data_9G8D
# 
_entry.id   9G8D 
# 
_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   9G8D         pdb_00009g8d 10.2210/pdb9g8d/pdb 
WWPDB D_1292140313 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-27 
2 'Structure model' 1 1 2024-12-11 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9G8D 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-23 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'Agp2 - Pfr'                    6G1Y unspecified 
PDB 'PAiRFP2 - Pfr'                 6G1Z unspecified 
PDB 'PAiRFP2 - Meta-F'              6G20 unspecified 
PDB 'PAiRFP2 SFX - Pfr (I0a)'       8RJM unspecified 
PDB 'PAiRFP2 SFX - Pfr (I0b)'       8RJN unspecified 
PDB 'PAiRFP2 SFX - intermediate I1' 8RJO unspecified 
PDB 'PAiRFP2 SFX - intermediate I2' 8RJP unspecified 
PDB 'PAiRFP2 SFX - intermediate I3' 8RJQ unspecified 
PDB 'PAiRFP2 SFX - intermediate I4' 8RJR unspecified 
PDB 'PAiRFP2 SFX - intermediate I5' 8RJS unspecified 
PDB 'PAiRFP2 SFX - intermediate I6' 8RJT unspecified 
PDB 'PAiRFP2 SFX - intermediate I7' 8RJU unspecified 
PDB 'Agp2-Y165oCNF - Pfr'           9G8C unspecified 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              patrick.scheerer@charite.de 
_pdbx_contact_author.name_first         Patrick 
_pdbx_contact_author.name_last          Scheerer 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5028-2075 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sauthof, L.'  1 0000-0002-6727-8395 
'Schmidt, A.'  2 0000-0003-1985-1908 
'Scheerer, P.' 3 0000-0001-5028-2075 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Phys.Chem.B 
_citation.journal_id_ASTM           JPCBFK 
_citation.journal_id_CSD            1278 
_citation.journal_id_ISSN           1089-5647 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            128 
_citation.language                  ? 
_citation.page_first                11644 
_citation.page_last                 11657 
_citation.title                     
'Hydrogen Bonding and Noncovalent Electric Field Effects in the Photoconversion of a Phytochrome.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jpcb.4c06419 
_citation.pdbx_database_id_PubMed   39561028 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nguyen, A.D.'    1  ? 
primary 'Michael, N.'     2  ? 
primary 'Sauthof, L.'     3  ? 
primary 'von Sass, J.'    4  ? 
primary 'Hoang, O.T.'     5  ? 
primary 'Schmidt, A.'     6  ? 
primary 'La Greca, M.'    7  ? 
primary 'Schlesinger, R.' 8  ? 
primary 'Budisa, N.'      9  ? 
primary 'Scheerer, P.'    10 ? 
primary 'Mroginski, M.A.' 11 ? 
primary 'Kraskov, A.'     12 ? 
primary 'Hildebrandt, P.' 13 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'histidine kinase' 56606.355 1   2.7.13.3 F192oCNF ? ? 
2 polymer     man 'histidine kinase' 56593.332 1   2.7.13.3 ?        ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER' 106.120   2   ?        ?        ? ? 
4 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL' 118.174   2   ?        ?        ? ? 
5 non-polymer syn 
;3-[(2Z)-2-({3-(2-carboxyethyl)-5-[(E)-(4-ethenyl-3-methyl-5-oxo-1,5-dihydro-2H-pyrrol-2-ylidene)methyl]-4-methyl-1H-pyrrol-2-yl}methylidene)-5-{(Z)-[(3E,4S)-3-ethylidene-4-methyl-5-oxopyrrolidin-2-ylidene]methyl}-4-methyl-2H-pyrrol-3-yl]propanoic acid
;
584.662   2   ?        ?        ? ? 
6 non-polymer syn 'CHLORIDE ION' 35.453    2   ?        ?        ? ? 
7 water       nat water 18.015    656 ?        ?        ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no yes 
;MASTDYHVDLTNCDREPIHIPGYIQPHGCLIACDNAMRMVLRHSENCGELLGLEGDLNGRTAEDVLGKKLVHDLRNALTV
TGRTTRPAMLPAMETSDGRSFDISLHRYKSTTIIEFEPSGSDAQPLGTARKMVDRIREADSVESLISRTTRLV(MLZ)AT
LGYDRVMIYRFQEDGAG(MLZ)VVSEA(MLZ)QPELESFLGQY(9IJ)PASDIPQQARALYL(MLZ)NTLRIISDASGTR
IPVLPAVDVSGEPLDLSYAHLRSVSPIHCEYLRNMGVAASMSISVIVDGALWGLIACHHYSPRVLSMPVRIAAEMFGEFF
SMHLQVLKQ(MLZ)RRLDTINHAHAALDRFLRLAAHHANIEELLVDSFQDFADLMPCDGVGLWVGNNWHGHGATPPHDAI
PRLARFVASASEGRVWATHALSQAIPEAEIYAGTAAGMLAIPLSQVKSDYLLFFR(MLZ)EIVQNLNWAGNPE(MLZ)SY
ETGPMGDRLTPR(MLZ)SFAIW(MLZ)ETVRLQAQPWSEADREIAEAARIALVEVAFHHSEHHHHHH
;
;MASTDYHVDLTNCDREPIHIPGYIQPHGCLIACDNAMRMVLRHSENCGELLGLEGDLNGRTAEDVLGKKLVHDLRNALTV
TGRTTRPAMLPAMETSDGRSFDISLHRYKSTTIIEFEPSGSDAQPLGTARKMVDRIREADSVESLISRTTRLVKATLGYD
RVMIYRFQEDGAGKVVSEAKQPELESFLGQYXPASDIPQQARALYLKNTLRIISDASGTRIPVLPAVDVSGEPLDLSYAH
LRSVSPIHCEYLRNMGVAASMSISVIVDGALWGLIACHHYSPRVLSMPVRIAAEMFGEFFSMHLQVLKQKRRLDTINHAH
AALDRFLRLAAHHANIEELLVDSFQDFADLMPCDGVGLWVGNNWHGHGATPPHDAIPRLARFVASASEGRVWATHALSQA
IPEAEIYAGTAAGMLAIPLSQVKSDYLLFFRKEIVQNLNWAGNPEKSYETGPMGDRLTPRKSFAIWKETVRLQAQPWSEA
DREIAEAARIALVEVAFHHSEHHHHHH
;
A ? 
2 'polypeptide(L)' no yes 
;MASTDYHVDLTNCDREPIHIPGYIQPHGCLIACDNAMRMVLRHSENCGELLGLEGDLNGRTAEDVLGKKLVHDLRNALTV
TGRTTRPAMLPAMETSDGRSFDISLHRYKSTTIIEFEPSGSDAQPLGTARKMVDRIREADSVESLISRTTRLV(MLZ)AT
LGYDRVMIYRFQEDGAG(MLZ)VVSEA(MLZ)QPELESFLGQY(9IJ)PASDIPQQARALYL(MLZ)NTLRIISDASGTR
IPVLPAVDVSGEPLDLSYAHLRSVSPIHCEYLRNMGVAASMSISVIVDGALWGLIACHHYSPRVLSMPVRIAAEMFGEFF
SMHLQVLKQ(MLZ)RRLDTINHAHAALDRFLRLAAHHANIEELLVDSFQDFADLMPCDGVGLWVGNNWHGHGATPPHDAI
PRLARFVASASEGRVWATHALSQAIPEAEIYAGTAAGMLAIPLSQVKSDYLLFFR(MLZ)EIVQNLNWAGNPE(MLZ)SY
ETGPMGDRLTPRKSFAIW(MLZ)ETVRLQAQPWSEADREIAEAARIALVEVAFHHSEHHHHHH
;
;MASTDYHVDLTNCDREPIHIPGYIQPHGCLIACDNAMRMVLRHSENCGELLGLEGDLNGRTAEDVLGKKLVHDLRNALTV
TGRTTRPAMLPAMETSDGRSFDISLHRYKSTTIIEFEPSGSDAQPLGTARKMVDRIREADSVESLISRTTRLVKATLGYD
RVMIYRFQEDGAGKVVSEAKQPELESFLGQYXPASDIPQQARALYLKNTLRIISDASGTRIPVLPAVDVSGEPLDLSYAH
LRSVSPIHCEYLRNMGVAASMSISVIVDGALWGLIACHHYSPRVLSMPVRIAAEMFGEFFSMHLQVLKQKRRLDTINHAH
AALDRFLRLAAHHANIEELLVDSFQDFADLMPCDGVGLWVGNNWHGHGATPPHDAIPRLARFVASASEGRVWATHALSQA
IPEAEIYAGTAAGMLAIPLSQVKSDYLLFFRKEIVQNLNWAGNPEKSYETGPMGDRLTPRKSFAIWKETVRLQAQPWSEA
DREIAEAARIALVEVAFHHSEHHHHHH
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DI(HYDROXYETHYL)ETHER' PEG 
4 '(4S)-2-METHYL-2,4-PENTANEDIOL' MPD 
5 
;3-[(2Z)-2-({3-(2-carboxyethyl)-5-[(E)-(4-ethenyl-3-methyl-5-oxo-1,5-dihydro-2H-pyrrol-2-ylidene)methyl]-4-methyl-1H-pyrrol-2-yl}methylidene)-5-{(Z)-[(3E,4S)-3-ethylidene-4-methyl-5-oxopyrrolidin-2-ylidene]methyl}-4-methyl-2H-pyrrol-3-yl]propanoic acid
;
EL5 
6 'CHLORIDE ION' CL  
7 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   ALA n 
1 3   SER n 
1 4   THR n 
1 5   ASP n 
1 6   TYR n 
1 7   HIS n 
1 8   VAL n 
1 9   ASP n 
1 10  LEU n 
1 11  THR n 
1 12  ASN n 
1 13  CYS n 
1 14  ASP n 
1 15  ARG n 
1 16  GLU n 
1 17  PRO n 
1 18  ILE n 
1 19  HIS n 
1 20  ILE n 
1 21  PRO n 
1 22  GLY n 
1 23  TYR n 
1 24  ILE n 
1 25  GLN n 
1 26  PRO n 
1 27  HIS n 
1 28  GLY n 
1 29  CYS n 
1 30  LEU n 
1 31  ILE n 
1 32  ALA n 
1 33  CYS n 
1 34  ASP n 
1 35  ASN n 
1 36  ALA n 
1 37  MET n 
1 38  ARG n 
1 39  MET n 
1 40  VAL n 
1 41  LEU n 
1 42  ARG n 
1 43  HIS n 
1 44  SER n 
1 45  GLU n 
1 46  ASN n 
1 47  CYS n 
1 48  GLY n 
1 49  GLU n 
1 50  LEU n 
1 51  LEU n 
1 52  GLY n 
1 53  LEU n 
1 54  GLU n 
1 55  GLY n 
1 56  ASP n 
1 57  LEU n 
1 58  ASN n 
1 59  GLY n 
1 60  ARG n 
1 61  THR n 
1 62  ALA n 
1 63  GLU n 
1 64  ASP n 
1 65  VAL n 
1 66  LEU n 
1 67  GLY n 
1 68  LYS n 
1 69  LYS n 
1 70  LEU n 
1 71  VAL n 
1 72  HIS n 
1 73  ASP n 
1 74  LEU n 
1 75  ARG n 
1 76  ASN n 
1 77  ALA n 
1 78  LEU n 
1 79  THR n 
1 80  VAL n 
1 81  THR n 
1 82  GLY n 
1 83  ARG n 
1 84  THR n 
1 85  THR n 
1 86  ARG n 
1 87  PRO n 
1 88  ALA n 
1 89  MET n 
1 90  LEU n 
1 91  PRO n 
1 92  ALA n 
1 93  MET n 
1 94  GLU n 
1 95  THR n 
1 96  SER n 
1 97  ASP n 
1 98  GLY n 
1 99  ARG n 
1 100 SER n 
1 101 PHE n 
1 102 ASP n 
1 103 ILE n 
1 104 SER n 
1 105 LEU n 
1 106 HIS n 
1 107 ARG n 
1 108 TYR n 
1 109 LYS n 
1 110 SER n 
1 111 THR n 
1 112 THR n 
1 113 ILE n 
1 114 ILE n 
1 115 GLU n 
1 116 PHE n 
1 117 GLU n 
1 118 PRO n 
1 119 SER n 
1 120 GLY n 
1 121 SER n 
1 122 ASP n 
1 123 ALA n 
1 124 GLN n 
1 125 PRO n 
1 126 LEU n 
1 127 GLY n 
1 128 THR n 
1 129 ALA n 
1 130 ARG n 
1 131 LYS n 
1 132 MET n 
1 133 VAL n 
1 134 ASP n 
1 135 ARG n 
1 136 ILE n 
1 137 ARG n 
1 138 GLU n 
1 139 ALA n 
1 140 ASP n 
1 141 SER n 
1 142 VAL n 
1 143 GLU n 
1 144 SER n 
1 145 LEU n 
1 146 ILE n 
1 147 SER n 
1 148 ARG n 
1 149 THR n 
1 150 THR n 
1 151 ARG n 
1 152 LEU n 
1 153 VAL n 
1 154 MLZ n 
1 155 ALA n 
1 156 THR n 
1 157 LEU n 
1 158 GLY n 
1 159 TYR n 
1 160 ASP n 
1 161 ARG n 
1 162 VAL n 
1 163 MET n 
1 164 ILE n 
1 165 TYR n 
1 166 ARG n 
1 167 PHE n 
1 168 GLN n 
1 169 GLU n 
1 170 ASP n 
1 171 GLY n 
1 172 ALA n 
1 173 GLY n 
1 174 MLZ n 
1 175 VAL n 
1 176 VAL n 
1 177 SER n 
1 178 GLU n 
1 179 ALA n 
1 180 MLZ n 
1 181 GLN n 
1 182 PRO n 
1 183 GLU n 
1 184 LEU n 
1 185 GLU n 
1 186 SER n 
1 187 PHE n 
1 188 LEU n 
1 189 GLY n 
1 190 GLN n 
1 191 TYR n 
1 192 9IJ n 
1 193 PRO n 
1 194 ALA n 
1 195 SER n 
1 196 ASP n 
1 197 ILE n 
1 198 PRO n 
1 199 GLN n 
1 200 GLN n 
1 201 ALA n 
1 202 ARG n 
1 203 ALA n 
1 204 LEU n 
1 205 TYR n 
1 206 LEU n 
1 207 MLZ n 
1 208 ASN n 
1 209 THR n 
1 210 LEU n 
1 211 ARG n 
1 212 ILE n 
1 213 ILE n 
1 214 SER n 
1 215 ASP n 
1 216 ALA n 
1 217 SER n 
1 218 GLY n 
1 219 THR n 
1 220 ARG n 
1 221 ILE n 
1 222 PRO n 
1 223 VAL n 
1 224 LEU n 
1 225 PRO n 
1 226 ALA n 
1 227 VAL n 
1 228 ASP n 
1 229 VAL n 
1 230 SER n 
1 231 GLY n 
1 232 GLU n 
1 233 PRO n 
1 234 LEU n 
1 235 ASP n 
1 236 LEU n 
1 237 SER n 
1 238 TYR n 
1 239 ALA n 
1 240 HIS n 
1 241 LEU n 
1 242 ARG n 
1 243 SER n 
1 244 VAL n 
1 245 SER n 
1 246 PRO n 
1 247 ILE n 
1 248 HIS n 
1 249 CYS n 
1 250 GLU n 
1 251 TYR n 
1 252 LEU n 
1 253 ARG n 
1 254 ASN n 
1 255 MET n 
1 256 GLY n 
1 257 VAL n 
1 258 ALA n 
1 259 ALA n 
1 260 SER n 
1 261 MET n 
1 262 SER n 
1 263 ILE n 
1 264 SER n 
1 265 VAL n 
1 266 ILE n 
1 267 VAL n 
1 268 ASP n 
1 269 GLY n 
1 270 ALA n 
1 271 LEU n 
1 272 TRP n 
1 273 GLY n 
1 274 LEU n 
1 275 ILE n 
1 276 ALA n 
1 277 CYS n 
1 278 HIS n 
1 279 HIS n 
1 280 TYR n 
1 281 SER n 
1 282 PRO n 
1 283 ARG n 
1 284 VAL n 
1 285 LEU n 
1 286 SER n 
1 287 MET n 
1 288 PRO n 
1 289 VAL n 
1 290 ARG n 
1 291 ILE n 
1 292 ALA n 
1 293 ALA n 
1 294 GLU n 
1 295 MET n 
1 296 PHE n 
1 297 GLY n 
1 298 GLU n 
1 299 PHE n 
1 300 PHE n 
1 301 SER n 
1 302 MET n 
1 303 HIS n 
1 304 LEU n 
1 305 GLN n 
1 306 VAL n 
1 307 LEU n 
1 308 LYS n 
1 309 GLN n 
1 310 MLZ n 
1 311 ARG n 
1 312 ARG n 
1 313 LEU n 
1 314 ASP n 
1 315 THR n 
1 316 ILE n 
1 317 ASN n 
1 318 HIS n 
1 319 ALA n 
1 320 HIS n 
1 321 ALA n 
1 322 ALA n 
1 323 LEU n 
1 324 ASP n 
1 325 ARG n 
1 326 PHE n 
1 327 LEU n 
1 328 ARG n 
1 329 LEU n 
1 330 ALA n 
1 331 ALA n 
1 332 HIS n 
1 333 HIS n 
1 334 ALA n 
1 335 ASN n 
1 336 ILE n 
1 337 GLU n 
1 338 GLU n 
1 339 LEU n 
1 340 LEU n 
1 341 VAL n 
1 342 ASP n 
1 343 SER n 
1 344 PHE n 
1 345 GLN n 
1 346 ASP n 
1 347 PHE n 
1 348 ALA n 
1 349 ASP n 
1 350 LEU n 
1 351 MET n 
1 352 PRO n 
1 353 CYS n 
1 354 ASP n 
1 355 GLY n 
1 356 VAL n 
1 357 GLY n 
1 358 LEU n 
1 359 TRP n 
1 360 VAL n 
1 361 GLY n 
1 362 ASN n 
1 363 ASN n 
1 364 TRP n 
1 365 HIS n 
1 366 GLY n 
1 367 HIS n 
1 368 GLY n 
1 369 ALA n 
1 370 THR n 
1 371 PRO n 
1 372 PRO n 
1 373 HIS n 
1 374 ASP n 
1 375 ALA n 
1 376 ILE n 
1 377 PRO n 
1 378 ARG n 
1 379 LEU n 
1 380 ALA n 
1 381 ARG n 
1 382 PHE n 
1 383 VAL n 
1 384 ALA n 
1 385 SER n 
1 386 ALA n 
1 387 SER n 
1 388 GLU n 
1 389 GLY n 
1 390 ARG n 
1 391 VAL n 
1 392 TRP n 
1 393 ALA n 
1 394 THR n 
1 395 HIS n 
1 396 ALA n 
1 397 LEU n 
1 398 SER n 
1 399 GLN n 
1 400 ALA n 
1 401 ILE n 
1 402 PRO n 
1 403 GLU n 
1 404 ALA n 
1 405 GLU n 
1 406 ILE n 
1 407 TYR n 
1 408 ALA n 
1 409 GLY n 
1 410 THR n 
1 411 ALA n 
1 412 ALA n 
1 413 GLY n 
1 414 MET n 
1 415 LEU n 
1 416 ALA n 
1 417 ILE n 
1 418 PRO n 
1 419 LEU n 
1 420 SER n 
1 421 GLN n 
1 422 VAL n 
1 423 LYS n 
1 424 SER n 
1 425 ASP n 
1 426 TYR n 
1 427 LEU n 
1 428 LEU n 
1 429 PHE n 
1 430 PHE n 
1 431 ARG n 
1 432 MLZ n 
1 433 GLU n 
1 434 ILE n 
1 435 VAL n 
1 436 GLN n 
1 437 ASN n 
1 438 LEU n 
1 439 ASN n 
1 440 TRP n 
1 441 ALA n 
1 442 GLY n 
1 443 ASN n 
1 444 PRO n 
1 445 GLU n 
1 446 MLZ n 
1 447 SER n 
1 448 TYR n 
1 449 GLU n 
1 450 THR n 
1 451 GLY n 
1 452 PRO n 
1 453 MET n 
1 454 GLY n 
1 455 ASP n 
1 456 ARG n 
1 457 LEU n 
1 458 THR n 
1 459 PRO n 
1 460 ARG n 
1 461 MLZ n 
1 462 SER n 
1 463 PHE n 
1 464 ALA n 
1 465 ILE n 
1 466 TRP n 
1 467 MLZ n 
1 468 GLU n 
1 469 THR n 
1 470 VAL n 
1 471 ARG n 
1 472 LEU n 
1 473 GLN n 
1 474 ALA n 
1 475 GLN n 
1 476 PRO n 
1 477 TRP n 
1 478 SER n 
1 479 GLU n 
1 480 ALA n 
1 481 ASP n 
1 482 ARG n 
1 483 GLU n 
1 484 ILE n 
1 485 ALA n 
1 486 GLU n 
1 487 ALA n 
1 488 ALA n 
1 489 ARG n 
1 490 ILE n 
1 491 ALA n 
1 492 LEU n 
1 493 VAL n 
1 494 GLU n 
1 495 VAL n 
1 496 ALA n 
1 497 PHE n 
1 498 HIS n 
1 499 HIS n 
1 500 SER n 
1 501 GLU n 
1 502 HIS n 
1 503 HIS n 
1 504 HIS n 
1 505 HIS n 
1 506 HIS n 
1 507 HIS n 
2 1   MET n 
2 2   ALA n 
2 3   SER n 
2 4   THR n 
2 5   ASP n 
2 6   TYR n 
2 7   HIS n 
2 8   VAL n 
2 9   ASP n 
2 10  LEU n 
2 11  THR n 
2 12  ASN n 
2 13  CYS n 
2 14  ASP n 
2 15  ARG n 
2 16  GLU n 
2 17  PRO n 
2 18  ILE n 
2 19  HIS n 
2 20  ILE n 
2 21  PRO n 
2 22  GLY n 
2 23  TYR n 
2 24  ILE n 
2 25  GLN n 
2 26  PRO n 
2 27  HIS n 
2 28  GLY n 
2 29  CYS n 
2 30  LEU n 
2 31  ILE n 
2 32  ALA n 
2 33  CYS n 
2 34  ASP n 
2 35  ASN n 
2 36  ALA n 
2 37  MET n 
2 38  ARG n 
2 39  MET n 
2 40  VAL n 
2 41  LEU n 
2 42  ARG n 
2 43  HIS n 
2 44  SER n 
2 45  GLU n 
2 46  ASN n 
2 47  CYS n 
2 48  GLY n 
2 49  GLU n 
2 50  LEU n 
2 51  LEU n 
2 52  GLY n 
2 53  LEU n 
2 54  GLU n 
2 55  GLY n 
2 56  ASP n 
2 57  LEU n 
2 58  ASN n 
2 59  GLY n 
2 60  ARG n 
2 61  THR n 
2 62  ALA n 
2 63  GLU n 
2 64  ASP n 
2 65  VAL n 
2 66  LEU n 
2 67  GLY n 
2 68  LYS n 
2 69  LYS n 
2 70  LEU n 
2 71  VAL n 
2 72  HIS n 
2 73  ASP n 
2 74  LEU n 
2 75  ARG n 
2 76  ASN n 
2 77  ALA n 
2 78  LEU n 
2 79  THR n 
2 80  VAL n 
2 81  THR n 
2 82  GLY n 
2 83  ARG n 
2 84  THR n 
2 85  THR n 
2 86  ARG n 
2 87  PRO n 
2 88  ALA n 
2 89  MET n 
2 90  LEU n 
2 91  PRO n 
2 92  ALA n 
2 93  MET n 
2 94  GLU n 
2 95  THR n 
2 96  SER n 
2 97  ASP n 
2 98  GLY n 
2 99  ARG n 
2 100 SER n 
2 101 PHE n 
2 102 ASP n 
2 103 ILE n 
2 104 SER n 
2 105 LEU n 
2 106 HIS n 
2 107 ARG n 
2 108 TYR n 
2 109 LYS n 
2 110 SER n 
2 111 THR n 
2 112 THR n 
2 113 ILE n 
2 114 ILE n 
2 115 GLU n 
2 116 PHE n 
2 117 GLU n 
2 118 PRO n 
2 119 SER n 
2 120 GLY n 
2 121 SER n 
2 122 ASP n 
2 123 ALA n 
2 124 GLN n 
2 125 PRO n 
2 126 LEU n 
2 127 GLY n 
2 128 THR n 
2 129 ALA n 
2 130 ARG n 
2 131 LYS n 
2 132 MET n 
2 133 VAL n 
2 134 ASP n 
2 135 ARG n 
2 136 ILE n 
2 137 ARG n 
2 138 GLU n 
2 139 ALA n 
2 140 ASP n 
2 141 SER n 
2 142 VAL n 
2 143 GLU n 
2 144 SER n 
2 145 LEU n 
2 146 ILE n 
2 147 SER n 
2 148 ARG n 
2 149 THR n 
2 150 THR n 
2 151 ARG n 
2 152 LEU n 
2 153 VAL n 
2 154 MLZ n 
2 155 ALA n 
2 156 THR n 
2 157 LEU n 
2 158 GLY n 
2 159 TYR n 
2 160 ASP n 
2 161 ARG n 
2 162 VAL n 
2 163 MET n 
2 164 ILE n 
2 165 TYR n 
2 166 ARG n 
2 167 PHE n 
2 168 GLN n 
2 169 GLU n 
2 170 ASP n 
2 171 GLY n 
2 172 ALA n 
2 173 GLY n 
2 174 MLZ n 
2 175 VAL n 
2 176 VAL n 
2 177 SER n 
2 178 GLU n 
2 179 ALA n 
2 180 MLZ n 
2 181 GLN n 
2 182 PRO n 
2 183 GLU n 
2 184 LEU n 
2 185 GLU n 
2 186 SER n 
2 187 PHE n 
2 188 LEU n 
2 189 GLY n 
2 190 GLN n 
2 191 TYR n 
2 192 9IJ n 
2 193 PRO n 
2 194 ALA n 
2 195 SER n 
2 196 ASP n 
2 197 ILE n 
2 198 PRO n 
2 199 GLN n 
2 200 GLN n 
2 201 ALA n 
2 202 ARG n 
2 203 ALA n 
2 204 LEU n 
2 205 TYR n 
2 206 LEU n 
2 207 MLZ n 
2 208 ASN n 
2 209 THR n 
2 210 LEU n 
2 211 ARG n 
2 212 ILE n 
2 213 ILE n 
2 214 SER n 
2 215 ASP n 
2 216 ALA n 
2 217 SER n 
2 218 GLY n 
2 219 THR n 
2 220 ARG n 
2 221 ILE n 
2 222 PRO n 
2 223 VAL n 
2 224 LEU n 
2 225 PRO n 
2 226 ALA n 
2 227 VAL n 
2 228 ASP n 
2 229 VAL n 
2 230 SER n 
2 231 GLY n 
2 232 GLU n 
2 233 PRO n 
2 234 LEU n 
2 235 ASP n 
2 236 LEU n 
2 237 SER n 
2 238 TYR n 
2 239 ALA n 
2 240 HIS n 
2 241 LEU n 
2 242 ARG n 
2 243 SER n 
2 244 VAL n 
2 245 SER n 
2 246 PRO n 
2 247 ILE n 
2 248 HIS n 
2 249 CYS n 
2 250 GLU n 
2 251 TYR n 
2 252 LEU n 
2 253 ARG n 
2 254 ASN n 
2 255 MET n 
2 256 GLY n 
2 257 VAL n 
2 258 ALA n 
2 259 ALA n 
2 260 SER n 
2 261 MET n 
2 262 SER n 
2 263 ILE n 
2 264 SER n 
2 265 VAL n 
2 266 ILE n 
2 267 VAL n 
2 268 ASP n 
2 269 GLY n 
2 270 ALA n 
2 271 LEU n 
2 272 TRP n 
2 273 GLY n 
2 274 LEU n 
2 275 ILE n 
2 276 ALA n 
2 277 CYS n 
2 278 HIS n 
2 279 HIS n 
2 280 TYR n 
2 281 SER n 
2 282 PRO n 
2 283 ARG n 
2 284 VAL n 
2 285 LEU n 
2 286 SER n 
2 287 MET n 
2 288 PRO n 
2 289 VAL n 
2 290 ARG n 
2 291 ILE n 
2 292 ALA n 
2 293 ALA n 
2 294 GLU n 
2 295 MET n 
2 296 PHE n 
2 297 GLY n 
2 298 GLU n 
2 299 PHE n 
2 300 PHE n 
2 301 SER n 
2 302 MET n 
2 303 HIS n 
2 304 LEU n 
2 305 GLN n 
2 306 VAL n 
2 307 LEU n 
2 308 LYS n 
2 309 GLN n 
2 310 MLZ n 
2 311 ARG n 
2 312 ARG n 
2 313 LEU n 
2 314 ASP n 
2 315 THR n 
2 316 ILE n 
2 317 ASN n 
2 318 HIS n 
2 319 ALA n 
2 320 HIS n 
2 321 ALA n 
2 322 ALA n 
2 323 LEU n 
2 324 ASP n 
2 325 ARG n 
2 326 PHE n 
2 327 LEU n 
2 328 ARG n 
2 329 LEU n 
2 330 ALA n 
2 331 ALA n 
2 332 HIS n 
2 333 HIS n 
2 334 ALA n 
2 335 ASN n 
2 336 ILE n 
2 337 GLU n 
2 338 GLU n 
2 339 LEU n 
2 340 LEU n 
2 341 VAL n 
2 342 ASP n 
2 343 SER n 
2 344 PHE n 
2 345 GLN n 
2 346 ASP n 
2 347 PHE n 
2 348 ALA n 
2 349 ASP n 
2 350 LEU n 
2 351 MET n 
2 352 PRO n 
2 353 CYS n 
2 354 ASP n 
2 355 GLY n 
2 356 VAL n 
2 357 GLY n 
2 358 LEU n 
2 359 TRP n 
2 360 VAL n 
2 361 GLY n 
2 362 ASN n 
2 363 ASN n 
2 364 TRP n 
2 365 HIS n 
2 366 GLY n 
2 367 HIS n 
2 368 GLY n 
2 369 ALA n 
2 370 THR n 
2 371 PRO n 
2 372 PRO n 
2 373 HIS n 
2 374 ASP n 
2 375 ALA n 
2 376 ILE n 
2 377 PRO n 
2 378 ARG n 
2 379 LEU n 
2 380 ALA n 
2 381 ARG n 
2 382 PHE n 
2 383 VAL n 
2 384 ALA n 
2 385 SER n 
2 386 ALA n 
2 387 SER n 
2 388 GLU n 
2 389 GLY n 
2 390 ARG n 
2 391 VAL n 
2 392 TRP n 
2 393 ALA n 
2 394 THR n 
2 395 HIS n 
2 396 ALA n 
2 397 LEU n 
2 398 SER n 
2 399 GLN n 
2 400 ALA n 
2 401 ILE n 
2 402 PRO n 
2 403 GLU n 
2 404 ALA n 
2 405 GLU n 
2 406 ILE n 
2 407 TYR n 
2 408 ALA n 
2 409 GLY n 
2 410 THR n 
2 411 ALA n 
2 412 ALA n 
2 413 GLY n 
2 414 MET n 
2 415 LEU n 
2 416 ALA n 
2 417 ILE n 
2 418 PRO n 
2 419 LEU n 
2 420 SER n 
2 421 GLN n 
2 422 VAL n 
2 423 LYS n 
2 424 SER n 
2 425 ASP n 
2 426 TYR n 
2 427 LEU n 
2 428 LEU n 
2 429 PHE n 
2 430 PHE n 
2 431 ARG n 
2 432 MLZ n 
2 433 GLU n 
2 434 ILE n 
2 435 VAL n 
2 436 GLN n 
2 437 ASN n 
2 438 LEU n 
2 439 ASN n 
2 440 TRP n 
2 441 ALA n 
2 442 GLY n 
2 443 ASN n 
2 444 PRO n 
2 445 GLU n 
2 446 MLZ n 
2 447 SER n 
2 448 TYR n 
2 449 GLU n 
2 450 THR n 
2 451 GLY n 
2 452 PRO n 
2 453 MET n 
2 454 GLY n 
2 455 ASP n 
2 456 ARG n 
2 457 LEU n 
2 458 THR n 
2 459 PRO n 
2 460 ARG n 
2 461 LYS n 
2 462 SER n 
2 463 PHE n 
2 464 ALA n 
2 465 ILE n 
2 466 TRP n 
2 467 MLZ n 
2 468 GLU n 
2 469 THR n 
2 470 VAL n 
2 471 ARG n 
2 472 LEU n 
2 473 GLN n 
2 474 ALA n 
2 475 GLN n 
2 476 PRO n 
2 477 TRP n 
2 478 SER n 
2 479 GLU n 
2 480 ALA n 
2 481 ASP n 
2 482 ARG n 
2 483 GLU n 
2 484 ILE n 
2 485 ALA n 
2 486 GLU n 
2 487 ALA n 
2 488 ALA n 
2 489 ARG n 
2 490 ILE n 
2 491 ALA n 
2 492 LEU n 
2 493 VAL n 
2 494 GLU n 
2 495 VAL n 
2 496 ALA n 
2 497 PHE n 
2 498 HIS n 
2 499 HIS n 
2 500 SER n 
2 501 GLU n 
2 502 HIS n 
2 503 HIS n 
2 504 HIS n 
2 505 HIS n 
2 506 HIS n 
2 507 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 507 ? ? Atu2165 ? ? ? ? ? ? 'Agrobacterium fabrum str. C58' 176299 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 507 ? ? Atu2165 ? ? ? ? ? ? 'Agrobacterium fabrum str. C58' 176299 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
9IJ non-polymer         n 2-cyano-L-phenylalanine ?                                     'C10 H10 N2 O2'  190.199 
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 
CL  non-polymer         . 'CHLORIDE ION' ?                                     'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE ?                                     'C3 H7 N O2 S'   121.158 
EL5 non-polymer         . 
;3-[(2Z)-2-({3-(2-carboxyethyl)-5-[(E)-(4-ethenyl-3-methyl-5-oxo-1,5-dihydro-2H-pyrrol-2-ylidene)methyl]-4-methyl-1H-pyrrol-2-yl}methylidene)-5-{(Z)-[(3E,4S)-3-ethylidene-4-methyl-5-oxopyrrolidin-2-ylidene]methyl}-4-methyl-2H-pyrrol-3-yl]propanoic acid
;
'biliverdin, bound form at Pfr state' 'C33 H36 N4 O6'  584.662 
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 
MLZ 'L-peptide linking' n N-METHYL-LYSINE ?                                     'C7 H16 N2 O2'   160.214 
MPD non-polymer         . '(4S)-2-METHYL-2,4-PENTANEDIOL' ?                                     'C6 H14 O2'      118.174 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                                     'C4 H10 O3'      106.120 
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   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   ?   ?   ?   A . n 
A 1 4   THR 4   4   ?   ?   ?   A . n 
A 1 5   ASP 5   5   ?   ?   ?   A . n 
A 1 6   TYR 6   6   ?   ?   ?   A . n 
A 1 7   HIS 7   7   7   HIS HIS A . n 
A 1 8   VAL 8   8   8   VAL VAL A . n 
A 1 9   ASP 9   9   9   ASP ASP A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  ASN 12  12  12  ASN ASN A . n 
A 1 13  CYS 13  13  13  CYS CYS A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ARG 15  15  15  ARG ARG A . n 
A 1 16  GLU 16  16  16  GLU GLU A . n 
A 1 17  PRO 17  17  17  PRO PRO A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  HIS 19  19  19  HIS HIS A . n 
A 1 20  ILE 20  20  20  ILE ILE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  TYR 23  23  23  TYR TYR A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  PRO 26  26  26  PRO PRO A . n 
A 1 27  HIS 27  27  27  HIS HIS A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  CYS 29  29  29  CYS CYS A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  CYS 33  33  33  CYS CYS A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  ASN 35  35  35  ASN ASN A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  MET 37  37  37  MET MET A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  MET 39  39  39  MET MET A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  ARG 42  42  42  ARG ARG A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  CYS 47  47  47  CYS CYS A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  ASP 64  64  64  ASP ASP A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  HIS 72  72  72  HIS HIS A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  ASN 76  76  76  ASN ASN A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  GLY 82  82  ?   ?   ?   A . n 
A 1 83  ARG 83  83  ?   ?   ?   A . n 
A 1 84  THR 84  84  ?   ?   ?   A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  MET 89  89  89  MET MET A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  MET 93  93  93  MET MET A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  THR 95  95  95  THR THR A . n 
A 1 96  SER 96  96  ?   ?   ?   A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 PHE 101 101 101 PHE PHE A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 HIS 106 106 106 HIS HIS A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 SER 110 110 110 SER SER A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 PRO 118 118 118 PRO PRO A . n 
A 1 119 SER 119 119 119 SER SER A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 ?   ?   ?   A . n 
A 1 122 ASP 122 122 ?   ?   ?   A . n 
A 1 123 ALA 123 123 ?   ?   ?   A . n 
A 1 124 GLN 124 124 ?   ?   ?   A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 ARG 130 130 130 ARG ARG A . n 
A 1 131 LYS 131 131 131 LYS LYS A . n 
A 1 132 MET 132 132 132 MET MET A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 ASP 134 134 134 ASP ASP A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 ARG 137 137 137 ARG ARG A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 ARG 151 151 151 ARG ARG A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 MLZ 154 154 154 MLZ MLZ A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 TYR 159 159 159 TYR TYR A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 MET 163 163 163 MET MET A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 TYR 165 165 165 TYR TYR A . n 
A 1 166 ARG 166 166 166 ARG ARG A . n 
A 1 167 PHE 167 167 167 PHE PHE A . n 
A 1 168 GLN 168 168 168 GLN GLN A . n 
A 1 169 GLU 169 169 169 GLU GLU A . n 
A 1 170 ASP 170 170 170 ASP ASP A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 MLZ 174 174 174 MLZ MLZ A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 VAL 176 176 176 VAL VAL A . n 
A 1 177 SER 177 177 177 SER SER A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 MLZ 180 180 180 MLZ MLZ A . n 
A 1 181 GLN 181 181 181 GLN GLN A . n 
A 1 182 PRO 182 182 182 PRO PRO A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 PHE 187 187 187 PHE PHE A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 GLN 190 190 190 GLN GLN A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 9IJ 192 192 192 9IJ oCF A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 ASP 196 196 196 ASP ASP A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 GLN 199 199 199 GLN GLN A . n 
A 1 200 GLN 200 200 200 GLN GLN A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 ARG 202 202 202 ARG ARG A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 TYR 205 205 205 TYR TYR A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 MLZ 207 207 207 MLZ MLZ A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 SER 214 214 214 SER SER A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 GLY 218 218 218 GLY GLY A . n 
A 1 219 THR 219 219 219 THR THR A . n 
A 1 220 ARG 220 220 220 ARG ARG A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 PRO 225 225 225 PRO PRO A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 VAL 227 227 227 VAL VAL A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 VAL 229 229 229 VAL VAL A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 GLU 232 232 232 GLU GLU A . n 
A 1 233 PRO 233 233 233 PRO PRO A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 SER 237 237 237 SER SER A . n 
A 1 238 TYR 238 238 238 TYR TYR A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 HIS 240 240 240 HIS HIS A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 ARG 242 242 242 ARG ARG A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 SER 245 245 245 SER SER A . n 
A 1 246 PRO 246 246 246 PRO PRO A . n 
A 1 247 ILE 247 247 247 ILE ILE A . n 
A 1 248 HIS 248 248 248 HIS HIS A . n 
A 1 249 CYS 249 249 249 CYS CYS A . n 
A 1 250 GLU 250 250 250 GLU GLU A . n 
A 1 251 TYR 251 251 251 TYR TYR A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 ASN 254 254 254 ASN ASN A . n 
A 1 255 MET 255 255 255 MET MET A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 MET 261 261 261 MET MET A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 ILE 263 263 263 ILE ILE A . n 
A 1 264 SER 264 264 264 SER SER A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 ILE 266 266 266 ILE ILE A . n 
A 1 267 VAL 267 267 267 VAL VAL A . n 
A 1 268 ASP 268 268 268 ASP ASP A . n 
A 1 269 GLY 269 269 269 GLY GLY A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 TRP 272 272 272 TRP TRP A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 CYS 277 277 277 CYS CYS A . n 
A 1 278 HIS 278 278 278 HIS HIS A . n 
A 1 279 HIS 279 279 279 HIS HIS A . n 
A 1 280 TYR 280 280 280 TYR TYR A . n 
A 1 281 SER 281 281 281 SER SER A . n 
A 1 282 PRO 282 282 282 PRO PRO A . n 
A 1 283 ARG 283 283 283 ARG ARG A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 MET 287 287 287 MET MET A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 ARG 290 290 290 ARG ARG A . n 
A 1 291 ILE 291 291 291 ILE ILE A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 ALA 293 293 293 ALA ALA A . n 
A 1 294 GLU 294 294 294 GLU GLU A . n 
A 1 295 MET 295 295 295 MET MET A . n 
A 1 296 PHE 296 296 296 PHE PHE A . n 
A 1 297 GLY 297 297 297 GLY GLY A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 PHE 299 299 299 PHE PHE A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 MET 302 302 302 MET MET A . n 
A 1 303 HIS 303 303 303 HIS HIS A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 GLN 305 305 305 GLN GLN A . n 
A 1 306 VAL 306 306 306 VAL VAL A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 GLN 309 309 309 GLN GLN A . n 
A 1 310 MLZ 310 310 310 MLZ MLZ A . n 
A 1 311 ARG 311 311 311 ARG ARG A . n 
A 1 312 ARG 312 312 312 ARG ARG A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 ASP 314 314 314 ASP ASP A . n 
A 1 315 THR 315 315 315 THR THR A . n 
A 1 316 ILE 316 316 316 ILE ILE A . n 
A 1 317 ASN 317 317 317 ASN ASN A . n 
A 1 318 HIS 318 318 318 HIS HIS A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 HIS 320 320 320 HIS HIS A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 ALA 322 322 322 ALA ALA A . n 
A 1 323 LEU 323 323 323 LEU LEU A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 ARG 325 325 325 ARG ARG A . n 
A 1 326 PHE 326 326 326 PHE PHE A . n 
A 1 327 LEU 327 327 327 LEU LEU A . n 
A 1 328 ARG 328 328 328 ARG ARG A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 HIS 332 332 332 HIS HIS A . n 
A 1 333 HIS 333 333 333 HIS HIS A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 ASN 335 335 335 ASN ASN A . n 
A 1 336 ILE 336 336 336 ILE ILE A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 GLU 338 338 338 GLU GLU A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 ASP 342 342 342 ASP ASP A . n 
A 1 343 SER 343 343 343 SER SER A . n 
A 1 344 PHE 344 344 344 PHE PHE A . n 
A 1 345 GLN 345 345 345 GLN GLN A . n 
A 1 346 ASP 346 346 346 ASP ASP A . n 
A 1 347 PHE 347 347 347 PHE PHE A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 MET 351 351 351 MET MET A . n 
A 1 352 PRO 352 352 352 PRO PRO A . n 
A 1 353 CYS 353 353 353 CYS CYS A . n 
A 1 354 ASP 354 354 354 ASP ASP A . n 
A 1 355 GLY 355 355 355 GLY GLY A . n 
A 1 356 VAL 356 356 356 VAL VAL A . n 
A 1 357 GLY 357 357 357 GLY GLY A . n 
A 1 358 LEU 358 358 358 LEU LEU A . n 
A 1 359 TRP 359 359 359 TRP TRP A . n 
A 1 360 VAL 360 360 360 VAL VAL A . n 
A 1 361 GLY 361 361 361 GLY GLY A . n 
A 1 362 ASN 362 362 362 ASN ASN A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 TRP 364 364 364 TRP TRP A . n 
A 1 365 HIS 365 365 365 HIS HIS A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 HIS 367 367 367 HIS HIS A . n 
A 1 368 GLY 368 368 368 GLY GLY A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 THR 370 370 370 THR THR A . n 
A 1 371 PRO 371 371 371 PRO PRO A . n 
A 1 372 PRO 372 372 372 PRO PRO A . n 
A 1 373 HIS 373 373 373 HIS HIS A . n 
A 1 374 ASP 374 374 374 ASP ASP A . n 
A 1 375 ALA 375 375 375 ALA ALA A . n 
A 1 376 ILE 376 376 376 ILE ILE A . n 
A 1 377 PRO 377 377 377 PRO PRO A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 ALA 380 380 380 ALA ALA A . n 
A 1 381 ARG 381 381 381 ARG ARG A . n 
A 1 382 PHE 382 382 382 PHE PHE A . n 
A 1 383 VAL 383 383 383 VAL VAL A . n 
A 1 384 ALA 384 384 384 ALA ALA A . n 
A 1 385 SER 385 385 385 SER SER A . n 
A 1 386 ALA 386 386 386 ALA ALA A . n 
A 1 387 SER 387 387 387 SER SER A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 ARG 390 390 390 ARG ARG A . n 
A 1 391 VAL 391 391 391 VAL VAL A . n 
A 1 392 TRP 392 392 392 TRP TRP A . n 
A 1 393 ALA 393 393 393 ALA ALA A . n 
A 1 394 THR 394 394 394 THR THR A . n 
A 1 395 HIS 395 395 395 HIS HIS A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 LEU 397 397 397 LEU LEU A . n 
A 1 398 SER 398 398 398 SER SER A . n 
A 1 399 GLN 399 399 399 GLN GLN A . n 
A 1 400 ALA 400 400 400 ALA ALA A . n 
A 1 401 ILE 401 401 401 ILE ILE A . n 
A 1 402 PRO 402 402 402 PRO PRO A . n 
A 1 403 GLU 403 403 403 GLU GLU A . n 
A 1 404 ALA 404 404 404 ALA ALA A . n 
A 1 405 GLU 405 405 405 GLU GLU A . n 
A 1 406 ILE 406 406 406 ILE ILE A . n 
A 1 407 TYR 407 407 407 TYR TYR A . n 
A 1 408 ALA 408 408 408 ALA ALA A . n 
A 1 409 GLY 409 409 409 GLY GLY A . n 
A 1 410 THR 410 410 410 THR THR A . n 
A 1 411 ALA 411 411 411 ALA ALA A . n 
A 1 412 ALA 412 412 412 ALA ALA A . n 
A 1 413 GLY 413 413 413 GLY GLY A . n 
A 1 414 MET 414 414 414 MET MET A . n 
A 1 415 LEU 415 415 415 LEU LEU A . n 
A 1 416 ALA 416 416 416 ALA ALA A . n 
A 1 417 ILE 417 417 417 ILE ILE A . n 
A 1 418 PRO 418 418 418 PRO PRO A . n 
A 1 419 LEU 419 419 419 LEU LEU A . n 
A 1 420 SER 420 420 420 SER SER A . n 
A 1 421 GLN 421 421 421 GLN GLN A . n 
A 1 422 VAL 422 422 422 VAL VAL A . n 
A 1 423 LYS 423 423 423 LYS LYS A . n 
A 1 424 SER 424 424 424 SER SER A . n 
A 1 425 ASP 425 425 425 ASP ASP A . n 
A 1 426 TYR 426 426 426 TYR TYR A . n 
A 1 427 LEU 427 427 427 LEU LEU A . n 
A 1 428 LEU 428 428 428 LEU LEU A . n 
A 1 429 PHE 429 429 429 PHE PHE A . n 
A 1 430 PHE 430 430 430 PHE PHE A . n 
A 1 431 ARG 431 431 431 ARG ARG A . n 
A 1 432 MLZ 432 432 432 MLZ MLZ A . n 
A 1 433 GLU 433 433 433 GLU GLU A . n 
A 1 434 ILE 434 434 434 ILE ILE A . n 
A 1 435 VAL 435 435 435 VAL VAL A . n 
A 1 436 GLN 436 436 436 GLN GLN A . n 
A 1 437 ASN 437 437 437 ASN ASN A . n 
A 1 438 LEU 438 438 438 LEU LEU A . n 
A 1 439 ASN 439 439 439 ASN ASN A . n 
A 1 440 TRP 440 440 440 TRP TRP A . n 
A 1 441 ALA 441 441 441 ALA ALA A . n 
A 1 442 GLY 442 442 442 GLY GLY A . n 
A 1 443 ASN 443 443 443 ASN ASN A . n 
A 1 444 PRO 444 444 444 PRO PRO A . n 
A 1 445 GLU 445 445 445 GLU GLU A . n 
A 1 446 MLZ 446 446 446 MLZ MLZ A . n 
A 1 447 SER 447 447 447 SER SER A . n 
A 1 448 TYR 448 448 448 TYR TYR A . n 
A 1 449 GLU 449 449 449 GLU GLU A . n 
A 1 450 THR 450 450 450 THR THR A . n 
A 1 451 GLY 451 451 451 GLY GLY A . n 
A 1 452 PRO 452 452 452 PRO PRO A . n 
A 1 453 MET 453 453 453 MET MET A . n 
A 1 454 GLY 454 454 454 GLY GLY A . n 
A 1 455 ASP 455 455 455 ASP ASP A . n 
A 1 456 ARG 456 456 456 ARG ARG A . n 
A 1 457 LEU 457 457 457 LEU LEU A . n 
A 1 458 THR 458 458 458 THR THR A . n 
A 1 459 PRO 459 459 459 PRO PRO A . n 
A 1 460 ARG 460 460 460 ARG ARG A . n 
A 1 461 MLZ 461 461 461 MLZ MLZ A . n 
A 1 462 SER 462 462 462 SER SER A . n 
A 1 463 PHE 463 463 463 PHE PHE A . n 
A 1 464 ALA 464 464 464 ALA ALA A . n 
A 1 465 ILE 465 465 465 ILE ILE A . n 
A 1 466 TRP 466 466 466 TRP TRP A . n 
A 1 467 MLZ 467 467 467 MLZ MLZ A . n 
A 1 468 GLU 468 468 468 GLU GLU A . n 
A 1 469 THR 469 469 469 THR THR A . n 
A 1 470 VAL 470 470 470 VAL VAL A . n 
A 1 471 ARG 471 471 471 ARG ARG A . n 
A 1 472 LEU 472 472 472 LEU LEU A . n 
A 1 473 GLN 473 473 473 GLN GLN A . n 
A 1 474 ALA 474 474 474 ALA ALA A . n 
A 1 475 GLN 475 475 475 GLN GLN A . n 
A 1 476 PRO 476 476 476 PRO PRO A . n 
A 1 477 TRP 477 477 477 TRP TRP A . n 
A 1 478 SER 478 478 478 SER SER A . n 
A 1 479 GLU 479 479 479 GLU GLU A . n 
A 1 480 ALA 480 480 480 ALA ALA A . n 
A 1 481 ASP 481 481 481 ASP ASP A . n 
A 1 482 ARG 482 482 482 ARG ARG A . n 
A 1 483 GLU 483 483 483 GLU GLU A . n 
A 1 484 ILE 484 484 484 ILE ILE A . n 
A 1 485 ALA 485 485 485 ALA ALA A . n 
A 1 486 GLU 486 486 486 GLU GLU A . n 
A 1 487 ALA 487 487 487 ALA ALA A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 ARG 489 489 489 ARG ARG A . n 
A 1 490 ILE 490 490 490 ILE ILE A . n 
A 1 491 ALA 491 491 491 ALA ALA A . n 
A 1 492 LEU 492 492 492 LEU LEU A . n 
A 1 493 VAL 493 493 493 VAL VAL A . n 
A 1 494 GLU 494 494 494 GLU GLU A . n 
A 1 495 VAL 495 495 495 VAL VAL A . n 
A 1 496 ALA 496 496 496 ALA ALA A . n 
A 1 497 PHE 497 497 497 PHE PHE A . n 
A 1 498 HIS 498 498 498 HIS HIS A . n 
A 1 499 HIS 499 499 499 HIS HIS A . n 
A 1 500 SER 500 500 500 SER SER A . n 
A 1 501 GLU 501 501 501 GLU GLU A . n 
A 1 502 HIS 502 502 502 HIS HIS A . n 
A 1 503 HIS 503 503 503 HIS HIS A . n 
A 1 504 HIS 504 504 ?   ?   ?   A . n 
A 1 505 HIS 505 505 ?   ?   ?   A . n 
A 1 506 HIS 506 506 ?   ?   ?   A . n 
A 1 507 HIS 507 507 ?   ?   ?   A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   ALA 2   2   ?   ?   ?   B . n 
B 2 3   SER 3   3   ?   ?   ?   B . n 
B 2 4   THR 4   4   ?   ?   ?   B . n 
B 2 5   ASP 5   5   ?   ?   ?   B . n 
B 2 6   TYR 6   6   6   TYR TYR B . n 
B 2 7   HIS 7   7   7   HIS HIS B . n 
B 2 8   VAL 8   8   8   VAL VAL B . n 
B 2 9   ASP 9   9   9   ASP ASP B . n 
B 2 10  LEU 10  10  10  LEU LEU B . n 
B 2 11  THR 11  11  11  THR THR B . n 
B 2 12  ASN 12  12  12  ASN ASN B . n 
B 2 13  CYS 13  13  13  CYS CYS B . n 
B 2 14  ASP 14  14  14  ASP ASP B . n 
B 2 15  ARG 15  15  15  ARG ARG B . n 
B 2 16  GLU 16  16  16  GLU GLU B . n 
B 2 17  PRO 17  17  17  PRO PRO B . n 
B 2 18  ILE 18  18  18  ILE ILE B . n 
B 2 19  HIS 19  19  19  HIS HIS B . n 
B 2 20  ILE 20  20  20  ILE ILE B . n 
B 2 21  PRO 21  21  21  PRO PRO B . n 
B 2 22  GLY 22  22  22  GLY GLY B . n 
B 2 23  TYR 23  23  23  TYR TYR B . n 
B 2 24  ILE 24  24  24  ILE ILE B . n 
B 2 25  GLN 25  25  25  GLN GLN B . n 
B 2 26  PRO 26  26  26  PRO PRO B . n 
B 2 27  HIS 27  27  27  HIS HIS B . n 
B 2 28  GLY 28  28  28  GLY GLY B . n 
B 2 29  CYS 29  29  29  CYS CYS B . n 
B 2 30  LEU 30  30  30  LEU LEU B . n 
B 2 31  ILE 31  31  31  ILE ILE B . n 
B 2 32  ALA 32  32  32  ALA ALA B . n 
B 2 33  CYS 33  33  33  CYS CYS B . n 
B 2 34  ASP 34  34  34  ASP ASP B . n 
B 2 35  ASN 35  35  35  ASN ASN B . n 
B 2 36  ALA 36  36  36  ALA ALA B . n 
B 2 37  MET 37  37  37  MET MET B . n 
B 2 38  ARG 38  38  38  ARG ARG B . n 
B 2 39  MET 39  39  39  MET MET B . n 
B 2 40  VAL 40  40  40  VAL VAL B . n 
B 2 41  LEU 41  41  41  LEU LEU B . n 
B 2 42  ARG 42  42  42  ARG ARG B . n 
B 2 43  HIS 43  43  43  HIS HIS B . n 
B 2 44  SER 44  44  44  SER SER B . n 
B 2 45  GLU 45  45  45  GLU GLU B . n 
B 2 46  ASN 46  46  46  ASN ASN B . n 
B 2 47  CYS 47  47  47  CYS CYS B . n 
B 2 48  GLY 48  48  48  GLY GLY B . n 
B 2 49  GLU 49  49  49  GLU GLU B . n 
B 2 50  LEU 50  50  50  LEU LEU B . n 
B 2 51  LEU 51  51  51  LEU LEU B . n 
B 2 52  GLY 52  52  52  GLY GLY B . n 
B 2 53  LEU 53  53  53  LEU LEU B . n 
B 2 54  GLU 54  54  54  GLU GLU B . n 
B 2 55  GLY 55  55  55  GLY GLY B . n 
B 2 56  ASP 56  56  56  ASP ASP B . n 
B 2 57  LEU 57  57  57  LEU LEU B . n 
B 2 58  ASN 58  58  58  ASN ASN B . n 
B 2 59  GLY 59  59  59  GLY GLY B . n 
B 2 60  ARG 60  60  60  ARG ARG B . n 
B 2 61  THR 61  61  61  THR THR B . n 
B 2 62  ALA 62  62  62  ALA ALA B . n 
B 2 63  GLU 63  63  63  GLU GLU B . n 
B 2 64  ASP 64  64  64  ASP ASP B . n 
B 2 65  VAL 65  65  65  VAL VAL B . n 
B 2 66  LEU 66  66  66  LEU LEU B . n 
B 2 67  GLY 67  67  67  GLY GLY B . n 
B 2 68  LYS 68  68  68  LYS LYS B . n 
B 2 69  LYS 69  69  69  LYS LYS B . n 
B 2 70  LEU 70  70  70  LEU LEU B . n 
B 2 71  VAL 71  71  71  VAL VAL B . n 
B 2 72  HIS 72  72  72  HIS HIS B . n 
B 2 73  ASP 73  73  73  ASP ASP B . n 
B 2 74  LEU 74  74  74  LEU LEU B . n 
B 2 75  ARG 75  75  75  ARG ARG B . n 
B 2 76  ASN 76  76  76  ASN ASN B . n 
B 2 77  ALA 77  77  77  ALA ALA B . n 
B 2 78  LEU 78  78  78  LEU LEU B . n 
B 2 79  THR 79  79  79  THR THR B . n 
B 2 80  VAL 80  80  80  VAL VAL B . n 
B 2 81  THR 81  81  ?   ?   ?   B . n 
B 2 82  GLY 82  82  ?   ?   ?   B . n 
B 2 83  ARG 83  83  ?   ?   ?   B . n 
B 2 84  THR 84  84  ?   ?   ?   B . n 
B 2 85  THR 85  85  ?   ?   ?   B . n 
B 2 86  ARG 86  86  86  ARG ARG B . n 
B 2 87  PRO 87  87  87  PRO PRO B . n 
B 2 88  ALA 88  88  88  ALA ALA B . n 
B 2 89  MET 89  89  89  MET MET B . n 
B 2 90  LEU 90  90  90  LEU LEU B . n 
B 2 91  PRO 91  91  91  PRO PRO B . n 
B 2 92  ALA 92  92  92  ALA ALA B . n 
B 2 93  MET 93  93  93  MET MET B . n 
B 2 94  GLU 94  94  94  GLU GLU B . n 
B 2 95  THR 95  95  95  THR THR B . n 
B 2 96  SER 96  96  96  SER SER B . n 
B 2 97  ASP 97  97  97  ASP ASP B . n 
B 2 98  GLY 98  98  98  GLY GLY B . n 
B 2 99  ARG 99  99  99  ARG ARG B . n 
B 2 100 SER 100 100 100 SER SER B . n 
B 2 101 PHE 101 101 101 PHE PHE B . n 
B 2 102 ASP 102 102 102 ASP ASP B . n 
B 2 103 ILE 103 103 103 ILE ILE B . n 
B 2 104 SER 104 104 104 SER SER B . n 
B 2 105 LEU 105 105 105 LEU LEU B . n 
B 2 106 HIS 106 106 106 HIS HIS B . n 
B 2 107 ARG 107 107 107 ARG ARG B . n 
B 2 108 TYR 108 108 108 TYR TYR B . n 
B 2 109 LYS 109 109 109 LYS LYS B . n 
B 2 110 SER 110 110 110 SER SER B . n 
B 2 111 THR 111 111 111 THR THR B . n 
B 2 112 THR 112 112 112 THR THR B . n 
B 2 113 ILE 113 113 113 ILE ILE B . n 
B 2 114 ILE 114 114 114 ILE ILE B . n 
B 2 115 GLU 115 115 115 GLU GLU B . n 
B 2 116 PHE 116 116 116 PHE PHE B . n 
B 2 117 GLU 117 117 117 GLU GLU B . n 
B 2 118 PRO 118 118 118 PRO PRO B . n 
B 2 119 SER 119 119 119 SER SER B . n 
B 2 120 GLY 120 120 120 GLY GLY B . n 
B 2 121 SER 121 121 121 SER SER B . n 
B 2 122 ASP 122 122 122 ASP ASP B . n 
B 2 123 ALA 123 123 123 ALA ALA B . n 
B 2 124 GLN 124 124 124 GLN GLN B . n 
B 2 125 PRO 125 125 125 PRO PRO B . n 
B 2 126 LEU 126 126 126 LEU LEU B . n 
B 2 127 GLY 127 127 127 GLY GLY B . n 
B 2 128 THR 128 128 128 THR THR B . n 
B 2 129 ALA 129 129 129 ALA ALA B . n 
B 2 130 ARG 130 130 130 ARG ARG B . n 
B 2 131 LYS 131 131 131 LYS LYS B . n 
B 2 132 MET 132 132 132 MET MET B . n 
B 2 133 VAL 133 133 133 VAL VAL B . n 
B 2 134 ASP 134 134 134 ASP ASP B . n 
B 2 135 ARG 135 135 135 ARG ARG B . n 
B 2 136 ILE 136 136 136 ILE ILE B . n 
B 2 137 ARG 137 137 137 ARG ARG B . n 
B 2 138 GLU 138 138 138 GLU GLU B . n 
B 2 139 ALA 139 139 139 ALA ALA B . n 
B 2 140 ASP 140 140 140 ASP ASP B . n 
B 2 141 SER 141 141 141 SER SER B . n 
B 2 142 VAL 142 142 142 VAL VAL B . n 
B 2 143 GLU 143 143 143 GLU GLU B . n 
B 2 144 SER 144 144 144 SER SER B . n 
B 2 145 LEU 145 145 145 LEU LEU B . n 
B 2 146 ILE 146 146 146 ILE ILE B . n 
B 2 147 SER 147 147 147 SER SER B . n 
B 2 148 ARG 148 148 148 ARG ARG B . n 
B 2 149 THR 149 149 149 THR THR B . n 
B 2 150 THR 150 150 150 THR THR B . n 
B 2 151 ARG 151 151 151 ARG ARG B . n 
B 2 152 LEU 152 152 152 LEU LEU B . n 
B 2 153 VAL 153 153 153 VAL VAL B . n 
B 2 154 MLZ 154 154 154 MLZ MLZ B . n 
B 2 155 ALA 155 155 155 ALA ALA B . n 
B 2 156 THR 156 156 156 THR THR B . n 
B 2 157 LEU 157 157 157 LEU LEU B . n 
B 2 158 GLY 158 158 158 GLY GLY B . n 
B 2 159 TYR 159 159 159 TYR TYR B . n 
B 2 160 ASP 160 160 160 ASP ASP B . n 
B 2 161 ARG 161 161 161 ARG ARG B . n 
B 2 162 VAL 162 162 162 VAL VAL B . n 
B 2 163 MET 163 163 163 MET MET B . n 
B 2 164 ILE 164 164 164 ILE ILE B . n 
B 2 165 TYR 165 165 165 TYR TYR B . n 
B 2 166 ARG 166 166 166 ARG ARG B . n 
B 2 167 PHE 167 167 167 PHE PHE B . n 
B 2 168 GLN 168 168 168 GLN GLN B . n 
B 2 169 GLU 169 169 169 GLU GLU B . n 
B 2 170 ASP 170 170 170 ASP ASP B . n 
B 2 171 GLY 171 171 171 GLY GLY B . n 
B 2 172 ALA 172 172 172 ALA ALA B . n 
B 2 173 GLY 173 173 173 GLY GLY B . n 
B 2 174 MLZ 174 174 174 MLZ MLZ B . n 
B 2 175 VAL 175 175 175 VAL VAL B . n 
B 2 176 VAL 176 176 176 VAL VAL B . n 
B 2 177 SER 177 177 177 SER SER B . n 
B 2 178 GLU 178 178 178 GLU GLU B . n 
B 2 179 ALA 179 179 179 ALA ALA B . n 
B 2 180 MLZ 180 180 180 MLZ MLZ B . n 
B 2 181 GLN 181 181 181 GLN GLN B . n 
B 2 182 PRO 182 182 182 PRO PRO B . n 
B 2 183 GLU 183 183 183 GLU GLU B . n 
B 2 184 LEU 184 184 184 LEU LEU B . n 
B 2 185 GLU 185 185 185 GLU GLU B . n 
B 2 186 SER 186 186 186 SER SER B . n 
B 2 187 PHE 187 187 187 PHE PHE B . n 
B 2 188 LEU 188 188 188 LEU LEU B . n 
B 2 189 GLY 189 189 189 GLY GLY B . n 
B 2 190 GLN 190 190 190 GLN GLN B . n 
B 2 191 TYR 191 191 191 TYR TYR B . n 
B 2 192 9IJ 192 192 192 9IJ oCF B . n 
B 2 193 PRO 193 193 193 PRO PRO B . n 
B 2 194 ALA 194 194 194 ALA ALA B . n 
B 2 195 SER 195 195 195 SER SER B . n 
B 2 196 ASP 196 196 196 ASP ASP B . n 
B 2 197 ILE 197 197 197 ILE ILE B . n 
B 2 198 PRO 198 198 198 PRO PRO B . n 
B 2 199 GLN 199 199 199 GLN GLN B . n 
B 2 200 GLN 200 200 200 GLN GLN B . n 
B 2 201 ALA 201 201 201 ALA ALA B . n 
B 2 202 ARG 202 202 202 ARG ARG B . n 
B 2 203 ALA 203 203 203 ALA ALA B . n 
B 2 204 LEU 204 204 204 LEU LEU B . n 
B 2 205 TYR 205 205 205 TYR TYR B . n 
B 2 206 LEU 206 206 206 LEU LEU B . n 
B 2 207 MLZ 207 207 207 MLZ MLZ B . n 
B 2 208 ASN 208 208 208 ASN ASN B . n 
B 2 209 THR 209 209 209 THR THR B . n 
B 2 210 LEU 210 210 210 LEU LEU B . n 
B 2 211 ARG 211 211 211 ARG ARG B . n 
B 2 212 ILE 212 212 212 ILE ILE B . n 
B 2 213 ILE 213 213 213 ILE ILE B . n 
B 2 214 SER 214 214 214 SER SER B . n 
B 2 215 ASP 215 215 215 ASP ASP B . n 
B 2 216 ALA 216 216 216 ALA ALA B . n 
B 2 217 SER 217 217 217 SER SER B . n 
B 2 218 GLY 218 218 218 GLY GLY B . n 
B 2 219 THR 219 219 219 THR THR B . n 
B 2 220 ARG 220 220 220 ARG ARG B . n 
B 2 221 ILE 221 221 221 ILE ILE B . n 
B 2 222 PRO 222 222 222 PRO PRO B . n 
B 2 223 VAL 223 223 223 VAL VAL B . n 
B 2 224 LEU 224 224 224 LEU LEU B . n 
B 2 225 PRO 225 225 225 PRO PRO B . n 
B 2 226 ALA 226 226 226 ALA ALA B . n 
B 2 227 VAL 227 227 227 VAL VAL B . n 
B 2 228 ASP 228 228 228 ASP ASP B . n 
B 2 229 VAL 229 229 ?   ?   ?   B . n 
B 2 230 SER 230 230 230 SER SER B . n 
B 2 231 GLY 231 231 231 GLY GLY B . n 
B 2 232 GLU 232 232 232 GLU GLU B . n 
B 2 233 PRO 233 233 233 PRO PRO B . n 
B 2 234 LEU 234 234 234 LEU LEU B . n 
B 2 235 ASP 235 235 235 ASP ASP B . n 
B 2 236 LEU 236 236 236 LEU LEU B . n 
B 2 237 SER 237 237 237 SER SER B . n 
B 2 238 TYR 238 238 238 TYR TYR B . n 
B 2 239 ALA 239 239 239 ALA ALA B . n 
B 2 240 HIS 240 240 240 HIS HIS B . n 
B 2 241 LEU 241 241 241 LEU LEU B . n 
B 2 242 ARG 242 242 242 ARG ARG B . n 
B 2 243 SER 243 243 243 SER SER B . n 
B 2 244 VAL 244 244 244 VAL VAL B . n 
B 2 245 SER 245 245 245 SER SER B . n 
B 2 246 PRO 246 246 246 PRO PRO B . n 
B 2 247 ILE 247 247 247 ILE ILE B . n 
B 2 248 HIS 248 248 248 HIS HIS B . n 
B 2 249 CYS 249 249 249 CYS CYS B . n 
B 2 250 GLU 250 250 250 GLU GLU B . n 
B 2 251 TYR 251 251 251 TYR TYR B . n 
B 2 252 LEU 252 252 252 LEU LEU B . n 
B 2 253 ARG 253 253 253 ARG ARG B . n 
B 2 254 ASN 254 254 254 ASN ASN B . n 
B 2 255 MET 255 255 255 MET MET B . n 
B 2 256 GLY 256 256 256 GLY GLY B . n 
B 2 257 VAL 257 257 257 VAL VAL B . n 
B 2 258 ALA 258 258 258 ALA ALA B . n 
B 2 259 ALA 259 259 259 ALA ALA B . n 
B 2 260 SER 260 260 260 SER SER B . n 
B 2 261 MET 261 261 261 MET MET B . n 
B 2 262 SER 262 262 262 SER SER B . n 
B 2 263 ILE 263 263 263 ILE ILE B . n 
B 2 264 SER 264 264 264 SER SER B . n 
B 2 265 VAL 265 265 265 VAL VAL B . n 
B 2 266 ILE 266 266 266 ILE ILE B . n 
B 2 267 VAL 267 267 267 VAL VAL B . n 
B 2 268 ASP 268 268 268 ASP ASP B . n 
B 2 269 GLY 269 269 269 GLY GLY B . n 
B 2 270 ALA 270 270 270 ALA ALA B . n 
B 2 271 LEU 271 271 271 LEU LEU B . n 
B 2 272 TRP 272 272 272 TRP TRP B . n 
B 2 273 GLY 273 273 273 GLY GLY B . n 
B 2 274 LEU 274 274 274 LEU LEU B . n 
B 2 275 ILE 275 275 275 ILE ILE B . n 
B 2 276 ALA 276 276 276 ALA ALA B . n 
B 2 277 CYS 277 277 277 CYS CYS B . n 
B 2 278 HIS 278 278 278 HIS HIS B . n 
B 2 279 HIS 279 279 279 HIS HIS B . n 
B 2 280 TYR 280 280 280 TYR TYR B . n 
B 2 281 SER 281 281 281 SER SER B . n 
B 2 282 PRO 282 282 282 PRO PRO B . n 
B 2 283 ARG 283 283 283 ARG ARG B . n 
B 2 284 VAL 284 284 284 VAL VAL B . n 
B 2 285 LEU 285 285 285 LEU LEU B . n 
B 2 286 SER 286 286 286 SER SER B . n 
B 2 287 MET 287 287 287 MET MET B . n 
B 2 288 PRO 288 288 288 PRO PRO B . n 
B 2 289 VAL 289 289 289 VAL VAL B . n 
B 2 290 ARG 290 290 290 ARG ARG B . n 
B 2 291 ILE 291 291 291 ILE ILE B . n 
B 2 292 ALA 292 292 292 ALA ALA B . n 
B 2 293 ALA 293 293 293 ALA ALA B . n 
B 2 294 GLU 294 294 294 GLU GLU B . n 
B 2 295 MET 295 295 295 MET MET B . n 
B 2 296 PHE 296 296 296 PHE PHE B . n 
B 2 297 GLY 297 297 297 GLY GLY B . n 
B 2 298 GLU 298 298 298 GLU GLU B . n 
B 2 299 PHE 299 299 299 PHE PHE B . n 
B 2 300 PHE 300 300 300 PHE PHE B . n 
B 2 301 SER 301 301 301 SER SER B . n 
B 2 302 MET 302 302 302 MET MET B . n 
B 2 303 HIS 303 303 303 HIS HIS B . n 
B 2 304 LEU 304 304 304 LEU LEU B . n 
B 2 305 GLN 305 305 305 GLN GLN B . n 
B 2 306 VAL 306 306 306 VAL VAL B . n 
B 2 307 LEU 307 307 307 LEU LEU B . n 
B 2 308 LYS 308 308 308 LYS LYS B . n 
B 2 309 GLN 309 309 309 GLN GLN B . n 
B 2 310 MLZ 310 310 310 MLZ MLZ B . n 
B 2 311 ARG 311 311 311 ARG ARG B . n 
B 2 312 ARG 312 312 312 ARG ARG B . n 
B 2 313 LEU 313 313 313 LEU LEU B . n 
B 2 314 ASP 314 314 314 ASP ASP B . n 
B 2 315 THR 315 315 315 THR THR B . n 
B 2 316 ILE 316 316 316 ILE ILE B . n 
B 2 317 ASN 317 317 317 ASN ASN B . n 
B 2 318 HIS 318 318 318 HIS HIS B . n 
B 2 319 ALA 319 319 319 ALA ALA B . n 
B 2 320 HIS 320 320 320 HIS HIS B . n 
B 2 321 ALA 321 321 321 ALA ALA B . n 
B 2 322 ALA 322 322 322 ALA ALA B . n 
B 2 323 LEU 323 323 323 LEU LEU B . n 
B 2 324 ASP 324 324 324 ASP ASP B . n 
B 2 325 ARG 325 325 325 ARG ARG B . n 
B 2 326 PHE 326 326 326 PHE PHE B . n 
B 2 327 LEU 327 327 327 LEU LEU B . n 
B 2 328 ARG 328 328 328 ARG ARG B . n 
B 2 329 LEU 329 329 329 LEU LEU B . n 
B 2 330 ALA 330 330 330 ALA ALA B . n 
B 2 331 ALA 331 331 331 ALA ALA B . n 
B 2 332 HIS 332 332 332 HIS HIS B . n 
B 2 333 HIS 333 333 333 HIS HIS B . n 
B 2 334 ALA 334 334 334 ALA ALA B . n 
B 2 335 ASN 335 335 335 ASN ASN B . n 
B 2 336 ILE 336 336 336 ILE ILE B . n 
B 2 337 GLU 337 337 337 GLU GLU B . n 
B 2 338 GLU 338 338 338 GLU GLU B . n 
B 2 339 LEU 339 339 339 LEU LEU B . n 
B 2 340 LEU 340 340 340 LEU LEU B . n 
B 2 341 VAL 341 341 341 VAL VAL B . n 
B 2 342 ASP 342 342 342 ASP ASP B . n 
B 2 343 SER 343 343 343 SER SER B . n 
B 2 344 PHE 344 344 344 PHE PHE B . n 
B 2 345 GLN 345 345 345 GLN GLN B . n 
B 2 346 ASP 346 346 346 ASP ASP B . n 
B 2 347 PHE 347 347 347 PHE PHE B . n 
B 2 348 ALA 348 348 348 ALA ALA B . n 
B 2 349 ASP 349 349 349 ASP ASP B . n 
B 2 350 LEU 350 350 350 LEU LEU B . n 
B 2 351 MET 351 351 351 MET MET B . n 
B 2 352 PRO 352 352 352 PRO PRO B . n 
B 2 353 CYS 353 353 353 CYS CYS B . n 
B 2 354 ASP 354 354 354 ASP ASP B . n 
B 2 355 GLY 355 355 355 GLY GLY B . n 
B 2 356 VAL 356 356 356 VAL VAL B . n 
B 2 357 GLY 357 357 357 GLY GLY B . n 
B 2 358 LEU 358 358 358 LEU LEU B . n 
B 2 359 TRP 359 359 359 TRP TRP B . n 
B 2 360 VAL 360 360 360 VAL VAL B . n 
B 2 361 GLY 361 361 361 GLY GLY B . n 
B 2 362 ASN 362 362 362 ASN ASN B . n 
B 2 363 ASN 363 363 363 ASN ASN B . n 
B 2 364 TRP 364 364 364 TRP TRP B . n 
B 2 365 HIS 365 365 365 HIS HIS B . n 
B 2 366 GLY 366 366 366 GLY GLY B . n 
B 2 367 HIS 367 367 367 HIS HIS B . n 
B 2 368 GLY 368 368 368 GLY GLY B . n 
B 2 369 ALA 369 369 369 ALA ALA B . n 
B 2 370 THR 370 370 370 THR THR B . n 
B 2 371 PRO 371 371 371 PRO PRO B . n 
B 2 372 PRO 372 372 372 PRO PRO B . n 
B 2 373 HIS 373 373 373 HIS HIS B . n 
B 2 374 ASP 374 374 374 ASP ASP B . n 
B 2 375 ALA 375 375 375 ALA ALA B . n 
B 2 376 ILE 376 376 376 ILE ILE B . n 
B 2 377 PRO 377 377 377 PRO PRO B . n 
B 2 378 ARG 378 378 378 ARG ARG B . n 
B 2 379 LEU 379 379 379 LEU LEU B . n 
B 2 380 ALA 380 380 380 ALA ALA B . n 
B 2 381 ARG 381 381 381 ARG ARG B . n 
B 2 382 PHE 382 382 382 PHE PHE B . n 
B 2 383 VAL 383 383 383 VAL VAL B . n 
B 2 384 ALA 384 384 384 ALA ALA B . n 
B 2 385 SER 385 385 385 SER SER B . n 
B 2 386 ALA 386 386 386 ALA ALA B . n 
B 2 387 SER 387 387 387 SER SER B . n 
B 2 388 GLU 388 388 388 GLU GLU B . n 
B 2 389 GLY 389 389 389 GLY GLY B . n 
B 2 390 ARG 390 390 390 ARG ARG B . n 
B 2 391 VAL 391 391 391 VAL VAL B . n 
B 2 392 TRP 392 392 392 TRP TRP B . n 
B 2 393 ALA 393 393 393 ALA ALA B . n 
B 2 394 THR 394 394 394 THR THR B . n 
B 2 395 HIS 395 395 395 HIS HIS B . n 
B 2 396 ALA 396 396 396 ALA ALA B . n 
B 2 397 LEU 397 397 397 LEU LEU B . n 
B 2 398 SER 398 398 398 SER SER B . n 
B 2 399 GLN 399 399 399 GLN GLN B . n 
B 2 400 ALA 400 400 400 ALA ALA B . n 
B 2 401 ILE 401 401 401 ILE ILE B . n 
B 2 402 PRO 402 402 402 PRO PRO B . n 
B 2 403 GLU 403 403 403 GLU GLU B . n 
B 2 404 ALA 404 404 404 ALA ALA B . n 
B 2 405 GLU 405 405 405 GLU GLU B . n 
B 2 406 ILE 406 406 406 ILE ILE B . n 
B 2 407 TYR 407 407 407 TYR TYR B . n 
B 2 408 ALA 408 408 408 ALA ALA B . n 
B 2 409 GLY 409 409 409 GLY GLY B . n 
B 2 410 THR 410 410 410 THR THR B . n 
B 2 411 ALA 411 411 411 ALA ALA B . n 
B 2 412 ALA 412 412 412 ALA ALA B . n 
B 2 413 GLY 413 413 413 GLY GLY B . n 
B 2 414 MET 414 414 414 MET MET B . n 
B 2 415 LEU 415 415 415 LEU LEU B . n 
B 2 416 ALA 416 416 416 ALA ALA B . n 
B 2 417 ILE 417 417 417 ILE ILE B . n 
B 2 418 PRO 418 418 418 PRO PRO B . n 
B 2 419 LEU 419 419 419 LEU LEU B . n 
B 2 420 SER 420 420 420 SER SER B . n 
B 2 421 GLN 421 421 421 GLN GLN B . n 
B 2 422 VAL 422 422 422 VAL VAL B . n 
B 2 423 LYS 423 423 423 LYS LYS B . n 
B 2 424 SER 424 424 424 SER SER B . n 
B 2 425 ASP 425 425 425 ASP ASP B . n 
B 2 426 TYR 426 426 426 TYR TYR B . n 
B 2 427 LEU 427 427 427 LEU LEU B . n 
B 2 428 LEU 428 428 428 LEU LEU B . n 
B 2 429 PHE 429 429 429 PHE PHE B . n 
B 2 430 PHE 430 430 430 PHE PHE B . n 
B 2 431 ARG 431 431 431 ARG ARG B . n 
B 2 432 MLZ 432 432 432 MLZ MLZ B . n 
B 2 433 GLU 433 433 433 GLU GLU B . n 
B 2 434 ILE 434 434 434 ILE ILE B . n 
B 2 435 VAL 435 435 435 VAL VAL B . n 
B 2 436 GLN 436 436 436 GLN GLN B . n 
B 2 437 ASN 437 437 437 ASN ASN B . n 
B 2 438 LEU 438 438 438 LEU LEU B . n 
B 2 439 ASN 439 439 439 ASN ASN B . n 
B 2 440 TRP 440 440 440 TRP TRP B . n 
B 2 441 ALA 441 441 441 ALA ALA B . n 
B 2 442 GLY 442 442 442 GLY GLY B . n 
B 2 443 ASN 443 443 443 ASN ASN B . n 
B 2 444 PRO 444 444 444 PRO PRO B . n 
B 2 445 GLU 445 445 445 GLU GLU B . n 
B 2 446 MLZ 446 446 446 MLZ MLZ B . n 
B 2 447 SER 447 447 447 SER SER B . n 
B 2 448 TYR 448 448 448 TYR TYR B . n 
B 2 449 GLU 449 449 449 GLU GLU B . n 
B 2 450 THR 450 450 450 THR THR B . n 
B 2 451 GLY 451 451 451 GLY GLY B . n 
B 2 452 PRO 452 452 452 PRO PRO B . n 
B 2 453 MET 453 453 453 MET MET B . n 
B 2 454 GLY 454 454 454 GLY GLY B . n 
B 2 455 ASP 455 455 455 ASP ASP B . n 
B 2 456 ARG 456 456 456 ARG ARG B . n 
B 2 457 LEU 457 457 457 LEU LEU B . n 
B 2 458 THR 458 458 458 THR THR B . n 
B 2 459 PRO 459 459 459 PRO PRO B . n 
B 2 460 ARG 460 460 460 ARG ARG B . n 
B 2 461 LYS 461 461 461 LYS LYS B . n 
B 2 462 SER 462 462 462 SER SER B . n 
B 2 463 PHE 463 463 463 PHE PHE B . n 
B 2 464 ALA 464 464 464 ALA ALA B . n 
B 2 465 ILE 465 465 465 ILE ILE B . n 
B 2 466 TRP 466 466 466 TRP TRP B . n 
B 2 467 MLZ 467 467 467 MLZ MLZ B . n 
B 2 468 GLU 468 468 468 GLU GLU B . n 
B 2 469 THR 469 469 469 THR THR B . n 
B 2 470 VAL 470 470 470 VAL VAL B . n 
B 2 471 ARG 471 471 471 ARG ARG B . n 
B 2 472 LEU 472 472 472 LEU LEU B . n 
B 2 473 GLN 473 473 473 GLN GLN B . n 
B 2 474 ALA 474 474 474 ALA ALA B . n 
B 2 475 GLN 475 475 475 GLN GLN B . n 
B 2 476 PRO 476 476 476 PRO PRO B . n 
B 2 477 TRP 477 477 477 TRP TRP B . n 
B 2 478 SER 478 478 478 SER SER B . n 
B 2 479 GLU 479 479 479 GLU GLU B . n 
B 2 480 ALA 480 480 480 ALA ALA B . n 
B 2 481 ASP 481 481 481 ASP ASP B . n 
B 2 482 ARG 482 482 482 ARG ARG B . n 
B 2 483 GLU 483 483 483 GLU GLU B . n 
B 2 484 ILE 484 484 484 ILE ILE B . n 
B 2 485 ALA 485 485 485 ALA ALA B . n 
B 2 486 GLU 486 486 486 GLU GLU B . n 
B 2 487 ALA 487 487 487 ALA ALA B . n 
B 2 488 ALA 488 488 488 ALA ALA B . n 
B 2 489 ARG 489 489 489 ARG ARG B . n 
B 2 490 ILE 490 490 490 ILE ILE B . n 
B 2 491 ALA 491 491 491 ALA ALA B . n 
B 2 492 LEU 492 492 492 LEU LEU B . n 
B 2 493 VAL 493 493 493 VAL VAL B . n 
B 2 494 GLU 494 494 494 GLU GLU B . n 
B 2 495 VAL 495 495 495 VAL VAL B . n 
B 2 496 ALA 496 496 496 ALA ALA B . n 
B 2 497 PHE 497 497 497 PHE PHE B . n 
B 2 498 HIS 498 498 498 HIS HIS B . n 
B 2 499 HIS 499 499 499 HIS HIS B . n 
B 2 500 SER 500 500 500 SER SER B . n 
B 2 501 GLU 501 501 501 GLU GLU B . n 
B 2 502 HIS 502 502 502 HIS HIS B . n 
B 2 503 HIS 503 503 503 HIS HIS B . n 
B 2 504 HIS 504 504 ?   ?   ?   B . n 
B 2 505 HIS 505 505 ?   ?   ?   B . n 
B 2 506 HIS 506 506 ?   ?   ?   B . n 
B 2 507 HIS 507 507 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        EL5 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   EL5 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 PEG 1   601  1   PEG PEG A . 
D 4 MPD 1   602  2   MPD MPD A . 
E 5 EL5 1   603  1   EL5 EL5 A . 
F 6 CL  1   604  1   CL  CL  A . 
G 6 CL  1   605  2   CL  CL  A . 
H 3 PEG 1   601  2   PEG PEG B . 
I 4 MPD 1   602  1   MPD MPD B . 
J 5 EL5 1   603  2   EL5 EL5 B . 
K 7 HOH 1   701  429 HOH HOH A . 
K 7 HOH 2   702  113 HOH HOH A . 
K 7 HOH 3   703  634 HOH HOH A . 
K 7 HOH 4   704  630 HOH HOH A . 
K 7 HOH 5   705  64  HOH HOH A . 
K 7 HOH 6   706  445 HOH HOH A . 
K 7 HOH 7   707  628 HOH HOH A . 
K 7 HOH 8   708  133 HOH HOH A . 
K 7 HOH 9   709  221 HOH HOH A . 
K 7 HOH 10  710  563 HOH HOH A . 
K 7 HOH 11  711  337 HOH HOH A . 
K 7 HOH 12  712  17  HOH HOH A . 
K 7 HOH 13  713  564 HOH HOH A . 
K 7 HOH 14  714  667 HOH HOH A . 
K 7 HOH 15  715  470 HOH HOH A . 
K 7 HOH 16  716  193 HOH HOH A . 
K 7 HOH 17  717  205 HOH HOH A . 
K 7 HOH 18  718  263 HOH HOH A . 
K 7 HOH 19  719  371 HOH HOH A . 
K 7 HOH 20  720  474 HOH HOH A . 
K 7 HOH 21  721  89  HOH HOH A . 
K 7 HOH 22  722  633 HOH HOH A . 
K 7 HOH 23  723  111 HOH HOH A . 
K 7 HOH 24  724  420 HOH HOH A . 
K 7 HOH 25  725  562 HOH HOH A . 
K 7 HOH 26  726  668 HOH HOH A . 
K 7 HOH 27  727  251 HOH HOH A . 
K 7 HOH 28  728  243 HOH HOH A . 
K 7 HOH 29  729  80  HOH HOH A . 
K 7 HOH 30  730  417 HOH HOH A . 
K 7 HOH 31  731  561 HOH HOH A . 
K 7 HOH 32  732  281 HOH HOH A . 
K 7 HOH 33  733  573 HOH HOH A . 
K 7 HOH 34  734  143 HOH HOH A . 
K 7 HOH 35  735  538 HOH HOH A . 
K 7 HOH 36  736  493 HOH HOH A . 
K 7 HOH 37  737  367 HOH HOH A . 
K 7 HOH 38  738  433 HOH HOH A . 
K 7 HOH 39  739  126 HOH HOH A . 
K 7 HOH 40  740  87  HOH HOH A . 
K 7 HOH 41  741  535 HOH HOH A . 
K 7 HOH 42  742  92  HOH HOH A . 
K 7 HOH 43  743  364 HOH HOH A . 
K 7 HOH 44  744  62  HOH HOH A . 
K 7 HOH 45  745  232 HOH HOH A . 
K 7 HOH 46  746  165 HOH HOH A . 
K 7 HOH 47  747  169 HOH HOH A . 
K 7 HOH 48  748  86  HOH HOH A . 
K 7 HOH 49  749  24  HOH HOH A . 
K 7 HOH 50  750  543 HOH HOH A . 
K 7 HOH 51  751  450 HOH HOH A . 
K 7 HOH 52  752  128 HOH HOH A . 
K 7 HOH 53  753  395 HOH HOH A . 
K 7 HOH 54  754  402 HOH HOH A . 
K 7 HOH 55  755  140 HOH HOH A . 
K 7 HOH 56  756  78  HOH HOH A . 
K 7 HOH 57  757  518 HOH HOH A . 
K 7 HOH 58  758  360 HOH HOH A . 
K 7 HOH 59  759  639 HOH HOH A . 
K 7 HOH 60  760  646 HOH HOH A . 
K 7 HOH 61  761  206 HOH HOH A . 
K 7 HOH 62  762  362 HOH HOH A . 
K 7 HOH 63  763  175 HOH HOH A . 
K 7 HOH 64  764  129 HOH HOH A . 
K 7 HOH 65  765  106 HOH HOH A . 
K 7 HOH 66  766  73  HOH HOH A . 
K 7 HOH 67  767  67  HOH HOH A . 
K 7 HOH 68  768  16  HOH HOH A . 
K 7 HOH 69  769  153 HOH HOH A . 
K 7 HOH 70  770  409 HOH HOH A . 
K 7 HOH 71  771  75  HOH HOH A . 
K 7 HOH 72  772  419 HOH HOH A . 
K 7 HOH 73  773  652 HOH HOH A . 
K 7 HOH 74  774  552 HOH HOH A . 
K 7 HOH 75  775  556 HOH HOH A . 
K 7 HOH 76  776  41  HOH HOH A . 
K 7 HOH 77  777  261 HOH HOH A . 
K 7 HOH 78  778  42  HOH HOH A . 
K 7 HOH 79  779  259 HOH HOH A . 
K 7 HOH 80  780  77  HOH HOH A . 
K 7 HOH 81  781  224 HOH HOH A . 
K 7 HOH 82  782  110 HOH HOH A . 
K 7 HOH 83  783  309 HOH HOH A . 
K 7 HOH 84  784  209 HOH HOH A . 
K 7 HOH 85  785  331 HOH HOH A . 
K 7 HOH 86  786  404 HOH HOH A . 
K 7 HOH 87  787  365 HOH HOH A . 
K 7 HOH 88  788  123 HOH HOH A . 
K 7 HOH 89  789  624 HOH HOH A . 
K 7 HOH 90  790  455 HOH HOH A . 
K 7 HOH 91  791  26  HOH HOH A . 
K 7 HOH 92  792  610 HOH HOH A . 
K 7 HOH 93  793  303 HOH HOH A . 
K 7 HOH 94  794  50  HOH HOH A . 
K 7 HOH 95  795  167 HOH HOH A . 
K 7 HOH 96  796  135 HOH HOH A . 
K 7 HOH 97  797  523 HOH HOH A . 
K 7 HOH 98  798  172 HOH HOH A . 
K 7 HOH 99  799  502 HOH HOH A . 
K 7 HOH 100 800  250 HOH HOH A . 
K 7 HOH 101 801  344 HOH HOH A . 
K 7 HOH 102 802  254 HOH HOH A . 
K 7 HOH 103 803  467 HOH HOH A . 
K 7 HOH 104 804  233 HOH HOH A . 
K 7 HOH 105 805  457 HOH HOH A . 
K 7 HOH 106 806  625 HOH HOH A . 
K 7 HOH 107 807  622 HOH HOH A . 
K 7 HOH 108 808  516 HOH HOH A . 
K 7 HOH 109 809  352 HOH HOH A . 
K 7 HOH 110 810  617 HOH HOH A . 
K 7 HOH 111 811  23  HOH HOH A . 
K 7 HOH 112 812  57  HOH HOH A . 
K 7 HOH 113 813  376 HOH HOH A . 
K 7 HOH 114 814  640 HOH HOH A . 
K 7 HOH 115 815  84  HOH HOH A . 
K 7 HOH 116 816  533 HOH HOH A . 
K 7 HOH 117 817  584 HOH HOH A . 
K 7 HOH 118 818  494 HOH HOH A . 
K 7 HOH 119 819  393 HOH HOH A . 
K 7 HOH 120 820  320 HOH HOH A . 
K 7 HOH 121 821  12  HOH HOH A . 
K 7 HOH 122 822  40  HOH HOH A . 
K 7 HOH 123 823  36  HOH HOH A . 
K 7 HOH 124 824  439 HOH HOH A . 
K 7 HOH 125 825  496 HOH HOH A . 
K 7 HOH 126 826  327 HOH HOH A . 
K 7 HOH 127 827  299 HOH HOH A . 
K 7 HOH 128 828  63  HOH HOH A . 
K 7 HOH 129 829  517 HOH HOH A . 
K 7 HOH 130 830  341 HOH HOH A . 
K 7 HOH 131 831  323 HOH HOH A . 
K 7 HOH 132 832  480 HOH HOH A . 
K 7 HOH 133 833  32  HOH HOH A . 
K 7 HOH 134 834  313 HOH HOH A . 
K 7 HOH 135 835  211 HOH HOH A . 
K 7 HOH 136 836  377 HOH HOH A . 
K 7 HOH 137 837  347 HOH HOH A . 
K 7 HOH 138 838  507 HOH HOH A . 
K 7 HOH 139 839  180 HOH HOH A . 
K 7 HOH 140 840  9   HOH HOH A . 
K 7 HOH 141 841  293 HOH HOH A . 
K 7 HOH 142 842  431 HOH HOH A . 
K 7 HOH 143 843  25  HOH HOH A . 
K 7 HOH 144 844  48  HOH HOH A . 
K 7 HOH 145 845  104 HOH HOH A . 
K 7 HOH 146 846  183 HOH HOH A . 
K 7 HOH 147 847  626 HOH HOH A . 
K 7 HOH 148 848  407 HOH HOH A . 
K 7 HOH 149 849  295 HOH HOH A . 
K 7 HOH 150 850  623 HOH HOH A . 
K 7 HOH 151 851  406 HOH HOH A . 
K 7 HOH 152 852  621 HOH HOH A . 
K 7 HOH 153 853  315 HOH HOH A . 
K 7 HOH 154 854  145 HOH HOH A . 
K 7 HOH 155 855  619 HOH HOH A . 
K 7 HOH 156 856  157 HOH HOH A . 
K 7 HOH 157 857  33  HOH HOH A . 
K 7 HOH 158 858  659 HOH HOH A . 
K 7 HOH 159 859  503 HOH HOH A . 
K 7 HOH 160 860  151 HOH HOH A . 
K 7 HOH 161 861  156 HOH HOH A . 
K 7 HOH 162 862  545 HOH HOH A . 
K 7 HOH 163 863  28  HOH HOH A . 
K 7 HOH 164 864  399 HOH HOH A . 
K 7 HOH 165 865  421 HOH HOH A . 
K 7 HOH 166 866  119 HOH HOH A . 
K 7 HOH 167 867  666 HOH HOH A . 
K 7 HOH 168 868  638 HOH HOH A . 
K 7 HOH 169 869  235 HOH HOH A . 
K 7 HOH 170 870  368 HOH HOH A . 
K 7 HOH 171 871  569 HOH HOH A . 
K 7 HOH 172 872  582 HOH HOH A . 
K 7 HOH 173 873  382 HOH HOH A . 
K 7 HOH 174 874  4   HOH HOH A . 
K 7 HOH 175 875  553 HOH HOH A . 
K 7 HOH 176 876  632 HOH HOH A . 
K 7 HOH 177 877  271 HOH HOH A . 
K 7 HOH 178 878  307 HOH HOH A . 
K 7 HOH 179 879  585 HOH HOH A . 
K 7 HOH 180 880  560 HOH HOH A . 
K 7 HOH 181 881  186 HOH HOH A . 
K 7 HOH 182 882  346 HOH HOH A . 
K 7 HOH 183 883  357 HOH HOH A . 
K 7 HOH 184 884  226 HOH HOH A . 
K 7 HOH 185 885  161 HOH HOH A . 
K 7 HOH 186 886  380 HOH HOH A . 
K 7 HOH 187 887  285 HOH HOH A . 
K 7 HOH 188 888  311 HOH HOH A . 
K 7 HOH 189 889  176 HOH HOH A . 
K 7 HOH 190 890  288 HOH HOH A . 
K 7 HOH 191 891  218 HOH HOH A . 
K 7 HOH 192 892  171 HOH HOH A . 
K 7 HOH 193 893  2   HOH HOH A . 
K 7 HOH 194 894  434 HOH HOH A . 
K 7 HOH 195 895  13  HOH HOH A . 
K 7 HOH 196 896  149 HOH HOH A . 
K 7 HOH 197 897  214 HOH HOH A . 
K 7 HOH 198 898  324 HOH HOH A . 
K 7 HOH 199 899  170 HOH HOH A . 
K 7 HOH 200 900  70  HOH HOH A . 
K 7 HOH 201 901  60  HOH HOH A . 
K 7 HOH 202 902  59  HOH HOH A . 
K 7 HOH 203 903  301 HOH HOH A . 
K 7 HOH 204 904  136 HOH HOH A . 
K 7 HOH 205 905  177 HOH HOH A . 
K 7 HOH 206 906  168 HOH HOH A . 
K 7 HOH 207 907  207 HOH HOH A . 
K 7 HOH 208 908  482 HOH HOH A . 
K 7 HOH 209 909  686 HOH HOH A . 
K 7 HOH 210 910  322 HOH HOH A . 
K 7 HOH 211 911  120 HOH HOH A . 
K 7 HOH 212 912  270 HOH HOH A . 
K 7 HOH 213 913  29  HOH HOH A . 
K 7 HOH 214 914  488 HOH HOH A . 
K 7 HOH 215 915  577 HOH HOH A . 
K 7 HOH 216 916  229 HOH HOH A . 
K 7 HOH 217 917  479 HOH HOH A . 
K 7 HOH 218 918  432 HOH HOH A . 
K 7 HOH 219 919  66  HOH HOH A . 
K 7 HOH 220 920  310 HOH HOH A . 
K 7 HOH 221 921  31  HOH HOH A . 
K 7 HOH 222 922  292 HOH HOH A . 
K 7 HOH 223 923  300 HOH HOH A . 
K 7 HOH 224 924  384 HOH HOH A . 
K 7 HOH 225 925  164 HOH HOH A . 
K 7 HOH 226 926  52  HOH HOH A . 
K 7 HOH 227 927  274 HOH HOH A . 
K 7 HOH 228 928  426 HOH HOH A . 
K 7 HOH 229 929  228 HOH HOH A . 
K 7 HOH 230 930  98  HOH HOH A . 
K 7 HOH 231 931  314 HOH HOH A . 
K 7 HOH 232 932  527 HOH HOH A . 
K 7 HOH 233 933  629 HOH HOH A . 
K 7 HOH 234 934  81  HOH HOH A . 
K 7 HOH 235 935  663 HOH HOH A . 
K 7 HOH 236 936  103 HOH HOH A . 
K 7 HOH 237 937  287 HOH HOH A . 
K 7 HOH 238 938  91  HOH HOH A . 
K 7 HOH 239 939  276 HOH HOH A . 
K 7 HOH 240 940  526 HOH HOH A . 
K 7 HOH 241 941  267 HOH HOH A . 
K 7 HOH 242 942  449 HOH HOH A . 
K 7 HOH 243 943  20  HOH HOH A . 
K 7 HOH 244 944  159 HOH HOH A . 
K 7 HOH 245 945  30  HOH HOH A . 
K 7 HOH 246 946  101 HOH HOH A . 
K 7 HOH 247 947  546 HOH HOH A . 
K 7 HOH 248 948  100 HOH HOH A . 
K 7 HOH 249 949  294 HOH HOH A . 
K 7 HOH 250 950  505 HOH HOH A . 
K 7 HOH 251 951  8   HOH HOH A . 
K 7 HOH 252 952  264 HOH HOH A . 
K 7 HOH 253 953  532 HOH HOH A . 
K 7 HOH 254 954  155 HOH HOH A . 
K 7 HOH 255 955  279 HOH HOH A . 
K 7 HOH 256 956  154 HOH HOH A . 
K 7 HOH 257 957  69  HOH HOH A . 
K 7 HOH 258 958  391 HOH HOH A . 
K 7 HOH 259 959  466 HOH HOH A . 
K 7 HOH 260 960  83  HOH HOH A . 
K 7 HOH 261 961  343 HOH HOH A . 
K 7 HOH 262 962  355 HOH HOH A . 
K 7 HOH 263 963  166 HOH HOH A . 
K 7 HOH 264 964  195 HOH HOH A . 
K 7 HOH 265 965  372 HOH HOH A . 
K 7 HOH 266 966  146 HOH HOH A . 
K 7 HOH 267 967  210 HOH HOH A . 
K 7 HOH 268 968  418 HOH HOH A . 
K 7 HOH 269 969  216 HOH HOH A . 
K 7 HOH 270 970  443 HOH HOH A . 
K 7 HOH 271 971  5   HOH HOH A . 
K 7 HOH 272 972  258 HOH HOH A . 
K 7 HOH 273 973  676 HOH HOH A . 
K 7 HOH 274 974  385 HOH HOH A . 
K 7 HOH 275 975  196 HOH HOH A . 
K 7 HOH 276 976  328 HOH HOH A . 
K 7 HOH 277 977  415 HOH HOH A . 
K 7 HOH 278 978  272 HOH HOH A . 
K 7 HOH 279 979  158 HOH HOH A . 
K 7 HOH 280 980  97  HOH HOH A . 
K 7 HOH 281 981  34  HOH HOH A . 
K 7 HOH 282 982  227 HOH HOH A . 
K 7 HOH 283 983  241 HOH HOH A . 
K 7 HOH 284 984  117 HOH HOH A . 
K 7 HOH 285 985  390 HOH HOH A . 
K 7 HOH 286 986  49  HOH HOH A . 
K 7 HOH 287 987  192 HOH HOH A . 
K 7 HOH 288 988  465 HOH HOH A . 
K 7 HOH 289 989  319 HOH HOH A . 
K 7 HOH 290 990  312 HOH HOH A . 
K 7 HOH 291 991  685 HOH HOH A . 
K 7 HOH 292 992  43  HOH HOH A . 
K 7 HOH 293 993  604 HOH HOH A . 
K 7 HOH 294 994  491 HOH HOH A . 
K 7 HOH 295 995  289 HOH HOH A . 
K 7 HOH 296 996  416 HOH HOH A . 
K 7 HOH 297 997  306 HOH HOH A . 
K 7 HOH 298 998  278 HOH HOH A . 
K 7 HOH 299 999  283 HOH HOH A . 
K 7 HOH 300 1000 410 HOH HOH A . 
K 7 HOH 301 1001 664 HOH HOH A . 
K 7 HOH 302 1002 388 HOH HOH A . 
K 7 HOH 303 1003 422 HOH HOH A . 
K 7 HOH 304 1004 540 HOH HOH A . 
K 7 HOH 305 1005 558 HOH HOH A . 
K 7 HOH 306 1006 208 HOH HOH A . 
K 7 HOH 307 1007 424 HOH HOH A . 
K 7 HOH 308 1008 148 HOH HOH A . 
K 7 HOH 309 1009 222 HOH HOH A . 
K 7 HOH 310 1010 684 HOH HOH A . 
K 7 HOH 311 1011 675 HOH HOH A . 
K 7 HOH 312 1012 220 HOH HOH A . 
K 7 HOH 313 1013 256 HOH HOH A . 
K 7 HOH 314 1014 387 HOH HOH A . 
K 7 HOH 315 1015 202 HOH HOH A . 
K 7 HOH 316 1016 592 HOH HOH A . 
K 7 HOH 317 1017 594 HOH HOH A . 
K 7 HOH 318 1018 591 HOH HOH A . 
K 7 HOH 319 1019 541 HOH HOH A . 
K 7 HOH 320 1020 567 HOH HOH A . 
K 7 HOH 321 1021 392 HOH HOH A . 
K 7 HOH 322 1022 485 HOH HOH A . 
K 7 HOH 323 1023 333 HOH HOH A . 
K 7 HOH 324 1024 242 HOH HOH A . 
K 7 HOH 325 1025 672 HOH HOH A . 
K 7 HOH 326 1026 650 HOH HOH A . 
K 7 HOH 327 1027 598 HOH HOH A . 
K 7 HOH 328 1028 597 HOH HOH A . 
K 7 HOH 329 1029 644 HOH HOH A . 
K 7 HOH 330 1030 132 HOH HOH A . 
K 7 HOH 331 1031 551 HOH HOH A . 
K 7 HOH 332 1032 468 HOH HOH A . 
K 7 HOH 333 1033 539 HOH HOH A . 
K 7 HOH 334 1034 477 HOH HOH A . 
K 7 HOH 335 1035 602 HOH HOH A . 
K 7 HOH 336 1036 534 HOH HOH A . 
K 7 HOH 337 1037 603 HOH HOH A . 
K 7 HOH 338 1038 595 HOH HOH A . 
K 7 HOH 339 1039 442 HOH HOH A . 
K 7 HOH 340 1040 606 HOH HOH A . 
L 7 HOH 1   701  464 HOH HOH B . 
L 7 HOH 2   702  437 HOH HOH B . 
L 7 HOH 3   703  452 HOH HOH B . 
L 7 HOH 4   704  655 HOH HOH B . 
L 7 HOH 5   705  189 HOH HOH B . 
L 7 HOH 6   706  184 HOH HOH B . 
L 7 HOH 7   707  349 HOH HOH B . 
L 7 HOH 8   708  497 HOH HOH B . 
L 7 HOH 9   709  683 HOH HOH B . 
L 7 HOH 10  710  54  HOH HOH B . 
L 7 HOH 11  711  469 HOH HOH B . 
L 7 HOH 12  712  401 HOH HOH B . 
L 7 HOH 13  713  174 HOH HOH B . 
L 7 HOH 14  714  447 HOH HOH B . 
L 7 HOH 15  715  163 HOH HOH B . 
L 7 HOH 16  716  76  HOH HOH B . 
L 7 HOH 17  717  656 HOH HOH B . 
L 7 HOH 18  718  332 HOH HOH B . 
L 7 HOH 19  719  141 HOH HOH B . 
L 7 HOH 20  720  109 HOH HOH B . 
L 7 HOH 21  721  212 HOH HOH B . 
L 7 HOH 22  722  411 HOH HOH B . 
L 7 HOH 23  723  512 HOH HOH B . 
L 7 HOH 24  724  653 HOH HOH B . 
L 7 HOH 25  725  247 HOH HOH B . 
L 7 HOH 26  726  651 HOH HOH B . 
L 7 HOH 27  727  499 HOH HOH B . 
L 7 HOH 28  728  203 HOH HOH B . 
L 7 HOH 29  729  74  HOH HOH B . 
L 7 HOH 30  730  305 HOH HOH B . 
L 7 HOH 31  731  231 HOH HOH B . 
L 7 HOH 32  732  484 HOH HOH B . 
L 7 HOH 33  733  611 HOH HOH B . 
L 7 HOH 34  734  124 HOH HOH B . 
L 7 HOH 35  735  182 HOH HOH B . 
L 7 HOH 36  736  618 HOH HOH B . 
L 7 HOH 37  737  255 HOH HOH B . 
L 7 HOH 38  738  147 HOH HOH B . 
L 7 HOH 39  739  22  HOH HOH B . 
L 7 HOH 40  740  587 HOH HOH B . 
L 7 HOH 41  741  345 HOH HOH B . 
L 7 HOH 42  742  657 HOH HOH B . 
L 7 HOH 43  743  461 HOH HOH B . 
L 7 HOH 44  744  627 HOH HOH B . 
L 7 HOH 45  745  219 HOH HOH B . 
L 7 HOH 46  746  152 HOH HOH B . 
L 7 HOH 47  747  58  HOH HOH B . 
L 7 HOH 48  748  173 HOH HOH B . 
L 7 HOH 49  749  39  HOH HOH B . 
L 7 HOH 50  750  139 HOH HOH B . 
L 7 HOH 51  751  275 HOH HOH B . 
L 7 HOH 52  752  350 HOH HOH B . 
L 7 HOH 53  753  519 HOH HOH B . 
L 7 HOH 54  754  51  HOH HOH B . 
L 7 HOH 55  755  284 HOH HOH B . 
L 7 HOH 56  756  197 HOH HOH B . 
L 7 HOH 57  757  370 HOH HOH B . 
L 7 HOH 58  758  291 HOH HOH B . 
L 7 HOH 59  759  93  HOH HOH B . 
L 7 HOH 60  760  200 HOH HOH B . 
L 7 HOH 61  761  179 HOH HOH B . 
L 7 HOH 62  762  105 HOH HOH B . 
L 7 HOH 63  763  150 HOH HOH B . 
L 7 HOH 64  764  273 HOH HOH B . 
L 7 HOH 65  765  215 HOH HOH B . 
L 7 HOH 66  766  121 HOH HOH B . 
L 7 HOH 67  767  82  HOH HOH B . 
L 7 HOH 68  768  342 HOH HOH B . 
L 7 HOH 69  769  373 HOH HOH B . 
L 7 HOH 70  770  96  HOH HOH B . 
L 7 HOH 71  771  162 HOH HOH B . 
L 7 HOH 72  772  579 HOH HOH B . 
L 7 HOH 73  773  21  HOH HOH B . 
L 7 HOH 74  774  194 HOH HOH B . 
L 7 HOH 75  775  536 HOH HOH B . 
L 7 HOH 76  776  204 HOH HOH B . 
L 7 HOH 77  777  498 HOH HOH B . 
L 7 HOH 78  778  620 HOH HOH B . 
L 7 HOH 79  779  260 HOH HOH B . 
L 7 HOH 80  780  423 HOH HOH B . 
L 7 HOH 81  781  230 HOH HOH B . 
L 7 HOH 82  782  649 HOH HOH B . 
L 7 HOH 83  783  115 HOH HOH B . 
L 7 HOH 84  784  356 HOH HOH B . 
L 7 HOH 85  785  616 HOH HOH B . 
L 7 HOH 86  786  108 HOH HOH B . 
L 7 HOH 87  787  462 HOH HOH B . 
L 7 HOH 88  788  6   HOH HOH B . 
L 7 HOH 89  789  321 HOH HOH B . 
L 7 HOH 90  790  3   HOH HOH B . 
L 7 HOH 91  791  10  HOH HOH B . 
L 7 HOH 92  792  400 HOH HOH B . 
L 7 HOH 93  793  265 HOH HOH B . 
L 7 HOH 94  794  318 HOH HOH B . 
L 7 HOH 95  795  631 HOH HOH B . 
L 7 HOH 96  796  662 HOH HOH B . 
L 7 HOH 97  797  72  HOH HOH B . 
L 7 HOH 98  798  239 HOH HOH B . 
L 7 HOH 99  799  223 HOH HOH B . 
L 7 HOH 100 800  369 HOH HOH B . 
L 7 HOH 101 801  79  HOH HOH B . 
L 7 HOH 102 802  454 HOH HOH B . 
L 7 HOH 103 803  280 HOH HOH B . 
L 7 HOH 104 804  190 HOH HOH B . 
L 7 HOH 105 805  453 HOH HOH B . 
L 7 HOH 106 806  521 HOH HOH B . 
L 7 HOH 107 807  234 HOH HOH B . 
L 7 HOH 108 808  531 HOH HOH B . 
L 7 HOH 109 809  252 HOH HOH B . 
L 7 HOH 110 810  673 HOH HOH B . 
L 7 HOH 111 811  7   HOH HOH B . 
L 7 HOH 112 812  253 HOH HOH B . 
L 7 HOH 113 813  282 HOH HOH B . 
L 7 HOH 114 814  381 HOH HOH B . 
L 7 HOH 115 815  500 HOH HOH B . 
L 7 HOH 116 816  88  HOH HOH B . 
L 7 HOH 117 817  35  HOH HOH B . 
L 7 HOH 118 818  187 HOH HOH B . 
L 7 HOH 119 819  269 HOH HOH B . 
L 7 HOH 120 820  18  HOH HOH B . 
L 7 HOH 121 821  191 HOH HOH B . 
L 7 HOH 122 822  446 HOH HOH B . 
L 7 HOH 123 823  213 HOH HOH B . 
L 7 HOH 124 824  678 HOH HOH B . 
L 7 HOH 125 825  386 HOH HOH B . 
L 7 HOH 126 826  529 HOH HOH B . 
L 7 HOH 127 827  688 HOH HOH B . 
L 7 HOH 128 828  131 HOH HOH B . 
L 7 HOH 129 829  405 HOH HOH B . 
L 7 HOH 130 830  27  HOH HOH B . 
L 7 HOH 131 831  334 HOH HOH B . 
L 7 HOH 132 832  185 HOH HOH B . 
L 7 HOH 133 833  398 HOH HOH B . 
L 7 HOH 134 834  658 HOH HOH B . 
L 7 HOH 135 835  238 HOH HOH B . 
L 7 HOH 136 836  68  HOH HOH B . 
L 7 HOH 137 837  335 HOH HOH B . 
L 7 HOH 138 838  127 HOH HOH B . 
L 7 HOH 139 839  14  HOH HOH B . 
L 7 HOH 140 840  339 HOH HOH B . 
L 7 HOH 141 841  248 HOH HOH B . 
L 7 HOH 142 842  122 HOH HOH B . 
L 7 HOH 143 843  297 HOH HOH B . 
L 7 HOH 144 844  102 HOH HOH B . 
L 7 HOH 145 845  456 HOH HOH B . 
L 7 HOH 146 846  375 HOH HOH B . 
L 7 HOH 147 847  478 HOH HOH B . 
L 7 HOH 148 848  679 HOH HOH B . 
L 7 HOH 149 849  237 HOH HOH B . 
L 7 HOH 150 850  427 HOH HOH B . 
L 7 HOH 151 851  201 HOH HOH B . 
L 7 HOH 152 852  53  HOH HOH B . 
L 7 HOH 153 853  549 HOH HOH B . 
L 7 HOH 154 854  537 HOH HOH B . 
L 7 HOH 155 855  286 HOH HOH B . 
L 7 HOH 156 856  137 HOH HOH B . 
L 7 HOH 157 857  528 HOH HOH B . 
L 7 HOH 158 858  142 HOH HOH B . 
L 7 HOH 159 859  530 HOH HOH B . 
L 7 HOH 160 860  635 HOH HOH B . 
L 7 HOH 161 861  225 HOH HOH B . 
L 7 HOH 162 862  336 HOH HOH B . 
L 7 HOH 163 863  61  HOH HOH B . 
L 7 HOH 164 864  329 HOH HOH B . 
L 7 HOH 165 865  403 HOH HOH B . 
L 7 HOH 166 866  199 HOH HOH B . 
L 7 HOH 167 867  669 HOH HOH B . 
L 7 HOH 168 868  65  HOH HOH B . 
L 7 HOH 169 869  116 HOH HOH B . 
L 7 HOH 170 870  257 HOH HOH B . 
L 7 HOH 171 871  397 HOH HOH B . 
L 7 HOH 172 872  249 HOH HOH B . 
L 7 HOH 173 873  586 HOH HOH B . 
L 7 HOH 174 874  38  HOH HOH B . 
L 7 HOH 175 875  348 HOH HOH B . 
L 7 HOH 176 876  637 HOH HOH B . 
L 7 HOH 177 877  240 HOH HOH B . 
L 7 HOH 178 878  130 HOH HOH B . 
L 7 HOH 179 879  94  HOH HOH B . 
L 7 HOH 180 880  44  HOH HOH B . 
L 7 HOH 181 881  198 HOH HOH B . 
L 7 HOH 182 882  112 HOH HOH B . 
L 7 HOH 183 883  389 HOH HOH B . 
L 7 HOH 184 884  277 HOH HOH B . 
L 7 HOH 185 885  473 HOH HOH B . 
L 7 HOH 186 886  550 HOH HOH B . 
L 7 HOH 187 887  428 HOH HOH B . 
L 7 HOH 188 888  654 HOH HOH B . 
L 7 HOH 189 889  118 HOH HOH B . 
L 7 HOH 190 890  459 HOH HOH B . 
L 7 HOH 191 891  296 HOH HOH B . 
L 7 HOH 192 892  460 HOH HOH B . 
L 7 HOH 193 893  441 HOH HOH B . 
L 7 HOH 194 894  394 HOH HOH B . 
L 7 HOH 195 895  682 HOH HOH B . 
L 7 HOH 196 896  489 HOH HOH B . 
L 7 HOH 197 897  125 HOH HOH B . 
L 7 HOH 198 898  160 HOH HOH B . 
L 7 HOH 199 899  566 HOH HOH B . 
L 7 HOH 200 900  374 HOH HOH B . 
L 7 HOH 201 901  472 HOH HOH B . 
L 7 HOH 202 902  217 HOH HOH B . 
L 7 HOH 203 903  361 HOH HOH B . 
L 7 HOH 204 904  363 HOH HOH B . 
L 7 HOH 205 905  236 HOH HOH B . 
L 7 HOH 206 906  648 HOH HOH B . 
L 7 HOH 207 907  46  HOH HOH B . 
L 7 HOH 208 908  37  HOH HOH B . 
L 7 HOH 209 909  353 HOH HOH B . 
L 7 HOH 210 910  19  HOH HOH B . 
L 7 HOH 211 911  413 HOH HOH B . 
L 7 HOH 212 912  85  HOH HOH B . 
L 7 HOH 213 913  47  HOH HOH B . 
L 7 HOH 214 914  471 HOH HOH B . 
L 7 HOH 215 915  245 HOH HOH B . 
L 7 HOH 216 916  589 HOH HOH B . 
L 7 HOH 217 917  379 HOH HOH B . 
L 7 HOH 218 918  492 HOH HOH B . 
L 7 HOH 219 919  513 HOH HOH B . 
L 7 HOH 220 920  55  HOH HOH B . 
L 7 HOH 221 921  71  HOH HOH B . 
L 7 HOH 222 922  178 HOH HOH B . 
L 7 HOH 223 923  340 HOH HOH B . 
L 7 HOH 224 924  440 HOH HOH B . 
L 7 HOH 225 925  144 HOH HOH B . 
L 7 HOH 226 926  571 HOH HOH B . 
L 7 HOH 227 927  354 HOH HOH B . 
L 7 HOH 228 928  444 HOH HOH B . 
L 7 HOH 229 929  266 HOH HOH B . 
L 7 HOH 230 930  244 HOH HOH B . 
L 7 HOH 231 931  181 HOH HOH B . 
L 7 HOH 232 932  317 HOH HOH B . 
L 7 HOH 233 933  1   HOH HOH B . 
L 7 HOH 234 934  581 HOH HOH B . 
L 7 HOH 235 935  555 HOH HOH B . 
L 7 HOH 236 936  330 HOH HOH B . 
L 7 HOH 237 937  383 HOH HOH B . 
L 7 HOH 238 938  56  HOH HOH B . 
L 7 HOH 239 939  495 HOH HOH B . 
L 7 HOH 240 940  554 HOH HOH B . 
L 7 HOH 241 941  358 HOH HOH B . 
L 7 HOH 242 942  547 HOH HOH B . 
L 7 HOH 243 943  15  HOH HOH B . 
L 7 HOH 244 944  687 HOH HOH B . 
L 7 HOH 245 945  326 HOH HOH B . 
L 7 HOH 246 946  134 HOH HOH B . 
L 7 HOH 247 947  583 HOH HOH B . 
L 7 HOH 248 948  509 HOH HOH B . 
L 7 HOH 249 949  268 HOH HOH B . 
L 7 HOH 250 950  481 HOH HOH B . 
L 7 HOH 251 951  490 HOH HOH B . 
L 7 HOH 252 952  565 HOH HOH B . 
L 7 HOH 253 953  138 HOH HOH B . 
L 7 HOH 254 954  262 HOH HOH B . 
L 7 HOH 255 955  609 HOH HOH B . 
L 7 HOH 256 956  548 HOH HOH B . 
L 7 HOH 257 957  11  HOH HOH B . 
L 7 HOH 258 958  359 HOH HOH B . 
L 7 HOH 259 959  45  HOH HOH B . 
L 7 HOH 260 960  557 HOH HOH B . 
L 7 HOH 261 961  636 HOH HOH B . 
L 7 HOH 262 962  188 HOH HOH B . 
L 7 HOH 263 963  600 HOH HOH B . 
L 7 HOH 264 964  475 HOH HOH B . 
L 7 HOH 265 965  615 HOH HOH B . 
L 7 HOH 266 966  671 HOH HOH B . 
L 7 HOH 267 967  114 HOH HOH B . 
L 7 HOH 268 968  99  HOH HOH B . 
L 7 HOH 269 969  95  HOH HOH B . 
L 7 HOH 270 970  396 HOH HOH B . 
L 7 HOH 271 971  304 HOH HOH B . 
L 7 HOH 272 972  414 HOH HOH B . 
L 7 HOH 273 973  463 HOH HOH B . 
L 7 HOH 274 974  593 HOH HOH B . 
L 7 HOH 275 975  501 HOH HOH B . 
L 7 HOH 276 976  608 HOH HOH B . 
L 7 HOH 277 977  614 HOH HOH B . 
L 7 HOH 278 978  316 HOH HOH B . 
L 7 HOH 279 979  574 HOH HOH B . 
L 7 HOH 280 980  325 HOH HOH B . 
L 7 HOH 281 981  544 HOH HOH B . 
L 7 HOH 282 982  351 HOH HOH B . 
L 7 HOH 283 983  601 HOH HOH B . 
L 7 HOH 284 984  520 HOH HOH B . 
L 7 HOH 285 985  366 HOH HOH B . 
L 7 HOH 286 986  486 HOH HOH B . 
L 7 HOH 287 987  412 HOH HOH B . 
L 7 HOH 288 988  568 HOH HOH B . 
L 7 HOH 289 989  378 HOH HOH B . 
L 7 HOH 290 990  572 HOH HOH B . 
L 7 HOH 291 991  605 HOH HOH B . 
L 7 HOH 292 992  596 HOH HOH B . 
L 7 HOH 293 993  308 HOH HOH B . 
L 7 HOH 294 994  588 HOH HOH B . 
L 7 HOH 295 995  590 HOH HOH B . 
L 7 HOH 296 996  408 HOH HOH B . 
L 7 HOH 297 997  436 HOH HOH B . 
L 7 HOH 298 998  578 HOH HOH B . 
L 7 HOH 299 999  90  HOH HOH B . 
L 7 HOH 300 1000 570 HOH HOH B . 
L 7 HOH 301 1001 677 HOH HOH B . 
L 7 HOH 302 1002 510 HOH HOH B . 
L 7 HOH 303 1003 674 HOH HOH B . 
L 7 HOH 304 1004 645 HOH HOH B . 
L 7 HOH 305 1005 511 HOH HOH B . 
L 7 HOH 306 1006 430 HOH HOH B . 
L 7 HOH 307 1007 612 HOH HOH B . 
L 7 HOH 308 1008 607 HOH HOH B . 
L 7 HOH 309 1009 487 HOH HOH B . 
L 7 HOH 310 1010 613 HOH HOH B . 
L 7 HOH 311 1011 451 HOH HOH B . 
L 7 HOH 312 1012 448 HOH HOH B . 
L 7 HOH 313 1013 298 HOH HOH B . 
L 7 HOH 314 1014 599 HOH HOH B . 
L 7 HOH 315 1015 575 HOH HOH B . 
L 7 HOH 316 1016 542 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A HIS 7   ? CG  ? A HIS 7   CG  
2   1 Y 1 A HIS 7   ? ND1 ? A HIS 7   ND1 
3   1 Y 1 A HIS 7   ? CD2 ? A HIS 7   CD2 
4   1 Y 1 A HIS 7   ? CE1 ? A HIS 7   CE1 
5   1 Y 1 A HIS 7   ? NE2 ? A HIS 7   NE2 
6   1 Y 1 A ARG 38  ? CG  ? A ARG 38  CG  
7   1 Y 1 A ARG 38  ? CD  ? A ARG 38  CD  
8   1 Y 1 A ARG 38  ? NE  ? A ARG 38  NE  
9   1 Y 1 A ARG 38  ? CZ  ? A ARG 38  CZ  
10  1 Y 1 A ARG 38  ? NH1 ? A ARG 38  NH1 
11  1 Y 1 A ARG 38  ? NH2 ? A ARG 38  NH2 
12  1 Y 1 A GLU 49  ? CG  ? A GLU 49  CG  
13  1 Y 1 A GLU 49  ? CD  ? A GLU 49  CD  
14  1 Y 1 A GLU 49  ? OE1 ? A GLU 49  OE1 
15  1 Y 1 A GLU 49  ? OE2 ? A GLU 49  OE2 
16  1 Y 1 A LYS 69  ? CG  ? A LYS 69  CG  
17  1 Y 1 A LYS 69  ? CD  ? A LYS 69  CD  
18  1 Y 1 A LYS 69  ? CE  ? A LYS 69  CE  
19  1 Y 1 A LYS 69  ? NZ  ? A LYS 69  NZ  
20  1 Y 1 A VAL 80  ? CG1 ? A VAL 80  CG1 
21  1 Y 1 A VAL 80  ? CG2 ? A VAL 80  CG2 
22  1 Y 1 A THR 81  ? OG1 ? A THR 81  OG1 
23  1 Y 1 A THR 81  ? CG2 ? A THR 81  CG2 
24  1 Y 1 A ARG 86  ? CG  ? A ARG 86  CG  
25  1 Y 1 A ARG 86  ? CD  ? A ARG 86  CD  
26  1 Y 1 A ARG 86  ? NE  ? A ARG 86  NE  
27  1 Y 1 A ARG 86  ? CZ  ? A ARG 86  CZ  
28  1 Y 1 A ARG 86  ? NH1 ? A ARG 86  NH1 
29  1 Y 1 A ARG 86  ? NH2 ? A ARG 86  NH2 
30  1 Y 1 A GLU 94  ? CG  ? A GLU 94  CG  
31  1 Y 1 A GLU 94  ? CD  ? A GLU 94  CD  
32  1 Y 1 A GLU 94  ? OE1 ? A GLU 94  OE1 
33  1 Y 1 A GLU 94  ? OE2 ? A GLU 94  OE2 
34  1 Y 1 A LEU 126 ? CG  ? A LEU 126 CG  
35  1 Y 1 A LEU 126 ? CD1 ? A LEU 126 CD1 
36  1 Y 1 A LEU 126 ? CD2 ? A LEU 126 CD2 
37  1 Y 1 A ARG 130 ? CG  ? A ARG 130 CG  
38  1 Y 1 A ARG 130 ? CD  ? A ARG 130 CD  
39  1 Y 1 A ARG 130 ? NE  ? A ARG 130 NE  
40  1 Y 1 A ARG 130 ? CZ  ? A ARG 130 CZ  
41  1 Y 1 A ARG 130 ? NH1 ? A ARG 130 NH1 
42  1 Y 1 A ARG 130 ? NH2 ? A ARG 130 NH2 
43  1 Y 1 A MET 302 ? CG  ? A MET 302 CG  
44  1 Y 1 A MET 302 ? SD  ? A MET 302 SD  
45  1 Y 1 A MET 302 ? CE  ? A MET 302 CE  
46  1 Y 1 A ASP 374 ? CG  ? A ASP 374 CG  
47  1 Y 1 A ASP 374 ? OD1 ? A ASP 374 OD1 
48  1 Y 1 A ASP 374 ? OD2 ? A ASP 374 OD2 
49  1 Y 1 A ARG 381 ? CG  ? A ARG 381 CG  
50  1 Y 1 A ARG 381 ? CD  ? A ARG 381 CD  
51  1 Y 1 A ARG 381 ? NE  ? A ARG 381 NE  
52  1 Y 1 A ARG 381 ? CZ  ? A ARG 381 CZ  
53  1 Y 1 A ARG 381 ? NH1 ? A ARG 381 NH1 
54  1 Y 1 A ARG 381 ? NH2 ? A ARG 381 NH2 
55  1 Y 1 A SER 385 ? OG  ? A SER 385 OG  
56  1 Y 1 A GLU 388 ? CG  ? A GLU 388 CG  
57  1 Y 1 A GLU 388 ? CD  ? A GLU 388 CD  
58  1 Y 1 A GLU 388 ? OE1 ? A GLU 388 OE1 
59  1 Y 1 A GLU 388 ? OE2 ? A GLU 388 OE2 
60  1 Y 1 A ILE 406 ? CG1 ? A ILE 406 CG1 
61  1 Y 1 A ILE 406 ? CG2 ? A ILE 406 CG2 
62  1 Y 1 A ILE 406 ? CD1 ? A ILE 406 CD1 
63  1 Y 1 A LYS 423 ? CG  ? A LYS 423 CG  
64  1 Y 1 A LYS 423 ? CD  ? A LYS 423 CD  
65  1 Y 1 A LYS 423 ? CE  ? A LYS 423 CE  
66  1 Y 1 A LYS 423 ? NZ  ? A LYS 423 NZ  
67  1 Y 1 A GLU 468 ? CG  ? A GLU 468 CG  
68  1 Y 1 A GLU 468 ? CD  ? A GLU 468 CD  
69  1 Y 1 A GLU 468 ? OE1 ? A GLU 468 OE1 
70  1 Y 1 A GLU 468 ? OE2 ? A GLU 468 OE2 
71  1 Y 1 B HIS 7   ? CG  ? B HIS 7   CG  
72  1 Y 1 B HIS 7   ? ND1 ? B HIS 7   ND1 
73  1 Y 1 B HIS 7   ? CD2 ? B HIS 7   CD2 
74  1 Y 1 B HIS 7   ? CE1 ? B HIS 7   CE1 
75  1 Y 1 B HIS 7   ? NE2 ? B HIS 7   NE2 
76  1 Y 1 B ARG 38  ? CG  ? B ARG 38  CG  
77  1 Y 1 B ARG 38  ? CD  ? B ARG 38  CD  
78  1 Y 1 B ARG 38  ? NE  ? B ARG 38  NE  
79  1 Y 1 B ARG 38  ? CZ  ? B ARG 38  CZ  
80  1 Y 1 B ARG 38  ? NH1 ? B ARG 38  NH1 
81  1 Y 1 B ARG 38  ? NH2 ? B ARG 38  NH2 
82  1 Y 1 B GLU 49  ? CG  ? B GLU 49  CG  
83  1 Y 1 B GLU 49  ? CD  ? B GLU 49  CD  
84  1 Y 1 B GLU 49  ? OE1 ? B GLU 49  OE1 
85  1 Y 1 B GLU 49  ? OE2 ? B GLU 49  OE2 
86  1 Y 1 B GLU 54  ? CG  ? B GLU 54  CG  
87  1 Y 1 B GLU 54  ? CD  ? B GLU 54  CD  
88  1 Y 1 B GLU 54  ? OE1 ? B GLU 54  OE1 
89  1 Y 1 B GLU 54  ? OE2 ? B GLU 54  OE2 
90  1 Y 1 B ASP 56  ? CG  ? B ASP 56  CG  
91  1 Y 1 B ASP 56  ? OD1 ? B ASP 56  OD1 
92  1 Y 1 B ASP 56  ? OD2 ? B ASP 56  OD2 
93  1 Y 1 B LYS 68  ? CG  ? B LYS 68  CG  
94  1 Y 1 B LYS 68  ? CD  ? B LYS 68  CD  
95  1 Y 1 B LYS 68  ? CE  ? B LYS 68  CE  
96  1 Y 1 B LYS 68  ? NZ  ? B LYS 68  NZ  
97  1 Y 1 B ARG 86  ? CG  ? B ARG 86  CG  
98  1 Y 1 B ARG 86  ? CD  ? B ARG 86  CD  
99  1 Y 1 B ARG 86  ? NE  ? B ARG 86  NE  
100 1 Y 1 B ARG 86  ? CZ  ? B ARG 86  CZ  
101 1 Y 1 B ARG 86  ? NH1 ? B ARG 86  NH1 
102 1 Y 1 B ARG 86  ? NH2 ? B ARG 86  NH2 
103 1 Y 1 B GLU 94  ? CG  ? B GLU 94  CG  
104 1 Y 1 B GLU 94  ? CD  ? B GLU 94  CD  
105 1 Y 1 B GLU 94  ? OE1 ? B GLU 94  OE1 
106 1 Y 1 B GLU 94  ? OE2 ? B GLU 94  OE2 
107 1 Y 1 B ARG 107 ? CG  ? B ARG 107 CG  
108 1 Y 1 B ARG 107 ? CD  ? B ARG 107 CD  
109 1 Y 1 B ARG 107 ? NE  ? B ARG 107 NE  
110 1 Y 1 B ARG 107 ? CZ  ? B ARG 107 CZ  
111 1 Y 1 B ARG 107 ? NH1 ? B ARG 107 NH1 
112 1 Y 1 B ARG 107 ? NH2 ? B ARG 107 NH2 
113 1 Y 1 B SER 110 ? OG  ? B SER 110 OG  
114 1 Y 1 B ARG 130 ? CG  ? B ARG 130 CG  
115 1 Y 1 B ARG 130 ? CD  ? B ARG 130 CD  
116 1 Y 1 B ARG 130 ? NE  ? B ARG 130 NE  
117 1 Y 1 B ARG 130 ? CZ  ? B ARG 130 CZ  
118 1 Y 1 B ARG 130 ? NH1 ? B ARG 130 NH1 
119 1 Y 1 B ARG 130 ? NH2 ? B ARG 130 NH2 
120 1 Y 1 B LYS 131 ? CG  ? B LYS 131 CG  
121 1 Y 1 B LYS 131 ? CD  ? B LYS 131 CD  
122 1 Y 1 B LYS 131 ? CE  ? B LYS 131 CE  
123 1 Y 1 B LYS 131 ? NZ  ? B LYS 131 NZ  
124 1 Y 1 B THR 219 ? OG1 ? B THR 219 OG1 
125 1 Y 1 B THR 219 ? CG2 ? B THR 219 CG2 
126 1 Y 1 B GLU 298 ? CG  ? B GLU 298 CG  
127 1 Y 1 B GLU 298 ? CD  ? B GLU 298 CD  
128 1 Y 1 B GLU 298 ? OE1 ? B GLU 298 OE1 
129 1 Y 1 B GLU 298 ? OE2 ? B GLU 298 OE2 
130 1 Y 1 B GLN 309 ? CG  ? B GLN 309 CG  
131 1 Y 1 B GLN 309 ? CD  ? B GLN 309 CD  
132 1 Y 1 B GLN 309 ? OE1 ? B GLN 309 OE1 
133 1 Y 1 B GLN 309 ? NE2 ? B GLN 309 NE2 
134 1 Y 1 B ARG 381 ? CG  ? B ARG 381 CG  
135 1 Y 1 B ARG 381 ? CD  ? B ARG 381 CD  
136 1 Y 1 B ARG 381 ? NE  ? B ARG 381 NE  
137 1 Y 1 B ARG 381 ? CZ  ? B ARG 381 CZ  
138 1 Y 1 B ARG 381 ? NH1 ? B ARG 381 NH1 
139 1 Y 1 B ARG 381 ? NH2 ? B ARG 381 NH2 
140 1 Y 1 B GLU 388 ? CG  ? B GLU 388 CG  
141 1 Y 1 B GLU 388 ? CD  ? B GLU 388 CD  
142 1 Y 1 B GLU 388 ? OE1 ? B GLU 388 OE1 
143 1 Y 1 B GLU 388 ? OE2 ? B GLU 388 OE2 
144 1 Y 1 B LYS 423 ? CG  ? B LYS 423 CG  
145 1 Y 1 B LYS 423 ? CD  ? B LYS 423 CD  
146 1 Y 1 B LYS 423 ? CE  ? B LYS 423 CE  
147 1 Y 1 B LYS 423 ? NZ  ? B LYS 423 NZ  
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G8D 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.644 
_cell.length_a_esd                 ? 
