.88570 34.35346 1.000 12.50391 ? 39  ASP A OD2 1 
ATOM   300  N  N   . THR A 1 145 ? 41.94352 50.18006 35.96657 1.000 5.92041  ? 40  THR A N   1 
ATOM   301  C  CA  . THR A 1 145 ? 41.06307 51.02392 36.80303 1.000 6.05421  ? 40  THR A CA  1 
ATOM   302  C  C   . THR A 1 145 ? 40.07515 51.85164 35.98725 1.000 6.92722  ? 40  THR A C   1 
ATOM   303  O  O   . THR A 1 145 ? 39.35153 52.66024 36.58349 1.000 7.33938  ? 40  THR A O   1 
ATOM   304  C  CB  . THR A 1 145 ? 41.87115 51.99351 37.69519 1.000 6.24644  ? 40  THR A CB  1 
ATOM   305  O  OG1 . THR A 1 145 ? 42.59472 52.88372 36.80255 1.000 7.74778  ? 40  THR A OG1 1 
ATOM   306  C  CG2 . THR A 1 145 ? 42.84110 51.21737 38.60329 1.000 10.50277 ? 40  THR A CG2 1 
ATOM   307  N  N   . GLY A 1 146 ? 40.03734 51.68189 34.66194 1.000 6.99226  ? 41  GLY A N   1 
ATOM   308  C  CA  . GLY A 1 146 ? 39.22994 52.52075 33.79306 1.000 7.83284  ? 41  GLY A CA  1 
ATOM   309  C  C   . GLY A 1 146 ? 40.09717 53.41998 32.92799 1.000 7.36422  ? 41  GLY A C   1 
ATOM   310  O  O   . GLY A 1 146 ? 41.32448 53.40486 32.99316 1.000 10.00815 ? 41  GLY A O   1 
ATOM   311  N  N   . ILE A 1 147 ? 39.43611 54.20406 32.09106 1.000 6.79076  ? 42  ILE A N   1 
ATOM   312  C  CA  . ILE A 1 147 ? 40.10870 55.15213 31.19242 1.000 6.11333  ? 42  ILE A CA  1 
ATOM   313  C  C   . ILE A 1 147 ? 39.31916 56.45088 31.23865 1.000 8.54104  ? 42  ILE A C   1 
ATOM   314  O  O   . ILE A 1 147 ? 38.08960 56.44320 31.04180 1.000 9.43828  ? 42  ILE A O   1 
ATOM   315  C  CB  . ILE A 1 147 ? 40.17103 54.68272 29.72014 1.000 9.06010  ? 42  ILE A CB  1 
ATOM   316  C  CG1 . ILE A 1 147 ? 40.80475 53.30443 29.58823 1.000 7.70734  ? 42  ILE A CG1 1 
ATOM   317  C  CG2 . ILE A 1 147 ? 40.97854 55.72816 28.86335 1.000 10.95817 ? 42  ILE A CG2 1 
ATOM   318  C  CD1 . ILE A 1 147 ? 40.73492 52.78851 28.10982 1.000 9.17152  ? 42  ILE A CD1 1 
ATOM   319  N  N   . GLU A 1 148 ? 40.01377 57.57003 31.43915 1.000 6.74244  ? 43  GLU A N   1 
ATOM   320  C  CA  . GLU A 1 148 ? 39.36464 58.87552 31.28023 1.000 7.25849  ? 43  GLU A CA  1 
ATOM   321  C  C   . GLU A 1 148 ? 39.22669 59.16368 29.78386 1.000 9.57490  ? 43  GLU A C   1 
ATOM   322  O  O   . GLU A 1 148 ? 40.08193 59.81740 29.14661 1.000 10.14198 ? 43  GLU A O   1 
ATOM   323  C  CB  . GLU A 1 148 ? 40.14707 59.97190 31.98597 1.000 8.63586  ? 43  GLU A CB  1 
ATOM   324  C  CG  . GLU A 1 148 ? 39.42362 61.33936 32.00907 1.000 8.09958  ? 43  GLU A CG  1 
ATOM   325  C  CD  . GLU A 1 148 ? 40.19467 62.33851 32.83449 1.000 11.58982 ? 43  GLU A CD  1 
ATOM   326  O  OE1 . GLU A 1 148 ? 40.00814 62.31244 34.06824 1.000 12.87513 ? 43  GLU A OE1 1 
ATOM   327  O  OE2 . GLU A 1 148 ? 40.97615 63.11786 32.22284 1.000 12.72222 ? 43  GLU A OE2 1 
ATOM   328  N  N   . ALA A 1 149 ? 38.10293 58.67712 29.21883 1.000 9.38471  ? 44  ALA A N   1 
ATOM   329  C  CA  . ALA A 1 149 ? 37.94791 58.69817 27.76147 1.000 12.03635 ? 44  ALA A CA  1 
ATOM   330  C  C   . ALA A 1 149 ? 37.87118 60.10298 27.18555 1.000 12.82970 ? 44  ALA A C   1 
ATOM   331  O  O   . ALA A 1 149 ? 38.17225 60.28095 26.00115 1.000 17.63593 ? 44  ALA A O   1 
ATOM   332  C  CB  . ALA A 1 149 ? 36.70549 57.89684 27.36555 1.000 16.73479 ? 44  ALA A CB  1 
ATOM   333  N  N   . SER A 1 150 ? 37.51062 61.10613 27.98938 1.000 9.49590  ? 45  SER A N   1 
ATOM   334  C  CA  . SER A 1 150 ? 37.41037 62.49444 27.54595 1.000 9.41465  ? 45  SER A CA  1 
ATOM   335  C  C   . SER A 1 150 ? 38.75318 63.20312 27.44378 1.000 10.84783 ? 45  SER A C   1 
ATOM   336  O  O   . SER A 1 150 ? 38.78333 64.36917 27.02448 1.000 11.90223 ? 45  SER A O   1 
ATOM   337  C  CB  . SER A 1 150 ? 36.47589 63.25968 28.48552 1.000 13.51518 ? 45  SER A CB  1 
ATOM   338  O  OG  . SER A 1 150 ? 37.08406 63.39879 29.75850 1.000 19.17820 ? 45  SER A OG  1 
ATOM   339  N  N   . HIS A 1 151 ? 39.85769 62.56194 27.87982 1.000 9.91935  ? 46  HIS A N   1 
ATOM   340  C  CA  . HIS A 1 151 ? 41.14469 63.22781 27.80520 1.000 8.93236  ? 46  HIS A CA  1 
ATOM   341  C  C   . HIS A 1 151 ? 41.42263 63.62002 26.35321 1.000 9.63377  ? 46  HIS A C   1 
ATOM   342  O  O   . HIS A 1 151 ? 41.30622 62.77072 25.46094 1.000 9.86444  ? 46  HIS A O   1 
ATOM   343  C  CB  . HIS A 1 151 ? 42.22996 62.28254 28.30749 1.000 8.03779  ? 46  HIS A CB  1 
ATOM   344  C  CG  . HIS A 1 151 ? 43.50995 62.97488 28.69849 1.000 10.48120 ? 46  HIS A CG  1 
ATOM   345  N  ND1 . HIS A 1 151 ? 44.26423 63.71881 27.80374 1.000 9.21546  ? 46  HIS A ND1 1 
ATOM   346  C  CD2 . HIS A 1 151 ? 44.16785 63.02769 29.88887 1.000 10.22563 ? 46  HIS A CD2 1 
ATOM   347  C  CE1 . HIS A 1 151 ? 45.32461 64.19741 28.42680 1.000 10.41628 ? 46  HIS A CE1 1 
ATOM   348  N  NE2 . HIS A 1 151 ? 45.28180 63.80320 29.69104 1.000 9.52737  ? 46  HIS A NE2 1 
ATOM   349  N  N   . PRO A 1 152 ? 41.81112 64.86798 26.08005 1.000 9.74735  ? 47  PRO A N   1 
ATOM   350  C  CA  . PRO A 1 152 ? 42.05880 65.28659 24.68069 1.000 9.07720  ? 47  PRO A CA  1 
ATOM   351  C  C   . PRO A 1 152 ? 43.04663 64.40873 23.95035 1.000 8.73191  ? 47  PRO A C   1 
ATOM   352  O  O   . PRO A 1 152 ? 42.94543 64.26872 22.72180 1.000 10.37086 ? 47  PRO A O   1 
ATOM   353  C  CB  . PRO A 1 152 ? 42.59733 66.71761 24.83884 1.000 14.23645 ? 47  PRO A CB  1 
ATOM   354  C  CG  . PRO A 1 152 ? 42.03229 67.19023 26.10931 1.000 15.23859 ? 47  PRO A CG  1 
ATOM   355  C  CD  . PRO A 1 152 ? 41.91560 65.99948 27.02900 1.000 9.64993  ? 47  PRO A CD  1 
ATOM   356  N  N   . GLU A 1 153 ? 43.96638 63.76286 24.66286 1.000 8.26296  ? 48  GLU A N   1 
ATOM   357  C  CA  . GLU A 1 153 ? 44.99386 62.96650 24.01454 1.000 7.70747  ? 48  GLU A CA  1 
ATOM   358  C  C   . GLU A 1 153 ? 44.45253 61.70042 23.39383 1.000 7.40763  ? 48  GLU A C   1 
ATOM   359  O  O   . GLU A 1 153 ? 45.15650 61.09137 22.59086 1.000 8.55847  ? 48  GLU A O   1 
ATOM   360  C  CB  . GLU A 1 153 ? 46.07796 62.60986 25.02877 1.000 7.74438  ? 48  GLU A CB  1 
ATOM   361  C  CG  . GLU A 1 153 ? 47.05646 63.74640 25.27015 1.000 10.10961 ? 48  GLU A CG  1 
ATOM   362  C  CD  . GLU A 1 153 ? 48.11145 63.75400 24.21162 1.000 17.38127 ? 48  GLU A CD  1 
ATOM   363  O  OE1 . GLU A 1 153 ? 48.36362 62.66264 23.66094 1.000 19.06696 ? 48  GLU A OE1 1 
ATOM   364  O  OE2 . GLU A 1 153 ? 48.65332 64.82095 23.92194 1.000 19.57810 ? 48  GLU A OE2 1 
ATOM   365  N  N   . PHE A 1 154 ? 43.21457 61.30744 23.70374 1.000 7.42876  ? 49  PHE A N   1 
ATOM   366  C  CA  . PHE A 1 154 ? 42.67886 60.11242 23.05655 1.000 7.54723  ? 49  PHE A CA  1 
ATOM   367  C  C   . PHE A 1 154 ? 41.87227 60.44160 21.80789 1.000 8.55060  ? 49  PHE A C   1 
ATOM   368  O  O   . PHE A 1 154 ? 41.52842 59.51261 21.06903 1.000 8.33351  ? 49  PHE A O   1 
ATOM   369  C  CB  . PHE A 1 154 ? 41.79926 59.30817 24.02896 1.000 7.00239  ? 49  PHE A CB  1 
ATOM   370  C  CG  . PHE A 1 154 ? 42.56411 58.73501 25.18408 1.000 7.30983  ? 49  PHE A CG  1 
ATOM   371  C  CD1 . PHE A 1 154 ? 43.62648 57.88146 24.95285 1.000 9.03318  ? 49  PHE A CD1 1 
ATOM   372  C  CD2 . PHE A 1 154 ? 42.24099 59.08058 26.47983 1.000 6.63553  ? 49  PHE A CD2 1 
ATOM   373  C  CE1 . PHE A 1 154 ? 44.37029 57.34792 26.02432 1.000 9.61245  ? 49  PHE A CE1 1 
ATOM   374  C  CE2 . PHE A 1 154 ? 42.95732 58.54684 27.56588 1.000 9.43542  ? 49  PHE A CE2 1 
ATOM   375  C  CZ  . PHE A 1 154 ? 44.04403 57.68688 27.32606 1.000 7.59941  ? 49  PHE A CZ  1 
ATOM   376  N  N   . GLU A 1 155 ? 41.54047 61.71929 21.55495 1.000 8.23772  ? 50  GLU A N   1 
ATOM   377  C  CA  . GLU A 1 155 ? 40.96151 62.16650 20.27169 1.000 8.79086  ? 50  GLU A CA  1 
ATOM   378  C  C   . GLU A 1 155 ? 39.65387 61.46187 19.93800 1.000 9.81552  ? 50  GLU A C   1 
ATOM   379  O  O   . GLU A 1 155 ? 39.33460 61.26655 18.76844 1.000 13.85118 ? 50  GLU A O   1 
ATOM   380  C  CB  . GLU A 1 155 ? 41.95774 61.98631 19.12107 1.000 11.68571 ? 50  GLU A CB  1 
ATOM   381  C  CG  . GLU A 1 155 ? 43.33170 62.59803 19.37060 1.000 14.39137 ? 50  GLU A CG  1 
ATOM   382  C  CD  . GLU A 1 155 ? 44.29326 62.30618 18.23692 1.000 16.92192 ? 50  GLU A CD  1 
ATOM   383  O  OE1 . GLU A 1 155 ? 44.56942 61.12530 17.99986 1.000 13.74422 ? 50  GLU A OE1 1 
ATOM   384  O  OE2 . GLU A 1 155 ? 44.73521 63.24868 17.52307 1.000 16.11315 ? 50  GLU A OE2 1 
ATOM   385  N  N   . GLY A 1 156 ? 38.91584 61.03895 20.95160 1.000 10.45827 ? 51  GLY A N   1 
ATOM   386  C  CA  . GLY A 1 156 ? 37.65228 60.36144 20.70982 1.000 11.95160 ? 51  GLY A CA  1 
ATOM   387  C  C   . GLY A 1 156 ? 37.79113 58.88648 20.42540 1.000 12.03045 ? 51  GLY A C   1 
ATOM   388  O  O   . GLY A 1 156 ? 36.77446 58.22977 20.11312 1.000 12.57700 ? 51  GLY A O   1 
ATOM   389  N  N   . ARG A 1 157 ? 39.00367 58.35415 20.47956 1.000 8.37709  ? 52  ARG A N   1 
ATOM   390  C  CA  . ARG A 1 157 ? 39.24065 56.94667 20.13693 1.000 7.56333  ? 52  ARG A CA  1 
ATOM   391  C  C   . ARG A 1 157 ? 39.13782 55.99757 21.32679 1.000 11.08305 ? 52  ARG A C   1 
ATOM   392  O  O   . ARG A 1 157 ? 39.41474 54.79319 21.16629 1.000 11.58435 ? 52  ARG A O   1 
ATOM   393  C  CB  . ARG A 1 157 ? 40.62278 56.77470 19.50028 1.000 7.87221  ? 52  ARG A CB  1 
ATOM   394  C  CG  . ARG A 1 157 ? 40.70913 57.39509 18.11830 1.000 8.49154  ? 52  ARG A CG  1 
ATOM   395  C  CD  . ARG A 1 157 ? 42.11659 57.30735 17.52262 1.000 10.10447 ? 52  ARG A CD  1 
ATOM   396  N  NE  . ARG A 1 157 ? 43.06601 58.20667 18.19595 1.000 8.59945  ? 52  ARG A NE  1 
ATOM   397  C  CZ  . ARG A 1 157 ? 43.95921 57.79476 19.09583 1.000 9.23703  ? 52  ARG A CZ  1 
ATOM   398  N  NH1 . ARG A 1 157 ? 44.05140 56.51100 19.47627 1.000 8.51778  ? 52  ARG A NH1 1 
ATOM   399  N  NH2 . ARG A 1 157 ? 44.75957 58.69589 19.68555 1.000 8.65453  ? 52  ARG A NH2 1 
ATOM   400  N  N   . ALA A 1 158 ? 38.75267 56.48523 22.49617 1.000 9.76109  ? 53  ALA A N   1 
ATOM   401  C  CA  . ALA A 1 158 ? 38.69215 55.66144 23.71051 1.000 7.24101  ? 53  ALA A CA  1 
ATOM   402  C  C   . ALA A 1 158 ? 37.25435 55.62071 24.19815 1.000 9.88862  ? 53  ALA A C   1 
ATOM   403  O  O   . ALA A 1 158 ? 36.53148 56.63059 24.12921 1.000 12.55569 ? 53  ALA A O   1 
ATOM   404  C  CB  . ALA A 1 158 ? 39.60931 56.20450 24.84175 1.000 9.49754  ? 53  ALA A CB  1 
ATOM   405  N  N   . GLN A 1 159 ? 36.83079 54.45657 24.67762 1.000 9.03226  ? 54  GLN A N   1 
ATOM   406  C  CA  . GLN A 1 159 ? 35.52257 54.41894 25.31479 1.000 10.23387 ? 54  GLN A CA  1 
ATOM   407  C  C   . GLN A 1 159 ? 35.50062 53.33189 26.37402 1.000 9.91898  ? 54  GLN A C   1 
ATOM   408  O  O   . GLN A 1 159 ? 36.17837 52.30820 26.25188 1.000 11.19600 ? 54  GLN A O   1 
ATOM   409  C  CB  . GLN A 1 159 ? 34.45460 54.23141 24.25442 1.000 21.54942 ? 54  GLN A CB  1 
ATOM   410  C  CG  . GLN A 1 159 ? 34.30589 52.89176 23.75242 1.000 19.95009 ? 54  GLN A CG  1 
ATOM   411  C  CD  . GLN A 1 159 ? 33.21648 52.83458 22.69308 1.000 50.34313 ? 54  GLN A CD  1 
ATOM   412  O  OE1 . GLN A 1 159 ? 32.04846 52.55670 22.98235 1.000 52.99956 ? 54  GLN A OE1 1 
ATOM   413  N  NE2 . GLN A 1 159 ? 33.60518 53.09856 21.44712 1.000 37.89710 ? 54  GLN A NE2 1 
ATOM   414  N  N   . MET A 1 160 ? 34.72402 53.57672 27.42957 1.000 9.52274  ? 55  MET A N   1 
ATOM   415  C  CA  . MET A 1 160 ? 34.52695 52.52554 28.41582 1.000 7.44166  ? 55  MET A CA  1 
ATOM   416  C  C   . MET A 1 160 ? 33.42012 51.59980 27.96964 1.000 10.52422 ? 55  MET A C   1 
ATOM   417  O  O   . MET A 1 160 ? 32.35831 52.07513 27.52661 1.000 14.06549 ? 55  MET A O   1 
ATOM   418  C  CB  . MET A 1 160 ? 34.15967 53.06348 29.80374 1.000 8.44696  ? 55  MET A CB  1 
ATOM   419  C  CG  . MET A 1 160 ? 35.24186 53.91469 30.45255 1.000 9.65811  ? 55  MET A CG  1 
ATOM   420  S  SD  . MET A 1 160 ? 36.56243 52.81748 30.97678 1.000 10.10991 ? 55  MET A SD  1 
ATOM   421  C  CE  . MET A 1 160 ? 35.76135 51.71441 32.10504 1.000 10.93835 ? 55  MET A CE  1 
ATOM   422  N  N   . VAL A 1 161 ? 33.65796 50.28549 28.07650 1.000 8.34924  ? 56  VAL A N   1 
ATOM   423  C  CA  . VAL A 1 161 ? 32.66485 49.30635 27.66681 1.000 7.26553  ? 56  VAL A CA  1 
ATOM   424  C  C   . VAL A 1 161 ? 32.12416 48.47986 28.82788 1.000 8.29110  ? 56  VAL A C   1 
ATOM   425  O  O   . VAL A 1 161 ? 31.04969 47.87782 28.67526 1.000 12.68244 ? 56  VAL A O   1 
ATOM   426  C  CB  . VAL A 1 161 ? 33.19098 48.38607 26.54608 1.000 9.47401  ? 56  VAL A CB  1 
ATOM   427  C  CG1 . VAL A 1 161 ? 33.50028 49.21916 25.27518 1.000 14.46728 ? 56  VAL A CG1 1 
ATOM   428  C  CG2 . VAL A 1 161 ? 34.39438 47.59464 26.99578 1.000 13.99828 ? 56  VAL A CG2 1 
ATOM   429  N  N   . LYS A 1 162 ? 32.79069 48.45466 29.99655 1.000 8.13957  ? 57  LYS A N   1 
ATOM   430  C  CA  . LYS A 1 162 ? 32.29370 47.62497 31.09718 1.000 8.63173  ? 57  LYS A CA  1 
ATOM   431  C  C   . LYS A 1 162 ? 32.92574 48.07423 32.40012 1.000 8.29426  ? 57  LYS A C   1 
ATOM   432  O  O   . LYS A 1 162 ? 34.10703 48.36869 32.42372 1.000 9.36514  ? 57  LYS A O   1 
ATOM   433  C  CB  . LYS A 1 162 ? 32.65246 46.14331 30.82436 1.000 9.80241  ? 57  LYS A CB  1 
ATOM   434  C  CG  . LYS A 1 162 ? 32.26888 45.15663 31.93227 1.000 10.32890 ? 57  LYS A CG  1 
ATOM   435  C  CD  . LYS A 1 162 ? 30.76691 44.92800 31.93405 1.000 13.54019 ? 57  LYS A CD  1 
ATOM   436  C  CE  . LYS A 1 162 ? 30.41160 43.96953 33.04890 1.000 21.91391 ? 57  LYS A CE  1 
ATOM   437  N  NZ  . LYS A 1 162 ? 28.94492 43.75506 33.15595 1.000 28.37986 ? 57  LYS A NZ  1 
ATOM   438  N  N   . THR A 1 163 ? 32.13724 48.10223 33.47487 1.000 8.72505  ? 58  THR A N   1 
ATOM   439  C  CA  . THR A 1 163 ? 32.68393 48.30634 34.80739 1.000 8.20737  ? 58  THR A CA  1 
ATOM   440  C  C   . THR A 1 163 ? 32.08420 47.27627 35.76197 1.000 8.28040  ? 58  THR A C   1 
ATOM   441  O  O   . THR A 1 163 ? 30.94190 46.82263 35.58754 1.000 12.42996 ? 58  THR A O   1 
ATOM   442  C  CB  . THR A 1 163 ? 32.42529 49.74236 35.33103 1.000 8.15083  ? 58  THR A CB  1 
ATOM   443  O  OG1 . THR A 1 163 ? 33.00090 49.86867 36.63839 1.000 9.37293  ? 58  THR A OG1 1 
ATOM   444  C  CG2 . THR A 1 163 ? 30.92030 50.06691 35.42945 1.000 10.56296 ? 58  THR A CG2 1 
ATOM   445  N  N   . TYR A 1 164 ? 32.87301 46.92402 36.78084 1.000 8.06032  ? 59  TYR A N   1 
ATOM   446  C  CA  . TYR A 1 164 ? 32.43833 46.01925 37.83460 1.000 8.32391  ? 59  TYR A CA  1 
ATOM   447  C  C   . TYR A 1 164 ? 32.22987 46.75380 39.14113 1.000 9.12023  ? 59  TYR A C   1 
ATOM   448  O  O   . TYR A 1 164 ? 32.07780 46.11646 40.19834 1.000 12.36294 ? 59  TYR A O   1 
ATOM   449  C  CB  . TYR A 1 164 ? 33.44239 44.86109 37.99373 1.000 10.78304 ? 59  TYR A CB  1 
ATOM   450  C  CG  . TYR A 1 164 ? 33.39343 43.95536 36.79919 1.000 7.68512  ? 59  TYR A CG  1 
ATOM   451  C  CD1 . TYR A 1 164 ? 32.47663 42.90978 36.73857 1.000 13.39935 ? 59  TYR A CD1 1 
ATOM   452  C  CD2 . TYR A 1 164 ? 34.24993 44.15397 35.71084 1.000 7.97138  ? 59  TYR A CD2 1 
ATOM   453  C  CE1 . TYR A 1 164 ? 32.39225 42.08405 35.60559 1.000 11.78469 ? 59  TYR A CE1 1 
ATOM   454  C  CE2 . TYR A 1 164 ? 34.16022 43.34117 34.58169 1.000 9.23388  ? 59  TYR A CE2 1 
ATOM   455  C  CZ  . TYR A 1 164 ? 33.23638 42.30514 34.55052 1.000 10.52911 ? 59  TYR A CZ  1 
ATOM   456  O  OH  . TYR A 1 164 ? 33.14395 41.50011 33.43726 1.000 12.96549 ? 59  TYR A OH  1 
ATOM   457  N  N   . TYR A 1 165 ? 32.20905 48.09544 39.09996 1.000 10.85060 ? 60  TYR A N   1 
ATOM   458  C  CA  . TYR A 1 165 ? 31.97945 48.90685 40.28057 1.000 10.17420 ? 60  TYR A CA  1 
ATOM   459  C  C   . TYR A 1 165 ? 30.86187 49.91289 40.03119 1.000 11.81261 ? 60  TYR A C   1 
ATOM   460  O  O   . TYR A 1 165 ? 30.13592 49.80757 39.03108 1.000 15.68821 ? 60  TYR A O   1 
ATOM   461  C  CB  . TYR A 1 165 ? 33.27970 49.62004 40.67433 1.000 11.03366 ? 60  TYR A CB  1 
ATOM   462  C  CG  . TYR A 1 165 ? 34.35433 48.60223 40.95769 1.000 12.52550 ? 60  TYR A CG  1 
ATOM   463  C  CD1 . TYR A 1 165 ? 34.52511 48.08578 42.23667 1.000 14.13786 ? 60  TYR A CD1 1 
ATOM   464  C  CD2 . TYR A 1 165 ? 35.16613 48.13716 39.92923 1.000 17.36141 ? 60  TYR A CD2 1 
ATOM   465  C  CE1 . TYR A 1 165 ? 35.51270 47.09854 42.47947 1.000 17.66067 ? 60  TYR A CE1 1 
ATOM   466  C  CE2 . TYR A 1 165 ? 36.11809 47.17325 40.14665 1.000 14.13884 ? 60  TYR A CE2 1 
ATOM   467  C  CZ  . TYR A 1 165 ? 36.28260 46.66031 41.39882 1.000 12.42708 ? 60  TYR A CZ  1 
ATOM   468  O  OH  . TYR A 1 165 ? 37.26306 45.69095 41.55275 1.000 19.56429 ? 60  TYR A OH  1 
ATOM   469  N  N   . TYR A 1 166 ? 30.70462 50.87760 40.94530 1.000 10.39957 ? 61  TYR A N   1 
ATOM   470  C  CA  . TYR A 1 166 ? 29.52945 51.73979 40.89039 1.000 12.69938 ? 61  TYR A CA  1 
ATOM   471  C  C   . TYR A 1 166 ? 29.56164 52.68407 39.70833 1.000 14.61434 ? 61  TYR A C   1 
ATOM   472  O  O   . TYR A 1 166 ? 28.49779 53.08562 39.21940 1.000 19.06169 ? 61  TYR A O   1 
ATOM   473  C  CB  . TYR A 1 166 ? 29.40554 52.54256 42.17184 1.000 13.98292 ? 61  TYR A CB  1 
ATOM   474  C  CG  . TYR A 1 166 ? 29.56281 51.72018 43.40223 1.000 18.88251 ? 61  TYR A CG  1 
ATOM   475  C  CD1 . TYR A 1 166 ? 28.45963 51.06002 43.96494 1.000 18.18577 ? 61  TYR A CD1 1 
ATOM   476  C  CD2 . TYR A 1 166 ? 30.79875 51.61095 44.04136 1.000 19.92743 ? 61  TYR A CD2 1 
ATOM   477  C  CE1 . TYR A 1 166 ? 28.58986 50.29494 45.13370 1.000 16.68747 ? 61  TYR A CE1 1 
ATOM   478  C  CE2 . TYR A 1 166 ? 30.93564 50.83664 45.20255 1.000 20.03318 ? 61  TYR A CE2 1 
ATOM   479  C  CZ  . TYR A 1 166 ? 29.84385 50.18772 45.72984 1.000 23.62939 ? 61  TYR A CZ  1 
ATOM   480  O  OH  . TYR A 1 166 ? 30.02573 49.44133 46.87605 1.000 25.75215 ? 61  TYR A OH  1 
ATOM   481  N  N   A SER A 1 167 ? 30.76409 53.04702 39.25692 0.736 13.82109 ? 62  SER A N   1 
ATOM   482  N  N   B SER A 1 167 ? 30.74460 53.07428 39.23399 0.264 13.81989 ? 62  SER A N   1 
ATOM   483  C  CA  A SER A 1 167 ? 30.96251 53.97969 38.16356 0.736 13.98417 ? 62  SER A CA  1 
ATOM   484  C  CA  B SER A 1 167 ? 30.83327 53.93067 38.05819 0.264 13.30362 ? 62  SER A CA  1 
ATOM   485  C  C   A SER A 1 167 ? 31.97608 53.39531 37.19834 0.736 13.83352 ? 62  SER A C   1 
ATOM   486  C  C   B SER A 1 167 ? 31.84917 53.36356 37.08203 0.264 13.80567 ? 62  SER A C   1 
ATOM   487  O  O   A SER A 1 167 ? 32.76995 52.52322 37.56469 0.736 12.51180 ? 62  SER A O   1 
ATOM   488  O  O   B SER A 1 167 ? 32.58394 52.41898 37.38608 0.264 12.31690 ? 62  SER A O   1 
ATOM   489  C  CB  A SER A 1 167 ? 31.47116 55.32680 38.69727 0.736 17.42198 ? 62  SER A CB  1 
ATOM   490  C  CB  B SER A 1 167 ? 31.23262 55.37060 38.41454 0.264 18.27495 ? 62  SER A CB  1 
ATOM   491  O  OG  A SER A 1 167 ? 31.78967 56.21105 37.65623 0.736 13.98787 ? 62  SER A OG  1 
ATOM   492  O  OG  B SER A 1 167 ? 32.55607 55.42278 38.90331 0.264 12.40376 ? 62  SER A OG  1 
ATOM   493  N  N   A SER A 1 168 ? 31.93956 53.88110 35.95758 0.736 11.73201 ? 63  SER A N   1 
ATOM   494  N  N   B SER A 1 168 ? 31.88062 53.96976 35.89575 0.264 11.68987 ? 63  SER A N   1 
ATOM   495  C  CA  A SER A 1 168 ? 32.96712 53.54082 34.98808 0.736 10.87611 ? 63  SER A CA  1 
ATOM   496  C  CA  B SER A 1 168 ? 32.86992 53.65370 34.87924 0.264 11.57321 ? 63  SER A CA  1 
ATOM   497  C  C   A SER A 1 168 ? 34.13070 54.51948 34.98609 0.736 13.85511 ? 63  SER A C   1 
ATOM   498  C  C   B SER A 1 168 ? 34.08970 54.55953 34.93528 0.264 13.68958 ? 63  SER A C   1 
ATOM   499  O  O   A SER A 1 168 ? 35.10408 54.28566 34.26610 0.736 13.08080 ? 63  SER A O   1 
ATOM   500  O  O   B SER A 1 168 ? 35.04547 54.32636 34.18975 0.264 13.16901 ? 63  SER A O   1 
ATOM   501  C  CB  A SER A 1 168 ? 32.35933 53.46962 33.58434 0.736 14.94746 ? 63  SER A CB  1 
ATOM   502  C  CB  B SER A 1 168 ? 32.24252 53.75317 33.48513 0.264 13.85658 ? 63  SER A CB  1 
ATOM   503  O  OG  A SER A 1 168 ? 31.82224 54.72880 33.24556 0.736 17.87291 ? 63  SER A OG  1 
ATOM   504  O  OG  B SER A 1 168 ? 31.24500 52.76589 33.30499 0.264 12.14459 ? 63  SER A OG  1 
ATOM   505  N  N   . ARG A 1 169 ? 34.08918 55.56894 35.79914 1.000 10.38421 ? 64  ARG A N   1 
ATOM   506  C  CA  . ARG A 1 169 ? 35.18538 56.53562 35.82625 1.000 12.15692 ? 64  ARG A CA  1 
ATOM   507  C  C   . ARG A 1 169 ? 36.46790 55.94734 36.38936 1.000 11.83658 ? 64  ARG A C   1 
ATOM   508  O  O   . ARG A 1 169 ? 36.46366 55.17491 37.35797 1.000 11.82680 ? 64  ARG A O   1 
ATOM   509  C  CB  . ARG A 1 169 ? 34.82530 57.76044 36.67629 1.000 15.40588 ? 64  ARG A CB  1 
ATOM   510  C  CG  . ARG A 1 169 ? 33.74549 58.67033 36.09528 1.000 34.17092 ? 64  ARG A CG  1 
ATOM   511  C  CD  . ARG A 1 169 ? 33.42304 59.83945 37.06779 1.000 53.84827 ? 64  ARG A CD  1 
ATOM   512  N  NE  . ARG A 1 169 ? 34.62480 60.49940 37.59476 1.000 68.43924 ? 64  ARG A NE  1 
ATOM   513  C  CZ  . ARG A 1 169 ? 35.28589 60.16294 38.70091 1.000 65.88328 ? 64  ARG A CZ  1 
ATOM   514  N  NH1 . ARG A 1 169 ? 34.87148 59.18000 39.49025 1.000 68.41845 ? 64  ARG A NH1 1 
ATOM   515  N  NH2 . ARG A 1 169 ? 36.39452 60.83014 39.02379 1.000 53.49542 ? 64  ARG A NH2 1 
ATOM   516  N  N   . ASP A 1 170 ? 37.59134 56.38606 35.83493 1.000 8.81348  ? 65  ASP A N   1 
ATOM   517  C  CA  . ASP A 1 170 ? 38.88665 56.09818 36.43982 1.000 7.37727  ? 65  ASP A CA  1 
ATOM   518  C  C   . ASP A 1 170 ? 39.13925 57.11931 37.54816 1.000 10.16898 ? 65  ASP A C   1 
ATOM   519  O  O   . ASP A 1 170 ? 39.50426 58.27225 37.27989 1.000 10.32103 ? 65  ASP A O   1 
ATOM   520  C  CB  . ASP A 1 170 ? 39.97397 56.15379 35.37028 1.000 7.70402  ? 65  ASP A CB  1 
ATOM   521  C  CG  . ASP A 1 170 ? 41.36205 55.88577 35.93126 1.000 9.53438  ? 65  ASP A CG  1 
ATOM   522  O  OD1 . ASP A 1 170 ? 41.47491 55.43420 37.08679 1.000 8.14484  ? 65  ASP A OD1 1 
ATOM   523  O  OD2 . ASP A 1 170 ? 42.32646 56.10188 35.17184 1.000 9.13193  ? 65  ASP A OD2 1 
ATOM   524  N  N   . GLY A 1 171 ? 38.96266 56.70237 38.80324 1.000 8.08077  ? 66  GLY A N   1 
ATOM   525  C  CA  . GLY A 1 171 ? 39.24738 57.57821 39.92248 1.000 9.57816  ? 66  GLY A CA  1 
ATOM   526  C  C   . GLY A 1 171 ? 40.65498 57.44854 40.44410 1.000 8.35337  ? 66  GLY A C   1 
ATOM   527  O  O   . GLY A 1 171 ? 40.97419 58.02809 41.48907 1.000 13.12144 ? 66  GLY A O   1 
ATOM   528  N  N   . ASN A 1 172 ? 41.47484 56.63464 39.80067 1.000 8.31399  ? 67  ASN A N   1 
ATOM   529  C  CA  . ASN A 1 172 ? 42.82761 56.35848 40.24892 1.000 7.85159  ? 67  ASN A CA  1 
ATOM   530  C  C   . ASN A 1 172 ? 43.89189 57.01423 39.37405 1.000 10.36526 ? 67  ASN A C   1 
ATOM   531  O  O   . ASN A 1 172 ? 44.75014 57.76635 39.89120 1.000 10.36852 ? 67  ASN A O   1 
ATOM   532  C  CB  . ASN A 1 172 ? 43.05061 54.84150 40.29705 1.000 9.41747  ? 67  ASN A CB  1 
ATOM   533  C  CG  . ASN A 1 172 ? 44.42924 54.48303 40.79169 1.000 12.21220 ? 67  ASN A CG  1 
ATOM   534  O  OD1 . ASN A 1 172 ? 45.38307 54.42649 40.00891 1.000 11.23020 ? 67  ASN A OD1 1 
ATOM   535  N  ND2 . ASN A 1 172 ? 44.56591 54.27603 42.10492 1.000 13.95550 ? 67  ASN A ND2 1 
ATOM   536  N  N   . GLY A 1 173 ? 43.85507 56.77588 38.05642 1.000 8.62438  ? 68  GLY A N   1 
ATOM   537  C  CA  . GLY A 1 173 ? 44.85598 57.28177 37.13013 1.000 6.67864  ? 68  GLY A CA  1 
ATOM   538  C  C   . GLY A 1 173 ? 45.62185 56.17843 36.43038 1.000 6.17980  ? 68  GLY A C   1 
ATOM   539  O  O   . GLY A 1 173 ? 46.02314 56.34719 35.28822 1.000 7.15873  ? 68  GLY A O   1 
ATOM   540  N  N   . HIS A 1 174 ? 45.83822 55.04350 37.11142 1.000 6.50180  ? 69  HIS A N   1 
ATOM   541  C  CA  . HIS A 1 174 ? 46.67023 53.98059 36.54855 1.000 6.09910  ? 69  HIS A CA  1 
ATOM   542  C  C   . HIS A 1 174 ? 46.17349 53.51192 35.17422 1.000 6.62656  ? 69  HIS A C   1 
ATOM   543  O  O   . HIS A 1 174 ? 46.95867 53.38062 34.22635 1.000 6.14690  ? 69  HIS A O   1 
ATOM   544  C  CB  . HIS A 1 174 ? 46.66749 52.83830 37.55988 1.000 7.36402  ? 69  HIS A CB  1 
ATOM   545  C  CG  . HIS A 1 174 ? 47.58626 51.69850 37.24846 1.000 6.61134  ? 69  HIS A CG  1 
ATOM   546  N  ND1 . HIS A 1 174 ? 47.15457 50.55726 36.59218 1.000 7.86987  ? 69  HIS A ND1 1 
ATOM   547  C  CD2 . HIS A 1 174 ? 48.88956 51.47699 37.57934 1.000 9.48304  ? 69  HIS A CD2 1 
ATOM   548  C  CE1 . HIS A 1 174 ? 48.16460 49.69501 36.51393 1.000 8.49684  ? 69  HIS A CE1 1 
ATOM   549  N  NE2 . HIS A 1 174 ? 49.20904 50.21175 37.14294 1.000 9.23903  ? 69  HIS A NE2 1 
ATOM   550  N  N   . GLY A 1 175 ? 44.87133 53.23463 35.05331 1.000 5.43608  ? 70  GLY A N   1 
ATOM   551  C  CA  . GLY A 1 175 ? 44.35219 52.76006 33.77022 1.000 6.31176  ? 70  GLY A CA  1 
ATOM   552  C  C   . GLY A 1 175 ? 44.48124 53.79301 32.66030 1.000 5.65204  ? 70  GLY A C   1 
ATOM   553  O  O   . GLY A 1 175 ? 44.76403 53.44700 31.49508 1.000 5.76626  ? 70  GLY A O   1 
ATOM   554  N  N   . THR A 1 176 ? 44.27853 55.07784 33.00095 1.000 5.52979  ? 71  THR A N   1 
ATOM   555  C  CA  . THR A 1 176 ? 44.43294 56.14685 32.01866 1.000 5.63128  ? 71  THR A CA  1 
ATOM   556  C  C   . THR A 1 176 ? 45.88384 56.28320 31.56190 1.000 5.70372  ? 71  THR A C   1 
ATOM   557  O  O   . THR A 1 176 ? 46.14099 56.49098 30.36292 1.000 6.17140  ? 71  THR A O   1 
ATOM   558  C  CB  . THR A 1 176 ? 43.91155 57.43789 32.63769 1.000 6.07776  ? 71  THR A CB  1 
ATOM   559  O  OG1 . THR A 1 176 ? 42.48639 57.31919 32.81798 1.000 7.40363  ? 71  THR A OG1 1 
ATOM   560  C  CG2 . THR A 1 176 ? 44.21860 58.64552 31.74646 1.000 8.06642  ? 71  THR A CG2 1 
ATOM   561  N  N   . HIS A 1 177 ? 46.84797 56.09907 32.48853 1.000 5.47773  ? 72  HIS A N   1 
ATOM   562  C  CA  . HIS A 1 177 ? 48.26284 56.12325 32.11587 1.000 5.29648  ? 72  HIS A CA  1 
ATOM   563  C  C   . HIS A 1 177 ? 48.60007 54.97761 31.16724 1.000 4.96846  ? 72  HIS A C   1 
ATOM   564  O  O   . HIS A 1 177 ? 49.20520 55.17899 30.11006 1.000 5.27940  ? 72  HIS A O   1 
ATOM   565  C  CB  . HIS A 1 177 ? 49.10055 56.03632 33.40531 1.000 6.16241  ? 72  HIS A CB  1 
ATOM   566  C  CG  . HIS A 1 177 ? 50.52473 56.45068 33.23568 1.000 5.57658  ? 72  HIS A CG  1 
ATOM   567  N  ND1 . HIS A 1 177 ? 51.49594 55.56335 32.81559 1.000 7.80055  ? 72  HIS A ND1 1 
ATOM   568  C  CD2 . HIS A 1 177 ? 51.15544 57.63359 33.47467 1.000 6.43367  ? 72  HIS A CD2 1 
ATOM   569  C  CE1 . HIS A 1 177 ? 52.66236 56.19180 32.76864 1.000 6.58074  ? 72  HIS A CE1 1 
ATOM   570  N  NE2 . HIS A 1 177 ? 52.48175 57.44524 33.15714 1.000 5.70758  ? 72  HIS A NE2 1 
ATOM   571  N  N   . CYS A 1 178 ? 48.15921 53.76416 31.50697 1.000 4.79582  ? 73  CYS A N   1 
ATOM   572  C  CA  . CYS A 1 178 ? 48.47291 52.61508 30.65306 1.000 4.54425  ? 73  CYS A CA  1 
ATOM   573  C  C   . CYS A 1 178 ? 47.84204 52.77597 29.27860 1.000 6.09223  ? 73  CYS A C   1 
ATOM   574  O  O   . CYS A 1 178 ? 48.48612 52.50507 28.25403 1.000 6.06193  ? 73  CYS A O   1 
ATOM   575  C  CB  . CYS A 1 178 ? 47.96202 51.33345 31.32428 1.000 5.87982  ? 73  CYS A CB  1 
ATOM   576  S  SG  . CYS A 1 178 ? 48.87803 50.91442 32.81768 1.000 7.44158  ? 73  CYS A SG  1 
ATOM   577  N  N   . ALA A 1 179 ? 46.57108 53.20908 29.22972 1.000 4.67310  ? 74  ALA A N   1 
ATOM   578  C  CA  . ALA A 1 179 ? 45.91472 53.41553 27.93966 1.000 4.88470  ? 74  ALA A CA  1 
ATOM   579  C  C   . ALA A 1 179 ? 46.65383 54.46677 27.10770 1.000 5.63178  ? 74  ALA A C   1 
ATOM   580  O  O   . ALA A 1 179 ? 46.73966 54.34064 25.87705 1.000 5.57996  ? 74  ALA A O   1 
ATOM   581  C  CB  . ALA A 1 179 ? 44.43920 53.83589 28.16253 1.000 6.03240  ? 74  ALA A CB  1 
ATOM   582  N  N   . GLY A 1 180 ? 47.18416 55.51522 27.76197 1.000 5.04929  ? 75  GLY A N   1 
ATOM   583  C  CA  . GLY A 1 180 ? 47.92296 56.53123 27.01745 1.000 5.94786  ? 75  GLY A CA  1 
ATOM   584  C  C   . GLY A 1 180 ? 49.17849 55.97492 26.36396 1.000 6.37917  ? 75  GLY A C   1 
ATOM   585  O  O   . GLY A 1 180 ? 49.55627 56.40936 25.26553 1.000 7.24643  ? 75  GLY A O   1 
ATOM   586  N  N   . THR A 1 181 ? 49.85410 55.01798 27.03453 1.000 4.86780  ? 76  THR A N   1 
ATOM   587  C  CA  . THR A 1 181 ? 51.05435 54.44214 26.42097 1.000 4.79673  ? 76  THR A CA  1 
ATOM   588  C  C   . THR A 1 181 ? 50.68857 53.54065 25.24156 1.000 4.71587  ? 76  THR A C   1 
ATOM   589  O  O   . THR A 1 181 ? 51.44299 53.43386 24.26150 1.000 5.43030  ? 76  THR A O   1 
ATOM   590  C  CB  . THR A 1 181 ? 51.84177 53.69836 27.49524 1.000 6.75083  ? 76  THR A CB  1 
ATOM   591  O  OG1 . THR A 1 181 ? 52.28646 54.66815 28.44732 1.000 6.24587  ? 76  THR A OG1 1 
ATOM   592  C  CG2 . THR A 1 181 ? 53.06584 52.96669 26.92802 1.000 7.70069  ? 76  THR A CG2 1 
ATOM   593  N  N   . VAL A 1 182 ? 49.52175 52.88626 25.31419 1.000 5.08570  ? 77  VAL A N   1 
ATOM   594  C  CA  . VAL A 1 182 ? 49.03865 52.11798 24.15192 1.000 4.61045  ? 77  VAL A CA  1 
ATOM   595  C  C   . VAL A 1 182 ? 48.75900 53.04260 22.97280 1.000 5.08318  ? 77  VAL A C   1 
ATOM   596  O  O   . VAL A 1 182 ? 49.25334 52.82549 21.86310 1.000 6.07047  ? 77  VAL A O   1 
ATOM   597  C  CB  . VAL A 1 182 ? 47.76795 51.33455 24.50001 1.000 4.56307  ? 77  VAL A CB  1 
ATOM   598  C  CG1 . VAL A 1 182 ? 47.30073 50.61720 23.20231 1.000 7.04774  ? 77  VAL A CG1 1 
ATOM   599  C  CG2 . VAL A 1 182 ? 48.02244 50.28966 25.56340 1.000 7.75291  ? 77  VAL A CG2 1 
ATOM   600  N  N   . GLY A 1 183 ? 47.97500 54.09979 23.20207 1.000 5.07609  ? 78  GLY A N   1 
ATOM   601  C  CA  . GLY A 1 183 ? 47.35955 54.73176 22.04568 1.000 6.90850  ? 78  GLY A CA  1 
ATOM   602  C  C   . GLY A 1 183 ? 47.01860 56.21054 22.13463 1.000 8.73851  ? 78  GLY A C   1 
ATOM   603  O  O   . GLY A 1 183 ? 46.24938 56.66956 21.30307 1.000 9.97186  ? 78  GLY A O   1 
ATOM   604  N  N   . SER A 1 184 ? 47.53688 56.97603 23.08863 1.000 6.41961  ? 79  SER A N   1 
ATOM   605  C  CA  . SER A 1 184 ? 47.32954 58.42709 23.01015 1.000 6.12428  ? 79  SER A CA  1 
ATOM   606  C  C   . SER A 1 184 ? 48.16588 59.04344 21.88013 1.000 9.22037  ? 79  SER A C   1 
ATOM   607  O  O   . SER A 1 184 ? 49.14233 58.45925 21.41052 1.000 8.34379  ? 79  SER A O   1 
ATOM   608  C  CB  . SER A 1 184 ? 47.68883 59.08966 24.35083 1.000 6.92271  ? 79  SER A CB  1 
ATOM   609  O  OG  . SER A 1 184 ? 49.11146 59.02130 24.59308 1.000 7.71846  ? 79  SER A OG  1 
ATOM   610  N  N   . ARG A 1 185 ? 47.78985 60.26547 21.47976 1.000 6.88391  ? 80  ARG A N   1 
ATOM   611  C  CA  . ARG A 1 185 ? 48.46144 60.94415 20.37628 1.000 7.28159  ? 80  ARG A CA  1 
ATOM   612  C  C   . ARG A 1 185 ? 49.93187 61.21028 20.68491 1.000 8.47761  ? 80  ARG A C   1 
ATOM   613  O  O   . ARG A 1 185 ? 50.81812 60.81967 19.91413 1.000 9.31186  ? 80  ARG A O   1 
ATOM   614  C  CB  . ARG A 1 185 ? 47.70496 62.23811 20.03992 1.000 9.99713  ? 80  ARG A CB  1 
ATOM   615  C  CG  . ARG A 1 185 ? 48.35320 63.07753 18.92755 1.000 13.28186 ? 80  ARG A CG  1 
ATOM   616  C  CD  . ARG A 1 185 ? 47.90918 64.54551 19.01677 1.000 21.69589 ? 80  ARG A CD  1 
ATOM   617  N  NE  . ARG A 1 185 ? 48.65070 65.22544 20.06310 1.000 33.21487 ? 80  ARG A NE  1 
ATOM   618  C  CZ  . ARG A 1 185 ? 49.05305 66.48755 19.98584 1.000 50.34650 ? 80  ARG A CZ  1 
ATOM   619  N  NH1 . ARG A 1 185 ? 48.75270 67.24487 18.94188 1.000 50.22755 ? 80  ARG A NH1 1 
ATOM   620  N  NH2 . ARG A 1 185 ? 49.80881 66.98942 20.95990 1.000 44.53442 ? 80  ARG A NH2 1 
ATOM   621  N  N   . THR A 1 186 ? 50.21698 61.81958 21.83953 1.000 8.64452  ? 81  THR A N   1 
ATOM   622  C  CA  . THR A 1 186 ? 51.59251 62.18529 22.15143 1.000 7.28226  ? 81  THR A CA  1 
ATOM   623  C  C   . THR A 1 186 ? 52.36765 61.07177 22.83066 1.000 10.06053 ? 81  THR A C   1 
ATOM   624  O  O   . THR A 1 186 ? 53.58114 60.94020 22.61174 1.000 10.98284 ? 81  THR A O   1 
ATOM   625  C  CB  . THR A 1 186 ? 51.59637 63.43160 23.05816 1.000 8.27074  ? 81  THR A CB  1 
ATOM   626  O  OG1 . THR A 1 186 ? 50.85571 64.48478 22.41915 1.000 9.84662  ? 81  THR A OG1 1 
ATOM   627  C  CG2 . THR A 1 186 ? 53.02289 63.93917 23.31654 1.000 11.59310 ? 81  THR A CG2 1 
ATOM   628  N  N   . TYR A 1 187 ? 51.71234 60.25180 23.63779 1.000 6.44252  ? 82  TYR A N   1 
ATOM   629  C  CA  . TYR A 1 187 ? 52.44720 59.33541 24.50068 1.000 6.67145  ? 82  TYR A CA  1 
ATOM   630  C  C   . TYR A 1 187 ? 52.30685 57.88675 24.06937 1.000 5.76149  ? 82  TYR A C   1 
ATOM   631  O  O   . TYR A 1 187 ? 52.88141 57.00923 24.70880 1.000 6.92435  ? 82  TYR A O   1 
ATOM   632  C  CB  . TYR A 1 187 ? 52.02947 59.50859 26.00241 1.000 7.01952  ? 82  TYR A CB  1 
ATOM   633  C  CG  . TYR A 1 187 ? 52.02029 60.96832 26.38194 1.000 6.41120  ? 82  TYR A CG  1 
ATOM   634  C  CD1 . TYR A 1 187 ? 53.21183 61.64757 26.59753 1.000 12.02033 ? 82  TYR A CD1 1 
ATOM   635  C  CD2 . TYR A 1 187 ? 50.84806 61.68625 26.40330 1.000 7.24147  ? 82  TYR A CD2 1 
ATOM   636  C  CE1 . TYR A 1 187 ? 53.21619 63.01054 26.86192 1.000 10.06561 ? 82  TYR A CE1 1 
ATOM   637  C  CE2 . TYR A 1 187 ? 50.83910 63.06981 26.67602 1.000 8.86470  ? 82  TYR A CE2 1 
ATOM   638  C  CZ  . TYR A 1 187 ? 52.02214 63.71535 26.88848 1.000 10.27676 ? 82  TYR A CZ  1 
ATOM   639  O  OH  . TYR A 1 187 ? 52.04469 65.08835 27.16137 1.000 12.98404 ? 82  TYR A OH  1 
ATOM   640  N  N   . GLY A 1 188 ? 51.64715 57.61409 22.94928 1.000 5.81929  ? 83  GLY A N   1 
ATOM   641  C  CA  . GLY A 1 188 ? 51.22575 56.25252 22.60830 1.000 6.99670  ? 83  GLY A CA  1 
ATOM   642  C  C   . GLY A 1 188 ? 52.06570 55.62060 21.51317 1.000 7.64386  ? 83  GLY A C   1 
ATOM   643  O  O   . GLY A 1 188 ? 52.55332 56.30244 20.60974 1.000 7.30004  ? 83  GLY A O   1 
ATOM   644  N  N   . VAL A 1 189 ? 52.14446 54.28692 21.56834 1.000 5.36408  ? 84  VAL A N   1 
ATOM   645  C  CA  . VAL A 1 189 ? 52.85228 53.52066 20.53581 1.000 5.47458  ? 84  VAL A CA  1 
ATOM   646  C  C   . VAL A 1 189 ? 52.02855 53.46178 19.25683 1.000 7.73082  ? 84  VAL A C   1 
ATOM   647  O  O   . VAL A 1 189 ? 52.55897 53.60777 18.14388 1.000 8.72829  ? 84  VAL A O   1 
ATOM   648  C  CB  . VAL A 1 189 ? 53.12784 52.10630 21.05065 1.000 5.30442  ? 84  VAL A CB  1 
ATOM   649  C  CG1 . VAL A 1 189 ? 53.70883 51.23132 19.92280 1.000 6.88480  ? 84  VAL A CG1 1 
ATOM   650  C  CG2 . VAL A 1 189 ? 54.04697 52.15331 22.26168 1.000 6.35119  ? 84  VAL A CG2 1 
ATOM   651  N  N   . ALA A 1 190 ? 50.74016 53.16837 19.38770 1.000 7.20961  ? 85  ALA A N   1 
ATOM   652  C  CA  . ALA A 1 190 ? 49.84479 52.92223 18.25122 1.000 5.82691  ? 85  ALA A CA  1 
ATOM   653  C  C   . ALA A 1 190 ? 48.81673 54.04808 18.24194 1.000 7.18056  ? 85  ALA A C   1 
ATOM   654  O  O   . ALA A 1 190 ? 47.73188 53.92278 18.82297 1.000 7.24112  ? 85  ALA A O   1 
ATOM   655  C  CB  . ALA A 1 190 ? 49.16349 51.53575 18.39801 1.000 6.63901  ? 85  ALA A CB  1 
ATOM   656  N  N   . LYS A 1 191 ? 49.15859 55.13377 17.54328 1.000 7.78095  ? 86  LYS A N   1 
ATOM   657  C  CA  . LYS A 1 191 ? 48.47597 56.41909 17.73839 1.000 6.67758  ? 86  LYS A CA  1 
ATOM   658  C  C   . LYS A 1 191 ? 47.10484 56.49484 17.08741 1.000 9.62412  ? 86  LYS A C   1 
ATOM   659  O  O   . LYS A 1 191 ? 46.39137 57.50051 17.30673 1.000 11.32189 ? 86  LYS A O   1 
ATOM   660  C  CB  . LYS A 1 191 ? 49.37339 57.55511 17.23573 1.000 9.27994  ? 86  LYS A CB  1 
ATOM   661  C  CG  . LYS A 1 191 ? 50.64362 57.64956 18.05380 1.000 8.28685  ? 86  LYS A CG  1 
ATOM   662  C  CD  . LYS A 1 191 ? 51.56277 58.74937 17.47867 1.000 9.41353  ? 86  LYS A CD  1 
ATOM   663  C  CE  . LYS A 1 191 ? 52.93551 58.73837 18.12962 1.000 8.39001  ? 86  LYS A CE  1 
ATOM   664  N  NZ  . LYS A 1 191 ? 52.88899 59.02988 19.61612 1.000 8.14385  ? 86  LYS A NZ  1 
ATOM   665  N  N   . LYS A 1 192 ? 46.70103 55.47586 16.31729 1.000 8.19463  ? 87  LYS A N   1 
ATOM   666  C  CA  . LYS A 1 192 ? 45.38328 55.48087 15.68560 1.000 7.39915  ? 87  LYS A CA  1 
ATOM   667  C  C   . LYS A 1 192 ? 44.55092 54.24901 16.05417 1.000 7.04943  ? 87  LYS A C   1 
ATOM   668  O  O   . LYS A 1 192 ? 43.49314 54.02053 15.41486 1.000 9.86581  ? 87  LYS A O   1 
ATOM   669  C  CB  . LYS A 1 192 ? 45.52739 55.60283 14.16390 1.000 9.21741  ? 87  LYS A CB  1 
ATOM   670  C  CG  . LYS A 1 192 ? 46.06309 56.96675 13.74762 1.000 11.36102 ? 87  LYS A CG  1 
ATOM   671  C  CD  . LYS A 1 192 ? 46.05271 57.03059 12.19732 1.000 22.83409 ? 87  LYS A CD  1 
ATOM   672  C  CE  . LYS A 1 192 ? 46.72752 58.30986 11.68413 1.000 43.96445 ? 87  LYS A CE  1 
ATOM   673  N  NZ  . LYS A 1 192 ? 47.49960 58.08994 10.41645 1.000 41.98084 ? 87  LYS A NZ  1 
ATOM   674  N  N   . THR A 1 193 ? 44.94570 53.49023 17.09279 1.000 7.44924  ? 88  THR A N   1 
ATOM   675  C  CA  . THR A 1 193 ? 44.15939 52.32808 17.50818 1.000 7.36249  ? 88  THR A CA  1 
ATOM   676  C  C   . THR A 1 193 ? 42.89263 52.77145 18.24885 1.000 9.11237  ? 88  THR A C   1 
ATOM   677  O  O   . THR A 1 193 ? 42.75108 53.91697 18.66333 1.000 8.71443  ? 88  THR A O   1 
ATOM   678  C  CB  . THR A 1 193 ? 45.01902 51.39330 18.37095 1.000 9.25374  ? 88  THR A CB  1 
ATOM   679  O  OG1 . THR A 1 193 ? 44.38038 50.11436 18.49227 1.000 9.40573  ? 88  THR A OG1 1 
ATOM   680  C  CG2 . THR A 1 193 ? 45.21610 51.93491 19.79299 1.000 9.24525  ? 88  THR A CG2 1 
ATOM   681  N  N   A GLN A 1 194 ? 41.93389 51.85197 18.36573 0.570 6.82121  ? 89  GLN A N   1 
ATOM   682  N  N   B GLN A 1 194 ? 41.96005 51.84038 18.38198 0.430 6.84186  ? 89  GLN A N   1 
ATOM   683  C  CA  A GLN A 1 194 ? 40.72545 52.06965 19.16699 0.570 8.01833  ? 89  GLN A CA  1 
ATOM   684  C  CA  B GLN A 1 194 ? 40.76138 52.04829 19.18202 0.430 8.10590  ? 89  GLN A CA  1 
ATOM   685  C  C   A GLN A 1 194 ? 40.93171 51.44659 20.54476 0.570 7.21655  ? 89  GLN A C   1 
ATOM   686  C  C   B GLN A 1 194 ? 41.01800 51.46798 20.56756 0.430 7.25169  ? 89  GLN A C   1 
ATOM   687  O  O   A GLN A 1 194 ? 41.32595 50.28110 20.63767 0.570 9.97073  ? 89  GLN A O   1 
ATOM   688  O  O   B GLN A 1 194 ? 41.58348 50.37876 20.69064 0.430 9.18170  ? 89  GLN A O   1 
ATOM   689  C  CB  A GLN A 1 194 ? 39.49815 51.44741 18.50033 0.570 9.16513  ? 89  GLN A CB  1 
ATOM   690  C  CB  B GLN A 1 194 ? 39.56124 51.38832 18.50992 0.430 9.15441  ? 89  GLN A CB  1 
ATOM   691  C  CG  A GLN A 1 194 ? 38.30072 51.29980 19.43935 0.570 13.57043 ? 89  GLN A CG  1 
ATOM   692  C  CG  B GLN A 1 194 ? 39.10729 52.14891 17.27076 0.430 9.80109  ? 89  GLN A CG  1 
ATOM   693  C  CD  A GLN A 1 194 ? 37.49261 52.58633 19.60736 0.570 21.06552 ? 89  GLN A CD  1 
ATOM   694  C  CD  B GLN A 1 194 ? 38.26594 53.36787 17.59517 0.430 17.51934 ? 89  GLN A CD  1 
ATOM   695  O  OE1 A GLN A 1 194 ? 37.19360 53.25665 18.62116 0.570 28.34966 ? 89  GLN A OE1 1 
ATOM   696  O  OE1 B GLN A 1 194 ? 37.32379 53.28306 18.38485 0.430 27.23712 ? 89  GLN A OE1 1 
ATOM   697  N  NE2 A GLN A 1 194 ? 37.12279 52.92888 20.85247 0.570 11.54042 ? 89  GLN A NE2 1 
ATOM   698  N  NE2 B GLN A 1 194 ? 38.58127 54.50296 16.97142 0.430 16.43303 ? 89  GLN A NE2 1 
ATOM   699  N  N   . LEU A 1 195 ? 40.64934 52.20653 21.60874 1.000 5.92643  ? 90  LEU A N   1 
ATOM   700  C  CA  . LEU A 1 195 ? 40.86418 51.75379 22.98569 1.000 5.59279  ? 90  LEU A CA  1 
ATOM   701  C  C   . LEU A 1 195 ? 39.53760 51.47177 23.66066 1.000 7.54253  ? 90  LEU A C   1 
ATOM   702  O  O   . LEU A 1 195 ? 38.63512 52.30598 23.60254 1.000 9.63822  ? 90  LEU A O   1 
ATOM   703  C  CB  . LEU A 1 195 ? 41.60657 52.82783 23.80267 1.000 5.51711  ? 90  LEU A CB  1 
ATOM   704  C  CG  . LEU A 1 195 ? 43.00809 53.08823 23.26710 1.000 10.56270 ? 90  LEU A CG  1 
ATOM   705  C  CD1 . LEU A 1 195 ? 43.45257 54.51430 23.66940 1.000 17.74210 ? 90  LEU A CD1 1 
ATOM   706  C  CD2 . LEU A 1 195 ? 44.01643 52.05441 23.70568 1.000 16.71274 ? 90  LEU A CD2 1 
ATOM   707  N  N   . PHE A 1 196 ? 39.43688 50.31151 24.31452 1.000 5.85409  ? 91  PHE A N   1 
ATOM   708  C  CA  . PHE A 1 196 ? 38.24338 49.93471 25.06455 1.000 6.60678  ? 91  PHE A CA  1 
ATOM   709  C  C   . PHE A 1 196 ? 38.63061 49.71830 26.51689 1.000 8.17441  ? 91  PHE A C   1 
ATOM   710  O  O   . PHE A 1 196 ? 39.56210 48.96219 26.81194 1.000 9.07611  ? 91  PHE A O   1 
ATOM   711  C  CB  . PHE A 1 196 ? 37.63854 48.64262 24.51734 1.000 6.47439  ? 91  PHE A CB  1 
ATOM   712  C  CG  . PHE A 1 196 ? 37.12588 48.74421 23.12113 1.000 9.10778  ? 91  PHE A CG  1 
ATOM   713  C  CD1 . PHE A 1 196 ? 36.19956 49.70592 22.79210 1.000 12.28636 ? 91  PHE A CD1 1 
ATOM   714  C  CD2 . PHE A 1 196 ? 37.54541 47.83506 22.14794 1.000 12.32774 ? 91  PHE A CD2 1 
ATOM   715  C  CE1 . PHE A 1 196 ? 35.69592 49.81151 21.48229 1.000 13.97173 ? 91  PHE A CE1 1 
ATOM   716  C  CE2 . PHE A 1 196 ? 37.04046 47.93178 20.83160 1.000 17.44607 ? 91  PHE A CE2 1 
ATOM   717  C  CZ  . PHE A 1 196 ? 36.11989 48.91637 20.51989 1.000 13.66354 ? 91  PHE A CZ  1 
ATOM   718  N  N   . GLY A 1 197 ? 37.92270 50.36354 27.43902 1.000 6.31993  ? 92  GLY A N   1 
ATOM   719  C  CA  . GLY A 1 197 ? 38.25670 50.22608 28.85757 1.000 5.93127  ? 92  GLY A CA  1 
ATOM   720  C  C   . GLY A 1 197 ? 37.33898 49.25358 29.57628 1.000 6.70691  ? 92  GLY A C   1 
ATOM   721  O  O   . GLY A 1 197 ? 36.11616 49.28760 29.40143 1.000 8.40154  ? 92  GLY A O   1 
ATOM   722  N  N   . VAL A 1 198 ? 37.94762 48.37294 30.38582 1.000 5.55956  ? 93  VAL A N   1 
ATOM   723  C  CA  . VAL A 1 198 ? 37.21107 47.43779 31.25696 1.000 5.87355  ? 93  VAL A CA  1 
ATOM   724  C  C   . VAL A 1 198 ? 37.70063 47.68398 32.68163 1.000 7.09408  ? 93  VAL A C   1 
ATOM   725  O  O   . VAL A 1 198 ? 38.88505 47.47153 32.96887 1.000 7.59805  ? 93  VAL A O   1 
ATOM   726  C  CB  . VAL A 1 198 ? 37.44363 45.98761 30.82098 1.000 6.40492  ? 93  VAL A CB  1 
ATOM   727  C  CG1 . VAL A 1 198 ? 36.64464 45.05371 31.72537 1.000 9.85778  ? 93  VAL A CG1 1 
ATOM   728  C  CG2 . VAL A 1 198 ? 37.03351 45.80762 29.35974 1.000 13.89731 ? 93  VAL A CG2 1 
ATOM   729  N  N   . LYS A 1 199 ? 36.81809 48.18958 33.55562 1.000 6.16791  ? 94  LYS A N   1 
ATOM   730  C  CA  . LYS A 1 199 ? 37.23826 48.55272 34.91943 1.000 6.76266  ? 94  LYS A CA  1 
ATOM   731  C  C   . LYS A 1 199 ? 37.05691 47.34727 35.84934 1.000 7.03247  ? 94  LYS A C   1 
ATOM   732  O  O   . LYS A 1 199 ? 35.95393 47.09366 36.36167 1.000 8.50101  ? 94  LYS A O   1 
ATOM   733  C  CB  . LYS A 1 199 ? 36.46200 49.77411 35.40143 1.000 7.67874  ? 94  LYS A CB  1 
ATOM   734  C  CG  . LYS A 1 199 ? 36.87388 50.21863 36.82465 1.000 6.96074  ? 94  LYS A CG  1 
ATOM   735  C  CD  . LYS A 1 199 ? 36.19130 51.56799 37.17599 1.000 7.42370  ? 94  LYS A CD  1 
ATOM   736  C  CE  . LYS A 1 199 ? 36.42882 51.94955 38.65119 1.000 10.37465 ? 94  LYS A CE  1 
ATOM   737  N  NZ  . LYS A 1 199 ? 37.93062 52.09332 38.98860 1.000 9.45668  ? 94  LYS A NZ  1 
ATOM   738  N  N   . VAL A 1 200 ? 38.14101 46.59184 36.05180 1.000 7.23872  ? 95  VAL A N   1 
ATOM   739  C  CA  . VAL A 1 200 ? 38.13635 45.49102 37.02259 1.000 6.80152  ? 95  VAL A CA  1 
ATOM   740  C  C   . VAL A 1 200 ? 38.83407 45.86221 38.32128 1.000 6.52750  ? 95  VAL A C   1 
ATOM   741  O  O   . VAL A 1 200 ? 38.75117 45.08614 39.29873 1.000 8.14152  ? 95  VAL A O   1 
ATOM   742  C  CB  . VAL A 1 200 ? 38.81484 44.20725 36.47221 1.000 6.48134  ? 95  VAL A CB  1 
ATOM   743  C  CG1 . VAL A 1 200 ? 38.09674 43.66236 35.19363 1.000 8.63806  ? 95  VAL A CG1 1 
ATOM   744  C  CG2 . VAL A 1 200 ? 40.30599 44.47525 36.19562 1.000 8.93630  ? 95  VAL A CG2 1 
ATOM   745  N  N   . LEU A 1 201 ? 39.52936 47.00265 38.37143 1.000 7.90333  ? 96  LEU A N   1 
ATOM   746  C  CA  . LEU A 1 201 ? 40.18308 47.44623 39.60811 1.000 7.72574  ? 96  LEU A CA  1 
ATOM   747  C  C   . LEU A 1 201 ? 39.43916 48.64512 40.16469 1.000 9.05137  ? 96  LEU A C   1 
ATOM   748  O  O   . LEU A 1 201 ? 39.01996 49.51781 39.40248 1.000 9.49806  ? 96  LEU A O   1 
ATOM   749  C  CB  . LEU A 1 201 ? 41.66263 47.82239 39.35857 1.000 9.18237  ? 96  LEU A CB  1 
ATOM   750  C  CG  . LEU A 1 201 ? 42.53581 46.71989 38.73395 1.000 9.80298  ? 96  LEU A CG  1 
ATOM   751  C  CD1 . LEU A 1 201 ? 43.99640 47.21226 38.42260 1.000 10.95419 ? 96  LEU A CD1 1 
ATOM   752  C  CD2 . LEU A 1 201 ? 42.55251 45.49528 39.63971 1.000 12.79814 ? 96  LEU A CD2 1 
ATOM   753  N  N   . ASP A 1 202 ? 39.35322 48.72136 41.49764 1.000 9.80118  ? 97  ASP A N   1 
ATOM   754  C  CA  . ASP A 1 202 ? 38.67527 49.85495 42.12221 1.000 9.70979  ? 97  ASP A CA  1 
ATOM   755  C  C   . ASP A 1 202 ? 39.60087 51.08181 42.11156 1.000 10.47126 ? 97  ASP A C   1 
ATOM   756  O  O   . ASP A 1 202 ? 40.70868 51.05742 41.54178 1.000 10.47913 ? 97  ASP A O   1 
ATOM   757  C  CB  . ASP A 1 202 ? 38.17784 49.46091 43.52796 1.000 9.89545  ? 97  ASP A CB  1 
ATOM   758  C  CG  . ASP A 1 202 ? 39.29072 49.24769 44.54478 1.000 19.21701 ? 97  ASP A CG  1 
ATOM   759  O  OD1 . ASP A 1 202 ? 40.42864 49.75169 44.38756 1.000 13.67351 ? 97  ASP A OD1 1 
ATOM   760  O  OD2 . ASP A 1 202 ? 38.98517 48.60335 45.58949 1.000 21.09687 ? 97  ASP A OD2 1 
ATOM   761  N  N   . ASP A 1 203 ? 39.12492 52.19969 42.66950 1.000 9.81366  ? 98  ASP A N   1 
ATOM   762  C  CA  . ASP A 1 203 ? 39.87978 53.44779 42.54998 1.000 11.05136 ? 98  ASP A CA  1 
ATOM   763  C  C   . ASP A 1 203 ? 41.07919 53.48699 43.47495 1.000 14.60410 ? 98  ASP A C   1 
ATOM   764  O  O   . ASP A 1 203 ? 41.85821 54.44015 43.42363 1.000 14.05895 ? 98  ASP A O   1 
ATOM   765  C  CB  . ASP A 1 203 ? 38.96060 54.64213 42.78789 1.000 10.00612 ? 98  ASP A CB  1 
ATOM   766  C  CG  . ASP A 1 203 ? 37.99092 54.87058 41.64813 1.000 12.94041 ? 98  ASP A CG  1 
ATOM   767  O  OD1 . ASP A 1 203 ? 38.25568 54.42849 40.51010 1.000 11.29162 ? 98  ASP A OD1 1 
ATOM   768  O  OD2 . ASP A 1 203 ? 36.93449 55.50299 41.88294 1.000 16.10776 ? 98  ASP A OD2 1 
ATOM   769  N  N   . ASN A 1 204 ? 41.25063 52.47533 44.32157 1.000 14.57481 ? 99  ASN A N   1 
ATOM   770  C  CA  . ASN A 1 204 ? 42.50002 52.31755 45.03756 1.000 15.15206 ? 99  ASN A CA  1 
ATOM   771  C  C   . ASN A 1 204 ? 43.46595 51.40277 44.31800 1.000 19.72166 ? 99  ASN A C   1 
ATOM   772  O  O   . ASN A 1 204 ? 44.55768 51.16142 44.82960 1.000 19.96955 ? 99  ASN A O   1 
ATOM   773  C  CB  . ASN A 1 204 ? 42.23769 51.77490 46.44203 1.000 20.37293 ? 99  ASN A CB  1 
ATOM   774  C  CG  . ASN A 1 204 ? 41.52062 52.78036 47.29953 1.000 25.82745 ? 99  ASN A CG  1 
ATOM   775  O  OD1 . ASN A 1 204 ? 41.88217 53.95784 47.30598 1.000 31.57776 ? 99  ASN A OD1 1 
ATOM   776  N  ND2 . ASN A 1 204 ? 40.48724 52.33582 48.01174 1.000 28.33721 ? 99  ASN A ND2 1 
ATOM   777  N  N   . GLY A 1 205 ? 43.10094 50.88724 43.14700 1.000 12.00890 ? 100 GLY A N   1 
ATOM   778  C  CA  . GLY A 1 205 ? 43.98585 50.01870 42.41005 1.000 11.66340 ? 100 GLY A CA  1 
ATOM   779  C  C   . GLY A 1 205 ? 43.87737 48.55800 42.75793 1.000 19.62533 ? 100 GLY A C   1 
ATOM   780  O  O   . GLY A 1 205 ? 44.72225 47.77638 42.31227 1.000 20.42218 ? 100 GLY A O   1 
ATOM   781  N  N   . SER A 1 206 ? 42.87475 48.16599 43.53630 1.000 14.76358 ? 101 SER A N   1 
ATOM   782  C  CA  . SER A 1 206 ? 42.73381 46.79497 44.02674 1.000 16.36587 ? 101 SER A CA  1 
ATOM   783  C  C   . SER A 1 206 ? 41.54626 46.11506 43.36534 1.000 18.41963 ? 101 SER A C   1 
ATOM   784  O  O   . SER A 1 206 ? 40.60729 46.75887 42.90150 1.000 15.52569 ? 101 SER A O   1 
ATOM   785  C  CB  . SER A 1 206 ? 42.51098 46.75128 45.54783 1.000 23.90467 ? 101 SER A CB  1 
ATOM   786  O  OG  . SER A 1 206 ? 43.41325 47.57717 46.23479 1.000 48.32486 ? 101 SER A OG  1 
ATOM   787  N  N   . GLY A 1 207 ? 41.56929 44.79065 43.37528 1.000 20.41822 ? 102 GLY A N   1 
ATOM   788  C  CA  . GLY A 1 207 ? 40.45644 44.03827 42.82698 1.000 13.62412 ? 102 GLY A CA  1 
ATOM   789  C  C   . GLY A 1 207 ? 40.57704 42.57283 43.17500 1.000 16.47805 ? 102 GLY A C   1 
ATOM   790  O  O   . GLY A 1 207 ? 41.68548 42.04635 43.27536 1.000 22.38979 ? 102 GLY A O   1 
ATOM   791  N  N   . GLN A 1 208 ? 39.45342 41.92085 43.37269 1.000 13.01244 ? 103 GLN A N   1 
ATOM   792  C  CA  . GLN A 1 208 ? 39.42178 40.49895 43.67062 1.000 13.46231 ? 103 GLN A CA  1 
ATOM   793  C  C   . GLN A 1 208 ? 39.62590 39.66981 42.42173 1.000 11.81864 ? 103 GLN A C   1 
ATOM   794  O  O   . GLN A 1 208 ? 39.26557 40.06007 41.31399 1.000 12.07389 ? 103 GLN A O   1 
ATOM   795  C  CB  . GLN A 1 208 ? 38.09570 40.09738 44.29415 1.000 18.98070 ? 103 GLN A CB  1 
ATOM   796  C  CG  . GLN A 1 208 ? 37.58594 41.06251 45.32088 1.000 35.76303 ? 103 GLN A CG  1 
ATOM   797  C  CD  . GLN A 1 208 ? 37.01654 40.32536 46.51196 1.000 71.11777 ? 103 GLN A CD  1 
ATOM   798  O  OE1 . GLN A 1 208 ? 36.17795 39.42590 46.35723 1.000 67.38717 ? 103 GLN A OE1 1 
ATOM   799  N  NE2 . GLN A 1 208 ? 37.50337 40.66253 47.70801 1.000 55.20837 ? 103 GLN A NE2 1 
ATOM   800  N  N   . TYR A 1 209 ? 40.19685 38.48747 42.62514 1.000 11.24656 ? 104 TYR A N   1 
ATOM   801  C  CA  . TYR A 1 209 ? 40.50145 37.64719 41.47770 1.000 10.02591 ? 104 TYR A CA  1 
ATOM   802  C  C   . TYR A 1 209 ? 39.23952 37.26383 40.69559 1.000 9.91974  ? 104 TYR A C   1 
ATOM   803  O  O   . TYR A 1 209 ? 39.28832 37.20174 39.45855 1.000 10.97113 ? 104 TYR A O   1 
ATOM   804  C  CB  . TYR A 1 209 ? 41.27212 36.42199 41.96767 1.000 12.90287 ? 104 TYR A CB  1 
ATOM   805  C  CG  . TYR A 1 209 ? 42.79016 36.60740 41.95916 1.000 17.69332 ? 104 TYR A CG  1 
ATOM   806  C  CD1 . TYR A 1 209 ? 43.38862 37.66256 41.24394 1.000 19.03268 ? 104 TYR A CD1 1 
ATOM   807  C  CD2 . TYR A 1 209 ? 43.61611 35.69377 42.60046 1.000 13.10240 ? 104 TYR A CD2 1 
ATOM   808  C  CE1 . TYR A 1 209 ? 44.78964 37.81846 41.18629 1.000 26.85386 ? 104 TYR A CE1 1 
ATOM   809  C  CE2 . TYR A 1 209 ? 45.03104 35.84170 42.56039 1.000 19.02590 ? 104 TYR A CE2 1 
ATOM   810  C  CZ  . TYR A 1 209 ? 45.59794 36.90070 41.85576 1.000 27.36227 ? 104 TYR A CZ  1 
ATOM   811  O  OH  . TYR A 1 209 ? 46.97690 37.02654 41.78739 1.000 23.13484 ? 104 TYR A OH  1 
ATOM   812  N  N   . SER A 1 210 ? 38.10455 37.03298 41.38150 1.000 12.43066 ? 105 SER A N   1 
ATOM   813  C  CA  . SER A 1 210 ? 36.87290 36.66973 40.67543 1.000 13.77505 ? 105 SER A CA  1 
ATOM   814  C  C   . SER A 1 210 ? 36.45530 37.75750 39.69007 1.000 11.28000 ? 105 SER A C   1 
ATOM   815  O  O   . SER A 1 210 ? 35.96313 37.44831 38.58964 1.000 11.69226 ? 105 SER A O   1 
ATOM   816  C  CB  . SER A 1 210 ? 35.74714 36.37054 41.67943 1.000 13.88670 ? 105 SER A CB  1 
ATOM   817  O  OG  . SER A 1 210 ? 35.54973 37.49818 42.50020 1.000 25.80105 ? 105 SER A OG  1 
ATOM   818  N  N   . THR A 1 211 ? 36.66908 39.03226 40.05174 1.000 9.09203  ? 106 THR A N   1 
ATOM   819  C  CA  . THR A 1 211 ? 36.30528 40.14100 39.17136 1.000 8.43551  ? 106 THR A CA  1 
ATOM   820  C  C   . THR A 1 211 ? 37.26840 40.23626 37.99541 1.000 9.80483  ? 106 THR A C   1 
ATOM   821  O  O   . THR A 1 211 ? 36.86400 40.52432 36.85363 1.000 9.40021  ? 106 THR A O   1 
ATOM   822  C  CB  . THR A 1 211 ? 36.29142 41.43065 39.98623 1.000 10.00562 ? 106 THR A CB  1 
ATOM   823  O  OG1 . THR A 1 211 ? 35.31353 41.29825 41.03384 1.000 17.50145 ? 106 THR A OG1 1 
ATOM   824  C  CG2 . THR A 1 211 ? 35.94738 42.60430 39.09014 1.000 12.54919 ? 106 THR A CG2 1 
ATOM   825  N  N   . ILE A 1 212 ? 38.56304 40.03146 38.25792 1.000 7.08974  ? 107 ILE A N   1 
ATOM   826  C  CA  . ILE A 1 212 ? 39.54610 40.09855 37.18710 1.000 6.31068  ? 107 ILE A CA  1 
ATOM   827  C  C   . ILE A 1 212 ? 39.28740 38.98696 36.16318 1.000 9.15155  ? 107 ILE A C   1 
ATOM   828  O  O   . ILE A 1 212 ? 39.34060 39.20966 34.94126 1.000 9.15693  ? 107 ILE A O   1 
ATOM   829  C  CB  . ILE A 1 212 ? 40.96454 40.02812 37.79868 1.000 8.18564  ? 107 ILE A CB  1 
ATOM   830  C  CG1 . ILE A 1 212 ? 41.26297 41.32208 38.54961 1.000 10.59682 ? 107 ILE A CG1 1 
ATOM   831  C  CG2 . ILE A 1 212 ? 41.96306 39.78936 36.69305 1.000 12.27973 ? 107 ILE A CG2 1 
ATOM   832  C  CD1 . ILE A 1 212 ? 42.38141 41.17701 39.63270 1.000 15.15134 ? 107 ILE A CD1 1 
ATOM   833  N  N   . ILE A 1 213 ? 38.94511 37.78782 36.64931 1.000 7.92931  ? 108 ILE A N   1 
ATOM   834  C  CA  . ILE A 1 213 ? 38.59418 36.68191 35.75821 1.000 6.63342  ? 108 ILE A CA  1 
ATOM   835  C  C   . ILE A 1 213 ? 37.35995 37.03149 34.93943 1.000 8.47073  ? 108 ILE A C   1 
ATOM   836  O  O   . ILE A 1 213 ? 37.33125 36.83482 33.72583 1.000 7.47197  ? 108 ILE A O   1 
ATOM   837  C  CB  . ILE A 1 213 ? 38.36911 35.39616 36.57813 1.000 7.09680  ? 108 ILE A CB  1 
ATOM   838  C  CG1 . ILE A 1 213 ? 39.71872 34.87065 37.10511 1.000 8.63400  ? 108 ILE A CG1 1 
ATOM   839  C  CG2 . ILE A 1 213 ? 37.67709 34.29209 35.71741 1.000 8.06307  ? 108 ILE A CG2 1 
ATOM   840  C  CD1 . ILE A 1 213 ? 39.54504 33.81633 38.19173 1.000 12.85122 ? 108 ILE A CD1 1 
ATOM   841  N  N   . ALA A 1 214 ? 36.32188 37.57647 35.58135 1.000 6.99117  ? 109 ALA A N   1 
ATOM   842  C  CA  . ALA A 1 214 ? 35.11801 37.93336 34.81885 1.000 7.22510  ? 109 ALA A CA  1 
ATOM   843  C  C   . ALA A 1 214 ? 35.41486 38.93753 33.71387 1.000 8.98155  ? 109 ALA A C   1 
ATOM   844  O  O   . ALA A 1 214 ? 34.85401 38.84554 32.59962 1.000 8.26357  ? 109 ALA A O   1 
ATOM   845  C  CB  . ALA A 1 214 ? 34.02790 38.47053 35.76321 1.000 8.67005  ? 109 ALA A CB  1 
ATOM   846  N  N   . GLY A 1 215 ? 36.29014 39.90042 33.98981 1.000 6.43309  ? 110 GLY A N   1 
ATOM   847  C  CA  . GLY A 1 215 ? 36.63818 40.89237 32.98949 1.000 7.41127  ? 110 GLY A CA  1 
ATOM   848  C  C   . GLY A 1 215 ? 37.37461 40.28445 31.80807 1.000 10.25460 ? 110 GLY A C   1 
ATOM   849  O  O   . GLY A 1 215 ? 37.16145 40.71338 30.67990 1.000 8.72422  ? 110 GLY A O   1 
ATOM   850  N  N   . MET A 1 216 ? 38.23152 39.26610 32.04273 1.000 6.10133  ? 111 MET A N   1 
ATOM   851  C  CA  . MET A 1 216 ? 38.88335 38.58776 30.91426 1.000 5.73184  ? 111 MET A CA  1 
ATOM   852  C  C   . MET A 1 216 ? 37.84518 37.82412 30.08023 1.000 7.08813  ? 111 MET A C   1 
ATOM   853  O  O   . MET A 1 216 ? 37.85237 37.88037 28.83298 1.000 7.96050  ? 111 MET A O   1 
ATOM   854  C  CB  . MET A 1 216 ? 39.99165 37.66046 31.44576 1.000 7.33494  ? 111 MET A CB  1 
ATOM   855  C  CG  . MET A 1 216 ? 41.21146 38.46382 31.87182 1.000 6.17923  ? 111 MET A CG  1 
ATOM   856  S  SD  . MET A 1 216 ? 42.59075 37.30385 32.22882 1.000 12.90487 ? 111 MET A SD  1 
ATOM   857  C  CE  . MET A 1 216 ? 42.53631 37.30262 33.99034 1.000 15.43028 ? 111 MET A CE  1 
ATOM   858  N  N   . ASP A 1 217 ? 36.95022 37.09833 30.74052 1.000 6.56184  ? 112 ASP A N   1 
ATOM   859  C  CA  . ASP A 1 217 ? 35.94525 36.36607 29.96510 1.000 6.68716  ? 112 ASP A CA  1 
ATOM   860  C  C   . ASP A 1 217 ? 35.03283 37.33922 29.23096 1.000 8.75838  ? 112 ASP A C   1 
ATOM   861  O  O   . ASP A 1 217 ? 34.54058 37.03271 28.13114 1.000 7.12442  ? 112 ASP A O   1 
ATOM   862  C  CB  . ASP A 1 217 ? 35.11151 35.44095 30.86894 1.000 7.04568  ? 112 ASP A CB  1 
ATOM   863  C  CG  . ASP A 1 217 ? 35.90767 34.24579 31.46407 1.000 12.96031 ? 112 ASP A CG  1 
ATOM   864  O  OD1 . ASP A 1 217 ? 36.77284 33.72860 30.75939 1.000 20.68965 ? 112 ASP A OD1 1 
ATOM   865  O  OD2 . ASP A 1 217 ? 35.53687 33.84862 32.58405 1.000 23.67913 ? 112 ASP A OD2 1 
ATOM   866  N  N   . PHE A 1 218 ? 34.77640 38.52339 29.81726 1.000 7.37280  ? 113 PHE A N   1 
ATOM   867  C  CA  . PHE A 1 218 ? 33.98016 39.51604 29.10992 1.000 8.95093  ? 113 PHE A CA  1 
ATOM   868  C  C   . PHE A 1 218 ? 34.63786 39.93654 27.79536 1.000 7.81892  ? 113 PHE A C   1 
ATOM   869  O  O   . PHE A 1 218 ? 33.95765 40.04875 26.77103 1.000 8.15646  ? 113 PHE A O   1 
ATOM   870  C  CB  . PHE A 1 218 ? 33.76210 40.74919 30.01862 1.000 8.00326  ? 113 PHE A CB  1 
ATOM   871  C  CG  . PHE A 1 218 ? 33.13969 41.90751 29.28286 1.000 7.51678  ? 113 PHE A CG  1 
ATOM   872  C  CD1 . PHE A 1 218 ? 31.76777 41.96185 29.10152 1.000 15.30760 ? 113 PHE A CD1 1 
ATOM   873  C  CD2 . PHE A 1 218 ? 33.93350 42.88335 28.73278 1.000 8.90040  ? 113 PHE A CD2 1 
ATOM   874  C  CE1 . PHE A 1 218 ? 31.18943 43.02168 28.38431 1.000 15.05544 ? 113 PHE A CE1 1 
ATOM   875  C  CE2 . PHE A 1 218 ? 33.33345 43.93022 27.98272 1.000 10.99195 ? 113 PHE A CE2 1 
ATOM   876  C  CZ  . PHE A 1 218 ? 31.97897 43.96969 27.84910 1.000 13.15087 ? 113 PHE A CZ  1 
ATOM   877  N  N   . VAL A 1 219 ? 35.94969 40.20503 27.80739 1.000 6.08489  ? 114 VAL A N   1 
ATOM   878  C  CA  . VAL A 1 219 ? 36.62722 40.65455 26.57630 1.000 5.81218  ? 114 VAL A CA  1 
ATOM   879  C  C   . VAL A 1 219 ? 36.55155 39.57271 25.49894 1.000 5.97384  ? 114 VAL A C   1 
ATOM   880  O  O   . VAL A 1 219 ? 36.38012 39.85747 24.30682 1.000 7.52232  ? 114 VAL A O   1 
ATOM   881  C  CB  . VAL A 1 219 ? 38.08787 41.05094 26.88172 1.000 6.48690  ? 114 VAL A CB  1 
ATOM   882  C  CG1 . VAL A 1 219 ? 38.84273 41.37591 25.58552 1.000 9.15609  ? 114 VAL A CG1 1 
ATOM   883  C  CG2 . VAL A 1 219 ? 38.09605 42.21392 27.85741 1.000 10.56982 ? 114 VAL A CG2 1 
ATOM   884  N  N   . ALA A 1 220 ? 36.70724 38.30748 25.89022 1.000 6.04553  ? 115 ALA A N   1 
ATOM   885  C  CA  . ALA A 1 220 ? 36.68801 37.24306 24.88778 1.000 6.43728  ? 115 ALA A CA  1 
ATOM   886  C  C   . ALA A 1 220 ? 35.37165 37.20266 24.14263 1.000 8.38046  ? 115 ALA A C   1 
ATOM   887  O  O   . ALA A 1 220 ? 35.33657 36.86928 22.95388 1.000 12.71365 ? 115 ALA A O   1 
ATOM   888  C  CB  . ALA A 1 220 ? 36.95170 35.87990 25.55944 1.000 8.79707  ? 115 ALA A CB  1 
ATOM   889  N  N   . SER A 1 221 ? 34.27132 37.52741 24.83109 1.000 7.31561  ? 116 SER A N   1 
ATOM   890  C  CA  . SER A 1 221 ? 32.97566 37.60139 24.17850 1.000 7.36547  ? 116 SER A CA  1 
ATOM   891  C  C   . SER A 1 221 ? 32.74976 38.94159 23.46830 1.000 10.20691 ? 116 SER A C   1 
ATOM   892  O  O   . SER A 1 221 ? 32.20579 38.98340 22.34446 1.000 10.12011 ? 116 SER A O   1 
ATOM   893  C  CB  . SER A 1 221 ? 31.87236 37.36167 25.22499 1.000 7.88800  ? 116 SER A CB  1 
ATOM   894  O  OG  . SER A 1 221 ? 30.55837 37.44239 24.64483 1.000 10.29599 ? 116 SER A OG  1 
ATOM   895  N  N   . ASP A 1 222 ? 33.06538 40.05080 24.14554 1.000 7.10004  ? 117 ASP A N   1 
ATOM   896  C  CA  . ASP A 1 222 ? 32.70093 41.35337 23.61686 1.000 7.20907  ? 117 ASP A CA  1 
ATOM   897  C  C   . ASP A 1 222 ? 33.38261 41.63805 22.28858 1.000 8.97664  ? 117 ASP A C   1 
ATOM   898  O  O   . ASP A 1 222 ? 32.82972 42.38178 21.47161 1.000 10.02316 ? 117 ASP A O   1 
ATOM   899  C  CB  . ASP A 1 222 ? 33.08610 42.42821 24.64606 1.000 7.33936  ? 117 ASP A CB  1 
ATOM   900  C  CG  . ASP A 1 222 ? 32.66028 43.83293 24.21357 1.000 9.52588  ? 117 ASP A CG  1 
ATOM   901  O  OD1 . ASP A 1 222 ? 31.43971 44.08255 24.23581 1.000 11.54079 ? 117 ASP A OD1 1 
ATOM   902  O  OD2 . ASP A 1 222 ? 33.56284 44.61877 23.83654 1.000 9.89808  ? 117 ASP A OD2 1 
ATOM   903  N  N   . LYS A 1 223 ? 34.58771 41.09466 22.06494 1.000 7.96331  ? 118 LYS A N   1 
ATOM   904  C  CA  . LYS A 1 223 ? 35.29042 41.41737 20.82182 1.000 7.93420  ? 118 LYS A CA  1 
ATOM   905  C  C   . LYS A 1 223 ? 34.48820 40.95939 19.61509 1.000 11.15565 ? 118 LYS A C   1 
ATOM   906  O  O   . LYS A 1 223 ? 34.63871 41.53232 18.52445 1.000 15.04416 ? 118 LYS A O   1 
ATOM   907  C  CB  . LYS A 1 223 ? 36.69192 40.77340 20.82140 1.000 9.77656  ? 118 LYS A CB  1 
ATOM   908  C  CG  . LYS A 1 223 ? 36.56688 39.21894 20.69053 1.000 18.14555 ? 118 LYS A CG  1 
ATOM   909  C  CD  . LYS A 1 223 ? 37.87014 38.59417 20.41417 1.000 22.50031 ? 118 LYS A CD  1 
ATOM   910  C  CE  . LYS A 1 223 ? 37.76107 37.19897 19.88340 1.000 18.88469 ? 118 LYS A CE  1 
ATOM   911  N  NZ  . LYS A 1 223 ? 37.01804 36.34300 20.79715 1.000 19.04099 ? 118 LYS A NZ  1 
ATOM   912  N  N   . ASN A 1 224 ? 33.59530 39.97705 19.79258 1.000 12.02804 ? 119 ASN A N   1 
ATOM   913  C  CA  . ASN A 1 224 ? 32.77990 39.52153 18.66535 1.000 13.80132 ? 119 ASN A CA  1 
ATOM   914  C  C   . ASN A 1 224 ? 31.69799 40.53555 18.27466 1.000 17.15337 ? 119 ASN A C   1 
ATOM   915  O  O   . ASN A 1 224 ? 31.05260 40.35255 17.23697 1.000 25.50826 ? 119 ASN A O   1 
ATOM   916  C  CB  . ASN A 1 224 ? 32.16339 38.13805 19.01557 1.000 14.73705 ? 119 ASN A CB  1 
ATOM   917  C  CG  . ASN A 1 224 ? 33.20829 37.06291 19.41579 1.000 25.54861 ? 119 ASN A CG  1 
ATOM   918  O  OD1 . ASN A 1 224 ? 32.99659 36.29716 20.37751 1.000 19.01458 ? 119 ASN A OD1 1 
ATOM   919  N  ND2 . ASN A 1 224 ? 34.30853 36.96811 18.66641 1.000 23.70856 ? 119 ASN A ND2 1 
ATOM   920  N  N   A ASN A 1 225 ? 31.49143 41.59543 19.05243 0.702 15.99191 ? 120 ASN A N   1 
ATOM   921  N  N   B ASN A 1 225 ? 31.46759 41.58686 19.06433 0.298 16.06196 ? 120 ASN A N   1 
ATOM   922  C  CA  A ASN A 1 225 ? 30.51202 42.63565 18.75844 0.702 20.70322 ? 120 ASN A CA  1 
ATOM   923  C  CA  B ASN A 1 225 ? 30.51319 42.62730 18.69411 0.298 20.71757 ? 120 ASN A CA  1 
ATOM   924  C  C   A ASN A 1 225 ? 31.14760 43.90006 18.17558 0.702 19.06850 ? 120 ASN A C   1 
ATOM   925  C  C   B ASN A 1 225 ? 31.20235 43.96185 18.40245 0.298 19.14530 ? 120 ASN A C   1 
ATOM   926  O  O   A ASN A 1 225 ? 30.42189 44.85620 17.86906 0.702 21.35055 ? 120 ASN A O   1 
ATOM   927  O  O   B ASN A 1 225 ? 30.57936 45.02466 18.52104 0.298 18.13200 ? 120 ASN A O   1 
ATOM   928  C  CB  A ASN A 1 225 ? 29.71535 43.00963 20.02754 0.702 21.31560 ? 120 ASN A CB  1 
ATOM   929  C  CB  B ASN A 1 225 ? 29.41983 42.78491 19.76436 0.298 23.01005 ? 120 ASN A CB  1 
ATOM   930  C  CG  A ASN A 1 225 ? 29.03448 41.81235 20.68793 0.702 21.00412 ? 120 ASN A CG  1 
ATOM   931  C  CG  B ASN A 1 225 ? 29.94631 43.28273 21.11209 0.298 16.89896 ? 120 ASN A CG  1 
ATOM   932  O  OD1 A ASN A 1 225 ? 28.70852 40.81294 20.03836 0.702 33.98760 ? 120 ASN A OD1 1 
ATOM   933  O  OD1 B ASN A 1 225 ? 30.68773 44.26168 21.18299 0.298 24.40614 ? 120 ASN A OD1 1 
ATOM   934  N  ND2 A ASN A 1 225 ? 28.86844 41.89386 22.00346 0.702 32.96499 ? 120 ASN A ND2 1 
ATOM   935  N  ND2 B ASN A 1 225 ? 29.52930 42.61733 22.20007 0.298 11.25473 ? 120 ASN A ND2 1 
ATOM   936  N  N   . ARG A 1 226 ? 32.47710 43.92717 18.01188 1.000 14.42654 ? 121 ARG A N   1 
ATOM   937  C  CA  . ARG A 1 226 ? 33.21741 45.14080 17.67234 1.000 12.66103 ? 121 ARG A CA  1 
ATOM   938  C  C   . ARG A 1 226 ? 33.85216 44.97431 16.30680 1.000 16.71316 ? 121 ARG A C   1 
ATOM   939  O  O   . ARG A 1 226 ? 34.17858 43.86454 15.88086 1.000 18.31501 ? 121 ARG A O   1 
ATOM   940  C  CB  . ARG A 1 226 ? 34.33756 45.45545 18.65104 1.000 12.49116 ? 121 ARG A CB  1 
ATOM   941  C  CG  . ARG A 1 226 ? 33.95770 45.41903 20.13612 1.000 17.66154 ? 121 ARG A CG  1 
ATOM   942  C  CD  . ARG A 1 226 ? 33.22460 46.67179 20.57687 1.000 16.60912 ? 121 ARG A CD  1 
ATOM   943  N  NE  . ARG A 1 226 ? 32.68670 46.56710 21.92584 1.000 14.10602 ? 121 ARG A NE  1 
ATOM   944  C  CZ  . ARG A 1 226 ? 31.73648 47.34808 22.40568 1.000 12.77642 ? 121 ARG A CZ  1 
ATOM   945  N  NH1 . ARG A 1 226 ? 31.26420 48.37795 21.70169 1.000 17.33318 ? 121 ARG A NH1 1 
ATOM   946  N  NH2 . ARG A 1 226 ? 31.17149 47.04608 23.57410 1.000 14.83947 ? 121 ARG A NH2 1 
ATOM   947  N  N   . ASN A 1 227 ? 34.05035 46.09671 15.62849 1.000 16.68750 ? 122 ASN A N   1 
ATOM   948  C  CA  . ASN A 1 227 ? 34.64945 46.08726 14.29952 1.000 15.82470 ? 122 ASN A CA  1 
ATOM   949  C  C   . ASN A 1 227 ? 36.15004 46.38943 14.44938 1.000 15.20004 ? 122 ASN A C   1 
ATOM   950  O  O   . ASN A 1 227 ? 36.56871 47.54324 14.58967 1.000 16.47232 ? 122 ASN A O   1 
ATOM   951  C  CB  . ASN A 1 227 ? 33.95751 47.09784 13.40370 1.000 19.00386 ? 122 ASN A CB  1 
ATOM   952  C  CG  . ASN A 1 227 ? 33.94325 46.64666 11.98521 1.000 32.63246 ? 122 ASN A CG  1 
ATOM   953  O  OD1 . ASN A 1 227 ? 34.98766 46.40533 11.39553 1.000 35.02038 ? 122 ASN A OD1 1 
ATOM   954  N  ND2 . ASN A 1 227 ? 32.75374 46.53022 11.41504 1.000 47.40717 ? 122 ASN A ND2 1 
ATOM   955  N  N   . CYS A 1 228 ? 36.94895 45.32998 14.43604 1.000 11.88192 ? 123 CYS A N   1 
ATOM   956  C  CA  . CYS A 1 228 ? 38.39320 45.38436 14.66457 1.000 9.20027  ? 123 CYS A CA  1 
ATOM   957  C  C   . CYS A 1 228 ? 39.06956 44.55120 13.57575 1.000 9.62342  ? 123 CYS A C   1 
ATOM   958  O  O   . CYS A 1 228 ? 39.59765 43.45128 13.83345 1.000 11.51697 ? 123 CYS A O   1 
ATOM   959  C  CB  . CYS A 1 228 ? 38.73483 44.83976 16.05247 1.000 12.87356 ? 123 CYS A CB  1 
ATOM   960  S  SG  . CYS A 1 228 ? 37.86798 45.71998 17.40144 1.000 11.68238 ? 123 CYS A SG  1 
ATOM   961  N  N   . PRO A 1 229 ? 39.05800 45.03919 12.33803 1.000 10.18252 ? 124 PRO A N   1 
ATOM   962  C  CA  . PRO A 1 229 ? 39.44829 44.17047 11.20957 1.000 11.17556 ? 124 PRO A CA  1 
ATOM   963  C  C   . PRO A 1 229 ? 40.91326 43.76548 11.24525 1.000 14.54204 ? 124 PRO A C   1 
ATOM   964  O  O   . PRO A 1 229 ? 41.25882 42.70129 10.71520 1.000 17.98781 ? 124 PRO A O   1 
ATOM   965  C  CB  . PRO A 1 229 ? 39.11155 45.02265 9.97494  1.000 14.08497 ? 124 PRO A CB  1 
ATOM   966  C  CG  . PRO A 1 229 ? 39.02283 46.42935 10.47722 1.000 14.92729 ? 124 PRO A CG  1 
ATOM   967  C  CD  . PRO A 1 229 ? 38.50930 46.33023 11.89542 1.000 9.96414  ? 124 PRO A CD  1 
ATOM   968  N  N   . LYS A 1 230 ? 41.77114 44.52835 11.90468 1.000 9.13303  ? 125 LYS A N   1 
ATOM   969  C  CA  . LYS A 1 230 ? 43.17842 44.16222 11.95809 1.000 10.23325 ? 125 LYS A CA  1 
ATOM   970  C  C   . LYS A 1 230 ? 43.52916 43.35471 13.20458 1.000 13.64177 ? 125 LYS A C   1 
ATOM   971  O  O   . LYS A 1 230 ? 44.66346 42.89175 13.30125 1.000 15.64143 ? 125 LYS A O   1 
ATOM   972  C  CB  . LYS A 1 230 ? 44.07705 45.41360 11.88307 1.000 11.43148 ? 125 LYS A CB  1 
ATOM   973  C  CG  . LYS A 1 230 ? 43.91258 46.23647 10.61825 1.000 11.22725 ? 125 LYS A CG  1 
ATOM   974  C  CD  . LYS A 1 230 ? 44.17379 45.42403 9.37484  1.000 16.18957 ? 125 LYS A CD  1 
ATOM   975  C  CE  . LYS A 1 230 ? 44.21343 46.38615 8.14556  1.000 24.99325 ? 125 LYS A CE  1 
ATOM   976  N  NZ  . LYS A 1 230 ? 44.11549 45.62581 6.88565  1.000 37.31202 ? 125 LYS A NZ  1 
ATOM   977  N  N   . GLY A 1 231 ? 42.60256 43.14496 14.13165 1.000 9.96057  ? 126 GLY A N   1 
ATOM   978  C  CA  . GLY A 1 231 ? 42.84688 42.25456 15.25239 1.000 9.56725  ? 126 GLY A CA  1 
ATOM   979  C  C   . GLY A 1 231 ? 42.64898 42.93572 16.59160 1.000 11.33407 ? 126 GLY A C   1 
ATOM   980  O  O   . GLY A 1 231 ? 42.41187 44.13717 16.68854 1.000 9.92160  ? 126 GLY A O   1 
ATOM   981  N  N   A VAL A 1 232 ? 42.77472 42.12317 17.64454 0.860 6.17483  ? 127 VAL A N   1 
ATOM   982  N  N   B VAL A 1 232 ? 42.75124 42.12441 17.64162 0.140 6.31204  ? 127 VAL A N   1 
ATOM   983  C  CA  A VAL A 1 232 ? 42.38729 42.52350 19.00070 0.860 5.57655  ? 127 VAL A CA  1 
ATOM   984  C  CA  B VAL A 1 232 ? 42.41716 42.56678 18.99011 0.140 5.57310  ? 127 VAL A CA  1 
ATOM   985  C  C   A VAL A 1 232 ? 43.51493 42.18381 19.97050 0.860 6.89845  ? 127 VAL A C   1 
ATOM   986  C  C   B VAL A 1 232 ? 43.54824 42.21065 19.94761 0.140 6.91432  ? 127 VAL A C   1 
ATOM   987  O  O   A VAL A 1 232 ? 44.04481 41.06321 19.94128 0.860 8.22720  ? 127 VAL A O   1 
ATOM   988  O  O   B VAL A 1 232 ? 44.14357 41.12997 19.85974 0.140 8.18146  ? 127 VAL A O   1 
ATOM   989  C  CB  A VAL A 1 232 ? 41.07946 41.81939 19.42671 0.860 6.21532  ? 127 VAL A CB  1 
ATOM   990  C  CB  B VAL A 1 232 ? 41.07373 41.96292 19.45774 0.140 6.51391  ? 127 VAL A CB  1 
ATOM   991  C  CG1 A VAL A 1 232 ? 40.65935 42.26097 20.82809 0.860 8.70937  ? 127 VAL A CG1 1 
ATOM   992  C  CG1 B VAL A 1 232 ? 41.12634 40.45202 19.42265 0.140 7.74767  ? 127 VAL A CG1 1 
ATOM   993  C  CG2 A VAL A 1 232 ? 39.96761 42.12278 18.45359 0.860 9.77729  ? 127 VAL A CG2 1 
ATOM   994  C  CG2 B VAL A 1 232 ? 40.70449 42.46892 20.84898 0.140 8.37559  ? 127 VAL A CG2 1 
ATOM   995  N  N   . VAL A 1 233 ? 43.84235 43.14049 20.85580 1.000 5.64159  ? 128 VAL A N   1 
ATOM   996  C  CA  . VAL A 1 233 ? 44.87170 43.02572 21.89317 1.000 4.74517  ? 128 VAL A CA  1 
ATOM   997  C  C   . VAL A 1 233 ? 44.22331 43.29913 23.24951 1.000 4.55372  ? 128 VAL A C   1 
ATOM   998  O  O   . VAL A 1 233 ? 43.25479 44.05226 23.35075 1.000 6.91164  ? 128 VAL A O   1 
ATOM   999  C  CB  . VAL A 1 233 ? 46.02602 44.04448 21.61655 1.000 6.96242  ? 128 VAL A CB  1 
ATOM   1000 C  CG1 . VAL A 1 233 ? 47.14397 43.96237 22.65455 1.000 7.68869  ? 128 VAL A CG1 1 
ATOM   1001 C  CG2 . VAL A 1 233 ? 46.58999 43.82733 20.23543 1.000 9.09630  ? 128 VAL A CG2 1 
ATOM   1002 N  N   . ALA A 1 234 ? 44.74057 42.66011 24.30376 1.000 4.62131  ? 129 ALA A N   1 
ATOM   1003 C  CA  . ALA A 1 234 ? 44.32552 42.99207 25.68012 1.000 4.32915  ? 129 ALA A CA  1 
ATOM   1004 C  C   . ALA A 1 234 ? 45.57485 43.25048 26.49475 1.000 10.03557 ? 129 ALA A C   1 
ATOM   1005 O  O   . ALA A 1 234 ? 46.52867 42.47718 26.43996 1.000 9.52723  ? 129 ALA A O   1 
ATOM   1006 C  CB  . ALA A 1 234 ? 43.50954 41.83730 26.32389 1.000 7.02766  ? 129 ALA A CB  1 
ATOM   1007 N  N   A SER A 1 235 ? 45.55809 44.31863 27.26141 0.827 4.73269  ? 130 SER A N   1 
ATOM   1008 N  N   B SER A 1 235 ? 45.57436 44.34329 27.24186 0.173 4.82396  ? 130 SER A N   1 
ATOM   1009 C  CA  A SER A 1 235 ? 46.69961 44.74547 28.07156 0.827 4.82330  ? 130 SER A CA  1 
ATOM   1010 C  CA  B SER A 1 235 ? 46.71211 44.72386 28.06866 0.173 4.93424  ? 130 SER A CA  1 
ATOM   1011 C  C   A SER A 1 235 ? 46.32076 44.63579 29.54498 0.827 5.95394  ? 130 SER A C   1 
ATOM   1012 C  C   B SER A 1 235 ? 46.31985 44.58804 29.53403 0.173 5.99646  ? 130 SER A C   1 
ATOM   1013 O  O   A SER A 1 235 ? 45.35634 45.27922 29.98166 0.827 6.94946  ? 130 SER A O   1 
ATOM   1014 O  O   B SER A 1 235 ? 45.32263 45.17421 29.97048 0.173 6.94123  ? 130 SER A O   1 
ATOM   1015 C  CB  A SER A 1 235 ? 47.05863 46.18045 27.67610 0.827 7.37963  ? 130 SER A CB  1 
ATOM   1016 C  CB  B SER A 1 235 ? 47.16213 46.14618 27.73408 0.173 7.55518  ? 130 SER A CB  1 
ATOM   1017 O  OG  A SER A 1 235 ? 48.30467 46.57094 28.24293 0.827 7.71243  ? 130 SER A OG  1 
ATOM   1018 O  OG  B SER A 1 235 ? 46.21625 47.10338 28.16422 0.173 13.04653 ? 130 SER A OG  1 
ATOM   1019 N  N   A LEU A 1 236 ? 47.07287 43.82002 30.31927 0.827 4.97843  ? 131 LEU A N   1 
ATOM   1020 N  N   B LEU A 1 236 ? 47.09745 43.80242 30.28426 0.173 5.11969  ? 131 LEU A N   1 
ATOM   1021 C  CA  A LEU A 1 236 ? 46.75158 43.55876 31.73610 0.827 6.18946  ? 131 LEU A CA  1 
ATOM   1022 C  CA  B LEU A 1 236 ? 46.84154 43.51666 31.69688 0.173 6.28258  ? 131 LEU A CA  1 
ATOM   1023 C  C   A LEU A 1 236 ? 47.92803 43.97888 32.60665 0.827 5.98230  ? 131 LEU A C   1 
ATOM   1024 C  C   B LEU A 1 236 ? 48.02180 44.01671 32.52117 0.173 6.17070  ? 131 LEU A C   1 
ATOM   1025 O  O   A LEU A 1 236 ? 48.83157 43.18139 32.84415 0.827 7.29558  ? 131 LEU A O   1 
ATOM   1026 O  O   B LEU A 1 236 ? 49.02956 43.31802 32.65686 0.173 7.37794  ? 131 LEU A O   1 
ATOM   1027 C  CB  A LEU A 1 236 ? 46.43140 42.05383 32.00064 0.827 7.57084  ? 131 LEU A CB  1 
ATOM   1028 C  CB  B LEU A 1 236 ? 46.61256 42.01924 31.91979 0.173 7.38336  ? 131 LEU A CB  1 
ATOM   1029 C  CG  A LEU A 1 236 ? 45.02063 41.71508 31.54272 0.827 9.43388  ? 131 LEU A CG  1 
ATOM   1030 C  CG  B LEU A 1 236 ? 45.30047 41.44283 31.39600 0.173 9.61642  ? 131 LEU A CG  1 
ATOM   1031 C  CD1 A LEU A 1 236 ? 45.08049 41.00119 30.21538 0.827 14.86199 ? 131 LEU A CD1 1 
ATOM   1032 C  CD1 B LEU A 1 236 ? 45.33330 39.94023 31.42225 0.173 4.63872  ? 131 LEU A CD1 1 
ATOM   1033 C  CD2 A LEU A 1 236 ? 44.28518 40.85894 32.57178 0.827 24.45155 ? 131 LEU A CD2 1 
ATOM   1034 C  CD2 B LEU A 1 236 ? 44.17577 41.93085 32.28539 0.173 11.44227 ? 131 LEU A CD2 1 
ATOM   1035 N  N   . SER A 1 237 ? 47.90475 45.22109 33.07274 1.000 6.03467  ? 132 SER A N   1 
ATOM   1036 C  CA  . SER A 1 237 ? 48.95301 45.74723 33.95988 1.000 4.43279  ? 132 SER A CA  1 
ATOM   1037 C  C   . SER A 1 237 ? 48.52388 45.53827 35.40622 1.000 8.10721  ? 132 SER A C   1 
ATOM   1038 O  O   . SER A 1 237 ? 48.23288 46.49480 36.13497 1.000 11.24148 ? 132 SER A O   1 
ATOM   1039 C  CB  . SER A 1 237 ? 49.19666 47.22520 33.67036 1.000 6.08791  ? 132 SER A CB  1 
ATOM   1040 O  OG  . SER A 1 237 ? 49.81845 47.37558 32.40479 1.000 6.27477  ? 132 SER A OG  1 
ATOM   1041 N  N   . LEU A 1 238 ? 48.46554 44.26078 35.80681 1.000 7.53687  ? 133 LEU A N   1 
ATOM   1042 C  CA  . LEU A 1 238 ? 47.98985 43.88376 37.12945 1.000 6.73603  ? 133 LEU A CA  1 
ATOM   1043 C  C   . LEU A 1 238 ? 48.48610 42.47436 37.44021 1.000 9.65648  ? 133 LEU A C   1 
ATOM   1044 O  O   . LEU A 1 238 ? 48.97360 41.74479 36.56974 1.000 11.48415 ? 133 LEU A O   1 
ATOM   1045 C  CB  . LEU A 1 238 ? 46.45152 43.97008 37.22940 1.000 11.04386 ? 133 LEU A CB  1 
ATOM   1046 C  CG  . LEU A 1 238 ? 45.66260 43.17008 36.19132 1.000 11.52404 ? 133 LEU A CG  1 
ATOM   1047 C  CD1 . LEU A 1 238 ? 45.54236 41.70006 36.55203 1.000 15.23093 ? 133 LEU A CD1 1 
ATOM   1048 C  CD2 . LEU A 1 238 ? 44.27623 43.75370 36.09964 1.000 16.57337 ? 133 LEU A CD2 1 
ATOM   1049 N  N   . GLY A 1 239 ? 48.35846 42.10322 38.70645 1.000 11.55672 ? 134 GLY A N   1 
ATOM   1050 C  CA  . GLY A 1 239 ? 48.63911 40.73752 39.08095 1.000 15.29230 ? 134 GLY A CA  1 
ATOM   1051 C  C   . GLY A 1 239 ? 48.74321 40.63188 40.58215 1.000 16.03198 ? 134 GLY A C   1 
ATOM   1052 O  O   . GLY A 1 239 ? 48.71070 41.62981 41.31647 1.000 16.94142 ? 134 GLY A O   1 
ATOM   1053 N  N   . GLY A 1 240 ? 48.94188 39.41045 41.01340 1.000 12.29852 ? 135 GLY A N   1 
ATOM   1054 C  CA  . GLY A 1 240 ? 49.09191 39.10185 42.41758 1.000 10.30934 ? 135 GLY A CA  1 
ATOM   1055 C  C   . GLY A 1 240 ? 49.70791 37.72502 42.54760 1.000 10.65543 ? 135 GLY A C   1 
ATOM   1056 O  O   . GLY A 1 240 ? 50.35570 37.23150 41.62736 1.000 11.31925 ? 135 GLY A O   1 
ATOM   1057 N  N   . GLY A 1 241 ? 49.49662 37.09902 43.69841 1.000 10.71614 ? 136 GLY A N   1 
ATOM   1058 C  CA  . GLY A 1 241 ? 50.07927 35.77694 43.92000 1.000 11.26679 ? 136 GLY A CA  1 
ATOM   1059 C  C   . GLY A 1 241 ? 49.48340 34.72665 42.99385 1.000 11.87003 ? 136 GLY A C   1 
ATOM   1060 O  O   . GLY A 1 241 ? 48.39209 34.89165 42.43231 1.000 13.30163 ? 136 GLY A O   1 
ATOM   1061 N  N   . TYR A 1 242 ? 50.23083 33.62857 42.84337 1.000 10.05889 ? 137 TYR A N   1 
ATOM   1062 C  CA  . TYR A 1 242 ? 49.86368 32.54771 41.93110 1.000 8.56112  ? 137 TYR A CA  1 
ATOM   1063 C  C   . TYR A 1 242 ? 48.44168 32.05608 42.17223 1.000 10.51998 ? 137 TYR A C   1 
ATOM   1064 O  O   . TYR A 1 242 ? 48.05078 31.74676 43.31698 1.000 12.24974 ? 137 TYR A O   1 
ATOM   1065 C  CB  . TYR A 1 242 ? 50.82496 31.35541 42.11342 1.000 10.08401 ? 137 TYR A CB  1 
ATOM   1066 C  CG  . TYR A 1 242 ? 50.47999 30.22720 41.16184 1.000 9.05053  ? 137 TYR A CG  1 
ATOM   1067 C  CD1 . TYR A 1 242 ? 50.99728 30.21283 39.87016 1.000 12.71135 ? 137 TYR A CD1 1 
ATOM   1068 C  CD2 . TYR A 1 242 ? 49.62692 29.19206 41.56173 1.000 9.50136  ? 137 TYR A CD2 1 
ATOM   1069 C  CE1 . TYR A 1 242 ? 50.65446 29.19417 38.98306 1.000 14.86799 ? 137 TYR A CE1 1 
ATOM   1070 C  CE2 . TYR A 1 242 ? 49.28286 28.17260 40.68582 1.000 14.60866 ? 137 TYR A CE2 1 
ATOM   1071 C  CZ  . TYR A 1 242 ? 49.78199 28.19306 39.41528 1.000 12.10166 ? 137 TYR A CZ  1 
ATOM   1072 O  OH  . TYR A 1 242 ? 49.43031 27.14919 38.57200 1.000 21.34257 ? 137 TYR A OH  1 
ATOM   1073 N  N   . SER A 1 243 ? 47.69094 31.93621 41.07539 1.000 9.33774  ? 138 SER A N   1 
ATOM   1074 C  CA  . SER A 1 243 ? 46.34219 31.36828 41.07740 1.000 8.52964  ? 138 SER A CA  1 
ATOM   1075 C  C   . SER A 1 243 ? 46.15933 30.61975 39.76524 1.000 10.25900 ? 138 SER A C   1 
ATOM   1076 O  O   . SER A 1 243 ? 46.27021 31.21997 38.68749 1.000 11.64049 ? 138 SER A O   1 
ATOM   1077 C  CB  . SER A 1 243 ? 45.28308 32.47984 41.17020 1.000 13.46207 ? 138 SER A CB  1 
ATOM   1078 O  OG  . SER A 1 243 ? 43.97078 31.98427 40.80850 1.000 14.12621 ? 138 SER A OG  1 
ATOM   1079 N  N   A SER A 1 244 ? 45.86748 29.31891 39.85041 0.629 10.92160 ? 139 SER A N   1 
ATOM   1080 N  N   B SER A 1 244 ? 45.86666 29.32128 39.85731 0.371 10.92454 ? 139 SER A N   1 
ATOM   1081 C  CA  A SER A 1 244 ? 45.65870 28.57305 38.62025 0.629 9.49406  ? 139 SER A CA  1 
ATOM   1082 C  CA  B SER A 1 244 ? 45.61841 28.55215 38.64741 0.371 9.55152  ? 139 SER A CA  1 
ATOM   1083 C  C   A SER A 1 244 ? 44.39485 29.04223 37.90110 0.629 10.36667 ? 139 SER A C   1 
ATOM   1084 C  C   B SER A 1 244 ? 44.40626 29.08145 37.88757 0.371 10.38976 ? 139 SER A C   1 
ATOM   1085 O  O   A SER A 1 244 ? 44.35043 28.99983 36.66987 0.629 11.47362 ? 139 SER A O   1 
ATOM   1086 O  O   B SER A 1 244 ? 44.41440 29.09234 36.65253 0.371 11.28189 ? 139 SER A O   1 
ATOM   1087 C  CB  A SER A 1 244 ? 45.60706 27.07739 38.90237 0.629 12.23518 ? 139 SER A CB  1 
ATOM   1088 C  CB  B SER A 1 244 ? 45.43732 27.08062 38.99179 0.371 12.40450 ? 139 SER A CB  1 
ATOM   1089 O  OG  A SER A 1 244 ? 44.51677 26.73045 39.73830 0.629 15.15143 ? 139 SER A OG  1 
ATOM   1090 O  OG  B SER A 1 244 ? 45.15404 26.33066 37.82437 0.371 14.46933 ? 139 SER A OG  1 
ATOM   1091 N  N   A SER A 1 245 ? 43.39256 29.54084 38.63468 0.629 10.02578 ? 140 SER A N   1 
ATOM   1092 N  N   B SER A 1 245 ? 43.37931 29.55872 38.59805 0.371 10.16615 ? 140 SER A N   1 
ATOM   1093 C  CA  A SER A 1 245 ? 42.18176 30.01796 37.95367 0.629 8.91417  ? 140 SER A CA  1 
ATOM   1094 C  CA  B SER A 1 245 ? 42.17262 30.00904 37.90073 0.371 8.91187  ? 140 SER A CA  1 
ATOM   1095 C  C   A SER A 1 245 ? 42.44680 31.29507 37.16796 0.629 9.20785  ? 140 SER A C   1 
ATOM   1096 C  C   B SER A 1 245 ? 42.37821 31.34659 37.19899 0.371 9.20577  ? 140 SER A C   1 
ATOM   1097 O  O   A SER A 1 245 ? 41.90384 31.47657 36.06999 0.629 9.79302  ? 140 SER A O   1 
ATOM   1098 O  O   B SER A 1 245 ? 41.72517 31.61392 36.18222 0.371 9.91000  ? 140 SER A O   1 
ATOM   1099 C  CB  A SER A 1 245 ? 41.03944 30.26178 38.93972 0.629 10.76819 ? 140 SER A CB  1 
ATOM   1100 C  CB  B SER A 1 245 ? 40.98544 30.10184 38.86124 0.371 10.44793 ? 140 SER A CB  1 
ATOM   1101 O  OG  A SER A 1 245 ? 40.85335 29.16056 39.80291 0.629 20.08443 ? 140 SER A OG  1 
ATOM   1102 O  OG  B SER A 1 245 ? 41.29300 30.90160 39.99097 0.371 13.27580 ? 140 SER A OG  1 
ATOM   1103 N  N   . VAL A 1 246 ? 43.26683 32.20515 37.71424 1.000 7.40003  ? 141 VAL A N   1 
ATOM   1104 C  CA  . VAL A 1 246 ? 43.58517 33.43453 37.00067 1.000 6.86358  ? 141 VAL A CA  1 
ATOM   1105 C  C   . VAL A 1 246 ? 44.41875 33.10164 35.77656 1.000 6.99470  ? 141 VAL A C   1 
ATOM   1106 O  O   . VAL A 1 246 ? 44.17621 33.63541 34.69753 1.000 8.89129  ? 141 VAL A O   1 
ATOM   1107 C  CB  . VAL A 1 246 ? 44.31083 34.43293 37.92794 1.000 8.82522  ? 141 VAL A CB  1 
ATOM   1108 C  CG1 . VAL A 1 246 ? 44.79593 35.65055 37.12667 1.000 9.50588  ? 141 VAL A CG1 1 
ATOM   1109 C  CG2 . VAL A 1 246 ? 43.37745 34.86465 39.03334 1.000 10.47953 ? 141 VAL A CG2 1 
ATOM   1110 N  N   . ASN A 1 247 ? 45.35295 32.14651 35.90655 1.000 7.86538  ? 142 ASN A N   1 
ATOM   1111 C  CA  . ASN A 1 247 ? 46.14500 31.77823 34.73313 1.000 7.59973  ? 142 ASN A CA  1 
ATOM   1112 C  C   . ASN A 1 247 ? 45.25346 31.18932 33.66376 1.000 7.87143  ? 142 ASN A C   1 
ATOM   1113 O  O   . ASN A 1 247 ? 45.42420 31.48192 32.46452 1.000 8.24987  ? 142 ASN A O   1 
ATOM   1114 C  CB  . ASN A 1 247 ? 47.23825 30.77737 35.08932 1.000 8.31165  ? 142 ASN A CB  1 
ATOM   1115 C  CG  . ASN A 1 247 ? 48.42822 31.42767 35.77416 1.000 10.20502 ? 142 ASN A CG  1 
ATOM   1116 O  OD1 . ASN A 1 247 ? 48.39635 32.59855 36.16215 1.000 10.14488 ? 142 ASN A OD1 1 
ATOM   1117 N  ND2 . ASN A 1 247 ? 49.49806 30.63801 35.94788 1.000 10.58979 ? 142 ASN A ND2 1 
ATOM   1118 N  N   A SER A 1 248 ? 44.29453 30.36718 34.07900 0.613 9.21282  ? 143 SER A N   1 
ATOM   1119 N  N   B SER A 1 248 ? 44.31038 30.33446 34.06521 0.387 9.23754  ? 143 SER A N   1 
ATOM   1120 C  CA  A SER A 1 248 ? 43.42629 29.69988 33.12435 0.613 7.86937  ? 143 SER A CA  1 
ATOM   1121 C  CA  B SER A 1 248 ? 43.42497 29.70347 33.09350 0.387 7.92168  ? 143 SER A CA  1 
ATOM   1122 C  C   A SER A 1 248 ? 42.57441 30.71919 32.38385 0.613 10.23529 ? 143 SER A C   1 
ATOM   1123 C  C   B SER A 1 248 ? 42.58581 30.74051 32.36721 0.387 10.18317 ? 143 SER A C   1 
ATOM   1124 O  O   A SER A 1 248 ? 42.32464 30.56640 31.18110 0.613 9.73488  ? 143 SER A O   1 
ATOM   1125 O  O   B SER A 1 248 ? 42.34814 30.61682 31.15955 0.387 9.74014  ? 143 SER A O   1 
ATOM   1126 C  CB  A SER A 1 248 ? 42.54903 28.67476 33.84334 0.613 10.08774 ? 143 SER A CB  1 
ATOM   1127 C  CB  B SER A 1 248 ? 42.52785 28.66897 33.77426 0.387 10.10106 ? 143 SER A CB  1 
ATOM   1128 O  OG  A SER A 1 248 ? 41.64809 28.07384 32.93975 0.613 14.72626 ? 143 SER A OG  1 
ATOM   1129 O  OG  B SER A 1 248 ? 43.30658 27.62610 34.32598 0.387 15.73394 ? 143 SER A OG  1 
ATOM   1130 N  N   . ALA A 1 249 ? 42.11871 31.76951 33.07998 1.000 6.68018  ? 144 ALA A N   1 
ATOM   1131 C  CA  . ALA A 1 249 ? 41.35179 32.80620 32.40541 1.000 6.40896  ? 144 ALA A CA  1 
ATOM   1132 C  C   . ALA A 1 249 ? 42.18499 33.55075 31.36728 1.000 8.00464  ? 144 ALA A C   1 
ATOM   1133 O  O   . ALA A 1 249 ? 41.68998 33.85547 30.27415 1.000 7.00407  ? 144 ALA A O   1 
ATOM   1134 C  CB  . ALA A 1 249 ? 40.76113 33.78824 33.43841 1.000 10.42379 ? 144 ALA A CB  1 
ATOM   1135 N  N   . ALA A 1 250 ? 43.47550 33.79502 31.66240 1.000 6.72751  ? 145 ALA A N   1 
ATOM   1136 C  CA  . ALA A 1 250 ? 44.32176 34.45786 30.66935 1.000 5.52462  ? 145 ALA A CA  1 
ATOM   1137 C  C   . ALA A 1 250 ? 44.54533 33.55821 29.45324 1.000 6.29796  ? 145 ALA A C   1 
ATOM   1138 O  O   . ALA A 1 250 ? 44.55528 34.04263 28.30853 1.000 6.18809  ? 145 ALA A O   1 
ATOM   1139 C  CB  . ALA A 1 250 ? 45.64362 34.85009 31.34765 1.000 7.66153  ? 145 ALA A CB  1 
ATOM   1140 N  N   . ALA A 1 251 ? 44.80024 32.26539 29.69672 1.000 6.69054  ? 146 ALA A N   1 
ATOM   1141 C  CA  . ALA A 1 251 ? 44.94419 31.29543 28.60901 1.000 7.40233  ? 146 ALA A CA  1 
ATOM   1142 C  C   . ALA A 1 251 ? 43.68346 31.23116 27.74096 1.000 7.17221  ? 146 ALA A C   1 
ATOM   1143 O  O   . ALA A 1 251 ? 43.78318 31.13331 26.50602 1.000 8.30567  ? 146 ALA A O   1 
ATOM   1144 C  CB  . ALA A 1 251 ? 45.27153 29.91660 29.19095 1.000 7.30011  ? 146 ALA A CB  1 
ATOM   1145 N  N   . ARG A 1 252 ? 42.49154 31.29959 28.35778 1.000 6.44057  ? 147 ARG A N   1 
ATOM   1146 C  CA  . ARG A 1 252 ? 41.25668 31.28614 27.56920 1.000 6.52294  ? 147 ARG A CA  1 
ATOM   1147 C  C   . ARG A 1 252 ? 41.17537 32.51190 26.68004 1.000 7.57515  ? 147 ARG A C   1 
ATOM   1148 O  O   . ARG A 1 252 ? 40.77485 32.41605 25.50797 1.000 8.38657  ? 147 ARG A O   1 
ATOM   1149 C  CB  . ARG A 1 252 ? 40.01647 31.25314 28.49136 1.000 9.69557  ? 147 ARG A CB  1 
ATOM   1150 C  CG  . ARG A 1 252 ? 39.74130 29.95288 29.17375 1.000 13.75926 ? 147 ARG A CG  1 
ATOM   1151 C  CD  . ARG A 1 252 ? 38.25595 29.96924 29.68794 1.000 10.78290 ? 147 ARG A CD  1 
ATOM   1152 N  NE  . ARG A 1 252 ? 38.02128 30.99182 30.71316 1.000 9.85153  ? 147 ARG A NE  1 
ATOM   1153 C  CZ  . ARG A 1 252 ? 38.31111 30.83134 32.00243 1.000 11.24162 ? 147 ARG A CZ  1 
ATOM   1154 N  NH1 . ARG A 1 252 ? 38.95570 29.76883 32.44845 1.000 11.31510 ? 147 ARG A NH1 1 
ATOM   1155 N  NH2 . ARG A 1 252 ? 37.92763 31.76826 32.88513 1.000 9.28454  ? 147 ARG A NH2 1 
ATOM   1156 N  N   . LEU A 1 253 ? 41.48432 33.69154 27.23998 1.000 6.12609  ? 148 LEU A N   1 
ATOM   1157 C  CA  . LEU A 1 253 ? 41.41393 34.90708 26.44905 1.000 5.64125  ? 148 LEU A CA  1 
ATOM   1158 C  C   . LEU A 1 253 ? 42.35520 34.83543 25.24419 1.000 6.76545  ? 148 LEU A C   1 
ATOM   1159 O  O   . LEU A 1 253 ? 41.95743 35.14469 24.11318 1.000 7.49937  ? 148 LEU A O   1 
ATOM   1160 C  CB  . LEU A 1 253 ? 41.71700 36.10327 27.36731 1.000 7.08249  ? 148 LEU A CB  1 
ATOM   1161 C  CG  . LEU A 1 253 ? 41.61918 37.49749 26.72002 1.000 7.25256  ? 148 LEU A CG  1 
ATOM   1162 C  CD1 . LEU A 1 253 ? 40.25378 37.78445 26.06067 1.000 9.42181  ? 148 LEU A CD1 1 
ATOM   1163 C  CD2 . LEU A 1 253 ? 41.97086 38.53383 27.75815 1.000 9.71678  ? 148 LEU A CD2 1 
ATOM   1164 N  N   . GLN A 1 254 ? 43.57381 34.35659 25.45843 1.000 7.12016  ? 149 GLN A N   1 
ATOM   1165 C  CA  . GLN A 1 254 ? 44.52414 34.19493 24.35580 1.000 7.12655  ? 149 GLN A CA  1 
ATOM   1166 C  C   . GLN A 1 254 ? 43.98813 33.20885 23.31108 1.000 8.05192  ? 149 GLN A C   1 
ATOM   1167 O  O   . GLN A 1 254 ? 44.01815 33.48366 22.09980 1.000 7.80158  ? 149 GLN A O   1 
ATOM   1168 C  CB  . GLN A 1 254 ? 45.87516 33.74387 24.95514 1.000 6.69922  ? 149 GLN A CB  1 
ATOM   1169 C  CG  . GLN A 1 254 ? 46.93512 33.43192 23.90594 1.000 8.67418  ? 149 GLN A CG  1 
ATOM   1170 C  CD  . GLN A 1 254 ? 47.49453 34.67751 23.25096 1.000 8.41104  ? 149 GLN A CD  1 
ATOM   1171 O  OE1 . GLN A 1 254 ? 47.76235 35.69427 23.89877 1.000 7.61021  ? 149 GLN A OE1 1 
ATOM   1172 N  NE2 . GLN A 1 254 ? 47.63986 34.60718 21.92367 1.000 13.29727 ? 149 GLN A NE2 1 
ATOM   1173 N  N   A SER A 1 255 ? 43.46389 32.07011 23.77831 0.519 7.14796  ? 150 SER A N   1 
ATOM   1174 N  N   B SER A 1 255 ? 43.47042 32.06356 23.74776 0.481 7.18179  ? 150 SER A N   1 
ATOM   1175 C  CA  A SER A 1 255 ? 42.93685 31.04083 22.88259 0.519 6.69270  ? 150 SER A CA  1 
ATOM   1176 C  CA  B SER A 1 255 ? 43.02212 31.08955 22.75373 0.481 6.68694  ? 150 SER A CA  1 
ATOM   1177 C  C   A SER A 1 255 ? 41.79475 31.57065 22.02105 0.519 8.25401  ? 150 SER A C   1 
ATOM   1178 C  C   B SER A 1 255 ? 41.76057 31.53987 22.01161 0.481 8.33260  ? 150 SER A C   1 
ATOM   1179 O  O   A SER A 1 255 ? 41.62327 31.13751 20.86826 0.519 11.17669 ? 150 SER A O   1 
ATOM   1180 O  O   B SER A 1 255 ? 41.47618 31.01266 20.92358 0.481 10.56975 ? 150 SER A O   1 
ATOM   1181 C  CB  A SER A 1 255 ? 42.47975 29.84453 23.72687 0.519 8.53125  ? 150 SER A CB  1 
ATOM   1182 C  CB  B SER A 1 255 ? 42.81110 29.73517 23.42601 0.481 12.03260 ? 150 SER A CB  1 
ATOM   1183 O  OG  A SER A 1 255 ? 41.67072 28.92287 23.00368 0.519 10.75713 ? 150 SER A OG  1 
ATOM   1184 O  OG  B SER A 1 255 ? 41.62950 29.75751 24.18549 0.481 11.20362 ? 150 SER A OG  1 
ATOM   1185 N  N   . SER A 1 256 ? 41.00040 32.49455 22.56186 1.000 7.10044  ? 151 SER A N   1 
ATOM   1186 C  CA  . SER A 1 256 ? 39.84051 33.04212 21.85169 1.000 6.72680  ? 151 SER A CA  1 
ATOM   1187 C  C   . SER A 1 256 ? 40.21622 33.93659 20.67652 1.000 9.27475  ? 151 SER A C   1 
ATOM   1188 O  O   . SER A 1 256 ? 39.31998 34.35031 19.92107 1.000 11.14122 ? 151 SER A O   1 
ATOM   1189 C  CB  . SER A 1 256 ? 38.97252 33.82321 22.83682 1.000 7.30906  ? 151 SER A CB  1 
ATOM   1190 O  OG  . SER A 1 256 ? 39.41257 35.17008 22.98874 1.000 9.10791  ? 151 SER A OG  1 
ATOM   1191 N  N   . GLY A 1 257 ? 41.49794 34.25264 20.51444 1.000 8.15227  ? 152 GLY A N   1 
ATOM   1192 C  CA  . GLY A 1 257 ? 41.98158 35.04210 19.38338 1.000 8.52295  ? 152 GLY A CA  1 
ATOM   1193 C  C   . GLY A 1 257 ? 42.39824 36.45904 19.73226 1.000 8.07430  ? 152 GLY A C   1 
ATOM   1194 O  O   . GLY A 1 257 ? 42.32094 37.34341 18.87158 1.000 14.72719 ? 152 GLY A O   1 
ATOM   1195 N  N   . VAL A 1 258 ? 42.78442 36.70475 20.97933 1.000 6.91595  ? 153 VAL A N   1 
ATOM   1196 C  CA  . VAL A 1 258 ? 43.17786 38.02844 21.46769 1.000 6.55301  ? 153 VAL A CA  1 
ATOM   1197 C  C   . VAL A 1 258 ? 44.64822 37.93093 21.85681 1.000 8.73629  ? 153 VAL A C   1 
ATOM   1198 O  O   . VAL A 1 258 ? 45.03387 37.00014 22.56566 1.000 8.94247  ? 153 VAL A O   1 
ATOM   1199 C  CB  . VAL A 1 258 ? 42.32223 38.42694 22.68709 1.000 6.88331  ? 153 VAL A CB  1 
ATOM   1200 C  CG1 . VAL A 1 258 ? 42.81326 39.75336 23.29622 1.000 8.52541  ? 153 VAL A CG1 1 
ATOM   1201 C  CG2 . VAL A 1 258 ? 40.83406 38.59439 22.30756 1.000 9.46627  ? 153 VAL A CG2 1 
ATOM   1202 N  N   . MET A 1 259 ? 45.46609 38.90958 21.44948 1.000 5.07441  ? 154 MET A N   1 
ATOM   1203 C  CA  . MET A 1 259 ? 46.84847 38.96577 21.89540 1.000 6.47246  ? 154 MET A CA  1 
ATOM   1204 C  C   . MET A 1 259 ? 46.86333 39.46792 23.32718 1.000 6.54302  ? 154 MET A C   1 
ATOM   1205 O  O   . MET A 1 259 ? 46.51771 40.61979 23.56510 1.000 6.55991  ? 154 MET A O   1 
ATOM   1206 C  CB  . MET A 1 259 ? 47.63803 39.89976 20.98181 1.000 7.35183  ? 154 MET A CB  1 
ATOM   1207 C  CG  . MET A 1 259 ? 49.15984 39.78266 21.13770 1.000 12.80222 ? 154 MET A CG  1 
ATOM   1208 S  SD  . MET A 1 259 ? 49.74752 40.73822 22.60399 1.000 11.45819 ? 154 MET A SD  1 
ATOM   1209 C  CE  . MET A 1 259 ? 51.52860 40.35213 22.45402 1.000 14.06606 ? 154 MET A CE  1 
ATOM   1210 N  N   . VAL A 1 260 ? 47.26498 38.62810 24.28435 1.000 4.66713  ? 155 VAL A N   1 
ATOM   1211 C  CA  . VAL A 1 260 ? 47.25544 39.02529 25.69634 1.000 4.50653  ? 155 VAL A CA  1 
ATOM   1212 C  C   . VAL A 1 260 ? 48.66882 39.38477 26.13254 1.000 6.91119  ? 155 VAL A C   1 
ATOM   1213 O  O   . VAL A 1 260 ? 49.57836 38.53590 26.08609 1.000 7.23852  ? 155 VAL A O   1 
ATOM   1214 C  CB  . VAL A 1 260 ? 46.69594 37.90267 26.57074 1.000 4.64531  ? 155 VAL A CB  1 
ATOM   1215 C  CG1 . VAL A 1 260 ? 46.67590 38.33162 28.02270 1.000 8.12258  ? 155 VAL A CG1 1 
ATOM   1216 C  CG2 . VAL A 1 260 ? 45.28578 37.52679 26.10061 1.000 7.26447  ? 155 VAL A CG2 1 
ATOM   1217 N  N   . ALA A 1 261 ? 48.84687 40.61237 26.62779 1.000 4.69751  ? 156 ALA A N   1 
ATOM   1218 C  CA  . ALA A 1 261 ? 50.11116 41.03726 27.22457 1.000 4.23727  ? 156 ALA A CA  1 
ATOM   1219 C  C   . ALA A 1 261 ? 49.89171 41.30255 28.70502 1.000 5.19781  ? 156 ALA A C   1 
ATOM   1220 O  O   . ALA A 1 261 ? 48.91204 41.97152 29.07039 1.000 6.57268  ? 156 ALA A O   1 
ATOM   1221 C  CB  . ALA A 1 261 ? 50.59810 42.31740 26.54293 1.000 8.04140  ? 156 ALA A CB  1 
ATOM   1222 N  N   . VAL A 1 262 ? 50.77120 40.76155 29.55546 1.000 4.32843  ? 157 VAL A N   1 
ATOM   1223 C  CA  . VAL A 1 262 ? 50.58850 40.90913 31.00119 1.000 5.50053  ? 157 VAL A CA  1 
ATOM   1224 C  C   . VAL A 1 262 ? 51.88321 41.36353 31.66177 1.000 6.68404  ? 157 VAL A C   1 
ATOM   1225 O  O   . VAL A 1 262 ? 52.99396 41.02957 31.22643 1.000 6.61835  ? 157 VAL A O   1 
ATOM   1226 C  CB  . VAL A 1 262 ? 50.09696 39.61582 31.69785 1.000 7.46621  ? 157 VAL A CB  1 
ATOM   1227 C  CG1 . VAL A 1 262 ? 48.88430 39.05343 30.96954 1.000 7.93822  ? 157 VAL A CG1 1 
ATOM   1228 C  CG2 . VAL A 1 262 ? 51.18690 38.57690 31.77525 1.000 14.63750 ? 157 VAL A CG2 1 
ATOM   1229 N  N   . ALA A 1 263 ? 51.73512 42.09740 32.76942 1.000 5.16137  ? 158 ALA A N   1 
ATOM   1230 C  CA  . ALA A 1 263 ? 52.91648 42.57335 33.48847 1.000 4.69258  ? 158 ALA A CA  1 
ATOM   1231 C  C   . ALA A 1 263 ? 53.61887 41.46014 34.25755 1.000 6.16648  ? 158 ALA A C   1 
ATOM   1232 O  O   . ALA A 1 263 ? 52.97068 40.60841 34.89289 1.000 7.55253  ? 158 ALA A O   1 
ATOM   1233 C  CB  . ALA A 1 263 ? 52.51012 43.68769 34.44591 1.000 6.62288  ? 158 ALA A CB  1 
ATOM   1234 N  N   . ALA A 1 264 ? 54.97736 41.50443 34.26982 1.000 5.24032  ? 159 ALA A N   1 
ATOM   1235 C  CA  . ALA A 1 264 ? 55.67422 40.46085 35.01455 1.000 6.26495  ? 159 ALA A CA  1 
ATOM   1236 C  C   . ALA A 1 264 ? 55.55851 40.63342 36.53573 1.000 7.96433  ? 159 ALA A C   1 
ATOM   1237 O  O   . ALA A 1 264 ? 55.67125 39.64204 37.27214 1.000 8.24333  ? 159 ALA A O   1 
ATOM   1238 C  CB  . ALA A 1 264 ? 57.15931 40.41500 34.63992 1.000 7.88214  ? 159 ALA A CB  1 
ATOM   1239 N  N   . GLY A 1 265 ? 55.36562 41.86006 37.02049 1.000 7.70766  ? 160 GLY A N   1 
ATOM   1240 C  CA  . GLY A 1 265 ? 55.29977 42.15478 38.43761 1.000 8.07317  ? 160 GLY A CA  1 
ATOM   1241 C  C   . GLY A 1 265 ? 56.53402 42.89745 38.92784 1.000 9.19370  ? 160 GLY A C   1 
ATOM   1242 O  O   . GLY A 1 265 ? 57.58921 42.90155 38.28932 1.000 7.86304  ? 160 GLY A O   1 
ATOM   1243 N  N   . ASN A 1 266 ? 56.38848 43.54993 40.09965 1.000 7.90058  ? 161 ASN A N   1 
ATOM   1244 C  CA  . ASN A 1 266 ? 57.37723 44.51345 40.60326 1.000 7.78065  ? 161 ASN A CA  1 
ATOM   1245 C  C   . ASN A 1 266 ? 58.03753 44.08333 41.90254 1.000 10.49056 ? 161 ASN A C   1 
ATOM   1246 O  O   . ASN A 1 266 ? 58.35230 44.93671 42.74246 1.000 12.85803 ? 161 ASN A O   1 
ATOM   1247 C  CB  . ASN A 1 266 ? 56.75027 45.89992 40.79530 1.000 8.49389  ? 161 ASN A CB  1 
ATOM   1248 C  CG  . ASN A 1 266 ? 56.06217 46.43855 39.54924 1.000 16.62944 ? 161 ASN A CG  1 
ATOM   1249 O  OD1 . ASN A 1 266 ? 56.45066 46.13644 38.42662 1.000 15.29028 ? 161 ASN A OD1 1 
ATOM   1250 N  ND2 . ASN A 1 266 ? 54.97539 47.17350 39.74637 1.000 35.22880 ? 161 ASN A ND2 1 
ATOM   1251 N  N   . ASN A 1 267 ? 58.33265 42.77972 42.07747 1.000 7.77777  ? 162 ASN A N   1 
ATOM   1252 C  CA  . ASN A 1 267 ? 58.89072 42.27641 43.34018 1.000 8.45425  ? 162 ASN A CA  1 
ATOM   1253 C  C   . ASN A 1 267 ? 60.36132 41.88255 43.25700 1.000 13.18284 ? 162 ASN A C   1 
ATOM   1254 O  O   . ASN A 1 267 ? 60.88580 41.26573 44.21057 1.000 12.97122 ? 162 ASN A O   1 
ATOM   1255 C  CB  . ASN A 1 267 ? 58.08916 41.05030 43.80227 1.000 13.69556 ? 162 ASN A CB  1 
ATOM   1256 C  CG  . ASN A 1 267 ? 56.58252 41.17711 43.51611 1.000 36.55968 ? 162 ASN A CG  1 
ATOM   1257 O  OD1 . ASN A 1 267 ? 56.05833 40.76993 42.44572 1.000 26.32259 ? 162 ASN A OD1 1 
ATOM   1258 N  ND2 . ASN A 1 267 ? 55.88362 41.77587 44.46989 1.000 25.45610 ? 162 ASN A ND2 1 
ATOM   1259 N  N   . ASN A 1 268 ? 61.03462 42.18612 42.14135 1.000 9.91945  ? 163 ASN A N   1 
ATOM   1260 C  CA  . ASN A 1 268 ? 62.43352 41.77285 41.93863 1.000 8.93657  ? 163 ASN A CA  1 
ATOM   1261 C  C   . ASN A 1 268 ? 62.60647 40.28810 42.27578 1.000 9.34122  ? 163 ASN A C   1 
ATOM   1262 O  O   . ASN A 1 268 ? 63.51734 39.87108 43.01461 1.000 11.66975 ? 163 ASN A O   1 
ATOM   1263 C  CB  . ASN A 1 268 ? 63.37945 42.66072 42.75937 1.000 9.44561  ? 163 ASN A CB  1 
ATOM   1264 C  CG  . ASN A 1 268 ? 64.82884 42.39113 42.47569 1.000 12.01067 ? 163 ASN A CG  1 
ATOM   1265 O  OD1 . ASN A 1 268 ? 65.20033 42.09636 41.35551 1.000 12.53755 ? 163 ASN A OD1 1 
ATOM   1266 N  ND2 . ASN A 1 268 ? 65.66447 42.43239 43.52190 1.000 13.28022 ? 163 ASN A ND2 1 
ATOM   1267 N  N   . ALA A 1 269 ? 61.67694 39.47863 41.74331 1.000 9.16581  ? 164 ALA A N   1 
ATOM   1268 C  CA  . ALA A 1 269 ? 61.63498 38.05685 42.06754 1.000 9.89581  ? 164 ALA A CA  1 
ATOM   1269 C  C   . ALA A 1 269 ? 61.27529 37.27254 40.81320 1.000 9.34042  ? 164 ALA A C   1 
ATOM   1270 O  O   . ALA A 1 269 ? 60.97179 37.84350 39.75529 1.000 11.33352 ? 164 ALA A O   1 
ATOM   1271 C  CB  . ALA A 1 269 ? 60.60466 37.80205 43.17529 1.000 14.64107 ? 164 ALA A CB  1 
ATOM   1272 N  N   . ASP A 1 270 ? 61.28881 35.94077 40.94444 1.000 12.32576 ? 165 ASP A N   1 
ATOM   1273 C  CA  . ASP A 1 270 ? 60.89840 35.08347 39.82909 1.000 9.12653  ? 165 ASP A CA  1 
ATOM   1274 C  C   . ASP A 1 270 ? 59.39443 35.16630 39.62126 1.000 8.89726  ? 165 ASP A C   1 
ATOM   1275 O  O   . ASP A 1 270 ? 58.61530 34.91749 40.55552 1.000 11.27855 ? 165 ASP A O   1 
ATOM   1276 C  CB  . ASP A 1 270 ? 61.32279 33.64641 40.10419 1.000 12.00242 ? 165 ASP A CB  1 
ATOM   1277 C  CG  . ASP A 1 270 ? 61.32535 32.78396 38.83812 1.000 16.88404 ? 165 ASP A CG  1 
ATOM   1278 O  OD1 . ASP A 1 270 ? 60.32315 32.79122 38.10126 1.000 15.77346 ? 165 ASP A OD1 1 
ATOM   1279 O  OD2 . ASP A 1 270 ? 62.32442 32.06110 38.57821 1.000 23.39083 ? 165 ASP A OD2 1 
ATOM   1280 N  N   . ALA A 1 271 ? 58.99529 35.51709 38.39490 1.000 7.99982  ? 166 ALA A N   1 
ATOM   1281 C  CA  . ALA A 1 271 ? 57.58861 35.69709 38.06030 1.000 8.56523  ? 166 ALA A CA  1 
ATOM   1282 C  C   . ALA A 1 271 ? 56.78275 34.40895 38.08597 1.000 9.73824  ? 166 ALA A C   1 
ATOM   1283 O  O   . ALA A 1 271 ? 55.55457 34.50400 37.96451 1.000 9.78673  ? 166 ALA A O   1 
ATOM   1284 C  CB  . ALA A 1 271 ? 57.47111 36.36344 36.67796 1.000 9.58296  ? 166 ALA A CB  1 
ATOM   1285 N  N   . ARG A 1 272 ? 57.42640 33.23580 38.27879 1.000 10.41680 ? 167 ARG A N   1 
ATOM   1286 C  CA  . ARG A 1 272 ? 56.69348 31.96439 38.34212 1.000 10.17357 ? 167 ARG A CA  1 
ATOM   1287 C  C   . ARG A 1 272 ? 55.72008 31.93955 39.51037 1.000 11.88628 ? 167 ARG A C   1 
ATOM   1288 O  O   . ARG A 1 272 ? 54.77599 31.13548 39.51064 1.000 10.80400 ? 167 ARG A O   1 
ATOM   1289 C  CB  . ARG A 1 272 ? 57.68706 30.80577 38.43765 1.000 13.56265 ? 167 ARG A CB  1 
ATOM   1290 C  CG  . ARG A 1 272 ? 58.32390 30.72293 39.80797 1.000 20.96599 ? 167 ARG A CG  1 
ATOM   1291 C  CD  . ARG A 1 272 ? 59.26856 29.51059 39.96651 1.000 49.21177 ? 167 ARG A CD  1 
ATOM   1292 N  NE  . ARG A 1 272 ? 60.16778 29.36313 38.82943 1.000 57.07167 ? 167 ARG A NE  1 
ATOM   1293 C  CZ  . ARG A 1 272 ? 60.49423 28.20097 38.28212 1.000 65.72265 ? 167 ARG A CZ  1 
ATOM   1294 N  NH1 . ARG A 1 272 ? 60.07809 27.05253 38.79714 1.000 49.97604 ? 167 ARG A NH1 1 
ATOM   1295 N  NH2 . ARG A 1 272 ? 61.26583 28.18975 37.19762 1.000 65.92122 ? 167 ARG A NH2 1 
ATOM   1296 N  N   . ASN A 1 273 ? 55.89321 32.82127 40.49625 1.000 8.71248  ? 168 ASN A N   1 
ATOM   1297 C  CA  . ASN A 1 273 ? 55.03411 32.79706 41.66652 1.000 9.91329  ? 168 ASN A CA  1 
ATOM   1298 C  C   . ASN A 1 273 ? 53.92941 33.84324 41.61130 1.000 8.48499  ? 168 ASN A C   1 
ATOM   1299 O  O   . ASN A 1 273 ? 53.29224 34.11165 42.64113 1.000 11.24260 ? 168 ASN A O   1 
ATOM   1300 C  CB  . ASN A 1 273 ? 55.87132 32.98097 42.92556 1.000 9.57051  ? 168 ASN A CB  1 
ATOM   1301 C  CG  . ASN A 1 273 ? 56.64095 31.72870 43.27671 1.000 18.63288 ? 168 ASN A CG  1 
ATOM   1302 O  OD1 . ASN A 1 273 ? 56.16594 30.60456 43.05525 1.000 17.60076 ? 168 ASN A OD1 1 
ATOM   1303 N  ND2 . ASN A 1 273 ? 57.84391 31.90480 43.81674 1.000 14.00672 ? 168 ASN A ND2 1 
ATOM   1304 N  N   . TYR A 1 274 ? 53.67640 34.43243 40.44733 1.000 8.80160  ? 169 TYR A N   1 
ATOM   1305 C  CA  . TYR A 1 274 ? 52.67852 35.48005 40.30007 1.000 7.83501  ? 169 TYR A CA  1 
ATOM   1306 C  C   . TYR A 1 274 ? 51.76108 35.18881 39.12031 1.000 8.23996  ? 169 TYR A C   1 
ATOM   1307 O  O   . TYR A 1 274 ? 52.15292 34.51051 38.16618 1.000 9.74893  ? 169 TYR A O   1 
ATOM   1308 C  CB  . TYR A 1 274 ? 53.37651 36.86928 40.09217 1.000 11.70369 ? 169 TYR A CB  1 
ATOM   1309 C  CG  . TYR A 1 274 ? 54.23387 37.20329 41.28811 1.000 8.71291  ? 169 TYR A CG  1 
ATOM   1310 C  CD1 . TYR A 1 274 ? 53.66740 37.79809 42.40411 1.000 18.65916 ? 169 TYR A CD1 1 
ATOM   1311 C  CD2 . TYR A 1 274 ? 55.58220 36.85994 41.31768 1.000 11.22809 ? 169 TYR A CD2 1 
ATOM   1312 C  CE1 . TYR A 1 274 ? 54.41159 38.07526 43.53438 1.000 20.27082 ? 169 TYR A CE1 1 
ATOM   1313 C  CE2 . TYR A 1 274 ? 56.35865 37.11192 42.47629 1.000 11.15064 ? 169 TYR A CE2 1 
ATOM   1314 C  CZ  . TYR A 1 274 ? 55.74342 37.73841 43.57384 1.000 15.48410 ? 169 TYR A CZ  1 
ATOM   1315 O  OH  . TYR A 1 274 ? 56.47258 38.04519 44.72151 1.000 20.62309 ? 169 TYR A OH  1 
ATOM   1316 N  N   . SER A 1 275 ? 50.52184 35.68926 39.19296 1.000 8.02980  ? 170 SER A N   1 
ATOM   1317 C  CA  . SER A 1 275 ? 49.54136 35.49292 38.12686 1.000 6.56743  ? 170 SER A CA  1 
ATOM   1318 C  C   . SER A 1 275 ? 48.90071 36.81585 37.73288 1.000 8.42419  ? 170 SER A C   1 
ATOM   1319 O  O   . SER A 1 275 ? 48.63688 37.66729 38.60251 1.000 10.72654 ? 170 SER A O   1 
ATOM   1320 C  CB  . SER A 1 275 ? 48.41387 34.55833 38.59873 1.000 8.24352  ? 170 SER A CB  1 
ATOM   1321 O  OG  . SER A 1 275 ? 48.90523 33.24515 38.75500 1.000 8.84566  ? 170 SER A OG  1 
ATOM   1322 N  N   . PRO A 1 276 ? 48.53667 36.97821 36.44910 1.000 6.78321  ? 171 PRO A N   1 
ATOM   1323 C  CA  . PRO A 1 276 ? 48.69033 36.00459 35.35432 1.000 6.78478  ? 171 PRO A CA  1 
ATOM   1324 C  C   . PRO A 1 276 ? 50.08068 35.93965 34.72080 1.000 6.45729  ? 171 PRO A C   1 
ATOM   1325 O  O   . PRO A 1 276 ? 50.26324 35.24403 33.70083 1.000 9.17763  ? 171 PRO A O   1 
ATOM   1326 C  CB  . PRO A 1 276 ? 47.64136 36.49318 34.32300 1.000 7.26307  ? 171 PRO A CB  1 
ATOM   1327 C  CG  . PRO A 1 276 ? 47.57159 37.95739 34.54790 1.000 9.94953  ? 171 PRO A CG  1 
ATOM   1328 C  CD  . PRO A 1 276 ? 47.74668 38.15510 36.03938 1.000 8.79230  ? 171 PRO A CD  1 
ATOM   1329 N  N   . ALA A 1 277 ? 51.06856 36.60686 35.33133 1.000 7.14531  ? 172 ALA A N   1 
ATOM   1330 C  CA  . ALA A 1 277 ? 52.44174 36.59289 34.81005 1.000 8.17610  ? 172 ALA A CA  1 
ATOM   1331 C  C   . ALA A 1 277 ? 52.93064 35.18705 34.47727 1.000 8.73258  ? 172 ALA A C   1 
ATOM   1332 O  O   . ALA A 1 277 ? 53.62094 34.99219 33.47790 1.000 8.64506  ? 172 ALA A O   1 
ATOM   1333 C  CB  . ALA A 1 277 ? 53.40476 37.22410 35.82851 1.000 9.97964  ? 172 ALA A CB  1 
ATOM   1334 N  N   . SER A 1 278 ? 52.59633 34.19040 35.30839 1.000 6.58201  ? 173 SER A N   1 
ATOM   1335 C  CA  . SER A 1 278 ? 53.18258 32.85638 35.17343 1.000 6.93921  ? 173 SER A CA  1 
ATOM   1336 C  C   . SER A 1 278 ? 52.47159 31.96935 34.14996 1.000 8.00896  ? 173 SER A C   1 
ATOM   1337 O  O   . SER A 1 278 ? 52.90334 30.82412 33.97085 1.000 10.86308 ? 173 SER A O   1 
ATOM   1338 C  CB  . SER A 1 278 ? 53.20557 32.16116 36.55240 1.000 8.41814  ? 173 SER A CB  1 
ATOM   1339 O  OG  . SER A 1 278 ? 51.89247 32.07200 37.09959 1.000 9.28393  ? 173 SER A OG  1 
ATOM   1340 N  N   . GLU A 1 279 ? 51.41640 32.45199 33.48677 1.000 8.36127  ? 174 GLU A N   1 
ATOM   1341 C  CA  . GLU A 1 279 ? 50.74202 31.64935 32.45276 1.000 8.71467  ? 174 GLU A CA  1 
ATOM   1342 C  C   . GLU A 1 279 ? 51.60852 31.60496 31.18959 1.000 7.54086  ? 174 GLU A C   1 
ATOM   1343 O  O   . GLU A 1 279 ? 51.84239 32.63937 30.57396 1.000 7.30884  ? 174 GLU A O   1 
ATOM   1344 C  CB  . GLU A 1 279 ? 49.36389 32.25744 32.15459 1.000 7.65434  ? 174 GLU A CB  1 
ATOM   1345 C  CG  . GLU A 1 279 ? 48.66770 31.66890 30.88256 1.000 8.13824  ? 174 GLU A CG  1 
ATOM   1346 C  CD  . GLU A 1 279 ? 48.65978 30.13406 30.87266 1.000 9.33863  ? 174 GLU A CD  1 
ATOM   1347 O  OE1 . GLU A 1 279 ? 48.47608 29.47040 31.93814 1.000 11.33225 ? 174 GLU A OE1 1 
ATOM   1348 O  OE2 . GLU A 1 279 ? 48.88041 29.53559 29.76985 1.000 10.10790 ? 174 GLU A OE2 1 
ATOM   1349 N  N   . PRO A 1 280 ? 52.11548 30.43890 30.76497 1.000 9.19668  ? 175 PRO A N   1 
ATOM   1350 C  CA  . PRO A 1 280 ? 53.09501 30.46071 29.66680 1.000 7.89704  ? 175 PRO A CA  1 
ATOM   1351 C  C   . PRO A 1 280 ? 52.51647 30.95619 28.34635 1.000 7.93534  ? 175 PRO A C   1 
ATOM   1352 O  O   . PRO A 1 280 ? 53.26347 31.52097 27.53629 1.000 9.78496  ? 175 PRO A O   1 
ATOM   1353 C  CB  . PRO A 1 280 ? 53.54781 28.99800 29.53599 1.000 12.50535 ? 175 PRO A CB  1 
ATOM   1354 C  CG  . PRO A 1 280 ? 52.88346 28.25417 30.59373 1.000 24.23366 ? 175 PRO A CG  1 
ATOM   1355 C  CD  . PRO A 1 280 ? 52.10963 29.15585 31.49697 1.000 12.14111 ? 175 PRO A CD  1 
ATOM   1356 N  N   . SER A 1 281 ? 51.22040 30.75637 28.09632 1.000 6.47652  ? 176 SER A N   1 
ATOM   1357 C  CA  . SER A 1 281 ? 50.71536 31.01252 26.75290 1.000 6.35654  ? 176 SER A CA  1 
ATOM   1358 C  C   . SER A 1 281 ? 50.45662 32.47370 26.43002 1.000 10.40334 ? 176 SER A C   1 
ATOM   1359 O  O   . SER A 1 281 ? 50.12589 32.76185 25.26847 1.000 11.25664 ? 176 SER A O   1 
ATOM   1360 C  CB  . SER A 1 281 ? 49.43894 30.19214 26.51241 1.000 11.88769 ? 176 SER A CB  1 
ATOM   1361 O  OG  . SER A 1 281 ? 48.34943 30.65772 27.29341 1.000 12.34454 ? 176 SER A OG  1 
ATOM   1362 N  N   . VAL A 1 282 ? 50.57466 33.39112 27.39157 1.000 7.38119  ? 177 VAL A N   1 
ATOM   1363 C  CA  . VAL A 1 282 ? 50.38964 34.80636 27.11598 1.000 7.51117  ? 177 VAL A CA  1 
ATOM   1364 C  C   . VAL A 1 282 ? 51.77129 35.44507 26.99757 1.000 7.77534  ? 177 VAL A C   1 
ATOM   1365 O  O   . VAL A 1 282 ? 52.79409 34.74364 26.97554 1.000 9.79020  ? 177 VAL A O   1 
ATOM   1366 C  CB  . VAL A 1 282 ? 49.52834 35.48445 28.20636 1.000 6.54140  ? 177 VAL A CB  1 