_cell.length_b                     93.577 
_cell.length_b_esd                 ? 
_cell.length_c                     173.945 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9G8D 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9G8D 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.00 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_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    '30 - 40% MPD, 5 - 15% PEG 8000, 0.1 M MES pH 5.5 - 9.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            279 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-07-02 
_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   0.97625 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97625 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G8D 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.059 
_reflns.d_resolution_low                               45.83 
_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                                     75997 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.0 
_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                                   0.857 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.059 
_reflns_shell.d_res_low                                     2.11 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5170 
_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                                  0.201 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.56 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            1.61 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -2.17 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               33.077 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.939 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9G8D 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.059 
_refine.ls_d_res_low                             45.83 
_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                     72339 
_refine.ls_number_reflns_R_free                  3718 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.82 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18776 
_refine.ls_R_factor_R_free                       0.22409 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18592 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.180 
_refine.pdbx_overall_ESU_R_Free                  0.159 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             4.913 
_refine.overall_SU_ML                            0.128 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.059 
_refine_hist.d_res_low                        45.83 
_refine_hist.number_atoms_solvent             656 
_refine_hist.number_atoms_total               8321 
_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        7547 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         118 
_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' ? 0.005  0.013  7877  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.015  7362  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.326  1.646  10700 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.306  1.575  16874 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.129  5.000  984   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 27.789 20.360 417   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.877 15.000 1156  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.012 15.000 61    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.055  0.200  1028  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  8897  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  1809  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.696  3.412  3931  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.695  3.411  3930  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.662  5.104  4893  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.662  5.105  4894  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.041  3.629  3946  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.041  3.629  3947  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.297  5.351  5800  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.083  40.726 8777  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.981  40.404 8655  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.059 
_refine_ls_shell.d_res_low                        2.112 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             259 
_refine_ls_shell.number_reflns_R_work             5170 
_refine_ls_shell.percent_reflns_obs               98.03 
_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                  0.269 
_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   20 
_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                  0.292 
# 
_struct.entry_id                     9G8D 
_struct.title                        
;Crystal structure of the photosensory core module (PCM) of a cyano-phenylalanine mutant oCNF192 of the bathy phytochrome Agp2 from Agrobacterium fabrum in the Pfr state.
;
_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        9G8D 
_struct_keywords.text            
'fluorescent protein, phytochrome, bacteriophytochrome, Pfr-state, ortho-cyano-phenylalanine, Stark labels, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 6 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 7 ? 
L N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP A9CI81_AGRFC A9CI81 ? 1 
;MASTDYHVDLTNCDREPIHIPGYIQPHGCLIACDNAMRMVLRHSENCGELLGLEGDLNGRTAEDVLGKKLVHDLRNALTV
TGRTTRPAMLPAMETSDGRSFDISLHRYKSTTIIEFEPSGSDAQPLGTARKMVDRIREADSVESLISRTTRLVKATLGYD
RVMIYRFQEDGAGKVVSEAKQPELESFLGQYFPASDIPQQARALYLKNTLRIISDASGTRIPVLPAVDVSGEPLDLSYAH
LRSVSPIHCEYLRNMGVAASMSISVIVDGALWGLIACHHYSPRVLSMPVRIAAEMFGEFFSMHLQVLKQKRRLDTINHAH
AALDRFLRLAAHHANIEELLVDSFQDFADLMPCDGVGLWVGNNWHGHGATPPHDAIPRLARFVASASEGRVWATHALSQA
IPEAEIYAGTAAGMLAIPLSQVKSDYLLFFRKEIVQNLNWAGNPEKSYETGPMGDRLTPRKSFAIWKETVRLQAQPWSEA
DREIAEAARIALVEVAFHHSE
;
1 
2 UNP A9CI81_AGRFC A9CI81 ? 2 
;MASTDYHVDLTNCDREPIHIPGYIQPHGCLIACDNAMRMVLRHSENCGELLGLEGDLNGRTAEDVLGKKLVHDLRNALTV
TGRTTRPAMLPAMETSDGRSFDISLHRYKSTTIIEFEPSGSDAQPLGTARKMVDRIREADSVESLISRTTRLVKATLGYD
RVMIYRFQEDGAGKVVSEAKQPELESFLGQYFPASDIPQQARALYLKNTLRIISDASGTRIPVLPAVDVSGEPLDLSYAH
LRSVSPIHCEYLRNMGVAASMSISVIVDGALWGLIACHHYSPRVLSMPVRIAAEMFGEFFSMHLQVLKQKRRLDTINHAH
AALDRFLRLAAHHANIEELLVDSFQDFADLMPCDGVGLWVGNNWHGHGATPPHDAIPRLARFVASASEGRVWATHALSQA
IPEAEIYAGTAAGMLAIPLSQVKSDYLLFFRKEIVQNLNWAGNPEKSYETGPMGDRLTPRKSFAIWKETVRLQAQPWSEA
DREIAEAARIALVEVAFHHSE
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9G8D A 1 ? 501 ? A9CI81 1 ? 501 ? 1 501 
2 2 9G8D B 1 ? 501 ? A9CI81 1 ? 501 ? 1 501 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9G8D HIS A 502 ? UNP A9CI81 ? ? 'expression tag' 502 1  
1 9G8D HIS A 503 ? UNP A9CI81 ? ? 'expression tag' 503 2  
1 9G8D HIS A 504 ? UNP A9CI81 ? ? 'expression tag' 504 3  
1 9G8D HIS A 505 ? UNP A9CI81 ? ? 'expression tag' 505 4  
1 9G8D HIS A 506 ? UNP A9CI81 ? ? 'expression tag' 506 5  
1 9G8D HIS A 507 ? UNP A9CI81 ? ? 'expression tag' 507 6  
2 9G8D HIS B 502 ? UNP A9CI81 ? ? 'expression tag' 502 7  
2 9G8D HIS B 503 ? UNP A9CI81 ? ? 'expression tag' 503 8  
2 9G8D HIS B 504 ? UNP A9CI81 ? ? 'expression tag' 504 9  
2 9G8D HIS B 505 ? UNP A9CI81 ? ? 'expression tag' 505 10 
2 9G8D HIS B 506 ? UNP A9CI81 ? ? 'expression tag' 506 11 
2 9G8D HIS B 507 ? UNP A9CI81 ? ? 'expression tag' 507 12 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 3090  ? 
1 MORE         -41   ? 
1 'SSA (A^2)'  42390 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 12  ? GLU A 16  ? ASN A 12  GLU A 16  5 ? 5  
HELX_P HELX_P2  AA2 ASN A 46  ? GLY A 52  ? ASN A 46  GLY A 52  1 ? 7  
HELX_P HELX_P3  AA3 THR A 61  ? GLY A 67  ? THR A 61  GLY A 67  1 ? 7  
HELX_P HELX_P4  AA4 GLY A 67  ? THR A 81  ? GLY A 67  THR A 81  1 ? 15 
HELX_P HELX_P5  AA5 LEU A 126 ? ARG A 135 ? LEU A 126 ARG A 135 1 ? 10 
HELX_P HELX_P6  AA6 SER A 141 ? GLY A 158 ? SER A 141 GLY A 158 1 ? 18 
HELX_P HELX_P7  AA7 PRO A 193 ? ILE A 197 ? PRO A 193 ILE A 197 5 ? 5  
HELX_P HELX_P8  AA8 PRO A 198 ? ASN A 208 ? PRO A 198 ASN A 208 1 ? 11 
HELX_P HELX_P9  AA9 SER A 245 ? GLY A 256 ? SER A 245 GLY A 256 1 ? 12 
HELX_P HELX_P10 AB1 SER A 286 ? ALA A 331 ? SER A 286 ALA A 331 1 ? 46 
HELX_P HELX_P11 AB2 ASN A 335 ? PHE A 344 ? ASN A 335 PHE A 344 1 ? 10 
HELX_P HELX_P12 AB3 GLN A 345 ? MET A 351 ? GLN A 345 MET A 351 5 ? 7  
HELX_P HELX_P13 AB4 PRO A 372 ? ASP A 374 ? PRO A 372 ASP A 374 5 ? 3  
HELX_P HELX_P14 AB5 ALA A 375 ? SER A 387 ? ALA A 375 SER A 387 1 ? 13 
HELX_P HELX_P15 AB6 ALA A 396 ? ILE A 401 ? ALA A 396 ILE A 401 1 ? 6  
HELX_P HELX_P16 AB7 PRO A 402 ? ALA A 408 ? PRO A 402 ALA A 408 5 ? 7  
HELX_P HELX_P17 AB8 GLU A 433 ? LEU A 438 ? GLU A 433 LEU A 438 5 ? 6  
HELX_P HELX_P18 AB9 GLY A 454 ? LEU A 457 ? GLY A 454 LEU A 457 5 ? 4  
HELX_P HELX_P19 AC1 THR A 458 ? VAL A 470 ? THR A 458 VAL A 470 1 ? 13 
HELX_P HELX_P20 AC2 SER A 478 ? HIS A 503 ? SER A 478 HIS A 503 1 ? 26 
HELX_P HELX_P21 AC3 ASN B 12  ? GLU B 16  ? ASN B 12  GLU B 16  5 ? 5  
HELX_P HELX_P22 AC4 ASN B 46  ? GLY B 52  ? ASN B 46  GLY B 52  1 ? 7  
HELX_P HELX_P23 AC5 THR B 61  ? GLY B 67  ? THR B 61  GLY B 67  1 ? 7  
HELX_P HELX_P24 AC6 GLY B 67  ? VAL B 80  ? GLY B 67  VAL B 80  1 ? 14 
HELX_P HELX_P25 AC7 GLN B 124 ? ARG B 135 ? GLN B 124 ARG B 135 1 ? 12 
HELX_P HELX_P26 AC8 SER B 141 ? GLY B 158 ? SER B 141 GLY B 158 1 ? 18 
HELX_P HELX_P27 AC9 PRO B 193 ? ILE B 197 ? PRO B 193 ILE B 197 5 ? 5  
HELX_P HELX_P28 AD1 PRO B 198 ? ASN B 208 ? PRO B 198 ASN B 208 1 ? 11 
HELX_P HELX_P29 AD2 SER B 245 ? GLY B 256 ? SER B 245 GLY B 256 1 ? 12 
HELX_P HELX_P30 AD3 SER B 286 ? HIS B 332 ? SER B 286 HIS B 332 1 ? 47 
HELX_P HELX_P31 AD4 ASN B 335 ? PHE B 344 ? ASN B 335 PHE B 344 1 ? 10 
HELX_P HELX_P32 AD5 GLN B 345 ? MET B 351 ? GLN B 345 MET B 351 5 ? 7  
HELX_P HELX_P33 AD6 PRO B 372 ? ASP B 374 ? PRO B 372 ASP B 374 5 ? 3  
HELX_P HELX_P34 AD7 ALA B 375 ? SER B 387 ? ALA B 375 SER B 387 1 ? 13 
HELX_P HELX_P35 AD8 ALA B 396 ? ILE B 401 ? ALA B 396 ILE B 401 1 ? 6  
HELX_P HELX_P36 AD9 PRO B 402 ? ALA B 408 ? PRO B 402 ALA B 408 5 ? 7  
HELX_P HELX_P37 AE1 GLU B 433 ? LEU B 438 ? GLU B 433 LEU B 438 5 ? 6  
HELX_P HELX_P38 AE2 GLY B 454 ? LEU B 457 ? GLY B 454 LEU B 457 5 ? 4  
HELX_P HELX_P39 AE3 THR B 458 ? VAL B 470 ? THR B 458 VAL B 470 1 ? 13 
HELX_P HELX_P40 AE4 SER B 478 ? HIS B 503 ? SER B 478 HIS B 503 1 ? 26 
# 
_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 
covale1  covale none ? A CYS 13  SG ? ? ? 1_555 E EL5 .   CBA ? ? A CYS 13  A EL5 603 1_555 ? ? ? ? ? ? ? 1.701 ? ? 
covale2  covale both ? A VAL 153 C  ? ? ? 1_555 A MLZ 154 N   ? ? A VAL 153 A MLZ 154 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale3  covale both ? A MLZ 154 C  ? ? ? 1_555 A ALA 155 N   ? ? A MLZ 154 A ALA 155 1_555 ? ? ? ? ? ? ? 1.337 ? ? 
covale4  covale both ? A GLY 173 C  ? ? ? 1_555 A MLZ 174 N   ? ? A GLY 173 A MLZ 174 1_555 ? ? ? ? ? ? ? 1.342 ? ? 
covale5  covale both ? A MLZ 174 C  ? ? ? 1_555 A VAL 175 N   ? ? A MLZ 174 A VAL 175 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale6  covale both ? A ALA 179 C  ? ? ? 1_555 A MLZ 180 N   ? ? A ALA 179 A MLZ 180 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale7  covale both ? A MLZ 180 C  ? ? ? 1_555 A GLN 181 N   ? ? A MLZ 180 A GLN 181 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale8  covale both ? A TYR 191 C  ? ? ? 1_555 A 9IJ 192 N   ? ? A TYR 191 A 9IJ 192 1_555 ? ? ? ? ? ? ? 1.290 ? ? 
covale9  covale both ? A 9IJ 192 C  ? ? ? 1_555 A PRO 193 N   ? ? A 9IJ 192 A PRO 193 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale10 covale both ? A LEU 206 C  ? ? ? 1_555 A MLZ 207 N   ? ? A LEU 206 A MLZ 207 1_555 ? ? ? ? ? ? ? 1.340 ? ? 
covale11 covale both ? A MLZ 207 C  ? ? ? 1_555 A ASN 208 N   ? ? A MLZ 207 A ASN 208 1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale12 covale both ? A GLN 309 C  ? ? ? 1_555 A MLZ 310 N   ? ? A GLN 309 A MLZ 310 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale13 covale both ? A MLZ 310 C  ? ? ? 1_555 A ARG 311 N   ? ? A MLZ 310 A ARG 311 1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale14 covale both ? A ARG 431 C  ? ? ? 1_555 A MLZ 432 N   ? ? A ARG 431 A MLZ 432 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale15 covale both ? A MLZ 432 C  ? ? ? 1_555 A GLU 433 N   ? ? A MLZ 432 A GLU 433 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale16 covale both ? A GLU 445 C  ? ? ? 1_555 A MLZ 446 N   ? ? A GLU 445 A MLZ 446 1_555 ? ? ? ? ? ? ? 1.342 ? ? 
covale17 covale both ? A MLZ 446 C  ? ? ? 1_555 A SER 447 N   ? ? A MLZ 446 A SER 447 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale18 covale both ? A ARG 460 C  ? ? ? 1_555 A MLZ 461 N   ? ? A ARG 460 A MLZ 461 1_555 ? ? ? ? ? ? ? 1.340 ? ? 
covale19 covale both ? A MLZ 461 C  ? ? ? 1_555 A SER 462 N   ? ? A MLZ 461 A SER 462 1_555 ? ? ? ? ? ? ? 1.345 ? ? 
covale20 covale both ? A TRP 466 C  ? ? ? 1_555 A MLZ 467 N   ? ? A TRP 466 A MLZ 467 1_555 ? ? ? ? ? ? ? 1.341 ? ? 
covale21 covale both ? A MLZ 467 C  ? ? ? 1_555 A GLU 468 N   ? ? A MLZ 467 A GLU 468 1_555 ? ? ? ? ? ? ? 1.336 ? ? 
covale22 covale none ? B CYS 13  SG ? ? ? 1_555 J EL5 .   CBA ? ? B CYS 13  B EL5 603 1_555 ? ? ? ? ? ? ? 1.707 ? ? 
covale23 covale both ? B VAL 153 C  ? ? ? 1_555 B MLZ 154 N   ? ? B VAL 153 B MLZ 154 1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale24 covale both ? B MLZ 154 C  ? ? ? 1_555 B ALA 155 N   ? ? B MLZ 154 B ALA 155 1_555 ? ? ? ? ? ? ? 1.337 ? ? 
covale25 covale both ? B GLY 173 C  ? ? ? 1_555 B MLZ 174 N   ? ? B GLY 173 B MLZ 174 1_555 ? ? ? ? ? ? ? 1.343 ? ? 
covale26 covale both ? B MLZ 174 C  ? ? ? 1_555 B VAL 175 N   ? ? B MLZ 174 B VAL 175 1_555 ? ? ? ? ? ? ? 1.340 ? ? 
covale27 covale both ? B ALA 179 C  ? ? ? 1_555 B MLZ 180 N   ? ? B ALA 179 B MLZ 180 1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale28 covale both ? B MLZ 180 C  ? ? ? 1_555 B GLN 181 N   ? ? B MLZ 180 B GLN 181 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale29 covale both ? B TYR 191 C  ? ? ? 1_555 B 9IJ 192 N   ? ? B TYR 191 B 9IJ 192 1_555 ? ? ? ? ? ? ? 1.310 ? ? 
covale30 covale both ? B 9IJ 192 C  ? ? ? 1_555 B PRO 193 N   ? ? B 9IJ 192 B PRO 193 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale31 covale both ? B LEU 206 C  ? ? ? 1_555 B MLZ 207 N   ? ? B LEU 206 B MLZ 207 1_555 ? ? ? ? ? ? ? 1.336 ? ? 
covale32 covale both ? B MLZ 207 C  ? ? ? 1_555 B ASN 208 N   ? ? B MLZ 207 B ASN 208 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale33 covale both ? B GLN 309 C  ? ? ? 1_555 B MLZ 310 N   ? ? B GLN 309 B MLZ 310 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale34 covale both ? B MLZ 310 C  ? ? ? 1_555 B ARG 311 N   ? ? B MLZ 310 B ARG 311 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale35 covale both ? B ARG 431 C  ? ? ? 1_555 B MLZ 432 N   ? ? B ARG 431 B MLZ 432 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale36 covale both ? B MLZ 432 C  ? ? ? 1_555 B GLU 433 N   ? ? B MLZ 432 B GLU 433 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale37 covale both ? B GLU 445 C  ? ? ? 1_555 B MLZ 446 N   ? ? B GLU 445 B MLZ 446 1_555 ? ? ? ? ? ? ? 1.340 ? ? 
covale38 covale both ? B MLZ 446 C  ? ? ? 1_555 B SER 447 N   ? ? B MLZ 446 B SER 447 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale39 covale both ? B TRP 466 C  ? ? ? 1_555 B MLZ 467 N   ? ? B TRP 466 B MLZ 467 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale40 covale both ? B MLZ 467 C  ? ? ? 1_555 B GLU 468 N   ? ? B MLZ 467 B GLU 468 1_555 ? ? ? ? ? ? ? 1.338 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  MLZ A 154 ? .   . .  . MLZ A 154 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
2  MLZ A 174 ? .   . .  . MLZ A 174 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
3  MLZ A 180 ? .   . .  . MLZ A 180 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
4  9IJ A 192 ? .   . .  . 9IJ A 192 ? 1_555 .   . .  . .     .   .  PHE 1 9IJ Cyanation   'Named protein modification'     
5  MLZ A 207 ? .   . .  . MLZ A 207 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
6  MLZ A 310 ? .   . .  . MLZ A 310 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
7  MLZ A 432 ? .   . .  . MLZ A 432 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
8  MLZ A 446 ? .   . .  . MLZ A 446 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
9  MLZ A 461 ? .   . .  . MLZ A 461 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
10 MLZ A 467 ? .   . .  . MLZ A 467 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
11 MLZ B 154 ? .   . .  . MLZ B 154 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
12 MLZ B 174 ? .   . .  . MLZ B 174 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
13 MLZ B 180 ? .   . .  . MLZ B 180 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
14 9IJ B 192 ? .   . .  . 9IJ B 192 ? 1_555 .   . .  . .     .   .  PHE 1 9IJ Cyanation   'Named protein modification'     
15 MLZ B 207 ? .   . .  . MLZ B 207 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
16 MLZ B 310 ? .   . .  . MLZ B 310 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
17 MLZ B 432 ? .   . .  . MLZ B 432 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
18 MLZ B 446 ? .   . .  . MLZ B 446 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
19 MLZ B 467 ? .   . .  . MLZ B 467 ? 1_555 .   . .  . .     .   .  LYS 1 MLZ Methylation 'Named protein modification'     
20 EL5 E .   ? CYS A 13 ? EL5 A 603 ? 1_555 CYS A 13 ? 1_555 CBA SG CYS 1 EL5 None        'Covalent chemical modification' 
21 EL5 J .   ? CYS B 13 ? EL5 B 603 ? 1_555 CYS B 13 ? 1_555 CBA SG CYS 1 EL5 None        'Covalent chemical modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 224 A . ? LEU 224 A PRO 225 A ? PRO 225 A 1 -5.50 
2 LEU 224 B . ? LEU 224 B PRO 225 B ? PRO 225 B 1 -3.26 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 6 ? 
AA3 ? 5 ? 
AA4 ? 7 ? 
AA5 ? 6 ? 
AA6 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 23  ? ILE A 24  ? TYR A 23  ILE A 24  
AA1 2 ILE A 221 ? LEU A 224 ? ILE A 221 LEU A 224 
AA1 3 VAL A 40  ? SER A 44  ? VAL A 40  SER A 44  
AA1 4 CYS A 29  ? ASP A 34  ? CYS A 29  ASP A 34  
AA1 5 THR A 111 ? PRO A 118 ? THR A 111 PRO A 118 
AA1 6 SER A 100 ? TYR A 108 ? SER A 100 TYR A 108 
AA1 7 ALA A 88  ? GLU A 94  ? ALA A 88  GLU A 94  
AA2 1 TYR A 191 ? 9IJ A 192 ? TYR A 191 9IJ A 192 
AA2 2 GLY A 173 ? MLZ A 180 ? GLY A 173 MLZ A 180 
AA2 3 ARG A 161 ? PHE A 167 ? ARG A 161 PHE A 167 
AA2 4 ALA A 270 ? HIS A 279 ? ALA A 270 HIS A 279 
AA2 5 ALA A 259 ? VAL A 267 ? ALA A 259 VAL A 267 
AA2 6 LEU A 210 ? ILE A 213 ? LEU A 210 ILE A 213 
AA3 1 ASN A 363 ? GLY A 368 ? ASN A 363 GLY A 368 
AA3 2 GLY A 355 ? VAL A 360 ? GLY A 355 VAL A 360 
AA3 3 TYR A 426 ? ARG A 431 ? TYR A 426 ARG A 431 
AA3 4 GLY A 413 ? PRO A 418 ? GLY A 413 PRO A 418 
AA3 5 TRP A 392 ? THR A 394 ? TRP A 392 THR A 394 
AA4 1 TYR B 23  ? ILE B 24  ? TYR B 23  ILE B 24  
AA4 2 ILE B 221 ? LEU B 224 ? ILE B 221 LEU B 224 
AA4 3 VAL B 40  ? SER B 44  ? VAL B 40  SER B 44  
AA4 4 CYS B 29  ? ASP B 34  ? CYS B 29  ASP B 34  
AA4 5 THR B 111 ? PRO B 118 ? THR B 111 PRO B 118 
AA4 6 SER B 100 ? TYR B 108 ? SER B 100 TYR B 108 
AA4 7 ALA B 88  ? GLU B 94  ? ALA B 88  GLU B 94  
AA5 1 TYR B 191 ? 9IJ B 192 ? TYR B 191 9IJ B 192 
AA5 2 GLY B 173 ? MLZ B 180 ? GLY B 173 MLZ B 180 
AA5 3 ARG B 161 ? PHE B 167 ? ARG B 161 PHE B 167 
AA5 4 ALA B 270 ? HIS B 279 ? ALA B 270 HIS B 279 
AA5 5 ALA B 259 ? VAL B 267 ? ALA B 259 VAL B 267 
AA5 6 LEU B 210 ? ILE B 213 ? LEU B 210 ILE B 213 
AA6 1 ASN B 363 ? GLY B 368 ? ASN B 363 GLY B 368 
AA6 2 GLY B 355 ? VAL B 360 ? GLY B 355 VAL B 360 
AA6 3 TYR B 426 ? ARG B 431 ? TYR B 426 ARG B 431 
AA6 4 GLY B 413 ? PRO B 418 ? GLY B 413 PRO B 418 
AA6 5 TRP B 392 ? THR B 394 ? TRP B 392 THR B 394 
# 
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 ILE A 24  ? N ILE A 24  O ILE A 221 ? O ILE A 221 
AA1 2 3 O LEU A 224 ? O LEU A 224 N HIS A 43  ? N HIS A 43  
AA1 3 4 O LEU A 41  ? O LEU A 41  N ALA A 32  ? N ALA A 32  
AA1 4 5 N CYS A 33  ? N CYS A 33  O THR A 112 ? O THR A 112 
AA1 5 6 O GLU A 115 ? O GLU A 115 N SER A 104 ? N SER A 104 
AA1 6 7 O ILE A 103 ? O ILE A 103 N LEU A 90  ? N LEU A 90  
AA2 1 2 O 9IJ A 192 ? O 9IJ A 192 N GLY A 173 ? N GLY A 173 
AA2 2 3 O ALA A 179 ? O ALA A 179 N VAL A 162 ? N VAL A 162 
AA2 3 4 N ARG A 161 ? N ARG A 161 O HIS A 278 ? O HIS A 278 
AA2 4 5 O ILE A 275 ? O ILE A 275 N ILE A 263 ? N ILE A 263 
AA2 5 6 O SER A 260 ? O SER A 260 N ILE A 213 ? N ILE A 213 
AA3 1 2 O HIS A 365 ? O HIS A 365 N LEU A 358 ? N LEU A 358 
AA3 2 3 N GLY A 357 ? N GLY A 357 O LEU A 428 ? O LEU A 428 
AA3 3 4 O PHE A 429 ? O PHE A 429 N LEU A 415 ? N LEU A 415 
AA3 4 5 O ALA A 416 ? O ALA A 416 N TRP A 392 ? N TRP A 392 
AA4 1 2 N ILE B 24  ? N ILE B 24  O ILE B 221 ? O ILE B 221 
AA4 2 3 O LEU B 224 ? O LEU B 224 N HIS B 43  ? N HIS B 43  
AA4 3 4 O ARG B 42  ? O ARG B 42  N ALA B 32  ? N ALA B 32  
AA4 4 5 N CYS B 33  ? N CYS B 33  O THR B 112 ? O THR B 112 
AA4 5 6 O ILE B 113 ? O ILE B 113 N HIS B 106 ? N HIS B 106 
AA4 6 7 O ILE B 103 ? O ILE B 103 N LEU B 90  ? N LEU B 90  
AA5 1 2 O 9IJ B 192 ? O 9IJ B 192 N GLY B 173 ? N GLY B 173 
AA5 2 3 O ALA B 179 ? O ALA B 179 N VAL B 162 ? N VAL B 162 
AA5 3 4 N ARG B 161 ? N ARG B 161 O HIS B 278 ? O HIS B 278 
AA5 4 5 O GLY B 273 ? O GLY B 273 N VAL B 265 ? N VAL B 265 
AA5 5 6 O SER B 260 ? O SER B 260 N ILE B 213 ? N ILE B 213 
AA6 1 2 O HIS B 365 ? O HIS B 365 N LEU B 358 ? N LEU B 358 
AA6 2 3 N TRP B 359 ? N TRP B 359 O TYR B 426 ? O TYR B 426 
AA6 3 4 O PHE B 429 ? O PHE B 429 N LEU B 415 ? N LEU B 415 
AA6 4 5 O ALA B 416 ? O ALA B 416 N TRP B 392 ? N TRP B 392 
# 
_pdbx_entry_details.entry_id                   9G8D 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   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 SER A 420 ? ? -176.21 147.28 
2 1 LEU A 457 ? ? -99.10  52.80  
3 1 ASP B 215 ? ? -161.21 105.90 
4 1 GLU B 388 ? ? -100.24 42.68  
5 1 ASN B 439 ? ? -119.76 73.24  
6 1 LEU B 457 ? ? -93.04  50.87  
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  A MLZ 154 A MLZ 154 ? LYS 'modified residue' 
2  A MLZ 174 A MLZ 174 ? LYS 'modified residue' 
3  A MLZ 180 A MLZ 180 ? LYS 'modified residue' 
4  A 9IJ 192 A 9IJ 192 ? PHE 'modified residue' 
5  A MLZ 207 A MLZ 207 ? LYS 'modified residue' 
6  A MLZ 310 A MLZ 310 ? LYS 'modified residue' 
7  A MLZ 432 A MLZ 432 ? LYS 'modified residue' 
8  A MLZ 446 A MLZ 446 ? LYS 'modified residue' 
9  A MLZ 461 A MLZ 461 ? LYS 'modified residue' 
10 A MLZ 467 A MLZ 467 ? LYS 'modified residue' 
11 B MLZ 154 B MLZ 154 ? LYS 'modified residue' 
12 B MLZ 174 B MLZ 174 ? LYS 'modified residue' 
13 B MLZ 180 B MLZ 180 ? LYS 'modified residue' 
14 B 9IJ 192 B 9IJ 192 ? PHE 'modified residue' 
15 B MLZ 207 B MLZ 207 ? LYS 'modified residue' 
16 B MLZ 310 B MLZ 310 ? LYS 'modified residue' 
17 B MLZ 432 B MLZ 432 ? LYS 'modified residue' 
18 B MLZ 446 B MLZ 446 ? LYS 'modified residue' 
19 B MLZ 467 B MLZ 467 ? LYS 'modified residue' 
# 
_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                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1016 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.85 
_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 1   ? A MET 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A SER 3   ? A SER 3   
4  1 Y 1 A THR 4   ? A THR 4   
5  1 Y 1 A ASP 5   ? A ASP 5   
6  1 Y 1 A TYR 6   ? A TYR 6   
7  1 Y 1 A GLY 82  ? A GLY 82  
8  1 Y 1 A ARG 83  ? A ARG 83  
9  1 Y 1 A THR 84  ? A THR 84  
10 1 Y 1 A SER 96  ? A SER 96  
11 1 Y 1 A SER 121 ? A SER 121 
12 1 Y 1 A ASP 122 ? A ASP 122 
13 1 Y 1 A ALA 123 ? A ALA 123 
14 1 Y 1 A GLN 124 ? A GLN 124 
15 1 Y 1 A HIS 504 ? A HIS 504 
16 1 Y 1 A HIS 505 ? A HIS 505 
17 1 Y 1 A HIS 506 ? A HIS 506 
18 1 Y 1 A HIS 507 ? A HIS 507 
19 1 Y 1 B MET 1   ? B MET 1   
20 1 Y 1 B ALA 2   ? B ALA 2   
21 1 Y 1 B SER 3   ? B SER 3   
22 1 Y 1 B THR 4   ? B THR 4   
23 1 Y 1 B ASP 5   ? B ASP 5   
24 1 Y 1 B THR 81  ? B THR 81  
25 1 Y 1 B GLY 82  ? B GLY 82  
26 1 Y 1 B ARG 83  ? B ARG 83  
27 1 Y 1 B THR 84  ? B THR 84  
28 1 Y 1 B THR 85  ? B THR 85  
29 1 Y 1 B VAL 229 ? B VAL 229 
30 1 Y 1 B HIS 504 ? B HIS 504 
31 1 Y 1 B HIS 505 ? B HIS 505 
32 1 Y 1 B HIS 506 ? B HIS 506 
33 1 Y 1 B HIS 507 ? B HIS 507 
# 
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 
9IJ N    N  N N 1   
9IJ CA   C  N S 2   
9IJ C    C  N N 3   
9IJ CB   C  N N 4   
9IJ CG   C  Y N 5   
9IJ CD1  C  Y N 6   
9IJ CD2  C  Y N 7   
9IJ CE1  C  Y N 8   
9IJ CE2  C  Y N 9   
9IJ CZ   C  Y N 10  
9IJ C01  C  N N 11  
9IJ N01  N  N N 12  
9IJ O    O  N N 13  
9IJ H    H  N N 14  
9IJ H2   H  N N 15  
9IJ HA   H  N N 16  
9IJ HB2  H  N N 17  
9IJ HB3  H  N N 18  
9IJ HD1  H  N N 19  
9IJ HE1  H  N N 20  
9IJ HE2  H  N N 21  
9IJ HZ   H  N N 22  
9IJ OXT  O  N N 23  
9IJ HXT  H  N N 24  
ALA N    N  N N 25  
ALA CA   C  N S 26  
ALA C    C  N N 27  
ALA O    O  N N 28  
ALA CB   C  N N 29  
ALA OXT  O  N N 30  
ALA H    H  N N 31  
ALA H2   H  N N 32  
ALA HA   H  N N 33  
ALA HB1  H  N N 34  
ALA HB2  H  N N 35  
ALA HB3  H  N N 36  
ALA HXT  H  N N 37  
ARG N    N  N N 38  
ARG CA   C  N S 39  
ARG C    C  N N 40  
ARG O    O  N N 41  
ARG CB   C  N N 42  
ARG CG   C  N N 43  
ARG CD   C  N N 44  
ARG NE   N  N N 45  
ARG CZ   C  N N 46  
ARG NH1  N  N N 47  
ARG NH2  N  N N 48  
ARG OXT  O  N N 49  
ARG H    H  N N 50  
ARG H2   H  N N 51  
ARG HA   H  N N 52  
ARG HB2  H  N N 53  
ARG HB3  H  N N 54  
ARG HG2  H  N N 55  
ARG HG3  H  N N 56  
ARG HD2  H  N N 57  
ARG HD3  H  N N 58  
ARG HE   H  N N 59  
ARG HH11 H  N N 60  
ARG HH12 H  N N 61  
ARG HH21 H  N N 62  
ARG HH22 H  N N 63  
ARG HXT  H  N N 64  
ASN N    N  N N 65  
ASN CA   C  N S 66  
ASN C    C  N N 67  
ASN O    O  N N 68  
ASN CB   C  N N 69  
ASN CG   C  N N 70  
ASN OD1  O  N N 71  
ASN ND2  N  N N 72  
ASN OXT  O  N N 73  
ASN H    H  N N 74  
ASN H2   H  N N 75  
ASN HA   H  N N 76  
ASN HB2  H  N N 77  
ASN HB3  H  N N 78  
ASN HD21 H  N N 79  
ASN HD22 H  N N 80  
ASN HXT  H  N N 81  
ASP N    N  N N 82  
ASP CA   C  N S 83  
ASP C    C  N N 84  
ASP O    O  N N 85  
ASP CB   C  N N 86  
ASP CG   C  N N 87  
ASP OD1  O  N N 88  
ASP OD2  O  N N 89  
ASP OXT  O  N N 90  
ASP H    H  N N 91  
ASP H2   H  N N 92  
ASP HA   H  N N 93  
ASP HB2  H  N N 94  
ASP HB3  H  N N 95  
ASP HD2  H  N N 96  
ASP HXT  H  N N 97  
CL  CL   CL N N 98  
CYS N    N  N N 99  
CYS CA   C  N R 100 
CYS C    C  N N 101 
CYS O    O  N N 102 
CYS CB   C  N N 103 
CYS SG   S  N N 104 
CYS OXT  O  N N 105 
CYS H    H  N N 106 
CYS H2   H  N N 107 
CYS HA   H  N N 108 
CYS HB2  H  N N 109 
CYS HB3  H  N N 110 
CYS HG   H  N N 111 
CYS HXT  H  N N 112 
EL5 C1A  C  N N 113 
EL5 C1B  C  N N 114 
EL5 O1B  O  N N 115 
EL5 C1C  C  Y N 116 
EL5 O1C  O  N N 117 
EL5 C1D  C  N N 118 
EL5 C2A  C  N S 119 
EL5 C2B  C  N N 120 
EL5 O2B  O  N N 121 
EL5 C2C  C  Y N 122 
EL5 O2C  O  N N 123 
EL5 C2D  C  N N 124 
EL5 C3A  C  N N 125 
EL5 C3B  C  N N 126 
EL5 C3C  C  Y N 127 
EL5 C3D  C  N N 128 
EL5 C4A  C  N N 129 
EL5 C4B  C  N N 130 
EL5 C4C  C  Y N 131 
EL5 C4D  C  N N 132 
EL5 CAA  C  N N 133 
EL5 CAB  C  N N 134 
EL5 CAC  C  N N 135 
EL5 CAD  C  N N 136 
EL5 CBA  C  N N 137 
EL5 CBB  C  N N 138 
EL5 CBC  C  N N 139 
EL5 CBD  C  N N 140 
EL5 CGB  C  N N 141 
EL5 CGC  C  N N 142 
EL5 CHB  C  N N 143 
EL5 CHC  C  N N 144 
EL5 CHD  C  N N 145 
EL5 CMA  C  N N 146 
EL5 CMB  C  N N 147 
EL5 CMC  C  N N 148 
EL5 CMD  C  N N 149 
EL5 NA   N  N N 150 
EL5 OA   O  N N 151 
EL5 NB   N  N N 152 
EL5 NC   N  Y N 153 
EL5 ND   N  N N 154 
EL5 OD   O  N N 155 
EL5 H1   H  N N 156 
EL5 H2   H  N N 157 
EL5 H3   H  N N 158 
EL5 H4   H  N N 159 
EL5 H6   H  N N 160 
EL5 H7   H  N N 161 
EL5 H8   H  N N 162 
EL5 H9   H  N N 163 
EL5 H10  H  N N 164 
EL5 H12  H  N N 165 
EL5 H13  H  N N 166 
EL5 H14  H  N N 167 
EL5 H15  H  N N 168 
EL5 H16  H  N N 169 
EL5 H17  H  N N 170 
EL5 H18  H  N N 171 
EL5 H19  H  N N 172 
EL5 H20  H  N N 173 
EL5 H22  H  N N 174 
EL5 H24  H  N N 175 
EL5 H26  H  N N 176 
EL5 H28  H  N N 177 
EL5 H29  H  N N 178 
EL5 H30  H  N N 179 
EL5 H31  H  N N 180 
EL5 H32  H  N N 181 
EL5 H33  H  N N 182 
EL5 H34  H  N N 183 
EL5 H35  H  N N 184 
EL5 H36  H  N N 185 
EL5 H37  H  N N 186 
EL5 H38  H  N N 187 
EL5 H39  H  N N 188 
EL5 H40  H  N N 189 
EL5 H42  H  N N 190 
EL5 H5   H  N N 191 
GLN N    N  N N 192 
GLN CA   C  N S 193 
GLN C    C  N N 194 
GLN O    O  N N 195 
GLN CB   C  N N 196 
GLN CG   C  N N 197 
GLN CD   C  N N 198 
GLN OE1  O  N N 199 
GLN NE2  N  N N 200 
GLN OXT  O  N N 201 
GLN H    H  N N 202 
GLN H2   H  N N 203 
GLN HA   H  N N 204 
GLN HB2  H  N N 205 
GLN HB3  H  N N 206 
GLN HG2  H  N N 207 
GLN HG3  H  N N 208 
GLN HE21 H  N N 209 
GLN HE22 H  N N 210 
GLN HXT  H  N N 211 
GLU N    N  N N 212 
GLU CA   C  N S 213 
GLU C    C  N N 214 
GLU O    O  N N 215 
GLU CB   C  N N 216 
GLU CG   C  N N 217 
GLU CD   C  N N 218 
GLU OE1  O  N N 219 
GLU OE2  O  N N 220 
GLU OXT  O  N N 221 
GLU H    H  N N 222 
GLU H2   H  N N 223 
GLU HA   H  N N 224 
GLU HB2  H  N N 225 
GLU HB3  H  N N 226 
GLU HG2  H  N N 227 
GLU HG3  H  N N 228 
GLU HE2  H  N N 229 
GLU HXT  H  N N 230 
GLY N    N  N N 231 
GLY CA   C  N N 232 
GLY C    C  N N 233 
GLY O    O  N N 234 
GLY OXT  O  N N 235 
GLY H    H  N N 236 
GLY H2   H  N N 237 
GLY HA2  H  N N 238 
GLY HA3  H  N N 239 
GLY HXT  H  N N 240 
HIS N    N  N N 241 
HIS CA   C  N S 242 
HIS C    C  N N 243 
HIS O    O  N N 244 
HIS CB   C  N N 245 
HIS CG   C  Y N 246 
HIS ND1  N  Y N 247 
HIS CD2  C  Y N 248 
HIS CE1  C  Y N 249 
HIS NE2  N  Y N 250 
HIS OXT  O  N N 251 
HIS H    H  N N 252 
HIS H2   H  N N 253 
HIS HA   H  N N 254 
HIS HB2  H  N N 255 
HIS HB3  H  N N 256 
HIS HD1  H  N N 257 
HIS HD2  H  N N 258 
HIS HE1  H  N N 259 
HIS HE2  H  N N 260 
HIS HXT  H  N N 261 
HOH O    O  N N 262 
HOH H1   H  N N 263 
HOH H2   H  N N 264 
ILE N    N  N N 265 
ILE CA   C  N S 266 
ILE C    C  N N 267 
ILE O    O  N N 268 
ILE CB   C  N S 269 
ILE CG1  C  N N 270 
ILE CG2  C  N N 271 
ILE CD1  C  N N 272 
ILE OXT  O  N N 273 
ILE H    H  N N 274 
ILE H2   H  N N 275 
ILE HA   H  N N 276 
ILE HB   H  N N 277 
ILE HG12 H  N N 278 
ILE HG13 H  N N 279 
ILE HG21 H  N N 280 
ILE HG22 H  N N 281 
ILE HG23 H  N N 282 
ILE HD11 H  N N 283 
ILE HD12 H  N N 284 
ILE HD13 H  N N 285 
ILE HXT  H  N N 286 
LEU N    N  N N 287 
LEU CA   C  N S 288 
LEU C    C  N N 289 
LEU O    O  N N 290 
LEU CB   C  N N 291 
LEU CG   C  N N 292 
LEU CD1  C  N N 293 
LEU CD2  C  N N 294 
LEU OXT  O  N N 295 
LEU H    H  N N 296 
LEU H2   H  N N 297 
LEU HA   H  N N 298 
LEU HB2  H  N N 299 
LEU HB3  H  N N 300 
LEU HG   H  N N 301 
LEU HD11 H  N N 302 
LEU HD12 H  N N 303 
LEU HD13 H  N N 304 
LEU HD21 H  N N 305 
LEU HD22 H  N N 306 
LEU HD23 H  N N 307 
LEU HXT  H  N N 308 
LYS N    N  N N 309 
LYS CA   C  N S 310 
LYS C    C  N N 311 
LYS O    O  N N 312 
LYS CB   C  N N 313 
LYS CG   C  N N 314 
LYS CD   C  N N 315 
LYS CE   C  N N 316 
LYS NZ   N  N N 317 
LYS OXT  O  N N 318 
LYS H    H  N N 319 
LYS H2   H  N N 320 
LYS HA   H  N N 321 
LYS HB2  H  N N 322 
LYS HB3  H  N N 323 
LYS HG2  H  N N 324 
LYS HG3  H  N N 325 
LYS HD2  H  N N 326 
LYS HD3  H  N N 327 
LYS HE2  H  N N 328 
LYS HE3  H  N N 329 
LYS HZ1  H  N N 330 
LYS HZ2  H  N N 331 
LYS HZ3  H  N N 332 
LYS HXT  H  N N 333 
MET N    N  N N 334 
MET CA   C  N S 335 
MET C    C  N N 336 
MET O    O  N N 337 
MET CB   C  N N 338 
MET CG   C  N N 339 
MET SD   S  N N 340 
MET CE   C  N N 341 
MET OXT  O  N N 342 
MET H    H  N N 343 
MET H2   H  N N 344 
MET HA   H  N N 345 
MET HB2  H  N N 346 
MET HB3  H  N N 347 
MET HG2  H  N N 348 
MET HG3  H  N N 349 
MET HE1  H  N N 350 
MET HE2  H  N N 351 
MET HE3  H  N N 352 
MET HXT  H  N N 353 
MLZ N    N  N N 354 
MLZ CA   C  N S 355 
MLZ CB   C  N N 356 
MLZ CG   C  N N 357 
MLZ CD   C  N N 358 
MLZ CE   C  N N 359 
MLZ NZ   N  N N 360 
MLZ CM   C  N N 361 
MLZ C    C  N N 362 
MLZ O    O  N N 363 
MLZ OXT  O  N N 364 
MLZ H    H  N N 365 
MLZ H2   H  N N 366 
MLZ HA   H  N N 367 
MLZ HB2  H  N N 368 
MLZ HB3  H  N N 369 
MLZ HG2  H  N N 370 
MLZ HG3  H  N N 371 
MLZ HD2  H  N N 372 
MLZ HD3  H  N N 373 
MLZ HE2  H  N N 374 
MLZ HE3  H  N N 375 
MLZ HZ   H  N N 376 
MLZ HCM1 H  N N 377 
MLZ HCM2 H  N N 378 
MLZ HCM3 H  N N 379 
MLZ HXT  H  N N 380 
MPD C1   C  N N 381 
MPD C2   C  N N 382 
MPD O2   O  N N 383 
MPD CM   C  N N 384 
MPD C3   C  N N 385 
MPD C4   C  N S 386 
MPD O4   O  N N 387 
MPD C5   C  N N 388 
MPD H11  H  N N 389 
MPD H12  H  N N 390 
MPD H13  H  N N 391 
MPD HO2  H  N N 392 
MPD HM1  H  N N 393 
MPD HM2  H  N N 394 
MPD HM3  H  N N 395 
MPD H31  H  N N 396 
MPD H32  H  N N 397 
MPD H4   H  N N 398 
MPD HO4  H  N N 399 
MPD H51  H  N N 400 
MPD H52  H  N N 401 
MPD H53  H  N N 402 
PEG C1   C  N N 403 
PEG O1   O  N N 404 
PEG C2   C  N N 405 
PEG O2   O  N N 406 
PEG C3   C  N N 407 
PEG C4   C  N N 408 
PEG O4   O  N N 409 
PEG H11  H  N N 410 
PEG H12  H  N N 411 
PEG HO1  H  N N 412 
PEG H21  H  N N 413 
PEG H22  H  N N 414 
PEG H31  H  N N 415 
PEG H32  H  N N 416 
PEG H41  H  N N 417 
PEG H42  H  N N 418 
PEG HO4  H  N N 419 
PHE N    N  N N 420 
PHE CA   C  N S 421 
PHE C    C  N N 422 
PHE O    O  N N 423 
PHE CB   C  N N 424 
PHE CG   C  Y N 425 
PHE CD1  C  Y N 426 
PHE CD2  C  Y N 427 
PHE CE1  C  Y N 428 
PHE CE2  C  Y N 429 
PHE CZ   C  Y N 430 
PHE OXT  O  N N 431 
PHE H    H  N N 432 
PHE H2   H  N N 433 
PHE HA   H  N N 434 
PHE HB2  H  N N 435 
PHE HB3  H  N N 436 
PHE HD1  H  N N 437 
PHE HD2  H  N N 438 
PHE HE1  H  N N 439 
PHE HE2  H  N N 440 
PHE HZ   H  N N 441 
PHE HXT  H  N N 442 
PRO N    N  N N 443 
PRO CA   C  N S 444 
PRO C    C  N N 445 
PRO O    O  N N 446 
PRO CB   C  N N 447 
PRO CG   C  N N 448 
PRO CD   C  N N 449 
PRO OXT  O  N N 450 
PRO H    H  N N 451 
PRO HA   H  N N 452 
PRO HB2  H  N N 453 
PRO HB3  H  N N 454 
PRO HG2  H  N N 455 
PRO HG3  H  N N 456 
PRO HD2  H  N N 457 
PRO HD3  H  N N 458 
PRO HXT  H  N N 459 
SER N    N  N N 460 
SER CA   C  N S 461 
SER C    C  N N 462 
SER O    O  N N 463 
SER CB   C  N N 464 
SER OG   O  N N 465 
SER OXT  O  N N 466 
SER H    H  N N 467 
SER H2   H  N N 468 
SER HA   H  N N 469 
SER HB2  H  N N 470 
SER HB3  H  N N 471 
SER HG   H  N N 472 
SER HXT  H  N N 473 
THR N    N  N N 474 
THR CA   C  N S 475 
THR C    C  N N 476 
THR O    O  N N 477 
THR CB   C  N R 478 
THR OG1  O  N N 479 
THR CG2  C  N N 480 
THR OXT  O  N N 481 
THR H    H  N N 482 
THR H2   H  N N 483 
THR HA   H  N N 484 
THR HB   H  N N 485 
THR HG1  H  N N 486 
THR HG21 H  N N 487 
THR HG22 H  N N 488 
THR HG23 H  N N 489 
THR HXT  H  N N 490 
TRP N    N  N N 491 
TRP CA   C  N S 492 
TRP C    C  N N 493 
TRP O    O  N N 494 
TRP CB   C  N N 495 
TRP CG   C  Y N 496 
TRP CD1  C  Y N 497 
TRP CD2  C  Y N 498 
TRP NE1  N  Y N 499 
TRP CE2  C  Y N 500 
TRP CE3  C  Y N 501 
TRP CZ2  C  Y N 502 
TRP CZ3  C  Y N 503 
TRP CH2  C  Y N 504 
TRP OXT  O  N N 505 
TRP H    H  N N 506 
TRP H2   H  N N 507 
TRP HA   H  N N 508 
TRP HB2  H  N N 509 
TRP HB3  H  N N 510 
TRP HD1  H  N N 511 
TRP HE1  H  N N 512 
TRP HE3  H  N N 513 
TRP HZ2  H  N N 514 
TRP HZ3  H  N N 515 
TRP HH2  H  N N 516 
TRP HXT  H  N N 517 
TYR N    N  N N 518 
TYR CA   C  N S 519 
TYR C    C  N N 520 
TYR O    O  N N 521 
TYR CB   C  N N 522 
TYR CG   C  Y N 523 
TYR CD1  C  Y N 524 
TYR CD2  C  Y N 525 
TYR CE1  C  Y N 526 
TYR CE2  C  Y N 527 
TYR CZ   C  Y N 528 
TYR OH   O  N N 529 
TYR OXT  O  N N 530 
TYR H    H  N N 531 
TYR H2   H  N N 532 
TYR HA   H  N N 533 
TYR HB2  H  N N 534 
TYR HB3  H  N N 535 
TYR HD1  H  N N 536 
TYR HD2  H  N N 537 
TYR HE1  H  N N 538 
TYR HE2  H  N N 539 
TYR HH   H  N N 540 
TYR HXT  H  N N 541 
VAL N    N  N N 542 
VAL CA   C  N S 543 
VAL C    C  N N 544 
VAL O    O  N N 545 
VAL CB   C  N N 546 
VAL CG1  C  N N 547 
VAL CG2  C  N N 548 
VAL OXT  O  N N 549 
VAL H    H  N N 550 
VAL H2   H  N N 551 
VAL HA   H  N N 552 
VAL HB   H  N N 553 
VAL HG11 H  N N 554 
VAL HG12 H  N N 555 
VAL HG13 H  N N 556 
VAL HG21 H  N N 557 
VAL HG22 H  N N 558 
VAL HG23 H  N N 559 
VAL HXT  H  N N 560 
# 
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 
9IJ C   O    doub N N 1   
9IJ C   CA   sing N N 2   
9IJ CA  CB   sing N N 3   
9IJ CA  N    sing N N 4   
9IJ CB  CG   sing N N 5   
9IJ CG  CD1  doub Y N 6   
9IJ CG  CD2  sing Y N 7   
9IJ CD1 CE1  sing Y N 8   
9IJ N01 C01  trip N N 9   
9IJ C01 CD2  sing N N 10  
9IJ CD2 CE2  doub Y N 11  
9IJ CE1 CZ   doub Y N 12  
9IJ CE2 CZ   sing Y N 13  
9IJ N   H    sing N N 14  
9IJ N   H2   sing N N 15  
9IJ CA  HA   sing N N 16  
9IJ CB  HB2  sing N N 17  
9IJ CB  HB3  sing N N 18  
9IJ CD1 HD1  sing N N 19  
9IJ CE1 HE1  sing N N 20  
9IJ CE2 HE2  sing N N 21  
9IJ CZ  HZ   sing N N 22  
9IJ C   OXT  sing N N 23  
9IJ OXT HXT  sing N N 24  
ALA N   CA   sing N N 25  
ALA N   H    sing N N 26  
ALA N   H2   sing N N 27  
ALA CA  C    sing N N 28  
ALA CA  CB   sing N N 29  
ALA CA  HA   sing N N 30  
ALA C   O    doub N N 31  
ALA C   OXT  sing N N 32  
ALA CB  HB1  sing N N 33  
ALA CB  HB2  sing N N 34  
ALA CB  HB3  sing N N 35  
ALA OXT HXT  sing N N 36  
ARG N   CA   sing N N 37  
ARG N   H    sing N N 38  
ARG N   H2   sing N N 39  
ARG CA  C    sing N N 40  
ARG CA  CB   sing N N 41  
ARG CA  HA   sing N N 42  
ARG C   O    doub N N 43  
ARG C   OXT  sing N N 44  
ARG CB  CG   sing N N 45  
ARG CB  HB2  sing N N 46  
ARG CB  HB3  sing N N 47  
ARG CG  CD   sing N N 48  
ARG CG  HG2  sing N N 49  
ARG CG  HG3  sing N N 50  
ARG CD  NE   sing N N 51  
ARG CD  HD2  sing N N 52  
ARG CD  HD3  sing N N 53  
ARG NE  CZ   sing N N 54  
ARG NE  HE   sing N N 55  
ARG CZ  NH1  sing N N 56  
ARG CZ  NH2  doub N N 57  
ARG NH1 HH11 sing N N 58  
ARG NH1 HH12 sing N N 59  
ARG NH2 HH21 sing N N 60  
ARG NH2 HH22 sing N N 61  
ARG OXT HXT  sing N N 62  
ASN N   CA   sing N N 63  
ASN N   H    sing N N 64  
ASN N   H2   sing N N 65  
ASN CA  C    sing N N 66  
ASN CA  CB   sing N N 67  
ASN CA  HA   sing N N 68  
ASN C   O    doub N N 69  
ASN C   OXT  sing N N 70  
ASN CB  CG   sing N N 71  
ASN CB  HB2  sing N N 72  
ASN CB  HB3  sing N N 73  
ASN CG  OD1  doub N N 74  
ASN CG  ND2  sing N N 75  
ASN ND2 HD21 sing N N 76  
ASN ND2 HD22 sing N N 77  
ASN OXT HXT  sing N N 78  
ASP N   CA   sing N N 79  
ASP N   H    sing N N 80  
ASP N   H2   sing N N 81  
ASP CA  C    sing N N 82  
ASP CA  CB   sing N N 83  
ASP CA  HA   sing N N 84  
ASP C   O    doub N N 85  
ASP C   OXT  sing N N 86  
ASP CB  CG   sing N N 87  
ASP CB  HB2  sing N N 88  
ASP CB  HB3  sing N N 89  
ASP CG  OD1  doub N N 90  
ASP CG  OD2  sing N N 91  
ASP OD2 HD2  sing N N 92  
ASP OXT HXT  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
EL5 OD  C4D  doub N N 107 
EL5 ND  C4D  sing N N 108 
EL5 ND  C1D  sing N N 109 
EL5 CMA C2A  sing N N 110 
EL5 CBA CAA  sing N N 111 
EL5 C4D C3D  sing N N 112 
EL5 C2A C1A  sing N N 113 
EL5 C2A C3A  sing N N 114 
EL5 OA  C1A  doub N N 115 
EL5 CBD CAD  doub N N 116 
EL5 CAA C3A  doub N E 117 
EL5 C1A NA   sing N N 118 
EL5 CHD C1D  doub N E 119 
EL5 CHD C4C  sing N N 120 
EL5 C3A C4A  sing N N 121 
EL5 C1D C2D  sing N N 122 
EL5 C3D CAD  sing N N 123 
EL5 C3D C2D  doub N N 124 
EL5 CMC C3C  sing N N 125 
EL5 NA  C4A  sing N N 126 
EL5 C4A CHB  doub N Z 127 
EL5 C4C C3C  doub Y N 128 
EL5 C4C NC   sing Y N 129 
EL5 C2D CMD  sing N N 130 
EL5 C3C C2C  sing Y N 131 
EL5 NC  C1C  sing Y N 132 
EL5 CHB C1B  sing N N 133 
EL5 C2C C1C  doub Y N 134 
EL5 C2C CAC  sing N N 135 
EL5 NB  C1B  doub N N 136 
EL5 NB  C4B  sing N N 137 
EL5 C1C CHC  sing N N 138 
EL5 C1B C2B  sing N N 139 
EL5 CAC CBC  sing N N 140 
EL5 C4B CHC  doub N Z 141 
EL5 C4B C3B  sing N N 142 
EL5 C2B C3B  doub N N 143 
EL5 C2B CMB  sing N N 144 
EL5 O1C CGC  doub N N 145 
EL5 C3B CAB  sing N N 146 
EL5 CBC CGC  sing N N 147 
EL5 CGC O2C  sing N N 148 
EL5 CAB CBB  sing N N 149 
EL5 CBB CGB  sing N N 150 
EL5 CGB O2B  doub N N 151 
EL5 CGB O1B  sing N N 152 
EL5 O1B H1   sing N N 153 
EL5 C2A H2   sing N N 154 
EL5 O2C H3   sing N N 155 
EL5 CAA H4   sing N N 156 
EL5 CAB H6   sing N N 157 
EL5 CAB H7   sing N N 158 
EL5 CAC H8   sing N N 159 
EL5 CAC H9   sing N N 160 
EL5 CAD H10  sing N N 161 
EL5 CBA H12  sing N N 162 
EL5 CBA H13  sing N N 163 
EL5 CBA H14  sing N N 164 
EL5 CBB H15  sing N N 165 
EL5 CBB H16  sing N N 166 
EL5 CBC H17  sing N N 167 
EL5 CBC H18  sing N N 168 
EL5 CBD H19  sing N N 169 
EL5 CBD H20  sing N N 170 
EL5 CHB H22  sing N N 171 
EL5 CHC H24  sing N N 172 
EL5 CHD H26  sing N N 173 
EL5 CMA H28  sing N N 174 
EL5 CMA H29  sing N N 175 
EL5 CMA H30  sing N N 176 
EL5 CMB H31  sing N N 177 
EL5 CMB H32  sing N N 178 
EL5 CMB H33  sing N N 179 
EL5 CMC H34  sing N N 180 
EL5 CMC H35  sing N N 181 
EL5 CMC H36  sing N N 182 
EL5 CMD H37  sing N N 183 
EL5 CMD H38  sing N N 184 
EL5 CMD H39  sing N N 185 
EL5 NA  H40  sing N N 186 
EL5 NC  H42  sing N N 187 
EL5 ND  H5   sing N N 188 
GLN N   CA   sing N N 189 
GLN N   H    sing N N 190 
GLN N   H2   sing N N 191 
GLN CA  C    sing N N 192 
GLN CA  CB   sing N N 193 
GLN CA  HA   sing N N 194 
GLN C   O    doub N N 195 
GLN C   OXT  sing N N 196 
GLN CB  CG   sing N N 197 
GLN CB  HB2  sing N N 198 
GLN CB  HB3  sing N N 199 
GLN CG  CD   sing N N 200 
GLN CG  HG2  sing N N 201 
GLN CG  HG3  sing N N 202 
GLN CD  OE1  doub N N 203 
GLN CD  NE2  sing N N 204 
GLN NE2 HE21 sing N N 205 
GLN NE2 HE22 sing N N 206 
GLN OXT HXT  sing N N 207 
GLU N   CA   sing N N 208 
GLU N   H    sing N N 209 
GLU N   H2   sing N N 210 
GLU CA  C    sing N N 211 
GLU CA  CB   sing N N 212 
GLU CA  HA   sing N N 213 
GLU C   O    doub N N 214 
GLU C   OXT  sing N N 215 
GLU CB  CG   sing N N 216 
GLU CB  HB2  sing N N 217 
GLU CB  HB3  sing N N 218 
GLU CG  CD   sing N N 219 
GLU CG  HG2  sing N N 220 
GLU CG  HG3  sing N N 221 
GLU CD  OE1  doub N N 222 
GLU CD  OE2  sing N N 223 
GLU OE2 HE2  sing N N 224 
GLU OXT HXT  sing N N 225 
GLY N   CA   sing N N 226 
GLY N   H    sing N N 227 
GLY N   H2   sing N N 228 
GLY CA  C    sing N N 229 
GLY CA  HA2  sing N N 230 
GLY CA  HA3  sing N N 231 
GLY C   O    doub N N 232 
GLY C   OXT  sing N N 233 
GLY OXT HXT  sing N N 234 
HIS N   CA   sing N N 235 
HIS N   H    sing N N 236 
HIS N   H2   sing N N 237 
HIS CA  C    sing N N 238 
HIS CA  CB   sing N N 239 
HIS CA  HA   sing N N 240 
HIS C   O    doub N N 241 
HIS C   OXT  sing N N 242 
HIS CB  CG   sing N N 243 
HIS CB  HB2  sing N N 244 
HIS CB  HB3  sing N N 245 
HIS CG  ND1  sing Y N 246 
HIS CG  CD2  doub Y N 247 
HIS ND1 CE1  doub Y N 248 
HIS ND1 HD1  sing N N 249 
HIS CD2 NE2  sing Y N 250 
HIS CD2 HD2  sing N N 251 
HIS CE1 NE2  sing Y N 252 
HIS CE1 HE1  sing N N 253 
HIS NE2 HE2  sing N N 254 
HIS OXT HXT  sing N N 255 
HOH O   H1   sing N N 256 
HOH O   H2   sing N N 257 
ILE N   CA   sing N N 258 
ILE N   H    sing N N 259 
ILE N   H2   sing N N 260 
ILE CA  C    sing N N 261 
ILE CA  CB   sing N N 262 
ILE CA  HA   sing N N 263 
ILE C   O    doub N N 264 
ILE C   OXT  sing N N 265 
ILE CB  CG1  sing N N 266 
ILE CB  CG2  sing N N 267 
ILE CB  HB   sing N N 268 
ILE CG1 CD1  sing N N 269 
ILE CG1 HG12 sing N N 270 
ILE CG1 HG13 sing N N 271 
ILE CG2 HG21 sing N N 272 
ILE CG2 HG22 sing N N 273 
ILE CG2 HG23 sing N N 274 
ILE CD1 HD11 sing N N 275 
ILE CD1 HD12 sing N N 276 
ILE CD1 HD13 sing N N 277 
ILE OXT HXT  sing N N 278 
LEU N   CA   sing N N 279 
LEU N   H    sing N N 280 
LEU N   H2   sing N N 281 
LEU CA  C    sing N N 282 
LEU CA  CB   sing N N 283 
LEU CA  HA   sing N N 284 
LEU C   O    doub N N 285 
LEU C   OXT  sing N N 286 
LEU CB  CG   sing N N 287 
LEU CB  HB2  sing N N 288 
LEU CB  HB3  sing N N 289 
LEU CG  CD1  sing N N 290 
LEU CG  CD2  sing N N 291 
LEU CG  HG   sing N N 292 
LEU CD1 HD11 sing N N 293 
LEU CD1 HD12 sing N N 294 
LEU CD1 HD13 sing N N 295 
LEU CD2 HD21 sing N N 296 
LEU CD2 HD22 sing N N 297 
LEU CD2 HD23 sing N N 298 
LEU OXT HXT  sing N N 299 
LYS N   CA   sing N N 300 
LYS N   H    sing N N 301 
LYS N   H2   sing N N 302 
LYS CA  C    sing N N 303 
LYS CA  CB   sing N N 304 
LYS CA  HA   sing N N 305 
LYS C   O    doub N N 306 
LYS C   OXT  sing N N 307 
LYS CB  CG   sing N N 308 
LYS CB  HB2  sing N N 309 
LYS CB  HB3  sing N N 310 
LYS CG  CD   sing N N 311 
LYS CG  HG2  sing N N 312 
LYS CG  HG3  sing N N 313 
LYS CD  CE   sing N N 314 
LYS CD  HD2  sing N N 315 
LYS CD  HD3  sing N N 316 
LYS CE  NZ   sing N N 317 
LYS CE  HE2  sing N N 318 
LYS CE  HE3  sing N N 319 
LYS NZ  HZ1  sing N N 320 
LYS NZ  HZ2  sing N N 321 
LYS NZ  HZ3  sing N N 322 
LYS OXT HXT  sing N N 323 
MET N   CA   sing N N 324 
MET N   H    sing N N 325 
MET N   H2   sing N N 326 
MET CA  C    sing N N 327 
MET CA  CB   sing N N 328 
MET CA  HA   sing N N 329 
MET C   O    doub N N 330 
MET C   OXT  sing N N 331 
MET CB  CG   sing N N 332 
MET CB  HB2  sing N N 333 
MET CB  HB3  sing N N 334 
MET CG  SD   sing N N 335 
MET CG  HG2  sing N N 336 
MET CG  HG3  sing N N 337 
MET SD  CE   sing N N 338 
MET CE  HE1  sing N N 339 
MET CE  HE2  sing N N 340 
MET CE  HE3  sing N N 341 
MET OXT HXT  sing N N 342 
MLZ N   CA   sing N N 343 
MLZ N   H    sing N N 344 
MLZ N   H2   sing N N 345 
MLZ CA  CB   sing N N 346 
MLZ CA  C    sing N N 347 
MLZ CA  HA   sing N N 348 
MLZ CB  CG   sing N N 349 
MLZ CB  HB2  sing N N 350 
MLZ CB  HB3  sing N N 351 
MLZ CG  CD   sing N N 352 
MLZ CG  HG2  sing N N 353 
MLZ CG  HG3  sing N N 354 
MLZ CD  CE   sing N N 355 
MLZ CD  HD2  sing N N 356 
MLZ CD  HD3  sing N N 357 
MLZ CE  NZ   sing N N 358 
MLZ CE  HE2  sing N N 359 
MLZ CE  HE3  sing N N 360 
MLZ NZ  CM   sing N N 361 
MLZ NZ  HZ   sing N N 362 
MLZ CM  HCM1 sing N N 363 
MLZ CM  HCM2 sing N N 364 
MLZ CM  HCM3 sing N N 365 
MLZ C   O    doub N N 366 
MLZ C   OXT  sing N N 367 
MLZ OXT HXT  sing N N 368 
MPD C1  C2   sing N N 369 
MPD C1  H11  sing N N 370 
MPD C1  H12  sing N N 371 
MPD C1  H13  sing N N 372 
MPD C2  O2   sing N N 373 
MPD C2  CM   sing N N 374 
MPD C2  C3   sing N N 375 
MPD O2  HO2  sing N N 376 
MPD CM  HM1  sing N N 377 
MPD CM  HM2  sing N N 378 
MPD CM  HM3  sing N N 379 
MPD C3  C4   sing N N 380 
MPD C3  H31  sing N N 381 
MPD C3  H32  sing N N 382 
MPD C4  O4   sing N N 383 
MPD C4  C5   sing N N 384 
MPD C4  H4   sing N N 385 
MPD O4  HO4  sing N N 386 
MPD C5  H51  sing N N 387 
MPD C5  H52  sing N N 388 
MPD C5  H53  sing N N 389 
PEG C1  O1   sing N N 390 
PEG C1  C2   sing N N 391 
PEG C1  H11  sing N N 392 
PEG C1  H12  sing N N 393 
PEG O1  HO1  sing N N 394 
PEG C2  O2   sing N N 395 
PEG C2  H21  sing N N 396 
PEG C2  H22  sing N N 397 
PEG O2  C3   sing N N 398 
PEG C3  C4   sing N N 399 
PEG C3  H31  sing N N 400 
PEG C3  H32  sing N N 401 
PEG C4  O4   sing N N 402 
PEG C4  H41  sing N N 403 
PEG C4  H42  sing N N 404 
PEG O4  HO4  sing N N 405 
PHE N   CA   sing N N 406 
PHE N   H    sing N N 407 
PHE N   H2   sing N N 408 
PHE CA  C    sing N N 409 
PHE CA  CB   sing N N 410 
PHE CA  HA   sing N N 411 
PHE C   O    doub N N 412 
PHE C   OXT  sing N N 413 
PHE CB  CG   sing N N 414 
PHE CB  HB2  sing N N 415 
PHE CB  HB3  sing N N 416 
PHE CG  CD1  doub Y N 417 
PHE CG  CD2  sing Y N 418 
PHE CD1 CE1  sing Y N 419 
PHE CD1 HD1  sing N N 420 
PHE CD2 CE2  doub Y N 421 
PHE CD2 HD2  sing N N 422 
PHE CE1 CZ   doub Y N 423 
PHE CE1 HE1  sing N N 424 
PHE CE2 CZ   sing Y N 425 
PHE CE2 HE2  sing N N 426 
PHE CZ  HZ   sing N N 427 
PHE OXT HXT  sing N N 428 
PRO N   CA   sing N N 429 
PRO N   CD   sing N N 430 
PRO N   H    sing N N 431 
PRO CA  C    sing N N 432 
PRO CA  CB   sing N N 433 
PRO CA  HA   sing N N 434 
PRO C   O    doub N N 435 
PRO C   OXT  sing N N 436 
PRO CB  CG   sing N N 437 
PRO CB  HB2  sing N N 438 
PRO CB  HB3  sing N N 439 
PRO CG  CD   sing N N 440 
PRO CG  HG2  sing N N 441 
PRO CG  HG3  sing N N 442 
PRO CD  HD2  sing N N 443 
PRO CD  HD3  sing N N 444 
PRO OXT HXT  sing N N 445 
SER N   CA   sing N N 446 
SER N   H    sing N N 447 
SER N   H2   sing N N 448 
SER CA  C    sing N N 449 
SER CA  CB   sing N N 450 
SER CA  HA   sing N N 451 
SER C   O    doub N N 452 
SER C   OXT  sing N N 453 
SER CB  OG   sing N N 454 
SER CB  HB2  sing N N 455 
SER CB  HB3  sing N N 456 
SER OG  HG   sing N N 457 
SER OXT HXT  sing N N 458 
THR N   CA   sing N N 459 
THR N   H    sing N N 460 
THR N   H2   sing N N 461 
THR CA  C    sing N N 462 
THR CA  CB   sing N N 463 
THR CA  HA   sing N N 464 
THR C   O    doub N N 465 
THR C   OXT  sing N N 466 
THR CB  OG1  sing N N 467 
THR CB  CG2  sing N N 468 
THR CB  HB   sing N N 469 
THR OG1 HG1  sing N N 470 
THR CG2 HG21 sing N N 471 
THR CG2 HG22 sing N N 472 
THR CG2 HG23 sing N N 473 
THR OXT HXT  sing N N 474 
TRP N   CA   sing N N 475 
TRP N   H    sing N N 476 
TRP N   H2   sing N N 477 
TRP CA  C    sing N N 478 
TRP CA  CB   sing N N 479 
TRP CA  HA   sing N N 480 
TRP C   O    doub N N 481 
TRP C   OXT  sing N N 482 
TRP CB  CG   sing N N 483 
TRP CB  HB2  sing N N 484 
TRP CB  HB3  sing N N 485 
TRP CG  CD1  doub Y N 486 
TRP CG  CD2  sing Y N 487 
TRP CD1 NE1  sing Y N 488 
TRP CD1 HD1  sing N N 489 
TRP CD2 CE2  doub Y N 490 
TRP CD2 CE3  sing Y N 491 
TRP NE1 CE2  sing Y N 492 
TRP NE1 HE1  sing N N 493 
TRP CE2 CZ2  sing Y N 494 
TRP CE3 CZ3  doub Y N 495 
TRP CE3 HE3  sing N N 496 
TRP CZ2 CH2  doub Y N 497 
TRP CZ2 HZ2  sing N N 498 
TRP CZ3 CH2  sing Y N 499 
TRP CZ3 HZ3  sing N N 500 
TRP CH2 HH2  sing N N 501 
TRP OXT HXT  sing N N 502 
TYR N   CA   sing N N 503 
TYR N   H    sing N N 504 
TYR N   H2   sing N N 505 
TYR CA  C    sing N N 506 
TYR CA  CB   sing N N 507 
TYR CA  HA   sing N N 508 
TYR C   O    doub N N 509 
TYR C   OXT  sing N N 510 
TYR CB  CG   sing N N 511 
TYR CB  HB2  sing N N 512 
TYR CB  HB3  sing N N 513 
TYR CG  CD1  doub Y N 514 
TYR CG  CD2  sing Y N 515 
TYR CD1 CE1  sing Y N 516 
TYR CD1 HD1  sing N N 517 
TYR CD2 CE2  doub Y N 518 
TYR CD2 HD2  sing N N 519 
TYR CE1 CZ   doub Y N 520 
TYR CE1 HE1  sing N N 521 
TYR CE2 CZ   sing Y N 522 
TYR CE2 HE2  sing N N 523 
TYR CZ  OH   sing N N 524 
TYR OH  HH   sing N N 525 
TYR OXT HXT  sing N N 526 
VAL N   CA   sing N N 527 
VAL N   H    sing N N 528 
VAL N   H2   sing N N 529 
VAL CA  C    sing N N 530 
VAL CA  CB   sing N N 531 
VAL CA  HA   sing N N 532 
VAL C   O    doub N N 533 
VAL C   OXT  sing N N 534 
VAL CB  CG1  sing N N 535 
VAL CB  CG2  sing N N 536 
VAL CB  HB   sing N N 537 
VAL CG1 HG11 sing N N 538 
VAL CG1 HG12 sing N N 539 
VAL CG1 HG13 sing N N 540 
VAL CG2 HG21 sing N N 541 
VAL CG2 HG22 sing N N 542 
VAL CG2 HG23 sing N N 543 
VAL OXT HXT  sing N N 544 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'German Research Foundation (DFG)' Germany 'CRC1078 - project number 221545957 - subproject B06'      1 
'German Research Foundation (DFG)' Germany 'EXC 311 2008/1 - UniSysCat - 390540038 - Research Unit E' 2 
# 
_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   6G1Y 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9G8D 
_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]   0.013397 
_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]   0.010686 
_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]   0.005749 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 7   ? 37.929  154.441 28.089  1.00 58.03 ? 7    HIS A N   1 
ATOM   2    C  CA  . HIS A 1 7   ? 36.696  155.282 27.985  1.00 56.39 ? 7    HIS A CA  1 
ATOM   3    C  C   . HIS A 1 7   ? 35.929  154.928 26.699  1.00 55.16 ? 7    HIS A C   1 
ATOM   4    O  O   . HIS A 1 7   ? 36.151  155.607 25.672  1.00 54.94 ? 7    HIS A O   1 
ATOM   5    C  CB  . HIS A 1 7   ? 37.065  156.773 28.057  1.00 56.89 ? 7    HIS A CB  1 
ATOM   6    N  N   . VAL A 1 8   ? 35.066  153.905 26.748  1.00 47.26 ? 8    VAL A N   1 
ATOM   7    C  CA  . VAL A 1 8   ? 34.213  153.483 25.593  1.00 43.22 ? 8    VAL A CA  1 
ATOM   8    C  C   . VAL A 1 8   ? 33.188  154.587 25.312  1.00 41.41 ? 8    VAL A C   1 
ATOM   9    O  O   . VAL A 1 8   ? 32.623  155.134 26.268  1.00 40.48 ? 8    VAL A O   1 
ATOM   10   C  CB  . VAL A 1 8   ? 33.521  152.123 25.828  1.00 41.58 ? 8    VAL A CB  1 
ATOM   11   C  CG1 . VAL A 1 8   ? 32.475  152.184 26.933  1.00 41.28 ? 8    VAL A CG1 1 
ATOM   12   C  CG2 . VAL A 1 8   ? 32.910  151.578 24.542  1.00 39.61 ? 8    VAL A CG2 1 
ATOM   13   N  N   . ASP A 1 9   ? 32.982  154.914 24.037  1.00 40.37 ? 9    ASP A N   1 
ATOM   14   C  CA  . ASP A 1 9   ? 31.848  155.752 23.563  1.00 39.65 ? 9    ASP A CA  1 
ATOM   15   C  C   . ASP A 1 9   ? 31.396  155.196 22.208  1.00 36.89 ? 9    ASP A C   1 
ATOM   16   O  O   . ASP A 1 9   ? 31.915  154.138 21.810  1.00 37.92 ? 9    ASP A O   1 
ATOM   17   C  CB  . ASP A 1 9   ? 32.226  157.237 23.545  1.00 41.22 ? 9    ASP A CB  1 
ATOM   18   C  CG  . ASP A 1 9   ? 33.373  157.596 22.614  1.00 44.05 ? 9    ASP A CG  1 
ATOM   19   O  OD1 . ASP A 1 9   ? 33.653  156.813 21.675  1.00 43.65 ? 9    ASP A OD1 1 
ATOM   20   O  OD2 . ASP A 1 9   ? 33.978  158.666 22.836  1.00 48.07 ? 9    ASP A OD2 1 
ATOM   21   N  N   . LEU A 1 10  ? 30.488  155.886 21.515  1.00 36.89 ? 10   LEU A N   1 
ATOM   22   C  CA  . LEU A 1 10  ? 29.908  155.411 20.230  1.00 37.14 ? 10   LEU A CA  1 
ATOM   23   C  C   . LEU A 1 10  ? 30.989  155.357 19.141  1.00 39.18 ? 10   LEU A C   1 
ATOM   24   O  O   . LEU A 1 10  ? 30.775  154.638 18.149  1.00 40.88 ? 10   LEU A O   1 
ATOM   25   C  CB  . LEU A 1 10  ? 28.753  156.330 19.830  1.00 37.81 ? 10   LEU A CB  1 
ATOM   26   C  CG  . LEU A 1 10  ? 27.605  156.420 20.835  1.00 37.11 ? 10   LEU A CG  1 
ATOM   27   C  CD1 . LEU A 1 10  ? 26.464  157.252 20.270  1.00 35.93 ? 10   LEU A CD1 1 
ATOM   28   C  CD2 . LEU A 1 10  ? 27.116  155.031 21.242  1.00 37.49 ? 10   LEU A CD2 1 
ATOM   29   N  N   . THR A 1 11  ? 32.130  156.031 19.328  1.00 39.19 ? 11   THR A N   1 
ATOM   30   C  CA  . THR A 1 11  ? 33.216  156.078 18.307  1.00 38.78 ? 11   THR A CA  1 
ATOM   31   C  C   . THR A 1 11  ? 34.048  154.790 18.357  1.00 38.55 ? 11   THR A C   1 
ATOM   32   O  O   . THR A 1 11  ? 34.601  154.414 17.304  1.00 38.68 ? 11   THR A O   1 
ATOM   33   C  CB  . THR A 1 11  ? 34.128  157.302 18.474  1.00 39.20 ? 11   THR A CB  1 
ATOM   34   O  OG1 . THR A 1 11  ? 34.892  157.145 19.671  1.00 41.20 ? 11   THR A OG1 1 
ATOM   35   C  CG2 . THR A 1 11  ? 33.364  158.609 18.498  1.00 38.25 ? 11   THR A CG2 1 
ATOM   36   N  N   . ASN A 1 12  ? 34.163  154.142 19.519  1.00 37.17 ? 12   ASN A N   1 
ATOM   37   C  CA  . ASN A 1 12  ? 35.083  152.982 19.691  1.00 37.20 ? 12   ASN A CA  1 
ATOM   38   C  C   . ASN A 1 12  ? 34.366  151.757 20.285  1.00 36.14 ? 12   ASN A C   1 
ATOM   39   O  O   . ASN A 1 12  ? 35.053  150.741 20.492  1.00 33.15 ? 12   ASN A O   1 
ATOM   40   C  CB  . ASN A 1 12  ? 36.300  153.376 20.528  1.00 38.15 ? 12   ASN A CB  1 
ATOM   41   C  CG  . ASN A 1 12  ? 35.922  153.805 21.930  1.00 40.18 ? 12   ASN A CG  1 
ATOM   42   O  OD1 . ASN A 1 12  ? 34.842  153.485 22.413  1.00 42.50 ? 12   ASN A OD1 1 
ATOM   43   N  ND2 . ASN A 1 12  ? 36.798  154.540 22.588  1.00 41.55 ? 12   ASN A ND2 1 
ATOM   44   N  N   . CYS A 1 13  ? 33.047  151.812 20.518  1.00 36.73 ? 13   CYS A N   1 
ATOM   45   C  CA  . CYS A 1 13  ? 32.293  150.677 21.138  1.00 36.28 ? 13   CYS A CA  1 
ATOM   46   C  C   . CYS A 1 13  ? 32.322  149.449 20.211  1.00 35.59 ? 13   CYS A C   1 
ATOM   47   O  O   . CYS A 1 13  ? 32.190  148.324 20.729  1.00 33.16 ? 13   CYS A O   1 
ATOM   48   C  CB  . CYS A 1 13  ? 30.877  151.068 21.560  1.00 36.86 ? 13   CYS A CB  1 
ATOM   49   S  SG  . CYS A 1 13  ? 29.757  151.518 20.200  1.00 39.62 ? 13   CYS A SG  1 
ATOM   50   N  N   . ASP A 1 14  ? 32.574  149.629 18.908  1.00 33.76 ? 14   ASP A N   1 
ATOM   51   C  CA  . ASP A 1 14  ? 32.727  148.495 17.952  1.00 35.42 ? 14   ASP A CA  1 
ATOM   52   C  C   . ASP A 1 14  ? 33.967  147.658 18.303  1.00 35.27 ? 14   ASP A C   1 
ATOM   53   O  O   . ASP A 1 14  ? 34.034  146.509 17.837  1.00 33.90 ? 14   ASP A O   1 
ATOM   54   C  CB  . ASP A 1 14  ? 32.757  148.973 16.495  1.00 37.78 ? 14   ASP A CB  1 
ATOM   55   C  CG  . ASP A 1 14  ? 33.959  149.828 16.119  1.00 39.55 ? 14   ASP A CG  1 
ATOM   56   O  OD1 . ASP A 1 14  ? 34.630  150.341 17.028  1.00 41.69 ? 14   ASP A OD1 1 
ATOM   57   O  OD2 . ASP A 1 14  ? 34.212  149.973 14.916  1.00 45.98 ? 14   ASP A OD2 1 
ATOM   58   N  N   . ARG A 1 15  ? 34.931  148.213 19.052  1.00 36.13 ? 15   ARG A N   1 
ATOM   59   C  CA  . ARG A 1 15  ? 36.210  147.519 19.380  1.00 38.87 ? 15   ARG A CA  1 
ATOM   60   C  C   . ARG A 1 15  ? 36.408  147.414 20.901  1.00 35.85 ? 15   ARG A C   1 
ATOM   61   O  O   . ARG A 1 15  ? 37.520  147.063 21.312  1.00 32.58 ? 15   ARG A O   1 
ATOM   62   C  CB  . ARG A 1 15  ? 37.383  148.268 18.736  1.00 44.29 ? 15   ARG A CB  1 
ATOM   63   C  CG  . ARG A 1 15  ? 37.509  148.062 17.234  1.00 49.91 ? 15   ARG A CG  1 
ATOM   64   C  CD  . ARG A 1 15  ? 38.312  149.156 16.553  1.00 54.73 ? 15   ARG A CD  1 
ATOM   65   N  NE  . ARG A 1 15  ? 37.455  150.252 16.110  1.00 59.25 ? 15   ARG A NE  1 
ATOM   66   C  CZ  . ARG A 1 15  ? 37.500  151.513 16.548  1.00 61.84 ? 15   ARG A CZ  1 
ATOM   67   N  NH1 . ARG A 1 15  ? 36.647  152.401 16.061  1.00 60.11 ? 15   ARG A NH1 1 
ATOM   68   N  NH2 . ARG A 1 15  ? 38.390  151.895 17.452  1.00 64.30 ? 15   ARG A NH2 1 
ATOM   69   N  N   . GLU A 1 16  ? 35.377  147.700 21.702  1.00 35.12 ? 16   GLU A N   1 
ATOM   70   C  CA  . GLU A 1 16  ? 35.436  147.644 23.192  1.00 34.24 ? 16   GLU A CA  1 
ATOM   71   C  C   . GLU A 1 16  ? 35.925  146.265 23.630  1.00 32.82 ? 16   GLU A C   1 
ATOM   72   O  O   . GLU A 1 16  ? 35.363  145.255 23.215  1.00 30.80 ? 16   GLU A O   1 
ATOM   73   C  CB  . GLU A 1 16  ? 34.061  147.920 23.800  1.00 34.98 ? 16   GLU A CB  1 
ATOM   74   C  CG  . GLU A 1 16  ? 34.080  148.045 25.314  1.00 35.32 ? 16   GLU A CG  1 
ATOM   75   C  CD  . GLU A 1 16  ? 32.722  148.277 25.947  1.00 35.24 ? 16   GLU A CD  1 
ATOM   76   O  OE1 . GLU A 1 16  ? 31.715  148.247 25.205  1.00 36.47 ? 16   GLU A OE1 1 
ATOM   77   O  OE2 . GLU A 1 16  ? 32.674  148.487 27.181  1.00 33.77 ? 16   GLU A OE2 1 
ATOM   78   N  N   . PRO A 1 17  ? 36.979  146.171 24.477  1.00 32.94 ? 17   PRO A N   1 
ATOM   79   C  CA  . PRO A 1 17  ? 37.502  144.878 24.921  1.00 31.33 ? 17   PRO A CA  1 
ATOM   80   C  C   . PRO A 1 17  ? 36.661  144.322 26.082  1.00 31.76 ? 17   PRO A C   1 
ATOM   81   O  O   . PRO A 1 17  ? 37.108  144.337 27.217  1.00 32.21 ? 17   PRO A O   1 
ATOM   82   C  CB  . PRO A 1 17  ? 38.935  145.248 25.334  1.00 31.87 ? 17   PRO A CB  1 
ATOM   83   C  CG  . PRO A 1 17  ? 38.774  146.626 25.932  1.00 31.59 ? 17   PRO A CG  1 
ATOM   84   C  CD  . PRO A 1 17  ? 37.724  147.299 25.065  1.00 33.03 ? 17   PRO A CD  1 
ATOM   85   N  N   . ILE A 1 18  ? 35.450  143.858 25.765  1.00 31.19 ? 18   ILE A N   1 
ATOM   86   C  CA  . ILE A 1 18  ? 34.396  143.481 26.757  1.00 30.02 ? 18   ILE A CA  1 
ATOM   87   C  C   . ILE A 1 18  ? 34.757  142.159 27.450  1.00 28.26 ? 18   ILE A C   1 
ATOM   88   O  O   . ILE A 1 18  ? 34.126  141.840 28.478  1.00 26.76 ? 18   ILE A O   1 
ATOM   89   C  CB  . ILE A 1 18  ? 33.012  143.434 26.087  1.00 30.36 ? 18   ILE A CB  1 
ATOM   90   C  CG1 . ILE A 1 18  ? 32.972  142.468 24.897  1.00 30.82 ? 18   ILE A CG1 1 
ATOM   91   C  CG2 . ILE A 1 18  ? 32.590  144.845 25.700  1.00 31.27 ? 18   ILE A CG2 1 
ATOM   92   C  CD1 . ILE A 1 18  ? 31.574  142.091 24.459  1.00 30.34 ? 18   ILE A CD1 1 
ATOM   93   N  N   . HIS A 1 19  ? 35.747  141.435 26.929  1.00 27.83 ? 19   HIS A N   1 
ATOM   94   C  CA  . HIS A 1 19  ? 36.241  140.157 27.515  1.00 29.08 ? 19   HIS A CA  1 
ATOM   95   C  C   . HIS A 1 19  ? 37.170  140.436 28.707  1.00 28.11 ? 19   HIS A C   1 
ATOM   96   O  O   . HIS A 1 19  ? 37.351  139.506 29.510  1.00 27.75 ? 19   HIS A O   1 
ATOM   97   C  CB  . HIS A 1 19  ? 36.890  139.270 26.443  1.00 29.26 ? 19   HIS A CB  1 
ATOM   98   C  CG  . HIS A 1 19  ? 38.125  139.845 25.843  1.00 29.08 ? 19   HIS A CG  1 
ATOM   99   N  ND1 . HIS A 1 19  ? 38.132  141.066 25.203  1.00 30.05 ? 19   HIS A ND1 1 
ATOM   100  C  CD2 . HIS A 1 19  ? 39.382  139.367 25.759  1.00 29.03 ? 19   HIS A CD2 1 
ATOM   101  C  CE1 . HIS A 1 19  ? 39.347  141.325 24.764  1.00 29.52 ? 19   HIS A CE1 1 
ATOM   102  N  NE2 . HIS A 1 19  ? 40.130  140.299 25.092  1.00 29.59 ? 19   HIS A NE2 1 
ATOM   103  N  N   . ILE A 1 20  ? 37.695  141.662 28.841  1.00 27.85 ? 20   ILE A N   1 
ATOM   104  C  CA  . ILE A 1 20  ? 38.651  142.049 29.929  1.00 29.74 ? 20   ILE A CA  1 
ATOM   105  C  C   . ILE A 1 20  ? 38.199  143.349 30.579  1.00 28.30 ? 20   ILE A C   1 
ATOM   106  O  O   . ILE A 1 20  ? 38.960  144.304 30.632  1.00 28.64 ? 20   ILE A O   1 
ATOM   107  C  CB  . ILE A 1 20  ? 40.098  142.180 29.399  1.00 29.71 ? 20   ILE A CB  1 
ATOM   108  C  CG1 . ILE A 1 20  ? 40.178  143.075 28.157  1.00 30.93 ? 20   ILE A CG1 1 
ATOM   109  C  CG2 . ILE A 1 20  ? 40.704  140.810 29.159  1.00 29.69 ? 20   ILE A CG2 1 
ATOM   110  C  CD1 . ILE A 1 20  ? 41.583  143.516 27.789  1.00 31.55 ? 20   ILE A CD1 1 
ATOM   111  N  N   . PRO A 1 21  ? 36.965  143.432 31.119  1.00 28.56 ? 21   PRO A N   1 
ATOM   112  C  CA  . PRO A 1 21  ? 36.472  144.699 31.653  1.00 28.55 ? 21   PRO A CA  1 
ATOM   113  C  C   . PRO A 1 21  ? 37.099  145.091 33.002  1.00 28.83 ? 21   PRO A C   1 
ATOM   114  O  O   . PRO A 1 21  ? 37.032  146.265 33.346  1.00 28.68 ? 21   PRO A O   1 
ATOM   115  C  CB  . PRO A 1 21  ? 34.968  144.437 31.790  1.00 28.78 ? 21   PRO A CB  1 
ATOM   116  C  CG  . PRO A 1 21  ? 34.880  142.947 32.059  1.00 29.53 ? 21   PRO A CG  1 
ATOM   117  C  CD  . PRO A 1 21  ? 35.996  142.331 31.244  1.00 28.35 ? 21   PRO A CD  1 
ATOM   118  N  N   . GLY A 1 22  ? 37.671  144.123 33.728  1.00 27.81 ? 22   GLY A N   1 
ATOM   119  C  CA  . GLY A 1 22  ? 38.313  144.350 35.039  1.00 28.43 ? 22   GLY A CA  1 
ATOM   120  C  C   . GLY A 1 22  ? 37.300  144.468 36.167  1.00 28.98 ? 22   GLY A C   1 
ATOM   121  O  O   . GLY A 1 22  ? 37.694  144.901 37.259  1.00 27.78 ? 22   GLY A O   1 
ATOM   122  N  N   . TYR A 1 23  ? 36.047  144.078 35.919  1.00 28.29 ? 23   TYR A N   1 
ATOM   123  C  CA  . TYR A 1 23  ? 34.922  144.141 36.890  1.00 28.51 ? 23   TYR A CA  1 
ATOM   124  C  C   . TYR A 1 23  ? 34.036  142.904 36.751  1.00 27.59 ? 23   TYR A C   1 
ATOM   125  O  O   . TYR A 1 23  ? 33.977  142.336 35.650  1.00 26.70 ? 23   TYR A O   1 
ATOM   126  C  CB  . TYR A 1 23  ? 34.042  145.360 36.627  1.00 29.77 ? 23   TYR A CB  1 
ATOM   127  C  CG  . TYR A 1 23  ? 34.716  146.675 36.890  1.00 32.09 ? 23   TYR A CG  1 
ATOM   128  C  CD1 . TYR A 1 23  ? 34.740  147.212 38.165  1.00 32.17 ? 23   TYR A CD1 1 
ATOM   129  C  CD2 . TYR A 1 23  ? 35.352  147.369 35.870  1.00 34.00 ? 23   TYR A CD2 1 
ATOM   130  C  CE1 . TYR A 1 23  ? 35.372  148.417 38.424  1.00 35.95 ? 23   TYR A CE1 1 
ATOM   131  C  CE2 . TYR A 1 23  ? 35.983  148.580 36.111  1.00 36.09 ? 23   TYR A CE2 1 
ATOM   132  C  CZ  . TYR A 1 23  ? 35.996  149.101 37.394  1.00 36.64 ? 23   TYR A CZ  1 
ATOM   133  O  OH  . TYR A 1 23  ? 36.618  150.282 37.660  1.00 40.53 ? 23   TYR A OH  1 
ATOM   134  N  N   . ILE A 1 24  ? 33.325  142.554 37.824  1.00 26.15 ? 24   ILE A N   1 
ATOM   135  C  CA  . ILE A 1 24  ? 32.257  141.520 37.808  1.00 26.03 ? 24   ILE A CA  1 
ATOM   136  C  C   . ILE A 1 24  ? 30.944  142.177 38.229  1.00 27.39 ? 24   ILE A C   1 
ATOM   137  O  O   . ILE A 1 24  ? 30.979  143.321 38.742  1.00 27.12 ? 24   ILE A O   1 
ATOM   138  C  CB  . ILE A 1 24  ? 32.604  140.322 38.709  1.00 25.40 ? 24   ILE A CB  1 
ATOM   139  C  CG1 . ILE A 1 24  ? 32.754  140.745 40.172  1.00 24.68 ? 24   ILE A CG1 1 
ATOM   140  C  CG2 . ILE A 1 24  ? 33.831  139.587 38.188  1.00 24.96 ? 24   ILE A CG2 1 
ATOM   141  C  CD1 . ILE A 1 24  ? 32.660  139.606 41.140  1.00 25.23 ? 24   ILE A CD1 1 
ATOM   142  N  N   . GLN A 1 25  ? 29.842  141.453 38.026  1.00 26.56 ? 25   GLN A N   1 
ATOM   143  C  CA  . GLN A 1 25  ? 28.486  141.834 38.492  1.00 27.69 ? 25   GLN A CA  1 
ATOM   144  C  C   . GLN A 1 25  ? 28.358  141.469 39.970  1.00 27.68 ? 25   GLN A C   1 
ATOM   145  O  O   . GLN A 1 25  ? 29.049  140.575 40.457  1.00 27.06 ? 25   GLN A O   1 
ATOM   146  C  CB  . GLN A 1 25  ? 27.426  141.150 37.630  1.00 26.85 ? 25   GLN A CB  1 
ATOM   147  C  CG  . GLN A 1 25  ? 27.483  141.546 36.164  1.00 27.53 ? 25   GLN A CG  1 
ATOM   148  C  CD  . GLN A 1 25  ? 26.405  140.834 35.382  1.00 26.58 ? 25   GLN A CD  1 
ATOM   149  O  OE1 . GLN A 1 25  ? 25.224  140.904 35.717  1.00 26.40 ? 25   GLN A OE1 1 
ATOM   150  N  NE2 . GLN A 1 25  ? 26.810  140.107 34.357  1.00 26.53 ? 25   GLN A NE2 1 
ATOM   151  N  N   . PRO A 1 26  ? 27.494  142.170 40.739  1.00 29.16 ? 26   PRO A N   1 
ATOM   152  C  CA  . PRO A 1 26  ? 27.462  141.997 42.193  1.00 29.24 ? 26   PRO A CA  1 
ATOM   153  C  C   . PRO A 1 26  ? 26.753  140.746 42.739  1.00 29.97 ? 26   PRO A C   1 
ATOM   154  O  O   . PRO A 1 26  ? 26.826  140.544 43.946  1.00 30.36 ? 26   PRO A O   1 
ATOM   155  C  CB  . PRO A 1 26  ? 26.770  143.275 42.704  1.00 30.05 ? 26   PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 26  ? 25.987  143.826 41.517  1.00 31.63 ? 26   PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 26  ? 26.623  143.256 40.266  1.00 29.77 ? 26   PRO A CD  1 
ATOM   158  N  N   . HIS A 1 27  ? 26.146  139.912 41.886  1.00 28.82 ? 27   HIS A N   1 
ATOM   159  C  CA  . HIS A 1 27  ? 25.354  138.727 42.322  1.00 29.18 ? 27   HIS A CA  1 
ATOM   160  C  C   . HIS A 1 27  ? 26.268  137.530 42.616  1.00 28.98 ? 27   HIS A C   1 
ATOM   161  O  O   . HIS A 1 27  ? 25.742  136.452 42.940  1.00 30.43 ? 27   HIS A O   1 
ATOM   162  C  CB  . HIS A 1 27  ? 24.241  138.395 41.317  1.00 29.89 ? 27   HIS A CB  1 
ATOM   163  C  CG  . HIS A 1 27  ? 24.722  137.917 39.993  1.00 29.30 ? 27   HIS A CG  1 
ATOM   164  N  ND1 . HIS A 1 27  ? 25.074  138.791 38.979  1.00 31.05 ? 27   HIS A ND1 1 
ATOM   165  C  CD2 . HIS A 1 27  ? 24.897  136.671 39.506  1.00 29.86 ? 27   HIS A CD2 1 
ATOM   166  C  CE1 . HIS A 1 27  ? 25.461  138.098 37.926  1.00 30.07 ? 27   HIS A CE1 1 
ATOM   167  N  NE2 . HIS A 1 27  ? 25.365  136.792 38.227  1.00 29.61 ? 27   HIS A NE2 1 
ATOM   168  N  N   . GLY A 1 28  ? 27.587  137.703 42.529  1.00 27.19 ? 28   GLY A N   1 
ATOM   169  C  CA  . GLY A 1 28  ? 28.542  136.680 42.986  1.00 26.60 ? 28   GLY A CA  1 
ATOM   170  C  C   . GLY A 1 28  ? 29.897  137.282 43.270  1.00 25.92 ? 28   GLY A C   1 
ATOM   171  O  O   . GLY A 1 28  ? 30.035  138.512 43.146  1.00 25.75 ? 28   GLY A O   1 
ATOM   172  N  N   . CYS A 1 29  ? 30.870  136.447 43.628  1.00 25.65 ? 29   CYS A N   1 
ATOM   173  C  CA  . CYS A 1 29  ? 32.283  136.879 43.771  1.00 25.59 ? 29   CYS A CA  1 
ATOM   174  C  C   . CYS A 1 29  ? 33.175  135.913 42.994  1.00 25.31 ? 29   CYS A C   1 
ATOM   175  O  O   . CYS A 1 29  ? 32.707  134.818 42.621  1.00 23.17 ? 29   CYS A O   1 
ATOM   176  C  CB  . CYS A 1 29  ? 32.687  137.011 45.235  1.00 26.29 ? 29   CYS A CB  1 
ATOM   177  S  SG  . CYS A 1 29  ? 32.718  135.446 46.144  1.00 27.51 ? 29   CYS A SG  1 
ATOM   178  N  N   . LEU A 1 30  ? 34.408  136.339 42.740  1.00 25.85 ? 30   LEU A N   1 
ATOM   179  C  CA  . LEU A 1 30  ? 35.338  135.670 41.799  1.00 27.70 ? 30   LEU A CA  1 
ATOM   180  C  C   . LEU A 1 30  ? 36.720  135.615 42.449  1.00 27.54 ? 30   LEU A C   1 
ATOM   181  O  O   . LEU A 1 30  ? 37.161  136.662 42.964  1.00 26.89 ? 30   LEU A O   1 
ATOM   182  C  CB  . LEU A 1 30  ? 35.374  136.462 40.485  1.00 27.53 ? 30   LEU A CB  1 
ATOM   183  C  CG  . LEU A 1 30  ? 36.176  135.831 39.345  1.00 27.32 ? 30   LEU A CG  1 
ATOM   184  C  CD1 . LEU A 1 30  ? 35.540  136.140 37.998  1.00 27.40 ? 30   LEU A CD1 1 
ATOM   185  C  CD2 . LEU A 1 30  ? 37.620  136.298 39.364  1.00 28.75 ? 30   LEU A CD2 1 
ATOM   186  N  N   . ILE A 1 31  ? 37.337  134.436 42.433  1.00 28.13 ? 31   ILE A N   1 
ATOM   187  C  CA  . ILE A 1 31  ? 38.775  134.216 42.766  1.00 30.31 ? 31   ILE A CA  1 
ATOM   188  C  C   . ILE A 1 31  ? 39.478  133.693 41.510  1.00 29.81 ? 31   ILE A C   1 
ATOM   189  O  O   . ILE A 1 31  ? 38.958  132.747 40.883  1.00 28.99 ? 31   ILE A O   1 
ATOM   190  C  CB  . ILE A 1 31  ? 38.929  133.262 43.967  1.00 30.02 ? 31   ILE A CB  1 
ATOM   191  C  CG1 . ILE A 1 31  ? 38.400  133.906 45.251  1.00 29.68 ? 31   ILE A CG1 1 
ATOM   192  C  CG2 . ILE A 1 31  ? 40.375  132.815 44.120  1.00 31.22 ? 31   ILE A CG2 1 
ATOM   193  C  CD1 . ILE A 1 31  ? 38.250  132.949 46.412  1.00 29.56 ? 31   ILE A CD1 1 
ATOM   194  N  N   . ALA A 1 32  ? 40.600  134.315 41.147  1.00 30.54 ? 32   ALA A N   1 
ATOM   195  C  CA  . ALA A 1 32  ? 41.506  133.861 40.067  1.00 31.63 ? 32   ALA A CA  1 
ATOM   196  C  C   . ALA A 1 32  ? 42.746  133.234 40.703  1.00 31.87 ? 32   ALA A C   1 
ATOM   197  O  O   . ALA A 1 32  ? 43.449  133.945 41.465  1.00 31.90 ? 32   ALA A O   1 
ATOM   198  C  CB  . ALA A 1 32  ? 41.871  135.018 39.171  1.00 32.72 ? 32   ALA A CB  1 
ATOM   199  N  N   . CYS A 1 33  ? 42.984  131.954 40.425  1.00 31.38 ? 33   CYS A N   1 
ATOM   200  C  CA  . CYS A 1 33  ? 44.193  131.210 40.880  1.00 34.03 ? 33   CYS A CA  1 
ATOM   201  C  C   . CYS A 1 33  ? 45.102  130.934 39.685  1.00 34.61 ? 33   CYS A C   1 
ATOM   202  O  O   . CYS A 1 33  ? 44.659  131.143 38.537  1.00 33.64 ? 33   CYS A O   1 
ATOM   203  C  CB  . CYS A 1 33  ? 43.832  129.900 41.569  1.00 33.76 ? 33   CYS A CB  1 
ATOM   204  S  SG  . CYS A 1 33  ? 42.788  130.147 43.028  1.00 34.99 ? 33   CYS A SG  1 
ATOM   205  N  N   . ASP A 1 34  ? 46.325  130.485 39.960  1.00 35.45 ? 34   ASP A N   1 
ATOM   206  C  CA  . ASP A 1 34  ? 47.267  129.989 38.923  1.00 37.92 ? 34   ASP A CA  1 
ATOM   207  C  C   . ASP A 1 34  ? 46.695  128.699 38.337  1.00 39.95 ? 34   ASP A C   1 
ATOM   208  O  O   . ASP A 1 34  ? 45.693  128.176 38.882  1.00 37.89 ? 34   ASP A O   1 
ATOM   209  C  CB  . ASP A 1 34  ? 48.660  129.735 39.494  1.00 39.98 ? 34   ASP A CB  1 
ATOM   210  C  CG  . ASP A 1 34  ? 48.626  128.764 40.658  1.00 40.98 ? 34   ASP A CG  1 
ATOM   211  O  OD1 . ASP A 1 34  ? 48.256  127.596 40.441  1.00 44.09 ? 34   ASP A OD1 1 
ATOM   212  O  OD2 . ASP A 1 34  ? 48.921  129.200 41.775  1.00 45.97 ? 34   ASP A OD2 1 
ATOM   213  N  N   . ASN A 1 35  ? 47.359  128.181 37.306  1.00 41.23 ? 35   ASN A N   1 
ATOM   214  C  CA  . ASN A 1 35  ? 46.890  127.031 36.499  1.00 42.67 ? 35   ASN A CA  1 
ATOM   215  C  C   . ASN A 1 35  ? 46.709  125.783 37.366  1.00 41.97 ? 35   ASN A C   1 
ATOM   216  O  O   . ASN A 1 35  ? 45.799  124.994 37.049  1.00 44.73 ? 35   ASN A O   1 
ATOM   217  C  CB  . ASN A 1 35  ? 47.839  126.738 35.339  1.00 48.46 ? 35   ASN A CB  1 
ATOM   218  C  CG  . ASN A 1 35  ? 47.115  126.011 34.233  1.00 50.13 ? 35   ASN A CG  1 
ATOM   219  O  OD1 . ASN A 1 35  ? 46.190  126.561 33.646  1.00 53.28 ? 35   ASN A OD1 1 
ATOM   220  N  ND2 . ASN A 1 35  ? 47.493  124.770 33.983  1.00 53.34 ? 35   ASN A ND2 1 
ATOM   221  N  N   . ALA A 1 36  ? 47.519  125.617 38.417  1.00 39.36 ? 36   ALA A N   1 
ATOM   222  C  CA  . ALA A 1 36  ? 47.513  124.430 39.309  1.00 38.39 ? 36   ALA A CA  1 
ATOM   223  C  C   . ALA A 1 36  ? 46.605  124.656 40.530  1.00 38.11 ? 36   ALA A C   1 
ATOM   224  O  O   . ALA A 1 36  ? 46.635  123.817 41.449  1.00 37.60 ? 36   ALA A O   1 
ATOM   225  C  CB  . ALA A 1 36  ? 48.930  124.106 39.724  1.00 39.11 ? 36   ALA A CB  1 
ATOM   226  N  N   . MET A 1 37  ? 45.819  125.736 40.539  1.00 40.23 ? 37   MET A N   1 
ATOM   227  C  CA  . MET A 1 37  ? 44.951  126.150 41.678  1.00 40.92 ? 37   MET A CA  1 
ATOM   228  C  C   . MET A 1 37  ? 45.722  125.988 42.999  1.00 39.57 ? 37   MET A C   1 
ATOM   229  O  O   . MET A 1 37  ? 45.201  125.336 43.923  1.00 37.83 ? 37   MET A O   1 
ATOM   230  C  CB  . MET A 1 37  ? 43.655  125.329 41.706  1.00 44.11 ? 37   MET A CB  1 
ATOM   231  C  CG  . MET A 1 37  ? 42.432  126.161 42.067  1.00 47.60 ? 37   MET A CG  1 
ATOM   232  S  SD  . MET A 1 37  ? 40.971  125.181 42.488  1.00 53.37 ? 37   MET A SD  1 
ATOM   233  C  CE  . MET A 1 37  ? 40.869  124.102 41.062  1.00 52.72 ? 37   MET A CE  1 
ATOM   234  N  N   . ARG A 1 38  ? 46.936  126.547 43.058  1.00 38.61 ? 38   ARG A N   1 
ATOM   235  C  CA  . ARG A 1 38  ? 47.817  126.538 44.264  1.00 38.15 ? 38   ARG A CA  1 
ATOM   236  C  C   . ARG A 1 38  ? 47.696  127.872 45.016  1.00 36.02 ? 38   ARG A C   1 
ATOM   237  O  O   . ARG A 1 38  ? 47.582  127.843 46.259  1.00 38.24 ? 38   ARG A O   1 
ATOM   238  C  CB  . ARG A 1 38  ? 49.271  126.267 43.861  1.00 35.40 ? 38   ARG A CB  1 
ATOM   239  N  N   . MET A 1 39  ? 47.726  128.987 44.288  1.00 34.13 ? 39   MET A N   1 
ATOM   240  C  CA  . MET A 1 39  ? 47.832  130.367 44.834  1.00 36.87 ? 39   MET A CA  1 
ATOM   241  C  C   . MET A 1 39  ? 46.681  131.222 44.295  1.00 36.64 ? 39   MET A C   1 
ATOM   242  O  O   . MET A 1 39  ? 46.376  131.100 43.085  1.00 35.09 ? 39   MET A O   1 
ATOM   243  C  CB  . MET A 1 39  ? 49.142  131.032 44.398  1.00 38.78 ? 39   MET A CB  1 
ATOM   244  C  CG  . MET A 1 39  ? 50.393  130.329 44.897  1.00 43.80 ? 39   MET A CG  1 
ATOM   245  S  SD  . MET A 1 39  ? 50.654  130.500 46.687  1.00 46.67 ? 39   MET A SD  1 
ATOM   246  C  CE  . MET A 1 39  ? 50.341  132.250 46.918  1.00 41.63 ? 39   MET A CE  1 
ATOM   247  N  N   . VAL A 1 40  ? 46.107  132.075 45.149  1.00 32.43 ? 40   VAL A N   1 
ATOM   248  C  CA  . VAL A 1 40  ? 45.156  133.153 44.745  1.00 32.40 ? 40   VAL A CA  1 
ATOM   249  C  C   . VAL A 1 40  ? 45.968  134.290 44.116  1.00 30.21 ? 40   VAL A C   1 
ATOM   250  O  O   . VAL A 1 40  ? 46.862  134.818 44.796  1.00 26.03 ? 40   VAL A O   1 
ATOM   251  C  CB  . VAL A 1 40  ? 44.326  133.668 45.937  1.00 32.31 ? 40   VAL A CB  1 
ATOM   252  C  CG1 . VAL A 1 40  ? 43.454  134.857 45.542  1.00 32.98 ? 40   VAL A CG1 1 
ATOM   253  C  CG2 . VAL A 1 40  ? 43.487  132.562 46.555  1.00 31.99 ? 40   VAL A CG2 1 
ATOM   254  N  N   . LEU A 1 41  ? 45.657  134.648 42.870  1.00 28.75 ? 41   LEU A N   1 
ATOM   255  C  CA  . LEU A 1 41  ? 46.343  135.730 42.123  1.00 29.15 ? 41   LEU A CA  1 
ATOM   256  C  C   . LEU A 1 41  ? 45.463  136.979 42.114  1.00 27.65 ? 41   LEU A C   1 
ATOM   257  O  O   . LEU A 1 41  ? 46.003  138.087 42.192  1.00 26.91 ? 41   LEU A O   1 
ATOM   258  C  CB  . LEU A 1 41  ? 46.643  135.250 40.698  1.00 31.38 ? 41   LEU A CB  1 
ATOM   259  C  CG  . LEU A 1 41  ? 47.633  134.089 40.567  1.00 32.27 ? 41   LEU A CG  1 
ATOM   260  C  CD1 . LEU A 1 41  ? 47.894  133.769 39.102  1.00 32.10 ? 41   LEU A CD1 1 
ATOM   261  C  CD2 . LEU A 1 41  ? 48.947  134.396 41.264  1.00 32.77 ? 41   LEU A CD2 1 
ATOM   262  N  N   . ARG A 1 42  ? 44.149  136.810 41.991  1.00 27.92 ? 42   ARG A N   1 
ATOM   263  C  CA  . ARG A 1 42  ? 43.214  137.966 41.951  1.00 27.74 ? 42   ARG A CA  1 
ATOM   264  C  C   . ARG A 1 42  ? 41.928  137.579 42.663  1.00 27.14 ? 42   ARG A C   1 
ATOM   265  O  O   . ARG A 1 42  ? 41.670  136.373 42.797  1.00 28.73 ? 42   ARG A O   1 
ATOM   266  C  CB  . ARG A 1 42  ? 42.884  138.394 40.518  1.00 30.19 ? 42   ARG A CB  1 
ATOM   267  C  CG  . ARG A 1 42  ? 44.027  138.238 39.527  1.00 30.87 ? 42   ARG A CG  1 
ATOM   268  C  CD  . ARG A 1 42  ? 43.765  139.100 38.312  1.00 32.24 ? 42   ARG A CD  1 
ATOM   269  N  NE  . ARG A 1 42  ? 44.586  138.726 37.168  1.00 33.39 ? 42   ARG A NE  1 
ATOM   270  C  CZ  . ARG A 1 42  ? 44.990  139.566 36.222  1.00 33.25 ? 42   ARG A CZ  1 
ATOM   271  N  NH1 . ARG A 1 42  ? 45.715  139.118 35.209  1.00 34.73 ? 42   ARG A NH1 1 
ATOM   272  N  NH2 . ARG A 1 42  ? 44.666  140.844 36.283  1.00 32.98 ? 42   ARG A NH2 1 
ATOM   273  N  N   . HIS A 1 43  ? 41.158  138.579 43.075  1.00 26.34 ? 43   HIS A N   1 
ATOM   274  C  CA  . HIS A 1 43  ? 39.847  138.400 43.740  1.00 27.74 ? 43   HIS A CA  1 
ATOM   275  C  C   . HIS A 1 43  ? 38.997  139.644 43.507  1.00 26.82 ? 43   HIS A C   1 
ATOM   276  O  O   . HIS A 1 43  ? 39.557  140.754 43.452  1.00 25.97 ? 43   HIS A O   1 
ATOM   277  C  CB  . HIS A 1 43  ? 40.034  138.073 45.227  1.00 28.26 ? 43   HIS A CB  1 
ATOM   278  C  CG  . HIS A 1 43  ? 40.608  139.189 46.032  1.00 28.34 ? 43   HIS A CG  1 
ATOM   279  N  ND1 . HIS A 1 43  ? 41.923  139.589 45.906  1.00 29.14 ? 43   HIS A ND1 1 
ATOM   280  C  CD2 . HIS A 1 43  ? 40.060  139.970 46.987  1.00 28.97 ? 43   HIS A CD2 1 
ATOM   281  C  CE1 . HIS A 1 43  ? 42.151  140.589 46.733  1.00 29.33 ? 43   HIS A CE1 1 
ATOM   282  N  NE2 . HIS A 1 43  ? 41.027  140.839 47.414  1.00 27.92 ? 43   HIS A NE2 1 
ATOM   283  N  N   . SER A 1 44  ? 37.692  139.449 43.347  1.00 27.39 ? 44   SER A N   1 
ATOM   284  C  CA  . SER A 1 44  ? 36.721  140.570 43.314  1.00 27.51 ? 44   SER A CA  1 
ATOM   285  C  C   . SER A 1 44  ? 36.649  141.175 44.722  1.00 27.54 ? 44   SER A C   1 
ATOM   286  O  O   . SER A 1 44  ? 36.762  140.421 45.705  1.00 27.59 ? 44   SER A O   1 
ATOM   287  C  CB  . SER A 1 44  ? 35.380  140.138 42.786  1.00 28.40 ? 44   SER A CB  1 
ATOM   288  O  OG  . SER A 1 44  ? 34.762  139.198 43.643  1.00 27.15 ? 44   SER A OG  1 
ATOM   289  N  N   . GLU A 1 45  ? 36.521  142.498 44.804  1.00 28.89 ? 45   GLU A N   1 
ATOM   290  C  CA  . GLU A 1 45  ? 36.536  143.279 46.069  1.00 30.55 ? 45   GLU A CA  1 
ATOM   291  C  C   . GLU A 1 45  ? 35.462  142.759 47.033  1.00 30.71 ? 45   GLU A C   1 
ATOM   292  O  O   . GLU A 1 45  ? 35.641  142.944 48.248  1.00 32.04 ? 45   GLU A O   1 
ATOM   293  C  CB  . GLU A 1 45  ? 36.313  144.761 45.762  1.00 34.05 ? 45   GLU A CB  1 
ATOM   294  C  CG  . GLU A 1 45  ? 36.672  145.691 46.901  1.00 37.19 ? 45   GLU A CG  1 
ATOM   295  C  CD  . GLU A 1 45  ? 36.801  147.141 46.457  1.00 42.10 ? 45   GLU A CD  1 
ATOM   296  O  OE1 . GLU A 1 45  ? 35.836  147.669 45.870  1.00 42.93 ? 45   GLU A OE1 1 
ATOM   297  O  OE2 . GLU A 1 45  ? 37.875  147.733 46.676  1.00 49.92 ? 45   GLU A OE2 1 
ATOM   298  N  N   . ASN A 1 46  ? 34.405  142.110 46.532  1.00 28.69 ? 46   ASN A N   1 
ATOM   299  C  CA  . ASN A 1 46  ? 33.267  141.643 47.374  1.00 28.46 ? 46   ASN A CA  1 
ATOM   300  C  C   . ASN A 1 46  ? 33.500  140.220 47.915  1.00 27.87 ? 46   ASN A C   1 
ATOM   301  O  O   . ASN A 1 46  ? 32.570  139.681 48.539  1.00 28.08 ? 46   ASN A O   1 
ATOM   302  C  CB  . ASN A 1 46  ? 31.943  141.735 46.612  1.00 27.75 ? 46   ASN A CB  1 
ATOM   303  C  CG  . ASN A 1 46  ? 31.881  140.798 45.428  1.00 27.27 ? 46   ASN A CG  1 
ATOM   304  O  OD1 . ASN A 1 46  ? 32.907  140.306 44.963  1.00 30.15 ? 46   ASN A OD1 1 
ATOM   305  N  ND2 . ASN A 1 46  ? 30.682  140.544 44.934  1.00 28.70 ? 46   ASN A ND2 1 
ATOM   306  N  N   . CYS A 1 47  ? 34.680  139.631 47.727  1.00 27.05 ? 47   CYS A N   1 
ATOM   307  C  CA  . CYS A 1 47  ? 34.989  138.255 48.220  1.00 28.34 ? 47   CYS A CA  1 
ATOM   308  C  C   . CYS A 1 47  ? 34.908  138.184 49.747  1.00 29.87 ? 47   CYS A C   1 
ATOM   309  O  O   . CYS A 1 47  ? 34.378  137.185 50.260  1.00 28.89 ? 47   CYS A O   1 
ATOM   310  C  CB  . CYS A 1 47  ? 36.377  137.788 47.816  1.00 27.99 ? 47   CYS A CB  1 
ATOM   311  S  SG  . CYS A 1 47  ? 36.422  137.092 46.153  1.00 28.70 ? 47   CYS A SG  1 
ATOM   312  N  N   . GLY A 1 48  ? 35.457  139.184 50.438  1.00 31.30 ? 48   GLY A N   1 
ATOM   313  C  CA  . GLY A 1 48  ? 35.450  139.255 51.911  1.00 32.44 ? 48   GLY A CA  1 
ATOM   314  C  C   . GLY A 1 48  ? 34.036  139.166 52.454  1.00 34.03 ? 48   GLY A C   1 
ATOM   315  O  O   . GLY A 1 48  ? 33.786  138.268 53.292  1.00 32.84 ? 48   GLY A O   1 
ATOM   316  N  N   . GLU A 1 49  ? 33.153  140.058 51.974  1.00 34.56 ? 49   GLU A N   1 
ATOM   317  C  CA  . GLU A 1 49  ? 31.721  140.158 52.366  1.00 36.31 ? 49   GLU A CA  1 
ATOM   318  C  C   . GLU A 1 49  ? 31.014  138.826 52.107  1.00 37.32 ? 49   GLU A C   1 
ATOM   319  O  O   . GLU A 1 49  ? 30.428  138.298 53.062  1.00 37.98 ? 49   GLU A O   1 
ATOM   320  C  CB  . GLU A 1 49  ? 31.001  141.269 51.598  1.00 37.72 ? 49   GLU A CB  1 
ATOM   321  N  N   . LEU A 1 50  ? 31.079  138.309 50.873  1.00 35.14 ? 50   LEU A N   1 
ATOM   322  C  CA  . LEU A 1 50  ? 30.296  137.117 50.444  1.00 35.45 ? 50   LEU A CA  1 
ATOM   323  C  C   . LEU A 1 50  ? 30.814  135.846 51.116  1.00 32.75 ? 50   LEU A C   1 
ATOM   324  O  O   . LEU A 1 50  ? 29.976  135.044 51.516  1.00 30.50 ? 50   LEU A O   1 
ATOM   325  C  CB  . LEU A 1 50  ? 30.333  136.959 48.921  1.00 39.21 ? 50   LEU A CB  1 
ATOM   326  C  CG  . LEU A 1 50  ? 29.077  137.435 48.196  1.00 42.11 ? 50   LEU A CG  1 
ATOM   327  C  CD1 . LEU A 1 50  ? 28.893  138.937 48.369  1.00 44.61 ? 50   LEU A CD1 1 
ATOM   328  C  CD2 . LEU A 1 50  ? 29.128  137.064 46.721  1.00 42.47 ? 50   LEU A CD2 1 
ATOM   329  N  N   . LEU A 1 51  ? 32.132  135.656 51.205  1.00 31.61 ? 51   LEU A N   1 
ATOM   330  C  CA  . LEU A 1 51  ? 32.734  134.380 51.679  1.00 32.81 ? 51   LEU A CA  1 
ATOM   331  C  C   . LEU A 1 51  ? 33.152  134.480 53.152  1.00 32.96 ? 51   LEU A C   1 
ATOM   332  O  O   . LEU A 1 51  ? 33.522  133.431 53.696  1.00 33.28 ? 51   LEU A O   1 
ATOM   333  C  CB  . LEU A 1 51  ? 33.938  134.013 50.802  1.00 34.62 ? 51   LEU A CB  1 
ATOM   334  C  CG  . LEU A 1 51  ? 33.639  133.755 49.325  1.00 35.37 ? 51   LEU A CG  1 
ATOM   335  C  CD1 . LEU A 1 51  ? 34.912  133.386 48.575  1.00 34.59 ? 51   LEU A CD1 1 
ATOM   336  C  CD2 . LEU A 1 51  ? 32.594  132.657 49.158  1.00 35.52 ? 51   LEU A CD2 1 
ATOM   337  N  N   . GLY A 1 52  ? 33.088  135.666 53.774  1.00 33.33 ? 52   GLY A N   1 
ATOM   338  C  CA  . GLY A 1 52  ? 33.509  135.868 55.179  1.00 32.83 ? 52   GLY A CA  1 
ATOM   339  C  C   . GLY A 1 52  ? 35.010  135.674 55.331  1.00 33.60 ? 52   GLY A C   1 
ATOM   340  O  O   . GLY A 1 52  ? 35.447  134.879 56.188  1.00 34.69 ? 52   GLY A O   1 
ATOM   341  N  N   . LEU A 1 53  ? 35.777  136.348 54.478  1.00 33.14 ? 53   LEU A N   1 
ATOM   342  C  CA  . LEU A 1 53  ? 37.258  136.318 54.465  1.00 33.84 ? 53   LEU A CA  1 
ATOM   343  C  C   . LEU A 1 53  ? 37.760  137.727 54.781  1.00 34.13 ? 53   LEU A C   1 
ATOM   344  O  O   . LEU A 1 53  ? 37.045  138.689 54.447  1.00 34.10 ? 53   LEU A O   1 
ATOM   345  C  CB  . LEU A 1 53  ? 37.731  135.847 53.088  1.00 34.34 ? 53   LEU A CB  1 
ATOM   346  C  CG  . LEU A 1 53  ? 37.397  134.398 52.733  1.00 37.37 ? 53   LEU A CG  1 
ATOM   347  C  CD1 . LEU A 1 53  ? 37.609  134.154 51.248  1.00 37.80 ? 53   LEU A CD1 1 
ATOM   348  C  CD2 . LEU A 1 53  ? 38.220  133.420 53.560  1.00 38.20 ? 53   LEU A CD2 1 
ATOM   349  N  N   . GLU A 1 54  ? 38.925  137.840 55.421  1.00 32.14 ? 54   GLU A N   1 
ATOM   350  C  CA  . GLU A 1 54  ? 39.502  139.149 55.816  1.00 31.90 ? 54   GLU A CA  1 
ATOM   351  C  C   . GLU A 1 54  ? 40.802  139.363 55.042  1.00 31.04 ? 54   GLU A C   1 
ATOM   352  O  O   . GLU A 1 54  ? 41.493  138.368 54.749  1.00 30.45 ? 54   GLU A O   1 
ATOM   353  C  CB  . GLU A 1 54  ? 39.735  139.218 57.329  1.00 32.63 ? 54   GLU A CB  1 
ATOM   354  C  CG  . GLU A 1 54  ? 38.456  139.186 58.147  1.00 32.55 ? 54   GLU A CG  1 
ATOM   355  C  CD  . GLU A 1 54  ? 38.650  139.005 59.646  1.00 34.52 ? 54   GLU A CD  1 
ATOM   356  O  OE1 . GLU A 1 54  ? 39.223  137.977 60.052  1.00 34.43 ? 54   GLU A OE1 1 
ATOM   357  O  OE2 . GLU A 1 54  ? 38.239  139.905 60.407  1.00 37.47 ? 54   GLU A OE2 1 
ATOM   358  N  N   . GLY A 1 55  ? 41.075  140.619 54.696  1.00 31.85 ? 55   GLY A N   1 
ATOM   359  C  CA  . GLY A 1 55  ? 42.379  141.080 54.190  1.00 32.89 ? 55   GLY A CA  1 
ATOM   360  C  C   . GLY A 1 55  ? 42.494  140.907 52.692  1.00 31.53 ? 55   GLY A C   1 
ATOM   361  O  O   . GLY A 1 55  ? 41.491  140.539 52.054  1.00 29.50 ? 55   GLY A O   1 
ATOM   362  N  N   . ASP A 1 56  ? 43.683  141.186 52.165  1.00 31.88 ? 56   ASP A N   1 
ATOM   363  C  CA  . ASP A 1 56  ? 44.043  140.975 50.742  1.00 31.51 ? 56   ASP A CA  1 
ATOM   364  C  C   . ASP A 1 56  ? 44.199  139.467 50.515  1.00 30.81 ? 56   ASP A C   1 
ATOM   365  O  O   . ASP A 1 56  ? 45.118  138.879 51.110  1.00 31.01 ? 56   ASP A O   1 
ATOM   366  C  CB  . ASP A 1 56  ? 45.314  141.750 50.386  1.00 32.04 ? 56   ASP A CB  1 
ATOM   367  C  CG  . ASP A 1 56  ? 45.646  141.724 48.903  1.00 33.34 ? 56   ASP A CG  1 
ATOM   368  O  OD1 . ASP A 1 56  ? 45.020  140.917 48.165  1.00 32.96 ? 56   ASP A OD1 1 
ATOM   369  O  OD2 . ASP A 1 56  ? 46.527  142.505 48.498  1.00 33.34 ? 56   ASP A OD2 1 
ATOM   370  N  N   . LEU A 1 57  ? 43.342  138.869 49.683  1.00 28.80 ? 57   LEU A N   1 
ATOM   371  C  CA  . LEU A 1 57  ? 43.347  137.402 49.428  1.00 28.36 ? 57   LEU A CA  1 
ATOM   372  C  C   . LEU A 1 57  ? 44.518  137.017 48.515  1.00 26.99 ? 57   LEU A C   1 
ATOM   373  O  O   . LEU A 1 57  ? 44.883  135.829 48.507  1.00 25.30 ? 57   LEU A O   1 
ATOM   374  C  CB  . LEU A 1 57  ? 42.015  136.982 48.802  1.00 29.06 ? 57   LEU A CB  1 
ATOM   375  C  CG  . LEU A 1 57  ? 40.764  137.316 49.610  1.00 28.91 ? 57   LEU A CG  1 
ATOM   376  C  CD1 . LEU A 1 57  ? 39.552  136.606 49.029  1.00 29.94 ? 57   LEU A CD1 1 
ATOM   377  C  CD2 . LEU A 1 57  ? 40.947  136.949 51.072  1.00 31.03 ? 57   LEU A CD2 1 
ATOM   378  N  N   . ASN A 1 58  ? 45.073  137.975 47.768  1.00 26.43 ? 58   ASN A N   1 
ATOM   379  C  CA  . ASN A 1 58  ? 46.183  137.736 46.805  1.00 26.74 ? 58   ASN A CA  1 
ATOM   380  C  C   . ASN A 1 58  ? 47.445  137.343 47.581  1.00 26.67 ? 58   ASN A C   1 
ATOM   381  O  O   . ASN A 1 58  ? 47.733  138.000 48.583  1.00 28.31 ? 58   ASN A O   1 
ATOM   382  C  CB  . ASN A 1 58  ? 46.395  138.954 45.909  1.00 26.64 ? 58   ASN A CB  1 
ATOM   383  C  CG  . ASN A 1 58  ? 45.173  139.232 45.060  1.00 27.41 ? 58   ASN A CG  1 
ATOM   384  O  OD1 . ASN A 1 58  ? 44.380  138.323 44.807  1.00 27.20 ? 58   ASN A OD1 1 
ATOM   385  N  ND2 . ASN A 1 58  ? 45.006  140.470 44.628  1.00 27.17 ? 58   ASN A ND2 1 
ATOM   386  N  N   . GLY A 1 59  ? 48.133  136.284 47.148  1.00 27.32 ? 59   GLY A N   1 
ATOM   387  C  CA  . GLY A 1 59  ? 49.362  135.774 47.795  1.00 29.89 ? 59   GLY A CA  1 
ATOM   388  C  C   . GLY A 1 59  ? 49.063  134.763 48.893  1.00 31.23 ? 59   GLY A C   1 
ATOM   389  O  O   . GLY A 1 59  ? 50.017  134.171 49.426  1.00 31.54 ? 59   GLY A O   1 
ATOM   390  N  N   . ARG A 1 60  ? 47.784  134.561 49.223  1.00 29.91 ? 60   ARG A N   1 
ATOM   391  C  CA  . ARG A 1 60  ? 47.337  133.458 50.113  1.00 29.44 ? 60   ARG A CA  1 
ATOM   392  C  C   . ARG A 1 60  ? 47.163  132.210 49.244  1.00 29.84 ? 60   ARG A C   1 
ATOM   393  O  O   . ARG A 1 60  ? 46.834  132.384 48.052  1.00 28.06 ? 60   ARG A O   1 
ATOM   394  C  CB  . ARG A 1 60  ? 46.051  133.855 50.843  1.00 29.40 ? 60   ARG A CB  1 
ATOM   395  C  CG  . ARG A 1 60  ? 46.215  135.055 51.764  1.00 30.18 ? 60   ARG A CG  1 
ATOM   396  C  CD  . ARG A 1 60  ? 44.967  135.402 52.553  1.00 29.76 ? 60   ARG A CD  1 
ATOM   397  N  NE  . ARG A 1 60  ? 44.492  134.315 53.395  1.00 29.42 ? 60   ARG A NE  1 
ATOM   398  C  CZ  . ARG A 1 60  ? 43.410  134.368 54.157  1.00 29.97 ? 60   ARG A CZ  1 
ATOM   399  N  NH1 . ARG A 1 60  ? 42.689  135.475 54.217  1.00 32.37 ? 60   ARG A NH1 1 
ATOM   400  N  NH2 . ARG A 1 60  ? 43.056  133.316 54.874  1.00 31.54 ? 60   ARG A NH2 1 
ATOM   401  N  N   . THR A 1 61  ? 47.382  131.012 49.800  1.00 29.70 ? 61   THR A N   1 
ATOM   402  C  CA  . THR A 1 61  ? 47.231  129.735 49.040  1.00 29.59 ? 61   THR A CA  1 
ATOM   403  C  C   . THR A 1 61  ? 45.736  129.460 48.832  1.00 29.03 ? 61   THR A C   1 
ATOM   404  O  O   . THR A 1 61  ? 44.923  129.932 49.649  1.00 28.08 ? 61   THR A O   1 
ATOM   405  C  CB  . THR A 1 61  ? 47.913  128.532 49.712  1.00 28.36 ? 61   THR A CB  1 
ATOM   406  O  OG1 . THR A 1 61  ? 47.171  128.157 50.873  1.00 27.54 ? 61   THR A OG1 1 
ATOM   407  C  CG2 . THR A 1 61  ? 49.362  128.793 50.066  1.00 29.31 ? 61   THR A CG2 1 
ATOM   408  N  N   . ALA A 1 62  ? 45.388  128.700 47.792  1.00 29.77 ? 62   ALA A N   1 
ATOM   409  C  CA  . ALA A 1 62  ? 44.000  128.248 47.538  1.00 30.95 ? 62   ALA A CA  1 
ATOM   410  C  C   . ALA A 1 62  ? 43.515  127.472 48.767  1.00 30.73 ? 62   ALA A C   1 
ATOM   411  O  O   . ALA A 1 62  ? 42.371  127.682 49.184  1.00 29.43 ? 62   ALA A O   1 
ATOM   412  C  CB  . ALA A 1 62  ? 43.937  127.413 46.280  1.00 31.34 ? 62   ALA A CB  1 
ATOM   413  N  N   . GLU A 1 63  ? 44.395  126.650 49.344  1.00 31.33 ? 63   GLU A N   1 
ATOM   414  C  CA  . GLU A 1 63  ? 44.116  125.793 50.529  1.00 33.03 ? 63   GLU A CA  1 
ATOM   415  C  C   . GLU A 1 63  ? 43.775  126.671 51.739  1.00 29.93 ? 63   GLU A C   1 
ATOM   416  O  O   . GLU A 1 63  ? 42.820  126.346 52.461  1.00 29.68 ? 63   GLU A O   1 
ATOM   417  C  CB  . GLU A 1 63  ? 45.327  124.910 50.818  1.00 34.61 ? 63   GLU A CB  1 
ATOM   418  C  CG  . GLU A 1 63  ? 45.088  123.877 51.898  1.00 38.24 ? 63   GLU A CG  1 
ATOM   419  C  CD  . GLU A 1 63  ? 46.252  122.913 52.067  1.00 42.64 ? 63   GLU A CD  1 
ATOM   420  O  OE1 . GLU A 1 63  ? 46.744  122.787 53.205  1.00 46.50 ? 63   GLU A OE1 1 
ATOM   421  O  OE2 . GLU A 1 63  ? 46.673  122.298 51.057  1.00 42.51 ? 63   GLU A OE2 1 
ATOM   422  N  N   . ASP A 1 64  ? 44.532  127.748 51.933  1.00 30.51 ? 64   ASP A N   1 
ATOM   423  C  CA  . ASP A 1 64  ? 44.305  128.741 53.013  1.00 30.81 ? 64   ASP A CA  1 
ATOM   424  C  C   . ASP A 1 64  ? 42.900  129.328 52.837  1.00 30.17 ? 64   ASP A C   1 
ATOM   425  O  O   . ASP A 1 64  ? 42.067  129.175 53.752  1.00 29.13 ? 64   ASP A O   1 
ATOM   426  C  CB  . ASP A 1 64  ? 45.427  129.784 53.010  1.00 30.32 ? 64   ASP A CB  1 
ATOM   427  C  CG  . ASP A 1 64  ? 45.224  130.935 53.977  1.00 30.55 ? 64   ASP A CG  1 
ATOM   428  O  OD1 . ASP A 1 64  ? 44.295  130.863 54.799  1.00 31.55 ? 64   ASP A OD1 1 
ATOM   429  O  OD2 . ASP A 1 64  ? 45.994  131.905 53.889  1.00 31.68 ? 64   ASP A OD2 1 
ATOM   430  N  N   . VAL A 1 65  ? 42.635  129.941 51.686  1.00 29.81 ? 65   VAL A N   1 
ATOM   431  C  CA  . VAL A 1 65  ? 41.393  130.736 51.443  1.00 32.34 ? 65   VAL A CA  1 
ATOM   432  C  C   . VAL A 1 65  ? 40.167  129.814 51.387  1.00 30.86 ? 65   VAL A C   1 
ATOM   433  O  O   . VAL A 1 65  ? 39.134  130.193 51.953  1.00 30.25 ? 65   VAL A O   1 
ATOM   434  C  CB  . VAL A 1 65  ? 41.537  131.597 50.175  1.00 32.81 ? 65   VAL A CB  1 
ATOM   435  C  CG1 . VAL A 1 65  ? 40.227  132.235 49.768  1.00 35.77 ? 65   VAL A CG1 1 
ATOM   436  C  CG2 . VAL A 1 65  ? 42.610  132.660 50.358  1.00 33.18 ? 65   VAL A CG2 1 
ATOM   437  N  N   . LEU A 1 66  ? 40.268  128.653 50.738  1.00 32.98 ? 66   LEU A N   1 
ATOM   438  C  CA  . LEU A 1 66  ? 39.099  127.773 50.454  1.00 33.25 ? 66   LEU A CA  1 
ATOM   439  C  C   . LEU A 1 66  ? 38.987  126.632 51.473  1.00 33.81 ? 66   LEU A C   1 
ATOM   440  O  O   . LEU A 1 66  ? 37.871  126.106 51.634  1.00 34.13 ? 66   LEU A O   1 
ATOM   441  C  CB  . LEU A 1 66  ? 39.234  127.231 49.029  1.00 35.14 ? 66   LEU A CB  1 
ATOM   442  C  CG  . LEU A 1 66  ? 39.302  128.287 47.927  1.00 35.15 ? 66   LEU A CG  1 
ATOM   443  C  CD1 . LEU A 1 66  ? 39.370  127.639 46.549  1.00 36.07 ? 66   LEU A CD1 1 
ATOM   444  C  CD2 . LEU A 1 66  ? 38.115  129.234 48.002  1.00 37.42 ? 66   LEU A CD2 1 
ATOM   445  N  N   . GLY A 1 67  ? 40.082  126.247 52.133  1.00 35.09 ? 67   GLY A N   1 
ATOM   446  C  CA  . GLY A 1 67  ? 40.108  125.058 53.012  1.00 34.99 ? 67   GLY A CA  1 
ATOM   447  C  C   . GLY A 1 67  ? 40.494  123.813 52.232  1.00 35.70 ? 67   GLY A C   1 
ATOM   448  O  O   . GLY A 1 67  ? 40.342  123.818 51.000  1.00 35.25 ? 67   GLY A O   1 
ATOM   449  N  N   . LYS A 1 68  ? 40.994  122.787 52.921  1.00 37.93 ? 68   LYS A N   1 
ATOM   450  C  CA  . LYS A 1 68  ? 41.537  121.547 52.304  1.00 39.21 ? 68   LYS A CA  1 
ATOM   451  C  C   . LYS A 1 68  ? 40.439  120.828 51.504  1.00 38.44 ? 68   LYS A C   1 
ATOM   452  O  O   . LYS A 1 68  ? 40.708  120.488 50.335  1.00 35.33 ? 68   LYS A O   1 
ATOM   453  C  CB  . LYS A 1 68  ? 42.169  120.663 53.383  1.00 43.19 ? 68   LYS A CB  1 
ATOM   454  C  CG  . LYS A 1 68  ? 43.534  121.157 53.852  1.00 47.04 ? 68   LYS A CG  1 
ATOM   455  C  CD  . LYS A 1 68  ? 44.284  120.204 54.761  1.00 50.09 ? 68   LYS A CD  1 
ATOM   456  C  CE  . LYS A 1 68  ? 45.697  120.671 55.049  1.00 51.01 ? 68   LYS A CE  1 
ATOM   457  N  NZ  . LYS A 1 68  ? 46.326  119.903 56.150  1.00 53.02 ? 68   LYS A NZ  1 
ATOM   458  N  N   . LYS A 1 69  ? 39.252  120.640 52.096  1.00 38.80 ? 69   LYS A N   1 
ATOM   459  C  CA  . LYS A 1 69  ? 38.102  119.909 51.490  1.00 38.04 ? 69   LYS A CA  1 
ATOM   460  C  C   . LYS A 1 69  ? 37.720  120.543 50.144  1.00 36.68 ? 69   LYS A C   1 
ATOM   461  O  O   . LYS A 1 69  ? 37.794  119.832 49.113  1.00 38.73 ? 69   LYS A O   1 
ATOM   462  C  CB  . LYS A 1 69  ? 36.899  119.896 52.440  1.00 39.01 ? 69   LYS A CB  1 
ATOM   463  N  N   . LEU A 1 70  ? 37.341  121.825 50.142  1.00 37.27 ? 70   LEU A N   1 
ATOM   464  C  CA  . LEU A 1 70  ? 36.834  122.526 48.926  1.00 37.21 ? 70   LEU A CA  1 
ATOM   465  C  C   . LEU A 1 70  ? 37.913  122.518 47.836  1.00 38.14 ? 70   LEU A C   1 
ATOM   466  O  O   . LEU A 1 70  ? 37.560  122.219 46.685  1.00 36.91 ? 70   LEU A O   1 
ATOM   467  C  CB  . LEU A 1 70  ? 36.380  123.951 49.260  1.00 38.05 ? 70   LEU A CB  1 
ATOM   468  C  CG  . LEU A 1 70  ? 35.775  124.742 48.094  1.00 36.95 ? 70   LEU A CG  1 
ATOM   469  C  CD1 . LEU A 1 70  ? 34.605  124.004 47.463  1.00 37.32 ? 70   LEU A CD1 1 
ATOM   470  C  CD2 . LEU A 1 70  ? 35.324  126.121 48.548  1.00 38.13 ? 70   LEU A CD2 1 
ATOM   471  N  N   . VAL A 1 71  ? 39.175  122.809 48.169  1.00 37.61 ? 71   VAL A N   1 
ATOM   472  C  CA  . VAL A 1 71  ? 40.288  122.756 47.173  1.00 40.29 ? 71   VAL A CA  1 
ATOM   473  C  C   . VAL A 1 71  ? 40.336  121.348 46.566  1.00 40.83 ? 71   VAL A C   1 
ATOM   474  O  O   . VAL A 1 71  ? 40.467  121.249 45.329  1.00 37.42 ? 71   VAL A O   1 
ATOM   475  C  CB  . VAL A 1 71  ? 41.655  123.152 47.763  1.00 44.60 ? 71   VAL A CB  1 
ATOM   476  C  CG1 . VAL A 1 71  ? 42.803  122.790 46.829  1.00 46.17 ? 71   VAL A CG1 1 
ATOM   477  C  CG2 . VAL A 1 71  ? 41.708  124.628 48.092  1.00 46.17 ? 71   VAL A CG2 1 
ATOM   478  N  N   . HIS A 1 72  ? 40.232  120.299 47.388  1.00 43.09 ? 72   HIS A N   1 
ATOM   479  C  CA  . HIS A 1 72  ? 40.291  118.891 46.908  1.00 46.00 ? 72   HIS A CA  1 
ATOM   480  C  C   . HIS A 1 72  ? 39.160  118.665 45.895  1.00 42.90 ? 72   HIS A C   1 
ATOM   481  O  O   . HIS A 1 72  ? 39.448  118.181 44.779  1.00 40.86 ? 72   HIS A O   1 
ATOM   482  C  CB  . HIS A 1 72  ? 40.253  117.891 48.071  1.00 51.38 ? 72   HIS A CB  1 
ATOM   483  C  CG  . HIS A 1 72  ? 40.151  116.469 47.621  1.00 55.09 ? 72   HIS A CG  1 
ATOM   484  N  ND1 . HIS A 1 72  ? 41.257  115.736 47.235  1.00 57.03 ? 72   HIS A ND1 1 
ATOM   485  C  CD2 . HIS A 1 72  ? 39.084  115.650 47.483  1.00 58.17 ? 72   HIS A CD2 1 
ATOM   486  C  CE1 . HIS A 1 72  ? 40.876  114.524 46.878  1.00 60.71 ? 72   HIS A CE1 1 
ATOM   487  N  NE2 . HIS A 1 72  ? 39.546  114.444 47.025  1.00 59.68 ? 72   HIS A NE2 1 
ATOM   488  N  N   . ASP A 1 73  ? 37.936  119.038 46.274  1.00 41.85 ? 73   ASP A N   1 
ATOM   489  C  CA  . ASP A 1 73  ? 36.701  118.883 45.458  1.00 43.37 ? 73   ASP A CA  1 
ATOM   490  C  C   . ASP A 1 73  ? 36.813  119.685 44.149  1.00 45.67 ? 73   ASP A C   1 
ATOM   491  O  O   . ASP A 1 73  ? 36.416  119.145 43.093  1.00 49.54 ? 73   ASP A O   1 
ATOM   492  C  CB  . ASP A 1 73  ? 35.462  119.261 46.277  1.00 42.80 ? 73   ASP A CB  1 
ATOM   493  C  CG  . ASP A 1 73  ? 35.180  118.314 47.437  1.00 42.66 ? 73   ASP A CG  1 
ATOM   494  O  OD1 . ASP A 1 73  ? 35.805  117.241 47.489  1.00 42.81 ? 73   ASP A OD1 1 
ATOM   495  O  OD2 . ASP A 1 73  ? 34.341  118.661 48.292  1.00 44.23 ? 73   ASP A OD2 1 
ATOM   496  N  N   . LEU A 1 74  ? 37.334  120.915 44.196  1.00 44.93 ? 74   LEU A N   1 
ATOM   497  C  CA  . LEU A 1 74  ? 37.414  121.812 43.008  1.00 46.00 ? 74   LEU A CA  1 
ATOM   498  C  C   . LEU A 1 74  ? 38.504  121.309 42.053  1.00 47.66 ? 74   LEU A C   1 
ATOM   499  O  O   . LEU A 1 74  ? 38.271  121.355 40.827  1.00 46.08 ? 74   LEU A O   1 
ATOM   500  C  CB  . LEU A 1 74  ? 37.678  123.254 43.451  1.00 43.89 ? 74   LEU A CB  1 
ATOM   501  C  CG  . LEU A 1 74  ? 36.538  123.941 44.203  1.00 45.30 ? 74   LEU A CG  1 
ATOM   502  C  CD1 . LEU A 1 74  ? 36.902  125.380 44.527  1.00 46.81 ? 74   LEU A CD1 1 
ATOM   503  C  CD2 . LEU A 1 74  ? 35.235  123.891 43.417  1.00 46.89 ? 74   LEU A CD2 1 
ATOM   504  N  N   . ARG A 1 75  ? 39.633  120.826 42.585  1.00 49.50 ? 75   ARG A N   1 
ATOM   505  C  CA  . ARG A 1 75  ? 40.738  120.260 41.756  1.00 50.92 ? 75   ARG A CA  1 
ATOM   506  C  C   . ARG A 1 75  ? 40.223  119.026 41.004  1.00 51.84 ? 75   ARG A C   1 
ATOM   507  O  O   . ARG A 1 75  ? 40.596  118.864 39.831  1.00 51.12 ? 75   ARG A O   1 
ATOM   508  C  CB  . ARG A 1 75  ? 41.967  119.933 42.610  1.00 52.10 ? 75   ARG A CB  1 
ATOM   509  C  CG  . ARG A 1 75  ? 42.927  121.106 42.762  1.00 53.95 ? 75   ARG A CG  1 
ATOM   510  C  CD  . ARG A 1 75  ? 44.190  120.786 43.541  1.00 54.34 ? 75   ARG A CD  1 
ATOM   511  N  NE  . ARG A 1 75  ? 44.835  122.019 43.995  1.00 55.75 ? 75   ARG A NE  1 
ATOM   512  C  CZ  . ARG A 1 75  ? 45.485  122.177 45.149  1.00 60.32 ? 75   ARG A CZ  1 
ATOM   513  N  NH1 . ARG A 1 75  ? 45.601  121.176 46.006  1.00 61.52 ? 75   ARG A NH1 1 
ATOM   514  N  NH2 . ARG A 1 75  ? 46.013  123.351 45.454  1.00 59.36 ? 75   ARG A NH2 1 
ATOM   515  N  N   . ASN A 1 76  ? 39.387  118.207 41.649  1.00 53.32 ? 76   ASN A N   1 
ATOM   516  C  CA  . ASN A 1 76  ? 38.739  117.021 41.026  1.00 58.00 ? 76   ASN A CA  1 
ATOM   517  C  C   . ASN A 1 76  ? 37.804  117.479 39.903  1.00 58.75 ? 76   ASN A C   1 
ATOM   518  O  O   . ASN A 1 76  ? 37.960  116.983 38.779  1.00 61.76 ? 76   ASN A O   1 
ATOM   519  C  CB  . ASN A 1 76  ? 37.997  116.163 42.051  1.00 60.07 ? 76   ASN A CB  1 
ATOM   520  C  CG  . ASN A 1 76  ? 38.940  115.356 42.917  1.00 63.12 ? 76   ASN A CG  1 
ATOM   521  O  OD1 . ASN A 1 76  ? 40.145  115.327 42.673  1.00 65.13 ? 76   ASN A OD1 1 
ATOM   522  N  ND2 . ASN A 1 76  ? 38.404  114.704 43.936  1.00 66.97 ? 76   ASN A ND2 1 
ATOM   523  N  N   . ALA A 1 77  ? 36.886  118.402 40.192  1.00 60.07 ? 77   ALA A N   1 
ATOM   524  C  CA  . ALA A 1 77  ? 35.922  118.956 39.208  1.00 61.53 ? 77   ALA A CA  1 
ATOM   525  C  C   . ALA A 1 77  ? 36.666  119.515 37.984  1.00 63.38 ? 77   ALA A C   1 
ATOM   526  O  O   . ALA A 1 77  ? 36.107  119.433 36.873  1.00 65.87 ? 77   ALA A O   1 
ATOM   527  C  CB  . ALA A 1 77  ? 35.060  120.012 39.853  1.00 60.83 ? 77   ALA A CB  1 
ATOM   528  N  N   . LEU A 1 78  ? 37.874  120.059 38.177  1.00 63.70 ? 78   LEU A N   1 
ATOM   529  C  CA  . LEU A 1 78  ? 38.689  120.702 37.104  1.00 66.48 ? 78   LEU A CA  1 
ATOM   530  C  C   . LEU A 1 78  ? 39.127  119.647 36.074  1.00 68.05 ? 78   LEU A C   1 
ATOM   531  O  O   . LEU A 1 78  ? 39.482  120.048 34.946  1.00 69.20 ? 78   LEU A O   1 
ATOM   532  C  CB  . LEU A 1 78  ? 39.889  121.423 37.732  1.00 65.45 ? 78   LEU A CB  1 
ATOM   533  C  CG  . LEU A 1 78  ? 40.425  122.636 36.967  1.00 65.62 ? 78   LEU A CG  1 
ATOM   534  C  CD1 . LEU A 1 78  ? 39.411  123.768 36.928  1.00 64.39 ? 78   LEU A CD1 1 
ATOM   535  C  CD2 . LEU A 1 78  ? 41.728  123.131 37.576  1.00 67.45 ? 78   LEU A CD2 1 
ATOM   536  N  N   . THR A 1 79  ? 39.107  118.360 36.447  1.00 69.65 ? 79   THR A N   1 
ATOM   537  C  CA  . THR A 1 79  ? 39.246  117.198 35.517  1.00 74.32 ? 79   THR A CA  1 
ATOM   538  C  C   . THR A 1 79  ? 38.118  117.208 34.471  1.00 77.42 ? 79   THR A C   1 
ATOM   539  O  O   . THR A 1 79  ? 38.433  117.060 33.270  1.00 78.70 ? 79   THR A O   1 
ATOM   540  C  CB  . THR A 1 79  ? 39.257  115.868 36.284  1.00 75.42 ? 79   THR A CB  1 
ATOM   541  O  OG1 . THR A 1 79  ? 40.306  115.936 37.251  1.00 74.10 ? 79   THR A OG1 1 
ATOM   542  C  CG2 . THR A 1 79  ? 39.447  114.660 35.391  1.00 76.08 ? 79   THR A CG2 1 
ATOM   543  N  N   . VAL A 1 80  ? 36.861  117.360 34.911  1.00 77.66 ? 80   VAL A N   1 
ATOM   544  C  CA  . VAL A 1 80  ? 35.648  117.427 34.034  1.00 77.69 ? 80   VAL A CA  1 
ATOM   545  C  C   . VAL A 1 80  ? 35.913  118.412 32.887  1.00 78.97 ? 80   VAL A C   1 
ATOM   546  O  O   . VAL A 1 80  ? 35.530  118.098 31.739  1.00 79.28 ? 80   VAL A O   1 
ATOM   547  C  CB  . VAL A 1 80  ? 34.388  117.821 34.829  1.00 73.05 ? 80   VAL A CB  1 
ATOM   548  N  N   . THR A 1 81  ? 36.542  119.554 33.193  1.00 78.67 ? 81   THR A N   1 
ATOM   549  C  CA  . THR A 1 81  ? 36.953  120.595 32.204  1.00 78.14 ? 81   THR A CA  1 
ATOM   550  C  C   . THR A 1 81  ? 37.757  119.953 31.065  1.00 78.57 ? 81   THR A C   1 
ATOM   551  O  O   . THR A 1 81  ? 38.951  119.669 31.299  1.00 75.37 ? 81   THR A O   1 
ATOM   552  C  CB  . THR A 1 81  ? 37.770  121.706 32.875  1.00 78.52 ? 81   THR A CB  1 
ATOM   553  N  N   . THR A 1 85  ? 36.110  121.446 27.804  1.00 68.81 ? 85   THR A N   1 
ATOM   554  C  CA  . THR A 1 85  ? 34.668  121.540 27.440  1.00 71.32 ? 85   THR A CA  1 
ATOM   555  C  C   . THR A 1 85  ? 34.135  122.932 27.826  1.00 70.92 ? 85   THR A C   1 
ATOM   556  O  O   . THR A 1 85  ? 34.625  123.921 27.241  1.00 75.67 ? 85   THR A O   1 
ATOM   557  C  CB  . THR A 1 85  ? 33.873  120.385 28.070  1.00 74.27 ? 85   THR A CB  1 
ATOM   558  O  OG1 . THR A 1 85  ? 34.671  119.202 28.026  1.00 75.69 ? 85   THR A OG1 1 
ATOM   559  C  CG2 . THR A 1 85  ? 32.552  120.141 27.374  1.00 73.99 ? 85   THR A CG2 1 
ATOM   560  N  N   . ARG A 1 86  ? 33.178  122.994 28.765  1.00 62.93 ? 86   ARG A N   1 
ATOM   561  C  CA  . ARG A 1 86  ? 32.572  124.243 29.321  1.00 55.63 ? 86   ARG A CA  1 
ATOM   562  C  C   . ARG A 1 86  ? 32.977  124.391 30.789  1.00 47.60 ? 86   ARG A C   1 
ATOM   563  O  O   . ARG A 1 86  ? 33.542  123.472 31.371  1.00 43.34 ? 86   ARG A O   1 
ATOM   564  C  CB  . ARG A 1 86  ? 31.045  124.188 29.191  1.00 53.21 ? 86   ARG A CB  1 
ATOM   565  N  N   . PRO A 1 87  ? 32.715  125.543 31.447  1.00 42.10 ? 87   PRO A N   1 
ATOM   566  C  CA  . PRO A 1 87  ? 32.841  125.626 32.903  1.00 41.42 ? 87   PRO A CA  1 
ATOM   567  C  C   . PRO A 1 87  ? 32.054  124.506 33.600  1.00 39.78 ? 87   PRO A C   1 
ATOM   568  O  O   . PRO A 1 87  ? 30.971  124.198 33.150  1.00 40.67 ? 87   PRO A O   1 
ATOM   569  C  CB  . PRO A 1 87  ? 32.263  127.012 33.234  1.00 40.20 ? 87   PRO A CB  1 
ATOM   570  C  CG  . PRO A 1 87  ? 32.532  127.821 31.984  1.00 40.83 ? 87   PRO A CG  1 
ATOM   571  C  CD  . PRO A 1 87  ? 32.343  126.833 30.846  1.00 42.15 ? 87   PRO A CD  1 
ATOM   572  N  N   . ALA A 1 88  ? 32.626  123.912 34.650  1.00 36.87 ? 88   ALA A N   1 
ATOM   573  C  CA  . ALA A 1 88  ? 31.922  122.984 35.565  1.00 37.21 ? 88   ALA A CA  1 
ATOM   574  C  C   . ALA A 1 88  ? 30.971  123.799 36.445  1.00 40.01 ? 88   ALA A C   1 
ATOM   575  O  O   . ALA A 1 88  ? 31.425  124.806 37.040  1.00 40.86 ? 88   ALA A O   1 
ATOM   576  C  CB  . ALA A 1 88  ? 32.906  122.197 36.397  1.00 36.92 ? 88   ALA A CB  1 
ATOM   577  N  N   . MET A 1 89  ? 29.693  123.409 36.481  1.00 41.67 ? 89   MET A N   1 
ATOM   578  C  CA  . MET A 1 89  ? 28.660  123.992 37.377  1.00 41.83 ? 89   MET A CA  1 
ATOM   579  C  C   . MET A 1 89  ? 28.491  123.048 38.569  1.00 41.29 ? 89   MET A C   1 
ATOM   580  O  O   . MET A 1 89  ? 28.108  121.886 38.342  1.00 42.91 ? 89   MET A O   1 
ATOM   581  C  CB  . MET A 1 89  ? 27.312  124.169 36.666  1.00 42.63 ? 89   MET A CB  1 
ATOM   582  C  CG  . MET A 1 89  ? 27.388  124.890 35.339  1.00 45.24 ? 89   MET A CG  1 
ATOM   583  S  SD  . MET A 1 89  ? 28.177  126.516 35.447  1.00 52.20 ? 89   MET A SD  1 
ATOM   584  C  CE  . MET A 1 89  ? 26.893  127.490 36.219  1.00 49.03 ? 89   MET A CE  1 
ATOM   585  N  N   . LEU A 1 90  ? 28.771  123.541 39.781  1.00 41.57 ? 90   LEU A N   1 
ATOM   586  C  CA  . LEU A 1 90  ? 28.739  122.771 41.052  1.00 40.35 ? 90   LEU A CA  1 
ATOM   587  C  C   . LEU A 1 90  ? 27.784  123.451 42.027  1.00 39.69 ? 90   LEU A C   1 
ATOM   588  O  O   . LEU A 1 90  ? 28.200  124.210 42.899  1.00 41.36 ? 90   LEU A O   1 
ATOM   589  C  CB  . LEU A 1 90  ? 30.161  122.684 41.612  1.00 40.92 ? 90   LEU A CB  1 
ATOM   590  C  CG  . LEU A 1 90  ? 31.198  122.157 40.624  1.00 42.84 ? 90   LEU A CG  1 
ATOM   591  C  CD1 . LEU A 1 90  ? 32.600  122.284 41.187  1.00 42.89 ? 90   LEU A CD1 1 
ATOM   592  C  CD2 . LEU A 1 90  ? 30.897  120.714 40.242  1.00 44.50 ? 90   LEU A CD2 1 
ATOM   593  N  N   . PRO A 1 91  ? 26.462  123.202 41.911  1.00 39.57 ? 91   PRO A N   1 
ATOM   594  C  CA  . PRO A 1 91  ? 25.497  123.784 42.839  1.00 38.57 ? 91   PRO A CA  1 
ATOM   595  C  C   . PRO A 1 91  ? 25.676  123.199 44.246  1.00 38.42 ? 91   PRO A C   1 
ATOM   596  O  O   . PRO A 1 91  ? 26.168  122.094 44.353  1.00 37.46 ? 91   PRO A O   1 
ATOM   597  C  CB  . PRO A 1 91  ? 24.127  123.395 42.270  1.00 38.33 ? 91   PRO A CB  1 
ATOM   598  C  CG  . PRO A 1 91  ? 24.410  122.914 40.858  1.00 38.36 ? 91   PRO A CG  1 
ATOM   599  C  CD  . PRO A 1 91  ? 25.821  122.364 40.887  1.00 38.93 ? 91   PRO A CD  1 
ATOM   600  N  N   . ALA A 1 92  ? 25.319  123.977 45.268  1.00 38.48 ? 92   ALA A N   1 
ATOM   601  C  CA  . ALA A 1 92  ? 25.138  123.531 46.672  1.00 43.21 ? 92   ALA A CA  1 
ATOM   602  C  C   . ALA A 1 92  ? 26.437  122.956 47.259  1.00 43.85 ? 92   ALA A C   1 
ATOM   603  O  O   . ALA A 1 92  ? 26.344  121.990 48.043  1.00 44.97 ? 92   ALA A O   1 
ATOM   604  C  CB  . ALA A 1 92  ? 24.015  122.519 46.736  1.00 42.02 ? 92   ALA A CB  1 
ATOM   605  N  N   . MET A 1 93  ? 27.597  123.532 46.927  1.00 46.19 ? 93   MET A N   1 
ATOM   606  C  CA  . MET A 1 93  ? 28.905  123.156 47.539  1.00 51.43 ? 93   MET A CA  1 
ATOM   607  C  C   . MET A 1 93  ? 28.995  123.745 48.953  1.00 53.48 ? 93   MET A C   1 
ATOM   608  O  O   . MET A 1 93  ? 28.583  124.911 49.125  1.00 51.25 ? 93   MET A O   1 
ATOM   609  C  CB  . MET A 1 93  ? 30.081  123.671 46.704  1.00 52.11 ? 93   MET A CB  1 
ATOM   610  C  CG  . MET A 1 93  ? 30.168  123.025 45.342  1.00 54.75 ? 93   MET A CG  1 
ATOM   611  S  SD  . MET A 1 93  ? 30.819  121.342 45.421  1.00 57.49 ? 93   MET A SD  1 
ATOM   612  C  CE  . MET A 1 93  ? 32.533  121.634 44.986  1.00 56.07 ? 93   MET A CE  1 
ATOM   613  N  N   . GLU A 1 94  ? 29.503  122.967 49.921  1.00 58.38 ? 94   GLU A N   1 
ATOM   614  C  CA  . GLU A 1 94  ? 29.707  123.399 51.335  1.00 61.95 ? 94   GLU A CA  1 
ATOM   615  C  C   . GLU A 1 94  ? 31.090  124.046 51.476  1.00 65.68 ? 94   GLU A C   1 
ATOM   616  O  O   . GLU A 1 94  ? 32.082  123.428 51.050  1.00 65.75 ? 94   GLU A O   1 
ATOM   617  C  CB  . GLU A 1 94  ? 29.575  122.228 52.310  1.00 59.17 ? 94   GLU A CB  1 
ATOM   618  N  N   . THR A 1 95  ? 31.140  125.250 52.052  1.00 71.67 ? 95   THR A N   1 
ATOM   619  C  CA  . THR A 1 95  ? 32.402  125.995 52.342  1.00 75.52 ? 95   THR A CA  1 
ATOM   620  C  C   . THR A 1 95  ? 33.120  125.340 53.530  1.00 76.68 ? 95   THR A C   1 
ATOM   621  O  O   . THR A 1 95  ? 32.403  124.801 54.398  1.00 77.94 ? 95   THR A O   1 
ATOM   622  C  CB  . THR A 1 95  ? 32.130  127.483 52.603  1.00 78.46 ? 95   THR A CB  1 
ATOM   623  O  OG1 . THR A 1 95  ? 30.809  127.624 53.124  1.00 79.56 ? 95   THR A OG1 1 
ATOM   624  C  CG2 . THR A 1 95  ? 32.264  128.332 51.359  1.00 80.13 ? 95   THR A CG2 1 
ATOM   625  N  N   . ASP A 1 97  ? 32.692  126.803 56.711  1.00 65.28 ? 97   ASP A N   1 
ATOM   626  C  CA  . ASP A 1 97  ? 31.777  127.349 57.755  1.00 63.11 ? 97   ASP A CA  1 
ATOM   627  C  C   . ASP A 1 97  ? 30.395  126.676 57.684  1.00 61.46 ? 97   ASP A C   1 
ATOM   628  O  O   . ASP A 1 97  ? 29.489  127.138 58.409  1.00 61.51 ? 97   ASP A O   1 
ATOM   629  C  CB  . ASP A 1 97  ? 31.677  128.875 57.653  1.00 63.39 ? 97   ASP A CB  1 
ATOM   630  C  CG  . ASP A 1 97  ? 31.286  129.400 56.280  1.00 66.24 ? 97   ASP A CG  1 
ATOM   631  O  OD1 . ASP A 1 97  ? 30.884  128.584 55.430  1.00 67.71 ? 97   ASP A OD1 1 
ATOM   632  O  OD2 . ASP A 1 97  ? 31.392  130.626 56.069  1.00 63.27 ? 97   ASP A OD2 1 
ATOM   633  N  N   . GLY A 1 98  ? 30.241  125.619 56.876  1.00 60.00 ? 98   GLY A N   1 
ATOM   634  C  CA  . GLY A 1 98  ? 28.962  124.909 56.665  1.00 60.78 ? 98   GLY A CA  1 
ATOM   635  C  C   . GLY A 1 98  ? 27.916  125.771 55.967  1.00 59.32 ? 98   GLY A C   1 
ATOM   636  O  O   . GLY A 1 98  ? 26.711  125.529 56.190  1.00 62.08 ? 98   GLY A O   1 
ATOM   637  N  N   . ARG A 1 99  ? 28.344  126.746 55.159  1.00 55.94 ? 99   ARG A N   1 
ATOM   638  C  CA  . ARG A 1 99  ? 27.430  127.561 54.305  1.00 51.92 ? 99   ARG A CA  1 
ATOM   639  C  C   . ARG A 1 99  ? 27.422  126.955 52.900  1.00 47.07 ? 99   ARG A C   1 
ATOM   640  O  O   . ARG A 1 99  ? 28.393  126.247 52.556  1.00 49.06 ? 99   ARG A O   1 
ATOM   641  C  CB  . ARG A 1 99  ? 27.858  129.031 54.264  1.00 53.36 ? 99   ARG A CB  1 
ATOM   642  C  CG  . ARG A 1 99  ? 27.297  129.872 55.401  1.00 56.58 ? 99   ARG A CG  1 
ATOM   643  C  CD  . ARG A 1 99  ? 27.471  131.352 55.131  1.00 58.23 ? 99   ARG A CD  1 
ATOM   644  N  NE  . ARG A 1 99  ? 28.883  131.708 55.046  1.00 59.54 ? 99   ARG A NE  1 
ATOM   645  C  CZ  . ARG A 1 99  ? 29.361  132.842 54.536  1.00 59.76 ? 99   ARG A CZ  1 
ATOM   646  N  NH1 . ARG A 1 99  ? 28.548  133.761 54.043  1.00 57.75 ? 99   ARG A NH1 1 
ATOM   647  N  NH2 . ARG A 1 99  ? 30.663  133.053 54.517  1.00 62.91 ? 99   ARG A NH2 1 
ATOM   648  N  N   . SER A 1 100 ? 26.385  127.253 52.113  1.00 42.71 ? 100  SER A N   1 
ATOM   649  C  CA  A SER A 1 100 ? 26.163  126.656 50.768  0.40 39.62 ? 100  SER A CA  1 
ATOM   650  C  CA  B SER A 1 100 ? 26.172  126.656 50.766  0.60 40.58 ? 100  SER A CA  1 
ATOM   651  C  C   . SER A 1 100 ? 26.414  127.712 49.687  1.00 37.53 ? 100  SER A C   1 
ATOM   652  O  O   . SER A 1 100 ? 25.828  128.803 49.795  1.00 37.84 ? 100  SER A O   1 
ATOM   653  C  CB  A SER A 1 100 ? 24.776  126.077 50.656  0.40 38.82 ? 100  SER A CB  1 
ATOM   654  C  CB  B SER A 1 100 ? 24.798  126.061 50.641  0.60 40.92 ? 100  SER A CB  1 
ATOM   655  O  OG  A SER A 1 100 ? 24.621  125.367 49.438  0.40 37.60 ? 100  SER A OG  1 
ATOM   656  O  OG  B SER A 1 100 ? 24.669  124.938 51.494  0.60 42.87 ? 100  SER A OG  1 
ATOM   657  N  N   . PHE A 1 101 ? 27.245  127.376 48.700  1.00 36.22 ? 101  PHE A N   1 
ATOM   658  C  CA  . PHE A 1 101 ? 27.558  128.240 47.532  1.00 34.48 ? 101  PHE A CA  1 
ATOM   659  C  C   . PHE A 1 101 ? 27.414  127.443 46.242  1.00 32.92 ? 101  PHE A C   1 
ATOM   660  O  O   . PHE A 1 101 ? 27.871  126.286 46.184  1.00 32.64 ? 101  PHE A O   1 
ATOM   661  C  CB  . PHE A 1 101 ? 28.961  128.834 47.652  1.00 34.64 ? 101  PHE A CB  1 
ATOM   662  C  CG  . PHE A 1 101 ? 29.042  129.898 48.711  1.00 34.72 ? 101  PHE A CG  1 
ATOM   663  C  CD1 . PHE A 1 101 ? 28.717  131.212 48.419  1.00 35.33 ? 101  PHE A CD1 1 
ATOM   664  C  CD2 . PHE A 1 101 ? 29.394  129.575 50.011  1.00 36.40 ? 101  PHE A CD2 1 
ATOM   665  C  CE1 . PHE A 1 101 ? 28.766  132.190 49.401  1.00 35.68 ? 101  PHE A CE1 1 
ATOM   666  C  CE2 . PHE A 1 101 ? 29.448  130.555 50.991  1.00 37.34 ? 101  PHE A CE2 1 
ATOM   667  C  CZ  . PHE A 1 101 ? 29.128  131.859 50.685  1.00 35.93 ? 101  PHE A CZ  1 
ATOM   668  N  N   . ASP A 1 102 ? 26.783  128.064 45.243  1.00 31.40 ? 102  ASP A N   1 
ATOM   669  C  CA  . ASP A 1 102 ? 26.779  127.576 43.842  1.00 31.47 ? 102  ASP A CA  1 
ATOM   670  C  C   . ASP A 1 102 ? 28.091  128.042 43.207  1.00 30.29 ? 102  ASP A C   1 
ATOM   671  O  O   . ASP A 1 102 ? 28.306  129.263 43.134  1.00 28.83 ? 102  ASP A O   1 
ATOM   672  C  CB  . ASP A 1 102 ? 25.526  128.055 43.107  1.00 31.96 ? 102  ASP A CB  1 
ATOM   673  C  CG  . ASP A 1 102 ? 24.233  127.589 43.760  1.00 32.77 ? 102  ASP A CG  1 
ATOM   674  O  OD1 . ASP A 1 102 ? 24.270  126.581 44.506  1.00 32.96 ? 102  ASP A OD1 1 
ATOM   675  O  OD2 . ASP A 1 102 ? 23.206  128.236 43.524  1.00 35.64 ? 102  ASP A OD2 1 
ATOM   676  N  N   . ILE A 1 103 ? 28.950  127.097 42.814  1.00 30.20 ? 103  ILE A N   1 
ATOM   677  C  CA  . ILE A 1 103 ? 30.324  127.390 42.322  1.00 29.84 ? 103  ILE A CA  1 
ATOM   678  C  C   . ILE A 1 103 ? 30.408  127.050 40.834  1.00 30.85 ? 103  ILE A C   1 
ATOM   679  O  O   . ILE A 1 103 ? 29.982  125.944 40.446  1.00 32.00 ? 103  ILE A O   1 
ATOM   680  C  CB  . ILE A 1 103 ? 31.379  126.629 43.140  1.00 30.92 ? 103  ILE A CB  1 
ATOM   681  C  CG1 . ILE A 1 103 ? 31.351  127.072 44.606  1.00 31.26 ? 103  ILE A CG1 1 
ATOM   682  C  CG2 . ILE A 1 103 ? 32.751  126.786 42.495  1.00 31.76 ? 103  ILE A CG2 1 
ATOM   683  C  CD1 . ILE A 1 103 ? 32.489  126.538 45.451  1.00 31.18 ? 103  ILE A CD1 1 
ATOM   684  N  N   . SER A 1 104 ? 30.931  127.986 40.049  1.00 30.03 ? 104  SER A N   1 
ATOM   685  C  CA  . SER A 1 104 ? 31.337  127.780 38.635  1.00 31.44 ? 104  SER A CA  1 
ATOM   686  C  C   . SER A 1 104 ? 32.863  127.864 38.543  1.00 30.87 ? 104  SER A C   1 
ATOM   687  O  O   . SER A 1 104 ? 33.462  128.788 39.131  1.00 32.07 ? 104  SER A O   1 
ATOM   688  C  CB  . SER A 1 104 ? 30.656  128.754 37.706  1.00 31.81 ? 104  SER A CB  1 
ATOM   689  O  OG  . SER A 1 104 ? 31.151  128.605 36.382  1.00 35.62 ? 104  SER A OG  1 
ATOM   690  N  N   . LEU A 1 105 ? 33.464  126.908 37.846  1.00 31.72 ? 105  LEU A N   1 
ATOM   691  C  CA  . LEU A 1 105 ? 34.929  126.685 37.819  1.00 33.39 ? 105  LEU A CA  1 
ATOM   692  C  C   . LEU A 1 105 ? 35.359  126.415 36.374  1.00 33.31 ? 105  LEU A C   1 
ATOM   693  O  O   . LEU A 1 105 ? 34.750  125.523 35.745  1.00 34.62 ? 105  LEU A O   1 
ATOM   694  C  CB  . LEU A 1 105 ? 35.222  125.491 38.735  1.00 36.10 ? 105  LEU A CB  1 
ATOM   695  C  CG  . LEU A 1 105 ? 36.675  125.034 38.793  1.00 39.47 ? 105  LEU A CG  1 
ATOM   696  C  CD1 . LEU A 1 105 ? 37.529  126.056 39.522  1.00 42.78 ? 105  LEU A CD1 1 
ATOM   697  C  CD2 . LEU A 1 105 ? 36.785  123.683 39.470  1.00 40.39 ? 105  LEU A CD2 1 
ATOM   698  N  N   . HIS A 1 106 ? 36.356  127.153 35.874  1.00 30.28 ? 106  HIS A N   1 
ATOM   699  C  CA  . HIS A 1 106 ? 36.996  126.897 34.557  1.00 31.44 ? 106  HIS A CA  1 
ATOM   700  C  C   . HIS A 1 106 ? 38.459  127.345 34.563  1.00 32.81 ? 106  HIS A C   1 
ATOM   701  O  O   . HIS A 1 106 ? 38.864  128.123 35.448  1.00 31.34 ? 106  HIS A O   1 
ATOM   702  C  CB  . HIS A 1 106 ? 36.223  127.574 33.419  1.00 29.31 ? 106  HIS A CB  1 
ATOM   703  C  CG  . HIS A 1 106 ? 36.385  129.053 33.367  1.00 27.85 ? 106  HIS A CG  1 
ATOM   704  N  ND1 . HIS A 1 106 ? 35.589  129.903 34.108  1.00 27.35 ? 106  HIS A ND1 1 
ATOM   705  C  CD2 . HIS A 1 106 ? 37.234  129.834 32.664  1.00 28.09 ? 106  HIS A CD2 1 
ATOM   706  C  CE1 . HIS A 1 106 ? 35.930  131.147 33.853  1.00 26.79 ? 106  HIS A CE1 1 
ATOM   707  N  NE2 . HIS A 1 106 ? 36.938  131.133 32.970  1.00 28.19 ? 106  HIS A NE2 1 
ATOM   708  N  N   . ARG A 1 107 ? 39.199  126.855 33.574  1.00 36.20 ? 107  ARG A N   1 
ATOM   709  C  CA  . ARG A 1 107 ? 40.608  127.220 33.298  1.00 39.73 ? 107  ARG A CA  1 
ATOM   710  C  C   . ARG A 1 107 ? 40.674  127.847 31.906  1.00 36.13 ? 107  ARG A C   1 
ATOM   711  O  O   . ARG A 1 107 ? 40.199  127.208 30.971  1.00 34.98 ? 107  ARG A O   1 
ATOM   712  C  CB  . ARG A 1 107 ? 41.492  125.975 33.368  1.00 44.44 ? 107  ARG A CB  1 
ATOM   713  C  CG  . ARG A 1 107 ? 42.442  125.944 34.555  1.00 52.79 ? 107  ARG A CG  1 
ATOM   714  C  CD  . ARG A 1 107 ? 43.697  125.181 34.183  1.00 56.47 ? 107  ARG A CD  1 
ATOM   715  N  NE  . ARG A 1 107 ? 43.391  123.786 33.897  1.00 60.30 ? 107  ARG A NE  1 
ATOM   716  C  CZ  . ARG A 1 107 ? 43.759  122.747 34.642  1.00 64.54 ? 107  ARG A CZ  1 
ATOM   717  N  NH1 . ARG A 1 107 ? 44.485  122.920 35.735  1.00 67.77 ? 107  ARG A NH1 1 
ATOM   718  N  NH2 . ARG A 1 107 ? 43.406  121.525 34.281  1.00 64.78 ? 107  ARG A NH2 1 
ATOM   719  N  N   . TYR A 1 108 ? 41.215  129.058 31.800  1.00 33.65 ? 108  TYR A N   1 
ATOM   720  C  CA  . TYR A 1 108 ? 41.460  129.747 30.511  1.00 36.12 ? 108  TYR A CA  1 
ATOM   721  C  C   . TYR A 1 108 ? 42.636  130.706 30.684  1.00 37.95 ? 108  TYR A C   1 
ATOM   722  O  O   . TYR A 1 108 ? 42.728  131.364 31.746  1.00 39.80 ? 108  TYR A O   1 
ATOM   723  C  CB  . TYR A 1 108 ? 40.192  130.456 30.037  1.00 35.39 ? 108  TYR A CB  1 
ATOM   724  C  CG  . TYR A 1 108 ? 40.274  131.033 28.647  1.00 36.98 ? 108  TYR A CG  1 
ATOM   725  C  CD1 . TYR A 1 108 ? 40.662  130.260 27.561  1.00 37.04 ? 108  TYR A CD1 1 
ATOM   726  C  CD2 . TYR A 1 108 ? 39.941  132.356 28.414  1.00 36.92 ? 108  TYR A CD2 1 
ATOM   727  C  CE1 . TYR A 1 108 ? 40.722  130.790 26.281  1.00 35.68 ? 108  TYR A CE1 1 
ATOM   728  C  CE2 . TYR A 1 108 ? 39.979  132.896 27.140  1.00 38.90 ? 108  TYR A CE2 1 
ATOM   729  C  CZ  . TYR A 1 108 ? 40.372  132.112 26.070  1.00 37.50 ? 108  TYR A CZ  1 
ATOM   730  O  OH  . TYR A 1 108 ? 40.423  132.683 24.832  1.00 36.60 ? 108  TYR A OH  1 
ATOM   731  N  N   . LYS A 1 109 ? 43.508  130.763 29.675  1.00 38.22 ? 109  LYS A N   1 
ATOM   732  C  CA  . LYS A 1 109 ? 44.712  131.627 29.659  1.00 38.21 ? 109  LYS A CA  1 
ATOM   733  C  C   . LYS A 1 109 ? 45.552  131.311 30.901  1.00 38.26 ? 109  LYS A C   1 
ATOM   734  O  O   . LYS A 1 109 ? 45.932  132.249 31.608  1.00 36.27 ? 109  LYS A O   1 
ATOM   735  C  CB  . LYS A 1 109 ? 44.296  133.101 29.606  1.00 40.00 ? 109  LYS A CB  1 
ATOM   736  C  CG  . LYS A 1 109 ? 43.536  133.521 28.355  1.00 43.23 ? 109  LYS A CG  1 
ATOM   737  C  CD  . LYS A 1 109 ? 44.334  133.357 27.078  1.00 44.40 ? 109  LYS A CD  1 
ATOM   738  C  CE  . LYS A 1 109 ? 43.631  133.892 25.851  1.00 45.82 ? 109  LYS A CE  1 
ATOM   739  N  NZ  . LYS A 1 109 ? 44.394  133.587 24.616  1.00 47.95 ? 109  LYS A NZ  1 
ATOM   740  N  N   . SER A 1 110 ? 45.787  130.025 31.172  1.00 37.91 ? 110  SER A N   1 
ATOM   741  C  CA  . SER A 1 110 ? 46.630  129.541 32.302  1.00 41.05 ? 110  SER A CA  1 
ATOM   742  C  C   . SER A 1 110 ? 46.183  130.167 33.634  1.00 39.72 ? 110  SER A C   1 
ATOM   743  O  O   . SER A 1 110 ? 47.055  130.390 34.508  1.00 41.82 ? 110  SER A O   1 
ATOM   744  C  CB  . SER A 1 110 ? 48.094  129.828 32.036  1.00 41.16 ? 110  SER A CB  1 
ATOM   745  O  OG  . SER A 1 110 ? 48.428  129.538 30.685  1.00 45.66 ? 110  SER A OG  1 
ATOM   746  N  N   . THR A 1 111 ? 44.884  130.436 33.781  1.00 38.09 ? 111  THR A N   1 
ATOM   747  C  CA  . THR A 1 111 ? 44.264  131.007 35.011  1.00 38.42 ? 111  THR A CA  1 
ATOM   748  C  C   . THR A 1 111 ? 43.022  130.202 35.394  1.00 37.30 ? 111  THR A C   1 
ATOM   749  O  O   . THR A 1 111 ? 42.149  130.018 34.517  1.00 36.85 ? 111  THR A O   1 
ATOM   750  C  CB  . THR A 1 111 ? 43.869  132.472 34.801  1.00 39.97 ? 111  THR A CB  1 
ATOM   751  O  OG1 . THR A 1 111 ? 44.996  133.147 34.243  1.00 41.30 ? 111  THR A OG1 1 
ATOM   752  C  CG2 . THR A 1 111 ? 43.428  133.156 36.077  1.00 40.49 ? 111  THR A CG2 1 
ATOM   753  N  N   . THR A 1 112 ? 42.942  129.752 36.651  1.00 33.52 ? 112  THR A N   1 
ATOM   754  C  CA  . THR A 1 112 ? 41.731  129.091 37.209  1.00 32.78 ? 112  THR A CA  1 
ATOM   755  C  C   . THR A 1 112 ? 40.800  130.160 37.778  1.00 31.92 ? 112  THR A C   1 
ATOM   756  O  O   . THR A 1 112 ? 41.212  130.865 38.710  1.00 32.31 ? 112  THR A O   1 
ATOM   757  C  CB  . THR A 1 112 ? 42.073  128.016 38.246  1.00 33.82 ? 112  THR A CB  1 
ATOM   758  O  OG1 . THR A 1 112 ? 42.927  127.059 37.618  1.00 35.27 ? 112  THR A OG1 1 
ATOM   759  C  CG2 . THR A 1 112 ? 40.841  127.317 38.782  1.00 34.50 ? 112  THR A CG2 1 
ATOM   760  N  N   . ILE A 1 113 ? 39.591  130.270 37.225  1.00 29.47 ? 113  ILE A N   1 
ATOM   761  C  CA  . ILE A 1 113 ? 38.562  131.237 37.692  1.00 30.42 ? 113  ILE A CA  1 
ATOM   762  C  C   . ILE A 1 113 ? 37.506  130.450 38.463  1.00 29.53 ? 113  ILE A C   1 
ATOM   763  O  O   . ILE A 1 113 ? 37.022  129.428 37.955  1.00 31.03 ? 113  ILE A O   1 
ATOM   764  C  CB  . ILE A 1 113 ? 38.002  132.063 36.520  1.00 31.54 ? 113  ILE A CB  1 
ATOM   765  C  CG1 . ILE A 1 113 ? 39.098  132.971 35.949  1.00 31.88 ? 113  ILE A CG1 1 
ATOM   766  C  CG2 . ILE A 1 113 ? 36.770  132.853 36.944  1.00 31.02 ? 113  ILE A CG2 1 
ATOM   767  C  CD1 . ILE A 1 113 ? 38.822  133.504 34.564  1.00 32.96 ? 113  ILE A CD1 1 
ATOM   768  N  N   . ILE A 1 114 ? 37.228  130.891 39.684  1.00 28.49 ? 114  ILE A N   1 
ATOM   769  C  CA  . ILE A 1 114 ? 36.235  130.267 40.598  1.00 27.05 ? 114  ILE A CA  1 
ATOM   770  C  C   . ILE A 1 114 ? 35.196  131.336 40.920  1.00 26.31 ? 114  ILE A C   1 
ATOM   771  O  O   . ILE A 1 114 ? 35.582  132.396 41.425  1.00 26.03 ? 114  ILE A O   1 
ATOM   772  C  CB  . ILE A 1 114 ? 36.913  129.709 41.863  1.00 28.36 ? 114  ILE A CB  1 
ATOM   773  C  CG1 . ILE A 1 114 ? 38.200  128.953 41.528  1.00 30.40 ? 114  ILE A CG1 1 
ATOM   774  C  CG2 . ILE A 1 114 ? 35.931  128.855 42.653  1.00 28.36 ? 114  ILE A CG2 1 
ATOM   775  C  CD1 . ILE A 1 114 ? 39.017  128.554 42.740  1.00 31.95 ? 114  ILE A CD1 1 
ATOM   776  N  N   . GLU A 1 115 ? 33.934  131.058 40.606  1.00 26.02 ? 115  GLU A N   1 
ATOM   777  C  CA  . GLU A 1 115 ? 32.809  132.009 40.763  1.00 25.58 ? 115  GLU A CA  1 
ATOM   778  C  C   . GLU A 1 115 ? 31.837  131.429 41.787  1.00 26.13 ? 115  GLU A C   1 
ATOM   779  O  O   . GLU A 1 115 ? 31.506  130.244 41.670  1.00 24.57 ? 115  GLU A O   1 
ATOM   780  C  CB  . GLU A 1 115 ? 32.159  132.256 39.409  1.00 26.89 ? 115  GLU A CB  1 
ATOM   781  C  CG  . GLU A 1 115 ? 33.122  132.856 38.404  1.00 27.73 ? 115  GLU A CG  1 
ATOM   782  C  CD  . GLU A 1 115 ? 32.469  133.195 37.081  1.00 28.51 ? 115  GLU A CD  1 
ATOM   783  O  OE1 . GLU A 1 115 ? 32.280  132.264 36.266  1.00 30.91 ? 115  GLU A OE1 1 
ATOM   784  O  OE2 . GLU A 1 115 ? 32.129  134.378 36.887  1.00 29.11 ? 115  GLU A OE2 1 
ATOM   785  N  N   . PHE A 1 116 ? 31.439  132.239 42.766  1.00 25.35 ? 116  PHE A N   1 
ATOM   786  C  CA  . PHE A 1 116 ? 30.609  131.820 43.920  1.00 27.24 ? 116  PHE A CA  1 
ATOM   787  C  C   . PHE A 1 116 ? 29.325  132.646 43.943  1.00 27.86 ? 116  PHE A C   1 
ATOM   788  O  O   . PHE A 1 116 ? 29.399  133.883 43.786  1.00 28.09 ? 116  PHE A O   1 
ATOM   789  C  CB  . PHE A 1 116 ? 31.345  132.037 45.246  1.00 27.84 ? 116  PHE A CB  1 
ATOM   790  C  CG  . PHE A 1 116 ? 32.693  131.376 45.388  1.00 28.38 ? 116  PHE A CG  1 
ATOM   791  C  CD1 . PHE A 1 116 ? 33.825  131.938 44.814  1.00 28.54 ? 116  PHE A CD1 1 
ATOM   792  C  CD2 . PHE A 1 116 ? 32.843  130.236 46.165  1.00 28.81 ? 116  PHE A CD2 1 
ATOM   793  C  CE1 . PHE A 1 116 ? 35.071  131.362 44.995  1.00 28.60 ? 116  PHE A CE1 1 
ATOM   794  C  CE2 . PHE A 1 116 ? 34.092  129.663 46.346  1.00 28.56 ? 116  PHE A CE2 1 
ATOM   795  C  CZ  . PHE A 1 116 ? 35.199  130.221 45.751  1.00 28.67 ? 116  PHE A CZ  1 
ATOM   796  N  N   . GLU A 1 117 ? 28.193  131.976 44.158  1.00 28.79 ? 117  GLU A N   1 
ATOM   797  C  CA  . GLU A 1 117 ? 26.889  132.620 44.440  1.00 29.92 ? 117  GLU A CA  1 
ATOM   798  C  C   . GLU A 1 117 ? 26.296  131.962 45.675  1.00 31.00 ? 117  GLU A C   1 
ATOM   799  O  O   . GLU A 1 117 ? 26.365  130.744 45.803  1.00 30.47 ? 117  GLU A O   1 
ATOM   800  C  CB  . GLU A 1 117 ? 25.907  132.436 43.285  1.00 30.59 ? 117  GLU A CB  1 
ATOM   801  C  CG  . GLU A 1 117 ? 26.426  132.892 41.938  1.00 32.73 ? 117  GLU A CG  1 
ATOM   802  C  CD  . GLU A 1 117 ? 25.626  132.258 40.815  1.00 32.79 ? 117  GLU A CD  1 
ATOM   803  O  OE1 . GLU A 1 117 ? 26.163  131.363 40.140  1.00 34.85 ? 117  GLU A OE1 1 
ATOM   804  O  OE2 . GLU A 1 117 ? 24.449  132.622 40.666  1.00 33.74 ? 117  GLU A OE2 1 
ATOM   805  N  N   . PRO A 1 118 ? 25.684  132.726 46.605  1.00 33.98 ? 118  PRO A N   1 
ATOM   806  C  CA  . PRO A 1 118 ? 24.936  132.114 47.704  1.00 36.87 ? 118  PRO A CA  1 
ATOM   807  C  C   . PRO A 1 118 ? 23.863  131.184 47.118  1.00 36.55 ? 118  PRO A C   1 
ATOM   808  O  O   . PRO A 1 118 ? 23.163  131.624 46.231  1.00 35.49 ? 118  PRO A O   1 
ATOM   809  C  CB  . PRO A 1 118 ? 24.331  133.309 48.457  1.00 36.99 ? 118  PRO A CB  1 
ATOM   810  C  CG  . PRO A 1 118 ? 25.198  134.489 48.067  1.00 37.51 ? 118  PRO A CG  1 
ATOM   811  C  CD  . PRO A 1 118 ? 25.666  134.194 46.655  1.00 35.06 ? 118  PRO A CD  1 
ATOM   812  N  N   . SER A 1 119 ? 23.806  129.929 47.580  1.00 37.11 ? 119  SER A N   1 
ATOM   813  C  CA  . SER A 1 119 ? 22.837  128.895 47.114  1.00 41.08 ? 119  SER A CA  1 
ATOM   814  C  C   . SER A 1 119 ? 21.402  129.257 47.513  1.00 45.23 ? 119  SER A C   1 
ATOM   815  O  O   . SER A 1 119 ? 21.226  130.081 48.432  1.00 48.06 ? 119  SER A O   1 
ATOM   816  C  CB  . SER A 1 119 ? 23.177  127.542 47.657  1.00 40.17 ? 119  SER A CB  1 
ATOM   817  O  OG  . SER A 1 119 ? 24.468  127.152 47.248  1.00 37.83 ? 119  SER A OG  1 
ATOM   818  N  N   . GLY A 1 120 ? 20.426  128.622 46.855  1.00 50.18 ? 120  GLY A N   1 
ATOM   819  C  CA  . GLY A 1 120 ? 18.985  128.713 47.166  1.00 53.73 ? 120  GLY A CA  1 
ATOM   820  C  C   . GLY A 1 120 ? 18.279  127.389 46.923  1.00 54.41 ? 120  GLY A C   1 
ATOM   821  O  O   . GLY A 1 120 ? 18.875  126.357 47.294  1.00 54.98 ? 120  GLY A O   1 
ATOM   822  N  N   . PRO A 1 125 ? 17.624  120.235 38.150  1.00 57.97 ? 125  PRO A N   1 
ATOM   823  C  CA  . PRO A 1 125 ? 17.835  120.718 36.786  1.00 57.09 ? 125  PRO A CA  1 
ATOM   824  C  C   . PRO A 1 125 ? 17.188  119.828 35.712  1.00 56.42 ? 125  PRO A C   1 
ATOM   825  O  O   . PRO A 1 125 ? 16.440  120.360 34.914  1.00 48.93 ? 125  PRO A O   1 
ATOM   826  C  CB  . PRO A 1 125 ? 19.371  120.724 36.683  1.00 57.11 ? 125  PRO A CB  1 
ATOM   827  C  CG  . PRO A 1 125 ? 19.832  120.994 38.107  1.00 56.92 ? 125  PRO A CG  1 
ATOM   828  C  CD  . PRO A 1 125 ? 18.824  120.277 38.990  1.00 57.57 ? 125  PRO A CD  1 
ATOM   829  N  N   . LEU A 1 126 ? 17.476  118.519 35.724  1.00 53.73 ? 126  LEU A N   1 
ATOM   830  C  CA  . LEU A 1 126 ? 16.929  117.524 34.756  1.00 53.25 ? 126  LEU A CA  1 
ATOM   831  C  C   . LEU A 1 126 ? 15.399  117.651 34.691  1.00 50.49 ? 126  LEU A C   1 
ATOM   832  O  O   . LEU A 1 126 ? 14.858  117.622 33.573  1.00 45.57 ? 126  LEU A O   1 
ATOM   833  C  CB  . LEU A 1 126 ? 17.348  116.113 35.182  1.00 53.56 ? 126  LEU A CB  1 
ATOM   834  N  N   . GLY A 1 127 ? 14.750  117.811 35.852  1.00 49.79 ? 127  GLY A N   1 
ATOM   835  C  CA  . GLY A 1 127 ? 13.282  117.899 36.016  1.00 46.59 ? 127  GLY A CA  1 
ATOM   836  C  C   . GLY A 1 127 ? 12.669  119.098 35.304  1.00 43.41 ? 127  GLY A C   1 
ATOM   837  O  O   . GLY A 1 127 ? 11.737  118.887 34.502  1.00 40.54 ? 127  GLY A O   1 
ATOM   838  N  N   . THR A 1 128 ? 13.146  120.314 35.597  1.00 39.40 ? 128  THR A N   1 
ATOM   839  C  CA  . THR A 1 128 ? 12.715  121.577 34.923  1.00 38.58 ? 128  THR A CA  1 
ATOM   840  C  C   . THR A 1 128 ? 12.990  121.474 33.413  1.00 34.92 ? 128  THR A C   1 
ATOM   841  O  O   . THR A 1 128 ? 12.069  121.748 32.621  1.00 34.36 ? 128  THR A O   1 
ATOM   842  C  CB  . THR A 1 128 ? 13.409  122.803 35.529  1.00 40.05 ? 128  THR A CB  1 
ATOM   843  O  OG1 . THR A 1 128 ? 13.184  122.778 36.939  1.00 43.17 ? 128  THR A OG1 1 
ATOM   844  C  CG2 . THR A 1 128 ? 12.920  124.114 34.954  1.00 40.73 ? 128  THR A CG2 1 
ATOM   845  N  N   . ALA A 1 129 ? 14.199  121.055 33.034  1.00 33.06 ? 129  ALA A N   1 
ATOM   846  C  CA  . ALA A 1 129 ? 14.629  120.873 31.626  1.00 34.22 ? 129  ALA A CA  1 
ATOM   847  C  C   . ALA A 1 129 ? 13.668  119.915 30.908  1.00 35.09 ? 129  ALA A C   1 
ATOM   848  O  O   . ALA A 1 129 ? 13.103  120.315 29.875  1.00 34.72 ? 129  ALA A O   1 
ATOM   849  C  CB  . ALA A 1 129 ? 16.045  120.369 31.582  1.00 33.32 ? 129  ALA A CB  1 
ATOM   850  N  N   . ARG A 1 130 ? 13.464  118.714 31.464  1.00 34.26 ? 130  ARG A N   1 
ATOM   851  C  CA  . ARG A 1 130 ? 12.587  117.656 30.876  1.00 34.24 ? 130  ARG A CA  1 
ATOM   852  C  C   . ARG A 1 130 ? 11.184  118.230 30.623  1.00 33.57 ? 130  ARG A C   1 
ATOM   853  O  O   . ARG A 1 130 ? 10.662  118.035 29.516  1.00 30.43 ? 130  ARG A O   1 
ATOM   854  C  CB  . ARG A 1 130 ? 12.531  116.419 31.782  1.00 34.81 ? 130  ARG A CB  1 
ATOM   855  N  N   . LYS A 1 131 ? 10.613  118.945 31.595  1.00 34.90 ? 131  LYS A N   1 
ATOM   856  C  CA  . LYS A 1 131 ? 9.254   119.549 31.482  1.00 37.11 ? 131  LYS A CA  1 
ATOM   857  C  C   . LYS A 1 131 ? 9.216   120.584 30.345  1.00 35.46 ? 131  LYS A C   1 
ATOM   858  O  O   . LYS A 1 131 ? 8.192   120.630 29.634  1.00 33.89 ? 131  LYS A O   1 
ATOM   859  C  CB  . LYS A 1 131 ? 8.813   120.170 32.810  1.00 41.35 ? 131  LYS A CB  1 
ATOM   860  C  CG  . LYS A 1 131 ? 8.359   119.162 33.858  1.00 47.10 ? 131  LYS A CG  1 
ATOM   861  C  CD  . LYS A 1 131 ? 8.191   119.737 35.245  1.00 52.20 ? 131  LYS A CD  1 
ATOM   862  C  CE  . LYS A 1 131 ? 8.055   118.659 36.300  1.00 58.30 ? 131  LYS A CE  1 
ATOM   863  N  NZ  . LYS A 1 131 ? 8.189   119.212 37.669  1.00 63.34 ? 131  LYS A NZ  1 
ATOM   864  N  N   . MET A 1 132 ? 10.261  121.400 30.183  1.00 32.02 ? 132  MET A N   1 
ATOM   865  C  CA  . MET A 1 132 ? 10.304  122.439 29.116  1.00 32.60 ? 132  MET A CA  1 
ATOM   866  C  C   . MET A 1 132 ? 10.437  121.742 27.757  1.00 30.60 ? 132  MET A C   1 
ATOM   867  O  O   . MET A 1 132 ? 9.674   122.075 26.847  1.00 31.00 ? 132  MET A O   1 
ATOM   868  C  CB  . MET A 1 132 ? 11.475  123.407 29.309  1.00 32.99 ? 132  MET A CB  1 
ATOM   869  C  CG  . MET A 1 132 ? 11.357  124.274 30.554  1.00 34.91 ? 132  MET A CG  1 
ATOM   870  S  SD  . MET A 1 132 ? 12.771  125.405 30.707  1.00 36.92 ? 132  MET A SD  1 
ATOM   871  C  CE  . MET A 1 132 ? 12.249  126.689 29.574  1.00 36.69 ? 132  MET A CE  1 
ATOM   872  N  N   . VAL A 1 133 ? 11.371  120.798 27.644  1.00 29.80 ? 133  VAL A N   1 
ATOM   873  C  CA  . VAL A 1 133 ? 11.664  120.061 26.383  1.00 29.78 ? 133  VAL A CA  1 
ATOM   874  C  C   . VAL A 1 133 ? 10.424  119.270 25.941  1.00 30.24 ? 133  VAL A C   1 
ATOM   875  O  O   . VAL A 1 133 ? 10.180  119.193 24.715  1.00 31.34 ? 133  VAL A O   1 
ATOM   876  C  CB  . VAL A 1 133 ? 12.901  119.158 26.544  1.00 29.89 ? 133  VAL A CB  1 
ATOM   877  C  CG1 . VAL A 1 133 ? 13.044  118.183 25.389  1.00 29.44 ? 133  VAL A CG1 1 
ATOM   878  C  CG2 . VAL A 1 133 ? 14.167  119.985 26.708  1.00 29.06 ? 133  VAL A CG2 1 
ATOM   879  N  N   . ASP A 1 134 ? 9.666   118.693 26.876  1.00 30.00 ? 134  ASP A N   1 
ATOM   880  C  CA  . ASP A 1 134 ? 8.441   117.918 26.538  1.00 32.55 ? 134  ASP A CA  1 
ATOM   881  C  C   . ASP A 1 134 ? 7.411   118.833 25.869  1.00 31.88 ? 134  ASP A C   1 
ATOM   882  O  O   . ASP A 1 134 ? 6.618   118.325 25.078  1.00 31.24 ? 134  ASP A O   1 
ATOM   883  C  CB  . ASP A 1 134 ? 7.856   117.199 27.753  1.00 34.22 ? 134  ASP A CB  1 
ATOM   884  C  CG  . ASP A 1 134 ? 8.624   115.932 28.101  1.00 38.03 ? 134  ASP A CG  1 
ATOM   885  O  OD1 . ASP A 1 134 ? 9.332   115.403 27.212  1.00 42.11 ? 134  ASP A OD1 1 
ATOM   886  O  OD2 . ASP A 1 134 ? 8.536   115.498 29.261  1.00 40.22 ? 134  ASP A OD2 1 
ATOM   887  N  N   . ARG A 1 135 ? 7.446   120.138 26.140  1.00 32.12 ? 135  ARG A N   1 
ATOM   888  C  CA  . ARG A 1 135 ? 6.444   121.087 25.584  1.00 31.78 ? 135  ARG A CA  1 
ATOM   889  C  C   . ARG A 1 135 ? 6.883   121.636 24.215  1.00 30.17 ? 135  ARG A C   1 
ATOM   890  O  O   . ARG A 1 135 ? 6.065   122.346 23.599  1.00 30.01 ? 135  ARG A O   1 
ATOM   891  C  CB  . ARG A 1 135 ? 6.154   122.153 26.636  1.00 33.38 ? 135  ARG A CB  1 
ATOM   892  C  CG  . ARG A 1 135 ? 5.383   121.572 27.813  1.00 33.61 ? 135  ARG A CG  1 
ATOM   893  C  CD  . ARG A 1 135 ? 5.032   122.599 28.857  1.00 34.34 ? 135  ARG A CD  1 
ATOM   894  N  NE  . ARG A 1 135 ? 4.143   123.622 28.340  1.00 34.60 ? 135  ARG A NE  1 
ATOM   895  C  CZ  . ARG A 1 135 ? 3.749   124.693 29.024  1.00 37.53 ? 135  ARG A CZ  1 
ATOM   896  N  NH1 . ARG A 1 135 ? 4.156   124.871 30.270  1.00 38.84 ? 135  ARG A NH1 1 
ATOM   897  N  NH2 . ARG A 1 135 ? 2.952   125.586 28.463  1.00 38.42 ? 135  ARG A NH2 1 
ATOM   898  N  N   . ILE A 1 136 ? 8.077   121.295 23.718  1.00 29.19 ? 136  ILE A N   1 
ATOM   899  C  CA  . ILE A 1 136 ? 8.540   121.754 22.371  1.00 31.24 ? 136  ILE A CA  1 
ATOM   900  C  C   . ILE A 1 136 ? 8.845   120.567 21.450  1.00 31.06 ? 136  ILE A C   1 
ATOM   901  O  O   . ILE A 1 136 ? 8.830   120.789 20.232  1.00 30.16 ? 136  ILE A O   1 
ATOM   902  C  CB  . ILE A 1 136 ? 9.742   122.717 22.453  1.00 31.12 ? 136  ILE A CB  1 
ATOM   903  C  CG1 . ILE A 1 136 ? 10.958  122.088 23.133  1.00 32.10 ? 136  ILE A CG1 1 
ATOM   904  C  CG2 . ILE A 1 136 ? 9.327   124.012 23.121  1.00 32.24 ? 136  ILE A CG2 1 
ATOM   905  C  CD1 . ILE A 1 136 ? 12.277  122.655 22.661  1.00 33.95 ? 136  ILE A CD1 1 
ATOM   906  N  N   . ARG A 1 137 ? 9.118   119.374 21.986  1.00 32.34 ? 137  ARG A N   1 
ATOM   907  C  CA  . ARG A 1 137 ? 9.640   118.233 21.175  1.00 35.49 ? 137  ARG A CA  1 
ATOM   908  C  C   . ARG A 1 137 ? 8.608   117.750 20.143  1.00 33.79 ? 137  ARG A C   1 
ATOM   909  O  O   . ARG A 1 137 ? 9.033   117.079 19.199  1.00 35.34 ? 137  ARG A O   1 
ATOM   910  C  CB  . ARG A 1 137 ? 10.101  117.080 22.070  1.00 38.61 ? 137  ARG A CB  1 
ATOM   911  C  CG  . ARG A 1 137 ? 8.989   116.200 22.617  1.00 42.58 ? 137  ARG A CG  1 
ATOM   912  C  CD  . ARG A 1 137 ? 9.488   115.415 23.818  1.00 47.81 ? 137  ARG A CD  1 
ATOM   913  N  NE  . ARG A 1 137 ? 10.705  114.666 23.519  1.00 51.95 ? 137  ARG A NE  1 
ATOM   914  C  CZ  . ARG A 1 137 ? 11.682  114.396 24.387  1.00 55.45 ? 137  ARG A CZ  1 
ATOM   915  N  NH1 . ARG A 1 137 ? 12.737  113.700 23.996  1.00 56.88 ? 137  ARG A NH1 1 
ATOM   916  N  NH2 . ARG A 1 137 ? 11.616  114.823 25.637  1.00 57.46 ? 137  ARG A NH2 1 
ATOM   917  N  N   . GLU A 1 138 ? 7.324   118.081 20.296  1.00 34.14 ? 138  GLU A N   1 
ATOM   918  C  CA  . GLU A 1 138 ? 6.255   117.686 19.338  1.00 36.72 ? 138  GLU A CA  1 
ATOM   919  C  C   . GLU A 1 138 ? 6.038   118.765 18.265  1.00 35.56 ? 138  GLU A C   1 
ATOM   920  O  O   . GLU A 1 138 ? 5.345   118.450 17.284  1.00 34.32 ? 138  GLU A O   1 
ATOM   921  C  CB  . GLU A 1 138 ? 4.934   117.413 20.060  1.00 40.42 ? 138  GLU A CB  1 
ATOM   922  C  CG  . GLU A 1 138 ? 4.984   116.223 20.998  1.00 43.66 ? 138  GLU A CG  1 
ATOM   923  C  CD  . GLU A 1 138 ? 3.687   115.960 21.748  1.00 48.73 ? 138  GLU A CD  1 
ATOM   924  O  OE1 . GLU A 1 138 ? 2.834   116.881 21.823  1.00 50.18 ? 138  GLU A OE1 1 
ATOM   925  O  OE2 . GLU A 1 138 ? 3.525   114.830 22.242  1.00 52.78 ? 138  GLU A OE2 1 
ATOM   926  N  N   . ALA A 1 139 ? 6.575   119.983 18.426  1.00 32.81 ? 139  ALA A N   1 
ATOM   927  C  CA  . ALA A 1 139 ? 6.519   121.033 17.375  1.00 32.08 ? 139  ALA A CA  1 
ATOM   928  C  C   . ALA A 1 139 ? 6.989   120.404 16.058  1.00 31.35 ? 139  ALA A C   1 
ATOM   929  O  O   . ALA A 1 139 ? 8.060   119.779 16.079  1.00 30.77 ? 139  ALA A O   1 
ATOM   930  C  CB  . ALA A 1 139 ? 7.364   122.233 17.747  1.00 29.37 ? 139  ALA A CB  1 
ATOM   931  N  N   . ASP A 1 140 ? 6.223   120.547 14.971  1.00 33.91 ? 140  ASP A N   1 
ATOM   932  C  CA  . ASP A 1 140 ? 6.556   119.932 13.651  1.00 37.60 ? 140  ASP A CA  1 
ATOM   933  C  C   . ASP A 1 140 ? 6.747   121.006 12.569  1.00 34.28 ? 140  ASP A C   1 
ATOM   934  O  O   . ASP A 1 140 ? 6.787   120.632 11.389  1.00 34.18 ? 140  ASP A O   1 
ATOM   935  C  CB  . ASP A 1 140 ? 5.513   118.890 13.229  1.00 41.58 ? 140  ASP A CB  1 
ATOM   936  C  CG  . ASP A 1 140 ? 4.107   119.438 13.071  1.00 46.21 ? 140  ASP A CG  1 
ATOM   937  O  OD1 . ASP A 1 140 ? 3.932   120.653 13.264  1.00 48.69 ? 140  ASP A OD1 1 
ATOM   938  O  OD2 . ASP A 1 140 ? 3.194   118.636 12.768  1.00 54.78 ? 140  ASP A OD2 1 
ATOM   939  N  N   . SER A 1 141 ? 6.900   122.278 12.949  1.00 32.11 ? 141  SER A N   1 
ATOM   940  C  CA  . SER A 1 141 ? 7.388   123.355 12.042  1.00 30.31 ? 141  SER A CA  1 
ATOM   941  C  C   . SER A 1 141 ? 8.306   124.288 12.827  1.00 30.28 ? 141  SER A C   1 
ATOM   942  O  O   . SER A 1 141 ? 8.120   124.401 14.064  1.00 29.33 ? 141  SER A O   1 
ATOM   943  C  CB  . SER A 1 141 ? 6.274   124.125 11.404  1.00 29.57 ? 141  SER A CB  1 
ATOM   944  O  OG  . SER A 1 141 ? 5.643   124.982 12.345  1.00 29.03 ? 141  SER A OG  1 
ATOM   945  N  N   . VAL A 1 142 ? 9.231   124.952 12.130  1.00 28.49 ? 142  VAL A N   1 
ATOM   946  C  CA  . VAL A 1 142 ? 10.101  126.005 12.732  1.00 29.68 ? 142  VAL A CA  1 
ATOM   947  C  C   . VAL A 1 142 ? 9.174   127.065 13.341  1.00 28.63 ? 142  VAL A C   1 
ATOM   948  O  O   . VAL A 1 142 ? 9.386   127.439 14.498  1.00 28.11 ? 142  VAL A O   1 
ATOM   949  C  CB  . VAL A 1 142 ? 11.085  126.600 11.705  1.00 30.34 ? 142  VAL A CB  1 
ATOM   950  C  CG1 . VAL A 1 142 ? 11.811  127.816 12.256  1.00 30.86 ? 142  VAL A CG1 1 
ATOM   951  C  CG2 . VAL A 1 142 ? 12.084  125.567 11.209  1.00 31.40 ? 142  VAL A CG2 1 
ATOM   952  N  N   . GLU A 1 143 ? 8.148   127.493 12.596  1.00 31.01 ? 143  GLU A N   1 
ATOM   953  C  CA  . GLU A 1 143 ? 7.170   128.527 13.035  1.00 31.22 ? 143  GLU A CA  1 
ATOM   954  C  C   . GLU A 1 143 ? 6.561   128.121 14.385  1.00 29.22 ? 143  GLU A C   1 
ATOM   955  O  O   . GLU A 1 143 ? 6.483   128.988 15.286  1.00 28.67 ? 143  GLU A O   1 
ATOM   956  C  CB  . GLU A 1 143 ? 6.070   128.736 11.988  1.00 35.81 ? 143  GLU A CB  1 
ATOM   957  C  CG  . GLU A 1 143 ? 6.556   129.344 10.680  1.00 38.77 ? 143  GLU A CG  1 
ATOM   958  C  CD  . GLU A 1 143 ? 7.147   128.378 9.655   1.00 42.41 ? 143  GLU A CD  1 
ATOM   959  O  OE1 . GLU A 1 143 ? 7.456   127.219 10.012  1.00 39.98 ? 143  GLU A OE1 1 
ATOM   960  O  OE2 . GLU A 1 143 ? 7.306   128.796 8.488   1.00 47.90 ? 143  GLU A OE2 1 
ATOM   961  N  N   . SER A 1 144 ? 6.121   126.865 14.516  1.00 26.23 ? 144  SER A N   1 
ATOM   962  C  CA  . SER A 1 144 ? 5.462   126.349 15.749  1.00 26.58 ? 144  SER A CA  1 
ATOM   963  C  C   . SER A 1 144 ? 6.456   126.339 16.922  1.00 24.78 ? 144  SER A C   1 
ATOM   964  O  O   . SER A 1 144 ? 6.071   126.744 18.020  1.00 25.68 ? 144  SER A O   1 
ATOM   965  C  CB  . SER A 1 144 ? 4.838   124.989 15.531  1.00 26.86 ? 144  SER A CB  1 
ATOM   966  O  OG  . SER A 1 144 ? 4.070   124.611 16.665  1.00 27.91 ? 144  SER A OG  1 
ATOM   967  N  N   . LEU A 1 145 ? 7.695   125.917 16.684  1.00 24.00 ? 145  LEU A N   1 
ATOM   968  C  CA  . LEU A 1 145 ? 8.760   125.835 17.717  1.00 24.41 ? 145  LEU A CA  1 
ATOM   969  C  C   . LEU A 1 145 ? 9.063   127.233 18.270  1.00 24.65 ? 145  LEU A C   1 
ATOM   970  O  O   . LEU A 1 145 ? 9.042   127.409 19.502  1.00 24.14 ? 145  LEU A O   1 
ATOM   971  C  CB  . LEU A 1 145 ? 10.009  125.209 17.088  1.00 24.03 ? 145  LEU A CB  1 
ATOM   972  C  CG  . LEU A 1 145 ? 11.245  125.149 17.983  1.00 23.08 ? 145  LEU A CG  1 
ATOM   973  C  CD1 . LEU A 1 145 ? 10.939  124.468 19.303  1.00 22.97 ? 145  LEU A CD1 1 
ATOM   974  C  CD2 . LEU A 1 145 ? 12.375  124.441 17.267  1.00 24.48 ? 145  LEU A CD2 1 
ATOM   975  N  N   . ILE A 1 146 ? 9.323   128.195 17.389  1.00 26.42 ? 146  ILE A N   1 
ATOM   976  C  CA  A ILE A 1 146 ? 9.764   129.557 17.820  0.50 27.76 ? 146  ILE A CA  1 
ATOM   977  C  CA  B ILE A 1 146 ? 9.743   129.582 17.752  0.50 28.09 ? 146  ILE A CA  1 
ATOM   978  C  C   . ILE A 1 146 ? 8.589   130.272 18.497  1.00 28.67 ? 146  ILE A C   1 
ATOM   979  O  O   . ILE A 1 146 ? 8.840   130.906 19.538  1.00 27.07 ? 146  ILE A O   1 
ATOM   980  C  CB  A ILE A 1 146 ? 10.398  130.376 16.678  0.50 28.71 ? 146  ILE A CB  1 
ATOM   981  C  CB  B ILE A 1 146 ? 10.221  130.315 16.477  0.50 29.53 ? 146  ILE A CB  1 
ATOM   982  C  CG1 A ILE A 1 146 ? 9.397   130.801 15.601  0.50 28.65 ? 146  ILE A CG1 1 
ATOM   983  C  CG1 B ILE A 1 146 ? 11.736  130.166 16.304  0.50 30.26 ? 146  ILE A CG1 1 
ATOM   984  C  CG2 A ILE A 1 146 ? 11.591  129.629 16.093  0.50 28.40 ? 146  ILE A CG2 1 
ATOM   985  C  CG2 B ILE A 1 146 ? 9.809   131.774 16.429  0.50 29.21 ? 146  ILE A CG2 1 
ATOM   986  C  CD1 A ILE A 1 146 ? 9.933   131.868 14.677  0.50 28.70 ? 146  ILE A CD1 1 
ATOM   987  C  CD1 B ILE A 1 146 ? 12.132  129.281 15.156  0.50 31.00 ? 146  ILE A CD1 1 
ATOM   988  N  N   . SER A 1 147 ? 7.367   130.117 17.974  1.00 28.99 ? 147  SER A N   1 
ATOM   989  C  CA  . SER A 1 147 ? 6.119   130.686 18.556  1.00 30.60 ? 147  SER A CA  1 
ATOM   990  C  C   . SER A 1 147 ? 5.943   130.210 20.004  1.00 29.90 ? 147  SER A C   1 
ATOM   991  O  O   . SER A 1 147 ? 5.815   131.059 20.906  1.00 31.66 ? 147  SER A O   1 
ATOM   992  C  CB  . SER A 1 147 ? 4.921   130.331 17.693  1.00 32.22 ? 147  SER A CB  1 
ATOM   993  O  OG  . SER A 1 147 ? 3.707   130.647 18.345  1.00 36.57 ? 147  SER A OG  1 
ATOM   994  N  N   . ARG A 1 148 ? 5.954   128.898 20.232  1.00 28.52 ? 148  ARG A N   1 
ATOM   995  C  CA  . ARG A 1 148 ? 5.651   128.321 21.572  1.00 28.33 ? 148  ARG A CA  1 
ATOM   996  C  C   . ARG A 1 148 ? 6.821   128.533 22.535  1.00 27.23 ? 148  ARG A C   1 
ATOM   997  O  O   . ARG A 1 148 ? 6.574   128.485 23.761  1.00 28.18 ? 148  ARG A O   1 
ATOM   998  C  CB  . ARG A 1 148 ? 5.307   126.832 21.486  1.00 30.60 ? 148  ARG A CB  1 
ATOM   999  C  CG  . ARG A 1 148 ? 6.437   125.934 21.019  1.00 33.01 ? 148  ARG A CG  1 
ATOM   1000 C  CD  . ARG A 1 148 ? 5.992   124.482 21.009  1.00 35.11 ? 148  ARG A CD  1 
ATOM   1001 N  NE  . ARG A 1 148 ? 5.133   124.104 19.897  1.00 35.18 ? 148  ARG A NE  1 
ATOM   1002 C  CZ  . ARG A 1 148 ? 4.368   123.012 19.867  1.00 36.36 ? 148  ARG A CZ  1 
ATOM   1003 N  NH1 . ARG A 1 148 ? 4.306   122.186 20.903  1.00 36.97 ? 148  ARG A NH1 1 
ATOM   1004 N  NH2 . ARG A 1 148 ? 3.639   122.761 18.799  1.00 39.05 ? 148  ARG A NH2 1 
ATOM   1005 N  N   . THR A 1 149 ? 8.039   128.753 22.028  1.00 24.49 ? 149  THR A N   1 
ATOM   1006 C  CA  . THR A 1 149 ? 9.247   128.805 22.894  1.00 24.13 ? 149  THR A CA  1 
ATOM   1007 C  C   . THR A 1 149 ? 9.210   130.078 23.747  1.00 23.46 ? 149  THR A C   1 
ATOM   1008 O  O   . THR A 1 149 ? 9.497   129.980 24.958  1.00 22.77 ? 149  THR A O   1 
ATOM   1009 C  CB  . THR A 1 149 ? 10.536  128.625 22.086  1.00 23.88 ? 149  THR A CB  1 
ATOM   1010 O  OG1 . THR A 1 149 ? 10.540  127.277 21.613  1.00 24.98 ? 149  THR A OG1 1 
ATOM   1011 C  CG2 . THR A 1 149 ? 11.783  128.881 22.903  1.00 23.56 ? 149  THR A CG2 1 
ATOM   1012 N  N   . THR A 1 150 ? 8.882   131.232 23.160  1.00 24.67 ? 150  THR A N   1 
ATOM   1013 C  CA  . THR A 1 150 ? 8.869   132.515 23.916  1.00 24.27 ? 150  THR A CA  1 
ATOM   1014 C  C   . THR A 1 150 ? 7.817   132.414 25.028  1.00 24.19 ? 150  THR A C   1 
ATOM   1015 O  O   . THR A 1 150 ? 8.113   132.811 26.161  1.00 23.83 ? 150  THR A O   1 
ATOM   1016 C  CB  . THR A 1 150 ? 8.700   133.723 22.993  1.00 23.66 ? 150  THR A CB  1 
ATOM   1017 O  OG1 . THR A 1 150 ? 7.547   133.570 22.168  1.00 24.22 ? 150  THR A OG1 1 
ATOM   1018 C  CG2 . THR A 1 150 ? 9.924   133.935 22.132  1.00 23.93 ? 150  THR A CG2 1 
ATOM   1019 N  N   . ARG A 1 151 ? 6.647   131.874 24.696  1.00 25.40 ? 151  ARG A N   1 
ATOM   1020 C  CA  . ARG A 1 151 ? 5.512   131.674 25.633  1.00 26.74 ? 151  ARG A CA  1 
ATOM   1021 C  C   . ARG A 1 151 ? 5.976   130.780 26.794  1.00 26.22 ? 151  ARG A C   1 
ATOM   1022 O  O   . ARG A 1 151 ? 5.791   131.158 27.962  1.00 27.05 ? 151  ARG A O   1 
ATOM   1023 C  CB  . ARG A 1 151 ? 4.351   131.083 24.827  1.00 28.93 ? 151  ARG A CB  1 
ATOM   1024 C  CG  . ARG A 1 151 ? 3.007   131.056 25.537  1.00 31.98 ? 151  ARG A CG  1 
ATOM   1025 C  CD  . ARG A 1 151 ? 1.941   130.412 24.656  1.00 33.28 ? 151  ARG A CD  1 
ATOM   1026 N  NE  . ARG A 1 151 ? 1.963   130.974 23.313  1.00 32.57 ? 151  ARG A NE  1 
ATOM   1027 C  CZ  . ARG A 1 151 ? 2.054   130.285 22.177  1.00 33.96 ? 151  ARG A CZ  1 
ATOM   1028 N  NH1 . ARG A 1 151 ? 2.087   130.945 21.030  1.00 35.02 ? 151  ARG A NH1 1 
ATOM   1029 N  NH2 . ARG A 1 151 ? 2.088   128.956 22.172  1.00 33.40 ? 151  ARG A NH2 1 
ATOM   1030 N  N   . LEU A 1 152 ? 6.608   129.655 26.469  1.00 27.66 ? 152  LEU A N   1 
ATOM   1031 C  CA  . LEU A 1 152 ? 7.035   128.624 27.449  1.00 28.28 ? 152  LEU A CA  1 
ATOM   1032 C  C   . LEU A 1 152 ? 8.157   129.170 28.343  1.00 26.94 ? 152  LEU A C   1 
ATOM   1033 O  O   . LEU A 1 152 ? 8.107   128.940 29.576  1.00 24.89 ? 152  LEU A O   1 
ATOM   1034 C  CB  . LEU A 1 152 ? 7.509   127.383 26.688  1.00 29.20 ? 152  LEU A CB  1 
ATOM   1035 C  CG  . LEU A 1 152 ? 8.149   126.307 27.559  1.00 30.47 ? 152  LEU A CG  1 
ATOM   1036 C  CD1 . LEU A 1 152 ? 7.089   125.610 28.392  1.00 31.92 ? 152  LEU A CD1 1 
ATOM   1037 C  CD2 . LEU A 1 152 ? 8.919   125.305 26.718  1.00 31.84 ? 152  LEU A CD2 1 
ATOM   1038 N  N   . VAL A 1 153 ? 9.162   129.816 27.752  1.00 24.90 ? 153  VAL A N   1 
ATOM   1039 C  CA  . VAL A 1 153 ? 10.334  130.325 28.525  1.00 26.20 ? 153  VAL A CA  1 
ATOM   1040 C  C   . VAL A 1 153 ? 9.849   131.431 29.464  1.00 25.87 ? 153  VAL A C   1 
ATOM   1041 O  O   . VAL A 1 153 ? 10.244  131.482 30.627  1.00 28.26 ? 153  VAL A O   1 
ATOM   1042 C  CB  . VAL A 1 153 ? 11.487  130.771 27.606  1.00 25.61 ? 153  VAL A CB  1 
ATOM   1043 C  CG1 . VAL A 1 153 ? 12.540  131.566 28.364  1.00 26.50 ? 153  VAL A CG1 1 
ATOM   1044 C  CG2 . VAL A 1 153 ? 12.125  129.576 26.897  1.00 24.79 ? 153  VAL A CG2 1 
HETATM 1045 N  N   . MLZ A 1 154 ? 8.956   132.290 28.974  1.00 26.68 ? 154  MLZ A N   1 
HETATM 1046 C  CA  . MLZ A 1 154 ? 8.435   133.381 29.788  1.00 28.63 ? 154  MLZ A CA  1 
HETATM 1047 C  CB  . MLZ A 1 154 ? 7.473   134.253 28.979  1.00 30.08 ? 154  MLZ A CB  1 
HETATM 1048 C  CG  . MLZ A 1 154 ? 6.924   135.445 29.739  1.00 30.88 ? 154  MLZ A CG  1 
HETATM 1049 C  CD  . MLZ A 1 154 ? 5.942   136.261 28.959  1.00 32.96 ? 154  MLZ A CD  1 
HETATM 1050 C  CE  . MLZ A 1 154 ? 5.236   137.258 29.863  1.00 36.04 ? 154  MLZ A CE  1 
HETATM 1051 N  NZ  . MLZ A 1 154 ? 3.985   136.743 30.428  1.00 36.68 ? 154  MLZ A NZ  1 
HETATM 1052 C  CM  . MLZ A 1 154 ? 3.466   137.519 31.563  1.00 39.82 ? 154  MLZ A CM  1 
HETATM 1053 C  C   . MLZ A 1 154 ? 7.733   132.851 31.038  1.00 27.79 ? 154  MLZ A C   1 
HETATM 1054 O  O   . MLZ A 1 154 ? 8.016   133.312 32.142  1.00 29.10 ? 154  MLZ A O   1 
ATOM   1055 N  N   . ALA A 1 155 ? 6.832   131.877 30.872  1.00 27.22 ? 155  ALA A N   1 
ATOM   1056 C  CA  . ALA A 1 155 ? 6.070   131.353 31.998  1.00 28.14 ? 155  ALA A CA  1 
ATOM   1057 C  C   . ALA A 1 155 ? 6.974   130.522 32.916  1.00 28.88 ? 155  ALA A C   1 
ATOM   1058 O  O   . ALA A 1 155 ? 6.717   130.494 34.124  1.00 30.53 ? 155  ALA A O   1 
ATOM   1059 C  CB  . ALA A 1 155 ? 4.889   130.541 31.525  1.00 27.42 ? 155  ALA A CB  1 
ATOM   1060 N  N   . THR A 1 156 ? 7.992   129.852 32.378  1.00 29.51 ? 156  THR A N   1 
ATOM   1061 C  CA  . THR A 1 156 ? 8.838   128.938 33.187  1.00 29.54 ? 156  THR A CA  1 
ATOM   1062 C  C   . THR A 1 156 ? 9.886   129.762 33.949  1.00 30.32 ? 156  THR A C   1 
ATOM   1063 O  O   . THR A 1 156 ? 10.050  129.515 35.161  1.00 28.36 ? 156  THR A O   1 
ATOM   1064 C  CB  . THR A 1 156 ? 9.424   127.814 32.325  1.00 30.95 ? 156  THR A CB  1 
ATOM   1065 O  OG1 . THR A 1 156 ? 8.357   127.168 31.627  1.00 32.24 ? 156  THR A OG1 1 
ATOM   1066 C  CG2 . THR A 1 156 ? 10.161  126.778 33.142  1.00 31.16 ? 156  THR A CG2 1 
ATOM   1067 N  N   . LEU A 1 157 ? 10.564  130.708 33.289  1.00 29.14 ? 157  LEU A N   1 
ATOM   1068 C  CA  . LEU A 1 157 ? 11.725  131.433 33.886  1.00 28.43 ? 157  LEU A CA  1 
ATOM   1069 C  C   . LEU A 1 157 ? 11.283  132.766 34.502  1.00 27.66 ? 157  LEU A C   1 
ATOM   1070 O  O   . LEU A 1 157 ? 12.089  133.368 35.231  1.00 29.16 ? 157  LEU A O   1 
ATOM   1071 C  CB  . LEU A 1 157 ? 12.804  131.639 32.820  1.00 27.87 ? 157  LEU A CB  1 
ATOM   1072 C  CG  . LEU A 1 157 ? 13.314  130.369 32.145  1.00 28.55 ? 157  LEU A CG  1 
ATOM   1073 C  CD1 . LEU A 1 157 ? 14.568  130.663 31.339  1.00 29.32 ? 157  LEU A CD1 1 
ATOM   1074 C  CD2 . LEU A 1 157 ? 13.585  129.270 33.162  1.00 29.36 ? 157  LEU A CD2 1 
ATOM   1075 N  N   . GLY A 1 158 ? 10.055  133.203 34.236  1.00 27.03 ? 158  GLY A N   1 
ATOM   1076 C  CA  . GLY A 1 158 ? 9.428   134.336 34.941  1.00 27.65 ? 158  GLY A CA  1 
ATOM   1077 C  C   . GLY A 1 158 ? 10.032  135.681 34.561  1.00 28.01 ? 158  GLY A C   1 
ATOM   1078 O  O   . GLY A 1 158 ? 10.125  136.543 35.448  1.00 28.42 ? 158  GLY A O   1 
ATOM   1079 N  N   . TYR A 1 159 ? 10.400  135.875 33.289  1.00 25.27 ? 159  TYR A N   1 
ATOM   1080 C  CA  . TYR A 1 159 ? 10.851  137.185 32.753  1.00 24.69 ? 159  TYR A CA  1 
ATOM   1081 C  C   . TYR A 1 159 ? 9.659   137.934 32.142  1.00 24.25 ? 159  TYR A C   1 
ATOM   1082 O  O   . TYR A 1 159 ? 8.733   137.292 31.607  1.00 24.18 ? 159  TYR A O   1 
ATOM   1083 C  CB  . TYR A 1 159 ? 12.012  137.003 31.771  1.00 23.95 ? 159  TYR A CB  1 
ATOM   1084 C  CG  . TYR A 1 159 ? 13.340  136.738 32.435  1.00 23.44 ? 159  TYR A CG  1 
ATOM   1085 C  CD1 . TYR A 1 159 ? 13.620  135.495 32.982  1.00 24.61 ? 159  TYR A CD1 1 
ATOM   1086 C  CD2 . TYR A 1 159 ? 14.320  137.714 32.512  1.00 23.35 ? 159  TYR A CD2 1 
ATOM   1087 C  CE1 . TYR A 1 159 ? 14.830  135.231 33.600  1.00 24.35 ? 159  TYR A CE1 1 
ATOM   1088 C  CE2 . TYR A 1 159 ? 15.545  137.461 33.116  1.00 24.65 ? 159  TYR A CE2 1 
ATOM   1089 C  CZ  . TYR A 1 159 ? 15.802  136.213 33.662  1.00 24.81 ? 159  TYR A CZ  1 
ATOM   1090 O  OH  . TYR A 1 159 ? 16.994  135.932 34.272  1.00 24.54 ? 159  TYR A OH  1 
ATOM   1091 N  N   . ASP A 1 160 ? 9.703   139.267 32.210  1.00 24.48 ? 160  ASP A N   1 
ATOM   1092 C  CA  . ASP A 1 160 ? 8.633   140.183 31.735  1.00 24.58 ? 160  ASP A CA  1 
ATOM   1093 C  C   . ASP A 1 160 ? 8.499   140.062 30.216  1.00 23.92 ? 160  ASP A C   1 
ATOM   1094 O  O   . ASP A 1 160 ? 7.376   140.219 29.705  1.00 23.90 ? 160  ASP A O   1 
ATOM   1095 C  CB  . ASP A 1 160 ? 8.934   141.630 32.115  1.00 25.82 ? 160  ASP A CB  1 
ATOM   1096 C  CG  . ASP A 1 160 ? 8.814   141.915 33.602  1.00 27.43 ? 160  ASP A CG  1 
ATOM   1097 O  OD1 . ASP A 1 160 ? 7.942   141.295 34.247  1.00 27.17 ? 160  ASP A OD1 1 
ATOM   1098 O  OD2 . ASP A 1 160 ? 9.567   142.786 34.093  1.00 26.91 ? 160  ASP A OD2 1 
ATOM   1099 N  N   . ARG A 1 161 ? 9.608   139.814 29.521  1.00 22.48 ? 161  ARG A N   1 
ATOM   1100 C  CA  . ARG A 1 161 ? 9.592   139.631 28.050  1.00 23.02 ? 161  ARG A CA  1 
ATOM   1101 C  C   . ARG A 1 161 ? 10.575  138.531 27.659  1.00 22.88 ? 161  ARG A C   1 
ATOM   1102 O  O   . ARG A 1 161 ? 11.676  138.461 28.223  1.00 22.73 ? 161  ARG A O   1 
ATOM   1103 C  CB  . ARG A 1 161 ? 9.939   140.925 27.318  1.00 23.15 ? 161  ARG A CB  1 
ATOM   1104 C  CG  . ARG A 1 161 ? 9.687   140.869 25.819  1.00 23.41 ? 161  ARG A CG  1 
ATOM   1105 C  CD  . ARG A 1 161 ? 10.488  141.925 25.086  1.00 24.56 ? 161  ARG A CD  1 
ATOM   1106 N  NE  . ARG A 1 161 ? 10.214  143.265 25.579  1.00 25.13 ? 161  ARG A NE  1 
ATOM   1107 C  CZ  . ARG A 1 161 ? 9.187   144.022 25.209  1.00 27.14 ? 161  ARG A CZ  1 
ATOM   1108 N  NH1 . ARG A 1 161 ? 8.297   143.574 24.336  1.00 28.00 ? 161  ARG A NH1 1 
ATOM   1109 N  NH2 . ARG A 1 161 ? 9.059   145.236 25.709  1.00 26.89 ? 161  ARG A NH2 1 
ATOM   1110 N  N   . VAL A 1 162 ? 10.172  137.701 26.710  1.00 22.61 ? 162  VAL A N   1 
ATOM   1111 C  CA  . VAL A 1 162 ? 11.079  136.712 26.076  1.00 22.71 ? 162  VAL A CA  1 
ATOM   1112 C  C   . VAL A 1 162 ? 10.923  136.898 24.575  1.00 22.91 ? 162  VAL A C   1 
ATOM   1113 O  O   . VAL A 1 162 ? 9.772   136.847 24.101  1.00 22.34 ? 162  VAL A O   1 
ATOM   1114 C  CB  . VAL A 1 162 ? 10.773  135.270 26.517  1.00 22.35 ? 162  VAL A CB  1 
ATOM   1115 C  CG1 . VAL A 1 162 ? 11.688  134.280 25.809  1.00 23.56 ? 162  VAL A CG1 1 
ATOM   1116 C  CG2 . VAL A 1 162 ? 10.870  135.117 28.022  1.00 21.88 ? 162  VAL A CG2 1 
ATOM   1117 N  N   . MET A 1 163 ? 12.045  137.104 23.885  1.00 22.92 ? 163  MET A N   1 
ATOM   1118 C  CA  . MET A 1 163 ? 12.107  137.263 22.416  1.00 22.04 ? 163  MET A CA  1 
ATOM   1119 C  C   . MET A 1 163 ? 13.020  136.178 21.842  1.00 21.35 ? 163  MET A C   1 
ATOM   1120 O  O   . MET A 1 163 ? 13.889  135.641 22.569  1.00 20.72 ? 163  MET A O   1 
ATOM   1121 C  CB  . MET A 1 163 ? 12.640  138.646 22.026  1.00 22.73 ? 163  MET A CB  1 
ATOM   1122 C  CG  . MET A 1 163 ? 11.656  139.778 22.275  1.00 23.73 ? 163  MET A CG  1 
ATOM   1123 S  SD  . MET A 1 163 ? 12.247  141.403 21.713  1.00 24.68 ? 163  MET A SD  1 
ATOM   1124 C  CE  . MET A 1 163 ? 13.465  141.746 22.980  1.00 24.69 ? 163  MET A CE  1 
ATOM   1125 N  N   . ILE A 1 164 ? 12.803  135.854 20.573  1.00 21.42 ? 164  ILE A N   1 
ATOM   1126 C  CA  . ILE A 1 164 ? 13.805  135.143 19.735  1.00 21.81 ? 164  ILE A CA  1 
ATOM   1127 C  C   . ILE A 1 164 ? 14.194  136.069 18.588  1.00 21.57 ? 164  ILE A C   1 
ATOM   1128 O  O   . ILE A 1 164 ? 13.294  136.600 17.908  1.00 22.03 ? 164  ILE A O   1 
ATOM   1129 C  CB  . ILE A 1 164 ? 13.286  133.776 19.260  1.00 21.80 ? 164  ILE A CB  1 
ATOM   1130 C  CG1 . ILE A 1 164 ? 13.049  132.854 20.459  1.00 21.44 ? 164  ILE A CG1 1 
ATOM   1131 C  CG2 . ILE A 1 164 ? 14.242  133.153 18.243  1.00 22.50 ? 164  ILE A CG2 1 
ATOM   1132 C  CD1 . ILE A 1 164 ? 12.363  131.545 20.114  1.00 22.31 ? 164  ILE A CD1 1 
ATOM   1133 N  N   . TYR A 1 165 ? 15.498  136.261 18.417  1.00 21.61 ? 165  TYR A N   1 
ATOM   1134 C  CA  . TYR A 1 165 ? 16.098  136.932 17.241  1.00 22.37 ? 165  TYR A CA  1 
ATOM   1135 C  C   . TYR A 1 165 ? 16.648  135.849 16.322  1.00 22.77 ? 165  TYR A C   1 
ATOM   1136 O  O   . TYR A 1 165 ? 17.324  134.936 16.821  1.00 22.01 ? 165  TYR A O   1 
ATOM   1137 C  CB  . TYR A 1 165 ? 17.243  137.876 17.616  1.00 21.91 ? 165  TYR A CB  1 
ATOM   1138 C  CG  . TYR A 1 165 ? 17.055  138.682 18.873  1.00 21.81 ? 165  TYR A CG  1 
ATOM   1139 C  CD1 . TYR A 1 165 ? 15.868  139.344 19.145  1.00 22.23 ? 165  TYR A CD1 1 
ATOM   1140 C  CD2 . TYR A 1 165 ? 18.103  138.836 19.765  1.00 22.25 ? 165  TYR A CD2 1 
ATOM   1141 C  CE1 . TYR A 1 165 ? 15.714  140.100 20.296  1.00 21.43 ? 165  TYR A CE1 1 
ATOM   1142 C  CE2 . TYR A 1 165 ? 17.969  139.587 20.918  1.00 20.64 ? 165  TYR A CE2 1 
ATOM   1143 C  CZ  . TYR A 1 165 ? 16.768  140.212 21.189  1.00 21.10 ? 165  TYR A CZ  1 
ATOM   1144 O  OH  . TYR A 1 165 ? 16.631  140.958 22.320  1.00 20.43 ? 165  TYR A OH  1 
ATOM   1145 N  N   . ARG A 1 166 ? 16.384  135.977 15.026  1.00 23.88 ? 166  ARG A N   1 
ATOM   1146 C  CA  . ARG A 1 166 ? 17.126  135.236 13.975  1.00 24.84 ? 166  ARG A CA  1 
ATOM   1147 C  C   . ARG A 1 166 ? 18.091  136.212 13.297  1.00 23.40 ? 166  ARG A C   1 
ATOM   1148 O  O   . ARG A 1 166 ? 17.623  137.251 12.805  1.00 23.47 ? 166  ARG A O   1 
ATOM   1149 C  CB  . ARG A 1 166 ? 16.136  134.633 12.978  1.00 27.65 ? 166  ARG A CB  1 
ATOM   1150 C  CG  . ARG A 1 166 ? 16.779  133.787 11.892  1.00 31.18 ? 166  ARG A CG  1 
ATOM   1151 C  CD  . ARG A 1 166 ? 15.729  133.184 10.984  1.00 35.36 ? 166  ARG A CD  1 
ATOM   1152 N  NE  . ARG A 1 166 ? 16.384  132.338 10.000  1.00 40.69 ? 166  ARG A NE  1 
ATOM   1153 C  CZ  . ARG A 1 166 ? 16.989  132.782 8.903   1.00 45.24 ? 166  ARG A CZ  1 
ATOM   1154 N  NH1 . ARG A 1 166 ? 17.002  134.077 8.624   1.00 44.58 ? 166  ARG A NH1 1 
ATOM   1155 N  NH2 . ARG A 1 166 ? 17.577  131.925 8.085   1.00 46.97 ? 166  ARG A NH2 1 
ATOM   1156 N  N   . PHE A 1 167 ? 19.388  135.901 13.275  1.00 23.52 ? 167  PHE A N   1 
ATOM   1157 C  CA  . PHE A 1 167 ? 20.404  136.736 12.590  1.00 24.42 ? 167  PHE A CA  1 
ATOM   1158 C  C   . PHE A 1 167 ? 20.250  136.542 11.087  1.00 24.80 ? 167  PHE A C   1 
ATOM   1159 O  O   . PHE A 1 167 ? 20.001  135.390 10.658  1.00 24.12 ? 167  PHE A O   1 
ATOM   1160 C  CB  . PHE A 1 167 ? 21.818  136.433 13.086  1.00 25.08 ? 167  PHE A CB  1 
ATOM   1161 C  CG  . PHE A 1 167 ? 22.037  136.917 14.494  1.00 23.76 ? 167  PHE A CG  1 
ATOM   1162 C  CD1 . PHE A 1 167 ? 21.852  138.250 14.811  1.00 24.02 ? 167  PHE A CD1 1 
ATOM   1163 C  CD2 . PHE A 1 167 ? 22.379  136.037 15.506  1.00 23.99 ? 167  PHE A CD2 1 
ATOM   1164 C  CE1 . PHE A 1 167 ? 22.029  138.702 16.110  1.00 24.00 ? 167  PHE A CE1 1 
ATOM   1165 C  CE2 . PHE A 1 167 ? 22.558  136.488 16.804  1.00 24.94 ? 167  PHE A CE2 1 
ATOM   1166 C  CZ  . PHE A 1 167 ? 22.380  137.819 17.101  1.00 25.91 ? 167  PHE A CZ  1 
ATOM   1167 N  N   . GLN A 1 168 ? 20.328  137.657 10.352  1.00 25.47 ? 168  GLN A N   1 
ATOM   1168 C  CA  . GLN A 1 168 ? 20.224  137.729 8.873   1.00 26.59 ? 168  GLN A CA  1 
ATOM   1169 C  C   . GLN A 1 168 ? 21.623  137.524 8.286   1.00 26.34 ? 168  GLN A C   1 
ATOM   1170 O  O   . GLN A 1 168 ? 22.587  137.540 9.062   1.00 26.03 ? 168  GLN A O   1 
ATOM   1171 C  CB  . GLN A 1 168 ? 19.639  139.077 8.445   1.00 27.54 ? 168  GLN A CB  1 
ATOM   1172 C  CG  . GLN A 1 168 ? 18.358  139.447 9.180   1.00 28.80 ? 168  GLN A CG  1 
ATOM   1173 C  CD  . GLN A 1 168 ? 17.240  138.480 8.870   1.00 29.56 ? 168  GLN A CD  1 
ATOM   1174 O  OE1 . GLN A 1 168 ? 16.781  138.404 7.737   1.00 28.99 ? 168  GLN A OE1 1 
ATOM   1175 N  NE2 . GLN A 1 168 ? 16.795  137.732 9.872   1.00 28.64 ? 168  GLN A NE2 1 
ATOM   1176 N  N   . GLU A 1 169 ? 21.728  137.350 6.967   1.00 27.35 ? 169  GLU A N   1 
ATOM   1177 C  CA  . GLU A 1 169 ? 23.030  137.162 6.271   1.00 31.76 ? 169  GLU A CA  1 
ATOM   1178 C  C   . GLU A 1 169 ? 23.965  138.332 6.611   1.00 29.73 ? 169  GLU A C   1 
ATOM   1179 O  O   . GLU A 1 169 ? 25.139  138.062 6.810   1.00 29.75 ? 169  GLU A O   1 
ATOM   1180 C  CB  . GLU A 1 169 ? 22.843  137.009 4.759   1.00 35.06 ? 169  GLU A CB  1 
ATOM   1181 C  CG  . GLU A 1 169 ? 22.037  135.773 4.382   1.00 42.12 ? 169  GLU A CG  1 
ATOM   1182 C  CD  . GLU A 1 169 ? 22.188  135.308 2.939   1.00 47.58 ? 169  GLU A CD  1 
ATOM   1183 O  OE1 . GLU A 1 169 ? 23.170  135.732 2.277   1.00 47.27 ? 169  GLU A OE1 1 
ATOM   1184 O  OE2 . GLU A 1 169 ? 21.326  134.515 2.480   1.00 50.10 ? 169  GLU A OE2 1 
ATOM   1185 N  N   . ASP A 1 170 ? 23.448  139.563 6.731   1.00 29.62 ? 170  ASP A N   1 
ATOM   1186 C  CA  . ASP A 1 170 ? 24.261  140.785 6.997   1.00 29.20 ? 170  ASP A CA  1 
ATOM   1187 C  C   . ASP A 1 170 ? 24.531  140.966 8.502   1.00 28.50 ? 170  ASP A C   1 
ATOM   1188 O  O   . ASP A 1 170 ? 25.157  141.974 8.868   1.00 27.94 ? 170  ASP A O   1 
ATOM   1189 C  CB  . ASP A 1 170 ? 23.609  142.031 6.387   1.00 29.98 ? 170  ASP A CB  1 
ATOM   1190 C  CG  . ASP A 1 170 ? 22.295  142.452 7.023   1.00 31.00 ? 170  ASP A CG  1 
ATOM   1191 O  OD1 . ASP A 1 170 ? 21.879  141.822 8.019   1.00 29.28 ? 170  ASP A OD1 1 
ATOM   1192 O  OD2 . ASP A 1 170 ? 21.700  143.411 6.519   1.00 33.75 ? 170  ASP A OD2 1 
ATOM   1193 N  N   . GLY A 1 171 ? 24.070  140.049 9.356   1.00 27.11 ? 171  GLY A N   1 
ATOM   1194 C  CA  . GLY A 1 171 ? 24.328  140.108 10.808  1.00 26.09 ? 171  GLY A CA  1 
ATOM   1195 C  C   . GLY A 1 171 ? 23.265  140.879 11.579  1.00 25.70 ? 171  GLY A C   1 
ATOM   1196 O  O   . GLY A 1 171 ? 23.350  140.879 12.809  1.00 25.26 ? 171  GLY A O   1 
ATOM   1197 N  N   . ALA A 1 172 ? 22.292  141.510 10.907  1.00 24.24 ? 172  ALA A N   1 
ATOM   1198 C  CA  . ALA A 1 172 ? 21.122  142.134 11.575  1.00 24.14 ? 172  ALA A CA  1 
ATOM   1199 C  C   . ALA A 1 172 ? 20.350  141.051 12.338  1.00 22.94 ? 172  ALA A C   1 
ATOM   1200 O  O   . ALA A 1 172 ? 20.426  139.875 11.955  1.00 20.29 ? 172  ALA A O   1 
ATOM   1201 C  CB  . ALA A 1 172 ? 20.215  142.830 10.584  1.00 22.89 ? 172  ALA A CB  1 
ATOM   1202 N  N   . GLY A 1 173 ? 19.616  141.452 13.370  1.00 21.99 ? 173  GLY A N   1 
ATOM   1203 C  CA  . GLY A 1 173 ? 18.694  140.561 14.093  1.00 23.43 ? 173  GLY A CA  1 
ATOM   1204 C  C   . GLY A 1 173 ? 17.248  140.951 13.796  1.00 24.08 ? 173  GLY A C   1 
ATOM   1205 O  O   . GLY A 1 173 ? 16.928  142.145 13.759  1.00 22.04 ? 173  GLY A O   1 
HETATM 1206 N  N   . MLZ A 1 174 ? 16.420  139.925 13.543  1.00 22.49 ? 174  MLZ A N   1 
HETATM 1207 C  CA  . MLZ A 1 174 ? 14.988  140.075 13.405  1.00 23.27 ? 174  MLZ A CA  1 
HETATM 1208 C  CB  . MLZ A 1 174 ? 14.497  139.416 12.113  1.00 24.01 ? 174  MLZ A CB  1 
HETATM 1209 C  CG  . MLZ A 1 174 ? 13.032  139.661 11.791  1.00 26.76 ? 174  MLZ A CG  1 
HETATM 1210 C  CD  . MLZ A 1 174 ? 12.511  138.849 10.632  1.00 29.02 ? 174  MLZ A CD  1 
HETATM 1211 C  CE  . MLZ A 1 174 ? 11.025  139.078 10.406  1.00 31.75 ? 174  MLZ A CE  1 
HETATM 1212 N  NZ  . MLZ A 1 174 ? 10.486  138.036 9.530   1.00 33.01 ? 174  MLZ A NZ  1 
HETATM 1213 C  CM  . MLZ A 1 174 ? 11.039  137.990 8.171   1.00 36.58 ? 174  MLZ A CM  1 
HETATM 1214 C  C   . MLZ A 1 174 ? 14.315  139.436 14.620  1.00 22.44 ? 174  MLZ A C   1 
HETATM 1215 O  O   . MLZ A 1 174 ? 14.629  138.308 14.992  1.00 22.17 ? 174  MLZ A O   1 
ATOM   1216 N  N   . VAL A 1 175 ? 13.366  140.156 15.218  1.00 21.68 ? 175  VAL A N   1 
ATOM   1217 C  CA  . VAL A 1 175 ? 12.558  139.599 16.288  1.00 21.97 ? 175  VAL A CA  1 
ATOM   1218 C  C   . VAL A 1 175 ? 11.484  138.708 15.650  1.00 22.58 ? 175  VAL A C   1 
ATOM   1219 O  O   . VAL A 1 175 ? 10.530  139.256 15.051  1.00 20.69 ? 175  VAL A O   1 
ATOM   1220 C  CB  . VAL A 1 175 ? 11.931  140.696 17.167  1.00 22.09 ? 175  VAL A CB  1 
ATOM   1221 C  CG1 . VAL A 1 175 ? 11.171  140.089 18.336  1.00 21.91 ? 175  VAL A CG1 1 
ATOM   1222 C  CG2 . VAL A 1 175 ? 12.966  141.704 17.658  1.00 22.36 ? 175  VAL A CG2 1 
ATOM   1223 N  N   . VAL A 1 176 ? 11.622  137.386 15.780  1.00 22.86 ? 176  VAL A N   1 
ATOM   1224 C  CA  . VAL A 1 176 ? 10.738  136.407 15.079  1.00 23.29 ? 176  VAL A CA  1 
ATOM   1225 C  C   . VAL A 1 176 ? 9.731   135.810 16.064  1.00 23.77 ? 176  VAL A C   1 
ATOM   1226 O  O   . VAL A 1 176 ? 8.758   135.193 15.609  1.00 24.12 ? 176  VAL A O   1 
ATOM   1227 C  CB  . VAL A 1 176 ? 11.554  135.331 14.342  1.00 23.55 ? 176  VAL A CB  1 
ATOM   1228 C  CG1 . VAL A 1 176 ? 12.271  135.941 13.139  1.00 23.56 ? 176  VAL A CG1 1 
ATOM   1229 C  CG2 . VAL A 1 176 ? 12.527  134.608 15.267  1.00 23.94 ? 176  VAL A CG2 1 
ATOM   1230 N  N   . SER A 1 177 ? 9.931   135.998 17.364  1.00 23.75 ? 177  SER A N   1 
ATOM   1231 C  CA  . SER A 1 177 ? 8.946   135.550 18.378  1.00 22.74 ? 177  SER A CA  1 
ATOM   1232 C  C   . SER A 1 177 ? 9.051   136.444 19.610  1.00 23.34 ? 177  SER A C   1 
ATOM   1233 O  O   . SER A 1 177 ? 10.124  137.014 19.847  1.00 22.95 ? 177  SER A O   1 
ATOM   1234 C  CB  . SER A 1 177 ? 9.139   134.087 18.688  1.00 22.67 ? 177  SER A CB  1 
ATOM   1235 O  OG  . SER A 1 177 ? 8.130   133.612 19.557  1.00 23.22 ? 177  SER A OG  1 
ATOM   1236 N  N   . GLU A 1 178 ? 7.940   136.602 20.321  1.00 23.89 ? 178  GLU A N   1 
ATOM   1237 C  CA  . GLU A 1 178 ? 7.833   137.503 21.490  1.00 24.31 ? 178  GLU A CA  1 
ATOM   1238 C  C   . GLU A 1 178 ? 6.693   137.013 22.375  1.00 24.02 ? 178  GLU A C   1 
ATOM   1239 O  O   . GLU A 1 178 ? 5.618   136.729 21.838  1.00 24.19 ? 178  GLU A O   1 
ATOM   1240 C  CB  . GLU A 1 178 ? 7.575   138.937 21.028  1.00 24.59 ? 178  GLU A CB  1 
ATOM   1241 C  CG  . GLU A 1 178 ? 7.387   139.925 22.167  1.00 24.50 ? 178  GLU A CG  1 
ATOM   1242 C  CD  . GLU A 1 178 ? 7.069   141.333 21.696  1.00 26.26 ? 178  GLU A CD  1 
ATOM   1243 O  OE1 . GLU A 1 178 ? 5.976   141.506 21.123  1.00 26.09 ? 178  GLU A OE1 1 
ATOM   1244 O  OE2 . GLU A 1 178 ? 7.924   142.250 21.880  1.00 24.36 ? 178  GLU A OE2 1 
ATOM   1245 N  N   . ALA A 1 179 ? 6.949   136.918 23.673  1.00 23.62 ? 179  ALA A N   1 
ATOM   1246 C  CA  . ALA A 1 179 ? 5.924   136.833 24.735  1.00 24.70 ? 179  ALA A CA  1 
ATOM   1247 C  C   . ALA A 1 179 ? 6.274   137.904 25.758  1.00 25.61 ? 179  ALA A C   1 
ATOM   1248 O  O   . ALA A 1 179 ? 7.442   138.075 26.087  1.00 27.06 ? 179  ALA A O   1 
ATOM   1249 C  CB  . ALA A 1 179 ? 5.894   135.452 25.337  1.00 24.39 ? 179  ALA A CB  1 
HETATM 1250 N  N   . MLZ A 1 180 ? 5.261   138.627 26.233  1.00 25.88 ? 180  MLZ A N   1 
HETATM 1251 C  CA  . MLZ A 1 180 ? 5.485   139.840 26.997  1.00 27.11 ? 180  MLZ A CA  1 
HETATM 1252 C  CB  . MLZ A 1 180 ? 5.679   141.035 26.060  1.00 26.18 ? 180  MLZ A CB  1 
HETATM 1253 C  CG  . MLZ A 1 180 ? 4.543   141.258 25.069  1.00 27.51 ? 180  MLZ A CG  1 
HETATM 1254 C  CD  . MLZ A 1 180 ? 4.429   142.679 24.574  1.00 28.10 ? 180  MLZ A CD  1 
HETATM 1255 C  CE  . MLZ A 1 180 ? 3.589   142.823 23.313  1.00 29.06 ? 180  MLZ A CE  1 
HETATM 1256 N  NZ  . MLZ A 1 180 ? 2.151   142.677 23.559  1.00 31.92 ? 180  MLZ A NZ  1 
HETATM 1257 C  CM  . MLZ A 1 180 ? 1.498   143.643 24.452  1.00 32.00 ? 180  MLZ A CM  1 
HETATM 1258 C  C   . MLZ A 1 180 ? 4.290   140.120 27.901  1.00 27.08 ? 180  MLZ A C   1 
HETATM 1259 O  O   . MLZ A 1 180 ? 3.167   139.706 27.611  1.00 26.57 ? 180  MLZ A O   1 
ATOM   1260 N  N   . GLN A 1 181 ? 4.559   140.874 28.968  1.00 27.96 ? 181  GLN A N   1 
ATOM   1261 C  CA  . GLN A 1 181 ? 3.519   141.484 29.775  1.00 29.34 ? 181  GLN A CA  1 
ATOM   1262 C  C   . GLN A 1 181 ? 2.631   142.336 28.869  1.00 29.38 ? 181  GLN A C   1 
ATOM   1263 O  O   . GLN A 1 181 ? 3.120   143.032 27.978  1.00 28.55 ? 181  GLN A O   1 
ATOM   1264 C  CB  . GLN A 1 181 ? 4.108   142.370 30.879  1.00 29.58 ? 181  GLN A CB  1 
ATOM   1265 C  CG  . GLN A 1 181 ? 5.015   141.637 31.858  1.00 30.57 ? 181  GLN A CG  1 
ATOM   1266 C  CD  . GLN A 1 181 ? 4.271   140.710 32.785  1.00 31.40 ? 181  GLN A CD  1 
ATOM   1267 O  OE1 . GLN A 1 181 ? 3.049   140.620 32.756  1.00 33.57 ? 181  GLN A OE1 1 
ATOM   1268 N  NE2 . GLN A 1 181 ? 5.013   140.001 33.618  1.00 33.70 ? 181  GLN A NE2 1 
ATOM   1269 N  N   . PRO A 1 182 ? 1.297   142.310 29.071  1.00 30.54 ? 182  PRO A N   1 
ATOM   1270 C  CA  . PRO A 1 182 ? 0.378   143.050 28.204  1.00 31.19 ? 182  PRO A CA  1 
ATOM   1271 C  C   . PRO A 1 182 ? 0.590   144.574 28.189  1.00 31.20 ? 182  PRO A C   1 
ATOM   1272 O  O   . PRO A 1 182 ? 0.158   145.200 27.250  1.00 31.03 ? 182  PRO A O   1 
ATOM   1273 C  CB  . PRO A 1 182 ? -1.033  142.715 28.732  1.00 32.23 ? 182  PRO A CB  1 