ATOM   1367 C  CG1 . VAL A 1 282 ? 48.14436 34.78655 28.27601 1.000 11.38303 ? 177 VAL A CG1 1 
ATOM   1368 C  CG2 . VAL A 1 282 ? 50.19132 35.42633 29.57383 1.000 8.37068  ? 177 VAL A CG2 1 
ATOM   1369 N  N   . CYS A 1 283 ? 51.81696 36.77531 26.83335 1.000 5.59112  ? 178 CYS A N   1 
ATOM   1370 C  CA  . CYS A 1 283 ? 53.08476 37.46997 26.61118 1.000 5.38164  ? 178 CYS A CA  1 
ATOM   1371 C  C   . CYS A 1 283 ? 53.43253 38.21363 27.89604 1.000 8.18243  ? 178 CYS A C   1 
ATOM   1372 O  O   . CYS A 1 283 ? 52.79480 39.21854 28.21880 1.000 7.44984  ? 178 CYS A O   1 
ATOM   1373 C  CB  . CYS A 1 283 ? 52.92820 38.45233 25.43843 1.000 5.55152  ? 178 CYS A CB  1 
ATOM   1374 S  SG  . CYS A 1 283 ? 54.50503 38.78983 24.58564 1.000 6.91077  ? 178 CYS A SG  1 
ATOM   1375 N  N   A THR A 1 284 ? 54.45752 37.73971 28.61452 0.916 6.22644  ? 179 THR A N   1 
ATOM   1376 N  N   B THR A 1 284 ? 54.43492 37.74381 28.61591 0.084 6.22588  ? 179 THR A N   1 
ATOM   1377 C  CA  A THR A 1 284 ? 54.77422 38.28934 29.93750 0.916 5.10994  ? 179 THR A CA  1 
ATOM   1378 C  CA  B THR A 1 284 ? 54.76368 38.33221 29.90307 0.084 5.09894  ? 179 THR A CA  1 
ATOM   1379 C  C   A THR A 1 284 ? 55.92321 39.28078 29.79854 0.916 5.68251  ? 179 THR A C   1 
ATOM   1380 C  C   B THR A 1 284 ? 55.90558 39.31681 29.74177 0.084 5.72006  ? 179 THR A C   1 
ATOM   1381 O  O   A THR A 1 284 ? 56.97215 38.93002 29.24784 0.916 6.44609  ? 179 THR A O   1 
ATOM   1382 O  O   B THR A 1 284 ? 56.93049 38.99888 29.12928 0.084 6.38214  ? 179 THR A O   1 
ATOM   1383 C  CB  A THR A 1 284 ? 55.15141 37.15443 30.89201 0.916 5.44872  ? 179 THR A CB  1 
ATOM   1384 C  CB  B THR A 1 284 ? 55.10822 37.24504 30.90206 0.084 5.47298  ? 179 THR A CB  1 
ATOM   1385 O  OG1 A THR A 1 284 ? 54.04493 36.24322 30.99336 0.916 6.94580  ? 179 THR A OG1 1 
ATOM   1386 O  OG1 B THR A 1 284 ? 56.19449 36.46973 30.39123 0.084 5.73525  ? 179 THR A OG1 1 
ATOM   1387 C  CG2 A THR A 1 284 ? 55.52555 37.69780 32.30826 0.916 6.44875  ? 179 THR A CG2 1 
ATOM   1388 C  CG2 B THR A 1 284 ? 53.91174 36.37895 31.03513 0.084 6.74124  ? 179 THR A CG2 1 
ATOM   1389 N  N   . VAL A 1 285 ? 55.71730 40.51087 30.28972 1.000 4.94136  ? 180 VAL A N   1 
ATOM   1390 C  CA  . VAL A 1 285 ? 56.55110 41.67629 29.95866 1.000 5.67963  ? 180 VAL A CA  1 
ATOM   1391 C  C   . VAL A 1 285 ? 57.29417 42.17545 31.17963 1.000 5.20837  ? 180 VAL A C   1 
ATOM   1392 O  O   . VAL A 1 285 ? 56.66710 42.59024 32.16649 1.000 6.94802  ? 180 VAL A O   1 
ATOM   1393 C  CB  . VAL A 1 285 ? 55.67340 42.79603 29.38143 1.000 5.51101  ? 180 VAL A CB  1 
ATOM   1394 C  CG1 . VAL A 1 285 ? 56.57328 43.99760 28.93842 1.000 7.31721  ? 180 VAL A CG1 1 
ATOM   1395 C  CG2 . VAL A 1 285 ? 54.87647 42.23360 28.19274 1.000 5.88719  ? 180 VAL A CG2 1 
ATOM   1396 N  N   . GLY A 1 286 ? 58.64690 42.18306 31.11004 1.000 5.38056  ? 181 GLY A N   1 
ATOM   1397 C  CA  . GLY A 1 286 ? 59.45775 42.83969 32.13909 1.000 7.15160  ? 181 GLY A CA  1 
ATOM   1398 C  C   . GLY A 1 286 ? 59.75850 44.29937 31.77186 1.000 6.03528  ? 181 GLY A C   1 
ATOM   1399 O  O   . GLY A 1 286 ? 59.44449 44.76928 30.68321 1.000 6.46189  ? 181 GLY A O   1 
ATOM   1400 N  N   . ALA A 1 287 ? 60.39170 45.01264 32.69885 1.000 5.74879  ? 182 ALA A N   1 
ATOM   1401 C  CA  . ALA A 1 287 ? 60.66630 46.44121 32.52258 1.000 6.72212  ? 182 ALA A CA  1 
ATOM   1402 C  C   . ALA A 1 287 ? 62.15912 46.74010 32.44230 1.000 7.31078  ? 182 ALA A C   1 
ATOM   1403 O  O   . ALA A 1 287 ? 62.95940 46.16199 33.18985 1.000 7.14184  ? 182 ALA A O   1 
ATOM   1404 C  CB  . ALA A 1 287 ? 60.08005 47.25599 33.69568 1.000 5.76485  ? 182 ALA A CB  1 
ATOM   1405 N  N   . SER A 1 288 ? 62.50504 47.72698 31.58878 1.000 6.14443  ? 183 SER A N   1 
ATOM   1406 C  CA  . SER A 1 288 ? 63.87189 48.25500 31.52082 1.000 6.56734  ? 183 SER A CA  1 
ATOM   1407 C  C   . SER A 1 288 ? 63.87838 49.76314 31.73792 1.000 6.62395  ? 183 SER A C   1 
ATOM   1408 O  O   . SER A 1 288 ? 62.84288 50.43180 31.67750 1.000 7.96538  ? 183 SER A O   1 
ATOM   1409 C  CB  . SER A 1 288 ? 64.48920 47.93488 30.14567 1.000 7.35825  ? 183 SER A CB  1 
ATOM   1410 O  OG  . SER A 1 288 ? 63.71507 48.61282 29.15802 1.000 10.51390 ? 183 SER A OG  1 
ATOM   1411 N  N   . ASP A 1 289 ? 65.07105 50.33122 31.96565 1.000 7.07108  ? 184 ASP A N   1 
ATOM   1412 C  CA  . ASP A 1 289 ? 65.18388 51.77153 32.14836 1.000 7.21773  ? 184 ASP A CA  1 
ATOM   1413 C  C   . ASP A 1 289 ? 65.92936 52.41185 30.96830 1.000 8.90682  ? 184 ASP A C   1 
ATOM   1414 O  O   . ASP A 1 289 ? 66.33180 51.73506 30.02555 1.000 7.72641  ? 184 ASP A O   1 
ATOM   1415 C  CB  . ASP A 1 289 ? 65.82321 52.11287 33.52177 1.000 7.63951  ? 184 ASP A CB  1 
ATOM   1416 C  CG  . ASP A 1 289 ? 67.35171 51.82168 33.60791 1.000 11.93806 ? 184 ASP A CG  1 
ATOM   1417 O  OD1 . ASP A 1 289 ? 68.02898 51.62259 32.56496 1.000 9.47571  ? 184 ASP A OD1 1 
ATOM   1418 O  OD2 . ASP A 1 289 ? 67.84417 51.77144 34.76057 1.000 11.70930 ? 184 ASP A OD2 1 
ATOM   1419 N  N   . ARG A 1 290 ? 66.09342 53.75060 31.02123 1.000 8.20138  ? 185 ARG A N   1 
ATOM   1420 C  CA  . ARG A 1 290 ? 66.59048 54.42204 29.80930 1.000 8.61642  ? 185 ARG A CA  1 
ATOM   1421 C  C   . ARG A 1 290 ? 68.08066 54.19630 29.54927 1.000 9.93196  ? 185 ARG A C   1 
ATOM   1422 O  O   . ARG A 1 290 ? 68.57307 54.59485 28.48600 1.000 13.13092 ? 185 ARG A O   1 
ATOM   1423 C  CB  . ARG A 1 290 ? 66.32420 55.93049 29.87648 1.000 13.43691 ? 185 ARG A CB  1 
ATOM   1424 C  CG  . ARG A 1 290 ? 67.11954 56.58098 30.95883 1.000 16.44481 ? 185 ARG A CG  1 
ATOM   1425 C  CD  . ARG A 1 290 ? 67.07633 58.12867 30.85557 1.000 25.20243 ? 185 ARG A CD  1 
ATOM   1426 N  NE  . ARG A 1 290 ? 65.79247 58.66407 31.27738 1.000 31.27090 ? 185 ARG A NE  1 
ATOM   1427 C  CZ  . ARG A 1 290 ? 65.07656 59.52914 30.56779 1.000 48.73946 ? 185 ARG A CZ  1 
ATOM   1428 N  NH1 . ARG A 1 290 ? 65.47693 59.94461 29.37479 1.000 37.25957 ? 185 ARG A NH1 1 
ATOM   1429 N  NH2 . ARG A 1 290 ? 63.93872 60.00214 31.07473 1.000 41.53407 ? 185 ARG A NH2 1 
ATOM   1430 N  N   . TYR A 1 291 ? 68.79448 53.53646 30.44794 1.000 8.74925  ? 186 TYR A N   1 
ATOM   1431 C  CA  . TYR A 1 291 ? 70.18647 53.14262 30.25819 1.000 11.16134 ? 186 TYR A CA  1 
ATOM   1432 C  C   . TYR A 1 291 ? 70.32834 51.66993 29.89746 1.000 11.18828 ? 186 TYR A C   1 
ATOM   1433 O  O   . TYR A 1 291 ? 71.44136 51.11556 29.97349 1.000 11.33396 ? 186 TYR A O   1 
ATOM   1434 C  CB  . TYR A 1 291 ? 70.99062 53.48284 31.51209 1.000 9.68421  ? 186 TYR A CB  1 
ATOM   1435 C  CG  . TYR A 1 291 ? 70.98373 54.97476 31.85665 1.000 15.08343 ? 186 TYR A CG  1 
ATOM   1436 C  CD1 . TYR A 1 291 ? 71.63462 55.88957 31.03948 1.000 25.88180 ? 186 TYR A CD1 1 
ATOM   1437 C  CD2 . TYR A 1 291 ? 70.15301 55.45952 32.85369 1.000 17.89348 ? 186 TYR A CD2 1 
ATOM   1438 C  CE1 . TYR A 1 291 ? 71.60929 57.26301 31.34473 1.000 25.07036 ? 186 TYR A CE1 1 
ATOM   1439 C  CE2 . TYR A 1 291 ? 70.10304 56.81286 33.14808 1.000 25.97132 ? 186 TYR A CE2 1 
ATOM   1440 C  CZ  . TYR A 1 291 ? 70.82257 57.70024 32.39443 1.000 31.53672 ? 186 TYR A CZ  1 
ATOM   1441 O  OH  . TYR A 1 291 ? 70.74350 59.04141 32.70403 1.000 41.10198 ? 186 TYR A OH  1 
ATOM   1442 N  N   . ASP A 1 292 ? 69.22417 51.02614 29.49643 1.000 8.59517  ? 187 ASP A N   1 
ATOM   1443 C  CA  . ASP A 1 292 ? 69.17840 49.61359 29.11850 1.000 9.09674  ? 187 ASP A CA  1 
ATOM   1444 C  C   . ASP A 1 292 ? 69.56295 48.69044 30.26950 1.000 9.59569  ? 187 ASP A C   1 
ATOM   1445 O  O   . ASP A 1 292 ? 70.14904 47.62449 30.04362 1.000 13.83194 ? 187 ASP A O   1 
ATOM   1446 C  CB  . ASP A 1 292 ? 70.06204 49.33389 27.89151 1.000 9.85911  ? 187 ASP A CB  1 
ATOM   1447 C  CG  . ASP A 1 292 ? 69.39085 49.74772 26.58486 1.000 17.55148 ? 187 ASP A CG  1 
ATOM   1448 O  OD1 . ASP A 1 292 ? 68.20889 50.14442 26.62673 1.000 12.11855 ? 187 ASP A OD1 1 
ATOM   1449 O  OD2 . ASP A 1 292 ? 70.05010 49.67694 25.51239 1.000 15.16150 ? 187 ASP A OD2 1 
ATOM   1450 N  N   . ARG A 1 293 ? 69.24838 49.08256 31.50455 1.000 10.48793 ? 188 ARG A N   1 
ATOM   1451 C  CA  . ARG A 1 293 ? 69.30222 48.14959 32.62749 1.000 8.79476  ? 188 ARG A CA  1 
ATOM   1452 C  C   . ARG A 1 293 ? 67.92117 47.56412 32.89301 1.000 8.23627  ? 188 ARG A C   1 
ATOM   1453 O  O   . ARG A 1 293 ? 66.90608 48.22651 32.68843 1.000 10.19351 ? 188 ARG A O   1 
ATOM   1454 C  CB  . ARG A 1 293 ? 69.79479 48.84889 33.89037 1.000 9.18856  ? 188 ARG A CB  1 
ATOM   1455 C  CG  . ARG A 1 293 ? 71.10133 49.55434 33.67195 1.000 10.92774 ? 188 ARG A CG  1 
ATOM   1456 C  CD  . ARG A 1 293 ? 71.53484 50.27213 34.93064 1.000 13.44066 ? 188 ARG A CD  1 
ATOM   1457 N  NE  . ARG A 1 293 ? 70.67062 51.41682 35.15251 1.000 16.85312 ? 188 ARG A NE  1 
ATOM   1458 C  CZ  . ARG A 1 293 ? 71.08297 52.59967 35.58146 1.000 10.22782 ? 188 ARG A CZ  1 
ATOM   1459 N  NH1 . ARG A 1 293 ? 72.36432 52.85241 35.80747 1.000 13.96603 ? 188 ARG A NH1 1 
ATOM   1460 N  NH2 . ARG A 1 293 ? 70.19361 53.55725 35.76491 1.000 13.09064 ? 188 ARG A NH2 1 
ATOM   1461 N  N   . ARG A 1 294 ? 67.88104 46.29646 33.32156 1.000 8.31938  ? 189 ARG A N   1 
ATOM   1462 C  CA  . ARG A 1 294 ? 66.63853 45.80706 33.91319 1.000 8.86961  ? 189 ARG A CA  1 
ATOM   1463 C  C   . ARG A 1 294 ? 66.22263 46.77336 35.01920 1.000 7.90781  ? 189 ARG A C   1 
ATOM   1464 O  O   . ARG A 1 294 ? 67.04848 47.16511 35.85663 1.000 9.78124  ? 189 ARG A O   1 
ATOM   1465 C  CB  . ARG A 1 294 ? 66.82746 44.38789 34.48838 1.000 9.30784  ? 189 ARG A CB  1 
ATOM   1466 C  CG  . ARG A 1 294 ? 65.57113 43.87059 35.17128 1.000 10.88376 ? 189 ARG A CG  1 
ATOM   1467 C  CD  . ARG A 1 294 ? 65.72056 42.42116 35.65121 1.000 11.11426 ? 189 ARG A CD  1 
ATOM   1468 N  NE  . ARG A 1 294 ? 66.73858 42.27537 36.67295 1.000 12.66451 ? 189 ARG A NE  1 
ATOM   1469 C  CZ  . ARG A 1 294 ? 66.53412 42.34720 37.98524 1.000 18.39135 ? 189 ARG A CZ  1 
ATOM   1470 N  NH1 . ARG A 1 294 ? 65.31662 42.49798 38.49735 1.000 14.31672 ? 189 ARG A NH1 1 
ATOM   1471 N  NH2 . ARG A 1 294 ? 67.57316 42.23290 38.81115 1.000 22.20825 ? 189 ARG A NH2 1 
ATOM   1472 N  N   . SER A 1 295 ? 64.95724 47.17357 35.01390 1.000 7.42787  ? 190 SER A N   1 
ATOM   1473 C  CA  . SER A 1 295 ? 64.46500 48.03656 36.08768 1.000 7.45918  ? 190 SER A CA  1 
ATOM   1474 C  C   . SER A 1 295 ? 64.64211 47.34957 37.43397 1.000 7.83874  ? 190 SER A C   1 
ATOM   1475 O  O   . SER A 1 295 ? 64.45643 46.13445 37.56484 1.000 9.82799  ? 190 SER A O   1 
ATOM   1476 C  CB  . SER A 1 295 ? 62.97799 48.38114 35.88677 1.000 8.01794  ? 190 SER A CB  1 
ATOM   1477 O  OG  . SER A 1 295 ? 62.74113 49.09474 34.67282 1.000 8.10875  ? 190 SER A OG  1 
ATOM   1478 N  N   . SER A 1 296 ? 65.01001 48.13356 38.45665 1.000 8.34335  ? 191 SER A N   1 
ATOM   1479 C  CA  . SER A 1 296 ? 65.43509 47.46785 39.68485 1.000 8.74677  ? 191 SER A CA  1 
ATOM   1480 C  C   . SER A 1 296 ? 64.33135 46.68991 40.36845 1.000 12.07475 ? 191 SER A C   1 
ATOM   1481 O  O   . SER A 1 296 ? 64.64993 45.78695 41.14478 1.000 14.03998 ? 191 SER A O   1 
ATOM   1482 C  CB  . SER A 1 296 ? 66.00173 48.49173 40.65792 1.000 12.39182 ? 191 SER A CB  1 
ATOM   1483 O  OG  . SER A 1 296 ? 64.99670 49.43795 40.94722 1.000 21.58254 ? 191 SER A OG  1 
ATOM   1484 N  N   . PHE A 1 297 ? 63.06839 47.03371 40.10437 1.000 8.26506  ? 192 PHE A N   1 
ATOM   1485 C  CA  . PHE A 1 297 ? 61.91962 46.33675 40.65995 1.000 7.94202  ? 192 PHE A CA  1 
ATOM   1486 C  C   . PHE A 1 297 ? 61.43002 45.20125 39.78344 1.000 9.81630  ? 192 PHE A C   1 
ATOM   1487 O  O   . PHE A 1 297 ? 60.51271 44.47930 40.19633 1.000 10.33809 ? 192 PHE A O   1 
ATOM   1488 C  CB  . PHE A 1 297 ? 60.74643 47.31760 40.84190 1.000 9.91731  ? 192 PHE A CB  1 
ATOM   1489 C  CG  . PHE A 1 297 ? 60.47435 48.15405 39.61084 1.000 8.08169  ? 192 PHE A CG  1 
ATOM   1490 C  CD1 . PHE A 1 297 ? 59.74462 47.63369 38.53332 1.000 10.32862 ? 192 PHE A CD1 1 
ATOM   1491 C  CD2 . PHE A 1 297 ? 61.03678 49.42081 39.47438 1.000 8.75378  ? 192 PHE A CD2 1 
ATOM   1492 C  CE1 . PHE A 1 297 ? 59.50966 48.35954 37.39442 1.000 9.34928  ? 192 PHE A CE1 1 
ATOM   1493 C  CE2 . PHE A 1 297 ? 60.79276 50.17916 38.32329 1.000 8.25421  ? 192 PHE A CE2 1 
ATOM   1494 C  CZ  . PHE A 1 297 ? 60.05061 49.64908 37.28201 1.000 11.00402 ? 192 PHE A CZ  1 
ATOM   1495 N  N   . SER A 1 298 ? 61.94018 45.05650 38.55503 1.000 7.36134  ? 193 SER A N   1 
ATOM   1496 C  CA  . SER A 1 298 ? 61.26305 44.15797 37.62139 1.000 6.97792  ? 193 SER A CA  1 
ATOM   1497 C  C   . SER A 1 298 ? 61.43177 42.69722 38.02847 1.000 7.26779  ? 193 SER A C   1 
ATOM   1498 O  O   . SER A 1 298 ? 62.54123 42.24835 38.34192 1.000 10.18722 ? 193 SER A O   1 
ATOM   1499 C  CB  . SER A 1 298 ? 61.80570 44.34952 36.19679 1.000 9.53521  ? 193 SER A CB  1 
ATOM   1500 O  OG  . SER A 1 298 ? 61.12338 43.45895 35.29532 1.000 8.73132  ? 193 SER A OG  1 
ATOM   1501 N  N   . ASN A 1 299 ? 60.33138 41.93459 37.97680 1.000 7.03619  ? 194 ASN A N   1 
ATOM   1502 C  CA  . ASN A 1 299 ? 60.47888 40.48342 38.08094 1.000 7.30186  ? 194 ASN A CA  1 
ATOM   1503 C  C   . ASN A 1 299 ? 61.22970 39.93552 36.86956 1.000 10.31820 ? 194 ASN A C   1 
ATOM   1504 O  O   . ASN A 1 299 ? 61.40820 40.61148 35.84392 1.000 10.15315 ? 194 ASN A O   1 
ATOM   1505 C  CB  . ASN A 1 299 ? 59.09926 39.80166 38.19380 1.000 7.82813  ? 194 ASN A CB  1 
ATOM   1506 C  CG  . ASN A 1 299 ? 58.50451 39.92378 39.59303 1.000 9.31856  ? 194 ASN A CG  1 
ATOM   1507 O  OD1 . ASN A 1 299 ? 59.15888 40.37400 40.55202 1.000 9.11285  ? 194 ASN A OD1 1 
ATOM   1508 N  ND2 . ASN A 1 299 ? 57.23675 39.56225 39.71722 1.000 8.28977  ? 194 ASN A ND2 1 
ATOM   1509 N  N   . TYR A 1 300 ? 61.69750 38.69126 37.00505 1.000 9.56981  ? 195 TYR A N   1 
ATOM   1510 C  CA  . TYR A 1 300 ? 62.49875 38.05669 35.96140 1.000 8.95021  ? 195 TYR A CA  1 
ATOM   1511 C  C   . TYR A 1 300 ? 62.13537 36.57211 35.92794 1.000 9.86095  ? 195 TYR A C   1 
ATOM   1512 O  O   . TYR A 1 300 ? 61.16057 36.14585 36.55238 1.000 11.81903 ? 195 TYR A O   1 
ATOM   1513 C  CB  . TYR A 1 300 ? 64.00180 38.26900 36.23574 1.000 10.47534 ? 195 TYR A CB  1 
ATOM   1514 C  CG  . TYR A 1 300 ? 64.39229 37.89340 37.63970 1.000 12.88939 ? 195 TYR A CG  1 
ATOM   1515 C  CD1 . TYR A 1 300 ? 64.70191 36.58588 37.97419 1.000 11.29382 ? 195 TYR A CD1 1 
ATOM   1516 C  CD2 . TYR A 1 300 ? 64.43837 38.86424 38.64204 1.000 14.66217 ? 195 TYR A CD2 1 
ATOM   1517 C  CE1 . TYR A 1 300 ? 65.06471 36.25647 39.28833 1.000 20.79563 ? 195 TYR A CE1 1 
ATOM   1518 C  CE2 . TYR A 1 300 ? 64.78866 38.54459 39.92482 1.000 15.98721 ? 195 TYR A CE2 1 
ATOM   1519 C  CZ  . TYR A 1 300 ? 65.09895 37.24858 40.24729 1.000 21.19148 ? 195 TYR A CZ  1 
ATOM   1520 O  OH  . TYR A 1 300 ? 65.45756 36.97943 41.54930 1.000 28.34172 ? 195 TYR A OH  1 
ATOM   1521 N  N   . GLY A 1 301 ? 62.90905 35.77241 35.21058 1.000 9.40702  ? 196 GLY A N   1 
ATOM   1522 C  CA  . GLY A 1 301 ? 62.69035 34.33727 35.20502 1.000 10.41267 ? 196 GLY A CA  1 
ATOM   1523 C  C   . GLY A 1 301 ? 62.37045 33.80762 33.81978 1.000 10.23720 ? 196 GLY A C   1 
ATOM   1524 O  O   . GLY A 1 301 ? 62.17409 34.55256 32.85957 1.000 11.96469 ? 196 GLY A O   1 
ATOM   1525 N  N   . SER A 1 302 ? 62.32894 32.47136 33.74635 1.000 11.58744 ? 197 SER A N   1 
ATOM   1526 C  CA  . SER A 1 302 ? 62.14725 31.81234 32.44488 1.000 11.56398 ? 197 SER A CA  1 
ATOM   1527 C  C   . SER A 1 302 ? 60.79864 32.09497 31.78878 1.000 9.77381  ? 197 SER A C   1 
ATOM   1528 O  O   . SER A 1 302 ? 60.68341 31.93910 30.56239 1.000 13.08662 ? 197 SER A O   1 
ATOM   1529 C  CB  . SER A 1 302 ? 62.33749 30.30573 32.60581 1.000 16.18407 ? 197 SER A CB  1 
ATOM   1530 O  OG  . SER A 1 302 ? 61.38016 29.80296 33.49097 1.000 21.36770 ? 197 SER A OG  1 
ATOM   1531 N  N   . VAL A 1 303 ? 59.77823 32.50766 32.55090 1.000 9.23685  ? 198 VAL A N   1 
ATOM   1532 C  CA  . VAL A 1 303 ? 58.46707 32.76477 31.94374 1.000 7.33781  ? 198 VAL A CA  1 
ATOM   1533 C  C   . VAL A 1 303 ? 58.37426 34.13035 31.27253 1.000 7.90434  ? 198 VAL A C   1 
ATOM   1534 O  O   . VAL A 1 303 ? 57.41617 34.36230 30.49125 1.000 12.30523 ? 198 VAL A O   1 
ATOM   1535 C  CB  . VAL A 1 303 ? 57.36145 32.58964 33.00093 1.000 11.37633 ? 198 VAL A CB  1 
ATOM   1536 C  CG1 . VAL A 1 303 ? 57.29859 33.77938 33.96211 1.000 14.14099 ? 198 VAL A CG1 1 
ATOM   1537 C  CG2 . VAL A 1 303 ? 55.99750 32.34036 32.31385 1.000 16.31260 ? 198 VAL A CG2 1 
ATOM   1538 N  N   . LEU A 1 304 ? 59.35262 35.02361 31.47128 1.000 7.14279  ? 199 LEU A N   1 
ATOM   1539 C  CA  . LEU A 1 304 ? 59.28594 36.28813 30.75240 1.000 6.49162  ? 199 LEU A CA  1 
ATOM   1540 C  C   . LEU A 1 304 ? 59.50636 36.04107 29.26794 1.000 7.18445  ? 199 LEU A C   1 
ATOM   1541 O  O   . LEU A 1 304 ? 60.34657 35.20969 28.87631 1.000 10.21631 ? 199 LEU A O   1 
ATOM   1542 C  CB  . LEU A 1 304 ? 60.35703 37.25279 31.23359 1.000 7.66368  ? 199 LEU A CB  1 
ATOM   1543 C  CG  . LEU A 1 304 ? 59.88117 38.21575 32.32323 1.000 11.47927 ? 199 LEU A CG  1 
ATOM   1544 C  CD1 . LEU A 1 304 ? 59.63770 37.44874 33.61425 1.000 12.95119 ? 199 LEU A CD1 1 
ATOM   1545 C  CD2 . LEU A 1 304 ? 60.92127 39.32432 32.53954 1.000 14.75180 ? 199 LEU A CD2 1 
ATOM   1546 N  N   . ASP A 1 305 ? 58.77377 36.79439 28.43718 1.000 6.13447  ? 200 ASP A N   1 
ATOM   1547 C  CA  . ASP A 1 305 ? 58.93369 36.69133 26.99080 1.000 6.19629  ? 200 ASP A CA  1 
ATOM   1548 C  C   . ASP A 1 305 ? 59.73422 37.84030 26.40439 1.000 6.18075  ? 200 ASP A C   1 
ATOM   1549 O  O   . ASP A 1 305 ? 60.36137 37.65884 25.34600 1.000 8.78556  ? 200 ASP A O   1 
ATOM   1550 C  CB  . ASP A 1 305 ? 57.55336 36.68529 26.30122 1.000 5.89584  ? 200 ASP A CB  1 
ATOM   1551 C  CG  . ASP A 1 305 ? 56.74402 35.47033 26.64759 1.000 8.53806  ? 200 ASP A CG  1 
ATOM   1552 O  OD1 . ASP A 1 305 ? 57.04593 34.41222 26.07345 1.000 10.56431 ? 200 ASP A OD1 1 
ATOM   1553 O  OD2 . ASP A 1 305 ? 55.82584 35.52284 27.48985 1.000 7.89150  ? 200 ASP A OD2 1 
ATOM   1554 N  N   . ILE A 1 306 ? 59.68193 39.02347 27.02815 1.000 6.41693  ? 201 ILE A N   1 
ATOM   1555 C  CA  . ILE A 1 306 ? 60.13952 40.26618 26.39024 1.000 6.47617  ? 201 ILE A CA  1 
ATOM   1556 C  C   . ILE A 1 306 ? 60.26351 41.34731 27.44728 1.000 8.10619  ? 201 ILE A C   1 
ATOM   1557 O  O   . ILE A 1 306 ? 59.56784 41.29555 28.46604 1.000 7.35181  ? 201 ILE A O   1 
ATOM   1558 C  CB  . ILE A 1 306 ? 59.14307 40.65957 25.26703 1.000 7.35460  ? 201 ILE A CB  1 
ATOM   1559 C  CG1 . ILE A 1 306 ? 59.65782 41.80539 24.38835 1.000 7.62085  ? 201 ILE A CG1 1 
ATOM   1560 C  CG2 . ILE A 1 306 ? 57.77850 41.05673 25.83997 1.000 7.36767  ? 201 ILE A CG2 1 
ATOM   1561 C  CD1 . ILE A 1 306 ? 60.80301 41.32857 23.50736 1.000 9.27291  ? 201 ILE A CD1 1 
ATOM   1562 N  N   . PHE A 1 307 ? 61.14082 42.32150 27.22219 1.000 5.86981  ? 202 PHE A N   1 
ATOM   1563 C  CA  . PHE A 1 307 ? 61.21346 43.52178 28.05368 1.000 5.77190  ? 202 PHE A CA  1 
ATOM   1564 C  C   . PHE A 1 307 ? 60.75291 44.72690 27.25810 1.000 7.89707  ? 202 PHE A C   1 
ATOM   1565 O  O   . PHE A 1 307 ? 60.87928 44.76453 26.03247 1.000 7.97312  ? 202 PHE A O   1 
ATOM   1566 C  CB  . PHE A 1 307 ? 62.65749 43.76082 28.52740 1.000 6.98947  ? 202 PHE A CB  1 
ATOM   1567 C  CG  . PHE A 1 307 ? 63.07328 42.87515 29.67646 1.000 7.38721  ? 202 PHE A CG  1 
ATOM   1568 C  CD1 . PHE A 1 307 ? 63.51338 41.55636 29.45979 1.000 9.08588  ? 202 PHE A CD1 1 
ATOM   1569 C  CD2 . PHE A 1 307 ? 63.01213 43.36029 30.98073 1.000 7.67728  ? 202 PHE A CD2 1 
ATOM   1570 C  CE1 . PHE A 1 307 ? 63.88022 40.74770 30.53921 1.000 11.96350 ? 202 PHE A CE1 1 
ATOM   1571 C  CE2 . PHE A 1 307 ? 63.35551 42.58099 32.05951 1.000 8.55759  ? 202 PHE A CE2 1 
ATOM   1572 C  CZ  . PHE A 1 307 ? 63.82071 41.26829 31.84268 1.000 12.39430 ? 202 PHE A CZ  1 
ATOM   1573 N  N   . GLY A 1 308 ? 60.17777 45.70501 27.95459 1.000 6.20821  ? 203 GLY A N   1 
ATOM   1574 C  CA  . GLY A 1 308 ? 59.88214 46.98991 27.35049 1.000 6.93286  ? 203 GLY A CA  1 
ATOM   1575 C  C   . GLY A 1 308 ? 60.19461 48.09660 28.33605 1.000 6.24440  ? 203 GLY A C   1 
ATOM   1576 O  O   . GLY A 1 308 ? 60.40147 47.84449 29.53188 1.000 6.18289  ? 203 GLY A O   1 
ATOM   1577 N  N   . PRO A 1 309 ? 60.17082 49.34544 27.89452 1.000 6.81911  ? 204 PRO A N   1 
ATOM   1578 C  CA  . PRO A 1 309 ? 60.48278 50.46803 28.79401 1.000 5.53093  ? 204 PRO A CA  1 
ATOM   1579 C  C   . PRO A 1 309 ? 59.49912 50.58469 29.95524 1.000 5.34610  ? 204 PRO A C   1 
ATOM   1580 O  O   . PRO A 1 309 ? 58.27277 50.61570 29.74873 1.000 6.66815  ? 204 PRO A O   1 
ATOM   1581 C  CB  . PRO A 1 309 ? 60.37477 51.69326 27.87446 1.000 7.12389  ? 204 PRO A CB  1 
ATOM   1582 C  CG  . PRO A 1 309 ? 60.63324 51.11613 26.49668 1.000 7.19786  ? 204 PRO A CG  1 
ATOM   1583 C  CD  . PRO A 1 309 ? 60.01557 49.77349 26.48714 1.000 10.98687 ? 204 PRO A CD  1 
ATOM   1584 N  N   . GLY A 1 310 ? 60.04518 50.66070 31.17803 1.000 5.55370  ? 205 GLY A N   1 
ATOM   1585 C  CA  . GLY A 1 310 ? 59.15133 50.69275 32.35423 1.000 5.46729  ? 205 GLY A CA  1 
ATOM   1586 C  C   . GLY A 1 310 ? 59.51288 51.66842 33.45321 1.000 7.56388  ? 205 GLY A C   1 
ATOM   1587 O  O   . GLY A 1 310 ? 58.71844 51.85787 34.37808 1.000 10.21893 ? 205 GLY A O   1 
ATOM   1588 N  N   . THR A 1 311 ? 60.66785 52.32042 33.39665 1.000 6.08239  ? 206 THR A N   1 
ATOM   1589 C  CA  . THR A 1 311 ? 61.06598 53.26842 34.43650 1.000 6.43998  ? 206 THR A CA  1 
ATOM   1590 C  C   . THR A 1 311 ? 60.91437 54.70184 33.91699 1.000 7.23268  ? 206 THR A C   1 
ATOM   1591 O  O   . THR A 1 311 ? 61.42678 55.02306 32.84570 1.000 9.19390  ? 206 THR A O   1 
ATOM   1592 C  CB  . THR A 1 311 ? 62.52162 53.01326 34.87680 1.000 6.87508  ? 206 THR A CB  1 
ATOM   1593 O  OG1 . THR A 1 311 ? 62.62389 51.67853 35.42003 1.000 9.86539  ? 206 THR A OG1 1 
ATOM   1594 C  CG2 . THR A 1 311 ? 62.97057 54.05244 35.89085 1.000 7.31752  ? 206 THR A CG2 1 
ATOM   1595 N  N   A ASP A 1 312 ? 60.18758 55.54357 34.66973 0.590 6.66939  ? 207 ASP A N   1 
ATOM   1596 N  N   B ASP A 1 312 ? 60.20089 55.54723 34.67012 0.410 6.69992  ? 207 ASP A N   1 
ATOM   1597 C  CA  A ASP A 1 312 ? 60.03668 56.97560 34.38178 0.590 7.16421  ? 207 ASP A CA  1 
ATOM   1598 C  CA  B ASP A 1 312 ? 60.07305 56.96784 34.34413 0.410 7.19093  ? 207 ASP A CA  1 
ATOM   1599 C  C   A ASP A 1 312 ? 59.35629 57.20289 33.02601 0.590 6.48627  ? 207 ASP A C   1 
ATOM   1600 C  C   B ASP A 1 312 ? 59.38046 57.15274 32.98836 0.410 6.47625  ? 207 ASP A C   1 
ATOM   1601 O  O   A ASP A 1 312 ? 59.90529 57.83961 32.11522 0.590 9.00625  ? 207 ASP A O   1 
ATOM   1602 O  O   B ASP A 1 312 ? 59.95087 57.69209 32.03086 0.410 8.78431  ? 207 ASP A O   1 
ATOM   1603 C  CB  A ASP A 1 312 ? 61.39409 57.69134 34.45132 0.590 8.12939  ? 207 ASP A CB  1 
ATOM   1604 C  CB  B ASP A 1 312 ? 61.45497 57.64324 34.37269 0.410 8.17335  ? 207 ASP A CB  1 
ATOM   1605 C  CG  A ASP A 1 312 ? 61.94948 57.75836 35.84762 0.590 12.19036 ? 207 ASP A CG  1 
ATOM   1606 C  CG  B ASP A 1 312 ? 61.37564 59.15582 34.41510 0.410 15.54705 ? 207 ASP A CG  1 
ATOM   1607 O  OD1 A ASP A 1 312 ? 61.16135 57.71770 36.82896 0.590 12.50807 ? 207 ASP A OD1 1 
ATOM   1608 O  OD1 B ASP A 1 312 ? 60.32987 59.69777 34.82555 0.410 16.98266 ? 207 ASP A OD1 1 
ATOM   1609 O  OD2 A ASP A 1 312 ? 63.19528 57.84210 35.97111 0.590 14.83648 ? 207 ASP A OD2 1 
ATOM   1610 O  OD2 B ASP A 1 312 ? 62.37226 59.80669 34.02290 0.410 21.51198 ? 207 ASP A OD2 1 
ATOM   1611 N  N   . ILE A 1 313 ? 58.13507 56.67735 32.91344 1.000 6.13713  ? 208 ILE A N   1 
ATOM   1612 C  CA  . ILE A 1 313 ? 57.35307 56.67235 31.68282 1.000 5.87835  ? 208 ILE A CA  1 
ATOM   1613 C  C   . ILE A 1 313 ? 56.28633 57.76986 31.76262 1.000 6.41290  ? 208 ILE A C   1 
ATOM   1614 O  O   . ILE A 1 313 ? 55.40106 57.72349 32.63706 1.000 6.69645  ? 208 ILE A O   1 
ATOM   1615 C  CB  . ILE A 1 313 ? 56.70001 55.29325 31.45201 1.000 5.50071  ? 208 ILE A CB  1 
ATOM   1616 C  CG1 . ILE A 1 313 ? 57.74969 54.15539 31.39940 1.000 6.05149  ? 208 ILE A CG1 1 
ATOM   1617 C  CG2 . ILE A 1 313 ? 55.81209 55.32794 30.18954 1.000 6.99576  ? 208 ILE A CG2 1 
ATOM   1618 C  CD1 . ILE A 1 313 ? 58.78842 54.34533 30.30870 1.000 7.97183  ? 208 ILE A CD1 1 
ATOM   1619 N  N   . LEU A 1 314 ? 56.38130 58.77014 30.85847 1.000 7.52051  ? 209 LEU A N   1 
ATOM   1620 C  CA  . LEU A 1 314 ? 55.41997 59.88043 30.81365 1.000 6.32288  ? 209 LEU A CA  1 
ATOM   1621 C  C   . LEU A 1 314 ? 54.19659 59.45101 30.00713 1.000 7.06233  ? 209 LEU A C   1 
ATOM   1622 O  O   . LEU A 1 314 ? 54.33641 58.92960 28.89482 1.000 7.32693  ? 209 LEU A O   1 
ATOM   1623 C  CB  . LEU A 1 314 ? 56.08506 61.09493 30.14293 1.000 6.70925  ? 209 LEU A CB  1 
ATOM   1624 C  CG  . LEU A 1 314 ? 55.23700 62.34403 29.94958 1.000 9.33462  ? 209 LEU A CG  1 
ATOM   1625 C  CD1 . LEU A 1 314 ? 54.89016 62.88981 31.30255 1.000 13.92446 ? 209 LEU A CD1 1 
ATOM   1626 C  CD2 . LEU A 1 314 ? 56.08708 63.33015 29.16359 1.000 12.35077 ? 209 LEU A CD2 1 
ATOM   1627 N  N   . SER A 1 315 ? 53.00653 59.69081 30.55760 1.000 6.06768  ? 210 SER A N   1 
ATOM   1628 C  CA  . SER A 1 315 ? 51.77392 59.35413 29.83759 1.000 5.89583  ? 210 SER A CA  1 
ATOM   1629 C  C   . SER A 1 315 ? 50.64019 60.21063 30.39824 1.000 6.15198  ? 210 SER A C   1 
ATOM   1630 O  O   . SER A 1 315 ? 50.85276 61.08668 31.25416 1.000 7.61731  ? 210 SER A O   1 
ATOM   1631 C  CB  . SER A 1 315 ? 51.49623 57.84555 29.93950 1.000 5.50257  ? 210 SER A CB  1 
ATOM   1632 O  OG  . SER A 1 315 ? 50.44068 57.51173 29.04628 1.000 6.02938  ? 210 SER A OG  1 
ATOM   1633 N  N   . THR A 1 316 ? 49.41672 59.94183 29.89763 1.000 6.07206  ? 211 THR A N   1 
ATOM   1634 C  CA  . THR A 1 316 ? 48.21138 60.62511 30.34587 1.000 6.35136  ? 211 THR A CA  1 
ATOM   1635 C  C   . THR A 1 316 ? 47.84570 60.26020 31.78811 1.000 7.18324  ? 211 THR A C   1 
ATOM   1636 O  O   . THR A 1 316 ? 48.18515 59.19260 32.29099 1.000 9.31414  ? 211 THR A O   1 
ATOM   1637 C  CB  . THR A 1 316 ? 47.04004 60.23444 29.44034 1.000 6.82146  ? 211 THR A CB  1 
ATOM   1638 O  OG1 . THR A 1 316 ? 47.11924 58.82639 29.15442 1.000 7.15719  ? 211 THR A OG1 1 
ATOM   1639 C  CG2 . THR A 1 316 ? 47.16209 60.97761 28.08801 1.000 9.09217  ? 211 THR A CG2 1 
ATOM   1640 N  N   . TRP A 1 317 ? 47.13393 61.17702 32.44419 1.000 6.76231  ? 212 TRP A N   1 
ATOM   1641 C  CA  . TRP A 1 317 ? 46.63892 60.98352 33.80141 1.000 7.54407  ? 212 TRP A CA  1 
ATOM   1642 C  C   . TRP A 1 317 ? 45.26078 61.61989 33.89770 1.000 8.91192  ? 212 TRP A C   1 
ATOM   1643 O  O   . TRP A 1 317 ? 44.85036 62.37193 33.00555 1.000 9.46774  ? 212 TRP A O   1 
ATOM   1644 C  CB  . TRP A 1 317 ? 47.58390 61.61724 34.83639 1.000 8.24753  ? 212 TRP A CB  1 
ATOM   1645 C  CG  . TRP A 1 317 ? 47.39945 61.08508 36.25958 1.000 7.29775  ? 212 TRP A CG  1 
ATOM   1646 C  CD1 . TRP A 1 317 ? 46.80316 61.73207 37.32335 1.000 8.91214  ? 212 TRP A CD1 1 
ATOM   1647 C  CD2 . TRP A 1 317 ? 47.85379 59.81497 36.76964 1.000 7.65684  ? 212 TRP A CD2 1 
ATOM   1648 N  NE1 . TRP A 1 317 ? 46.86077 60.93226 38.46026 1.000 9.79807  ? 212 TRP A NE1 1 
ATOM   1649 C  CE2 . TRP A 1 317 ? 47.49808 59.76152 38.14007 1.000 8.38953  ? 212 TRP A CE2 1 
ATOM   1650 C  CE3 . TRP A 1 317 ? 48.52686 58.72545 36.20079 1.000 6.99984  ? 212 TRP A CE3 1 
ATOM   1651 C  CZ2 . TRP A 1 317 ? 47.81524 58.66448 38.95627 1.000 8.02923  ? 212 TRP A CZ2 1 
ATOM   1652 C  CZ3 . TRP A 1 317 ? 48.84024 57.62444 37.02102 1.000 8.12801  ? 212 TRP A CZ3 1 
ATOM   1653 C  CH2 . TRP A 1 317 ? 48.46829 57.61035 38.37458 1.000 8.77322  ? 212 TRP A CH2 1 
ATOM   1654 N  N   . ILE A 1 318 ? 44.54055 61.28691 34.97701 1.000 7.44004  ? 213 ILE A N   1 
ATOM   1655 C  CA  . ILE A 1 318 ? 43.18823 61.82860 35.12873 1.000 7.86460  ? 213 ILE A CA  1 
ATOM   1656 C  C   . ILE A 1 318 ? 43.22562 63.33890 35.40528 1.000 9.05750  ? 213 ILE A C   1 
ATOM   1657 O  O   . ILE A 1 318 ? 44.26563 63.95088 35.70996 1.000 10.37312 ? 213 ILE A O   1 
ATOM   1658 C  CB  . ILE A 1 318 ? 42.40833 61.07125 36.20616 1.000 7.95373  ? 213 ILE A CB  1 
ATOM   1659 C  CG1 . ILE A 1 318 ? 43.15075 61.10835 37.54244 1.000 14.25473 ? 213 ILE A CG1 1 
ATOM   1660 C  CG2 . ILE A 1 318 ? 42.20268 59.62494 35.76532 1.000 8.72246  ? 213 ILE A CG2 1 
ATOM   1661 C  CD1 . ILE A 1 318 ? 42.27071 60.59867 38.72138 1.000 12.22657 ? 213 ILE A CD1 1 
ATOM   1662 N  N   . GLY A 1 319 ? 42.06396 63.94883 35.22331 1.000 8.87830  ? 214 GLY A N   1 
ATOM   1663 C  CA  . GLY A 1 319 ? 41.98884 65.39838 35.25999 1.000 10.63575 ? 214 GLY A CA  1 
ATOM   1664 C  C   . GLY A 1 319 ? 42.60410 66.06676 34.05867 1.000 11.64108 ? 214 GLY A C   1 
ATOM   1665 O  O   . GLY A 1 319 ? 42.97735 67.24785 34.15270 1.000 13.61527 ? 214 GLY A O   1 
ATOM   1666 N  N   . GLY A 1 320 ? 42.68603 65.36242 32.92600 1.000 9.53434  ? 215 GLY A N   1 
ATOM   1667 C  CA  . GLY A 1 320 ? 43.25423 65.93882 31.71198 1.000 10.00901 ? 215 GLY A CA  1 
ATOM   1668 C  C   . GLY A 1 320 ? 44.72477 66.27154 31.82476 1.000 12.20889 ? 215 GLY A C   1 
ATOM   1669 O  O   . GLY A 1 320 ? 45.20248 67.19837 31.16294 1.000 13.95387 ? 215 GLY A O   1 
ATOM   1670 N  N   A SER A 1 321 ? 45.45049 65.55131 32.67982 0.674 9.27702  ? 216 SER A N   1 
ATOM   1671 N  N   B SER A 1 321 ? 45.46058 65.53066 32.63998 0.326 9.32033  ? 216 SER A N   1 
ATOM   1672 C  CA  A SER A 1 321 ? 46.83050 65.87312 33.01709 0.674 8.60230  ? 216 SER A CA  1 
ATOM   1673 C  CA  B SER A 1 321 ? 46.83710 65.86851 32.97199 0.326 8.59455  ? 216 SER A CA  1 
ATOM   1674 C  C   A SER A 1 321 ? 47.80401 64.83063 32.42510 0.674 8.02198  ? 216 SER A C   1 
ATOM   1675 C  C   B SER A 1 321 ? 47.79985 64.78675 32.46021 0.326 8.00838  ? 216 SER A C   1 
ATOM   1676 O  O   A SER A 1 321 ? 47.43993 63.98206 31.59699 0.674 8.97581  ? 216 SER A O   1 
ATOM   1677 O  O   B SER A 1 321 ? 47.41764 63.86526 31.72828 0.326 8.88111  ? 216 SER A O   1 
ATOM   1678 C  CB  A SER A 1 321 ? 46.96740 66.00177 34.55154 0.674 9.46906  ? 216 SER A CB  1 
ATOM   1679 C  CB  B SER A 1 321 ? 46.95958 66.08176 34.48472 0.326 9.54859  ? 216 SER A CB  1 
ATOM   1680 O  OG  A SER A 1 321 ? 46.76765 64.75755 35.21315 0.674 8.67109  ? 216 SER A OG  1 
ATOM   1681 O  OG  B SER A 1 321 ? 48.15737 66.75618 34.80125 0.326 9.10476  ? 216 SER A OG  1 
ATOM   1682 N  N   . THR A 1 322 ? 49.07093 64.91435 32.85374 1.000 8.37624  ? 217 THR A N   1 
ATOM   1683 C  CA  . THR A 1 322 ? 50.09903 63.93617 32.51685 1.000 7.56498  ? 217 THR A CA  1 
ATOM   1684 C  C   . THR A 1 322 ? 50.94234 63.69939 33.75268 1.000 7.61156  ? 217 THR A C   1 
ATOM   1685 O  O   . THR A 1 322 ? 51.02838 64.55455 34.62651 1.000 11.96492 ? 217 THR A O   1 
ATOM   1686 C  CB  . THR A 1 322 ? 51.02831 64.39243 31.37850 1.000 9.19024  ? 217 THR A CB  1 
ATOM   1687 O  OG1 . THR A 1 322 ? 51.64680 65.62884 31.77593 1.000 13.61090 ? 217 THR A OG1 1 
ATOM   1688 C  CG2 . THR A 1 322 ? 50.23783 64.64228 30.09798 1.000 11.40483 ? 217 THR A CG2 1 
ATOM   1689 N  N   . ARG A 1 323 ? 51.58482 62.53874 33.80022 1.000 7.21226  ? 218 ARG A N   1 
ATOM   1690 C  CA  . ARG A 1 323 ? 52.62598 62.35296 34.80967 1.000 8.55614  ? 218 ARG A CA  1 
ATOM   1691 C  C   . ARG A 1 323 ? 53.49614 61.16667 34.43678 1.000 6.93250  ? 218 ARG A C   1 
ATOM   1692 O  O   . ARG A 1 323 ? 53.18195 60.37252 33.54007 1.000 6.55006  ? 218 ARG A O   1 
ATOM   1693 C  CB  . ARG A 1 323 ? 52.07304 62.21169 36.23676 1.000 19.92878 ? 218 ARG A CB  1 
ATOM   1694 C  CG  . ARG A 1 323 ? 51.34844 60.96390 36.53672 1.000 11.75156 ? 218 ARG A CG  1 
ATOM   1695 C  CD  . ARG A 1 323 ? 50.96991 60.86310 38.07681 1.000 8.38411  ? 218 ARG A CD  1 
ATOM   1696 N  NE  . ARG A 1 323 ? 50.14683 62.01055 38.46470 1.000 9.54999  ? 218 ARG A NE  1 
ATOM   1697 C  CZ  . ARG A 1 323 ? 49.66843 62.21812 39.68881 1.000 9.62456  ? 218 ARG A CZ  1 
ATOM   1698 N  NH1 . ARG A 1 323 ? 49.93214 61.38705 40.68024 1.000 11.96411 ? 218 ARG A NH1 1 
ATOM   1699 N  NH2 . ARG A 1 323 ? 48.93148 63.30151 39.92404 1.000 11.32788 ? 218 ARG A NH2 1 
ATOM   1700 N  N   A SER A 1 324 ? 54.62887 61.08688 35.11978 0.591 8.23668  ? 219 SER A N   1 
ATOM   1701 N  N   B SER A 1 324 ? 54.62374 61.07692 35.13301 0.302 8.27841  ? 219 SER A N   1 
ATOM   1702 N  N   C SER A 1 324 ? 54.62535 61.05594 35.12754 0.107 8.30803  ? 219 SER A N   1 
ATOM   1703 C  CA  A SER A 1 324 ? 55.59995 60.01834 34.90396 0.591 7.91331  ? 219 SER A CA  1 
ATOM   1704 C  CA  B SER A 1 324 ? 55.61248 60.02712 34.92075 0.302 7.97102  ? 219 SER A CA  1 
ATOM   1705 C  CA  C SER A 1 324 ? 55.59860 60.00165 34.86172 0.107 7.97224  ? 219 SER A CA  1 
ATOM   1706 C  C   A SER A 1 324 ? 55.57463 59.08086 36.09931 0.591 8.50627  ? 219 SER A C   1 
ATOM   1707 C  C   B SER A 1 324 ? 55.58680 59.07910 36.10685 0.302 8.55272  ? 219 SER A C   1 
ATOM   1708 C  C   C SER A 1 324 ? 55.67661 59.07616 36.06665 0.107 8.58521  ? 219 SER A C   1 
ATOM   1709 O  O   A SER A 1 324 ? 55.67540 59.53406 37.24622 0.591 11.81795 ? 219 SER A O   1 
ATOM   1710 O  O   B SER A 1 324 ? 55.70816 59.52107 37.25539 0.302 11.70065 ? 219 SER A O   1 
ATOM   1711 O  O   C SER A 1 324 ? 55.95456 59.52925 37.18309 0.107 11.20195 ? 219 SER A O   1 
ATOM   1712 C  CB  A SER A 1 324 ? 56.99807 60.61674 34.72921 0.591 9.93423  ? 219 SER A CB  1 
ATOM   1713 C  CB  B SER A 1 324 ? 57.01011 60.63118 34.78219 0.302 9.87074  ? 219 SER A CB  1 
ATOM   1714 C  CB  C SER A 1 324 ? 56.97305 60.59283 34.55268 0.107 9.89576  ? 219 SER A CB  1 
ATOM   1715 O  OG  A SER A 1 324 ? 57.97962 59.62149 34.50739 0.591 11.95232 ? 219 SER A OG  1 
ATOM   1716 O  OG  B SER A 1 324 ? 57.08160 61.50260 33.67139 0.302 7.89224  ? 219 SER A OG  1 
ATOM   1717 O  OG  C SER A 1 324 ? 57.48527 61.28030 35.67750 0.107 9.92092  ? 219 SER A OG  1 
ATOM   1718 N  N   . ILE A 1 325 ? 55.44422 57.78267 35.83779 1.000 7.34607  ? 220 ILE A N   1 
ATOM   1719 C  CA  . ILE A 1 325 ? 55.49303 56.77226 36.89561 1.000 6.95558  ? 220 ILE A CA  1 
ATOM   1720 C  C   . ILE A 1 325 ? 56.24320 55.55881 36.34431 1.000 6.97692  ? 220 ILE A C   1 
ATOM   1721 O  O   . ILE A 1 325 ? 56.56050 55.47460 35.15132 1.000 7.22127  ? 220 ILE A O   1 
ATOM   1722 C  CB  . ILE A 1 325 ? 54.09208 56.37150 37.44286 1.000 9.05881  ? 220 ILE A CB  1 
ATOM   1723 C  CG1 . ILE A 1 325 ? 53.18588 55.87749 36.32652 1.000 11.54197 ? 220 ILE A CG1 1 
ATOM   1724 C  CG2 . ILE A 1 325 ? 53.40000 57.53448 38.17483 1.000 11.89940 ? 220 ILE A CG2 1 
ATOM   1725 C  CD1 . ILE A 1 325 ? 51.83232 55.19061 36.80186 1.000 11.59180 ? 220 ILE A CD1 1 
ATOM   1726 N  N   . SER A 1 326 ? 56.51912 54.59281 37.23267 1.000 7.44606  ? 221 SER A N   1 
ATOM   1727 C  CA  . SER A 1 326 ? 57.36666 53.45330 36.89369 1.000 6.74515  ? 221 SER A CA  1 
ATOM   1728 C  C   . SER A 1 326 ? 56.68769 52.13982 37.28289 1.000 9.34328  ? 221 SER A C   1 
ATOM   1729 O  O   . SER A 1 326 ? 55.96080 52.07605 38.27917 1.000 12.66750 ? 221 SER A O   1 
ATOM   1730 C  CB  . SER A 1 326 ? 58.71597 53.52232 37.61590 1.000 8.57620  ? 221 SER A CB  1 
ATOM   1731 O  OG  . SER A 1 326 ? 59.42447 54.73245 37.33214 1.000 9.18250  ? 221 SER A OG  1 
ATOM   1732 N  N   . GLY A 1 327 ? 56.92018 51.10431 36.49180 1.000 7.22335  ? 222 GLY A N   1 
ATOM   1733 C  CA  . GLY A 1 327 ? 56.47692 49.76910 36.85542 1.000 6.81368  ? 222 GLY A CA  1 
ATOM   1734 C  C   . GLY A 1 327 ? 56.50380 48.84415 35.66217 1.000 6.32769  ? 222 GLY A C   1 
ATOM   1735 O  O   . GLY A 1 327 ? 56.57493 49.27420 34.51473 1.000 7.71899  ? 222 GLY A O   1 
ATOM   1736 N  N   . THR A 1 328 ? 56.36709 47.52052 35.92740 1.000 6.41635  ? 223 THR A N   1 
ATOM   1737 C  CA  . THR A 1 328 ? 56.10003 46.64500 34.78812 1.000 6.57462  ? 223 THR A CA  1 
ATOM   1738 C  C   . THR A 1 328 ? 54.72652 46.92049 34.20058 1.000 5.97321  ? 223 THR A C   1 
ATOM   1739 O  O   . THR A 1 328 ? 54.49737 46.55874 33.04532 1.000 6.80069  ? 223 THR A O   1 
ATOM   1740 C  CB  . THR A 1 328 ? 56.21559 45.13377 35.12968 1.000 5.24296  ? 223 THR A CB  1 
ATOM   1741 O  OG1 . THR A 1 328 ? 55.32404 44.78260 36.20652 1.000 8.20836  ? 223 THR A OG1 1 
ATOM   1742 C  CG2 . THR A 1 328 ? 57.64280 44.76842 35.52787 1.000 7.32722  ? 223 THR A CG2 1 
ATOM   1743 N  N   . SER A 1 329 ? 53.84006 47.61755 34.95353 1.000 5.83736  ? 224 SER A N   1 
ATOM   1744 C  CA  . SER A 1 329 ? 52.57466 48.09104 34.40527 1.000 4.84278  ? 224 SER A CA  1 
ATOM   1745 C  C   . SER A 1 329 ? 52.78775 49.04943 33.25917 1.000 5.90336  ? 224 SER A C   1 
ATOM   1746 O  O   . SER A 1 329 ? 51.88789 49.19535 32.42005 1.000 5.57926  ? 224 SER A O   1 
ATOM   1747 C  CB  . SER A 1 329 ? 51.78694 48.88007 35.45118 1.000 9.81198  ? 224 SER A CB  1 
ATOM   1748 O  OG  . SER A 1 329 ? 51.27304 48.03182 36.46978 1.000 13.36397 ? 224 SER A OG  1 
ATOM   1749 N  N   . MET A 1 330 ? 53.93735 49.71656 33.21363 1.000 5.88124  ? 225 MET A N   1 
ATOM   1750 C  CA  . MET A 1 330 ? 54.14322 50.72533 32.18977 1.000 4.66007  ? 225 MET A CA  1 
ATOM   1751 C  C   . MET A 1 330 ? 54.82735 50.06524 30.97425 1.000 4.57443  ? 225 MET A C   1 
ATOM   1752 O  O   . MET A 1 330 ? 54.70021 50.52898 29.83432 1.000 6.21791  ? 225 MET A O   1 
ATOM   1753 C  CB  . MET A 1 330 ? 55.12257 51.84365 32.62006 1.000 6.82668  ? 225 MET A CB  1 
ATOM   1754 C  CG  . MET A 1 330 ? 54.69233 52.92381 33.64677 1.000 9.06265  ? 225 MET A CG  1 
ATOM   1755 S  SD  . MET A 1 330 ? 53.79108 52.30509 35.14517 1.000 8.17342  ? 225 MET A SD  1 
ATOM   1756 C  CE  . MET A 1 330 ? 52.05579 52.33335 34.69044 1.000 11.56251 ? 225 MET A CE  1 
ATOM   1757 N  N   . ALA A 1 331 ? 55.57478 48.96409 31.19605 1.000 4.90964  ? 226 ALA A N   1 
ATOM   1758 C  CA  . ALA A 1 331 ? 56.20797 48.25140 30.09707 1.000 6.12930  ? 226 ALA A CA  1 
ATOM   1759 C  C   . ALA A 1 331 ? 55.17380 47.49129 29.27384 1.000 4.81220  ? 226 ALA A C   1 
ATOM   1760 O  O   . ALA A 1 331 ? 55.26541 47.44335 28.03707 1.000 6.50228  ? 226 ALA A O   1 
ATOM   1761 C  CB  . ALA A 1 331 ? 57.27341 47.27983 30.65770 1.000 6.98772  ? 226 ALA A CB  1 
ATOM   1762 N  N   . THR A 1 332 ? 54.18438 46.89082 29.94948 1.000 4.38901  ? 227 THR A N   1 
ATOM   1763 C  CA  . THR A 1 332 ? 53.18481 46.06138 29.26627 1.000 4.18141  ? 227 THR A CA  1 
ATOM   1764 C  C   . THR A 1 332 ? 52.45473 46.81050 28.14119 1.000 5.24144  ? 227 THR A C   1 
ATOM   1765 O  O   . THR A 1 332 ? 52.35821 46.25885 27.02742 1.000 5.07844  ? 227 THR A O   1 
ATOM   1766 C  CB  . THR A 1 332 ? 52.22396 45.51270 30.32749 1.000 5.50047  ? 227 THR A CB  1 
ATOM   1767 O  OG1 . THR A 1 332 ? 52.98640 44.74037 31.29292 1.000 5.93635  ? 227 THR A OG1 1 
ATOM   1768 C  CG2 . THR A 1 332 ? 51.14302 44.61150 29.67944 1.000 8.01984  ? 227 THR A CG2 1 
ATOM   1769 N  N   . PRO A 1 333 ? 51.95577 48.03694 28.32780 1.000 4.66549  ? 228 PRO A N   1 
ATOM   1770 C  CA  . PRO A 1 333 ? 51.27418 48.70907 27.21785 1.000 4.31610  ? 228 PRO A CA  1 
ATOM   1771 C  C   . PRO A 1 333 ? 52.18113 49.08640 26.06022 1.000 4.96394  ? 228 PRO A C   1 
ATOM   1772 O  O   . PRO A 1 333 ? 51.66999 49.25410 24.94457 1.000 6.29221  ? 228 PRO A O   1 
ATOM   1773 C  CB  . PRO A 1 333 ? 50.65419 49.97010 27.85705 1.000 5.55659  ? 228 PRO A CB  1 
ATOM   1774 C  CG  . PRO A 1 333 ? 51.38458 50.14045 29.15909 1.000 5.99868  ? 228 PRO A CG  1 
ATOM   1775 C  CD  . PRO A 1 333 ? 51.75238 48.73667 29.60283 1.000 4.14973  ? 228 PRO A CD  1 
ATOM   1776 N  N   . HIS A 1 334 ? 53.50008 49.21340 26.27143 1.000 4.34142  ? 229 HIS A N   1 
ATOM   1777 C  CA  . HIS A 1 334 ? 54.37365 49.40394 25.11240 1.000 4.89556  ? 229 HIS A CA  1 
ATOM   1778 C  C   . HIS A 1 334 ? 54.30037 48.17678 24.21154 1.000 6.19226  ? 229 HIS A C   1 
ATOM   1779 O  O   . HIS A 1 334 ? 54.26970 48.30733 22.98075 1.000 6.53270  ? 229 HIS A O   1 
ATOM   1780 C  CB  . HIS A 1 334 ? 55.84145 49.61891 25.54800 1.000 5.77412  ? 229 HIS A CB  1 
ATOM   1781 C  CG  . HIS A 1 334 ? 56.16461 50.99287 26.04601 1.000 5.09747  ? 229 HIS A CG  1 
ATOM   1782 N  ND1 . HIS A 1 334 ? 56.08513 51.32349 27.38341 1.000 6.11791  ? 229 HIS A ND1 1 
ATOM   1783 C  CD2 . HIS A 1 334 ? 56.71314 52.06906 25.41801 1.000 6.41893  ? 229 HIS A CD2 1 
ATOM   1784 C  CE1 . HIS A 1 334 ? 56.49062 52.57855 27.54358 1.000 7.30238  ? 229 HIS A CE1 1 
ATOM   1785 N  NE2 . HIS A 1 334 ? 56.87315 53.05830 26.36656 1.000 7.47844  ? 229 HIS A NE2 1 
ATOM   1786 N  N   . VAL A 1 335 ? 54.30345 46.95817 24.81934 1.000 5.17049  ? 230 VAL A N   1 
ATOM   1787 C  CA  . VAL A 1 335 ? 54.25987 45.73097 24.03180 1.000 5.01054  ? 230 VAL A CA  1 
ATOM   1788 C  C   . VAL A 1 335 ? 52.86285 45.51998 23.44558 1.000 7.56587  ? 230 VAL A C   1 
ATOM   1789 O  O   . VAL A 1 335 ? 52.73375 45.12214 22.28677 1.000 6.80272  ? 230 VAL A O   1 
ATOM   1790 C  CB  . VAL A 1 335 ? 54.73546 44.54817 24.89909 1.000 4.64722  ? 230 VAL A CB  1 
ATOM   1791 C  CG1 . VAL A 1 335 ? 54.43966 43.19464 24.24085 1.000 7.78924  ? 230 VAL A CG1 1 
ATOM   1792 C  CG2 . VAL A 1 335 ? 56.25437 44.69766 25.19170 1.000 7.37986  ? 230 VAL A CG2 1 
ATOM   1793 N  N   . ALA A 1 336 ? 51.79087 45.82260 24.21243 1.000 5.49669  ? 231 ALA A N   1 
ATOM   1794 C  CA  . ALA A 1 336 ? 50.42898 45.72407 23.65918 1.000 4.24590  ? 231 ALA A CA  1 
ATOM   1795 C  C   . ALA A 1 336 ? 50.23473 46.66881 22.47441 1.000 5.71832  ? 231 ALA A C   1 
ATOM   1796 O  O   . ALA A 1 336 ? 49.67130 46.28531 21.43207 1.000 5.55448  ? 231 ALA A O   1 
ATOM   1797 C  CB  . ALA A 1 336 ? 49.41277 46.06867 24.75820 1.000 6.02749  ? 231 ALA A CB  1 
ATOM   1798 N  N   . GLY A 1 337 ? 50.70317 47.91431 22.60525 1.000 4.46856  ? 232 GLY A N   1 
ATOM   1799 C  CA  . GLY A 1 337 ? 50.62844 48.85087 21.48577 1.000 4.84057  ? 232 GLY A CA  1 
ATOM   1800 C  C   . GLY A 1 337 ? 51.46564 48.38999 20.29284 1.000 5.39383  ? 232 GLY A C   1 
ATOM   1801 O  O   . GLY A 1 337 ? 51.05522 48.56105 19.13816 1.000 7.99641  ? 232 GLY A O   1 
ATOM   1802 N  N   . LEU A 1 338 ? 52.68300 47.86979 20.55610 1.000 5.02505  ? 233 LEU A N   1 
ATOM   1803 C  CA  . LEU A 1 338 ? 53.51239 47.35704 19.45758 1.000 5.56881  ? 233 LEU A CA  1 
ATOM   1804 C  C   . LEU A 1 338 ? 52.81049 46.20949 18.72158 1.000 6.44783  ? 233 LEU A C   1 
ATOM   1805 O  O   . LEU A 1 338 ? 52.83264 46.14429 17.48068 1.000 6.79351  ? 233 LEU A O   1 
ATOM   1806 C  CB  . LEU A 1 338 ? 54.86956 46.90803 20.00960 1.000 5.62850  ? 233 LEU A CB  1 
ATOM   1807 C  CG  . LEU A 1 338 ? 55.83135 46.36339 18.96351 1.000 8.20634  ? 233 LEU A CG  1 
ATOM   1808 C  CD1 . LEU A 1 338 ? 56.11911 47.40142 17.82632 1.000 11.05720 ? 233 LEU A CD1 1 
ATOM   1809 C  CD2 . LEU A 1 338 ? 57.13207 45.90441 19.63510 1.000 10.77798 ? 233 LEU A CD2 1 
ATOM   1810 N  N   . ALA A 1 339 ? 52.15591 45.30848 19.45866 1.000 6.74093  ? 234 ALA A N   1 
ATOM   1811 C  CA  . ALA A 1 339 ? 51.42451 44.23592 18.80690 1.000 5.18797  ? 234 ALA A CA  1 
ATOM   1812 C  C   . ALA A 1 339 ? 50.31601 44.78703 17.90049 1.000 6.24934  ? 234 ALA A C   1 
ATOM   1813 O  O   . ALA A 1 339 ? 50.12154 44.30272 16.77532 1.000 7.18556  ? 234 ALA A O   1 
ATOM   1814 C  CB  . ALA A 1 339 ? 50.87901 43.26192 19.87725 1.000 5.66619  ? 234 ALA A CB  1 
ATOM   1815 N  N   . ALA A 1 340 ? 49.52443 45.74528 18.40005 1.000 5.20574  ? 235 ALA A N   1 
ATOM   1816 C  CA  . ALA A 1 340 ? 48.47001 46.32977 17.55996 1.000 5.44067  ? 235 ALA A CA  1 
ATOM   1817 C  C   . ALA A 1 340 ? 49.04591 46.94582 16.29772 1.000 7.14942  ? 235 ALA A C   1 
ATOM   1818 O  O   . ALA A 1 340 ? 48.50490 46.75711 15.19583 1.000 8.56927  ? 235 ALA A O   1 
ATOM   1819 C  CB  . ALA A 1 340 ? 47.66368 47.39039 18.34975 1.000 7.66787  ? 235 ALA A CB  1 
ATOM   1820 N  N   . TYR A 1 341 ? 50.16182 47.67696 16.44544 1.000 7.05121  ? 236 TYR A N   1 
ATOM   1821 C  CA  . TYR A 1 341 ? 50.84976 48.29174 15.31395 1.000 6.23745  ? 236 TYR A CA  1 
ATOM   1822 C  C   . TYR A 1 341 ? 51.31160 47.25671 14.28853 1.000 6.72169  ? 236 TYR A C   1 
ATOM   1823 O  O   . TYR A 1 341 ? 51.11920 47.44197 13.07100 1.000 7.88846  ? 236 TYR A O   1 
ATOM   1824 C  CB  . TYR A 1 341 ? 52.03352 49.09964 15.88358 1.000 6.15432  ? 236 TYR A CB  1 
ATOM   1825 C  CG  . TYR A 1 341 ? 53.05105 49.60335 14.86572 1.000 6.60750  ? 236 TYR A CG  1 
ATOM   1826 C  CD1 . TYR A 1 341 ? 52.91377 50.86700 14.28144 1.000 9.02645  ? 236 TYR A CD1 1 
ATOM   1827 C  CD2 . TYR A 1 341 ? 54.17984 48.85764 14.56370 1.000 8.26976  ? 236 TYR A CD2 1 
ATOM   1828 C  CE1 . TYR A 1 341 ? 53.85230 51.33213 13.40618 1.000 9.30989  ? 236 TYR A CE1 1 
ATOM   1829 C  CE2 . TYR A 1 341 ? 55.12284 49.31469 13.67234 1.000 8.59697  ? 236 TYR A CE2 1 
ATOM   1830 C  CZ  . TYR A 1 341 ? 54.97645 50.56617 13.12148 1.000 11.24209 ? 236 TYR A CZ  1 
ATOM   1831 O  OH  . TYR A 1 341 ? 55.92826 51.01432 12.25092 1.000 11.49470 ? 236 TYR A OH  1 
ATOM   1832 N  N   . LEU A 1 342 ? 51.90434 46.15326 14.76340 1.000 6.40417  ? 237 LEU A N   1 
ATOM   1833 C  CA  . LEU A 1 342 ? 52.38822 45.13432 13.83668 1.000 6.77532  ? 237 LEU A CA  1 
ATOM   1834 C  C   . LEU A 1 342 ? 51.24737 44.34435 13.19133 1.000 8.10519  ? 237 LEU A C   1 
ATOM   1835 O  O   . LEU A 1 342 ? 51.35323 43.92603 12.01015 1.000 9.43625  ? 237 LEU A O   1 
ATOM   1836 C  CB  . LEU A 1 342 ? 53.31067 44.16660 14.57546 1.000 7.15865  ? 237 LEU A CB  1 
ATOM   1837 C  CG  . LEU A 1 342 ? 54.60186 44.83034 15.05908 1.000 8.82172  ? 237 LEU A CG  1 
ATOM   1838 C  CD1 . LEU A 1 342 ? 55.32670 43.86123 16.03020 1.000 10.60028 ? 237 LEU A CD1 1 
ATOM   1839 C  CD2 . LEU A 1 342 ? 55.49835 45.23329 13.88559 1.000 10.21967 ? 237 LEU A CD2 1 
ATOM   1840 N  N   . MET A 1 343 ? 50.14898 44.13174 13.91369 1.000 7.15102  ? 238 MET A N   1 
ATOM   1841 C  CA  . MET A 1 343 ? 49.00620 43.45180 13.29619 1.000 6.88262  ? 238 MET A CA  1 
ATOM   1842 C  C   . MET A 1 343 ? 48.36806 44.30520 12.19796 1.000 7.91327  ? 238 MET A C   1 
ATOM   1843 O  O   . MET A 1 343 ? 47.98917 43.77486 11.12902 1.000 9.34081  ? 238 MET A O   1 
ATOM   1844 C  CB  . MET A 1 343 ? 47.95072 43.08491 14.37009 1.000 9.18509  ? 238 MET A CB  1 
ATOM   1845 C  CG  . MET A 1 343 ? 48.42612 41.92028 15.26370 1.000 9.02868  ? 238 MET A CG  1 
ATOM   1846 S  SD  . MET A 1 343 ? 47.77546 41.87793 17.00130 1.000 20.08954 ? 238 MET A SD  1 
ATOM   1847 C  CE  . MET A 1 343 ? 46.13764 41.50209 16.46356 1.000 18.36994 ? 238 MET A CE  1 
ATOM   1848 N  N   . THR A 1 344 ? 48.26646 45.63260 12.40641 1.000 7.22015  ? 239 THR A N   1 
ATOM   1849 C  CA  . THR A 1 344 ? 47.75476 46.49385 11.34587 1.000 7.70808  ? 239 THR A CA  1 
ATOM   1850 C  C   . THR A 1 344 ? 48.63474 46.44396 10.08824 1.000 8.85956  ? 239 THR A C   1 
ATOM   1851 O  O   . THR A 1 344 ? 48.12481 46.49037 8.95434  1.000 12.69550 ? 239 THR A O   1 
ATOM   1852 C  CB  . THR A 1 344 ? 47.67196 47.92580 11.89235 1.000 8.37293  ? 239 THR A CB  1 
ATOM   1853 O  OG1 . THR A 1 344 ? 46.60155 47.98309 12.84426 1.000 12.16100 ? 239 THR A OG1 1 
ATOM   1854 C  CG2 . THR A 1 344 ? 47.47699 48.96506 10.79741 1.000 11.01888 ? 239 THR A CG2 1 
ATOM   1855 N  N   . LEU A 1 345 ? 49.96653 46.35747 10.25823 1.000 9.53429  ? 240 LEU A N   1 
ATOM   1856 C  CA  . LEU A 1 345 ? 50.87607 46.21703 9.12098  1.000 8.89056  ? 240 LEU A CA  1 
ATOM   1857 C  C   . LEU A 1 345 ? 50.82479 44.84101 8.47476  1.000 11.25644 ? 240 LEU A C   1 
ATOM   1858 O  O   . LEU A 1 345 ? 51.41713 44.66885 7.39811  1.000 15.75474 ? 240 LEU A O   1 
ATOM   1859 C  CB  . LEU A 1 345 ? 52.31599 46.48017 9.58994  1.000 10.92785 ? 240 LEU A CB  1 
ATOM   1860 C  CG  . LEU A 1 345 ? 52.62305 47.95608 9.85000  1.000 15.45887 ? 240 LEU A CG  1 
ATOM   1861 C  CD1 . LEU A 1 345 ? 53.99699 48.12381 10.46438 1.000 19.93193 ? 240 LEU A CD1 1 
ATOM   1862 C  CD2 . LEU A 1 345 ? 52.56177 48.70625 8.54874  1.000 18.98518 ? 240 LEU A CD2 1 
ATOM   1863 N  N   . GLY A 1 346 ? 50.15102 43.88595 9.09247  1.000 8.94555  ? 241 GLY A N   1 
ATOM   1864 C  CA  . GLY A 1 346 ? 50.05218 42.55063 8.51929  1.000 9.10322  ? 241 GLY A CA  1 
ATOM   1865 C  C   . GLY A 1 346 ? 51.24014 41.64561 8.76624  1.000 9.85625  ? 241 GLY A C   1 
ATOM   1866 O  O   . GLY A 1 346 ? 51.36209 40.60935 8.09739  1.000 13.93988 ? 241 GLY A O   1 
ATOM   1867 N  N   . LYS A 1 347 ? 52.13748 42.02695 9.66040  1.000 10.73027 ? 242 LYS A N   1 
ATOM   1868 C  CA  . LYS A 1 347 ? 53.35503 41.26366 9.88816  1.000 8.74687  ? 242 LYS A CA  1 
ATOM   1869 C  C   . LYS A 1 347 ? 53.11324 40.04782 10.74986 1.000 10.34350 ? 242 LYS A C   1 
ATOM   1870 O  O   . LYS A 1 347 ? 53.91623 39.10456 10.68497 1.000 12.76637 ? 242 LYS A O   1 
ATOM   1871 C  CB  . LYS A 1 347 ? 54.42698 42.14182 10.54816 1.000 12.21663 ? 242 LYS A CB  1 
ATOM   1872 C  CG  . LYS A 1 347 ? 54.73820 43.36095 9.69043  1.000 20.79994 ? 242 LYS A CG  1 
ATOM   1873 C  CD  . LYS A 1 347 ? 56.23320 43.60414 9.65210  1.000 36.64296 ? 242 LYS A CD  1 
ATOM   1874 C  CE  . LYS A 1 347 ? 56.63037 44.82490 8.83090  1.000 41.07282 ? 242 LYS A CE  1 
ATOM   1875 N  NZ  . LYS A 1 347 ? 56.35829 44.64948 7.37544  1.000 40.47582 ? 242 LYS A NZ  1 
ATOM   1876 N  N   . THR A 1 348 ? 52.04332 40.05391 11.54426 1.000 10.44138 ? 243 THR A N   1 
ATOM   1877 C  CA  . THR A 1 348 ? 51.81447 38.95809 12.47410 1.000 9.80517  ? 243 THR A CA  1 
ATOM   1878 C  C   . THR A 1 348 ? 50.33140 38.93036 12.82629 1.000 12.65231 ? 243 THR A C   1 
ATOM   1879 O  O   . THR A 1 348 ? 49.55182 39.77779 12.38271 1.000 11.92141 ? 243 THR A O   1 
ATOM   1880 C  CB  . THR A 1 348 ? 52.70132 39.10619 13.71944 1.000 13.28752 ? 243 THR A CB  1 
ATOM   1881 O  OG1 . THR A 1 348 ? 52.63164 37.91199 14.51564 1.000 11.92998 ? 243 THR A OG1 1 
ATOM   1882 C  CG2 . THR A 1 348 ? 52.28188 40.31068 14.58908 1.000 10.10084 ? 243 THR A CG2 1 
ATOM   1883 N  N   . THR A 1 349 ? 49.93891 37.91090 13.57663 1.000 10.32937 ? 244 THR A N   1 
ATOM   1884 C  CA  . THR A 1 349 ? 48.55325 37.69537 14.00006 1.000 11.80492 ? 244 THR A CA  1 
ATOM   1885 C  C   . THR A 1 349 ? 48.51475 37.66847 15.51564 1.000 10.62080 ? 244 THR A C   1 
ATOM   1886 O  O   . THR A 1 349 ? 49.55524 37.63041 16.16616 1.000 10.20113 ? 244 THR A O   1 
ATOM   1887 C  CB  . THR A 1 349 ? 48.00463 36.35750 13.49136 1.000 14.66016 ? 244 THR A CB  1 
ATOM   1888 O  OG1 . THR A 1 349 ? 48.74810 35.30638 14.13975 1.000 17.02031 ? 244 THR A OG1 1 
ATOM   1889 C  CG2 . THR A 1 349 ? 48.22259 36.23840 12.00939 1.000 15.93656 ? 244 THR A CG2 1 
ATOM   1890 N  N   . ALA A 1 350 ? 47.29624 37.66891 16.08939 1.000 10.67348 ? 245 ALA A N   1 
ATOM   1891 C  CA  . ALA A 1 350 ? 47.19536 37.64441 17.55286 1.000 8.58135  ? 245 ALA A CA  1 
ATOM   1892 C  C   . ALA A 1 350 ? 47.83885 36.39868 18.13418 1.000 10.80915 ? 245 ALA A C   1 
ATOM   1893 O  O   . ALA A 1 350 ? 48.40671 36.44914 19.23587 1.000 12.25264 ? 245 ALA A O   1 
ATOM   1894 C  CB  . ALA A 1 350 ? 45.72392 37.71559 17.99907 1.000 9.32503  ? 245 ALA A CB  1 
ATOM   1895 N  N   . ALA A 1 351 ? 47.72695 35.25570 17.43636 1.000 8.92001  ? 246 ALA A N   1 
ATOM   1896 C  CA  . ALA A 1 351 ? 48.24291 34.01165 17.97754 1.000 11.02118 ? 246 ALA A CA  1 
ATOM   1897 C  C   . ALA A 1 351 ? 49.75535 33.99998 18.02942 1.000 11.90886 ? 246 ALA A C   1 
ATOM   1898 O  O   . ALA A 1 351 ? 50.33713 33.35761 18.90823 1.000 14.94149 ? 246 ALA A O   1 
ATOM   1899 C  CB  . ALA A 1 351 ? 47.77074 32.80853 17.15307 1.000 13.15373 ? 246 ALA A CB  1 