ATOM   1274 C  CG  . PRO A 1 182 ? -0.841  141.939 30.027  1.00 32.08 ? 182  PRO A CG  1 
ATOM   1275 C  CD  . PRO A 1 182 ? 0.615   141.527 30.113  1.00 31.39 ? 182  PRO A CD  1 
ATOM   1276 N  N   . GLU A 1 183 ? 1.252   145.139 29.201  1.00 32.26 ? 183  GLU A N   1 
ATOM   1277 C  CA  . GLU A 1 183 ? 1.458   146.609 29.311  1.00 35.26 ? 183  GLU A CA  1 
ATOM   1278 C  C   . GLU A 1 183 ? 2.683   147.049 28.494  1.00 33.12 ? 183  GLU A C   1 
ATOM   1279 O  O   . GLU A 1 183 ? 2.834   148.263 28.296  1.00 34.79 ? 183  GLU A O   1 
ATOM   1280 C  CB  . GLU A 1 183 ? 1.612   147.039 30.773  1.00 37.67 ? 183  GLU A CB  1 
ATOM   1281 C  CG  . GLU A 1 183 ? 0.445   146.626 31.656  1.00 41.11 ? 183  GLU A CG  1 
ATOM   1282 C  CD  . GLU A 1 183 ? 0.567   145.282 32.362  1.00 44.78 ? 183  GLU A CD  1 
ATOM   1283 O  OE1 . GLU A 1 183 ? 1.503   144.511 32.034  1.00 40.36 ? 183  GLU A OE1 1 
ATOM   1284 O  OE2 . GLU A 1 183 ? -0.286  145.002 33.245  1.00 48.55 ? 183  GLU A OE2 1 
ATOM   1285 N  N   . LEU A 1 184 ? 3.532   146.124 28.039  1.00 31.03 ? 184  LEU A N   1 
ATOM   1286 C  CA  . LEU A 1 184 ? 4.788   146.485 27.320  1.00 30.05 ? 184  LEU A CA  1 
ATOM   1287 C  C   . LEU A 1 184 ? 4.487   146.795 25.846  1.00 29.62 ? 184  LEU A C   1 
ATOM   1288 O  O   . LEU A 1 184 ? 3.481   146.283 25.308  1.00 29.27 ? 184  LEU A O   1 
ATOM   1289 C  CB  . LEU A 1 184 ? 5.803   145.346 27.450  1.00 29.52 ? 184  LEU A CB  1 
ATOM   1290 C  CG  . LEU A 1 184 ? 6.404   145.143 28.841  1.00 29.49 ? 184  LEU A CG  1 
ATOM   1291 C  CD1 . LEU A 1 184 ? 7.230   143.862 28.891  1.00 29.07 ? 184  LEU A CD1 1 
ATOM   1292 C  CD2 . LEU A 1 184 ? 7.249   146.343 29.262  1.00 29.58 ? 184  LEU A CD2 1 
ATOM   1293 N  N   . GLU A 1 185 ? 5.337   147.613 25.223  1.00 28.86 ? 185  GLU A N   1 
ATOM   1294 C  CA  . GLU A 1 185 ? 5.373   147.799 23.751  1.00 29.42 ? 185  GLU A CA  1 
ATOM   1295 C  C   . GLU A 1 185 ? 5.855   146.485 23.120  1.00 29.41 ? 185  GLU A C   1 
ATOM   1296 O  O   . GLU A 1 185 ? 6.559   145.710 23.804  1.00 28.09 ? 185  GLU A O   1 
ATOM   1297 C  CB  . GLU A 1 185 ? 6.260   148.993 23.375  1.00 30.12 ? 185  GLU A CB  1 
ATOM   1298 C  CG  . GLU A 1 185 ? 7.763   148.723 23.421  1.00 31.11 ? 185  GLU A CG  1 
ATOM   1299 C  CD  . GLU A 1 185 ? 8.425   148.797 24.790  1.00 31.43 ? 185  GLU A CD  1 
ATOM   1300 O  OE1 . GLU A 1 185 ? 7.925   148.141 25.737  1.00 31.14 ? 185  GLU A OE1 1 
ATOM   1301 O  OE2 . GLU A 1 185 ? 9.446   149.501 24.902  1.00 29.37 ? 185  GLU A OE2 1 
ATOM   1302 N  N   . SER A 1 186 ? 5.462   146.239 21.873  1.00 28.43 ? 186  SER A N   1 
ATOM   1303 C  CA  . SER A 1 186 ? 5.882   145.052 21.080  1.00 28.51 ? 186  SER A CA  1 
ATOM   1304 C  C   . SER A 1 186 ? 7.109   145.404 20.223  1.00 27.47 ? 186  SER A C   1 
ATOM   1305 O  O   . SER A 1 186 ? 7.185   146.546 19.706  1.00 27.45 ? 186  SER A O   1 
ATOM   1306 C  CB  . SER A 1 186 ? 4.754   144.530 20.235  1.00 27.36 ? 186  SER A CB  1 
ATOM   1307 O  OG  . SER A 1 186 ? 5.144   143.347 19.544  1.00 26.14 ? 186  SER A OG  1 
ATOM   1308 N  N   . PHE A 1 187 ? 8.032   144.451 20.086  1.00 25.30 ? 187  PHE A N   1 
ATOM   1309 C  CA  . PHE A 1 187 ? 9.193   144.511 19.156  1.00 25.38 ? 187  PHE A CA  1 
ATOM   1310 C  C   . PHE A 1 187 ? 9.057   143.439 18.064  1.00 23.43 ? 187  PHE A C   1 
ATOM   1311 O  O   . PHE A 1 187 ? 9.961   143.318 17.233  1.00 23.38 ? 187  PHE A O   1 
ATOM   1312 C  CB  . PHE A 1 187 ? 10.502  144.355 19.934  1.00 25.57 ? 187  PHE A CB  1 
ATOM   1313 C  CG  . PHE A 1 187 ? 10.761  145.408 20.984  1.00 24.70 ? 187  PHE A CG  1 
ATOM   1314 C  CD1 . PHE A 1 187 ? 10.782  146.755 20.653  1.00 25.33 ? 187  PHE A CD1 1 
ATOM   1315 C  CD2 . PHE A 1 187 ? 11.043  145.050 22.294  1.00 25.36 ? 187  PHE A CD2 1 
ATOM   1316 C  CE1 . PHE A 1 187 ? 11.053  147.720 21.612  1.00 24.90 ? 187  PHE A CE1 1 
ATOM   1317 C  CE2 . PHE A 1 187 ? 11.307  146.019 23.256  1.00 24.97 ? 187  PHE A CE2 1 
ATOM   1318 C  CZ  . PHE A 1 187 ? 11.299  147.353 22.916  1.00 24.50 ? 187  PHE A CZ  1 
ATOM   1319 N  N   . LEU A 1 188 ? 7.946   142.699 18.036  1.00 24.58 ? 188  LEU A N   1 
ATOM   1320 C  CA  . LEU A 1 188 ? 7.768   141.568 17.089  1.00 24.65 ? 188  LEU A CA  1 
ATOM   1321 C  C   . LEU A 1 188 ? 7.839   142.114 15.659  1.00 24.57 ? 188  LEU A C   1 
ATOM   1322 O  O   . LEU A 1 188 ? 7.171   143.127 15.363  1.00 24.48 ? 188  LEU A O   1 
ATOM   1323 C  CB  . LEU A 1 188 ? 6.448   140.844 17.358  1.00 24.97 ? 188  LEU A CB  1 
ATOM   1324 C  CG  . LEU A 1 188 ? 6.210   139.590 16.509  1.00 26.07 ? 188  LEU A CG  1 
ATOM   1325 C  CD1 . LEU A 1 188 ? 7.237   138.507 16.814  1.00 24.82 ? 188  LEU A CD1 1 
ATOM   1326 C  CD2 . LEU A 1 188 ? 4.799   139.051 16.725  1.00 26.55 ? 188  LEU A CD2 1 
ATOM   1327 N  N   . GLY A 1 189 ? 8.675   141.504 14.819  1.00 23.67 ? 189  GLY A N   1 
ATOM   1328 C  CA  . GLY A 1 189 ? 8.809   141.893 13.403  1.00 24.09 ? 189  GLY A CA  1 
ATOM   1329 C  C   . GLY A 1 189 ? 9.772   143.051 13.223  1.00 23.88 ? 189  GLY A C   1 
ATOM   1330 O  O   . GLY A 1 189 ? 10.014  143.437 12.068  1.00 24.48 ? 189  GLY A O   1 
ATOM   1331 N  N   . GLN A 1 190 ? 10.343  143.557 14.318  1.00 24.24 ? 190  GLN A N   1 
ATOM   1332 C  CA  . GLN A 1 190 ? 11.393  144.612 14.296  1.00 24.17 ? 190  GLN A CA  1 
ATOM   1333 C  C   . GLN A 1 190 ? 12.735  143.982 13.906  1.00 23.51 ? 190  GLN A C   1 
ATOM   1334 O  O   . GLN A 1 190 ? 12.930  142.779 14.156  1.00 22.80 ? 190  GLN A O   1 
ATOM   1335 C  CB  . GLN A 1 190 ? 11.480  145.290 15.664  1.00 24.33 ? 190  GLN A CB  1 
ATOM   1336 C  CG  . GLN A 1 190 ? 12.340  146.539 15.668  1.00 25.50 ? 190  GLN A CG  1 
ATOM   1337 C  CD  . GLN A 1 190 ? 12.007  147.466 16.808  1.00 26.05 ? 190  GLN A CD  1 
ATOM   1338 O  OE1 . GLN A 1 190 ? 10.855  147.582 17.224  1.00 26.62 ? 190  GLN A OE1 1 
ATOM   1339 N  NE2 . GLN A 1 190 ? 13.019  148.150 17.319  1.00 28.38 ? 190  GLN A NE2 1 
ATOM   1340 N  N   . TYR A 1 191 ? 13.621  144.773 13.302  1.00 22.60 ? 191  TYR A N   1 
ATOM   1341 C  CA  . TYR A 1 191 ? 15.032  144.405 13.030  1.00 23.39 ? 191  TYR A CA  1 
ATOM   1342 C  C   . TYR A 1 191 ? 15.942  145.388 13.775  1.00 23.12 ? 191  TYR A C   1 
ATOM   1343 O  O   . TYR A 1 191 ? 15.566  146.542 14.026  1.00 24.54 ? 191  TYR A O   1 
ATOM   1344 C  CB  . TYR A 1 191 ? 15.356  144.432 11.537  1.00 23.17 ? 191  TYR A CB  1 
ATOM   1345 C  CG  . TYR A 1 191 ? 14.668  143.438 10.635  1.00 23.96 ? 191  TYR A CG  1 
ATOM   1346 C  CD1 . TYR A 1 191 ? 13.324  143.565 10.324  1.00 24.79 ? 191  TYR A CD1 1 
ATOM   1347 C  CD2 . TYR A 1 191 ? 15.393  142.461 9.966   1.00 24.31 ? 191  TYR A CD2 1 
ATOM   1348 C  CE1 . TYR A 1 191 ? 12.701  142.703 9.435   1.00 24.35 ? 191  TYR A CE1 1 
ATOM   1349 C  CE2 . TYR A 1 191 ? 14.791  141.605 9.059   1.00 23.64 ? 191  TYR A CE2 1 
ATOM   1350 C  CZ  . TYR A 1 191 ? 13.441  141.730 8.788   1.00 24.80 ? 191  TYR A CZ  1 
ATOM   1351 O  OH  . TYR A 1 191 ? 12.825  140.883 7.912   1.00 24.97 ? 191  TYR A OH  1 
HETATM 1352 N  N   . 9IJ A 1 192 ? 17.107  144.935 14.092  1.00 23.33 ? 192  9IJ A N   1 
HETATM 1353 C  CA  . 9IJ A 1 192 ? 18.175  145.805 14.605  1.00 22.67 ? 192  9IJ A CA  1 
HETATM 1354 C  C   . 9IJ A 1 192 ? 19.427  145.656 13.744  1.00 23.59 ? 192  9IJ A C   1 
HETATM 1355 C  CB  . 9IJ A 1 192 ? 18.476  145.626 16.086  1.00 23.69 ? 192  9IJ A CB  1 
HETATM 1356 C  CG  . 9IJ A 1 192 ? 18.670  144.213 16.565  1.00 23.46 ? 192  9IJ A CG  1 
HETATM 1357 C  CD1 . 9IJ A 1 192 ? 19.956  143.671 16.565  1.00 23.87 ? 192  9IJ A CD1 1 
HETATM 1358 C  CD2 . 9IJ A 1 192 ? 17.589  143.473 17.047  1.00 24.06 ? 192  9IJ A CD2 1 
HETATM 1359 C  CE1 . 9IJ A 1 192 ? 20.162  142.361 17.034  1.00 22.97 ? 192  9IJ A CE1 1 
HETATM 1360 C  CE2 . 9IJ A 1 192 ? 17.809  142.171 17.495  1.00 23.63 ? 192  9IJ A CE2 1 
HETATM 1361 C  CZ  . 9IJ A 1 192 ? 19.084  141.619 17.488  1.00 22.46 ? 192  9IJ A CZ  1 
HETATM 1362 C  C01 . 9IJ A 1 192 ? 16.386  143.966 17.028  1.00 25.19 ? 192  9IJ A C01 1 
HETATM 1363 N  N01 . 9IJ A 1 192 ? 15.325  144.453 16.914  1.00 25.51 ? 192  9IJ A N01 1 
HETATM 1364 O  O   . 9IJ A 1 192 ? 19.665  144.320 13.368  1.00 21.19 ? 192  9IJ A O   1 
ATOM   1365 N  N   . PRO A 1 193 ? 20.297  146.648 13.563  1.00 25.52 ? 193  PRO A N   1 
ATOM   1366 C  CA  . PRO A 1 193 ? 21.460  146.413 12.690  1.00 24.84 ? 193  PRO A CA  1 
ATOM   1367 C  C   . PRO A 1 193 ? 22.541  145.533 13.333  1.00 23.56 ? 193  PRO A C   1 
ATOM   1368 O  O   . PRO A 1 193 ? 22.531  145.328 14.540  1.00 22.25 ? 193  PRO A O   1 
ATOM   1369 C  CB  . PRO A 1 193 ? 22.004  147.827 12.427  1.00 25.44 ? 193  PRO A CB  1 
ATOM   1370 C  CG  . PRO A 1 193 ? 21.676  148.569 13.689  1.00 25.85 ? 193  PRO A CG  1 
ATOM   1371 C  CD  . PRO A 1 193 ? 20.377  147.968 14.181  1.00 25.54 ? 193  PRO A CD  1 
ATOM   1372 N  N   . ALA A 1 194 ? 23.468  145.059 12.508  1.00 22.80 ? 194  ALA A N   1 
ATOM   1373 C  CA  . ALA A 1 194 ? 24.611  144.234 12.943  1.00 24.62 ? 194  ALA A CA  1 
ATOM   1374 C  C   . ALA A 1 194 ? 25.390  144.978 14.043  1.00 25.01 ? 194  ALA A C   1 
ATOM   1375 O  O   . ALA A 1 194 ? 25.808  144.332 15.012  1.00 24.72 ? 194  ALA A O   1 
ATOM   1376 C  CB  . ALA A 1 194 ? 25.478  143.902 11.754  1.00 24.87 ? 194  ALA A CB  1 
ATOM   1377 N  N   . SER A 1 195 ? 25.560  146.297 13.900  1.00 26.15 ? 195  SER A N   1 
ATOM   1378 C  CA  . SER A 1 195 ? 26.430  147.130 14.778  1.00 26.87 ? 195  SER A CA  1 
ATOM   1379 C  C   . SER A 1 195 ? 25.900  147.150 16.221  1.00 25.70 ? 195  SER A C   1 
ATOM   1380 O  O   . SER A 1 195 ? 26.688  147.466 17.114  1.00 26.90 ? 195  SER A O   1 
ATOM   1381 C  CB  . SER A 1 195 ? 26.585  148.521 14.232  1.00 27.45 ? 195  SER A CB  1 
ATOM   1382 O  OG  . SER A 1 195 ? 25.331  149.182 14.182  1.00 27.59 ? 195  SER A OG  1 
ATOM   1383 N  N   . ASP A 1 196 ? 24.623  146.818 16.436  1.00 25.42 ? 196  ASP A N   1 
ATOM   1384 C  CA  . ASP A 1 196 ? 23.986  146.753 17.782  1.00 24.51 ? 196  ASP A CA  1 
ATOM   1385 C  C   . ASP A 1 196 ? 24.620  145.635 18.611  1.00 24.16 ? 196  ASP A C   1 
ATOM   1386 O  O   . ASP A 1 196 ? 24.557  145.705 19.859  1.00 23.85 ? 196  ASP A O   1 
ATOM   1387 C  CB  . ASP A 1 196 ? 22.471  146.576 17.685  1.00 23.94 ? 196  ASP A CB  1 
ATOM   1388 C  CG  . ASP A 1 196 ? 21.722  147.888 17.554  1.00 24.64 ? 196  ASP A CG  1 
ATOM   1389 O  OD1 . ASP A 1 196 ? 22.371  148.911 17.270  1.00 25.90 ? 196  ASP A OD1 1 
ATOM   1390 O  OD2 . ASP A 1 196 ? 20.502  147.874 17.732  1.00 27.02 ? 196  ASP A OD2 1 
ATOM   1391 N  N   . ILE A 1 197 ? 25.187  144.625 17.960  1.00 24.50 ? 197  ILE A N   1 
ATOM   1392 C  CA  . ILE A 1 197 ? 25.934  143.547 18.670  1.00 25.40 ? 197  ILE A CA  1 
ATOM   1393 C  C   . ILE A 1 197 ? 27.320  143.451 18.050  1.00 25.69 ? 197  ILE A C   1 
ATOM   1394 O  O   . ILE A 1 197 ? 27.485  142.824 17.008  1.00 25.03 ? 197  ILE A O   1 
ATOM   1395 C  CB  . ILE A 1 197 ? 25.183  142.204 18.652  1.00 25.79 ? 197  ILE A CB  1 
ATOM   1396 C  CG1 . ILE A 1 197 ? 23.758  142.339 19.191  1.00 25.66 ? 197  ILE A CG1 1 
ATOM   1397 C  CG2 . ILE A 1 197 ? 25.971  141.155 19.429  1.00 26.72 ? 197  ILE A CG2 1 
ATOM   1398 C  CD1 . ILE A 1 197 ? 22.955  141.067 19.096  1.00 25.25 ? 197  ILE A CD1 1 
ATOM   1399 N  N   . PRO A 1 198 ? 28.347  144.062 18.683  1.00 27.89 ? 198  PRO A N   1 
ATOM   1400 C  CA  . PRO A 1 198 ? 29.702  144.070 18.133  1.00 29.22 ? 198  PRO A CA  1 
ATOM   1401 C  C   . PRO A 1 198 ? 30.321  142.669 18.048  1.00 28.99 ? 198  PRO A C   1 
ATOM   1402 O  O   . PRO A 1 198 ? 29.860  141.770 18.729  1.00 26.56 ? 198  PRO A O   1 
ATOM   1403 C  CB  . PRO A 1 198 ? 30.480  144.981 19.101  1.00 30.45 ? 198  PRO A CB  1 
ATOM   1404 C  CG  . PRO A 1 198 ? 29.706  144.934 20.386  1.00 31.49 ? 198  PRO A CG  1 
ATOM   1405 C  CD  . PRO A 1 198 ? 28.260  144.783 19.964  1.00 30.42 ? 198  PRO A CD  1 
ATOM   1406 N  N   . GLN A 1 199 ? 31.368  142.527 17.228  1.00 30.19 ? 199  GLN A N   1 
ATOM   1407 C  CA  . GLN A 1 199 ? 31.965  141.210 16.873  1.00 32.19 ? 199  GLN A CA  1 
ATOM   1408 C  C   . GLN A 1 199 ? 32.404  140.457 18.135  1.00 29.81 ? 199  GLN A C   1 
ATOM   1409 O  O   . GLN A 1 199 ? 32.188  139.241 18.170  1.00 30.17 ? 199  GLN A O   1 
ATOM   1410 C  CB  . GLN A 1 199 ? 33.114  141.378 15.879  1.00 36.53 ? 199  GLN A CB  1 
ATOM   1411 C  CG  . GLN A 1 199 ? 32.638  141.754 14.482  1.00 41.70 ? 199  GLN A CG  1 
ATOM   1412 C  CD  . GLN A 1 199 ? 31.577  140.809 13.964  1.00 46.99 ? 199  GLN A CD  1 
ATOM   1413 O  OE1 . GLN A 1 199 ? 30.454  141.212 13.661  1.00 56.59 ? 199  GLN A OE1 1 
ATOM   1414 N  NE2 . GLN A 1 199 ? 31.914  139.531 13.884  1.00 49.27 ? 199  GLN A NE2 1 
ATOM   1415 N  N   . GLN A 1 200 ? 32.971  141.139 19.134  1.00 30.96 ? 200  GLN A N   1 
ATOM   1416 C  CA  . GLN A 1 200 ? 33.456  140.491 20.389  1.00 32.38 ? 200  GLN A CA  1 
ATOM   1417 C  C   . GLN A 1 200 ? 32.250  139.943 21.171  1.00 29.22 ? 200  GLN A C   1 
ATOM   1418 O  O   . GLN A 1 200 ? 32.346  138.819 21.725  1.00 28.03 ? 200  GLN A O   1 
ATOM   1419 C  CB  . GLN A 1 200 ? 34.310  141.470 21.200  1.00 37.48 ? 200  GLN A CB  1 
ATOM   1420 C  CG  . GLN A 1 200 ? 34.843  140.906 22.517  1.00 43.55 ? 200  GLN A CG  1 
ATOM   1421 C  CD  . GLN A 1 200 ? 35.947  139.884 22.366  1.00 49.06 ? 200  GLN A CD  1 
ATOM   1422 O  OE1 . GLN A 1 200 ? 35.884  138.790 22.920  1.00 56.94 ? 200  GLN A OE1 1 
ATOM   1423 N  NE2 . GLN A 1 200 ? 36.985  140.235 21.624  1.00 52.34 ? 200  GLN A NE2 1 
ATOM   1424 N  N   . ALA A 1 201 ? 31.137  140.681 21.207  1.00 28.41 ? 201  ALA A N   1 
ATOM   1425 C  CA  . ALA A 1 201 ? 29.889  140.220 21.870  1.00 27.26 ? 201  ALA A CA  1 
ATOM   1426 C  C   . ALA A 1 201 ? 29.386  138.967 21.144  1.00 26.42 ? 201  ALA A C   1 
ATOM   1427 O  O   . ALA A 1 201 ? 29.046  137.985 21.832  1.00 25.21 ? 201  ALA A O   1 
ATOM   1428 C  CB  . ALA A 1 201 ? 28.861  141.325 21.918  1.00 27.02 ? 201  ALA A CB  1 
ATOM   1429 N  N   . ARG A 1 202 ? 29.408  138.964 19.803  1.00 27.77 ? 202  ARG A N   1 
ATOM   1430 C  CA  . ARG A 1 202 ? 28.966  137.787 19.000  1.00 27.72 ? 202  ARG A CA  1 
ATOM   1431 C  C   . ARG A 1 202 ? 29.835  136.571 19.330  1.00 27.89 ? 202  ARG A C   1 
ATOM   1432 O  O   . ARG A 1 202 ? 29.271  135.485 19.539  1.00 27.15 ? 202  ARG A O   1 
ATOM   1433 C  CB  . ARG A 1 202 ? 29.019  138.063 17.497  1.00 29.63 ? 202  ARG A CB  1 
ATOM   1434 C  CG  . ARG A 1 202 ? 27.891  138.958 17.020  1.00 31.03 ? 202  ARG A CG  1 
ATOM   1435 C  CD  . ARG A 1 202 ? 28.016  139.378 15.572  1.00 31.81 ? 202  ARG A CD  1 
ATOM   1436 N  NE  . ARG A 1 202 ? 27.106  140.496 15.392  1.00 31.94 ? 202  ARG A NE  1 
ATOM   1437 C  CZ  . ARG A 1 202 ? 25.859  140.420 14.955  1.00 30.62 ? 202  ARG A CZ  1 
ATOM   1438 N  NH1 . ARG A 1 202 ? 25.334  139.264 14.586  1.00 32.39 ? 202  ARG A NH1 1 
ATOM   1439 N  NH2 . ARG A 1 202 ? 25.144  141.525 14.872  1.00 30.61 ? 202  ARG A NH2 1 
ATOM   1440 N  N   . ALA A 1 203 ? 31.158  136.745 19.330  1.00 27.68 ? 203  ALA A N   1 
ATOM   1441 C  CA  . ALA A 1 203 ? 32.144  135.688 19.649  1.00 28.00 ? 203  ALA A CA  1 
ATOM   1442 C  C   . ALA A 1 203 ? 31.802  135.102 21.024  1.00 27.35 ? 203  ALA A C   1 
ATOM   1443 O  O   . ALA A 1 203 ? 31.811  133.866 21.169  1.00 27.55 ? 203  ALA A O   1 
ATOM   1444 C  CB  . ALA A 1 203 ? 33.550  136.251 19.603  1.00 28.73 ? 203  ALA A CB  1 
ATOM   1445 N  N   . LEU A 1 204 ? 31.472  135.963 21.992  1.00 27.73 ? 204  LEU A N   1 
ATOM   1446 C  CA  . LEU A 1 204 ? 31.161  135.538 23.388  1.00 27.24 ? 204  LEU A CA  1 
ATOM   1447 C  C   . LEU A 1 204 ? 29.797  134.834 23.442  1.00 26.59 ? 204  LEU A C   1 
ATOM   1448 O  O   . LEU A 1 204 ? 29.685  133.868 24.215  1.00 24.91 ? 204  LEU A O   1 
ATOM   1449 C  CB  . LEU A 1 204 ? 31.238  136.749 24.325  1.00 26.51 ? 204  LEU A CB  1 
ATOM   1450 C  CG  . LEU A 1 204 ? 32.663  137.241 24.596  1.00 26.86 ? 204  LEU A CG  1 
ATOM   1451 C  CD1 . LEU A 1 204 ? 32.672  138.575 25.318  1.00 27.99 ? 204  LEU A CD1 1 
ATOM   1452 C  CD2 . LEU A 1 204 ? 33.459  136.219 25.387  1.00 26.83 ? 204  LEU A CD2 1 
ATOM   1453 N  N   . TYR A 1 205 ? 28.811  135.274 22.644  1.00 27.02 ? 205  TYR A N   1 
ATOM   1454 C  CA  . TYR A 1 205 ? 27.487  134.602 22.529  1.00 26.64 ? 205  TYR A CA  1 
ATOM   1455 C  C   . TYR A 1 205 ? 27.689  133.194 21.942  1.00 27.23 ? 205  TYR A C   1 
ATOM   1456 O  O   . TYR A 1 205 ? 27.013  132.248 22.382  1.00 26.86 ? 205  TYR A O   1 
ATOM   1457 C  CB  . TYR A 1 205 ? 26.487  135.424 21.706  1.00 25.39 ? 205  TYR A CB  1 
ATOM   1458 C  CG  . TYR A 1 205 ? 25.891  136.611 22.415  1.00 24.39 ? 205  TYR A CG  1 
ATOM   1459 C  CD1 . TYR A 1 205 ? 25.275  136.485 23.650  1.00 23.73 ? 205  TYR A CD1 1 
ATOM   1460 C  CD2 . TYR A 1 205 ? 25.936  137.873 21.846  1.00 24.28 ? 205  TYR A CD2 1 
ATOM   1461 C  CE1 . TYR A 1 205 ? 24.744  137.583 24.308  1.00 24.45 ? 205  TYR A CE1 1 
ATOM   1462 C  CE2 . TYR A 1 205 ? 25.406  138.978 22.490  1.00 24.36 ? 205  TYR A CE2 1 
ATOM   1463 C  CZ  . TYR A 1 205 ? 24.805  138.837 23.724  1.00 24.08 ? 205  TYR A CZ  1 
ATOM   1464 O  OH  . TYR A 1 205 ? 24.283  139.936 24.352  1.00 23.86 ? 205  TYR A OH  1 
ATOM   1465 N  N   . LEU A 1 206 ? 28.629  133.040 21.008  1.00 28.69 ? 206  LEU A N   1 
ATOM   1466 C  CA  . LEU A 1 206 ? 28.919  131.731 20.361  1.00 30.45 ? 206  LEU A CA  1 
ATOM   1467 C  C   . LEU A 1 206 ? 29.626  130.809 21.357  1.00 31.73 ? 206  LEU A C   1 
ATOM   1468 O  O   . LEU A 1 206 ? 29.349  129.611 21.390  1.00 33.85 ? 206  LEU A O   1 
ATOM   1469 C  CB  . LEU A 1 206 ? 29.741  131.986 19.091  1.00 33.15 ? 206  LEU A CB  1 
ATOM   1470 C  CG  . LEU A 1 206 ? 30.074  130.768 18.228  1.00 33.86 ? 206  LEU A CG  1 
ATOM   1471 C  CD1 . LEU A 1 206 ? 28.817  130.025 17.811  1.00 33.73 ? 206  LEU A CD1 1 
ATOM   1472 C  CD2 . LEU A 1 206 ? 30.882  131.180 17.004  1.00 34.07 ? 206  LEU A CD2 1 
HETATM 1473 N  N   . MLZ A 1 207 ? 30.491  131.378 22.207  1.00 31.92 ? 207  MLZ A N   1 
HETATM 1474 C  CA  . MLZ A 1 207 ? 31.309  130.606 23.135  1.00 33.44 ? 207  MLZ A CA  1 
HETATM 1475 C  CB  . MLZ A 1 207 ? 32.531  131.422 23.570  1.00 37.38 ? 207  MLZ A CB  1 
HETATM 1476 C  CG  . MLZ A 1 207 ? 33.667  131.479 22.562  1.00 41.07 ? 207  MLZ A CG  1 
HETATM 1477 C  CD  . MLZ A 1 207 ? 34.723  132.508 22.906  1.00 44.05 ? 207  MLZ A CD  1 
HETATM 1478 C  CE  . MLZ A 1 207 ? 36.031  132.271 22.164  1.00 46.80 ? 207  MLZ A CE  1 
HETATM 1479 N  NZ  . MLZ A 1 207 ? 37.014  133.322 22.439  1.00 48.93 ? 207  MLZ A NZ  1 
HETATM 1480 C  CM  . MLZ A 1 207 ? 37.439  133.497 23.834  1.00 47.80 ? 207  MLZ A CM  1 
HETATM 1481 C  C   . MLZ A 1 207 ? 30.544  130.193 24.393  1.00 31.77 ? 207  MLZ A C   1 
HETATM 1482 O  O   . MLZ A 1 207 ? 30.884  129.184 24.997  1.00 32.46 ? 207  MLZ A O   1 
ATOM   1483 N  N   . ASN A 1 208 ? 29.571  130.999 24.835  1.00 30.99 ? 208  ASN A N   1 
ATOM   1484 C  CA  . ASN A 1 208 ? 28.842  130.728 26.068  1.00 29.34 ? 208  ASN A CA  1 
ATOM   1485 C  C   . ASN A 1 208 ? 27.364  130.504 25.733  1.00 28.40 ? 208  ASN A C   1 
ATOM   1486 O  O   . ASN A 1 208 ? 26.799  131.312 25.005  1.00 28.11 ? 208  ASN A O   1 
ATOM   1487 C  CB  . ASN A 1 208 ? 28.951  131.890 27.063  1.00 31.02 ? 208  ASN A CB  1 
ATOM   1488 C  CG  . ASN A 1 208 ? 30.368  132.229 27.477  1.00 33.05 ? 208  ASN A CG  1 
ATOM   1489 O  OD1 . ASN A 1 208 ? 30.966  131.519 28.284  1.00 36.57 ? 208  ASN A OD1 1 
ATOM   1490 N  ND2 . ASN A 1 208 ? 30.898  133.335 26.976  1.00 31.46 ? 208  ASN A ND2 1 
ATOM   1491 N  N   . THR A 1 209 ? 26.745  129.457 26.268  1.00 29.72 ? 209  THR A N   1 
ATOM   1492 C  CA  . THR A 1 209 ? 25.297  129.180 26.062  1.00 29.76 ? 209  THR A CA  1 
ATOM   1493 C  C   . THR A 1 209 ? 24.462  130.296 26.692  1.00 27.28 ? 209  THR A C   1 
ATOM   1494 O  O   . THR A 1 209 ? 23.477  130.714 26.053  1.00 25.75 ? 209  THR A O   1 
ATOM   1495 C  CB  . THR A 1 209 ? 24.881  127.830 26.654  1.00 31.99 ? 209  THR A CB  1 
ATOM   1496 O  OG1 . THR A 1 209 ? 25.693  126.843 26.026  1.00 33.31 ? 209  THR A OG1 1 
ATOM   1497 C  CG2 . THR A 1 209 ? 23.417  127.520 26.428  1.00 33.50 ? 209  THR A CG2 1 
ATOM   1498 N  N   . LEU A 1 210 ? 24.842  130.730 27.900  1.00 25.41 ? 210  LEU A N   1 
ATOM   1499 C  CA  . LEU A 1 210 ? 24.093  131.726 28.715  1.00 26.97 ? 210  LEU A CA  1 
ATOM   1500 C  C   . LEU A 1 210 ? 24.917  133.003 28.870  1.00 27.30 ? 210  LEU A C   1 
ATOM   1501 O  O   . LEU A 1 210 ? 26.134  132.923 29.134  1.00 28.13 ? 210  LEU A O   1 
ATOM   1502 C  CB  . LEU A 1 210 ? 23.770  131.167 30.106  1.00 27.56 ? 210  LEU A CB  1 
ATOM   1503 C  CG  . LEU A 1 210 ? 22.874  129.934 30.162  1.00 27.42 ? 210  LEU A CG  1 
ATOM   1504 C  CD1 . LEU A 1 210 ? 22.510  129.618 31.604  1.00 28.30 ? 210  LEU A CD1 1 
ATOM   1505 C  CD2 . LEU A 1 210 ? 21.616  130.130 29.342  1.00 28.22 ? 210  LEU A CD2 1 
ATOM   1506 N  N   . ARG A 1 211 ? 24.247  134.141 28.745  1.00 25.77 ? 211  ARG A N   1 
ATOM   1507 C  CA  . ARG A 1 211 ? 24.779  135.450 29.173  1.00 25.61 ? 211  ARG A CA  1 
ATOM   1508 C  C   . ARG A 1 211 ? 23.779  135.995 30.195  1.00 26.92 ? 211  ARG A C   1 
ATOM   1509 O  O   . ARG A 1 211 ? 22.583  136.169 29.827  1.00 25.27 ? 211  ARG A O   1 
ATOM   1510 C  CB  . ARG A 1 211 ? 24.974  136.364 27.959  1.00 25.56 ? 211  ARG A CB  1 
ATOM   1511 C  CG  . ARG A 1 211 ? 25.429  137.775 28.299  1.00 25.88 ? 211  ARG A CG  1 
ATOM   1512 C  CD  . ARG A 1 211 ? 26.624  137.796 29.227  1.00 25.26 ? 211  ARG A CD  1 
ATOM   1513 N  NE  . ARG A 1 211 ? 27.200  139.127 29.319  1.00 25.26 ? 211  ARG A NE  1 
ATOM   1514 C  CZ  . ARG A 1 211 ? 28.021  139.545 30.282  1.00 26.18 ? 211  ARG A CZ  1 
ATOM   1515 N  NH1 . ARG A 1 211 ? 28.347  138.748 31.290  1.00 26.19 ? 211  ARG A NH1 1 
ATOM   1516 N  NH2 . ARG A 1 211 ? 28.508  140.772 30.234  1.00 25.02 ? 211  ARG A NH2 1 
ATOM   1517 N  N   . ILE A 1 212 ? 24.246  136.236 31.424  1.00 24.98 ? 212  ILE A N   1 
ATOM   1518 C  CA  . ILE A 1 212 ? 23.418  136.735 32.557  1.00 25.15 ? 212  ILE A CA  1 
ATOM   1519 C  C   . ILE A 1 212 ? 23.757  138.206 32.819  1.00 24.99 ? 212  ILE A C   1 
ATOM   1520 O  O   . ILE A 1 212 ? 24.954  138.537 32.932  1.00 24.74 ? 212  ILE A O   1 
ATOM   1521 C  CB  . ILE A 1 212 ? 23.645  135.877 33.815  1.00 25.63 ? 212  ILE A CB  1 
ATOM   1522 C  CG1 . ILE A 1 212 ? 23.227  134.425 33.584  1.00 27.38 ? 212  ILE A CG1 1 
ATOM   1523 C  CG2 . ILE A 1 212 ? 22.935  136.485 35.018  1.00 25.93 ? 212  ILE A CG2 1 
ATOM   1524 C  CD1 . ILE A 1 212 ? 24.355  133.524 33.152  1.00 28.28 ? 212  ILE A CD1 1 
ATOM   1525 N  N   . ILE A 1 213 ? 22.729  139.040 32.948  1.00 24.10 ? 213  ILE A N   1 
ATOM   1526 C  CA  . ILE A 1 213 ? 22.833  140.423 33.491  1.00 24.88 ? 213  ILE A CA  1 
ATOM   1527 C  C   . ILE A 1 213 ? 21.804  140.528 34.621  1.00 25.83 ? 213  ILE A C   1 
ATOM   1528 O  O   . ILE A 1 213 ? 20.605  140.557 34.322  1.00 25.17 ? 213  ILE A O   1 
ATOM   1529 C  CB  . ILE A 1 213 ? 22.628  141.481 32.389  1.00 24.74 ? 213  ILE A CB  1 
ATOM   1530 C  CG1 . ILE A 1 213 ? 23.652  141.320 31.260  1.00 25.17 ? 213  ILE A CG1 1 
ATOM   1531 C  CG2 . ILE A 1 213 ? 22.648  142.880 32.989  1.00 25.68 ? 213  ILE A CG2 1 
ATOM   1532 C  CD1 . ILE A 1 213 ? 23.411  142.216 30.071  1.00 24.11 ? 213  ILE A CD1 1 
ATOM   1533 N  N   . SER A 1 214 ? 22.274  140.535 35.870  1.00 26.12 ? 214  SER A N   1 
ATOM   1534 C  CA  . SER A 1 214 ? 21.423  140.554 37.086  1.00 27.36 ? 214  SER A CA  1 
ATOM   1535 C  C   . SER A 1 214 ? 20.855  141.960 37.311  1.00 27.96 ? 214  SER A C   1 
ATOM   1536 O  O   . SER A 1 214 ? 19.726  142.055 37.836  1.00 28.67 ? 214  SER A O   1 
ATOM   1537 C  CB  . SER A 1 214 ? 22.201  140.068 38.286  1.00 27.41 ? 214  SER A CB  1 
ATOM   1538 O  OG  . SER A 1 214 ? 23.366  140.858 38.476  1.00 27.39 ? 214  SER A OG  1 
ATOM   1539 N  N   . ASP A 1 215 ? 21.595  143.011 36.933  1.00 29.57 ? 215  ASP A N   1 
ATOM   1540 C  CA  . ASP A 1 215 ? 21.207  144.424 37.210  1.00 31.04 ? 215  ASP A CA  1 
ATOM   1541 C  C   . ASP A 1 215 ? 21.912  145.384 36.241  1.00 32.21 ? 215  ASP A C   1 
ATOM   1542 O  O   . ASP A 1 215 ? 23.134  145.523 36.333  1.00 33.53 ? 215  ASP A O   1 
ATOM   1543 C  CB  . ASP A 1 215 ? 21.528  144.791 38.661  1.00 34.56 ? 215  ASP A CB  1 
ATOM   1544 C  CG  . ASP A 1 215 ? 20.812  146.032 39.173  1.00 38.58 ? 215  ASP A CG  1 
ATOM   1545 O  OD1 . ASP A 1 215 ? 20.212  146.777 38.345  1.00 41.52 ? 215  ASP A OD1 1 
ATOM   1546 O  OD2 . ASP A 1 215 ? 20.862  146.250 40.399  1.00 40.12 ? 215  ASP A OD2 1 
ATOM   1547 N  N   . ALA A 1 216 ? 21.160  146.073 35.382  1.00 31.30 ? 216  ALA A N   1 
ATOM   1548 C  CA  . ALA A 1 216 ? 21.706  147.027 34.393  1.00 32.46 ? 216  ALA A CA  1 
ATOM   1549 C  C   . ALA A 1 216 ? 22.155  148.319 35.093  1.00 35.84 ? 216  ALA A C   1 
ATOM   1550 O  O   . ALA A 1 216 ? 22.891  149.096 34.451  1.00 36.69 ? 216  ALA A O   1 
ATOM   1551 C  CB  . ALA A 1 216 ? 20.686  147.309 33.327  1.00 32.12 ? 216  ALA A CB  1 
ATOM   1552 N  N   . SER A 1 217 ? 21.714  148.541 36.338  1.00 36.39 ? 217  SER A N   1 
ATOM   1553 C  CA  . SER A 1 217 ? 22.063  149.713 37.192  1.00 37.83 ? 217  SER A CA  1 
ATOM   1554 C  C   . SER A 1 217 ? 22.812  149.266 38.456  1.00 40.90 ? 217  SER A C   1 
ATOM   1555 O  O   . SER A 1 217 ? 22.939  150.079 39.376  1.00 46.72 ? 217  SER A O   1 
ATOM   1556 C  CB  . SER A 1 217 ? 20.831  150.486 37.569  1.00 38.86 ? 217  SER A CB  1 
ATOM   1557 O  OG  . SER A 1 217 ? 20.091  150.861 36.420  1.00 40.72 ? 217  SER A OG  1 
ATOM   1558 N  N   . GLY A 1 218 ? 23.271  148.014 38.507  1.00 45.09 ? 218  GLY A N   1 
ATOM   1559 C  CA  . GLY A 1 218 ? 24.096  147.476 39.607  1.00 45.55 ? 218  GLY A CA  1 
ATOM   1560 C  C   . GLY A 1 218 ? 25.494  148.068 39.575  1.00 46.96 ? 218  GLY A C   1 
ATOM   1561 O  O   . GLY A 1 218 ? 26.028  148.295 38.464  1.00 48.52 ? 218  GLY A O   1 
ATOM   1562 N  N   . THR A 1 219 ? 26.073  148.354 40.740  1.00 43.44 ? 219  THR A N   1 
ATOM   1563 C  CA  . THR A 1 219 ? 27.452  148.898 40.821  1.00 44.77 ? 219  THR A CA  1 
ATOM   1564 C  C   . THR A 1 219 ? 28.427  147.759 40.507  1.00 40.89 ? 219  THR A C   1 
ATOM   1565 O  O   . THR A 1 219 ? 28.374  146.735 41.209  1.00 47.41 ? 219  THR A O   1 
ATOM   1566 C  CB  . THR A 1 219 ? 27.724  149.568 42.173  1.00 47.64 ? 219  THR A CB  1 
ATOM   1567 O  OG1 . THR A 1 219 ? 26.702  150.544 42.378  1.00 48.46 ? 219  THR A OG1 1 
ATOM   1568 C  CG2 . THR A 1 219 ? 29.087  150.226 42.235  1.00 46.99 ? 219  THR A CG2 1 
ATOM   1569 N  N   . ARG A 1 220 ? 29.263  147.936 39.483  1.00 36.39 ? 220  ARG A N   1 
ATOM   1570 C  CA  . ARG A 1 220 ? 30.346  146.984 39.114  1.00 36.05 ? 220  ARG A CA  1 
ATOM   1571 C  C   . ARG A 1 220 ? 31.252  146.763 40.330  1.00 32.60 ? 220  ARG A C   1 
ATOM   1572 O  O   . ARG A 1 220 ? 31.430  147.700 41.096  1.00 31.32 ? 220  ARG A O   1 
ATOM   1573 C  CB  . ARG A 1 220 ? 31.185  147.539 37.959  1.00 38.02 ? 220  ARG A CB  1 
ATOM   1574 C  CG  . ARG A 1 220 ? 30.416  147.712 36.661  1.00 40.70 ? 220  ARG A CG  1 
ATOM   1575 C  CD  . ARG A 1 220 ? 31.239  148.322 35.541  1.00 42.59 ? 220  ARG A CD  1 
ATOM   1576 N  NE  . ARG A 1 220 ? 30.421  148.406 34.328  1.00 46.43 ? 220  ARG A NE  1 
ATOM   1577 C  CZ  . ARG A 1 220 ? 29.487  149.332 34.092  1.00 46.17 ? 220  ARG A CZ  1 
ATOM   1578 N  NH1 . ARG A 1 220 ? 29.245  150.281 34.982  1.00 46.28 ? 220  ARG A NH1 1 
ATOM   1579 N  NH2 . ARG A 1 220 ? 28.799  149.313 32.960  1.00 44.01 ? 220  ARG A NH2 1 
ATOM   1580 N  N   . ILE A 1 221 ? 31.801  145.559 40.480  1.00 31.27 ? 221  ILE A N   1 
ATOM   1581 C  CA  . ILE A 1 221 ? 32.762  145.184 41.557  1.00 30.03 ? 221  ILE A CA  1 
ATOM   1582 C  C   . ILE A 1 221 ? 34.126  144.989 40.904  1.00 28.94 ? 221  ILE A C   1 
ATOM   1583 O  O   . ILE A 1 221 ? 34.272  144.144 40.026  1.00 28.90 ? 221  ILE A O   1 
ATOM   1584 C  CB  . ILE A 1 221 ? 32.299  143.910 42.289  1.00 29.83 ? 221  ILE A CB  1 
ATOM   1585 C  CG1 . ILE A 1 221 ? 30.837  144.003 42.740  1.00 30.14 ? 221  ILE A CG1 1 
ATOM   1586 C  CG2 . ILE A 1 221 ? 33.232  143.581 43.447  1.00 29.86 ? 221  ILE A CG2 1 
ATOM   1587 C  CD1 . ILE A 1 221 ? 30.554  145.096 43.743  1.00 31.05 ? 221  ILE A CD1 1 
ATOM   1588 N  N   . PRO A 1 222 ? 35.166  145.752 41.303  1.00 28.73 ? 222  PRO A N   1 
ATOM   1589 C  CA  . PRO A 1 222 ? 36.482  145.588 40.698  1.00 28.04 ? 222  PRO A CA  1 
ATOM   1590 C  C   . PRO A 1 222 ? 37.111  144.218 41.004  1.00 28.18 ? 222  PRO A C   1 
ATOM   1591 O  O   . PRO A 1 222 ? 36.925  143.677 42.086  1.00 28.39 ? 222  PRO A O   1 
ATOM   1592 C  CB  . PRO A 1 222 ? 37.333  146.731 41.271  1.00 29.14 ? 222  PRO A CB  1 
ATOM   1593 C  CG  . PRO A 1 222 ? 36.554  147.289 42.447  1.00 28.52 ? 222  PRO A CG  1 
ATOM   1594 C  CD  . PRO A 1 222 ? 35.124  146.816 42.321  1.00 28.01 ? 222  PRO A CD  1 
ATOM   1595 N  N   . VAL A 1 223 ? 37.819  143.685 40.012  1.00 27.11 ? 223  VAL A N   1 
ATOM   1596 C  CA  . VAL A 1 223 ? 38.755  142.538 40.142  1.00 29.93 ? 223  VAL A CA  1 
ATOM   1597 C  C   . VAL A 1 223 ? 40.104  143.109 40.590  1.00 29.90 ? 223  VAL A C   1 
ATOM   1598 O  O   . VAL A 1 223 ? 40.634  143.980 39.875  1.00 32.77 ? 223  VAL A O   1 
ATOM   1599 C  CB  . VAL A 1 223 ? 38.883  141.783 38.805  1.00 29.88 ? 223  VAL A CB  1 
ATOM   1600 C  CG1 . VAL A 1 223 ? 39.910  140.663 38.883  1.00 30.29 ? 223  VAL A CG1 1 
ATOM   1601 C  CG2 . VAL A 1 223 ? 37.539  141.257 38.331  1.00 30.98 ? 223  VAL A CG2 1 
ATOM   1602 N  N   . LEU A 1 224 ? 40.648  142.630 41.707  1.00 29.75 ? 224  LEU A N   1 
ATOM   1603 C  CA  . LEU A 1 224 ? 41.903  143.174 42.291  1.00 29.73 ? 224  LEU A CA  1 
ATOM   1604 C  C   . LEU A 1 224 ? 43.022  142.155 42.107  1.00 29.76 ? 224  LEU A C   1 
ATOM   1605 O  O   . LEU A 1 224 ? 42.946  141.066 42.677  1.00 29.32 ? 224  LEU A O   1 
ATOM   1606 C  CB  . LEU A 1 224 ? 41.685  143.478 43.774  1.00 30.65 ? 224  LEU A CB  1 
ATOM   1607 C  CG  . LEU A 1 224 ? 40.531  144.418 44.105  1.00 32.09 ? 224  LEU A CG  1 
ATOM   1608 C  CD1 . LEU A 1 224 ? 40.352  144.513 45.617  1.00 32.75 ? 224  LEU A CD1 1 
ATOM   1609 C  CD2 . LEU A 1 224 ? 40.760  145.796 43.497  1.00 32.42 ? 224  LEU A CD2 1 
ATOM   1610 N  N   . PRO A 1 225 ? 44.082  142.452 41.313  1.00 29.90 ? 225  PRO A N   1 
ATOM   1611 C  CA  . PRO A 1 225 ? 44.175  143.673 40.508  1.00 31.21 ? 225  PRO A CA  1 
ATOM   1612 C  C   . PRO A 1 225 ? 43.539  143.531 39.114  1.00 32.15 ? 225  PRO A C   1 
ATOM   1613 O  O   . PRO A 1 225 ? 43.401  142.414 38.649  1.00 28.66 ? 225  PRO A O   1 
ATOM   1614 C  CB  . PRO A 1 225 ? 45.693  143.837 40.364  1.00 31.97 ? 225  PRO A CB  1 
ATOM   1615 C  CG  . PRO A 1 225 ? 46.192  142.407 40.264  1.00 32.06 ? 225  PRO A CG  1 
ATOM   1616 C  CD  . PRO A 1 225 ? 45.270  141.601 41.157  1.00 30.15 ? 225  PRO A CD  1 
ATOM   1617 N  N   . ALA A 1 226 ? 43.180  144.655 38.484  1.00 33.52 ? 226  ALA A N   1 
ATOM   1618 C  CA  . ALA A 1 226 ? 42.667  144.710 37.094  1.00 34.88 ? 226  ALA A CA  1 
ATOM   1619 C  C   . ALA A 1 226 ? 43.794  144.288 36.145  1.00 36.04 ? 226  ALA A C   1 
ATOM   1620 O  O   . ALA A 1 226 ? 43.572  143.403 35.290  1.00 38.53 ? 226  ALA A O   1 
ATOM   1621 C  CB  . ALA A 1 226 ? 42.153  146.095 36.775  1.00 35.90 ? 226  ALA A CB  1 
ATOM   1622 N  N   . VAL A 1 227 ? 44.976  144.871 36.343  1.00 35.77 ? 227  VAL A N   1 
ATOM   1623 C  CA  . VAL A 1 227 ? 46.212  144.567 35.567  1.00 36.03 ? 227  VAL A CA  1 
ATOM   1624 C  C   . VAL A 1 227 ? 47.272  144.077 36.555  1.00 34.47 ? 227  VAL A C   1 
ATOM   1625 O  O   . VAL A 1 227 ? 47.610  144.838 37.478  1.00 33.66 ? 227  VAL A O   1 
ATOM   1626 C  CB  . VAL A 1 227 ? 46.677  145.800 34.773  1.00 36.50 ? 227  VAL A CB  1 
ATOM   1627 C  CG1 . VAL A 1 227 ? 47.931  145.501 33.963  1.00 36.51 ? 227  VAL A CG1 1 
ATOM   1628 C  CG2 . VAL A 1 227 ? 45.563  146.324 33.872  1.00 37.06 ? 227  VAL A CG2 1 
ATOM   1629 N  N   . ASP A 1 228 ? 47.755  142.850 36.366  1.00 35.30 ? 228  ASP A N   1 
ATOM   1630 C  CA  . ASP A 1 228 ? 48.666  142.157 37.317  1.00 37.84 ? 228  ASP A CA  1 
ATOM   1631 C  C   . ASP A 1 228 ? 50.090  142.719 37.175  1.00 39.95 ? 228  ASP A C   1 
ATOM   1632 O  O   . ASP A 1 228 ? 50.297  143.666 36.385  1.00 36.61 ? 228  ASP A O   1 
ATOM   1633 C  CB  . ASP A 1 228 ? 48.591  140.638 37.134  1.00 37.90 ? 228  ASP A CB  1 
ATOM   1634 C  CG  . ASP A 1 228 ? 49.308  140.074 35.919  1.00 39.37 ? 228  ASP A CG  1 
ATOM   1635 O  OD1 . ASP A 1 228 ? 49.945  140.858 35.173  1.00 40.43 ? 228  ASP A OD1 1 
ATOM   1636 O  OD2 . ASP A 1 228 ? 49.218  138.844 35.727  1.00 39.41 ? 228  ASP A OD2 1 
ATOM   1637 N  N   . VAL A 1 229 ? 51.043  142.156 37.919  1.00 41.17 ? 229  VAL A N   1 
ATOM   1638 C  CA  . VAL A 1 229 ? 52.431  142.701 38.011  1.00 43.69 ? 229  VAL A CA  1 
ATOM   1639 C  C   . VAL A 1 229 ? 53.120  142.568 36.642  1.00 43.71 ? 229  VAL A C   1 
ATOM   1640 O  O   . VAL A 1 229 ? 53.965  143.428 36.339  1.00 42.01 ? 229  VAL A O   1 
ATOM   1641 C  CB  . VAL A 1 229 ? 53.226  142.033 39.149  1.00 43.70 ? 229  VAL A CB  1 
ATOM   1642 C  CG1 . VAL A 1 229 ? 53.551  140.576 38.861  1.00 42.58 ? 229  VAL A CG1 1 
ATOM   1643 C  CG2 . VAL A 1 229 ? 54.483  142.822 39.476  1.00 44.59 ? 229  VAL A CG2 1 
ATOM   1644 N  N   . SER A 1 230 ? 52.722  141.575 35.832  1.00 43.01 ? 230  SER A N   1 
ATOM   1645 C  CA  . SER A 1 230 ? 53.253  141.311 34.462  1.00 43.75 ? 230  SER A CA  1 
ATOM   1646 C  C   . SER A 1 230 ? 52.557  142.181 33.400  1.00 44.24 ? 230  SER A C   1 
ATOM   1647 O  O   . SER A 1 230 ? 52.958  142.088 32.226  1.00 43.53 ? 230  SER A O   1 
ATOM   1648 C  CB  . SER A 1 230 ? 53.119  139.856 34.096  1.00 43.71 ? 230  SER A CB  1 
ATOM   1649 O  OG  . SER A 1 230 ? 53.594  139.019 35.136  1.00 45.36 ? 230  SER A OG  1 
ATOM   1650 N  N   . GLY A 1 231 ? 51.544  142.967 33.773  1.00 42.30 ? 231  GLY A N   1 
ATOM   1651 C  CA  . GLY A 1 231 ? 50.797  143.838 32.840  1.00 43.94 ? 231  GLY A CA  1 
ATOM   1652 C  C   . GLY A 1 231 ? 49.684  143.100 32.098  1.00 42.99 ? 231  GLY A C   1 
ATOM   1653 O  O   . GLY A 1 231 ? 49.205  143.632 31.082  1.00 43.38 ? 231  GLY A O   1 
ATOM   1654 N  N   . GLU A 1 232 ? 49.272  141.928 32.588  1.00 40.83 ? 232  GLU A N   1 
ATOM   1655 C  CA  . GLU A 1 232 ? 48.211  141.086 31.974  1.00 41.69 ? 232  GLU A CA  1 
ATOM   1656 C  C   . GLU A 1 232 ? 46.858  141.434 32.586  1.00 41.01 ? 232  GLU A C   1 
ATOM   1657 O  O   . GLU A 1 232 ? 46.704  141.401 33.810  1.00 38.23 ? 232  GLU A O   1 
ATOM   1658 C  CB  . GLU A 1 232 ? 48.477  139.599 32.210  1.00 44.99 ? 232  GLU A CB  1 
ATOM   1659 C  CG  . GLU A 1 232 ? 49.682  139.060 31.467  1.00 49.41 ? 232  GLU A CG  1 
ATOM   1660 C  CD  . GLU A 1 232 ? 49.591  139.160 29.957  1.00 51.98 ? 232  GLU A CD  1 
ATOM   1661 O  OE1 . GLU A 1 232 ? 50.653  139.242 29.314  1.00 53.43 ? 232  GLU A OE1 1 
ATOM   1662 O  OE2 . GLU A 1 232 ? 48.457  139.153 29.429  1.00 57.69 ? 232  GLU A OE2 1 
ATOM   1663 N  N   . PRO A 1 233 ? 45.832  141.749 31.760  1.00 38.41 ? 233  PRO A N   1 
ATOM   1664 C  CA  . PRO A 1 233 ? 44.461  141.827 32.252  1.00 36.55 ? 233  PRO A CA  1 
ATOM   1665 C  C   . PRO A 1 233 ? 43.962  140.400 32.503  1.00 34.07 ? 233  PRO A C   1 
ATOM   1666 O  O   . PRO A 1 233 ? 44.606  139.468 32.043  1.00 33.84 ? 233  PRO A O   1 
ATOM   1667 C  CB  . PRO A 1 233 ? 43.698  142.515 31.117  1.00 37.90 ? 233  PRO A CB  1 
ATOM   1668 C  CG  . PRO A 1 233 ? 44.468  142.116 29.876  1.00 39.07 ? 233  PRO A CG  1 
ATOM   1669 C  CD  . PRO A 1 233 ? 45.919  142.030 30.316  1.00 39.43 ? 233  PRO A CD  1 
ATOM   1670 N  N   . LEU A 1 234 ? 42.860  140.267 33.242  1.00 31.22 ? 234  LEU A N   1 
ATOM   1671 C  CA  . LEU A 1 234 ? 42.185  138.970 33.485  1.00 31.32 ? 234  LEU A CA  1 
ATOM   1672 C  C   . LEU A 1 234 ? 41.149  138.733 32.383  1.00 29.66 ? 234  LEU A C   1 
ATOM   1673 O  O   . LEU A 1 234 ? 40.167  139.507 32.311  1.00 31.98 ? 234  LEU A O   1 
ATOM   1674 C  CB  . LEU A 1 234 ? 41.517  138.990 34.861  1.00 30.78 ? 234  LEU A CB  1 
ATOM   1675 C  CG  . LEU A 1 234 ? 40.759  137.712 35.209  1.00 31.67 ? 234  LEU A CG  1 
ATOM   1676 C  CD1 . LEU A 1 234 ? 41.707  136.527 35.309  1.00 31.34 ? 234  LEU A CD1 1 
ATOM   1677 C  CD2 . LEU A 1 234 ? 39.975  137.883 36.504  1.00 33.61 ? 234  LEU A CD2 1 
ATOM   1678 N  N   . ASP A 1 235 ? 41.336  137.689 31.583  1.00 28.55 ? 235  ASP A N   1 
ATOM   1679 C  CA  . ASP A 1 235 ? 40.378  137.299 30.517  1.00 29.02 ? 235  ASP A CA  1 
ATOM   1680 C  C   . ASP A 1 235 ? 39.168  136.603 31.158  1.00 28.54 ? 235  ASP A C   1 
ATOM   1681 O  O   . ASP A 1 235 ? 39.314  135.465 31.627  1.00 28.32 ? 235  ASP A O   1 
ATOM   1682 C  CB  . ASP A 1 235 ? 41.050  136.447 29.440  1.00 30.04 ? 235  ASP A CB  1 
ATOM   1683 C  CG  . ASP A 1 235 ? 40.181  136.300 28.200  1.00 30.94 ? 235  ASP A CG  1 
ATOM   1684 O  OD1 . ASP A 1 235 ? 38.985  136.003 28.351  1.00 28.93 ? 235  ASP A OD1 1 
ATOM   1685 O  OD2 . ASP A 1 235 ? 40.697  136.508 27.103  1.00 36.20 ? 235  ASP A OD2 1 
ATOM   1686 N  N   . LEU A 1 236 ? 38.003  137.263 31.130  1.00 29.57 ? 236  LEU A N   1 
ATOM   1687 C  CA  . LEU A 1 236 ? 36.741  136.793 31.772  1.00 28.46 ? 236  LEU A CA  1 
ATOM   1688 C  C   . LEU A 1 236 ? 35.770  136.241 30.720  1.00 28.06 ? 236  LEU A C   1 
ATOM   1689 O  O   . LEU A 1 236 ? 34.555  136.211 31.002  1.00 26.28 ? 236  LEU A O   1 
ATOM   1690 C  CB  . LEU A 1 236 ? 36.122  137.968 32.533  1.00 29.54 ? 236  LEU A CB  1 
ATOM   1691 C  CG  . LEU A 1 236 ? 36.880  138.438 33.775  1.00 29.18 ? 236  LEU A CG  1 
ATOM   1692 C  CD1 . LEU A 1 236 ? 36.249  139.704 34.332  1.00 30.43 ? 236  LEU A CD1 1 
ATOM   1693 C  CD2 . LEU A 1 236 ? 36.917  137.354 34.840  1.00 29.14 ? 236  LEU A CD2 1 
ATOM   1694 N  N   . SER A 1 237 ? 36.289  135.757 29.584  1.00 27.73 ? 237  SER A N   1 
ATOM   1695 C  CA  . SER A 1 237 ? 35.480  135.272 28.433  1.00 28.32 ? 237  SER A CA  1 
ATOM   1696 C  C   . SER A 1 237 ? 34.452  134.228 28.896  1.00 28.59 ? 237  SER A C   1 
ATOM   1697 O  O   . SER A 1 237 ? 33.289  134.302 28.437  1.00 28.94 ? 237  SER A O   1 
ATOM   1698 C  CB  . SER A 1 237 ? 36.354  134.735 27.326  1.00 29.23 ? 237  SER A CB  1 
ATOM   1699 O  OG  . SER A 1 237 ? 37.029  135.787 26.654  1.00 28.11 ? 237  SER A OG  1 
ATOM   1700 N  N   . TYR A 1 238 ? 34.847  133.309 29.783  1.00 28.04 ? 238  TYR A N   1 
ATOM   1701 C  CA  . TYR A 1 238 ? 34.018  132.153 30.216  1.00 28.02 ? 238  TYR A CA  1 
ATOM   1702 C  C   . TYR A 1 238 ? 33.445  132.381 31.619  1.00 27.12 ? 238  TYR A C   1 
ATOM   1703 O  O   . TYR A 1 238 ? 32.820  131.447 32.162  1.00 27.53 ? 238  TYR A O   1 
ATOM   1704 C  CB  . TYR A 1 238 ? 34.837  130.865 30.119  1.00 29.20 ? 238  TYR A CB  1 
ATOM   1705 C  CG  . TYR A 1 238 ? 35.233  130.520 28.707  1.00 31.62 ? 238  TYR A CG  1 
ATOM   1706 C  CD1 . TYR A 1 238 ? 34.341  129.880 27.859  1.00 32.41 ? 238  TYR A CD1 1 
ATOM   1707 C  CD2 . TYR A 1 238 ? 36.476  130.870 28.204  1.00 32.24 ? 238  TYR A CD2 1 
ATOM   1708 C  CE1 . TYR A 1 238 ? 34.682  129.565 26.555  1.00 32.14 ? 238  TYR A CE1 1 
ATOM   1709 C  CE2 . TYR A 1 238 ? 36.830  130.569 26.898  1.00 33.85 ? 238  TYR A CE2 1 
ATOM   1710 C  CZ  . TYR A 1 238 ? 35.932  129.909 26.074  1.00 34.56 ? 238  TYR A CZ  1 
ATOM   1711 O  OH  . TYR A 1 238 ? 36.263  129.602 24.786  1.00 38.48 ? 238  TYR A OH  1 
ATOM   1712 N  N   . ALA A 1 239 ? 33.638  133.574 32.188  1.00 26.68 ? 239  ALA A N   1 
ATOM   1713 C  CA  . ALA A 1 239 ? 33.163  133.934 33.547  1.00 26.34 ? 239  ALA A CA  1 
ATOM   1714 C  C   . ALA A 1 239 ? 31.735  134.471 33.445  1.00 25.16 ? 239  ALA A C   1 
ATOM   1715 O  O   . ALA A 1 239 ? 31.543  135.502 32.772  1.00 24.55 ? 239  ALA A O   1 
ATOM   1716 C  CB  . ALA A 1 239 ? 34.077  134.957 34.178  1.00 26.64 ? 239  ALA A CB  1 
ATOM   1717 N  N   . HIS A 1 240 ? 30.777  133.819 34.105  1.00 26.60 ? 240  HIS A N   1 
ATOM   1718 C  CA  . HIS A 1 240 ? 29.341  134.209 34.053  1.00 26.24 ? 240  HIS A CA  1 
ATOM   1719 C  C   . HIS A 1 240 ? 29.136  135.548 34.783  1.00 25.66 ? 240  HIS A C   1 
ATOM   1720 O  O   . HIS A 1 240 ? 28.167  136.260 34.436  1.00 26.19 ? 240  HIS A O   1 
ATOM   1721 C  CB  . HIS A 1 240 ? 28.428  133.058 34.521  1.00 25.91 ? 240  HIS A CB  1 
ATOM   1722 C  CG  . HIS A 1 240 ? 28.413  132.787 35.989  1.00 25.84 ? 240  HIS A CG  1 
ATOM   1723 N  ND1 . HIS A 1 240 ? 27.770  133.607 36.886  1.00 26.65 ? 240  HIS A ND1 1 
ATOM   1724 C  CD2 . HIS A 1 240 ? 28.919  131.763 36.713  1.00 26.51 ? 240  HIS A CD2 1 
ATOM   1725 C  CE1 . HIS A 1 240 ? 27.899  133.114 38.105  1.00 26.20 ? 240  HIS A CE1 1 
ATOM   1726 N  NE2 . HIS A 1 240 ? 28.594  131.981 38.024  1.00 25.40 ? 240  HIS A NE2 1 
ATOM   1727 N  N   . LEU A 1 241 ? 30.035  135.915 35.702  1.00 24.83 ? 241  LEU A N   1 
ATOM   1728 C  CA  . LEU A 1 241 ? 29.938  137.167 36.505  1.00 25.19 ? 241  LEU A CA  1 
ATOM   1729 C  C   . LEU A 1 241 ? 30.538  138.361 35.762  1.00 25.28 ? 241  LEU A C   1 
ATOM   1730 O  O   . LEU A 1 241 ? 30.417  139.489 36.294  1.00 23.94 ? 241  LEU A O   1 
ATOM   1731 C  CB  . LEU A 1 241 ? 30.664  136.973 37.840  1.00 27.30 ? 241  LEU A CB  1 
ATOM   1732 C  CG  . LEU A 1 241 ? 30.024  135.974 38.802  1.00 27.66 ? 241  LEU A CG  1 
ATOM   1733 C  CD1 . LEU A 1 241 ? 30.894  135.776 40.034  1.00 27.36 ? 241  LEU A CD1 1 
ATOM   1734 C  CD2 . LEU A 1 241 ? 28.628  136.436 39.203  1.00 29.42 ? 241  LEU A CD2 1 
ATOM   1735 N  N   . ARG A 1 242 ? 31.186  138.133 34.612  1.00 25.23 ? 242  ARG A N   1 
ATOM   1736 C  CA  . ARG A 1 242 ? 31.824  139.210 33.807  1.00 25.72 ? 242  ARG A CA  1 
ATOM   1737 C  C   . ARG A 1 242 ? 30.878  140.413 33.717  1.00 25.76 ? 242  ARG A C   1 
ATOM   1738 O  O   . ARG A 1 242 ? 29.689  140.206 33.364  1.00 24.65 ? 242  ARG A O   1 
ATOM   1739 C  CB  . ARG A 1 242 ? 32.180  138.709 32.404  1.00 26.03 ? 242  ARG A CB  1 
ATOM   1740 C  CG  . ARG A 1 242 ? 32.788  139.770 31.497  1.00 26.63 ? 242  ARG A CG  1 
ATOM   1741 C  CD  . ARG A 1 242 ? 33.342  139.138 30.233  1.00 27.82 ? 242  ARG A CD  1 
ATOM   1742 N  NE  . ARG A 1 242 ? 32.309  138.315 29.615  1.00 30.06 ? 242  ARG A NE  1 
ATOM   1743 C  CZ  . ARG A 1 242 ? 31.396  138.751 28.757  1.00 30.63 ? 242  ARG A CZ  1 
ATOM   1744 N  NH1 . ARG A 1 242 ? 31.398  140.011 28.354  1.00 31.20 ? 242  ARG A NH1 1 
ATOM   1745 N  NH2 . ARG A 1 242 ? 30.492  137.911 28.288  1.00 32.54 ? 242  ARG A NH2 1 
ATOM   1746 N  N   . SER A 1 243 ? 31.401  141.620 33.972  1.00 24.36 ? 243  SER A N   1 
ATOM   1747 C  CA  . SER A 1 243 ? 30.627  142.889 33.940  1.00 24.83 ? 243  SER A CA  1 
ATOM   1748 C  C   . SER A 1 243 ? 30.184  143.188 32.503  1.00 25.37 ? 243  SER A C   1 
ATOM   1749 O  O   . SER A 1 243 ? 30.634  142.502 31.557  1.00 25.86 ? 243  SER A O   1 
ATOM   1750 C  CB  . SER A 1 243 ? 31.389  144.037 34.545  1.00 24.02 ? 243  SER A CB  1 
ATOM   1751 O  OG  . SER A 1 243 ? 32.545  144.330 33.776  1.00 24.60 ? 243  SER A OG  1 
ATOM   1752 N  N   . VAL A 1 244 ? 29.307  144.177 32.360  1.00 27.57 ? 244  VAL A N   1 
ATOM   1753 C  CA  . VAL A 1 244 ? 28.614  144.512 31.084  1.00 28.08 ? 244  VAL A CA  1 
ATOM   1754 C  C   . VAL A 1 244 ? 29.113  145.868 30.593  1.00 28.74 ? 244  VAL A C   1 
ATOM   1755 O  O   . VAL A 1 244 ? 29.264  146.780 31.430  1.00 27.31 ? 244  VAL A O   1 
ATOM   1756 C  CB  . VAL A 1 244 ? 27.087  144.536 31.277  1.00 27.98 ? 244  VAL A CB  1 
ATOM   1757 C  CG1 . VAL A 1 244 ? 26.363  144.773 29.958  1.00 28.78 ? 244  VAL A CG1 1 
ATOM   1758 C  CG2 . VAL A 1 244 ? 26.595  143.263 31.935  1.00 28.63 ? 244  VAL A CG2 1 
ATOM   1759 N  N   . SER A 1 245 ? 29.312  146.001 29.279  1.00 29.01 ? 245  SER A N   1 
ATOM   1760 C  CA  . SER A 1 245 ? 29.606  147.308 28.629  1.00 27.79 ? 245  SER A CA  1 
ATOM   1761 C  C   . SER A 1 245 ? 28.652  148.377 29.157  1.00 28.82 ? 245  SER A C   1 
ATOM   1762 O  O   . SER A 1 245 ? 27.441  148.154 29.204  1.00 30.48 ? 245  SER A O   1 
ATOM   1763 C  CB  . SER A 1 245 ? 29.516  147.226 27.140  1.00 27.60 ? 245  SER A CB  1 
ATOM   1764 O  OG  . SER A 1 245 ? 29.478  148.532 26.584  1.00 27.52 ? 245  SER A OG  1 
ATOM   1765 N  N   . PRO A 1 246 ? 29.161  149.569 29.551  1.00 28.82 ? 246  PRO A N   1 
ATOM   1766 C  CA  . PRO A 1 246 ? 28.313  150.709 29.889  1.00 28.20 ? 246  PRO A CA  1 
ATOM   1767 C  C   . PRO A 1 246 ? 27.439  151.158 28.707  1.00 27.66 ? 246  PRO A C   1 
ATOM   1768 O  O   . PRO A 1 246 ? 26.398  151.762 28.937  1.00 27.98 ? 246  PRO A O   1 
ATOM   1769 C  CB  . PRO A 1 246 ? 29.279  151.857 30.233  1.00 29.08 ? 246  PRO A CB  1 
ATOM   1770 C  CG  . PRO A 1 246 ? 30.635  151.216 30.390  1.00 29.67 ? 246  PRO A CG  1 
ATOM   1771 C  CD  . PRO A 1 246 ? 30.591  149.887 29.667  1.00 29.48 ? 246  PRO A CD  1 
ATOM   1772 N  N   . ILE A 1 247 ? 27.876  150.872 27.479  1.00 25.89 ? 247  ILE A N   1 
ATOM   1773 C  CA  . ILE A 1 247 ? 27.065  151.142 26.258  1.00 27.10 ? 247  ILE A CA  1 
ATOM   1774 C  C   . ILE A 1 247 ? 25.766  150.345 26.392  1.00 26.25 ? 247  ILE A C   1 
ATOM   1775 O  O   . ILE A 1 247 ? 24.681  150.954 26.358  1.00 26.52 ? 247  ILE A O   1 
ATOM   1776 C  CB  . ILE A 1 247 ? 27.828  150.782 24.971  1.00 28.60 ? 247  ILE A CB  1 
ATOM   1777 C  CG1 . ILE A 1 247 ? 29.129  151.574 24.843  1.00 30.65 ? 247  ILE A CG1 1 
ATOM   1778 C  CG2 . ILE A 1 247 ? 26.935  150.965 23.749  1.00 29.43 ? 247  ILE A CG2 1 
ATOM   1779 C  CD1 . ILE A 1 247 ? 28.942  153.074 24.805  1.00 31.24 ? 247  ILE A CD1 1 
ATOM   1780 N  N   . HIS A 1 248 ? 25.885  149.028 26.563  1.00 26.84 ? 248  HIS A N   1 
ATOM   1781 C  CA  . HIS A 1 248 ? 24.719  148.113 26.628  1.00 26.79 ? 248  HIS A CA  1 
ATOM   1782 C  C   . HIS A 1 248 ? 23.888  148.413 27.879  1.00 26.19 ? 248  HIS A C   1 
ATOM   1783 O  O   . HIS A 1 248 ? 22.653  148.379 27.780  1.00 27.56 ? 248  HIS A O   1 
ATOM   1784 C  CB  . HIS A 1 248 ? 25.136  146.640 26.553  1.00 26.39 ? 248  HIS A CB  1 
ATOM   1785 C  CG  . HIS A 1 248 ? 23.940  145.759 26.508  1.00 25.63 ? 248  HIS A CG  1 
ATOM   1786 N  ND1 . HIS A 1 248 ? 22.963  145.924 25.550  1.00 25.61 ? 248  HIS A ND1 1 
ATOM   1787 C  CD2 . HIS A 1 248 ? 23.520  144.760 27.315  1.00 25.92 ? 248  HIS A CD2 1 
ATOM   1788 C  CE1 . HIS A 1 248 ? 22.007  145.034 25.743  1.00 26.12 ? 248  HIS A CE1 1 
ATOM   1789 N  NE2 . HIS A 1 248 ? 22.323  144.306 26.815  1.00 24.85 ? 248  HIS A NE2 1 
ATOM   1790 N  N   . CYS A 1 249 ? 24.514  148.722 29.014  1.00 27.27 ? 249  CYS A N   1 
ATOM   1791 C  CA  . CYS A 1 249 ? 23.756  149.059 30.256  1.00 29.29 ? 249  CYS A CA  1 
ATOM   1792 C  C   . CYS A 1 249 ? 22.880  150.302 30.036  1.00 27.64 ? 249  CYS A C   1 
ATOM   1793 O  O   . CYS A 1 249 ? 21.727  150.297 30.484  1.00 28.89 ? 249  CYS A O   1 
ATOM   1794 C  CB  . CYS A 1 249 ? 24.689  149.245 31.444  1.00 31.30 ? 249  CYS A CB  1 
ATOM   1795 S  SG  . CYS A 1 249 ? 25.351  147.662 32.023  1.00 33.40 ? 249  CYS A SG  1 
ATOM   1796 N  N   . GLU A 1 250 ? 23.407  151.320 29.363  1.00 28.29 ? 250  GLU A N   1 
ATOM   1797 C  CA  . GLU A 1 250 ? 22.667  152.564 29.028  1.00 28.71 ? 250  GLU A CA  1 
ATOM   1798 C  C   . GLU A 1 250 ? 21.508  152.206 28.092  1.00 28.05 ? 250  GLU A C   1 
ATOM   1799 O  O   . GLU A 1 250 ? 20.393  152.689 28.339  1.00 26.52 ? 250  GLU A O   1 
ATOM   1800 C  CB  . GLU A 1 250 ? 23.615  153.596 28.410  1.00 30.49 ? 250  GLU A CB  1 
ATOM   1801 C  CG  . GLU A 1 250 ? 22.963  154.945 28.149  1.00 32.65 ? 250  GLU A CG  1 
ATOM   1802 C  CD  . GLU A 1 250 ? 23.938  156.099 27.955  1.00 35.22 ? 250  GLU A CD  1 
ATOM   1803 O  OE1 . GLU A 1 250 ? 23.630  157.021 27.164  1.00 37.04 ? 250  GLU A OE1 1 
ATOM   1804 O  OE2 . GLU A 1 250 ? 25.003  156.071 28.590  1.00 34.91 ? 250  GLU A OE2 1 
ATOM   1805 N  N   . TYR A 1 251 ? 21.757  151.362 27.078  1.00 27.24 ? 251  TYR A N   1 
ATOM   1806 C  CA  . TYR A 1 251 ? 20.718  150.867 26.133  1.00 26.04 ? 251  TYR A CA  1 
ATOM   1807 C  C   . TYR A 1 251 ? 19.563  150.238 26.936  1.00 25.11 ? 251  TYR A C   1 
ATOM   1808 O  O   . TYR A 1 251 ? 18.388  150.653 26.766  1.00 23.84 ? 251  TYR A O   1 
ATOM   1809 C  CB  . TYR A 1 251 ? 21.319  149.892 25.110  1.00 27.31 ? 251  TYR A CB  1 
ATOM   1810 C  CG  . TYR A 1 251 ? 20.496  149.763 23.854  1.00 25.85 ? 251  TYR A CG  1 
ATOM   1811 C  CD1 . TYR A 1 251 ? 19.228  149.209 23.894  1.00 27.06 ? 251  TYR A CD1 1 
ATOM   1812 C  CD2 . TYR A 1 251 ? 20.959  150.232 22.634  1.00 25.41 ? 251  TYR A CD2 1 
ATOM   1813 C  CE1 . TYR A 1 251 ? 18.448  149.100 22.754  1.00 26.57 ? 251  TYR A CE1 1 
ATOM   1814 C  CE2 . TYR A 1 251 ? 20.197  150.125 21.481  1.00 24.28 ? 251  TYR A CE2 1 
ATOM   1815 C  CZ  . TYR A 1 251 ? 18.932  149.564 21.545  1.00 24.84 ? 251  TYR A CZ  1 
ATOM   1816 O  OH  . TYR A 1 251 ? 18.146  149.487 20.436  1.00 23.04 ? 251  TYR A OH  1 
ATOM   1817 N  N   . LEU A 1 252 ? 19.867  149.293 27.825  1.00 23.78 ? 252  LEU A N   1 
ATOM   1818 C  CA  . LEU A 1 252 ? 18.813  148.618 28.635  1.00 26.00 ? 252  LEU A CA  1 
ATOM   1819 C  C   . LEU A 1 252 ? 18.099  149.653 29.521  1.00 26.14 ? 252  LEU A C   1 
ATOM   1820 O  O   . LEU A 1 252 ? 16.854  149.640 29.562  1.00 24.91 ? 252  LEU A O   1 
ATOM   1821 C  CB  . LEU A 1 252 ? 19.427  147.492 29.473  1.00 25.36 ? 252  LEU A CB  1 
ATOM   1822 C  CG  . LEU A 1 252 ? 20.048  146.336 28.694  1.00 25.46 ? 252  LEU A CG  1 
ATOM   1823 C  CD1 . LEU A 1 252 ? 20.496  145.253 29.652  1.00 25.24 ? 252  LEU A CD1 1 
ATOM   1824 C  CD2 . LEU A 1 252 ? 19.086  145.774 27.649  1.00 26.06 ? 252  LEU A CD2 1 
ATOM   1825 N  N   . ARG A 1 253 ? 18.851  150.530 30.195  1.00 27.72 ? 253  ARG A N   1 
ATOM   1826 C  CA  . ARG A 1 253 ? 18.248  151.577 31.066  1.00 27.69 ? 253  ARG A CA  1 
ATOM   1827 C  C   . ARG A 1 253 ? 17.283  152.433 30.236  1.00 27.23 ? 253  ARG A C   1 
ATOM   1828 O  O   . ARG A 1 253 ? 16.180  152.664 30.728  1.00 27.88 ? 253  ARG A O   1 
ATOM   1829 C  CB  . ARG A 1 253 ? 19.326  152.386 31.789  1.00 28.90 ? 253  ARG A CB  1 
ATOM   1830 C  CG  . ARG A 1 253 ? 19.862  151.681 33.028  1.00 30.79 ? 253  ARG A CG  1 
ATOM   1831 C  CD  . ARG A 1 253 ? 20.601  152.635 33.947  1.00 32.12 ? 253  ARG A CD  1 
ATOM   1832 N  NE  . ARG A 1 253 ? 21.698  153.245 33.218  1.00 33.29 ? 253  ARG A NE  1 
ATOM   1833 C  CZ  . ARG A 1 253 ? 22.929  152.755 33.136  1.00 33.99 ? 253  ARG A CZ  1 
ATOM   1834 N  NH1 . ARG A 1 253 ? 23.267  151.656 33.787  1.00 34.29 ? 253  ARG A NH1 1 
ATOM   1835 N  NH2 . ARG A 1 253 ? 23.831  153.391 32.415  1.00 35.41 ? 253  ARG A NH2 1 
ATOM   1836 N  N   . ASN A 1 254 ? 17.646  152.825 29.009  1.00 27.60 ? 254  ASN A N   1 
ATOM   1837 C  CA  . ASN A 1 254 ? 16.741  153.596 28.112  1.00 28.19 ? 254  ASN A CA  1 
ATOM   1838 C  C   . ASN A 1 254 ? 15.471  152.777 27.820  1.00 28.48 ? 254  ASN A C   1 
ATOM   1839 O  O   . ASN A 1 254 ? 14.403  153.387 27.639  1.00 29.18 ? 254  ASN A O   1 
ATOM   1840 C  CB  . ASN A 1 254 ? 17.417  154.016 26.803  1.00 29.06 ? 254  ASN A CB  1 
ATOM   1841 C  CG  . ASN A 1 254 ? 18.572  154.977 26.993  1.00 29.42 ? 254  ASN A CG  1 
ATOM   1842 O  OD1 . ASN A 1 254 ? 18.704  155.602 28.050  1.00 30.40 ? 254  ASN A OD1 1 
ATOM   1843 N  ND2 . ASN A 1 254 ? 19.429  155.079 25.985  1.00 26.82 ? 254  ASN A ND2 1 
ATOM   1844 N  N   . MET A 1 255 ? 15.567  151.449 27.730  1.00 26.28 ? 255  MET A N   1 
ATOM   1845 C  CA  . MET A 1 255 ? 14.382  150.592 27.453  1.00 27.01 ? 255  MET A CA  1 
ATOM   1846 C  C   . MET A 1 255 ? 13.493  150.472 28.700  1.00 26.69 ? 255  MET A C   1 
ATOM   1847 O  O   . MET A 1 255 ? 12.278  150.258 28.522  1.00 26.09 ? 255  MET A O   1 
ATOM   1848 C  CB  . MET A 1 255 ? 14.806  149.194 27.000  1.00 26.87 ? 255  MET A CB  1 
ATOM   1849 C  CG  . MET A 1 255 ? 15.475  149.196 25.644  1.00 25.87 ? 255  MET A CG  1 
ATOM   1850 S  SD  . MET A 1 255 ? 16.094  147.564 25.235  1.00 26.93 ? 255  MET A SD  1 
ATOM   1851 C  CE  . MET A 1 255 ? 14.558  146.712 24.891  1.00 25.36 ? 255  MET A CE  1 
ATOM   1852 N  N   . GLY A 1 256 ? 14.074  150.606 29.899  1.00 25.72 ? 256  GLY A N   1 
ATOM   1853 C  CA  . GLY A 1 256 ? 13.423  150.285 31.183  1.00 25.47 ? 256  GLY A CA  1 
ATOM   1854 C  C   . GLY A 1 256 ? 13.772  148.876 31.631  1.00 25.60 ? 256  GLY A C   1 
ATOM   1855 O  O   . GLY A 1 256 ? 13.259  148.422 32.671  1.00 27.00 ? 256  GLY A O   1 
ATOM   1856 N  N   . VAL A 1 257 ? 14.619  148.186 30.869  1.00 25.60 ? 257  VAL A N   1 
ATOM   1857 C  CA  . VAL A 1 257 ? 15.080  146.812 31.215  1.00 25.63 ? 257  VAL A CA  1 
ATOM   1858 C  C   . VAL A 1 257 ? 16.136  146.950 32.314  1.00 26.22 ? 257  VAL A C   1 
ATOM   1859 O  O   . VAL A 1 257 ? 16.987  147.838 32.203  1.00 25.91 ? 257  VAL A O   1 
ATOM   1860 C  CB  . VAL A 1 257 ? 15.617  146.072 29.977  1.00 26.00 ? 257  VAL A CB  1 
ATOM   1861 C  CG1 . VAL A 1 257 ? 16.221  144.725 30.347  1.00 25.51 ? 257  VAL A CG1 1 
ATOM   1862 C  CG2 . VAL A 1 257 ? 14.527  145.905 28.917  1.00 26.11 ? 257  VAL A CG2 1 
ATOM   1863 N  N   . ALA A 1 258 ? 16.067  146.104 33.344  1.00 27.53 ? 258  ALA A N   1 
ATOM   1864 C  CA  . ALA A 1 258 ? 16.992  146.120 34.500  1.00 26.19 ? 258  ALA A CA  1 
ATOM   1865 C  C   . ALA A 1 258 ? 17.815  144.830 34.559  1.00 26.10 ? 258  ALA A C   1 
ATOM   1866 O  O   . ALA A 1 258 ? 18.837  144.823 35.260  1.00 27.60 ? 258  ALA A O   1 
ATOM   1867 C  CB  . ALA A 1 258 ? 16.196  146.332 35.765  1.00 28.02 ? 258  ALA A CB  1 
ATOM   1868 N  N   . ALA A 1 259 ? 17.401  143.770 33.863  1.00 24.48 ? 259  ALA A N   1 
ATOM   1869 C  CA  . ALA A 1 259 ? 18.093  142.463 33.905  1.00 23.72 ? 259  ALA A CA  1 
ATOM   1870 C  C   . ALA A 1 259 ? 17.799  141.666 32.639  1.00 23.43 ? 259  ALA A C   1 
ATOM   1871 O  O   . ALA A 1 259 ? 16.785  141.922 31.966  1.00 22.47 ? 259  ALA A O   1 
ATOM   1872 C  CB  . ALA A 1 259 ? 17.694  141.693 35.139  1.00 24.74 ? 259  ALA A CB  1 
ATOM   1873 N  N   . SER A 1 260 ? 18.671  140.713 32.334  1.00 23.54 ? 260  SER A N   1 
ATOM   1874 C  CA  . SER A 1 260 ? 18.519  139.873 31.125  1.00 23.02 ? 260  SER A CA  1 
ATOM   1875 C  C   . SER A 1 260 ? 19.209  138.530 31.318  1.00 22.59 ? 260  SER A C   1 
ATOM   1876 O  O   . SER A 1 260 ? 20.125  138.422 32.170  1.00 21.07 ? 260  SER A O   1 
ATOM   1877 C  CB  . SER A 1 260 ? 19.013  140.592 29.887  1.00 22.90 ? 260  SER A CB  1 
ATOM   1878 O  OG  . SER A 1 260 ? 20.430  140.728 29.882  1.00 23.46 ? 260  SER A OG  1 
ATOM   1879 N  N   . MET A 1 261 ? 18.751  137.551 30.545  1.00 23.08 ? 261  MET A N   1 
ATOM   1880 C  CA  . MET A 1 261 ? 19.480  136.291 30.281  1.00 24.00 ? 261  MET A CA  1 
ATOM   1881 C  C   . MET A 1 261 ? 19.216  135.890 28.835  1.00 23.73 ? 261  MET A C   1 
ATOM   1882 O  O   . MET A 1 261 ? 18.032  135.763 28.461  1.00 24.82 ? 261  MET A O   1 
ATOM   1883 C  CB  . MET A 1 261 ? 19.048  135.146 31.202  1.00 25.03 ? 261  MET A CB  1 
ATOM   1884 C  CG  . MET A 1 261 ? 19.980  133.957 31.082  1.00 26.99 ? 261  MET A CG  1 
ATOM   1885 S  SD  . MET A 1 261 ? 19.632  132.638 32.245  1.00 28.96 ? 261  MET A SD  1 
ATOM   1886 C  CE  . MET A 1 261 ? 18.168  131.956 31.469  1.00 28.49 ? 261  MET A CE  1 
ATOM   1887 N  N   . SER A 1 262 ? 20.277  135.665 28.064  1.00 23.08 ? 262  SER A N   1 
ATOM   1888 C  CA  . SER A 1 262 ? 20.161  135.131 26.687  1.00 24.75 ? 262  SER A CA  1 
ATOM   1889 C  C   . SER A 1 262 ? 20.591  133.663 26.686  1.00 24.17 ? 262  SER A C   1 
ATOM   1890 O  O   . SER A 1 262 ? 21.515  133.298 27.430  1.00 24.97 ? 262  SER A O   1 
ATOM   1891 C  CB  . SER A 1 262 ? 20.927  135.957 25.681  1.00 25.46 ? 262  SER A CB  1 
ATOM   1892 O  OG  . SER A 1 262 ? 22.294  136.034 26.035  1.00 27.63 ? 262  SER A OG  1 
ATOM   1893 N  N   . ILE A 1 263 ? 19.890  132.852 25.903  1.00 23.85 ? 263  ILE A N   1 
ATOM   1894 C  CA  . ILE A 1 263 ? 20.290  131.463 25.547  1.00 23.59 ? 263  ILE A CA  1 
ATOM   1895 C  C   . ILE A 1 263 ? 20.689  131.502 24.075  1.00 23.44 ? 263  ILE A C   1 
ATOM   1896 O  O   . ILE A 1 263 ? 19.839  131.859 23.229  1.00 22.77 ? 263  ILE A O   1 
ATOM   1897 C  CB  . ILE A 1 263 ? 19.157  130.461 25.829  1.00 24.15 ? 263  ILE A CB  1 
ATOM   1898 C  CG1 . ILE A 1 263 ? 18.581  130.652 27.234  1.00 24.31 ? 263  ILE A CG1 1 
ATOM   1899 C  CG2 . ILE A 1 263 ? 19.638  129.042 25.595  1.00 24.20 ? 263  ILE A CG2 1 
ATOM   1900 C  CD1 . ILE A 1 263 ? 17.247  129.998 27.449  1.00 25.30 ? 263  ILE A CD1 1 
ATOM   1901 N  N   . SER A 1 264 ? 21.951  131.186 23.796  1.00 23.42 ? 264  SER A N   1 
ATOM   1902 C  CA  . SER A 1 264 ? 22.502  131.165 22.417  1.00 23.64 ? 264  SER A CA  1 
ATOM   1903 C  C   . SER A 1 264 ? 21.874  130.009 21.630  1.00 25.14 ? 264  SER A C   1 
ATOM   1904 O  O   . SER A 1 264 ? 21.775  128.894 22.183  1.00 25.81 ? 264  SER A O   1 
ATOM   1905 C  CB  . SER A 1 264 ? 23.997  131.103 22.442  1.00 23.06 ? 264  SER A CB  1 
ATOM   1906 O  OG  . SER A 1 264 ? 24.514  132.314 22.973  1.00 23.69 ? 264  SER A OG  1 
ATOM   1907 N  N   . VAL A 1 265 ? 21.428  130.273 20.400  1.00 24.69 ? 265  VAL A N   1 
ATOM   1908 C  CA  . VAL A 1 265 ? 20.934  129.216 19.473  1.00 26.20 ? 265  VAL A CA  1 
ATOM   1909 C  C   . VAL A 1 265 ? 22.040  128.967 18.452  1.00 26.75 ? 265  VAL A C   1 
ATOM   1910 O  O   . VAL A 1 265 ? 22.388  129.910 17.717  1.00 25.54 ? 265  VAL A O   1 
ATOM   1911 C  CB  . VAL A 1 265 ? 19.602  129.601 18.808  1.00 27.09 ? 265  VAL A CB  1 
ATOM   1912 C  CG1 . VAL A 1 265 ? 19.072  128.471 17.935  1.00 27.72 ? 265  VAL A CG1 1 
ATOM   1913 C  CG2 . VAL A 1 265 ? 18.566  130.016 19.842  1.00 26.37 ? 265  VAL A CG2 1 
ATOM   1914 N  N   . ILE A 1 266 ? 22.601  127.761 18.480  1.00 30.30 ? 266  ILE A N   1 
ATOM   1915 C  CA  . ILE A 1 266 ? 23.742  127.317 17.630  1.00 33.54 ? 266  ILE A CA  1 
ATOM   1916 C  C   . ILE A 1 266 ? 23.195  126.323 16.601  1.00 35.13 ? 266  ILE A C   1 
ATOM   1917 O  O   . ILE A 1 266 ? 22.626  125.309 17.017  1.00 32.52 ? 266  ILE A O   1 
ATOM   1918 C  CB  . ILE A 1 266 ? 24.861  126.704 18.496  1.00 35.37 ? 266  ILE A CB  1 
ATOM   1919 C  CG1 . ILE A 1 266 ? 25.213  127.599 19.686  1.00 35.36 ? 266  ILE A CG1 1 
ATOM   1920 C  CG2 . ILE A 1 266 ? 26.091  126.369 17.658  1.00 36.08 ? 266  ILE A CG2 1 
ATOM   1921 C  CD1 . ILE A 1 266 ? 25.675  128.986 19.299  1.00 37.06 ? 266  ILE A CD1 1 
ATOM   1922 N  N   . VAL A 1 267 ? 23.298  126.664 15.315  1.00 36.68 ? 267  VAL A N   1 
ATOM   1923 C  CA  . VAL A 1 267 ? 22.915  125.799 14.158  1.00 38.34 ? 267  VAL A CA  1 
ATOM   1924 C  C   . VAL A 1 267 ? 24.148  125.677 13.250  1.00 41.62 ? 267  VAL A C   1 
ATOM   1925 O  O   . VAL A 1 267 ? 24.804  126.707 12.998  1.00 38.04 ? 267  VAL A O   1 
ATOM   1926 C  CB  . VAL A 1 267 ? 21.692  126.366 13.412  1.00 38.27 ? 267  VAL A CB  1 
ATOM   1927 C  CG1 . VAL A 1 267 ? 21.445  125.664 12.082  1.00 40.44 ? 267  VAL A CG1 1 
ATOM   1928 C  CG2 . VAL A 1 267 ? 20.436  126.316 14.267  1.00 36.68 ? 267  VAL A CG2 1 
ATOM   1929 N  N   . ASP A 1 268 ? 24.480  124.460 12.813  1.00 45.11 ? 268  ASP A N   1 
ATOM   1930 C  CA  . ASP A 1 268 ? 25.645  124.200 11.921  1.00 46.58 ? 268  ASP A CA  1 
ATOM   1931 C  C   . ASP A 1 268 ? 26.890  124.886 12.506  1.00 42.84 ? 268  ASP A C   1 
ATOM   1932 O  O   . ASP A 1 268 ? 27.654  125.483 11.723  1.00 45.65 ? 268  ASP A O   1 
ATOM   1933 C  CB  . ASP A 1 268 ? 25.356  124.687 10.492  1.00 50.58 ? 268  ASP A CB  1 
ATOM   1934 C  CG  . ASP A 1 268 ? 24.146  124.046 9.820   1.00 53.04 ? 268  ASP A CG  1 
ATOM   1935 O  OD1 . ASP A 1 268 ? 23.935  122.827 10.011  1.00 54.99 ? 268  ASP A OD1 1 
ATOM   1936 O  OD2 . ASP A 1 268 ? 23.423  124.769 9.102   1.00 52.21 ? 268  ASP A OD2 1 
ATOM   1937 N  N   . GLY A 1 269 ? 27.059  124.843 13.833  1.00 40.68 ? 269  GLY A N   1 
ATOM   1938 C  CA  . GLY A 1 269 ? 28.227  125.390 14.565  1.00 37.21 ? 269  GLY A CA  1 
ATOM   1939 C  C   . GLY A 1 269 ? 28.319  126.915 14.544  1.00 38.48 ? 269  GLY A C   1 
ATOM   1940 O  O   . GLY A 1 269 ? 29.380  127.444 14.925  1.00 40.57 ? 269  GLY A O   1 
ATOM   1941 N  N   . ALA A 1 270 ? 27.260  127.618 14.129  1.00 35.35 ? 270  ALA A N   1 
ATOM   1942 C  CA  . ALA A 1 270 ? 27.235  129.095 13.984  1.00 32.09 ? 270  ALA A CA  1 
ATOM   1943 C  C   . ALA A 1 270 ? 26.113  129.684 14.851  1.00 28.77 ? 270  ALA A C   1 
ATOM   1944 O  O   . ALA A 1 270 ? 25.220  128.934 15.276  1.00 25.56 ? 270  ALA A O   1 
ATOM   1945 C  CB  . ALA A 1 270 ? 27.074  129.464 12.531  1.00 30.92 ? 270  ALA A CB  1 
ATOM   1946 N  N   . LEU A 1 271 ? 26.184  130.984 15.131  1.00 27.33 ? 271  LEU A N   1 
ATOM   1947 C  CA  . LEU A 1 271 ? 25.193  131.682 15.991  1.00 26.30 ? 271  LEU A CA  1 
ATOM   1948 C  C   . LEU A 1 271 ? 23.956  131.999 15.144  1.00 24.97 ? 271  LEU A C   1 
ATOM   1949 O  O   . LEU A 1 271 ? 23.989  132.972 14.386  1.00 23.87 ? 271  LEU A O   1 
ATOM   1950 C  CB  . LEU A 1 271 ? 25.828  132.944 16.580  1.00 25.96 ? 271  LEU A CB  1 
ATOM   1951 C  CG  . LEU A 1 271 ? 24.964  133.693 17.593  1.00 26.77 ? 271  LEU A CG  1 
ATOM   1952 C  CD1 . LEU A 1 271 ? 24.699  132.833 18.817  1.00 26.04 ? 271  LEU A CD1 1 
ATOM   1953 C  CD2 . LEU A 1 271 ? 25.616  135.010 17.996  1.00 27.04 ? 271  LEU A CD2 1 
ATOM   1954 N  N   . TRP A 1 272 ? 22.920  131.168 15.245  1.00 24.73 ? 272  TRP A N   1 
ATOM   1955 C  CA  . TRP A 1 272 ? 21.647  131.330 14.491  1.00 24.32 ? 272  TRP A CA  1 
ATOM   1956 C  C   . TRP A 1 272 ? 20.883  132.544 15.036  1.00 23.08 ? 272  TRP A C   1 
ATOM   1957 O  O   . TRP A 1 272 ? 20.244  133.261 14.244  1.00 23.68 ? 272  TRP A O   1 
ATOM   1958 C  CB  . TRP A 1 272 ? 20.822  130.043 14.583  1.00 24.30 ? 272  TRP A CB  1 
ATOM   1959 C  CG  . TRP A 1 272 ? 19.495  130.083 13.888  1.00 24.73 ? 272  TRP A CG  1 
ATOM   1960 C  CD1 . TRP A 1 272 ? 19.223  129.650 12.621  1.00 26.36 ? 272  TRP A CD1 1 
ATOM   1961 C  CD2 . TRP A 1 272 ? 18.240  130.536 14.430  1.00 24.65 ? 272  TRP A CD2 1 
ATOM   1962 N  NE1 . TRP A 1 272 ? 17.893  129.812 12.334  1.00 25.52 ? 272  TRP A NE1 1 
ATOM   1963 C  CE2 . TRP A 1 272 ? 17.263  130.349 13.426  1.00 26.29 ? 272  TRP A CE2 1 
ATOM   1964 C  CE3 . TRP A 1 272 ? 17.844  131.075 15.658  1.00 26.44 ? 272  TRP A CE3 1 
ATOM   1965 C  CZ2 . TRP A 1 272 ? 15.924  130.699 13.611  1.00 27.71 ? 272  TRP A CZ2 1 
ATOM   1966 C  CZ3 . TRP A 1 272 ? 16.518  131.408 15.846  1.00 27.95 ? 272  TRP A CZ3 1 
ATOM   1967 C  CH2 . TRP A 1 272 ? 15.571  131.221 14.836  1.00 27.79 ? 272  TRP A CH2 1 
ATOM   1968 N  N   . GLY A 1 273 ? 20.939  132.742 16.352  1.00 22.21 ? 273  GLY A N   1 
ATOM   1969 C  CA  . GLY A 1 273 ? 20.174  133.785 17.053  1.00 21.55 ? 273  GLY A CA  1 
ATOM   1970 C  C   . GLY A 1 273 ? 20.269  133.637 18.552  1.00 20.99 ? 273  GLY A C   1 
ATOM   1971 O  O   . GLY A 1 273 ? 21.160  132.916 19.022  1.00 20.92 ? 273  GLY A O   1 
ATOM   1972 N  N   . LEU A 1 274 ? 19.359  134.296 19.270  1.00 21.18 ? 274  LEU A N   1 
ATOM   1973 C  CA  . LEU A 1 274 ? 19.301  134.278 20.746  1.00 21.61 ? 274  LEU A CA  1 
ATOM   1974 C  C   . LEU A 1 274 ? 17.859  134.074 21.185  1.00 21.71 ? 274  LEU A C   1 
ATOM   1975 O  O   . LEU A 1 274 ? 16.949  134.576 20.495  1.00 21.34 ? 274  LEU A O   1 
ATOM   1976 C  CB  . LEU A 1 274 ? 19.806  135.615 21.290  1.00 21.83 ? 274  LEU A CB  1 
ATOM   1977 C  CG  . LEU A 1 274 ? 21.252  135.978 20.977  1.00 22.30 ? 274  LEU A CG  1 
ATOM   1978 C  CD1 . LEU A 1 274 ? 21.546  137.380 21.499  1.00 22.62 ? 274  LEU A CD1 1 
ATOM   1979 C  CD2 . LEU A 1 274 ? 22.224  134.974 21.587  1.00 22.05 ? 274  LEU A CD2 1 
ATOM   1980 N  N   . ILE A 1 275 ? 17.674  133.366 22.294  1.00 21.79 ? 275  ILE A N   1 
ATOM   1981 C  CA  . ILE A 1 275 ? 16.452  133.501 23.132  1.00 22.36 ? 275  ILE A CA  1 
ATOM   1982 C  C   . ILE A 1 275 ? 16.800  134.562 24.174  1.00 21.96 ? 275  ILE A C   1 
ATOM   1983 O  O   . ILE A 1 275 ? 17.642  134.276 25.024  1.00 22.83 ? 275  ILE A O   1 
ATOM   1984 C  CB  . ILE A 1 275 ? 16.023  132.166 23.766  1.00 22.41 ? 275  ILE A CB  1 
ATOM   1985 C  CG1 . ILE A 1 275 ? 15.866  131.064 22.719  1.00 22.16 ? 275  ILE A CG1 1 
ATOM   1986 C  CG2 . ILE A 1 275 ? 14.760  132.360 24.595  1.00 23.46 ? 275  ILE A CG2 1 
ATOM   1987 C  CD1 . ILE A 1 275 ? 15.829  129.674 23.293  1.00 22.22 ? 275  ILE A CD1 1 
ATOM   1988 N  N   . ALA A 1 276 ? 16.236  135.760 24.037  1.00 22.19 ? 276  ALA A N   1 
ATOM   1989 C  CA  . ALA A 1 276 ? 16.562  136.930 24.879  1.00 22.51 ? 276  ALA A CA  1 
ATOM   1990 C  C   . ALA A 1 276 ? 15.455  137.109 25.922  1.00 22.50 ? 276  ALA A C   1 
ATOM   1991 O  O   . ALA A 1 276 ? 14.292  137.333 25.515  1.00 22.53 ? 276  ALA A O   1 
ATOM   1992 C  CB  . ALA A 1 276 ? 16.734  138.149 24.017  1.00 23.05 ? 276  ALA A CB  1 
ATOM   1993 N  N   . CYS A 1 277 ? 15.809  136.962 27.202  1.00 22.20 ? 277  CYS A N   1 
ATOM   1994 C  CA  . CYS A 1 277 ? 14.880  137.154 28.352  1.00 22.95 ? 277  CYS A CA  1 
ATOM   1995 C  C   . CYS A 1 277 ? 15.184  138.513 28.995  1.00 22.21 ? 277  CYS A C   1 
ATOM   1996 O  O   . CYS A 1 277 ? 16.335  138.724 29.421  1.00 21.74 ? 277  CYS A O   1 
ATOM   1997 C  CB  . CYS A 1 277 ? 15.005  136.029 29.371  1.00 23.75 ? 277  CYS A CB  1 
ATOM   1998 S  SG  . CYS A 1 277 ? 14.890  134.372 28.643  1.00 25.14 ? 277  CYS A SG  1 
ATOM   1999 N  N   . HIS A 1 278 ? 14.199  139.409 29.008  1.00 21.51 ? 278  HIS A N   1 
ATOM   2000 C  CA  . HIS A 1 278 ? 14.294  140.779 29.577  1.00 22.43 ? 278  HIS A CA  1 
ATOM   2001 C  C   . HIS A 1 278 ? 13.341  140.918 30.767  1.00 23.37 ? 278  HIS A C   1 
ATOM   2002 O  O   . HIS A 1 278 ? 12.165  140.507 30.653  1.00 24.06 ? 278  HIS A O   1 
ATOM   2003 C  CB  . HIS A 1 278 ? 13.966  141.832 28.520  1.00 21.66 ? 278  HIS A CB  1 
ATOM   2004 C  CG  . HIS A 1 278 ? 14.994  141.990 27.456  1.00 21.42 ? 278  HIS A CG  1 
ATOM   2005 N  ND1 . HIS A 1 278 ? 14.819  142.868 26.415  1.00 21.37 ? 278  HIS A ND1 1 
ATOM   2006 C  CD2 . HIS A 1 278 ? 16.196  141.402 27.268  1.00 21.00 ? 278  HIS A CD2 1 
ATOM   2007 C  CE1 . HIS A 1 278 ? 15.888  142.833 25.638  1.00 22.45 ? 278  HIS A CE1 1 
ATOM   2008 N  NE2 . HIS A 1 278 ? 16.743  141.943 26.141  1.00 21.27 ? 278  HIS A NE2 1 
ATOM   2009 N  N   . HIS A 1 279 ? 13.838  141.492 31.859  1.00 23.67 ? 279  HIS A N   1 
ATOM   2010 C  CA  . HIS A 1 279 ? 13.054  141.815 33.073  1.00 24.26 ? 279  HIS A CA  1 
ATOM   2011 C  C   . HIS A 1 279 ? 13.159  143.318 33.307  1.00 24.41 ? 279  HIS A C   1 
ATOM   2012 O  O   . HIS A 1 279 ? 14.254  143.866 33.080  1.00 26.13 ? 279  HIS A O   1 
ATOM   2013 C  CB  . HIS A 1 279 ? 13.535  140.995 34.275  1.00 24.84 ? 279  HIS A CB  1 
ATOM   2014 C  CG  . HIS A 1 279 ? 12.430  140.574 35.182  1.00 26.22 ? 279  HIS A CG  1 
ATOM   2015 N  ND1 . HIS A 1 279 ? 11.317  139.898 34.712  1.00 26.75 ? 279  HIS A ND1 1 
ATOM   2016 C  CD2 . HIS A 1 279 ? 12.263  140.702 36.516  1.00 26.31 ? 279  HIS A CD2 1 
ATOM   2017 C  CE1 . HIS A 1 279 ? 10.511  139.626 35.721  1.00 27.30 ? 279  HIS A CE1 1 
ATOM   2018 N  NE2 . HIS A 1 279 ? 11.070  140.112 36.842  1.00 26.87 ? 279  HIS A NE2 1 
ATOM   2019 N  N   . TYR A 1 280 ? 12.061  143.936 33.744  1.00 25.44 ? 280  TYR A N   1 
ATOM   2020 C  CA  . TYR A 1 280 ? 11.940  145.397 33.994  1.00 25.92 ? 280  TYR A CA  1 
ATOM   2021 C  C   . TYR A 1 280 ? 12.204  145.692 35.478  1.00 26.04 ? 280  TYR A C   1 
ATOM   2022 O  O   . TYR A 1 280 ? 11.961  146.821 35.921  1.00 27.52 ? 280  TYR A O   1 
ATOM   2023 C  CB  . TYR A 1 280 ? 10.612  145.907 33.437  1.00 25.59 ? 280  TYR A CB  1 
ATOM   2024 C  CG  . TYR A 1 280 ? 10.647  146.027 31.934  1.00 26.72 ? 280  TYR A CG  1 
ATOM   2025 C  CD1 . TYR A 1 280 ? 10.665  144.899 31.132  1.00 26.02 ? 280  TYR A CD1 1 
ATOM   2026 C  CD2 . TYR A 1 280 ? 10.736  147.265 31.312  1.00 25.94 ? 280  TYR A CD2 1 
ATOM   2027 C  CE1 . TYR A 1 280 ? 10.728  144.996 29.751  1.00 26.94 ? 280  TYR A CE1 1 
ATOM   2028 C  CE2 . TYR A 1 280 ? 10.809  147.379 29.934  1.00 25.88 ? 280  TYR A CE2 1 
ATOM   2029 C  CZ  . TYR A 1 280 ? 10.800  146.238 29.149  1.00 26.17 ? 280  TYR A CZ  1 
ATOM   2030 O  OH  . TYR A 1 280 ? 10.872  146.337 27.794  1.00 26.24 ? 280  TYR A OH  1 
ATOM   2031 N  N   . SER A 1 281 ? 12.762  144.714 36.192  1.00 26.22 ? 281  SER A N   1 
ATOM   2032 C  CA  . SER A 1 281 ? 13.391  144.868 37.530  1.00 26.33 ? 281  SER A CA  1 
ATOM   2033 C  C   . SER A 1 281 ? 14.552  143.884 37.626  1.00 26.95 ? 281  SER A C   1 
ATOM   2034 O  O   . SER A 1 281 ? 14.639  142.969 36.811  1.00 28.37 ? 281  SER A O   1 
ATOM   2035 C  CB  . SER A 1 281 ? 12.371  144.686 38.645  1.00 26.85 ? 281  SER A CB  1 
ATOM   2036 O  OG  . SER A 1 281 ? 11.593  143.520 38.434  1.00 28.33 ? 281  SER A OG  1 
ATOM   2037 N  N   . PRO A 1 282 ? 15.499  144.038 38.584  1.00 26.86 ? 282  PRO A N   1 
ATOM   2038 C  CA  . PRO A 1 282 ? 16.629  143.119 38.696  1.00 26.14 ? 282  PRO A CA  1 
ATOM   2039 C  C   . PRO A 1 282 ? 16.166  141.660 38.804  1.00 26.51 ? 282  PRO A C   1 
ATOM   2040 O  O   . PRO A 1 282 ? 15.133  141.409 39.390  1.00 26.88 ? 282  PRO A O   1 
ATOM   2041 C  CB  . PRO A 1 282 ? 17.330  143.566 39.991  1.00 26.66 ? 282  PRO A CB  1 
ATOM   2042 C  CG  . PRO A 1 282 ? 16.967  145.025 40.106  1.00 26.08 ? 282  PRO A CG  1 
ATOM   2043 C  CD  . PRO A 1 282 ? 15.536  145.089 39.616  1.00 26.78 ? 282  PRO A CD  1 
ATOM   2044 N  N   . ARG A 1 283 ? 16.935  140.733 38.241  1.00 27.33 ? 283  ARG A N   1 
ATOM   2045 C  CA  . ARG A 1 283 ? 16.576  139.289 38.230  1.00 27.70 ? 283  ARG A CA  1 
ATOM   2046 C  C   . ARG A 1 283 ? 17.805  138.459 37.879  1.00 27.46 ? 283  ARG A C   1 
ATOM   2047 O  O   . ARG A 1 283 ? 18.478  138.773 36.886  1.00 29.43 ? 283  ARG A O   1 
ATOM   2048 C  CB  . ARG A 1 283 ? 15.453  139.010 37.228  1.00 27.68 ? 283  ARG A CB  1 
ATOM   2049 C  CG  . ARG A 1 283 ? 14.950  137.575 37.254  1.00 27.55 ? 283  ARG A CG  1 
ATOM   2050 C  CD  . ARG A 1 283 ? 13.657  137.436 36.481  1.00 27.92 ? 283  ARG A CD  1 
ATOM   2051 N  NE  . ARG A 1 283 ? 13.077  136.115 36.656  1.00 28.41 ? 283  ARG A NE  1 
ATOM   2052 C  CZ  . ARG A 1 283 ? 12.486  135.704 37.773  1.00 28.90 ? 283  ARG A CZ  1 
ATOM   2053 N  NH1 . ARG A 1 283 ? 12.409  136.505 38.825  1.00 28.36 ? 283  ARG A NH1 1 
ATOM   2054 N  NH2 . ARG A 1 283 ? 11.997  134.482 37.843  1.00 28.38 ? 283  ARG A NH2 1 
ATOM   2055 N  N   . VAL A 1 284 ? 18.080  137.432 38.670  1.00 27.42 ? 284  VAL A N   1 
ATOM   2056 C  CA  . VAL A 1 284 ? 19.083  136.394 38.305  1.00 28.70 ? 284  VAL A CA  1 
ATOM   2057 C  C   . VAL A 1 284 ? 18.522  135.042 38.747  1.00 27.85 ? 284  VAL A C   1 
ATOM   2058 O  O   . VAL A 1 284 ? 18.069  134.932 39.890  1.00 25.14 ? 284  VAL A O   1 
ATOM   2059 C  CB  . VAL A 1 284 ? 20.476  136.698 38.895  1.00 28.56 ? 284  VAL A CB  1 
ATOM   2060 C  CG1 . VAL A 1 284 ? 20.450  136.872 40.403  1.00 29.23 ? 284  VAL A CG1 1 
ATOM   2061 C  CG2 . VAL A 1 284 ? 21.495  135.650 38.481  1.00 28.59 ? 284  VAL A CG2 1 
ATOM   2062 N  N   . LEU A 1 285 ? 18.513  134.076 37.835  1.00 29.25 ? 285  LEU A N   1 
ATOM   2063 C  CA  . LEU A 1 285 ? 18.067  132.688 38.107  1.00 28.65 ? 285  LEU A CA  1 
ATOM   2064 C  C   . LEU A 1 285 ? 19.166  131.973 38.891  1.00 29.54 ? 285  LEU A C   1 
ATOM   2065 O  O   . LEU A 1 285 ? 20.356  132.217 38.616  1.00 28.93 ? 285  LEU A O   1 
ATOM   2066 C  CB  . LEU A 1 285 ? 17.771  131.983 36.781  1.00 28.89 ? 285  LEU A CB  1 
ATOM   2067 C  CG  . LEU A 1 285 ? 16.660  132.606 35.934  1.00 29.61 ? 285  LEU A CG  1 
ATOM   2068 C  CD1 . LEU A 1 285 ? 16.478  131.843 34.629  1.00 28.90 ? 285  LEU A CD1 1 
ATOM   2069 C  CD2 . LEU A 1 285 ? 15.350  132.657 36.695  1.00 29.72 ? 285  LEU A CD2 1 
ATOM   2070 N  N   . SER A 1 286 ? 18.769  131.110 39.823  1.00 29.85 ? 286  SER A N   1 
ATOM   2071 C  CA  . SER A 1 286 ? 19.705  130.240 40.582  1.00 32.17 ? 286  SER A CA  1 
ATOM   2072 C  C   . SER A 1 286 ? 20.454  129.336 39.599  1.00 32.73 ? 286  SER A C   1 
ATOM   2073 O  O   . SER A 1 286 ? 19.912  129.061 38.499  1.00 32.37 ? 286  SER A O   1 
ATOM   2074 C  CB  . SER A 1 286 ? 18.967  129.445 41.624  1.00 34.43 ? 286  SER A CB  1 
ATOM   2075 O  OG  . SER A 1 286 ? 18.099  128.505 41.012  1.00 35.10 ? 286  SER A OG  1 
ATOM   2076 N  N   . MET A 1 287 ? 21.651  128.883 39.977  1.00 31.63 ? 287  MET A N   1 
ATOM   2077 C  CA  . MET A 1 287 ? 22.483  127.995 39.130  1.00 32.57 ? 287  MET A CA  1 
ATOM   2078 C  C   . MET A 1 287 ? 21.683  126.779 38.655  1.00 30.26 ? 287  MET A C   1 
ATOM   2079 O  O   . MET A 1 287 ? 21.763  126.424 37.486  1.00 28.59 ? 287  MET A O   1 
ATOM   2080 C  CB  . MET A 1 287 ? 23.733  127.518 39.865  1.00 34.09 ? 287  MET A CB  1 
ATOM   2081 C  CG  . MET A 1 287 ? 24.604  126.659 38.987  1.00 35.95 ? 287  MET A CG  1 
ATOM   2082 S  SD  . MET A 1 287 ? 26.233  126.393 39.692  1.00 38.64 ? 287  MET A SD  1 
ATOM   2083 C  CE  . MET A 1 287 ? 26.893  128.058 39.577  1.00 38.55 ? 287  MET A CE  1 
ATOM   2084 N  N   . PRO A 1 288 ? 20.940  126.055 39.522  1.00 29.46 ? 288  PRO A N   1 
ATOM   2085 C  CA  . PRO A 1 288 ? 20.198  124.876 39.067  1.00 30.72 ? 288  PRO A CA  1 
ATOM   2086 C  C   . PRO A 1 288 ? 19.227  125.174 37.913  1.00 29.93 ? 288  PRO A C   1 
ATOM   2087 O  O   . PRO A 1 288 ? 19.101  124.357 37.016  1.00 28.01 ? 288  PRO A O   1 
ATOM   2088 C  CB  . PRO A 1 288 ? 19.434  124.423 40.322  1.00 30.72 ? 288  PRO A CB  1 
ATOM   2089 C  CG  . PRO A 1 288 ? 20.294  124.932 41.462  1.00 30.65 ? 288  PRO A CG  1 
ATOM   2090 C  CD  . PRO A 1 288 ? 20.812  126.270 40.973  1.00 29.93 ? 288  PRO A CD  1 
ATOM   2091 N  N   . VAL A 1 289 ? 18.584  126.342 37.952  1.00 29.70 ? 289  VAL A N   1 
ATOM   2092 C  CA  . VAL A 1 289 ? 17.590  126.763 36.923  1.00 28.87 ? 289  VAL A CA  1 
ATOM   2093 C  C   . VAL A 1 289 ? 18.343  127.138 35.637  1.00 28.17 ? 289  VAL A C   1 
ATOM   2094 O  O   . VAL A 1 289 ? 17.867  126.765 34.550  1.00 26.99 ? 289  VAL A O   1 
ATOM   2095 C  CB  . VAL A 1 289 ? 16.680  127.884 37.451  1.00 28.80 ? 289  VAL A CB  1 
ATOM   2096 C  CG1 . VAL A 1 289 ? 15.670  128.328 36.407  1.00 28.65 ? 289  VAL A CG1 1 
ATOM   2097 C  CG2 . VAL A 1 289 ? 15.974  127.454 38.733  1.00 28.39 ? 289  VAL A CG2 1 
ATOM   2098 N  N   . ARG A 1 290 ? 19.512  127.771 35.764  1.00 27.57 ? 290  ARG A N   1 
ATOM   2099 C  CA  . ARG A 1 290 ? 20.372  128.154 34.609  1.00 27.51 ? 290  ARG A CA  1 
ATOM   2100 C  C   . ARG A 1 290 ? 20.871  126.893 33.897  1.00 27.21 ? 290  ARG A C   1 
ATOM   2101 O  O   . ARG A 1 290 ? 20.945  126.894 32.649  1.00 27.83 ? 290  ARG A O   1 
ATOM   2102 C  CB  . ARG A 1 290 ? 21.528  129.045 35.071  1.00 27.26 ? 290  ARG A CB  1 
ATOM   2103 C  CG  . ARG A 1 290 ? 21.075  130.384 35.630  1.00 27.11 ? 290  ARG A CG  1 
ATOM   2104 C  CD  . ARG A 1 290 ? 22.156  131.452 35.623  1.00 27.82 ? 290  ARG A CD  1 
ATOM   2105 N  NE  . ARG A 1 290 ? 23.457  130.990 36.110  1.00 27.65 ? 290  ARG A NE  1 
ATOM   2106 C  CZ  . ARG A 1 290 ? 23.917  131.137 37.354  1.00 28.39 ? 290  ARG A CZ  1 
ATOM   2107 N  NH1 . ARG A 1 290 ? 23.182  131.725 38.287  1.00 28.14 ? 290  ARG A NH1 1 
ATOM   2108 N  NH2 . ARG A 1 290 ? 25.121  130.688 37.662  1.00 28.52 ? 290  ARG A NH2 1 
ATOM   2109 N  N   . ILE A 1 291 ? 21.195  125.849 34.657  1.00 27.52 ? 291  ILE A N   1 
ATOM   2110 C  CA  . ILE A 1 291 ? 21.628  124.538 34.096  1.00 28.39 ? 291  ILE A CA  1 
ATOM   2111 C  C   . ILE A 1 291 ? 20.467  123.976 33.259  1.00 29.29 ? 291  ILE A C   1 
ATOM   2112 O  O   . ILE A 1 291 ? 20.710  123.587 32.101  1.00 28.84 ? 291  ILE A O   1 
ATOM   2113 C  CB  . ILE A 1 291 ? 22.103  123.597 35.221  1.00 29.43 ? 291  ILE A CB  1 
ATOM   2114 C  CG1 . ILE A 1 291 ? 23.440  124.081 35.796  1.00 31.03 ? 291  ILE A CG1 1 
ATOM   2115 C  CG2 . ILE A 1 291 ? 22.184  122.161 34.733  1.00 29.71 ? 291  ILE A CG2 1 
ATOM   2116 C  CD1 . ILE A 1 291 ? 23.972  123.244 36.941  1.00 31.12 ? 291  ILE A CD1 1 
ATOM   2117 N  N   . ALA A 1 292 ? 19.245  124.005 33.796  1.00 28.08 ? 292  ALA A N   1 
ATOM   2118 C  CA  . ALA A 1 292 ? 18.018  123.590 33.075  1.00 28.99 ? 292  ALA A CA  1 
ATOM   2119 C  C   . ALA A 1 292 ? 17.866  124.421 31.794  1.00 27.89 ? 292  ALA A C   1 
ATOM   2120 O  O   . ALA A 1 292 ? 17.649  123.823 30.727  1.00 27.12 ? 292  ALA A O   1 
ATOM   2121 C  CB  . ALA A 1 292 ? 16.812  123.719 33.968  1.00 30.16 ? 292  ALA A CB  1 
ATOM   2122 N  N   . ALA A 1 293 ? 17.985  125.750 31.889  1.00 28.61 ? 293  ALA A N   1 
ATOM   2123 C  CA  . ALA A 1 293 ? 17.845  126.674 30.737  1.00 29.06 ? 293  ALA A CA  1 
ATOM   2124 C  C   . ALA A 1 293 ? 18.869  126.297 29.657  1.00 30.61 ? 293  ALA A C   1 
ATOM   2125 O  O   . ALA A 1 293 ? 18.489  126.214 28.482  1.00 31.67 ? 293  ALA A O   1 
ATOM   2126 C  CB  . ALA A 1 293 ? 17.986  128.103 31.187  1.00 29.44 ? 293  ALA A CB  1 
ATOM   2127 N  N   . GLU A 1 294 ? 20.112  126.032 30.056  1.00 32.39 ? 294  GLU A N   1 
ATOM   2128 C  CA  . GLU A 1 294 ? 21.215  125.597 29.157  1.00 35.59 ? 294  GLU A CA  1 
ATOM   2129 C  C   . GLU A 1 294 ? 20.860  124.273 28.462  1.00 32.86 ? 294  GLU A C   1 
ATOM   2130 O  O   . GLU A 1 294 ? 21.101  124.177 27.242  1.00 30.91 ? 294  GLU A O   1 
ATOM   2131 C  CB  . GLU A 1 294 ? 22.511  125.484 29.957  1.00 39.89 ? 294  GLU A CB  1 
ATOM   2132 C  CG  . GLU A 1 294 ? 23.663  124.890 29.173  1.00 46.63 ? 294  GLU A CG  1 
ATOM   2133 C  CD  . GLU A 1 294 ? 25.032  125.205 29.752  1.00 52.10 ? 294  GLU A CD  1 
ATOM   2134 O  OE1 . GLU A 1 294 ? 25.085  125.759 30.869  1.00 56.70 ? 294  GLU A OE1 1 
ATOM   2135 O  OE2 . GLU A 1 294 ? 26.040  124.906 29.079  1.00 61.93 ? 294  GLU A OE2 1 
ATOM   2136 N  N   . MET A 1 295 ? 20.321  123.294 29.199  1.00 31.40 ? 295  MET A N   1 
ATOM   2137 C  CA  . MET A 1 295 ? 19.868  121.986 28.643  1.00 32.16 ? 295  MET A CA  1 
ATOM   2138 C  C   . MET A 1 295 ? 18.701  122.203 27.667  1.00 28.85 ? 295  MET A C   1 
ATOM   2139 O  O   . MET A 1 295 ? 18.691  121.580 26.600  1.00 26.43 ? 295  MET A O   1 
ATOM   2140 C  CB  . MET A 1 295 ? 19.417  121.035 29.754  1.00 34.84 ? 295  MET A CB  1 
ATOM   2141 C  CG  . MET A 1 295 ? 20.556  120.510 30.592  1.00 38.63 ? 295  MET A CG  1 
ATOM   2142 S  SD  . MET A 1 295 ? 19.966  119.508 31.991  1.00 45.89 ? 295  MET A SD  1 
ATOM   2143 C  CE  . MET A 1 295 ? 21.522  119.229 32.835  1.00 46.09 ? 295  MET A CE  1 
ATOM   2144 N  N   . PHE A 1 296 ? 17.742  123.049 28.027  1.00 27.27 ? 296  PHE A N   1 
ATOM   2145 C  CA  . PHE A 1 296 ? 16.637  123.453 27.127  1.00 27.39 ? 296  PHE A CA  1 
ATOM   2146 C  C   . PHE A 1 296 ? 17.225  124.022 25.826  1.00 26.79 ? 296  PHE A C   1 
ATOM   2147 O  O   . PHE A 1 296 ? 16.776  123.605 24.748  1.00 26.29 ? 296  PHE A O   1 
ATOM   2148 C  CB  . PHE A 1 296 ? 15.704  124.459 27.796  1.00 27.54 ? 296  PHE A CB  1 
ATOM   2149 C  CG  . PHE A 1 296 ? 14.621  124.942 26.867  1.00 28.02 ? 296  PHE A CG  1 
ATOM   2150 C  CD1 . PHE A 1 296 ? 13.525  124.140 26.589  1.00 27.35 ? 296  PHE A CD1 1 
ATOM   2151 C  CD2 . PHE A 1 296 ? 14.727  126.171 26.225  1.00 27.45 ? 296  PHE A CD2 1 
ATOM   2152 C  CE1 . PHE A 1 296 ? 12.543  124.568 25.707  1.00 27.60 ? 296  PHE A CE1 1 
ATOM   2153 C  CE2 . PHE A 1 296 ? 13.741  126.595 25.344  1.00 27.00 ? 296  PHE A CE2 1 
ATOM   2154 C  CZ  . PHE A 1 296 ? 12.654  125.790 25.088  1.00 27.29 ? 296  PHE A CZ  1 
ATOM   2155 N  N   . GLY A 1 297 ? 18.206  124.922 25.932  1.00 26.70 ? 297  GLY A N   1 
ATOM   2156 C  CA  . GLY A 1 297 ? 18.841  125.603 24.785  1.00 27.56 ? 297  GLY A CA  1 
ATOM   2157 C  C   . GLY A 1 297 ? 19.436  124.619 23.791  1.00 27.85 ? 297  GLY A C   1 
ATOM   2158 O  O   . GLY A 1 297 ? 19.257  124.800 22.574  1.00 28.89 ? 297  GLY A O   1 
ATOM   2159 N  N   . GLU A 1 298 ? 20.141  123.608 24.287  1.00 29.97 ? 298  GLU A N   1 
ATOM   2160 C  CA  . GLU A 1 298 ? 20.774  122.567 23.439  1.00 31.95 ? 298  GLU A CA  1 
ATOM   2161 C  C   . GLU A 1 298 ? 19.684  121.762 22.733  1.00 29.57 ? 298  GLU A C   1 
ATOM   2162 O  O   . GLU A 1 298 ? 19.863  121.454 21.549  1.00 28.01 ? 298  GLU A O   1 
ATOM   2163 C  CB  . GLU A 1 298 ? 21.673  121.663 24.274  1.00 34.77 ? 298  GLU A CB  1 
ATOM   2164 C  CG  . GLU A 1 298 ? 22.933  122.370 24.718  1.00 41.05 ? 298  GLU A CG  1 
ATOM   2165 C  CD  . GLU A 1 298 ? 23.937  121.468 25.407  1.00 46.27 ? 298  GLU A CD  1 
ATOM   2166 O  OE1 . GLU A 1 298 ? 25.042  121.958 25.721  1.00 51.24 ? 298  GLU A OE1 1 
ATOM   2167 O  OE2 . GLU A 1 298 ? 23.608  120.277 25.620  1.00 49.40 ? 298  GLU A OE2 1 
ATOM   2168 N  N   . PHE A 1 299 ? 18.593  121.429 23.421  1.00 29.31 ? 299  PHE A N   1 
ATOM   2169 C  CA  . PHE A 1 299 ? 17.475  120.692 22.785  1.00 29.19 ? 299  PHE A CA  1 
ATOM   2170 C  C   . PHE A 1 299 ? 16.808  121.593 21.739  1.00 29.30 ? 299  PHE A C   1 
ATOM   2171 O  O   . PHE A 1 299 ? 16.510  121.114 20.626  1.00 28.90 ? 299  PHE A O   1 
ATOM   2172 C  CB  . PHE A 1 299 ? 16.442  120.198 23.794  1.00 31.65 ? 299  PHE A CB  1 
ATOM   2173 C  CG  . PHE A 1 299 ? 15.434  119.290 23.142  1.00 34.84 ? 299  PHE A CG  1 
ATOM   2174 C  CD1 . PHE A 1 299 ? 14.342  119.814 22.469  1.00 35.98 ? 299  PHE A CD1 1 
ATOM   2175 C  CD2 . PHE A 1 299 ? 15.631  117.917 23.116  1.00 37.64 ? 299  PHE A CD2 1 
ATOM   2176 C  CE1 . PHE A 1 299 ? 13.431  118.983 21.835  1.00 38.93 ? 299  PHE A CE1 1 
ATOM   2177 C  CE2 . PHE A 1 299 ? 14.724  117.088 22.472  1.00 38.89 ? 299  PHE A CE2 1 
ATOM   2178 C  CZ  . PHE A 1 299 ? 13.625  117.620 21.837  1.00 38.89 ? 299  PHE A CZ  1 
ATOM   2179 N  N   . PHE A 1 300 ? 16.552  122.855 22.091  1.00 26.31 ? 300  PHE A N   1 
ATOM   2180 C  CA  . PHE A 1 300 ? 15.931  123.836 21.168  1.00 26.17 ? 300  PHE A CA  1 
ATOM   2181 C  C   . PHE A 1 300 ? 16.754  123.902 19.877  1.00 26.43 ? 300  PHE A C   1 
ATOM   2182 O  O   . PHE A 1 300 ? 16.172  123.792 18.787  1.00 25.80 ? 300  PHE A O   1 
ATOM   2183 C  CB  . PHE A 1 300 ? 15.804  125.208 21.825  1.00 25.46 ? 300  PHE A CB  1 
ATOM   2184 C  CG  . PHE A 1 300 ? 15.272  126.270 20.900  1.00 24.34 ? 300  PHE A CG  1 
ATOM   2185 C  CD1 . PHE A 1 300 ? 16.132  127.007 20.099  1.00 24.06 ? 300  PHE A CD1 1 
ATOM   2186 C  CD2 . PHE A 1 300 ? 13.912  126.514 20.807  1.00 24.67 ? 300  PHE A CD2 1 
ATOM   2187 C  CE1 . PHE A 1 300 ? 15.641  127.974 19.237  1.00 24.68 ? 300  PHE A CE1 1 
ATOM   2188 C  CE2 . PHE A 1 300 ? 13.423  127.486 19.946  1.00 23.93 ? 300  PHE A CE2 1 
ATOM   2189 C  CZ  . PHE A 1 300 ? 14.288  128.215 19.164  1.00 25.07 ? 300  PHE A CZ  1 
ATOM   2190 N  N   . SER A 1 301 ? 18.070  124.079 20.013  1.00 27.74 ? 301  SER A N   1 
ATOM   2191 C  CA  . SER A 1 301 ? 19.023  124.195 18.874  1.00 29.35 ? 301  SER A CA  1 
ATOM   2192 C  C   . SER A 1 301 ? 18.936  122.937 17.995  1.00 29.50 ? 301  SER A C   1 
ATOM   2193 O  O   . SER A 1 301 ? 18.798  123.074 16.763  1.00 27.27 ? 301  SER A O   1 
ATOM   2194 C  CB  . SER A 1 301 ? 20.440  124.438 19.357  1.00 32.13 ? 301  SER A CB  1 
ATOM   2195 O  OG  . SER A 1 301 ? 20.562  125.699 20.014  1.00 34.85 ? 301  SER A OG  1 