ATOM   1900 N  N   A SER A 1 352 ? 50.41554 34.68399 17.09740 0.574 7.00619  ? 247 SER A N   1 
ATOM   1901 N  N   B SER A 1 352 ? 50.40189 34.71580 17.11213 0.426 7.07788  ? 247 SER A N   1 
ATOM   1902 C  CA  A SER A 1 352 ? 51.86419 34.58574 16.97754 0.574 9.90410  ? 247 SER A CA  1 
ATOM   1903 C  CA  B SER A 1 352 ? 51.83851 34.62260 16.91241 0.426 9.98183  ? 247 SER A CA  1 
ATOM   1904 C  C   A SER A 1 352 ? 52.58821 35.89735 17.26796 0.574 12.01342 ? 247 SER A C   1 
ATOM   1905 C  C   B SER A 1 352 ? 52.58940 35.88033 17.32059 0.426 12.02403 ? 247 SER A C   1 
ATOM   1906 O  O   A SER A 1 352 ? 53.81203 35.95335 17.10977 0.574 9.80562  ? 247 SER A O   1 
ATOM   1907 O  O   B SER A 1 352 ? 53.82463 35.88112 17.28601 0.426 9.65041  ? 247 SER A O   1 
ATOM   1908 C  CB  A SER A 1 352 ? 52.24813 34.08789 15.57097 0.574 10.78818 ? 247 SER A CB  1 
ATOM   1909 C  CB  B SER A 1 352 ? 52.13614 34.32781 15.43480 0.426 9.97229  ? 247 SER A CB  1 
ATOM   1910 O  OG  A SER A 1 352 ? 51.76629 34.96171 14.56159 0.574 14.64899 ? 247 SER A OG  1 
ATOM   1911 O  OG  B SER A 1 352 ? 51.58339 33.09019 15.05145 0.426 18.03423 ? 247 SER A OG  1 
ATOM   1912 N  N   . ALA A 1 353 ? 51.88683 36.94114 17.72407 1.000 8.16535  ? 248 ALA A N   1 
ATOM   1913 C  CA  . ALA A 1 353 ? 52.54362 38.23352 17.86236 1.000 6.08473  ? 248 ALA A CA  1 
ATOM   1914 C  C   . ALA A 1 353 ? 53.62413 38.23230 18.94346 1.000 8.77652  ? 248 ALA A C   1 
ATOM   1915 O  O   . ALA A 1 353 ? 54.65472 38.88154 18.78166 1.000 8.26249  ? 248 ALA A O   1 
ATOM   1916 C  CB  . ALA A 1 353 ? 51.48911 39.31728 18.13007 1.000 8.94299  ? 248 ALA A CB  1 
ATOM   1917 N  N   . CYS A 1 354 ? 53.40654 37.53550 20.06930 1.000 5.78149  ? 249 CYS A N   1 
ATOM   1918 C  CA  . CYS A 1 354 ? 54.43807 37.56208 21.11417 1.000 6.32700  ? 249 CYS A CA  1 
ATOM   1919 C  C   . CYS A 1 354 ? 55.73311 36.94904 20.59402 1.000 10.45963 ? 249 CYS A C   1 
ATOM   1920 O  O   . CYS A 1 354 ? 56.83730 37.49738 20.80715 1.000 9.05510  ? 249 CYS A O   1 
ATOM   1921 C  CB  . CYS A 1 354 ? 53.92023 36.81372 22.34715 1.000 6.41552  ? 249 CYS A CB  1 
ATOM   1922 S  SG  . CYS A 1 354 ? 55.00364 36.99047 23.81722 1.000 8.34704  ? 249 CYS A SG  1 
ATOM   1923 N  N   A ARG A 1 355 ? 55.61737 35.81399 19.90435 0.494 7.25650  ? 250 ARG A N   1 
ATOM   1924 N  N   B ARG A 1 355 ? 55.61554 35.79497 19.92791 0.506 7.20718  ? 250 ARG A N   1 
ATOM   1925 C  CA  A ARG A 1 355 ? 56.78178 35.16120 19.31568 0.494 7.55221  ? 250 ARG A CA  1 
ATOM   1926 C  CA  B ARG A 1 355 ? 56.76663 35.14709 19.30287 0.506 7.56929  ? 250 ARG A CA  1 
ATOM   1927 C  C   A ARG A 1 355 ? 57.43268 36.03007 18.23905 0.494 8.68111  ? 250 ARG A C   1 
ATOM   1928 C  C   B ARG A 1 355 ? 57.42567 36.04899 18.25975 0.506 8.68265  ? 250 ARG A C   1 
ATOM   1929 O  O   A ARG A 1 355 ? 58.66263 36.10311 18.15927 0.494 10.55851 ? 250 ARG A O   1 
ATOM   1930 O  O   B ARG A 1 355 ? 58.65400 36.17229 18.23276 0.506 10.54439 ? 250 ARG A O   1 
ATOM   1931 C  CB  A ARG A 1 355 ? 56.35323 33.80325 18.76025 0.494 12.93706 ? 250 ARG A CB  1 
ATOM   1932 C  CB  B ARG A 1 355 ? 56.32369 33.80815 18.69510 0.506 12.89131 ? 250 ARG A CB  1 
ATOM   1933 C  CG  A ARG A 1 355 ? 57.49487 32.98426 18.21571 0.494 19.07761 ? 250 ARG A CG  1 
ATOM   1934 C  CG  B ARG A 1 355 ? 57.41140 33.13770 17.87287 0.506 18.18306 ? 250 ARG A CG  1 
ATOM   1935 C  CD  A ARG A 1 355 ? 58.46882 32.57423 19.31767 0.494 23.93008 ? 250 ARG A CD  1 
ATOM   1936 C  CD  B ARG A 1 355 ? 56.89749 31.99467 16.98693 0.506 17.10667 ? 250 ARG A CD  1 
ATOM   1937 N  NE  A ARG A 1 355 ? 59.74009 33.28300 19.24229 0.494 26.37095 ? 250 ARG A NE  1 
ATOM   1938 N  NE  B ARG A 1 355 ? 56.18666 30.95603 17.71917 0.506 31.13975 ? 250 ARG A NE  1 
ATOM   1939 C  CZ  A ARG A 1 355 ? 60.62113 33.33994 20.22725 0.494 16.04969 ? 250 ARG A CZ  1 
ATOM   1940 C  CZ  B ARG A 1 355 ? 56.73347 29.81177 18.11401 0.506 31.45861 ? 250 ARG A CZ  1 
ATOM   1941 N  NH1 A ARG A 1 355 ? 60.36684 32.80032 21.40899 0.494 31.50286 ? 250 ARG A NH1 1 
ATOM   1942 N  NH1 B ARG A 1 355 ? 58.03823 29.60901 18.05334 0.506 35.71635 ? 250 ARG A NH1 1 
ATOM   1943 N  NH2 A ARG A 1 355 ? 61.79599 33.92698 20.01650 0.494 30.15979 ? 250 ARG A NH2 1 
ATOM   1944 N  NH2 B ARG A 1 355 ? 55.95224 28.85209 18.59724 0.506 38.86644 ? 250 ARG A NH2 1 
ATOM   1945 N  N   . TYR A 1 356 ? 56.62859 36.70511 17.40896 1.000 8.82916  ? 251 TYR A N   1 
ATOM   1946 C  CA  . TYR A 1 356 ? 57.18659 37.61605 16.40565 1.000 9.98573  ? 251 TYR A CA  1 
ATOM   1947 C  C   . TYR A 1 356 ? 57.94562 38.77895 17.04817 1.000 9.09481  ? 251 TYR A C   1 
ATOM   1948 O  O   . TYR A 1 356 ? 59.04057 39.13982 16.59648 1.000 9.26386  ? 251 TYR A O   1 
ATOM   1949 C  CB  . TYR A 1 356 ? 56.06253 38.14801 15.49972 1.000 8.60816  ? 251 TYR A CB  1 
ATOM   1950 C  CG  . TYR A 1 356 ? 56.54941 39.07722 14.41215 1.000 7.59707  ? 251 TYR A CG  1 
ATOM   1951 C  CD1 . TYR A 1 356 ? 56.95999 38.57771 13.19583 1.000 10.06562 ? 251 TYR A CD1 1 
ATOM   1952 C  CD2 . TYR A 1 356 ? 56.62462 40.45256 14.62486 1.000 8.56533  ? 251 TYR A CD2 1 
ATOM   1953 C  CE1 . TYR A 1 356 ? 57.44621 39.40899 12.20868 1.000 14.40843 ? 251 TYR A CE1 1 
ATOM   1954 C  CE2 . TYR A 1 356 ? 57.10652 41.30215 13.66086 1.000 8.78443  ? 251 TYR A CE2 1 
ATOM   1955 C  CZ  . TYR A 1 356 ? 57.50413 40.76973 12.43634 1.000 12.04917 ? 251 TYR A CZ  1 
ATOM   1956 O  OH  . TYR A 1 356 ? 57.99562 41.58428 11.42151 1.000 14.54263 ? 251 TYR A OH  1 
ATOM   1957 N  N   . ILE A 1 357 ? 57.37517 39.37559 18.10275 1.000 6.90085  ? 252 ILE A N   1 
ATOM   1958 C  CA  . ILE A 1 357 ? 58.05405 40.45242 18.82414 1.000 6.39804  ? 252 ILE A CA  1 
ATOM   1959 C  C   . ILE A 1 357 ? 59.38298 39.96499 19.40948 1.000 8.10420  ? 252 ILE A C   1 
ATOM   1960 O  O   . ILE A 1 357 ? 60.41512 40.65394 19.29334 1.000 8.89532  ? 252 ILE A O   1 
ATOM   1961 C  CB  . ILE A 1 357 ? 57.10454 41.03238 19.88667 1.000 7.40280  ? 252 ILE A CB  1 
ATOM   1962 C  CG1 . ILE A 1 357 ? 56.00264 41.80744 19.16298 1.000 8.33693  ? 252 ILE A CG1 1 
ATOM   1963 C  CG2 . ILE A 1 357 ? 57.85536 41.92680 20.86004 1.000 8.38043  ? 252 ILE A CG2 1 
ATOM   1964 C  CD1 . ILE A 1 357 ? 54.83323 42.24225 20.05966 1.000 9.98987  ? 252 ILE A CD1 1 
ATOM   1965 N  N   . ALA A 1 358 ? 59.40388 38.74063 19.97961 1.000 7.07391  ? 253 ALA A N   1 
ATOM   1966 C  CA  . ALA A 1 358 ? 60.65259 38.18096 20.50798 1.000 8.38428  ? 253 ALA A CA  1 
ATOM   1967 C  C   . ALA A 1 358 ? 61.67244 37.91781 19.39359 1.000 11.56848 ? 253 ALA A C   1 
ATOM   1968 O  O   . ALA A 1 358 ? 62.87444 38.19516 19.57009 1.000 12.11334 ? 253 ALA A O   1 
ATOM   1969 C  CB  . ALA A 1 358 ? 60.36128 36.89324 21.30258 1.000 10.74102 ? 253 ALA A CB  1 
ATOM   1970 N  N   . ASP A 1 359 ? 61.21956 37.39614 18.23736 1.000 7.85995  ? 254 ASP A N   1 
ATOM   1971 C  CA  . ASP A 1 359 ? 62.13306 37.04837 17.14189 1.000 9.69656  ? 254 ASP A CA  1 
ATOM   1972 C  C   . ASP A 1 359 ? 62.80106 38.28091 16.56529 1.000 10.11928 ? 254 ASP A C   1 
ATOM   1973 O  O   . ASP A 1 359 ? 63.91791 38.18165 16.00385 1.000 13.88473 ? 254 ASP A O   1 
ATOM   1974 C  CB  . ASP A 1 359 ? 61.37594 36.37960 16.01027 1.000 12.55820 ? 254 ASP A CB  1 
ATOM   1975 C  CG  . ASP A 1 359 ? 61.06940 34.90598 16.26423 1.000 21.29134 ? 254 ASP A CG  1 
ATOM   1976 O  OD1 . ASP A 1 359 ? 61.60756 34.30949 17.21455 1.000 24.36726 ? 254 ASP A OD1 1 
ATOM   1977 O  OD2 . ASP A 1 359 ? 60.26265 34.38787 15.48705 1.000 24.99943 ? 254 ASP A OD2 1 
ATOM   1978 N  N   . THR A 1 360 ? 62.09324 39.41349 16.58842 1.000 9.61167  ? 255 THR A N   1 
ATOM   1979 C  CA  . THR A 1 360 ? 62.55435 40.63805 15.92906 1.000 10.05867 ? 255 THR A CA  1 
ATOM   1980 C  C   . THR A 1 360 ? 63.06255 41.67128 16.93235 1.000 9.28217  ? 255 THR A C   1 
ATOM   1981 O  O   . THR A 1 360 ? 63.34957 42.81807 16.54410 1.000 10.76714 ? 255 THR A O   1 
ATOM   1982 C  CB  . THR A 1 360 ? 61.43220 41.25056 15.05699 1.000 11.36441 ? 255 THR A CB  1 
ATOM   1983 O  OG1 . THR A 1 360 ? 60.27667 41.56233 15.86278 1.000 9.28889  ? 255 THR A OG1 1 
ATOM   1984 C  CG2 . THR A 1 360 ? 60.98940 40.29909 13.96333 1.000 13.20823 ? 255 THR A CG2 1 
ATOM   1985 N  N   . ALA A 1 361 ? 63.17219 41.29675 18.20493 1.000 8.56861  ? 256 ALA A N   1 
ATOM   1986 C  CA  . ALA A 1 361 ? 63.64007 42.18870 19.26770 1.000 7.64027  ? 256 ALA A CA  1 
ATOM   1987 C  C   . ALA A 1 361 ? 65.11695 42.55146 19.11350 1.000 10.86169 ? 256 ALA A C   1 
ATOM   1988 O  O   . ALA A 1 361 ? 65.89236 41.84593 18.46055 1.000 12.47078 ? 256 ALA A O   1 
ATOM   1989 C  CB  . ALA A 1 361 ? 63.45282 41.48663 20.60184 1.000 9.27662  ? 256 ALA A CB  1 
ATOM   1990 N  N   . ASN A 1 362 ? 65.51904 43.61161 19.82415 1.000 8.05105  ? 257 ASN A N   1 
ATOM   1991 C  CA  . ASN A 1 362 ? 66.94577 43.86215 20.02705 1.000 9.14153  ? 257 ASN A CA  1 
ATOM   1992 C  C   . ASN A 1 362 ? 67.46717 42.85805 21.03685 1.000 10.99145 ? 257 ASN A C   1 
ATOM   1993 O  O   . ASN A 1 362 ? 66.89078 42.71166 22.12172 1.000 12.09092 ? 257 ASN A O   1 
ATOM   1994 C  CB  . ASN A 1 362 ? 67.18263 45.28344 20.52614 1.000 11.18423 ? 257 ASN A CB  1 
ATOM   1995 C  CG  . ASN A 1 362 ? 67.12487 46.31336 19.41073 1.000 13.64719 ? 257 ASN A CG  1 
ATOM   1996 O  OD1 . ASN A 1 362 ? 67.76769 46.14395 18.36203 1.000 15.52665 ? 257 ASN A OD1 1 
ATOM   1997 N  ND2 . ASN A 1 362 ? 66.31851 47.36129 19.60643 1.000 14.33237 ? 257 ASN A ND2 1 
ATOM   1998 N  N   . LYS A 1 363 ? 68.53530 42.13761 20.67021 1.000 9.99426  ? 258 LYS A N   1 
ATOM   1999 C  CA  . LYS A 1 363 ? 68.98258 40.97896 21.44431 1.000 11.24845 ? 258 LYS A CA  1 
ATOM   2000 C  C   . LYS A 1 363 ? 70.30147 41.29881 22.14216 1.000 12.77171 ? 258 LYS A C   1 
ATOM   2001 O  O   . LYS A 1 363 ? 71.23769 41.79553 21.50931 1.000 16.88302 ? 258 LYS A O   1 
ATOM   2002 C  CB  . LYS A 1 363 ? 69.16809 39.75464 20.52641 1.000 14.72398 ? 258 LYS A CB  1 
ATOM   2003 C  CG  . LYS A 1 363 ? 67.90767 39.03975 20.13831 1.000 30.70714 ? 258 LYS A CG  1 
ATOM   2004 C  CD  . LYS A 1 363 ? 67.89296 38.51297 18.70131 1.000 43.64912 ? 258 LYS A CD  1 
ATOM   2005 C  CE  . LYS A 1 363 ? 66.47153 38.42584 18.11866 1.000 36.52909 ? 258 LYS A CE  1 
ATOM   2006 N  NZ  . LYS A 1 363 ? 66.29833 39.41724 17.00257 1.000 28.82221 ? 258 LYS A NZ  1 
ATOM   2007 N  N   . GLY A 1 364 ? 70.38229 40.99457 23.43720 1.000 11.49758 ? 259 GLY A N   1 
ATOM   2008 C  CA  . GLY A 1 364 ? 71.63986 41.08257 24.17386 1.000 11.70919 ? 259 GLY A CA  1 
ATOM   2009 C  C   . GLY A 1 364 ? 72.03979 42.46468 24.64851 1.000 16.42547 ? 259 GLY A C   1 
ATOM   2010 O  O   . GLY A 1 364 ? 73.16466 42.62846 25.14068 1.000 19.10939 ? 259 GLY A O   1 
ATOM   2011 N  N   . ASP A 1 365 ? 71.16265 43.46433 24.54197 1.000 13.25617 ? 260 ASP A N   1 
ATOM   2012 C  CA  . ASP A 1 365 ? 71.52892 44.84552 24.84523 1.000 13.96337 ? 260 ASP A CA  1 
ATOM   2013 C  C   . ASP A 1 365 ? 71.27223 45.24263 26.29666 1.000 13.91284 ? 260 ASP A C   1 
ATOM   2014 O  O   . ASP A 1 365 ? 71.77302 46.29108 26.73875 1.000 16.71258 ? 260 ASP A O   1 
ATOM   2015 C  CB  . ASP A 1 365 ? 70.78516 45.78793 23.89108 1.000 15.50953 ? 260 ASP A CB  1 
ATOM   2016 C  CG  . ASP A 1 365 ? 71.25080 45.62668 22.43601 1.000 26.82055 ? 260 ASP A CG  1 
ATOM   2017 O  OD1 . ASP A 1 365 ? 72.45061 45.35668 22.21612 1.000 30.22826 ? 260 ASP A OD1 1 
ATOM   2018 O  OD2 . ASP A 1 365 ? 70.41674 45.72229 21.51448 1.000 31.05030 ? 260 ASP A OD2 1 
ATOM   2019 N  N   . LEU A 1 366 ? 70.53991 44.43739 27.06438 1.000 10.68666 ? 261 LEU A N   1 
ATOM   2020 C  CA  . LEU A 1 366 ? 70.17506 44.83673 28.42065 1.000 10.92396 ? 261 LEU A CA  1 
ATOM   2021 C  C   . LEU A 1 366 ? 71.20908 44.32799 29.42535 1.000 13.56521 ? 261 LEU A C   1 
ATOM   2022 O  O   . LEU A 1 366 ? 71.84152 43.27783 29.22801 1.000 14.12700 ? 261 LEU A O   1 
ATOM   2023 C  CB  . LEU A 1 366 ? 68.79857 44.27447 28.77609 1.000 9.45653  ? 261 LEU A CB  1 
ATOM   2024 C  CG  . LEU A 1 366 ? 67.65500 44.81489 27.95280 1.000 9.45701  ? 261 LEU A CG  1 
ATOM   2025 C  CD1 . LEU A 1 366 ? 66.41632 43.98746 28.35873 1.000 15.05576 ? 261 LEU A CD1 1 
ATOM   2026 C  CD2 . LEU A 1 366 ? 67.47823 46.30891 28.28656 1.000 15.21643 ? 261 LEU A CD2 1 
ATOM   2027 N  N   A SER A 1 367 ? 71.42729 45.09718 30.48433 0.525 10.13031 ? 262 SER A N   1 
ATOM   2028 N  N   B SER A 1 367 ? 71.37723 45.09215 30.50216 0.475 10.18192 ? 262 SER A N   1 
ATOM   2029 C  CA  A SER A 1 367 ? 72.30520 44.65876 31.56015 0.525 11.55296 ? 262 SER A CA  1 
ATOM   2030 C  CA  B SER A 1 367 ? 72.22981 44.74725 31.63152 0.475 11.59484 ? 262 SER A CA  1 
ATOM   2031 C  C   A SER A 1 367 ? 71.47477 44.28732 32.78095 0.525 10.50357 ? 262 SER A C   1 
ATOM   2032 C  C   B SER A 1 367 ? 71.37843 44.32124 32.82364 0.475 10.67215 ? 262 SER A C   1 
ATOM   2033 O  O   A SER A 1 367 ? 70.29226 44.64500 32.88462 0.525 13.12240 ? 262 SER A O   1 
ATOM   2034 O  O   B SER A 1 367 ? 70.16355 44.55954 32.87090 0.475 12.60215 ? 262 SER A O   1 
ATOM   2035 C  CB  A SER A 1 367 ? 73.32651 45.73808 31.93665 0.525 14.57374 ? 262 SER A CB  1 
ATOM   2036 C  CB  B SER A 1 367 ? 73.13004 45.92819 32.02177 0.475 15.01570 ? 262 SER A CB  1 
ATOM   2037 O  OG  A SER A 1 367 ? 72.67985 46.85154 32.51860 0.525 13.92591 ? 262 SER A OG  1 
ATOM   2038 O  OG  B SER A 1 367 ? 74.10668 46.17412 31.02708 0.475 21.45020 ? 262 SER A OG  1 
ATOM   2039 N  N   A ASN A 1 368 ? 72.11666 43.54424 33.69438 0.525 11.53669 ? 263 ASN A N   1 
ATOM   2040 N  N   B ASN A 1 368 ? 72.05627 43.69933 33.79461 0.475 12.05625 ? 263 ASN A N   1 
ATOM   2041 C  CA  A ASN A 1 368 ? 71.52927 43.10252 34.96797 0.525 11.99473 ? 263 ASN A CA  1 
ATOM   2042 C  CA  B ASN A 1 368 ? 71.45510 43.09176 34.99682 0.475 11.93021 ? 263 ASN A CA  1 
ATOM   2043 C  C   A ASN A 1 368 ? 70.40053 42.08072 34.77813 0.525 11.49911 ? 263 ASN A C   1 
ATOM   2044 C  C   B ASN A 1 368 ? 70.26858 42.19614 34.64807 0.475 11.46032 ? 263 ASN A C   1 
ATOM   2045 O  O   A ASN A 1 368 ? 69.48923 41.98496 35.60231 0.525 11.36405 ? 263 ASN A O   1 
ATOM   2046 O  O   B ASN A 1 368 ? 69.16995 42.31463 35.20376 0.475 9.56868  ? 263 ASN A O   1 
ATOM   2047 C  CB  A ASN A 1 368 ? 71.08207 44.30588 35.80952 0.525 17.26516 ? 263 ASN A CB  1 
ATOM   2048 C  CB  B ASN A 1 368 ? 71.05142 44.13510 36.03727 0.475 17.03187 ? 263 ASN A CB  1 
ATOM   2049 C  CG  A ASN A 1 368 ? 72.21604 45.32413 36.00303 0.525 17.57618 ? 263 ASN A CG  1 
ATOM   2050 C  CG  B ASN A 1 368 ? 70.94368 43.53958 37.45092 0.475 15.63912 ? 263 ASN A CG  1 
ATOM   2051 O  OD1 A ASN A 1 368 ? 73.38415 44.99092 35.82517 0.525 16.40374 ? 263 ASN A OD1 1 
ATOM   2052 O  OD1 B ASN A 1 368 ? 71.67103 42.59247 37.81132 0.475 22.60671 ? 263 ASN A OD1 1 
ATOM   2053 N  ND2 A ASN A 1 368 ? 71.87093 46.56796 36.36399 0.525 15.05099 ? 263 ASN A ND2 1 
ATOM   2054 N  ND2 B ASN A 1 368 ? 70.05144 44.09783 38.25649 0.475 21.25789 ? 263 ASN A ND2 1 
ATOM   2055 N  N   . ILE A 1 369 ? 70.50789 41.27573 33.72789 1.000 13.44311 ? 264 ILE A N   1 
ATOM   2056 C  CA  . ILE A 1 369 ? 69.56006 40.21165 33.40139 1.000 10.80523 ? 264 ILE A CA  1 
ATOM   2057 C  C   . ILE A 1 369 ? 70.09937 38.90294 33.98247 1.000 12.70048 ? 264 ILE A C   1 
ATOM   2058 O  O   . ILE A 1 369 ? 71.21053 38.48715 33.61996 1.000 14.85492 ? 264 ILE A O   1 
ATOM   2059 C  CB  . ILE A 1 369 ? 69.37089 40.10416 31.87860 1.000 15.16702 ? 264 ILE A CB  1 
ATOM   2060 C  CG1 . ILE A 1 369 ? 68.85470 41.43382 31.30266 1.000 17.27254 ? 264 ILE A CG1 1 
ATOM   2061 C  CG2 . ILE A 1 369 ? 68.42920 38.92212 31.53921 1.000 16.71701 ? 264 ILE A CG2 1 
ATOM   2062 C  CD1 . ILE A 1 369 ? 67.44992 41.72361 31.72846 1.000 19.06794 ? 264 ILE A CD1 1 
ATOM   2063 N  N   . PRO A 1 370 ? 69.40708 38.26544 34.92798 1.000 13.50305 ? 265 PRO A N   1 
ATOM   2064 C  CA  . PRO A 1 370 ? 69.91900 37.01374 35.51665 1.000 11.57812 ? 265 PRO A CA  1 
ATOM   2065 C  C   . PRO A 1 370 ? 69.96970 35.89684 34.49678 1.000 17.24361 ? 265 PRO A C   1 
ATOM   2066 O  O   . PRO A 1 370 ? 69.16929 35.85189 33.56260 1.000 14.33234 ? 265 PRO A O   1 
ATOM   2067 C  CB  . PRO A 1 370 ? 68.89797 36.69067 36.61373 1.000 19.47812 ? 265 PRO A CB  1 
ATOM   2068 C  CG  . PRO A 1 370 ? 68.11324 37.92265 36.81121 1.000 19.99261 ? 265 PRO A CG  1 
ATOM   2069 C  CD  . PRO A 1 370 ? 68.11408 38.65373 35.51229 1.000 13.46243 ? 265 PRO A CD  1 
ATOM   2070 N  N   . PHE A 1 371 ? 70.92746 34.97739 34.68960 1.000 16.26173 ? 266 PHE A N   1 
ATOM   2071 C  CA  . PHE A 1 371 ? 70.99709 33.79564 33.84435 1.000 15.21777 ? 266 PHE A CA  1 
ATOM   2072 C  C   . PHE A 1 371 ? 69.66597 33.05756 33.82907 1.000 14.94792 ? 266 PHE A C   1 
ATOM   2073 O  O   . PHE A 1 371 ? 69.05391 32.83285 34.87128 1.000 19.37505 ? 266 PHE A O   1 
ATOM   2074 C  CB  . PHE A 1 371 ? 72.14575 32.86636 34.28926 1.000 17.16457 ? 266 PHE A CB  1 
ATOM   2075 C  CG  . PHE A 1 371 ? 72.53900 31.87477 33.22656 1.000 20.40023 ? 266 PHE A CG  1 
ATOM   2076 C  CD1 . PHE A 1 371 ? 73.42162 32.21233 32.20790 1.000 31.00679 ? 266 PHE A CD1 1 
ATOM   2077 C  CD2 . PHE A 1 371 ? 72.00159 30.59260 33.27141 1.000 23.35928 ? 266 PHE A CD2 1 
ATOM   2078 C  CE1 . PHE A 1 371 ? 73.73685 31.28669 31.22202 1.000 28.40075 ? 266 PHE A CE1 1 
ATOM   2079 C  CE2 . PHE A 1 371 ? 72.30248 29.64392 32.30240 1.000 18.15586 ? 266 PHE A CE2 1 
ATOM   2080 C  CZ  . PHE A 1 371 ? 73.16720 29.98819 31.27754 1.000 32.61499 ? 266 PHE A CZ  1 
ATOM   2081 N  N   . GLY A 1 372 ? 69.20440 32.71441 32.62411 1.000 16.30639 ? 267 GLY A N   1 
ATOM   2082 C  CA  . GLY A 1 372 ? 67.95005 32.01723 32.47295 1.000 16.95894 ? 267 GLY A CA  1 
ATOM   2083 C  C   . GLY A 1 372 ? 66.78094 32.91004 32.10208 1.000 13.11876 ? 267 GLY A C   1 
ATOM   2084 O  O   . GLY A 1 372 ? 65.68810 32.39413 31.78458 1.000 17.63707 ? 267 GLY A O   1 
ATOM   2085 N  N   . THR A 1 373 ? 66.96610 34.22684 32.14602 1.000 9.83743  ? 268 THR A N   1 
ATOM   2086 C  CA  . THR A 1 373 ? 65.95309 35.16660 31.66503 1.000 9.08700  ? 268 THR A CA  1 
ATOM   2087 C  C   . THR A 1 373 ? 66.35397 35.68468 30.27615 1.000 9.55443  ? 268 THR A C   1 
ATOM   2088 O  O   . THR A 1 373 ? 67.54729 35.89015 30.00076 1.000 11.97155 ? 268 THR A O   1 
ATOM   2089 C  CB  . THR A 1 373 ? 65.84241 36.32565 32.66719 1.000 11.26951 ? 268 THR A CB  1 
ATOM   2090 O  OG1 . THR A 1 373 ? 65.42533 35.83090 33.94588 1.000 13.11982 ? 268 THR A OG1 1 
ATOM   2091 C  CG2 . THR A 1 373 ? 64.87112 37.41253 32.18693 1.000 10.29679 ? 268 THR A CG2 1 
ATOM   2092 N  N   . VAL A 1 374 ? 65.36175 35.85521 29.38991 1.000 10.01907 ? 269 VAL A N   1 
ATOM   2093 C  CA  . VAL A 1 374 ? 65.68061 36.35747 28.04787 1.000 10.17440 ? 269 VAL A CA  1 
ATOM   2094 C  C   . VAL A 1 374 ? 66.25182 37.77002 28.10426 1.000 10.05370 ? 269 VAL A C   1 
ATOM   2095 O  O   . VAL A 1 374 ? 65.91030 38.58237 28.98026 1.000 13.10887 ? 269 VAL A O   1 
ATOM   2096 C  CB  . VAL A 1 374 ? 64.46077 36.32912 27.11180 1.000 13.01399 ? 269 VAL A CB  1 
ATOM   2097 C  CG1 . VAL A 1 374 ? 64.02954 34.89126 26.86379 1.000 16.95653 ? 269 VAL A CG1 1 
ATOM   2098 C  CG2 . VAL A 1 374 ? 63.32719 37.18156 27.64209 1.000 11.28906 ? 269 VAL A CG2 1 
ATOM   2099 N  N   . ASN A 1 375 ? 67.14483 38.05917 27.16457 1.000 8.83488  ? 270 ASN A N   1 
ATOM   2100 C  CA  . ASN A 1 375 ? 67.69312 39.41094 27.00353 1.000 8.65437  ? 270 ASN A CA  1 
ATOM   2101 C  C   . ASN A 1 375 ? 67.19158 39.93888 25.66689 1.000 9.73470  ? 270 ASN A C   1 
ATOM   2102 O  O   . ASN A 1 375 ? 67.90581 39.92984 24.66557 1.000 10.59992 ? 270 ASN A O   1 
ATOM   2103 C  CB  . ASN A 1 375 ? 69.25189 39.36776 27.07739 1.000 9.91349  ? 270 ASN A CB  1 
ATOM   2104 C  CG  . ASN A 1 375 ? 69.86013 40.73144 27.25182 1.000 13.26529 ? 270 ASN A CG  1 
ATOM   2105 O  OD1 . ASN A 1 375 ? 69.34031 41.71582 26.73496 1.000 12.55135 ? 270 ASN A OD1 1 
ATOM   2106 N  ND2 . ASN A 1 375 ? 70.98638 40.79885 27.96110 1.000 14.49762 ? 270 ASN A ND2 1 
ATOM   2107 N  N   . LEU A 1 376 ? 65.93032 40.39021 25.66003 1.000 8.46170  ? 271 LEU A N   1 
ATOM   2108 C  CA  . LEU A 1 376 ? 65.20536 40.80362 24.45853 1.000 7.97305  ? 271 LEU A CA  1 
ATOM   2109 C  C   . LEU A 1 376 ? 64.41942 42.06110 24.77376 1.000 9.91429  ? 271 LEU A C   1 
ATOM   2110 O  O   . LEU A 1 376 ? 63.65962 42.07794 25.74733 1.000 8.70324  ? 271 LEU A O   1 
ATOM   2111 C  CB  . LEU A 1 376 ? 64.22476 39.73896 23.99660 1.000 7.92308  ? 271 LEU A CB  1 
ATOM   2112 C  CG  . LEU A 1 376 ? 64.82625 38.35932 23.69065 1.000 9.43027  ? 271 LEU A CG  1 
ATOM   2113 C  CD1 . LEU A 1 376 ? 63.67522 37.35399 23.49967 1.000 11.29431 ? 271 LEU A CD1 1 
ATOM   2114 C  CD2 . LEU A 1 376 ? 65.62253 38.44608 22.43003 1.000 13.19568 ? 271 LEU A CD2 1 
ATOM   2115 N  N   . LEU A 1 377 ? 64.58845 43.08907 23.95122 1.000 7.21262  ? 272 LEU A N   1 
ATOM   2116 C  CA  . LEU A 1 377 ? 63.96253 44.40232 24.13917 1.000 6.75109  ? 272 LEU A CA  1 
ATOM   2117 C  C   . LEU A 1 377 ? 63.08282 44.67779 22.92217 1.000 7.47684  ? 272 LEU A C   1 
ATOM   2118 O  O   . LEU A 1 377 ? 63.56746 44.60206 21.79477 1.000 9.24599  ? 272 LEU A O   1 
ATOM   2119 C  CB  . LEU A 1 377 ? 65.04767 45.48347 24.30229 1.000 8.21556  ? 272 LEU A CB  1 
ATOM   2120 C  CG  . LEU A 1 377 ? 64.55800 46.92927 24.54522 1.000 9.77180  ? 272 LEU A CG  1 
ATOM   2121 C  CD1 . LEU A 1 377 ? 63.73799 47.00056 25.83595 1.000 11.82465 ? 272 LEU A CD1 1 
ATOM   2122 C  CD2 . LEU A 1 377 ? 65.77879 47.88675 24.60136 1.000 12.25617 ? 272 LEU A CD2 1 
ATOM   2123 N  N   . ALA A 1 378 ? 61.79544 44.98028 23.15641 1.000 6.14924  ? 273 ALA A N   1 
ATOM   2124 C  CA  . ALA A 1 378 ? 60.82631 45.19601 22.08074 1.000 8.15394  ? 273 ALA A CA  1 
ATOM   2125 C  C   . ALA A 1 378 ? 61.34028 46.24628 21.09100 1.000 8.10398  ? 273 ALA A C   1 
ATOM   2126 O  O   . ALA A 1 378 ? 61.83336 47.30200 21.49658 1.000 9.64697  ? 273 ALA A O   1 
ATOM   2127 C  CB  . ALA A 1 378 ? 59.50220 45.68437 22.69690 1.000 8.83112  ? 273 ALA A CB  1 
ATOM   2128 N  N   . TYR A 1 379 ? 61.15024 45.98057 19.79113 1.000 7.22833  ? 274 TYR A N   1 
ATOM   2129 C  CA  . TYR A 1 379 ? 61.71169 46.80642 18.72234 1.000 6.99039  ? 274 TYR A CA  1 
ATOM   2130 C  C   . TYR A 1 379 ? 60.77988 46.75185 17.51231 1.000 10.56334 ? 274 TYR A C   1 
ATOM   2131 O  O   . TYR A 1 379 ? 60.33911 45.66399 17.12297 1.000 11.09455 ? 274 TYR A O   1 
ATOM   2132 C  CB  . TYR A 1 379 ? 63.11279 46.28573 18.35722 1.000 7.45640  ? 274 TYR A CB  1 
ATOM   2133 C  CG  . TYR A 1 379 ? 63.79761 47.00277 17.19415 1.000 7.95273  ? 274 TYR A CG  1 
ATOM   2134 C  CD1 . TYR A 1 379 ? 63.85300 48.38785 17.14959 1.000 10.53260 ? 274 TYR A CD1 1 
ATOM   2135 C  CD2 . TYR A 1 379 ? 64.39395 46.28481 16.16565 1.000 12.80675 ? 274 TYR A CD2 1 
ATOM   2136 C  CE1 . TYR A 1 379 ? 64.49671 49.03085 16.09597 1.000 10.15236 ? 274 TYR A CE1 1 
ATOM   2137 C  CE2 . TYR A 1 379 ? 65.03335 46.91010 15.12760 1.000 14.03820 ? 274 TYR A CE2 1 
ATOM   2138 C  CZ  . TYR A 1 379 ? 65.05676 48.26802 15.07663 1.000 12.98135 ? 274 TYR A CZ  1 
ATOM   2139 O  OH  . TYR A 1 379 ? 65.69341 48.85596 13.97496 1.000 15.02465 ? 274 TYR A OH  1 
ATOM   2140 N  N   . ASN A 1 380 ? 60.48588 47.91168 16.91074 1.000 7.94674  ? 275 ASN A N   1 
ATOM   2141 C  CA  . ASN A 1 380 ? 59.51385 47.91076 15.81043 1.000 7.19300  ? 275 ASN A CA  1 
ATOM   2142 C  C   . ASN A 1 380 ? 60.12988 47.73417 14.42312 1.000 11.53572 ? 275 ASN A C   1 
ATOM   2143 O  O   . ASN A 1 380 ? 59.38536 47.59376 13.46015 1.000 9.92668  ? 275 ASN A O   1 
ATOM   2144 C  CB  . ASN A 1 380 ? 58.62519 49.19613 15.89571 1.000 7.11546  ? 275 ASN A CB  1 
ATOM   2145 C  CG  . ASN A 1 380 ? 59.32484 50.46430 15.43043 1.000 9.86834  ? 275 ASN A CG  1 
ATOM   2146 O  OD1 . ASN A 1 380 ? 60.50522 50.46899 15.07584 1.000 9.69223  ? 275 ASN A OD1 1 
ATOM   2147 N  ND2 . ASN A 1 380 ? 58.55193 51.56472 15.42127 1.000 11.35563 ? 275 ASN A ND2 1 
ATOM   2148 N  N   A ASN A 1 381 ? 61.46505 47.74387 14.28901 0.501 11.68025 ? 276 ASN A N   1 
ATOM   2149 N  N   B ASN A 1 381 ? 61.45652 47.68693 14.30453 0.499 11.60345 ? 276 ASN A N   1 
ATOM   2150 C  CA  A ASN A 1 381 ? 62.15852 47.43883 13.02482 0.501 10.64946 ? 276 ASN A CA  1 
ATOM   2151 C  CA  B ASN A 1 381 ? 62.09997 47.41051 13.01813 0.499 10.66104 ? 276 ASN A CA  1 
ATOM   2152 C  C   A ASN A 1 381 ? 61.83826 48.42379 11.89230 0.501 11.07264 ? 276 ASN A C   1 
ATOM   2153 C  C   B ASN A 1 381 ? 61.56882 48.33609 11.91661 0.499 9.43947  ? 276 ASN A C   1 
ATOM   2154 O  O   A ASN A 1 381 ? 62.00563 48.11024 10.70135 0.501 10.57606 ? 276 ASN A O   1 
ATOM   2155 O  O   B ASN A 1 381 ? 61.26134 47.89100 10.80091 0.499 10.37380 ? 276 ASN A O   1 
ATOM   2156 C  CB  A ASN A 1 381 ? 61.84847 46.00456 12.59172 0.501 13.05598 ? 276 ASN A CB  1 
ATOM   2157 C  CB  B ASN A 1 381 ? 61.88778 45.94685 12.61636 0.499 13.08683 ? 276 ASN A CB  1 
ATOM   2158 C  CG  A ASN A 1 381 ? 62.65076 45.00548 13.37310 0.501 12.29431 ? 276 ASN A CG  1 
ATOM   2159 C  CG  B ASN A 1 381 ? 62.96185 45.43483 11.68747 0.499 16.34709 ? 276 ASN A CG  1 
ATOM   2160 O  OD1 A ASN A 1 381 ? 62.17236 44.43827 14.36209 0.501 17.63272 ? 276 ASN A OD1 1 
ATOM   2161 O  OD1 B ASN A 1 381 ? 63.81413 46.18589 11.23602 0.499 28.15313 ? 276 ASN A OD1 1 
ATOM   2162 N  ND2 A ASN A 1 381 ? 63.88019 44.79654 12.95699 0.501 10.89540 ? 276 ASN A ND2 1 
ATOM   2163 N  ND2 B ASN A 1 381 ? 62.90118 44.14443 11.37198 0.499 30.36574 ? 276 ASN A ND2 1 
ATOM   2164 N  N   . TYR A 1 382 ? 61.42401 49.63316 12.23028 1.000 12.71972 ? 277 TYR A N   1 
ATOM   2165 C  CA  . TYR A 1 382 ? 60.96804 50.57266 11.21802 1.000 12.17221 ? 277 TYR A CA  1 
ATOM   2166 C  C   . TYR A 1 382 ? 62.12894 51.01541 10.33898 1.000 13.96630 ? 277 TYR A C   1 
ATOM   2167 O  O   . TYR A 1 382 ? 63.18930 51.37826 10.83780 1.000 20.39141 ? 277 TYR A O   1 
ATOM   2168 C  CB  . TYR A 1 382 ? 60.30326 51.77470 11.88619 1.000 12.57611 ? 277 TYR A CB  1 
ATOM   2169 C  CG  . TYR A 1 382 ? 59.82934 52.83752 10.88832 1.000 13.55031 ? 277 TYR A CG  1 
ATOM   2170 C  CD1 . TYR A 1 382 ? 58.68167 52.61671 10.12613 1.000 22.18525 ? 277 TYR A CD1 1 
ATOM   2171 C  CD2 . TYR A 1 382 ? 60.55934 53.97717 10.68630 1.000 22.68364 ? 277 TYR A CD2 1 
ATOM   2172 C  CE1 . TYR A 1 382 ? 58.24267 53.55850 9.20539  1.000 23.65439 ? 277 TYR A CE1 1 
ATOM   2173 C  CE2 . TYR A 1 382 ? 60.14289 54.92698 9.76909  1.000 19.80750 ? 277 TYR A CE2 1 
ATOM   2174 C  CZ  . TYR A 1 382 ? 58.97251 54.70509 9.05881  1.000 17.56556 ? 277 TYR A CZ  1 
ATOM   2175 O  OH  . TYR A 1 382 ? 58.58193 55.66559 8.14636  1.000 26.64709 ? 277 TYR A OH  1 
ATOM   2176 N  N   . GLN A 1 383 ? 61.91569 50.95009 9.03313  1.000 14.86803 ? 278 GLN A N   1 
ATOM   2177 C  CA  . GLN A 1 383 ? 62.84873 51.46255 8.03105  1.000 25.94734 ? 278 GLN A CA  1 
ATOM   2178 C  C   . GLN A 1 383 ? 62.05886 52.40627 7.14017  1.000 20.70053 ? 278 GLN A C   1 
ATOM   2179 O  O   . GLN A 1 383 ? 61.08123 51.98384 6.51075  1.000 31.96035 ? 278 GLN A O   1 
ATOM   2180 C  CB  . GLN A 1 383 ? 63.45263 50.32597 7.18778  1.000 41.61378 ? 278 GLN A CB  1 
ATOM   2181 C  CG  . GLN A 1 383 ? 63.86403 49.06273 7.96263  1.000 50.79337 ? 278 GLN A CG  1 
ATOM   2182 C  CD  . GLN A 1 383 ? 65.02134 49.30702 8.92025  1.000 70.85471 ? 278 GLN A CD  1 
ATOM   2183 O  OE1 . GLN A 1 383 ? 65.78624 50.26516 8.75259  1.000 70.36362 ? 278 GLN A OE1 1 
ATOM   2184 N  NE2 . GLN A 1 383 ? 65.14172 48.45521 9.94562  1.000 57.59852 ? 278 GLN A NE2 1 
ATOM   2185 N  N   . ALA A 1 384 ? 62.46100 53.67041 7.09986  1.000 18.86896 ? 279 ALA A N   1 
ATOM   2186 C  CA  . ALA A 1 384 ? 61.80449 54.65002 6.23223  1.000 25.06963 ? 279 ALA A CA  1 
ATOM   2187 C  C   . ALA A 1 384 ? 61.98431 54.25216 4.76313  1.000 31.86464 ? 279 ALA A C   1 
ATOM   2188 O  O   . ALA A 1 384 ? 62.98481 53.64127 4.38597  1.000 31.46634 ? 279 ALA A O   1 
ATOM   2189 C  CB  . ALA A 1 384 ? 62.35457 56.03229 6.48922  1.000 32.98314 ? 279 ALA A CB  1 
ATOM   2190 O  OXT . ALA A 1 384 ? 61.11271 54.47775 3.91797  1.000 37.12708 ? 279 ALA A OXT 1 
HETATM 2191 N  N   . NO3 B 2 .   ? 35.58703 52.09234 43.10912 1.000 31.76339 ? 301 NO3 A N   1 
HETATM 2192 O  O1  . NO3 B 2 .   ? 35.86701 51.98843 41.88249 1.000 21.19669 ? 301 NO3 A O1  1 
HETATM 2193 O  O2  . NO3 B 2 .   ? 36.51719 52.33716 43.93831 1.000 26.33289 ? 301 NO3 A O2  1 
HETATM 2194 O  O3  . NO3 B 2 .   ? 34.37507 51.95819 43.48873 1.000 35.98815 ? 301 NO3 A O3  1 
HETATM 2195 CA CA  . CA  C 3 .   ? 54.77925 33.34462 27.18004 1.000 8.76587  ? 302 CA  A CA  1 
HETATM 2196 O  O   . HOH D 4 .   ? 69.42714 47.82418 21.04812 1.000 28.19321 ? 401 HOH A O   1 
HETATM 2197 O  O   . HOH D 4 .   ? 42.61781 29.00506 41.57854 1.000 27.71964 ? 402 HOH A O   1 
HETATM 2198 O  O   . HOH D 4 .   ? 65.03503 57.48404 34.29345 1.000 27.46276 ? 403 HOH A O   1 
HETATM 2199 O  O   . HOH D 4 .   ? 35.00120 32.25252 34.49733 1.000 26.76316 ? 404 HOH A O   1 
HETATM 2200 O  O   . HOH D 4 .   ? 48.61864 27.06658 29.10456 1.000 25.88401 ? 405 HOH A O   1 
HETATM 2201 O  O   . HOH D 4 .   ? 64.62241 56.30814 18.10088 1.000 26.23725 ? 406 HOH A O   1 
HETATM 2202 O  O   . HOH D 4 .   ? 45.87399 47.18200 32.41796 1.000 8.92586  ? 407 HOH A O   1 
HETATM 2203 O  O   . HOH D 4 .   ? 48.57195 27.51628 36.15808 1.000 35.35002 ? 408 HOH A O   1 
HETATM 2204 O  O   . HOH D 4 .   ? 56.16423 59.46166 39.80566 1.000 26.54265 ? 409 HOH A O   1 
HETATM 2205 O  O   . HOH D 4 .   ? 46.64589 60.12246 16.78580 1.000 27.85739 ? 410 HOH A O   1 
HETATM 2206 O  O   . HOH D 4 .   ? 53.62221 48.61120 38.02805 1.000 23.76519 ? 411 HOH A O   1 
HETATM 2207 O  O   . HOH D 4 .   ? 29.47868 42.54636 25.05438 1.000 28.15488 ? 412 HOH A O   1 
HETATM 2208 O  O   . HOH D 4 .   ? 38.44577 60.56050 35.24813 1.000 27.26508 ? 413 HOH A O   1 
HETATM 2209 O  O   . HOH D 4 .   ? 72.54657 48.87419 25.34585 1.000 18.40624 ? 414 HOH A O   1 
HETATM 2210 O  O   . HOH D 4 .   ? 62.77497 30.89479 36.26435 1.000 21.55935 ? 415 HOH A O   1 
HETATM 2211 O  O   . HOH D 4 .   ? 47.84206 47.88840 30.47996 1.000 10.73538 ? 416 HOH A O   1 
HETATM 2212 O  O   . HOH D 4 .   ? 56.15100 54.93398 6.72676  1.000 35.38225 ? 417 HOH A O   1 
HETATM 2213 O  O   . HOH D 4 .   ? 37.85236 59.17879 23.58928 1.000 17.89067 ? 418 HOH A O   1 
HETATM 2214 O  O   . HOH D 4 .   ? 38.97119 34.61016 29.52325 1.000 20.08857 ? 419 HOH A O   1 
HETATM 2215 O  O   . HOH D 4 .   ? 44.54898 65.77370 18.40044 1.000 36.31824 ? 420 HOH A O   1 
HETATM 2216 O  O   . HOH D 4 .   ? 42.62739 39.20868 16.96902 1.000 13.58938 ? 421 HOH A O   1 
HETATM 2217 O  O   . HOH D 4 .   ? 57.80812 49.22389 11.56589 1.000 19.74519 ? 422 HOH A O   1 
HETATM 2218 O  O   . HOH D 4 .   ? 30.87845 40.03607 33.40456 1.000 24.41714 ? 423 HOH A O   1 
HETATM 2219 O  O   . HOH D 4 .   ? 51.79253 54.92657 15.91821 1.000 12.95099 ? 424 HOH A O   1 
HETATM 2220 O  O   . HOH D 4 .   ? 46.50854 63.53290 15.50842 1.000 29.88542 ? 425 HOH A O   1 
HETATM 2221 O  O   . HOH D 4 .   ? 60.36694 43.32179 18.84066 1.000 9.79430  ? 426 HOH A O   1 
HETATM 2222 O  O   . HOH D 4 .   ? 35.08254 55.39101 39.90944 1.000 17.04014 ? 427 HOH A O   1 
HETATM 2223 O  O   . HOH D 4 .   ? 66.75117 55.23667 22.02144 1.000 13.21674 ? 428 HOH A O   1 
HETATM 2224 O  O   . HOH D 4 .   ? 66.54706 33.84843 35.42025 1.000 23.27579 ? 429 HOH A O   1 
HETATM 2225 O  O   . HOH D 4 .   ? 64.31551 48.39142 21.30892 1.000 14.92346 ? 430 HOH A O   1 
HETATM 2226 O  O   . HOH D 4 .   ? 72.11688 56.39843 20.37508 1.000 28.13299 ? 431 HOH A O   1 
HETATM 2227 O  O   . HOH D 4 .   ? 50.76027 39.65325 36.17361 1.000 14.56373 ? 432 HOH A O   1 
HETATM 2228 O  O   . HOH D 4 .   ? 66.67539 52.78295 37.01084 1.000 26.78966 ? 433 HOH A O   1 
HETATM 2229 O  O   . HOH D 4 .   ? 53.99056 61.55480 8.07851  1.000 29.36321 ? 434 HOH A O   1 
HETATM 2230 O  O   . HOH D 4 .   ? 59.93873 31.85626 35.55231 1.000 26.94002 ? 435 HOH A O   1 
HETATM 2231 O  O   . HOH D 4 .   ? 69.32715 46.74077 37.37919 1.000 29.86017 ? 436 HOH A O   1 
HETATM 2232 O  O   . HOH D 4 .   ? 48.79637 24.77638 39.80435 1.000 26.74600 ? 437 HOH A O   1 
HETATM 2233 O  O   . HOH D 4 .   ? 54.06042 33.84792 29.48881 1.000 9.32930  ? 438 HOH A O   1 
HETATM 2234 O  O   . HOH D 4 .   ? 56.54824 32.45519 28.70157 1.000 12.48769 ? 439 HOH A O   1 
HETATM 2235 O  O   . HOH D 4 .   ? 36.56328 41.63209 16.55461 1.000 31.42348 ? 440 HOH A O   1 
HETATM 2236 O  O   . HOH D 4 .   ? 32.24527 37.98597 32.35672 1.000 11.85097 ? 441 HOH A O   1 
HETATM 2237 O  O   . HOH D 4 .   ? 42.04218 28.52689 19.85338 1.000 31.32748 ? 442 HOH A O   1 
HETATM 2238 O  O   . HOH D 4 .   ? 62.74177 34.59752 30.15066 1.000 9.98044  ? 443 HOH A O   1 
HETATM 2239 O  O   . HOH D 4 .   ? 50.26426 31.05688 23.08889 1.000 25.41312 ? 444 HOH A O   1 
HETATM 2240 O  O   . HOH D 4 .   ? 39.61089 64.82444 30.51698 1.000 19.13191 ? 445 HOH A O   1 
HETATM 2241 O  O   . HOH D 4 .   ? 65.57314 50.17202 27.80819 1.000 10.89386 ? 446 HOH A O   1 
HETATM 2242 O  O   . HOH D 4 .   ? 39.28466 30.57908 35.35517 1.000 14.90132 ? 447 HOH A O   1 
HETATM 2243 O  O   . HOH D 4 .   ? 69.93526 56.87037 27.64321 1.000 33.39510 ? 448 HOH A O   1 
HETATM 2244 O  O   . HOH D 4 .   ? 73.20524 49.07355 30.65715 1.000 29.22506 ? 449 HOH A O   1 
HETATM 2245 O  O   . HOH D 4 .   ? 29.08139 39.72318 25.26090 1.000 27.85866 ? 450 HOH A O   1 
HETATM 2246 O  O   . HOH D 4 .   ? 58.86980 44.07802 12.31699 1.000 21.10915 ? 451 HOH A O   1 
HETATM 2247 O  O   . HOH D 4 .   ? 34.04706 34.45294 27.18750 0.50  12.70337 ? 452 HOH A O   1 
HETATM 2248 O  O   . HOH D 4 .   ? 54.01682 36.04600 12.96480 1.000 28.00957 ? 453 HOH A O   1 
HETATM 2249 O  O   . HOH D 4 .   ? 54.09568 56.60147 27.19447 1.000 9.93396  ? 454 HOH A O   1 
HETATM 2250 O  O   . HOH D 4 .   ? 69.80404 42.44411 18.19338 1.000 26.93050 ? 455 HOH A O   1 
HETATM 2251 O  O   . HOH D 4 .   ? 50.27520 36.86405 23.49966 1.000 13.89900 ? 456 HOH A O   1 
HETATM 2252 O  O   . HOH D 4 .   ? 73.51973 47.49698 28.62584 1.000 28.93065 ? 457 HOH A O   1 
HETATM 2253 O  O   . HOH D 4 .   ? 67.49764 49.90911 36.82823 1.000 22.78399 ? 458 HOH A O   1 
HETATM 2254 O  O   . HOH D 4 .   ? 35.58861 57.10502 32.12478 1.000 32.78308 ? 459 HOH A O   1 
HETATM 2255 O  O   . HOH D 4 .   ? 46.11939 29.88244 25.57134 1.000 16.61487 ? 460 HOH A O   1 
HETATM 2256 O  O   . HOH D 4 .   ? 55.89349 51.12485 16.54698 1.000 12.80620 ? 461 HOH A O   1 
HETATM 2257 O  O   . HOH D 4 .   ? 59.24940 34.39034 43.24730 1.000 22.28516 ? 462 HOH A O   1 
HETATM 2258 O  O   . HOH D 4 .   ? 49.70580 28.10064 34.06950 1.000 30.10279 ? 463 HOH A O   1 
HETATM 2259 O  O   . HOH D 4 .   ? 60.72810 35.04795 24.35406 1.000 14.95442 ? 464 HOH A O   1 
HETATM 2260 O  O   . HOH D 4 .   ? 46.37469 27.64689 32.39561 1.000 25.28645 ? 465 HOH A O   1 
HETATM 2261 O  O   . HOH D 4 .   ? 50.38547 50.08803 12.17180 1.000 11.60727 ? 466 HOH A O   1 
HETATM 2262 O  O   . HOH D 4 .   ? 51.70245 34.47403 23.67084 1.000 16.99613 ? 467 HOH A O   1 
HETATM 2263 O  O   . HOH D 4 .   ? 67.42274 55.37422 26.02779 1.000 19.36390 ? 468 HOH A O   1 
HETATM 2264 O  O   . HOH D 4 .   ? 68.23867 43.24467 24.54624 1.000 13.57850 ? 469 HOH A O   1 
HETATM 2265 O  O   . HOH D 4 .   ? 50.77373 36.28436 20.76930 1.000 12.19647 ? 470 HOH A O   1 
HETATM 2266 O  O   . HOH D 4 .   ? 58.88652 56.89752 28.03849 1.000 11.65021 ? 471 HOH A O   1 
HETATM 2267 O  O   . HOH D 4 .   ? 50.54262 67.18208 36.26131 1.000 30.60982 ? 472 HOH A O   1 
HETATM 2268 O  O   . HOH D 4 .   ? 59.19809 44.06260 15.08022 1.000 14.13497 ? 473 HOH A O   1 
HETATM 2269 O  O   . HOH D 4 .   ? 54.18666 33.42502 24.87958 1.000 13.79891 ? 474 HOH A O   1 
HETATM 2270 O  O   . HOH D 4 .   ? 63.94370 64.34739 18.58164 1.000 24.08112 ? 475 HOH A O   1 
HETATM 2271 O  O   . HOH D 4 .   ? 64.38376 51.23521 37.60787 1.000 14.45090 ? 476 HOH A O   1 
HETATM 2272 O  O   . HOH D 4 .   ? 59.13901 59.10271 29.68264 1.000 12.84854 ? 477 HOH A O   1 
HETATM 2273 O  O   . HOH D 4 .   ? 65.36474 56.18652 24.45089 1.000 15.19387 ? 478 HOH A O   1 
HETATM 2274 O  O   . HOH D 4 .   ? 36.70515 43.34259 43.07576 1.000 21.58672 ? 479 HOH A O   1 
HETATM 2275 O  O   . HOH D 4 .   ? 53.37453 34.99579 45.35869 1.000 26.79746 ? 480 HOH A O   1 
HETATM 2276 O  O   . HOH D 4 .   ? 60.60648 45.83218 44.25996 1.000 29.48653 ? 481 HOH A O   1 
HETATM 2277 O  O   . HOH D 4 .   ? 45.34016 40.15719 12.79380 1.000 31.74890 ? 482 HOH A O   1 
HETATM 2278 O  O   . HOH D 4 .   ? 44.82189 38.26877 14.77933 1.000 21.75264 ? 483 HOH A O   1 
HETATM 2279 O  O   . HOH D 4 .   ? 49.01152 31.63919 20.78009 1.000 34.17960 ? 484 HOH A O   1 
HETATM 2280 O  O   . HOH D 4 .   ? 51.76005 49.88465 38.60472 1.000 34.17135 ? 485 HOH A O   1 
HETATM 2281 O  O   . HOH D 4 .   ? 33.34379 56.08957 27.59562 1.000 20.83944 ? 486 HOH A O   1 
HETATM 2282 O  O   . HOH D 4 .   ? 34.38614 35.09251 38.02776 1.000 31.34906 ? 487 HOH A O   1 
HETATM 2283 O  O   . HOH D 4 .   ? 49.63920 66.35172 26.17457 1.000 27.23284 ? 488 HOH A O   1 
HETATM 2284 O  O   . HOH D 4 .   ? 53.99501 65.70202 33.46147 1.000 32.81979 ? 489 HOH A O   1 
HETATM 2285 O  O   . HOH D 4 .   ? 64.43937 55.28538 32.83723 1.000 14.15873 ? 490 HOH A O   1 
HETATM 2286 O  O   . HOH D 4 .   ? 31.51744 45.75821 43.01744 1.000 20.96274 ? 491 HOH A O   1 
HETATM 2287 O  O   . HOH D 4 .   ? 48.08731 47.22044 38.93602 1.000 23.65935 ? 492 HOH A O   1 
HETATM 2288 O  O   . HOH D 4 .   ? 54.51944 62.39797 14.58273 1.000 28.34960 ? 493 HOH A O   1 
HETATM 2289 O  O   . HOH D 4 .   ? 72.94410 35.58333 36.69217 1.000 32.82670 ? 494 HOH A O   1 
HETATM 2290 O  O   . HOH D 4 .   ? 40.77539 50.30006 32.19694 1.000 12.60224 ? 495 HOH A O   1 
HETATM 2291 O  O   . HOH D 4 .   ? 46.06910 27.15440 35.11708 1.000 22.33993 ? 496 HOH A O   1 
HETATM 2292 O  O   . HOH D 4 .   ? 37.40952 58.66593 34.01681 1.000 21.19048 ? 497 HOH A O   1 
HETATM 2293 O  O   . HOH D 4 .   ? 36.13365 42.60949 13.74105 1.000 25.75326 ? 498 HOH A O   1 
HETATM 2294 O  O   . HOH D 4 .   ? 72.18243 38.46172 29.24948 1.000 28.96402 ? 499 HOH A O   1 
HETATM 2295 O  O   . HOH D 4 .   ? 62.71173 33.76049 22.87242 1.000 26.58116 ? 500 HOH A O   1 
HETATM 2296 O  O   . HOH D 4 .   ? 56.89494 55.98918 26.54010 1.000 9.55524  ? 501 HOH A O   1 
HETATM 2297 O  O   . HOH D 4 .   ? 56.66161 64.99366 21.21239 1.000 24.62630 ? 502 HOH A O   1 
HETATM 2298 O  O   . HOH D 4 .   ? 42.22141 27.59102 30.09834 1.000 31.41128 ? 503 HOH A O   1 
HETATM 2299 O  O   . HOH D 4 .   ? 51.99045 53.23822 31.06643 1.000 8.09809  ? 504 HOH A O   1 
HETATM 2300 O  O   . HOH D 4 .   ? 68.07553 36.04119 25.20386 1.000 26.19474 ? 505 HOH A O   1 
HETATM 2301 O  O   . HOH D 4 .   ? 74.88258 42.66365 33.05371 1.000 29.59685 ? 506 HOH A O   1 
HETATM 2302 O  O   . HOH D 4 .   ? 55.44864 63.42296 36.76687 1.000 14.04564 ? 507 HOH A O   1 
HETATM 2303 O  O   . HOH D 4 .   ? 59.50515 59.01216 8.42037  1.000 35.70269 ? 508 HOH A O   1 
HETATM 2304 O  O   . HOH D 4 .   ? 38.13572 36.45511 44.30835 1.000 26.74361 ? 509 HOH A O   1 
HETATM 2305 O  O   . HOH D 4 .   ? 56.26013 55.17594 40.14966 1.000 23.32938 ? 510 HOH A O   1 
HETATM 2306 O  O   . HOH D 4 .   ? 55.83853 31.33297 26.00105 1.000 15.20857 ? 511 HOH A O   1 
HETATM 2307 O  O   . HOH D 4 .   ? 27.72335 50.45550 37.36028 1.000 32.62596 ? 512 HOH A O   1 
HETATM 2308 O  O   . HOH D 4 .   ? 51.34189 58.77533 41.17792 1.000 22.46933 ? 513 HOH A O   1 
HETATM 2309 O  O   . HOH D 4 .   ? 33.29186 53.34118 40.97991 1.000 22.06339 ? 514 HOH A O   1 
HETATM 2310 O  O   . HOH D 4 .   ? 59.27832 32.47895 27.90978 1.000 30.23563 ? 515 HOH A O   1 
HETATM 2311 O  O   . HOH D 4 .   ? 52.91596 34.17100 20.38119 1.000 18.03284 ? 516 HOH A O   1 
HETATM 2312 O  O   . HOH D 4 .   ? 53.49012 30.14864 44.54078 1.000 13.72856 ? 517 HOH A O   1 
HETATM 2313 O  O   . HOH D 4 .   ? 29.13728 48.21037 32.71826 1.000 16.51823 ? 518 HOH A O   1 
HETATM 2314 O  O   . HOH D 4 .   ? 61.78376 34.47377 43.63662 1.000 29.24759 ? 519 HOH A O   1 
HETATM 2315 O  O   . HOH D 4 .   ? 45.35612 34.78522 15.43463 1.000 25.66114 ? 520 HOH A O   1 
HETATM 2316 O  O   . HOH D 4 .   ? 72.75541 41.13085 31.49267 1.000 27.16496 ? 521 HOH A O   1 
HETATM 2317 O  O   . HOH D 4 .   ? 61.26254 61.03406 28.52069 1.000 22.96779 ? 522 HOH A O   1 
HETATM 2318 O  O   . HOH D 4 .   ? 48.42783 62.83172 43.10790 1.000 21.58392 ? 523 HOH A O   1 
HETATM 2319 O  O   . HOH D 4 .   ? 35.84305 60.35523 30.78674 1.000 28.30055 ? 524 HOH A O   1 
HETATM 2320 O  O   . HOH D 4 .   ? 46.81090 49.28723 40.16245 1.000 29.12621 ? 525 HOH A O   1 
HETATM 2321 O  O   . HOH D 4 .   ? 25.57741 52.31580 40.68938 1.000 36.14225 ? 526 HOH A O   1 
HETATM 2322 O  O   . HOH D 4 .   ? 47.75681 44.87678 40.54231 1.000 26.25633 ? 527 HOH A O   1 
HETATM 2323 O  O   . HOH D 4 .   ? 56.94010 62.29038 39.02121 1.000 18.74952 ? 528 HOH A O   1 
HETATM 2324 O  O   . HOH D 4 .   ? 42.24534 27.79687 27.00879 1.000 36.91044 ? 529 HOH A O   1 
HETATM 2325 O  O   . HOH D 4 .   ? 52.44783 39.92258 38.77817 1.000 26.92501 ? 530 HOH A O   1 
HETATM 2326 O  O   . HOH D 4 .   ? 56.78138 27.16422 40.30717 1.000 28.92211 ? 531 HOH A O   1 
HETATM 2327 O  O   . HOH D 4 .   ? 30.39122 47.98327 43.18648 1.000 27.24463 ? 532 HOH A O   1 
HETATM 2328 O  O   . HOH D 4 .   ? 26.62623 54.65283 42.19394 1.000 29.34531 ? 533 HOH A O   1 
HETATM 2329 O  O   . HOH D 4 .   ? 74.83448 55.46340 20.11198 1.000 34.16729 ? 534 HOH A O   1 
HETATM 2330 O  O   . HOH D 4 .   ? 32.05762 55.26574 42.99690 1.000 29.75362 ? 535 HOH A O   1 
HETATM 2331 O  O   . HOH D 4 .   ? 46.71186 29.64843 22.94466 1.000 28.90625 ? 536 HOH A O   1 
HETATM 2332 O  O   . HOH D 4 .   ? 75.56127 29.33401 30.30769 1.000 30.11142 ? 537 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   . ALA A 106 ? 0.25955 0.16546 0.15217 -0.03169 0.03009  0.03552  1   ALA A N   
2    C  CA  . ALA A 106 ? 0.25444 0.15715 0.15501 -0.03011 0.02595  0.03813  1   ALA A CA  
3    C  C   . ALA A 106 ? 0.24342 0.14899 0.15720 -0.03134 0.02981  0.03523  1   ALA A C   
4    O  O   . ALA A 106 ? 0.23074 0.14144 0.14876 -0.03213 0.03393  0.03109  1   ALA A O   
5    C  CB  . ALA A 106 ? 0.26153 0.16360 0.16226 -0.02591 0.01824  0.03817  1   ALA A CB  
6    N  N   . ALA A 107 ? 0.23813 0.14068 0.15941 -0.03148 0.02832  0.03712  2   ALA A N   
7    C  CA  . ALA A 107 ? 0.23940 0.14514 0.17383 -0.03291 0.03119  0.03404  2   ALA A CA  
8    C  C   . ALA A 107 ? 0.34242 0.24438 0.28350 -0.03073 0.02582  0.03462  2   ALA A C   
9    O  O   . ALA A 107 ? 0.34505 0.24129 0.28334 -0.03010 0.02295  0.03863  2   ALA A O   
10   C  CB  . ALA A 107 ? 0.26579 0.17274 0.20382 -0.03715 0.03739  0.03487  2   ALA A CB  
11   N  N   . GLN A 108 ? 0.19300 0.10071 0.14451 -0.02870 0.02381  0.02990  3   GLN A N   
12   C  CA  . GLN A 108 ? 0.16170 0.06724 0.12093 -0.02684 0.01954  0.02889  3   GLN A CA  
13   C  C   . GLN A 108 ? 0.17643 0.08412 0.14662 -0.03016 0.02271  0.02650  3   GLN A C   
14   O  O   . GLN A 108 ? 0.16749 0.08374 0.14513 -0.03047 0.02420  0.02230  3   GLN A O   
15   C  CB  . GLN A 108 ? 0.14990 0.06163 0.11272 -0.02225 0.01469  0.02488  3   GLN A CB  
16   C  CG  . GLN A 108 ? 0.15200 0.06221 0.12250 -0.02034 0.01097  0.02283  3   GLN A CG  
17   C  CD  . GLN A 108 ? 0.16762 0.08492 0.14189 -0.01652 0.00733  0.01857  3   GLN A CD  
18   O  OE1 . GLN A 108 ? 0.17679 0.09930 0.14768 -0.01508 0.00699  0.01777  3   GLN A OE1 
19   N  NE2 . GLN A 108 ? 0.16830 0.08557 0.14940 -0.01516 0.00486  0.01562  3   GLN A NE2 
20   N  N   . THR A 109 ? 0.19387 0.09450 0.16596 -0.03247 0.02316  0.02912  4   THR A N   
21   C  CA  . THR A 109 ? 0.21447 0.11798 0.19785 -0.03583 0.02536  0.02660  4   THR A CA  
22   C  C   . THR A 109 ? 0.18057 0.08497 0.17241 -0.03402 0.02129  0.02195  4   THR A C   
23   O  O   . THR A 109 ? 0.21614 0.11773 0.20561 -0.02999 0.01658  0.02151  4   THR A O   
24   C  CB  . THR A 109 ? 0.25899 0.15699 0.24234 -0.03881 0.02666  0.03070  4   THR A CB  
25   O  OG1 . THR A 109 ? 0.34662 0.23653 0.32702 -0.03613 0.02202  0.03337  4   THR A OG1 
26   C  CG2 . THR A 109 ? 0.26419 0.16223 0.23896 -0.04101 0.03124  0.03486  4   THR A CG2 
27   N  N   . ASN A 110 ? 0.22617 0.13657 0.22858 -0.03663 0.02259  0.01805  5   ASN A N   
28   C  CA  . ASN A 110 ? 0.21585 0.12929 0.22624 -0.03527 0.01836  0.01297  5   ASN A CA  
29   C  C   . ASN A 110 ? 0.19512 0.11357 0.20246 -0.03003 0.01421  0.01048  5   ASN A C   
30   O  O   . ASN A 110 ? 0.22457 0.14089 0.23216 -0.02722 0.01023  0.00831  5   ASN A O   
31   C  CB  . ASN A 110 ? 0.24177 0.14657 0.25355 -0.03573 0.01591  0.01335  5   ASN A CB  
32   C  CG  . ASN A 110 ? 0.46603 0.36983 0.48226 -0.04047 0.01828  0.01480  5   ASN A CG  
33   O  OD1 . ASN A 110 ? 0.59709 0.50799 0.62117 -0.04352 0.01991  0.01209  5   ASN A OD1 
34   N  ND2 . ASN A 110 ? 0.61952 0.51480 0.63123 -0.04113 0.01830  0.01936  5   ASN A ND2 
35   N  N   . ALA A 111 ? 0.16493 0.08994 0.16946 -0.02884 0.01559  0.01069  6   ALA A N   
36   C  CA  . ALA A 111 ? 0.13643 0.06622 0.13806 -0.02447 0.01224  0.00882  6   ALA A CA  
37   C  C   . ALA A 111 ? 0.12707 0.06454 0.13660 -0.02399 0.00976  0.00397  6   ALA A C   
38   O  O   . ALA A 111 ? 0.17843 0.11972 0.19563 -0.02701 0.01109  0.00229  6   ALA A O   
39   C  CB  . ALA A 111 ? 0.18008 0.11349 0.17628 -0.02381 0.01471  0.01046  6   ALA A CB  
40   N  N   . PRO A 112 ? 0.12851 0.06898 0.13618 -0.02037 0.00617  0.00190  7   PRO A N   
41   C  CA  . PRO A 112 ? 0.11572 0.06421 0.12878 -0.01992 0.00398  -0.00187 7   PRO A CA  
42   C  C   . PRO A 112 ? 0.12402 0.07934 0.14108 -0.02121 0.00634  -0.00160 7   PRO A C   
43   O  O   . PRO A 112 ? 0.14080 0.09597 0.15411 -0.02089 0.00925  0.00075  7   PRO A O   
44   C  CB  . PRO A 112 ? 0.15342 0.10363 0.16157 -0.01589 0.00111  -0.00268 7   PRO A CB  
45   C  CG  . PRO A 112 ? 0.18242 0.12507 0.18503 -0.01416 0.00079  -0.00047 7   PRO A CG  
46   C  CD  . PRO A 112 ? 0.14740 0.08478 0.14799 -0.01667 0.00411  0.00332  7   PRO A CD  
47   N  N   . TRP A 113 ? 0.09647 0.05787 0.12141 -0.02263 0.00495  -0.00423 8   TRP A N   
48   C  CA  . TRP A 113 ? 0.09050 0.05834 0.12197 -0.02399 0.00742  -0.00400 8   TRP A CA  
49   C  C   . TRP A 113 ? 0.08584 0.05705 0.11393 -0.02111 0.00817  -0.00306 8   TRP A C   
50   O  O   . TRP A 113 ? 0.10047 0.07398 0.13111 -0.02187 0.01205  -0.00215 8   TRP A O   
51   C  CB  . TRP A 113 ? 0.09546 0.07002 0.13657 -0.02553 0.00443  -0.00687 8   TRP A CB  
52   C  CG  . TRP A 113 ? 0.08196 0.06191 0.12250 -0.02280 -0.00008 -0.00845 8   TRP A CG  
53   C  CD1 . TRP A 113 ? 0.11813 0.09754 0.15544 -0.02195 -0.00444 -0.01070 8   TRP A CD1 
54   C  CD2 . TRP A 113 ? 0.08150 0.06787 0.12478 -0.02081 -0.00052 -0.00788 8   TRP A CD2 
55   N  NE1 . TRP A 113 ? 0.09086 0.07596 0.12768 -0.01979 -0.00747 -0.01102 8   TRP A NE1 
56   C  CE2 . TRP A 113 ? 0.09207 0.08114 0.13279 -0.01894 -0.00539 -0.00911 8   TRP A CE2 
57   C  CE3 . TRP A 113 ? 0.07481 0.06446 0.12227 -0.02036 0.00301  -0.00653 8   TRP A CE3 
58   C  CZ2 . TRP A 113 ? 0.08248 0.07691 0.12478 -0.01675 -0.00720 -0.00834 8   TRP A CZ2 
59   C  CZ3 . TRP A 113 ? 0.07743 0.07224 0.12718 -0.01784 0.00129  -0.00633 8   TRP A CZ3 
60   C  CH2 . TRP A 113 ? 0.07145 0.06844 0.11870 -0.01607 -0.00401 -0.00690 8   TRP A CH2 
61   N  N   . GLY A 114 ? 0.09304 0.06458 0.11590 -0.01803 0.00490  -0.00353 9   GLY A N   
62   C  CA  . GLY A 114 ? 0.09123 0.06571 0.11159 -0.01562 0.00531  -0.00286 9   GLY A CA  
63   C  C   . GLY A 114 ? 0.08532 0.05536 0.09870 -0.01536 0.00888  -0.00072 9   GLY A C   
64   O  O   . GLY A 114 ? 0.10427 0.07650 0.11773 -0.01481 0.01132  -0.00051 9   GLY A O   
65   N  N   . LEU A 115 ? 0.09391 0.05738 0.10091 -0.01566 0.00897  0.00081  10  LEU A N   
66   C  CA  . LEU A 115 ? 0.09795 0.05687 0.09724 -0.01589 0.01190  0.00325  10  LEU A CA  
67   C  C   . LEU A 115 ? 0.13048 0.08944 0.13229 -0.01894 0.01724  0.00402  10  LEU A C   
68   O  O   . LEU A 115 ? 0.14901 0.10805 0.14688 -0.01912 0.02065  0.00454  10  LEU A O   
69   C  CB  . LEU A 115 ? 0.12389 0.07560 0.11671 -0.01555 0.01034  0.00537  10  LEU A CB  
70   C  CG  . LEU A 115 ? 0.14225 0.09381 0.13307 -0.01243 0.00575  0.00451  10  LEU A CG  
71   C  CD1 . LEU A 115 ? 0.14887 0.09306 0.13402 -0.01173 0.00455  0.00711  10  LEU A CD1 
72   C  CD2 . LEU A 115 ? 0.15617 0.11167 0.14410 -0.01024 0.00464  0.00397  10  LEU A CD2 
73   N  N   . ALA A 116 ? 0.11751 0.07639 0.12592 -0.02165 0.01836  0.00380  11  ALA A N   
74   C  CA  . ALA A 116 ? 0.10318 0.06323 0.11556 -0.02485 0.02399  0.00436  11  ALA A CA  
75   C  C   . ALA A 116 ? 0.11488 0.08261 0.13393 -0.02394 0.02597  0.00222  11  ALA A C   
76   O  O   . ALA A 116 ? 0.14096 0.10930 0.15920 -0.02508 0.03135  0.00248  11  ALA A O   
77   C  CB  . ALA A 116 ? 0.12105 0.08069 0.14137 -0.02816 0.02434  0.00409  11  ALA A CB  
78   N  N   . ARG A 117 ? 0.09854 0.07186 0.12391 -0.02177 0.02176  0.00013  12  ARG A N   
79   C  CA  . ARG A 117 ? 0.08657 0.06705 0.12025 -0.02065 0.02299  -0.00157 12  ARG A CA  
80   C  C   . ARG A 117 ? 0.12875 0.10805 0.15586 -0.01858 0.02532  -0.00156 12  ARG A C   
81   O  O   . ARG A 117 ? 0.10845 0.09124 0.14077 -0.01853 0.02946  -0.00275 12  ARG A O   
82   C  CB  . ARG A 117 ? 0.09180 0.07764 0.13199 -0.01872 0.01707  -0.00304 12  ARG A CB  
83   C  CG  . ARG A 117 ? 0.09001 0.08341 0.14102 -0.01746 0.01752  -0.00427 12  ARG A CG  
84   C  CD  . ARG A 117 ? 0.12328 0.12123 0.18603 -0.02035 0.02080  -0.00499 12  ARG A CD  
85   N  NE  . ARG A 117 ? 0.08601 0.09108 0.16020 -0.01893 0.02246  -0.00611 12  ARG A NE  
86   C  CZ  . ARG A 117 ? 0.11074 0.11611 0.18607 -0.01854 0.02872  -0.00665 12  ARG A CZ  
87   N  NH1 . ARG A 117 ? 0.11169 0.11054 0.17544 -0.01942 0.03332  -0.00600 12  ARG A NH1 
88   N  NH2 . ARG A 117 ? 0.11566 0.12800 0.20394 -0.01717 0.03030  -0.00800 12  ARG A NH2 
89   N  N   . ILE A 118 ? 0.10302 0.07786 0.11975 -0.01680 0.02262  -0.00067 13  ILE A N   
90   C  CA  . ILE A 118 ? 0.09465 0.06827 0.10516 -0.01520 0.02423  -0.00108 13  ILE A CA  
91   C  C   . ILE A 118 ? 0.11843 0.08777 0.12139 -0.01727 0.02983  -0.00030 13  ILE A C   
92   O  O   . ILE A 118 ? 0.14148 0.10975 0.13911 -0.01643 0.03182  -0.00131 13  ILE A O   
93   C  CB  . ILE A 118 ? 0.13582 0.10701 0.13874 -0.01292 0.01949  -0.00056 13  ILE A CB  
94   C  CG1 . ILE A 118 ? 0.20652 0.17198 0.20100 -0.01362 0.01787  0.00154  13  ILE A CG1 
95   C  CG2 . ILE A 118 ? 0.19911 0.17492 0.20848 -0.01091 0.01467  -0.00144 13  ILE A CG2 
96   C  CD1 . ILE A 118 ? 0.33356 0.29694 0.32020 -0.01154 0.01452  0.00196  13  ILE A CD1 
97   N  N   . SER A 119 ? 0.10764 0.07411 0.10939 -0.02025 0.03257  0.00144  14  SER A N   
98   C  CA  . SER A 119 ? 0.14185 0.10433 0.13573 -0.02276 0.03856  0.00254  14  SER A CA  
99   C  C   . SER A 119 ? 0.17010 0.13620 0.17291 -0.02564 0.04495  0.00176  14  SER A C   
100  O  O   . SER A 119 ? 0.20191 0.16451 0.19876 -0.02873 0.05053  0.00325  14  SER A O   
101  C  CB  . SER A 119 ? 0.16450 0.11924 0.14705 -0.02408 0.03692  0.00616  14  SER A CB  
102  O  OG  . SER A 119 ? 0.17462 0.12792 0.16238 -0.02599 0.03606  0.00782  14  SER A OG  
103  N  N   . SER A 120 ? 0.12026 0.09373 0.13731 -0.02474 0.04447  -0.00053 15  SER A N   
104  C  CA  . SER A 120 ? 0.10903 0.08759 0.13770 -0.02731 0.04981  -0.00150 15  SER A CA  
105  C  C   . SER A 120 ? 0.12665 0.11305 0.16752 -0.02489 0.05108  -0.00472 15  SER A C   