ATOM   2196 N  N   . MET A 1 302 ? 19.013  121.751 18.608  1.00 29.97 ? 302  MET A N   1 
ATOM   2197 C  CA  . MET A 1 302 ? 18.995  120.452 17.881  1.00 29.31 ? 302  MET A CA  1 
ATOM   2198 C  C   . MET A 1 302 ? 17.648  120.302 17.162  1.00 29.05 ? 302  MET A C   1 
ATOM   2199 O  O   . MET A 1 302 ? 17.663  120.006 15.961  1.00 31.44 ? 302  MET A O   1 
ATOM   2200 C  CB  . MET A 1 302 ? 19.205  119.273 18.834  1.00 29.80 ? 302  MET A CB  1 
ATOM   2201 N  N   . HIS A 1 303 ? 16.529  120.528 17.858  1.00 26.67 ? 303  HIS A N   1 
ATOM   2202 C  CA  . HIS A 1 303 ? 15.157  120.406 17.295  1.00 27.34 ? 303  HIS A CA  1 
ATOM   2203 C  C   . HIS A 1 303 ? 14.972  121.428 16.168  1.00 25.93 ? 303  HIS A C   1 
ATOM   2204 O  O   . HIS A 1 303 ? 14.417  121.044 15.117  1.00 25.19 ? 303  HIS A O   1 
ATOM   2205 C  CB  . HIS A 1 303 ? 14.089  120.530 18.390  1.00 28.89 ? 303  HIS A CB  1 
ATOM   2206 C  CG  . HIS A 1 303 ? 12.733  120.083 17.955  1.00 30.56 ? 303  HIS A CG  1 
ATOM   2207 N  ND1 . HIS A 1 303 ? 12.506  118.832 17.411  1.00 33.79 ? 303  HIS A ND1 1 
ATOM   2208 C  CD2 . HIS A 1 303 ? 11.535  120.711 17.969  1.00 33.07 ? 303  HIS A CD2 1 
ATOM   2209 C  CE1 . HIS A 1 303 ? 11.227  118.712 17.105  1.00 34.04 ? 303  HIS A CE1 1 
ATOM   2210 N  NE2 . HIS A 1 303 ? 10.605  119.850 17.440  1.00 32.76 ? 303  HIS A NE2 1 
ATOM   2211 N  N   . LEU A 1 304 ? 15.416  122.675 16.376  1.00 25.78 ? 304  LEU A N   1 
ATOM   2212 C  CA  . LEU A 1 304 ? 15.385  123.734 15.329  1.00 26.19 ? 304  LEU A CA  1 
ATOM   2213 C  C   . LEU A 1 304 ? 16.142  123.224 14.100  1.00 27.47 ? 304  LEU A C   1 
ATOM   2214 O  O   . LEU A 1 304 ? 15.608  123.340 12.981  1.00 27.36 ? 304  LEU A O   1 
ATOM   2215 C  CB  . LEU A 1 304 ? 16.003  125.038 15.841  1.00 26.23 ? 304  LEU A CB  1 
ATOM   2216 C  CG  . LEU A 1 304 ? 16.223  126.111 14.774  1.00 26.55 ? 304  LEU A CG  1 
ATOM   2217 C  CD1 . LEU A 1 304 ? 14.908  126.526 14.146  1.00 26.81 ? 304  LEU A CD1 1 
ATOM   2218 C  CD2 . LEU A 1 304 ? 16.947  127.319 15.350  1.00 27.73 ? 304  LEU A CD2 1 
ATOM   2219 N  N   . GLN A 1 305 ? 17.340  122.680 14.302  1.00 28.97 ? 305  GLN A N   1 
ATOM   2220 C  CA  . GLN A 1 305 ? 18.209  122.233 13.182  1.00 31.50 ? 305  GLN A CA  1 
ATOM   2221 C  C   . GLN A 1 305 ? 17.499  121.100 12.425  1.00 31.20 ? 305  GLN A C   1 
ATOM   2222 O  O   . GLN A 1 305 ? 17.528  121.124 11.181  1.00 33.01 ? 305  GLN A O   1 
ATOM   2223 C  CB  . GLN A 1 305 ? 19.594  121.862 13.706  1.00 32.97 ? 305  GLN A CB  1 
ATOM   2224 C  CG  . GLN A 1 305 ? 20.517  121.345 12.618  1.00 36.76 ? 305  GLN A CG  1 
ATOM   2225 C  CD  . GLN A 1 305 ? 21.983  121.583 12.902  1.00 39.46 ? 305  GLN A CD  1 
ATOM   2226 O  OE1 . GLN A 1 305 ? 22.361  122.278 13.840  1.00 41.54 ? 305  GLN A OE1 1 
ATOM   2227 N  NE2 . GLN A 1 305 ? 22.830  121.037 12.046  1.00 42.52 ? 305  GLN A NE2 1 
ATOM   2228 N  N   . VAL A 1 306 ? 16.825  120.190 13.140  1.00 30.35 ? 306  VAL A N   1 
ATOM   2229 C  CA  . VAL A 1 306 ? 16.068  119.048 12.544  1.00 31.72 ? 306  VAL A CA  1 
ATOM   2230 C  C   . VAL A 1 306 ? 14.902  119.590 11.706  1.00 31.65 ? 306  VAL A C   1 
ATOM   2231 O  O   . VAL A 1 306 ? 14.774  119.164 10.550  1.00 30.74 ? 306  VAL A O   1 
ATOM   2232 C  CB  . VAL A 1 306 ? 15.585  118.042 13.610  1.00 32.18 ? 306  VAL A CB  1 
ATOM   2233 C  CG1 . VAL A 1 306 ? 14.503  117.111 13.077  1.00 32.80 ? 306  VAL A CG1 1 
ATOM   2234 C  CG2 . VAL A 1 306 ? 16.749  117.234 14.167  1.00 32.41 ? 306  VAL A CG2 1 
ATOM   2235 N  N   . LEU A 1 307 ? 14.069  120.469 12.267  1.00 30.86 ? 307  LEU A N   1 
ATOM   2236 C  CA  . LEU A 1 307 ? 12.909  121.056 11.546  1.00 29.81 ? 307  LEU A CA  1 
ATOM   2237 C  C   . LEU A 1 307 ? 13.394  121.834 10.321  1.00 29.36 ? 307  LEU A C   1 
ATOM   2238 O  O   . LEU A 1 307 ? 12.728  121.731 9.293   1.00 27.61 ? 307  LEU A O   1 
ATOM   2239 C  CB  . LEU A 1 307 ? 12.105  121.955 12.487  1.00 30.04 ? 307  LEU A CB  1 
ATOM   2240 C  CG  . LEU A 1 307 ? 11.357  121.214 13.588  1.00 31.13 ? 307  LEU A CG  1 
ATOM   2241 C  CD1 . LEU A 1 307 ? 10.740  122.185 14.575  1.00 30.91 ? 307  LEU A CD1 1 
ATOM   2242 C  CD2 . LEU A 1 307 ? 10.299  120.291 13.004  1.00 32.36 ? 307  LEU A CD2 1 
ATOM   2243 N  N   . LYS A 1 308 ? 14.511  122.564 10.430  1.00 30.56 ? 308  LYS A N   1 
ATOM   2244 C  CA  . LYS A 1 308 ? 15.054  123.434 9.346   1.00 33.80 ? 308  LYS A CA  1 
ATOM   2245 C  C   . LYS A 1 308 ? 15.463  122.563 8.146   1.00 37.83 ? 308  LYS A C   1 
ATOM   2246 O  O   . LYS A 1 308 ? 15.164  122.960 6.992   1.00 35.20 ? 308  LYS A O   1 
ATOM   2247 C  CB  . LYS A 1 308 ? 16.208  124.286 9.888   1.00 36.41 ? 308  LYS A CB  1 
ATOM   2248 C  CG  . LYS A 1 308 ? 16.699  125.409 8.983   1.00 39.45 ? 308  LYS A CG  1 
ATOM   2249 C  CD  . LYS A 1 308 ? 17.815  126.228 9.602   1.00 40.56 ? 308  LYS A CD  1 
ATOM   2250 C  CE  . LYS A 1 308 ? 18.304  127.366 8.728   1.00 42.35 ? 308  LYS A CE  1 
ATOM   2251 N  NZ  . LYS A 1 308 ? 19.520  126.995 7.966   1.00 44.26 ? 308  LYS A NZ  1 
ATOM   2252 N  N   . GLN A 1 309 ? 16.095  121.411 8.410   1.00 38.41 ? 309  GLN A N   1 
ATOM   2253 C  CA  . GLN A 1 309 ? 16.515  120.405 7.389   1.00 39.57 ? 309  GLN A CA  1 
ATOM   2254 C  C   . GLN A 1 309 ? 15.287  119.839 6.682   1.00 37.72 ? 309  GLN A C   1 
ATOM   2255 O  O   . GLN A 1 309 ? 15.289  119.682 5.464   1.00 32.75 ? 309  GLN A O   1 
ATOM   2256 C  CB  . GLN A 1 309 ? 17.319  119.269 8.032   1.00 42.40 ? 309  GLN A CB  1 
ATOM   2257 C  CG  . GLN A 1 309 ? 18.702  119.705 8.504   1.00 48.08 ? 309  GLN A CG  1 
ATOM   2258 C  CD  . GLN A 1 309 ? 19.460  118.656 9.286   1.00 53.06 ? 309  GLN A CD  1 
ATOM   2259 O  OE1 . GLN A 1 309 ? 19.008  117.526 9.477   1.00 51.31 ? 309  GLN A OE1 1 
ATOM   2260 N  NE2 . GLN A 1 309 ? 20.641  119.033 9.753   1.00 55.54 ? 309  GLN A NE2 1 
HETATM 2261 N  N   . MLZ A 1 310 ? 14.249  119.513 7.461   1.00 35.38 ? 310  MLZ A N   1 
HETATM 2262 C  CA  . MLZ A 1 310 ? 13.031  118.946 6.906   1.00 37.08 ? 310  MLZ A CA  1 
HETATM 2263 C  CB  . MLZ A 1 310 ? 12.093  118.494 8.027   1.00 38.76 ? 310  MLZ A CB  1 
HETATM 2264 C  CG  . MLZ A 1 310 ? 10.691  118.106 7.582   1.00 40.70 ? 310  MLZ A CG  1 
HETATM 2265 C  CD  . MLZ A 1 310 ? 10.638  116.932 6.636   1.00 41.72 ? 310  MLZ A CD  1 
HETATM 2266 C  CE  . MLZ A 1 310 ? 9.216   116.403 6.558   1.00 43.97 ? 310  MLZ A CE  1 
HETATM 2267 N  NZ  . MLZ A 1 310 ? 9.014   115.431 5.479   1.00 46.32 ? 310  MLZ A NZ  1 
HETATM 2268 C  CM  . MLZ A 1 310 ? 7.603   115.111 5.200   1.00 45.35 ? 310  MLZ A CM  1 
HETATM 2269 C  C   . MLZ A 1 310 ? 12.335  119.955 5.990   1.00 36.48 ? 310  MLZ A C   1 
HETATM 2270 O  O   . MLZ A 1 310 ? 11.872  119.592 4.908   1.00 35.68 ? 310  MLZ A O   1 
ATOM   2271 N  N   . ARG A 1 311 ? 12.229  121.212 6.438   1.00 33.03 ? 311  ARG A N   1 
ATOM   2272 C  CA  . ARG A 1 311 ? 11.584  122.241 5.639   1.00 34.69 ? 311  ARG A CA  1 
ATOM   2273 C  C   . ARG A 1 311 ? 12.354  122.413 4.325   1.00 33.31 ? 311  ARG A C   1 
ATOM   2274 O  O   . ARG A 1 311 ? 11.706  122.504 3.264   1.00 31.92 ? 311  ARG A O   1 
ATOM   2275 C  CB  . ARG A 1 311 ? 11.508  123.566 6.401   1.00 36.77 ? 311  ARG A CB  1 
ATOM   2276 C  CG  . ARG A 1 311 ? 10.869  124.705 5.616   1.00 38.89 ? 311  ARG A CG  1 
ATOM   2277 C  CD  . ARG A 1 311 ? 10.910  126.022 6.370   1.00 44.35 ? 311  ARG A CD  1 
ATOM   2278 N  NE  . ARG A 1 311 ? 12.261  126.432 6.753   1.00 47.79 ? 311  ARG A NE  1 
ATOM   2279 C  CZ  . ARG A 1 311 ? 12.549  127.380 7.645   1.00 49.81 ? 311  ARG A CZ  1 
ATOM   2280 N  NH1 . ARG A 1 311 ? 11.581  128.046 8.255   1.00 52.63 ? 311  ARG A NH1 1 
ATOM   2281 N  NH2 . ARG A 1 311 ? 13.811  127.659 7.923   1.00 51.12 ? 311  ARG A NH2 1 
ATOM   2282 N  N   . ARG A 1 312 ? 13.684  122.442 4.401   1.00 32.94 ? 312  ARG A N   1 
ATOM   2283 C  CA  . ARG A 1 312 ? 14.566  122.571 3.204   1.00 35.26 ? 312  ARG A CA  1 
ATOM   2284 C  C   . ARG A 1 312 ? 14.299  121.411 2.238   1.00 34.58 ? 312  ARG A C   1 
ATOM   2285 O  O   . ARG A 1 312 ? 14.068  121.682 1.051   1.00 34.62 ? 312  ARG A O   1 
ATOM   2286 C  CB  . ARG A 1 312 ? 16.043  122.608 3.600   1.00 35.06 ? 312  ARG A CB  1 
ATOM   2287 C  CG  . ARG A 1 312 ? 16.961  123.040 2.467   1.00 36.50 ? 312  ARG A CG  1 
ATOM   2288 C  CD  . ARG A 1 312 ? 18.423  122.981 2.861   1.00 37.07 ? 312  ARG A CD  1 
ATOM   2289 N  NE  . ARG A 1 312 ? 19.256  123.601 1.842   1.00 38.10 ? 312  ARG A NE  1 
ATOM   2290 C  CZ  . ARG A 1 312 ? 19.549  123.055 0.664   1.00 40.14 ? 312  ARG A CZ  1 
ATOM   2291 N  NH1 . ARG A 1 312 ? 19.076  121.862 0.335   1.00 40.76 ? 312  ARG A NH1 1 
ATOM   2292 N  NH2 . ARG A 1 312 ? 20.317  123.709 -0.191  1.00 40.00 ? 312  ARG A NH2 1 
ATOM   2293 N  N   . LEU A 1 313 ? 14.325  120.175 2.737   1.00 35.46 ? 313  LEU A N   1 
ATOM   2294 C  CA  . LEU A 1 313 ? 14.089  118.935 1.942   1.00 35.89 ? 313  LEU A CA  1 
ATOM   2295 C  C   . LEU A 1 313 ? 12.723  119.013 1.247   1.00 34.55 ? 313  LEU A C   1 
ATOM   2296 O  O   . LEU A 1 313 ? 12.657  118.739 0.036   1.00 32.59 ? 313  LEU A O   1 
ATOM   2297 C  CB  . LEU A 1 313 ? 14.146  117.720 2.871   1.00 36.88 ? 313  LEU A CB  1 
ATOM   2298 C  CG  . LEU A 1 313 ? 13.788  116.383 2.224   1.00 39.81 ? 313  LEU A CG  1 
ATOM   2299 C  CD1 . LEU A 1 313 ? 14.915  115.909 1.316   1.00 38.46 ? 313  LEU A CD1 1 
ATOM   2300 C  CD2 . LEU A 1 313 ? 13.473  115.333 3.278   1.00 39.57 ? 313  LEU A CD2 1 
ATOM   2301 N  N   . ASP A 1 314 ? 11.672  119.345 2.000   1.00 33.49 ? 314  ASP A N   1 
ATOM   2302 C  CA  . ASP A 1 314 ? 10.285  119.477 1.479   1.00 35.09 ? 314  ASP A CA  1 
ATOM   2303 C  C   . ASP A 1 314 ? 10.260  120.511 0.342   1.00 34.19 ? 314  ASP A C   1 
ATOM   2304 O  O   . ASP A 1 314 ? 9.618   120.239 -0.681  1.00 34.79 ? 314  ASP A O   1 
ATOM   2305 C  CB  . ASP A 1 314 ? 9.310   119.843 2.601   1.00 37.93 ? 314  ASP A CB  1 
ATOM   2306 C  CG  . ASP A 1 314 ? 9.075   118.717 3.600   1.00 41.15 ? 314  ASP A CG  1 
ATOM   2307 O  OD1 . ASP A 1 314 ? 9.615   117.613 3.385   1.00 42.31 ? 314  ASP A OD1 1 
ATOM   2308 O  OD2 . ASP A 1 314 ? 8.354   118.955 4.590   1.00 41.98 ? 314  ASP A OD2 1 
ATOM   2309 N  N   . THR A 1 315 ? 10.927  121.654 0.523   1.00 33.81 ? 315  THR A N   1 
ATOM   2310 C  CA  . THR A 1 315 ? 10.946  122.769 -0.464  1.00 36.51 ? 315  THR A CA  1 
ATOM   2311 C  C   . THR A 1 315 ? 11.660  122.322 -1.749  1.00 35.94 ? 315  THR A C   1 
ATOM   2312 O  O   . THR A 1 315 ? 11.114  122.583 -2.839  1.00 32.08 ? 315  THR A O   1 
ATOM   2313 C  CB  . THR A 1 315 ? 11.574  124.030 0.140   1.00 36.77 ? 315  THR A CB  1 
ATOM   2314 O  OG1 . THR A 1 315 ? 10.866  124.288 1.351   1.00 40.61 ? 315  THR A OG1 1 
ATOM   2315 C  CG2 . THR A 1 315 ? 11.488  125.234 -0.768  1.00 38.32 ? 315  THR A CG2 1 
ATOM   2316 N  N   . ILE A 1 316 ? 12.837  121.700 -1.621  1.00 35.20 ? 316  ILE A N   1 
ATOM   2317 C  CA  . ILE A 1 316 ? 13.633  121.174 -2.772  1.00 36.31 ? 316  ILE A CA  1 
ATOM   2318 C  C   . ILE A 1 316 ? 12.806  120.095 -3.483  1.00 35.61 ? 316  ILE A C   1 
ATOM   2319 O  O   . ILE A 1 316 ? 12.785  120.097 -4.730  1.00 33.61 ? 316  ILE A O   1 
ATOM   2320 C  CB  . ILE A 1 316 ? 15.011  120.629 -2.330  1.00 39.52 ? 316  ILE A CB  1 
ATOM   2321 C  CG1 . ILE A 1 316 ? 15.850  121.670 -1.583  1.00 39.38 ? 316  ILE A CG1 1 
ATOM   2322 C  CG2 . ILE A 1 316 ? 15.775  120.071 -3.528  1.00 40.98 ? 316  ILE A CG2 1 
ATOM   2323 C  CD1 . ILE A 1 316 ? 15.937  123.009 -2.276  1.00 39.01 ? 316  ILE A CD1 1 
ATOM   2324 N  N   . ASN A 1 317 ? 12.159  119.206 -2.721  1.00 34.95 ? 317  ASN A N   1 
ATOM   2325 C  CA  . ASN A 1 317 ? 11.357  118.083 -3.280  1.00 36.55 ? 317  ASN A CA  1 
ATOM   2326 C  C   . ASN A 1 317 ? 10.164  118.660 -4.054  1.00 37.19 ? 317  ASN A C   1 
ATOM   2327 O  O   . ASN A 1 317 ? 9.903   118.196 -5.173  1.00 37.34 ? 317  ASN A O   1 
ATOM   2328 C  CB  . ASN A 1 317 ? 10.890  117.101 -2.202  1.00 38.08 ? 317  ASN A CB  1 
ATOM   2329 C  CG  . ASN A 1 317 ? 11.945  116.102 -1.765  1.00 39.03 ? 317  ASN A CG  1 
ATOM   2330 O  OD1 . ASN A 1 317 ? 13.061  116.074 -2.276  1.00 40.01 ? 317  ASN A OD1 1 
ATOM   2331 N  ND2 . ASN A 1 317 ? 11.593  115.265 -0.805  1.00 39.95 ? 317  ASN A ND2 1 
ATOM   2332 N  N   . HIS A 1 318 ? 9.461   119.631 -3.467  1.00 36.63 ? 318  HIS A N   1 
ATOM   2333 C  CA  . HIS A 1 318 ? 8.336   120.362 -4.107  1.00 35.21 ? 318  HIS A CA  1 
ATOM   2334 C  C   . HIS A 1 318 ? 8.800   120.925 -5.458  1.00 34.40 ? 318  HIS A C   1 
ATOM   2335 O  O   . HIS A 1 318 ? 8.063   120.764 -6.446  1.00 31.66 ? 318  HIS A O   1 
ATOM   2336 C  CB  . HIS A 1 318 ? 7.811   121.441 -3.152  1.00 37.48 ? 318  HIS A CB  1 
ATOM   2337 C  CG  . HIS A 1 318 ? 6.679   122.241 -3.697  1.00 40.81 ? 318  HIS A CG  1 
ATOM   2338 N  ND1 . HIS A 1 318 ? 6.873   123.473 -4.307  1.00 43.61 ? 318  HIS A ND1 1 
ATOM   2339 C  CD2 . HIS A 1 318 ? 5.349   122.008 -3.724  1.00 43.12 ? 318  HIS A CD2 1 
ATOM   2340 C  CE1 . HIS A 1 318 ? 5.710   123.962 -4.677  1.00 42.32 ? 318  HIS A CE1 1 
ATOM   2341 N  NE2 . HIS A 1 318 ? 4.761   123.080 -4.341  1.00 42.98 ? 318  HIS A NE2 1 
ATOM   2342 N  N   . ALA A 1 319 ? 9.987   121.542 -5.498  1.00 31.76 ? 319  ALA A N   1 
ATOM   2343 C  CA  . ALA A 1 319 ? 10.568  122.176 -6.706  1.00 31.94 ? 319  ALA A CA  1 
ATOM   2344 C  C   . ALA A 1 319 ? 10.796  121.112 -7.783  1.00 31.90 ? 319  ALA A C   1 
ATOM   2345 O  O   . ALA A 1 319 ? 10.349  121.318 -8.934  1.00 30.17 ? 319  ALA A O   1 
ATOM   2346 C  CB  . ALA A 1 319 ? 11.846  122.897 -6.352  1.00 32.62 ? 319  ALA A CB  1 
ATOM   2347 N  N   . HIS A 1 320 ? 11.438  120.003 -7.408  1.00 32.49 ? 320  HIS A N   1 
ATOM   2348 C  CA  . HIS A 1 320 ? 11.757  118.865 -8.314  1.00 34.49 ? 320  HIS A CA  1 
ATOM   2349 C  C   . HIS A 1 320 ? 10.471  118.292 -8.922  1.00 33.49 ? 320  HIS A C   1 
ATOM   2350 O  O   . HIS A 1 320 ? 10.461  118.054 -10.145 1.00 31.76 ? 320  HIS A O   1 
ATOM   2351 C  CB  . HIS A 1 320 ? 12.570  117.782 -7.589  1.00 35.89 ? 320  HIS A CB  1 
ATOM   2352 C  CG  . HIS A 1 320 ? 13.987  118.158 -7.324  1.00 36.76 ? 320  HIS A CG  1 
ATOM   2353 N  ND1 . HIS A 1 320 ? 14.785  118.744 -8.281  1.00 40.81 ? 320  HIS A ND1 1 
ATOM   2354 C  CD2 . HIS A 1 320 ? 14.762  118.005 -6.229  1.00 40.78 ? 320  HIS A CD2 1 
ATOM   2355 C  CE1 . HIS A 1 320 ? 15.990  118.955 -7.781  1.00 42.29 ? 320  HIS A CE1 1 
ATOM   2356 N  NE2 . HIS A 1 320 ? 16.001  118.511 -6.522  1.00 41.85 ? 320  HIS A NE2 1 
ATOM   2357 N  N   . ALA A 1 321 ? 9.441   118.055 -8.100  1.00 33.03 ? 321  ALA A N   1 
ATOM   2358 C  CA  . ALA A 1 321 ? 8.145   117.468 -8.528  1.00 32.31 ? 321  ALA A CA  1 
ATOM   2359 C  C   . ALA A 1 321 ? 7.442   118.413 -9.512  1.00 31.99 ? 321  ALA A C   1 
ATOM   2360 O  O   . ALA A 1 321 ? 6.822   117.912 -10.474 1.00 31.97 ? 321  ALA A O   1 
ATOM   2361 C  CB  . ALA A 1 321 ? 7.271   117.158 -7.334  1.00 32.89 ? 321  ALA A CB  1 
ATOM   2362 N  N   . ALA A 1 322 ? 7.530   119.727 -9.283  1.00 29.26 ? 322  ALA A N   1 
ATOM   2363 C  CA  . ALA A 1 322 ? 6.945   120.761 -10.171 1.00 30.22 ? 322  ALA A CA  1 
ATOM   2364 C  C   . ALA A 1 322 ? 7.706   120.810 -11.508 1.00 29.09 ? 322  ALA A C   1 
ATOM   2365 O  O   . ALA A 1 322 ? 7.060   120.887 -12.571 1.00 27.45 ? 322  ALA A O   1 
ATOM   2366 C  CB  . ALA A 1 322 ? 6.951   122.098 -9.473  1.00 30.89 ? 322  ALA A CB  1 
ATOM   2367 N  N   . LEU A 1 323 ? 9.036   120.781 -11.459 1.00 29.73 ? 323  LEU A N   1 
ATOM   2368 C  CA  . LEU A 1 323 ? 9.901   120.858 -12.669 1.00 30.84 ? 323  LEU A CA  1 
ATOM   2369 C  C   . LEU A 1 323 ? 9.762   119.570 -13.494 1.00 32.36 ? 323  LEU A C   1 
ATOM   2370 O  O   . LEU A 1 323 ? 9.824   119.665 -14.731 1.00 33.16 ? 323  LEU A O   1 
ATOM   2371 C  CB  . LEU A 1 323 ? 11.345  121.115 -12.239 1.00 30.35 ? 323  LEU A CB  1 
ATOM   2372 C  CG  . LEU A 1 323 ? 11.626  122.518 -11.687 1.00 29.61 ? 323  LEU A CG  1 
ATOM   2373 C  CD1 . LEU A 1 323 ? 13.015  122.584 -11.085 1.00 28.84 ? 323  LEU A CD1 1 
ATOM   2374 C  CD2 . LEU A 1 323 ? 11.477  123.589 -12.762 1.00 28.95 ? 323  LEU A CD2 1 
ATOM   2375 N  N   . ASP A 1 324 ? 9.572   118.422 -12.838 1.00 34.29 ? 324  ASP A N   1 
ATOM   2376 C  CA  . ASP A 1 324 ? 9.297   117.119 -13.502 1.00 36.99 ? 324  ASP A CA  1 
ATOM   2377 C  C   . ASP A 1 324 ? 7.950   117.194 -14.229 1.00 36.16 ? 324  ASP A C   1 
ATOM   2378 O  O   . ASP A 1 324 ? 7.902   116.756 -15.396 1.00 34.43 ? 324  ASP A O   1 
ATOM   2379 C  CB  . ASP A 1 324 ? 9.327   115.947 -12.518 1.00 41.47 ? 324  ASP A CB  1 
ATOM   2380 C  CG  . ASP A 1 324 ? 10.731  115.532 -12.110 1.00 48.42 ? 324  ASP A CG  1 
ATOM   2381 O  OD1 . ASP A 1 324 ? 11.650  115.616 -12.962 1.00 49.62 ? 324  ASP A OD1 1 
ATOM   2382 O  OD2 . ASP A 1 324 ? 10.898  115.128 -10.935 1.00 57.17 ? 324  ASP A OD2 1 
ATOM   2383 N  N   . ARG A 1 325 ? 6.901   117.718 -13.578 1.00 34.35 ? 325  ARG A N   1 
ATOM   2384 C  CA  . ARG A 1 325 ? 5.592   117.954 -14.249 1.00 35.30 ? 325  ARG A CA  1 
ATOM   2385 C  C   . ARG A 1 325 ? 5.819   118.826 -15.486 1.00 33.71 ? 325  ARG A C   1 
ATOM   2386 O  O   . ARG A 1 325 ? 5.301   118.469 -16.549 1.00 35.80 ? 325  ARG A O   1 
ATOM   2387 C  CB  . ARG A 1 325 ? 4.564   118.617 -13.329 1.00 39.32 ? 325  ARG A CB  1 
ATOM   2388 C  CG  . ARG A 1 325 ? 3.975   117.683 -12.283 1.00 42.33 ? 325  ARG A CG  1 
ATOM   2389 C  CD  . ARG A 1 325 ? 2.729   118.261 -11.638 1.00 43.63 ? 325  ARG A CD  1 
ATOM   2390 N  NE  . ARG A 1 325 ? 2.922   119.629 -11.168 1.00 46.19 ? 325  ARG A NE  1 
ATOM   2391 C  CZ  . ARG A 1 325 ? 3.399   119.985 -9.976  1.00 45.02 ? 325  ARG A CZ  1 
ATOM   2392 N  NH1 . ARG A 1 325 ? 3.769   119.077 -9.087  1.00 44.17 ? 325  ARG A NH1 1 
ATOM   2393 N  NH2 . ARG A 1 325 ? 3.518   121.269 -9.686  1.00 46.43 ? 325  ARG A NH2 1 
ATOM   2394 N  N   . PHE A 1 326 ? 6.590   119.908 -15.366 1.00 31.31 ? 326  PHE A N   1 
ATOM   2395 C  CA  . PHE A 1 326 ? 6.839   120.832 -16.498 1.00 31.47 ? 326  PHE A CA  1 
ATOM   2396 C  C   . PHE A 1 326 ? 7.527   120.076 -17.647 1.00 31.88 ? 326  PHE A C   1 
ATOM   2397 O  O   . PHE A 1 326 ? 7.133   120.267 -18.824 1.00 29.43 ? 326  PHE A O   1 
ATOM   2398 C  CB  . PHE A 1 326 ? 7.656   122.054 -16.086 1.00 31.53 ? 326  PHE A CB  1 
ATOM   2399 C  CG  . PHE A 1 326 ? 7.721   123.070 -17.197 1.00 31.28 ? 326  PHE A CG  1 
ATOM   2400 C  CD1 . PHE A 1 326 ? 6.582   123.759 -17.583 1.00 32.72 ? 326  PHE A CD1 1 
ATOM   2401 C  CD2 . PHE A 1 326 ? 8.892   123.288 -17.899 1.00 31.76 ? 326  PHE A CD2 1 
ATOM   2402 C  CE1 . PHE A 1 326 ? 6.627   124.669 -18.629 1.00 33.59 ? 326  PHE A CE1 1 
ATOM   2403 C  CE2 . PHE A 1 326 ? 8.938   124.205 -18.939 1.00 32.58 ? 326  PHE A CE2 1 
ATOM   2404 C  CZ  . PHE A 1 326 ? 7.803   124.892 -19.305 1.00 32.93 ? 326  PHE A CZ  1 
ATOM   2405 N  N   . LEU A 1 327 ? 8.525   119.254 -17.323 1.00 32.47 ? 327  LEU A N   1 
ATOM   2406 C  CA  . LEU A 1 327 ? 9.290   118.446 -18.315 1.00 35.16 ? 327  LEU A CA  1 
ATOM   2407 C  C   . LEU A 1 327 ? 8.339   117.506 -19.064 1.00 34.69 ? 327  LEU A C   1 
ATOM   2408 O  O   . LEU A 1 327 ? 8.446   117.431 -20.308 1.00 33.24 ? 327  LEU A O   1 
ATOM   2409 C  CB  . LEU A 1 327 ? 10.391  117.657 -17.602 1.00 37.57 ? 327  LEU A CB  1 
ATOM   2410 C  CG  . LEU A 1 327 ? 11.759  118.331 -17.560 1.00 39.65 ? 327  LEU A CG  1 
ATOM   2411 C  CD1 . LEU A 1 327 ? 12.659  117.675 -16.518 1.00 40.47 ? 327  LEU A CD1 1 
ATOM   2412 C  CD2 . LEU A 1 327 ? 12.417  118.295 -18.927 1.00 40.73 ? 327  LEU A CD2 1 
ATOM   2413 N  N   . ARG A 1 328 ? 7.452   116.814 -18.342 1.00 36.27 ? 328  ARG A N   1 
ATOM   2414 C  CA  . ARG A 1 328 ? 6.484   115.858 -18.951 1.00 40.03 ? 328  ARG A CA  1 
ATOM   2415 C  C   . ARG A 1 328 ? 5.503   116.629 -19.842 1.00 38.72 ? 328  ARG A C   1 
ATOM   2416 O  O   . ARG A 1 328 ? 5.245   116.170 -20.964 1.00 38.59 ? 328  ARG A O   1 
ATOM   2417 C  CB  . ARG A 1 328 ? 5.767   115.053 -17.865 1.00 44.22 ? 328  ARG A CB  1 
ATOM   2418 C  CG  . ARG A 1 328 ? 6.692   114.091 -17.134 1.00 51.16 ? 328  ARG A CG  1 
ATOM   2419 C  CD  . ARG A 1 328 ? 6.007   113.276 -16.052 1.00 58.38 ? 328  ARG A CD  1 
ATOM   2420 N  NE  . ARG A 1 328 ? 6.953   112.886 -15.007 1.00 65.49 ? 328  ARG A NE  1 
ATOM   2421 C  CZ  . ARG A 1 328 ? 7.807   111.863 -15.081 1.00 70.49 ? 328  ARG A CZ  1 
ATOM   2422 N  NH1 . ARG A 1 328 ? 8.622   111.612 -14.068 1.00 73.78 ? 328  ARG A NH1 1 
ATOM   2423 N  NH2 . ARG A 1 328 ? 7.846   111.089 -16.153 1.00 71.67 ? 328  ARG A NH2 1 
ATOM   2424 N  N   . LEU A 1 329 ? 4.987   117.754 -19.343 1.00 38.26 ? 329  LEU A N   1 
ATOM   2425 C  CA  . LEU A 1 329 ? 4.102   118.695 -20.080 1.00 39.02 ? 329  LEU A CA  1 
ATOM   2426 C  C   . LEU A 1 329 ? 4.757   119.073 -21.410 1.00 37.09 ? 329  LEU A C   1 
ATOM   2427 O  O   . LEU A 1 329 ? 4.106   118.924 -22.462 1.00 34.41 ? 329  LEU A O   1 
ATOM   2428 C  CB  . LEU A 1 329 ? 3.889   119.947 -19.220 1.00 42.23 ? 329  LEU A CB  1 
ATOM   2429 C  CG  . LEU A 1 329 ? 2.468   120.491 -19.162 1.00 44.63 ? 329  LEU A CG  1 
ATOM   2430 C  CD1 . LEU A 1 329 ? 1.531   119.474 -18.531 1.00 46.74 ? 329  LEU A CD1 1 
ATOM   2431 C  CD2 . LEU A 1 329 ? 2.437   121.805 -18.387 1.00 44.91 ? 329  LEU A CD2 1 
ATOM   2432 N  N   . ALA A 1 330 ? 6.003   119.547 -21.341 1.00 35.62 ? 330  ALA A N   1 
ATOM   2433 C  CA  . ALA A 1 330 ? 6.742   120.173 -22.462 1.00 36.85 ? 330  ALA A CA  1 
ATOM   2434 C  C   . ALA A 1 330 ? 6.956   119.175 -23.610 1.00 38.42 ? 330  ALA A C   1 
ATOM   2435 O  O   . ALA A 1 330 ? 6.993   119.619 -24.776 1.00 35.72 ? 330  ALA A O   1 
ATOM   2436 C  CB  . ALA A 1 330 ? 8.051   120.727 -21.964 1.00 36.67 ? 330  ALA A CB  1 
ATOM   2437 N  N   . ALA A 1 331 ? 7.108   117.886 -23.300 1.00 38.43 ? 331  ALA A N   1 
ATOM   2438 C  CA  . ALA A 1 331 ? 7.347   116.818 -24.299 1.00 41.46 ? 331  ALA A CA  1 
ATOM   2439 C  C   . ALA A 1 331 ? 6.215   116.801 -25.339 1.00 43.78 ? 331  ALA A C   1 
ATOM   2440 O  O   . ALA A 1 331 ? 6.486   116.418 -26.487 1.00 44.10 ? 331  ALA A O   1 
ATOM   2441 C  CB  . ALA A 1 331 ? 7.487   115.486 -23.605 1.00 42.58 ? 331  ALA A CB  1 
ATOM   2442 N  N   . HIS A 1 332 ? 5.002   117.217 -24.959 1.00 46.21 ? 332  HIS A N   1 
ATOM   2443 C  CA  . HIS A 1 332 ? 3.783   117.179 -25.816 1.00 48.09 ? 332  HIS A CA  1 
ATOM   2444 C  C   . HIS A 1 332 ? 3.533   118.528 -26.495 1.00 46.89 ? 332  HIS A C   1 
ATOM   2445 O  O   . HIS A 1 332 ? 2.439   118.680 -27.066 1.00 46.83 ? 332  HIS A O   1 
ATOM   2446 C  CB  . HIS A 1 332 ? 2.562   116.755 -24.993 1.00 52.25 ? 332  HIS A CB  1 
ATOM   2447 C  CG  . HIS A 1 332 ? 2.649   115.355 -24.494 1.00 60.06 ? 332  HIS A CG  1 
ATOM   2448 N  ND1 . HIS A 1 332 ? 2.812   115.060 -23.154 1.00 65.25 ? 332  HIS A ND1 1 
ATOM   2449 C  CD2 . HIS A 1 332 ? 2.620   114.171 -25.148 1.00 64.33 ? 332  HIS A CD2 1 
ATOM   2450 C  CE1 . HIS A 1 332 ? 2.865   113.751 -22.999 1.00 67.28 ? 332  HIS A CE1 1 
ATOM   2451 N  NE2 . HIS A 1 332 ? 2.749   113.181 -24.210 1.00 67.68 ? 332  HIS A NE2 1 
ATOM   2452 N  N   . HIS A 1 333 ? 4.498   119.456 -26.445 1.00 42.69 ? 333  HIS A N   1 
ATOM   2453 C  CA  . HIS A 1 333 ? 4.381   120.825 -27.015 1.00 42.42 ? 333  HIS A CA  1 
ATOM   2454 C  C   . HIS A 1 333 ? 5.442   121.037 -28.101 1.00 43.25 ? 333  HIS A C   1 
ATOM   2455 O  O   . HIS A 1 333 ? 6.634   120.880 -27.798 1.00 47.35 ? 333  HIS A O   1 
ATOM   2456 C  CB  . HIS A 1 333 ? 4.480   121.885 -25.906 1.00 39.27 ? 333  HIS A CB  1 
ATOM   2457 C  CG  . HIS A 1 333 ? 3.232   122.042 -25.105 1.00 35.92 ? 333  HIS A CG  1 
ATOM   2458 N  ND1 . HIS A 1 333 ? 2.299   123.020 -25.371 1.00 36.76 ? 333  HIS A ND1 1 
ATOM   2459 C  CD2 . HIS A 1 333 ? 2.758   121.353 -24.049 1.00 37.08 ? 333  HIS A CD2 1 
ATOM   2460 C  CE1 . HIS A 1 333 ? 1.303   122.926 -24.514 1.00 36.44 ? 333  HIS A CE1 1 
ATOM   2461 N  NE2 . HIS A 1 333 ? 1.557   121.905 -23.695 1.00 36.17 ? 333  HIS A NE2 1 
ATOM   2462 N  N   . ALA A 1 334 ? 5.016   121.430 -29.302 1.00 45.29 ? 334  ALA A N   1 
ATOM   2463 C  CA  . ALA A 1 334 ? 5.891   121.749 -30.458 1.00 45.15 ? 334  ALA A CA  1 
ATOM   2464 C  C   . ALA A 1 334 ? 6.461   123.164 -30.314 1.00 43.72 ? 334  ALA A C   1 
ATOM   2465 O  O   . ALA A 1 334 ? 7.565   123.408 -30.832 1.00 47.72 ? 334  ALA A O   1 
ATOM   2466 C  CB  . ALA A 1 334 ? 5.123   121.607 -31.749 1.00 46.32 ? 334  ALA A CB  1 
ATOM   2467 N  N   . ASN A 1 335 ? 5.732   124.066 -29.654 1.00 41.00 ? 335  ASN A N   1 
ATOM   2468 C  CA  . ASN A 1 335 ? 6.158   125.477 -29.452 1.00 40.44 ? 335  ASN A CA  1 
ATOM   2469 C  C   . ASN A 1 335 ? 6.492   125.691 -27.969 1.00 38.32 ? 335  ASN A C   1 
ATOM   2470 O  O   . ASN A 1 335 ? 5.552   125.814 -27.166 1.00 36.41 ? 335  ASN A O   1 
ATOM   2471 C  CB  . ASN A 1 335 ? 5.091   126.451 -29.955 1.00 41.83 ? 335  ASN A CB  1 
ATOM   2472 C  CG  . ASN A 1 335 ? 5.583   127.880 -30.006 1.00 44.84 ? 335  ASN A CG  1 
ATOM   2473 O  OD1 . ASN A 1 335 ? 6.645   128.205 -29.466 1.00 45.37 ? 335  ASN A OD1 1 
ATOM   2474 N  ND2 . ASN A 1 335 ? 4.810   128.744 -30.645 1.00 47.05 ? 335  ASN A ND2 1 
ATOM   2475 N  N   . ILE A 1 336 ? 7.786   125.749 -27.641 1.00 36.42 ? 336  ILE A N   1 
ATOM   2476 C  CA  . ILE A 1 336 ? 8.319   125.858 -26.247 1.00 38.57 ? 336  ILE A CA  1 
ATOM   2477 C  C   . ILE A 1 336 ? 8.151   127.295 -25.752 1.00 37.06 ? 336  ILE A C   1 
ATOM   2478 O  O   . ILE A 1 336 ? 7.790   127.462 -24.576 1.00 35.14 ? 336  ILE A O   1 
ATOM   2479 C  CB  . ILE A 1 336 ? 9.793   125.398 -26.170 1.00 40.67 ? 336  ILE A CB  1 
ATOM   2480 C  CG1 . ILE A 1 336 ? 9.927   123.889 -26.397 1.00 39.69 ? 336  ILE A CG1 1 
ATOM   2481 C  CG2 . ILE A 1 336 ? 10.438  125.824 -24.856 1.00 41.28 ? 336  ILE A CG2 1 
ATOM   2482 C  CD1 . ILE A 1 336 ? 9.025   123.051 -25.519 1.00 38.62 ? 336  ILE A CD1 1 
ATOM   2483 N  N   . GLU A 1 337 ? 8.413   128.281 -26.613 1.00 38.89 ? 337  GLU A N   1 
ATOM   2484 C  CA  . GLU A 1 337 ? 8.243   129.724 -26.294 1.00 40.27 ? 337  GLU A CA  1 
ATOM   2485 C  C   . GLU A 1 337 ? 6.800   129.971 -25.842 1.00 37.31 ? 337  GLU A C   1 
ATOM   2486 O  O   . GLU A 1 337 ? 6.614   130.625 -24.804 1.00 34.86 ? 337  GLU A O   1 
ATOM   2487 C  CB  . GLU A 1 337 ? 8.594   130.593 -27.499 1.00 42.16 ? 337  GLU A CB  1 
ATOM   2488 C  CG  . GLU A 1 337 ? 8.606   132.076 -27.178 1.00 46.58 ? 337  GLU A CG  1 
ATOM   2489 C  CD  . GLU A 1 337 ? 9.139   132.980 -28.276 1.00 49.54 ? 337  GLU A CD  1 
ATOM   2490 O  OE1 . GLU A 1 337 ? 8.486   133.997 -28.551 1.00 54.58 ? 337  GLU A OE1 1 
ATOM   2491 O  OE2 . GLU A 1 337 ? 10.215  132.680 -28.837 1.00 55.01 ? 337  GLU A OE2 1 
ATOM   2492 N  N   . GLU A 1 338 ? 5.821   129.442 -26.585 1.00 37.45 ? 338  GLU A N   1 
ATOM   2493 C  CA  . GLU A 1 338 ? 4.374   129.599 -26.275 1.00 37.54 ? 338  GLU A CA  1 
ATOM   2494 C  C   . GLU A 1 338 ? 4.059   128.931 -24.933 1.00 34.76 ? 338  GLU A C   1 
ATOM   2495 O  O   . GLU A 1 338 ? 3.316   129.531 -24.140 1.00 36.61 ? 338  GLU A O   1 
ATOM   2496 C  CB  . GLU A 1 338 ? 3.497   129.003 -27.379 1.00 39.33 ? 338  GLU A CB  1 
ATOM   2497 C  CG  . GLU A 1 338 ? 2.005   129.112 -27.099 1.00 39.63 ? 338  GLU A CG  1 
ATOM   2498 C  CD  . GLU A 1 338 ? 1.127   128.541 -28.204 1.00 41.16 ? 338  GLU A CD  1 
ATOM   2499 O  OE1 . GLU A 1 338 ? 0.904   127.312 -28.215 1.00 43.41 ? 338  GLU A OE1 1 
ATOM   2500 O  OE2 . GLU A 1 338 ? 0.686   129.321 -29.056 1.00 40.52 ? 338  GLU A OE2 1 
ATOM   2501 N  N   . LEU A 1 339 ? 4.583   127.730 -24.689 1.00 32.98 ? 339  LEU A N   1 
ATOM   2502 C  CA  . LEU A 1 339 ? 4.315   127.011 -23.416 1.00 35.08 ? 339  LEU A CA  1 
ATOM   2503 C  C   . LEU A 1 339 ? 4.825   127.855 -22.239 1.00 31.87 ? 339  LEU A C   1 
ATOM   2504 O  O   . LEU A 1 339 ? 4.119   127.909 -21.221 1.00 31.00 ? 339  LEU A O   1 
ATOM   2505 C  CB  . LEU A 1 339 ? 4.971   125.627 -23.416 1.00 35.94 ? 339  LEU A CB  1 
ATOM   2506 C  CG  . LEU A 1 339 ? 4.850   124.869 -22.092 1.00 34.99 ? 339  LEU A CG  1 
ATOM   2507 C  CD1 . LEU A 1 339 ? 3.393   124.686 -21.702 1.00 35.88 ? 339  LEU A CD1 1 
ATOM   2508 C  CD2 . LEU A 1 339 ? 5.560   123.527 -22.171 1.00 36.09 ? 339  LEU A CD2 1 
ATOM   2509 N  N   . LEU A 1 340 ? 5.994   128.482 -22.386 1.00 31.62 ? 340  LEU A N   1 
ATOM   2510 C  CA  . LEU A 1 340 ? 6.645   129.285 -21.314 1.00 34.44 ? 340  LEU A CA  1 
ATOM   2511 C  C   . LEU A 1 340 ? 5.870   130.591 -21.100 1.00 34.07 ? 340  LEU A C   1 
ATOM   2512 O  O   . LEU A 1 340 ? 5.684   130.986 -19.925 1.00 31.25 ? 340  LEU A O   1 
ATOM   2513 C  CB  . LEU A 1 340 ? 8.104   129.571 -21.686 1.00 36.62 ? 340  LEU A CB  1 
ATOM   2514 C  CG  . LEU A 1 340 ? 9.140   128.641 -21.059 1.00 39.44 ? 340  LEU A CG  1 
ATOM   2515 C  CD1 . LEU A 1 340 ? 10.538  129.018 -21.522 1.00 41.30 ? 340  LEU A CD1 1 
ATOM   2516 C  CD2 . LEU A 1 340 ? 9.063   128.676 -19.540 1.00 39.48 ? 340  LEU A CD2 1 
ATOM   2517 N  N   . VAL A 1 341 ? 5.415   131.221 -22.188 1.00 32.57 ? 341  VAL A N   1 
ATOM   2518 C  CA  . VAL A 1 341 ? 4.575   132.453 -22.126 1.00 32.06 ? 341  VAL A CA  1 
ATOM   2519 C  C   . VAL A 1 341 ? 3.309   132.136 -21.321 1.00 30.71 ? 341  VAL A C   1 
ATOM   2520 O  O   . VAL A 1 341 ? 2.913   132.973 -20.506 1.00 31.82 ? 341  VAL A O   1 
ATOM   2521 C  CB  . VAL A 1 341 ? 4.267   133.002 -23.534 1.00 32.84 ? 341  VAL A CB  1 
ATOM   2522 C  CG1 . VAL A 1 341 ? 3.150   134.043 -23.524 1.00 32.63 ? 341  VAL A CG1 1 
ATOM   2523 C  CG2 . VAL A 1 341 ? 5.521   133.570 -24.181 1.00 31.99 ? 341  VAL A CG2 1 
ATOM   2524 N  N   . ASP A 1 342 ? 2.725   130.953 -21.514 1.00 30.21 ? 342  ASP A N   1 
ATOM   2525 C  CA  . ASP A 1 342 ? 1.489   130.525 -20.812 1.00 31.53 ? 342  ASP A CA  1 
ATOM   2526 C  C   . ASP A 1 342 ? 1.789   130.050 -19.385 1.00 30.72 ? 342  ASP A C   1 
ATOM   2527 O  O   . ASP A 1 342 ? 0.847   130.042 -18.580 1.00 28.16 ? 342  ASP A O   1 
ATOM   2528 C  CB  . ASP A 1 342 ? 0.778   129.430 -21.605 1.00 33.53 ? 342  ASP A CB  1 
ATOM   2529 C  CG  . ASP A 1 342 ? 0.295   129.903 -22.967 1.00 37.37 ? 342  ASP A CG  1 
ATOM   2530 O  OD1 . ASP A 1 342 ? 0.043   131.130 -23.114 1.00 38.59 ? 342  ASP A OD1 1 
ATOM   2531 O  OD2 . ASP A 1 342 ? 0.182   129.048 -23.878 1.00 35.61 ? 342  ASP A OD2 1 
ATOM   2532 N  N   . SER A 1 343 ? 3.031   129.644 -19.091 1.00 31.45 ? 343  SER A N   1 
ATOM   2533 C  CA  . SER A 1 343 ? 3.380   128.837 -17.885 1.00 30.59 ? 343  SER A CA  1 
ATOM   2534 C  C   . SER A 1 343 ? 4.228   129.612 -16.870 1.00 28.78 ? 343  SER A C   1 
ATOM   2535 O  O   . SER A 1 343 ? 4.247   129.182 -15.704 1.00 26.94 ? 343  SER A O   1 
ATOM   2536 C  CB  . SER A 1 343 ? 4.100   127.570 -18.287 1.00 31.73 ? 343  SER A CB  1 
ATOM   2537 O  OG  . SER A 1 343 ? 3.239   126.711 -19.018 1.00 34.17 ? 343  SER A OG  1 
ATOM   2538 N  N   . PHE A 1 344 ? 4.950   130.656 -17.290 1.00 27.93 ? 344  PHE A N   1 
ATOM   2539 C  CA  . PHE A 1 344 ? 6.073   131.247 -16.509 1.00 28.78 ? 344  PHE A CA  1 
ATOM   2540 C  C   . PHE A 1 344 ? 5.617   131.656 -15.099 1.00 29.20 ? 344  PHE A C   1 
ATOM   2541 O  O   . PHE A 1 344 ? 6.420   131.500 -14.159 1.00 31.23 ? 344  PHE A O   1 
ATOM   2542 C  CB  . PHE A 1 344 ? 6.719   132.419 -17.252 1.00 28.53 ? 344  PHE A CB  1 
ATOM   2543 C  CG  . PHE A 1 344 ? 5.921   133.694 -17.218 1.00 28.96 ? 344  PHE A CG  1 
ATOM   2544 C  CD1 . PHE A 1 344 ? 4.986   133.967 -18.199 1.00 28.75 ? 344  PHE A CD1 1 
ATOM   2545 C  CD2 . PHE A 1 344 ? 6.107   134.619 -16.203 1.00 28.09 ? 344  PHE A CD2 1 
ATOM   2546 C  CE1 . PHE A 1 344 ? 4.245   135.137 -18.166 1.00 29.06 ? 344  PHE A CE1 1 
ATOM   2547 C  CE2 . PHE A 1 344 ? 5.359   135.784 -16.166 1.00 28.98 ? 344  PHE A CE2 1 
ATOM   2548 C  CZ  . PHE A 1 344 ? 4.432   136.044 -17.150 1.00 29.72 ? 344  PHE A CZ  1 
ATOM   2549 N  N   . GLN A 1 345 ? 4.389   132.164 -14.942 1.00 28.28 ? 345  GLN A N   1 
ATOM   2550 C  CA  . GLN A 1 345 ? 3.875   132.677 -13.641 1.00 28.84 ? 345  GLN A CA  1 
ATOM   2551 C  C   . GLN A 1 345 ? 3.883   131.542 -12.608 1.00 29.18 ? 345  GLN A C   1 
ATOM   2552 O  O   . GLN A 1 345 ? 4.100   131.833 -11.421 1.00 28.43 ? 345  GLN A O   1 
ATOM   2553 C  CB  . GLN A 1 345 ? 2.496   133.335 -13.787 1.00 29.49 ? 345  GLN A CB  1 
ATOM   2554 C  CG  . GLN A 1 345 ? 1.352   132.369 -14.073 1.00 29.84 ? 345  GLN A CG  1 
ATOM   2555 C  CD  . GLN A 1 345 ? 1.282   131.937 -15.519 1.00 30.24 ? 345  GLN A CD  1 
ATOM   2556 O  OE1 . GLN A 1 345 ? 1.638   132.678 -16.434 1.00 31.44 ? 345  GLN A OE1 1 
ATOM   2557 N  NE2 . GLN A 1 345 ? 0.815   130.721 -15.744 1.00 30.58 ? 345  GLN A NE2 1 
ATOM   2558 N  N   . ASP A 1 346 ? 3.699   130.291 -13.040 1.00 28.94 ? 346  ASP A N   1 
ATOM   2559 C  CA  . ASP A 1 346 ? 3.707   129.112 -12.133 1.00 29.23 ? 346  ASP A CA  1 
ATOM   2560 C  C   . ASP A 1 346 ? 5.094   128.934 -11.495 1.00 28.65 ? 346  ASP A C   1 
ATOM   2561 O  O   . ASP A 1 346 ? 5.151   128.397 -10.373 1.00 28.71 ? 346  ASP A O   1 
ATOM   2562 C  CB  . ASP A 1 346 ? 3.264   127.838 -12.853 1.00 31.59 ? 346  ASP A CB  1 
ATOM   2563 C  CG  . ASP A 1 346 ? 1.812   127.836 -13.305 1.00 33.64 ? 346  ASP A CG  1 
ATOM   2564 O  OD1 . ASP A 1 346 ? 1.169   128.909 -13.299 1.00 31.33 ? 346  ASP A OD1 1 
ATOM   2565 O  OD2 . ASP A 1 346 ? 1.333   126.754 -13.667 1.00 40.82 ? 346  ASP A OD2 1 
ATOM   2566 N  N   . PHE A 1 347 ? 6.173   129.385 -12.147 1.00 28.31 ? 347  PHE A N   1 
ATOM   2567 C  CA  . PHE A 1 347 ? 7.563   129.248 -11.623 1.00 29.60 ? 347  PHE A CA  1 
ATOM   2568 C  C   . PHE A 1 347 ? 7.754   130.110 -10.357 1.00 29.88 ? 347  PHE A C   1 
ATOM   2569 O  O   . PHE A 1 347 ? 8.679   129.810 -9.570  1.00 28.56 ? 347  PHE A O   1 
ATOM   2570 C  CB  . PHE A 1 347 ? 8.596   129.556 -12.712 1.00 30.55 ? 347  PHE A CB  1 
ATOM   2571 C  CG  . PHE A 1 347 ? 8.752   128.475 -13.756 1.00 31.34 ? 347  PHE A CG  1 
ATOM   2572 C  CD1 . PHE A 1 347 ? 7.768   128.254 -14.708 1.00 32.58 ? 347  PHE A CD1 1 
ATOM   2573 C  CD2 . PHE A 1 347 ? 9.881   127.670 -13.783 1.00 34.89 ? 347  PHE A CD2 1 
ATOM   2574 C  CE1 . PHE A 1 347 ? 7.910   127.259 -15.664 1.00 33.96 ? 347  PHE A CE1 1 
ATOM   2575 C  CE2 . PHE A 1 347 ? 10.029  126.681 -14.747 1.00 35.62 ? 347  PHE A CE2 1 
ATOM   2576 C  CZ  . PHE A 1 347 ? 9.042   126.477 -15.686 1.00 35.25 ? 347  PHE A CZ  1 
ATOM   2577 N  N   . ALA A 1 348 ? 6.885   131.105 -10.122 1.00 29.11 ? 348  ALA A N   1 
ATOM   2578 C  CA  . ALA A 1 348 ? 6.875   131.936 -8.888  1.00 29.99 ? 348  ALA A CA  1 
ATOM   2579 C  C   . ALA A 1 348 ? 6.658   131.061 -7.650  1.00 29.76 ? 348  ALA A C   1 
ATOM   2580 O  O   . ALA A 1 348 ? 7.061   131.487 -6.562  1.00 32.20 ? 348  ALA A O   1 
ATOM   2581 C  CB  . ALA A 1 348 ? 5.813   133.006 -8.966  1.00 29.72 ? 348  ALA A CB  1 
ATOM   2582 N  N   . ASP A 1 349 ? 6.038   129.889 -7.805  1.00 31.09 ? 349  ASP A N   1 
ATOM   2583 C  CA  . ASP A 1 349 ? 5.758   128.957 -6.683  1.00 33.38 ? 349  ASP A CA  1 
ATOM   2584 C  C   . ASP A 1 349 ? 7.032   128.203 -6.253  1.00 33.34 ? 349  ASP A C   1 
ATOM   2585 O  O   . ASP A 1 349 ? 6.987   127.585 -5.170  1.00 33.04 ? 349  ASP A O   1 
ATOM   2586 C  CB  . ASP A 1 349 ? 4.630   127.993 -7.059  1.00 38.48 ? 349  ASP A CB  1 
ATOM   2587 C  CG  . ASP A 1 349 ? 3.972   127.331 -5.860  1.00 44.65 ? 349  ASP A CG  1 
ATOM   2588 O  OD1 . ASP A 1 349 ? 3.691   128.053 -4.874  1.00 48.96 ? 349  ASP A OD1 1 
ATOM   2589 O  OD2 . ASP A 1 349 ? 3.755   126.098 -5.913  1.00 48.06 ? 349  ASP A OD2 1 
ATOM   2590 N  N   . LEU A 1 350 ? 8.124   128.242 -7.031  1.00 30.07 ? 350  LEU A N   1 
ATOM   2591 C  CA  . LEU A 1 350 ? 9.364   127.461 -6.740  1.00 30.49 ? 350  LEU A CA  1 
ATOM   2592 C  C   . LEU A 1 350 ? 10.088  128.023 -5.505  1.00 29.61 ? 350  LEU A C   1 
ATOM   2593 O  O   . LEU A 1 350 ? 10.692  127.230 -4.773  1.00 29.42 ? 350  LEU A O   1 
ATOM   2594 C  CB  . LEU A 1 350 ? 10.291  127.475 -7.961  1.00 30.83 ? 350  LEU A CB  1 
ATOM   2595 C  CG  . LEU A 1 350 ? 9.780   126.736 -9.203  1.00 32.22 ? 350  LEU A CG  1 
ATOM   2596 C  CD1 . LEU A 1 350 ? 10.812  126.794 -10.316 1.00 33.51 ? 350  LEU A CD1 1 
ATOM   2597 C  CD2 . LEU A 1 350 ? 9.430   125.286 -8.894  1.00 31.85 ? 350  LEU A CD2 1 
ATOM   2598 N  N   . MET A 1 351 ? 10.051  129.342 -5.297  1.00 28.73 ? 351  MET A N   1 
ATOM   2599 C  CA  . MET A 1 351 ? 10.822  130.041 -4.228  1.00 28.11 ? 351  MET A CA  1 
ATOM   2600 C  C   . MET A 1 351 ? 10.118  131.344 -3.863  1.00 27.55 ? 351  MET A C   1 
ATOM   2601 O  O   . MET A 1 351 ? 9.348   131.884 -4.659  1.00 27.58 ? 351  MET A O   1 
ATOM   2602 C  CB  . MET A 1 351 ? 12.252  130.352 -4.681  1.00 29.58 ? 351  MET A CB  1 
ATOM   2603 C  CG  . MET A 1 351 ? 12.337  131.503 -5.667  1.00 29.93 ? 351  MET A CG  1 
ATOM   2604 S  SD  . MET A 1 351 ? 13.991  131.767 -6.338  1.00 32.23 ? 351  MET A SD  1 
ATOM   2605 C  CE  . MET A 1 351 ? 14.114  130.424 -7.516  1.00 32.31 ? 351  MET A CE  1 
ATOM   2606 N  N   . PRO A 1 352 ? 10.349  131.882 -2.646  1.00 26.81 ? 352  PRO A N   1 
ATOM   2607 C  CA  . PRO A 1 352 ? 9.768   133.168 -2.264  1.00 27.04 ? 352  PRO A CA  1 
ATOM   2608 C  C   . PRO A 1 352 ? 10.201  134.282 -3.231  1.00 26.64 ? 352  PRO A C   1 
ATOM   2609 O  O   . PRO A 1 352 ? 11.405  134.451 -3.487  1.00 25.59 ? 352  PRO A O   1 
ATOM   2610 C  CB  . PRO A 1 352 ? 10.288  133.403 -0.835  1.00 27.44 ? 352  PRO A CB  1 
ATOM   2611 C  CG  . PRO A 1 352 ? 10.663  132.014 -0.330  1.00 27.33 ? 352  PRO A CG  1 
ATOM   2612 C  CD  . PRO A 1 352 ? 11.130  131.263 -1.562  1.00 26.65 ? 352  PRO A CD  1 
ATOM   2613 N  N   . CYS A 1 353 ? 9.219   134.989 -3.784  1.00 25.46 ? 353  CYS A N   1 
ATOM   2614 C  CA  . CYS A 1 353 ? 9.437   136.125 -4.718  1.00 26.57 ? 353  CYS A CA  1 
ATOM   2615 C  C   . CYS A 1 353 ? 8.172   136.976 -4.779  1.00 24.82 ? 353  CYS A C   1 
ATOM   2616 O  O   . CYS A 1 353 ? 7.106   136.464 -4.432  1.00 24.51 ? 353  CYS A O   1 
ATOM   2617 C  CB  . CYS A 1 353 ? 9.836   135.638 -6.106  1.00 27.56 ? 353  CYS A CB  1 
ATOM   2618 S  SG  . CYS A 1 353 ? 8.565   134.654 -6.934  1.00 28.53 ? 353  CYS A SG  1 
ATOM   2619 N  N   . ASP A 1 354 ? 8.308   138.247 -5.149  1.00 24.91 ? 354  ASP A N   1 
ATOM   2620 C  CA  . ASP A 1 354 ? 7.170   139.195 -5.252  1.00 24.47 ? 354  ASP A CA  1 
ATOM   2621 C  C   . ASP A 1 354 ? 6.753   139.335 -6.717  1.00 24.47 ? 354  ASP A C   1 
ATOM   2622 O  O   . ASP A 1 354 ? 5.615   139.777 -6.963  1.00 23.85 ? 354  ASP A O   1 
ATOM   2623 C  CB  . ASP A 1 354 ? 7.533   140.516 -4.579  1.00 26.56 ? 354  ASP A CB  1 
ATOM   2624 C  CG  . ASP A 1 354 ? 7.835   140.324 -3.105  1.00 26.49 ? 354  ASP A CG  1 
ATOM   2625 O  OD1 . ASP A 1 354 ? 7.001   139.713 -2.438  1.00 26.22 ? 354  ASP A OD1 1 
ATOM   2626 O  OD2 . ASP A 1 354 ? 8.932   140.738 -2.653  1.00 27.40 ? 354  ASP A OD2 1 
ATOM   2627 N  N   . GLY A 1 355 ? 7.640   138.969 -7.648  1.00 24.78 ? 355  GLY A N   1 
ATOM   2628 C  CA  . GLY A 1 355 ? 7.364   138.993 -9.097  1.00 25.25 ? 355  GLY A CA  1 
ATOM   2629 C  C   . GLY A 1 355 ? 8.199   137.975 -9.852  1.00 24.04 ? 355  GLY A C   1 
ATOM   2630 O  O   . GLY A 1 355 ? 9.227   137.529 -9.322  1.00 22.30 ? 355  GLY A O   1 
ATOM   2631 N  N   . VAL A 1 356 ? 7.750   137.626 -11.053 1.00 24.20 ? 356  VAL A N   1 
ATOM   2632 C  CA  . VAL A 1 356 ? 8.464   136.725 -11.999 1.00 24.98 ? 356  VAL A CA  1 
ATOM   2633 C  C   . VAL A 1 356 ? 8.185   137.255 -13.397 1.00 26.15 ? 356  VAL A C   1 
ATOM   2634 O  O   . VAL A 1 356 ? 7.107   137.851 -13.591 1.00 26.43 ? 356  VAL A O   1 
ATOM   2635 C  CB  . VAL A 1 356 ? 8.026   135.253 -11.851 1.00 26.28 ? 356  VAL A CB  1 
ATOM   2636 C  CG1 . VAL A 1 356 ? 6.586   135.037 -12.287 1.00 26.70 ? 356  VAL A CG1 1 
ATOM   2637 C  CG2 . VAL A 1 356 ? 8.939   134.308 -12.606 1.00 27.22 ? 356  VAL A CG2 1 
ATOM   2638 N  N   . GLY A 1 357 ? 9.116   137.037 -14.326 1.00 25.51 ? 357  GLY A N   1 
ATOM   2639 C  CA  . GLY A 1 357 ? 8.944   137.469 -15.717 1.00 27.91 ? 357  GLY A CA  1 
ATOM   2640 C  C   . GLY A 1 357 ? 9.762   136.657 -16.697 1.00 27.20 ? 357  GLY A C   1 
ATOM   2641 O  O   . GLY A 1 357 ? 10.769  136.042 -16.300 1.00 25.47 ? 357  GLY A O   1 
ATOM   2642 N  N   . LEU A 1 358 ? 9.334   136.693 -17.952 1.00 27.84 ? 358  LEU A N   1 
ATOM   2643 C  CA  . LEU A 1 358 ? 9.960   135.954 -19.068 1.00 28.81 ? 358  LEU A CA  1 
ATOM   2644 C  C   . LEU A 1 358 ? 10.442  136.973 -20.090 1.00 29.08 ? 358  LEU A C   1 
ATOM   2645 O  O   . LEU A 1 358 ? 9.634   137.817 -20.522 1.00 28.96 ? 358  LEU A O   1 
ATOM   2646 C  CB  . LEU A 1 358 ? 8.935   134.991 -19.670 1.00 30.08 ? 358  LEU A CB  1 
ATOM   2647 C  CG  . LEU A 1 358 ? 9.463   134.103 -20.790 1.00 31.67 ? 358  LEU A CG  1 
ATOM   2648 C  CD1 . LEU A 1 358 ? 10.507  133.123 -20.263 1.00 31.34 ? 358  LEU A CD1 1 
ATOM   2649 C  CD2 . LEU A 1 358 ? 8.313   133.376 -21.471 1.00 31.62 ? 358  LEU A CD2 1 
ATOM   2650 N  N   . TRP A 1 359 ? 11.729  136.908 -20.412 1.00 29.97 ? 359  TRP A N   1 
ATOM   2651 C  CA  . TRP A 1 359 ? 12.399  137.772 -21.413 1.00 30.35 ? 359  TRP A CA  1 
ATOM   2652 C  C   . TRP A 1 359 ? 12.960  136.863 -22.502 1.00 30.88 ? 359  TRP A C   1 
ATOM   2653 O  O   . TRP A 1 359 ? 14.019  136.249 -22.282 1.00 29.30 ? 359  TRP A O   1 
ATOM   2654 C  CB  . TRP A 1 359 ? 13.472  138.615 -20.729 1.00 29.89 ? 359  TRP A CB  1 
ATOM   2655 C  CG  . TRP A 1 359 ? 14.230  139.513 -21.649 1.00 32.09 ? 359  TRP A CG  1 
ATOM   2656 C  CD1 . TRP A 1 359 ? 15.545  139.404 -21.998 1.00 32.78 ? 359  TRP A CD1 1 
ATOM   2657 C  CD2 . TRP A 1 359 ? 13.728  140.681 -22.320 1.00 32.50 ? 359  TRP A CD2 1 
ATOM   2658 N  NE1 . TRP A 1 359 ? 15.898  140.428 -22.832 1.00 32.26 ? 359  TRP A NE1 1 
ATOM   2659 C  CE2 . TRP A 1 359 ? 14.805  141.226 -23.051 1.00 33.45 ? 359  TRP A CE2 1 
ATOM   2660 C  CE3 . TRP A 1 359 ? 12.487  141.325 -22.369 1.00 33.08 ? 359  TRP A CE3 1 
ATOM   2661 C  CZ2 . TRP A 1 359 ? 14.669  142.376 -23.831 1.00 31.91 ? 359  TRP A CZ2 1 
ATOM   2662 C  CZ3 . TRP A 1 359 ? 12.356  142.464 -23.135 1.00 32.06 ? 359  TRP A CZ3 1 
ATOM   2663 C  CH2 . TRP A 1 359 ? 13.433  142.976 -23.858 1.00 31.53 ? 359  TRP A CH2 1 
ATOM   2664 N  N   . VAL A 1 360 ? 12.206  136.705 -23.588 1.00 32.52 ? 360  VAL A N   1 
ATOM   2665 C  CA  . VAL A 1 360 ? 12.540  135.769 -24.698 1.00 34.95 ? 360  VAL A CA  1 
ATOM   2666 C  C   . VAL A 1 360 ? 12.325  136.509 -26.020 1.00 36.85 ? 360  VAL A C   1 
ATOM   2667 O  O   . VAL A 1 360 ? 11.232  137.074 -26.198 1.00 34.91 ? 360  VAL A O   1 
ATOM   2668 C  CB  . VAL A 1 360 ? 11.699  134.484 -24.604 1.00 35.49 ? 360  VAL A CB  1 
ATOM   2669 C  CG1 . VAL A 1 360 ? 11.858  133.609 -25.840 1.00 37.01 ? 360  VAL A CG1 1 
ATOM   2670 C  CG2 . VAL A 1 360 ? 12.039  133.691 -23.355 1.00 35.56 ? 360  VAL A CG2 1 
ATOM   2671 N  N   . GLY A 1 361 ? 13.338  136.505 -26.893 1.00 39.44 ? 361  GLY A N   1 
ATOM   2672 C  CA  . GLY A 1 361 ? 13.304  137.183 -28.204 1.00 41.39 ? 361  GLY A CA  1 
ATOM   2673 C  C   . GLY A 1 361 ? 12.922  138.650 -28.076 1.00 42.96 ? 361  GLY A C   1 
ATOM   2674 O  O   . GLY A 1 361 ? 12.124  139.119 -28.905 1.00 45.33 ? 361  GLY A O   1 
ATOM   2675 N  N   . ASN A 1 362 ? 13.461  139.337 -27.062 1.00 41.73 ? 362  ASN A N   1 
ATOM   2676 C  CA  . ASN A 1 362 ? 13.212  140.771 -26.752 1.00 43.06 ? 362  ASN A CA  1 
ATOM   2677 C  C   . ASN A 1 362 ? 11.727  141.044 -26.469 1.00 40.28 ? 362  ASN A C   1 
ATOM   2678 O  O   . ASN A 1 362 ? 11.312  142.210 -26.628 1.00 38.98 ? 362  ASN A O   1 
ATOM   2679 C  CB  . ASN A 1 362 ? 13.720  141.679 -27.871 1.00 47.48 ? 362  ASN A CB  1 
ATOM   2680 C  CG  . ASN A 1 362 ? 15.230  141.739 -27.918 1.00 50.99 ? 362  ASN A CG  1 
ATOM   2681 O  OD1 . ASN A 1 362 ? 15.862  142.234 -26.989 1.00 53.00 ? 362  ASN A OD1 1 
ATOM   2682 N  ND2 . ASN A 1 362 ? 15.814  141.248 -28.998 1.00 55.24 ? 362  ASN A ND2 1 
ATOM   2683 N  N   . ASN A 1 363 ? 10.963  140.041 -26.026 1.00 37.40 ? 363  ASN A N   1 
ATOM   2684 C  CA  . ASN A 1 363 ? 9.553   140.227 -25.589 1.00 38.36 ? 363  ASN A CA  1 
ATOM   2685 C  C   . ASN A 1 363 ? 9.460   139.962 -24.085 1.00 36.16 ? 363  ASN A C   1 
ATOM   2686 O  O   . ASN A 1 363 ? 9.997   138.935 -23.632 1.00 32.85 ? 363  ASN A O   1 
ATOM   2687 C  CB  . ASN A 1 363 ? 8.581   139.336 -26.361 1.00 39.60 ? 363  ASN A CB  1 
ATOM   2688 C  CG  . ASN A 1 363 ? 8.542   139.680 -27.833 1.00 43.04 ? 363  ASN A CG  1 
ATOM   2689 O  OD1 . ASN A 1 363 ? 8.386   140.841 -28.195 1.00 47.41 ? 363  ASN A OD1 1 
ATOM   2690 N  ND2 . ASN A 1 363 ? 8.704   138.686 -28.687 1.00 44.40 ? 363  ASN A ND2 1 
ATOM   2691 N  N   . TRP A 1 364 ? 8.759   140.838 -23.366 1.00 33.99 ? 364  TRP A N   1 
ATOM   2692 C  CA  . TRP A 1 364 ? 8.611   140.798 -21.891 1.00 34.09 ? 364  TRP A CA  1 
ATOM   2693 C  C   . TRP A 1 364 ? 7.210   140.309 -21.510 1.00 33.28 ? 364  TRP A C   1 
ATOM   2694 O  O   . TRP A 1 364 ? 6.228   140.812 -22.066 1.00 33.98 ? 364  TRP A O   1 
ATOM   2695 C  CB  . TRP A 1 364 ? 8.897   142.183 -21.303 1.00 34.32 ? 364  TRP A CB  1 
ATOM   2696 C  CG  . TRP A 1 364 ? 8.622   142.295 -19.837 1.00 34.99 ? 364  TRP A CG  1 
ATOM   2697 C  CD1 . TRP A 1 364 ? 7.678   143.073 -19.234 1.00 36.64 ? 364  TRP A CD1 1 
ATOM   2698 C  CD2 . TRP A 1 364 ? 9.307   141.604 -18.779 1.00 35.73 ? 364  TRP A CD2 1 
ATOM   2699 N  NE1 . TRP A 1 364 ? 7.730   142.917 -17.875 1.00 37.72 ? 364  TRP A NE1 1 
ATOM   2700 C  CE2 . TRP A 1 364 ? 8.724   142.030 -17.566 1.00 37.17 ? 364  TRP A CE2 1 
ATOM   2701 C  CE3 . TRP A 1 364 ? 10.362  140.686 -18.737 1.00 36.60 ? 364  TRP A CE3 1 
ATOM   2702 C  CZ2 . TRP A 1 364 ? 9.161   141.563 -16.330 1.00 38.36 ? 364  TRP A CZ2 1 
ATOM   2703 C  CZ3 . TRP A 1 364 ? 10.790  140.220 -17.514 1.00 37.53 ? 364  TRP A CZ3 1 
ATOM   2704 C  CH2 . TRP A 1 364 ? 10.197  140.658 -16.329 1.00 38.15 ? 364  TRP A CH2 1 
ATOM   2705 N  N   . HIS A 1 365 ? 7.136   139.371 -20.571 1.00 32.26 ? 365  HIS A N   1 
ATOM   2706 C  CA  . HIS A 1 365 ? 5.890   138.965 -19.876 1.00 33.18 ? 365  HIS A CA  1 
ATOM   2707 C  C   . HIS A 1 365 ? 6.166   139.014 -18.372 1.00 33.54 ? 365  HIS A C   1 
ATOM   2708 O  O   . HIS A 1 365 ? 7.147   138.375 -17.928 1.00 32.32 ? 365  HIS A O   1 
ATOM   2709 C  CB  . HIS A 1 365 ? 5.423   137.592 -20.377 1.00 35.17 ? 365  HIS A CB  1 
ATOM   2710 C  CG  . HIS A 1 365 ? 5.216   137.551 -21.852 1.00 36.63 ? 365  HIS A CG  1 
ATOM   2711 N  ND1 . HIS A 1 365 ? 6.216   137.173 -22.726 1.00 39.73 ? 365  HIS A ND1 1 
ATOM   2712 C  CD2 . HIS A 1 365 ? 4.145   137.871 -22.610 1.00 38.13 ? 365  HIS A CD2 1 
ATOM   2713 C  CE1 . HIS A 1 365 ? 5.763   137.254 -23.963 1.00 38.24 ? 365  HIS A CE1 1 
ATOM   2714 N  NE2 . HIS A 1 365 ? 4.498   137.680 -23.914 1.00 37.74 ? 365  HIS A NE2 1 
ATOM   2715 N  N   . GLY A 1 366 ? 5.354   139.773 -17.636 1.00 31.49 ? 366  GLY A N   1 
ATOM   2716 C  CA  . GLY A 1 366 ? 5.530   140.014 -16.196 1.00 31.54 ? 366  GLY A CA  1 
ATOM   2717 C  C   . GLY A 1 366 ? 4.358   139.482 -15.406 1.00 32.68 ? 366  GLY A C   1 
ATOM   2718 O  O   . GLY A 1 366 ? 3.241   139.438 -15.959 1.00 32.62 ? 366  GLY A O   1 
ATOM   2719 N  N   . HIS A 1 367 ? 4.611   139.055 -14.168 1.00 31.53 ? 367  HIS A N   1 
ATOM   2720 C  CA  . HIS A 1 367 ? 3.567   138.672 -13.185 1.00 31.23 ? 367  HIS A CA  1 
ATOM   2721 C  C   . HIS A 1 367 ? 3.980   139.173 -11.799 1.00 29.37 ? 367  HIS A C   1 
ATOM   2722 O  O   . HIS A 1 367 ? 5.144   138.946 -11.413 1.00 25.93 ? 367  HIS A O   1 
ATOM   2723 C  CB  . HIS A 1 367 ? 3.327   137.157 -13.208 1.00 34.17 ? 367  HIS A CB  1 
ATOM   2724 C  CG  . HIS A 1 367 ? 2.292   136.697 -12.236 1.00 36.50 ? 367  HIS A CG  1 
ATOM   2725 N  ND1 . HIS A 1 367 ? 0.942   136.900 -12.450 1.00 40.16 ? 367  HIS A ND1 1 
ATOM   2726 C  CD2 . HIS A 1 367 ? 2.400   136.046 -11.056 1.00 39.57 ? 367  HIS A CD2 1 
ATOM   2727 C  CE1 . HIS A 1 367 ? 0.259   136.395 -11.442 1.00 41.75 ? 367  HIS A CE1 1 
ATOM   2728 N  NE2 . HIS A 1 367 ? 1.132   135.863 -10.572 1.00 41.60 ? 367  HIS A NE2 1 
ATOM   2729 N  N   . GLY A 1 368 ? 3.048   139.815 -11.086 1.00 27.61 ? 368  GLY A N   1 
ATOM   2730 C  CA  . GLY A 1 368 ? 3.283   140.406 -9.760  1.00 27.04 ? 368  GLY A CA  1 
ATOM   2731 C  C   . GLY A 1 368 ? 4.155   141.644 -9.849  1.00 27.58 ? 368  GLY A C   1 
ATOM   2732 O  O   . GLY A 1 368 ? 4.049   142.379 -10.849 1.00 29.33 ? 368  GLY A O   1 
ATOM   2733 N  N   . ALA A 1 369 ? 5.005   141.853 -8.842  1.00 28.49 ? 369  ALA A N   1 
ATOM   2734 C  CA  . ALA A 1 369 ? 5.875   143.041 -8.690  1.00 29.13 ? 369  ALA A CA  1 
ATOM   2735 C  C   . ALA A 1 369 ? 7.153   142.844 -9.516  1.00 28.95 ? 369  ALA A C   1 
ATOM   2736 O  O   . ALA A 1 369 ? 8.030   142.054 -9.104  1.00 29.04 ? 369  ALA A O   1 
ATOM   2737 C  CB  . ALA A 1 369 ? 6.173   143.280 -7.227  1.00 28.91 ? 369  ALA A CB  1 
ATOM   2738 N  N   . THR A 1 370 ? 7.247   143.551 -10.641 1.00 28.52 ? 370  THR A N   1 
ATOM   2739 C  CA  . THR A 1 370 ? 8.423   143.518 -11.548 1.00 31.07 ? 370  THR A CA  1 
ATOM   2740 C  C   . THR A 1 370 ? 8.825   144.939 -11.927 1.00 32.47 ? 370  THR A C   1 
ATOM   2741 O  O   . THR A 1 370 ? 8.029   145.867 -11.817 1.00 32.30 ? 370  THR A O   1 
ATOM   2742 C  CB  . THR A 1 370 ? 8.129   142.719 -12.826 1.00 32.37 ? 370  THR A CB  1 
ATOM   2743 O  OG1 . THR A 1 370 ? 7.270   143.534 -13.626 1.00 32.71 ? 370  THR A OG1 1 
ATOM   2744 C  CG2 . THR A 1 370 ? 7.512   141.358 -12.573 1.00 30.34 ? 370  THR A CG2 1 
ATOM   2745 N  N   . PRO A 1 371 ? 10.063  145.138 -12.429 1.00 33.68 ? 371  PRO A N   1 
ATOM   2746 C  CA  . PRO A 1 371 ? 10.415  146.384 -13.103 1.00 35.59 ? 371  PRO A CA  1 
ATOM   2747 C  C   . PRO A 1 371 ? 9.496   146.559 -14.307 1.00 36.32 ? 371  PRO A C   1 
ATOM   2748 O  O   . PRO A 1 371 ? 8.938   145.579 -14.789 1.00 33.98 ? 371  PRO A O   1 
ATOM   2749 C  CB  . PRO A 1 371 ? 11.870  146.191 -13.549 1.00 34.55 ? 371  PRO A CB  1 
ATOM   2750 C  CG  . PRO A 1 371 ? 12.382  145.017 -12.737 1.00 34.04 ? 371  PRO A CG  1 
ATOM   2751 C  CD  . PRO A 1 371 ? 11.170  144.171 -12.412 1.00 33.68 ? 371  PRO A CD  1 
ATOM   2752 N  N   . PRO A 1 372 ? 9.293   147.793 -14.818 1.00 39.91 ? 372  PRO A N   1 
ATOM   2753 C  CA  . PRO A 1 372 ? 8.482   147.997 -16.021 1.00 43.04 ? 372  PRO A CA  1 
ATOM   2754 C  C   . PRO A 1 372 ? 9.215   147.467 -17.261 1.00 44.19 ? 372  PRO A C   1 
ATOM   2755 O  O   . PRO A 1 372 ? 10.428  147.360 -17.213 1.00 40.17 ? 372  PRO A O   1 
ATOM   2756 C  CB  . PRO A 1 372 ? 8.290   149.521 -16.069 1.00 43.27 ? 372  PRO A CB  1 
ATOM   2757 C  CG  . PRO A 1 372 ? 9.519   150.064 -15.363 1.00 41.57 ? 372  PRO A CG  1 
ATOM   2758 C  CD  . PRO A 1 372 ? 9.829   149.052 -14.277 1.00 40.24 ? 372  PRO A CD  1 
ATOM   2759 N  N   . HIS A 1 373 ? 8.475   147.146 -18.329 1.00 49.93 ? 373  HIS A N   1 
ATOM   2760 C  CA  . HIS A 1 373 ? 9.023   146.551 -19.584 1.00 52.56 ? 373  HIS A CA  1 
ATOM   2761 C  C   . HIS A 1 373 ? 10.224  147.378 -20.070 1.00 48.59 ? 373  HIS A C   1 
ATOM   2762 O  O   . HIS A 1 373 ? 11.216  146.764 -20.501 1.00 49.65 ? 373  HIS A O   1 
ATOM   2763 C  CB  . HIS A 1 373 ? 7.923   146.393 -20.650 1.00 58.74 ? 373  HIS A CB  1 
ATOM   2764 C  CG  . HIS A 1 373 ? 7.678   147.611 -21.476 1.00 63.84 ? 373  HIS A CG  1 
ATOM   2765 N  ND1 . HIS A 1 373 ? 7.113   148.761 -20.951 1.00 66.78 ? 373  HIS A ND1 1 
ATOM   2766 C  CD2 . HIS A 1 373 ? 7.922   147.866 -22.781 1.00 67.09 ? 373  HIS A CD2 1 
ATOM   2767 C  CE1 . HIS A 1 373 ? 7.023   149.674 -21.898 1.00 67.02 ? 373  HIS A CE1 1 
ATOM   2768 N  NE2 . HIS A 1 373 ? 7.510   149.148 -23.033 1.00 67.71 ? 373  HIS A NE2 1 
ATOM   2769 N  N   . ASP A 1 374 ? 10.148  148.708 -19.942 1.00 48.71 ? 374  ASP A N   1 
ATOM   2770 C  CA  . ASP A 1 374 ? 11.184  149.695 -20.368 1.00 48.53 ? 374  ASP A CA  1 
ATOM   2771 C  C   . ASP A 1 374 ? 12.547  149.384 -19.727 1.00 47.62 ? 374  ASP A C   1 
ATOM   2772 O  O   . ASP A 1 374 ? 13.583  149.708 -20.358 1.00 47.33 ? 374  ASP A O   1 
ATOM   2773 C  CB  . ASP A 1 374 ? 10.742  151.120 -20.018 1.00 48.80 ? 374  ASP A CB  1 
ATOM   2774 N  N   . ALA A 1 375 ? 12.552  148.789 -18.527 1.00 43.36 ? 375  ALA A N   1 
ATOM   2775 C  CA  . ALA A 1 375 ? 13.754  148.559 -17.685 1.00 41.98 ? 375  ALA A CA  1 
ATOM   2776 C  C   . ALA A 1 375 ? 14.452  147.235 -18.026 1.00 41.27 ? 375  ALA A C   1 
ATOM   2777 O  O   . ALA A 1 375 ? 15.646  147.100 -17.696 1.00 42.86 ? 375  ALA A O   1 
ATOM   2778 C  CB  . ALA A 1 375 ? 13.354  148.589 -16.229 1.00 42.15 ? 375  ALA A CB  1 
ATOM   2779 N  N   . ILE A 1 376 ? 13.749  146.281 -18.643 1.00 41.46 ? 376  ILE A N   1 
ATOM   2780 C  CA  . ILE A 1 376 ? 14.205  144.856 -18.739 1.00 41.81 ? 376  ILE A CA  1 
ATOM   2781 C  C   . ILE A 1 376 ? 15.428  144.725 -19.653 1.00 41.97 ? 376  ILE A C   1 
ATOM   2782 O  O   . ILE A 1 376 ? 16.349  143.971 -19.332 1.00 42.28 ? 376  ILE A O   1 
ATOM   2783 C  CB  . ILE A 1 376 ? 13.039  143.931 -19.157 1.00 41.58 ? 376  ILE A CB  1 
ATOM   2784 C  CG1 . ILE A 1 376 ? 11.825  144.088 -18.236 1.00 41.60 ? 376  ILE A CG1 1 
ATOM   2785 C  CG2 . ILE A 1 376 ? 13.494  142.482 -19.239 1.00 42.53 ? 376  ILE A CG2 1 
ATOM   2786 C  CD1 . ILE A 1 376 ? 12.132  143.948 -16.756 1.00 42.10 ? 376  ILE A CD1 1 
ATOM   2787 N  N   . PRO A 1 377 ? 15.502  145.412 -20.819 1.00 44.35 ? 377  PRO A N   1 
ATOM   2788 C  CA  . PRO A 1 377 ? 16.681  145.308 -21.686 1.00 44.27 ? 377  PRO A CA  1 
ATOM   2789 C  C   . PRO A 1 377 ? 18.014  145.540 -20.961 1.00 44.51 ? 377  PRO A C   1 
ATOM   2790 O  O   . PRO A 1 377 ? 18.934  144.766 -21.174 1.00 45.85 ? 377  PRO A O   1 
ATOM   2791 C  CB  . PRO A 1 377 ? 16.449  146.409 -22.729 1.00 45.46 ? 377  PRO A CB  1 
ATOM   2792 C  CG  . PRO A 1 377 ? 14.941  146.507 -22.816 1.00 45.67 ? 377  PRO A CG  1 
ATOM   2793 C  CD  . PRO A 1 377 ? 14.455  146.270 -21.400 1.00 44.23 ? 377  PRO A CD  1 
ATOM   2794 N  N   . ARG A 1 378 ? 18.064  146.571 -20.112 1.00 45.19 ? 378  ARG A N   1 
ATOM   2795 C  CA  . ARG A 1 378 ? 19.266  146.969 -19.319 1.00 45.24 ? 378  ARG A CA  1 
ATOM   2796 C  C   . ARG A 1 378 ? 19.650  145.849 -18.343 1.00 43.39 ? 378  ARG A C   1 
ATOM   2797 O  O   . ARG A 1 378 ? 20.866  145.543 -18.229 1.00 44.55 ? 378  ARG A O   1 
ATOM   2798 C  CB  . ARG A 1 378 ? 18.969  148.264 -18.555 1.00 50.24 ? 378  ARG A CB  1 
ATOM   2799 C  CG  . ARG A 1 378 ? 20.094  148.742 -17.650 1.00 53.68 ? 378  ARG A CG  1 
ATOM   2800 C  CD  . ARG A 1 378 ? 21.212  149.419 -18.420 1.00 58.30 ? 378  ARG A CD  1 
ATOM   2801 N  NE  . ARG A 1 378 ? 22.117  150.107 -17.506 1.00 64.51 ? 378  ARG A NE  1 
ATOM   2802 C  CZ  . ARG A 1 378 ? 23.250  149.611 -17.004 1.00 66.66 ? 378  ARG A CZ  1 
ATOM   2803 N  NH1 . ARG A 1 378 ? 23.673  148.400 -17.335 1.00 68.36 ? 378  ARG A NH1 1 
ATOM   2804 N  NH2 . ARG A 1 378 ? 23.969  150.345 -16.172 1.00 66.98 ? 378  ARG A NH2 1 
ATOM   2805 N  N   . LEU A 1 379 ? 18.662  145.269 -17.655 1.00 40.34 ? 379  LEU A N   1 
ATOM   2806 C  CA  . LEU A 1 379 ? 18.875  144.138 -16.713 1.00 40.95 ? 379  LEU A CA  1 
ATOM   2807 C  C   . LEU A 1 379 ? 19.406  142.936 -17.503 1.00 41.22 ? 379  LEU A C   1 
ATOM   2808 O  O   . LEU A 1 379 ? 20.458  142.395 -17.111 1.00 38.13 ? 379  LEU A O   1 
ATOM   2809 C  CB  . LEU A 1 379 ? 17.565  143.799 -15.991 1.00 40.08 ? 379  LEU A CB  1 
ATOM   2810 C  CG  . LEU A 1 379 ? 17.042  144.866 -15.030 1.00 39.35 ? 379  LEU A CG  1 
ATOM   2811 C  CD1 . LEU A 1 379 ? 15.632  144.531 -14.564 1.00 40.18 ? 379  LEU A CD1 1 
ATOM   2812 C  CD2 . LEU A 1 379 ? 17.966  145.027 -13.839 1.00 39.27 ? 379  LEU A CD2 1 
ATOM   2813 N  N   . ALA A 1 380 ? 18.714  142.548 -18.579 1.00 41.26 ? 380  ALA A N   1 
ATOM   2814 C  CA  . ALA A 1 380 ? 19.112  141.421 -19.459 1.00 42.89 ? 380  ALA A CA  1 
ATOM   2815 C  C   . ALA A 1 380 ? 20.567  141.618 -19.906 1.00 44.77 ? 380  ALA A C   1 
ATOM   2816 O  O   . ALA A 1 380 ? 21.379  140.675 -19.742 1.00 44.03 ? 380  ALA A O   1 
ATOM   2817 C  CB  . ALA A 1 380 ? 18.177  141.329 -20.643 1.00 43.91 ? 380  ALA A CB  1 
ATOM   2818 N  N   . ARG A 1 381 ? 20.874  142.811 -20.434 1.00 45.52 ? 381  ARG A N   1 
ATOM   2819 C  CA  . ARG A 1 381 ? 22.246  143.230 -20.850 1.00 43.68 ? 381  ARG A CA  1 
ATOM   2820 C  C   . ARG A 1 381 ? 23.233  142.980 -19.704 1.00 44.84 ? 381  ARG A C   1 
ATOM   2821 O  O   . ARG A 1 381 ? 24.263  142.317 -19.937 1.00 45.11 ? 381  ARG A O   1 
ATOM   2822 C  CB  . ARG A 1 381 ? 22.269  144.707 -21.259 1.00 44.13 ? 381  ARG A CB  1 
ATOM   2823 N  N   . PHE A 1 382 ? 22.930  143.477 -18.501 1.00 44.38 ? 382  PHE A N   1 
ATOM   2824 C  CA  . PHE A 1 382 ? 23.857  143.407 -17.341 1.00 43.98 ? 382  PHE A CA  1 
ATOM   2825 C  C   . PHE A 1 382 ? 24.118  141.947 -16.946 1.00 44.08 ? 382  PHE A C   1 
ATOM   2826 O  O   . PHE A 1 382 ? 25.280  141.612 -16.645 1.00 43.80 ? 382  PHE A O   1 
ATOM   2827 C  CB  . PHE A 1 382 ? 23.342  144.201 -16.140 1.00 46.39 ? 382  PHE A CB  1 
ATOM   2828 C  CG  . PHE A 1 382 ? 24.368  144.280 -15.041 1.00 48.92 ? 382  PHE A CG  1 
ATOM   2829 C  CD1 . PHE A 1 382 ? 24.430  143.307 -14.055 1.00 48.14 ? 382  PHE A CD1 1 
ATOM   2830 C  CD2 . PHE A 1 382 ? 25.327  145.281 -15.042 1.00 50.82 ? 382  PHE A CD2 1 
ATOM   2831 C  CE1 . PHE A 1 382 ? 25.404  143.356 -13.071 1.00 50.40 ? 382  PHE A CE1 1 
ATOM   2832 C  CE2 . PHE A 1 382 ? 26.301  145.328 -14.056 1.00 50.96 ? 382  PHE A CE2 1 
ATOM   2833 C  CZ  . PHE A 1 382 ? 26.336  144.368 -13.071 1.00 50.89 ? 382  PHE A CZ  1 
ATOM   2834 N  N   . VAL A 1 383 ? 23.080  141.106 -16.916 1.00 43.22 ? 383  VAL A N   1 
ATOM   2835 C  CA  . VAL A 1 383 ? 23.227  139.661 -16.561 1.00 45.10 ? 383  VAL A CA  1 
ATOM   2836 C  C   . VAL A 1 383 ? 24.122  138.986 -17.613 1.00 44.87 ? 383  VAL A C   1 
ATOM   2837 O  O   . VAL A 1 383 ? 25.053  138.252 -17.215 1.00 43.54 ? 383  VAL A O   1 
ATOM   2838 C  CB  . VAL A 1 383 ? 21.867  138.950 -16.429 1.00 43.99 ? 383  VAL A CB  1 
ATOM   2839 C  CG1 . VAL A 1 383 ? 22.049  137.455 -16.201 1.00 43.25 ? 383  VAL A CG1 1 
ATOM   2840 C  CG2 . VAL A 1 383 ? 21.018  139.557 -15.319 1.00 43.96 ? 383  VAL A CG2 1 
ATOM   2841 N  N   . ALA A 1 384 ? 23.860  139.239 -18.898 1.00 45.65 ? 384  ALA A N   1 
ATOM   2842 C  CA  . ALA A 1 384 ? 24.648  138.706 -20.037 1.00 50.89 ? 384  ALA A CA  1 
ATOM   2843 C  C   . ALA A 1 384 ? 26.130  139.020 -19.807 1.00 54.17 ? 384  ALA A C   1 
ATOM   2844 O  O   . ALA A 1 384 ? 26.953  138.094 -19.901 1.00 59.39 ? 384  ALA A O   1 
ATOM   2845 C  CB  . ALA A 1 384 ? 24.150  139.275 -21.344 1.00 50.40 ? 384  ALA A CB  1 
ATOM   2846 N  N   . SER A 1 385 ? 26.437  140.274 -19.464 1.00 59.85 ? 385  SER A N   1 
ATOM   2847 C  CA  . SER A 1 385 ? 27.812  140.750 -19.143 1.00 61.80 ? 385  SER A CA  1 
ATOM   2848 C  C   . SER A 1 385 ? 28.327  140.045 -17.880 1.00 64.35 ? 385  SER A C   1 
ATOM   2849 O  O   . SER A 1 385 ? 29.443  139.492 -17.927 1.00 64.36 ? 385  SER A O   1 
ATOM   2850 C  CB  . SER A 1 385 ? 27.846  142.249 -18.991 1.00 62.69 ? 385  SER A CB  1 
ATOM   2851 N  N   . ALA A 1 386 ? 27.528  140.039 -16.807 1.00 65.06 ? 386  ALA A N   1 
ATOM   2852 C  CA  . ALA A 1 386 ? 27.939  139.659 -15.430 1.00 63.60 ? 386  ALA A CA  1 
ATOM   2853 C  C   . ALA A 1 386 ? 28.024  138.135 -15.267 1.00 65.51 ? 386  ALA A C   1 
ATOM   2854 O  O   . ALA A 1 386 ? 28.973  137.670 -14.610 1.00 62.92 ? 386  ALA A O   1 
ATOM   2855 C  CB  . ALA A 1 386 ? 26.982  140.255 -14.426 1.00 63.10 ? 386  ALA A CB  1 
ATOM   2856 N  N   . SER A 1 387 ? 27.060  137.394 -15.822 1.00 68.36 ? 387  SER A N   1 
ATOM   2857 C  CA  . SER A 1 387 ? 26.903  135.923 -15.630 1.00 69.32 ? 387  SER A CA  1 
ATOM   2858 C  C   . SER A 1 387 ? 27.848  135.143 -16.552 1.00 71.76 ? 387  SER A C   1 
ATOM   2859 O  O   . SER A 1 387 ? 28.106  135.608 -17.681 1.00 73.23 ? 387  SER A O   1 
ATOM   2860 C  CB  . SER A 1 387 ? 25.477  135.486 -15.854 1.00 70.24 ? 387  SER A CB  1 
ATOM   2861 O  OG  . SER A 1 387 ? 25.365  134.070 -15.788 1.00 67.55 ? 387  SER A OG  1 
ATOM   2862 N  N   . GLU A 1 388 ? 28.308  133.975 -16.089 1.00 71.63 ? 388  GLU A N   1 
ATOM   2863 C  CA  . GLU A 1 388 ? 29.120  133.004 -16.873 1.00 70.04 ? 388  GLU A CA  1 
ATOM   2864 C  C   . GLU A 1 388 ? 28.232  131.831 -17.310 1.00 66.81 ? 388  GLU A C   1 
ATOM   2865 O  O   . GLU A 1 388 ? 28.714  130.681 -17.252 1.00 69.71 ? 388  GLU A O   1 
ATOM   2866 C  CB  . GLU A 1 388 ? 30.307  132.510 -16.040 1.00 70.96 ? 388  GLU A CB  1 
ATOM   2867 N  N   . GLY A 1 389 ? 26.984  132.116 -17.712 1.00 61.70 ? 389  GLY A N   1 
ATOM   2868 C  CA  . GLY A 1 389 ? 26.004  131.122 -18.202 1.00 56.71 ? 389  GLY A CA  1 
ATOM   2869 C  C   . GLY A 1 389 ? 25.251  130.395 -17.092 1.00 52.13 ? 389  GLY A C   1 
ATOM   2870 O  O   . GLY A 1 389 ? 24.400  129.556 -17.430 1.00 50.46 ? 389  GLY A O   1 
ATOM   2871 N  N   . ARG A 1 390 ? 25.541  130.691 -15.819 1.00 47.93 ? 390  ARG A N   1 
ATOM   2872 C  CA  . ARG A 1 390 ? 24.861  130.061 -14.649 1.00 48.76 ? 390  ARG A CA  1 
ATOM   2873 C  C   . ARG A 1 390 ? 23.863  131.060 -14.036 1.00 42.34 ? 390  ARG A C   1 
ATOM   2874 O  O   . ARG A 1 390 ? 23.727  132.182 -14.564 1.00 38.79 ? 390  ARG A O   1 
ATOM   2875 C  CB  . ARG A 1 390 ? 25.902  129.567 -13.636 1.00 53.85 ? 390  ARG A CB  1 
ATOM   2876 C  CG  . ARG A 1 390 ? 26.563  128.246 -14.016 1.00 57.48 ? 390  ARG A CG  1 
ATOM   2877 C  CD  . ARG A 1 390 ? 25.704  127.036 -13.693 1.00 60.51 ? 390  ARG A CD  1 
ATOM   2878 N  NE  . ARG A 1 390 ? 26.242  125.788 -14.230 1.00 65.40 ? 390  ARG A NE  1 
ATOM   2879 C  CZ  . ARG A 1 390 ? 26.989  124.902 -13.562 1.00 68.07 ? 390  ARG A CZ  1 
ATOM   2880 N  NH1 . ARG A 1 390 ? 27.317  125.102 -12.295 1.00 69.09 ? 390  ARG A NH1 1 
ATOM   2881 N  NH2 . ARG A 1 390 ? 27.412  123.808 -14.173 1.00 67.54 ? 390  ARG A NH2 1 
ATOM   2882 N  N   . VAL A 1 391 ? 23.165  130.654 -12.973 1.00 39.35 ? 391  VAL A N   1 
ATOM   2883 C  CA  . VAL A 1 391 ? 22.203  131.530 -12.243 1.00 37.16 ? 391  VAL A CA  1 
ATOM   2884 C  C   . VAL A 1 391 ? 22.983  132.755 -11.762 1.00 36.44 ? 391  VAL A C   1 
ATOM   2885 O  O   . VAL A 1 391 ? 24.099  132.569 -11.235 1.00 38.07 ? 391  VAL A O   1 
ATOM   2886 C  CB  . VAL A 1 391 ? 21.518  130.788 -11.079 1.00 36.75 ? 391  VAL A CB  1 
ATOM   2887 C  CG1 . VAL A 1 391 ? 20.639  131.708 -10.238 1.00 35.83 ? 391  VAL A CG1 1 
ATOM   2888 C  CG2 . VAL A 1 391 ? 20.710  129.601 -11.576 1.00 36.76 ? 391  VAL A CG2 1 
ATOM   2889 N  N   . TRP A 1 392 ? 22.440  133.954 -11.976 1.00 35.68 ? 392  TRP A N   1 
ATOM   2890 C  CA  . TRP A 1 392 ? 22.979  135.228 -11.426 1.00 34.53 ? 392  TRP A CA  1 
ATOM   2891 C  C   . TRP A 1 392 ? 21.898  135.878 -10.552 1.00 33.85 ? 392  TRP A C   1 
ATOM   2892 O  O   . TRP A 1 392 ? 20.754  135.989 -11.022 1.00 29.71 ? 392  TRP A O   1 
ATOM   2893 C  CB  . TRP A 1 392 ? 23.442  136.164 -12.549 1.00 35.57 ? 392  TRP A CB  1 
ATOM   2894 C  CG  . TRP A 1 392 ? 24.165  137.372 -12.037 1.00 37.33 ? 392  TRP A CG  1 
ATOM   2895 C  CD1 . TRP A 1 392 ? 25.509  137.500 -11.834 1.00 39.42 ? 392  TRP A CD1 1 
ATOM   2896 C  CD2 . TRP A 1 392 ? 23.576  138.614 -11.612 1.00 37.12 ? 392  TRP A CD2 1 
ATOM   2897 N  NE1 . TRP A 1 392 ? 25.798  138.738 -11.326 1.00 39.20 ? 392  TRP A NE1 1 
ATOM   2898 C  CE2 . TRP A 1 392 ? 24.633  139.441 -11.174 1.00 38.17 ? 392  TRP A CE2 1 
ATOM   2899 C  CE3 . TRP A 1 392 ? 22.264  139.099 -11.541 1.00 38.05 ? 392  TRP A CE3 1 
ATOM   2900 C  CZ2 . TRP A 1 392 ? 24.416  140.730 -10.689 1.00 37.83 ? 392  TRP A CZ2 1 
ATOM   2901 C  CZ3 . TRP A 1 392 ? 22.050  140.375 -11.070 1.00 37.92 ? 392  TRP A CZ3 1 
ATOM   2902 C  CH2 . TRP A 1 392 ? 23.115  141.176 -10.649 1.00 38.55 ? 392  TRP A CH2 1 
ATOM   2903 N  N   . ALA A 1 393 ? 22.244  136.303 -9.332  1.00 32.83 ? 393  ALA A N   1 
ATOM   2904 C  CA  . ALA A 1 393 ? 21.274  136.862 -8.363  1.00 31.60 ? 393  ALA A CA  1 
ATOM   2905 C  C   . ALA A 1 393 ? 21.916  137.962 -7.510  1.00 31.74 ? 393  ALA A C   1 
ATOM   2906 O  O   . ALA A 1 393 ? 23.083  137.823 -7.112  1.00 31.54 ? 393  ALA A O   1 
ATOM   2907 C  CB  . ALA A 1 393 ? 20.715  135.750 -7.511  1.00 31.87 ? 393  ALA A CB  1 
ATOM   2908 N  N   . THR A 1 394 ? 21.151  139.017 -7.230  1.00 29.55 ? 394  THR A N   1 
ATOM   2909 C  CA  . THR A 1 394 ? 21.538  140.118 -6.311  1.00 29.43 ? 394  THR A CA  1 
ATOM   2910 C  C   . THR A 1 394 ? 20.322  140.517 -5.479  1.00 27.39 ? 394  THR A C   1 
ATOM   2911 O  O   . THR A 1 394 ? 19.206  140.453 -6.010  1.00 25.69 ? 394  THR A O   1 
ATOM   2912 C  CB  . THR A 1 394 ? 22.057  141.334 -7.084  1.00 30.65 ? 394  THR A CB  1 
ATOM   2913 O  OG1 . THR A 1 394 ? 22.410  142.324 -6.125  1.00 31.68 ? 394  THR A OG1 1 
ATOM   2914 C  CG2 . THR A 1 394 ? 21.046  141.924 -8.042  1.00 31.83 ? 394  THR A CG2 1 
ATOM   2915 N  N   . HIS A 1 395 ? 20.536  140.981 -4.251  1.00 27.44 ? 395  HIS A N   1 
ATOM   2916 C  CA  . HIS A 1 395 ? 19.466  141.584 -3.412  1.00 28.65 ? 395  HIS A CA  1 
ATOM   2917 C  C   . HIS A 1 395 ? 19.598  143.106 -3.403  1.00 28.06 ? 395  HIS A C   1 
ATOM   2918 O  O   . HIS A 1 395 ? 18.897  143.744 -2.608  1.00 28.06 ? 395  HIS A O   1 
ATOM   2919 C  CB  . HIS A 1 395 ? 19.492  141.010 -2.000  1.00 31.00 ? 395  HIS A CB  1 
ATOM   2920 C  CG  . HIS A 1 395 ? 20.804  141.176 -1.319  1.00 33.08 ? 395  HIS A CG  1 
ATOM   2921 N  ND1 . HIS A 1 395 ? 21.801  140.217 -1.398  1.00 36.52 ? 395  HIS A ND1 1 
ATOM   2922 C  CD2 . HIS A 1 395 ? 21.285  142.173 -0.547  1.00 34.47 ? 395  HIS A CD2 1 
ATOM   2923 C  CE1 . HIS A 1 395 ? 22.841  140.621 -0.697  1.00 37.00 ? 395  HIS A CE1 1 
ATOM   2924 N  NE2 . HIS A 1 395 ? 22.548  141.818 -0.170  1.00 37.11 ? 395  HIS A NE2 1 
ATOM   2925 N  N   . ALA A 1 396 ? 20.440  143.671 -4.268  1.00 28.15 ? 396  ALA A N   1 
ATOM   2926 C  CA  . ALA A 1 396 ? 20.739  145.122 -4.283  1.00 30.02 ? 396  ALA A CA  1 
ATOM   2927 C  C   . ALA A 1 396 ? 20.942  145.592 -5.722  1.00 30.79 ? 396  ALA A C   1 
ATOM   2928 O  O   . ALA A 1 396 ? 22.086  145.927 -6.086  1.00 31.12 ? 396  ALA A O   1 
ATOM   2929 C  CB  . ALA A 1 396 ? 21.944  145.404 -3.414  1.00 30.58 ? 396  ALA A CB  1 
ATOM   2930 N  N   . LEU A 1 397 ? 19.852  145.643 -6.491  1.00 32.58 ? 397  LEU A N   1 
ATOM   2931 C  CA  . LEU A 1 397 ? 19.877  145.942 -7.947  1.00 35.74 ? 397  LEU A CA  1 
ATOM   2932 C  C   . LEU A 1 397 ? 20.527  147.305 -8.224  1.00 38.13 ? 397  LEU A C   1 
ATOM   2933 O  O   . LEU A 1 397 ? 21.202  147.414 -9.264  1.00 37.20 ? 397  LEU A O   1 
ATOM   2934 C  CB  . LEU A 1 397 ? 18.453  145.912 -8.503  1.00 36.84 ? 397  LEU A CB  1 
ATOM   2935 C  CG  . LEU A 1 397 ? 18.026  144.586 -9.120  1.00 38.78 ? 397  LEU A CG  1 
ATOM   2936 C  CD1 . LEU A 1 397 ? 16.531  144.581 -9.409  1.00 39.45 ? 397  LEU A CD1 1 
ATOM   2937 C  CD2 . LEU A 1 397 ? 18.820  144.294 -10.386 1.00 39.27 ? 397  LEU A CD2 1 
ATOM   2938 N  N   . SER A 1 398 ? 20.310  148.304 -7.362  1.00 39.30 ? 398  SER A N   1 
ATOM   2939 C  CA  A SER A 1 398 ? 20.791  149.702 -7.564  0.38 40.56 ? 398  SER A CA  1 
ATOM   2940 C  CA  B SER A 1 398 ? 20.789  149.699 -7.584  0.62 40.11 ? 398  SER A CA  1 
ATOM   2941 C  C   . SER A 1 398 ? 22.323  149.758 -7.532  1.00 41.03 ? 398  SER A C   1 
ATOM   2942 O  O   . SER A 1 398 ? 22.889  150.641 -8.190  1.00 46.71 ? 398  SER A O   1 
ATOM   2943 C  CB  A SER A 1 398 ? 20.194  150.644 -6.547  0.38 39.34 ? 398  SER A CB  1 
ATOM   2944 C  CB  B SER A 1 398 ? 20.165  150.662 -6.610  0.62 37.96 ? 398  SER A CB  1 
ATOM   2945 O  OG  A SER A 1 398 ? 18.829  150.898 -6.838  0.38 38.50 ? 398  SER A OG  1 
ATOM   2946 O  OG  B SER A 1 398 ? 20.616  150.406 -5.293  0.62 35.54 ? 398  SER A OG  1 
ATOM   2947 N  N   . GLN A 1 399 ? 22.956  148.853 -6.786  1.00 43.83 ? 399  GLN A N   1 
ATOM   2948 C  CA  . GLN A 1 399 ? 24.438  148.767 -6.677  1.00 44.74 ? 399  GLN A CA  1 
ATOM   2949 C  C   . GLN A 1 399 ? 25.042  148.254 -7.990  1.00 48.05 ? 399  GLN A C   1 
ATOM   2950 O  O   . GLN A 1 399 ? 26.204  148.590 -8.276  1.00 49.95 ? 399  GLN A O   1 
ATOM   2951 C  CB  . GLN A 1 399 ? 24.840  147.849 -5.527  1.00 46.03 ? 399  GLN A CB  1 
ATOM   2952 C  CG  . GLN A 1 399 ? 24.471  148.402 -4.162  1.00 47.45 ? 399  GLN A CG  1 
ATOM   2953 C  CD  . GLN A 1 399 ? 25.133  147.622 -3.055  1.00 49.26 ? 399  GLN A CD  1 
ATOM   2954 O  OE1 . GLN A 1 399 ? 26.171  146.993 -3.246  1.00 54.01 ? 399  GLN A OE1 1 
ATOM   2955 N  NE2 . GLN A 1 399 ? 24.529  147.653 -1.879  1.00 50.98 ? 399  GLN A NE2 1 
ATOM   2956 N  N   . ALA A 1 400 ? 24.294  147.453 -8.750  1.00 47.66 ? 400  ALA A N   1 
ATOM   2957 C  CA  . ALA A 1 400 ? 24.719  146.915 -10.062 1.00 46.22 ? 400  ALA A CA  1 
ATOM   2958 C  C   . ALA A 1 400 ? 24.313  147.888 -11.172 1.00 46.76 ? 400  ALA A C   1 
ATOM   2959 O  O   . ALA A 1 400 ? 25.082  148.045 -12.128 1.00 49.24 ? 400  ALA A O   1 
ATOM   2960 C  CB  . ALA A 1 400 ? 24.121  145.549 -10.275 1.00 46.82 ? 400  ALA A CB  1 
ATOM   2961 N  N   . ILE A 1 401 ? 23.138  148.504 -11.039 1.00 48.40 ? 401  ILE A N   1 
ATOM   2962 C  CA  . ILE A 1 401 ? 22.478  149.319 -12.099 1.00 49.42 ? 401  ILE A CA  1 
ATOM   2963 C  C   . ILE A 1 401 ? 21.814  150.522 -11.437 1.00 49.23 ? 401  ILE A C   1 
ATOM   2964 O  O   . ILE A 1 401 ? 20.635  150.473 -11.099 1.00 47.66 ? 401  ILE A O   1 
ATOM   2965 C  CB  . ILE A 1 401 ? 21.476  148.451 -12.888 1.00 50.31 ? 401  ILE A CB  1 
ATOM   2966 C  CG1 . ILE A 1 401 ? 22.161  147.221 -13.488 1.00 52.53 ? 401  ILE A CG1 1 
ATOM   2967 C  CG2 . ILE A 1 401 ? 20.756  149.272 -13.951 1.00 49.57 ? 401  ILE A CG2 1 
ATOM   2968 C  CD1 . ILE A 1 401 ? 21.211  146.128 -13.901 1.00 54.84 ? 401  ILE A CD1 1 
ATOM   2969 N  N   . PRO A 1 402 ? 22.555  151.634 -11.224 1.00 51.95 ? 402  PRO A N   1 
ATOM   2970 C  CA  . PRO A 1 402 ? 22.007  152.834 -10.585 1.00 51.56 ? 402  PRO A CA  1 
ATOM   2971 C  C   . PRO A 1 402 ? 20.575  153.223 -10.985 1.00 52.58 ? 402  PRO A C   1 
ATOM   2972 O  O   . PRO A 1 402 ? 19.821  153.621 -10.112 1.00 53.94 ? 402  PRO A O   1 
ATOM   2973 C  CB  . PRO A 1 402 ? 23.003  153.904 -11.053 1.00 53.08 ? 402  PRO A CB  1 
ATOM   2974 C  CG  . PRO A 1 402 ? 24.324  153.169 -11.052 1.00 52.27 ? 402  PRO A CG  1 
ATOM   2975 C  CD  . PRO A 1 402 ? 23.980  151.787 -11.568 1.00 52.49 ? 402  PRO A CD  1 
ATOM   2976 N  N   . GLU A 1 403 ? 20.231  153.103 -12.272 1.00 51.43 ? 403  GLU A N   1 
ATOM   2977 C  CA  . GLU A 1 403 ? 18.880  153.452 -12.796 1.00 50.37 ? 403  GLU A CA  1 
ATOM   2978 C  C   . GLU A 1 403 ? 17.821  152.593 -12.093 1.00 45.71 ? 403  GLU A C   1 
ATOM   2979 O  O   . GLU A 1 403 ? 16.653  153.009 -12.085 1.00 40.62 ? 403  GLU A O   1 
ATOM   2980 C  CB  . GLU A 1 403 ? 18.766  153.239 -14.309 1.00 56.18 ? 403  GLU A CB  1 
ATOM   2981 C  CG  . GLU A 1 403 ? 19.867  153.900 -15.120 1.00 61.31 ? 403  GLU A CG  1 
ATOM   2982 C  CD  . GLU A 1 403 ? 20.966  152.952 -15.574 1.00 64.37 ? 403  GLU A CD  1 
ATOM   2983 O  OE1 . GLU A 1 403 ? 22.031  152.921 -14.913 1.00 62.49 ? 403  GLU A OE1 1 
ATOM   2984 O  OE2 . GLU A 1 403 ? 20.755  152.246 -16.591 1.00 67.04 ? 403  GLU A OE2 1 
ATOM   2985 N  N   . ALA A 1 404 ? 18.215  151.438 -11.540 1.00 43.44 ? 404  ALA A N   1 
ATOM   2986 C  CA  . ALA A 1 404 ? 17.311  150.487 -10.848 1.00 41.20 ? 404  ALA A CA  1 
ATOM   2987 C  C   . ALA A 1 404 ? 16.714  151.133 -9.596  1.00 39.60 ? 404  ALA A C   1 
ATOM   2988 O  O   . ALA A 1 404 ? 15.668  150.652 -9.152  1.00 40.35 ? 404  ALA A O   1 
ATOM   2989 C  CB  . ALA A 1 404 ? 18.027  149.207 -10.506 1.00 41.99 ? 404  ALA A CB  1 
ATOM   2990 N  N   . GLU A 1 405 ? 17.329  152.195 -9.062  1.00 39.67 ? 405  GLU A N   1 
ATOM   2991 C  CA  . GLU A 1 405 ? 16.816  152.900 -7.854  1.00 39.60 ? 405  GLU A CA  1 
ATOM   2992 C  C   . GLU A 1 405 ? 15.369  153.358 -8.084  1.00 39.75 ? 405  GLU A C   1 
ATOM   2993 O  O   . GLU A 1 405 ? 14.571  153.242 -7.135  1.00 38.47 ? 405  GLU A O   1 
ATOM   2994 C  CB  . GLU A 1 405 ? 17.717  154.071 -7.471  1.00 40.34 ? 405  GLU A CB  1 
ATOM   2995 C  CG  . GLU A 1 405 ? 17.250  154.770 -6.208  1.00 41.42 ? 405  GLU A CG  1 
ATOM   2996 C  CD  . GLU A 1 405 ? 18.233  155.746 -5.588  1.00 41.72 ? 405  GLU A CD  1 
ATOM   2997 O  OE1 . GLU A 1 405 ? 19.429  155.688 -5.934  1.00 42.05 ? 405  GLU A OE1 1 
ATOM   2998 O  OE2 . GLU A 1 405 ? 17.791  156.550 -4.742  1.00 42.59 ? 405  GLU A OE2 1 
ATOM   2999 N  N   . ILE A 1 406 ? 15.053  153.842 -9.294  1.00 39.91 ? 406  ILE A N   1 
ATOM   3000 C  CA  . ILE A 1 406 ? 13.706  154.348 -9.704  1.00 39.37 ? 406  ILE A CA  1 
ATOM   3001 C  C   . ILE A 1 406 ? 12.614  153.361 -9.261  1.00 38.05 ? 406  ILE A C   1 
ATOM   3002 O  O   . ILE A 1 406 ? 11.618  153.815 -8.665  1.00 37.38 ? 406  ILE A O   1 
ATOM   3003 C  CB  . ILE A 1 406 ? 13.661  154.606 -11.227 1.00 40.58 ? 406  ILE A CB  1 
ATOM   3004 N  N   . TYR A 1 407 ? 12.788  152.060 -9.523  1.00 35.98 ? 407  TYR A N   1 
ATOM   3005 C  CA  . TYR A 1 407 ? 11.725  151.033 -9.321  1.00 36.71 ? 407  TYR A CA  1 
ATOM   3006 C  C   . TYR A 1 407 ? 12.030  150.124 -8.113  1.00 34.37 ? 407  TYR A C   1 
ATOM   3007 O  O   . TYR A 1 407 ? 11.319  149.128 -7.939  1.00 35.62 ? 407  TYR A O   1 
ATOM   3008 C  CB  . TYR A 1 407 ? 11.479  150.260 -10.620 1.00 34.53 ? 407  TYR A CB  1 
ATOM   3009 C  CG  . TYR A 1 407 ? 12.693  149.640 -11.263 1.00 35.60 ? 407  TYR A CG  1 
ATOM   3010 C  CD1 . TYR A 1 407 ? 13.234  148.457 -10.779 1.00 35.70 ? 407  TYR A CD1 1 
ATOM   3011 C  CD2 . TYR A 1 407 ? 13.273  150.207 -12.386 1.00 34.30 ? 407  TYR A CD2 1 
ATOM   3012 C  CE1 . TYR A 1 407 ? 14.332  147.865 -11.380 1.00 35.03 ? 407  TYR A CE1 1 
ATOM   3013 C  CE2 . TYR A 1 407 ? 14.379  149.634 -12.990 1.00 34.62 ? 407  TYR A CE2 1 
ATOM   3014 C  CZ  . TYR A 1 407 ? 14.904  148.456 -12.491 1.00 35.19 ? 407  TYR A CZ  1 
ATOM   3015 O  OH  . TYR A 1 407 ? 15.982  147.877 -13.089 1.00 38.49 ? 407  TYR A OH  1 
ATOM   3016 N  N   . ALA A 1 408 ? 12.987  150.502 -7.262  1.00 35.86 ? 408  ALA A N   1 
ATOM   3017 C  CA  . ALA A 1 408 ? 13.446  149.724 -6.083  1.00 37.36 ? 408  ALA A CA  1 
ATOM   3018 C  C   . ALA A 1 408 ? 12.265  149.344 -5.183  1.00 37.55 ? 408  ALA A C   1 
ATOM   3019 O  O   . ALA A 1 408 ? 12.302  148.233 -4.616  1.00 38.77 ? 408  ALA A O   1 
ATOM   3020 C  CB  . ALA A 1 408 ? 14.475  150.509 -5.310  1.00 38.35 ? 408  ALA A CB  1 
ATOM   3021 N  N   . GLY A 1 409 ? 11.271  150.232 -5.051  1.00 38.16 ? 409  GLY A N   1 
ATOM   3022 C  CA  . GLY A 1 409 ? 10.024  149.989 -4.299  1.00 37.47 ? 409  GLY A CA  1 
ATOM   3023 C  C   . GLY A 1 409 ? 9.331   148.720 -4.769  1.00 39.22 ? 409  GLY A C   1 
ATOM   3024 O  O   . GLY A 1 409 ? 8.871   147.921 -3.905  1.00 36.98 ? 409  GLY A O   1 
ATOM   3025 N  N   . THR A 1 410 ? 9.299   148.509 -6.087  1.00 34.64 ? 410  THR A N   1 
ATOM   3026 C  CA  . THR A 1 410 ? 8.618   147.347 -6.727  1.00 34.11 ? 410  THR A CA  1 
ATOM   3027 C  C   . THR A 1 410 ? 9.559   146.137 -6.768  1.00 31.80 ? 410  THR A C   1 
ATOM   3028 O  O   . THR A 1 410 ? 9.102   145.031 -6.419  1.00 30.96 ? 410  THR A O   1 
ATOM   3029 C  CB  . THR A 1 410 ? 8.088   147.740 -8.108  1.00 34.34 ? 410  THR A CB  1 
ATOM   3030 O  OG1 . THR A 1 410 ? 7.187   148.810 -7.832  1.00 36.83 ? 410  THR A OG1 1 
ATOM   3031 C  CG2 . THR A 1 410 ? 7.386   146.618 -8.841  1.00 35.39 ? 410  THR A CG2 1 
ATOM   3032 N  N   . ALA A 1 411 ? 10.811  146.345 -7.187  1.00 30.34 ? 411  ALA A N   1 
ATOM   3033 C  CA  . ALA A 1 411 ? 11.817  145.278 -7.396  1.00 31.03 ? 411  ALA A CA  1 
ATOM   3034 C  C   . ALA A 1 411 ? 13.217  145.790 -7.043  1.00 30.54 ? 411  ALA A C   1 
ATOM   3035 O  O   . ALA A 1 411 ? 13.807  146.513 -7.865  1.00 33.74 ? 411  ALA A O   1 
ATOM   3036 C  CB  . ALA A 1 411 ? 11.752  144.784 -8.826  1.00 30.84 ? 411  ALA A CB  1 
ATOM   3037 N  N   . ALA A 1 412 ? 13.727  145.402 -5.872  1.00 28.31 ? 412  ALA A N   1 
ATOM   3038 C  CA  . ALA A 1 412 ? 15.079  145.746 -5.372  1.00 27.07 ? 412  ALA A CA  1 
ATOM   3039 C  C   . ALA A 1 412 ? 16.038  144.558 -5.551  1.00 26.95 ? 412  ALA A C   1 
ATOM   3040 O  O   . ALA A 1 412 ? 17.264  144.785 -5.528  1.00 26.72 ? 412  ALA A O   1 
ATOM   3041 C  CB  . ALA A 1 412 ? 14.984  146.183 -3.933  1.00 26.69 ? 412  ALA A CB  1 
ATOM   3042 N  N   . GLY A 1 413 ? 15.501  143.345 -5.718  1.00 25.41 ? 413  GLY A N   1 
ATOM   3043 C  CA  . GLY A 1 413 ? 16.274  142.093 -5.845  1.00 24.70 ? 413  GLY A CA  1 
ATOM   3044 C  C   . GLY A 1 413 ? 15.870  141.322 -7.089  1.00 24.27 ? 413  GLY A C   1 
ATOM   3045 O  O   . GLY A 1 413 ? 14.672  141.326 -7.416  1.00 22.78 ? 413  GLY A O   1 
ATOM   3046 N  N   . MET A 1 414 ? 16.833  140.698 -7.769  1.00 24.64 ? 414  MET A N   1 
ATOM   3047 C  CA  . MET A 1 414 ? 16.589  139.931 -9.016  1.00 25.26 ? 414  MET A CA  1 
ATOM   3048 C  C   . MET A 1 414 ? 17.429  138.656 -8.990  1.00 25.94 ? 414  MET A C   1 
ATOM   3049 O  O   . MET A 1 414 ? 18.621  138.727 -8.618  1.00 25.47 ? 414  MET A O   1 
ATOM   3050 C  CB  . MET A 1 414 ? 16.946  140.738 -10.265 1.00 26.33 ? 414  MET A CB  1 
ATOM   3051 C  CG  . MET A 1 414 ? 16.767  139.958 -11.564 1.00 28.38 ? 414  MET A CG  1 
ATOM   3052 S  SD  . MET A 1 414 ? 17.066  140.990 -13.017 1.00 30.59 ? 414  MET A SD  1 
ATOM   3053 C  CE  . MET A 1 414 ? 18.855  141.086 -12.986 1.00 28.84 ? 414  MET A CE  1 
ATOM   3054 N  N   . LEU A 1 415 ? 16.809  137.542 -9.375  1.00 24.77 ? 415  LEU A N   1 
ATOM   3055 C  CA  . LEU A 1 415 ? 17.498  136.264 -9.655  1.00 25.26 ? 415  LEU A CA  1 
ATOM   3056 C  C   . LEU A 1 415 ? 17.205  135.915 -11.113 1.00 26.20 ? 415  LEU A C   1 
ATOM   3057 O  O   . LEU A 1 415 ? 16.009  135.887 -11.487 1.00 25.71 ? 415  LEU A O   1 
ATOM   3058 C  CB  . LEU A 1 415 ? 17.009  135.198 -8.669  1.00 24.93 ? 415  LEU A CB  1 
ATOM   3059 C  CG  . LEU A 1 415 ? 17.659  133.822 -8.809  1.00 24.83 ? 415  LEU A CG  1 
ATOM   3060 C  CD1 . LEU A 1 415 ? 17.647  133.080 -7.486  1.00 25.99 ? 415  LEU A CD1 1 
ATOM   3061 C  CD2 . LEU A 1 415 ? 16.971  132.997 -9.889  1.00 24.29 ? 415  LEU A CD2 1 
ATOM   3062 N  N   . ALA A 1 416 ? 18.264  135.706 -11.902 1.00 26.41 ? 416  ALA A N   1 
ATOM   3063 C  CA  . ALA A 1 416 ? 18.217  135.483 -13.366 1.00 26.28 ? 416  ALA A CA  1 
ATOM   3064 C  C   . ALA A 1 416 ? 18.616  134.037 -13.680 1.00 26.76 ? 416  ALA A C   1 
ATOM   3065 O  O   . ALA A 1 416 ? 19.710  133.617 -13.267 1.00 28.37 ? 416  ALA A O   1 
ATOM   3066 C  CB  . ALA A 1 416 ? 19.126  136.474 -14.050 1.00 26.59 ? 416  ALA A CB  1 
ATOM   3067 N  N   . ILE A 1 417 ? 17.742  133.298 -14.357 1.00 26.91 ? 417  ILE A N   1 
ATOM   3068 C  CA  . ILE A 1 417 ? 18.018  131.921 -14.860 1.00 28.22 ? 417  ILE A CA  1 
ATOM   3069 C  C   . ILE A 1 417 ? 18.205  132.006 -16.372 1.00 30.09 ? 417  ILE A C   1 
ATOM   3070 O  O   . ILE A 1 417 ? 17.258  132.334 -17.080 1.00 28.91 ? 417  ILE A O   1 
ATOM   3071 C  CB  . ILE A 1 417 ? 16.893  130.950 -14.468 1.00 27.17 ? 417  ILE A CB  1 
ATOM   3072 C  CG1 . ILE A 1 417 ? 16.680  130.927 -12.952 1.00 26.13 ? 417  ILE A CG1 1 
ATOM   3073 C  CG2 . ILE A 1 417 ? 17.171  129.561 -15.030 1.00 27.71 ? 417  ILE A CG2 1 
ATOM   3074 C  CD1 . ILE A 1 417 ? 15.623  129.957 -12.493 1.00 25.61 ? 417  ILE A CD1 1 
ATOM   3075 N  N   . PRO A 1 418 ? 19.424  131.760 -16.907 1.00 32.82 ? 418  PRO A N   1 
ATOM   3076 C  CA  . PRO A 1 418 ? 19.642  131.768 -18.355 1.00 35.52 ? 418  PRO A CA  1 
ATOM   3077 C  C   . PRO A 1 418 ? 18.848  130.650 -19.047 1.00 36.13 ? 418  PRO A C   1 
ATOM   3078 O  O   . PRO A 1 418 ? 18.790  129.562 -18.501 1.00 38.44 ? 418  PRO A O   1 
ATOM   3079 C  CB  . PRO A 1 418 ? 21.152  131.549 -18.529 1.00 36.57 ? 418  PRO A CB  1 
ATOM   3080 C  CG  . PRO A 1 418 ? 21.747  131.846 -17.167 1.00 36.81 ? 418  PRO A CG  1 
ATOM   3081 C  CD  . PRO A 1 418 ? 20.664  131.512 -16.160 1.00 34.64 ? 418  PRO A CD  1 
ATOM   3082 N  N   . LEU A 1 419 ? 18.233  130.951 -20.194 1.00 34.48 ? 419  LEU A N   1 
ATOM   3083 C  CA  . LEU A 1 419 ? 17.469  129.970 -21.012 1.00 36.50 ? 419  LEU A CA  1 
ATOM   3084 C  C   . LEU A 1 419 ? 18.267  129.576 -22.262 1.00 38.28 ? 419  LEU A C   1 
ATOM   3085 O  O   . LEU A 1 419 ? 17.716  128.813 -23.086 1.00 40.02 ? 419  LEU A O   1 
ATOM   3086 C  CB  . LEU A 1 419 ? 16.113  130.575 -21.387 1.00 37.39 ? 419  LEU A CB  1 
ATOM   3087 C  CG  . LEU A 1 419 ? 15.240  131.008 -20.211 1.00 37.91 ? 419  LEU A CG  1 
ATOM   3088 C  CD1 . LEU A 1 419 ? 13.892  131.519 -20.688 1.00 38.94 ? 419  LEU A CD1 1 
ATOM   3089 C  CD2 . LEU A 1 419 ? 15.043  129.871 -19.229 1.00 39.14 ? 419  LEU A CD2 1 
ATOM   3090 N  N   . SER A 1 420 ? 19.519  130.040 -22.375 1.00 38.33 ? 420  SER A N   1 
ATOM   3091 C  CA  . SER A 1 420 ? 20.415  129.810 -23.547 1.00 39.69 ? 420  SER A CA  1 
ATOM   3092 C  C   . SER A 1 420 ? 21.796  130.413 -23.273 1.00 41.38 ? 420  SER A C   1 
ATOM   3093 O  O   . SER A 1 420 ? 21.850  131.455 -22.606 1.00 39.71 ? 420  SER A O   1 
ATOM   3094 C  CB  . SER A 1 420 ? 19.805  130.395 -24.814 1.00 40.35 ? 420  SER A CB  1 
ATOM   3095 O  OG  . SER A 1 420 ? 20.745  130.456 -25.881 1.00 40.51 ? 420  SER A OG  1 
ATOM   3096 N  N   . GLN A 1 421 ? 22.865  129.804 -23.799 1.00 43.70 ? 421  GLN A N   1 
ATOM   3097 C  CA  . GLN A 1 421 ? 24.244  130.372 -23.747 1.00 45.49 ? 421  GLN A CA  1 
ATOM   3098 C  C   . GLN A 1 421 ? 24.513  131.211 -25.001 1.00 48.01 ? 421  GLN A C   1 
ATOM   3099 O  O   . GLN A 1 421 ? 25.586  131.831 -25.065 1.00 50.09 ? 421  GLN A O   1 
ATOM   3100 C  CB  . GLN A 1 421 ? 25.293  129.265 -23.640 1.00 48.00 ? 421  GLN A CB  1 
ATOM   3101 C  CG  . GLN A 1 421 ? 25.138  128.408 -22.394 1.00 49.92 ? 421  GLN A CG  1 
ATOM   3102 C  CD  . GLN A 1 421 ? 26.274  127.430 -22.223 1.00 50.55 ? 421  GLN A CD  1 
ATOM   3103 O  OE1 . GLN A 1 421 ? 27.085  127.216 -23.122 1.00 49.66 ? 421  GLN A OE1 1 
ATOM   3104 N  NE2 . GLN A 1 421 ? 26.334  126.818 -21.053 1.00 52.63 ? 421  GLN A NE2 1 
ATOM   3105 N  N   . VAL A 1 422 ? 23.579  131.211 -25.957 1.00 47.69 ? 422  VAL A N   1 
ATOM   3106 C  CA  . VAL A 1 422 ? 23.730  131.863 -27.290 1.00 51.00 ? 422  VAL A CA  1 
ATOM   3107 C  C   . VAL A 1 422 ? 22.854  133.118 -27.347 1.00 51.07 ? 422  VAL A C   1 
ATOM   3108 O  O   . VAL A 1 422 ? 23.305  134.103 -27.948 1.00 53.99 ? 422  VAL A O   1 
ATOM   3109 C  CB  . VAL A 1 422 ? 23.383  130.874 -28.420 1.00 54.05 ? 422  VAL A CB  1 
ATOM   3110 C  CG1 . VAL A 1 422 ? 22.996  131.577 -29.713 1.00 54.34 ? 422  VAL A CG1 1 
ATOM   3111 C  CG2 . VAL A 1 422 ? 24.528  129.899 -28.659 1.00 55.56 ? 422  VAL A CG2 1 
ATOM   3112 N  N   . LYS A 1 423 ? 21.640  133.047 -26.791 1.00 47.56 ? 423  LYS A N   1 
ATOM   3113 C  CA  . LYS A 1 423 ? 20.640  134.147 -26.768 1.00 45.38 ? 423  LYS A CA  1 
ATOM   3114 C  C   . LYS A 1 423 ? 20.535  134.705 -25.344 1.00 44.35 ? 423  LYS A C   1 
ATOM   3115 O  O   . LYS A 1 423 ? 20.665  133.928 -24.372 1.00 43.78 ? 423  LYS A O   1 
ATOM   3116 C  CB  . LYS A 1 423 ? 19.279  133.646 -27.263 1.00 43.62 ? 423  LYS A CB  1 