106  O  O   . SER A 120 ? 0.13127 0.11993 0.17489 -0.02148 0.04583  -0.00569 15  SER A O   
107  C  CB  . SER A 120 ? 0.14364 0.12383 0.18088 -0.02928 0.04659  -0.00058 15  SER A CB  
108  O  OG  . SER A 120 ? 0.19085 0.17652 0.24025 -0.03228 0.05201  -0.00151 15  SER A OG  
109  N  N   . THR A 121 ? 0.16317 0.15381 0.21213 -0.02669 0.05820  -0.00621 16  THR A N   
110  C  CA  . THR A 121 ? 0.15323 0.15202 0.21703 -0.02418 0.05919  -0.00916 16  THR A CA  
111  C  C   . THR A 121 ? 0.20626 0.21282 0.28703 -0.02491 0.05614  -0.00930 16  THR A C   
112  O  O   . THR A 121 ? 0.31168 0.32597 0.40710 -0.02297 0.05664  -0.01133 16  THR A O   
113  C  CB  . THR A 121 ? 0.17465 0.17512 0.24031 -0.02507 0.06874  -0.01155 16  THR A CB  
114  O  OG1 . THR A 121 ? 0.21576 0.21646 0.28274 -0.02980 0.07470  -0.01036 16  THR A OG1 
115  C  CG2 . THR A 121 ? 0.19212 0.18529 0.24087 -0.02422 0.07104  -0.01216 16  THR A CG2 
116  N  N   . SER A 122 ? 0.16925 0.17395 0.24901 -0.02768 0.05288  -0.00735 17  SER A N   
117  C  CA  . SER A 122 ? 0.16897 0.18083 0.26413 -0.02895 0.04937  -0.00784 17  SER A CA  
118  C  C   . SER A 122 ? 0.17883 0.18674 0.26837 -0.02943 0.04168  -0.00643 17  SER A C   
119  O  O   . SER A 122 ? 0.15394 0.15341 0.22958 -0.03024 0.04129  -0.00461 17  SER A O   
120  C  CB  . SER A 122 ? 0.20491 0.22009 0.30927 -0.03367 0.05606  -0.00795 17  SER A CB  
121  O  OG  . SER A 122 ? 0.33352 0.34012 0.42511 -0.03717 0.05857  -0.00549 17  SER A OG  
122  N  N   . PRO A 123 ? 0.14544 0.15922 0.24533 -0.02886 0.03536  -0.00735 18  PRO A N   
123  C  CA  . PRO A 123 ? 0.13080 0.14091 0.22550 -0.02972 0.02873  -0.00681 18  PRO A CA  
124  C  C   . PRO A 123 ? 0.12362 0.13098 0.22025 -0.03477 0.03093  -0.00631 18  PRO A C   
125  O  O   . PRO A 123 ? 0.17142 0.18150 0.27584 -0.03797 0.03704  -0.00630 18  PRO A O   
126  C  CB  . PRO A 123 ? 0.16021 0.17828 0.26559 -0.02782 0.02178  -0.00818 18  PRO A CB  
127  C  CG  . PRO A 123 ? 0.19775 0.22475 0.31949 -0.02831 0.02546  -0.00926 18  PRO A CG  
128  C  CD  . PRO A 123 ? 0.22024 0.24439 0.33721 -0.02744 0.03379  -0.00900 18  PRO A CD  
129  N  N   . GLY A 124 ? 0.14078 0.14230 0.23026 -0.03555 0.02626  -0.00597 19  GLY A N   
130  C  CA  . GLY A 124 ? 0.15196 0.15018 0.24413 -0.04025 0.02697  -0.00581 19  GLY A CA  
131  C  C   . GLY A 124 ? 0.22284 0.21100 0.30405 -0.04240 0.03183  -0.00304 19  GLY A C   
132  O  O   . GLY A 124 ? 0.23901 0.22375 0.32188 -0.04613 0.03270  -0.00241 19  GLY A O   
133  N  N   . THR A 125 ? 0.17629 0.15962 0.24538 -0.03988 0.03433  -0.00114 20  THR A N   
134  C  CA  . THR A 125 ? 0.15728 0.13063 0.21454 -0.04169 0.03795  0.00213  20  THR A CA  
135  C  C   . THR A 125 ? 0.16207 0.12760 0.20929 -0.03956 0.03228  0.00296  20  THR A C   
136  O  O   . THR A 125 ? 0.20793 0.17584 0.25520 -0.03636 0.02658  0.00093  20  THR A O   
137  C  CB  . THR A 125 ? 0.22136 0.19328 0.26983 -0.04048 0.04343  0.00370  20  THR A CB  
138  O  OG1 . THR A 125 ? 0.21174 0.18297 0.25215 -0.03570 0.03933  0.00316  20  THR A OG1 
139  C  CG2 . THR A 125 ? 0.21802 0.19848 0.27716 -0.04161 0.04934  0.00197  20  THR A CG2 
140  N  N   . SER A 126 ? 0.19738 0.15339 0.23611 -0.04137 0.03404  0.00614  21  SER A N   
141  C  CA  . SER A 126 ? 0.21923 0.16789 0.25048 -0.03919 0.02888  0.00678  21  SER A CA  
142  C  C   . SER A 126 ? 0.20220 0.14272 0.21945 -0.03752 0.02981  0.01066  21  SER A C   
143  O  O   . SER A 126 ? 0.24501 0.17870 0.25684 -0.03585 0.02608  0.01179  21  SER A O   
144  C  CB  . SER A 126 ? 0.26804 0.21167 0.30438 -0.04258 0.02766  0.00654  21  SER A CB  
145  O  OG  . SER A 126 ? 0.33824 0.27833 0.37292 -0.04604 0.03244  0.00993  21  SER A OG  
146  N  N   . THR A 127 ? 0.16374 0.10478 0.17515 -0.03795 0.03453  0.01257  22  THR A N   
147  C  CA  . THR A 127 ? 0.16423 0.09802 0.16150 -0.03659 0.03475  0.01625  22  THR A CA  
148  C  C   . THR A 127 ? 0.17231 0.11058 0.16479 -0.03274 0.03326  0.01459  22  THR A C   
149  O  O   . THR A 127 ? 0.18962 0.13498 0.18701 -0.03269 0.03613  0.01211  22  THR A O   
150  C  CB  . THR A 127 ? 0.17740 0.10680 0.16882 -0.04073 0.04146  0.01998  22  THR A CB  
151  O  OG1 . THR A 127 ? 0.25252 0.17910 0.24910 -0.04376 0.04170  0.02155  22  THR A OG1 
152  C  CG2 . THR A 127 ? 0.22110 0.14315 0.19694 -0.03954 0.04096  0.02401  22  THR A CG2 
153  N  N   . TYR A 128 ? 0.13434 0.06845 0.11809 -0.02958 0.02889  0.01592  23  TYR A N   
154  C  CA  . TYR A 128 ? 0.12996 0.06724 0.10819 -0.02644 0.02743  0.01470  23  TYR A CA  
155  C  C   . TYR A 128 ? 0.16870 0.10076 0.13397 -0.02754 0.03020  0.01794  23  TYR A C   
156  O  O   . TYR A 128 ? 0.16605 0.09078 0.12321 -0.02757 0.02814  0.02173  23  TYR A O   
157  C  CB  . TYR A 128 ? 0.12403 0.06116 0.10153 -0.02251 0.02088  0.01381  23  TYR A CB  
158  C  CG  . TYR A 128 ? 0.13357 0.07303 0.10519 -0.01956 0.01873  0.01300  23  TYR A CG  
159  C  CD1 . TYR A 128 ? 0.12922 0.07387 0.10181 -0.01955 0.02151  0.01078  23  TYR A CD1 
160  C  CD2 . TYR A 128 ? 0.15296 0.08958 0.11937 -0.01679 0.01391  0.01419  23  TYR A CD2 
161  C  CE1 . TYR A 128 ? 0.12082 0.06710 0.08860 -0.01717 0.01937  0.00975  23  TYR A CE1 
162  C  CE2 . TYR A 128 ? 0.11765 0.05690 0.07984 -0.01451 0.01172  0.01324  23  TYR A CE2 
163  C  CZ  . TYR A 128 ? 0.15286 0.09659 0.11543 -0.01495 0.01451  0.01102  23  TYR A CZ  
164  O  OH  . TYR A 128 ? 0.15299 0.09871 0.11169 -0.01313 0.01244  0.00988  23  TYR A OH  
165  N  N   A TYR A 129 ? 0.16744 0.10309 0.13073 -0.02841 0.03477  0.01638  24  TYR A N   
166  N  N   B TYR A 129 ? 0.16739 0.10294 0.13060 -0.02849 0.03486  0.01644  24  TYR A N   
167  C  CA  A TYR A 129 ? 0.18174 0.11301 0.13172 -0.02992 0.03799  0.01862  24  TYR A CA  
168  C  CA  B TYR A 129 ? 0.18013 0.11106 0.12971 -0.02990 0.03780  0.01881  24  TYR A CA  
169  C  C   A TYR A 129 ? 0.17618 0.10888 0.11984 -0.02674 0.03437  0.01691  24  TYR A C   
170  C  C   B TYR A 129 ? 0.17642 0.10904 0.11999 -0.02677 0.03438  0.01696  24  TYR A C   
171  O  O   A TYR A 129 ? 0.20110 0.14003 0.15174 -0.02476 0.03392  0.01301  24  TYR A O   
172  O  O   B TYR A 129 ? 0.19936 0.13826 0.14989 -0.02491 0.03424  0.01301  24  TYR A O   
173  C  CB  A TYR A 129 ? 0.18448 0.11890 0.13661 -0.03314 0.04623  0.01710  24  TYR A CB  
174  C  CB  B TYR A 129 ? 0.19423 0.12745 0.14450 -0.03336 0.04612  0.01776  24  TYR A CB  
175  C  CG  A TYR A 129 ? 0.15887 0.09385 0.12009 -0.03685 0.05069  0.01807  24  TYR A CG  
176  C  CG  B TYR A 129 ? 0.18878 0.11939 0.14265 -0.03756 0.05060  0.02039  24  TYR A CG  
177  C  CD1 A TYR A 129 ? 0.30138 0.23018 0.25577 -0.04031 0.05358  0.02234  24  TYR A CD1 
178  C  CD1 B TYR A 129 ? 0.18104 0.10454 0.12458 -0.03963 0.05101  0.02516  24  TYR A CD1 
179  C  CD2 A TYR A 129 ? 0.17117 0.11388 0.14841 -0.03672 0.05137  0.01461  24  TYR A CD2 
180  C  CD2 B TYR A 129 ? 0.19051 0.12741 0.15942 -0.03894 0.05340  0.01782  24  TYR A CD2 
181  C  CE1 A TYR A 129 ? 0.26323 0.19421 0.22723 -0.04317 0.05655  0.02270  24  TYR A CE1 
182  C  CE1 B TYR A 129 ? 0.23850 0.16161 0.18728 -0.04264 0.05377  0.02706  24  TYR A CE1 
183  C  CE2 A TYR A 129 ? 0.22378 0.16766 0.21033 -0.04056 0.05527  0.01524  24  TYR A CE2 
184  C  CE2 B TYR A 129 ? 0.22965 0.16573 0.20354 -0.04253 0.05660  0.01964  24  TYR A CE2 
185  C  CZ  A TYR A 129 ? 0.22307 0.16135 0.20305 -0.04359 0.05767  0.01909  24  TYR A CZ  
186  C  CZ  B TYR A 129 ? 0.24971 0.17909 0.21356 -0.04420 0.05666  0.02416  24  TYR A CZ  
187  O  OH  A TYR A 129 ? 0.24165 0.18235 0.23106 -0.04669 0.06012  0.01945  24  TYR A OH  
188  O  OH  B TYR A 129 ? 0.30733 0.23664 0.27681 -0.04749 0.05922  0.02589  24  TYR A OH  
189  N  N   . TYR A 130 ? 0.15982 0.08674 0.09077 -0.02638 0.03148  0.02000  25  TYR A N   
190  C  CA  . TYR A 130 ? 0.17317 0.10163 0.09880 -0.02370 0.02740  0.01830  25  TYR A CA  
191  C  C   . TYR A 130 ? 0.19501 0.11730 0.10477 -0.02487 0.02630  0.02167  25  TYR A C   
192  O  O   . TYR A 130 ? 0.20515 0.12116 0.10832 -0.02676 0.02664  0.02633  25  TYR A O   
193  C  CB  . TYR A 130 ? 0.17533 0.10605 0.10801 -0.02000 0.02052  0.01766  25  TYR A CB  
194  C  CG  . TYR A 130 ? 0.17460 0.09967 0.10515 -0.01921 0.01623  0.02178  25  TYR A CG  
195  C  CD1 . TYR A 130 ? 0.16912 0.09196 0.10639 -0.02029 0.01729  0.02306  25  TYR A CD1 
196  C  CD2 . TYR A 130 ? 0.16519 0.08685 0.08746 -0.01747 0.01104  0.02439  25  TYR A CD2 
197  C  CE1 . TYR A 130 ? 0.17682 0.09337 0.11243 -0.01946 0.01367  0.02674  25  TYR A CE1 
198  C  CE2 . TYR A 130 ? 0.17697 0.09315 0.09836 -0.01625 0.00701  0.02836  25  TYR A CE2 
199  C  CZ  . TYR A 130 ? 0.21420 0.12754 0.14246 -0.01711 0.00852  0.02938  25  TYR A CZ  
200  O  OH  . TYR A 130 ? 0.28844 0.19546 0.21654 -0.01575 0.00479  0.03308  25  TYR A OH  
201  N  N   . ASP A 131 ? 0.16921 0.09304 0.07257 -0.02403 0.02499  0.01932  26  ASP A N   
202  C  CA  . ASP A 131 ? 0.19335 0.11202 0.08128 -0.02497 0.02244  0.02214  26  ASP A CA  
203  C  C   . ASP A 131 ? 0.18154 0.09779 0.06879 -0.02229 0.01421  0.02578  26  ASP A C   
204  O  O   . ASP A 131 ? 0.20321 0.12381 0.09986 -0.01909 0.00984  0.02376  26  ASP A O   
205  C  CB  . ASP A 131 ? 0.20899 0.13029 0.09138 -0.02492 0.02282  0.01775  26  ASP A CB  
206  C  CG  . ASP A 131 ? 0.25052 0.16756 0.11702 -0.02650 0.02065  0.01975  26  ASP A CG  
207  O  OD1 . ASP A 131 ? 0.33678 0.25294 0.19740 -0.02909 0.02578  0.01930  26  ASP A OD1 
208  O  OD2 . ASP A 131 ? 0.25637 0.17330 0.11987 -0.02464 0.01326  0.02107  26  ASP A OD2 
209  N  N   . GLU A 132 ? 0.23107 0.14172 0.10834 -0.02331 0.01204  0.03071  27  GLU A N   
210  C  CA  . GLU A 132 ? 0.23493 0.14361 0.11286 -0.02047 0.00436  0.03453  27  GLU A CA  
211  C  C   . GLU A 132 ? 0.23054 0.14271 0.10891 -0.01764 -0.00208 0.03264  27  GLU A C   
212  O  O   . GLU A 132 ? 0.24840 0.16066 0.13207 -0.01453 -0.00802 0.03459  27  GLU A O   
213  C  CB  . GLU A 132 ? 0.32989 0.23517 0.19863 -0.02157 0.00279  0.03898  27  GLU A CB  
214  C  CG  . GLU A 132 ? 0.62196 0.52277 0.48914 -0.02402 0.00698  0.04302  27  GLU A CG  
215  C  CD  . GLU A 132 ? 0.81608 0.71768 0.68491 -0.02759 0.01590  0.04070  27  GLU A CD  
216  O  OE1 . GLU A 132 ? 0.41674 0.32187 0.28363 -0.02887 0.02005  0.03612  27  GLU A OE1 
217  O  OE2 . GLU A 132 ? 0.55810 0.45691 0.43068 -0.02919 0.01891  0.04349  27  GLU A OE2 
218  N  N   . SER A 133 ? 0.22545 0.14076 0.09903 -0.01867 -0.00099 0.02866  28  SER A N   
219  C  CA  . SER A 133 ? 0.19134 0.11047 0.06618 -0.01647 -0.00710 0.02669  28  SER A CA  
220  C  C   . SER A 133 ? 0.21747 0.14189 0.10776 -0.01315 -0.00901 0.02452  28  SER A C   
221  O  O   . SER A 133 ? 0.20433 0.13148 0.09884 -0.01053 -0.01504 0.02483  28  SER A O   
222  C  CB  . SER A 133 ? 0.20028 0.12186 0.06934 -0.01842 -0.00466 0.02185  28  SER A CB  
223  O  OG  . SER A 133 ? 0.23351 0.15764 0.10922 -0.01921 0.00221  0.01771  28  SER A OG  
224  N  N   . ALA A 134 ? 0.18099 0.10757 0.08025 -0.01333 -0.00388 0.02212  29  ALA A N   
225  C  CA  . ALA A 134 ? 0.14758 0.07824 0.06057 -0.01061 -0.00511 0.02065  29  ALA A CA  
226  C  C   . ALA A 134 ? 0.16433 0.10090 0.08326 -0.00820 -0.00936 0.01792  29  ALA A C   
227  O  O   . ALA A 134 ? 0.18135 0.12022 0.10832 -0.00558 -0.01247 0.01809  29  ALA A O   
228  C  CB  . ALA A 134 ? 0.19642 0.12288 0.11201 -0.00920 -0.00754 0.02466  29  ALA A CB  
229  N  N   . GLY A 135 ? 0.13838 0.07751 0.05401 -0.00925 -0.00899 0.01497  30  GLY A N   
230  C  CA  . GLY A 135 ? 0.14292 0.08755 0.06496 -0.00749 -0.01253 0.01257  30  GLY A CA  
231  C  C   . GLY A 135 ? 0.14963 0.09493 0.06939 -0.00617 -0.01910 0.01447  30  GLY A C   
232  O  O   . GLY A 135 ? 0.15903 0.10958 0.08560 -0.00480 -0.02193 0.01260  30  GLY A O   
233  N  N   . GLN A 136 ? 0.17965 0.12008 0.09027 -0.00671 -0.02167 0.01827  31  GLN A N   
234  C  CA  . GLN A 136 ? 0.15058 0.09201 0.05942 -0.00532 -0.02878 0.02043  31  GLN A CA  
235  C  C   . GLN A 136 ? 0.21513 0.16043 0.12158 -0.00678 -0.03089 0.01709  31  GLN A C   
236  O  O   . GLN A 136 ? 0.23796 0.18114 0.13585 -0.00969 -0.02789 0.01494  31  GLN A O   
237  C  CB  . GLN A 136 ? 0.21725 0.15200 0.11451 -0.00617 -0.03124 0.02549  31  GLN A CB  
238  C  CG  . GLN A 136 ? 0.32214 0.25944 0.22508 -0.00310 -0.03802 0.02832  31  GLN A CG  
239  C  CD  . GLN A 136 ? 0.64287 0.57588 0.53892 -0.00349 -0.03934 0.03286  31  GLN A CD  
240  O  OE1 . GLN A 136 ? 0.79034 0.71781 0.67996 -0.00541 -0.03493 0.03472  31  GLN A OE1 
241  N  NE2 . GLN A 136 ? 0.87177 0.80761 0.76965 -0.00172 -0.04536 0.03483  31  GLN A NE2 
242  N  N   . GLY A 137 ? 0.14560 0.09644 0.05980 -0.00491 -0.03595 0.01649  32  GLY A N   
243  C  CA  . GLY A 137 ? 0.18627 0.14102 0.09964 -0.00659 -0.03843 0.01328  32  GLY A CA  
244  C  C   . GLY A 137 ? 0.17613 0.13535 0.09821 -0.00697 -0.03484 0.00892  32  GLY A C   
245  O  O   . GLY A 137 ? 0.16363 0.12637 0.08735 -0.00827 -0.03713 0.00631  32  GLY A O   
246  N  N   . SER A 138 ? 0.14606 0.10517 0.07392 -0.00604 -0.02968 0.00823  33  SER A N   
247  C  CA  . SER A 138 ? 0.11993 0.08324 0.05666 -0.00596 -0.02683 0.00508  33  SER A CA  
248  C  C   . SER A 138 ? 0.12643 0.09481 0.07429 -0.00320 -0.02844 0.00584  33  SER A C   
249  O  O   . SER A 138 ? 0.14041 0.10842 0.09008 -0.00096 -0.03082 0.00845  33  SER A O   
250  C  CB  . SER A 138 ? 0.13916 0.09986 0.07568 -0.00668 -0.02057 0.00378  33  SER A CB  
251  O  OG  . SER A 138 ? 0.15721 0.11684 0.09695 -0.00497 -0.01909 0.00594  33  SER A OG  
252  N  N   . CYS A 139 ? 0.09957 0.07246 0.05474 -0.00341 -0.02709 0.00350  34  CYS A N   
253  C  CA  . CYS A 139 ? 0.10012 0.07824 0.06517 -0.00128 -0.02757 0.00356  34  CYS A CA  
254  C  C   . CYS A 139 ? 0.10539 0.08462 0.07473 -0.00150 -0.02317 0.00207  34  CYS A C   
255  O  O   . CYS A 139 ? 0.13521 0.11383 0.10341 -0.00339 -0.02116 0.00048  34  CYS A O   
256  C  CB  . CYS A 139 ? 0.11671 0.10068 0.08717 -0.00156 -0.03116 0.00273  34  CYS A CB  
257  S  SG  . CYS A 139 ? 0.14624 0.13023 0.11297 -0.00113 -0.03787 0.00473  34  CYS A SG  
258  N  N   . VAL A 140 ? 0.08035 0.06124 0.05487 0.00047  -0.02199 0.00246  35  VAL A N   
259  C  CA  . VAL A 140 ? 0.08393 0.06631 0.06199 0.00020  -0.01859 0.00130  35  VAL A CA  
260  C  C   . VAL A 140 ? 0.09018 0.07810 0.07523 0.00148  -0.01891 0.00072  35  VAL A C   
261  O  O   . VAL A 140 ? 0.10667 0.09539 0.09444 0.00363  -0.01978 0.00103  35  VAL A O   
262  C  CB  . VAL A 140 ? 0.07930 0.05795 0.05567 0.00065  -0.01606 0.00174  35  VAL A CB  
263  C  CG1 . VAL A 140 ? 0.10184 0.08256 0.08180 0.00030  -0.01354 0.00071  35  VAL A CG1 
264  C  CG2 . VAL A 140 ? 0.08899 0.06241 0.05846 -0.00082 -0.01486 0.00228  35  VAL A CG2 
265  N  N   . TYR A 141 ? 0.07826 0.06961 0.06623 0.00011  -0.01772 -0.00015 36  TYR A N   
266  C  CA  . TYR A 141 ? 0.06329 0.06003 0.05703 0.00075  -0.01681 -0.00077 36  TYR A CA  
267  C  C   . TYR A 141 ? 0.10862 0.10457 0.10183 0.00099  -0.01416 -0.00105 36  TYR A C   
268  O  O   . TYR A 141 ? 0.09297 0.08661 0.08383 -0.00030 -0.01291 -0.00069 36  TYR A O   
269  C  CB  . TYR A 141 ? 0.06730 0.06777 0.06388 -0.00140 -0.01673 -0.00104 36  TYR A CB  
270  C  CG  . TYR A 141 ? 0.07613 0.07936 0.07522 -0.00191 -0.01978 -0.00123 36  TYR A CG  
271  C  CD1 . TYR A 141 ? 0.07463 0.07428 0.06912 -0.00330 -0.02203 -0.00124 36  TYR A CD1 
272  C  CD2 . TYR A 141 ? 0.06303 0.07286 0.06928 -0.00123 -0.02037 -0.00169 36  TYR A CD2 
273  C  CE1 . TYR A 141 ? 0.10300 0.10549 0.09950 -0.00411 -0.02563 -0.00154 36  TYR A CE1 
274  C  CE2 . TYR A 141 ? 0.06503 0.07843 0.07502 -0.00188 -0.02374 -0.00187 36  TYR A CE2 
275  C  CZ  . TYR A 141 ? 0.07907 0.08867 0.08387 -0.00336 -0.02678 -0.00171 36  TYR A CZ  
276  O  OH  . TYR A 141 ? 0.11518 0.12868 0.12354 -0.00431 -0.03080 -0.00204 36  TYR A OH  
277  N  N   . VAL A 142 ? 0.06049 0.05828 0.05611 0.00271  -0.01348 -0.00189 37  VAL A N   
278  C  CA  . VAL A 142 ? 0.05946 0.05693 0.05412 0.00267  -0.01145 -0.00260 37  VAL A CA  
279  C  C   . VAL A 142 ? 0.07162 0.07452 0.06890 0.00217  -0.00987 -0.00342 37  VAL A C   
280  O  O   . VAL A 142 ? 0.08818 0.09460 0.08925 0.00354  -0.00954 -0.00471 37  VAL A O   
281  C  CB  . VAL A 142 ? 0.09539 0.08999 0.08987 0.00453  -0.01150 -0.00353 37  VAL A CB  
282  C  CG1 . VAL A 142 ? 0.14031 0.13466 0.13348 0.00401  -0.00992 -0.00474 37  VAL A CG1 
283  C  CG2 . VAL A 142 ? 0.15262 0.14179 0.14416 0.00462  -0.01268 -0.00218 37  VAL A CG2 
284  N  N   . ILE A 143 ? 0.05888 0.06253 0.05445 0.00018  -0.00879 -0.00247 38  ILE A N   
285  C  CA  . ILE A 143 ? 0.06436 0.07273 0.06120 -0.00110 -0.00702 -0.00242 38  ILE A CA  
286  C  C   . ILE A 143 ? 0.07229 0.08091 0.06594 -0.00111 -0.00562 -0.00322 38  ILE A C   
287  O  O   . ILE A 143 ? 0.08986 0.09604 0.08025 -0.00206 -0.00614 -0.00194 38  ILE A O   
288  C  CB  . ILE A 143 ? 0.08118 0.08918 0.07774 -0.00353 -0.00713 -0.00028 38  ILE A CB  
289  C  CG1 . ILE A 143 ? 0.13143 0.13839 0.13014 -0.00374 -0.00898 -0.00023 38  ILE A CG1 
290  C  CG2 . ILE A 143 ? 0.10496 0.11736 0.10231 -0.00548 -0.00495 0.00052  38  ILE A CG2 
291  C  CD1 . ILE A 143 ? 0.16082 0.16582 0.15924 -0.00623 -0.00917 0.00127  38  ILE A CD1 
292  N  N   . ASP A 144 ? 0.06154 0.07298 0.05632 0.00010  -0.00407 -0.00566 39  ASP A N   
293  C  CA  . ASP A 144 ? 0.06417 0.07457 0.05524 0.00036  -0.00335 -0.00745 39  ASP A CA  
294  C  C   . ASP A 144 ? 0.07987 0.09418 0.07240 0.00137  -0.00066 -0.01068 39  ASP A C   
295  O  O   . ASP A 144 ? 0.07885 0.09798 0.07401 0.00076  0.00138  -0.01063 39  ASP A O   
296  C  CB  . ASP A 144 ? 0.07435 0.07959 0.06508 0.00167  -0.00528 -0.00799 39  ASP A CB  
297  C  CG  . ASP A 144 ? 0.11440 0.11782 0.10118 0.00078  -0.00573 -0.00867 39  ASP A CG  
298  O  OD1 . ASP A 144 ? 0.09860 0.10322 0.08360 0.00093  -0.00453 -0.01146 39  ASP A OD1 
299  O  OD2 . ASP A 144 ? 0.16280 0.16371 0.14858 -0.00010 -0.00732 -0.00673 39  ASP A OD2 
300  N  N   . THR A 145 ? 0.07377 0.08617 0.06501 0.00268  -0.00027 -0.01376 40  THR A N   
301  C  CA  . THR A 145 ? 0.07389 0.08946 0.06668 0.00394  0.00281  -0.01774 40  THR A CA  
302  C  C   . THR A 145 ? 0.08211 0.09824 0.08285 0.00715  0.00283  -0.01927 40  THR A C   
303  O  O   . THR A 145 ? 0.08558 0.10399 0.08928 0.00887  0.00549  -0.02302 40  THR A O   
304  C  CB  . THR A 145 ? 0.07887 0.09162 0.06685 0.00388  0.00323  -0.02116 40  THR A CB  
305  O  OG1 . THR A 145 ? 0.09910 0.10610 0.08918 0.00544  0.00065  -0.02140 40  THR A OG1 
306  C  CG2 . THR A 145 ? 0.13541 0.14820 0.11544 0.00078  0.00246  -0.01952 40  THR A CG2 
307  N  N   . GLY A 146 ? 0.08251 0.09656 0.08660 0.00804  -0.00010 -0.01659 41  GLY A N   
308  C  CA  . GLY A 146 ? 0.09096 0.10469 0.10197 0.01121  -0.00130 -0.01723 41  GLY A CA  
309  C  C   . GLY A 146 ? 0.08791 0.09428 0.09761 0.01253  -0.00402 -0.01647 41  GLY A C   
310  O  O   . GLY A 146 ? 0.12460 0.12675 0.12892 0.01090  -0.00467 -0.01583 41  GLY A O   
311  N  N   . ILE A 147 ? 0.07927 0.08429 0.09446 0.01545  -0.00573 -0.01624 42  ILE A N   
312  C  CA  . ILE A 147 ? 0.07352 0.07106 0.08770 0.01674  -0.00819 -0.01496 42  ILE A CA  
313  C  C   . ILE A 147 ? 0.10242 0.09878 0.12333 0.02059  -0.00809 -0.01719 42  ILE A C   
314  O  O   . ILE A 147 ? 0.10985 0.11098 0.13778 0.02287  -0.00852 -0.01732 42  ILE A O   
315  C  CB  . ILE A 147 ? 0.11202 0.10737 0.12485 0.01632  -0.01164 -0.01072 42  ILE A CB  
316  C  CG1 . ILE A 147 ? 0.09620 0.09284 0.10380 0.01292  -0.01155 -0.00887 42  ILE A CG1 
317  C  CG2 . ILE A 147 ? 0.13966 0.12661 0.15010 0.01712  -0.01348 -0.00906 42  ILE A CG2 
318  C  CD1 . ILE A 147 ? 0.11599 0.11071 0.12178 0.01238  -0.01460 -0.00553 42  ILE A CD1 
319  N  N   . GLU A 148 ? 0.08217 0.07207 0.10195 0.02139  -0.00775 -0.01888 43  GLU A N   
320  C  CA  . GLU A 148 ? 0.08753 0.07419 0.11407 0.02536  -0.00819 -0.02044 43  GLU A CA  
321  C  C   . GLU A 148 ? 0.11792 0.10019 0.14568 0.02686  -0.01247 -0.01557 43  GLU A C   
322  O  O   . GLU A 148 ? 0.12894 0.10322 0.15319 0.02636  -0.01400 -0.01344 43  GLU A O   
323  C  CB  . GLU A 148 ? 0.10760 0.08797 0.13255 0.02537  -0.00647 -0.02405 43  GLU A CB  
324  C  CG  . GLU A 148 ? 0.09944 0.07598 0.13233 0.02978  -0.00626 -0.02657 43  GLU A CG  
325  C  CD  . GLU A 148 ? 0.14636 0.11666 0.17734 0.02920  -0.00420 -0.03111 43  GLU A CD  
326  O  OE1 . GLU A 148 ? 0.16156 0.13566 0.19197 0.02878  -0.00065 -0.03645 43  GLU A OE1 
327  O  OE2 . GLU A 148 ? 0.16402 0.12566 0.19370 0.02881  -0.00611 -0.02925 43  GLU A OE2 
328  N  N   . ALA A 149 ? 0.11201 0.09979 0.14478 0.02848  -0.01449 -0.01370 44  ALA A N   
329  C  CA  . ALA A 149 ? 0.14692 0.13156 0.17884 0.02917  -0.01918 -0.00867 44  ALA A CA  
330  C  C   . ALA A 149 ? 0.15846 0.13539 0.19362 0.03257  -0.02154 -0.00714 44  ALA A C   
331  O  O   . ALA A 149 ? 0.22256 0.19404 0.25349 0.03224  -0.02507 -0.00248 44  ALA A O   
332  C  CB  . ALA A 149 ? 0.20188 0.19474 0.23923 0.03001  -0.02134 -0.00751 44  ALA A CB  
333  N  N   . SER A 150 ? 0.11437 0.09006 0.15637 0.03567  -0.01949 -0.01091 45  SER A N   
334  C  CA  . SER A 150 ? 0.11466 0.08211 0.16094 0.03923  -0.02152 -0.00971 45  SER A CA  
335  C  C   . SER A 150 ? 0.13856 0.09569 0.17792 0.03695  -0.02076 -0.00899 45  SER A C   
336  O  O   . SER A 150 ? 0.15378 0.10254 0.19591 0.03935  -0.02242 -0.00742 45  SER A O   
337  C  CB  . SER A 150 ? 0.16204 0.13215 0.21933 0.04358  -0.01909 -0.01483 45  SER A CB  
338  O  OG  . SER A 150 ? 0.23476 0.20452 0.28941 0.04175  -0.01404 -0.02057 45  SER A OG  
339  N  N   . HIS A 151 ? 0.12928 0.08683 0.16078 0.03243  -0.01823 -0.01024 46  HIS A N   
340  C  CA  . HIS A 151 ? 0.12140 0.07020 0.14779 0.02996  -0.01745 -0.00980 46  HIS A CA  
341  C  C   . HIS A 151 ? 0.13389 0.07531 0.15684 0.02982  -0.02091 -0.00337 46  HIS A C   
342  O  O   . HIS A 151 ? 0.13733 0.08160 0.15588 0.02862  -0.02303 0.00056  46  HIS A O   
343  C  CB  . HIS A 151 ? 0.11136 0.06335 0.13069 0.02526  -0.01515 -0.01110 46  HIS A CB  
344  C  CG  . HIS A 151 ? 0.14544 0.09086 0.16194 0.02260  -0.01355 -0.01281 46  HIS A CG  
345  N  ND1 . HIS A 151 ? 0.13305 0.06968 0.14741 0.02143  -0.01471 -0.00921 46  HIS A ND1 
346  C  CD2 . HIS A 151 ? 0.14217 0.08876 0.15760 0.02054  -0.01106 -0.01768 46  HIS A CD2 
347  C  CE1 . HIS A 151 ? 0.14983 0.08285 0.16309 0.01871  -0.01289 -0.01200 46  HIS A CE1 
348  N  NE2 . HIS A 151 ? 0.13642 0.07537 0.15021 0.01823  -0.01100 -0.01724 46  HIS A NE2 
349  N  N   . PRO A 152 ? 0.13824 0.06980 0.16231 0.03065  -0.02144 -0.00214 47  PRO A N   
350  C  CA  . PRO A 152 ? 0.13377 0.05763 0.15349 0.03027  -0.02461 0.00468  47  PRO A CA  
351  C  C   . PRO A 152 ? 0.13249 0.05686 0.14242 0.02551  -0.02409 0.00791  47  PRO A C   
352  O  O   . PRO A 152 ? 0.15584 0.07761 0.16060 0.02512  -0.02685 0.01346  47  PRO A O   
353  C  CB  . PRO A 152 ? 0.20185 0.11508 0.22399 0.03056  -0.02363 0.00429  47  PRO A CB  
354  C  CG  . PRO A 152 ? 0.21092 0.12702 0.24106 0.03326  -0.02131 -0.00233 47  PRO A CG  
355  C  CD  . PRO A 152 ? 0.13685 0.06336 0.16645 0.03219  -0.01926 -0.00698 47  PRO A CD  
356  N  N   . GLU A 153 ? 0.12625 0.05430 0.13341 0.02199  -0.02074 0.00452  48  GLU A N   
357  C  CA  . GLU A 153 ? 0.12169 0.05013 0.12103 0.01772  -0.01966 0.00704  48  GLU A CA  
358  C  C   . GLU A 153 ? 0.11693 0.05199 0.11254 0.01754  -0.02121 0.00893  48  GLU A C   
359  O  O   . GLU A 153 ? 0.13403 0.06837 0.12278 0.01454  -0.02062 0.01153  48  GLU A O   
360  C  CB  . GLU A 153 ? 0.12127 0.05255 0.12043 0.01453  -0.01624 0.00279  48  GLU A CB  
361  C  CG  . GLU A 153 ? 0.15339 0.07694 0.15379 0.01269  -0.01471 0.00195  48  GLU A CG  
362  C  CD  . GLU A 153 ? 0.24888 0.16773 0.24380 0.00910  -0.01380 0.00633  48  GLU A CD  
363  O  OE1 . GLU A 153 ? 0.27029 0.19370 0.26046 0.00744  -0.01334 0.00805  48  GLU A OE1 
364  O  OE2 . GLU A 153 ? 0.27927 0.18986 0.27475 0.00788  -0.01328 0.00793  48  GLU A OE2 
365  N  N   . PHE A 154 ? 0.11354 0.05490 0.11382 0.02053  -0.02300 0.00752  49  PHE A N   
366  C  CA  . PHE A 154 ? 0.11417 0.06140 0.11119 0.01992  -0.02483 0.00924  49  PHE A CA  
367  C  C   . PHE A 154 ? 0.12838 0.07271 0.12380 0.02186  -0.02946 0.01408  49  PHE A C   
368  O  O   . PHE A 154 ? 0.12587 0.07376 0.11700 0.02075  -0.03146 0.01581  49  PHE A O   
369  C  CB  . PHE A 154 ? 0.10218 0.05891 0.10497 0.02119  -0.02420 0.00533  49  PHE A CB  
370  C  CG  . PHE A 154 ? 0.10506 0.06529 0.10739 0.01884  -0.02031 0.00137  49  PHE A CG  
371  C  CD1 . PHE A 154 ? 0.12891 0.08921 0.12511 0.01524  -0.01877 0.00208  49  PHE A CD1 
372  C  CD2 . PHE A 154 ? 0.09369 0.05689 0.10155 0.02029  -0.01828 -0.00300 49  PHE A CD2 
373  C  CE1 . PHE A 154 ? 0.13520 0.09872 0.13131 0.01324  -0.01594 -0.00103 49  PHE A CE1 
374  C  CE2 . PHE A 154 ? 0.12865 0.09499 0.13487 0.01791  -0.01530 -0.00626 49  PHE A CE2 
375  C  CZ  . PHE A 154 ? 0.10727 0.07368 0.10780 0.01445  -0.01452 -0.00493 49  PHE A CZ  
376  N  N   . GLU A 155 ? 0.12550 0.06328 0.12422 0.02472  -0.03157 0.01631  50  GLU A N   
377  C  CA  . GLU A 155 ? 0.13503 0.06824 0.13074 0.02630  -0.03656 0.02213  50  GLU A CA  
378  C  C   . GLU A 155 ? 0.14430 0.08535 0.14330 0.02844  -0.04085 0.02265  50  GLU A C   
379  O  O   . GLU A 155 ? 0.19786 0.13753 0.19088 0.02802  -0.04510 0.02713  50  GLU A O   
380  C  CB  . GLU A 155 ? 0.17779 0.10498 0.16123 0.02223  -0.03618 0.02650  50  GLU A CB  
381  C  CG  . GLU A 155 ? 0.21527 0.13556 0.19598 0.01934  -0.03170 0.02616  50  GLU A CG  
382  C  CD  . GLU A 155 ? 0.25270 0.16845 0.22180 0.01508  -0.03038 0.03008  50  GLU A CD  
383  O  OE1 . GLU A 155 ? 0.21235 0.13338 0.17648 0.01262  -0.02899 0.02877  50  GLU A OE1 
384  O  OE2 . GLU A 155 ? 0.24675 0.15383 0.21165 0.01410  -0.03044 0.03450  50  GLU A OE2 
385  N  N   . GLY A 156 ? 0.14661 0.09616 0.15460 0.03028  -0.03968 0.01801  51  GLY A N   
386  C  CA  . GLY A 156 ? 0.16108 0.11902 0.17400 0.03198  -0.04345 0.01812  51  GLY A CA  
387  C  C   . GLY A 156 ? 0.16223 0.12596 0.16891 0.02808  -0.04300 0.01736  51  GLY A C   
388  O  O   . GLY A 156 ? 0.16572 0.13633 0.17582 0.02868  -0.04646 0.01754  51  GLY A O   
389  N  N   . ARG A 157 ? 0.11962 0.08069 0.11798 0.02415  -0.03909 0.01652  52  ARG A N   
390  C  CA  . ARG A 157 ? 0.11002 0.07517 0.10219 0.02049  -0.03843 0.01578  52  ARG A CA  
391  C  C   . ARG A 157 ? 0.15033 0.12315 0.14763 0.01951  -0.03486 0.01116  52  ARG A C   
392  O  O   . ARG A 157 ? 0.15723 0.13277 0.15015 0.01646  -0.03382 0.01030  52  ARG A O   
393  C  CB  . ARG A 157 ? 0.11981 0.07839 0.10091 0.01686  -0.03588 0.01735  52  ARG A CB  
394  C  CG  . ARG A 157 ? 0.13277 0.08415 0.10571 0.01661  -0.03932 0.02250  52  ARG A CG  
395  C  CD  . ARG A 157 ? 0.15877 0.10385 0.12131 0.01283  -0.03566 0.02382  52  ARG A CD  
396  N  NE  . ARG A 157 ? 0.14042 0.08077 0.10555 0.01276  -0.03177 0.02322  52  ARG A NE  
397  C  CZ  . ARG A 157 ? 0.14699 0.08959 0.11439 0.01103  -0.02709 0.01955  52  ARG A CZ  
398  N  NH1 . ARG A 157 ? 0.13570 0.08463 0.10331 0.00951  -0.02542 0.01648  52  ARG A NH1 
399  N  NH2 . ARG A 157 ? 0.14011 0.07847 0.11026 0.01083  -0.02436 0.01892  52  ARG A NH2 
400  N  N   . ALA A 158 ? 0.12968 0.10562 0.13558 0.02186  -0.03281 0.00821  53  ALA A N   
401  C  CA  . ALA A 158 ? 0.09430 0.07696 0.10387 0.02068  -0.02907 0.00421  53  ALA A CA  
402  C  C   . ALA A 158 ? 0.12175 0.11235 0.14163 0.02329  -0.03018 0.00251  53  ALA A C   
403  O  O   . ALA A 158 ? 0.15342 0.14357 0.18007 0.02705  -0.03220 0.00291  53  ALA A O   
404  C  CB  . ALA A 158 ? 0.12376 0.10376 0.13334 0.02042  -0.02469 0.00143  53  ALA A CB  
405  N  N   . GLN A 159 ? 0.10785 0.10566 0.12967 0.02131  -0.02877 0.00071  54  GLN A N   
406  C  CA  . GLN A 159 ? 0.11667 0.12289 0.14928 0.02336  -0.02855 -0.00140 54  GLN A CA  
407  C  C   . GLN A 159 ? 0.11048 0.12271 0.14369 0.02057  -0.02431 -0.00405 54  GLN A C   
408  O  O   . GLN A 159 ? 0.12932 0.14039 0.15569 0.01706  -0.02353 -0.00337 54  GLN A O   
409  C  CB  . GLN A 159 ? 0.25737 0.26719 0.29422 0.02437  -0.03407 0.00095  54  GLN A CB  
410  C  CG  . GLN A 159 ? 0.23712 0.25033 0.27056 0.02070  -0.03550 0.00156  54  GLN A CG  
411  C  CD  . GLN A 159 ? 0.61935 0.63625 0.65721 0.02170  -0.04181 0.00366  54  GLN A CD  
412  O  OE1 . GLN A 159 ? 0.64655 0.67220 0.69499 0.02248  -0.04279 0.00236  54  GLN A OE1 
413  N  NE2 . GLN A 159 ? 0.46664 0.47707 0.49621 0.02144  -0.04619 0.00699  54  GLN A NE2 
414  N  N   . MET A 160 ? 0.10067 0.11903 0.14212 0.02222  -0.02132 -0.00705 55  MET A N   
415  C  CA  . MET A 160 ? 0.07203 0.09658 0.11414 0.01937  -0.01738 -0.00896 55  MET A CA  
416  C  C   . MET A 160 ? 0.10654 0.13852 0.15481 0.01807  -0.01946 -0.00813 55  MET A C   
417  O  O   . MET A 160 ? 0.14688 0.18323 0.20432 0.02079  -0.02226 -0.00803 55  MET A O   
418  C  CB  . MET A 160 ? 0.08178 0.11028 0.12889 0.02088  -0.01238 -0.01281 55  MET A CB  
419  C  CG  . MET A 160 ? 0.10139 0.12314 0.14243 0.02151  -0.01001 -0.01454 55  MET A CG  
420  S  SD  . MET A 160 ? 0.11183 0.13084 0.14145 0.01672  -0.00806 -0.01363 55  MET A SD  
421  C  CE  . MET A 160 ? 0.11850 0.14645 0.15065 0.01421  -0.00396 -0.01505 55  MET A CE  
422  N  N   . VAL A 161 ? 0.07995 0.11330 0.12399 0.01394  -0.01839 -0.00751 56  VAL A N   
423  C  CA  . VAL A 161 ? 0.06216 0.10207 0.11183 0.01186  -0.02029 -0.00696 56  VAL A CA  
424  C  C   . VAL A 161 ? 0.07137 0.11830 0.12536 0.00931  -0.01547 -0.00856 56  VAL A C   
425  O  O   . VAL A 161 ? 0.12185 0.17607 0.18396 0.00795  -0.01633 -0.00870 56  VAL A O   
426  C  CB  . VAL A 161 ? 0.09419 0.12950 0.13628 0.00887  -0.02390 -0.00476 56  VAL A CB  
427  C  CG1 . VAL A 161 ? 0.16078 0.19014 0.19877 0.01115  -0.02888 -0.00283 56  VAL A CG1 
428  C  CG2 . VAL A 161 ? 0.15627 0.18642 0.18918 0.00592  -0.02077 -0.00449 56  VAL A CG2 
429  N  N   . LYS A 162 ? 0.07164 0.11696 0.12067 0.00842  -0.01053 -0.00968 57  LYS A N   
430  C  CA  . LYS A 162 ? 0.07501 0.12644 0.12652 0.00552  -0.00581 -0.01054 57  LYS A CA  
431  C  C   . LYS A 162 ? 0.07309 0.12285 0.11920 0.00583  -0.00092 -0.01224 57  LYS A C   
432  O  O   . LYS A 162 ? 0.09189 0.13447 0.12948 0.00614  -0.00156 -0.01174 57  LYS A O   
433  C  CB  . LYS A 162 ? 0.09215 0.14159 0.13871 0.00096  -0.00661 -0.00818 57  LYS A CB  
434  C  CG  . LYS A 162 ? 0.09694 0.15104 0.14447 -0.00274 -0.00188 -0.00799 57  LYS A CG  
435  C  CD  . LYS A 162 ? 0.13029 0.19417 0.19001 -0.00356 -0.00107 -0.00898 57  LYS A CD  
436  C  CE  . LYS A 162 ? 0.23484 0.30289 0.29490 -0.00771 0.00424  -0.00840 57  LYS A CE  
437  N  NZ  . LYS A 162 ? 0.30890 0.38746 0.38194 -0.00893 0.00600  -0.00955 57  LYS A NZ  
438  N  N   . THR A 163 ? 0.07461 0.13130 0.12560 0.00543  0.00399  -0.01438 58  THR A N   
439  C  CA  . THR A 163 ? 0.07071 0.12630 0.11483 0.00465  0.00886  -0.01601 58  THR A CA  
440  C  C   . THR A 163 ? 0.06943 0.13116 0.11403 0.00068  0.01358  -0.01549 58  THR A C   
441  O  O   . THR A 163 ? 0.11639 0.18545 0.17045 -0.00037 0.01452  -0.01547 58  THR A O   
442  C  CB  . THR A 163 ? 0.06846 0.12508 0.11615 0.00872  0.01130  -0.02021 58  THR A CB  
443  O  OG1 . THR A 163 ? 0.08718 0.14246 0.12649 0.00732  0.01579  -0.02211 58  THR A OG1 
444  C  CG2 . THR A 163 ? 0.09132 0.15741 0.15262 0.01068  0.01374  -0.02270 58  THR A CG2 
445  N  N   . TYR A 164 ? 0.07107 0.12977 0.10542 -0.00171 0.01637  -0.01484 59  TYR A N   
446  C  CA  . TYR A 164 ? 0.07358 0.13683 0.10586 -0.00574 0.02127  -0.01381 59  TYR A CA  
447  C  C   . TYR A 164 ? 0.08357 0.15004 0.11292 -0.00520 0.02708  -0.01744 59  TYR A C   
448  O  O   . TYR A 164 ? 0.12553 0.19457 0.14963 -0.00876 0.03164  -0.01651 59  TYR A O   
449  C  CB  . TYR A 164 ? 0.11006 0.16728 0.13237 -0.00937 0.01963  -0.00944 59  TYR A CB  
450  C  CG  . TYR A 164 ? 0.07016 0.12539 0.09645 -0.01060 0.01531  -0.00657 59  TYR A CG  
451  C  CD1 . TYR A 164 ? 0.13903 0.19892 0.17117 -0.01406 0.01669  -0.00485 59  TYR A CD1 
452  C  CD2 . TYR A 164 ? 0.07669 0.12534 0.10085 -0.00861 0.01008  -0.00589 59  TYR A CD2 
453  C  CE1 . TYR A 164 ? 0.11807 0.17586 0.15384 -0.01543 0.01254  -0.00296 59  TYR A CE1 
454  C  CE2 . TYR A 164 ? 0.09231 0.13910 0.11943 -0.00986 0.00640  -0.00399 59  TYR A CE2 
455  C  CZ  . TYR A 164 ? 0.10538 0.15658 0.13810 -0.01326 0.00749  -0.00272 59  TYR A CZ  
456  O  OH  . TYR A 164 ? 0.13614 0.18510 0.17138 -0.01477 0.00372  -0.00149 59  TYR A OH  
457  N  N   . TYR A 165 ? 0.10470 0.17066 0.13691 -0.00092 0.02721  -0.02164 60  TYR A N   
458  C  CA  . TYR A 165 ? 0.09603 0.16465 0.12590 -0.00002 0.03291  -0.02626 60  TYR A CA  
459  C  C   . TYR A 165 ? 0.11032 0.18483 0.15368 0.00423  0.03497  -0.03074 60  TYR A C   
460  O  O   . TYR A 165 ? 0.15442 0.23242 0.20924 0.00579  0.03204  -0.02953 60  TYR A O   
461  C  CB  . TYR A 165 ? 0.11335 0.17389 0.13199 0.00093  0.03118  -0.02767 60  TYR A CB  
462  C  CG  . TYR A 165 ? 0.13777 0.19346 0.14468 -0.00294 0.02892  -0.02310 60  TYR A CG  
463  C  CD1 . TYR A 165 ? 0.16110 0.21799 0.15809 -0.00654 0.03276  -0.02254 60  TYR A CD1 
464  C  CD2 . TYR A 165 ? 0.20119 0.25122 0.20724 -0.00293 0.02300  -0.01922 60  TYR A CD2 
465  C  CE1 . TYR A 165 ? 0.21055 0.26282 0.19765 -0.00980 0.02998  -0.01762 60  TYR A CE1 
466  C  CE2 . TYR A 165 ? 0.16468 0.21055 0.16198 -0.00597 0.02092  -0.01508 60  TYR A CE2 
467  C  CZ  . TYR A 165 ? 0.14558 0.19253 0.13407 -0.00919 0.02405  -0.01408 60  TYR A CZ  
468  O  OH  . TYR A 165 ? 0.24005 0.28244 0.22086 -0.01174 0.02114  -0.00938 60  TYR A OH  
469  N  N   . TYR A 166 ? 0.09237 0.16807 0.13469 0.00612  0.03987  -0.03606 61  TYR A N   
470  C  CA  . TYR A 166 ? 0.11456 0.19696 0.17100 0.01015  0.04311  -0.04067 61  TYR A CA  
471  C  C   . TYR A 166 ? 0.13726 0.21570 0.20232 0.01538  0.03723  -0.04100 61  TYR A C   
472  O  O   . TYR A 166 ? 0.18665 0.27117 0.26643 0.01874  0.03727  -0.04246 61  TYR A O   
473  C  CB  . TYR A 166 ? 0.13166 0.21543 0.18419 0.01092  0.05021  -0.04692 61  TYR A CB  
474  C  CG  . TYR A 166 ? 0.19705 0.28298 0.23742 0.00555  0.05566  -0.04634 61  TYR A CG  
475  C  CD1 . TYR A 166 ? 0.18312 0.27890 0.22896 0.00289  0.06222  -0.04657 61  TYR A CD1 
476  C  CD2 . TYR A 166 ? 0.21840 0.29685 0.24190 0.00292  0.05435  -0.04542 61  TYR A CD2 
477  C  CE1 . TYR A 166 ? 0.16799 0.26485 0.20120 -0.00241 0.06726  -0.04519 61  TYR A CE1 
478  C  CE2 . TYR A 166 ? 0.22323 0.30344 0.23450 -0.00213 0.05889  -0.04421 61  TYR A CE2 
479  C  CZ  . TYR A 166 ? 0.26435 0.35349 0.27997 -0.00482 0.06547  -0.04402 61  TYR A CZ  
480  O  OH  . TYR A 166 ? 0.29603 0.38443 0.29800 -0.00978 0.06878  -0.04140 61  TYR A OH  
481  N  N   A SER A 167 ? 0.13339 0.20194 0.18981 0.01602  0.03220  -0.03943 62  SER A N   
482  N  N   B SER A 167 ? 0.13324 0.20182 0.19003 0.01617  0.03214  -0.03949 62  SER A N   
483  C  CA  A SER A 167 ? 0.13542 0.19849 0.19743 0.02046  0.02668  -0.03912 62  SER A CA  
484  C  CA  B SER A 167 ? 0.12603 0.18990 0.18955 0.02060  0.02643  -0.03884 62  SER A CA  
485  C  C   A SER A 167 ? 0.13829 0.19443 0.19289 0.01854  0.02022  -0.03371 62  SER A C   
486  C  C   B SER A 167 ? 0.13723 0.19404 0.19329 0.01873  0.01992  -0.03347 62  SER A C   
487  O  O   A SER A 167 ? 0.12585 0.17966 0.16988 0.01447  0.02027  -0.03132 62  SER A O   
488  O  O   B SER A 167 ? 0.12237 0.17723 0.16839 0.01457  0.01985  -0.03082 62  SER A O   
489  C  CB  A SER A 167 ? 0.18197 0.23893 0.24106 0.02347  0.02836  -0.04407 62  SER A CB  
490  C  CB  B SER A 167 ? 0.19127 0.24914 0.25395 0.02436  0.02752  -0.04363 62  SER A CB  
491  O  OG  A SER A 167 ? 0.13941 0.18960 0.20247 0.02723  0.02296  -0.04299 62  SER A OG  
492  O  OG  B SER A 167 ? 0.12419 0.17435 0.17275 0.02187  0.02697  -0.04368 62  SER A OG  
493  N  N   A SER A 168 ? 0.11091 0.16371 0.17115 0.02158  0.01473  -0.03172 63  SER A N   
494  N  N   B SER A 168 ? 0.11005 0.16287 0.17124 0.02200  0.01453  -0.03182 63  SER A N   
495  C  CA  A SER A 168 ? 0.10500 0.15038 0.15787 0.02021  0.00915  -0.02734 63  SER A CA  
496  C  CA  B SER A 168 ? 0.11334 0.15881 0.16758 0.02078  0.00880  -0.02740 63  SER A CA  
497  C  C   A SER A 168 ? 0.14821 0.18413 0.19410 0.02153  0.00778  -0.02833 63  SER A C   
498  C  C   B SER A 168 ? 0.14592 0.18186 0.19236 0.02175  0.00763  -0.02832 63  SER A C   
499  O  O   A SER A 168 ? 0.14264 0.17236 0.18201 0.02017  0.00399  -0.02504 63  SER A O   
500  O  O   B SER A 168 ? 0.14351 0.17328 0.18357 0.02043  0.00376  -0.02497 63  SER A O   
501  C  CB  A SER A 168 ? 0.15360 0.20005 0.21429 0.02203  0.00371  -0.02418 63  SER A CB  
502  C  CB  B SER A 168 ? 0.13921 0.18545 0.20183 0.02316  0.00334  -0.02454 63  SER A CB  
503  O  OG  A SER A 168 ? 0.18799 0.23367 0.25743 0.02704  0.00246  -0.02601 63  SER A OG  
504  O  OG  B SER A 168 ? 0.11244 0.16720 0.18180 0.02136  0.00339  -0.02325 63  SER A OG  
505  N  N   . ARG A 169 ? 0.10429 0.13895 0.15131 0.02376  0.01113  -0.03308 64  ARG A N   
506  C  CA  . ARG A 169 ? 0.13177 0.15725 0.17288 0.02459  0.00982  -0.03439 64  ARG A CA  
507  C  C   . ARG A 169 ? 0.13303 0.15503 0.16167 0.02034  0.00995  -0.03345 64  ARG A C   
508  O  O   . ARG A 169 ? 0.13319 0.15950 0.15667 0.01735  0.01313  -0.03419 64  ARG A O   
509  C  CB  . ARG A 169 ? 0.17185 0.19657 0.21693 0.02763  0.01376  -0.04058 64  ARG A CB  
510  C  CG  . ARG A 169 ? 0.40458 0.43056 0.46320 0.03298  0.01305  -0.04186 64  ARG A CG  
511  C  CD  . ARG A 169 ? 0.65285 0.67773 0.71541 0.03598  0.01790  -0.04895 64  ARG A CD  
512  N  NE  . ARG A 169 ? 0.84382 0.85992 0.89664 0.03448  0.01823  -0.05162 64  ARG A NE  
513  C  CZ  . ARG A 169 ? 0.81497 0.83128 0.85702 0.03063  0.02138  -0.05441 64  ARG A CZ  
514  N  NH1 . ARG A 169 ? 0.84557 0.86992 0.88410 0.02780  0.02517  -0.05486 64  ARG A NH1 
515  N  NH2 . ARG A 169 ? 0.66328 0.67148 0.69782 0.02934  0.02047  -0.05659 64  ARG A NH2 
516  N  N   . ASP A 170 ? 0.09893 0.11301 0.12293 0.02009  0.00658  -0.03187 65  ASP A N   
517  C  CA  . ASP A 170 ? 0.08527 0.09588 0.09915 0.01668  0.00646  -0.03180 65  ASP A CA  
518  C  C   . ASP A 170 ? 0.12225 0.13053 0.13360 0.01713  0.00933  -0.03758 65  ASP A C   
519  O  O   . ASP A 170 ? 0.12563 0.12756 0.13896 0.01907  0.00823  -0.03957 65  ASP A O   
520  C  CB  . ASP A 170 ? 0.09253 0.09644 0.10375 0.01602  0.00215  -0.02803 65  ASP A CB  
521  C  CG  . ASP A 170 ? 0.11950 0.12047 0.12229 0.01274  0.00158  -0.02788 65  ASP A CG  
522  O  OD1 . ASP A 170 ? 0.10245 0.10676 0.10025 0.01065  0.00371  -0.02966 65  ASP A OD1 
523  O  OD2 . ASP A 170 ? 0.11668 0.11226 0.11803 0.01218  -0.00113 -0.02567 65  ASP A OD2 
524  N  N   . GLY A 171 ? 0.09595 0.10883 0.10225 0.01506  0.01305  -0.04033 66  GLY A N   
525  C  CA  . GLY A 171 ? 0.11710 0.12781 0.11902 0.01484  0.01580  -0.04631 66  GLY A CA  
526  C  C   . GLY A 171 ? 0.10629 0.11307 0.09803 0.01131  0.01358  -0.04606 66  GLY A C   
527  O  O   . GLY A 171 ? 0.16902 0.17442 0.15511 0.01019  0.01544  -0.05110 66  GLY A O   
528  N  N   . ASN A 172 ? 0.10701 0.11261 0.09627 0.00937  0.00976  -0.04059 67  ASN A N   
529  C  CA  . ASN A 172 ? 0.10466 0.10779 0.08587 0.00610  0.00716  -0.03962 67  ASN A CA  
530  C  C   . ASN A 172 ? 0.13801 0.13442 0.12140 0.00636  0.00346  -0.03846 67  ASN A C   
531  O  O   . ASN A 172 ? 0.14039 0.13300 0.12056 0.00506  0.00250  -0.04169 67  ASN A O   
532  C  CB  . ASN A 172 ? 0.12452 0.13165 0.10166 0.00354  0.00599  -0.03432 67  ASN A CB  
533  C  CG  . ASN A 172 ? 0.16288 0.16825 0.13288 0.00053  0.00288  -0.03291 67  ASN A CG  
534  O  OD1 . ASN A 172 ? 0.15091 0.15295 0.12283 0.00027  -0.00049 -0.03021 67  ASN A OD1 
535  N  ND2 . ASN A 172 ? 0.18692 0.19468 0.14865 -0.00182 0.00393  -0.03483 67  ASN A ND2 
536  N  N   . GLY A 173 ? 0.11476 0.10958 0.10334 0.00770  0.00148  -0.03410 68  GLY A N   
537  C  CA  . GLY A 173 ? 0.09159 0.08036 0.08181 0.00752  -0.00143 -0.03221 68  GLY A CA  
538  C  C   . GLY A 173 ? 0.08551 0.07508 0.07422 0.00569  -0.00377 -0.02695 68  GLY A C   
539  O  O   . GLY A 173 ? 0.09826 0.08412 0.08962 0.00616  -0.00535 -0.02424 68  GLY A O   
540  N  N   . HIS A 174 ? 0.08957 0.08362 0.07385 0.00358  -0.00384 -0.02546 69  HIS A N   
541  C  CA  . HIS A 174 ? 0.08463 0.07902 0.06808 0.00201  -0.00596 -0.02097 69  HIS A CA  
542  C  C   . HIS A 174 ? 0.09022 0.08396 0.07760 0.00339  -0.00627 -0.01753 69  HIS A C   
543  O  O   . HIS A 174 ? 0.08479 0.07558 0.07319 0.00298  -0.00772 -0.01513 69  HIS A O   
544  C  CB  . HIS A 174 ? 0.10071 0.09978 0.07931 0.00008  -0.00577 -0.01972 69  HIS A CB  
545  C  CG  . HIS A 174 ? 0.09128 0.09069 0.06923 -0.00141 -0.00799 -0.01551 69  HIS A CG  
546  N  ND1 . HIS A 174 ? 0.10623 0.10699 0.08581 -0.00126 -0.00778 -0.01195 69  HIS A ND1 
547  C  CD2 . HIS A 174 ? 0.12832 0.12722 0.10477 -0.00305 -0.01047 -0.01454 69  HIS A CD2 
548  C  CE1 . HIS A 174 ? 0.11443 0.11486 0.09355 -0.00247 -0.00972 -0.00908 69  HIS A CE1 
549  N  NE2 . HIS A 174 ? 0.12457 0.12439 0.10208 -0.00346 -0.01146 -0.01040 69  HIS A NE2 
550  N  N   . GLY A 175 ? 0.07338 0.07021 0.06295 0.00481  -0.00485 -0.01744 70  GLY A N   
551  C  CA  . GLY A 175 ? 0.08350 0.08005 0.07626 0.00579  -0.00578 -0.01443 70  GLY A CA  
552  C  C   . GLY A 175 ? 0.07603 0.06734 0.07138 0.00753  -0.00706 -0.01410 70  GLY A C   
553  O  O   . GLY A 175 ? 0.07830 0.06730 0.07350 0.00730  -0.00849 -0.01118 70  GLY A O   
554  N  N   . THR A 176 ? 0.07465 0.06350 0.07196 0.00918  -0.00643 -0.01709 71  THR A N   
555  C  CA  . THR A 176 ? 0.07720 0.05998 0.07678 0.01074  -0.00772 -0.01633 71  THR A CA  
556  C  C   . THR A 176 ? 0.08059 0.05870 0.07742 0.00856  -0.00862 -0.01478 71  THR A C   
557  O  O   . THR A 176 ? 0.08788 0.06192 0.08469 0.00870  -0.00971 -0.01191 71  THR A O   
558  C  CB  . THR A 176 ? 0.08243 0.06320 0.08530 0.01298  -0.00657 -0.02027 71  THR A CB  
559  O  OG1 . THR A 176 ? 0.09613 0.08175 0.10342 0.01544  -0.00555 -0.02134 71  THR A OG1 
560  C  CG2 . THR A 176 ? 0.10948 0.08250 0.11450 0.01432  -0.00797 -0.01927 71  THR A CG2 
561  N  N   . HIS A 177 ? 0.07819 0.05734 0.07260 0.00632  -0.00824 -0.01644 72  HIS A N   
562  C  CA  . HIS A 177 ? 0.07719 0.05343 0.07062 0.00407  -0.00899 -0.01509 72  HIS A CA  
563  C  C   . HIS A 177 ? 0.07296 0.05040 0.06542 0.00323  -0.00936 -0.01129 72  HIS A C   
564  O  O   . HIS A 177 ? 0.07810 0.05183 0.07067 0.00263  -0.00940 -0.00920 72  HIS A O   
565  C  CB  . HIS A 177 ? 0.08797 0.06654 0.07963 0.00198  -0.00925 -0.01766 72  HIS A CB  
566  C  CG  . HIS A 177 ? 0.08111 0.05692 0.07386 -0.00024 -0.01012 -0.01755 72  HIS A CG  
567  N  ND1 . HIS A 177 ? 0.10851 0.08608 0.10179 -0.00181 -0.01070 -0.01483 72  HIS A ND1 
568  C  CD2 . HIS A 177 ? 0.09281 0.06456 0.08708 -0.00132 -0.01039 -0.02008 72  HIS A CD2 
569  C  CE1 . HIS A 177 ? 0.09299 0.06842 0.08862 -0.00376 -0.01118 -0.01552 72  HIS A CE1 
570  N  NE2 . HIS A 177 ? 0.08303 0.05474 0.07909 -0.00373 -0.01112 -0.01861 72  HIS A NE2 
571  N  N   . CYS A 178 ? 0.06956 0.05180 0.06086 0.00306  -0.00930 -0.01046 73  CYS A N   
572  C  CA  . CYS A 178 ? 0.06641 0.04927 0.05698 0.00226  -0.00948 -0.00750 73  CYS A CA  
573  C  C   . CYS A 178 ? 0.08699 0.06707 0.07742 0.00338  -0.00975 -0.00567 73  CYS A C   
574  O  O   . CYS A 178 ? 0.08789 0.06541 0.07703 0.00249  -0.00954 -0.00381 73  CYS A O   
575  C  CB  . CYS A 178 ? 0.08199 0.06972 0.07169 0.00185  -0.00940 -0.00697 73  CYS A CB  
576  S  SG  . CYS A 178 ? 0.10128 0.09193 0.08953 0.00016  -0.00989 -0.00778 73  CYS A SG  
577  N  N   . ALA A 179 ? 0.06834 0.04914 0.06008 0.00532  -0.01024 -0.00621 74  ALA A N   
578  C  CA  . ALA A 179 ? 0.07194 0.05028 0.06337 0.00648  -0.01147 -0.00416 74  ALA A CA  
579  C  C   . ALA A 179 ? 0.08400 0.05589 0.07409 0.00633  -0.01163 -0.00288 74  ALA A C   
580  O  O   . ALA A 179 ? 0.08530 0.05427 0.07244 0.00590  -0.01224 -0.00035 74  ALA A O   
581  C  CB  . ALA A 179 ? 0.08441 0.06534 0.07946 0.00898  -0.01233 -0.00512 74  ALA A CB  
582  N  N   . GLY A 180 ? 0.07694 0.04623 0.06868 0.00636  -0.01097 -0.00465 75  GLY A N   
583  C  CA  . GLY A 180 ? 0.09079 0.05349 0.08171 0.00571  -0.01081 -0.00321 75  GLY A CA  
584  C  C   . GLY A 180 ? 0.09745 0.05910 0.08583 0.00299  -0.00949 -0.00152 75  GLY A C   
585  O  O   . GLY A 180 ? 0.11087 0.06768 0.09678 0.00219  -0.00907 0.00100  75  GLY A O   
586  N  N   . THR A 181 ? 0.07657 0.04270 0.06568 0.00158  -0.00867 -0.00274 76  THR A N   
587  C  CA  . THR A 181 ? 0.07602 0.04183 0.06440 -0.00059 -0.00709 -0.00148 76  THR A CA  
588  C  C   . THR A 181 ? 0.07635 0.04190 0.06093 -0.00055 -0.00675 0.00059  76  THR A C   
589  O  O   . THR A 181 ? 0.08696 0.04999 0.06937 -0.00205 -0.00495 0.00199  76  THR A O   
590  C  CB  . THR A 181 ? 0.09822 0.06882 0.08945 -0.00162 -0.00696 -0.00314 76  THR A CB  
591  O  OG1 . THR A 181 ? 0.09116 0.06126 0.08490 -0.00220 -0.00750 -0.00529 76  THR A OG1 
592  C  CG2 . THR A 181 ? 0.10959 0.08094 0.10206 -0.00332 -0.00523 -0.00215 76  THR A CG2 
593  N  N   . VAL A 182 ? 0.08045 0.04868 0.06410 0.00087  -0.00827 0.00053  77  VAL A N   
594  C  CA  . VAL A 182 ? 0.07600 0.04356 0.05561 0.00070  -0.00858 0.00208  77  VAL A CA  
595  C  C   . VAL A 182 ? 0.08511 0.04739 0.06064 0.00093  -0.00933 0.00435  77  VAL A C   
596  O  O   . VAL A 182 ? 0.10020 0.05953 0.07092 -0.00056 -0.00807 0.00580  77  VAL A O   
597  C  CB  . VAL A 182 ? 0.07371 0.04544 0.05423 0.00185  -0.01041 0.00148  77  VAL A CB  
598  C  CG1 . VAL A 182 ? 0.10711 0.07761 0.08306 0.00124  -0.01123 0.00273  77  VAL A CG1 
599  C  CG2 . VAL A 182 ? 0.11171 0.08788 0.09498 0.00127  -0.00964 0.00011  77  VAL A CG2 
600  N  N   . GLY A 183 ? 0.08498 0.04570 0.06219 0.00282  -0.01128 0.00474  78  GLY A N   
601  C  CA  . GLY A 183 ? 0.11101 0.06732 0.08417 0.00357  -0.01326 0.00761  78  GLY A CA  
602  C  C   . GLY A 183 ? 0.13496 0.08677 0.11029 0.00538  -0.01466 0.00875  78  GLY A C   
603  O  O   . GLY A 183 ? 0.15233 0.10126 0.12529 0.00673  -0.01734 0.01143  78  GLY A O   
604  N  N   . SER A 184 ? 0.10446 0.05523 0.08423 0.00549  -0.01331 0.00683  79  SER A N   
605  C  CA  . SER A 184 ? 0.10215 0.04683 0.08372 0.00696  -0.01435 0.00801  79  SER A CA  
606  C  C   . SER A 184 ? 0.14552 0.08288 0.12192 0.00478  -0.01334 0.01173  79  SER A C   
607  O  O   . SER A 184 ? 0.13557 0.07317 0.10829 0.00187  -0.01081 0.01230  79  SER A O   
608  C  CB  . SER A 184 ? 0.11025 0.05525 0.09753 0.00723  -0.01306 0.00424  79  SER A CB  
609  O  OG  . SER A 184 ? 0.12067 0.06504 0.10756 0.00399  -0.01049 0.00334  79  SER A OG  
610  N  N   . ARG A 185 ? 0.11810 0.04871 0.09475 0.00622  -0.01503 0.01429  80  ARG A N   
611  C  CA  . ARG A 185 ? 0.12761 0.05040 0.09866 0.00404  -0.01416 0.01865  80  ARG A CA  
612  C  C   . ARG A 185 ? 0.14293 0.06391 0.11527 0.00044  -0.01006 0.01741  80  ARG A C   
613  O  O   . ARG A 185 ? 0.15541 0.07559 0.12282 -0.00273 -0.00731 0.01919  80  ARG A O   
614  C  CB  . ARG A 185 ? 0.16405 0.07948 0.13631 0.00669  -0.01723 0.02183  80  ARG A CB  
615  C  CG  . ARG A 185 ? 0.21088 0.11686 0.17691 0.00429  -0.01644 0.02720  80  ARG A CG  
616  C  CD  . ARG A 185 ? 0.31886 0.21638 0.28910 0.00670  -0.01867 0.02936  80  ARG A CD  
617  N  NE  . ARG A 185 ? 0.46307 0.35866 0.44028 0.00559  -0.01594 0.02545  80  ARG A NE  
618  C  CZ  . ARG A 185 ? 0.68217 0.56917 0.66159 0.00477  -0.01516 0.02721  80  ARG A CZ  
619  N  NH1 . ARG A 185 ? 0.68325 0.56551 0.65965 0.00531  -0.01606 0.03267  80  ARG A NH1 
620  N  NH2 . ARG A 185 ? 0.60708 0.49260 0.59242 0.00305  -0.01280 0.02298  80  ARG A NH2 
621  N  N   . THR A 186 ? 0.14271 0.06375 0.12200 0.00071  -0.00948 0.01388  81  THR A N   
622  C  CA  . THR A 186 ? 0.12518 0.04463 0.10688 -0.00290 -0.00630 0.01263  81  THR A CA  
623  C  C   . THR A 186 ? 0.15689 0.08456 0.14081 -0.00460 -0.00444 0.00917  81  THR A C   
624  O  O   . THR A 186 ? 0.16823 0.09630 0.15276 -0.00795 -0.00155 0.00937  81  THR A O   
625  C  CB  . THR A 186 ? 0.13716 0.05205 0.12504 -0.00225 -0.00694 0.01014  81  THR A CB  
626  O  OG1 . THR A 186 ? 0.16028 0.06677 0.14707 -0.00019 -0.00890 0.01370  81  THR A OG1 
627  C  CG2 . THR A 186 ? 0.17893 0.09163 0.16993 -0.00651 -0.00412 0.00899  81  THR A CG2 
628  N  N   . TYR A 187 ? 0.10829 0.04262 0.09388 -0.00243 -0.00596 0.00627  82  TYR A N   
629  C  CA  . TYR A 187 ? 0.10788 0.04921 0.09639 -0.00378 -0.00485 0.00312  82  TYR A CA  
630  C  C   . TYR A 187 ? 0.09563 0.04223 0.08104 -0.00359 -0.00446 0.00384  82  TYR A C   
631  O  O   . TYR A 187 ? 0.10770 0.05982 0.09557 -0.00439 -0.00379 0.00186  82  TYR A O   
632  C  CB  . TYR A 187 ? 0.10974 0.05446 0.10251 -0.00224 -0.00644 -0.00118 82  TYR A CB  
633  C  CG  . TYR A 187 ? 0.10314 0.04168 0.09878 -0.00213 -0.00684 -0.00253 82  TYR A CG  
634  C  CD1 . TYR A 187 ? 0.17411 0.10990 0.17270 -0.00529 -0.00559 -0.00354 82  TYR A CD1 
635  C  CD2 . TYR A 187 ? 0.11467 0.04968 0.11079 0.00105  -0.00841 -0.00260 82  TYR A CD2 
636  C  CE1 . TYR A 187 ? 0.15075 0.07965 0.15205 -0.00551 -0.00588 -0.00481 82  TYR A CE1 
637  C  CE2 . TYR A 187 ? 0.13653 0.06452 0.13577 0.00138  -0.00862 -0.00387 82  TYR A CE2 
638  C  CZ  . TYR A 187 ? 0.15484 0.07939 0.15624 -0.00204 -0.00733 -0.00497 82  TYR A CZ  
639  O  OH  . TYR A 187 ? 0.19062 0.10736 0.19536 -0.00207 -0.00750 -0.00652 82  TYR A OH  
640  N  N   . GLY A 188 ? 0.09886 0.04342 0.07882 -0.00281 -0.00497 0.00672  83  GLY A N   
641  C  CA  . GLY A 188 ? 0.11323 0.06234 0.09027 -0.00230 -0.00523 0.00670  83  GLY A CA  
642  C  C   . GLY A 188 ? 0.12318 0.07138 0.09588 -0.00468 -0.00235 0.00821  83  GLY A C   
643  O  O   . GLY A 188 ? 0.12175 0.06475 0.09087 -0.00637 -0.00064 0.01067  83  GLY A O   
644  N  N   . VAL A 189 ? 0.09274 0.04567 0.06540 -0.00476 -0.00168 0.00676  84  VAL A N   
645  C  CA  . VAL A 189 ? 0.09563 0.04806 0.06432 -0.00666 0.00146  0.00727  84  VAL A CA  
646  C  C   . VAL A 189 ? 0.12841 0.07714 0.08818 -0.00663 0.00039  0.00951  84  VAL A C   
647  O  O   . VAL A 189 ? 0.14432 0.08929 0.09802 -0.00865 0.00303  0.01117  84  VAL A O   
648  C  CB  . VAL A 189 ? 0.09049 0.04838 0.06267 -0.00638 0.00218  0.00482  84  VAL A CB  
649  C  CG1 . VAL A 189 ? 0.11217 0.06921 0.08021 -0.00791 0.00563  0.00462  84  VAL A CG1 
650  C  CG2 . VAL A 189 ? 0.09977 0.06139 0.08015 -0.00659 0.00269  0.00312  84  VAL A CG2 
651  N  N   . ALA A 190 ? 0.12165 0.07192 0.08037 -0.00462 -0.00342 0.00946  85  ALA A N   
652  C  CA  . ALA A 190 ? 0.10750 0.05560 0.05830 -0.00456 -0.00559 0.01119  85  ALA A CA  
653  C  C   . ALA A 190 ? 0.12552 0.07103 0.07627 -0.00250 -0.00968 0.01368  85  ALA A C   
654  O  O   . ALA A 190 ? 0.12379 0.07277 0.07857 -0.00024 -0.01301 0.01283  85  ALA A O   
655  C  CB  . ALA A 190 ? 0.11606 0.06884 0.06735 -0.00406 -0.00699 0.00886  85  ALA A CB  
656  N  N   . LYS A 191 ? 0.13662 0.07591 0.08312 -0.00333 -0.00922 0.01691  86  LYS A N   
657  C  CA  . LYS A 191 ? 0.12304 0.05875 0.07192 -0.00114 -0.01243 0.01926  86  LYS A CA  
658  C  C   . LYS A 191 ? 0.16167 0.09688 0.10713 0.00094  -0.01764 0.02163  86  LYS A C   
659  O  O   . LYS A 191 ? 0.18271 0.11559 0.13188 0.00356  -0.02079 0.02340  86  LYS A O   
660  C  CB  . LYS A 191 ? 0.15939 0.08781 0.10539 -0.00304 -0.01006 0.02232  86  LYS A CB  
661  C  CG  . LYS A 191 ? 0.14432 0.07411 0.09644 -0.00486 -0.00574 0.01971  86  LYS A CG  
662  C  CD  . LYS A 191 ? 0.16180 0.08440 0.11147 -0.00746 -0.00297 0.02284  86  LYS A CD  
663  C  CE  . LYS A 191 ? 0.14598 0.07083 0.10198 -0.00997 0.00142  0.02021  86  LYS A CE  
664  N  NZ  . LYS A 191 ? 0.13851 0.06670 0.10422 -0.00832 -0.00010 0.01660  86  LYS A NZ  
665  N  N   . LYS A 192 ? 0.14489 0.08228 0.08419 -0.00003 -0.01889 0.02147  87  LYS A N   
666  C  CA  . LYS A 192 ? 0.13557 0.07345 0.07211 0.00167  -0.02460 0.02356  87  LYS A CA  
667  C  C   . LYS A 192 ? 0.12743 0.07280 0.06762 0.00222  -0.02648 0.02021  87  LYS A C   
668  O  O   . LYS A 192 ? 0.16345 0.11028 0.10112 0.00290  -0.03132 0.02145  87  LYS A O   
669  C  CB  . LYS A 192 ? 0.16486 0.09696 0.08840 -0.00055 -0.02561 0.02741  87  LYS A CB  
670  C  CG  . LYS A 192 ? 0.19585 0.11988 0.11594 -0.00089 -0.02483 0.03198  87  LYS A CG  
671  C  CD  . LYS A 192 ? 0.34755 0.26648 0.25356 -0.00323 -0.02619 0.03611  87  LYS A CD  
672  C  CE  . LYS A 192 ? 0.61811 0.53058 0.52176 -0.00432 -0.02383 0.04024  87  LYS A CE  
673  N  NZ  . LYS A 192 ? 0.59772 0.50772 0.48964 -0.00828 -0.02003 0.04161  87  LYS A NZ  
674  N  N   . THR A 193 ? 0.12878 0.07895 0.07530 0.00192  -0.02326 0.01632  88  THR A N   
675  C  CA  . THR A 193 ? 0.12421 0.08092 0.07461 0.00212  -0.02471 0.01351  88  THR A CA  
676  C  C   . THR A 193 ? 0.14197 0.10313 0.10113 0.00524  -0.02831 0.01339  88  THR A C   
677  O  O   . THR A 193 ? 0.13611 0.09549 0.09951 0.00754  -0.02894 0.01458  88  THR A O   
678  C  CB  . THR A 193 ? 0.14602 0.10564 0.09994 0.00080  -0.02026 0.01018  88  THR A CB  
679  O  OG1 . THR A 193 ? 0.14589 0.11016 0.10133 0.00011  -0.02130 0.00798  88  THR A OG1 
680  C  CG2 . THR A 193 ? 0.14227 0.10426 0.10475 0.00247  -0.01877 0.00890  88  THR A CG2 
681  N  N   A GLN A 194 ? 0.10998 0.07692 0.07227 0.00523  -0.03056 0.01176  89  GLN A N   
682  N  N   B GLN A 194 ? 0.11024 0.07718 0.07254 0.00519  -0.03044 0.01171  89  GLN A N   
683  C  CA  A GLN A 194 ? 0.11989 0.09276 0.09201 0.00786  -0.03298 0.01092  89  GLN A CA  
684  C  CA  B GLN A 194 ? 0.12104 0.09388 0.09307 0.00779  -0.03282 0.01085  89  GLN A CA  
685  C  C   A GLN A 194 ? 0.10604 0.08364 0.08452 0.00754  -0.02917 0.00766  89  GLN A C   
686  C  C   B GLN A 194 ? 0.10665 0.08395 0.08493 0.00750  -0.02891 0.00764  89  GLN A C   
687  O  O   A GLN A 194 ? 0.14112 0.12010 0.11762 0.00515  -0.02721 0.00606  89  GLN A O   
688  O  O   B GLN A 194 ? 0.13162 0.10969 0.10755 0.00510  -0.02651 0.00610  89  GLN A O   
689  C  CB  A GLN A 194 ? 0.13276 0.10992 0.10555 0.00763  -0.03781 0.01119  89  GLN A CB  
690  C  CB  B GLN A 194 ? 0.13275 0.10983 0.10524 0.00744  -0.03754 0.01107  89  GLN A CB  
691  C  CG  A GLN A 194 ? 0.18197 0.16723 0.16641 0.00951  -0.03899 0.00941  89  GLN A CG  
692  C  CG  B GLN A 194 ? 0.14396 0.11729 0.11115 0.00838  -0.04269 0.01479  89  GLN A CG  
693  C  CD  A GLN A 194 ? 0.27420 0.26034 0.26585 0.01357  -0.04185 0.01100  89  GLN A CD  
694  C  CD  B GLN A 194 ? 0.23858 0.21301 0.21406 0.01251  -0.04581 0.01665  89  GLN A CD  
695  O  OE1 A GLN A 194 ? 0.36865 0.35140 0.35710 0.01480  -0.04627 0.01422  89  GLN A OE1 
696  O  OE1 B GLN A 194 ? 0.35579 0.33714 0.34196 0.01446  -0.04659 0.01479  89  GLN A OE1 
697  N  NE2 A GLN A 194 ? 0.14891 0.13940 0.15017 0.01572  -0.03935 0.00877  89  GLN A NE2 
698  N  NE2 B GLN A 194 ? 0.22866 0.19611 0.19962 0.01386  -0.04740 0.02038  89  GLN A NE2 
699  N  N   . LEU A 195 ? 0.08657 0.06629 0.07233 0.00993  -0.02818 0.00667  90  LEU A N   
700  C  CA  . LEU A 195 ? 0.07944 0.06323 0.06984 0.00955  -0.02462 0.00386  90  LEU A CA  
701  C  C   . LEU A 195 ? 0.09896 0.09019 0.09743 0.01080  -0.02552 0.00237  90  LEU A C   
702  O  O   . LEU A 195 ? 0.12317 0.11600 0.12703 0.01358  -0.02775 0.00275  90  LEU A O   
703  C  CB  . LEU A 195 ? 0.07903 0.05974 0.07085 0.01079  -0.02214 0.00305  90  LEU A CB  
704  C  CG  . LEU A 195 ? 0.14725 0.12148 0.13260 0.00908  -0.02054 0.00431  90  LEU A CG  
705  C  CD1 . LEU A 195 ? 0.23904 0.20884 0.22624 0.01058  -0.01973 0.00427  90  LEU A CD1 
706  C  CD2 . LEU A 195 ? 0.22546 0.20080 0.20875 0.00655  -0.01759 0.00300  90  LEU A CD2 
707  N  N   . PHE A 196 ? 0.07562 0.07131 0.07550 0.00878  -0.02359 0.00082  91  PHE A N   
708  C  CA  . PHE A 196 ? 0.08004 0.08330 0.08769 0.00921  -0.02337 -0.00065 91  PHE A CA  
709  C  C   . PHE A 196 ? 0.09872 0.10419 0.10768 0.00857  -0.01908 -0.00254 91  PHE A C   
710  O  O   . PHE A 196 ? 0.11235 0.11578 0.11672 0.00634  -0.01720 -0.00242 91  PHE A O   
711  C  CB  . PHE A 196 ? 0.07718 0.08375 0.08507 0.00666  -0.02511 -0.00043 91  PHE A CB  
712  C  CG  . PHE A 196 ? 0.11156 0.11690 0.11760 0.00683  -0.02994 0.00113  91  PHE A CG  
713  C  CD1 . PHE A 196 ? 0.14929 0.15684 0.16069 0.00979  -0.03332 0.00201  91  PHE A CD1 
714  C  CD2 . PHE A 196 ? 0.15582 0.15783 0.15474 0.00403  -0.03124 0.00158  91  PHE A CD2 
715  C  CE1 . PHE A 196 ? 0.17177 0.17827 0.18082 0.00991  -0.03872 0.00397  91  PHE A CE1 
716  C  CE2 . PHE A 196 ? 0.22213 0.22296 0.21778 0.00384  -0.03612 0.00290  91  PHE A CE2 
717  C  CZ  . PHE A 196 ? 0.17182 0.17503 0.17230 0.00671  -0.04012 0.00436  91  PHE A CZ  
718  N  N   . GLY A 197 ? 0.07178 0.08145 0.08690 0.01054  -0.01753 -0.00432 92  GLY A N   
719  C  CA  . GLY A 197 ? 0.06628 0.07797 0.08111 0.00973  -0.01349 -0.00624 92  GLY A CA  
720  C  C   . GLY A 197 ? 0.07230 0.09120 0.09133 0.00801  -0.01156 -0.00694 92  GLY A C   
721  O  O   . GLY A 197 ? 0.08949 0.11392 0.11581 0.00897  -0.01236 -0.00743 92  GLY A O   
722  N  N   . VAL A 198 ? 0.05919 0.07808 0.07397 0.00535  -0.00912 -0.00668 93  VAL A N   
723  C  CA  . VAL A 198 ? 0.06028 0.08515 0.07774 0.00313  -0.00650 -0.00687 93  VAL A CA  
724  C  C   . VAL A 198 ? 0.07685 0.10211 0.09058 0.00271  -0.00290 -0.00818 93  VAL A C   
725  O  O   . VAL A 198 ? 0.08689 0.10768 0.09412 0.00165  -0.00301 -0.00724 93  VAL A O   
726  C  CB  . VAL A 198 ? 0.06824 0.09183 0.08329 -0.00011 -0.00750 -0.00462 93  VAL A CB  
727  C  CG1 . VAL A 198 ? 0.10908 0.13832 0.12714 -0.00275 -0.00464 -0.00433 93  VAL A CG1 
728  C  CG2 . VAL A 198 ? 0.16279 0.18537 0.17988 0.00007  -0.01137 -0.00392 93  VAL A CG2 
729  N  N   . LYS A 199 ? 0.06193 0.09260 0.07983 0.00363  0.00018  -0.01059 94  LYS A N   
730  C  CA  . LYS A 199 ? 0.07099 0.10189 0.08407 0.00319  0.00365  -0.01249 94  LYS A CA  
731  C  C   . LYS A 199 ? 0.07431 0.10860 0.08429 -0.00046 0.00643  -0.01085 94  LYS A C   
732  O  O   . LYS A 199 ? 0.08925 0.12997 0.10378 -0.00136 0.00966  -0.01171 94  LYS A O   
733  C  CB  . LYS A 199 ? 0.07978 0.11394 0.09804 0.00612  0.00614  -0.01651 94  LYS A CB  
734  C  CG  . LYS A 199 ? 0.07274 0.10688 0.08486 0.00546  0.00989  -0.01938 94  LYS A CG  
735  C  CD  . LYS A 199 ? 0.07614 0.11209 0.09383 0.00892  0.01240  -0.02424 94  LYS A CD  
736  C  CE  . LYS A 199 ? 0.11548 0.15215 0.12656 0.00784  0.01678  -0.02797 94  LYS A CE  
737  N  NZ  . LYS A 199 ? 0.10953 0.13945 0.11033 0.00630  0.01449  -0.02751 94  LYS A NZ  
738  N  N   . VAL A 200 ? 0.08076 0.11074 0.08355 -0.00260 0.00521  -0.00822 95  VAL A N   
739  C  CA  . VAL A 200 ? 0.07610 0.10779 0.07455 -0.00604 0.00744  -0.00591 95  VAL A CA  
740  C  C   . VAL A 200 ? 0.07566 0.10644 0.06592 -0.00672 0.00913  -0.00681 95  VAL A C   
741  O  O   . VAL A 200 ? 0.09716 0.12962 0.08257 -0.00959 0.01130  -0.00482 95  VAL A O   
742  C  CB  . VAL A 200 ? 0.07413 0.10162 0.07052 -0.00810 0.00477  -0.00185 95  VAL A CB  
743  C  CG1 . VAL A 200 ? 0.09891 0.12708 0.10222 -0.00825 0.00296  -0.00119 95  VAL A CG1 
744  C  CG2 . VAL A 200 ? 0.10889 0.13018 0.10047 -0.00695 0.00174  -0.00125 95  VAL A CG2 
745  N  N   . LEU A 201 ? 0.09478 0.12266 0.08285 -0.00451 0.00801  -0.00956 96  LEU A N   
746  C  CA  . LEU A 201 ? 0.09546 0.12260 0.07549 -0.00536 0.00914  -0.01116 96  LEU A CA  
747  C  C   . LEU A 201 ? 0.11069 0.14083 0.09239 -0.00359 0.01265  -0.01643 96  LEU A C   
748  O  O   . LEU A 201 ? 0.11411 0.14393 0.10284 -0.00059 0.01224  -0.01887 96  LEU A O   
749  C  CB  . LEU A 201 ? 0.11705 0.13844 0.09340 -0.00473 0.00516  -0.01077 96  LEU A CB  
750  C  CG  . LEU A 201 ? 0.12615 0.14426 0.10206 -0.00584 0.00181  -0.00615 96  LEU A CG  
751  C  CD1 . LEU A 201 ? 0.14282 0.15626 0.11713 -0.00502 -0.00166 -0.00628 96  LEU A CD1 
752  C  CD2 . LEU A 201 ? 0.16535 0.18479 0.13613 -0.00880 0.00248  -0.00250 96  LEU A CD2 
753  N  N   . ASP A 202 ? 0.12177 0.15418 0.09645 -0.00539 0.01592  -0.01821 97  ASP A N   
754  C  CA  . ASP A 202 ? 0.11936 0.15441 0.09516 -0.00374 0.01999  -0.02406 97  ASP A CA  
755  C  C   . ASP A 202 ? 0.13156 0.16125 0.10505 -0.00183 0.01764  -0.02772 97  ASP A C   
756  O  O   . ASP A 202 ? 0.13378 0.15849 0.10588 -0.00181 0.01302  -0.02549 97  ASP A O   
757  C  CB  . ASP A 202 ? 0.12270 0.16227 0.09101 -0.00674 0.02506  -0.02497 97  ASP A CB  
758  C  CG  . ASP A 202 ? 0.24623 0.28267 0.20126 -0.00954 0.02336  -0.02391 97  ASP A CG  
759  O  OD1 . ASP A 202 ? 0.17868 0.21010 0.13075 -0.00881 0.01903  -0.02451 97  ASP A OD1 
760  O  OD2 . ASP A 202 ? 0.27164 0.31109 0.21885 -0.01277 0.02661  -0.02255 97  ASP A OD2 
761  N  N   . ASP A 203 ? 0.12267 0.15322 0.09699 -0.00013 0.02105  -0.03367 98  ASP A N   
762  C  CA  . ASP A 203 ? 0.14036 0.16522 0.11432 0.00176  0.01895  -0.03752 98  ASP A CA  
763  C  C   . ASP A 203 ? 0.19016 0.21199 0.15274 -0.00108 0.01704  -0.03826 98  ASP A C   
764  O  O   . ASP A 203 ? 0.18516 0.20207 0.14695 -0.00033 0.01482  -0.04125 98  ASP A O   
765  C  CB  . ASP A 203 ? 0.12482 0.15080 0.10457 0.00485  0.02312  -0.04393 98  ASP A CB  
766  C  CG  . ASP A 203 ? 0.15706 0.18474 0.14987 0.00852  0.02301  -0.04306 98  ASP A CG  
767  O  OD1 . ASP A 203 ? 0.13557 0.16135 0.13211 0.00894  0.01879  -0.03826 98  ASP A OD1 
768  O  OD2 . ASP A 203 ? 0.19375 0.22489 0.19338 0.01108  0.02714  -0.04735 98  ASP A OD2 
769  N  N   . ASN A 204 ? 0.19178 0.21633 0.14567 -0.00449 0.01752  -0.03540 99  ASN A N   
770  C  CA  . ASN A 204 ? 0.20337 0.22524 0.14710 -0.00721 0.01396  -0.03448 99  ASN A CA  
771  C  C   . ASN A 204 ? 0.26159 0.28125 0.20650 -0.00799 0.00863  -0.02808 99  ASN A C   
772  O  O   . ASN A 204 ? 0.26752 0.28551 0.20572 -0.01002 0.00494  -0.02651 99  ASN A O   
773  C  CB  . ASN A 204 ? 0.27214 0.29758 0.20436 -0.01057 0.01694  -0.03463 99  ASN A CB  
774  C  CG  . ASN A 204 ? 0.34171 0.36878 0.27084 -0.01015 0.02237  -0.04214 99  ASN A CG  
775  O  OD1 . ASN A 204 ? 0.41540 0.43889 0.34552 -0.00863 0.02170  -0.04768 99  ASN A OD1 
776  N  ND2 . ASN A 204 ? 0.37283 0.40512 0.29873 -0.01155 0.02819  -0.04262 99  ASN A ND2 
777  N  N   . GLY A 205 ? 0.16102 0.18077 0.11450 -0.00640 0.00804  -0.02461 100 GLY A N   
778  C  CA  . GLY A 205 ? 0.15688 0.17432 0.11196 -0.00692 0.00370  -0.01924 100 GLY A CA  
779  C  C   . GLY A 205 ? 0.25820 0.27773 0.20974 -0.00927 0.00360  -0.01386 100 GLY A C   
780  O  O   . GLY A 205 ? 0.26878 0.28609 0.22108 -0.00974 -0.00003 -0.00959 100 GLY A O   
781  N  N   . SER A 206 ? 0.19642 0.21996 0.14457 -0.01080 0.00773  -0.01393 101 SER A N   
782  C  CA  . SER A 206 ? 0.21771 0.24268 0.16143 -0.01361 0.00803  -0.00852 101 SER A CA  
783  C  C   . SER A 206 ? 0.24026 0.26806 0.19154 -0.01353 0.01101  -0.00674 101 SER A C   
784  O  O   . SER A 206 ? 0.20041 0.23085 0.15865 -0.01165 0.01384  -0.01027 101 SER A O   
785  C  CB  . SER A 206 ? 0.31615 0.34361 0.24851 -0.01648 0.01083  -0.00926 101 SER A CB  
786  O  OG  . SER A 206 ? 0.62845 0.65406 0.55361 -0.01671 0.00848  -0.01243 101 SER A OG  
787  N  N   . GLY A 207 ? 0.26611 0.29338 0.21631 -0.01572 0.01020  -0.00119 102 GLY A N   
788  C  CA  . GLY A 207 ? 0.17686 0.20681 0.13398 -0.01646 0.01282  0.00059  102 GLY A CA  
789  C  C   . GLY A 207 ? 0.21469 0.24312 0.16829 -0.01964 0.01223  0.00681  102 GLY A C   
790  O  O   . GLY A 207 ? 0.29238 0.31642 0.24191 -0.01997 0.00814  0.01033  102 GLY A O   
791  N  N   . GLN A 208 ? 0.16885 0.20086 0.12470 -0.02198 0.01625  0.00826  103 GLN A N   
792  C  CA  . GLN A 208 ? 0.17603 0.20606 0.12942 -0.02535 0.01618  0.01441  103 GLN A CA  
793  C  C   . GLN A 208 ? 0.15380 0.17998 0.11528 -0.02464 0.01285  0.01682  103 GLN A C   
794  O  O   . GLN A 208 ? 0.15388 0.18104 0.12383 -0.02249 0.01223  0.01377  103 GLN A O   
795  C  CB  . GLN A 208 ? 0.24399 0.27940 0.19779 -0.02866 0.02224  0.01499  103 GLN A CB  
796  C  CG  . GLN A 208 ? 0.45668 0.49726 0.40489 -0.02897 0.02712  0.01074  103 GLN A CG  
797  C  CD  . GLN A 208 ? 0.90633 0.94921 0.84661 -0.03368 0.03196  0.01430  103 GLN A CD  
798  O  OE1 . GLN A 208 ? 0.85671 0.90152 0.80218 -0.03647 0.03476  0.01731  103 GLN A OE1 
799  N  NE2 . GLN A 208 ? 0.70944 0.75175 0.63648 -0.03499 0.03279  0.01425  103 GLN A NE2 
800  N  N   . TYR A 209 ? 0.14915 0.17060 0.10757 -0.02656 0.01066  0.02244  104 TYR A N   
801  C  CA  . TYR A 209 ? 0.13287 0.14973 0.09834 -0.02588 0.00764  0.02430  104 TYR A CA  
802  C  C   . TYR A 209 ? 0.12762 0.14737 0.10191 -0.02724 0.01017  0.02303  104 TYR A C   
803  O  O   . TYR A 209 ? 0.13927 0.15721 0.12037 -0.02557 0.00794  0.02125  104 TYR A O   
804  C  CB  . TYR A 209 ? 0.17271 0.18373 0.13380 -0.02763 0.00520  0.03065  104 TYR A CB  
805  C  CG  . TYR A 209 ? 0.23572 0.24255 0.19399 -0.02493 0.00023  0.03156  104 TYR A CG  
806  C  CD1 . TYR A 209 ? 0.25147 0.25897 0.21272 -0.02151 -0.00167 0.02686  104 TYR A CD1 
807  C  CD2 . TYR A 209 ? 0.18061 0.18280 0.13442 -0.02584 -0.00269 0.03736  104 TYR A CD2 
808  C  CE1 . TYR A 209 ? 0.35187 0.35626 0.31219 -0.01932 -0.00597 0.02754  104 TYR A CE1 
809  C  CE2 . TYR A 209 ? 0.25680 0.25606 0.21004 -0.02318 -0.00757 0.03814  104 TYR A CE2 
810  C  CZ  . TYR A 209 ? 0.36069 0.36145 0.31749 -0.02010 -0.00894 0.03303  104 TYR A CZ  
811  O  OH  . TYR A 209 ? 0.30757 0.30618 0.26526 -0.01781 -0.01338 0.03369  104 TYR A OH  
812  N  N   . SER A 210 ? 0.15780 0.18240 0.13211 -0.03041 0.01483  0.02369  105 SER A N   
813  C  CA  . SER A 210 ? 0.17033 0.19873 0.15433 -0.03203 0.01698  0.02239  105 SER A CA  
814  C  C   . SER A 210 ? 0.13492 0.16735 0.12632 -0.02856 0.01614  0.01671  105 SER A C   
815  O  O   . SER A 210 ? 0.13734 0.17006 0.13685 -0.02853 0.01456  0.01559  105 SER A O   
816  C  CB  . SER A 210 ? 0.17008 0.20420 0.15334 -0.03610 0.02283  0.02377  105 SER A CB  
817  O  OG  . SER A 210 ? 0.32072 0.36011 0.29949 -0.03484 0.02606  0.02041  105 SER A OG  
818  N  N   . THR A 211 ? 0.10736 0.14234 0.09576 -0.02569 0.01679  0.01314  106 THR A N   
819  C  CA  . THR A 211 ? 0.09579 0.13378 0.09094 -0.02212 0.01580  0.00827  106 THR A CA  
820  C  C   . THR A 211 ? 0.11489 0.14684 0.11081 -0.01949 0.01061  0.00805  106 THR A C   
821  O  O   . THR A 211 ? 0.10726 0.14002 0.10988 -0.01786 0.00871  0.00596  106 THR A O   
822  C  CB  . THR A 211 ? 0.11578 0.15710 0.10728 -0.02006 0.01833  0.00457  106 THR A CB  
823  O  OG1 . THR A 211 ? 0.20886 0.25631 0.19981 -0.02273 0.02403  0.00436  106 THR A OG1 
824  C  CG2 . THR A 211 ? 0.14488 0.18828 0.14365 -0.01608 0.01703  0.00005  106 THR A CG2 
825  N  N   . ILE A 212 ? 0.08473 0.11087 0.07378 -0.01906 0.00824  0.01019  107 ILE A N   
826  C  CA  . ILE A 212 ? 0.07637 0.09712 0.06629 -0.01677 0.00414  0.00990  107 ILE A CA  
827  C  C   . ILE A 212 ? 0.11159 0.12966 0.10646 -0.01819 0.00266  0.01140  107 ILE A C   
828  O  O   . ILE A 212 ? 0.11099 0.12750 0.10944 -0.01658 0.00044  0.00946  107 ILE A O   
829  C  CB  . ILE A 212 ? 0.10395 0.12015 0.08692 -0.01625 0.00214  0.01199  107 ILE A CB  
830  C  CG1 . ILE A 212 ? 0.13521 0.15363 0.11379 -0.01464 0.00284  0.00915  107 ILE A CG1 
831  C  CG2 . ILE A 212 ? 0.15690 0.16774 0.14193 -0.01452 -0.00127 0.01223  107 ILE A CG2 
832  C  CD1 . ILE A 212 ? 0.19636 0.21243 0.16689 -0.01536 0.00132  0.01154  107 ILE A CD1 
833  N  N   . ILE A 213 ? 0.09640 0.11372 0.09116 -0.02154 0.00399  0.01479  108 ILE A N   
834  C  CA  . ILE A 213 ? 0.07925 0.09378 0.07900 -0.02346 0.00288  0.01576  108 ILE A CA  
835  C  C   . ILE A 213 ? 0.09832 0.11817 0.10537 -0.02368 0.00318  0.01254  108 ILE A C   
836  O  O   . ILE A 213 ? 0.08530 0.10293 0.09567 -0.02319 0.00058  0.01096  108 ILE A O   
837  C  CB  . ILE A 213 ? 0.08619 0.09878 0.08468 -0.02737 0.00465  0.02027  108 ILE A CB  
838  C  CG1 . ILE A 213 ? 0.10989 0.11581 0.10235 -0.02669 0.00276  0.02400  108 ILE A CG1 
839  C  CG2 . ILE A 213 ? 0.09687 0.10755 0.10195 -0.03018 0.00419  0.02051  108 ILE A CG2 
840  C  CD1 . ILE A 213 ? 0.16502 0.16903 0.15424 -0.03030 0.00449  0.02936  108 ILE A CD1 
841  N  N   . ALA A 214 ? 0.07622 0.10345 0.08597 -0.02435 0.00626  0.01136  109 ALA A N   
842  C  CA  . ALA A 214 ? 0.07430 0.10756 0.09267 -0.02424 0.00605  0.00843  109 ALA A CA  
843  C  C   . ALA A 214 ? 0.09652 0.12880 0.11594 -0.02030 0.00253  0.00541  109 ALA A C   
844  O  O   . ALA A 214 ? 0.08532 0.11862 0.11004 -0.02033 -0.00013 0.00395  109 ALA A O   
845  C  CB  . ALA A 214 ? 0.08848 0.13044 0.11051 -0.02496 0.01051  0.00727  109 ALA A CB  
846  N  N   . GLY A 215 ? 0.06673 0.09683 0.08086 -0.01719 0.00224  0.00458  110 GLY A N   
847  C  CA  . GLY A 215 ? 0.07960 0.10795 0.09405 -0.01371 -0.00076 0.00231  110 GLY A CA  
848  C  C   . GLY A 215 ? 0.11843 0.14031 0.13089 -0.01387 -0.00411 0.00293  110 GLY A C   
849  O  O   . GLY A 215 ? 0.09854 0.12005 0.11290 -0.01248 -0.00679 0.00138  110 GLY A O   
850  N  N   . MET A 216 ? 0.06889 0.08548 0.07745 -0.01554 -0.00397 0.00522  111 MET A N   
851  C  CA  . MET A 216 ? 0.06664 0.07713 0.07401 -0.01578 -0.00639 0.00518  111 MET A CA  
852  C  C   . MET A 216 ? 0.08176 0.09357 0.09399 -0.01827 -0.00764 0.00428  111 MET A C   
853  O  O   . MET A 216 ? 0.09357 0.10324 0.10565 -0.01778 -0.01026 0.00246  111 MET A O   
854  C  CB  . MET A 216 ? 0.09002 0.09487 0.09380 -0.01660 -0.00583 0.00779  111 MET A CB  
855  C  CG  . MET A 216 ? 0.07746 0.08047 0.07686 -0.01393 -0.00600 0.00802  111 MET A CG  
856  S  SD  . MET A 216 ? 0.16558 0.16199 0.16276 -0.01432 -0.00647 0.01109  111 MET A SD  
857  C  CE  . MET A 216 ? 0.19766 0.19703 0.19159 -0.01544 -0.00502 0.01424  111 MET A CE  
858  N  N   . ASP A 217 ? 0.07258 0.08792 0.08881 -0.02132 -0.00583 0.00551  112 ASP A N   
859  C  CA  . ASP A 217 ? 0.07176 0.08878 0.09355 -0.02418 -0.00729 0.00440  112 ASP A CA  
860  C  C   . ASP A 217 ? 0.09448 0.11757 0.12073 -0.02257 -0.00953 0.00181  112 ASP A C   
861  O  O   . ASP A 217 ? 0.07300 0.09603 0.10167 -0.02375 -0.01269 0.00016  112 ASP A O   
862  C  CB  . ASP A 217 ? 0.07378 0.09395 0.09998 -0.02822 -0.00449 0.00643  112 ASP A CB  
863  C  CG  . ASP A 217 ? 0.15235 0.16531 0.17477 -0.03034 -0.00308 0.00972  112 ASP A CG  
864  O  OD1 . ASP A 217 ? 0.25361 0.25929 0.27321 -0.02973 -0.00499 0.00938  112 ASP A OD1 
865  O  OD2 . ASP A 217 ? 0.28720 0.30235 0.31016 -0.03269 -0.00000 0.01250  112 ASP A OD2 
866  N  N   . PHE A 218 ? 0.07480 0.10305 0.10229 -0.01983 -0.00821 0.00134  113 PHE A N   
867  C  CA  . PHE A 218 ? 0.09147 0.12482 0.12380 -0.01757 -0.01075 -0.00073 113 PHE A CA  
868  C  C   . PHE A 218 ? 0.08064 0.10845 0.10799 -0.01552 -0.01480 -0.00163 113 PHE A C   
869  O  O   . PHE A 218 ? 0.08327 0.11306 0.11358 -0.01561 -0.01852 -0.00279 113 PHE A O   
870  C  CB  . PHE A 218 ? 0.07723 0.11549 0.11136 -0.01451 -0.00818 -0.00136 113 PHE A CB  
871  C  CG  . PHE A 218 ? 0.06825 0.11019 0.10716 -0.01118 -0.01111 -0.00311 113 PHE A CG  
872  C  CD1 . PHE A 218 ? 0.16076 0.21095 0.20991 -0.01163 -0.01206 -0.00416 113 PHE A CD1 
873  C  CD2 . PHE A 218 ? 0.08916 0.12615 0.12287 -0.00780 -0.01318 -0.00339 113 PHE A CD2 
874  C  CE1 . PHE A 218 ? 0.15479 0.20820 0.20905 -0.00816 -0.01555 -0.00530 113 PHE A CE1 
875  C  CE2 . PHE A 218 ? 0.11337 0.15286 0.15141 -0.00469 -0.01647 -0.00430 113 PHE A CE2 
876  C  CZ  . PHE A 218 ? 0.13462 0.18221 0.18284 -0.00475 -0.01774 -0.00514 113 PHE A CZ  
877  N  N   . VAL A 219 ? 0.06338 0.08464 0.08318 -0.01379 -0.01419 -0.00103 114 VAL A N   
878  C  CA  . VAL A 219 ? 0.06344 0.07944 0.07795 -0.01210 -0.01716 -0.00175 114 VAL A CA  
879  C  C   . VAL A 219 ? 0.06716 0.07970 0.08011 -0.01487 -0.01948 -0.00261 114 VAL A C   
880  O  O   . VAL A 219 ? 0.08795 0.09923 0.09863 -0.01451 -0.02289 -0.00369 114 VAL A O   
881  C  CB  . VAL A 219 ? 0.07605 0.08636 0.08407 -0.01025 -0.01541 -0.00102 114 VAL A CB  
882  C  CG1 . VAL A 219 ? 0.11364 0.11831 0.11594 -0.00921 -0.01754 -0.00164 114 VAL A CG1 
883  C  CG2 . VAL A 219 ? 0.12631 0.13978 0.13551 -0.00773 -0.01365 -0.00092 114 VAL A CG2 
884  N  N   . ALA A 220 ? 0.06865 0.07892 0.08213 -0.01780 -0.01774 -0.00215 115 ALA A N   
885  C  CA  . ALA A 220 ? 0.07557 0.08153 0.08749 -0.02055 -0.01962 -0.00365 115 ALA A CA  
886  C  C   . ALA A 220 ? 0.09692 0.10796 0.11354 -0.02236 -0.02326 -0.00523 115 ALA A C   
887  O  O   . ALA A 220 ? 0.15398 0.16190 0.16718 -0.02365 -0.02633 -0.00718 115 ALA A O   
888  C  CB  . ALA A 220 ? 0.10614 0.10866 0.11945 -0.02342 -0.01708 -0.00262 115 ALA A CB  
889  N  N   . SER A 221 ? 0.07801 0.09728 0.10267 -0.02260 -0.02297 -0.00460 116 SER A N   
890  C  CA  . SER A 221 ? 0.07433 0.10003 0.10549 -0.02394 -0.02686 -0.00596 116 SER A CA  
891  C  C   . SER A 221 ? 0.10976 0.13797 0.14009 -0.02023 -0.03052 -0.00617 116 SER A C   
892  O  O   . SER A 221 ? 0.10839 0.13758 0.13855 -0.02093 -0.03555 -0.00733 116 SER A O   
893  C  CB  . SER A 221 ? 0.07460 0.10882 0.11629 -0.02580 -0.02447 -0.00527 116 SER A CB  
894  O  OG  . SER A 221 ? 0.09965 0.14159 0.14997 -0.02710 -0.02837 -0.00664 116 SER A OG  
895  N  N   . ASP A 222 ? 0.06997 0.09951 0.10029 -0.01643 -0.02837 -0.00498 117 ASP A N   
896  C  CA  . ASP A 222 ? 0.07006 0.10223 0.10162 -0.01279 -0.03166 -0.00478 117 ASP A CA  
897  C  C   . ASP A 222 ? 0.09797 0.12321 0.11989 -0.01203 -0.03533 -0.00475 117 ASP A C   
898  O  O   . ASP A 222 ? 0.11034 0.13751 0.13299 -0.01034 -0.03998 -0.00437 117 ASP A O   
899  C  CB  . ASP A 222 ? 0.07115 0.10418 0.10353 -0.00914 -0.02800 -0.00398 117 ASP A CB  
900  C  CG  . ASP A 222 ? 0.09717 0.13245 0.13232 -0.00501 -0.03107 -0.00365 117 ASP A CG  
901  O  OD1 . ASP A 222 ? 0.11674 0.15991 0.16184 -0.00432 -0.03302 -0.00412 117 ASP A OD1 
902  O  OD2 . ASP A 222 ? 0.10639 0.13541 0.13428 -0.00267 -0.03151 -0.00282 117 ASP A OD2 
903  N  N   . LYS A 223 ? 0.09079 0.10804 0.10374 -0.01313 -0.03323 -0.00496 118 LYS A N   
904  C  CA  . LYS A 223 ? 0.09587 0.10661 0.09898 -0.01255 -0.03568 -0.00505 118 LYS A CA  
905  C  C   . LYS A 223 ? 0.13676 0.14850 0.13860 -0.01496 -0.04106 -0.00635 118 LYS A C   
906  O  O   . LYS A 223 ? 0.18944 0.19809 0.18408 -0.01412 -0.04455 -0.00590 118 LYS A O   
907  C  CB  . LYS A 223 ? 0.12436 0.12728 0.11983 -0.01351 -0.03184 -0.00560 118 LYS A CB  
908  C  CG  . LYS A 223 ? 0.23075 0.23190 0.22680 -0.01751 -0.03132 -0.00760 118 LYS A CG  
909  C  CD  . LYS A 223 ? 0.29086 0.28413 0.27992 -0.01808 -0.02832 -0.00857 118 LYS A CD  
910  C  CE  . LYS A 223 ? 0.24659 0.23634 0.23461 -0.02173 -0.02864 -0.01119 118 LYS A CE  
911  N  NZ  . LYS A 223 ? 0.24453 0.23787 0.24106 -0.02399 -0.02785 -0.01085 118 LYS A NZ  
912  N  N   . ASN A 224 ? 0.14406 0.16025 0.15270 -0.01817 -0.04205 -0.00781 119 ASN A N   
913  C  CA  . ASN A 224 ? 0.16623 0.18395 0.17421 -0.02091 -0.04780 -0.00948 119 ASN A CA  
914  C  C   . ASN A 224 ? 0.20442 0.22926 0.21807 -0.01868 -0.05346 -0.00810 119 ASN A C   
915  O  O   . ASN A 224 ? 0.31029 0.33654 0.32237 -0.02052 -0.05945 -0.00903 119 ASN A O   
916  C  CB  . ASN A 224 ? 0.17504 0.19521 0.18969 -0.02549 -0.04707 -0.01156 119 ASN A CB  
917  C  CG  . ASN A 224 ? 0.31608 0.32853 0.32612 -0.02746 -0.04183 -0.01258 119 ASN A CG  
918  O  OD1 . ASN A 224 ? 0.23050 0.24466 0.24730 -0.02940 -0.03855 -0.01230 119 ASN A OD1 
919  N  ND2 . ASN A 224 ? 0.29927 0.30329 0.29827 -0.02708 -0.04100 -0.01363 119 ASN A ND2 
920  N  N   A ASN A 225 ? 0.18610 0.21525 0.20628 -0.01472 -0.05201 -0.00608 120 ASN A N   
921  N  N   B ASN A 225 ? 0.18684 0.21617 0.20727 -0.01475 -0.05202 -0.00610 120 ASN A N   
922  C  CA  A ASN A 225 ? 0.24131 0.27692 0.26840 -0.01172 -0.05706 -0.00459 120 ASN A CA  
923  C  CA  B ASN A 225 ? 0.24169 0.27711 0.26837 -0.01180 -0.05732 -0.00460 120 ASN A CA  
924  C  C   A ASN A 225 ? 0.22518 0.25520 0.24414 -0.00781 -0.05879 -0.00211 120 ASN A C   
925  C  C   B ASN A 225 ? 0.22574 0.25600 0.24570 -0.00743 -0.05773 -0.00208 120 ASN A C   
926  O  O   A ASN A 225 ? 0.25106 0.28504 0.27513 -0.00475 -0.06337 -0.00031 120 ASN A O   
927  O  O   B ASN A 225 ? 0.20912 0.24372 0.23609 -0.00368 -0.06015 -0.00040 120 ASN A O   
928  C  CB  A ASN A 225 ? 0.24127 0.28584 0.28279 -0.00974 -0.05403 -0.00444 120 ASN A CB  
929  C  CB  B ASN A 225 ? 0.26190 0.30785 0.30453 -0.01076 -0.05582 -0.00479 120 ASN A CB  
930  C  CG  A ASN A 225 ? 0.23245 0.28294 0.28267 -0.01391 -0.05168 -0.00631 120 ASN A CG  
931  C  CG  B ASN A 225 ? 0.18376 0.22948 0.22884 -0.00817 -0.04880 -0.00430 120 ASN A CG  
932  O  OD1 A ASN A 225 ? 0.39720 0.44762 0.44655 -0.01810 -0.05465 -0.00781 120 ASN A OD1 
933  O  OD1 B ASN A 225 ? 0.28223 0.32311 0.32198 -0.00469 -0.04754 -0.00297 120 ASN A OD1 
934  N  ND2 A ASN A 225 ? 0.37993 0.43486 0.43774 -0.01312 -0.04597 -0.00628 120 ASN A ND2 
935  N  ND2 B ASN A 225 ? 0.10783 0.15888 0.16092 -0.01020 -0.04426 -0.00536 120 ASN A ND2 
936  N  N   . ARG A 226 ? 0.17330 0.19428 0.18055 -0.00786 -0.05525 -0.00182 121 ARG A N   
937  C  CA  . ARG A 226 ? 0.15520 0.17045 0.15542 -0.00451 -0.05528 0.00069  121 ARG A CA  
938  C  C   . ARG A 226 ? 0.21376 0.22152 0.19975 -0.00644 -0.05785 0.00106  121 ARG A C   
939  O  O   . ARG A 226 ? 0.23695 0.24190 0.21704 -0.01014 -0.05698 -0.00138 121 ARG A O   
940  C  CB  . ARG A 226 ? 0.15491 0.16613 0.15357 -0.00302 -0.04851 0.00080  121 ARG A CB  
941  C  CG  . ARG A 226 ? 0.21465 0.23200 0.22440 -0.00198 -0.04440 -0.00015 121 ARG A CG  
942  C  CD  . ARG A 226 ? 0.19684 0.21889 0.21534 0.00221  -0.04569 0.00100  121 ARG A CD  
943  N  NE  . ARG A 226 ? 0.15937 0.18826 0.18833 0.00276  -0.04169 -0.00049 121 ARG A NE  
944  C  CZ  . ARG A 226 ? 0.13676 0.17222 0.17647 0.00582  -0.04232 -0.00063 121 ARG A CZ  
945  N  NH1 . ARG A 226 ? 0.19360 0.22918 0.23580 0.00920  -0.04715 0.00104  121 ARG A NH1 
946  N  NH2 . ARG A 226 ? 0.15761 0.19997 0.20625 0.00541  -0.03819 -0.00238 121 ARG A NH2 
947  N  N   . ASN A 227 ? 0.21663 0.22063 0.19679 -0.00397 -0.06065 0.00408  122 ASN A N   
948  C  CA  . ASN A 227 ? 0.21281 0.20978 0.17867 -0.00569 -0.06173 0.00484  122 ASN A CA  
949  C  C   . ASN A 227 ? 0.21052 0.19939 0.16762 -0.00548 -0.05635 0.00539  122 ASN A C   
950  O  O   . ASN A 227 ? 0.22785 0.21377 0.18425 -0.00264 -0.05541 0.00828  122 ASN A O   
951  C  CB  . ASN A 227 ? 0.25307 0.25090 0.21809 -0.00344 -0.06621 0.00817  122 ASN A CB  
952  C  CG  . ASN A 227 ? 0.43035 0.42534 0.38419 -0.00626 -0.06833 0.00775  122 ASN A CG  
953  O  OD1 . ASN A 227 ? 0.46697 0.45493 0.40872 -0.00824 -0.06528 0.00717  122 ASN A OD1 
954  N  ND2 . ASN A 227 ? 0.61418 0.61494 0.57213 -0.00648 -0.07347 0.00783  122 ASN A ND2 
955  N  N   . CYS A 228 ? 0.17124 0.15691 0.12331 -0.00843 -0.05192 0.00236  123 CYS A N   
956  C  CA  . CYS A 228 ? 0.14109 0.12074 0.08774 -0.00844 -0.04542 0.00207  123 CYS A CA  
957  C  C   . CYS A 228 ? 0.15243 0.12637 0.08685 -0.01185 -0.04409 -0.00022 123 CYS A C   
958  O  O   . CYS A 228 ? 0.17667 0.14942 0.11150 -0.01379 -0.04011 -0.00354 123 CYS A O   
959  C  CB  . CYS A 228 ? 0.18357 0.16602 0.13954 -0.00801 -0.04037 0.00028  123 CYS A CB  
960  S  SG  . CYS A 228 ? 0.16148 0.15112 0.13128 -0.00442 -0.04108 0.00188  123 CYS A SG  
961  N  N   . PRO A 229 ? 0.16459 0.13460 0.08770 -0.01267 -0.04732 0.00147  124 PRO A N   
962  C  CA  . PRO A 229 ? 0.18180 0.14809 0.09473 -0.01592 -0.04559 -0.00147 124 PRO A CA  
963  C  C   . PRO A 229 ? 0.22878 0.18879 0.13496 -0.01722 -0.03879 -0.00361 124 PRO A C   
964  O  O   . PRO A 229 ? 0.27476 0.23242 0.17628 -0.01980 -0.03622 -0.00763 124 PRO A O   
965  C  CB  . PRO A 229 ? 0.22150 0.18669 0.12698 -0.01551 -0.04877 0.00171  124 PRO A CB  
966  C  CG  . PRO A 229 ? 0.23054 0.19609 0.14054 -0.01201 -0.05020 0.00653  124 PRO A CG  
967  C  CD  . PRO A 229 ? 0.16145 0.13234 0.08480 -0.01010 -0.05108 0.00589  124 PRO A CD  
968  N  N   . LYS A 230 ? 0.15957 0.11835 0.06909 -0.01497 -0.03454 -0.00142 125 LYS A N   
969  C  CA  . LYS A 230 ? 0.17573 0.13046 0.08262 -0.01570 -0.02728 -0.00338 125 LYS A CA  
970  C  C   . LYS A 230 ? 0.21408 0.17172 0.13252 -0.01487 -0.02364 -0.00571 125 LYS A C   
971  O  O   . LYS A 230 ? 0.24039 0.19537 0.15854 -0.01527 -0.01805 -0.00763 125 LYS A O   
972  C  CB  . LYS A 230 ? 0.19307 0.14451 0.09676 -0.01435 -0.02435 0.00020  125 LYS A CB  
973  C  CG  . LYS A 230 ? 0.19622 0.14337 0.08699 -0.01542 -0.02719 0.00331  125 LYS A CG  
974  C  CD  . LYS A 230 ? 0.26375 0.20790 0.14348 -0.01859 -0.02542 0.00026  125 LYS A CD  
975  C  CE  . LYS A 230 ? 0.37930 0.32067 0.24967 -0.01910 -0.02632 0.00406  125 LYS A CE  
976  N  NZ  . LYS A 230 ? 0.53863 0.47905 0.40000 -0.02175 -0.02605 0.00119  125 LYS A NZ  
977  N  N   . GLY A 231 ? 0.16231 0.12535 0.09080 -0.01383 -0.02654 -0.00548 126 GLY A N   
978  C  CA  . GLY A 231 ? 0.15348 0.11876 0.09128 -0.01361 -0.02353 -0.00732 126 GLY A CA  
979  C  C   . GLY A 231 ? 0.17105 0.14088 0.11872 -0.01098 -0.02350 -0.00491 126 GLY A C   
980  O  O   . GLY A 231 ? 0.15263 0.12353 0.10082 -0.00904 -0.02525 -0.00221 126 GLY A O   
981  N  N   A VAL A 232 ? 0.10247 0.07447 0.05767 -0.01101 -0.02131 -0.00601 127 VAL A N   
982  N  N   B VAL A 232 ? 0.10418 0.07624 0.05941 -0.01101 -0.02139 -0.00601 127 VAL A N   
983  C  CA  A VAL A 232 ? 0.09028 0.06722 0.05438 -0.00918 -0.02137 -0.00439 127 VAL A CA  
984  C  CA  B VAL A 232 ? 0.09032 0.06716 0.05427 -0.00912 -0.02133 -0.00433 127 VAL A CA  
985  C  C   A VAL A 232 ? 0.10619 0.08216 0.07375 -0.00854 -0.01707 -0.00447 127 VAL A C   
986  C  C   B VAL A 232 ? 0.10650 0.08234 0.07387 -0.00852 -0.01702 -0.00445 127 VAL A C   
987  O  O   A VAL A 232 ? 0.12377 0.09738 0.09144 -0.00984 -0.01495 -0.00612 127 VAL A O   
988  O  O   B VAL A 232 ? 0.12352 0.09675 0.09058 -0.00978 -0.01478 -0.00613 127 VAL A O   
989  C  CB  A VAL A 232 ? 0.09463 0.07657 0.06495 -0.01036 -0.02403 -0.00506 127 VAL A CB  
990  C  CB  B VAL A 232 ? 0.09831 0.08045 0.06873 -0.01008 -0.02411 -0.00482 127 VAL A CB  
991  C  CG1 A VAL A 232 ? 0.12168 0.10893 0.10031 -0.00865 -0.02333 -0.00361 127 VAL A CG1 
992  C  CG1 B VAL A 232 ? 0.11424 0.09475 0.08538 -0.01273 -0.02290 -0.00713 127 VAL A CG1 
993  C  CG2 A VAL A 232 ? 0.13992 0.12364 0.10793 -0.01100 -0.02905 -0.00502 127 VAL A CG2 
994  C  CG2 B VAL A 232 ? 0.11749 0.10475 0.09599 -0.00825 -0.02332 -0.00336 127 VAL A CG2 
995  N  N   . VAL A 233 ? 0.08858 0.06635 0.05942 -0.00651 -0.01615 -0.00277 128 VAL A N   
996  C  CA  . VAL A 233 ? 0.07605 0.05383 0.05042 -0.00576 -0.01308 -0.00245 128 VAL A CA  
997  C  C   . VAL A 233 ? 0.07001 0.05272 0.05029 -0.00481 -0.01371 -0.00150 128 VAL A C   
998  O  O   . VAL A 233 ? 0.09835 0.08404 0.08022 -0.00388 -0.01571 -0.00104 128 VAL A O   
999  C  CB  . VAL A 233 ? 0.10601 0.08092 0.07760 -0.00473 -0.01120 -0.00175 128 VAL A CB  
1000 C  CG1 . VAL A 233 ? 0.11359 0.08912 0.08942 -0.00410 -0.00873 -0.00154 128 VAL A CG1 
1001 C  CG2 . VAL A 233 ? 0.13679 0.10713 0.10170 -0.00595 -0.00992 -0.00271 128 VAL A CG2 
1002 N  N   . ALA A 234 ? 0.06948 0.05310 0.05301 -0.00501 -0.01196 -0.00120 129 ALA A N   
1003 C  CA  . ALA A 234 ? 0.06305 0.05097 0.05047 -0.00432 -0.01185 -0.00035 129 ALA A CA  
1004 C  C   . ALA A 234 ? 0.13551 0.12254 0.12326 -0.00356 -0.01027 0.00024  129 ALA A C   
1005 O  O   . ALA A 234 ? 0.12981 0.11445 0.11773 -0.00401 -0.00919 0.00043  129 ALA A O   
1006 C  CB  . ALA A 234 ? 0.09528 0.08586 0.08587 -0.00600 -0.01185 0.00002  129 ALA A CB  
1007 N  N   A SER A 235 ? 0.06742 0.05651 0.05589 -0.00238 -0.01029 0.00028  130 SER A N   
1008 N  N   B SER A 235 ? 0.06862 0.05764 0.05703 -0.00236 -0.01029 0.00027  130 SER A N   
1009 C  CA  A SER A 235 ? 0.06858 0.05734 0.05735 -0.00189 -0.00948 0.00050  130 SER A CA  
1010 C  CA  B SER A 235 ? 0.06999 0.05872 0.05877 -0.00191 -0.00947 0.00052  130 SER A CA  
1011 C  C   A SER A 235 ? 0.08128 0.07378 0.07116 -0.00212 -0.00938 0.00089  130 SER A C   
1012 C  C   B SER A 235 ? 0.08182 0.07430 0.07172 -0.00216 -0.00938 0.00093  130 SER A C   
1013 O  O   A SER A 235 ? 0.09278 0.08809 0.08318 -0.00160 -0.00937 0.00007  130 SER A O   
1014 O  O   B SER A 235 ? 0.09264 0.08800 0.08309 -0.00171 -0.00937 0.00017  130 SER A O   
1015 C  CB  A SER A 235 ? 0.10188 0.08893 0.08958 -0.00076 -0.00955 -0.00020 130 SER A CB  
1016 C  CB  B SER A 235 ? 0.10408 0.09112 0.09186 -0.00081 -0.00947 -0.00018 130 SER A CB  
1017 O  OG  A SER A 235 ? 0.10606 0.09247 0.09451 -0.00077 -0.00893 -0.00029 130 SER A OG  
1018 O  OG  B SER A 235 ? 0.17272 0.16178 0.16120 0.00026  -0.01011 -0.00091 130 SER A OG  
1019 N  N   A LEU A 236 ? 0.06880 0.06136 0.05900 -0.00285 -0.00926 0.00220  131 LEU A N   
1020 N  N   B LEU A 236 ? 0.07062 0.06307 0.06084 -0.00285 -0.00926 0.00221  131 LEU A N   
1021 C  CA  A LEU A 236 ? 0.08332 0.07901 0.07284 -0.00358 -0.00920 0.00316  131 LEU A CA  
1022 C  CA  B LEU A 236 ? 0.08456 0.08001 0.07414 -0.00357 -0.00924 0.00323  131 LEU A CA  
1023 C  C   A LEU A 236 ? 0.08097 0.07678 0.06955 -0.00334 -0.00998 0.00341  131 LEU A C   
1024 C  C   B LEU A 236 ? 0.08339 0.07894 0.07213 -0.00326 -0.01002 0.00334  131 LEU A C   
1025 O  O   A LEU A 236 ? 0.09764 0.09239 0.08717 -0.00364 -0.01083 0.00521  131 LEU A O   
1026 O  O   B LEU A 236 ? 0.09869 0.09301 0.08863 -0.00342 -0.01086 0.00491  131 LEU A O   
1027 C  CB  A LEU A 236 ? 0.10065 0.09617 0.09084 -0.00510 -0.00906 0.00541  131 LEU A CB  
1028 C  CB  B LEU A 236 ? 0.09840 0.09342 0.08871 -0.00500 -0.00917 0.00546  131 LEU A CB  
1029 C  CG  A LEU A 236 ? 0.12329 0.12041 0.11474 -0.00603 -0.00843 0.00492  131 LEU A CG  
1030 C  CG  B LEU A 236 ? 0.12596 0.12188 0.11754 -0.00610 -0.00859 0.00527  131 LEU A CG  
1031 C  CD1 A LEU A 236 ? 0.19280 0.18642 0.18547 -0.00635 -0.00887 0.00451  131 LEU A CD1 
1032 C  CD1 B LEU A 236 ? 0.06326 0.05695 0.05604 -0.00768 -0.00856 0.00732  131 LEU A CD1 
1033 C  CD2 A LEU A 236 ? 0.31269 0.31224 0.30412 -0.00796 -0.00752 0.00686  131 LEU A CD2 
1034 C  CD2 B LEU A 236 ? 0.14758 0.14826 0.13892 -0.00657 -0.00760 0.00485  131 LEU A CD2 
1035 N  N   . SER A 237 ? 0.08165 0.07868 0.06896 -0.00277 -0.00995 0.00148  132 SER A N   
1036 C  CA  . SER A 237 ? 0.06157 0.05908 0.04777 -0.00296 -0.01113 0.00108  132 SER A CA  
1037 C  C   . SER A 237 ? 0.10838 0.10891 0.09074 -0.00404 -0.01124 0.00156  132 SER A C   
1038 O  O   . SER A 237 ? 0.14843 0.15046 0.12824 -0.00406 -0.01075 -0.00084 132 SER A O   
1039 C  CB  . SER A 237 ? 0.08280 0.07910 0.06941 -0.00216 -0.01098 -0.00165 132 SER A CB  
1040 O  OG  . SER A 237 ? 0.08533 0.07859 0.07449 -0.00168 -0.01076 -0.00145 132 SER A OG  
1041 N  N   . LEU A 238 ? 0.10127 0.10222 0.08288 -0.00505 -0.01164 0.00465  133 LEU A N   
1042 C  CA  . LEU A 238 ? 0.09188 0.09532 0.06874 -0.00655 -0.01140 0.00600  133 LEU A CA  
1043 C  C   . LEU A 238 ? 0.12932 0.13144 0.10614 -0.00745 -0.01298 0.01038  133 LEU A C   
1044 O  O   . LEU A 238 ? 0.15188 0.15130 0.13317 -0.00673 -0.01363 0.01175  133 LEU A O   
1045 C  CB  . LEU A 238 ? 0.14584 0.15179 0.12199 -0.00706 -0.00842 0.00483  133 LEU A CB  
1046 C  CG  . LEU A 238 ? 0.15074 0.15594 0.13118 -0.00713 -0.00742 0.00587  133 LEU A CG  
1047 C  CD1 . LEU A 238 ? 0.19814 0.20256 0.17801 -0.00900 -0.00748 0.00977  133 LEU A CD1 
1048 C  CD2 . LEU A 238 ? 0.21307 0.22162 0.19503 -0.00691 -0.00504 0.00348  133 LEU A CD2 
1049 N  N   . GLY A 239 ? 0.15467 0.15836 0.12608 -0.00903 -0.01348 0.01257  134 GLY A N   
1050 C  CA  . GLY A 239 ? 0.20271 0.20460 0.17372 -0.00998 -0.01495 0.01745  134 GLY A CA  
1051 C  C   . GLY A 239 ? 0.21413 0.21770 0.17731 -0.01176 -0.01627 0.01988  134 GLY A C   
1052 O  O   . GLY A 239 ? 0.22652 0.23269 0.18448 -0.01226 -0.01611 0.01715  134 GLY A O   
1053 N  N   . GLY A 240 ? 0.16789 0.16936 0.13003 -0.01271 -0.01782 0.02504  135 GLY A N   
1054 C  CA  . GLY A 240 ? 0.14525 0.14751 0.09895 -0.01465 -0.01963 0.02870  135 GLY A CA  
1055 C  C   . GLY A 240 ? 0.15025 0.14864 0.10597 -0.01459 -0.02273 0.03495  135 GLY A C   
1056 O  O   . GLY A 240 ? 0.15678 0.15239 0.12091 -0.01250 -0.02410 0.03540  135 GLY A O   
1057 N  N   . GLY A 241 ? 0.15383 0.15170 0.10163 -0.01689 -0.02361 0.03982  136 GLY A N   
1058 C  CA  . GLY A 241 ? 0.16171 0.15513 0.11124 -0.01674 -0.02702 0.04656  136 GLY A CA  
1059 C  C   . GLY A 241 ? 0.16834 0.15751 0.12516 -0.01670 -0.02434 0.04796  136 GLY A C   
1060 O  O   . GLY A 241 ? 0.18563 0.17589 0.14389 -0.01782 -0.01978 0.04479  136 GLY A O   
1061 N  N   . TYR A 242 ? 0.14532 0.12955 0.10732 -0.01535 -0.02756 0.05264  137 TYR A N   
1062 C  CA  . TYR A 242 ? 0.12554 0.10455 0.09520 -0.01512 -0.02564 0.05368  137 TYR A CA  
1063 C  C   . TYR A 242 ? 0.15197 0.13020 0.11755 -0.01888 -0.02135 0.05519  137 TYR A C   
1064 O  O   . TYR A 242 ? 0.17649 0.15488 0.13406 -0.02148 -0.02106 0.05938  137 TYR A O   
1065 C  CB  . TYR A 242 ? 0.14496 0.11859 0.11960 -0.01322 -0.02943 0.05874  137 TYR A CB  
1066 C  CG  . TYR A 242 ? 0.13132 0.09867 0.11388 -0.01303 -0.02739 0.05923  137 TYR A CG  
1067 C  CD1 . TYR A 242 ? 0.17517 0.14059 0.16721 -0.01032 -0.02710 0.05545  137 TYR A CD1 
1068 C  CD2 . TYR A 242 ? 0.13902 0.10256 0.11944 -0.01568 -0.02520 0.06248  137 TYR A CD2 
1069 C  CE1 . TYR A 242 ? 0.20233 0.16165 0.20093 -0.01040 -0.02501 0.05495  137 TYR A CE1 
1070 C  CE2 . TYR A 242 ? 0.20328 0.16087 0.19090 -0.01585 -0.02332 0.06215  137 TYR A CE2 
1071 C  CZ  . TYR A 242 ? 0.16937 0.12480 0.16563 -0.01329 -0.02334 0.05830  137 TYR A CZ  
1072 O  OH  . TYR A 242 ? 0.28635 0.23557 0.28900 -0.01366 -0.02133 0.05716  137 TYR A OH  
1073 N  N   . SER A 243 ? 0.13518 0.11276 0.10685 -0.01914 -0.01789 0.05131  138 SER A N   
1074 C  CA  . SER A 243 ? 0.12537 0.10238 0.09634 -0.02274 -0.01389 0.05221  138 SER A CA  
1075 C  C   . SER A 243 ? 0.14569 0.11814 0.12596 -0.02215 -0.01298 0.05006  138 SER A C   
1076 O  O   . SER A 243 ? 0.16112 0.13519 0.14598 -0.02008 -0.01250 0.04445  138 SER A O   
1077 C  CB  . SER A 243 ? 0.18658 0.17083 0.15408 -0.02423 -0.01003 0.04749  138 SER A CB  
1078 O  OG  . SER A 243 ? 0.19381 0.17853 0.16439 -0.02725 -0.00613 0.04692  138 SER A OG  
1079 N  N   A SER A 244 ? 0.15539 0.12174 0.13784 -0.02423 -0.01271 0.05447  139 SER A N   
1080 N  N   B SER A 244 ? 0.15544 0.12180 0.13784 -0.02424 -0.01271 0.05449  139 SER A N   
1081 C  CA  A SER A 244 ? 0.13616 0.09766 0.12692 -0.02408 -0.01180 0.05182  139 SER A CA  
1082 C  CA  B SER A 244 ? 0.13693 0.09842 0.12756 -0.02425 -0.01171 0.05196  139 SER A CA  
1083 C  C   A SER A 244 ? 0.14512 0.11125 0.13751 -0.02626 -0.00832 0.04659  139 SER A C   
1084 C  C   B SER A 244 ? 0.14537 0.11166 0.13773 -0.02617 -0.00833 0.04643  139 SER A C   
1085 O  O   A SER A 244 ? 0.15778 0.12248 0.15568 -0.02520 -0.00808 0.04191  139 SER A O   
1086 O  O   B SER A 244 ? 0.15529 0.12031 0.15306 -0.02491 -0.00819 0.04165  139 SER A O   
1087 C  CB  A SER A 244 ? 0.17284 0.12606 0.16598 -0.02600 -0.01228 0.05749  139 SER A CB  
1088 C  CB  B SER A 244 ? 0.17506 0.12873 0.16752 -0.02660 -0.01187 0.05771  139 SER A CB  
1089 O  OG  A SER A 244 ? 0.21075 0.16558 0.19935 -0.03015 -0.00946 0.06030  139 SER A OG  
1090 O  OG  B SER A 244 ? 0.20036 0.14886 0.20054 -0.02704 -0.01083 0.05463  139 SER A OG  
1091 N  N   A SER A 245 ? 0.14038 0.11247 0.12809 -0.02911 -0.00570 0.04705  140 SER A N   
1092 N  N   B SER A 245 ? 0.14207 0.11426 0.12994 -0.02908 -0.00567 0.04685  140 SER A N   
1093 C  CA  A SER A 245 ? 0.12347 0.10085 0.11438 -0.03079 -0.00283 0.04213  140 SER A CA  
1094 C  CA  B SER A 245 ? 0.12337 0.10068 0.11456 -0.03077 -0.00284 0.04196  140 SER A CA  
1095 C  C   A SER A 245 ? 0.12537 0.10732 0.11717 -0.02735 -0.00355 0.03614  140 SER A C   
1096 C  C   B SER A 245 ? 0.12523 0.10766 0.11688 -0.02747 -0.00337 0.03604  140 SER A C   
1097 O  O   A SER A 245 ? 0.13081 0.11399 0.12729 -0.02727 -0.00308 0.03174  140 SER A O   
1098 O  O   B SER A 245 ? 0.13198 0.11650 0.12805 -0.02755 -0.00266 0.03161  140 SER A O   
1099 C  CB  A SER A 245 ? 0.14622 0.12961 0.13331 -0.03444 0.00074  0.04376  140 SER A CB  
1100 C  CB  B SER A 245 ? 0.14214 0.12482 0.13001 -0.03476 0.00078  0.04394  140 SER A CB  
1101 O  OG  A SER A 245 ? 0.26647 0.24555 0.25110 -0.03795 0.00165  0.05017  140 SER A OG  
1102 O  OG  B SER A 245 ? 0.17930 0.16602 0.15910 -0.03406 0.00109  0.04543  140 SER A OG  
1103 N  N   . VAL A 246 ? 0.10324 0.08757 0.09035 -0.02475 -0.00491 0.03600  141 VAL A N   
1104 C  CA  . VAL A 246 ? 0.09502 0.08279 0.08298 -0.02169 -0.00554 0.03079  141 VAL A CA  
1105 C  C   . VAL A 246 ? 0.09673 0.07951 0.08953 -0.01933 -0.00743 0.02875  141 VAL A C   
1106 O  O   . VAL A 246 ? 0.11948 0.10352 0.11483 -0.01831 -0.00711 0.02434  141 VAL A O   
1107 C  CB  . VAL A 246 ? 0.12080 0.11167 0.10285 -0.01999 -0.00663 0.03107  141 VAL A CB  
1108 C  CG1 . VAL A 246 ? 0.12819 0.12116 0.11183 -0.01690 -0.00748 0.02608  141 VAL A CG1 
1109 C  CG2 . VAL A 246 ? 0.14179 0.13793 0.11846 -0.02239 -0.00389 0.03176  141 VAL A CG2 
1110 N  N   . ASN A 247 ? 0.10924 0.08609 0.10352 -0.01855 -0.00925 0.03205  142 ASN A N   
1111 C  CA  . ASN A 247 ? 0.10573 0.07790 0.10513 -0.01627 -0.01020 0.02956  142 ASN A CA  
1112 C  C   . ASN A 247 ? 0.10876 0.07862 0.11170 -0.01817 -0.00870 0.02666  142 ASN A C   
1113 O  O   . ASN A 247 ? 0.11315 0.08230 0.11801 -0.01684 -0.00855 0.02220  142 ASN A O   
1114 C  CB  . ASN A 247 ? 0.11587 0.08207 0.11787 -0.01485 -0.01225 0.03357  142 ASN A CB  
1115 C  CG  . ASN A 247 ? 0.13961 0.10816 0.13997 -0.01216 -0.01475 0.03516  142 ASN A CG  
1116 O  OD1 . ASN A 247 ? 0.13837 0.11258 0.13451 -0.01188 -0.01482 0.03361  142 ASN A OD1 
1117 N  ND2 . ASN A 247 ? 0.14463 0.10868 0.14905 -0.01014 -0.01707 0.03825  142 ASN A ND2 
1118 N  N   A SER A 248 ? 0.12596 0.09468 0.12941 -0.02163 -0.00760 0.02915  143 SER A N   
1119 N  N   B SER A 248 ? 0.12630 0.09481 0.12987 -0.02163 -0.00762 0.02917  143 SER A N   
1120 C  CA  A SER A 248 ? 0.10841 0.07482 0.11577 -0.02406 -0.00664 0.02645  143 SER A CA  
1121 C  CA  B SER A 248 ? 0.10906 0.07545 0.11648 -0.02404 -0.00665 0.02633  143 SER A CA  
1122 C  C   A SER A 248 ? 0.13633 0.10911 0.14345 -0.02427 -0.00607 0.02168  143 SER A C   
1123 C  C   B SER A 248 ? 0.13567 0.10849 0.14276 -0.02421 -0.00608 0.02160  143 SER A C   
1124 O  O   A SER A 248 ? 0.12981 0.10090 0.13917 -0.02456 -0.00645 0.01770  143 SER A O   
1125 O  O   B SER A 248 ? 0.12987 0.10109 0.13913 -0.02442 -0.00648 0.01757  143 SER A O   
1126 C  CB  A SER A 248 ? 0.13678 0.10127 0.14524 -0.02825 -0.00543 0.03049  143 SER A CB  
1127 C  CB  B SER A 248 ? 0.13690 0.10134 0.14556 -0.02827 -0.00543 0.03022  143 SER A CB  
1128 O  OG  A SER A 248 ? 0.19462 0.15751 0.20740 -0.03110 -0.00477 0.02749  143 SER A OG  
1129 O  OG  B SER A 248 ? 0.21046 0.16753 0.21983 -0.02797 -0.00640 0.03497  143 SER A OG  
1130 N  N   . ALA A 249 ? 0.08988 0.06980 0.09414 -0.02408 -0.00530 0.02193  144 ALA A N   
1131 C  CA  . ALA A 249 ? 0.08427 0.07007 0.08917 -0.02362 -0.00513 0.01777  144 ALA A CA  
1132 C  C   . ALA A 249 ? 0.10531 0.08971 0.10913 -0.02030 -0.00659 0.01430  144 ALA A C   
1133 O  O   . ALA A 249 ? 0.09193 0.07729 0.09690 -0.02034 -0.00728 0.01082  144 ALA A O   
1134 C  CB  . ALA A 249 ? 0.13342 0.12658 0.13605 -0.02367 -0.00358 0.01849  144 ALA A CB  
1135 N  N   . ALA A 250 ? 0.09064 0.07265 0.09233 -0.01767 -0.00721 0.01540  145 ALA A N   
1136 C  CA  . ALA A 250 ? 0.07608 0.05669 0.07714 -0.01496 -0.00794 0.01232  145 ALA A CA  
1137 C  C   . ALA A 250 ? 0.08712 0.06196 0.09021 -0.01536 -0.00801 0.01005  145 ALA A C   
1138 O  O   . ALA A 250 ? 0.08621 0.06080 0.08811 -0.01465 -0.00820 0.00655  145 ALA A O   
1139 C  CB  . ALA A 250 ? 0.10375 0.08384 0.10351 -0.01251 -0.00853 0.01409  145 ALA A CB  
1140 N  N   . ALA A 251 ? 0.09297 0.06259 0.09865 -0.01641 -0.00783 0.01202  146 ALA A N   
1141 C  CA  . ALA A 251 ? 0.10334 0.06674 0.11118 -0.01707 -0.00753 0.00932  146 ALA A CA  
1142 C  C   . ALA A 251 ? 0.10007 0.06482 0.10762 -0.01988 -0.00786 0.00612  146 ALA A C   
1143 O  O   . ALA A 251 ? 0.11576 0.07767 0.12215 -0.01988 -0.00797 0.00208  146 ALA A O   
1144 C  CB  . ALA A 251 ? 0.10288 0.06015 0.11434 -0.01788 -0.00738 0.01250  146 ALA A CB  
1145 N  N   . ARG A 252 ? 0.08889 0.05836 0.09747 -0.02241 -0.00803 0.00773  147 ARG A N   
1146 C  CA  . ARG A 252 ? 0.08868 0.06075 0.09841 -0.02508 -0.00895 0.00479  147 ARG A CA  
1147 C  C   . ARG A 252 ? 0.10181 0.07766 0.10835 -0.02316 -0.01020 0.00170  147 ARG A C   
1148 O  O   . ARG A 252 ? 0.11280 0.08754 0.11831 -0.02427 -0.01163 -0.00177 147 ARG A O   
1149 C  CB  . ARG A 252 ? 0.12587 0.10383 0.13869 -0.02792 -0.00841 0.00722  147 ARG A CB  
1150 C  CG  . ARG A 252 ? 0.17754 0.15167 0.19358 -0.03118 -0.00727 0.01025  147 ARG A CG  
1151 C  CD  . ARG A 252 ? 0.13619 0.11736 0.15615 -0.03486 -0.00644 0.01119  147 ARG A CD  
1152 N  NE  . ARG A 252 ? 0.12245 0.11100 0.14086 -0.03351 -0.00497 0.01325  147 ARG A NE  
1153 C  CZ  . ARG A 252 ? 0.14083 0.12926 0.15704 -0.03381 -0.00300 0.01764  147 ARG A CZ  
1154 N  NH1 . ARG A 252 ? 0.14445 0.12564 0.15983 -0.03476 -0.00274 0.02115  147 ARG A NH1 
1155 N  NH2 . ARG A 252 ? 0.11421 0.10979 0.12877 -0.03312 -0.00131 0.01853  147 ARG A NH2 
1156 N  N   . LEU A 253 ? 0.08263 0.06286 0.08728 -0.02055 -0.00992 0.00300  148 LEU A N   
1157 C  CA  . LEU A 253 ? 0.07648 0.05956 0.07830 -0.01867 -0.01114 0.00072  148 LEU A CA  
1158 C  C   . LEU A 253 ? 0.09385 0.07133 0.09188 -0.01751 -0.01124 -0.00189 148 LEU A C   
1159 O  O   . LEU A 253 ? 0.10408 0.08149 0.09937 -0.01797 -0.01277 -0.00451 148 LEU A O   
1160 C  CB  . LEU A 253 ? 0.09364 0.08100 0.09446 -0.01618 -0.01045 0.00250  148 LEU A CB  
1161 C  CG  . LEU A 253 ? 0.09569 0.08570 0.09418 -0.01403 -0.01164 0.00083  148 LEU A CG  
1162 C  CD1 . LEU A 253 ? 0.12111 0.11528 0.12160 -0.01514 -0.01373 -0.00067 148 LEU A CD1 
1163 C  CD2 . LEU A 253 ? 0.12600 0.11916 0.12403 -0.01194 -0.01066 0.00224  148 LEU A CD2 
1164 N  N   . GLN A 254 ? 0.09990 0.07275 0.09789 -0.01620 -0.00961 -0.00121 149 GLN A N   
1165 C  CA  . GLN A 254 ? 0.10262 0.07034 0.09782 -0.01517 -0.00867 -0.00401 149 GLN A CA  
1166 C  C   . GLN A 254 ? 0.11603 0.07956 0.11035 -0.01776 -0.00916 -0.00736 149 GLN A C   
1167 O  O   . GLN A 254 ? 0.11502 0.07693 0.10447 -0.01802 -0.00950 -0.01058 149 GLN A O   
1168 C  CB  . GLN A 254 ? 0.09741 0.06185 0.09528 -0.01316 -0.00684 -0.00242 149 GLN A CB  
1169 C  CG  . GLN A 254 ? 0.12449 0.08386 0.12123 -0.01200 -0.00489 -0.00555 149 GLN A CG  
1170 C  CD  . GLN A 254 ? 0.12192 0.08322 0.11444 -0.01045 -0.00416 -0.00679 149 GLN A CD  
1171 O  OE1 . GLN A 254 ? 0.11039 0.07569 0.10307 -0.00901 -0.00460 -0.00462 149 GLN A OE1 
1172 N  NE2 . GLN A 254 ? 0.18638 0.14442 0.17443 -0.01109 -0.00296 -0.01046 149 GLN A NE2 
1173 N  N   A SER A 255 ? 0.10385 0.06541 0.10233 -0.02005 -0.00929 -0.00660 150 SER A N   
1174 N  N   B SER A 255 ? 0.10434 0.06579 0.10274 -0.02006 -0.00928 -0.00669 150 SER A N   
1175 C  CA  A SER A 255 ? 0.09963 0.05667 0.09800 -0.02300 -0.00987 -0.01009 150 SER A CA  
1176 C  CA  B SER A 255 ? 0.09986 0.05660 0.09761 -0.02282 -0.00980 -0.01048 150 SER A CA  
1177 C  C   A SER A 255 ? 0.11910 0.08013 0.11438 -0.02504 -0.01269 -0.01248 150 SER A C   
1178 C  C   B SER A 255 ? 0.12008 0.08108 0.11544 -0.02516 -0.01274 -0.01254 150 SER A C   
1179 O  O   A SER A 255 ? 0.15851 0.11593 0.15023 -0.02684 -0.01358 -0.01659 150 SER A O   
1180 O  O   B SER A 255 ? 0.15055 0.10805 0.14301 -0.02732 -0.01378 -0.01655 150 SER A O   
1181 C  CB  A SER A 255 ? 0.12174 0.07643 0.12598 -0.02542 -0.00961 -0.00792 150 SER A CB  
1182 C  CB  B SER A 255 ? 0.16707 0.11967 0.17044 -0.02493 -0.00918 -0.00903 150 SER A CB  
1183 O  OG  A SER A 255 ? 0.15070 0.10215 0.15587 -0.02915 -0.01071 -0.01117 150 SER A OG  
1184 O  OG  B SER A 255 ? 0.15374 0.11158 0.16036 -0.02738 -0.01048 -0.00643 150 SER A OG  
1185 N  N   . SER A 256 ? 0.10154 0.07001 0.09824 -0.02473 -0.01427 -0.01015 151 SER A N   
1186 C  CA  . SER A 256 ? 0.09555 0.06886 0.09118 -0.02624 -0.01760 -0.01174 151 SER A CA  
1187 C  C   . SER A 256 ? 0.13064 0.10305 0.11871 -0.02462 -0.01890 -0.01379 151 SER A C   
1188 O  O   . SER A 256 ? 0.15385 0.12941 0.14006 -0.02578 -0.02241 -0.01508 151 SER A O   
1189 C  CB  . SER A 256 ? 0.09853 0.08013 0.09905 -0.02568 -0.01830 -0.00870 151 SER A CB  
1190 O  OG  . SER A 256 ? 0.12131 0.10568 0.11907 -0.02215 -0.01811 -0.00735 151 SER A OG  
1191 N  N   . GLY A 257 ? 0.11909 0.08758 0.10308 -0.02211 -0.01629 -0.01383 152 GLY A N   
1192 C  CA  . GLY A 257 ? 0.12704 0.09373 0.10307 -0.02098 -0.01663 -0.01548 152 GLY A CA  
1193 C  C   . GLY A 257 ? 0.12066 0.09061 0.09551 -0.01790 -0.01627 -0.01268 152 GLY A C   
1194 O  O   . GLY A 257 ? 0.20683 0.17697 0.17577 -0.01737 -0.01784 -0.01294 152 GLY A O   
1195 N  N   . VAL A 258 ? 0.10351 0.07577 0.08349 -0.01611 -0.01455 -0.00994 153 VAL A N   
1196 C  CA  . VAL A 258 ? 0.09804 0.07319 0.07776 -0.01344 -0.01415 -0.00764 153 VAL A CA  
1197 C  C   . VAL A 258 ? 0.12660 0.09863 0.10671 -0.01184 -0.01079 -0.00717 153 VAL A C   
1198 O  O   . VAL A 258 ? 0.12828 0.09898 0.11251 -0.01205 -0.00940 -0.00664 153 VAL A O   
1199 C  CB  . VAL A 258 ? 0.09827 0.07950 0.08377 -0.01297 -0.01513 -0.00534 153 VAL A CB  
1200 C  CG1 . VAL A 258 ? 0.11839 0.10176 0.10377 -0.01025 -0.01441 -0.00360 153 VAL A CG1 
1201 C  CG2 . VAL A 258 ? 0.12893 0.11459 0.11615 -0.01427 -0.01849 -0.00585 153 VAL A CG2 
1202 N  N   . MET A 259 ? 0.08170 0.05279 0.05831 -0.01025 -0.00967 -0.00699 154 MET A N   
1203 C  CA  . MET A 259 ? 0.09922 0.06885 0.07786 -0.00872 -0.00679 -0.00641 154 MET A CA  
1204 C  C   . MET A 259 ? 0.09720 0.07091 0.08050 -0.00745 -0.00735 -0.00378 154 MET A C   
1205 O  O   . MET A 259 ? 0.09679 0.07324 0.07922 -0.00659 -0.00846 -0.00280 154 MET A O   
1206 C  CB  . MET A 259 ? 0.11265 0.08035 0.08634 -0.00806 -0.00523 -0.00703 154 MET A CB  
1207 C  CG  . MET A 259 ? 0.18126 0.14740 0.15776 -0.00695 -0.00174 -0.00731 154 MET A CG  
1208 S  SD  . MET A 259 ? 0.16096 0.13132 0.14308 -0.00513 -0.00225 -0.00442 154 MET A SD  
1209 C  CE  . MET A 259 ? 0.19309 0.16184 0.17952 -0.00423 0.00153  -0.00538 154 MET A CE  
1210 N  N   . VAL A 260 ? 0.07193 0.04565 0.05975 -0.00731 -0.00667 -0.00263 155 VAL A N   
1211 C  CA  . VAL A 260 ? 0.06767 0.04516 0.05840 -0.00653 -0.00735 -0.00017 155 VAL A CA  
1212 C  C   . VAL A 260 ? 0.09760 0.07481 0.09019 -0.00494 -0.00627 0.00056  155 VAL A C   
1213 O  O   . VAL A 260 ? 0.10160 0.07632 0.09710 -0.00451 -0.00515 0.00055  155 VAL A O   
1214 C  CB  . VAL A 260 ? 0.06828 0.04621 0.06200 -0.00780 -0.00783 0.00144  155 VAL A CB  
1215 C  CG1 . VAL A 260 ? 0.11067 0.09242 0.10553 -0.00732 -0.00832 0.00394  155 VAL A CG1 
1216 C  CG2 . VAL A 260 ? 0.10132 0.08016 0.09453 -0.00983 -0.00890 0.00045  155 VAL A CG2 
1217 N  N   . ALA A 261 ? 0.06888 0.04881 0.06080 -0.00406 -0.00675 0.00112  156 ALA A N   
1218 C  CA  . ALA A 261 ? 0.06196 0.04267 0.05637 -0.00299 -0.00639 0.00183  156 ALA A CA  