ATOM   3117 N  N   . SER A 1 424 ? 20.272  136.004 -25.239 1.00 41.82 ? 424  SER A N   1 
ATOM   3118 C  CA  . SER A 1 424 ? 20.132  136.742 -23.953 1.00 41.36 ? 424  SER A CA  1 
ATOM   3119 C  C   . SER A 1 424 ? 18.686  136.611 -23.439 1.00 38.91 ? 424  SER A C   1 
ATOM   3120 O  O   . SER A 1 424 ? 18.045  137.647 -23.173 1.00 37.79 ? 424  SER A O   1 
ATOM   3121 C  CB  . SER A 1 424 ? 20.560  138.174 -24.132 1.00 42.36 ? 424  SER A CB  1 
ATOM   3122 O  OG  . SER A 1 424 ? 20.960  138.735 -22.895 1.00 49.40 ? 424  SER A OG  1 
ATOM   3123 N  N   . ASP A 1 425 ? 18.200  135.368 -23.319 1.00 35.83 ? 425  ASP A N   1 
ATOM   3124 C  CA  . ASP A 1 425 ? 16.835  135.006 -22.849 1.00 33.41 ? 425  ASP A CA  1 
ATOM   3125 C  C   . ASP A 1 425 ? 16.925  134.520 -21.396 1.00 31.40 ? 425  ASP A C   1 
ATOM   3126 O  O   . ASP A 1 425 ? 17.889  133.804 -21.067 1.00 30.13 ? 425  ASP A O   1 
ATOM   3127 C  CB  . ASP A 1 425 ? 16.194  133.941 -23.742 1.00 34.02 ? 425  ASP A CB  1 
ATOM   3128 C  CG  . ASP A 1 425 ? 16.001  134.357 -25.194 1.00 35.76 ? 425  ASP A CG  1 
ATOM   3129 O  OD1 . ASP A 1 425 ? 15.797  135.562 -25.446 1.00 37.01 ? 425  ASP A OD1 1 
ATOM   3130 O  OD2 . ASP A 1 425 ? 16.029  133.464 -26.063 1.00 35.85 ? 425  ASP A OD2 1 
ATOM   3131 N  N   . TYR A 1 426 ? 15.957  134.908 -20.563 1.00 30.45 ? 426  TYR A N   1 
ATOM   3132 C  CA  . TYR A 1 426 ? 15.984  134.737 -19.087 1.00 29.73 ? 426  TYR A CA  1 
ATOM   3133 C  C   . TYR A 1 426 ? 14.571  134.544 -18.551 1.00 27.54 ? 426  TYR A C   1 
ATOM   3134 O  O   . TYR A 1 426 ? 13.622  135.148 -19.077 1.00 27.38 ? 426  TYR A O   1 
ATOM   3135 C  CB  . TYR A 1 426 ? 16.607  135.953 -18.393 1.00 31.30 ? 426  TYR A CB  1 
ATOM   3136 C  CG  . TYR A 1 426 ? 18.041  136.206 -18.771 1.00 33.23 ? 426  TYR A CG  1 
ATOM   3137 C  CD1 . TYR A 1 426 ? 19.060  135.416 -18.262 1.00 36.56 ? 426  TYR A CD1 1 
ATOM   3138 C  CD2 . TYR A 1 426 ? 18.380  137.220 -19.650 1.00 37.06 ? 426  TYR A CD2 1 
ATOM   3139 C  CE1 . TYR A 1 426 ? 20.381  135.619 -18.625 1.00 36.76 ? 426  TYR A CE1 1 
ATOM   3140 C  CE2 . TYR A 1 426 ? 19.697  137.445 -20.014 1.00 38.22 ? 426  TYR A CE2 1 
ATOM   3141 C  CZ  . TYR A 1 426 ? 20.699  136.637 -19.504 1.00 39.00 ? 426  TYR A CZ  1 
ATOM   3142 O  OH  . TYR A 1 426 ? 21.999  136.858 -19.849 1.00 42.30 ? 426  TYR A OH  1 
ATOM   3143 N  N   . LEU A 1 427 ? 14.469  133.696 -17.531 1.00 27.44 ? 427  LEU A N   1 
ATOM   3144 C  CA  . LEU A 1 427 ? 13.389  133.698 -16.519 1.00 26.85 ? 427  LEU A CA  1 
ATOM   3145 C  C   . LEU A 1 427 ? 13.917  134.510 -15.334 1.00 26.07 ? 427  LEU A C   1 
ATOM   3146 O  O   . LEU A 1 427 ? 15.006  134.169 -14.834 1.00 25.30 ? 427  LEU A O   1 
ATOM   3147 C  CB  . LEU A 1 427 ? 13.063  132.247 -16.146 1.00 27.83 ? 427  LEU A CB  1 
ATOM   3148 C  CG  . LEU A 1 427 ? 11.834  132.025 -15.267 1.00 28.55 ? 427  LEU A CG  1 
ATOM   3149 C  CD1 . LEU A 1 427 ? 10.560  132.442 -15.987 1.00 28.83 ? 427  LEU A CD1 1 
ATOM   3150 C  CD2 . LEU A 1 427 ? 11.748  130.564 -14.849 1.00 27.95 ? 427  LEU A CD2 1 
ATOM   3151 N  N   . LEU A 1 428 ? 13.210  135.581 -14.961 1.00 24.94 ? 428  LEU A N   1 
ATOM   3152 C  CA  . LEU A 1 428 ? 13.646  136.562 -13.938 1.00 25.67 ? 428  LEU A CA  1 
ATOM   3153 C  C   . LEU A 1 428 ? 12.698  136.496 -12.745 1.00 25.04 ? 428  LEU A C   1 
ATOM   3154 O  O   . LEU A 1 428 ? 11.488  136.516 -12.955 1.00 25.24 ? 428  LEU A O   1 
ATOM   3155 C  CB  . LEU A 1 428 ? 13.655  137.962 -14.557 1.00 25.82 ? 428  LEU A CB  1 
ATOM   3156 C  CG  . LEU A 1 428 ? 14.610  138.143 -15.735 1.00 27.35 ? 428  LEU A CG  1 
ATOM   3157 C  CD1 . LEU A 1 428 ? 14.568  139.585 -16.224 1.00 27.31 ? 428  LEU A CD1 1 
ATOM   3158 C  CD2 . LEU A 1 428 ? 16.034  137.748 -15.349 1.00 27.51 ? 428  LEU A CD2 1 
ATOM   3159 N  N   . PHE A 1 429 ? 13.254  136.376 -11.545 1.00 24.28 ? 429  PHE A N   1 
ATOM   3160 C  CA  . PHE A 1 429 ? 12.512  136.429 -10.264 1.00 24.69 ? 429  PHE A CA  1 
ATOM   3161 C  C   . PHE A 1 429 ? 12.869  137.743 -9.572  1.00 24.09 ? 429  PHE A C   1 
ATOM   3162 O  O   . PHE A 1 429 ? 14.046  138.131 -9.615  1.00 23.44 ? 429  PHE A O   1 
ATOM   3163 C  CB  . PHE A 1 429 ? 12.857  135.214 -9.406  1.00 25.53 ? 429  PHE A CB  1 
ATOM   3164 C  CG  . PHE A 1 429 ? 12.494  133.892 -10.027 1.00 25.54 ? 429  PHE A CG  1 
ATOM   3165 C  CD1 . PHE A 1 429 ? 13.237  133.374 -11.073 1.00 26.14 ? 429  PHE A CD1 1 
ATOM   3166 C  CD2 . PHE A 1 429 ? 11.426  133.154 -9.543  1.00 27.22 ? 429  PHE A CD2 1 
ATOM   3167 C  CE1 . PHE A 1 429 ? 12.903  132.153 -11.641 1.00 27.11 ? 429  PHE A CE1 1 
ATOM   3168 C  CE2 . PHE A 1 429 ? 11.095  131.931 -10.110 1.00 27.29 ? 429  PHE A CE2 1 
ATOM   3169 C  CZ  . PHE A 1 429 ? 11.833  131.433 -11.156 1.00 27.15 ? 429  PHE A CZ  1 
ATOM   3170 N  N   . PHE A 1 430 ? 11.887  138.402 -8.957  1.00 24.33 ? 430  PHE A N   1 
ATOM   3171 C  CA  . PHE A 1 430 ? 12.083  139.710 -8.283  1.00 24.11 ? 430  PHE A CA  1 
ATOM   3172 C  C   . PHE A 1 430 ? 11.584  139.647 -6.847  1.00 24.33 ? 430  PHE A C   1 
ATOM   3173 O  O   . PHE A 1 430 ? 10.685  138.853 -6.548  1.00 22.92 ? 430  PHE A O   1 
ATOM   3174 C  CB  . PHE A 1 430 ? 11.373  140.827 -9.038  1.00 25.29 ? 430  PHE A CB  1 
ATOM   3175 C  CG  . PHE A 1 430 ? 11.866  140.974 -10.450 1.00 25.98 ? 430  PHE A CG  1 
ATOM   3176 C  CD1 . PHE A 1 430 ? 13.053  141.633 -10.716 1.00 26.42 ? 430  PHE A CD1 1 
ATOM   3177 C  CD2 . PHE A 1 430 ? 11.171  140.408 -11.504 1.00 27.87 ? 430  PHE A CD2 1 
ATOM   3178 C  CE1 . PHE A 1 430 ? 13.517  141.755 -12.016 1.00 25.47 ? 430  PHE A CE1 1 
ATOM   3179 C  CE2 . PHE A 1 430 ? 11.637  140.538 -12.802 1.00 27.03 ? 430  PHE A CE2 1 
ATOM   3180 C  CZ  . PHE A 1 430 ? 12.806  141.212 -13.051 1.00 25.62 ? 430  PHE A CZ  1 
ATOM   3181 N  N   . ARG A 1 431 ? 12.192  140.477 -6.003  1.00 23.59 ? 431  ARG A N   1 
ATOM   3182 C  CA  . ARG A 1 431 ? 11.737  140.740 -4.621  1.00 25.11 ? 431  ARG A CA  1 
ATOM   3183 C  C   . ARG A 1 431 ? 11.675  142.245 -4.406  1.00 25.82 ? 431  ARG A C   1 
ATOM   3184 O  O   . ARG A 1 431 ? 12.491  142.997 -4.945  1.00 24.46 ? 431  ARG A O   1 
ATOM   3185 C  CB  . ARG A 1 431 ? 12.677  140.075 -3.614  1.00 25.99 ? 431  ARG A CB  1 
ATOM   3186 C  CG  . ARG A 1 431 ? 12.465  138.576 -3.516  1.00 26.14 ? 431  ARG A CG  1 
ATOM   3187 C  CD  . ARG A 1 431 ? 13.451  137.934 -2.578  1.00 26.40 ? 431  ARG A CD  1 
ATOM   3188 N  NE  . ARG A 1 431 ? 13.240  136.502 -2.545  1.00 26.08 ? 431  ARG A NE  1 
ATOM   3189 C  CZ  . ARG A 1 431 ? 14.009  135.641 -1.899  1.00 26.69 ? 431  ARG A CZ  1 
ATOM   3190 N  NH1 . ARG A 1 431 ? 15.048  136.069 -1.199  1.00 27.15 ? 431  ARG A NH1 1 
ATOM   3191 N  NH2 . ARG A 1 431 ? 13.721  134.350 -1.946  1.00 26.01 ? 431  ARG A NH2 1 
HETATM 3192 N  N   . MLZ A 1 432 ? 10.695  142.644 -3.598  1.00 25.72 ? 432  MLZ A N   1 
HETATM 3193 C  CA  . MLZ A 1 432 ? 10.514  144.025 -3.211  1.00 26.98 ? 432  MLZ A CA  1 
HETATM 3194 C  CB  . MLZ A 1 432 ? 9.159   144.212 -2.523  1.00 28.34 ? 432  MLZ A CB  1 
HETATM 3195 C  CG  . MLZ A 1 432 ? 7.937   144.098 -3.421  1.00 30.92 ? 432  MLZ A CG  1 
HETATM 3196 C  CD  . MLZ A 1 432 ? 6.651   144.336 -2.662  1.00 33.67 ? 432  MLZ A CD  1 
HETATM 3197 C  CE  . MLZ A 1 432 ? 5.395   144.104 -3.487  1.00 37.38 ? 432  MLZ A CE  1 
HETATM 3198 N  NZ  . MLZ A 1 432 ? 4.191   144.043 -2.651  1.00 39.57 ? 432  MLZ A NZ  1 
HETATM 3199 C  CM  . MLZ A 1 432 ? 4.114   142.955 -1.666  1.00 40.29 ? 432  MLZ A CM  1 
HETATM 3200 C  C   . MLZ A 1 432 ? 11.613  144.431 -2.236  1.00 26.59 ? 432  MLZ A C   1 
HETATM 3201 O  O   . MLZ A 1 432 ? 12.230  143.593 -1.580  1.00 24.92 ? 432  MLZ A O   1 
ATOM   3202 N  N   . GLU A 1 433 ? 11.837  145.743 -2.177  1.00 28.07 ? 433  GLU A N   1 
ATOM   3203 C  CA  . GLU A 1 433 ? 12.560  146.377 -1.093  1.00 31.38 ? 433  GLU A CA  1 
ATOM   3204 C  C   . GLU A 1 433 ? 12.060  145.774 0.230   1.00 30.03 ? 433  GLU A C   1 
ATOM   3205 O  O   . GLU A 1 433 ? 10.832  145.726 0.438   1.00 26.74 ? 433  GLU A O   1 
ATOM   3206 C  CB  . GLU A 1 433 ? 12.333  147.887 -1.193  1.00 34.34 ? 433  GLU A CB  1 
ATOM   3207 C  CG  . GLU A 1 433 ? 13.255  148.691 -0.315  1.00 39.56 ? 433  GLU A CG  1 
ATOM   3208 C  CD  . GLU A 1 433 ? 13.221  150.192 -0.531  1.00 40.96 ? 433  GLU A CD  1 
ATOM   3209 O  OE1 . GLU A 1 433 ? 12.343  150.671 -1.296  1.00 41.24 ? 433  GLU A OE1 1 
ATOM   3210 O  OE2 . GLU A 1 433 ? 14.072  150.871 0.080   1.00 42.56 ? 433  GLU A OE2 1 
ATOM   3211 N  N   . ILE A 1 434 ? 12.974  145.302 1.074   1.00 29.89 ? 434  ILE A N   1 
ATOM   3212 C  CA  . ILE A 1 434 ? 12.641  144.470 2.269   1.00 31.91 ? 434  ILE A CA  1 
ATOM   3213 C  C   . ILE A 1 434 ? 11.773  145.284 3.245   1.00 31.89 ? 434  ILE A C   1 
ATOM   3214 O  O   . ILE A 1 434 ? 10.946  144.672 3.938   1.00 34.32 ? 434  ILE A O   1 
ATOM   3215 C  CB  . ILE A 1 434 ? 13.922  143.886 2.903   1.00 32.43 ? 434  ILE A CB  1 
ATOM   3216 C  CG1 . ILE A 1 434 ? 13.591  142.871 3.996   1.00 34.74 ? 434  ILE A CG1 1 
ATOM   3217 C  CG2 . ILE A 1 434 ? 14.847  144.978 3.410   1.00 34.33 ? 434  ILE A CG2 1 
ATOM   3218 C  CD1 . ILE A 1 434 ? 14.798  142.161 4.562   1.00 35.43 ? 434  ILE A CD1 1 
ATOM   3219 N  N   . VAL A 1 435 ? 11.894  146.612 3.257   1.00 31.24 ? 435  VAL A N   1 
ATOM   3220 C  CA  . VAL A 1 435 ? 11.079  147.503 4.136   1.00 33.46 ? 435  VAL A CA  1 
ATOM   3221 C  C   . VAL A 1 435 ? 9.592   147.434 3.740   1.00 34.69 ? 435  VAL A C   1 
ATOM   3222 O  O   . VAL A 1 435 ? 8.754   147.628 4.623   1.00 34.66 ? 435  VAL A O   1 
ATOM   3223 C  CB  . VAL A 1 435 ? 11.617  148.946 4.111   1.00 34.70 ? 435  VAL A CB  1 
ATOM   3224 C  CG1 . VAL A 1 435 ? 11.156  149.718 2.883   1.00 33.99 ? 435  VAL A CG1 1 
ATOM   3225 C  CG2 . VAL A 1 435 ? 11.256  149.693 5.386   1.00 35.26 ? 435  VAL A CG2 1 
ATOM   3226 N  N   . GLN A 1 436 ? 9.277   147.153 2.470   1.00 36.54 ? 436  GLN A N   1 
ATOM   3227 C  CA  . GLN A 1 436 ? 7.882   147.069 1.946   1.00 38.95 ? 436  GLN A CA  1 
ATOM   3228 C  C   . GLN A 1 436 ? 7.178   145.807 2.462   1.00 38.02 ? 436  GLN A C   1 
ATOM   3229 O  O   . GLN A 1 436 ? 5.938   145.791 2.442   1.00 41.43 ? 436  GLN A O   1 
ATOM   3230 C  CB  . GLN A 1 436 ? 7.841   147.014 0.417   1.00 40.71 ? 436  GLN A CB  1 
ATOM   3231 C  CG  . GLN A 1 436 ? 8.603   148.131 -0.280  1.00 42.69 ? 436  GLN A CG  1 
ATOM   3232 C  CD  . GLN A 1 436 ? 7.938   149.480 -0.176  1.00 47.15 ? 436  GLN A CD  1 
ATOM   3233 O  OE1 . GLN A 1 436 ? 6.718   149.590 -0.065  1.00 50.75 ? 436  GLN A OE1 1 
ATOM   3234 N  NE2 . GLN A 1 436 ? 8.745   150.529 -0.239  1.00 51.35 ? 436  GLN A NE2 1 
ATOM   3235 N  N   . ASN A 1 437 ? 7.928   144.775 2.860   1.00 38.15 ? 437  ASN A N   1 
ATOM   3236 C  CA  . ASN A 1 437 ? 7.365   143.469 3.296   1.00 38.59 ? 437  ASN A CA  1 
ATOM   3237 C  C   . ASN A 1 437 ? 7.361   143.373 4.823   1.00 35.96 ? 437  ASN A C   1 
ATOM   3238 O  O   . ASN A 1 437 ? 7.044   142.279 5.311   1.00 34.48 ? 437  ASN A O   1 
ATOM   3239 C  CB  . ASN A 1 437 ? 8.127   142.282 2.693   1.00 42.01 ? 437  ASN A CB  1 
ATOM   3240 C  CG  . ASN A 1 437 ? 7.863   142.094 1.214   1.00 41.69 ? 437  ASN A CG  1 
ATOM   3241 O  OD1 . ASN A 1 437 ? 6.821   142.500 0.705   1.00 43.49 ? 437  ASN A OD1 1 
ATOM   3242 N  ND2 . ASN A 1 437 ? 8.806   141.483 0.517   1.00 42.87 ? 437  ASN A ND2 1 
ATOM   3243 N  N   . LEU A 1 438 ? 7.714   144.455 5.530   1.00 33.19 ? 438  LEU A N   1 
ATOM   3244 C  CA  . LEU A 1 438 ? 7.737   144.513 7.019   1.00 33.77 ? 438  LEU A CA  1 
ATOM   3245 C  C   . LEU A 1 438 ? 6.359   144.140 7.581   1.00 32.71 ? 438  LEU A C   1 
ATOM   3246 O  O   . LEU A 1 438 ? 5.349   144.567 7.001   1.00 32.08 ? 438  LEU A O   1 
ATOM   3247 C  CB  . LEU A 1 438 ? 8.105   145.924 7.490   1.00 34.01 ? 438  LEU A CB  1 
ATOM   3248 C  CG  . LEU A 1 438 ? 9.585   146.211 7.727   1.00 34.50 ? 438  LEU A CG  1 
ATOM   3249 C  CD1 . LEU A 1 438 ? 9.757   147.642 8.221   1.00 34.18 ? 438  LEU A CD1 1 
ATOM   3250 C  CD2 . LEU A 1 438 ? 10.193  145.225 8.714   1.00 34.87 ? 438  LEU A CD2 1 
ATOM   3251 N  N   . ASN A 1 439 ? 6.330   143.399 8.689   1.00 31.66 ? 439  ASN A N   1 
ATOM   3252 C  CA  . ASN A 1 439 ? 5.095   143.141 9.479   1.00 31.67 ? 439  ASN A CA  1 
ATOM   3253 C  C   . ASN A 1 439 ? 5.421   143.454 10.938  1.00 30.64 ? 439  ASN A C   1 
ATOM   3254 O  O   . ASN A 1 439 ? 5.542   142.527 11.750  1.00 30.63 ? 439  ASN A O   1 
ATOM   3255 C  CB  . ASN A 1 439 ? 4.567   141.719 9.273   1.00 32.52 ? 439  ASN A CB  1 
ATOM   3256 C  CG  . ASN A 1 439 ? 3.267   141.473 10.011  1.00 33.93 ? 439  ASN A CG  1 
ATOM   3257 O  OD1 . ASN A 1 439 ? 2.478   142.390 10.209  1.00 35.91 ? 439  ASN A OD1 1 
ATOM   3258 N  ND2 . ASN A 1 439 ? 3.031   140.238 10.413  1.00 34.76 ? 439  ASN A ND2 1 
ATOM   3259 N  N   . TRP A 1 440 ? 5.626   144.730 11.227  1.00 30.94 ? 440  TRP A N   1 
ATOM   3260 C  CA  . TRP A 1 440 ? 6.077   145.217 12.551  1.00 30.01 ? 440  TRP A CA  1 
ATOM   3261 C  C   . TRP A 1 440 ? 4.854   145.426 13.447  1.00 30.28 ? 440  TRP A C   1 
ATOM   3262 O  O   . TRP A 1 440 ? 3.946   146.150 13.025  1.00 28.64 ? 440  TRP A O   1 
ATOM   3263 C  CB  . TRP A 1 440 ? 6.889   146.495 12.359  1.00 31.48 ? 440  TRP A CB  1 
ATOM   3264 C  CG  . TRP A 1 440 ? 7.392   147.103 13.629  1.00 32.52 ? 440  TRP A CG  1 
ATOM   3265 C  CD1 . TRP A 1 440 ? 8.123   146.494 14.606  1.00 32.30 ? 440  TRP A CD1 1 
ATOM   3266 C  CD2 . TRP A 1 440 ? 7.202   148.463 14.054  1.00 34.51 ? 440  TRP A CD2 1 
ATOM   3267 N  NE1 . TRP A 1 440 ? 8.403   147.382 15.609  1.00 33.58 ? 440  TRP A NE1 1 
ATOM   3268 C  CE2 . TRP A 1 440 ? 7.864   148.600 15.294  1.00 33.92 ? 440  TRP A CE2 1 
ATOM   3269 C  CE3 . TRP A 1 440 ? 6.549   149.573 13.503  1.00 35.04 ? 440  TRP A CE3 1 
ATOM   3270 C  CZ2 . TRP A 1 440 ? 7.879   149.801 15.998  1.00 34.87 ? 440  TRP A CZ2 1 
ATOM   3271 C  CZ3 . TRP A 1 440 ? 6.576   150.763 14.193  1.00 36.71 ? 440  TRP A CZ3 1 
ATOM   3272 C  CH2 . TRP A 1 440 ? 7.232   150.871 15.423  1.00 36.78 ? 440  TRP A CH2 1 
ATOM   3273 N  N   . ALA A 1 441 ? 4.850   144.812 14.634  1.00 30.88 ? 441  ALA A N   1 
ATOM   3274 C  CA  . ALA A 1 441 ? 3.724   144.831 15.596  1.00 32.83 ? 441  ALA A CA  1 
ATOM   3275 C  C   . ALA A 1 441 ? 3.908   145.976 16.598  1.00 33.10 ? 441  ALA A C   1 
ATOM   3276 O  O   . ALA A 1 441 ? 3.077   146.107 17.504  1.00 33.69 ? 441  ALA A O   1 
ATOM   3277 C  CB  . ALA A 1 441 ? 3.628   143.498 16.294  1.00 32.85 ? 441  ALA A CB  1 
ATOM   3278 N  N   . GLY A 1 442 ? 4.956   146.782 16.434  1.00 33.35 ? 442  GLY A N   1 
ATOM   3279 C  CA  . GLY A 1 442 ? 5.347   147.794 17.428  1.00 34.68 ? 442  GLY A CA  1 
ATOM   3280 C  C   . GLY A 1 442 ? 4.511   149.057 17.330  1.00 36.72 ? 442  GLY A C   1 
ATOM   3281 O  O   . GLY A 1 442 ? 3.654   149.156 16.429  1.00 35.04 ? 442  GLY A O   1 
ATOM   3282 N  N   . ASN A 1 443 ? 4.763   149.989 18.247  1.00 38.25 ? 443  ASN A N   1 
ATOM   3283 C  CA  . ASN A 1 443 ? 4.007   151.255 18.418  1.00 40.88 ? 443  ASN A CA  1 
ATOM   3284 C  C   . ASN A 1 443 ? 4.912   152.409 18.002  1.00 43.26 ? 443  ASN A C   1 
ATOM   3285 O  O   . ASN A 1 443 ? 5.845   152.757 18.726  1.00 43.55 ? 443  ASN A O   1 
ATOM   3286 C  CB  . ASN A 1 443 ? 3.512   151.407 19.857  1.00 41.78 ? 443  ASN A CB  1 
ATOM   3287 C  CG  . ASN A 1 443 ? 2.709   152.669 20.081  1.00 44.30 ? 443  ASN A CG  1 
ATOM   3288 O  OD1 . ASN A 1 443 ? 2.746   153.591 19.269  1.00 45.51 ? 443  ASN A OD1 1 
ATOM   3289 N  ND2 . ASN A 1 443 ? 1.979   152.717 21.182  1.00 47.96 ? 443  ASN A ND2 1 
ATOM   3290 N  N   . PRO A 1 444 ? 4.679   153.034 16.825  1.00 45.62 ? 444  PRO A N   1 
ATOM   3291 C  CA  . PRO A 1 444 ? 5.540   154.122 16.364  1.00 47.36 ? 444  PRO A CA  1 
ATOM   3292 C  C   . PRO A 1 444 ? 5.429   155.380 17.241  1.00 49.31 ? 444  PRO A C   1 
ATOM   3293 O  O   . PRO A 1 444 ? 6.245   156.259 17.064  1.00 50.20 ? 444  PRO A O   1 
ATOM   3294 C  CB  . PRO A 1 444 ? 5.080   154.393 14.922  1.00 47.40 ? 444  PRO A CB  1 
ATOM   3295 C  CG  . PRO A 1 444 ? 3.676   153.819 14.833  1.00 46.29 ? 444  PRO A CG  1 
ATOM   3296 C  CD  . PRO A 1 444 ? 3.591   152.729 15.883  1.00 46.78 ? 444  PRO A CD  1 
ATOM   3297 N  N   . GLU A 1 445 ? 4.466   155.426 18.171  1.00 50.88 ? 445  GLU A N   1 
ATOM   3298 C  CA  . GLU A 1 445 ? 4.271   156.568 19.110  1.00 54.43 ? 445  GLU A CA  1 
ATOM   3299 C  C   . GLU A 1 445 ? 5.096   156.380 20.385  1.00 51.30 ? 445  GLU A C   1 
ATOM   3300 O  O   . GLU A 1 445 ? 5.309   157.347 21.115  1.00 50.90 ? 445  GLU A O   1 
ATOM   3301 C  CB  . GLU A 1 445 ? 2.792   156.752 19.465  1.00 58.49 ? 445  GLU A CB  1 
ATOM   3302 C  CG  . GLU A 1 445 ? 1.882   156.975 18.266  1.00 61.89 ? 445  GLU A CG  1 
ATOM   3303 C  CD  . GLU A 1 445 ? 2.081   158.286 17.521  1.00 65.17 ? 445  GLU A CD  1 
ATOM   3304 O  OE1 . GLU A 1 445 ? 1.135   159.102 17.501  1.00 68.85 ? 445  GLU A OE1 1 
ATOM   3305 O  OE2 . GLU A 1 445 ? 3.171   158.481 16.943  1.00 69.96 ? 445  GLU A OE2 1 
HETATM 3306 N  N   . MLZ A 1 446 ? 5.549   155.146 20.655  1.00 46.67 ? 446  MLZ A N   1 
HETATM 3307 C  CA  . MLZ A 1 446 ? 6.327   154.865 21.854  1.00 42.62 ? 446  MLZ A CA  1 
HETATM 3308 C  CB  . MLZ A 1 446 ? 6.391   153.356 22.121  1.00 42.47 ? 446  MLZ A CB  1 
HETATM 3309 C  CG  . MLZ A 1 446 ? 7.425   152.907 23.148  1.00 43.17 ? 446  MLZ A CG  1 
HETATM 3310 C  CD  . MLZ A 1 446 ? 7.211   153.456 24.543  1.00 43.68 ? 446  MLZ A CD  1 
HETATM 3311 C  CE  . MLZ A 1 446 ? 8.089   152.716 25.538  1.00 44.36 ? 446  MLZ A CE  1 
HETATM 3312 N  NZ  . MLZ A 1 446 ? 8.057   153.261 26.900  1.00 45.91 ? 446  MLZ A NZ  1 
HETATM 3313 C  CM  . MLZ A 1 446 ? 9.378   153.440 27.530  1.00 46.00 ? 446  MLZ A CM  1 
HETATM 3314 C  C   . MLZ A 1 446 ? 7.713   155.487 21.694  1.00 41.45 ? 446  MLZ A C   1 
HETATM 3315 O  O   . MLZ A 1 446 ? 8.402   155.256 20.703  1.00 39.80 ? 446  MLZ A O   1 
ATOM   3316 N  N   . SER A 1 447 ? 8.101   156.312 22.668  1.00 40.82 ? 447  SER A N   1 
ATOM   3317 C  CA  . SER A 1 447 ? 9.393   156.969 22.632  1.00 41.38 ? 447  SER A CA  1 
ATOM   3318 C  C   . SER A 1 447 ? 10.187  156.578 23.879  1.00 37.91 ? 447  SER A C   1 
ATOM   3319 O  O   . SER A 1 447 ? 9.580   156.035 24.831  1.00 38.49 ? 447  SER A O   1 
ATOM   3320 C  CB  . SER A 1 447 ? 9.241   158.461 22.511  1.00 43.11 ? 447  SER A CB  1 
ATOM   3321 O  OG  . SER A 1 447 ? 8.584   158.976 23.654  1.00 48.89 ? 447  SER A OG  1 
ATOM   3322 N  N   . TYR A 1 448 ? 11.488  156.857 23.866  1.00 33.89 ? 448  TYR A N   1 
ATOM   3323 C  CA  . TYR A 1 448 ? 12.464  156.387 24.880  1.00 34.82 ? 448  TYR A CA  1 
ATOM   3324 C  C   . TYR A 1 448 ? 13.224  157.587 25.437  1.00 37.06 ? 448  TYR A C   1 
ATOM   3325 O  O   . TYR A 1 448 ? 13.580  158.487 24.661  1.00 36.19 ? 448  TYR A O   1 
ATOM   3326 C  CB  . TYR A 1 448 ? 13.400  155.348 24.256  1.00 32.89 ? 448  TYR A CB  1 
ATOM   3327 C  CG  . TYR A 1 448 ? 12.674  154.100 23.818  1.00 30.59 ? 448  TYR A CG  1 
ATOM   3328 C  CD1 . TYR A 1 448 ? 12.387  153.099 24.729  1.00 30.29 ? 448  TYR A CD1 1 
ATOM   3329 C  CD2 . TYR A 1 448 ? 12.229  153.940 22.517  1.00 29.27 ? 448  TYR A CD2 1 
ATOM   3330 C  CE1 . TYR A 1 448 ? 11.694  151.960 24.360  1.00 29.79 ? 448  TYR A CE1 1 
ATOM   3331 C  CE2 . TYR A 1 448 ? 11.526  152.809 22.130  1.00 28.84 ? 448  TYR A CE2 1 
ATOM   3332 C  CZ  . TYR A 1 448 ? 11.259  151.813 23.055  1.00 28.91 ? 448  TYR A CZ  1 
ATOM   3333 O  OH  . TYR A 1 448 ? 10.558  150.696 22.715  1.00 27.27 ? 448  TYR A OH  1 
ATOM   3334 N  N   . GLU A 1 449 ? 13.447  157.588 26.750  1.00 38.92 ? 449  GLU A N   1 
ATOM   3335 C  CA  . GLU A 1 449 ? 14.425  158.480 27.420  1.00 43.19 ? 449  GLU A CA  1 
ATOM   3336 C  C   . GLU A 1 449 ? 15.827  158.016 27.014  1.00 41.47 ? 449  GLU A C   1 
ATOM   3337 O  O   . GLU A 1 449 ? 15.967  156.865 26.551  1.00 42.95 ? 449  GLU A O   1 
ATOM   3338 C  CB  . GLU A 1 449 ? 14.193  158.474 28.931  1.00 48.68 ? 449  GLU A CB  1 
ATOM   3339 C  CG  . GLU A 1 449 ? 12.804  158.970 29.295  1.00 54.56 ? 449  GLU A CG  1 
ATOM   3340 C  CD  . GLU A 1 449 ? 12.583  159.309 30.756  1.00 58.85 ? 449  GLU A CD  1 
ATOM   3341 O  OE1 . GLU A 1 449 ? 13.293  158.745 31.609  1.00 62.34 ? 449  GLU A OE1 1 
ATOM   3342 O  OE2 . GLU A 1 449 ? 11.693  160.139 31.031  1.00 67.76 ? 449  GLU A OE2 1 
ATOM   3343 N  N   . THR A 1 450 ? 16.817  158.896 27.130  1.00 36.74 ? 450  THR A N   1 
ATOM   3344 C  CA  . THR A 1 450 ? 18.214  158.611 26.732  1.00 36.53 ? 450  THR A CA  1 
ATOM   3345 C  C   . THR A 1 450 ? 19.138  159.098 27.840  1.00 35.76 ? 450  THR A C   1 
ATOM   3346 O  O   . THR A 1 450 ? 18.698  159.914 28.646  1.00 37.13 ? 450  THR A O   1 
ATOM   3347 C  CB  . THR A 1 450 ? 18.553  159.254 25.382  1.00 35.92 ? 450  THR A CB  1 
ATOM   3348 O  OG1 . THR A 1 450 ? 18.511  160.672 25.541  1.00 36.42 ? 450  THR A OG1 1 
ATOM   3349 C  CG2 . THR A 1 450 ? 17.604  158.837 24.280  1.00 35.16 ? 450  THR A CG2 1 
ATOM   3350 N  N   . GLY A 1 451 ? 20.362  158.582 27.862  1.00 39.12 ? 451  GLY A N   1 
ATOM   3351 C  CA  . GLY A 1 451 ? 21.450  159.055 28.734  1.00 39.93 ? 451  GLY A CA  1 
ATOM   3352 C  C   . GLY A 1 451 ? 22.464  159.864 27.932  1.00 40.16 ? 451  GLY A C   1 
ATOM   3353 O  O   . GLY A 1 451 ? 22.192  160.269 26.803  1.00 39.92 ? 451  GLY A O   1 
ATOM   3354 N  N   . PRO A 1 452 ? 23.673  160.091 28.488  1.00 41.06 ? 452  PRO A N   1 
ATOM   3355 C  CA  . PRO A 1 452 ? 24.699  160.899 27.827  1.00 40.79 ? 452  PRO A CA  1 
ATOM   3356 C  C   . PRO A 1 452 ? 25.074  160.516 26.385  1.00 40.78 ? 452  PRO A C   1 
ATOM   3357 O  O   . PRO A 1 452 ? 25.605  161.367 25.693  1.00 40.05 ? 452  PRO A O   1 
ATOM   3358 C  CB  . PRO A 1 452 ? 25.930  160.680 28.722  1.00 41.76 ? 452  PRO A CB  1 
ATOM   3359 C  CG  . PRO A 1 452 ? 25.344  160.411 30.089  1.00 43.05 ? 452  PRO A CG  1 
ATOM   3360 C  CD  . PRO A 1 452 ? 24.095  159.602 29.810  1.00 41.49 ? 452  PRO A CD  1 
ATOM   3361 N  N   . MET A 1 453 ? 24.847  159.264 25.971  1.00 38.20 ? 453  MET A N   1 
ATOM   3362 C  CA  . MET A 1 453 ? 25.267  158.777 24.628  1.00 36.17 ? 453  MET A CA  1 
ATOM   3363 C  C   . MET A 1 453 ? 24.220  159.179 23.587  1.00 34.52 ? 453  MET A C   1 
ATOM   3364 O  O   . MET A 1 453 ? 24.536  159.098 22.392  1.00 35.66 ? 453  MET A O   1 
ATOM   3365 C  CB  . MET A 1 453 ? 25.464  157.259 24.608  1.00 38.61 ? 453  MET A CB  1 
ATOM   3366 C  CG  . MET A 1 453 ? 26.629  156.788 25.454  1.00 41.41 ? 453  MET A CG  1 
ATOM   3367 S  SD  . MET A 1 453 ? 28.225  157.279 24.753  1.00 47.75 ? 453  MET A SD  1 
ATOM   3368 C  CE  . MET A 1 453 ? 28.648  158.650 25.828  1.00 51.23 ? 453  MET A CE  1 
ATOM   3369 N  N   . GLY A 1 454 ? 23.023  159.579 24.026  1.00 35.12 ? 454  GLY A N   1 
ATOM   3370 C  CA  . GLY A 1 454 ? 21.947  160.084 23.148  1.00 36.09 ? 454  GLY A CA  1 
ATOM   3371 C  C   . GLY A 1 454 ? 21.086  158.971 22.565  1.00 36.07 ? 454  GLY A C   1 
ATOM   3372 O  O   . GLY A 1 454 ? 21.180  157.807 23.034  1.00 34.41 ? 454  GLY A O   1 
ATOM   3373 N  N   . ASP A 1 455 ? 20.291  159.304 21.547  1.00 34.63 ? 455  ASP A N   1 
ATOM   3374 C  CA  . ASP A 1 455 ? 19.157  158.464 21.085  1.00 35.44 ? 455  ASP A CA  1 
ATOM   3375 C  C   . ASP A 1 455 ? 19.658  157.235 20.310  1.00 32.67 ? 455  ASP A C   1 
ATOM   3376 O  O   . ASP A 1 455 ? 18.817  156.368 20.023  1.00 34.99 ? 455  ASP A O   1 
ATOM   3377 C  CB  . ASP A 1 455 ? 18.134  159.300 20.309  1.00 39.29 ? 455  ASP A CB  1 
ATOM   3378 C  CG  . ASP A 1 455 ? 18.484  159.525 18.853  1.00 40.37 ? 455  ASP A CG  1 
ATOM   3379 O  OD1 . ASP A 1 455 ? 19.680  159.735 18.567  1.00 47.46 ? 455  ASP A OD1 1 
ATOM   3380 O  OD2 . ASP A 1 455 ? 17.560  159.465 18.017  1.00 43.46 ? 455  ASP A OD2 1 
ATOM   3381 N  N   . ARG A 1 456 ? 20.960  157.141 20.011  1.00 31.09 ? 456  ARG A N   1 
ATOM   3382 C  CA  . ARG A 1 456 ? 21.572  155.946 19.358  1.00 31.01 ? 456  ARG A CA  1 
ATOM   3383 C  C   . ARG A 1 456 ? 21.195  154.667 20.127  1.00 30.16 ? 456  ARG A C   1 
ATOM   3384 O  O   . ARG A 1 456 ? 21.002  153.632 19.470  1.00 29.71 ? 456  ARG A O   1 
ATOM   3385 C  CB  . ARG A 1 456 ? 23.093  156.074 19.235  1.00 29.86 ? 456  ARG A CB  1 
ATOM   3386 C  CG  . ARG A 1 456 ? 23.793  154.840 18.674  1.00 30.91 ? 456  ARG A CG  1 
ATOM   3387 C  CD  . ARG A 1 456 ? 23.272  154.418 17.305  1.00 30.13 ? 456  ARG A CD  1 
ATOM   3388 N  NE  . ARG A 1 456 ? 23.881  153.198 16.786  1.00 31.87 ? 456  ARG A NE  1 
ATOM   3389 C  CZ  . ARG A 1 456 ? 23.442  151.951 16.996  1.00 31.02 ? 456  ARG A CZ  1 
ATOM   3390 N  NH1 . ARG A 1 456 ? 22.375  151.719 17.745  1.00 29.79 ? 456  ARG A NH1 1 
ATOM   3391 N  NH2 . ARG A 1 456 ? 24.087  150.933 16.453  1.00 29.98 ? 456  ARG A NH2 1 
ATOM   3392 N  N   . LEU A 1 457 ? 21.086  154.729 21.458  1.00 28.62 ? 457  LEU A N   1 
ATOM   3393 C  CA  . LEU A 1 457 ? 20.940  153.514 22.306  1.00 27.27 ? 457  LEU A CA  1 
ATOM   3394 C  C   . LEU A 1 457 ? 19.463  153.329 22.654  1.00 27.12 ? 457  LEU A C   1 
ATOM   3395 O  O   . LEU A 1 457 ? 19.137  153.203 23.836  1.00 27.91 ? 457  LEU A O   1 
ATOM   3396 C  CB  . LEU A 1 457 ? 21.825  153.637 23.549  1.00 27.54 ? 457  LEU A CB  1 
ATOM   3397 C  CG  . LEU A 1 457 ? 23.308  153.916 23.302  1.00 27.30 ? 457  LEU A CG  1 
ATOM   3398 C  CD1 . LEU A 1 457 ? 24.041  154.070 24.626  1.00 28.91 ? 457  LEU A CD1 1 
ATOM   3399 C  CD2 . LEU A 1 457 ? 23.968  152.832 22.465  1.00 27.05 ? 457  LEU A CD2 1 
ATOM   3400 N  N   . THR A 1 458 ? 18.602  153.318 21.636  1.00 27.22 ? 458  THR A N   1 
ATOM   3401 C  CA  . THR A 1 458 ? 17.134  153.154 21.781  1.00 27.68 ? 458  THR A CA  1 
ATOM   3402 C  C   . THR A 1 458 ? 16.650  152.236 20.666  1.00 27.11 ? 458  THR A C   1 
ATOM   3403 O  O   . THR A 1 458 ? 17.177  152.284 19.558  1.00 27.87 ? 458  THR A O   1 
ATOM   3404 C  CB  . THR A 1 458 ? 16.414  154.510 21.752  1.00 28.85 ? 458  THR A CB  1 
ATOM   3405 O  OG1 . THR A 1 458 ? 16.638  155.112 20.477  1.00 28.59 ? 458  THR A OG1 1 
ATOM   3406 C  CG2 . THR A 1 458 ? 16.892  155.450 22.838  1.00 29.83 ? 458  THR A CG2 1 
ATOM   3407 N  N   . PRO A 1 459 ? 15.669  151.348 20.924  1.00 27.31 ? 459  PRO A N   1 
ATOM   3408 C  CA  . PRO A 1 459 ? 15.103  150.513 19.864  1.00 27.46 ? 459  PRO A CA  1 
ATOM   3409 C  C   . PRO A 1 459 ? 14.599  151.332 18.664  1.00 28.08 ? 459  PRO A C   1 
ATOM   3410 O  O   . PRO A 1 459 ? 14.716  150.852 17.555  1.00 27.90 ? 459  PRO A O   1 
ATOM   3411 C  CB  . PRO A 1 459 ? 13.964  149.798 20.603  1.00 27.35 ? 459  PRO A CB  1 
ATOM   3412 C  CG  . PRO A 1 459 ? 14.482  149.681 22.009  1.00 26.77 ? 459  PRO A CG  1 
ATOM   3413 C  CD  . PRO A 1 459 ? 15.110  151.032 22.250  1.00 26.99 ? 459  PRO A CD  1 
ATOM   3414 N  N   . ARG A 1 460 ? 14.074  152.541 18.904  1.00 29.77 ? 460  ARG A N   1 
ATOM   3415 C  CA  . ARG A 1 460 ? 13.533  153.405 17.813  1.00 31.45 ? 460  ARG A CA  1 
ATOM   3416 C  C   . ARG A 1 460 ? 14.645  153.745 16.828  1.00 29.22 ? 460  ARG A C   1 
ATOM   3417 O  O   . ARG A 1 460 ? 14.440  153.654 15.621  1.00 28.58 ? 460  ARG A O   1 
ATOM   3418 C  CB  . ARG A 1 460 ? 12.898  154.691 18.344  1.00 34.33 ? 460  ARG A CB  1 
ATOM   3419 C  CG  . ARG A 1 460 ? 12.460  155.640 17.237  1.00 38.52 ? 460  ARG A CG  1 
ATOM   3420 C  CD  . ARG A 1 460 ? 12.012  156.999 17.739  1.00 43.30 ? 460  ARG A CD  1 
ATOM   3421 N  NE  . ARG A 1 460 ? 10.656  156.984 18.261  1.00 45.99 ? 460  ARG A NE  1 
ATOM   3422 C  CZ  . ARG A 1 460 ? 9.548   156.875 17.524  1.00 51.33 ? 460  ARG A CZ  1 
ATOM   3423 N  NH1 . ARG A 1 460 ? 9.609   156.749 16.206  1.00 51.02 ? 460  ARG A NH1 1 
ATOM   3424 N  NH2 . ARG A 1 460 ? 8.367   156.885 18.119  1.00 51.07 ? 460  ARG A NH2 1 
HETATM 3425 N  N   . MLZ A 1 461 ? 15.811  154.146 17.352  1.00 28.17 ? 461  MLZ A N   1 
HETATM 3426 C  CA  . MLZ A 1 461 ? 16.910  154.565 16.506  1.00 28.39 ? 461  MLZ A CA  1 
HETATM 3427 C  CB  . MLZ A 1 461 ? 17.930  155.394 17.290  1.00 30.16 ? 461  MLZ A CB  1 
HETATM 3428 C  CG  . MLZ A 1 461 ? 19.029  156.018 16.439  1.00 32.51 ? 461  MLZ A CG  1 
HETATM 3429 C  CD  . MLZ A 1 461 ? 18.519  156.842 15.265  1.00 34.15 ? 461  MLZ A CD  1 
HETATM 3430 C  CE  . MLZ A 1 461 ? 19.661  157.375 14.420  1.00 37.68 ? 461  MLZ A CE  1 
HETATM 3431 N  NZ  . MLZ A 1 461 ? 19.190  158.190 13.296  1.00 43.24 ? 461  MLZ A NZ  1 
HETATM 3432 C  CM  . MLZ A 1 461 ? 20.263  158.788 12.488  1.00 44.54 ? 461  MLZ A CM  1 
HETATM 3433 C  C   . MLZ A 1 461 ? 17.570  153.350 15.858  1.00 25.88 ? 461  MLZ A C   1 
HETATM 3434 O  O   . MLZ A 1 461 ? 17.927  153.424 14.693  1.00 24.36 ? 461  MLZ A O   1 
ATOM   3435 N  N   . SER A 1 462 ? 17.736  152.254 16.620  1.00 24.97 ? 462  SER A N   1 
ATOM   3436 C  CA  . SER A 1 462 ? 18.224  150.992 16.080  1.00 24.13 ? 462  SER A CA  1 
ATOM   3437 C  C   . SER A 1 462 ? 17.424  150.609 14.825  1.00 22.84 ? 462  SER A C   1 
ATOM   3438 O  O   . SER A 1 462 ? 18.032  150.279 13.809  1.00 22.48 ? 462  SER A O   1 
ATOM   3439 C  CB  . SER A 1 462 ? 18.158  149.886 17.111  1.00 24.59 ? 462  SER A CB  1 
ATOM   3440 O  OG  . SER A 1 462 ? 19.194  149.991 18.071  1.00 24.41 ? 462  SER A OG  1 
ATOM   3441 N  N   . PHE A 1 463 ? 16.098  150.670 14.899  1.00 24.10 ? 463  PHE A N   1 
ATOM   3442 C  CA  . PHE A 1 463 ? 15.191  150.258 13.801  1.00 24.36 ? 463  PHE A CA  1 
ATOM   3443 C  C   . PHE A 1 463 ? 15.425  151.192 12.607  1.00 25.58 ? 463  PHE A C   1 
ATOM   3444 O  O   . PHE A 1 463 ? 15.580  150.693 11.476  1.00 25.03 ? 463  PHE A O   1 
ATOM   3445 C  CB  . PHE A 1 463 ? 13.740  150.220 14.288  1.00 24.56 ? 463  PHE A CB  1 
ATOM   3446 C  CG  . PHE A 1 463 ? 12.774  149.410 13.451  1.00 25.63 ? 463  PHE A CG  1 
ATOM   3447 C  CD1 . PHE A 1 463 ? 13.210  148.519 12.476  1.00 24.52 ? 463  PHE A CD1 1 
ATOM   3448 C  CD2 . PHE A 1 463 ? 11.406  149.504 13.684  1.00 25.90 ? 463  PHE A CD2 1 
ATOM   3449 C  CE1 . PHE A 1 463 ? 12.305  147.772 11.735  1.00 25.13 ? 463  PHE A CE1 1 
ATOM   3450 C  CE2 . PHE A 1 463 ? 10.504  148.751 12.941  1.00 26.45 ? 463  PHE A CE2 1 
ATOM   3451 C  CZ  . PHE A 1 463 ? 10.951  147.887 11.968  1.00 25.59 ? 463  PHE A CZ  1 
ATOM   3452 N  N   . ALA A 1 464 ? 15.488  152.505 12.855  1.00 25.37 ? 464  ALA A N   1 
ATOM   3453 C  CA  . ALA A 1 464 ? 15.752  153.532 11.815  1.00 24.62 ? 464  ALA A CA  1 
ATOM   3454 C  C   . ALA A 1 464 ? 17.098  153.240 11.148  1.00 24.01 ? 464  ALA A C   1 
ATOM   3455 O  O   . ALA A 1 464 ? 17.164  153.286 9.905   1.00 24.41 ? 464  ALA A O   1 
ATOM   3456 C  CB  . ALA A 1 464 ? 15.713  154.924 12.397  1.00 24.48 ? 464  ALA A CB  1 
ATOM   3457 N  N   . ILE A 1 465 ? 18.132  152.931 11.933  1.00 24.34 ? 465  ILE A N   1 
ATOM   3458 C  CA  . ILE A 1 465 ? 19.482  152.614 11.381  1.00 25.07 ? 465  ILE A CA  1 
ATOM   3459 C  C   . ILE A 1 465 ? 19.379  151.352 10.515  1.00 26.10 ? 465  ILE A C   1 
ATOM   3460 O  O   . ILE A 1 465 ? 19.967  151.333 9.412   1.00 25.60 ? 465  ILE A O   1 
ATOM   3461 C  CB  . ILE A 1 465 ? 20.537  152.482 12.490  1.00 25.54 ? 465  ILE A CB  1 
ATOM   3462 C  CG1 . ILE A 1 465 ? 20.798  153.834 13.168  1.00 26.93 ? 465  ILE A CG1 1 
ATOM   3463 C  CG2 . ILE A 1 465 ? 21.818  151.882 11.933  1.00 26.03 ? 465  ILE A CG2 1 
ATOM   3464 C  CD1 . ILE A 1 465 ? 21.640  153.755 14.421  1.00 26.82 ? 465  ILE A CD1 1 
ATOM   3465 N  N   . TRP A 1 466 ? 18.671  150.320 10.976  1.00 24.90 ? 466  TRP A N   1 
ATOM   3466 C  CA  . TRP A 1 466 ? 18.547  149.080 10.165  1.00 24.65 ? 466  TRP A CA  1 
ATOM   3467 C  C   . TRP A 1 466 ? 17.958  149.440 8.802   1.00 24.17 ? 466  TRP A C   1 
ATOM   3468 O  O   . TRP A 1 466 ? 18.464  148.993 7.778   1.00 23.29 ? 466  TRP A O   1 
ATOM   3469 C  CB  . TRP A 1 466 ? 17.725  148.002 10.876  1.00 24.33 ? 466  TRP A CB  1 
ATOM   3470 C  CG  . TRP A 1 466 ? 17.438  146.842 9.977   1.00 23.54 ? 466  TRP A CG  1 
ATOM   3471 C  CD1 . TRP A 1 466 ? 18.268  145.805 9.680   1.00 23.04 ? 466  TRP A CD1 1 
ATOM   3472 C  CD2 . TRP A 1 466 ? 16.237  146.628 9.217   1.00 23.31 ? 466  TRP A CD2 1 
ATOM   3473 N  NE1 . TRP A 1 466 ? 17.656  144.945 8.809   1.00 23.35 ? 466  TRP A NE1 1 
ATOM   3474 C  CE2 . TRP A 1 466 ? 16.410  145.422 8.503   1.00 23.61 ? 466  TRP A CE2 1 
ATOM   3475 C  CE3 . TRP A 1 466 ? 15.027  147.316 9.096   1.00 23.06 ? 466  TRP A CE3 1 
ATOM   3476 C  CZ2 . TRP A 1 466 ? 15.421  144.897 7.669   1.00 23.54 ? 466  TRP A CZ2 1 
ATOM   3477 C  CZ3 . TRP A 1 466 ? 14.055  146.805 8.261   1.00 24.70 ? 466  TRP A CZ3 1 
ATOM   3478 C  CH2 . TRP A 1 466 ? 14.252  145.613 7.554   1.00 23.46 ? 466  TRP A CH2 1 
HETATM 3479 N  N   . MLZ A 1 467 ? 16.905  150.270 8.802   1.00 23.28 ? 467  MLZ A N   1 
HETATM 3480 C  CA  . MLZ A 1 467 ? 16.195  150.607 7.577   1.00 25.44 ? 467  MLZ A CA  1 
HETATM 3481 C  CB  . MLZ A 1 467 ? 14.981  151.491 7.857   1.00 26.15 ? 467  MLZ A CB  1 
HETATM 3482 C  CG  . MLZ A 1 467 ? 13.809  150.796 8.526   1.00 27.30 ? 467  MLZ A CG  1 
HETATM 3483 C  CD  . MLZ A 1 467 ? 12.651  151.725 8.795   1.00 27.75 ? 467  MLZ A CD  1 
HETATM 3484 C  CE  . MLZ A 1 467 ? 11.525  150.981 9.494   1.00 29.97 ? 467  MLZ A CE  1 
HETATM 3485 N  NZ  . MLZ A 1 467 ? 10.472  151.866 9.993   1.00 31.02 ? 467  MLZ A NZ  1 
HETATM 3486 C  CM  . MLZ A 1 467 ? 9.263   151.184 10.470  1.00 31.33 ? 467  MLZ A CM  1 
HETATM 3487 C  C   . MLZ A 1 467 ? 17.129  151.308 6.591   1.00 26.20 ? 467  MLZ A C   1 
HETATM 3488 O  O   . MLZ A 1 467 ? 17.069  151.042 5.390   1.00 24.19 ? 467  MLZ A O   1 
ATOM   3489 N  N   . GLU A 1 468 ? 18.001  152.181 7.104   1.00 27.23 ? 468  GLU A N   1 
ATOM   3490 C  CA  . GLU A 1 468 ? 18.978  152.864 6.269   1.00 27.62 ? 468  GLU A CA  1 
ATOM   3491 C  C   . GLU A 1 468 ? 19.946  151.834 5.678   1.00 26.96 ? 468  GLU A C   1 
ATOM   3492 O  O   . GLU A 1 468 ? 20.251  151.966 4.499   1.00 27.10 ? 468  GLU A O   1 
ATOM   3493 C  CB  . GLU A 1 468 ? 19.722  153.957 7.051   1.00 29.42 ? 468  GLU A CB  1 
ATOM   3494 N  N   . THR A 1 469 ? 20.392  150.833 6.445   1.00 26.94 ? 469  THR A N   1 
ATOM   3495 C  CA  . THR A 1 469 ? 21.351  149.802 5.944   1.00 28.02 ? 469  THR A CA  1 
ATOM   3496 C  C   . THR A 1 469 ? 20.727  148.902 4.862   1.00 27.46 ? 469  THR A C   1 
ATOM   3497 O  O   . THR A 1 469 ? 21.515  148.286 4.137   1.00 27.46 ? 469  THR A O   1 
ATOM   3498 C  CB  . THR A 1 469 ? 21.891  148.873 7.041   1.00 28.38 ? 469  THR A CB  1 
ATOM   3499 O  OG1 . THR A 1 469 ? 20.796  148.094 7.535   1.00 28.88 ? 469  THR A OG1 1 
ATOM   3500 C  CG2 . THR A 1 469 ? 22.583  149.611 8.167   1.00 28.74 ? 469  THR A CG2 1 
ATOM   3501 N  N   . VAL A 1 470 ? 19.397  148.762 4.770   1.00 28.20 ? 470  VAL A N   1 
ATOM   3502 C  CA  . VAL A 1 470 ? 18.757  147.858 3.754   1.00 27.13 ? 470  VAL A CA  1 
ATOM   3503 C  C   . VAL A 1 470 ? 18.000  148.678 2.702   1.00 27.72 ? 470  VAL A C   1 
ATOM   3504 O  O   . VAL A 1 470 ? 17.272  148.070 1.871   1.00 23.73 ? 470  VAL A O   1 
ATOM   3505 C  CB  . VAL A 1 470 ? 17.840  146.798 4.397   1.00 27.44 ? 470  VAL A CB  1 
ATOM   3506 C  CG1 . VAL A 1 470 ? 18.640  145.812 5.231   1.00 28.21 ? 470  VAL A CG1 1 
ATOM   3507 C  CG2 . VAL A 1 470 ? 16.698  147.404 5.197   1.00 27.17 ? 470  VAL A CG2 1 
ATOM   3508 N  N   . ARG A 1 471 ? 18.150  150.004 2.729   1.00 29.65 ? 471  ARG A N   1 
ATOM   3509 C  CA  . ARG A 1 471 ? 17.470  150.905 1.759   1.00 31.32 ? 471  ARG A CA  1 
ATOM   3510 C  C   . ARG A 1 471 ? 17.851  150.433 0.345   1.00 28.71 ? 471  ARG A C   1 
ATOM   3511 O  O   . ARG A 1 471 ? 19.042  150.136 0.131   1.00 26.46 ? 471  ARG A O   1 
ATOM   3512 C  CB  . ARG A 1 471 ? 17.834  152.371 2.029   1.00 34.37 ? 471  ARG A CB  1 
ATOM   3513 C  CG  . ARG A 1 471 ? 16.844  153.376 1.454   1.00 37.27 ? 471  ARG A CG  1 
ATOM   3514 C  CD  . ARG A 1 471 ? 17.195  154.816 1.792   1.00 40.44 ? 471  ARG A CD  1 
ATOM   3515 N  NE  . ARG A 1 471 ? 18.531  155.160 1.318   1.00 43.03 ? 471  ARG A NE  1 
ATOM   3516 C  CZ  . ARG A 1 471 ? 18.838  155.520 0.072   1.00 47.01 ? 471  ARG A CZ  1 
ATOM   3517 N  NH1 . ARG A 1 471 ? 17.901  155.599 -0.859  1.00 47.75 ? 471  ARG A NH1 1 
ATOM   3518 N  NH2 . ARG A 1 471 ? 20.094  155.786 -0.248  1.00 48.78 ? 471  ARG A NH2 1 
ATOM   3519 N  N   . LEU A 1 472 ? 16.859  150.285 -0.541  1.00 28.35 ? 472  LEU A N   1 
ATOM   3520 C  CA  . LEU A 1 472 ? 17.018  149.859 -1.964  1.00 29.92 ? 472  LEU A CA  1 
ATOM   3521 C  C   . LEU A 1 472 ? 17.474  148.396 -2.043  1.00 29.74 ? 472  LEU A C   1 
ATOM   3522 O  O   . LEU A 1 472 ? 17.950  147.986 -3.115  1.00 32.28 ? 472  LEU A O   1 
ATOM   3523 C  CB  . LEU A 1 472 ? 18.025  150.777 -2.674  1.00 31.64 ? 472  LEU A CB  1 
ATOM   3524 C  CG  . LEU A 1 472 ? 17.754  152.282 -2.590  1.00 32.07 ? 472  LEU A CG  1 
ATOM   3525 C  CD1 . LEU A 1 472 ? 18.747  153.051 -3.445  1.00 32.25 ? 472  LEU A CD1 1 
ATOM   3526 C  CD2 . LEU A 1 472 ? 16.329  152.621 -3.004  1.00 32.84 ? 472  LEU A CD2 1 
ATOM   3527 N  N   . GLN A 1 473 ? 17.303  147.617 -0.975  1.00 28.62 ? 473  GLN A N   1 
ATOM   3528 C  CA  . GLN A 1 473 ? 17.727  146.195 -0.945  1.00 29.49 ? 473  GLN A CA  1 
ATOM   3529 C  C   . GLN A 1 473 ? 16.540  145.296 -0.613  1.00 28.99 ? 473  GLN A C   1 
ATOM   3530 O  O   . GLN A 1 473 ? 15.650  145.729 0.138   1.00 27.13 ? 473  GLN A O   1 
ATOM   3531 C  CB  . GLN A 1 473 ? 18.818  145.943 0.090   1.00 30.98 ? 473  GLN A CB  1 
ATOM   3532 C  CG  . GLN A 1 473 ? 20.112  146.680 -0.198  1.00 33.33 ? 473  GLN A CG  1 
ATOM   3533 C  CD  . GLN A 1 473 ? 21.211  146.238 0.738   1.00 34.77 ? 473  GLN A CD  1 
ATOM   3534 O  OE1 . GLN A 1 473 ? 21.184  145.147 1.299   1.00 39.29 ? 473  GLN A OE1 1 
ATOM   3535 N  NE2 . GLN A 1 473 ? 22.189  147.101 0.925   1.00 37.10 ? 473  GLN A NE2 1 
ATOM   3536 N  N   . ALA A 1 474 ? 16.577  144.075 -1.147  1.00 28.20 ? 474  ALA A N   1 
ATOM   3537 C  CA  . ALA A 1 474 ? 15.578  143.014 -0.929  1.00 28.51 ? 474  ALA A CA  1 
ATOM   3538 C  C   . ALA A 1 474 ? 16.153  141.977 0.041   1.00 28.52 ? 474  ALA A C   1 
ATOM   3539 O  O   . ALA A 1 474 ? 17.369  142.033 0.344   1.00 26.79 ? 474  ALA A O   1 
ATOM   3540 C  CB  . ALA A 1 474 ? 15.222  142.393 -2.256  1.00 29.82 ? 474  ALA A CB  1 
ATOM   3541 N  N   . GLN A 1 475 ? 15.291  141.080 0.517   1.00 28.71 ? 475  GLN A N   1 
ATOM   3542 C  CA  . GLN A 1 475 ? 15.677  139.819 1.200   1.00 29.28 ? 475  GLN A CA  1 
ATOM   3543 C  C   . GLN A 1 475 ? 16.708  139.109 0.328   1.00 27.41 ? 475  GLN A C   1 
ATOM   3544 O  O   . GLN A 1 475 ? 16.441  138.854 -0.843  1.00 27.62 ? 475  GLN A O   1 
ATOM   3545 C  CB  . GLN A 1 475 ? 14.418  138.974 1.415   1.00 31.63 ? 475  GLN A CB  1 
ATOM   3546 C  CG  . GLN A 1 475 ? 14.673  137.631 2.079   1.00 34.25 ? 475  GLN A CG  1 
ATOM   3547 C  CD  . GLN A 1 475 ? 15.049  137.788 3.530   1.00 37.89 ? 475  GLN A CD  1 
ATOM   3548 O  OE1 . GLN A 1 475 ? 14.687  138.764 4.184   1.00 43.69 ? 475  GLN A OE1 1 
ATOM   3549 N  NE2 . GLN A 1 475 ? 15.789  136.822 4.047   1.00 40.10 ? 475  GLN A NE2 1 
ATOM   3550 N  N   . PRO A 1 476 ? 17.920  138.781 0.837   1.00 27.23 ? 476  PRO A N   1 
ATOM   3551 C  CA  . PRO A 1 476 ? 18.896  138.010 0.062   1.00 27.23 ? 476  PRO A CA  1 
ATOM   3552 C  C   . PRO A 1 476 ? 18.382  136.646 -0.432  1.00 26.11 ? 476  PRO A C   1 
ATOM   3553 O  O   . PRO A 1 476 ? 17.604  136.004 0.260   1.00 23.54 ? 476  PRO A O   1 
ATOM   3554 C  CB  . PRO A 1 476 ? 20.063  137.780 1.033   1.00 27.90 ? 476  PRO A CB  1 
ATOM   3555 C  CG  . PRO A 1 476 ? 19.925  138.888 2.059   1.00 29.17 ? 476  PRO A CG  1 
ATOM   3556 C  CD  . PRO A 1 476 ? 18.433  139.157 2.163   1.00 28.86 ? 476  PRO A CD  1 
ATOM   3557 N  N   . TRP A 1 477 ? 18.809  136.251 -1.632  1.00 26.36 ? 477  TRP A N   1 
ATOM   3558 C  CA  . TRP A 1 477 ? 18.512  134.914 -2.213  1.00 27.00 ? 477  TRP A CA  1 
ATOM   3559 C  C   . TRP A 1 477 ? 19.319  133.868 -1.432  1.00 29.64 ? 477  TRP A C   1 
ATOM   3560 O  O   . TRP A 1 477 ? 20.558  133.907 -1.504  1.00 31.08 ? 477  TRP A O   1 
ATOM   3561 C  CB  . TRP A 1 477 ? 18.805  134.884 -3.717  1.00 25.73 ? 477  TRP A CB  1 
ATOM   3562 C  CG  . TRP A 1 477 ? 18.083  135.948 -4.491  1.00 25.72 ? 477  TRP A CG  1 
ATOM   3563 C  CD1 . TRP A 1 477 ? 18.579  137.166 -4.856  1.00 25.47 ? 477  TRP A CD1 1 
ATOM   3564 C  CD2 . TRP A 1 477 ? 16.723  135.915 -4.967  1.00 24.17 ? 477  TRP A CD2 1 
ATOM   3565 N  NE1 . TRP A 1 477 ? 17.632  137.882 -5.537  1.00 25.58 ? 477  TRP A NE1 1 
ATOM   3566 C  CE2 . TRP A 1 477 ? 16.485  137.142 -5.625  1.00 24.44 ? 477  TRP A CE2 1 
ATOM   3567 C  CE3 . TRP A 1 477 ? 15.682  134.985 -4.897  1.00 23.90 ? 477  TRP A CE3 1 
ATOM   3568 C  CZ2 . TRP A 1 477 ? 15.257  137.452 -6.210  1.00 24.28 ? 477  TRP A CZ2 1 
ATOM   3569 C  CZ3 . TRP A 1 477 ? 14.473  135.284 -5.489  1.00 24.29 ? 477  TRP A CZ3 1 
ATOM   3570 C  CH2 . TRP A 1 477 ? 14.261  136.506 -6.126  1.00 23.80 ? 477  TRP A CH2 1 
ATOM   3571 N  N   . SER A 1 478 ? 18.631  132.987 -0.695  1.00 30.97 ? 478  SER A N   1 
ATOM   3572 C  CA  . SER A 1 478 ? 19.243  131.934 0.159   1.00 31.90 ? 478  SER A CA  1 
ATOM   3573 C  C   . SER A 1 478 ? 19.984  130.900 -0.695  1.00 34.29 ? 478  SER A C   1 
ATOM   3574 O  O   . SER A 1 478 ? 19.734  130.821 -1.921  1.00 32.55 ? 478  SER A O   1 
ATOM   3575 C  CB  . SER A 1 478 ? 18.194  131.244 0.978   1.00 30.84 ? 478  SER A CB  1 
ATOM   3576 O  OG  . SER A 1 478 ? 17.383  130.429 0.147   1.00 27.94 ? 478  SER A OG  1 
ATOM   3577 N  N   . GLU A 1 479 ? 20.807  130.079 -0.044  1.00 34.30 ? 479  GLU A N   1 
ATOM   3578 C  CA  . GLU A 1 479 ? 21.509  128.948 -0.704  1.00 35.32 ? 479  GLU A CA  1 
ATOM   3579 C  C   . GLU A 1 479 ? 20.447  127.975 -1.248  1.00 32.95 ? 479  GLU A C   1 
ATOM   3580 O  O   . GLU A 1 479 ? 20.675  127.432 -2.335  1.00 30.90 ? 479  GLU A O   1 
ATOM   3581 C  CB  . GLU A 1 479 ? 22.545  128.328 0.242   1.00 37.62 ? 479  GLU A CB  1 
ATOM   3582 C  CG  . GLU A 1 479 ? 21.970  127.755 1.523   1.00 41.53 ? 479  GLU A CG  1 
ATOM   3583 C  CD  . GLU A 1 479 ? 21.347  126.380 1.375   1.00 46.11 ? 479  GLU A CD  1 
ATOM   3584 O  OE1 . GLU A 1 479 ? 21.787  125.629 0.476   1.00 50.31 ? 479  GLU A OE1 1 
ATOM   3585 O  OE2 . GLU A 1 479 ? 20.407  126.066 2.137   1.00 49.52 ? 479  GLU A OE2 1 
ATOM   3586 N  N   . ALA A 1 480 ? 19.315  127.800 -0.552  1.00 29.99 ? 480  ALA A N   1 
ATOM   3587 C  CA  . ALA A 1 480 ? 18.176  126.963 -0.998  1.00 30.03 ? 480  ALA A CA  1 
ATOM   3588 C  C   . ALA A 1 480 ? 17.535  127.561 -2.261  1.00 29.99 ? 480  ALA A C   1 
ATOM   3589 O  O   . ALA A 1 480 ? 17.328  126.808 -3.228  1.00 30.39 ? 480  ALA A O   1 
ATOM   3590 C  CB  . ALA A 1 480 ? 17.162  126.815 0.108   1.00 31.48 ? 480  ALA A CB  1 
ATOM   3591 N  N   . ASP A 1 481 ? 17.216  128.857 -2.252  1.00 30.33 ? 481  ASP A N   1 
ATOM   3592 C  CA  . ASP A 1 481 ? 16.664  129.574 -3.438  1.00 30.01 ? 481  ASP A CA  1 
ATOM   3593 C  C   . ASP A 1 481 ? 17.566  129.313 -4.653  1.00 29.45 ? 481  ASP A C   1 
ATOM   3594 O  O   . ASP A 1 481 ? 17.042  129.002 -5.735  1.00 28.64 ? 481  ASP A O   1 
ATOM   3595 C  CB  . ASP A 1 481 ? 16.565  131.081 -3.196  1.00 29.67 ? 481  ASP A CB  1 
ATOM   3596 C  CG  . ASP A 1 481 ? 15.599  131.497 -2.100  1.00 31.19 ? 481  ASP A CG  1 
ATOM   3597 O  OD1 . ASP A 1 481 ? 14.650  130.731 -1.825  1.00 29.75 ? 481  ASP A OD1 1 
ATOM   3598 O  OD2 . ASP A 1 481 ? 15.811  132.599 -1.530  1.00 30.17 ? 481  ASP A OD2 1 
ATOM   3599 N  N   . ARG A 1 482 ? 18.882  129.422 -4.461  1.00 29.79 ? 482  ARG A N   1 
ATOM   3600 C  CA  . ARG A 1 482 ? 19.893  129.245 -5.541  1.00 31.92 ? 482  ARG A CA  1 
ATOM   3601 C  C   . ARG A 1 482 ? 19.899  127.786 -6.007  1.00 31.54 ? 482  ARG A C   1 
ATOM   3602 O  O   . ARG A 1 482 ? 20.029  127.568 -7.217  1.00 34.63 ? 482  ARG A O   1 
ATOM   3603 C  CB  . ARG A 1 482 ? 21.271  129.697 -5.055  1.00 32.83 ? 482  ARG A CB  1 
ATOM   3604 C  CG  . ARG A 1 482 ? 21.394  131.210 -4.960  1.00 35.01 ? 482  ARG A CG  1 
ATOM   3605 C  CD  . ARG A 1 482 ? 22.574  131.665 -4.132  1.00 35.00 ? 482  ARG A CD  1 
ATOM   3606 N  NE  . ARG A 1 482 ? 22.582  133.117 -4.042  1.00 35.97 ? 482  ARG A NE  1 
ATOM   3607 C  CZ  . ARG A 1 482 ? 23.058  133.937 -4.975  1.00 36.35 ? 482  ARG A CZ  1 
ATOM   3608 N  NH1 . ARG A 1 482 ? 23.579  133.460 -6.097  1.00 36.01 ? 482  ARG A NH1 1 
ATOM   3609 N  NH2 . ARG A 1 482 ? 23.001  135.242 -4.783  1.00 38.21 ? 482  ARG A NH2 1 
ATOM   3610 N  N   . GLU A 1 483 ? 19.754  126.829 -5.089  1.00 31.77 ? 483  GLU A N   1 
ATOM   3611 C  CA  . GLU A 1 483 ? 19.693  125.385 -5.439  1.00 33.42 ? 483  GLU A CA  1 
ATOM   3612 C  C   . GLU A 1 483 ? 18.443  125.147 -6.292  1.00 32.13 ? 483  GLU A C   1 
ATOM   3613 O  O   . GLU A 1 483 ? 18.556  124.484 -7.335  1.00 32.48 ? 483  GLU A O   1 
ATOM   3614 C  CB  . GLU A 1 483 ? 19.697  124.492 -4.199  1.00 36.38 ? 483  GLU A CB  1 
ATOM   3615 C  CG  . GLU A 1 483 ? 19.858  123.016 -4.530  1.00 39.64 ? 483  GLU A CG  1 
ATOM   3616 C  CD  . GLU A 1 483 ? 19.909  122.085 -3.328  1.00 44.06 ? 483  GLU A CD  1 
ATOM   3617 O  OE1 . GLU A 1 483 ? 19.142  121.093 -3.308  1.00 46.84 ? 483  GLU A OE1 1 
ATOM   3618 O  OE2 . GLU A 1 483 ? 20.723  122.346 -2.417  1.00 47.87 ? 483  GLU A OE2 1 
ATOM   3619 N  N   . ILE A 1 484 ? 17.297  125.690 -5.878  1.00 30.64 ? 484  ILE A N   1 
ATOM   3620 C  CA  . ILE A 1 484 ? 16.019  125.565 -6.636  1.00 28.88 ? 484  ILE A CA  1 
ATOM   3621 C  C   . ILE A 1 484 ? 16.193  126.214 -8.024  1.00 26.86 ? 484  ILE A C   1 
ATOM   3622 O  O   . ILE A 1 484 ? 15.709  125.634 -9.010  1.00 28.85 ? 484  ILE A O   1 
ATOM   3623 C  CB  . ILE A 1 484 ? 14.841  126.149 -5.832  1.00 28.87 ? 484  ILE A CB  1 
ATOM   3624 C  CG1 . ILE A 1 484 ? 14.564  125.322 -4.573  1.00 31.63 ? 484  ILE A CG1 1 
ATOM   3625 C  CG2 . ILE A 1 484 ? 13.602  126.255 -6.707  1.00 28.81 ? 484  ILE A CG2 1 
ATOM   3626 C  CD1 . ILE A 1 484 ? 13.812  126.062 -3.489  1.00 31.47 ? 484  ILE A CD1 1 
ATOM   3627 N  N   . ALA A 1 485 ? 16.839  127.378 -8.103  1.00 27.24 ? 485  ALA A N   1 
ATOM   3628 C  CA  . ALA A 1 485 ? 17.079  128.114 -9.369  1.00 27.05 ? 485  ALA A CA  1 
ATOM   3629 C  C   . ALA A 1 485 ? 17.945  127.260 -10.304 1.00 27.70 ? 485  ALA A C   1 
ATOM   3630 O  O   . ALA A 1 485 ? 17.665  127.229 -11.514 1.00 26.64 ? 485  ALA A O   1 
ATOM   3631 C  CB  . ALA A 1 485 ? 17.733  129.443 -9.099  1.00 27.86 ? 485  ALA A CB  1 
ATOM   3632 N  N   . GLU A 1 486 ? 18.971  126.604 -9.761  1.00 29.30 ? 486  GLU A N   1 
ATOM   3633 C  CA  . GLU A 1 486 ? 19.888  125.743 -10.553 1.00 31.58 ? 486  GLU A CA  1 
ATOM   3634 C  C   . GLU A 1 486 ? 19.098  124.547 -11.104 1.00 29.97 ? 486  GLU A C   1 
ATOM   3635 O  O   . GLU A 1 486 ? 19.307  124.199 -12.285 1.00 29.61 ? 486  GLU A O   1 
ATOM   3636 C  CB  . GLU A 1 486 ? 21.090  125.326 -9.703  1.00 33.99 ? 486  GLU A CB  1 
ATOM   3637 C  CG  . GLU A 1 486 ? 22.052  124.396 -10.417 1.00 36.08 ? 486  GLU A CG  1 
ATOM   3638 C  CD  . GLU A 1 486 ? 22.718  124.976 -11.654 1.00 38.58 ? 486  GLU A CD  1 
ATOM   3639 O  OE1 . GLU A 1 486 ? 22.616  126.198 -11.873 1.00 41.40 ? 486  GLU A OE1 1 
ATOM   3640 O  OE2 . GLU A 1 486 ? 23.351  124.198 -12.392 1.00 42.26 ? 486  GLU A OE2 1 
ATOM   3641 N  N   . ALA A 1 487 ? 18.227  123.943 -10.290 1.00 28.44 ? 487  ALA A N   1 
ATOM   3642 C  CA  . ALA A 1 487 ? 17.365  122.809 -10.706 1.00 29.10 ? 487  ALA A CA  1 
ATOM   3643 C  C   . ALA A 1 487 ? 16.450  123.267 -11.847 1.00 28.24 ? 487  ALA A C   1 
ATOM   3644 O  O   . ALA A 1 487 ? 16.228  122.478 -12.762 1.00 26.63 ? 487  ALA A O   1 
ATOM   3645 C  CB  . ALA A 1 487 ? 16.574  122.276 -9.535  1.00 29.16 ? 487  ALA A CB  1 
ATOM   3646 N  N   . ALA A 1 488 ? 15.952  124.508 -11.791 1.00 27.59 ? 488  ALA A N   1 
ATOM   3647 C  CA  . ALA A 1 488 ? 15.085  125.103 -12.835 1.00 26.80 ? 488  ALA A CA  1 
ATOM   3648 C  C   . ALA A 1 488 ? 15.899  125.339 -14.113 1.00 26.08 ? 488  ALA A C   1 
ATOM   3649 O  O   . ALA A 1 488 ? 15.403  124.994 -15.187 1.00 26.54 ? 488  ALA A O   1 
ATOM   3650 C  CB  . ALA A 1 488 ? 14.461  126.388 -12.343 1.00 26.78 ? 488  ALA A CB  1 
ATOM   3651 N  N   . ARG A 1 489 ? 17.094  125.920 -14.002 1.00 26.63 ? 489  ARG A N   1 
ATOM   3652 C  CA  . ARG A 1 489 ? 17.962  126.187 -15.187 1.00 28.29 ? 489  ARG A CA  1 
ATOM   3653 C  C   . ARG A 1 489 ? 18.162  124.880 -15.959 1.00 29.40 ? 489  ARG A C   1 
ATOM   3654 O  O   . ARG A 1 489 ? 18.045  124.857 -17.197 1.00 27.05 ? 489  ARG A O   1 
ATOM   3655 C  CB  . ARG A 1 489 ? 19.327  126.730 -14.764 1.00 29.47 ? 489  ARG A CB  1 
ATOM   3656 C  CG  . ARG A 1 489 ? 20.207  127.151 -15.936 1.00 29.41 ? 489  ARG A CG  1 
ATOM   3657 C  CD  . ARG A 1 489 ? 21.585  127.566 -15.472 1.00 29.98 ? 489  ARG A CD  1 
ATOM   3658 N  NE  . ARG A 1 489 ? 22.342  126.444 -14.935 1.00 30.61 ? 489  ARG A NE  1 
ATOM   3659 C  CZ  . ARG A 1 489 ? 22.931  125.498 -15.668 1.00 32.72 ? 489  ARG A CZ  1 
ATOM   3660 N  NH1 . ARG A 1 489 ? 22.843  125.508 -16.987 1.00 32.01 ? 489  ARG A NH1 1 
ATOM   3661 N  NH2 . ARG A 1 489 ? 23.602  124.531 -15.071 1.00 34.57 ? 489  ARG A NH2 1 
ATOM   3662 N  N   . ILE A 1 490 ? 18.448  123.823 -15.210 1.00 31.59 ? 490  ILE A N   1 
ATOM   3663 C  CA  . ILE A 1 490 ? 18.867  122.498 -15.739 1.00 32.88 ? 490  ILE A CA  1 
ATOM   3664 C  C   . ILE A 1 490 ? 17.648  121.773 -16.329 1.00 33.05 ? 490  ILE A C   1 
ATOM   3665 O  O   . ILE A 1 490 ? 17.810  121.117 -17.378 1.00 31.35 ? 490  ILE A O   1 
ATOM   3666 C  CB  . ILE A 1 490 ? 19.555  121.734 -14.598 1.00 36.65 ? 490  ILE A CB  1 
ATOM   3667 C  CG1 . ILE A 1 490 ? 21.054  122.031 -14.547 1.00 38.44 ? 490  ILE A CG1 1 
ATOM   3668 C  CG2 . ILE A 1 490 ? 19.258  120.263 -14.683 1.00 39.25 ? 490  ILE A CG2 1 
ATOM   3669 C  CD1 . ILE A 1 490 ? 21.696  121.669 -13.225 1.00 41.73 ? 490  ILE A CD1 1 
ATOM   3670 N  N   . ALA A 1 491 ? 16.479  121.878 -15.685 1.00 29.76 ? 491  ALA A N   1 
ATOM   3671 C  CA  . ALA A 1 491 ? 15.190  121.383 -16.224 1.00 29.87 ? 491  ALA A CA  1 
ATOM   3672 C  C   . ALA A 1 491 ? 14.897  122.054 -17.574 1.00 29.73 ? 491  ALA A C   1 
ATOM   3673 O  O   . ALA A 1 491 ? 14.462  121.349 -18.506 1.00 26.61 ? 491  ALA A O   1 
ATOM   3674 C  CB  . ALA A 1 491 ? 14.068  121.624 -15.253 1.00 30.06 ? 491  ALA A CB  1 
ATOM   3675 N  N   . LEU A 1 492 ? 15.110  123.367 -17.675 1.00 28.04 ? 492  LEU A N   1 
ATOM   3676 C  CA  . LEU A 1 492 ? 14.821  124.139 -18.909 1.00 29.39 ? 492  LEU A CA  1 
ATOM   3677 C  C   . LEU A 1 492 ? 15.826  123.771 -20.009 1.00 29.23 ? 492  LEU A C   1 
ATOM   3678 O  O   . LEU A 1 492 ? 15.389  123.668 -21.171 1.00 27.87 ? 492  LEU A O   1 
ATOM   3679 C  CB  . LEU A 1 492 ? 14.810  125.634 -18.583 1.00 31.18 ? 492  LEU A CB  1 
ATOM   3680 C  CG  . LEU A 1 492 ? 13.641  126.076 -17.694 1.00 33.17 ? 492  LEU A CG  1 
ATOM   3681 C  CD1 . LEU A 1 492 ? 13.901  127.433 -17.071 1.00 34.67 ? 492  LEU A CD1 1 
ATOM   3682 C  CD2 . LEU A 1 492 ? 12.332  126.101 -18.469 1.00 34.85 ? 492  LEU A CD2 1 
ATOM   3683 N  N   . VAL A 1 493 ? 17.100  123.536 -19.670 1.00 29.51 ? 493  VAL A N   1 
ATOM   3684 C  CA  . VAL A 1 493 ? 18.119  123.033 -20.645 1.00 29.60 ? 493  VAL A CA  1 
ATOM   3685 C  C   . VAL A 1 493 ? 17.596  121.730 -21.251 1.00 30.41 ? 493  VAL A C   1 
ATOM   3686 O  O   . VAL A 1 493 ? 17.662  121.564 -22.490 1.00 31.14 ? 493  VAL A O   1 
ATOM   3687 C  CB  . VAL A 1 493 ? 19.495  122.807 -19.996 1.00 30.08 ? 493  VAL A CB  1 
ATOM   3688 C  CG1 . VAL A 1 493 ? 20.351  121.845 -20.813 1.00 30.69 ? 493  VAL A CG1 1 
ATOM   3689 C  CG2 . VAL A 1 493 ? 20.224  124.119 -19.772 1.00 29.71 ? 493  VAL A CG2 1 
ATOM   3690 N  N   . GLU A 1 494 ? 17.096  120.844 -20.389 1.00 29.76 ? 494  GLU A N   1 
ATOM   3691 C  CA  . GLU A 1 494 ? 16.581  119.508 -20.773 1.00 31.10 ? 494  GLU A CA  1 
ATOM   3692 C  C   . GLU A 1 494 ? 15.354  119.667 -21.688 1.00 31.70 ? 494  GLU A C   1 
ATOM   3693 O  O   . GLU A 1 494 ? 15.313  118.974 -22.734 1.00 30.47 ? 494  GLU A O   1 
ATOM   3694 C  CB  . GLU A 1 494 ? 16.307  118.679 -19.524 1.00 31.94 ? 494  GLU A CB  1 
ATOM   3695 C  CG  . GLU A 1 494 ? 15.874  117.277 -19.872 1.00 36.37 ? 494  GLU A CG  1 
ATOM   3696 C  CD  . GLU A 1 494 ? 16.013  116.232 -18.783 1.00 36.44 ? 494  GLU A CD  1 
ATOM   3697 O  OE1 . GLU A 1 494 ? 16.364  116.587 -17.637 1.00 36.12 ? 494  GLU A OE1 1 
ATOM   3698 O  OE2 . GLU A 1 494 ? 15.740  115.060 -19.095 1.00 42.20 ? 494  GLU A OE2 1 
ATOM   3699 N  N   . VAL A 1 495 ? 14.412  120.553 -21.343 1.00 29.96 ? 495  VAL A N   1 
ATOM   3700 C  CA  . VAL A 1 495 ? 13.239  120.878 -22.213 1.00 30.56 ? 495  VAL A CA  1 
ATOM   3701 C  C   . VAL A 1 495 ? 13.762  121.254 -23.603 1.00 29.91 ? 495  VAL A C   1 
ATOM   3702 O  O   . VAL A 1 495 ? 13.291  120.660 -24.581 1.00 32.22 ? 495  VAL A O   1 
ATOM   3703 C  CB  . VAL A 1 495 ? 12.356  122.000 -21.631 1.00 30.93 ? 495  VAL A CB  1 
ATOM   3704 C  CG1 . VAL A 1 495 ? 11.408  122.571 -22.676 1.00 30.66 ? 495  VAL A CG1 1 
ATOM   3705 C  CG2 . VAL A 1 495 ? 11.586  121.528 -20.409 1.00 31.10 ? 495  VAL A CG2 1 
ATOM   3706 N  N   . ALA A 1 496 ? 14.713  122.185 -23.680 1.00 30.96 ? 496  ALA A N   1 
ATOM   3707 C  CA  . ALA A 1 496 ? 15.251  122.719 -24.954 1.00 32.77 ? 496  ALA A CA  1 
ATOM   3708 C  C   . ALA A 1 496 ? 15.955  121.597 -25.732 1.00 35.25 ? 496  ALA A C   1 
ATOM   3709 O  O   . ALA A 1 496 ? 15.718  121.485 -26.953 1.00 36.00 ? 496  ALA A O   1 
ATOM   3710 C  CB  . ALA A 1 496 ? 16.173  123.882 -24.694 1.00 32.95 ? 496  ALA A CB  1 
ATOM   3711 N  N   . PHE A 1 497 ? 16.771  120.784 -25.055 1.00 35.62 ? 497  PHE A N   1 
ATOM   3712 C  CA  . PHE A 1 497 ? 17.533  119.676 -25.687 1.00 37.21 ? 497  PHE A CA  1 
ATOM   3713 C  C   . PHE A 1 497 ? 16.567  118.642 -26.275 1.00 36.66 ? 497  PHE A C   1 
ATOM   3714 O  O   . PHE A 1 497 ? 16.729  118.302 -27.468 1.00 35.54 ? 497  PHE A O   1 
ATOM   3715 C  CB  . PHE A 1 497 ? 18.493  119.001 -24.708 1.00 39.42 ? 497  PHE A CB  1 
ATOM   3716 C  CG  . PHE A 1 497 ? 19.271  117.873 -25.338 1.00 40.66 ? 497  PHE A CG  1 
ATOM   3717 C  CD1 . PHE A 1 497 ? 20.152  118.120 -26.380 1.00 43.54 ? 497  PHE A CD1 1 
ATOM   3718 C  CD2 . PHE A 1 497 ? 19.104  116.565 -24.912 1.00 41.93 ? 497  PHE A CD2 1 
ATOM   3719 C  CE1 . PHE A 1 497 ? 20.864  117.085 -26.968 1.00 43.40 ? 497  PHE A CE1 1 
ATOM   3720 C  CE2 . PHE A 1 497 ? 19.818  115.532 -25.500 1.00 43.75 ? 497  PHE A CE2 1 
ATOM   3721 C  CZ  . PHE A 1 497 ? 20.692  115.793 -26.530 1.00 43.36 ? 497  PHE A CZ  1 
ATOM   3722 N  N   . HIS A 1 498 ? 15.617  118.141 -25.479 1.00 35.50 ? 498  HIS A N   1 
ATOM   3723 C  CA  . HIS A 1 498 ? 14.658  117.087 -25.915 1.00 39.27 ? 498  HIS A CA  1 
ATOM   3724 C  C   . HIS A 1 498 ? 13.813  117.631 -27.069 1.00 40.24 ? 498  HIS A C   1 
ATOM   3725 O  O   . HIS A 1 498 ? 13.444  116.842 -27.952 1.00 38.01 ? 498  HIS A O   1 
ATOM   3726 C  CB  . HIS A 1 498 ? 13.792  116.566 -24.762 1.00 40.02 ? 498  HIS A CB  1 
ATOM   3727 C  CG  . HIS A 1 498 ? 14.571  115.898 -23.681 1.00 44.03 ? 498  HIS A CG  1 
ATOM   3728 N  ND1 . HIS A 1 498 ? 15.720  115.170 -23.937 1.00 46.30 ? 498  HIS A ND1 1 
ATOM   3729 C  CD2 . HIS A 1 498 ? 14.371  115.838 -22.348 1.00 44.58 ? 498  HIS A CD2 1 
ATOM   3730 C  CE1 . HIS A 1 498 ? 16.200  114.698 -22.804 1.00 48.48 ? 498  HIS A CE1 1 
ATOM   3731 N  NE2 . HIS A 1 498 ? 15.388  115.093 -21.814 1.00 46.95 ? 498  HIS A NE2 1 
ATOM   3732 N  N   . HIS A 1 499 ? 13.543  118.937 -27.068 1.00 40.99 ? 499  HIS A N   1 
ATOM   3733 C  CA  . HIS A 1 499 ? 12.781  119.608 -28.150 1.00 44.94 ? 499  HIS A CA  1 
ATOM   3734 C  C   . HIS A 1 499 ? 13.600  119.572 -29.448 1.00 45.65 ? 499  HIS A C   1 
ATOM   3735 O  O   . HIS A 1 499 ? 13.016  119.222 -30.481 1.00 48.49 ? 499  HIS A O   1 
ATOM   3736 C  CB  . HIS A 1 499 ? 12.370  121.022 -27.743 1.00 45.31 ? 499  HIS A CB  1 
ATOM   3737 C  CG  . HIS A 1 499 ? 11.422  121.629 -28.713 1.00 46.70 ? 499  HIS A CG  1 
ATOM   3738 N  ND1 . HIS A 1 499 ? 11.839  122.515 -29.691 1.00 47.68 ? 499  HIS A ND1 1 
ATOM   3739 C  CD2 . HIS A 1 499 ? 10.096  121.440 -28.896 1.00 46.79 ? 499  HIS A CD2 1 
ATOM   3740 C  CE1 . HIS A 1 499 ? 10.804  122.869 -30.420 1.00 48.80 ? 499  HIS A CE1 1 
ATOM   3741 N  NE2 . HIS A 1 499 ? 9.722   122.220 -29.954 1.00 49.71 ? 499  HIS A NE2 1 
ATOM   3742 N  N   . SER A 1 500 ? 14.900  119.888 -29.395 1.00 44.46 ? 500  SER A N   1 
ATOM   3743 C  CA  . SER A 1 500 ? 15.796  119.856 -30.590 1.00 46.56 ? 500  SER A CA  1 
ATOM   3744 C  C   . SER A 1 500 ? 15.982  118.404 -31.065 1.00 48.75 ? 500  SER A C   1 
ATOM   3745 O  O   . SER A 1 500 ? 15.997  118.184 -32.294 1.00 50.28 ? 500  SER A O   1 
ATOM   3746 C  CB  . SER A 1 500 ? 17.112  120.549 -30.350 1.00 45.49 ? 500  SER A CB  1 
ATOM   3747 O  OG  . SER A 1 500 ? 17.711  120.117 -29.142 1.00 50.77 ? 500  SER A OG  1 
ATOM   3748 N  N   . GLU A 1 501 ? 16.064  117.443 -30.135 1.00 47.63 ? 501  GLU A N   1 
ATOM   3749 C  CA  . GLU A 1 501 ? 16.173  115.989 -30.442 1.00 48.40 ? 501  GLU A CA  1 
ATOM   3750 C  C   . GLU A 1 501 ? 15.013  115.550 -31.347 1.00 51.48 ? 501  GLU A C   1 
ATOM   3751 O  O   . GLU A 1 501 ? 15.279  114.818 -32.321 1.00 51.38 ? 501  GLU A O   1 
ATOM   3752 C  CB  . GLU A 1 501 ? 16.177  115.137 -29.168 1.00 48.27 ? 501  GLU A CB  1 
ATOM   3753 C  CG  . GLU A 1 501 ? 17.527  115.047 -28.472 1.00 46.47 ? 501  GLU A CG  1 
ATOM   3754 C  CD  . GLU A 1 501 ? 17.530  114.097 -27.281 1.00 47.21 ? 501  GLU A CD  1 
ATOM   3755 O  OE1 . GLU A 1 501 ? 16.636  114.226 -26.426 1.00 45.48 ? 501  GLU A OE1 1 
ATOM   3756 O  OE2 . GLU A 1 501 ? 18.406  113.207 -27.225 1.00 45.65 ? 501  GLU A OE2 1 
ATOM   3757 N  N   . HIS A 1 502 ? 13.778  115.952 -31.031 1.00 54.67 ? 502  HIS A N   1 
ATOM   3758 C  CA  . HIS A 1 502 ? 12.543  115.484 -31.724 1.00 59.19 ? 502  HIS A CA  1 
ATOM   3759 C  C   . HIS A 1 502 ? 12.057  116.497 -32.776 1.00 63.00 ? 502  HIS A C   1 
ATOM   3760 O  O   . HIS A 1 502 ? 11.117  116.148 -33.513 1.00 69.29 ? 502  HIS A O   1 
ATOM   3761 C  CB  . HIS A 1 502 ? 11.441  115.162 -30.706 1.00 60.54 ? 502  HIS A CB  1 
ATOM   3762 C  CG  . HIS A 1 502 ? 11.846  114.184 -29.654 1.00 61.87 ? 502  HIS A CG  1 
ATOM   3763 N  ND1 . HIS A 1 502 ? 12.071  112.848 -29.928 1.00 63.11 ? 502  HIS A ND1 1 
ATOM   3764 C  CD2 . HIS A 1 502 ? 12.047  114.335 -28.326 1.00 62.08 ? 502  HIS A CD2 1 
ATOM   3765 C  CE1 . HIS A 1 502 ? 12.404  112.221 -28.815 1.00 62.86 ? 502  HIS A CE1 1 
ATOM   3766 N  NE2 . HIS A 1 502 ? 12.397  113.113 -27.817 1.00 61.75 ? 502  HIS A NE2 1 
ATOM   3767 N  N   . HIS A 1 503 ? 12.648  117.696 -32.842 1.00 65.60 ? 503  HIS A N   1 
ATOM   3768 C  CA  . HIS A 1 503 ? 12.291  118.774 -33.808 1.00 68.10 ? 503  HIS A CA  1 
ATOM   3769 C  C   . HIS A 1 503 ? 13.571  119.407 -34.365 1.00 68.75 ? 503  HIS A C   1 
ATOM   3770 O  O   . HIS A 1 503 ? 13.696  119.590 -35.575 1.00 71.52 ? 503  HIS A O   1 
ATOM   3771 C  CB  . HIS A 1 503 ? 11.387  119.841 -33.163 1.00 70.63 ? 503  HIS A CB  1 
ATOM   3772 C  CG  . HIS A 1 503 ? 10.142  119.311 -32.529 1.00 71.91 ? 503  HIS A CG  1 
ATOM   3773 N  ND1 . HIS A 1 503 ? 8.899   119.421 -33.132 1.00 73.66 ? 503  HIS A ND1 1 
ATOM   3774 C  CD2 . HIS A 1 503 ? 9.934   118.689 -31.346 1.00 70.60 ? 503  HIS A CD2 1 
ATOM   3775 C  CE1 . HIS A 1 503 ? 7.984   118.882 -32.349 1.00 73.46 ? 503  HIS A CE1 1 
ATOM   3776 N  NE2 . HIS A 1 503 ? 8.594   118.425 -31.246 1.00 71.81 ? 503  HIS A NE2 1 
ATOM   3777 N  N   . TYR B 2 6   ? -1.539  73.283  19.856  1.00 79.52 ? 6    TYR B N   1 
ATOM   3778 C  CA  . TYR B 2 6   ? -0.602  74.047  18.975  1.00 79.77 ? 6    TYR B CA  1 
ATOM   3779 C  C   . TYR B 2 6   ? 0.853   73.738  19.350  1.00 78.36 ? 6    TYR B C   1 
ATOM   3780 O  O   . TYR B 2 6   ? 1.210   73.860  20.539  1.00 82.68 ? 6    TYR B O   1 
ATOM   3781 C  CB  . TYR B 2 6   ? -0.838  75.557  19.077  1.00 80.40 ? 6    TYR B CB  1 
ATOM   3782 C  CG  . TYR B 2 6   ? 0.189   76.390  18.350  1.00 80.28 ? 6    TYR B CG  1 
ATOM   3783 C  CD1 . TYR B 2 6   ? 0.294   76.340  16.968  1.00 79.18 ? 6    TYR B CD1 1 
ATOM   3784 C  CD2 . TYR B 2 6   ? 1.066   77.217  19.037  1.00 77.83 ? 6    TYR B CD2 1 
ATOM   3785 C  CE1 . TYR B 2 6   ? 1.236   77.092  16.284  1.00 77.44 ? 6    TYR B CE1 1 
ATOM   3786 C  CE2 . TYR B 2 6   ? 2.015   77.976  18.368  1.00 78.13 ? 6    TYR B CE2 1 
ATOM   3787 C  CZ  . TYR B 2 6   ? 2.099   77.914  16.986  1.00 77.79 ? 6    TYR B CZ  1 
ATOM   3788 O  OH  . TYR B 2 6   ? 3.023   78.653  16.307  1.00 72.44 ? 6    TYR B OH  1 
ATOM   3789 N  N   . HIS B 2 7   ? 1.658   73.364  18.350  1.00 70.52 ? 7    HIS B N   1 
ATOM   3790 C  CA  . HIS B 2 7   ? 3.132   73.180  18.441  1.00 64.90 ? 7    HIS B CA  1 
ATOM   3791 C  C   . HIS B 2 7   ? 3.803   73.974  17.310  1.00 58.77 ? 7    HIS B C   1 
ATOM   3792 O  O   . HIS B 2 7   ? 3.387   73.805  16.145  1.00 54.32 ? 7    HIS B O   1 
ATOM   3793 C  CB  . HIS B 2 7   ? 3.487   71.687  18.398  1.00 65.26 ? 7    HIS B CB  1 
ATOM   3794 N  N   . VAL B 2 8   ? 4.781   74.825  17.634  1.00 49.76 ? 8    VAL B N   1 
ATOM   3795 C  CA  . VAL B 2 8   ? 5.550   75.595  16.610  1.00 47.27 ? 8    VAL B CA  1 
ATOM   3796 C  C   . VAL B 2 8   ? 6.547   74.642  15.947  1.00 42.79 ? 8    VAL B C   1 
ATOM   3797 O  O   . VAL B 2 8   ? 7.118   73.804  16.663  1.00 43.98 ? 8    VAL B O   1 
ATOM   3798 C  CB  . VAL B 2 8   ? 6.250   76.839  17.196  1.00 48.42 ? 8    VAL B CB  1 
ATOM   3799 C  CG1 . VAL B 2 8   ? 7.392   76.486  18.141  1.00 47.87 ? 8    VAL B CG1 1 
ATOM   3800 C  CG2 . VAL B 2 8   ? 6.737   77.766  16.092  1.00 45.55 ? 8    VAL B CG2 1 
ATOM   3801 N  N   . ASP B 2 9   ? 6.725   74.757  14.628  1.00 40.55 ? 9    ASP B N   1 
ATOM   3802 C  CA  . ASP B 2 9   ? 7.767   74.026  13.856  1.00 39.71 ? 9    ASP B CA  1 
ATOM   3803 C  C   . ASP B 2 9   ? 8.191   74.877  12.646  1.00 37.95 ? 9    ASP B C   1 
ATOM   3804 O  O   . ASP B 2 9   ? 7.749   76.039  12.538  1.00 35.31 ? 9    ASP B O   1 
ATOM   3805 C  CB  . ASP B 2 9   ? 7.281   72.622  13.481  1.00 41.85 ? 9    ASP B CB  1 
ATOM   3806 C  CG  . ASP B 2 9   ? 6.179   72.583  12.432  1.00 43.73 ? 9    ASP B CG  1 
ATOM   3807 O  OD1 . ASP B 2 9   ? 6.048   73.560  11.674  1.00 41.75 ? 9    ASP B OD1 1 
ATOM   3808 O  OD2 . ASP B 2 9   ? 5.452   71.572  12.389  1.00 48.39 ? 9    ASP B OD2 1 
ATOM   3809 N  N   . LEU B 2 10  ? 9.018   74.323  11.758  1.00 37.07 ? 10   LEU B N   1 
ATOM   3810 C  CA  . LEU B 2 10  ? 9.599   75.078  10.613  1.00 38.95 ? 10   LEU B CA  1 
ATOM   3811 C  C   . LEU B 2 10  ? 8.517   75.435  9.580   1.00 39.84 ? 10   LEU B C   1 
ATOM   3812 O  O   . LEU B 2 10  ? 8.781   76.343  8.773   1.00 43.36 ? 10   LEU B O   1 
ATOM   3813 C  CB  . LEU B 2 10  ? 10.727  74.257  9.981   1.00 36.81 ? 10   LEU B CB  1 
ATOM   3814 C  CG  . LEU B 2 10  ? 11.921  73.970  10.891  1.00 35.89 ? 10   LEU B CG  1 
ATOM   3815 C  CD1 . LEU B 2 10  ? 13.043  73.310  10.109  1.00 34.51 ? 10   LEU B CD1 1 
ATOM   3816 C  CD2 . LEU B 2 10  ? 12.422  75.238  11.567  1.00 34.93 ? 10   LEU B CD2 1 
ATOM   3817 N  N   . THR B 2 11  ? 7.340   74.797  9.622   1.00 40.11 ? 11   THR B N   1 
ATOM   3818 C  CA  A THR B 2 11  ? 6.247   75.067  8.639   0.55 40.62 ? 11   THR B CA  1 
ATOM   3819 C  CA  B THR B 2 11  ? 6.208   75.033  8.679   0.45 41.00 ? 11   THR B CA  1 
ATOM   3820 C  C   . THR B 2 11  ? 5.407   76.276  9.088   1.00 41.41 ? 11   THR B C   1 
ATOM   3821 O  O   . THR B 2 11  ? 4.818   76.914  8.200   1.00 41.26 ? 11   THR B O   1 
ATOM   3822 C  CB  A THR B 2 11  ? 5.392   73.819  8.389   0.55 40.31 ? 11   THR B CB  1 
ATOM   3823 C  CB  B THR B 2 11  ? 5.248   73.835  8.640   0.45 41.04 ? 11   THR B CB  1 
ATOM   3824 O  OG1 A THR B 2 11  ? 4.725   73.457  9.597   0.55 38.40 ? 11   THR B OG1 1 
ATOM   3825 O  OG1 B THR B 2 11  ? 6.004   72.626  8.555   0.45 39.84 ? 11   THR B OG1 1 
ATOM   3826 C  CG2 A THR B 2 11  ? 6.212   72.653  7.884   0.55 39.83 ? 11   THR B CG2 1 
ATOM   3827 C  CG2 B THR B 2 11  ? 4.264   73.909  7.492   0.45 41.06 ? 11   THR B CG2 1 
ATOM   3828 N  N   . ASN B 2 12  ? 5.362   76.593  10.390  1.00 42.03 ? 12   ASN B N   1 
ATOM   3829 C  CA  . ASN B 2 12  ? 4.476   77.677  10.906  1.00 43.45 ? 12   ASN B CA  1 
ATOM   3830 C  C   . ASN B 2 12  ? 5.228   78.716  11.760  1.00 41.61 ? 12   ASN B C   1 
ATOM   3831 O  O   . ASN B 2 12  ? 4.560   79.675  12.212  1.00 39.20 ? 12   ASN B O   1 
ATOM   3832 C  CB  . ASN B 2 12  ? 3.285   77.095  11.675  1.00 44.39 ? 12   ASN B CB  1 
ATOM   3833 C  CG  . ASN B 2 12  ? 3.695   76.252  12.864  1.00 47.20 ? 12   ASN B CG  1 
ATOM   3834 O  OD1 . ASN B 2 12  ? 4.754   76.458  13.445  1.00 45.67 ? 12   ASN B OD1 1 
ATOM   3835 N  ND2 . ASN B 2 12  ? 2.857   75.303  13.245  1.00 50.00 ? 12   ASN B ND2 1 
ATOM   3836 N  N   . CYS B 2 13  ? 6.544   78.584  11.972  1.00 39.41 ? 13   CYS B N   1 
ATOM   3837 C  CA  . CYS B 2 13  ? 7.300   79.516  12.867  1.00 38.72 ? 13   CYS B CA  1 
ATOM   3838 C  C   . CYS B 2 13  ? 7.267   80.946  12.296  1.00 36.61 ? 13   CYS B C   1 
ATOM   3839 O  O   . CYS B 2 13  ? 7.429   81.908  13.084  1.00 34.26 ? 13   CYS B O   1 
ATOM   3840 C  CB  . CYS B 2 13  ? 8.728   79.051  13.154  1.00 39.18 ? 13   CYS B CB  1 
ATOM   3841 S  SG  . CYS B 2 13  ? 9.824   78.957  11.703  1.00 42.26 ? 13   CYS B SG  1 
ATOM   3842 N  N   . ASP B 2 14  ? 6.997   81.098  10.996  1.00 36.16 ? 14   ASP B N   1 
ATOM   3843 C  CA  . ASP B 2 14  ? 6.824   82.423  10.334  1.00 38.26 ? 14   ASP B CA  1 
ATOM   3844 C  C   . ASP B 2 14  ? 5.601   83.165  10.894  1.00 36.50 ? 14   ASP B C   1 
ATOM   3845 O  O   . ASP B 2 14  ? 5.531   84.388  10.667  1.00 38.88 ? 14   ASP B O   1 
ATOM   3846 C  CB  . ASP B 2 14  ? 6.724   82.279  8.813   1.00 39.91 ? 14   ASP B CB  1 
ATOM   3847 C  CG  . ASP B 2 14  ? 5.522   81.478  8.333   1.00 41.49 ? 14   ASP B CG  1 
ATOM   3848 O  OD1 . ASP B 2 14  ? 4.876   80.801  9.174   1.00 41.78 ? 14   ASP B OD1 1 
ATOM   3849 O  OD2 . ASP B 2 14  ? 5.250   81.530  7.118   1.00 44.82 ? 14   ASP B OD2 1 
ATOM   3850 N  N   . ARG B 2 15  ? 4.680   82.471  11.578  1.00 37.77 ? 15   ARG B N   1 
ATOM   3851 C  CA  . ARG B 2 15  ? 3.444   83.064  12.177  1.00 40.80 ? 15   ARG B CA  1 
ATOM   3852 C  C   . ARG B 2 15  ? 3.311   82.726  13.673  1.00 40.25 ? 15   ARG B C   1 
ATOM   3853 O  O   . ARG B 2 15  ? 2.208   82.923  14.221  1.00 38.89 ? 15   ARG B O   1 
ATOM   3854 C  CB  . ARG B 2 15  ? 2.200   82.538  11.454  1.00 44.10 ? 15   ARG B CB  1 
ATOM   3855 C  CG  . ARG B 2 15  ? 2.007   83.070  10.041  1.00 49.24 ? 15   ARG B CG  1 
ATOM   3856 C  CD  . ARG B 2 15  ? 0.945   82.271  9.296   1.00 52.54 ? 15   ARG B CD  1 
ATOM   3857 N  NE  . ARG B 2 15  ? 1.385   80.895  9.089   1.00 56.08 ? 15   ARG B NE  1 
ATOM   3858 C  CZ  . ARG B 2 15  ? 2.076   80.454  8.037   1.00 59.10 ? 15   ARG B CZ  1 
ATOM   3859 N  NH1 . ARG B 2 15  ? 2.400   81.273  7.046   1.00 59.96 ? 15   ARG B NH1 1 
ATOM   3860 N  NH2 . ARG B 2 15  ? 2.439   79.182  7.980   1.00 56.31 ? 15   ARG B NH2 1 
ATOM   3861 N  N   . GLU B 2 16  ? 4.368   82.243  14.331  1.00 36.75 ? 16   GLU B N   1 
ATOM   3862 C  CA  . GLU B 2 16  ? 4.308   81.902  15.779  1.00 36.47 ? 16   GLU B CA  1 
ATOM   3863 C  C   . GLU B 2 16  ? 3.864   83.137  16.567  1.00 36.53 ? 16   GLU B C   1 
ATOM   3864 O  O   . GLU B 2 16  ? 4.439   84.213  16.410  1.00 33.63 ? 16   GLU B O   1 
ATOM   3865 C  CB  . GLU B 2 16  ? 5.662   81.380  16.259  1.00 36.24 ? 16   GLU B CB  1 
ATOM   3866 C  CG  . GLU B 2 16  ? 5.625   80.727  17.629  1.00 35.00 ? 16   GLU B CG  1 
ATOM   3867 C  CD  . GLU B 2 16  ? 7.008   80.562  18.241  1.00 34.88 ? 16   GLU B CD  1 
ATOM   3868 O  OE1 . GLU B 2 16  ? 8.004   80.818  17.518  1.00 33.62 ? 16   GLU B OE1 1 
ATOM   3869 O  OE2 . GLU B 2 16  ? 7.089   80.183  19.427  1.00 34.89 ? 16   GLU B OE2 1 
ATOM   3870 N  N   . PRO B 2 17  ? 2.813   83.024  17.418  1.00 38.81 ? 17   PRO B N   1 
ATOM   3871 C  CA  . PRO B 2 17  ? 2.349   84.135  18.249  1.00 37.29 ? 17   PRO B CA  1 
ATOM   3872 C  C   . PRO B 2 17  ? 3.234   84.310  19.496  1.00 36.82 ? 17   PRO B C   1 
ATOM   3873 O  O   . PRO B 2 17  ? 2.826   83.986  20.607  1.00 32.30 ? 17   PRO B O   1 
ATOM   3874 C  CB  . PRO B 2 17  ? 0.915   83.706  18.587  1.00 40.07 ? 17   PRO B CB  1 
ATOM   3875 C  CG  . PRO B 2 17  ? 1.016   82.203  18.704  1.00 40.62 ? 17   PRO B CG  1 
ATOM   3876 C  CD  . PRO B 2 17  ? 2.016   81.802  17.634  1.00 40.68 ? 17   PRO B CD  1 
ATOM   3877 N  N   . ILE B 2 18  ? 4.421   84.876  19.275  1.00 37.06 ? 18   ILE B N   1 
ATOM   3878 C  CA  . ILE B 2 18  ? 5.528   84.999  20.273  1.00 36.95 ? 18   ILE B CA  1 
ATOM   3879 C  C   . ILE B 2 18  ? 5.214   86.105  21.290  1.00 37.13 ? 18   ILE B C   1 
ATOM   3880 O  O   . ILE B 2 18  ? 5.932   86.176  22.299  1.00 37.25 ? 18   ILE B O   1 
ATOM   3881 C  CB  . ILE B 2 18  ? 6.871   85.229  19.549  1.00 36.40 ? 18   ILE B CB  1 
ATOM   3882 C  CG1 . ILE B 2 18  ? 6.863   86.510  18.710  1.00 34.88 ? 18   ILE B CG1 1 
ATOM   3883 C  CG2 . ILE B 2 18  ? 7.229   84.002  18.720  1.00 36.09 ? 18   ILE B CG2 1 
ATOM   3884 C  CD1 . ILE B 2 18  ? 8.216   86.914  18.176  1.00 36.56 ? 18   ILE B CD1 1 
ATOM   3885 N  N   . HIS B 2 19  ? 4.186   86.925  21.041  1.00 37.86 ? 19   HIS B N   1 
ATOM   3886 C  CA  . HIS B 2 19  ? 3.715   88.001  21.959  1.00 38.19 ? 19   HIS B CA  1 
ATOM   3887 C  C   . HIS B 2 19  ? 2.866   87.428  23.109  1.00 37.31 ? 19   HIS B C   1 
ATOM   3888 O  O   . HIS B 2 19  ? 2.736   88.126  24.133  1.00 37.16 ? 19   HIS B O   1 
ATOM   3889 C  CB  . HIS B 2 19  ? 2.954   89.086  21.187  1.00 40.46 ? 19   HIS B CB  1 
ATOM   3890 C  CG  . HIS B 2 19  ? 1.711   88.591  20.525  1.00 42.90 ? 19   HIS B CG  1 
ATOM   3891 N  ND1 . HIS B 2 19  ? 1.745   87.726  19.445  1.00 42.98 ? 19   HIS B ND1 1 
ATOM   3892 C  CD2 . HIS B 2 19  ? 0.407   88.835  20.776  1.00 43.54 ? 19   HIS B CD2 1 
ATOM   3893 C  CE1 . HIS B 2 19  ? 0.513   87.453  19.067  1.00 43.51 ? 19   HIS B CE1 1 
ATOM   3894 N  NE2 . HIS B 2 19  ? -0.327  88.125  19.865  1.00 42.54 ? 19   HIS B NE2 1 
ATOM   3895 N  N   . ILE B 2 20  ? 2.329   86.212  22.967  1.00 37.26 ? 20   ILE B N   1 
ATOM   3896 C  CA  . ILE B 2 20  ? 1.414   85.575  23.967  1.00 38.63 ? 20   ILE B CA  1 
ATOM   3897 C  C   . ILE B 2 20  ? 1.846   84.135  24.239  1.00 37.53 ? 20   ILE B C   1 
ATOM   3898 O  O   . ILE B 2 20  ? 1.053   83.207  24.095  1.00 39.52 ? 20   ILE B O   1 
ATOM   3899 C  CB  . ILE B 2 20  ? -0.054  85.663  23.495  1.00 39.23 ? 20   ILE B CB  1 
ATOM   3900 C  CG1 . ILE B 2 20  ? -0.217  85.234  22.034  1.00 41.18 ? 20   ILE B CG1 1 
ATOM   3901 C  CG2 . ILE B 2 20  ? -0.598  87.061  23.739  1.00 38.15 ? 20   ILE B CG2 1 
ATOM   3902 C  CD1 . ILE B 2 20  ? -1.649  84.958  21.621  1.00 44.99 ? 20   ILE B CD1 1 
ATOM   3903 N  N   . PRO B 2 21  ? 3.100   83.898  24.692  1.00 36.40 ? 21   PRO B N   1 
ATOM   3904 C  CA  . PRO B 2 21  ? 3.597   82.534  24.884  1.00 34.79 ? 21   PRO B CA  1 
ATOM   3905 C  C   . PRO B 2 21  ? 3.016   81.836  26.123  1.00 34.72 ? 21   PRO B C   1 
ATOM   3906 O  O   . PRO B 2 21  ? 3.007   80.633  26.153  1.00 34.81 ? 21   PRO B O   1 
ATOM   3907 C  CB  . PRO B 2 21  ? 5.105   82.758  25.031  1.00 34.96 ? 21   PRO B CB  1 
ATOM   3908 C  CG  . PRO B 2 21  ? 5.195   84.110  25.713  1.00 34.79 ? 21   PRO B CG  1 
ATOM   3909 C  CD  . PRO B 2 21  ? 4.097   84.922  25.056  1.00 35.44 ? 21   PRO B CD  1 
ATOM   3910 N  N   . GLY B 2 22  ? 2.544   82.603  27.107  1.00 35.05 ? 22   GLY B N   1 
ATOM   3911 C  CA  . GLY B 2 22  ? 1.939   82.061  28.338  1.00 35.61 ? 22   GLY B CA  1 
ATOM   3912 C  C   . GLY B 2 22  ? 2.990   81.779  29.394  1.00 36.93 ? 22   GLY B C   1 
ATOM   3913 O  O   . GLY B 2 22  ? 2.637   81.219  30.456  1.00 36.91 ? 22   GLY B O   1 
ATOM   3914 N  N   . TYR B 2 23  ? 4.238   82.181  29.136  1.00 36.31 ? 23   TYR B N   1 
ATOM   3915 C  CA  . TYR B 2 23  ? 5.391   81.898  30.026  1.00 35.96 ? 23   TYR B CA  1 
ATOM   3916 C  C   . TYR B 2 23  ? 6.267   83.148  30.165  1.00 34.49 ? 23   TYR B C   1 
ATOM   3917 O  O   . TYR B 2 23  ? 6.237   84.052  29.301  1.00 31.93 ? 23   TYR B O   1 
ATOM   3918 C  CB  . TYR B 2 23  ? 6.203   80.714  29.496  1.00 37.34 ? 23   TYR B CB  1 
ATOM   3919 C  CG  . TYR B 2 23  ? 5.480   79.391  29.465  1.00 40.26 ? 23   TYR B CG  1 
ATOM   3920 C  CD1 . TYR B 2 23  ? 4.684   79.039  28.387  1.00 43.07 ? 23   TYR B CD1 1 
ATOM   3921 C  CD2 . TYR B 2 23  ? 5.602   78.480  30.505  1.00 43.11 ? 23   TYR B CD2 1 
ATOM   3922 C  CE1 . TYR B 2 23  ? 4.022   77.822  28.342  1.00 44.47 ? 23   TYR B CE1 1 
ATOM   3923 C  CE2 . TYR B 2 23  ? 4.953   77.256  30.474  1.00 43.96 ? 23   TYR B CE2 1 
ATOM   3924 C  CZ  . TYR B 2 23  ? 4.155   76.929  29.391  1.00 45.38 ? 23   TYR B CZ  1 
ATOM   3925 O  OH  . TYR B 2 23  ? 3.506   75.731  29.351  1.00 48.68 ? 23   TYR B OH  1 
ATOM   3926 N  N   . ILE B 2 24  ? 7.038   83.187  31.249  1.00 33.99 ? 24   ILE B N   1 
ATOM   3927 C  CA  . ILE B 2 24  ? 8.144   84.164  31.439  1.00 33.45 ? 24   ILE B CA  1 
ATOM   3928 C  C   . ILE B 2 24  ? 9.451   83.382  31.619  1.00 33.07 ? 24   ILE B C   1 
ATOM   3929 O  O   . ILE B 2 24  ? 9.410   82.146  31.827  1.00 32.69 ? 24   ILE B O   1 
ATOM   3930 C  CB  . ILE B 2 24  ? 7.874   85.120  32.616  1.00 34.13 ? 24   ILE B CB  1 
ATOM   3931 C  CG1 . ILE B 2 24  ? 7.697   84.370  33.939  1.00 35.05 ? 24   ILE B CG1 1 
ATOM   3932 C  CG2 . ILE B 2 24  ? 6.693   86.037  32.321  1.00 34.33 ? 24   ILE B CG2 1 
ATOM   3933 C  CD1 . ILE B 2 24  ? 7.970   85.225  35.151  1.00 35.32 ? 24   ILE B CD1 1 
ATOM   3934 N  N   . GLN B 2 25  ? 10.566  84.097  31.538  1.00 30.76 ? 25   GLN B N   1 
ATOM   3935 C  CA  . GLN B 2 25  ? 11.910  83.560  31.842  1.00 33.60 ? 25   GLN B CA  1 
ATOM   3936 C  C   . GLN B 2 25  ? 12.088  83.602  33.357  1.00 33.34 ? 25   GLN B C   1 
ATOM   3937 O  O   . GLN B 2 25  ? 11.463  84.416  34.027  1.00 34.75 ? 25   GLN B O   1 
ATOM   3938 C  CB  . GLN B 2 25  ? 12.975  84.372  31.107  1.00 31.84 ? 25   GLN B CB  1 
ATOM   3939 C  CG  . GLN B 2 25  ? 12.752  84.447  29.605  1.00 30.38 ? 25   GLN B CG  1 
ATOM   3940 C  CD  . GLN B 2 25  ? 13.811  85.316  28.978  1.00 31.71 ? 25   GLN B CD  1 
ATOM   3941 O  OE1 . GLN B 2 25  ? 15.007  85.119  29.210  1.00 31.30 ? 25   GLN B OE1 1 
ATOM   3942 N  NE2 . GLN B 2 25  ? 13.381  86.296  28.195  1.00 30.63 ? 25   GLN B NE2 1 
ATOM   3943 N  N   . PRO B 2 26  ? 12.938  82.727  33.933  1.00 34.78 ? 26   PRO B N   1 
ATOM   3944 C  CA  . PRO B 2 26  ? 13.024  82.589  35.387  1.00 34.18 ? 26   PRO B CA  1 
ATOM   3945 C  C   . PRO B 2 26  ? 13.875  83.614  36.156  1.00 34.10 ? 26   PRO B C   1 
ATOM   3946 O  O   . PRO B 2 26  ? 13.980  83.451  37.355  1.00 36.64 ? 26   PRO B O   1 
ATOM   3947 C  CB  . PRO B 2 26  ? 13.620  81.177  35.545  1.00 35.19 ? 26   PRO B CB  1 
ATOM   3948 C  CG  . PRO B 2 26  ? 14.465  80.966  34.307  1.00 35.76 ? 26   PRO B CG  1 
ATOM   3949 C  CD  . PRO B 2 26  ? 13.795  81.771  33.209  1.00 35.57 ? 26   PRO B CD  1 
ATOM   3950 N  N   . HIS B 2 27  ? 14.423  84.648  35.503  1.00 32.65 ? 27   HIS B N   1 
ATOM   3951 C  CA  . HIS B 2 27  ? 15.325  85.639  36.160  1.00 31.43 ? 27   HIS B CA  1 
ATOM   3952 C  C   . HIS B 2 27  ? 14.502  86.760  36.820  1.00 31.77 ? 27   HIS B C   1 
ATOM   3953 O  O   . HIS B 2 27  ? 15.102  87.629  37.494  1.00 32.08 ? 27   HIS B O   1 
ATOM   3954 C  CB  . HIS B 2 27  ? 16.406  86.134  35.183  1.00 31.36 ? 27   HIS B CB  1 
ATOM   3955 C  CG  . HIS B 2 27  ? 15.882  86.925  34.038  1.00 29.43 ? 27   HIS B CG  1 
ATOM   3956 N  ND1 . HIS B 2 27  ? 15.422  86.327  32.884  1.00 28.57 ? 27   HIS B ND1 1 
ATOM   3957 C  CD2 . HIS B 2 27  ? 15.736  88.255  33.868  1.00 29.39 ? 27   HIS B CD2 1 
ATOM   3958 C  CE1 . HIS B 2 27  ? 15.013  87.257  32.047  1.00 29.24 ? 27   HIS B CE1 1 
ATOM   3959 N  NE2 . HIS B 2 27  ? 15.185  88.448  32.630  1.00 29.91 ? 27   HIS B NE2 1 
ATOM   3960 N  N   . GLY B 2 28  ? 13.175  86.728  36.672  1.00 30.63 ? 28   GLY B N   1 
ATOM   3961 C  CA  . GLY B 2 28  ? 12.250  87.577  37.448  1.00 30.45 ? 28   GLY B CA  1 
ATOM   3962 C  C   . GLY B 2 28  ? 10.893  86.923  37.629  1.00 29.28 ? 28   GLY B C   1 
ATOM   3963 O  O   . GLY B 2 28  ? 10.716  85.776  37.182  1.00 29.33 ? 28   GLY B O   1 
ATOM   3964 N  N   . CYS B 2 29  ? 9.954   87.632  38.257  1.00 31.34 ? 29   CYS B N   1 
ATOM   3965 C  CA  . CYS B 2 29  ? 8.533   87.197  38.350  1.00 32.15 ? 29   CYS B CA  1 
ATOM   3966 C  C   . CYS B 2 29  ? 7.640   88.339  37.872  1.00 32.04 ? 29   CYS B C   1 
ATOM   3967 O  O   . CYS B 2 29  ? 8.115   89.494  37.823  1.00 33.14 ? 29   CYS B O   1 
ATOM   3968 C  CB  . CYS B 2 29  ? 8.156   86.732  39.754  1.00 33.46 ? 29   CYS B CB  1 
ATOM   3969 S  SG  . CYS B 2 29  ? 8.187   88.050  40.991  1.00 34.80 ? 29   CYS B SG  1 
ATOM   3970 N  N   . LEU B 2 30  ? 6.408   88.002  37.504  1.00 32.46 ? 30   LEU B N   1 
ATOM   3971 C  CA  . LEU B 2 30  ? 5.453   88.923  36.846  1.00 34.67 ? 30   LEU B CA  1 
ATOM   3972 C  C   . LEU B 2 30  ? 4.091   88.823  37.543  1.00 36.29 ? 30   LEU B C   1 
ATOM   3973 O  O   . LEU B 2 30  ? 3.575   87.689  37.690  1.00 35.35 ? 30   LEU B O   1 
ATOM   3974 C  CB  . LEU B 2 30  ? 5.358   88.538  35.369  1.00 34.09 ? 30   LEU B CB  1 
ATOM   3975 C  CG  . LEU B 2 30  ? 4.434   89.406  34.517  1.00 34.24 ? 30   LEU B CG  1 
ATOM   3976 C  CD1 . LEU B 2 30  ? 4.870   89.386  33.058  1.00 32.99 ? 30   LEU B CD1 1 
ATOM   3977 C  CD2 . LEU B 2 30  ? 2.985   88.950  34.646  1.00 35.95 ? 30   LEU B CD2 1 
ATOM   3978 N  N   . ILE B 2 31  ? 3.543   89.972  37.942  1.00 35.51 ? 31   ILE B N   1 
ATOM   3979 C  CA  . ILE B 2 31  ? 2.141   90.108  38.427  1.00 37.99 ? 31   ILE B CA  1 
ATOM   3980 C  C   . ILE B 2 31  ? 1.392   90.981  37.415  1.00 36.94 ? 31   ILE B C   1 
ATOM   3981 O  O   . ILE B 2 31  ? 1.905   92.061  37.066  1.00 35.27 ? 31   ILE B O   1 
ATOM   3982 C  CB  . ILE B 2 31  ? 2.097   90.661  39.869  1.00 38.09 ? 31   ILE B CB  1 
ATOM   3983 C  CG1 . ILE B 2 31  ? 2.775   89.699  40.850  1.00 37.45 ? 31   ILE B CG1 1 
ATOM   3984 C  CG2 . ILE B 2 31  ? 0.666   90.969  40.284  1.00 37.88 ? 31   ILE B CG2 1 
ATOM   3985 C  CD1 . ILE B 2 31  ? 2.967   90.252  42.238  1.00 37.07 ? 31   ILE B CD1 1 
ATOM   3986 N  N   . ALA B 2 32  ? 0.262   90.473  36.917  1.00 37.47 ? 32   ALA B N   1 
ATOM   3987 C  CA  . ALA B 2 32  ? -0.672  91.183  36.013  1.00 38.60 ? 32   ALA B CA  1 
ATOM   3988 C  C   . ALA B 2 32  ? -1.882  91.636  36.835  1.00 37.98 ? 32   ALA B C   1 
ATOM   3989 O  O   . ALA B 2 32  ? -2.493  90.784  37.508  1.00 33.28 ? 32   ALA B O   1 
ATOM   3990 C  CB  . ALA B 2 32  ? -1.078  90.292  34.867  1.00 38.17 ? 32   ALA B CB  1 
ATOM   3991 N  N   . CYS B 2 33  ? -2.163  92.938  36.808  1.00 38.61 ? 33   CYS B N   1 
ATOM   3992 C  CA  . CYS B 2 33  ? -3.306  93.582  37.507  1.00 40.00 ? 33   CYS B CA  1 
ATOM   3993 C  C   . CYS B 2 33  ? -4.276  94.179  36.488  1.00 41.83 ? 33   CYS B C   1 
ATOM   3994 O  O   . CYS B 2 33  ? -3.887  94.331  35.309  1.00 40.46 ? 33   CYS B O   1 
ATOM   3995 C  CB  . CYS B 2 33  ? -2.832  94.693  38.435  1.00 41.50 ? 33   CYS B CB  1 
ATOM   3996 S  SG  . CYS B 2 33  ? -1.893  94.093  39.861  1.00 44.17 ? 33   CYS B SG  1 
ATOM   3997 N  N   . ASP B 2 34  ? -5.480  94.530  36.945  1.00 43.25 ? 34   ASP B N   1 
ATOM   3998 C  CA  . ASP B 2 34  ? -6.465  95.328  36.167  1.00 46.43 ? 34   ASP B CA  1 
ATOM   3999 C  C   . ASP B 2 34  ? -5.847  96.706  35.903  1.00 48.09 ? 34   ASP B C   1 
ATOM   4000 O  O   . ASP B 2 34  ? -4.816  97.030  36.538  1.00 44.44 ? 34   ASP B O   1 
ATOM   4001 C  CB  . ASP B 2 34  ? -7.813  95.428  36.892  1.00 48.20 ? 34   ASP B CB  1 
ATOM   4002 C  CG  . ASP B 2 34  ? -7.748  96.170  38.216  1.00 48.59 ? 34   ASP B CG  1 
ATOM   4003 O  OD1 . ASP B 2 34  ? -7.514  97.401  38.199  1.00 46.36 ? 34   ASP B OD1 1 
ATOM   4004 O  OD2 . ASP B 2 34  ? -7.915  95.507  39.257  1.00 55.85 ? 34   ASP B OD2 1 
ATOM   4005 N  N   . ASN B 2 35  ? -6.487  97.503  35.042  1.00 49.57 ? 35   ASN B N   1 
ATOM   4006 C  CA  . ASN B 2 35  ? -5.938  98.783  34.520  1.00 52.82 ? 35   ASN B CA  1 
ATOM   4007 C  C   . ASN B 2 35  ? -5.752  99.800  35.657  1.00 53.23 ? 35   ASN B C   1 
ATOM   4008 O  O   . ASN B 2 35  ? -4.953  100.740 35.470  1.00 53.47 ? 35   ASN B O   1 
ATOM   4009 C  CB  . ASN B 2 35  ? -6.813  99.340  33.395  1.00 59.31 ? 35   ASN B CB  1 
ATOM   4010 C  CG  . ASN B 2 35  ? -6.062  100.299 32.497  1.00 64.49 ? 35   ASN B CG  1 
ATOM   4011 O  OD1 . ASN B 2 35  ? -5.045  99.937  31.911  1.00 70.69 ? 35   ASN B OD1 1 
ATOM   4012 N  ND2 . ASN B 2 35  ? -6.549  101.525 32.387  1.00 70.55 ? 35   ASN B ND2 1 
ATOM   4013 N  N   . ALA B 2 36  ? -6.441  99.619  36.791  1.00 53.56 ? 36   ALA B N   1 
ATOM   4014 C  CA  . ALA B 2 36  ? -6.403  100.529 37.964  1.00 55.81 ? 36   ALA B CA  1 
ATOM   4015 C  C   . ALA B 2 36  ? -5.415  100.031 39.031  1.00 54.60 ? 36   ALA B C   1 
ATOM   4016 O  O   . ALA B 2 36  ? -5.247  100.740 40.045  1.00 51.78 ? 36   ALA B O   1 
ATOM   4017 C  CB  . ALA B 2 36  ? -7.793  100.672 38.541  1.00 56.03 ? 36   ALA B CB  1 
ATOM   4018 N  N   . MET B 2 37  ? -4.781  98.872  38.820  1.00 53.91 ? 37   MET B N   1 
ATOM   4019 C  CA  . MET B 2 37  ? -3.928  98.195  39.839  1.00 55.67 ? 37   MET B CA  1 
ATOM   4020 C  C   . MET B 2 37  ? -4.710  98.071  41.154  1.00 54.59 ? 37   MET B C   1 
ATOM   4021 O  O   . MET B 2 37  ? -4.151  98.404  42.226  1.00 53.12 ? 37   MET B O   1 
ATOM   4022 C  CB  . MET B 2 37  ? -2.616  98.951  40.079  1.00 55.60 ? 37   MET B CB  1 
ATOM   4023 C  CG  . MET B 2 37  ? -1.412  98.239  39.499  1.00 57.61 ? 37   MET B CG  1 
ATOM   4024 S  SD  . MET B 2 37  ? 0.153   98.810  40.209  1.00 59.56 ? 37   MET B SD  1 
ATOM   4025 C  CE  . MET B 2 37  ? 0.229   100.466 39.531  1.00 58.23 ? 37   MET B CE  1 
ATOM   4026 N  N   . ARG B 2 38  ? -5.962  97.614  41.054  1.00 52.16 ? 38   ARG B N   1 
ATOM   4027 C  CA  . ARG B 2 38  ? -6.833  97.301  42.221  1.00 51.78 ? 38   ARG B CA  1 
ATOM   4028 C  C   . ARG B 2 38  ? -6.644  95.821  42.592  1.00 51.12 ? 38   ARG B C   1 
ATOM   4029 O  O   . ARG B 2 38  ? -6.400  95.544  43.786  1.00 50.83 ? 38   ARG B O   1 
ATOM   4030 C  CB  . ARG B 2 38  ? -8.292  97.648  41.902  1.00 53.08 ? 38   ARG B CB  1 
ATOM   4031 N  N   . MET B 2 39  ? -6.722  94.917  41.606  1.00 49.11 ? 39   MET B N   1 
ATOM   4032 C  CA  . MET B 2 39  ? -6.785  93.443  41.820  1.00 49.39 ? 39   MET B CA  1 
ATOM   4033 C  C   . MET B 2 39  ? -5.684  92.730  41.023  1.00 46.41 ? 39   MET B C   1 
ATOM   4034 O  O   . MET B 2 39  ? -5.438  93.119  39.862  1.00 41.82 ? 39   MET B O   1 
ATOM   4035 C  CB  . MET B 2 39  ? -8.138  92.881  41.373  1.00 54.90 ? 39   MET B CB  1 
ATOM   4036 C  CG  . MET B 2 39  ? -8.553  91.628  42.132  1.00 61.19 ? 39   MET B CG  1 
ATOM   4037 S  SD  . MET B 2 39  ? -9.822  91.904  43.411  1.00 70.57 ? 39   MET B SD  1 
ATOM   4038 C  CE  . MET B 2 39  ? -9.535  93.612  43.878  1.00 65.96 ? 39   MET B CE  1 