1219 C  C   . ALA A 261 ? 0.07274 0.05693 0.06782 -0.00292 -0.00798 0.00357  156 ALA A C   
1220 O  O   . ALA A 261 ? 0.09013 0.07658 0.08302 -0.00319 -0.00858 0.00337  156 ALA A O   
1221 C  CB  . ALA A 261 ? 0.11088 0.09116 0.10349 -0.00254 -0.00552 0.00066  156 ALA A CB  
1222 N  N   . VAL A 262 ? 0.06057 0.04529 0.05860 -0.00254 -0.00871 0.00524  157 VAL A N   
1223 C  CA  . VAL A 262 ? 0.07475 0.06248 0.07176 -0.00287 -0.01039 0.00708  157 VAL A CA  
1224 C  C   . VAL A 262 ? 0.08849 0.07775 0.08773 -0.00214 -0.01176 0.00762  157 VAL A C   
1225 O  O   . VAL A 262 ? 0.08651 0.07470 0.09025 -0.00127 -0.01157 0.00764  157 VAL A O   
1226 C  CB  . VAL A 262 ? 0.09978 0.08696 0.09694 -0.00379 -0.01103 0.00974  157 VAL A CB  
1227 C  CG1 . VAL A 262 ? 0.10650 0.09226 0.10285 -0.00495 -0.00983 0.00895  157 VAL A CG1 
1228 C  CG2 . VAL A 262 ? 0.18995 0.17474 0.19147 -0.00295 -0.01181 0.01163  157 VAL A CG2 
1229 N  N   . ALA A 263 ? 0.06919 0.06131 0.06561 -0.00260 -0.01316 0.00784  158 ALA A N   
1230 C  CA  . ALA A 263 ? 0.06202 0.05605 0.06024 -0.00235 -0.01521 0.00811  158 ALA A CA  
1231 C  C   . ALA A 263 ? 0.07974 0.07415 0.08040 -0.00210 -0.01762 0.01142  158 ALA A C   
1232 O  O   . ALA A 263 ? 0.09838 0.09230 0.09628 -0.00275 -0.01822 0.01396  158 ALA A O   
1233 C  CB  . ALA A 263 ? 0.08720 0.08367 0.08077 -0.00315 -0.01604 0.00674  158 ALA A CB  
1234 N  N   . ALA A 264 ? 0.06576 0.06128 0.07206 -0.00124 -0.01925 0.01168  159 ALA A N   
1235 C  CA  . ALA A 264 ? 0.07751 0.07347 0.08706 -0.00056 -0.02227 0.01526  159 ALA A CA  
1236 C  C   . ALA A 264 ? 0.10011 0.09861 0.10389 -0.00176 -0.02585 0.01745  159 ALA A C   
1237 O  O   . ALA A 264 ? 0.10398 0.10191 0.10732 -0.00165 -0.02836 0.02147  159 ALA A O   
1238 C  CB  . ALA A 264 ? 0.09443 0.09185 0.11321 0.00091  -0.02327 0.01500  159 ALA A CB  
1239 N  N   . GLY A 265 ? 0.09767 0.09850 0.09669 -0.00298 -0.02614 0.01491  160 GLY A N   
1240 C  CA  . GLY A 265 ? 0.10372 0.10698 0.09604 -0.00443 -0.02921 0.01598  160 GLY A CA  
1241 C  C   . GLY A 265 ? 0.11594 0.12235 0.11104 -0.00469 -0.03293 0.01485  160 GLY A C   
1242 O  O   . GLY A 265 ? 0.09588 0.10309 0.09979 -0.00356 -0.03360 0.01445  160 GLY A O   
1243 N  N   . ASN A 266 ? 0.10141 0.10990 0.08887 -0.00647 -0.03521 0.01398  161 ASN A N   
1244 C  CA  . ASN A 266 ? 0.09847 0.10994 0.08722 -0.00746 -0.03867 0.01159  161 ASN A CA  
1245 C  C   . ASN A 266 ? 0.13303 0.14725 0.11832 -0.00843 -0.04469 0.01475  161 ASN A C   
1246 O  O   . ASN A 266 ? 0.16382 0.18031 0.14441 -0.01031 -0.04758 0.01233  161 ASN A O   
1247 C  CB  . ASN A 266 ? 0.10957 0.12073 0.09242 -0.00895 -0.03646 0.00648  161 ASN A CB  
1248 C  CG  . ASN A 266 ? 0.21260 0.22090 0.19834 -0.00794 -0.03124 0.00375  161 ASN A CG  
1249 O  OD1 . ASN A 266 ? 0.19357 0.20066 0.18673 -0.00662 -0.02966 0.00442  161 ASN A OD1 
1250 N  ND2 . ASN A 266 ? 0.45060 0.45778 0.43015 -0.00847 -0.02847 0.00084  161 ASN A ND2 
1251 N  N   . ASN A 267 ? 0.09797 0.11178 0.08578 -0.00719 -0.04716 0.02016  162 ASN A N   
1252 C  CA  . ASN A 267 ? 0.10725 0.12319 0.09079 -0.00800 -0.05353 0.02429  162 ASN A CA  
1253 C  C   . ASN A 267 ? 0.16230 0.18113 0.15746 -0.00628 -0.05840 0.02640  162 ASN A C   
1254 O  O   . ASN A 267 ? 0.15987 0.17966 0.15332 -0.00592 -0.06184 0.02962  162 ASN A O   
1255 C  CB  . ASN A 267 ? 0.17683 0.18967 0.15387 -0.00798 -0.05307 0.02974  162 ASN A CB  
1256 C  CG  . ASN A 267 ? 0.46964 0.47974 0.43972 -0.00900 -0.04659 0.02776  162 ASN A CG  
1257 O  OD1 . ASN A 267 ? 0.33910 0.34649 0.31454 -0.00765 -0.04219 0.02731  162 ASN A OD1 
1258 N  ND2 . ASN A 267 ? 0.33258 0.34374 0.29089 -0.01145 -0.04596 0.02614  162 ASN A ND2 
1259 N  N   . ASN A 268 ? 0.11655 0.13647 0.12387 -0.00484 -0.05667 0.02387  163 ASN A N   
1260 C  CA  . ASN A 268 ? 0.09844 0.12187 0.11924 -0.00293 -0.06053 0.02562  163 ASN A CA  
1261 C  C   . ASN A 268 ? 0.10365 0.12493 0.12634 -0.00062 -0.06187 0.03115  163 ASN A C   
1262 O  O   . ASN A 268 ? 0.13135 0.15500 0.15705 0.00016  -0.06594 0.03341  163 ASN A O   
1263 C  CB  . ASN A 268 ? 0.10317 0.13148 0.12424 -0.00465 -0.06452 0.02313  163 ASN A CB  
1264 C  CG  . ASN A 268 ? 0.12930 0.16186 0.16519 -0.00284 -0.06691 0.02374  163 ASN A CG  
1265 O  OD1 . ASN A 268 ? 0.13195 0.16469 0.17973 -0.00088 -0.06425 0.02347  163 ASN A OD1 
1266 N  ND2 . ASN A 268 ? 0.14432 0.18059 0.17968 -0.00338 -0.07185 0.02459  163 ASN A ND2 
1267 N  N   . ALA A 269 ? 0.10376 0.12010 0.12440 0.00033  -0.05849 0.03334  164 ALA A N   
1268 C  CA  . ALA A 269 ? 0.11402 0.12682 0.13515 0.00202  -0.05915 0.03843  164 ALA A CA  
1269 C  C   . ALA A 269 ? 0.10593 0.11441 0.13455 0.00419  -0.05503 0.03888  164 ALA A C   
1270 O  O   . ALA A 269 ? 0.13052 0.13855 0.16155 0.00413  -0.05020 0.03448  164 ALA A O   
1271 C  CB  . ALA A 269 ? 0.17999 0.19023 0.18607 -0.00027 -0.05929 0.04105  164 ALA A CB  
1272 N  N   . ASP A 270 ? 0.14430 0.14878 0.17525 0.00583  -0.05515 0.04290  165 ASP A N   
1273 C  CA  . ASP A 270 ? 0.10342 0.10276 0.14059 0.00769  -0.05103 0.04298  165 ASP A CA  
1274 C  C   . ASP A 270 ? 0.10530 0.10072 0.13204 0.00539  -0.04712 0.04245  165 ASP A C   
1275 O  O   . ASP A 270 ? 0.13948 0.13334 0.15572 0.00325  -0.04818 0.04565  165 ASP A O   
1276 C  CB  . ASP A 270 ? 0.13937 0.13509 0.18158 0.00973  -0.05224 0.04695  165 ASP A CB  
1277 C  CG  . ASP A 270 ? 0.19949 0.19050 0.25153 0.01220  -0.04798 0.04556  165 ASP A CG  
1278 O  OD1 . ASP A 270 ? 0.18789 0.17499 0.23644 0.01127  -0.04395 0.04395  165 ASP A OD1 
1279 O  OD2 . ASP A 270 ? 0.27820 0.26918 0.34136 0.01505  -0.04851 0.04582  165 ASP A OD2 
1280 N  N   . ALA A 271 ? 0.09358 0.08778 0.12259 0.00544  -0.04130 0.03733  166 ALA A N   
1281 C  CA  . ALA A 271 ? 0.10457 0.09605 0.12482 0.00321  -0.03673 0.03530  166 ALA A CA  
1282 C  C   . ALA A 271 ? 0.12196 0.10762 0.14043 0.00288  -0.03561 0.03888  166 ALA A C   
1283 O  O   . ALA A 271 ? 0.12542 0.10959 0.13685 0.00066  -0.03237 0.03772  166 ALA A O   
1284 C  CB  . ALA A 271 ? 0.11634 0.10788 0.13988 0.00352  -0.03165 0.02941  166 ALA A CB  
1285 N  N   . ARG A 272 ? 0.12940 0.11180 0.15459 0.00494  -0.03836 0.04325  167 ARG A N   
1286 C  CA  . ARG A 272 ? 0.12893 0.10474 0.15288 0.00436  -0.03745 0.04701  167 ARG A CA  
1287 C  C   . ARG A 272 ? 0.15469 0.13037 0.16656 0.00104  -0.03853 0.05101  167 ARG A C   
1288 O  O   . ARG A 272 ? 0.14353 0.11463 0.15234 -0.00073 -0.03616 0.05284  167 ARG A O   
1289 C  CB  . ARG A 272 ? 0.16967 0.14281 0.20284 0.00725  -0.03956 0.04963  167 ARG A CB  
1290 C  CG  . ARG A 272 ? 0.26347 0.23975 0.29339 0.00719  -0.04448 0.05367  167 ARG A CG  
1291 C  CD  . ARG A 272 ? 0.61913 0.59277 0.65792 0.01006  -0.04658 0.05637  167 ARG A CD  
1292 N  NE  . ARG A 272 ? 0.71416 0.68804 0.76626 0.01336  -0.04481 0.05263  167 ARG A NE  
1293 C  CZ  . ARG A 272 ? 0.82253 0.79157 0.88306 0.01567  -0.04324 0.05263  167 ARG A CZ  
1294 N  NH1 . ARG A 272 ? 0.62587 0.58924 0.68375 0.01525  -0.04393 0.05667  167 ARG A NH1 
1295 N  NH2 . ARG A 272 ? 0.82102 0.79088 0.89281 0.01838  -0.04063 0.04828  167 ARG A NH2 
1296 N  N   . ASN A 273 ? 0.11515 0.09609 0.11979 -0.00022 -0.04119 0.05137  168 ASN A N   
1297 C  CA  . ASN A 273 ? 0.13422 0.11558 0.12685 -0.00341 -0.04112 0.05410  168 ASN A CA  
1298 C  C   . ASN A 273 ? 0.11796 0.10217 0.10226 -0.00614 -0.03777 0.05071  168 ASN A C   
1299 O  O   . ASN A 273 ? 0.15579 0.14178 0.12959 -0.00884 -0.03762 0.05222  168 ASN A O   
1300 C  CB  . ASN A 273 ? 0.13004 0.11482 0.11877 -0.00327 -0.04564 0.05615  168 ASN A CB  
1301 C  CG  . ASN A 273 ? 0.24404 0.22548 0.23845 -0.00124 -0.04846 0.06050  168 ASN A CG  
1302 O  OD1 . ASN A 273 ? 0.23219 0.20805 0.22850 -0.00125 -0.04660 0.06312  168 ASN A OD1 
1303 N  ND2 . ASN A 273 ? 0.18325 0.16804 0.18090 0.00048  -0.05307 0.06118  168 ASN A ND2 
1304 N  N   . TYR A 274 ? 0.12012 0.10526 0.10904 -0.00537 -0.03386 0.04474  169 TYR A N   
1305 C  CA  . TYR A 274 ? 0.10875 0.09708 0.09186 -0.00721 -0.03003 0.04004  169 TYR A CA  
1306 C  C   . TYR A 274 ? 0.11349 0.09935 0.10024 -0.00745 -0.02544 0.03716  169 TYR A C   
1307 O  O   . TYR A 274 ? 0.13125 0.11354 0.12563 -0.00577 -0.02496 0.03671  169 TYR A O   
1308 C  CB  . TYR A 274 ? 0.15586 0.14866 0.14017 -0.00611 -0.03083 0.03515  169 TYR A CB  
1309 C  CG  . TYR A 274 ? 0.11834 0.11404 0.09868 -0.00640 -0.03583 0.03744  169 TYR A CG  
1310 C  CD1 . TYR A 274 ? 0.24712 0.24536 0.21649 -0.00889 -0.03608 0.03742  169 TYR A CD1 
1311 C  CD2 . TYR A 274 ? 0.14765 0.14368 0.13529 -0.00427 -0.04037 0.03961  169 TYR A CD2 
1312 C  CE1 . TYR A 274 ? 0.26846 0.26916 0.23258 -0.00961 -0.04106 0.03939  169 TYR A CE1 
1313 C  CE2 . TYR A 274 ? 0.14693 0.14601 0.13073 -0.00478 -0.04600 0.04211  169 TYR A CE2 
1314 C  CZ  . TYR A 274 ? 0.20528 0.20647 0.17657 -0.00761 -0.04615 0.04167  169 TYR A CZ  
1315 O  OH  . TYR A 274 ? 0.27083 0.27487 0.23788 -0.00812 -0.04995 0.04192  169 TYR A OH  
1316 N  N   . SER A 275 ? 0.11191 0.09985 0.09333 -0.00958 -0.02211 0.03499  170 SER A N   
1317 C  CA  . SER A 275 ? 0.09282 0.07938 0.07733 -0.01015 -0.01841 0.03219  170 SER A CA  
1318 C  C   . SER A 275 ? 0.11556 0.10631 0.09822 -0.01020 -0.01606 0.02700  170 SER A C   
1319 O  O   . SER A 275 ? 0.14537 0.13989 0.12229 -0.01104 -0.01588 0.02619  170 SER A O   
1320 C  CB  . SER A 275 ? 0.11555 0.10045 0.09721 -0.01306 -0.01657 0.03552  170 SER A CB  
1321 O  OG  . SER A 275 ? 0.12404 0.10352 0.10853 -0.01295 -0.01847 0.04034  170 SER A OG  
1322 N  N   . PRO A 276 ? 0.09364 0.08349 0.08059 -0.00947 -0.01416 0.02349  171 PRO A N   
1323 C  CA  . PRO A 276 ? 0.09331 0.07858 0.08590 -0.00889 -0.01373 0.02338  171 PRO A CA  
1324 C  C   . PRO A 276 ? 0.08823 0.07126 0.08586 -0.00633 -0.01512 0.02259  171 PRO A C   
1325 O  O   . PRO A 276 ? 0.12246 0.10166 0.12459 -0.00564 -0.01413 0.02139  171 PRO A O   
1326 C  CB  . PRO A 276 ? 0.09879 0.08527 0.09190 -0.00947 -0.01136 0.01938  171 PRO A CB  
1327 C  CG  . PRO A 276 ? 0.13232 0.12316 0.12256 -0.00870 -0.01116 0.01680  171 PRO A CG  
1328 C  CD  . PRO A 276 ? 0.11838 0.11169 0.10401 -0.00946 -0.01217 0.01927  171 PRO A CD  
1329 N  N   . ALA A 277 ? 0.09623 0.08173 0.09352 -0.00511 -0.01727 0.02305  172 ALA A N   
1330 C  CA  . ALA A 277 ? 0.10751 0.09213 0.11102 -0.00279 -0.01842 0.02232  172 ALA A CA  
1331 C  C   . ALA A 277 ? 0.11413 0.09401 0.12366 -0.00166 -0.01880 0.02457  172 ALA A C   
1332 O  O   . ALA A 277 ? 0.11166 0.08970 0.12711 0.00004  -0.01750 0.02224  172 ALA A O   
1333 C  CB  . ALA A 277 ? 0.12937 0.11757 0.13224 -0.00220 -0.02175 0.02372  172 ALA A CB  
1334 N  N   . SER A 278 ? 0.08816 0.06564 0.09629 -0.00261 -0.02029 0.02909  173 SER A N   
1335 C  CA  . SER A 278 ? 0.09226 0.06455 0.10685 -0.00118 -0.02130 0.03188  173 SER A CA  
1336 C  C   . SER A 278 ? 0.10682 0.07377 0.12371 -0.00196 -0.01823 0.02993  173 SER A C   
1337 O  O   . SER A 278 ? 0.14281 0.10445 0.16549 -0.00075 -0.01864 0.03166  173 SER A O   
1338 C  CB  . SER A 278 ? 0.11231 0.08346 0.12408 -0.00195 -0.02472 0.03840  173 SER A CB  
1339 O  OG  . SER A 278 ? 0.12581 0.09696 0.12998 -0.00527 -0.02327 0.03999  173 SER A OG  
1340 N  N   . GLU A 279 ? 0.11220 0.08028 0.12521 -0.00387 -0.01554 0.02634  174 GLU A N   
1341 C  CA  . GLU A 279 ? 0.11763 0.08096 0.13252 -0.00498 -0.01316 0.02389  174 GLU A CA  
1342 C  C   . GLU A 279 ? 0.10186 0.06289 0.12177 -0.00271 -0.01149 0.01960  174 GLU A C   
1343 O  O   . GLU A 279 ? 0.09831 0.06269 0.11670 -0.00206 -0.01038 0.01620  174 GLU A O   
1344 C  CB  . GLU A 279 ? 0.10494 0.07127 0.11461 -0.00764 -0.01154 0.02149  174 GLU A CB  
1345 C  CG  . GLU A 279 ? 0.11187 0.07441 0.12293 -0.00901 -0.00958 0.01775  174 GLU A CG  
1346 C  CD  . GLU A 279 ? 0.12803 0.08354 0.14326 -0.00983 -0.00952 0.01958  174 GLU A CD  
1347 O  OE1 . GLU A 279 ? 0.15375 0.10771 0.16911 -0.01096 -0.01069 0.02458  174 GLU A OE1 
1348 O  OE2 . GLU A 279 ? 0.13838 0.08905 0.15662 -0.00939 -0.00817 0.01598  174 GLU A OE2 
1349 N  N   . PRO A 280 ? 0.12282 0.07789 0.14873 -0.00148 -0.01091 0.01953  175 PRO A N   
1350 C  CA  . PRO A 280 ? 0.10517 0.05884 0.13605 0.00093  -0.00872 0.01526  175 PRO A CA  
1351 C  C   . PRO A 280 ? 0.10712 0.06075 0.13364 -0.00049 -0.00575 0.00968  175 PRO A C   
1352 O  O   . PRO A 280 ? 0.12976 0.08468 0.15734 0.00095  -0.00372 0.00629  175 PRO A O   
1353 C  CB  . PRO A 280 ? 0.16349 0.10997 0.20168 0.00237  -0.00843 0.01608  175 PRO A CB  
1354 C  CG  . PRO A 280 ? 0.31332 0.25720 0.35025 0.00068  -0.01090 0.02148  175 PRO A CG  
1355 C  CD  . PRO A 280 ? 0.16074 0.11056 0.19000 -0.00162 -0.01253 0.02417  175 PRO A CD  
1356 N  N   . SER A 281 ? 0.09066 0.04300 0.11242 -0.00343 -0.00555 0.00881  176 SER A N   
1357 C  CA  . SER A 281 ? 0.09076 0.04208 0.10868 -0.00474 -0.00343 0.00363  176 SER A CA  
1358 C  C   . SER A 281 ? 0.14200 0.09895 0.15433 -0.00503 -0.00340 0.00219  176 SER A C   
1359 O  O   . SER A 281 ? 0.15442 0.11047 0.16282 -0.00596 -0.00202 -0.00167 176 SER A O   
1360 C  CB  . SER A 281 ? 0.16253 0.11049 0.17865 -0.00794 -0.00371 0.00289  176 SER A CB  
1361 O  OG  . SER A 281 ? 0.16786 0.12039 0.18079 -0.01007 -0.00546 0.00565  176 SER A OG  
1362 N  N   . VAL A 282 ? 0.10230 0.06443 0.11371 -0.00439 -0.00501 0.00507  177 VAL A N   
1363 C  CA  . VAL A 282 ? 0.10396 0.07053 0.11091 -0.00442 -0.00496 0.00373  177 VAL A CA  
1364 C  C   . VAL A 282 ? 0.10595 0.07388 0.11559 -0.00221 -0.00401 0.00318  177 VAL A C   
1365 O  O   . VAL A 282 ? 0.13028 0.09608 0.14562 -0.00059 -0.00319 0.00326  177 VAL A O   
1366 C  CB  . VAL A 282 ? 0.09103 0.06229 0.09522 -0.00542 -0.00689 0.00633  177 VAL A CB  
1367 C  CG1 . VAL A 282 ? 0.15297 0.12356 0.15598 -0.00793 -0.00729 0.00676  177 VAL A CG1 
1368 C  CG2 . VAL A 282 ? 0.11286 0.08595 0.11924 -0.00445 -0.00849 0.01006  177 VAL A CG2 
1369 N  N   . CYS A 283 ? 0.07824 0.04955 0.08465 -0.00214 -0.00392 0.00237  178 CYS A N   
1370 C  CA  . CYS A 283 ? 0.07418 0.04694 0.08335 -0.00070 -0.00267 0.00157  178 CYS A CA  
1371 C  C   . CYS A 283 ? 0.10776 0.08487 0.11827 -0.00019 -0.00515 0.00416  178 CYS A C   
1372 O  O   . CYS A 283 ? 0.09911 0.07862 0.10533 -0.00097 -0.00613 0.00428  178 CYS A O   
1373 C  CB  . CYS A 283 ? 0.07814 0.05055 0.08224 -0.00142 -0.00072 -0.00106 178 CYS A CB  
1374 S  SG  . CYS A 283 ? 0.09420 0.06629 0.10209 -0.00039 0.00296  -0.00313 178 CYS A SG  
1375 N  N   A THR A 284 ? 0.08062 0.05871 0.09725 0.00118  -0.00634 0.00601  179 THR A N   
1376 N  N   B THR A 284 ? 0.08065 0.05873 0.09717 0.00115  -0.00635 0.00601  179 THR A N   
1377 C  CA  A THR A 284 ? 0.06499 0.04706 0.08210 0.00133  -0.00946 0.00855  179 THR A CA  
1378 C  CA  B THR A 284 ? 0.06489 0.04698 0.08186 0.00130  -0.00938 0.00843  179 THR A CA  
1379 C  C   A THR A 284 ? 0.07004 0.05510 0.09077 0.00196  -0.00912 0.00725  179 THR A C   
1380 C  C   B THR A 284 ? 0.07059 0.05559 0.09115 0.00192  -0.00897 0.00710  179 THR A C   
1381 O  O   A THR A 284 ? 0.07756 0.06241 0.10496 0.00320  -0.00755 0.00633  179 THR A O   
1382 O  O   B THR A 284 ? 0.07695 0.06164 0.10391 0.00310  -0.00720 0.00602  179 THR A O   
1383 C  CB  A THR A 284 ? 0.06812 0.04956 0.08935 0.00223  -0.01201 0.01209  179 THR A CB  
1384 C  CB  B THR A 284 ? 0.06851 0.05015 0.08929 0.00212  -0.01201 0.01200  179 THR A CB  
1385 O  OG1 A THR A 284 ? 0.08925 0.06744 0.10722 0.00109  -0.01192 0.01341  179 THR A OG1 
1386 O  OG1 B THR A 284 ? 0.06966 0.04963 0.09863 0.00409  -0.01101 0.01160  179 THR A OG1 
1387 C  CG2 A THR A 284 ? 0.07968 0.06532 0.10002 0.00209  -0.01582 0.01483  179 THR A CG2 
1388 C  CG2 B THR A 284 ? 0.08686 0.06542 0.10385 0.00085  -0.01195 0.01333  179 THR A CG2 
1389 N  N   . VAL A 285 ? 0.06099 0.04879 0.07796 0.00100  -0.01029 0.00692  180 VAL A N   
1390 C  CA  . VAL A 285 ? 0.06897 0.05875 0.08809 0.00078  -0.00940 0.00513  180 VAL A CA  
1391 C  C   . VAL A 285 ? 0.06073 0.05458 0.08258 0.00066  -0.01288 0.00632  180 VAL A C   
1392 O  O   . VAL A 285 ? 0.08408 0.07916 0.10075 -0.00017 -0.01525 0.00707  180 VAL A O   
1393 C  CB  . VAL A 285 ? 0.06945 0.05794 0.08200 -0.00036 -0.00789 0.00334  180 VAL A CB  
1394 C  CG1 . VAL A 285 ? 0.09124 0.08064 0.10614 -0.00095 -0.00655 0.00180  180 VAL A CG1 
1395 C  CG2 . VAL A 285 ? 0.07661 0.06136 0.08572 -0.00047 -0.00537 0.00234  180 VAL A CG2 
1396 N  N   . GLY A 286 ? 0.05932 0.05565 0.08947 0.00133  -0.01313 0.00616  181 GLY A N   
1397 C  CA  . GLY A 286 ? 0.07924 0.07995 0.11253 0.00077  -0.01679 0.00668  181 GLY A CA  
1398 C  C   . GLY A 286 ? 0.06492 0.06649 0.09790 -0.00086 -0.01533 0.00403  181 GLY A C   
1399 O  O   . GLY A 286 ? 0.07201 0.07075 0.10276 -0.00135 -0.01146 0.00236  181 GLY A O   
1400 N  N   . ALA A 287 ? 0.05940 0.06457 0.09445 -0.00192 -0.01874 0.00381  182 ALA A N   
1401 C  CA  . ALA A 287 ? 0.07169 0.07712 0.10660 -0.00385 -0.01786 0.00130  182 ALA A CA  
1402 C  C   . ALA A 287 ? 0.07413 0.08381 0.11984 -0.00458 -0.01840 0.00063  182 ALA A C   
1403 O  O   . ALA A 287 ? 0.06839 0.08245 0.12052 -0.00390 -0.02221 0.00205  182 ALA A O   
1404 C  CB  . ALA A 287 ? 0.06180 0.06758 0.08966 -0.00519 -0.02118 0.00045  182 ALA A CB  
1405 N  N   . SER A 288 ? 0.05909 0.06759 0.10679 -0.00618 -0.01489 -0.00133 183 SER A N   
1406 C  CA  . SER A 288 ? 0.05950 0.07231 0.11772 -0.00772 -0.01493 -0.00238 183 SER A CA  
1407 C  C   . SER A 288 ? 0.06144 0.07295 0.11729 -0.01062 -0.01538 -0.00448 183 SER A C   
1408 O  O   . SER A 288 ? 0.08316 0.08974 0.12975 -0.01104 -0.01455 -0.00522 183 SER A O   
1409 C  CB  . SER A 288 ? 0.06745 0.08003 0.13210 -0.00737 -0.00907 -0.00269 183 SER A CB  
1410 O  OG  . SER A 288 ? 0.11213 0.11882 0.16853 -0.00841 -0.00473 -0.00342 183 SER A OG  
1411 N  N   . ASP A 289 ? 0.06248 0.07840 0.12779 -0.01268 -0.01666 -0.00561 184 ASP A N   
1412 C  CA  . ASP A 289 ? 0.06526 0.07943 0.12954 -0.01584 -0.01700 -0.00788 184 ASP A CA  
1413 C  C   . ASP A 289 ? 0.08469 0.09807 0.15566 -0.01797 -0.01161 -0.00842 184 ASP A C   
1414 O  O   . ASP A 289 ? 0.06780 0.08232 0.14345 -0.01694 -0.00737 -0.00737 184 ASP A O   
1415 C  CB  . ASP A 289 ? 0.06770 0.08690 0.13567 -0.01753 -0.02350 -0.00921 184 ASP A CB  
1416 C  CG  . ASP A 289 ? 0.11448 0.14163 0.19747 -0.01844 -0.02532 -0.00903 184 ASP A CG  
1417 O  OD1 . ASP A 289 ? 0.07987 0.10860 0.17157 -0.01842 -0.02052 -0.00857 184 ASP A OD1 
1418 O  OD2 . ASP A 289 ? 0.10899 0.14111 0.19480 -0.01916 -0.03173 -0.00938 184 ASP A OD2 
1419 N  N   . ARG A 290 ? 0.07659 0.08747 0.14756 -0.02119 -0.01142 -0.01022 185 ARG A N   
1420 C  CA  . ARG A 290 ? 0.08141 0.08979 0.15619 -0.02352 -0.00554 -0.01006 185 ARG A CA  
1421 C  C   . ARG A 290 ? 0.09069 0.10643 0.18024 -0.02521 -0.00395 -0.01028 185 ARG A C   
1422 O  O   . ARG A 290 ? 0.13040 0.14489 0.22363 -0.02725 0.00187  -0.00992 185 ARG A O   
1423 C  CB  . ARG A 290 ? 0.14569 0.14815 0.21670 -0.02658 -0.00548 -0.01154 185 ARG A CB  
1424 C  CG  . ARG A 290 ? 0.18005 0.18661 0.25817 -0.02945 -0.01023 -0.01411 185 ARG A CG  
1425 C  CD  . ARG A 290 ? 0.29356 0.29365 0.37037 -0.03312 -0.00919 -0.01586 185 ARG A CD  
1426 N  NE  . ARG A 290 ? 0.37669 0.36963 0.44183 -0.03166 -0.01082 -0.01691 185 ARG A NE  
1427 C  CZ  . ARG A 290 ? 0.60285 0.58709 0.66193 -0.03193 -0.00758 -0.01624 185 ARG A CZ  
1428 N  NH1 . ARG A 290 ? 0.45770 0.43861 0.51938 -0.03386 -0.00249 -0.01406 185 ARG A NH1 
1429 N  NH2 . ARG A 290 ? 0.51633 0.49509 0.56668 -0.03024 -0.00944 -0.01767 185 ARG A NH2 
1430 N  N   . TYR A 291 ? 0.07026 0.09376 0.16842 -0.02433 -0.00875 -0.01060 186 TYR A N   
1431 C  CA  . TYR A 291 ? 0.09268 0.12457 0.20683 -0.02507 -0.00776 -0.01073 186 TYR A CA  
1432 C  C   . TYR A 291 ? 0.09053 0.12582 0.20876 -0.02099 -0.00617 -0.00913 186 TYR A C   
1433 O  O   . TYR A 291 ? 0.08487 0.12818 0.21759 -0.02041 -0.00667 -0.00918 186 TYR A O   
1434 C  CB  . TYR A 291 ? 0.06881 0.10754 0.19160 -0.02701 -0.01501 -0.01218 186 TYR A CB  
1435 C  CG  . TYR A 291 ? 0.13918 0.17441 0.25952 -0.03154 -0.01635 -0.01457 186 TYR A CG  
1436 C  CD1 . TYR A 291 ? 0.27396 0.30831 0.40113 -0.03546 -0.01124 -0.01537 186 TYR A CD1 
1437 C  CD2 . TYR A 291 ? 0.17983 0.21088 0.28916 -0.03174 -0.02146 -0.01595 186 TYR A CD2 
1438 C  CE1 . TYR A 291 ? 0.26661 0.29614 0.38981 -0.03915 -0.01225 -0.01727 186 TYR A CE1 
1439 C  CE2 . TYR A 291 ? 0.28431 0.31113 0.39135 -0.03564 -0.02237 -0.01866 186 TYR A CE2 
1440 C  CZ  . TYR A 291 ? 0.35280 0.37856 0.46690 -0.03926 -0.01793 -0.01920 186 TYR A CZ  
1441 O  OH  . TYR A 291 ? 0.47725 0.49743 0.58701 -0.04250 -0.01861 -0.02146 186 TYR A OH  
1442 N  N   . ASP A 292 ? 0.06354 0.09288 0.17016 -0.01813 -0.00430 -0.00789 187 ASP A N   
1443 C  CA  . ASP A 292 ? 0.06880 0.09939 0.17744 -0.01429 -0.00260 -0.00668 187 ASP A CA  
1444 C  C   . ASP A 292 ? 0.07089 0.10742 0.18628 -0.01174 -0.00942 -0.00550 187 ASP A C   
1445 O  O   . ASP A 292 ? 0.12011 0.16053 0.24491 -0.00901 -0.00843 -0.00480 187 ASP A O   
1446 C  CB  . ASP A 292 ? 0.07441 0.10751 0.19268 -0.01455 0.00485  -0.00744 187 ASP A CB  
1447 C  CG  . ASP A 292 ? 0.17799 0.20350 0.28539 -0.01583 0.01196  -0.00762 187 ASP A CG  
1448 O  OD1 . ASP A 292 ? 0.11609 0.13469 0.20967 -0.01590 0.01060  -0.00692 187 ASP A OD1 
1449 O  OD2 . ASP A 292 ? 0.14555 0.17223 0.25829 -0.01679 0.01893  -0.00841 187 ASP A OD2 
1450 N  N   . ARG A 293 ? 0.08365 0.12066 0.19419 -0.01255 -0.01633 -0.00525 188 ARG A N   
1451 C  CA  . ARG A 293 ? 0.06048 0.10113 0.17255 -0.01005 -0.02320 -0.00324 188 ARG A CA  
1452 C  C   . ARG A 293 ? 0.06038 0.09466 0.15789 -0.00799 -0.02402 -0.00162 188 ARG A C   
1453 O  O   . ARG A 293 ? 0.09108 0.11940 0.17682 -0.00920 -0.02195 -0.00259 188 ARG A O   
1454 C  CB  . ARG A 293 ? 0.06318 0.10849 0.17746 -0.01248 -0.03059 -0.00393 188 ARG A CB  
1455 C  CG  . ARG A 293 ? 0.07817 0.12994 0.20709 -0.01529 -0.03010 -0.00583 188 ARG A CG  
1456 C  CD  . ARG A 293 ? 0.10828 0.16419 0.23822 -0.01810 -0.03788 -0.00701 188 ARG A CD  
1457 N  NE  . ARG A 293 ? 0.15805 0.20731 0.27498 -0.02101 -0.03752 -0.00931 188 ARG A NE  
1458 C  CZ  . ARG A 293 ? 0.07351 0.12349 0.19161 -0.02505 -0.03964 -0.01217 188 ARG A CZ  
1459 N  NH1 . ARG A 293 ? 0.11557 0.17162 0.24346 -0.02645 -0.04104 -0.01272 188 ARG A NH1 
1460 N  NH2 . ARG A 293 ? 0.11597 0.15901 0.22241 -0.02707 -0.03909 -0.01439 188 ARG A NH2 
1461 N  N   . ARG A 294 ? 0.06046 0.09598 0.15966 -0.00482 -0.02691 0.00101  189 ARG A N   
1462 C  CA  . ARG A 294 ? 0.07347 0.10412 0.15942 -0.00366 -0.02913 0.00284  189 ARG A CA  
1463 C  C   . ARG A 294 ? 0.06426 0.09484 0.14136 -0.00624 -0.03380 0.00192  189 ARG A C   
1464 O  O   . ARG A 294 ? 0.08446 0.12031 0.16688 -0.00771 -0.03902 0.00158  189 ARG A O   
1465 C  CB  . ARG A 294 ? 0.07710 0.10949 0.16706 -0.00046 -0.03305 0.00641  189 ARG A CB  
1466 C  CG  . ARG A 294 ? 0.10314 0.13076 0.17963 0.00015  -0.03521 0.00868  189 ARG A CG  
1467 C  CD  . ARG A 294 ? 0.10473 0.13264 0.18492 0.00317  -0.03863 0.01282  189 ARG A CD  
1468 N  NE  . ARG A 294 ? 0.11975 0.15384 0.20760 0.00352  -0.04579 0.01504  189 ARG A NE  
1469 C  CZ  . ARG A 294 ? 0.19443 0.22970 0.27466 0.00239  -0.05238 0.01733  189 ARG A CZ  
1470 N  NH1 . ARG A 294 ? 0.14941 0.18016 0.21439 0.00097  -0.05220 0.01773  189 ARG A NH1 
1471 N  NH2 . ARG A 294 ? 0.23888 0.27947 0.32545 0.00260  -0.05827 0.01897  189 ARG A NH2 
1472 N  N   . SER A 295 ? 0.06441 0.08928 0.12853 -0.00685 -0.03192 0.00115  190 SER A N   
1473 C  CA  . SER A 295 ? 0.06800 0.09231 0.12310 -0.00900 -0.03567 -0.00028 190 SER A CA  
1474 C  C   . SER A 295 ? 0.07230 0.10013 0.12541 -0.00851 -0.04248 0.00223  190 SER A C   
1475 O  O   . SER A 295 ? 0.09760 0.12522 0.15060 -0.00611 -0.04348 0.00573  190 SER A O   
1476 C  CB  . SER A 295 ? 0.08136 0.09941 0.12387 -0.00896 -0.03234 -0.00121 190 SER A CB  
1477 O  OG  . SER A 295 ? 0.08366 0.09788 0.12656 -0.00948 -0.02680 -0.00305 190 SER A OG  
1478 N  N   . SER A 296 ? 0.07845 0.10910 0.12946 -0.01100 -0.04741 0.00049  191 SER A N   
1479 C  CA  . SER A 296 ? 0.08241 0.11726 0.13267 -0.01075 -0.05467 0.00331  191 SER A CA  
1480 C  C   . SER A 296 ? 0.12985 0.16140 0.16753 -0.00964 -0.05554 0.00621  191 SER A C   
1481 O  O   . SER A 296 ? 0.15391 0.18791 0.19164 -0.00863 -0.06073 0.01019  191 SER A O   
1482 C  CB  . SER A 296 ? 0.12786 0.16618 0.17679 -0.01413 -0.06004 0.00036  191 SER A CB  
1483 O  OG  . SER A 296 ? 0.24997 0.28356 0.28651 -0.01606 -0.05779 -0.00318 191 SER A OG  
1484 N  N   . PHE A 297 ? 0.08671 0.11300 0.11432 -0.00989 -0.05074 0.00454  192 PHE A N   
1485 C  CA  . PHE A 297 ? 0.08737 0.11071 0.10369 -0.00920 -0.05036 0.00699  192 PHE A CA  
1486 C  C   . PHE A 297 ? 0.11122 0.13155 0.13020 -0.00654 -0.04648 0.01005  192 PHE A C   
1487 O  O   . PHE A 297 ? 0.12125 0.13921 0.13234 -0.00611 -0.04609 0.01262  192 PHE A O   
1488 C  CB  . PHE A 297 ? 0.11719 0.13708 0.12254 -0.01078 -0.04698 0.00317  192 PHE A CB  
1489 C  CG  . PHE A 297 ? 0.09371 0.11050 0.10286 -0.01058 -0.04138 -0.00017 192 PHE A CG  
1490 C  CD1 . PHE A 297 ? 0.12304 0.13644 0.13296 -0.00866 -0.03641 0.00102  192 PHE A CD1 
1491 C  CD2 . PHE A 297 ? 0.10100 0.11809 0.11351 -0.01248 -0.04143 -0.00418 192 PHE A CD2 
1492 C  CE1 . PHE A 297 ? 0.11081 0.12122 0.12320 -0.00853 -0.03187 -0.00135 192 PHE A CE1 
1493 C  CE2 . PHE A 297 ? 0.09489 0.10839 0.11034 -0.01237 -0.03642 -0.00641 192 PHE A CE2 
1494 C  CZ  . PHE A 297 ? 0.13089 0.14119 0.14602 -0.01033 -0.03182 -0.00480 192 PHE A CZ  
1495 N  N   . SER A 298 ? 0.07684 0.09684 0.10601 -0.00510 -0.04304 0.00946  193 SER A N   
1496 C  CA  . SER A 298 ? 0.07322 0.08923 0.10268 -0.00309 -0.03849 0.01096  193 SER A CA  
1497 C  C   . SER A 298 ? 0.07611 0.09209 0.10794 -0.00113 -0.04129 0.01576  193 SER A C   
1498 O  O   . SER A 298 ? 0.10900 0.12854 0.14952 -0.00004 -0.04532 0.01782  193 SER A O   
1499 C  CB  . SER A 298 ? 0.10275 0.11819 0.14136 -0.00226 -0.03383 0.00886  193 SER A CB  
1500 O  OG  . SER A 298 ? 0.09423 0.10553 0.13199 -0.00059 -0.02970 0.00982  193 SER A OG  
1501 N  N   . ASN A 299 ? 0.07677 0.08862 0.10195 -0.00064 -0.03916 0.01766  194 ASN A N   
1502 C  CA  . ASN A 299 ? 0.07944 0.08963 0.10836 0.00137  -0.04071 0.02214  194 ASN A CA  
1503 C  C   . ASN A 299 ? 0.11379 0.12335 0.15491 0.00375  -0.03780 0.02130  194 ASN A C   
1504 O  O   . ASN A 299 ? 0.11051 0.12022 0.15505 0.00354  -0.03362 0.01745  194 ASN A O   
1505 C  CB  . ASN A 299 ? 0.09066 0.09625 0.11052 0.00085  -0.03842 0.02401  194 ASN A CB  
1506 C  CG  . ASN A 299 ? 0.11298 0.11942 0.12167 -0.00119 -0.04165 0.02631  194 ASN A CG  
1507 O  OD1 . ASN A 299 ? 0.10977 0.11979 0.11669 -0.00208 -0.04642 0.02695  194 ASN A OD1 
1508 N  ND2 . ASN A 299 ? 0.10360 0.10702 0.10435 -0.00227 -0.03890 0.02723  194 ASN A ND2 
1509 N  N   . TYR A 300 ? 0.10245 0.11104 0.15012 0.00605  -0.03993 0.02501  195 TYR A N   
1510 C  CA  . TYR A 300 ? 0.09055 0.09870 0.15081 0.00869  -0.03717 0.02403  195 TYR A CA  
1511 C  C   . TYR A 300 ? 0.10340 0.10629 0.16499 0.01069  -0.03713 0.02753  195 TYR A C   
1512 O  O   . TYR A 300 ? 0.13248 0.13193 0.18465 0.00951  -0.03830 0.03039  195 TYR A O   
1513 C  CB  . TYR A 300 ? 0.10358 0.11811 0.17633 0.00998  -0.04095 0.02432  195 TYR A CB  
1514 C  CG  . TYR A 300 ? 0.13344 0.15060 0.20570 0.01031  -0.04886 0.02924  195 TYR A CG  
1515 C  CD1 . TYR A 300 ? 0.11251 0.12736 0.18924 0.01280  -0.05109 0.03341  195 TYR A CD1 
1516 C  CD2 . TYR A 300 ? 0.15691 0.17801 0.22217 0.00766  -0.05334 0.02909  195 TYR A CD2 
1517 C  CE1 . TYR A 300 ? 0.23389 0.25005 0.30620 0.01229  -0.05652 0.03705  195 TYR A CE1 
1518 C  CE2 . TYR A 300 ? 0.17463 0.19717 0.23563 0.00724  -0.05882 0.03245  195 TYR A CE2 
1519 C  CZ  . TYR A 300 ? 0.24029 0.26040 0.30449 0.00954  -0.06028 0.03653  195 TYR A CZ  
1520 O  OH  . TYR A 300 ? 0.33214 0.35360 0.39112 0.00897  -0.06552 0.03979  195 TYR A OH  
1521 N  N   . GLY A 301 ? 0.09393 0.09596 0.16753 0.01360  -0.03546 0.02720  196 GLY A N   
1522 C  CA  . GLY A 301 ? 0.10759 0.10398 0.18407 0.01573  -0.03575 0.03043  196 GLY A CA  
1523 C  C   . GLY A 301 ? 0.10615 0.09749 0.18533 0.01660  -0.02900 0.02651  196 GLY A C   
1524 O  O   . GLY A 301 ? 0.12865 0.12057 0.20538 0.01529  -0.02409 0.02171  196 GLY A O   
1525 N  N   . SER A 302 ? 0.12351 0.10931 0.20745 0.01877  -0.02909 0.02880  197 SER A N   
1526 C  CA  . SER A 302 ? 0.12380 0.10429 0.21128 0.01980  -0.02296 0.02467  197 SER A CA  
1527 C  C   . SER A 302 ? 0.10654 0.08313 0.18170 0.01659  -0.01887 0.02169  197 SER A C   
1528 O  O   . SER A 302 ? 0.14918 0.12285 0.22521 0.01666  -0.01352 0.01696  197 SER A O   
1529 C  CB  . SER A 302 ? 0.18223 0.15751 0.27518 0.02191  -0.02372 0.02706  197 SER A CB  
1530 O  OG  . SER A 302 ? 0.25225 0.22361 0.33602 0.02002  -0.02679 0.03166  197 SER A OG  
1531 N  N   . VAL A 303 ? 0.10345 0.08019 0.16732 0.01376  -0.02118 0.02410  198 VAL A N   
1532 C  CA  . VAL A 303 ? 0.08373 0.05758 0.13750 0.01093  -0.01772 0.02141  198 VAL A CA  
1533 C  C   . VAL A 303 ? 0.09107 0.06883 0.14043 0.00945  -0.01498 0.01710  198 VAL A C   
1534 O  O   . VAL A 303 ? 0.14982 0.12528 0.19244 0.00762  -0.01185 0.01423  198 VAL A O   
1535 C  CB  . VAL A 303 ? 0.13830 0.11093 0.18302 0.00858  -0.02057 0.02557  198 VAL A CB  
1536 C  CG1 . VAL A 303 ? 0.17345 0.15206 0.21179 0.00706  -0.02342 0.02679  198 VAL A CG1 
1537 C  CG2 . VAL A 303 ? 0.20445 0.17294 0.24241 0.00615  -0.01716 0.02331  198 VAL A CG2 
1538 N  N   . LEU A 304 ? 0.07819 0.06150 0.13170 0.01011  -0.01607 0.01650  199 LEU A N   
1539 C  CA  . LEU A 304 ? 0.07037 0.05619 0.12009 0.00859  -0.01311 0.01266  199 LEU A CA  
1540 C  C   . LEU A 304 ? 0.07915 0.06214 0.13169 0.00917  -0.00759 0.00847  199 LEU A C   
1541 O  O   . LEU A 304 ? 0.11483 0.09675 0.17660 0.01144  -0.00603 0.00774  199 LEU A O   
1542 C  CB  . LEU A 304 ? 0.08152 0.07348 0.13619 0.00878  -0.01520 0.01270  199 LEU A CB  
1543 C  CG  . LEU A 304 ? 0.13142 0.12635 0.17839 0.00678  -0.01891 0.01421  199 LEU A CG  
1544 C  CD1 . LEU A 304 ? 0.15085 0.14545 0.19578 0.00706  -0.02378 0.01889  199 LEU A CD1 
1545 C  CD2 . LEU A 304 ? 0.16943 0.16989 0.22118 0.00633  -0.02022 0.01290  199 LEU A CD2 
1546 N  N   . ASP A 305 ? 0.06889 0.05073 0.11346 0.00718  -0.00462 0.00564  200 ASP A N   
1547 C  CA  . ASP A 305 ? 0.07056 0.04968 0.11519 0.00713  0.00064  0.00159  200 ASP A CA  
1548 C  C   . ASP A 305 ? 0.06870 0.05128 0.11486 0.00653  0.00335  -0.00053 200 ASP A C   
1549 O  O   . ASP A 305 ? 0.10092 0.08252 0.15037 0.00696  0.00806  -0.00355 200 ASP A O   
1550 C  CB  . ASP A 305 ? 0.07164 0.04660 0.10577 0.00511  0.00194  0.00006  200 ASP A CB  
1551 C  CG  . ASP A 305 ? 0.10676 0.07771 0.13994 0.00511  0.00032  0.00149  200 ASP A CG  
1552 O  OD1 . ASP A 305 ? 0.13232 0.09930 0.16977 0.00620  0.00250  -0.00022 200 ASP A OD1 
1553 O  OD2 . ASP A 305 ? 0.09991 0.07137 0.12856 0.00394  -0.00277 0.00414  200 ASP A OD2 
1554 N  N   . ILE A 306 ? 0.07144 0.05758 0.11480 0.00525  0.00094  0.00072  201 ILE A N   
1555 C  CA  . ILE A 306 ? 0.07190 0.05990 0.11427 0.00381  0.00362  -0.00112 201 ILE A CA  
1556 C  C   . ILE A 306 ? 0.09129 0.08325 0.13346 0.00284  -0.00024 0.00054  201 ILE A C   
1557 O  O   . ILE A 306 ? 0.08294 0.07519 0.12120 0.00276  -0.00428 0.00256  201 ILE A O   
1558 C  CB  . ILE A 306 ? 0.08798 0.07164 0.11982 0.00213  0.00658  -0.00297 201 ILE A CB  
1559 C  CG1 . ILE A 306 ? 0.09172 0.07584 0.12199 0.00056  0.01017  -0.00451 201 ILE A CG1 
1560 C  CG2 . ILE A 306 ? 0.09136 0.07394 0.11464 0.00116  0.00313  -0.00144 201 ILE A CG2 
1561 C  CD1 . ILE A 306 ? 0.11018 0.09481 0.14734 0.00113  0.01531  -0.00680 201 ILE A CD1 
1562 N  N   . PHE A 307 ? 0.06066 0.05553 0.10684 0.00184  0.00122  -0.00052 202 PHE A N   
1563 C  CA  . PHE A 307 ? 0.05890 0.05652 0.10389 0.00034  -0.00190 0.00011  202 PHE A CA  
1564 C  C   . PHE A 307 ? 0.08907 0.08391 0.12708 -0.00168 0.00086  -0.00124 202 PHE A C   
1565 O  O   . PHE A 307 ? 0.09129 0.08370 0.12795 -0.00221 0.00548  -0.00253 202 PHE A O   
1566 C  CB  . PHE A 307 ? 0.06856 0.07190 0.12511 0.00037  -0.00315 0.00011  202 PHE A CB  
1567 C  CG  . PHE A 307 ? 0.07042 0.07711 0.13315 0.00222  -0.00813 0.00238  202 PHE A CG  
1568 C  CD1 . PHE A 307 ? 0.08952 0.09616 0.15954 0.00478  -0.00737 0.00310  202 PHE A CD1 
1569 C  CD2 . PHE A 307 ? 0.07384 0.08325 0.13461 0.00139  -0.01371 0.00384  202 PHE A CD2 
1570 C  CE1 . PHE A 307 ? 0.12330 0.13240 0.19885 0.00663  -0.01256 0.00600  202 PHE A CE1 
1571 C  CE2 . PHE A 307 ? 0.08276 0.09490 0.14748 0.00282  -0.01883 0.00653  202 PHE A CE2 
1572 C  CZ  . PHE A 307 ? 0.12877 0.14081 0.20135 0.00555  -0.01851 0.00801  202 PHE A CZ  
1573 N  N   . GLY A 308 ? 0.06938 0.06411 0.10239 -0.00278 -0.00197 -0.00089 203 GLY A N   
1574 C  CA  . GLY A 308 ? 0.08111 0.07311 0.10920 -0.00453 -0.00007 -0.00176 203 GLY A CA  
1575 C  C   . GLY A 308 ? 0.07111 0.06524 0.10091 -0.00585 -0.00310 -0.00212 203 GLY A C   
1576 O  O   . GLY A 308 ? 0.06832 0.06592 0.10069 -0.00545 -0.00708 -0.00172 203 GLY A O   
1577 N  N   . PRO A 309 ? 0.08001 0.07154 0.10755 -0.00757 -0.00157 -0.00286 204 PRO A N   
1578 C  CA  . PRO A 309 ? 0.06271 0.05541 0.09202 -0.00914 -0.00425 -0.00387 204 PRO A CA  
1579 C  C   . PRO A 309 ? 0.06229 0.05493 0.08592 -0.00834 -0.00816 -0.00423 204 PRO A C   
1580 O  O   . PRO A 309 ? 0.08247 0.07187 0.09902 -0.00730 -0.00775 -0.00398 204 PRO A O   
1581 C  CB  . PRO A 309 ? 0.08547 0.07329 0.11191 -0.01087 -0.00121 -0.00414 204 PRO A CB  
1582 C  CG  . PRO A 309 ? 0.08697 0.07330 0.11322 -0.01079 0.00346  -0.00322 204 PRO A CG  
1583 C  CD  . PRO A 309 ? 0.13556 0.12266 0.15923 -0.00844 0.00286  -0.00272 204 PRO A CD  
1584 N  N   . GLY A 310 ? 0.06253 0.05913 0.08936 -0.00897 -0.01195 -0.00494 205 GLY A N   
1585 C  CA  . GLY A 310 ? 0.06344 0.06034 0.08395 -0.00846 -0.01519 -0.00546 205 GLY A CA  
1586 C  C   . GLY A 310 ? 0.08952 0.08780 0.11008 -0.01029 -0.01835 -0.00779 205 GLY A C   
1587 O  O   . GLY A 310 ? 0.12535 0.12334 0.13958 -0.01011 -0.02019 -0.00889 205 GLY A O   
1588 N  N   . THR A 311 ? 0.06795 0.06777 0.09538 -0.01232 -0.01885 -0.00895 206 THR A N   
1589 C  CA  . THR A 311 ? 0.07202 0.07298 0.09968 -0.01455 -0.02223 -0.01174 206 THR A CA  
1590 C  C   . THR A 311 ? 0.08403 0.07958 0.11120 -0.01621 -0.01980 -0.01403 206 THR A C   
1591 O  O   . THR A 311 ? 0.10788 0.10161 0.13984 -0.01709 -0.01658 -0.01317 206 THR A O   
1592 C  CB  . THR A 311 ? 0.07237 0.07946 0.10939 -0.01610 -0.02548 -0.01161 206 THR A CB  
1593 O  OG1 . THR A 311 ? 0.10868 0.12007 0.14609 -0.01420 -0.02830 -0.00898 206 THR A OG1 
1594 C  CG2 . THR A 311 ? 0.07758 0.08570 0.11475 -0.01899 -0.02930 -0.01499 206 THR A CG2 
1595 N  N   A ASP A 312 ? 0.07987 0.07248 0.10105 -0.01659 -0.02104 -0.01687 207 ASP A N   
1596 N  N   B ASP A 312 ? 0.08023 0.07286 0.10148 -0.01662 -0.02106 -0.01688 207 ASP A N   
1597 C  CA  A ASP A 312 ? 0.08815 0.07486 0.10920 -0.01808 -0.01945 -0.01938 207 ASP A CA  
1598 C  CA  B ASP A 312 ? 0.08839 0.07513 0.10971 -0.01812 -0.01938 -0.01929 207 ASP A CA  
1599 C  C   A ASP A 312 ? 0.08195 0.06306 0.10144 -0.01656 -0.01514 -0.01714 207 ASP A C   
1600 C  C   B ASP A 312 ? 0.08172 0.06298 0.10137 -0.01654 -0.01507 -0.01698 207 ASP A C   
1601 O  O   A ASP A 312 ? 0.11362 0.09148 0.13710 -0.01816 -0.01274 -0.01631 207 ASP A O   
1602 O  O   B ASP A 312 ? 0.11056 0.08891 0.13429 -0.01804 -0.01257 -0.01591 207 ASP A O   
1603 C  CB  A ASP A 312 ? 0.09724 0.08524 0.12640 -0.02166 -0.02064 -0.02098 207 ASP A CB  
1604 C  CB  B ASP A 312 ? 0.09756 0.08575 0.12725 -0.02167 -0.02048 -0.02072 207 ASP A CB  
1605 C  CG  A ASP A 312 ? 0.14703 0.13958 0.17657 -0.02356 -0.02574 -0.02394 207 ASP A CG  
1606 C  CG  B ASP A 312 ? 0.19310 0.17495 0.22267 -0.02383 -0.01985 -0.02394 207 ASP A CG  
1607 O  OD1 A ASP A 312 ? 0.15375 0.14611 0.17538 -0.02263 -0.02774 -0.02590 207 ASP A OD1 
1608 O  OD1 B ASP A 312 ? 0.21496 0.19237 0.23793 -0.02249 -0.01977 -0.02613 207 ASP A OD1 
1609 O  OD2 A ASP A 312 ? 0.17638 0.17312 0.21421 -0.02618 -0.02781 -0.02435 207 ASP A OD2 
1610 O  OD2 B ASP A 312 ? 0.26642 0.24765 0.30329 -0.02691 -0.01918 -0.02435 207 ASP A OD2 
1611 N  N   . ILE A 313 ? 0.07989 0.06001 0.09329 -0.01371 -0.01432 -0.01602 208 ILE A N   
1612 C  CA  . ILE A 313 ? 0.07887 0.05469 0.08979 -0.01194 -0.01126 -0.01357 208 ILE A CA  
1613 C  C   . ILE A 313 ? 0.08874 0.05890 0.09602 -0.01079 -0.01091 -0.01532 208 ILE A C   
1614 O  O   . ILE A 313 ? 0.09315 0.06446 0.09683 -0.00927 -0.01205 -0.01735 208 ILE A O   
1615 C  CB  . ILE A 313 ? 0.07406 0.05299 0.08196 -0.00966 -0.01095 -0.01122 208 ILE A CB  
1616 C  CG1 . ILE A 313 ? 0.07782 0.06184 0.09026 -0.01027 -0.01129 -0.00961 208 ILE A CG1 
1617 C  CG2 . ILE A 313 ? 0.09552 0.07013 0.10015 -0.00807 -0.00851 -0.00905 208 ILE A CG2 
1618 C  CD1 . ILE A 313 ? 0.10071 0.08374 0.11844 -0.01184 -0.00859 -0.00842 208 ILE A CD1 
1619 N  N   . LEU A 314 ? 0.10442 0.06836 0.11297 -0.01151 -0.00912 -0.01445 209 LEU A N   
1620 C  CA  . LEU A 314 ? 0.09205 0.04965 0.09854 -0.01003 -0.00889 -0.01567 209 LEU A CA  
1621 C  C   . LEU A 314 ? 0.10308 0.05952 0.10574 -0.00690 -0.00809 -0.01290 209 LEU A C   
1622 O  O   . LEU A 314 ? 0.10693 0.06296 0.10850 -0.00698 -0.00678 -0.00936 209 LEU A O   
1623 C  CB  . LEU A 314 ? 0.09818 0.04894 0.10780 -0.01232 -0.00760 -0.01506 209 LEU A CB  
1624 C  CG  . LEU A 314 ? 0.13444 0.07706 0.14317 -0.01079 -0.00740 -0.01567 209 LEU A CG  
1625 C  CD1 . LEU A 314 ? 0.19240 0.13518 0.20149 -0.01031 -0.00898 -0.02109 209 LEU A CD1 
1626 C  CD2 . LEU A 314 ? 0.17387 0.10979 0.18562 -0.01376 -0.00587 -0.01384 209 LEU A CD2 
1627 N  N   . SER A 315 ? 0.09120 0.04730 0.09204 -0.00430 -0.00881 -0.01479 210 SER A N   
1628 C  CA  . SER A 315 ? 0.08995 0.04560 0.08847 -0.00133 -0.00863 -0.01240 210 SER A CA  
1629 C  C   . SER A 315 ? 0.09370 0.04704 0.09301 0.00133  -0.00901 -0.01513 210 SER A C   
1630 O  O   . SER A 315 ? 0.11247 0.06356 0.11339 0.00076  -0.00905 -0.01898 210 SER A O   
1631 C  CB  . SER A 315 ? 0.08339 0.04583 0.07985 -0.00082 -0.00883 -0.01121 210 SER A CB  
1632 O  OG  . SER A 315 ? 0.09085 0.05272 0.08552 0.00134  -0.00889 -0.00869 210 SER A OG  
1633 N  N   . THR A 316 ? 0.09264 0.04674 0.09133 0.00426  -0.00931 -0.01342 211 THR A N   
1634 C  CA  . THR A 316 ? 0.09574 0.04888 0.09670 0.00743  -0.00942 -0.01584 211 THR A CA  
1635 C  C   . THR A 316 ? 0.10444 0.06342 0.10508 0.00763  -0.00862 -0.02037 211 THR A C   
1636 O  O   . THR A 316 ? 0.13040 0.09508 0.12841 0.00597  -0.00856 -0.02029 211 THR A O   
1637 C  CB  . THR A 316 ? 0.10119 0.05555 0.10244 0.01021  -0.01038 -0.01262 211 THR A CB  
1638 O  OG1 . THR A 316 ? 0.10454 0.06455 0.10284 0.00897  -0.01049 -0.01049 211 THR A OG1 
1639 C  CG2 . THR A 316 ? 0.13256 0.07945 0.13345 0.01060  -0.01148 -0.00842 211 THR A CG2 
1640 N  N   . TRP A 317 ? 0.09889 0.05598 0.10207 0.00974  -0.00784 -0.02429 212 TRP A N   
1641 C  CA  . TRP A 317 ? 0.10746 0.06956 0.10962 0.01007  -0.00636 -0.02904 212 TRP A CA  
1642 C  C   . TRP A 317 ? 0.12337 0.08512 0.13012 0.01409  -0.00512 -0.03128 212 TRP A C   
1643 O  O   . TRP A 317 ? 0.13074 0.08728 0.14172 0.01655  -0.00605 -0.02935 212 TRP A O   
1644 C  CB  . TRP A 317 ? 0.11777 0.07765 0.11795 0.00748  -0.00616 -0.03367 212 TRP A CB  
1645 C  CG  . TRP A 317 ? 0.10514 0.07116 0.10098 0.00642  -0.00501 -0.03770 212 TRP A CG  
1646 C  CD1 . TRP A 317 ? 0.12581 0.09184 0.12097 0.00739  -0.00295 -0.04366 212 TRP A CD1 
1647 C  CD2 . TRP A 317 ? 0.10916 0.08161 0.10015 0.00403  -0.00576 -0.03594 212 TRP A CD2 
1648 N  NE1 . TRP A 317 ? 0.13701 0.10929 0.12598 0.00540  -0.00231 -0.04549 212 TRP A NE1 
1649 C  CE2 . TRP A 317 ? 0.11872 0.09475 0.10530 0.00341  -0.00430 -0.04048 212 TRP A CE2 
1650 C  CE3 . TRP A 317 ? 0.10029 0.07541 0.09026 0.00244  -0.00739 -0.03103 212 TRP A CE3 
1651 C  CZ2 . TRP A 317 ? 0.11418 0.09605 0.09484 0.00109  -0.00494 -0.03948 212 TRP A CZ2 
1652 C  CZ3 . TRP A 317 ? 0.11418 0.09505 0.09960 0.00053  -0.00804 -0.03034 212 TRP A CZ3 
1653 C  CH2 . TRP A 317 ? 0.12290 0.10692 0.10352 -0.00015 -0.00702 -0.03416 212 TRP A CH2 
1654 N  N   . ILE A 318 ? 0.10302 0.07058 0.10909 0.01475  -0.00296 -0.03509 213 ILE A N   
1655 C  CA  . ILE A 318 ? 0.10609 0.07472 0.11800 0.01876  -0.00115 -0.03770 213 ILE A CA  
1656 C  C   . ILE A 318 ? 0.12253 0.08353 0.13808 0.02053  -0.00034 -0.04223 213 ILE A C   
1657 O  O   . ILE A 318 ? 0.14195 0.09744 0.15474 0.01808  -0.00083 -0.04432 213 ILE A O   
1658 C  CB  . ILE A 318 ? 0.10493 0.08205 0.11523 0.01865  0.00181  -0.04066 213 ILE A CB  
1659 C  CG1 . ILE A 318 ? 0.18689 0.16456 0.19017 0.01553  0.00335  -0.04532 213 ILE A CG1 
1660 C  CG2 . ILE A 318 ? 0.11314 0.09668 0.12159 0.01733  0.00085  -0.03569 213 ILE A CG2 
1661 C  CD1 . ILE A 318 ? 0.15951 0.14462 0.16043 0.01551  0.00721  -0.04900 213 ILE A CD1 
1662 N  N   . GLY A 319 ? 0.11796 0.07848 0.14089 0.02492  0.00066  -0.04357 214 GLY A N   
1663 C  CA  . GLY A 319 ? 0.14133 0.09337 0.16941 0.02741  0.00110  -0.04705 214 GLY A CA  
1664 C  C   . GLY A 319 ? 0.15660 0.09951 0.18620 0.02742  -0.00219 -0.04211 214 GLY A C   
1665 O  O   . GLY A 319 ? 0.18377 0.11817 0.21538 0.02765  -0.00201 -0.04440 214 GLY A O   
1666 N  N   . GLY A 320 ? 0.12992 0.07429 0.15805 0.02687  -0.00491 -0.03519 215 GLY A N   
1667 C  CA  . GLY A 320 ? 0.13875 0.07462 0.16693 0.02652  -0.00769 -0.02986 215 GLY A CA  
1668 C  C   . GLY A 320 ? 0.17005 0.10027 0.19356 0.02200  -0.00762 -0.03026 215 GLY A C   
1669 O  O   . GLY A 320 ? 0.19475 0.11578 0.21965 0.02168  -0.00872 -0.02800 215 GLY A O   
1670 N  N   A SER A 321 ? 0.13281 0.06840 0.15127 0.01840  -0.00644 -0.03300 216 SER A N   
1671 N  N   B SER A 321 ? 0.13338 0.06898 0.15177 0.01837  -0.00651 -0.03277 216 SER A N   
1672 C  CA  A SER A 321 ? 0.12654 0.05835 0.14196 0.01404  -0.00650 -0.03457 216 SER A CA  
1673 C  CA  B SER A 321 ? 0.12647 0.05819 0.14190 0.01404  -0.00655 -0.03435 216 SER A CA  
1674 C  C   A SER A 321 ? 0.11945 0.05496 0.13039 0.01047  -0.00762 -0.02977 216 SER A C   
1675 C  C   B SER A 321 ? 0.11920 0.05508 0.13000 0.01044  -0.00759 -0.02986 216 SER A C   
1676 O  O   A SER A 321 ? 0.13077 0.06982 0.14046 0.01135  -0.00838 -0.02502 216 SER A O   
1677 O  O   B SER A 321 ? 0.12931 0.06942 0.13871 0.01128  -0.00826 -0.02542 216 SER A O   
1678 C  CB  A SER A 321 ? 0.13722 0.07184 0.15072 0.01272  -0.00478 -0.04206 216 SER A CB  
1679 C  CB  B SER A 321 ? 0.13833 0.07227 0.15220 0.01286  -0.00483 -0.04191 216 SER A CB  
1680 O  OG  A SER A 321 ? 0.12534 0.06974 0.13438 0.01186  -0.00415 -0.04252 216 SER A OG  
1681 O  OG  B SER A 321 ? 0.13481 0.06339 0.14774 0.00912  -0.00538 -0.04431 216 SER A OG  
1682 N  N   . THR A 322 ? 0.12484 0.05950 0.13392 0.00637  -0.00776 -0.03139 217 THR A N   
1683 C  CA  . THR A 322 ? 0.11408 0.05307 0.12029 0.00304  -0.00845 -0.02805 217 THR A CA  
1684 C  C   . THR A 322 ? 0.11395 0.05703 0.11822 -0.00011 -0.00883 -0.03241 217 THR A C   
1685 O  O   . THR A 322 ? 0.16988 0.10999 0.17474 -0.00077 -0.00868 -0.03769 217 THR A O   
1686 C  CB  . THR A 322 ? 0.13626 0.06916 0.14376 0.00077  -0.00865 -0.02380 217 THR A CB  
1687 O  OG1 . THR A 322 ? 0.19358 0.11961 0.20396 -0.00119 -0.00854 -0.02712 217 THR A OG1 
1688 C  CG2 . THR A 322 ? 0.16574 0.09401 0.17358 0.00357  -0.00886 -0.01881 217 THR A CG2 
1689 N  N   . ARG A 323 ? 0.10749 0.05708 0.10947 -0.00206 -0.00959 -0.03019 218 ARG A N   
1690 C  CA  . ARG A 323 ? 0.12375 0.07681 0.12453 -0.00547 -0.01094 -0.03319 218 ARG A CA  
1691 C  C   . ARG A 323 ? 0.10137 0.06000 0.10204 -0.00727 -0.01189 -0.02916 218 ARG A C   
1692 O  O   . ARG A 323 ? 0.09609 0.05633 0.09645 -0.00584 -0.01114 -0.02482 218 ARG A O   
1693 C  CB  . ARG A 323 ? 0.26785 0.22487 0.26448 -0.00502 -0.01104 -0.03820 218 ARG A CB  
1694 C  CG  . ARG A 323 ? 0.16319 0.12722 0.15609 -0.00348 -0.01062 -0.03638 218 ARG A CG  
1695 C  CD  . ARG A 323 ? 0.12109 0.08900 0.10846 -0.00401 -0.01041 -0.04143 218 ARG A CD  
1696 N  NE  . ARG A 323 ? 0.13709 0.10051 0.12525 -0.00214 -0.00829 -0.04666 218 ARG A NE  
1697 C  CZ  . ARG A 323 ? 0.13897 0.10418 0.12254 -0.00225 -0.00698 -0.05214 218 ARG A CZ  
1698 N  NH1 . ARG A 323 ? 0.16887 0.14004 0.14567 -0.00443 -0.00793 -0.05270 218 ARG A NH1 
1699 N  NH2 . ARG A 323 ? 0.16140 0.12195 0.14706 -0.00014 -0.00460 -0.05717 218 ARG A NH2 
1700 N  N   A SER A 324 ? 0.11670 0.07808 0.11817 -0.01046 -0.01373 -0.03091 219 SER A N   
1701 N  N   B SER A 324 ? 0.11722 0.07868 0.11864 -0.01045 -0.01375 -0.03093 219 SER A N   
1702 N  N   C SER A 324 ? 0.11757 0.07912 0.11897 -0.01044 -0.01375 -0.03086 219 SER A N   
1703 C  CA  A SER A 324 ? 0.11021 0.07718 0.11328 -0.01209 -0.01489 -0.02766 219 SER A CA  
1704 C  CA  B SER A 324 ? 0.11093 0.07792 0.11402 -0.01214 -0.01493 -0.02773 219 SER A CA  
1705 C  CA  C SER A 324 ? 0.11094 0.07789 0.11408 -0.01206 -0.01484 -0.02751 219 SER A CA  
1706 C  C   A SER A 324 ? 0.11680 0.09056 0.11584 -0.01228 -0.01704 -0.02881 219 SER A C   
1707 C  C   B SER A 324 ? 0.11737 0.09117 0.11642 -0.01231 -0.01707 -0.02883 219 SER A C   
1708 C  C   C SER A 324 ? 0.11765 0.09147 0.11708 -0.01247 -0.01714 -0.02869 219 SER A C   
1709 O  O   A SER A 324 ? 0.15943 0.13382 0.15578 -0.01366 -0.01872 -0.03308 219 SER A O   
1710 O  O   B SER A 324 ? 0.15789 0.13239 0.15429 -0.01373 -0.01880 -0.03306 219 SER A O   
1711 O  O   C SER A 324 ? 0.15119 0.12582 0.14862 -0.01422 -0.01909 -0.03280 219 SER A O   
1712 C  CB  A SER A 324 ? 0.13433 0.10006 0.14306 -0.01569 -0.01579 -0.02819 219 SER A CB  
1713 C  CB  B SER A 324 ? 0.13352 0.09932 0.14220 -0.01576 -0.01589 -0.02838 219 SER A CB  
1714 C  CB  C SER A 324 ? 0.13388 0.09928 0.14283 -0.01552 -0.01546 -0.02762 219 SER A CB  
1715 O  OG  A SER A 324 ? 0.15684 0.12842 0.16888 -0.01696 -0.01670 -0.02533 219 SER A OG  
1716 O  OG  B SER A 324 ? 0.10968 0.06866 0.12152 -0.01610 -0.01362 -0.02673 219 SER A OG  
1717 O  OG  C SER A 324 ? 0.13408 0.09958 0.14329 -0.01802 -0.01781 -0.03247 219 SER A OG  
1718 N  N   . ILE A 325 ? 0.10092 0.07922 0.09898 -0.01108 -0.01703 -0.02503 220 ILE A N   
1719 C  CA  . ILE A 325 ? 0.09525 0.07953 0.08950 -0.01138 -0.01924 -0.02483 220 ILE A CA  
1720 C  C   . ILE A 325 ? 0.09304 0.08116 0.09090 -0.01143 -0.02002 -0.02038 220 ILE A C   
1721 O  O   . ILE A 325 ? 0.09525 0.08161 0.09751 -0.01107 -0.01818 -0.01798 220 ILE A O   
1722 C  CB  . ILE A 325 ? 0.12358 0.10903 0.11158 -0.00927 -0.01783 -0.02541 220 ILE A CB  
1723 C  CG1 . ILE A 325 ? 0.15503 0.13934 0.14417 -0.00671 -0.01527 -0.02214 220 ILE A CG1 
1724 C  CG2 . ILE A 325 ? 0.16162 0.14403 0.14647 -0.00908 -0.01679 -0.03071 220 ILE A CG2 
1725 C  CD1 . ILE A 325 ? 0.15621 0.14336 0.14086 -0.00493 -0.01386 -0.02188 220 ILE A CD1 
1726 N  N   . SER A 326 ? 0.09804 0.09119 0.09369 -0.01183 -0.02267 -0.01925 221 SER A N   
1727 C  CA  . SER A 326 ? 0.08641 0.08322 0.08665 -0.01175 -0.02398 -0.01545 221 SER A CA  
1728 C  C   . SER A 326 ? 0.11993 0.11928 0.11579 -0.01023 -0.02432 -0.01253 221 SER A C   
1729 O  O   . SER A 326 ? 0.16403 0.16431 0.15297 -0.01034 -0.02502 -0.01357 221 SER A O   
1730 C  CB  . SER A 326 ? 0.10694 0.10763 0.11129 -0.01403 -0.02813 -0.01616 221 SER A CB  
1731 O  OG  . SER A 326 ? 0.11369 0.11229 0.12292 -0.01612 -0.02798 -0.01900 221 SER A OG  
1732 N  N   . GLY A 327 ? 0.09151 0.09165 0.09130 -0.00902 -0.02345 -0.00905 222 GLY A N   
1733 C  CA  . GLY A 327 ? 0.08659 0.08869 0.08362 -0.00794 -0.02417 -0.00590 222 GLY A CA  
1734 C  C   . GLY A 327 ? 0.07934 0.08032 0.08076 -0.00642 -0.02189 -0.00321 222 GLY A C   
1735 O  O   . GLY A 327 ? 0.09681 0.09525 0.10123 -0.00611 -0.01917 -0.00388 222 GLY A O   
1736 N  N   . THR A 328 ? 0.08018 0.08249 0.08112 -0.00559 -0.02285 -0.00008 223 THR A N   
1737 C  CA  . THR A 328 ? 0.08198 0.08224 0.08558 -0.00422 -0.02016 0.00162  223 THR A CA  
1738 C  C   . THR A 328 ? 0.07685 0.07437 0.07573 -0.00380 -0.01723 0.00061  223 THR A C   
1739 O  O   . THR A 328 ? 0.08757 0.08283 0.08800 -0.00307 -0.01490 0.00100  223 THR A O   
1740 C  CB  . THR A 328 ? 0.06440 0.06554 0.06927 -0.00339 -0.02166 0.00513  223 THR A CB  
1741 O  OG1 . THR A 328 ? 0.10406 0.10587 0.10195 -0.00399 -0.02296 0.00647  223 THR A OG1 
1742 C  CG2 . THR A 328 ? 0.08755 0.09159 0.09926 -0.00317 -0.02487 0.00657  223 THR A CG2 
1743 N  N   . SER A 329 ? 0.07682 0.07470 0.07027 -0.00425 -0.01733 -0.00104 224 SER A N   
1744 C  CA  . SER A 329 ? 0.06574 0.06173 0.05653 -0.00357 -0.01487 -0.00235 224 SER A CA  
1745 C  C   . SER A 329 ? 0.07940 0.07228 0.07263 -0.00320 -0.01334 -0.00376 224 SER A C   
1746 O  O   . SER A 329 ? 0.07630 0.06719 0.06850 -0.00233 -0.01171 -0.00381 224 SER A O   
1747 C  CB  . SER A 329 ? 0.12983 0.12700 0.11598 -0.00392 -0.01489 -0.00470 224 SER A CB  
1748 O  OG  . SER A 329 ? 0.17527 0.17509 0.15741 -0.00453 -0.01542 -0.00322 224 SER A OG  
1749 N  N   . MET A 330 ? 0.07818 0.07067 0.07462 -0.00405 -0.01402 -0.00468 225 MET A N   
1750 C  CA  . MET A 330 ? 0.06333 0.05228 0.06145 -0.00417 -0.01231 -0.00566 225 MET A CA  
1751 C  C   . MET A 330 ? 0.06148 0.04945 0.06288 -0.00415 -0.01059 -0.00387 225 MET A C   
1752 O  O   . MET A 330 ? 0.08363 0.06820 0.08442 -0.00412 -0.00852 -0.00367 225 MET A O   
1753 C  CB  . MET A 330 ? 0.08999 0.07860 0.09079 -0.00572 -0.01332 -0.00769 225 MET A CB  
1754 C  CG  . MET A 330 ? 0.11948 0.10746 0.11740 -0.00618 -0.01448 -0.01081 225 MET A CG  
1755 S  SD  . MET A 330 ? 0.10892 0.10070 0.10092 -0.00577 -0.01600 -0.01156 225 MET A SD  
1756 C  CE  . MET A 330 ? 0.15335 0.14360 0.14237 -0.00364 -0.01341 -0.01161 225 MET A CE  
1757 N  N   . ALA A 331 ? 0.06368 0.05441 0.06846 -0.00413 -0.01133 -0.00253 226 ALA A N   
1758 C  CA  . ALA A 331 ? 0.07823 0.06817 0.08649 -0.00389 -0.00911 -0.00151 226 ALA A CA  
1759 C  C   . ALA A 331 ? 0.06367 0.05125 0.06793 -0.00296 -0.00755 -0.00074 226 ALA A C   
1760 O  O   . ALA A 331 ? 0.08615 0.07111 0.08980 -0.00307 -0.00499 -0.00080 226 ALA A O   
1761 C  CB  . ALA A 331 ? 0.08585 0.07943 0.10021 -0.00363 -0.01064 -0.00044 226 ALA A CB  
1762 N  N   . THR A 332 ? 0.05899 0.04758 0.06020 -0.00239 -0.00902 -0.00009 227 THR A N   
1763 C  CA  . THR A 332 ? 0.05785 0.04479 0.05623 -0.00190 -0.00804 0.00051  227 THR A CA  
1764 C  C   . THR A 332 ? 0.07348 0.05742 0.06825 -0.00188 -0.00670 -0.00022 227 THR A C   
1765 O  O   . THR A 332 ? 0.07260 0.05432 0.06604 -0.00197 -0.00523 -0.00013 227 THR A O   
1766 C  CB  . THR A 332 ? 0.07457 0.06363 0.07080 -0.00182 -0.00968 0.00134  227 THR A CB  
1767 O  OG1 . THR A 332 ? 0.07854 0.06968 0.07734 -0.00191 -0.01131 0.00283  227 THR A OG1 
1768 C  CG2 . THR A 332 ? 0.10752 0.09532 0.10188 -0.00179 -0.00891 0.00185  227 THR A CG2 
1769 N  N   . PRO A 333 ? 0.06698 0.05034 0.05995 -0.00171 -0.00727 -0.00097 228 PRO A N   
1770 C  CA  . PRO A 333 ? 0.06469 0.04482 0.05449 -0.00142 -0.00664 -0.00091 228 PRO A CA  
1771 C  C   . PRO A 333 ? 0.07418 0.05098 0.06344 -0.00227 -0.00462 -0.00053 228 PRO A C   
1772 O  O   . PRO A 333 ? 0.09334 0.06716 0.07857 -0.00229 -0.00412 0.00013  228 PRO A O   
1773 C  CB  . PRO A 333 ? 0.08054 0.06057 0.07001 -0.00069 -0.00776 -0.00183 228 PRO A CB  
1774 C  CG  . PRO A 333 ? 0.08450 0.06704 0.07639 -0.00123 -0.00843 -0.00291 228 PRO A CG  
1775 C  CD  . PRO A 333 ? 0.05970 0.04515 0.05281 -0.00160 -0.00876 -0.00193 228 PRO A CD  
1776 N  N   . HIS A 334 ? 0.06477 0.04227 0.05791 -0.00315 -0.00346 -0.00083 229 HIS A N   
1777 C  CA  . HIS A 334 ? 0.07272 0.04762 0.06568 -0.00428 -0.00056 -0.00050 229 HIS A CA  
1778 C  C   . HIS A 334 ? 0.09003 0.06428 0.08097 -0.00422 0.00116  -0.00052 229 HIS A C   
1779 O  O   . HIS A 334 ? 0.09699 0.06790 0.08332 -0.00498 0.00322  -0.00024 229 HIS A O   
1780 C  CB  . HIS A 334 ? 0.08091 0.05802 0.08046 -0.00535 0.00054  -0.00106 229 HIS A CB  
1781 C  CG  . HIS A 334 ? 0.07205 0.04836 0.07327 -0.00632 -0.00028 -0.00146 229 HIS A CG  
1782 N  ND1 . HIS A 334 ? 0.08342 0.06224 0.08679 -0.00607 -0.00317 -0.00254 229 HIS A ND1 
1783 C  CD2 . HIS A 334 ? 0.08978 0.06291 0.09121 -0.00794 0.00165  -0.00111 229 HIS A CD2 
1784 C  CE1 . HIS A 334 ? 0.09856 0.07550 0.10340 -0.00736 -0.00320 -0.00330 229 HIS A CE1 
1785 N  NE2 . HIS A 334 ? 0.10225 0.07557 0.10633 -0.00853 -0.00033 -0.00221 229 HIS A NE2 
1786 N  N   . VAL A 335 ? 0.07519 0.05211 0.06915 -0.00346 0.00035  -0.00087 230 VAL A N   
1787 C  CA  . VAL A 335 ? 0.07397 0.04964 0.06676 -0.00341 0.00202  -0.00146 230 VAL A CA  
1788 C  C   . VAL A 335 ? 0.10918 0.08280 0.09550 -0.00344 0.00071  -0.00139 230 VAL A C   
1789 O  O   . VAL A 335 ? 0.10190 0.07272 0.08385 -0.00413 0.00235  -0.00214 230 VAL A O   
1790 C  CB  . VAL A 335 ? 0.06645 0.04481 0.06531 -0.00254 0.00129  -0.00144 230 VAL A CB  
1791 C  CG1 . VAL A 335 ? 0.10728 0.08355 0.10512 -0.00234 0.00253  -0.00230 230 VAL A CG1 
1792 C  CG2 . VAL A 335 ? 0.09779 0.07853 0.10408 -0.00248 0.00262  -0.00163 230 VAL A CG2 
1793 N  N   . ALA A 336 ? 0.08265 0.05792 0.06828 -0.00283 -0.00222 -0.00073 231 ALA A N   
1794 C  CA  . ALA A 336 ? 0.06863 0.04298 0.04972 -0.00285 -0.00386 -0.00064 231 ALA A CA  
1795 C  C   . ALA A 336 ? 0.09025 0.06120 0.06582 -0.00324 -0.00362 -0.00013 231 ALA A C   
1796 O  O   . ALA A 336 ? 0.09054 0.05944 0.06106 -0.00391 -0.00397 -0.00034 231 ALA A O   
1797 C  CB  . ALA A 336 ? 0.08954 0.06709 0.07239 -0.00200 -0.00635 -0.00019 231 ALA A CB  
1798 N  N   . GLY A 337 ? 0.07463 0.04451 0.05065 -0.00307 -0.00326 0.00068  232 GLY A N   
1799 C  CA  . GLY A 337 ? 0.08256 0.04830 0.05306 -0.00360 -0.00294 0.00196  232 GLY A CA  
1800 C  C   . GLY A 337 ? 0.09194 0.05483 0.05817 -0.00526 0.00041  0.00163  232 GLY A C   
1801 O  O   . GLY A 337 ? 0.12848 0.08801 0.08733 -0.00606 0.00023  0.00250  232 GLY A O   
1802 N  N   . LEU A 338 ? 0.08526 0.04955 0.05612 -0.00580 0.00354  0.00040  233 LEU A N   
1803 C  CA  . LEU A 338 ? 0.09389 0.05602 0.06168 -0.00724 0.00766  -0.00060 233 LEU A CA  
1804 C  C   . LEU A 338 ? 0.10717 0.06804 0.06977 -0.00751 0.00732  -0.00213 233 LEU A C   
1805 O  O   . LEU A 338 ? 0.11530 0.07274 0.07008 -0.00895 0.00926  -0.00256 233 LEU A O   
1806 C  CB  . LEU A 338 ? 0.09087 0.05588 0.06711 -0.00720 0.01068  -0.00191 233 LEU A CB  
1807 C  CG  . LEU A 338 ? 0.12436 0.08797 0.09947 -0.00842 0.01589  -0.00355 233 LEU A CG  
1808 C  CD1 . LEU A 338 ? 0.16419 0.12397 0.13197 -0.01055 0.01884  -0.00222 233 LEU A CD1 
1809 C  CD2 . LEU A 338 ? 0.15194 0.11955 0.13803 -0.00780 0.01822  -0.00476 233 LEU A CD2 
1810 N  N   . ALA A 339 ? 0.10887 0.07218 0.07507 -0.00648 0.00486  -0.00297 234 ALA A N   
1811 C  CA  . ALA A 339 ? 0.09110 0.05298 0.05304 -0.00711 0.00416  -0.00464 234 ALA A CA  
1812 C  C   . ALA A 339 ? 0.10815 0.06786 0.06144 -0.00790 0.00131  -0.00362 234 ALA A C   
1813 O  O   . ALA A 339 ? 0.12343 0.08023 0.06936 -0.00938 0.00195  -0.00505 234 ALA A O   
1814 C  CB  . ALA A 339 ? 0.09413 0.05892 0.06224 -0.00620 0.00193  -0.00509 234 ALA A CB  
1815 N  N   . ALA A 340 ? 0.09410 0.05532 0.04838 -0.00685 -0.00220 -0.00138 235 ALA A N   
1816 C  CA  . ALA A 340 ? 0.09995 0.05944 0.04733 -0.00713 -0.00562 0.00011  235 ALA A CA  
1817 C  C   . ALA A 340 ? 0.12618 0.08086 0.06460 -0.00860 -0.00358 0.00121  235 ALA A C   
1818 O  O   . ALA A 340 ? 0.14790 0.10009 0.07760 -0.00991 -0.00513 0.00121  235 ALA A O   
1819 C  CB  . ALA A 340 ? 0.12600 0.08774 0.07761 -0.00520 -0.00910 0.00227  235 ALA A CB  
1820 N  N   . TYR A 341 ? 0.12478 0.07817 0.06496 -0.00877 -0.00008 0.00219  236 TYR A N   
1821 C  CA  . TYR A 341 ? 0.11871 0.06751 0.05077 -0.01063 0.00295  0.00355  236 TYR A CA  
1822 C  C   . TYR A 341 ? 0.12769 0.07462 0.05309 -0.01262 0.00662  0.00078  236 TYR A C   
1823 O  O   . TYR A 341 ? 0.14755 0.09052 0.06165 -0.01443 0.00680  0.00160  236 TYR A O   
1824 C  CB  . TYR A 341 ? 0.11555 0.06453 0.05375 -0.01071 0.00644  0.00447  236 TYR A CB  
1825 C  CG  . TYR A 341 ? 0.12461 0.06968 0.05677 -0.01315 0.01138  0.00552  236 TYR A CG  
1826 C  CD1 . TYR A 341 ? 0.15884 0.09932 0.08480 -0.01407 0.01059  0.00938  236 TYR A CD1 
1827 C  CD2 . TYR A 341 ? 0.14479 0.09084 0.07858 -0.01446 0.01710  0.00282  236 TYR A CD2 
1828 C  CE1 . TYR A 341 ? 0.16547 0.10236 0.08590 -0.01674 0.01557  0.01070  236 TYR A CE1 
1829 C  CE2 . TYR A 341 ? 0.15149 0.09468 0.08047 -0.01693 0.02244  0.00359  236 TYR A CE2 
1830 C  CZ  . TYR A 341 ? 0.18878 0.12744 0.11093 -0.01830 0.02181  0.00767  236 TYR A CZ  
1831 O  OH  . TYR A 341 ? 0.19463 0.13036 0.11176 -0.02122 0.02762  0.00876  236 TYR A OH  
1832 N  N   . LEU A 342 ? 0.12066 0.07007 0.05260 -0.01229 0.00945  -0.00255 237 LEU A N   
1833 C  CA  . LEU A 342 ? 0.12777 0.07510 0.05456 -0.01389 0.01353  -0.00598 237 LEU A CA  
1834 C  C   . LEU A 342 ? 0.14760 0.09341 0.06696 -0.01474 0.01000  -0.00773 237 LEU A C   
1835 O  O   . LEU A 342 ? 0.16899 0.11127 0.07828 -0.01684 0.01226  -0.00989 237 LEU A O   
1836 C  CB  . LEU A 342 ? 0.12814 0.07826 0.06559 -0.01278 0.01706  -0.00889 237 LEU A CB  
1837 C  CG  . LEU A 342 ? 0.14601 0.09812 0.09106 -0.01244 0.02090  -0.00784 237 LEU A CG  
1838 C  CD1 . LEU A 342 ? 0.16317 0.11900 0.12059 -0.01065 0.02230  -0.00997 237 LEU A CD1 
1839 C  CD2 . LEU A 342 ? 0.16689 0.11614 0.10527 -0.01471 0.02682  -0.00826 237 LEU A CD2 
1840 N  N   . MET A 343 ? 0.13312 0.08165 0.05693 -0.01348 0.00464  -0.00711 238 MET A N   
1841 C  CA  . MET A 343 ? 0.13204 0.07973 0.04973 -0.01466 0.00070  -0.00867 238 MET A CA  
1842 C  C   . MET A 343 ? 0.14998 0.09488 0.05581 -0.01597 -0.00251 -0.00621 238 MET A C   
1843 O  O   . MET A 343 ? 0.17230 0.11451 0.06810 -0.01814 -0.00346 -0.00824 238 MET A O   
1844 C  CB  . MET A 343 ? 0.15683 0.10889 0.08328 -0.01324 -0.00400 -0.00827 238 MET A CB  
1845 C  CG  . MET A 343 ? 0.15124 0.10488 0.08693 -0.01260 -0.00147 -0.01078 238 MET A CG  
1846 S  SD  . MET A 343 ? 0.28538 0.24464 0.23330 -0.01056 -0.00458 -0.00879 238 MET A SD  
1847 C  CE  . MET A 343 ? 0.26452 0.22474 0.20871 -0.01205 -0.00995 -0.00942 238 MET A CE  
1848 N  N   . THR A 344 ? 0.14104 0.08600 0.04729 -0.01478 -0.00436 -0.00184 239 THR A N   
1849 C  CA  . THR A 344 ? 0.15215 0.09365 0.04707 -0.01583 -0.00752 0.00135  239 THR A CA  
1850 C  C   . THR A 344 ? 0.17265 0.10902 0.05495 -0.01869 -0.00263 0.00055  239 THR A C   
1851 O  O   . THR A 344 ? 0.22657 0.15974 0.09606 -0.02064 -0.00519 0.00125  239 THR A O   
1852 C  CB  . THR A 344 ? 0.15911 0.10064 0.05838 -0.01380 -0.00942 0.00607  239 THR A CB  
1853 O  OG1 . THR A 344 ? 0.20242 0.14861 0.11104 -0.01137 -0.01445 0.00653  239 THR A OG1 
1854 C  CG2 . THR A 344 ? 0.19818 0.13466 0.08583 -0.01484 -0.01154 0.01039  239 THR A CG2 
1855 N  N   . LEU A 345 ? 0.18029 0.11610 0.06587 -0.01911 0.00448  -0.00093 240 LEU A N   
1856 C  CA  . LEU A 345 ? 0.17709 0.10879 0.05192 -0.02192 0.01053  -0.00242 240 LEU A CA  
1857 C  C   . LEU A 345 ? 0.20921 0.13993 0.07856 -0.02355 0.01242  -0.00808 240 LEU A C   
1858 O  O   . LEU A 345 ? 0.27004 0.19803 0.13054 -0.02580 0.01702  -0.00979 240 LEU A O   
1859 C  CB  . LEU A 345 ? 0.19985 0.13257 0.08279 -0.02170 0.01770  -0.00276 240 LEU A CB  
1860 C  CG  . LEU A 345 ? 0.25702 0.18866 0.14169 -0.02145 0.01750  0.00253  240 LEU A CG  
1861 C  CD1 . LEU A 345 ? 0.30940 0.24334 0.20458 -0.02135 0.02378  0.00166  240 LEU A CD1 
1862 C  CD2 . LEU A 345 ? 0.30882 0.23472 0.17782 -0.02419 0.01804  0.00590  240 LEU A CD2 
1863 N  N   . GLY A 346 ? 0.17658 0.11014 0.05317 -0.02234 0.00910  -0.01092 241 GLY A N   
1864 C  CA  . GLY A 346 ? 0.18059 0.11248 0.05281 -0.02398 0.01058  -0.01665 241 GLY A CA  
1865 C  C   . GLY A 346 ? 0.18774 0.11962 0.06714 -0.02352 0.01808  -0.02123 241 GLY A C   
1866 O  O   . GLY A 346 ? 0.24143 0.17120 0.11702 -0.02486 0.02066  -0.02622 241 GLY A O   
1867 N  N   . LYS A 347 ? 0.19400 0.12874 0.08497 -0.02146 0.02135  -0.01954 242 LYS A N   
1868 C  CA  . LYS A 347 ? 0.16592 0.10129 0.06513 -0.02065 0.02829  -0.02335 242 LYS A CA  
1869 C  C   . LYS A 347 ? 0.18195 0.11895 0.09211 -0.01880 0.02666  -0.02619 242 LYS A C   
1870 O  O   . LYS A 347 ? 0.21127 0.14737 0.12642 -0.01827 0.03180  -0.03045 242 LYS A O   
1871 C  CB  . LYS A 347 ? 0.20579 0.14421 0.11418 -0.01933 0.03171  -0.02031 242 LYS A CB  
1872 C  CG  . LYS A 347 ? 0.31877 0.25482 0.21671 -0.02154 0.03396  -0.01711 242 LYS A CG  
1873 C  CD  . LYS A 347 ? 0.51695 0.45443 0.42089 -0.02187 0.04190  -0.01787 242 LYS A CD  
1874 C  CE  . LYS A 347 ? 0.57719 0.51204 0.47135 -0.02457 0.04495  -0.01431 242 LYS A CE  
1875 N  NZ  . LYS A 347 ? 0.57677 0.50698 0.45415 -0.02749 0.04675  -0.01569 242 LYS A NZ  
1876 N  N   . THR A 348 ? 0.18105 0.12030 0.09538 -0.01782 0.01997  -0.02384 243 THR A N   
1877 C  CA  . THR A 348 ? 0.16896 0.10965 0.09394 -0.01631 0.01845  -0.02556 243 THR A CA  
1878 C  C   . THR A 348 ? 0.20481 0.14697 0.12895 -0.01674 0.01125  -0.02381 243 THR A C   
1879 O  O   . THR A 348 ? 0.19796 0.14044 0.11456 -0.01770 0.00736  -0.02135 243 THR A O   
1880 C  CB  . THR A 348 ? 0.20723 0.15174 0.14590 -0.01359 0.02013  -0.02345 243 THR A CB  
1881 O  OG1 . THR A 348 ? 0.18681 0.13163 0.13484 -0.01226 0.01937  -0.02504 243 THR A OG1 
1882 C  CG2 . THR A 348 ? 0.16460 0.11295 0.10624 -0.01254 0.01589  -0.01829 243 THR A CG2 
1883 N  N   . THR A 349 ? 0.17247 0.11538 0.10462 -0.01614 0.00960  -0.02510 244 THR A N   
1884 C  CA  . THR A 349 ? 0.19000 0.13497 0.12356 -0.01681 0.00353  -0.02393 244 THR A CA  
1885 C  C   . THR A 349 ? 0.16964 0.11870 0.11520 -0.01466 0.00223  -0.02089 244 THR A C   
1886 O  O   . THR A 349 ? 0.16186 0.11156 0.11418 -0.01280 0.00549  -0.02021 244 THR A O   
1887 C  CB  . THR A 349 ? 0.22799 0.16950 0.15953 -0.01899 0.00284  -0.02849 244 THR A CB  
1888 O  OG1 . THR A 349 ? 0.25535 0.19517 0.19618 -0.01770 0.00638  -0.03034 244 THR A OG1 
1889 C  CG2 . THR A 349 ? 0.24993 0.18677 0.16882 -0.02129 0.00502  -0.03248 244 THR A CG2 
1890 N  N   . ALA A 350 ? 0.16834 0.12055 0.11665 -0.01505 -0.00261 -0.01912 245 ALA A N   
1891 C  CA  . ALA A 350 ? 0.13724 0.09333 0.09548 -0.01339 -0.00357 -0.01624 245 ALA A CA  
1892 C  C   . ALA A 350 ? 0.16388 0.11777 0.12905 -0.01294 -0.00097 -0.01759 245 ALA A C   
1893 O  O   . ALA A 350 ? 0.17910 0.13508 0.15137 -0.01109 -0.00017 -0.01516 245 ALA A O   
1894 C  CB  . ALA A 350 ? 0.14468 0.10468 0.10495 -0.01428 -0.00836 -0.01472 245 ALA A CB  
1895 N  N   . ALA A 351 ? 0.14207 0.09147 0.10538 -0.01465 -0.00002 -0.02140 246 ALA A N   
1896 C  CA  . ALA A 351 ? 0.16725 0.11363 0.13787 -0.01409 0.00207  -0.02251 246 ALA A CA  
1897 C  C   . ALA A 351 ? 0.17774 0.12272 0.15202 -0.01165 0.00661  -0.02302 246 ALA A C   
1898 O  O   . ALA A 351 ? 0.21343 0.15801 0.19627 -0.00994 0.00750  -0.02169 246 ALA A O   
1899 C  CB  . ALA A 351 ? 0.19696 0.13797 0.16485 -0.01661 0.00219  -0.02713 246 ALA A CB  
1900 N  N   A SER A 352 ? 0.11784 0.06221 0.08615 -0.01154 0.00949  -0.02473 247 SER A N   
1901 N  N   B SER A 352 ? 0.11872 0.06322 0.08699 -0.01154 0.00940  -0.02462 247 SER A N   
1902 C  CA  A SER A 352 ? 0.15348 0.09683 0.12600 -0.00959 0.01453  -0.02608 247 SER A CA  
1903 C  CA  B SER A 352 ? 0.15469 0.09799 0.12658 -0.00971 0.01454  -0.02618 247 SER A CA  
1904 C  C   A SER A 352 ? 0.17846 0.12615 0.15185 -0.00827 0.01546  -0.02301 247 SER A C   
1905 C  C   B SER A 352 ? 0.17843 0.12621 0.15222 -0.00820 0.01538  -0.02290 247 SER A C   
1906 O  O   A SER A 352 ? 0.14911 0.09699 0.12648 -0.00694 0.01978  -0.02408 247 SER A O   
1907 O  O   B SER A 352 ? 0.14658 0.09472 0.12537 -0.00668 0.01946  -0.02375 247 SER A O   
1908 C  CB  A SER A 352 ? 0.16864 0.10697 0.13429 -0.01094 0.01891  -0.03167 247 SER A CB  
1909 C  CB  B SER A 352 ? 0.15891 0.09761 0.12238 -0.01130 0.01857  -0.03143 247 SER A CB  
1910 O  OG  A SER A 352 ? 0.22163 0.15987 0.17509 -0.01312 0.01826  -0.03213 247 SER A OG  
1911 O  OG  B SER A 352 ? 0.26299 0.19684 0.22539 -0.01278 0.01820  -0.03535 247 SER A OG  
1912 N  N   . ALA A 353 ? 0.12935 0.08062 0.10028 -0.00857 0.01168  -0.01942 248 ALA A N   
1913 C  CA  . ALA A 353 ? 0.10202 0.05626 0.07291 -0.00777 0.01267  -0.01704 248 ALA A CA  
1914 C  C   . ALA A 353 ? 0.13151 0.08883 0.11312 -0.00555 0.01379  -0.01532 248 ALA A C   
1915 O  O   . ALA A 353 ? 0.12386 0.08258 0.10749 -0.00506 0.01676  -0.01519 248 ALA A O   
1916 C  CB  . ALA A 353 ? 0.13883 0.09554 0.10543 -0.00831 0.00826  -0.01397 248 ALA A CB  
1917 N  N   . CYS A 354 ? 0.09084 0.04945 0.07938 -0.00444 0.01122  -0.01370 249 CYS A N   
1918 C  CA  . CYS A 354 ? 0.09352 0.05528 0.09159 -0.00239 0.01136  -0.01169 249 CYS A CA  
1919 C  C   . CYS A 354 ? 0.14434 0.10479 0.14828 -0.00114 0.01596  -0.01431 249 CYS A C   
1920 O  O   . CYS A 354 ? 0.12356 0.08723 0.13326 -0.00008 0.01773  -0.01371 249 CYS A O   
1921 C  CB  . CYS A 354 ? 0.09281 0.05534 0.09561 -0.00172 0.00773  -0.00916 249 CYS A CB  
1922 S  SG  . CYS A 354 ? 0.11250 0.07955 0.12510 0.00050  0.00601  -0.00570 249 CYS A SG  
1923 N  N   A ARG A 355 ? 0.10552 0.06140 0.10879 -0.00131 0.01810  -0.01759 250 ARG A N   
1924 N  N   B ARG A 355 ? 0.10484 0.06072 0.10828 -0.00127 0.01803  -0.01755 250 ARG A N   
1925 C  CA  A ARG A 355 ? 0.10787 0.06211 0.11697 0.00009  0.02320  -0.02096 250 ARG A CA  
1926 C  CA  B ARG A 355 ? 0.10815 0.06231 0.11714 0.00006  0.02321  -0.02101 250 ARG A CA  
1927 C  C   A ARG A 355 ? 0.12353 0.07854 0.12777 -0.00101 0.02803  -0.02318 250 ARG A C   
1928 C  C   B ARG A 355 ? 0.12352 0.07862 0.12777 -0.00101 0.02793  -0.02308 250 ARG A C   
1929 O  O   A ARG A 355 ? 0.14398 0.10133 0.15586 0.00036  0.03197  -0.02417 250 ARG A O   
1930 O  O   B ARG A 355 ? 0.14364 0.10133 0.15567 0.00036  0.03165  -0.02383 250 ARG A O   
1931 C  CB  A ARG A 355 ? 0.17845 0.12664 0.18646 -0.00022 0.02444  -0.02463 250 ARG A CB  
1932 C  CB  B ARG A 355 ? 0.17812 0.12613 0.18556 -0.00035 0.02455  -0.02482 250 ARG A CB  
1933 C  CG  A ARG A 355 ? 0.25457 0.20049 0.26980 0.00168  0.02995  -0.02869 250 ARG A CG  
1934 C  CG  B ARG A 355 ? 0.24445 0.18994 0.25648 0.00097  0.03078  -0.02959 250 ARG A CG  
1935 C  CD  A ARG A 355 ? 0.31014 0.25902 0.34007 0.00513  0.02897  -0.02596 250 ARG A CD  
1936 C  CD  B ARG A 355 ? 0.23474 0.17315 0.24208 -0.00020 0.03281  -0.03474 250 ARG A CD  
1937 N  NE  A ARG A 355 ? 0.33712 0.29119 0.37367 0.00649  0.03233  -0.02605 250 ARG A NE  
1938 N  NE  B ARG A 355 ? 0.41223 0.34727 0.42367 0.00012  0.02882  -0.03341 250 ARG A NE  
1939 C  CZ  A ARG A 355 ? 0.20079 0.15961 0.24941 0.00905  0.03050  -0.02296 250 ARG A CZ  
1940 C  CZ  B ARG A 355 ? 0.41382 0.34560 0.43586 0.00260  0.02983  -0.03424 250 ARG A CZ  
1941 N  NH1 A ARG A 355 ? 0.39471 0.35357 0.44869 0.01053  0.02514  -0.01896 250 ARG A NH1 
1942 N  NH1 B ARG A 355 ? 0.46399 0.39748 0.49559 0.00560  0.03373  -0.03549 250 ARG A NH1 
1943 N  NH2 A ARG A 355 ? 0.37555 0.33930 0.43108 0.00992  0.03409  -0.02381 250 ARG A NH2 
1944 N  NH2 B ARG A 355 ? 0.50858 0.43591 0.53226 0.00202  0.02655  -0.03326 250 ARG A NH2 
1945 N  N   . TYR A 356 ? 0.13010 0.08337 0.12199 -0.00357 0.02773  -0.02367 251 TYR A N   
1946 C  CA  . TYR A 356 ? 0.14676 0.10022 0.13244 -0.00506 0.03210  -0.02481 251 TYR A CA  
1947 C  C   . TYR A 356 ? 0.13187 0.09042 0.12327 -0.00451 0.03198  -0.02140 251 TYR A C   
1948 O  O   . TYR A 356 ? 0.13241 0.09256 0.12701 -0.00468 0.03704  -0.02255 251 TYR A O   
1949 C  CB  . TYR A 356 ? 0.13526 0.08565 0.10616 -0.00781 0.03030  -0.02487 251 TYR A CB  
1950 C  CG  . TYR A 356 ? 0.12557 0.07509 0.08800 -0.00976 0.03459  -0.02533 251 TYR A CG  
1951 C  CD1 . TYR A 356 ? 0.16017 0.10613 0.11615 -0.01115 0.04025  -0.02979 251 TYR A CD1 
1952 C  CD2 . TYR A 356 ? 0.13758 0.08946 0.09840 -0.01036 0.03328  -0.02133 251 TYR A CD2 
1953 C  CE1 . TYR A 356 ? 0.21831 0.16335 0.16580 -0.01329 0.04475  -0.02987 251 TYR A CE1 
1954 C  CE2 . TYR A 356 ? 0.14332 0.09386 0.09659 -0.01241 0.03738  -0.02110 251 TYR A CE2 
1955 C  CZ  . TYR A 356 ? 0.18818 0.13538 0.13426 -0.01400 0.04319  -0.02517 251 TYR A CZ  
1956 O  OH  . TYR A 356 ? 0.22328 0.16883 0.16044 -0.01651 0.04794  -0.02475 251 TYR A OH  
1957 N  N   . ILE A 357 ? 0.10269 0.06388 0.09562 -0.00410 0.02649  -0.01751 252 ILE A N   
1958 C  CA  . ILE A 357 ? 0.09295 0.05861 0.09153 -0.00376 0.02574  -0.01471 252 ILE A CA  
1959 C  C   . ILE A 357 ? 0.10878 0.07818 0.12096 -0.00176 0.02776  -0.01525 252 ILE A C   
1960 O  O   . ILE A 357 ? 0.11611 0.08862 0.13326 -0.00214 0.03076  -0.01520 252 ILE A O   
1961 C  CB  . ILE A 357 ? 0.10556 0.07287 0.10284 -0.00358 0.01960  -0.01132 252 ILE A CB  
1962 C  CG1 . ILE A 357 ? 0.12225 0.08676 0.10776 -0.00538 0.01818  -0.01065 252 ILE A CG1 
1963 C  CG2 . ILE A 357 ? 0.11402 0.08585 0.11854 -0.00306 0.01825  -0.00907 252 ILE A CG2 
1964 C  CD1 . ILE A 357 ? 0.14326 0.10911 0.12720 -0.00505 0.01263  -0.00813 252 ILE A CD1 
1965 N  N   . ALA A 358 ? 0.09359 0.06263 0.11255 0.00033  0.02629  -0.01574 253 ALA A N   
1966 C  CA  . ALA A 358 ? 0.10440 0.07691 0.13725 0.00274  0.02762  -0.01601 253 ALA A CA  
1967 C  C   . ALA A 358 ? 0.14364 0.11588 0.18003 0.00286  0.03495  -0.02004 253 ALA A C   
1968 O  O   . ALA A 358 ? 0.14536 0.12250 0.19239 0.00376  0.03732  -0.02012 253 ALA A O   
1969 C  CB  . ALA A 358 ? 0.13293 0.10380 0.17138 0.00497  0.02422  -0.01513 253 ALA A CB  
1970 N  N   . ASP A 359 ? 0.10133 0.06827 0.12904 0.00175  0.03877  -0.02367 254 ASP A N   
1971 C  CA  . ASP A 359 ? 0.12411 0.09032 0.15399 0.00175  0.04656  -0.02824 254 ASP A CA  
1972 C  C   . ASP A 359 ? 0.12922 0.09854 0.15674 -0.00050 0.05078  -0.02790 254 ASP A C   
1973 O  O   . ASP A 359 ? 0.17383 0.14550 0.20823 -0.00021 0.05745  -0.03076 254 ASP A O   
1974 C  CB  . ASP A 359 ? 0.16660 0.12603 0.18453 0.00025  0.04924  -0.03233 254 ASP A CB  
1975 C  CG  . ASP A 359 ? 0.27695 0.23235 0.29968 0.00240  0.04793  -0.03457 254 ASP A CG  
1976 O  OD1 . ASP A 359 ? 0.31066 0.26831 0.34687 0.00546  0.04594  -0.03305 254 ASP A OD1 
1977 O  OD2 . ASP A 359 ? 0.32925 0.27895 0.34166 0.00075  0.04858  -0.03766 254 ASP A OD2 
1978 N  N   . THR A 360 ? 0.12629 0.09509 0.14381 -0.00289 0.04760  -0.02472 255 THR A N   
1979 C  CA  . THR A 360 ? 0.13315 0.10309 0.14594 -0.00563 0.05144  -0.02390 255 THR A CA  
1980 C  C   . THR A 360 ? 0.11872 0.09402 0.13993 -0.00568 0.04829  -0.02016 255 THR A C   
1981 O  O   . THR A 360 ? 0.13856 0.11435 0.15618 -0.00823 0.05045  -0.01869 255 THR A O   
1982 C  CB  . THR A 360 ? 0.15751 0.12196 0.15232 -0.00848 0.05045  -0.02301 255 THR A CB  
1983 O  OG1 . THR A 360 ? 0.13269 0.09640 0.12384 -0.00804 0.04271  -0.01968 255 THR A OG1 
1984 C  CG2 . THR A 360 ? 0.18579 0.14499 0.17107 -0.00913 0.05364  -0.02723 255 THR A CG2 
1985 N  N   . ALA A 361 ? 0.10501 0.08387 0.13668 -0.00320 0.04313  -0.01856 256 ALA A N   
1986 C  CA  . ALA A 361 ? 0.08892 0.07292 0.12845 -0.00329 0.03935  -0.01553 256 ALA A CA  
1987 C  C   . ALA A 361 ? 0.12383 0.11343 0.17544 -0.00381 0.04417  -0.01656 256 ALA A C   
1988 O  O   . ALA A 361 ? 0.14173 0.13253 0.19957 -0.00293 0.05003  -0.01967 256 ALA A O   
1989 C  CB  . ALA A 361 ? 0.10641 0.09267 0.15338 -0.00053 0.03300  -0.01386 256 ALA A CB  
1990 N  N   . ASN A 362 ? 0.08532 0.07884 0.14174 -0.00513 0.04142  -0.01421 257 ASN A N   
1991 C  CA  . ASN A 362 ? 0.09175 0.09230 0.16329 -0.00538 0.04413  -0.01487 257 ASN A CA  
1992 C  C   . ASN A 362 ? 0.10891 0.11437 0.19434 -0.00172 0.04016  -0.01486 257 ASN A C   
1993 O  O   . ASN A 362 ? 0.12322 0.12856 0.20762 -0.00037 0.03295  -0.01254 257 ASN A O   
1994 C  CB  . ASN A 362 ? 0.11653 0.11935 0.18907 -0.00822 0.04172  -0.01259 257 ASN A CB  
1995 C  CG  . ASN A 362 ? 0.15218 0.15111 0.21524 -0.01204 0.04724  -0.01238 257 ASN A CG  
1996 O  OD1 . ASN A 362 ? 0.17551 0.17478 0.23965 -0.01324 0.05485  -0.01436 257 ASN A OD1 
1997 N  ND2 . ASN A 362 ? 0.16554 0.16029 0.21874 -0.01389 0.04364  -0.00992 257 ASN A ND2 
1998 N  N   . LYS A 363 ? 0.09062 0.10022 0.18890 -0.00001 0.04498  -0.01737 258 LYS A N   
1999 C  CA  . LYS A 363 ? 0.10103 0.11399 0.21237 0.00415  0.04162  -0.01735 258 LYS A CA  
2000 C  C   . LYS A 363 ? 0.11108 0.13351 0.24067 0.00465  0.04005  -0.01666 258 LYS A C   
2001 O  O   . LYS A 363 ? 0.15912 0.18602 0.29634 0.00289  0.04611  -0.01857 258 LYS A O   
2002 C  CB  . LYS A 363 ? 0.14511 0.15531 0.25902 0.00655  0.04789  -0.02116 258 LYS A CB  
2003 C  CG  . LYS A 363 ? 0.35523 0.35673 0.45477 0.00702  0.04725  -0.02188 258 LYS A CG  
2004 C  CD  . LYS A 363 ? 0.52266 0.51957 0.61624 0.00650  0.05583  -0.02667 258 LYS A CD  
2005 C  CE  . LYS A 363 ? 0.44179 0.43018 0.51597 0.00467  0.05492  -0.02702 258 LYS A CE  
2006 N  NZ  . LYS A 363 ? 0.34920 0.33542 0.41050 0.00063  0.06007  -0.02794 258 LYS A NZ  
2007 N  N   . GLY A 364 ? 0.09151 0.11722 0.22812 0.00683  0.03191  -0.01386 259 GLY A N   
2008 C  CA  . GLY A 364 ? 0.08483 0.12000 0.24007 0.00789  0.02906  -0.01313 259 GLY A CA  
2009 C  C   . GLY A 364 ? 0.14238 0.18243 0.29928 0.00408  0.02649  -0.01199 259 GLY A C   
2010 O  O   . GLY A 364 ? 0.16809 0.21675 0.34123 0.00428  0.02457  -0.01187 259 GLY A O   
2011 N  N   . ASP A 365 ? 0.10915 0.14395 0.25057 0.00064  0.02600  -0.01122 260 ASP A N   
2012 C  CA  . ASP A 365 ? 0.11668 0.15466 0.25920 -0.00338 0.02463  -0.01071 260 ASP A CA  
2013 C  C   . ASP A 365 ? 0.11581 0.15560 0.25722 -0.00360 0.01494  -0.00832 260 ASP A C   
2014 O  O   . ASP A 365 ? 0.14859 0.19221 0.29421 -0.00670 0.01273  -0.00833 260 ASP A O   
2015 C  CB  . ASP A 365 ? 0.14376 0.17461 0.27092 -0.00694 0.02966  -0.01116 260 ASP A CB  
2016 C  CG  . ASP A 365 ? 0.28694 0.31699 0.41513 -0.00790 0.03977  -0.01360 260 ASP A CG  
2017 O  OD1 . ASP A 365 ? 0.32247 0.35965 0.46642 -0.00749 0.04372  -0.01530 260 ASP A OD1 
2018 O  OD2 . ASP A 365 ? 0.34794 0.37052 0.46131 -0.00897 0.04377  -0.01394 260 ASP A OD2 
2019 N  N   . LEU A 366 ? 0.07766 0.11480 0.21359 -0.00074 0.00927  -0.00642 261 LEU A N   
2020 C  CA  . LEU A 366 ? 0.08172 0.11978 0.21356 -0.00134 0.00067  -0.00430 261 LEU A CA  
2021 C  C   . LEU A 366 ? 0.10734 0.15369 0.25438 0.00057  -0.00553 -0.00292 261 LEU A C   
2022 O  O   . LEU A 366 ? 0.10954 0.15901 0.26822 0.00393  -0.00444 -0.00273 261 LEU A O   
2023 C  CB  . LEU A 366 ? 0.07036 0.10140 0.18755 0.00026  -0.00212 -0.00258 261 LEU A CB  
2024 C  CG  . LEU A 366 ? 0.07798 0.10136 0.17998 -0.00149 0.00215  -0.00351 261 LEU A CG  
2025 C  CD1 . LEU A 366 ? 0.15419 0.17234 0.24552 0.00053  -0.00078 -0.00181 261 LEU A CD1 
2026 C  CD2 . LEU A 366 ? 0.15287 0.17581 0.24948 -0.00508 0.00052  -0.00391 261 LEU A CD2 
2027 N  N   A SER A 367 ? 0.06243 0.11246 0.21002 -0.00157 -0.01213 -0.00217 262 SER A N   
2028 N  N   B SER A 367 ? 0.06339 0.11314 0.21034 -0.00155 -0.01224 -0.00211 262 SER A N   
2029 C  CA  A SER A 367 ? 0.07374 0.13151 0.23372 -0.00000 -0.01967 -0.00037 262 SER A CA  
2030 C  CA  B SER A 367 ? 0.07483 0.13227 0.23346 -0.00029 -0.02008 -0.00035 262 SER A CA  
2031 C  C   A SER A 367 ? 0.06522 0.11999 0.21388 0.00105  -0.02748 0.00262  262 SER A C   
2032 C  C   B SER A 367 ? 0.06800 0.12226 0.21523 0.00092  -0.02767 0.00267  262 SER A C   
2033 O  O   A SER A 367 ? 0.10611 0.15402 0.23846 -0.00023 -0.02708 0.00263  262 SER A O   
2034 O  O   B SER A 367 ? 0.10023 0.14734 0.23125 0.00001  -0.02694 0.00280  262 SER A O   
2035 C  CB  A SER A 367 ? 0.10792 0.17139 0.27443 -0.00346 -0.02171 -0.00185 262 SER A CB  
2036 C  CB  B SER A 367 ? 0.11454 0.17731 0.27868 -0.00410 -0.02222 -0.00193 262 SER A CB  
2037 O  OG  A SER A 367 ? 0.10366 0.16508 0.26038 -0.00717 -0.02514 -0.00256 262 SER A OG  
2038 O  OG  B SER A 367 ? 0.19157 0.25734 0.36610 -0.00501 -0.01532 -0.00409 262 SER A OG  
2039 N  N   A ASN A 368 ? 0.07531 0.13362 0.22942 0.00334  -0.03368 0.00523  263 ASN A N   
2040 N  N   B ASN A 368 ? 0.08229 0.14062 0.23517 0.00283  -0.03425 0.00515  263 ASN A N   
2041 C  CA  A ASN A 368 ? 0.08525 0.14140 0.22910 0.00415  -0.04129 0.00867  263 ASN A CA  
2042 C  CA  B ASN A 368 ? 0.08480 0.14064 0.22786 0.00416  -0.04144 0.00878  263 ASN A CA  
2043 C  C   A ASN A 368 ? 0.08358 0.13331 0.22003 0.00689  -0.04017 0.01101  263 ASN A C   
2044 C  C   B ASN A 368 ? 0.08345 0.13279 0.21919 0.00659  -0.03941 0.01060  263 ASN A C   
2045 O  O   A ASN A 368 ? 0.08717 0.13343 0.21118 0.00641  -0.04440 0.01328  263 ASN A O   
2046 O  O   B ASN A 368 ? 0.06636 0.11054 0.18666 0.00547  -0.04130 0.01175  263 ASN A O   
2047 C  CB  A ASN A 368 ? 0.15547 0.21173 0.28880 0.00014  -0.04561 0.00761  263 ASN A CB  
2048 C  CB  B ASN A 368 ? 0.15298 0.20907 0.28509 0.00054  -0.04689 0.00836  263 ASN A CB  
2049 C  CG  A ASN A 368 ? 0.15499 0.21707 0.29576 -0.00282 -0.04670 0.00507  263 ASN A CG  
2050 C  CG  B ASN A 368 ? 0.13816 0.19387 0.26219 0.00151  -0.05445 0.01202  263 ASN A CG  
2051 O  OD1 A ASN A 368 ? 0.13437 0.20131 0.28759 -0.00155 -0.04621 0.00513  263 ASN A OD1 
2052 O  OD1 B ASN A 368 ? 0.22360 0.28130 0.35405 0.00421  -0.05704 0.01472  263 ASN A OD1 
2053 N  ND2 A ASN A 368 ? 0.12575 0.18704 0.25907 -0.00682 -0.04806 0.00265  263 ASN A ND2 
2054 N  ND2 B ASN A 368 ? 0.21498 0.26800 0.32472 -0.00082 -0.05765 0.01200  263 ASN A ND2 
2055 N  N   . ILE A 369 ? 0.10643 0.15430 0.25005 0.00965  -0.03423 0.01033  264 ILE A N   
2056 C  CA  . ILE A 369 ? 0.07802 0.11836 0.21417 0.01210  -0.03180 0.01185  264 ILE A CA  
2057 C  C   . ILE A 369 ? 0.09994 0.14023 0.24239 0.01559  -0.03571 0.01536  264 ILE A C   
2058 O  O   . ILE A 369 ? 0.12209 0.16554 0.27679 0.01731  -0.03381 0.01435  264 ILE A O   
2059 C  CB  . ILE A 369 ? 0.13446 0.17084 0.27098 0.01239  -0.02221 0.00820  264 ILE A CB  
2060 C  CG1 . ILE A 369 ? 0.16518 0.19959 0.29151 0.00836  -0.01794 0.00514  264 ILE A CG1 
2061 C  CG2 . ILE A 369 ? 0.15906 0.18754 0.28857 0.01472  -0.02008 0.00935  264 ILE A CG2 
2062 C  CD1 . ILE A 369 ? 0.19583 0.22411 0.30455 0.00678  -0.01967 0.00616  264 ILE A CD1 
2063 N  N   . PRO A 370 ? 0.11468 0.15092 0.24745 0.01617  -0.04076 0.01940  265 PRO A N   
2064 C  CA  . PRO A 370 ? 0.08944 0.12437 0.22610 0.01892  -0.04407 0.02295  265 PRO A CA  
2065 C  C   . PRO A 370 ? 0.16028 0.19084 0.30406 0.02204  -0.03838 0.02188  265 PRO A C   
2066 O  O   . PRO A 370 ? 0.12607 0.15213 0.26637 0.02208  -0.03282 0.01961  265 PRO A O   
2067 C  CB  . PRO A 370 ? 0.19587 0.22630 0.31791 0.01798  -0.04908 0.02722  265 PRO A CB  
2068 C  CG  . PRO A 370 ? 0.20561 0.23686 0.31715 0.01458  -0.04962 0.02565  265 PRO A CG  
2069 C  CD  . PRO A 370 ? 0.12045 0.15304 0.23802 0.01410  -0.04334 0.02098  265 PRO A CD  
2070 N  N   . PHE A 371 ? 0.14415 0.17590 0.29783 0.02467  -0.03986 0.02330  266 PHE A N   
2071 C  CA  . PHE A 371 ? 0.13042 0.15742 0.29037 0.02762  -0.03495 0.02220  266 PHE A CA  
2072 C  C   . PHE A 371 ? 0.13367 0.15192 0.28236 0.02774  -0.03418 0.02405  266 PHE A C   
2073 O  O   . PHE A 371 ? 0.19371 0.20948 0.33296 0.02688  -0.03953 0.02846  266 PHE A O   
2074 C  CB  . PHE A 371 ? 0.15047 0.17974 0.32197 0.03053  -0.03812 0.02433  266 PHE A CB  
2075 C  CG  . PHE A 371 ? 0.18918 0.21547 0.37047 0.03343  -0.03192 0.02148  266 PHE A CG  
2076 C  CD1 . PHE A 371 ? 0.31831 0.34907 0.51073 0.03386  -0.02587 0.01661  266 PHE A CD1 
2077 C  CD2 . PHE A 371 ? 0.23006 0.24880 0.40869 0.03541  -0.03196 0.02357  266 PHE A CD2 
2078 C  CE1 . PHE A 371 ? 0.28382 0.31148 0.48380 0.03629  -0.01970 0.01349  266 PHE A CE1 
2079 C  CE2 . PHE A 371 ? 0.16264 0.17794 0.34927 0.03790  -0.02623 0.02048  266 PHE A CE2 
2080 C  CZ  . PHE A 371 ? 0.34081 0.36059 0.53782 0.03840  -0.02007 0.01530  266 PHE A CZ  
2081 N  N   . GLY A 372 ? 0.15235 0.16588 0.30133 0.02841  -0.02713 0.02039  267 GLY A N   
2082 C  CA  . GLY A 372 ? 0.16677 0.17182 0.30577 0.02823  -0.02579 0.02141  267 GLY A CA  
2083 C  C   . GLY A 372 ? 0.12254 0.12543 0.25049 0.02572  -0.02357 0.01984  267 GLY A C   
2084 O  O   . GLY A 372 ? 0.18487 0.18053 0.30472 0.02526  -0.02151 0.01985  267 GLY A O   
2085 N  N   . THR A 373 ? 0.07913 0.08793 0.20672 0.02394  -0.02411 0.01848  268 THR A N   
2086 C  CA  . THR A 373 ? 0.07464 0.08135 0.18927 0.02061  -0.02072 0.01586  268 THR A CA  
2087 C  C   . THR A 373 ? 0.07900 0.08677 0.19725 0.02002  -0.01295 0.01021  268 THR A C   
2088 O  O   . THR A 373 ? 0.10329 0.11691 0.23466 0.02127  -0.01152 0.00858  268 THR A O   
2089 C  CB  . THR A 373 ? 0.10305 0.11448 0.21066 0.01775  -0.02577 0.01752  268 THR A CB  
2090 O  OG1 . THR A 373 ? 0.12869 0.13885 0.23096 0.01792  -0.03248 0.02274  268 THR A OG1 
2091 C  CG2 . THR A 373 ? 0.09587 0.10529 0.19007 0.01416  -0.02209 0.01448  268 THR A CG2 
2092 N  N   . VAL A 374 ? 0.09052 0.09280 0.19736 0.01802  -0.00794 0.00739  269 VAL A N   
2093 C  CA  . VAL A 374 ? 0.09206 0.09463 0.19989 0.01704  -0.00056 0.00244  269 VAL A CA  
2094 C  C   . VAL A 374 ? 0.08810 0.09689 0.19700 0.01462  -0.00045 0.00154  269 VAL A C   
2095 O  O   . VAL A 374 ? 0.12818 0.13890 0.23100 0.01266  -0.00518 0.00362  269 VAL A O   
2096 C  CB  . VAL A 374 ? 0.13492 0.13049 0.22906 0.01508  0.00374  -0.00000 269 VAL A CB  
2097 C  CG1 . VAL A 374 ? 0.18675 0.17591 0.28161 0.01716  0.00466  -0.00018 269 VAL A CG1 
2098 C  CG2 . VAL A 374 ? 0.11796 0.11246 0.19851 0.01219  0.00053  0.00176  269 VAL A CG2 
2099 N  N   . ASN A 375 ? 0.06902 0.08077 0.18590 0.01456  0.00533  -0.00183 270 ASN A N   
2100 C  CA  . ASN A 375 ? 0.06466 0.08143 0.18274 0.01168  0.00678  -0.00306 270 ASN A CA  
2101 C  C   . ASN A 375 ? 0.08317 0.09545 0.19125 0.00925  0.01401  -0.00627 270 ASN A C   
2102 O  O   . ASN A 375 ? 0.09176 0.10536 0.20562 0.00914  0.02062  -0.00927 270 ASN A O   
2103 C  CB  . ASN A 375 ? 0.07151 0.09657 0.20859 0.01319  0.00743  -0.00379 270 ASN A CB  
2104 C  CG  . ASN A 375 ? 0.11104 0.14197 0.25100 0.00991  0.00696  -0.00423 270 ASN A CG  
2105 O  OD1 . ASN A 375 ? 0.10653 0.13454 0.23582 0.00657  0.00993  -0.00541 270 ASN A OD1 
2106 N  ND2 . ASN A 375 ? 0.11886 0.15802 0.27395 0.01077  0.00305  -0.00324 270 ASN A ND2 
2107 N  N   . LEU A 376 ? 0.07390 0.08094 0.16667 0.00729  0.01268  -0.00551 271 LEU A N   
2108 C  CA  . LEU A 376 ? 0.07343 0.07516 0.15435 0.00515  0.01797  -0.00770 271 LEU A CA  
2109 C  C   . LEU A 376 ? 0.10198 0.10248 0.17224 0.00240  0.01525  -0.00628 271 LEU A C   
2110 O  O   . LEU A 376 ? 0.08846 0.08827 0.15396 0.00263  0.00975  -0.00409 271 LEU A O   
2111 C  CB  . LEU A 376 ? 0.07752 0.07277 0.15075 0.00631  0.01891  -0.00849 271 LEU A CB  
2112 C  CG  . LEU A 376 ? 0.09360 0.08817 0.17653 0.00937  0.02152  -0.01026 271 LEU A CG  
2113 C  CD1 . LEU A 376 ? 0.12239 0.10990 0.19684 0.00997  0.02076  -0.01054 271 LEU A CD1 
2114 C  CD2 . LEU A 376 ? 0.13990 0.13511 0.22637 0.00887  0.02946  -0.01423 271 LEU A CD2 
2115 N  N   . LEU A 377 ? 0.06920 0.06909 0.13576 -0.00018 0.01935  -0.00749 272 LEU A N   
2116 C  CA  . LEU A 377 ? 0.06681 0.06502 0.12469 -0.00269 0.01737  -0.00632 272 LEU A CA  
2117 C  C   . LEU A 377 ? 0.08230 0.07427 0.12752 -0.00412 0.02118  -0.00709 272 LEU A C   
2118 O  O   . LEU A 377 ? 0.10514 0.09601 0.15015 -0.00501 0.02710  -0.00880 272 LEU A O   
2119 C  CB  . LEU A 377 ? 0.08117 0.08397 0.14701 -0.00481 0.01821  -0.00646 272 LEU A CB  
2120 C  CG  . LEU A 377 ? 0.10398 0.10461 0.16269 -0.00747 0.01625  -0.00551 272 LEU A CG  
2121 C  CD1 . LEU A 377 ? 0.13135 0.13189 0.18604 -0.00653 0.00941  -0.00418 272 LEU A CD1 
2122 C  CD2 . LEU A 377 ? 0.13078 0.13581 0.19909 -0.01000 0.01778  -0.00602 272 LEU A CD2 
2123 N  N   . ALA A 378 ? 0.07020 0.05842 0.10502 -0.00435 0.01776  -0.00584 273 ALA A N   
2124 C  CA  . ALA A 378 ? 0.10150 0.08408 0.12423 -0.00545 0.01987  -0.00612 273 ALA A CA  
2125 C  C   . ALA A 378 ? 0.10235 0.08334 0.12223 -0.00801 0.02442  -0.00623 273 ALA A C   
2126 O  O   . ALA A 378 ? 0.12012 0.10284 0.14358 -0.00943 0.02376  -0.00525 273 ALA A O   
2127 C  CB  . ALA A 378 ? 0.11330 0.09383 0.12841 -0.00533 0.01489  -0.00447 273 ALA A CB  
2128 N  N   . TYR A 379 ? 0.09508 0.07219 0.10737 -0.00893 0.02885  -0.00734 274 TYR A N   
2129 C  CA  . TYR A 379 ? 0.09394 0.06913 0.10253 -0.01164 0.03418  -0.00723 274 TYR A CA  
2130 C  C   . TYR A 379 ? 0.14608 0.11515 0.14013 -0.01271 0.03567  -0.00720 274 TYR A C   
2131 O  O   . TYR A 379 ? 0.15448 0.12206 0.14500 -0.01160 0.03609  -0.00923 274 TYR A O   
2132 C  CB  . TYR A 379 ? 0.09512 0.07436 0.11383 -0.01183 0.04020  -0.00957 274 TYR A CB  
2133 C  CG  . TYR A 379 ? 0.10306 0.08081 0.11830 -0.01504 0.04714  -0.00969 274 TYR A CG  
2134 C  CD1 . TYR A 379 ? 0.13724 0.11334 0.14961 -0.01775 0.04689  -0.00698 274 TYR A CD1 
2135 C  CD2 . TYR A 379 ? 0.16468 0.14237 0.17955 -0.01549 0.05421  -0.01258 274 TYR A CD2 
2136 C  CE1 . TYR A 379 ? 0.13413 0.10852 0.14309 -0.02109 0.05354  -0.00653 274 TYR A CE1 
2137 C  CE2 . TYR A 379 ? 0.18188 0.15844 0.19306 -0.01874 0.06116  -0.01261 274 TYR A CE2 
2138 C  CZ  . TYR A 379 ? 0.17025 0.14501 0.17797 -0.02165 0.06075  -0.00927 274 TYR A CZ  
2139 O  OH  . TYR A 379 ? 0.19825 0.17130 0.20132 -0.02534 0.06827  -0.00885 274 TYR A OH  
2140 N  N   . ASN A 380 ? 0.11705 0.08223 0.10266 -0.01496 0.03616  -0.00485 275 ASN A N   
2141 C  CA  . ASN A 380 ? 0.11427 0.07371 0.08533 -0.01592 0.03619  -0.00421 275 ASN A CA  
2142 C  C   . ASN A 380 ? 0.17239 0.12934 0.13658 -0.01833 0.04330  -0.00556 275 ASN A C   
2143 O  O   . ASN A 380 ? 0.15787 0.11018 0.10912 -0.01931 0.04328  -0.00544 275 ASN A O   
2144 C  CB  . ASN A 380 ? 0.11678 0.07248 0.08109 -0.01653 0.03174  -0.00041 275 ASN A CB  
2145 C  CG  . ASN A 380 ? 0.15290 0.10618 0.11587 -0.01933 0.03507  0.00210  275 ASN A CG  
2146 O  OD1 . ASN A 380 ? 0.14855 0.10366 0.11605 -0.02119 0.04095  0.00112  275 ASN A OD1 
2147 N  ND2 . ASN A 380 ? 0.17512 0.12407 0.13228 -0.01963 0.03131  0.00550  275 ASN A ND2 
2148 N  N   A ASN A 381 ? 0.17038 0.13062 0.14280 -0.01948 0.04942  -0.00696 276 ASN A N   
2149 N  N   B ASN A 381 ? 0.16931 0.12965 0.14192 -0.01936 0.04936  -0.00710 276 ASN A N   
2150 C  CA  A ASN A 381 ? 0.15955 0.11838 0.12671 -0.02172 0.05749  -0.00909 276 ASN A CA  
2151 C  CA  B ASN A 381 ? 0.15991 0.11856 0.12661 -0.02165 0.05727  -0.00911 276 ASN A CA  
2152 C  C   A ASN A 381 ? 0.17205 0.12474 0.12392 -0.02521 0.05958  -0.00599 276 ASN A C   
2153 C  C   B ASN A 381 ? 0.15210 0.10419 0.10237 -0.02481 0.05824  -0.00594 276 ASN A C   
2154 O  O   A ASN A 381 ? 0.17011 0.11990 0.11184 -0.02728 0.06519  -0.00754 276 ASN A O   
2155 O  O   B ASN A 381 ? 0.16942 0.11762 0.10711 -0.02616 0.06113  -0.00735 276 ASN A O   
2156 C  CB  A ASN A 381 ? 0.19134 0.14937 0.15536 -0.02010 0.05877  -0.01337 276 ASN A CB  
2157 C  CB  B ASN A 381 ? 0.19142 0.14970 0.15612 -0.01998 0.05890  -0.01357 276 ASN A CB  
2158 C  CG  A ASN A 381 ? 0.17442 0.13818 0.15453 -0.01730 0.06000  -0.01659 276 ASN A CG  
2159 C  CG  B ASN A 381 ? 0.23201 0.19128 0.19782 -0.02137 0.06820  -0.01732 276 ASN A CG  
2160 O  OD1 A ASN A 381 ? 0.23945 0.20486 0.22565 -0.01451 0.05425  -0.01656 276 ASN A OD1 
2161 O  OD1 B ASN A 381 ? 0.38092 0.34117 0.34760 -0.02400 0.07381  -0.01628 276 ASN A OD1 
2162 N  ND2 A ASN A 381 ? 0.15315 0.12011 0.14072 -0.01800 0.06749  -0.01912 276 ASN A ND2 
2163 N  ND2 B ASN A 381 ? 0.40978 0.36850 0.37548 -0.01977 0.07025  -0.02192 276 ASN A ND2 
2164 N  N   . TYR A 382 ? 0.19440 0.14471 0.14419 -0.02601 0.05540  -0.00158 277 TYR A N   
2165 C  CA  . TYR A 382 ? 0.19468 0.13822 0.12959 -0.02887 0.05594  0.00232  277 TYR A CA  
2166 C  C   . TYR A 382 ? 0.21818 0.16111 0.15137 -0.03279 0.06479  0.00276  277 TYR A C   
2167 O  O   . TYR A 382 ? 0.29384 0.24113 0.23981 -0.03372 0.06820  0.00246  277 TYR A O   
2168 C  CB  . TYR A 382 ? 0.20048 0.14141 0.13595 -0.02833 0.04943  0.00678  277 TYR A CB  
2169 C  CG  . TYR A 382 ? 0.22022 0.15341 0.14122 -0.03097 0.04922  0.01176  277 TYR A CG  
2170 C  CD1 . TYR A 382 ? 0.33592 0.26451 0.24250 -0.03053 0.04544  0.01308  277 TYR A CD1 
2171 C  CD2 . TYR A 382 ? 0.33641 0.26703 0.25844 -0.03406 0.05274  0.01512  277 TYR A CD2 
2172 C  CE1 . TYR A 382 ? 0.36142 0.28284 0.25450 -0.03274 0.04450  0.01819  277 TYR A CE1 
2173 C  CE2 . TYR A 382 ? 0.30640 0.23010 0.21609 -0.03601 0.05175  0.02000  277 TYR A CE2 
2174 C  CZ  . TYR A 382 ? 0.28370 0.20363 0.18008 -0.03478 0.04693  0.02140  277 TYR A CZ  
2175 O  OH  . TYR A 382 ? 0.40349 0.31848 0.29050 -0.03582 0.04452  0.02615  277 TYR A OH  
2176 N  N   . GLN A 383 ? 0.23624 0.17448 0.15420 -0.03500 0.06787  0.00323  278 GLN A N   
2177 C  CA  . GLN A 383 ? 0.37730 0.31552 0.29306 -0.03785 0.07343  0.00393  278 GLN A CA  
2178 C  C   . GLN A 383 ? 0.31822 0.24965 0.21865 -0.03943 0.06955  0.00909  278 GLN A C   
2179 O  O   . GLN A 383 ? 0.46609 0.39415 0.35410 -0.03874 0.06583  0.00903  278 GLN A O   
2180 C  CB  . GLN A 383 ? 0.57528 0.51611 0.48974 -0.03796 0.07944  -0.00142 278 GLN A CB  
2181 C  CG  . GLN A 383 ? 0.68524 0.63182 0.61286 -0.03515 0.08156  -0.00705 278 GLN A CG  
2182 C  CD  . GLN A 383 ? 0.93062 0.88400 0.87754 -0.03481 0.08459  -0.00762 278 GLN A CD  
2183 O  OE1 . GLN A 383 ? 0.92284 0.87723 0.87342 -0.03724 0.08713  -0.00514 278 GLN A OE1 
2184 N  NE2 . GLN A 383 ? 0.75677 0.71507 0.71664 -0.03181 0.08378  -0.01073 278 GLN A NE2 
2185 N  N   . ALA A 384 ? 0.29504 0.22469 0.19720 -0.04144 0.06992  0.01355  279 ALA A N   
2186 C  CA  . ALA A 384 ? 0.38008 0.30336 0.26909 -0.04281 0.06644  0.01904  279 ALA A CA  
2187 C  C   . ALA A 384 ? 0.47071 0.39281 0.34719 -0.04479 0.07038  0.01809  279 ALA A C   
2188 O  O   . ALA A 384 ? 0.46315 0.38915 0.34327 -0.04604 0.07752  0.01411  279 ALA A O   
2189 C  CB  . ALA A 384 ? 0.47883 0.40056 0.37381 -0.04474 0.06697  0.02358  279 ALA A CB  
2190 O  OXT . ALA A 384 ? 0.54347 0.46097 0.40622 -0.04504 0.06635  0.02100  279 ALA A OXT 
2191 N  N   . NO3 B .   ? 0.38894 0.43673 0.38119 0.00206  0.03402  -0.03856 301 NO3 A N   
2192 O  O1  . NO3 B .   ? 0.25424 0.29893 0.25221 0.00366  0.02889  -0.03527 301 NO3 A O1  
2193 O  O2  . NO3 B .   ? 0.32528 0.36912 0.30613 0.00031  0.03366  -0.04007 301 NO3 A O2  
2194 O  O3  . NO3 B .   ? 0.43807 0.49317 0.43614 0.00207  0.03947  -0.04045 301 NO3 A O3  
2195 CA CA  . CA  C .   ? 0.11383 0.07634 0.14290 0.00329  -0.00228 0.00416  302 CA  A CA  
2196 O  O   . HOH D .   ? 0.32132 0.33528 0.41462 -0.01509 0.04393  -0.01128 401 HOH A O   
2197 O  O   . HOH D .   ? 0.36912 0.34315 0.34095 -0.03585 -0.00286 0.05912  402 HOH A O   
2198 O  O   . HOH D .   ? 0.32864 0.33022 0.38460 -0.02821 -0.02361 -0.02049 403 HOH A O   
2199 O  O   . HOH D .   ? 0.32661 0.34093 0.34933 -0.03945 0.00560  0.01961  404 HOH A O   
2200 O  O   . HOH D .   ? 0.34041 0.27710 0.36596 -0.01130 -0.00698 0.01525  405 HOH A O   
2201 O  O   . HOH D .   ? 0.34098 0.30144 0.35447 -0.03288 0.04230  0.00676  406 HOH A O   
2202 O  O   . HOH D .   ? 0.11736 0.11592 0.10586 -0.00061 -0.00844 -0.00256 407 HOH A O   
2203 O  O   . HOH D .   ? 0.46154 0.41001 0.47159 -0.01421 -0.01640 0.04625  408 HOH A O   
2204 O  O   . HOH D .   ? 0.34683 0.32739 0.33429 -0.01717 -0.02382 -0.03971 409 HOH A O   
2205 O  O   . HOH D .   ? 0.39730 0.31541 0.34574 0.00467  -0.02220 0.03031  410 HOH A O   
2206 O  O   . HOH D .   ? 0.30613 0.30862 0.28822 -0.00687 -0.02152 -0.00417 411 HOH A O   
2207 O  O   . HOH D .   ? 0.31627 0.37417 0.37932 -0.00993 -0.03126 -0.00583 412 HOH A O   
2208 O  O   . HOH D .   ? 0.33733 0.32934 0.36928 0.02817  0.00418  -0.03876 413 HOH A O   
2209 O  O   . HOH D .   ? 0.17035 0.21320 0.31580 -0.01628 0.02313  -0.01053 414 HOH A O   
2210 O  O   . HOH D .   ? 0.25089 0.23576 0.33250 0.01948  -0.03993 0.04007  415 HOH A O   
2211 O  O   . HOH D .   ? 0.14264 0.13354 0.13171 -0.00005 -0.00946 -0.00208 416 HOH A O   
2212 O  O   . HOH D .   ? 0.52321 0.43408 0.38707 -0.03307 0.03314  0.02771  417 HOH A O   
2213 O  O   . HOH D .   ? 0.22874 0.20019 0.25083 0.03011  -0.03284 0.00623  418 HOH A O   
2214 O  O   . HOH D .   ? 0.25186 0.24870 0.26272 -0.02346 -0.00798 0.00693  419 HOH A O   
2215 O  O   . HOH D .   ? 0.50090 0.39906 0.47997 0.01808  -0.02960 0.03414  420 HOH A O   
2216 O  O   . HOH D .   ? 0.19821 0.16594 0.15219 -0.01618 -0.02004 -0.01252 421 HOH A O   
2217 O  O   . HOH D .   ? 0.29618 0.23644 0.21761 -0.02322 0.04000  0.00128  422 HOH A O   
2218 O  O   . HOH D .   ? 0.27169 0.33281 0.32324 -0.02112 0.00601  -0.00103 423 HOH A O   
2219 O  O   . HOH D .   ? 0.20742 0.14095 0.14371 -0.01018 0.00134  0.01817  424 HOH A O   
2220 O  O   . HOH D .   ? 0.43013 0.32828 0.37710 0.00641  -0.02543 0.04173  425 HOH A O   
2221 O  O   . HOH D .   ? 0.13071 0.10360 0.13783 -0.00626 0.03117  -0.01173 426 HOH A O   
2222 O  O   . HOH D .   ? 0.19563 0.23310 0.21872 0.01658  0.02521  -0.04354 427 HOH A O   
2223 O  O   . HOH D .   ? 0.15361 0.13931 0.20926 -0.02999 0.03140  -0.00188 428 HOH A O   
2224 O  O   . HOH D .   ? 0.25426 0.26393 0.36618 0.02187  -0.04079 0.03038  429 HOH A O   
2225 O  O   . HOH D .   ? 0.17880 0.16851 0.21971 -0.01297 0.03012  -0.00606 430 HOH A O   
2226 O  O   . HOH D .   ? 0.32112 0.32705 0.42076 -0.04316 0.05181  -0.00393 431 HOH A O   
2227 O  O   . HOH D .   ? 0.19018 0.18443 0.17874 -0.00563 -0.01705 0.01739  432 HOH A O   
2228 O  O   . HOH D .   ? 0.30757 0.33632 0.37399 -0.02154 -0.04069 -0.01269 433 HOH A O   
2229 O  O   . HOH D .   ? 0.44837 0.33827 0.32902 -0.02657 0.01192  0.05252  434 HOH A O   
2230 O  O   . HOH D .   ? 0.32840 0.30699 0.38822 0.01375  -0.03388 0.03723  435 HOH A O   
2231 O  O   . HOH D .   ? 0.32690 0.37747 0.43019 -0.00785 -0.05165 0.00380  436 HOH A O   
2232 O  O   . HOH D .   ? 0.35859 0.29812 0.35952 -0.01664 -0.02063 0.06530  437 HOH A O   
2233 O  O   . HOH D .   ? 0.12049 0.08838 0.14560 0.00206  -0.00842 0.01154  438 HOH A O   
2234 O  O   . HOH D .   ? 0.15571 0.11961 0.19916 0.00748  -0.00605 0.00981  439 HOH A O   
2235 O  O   . HOH D .   ? 0.40999 0.40339 0.38057 -0.01502 -0.04401 -0.00656 440 HOH A O   
2236 O  O   . HOH D .   ? 0.12065 0.16696 0.16267 -0.02560 0.00121  0.00282  441 HOH A O   
2237 O  O   . HOH D .   ? 0.41842 0.36042 0.41146 -0.03092 -0.01137 -0.02356 442 HOH A O   
2238 O  O   . HOH D .   ? 0.10159 0.09111 0.18651 0.01641  -0.01178 0.01204  443 HOH A O   
2239 O  O   . HOH D .   ? 0.33759 0.28242 0.34557 -0.00724 0.00210  -0.00993 444 HOH A O   
2240 O  O   . HOH D .   ? 0.24388 0.19601 0.28703 0.03690  -0.01096 -0.02432 445 HOH A O   
2241 O  O   . HOH D .   ? 0.11199 0.12086 0.18107 -0.01322 0.00246  -0.00540 446 HOH A O   
2242 O  O   . HOH D .   ? 0.19098 0.17855 0.19665 -0.03440 0.00070  0.02947  447 HOH A O   
2243 O  O   . HOH D .   ? 0.38430 0.39628 0.48828 -0.03620 0.00789  -0.01110 448 HOH A O   
2244 O  O   . HOH D .   ? 0.29689 0.35644 0.45708 -0.01502 -0.01187 -0.00767 449 HOH A O   
2245 O  O   . HOH D .   ? 0.31177 0.36986 0.37688 -0.02040 -0.02904 -0.00650 450 HOH A O   
2246 O  O   . HOH D .   ? 0.30224 0.25263 0.24718 -0.01725 0.04723  -0.01632 451 HOH A O   
2247 O  O   . HOH D .   ? 0.15296 0.15296 0.17675 -0.03162 -0.00761 -0.00761 452 HOH A O   
2248 O  O   . HOH D .   ? 0.39365 0.33088 0.33970 -0.01303 0.03004  -0.03526 453 HOH A O   
2249 O  O   . HOH D .   ? 0.13993 0.10091 0.13660 -0.00584 -0.00486 -0.00391 454 HOH A O   
2250 O  O   . HOH D .   ? 0.30479 0.31495 0.40350 -0.00371 0.06340  -0.02329 455 HOH A O   
2251 O  O   . HOH D .   ? 0.18972 0.15483 0.18355 -0.00537 -0.00077 -0.00534 456 HOH A O   
2252 O  O   . HOH D .   ? 0.29078 0.34955 0.45890 -0.01035 0.00149  -0.00806 457 HOH A O   
2253 O  O   . HOH D .   ? 0.24973 0.28717 0.32878 -0.01517 -0.04309 -0.00499 458 HOH A O   
2254 O  O   . HOH D .   ? 0.39545 0.40873 0.44144 0.02845  -0.00442 -0.02328 459 HOH A O   
2255 O  O   . HOH D .   ? 0.22434 0.17364 0.23331 -0.01617 -0.00541 -0.00083 460 HOH A O   
2256 O  O   . HOH D .   ? 0.19458 0.14375 0.14825 -0.01437 0.01865  0.00587  461 HOH A O   
2257 O  O   . HOH D .   ? 0.28205 0.27840 0.28628 0.00153  -0.05582 0.05234  462 HOH A O   
2258 O  O   . HOH D .   ? 0.39233 0.34070 0.41074 -0.00929 -0.01509 0.03630  463 HOH A O   
2259 O  O   . HOH D .   ? 0.17863 0.15227 0.23730 0.01043  0.01289  -0.00718 464 HOH A O   
2260 O  O   . HOH D .   ? 0.33237 0.28019 0.34821 -0.01810 -0.00938 0.02844  465 HOH A O   
2261 O  O   . HOH D .   ? 0.20095 0.13673 0.10334 -0.01475 0.00163  0.01084  466 HOH A O   
2262 O  O   . HOH D .   ? 0.22761 0.18589 0.23228 -0.00365 0.00208  -0.00638 467 HOH A O   
2263 O  O   . HOH D .   ? 0.21995 0.21963 0.29616 -0.02844 0.01338  -0.00698 468 HOH A O   
2264 O  O   . HOH D .   ? 0.13048 0.14866 0.23678 0.00070  0.02176  -0.00896 469 HOH A O   
2265 O  O   . HOH D .   ? 0.17344 0.13076 0.15921 -0.00682 0.00420  -0.01252 470 HOH A O   
2266 O  O   . HOH D .   ? 0.15246 0.12144 0.16875 -0.01497 -0.00239 -0.00675 471 HOH A O   
2267 O  O   . HOH D .   ? 0.40912 0.33676 0.41715 0.00003  -0.00694 -0.05099 472 HOH A O   
2268 O  O   . HOH D .   ? 0.20215 0.16161 0.17330 -0.01246 0.03972  -0.01373 473 HOH A O   
2269 O  O   . HOH D .   ? 0.18155 0.13949 0.20326 0.00134  0.00316  -0.00349 474 HOH A O   
2270 O  O   . HOH D .   ? 0.32831 0.24886 0.33781 -0.04461 0.03345  0.01974  475 HOH A O   
2271 O  O   . HOH D .   ? 0.16040 0.18331 0.20536 -0.01633 -0.04025 -0.00872 476 HOH A O   
2272 O  O   . HOH D .   ? 0.16785 0.13249 0.18784 -0.01781 -0.00611 -0.01214 477 HOH A O   
2273 O  O   . HOH D .   ? 0.18078 0.16377 0.23274 -0.02761 0.01763  -0.00348 478 HOH A O   
2274 O  O   . HOH D .   ? 0.26776 0.31328 0.23916 -0.02004 0.02605  -0.00119 479 HOH A O   
2275 O  O   . HOH D .   ? 0.35741 0.34961 0.31116 -0.01224 -0.04079 0.05345  480 HOH A O   
2276 O  O   . HOH D .   ? 0.37086 0.39509 0.35440 -0.01305 -0.05957 0.01091  481 HOH A O   
2277 O  O   . HOH D .   ? 0.44644 0.39681 0.36306 -0.01898 -0.01245 -0.01674 482 HOH A O   
2278 O  O   . HOH D .   ? 0.31172 0.26628 0.24850 -0.01846 -0.01236 -0.01888 483 HOH A O   
2279 O  O   . HOH D .   ? 0.45384 0.39725 0.44757 -0.01128 0.00264  -0.01741 484 HOH A O   
2280 O  O   . HOH D .   ? 0.44062 0.44229 0.41544 -0.00664 -0.01765 -0.00920 485 HOH A O   
2281 O  O   . HOH D .   ? 0.23807 0.25675 0.29698 0.03160  -0.02278 -0.00928 486 HOH A O   
2282 O  O   . HOH D .   ? 0.38226 0.41538 0.39347 -0.03656 0.01638  0.01989  487 HOH A O   
2283 O  O   . HOH D .   ? 0.37427 0.28053 0.37993 0.00602  -0.01075 -0.00218 488 HOH A O   
2284 O  O   . HOH D .   ? 0.43499 0.36559 0.44642 -0.00950 -0.01005 -0.03421 489 HOH A O   
2285 O  O   . HOH D .   ? 0.16012 0.16362 0.21423 -0.02223 -0.01818 -0.01402 490 HOH A O   
2286 O  O   . HOH D .   ? 0.23645 0.31281 0.24723 -0.01471 0.04490  -0.01824 491 HOH A O   
2287 O  O   . HOH D .   ? 0.30786 0.31449 0.27660 -0.00636 -0.01073 -0.00341 492 HOH A O   
2288 O  O   . HOH D .   ? 0.41626 0.31026 0.35064 -0.01995 0.00867  0.03825  493 HOH A O   
2289 O  O   . HOH D .   ? 0.34651 0.39123 0.50953 0.02396  -0.05270 0.02713  494 HOH A O   
2290 O  O   . HOH D .   ? 0.15566 0.16445 0.15872 0.00653  -0.00591 -0.00976 495 HOH A O   
2291 O  O   . HOH D .   ? 0.29671 0.24557 0.30654 -0.02103 -0.01095 0.04105  496 HOH A O   
2292 O  O   . HOH D .   ? 0.25580 0.25817 0.29117 0.02732  0.00108  -0.03102 497 HOH A O   
2293 O  O   . HOH D .   ? 0.34659 0.33473 0.29719 -0.01605 -0.05435 -0.00495 498 HOH A O   
2294 O  O   . HOH D .   ? 0.29441 0.33701 0.46908 0.01845  -0.00579 0.00122  499 HOH A O   
2295 O  O   . HOH D .   ? 0.32022 0.29276 0.39698 0.01452  0.02281  -0.01412 500 HOH A O   
2296 O  O   . HOH D .   ? 0.13136 0.09602 0.13568 -0.01080 -0.00084 -0.00300 501 HOH A O   
2297 O  O   . HOH D .   ? 0.34771 0.25021 0.33776 -0.02024 0.00651  0.01664  502 HOH A O   
2298 O  O   . HOH D .   ? 0.40723 0.36172 0.42454 -0.02907 -0.00642 0.01703  503 HOH A O   
2299 O  O   . HOH D .   ? 0.11119 0.09153 0.10497 -0.00201 -0.00991 -0.00822 504 HOH A O   
2300 O  O   . HOH D .   ? 0.28519 0.29260 0.41749 0.01964  0.01762  -0.00841 505 HOH A O   
2301 O  O   . HOH D .   ? 0.29082 0.35933 0.47440 0.00673  -0.03001 0.00403  506 HOH A O   
2302 O  O   . HOH D .   ? 0.19233 0.14599 0.19535 -0.01498 -0.01575 -0.04204 507 HOH A O   
2303 O  O   . HOH D .   ? 0.51734 0.42462 0.41458 -0.03924 0.04437  0.03659  508 HOH A O   
2304 O  O   . HOH D .   ? 0.34569 0.37121 0.29923 -0.03661 0.02018  0.03105  509 HOH A O   
2305 O  O   . HOH D .   ? 0.30247 0.29908 0.28485 -0.01475 -0.02749 -0.02590 510 HOH A O   
2306 O  O   . HOH D .   ? 0.19472 0.14819 0.23494 0.00608  0.00214  0.00007  511 HOH A O   
2307 O  O   . HOH D .   ? 0.35313 0.44518 0.44133 0.01208  0.02858  -0.03128 512 HOH A O   
2308 O  O   . HOH D .   ? 0.30037 0.28346 0.26991 -0.00871 -0.01337 -0.04387 513 HOH A O   
2309 O  O   . HOH D .   ? 0.25255 0.30729 0.27846 0.01148  0.03350  -0.04152 514 HOH A O   
2310 O  O   . HOH D .   ? 0.37288 0.34067 0.43527 0.01277  -0.00254 0.00633  515 HOH A O   
2311 O  O   . HOH D .   ? 0.24583 0.19611 0.24322 -0.00418 0.01105  -0.01702 516 HOH A O   
2312 O  O   . HOH D .   ? 0.19191 0.16442 0.16529 -0.00903 -0.04085 0.06796  517 HOH A O   
2313 O  O   . HOH D .   ? 0.15744 0.23301 0.23716 0.00771  0.00281  -0.01641 518 HOH A O   
2314 O  O   . HOH D .   ? 0.36272 0.36599 0.38256 0.00521  -0.06358 0.05254  519 HOH A O   
2315 O  O   . HOH D .   ? 0.35969 0.30694 0.30838 -0.02086 -0.00708 -0.02654 520 HOH A O   
2316 O  O   . HOH D .   ? 0.26861 0.32338 0.44015 0.01114  -0.02016 0.00406  521 HOH A O   
2317 O  O   . HOH D .   ? 0.29450 0.25238 0.32578 -0.02557 -0.00159 -0.01116 522 HOH A O   
2318 O  O   . HOH D .   ? 0.29430 0.26411 0.26168 -0.00354 -0.00180 -0.06823 523 HOH A O   
2319 O  O   . HOH D .   ? 0.34211 0.33691 0.39628 0.03709  -0.00994 -0.02257 524 HOH A O   
2320 O  O   . HOH D .   ? 0.37801 0.38699 0.34166 -0.00596 -0.00651 -0.01179 525 HOH A O   
2321 O  O   . HOH D .   ? 0.38645 0.49748 0.48931 0.01631  0.05266  -0.04768 526 HOH A O   
2322 O  O   . HOH D .   ? 0.34262 0.35200 0.30299 -0.00981 -0.01126 0.00415  527 HOH A O   
2323 O  O   . HOH D .   ? 0.24939 0.21616 0.24685 -0.02028 -0.02241 -0.04620 528 HOH A O   
2324 O  O   . HOH D .   ? 0.47851 0.42933 0.49459 -0.02838 -0.00764 0.00433  529 HOH A O   
2325 O  O   . HOH D .   ? 0.34743 0.34578 0.32982 -0.00633 -0.02430 0.02192  530 HOH A O   
2326 O  O   . HOH D .   ? 0.37117 0.32941 0.39832 0.00551  -0.04150 0.06278  531 HOH A O   
2327 O  O   . HOH D .   ? 0.30909 0.39291 0.33317 -0.00753 0.05036  -0.02921 532 HOH A O   
2328 O  O   . HOH D .   ? 0.31049 0.40704 0.39746 0.02158  0.05756  -0.05700 533 HOH A O   
2329 O  O   . HOH D .   ? 0.38213 0.40677 0.50930 -0.04284 0.05799  -0.00772 534 HOH A O   
2330 O  O   . HOH D .   ? 0.34657 0.40723 0.37670 0.01545  0.04670  -0.05613 535 HOH A O   
2331 O  O   . HOH D .   ? 0.38416 0.32638 0.38777 -0.01610 -0.00289 -0.01089 536 HOH A O   
2332 O  O   . HOH D .   ? 0.29671 0.32482 0.52257 0.04277  -0.01421 0.01019  537 HOH A O   
# 