ATOM   4039 N  N   . VAL B 2 40  ? -5.091  91.693  41.622  1.00 42.92 ? 40   VAL B N   1 
ATOM   4040 C  CA  . VAL B 2 40  ? -4.185  90.719  40.943  1.00 42.57 ? 40   VAL B CA  1 
ATOM   4041 C  C   . VAL B 2 40  ? -5.055  89.748  40.134  1.00 42.28 ? 40   VAL B C   1 
ATOM   4042 O  O   . VAL B 2 40  ? -5.899  89.062  40.752  1.00 43.12 ? 40   VAL B O   1 
ATOM   4043 C  CB  . VAL B 2 40  ? -3.304  89.962  41.956  1.00 41.17 ? 40   VAL B CB  1 
ATOM   4044 C  CG1 . VAL B 2 40  ? -2.411  88.941  41.268  1.00 40.47 ? 40   VAL B CG1 1 
ATOM   4045 C  CG2 . VAL B 2 40  ? -2.481  90.906  42.822  1.00 40.73 ? 40   VAL B CG2 1 
ATOM   4046 N  N   . LEU B 2 41  ? -4.854  89.706  38.812  1.00 41.81 ? 41   LEU B N   1 
ATOM   4047 C  CA  . LEU B 2 41  ? -5.590  88.837  37.851  1.00 39.59 ? 41   LEU B CA  1 
ATOM   4048 C  C   . LEU B 2 41  ? -4.728  87.623  37.506  1.00 39.00 ? 41   LEU B C   1 
ATOM   4049 O  O   . LEU B 2 41  ? -5.267  86.490  37.436  1.00 36.79 ? 41   LEU B O   1 
ATOM   4050 C  CB  . LEU B 2 41  ? -5.910  89.644  36.588  1.00 40.76 ? 41   LEU B CB  1 
ATOM   4051 C  CG  . LEU B 2 41  ? -6.674  90.947  36.806  1.00 42.66 ? 41   LEU B CG  1 
ATOM   4052 C  CD1 . LEU B 2 41  ? -6.891  91.665  35.485  1.00 43.08 ? 41   LEU B CD1 1 
ATOM   4053 C  CD2 . LEU B 2 41  ? -8.010  90.691  37.495  1.00 43.39 ? 41   LEU B CD2 1 
ATOM   4054 N  N   . ARG B 2 42  ? -3.437  87.852  37.256  1.00 39.52 ? 42   ARG B N   1 
ATOM   4055 C  CA  . ARG B 2 42  ? -2.493  86.747  36.925  1.00 40.48 ? 42   ARG B CA  1 
ATOM   4056 C  C   . ARG B 2 42  ? -1.162  86.956  37.641  1.00 38.63 ? 42   ARG B C   1 
ATOM   4057 O  O   . ARG B 2 42  ? -0.841  88.101  38.003  1.00 37.35 ? 42   ARG B O   1 
ATOM   4058 C  CB  . ARG B 2 42  ? -2.232  86.655  35.420  1.00 40.25 ? 42   ARG B CB  1 
ATOM   4059 C  CG  . ARG B 2 42  ? -3.427  87.007  34.550  1.00 40.55 ? 42   ARG B CG  1 
ATOM   4060 C  CD  . ARG B 2 42  ? -3.243  86.379  33.189  1.00 42.57 ? 42   ARG B CD  1 
ATOM   4061 N  NE  . ARG B 2 42  ? -4.102  86.975  32.178  1.00 44.01 ? 42   ARG B NE  1 
ATOM   4062 C  CZ  . ARG B 2 42  ? -4.568  86.343  31.107  1.00 42.40 ? 42   ARG B CZ  1 
ATOM   4063 N  NH1 . ARG B 2 42  ? -5.333  86.995  30.250  1.00 43.95 ? 42   ARG B NH1 1 
ATOM   4064 N  NH2 . ARG B 2 42  ? -4.284  85.068  30.896  1.00 41.12 ? 42   ARG B NH2 1 
ATOM   4065 N  N   . HIS B 2 43  ? -0.399  85.875  37.774  1.00 38.82 ? 43   HIS B N   1 
ATOM   4066 C  CA  . HIS B 2 43  ? 0.958   85.889  38.372  1.00 39.47 ? 43   HIS B CA  1 
ATOM   4067 C  C   . HIS B 2 43  ? 1.781   84.751  37.768  1.00 39.04 ? 43   HIS B C   1 
ATOM   4068 O  O   . HIS B 2 43  ? 1.186   83.705  37.420  1.00 39.61 ? 43   HIS B O   1 
ATOM   4069 C  CB  . HIS B 2 43  ? 0.844   85.807  39.898  1.00 40.07 ? 43   HIS B CB  1 
ATOM   4070 C  CG  . HIS B 2 43  ? 0.338   84.494  40.387  1.00 41.07 ? 43   HIS B CG  1 
ATOM   4071 N  ND1 . HIS B 2 43  ? -0.985  84.130  40.278  1.00 41.83 ? 43   HIS B ND1 1 
ATOM   4072 C  CD2 . HIS B 2 43  ? 0.974   83.456  40.973  1.00 41.87 ? 43   HIS B CD2 1 
ATOM   4073 C  CE1 . HIS B 2 43  ? -1.144  82.923  40.782  1.00 44.39 ? 43   HIS B CE1 1 
ATOM   4074 N  NE2 . HIS B 2 43  ? 0.044   82.488  41.216  1.00 43.00 ? 43   HIS B NE2 1 
ATOM   4075 N  N   . SER B 2 44  ? 3.094   84.945  37.640  1.00 36.05 ? 44   SER B N   1 
ATOM   4076 C  CA  . SER B 2 44  ? 4.033   83.829  37.349  1.00 37.55 ? 44   SER B CA  1 
ATOM   4077 C  C   . SER B 2 44  ? 4.127   82.906  38.578  1.00 39.01 ? 44   SER B C   1 
ATOM   4078 O  O   . SER B 2 44  ? 4.053   83.409  39.724  1.00 39.06 ? 44   SER B O   1 
ATOM   4079 C  CB  . SER B 2 44  ? 5.383   84.331  36.899  1.00 35.74 ? 44   SER B CB  1 
ATOM   4080 O  OG  . SER B 2 44  ? 5.931   85.248  37.832  1.00 33.72 ? 44   SER B OG  1 
ATOM   4081 N  N   . GLU B 2 45  ? 4.281   81.604  38.330  1.00 41.22 ? 45   GLU B N   1 
ATOM   4082 C  CA  . GLU B 2 45  ? 4.352   80.527  39.357  1.00 43.94 ? 45   GLU B CA  1 
ATOM   4083 C  C   . GLU B 2 45  ? 5.420   80.866  40.410  1.00 42.04 ? 45   GLU B C   1 
ATOM   4084 O  O   . GLU B 2 45  ? 5.214   80.514  41.596  1.00 41.30 ? 45   GLU B O   1 
ATOM   4085 C  CB  . GLU B 2 45  ? 4.643   79.186  38.673  1.00 46.94 ? 45   GLU B CB  1 
ATOM   4086 C  CG  . GLU B 2 45  ? 4.030   77.986  39.373  1.00 51.12 ? 45   GLU B CG  1 
ATOM   4087 C  CD  . GLU B 2 45  ? 3.834   76.779  38.466  1.00 57.29 ? 45   GLU B CD  1 
ATOM   4088 O  OE1 . GLU B 2 45  ? 4.850   76.152  38.086  1.00 57.01 ? 45   GLU B OE1 1 
ATOM   4089 O  OE2 . GLU B 2 45  ? 2.665   76.480  38.117  1.00 62.33 ? 45   GLU B OE2 1 
ATOM   4090 N  N   . ASN B 2 46  ? 6.504   81.535  40.004  1.00 37.61 ? 46   ASN B N   1 
ATOM   4091 C  CA  . ASN B 2 46  ? 7.697   81.802  40.854  1.00 37.58 ? 46   ASN B CA  1 
ATOM   4092 C  C   . ASN B 2 46  ? 7.512   83.060  41.728  1.00 37.16 ? 46   ASN B C   1 
ATOM   4093 O  O   . ASN B 2 46  ? 8.463   83.389  42.485  1.00 36.43 ? 46   ASN B O   1 
ATOM   4094 C  CB  . ASN B 2 46  ? 8.969   81.906  40.009  1.00 37.21 ? 46   ASN B CB  1 
ATOM   4095 C  CG  . ASN B 2 46  ? 8.971   83.092  39.065  1.00 38.53 ? 46   ASN B CG  1 
ATOM   4096 O  OD1 . ASN B 2 46  ? 7.911   83.605  38.693  1.00 36.15 ? 46   ASN B OD1 1 
ATOM   4097 N  ND2 . ASN B 2 46  ? 10.159  83.528  38.670  1.00 36.69 ? 46   ASN B ND2 1 
ATOM   4098 N  N   . CYS B 2 47  ? 6.375   83.758  41.633  1.00 35.68 ? 47   CYS B N   1 
ATOM   4099 C  CA  . CYS B 2 47  ? 6.072   84.947  42.484  1.00 38.46 ? 47   CYS B CA  1 
ATOM   4100 C  C   . CYS B 2 47  ? 6.164   84.548  43.960  1.00 40.04 ? 47   CYS B C   1 
ATOM   4101 O  O   . CYS B 2 47  ? 6.786   85.302  44.752  1.00 38.76 ? 47   CYS B O   1 
ATOM   4102 C  CB  . CYS B 2 47  ? 4.687   85.522  42.217  1.00 38.24 ? 47   CYS B CB  1 
ATOM   4103 S  SG  . CYS B 2 47  ? 4.624   86.609  40.771  1.00 38.43 ? 47   CYS B SG  1 
ATOM   4104 N  N   . GLY B 2 48  ? 5.575   83.398  44.299  1.00 41.32 ? 48   GLY B N   1 
ATOM   4105 C  CA  . GLY B 2 48  ? 5.616   82.818  45.654  1.00 42.84 ? 48   GLY B CA  1 
ATOM   4106 C  C   . GLY B 2 48  ? 7.039   82.778  46.169  1.00 42.85 ? 48   GLY B C   1 
ATOM   4107 O  O   . GLY B 2 48  ? 7.302   83.414  47.208  1.00 43.47 ? 48   GLY B O   1 
ATOM   4108 N  N   . GLU B 2 49  ? 7.924   82.095  45.434  1.00 41.73 ? 49   GLU B N   1 
ATOM   4109 C  CA  . GLU B 2 49  ? 9.348   81.875  45.804  1.00 43.92 ? 49   GLU B CA  1 
ATOM   4110 C  C   . GLU B 2 49  ? 10.084  83.217  45.840  1.00 44.70 ? 49   GLU B C   1 
ATOM   4111 O  O   . GLU B 2 49  ? 10.772  83.481  46.842  1.00 45.33 ? 49   GLU B O   1 
ATOM   4112 C  CB  . GLU B 2 49  ? 10.036  80.921  44.822  1.00 42.94 ? 49   GLU B CB  1 
ATOM   4113 N  N   . LEU B 2 50  ? 9.943   84.033  44.790  1.00 44.97 ? 50   LEU B N   1 
ATOM   4114 C  CA  . LEU B 2 50  ? 10.806  85.225  44.570  1.00 44.55 ? 50   LEU B CA  1 
ATOM   4115 C  C   . LEU B 2 50  ? 10.449  86.335  45.564  1.00 42.49 ? 50   LEU B C   1 
ATOM   4116 O  O   . LEU B 2 50  ? 11.380  86.881  46.195  1.00 42.50 ? 50   LEU B O   1 
ATOM   4117 C  CB  . LEU B 2 50  ? 10.674  85.714  43.124  1.00 46.97 ? 50   LEU B CB  1 
ATOM   4118 C  CG  . LEU B 2 50  ? 11.788  86.647  42.648  1.00 50.43 ? 50   LEU B CG  1 
ATOM   4119 C  CD1 . LEU B 2 50  ? 13.164  86.088  42.992  1.00 52.00 ? 50   LEU B CD1 1 
ATOM   4120 C  CD2 . LEU B 2 50  ? 11.686  86.896  41.150  1.00 50.53 ? 50   LEU B CD2 1 
ATOM   4121 N  N   . LEU B 2 51  ? 9.165   86.671  45.697  1.00 39.26 ? 51   LEU B N   1 
ATOM   4122 C  CA  . LEU B 2 51  ? 8.727   87.821  46.536  1.00 42.36 ? 51   LEU B CA  1 
ATOM   4123 C  C   . LEU B 2 51  ? 8.378   87.350  47.954  1.00 41.11 ? 51   LEU B C   1 
ATOM   4124 O  O   . LEU B 2 51  ? 8.225   88.218  48.831  1.00 38.02 ? 51   LEU B O   1 
ATOM   4125 C  CB  . LEU B 2 51  ? 7.542   88.519  45.864  1.00 43.57 ? 51   LEU B CB  1 
ATOM   4126 C  CG  . LEU B 2 51  ? 7.872   89.232  44.552  1.00 46.53 ? 51   LEU B CG  1 
ATOM   4127 C  CD1 . LEU B 2 51  ? 6.600   89.693  43.855  1.00 48.05 ? 51   LEU B CD1 1 
ATOM   4128 C  CD2 . LEU B 2 51  ? 8.812   90.409  44.793  1.00 45.92 ? 51   LEU B CD2 1 
ATOM   4129 N  N   . GLY B 2 52  ? 8.287   86.036  48.179  1.00 44.22 ? 52   GLY B N   1 
ATOM   4130 C  CA  . GLY B 2 52  ? 7.959   85.463  49.501  1.00 47.06 ? 52   GLY B CA  1 
ATOM   4131 C  C   . GLY B 2 52  ? 6.520   85.767  49.867  1.00 50.43 ? 52   GLY B C   1 
ATOM   4132 O  O   . GLY B 2 52  ? 6.286   86.379  50.929  1.00 52.82 ? 52   GLY B O   1 
ATOM   4133 N  N   . LEU B 2 53  ? 5.596   85.385  48.984  1.00 53.45 ? 53   LEU B N   1 
ATOM   4134 C  CA  . LEU B 2 53  ? 4.136   85.606  49.135  1.00 55.82 ? 53   LEU B CA  1 
ATOM   4135 C  C   . LEU B 2 53  ? 3.468   84.267  49.454  1.00 60.97 ? 53   LEU B C   1 
ATOM   4136 O  O   . LEU B 2 53  ? 3.558   83.348  48.617  1.00 67.16 ? 53   LEU B O   1 
ATOM   4137 C  CB  . LEU B 2 53  ? 3.584   86.215  47.844  1.00 54.70 ? 53   LEU B CB  1 
ATOM   4138 C  CG  . LEU B 2 53  ? 4.273   87.498  47.381  1.00 52.93 ? 53   LEU B CG  1 
ATOM   4139 C  CD1 . LEU B 2 53  ? 3.853   87.852  45.966  1.00 55.02 ? 53   LEU B CD1 1 
ATOM   4140 C  CD2 . LEU B 2 53  ? 3.980   88.649  48.329  1.00 52.97 ? 53   LEU B CD2 1 
ATOM   4141 N  N   . GLU B 2 54  ? 2.845   84.171  50.631  1.00 64.31 ? 54   GLU B N   1 
ATOM   4142 C  CA  . GLU B 2 54  ? 2.121   82.964  51.108  1.00 65.89 ? 54   GLU B CA  1 
ATOM   4143 C  C   . GLU B 2 54  ? 0.740   82.924  50.439  1.00 65.96 ? 54   GLU B C   1 
ATOM   4144 O  O   . GLU B 2 54  ? -0.019  83.893  50.631  1.00 66.23 ? 54   GLU B O   1 
ATOM   4145 C  CB  . GLU B 2 54  ? 2.009   82.995  52.635  1.00 64.36 ? 54   GLU B CB  1 
ATOM   4146 N  N   . GLY B 2 55  ? 0.459   81.871  49.656  1.00 67.72 ? 55   GLY B N   1 
ATOM   4147 C  CA  . GLY B 2 55  ? -0.878  81.553  49.105  1.00 63.60 ? 55   GLY B CA  1 
ATOM   4148 C  C   . GLY B 2 55  ? -1.074  82.081  47.694  1.00 63.63 ? 55   GLY B C   1 
ATOM   4149 O  O   . GLY B 2 55  ? -0.293  82.964  47.280  1.00 64.94 ? 55   GLY B O   1 
ATOM   4150 N  N   . ASP B 2 56  ? -2.096  81.574  46.991  1.00 61.66 ? 56   ASP B N   1 
ATOM   4151 C  CA  . ASP B 2 56  ? -2.474  82.000  45.613  1.00 57.90 ? 56   ASP B CA  1 
ATOM   4152 C  C   . ASP B 2 56  ? -2.802  83.500  45.626  1.00 55.00 ? 56   ASP B C   1 
ATOM   4153 O  O   . ASP B 2 56  ? -3.464  83.964  46.580  1.00 53.12 ? 56   ASP B O   1 
ATOM   4154 C  CB  . ASP B 2 56  ? -3.638  81.174  45.058  1.00 55.07 ? 56   ASP B CB  1 
ATOM   4155 N  N   . LEU B 2 57  ? -2.339  84.224  44.605  1.00 51.36 ? 57   LEU B N   1 
ATOM   4156 C  CA  . LEU B 2 57  ? -2.342  85.711  44.552  1.00 49.22 ? 57   LEU B CA  1 
ATOM   4157 C  C   . LEU B 2 57  ? -3.573  86.212  43.790  1.00 46.06 ? 57   LEU B C   1 
ATOM   4158 O  O   . LEU B 2 57  ? -4.012  87.350  44.069  1.00 42.67 ? 57   LEU B O   1 
ATOM   4159 C  CB  . LEU B 2 57  ? -1.048  86.191  43.884  1.00 48.32 ? 57   LEU B CB  1 
ATOM   4160 C  CG  . LEU B 2 57  ? 0.245   85.606  44.456  1.00 50.16 ? 57   LEU B CG  1 
ATOM   4161 C  CD1 . LEU B 2 57  ? 1.455   86.126  43.695  1.00 49.83 ? 57   LEU B CD1 1 
ATOM   4162 C  CD2 . LEU B 2 57  ? 0.378   85.913  45.942  1.00 50.13 ? 57   LEU B CD2 1 
ATOM   4163 N  N   . ASN B 2 58  ? -4.105  85.410  42.864  1.00 41.77 ? 58   ASN B N   1 
ATOM   4164 C  CA  . ASN B 2 58  ? -5.216  85.840  41.978  1.00 44.26 ? 58   ASN B CA  1 
ATOM   4165 C  C   . ASN B 2 58  ? -6.466  86.069  42.839  1.00 44.85 ? 58   ASN B C   1 
ATOM   4166 O  O   . ASN B 2 58  ? -6.803  85.181  43.655  1.00 44.51 ? 58   ASN B O   1 
ATOM   4167 C  CB  . ASN B 2 58  ? -5.422  84.850  40.829  1.00 44.03 ? 58   ASN B CB  1 
ATOM   4168 C  CG  . ASN B 2 58  ? -4.220  84.786  39.905  1.00 43.67 ? 58   ASN B CG  1 
ATOM   4169 O  OD1 . ASN B 2 58  ? -3.364  85.673  39.912  1.00 41.09 ? 58   ASN B OD1 1 
ATOM   4170 N  ND2 . ASN B 2 58  ? -4.139  83.735  39.108  1.00 43.20 ? 58   ASN B ND2 1 
ATOM   4171 N  N   . GLY B 2 59  ? -7.099  87.232  42.688  1.00 42.81 ? 59   GLY B N   1 
ATOM   4172 C  CA  . GLY B 2 59  ? -8.304  87.613  43.450  1.00 46.82 ? 59   GLY B CA  1 
ATOM   4173 C  C   . GLY B 2 59  ? -7.992  88.595  44.567  1.00 47.99 ? 59   GLY B C   1 
ATOM   4174 O  O   . GLY B 2 59  ? -8.893  89.365  44.928  1.00 48.09 ? 59   GLY B O   1 
ATOM   4175 N  N   . ARG B 2 60  ? -6.766  88.581  45.104  1.00 49.58 ? 60   ARG B N   1 
ATOM   4176 C  CA  . ARG B 2 60  ? -6.339  89.542  46.160  1.00 48.18 ? 60   ARG B CA  1 
ATOM   4177 C  C   . ARG B 2 60  ? -6.164  90.951  45.587  1.00 45.66 ? 60   ARG B C   1 
ATOM   4178 O  O   . ARG B 2 60  ? -5.948  91.072  44.368  1.00 46.41 ? 60   ARG B O   1 
ATOM   4179 C  CB  . ARG B 2 60  ? -4.991  89.159  46.767  1.00 48.91 ? 60   ARG B CB  1 
ATOM   4180 C  CG  . ARG B 2 60  ? -4.951  87.822  47.482  1.00 50.75 ? 60   ARG B CG  1 
ATOM   4181 C  CD  . ARG B 2 60  ? -3.720  87.887  48.363  1.00 53.80 ? 60   ARG B CD  1 
ATOM   4182 N  NE  . ARG B 2 60  ? -2.943  86.671  48.481  1.00 56.90 ? 60   ARG B NE  1 
ATOM   4183 C  CZ  . ARG B 2 60  ? -1.889  86.551  49.279  1.00 56.72 ? 60   ARG B CZ  1 
ATOM   4184 N  NH1 . ARG B 2 60  ? -1.219  85.413  49.321  1.00 58.96 ? 60   ARG B NH1 1 
ATOM   4185 N  NH2 . ARG B 2 60  ? -1.514  87.565  50.041  1.00 57.52 ? 60   ARG B NH2 1 
ATOM   4186 N  N   . THR B 2 61  ? -6.186  91.970  46.453  1.00 43.32 ? 61   THR B N   1 
ATOM   4187 C  CA  . THR B 2 61  ? -5.858  93.374  46.080  1.00 42.48 ? 61   THR B CA  1 
ATOM   4188 C  C   . THR B 2 61  ? -4.335  93.482  45.911  1.00 41.31 ? 61   THR B C   1 
ATOM   4189 O  O   . THR B 2 61  ? -3.599  92.670  46.523  1.00 39.66 ? 61   THR B O   1 
ATOM   4190 C  CB  . THR B 2 61  ? -6.387  94.395  47.095  1.00 42.59 ? 61   THR B CB  1 
ATOM   4191 O  OG1 . THR B 2 61  ? -5.588  94.307  48.277  1.00 41.73 ? 61   THR B OG1 1 
ATOM   4192 C  CG2 . THR B 2 61  ? -7.851  94.199  47.432  1.00 43.65 ? 61   THR B CG2 1 
ATOM   4193 N  N   . ALA B 2 62  ? -3.878  94.425  45.089  1.00 39.87 ? 62   ALA B N   1 
ATOM   4194 C  CA  . ALA B 2 62  ? -2.439  94.709  44.871  1.00 41.12 ? 62   ALA B CA  1 
ATOM   4195 C  C   . ALA B 2 62  ? -1.839  95.221  46.186  1.00 39.06 ? 62   ALA B C   1 
ATOM   4196 O  O   . ALA B 2 62  ? -0.707  94.836  46.508  1.00 36.27 ? 62   ALA B O   1 
ATOM   4197 C  CB  . ALA B 2 62  ? -2.254  95.693  43.740  1.00 39.77 ? 62   ALA B CB  1 
ATOM   4198 N  N   . GLU B 2 63  ? -2.608  96.018  46.932  1.00 41.87 ? 63   GLU B N   1 
ATOM   4199 C  CA  . GLU B 2 63  ? -2.196  96.599  48.239  1.00 44.13 ? 63   GLU B CA  1 
ATOM   4200 C  C   . GLU B 2 63  ? -2.013  95.478  49.270  1.00 41.71 ? 63   GLU B C   1 
ATOM   4201 O  O   . GLU B 2 63  ? -1.052  95.552  50.050  1.00 39.60 ? 63   GLU B O   1 
ATOM   4202 C  CB  . GLU B 2 63  ? -3.203  97.665  48.660  1.00 47.76 ? 63   GLU B CB  1 
ATOM   4203 C  CG  . GLU B 2 63  ? -3.201  98.850  47.714  1.00 51.12 ? 63   GLU B CG  1 
ATOM   4204 C  CD  . GLU B 2 63  ? -4.053  100.025 48.151  1.00 56.77 ? 63   GLU B CD  1 
ATOM   4205 O  OE1 . GLU B 2 63  ? -4.987  99.813  48.956  1.00 59.76 ? 63   GLU B OE1 1 
ATOM   4206 O  OE2 . GLU B 2 63  ? -3.768  101.152 47.694  1.00 62.58 ? 63   GLU B OE2 1 
ATOM   4207 N  N   . ASP B 2 64  ? -2.868  94.457  49.246  1.00 41.84 ? 64   ASP B N   1 
ATOM   4208 C  CA  . ASP B 2 64  ? -2.737  93.255  50.114  1.00 43.81 ? 64   ASP B CA  1 
ATOM   4209 C  C   . ASP B 2 64  ? -1.471  92.471  49.737  1.00 42.18 ? 64   ASP B C   1 
ATOM   4210 O  O   . ASP B 2 64  ? -0.752  92.033  50.651  1.00 40.73 ? 64   ASP B O   1 
ATOM   4211 C  CB  . ASP B 2 64  ? -3.973  92.359  50.015  1.00 45.92 ? 64   ASP B CB  1 
ATOM   4212 C  CG  . ASP B 2 64  ? -3.812  91.027  50.724  1.00 48.24 ? 64   ASP B CG  1 
ATOM   4213 O  OD1 . ASP B 2 64  ? -3.252  91.015  51.844  1.00 48.83 ? 64   ASP B OD1 1 
ATOM   4214 O  OD2 . ASP B 2 64  ? -4.247  90.016  50.152  1.00 50.89 ? 64   ASP B OD2 1 
ATOM   4215 N  N   . VAL B 2 65  ? -1.212  92.280  48.442  1.00 41.12 ? 65   VAL B N   1 
ATOM   4216 C  CA  . VAL B 2 65  ? -0.038  91.490  47.960  1.00 41.02 ? 65   VAL B CA  1 
ATOM   4217 C  C   . VAL B 2 65  ? 1.255   92.302  48.146  1.00 39.36 ? 65   VAL B C   1 
ATOM   4218 O  O   . VAL B 2 65  ? 2.236   91.714  48.629  1.00 40.91 ? 65   VAL B O   1 
ATOM   4219 C  CB  . VAL B 2 65  ? -0.236  91.021  46.506  1.00 42.27 ? 65   VAL B CB  1 
ATOM   4220 C  CG1 . VAL B 2 65  ? 1.058   90.538  45.868  1.00 44.88 ? 65   VAL B CG1 1 
ATOM   4221 C  CG2 . VAL B 2 65  ? -1.294  89.934  46.432  1.00 42.59 ? 65   VAL B CG2 1 
ATOM   4222 N  N   . LEU B 2 66  ? 1.259   93.590  47.786  1.00 37.18 ? 66   LEU B N   1 
ATOM   4223 C  CA  . LEU B 2 66  ? 2.500   94.403  47.643  1.00 37.37 ? 66   LEU B CA  1 
ATOM   4224 C  C   . LEU B 2 66  ? 2.663   95.407  48.791  1.00 37.37 ? 66   LEU B C   1 
ATOM   4225 O  O   . LEU B 2 66  ? 3.775   95.961  48.912  1.00 40.17 ? 66   LEU B O   1 
ATOM   4226 C  CB  . LEU B 2 66  ? 2.459   95.135  46.298  1.00 38.31 ? 66   LEU B CB  1 
ATOM   4227 C  CG  . LEU B 2 66  ? 2.502   94.256  45.048  1.00 38.11 ? 66   LEU B CG  1 
ATOM   4228 C  CD1 . LEU B 2 66  ? 2.512   95.119  43.795  1.00 38.89 ? 66   LEU B CD1 1 
ATOM   4229 C  CD2 . LEU B 2 66  ? 3.708   93.333  45.053  1.00 38.12 ? 66   LEU B CD2 1 
ATOM   4230 N  N   . GLY B 2 67  ? 1.617   95.639  49.594  1.00 35.36 ? 67   GLY B N   1 
ATOM   4231 C  CA  . GLY B 2 67  ? 1.586   96.701  50.618  1.00 35.98 ? 67   GLY B CA  1 
ATOM   4232 C  C   . GLY B 2 67  ? 1.102   98.014  50.025  1.00 38.10 ? 67   GLY B C   1 
ATOM   4233 O  O   . GLY B 2 67  ? 1.366   98.257  48.818  1.00 36.93 ? 67   GLY B O   1 
ATOM   4234 N  N   . LYS B 2 68  ? 0.433   98.841  50.837  1.00 37.42 ? 68   LYS B N   1 
ATOM   4235 C  CA  . LYS B 2 68  ? -0.190  100.125 50.408  1.00 38.37 ? 68   LYS B CA  1 
ATOM   4236 C  C   . LYS B 2 68  ? 0.880   101.048 49.818  1.00 37.55 ? 68   LYS B C   1 
ATOM   4237 O  O   . LYS B 2 68  ? 0.624   101.631 48.749  1.00 34.79 ? 68   LYS B O   1 
ATOM   4238 C  CB  . LYS B 2 68  ? -0.893  100.818 51.582  1.00 38.91 ? 68   LYS B CB  1 
ATOM   4239 N  N   . LYS B 2 69  ? 2.018   101.180 50.505  1.00 38.99 ? 69   LYS B N   1 
ATOM   4240 C  CA  . LYS B 2 69  ? 3.125   102.106 50.133  1.00 42.32 ? 69   LYS B CA  1 
ATOM   4241 C  C   . LYS B 2 69  ? 3.631   101.778 48.720  1.00 41.21 ? 69   LYS B C   1 
ATOM   4242 O  O   . LYS B 2 69  ? 3.751   102.718 47.906  1.00 39.66 ? 69   LYS B O   1 
ATOM   4243 C  CB  . LYS B 2 69  ? 4.255   102.033 51.166  1.00 46.97 ? 69   LYS B CB  1 
ATOM   4244 C  CG  . LYS B 2 69  ? 5.495   102.865 50.857  1.00 49.84 ? 69   LYS B CG  1 
ATOM   4245 C  CD  . LYS B 2 69  ? 5.201   104.289 50.416  1.00 53.89 ? 69   LYS B CD  1 
ATOM   4246 C  CE  . LYS B 2 69  ? 6.455   105.120 50.228  1.00 55.71 ? 69   LYS B CE  1 
ATOM   4247 N  NZ  . LYS B 2 69  ? 6.165   106.398 49.534  1.00 57.82 ? 69   LYS B NZ  1 
ATOM   4248 N  N   . LEU B 2 70  ? 3.917   100.506 48.423  1.00 37.64 ? 70   LEU B N   1 
ATOM   4249 C  CA  . LEU B 2 70  ? 4.526   100.126 47.117  1.00 39.01 ? 70   LEU B CA  1 
ATOM   4250 C  C   . LEU B 2 70  ? 3.515   100.378 45.990  1.00 39.92 ? 70   LEU B C   1 
ATOM   4251 O  O   . LEU B 2 70  ? 3.921   100.971 44.972  1.00 41.42 ? 70   LEU B O   1 
ATOM   4252 C  CB  . LEU B 2 70  ? 5.015   98.675  47.142  1.00 37.36 ? 70   LEU B CB  1 
ATOM   4253 C  CG  . LEU B 2 70  ? 5.703   98.199  45.863  1.00 37.29 ? 70   LEU B CG  1 
ATOM   4254 C  CD1 . LEU B 2 70  ? 6.815   99.148  45.438  1.00 38.76 ? 70   LEU B CD1 1 
ATOM   4255 C  CD2 . LEU B 2 70  ? 6.249   96.790  46.030  1.00 38.12 ? 70   LEU B CD2 1 
ATOM   4256 N  N   . VAL B 2 71  ? 2.246   99.995  46.174  1.00 39.64 ? 71   VAL B N   1 
ATOM   4257 C  CA  . VAL B 2 71  ? 1.166   100.208 45.161  1.00 40.76 ? 71   VAL B CA  1 
ATOM   4258 C  C   . VAL B 2 71  ? 0.985   101.712 44.919  1.00 41.36 ? 71   VAL B C   1 
ATOM   4259 O  O   . VAL B 2 71  ? 0.795   102.100 43.747  1.00 37.29 ? 71   VAL B O   1 
ATOM   4260 C  CB  . VAL B 2 71  ? -0.161  99.560  45.586  1.00 40.09 ? 71   VAL B CB  1 
ATOM   4261 C  CG1 . VAL B 2 71  ? -1.326  100.019 44.718  1.00 39.21 ? 71   VAL B CG1 1 
ATOM   4262 C  CG2 . VAL B 2 71  ? -0.056  98.047  45.581  1.00 40.46 ? 71   VAL B CG2 1 
ATOM   4263 N  N   . HIS B 2 72  ? 0.997   102.511 45.988  1.00 42.48 ? 72   HIS B N   1 
ATOM   4264 C  CA  . HIS B 2 72  ? 0.939   103.998 45.923  1.00 46.52 ? 72   HIS B CA  1 
ATOM   4265 C  C   . HIS B 2 72  ? 2.042   104.509 44.982  1.00 44.97 ? 72   HIS B C   1 
ATOM   4266 O  O   . HIS B 2 72  ? 1.713   105.273 44.056  1.00 41.97 ? 72   HIS B O   1 
ATOM   4267 C  CB  . HIS B 2 72  ? 1.029   104.615 47.330  1.00 50.74 ? 72   HIS B CB  1 
ATOM   4268 C  CG  . HIS B 2 72  ? 1.173   106.102 47.336  1.00 56.71 ? 72   HIS B CG  1 
ATOM   4269 N  ND1 . HIS B 2 72  ? 0.158   106.948 46.925  1.00 60.35 ? 72   HIS B ND1 1 
ATOM   4270 C  CD2 . HIS B 2 72  ? 2.202   106.899 47.700  1.00 59.65 ? 72   HIS B CD2 1 
ATOM   4271 C  CE1 . HIS B 2 72  ? 0.559   108.199 47.034  1.00 58.35 ? 72   HIS B CE1 1 
ATOM   4272 N  NE2 . HIS B 2 72  ? 1.805   108.195 47.512  1.00 58.71 ? 72   HIS B NE2 1 
ATOM   4273 N  N   . ASP B 2 73  ? 3.290   104.077 45.197  1.00 42.16 ? 73   ASP B N   1 
ATOM   4274 C  CA  . ASP B 2 73  ? 4.475   104.540 44.427  1.00 44.29 ? 73   ASP B CA  1 
ATOM   4275 C  C   . ASP B 2 73  ? 4.342   104.074 42.973  1.00 43.27 ? 73   ASP B C   1 
ATOM   4276 O  O   . ASP B 2 73  ? 4.571   104.897 42.068  1.00 43.48 ? 73   ASP B O   1 
ATOM   4277 C  CB  . ASP B 2 73  ? 5.781   104.055 45.061  1.00 44.77 ? 73   ASP B CB  1 
ATOM   4278 C  CG  . ASP B 2 73  ? 6.050   104.620 46.448  1.00 45.41 ? 73   ASP B CG  1 
ATOM   4279 O  OD1 . ASP B 2 73  ? 5.362   105.587 46.843  1.00 48.56 ? 73   ASP B OD1 1 
ATOM   4280 O  OD2 . ASP B 2 73  ? 6.942   104.083 47.127  1.00 45.10 ? 73   ASP B OD2 1 
ATOM   4281 N  N   . LEU B 2 74  ? 3.971   102.808 42.766  1.00 42.60 ? 74   LEU B N   1 
ATOM   4282 C  CA  . LEU B 2 74  ? 3.800   102.204 41.418  1.00 44.69 ? 74   LEU B CA  1 
ATOM   4283 C  C   . LEU B 2 74  ? 2.673   102.933 40.674  1.00 47.35 ? 74   LEU B C   1 
ATOM   4284 O  O   . LEU B 2 74  ? 2.819   103.152 39.449  1.00 43.99 ? 74   LEU B O   1 
ATOM   4285 C  CB  . LEU B 2 74  ? 3.509   100.706 41.551  1.00 43.78 ? 74   LEU B CB  1 
ATOM   4286 C  CG  . LEU B 2 74  ? 4.660   99.855  42.094  1.00 43.76 ? 74   LEU B CG  1 
ATOM   4287 C  CD1 . LEU B 2 74  ? 4.242   98.401  42.239  1.00 41.41 ? 74   LEU B CD1 1 
ATOM   4288 C  CD2 . LEU B 2 74  ? 5.900   99.970  41.212  1.00 43.86 ? 74   LEU B CD2 1 
ATOM   4289 N  N   . ARG B 2 75  ? 1.595   103.303 41.375  1.00 48.67 ? 75   ARG B N   1 
ATOM   4290 C  CA  . ARG B 2 75  ? 0.486   104.092 40.763  1.00 51.51 ? 75   ARG B CA  1 
ATOM   4291 C  C   . ARG B 2 75  ? 1.062   105.438 40.293  1.00 50.69 ? 75   ARG B C   1 
ATOM   4292 O  O   . ARG B 2 75  ? 0.813   105.810 39.126  1.00 52.52 ? 75   ARG B O   1 
ATOM   4293 C  CB  . ARG B 2 75  ? -0.698  104.231 41.728  1.00 50.88 ? 75   ARG B CB  1 
ATOM   4294 C  CG  . ARG B 2 75  ? -1.638  103.031 41.719  1.00 52.53 ? 75   ARG B CG  1 
ATOM   4295 C  CD  . ARG B 2 75  ? -2.800  103.153 42.692  1.00 54.00 ? 75   ARG B CD  1 
ATOM   4296 N  NE  . ARG B 2 75  ? -3.495  101.881 42.897  1.00 54.62 ? 75   ARG B NE  1 
ATOM   4297 C  CZ  . ARG B 2 75  ? -4.258  101.577 43.954  1.00 57.26 ? 75   ARG B CZ  1 
ATOM   4298 N  NH1 . ARG B 2 75  ? -4.440  102.452 44.931  1.00 56.89 ? 75   ARG B NH1 1 
ATOM   4299 N  NH2 . ARG B 2 75  ? -4.833  100.388 44.040  1.00 57.17 ? 75   ARG B NH2 1 
ATOM   4300 N  N   . ASN B 2 76  ? 1.853   106.102 41.143  1.00 49.65 ? 76   ASN B N   1 
ATOM   4301 C  CA  . ASN B 2 76  ? 2.508   107.405 40.842  1.00 53.88 ? 76   ASN B CA  1 
ATOM   4302 C  C   . ASN B 2 76  ? 3.411   107.268 39.607  1.00 55.15 ? 76   ASN B C   1 
ATOM   4303 O  O   . ASN B 2 76  ? 3.320   108.131 38.712  1.00 55.77 ? 76   ASN B O   1 
ATOM   4304 C  CB  . ASN B 2 76  ? 3.302   107.940 42.036  1.00 54.37 ? 76   ASN B CB  1 
ATOM   4305 C  CG  . ASN B 2 76  ? 2.421   108.325 43.207  1.00 58.85 ? 76   ASN B CG  1 
ATOM   4306 O  OD1 . ASN B 2 76  ? 1.208   108.467 43.061  1.00 63.38 ? 76   ASN B OD1 1 
ATOM   4307 N  ND2 . ASN B 2 76  ? 3.019   108.493 44.375  1.00 61.32 ? 76   ASN B ND2 1 
ATOM   4308 N  N   . ALA B 2 77  ? 4.250   106.230 39.562  1.00 54.94 ? 77   ALA B N   1 
ATOM   4309 C  CA  . ALA B 2 77  ? 5.200   105.969 38.452  1.00 57.31 ? 77   ALA B CA  1 
ATOM   4310 C  C   . ALA B 2 77  ? 4.430   105.786 37.136  1.00 56.94 ? 77   ALA B C   1 
ATOM   4311 O  O   . ALA B 2 77  ? 4.905   106.277 36.096  1.00 57.24 ? 77   ALA B O   1 
ATOM   4312 C  CB  . ALA B 2 77  ? 6.055   104.765 38.767  1.00 56.97 ? 77   ALA B CB  1 
ATOM   4313 N  N   . LEU B 2 78  ? 3.280   105.111 37.186  1.00 58.58 ? 78   LEU B N   1 
ATOM   4314 C  CA  . LEU B 2 78  ? 2.421   104.845 36.000  1.00 61.36 ? 78   LEU B CA  1 
ATOM   4315 C  C   . LEU B 2 78  ? 1.782   106.160 35.536  1.00 64.92 ? 78   LEU B C   1 
ATOM   4316 O  O   . LEU B 2 78  ? 1.497   106.289 34.333  1.00 65.91 ? 78   LEU B O   1 
ATOM   4317 C  CB  . LEU B 2 78  ? 1.360   103.804 36.372  1.00 61.58 ? 78   LEU B CB  1 
ATOM   4318 C  CG  . LEU B 2 78  ? 0.783   102.990 35.215  1.00 64.87 ? 78   LEU B CG  1 
ATOM   4319 C  CD1 . LEU B 2 78  ? 1.886   102.371 34.365  1.00 67.43 ? 78   LEU B CD1 1 
ATOM   4320 C  CD2 . LEU B 2 78  ? -0.150  101.905 35.734  1.00 65.87 ? 78   LEU B CD2 1 
ATOM   4321 N  N   . THR B 2 79  ? 1.572   107.094 36.468  1.00 70.51 ? 79   THR B N   1 
ATOM   4322 C  CA  . THR B 2 79  ? 0.994   108.444 36.218  1.00 73.52 ? 79   THR B CA  1 
ATOM   4323 C  C   . THR B 2 79  ? 2.043   109.307 35.499  1.00 76.41 ? 79   THR B C   1 
ATOM   4324 O  O   . THR B 2 79  ? 1.689   109.918 34.474  1.00 77.26 ? 79   THR B O   1 
ATOM   4325 C  CB  . THR B 2 79  ? 0.447   109.029 37.529  1.00 76.23 ? 79   THR B CB  1 
ATOM   4326 O  OG1 . THR B 2 79  ? -0.855  108.473 37.715  1.00 72.50 ? 79   THR B OG1 1 
ATOM   4327 C  CG2 . THR B 2 79  ? 0.361   110.540 37.555  1.00 77.94 ? 79   THR B CG2 1 
ATOM   4328 N  N   . VAL B 2 80  ? 3.285   109.333 36.001  1.00 78.49 ? 80   VAL B N   1 
ATOM   4329 C  CA  . VAL B 2 80  ? 4.428   110.093 35.402  1.00 77.68 ? 80   VAL B CA  1 
ATOM   4330 C  C   . VAL B 2 80  ? 4.934   109.355 34.152  1.00 76.62 ? 80   VAL B C   1 
ATOM   4331 O  O   . VAL B 2 80  ? 4.138   108.609 33.544  1.00 75.78 ? 80   VAL B O   1 
ATOM   4332 C  CB  . VAL B 2 80  ? 5.567   110.306 36.422  1.00 77.38 ? 80   VAL B CB  1 
ATOM   4333 C  CG1 . VAL B 2 80  ? 6.821   110.876 35.770  1.00 77.35 ? 80   VAL B CG1 1 
ATOM   4334 C  CG2 . VAL B 2 80  ? 5.133   111.183 37.589  1.00 76.55 ? 80   VAL B CG2 1 
ATOM   4335 N  N   . ARG B 2 86  ? 7.040   103.415 26.477  1.00 52.72 ? 86   ARG B N   1 
ATOM   4336 C  CA  . ARG B 2 86  ? 8.111   102.634 27.150  1.00 51.16 ? 86   ARG B CA  1 
ATOM   4337 C  C   . ARG B 2 86  ? 7.652   102.251 28.556  1.00 49.80 ? 86   ARG B C   1 
ATOM   4338 O  O   . ARG B 2 86  ? 7.112   103.083 29.279  1.00 47.54 ? 86   ARG B O   1 
ATOM   4339 C  CB  . ARG B 2 86  ? 9.404   103.453 27.195  1.00 52.18 ? 86   ARG B CB  1 
ATOM   4340 N  N   . PRO B 2 87  ? 7.809   100.976 28.984  1.00 46.30 ? 87   PRO B N   1 
ATOM   4341 C  CA  . PRO B 2 87  ? 7.647   100.613 30.393  1.00 44.29 ? 87   PRO B CA  1 
ATOM   4342 C  C   . PRO B 2 87  ? 8.480   101.485 31.346  1.00 41.32 ? 87   PRO B C   1 
ATOM   4343 O  O   . PRO B 2 87  ? 9.558   101.871 30.972  1.00 41.10 ? 87   PRO B O   1 
ATOM   4344 C  CB  . PRO B 2 87  ? 8.162   99.167  30.439  1.00 44.64 ? 87   PRO B CB  1 
ATOM   4345 C  CG  . PRO B 2 87  ? 7.856   98.630  29.056  1.00 45.92 ? 87   PRO B CG  1 
ATOM   4346 C  CD  . PRO B 2 87  ? 8.086   99.810  28.132  1.00 46.75 ? 87   PRO B CD  1 
ATOM   4347 N  N   . ALA B 2 88  ? 7.962   101.766 32.544  1.00 38.36 ? 88   ALA B N   1 
ATOM   4348 C  CA  . ALA B 2 88  ? 8.697   102.460 33.626  1.00 39.37 ? 88   ALA B CA  1 
ATOM   4349 C  C   . ALA B 2 88  ? 9.699   101.486 34.257  1.00 39.61 ? 88   ALA B C   1 
ATOM   4350 O  O   . ALA B 2 88  ? 9.267   100.397 34.664  1.00 41.67 ? 88   ALA B O   1 
ATOM   4351 C  CB  . ALA B 2 88  ? 7.736   103.007 34.652  1.00 40.06 ? 88   ALA B CB  1 
ATOM   4352 N  N   . MET B 2 89  ? 10.980  101.869 34.310  1.00 41.70 ? 89   MET B N   1 
ATOM   4353 C  CA  . MET B 2 89  ? 12.088  101.087 34.926  1.00 44.31 ? 89   MET B CA  1 
ATOM   4354 C  C   . MET B 2 89  ? 12.405  101.726 36.282  1.00 41.65 ? 89   MET B C   1 
ATOM   4355 O  O   . MET B 2 89  ? 12.925  102.856 36.287  1.00 42.57 ? 89   MET B O   1 
ATOM   4356 C  CB  . MET B 2 89  ? 13.362  101.080 34.065  1.00 47.04 ? 89   MET B CB  1 
ATOM   4357 C  CG  . MET B 2 89  ? 13.168  100.679 32.609  1.00 49.26 ? 89   MET B CG  1 
ATOM   4358 S  SD  . MET B 2 89  ? 12.307  99.107  32.349  1.00 58.32 ? 89   MET B SD  1 
ATOM   4359 C  CE  . MET B 2 89  ? 13.447  97.934  33.068  1.00 56.57 ? 89   MET B CE  1 
ATOM   4360 N  N   . LEU B 2 90  ? 12.093  101.027 37.377  1.00 39.64 ? 90   LEU B N   1 
ATOM   4361 C  CA  . LEU B 2 90  ? 12.179  101.548 38.769  1.00 38.85 ? 90   LEU B CA  1 
ATOM   4362 C  C   . LEU B 2 90  ? 13.153  100.679 39.558  1.00 37.63 ? 90   LEU B C   1 
ATOM   4363 O  O   . LEU B 2 90  ? 12.744  99.720  40.216  1.00 38.11 ? 90   LEU B O   1 
ATOM   4364 C  CB  . LEU B 2 90  ? 10.775  101.545 39.391  1.00 39.36 ? 90   LEU B CB  1 
ATOM   4365 C  CG  . LEU B 2 90  ? 9.687   102.205 38.540  1.00 40.66 ? 90   LEU B CG  1 
ATOM   4366 C  CD1 . LEU B 2 90  ? 8.298   101.892 39.075  1.00 39.14 ? 90   LEU B CD1 1 
ATOM   4367 C  CD2 . LEU B 2 90  ? 9.905   103.712 38.449  1.00 40.80 ? 90   LEU B CD2 1 
ATOM   4368 N  N   . PRO B 2 91  ? 14.474  100.973 39.509  1.00 35.03 ? 91   PRO B N   1 
ATOM   4369 C  CA  . PRO B 2 91  ? 15.457  100.191 40.253  1.00 35.52 ? 91   PRO B CA  1 
ATOM   4370 C  C   . PRO B 2 91  ? 15.346  100.408 41.771  1.00 36.01 ? 91   PRO B C   1 
ATOM   4371 O  O   . PRO B 2 91  ? 14.942  101.476 42.190  1.00 35.93 ? 91   PRO B O   1 
ATOM   4372 C  CB  . PRO B 2 91  ? 16.827  100.697 39.767  1.00 35.39 ? 91   PRO B CB  1 
ATOM   4373 C  CG  . PRO B 2 91  ? 16.529  101.583 38.562  1.00 36.43 ? 91   PRO B CG  1 
ATOM   4374 C  CD  . PRO B 2 91  ? 15.100  102.057 38.738  1.00 35.65 ? 91   PRO B CD  1 
ATOM   4375 N  N   . ALA B 2 92  ? 15.723  99.390  42.543  1.00 37.40 ? 92   ALA B N   1 
ATOM   4376 C  CA  . ALA B 2 92  ? 15.937  99.460  44.008  1.00 38.12 ? 92   ALA B CA  1 
ATOM   4377 C  C   . ALA B 2 92  ? 14.675  99.985  44.705  1.00 38.10 ? 92   ALA B C   1 
ATOM   4378 O  O   . ALA B 2 92  ? 14.799  100.902 45.532  1.00 41.46 ? 92   ALA B O   1 
ATOM   4379 C  CB  . ALA B 2 92  ? 17.133  100.335 44.291  1.00 37.74 ? 92   ALA B CB  1 
ATOM   4380 N  N   . MET B 2 93  ? 13.508  99.429  44.374  1.00 39.22 ? 93   MET B N   1 
ATOM   4381 C  CA  . MET B 2 93  ? 12.234  99.689  45.095  1.00 40.94 ? 93   MET B CA  1 
ATOM   4382 C  C   . MET B 2 93  ? 12.184  98.807  46.351  1.00 41.11 ? 93   MET B C   1 
ATOM   4383 O  O   . MET B 2 93  ? 12.407  97.590  46.224  1.00 41.32 ? 93   MET B O   1 
ATOM   4384 C  CB  . MET B 2 93  ? 11.024  99.392  44.207  1.00 40.51 ? 93   MET B CB  1 
ATOM   4385 C  CG  . MET B 2 93  ? 10.937  100.287 42.992  1.00 43.72 ? 93   MET B CG  1 
ATOM   4386 S  SD  . MET B 2 93  ? 10.573  102.010 43.408  1.00 48.10 ? 93   MET B SD  1 
ATOM   4387 C  CE  . MET B 2 93  ? 8.814   101.909 43.744  1.00 49.08 ? 93   MET B CE  1 
ATOM   4388 N  N   . GLU B 2 94  ? 11.906  99.412  47.512  1.00 43.25 ? 94   GLU B N   1 
ATOM   4389 C  CA  . GLU B 2 94  ? 11.741  98.721  48.821  1.00 43.69 ? 94   GLU B CA  1 
ATOM   4390 C  C   . GLU B 2 94  ? 10.370  98.037  48.844  1.00 43.65 ? 94   GLU B C   1 
ATOM   4391 O  O   . GLU B 2 94  ? 9.356   98.734  48.641  1.00 44.81 ? 94   GLU B O   1 
ATOM   4392 C  CB  . GLU B 2 94  ? 11.880  99.708  49.983  1.00 42.21 ? 94   GLU B CB  1 
ATOM   4393 N  N   . THR B 2 95  ? 10.357  96.718  49.043  1.00 43.91 ? 95   THR B N   1 
ATOM   4394 C  CA  . THR B 2 95  ? 9.119   95.903  49.211  1.00 48.05 ? 95   THR B CA  1 
ATOM   4395 C  C   . THR B 2 95  ? 8.742   95.883  50.698  1.00 49.95 ? 95   THR B C   1 
ATOM   4396 O  O   . THR B 2 95  ? 9.552   96.371  51.525  1.00 46.85 ? 95   THR B O   1 
ATOM   4397 C  CB  . THR B 2 95  ? 9.287   94.489  48.640  1.00 49.49 ? 95   THR B CB  1 
ATOM   4398 O  OG1 . THR B 2 95  ? 10.524  93.961  49.119  1.00 50.26 ? 95   THR B OG1 1 
ATOM   4399 C  CG2 . THR B 2 95  ? 9.263   94.468  47.128  1.00 52.97 ? 95   THR B CG2 1 
ATOM   4400 N  N   . SER B 2 96  ? 7.564   95.334  51.012  1.00 52.52 ? 96   SER B N   1 
ATOM   4401 C  CA  . SER B 2 96  ? 6.953   95.331  52.376  1.00 55.17 ? 96   SER B CA  1 
ATOM   4402 C  C   . SER B 2 96  ? 7.860   94.632  53.404  1.00 54.36 ? 96   SER B C   1 
ATOM   4403 O  O   . SER B 2 96  ? 7.743   94.972  54.597  1.00 57.66 ? 96   SER B O   1 
ATOM   4404 C  CB  . SER B 2 96  ? 5.566   94.719  52.367  1.00 54.92 ? 96   SER B CB  1 
ATOM   4405 O  OG  . SER B 2 96  ? 5.599   93.368  51.925  1.00 54.63 ? 96   SER B OG  1 
ATOM   4406 N  N   . ASP B 2 97  ? 8.720   93.699  52.971  1.00 51.53 ? 97   ASP B N   1 
ATOM   4407 C  CA  . ASP B 2 97  ? 9.566   92.858  53.866  1.00 50.48 ? 97   ASP B CA  1 
ATOM   4408 C  C   . ASP B 2 97  ? 10.984  93.437  53.984  1.00 48.89 ? 97   ASP B C   1 
ATOM   4409 O  O   . ASP B 2 97  ? 11.867  92.709  54.465  1.00 49.68 ? 97   ASP B O   1 
ATOM   4410 C  CB  . ASP B 2 97  ? 9.591   91.402  53.390  1.00 52.87 ? 97   ASP B CB  1 
ATOM   4411 C  CG  . ASP B 2 97  ? 10.203  91.184  52.013  1.00 55.41 ? 97   ASP B CG  1 
ATOM   4412 O  OD1 . ASP B 2 97  ? 10.890  92.103  51.511  1.00 49.62 ? 97   ASP B OD1 1 
ATOM   4413 O  OD2 . ASP B 2 97  ? 9.993   90.086  51.449  1.00 60.66 ? 97   ASP B OD2 1 
ATOM   4414 N  N   . GLY B 2 98  ? 11.198  94.685  53.556  1.00 50.82 ? 98   GLY B N   1 
ATOM   4415 C  CA  . GLY B 2 98  ? 12.486  95.400  53.690  1.00 52.66 ? 98   GLY B CA  1 
ATOM   4416 C  C   . GLY B 2 98  ? 13.373  95.293  52.451  1.00 51.86 ? 98   GLY B C   1 
ATOM   4417 O  O   . GLY B 2 98  ? 14.167  96.230  52.218  1.00 51.12 ? 98   GLY B O   1 
ATOM   4418 N  N   . ARG B 2 99  ? 13.243  94.213  51.673  1.00 48.62 ? 99   ARG B N   1 
ATOM   4419 C  CA  . ARG B 2 99  ? 14.168  93.870  50.554  1.00 47.77 ? 99   ARG B CA  1 
ATOM   4420 C  C   . ARG B 2 99  ? 13.991  94.848  49.384  1.00 45.22 ? 99   ARG B C   1 
ATOM   4421 O  O   . ARG B 2 99  ? 12.921  95.478  49.287  1.00 42.27 ? 99   ARG B O   1 
ATOM   4422 C  CB  . ARG B 2 99  ? 13.924  92.431  50.095  1.00 47.76 ? 99   ARG B CB  1 
ATOM   4423 C  CG  . ARG B 2 99  ? 14.239  91.388  51.157  1.00 49.09 ? 99   ARG B CG  1 
ATOM   4424 C  CD  . ARG B 2 99  ? 14.186  89.993  50.575  1.00 49.86 ? 99   ARG B CD  1 
ATOM   4425 N  NE  . ARG B 2 99  ? 12.829  89.634  50.185  1.00 50.31 ? 99   ARG B NE  1 
ATOM   4426 C  CZ  . ARG B 2 99  ? 12.501  88.603  49.410  1.00 50.74 ? 99   ARG B CZ  1 
ATOM   4427 N  NH1 . ARG B 2 99  ? 13.439  87.812  48.911  1.00 52.10 ? 99   ARG B NH1 1 
ATOM   4428 N  NH2 . ARG B 2 99  ? 11.230  88.367  49.132  1.00 48.90 ? 99   ARG B NH2 1 
ATOM   4429 N  N   . SER B 2 100 ? 15.017  94.954  48.529  1.00 45.40 ? 100  SER B N   1 
ATOM   4430 C  CA  . SER B 2 100 ? 15.046  95.825  47.323  1.00 43.19 ? 100  SER B CA  1 
ATOM   4431 C  C   . SER B 2 100 ? 14.763  94.984  46.073  1.00 40.50 ? 100  SER B C   1 
ATOM   4432 O  O   . SER B 2 100 ? 15.360  93.904  45.944  1.00 40.96 ? 100  SER B O   1 
ATOM   4433 C  CB  . SER B 2 100 ? 16.355  96.560  47.204  1.00 45.92 ? 100  SER B CB  1 
ATOM   4434 O  OG  . SER B 2 100 ? 16.406  97.653  48.111  1.00 46.98 ? 100  SER B OG  1 
ATOM   4435 N  N   . PHE B 2 101 ? 13.882  95.471  45.196  1.00 38.60 ? 101  PHE B N   1 
ATOM   4436 C  CA  . PHE B 2 101 ? 13.556  94.852  43.883  1.00 37.22 ? 101  PHE B CA  1 
ATOM   4437 C  C   . PHE B 2 101 ? 13.640  95.914  42.788  1.00 35.63 ? 101  PHE B C   1 
ATOM   4438 O  O   . PHE B 2 101 ? 13.184  97.055  43.013  1.00 37.62 ? 101  PHE B O   1 
ATOM   4439 C  CB  . PHE B 2 101 ? 12.183  94.175  43.917  1.00 38.19 ? 101  PHE B CB  1 
ATOM   4440 C  CG  . PHE B 2 101 ? 12.202  92.834  44.601  1.00 39.84 ? 101  PHE B CG  1 
ATOM   4441 C  CD1 . PHE B 2 101 ? 12.052  92.735  45.977  1.00 41.41 ? 101  PHE B CD1 1 
ATOM   4442 C  CD2 . PHE B 2 101 ? 12.426  91.674  43.876  1.00 41.48 ? 101  PHE B CD2 1 
ATOM   4443 C  CE1 . PHE B 2 101 ? 12.102  91.501  46.608  1.00 42.64 ? 101  PHE B CE1 1 
ATOM   4444 C  CE2 . PHE B 2 101 ? 12.477  90.440  44.511  1.00 43.16 ? 101  PHE B CE2 1 
ATOM   4445 C  CZ  . PHE B 2 101 ? 12.319  90.356  45.875  1.00 41.61 ? 101  PHE B CZ  1 
ATOM   4446 N  N   . ASP B 2 102 ? 14.244  95.547  41.654  1.00 33.99 ? 102  ASP B N   1 
ATOM   4447 C  CA  . ASP B 2 102 ? 14.192  96.336  40.397  1.00 32.34 ? 102  ASP B CA  1 
ATOM   4448 C  C   . ASP B 2 102 ? 12.846  96.008  39.738  1.00 30.93 ? 102  ASP B C   1 
ATOM   4449 O  O   . ASP B 2 102 ? 12.597  94.816  39.454  1.00 29.98 ? 102  ASP B O   1 
ATOM   4450 C  CB  . ASP B 2 102 ? 15.402  96.054  39.497  1.00 31.43 ? 102  ASP B CB  1 
ATOM   4451 C  CG  . ASP B 2 102 ? 16.753  96.375  40.125  1.00 32.09 ? 102  ASP B CG  1 
ATOM   4452 O  OD1 . ASP B 2 102 ? 16.801  97.171  41.094  1.00 30.14 ? 102  ASP B OD1 1 
ATOM   4453 O  OD2 . ASP B 2 102 ? 17.756  95.835  39.628  1.00 33.37 ? 102  ASP B OD2 1 
ATOM   4454 N  N   . ILE B 2 103 ? 11.988  97.014  39.556  1.00 29.69 ? 103  ILE B N   1 
ATOM   4455 C  CA  . ILE B 2 103 ? 10.600  96.803  39.054  1.00 30.60 ? 103  ILE B CA  1 
ATOM   4456 C  C   . ILE B 2 103 ? 10.459  97.470  37.684  1.00 30.02 ? 103  ILE B C   1 
ATOM   4457 O  O   . ILE B 2 103 ? 10.904  98.612  37.525  1.00 31.13 ? 103  ILE B O   1 
ATOM   4458 C  CB  . ILE B 2 103 ? 9.543   97.312  40.061  1.00 30.52 ? 103  ILE B CB  1 
ATOM   4459 C  CG1 . ILE B 2 103 ? 9.674   96.605  41.412  1.00 32.04 ? 103  ILE B CG1 1 
ATOM   4460 C  CG2 . ILE B 2 103 ? 8.142   97.167  39.483  1.00 29.22 ? 103  ILE B CG2 1 
ATOM   4461 C  CD1 . ILE B 2 103 ? 8.776   97.153  42.499  1.00 33.19 ? 103  ILE B CD1 1 
ATOM   4462 N  N   . SER B 2 104 ? 9.846   96.758  36.744  1.00 31.09 ? 104  SER B N   1 
ATOM   4463 C  CA  . SER B 2 104 ? 9.409   97.298  35.435  1.00 33.56 ? 104  SER B CA  1 
ATOM   4464 C  C   . SER B 2 104 ? 7.878   97.311  35.413  1.00 33.88 ? 104  SER B C   1 
ATOM   4465 O  O   . SER B 2 104 ? 7.277   96.290  35.767  1.00 35.06 ? 104  SER B O   1 
ATOM   4466 C  CB  . SER B 2 104 ? 10.003  96.502  34.304  1.00 34.49 ? 104  SER B CB  1 
ATOM   4467 O  OG  . SER B 2 104 ? 9.509   96.960  33.058  1.00 37.77 ? 104  SER B OG  1 
ATOM   4468 N  N   . LEU B 2 105 ? 7.278   98.438  35.033  1.00 35.10 ? 105  LEU B N   1 
ATOM   4469 C  CA  . LEU B 2 105 ? 5.812   98.670  35.130  1.00 37.46 ? 105  LEU B CA  1 
ATOM   4470 C  C   . LEU B 2 105 ? 5.295   99.214  33.795  1.00 34.71 ? 105  LEU B C   1 
ATOM   4471 O  O   . LEU B 2 105 ? 5.847   100.218 33.314  1.00 33.14 ? 105  LEU B O   1 
ATOM   4472 C  CB  . LEU B 2 105 ? 5.570   99.658  36.278  1.00 40.06 ? 105  LEU B CB  1 
ATOM   4473 C  CG  . LEU B 2 105 ? 4.120   100.078 36.515  1.00 45.23 ? 105  LEU B CG  1 
ATOM   4474 C  CD1 . LEU B 2 105 ? 3.316   98.953  37.145  1.00 47.14 ? 105  LEU B CD1 1 
ATOM   4475 C  CD2 . LEU B 2 105 ? 4.062   101.322 37.386  1.00 46.30 ? 105  LEU B CD2 1 
ATOM   4476 N  N   . HIS B 2 106 ? 4.260   98.592  33.232  1.00 33.10 ? 106  HIS B N   1 
ATOM   4477 C  CA  . HIS B 2 106 ? 3.559   99.127  32.036  1.00 35.35 ? 106  HIS B CA  1 
ATOM   4478 C  C   . HIS B 2 106 ? 2.095   98.692  32.038  1.00 37.62 ? 106  HIS B C   1 
ATOM   4479 O  O   . HIS B 2 106 ? 1.762   97.677  32.699  1.00 37.01 ? 106  HIS B O   1 
ATOM   4480 C  CB  . HIS B 2 106 ? 4.281   98.731  30.738  1.00 33.59 ? 106  HIS B CB  1 
ATOM   4481 C  CG  . HIS B 2 106 ? 4.061   97.315  30.311  1.00 33.14 ? 106  HIS B CG  1 
ATOM   4482 N  ND1 . HIS B 2 106 ? 4.820   96.272  30.795  1.00 32.06 ? 106  HIS B ND1 1 
ATOM   4483 C  CD2 . HIS B 2 106 ? 3.198   96.772  29.427  1.00 33.47 ? 106  HIS B CD2 1 
ATOM   4484 C  CE1 . HIS B 2 106 ? 4.429   95.142  30.236  1.00 32.20 ? 106  HIS B CE1 1 
ATOM   4485 N  NE2 . HIS B 2 106 ? 3.432   95.422  29.391  1.00 32.79 ? 106  HIS B NE2 1 
ATOM   4486 N  N   . ARG B 2 107 ? 1.271   99.475  31.337  1.00 39.94 ? 107  ARG B N   1 
ATOM   4487 C  CA  . ARG B 2 107 ? -0.151  99.172  31.029  1.00 40.79 ? 107  ARG B CA  1 
ATOM   4488 C  C   . ARG B 2 107 ? -0.244  98.909  29.526  1.00 41.14 ? 107  ARG B C   1 
ATOM   4489 O  O   . ARG B 2 107 ? 0.325   99.703  28.763  1.00 40.95 ? 107  ARG B O   1 
ATOM   4490 C  CB  . ARG B 2 107 ? -1.059  100.333 31.458  1.00 41.47 ? 107  ARG B CB  1 
ATOM   4491 N  N   . TYR B 2 108 ? -0.911  97.826  29.130  1.00 40.98 ? 108  TYR B N   1 
ATOM   4492 C  CA  . TYR B 2 108 ? -1.196  97.482  27.711  1.00 43.29 ? 108  TYR B CA  1 
ATOM   4493 C  C   . TYR B 2 108 ? -2.382  96.515  27.671  1.00 44.01 ? 108  TYR B C   1 
ATOM   4494 O  O   . TYR B 2 108 ? -2.477  95.660  28.579  1.00 42.21 ? 108  TYR B O   1 
ATOM   4495 C  CB  . TYR B 2 108 ? 0.054   96.903  27.039  1.00 43.64 ? 108  TYR B CB  1 
ATOM   4496 C  CG  . TYR B 2 108 ? -0.077  96.628  25.560  1.00 42.76 ? 108  TYR B CG  1 
ATOM   4497 C  CD1 . TYR B 2 108 ? -0.425  97.632  24.665  1.00 42.17 ? 108  TYR B CD1 1 
ATOM   4498 C  CD2 . TYR B 2 108 ? 0.163   95.360  25.049  1.00 40.61 ? 108  TYR B CD2 1 
ATOM   4499 C  CE1 . TYR B 2 108 ? -0.538  97.379  23.304  1.00 42.22 ? 108  TYR B CE1 1 
ATOM   4500 C  CE2 . TYR B 2 108 ? 0.044   95.091  23.695  1.00 40.47 ? 108  TYR B CE2 1 
ATOM   4501 C  CZ  . TYR B 2 108 ? -0.308  96.102  22.819  1.00 40.35 ? 108  TYR B CZ  1 
ATOM   4502 O  OH  . TYR B 2 108 ? -0.411  95.817  21.487  1.00 41.20 ? 108  TYR B OH  1 
ATOM   4503 N  N   . LYS B 2 109 ? -3.259  96.663  26.669  1.00 45.61 ? 109  LYS B N   1 
ATOM   4504 C  CA  . LYS B 2 109 ? -4.495  95.844  26.504  1.00 47.14 ? 109  LYS B CA  1 
ATOM   4505 C  C   . LYS B 2 109 ? -5.269  95.803  27.836  1.00 46.36 ? 109  LYS B C   1 
ATOM   4506 O  O   . LYS B 2 109 ? -5.588  94.688  28.298  1.00 43.85 ? 109  LYS B O   1 
ATOM   4507 C  CB  . LYS B 2 109 ? -4.147  94.424  26.038  1.00 48.75 ? 109  LYS B CB  1 
ATOM   4508 C  CG  . LYS B 2 109 ? -3.449  94.317  24.687  1.00 50.53 ? 109  LYS B CG  1 
ATOM   4509 C  CD  . LYS B 2 109 ? -4.338  94.638  23.504  1.00 51.85 ? 109  LYS B CD  1 
ATOM   4510 C  CE  . LYS B 2 109 ? -3.663  94.372  22.175  1.00 52.88 ? 109  LYS B CE  1 
ATOM   4511 N  NZ  . LYS B 2 109 ? -4.281  95.154  21.078  1.00 54.54 ? 109  LYS B NZ  1 
ATOM   4512 N  N   . SER B 2 110 ? -5.521  96.969  28.445  1.00 44.07 ? 110  SER B N   1 
ATOM   4513 C  CA  . SER B 2 110 ? -6.366  97.131  29.663  1.00 48.39 ? 110  SER B CA  1 
ATOM   4514 C  C   . SER B 2 110 ? -5.806  96.330  30.850  1.00 49.55 ? 110  SER B C   1 
ATOM   4515 O  O   . SER B 2 110 ? -6.601  95.956  31.737  1.00 53.39 ? 110  SER B O   1 
ATOM   4516 C  CB  . SER B 2 110 ? -7.794  96.733  29.372  1.00 45.22 ? 110  SER B CB  1 
ATOM   4517 N  N   . THR B 2 111 ? -4.493  96.076  30.870  1.00 48.22 ? 111  THR B N   1 
ATOM   4518 C  CA  . THR B 2 111 ? -3.815  95.235  31.899  1.00 46.79 ? 111  THR B CA  1 
ATOM   4519 C  C   . THR B 2 111 ? -2.555  95.950  32.390  1.00 45.48 ? 111  THR B C   1 
ATOM   4520 O  O   . THR B 2 111 ? -1.797  96.442  31.535  1.00 48.60 ? 111  THR B O   1 
ATOM   4521 C  CB  . THR B 2 111 ? -3.454  93.851  31.341  1.00 47.93 ? 111  THR B CB  1 
ATOM   4522 O  OG1 . THR B 2 111 ? -4.570  93.321  30.624  1.00 48.93 ? 111  THR B OG1 1 
ATOM   4523 C  CG2 . THR B 2 111 ? -3.034  92.871  32.414  1.00 47.86 ? 111  THR B CG2 1 
ATOM   4524 N  N   . THR B 2 112 ? -2.352  96.021  33.707  1.00 41.49 ? 112  THR B N   1 
ATOM   4525 C  CA  . THR B 2 112 ? -1.094  96.540  34.315  1.00 42.00 ? 112  THR B CA  1 
ATOM   4526 C  C   . THR B 2 112 ? -0.150  95.368  34.585  1.00 38.91 ? 112  THR B C   1 
ATOM   4527 O  O   . THR B 2 112 ? -0.543  94.450  35.324  1.00 39.35 ? 112  THR B O   1 
ATOM   4528 C  CB  . THR B 2 112 ? -1.340  97.336  35.600  1.00 44.42 ? 112  THR B CB  1 
ATOM   4529 O  OG1 . THR B 2 112 ? -2.189  98.432  35.267  1.00 46.47 ? 112  THR B OG1 1 
ATOM   4530 C  CG2 . THR B 2 112 ? -0.061  97.861  36.220  1.00 47.26 ? 112  THR B CG2 1 
ATOM   4531 N  N   . ILE B 2 113 ? 1.044   95.397  33.999  1.00 36.48 ? 113  ILE B N   1 
ATOM   4532 C  CA  . ILE B 2 113 ? 2.047   94.304  34.156  1.00 34.81 ? 113  ILE B CA  1 
ATOM   4533 C  C   . ILE B 2 113 ? 3.186   94.851  35.016  1.00 33.38 ? 113  ILE B C   1 
ATOM   4534 O  O   . ILE B 2 113 ? 3.799   95.874  34.639  1.00 32.57 ? 113  ILE B O   1 
ATOM   4535 C  CB  . ILE B 2 113 ? 2.504   93.752  32.793  1.00 36.30 ? 113  ILE B CB  1 
ATOM   4536 C  CG1 . ILE B 2 113 ? 1.377   92.962  32.120  1.00 35.90 ? 113  ILE B CG1 1 
ATOM   4537 C  CG2 . ILE B 2 113 ? 3.770   92.909  32.933  1.00 37.48 ? 113  ILE B CG2 1 
ATOM   4538 C  CD1 . ILE B 2 113 ? 1.578   92.730  30.640  1.00 36.34 ? 113  ILE B CD1 1 
ATOM   4539 N  N   . ILE B 2 114 ? 3.411   94.205  36.157  1.00 32.41 ? 114  ILE B N   1 
ATOM   4540 C  CA  . ILE B 2 114 ? 4.520   94.523  37.098  1.00 32.17 ? 114  ILE B CA  1 
ATOM   4541 C  C   . ILE B 2 114 ? 5.527   93.375  37.027  1.00 31.84 ? 114  ILE B C   1 
ATOM   4542 O  O   . ILE B 2 114 ? 5.116   92.204  37.198  1.00 30.89 ? 114  ILE B O   1 
ATOM   4543 C  CB  . ILE B 2 114 ? 4.011   94.742  38.532  1.00 32.92 ? 114  ILE B CB  1 
ATOM   4544 C  CG1 . ILE B 2 114 ? 2.667   95.477  38.552  1.00 35.00 ? 114  ILE B CG1 1 
ATOM   4545 C  CG2 . ILE B 2 114 ? 5.080   95.454  39.353  1.00 33.33 ? 114  ILE B CG2 1 
ATOM   4546 C  CD1 . ILE B 2 114 ? 1.997   95.501  39.909  1.00 36.10 ? 114  ILE B CD1 1 
ATOM   4547 N  N   . GLU B 2 115 ? 6.789   93.711  36.762  1.00 29.50 ? 115  GLU B N   1 
ATOM   4548 C  CA  . GLU B 2 115 ? 7.882   92.721  36.630  1.00 29.45 ? 115  GLU B CA  1 
ATOM   4549 C  C   . GLU B 2 115 ? 8.926   93.010  37.710  1.00 28.23 ? 115  GLU B C   1 
ATOM   4550 O  O   . GLU B 2 115 ? 9.243   94.192  37.918  1.00 27.87 ? 115  GLU B O   1 
ATOM   4551 C  CB  . GLU B 2 115 ? 8.442   92.770  35.213  1.00 29.38 ? 115  GLU B CB  1 
ATOM   4552 C  CG  . GLU B 2 115 ? 7.433   92.358  34.156  1.00 28.28 ? 115  GLU B CG  1 
ATOM   4553 C  CD  . GLU B 2 115 ? 8.024   92.394  32.762  1.00 28.50 ? 115  GLU B CD  1 
ATOM   4554 O  OE1 . GLU B 2 115 ? 8.190   93.507  32.217  1.00 29.41 ? 115  GLU B OE1 1 
ATOM   4555 O  OE2 . GLU B 2 115 ? 8.368   91.315  32.247  1.00 29.71 ? 115  GLU B OE2 1 
ATOM   4556 N  N   . PHE B 2 116 ? 9.424   91.960  38.363  1.00 27.30 ? 116  PHE B N   1 
ATOM   4557 C  CA  . PHE B 2 116 ? 10.301  92.057  39.558  1.00 30.31 ? 116  PHE B CA  1 
ATOM   4558 C  C   . PHE B 2 116 ? 11.583  91.258  39.338  1.00 29.03 ? 116  PHE B C   1 
ATOM   4559 O  O   . PHE B 2 116 ? 11.503  90.108  38.876  1.00 29.88 ? 116  PHE B O   1 
ATOM   4560 C  CB  . PHE B 2 116 ? 9.601   91.528  40.814  1.00 31.62 ? 116  PHE B CB  1 
ATOM   4561 C  CG  . PHE B 2 116 ? 8.295   92.195  41.170  1.00 32.53 ? 116  PHE B CG  1 
ATOM   4562 C  CD1 . PHE B 2 116 ? 7.109   91.792  40.575  1.00 33.73 ? 116  PHE B CD1 1 
ATOM   4563 C  CD2 . PHE B 2 116 ? 8.248   93.195  42.133  1.00 34.27 ? 116  PHE B CD2 1 
ATOM   4564 C  CE1 . PHE B 2 116 ? 5.905   92.390  40.918  1.00 35.40 ? 116  PHE B CE1 1 
ATOM   4565 C  CE2 . PHE B 2 116 ? 7.044   93.794  42.473  1.00 34.64 ? 116  PHE B CE2 1 
ATOM   4566 C  CZ  . PHE B 2 116 ? 5.877   93.394  41.862  1.00 34.81 ? 116  PHE B CZ  1 
ATOM   4567 N  N   . GLU B 2 117 ? 12.713  91.868  39.701  1.00 30.76 ? 117  GLU B N   1 
ATOM   4568 C  CA  . GLU B 2 117 ? 14.054  91.228  39.789  1.00 32.27 ? 117  GLU B CA  1 
ATOM   4569 C  C   . GLU B 2 117 ? 14.709  91.620  41.112  1.00 30.77 ? 117  GLU B C   1 
ATOM   4570 O  O   . GLU B 2 117 ? 14.674  92.787  41.505  1.00 27.62 ? 117  GLU B O   1 
ATOM   4571 C  CB  . GLU B 2 117 ? 14.951  91.693  38.639  1.00 34.72 ? 117  GLU B CB  1 
ATOM   4572 C  CG  . GLU B 2 117 ? 14.294  91.650  37.272  1.00 37.64 ? 117  GLU B CG  1 
ATOM   4573 C  CD  . GLU B 2 117 ? 15.074  92.448  36.245  1.00 38.01 ? 117  GLU B CD  1 
ATOM   4574 O  OE1 . GLU B 2 117 ? 14.634  93.554  35.893  1.00 37.48 ? 117  GLU B OE1 1 
ATOM   4575 O  OE2 . GLU B 2 117 ? 16.144  91.975  35.837  1.00 43.94 ? 117  GLU B OE2 1 
ATOM   4576 N  N   . PRO B 2 118 ? 15.346  90.676  41.838  1.00 32.84 ? 118  PRO B N   1 
ATOM   4577 C  CA  . PRO B 2 118 ? 16.105  91.030  43.037  1.00 34.18 ? 118  PRO B CA  1 
ATOM   4578 C  C   . PRO B 2 118 ? 17.107  92.144  42.704  1.00 34.39 ? 118  PRO B C   1 
ATOM   4579 O  O   . PRO B 2 118 ? 17.785  92.005  41.697  1.00 34.45 ? 118  PRO B O   1 
ATOM   4580 C  CB  . PRO B 2 118 ? 16.842  89.740  43.426  1.00 34.86 ? 118  PRO B CB  1 
ATOM   4581 C  CG  . PRO B 2 118 ? 16.081  88.620  42.737  1.00 35.78 ? 118  PRO B CG  1 
ATOM   4582 C  CD  . PRO B 2 118 ? 15.381  89.236  41.542  1.00 34.73 ? 118  PRO B CD  1 
ATOM   4583 N  N   . SER B 2 119 ? 17.146  93.220  43.496  1.00 33.12 ? 119  SER B N   1 
ATOM   4584 C  CA  . SER B 2 119 ? 18.115  94.337  43.306  1.00 35.59 ? 119  SER B CA  1 
ATOM   4585 C  C   . SER B 2 119 ? 19.515  93.866  43.710  1.00 37.49 ? 119  SER B C   1 
ATOM   4586 O  O   . SER B 2 119 ? 19.622  93.125  44.707  1.00 37.98 ? 119  SER B O   1 
ATOM   4587 C  CB  . SER B 2 119 ? 17.741  95.565  44.090  1.00 35.77 ? 119  SER B CB  1 
ATOM   4588 O  OG  . SER B 2 119 ? 16.486  96.070  43.676  1.00 37.32 ? 119  SER B OG  1 
ATOM   4589 N  N   . GLY B 2 120 ? 20.534  94.276  42.953  1.00 37.14 ? 120  GLY B N   1 
ATOM   4590 C  CA  . GLY B 2 120 ? 21.955  94.167  43.339  1.00 37.30 ? 120  GLY B CA  1 
ATOM   4591 C  C   . GLY B 2 120 ? 22.471  95.524  43.776  1.00 37.93 ? 120  GLY B C   1 
ATOM   4592 O  O   . GLY B 2 120 ? 21.645  96.349  44.219  1.00 40.21 ? 120  GLY B O   1 
ATOM   4593 N  N   . SER B 2 121 ? 23.778  95.752  43.642  1.00 36.55 ? 121  SER B N   1 
ATOM   4594 C  CA  . SER B 2 121 ? 24.432  97.075  43.847  1.00 39.77 ? 121  SER B CA  1 
ATOM   4595 C  C   . SER B 2 121 ? 24.907  97.621  42.495  1.00 40.23 ? 121  SER B C   1 
ATOM   4596 O  O   . SER B 2 121 ? 25.710  96.945  41.845  1.00 45.49 ? 121  SER B O   1 
ATOM   4597 C  CB  . SER B 2 121 ? 25.559  96.972  44.836  1.00 39.66 ? 121  SER B CB  1 
ATOM   4598 O  OG  . SER B 2 121 ? 25.119  96.317  46.018  1.00 41.50 ? 121  SER B OG  1 
ATOM   4599 N  N   . ASP B 2 122 ? 24.420  98.796  42.094  1.00 42.06 ? 122  ASP B N   1 
ATOM   4600 C  CA  . ASP B 2 122 ? 24.641  99.364  40.737  1.00 43.97 ? 122  ASP B CA  1 
ATOM   4601 C  C   . ASP B 2 122 ? 24.972  100.852 40.835  1.00 43.50 ? 122  ASP B C   1 
ATOM   4602 O  O   . ASP B 2 122 ? 24.512  101.502 41.787  1.00 39.38 ? 122  ASP B O   1 
ATOM   4603 C  CB  . ASP B 2 122 ? 23.407  99.161  39.861  1.00 47.04 ? 122  ASP B CB  1 
ATOM   4604 C  CG  . ASP B 2 122 ? 23.203  97.713  39.453  1.00 51.58 ? 122  ASP B CG  1 
ATOM   4605 O  OD1 . ASP B 2 122 ? 23.969  97.245  38.577  1.00 55.05 ? 122  ASP B OD1 1 
ATOM   4606 O  OD2 . ASP B 2 122 ? 22.298  97.061  40.030  1.00 50.56 ? 122  ASP B OD2 1 
ATOM   4607 N  N   . ALA B 2 123 ? 25.726  101.361 39.861  1.00 44.63 ? 123  ALA B N   1 
ATOM   4608 C  CA  . ALA B 2 123 ? 25.945  102.810 39.647  1.00 45.63 ? 123  ALA B CA  1 
ATOM   4609 C  C   . ALA B 2 123 ? 24.671  103.403 39.043  1.00 44.93 ? 123  ALA B C   1 
ATOM   4610 O  O   . ALA B 2 123 ? 23.819  102.625 38.559  1.00 43.16 ? 123  ALA B O   1 
ATOM   4611 C  CB  . ALA B 2 123 ? 27.141  103.042 38.753  1.00 46.44 ? 123  ALA B CB  1 
ATOM   4612 N  N   . GLN B 2 124 ? 24.545  104.729 39.076  1.00 44.87 ? 124  GLN B N   1 
ATOM   4613 C  CA  . GLN B 2 124 ? 23.475  105.460 38.351  1.00 47.98 ? 124  GLN B CA  1 
ATOM   4614 C  C   . GLN B 2 124 ? 23.582  105.124 36.864  1.00 44.08 ? 124  GLN B C   1 
ATOM   4615 O  O   . GLN B 2 124 ? 24.673  105.160 36.295  1.00 42.43 ? 124  GLN B O   1 
ATOM   4616 C  CB  . GLN B 2 124 ? 23.588  106.965 38.601  1.00 51.55 ? 124  GLN B CB  1 
ATOM   4617 C  CG  . GLN B 2 124 ? 23.139  107.378 39.995  1.00 55.16 ? 124  GLN B CG  1 
ATOM   4618 C  CD  . GLN B 2 124 ? 21.636  107.363 40.138  1.00 58.24 ? 124  GLN B CD  1 
ATOM   4619 O  OE1 . GLN B 2 124 ? 20.971  106.378 39.823  1.00 63.10 ? 124  GLN B OE1 1 
ATOM   4620 N  NE2 . GLN B 2 124 ? 21.083  108.464 40.624  1.00 58.18 ? 124  GLN B NE2 1 
ATOM   4621 N  N   . PRO B 2 125 ? 22.469  104.755 36.190  1.00 41.30 ? 125  PRO B N   1 
ATOM   4622 C  CA  . PRO B 2 125 ? 22.503  104.500 34.746  1.00 40.70 ? 125  PRO B CA  1 
ATOM   4623 C  C   . PRO B 2 125 ? 23.127  105.638 33.923  1.00 39.37 ? 125  PRO B C   1 
ATOM   4624 O  O   . PRO B 2 125 ? 23.887  105.357 33.015  1.00 37.71 ? 125  PRO B O   1 
ATOM   4625 C  CB  . PRO B 2 125 ? 21.021  104.335 34.386  1.00 39.77 ? 125  PRO B CB  1 
ATOM   4626 C  CG  . PRO B 2 125 ? 20.392  103.806 35.660  1.00 39.29 ? 125  PRO B CG  1 
ATOM   4627 C  CD  . PRO B 2 125 ? 21.144  104.496 36.780  1.00 39.23 ? 125  PRO B CD  1 
ATOM   4628 N  N   . LEU B 2 126 ? 22.810  106.888 34.265  1.00 39.51 ? 126  LEU B N   1 
ATOM   4629 C  CA  . LEU B 2 126 ? 23.252  108.086 33.500  1.00 41.25 ? 126  LEU B CA  1 
ATOM   4630 C  C   . LEU B 2 126 ? 24.788  108.144 33.473  1.00 40.15 ? 126  LEU B C   1 
ATOM   4631 O  O   . LEU B 2 126 ? 25.337  108.467 32.398  1.00 39.16 ? 126  LEU B O   1 
ATOM   4632 C  CB  . LEU B 2 126 ? 22.641  109.343 34.123  1.00 43.98 ? 126  LEU B CB  1 
ATOM   4633 C  CG  . LEU B 2 126 ? 22.491  110.539 33.182  1.00 49.39 ? 126  LEU B CG  1 
ATOM   4634 C  CD1 . LEU B 2 126 ? 21.198  111.292 33.474  1.00 52.07 ? 126  LEU B CD1 1 
ATOM   4635 C  CD2 . LEU B 2 126 ? 23.692  111.468 33.275  1.00 50.53 ? 126  LEU B CD2 1 
ATOM   4636 N  N   . GLY B 2 127 ? 25.452  107.807 34.586  1.00 35.76 ? 127  GLY B N   1 
ATOM   4637 C  CA  . GLY B 2 127 ? 26.925  107.767 34.682  1.00 35.33 ? 127  GLY B CA  1 
ATOM   4638 C  C   . GLY B 2 127 ? 27.523  106.694 33.780  1.00 35.49 ? 127  GLY B C   1 
ATOM   4639 O  O   . GLY B 2 127 ? 28.408  107.024 32.981  1.00 34.07 ? 127  GLY B O   1 
ATOM   4640 N  N   . THR B 2 128 ? 27.056  105.447 33.907  1.00 34.09 ? 128  THR B N   1 
ATOM   4641 C  CA  . THR B 2 128 ? 27.412  104.313 33.006  1.00 32.86 ? 128  THR B CA  1 
ATOM   4642 C  C   . THR B 2 128 ? 27.218  104.718 31.535  1.00 33.18 ? 128  THR B C   1 
ATOM   4643 O  O   . THR B 2 128 ? 28.159  104.514 30.751  1.00 33.27 ? 128  THR B O   1 
ATOM   4644 C  CB  . THR B 2 128 ? 26.580  103.075 33.351  1.00 34.57 ? 128  THR B CB  1 
ATOM   4645 O  OG1 . THR B 2 128 ? 26.711  102.874 34.758  1.00 40.63 ? 128  THR B OG1 1 
ATOM   4646 C  CG2 . THR B 2 128 ? 26.994  101.831 32.600  1.00 32.50 ? 128  THR B CG2 1 
ATOM   4647 N  N   . ALA B 2 129 ? 26.049  105.264 31.174  1.00 31.66 ? 129  ALA B N   1 
ATOM   4648 C  CA  . ALA B 2 129 ? 25.696  105.640 29.783  1.00 33.17 ? 129  ALA B CA  1 
ATOM   4649 C  C   . ALA B 2 129 ? 26.678  106.700 29.267  1.00 33.29 ? 129  ALA B C   1 
ATOM   4650 O  O   . ALA B 2 129 ? 27.174  106.531 28.134  1.00 32.75 ? 129  ALA B O   1 
ATOM   4651 C  CB  . ALA B 2 129 ? 24.265  106.114 29.691  1.00 32.51 ? 129  ALA B CB  1 
ATOM   4652 N  N   . ARG B 2 130 ? 26.960  107.729 30.077  1.00 32.30 ? 130  ARG B N   1 
ATOM   4653 C  CA  . ARG B 2 130 ? 27.822  108.883 29.698  1.00 33.54 ? 130  ARG B CA  1 
ATOM   4654 C  C   . ARG B 2 130 ? 29.234  108.386 29.339  1.00 33.28 ? 130  ARG B C   1 
ATOM   4655 O  O   . ARG B 2 130 ? 29.795  108.882 28.344  1.00 33.19 ? 130  ARG B O   1 
ATOM   4656 C  CB  . ARG B 2 130 ? 27.857  109.928 30.819  1.00 31.39 ? 130  ARG B CB  1 
ATOM   4657 N  N   . LYS B 2 131 ? 29.790  107.458 30.121  1.00 32.38 ? 131  LYS B N   1 
ATOM   4658 C  CA  . LYS B 2 131 ? 31.153  106.897 29.897  1.00 33.92 ? 131  LYS B CA  1 
ATOM   4659 C  C   . LYS B 2 131 ? 31.189  106.208 28.526  1.00 33.34 ? 131  LYS B C   1 
ATOM   4660 O  O   . LYS B 2 131 ? 32.115  106.515 27.753  1.00 35.68 ? 131  LYS B O   1 
ATOM   4661 C  CB  . LYS B 2 131 ? 31.552  105.942 31.029  1.00 32.95 ? 131  LYS B CB  1 
ATOM   4662 N  N   . MET B 2 132 ? 30.198  105.356 28.225  1.00 31.12 ? 132  MET B N   1 
ATOM   4663 C  CA  . MET B 2 132 ? 30.067  104.638 26.921  1.00 31.90 ? 132  MET B CA  1 
ATOM   4664 C  C   . MET B 2 132 ? 29.925  105.651 25.781  1.00 31.04 ? 132  MET B C   1 
ATOM   4665 O  O   . MET B 2 132 ? 30.686  105.568 24.796  1.00 30.00 ? 132  MET B O   1 
ATOM   4666 C  CB  . MET B 2 132 ? 28.836  103.729 26.898  1.00 32.76 ? 132  MET B CB  1 
ATOM   4667 C  CG  . MET B 2 132 ? 28.878  102.632 27.930  1.00 33.73 ? 132  MET B CG  1 
ATOM   4668 S  SD  . MET B 2 132 ? 27.416  101.578 27.862  1.00 35.40 ? 132  MET B SD  1 
ATOM   4669 C  CE  . MET B 2 132 ? 27.798  100.593 26.414  1.00 33.63 ? 132  MET B CE  1 
ATOM   4670 N  N   . VAL B 2 133 ? 28.970  106.566 25.924  1.00 30.02 ? 133  VAL B N   1 
ATOM   4671 C  CA  . VAL B 2 133 ? 28.648  107.620 24.920  1.00 31.34 ? 133  VAL B CA  1 
ATOM   4672 C  C   . VAL B 2 133 ? 29.903  108.458 24.640  1.00 30.94 ? 133  VAL B C   1 
ATOM   4673 O  O   . VAL B 2 133 ? 30.191  108.695 23.459  1.00 31.54 ? 133  VAL B O   1 
ATOM   4674 C  CB  . VAL B 2 133 ? 27.454  108.468 25.389  1.00 32.07 ? 133  VAL B CB  1 
ATOM   4675 C  CG1 . VAL B 2 133 ? 27.328  109.769 24.606  1.00 33.26 ? 133  VAL B CG1 1 
ATOM   4676 C  CG2 . VAL B 2 133 ? 26.164  107.658 25.331  1.00 31.03 ? 133  VAL B CG2 1 
ATOM   4677 N  N   . ASP B 2 134 ? 30.646  108.855 25.673  1.00 32.31 ? 134  ASP B N   1 
ATOM   4678 C  CA  . ASP B 2 134 ? 31.895  109.653 25.529  1.00 33.50 ? 134  ASP B CA  1 
ATOM   4679 C  C   . ASP B 2 134 ? 32.913  108.912 24.645  1.00 32.61 ? 134  ASP B C   1 
ATOM   4680 O  O   . ASP B 2 134 ? 33.768  109.590 24.061  1.00 31.52 ? 134  ASP B O   1 
ATOM   4681 C  CB  . ASP B 2 134 ? 32.530  109.980 26.885  1.00 35.71 ? 134  ASP B CB  1 
ATOM   4682 C  CG  . ASP B 2 134 ? 31.821  111.085 27.651  1.00 38.91 ? 134  ASP B CG  1 
ATOM   4683 O  OD1 . ASP B 2 134 ? 31.067  111.859 27.019  1.00 38.75 ? 134  ASP B OD1 1 
ATOM   4684 O  OD2 . ASP B 2 134 ? 32.025  111.156 28.880  1.00 44.47 ? 134  ASP B OD2 1 
ATOM   4685 N  N   . ARG B 2 135 ? 32.837  107.580 24.556  1.00 30.97 ? 135  ARG B N   1 
ATOM   4686 C  CA  . ARG B 2 135 ? 33.853  106.760 23.837  1.00 30.14 ? 135  ARG B CA  1 
ATOM   4687 C  C   . ARG B 2 135 ? 33.445  106.509 22.374  1.00 28.83 ? 135  ARG B C   1 
ATOM   4688 O  O   . ARG B 2 135 ? 34.278  105.963 21.647  1.00 26.38 ? 135  ARG B O   1 
ATOM   4689 C  CB  . ARG B 2 135 ? 34.118  105.482 24.629  1.00 31.10 ? 135  ARG B CB  1 
ATOM   4690 C  CG  . ARG B 2 135 ? 34.852  105.758 25.936  1.00 31.77 ? 135  ARG B CG  1 
ATOM   4691 C  CD  . ARG B 2 135 ? 35.162  104.496 26.711  1.00 32.46 ? 135  ARG B CD  1 
ATOM   4692 N  NE  . ARG B 2 135 ? 36.101  103.658 25.988  1.00 31.87 ? 135  ARG B NE  1 
ATOM   4693 C  CZ  . ARG B 2 135 ? 36.506  102.458 26.388  1.00 34.81 ? 135  ARG B CZ  1 
ATOM   4694 N  NH1 . ARG B 2 135 ? 36.045  101.935 27.515  1.00 36.11 ? 135  ARG B NH1 1 
ATOM   4695 N  NH2 . ARG B 2 135 ? 37.377  101.785 25.660  1.00 33.99 ? 135  ARG B NH2 1 
ATOM   4696 N  N   . ILE B 2 136 ? 32.242  106.917 21.949  1.00 29.28 ? 136  ILE B N   1 
ATOM   4697 C  CA  . ILE B 2 136 ? 31.798  106.842 20.520  1.00 30.90 ? 136  ILE B CA  1 
ATOM   4698 C  C   . ILE B 2 136 ? 31.482  108.235 19.953  1.00 32.57 ? 136  ILE B C   1 
ATOM   4699 O  O   . ILE B 2 136 ? 31.371  108.326 18.719  1.00 32.17 ? 136  ILE B O   1 
ATOM   4700 C  CB  . ILE B 2 136 ? 30.583  105.908 20.327  1.00 30.25 ? 136  ILE B CB  1 
ATOM   4701 C  CG1 . ILE B 2 136 ? 29.389  106.328 21.183  1.00 30.32 ? 136  ILE B CG1 1 
ATOM   4702 C  CG2 . ILE B 2 136 ? 30.960  104.457 20.557  1.00 30.14 ? 136  ILE B CG2 1 
ATOM   4703 C  CD1 . ILE B 2 136 ? 28.056  105.997 20.560  1.00 30.11 ? 136  ILE B CD1 1 
ATOM   4704 N  N   . ARG B 2 137 ? 31.301  109.272 20.784  1.00 35.98 ? 137  ARG B N   1 
ATOM   4705 C  CA  . ARG B 2 137 ? 30.828  110.609 20.304  1.00 39.48 ? 137  ARG B CA  1 
ATOM   4706 C  C   . ARG B 2 137 ? 31.860  111.262 19.359  1.00 37.25 ? 137  ARG B C   1 
ATOM   4707 O  O   . ARG B 2 137 ? 31.436  112.090 18.553  1.00 37.41 ? 137  ARG B O   1 
ATOM   4708 C  CB  . ARG B 2 137 ? 30.426  111.523 21.472  1.00 42.25 ? 137  ARG B CB  1 
ATOM   4709 C  CG  . ARG B 2 137 ? 31.553  111.925 22.412  1.00 45.58 ? 137  ARG B CG  1 
ATOM   4710 C  CD  . ARG B 2 137 ? 31.217  113.115 23.304  1.00 49.85 ? 137  ARG B CD  1 
ATOM   4711 N  NE  . ARG B 2 137 ? 30.047  112.938 24.161  1.00 52.86 ? 137  ARG B NE  1 
ATOM   4712 C  CZ  . ARG B 2 137 ? 28.858  113.521 23.987  1.00 56.29 ? 137  ARG B CZ  1 
ATOM   4713 N  NH1 . ARG B 2 137 ? 28.639  114.336 22.966  1.00 59.85 ? 137  ARG B NH1 1 
ATOM   4714 N  NH2 . ARG B 2 137 ? 27.880  113.285 24.846  1.00 56.24 ? 137  ARG B NH2 1 
ATOM   4715 N  N   . GLU B 2 138 ? 33.143  110.884 19.417  1.00 38.90 ? 138  GLU B N   1 
ATOM   4716 C  CA  . GLU B 2 138 ? 34.234  111.462 18.576  1.00 40.70 ? 138  GLU B CA  1 
ATOM   4717 C  C   . GLU B 2 138 ? 34.399  110.685 17.257  1.00 39.68 ? 138  GLU B C   1 
ATOM   4718 O  O   . GLU B 2 138 ? 35.218  111.126 16.417  1.00 39.03 ? 138  GLU B O   1 
ATOM   4719 C  CB  . GLU B 2 138 ? 35.565  111.473 19.335  1.00 44.87 ? 138  GLU B CB  1 
ATOM   4720 C  CG  . GLU B 2 138 ? 35.578  112.416 20.530  1.00 49.79 ? 138  GLU B CG  1 
ATOM   4721 C  CD  . GLU B 2 138 ? 36.834  112.382 21.395  1.00 53.23 ? 138  GLU B CD  1 
ATOM   4722 O  OE1 . GLU B 2 138 ? 37.720  111.527 21.153  1.00 52.21 ? 138  GLU B OE1 1 
ATOM   4723 O  OE2 . GLU B 2 138 ? 36.921  113.216 22.320  1.00 58.43 ? 138  GLU B OE2 1 
ATOM   4724 N  N   . ALA B 2 139 ? 33.688  109.567 17.079  1.00 35.44 ? 139  ALA B N   1 
ATOM   4725 C  CA  . ALA B 2 139 ? 33.655  108.801 15.811  1.00 35.32 ? 139  ALA B CA  1 
ATOM   4726 C  C   . ALA B 2 139 ? 33.205  109.738 14.678  1.00 33.15 ? 139  ALA B C   1 
ATOM   4727 O  O   . ALA B 2 139 ? 32.113  110.329 14.791  1.00 32.67 ? 139  ALA B O   1 
ATOM   4728 C  CB  . ALA B 2 139 ? 32.751  107.602 15.948  1.00 34.43 ? 139  ALA B CB  1 
ATOM   4729 N  N   . ASP B 2 140 ? 34.028  109.899 13.638  1.00 34.64 ? 140  ASP B N   1 
ATOM   4730 C  CA  . ASP B 2 140 ? 33.781  110.880 12.545  1.00 36.27 ? 140  ASP B CA  1 
ATOM   4731 C  C   . ASP B 2 140 ? 33.470  110.152 11.230  1.00 34.03 ? 140  ASP B C   1 
ATOM   4732 O  O   . ASP B 2 140 ? 33.403  110.831 10.192  1.00 33.10 ? 140  ASP B O   1 
ATOM   4733 C  CB  . ASP B 2 140 ? 34.960  111.845 12.402  1.00 41.82 ? 140  ASP B CB  1 
ATOM   4734 C  CG  . ASP B 2 140 ? 36.242  111.183 11.941  1.00 44.74 ? 140  ASP B CG  1 
ATOM   4735 O  OD1 . ASP B 2 140 ? 36.216  109.957 11.716  1.00 51.46 ? 140  ASP B OD1 1 
ATOM   4736 O  OD2 . ASP B 2 140 ? 37.260  111.898 11.819  1.00 55.90 ? 140  ASP B OD2 1 
ATOM   4737 N  N   . SER B 2 141 ? 33.281  108.829 11.269  1.00 31.70 ? 141  SER B N   1 
ATOM   4738 C  CA  . SER B 2 141 ? 32.770  108.037 10.114  1.00 29.89 ? 141  SER B CA  1 
ATOM   4739 C  C   . SER B 2 141 ? 31.865  106.909 10.611  1.00 29.03 ? 141  SER B C   1 
ATOM   4740 O  O   . SER B 2 141 ? 32.040  106.449 11.758  1.00 27.46 ? 141  SER B O   1 
ATOM   4741 C  CB  . SER B 2 141 ? 33.886  107.505 9.244   1.00 29.96 ? 141  SER B CB  1 
ATOM   4742 O  OG  . SER B 2 141 ? 34.606  106.473 9.905   1.00 30.67 ? 141  SER B OG  1 
ATOM   4743 N  N   . VAL B 2 142 ? 30.940  106.458 9.766   1.00 27.59 ? 142  VAL B N   1 
ATOM   4744 C  CA  . VAL B 2 142 ? 30.046  105.314 10.098  1.00 29.21 ? 142  VAL B CA  1 
ATOM   4745 C  C   . VAL B 2 142 ? 30.928  104.097 10.417  1.00 27.94 ? 142  VAL B C   1 
ATOM   4746 O  O   . VAL B 2 142 ? 30.645  103.394 11.402  1.00 27.96 ? 142  VAL B O   1 
ATOM   4747 C  CB  . VAL B 2 142 ? 29.051  105.031 8.959   1.00 29.94 ? 142  VAL B CB  1 
ATOM   4748 C  CG1 . VAL B 2 142 ? 28.203  103.806 9.258   1.00 30.79 ? 142  VAL B CG1 1 
ATOM   4749 C  CG2 . VAL B 2 142 ? 28.170  106.237 8.668   1.00 30.26 ? 142  VAL B CG2 1 
ATOM   4750 N  N   . GLU B 2 143 ? 31.984  103.885 9.630   1.00 28.99 ? 143  GLU B N   1 
ATOM   4751 C  CA  . GLU B 2 143 ? 32.916  102.734 9.760   1.00 31.04 ? 143  GLU B CA  1 
ATOM   4752 C  C   . GLU B 2 143 ? 33.553  102.743 11.156  1.00 27.82 ? 143  GLU B C   1 
ATOM   4753 O  O   . GLU B 2 143 ? 33.584  101.679 11.804  1.00 27.36 ? 143  GLU B O   1 
ATOM   4754 C  CB  . GLU B 2 143 ? 33.971  102.785 8.650   1.00 35.60 ? 143  GLU B CB  1 
ATOM   4755 C  CG  . GLU B 2 143 ? 33.392  102.567 7.255   1.00 39.95 ? 143  GLU B CG  1 
ATOM   4756 C  CD  . GLU B 2 143 ? 32.868  103.794 6.516   1.00 44.11 ? 143  GLU B CD  1 
ATOM   4757 O  OE1 . GLU B 2 143 ? 32.685  104.862 7.145   1.00 42.37 ? 143  GLU B OE1 1 
ATOM   4758 O  OE2 . GLU B 2 143 ? 32.650  103.678 5.292   1.00 51.52 ? 143  GLU B OE2 1 
ATOM   4759 N  N   . SER B 2 144 ? 34.056  103.894 11.601  1.00 26.58 ? 144  SER B N   1 
ATOM   4760 C  CA  . SER B 2 144 ? 34.724  104.047 12.922  1.00 25.97 ? 144  SER B CA  1 
ATOM   4761 C  C   . SER B 2 144 ? 33.714  103.811 14.059  1.00 25.04 ? 144  SER B C   1 
ATOM   4762 O  O   . SER B 2 144 ? 34.084  103.204 15.087  1.00 24.59 ? 144  SER B O   1 
ATOM   4763 C  CB  . SER B 2 144 ? 35.378  105.401 13.033  1.00 26.97 ? 144  SER B CB  1 
ATOM   4764 O  OG  . SER B 2 144 ? 36.159  105.490 14.215  1.00 28.79 ? 144  SER B OG  1 
ATOM   4765 N  N   . LEU B 2 145 ? 32.476  104.272 13.893  1.00 23.94 ? 145  LEU B N   1 
ATOM   4766 C  CA  . LEU B 2 145 ? 31.414  104.106 14.919  1.00 25.00 ? 145  LEU B CA  1 
ATOM   4767 C  C   . LEU B 2 145 ? 31.065  102.621 15.080  1.00 25.02 ? 145  LEU B C   1 
ATOM   4768 O  O   . LEU B 2 145 ? 31.010  102.124 16.236  1.00 22.92 ? 145  LEU B O   1 
ATOM   4769 C  CB  . LEU B 2 145 ? 30.185  104.913 14.497  1.00 24.80 ? 145  LEU B CB  1 
ATOM   4770 C  CG  . LEU B 2 145 ? 28.948  104.700 15.359  1.00 24.60 ? 145  LEU B CG  1 
ATOM   4771 C  CD1 . LEU B 2 145 ? 29.255  104.980 16.825  1.00 24.96 ? 145  LEU B CD1 1 
ATOM   4772 C  CD2 . LEU B 2 145 ? 27.796  105.569 14.865  1.00 24.68 ? 145  LEU B CD2 1 
ATOM   4773 N  N   . ILE B 2 146 ? 30.815  101.956 13.957  1.00 26.63 ? 146  ILE B N   1 
ATOM   4774 C  CA  A ILE B 2 146 ? 30.356  100.536 13.930  0.50 28.11 ? 146  ILE B CA  1 
ATOM   4775 C  CA  B ILE B 2 146 ? 30.377  100.528 13.873  0.50 28.54 ? 146  ILE B CA  1 
ATOM   4776 C  C   . ILE B 2 146 ? 31.500  99.635  14.418  1.00 29.28 ? 146  ILE B C   1 
ATOM   4777 O  O   . ILE B 2 146 ? 31.219  98.728  15.216  1.00 28.39 ? 146  ILE B O   1 
ATOM   4778 C  CB  A ILE B 2 146 ? 29.823  100.187 12.527  0.50 29.63 ? 146  ILE B CB  1 
ATOM   4779 C  CB  B ILE B 2 146 ? 30.002  100.195 12.412  0.50 30.69 ? 146  ILE B CB  1 
ATOM   4780 C  CG1 A ILE B 2 146 ? 28.464  100.852 12.292  0.50 29.14 ? 146  ILE B CG1 1 
ATOM   4781 C  CG1 B ILE B 2 146 ? 28.726  100.925 11.984  0.50 31.04 ? 146  ILE B CG1 1 
ATOM   4782 C  CG2 A ILE B 2 146 ? 29.749  98.690  12.291  0.50 30.63 ? 146  ILE B CG2 1 
ATOM   4783 C  CG2 B ILE B 2 146 ? 29.881  98.701  12.174  0.50 31.64 ? 146  ILE B CG2 1 
ATOM   4784 C  CD1 A ILE B 2 146 ? 28.024  100.831 10.854  0.50 29.27 ? 146  ILE B CD1 1 
ATOM   4785 C  CD1 B ILE B 2 146 ? 27.556  100.683 12.894  0.50 31.31 ? 146  ILE B CD1 1 
ATOM   4786 N  N   . SER B 2 147 ? 32.736  99.918  14.001  1.00 29.99 ? 147  SER B N   1 
ATOM   4787 C  CA  . SER B 2 147 ? 33.953  99.167  14.409  1.00 30.34 ? 147  SER B CA  1 
ATOM   4788 C  C   . SER B 2 147 ? 34.129  99.219  15.933  1.00 27.97 ? 147  SER B C   1 
ATOM   4789 O  O   . SER B 2 147 ? 34.255  98.156  16.573  1.00 26.42 ? 147  SER B O   1 
ATOM   4790 C  CB  . SER B 2 147 ? 35.168  99.712  13.696  1.00 31.69 ? 147  SER B CB  1 
ATOM   4791 O  OG  . SER B 2 147 ? 36.356  99.175  14.247  1.00 38.46 ? 147  SER B OG  1 
ATOM   4792 N  N   . ARG B 2 148 ? 34.162  100.421 16.502  1.00 26.68 ? 148  ARG B N   1 
ATOM   4793 C  CA  . ARG B 2 148 ? 34.515  100.614 17.933  1.00 26.76 ? 148  ARG B CA  1 
ATOM   4794 C  C   . ARG B 2 148 ? 33.358  100.186 18.841  1.00 25.75 ? 148  ARG B C   1 
ATOM   4795 O  O   . ARG B 2 148 ? 33.631  99.869  20.014  1.00 26.76 ? 148  ARG B O   1 
ATOM   4796 C  CB  . ARG B 2 148 ? 34.919  102.063 18.198  1.00 29.87 ? 148  ARG B CB  1 
ATOM   4797 C  CG  . ARG B 2 148 ? 33.764  103.046 18.215  1.00 31.81 ? 148  ARG B CG  1 
ATOM   4798 C  CD  . ARG B 2 148 ? 34.248  104.425 18.613  1.00 33.19 ? 148  ARG B CD  1 
ATOM   4799 N  NE  . ARG B 2 148 ? 35.083  105.055 17.612  1.00 33.60 ? 148  ARG B NE  1 
ATOM   4800 C  CZ  . ARG B 2 148 ? 35.845  106.124 17.831  1.00 36.60 ? 148  ARG B CZ  1 
ATOM   4801 N  NH1 . ARG B 2 148 ? 36.582  106.619 16.853  1.00 37.34 ? 148  ARG B NH1 1 
ATOM   4802 N  NH2 . ARG B 2 148 ? 35.880  106.692 19.028  1.00 38.75 ? 148  ARG B NH2 1 
ATOM   4803 N  N   . THR B 2 149 ? 32.117  100.143 18.342  1.00 24.37 ? 149  THR B N   1 
ATOM   4804 C  CA  . THR B 2 149 ? 30.920  99.973  19.221  1.00 23.44 ? 149  THR B CA  1 
ATOM   4805 C  C   . THR B 2 149 ? 30.901  98.544  19.792  1.00 23.09 ? 149  THR B C   1 
ATOM   4806 O  O   . THR B 2 149 ? 30.653  98.408  21.002  1.00 25.04 ? 149  THR B O   1 
ATOM   4807 C  CB  . THR B 2 149 ? 29.617  100.364 18.510  1.00 22.99 ? 149  THR B CB  1 
ATOM   4808 O  OG1 . THR B 2 149 ? 29.617  101.788 18.383  1.00 22.44 ? 149  THR B OG1 1 
ATOM   4809 C  CG2 . THR B 2 149 ? 28.376  99.926  19.262  1.00 23.43 ? 149  THR B CG2 1 
ATOM   4810 N  N   . THR B 2 150 ? 31.163  97.513  18.980  1.00 22.61 ? 150  THR B N   1 
ATOM   4811 C  CA  . THR B 2 150 ? 31.194  96.101  19.461  1.00 22.07 ? 150  THR B CA  1 
ATOM   4812 C  C   . THR B 2 150 ? 32.309  95.927  20.516  1.00 22.84 ? 150  THR B C   1 
ATOM   4813 O  O   . THR B 2 150 ? 32.049  95.265  21.536  1.00 21.57 ? 150  THR B O   1 
ATOM   4814 C  CB  . THR B 2 150 ? 31.273  95.110  18.294  1.00 21.71 ? 150  THR B CB  1 
ATOM   4815 O  OG1 . THR B 2 150 ? 32.432  95.396  17.519  1.00 21.31 ? 150  THR B OG1 1 
ATOM   4816 C  CG2 . THR B 2 150 ? 30.034  95.141  17.424  1.00 21.45 ? 150  THR B CG2 1 
ATOM   4817 N  N   . ARG B 2 151 ? 33.499  96.503  20.310  1.00 24.75 ? 151  ARG B N   1 
ATOM   4818 C  CA  . ARG B 2 151 ? 34.618  96.420  21.298  1.00 26.92 ? 151  ARG B CA  1 
ATOM   4819 C  C   . ARG B 2 151 ? 34.209  97.104  22.612  1.00 26.19 ? 151  ARG B C   1 
ATOM   4820 O  O   . ARG B 2 151 ? 34.422  96.510  23.689  1.00 25.14 ? 151  ARG B O   1 
ATOM   4821 C  CB  . ARG B 2 151 ? 35.906  97.049  20.757  1.00 28.64 ? 151  ARG B CB  1 
ATOM   4822 C  CG  . ARG B 2 151 ? 36.619  96.202  19.710  1.00 33.63 ? 151  ARG B CG  1 
ATOM   4823 C  CD  . ARG B 2 151 ? 38.039  96.651  19.374  1.00 35.99 ? 151  ARG B CD  1 
ATOM   4824 N  NE  . ARG B 2 151 ? 38.158  98.101  19.401  1.00 36.28 ? 151  ARG B NE  1 
ATOM   4825 C  CZ  . ARG B 2 151 ? 38.087  98.908  18.351  1.00 36.02 ? 151  ARG B CZ  1 
ATOM   4826 N  NH1 . ARG B 2 151 ? 37.939  98.429  17.120  1.00 34.46 ? 151  ARG B NH1 1 
ATOM   4827 N  NH2 . ARG B 2 151 ? 38.182  100.212 18.554  1.00 33.65 ? 151  ARG B NH2 1 
ATOM   4828 N  N   . LEU B 2 152 ? 33.640  98.309  22.525  1.00 25.27 ? 152  LEU B N   1 
ATOM   4829 C  CA  . LEU B 2 152 ? 33.216  99.110  23.704  1.00 25.59 ? 152  LEU B CA  1 
ATOM   4830 C  C   . LEU B 2 152 ? 32.091  98.393  24.469  1.00 24.88 ? 152  LEU B C   1 
ATOM   4831 O  O   . LEU B 2 152 ? 32.169  98.320  25.719  1.00 24.13 ? 152  LEU B O   1 
ATOM   4832 C  CB  . LEU B 2 152 ? 32.753  100.491 23.236  1.00 26.53 ? 152  LEU B CB  1 
ATOM   4833 C  CG  . LEU B 2 152 ? 32.163  101.369 24.332  1.00 27.79 ? 152  LEU B CG  1 
ATOM   4834 C  CD1 . LEU B 2 152 ? 33.192  101.608 25.419  1.00 28.22 ? 152  LEU B CD1 1 
ATOM   4835 C  CD2 . LEU B 2 152 ? 31.652  102.680 23.766  1.00 29.58 ? 152  LEU B CD2 1 
ATOM   4836 N  N   . VAL B 2 153 ? 31.068  97.914  23.761  1.00 24.82 ? 153  VAL B N   1 
ATOM   4837 C  CA  . VAL B 2 153 ? 29.882  97.251  24.381  1.00 24.51 ? 153  VAL B CA  1 
ATOM   4838 C  C   . VAL B 2 153 ? 30.335  95.964  25.070  1.00 24.47 ? 153  VAL B C   1 
ATOM   4839 O  O   . VAL B 2 153 ? 29.977  95.744  26.226  1.00 24.92 ? 153  VAL B O   1 
ATOM   4840 C  CB  . VAL B 2 153 ? 28.738  97.037  23.372  1.00 24.22 ? 153  VAL B CB  1 
ATOM   4841 C  CG1 . VAL B 2 153 ? 27.630  96.145  23.920  1.00 24.13 ? 153  VAL B CG1 1 
ATOM   4842 C  CG2 . VAL B 2 153 ? 28.156  98.363  22.921  1.00 24.14 ? 153  VAL B CG2 1 
HETATM 4843 N  N   . MLZ B 2 154 ? 31.159  95.152  24.395  1.00 24.90 ? 154  MLZ B N   1 
HETATM 4844 C  CA  . MLZ B 2 154 ? 31.654  93.913  24.987  1.00 26.20 ? 154  MLZ B CA  1 
HETATM 4845 C  CB  . MLZ B 2 154 ? 32.502  93.129  23.977  1.00 27.20 ? 154  MLZ B CB  1 
HETATM 4846 C  CG  . MLZ B 2 154 ? 33.175  91.875  24.521  1.00 28.49 ? 154  MLZ B CG  1 
HETATM 4847 C  CD  . MLZ B 2 154 ? 33.816  90.995  23.460  1.00 30.26 ? 154  MLZ B CD  1 
HETATM 4848 C  CE  . MLZ B 2 154 ? 34.541  89.775  24.011  1.00 31.16 ? 154  MLZ B CE  1 
HETATM 4849 N  NZ  . MLZ B 2 154 ? 35.737  90.125  24.780  1.00 31.00 ? 154  MLZ B NZ  1 
HETATM 4850 C  CM  . MLZ B 2 154 ? 36.812  90.814  24.055  1.00 30.75 ? 154  MLZ B CM  1 
HETATM 4851 C  C   . MLZ B 2 154 ? 32.438  94.226  26.267  1.00 26.14 ? 154  MLZ B C   1 
HETATM 4852 O  O   . MLZ B 2 154 ? 32.246  93.573  27.291  1.00 25.68 ? 154  MLZ B O   1 
ATOM   4853 N  N   . ALA B 2 155 ? 33.310  95.238  26.211  1.00 26.24 ? 155  ALA B N   1 
ATOM   4854 C  CA  . ALA B 2 155 ? 34.168  95.588  27.337  1.00 27.54 ? 155  ALA B CA  1 
ATOM   4855 C  C   . ALA B 2 155 ? 33.339  96.117  28.514  1.00 27.31 ? 155  ALA B C   1 
ATOM   4856 O  O   . ALA B 2 155 ? 33.750  95.894  29.662  1.00 27.62 ? 155  ALA B O   1 
ATOM   4857 C  CB  . ALA B 2 155 ? 35.207  96.596  26.905  1.00 28.86 ? 155  ALA B CB  1 
ATOM   4858 N  N   . THR B 2 156 ? 32.207  96.771  28.237  1.00 27.54 ? 156  THR B N   1 
ATOM   4859 C  CA  . THR B 2 156 ? 31.350  97.440  29.256  1.00 27.42 ? 156  THR B CA  1 
ATOM   4860 C  C   . THR B 2 156 ? 30.372  96.429  29.872  1.00 28.12 ? 156  THR B C   1 
ATOM   4861 O  O   . THR B 2 156 ? 30.190  96.452  31.108  1.00 27.51 ? 156  THR B O   1 
ATOM   4862 C  CB  . THR B 2 156 ? 30.609  98.636  28.642  1.00 28.01 ? 156  THR B CB  1 
ATOM   4863 O  OG1 . THR B 2 156 ? 31.556  99.596  28.170  1.00 27.04 ? 156  THR B OG1 1 
ATOM   4864 C  CG2 . THR B 2 156 ? 29.681  99.312  29.625  1.00 28.49 ? 156  THR B CG2 1 
ATOM   4865 N  N   . LEU B 2 157 ? 29.768  95.568  29.052  1.00 27.76 ? 157  LEU B N   1 
ATOM   4866 C  CA  . LEU B 2 157 ? 28.677  94.659  29.493  1.00 29.17 ? 157  LEU B CA  1 
ATOM   4867 C  C   . LEU B 2 157 ? 29.222  93.275  29.865  1.00 30.08 ? 157  LEU B C   1 
ATOM   4868 O  O   . LEU B 2 157 ? 28.540  92.582  30.630  1.00 31.37 ? 157  LEU B O   1 
ATOM   4869 C  CB  . LEU B 2 157 ? 27.626  94.565  28.385  1.00 29.57 ? 157  LEU B CB  1 
ATOM   4870 C  CG  . LEU B 2 157 ? 26.994  95.891  27.961  1.00 30.13 ? 157  LEU B CG  1 
ATOM   4871 C  CD1 . LEU B 2 157 ? 25.828  95.642  27.022  1.00 30.06 ? 157  LEU B CD1 1 
ATOM   4872 C  CD2 . LEU B 2 157 ? 26.536  96.708  29.164  1.00 31.08 ? 157  LEU B CD2 1 
ATOM   4873 N  N   . GLY B 2 158 ? 30.389  92.880  29.352  1.00 30.07 ? 158  GLY B N   1 
ATOM   4874 C  CA  . GLY B 2 158 ? 31.022  91.585  29.677  1.00 29.80 ? 158  GLY B CA  1 
ATOM   4875 C  C   . GLY B 2 158 ? 30.267  90.407  29.076  1.00 30.86 ? 158  GLY B C   1 
ATOM   4876 O  O   . GLY B 2 158 ? 29.934  89.464  29.824  1.00 33.98 ? 158  GLY B O   1 
ATOM   4877 N  N   . TYR B 2 159 ? 29.968  90.475  27.779  1.00 27.22 ? 159  TYR B N   1 
ATOM   4878 C  CA  . TYR B 2 159 ? 29.404  89.358  26.981  1.00 26.53 ? 159  TYR B CA  1 
ATOM   4879 C  C   . TYR B 2 159 ? 30.529  88.720  26.168  1.00 25.58 ? 159  TYR B C   1 
ATOM   4880 O  O   . TYR B 2 159 ? 31.516  89.418  25.870  1.00 26.18 ? 159  TYR B O   1 
ATOM   4881 C  CB  . TYR B 2 159 ? 28.249  89.839  26.101  1.00 27.62 ? 159  TYR B CB  1 
ATOM   4882 C  CG  . TYR B 2 159 ? 26.935  89.912  26.832  1.00 27.23 ? 159  TYR B CG  1 
ATOM   4883 C  CD1 . TYR B 2 159 ? 26.706  90.889  27.787  1.00 28.38 ? 159  TYR B CD1 1 
ATOM   4884 C  CD2 . TYR B 2 159 ? 25.933  88.990  26.593  1.00 28.14 ? 159  TYR B CD2 1 
ATOM   4885 C  CE1 . TYR B 2 159 ? 25.508  90.953  28.479  1.00 29.33 ? 159  TYR B CE1 1 
ATOM   4886 C  CE2 . TYR B 2 159 ? 24.726  89.045  27.269  1.00 28.40 ? 159  TYR B CE2 1 
ATOM   4887 C  CZ  . TYR B 2 159 ? 24.511  90.032  28.213  1.00 29.08 ? 159  TYR B CZ  1 
ATOM   4888 O  OH  . TYR B 2 159 ? 23.334  90.071  28.897  1.00 29.33 ? 159  TYR B OH  1 
ATOM   4889 N  N   . ASP B 2 160 ? 30.379  87.434  25.842  1.00 23.46 ? 160  ASP B N   1 
ATOM   4890 C  CA  . ASP B 2 160 ? 31.377  86.640  25.078  1.00 23.04 ? 160  ASP B CA  1 
ATOM   4891 C  C   . ASP B 2 160 ? 31.495  87.153  23.635  1.00 24.20 ? 160  ASP B C   1 
ATOM   4892 O  O   . ASP B 2 160 ? 32.613  87.073  23.070  1.00 21.90 ? 160  ASP B O   1 
ATOM   4893 C  CB  . ASP B 2 160 ? 31.006  85.162  25.073  1.00 23.40 ? 160  ASP B CB  1 
ATOM   4894 C  CG  . ASP B 2 160 ? 31.211  84.496  26.421  1.00 24.19 ? 160  ASP B CG  1 
ATOM   4895 O  OD1 . ASP B 2 160 ? 32.144  84.903  27.143  1.00 23.87 ? 160  ASP B OD1 1 
ATOM   4896 O  OD2 . ASP B 2 160 ? 30.423  83.600  26.742  1.00 24.38 ? 160  ASP B OD2 1 
ATOM   4897 N  N   . ARG B 2 161 ? 30.392  87.626  23.046  1.00 22.48 ? 161  ARG B N   1 
ATOM   4898 C  CA  . ARG B 2 161 ? 30.398  88.167  21.658  1.00 23.15 ? 161  ARG B CA  1 
ATOM   4899 C  C   . ARG B 2 161 ? 29.415  89.336  21.560  1.00 23.46 ? 161  ARG B C   1 
ATOM   4900 O  O   . ARG B 2 161 ? 28.300  89.241  22.096  1.00 21.76 ? 161  ARG B O   1 
ATOM   4901 C  CB  . ARG B 2 161 ? 30.053  87.094  20.621  1.00 23.21 ? 161  ARG B CB  1 
ATOM   4902 C  CG  . ARG B 2 161 ? 30.216  87.548  19.174  1.00 22.96 ? 161  ARG B CG  1 
ATOM   4903 C  CD  . ARG B 2 161 ? 29.430  86.694  18.193  1.00 23.48 ? 161  ARG B CD  1 
ATOM   4904 N  NE  . ARG B 2 161 ? 29.691  85.266  18.331  1.00 24.06 ? 161  ARG B NE  1 
ATOM   4905 C  CZ  . ARG B 2 161 ? 30.682  84.599  17.739  1.00 24.28 ? 161  ARG B CZ  1 
ATOM   4906 N  NH1 . ARG B 2 161 ? 31.537  85.223  16.948  1.00 24.83 ? 161  ARG B NH1 1 
ATOM   4907 N  NH2 . ARG B 2 161 ? 30.812  83.298  17.936  1.00 24.26 ? 161  ARG B NH2 1 
ATOM   4908 N  N   . VAL B 2 162 ? 29.846  90.411  20.909  1.00 24.45 ? 162  VAL B N   1 
ATOM   4909 C  CA  . VAL B 2 162 ? 28.950  91.515  20.480  1.00 22.94 ? 162  VAL B CA  1 
ATOM   4910 C  C   . VAL B 2 162 ? 29.123  91.692  18.970  1.00 23.01 ? 162  VAL B C   1 
ATOM   4911 O  O   . VAL B 2 162 ? 30.267  91.806  18.490  1.00 21.77 ? 162  VAL B O   1 
ATOM   4912 C  CB  . VAL B 2 162 ? 29.197  92.818  21.259  1.00 23.40 ? 162  VAL B CB  1 
ATOM   4913 C  CG1 . VAL B 2 162 ? 28.174  93.886  20.887  1.00 22.94 ? 162  VAL B CG1 1 
ATOM   4914 C  CG2 . VAL B 2 162 ? 29.184  92.576  22.762  1.00 23.93 ? 162  VAL B CG2 1 
ATOM   4915 N  N   . MET B 2 163 ? 28.001  91.654  18.259  1.00 21.54 ? 163  MET B N   1 
ATOM   4916 C  CA  . MET B 2 163 ? 27.929  91.864  16.801  1.00 22.51 ? 163  MET B CA  1 
ATOM   4917 C  C   . MET B 2 163 ? 27.004  93.044  16.544  1.00 20.95 ? 163  MET B C   1 
ATOM   4918 O  O   . MET B 2 163 ? 26.153  93.342  17.396  1.00 21.95 ? 163  MET B O   1 
ATOM   4919 C  CB  . MET B 2 163 ? 27.370  90.631  16.088  1.00 22.42 ? 163  MET B CB  1 
ATOM   4920 C  CG  . MET B 2 163 ? 28.259  89.435  16.205  1.00 22.60 ? 163  MET B CG  1 
ATOM   4921 S  SD  . MET B 2 163 ? 27.626  88.076  15.209  1.00 24.14 ? 163  MET B SD  1 
ATOM   4922 C  CE  . MET B 2 163 ? 26.385  87.414  16.313  1.00 24.45 ? 163  MET B CE  1 
ATOM   4923 N  N   . ILE B 2 164 ? 27.187  93.688  15.404  1.00 21.41 ? 164  ILE B N   1 
ATOM   4924 C  CA  . ILE B 2 164 ? 26.152  94.582  14.822  1.00 21.50 ? 164  ILE B CA  1 
ATOM   4925 C  C   . ILE B 2 164 ? 25.712  93.965  13.500  1.00 21.46 ? 164  ILE B C   1 
ATOM   4926 O  O   . ILE B 2 164 ? 26.590  93.620  12.663  1.00 20.78 ? 164  ILE B O   1 
ATOM   4927 C  CB  . ILE B 2 164 ? 26.663  96.021  14.653  1.00 20.66 ? 164  ILE B CB  1 
ATOM   4928 C  CG1 . ILE B 2 164 ? 26.939  96.674  16.006  1.00 22.04 ? 164  ILE B CG1 1 
ATOM   4929 C  CG2 . ILE B 2 164 ? 25.681  96.819  13.822  1.00 20.74 ? 164  ILE B CG2 1 
ATOM   4930 C  CD1 . ILE B 2 164 ? 27.708  97.971  15.928  1.00 22.57 ? 164  ILE B CD1 1 
ATOM   4931 N  N   . TYR B 2 165 ? 24.401  93.842  13.331  1.00 21.89 ? 165  TYR B N   1 
ATOM   4932 C  CA  . TYR B 2 165 ? 23.764  93.496  12.042  1.00 22.69 ? 165  TYR B CA  1 
ATOM   4933 C  C   . TYR B 2 165 ? 23.281  94.790  11.393  1.00 24.69 ? 165  TYR B C   1 
ATOM   4934 O  O   . TYR B 2 165 ? 22.760  95.657  12.111  1.00 25.04 ? 165  TYR B O   1 
ATOM   4935 C  CB  . TYR B 2 165 ? 22.580  92.547  12.227  1.00 23.22 ? 165  TYR B CB  1 
ATOM   4936 C  CG  . TYR B 2 165 ? 22.785  91.425  13.207  1.00 22.59 ? 165  TYR B CG  1 
ATOM   4937 C  CD1 . TYR B 2 165 ? 23.968  90.704  13.257  1.00 22.76 ? 165  TYR B CD1 1 
ATOM   4938 C  CD2 . TYR B 2 165 ? 21.769  91.069  14.078  1.00 23.55 ? 165  TYR B CD2 1 
ATOM   4939 C  CE1 . TYR B 2 165 ? 24.138  89.665  14.161  1.00 23.12 ? 165  TYR B CE1 1 
ATOM   4940 C  CE2 . TYR B 2 165 ? 21.925  90.037  14.988  1.00 23.08 ? 165  TYR B CE2 1 
ATOM   4941 C  CZ  . TYR B 2 165 ? 23.109  89.327  15.029  1.00 23.51 ? 165  TYR B CZ  1 
ATOM   4942 O  OH  . TYR B 2 165 ? 23.230  88.298  15.923  1.00 24.33 ? 165  TYR B OH  1 
ATOM   4943 N  N   . ARG B 2 166 ? 23.466  94.910  10.080  1.00 25.58 ? 166  ARG B N   1 
ATOM   4944 C  CA  . ARG B 2 166 ? 22.754  95.918  9.257   1.00 26.92 ? 166  ARG B CA  1 
ATOM   4945 C  C   . ARG B 2 166 ? 21.732  95.178  8.398   1.00 24.49 ? 166  ARG B C   1 
ATOM   4946 O  O   . ARG B 2 166 ? 22.148  94.289  7.632   1.00 23.43 ? 166  ARG B O   1 
ATOM   4947 C  CB  . ARG B 2 166 ? 23.718  96.719  8.377   1.00 29.83 ? 166  ARG B CB  1 
ATOM   4948 C  CG  . ARG B 2 166 ? 23.045  97.863  7.634   1.00 32.92 ? 166  ARG B CG  1 
ATOM   4949 C  CD  . ARG B 2 166 ? 24.027  98.627  6.775   1.00 37.88 ? 166  ARG B CD  1 
ATOM   4950 N  NE  . ARG B 2 166 ? 23.354  99.572  5.886   1.00 45.12 ? 166  ARG B NE  1 
ATOM   4951 C  CZ  . ARG B 2 166 ? 22.731  99.259  4.745   1.00 49.36 ? 166  ARG B CZ  1 
ATOM   4952 N  NH1 . ARG B 2 166 ? 22.671  98.006  4.322   1.00 49.04 ? 166  ARG B NH1 1 
ATOM   4953 N  NH2 . ARG B 2 166 ? 22.142  100.212 4.040   1.00 50.14 ? 166  ARG B NH2 1 
ATOM   4954 N  N   . PHE B 2 167 ? 20.451  95.531  8.511   1.00 24.56 ? 167  PHE B N   1 
ATOM   4955 C  CA  . PHE B 2 167 ? 19.394  94.945  7.647   1.00 26.21 ? 167  PHE B CA  1 
ATOM   4956 C  C   . PHE B 2 167 ? 19.560  95.509  6.237   1.00 26.96 ? 167  PHE B C   1 
ATOM   4957 O  O   . PHE B 2 167 ? 19.810  96.727  6.065   1.00 27.14 ? 167  PHE B O   1 
ATOM   4958 C  CB  . PHE B 2 167 ? 17.997  95.116  8.243   1.00 26.53 ? 167  PHE B CB  1 
ATOM   4959 C  CG  . PHE B 2 167 ? 17.782  94.264  9.469   1.00 26.26 ? 167  PHE B CG  1 
ATOM   4960 C  CD1 . PHE B 2 167 ? 17.933  92.886  9.406   1.00 26.84 ? 167  PHE B CD1 1 
ATOM   4961 C  CD2 . PHE B 2 167 ? 17.487  94.844  10.694  1.00 26.53 ? 167  PHE B CD2 1 
ATOM   4962 C  CE1 . PHE B 2 167 ? 17.765  92.104  10.539  1.00 27.12 ? 167  PHE B CE1 1 
ATOM   4963 C  CE2 . PHE B 2 167 ? 17.326  94.064  11.828  1.00 26.16 ? 167  PHE B CE2 1 
ATOM   4964 C  CZ  . PHE B 2 167 ? 17.463  92.695  11.748  1.00 27.26 ? 167  PHE B CZ  1 
ATOM   4965 N  N   . GLN B 2 168 ? 19.492  94.602  5.269   1.00 29.00 ? 168  GLN B N   1 
ATOM   4966 C  CA  . GLN B 2 168 ? 19.596  94.871  3.810   1.00 30.88 ? 168  GLN B CA  1 
ATOM   4967 C  C   . GLN B 2 168 ? 18.189  95.205  3.284   1.00 31.25 ? 168  GLN B C   1 
ATOM   4968 O  O   . GLN B 2 168 ? 17.219  95.039  4.055   1.00 30.39 ? 168  GLN B O   1 
ATOM   4969 C  CB  . GLN B 2 168 ? 20.204  93.645  3.116   1.00 31.33 ? 168  GLN B CB  1 
ATOM   4970 C  CG  . GLN B 2 168 ? 21.468  93.110  3.785   1.00 31.66 ? 168  GLN B CG  1 
ATOM   4971 C  CD  . GLN B 2 168 ? 22.602  94.105  3.781   1.00 32.63 ? 168  GLN B CD  1 
ATOM   4972 O  OE1 . GLN B 2 168 ? 22.971  94.684  4.808   1.00 34.15 ? 168  GLN B OE1 1 
ATOM   4973 N  NE2 . GLN B 2 168 ? 23.166  94.314  2.609   1.00 30.47 ? 168  GLN B NE2 1 
ATOM   4974 N  N   . GLU B 2 169 ? 18.075  95.650  2.028   1.00 33.65 ? 169  GLU B N   1 
ATOM   4975 C  CA  . GLU B 2 169 ? 16.777  96.001  1.382   1.00 37.25 ? 169  GLU B CA  1 
ATOM   4976 C  C   . GLU B 2 169 ? 15.811  94.814  1.449   1.00 35.25 ? 169  GLU B C   1 
ATOM   4977 O  O   . GLU B 2 169 ? 14.634  95.048  1.711   1.00 38.19 ? 169  GLU B O   1 
ATOM   4978 C  CB  . GLU B 2 169 ? 16.973  96.418  -0.075  1.00 39.96 ? 169  GLU B CB  1 
ATOM   4979 C  CG  . GLU B 2 169 ? 17.543  97.816  -0.217  1.00 45.91 ? 169  GLU B CG  1 
ATOM   4980 C  CD  . GLU B 2 169 ? 17.452  98.406  -1.615  1.00 49.05 ? 169  GLU B CD  1 
ATOM   4981 O  OE1 . GLU B 2 169 ? 16.793  97.779  -2.476  1.00 48.59 ? 169  GLU B OE1 1 
ATOM   4982 O  OE2 . GLU B 2 169 ? 18.047  99.492  -1.839  1.00 53.97 ? 169  GLU B OE2 1 
ATOM   4983 N  N   . ASP B 2 170 ? 16.304  93.595  1.234   1.00 34.18 ? 170  ASP B N   1 
ATOM   4984 C  CA  . ASP B 2 170 ? 15.489  92.352  1.230   1.00 34.43 ? 170  ASP B CA  1 
ATOM   4985 C  C   . ASP B 2 170 ? 15.253  91.847  2.666   1.00 33.25 ? 170  ASP B C   1 
ATOM   4986 O  O   . ASP B 2 170 ? 14.671  90.762  2.800   1.00 35.92 ? 170  ASP B O   1 
ATOM   4987 C  CB  . ASP B 2 170 ? 16.142  91.284  0.346   1.00 34.98 ? 170  ASP B CB  1 
ATOM   4988 C  CG  . ASP B 2 170 ? 17.469  90.741  0.861   1.00 36.48 ? 170  ASP B CG  1 
ATOM   4989 O  OD1 . ASP B 2 170 ? 17.980  91.271  1.874   1.00 34.81 ? 170  ASP B OD1 1 
ATOM   4990 O  OD2 . ASP B 2 170 ? 17.990  89.788  0.240   1.00 38.15 ? 170  ASP B OD2 1 
ATOM   4991 N  N   . GLY B 2 171 ? 15.690  92.579  3.701   1.00 31.42 ? 171  GLY B N   1 
ATOM   4992 C  CA  . GLY B 2 171 ? 15.443  92.228  5.120   1.00 30.91 ? 171  GLY B CA  1 
ATOM   4993 C  C   . GLY B 2 171 ? 16.499  91.289  5.701   1.00 29.24 ? 171  GLY B C   1 
ATOM   4994 O  O   . GLY B 2 171 ? 16.466  91.026  6.931   1.00 28.01 ? 171  GLY B O   1 
ATOM   4995 N  N   . ALA B 2 172 ? 17.407  90.782  4.867   1.00 26.93 ? 172  ALA B N   1 
ATOM   4996 C  CA  . ALA B 2 172 ? 18.574  89.982  5.305   1.00 26.65 ? 172  ALA B CA  1 
ATOM   4997 C  C   . ALA B 2 172 ? 19.394  90.798  6.309   1.00 25.60 ? 172  ALA B C   1 
ATOM   4998 O  O   . ALA B 2 172 ? 19.400  92.038  6.197   1.00 25.09 ? 172  ALA B O   1 
ATOM   4999 C  CB  . ALA B 2 172 ? 19.413  89.597  4.112   1.00 26.88 ? 172  ALA B CB  1 
ATOM   5000 N  N   . GLY B 2 173 ? 20.069  90.132  7.247   1.00 24.00 ? 173  GLY B N   1 
ATOM   5001 C  CA  . GLY B 2 173 ? 21.054  90.786  8.127   1.00 23.74 ? 173  GLY B CA  1 
ATOM   5002 C  C   . GLY B 2 173 ? 22.474  90.515  7.650   1.00 23.60 ? 173  GLY B C   1 
ATOM   5003 O  O   . GLY B 2 173 ? 22.764  89.396  7.235   1.00 23.84 ? 173  GLY B O   1 
HETATM 5004 N  N   . MLZ B 2 174 ? 23.323  91.555  7.699   1.00 23.86 ? 174  MLZ B N   1 
HETATM 5005 C  CA  . MLZ B 2 174 ? 24.757  91.426  7.485   1.00 25.06 ? 174  MLZ B CA  1 
HETATM 5006 C  CB  . MLZ B 2 174 ? 25.219  92.356  6.358   1.00 26.71 ? 174  MLZ B CB  1 
HETATM 5007 C  CG  . MLZ B 2 174 ? 26.672  92.175  5.940   1.00 28.49 ? 174  MLZ B CG  1 
HETATM 5008 C  CD  . MLZ B 2 174 ? 27.199  93.250  5.002   1.00 30.84 ? 174  MLZ B CD  1 
HETATM 5009 C  CE  . MLZ B 2 174 ? 28.638  92.953  4.602   1.00 33.75 ? 174  MLZ B CE  1 
HETATM 5010 N  NZ  . MLZ B 2 174 ? 29.304  94.083  3.945   1.00 37.62 ? 174  MLZ B NZ  1 
HETATM 5011 C  CM  . MLZ B 2 174 ? 28.652  94.642  2.749   1.00 39.76 ? 174  MLZ B CM  1 
HETATM 5012 C  C   . MLZ B 2 174 ? 25.497  91.755  8.784   1.00 23.20 ? 174  MLZ B C   1 
HETATM 5013 O  O   . MLZ B 2 174 ? 25.227  92.778  9.406   1.00 22.28 ? 174  MLZ B O   1 
ATOM   5014 N  N   . VAL B 2 175 ? 26.447  90.893  9.172   1.00 21.63 ? 175  VAL B N   1 
ATOM   5015 C  CA  . VAL B 2 175 ? 27.279  91.138  10.343  1.00 21.94 ? 175  VAL B CA  1 
ATOM   5016 C  C   . VAL B 2 175 ? 28.376  92.133  9.946   1.00 22.45 ? 175  VAL B C   1 
ATOM   5017 O  O   . VAL B 2 175 ? 29.311  91.732  9.212   1.00 21.67 ? 175  VAL B O   1 
ATOM   5018 C  CB  . VAL B 2 175 ? 27.887  89.840  10.910  1.00 22.17 ? 175  VAL B CB  1 
ATOM   5019 C  CG1 . VAL B 2 175 ? 28.685  90.100  12.183  1.00 21.70 ? 175  VAL B CG1 1 
ATOM   5020 C  CG2 . VAL B 2 175 ? 26.832  88.766  11.152  1.00 22.06 ? 175  VAL B CG2 1 
ATOM   5021 N  N   . VAL B 2 176 ? 28.266  93.381  10.399  1.00 22.50 ? 176  VAL B N   1 
ATOM   5022 C  CA  . VAL B 2 176 ? 29.158  94.496  9.945   1.00 23.01 ? 176  VAL B CA  1 
ATOM   5023 C  C   . VAL B 2 176 ? 30.159  94.860  11.041  1.00 23.63 ? 176  VAL B C   1 
ATOM   5024 O  O   . VAL B 2 176 ? 31.065  95.655  10.755  1.00 23.88 ? 176  VAL B O   1 
ATOM   5025 C  CB  . VAL B 2 176 ? 28.360  95.734  9.505   1.00 22.41 ? 176  VAL B CB  1 
ATOM   5026 C  CG1 . VAL B 2 176 ? 27.577  95.455  8.227   1.00 23.00 ? 176  VAL B CG1 1 
ATOM   5027 C  CG2 . VAL B 2 176 ? 27.454  96.250  10.611  1.00 22.61 ? 176  VAL B CG2 1 
ATOM   5028 N  N   . SER B 2 177 ? 30.013  94.310  12.247  1.00 22.67 ? 177  SER B N   1 
ATOM   5029 C  CA  . SER B 2 177 ? 31.005  94.521  13.333  1.00 23.02 ? 177  SER B CA  1 
ATOM   5030 C  C   . SER B 2 177 ? 30.956  93.336  14.300  1.00 22.75 ? 177  SER B C   1 
ATOM   5031 O  O   . SER B 2 177 ? 29.884  92.735  14.456  1.00 23.09 ? 177  SER B O   1 
ATOM   5032 C  CB  . SER B 2 177 ? 30.761  95.845  14.024  1.00 23.21 ? 177  SER B CB  1 
ATOM   5033 O  OG  . SER B 2 177 ? 31.777  96.126  14.977  1.00 23.42 ? 177  SER B OG  1 
ATOM   5034 N  N   . GLU B 2 178 ? 32.089  93.004  14.908  1.00 23.69 ? 178  GLU B N   1 
ATOM   5035 C  CA  . GLU B 2 178 ? 32.191  91.834  15.815  1.00 23.28 ? 178  GLU B CA  1 
ATOM   5036 C  C   . GLU B 2 178 ? 33.340  92.048  16.798  1.00 23.16 ? 178  GLU B C   1 
ATOM   5037 O  O   . GLU B 2 178 ? 34.426  92.476  16.376  1.00 21.95 ? 178  GLU B O   1 
ATOM   5038 C  CB  . GLU B 2 178 ? 32.405  90.555  15.016  1.00 23.40 ? 178  GLU B CB  1 
ATOM   5039 C  CG  . GLU B 2 178 ? 32.429  89.303  15.872  1.00 24.41 ? 178  GLU B CG  1 
ATOM   5040 C  CD  . GLU B 2 178 ? 32.839  88.064  15.096  1.00 24.85 ? 178  GLU B CD  1 
ATOM   5041 O  OE1 . GLU B 2 178 ? 33.939  88.081  14.510  1.00 25.33 ? 178  GLU B OE1 1 
ATOM   5042 O  OE2 . GLU B 2 178 ? 32.048  87.096  15.057  1.00 24.31 ? 178  GLU B OE2 1 
ATOM   5043 N  N   . ALA B 2 179 ? 33.076  91.746  18.064  1.00 22.90 ? 179  ALA B N   1 
ATOM   5044 C  CA  . ALA B 2 179 ? 34.085  91.601  19.130  1.00 23.93 ? 179  ALA B CA  1 
ATOM   5045 C  C   . ALA B 2 179 ? 33.749  90.299  19.844  1.00 23.74 ? 179  ALA B C   1 
ATOM   5046 O  O   . ALA B 2 179 ? 32.585  90.072  20.173  1.00 25.52 ? 179  ALA B O   1 
ATOM   5047 C  CB  . ALA B 2 179 ? 34.047  92.812  20.031  1.00 24.36 ? 179  ALA B CB  1 
HETATM 5048 N  N   . MLZ B 2 180 ? 34.745  89.422  19.993  1.00 23.35 ? 180  MLZ B N   1 
HETATM 5049 C  CA  . MLZ B 2 180 ? 34.502  88.065  20.453  1.00 24.05 ? 180  MLZ B CA  1 
HETATM 5050 C  CB  . MLZ B 2 180 ? 34.324  87.108  19.268  1.00 25.28 ? 180  MLZ B CB  1 
HETATM 5051 C  CG  . MLZ B 2 180 ? 35.496  87.062  18.288  1.00 26.13 ? 180  MLZ B CG  1 
HETATM 5052 C  CD  . MLZ B 2 180 ? 35.435  85.902  17.319  1.00 25.98 ? 180  MLZ B CD  1 
HETATM 5053 C  CE  . MLZ B 2 180 ? 36.384  85.986  16.129  1.00 26.76 ? 180  MLZ B CE  1 
HETATM 5054 N  NZ  . MLZ B 2 180 ? 37.805  86.063  16.488  1.00 27.06 ? 180  MLZ B NZ  1 
HETATM 5055 C  CM  . MLZ B 2 180 ? 38.322  85.159  17.522  1.00 26.62 ? 180  MLZ B CM  1 
HETATM 5056 C  C   . MLZ B 2 180 ? 35.667  87.577  21.305  1.00 24.34 ? 180  MLZ B C   1 
HETATM 5057 O  O   . MLZ B 2 180 ? 36.779  88.090  21.216  1.00 23.25 ? 180  MLZ B O   1 
ATOM   5058 N  N   . GLN B 2 181 ? 35.374  86.572  22.128  1.00 25.01 ? 181  GLN B N   1 
ATOM   5059 C  CA  . GLN B 2 181 ? 36.388  85.748  22.757  1.00 27.09 ? 181  GLN B CA  1 
ATOM   5060 C  C   . GLN B 2 181 ? 37.297  85.165  21.675  1.00 28.40 ? 181  GLN B C   1 
ATOM   5061 O  O   . GLN B 2 181 ? 36.828  84.807  20.598  1.00 28.06 ? 181  GLN B O   1 
ATOM   5062 C  CB  . GLN B 2 181 ? 35.722  84.634  23.566  1.00 26.73 ? 181  GLN B CB  1 
ATOM   5063 C  CG  . GLN B 2 181 ? 34.919  85.127  24.763  1.00 25.82 ? 181  GLN B CG  1 
ATOM   5064 C  CD  . GLN B 2 181 ? 35.782  85.658  25.881  1.00 26.93 ? 181  GLN B CD  1 
ATOM   5065 O  OE1 . GLN B 2 181 ? 36.986  85.827  25.744  1.00 27.92 ? 181  GLN B OE1 1 
ATOM   5066 N  NE2 . GLN B 2 181 ? 35.162  85.943  27.012  1.00 28.31 ? 181  GLN B NE2 1 
ATOM   5067 N  N   . PRO B 2 182 ? 38.623  85.044  21.921  1.00 31.18 ? 182  PRO B N   1 
ATOM   5068 C  CA  . PRO B 2 182 ? 39.550  84.536  20.908  1.00 31.07 ? 182  PRO B CA  1 
ATOM   5069 C  C   . PRO B 2 182 ? 39.311  83.078  20.485  1.00 30.74 ? 182  PRO B C   1 
ATOM   5070 O  O   . PRO B 2 182 ? 39.701  82.740  19.392  1.00 30.63 ? 182  PRO B O   1 
ATOM   5071 C  CB  . PRO B 2 182 ? 40.933  84.681  21.566  1.00 32.10 ? 182  PRO B CB  1 
ATOM   5072 C  CG  . PRO B 2 182 ? 40.637  84.685  23.053  1.00 34.08 ? 182  PRO B CG  1 
ATOM   5073 C  CD  . PRO B 2 182 ? 39.301  85.390  23.183  1.00 32.68 ? 182  PRO B CD  1 
ATOM   5074 N  N   . GLU B 2 183 ? 38.652  82.265  21.315  1.00 31.12 ? 183  GLU B N   1 
ATOM   5075 C  CA  . GLU B 2 183 ? 38.387  80.833  21.007  1.00 32.92 ? 183  GLU B CA  1 
ATOM   5076 C  C   . GLU B 2 183 ? 37.128  80.677  20.136  1.00 33.16 ? 183  GLU B C   1 
ATOM   5077 O  O   . GLU B 2 183 ? 36.897  79.553  19.655  1.00 31.99 ? 183  GLU B O   1 
ATOM   5078 C  CB  . GLU B 2 183 ? 38.289  80.002  22.288  1.00 36.78 ? 183  GLU B CB  1 
ATOM   5079 C  CG  . GLU B 2 183 ? 37.151  80.387  23.217  1.00 40.20 ? 183  GLU B CG  1 
ATOM   5080 C  CD  . GLU B 2 183 ? 37.516  81.344  24.348  1.00 46.32 ? 183  GLU B CD  1 
ATOM   5081 O  OE1 . GLU B 2 183 ? 38.335  82.277  24.118  1.00 45.72 ? 183  GLU B OE1 1 
ATOM   5082 O  OE2 . GLU B 2 183 ? 36.976  81.162  25.466  1.00 48.05 ? 183  GLU B OE2 1 
ATOM   5083 N  N   . LEU B 2 184 ? 36.329  81.731  19.927  1.00 30.13 ? 184  LEU B N   1 
ATOM   5084 C  CA  . LEU B 2 184 ? 35.042  81.599  19.182  1.00 28.52 ? 184  LEU B CA  1 
ATOM   5085 C  C   . LEU B 2 184 ? 35.301  81.641  17.675  1.00 27.95 ? 184  LEU B C   1 
ATOM   5086 O  O   . LEU B 2 184 ? 36.318  82.220  17.265  1.00 28.34 ? 184  LEU B O   1 
ATOM   5087 C  CB  . LEU B 2 184 ? 34.084  82.716  19.606  1.00 27.86 ? 184  LEU B CB  1 
ATOM   5088 C  CG  . LEU B 2 184 ? 33.449  82.543  20.982  1.00 26.94 ? 184  LEU B CG  1 
ATOM   5089 C  CD1 . LEU B 2 184 ? 32.615  83.767  21.337  1.00 28.27 ? 184  LEU B CD1 1 
ATOM   5090 C  CD2 . LEU B 2 184 ? 32.610  81.275  21.043  1.00 26.16 ? 184  LEU B CD2 1 
ATOM   5091 N  N   . GLU B 2 185 ? 34.392  81.069  16.881  1.00 29.24 ? 185  GLU B N   1 
ATOM   5092 C  CA  . GLU B 2 185 ? 34.348  81.276  15.409  1.00 28.80 ? 185  GLU B CA  1 
ATOM   5093 C  C   . GLU B 2 185 ? 33.904  82.719  15.135  1.00 28.77 ? 185  GLU B C   1 
ATOM   5094 O  O   . GLU B 2 185 ? 33.179  83.285  15.966  1.00 29.47 ? 185  GLU B O   1 
ATOM   5095 C  CB  . GLU B 2 185 ? 33.436  80.259  14.716  1.00 30.02 ? 185  GLU B CB  1 
ATOM   5096 C  CG  . GLU B 2 185 ? 31.942  80.514  14.875  1.00 30.02 ? 185  GLU B CG  1 
ATOM   5097 C  CD  . GLU B 2 185 ? 31.311  79.972  16.149  1.00 30.05 ? 185  GLU B CD  1 
ATOM   5098 O  OE1 . GLU B 2 185 ? 31.874  80.188  17.239  1.00 29.00 ? 185  GLU B OE1 1 
ATOM   5099 O  OE2 . GLU B 2 185 ? 30.245  79.346  16.048  1.00 31.67 ? 185  GLU B OE2 1 
ATOM   5100 N  N   . SER B 2 186 ? 34.354  83.291  14.021  1.00 27.34 ? 186  SER B N   1 
ATOM   5101 C  CA  . SER B 2 186 ? 33.944  84.636  13.539  1.00 27.17 ? 186  SER B CA  1 
ATOM   5102 C  C   . SER B 2 186 ? 32.686  84.514  12.674  1.00 27.07 ? 186  SER B C   1 
ATOM   5103 O  O   . SER B 2 186 ? 32.603  83.547  11.882  1.00 27.09 ? 186  SER B O   1 
ATOM   5104 C  CB  . SER B 2 186 ? 35.046  85.304  12.770  1.00 28.28 ? 186  SER B CB  1 
ATOM   5105 O  OG  . SER B 2 186 ? 34.681  86.633  12.416  1.00 29.87 ? 186  SER B OG  1 
ATOM   5106 N  N   . PHE B 2 187 ? 31.764  85.473  12.803  1.00 23.67 ? 187  PHE B N   1 
ATOM   5107 C  CA  . PHE B 2 187 ? 30.606  85.646  11.892  1.00 23.29 ? 187  PHE B CA  1 
ATOM   5108 C  C   . PHE B 2 187 ? 30.772  86.948  11.103  1.00 23.15 ? 187  PHE B C   1 
ATOM   5109 O  O   . PHE B 2 187 ? 29.820  87.360  10.434  1.00 23.76 ? 187  PHE B O   1 
ATOM   5110 C  CB  . PHE B 2 187 ? 29.289  85.637  12.672  1.00 23.16 ? 187  PHE B CB  1 
ATOM   5111 C  CG  . PHE B 2 187 ? 29.003  84.358  13.419  1.00 22.23 ? 187  PHE B CG  1 
ATOM   5112 C  CD1 . PHE B 2 187 ? 29.021  83.135  12.767  1.00 23.52 ? 187  PHE B CD1 1 
ATOM   5113 C  CD2 . PHE B 2 187 ? 28.691  84.377  14.769  1.00 22.19 ? 187  PHE B CD2 1 
ATOM   5114 C  CE1 . PHE B 2 187 ? 28.738  81.959  13.448  1.00 23.07 ? 187  PHE B CE1 1 
ATOM   5115 C  CE2 . PHE B 2 187 ? 28.420  83.200  15.454  1.00 21.96 ? 187  PHE B CE2 1 
ATOM   5116 C  CZ  . PHE B 2 187 ? 28.432  81.995  14.791  1.00 22.45 ? 187  PHE B CZ  1 
ATOM   5117 N  N   . LEU B 2 188 ? 31.933  87.597  11.182  1.00 22.44 ? 188  LEU B N   1 
ATOM   5118 C  CA  . LEU B 2 188 ? 32.095  88.940  10.571  1.00 23.82 ? 188  LEU B CA  1 
ATOM   5119 C  C   . LEU B 2 188 ? 31.968  88.790  9.052   1.00 24.16 ? 188  LEU B C   1 
ATOM   5120 O  O   . LEU B 2 188 ? 32.648  87.918  8.502   1.00 23.15 ? 188  LEU B O   1 
ATOM   5121 C  CB  . LEU B 2 188 ? 33.442  89.549  10.964  1.00 23.73 ? 188  LEU B CB  1 
ATOM   5122 C  CG  . LEU B 2 188 ? 33.666  90.985  10.490  1.00 25.61 ? 188  LEU B CG  1 
ATOM   5123 C  CD1 . LEU B 2 188 ? 32.601  91.933  11.048  1.00 24.15 ? 188  LEU B CD1 1 
ATOM   5124 C  CD2 . LEU B 2 188 ? 35.069  91.459  10.865  1.00 25.86 ? 188  LEU B CD2 1 
ATOM   5125 N  N   . GLY B 2 189 ? 31.099  89.590  8.423   1.00 24.26 ? 189  GLY B N   1 
ATOM   5126 C  CA  . GLY B 2 189 ? 30.890  89.608  6.963   1.00 24.14 ? 189  GLY B CA  1 
ATOM   5127 C  C   . GLY B 2 189 ? 29.936  88.513  6.501   1.00 24.85 ? 189  GLY B C   1 
ATOM   5128 O  O   . GLY B 2 189 ? 29.702  88.408  5.276   1.00 21.49 ? 189  GLY B O   1 
ATOM   5129 N  N   . GLN B 2 190 ? 29.388  87.735  7.439   1.00 25.27 ? 190  GLN B N   1 
ATOM   5130 C  CA  . GLN B 2 190 ? 28.335  86.723  7.159   1.00 25.30 ? 190  GLN B CA  1 
ATOM   5131 C  C   . GLN B 2 190 ? 26.995  87.436  6.955   1.00 24.12 ? 190  GLN B C   1 
ATOM   5132 O  O   . GLN B 2 190 ? 26.833  88.560  7.450   1.00 22.48 ? 190  GLN B O   1 
ATOM   5133 C  CB  . GLN B 2 190 ? 28.270  85.734  8.316   1.00 26.01 ? 190  GLN B CB  1 
ATOM   5134 C  CG  . GLN B 2 190 ? 27.282  84.598  8.107   1.00 26.69 ? 190  GLN B CG  1 
ATOM   5135 C  CD  . GLN B 2 190 ? 27.677  83.374  8.895   1.00 26.83 ? 190  GLN B CD  1 
ATOM   5136 O  OE1 . GLN B 2 190 ? 28.850  83.156  9.197   1.00 26.16 ? 190  GLN B OE1 1 
ATOM   5137 N  NE2 . GLN B 2 190 ? 26.695  82.547  9.211   1.00 27.27 ? 190  GLN B NE2 1 
ATOM   5138 N  N   . TYR B 2 191 ? 26.070  86.802  6.241   1.00 24.55 ? 191  TYR B N   1 
ATOM   5139 C  CA  . TYR B 2 191 ? 24.659  87.246  6.109   1.00 24.68 ? 191  TYR B CA  1 
ATOM   5140 C  C   . TYR B 2 191 ? 23.731  86.135  6.613   1.00 26.11 ? 191  TYR B C   1 
ATOM   5141 O  O   . TYR B 2 191 ? 24.081  84.945  6.487   1.00 27.81 ? 191  TYR B O   1 
ATOM   5142 C  CB  . TYR B 2 191 ? 24.311  87.564  4.656   1.00 25.92 ? 191  TYR B CB  1 
ATOM   5143 C  CG  . TYR B 2 191 ? 25.010  88.734  4.014   1.00 25.68 ? 191  TYR B CG  1 
ATOM   5144 C  CD1 . TYR B 2 191 ? 26.349  88.662  3.662   1.00 26.21 ? 191  TYR B CD1 1 
ATOM   5145 C  CD2 . TYR B 2 191 ? 24.304  89.874  3.652   1.00 25.61 ? 191  TYR B CD2 1 
ATOM   5146 C  CE1 . TYR B 2 191 ? 26.978  89.707  3.005   1.00 25.63 ? 191  TYR B CE1 1 
ATOM   5147 C  CE2 . TYR B 2 191 ? 24.920  90.927  2.991   1.00 25.58 ? 191  TYR B CE2 1 
ATOM   5148 C  CZ  . TYR B 2 191 ? 26.260  90.838  2.663   1.00 25.58 ? 191  TYR B CZ  1 
ATOM   5149 O  OH  . TYR B 2 191 ? 26.877  91.863  2.017   1.00 29.27 ? 191  TYR B OH  1 
HETATM 5150 N  N   . 9IJ B 2 192 ? 22.549  86.519  7.028   1.00 25.63 ? 192  9IJ B N   1 
HETATM 5151 C  CA  . 9IJ B 2 192 ? 21.486  85.541  7.333   1.00 25.55 ? 192  9IJ B CA  1 
HETATM 5152 C  C   . 9IJ B 2 192 ? 20.208  85.908  6.569   1.00 26.50 ? 192  9IJ B C   1 
HETATM 5153 C  CB  . 9IJ B 2 192 ? 21.216  85.353  8.838   1.00 24.71 ? 192  9IJ B CB  1 
HETATM 5154 C  CG  . 9IJ B 2 192 ? 21.080  86.625  9.647   1.00 25.10 ? 192  9IJ B CG  1 
HETATM 5155 C  CD1 . 9IJ B 2 192 ? 19.818  87.163  9.835   1.00 24.19 ? 192  9IJ B CD1 1 
HETATM 5156 C  CD2 . 9IJ B 2 192 ? 22.189  87.227  10.264  1.00 26.30 ? 192  9IJ B CD2 1 
HETATM 5157 C  CE1 . 9IJ B 2 192 ? 19.649  88.322  10.588  1.00 24.03 ? 192  9IJ B CE1 1 
HETATM 5158 C  CE2 . 9IJ B 2 192 ? 22.017  88.393  11.010  1.00 24.80 ? 192  9IJ B CE2 1 
HETATM 5159 C  CZ  . 9IJ B 2 192 ? 20.749  88.928  11.183  1.00 24.68 ? 192  9IJ B CZ  1 
HETATM 5160 C  C01 . 9IJ B 2 192 ? 23.378  86.743  10.101  1.00 26.39 ? 192  9IJ B C01 1 
HETATM 5161 N  N01 . 9IJ B 2 192 ? 24.427  86.295  9.863   1.00 27.32 ? 192  9IJ B N01 1 
HETATM 5162 O  O   . 9IJ B 2 192 ? 19.991  87.317  6.519   1.00 25.35 ? 192  9IJ B O   1 
ATOM   5163 N  N   . PRO B 2 193 ? 19.361  85.034  6.041   1.00 26.87 ? 193  PRO B N   1 
ATOM   5164 C  CA  . PRO B 2 193 ? 18.163  85.481  5.296   1.00 25.89 ? 193  PRO B CA  1 
ATOM   5165 C  C   . PRO B 2 193 ? 17.117  86.174  6.181   1.00 26.20 ? 193  PRO B C   1 
ATOM   5166 O  O   . PRO B 2 193 ? 17.163  86.013  7.389   1.00 25.67 ? 193  PRO B O   1 
ATOM   5167 C  CB  . PRO B 2 193 ? 17.621  84.170  4.726   1.00 26.16 ? 193  PRO B CB  1 
ATOM   5168 C  CG  . PRO B 2 193 ? 17.884  83.189  5.837   1.00 26.89 ? 193  PRO B CG  1 
ATOM   5169 C  CD  . PRO B 2 193 ? 19.215  83.623  6.424   1.00 26.33 ? 193  PRO B CD  1 
ATOM   5170 N  N   . ALA B 2 194 ? 16.229  86.957  5.569   1.00 25.67 ? 194  ALA B N   1 
ATOM   5171 C  CA  . ALA B 2 194 ? 15.123  87.668  6.256   1.00 27.89 ? 194  ALA B CA  1 
ATOM   5172 C  C   . ALA B 2 194 ? 14.305  86.685  7.111   1.00 26.62 ? 194  ALA B C   1 
ATOM   5173 O  O   . ALA B 2 194 ? 13.863  87.085  8.190   1.00 27.13 ? 194  ALA B O   1 
ATOM   5174 C  CB  . ALA B 2 194 ? 14.243  88.373  5.246   1.00 28.39 ? 194  ALA B CB  1 
ATOM   5175 N  N   . SER B 2 195 ? 14.108  85.449  6.639   1.00 27.27 ? 195  SER B N   1 
ATOM   5176 C  CA  . SER B 2 195 ? 13.245  84.425  7.299   1.00 27.51 ? 195  SER B CA  1 
ATOM   5177 C  C   . SER B 2 195 ? 13.787  84.021  8.684   1.00 27.26 ? 195  SER B C   1 
ATOM   5178 O  O   . SER B 2 195 ? 12.994  83.482  9.490   1.00 26.94 ? 195  SER B O   1 
ATOM   5179 C  CB  . SER B 2 195 ? 13.062  83.230  6.418   1.00 27.18 ? 195  SER B CB  1 
ATOM   5180 O  OG  . SER B 2 195 ? 14.309  82.655  6.086   1.00 28.64 ? 195  SER B OG  1 
ATOM   5181 N  N   . ASP B 2 196 ? 15.068  84.290  8.968   1.00 25.75 ? 196  ASP B N   1 
ATOM   5182 C  CA  . ASP B 2 196 ? 15.715  83.959  10.265  1.00 26.46 ? 196  ASP B CA  1 
ATOM   5183 C  C   . ASP B 2 196 ? 15.110  84.817  11.379  1.00 27.08 ? 196  ASP B C   1 
ATOM   5184 O  O   . ASP B 2 196 ? 15.166  84.372  12.537  1.00 27.71 ? 196  ASP B O   1 
ATOM   5185 C  CB  . ASP B 2 196 ? 17.235  84.126  10.206  1.00 26.86 ? 196  ASP B CB  1 
ATOM   5186 C  CG  . ASP B 2 196 ? 17.966  82.913  9.654   1.00 27.55 ? 196  ASP B CG  1 
ATOM   5187 O  OD1 . ASP B 2 196 ? 17.319  82.078  9.005   1.00 28.19 ? 196  ASP B OD1 1 
ATOM   5188 O  OD2 . ASP B 2 196 ? 19.184  82.817  9.870   1.00 28.08 ? 196  ASP B OD2 1 
ATOM   5189 N  N   . ILE B 2 197 ? 14.597  86.008  11.053  1.00 26.67 ? 197  ILE B N   1 
ATOM   5190 C  CA  . ILE B 2 197 ? 13.857  86.878  12.010  1.00 26.82 ? 197  ILE B CA  1 
ATOM   5191 C  C   . ILE B 2 197 ? 12.452  87.105  11.455  1.00 29.56 ? 197  ILE B C   1 
ATOM   5192 O  O   . ILE B 2 197 ? 12.267  87.940  10.574  1.00 29.85 ? 197  ILE B O   1 
ATOM   5193 C  CB  . ILE B 2 197 ? 14.592  88.201  12.308  1.00 26.99 ? 197  ILE B CB  1 
ATOM   5194 C  CG1 . ILE B 2 197 ? 16.080  87.983  12.612  1.00 26.29 ? 197  ILE B CG1 1 
ATOM   5195 C  CG2 . ILE B 2 197 ? 13.875  88.922  13.446  1.00 28.46 ? 197  ILE B CG2 1 
ATOM   5196 C  CD1 . ILE B 2 197 ? 16.858  89.237  12.912  1.00 25.02 ? 197  ILE B CD1 1 
ATOM   5197 N  N   . PRO B 2 198 ? 11.420  86.378  11.953  1.00 30.45 ? 198  PRO B N   1 
ATOM   5198 C  CA  . PRO B 2 198 ? 10.058  86.521  11.431  1.00 31.66 ? 198  PRO B CA  1 
ATOM   5199 C  C   . PRO B 2 198 ? 9.479   87.899  11.777  1.00 30.93 ? 198  PRO B C   1 
ATOM   5200 O  O   . PRO B 2 198 ? 10.015  88.565  12.647  1.00 26.01 ? 198  PRO B O   1 
ATOM   5201 C  CB  . PRO B 2 198 ? 9.265   85.370  12.068  1.00 31.07 ? 198  PRO B CB  1 
ATOM   5202 C  CG  . PRO B 2 198 ? 10.072  84.960  13.279  1.00 32.55 ? 198  PRO B CG  1 
ATOM   5203 C  CD  . PRO B 2 198 ? 11.509  85.355  13.001  1.00 31.46 ? 198  PRO B CD  1 
ATOM   5204 N  N   . GLN B 2 199 ? 8.418   88.298  11.066  1.00 34.23 ? 199  GLN B N   1 
ATOM   5205 C  CA  . GLN B 2 199 ? 7.917   89.701  11.029  1.00 34.67 ? 199  GLN B CA  1 
ATOM   5206 C  C   . GLN B 2 199 ? 7.509   90.142  12.437  1.00 33.50 ? 199  GLN B C   1 
ATOM   5207 O  O   . GLN B 2 199 ? 7.778   91.302  12.789  1.00 34.86 ? 199  GLN B O   1 
ATOM   5208 C  CB  . GLN B 2 199 ? 6.758   89.845  10.038  1.00 37.41 ? 199  GLN B CB  1 
ATOM   5209 C  CG  . GLN B 2 199 ? 7.205   89.797  8.581   1.00 42.12 ? 199  GLN B CG  1 
ATOM   5210 C  CD  . GLN B 2 199 ? 8.262   90.825  8.245   1.00 46.97 ? 199  GLN B CD  1 
ATOM   5211 O  OE1 . GLN B 2 199 ? 8.092   92.026  8.474   1.00 51.40 ? 199  GLN B OE1 1 
ATOM   5212 N  NE2 . GLN B 2 199 ? 9.377   90.362  7.696   1.00 48.34 ? 199  GLN B NE2 1 
ATOM   5213 N  N   . GLN B 2 200 ? 6.882   89.254  13.206  1.00 33.14 ? 200  GLN B N   1 
ATOM   5214 C  CA  . GLN B 2 200 ? 6.372   89.577  14.563  1.00 36.14 ? 200  GLN B CA  1 
ATOM   5215 C  C   . GLN B 2 200 ? 7.566   89.786  15.524  1.00 34.21 ? 200  GLN B C   1 
ATOM   5216 O  O   . GLN B 2 200 ? 7.471   90.652  16.423  1.00 31.47 ? 200  GLN B O   1 
ATOM   5217 C  CB  . GLN B 2 200 ? 5.337   88.523  14.960  1.00 38.97 ? 200  GLN B CB  1 
ATOM   5218 C  CG  . GLN B 2 200 ? 5.908   87.171  15.358  1.00 43.70 ? 200  GLN B CG  1 
ATOM   5219 C  CD  . GLN B 2 200 ? 6.209   86.190  14.244  1.00 45.59 ? 200  GLN B CD  1 
ATOM   5220 O  OE1 . GLN B 2 200 ? 5.981   86.435  13.052  1.00 39.70 ? 200  GLN B OE1 1 
ATOM   5221 N  NE2 . GLN B 2 200 ? 6.746   85.044  14.650  1.00 44.09 ? 200  GLN B NE2 1 
ATOM   5222 N  N   . ALA B 2 201 ? 8.682   89.082  15.313  1.00 32.35 ? 201  ALA B N   1 
ATOM   5223 C  CA  . ALA B 2 201 ? 9.958   89.324  16.039  1.00 30.65 ? 201  ALA B CA  1 
ATOM   5224 C  C   . ALA B 2 201 ? 10.495  90.716  15.669  1.00 29.25 ? 201  ALA B C   1 
ATOM   5225 O  O   . ALA B 2 201 ? 10.894  91.463  16.570  1.00 29.41 ? 201  ALA B O   1 
ATOM   5226 C  CB  . ALA B 2 201 ? 10.949  88.228  15.729  1.00 29.46 ? 201  ALA B CB  1 
ATOM   5227 N  N   . ARG B 2 202 ? 10.476  91.064  14.380  1.00 30.17 ? 202  ARG B N   1 
ATOM   5228 C  CA  . ARG B 2 202 ? 10.896  92.410  13.894  1.00 30.35 ? 202  ARG B CA  1 
ATOM   5229 C  C   . ARG B 2 202 ? 10.025  93.504  14.525  1.00 30.09 ? 202  ARG B C   1 
ATOM   5230 O  O   . ARG B 2 202 ? 10.581  94.553  14.928  1.00 31.16 ? 202  ARG B O   1 
ATOM   5231 C  CB  . ARG B 2 202 ? 10.813  92.482  12.368  1.00 30.99 ? 202  ARG B CB  1 
ATOM   5232 C  CG  . ARG B 2 202 ? 11.965  91.777  11.673  1.00 31.13 ? 202  ARG B CG  1 
ATOM   5233 C  CD  . ARG B 2 202 ? 11.692  91.509  10.212  1.00 30.05 ? 202  ARG B CD  1 
ATOM   5234 N  NE  . ARG B 2 202 ? 12.667  90.557  9.704   1.00 29.93 ? 202  ARG B NE  1 
ATOM   5235 C  CZ  . ARG B 2 202 ? 13.870  90.858  9.225   1.00 28.56 ? 202  ARG B CZ  1 
ATOM   5236 N  NH1 . ARG B 2 202 ? 14.288  92.113  9.158   1.00 28.68 ? 202  ARG B NH1 1 
ATOM   5237 N  NH2 . ARG B 2 202 ? 14.646  89.885  8.789   1.00 28.82 ? 202  ARG B NH2 1 
ATOM   5238 N  N   . ALA B 2 203 ? 8.710   93.288  14.570  1.00 30.26 ? 203  ALA B N   1 
ATOM   5239 C  CA  . ALA B 2 203 ? 7.733   94.223  15.174  1.00 31.63 ? 203  ALA B CA  1 
ATOM   5240 C  C   . ALA B 2 203 ? 8.124   94.471  16.636  1.00 31.36 ? 203  ALA B C   1 
ATOM   5241 O  O   . ALA B 2 203 ? 8.144   95.651  17.066  1.00 30.23 ? 203  ALA B O   1 
ATOM   5242 C  CB  . ALA B 2 203 ? 6.334   93.672  15.061  1.00 32.01 ? 203  ALA B CB  1 
ATOM   5243 N  N   . LEU B 2 204 ? 8.478   93.410  17.365  1.00 29.61 ? 204  LEU B N   1 
ATOM   5244 C  CA  . LEU B 2 204 ? 8.855   93.525  18.803  1.00 30.46 ? 204  LEU B CA  1 
ATOM   5245 C  C   . LEU B 2 204 ? 10.248  94.160  18.954  1.00 29.61 ? 204  LEU B C   1 
ATOM   5246 O  O   . LEU B 2 204 ? 10.428  94.926  19.917  1.00 29.36 ? 204  LEU B O   1 
ATOM   5247 C  CB  . LEU B 2 204 ? 8.736   92.147  19.460  1.00 31.27 ? 204  LEU B CB  1 
ATOM   5248 C  CG  . LEU B 2 204 ? 7.291   91.659  19.569  1.00 32.40 ? 204  LEU B CG  1 
ATOM   5249 C  CD1 . LEU B 2 204 ? 7.224   90.193  19.952  1.00 32.46 ? 204  LEU B CD1 1 
ATOM   5250 C  CD2 . LEU B 2 204 ? 6.499   92.511  20.549  1.00 32.68 ? 204  LEU B CD2 1 
ATOM   5251 N  N   . TYR B 2 205 ? 11.181  93.921  18.026  1.00 28.84 ? 205  TYR B N   1 
ATOM   5252 C  CA  . TYR B 2 205 ? 12.505  94.604  18.027  1.00 29.53 ? 205  TYR B CA  1 
ATOM   5253 C  C   . TYR B 2 205 ? 12.283  96.106  17.810  1.00 31.04 ? 205  TYR B C   1 
ATOM   5254 O  O   . TYR B 2 205 ? 13.034  96.910  18.392  1.00 28.03 ? 205  TYR B O   1 
ATOM   5255 C  CB  . TYR B 2 205 ? 13.470  94.007  16.996  1.00 28.19 ? 205  TYR B CB  1 
ATOM   5256 C  CG  . TYR B 2 205 ? 14.045  92.669  17.391  1.00 27.40 ? 205  TYR B CG  1 
ATOM   5257 C  CD1 . TYR B 2 205 ? 14.710  92.490  18.596  1.00 26.82 ? 205  TYR B CD1 1 
ATOM   5258 C  CD2 . TYR B 2 205 ? 13.919  91.574  16.556  1.00 26.61 ? 205  TYR B CD2 1 
ATOM   5259 C  CE1 . TYR B 2 205 ? 15.228  91.255  18.955  1.00 27.02 ? 205  TYR B CE1 1 
ATOM   5260 C  CE2 . TYR B 2 205 ? 14.421  90.334  16.902  1.00 26.63 ? 205  TYR B CE2 1 
ATOM   5261 C  CZ  . TYR B 2 205 ? 15.088  90.173  18.101  1.00 26.45 ? 205  TYR B CZ  1 
ATOM   5262 O  OH  . TYR B 2 205 ? 15.568  88.935  18.425  1.00 24.73 ? 205  TYR B OH  1 
ATOM   5263 N  N   . LEU B 2 206 ? 11.264  96.477  17.023  1.00 32.63 ? 206  LEU B N   1 
ATOM   5264 C  CA  . LEU B 2 206 ? 10.918  97.907  16.772  1.00 32.81 ? 206  LEU B CA  1 
ATOM   5265 C  C   . LEU B 2 206 ? 10.277  98.512  18.020  1.00 31.60 ? 206  LEU B C   1 
ATOM   5266 O  O   . LEU B 2 206 ? 10.573  99.646  18.379  1.00 30.94 ? 206  LEU B O   1 
ATOM   5267 C  CB  . LEU B 2 206 ? 9.993   98.001  15.554  1.00 34.25 ? 206  LEU B CB  1 
ATOM   5268 C  CG  . LEU B 2 206 ? 9.778   99.402  14.976  1.00 36.23 ? 206  LEU B CG  1 
ATOM   5269 C  CD1 . LEU B 2 206 ? 11.093  100.128 14.756  1.00 35.61 ? 206  LEU B CD1 1 
ATOM   5270 C  CD2 . LEU B 2 206 ? 9.003   99.328  13.667  1.00 38.45 ? 206  LEU B CD2 1 
HETATM 5271 N  N   . MLZ B 2 207 ? 9.428   97.736  18.700  1.00 33.34 ? 207  MLZ B N   1 
HETATM 5272 C  CA  . MLZ B 2 207 ? 8.641   98.234  19.822  1.00 35.65 ? 207  MLZ B CA  1 
HETATM 5273 C  CB  . MLZ B 2 207 ? 7.437   97.322  20.064  1.00 38.51 ? 207  MLZ B CB  1 
HETATM 5274 C  CG  . MLZ B 2 207 ? 6.270   97.554  19.114  1.00 41.66 ? 207  MLZ B CG  1 
HETATM 5275 C  CD  . MLZ B 2 207 ? 5.180   96.516  19.236  1.00 44.33 ? 207  MLZ B CD  1 
HETATM 5276 C  CE  . MLZ B 2 207 ? 3.822   97.017  18.769  1.00 44.97 ? 207  MLZ B CE  1 
HETATM 5277 N  NZ  . MLZ B 2 207 ? 2.865   95.911  18.711  1.00 46.41 ? 207  MLZ B NZ  1 
HETATM 5278 C  CM  . MLZ B 2 207 ? 2.551   95.232  19.976  1.00 46.19 ? 207  MLZ B CM  1 
HETATM 5279 C  C   . MLZ B 2 207 ? 9.466   98.340  21.105  1.00 35.27 ? 207  MLZ B C   1 
HETATM 5280 O  O   . MLZ B 2 207 ? 9.169   99.182  21.951  1.00 37.08 ? 207  MLZ B O   1 
ATOM   5281 N  N   . ASN B 2 208 ? 10.466  97.466  21.271  1.00 32.27 ? 208  ASN B N   1 
ATOM   5282 C  CA  . ASN B 2 208 ? 11.240  97.392  22.505  1.00 30.56 ? 208  ASN B CA  1 
ATOM   5283 C  C   . ASN B 2 208 ? 12.713  97.663  22.191  1.00 29.38 ? 208  ASN B C   1 
ATOM   5284 O  O   . ASN B 2 208 ? 13.253  97.000  21.292  1.00 28.26 ? 208  ASN B O   1 
ATOM   5285 C  CB  . ASN B 2 208 ? 11.109  96.017  23.164  1.00 31.68 ? 208  ASN B CB  1 
ATOM   5286 C  CG  . ASN B 2 208 ? 9.678   95.653  23.501  1.00 32.79 ? 208  ASN B CG  1 
ATOM   5287 O  OD1 . ASN B 2 208 ? 9.098   96.218  24.419  1.00 36.43 ? 208  ASN B OD1 1 
ATOM   5288 N  ND2 . ASN B 2 208 ? 9.106   94.704  22.778  1.00 33.54 ? 208  ASN B ND2 1 
ATOM   5289 N  N   . THR B 2 209 ? 13.363  98.575  22.909  1.00 28.75 ? 209  THR B N   1 
ATOM   5290 C  CA  . THR B 2 209 ? 14.802  98.866  22.659  1.00 30.28 ? 209  THR B CA  1 
ATOM   5291 C  C   . THR B 2 209 ? 15.652  97.635  22.995  1.00 27.69 ? 209  THR B C   1 
ATOM   5292 O  O   . THR B 2 209 ? 16.585  97.351  22.228  1.00 25.72 ? 209  THR B O   1 
ATOM   5293 C  CB  . THR B 2 209 ? 15.314  100.075 23.439  1.00 31.01 ? 209  THR B CB  1 
ATOM   5294 O  OG1 . THR B 2 209 ? 14.482  101.170 23.075  1.00 32.18 ? 209  THR B OG1 1 
ATOM   5295 C  CG2 . THR B 2 209 ? 16.764  100.377 23.131  1.00 32.45 ? 209  THR B CG2 1 
ATOM   5296 N  N   . LEU B 2 210 ? 15.332  96.947  24.096  1.00 26.30 ? 210  LEU B N   1 
ATOM   5297 C  CA  . LEU B 2 210 ? 16.108  95.793  24.616  1.00 26.89 ? 210  LEU B CA  1 
ATOM   5298 C  C   . LEU B 2 210 ? 15.292  94.507  24.489  1.00 27.05 ? 210  LEU B C   1 
ATOM   5299 O  O   . LEU B 2 210 ? 14.065  94.543  24.711  1.00 28.89 ? 210  LEU B O   1 
ATOM   5300 C  CB  . LEU B 2 210 ? 16.487  96.045  26.076  1.00 27.83 ? 210  LEU B CB  1 
ATOM   5301 C  CG  . LEU B 2 210 ? 17.334  97.280  26.335  1.00 27.80 ? 210  LEU B CG  1 
ATOM   5302 C  CD1 . LEU B 2 210 ? 17.711  97.358  27.804  1.00 28.72 ? 210  LEU B CD1 1 
ATOM   5303 C  CD2 . LEU B 2 210 ? 18.581  97.297  25.467  1.00 28.65 ? 210  LEU B CD2 1 
ATOM   5304 N  N   . ARG B 2 211 ? 15.968  93.415  24.137  1.00 26.20 ? 211  ARG B N   1 
ATOM   5305 C  CA  . ARG B 2 211 ? 15.410  92.039  24.188  1.00 25.61 ? 211  ARG B CA  1 
ATOM   5306 C  C   . ARG B 2 211 ? 16.400  91.183  24.981  1.00 26.55 ? 211  ARG B C   1 
ATOM   5307 O  O   . ARG B 2 211 ? 17.556  91.051  24.526  1.00 25.61 ? 211  ARG B O   1 
ATOM   5308 C  CB  . ARG B 2 211 ? 15.148  91.515  22.774  1.00 25.26 ? 211  ARG B CB  1 
ATOM   5309 C  CG  . ARG B 2 211 ? 14.581  90.105  22.715  1.00 25.21 ? 211  ARG B CG  1 
ATOM   5310 C  CD  . ARG B 2 211 ? 13.481  89.852  23.723  1.00 24.85 ? 211  ARG B CD  1 
ATOM   5311 N  NE  . ARG B 2 211 ? 12.877  88.540  23.524  1.00 25.05 ? 211  ARG B NE  1 
ATOM   5312 C  CZ  . ARG B 2 211 ? 12.087  87.907  24.388  1.00 24.42 ? 211  ARG B CZ  1 
ATOM   5313 N  NH1 . ARG B 2 211 ? 11.794  88.441  25.563  1.00 24.77 ? 211  ARG B NH1 1 
ATOM   5314 N  NH2 . ARG B 2 211 ? 11.610  86.715  24.073  1.00 24.79 ? 211  ARG B NH2 1 
ATOM   5315 N  N   . ILE B 2 212 ? 15.970  90.668  26.137  1.00 26.87 ? 212  ILE B N   1 
ATOM   5316 C  CA  . ILE B 2 212 ? 16.828  89.907  27.093  1.00 27.26 ? 212  ILE B CA  1 
ATOM   5317 C  C   . ILE B 2 212 ? 16.452  88.423  27.032  1.00 26.35 ? 212  ILE B C   1 
ATOM   5318 O  O   . ILE B 2 212 ? 15.264  88.102  27.153  1.00 26.41 ? 212  ILE B O   1 
ATOM   5319 C  CB  . ILE B 2 212 ? 16.709  90.466  28.527  1.00 28.22 ? 212  ILE B CB  1 
ATOM   5320 C  CG1 . ILE B 2 212 ? 17.138  91.933  28.609  1.00 31.15 ? 212  ILE B CG1 1 
ATOM   5321 C  CG2 . ILE B 2 212 ? 17.487  89.605  29.511  1.00 28.66 ? 212  ILE B CG2 1 
ATOM   5322 C  CD1 . ILE B 2 212 ? 15.987  92.911  28.761  1.00 33.55 ? 212  ILE B CD1 1 
ATOM   5323 N  N   . ILE B 2 213 ? 17.447  87.559  26.838  1.00 24.79 ? 213  ILE B N   1 
ATOM   5324 C  CA  . ILE B 2 213 ? 17.330  86.092  27.058  1.00 25.77 ? 213  ILE B CA  1 
ATOM   5325 C  C   . ILE B 2 213 ? 18.386  85.702  28.099  1.00 26.61 ? 213  ILE B C   1 
ATOM   5326 O  O   . ILE B 2 213 ? 19.600  85.781  27.785  1.00 26.28 ? 213  ILE B O   1 
ATOM   5327 C  CB  . ILE B 2 213 ? 17.467  85.313  25.738  1.00 26.43 ? 213  ILE B CB  1 
ATOM   5328 C  CG1 . ILE B 2 213 ? 16.488  85.831  24.678  1.00 26.37 ? 213  ILE B CG1 1 
ATOM   5329 C  CG2 . ILE B 2 213 ? 17.301  83.816  25.991  1.00 27.76 ? 213  ILE B CG2 1 
ATOM   5330 C  CD1 . ILE B 2 213 ? 16.593  85.136  23.337  1.00 26.03 ? 213  ILE B CD1 1 
ATOM   5331 N  N   . SER B 2 214 ? 17.943  85.330  29.303  1.00 27.12 ? 214  SER B N   1 
ATOM   5332 C  CA  . SER B 2 214 ? 18.850  84.985  30.433  1.00 27.92 ? 214  SER B CA  1 
ATOM   5333 C  C   . SER B 2 214 ? 19.404  83.566  30.258  1.00 27.44 ? 214  SER B C   1 
ATOM   5334 O  O   . SER B 2 214 ? 20.534  83.319  30.713  1.00 26.58 ? 214  SER B O   1 
ATOM   5335 C  CB  . SER B 2 214 ? 18.156  85.154  31.769  1.00 28.46 ? 214  SER B CB  1 
ATOM   5336 O  OG  . SER B 2 214 ? 17.000  84.337  31.837  1.00 28.68 ? 214  SER B OG  1 
ATOM   5337 N  N   . ASP B 2 215 ? 18.628  82.666  29.650  1.00 29.13 ? 215  ASP B N   1 
ATOM   5338 C  CA  . ASP B 2 215 ? 18.941  81.209  29.602  1.00 31.86 ? 215  ASP B CA  1 
ATOM   5339 C  C   . ASP B 2 215 ? 18.144  80.551  28.475  1.00 31.66 ? 215  ASP B C   1 
ATOM   5340 O  O   . ASP B 2 215 ? 16.950  80.320  28.654  1.00 35.13 ? 215  ASP B O   1 
ATOM   5341 C  CB  . ASP B 2 215 ? 18.661  80.526  30.947  1.00 33.21 ? 215  ASP B CB  1 
ATOM   5342 C  CG  . ASP B 2 215 ? 19.212  79.110  31.058  1.00 35.81 ? 215  ASP B CG  1 
ATOM   5343 O  OD1 . ASP B 2 215 ? 19.672  78.558  30.028  1.00 34.42 ? 215  ASP B OD1 1 
ATOM   5344 O  OD2 . ASP B 2 215 ? 19.194  78.571  32.181  1.00 41.12 ? 215  ASP B OD2 1 
ATOM   5345 N  N   . ALA B 2 216 ? 18.817  80.211  27.377  1.00 33.02 ? 216  ALA B N   1 
ATOM   5346 C  CA  . ALA B 2 216 ? 18.222  79.581  26.177  1.00 34.95 ? 216  ALA B CA  1 
ATOM   5347 C  C   . ALA B 2 216 ? 17.788  78.133  26.467  1.00 37.09 ? 216  ALA B C   1 
ATOM   5348 O  O   . ALA B 2 216 ? 17.048  77.577  25.626  1.00 38.75 ? 216  ALA B O   1 
ATOM   5349 C  CB  . ALA B 2 216 ? 19.209  79.644  25.039  1.00 33.79 ? 216  ALA B CB  1 
ATOM   5350 N  N   . SER B 2 217 ? 18.244  77.541  27.576  1.00 37.73 ? 217  SER B N   1 
ATOM   5351 C  CA  . SER B 2 217 ? 17.879  76.167  28.033  1.00 44.57 ? 217  SER B CA  1 
ATOM   5352 C  C   . SER B 2 217 ? 17.155  76.215  29.385  1.00 48.37 ? 217  SER B C   1 
ATOM   5353 O  O   . SER B 2 217 ? 17.083  75.164  30.041  1.00 54.81 ? 217  SER B O   1 
ATOM   5354 C  CB  . SER B 2 217 ? 19.093  75.276  28.137  1.00 47.19 ? 217  SER B CB  1 
ATOM   5355 O  OG  . SER B 2 217 ? 19.757  75.158  26.891  1.00 51.12 ? 217  SER B OG  1 
ATOM   5356 N  N   . GLY B 2 218 ? 16.638  77.383  29.777  1.00 51.20 ? 218  GLY B N   1 
ATOM   5357 C  CA  . GLY B 2 218 ? 16.028  77.632  31.097  1.00 51.58 ? 218  GLY B CA  1 
ATOM   5358 C  C   . GLY B 2 218 ? 14.590  77.152  31.154  1.00 51.04 ? 218  GLY B C   1 
ATOM   5359 O  O   . GLY B 2 218 ? 13.882  77.264  30.135  1.00 52.41 ? 218  GLY B O   1 
ATOM   5360 N  N   . THR B 2 219 ? 14.177  76.626  32.310  1.00 50.32 ? 219  THR B N   1 
ATOM   5361 C  CA  . THR B 2 219 ? 12.800  76.112  32.543  1.00 52.27 ? 219  THR B CA  1 
ATOM   5362 C  C   . THR B 2 219 ? 11.826  77.299  32.573  1.00 51.12 ? 219  THR B C   1 
ATOM   5363 O  O   . THR B 2 219 ? 11.868  78.075  33.546  1.00 58.76 ? 219  THR B O   1 
ATOM   5364 C  CB  . THR B 2 219 ? 12.730  75.256  33.814  1.00 51.53 ? 219  THR B CB  1 
ATOM   5365 N  N   . ARG B 2 220 ? 10.987  77.413  31.542  1.00 46.00 ? 220  ARG B N   1 
ATOM   5366 C  CA  . ARG B 2 220 ? 9.901   78.427  31.419  1.00 45.68 ? 220  ARG B CA  1 
ATOM   5367 C  C   . ARG B 2 220 ? 9.008   78.407  32.667  1.00 44.10 ? 220  ARG B C   1 
ATOM   5368 O  O   . ARG B 2 220 ? 8.689   77.305  33.147  1.00 41.99 ? 220  ARG B O   1 
ATOM   5369 C  CB  . ARG B 2 220 ? 9.046   78.128  30.185  1.00 47.14 ? 220  ARG B CB  1 
ATOM   5370 C  CG  . ARG B 2 220 ? 9.788   78.288  28.868  1.00 50.08 ? 220  ARG B CG  1 
ATOM   5371 C  CD  . ARG B 2 220 ? 8.895   78.042  27.669  1.00 54.00 ? 220  ARG B CD  1 
ATOM   5372 N  NE  . ARG B 2 220 ? 9.594   78.382  26.434  1.00 57.63 ? 220  ARG B NE  1 
ATOM   5373 C  CZ  . ARG B 2 220 ? 10.546  77.642  25.866  1.00 58.37 ? 220  ARG B CZ  1 
ATOM   5374 N  NH1 . ARG B 2 220 ? 10.928  76.497  26.414  1.00 56.46 ? 220  ARG B NH1 1 
ATOM   5375 N  NH2 . ARG B 2 220 ? 11.120  78.056  24.746  1.00 58.98 ? 220  ARG B NH2 1 
ATOM   5376 N  N   . ILE B 2 221 ? 8.618   79.587  33.161  1.00 40.45 ? 221  ILE B N   1 
ATOM   5377 C  CA  . ILE B 2 221 ? 7.697   79.746  34.325  1.00 39.11 ? 221  ILE B CA  1 
ATOM   5378 C  C   . ILE B 2 221 ? 6.325   80.117  33.774  1.00 37.72 ? 221  ILE B C   1 
ATOM   5379 O  O   . ILE B 2 221 ? 6.188   81.143  33.104  1.00 35.84 ? 221  ILE B O   1 
ATOM   5380 C  CB  . ILE B 2 221 ? 8.213   80.799  35.327  1.00 39.29 ? 221  ILE B CB  1 
ATOM   5381 C  CG1 . ILE B 2 221 ? 9.679   80.573  35.712  1.00 39.66 ? 221  ILE B CG1 1 
ATOM   5382 C  CG2 . ILE B 2 221 ? 7.308   80.868  36.551  1.00 39.97 ? 221  ILE B CG2 1 
ATOM   5383 C  CD1 . ILE B 2 221 ? 9.954   79.247  36.385  1.00 40.05 ? 221  ILE B CD1 1 
ATOM   5384 N  N   . PRO B 2 222 ? 5.276   79.304  34.040  1.00 37.12 ? 222  PRO B N   1 
ATOM   5385 C  CA  . PRO B 2 222 ? 3.944   79.568  33.497  1.00 37.70 ? 222  PRO B CA  1 
ATOM   5386 C  C   . PRO B 2 222 ? 3.304   80.813  34.124  1.00 36.69 ? 222  PRO B C   1 
ATOM   5387 O  O   . PRO B 2 222 ? 3.488   81.038  35.311  1.00 37.64 ? 222  PRO B O   1 
ATOM   5388 C  CB  . PRO B 2 222 ? 3.125   78.311  33.836  1.00 38.79 ? 222  PRO B CB  1 
ATOM   5389 C  CG  . PRO B 2 222 ? 3.871   77.641  34.976  1.00 38.98 ? 222  PRO B CG  1 
ATOM   5390 C  CD  . PRO B 2 222 ? 5.318   78.077  34.852  1.00 39.34 ? 222  PRO B CD  1 
ATOM   5391 N  N   . VAL B 2 223 ? 2.580   81.585  33.315  1.00 37.45 ? 223  VAL B N   1 
ATOM   5392 C  CA  . VAL B 2 223 ? 1.677   82.668  33.799  1.00 40.23 ? 223  VAL B CA  1 
ATOM   5393 C  C   . VAL B 2 223 ? 0.331   82.025  34.154  1.00 42.75 ? 223  VAL B C   1 
ATOM   5394 O  O   . VAL B 2 223 ? -0.262  81.381  33.271  1.00 43.54 ? 223  VAL B O   1 
ATOM   5395 C  CB  . VAL B 2 223 ? 1.504   83.787  32.761  1.00 41.15 ? 223  VAL B CB  1 
ATOM   5396 C  CG1 . VAL B 2 223 ? 0.574   84.876  33.273  1.00 42.23 ? 223  VAL B CG1 1 
ATOM   5397 C  CG2 . VAL B 2 223 ? 2.843   84.375  32.344  1.00 41.72 ? 223  VAL B CG2 1 
ATOM   5398 N  N   . LEU B 2 224 ? -0.114  82.198  35.402  1.00 43.53 ? 224  LEU B N   1 
ATOM   5399 C  CA  . LEU B 2 224 ? -1.336  81.562  35.968  1.00 43.57 ? 224  LEU B CA  1 
ATOM   5400 C  C   . LEU B 2 224 ? -2.419  82.622  36.154  1.00 42.53 ? 224  LEU B C   1 
ATOM   5401 O  O   . LEU B 2 224 ? -2.253  83.533  36.964  1.00 39.11 ? 224  LEU B O   1 
ATOM   5402 C  CB  . LEU B 2 224 ? -0.964  80.888  37.294  1.00 44.12 ? 224  LEU B CB  1 
ATOM   5403 C  CG  . LEU B 2 224 ? 0.136   79.830  37.190  1.00 44.10 ? 224  LEU B CG  1 
ATOM   5404 C  CD1 . LEU B 2 224 ? 0.617   79.403  38.571  1.00 45.22 ? 224  LEU B CD1 1 
ATOM   5405 C  CD2 . LEU B 2 224 ? -0.337  78.627  36.385  1.00 43.77 ? 224  LEU B CD2 1 
ATOM   5406 N  N   . PRO B 2 225 ? -3.551  82.559  35.409  1.00 45.35 ? 225  PRO B N   1 
ATOM   5407 C  CA  . PRO B 2 225 ? -3.771  81.552  34.367  1.00 45.62 ? 225  PRO B CA  1 
ATOM   5408 C  C   . PRO B 2 225 ? -3.276  81.998  32.979  1.00 45.45 ? 225  PRO B C   1 
ATOM   5409 O  O   . PRO B 2 225 ? -3.290  83.188  32.696  1.00 43.87 ? 225  PRO B O   1 
ATOM   5410 C  CB  . PRO B 2 225 ? -5.301  81.430  34.392  1.00 45.50 ? 225  PRO B CB  1 
ATOM   5411 C  CG  . PRO B 2 225 ? -5.757  82.858  34.630  1.00 46.06 ? 225  PRO B CG  1 
ATOM   5412 C  CD  . PRO B 2 225 ? -4.714  83.452  35.559  1.00 45.59 ? 225  PRO B CD  1 
ATOM   5413 N  N   . ALA B 2 226 ? -2.829  81.043  32.158  1.00 45.32 ? 226  ALA B N   1 
ATOM   5414 C  CA  . ALA B 2 226 ? -2.408  81.276  30.755  1.00 49.27 ? 226  ALA B CA  1 
ATOM   5415 C  C   . ALA B 2 226 ? -3.564  81.934  29.989  1.00 48.49 ? 226  ALA B C   1 
ATOM   5416 O  O   . ALA B 2 226 ? -3.328  82.920  29.272  1.00 49.52 ? 226  ALA B O   1 
ATOM   5417 C  CB  . ALA B 2 226 ? -1.974  79.977  30.113  1.00 49.76 ? 226  ALA B CB  1 
ATOM   5418 N  N   . VAL B 2 227 ? -4.777  81.409  30.164  1.00 50.60 ? 227  VAL B N   1 
ATOM   5419 C  CA  . VAL B 2 227 ? -6.042  81.968  29.595  1.00 51.48 ? 227  VAL B CA  1 
ATOM   5420 C  C   . VAL B 2 227 ? -6.972  82.326  30.764  1.00 50.50 ? 227  VAL B C   1 
ATOM   5421 O  O   . VAL B 2 227 ? -7.121  81.483  31.668  1.00 51.33 ? 227  VAL B O   1 
ATOM   5422 C  CB  . VAL B 2 227 ? -6.699  80.971  28.618  1.00 51.68 ? 227  VAL B CB  1 
ATOM   5423 C  CG1 . VAL B 2 227 ? -8.019  81.496  28.083  1.00 53.56 ? 227  VAL B CG1 1 
ATOM   5424 C  CG2 . VAL B 2 227 ? -5.772  80.609  27.467  1.00 51.52 ? 227  VAL B CG2 1 
ATOM   5425 N  N   . ASP B 2 228 ? -7.570  83.522  30.744  1.00 48.65 ? 228  ASP B N   1 
ATOM   5426 C  CA  . ASP B 2 228 ? -8.406  84.050  31.862  1.00 53.68 ? 228  ASP B CA  1 
ATOM   5427 C  C   . ASP B 2 228 ? -9.859  83.575  31.693  1.00 53.28 ? 228  ASP B C   1 
ATOM   5428 O  O   . ASP B 2 228 ? -10.086 82.743  30.793  1.00 50.94 ? 228  ASP B O   1 
ATOM   5429 C  CB  . ASP B 2 228 ? -8.296  85.576  31.975  1.00 51.92 ? 228  ASP B CB  1 
ATOM   5430 C  CG  . ASP B 2 228 ? -8.966  86.366  30.862  1.00 52.80 ? 228  ASP B CG  1 
ATOM   5431 O  OD1 . ASP B 2 228 ? -9.594  85.742  29.982  1.00 54.26 ? 228  ASP B OD1 1 
ATOM   5432 O  OD2 . ASP B 2 228 ? -8.853  87.607  30.885  1.00 56.80 ? 228  ASP B OD2 1 
ATOM   5433 N  N   . SER B 2 230 ? -12.730 84.541  30.289  1.00 68.32 ? 230  SER B N   1 
ATOM   5434 C  CA  . SER B 2 230 ? -13.085 85.254  29.027  1.00 66.89 ? 230  SER B CA  1 
ATOM   5435 C  C   . SER B 2 230 ? -12.394 84.644  27.796  1.00 64.90 ? 230  SER B C   1 
ATOM   5436 O  O   . SER B 2 230 ? -12.721 85.085  26.678  1.00 66.36 ? 230  SER B O   1 
ATOM   5437 C  CB  . SER B 2 230 ? -12.767 86.722  29.132  1.00 66.19 ? 230  SER B CB  1 
ATOM   5438 O  OG  . SER B 2 230 ? -13.261 87.262  30.348  1.00 68.40 ? 230  SER B OG  1 
ATOM   5439 N  N   . GLY B 2 231 ? -11.453 83.709  27.978  1.00 63.15 ? 231  GLY B N   1 
ATOM   5440 C  CA  . GLY B 2 231 ? -10.737 83.030  26.878  1.00 60.87 ? 231  GLY B CA  1 
ATOM   5441 C  C   . GLY B 2 231 ? -9.472  83.766  26.450  1.00 60.76 ? 231  GLY B C   1 
ATOM   5442 O  O   . GLY B 2 231 ? -8.809  83.279  25.515  1.00 58.34 ? 231  GLY B O   1 
ATOM   5443 N  N   . GLU B 2 232 ? -9.113  84.862  27.132  1.00 59.44 ? 232  GLU B N   1 
ATOM   5444 C  CA  . GLU B 2 232 ? -8.056  85.820  26.697  1.00 58.84 ? 232  GLU B CA  1 
ATOM   5445 C  C   . GLU B 2 232 ? -6.680  85.408  27.230  1.00 53.46 ? 232  GLU B C   1 
ATOM   5446 O  O   . GLU B 2 232 ? -6.512  85.156  28.425  1.00 48.11 ? 232  GLU B O   1 
ATOM   5447 C  CB  . GLU B 2 232 ? -8.408  87.238  27.153  1.00 61.69 ? 232  GLU B CB  1 
ATOM   5448 C  CG  . GLU B 2 232 ? -9.571  87.844  26.388  1.00 65.62 ? 232  GLU B CG  1 
ATOM   5449 C  CD  . GLU B 2 232 ? -9.203  88.350  25.003  1.00 67.59 ? 232  GLU B CD  1 
ATOM   5450 O  OE1 . GLU B 2 232 ? -8.394  89.295  24.924  1.00 70.43 ? 232  GLU B OE1 1 
ATOM   5451 O  OE2 . GLU B 2 232 ? -9.710  87.790  24.009  1.00 70.54 ? 232  GLU B OE2 1 
ATOM   5452 N  N   . PRO B 2 233 ? -5.646  85.351  26.354  1.00 50.58 ? 233  PRO B N   1 
ATOM   5453 C  CA  . PRO B 2 233 ? -4.259  85.181  26.793  1.00 47.29 ? 233  PRO B CA  1 
ATOM   5454 C  C   . PRO B 2 233 ? -3.635  86.516  27.232  1.00 42.14 ? 233  PRO B C   1 
ATOM   5455 O  O   . PRO B 2 233 ? -4.189  87.545  26.922  1.00 41.37 ? 233  PRO B O   1 
ATOM   5456 C  CB  . PRO B 2 233 ? -3.587  84.632  25.527  1.00 47.97 ? 233  PRO B CB  1 
ATOM   5457 C  CG  . PRO B 2 233 ? -4.322  85.331  24.403  1.00 48.08 ? 233  PRO B CG  1 
ATOM   5458 C  CD  . PRO B 2 233 ? -5.753  85.452  24.887  1.00 49.35 ? 233  PRO B CD  1 
ATOM   5459 N  N   . LEU B 2 234 ? -2.509  86.474  27.948  1.00 39.37 ? 234  LEU B N   1 
ATOM   5460 C  CA  . LEU B 2 234 ? -1.835  87.701  28.452  1.00 38.59 ? 234  LEU B CA  1 
ATOM   5461 C  C   . LEU B 2 234 ? -0.831  88.167  27.398  1.00 38.28 ? 234  LEU B C   1 
ATOM   5462 O  O   . LEU B 2 234 ? 0.105   87.391  27.084  1.00 34.28 ? 234  LEU B O   1 
ATOM   5463 C  CB  . LEU B 2 234 ? -1.148  87.417  29.791  1.00 38.20 ? 234  LEU B CB  1 
ATOM   5464 C  CG  . LEU B 2 234 ? -0.394  88.594  30.406  1.00 39.70 ? 234  LEU B CG  1 
ATOM   5465 C  CD1 . LEU B 2 234 ? -1.334  89.758  30.712  1.00 39.23 ? 234  LEU B CD1 1 
ATOM   5466 C  CD2 . LEU B 2 234 ? 0.346   88.159  31.668  1.00 39.60 ? 234  LEU B CD2 1 
ATOM   5467 N  N   . ASP B 2 235 ? -1.035  89.382  26.877  1.00 36.97 ? 235  ASP B N   1 
ATOM   5468 C  CA  . ASP B 2 235 ? -0.149  90.015  25.869  1.00 37.54 ? 235  ASP B CA  1 
ATOM   5469 C  C   . ASP B 2 235 ? 1.097   90.550  26.580  1.00 37.02 ? 235  ASP B C   1 
ATOM   5470 O  O   . ASP B 2 235 ? 0.990   91.588  27.267  1.00 36.47 ? 235  ASP B O   1 
ATOM   5471 C  CB  . ASP B 2 235 ? -0.873  91.110  25.082  1.00 38.34 ? 235  ASP B CB  1 
ATOM   5472 C  CG  . ASP B 2 235 ? -0.112  91.536  23.840  1.00 40.14 ? 235  ASP B CG  1 
ATOM   5473 O  OD1 . ASP B 2 235 ? 1.133   91.648  23.927  1.00 37.97 ? 235  ASP B OD1 1 
ATOM   5474 O  OD2 . ASP B 2 235 ? -0.767  91.748  22.797  1.00 40.49 ? 235  ASP B OD2 1 
ATOM   5475 N  N   . LEU B 2 236 ? 2.238   89.887  26.362  1.00 36.02 ? 236  LEU B N   1 
ATOM   5476 C  CA  . LEU B 2 236 ? 3.549   90.201  26.991  1.00 34.80 ? 236  LEU B CA  1 
ATOM   5477 C  C   . LEU B 2 236 ? 4.455   90.976  26.023  1.00 34.12 ? 236  LEU B C   1 
ATOM   5478 O  O   . LEU B 2 236 ? 5.675   90.993  26.264  1.00 35.18 ? 236  LEU B O   1 
ATOM   5479 C  CB  . LEU B 2 236 ? 4.189   88.873  27.405  1.00 35.47 ? 236  LEU B CB  1 
ATOM   5480 C  CG  . LEU B 2 236 ? 3.407   88.062  28.438  1.00 35.67 ? 236  LEU B CG  1 
ATOM   5481 C  CD1 . LEU B 2 236 ? 4.048   86.695  28.642  1.00 35.57 ? 236  LEU B CD1 1 
ATOM   5482 C  CD2 . LEU B 2 236 ? 3.313   88.819  29.755  1.00 36.54 ? 236  LEU B CD2 1 
ATOM   5483 N  N   . SER B 2 237 ? 3.888   91.646  25.011  1.00 32.93 ? 237  SER B N   1 
ATOM   5484 C  CA  . SER B 2 237 ? 4.658   92.393  23.976  1.00 32.10 ? 237  SER B CA  1 
ATOM   5485 C  C   . SER B 2 237 ? 5.717   93.294  24.620  1.00 31.36 ? 237  SER B C   1 
ATOM   5486 O  O   . SER B 2 237 ? 6.811   93.427  24.038  1.00 33.01 ? 237  SER B O   1 
ATOM   5487 C  CB  . SER B 2 237 ? 3.752   93.211  23.092  1.00 33.08 ? 237  SER B CB  1 
ATOM   5488 O  OG  . SER B 2 237 ? 2.996   92.374  22.239  1.00 29.77 ? 237  SER B OG  1 
ATOM   5489 N  N   . TYR B 2 238 ? 5.393   93.938  25.741  1.00 31.33 ? 238  TYR B N   1 
ATOM   5490 C  CA  . TYR B 2 238 ? 6.252   94.969  26.384  1.00 31.97 ? 238  TYR B CA  1 
ATOM   5491 C  C   . TYR B 2 238 ? 6.858   94.443  27.692  1.00 31.23 ? 238  TYR B C   1 
ATOM   5492 O  O   . TYR B 2 238 ? 7.593   95.204  28.364  1.00 31.12 ? 238  TYR B O   1 
ATOM   5493 C  CB  . TYR B 2 238 ? 5.453   96.252  26.616  1.00 32.72 ? 238  TYR B CB  1 
ATOM   5494 C  CG  . TYR B 2 238 ? 5.058   96.986  25.361  1.00 33.41 ? 238  TYR B CG  1 
ATOM   5495 C  CD1 . TYR B 2 238 ? 5.952   97.817  24.705  1.00 34.43 ? 238  TYR B CD1 1 
ATOM   5496 C  CD2 . TYR B 2 238 ? 3.784   96.861  24.834  1.00 34.83 ? 238  TYR B CD2 1 
ATOM   5497 C  CE1 . TYR B 2 238 ? 5.591   98.503  23.556  1.00 35.65 ? 238  TYR B CE1 1 
ATOM   5498 C  CE2 . TYR B 2 238 ? 3.408   97.534  23.682  1.00 36.57 ? 238  TYR B CE2 1 
ATOM   5499 C  CZ  . TYR B 2 238 ? 4.310   98.369  23.050  1.00 37.74 ? 238  TYR B CZ  1 
ATOM   5500 O  OH  . TYR B 2 238 ? 3.943   99.031  21.914  1.00 41.22 ? 238  TYR B OH  1 
ATOM   5501 N  N   . ALA B 2 239 ? 6.572   93.190  28.055  1.00 29.92 ? 239  ALA B N   1 
ATOM   5502 C  CA  . ALA B 2 239 ? 7.166   92.531  29.243  1.00 31.27 ? 239  ALA B CA  1 
ATOM   5503 C  C   . ALA B 2 239 ? 8.589   92.064  28.897  1.00 30.38 ? 239  ALA B C   1 
ATOM   5504 O  O   . ALA B 2 239 ? 8.737   91.294  27.931  1.00 30.26 ? 239  ALA B O   1 
ATOM   5505 C  CB  . ALA B 2 239 ? 6.289   91.388  29.698  1.00 30.60 ? 239  ALA B CB  1 
ATOM   5506 N  N   . HIS B 2 240 ? 9.602   92.502  29.651  1.00 30.90 ? 240  HIS B N   1 
ATOM   5507 C  CA  . HIS B 2 240 ? 11.016  92.103  29.398  1.00 30.71 ? 240  HIS B CA  1 
ATOM   5508 C  C   . HIS B 2 240 ? 11.211  90.631  29.791  1.00 31.64 ? 240  HIS B C   1 
ATOM   5509 O  O   . HIS B 2 240 ? 12.138  90.001  29.235  1.00 32.58 ? 240  HIS B O   1 
ATOM   5510 C  CB  . HIS B 2 240 ? 12.006  93.069  30.064  1.00 30.98 ? 240  HIS B CB  1 
ATOM   5511 C  CG  . HIS B 2 240 ? 12.023  93.022  31.554  1.00 31.81 ? 240  HIS B CG  1 
ATOM   5512 N  ND1 . HIS B 2 240 ? 12.796  92.116  32.250  1.00 31.08 ? 240  HIS B ND1 1 
ATOM   5513 C  CD2 . HIS B 2 240 ? 11.395  93.783  32.479  1.00 31.93 ? 240  HIS B CD2 1 
ATOM   5514 C  CE1 . HIS B 2 240 ? 12.628  92.306  33.549  1.00 33.87 ? 240  HIS B CE1 1 
ATOM   5515 N  NE2 . HIS B 2 240 ? 11.769  93.319  33.717  1.00 32.24 ? 240  HIS B NE2 1 
ATOM   5516 N  N   . LEU B 2 241 ? 10.355  90.088  30.672  1.00 28.55 ? 241  LEU B N   1 
ATOM   5517 C  CA  . LEU B 2 241 ? 10.446  88.679  31.137  1.00 28.82 ? 241  LEU B CA  1 
ATOM   5518 C  C   . LEU B 2 241 ? 9.784   87.713  30.147  1.00 28.77 ? 241  LEU B C   1 
ATOM   5519 O  O   . LEU B 2 241 ? 9.876   86.497  30.394  1.00 26.71 ? 241  LEU B O   1 
ATOM   5520 C  CB  . LEU B 2 241 ? 9.785   88.549  32.512  1.00 29.16 ? 241  LEU B CB  1 
ATOM   5521 C  CG  . LEU B 2 241 ? 10.465  89.303  33.648  1.00 28.59 ? 241  LEU B CG  1 
ATOM   5522 C  CD1 . LEU B 2 241 ? 9.670   89.143  34.937  1.00 28.58 ? 241  LEU B CD1 1 
ATOM   5523 C  CD2 . LEU B 2 241 ? 11.901  88.831  33.841  1.00 28.91 ? 241  LEU B CD2 1 
ATOM   5524 N  N   . ARG B 2 242 ? 9.126   88.209  29.092  1.00 27.84 ? 242  ARG B N   1 
ATOM   5525 C  CA  . ARG B 2 242 ? 8.436   87.332  28.100  1.00 28.27 ? 242  ARG B CA  1 
ATOM   5526 C  C   . ARG B 2 242 ? 9.349   86.173  27.662  1.00 29.18 ? 242  ARG B C   1 
ATOM   5527 O  O   . ARG B 2 242 ? 10.512  86.442  27.288  1.00 26.38 ? 242  ARG B O   1 
ATOM   5528 C  CB  . ARG B 2 242 ? 7.993   88.159  26.895  1.00 28.74 ? 242  ARG B CB  1 
ATOM   5529 C  CG  . ARG B 2 242 ? 7.319   87.355  25.793  1.00 29.30 ? 242  ARG B CG  1 
ATOM   5530 C  CD  . ARG B 2 242 ? 6.800   88.287  24.714  1.00 29.60 ? 242  ARG B CD  1 
ATOM   5531 N  NE  . ARG B 2 242 ? 7.838   89.206  24.261  1.00 32.22 ? 242  ARG B NE  1 
ATOM   5532 C  CZ  . ARG B 2 242 ? 8.654   89.005  23.226  1.00 33.29 ? 242  ARG B CZ  1 
ATOM   5533 N  NH1 . ARG B 2 242 ? 9.568   89.916  22.920  1.00 33.85 ? 242  ARG B NH1 1 
ATOM   5534 N  NH2 . ARG B 2 242 ? 8.544   87.919  22.481  1.00 35.00 ? 242  ARG B NH2 1 
ATOM   5535 N  N   . SER B 2 243 ? 8.818   84.940  27.643  1.00 28.61 ? 243  SER B N   1 
ATOM   5536 C  CA  . SER B 2 243 ? 9.557   83.711  27.244  1.00 28.06 ? 243  SER B CA  1 
ATOM   5537 C  C   . SER B 2 243 ? 9.907   83.770  25.752  1.00 27.26 ? 243  SER B C   1 
ATOM   5538 O  O   . SER B 2 243 ? 9.390   84.641  25.021  1.00 26.20 ? 243  SER B O   1 
ATOM   5539 C  CB  . SER B 2 243 ? 8.794   82.446  27.587  1.00 29.65 ? 243  SER B CB  1 
ATOM   5540 O  OG  . SER B 2 243 ? 7.637   82.308  26.773  1.00 32.03 ? 243  SER B OG  1 
ATOM   5541 N  N   . VAL B 2 244 ? 10.783  82.865  25.331  1.00 27.71 ? 244  VAL B N   1 
ATOM   5542 C  CA  . VAL B 2 244 ? 11.416  82.863  23.985  1.00 28.81 ? 244  VAL B CA  1 
ATOM   5543 C  C   . VAL B 2 244 ? 10.840  81.705  23.185  1.00 28.11 ? 244  VAL B C   1 
ATOM   5544 O  O   . VAL B 2 244 ? 10.613  80.643  23.787  1.00 28.02 ? 244  VAL B O   1 
ATOM   5545 C  CB  . VAL B 2 244 ? 12.944  82.727  24.093  1.00 28.55 ? 244  VAL B CB  1 
ATOM   5546 C  CG1 . VAL B 2 244 ? 13.606  82.755  22.724  1.00 29.92 ? 244  VAL B CG1 1 
ATOM   5547 C  CG2 . VAL B 2 244 ? 13.523  83.785  25.007  1.00 29.38 ? 244  VAL B CG2 1 
ATOM   5548 N  N   . SER B 2 245 ? 10.639  81.922  21.882  1.00 29.75 ? 245  SER B N   1 
ATOM   5549 C  CA  . SER B 2 245 ? 10.258  80.860  20.914  1.00 30.10 ? 245  SER B CA  1 
ATOM   5550 C  C   . SER B 2 245 ? 11.169  79.650  21.079  1.00 30.69 ? 245  SER B C   1 
ATOM   5551 O  O   . SER B 2 245 ? 12.391  79.787  21.053  1.00 32.66 ? 245  SER B O   1 
ATOM   5552 C  CB  . SER B 2 245 ? 10.303  81.342  19.495  1.00 30.48 ? 245  SER B CB  1 
ATOM   5553 O  OG  . SER B 2 245 ? 10.294  80.228  18.612  1.00 30.27 ? 245  SER B OG  1 
ATOM   5554 N  N   . PRO B 2 246 ? 10.603  78.428  21.217  1.00 32.28 ? 246  PRO B N   1 
ATOM   5555 C  CA  . PRO B 2 246 ? 11.399  77.199  21.167  1.00 31.18 ? 246  PRO B CA  1 
ATOM   5556 C  C   . PRO B 2 246 ? 12.318  77.114  19.939  1.00 29.34 ? 246  PRO B C   1 
ATOM   5557 O  O   . PRO B 2 246 ? 13.362  76.518  20.033  1.00 30.49 ? 246  PRO B O   1 
ATOM   5558 C  CB  . PRO B 2 246 ? 10.339  76.082  21.100  1.00 32.46 ? 246  PRO B CB  1 
ATOM   5559 C  CG  . PRO B 2 246 ? 9.112   76.685  21.766  1.00 33.99 ? 246  PRO B CG  1 
ATOM   5560 C  CD  . PRO B 2 246 ? 9.169   78.166  21.442  1.00 32.84 ? 246  PRO B CD  1 
ATOM   5561 N  N   . ILE B 2 247 ? 11.897  77.676  18.804  1.00 29.27 ? 247  ILE B N   1 
ATOM   5562 C  CA  . ILE B 2 247 ? 12.691  77.650  17.539  1.00 27.89 ? 247  ILE B CA  1 
ATOM   5563 C  C   . ILE B 2 247 ? 14.012  78.389  17.770  1.00 27.03 ? 247  ILE B C   1 
ATOM   5564 O  O   . ILE B 2 247 ? 15.075  77.843  17.427  1.00 26.00 ? 247  ILE B O   1 
ATOM   5565 C  CB  . ILE B 2 247 ? 11.891  78.264  16.378  1.00 29.27 ? 247  ILE B CB  1 
ATOM   5566 C  CG1 . ILE B 2 247 ? 10.692  77.394  15.993  1.00 31.26 ? 247  ILE B CG1 1 
ATOM   5567 C  CG2 . ILE B 2 247 ? 12.794  78.547  15.188  1.00 29.68 ? 247  ILE B CG2 1 
ATOM   5568 C  CD1 . ILE B 2 247 ? 11.048  75.993  15.543  1.00 32.98 ? 247  ILE B CD1 1 
ATOM   5569 N  N   . HIS B 2 248 ? 13.945  79.603  18.317  1.00 26.62 ? 248  HIS B N   1 
ATOM   5570 C  CA  . HIS B 2 248 ? 15.146  80.451  18.542  1.00 26.81 ? 248  HIS B CA  1 
ATOM   5571 C  C   . HIS B 2 248 ? 16.021  79.855  19.649  1.00 26.07 ? 248  HIS B C   1 
ATOM   5572 O  O   . HIS B 2 248 ? 17.259  79.934  19.529  1.00 25.59 ? 248  HIS B O   1 
ATOM   5573 C  CB  . HIS B 2 248 ? 14.764  81.900  18.846  1.00 25.91 ? 248  HIS B CB  1 
ATOM   5574 C  CG  . HIS B 2 248 ? 15.965  82.770  18.943  1.00 25.25 ? 248  HIS B CG  1 
ATOM   5575 N  ND1 . HIS B 2 248 ? 16.872  82.865  17.914  1.00 25.01 ? 248  HIS B ND1 1 
ATOM   5576 C  CD2 . HIS B 2 248 ? 16.441  83.535  19.950  1.00 25.40 ? 248  HIS B CD2 1 
ATOM   5577 C  CE1 . HIS B 2 248 ? 17.844  83.681  18.266  1.00 25.46 ? 248  HIS B CE1 1 
ATOM   5578 N  NE2 . HIS B 2 248 ? 17.602  84.108  19.509  1.00 24.43 ? 248  HIS B NE2 1 
ATOM   5579 N  N   . CYS B 2 249 ? 15.408  79.286  20.691  1.00 27.64 ? 249  CYS B N   1 
ATOM   5580 C  CA  . CYS B 2 249 ? 16.148  78.623  21.800  1.00 28.76 ? 249  CYS B CA  1 
ATOM   5581 C  C   . CYS B 2 249 ? 16.946  77.443  21.230  1.00 28.53 ? 249  CYS B C   1 
ATOM   5582 O  O   . CYS B 2 249 ? 18.096  77.242  21.662  1.00 27.74 ? 249  CYS B O   1 
ATOM   5583 C  CB  . CYS B 2 249 ? 15.204  78.163  22.905  1.00 30.30 ? 249  CYS B CB  1 
ATOM   5584 S  SG  . CYS B 2 249 ? 14.530  79.538  23.873  1.00 34.77 ? 249  CYS B SG  1 
ATOM   5585 N  N   . GLU B 2 250 ? 16.366  76.704  20.280  1.00 27.31 ? 250  GLU B N   1 
ATOM   5586 C  CA  . GLU B 2 250 ? 17.050  75.560  19.625  1.00 28.04 ? 250  GLU B CA  1 
ATOM   5587 C  C   . GLU B 2 250 ? 18.202  76.109  18.780  1.00 26.81 ? 250  GLU B C   1 
ATOM   5588 O  O   . GLU B 2 250 ? 19.310  75.538  18.822  1.00 26.30 ? 250  GLU B O   1 
ATOM   5589 C  CB  . GLU B 2 250 ? 16.060  74.747  18.791  1.00 28.96 ? 250  GLU B CB  1 
ATOM   5590 C  CG  . GLU B 2 250 ? 16.688  73.538  18.125  1.00 30.45 ? 250  GLU B CG  1 
ATOM   5591 C  CD  . GLU B 2 250 ? 15.701  72.462  17.681  1.00 32.42 ? 250  GLU B CD  1 
ATOM   5592 O  OE1 . GLU B 2 250 ? 15.994  71.779  16.685  1.00 35.83 ? 250  GLU B OE1 1 
ATOM   5593 O  OE2 . GLU B 2 250 ? 14.653  72.299  18.337  1.00 33.51 ? 250  GLU B OE2 1 
ATOM   5594 N  N   . TYR B 2 251 ? 17.949  77.181  18.033  1.00 26.07 ? 251  TYR B N   1 
ATOM   5595 C  CA  . TYR B 2 251 ? 18.979  77.848  17.198  1.00 25.50 ? 251  TYR B CA  1 
ATOM   5596 C  C   . TYR B 2 251 ? 20.167  78.220  18.094  1.00 23.91 ? 251  TYR B C   1 
ATOM   5597 O  O   . TYR B 2 251 ? 21.314  77.839  17.773  1.00 23.47 ? 251  TYR B O   1 
ATOM   5598 C  CB  . TYR B 2 251 ? 18.407  79.063  16.461  1.00 25.44 ? 251  TYR B CB  1 
ATOM   5599 C  CG  . TYR B 2 251 ? 19.225  79.455  15.260  1.00 26.07 ? 251  TYR B CG  1 
ATOM   5600 C  CD1 . TYR B 2 251 ? 20.535  79.885  15.404  1.00 26.85 ? 251  TYR B CD1 1 
ATOM   5601 C  CD2 . TYR B 2 251 ? 18.705  79.375  13.980  1.00 26.07 ? 251  TYR B CD2 1 
ATOM   5602 C  CE1 . TYR B 2 251 ? 21.301  80.243  14.309  1.00 27.06 ? 251  TYR B CE1 1 
ATOM   5603 C  CE2 . TYR B 2 251 ? 19.463  79.712  12.872  1.00 25.59 ? 251  TYR B CE2 1 
ATOM   5604 C  CZ  . TYR B 2 251 ? 20.766  80.144  13.039  1.00 27.09 ? 251  TYR B CZ  1 
ATOM   5605 O  OH  . TYR B 2 251 ? 21.523  80.486  11.963  1.00 27.48 ? 251  TYR B OH  1 
ATOM   5606 N  N   . LEU B 2 252 ? 19.900  78.940  19.184  1.00 24.04 ? 252  LEU B N   1 
ATOM   5607 C  CA  . LEU B 2 252 ? 20.941  79.392  20.149  1.00 25.07 ? 252  LEU B CA  1 
ATOM   5608 C  C   . LEU B 2 252 ? 21.668  78.173  20.738  1.00 26.73 ? 252  LEU B C   1 
ATOM   5609 O  O   . LEU B 2 252 ? 22.913  78.196  20.741  1.00 26.71 ? 252  LEU B O   1 
ATOM   5610 C  CB  . LEU B 2 252 ? 20.310  80.256  21.244  1.00 23.95 ? 252  LEU B CB  1 
ATOM   5611 C  CG  . LEU B 2 252 ? 19.813  81.636  20.812  1.00 23.44 ? 252  LEU B CG  1 
ATOM   5612 C  CD1 . LEU B 2 252 ? 19.308  82.415  22.012  1.00 23.47 ? 252  LEU B CD1 1 
ATOM   5613 C  CD2 . LEU B 2 252 ? 20.887  82.429  20.085  1.00 23.03 ? 252  LEU B CD2 1 
ATOM   5614 N  N   . ARG B 2 253 ? 20.944  77.140  21.196  1.00 27.23 ? 253  ARG B N   1 
ATOM   5615 C  CA  . ARG B 2 253 ? 21.590  75.914  21.760  1.00 28.72 ? 253  ARG B CA  1 
ATOM   5616 C  C   . ARG B 2 253 ? 22.539  75.290  20.721  1.00 26.61 ? 253  ARG B C   1 
ATOM   5617 O  O   . ARG B 2 253 ? 23.658  74.931  21.105  1.00 25.32 ? 253  ARG B O   1 
ATOM   5618 C  CB  . ARG B 2 253 ? 20.555  74.895  22.240  1.00 30.56 ? 253  ARG B CB  1 
ATOM   5619 C  CG  . ARG B 2 253 ? 19.940  75.237  23.588  1.00 33.63 ? 253  ARG B CG  1 
ATOM   5620 C  CD  . ARG B 2 253 ? 19.163  74.058  24.149  1.00 36.33 ? 253  ARG B CD  1 
ATOM   5621 N  NE  . ARG B 2 253 ? 18.039  73.690  23.294  1.00 38.41 ? 253  ARG B NE  1 
ATOM   5622 C  CZ  . ARG B 2 253 ? 16.814  74.199  23.378  1.00 37.64 ? 253  ARG B CZ  1 
ATOM   5623 N  NH1 . ARG B 2 253 ? 16.522  75.116  24.283  1.00 40.13 ? 253  ARG B NH1 1 
ATOM   5624 N  NH2 . ARG B 2 253 ? 15.880  73.791  22.544  1.00 41.44 ? 253  ARG B NH2 1 
ATOM   5625 N  N   . ASN B 2 254 ? 22.133  75.203  19.450  1.00 25.90 ? 254  ASN B N   1 
ATOM   5626 C  CA  . ASN B 2 254 ? 22.987  74.683  18.345  1.00 27.01 ? 254  ASN B CA  1 
ATOM   5627 C  C   . ASN B 2 254 ? 24.284  75.503  18.235  1.00 27.36 ? 254  ASN B C   1 
ATOM   5628 O  O   . ASN B 2 254 ? 25.350  74.902  17.974  1.00 27.28 ? 254  ASN B O   1 
ATOM   5629 C  CB  . ASN B 2 254 ? 22.245  74.650  17.005  1.00 28.21 ? 254  ASN B CB  1 
ATOM   5630 C  CG  . ASN B 2 254 ? 21.099  73.658  16.980  1.00 30.98 ? 254  ASN B CG  1 
ATOM   5631 O  OD1 . ASN B 2 254 ? 21.022  72.762  17.821  1.00 32.52 ? 254  ASN B OD1 1 
ATOM   5632 N  ND2 . ASN B 2 254 ? 20.201  73.810  16.021  1.00 31.66 ? 254  ASN B ND2 1 
ATOM   5633 N  N   . MET B 2 255 ? 24.201  76.823  18.404  1.00 25.65 ? 255  MET B N   1 
ATOM   5634 C  CA  . MET B 2 255 ? 25.372  77.735  18.333  1.00 26.30 ? 255  MET B CA  1 
ATOM   5635 C  C   . MET B 2 255 ? 26.270  77.530  19.562  1.00 26.15 ? 255  MET B C   1 
ATOM   5636 O  O   . MET B 2 255 ? 27.446  77.883  19.486  1.00 27.40 ? 255  MET B O   1 
ATOM   5637 C  CB  . MET B 2 255 ? 24.917  79.197  18.294  1.00 25.91 ? 255  MET B CB  1 
ATOM   5638 C  CG  . MET B 2 255 ? 24.237  79.599  16.999  1.00 24.79 ? 255  MET B CG  1 
ATOM   5639 S  SD  . MET B 2 255 ? 23.696  81.318  17.078  1.00 26.17 ? 255  MET B SD  1 
ATOM   5640 C  CE  . MET B 2 255 ? 25.261  82.165  16.896  1.00 25.86 ? 255  MET B CE  1 
ATOM   5641 N  N   . GLY B 2 256 ? 25.715  77.024  20.662  1.00 25.13 ? 256  GLY B N   1 
ATOM   5642 C  CA  . GLY B 2 256 ? 26.371  77.012  21.981  1.00 26.11 ? 256  GLY B CA  1 
ATOM   5643 C  C   . GLY B 2 256 ? 26.077  78.276  22.768  1.00 25.56 ? 256  GLY B C   1 
ATOM   5644 O  O   . GLY B 2 256 ? 26.624  78.410  23.856  1.00 25.25 ? 256  GLY B O   1 
ATOM   5645 N  N   . VAL B 2 257 ? 25.232  79.170  22.242  1.00 26.13 ? 257  VAL B N   1 
ATOM   5646 C  CA  . VAL B 2 257 ? 24.807  80.413  22.947  1.00 25.69 ? 257  VAL B CA  1 
ATOM   5647 C  C   . VAL B 2 257 ? 23.776  80.022  24.005  1.00 24.96 ? 257  VAL B C   1 
ATOM   5648 O  O   . VAL B 2 257 ? 22.910  79.203  23.694  1.00 24.42 ? 257  VAL B O   1 
ATOM   5649 C  CB  . VAL B 2 257 ? 24.259  81.466  21.971  1.00 24.88 ? 257  VAL B CB  1 
ATOM   5650 C  CG1 . VAL B 2 257 ? 23.687  82.667  22.706  1.00 24.05 ? 257  VAL B CG1 1 
ATOM   5651 C  CG2 . VAL B 2 257 ? 25.327  81.899  20.974  1.00 25.95 ? 257  VAL B CG2 1 
ATOM   5652 N  N   . ALA B 2 258 ? 23.917  80.564  25.218  1.00 24.73 ? 258  ALA B N   1 
ATOM   5653 C  CA  . ALA B 2 258 ? 23.048  80.279  26.387  1.00 24.77 ? 258  ALA B CA  1 
ATOM   5654 C  C   . ALA B 2 258 ? 22.217  81.517  26.728  1.00 24.95 ? 258  ALA B C   1 
ATOM   5655 O  O   . ALA B 2 258 ? 21.171  81.356  27.369  1.00 27.03 ? 258  ALA B O   1 
ATOM   5656 C  CB  . ALA B 2 258 ? 23.894  79.853  27.565  1.00 24.48 ? 258  ALA B CB  1 
ATOM   5657 N  N   . ALA B 2 259 ? 22.661  82.711  26.329  1.00 22.84 ? 259  ALA B N   1 
ATOM   5658 C  CA  . ALA B 2 259 ? 22.013  83.977  26.731  1.00 23.11 ? 259  ALA B CA  1 
ATOM   5659 C  C   . ALA B 2 259 ? 22.293  85.077  25.702  1.00 24.09 ? 259  ALA B C   1 
ATOM   5660 O  O   . ALA B 2 259 ? 23.273  84.967  24.912  1.00 22.89 ? 259  ALA B O   1 
ATOM   5661 C  CB  . ALA B 2 259 ? 22.483  84.359  28.112  1.00 23.31 ? 259  ALA B CB  1 
ATOM   5662 N  N   . SER B 2 260 ? 21.451  86.105  25.687  1.00 24.55 ? 260  SER B N   1 
ATOM   5663 C  CA  . SER B 2 260 ? 21.621  87.239  24.748  1.00 23.51 ? 260  SER B CA  1 
ATOM   5664 C  C   . SER B 2 260 ? 20.993  88.509  25.312  1.00 23.78 ? 260  SER B C   1 
ATOM   5665 O  O   . SER B 2 260 ? 20.115  88.426  26.203  1.00 22.26 ? 260  SER B O   1 
ATOM   5666 C  CB  . SER B 2 260 ? 21.081  86.906  23.373  1.00 24.66 ? 260  SER B CB  1 
ATOM   5667 O  OG  . SER B 2 260 ? 19.660  86.800  23.361  1.00 24.95 ? 260  SER B OG  1 
ATOM   5668 N  N   . MET B 2 261 ? 21.461  89.649  24.812  1.00 24.52 ? 261  MET B N   1 
ATOM   5669 C  CA  . MET B 2 261 ? 20.717  90.926  24.889  1.00 26.11 ? 261  MET B CA  1 
ATOM   5670 C  C   . MET B 2 261 ? 20.937  91.696  23.590  1.00 25.20 ? 261  MET B C   1 
ATOM   5671 O  O   . MET B 2 261 ? 22.091  91.839  23.184  1.00 25.95 ? 261  MET B O   1 
ATOM   5672 C  CB  . MET B 2 261 ? 21.149  91.783  26.079  1.00 27.90 ? 261  MET B CB  1 
ATOM   5673 C  CG  . MET B 2 261 ? 20.083  92.790  26.436  1.00 29.04 ? 261  MET B CG  1 
ATOM   5674 S  SD  . MET B 2 261 ? 20.599  94.009  27.637  1.00 33.56 ? 261  MET B SD  1 
ATOM   5675 C  CE  . MET B 2 261 ? 21.811  94.911  26.674  1.00 32.43 ? 261  MET B CE  1 
ATOM   5676 N  N   . SER B 2 262 ? 19.858  92.130  22.941  1.00 26.61 ? 262  SER B N   1 
ATOM   5677 C  CA  . SER B 2 262 ? 19.932  92.962  21.712  1.00 25.74 ? 262  SER B CA  1 
ATOM   5678 C  C   . SER B 2 262 ? 19.512  94.399  22.050  1.00 26.05 ? 262  SER B C   1 
ATOM   5679 O  O   . SER B 2 262 ? 18.602  94.598  22.888  1.00 25.47 ? 262  SER B O   1 
ATOM   5680 C  CB  . SER B 2 262 ? 19.135  92.361  20.587  1.00 26.71 ? 262  SER B CB  1 
ATOM   5681 O  OG  . SER B 2 262 ? 17.756  92.286  20.909  1.00 28.49 ? 262  SER B OG  1 
ATOM   5682 N  N   . ILE B 2 263 ? 20.224  95.361  21.478  1.00 25.50 ? 263  ILE B N   1 
ATOM   5683 C  CA  . ILE B 2 263 ? 19.865  96.803  21.472  1.00 24.99 ? 263  ILE B CA  1 
ATOM   5684 C  C   . ILE B 2 263 ? 19.381  97.108  20.056  1.00 25.03 ? 263  ILE B C   1 
ATOM   5685 O  O   . ILE B 2 263 ? 20.190  96.997  19.121  1.00 24.42 ? 263  ILE B O   1 
ATOM   5686 C  CB  . ILE B 2 263 ? 21.062  97.683  21.872  1.00 25.80 ? 263  ILE B CB  1 
ATOM   5687 C  CG1 . ILE B 2 263 ? 21.762  97.154  23.128  1.00 27.02 ? 263  ILE B CG1 1 
ATOM   5688 C  CG2 . ILE B 2 263 ? 20.624  99.129  22.023  1.00 26.26 ? 263  ILE B CG2 1 
ATOM   5689 C  CD1 . ILE B 2 263 ? 23.095  97.805  23.418  1.00 27.80 ? 263  ILE B CD1 1 
ATOM   5690 N  N   . SER B 2 264 ? 18.108  97.459  19.904  1.00 25.37 ? 264  SER B N   1 
ATOM   5691 C  CA  . SER B 2 264 ? 17.521  97.777  18.573  1.00 26.65 ? 264  SER B CA  1 
ATOM   5692 C  C   . SER B 2 264 ? 18.117  99.098  18.071  1.00 27.79 ? 264  SER B C   1 
ATOM   5693 O  O   . SER B 2 264 ? 18.280  100.014 18.897  1.00 28.86 ? 264  SER B O   1 
ATOM   5694 C  CB  . SER B 2 264 ? 16.033  97.796  18.649  1.00 26.09 ? 264  SER B CB  1 
ATOM   5695 O  OG  . SER B 2 264 ? 15.562  96.479  18.875  1.00 25.69 ? 264  SER B OG  1 
ATOM   5696 N  N   . VAL B 2 265 ? 18.523  99.163  16.801  1.00 29.19 ? 265  VAL B N   1 
ATOM   5697 C  CA  . VAL B 2 265 ? 19.012  100.422 16.167  1.00 30.19 ? 265  VAL B CA  1 
ATOM   5698 C  C   . VAL B 2 265 ? 17.882  100.959 15.285  1.00 31.43 ? 265  VAL B C   1 
ATOM   5699 O  O   . VAL B 2 265 ? 17.543  100.288 14.290  1.00 29.41 ? 265  VAL B O   1 
ATOM   5700 C  CB  . VAL B 2 265 ? 20.316  100.236 15.373  1.00 30.06 ? 265  VAL B CB  1 
ATOM   5701 C  CG1 . VAL B 2 265 ? 20.809  101.564 14.810  1.00 30.72 ? 265  VAL B CG1 1 
ATOM   5702 C  CG2 . VAL B 2 265 ? 21.408  99.576  16.202  1.00 29.60 ? 265  VAL B CG2 1 
ATOM   5703 N  N   . ILE B 2 266 ? 17.307  102.098 15.681  1.00 33.94 ? 266  ILE B N   1 
ATOM   5704 C  CA  . ILE B 2 266 ? 16.124  102.736 15.034  1.00 37.10 ? 266  ILE B CA  1 
ATOM   5705 C  C   . ILE B 2 266 ? 16.615  103.971 14.284  1.00 39.32 ? 266  ILE B C   1 
ATOM   5706 O  O   . ILE B 2 266 ? 17.152  104.872 14.942  1.00 38.70 ? 266  ILE B O   1 
ATOM   5707 C  CB  . ILE B 2 266 ? 15.031  103.098 16.060  1.00 38.92 ? 266  ILE B CB  1 
ATOM   5708 C  CG1 . ILE B 2 266 ? 14.653  101.902 16.935  1.00 39.78 ? 266  ILE B CG1 1 
ATOM   5709 C  CG2 . ILE B 2 266 ? 13.808  103.689 15.367  1.00 39.90 ? 266  ILE B CG2 1 
ATOM   5710 C  CD1 . ILE B 2 266 ? 14.240  100.679 16.155  1.00 40.49 ? 266  ILE B CD1 1 
ATOM   5711 N  N   . VAL B 2 267 ? 16.450  103.970 12.960  1.00 42.36 ? 267  VAL B N   1 
ATOM   5712 C  CA  . VAL B 2 267 ? 16.761  105.111 12.048  1.00 44.54 ? 267  VAL B CA  1 
ATOM   5713 C  C   . VAL B 2 267 ? 15.513  105.385 11.200  1.00 48.58 ? 267  VAL B C   1 
ATOM   5714 O  O   . VAL B 2 267 ? 14.975  104.427 10.603  1.00 46.70 ? 267  VAL B O   1 
ATOM   5715 C  CB  . VAL B 2 267 ? 18.002  104.809 11.187  1.00 45.80 ? 267  VAL B CB  1 
ATOM   5716 C  CG1 . VAL B 2 267 ? 18.201  105.834 10.079  1.00 48.64 ? 267  VAL B CG1 1 
ATOM   5717 C  CG2 . VAL B 2 267 ? 19.254  104.693 12.042  1.00 45.25 ? 267  VAL B CG2 1 
ATOM   5718 N  N   . ASP B 2 268 ? 15.040  106.636 11.198  1.00 51.61 ? 268  ASP B N   1 
ATOM   5719 C  CA  . ASP B 2 268 ? 13.823  107.068 10.457  1.00 51.83 ? 268  ASP B CA  1 
ATOM   5720 C  C   . ASP B 2 268 ? 12.627  106.231 10.930  1.00 47.92 ? 268  ASP B C   1 
ATOM   5721 O  O   . ASP B 2 268 ? 11.781  105.881 10.098  1.00 50.76 ? 268  ASP B O   1 
ATOM   5722 C  CB  . ASP B 2 268 ? 14.049  106.970 8.943   1.00 53.84 ? 268  ASP B CB  1 
ATOM   5723 C  CG  . ASP B 2 268 ? 15.160  107.880 8.432   1.00 59.34 ? 268  ASP B CG  1 
ATOM   5724 O  OD1 . ASP B 2 268 ? 15.347  108.958 9.032   1.00 60.12 ? 268  ASP B OD1 1 
ATOM   5725 O  OD2 . ASP B 2 268 ? 15.834  107.509 7.434   1.00 57.22 ? 268  ASP B OD2 1 
ATOM   5726 N  N   . GLY B 2 269 ? 12.568  105.908 12.222  1.00 45.51 ? 269  GLY B N   1 
ATOM   5727 C  CA  . GLY B 2 269 ? 11.469  105.131 12.831  1.00 41.90 ? 269  GLY B CA  1 
ATOM   5728 C  C   . GLY B 2 269 ? 11.398  103.703 12.312  1.00 39.11 ? 269  GLY B C   1 
ATOM   5729 O  O   . GLY B 2 269 ? 10.365  103.051 12.537  1.00 37.54 ? 269  GLY B O   1 
ATOM   5730 N  N   . ALA B 2 270 ? 12.460  103.227 11.655  1.00 36.77 ? 270  ALA B N   1 
ATOM   5731 C  CA  . ALA B 2 270 ? 12.577  101.866 11.082  1.00 36.34 ? 270  ALA B CA  1 
ATOM   5732 C  C   . ALA B 2 270 ? 13.755  101.129 11.736  1.00 33.73 ? 270  ALA B C   1 
ATOM   5733 O  O   . ALA B 2 270 ? 14.702  101.791 12.191  1.00 31.10 ? 270  ALA B O   1 
ATOM   5734 C  CB  . ALA B 2 270 ? 12.759  101.964 9.588   1.00 36.98 ? 270  ALA B CB  1 
ATOM   5735 N  N   . LEU B 2 271 ? 13.703  99.799  11.745  1.00 32.05 ? 271  LEU B N   1 
ATOM   5736 C  CA  . LEU B 2 271 ? 14.740  98.938  12.365  1.00 30.53 ? 271  LEU B CA  1 
ATOM   5737 C  C   . LEU B 2 271 ? 15.950  98.870  11.429  1.00 28.84 ? 271  LEU B C   1 
ATOM   5738 O  O   . LEU B 2 271 ? 15.915  98.089  10.456  1.00 29.28 ? 271  LEU B O   1 
ATOM   5739 C  CB  . LEU B 2 271 ? 14.145  97.551  12.639  1.00 31.31 ? 271  LEU B CB  1 
ATOM   5740 C  CG  . LEU B 2 271 ? 15.031  96.610  13.457  1.00 31.02 ? 271  LEU B CG  1 
ATOM   5741 C  CD1 . LEU B 2 271 ? 15.336  97.202  14.826  1.00 29.36 ? 271  LEU B CD1 1 
ATOM   5742 C  CD2 . LEU B 2 271 ? 14.391  95.238  13.600  1.00 32.22 ? 271  LEU B CD2 1 
ATOM   5743 N  N   . TRP B 2 272 ? 16.981  99.669  11.708  1.00 26.73 ? 272  TRP B N   1 
ATOM   5744 C  CA  . TRP B 2 272 ? 18.237  99.713  10.913  1.00 26.07 ? 272  TRP B CA  1 
ATOM   5745 C  C   . TRP B 2 272 ? 19.007  98.394  11.088  1.00 25.11 ? 272  TRP B C   1 
ATOM   5746 O  O   . TRP B 2 272 ? 19.609  97.914  10.125  1.00 24.02 ? 272  TRP B O   1 
ATOM   5747 C  CB  . TRP B 2 272 ? 19.082  100.912 11.351  1.00 27.26 ? 272  TRP B CB  1 
ATOM   5748 C  CG  . TRP B 2 272 ? 20.390  101.051 10.631  1.00 26.90 ? 272  TRP B CG  1 
ATOM   5749 C  CD1 . TRP B 2 272 ? 20.630  101.756 9.488   1.00 26.61 ? 272  TRP B CD1 1 
ATOM   5750 C  CD2 . TRP B 2 272 ? 21.652  100.477 11.022  1.00 28.19 ? 272  TRP B CD2 1 
ATOM   5751 N  NE1 . TRP B 2 272 ? 21.951  101.661 9.142   1.00 27.04 ? 272  TRP B NE1 1 
ATOM   5752 C  CE2 . TRP B 2 272 ? 22.600  100.875 10.059  1.00 28.11 ? 272  TRP B CE2 1 
ATOM   5753 C  CE3 . TRP B 2 272 ? 22.068  99.664  12.085  1.00 29.43 ? 272  TRP B CE3 1 
ATOM   5754 C  CZ2 . TRP B 2 272 ? 23.939  100.491 10.138  1.00 29.78 ? 272  TRP B CZ2 1 
ATOM   5755 C  CZ3 . TRP B 2 272 ? 23.390  99.287  12.160  1.00 29.31 ? 272  TRP B CZ3 1 
ATOM   5756 C  CH2 . TRP B 2 272 ? 24.311  99.694  11.196  1.00 29.24 ? 272  TRP B CH2 1 
ATOM   5757 N  N   . GLY B 2 273 ? 19.015  97.866  12.312  1.00 25.07 ? 273  GLY B N   1 
ATOM   5758 C  CA  . GLY B 2 273 ? 19.828  96.705  12.707  1.00 23.85 ? 273  GLY B CA  1 
ATOM   5759 C  C   . GLY B 2 273 ? 19.752  96.493  14.200  1.00 23.25 ? 273  GLY B C   1 
ATOM   5760 O  O   . GLY B 2 273 ? 18.911  97.163  14.858  1.00 23.04 ? 273  GLY B O   1 
ATOM   5761 N  N   . LEU B 2 274 ? 20.606  95.608  14.710  1.00 22.12 ? 274  LEU B N   1 
ATOM   5762 C  CA  . LEU B 2 274 ? 20.697  95.269  16.154  1.00 23.23 ? 274  LEU B CA  1 
ATOM   5763 C  C   . LEU B 2 274 ? 22.158  95.326  16.584  1.00 21.84 ? 274  LEU B C   1 
ATOM   5764 O  O   . LEU B 2 274 ? 23.033  95.027  15.759  1.00 21.92 ? 274  LEU B O   1 
ATOM   5765 C  CB  . LEU B 2 274 ? 20.164  93.855  16.413  1.00 23.25 ? 274  LEU B CB  1 
ATOM   5766 C  CG  . LEU B 2 274 ? 18.732  93.568  15.990  1.00 23.44 ? 274  LEU B CG  1 
ATOM   5767 C  CD1 . LEU B 2 274 ? 18.458  92.074  16.114  1.00 23.86 ? 274  LEU B CD1 1 
ATOM   5768 C  CD2 . LEU B 2 274 ? 17.751  94.374  16.827  1.00 25.13 ? 274  LEU B CD2 1 
ATOM   5769 N  N   . ILE B 2 275 ? 22.382  95.714  17.835  1.00 22.08 ? 275  ILE B N   1 
ATOM   5770 C  CA  . ILE B 2 275 ? 23.617  95.381  18.589  1.00 22.73 ? 275  ILE B CA  1 
ATOM   5771 C  C   . ILE B 2 275 ? 23.248  94.131  19.387  1.00 23.49 ? 275  ILE B C   1 
ATOM   5772 O  O   . ILE B 2 275 ? 22.465  94.261  20.363  1.00 23.89 ? 275  ILE B O   1 
ATOM   5773 C  CB  . ILE B 2 275 ? 24.087  96.557  19.466  1.00 22.49 ? 275  ILE B CB  1 
ATOM   5774 C  CG1 . ILE B 2 275 ? 24.157  97.858  18.663  1.00 23.22 ? 275  ILE B CG1 1 
ATOM   5775 C  CG2 . ILE B 2 275 ? 25.409  96.225  20.140  1.00 23.59 ? 275  ILE B CG2 1 
ATOM   5776 C  CD1 . ILE B 2 275 ? 24.259  99.109  19.510  1.00 23.77 ? 275  ILE B CD1 1 
ATOM   5777 N  N   . ALA B 2 276 ? 23.696  92.969  18.907  1.00 22.70 ? 276  ALA B N   1 
ATOM   5778 C  CA  . ALA B 2 276 ? 23.375  91.635  19.462  1.00 22.43 ? 276  ALA B CA  1 
ATOM   5779 C  C   . ALA B 2 276 ? 24.512  91.211  20.381  1.00 22.83 ? 276  ALA B C   1 
ATOM   5780 O  O   . ALA B 2 276 ? 25.663  91.103  19.904  1.00 23.81 ? 276  ALA B O   1 
ATOM   5781 C  CB  . ALA B 2 276 ? 23.164  90.641  18.347  1.00 22.30 ? 276  ALA B CB  1 
ATOM   5782 N  N   . CYS B 2 277 ? 24.210  91.017  21.662  1.00 23.56 ? 277  CYS B N   1 
ATOM   5783 C  CA  . CYS B 2 277 ? 25.187  90.552  22.680  1.00 23.27 ? 277  CYS B CA  1 
ATOM   5784 C  C   . CYS B 2 277 ? 24.882  89.083  22.969  1.00 24.05 ? 277  CYS B C   1 
ATOM   5785 O  O   . CYS B 2 277 ? 23.741  88.805  23.379  1.00 22.39 ? 277  CYS B O   1 
ATOM   5786 C  CB  . CYS B 2 277 ? 25.109  91.394  23.949  1.00 24.10 ? 277  CYS B CB  1 
ATOM   5787 S  SG  . CYS B 2 277 ? 25.258  93.176  23.639  1.00 23.62 ? 277  CYS B SG  1 
ATOM   5788 N  N   . HIS B 2 278 ? 25.841  88.183  22.728  1.00 23.78 ? 278  HIS B N   1 
ATOM   5789 C  CA  . HIS B 2 278 ? 25.671  86.713  22.912  1.00 22.88 ? 278  HIS B CA  1 
ATOM   5790 C  C   . HIS B 2 278 ? 26.622  86.227  24.007  1.00 23.95 ? 278  HIS B C   1 
ATOM   5791 O  O   . HIS B 2 278 ? 27.802  86.632  23.994  1.00 23.51 ? 278  HIS B O   1 
ATOM   5792 C  CB  . HIS B 2 278 ? 25.908  85.946  21.605  1.00 22.90 ? 278  HIS B CB  1 
ATOM   5793 C  CG  . HIS B 2 278 ? 24.850  86.109  20.561  1.00 23.06 ? 278  HIS B CG  1 
ATOM   5794 N  ND1 . HIS B 2 278 ? 24.984  85.573  19.291  1.00 24.14 ? 278  HIS B ND1 1 
ATOM   5795 C  CD2 . HIS B 2 278 ? 23.654  86.733  20.576  1.00 24.06 ? 278  HIS B CD2 1 
ATOM   5796 C  CE1 . HIS B 2 278 ? 23.908  85.852  18.575  1.00 24.58 ? 278  HIS B CE1 1 
ATOM   5797 N  NE2 . HIS B 2 278 ? 23.078  86.568  19.337  1.00 24.14 ? 278  HIS B NE2 1 
ATOM   5798 N  N   . HIS B 2 279 ? 26.131  85.384  24.915  1.00 23.93 ? 279  HIS B N   1 
ATOM   5799 C  CA  . HIS B 2 279 ? 26.956  84.742  25.972  1.00 24.55 ? 279  HIS B CA  1 
ATOM   5800 C  C   . HIS B 2 279 ? 26.806  83.224  25.860  1.00 25.30 ? 279  HIS B C   1 
ATOM   5801 O  O   . HIS B 2 279 ? 25.692  82.779  25.531  1.00 26.16 ? 279  HIS B O   1 
ATOM   5802 C  CB  . HIS B 2 279 ? 26.574  85.264  27.363  1.00 23.69 ? 279  HIS B CB  1 
ATOM   5803 C  CG  . HIS B 2 279 ? 27.738  85.315  28.292  1.00 24.46 ? 279  HIS B CG  1 
ATOM   5804 N  ND1 . HIS B 2 279 ? 28.834  86.120  28.050  1.00 23.98 ? 279  HIS B ND1 1 
ATOM   5805 C  CD2 . HIS B 2 279 ? 27.994  84.672  29.452  1.00 25.58 ? 279  HIS B CD2 1 
ATOM   5806 C  CE1 . HIS B 2 279 ? 29.703  85.982  29.027  1.00 25.38 ? 279  HIS B CE1 1 
ATOM   5807 N  NE2 . HIS B 2 279 ? 29.212  85.105  29.896  1.00 25.46 ? 279  HIS B NE2 1 
ATOM   5808 N  N   . TYR B 2 280 ? 27.887  82.483  26.118  1.00 25.20 ? 280  TYR B N   1 
ATOM   5809 C  CA  . TYR B 2 280 ? 27.970  81.003  25.973  1.00 27.18 ? 280  TYR B CA  1 
ATOM   5810 C  C   . TYR B 2 280 ? 27.745  80.354  27.347  1.00 28.72 ? 280  TYR B C   1 
ATOM   5811 O  O   . TYR B 2 280 ? 28.082  79.188  27.547  1.00 28.69 ? 280  TYR B O   1 
ATOM   5812 C  CB  . TYR B 2 280 ? 29.279  80.643  25.265  1.00 25.69 ? 280  TYR B CB  1 
ATOM   5813 C  CG  . TYR B 2 280 ? 29.236  80.972  23.796  1.00 25.96 ? 280  TYR B CG  1 
ATOM   5814 C  CD1 . TYR B 2 280 ? 29.298  82.287  23.357  1.00 25.54 ? 280  TYR B CD1 1 
ATOM   5815 C  CD2 . TYR B 2 280 ? 29.059  79.981  22.839  1.00 25.81 ? 280  TYR B CD2 1 
ATOM   5816 C  CE1 . TYR B 2 280 ? 29.227  82.606  22.007  1.00 24.67 ? 280  TYR B CE1 1 
ATOM   5817 C  CE2 . TYR B 2 280 ? 28.972  80.286  21.488  1.00 24.48 ? 280  TYR B CE2 1 
ATOM   5818 C  CZ  . TYR B 2 280 ? 29.057  81.604  21.067  1.00 24.97 ? 280  TYR B CZ  1 
ATOM   5819 O  OH  . TYR B 2 280 ? 28.980  81.913  19.734  1.00 24.09 ? 280  TYR B OH  1 
ATOM   5820 N  N   . SER B 2 281 ? 27.147  81.118  28.262  1.00 29.05 ? 281  SER B N   1 
ATOM   5821 C  CA  . SER B 2 281 ? 26.727  80.679  29.616  1.00 29.51 ? 281  SER B CA  1 
ATOM   5822 C  C   . SER B 2 281 ? 25.554  81.561  30.049  1.00 29.41 ? 281  SER B C   1 
ATOM   5823 O  O   . SER B 2 281 ? 25.475  82.715  29.619  1.00 28.73 ? 281  SER B O   1 
ATOM   5824 C  CB  . SER B 2 281 ? 27.902  80.769  30.559  1.00 29.93 ? 281  SER B CB  1 
ATOM   5825 O  OG  . SER B 2 281 ? 27.547  80.299  31.841  1.00 33.73 ? 281  SER B OG  1 
ATOM   5826 N  N   . PRO B 2 282 ? 24.566  81.061  30.826  1.00 27.94 ? 282  PRO B N   1 
ATOM   5827 C  CA  . PRO B 2 282 ? 23.457  81.909  31.271  1.00 29.24 ? 282  PRO B CA  1 
ATOM   5828 C  C   . PRO B 2 282 ? 23.943  83.214  31.920  1.00 30.27 ? 282  PRO B C   1 
ATOM   5829 O  O   . PRO B 2 282 ? 24.881  83.189  32.693  1.00 32.74 ? 282  PRO B O   1 
ATOM   5830 C  CB  . PRO B 2 282 ? 22.689  81.011  32.250  1.00 29.07 ? 282  PRO B CB  1 
ATOM   5831 C  CG  . PRO B 2 282 ? 22.966  79.605  31.733  1.00 29.52 ? 282  PRO B CG  1 
ATOM   5832 C  CD  . PRO B 2 282 ? 24.406  79.659  31.254  1.00 29.05 ? 282  PRO B CD  1 
ATOM   5833 N  N   . ARG B 2 283 ? 23.293  84.324  31.564  1.00 30.35 ? 283  ARG B N   1 
ATOM   5834 C  CA  . ARG B 2 283 ? 23.795  85.710  31.761  1.00 30.69 ? 283  ARG B CA  1 
ATOM   5835 C  C   . ARG B 2 283 ? 22.602  86.654  31.700  1.00 30.96 ? 283  ARG B C   1 
ATOM   5836 O  O   . ARG B 2 283 ? 21.801  86.523  30.765  1.00 29.04 ? 283  ARG B O   1 
ATOM   5837 C  CB  . ARG B 2 283 ? 24.760  86.104  30.635  1.00 32.82 ? 283  ARG B CB  1 
ATOM   5838 C  CG  . ARG B 2 283 ? 25.324  87.515  30.720  1.00 33.73 ? 283  ARG B CG  1 
ATOM   5839 C  CD  . ARG B 2 283 ? 26.540  87.554  31.614  1.00 35.46 ? 283  ARG B CD  1 
ATOM   5840 N  NE  . ARG B 2 283 ? 27.244  88.827  31.618  1.00 36.74 ? 283  ARG B NE  1 
ATOM   5841 C  CZ  . ARG B 2 283 ? 26.970  89.851  32.418  1.00 37.31 ? 283  ARG B CZ  1 
ATOM   5842 N  NH1 . ARG B 2 283 ? 25.975  89.786  33.292  1.00 40.70 ? 283  ARG B NH1 1 
ATOM   5843 N  NH2 . ARG B 2 283 ? 27.719  90.935  32.363  1.00 36.76 ? 283  ARG B NH2 1 
ATOM   5844 N  N   . VAL B 2 284 ? 22.517  87.593  32.635  1.00 30.95 ? 284  VAL B N   1 
ATOM   5845 C  CA  . VAL B 2 284 ? 21.538  88.710  32.560  1.00 31.58 ? 284  VAL B CA  1 
ATOM   5846 C  C   . VAL B 2 284 ? 22.188  89.930  33.199  1.00 31.13 ? 284  VAL B C   1 
ATOM   5847 O  O   . VAL B 2 284 ? 22.908  89.756  34.203  1.00 35.06 ? 284  VAL B O   1 
ATOM   5848 C  CB  . VAL B 2 284 ? 20.200  88.337  33.226  1.00 31.75 ? 284  VAL B CB  1 
ATOM   5849 C  CG1 . VAL B 2 284 ? 20.361  88.081  34.721  1.00 32.64 ? 284  VAL B CG1 1 
ATOM   5850 C  CG2 . VAL B 2 284 ? 19.139  89.392  32.952  1.00 32.04 ? 284  VAL B CG2 1 
ATOM   5851 N  N   . LEU B 2 285 ? 21.952  91.107  32.626  1.00 30.53 ? 285  LEU B N   1 
ATOM   5852 C  CA  . LEU B 2 285 ? 22.453  92.393  33.173  1.00 30.54 ? 285  LEU B CA  1 
ATOM   5853 C  C   . LEU B 2 285 ? 21.440  92.904  34.194  1.00 28.60 ? 285  LEU B C   1 
ATOM   5854 O  O   . LEU B 2 285 ? 20.243  92.662  33.997  1.00 27.36 ? 285  LEU B O   1 
ATOM   5855 C  CB  . LEU B 2 285 ? 22.630  93.396  32.029  1.00 32.05 ? 285  LEU B CB  1 
ATOM   5856 C  CG  . LEU B 2 285 ? 23.729  93.073  31.022  1.00 32.18 ? 285  LEU B CG  1 
ATOM   5857 C  CD1 . LEU B 2 285 ? 23.641  94.014  29.828  1.00 32.95 ? 285  LEU B CD1 1 
ATOM   5858 C  CD2 . LEU B 2 285 ? 25.101  93.158  31.662  1.00 33.32 ? 285  LEU B CD2 1 
ATOM   5859 N  N   . SER B 2 286 ? 21.907  93.611  35.221  1.00 28.41 ? 286  SER B N   1 
ATOM   5860 C  CA  . SER B 2 286 ? 21.034  94.305  36.203  1.00 28.68 ? 286  SER B CA  1 
ATOM   5861 C  C   . SER B 2 286 ? 20.234  95.393  35.473  1.00 28.08 ? 286  SER B C   1 
ATOM   5862 O  O   . SER B 2 286 ? 20.747  95.944  34.475  1.00 25.89 ? 286  SER B O   1 
ATOM   5863 C  CB  . SER B 2 286 ? 21.847  94.891  37.312  1.00 29.36 ? 286  SER B CB  1 
ATOM   5864 O  OG  . SER B 2 286 ? 22.581  96.005  36.822  1.00 32.56 ? 286  SER B OG  1 
ATOM   5865 N  N   . MET B 2 287 ? 19.028  95.700  35.955  1.00 26.58 ? 287  MET B N   1 
ATOM   5866 C  CA  . MET B 2 287 ? 18.152  96.738  35.359  1.00 28.53 ? 287  MET B CA  1 
ATOM   5867 C  C   . MET B 2 287 ? 18.919  98.046  35.160  1.00 27.29 ? 287  MET B C   1 
ATOM   5868 O  O   . MET B 2 287 ? 18.786  98.660  34.114  1.00 27.56 ? 287  MET B O   1 
ATOM   5869 C  CB  . MET B 2 287 ? 16.914  96.990  36.222  1.00 29.69 ? 287  MET B CB  1 
ATOM   5870 C  CG  . MET B 2 287 ? 16.098  98.169  35.737  1.00 29.67 ? 287  MET B CG  1 
ATOM   5871 S  SD  . MET B 2 287 ? 14.515  98.305  36.590  1.00 31.72 ? 287  MET B SD  1 
ATOM   5872 C  CE  . MET B 2 287 ? 13.705  96.814  36.011  1.00 30.83 ? 287  MET B CE  1 
ATOM   5873 N  N   . PRO B 2 288 ? 19.690  98.575  36.140  1.00 29.45 ? 288  PRO B N   1 
ATOM   5874 C  CA  . PRO B 2 288 ? 20.401  99.843  35.938  1.00 29.84 ? 288  PRO B CA  1 
ATOM   5875 C  C   . PRO B 2 288 ? 21.400  99.846  34.770  1.00 29.83 ? 288  PRO B C   1 
ATOM   5876 O  O   . PRO B 2 288 ? 21.545  100.880 34.124  1.00 28.28 ? 288  PRO B O   1 
ATOM   5877 C  CB  . PRO B 2 288 ? 21.117  100.061 37.277  1.00 30.44 ? 288  PRO B CB  1 
ATOM   5878 C  CG  . PRO B 2 288 ? 20.224  99.347  38.260  1.00 29.89 ? 288  PRO B CG  1 
ATOM   5879 C  CD  . PRO B 2 288 ? 19.843  98.079  37.516  1.00 30.59 ? 288  PRO B CD  1 
ATOM   5880 N  N   . VAL B 2 289 ? 22.063  98.716  34.517  1.00 29.15 ? 289  VAL B N   1 
ATOM   5881 C  CA  . VAL B 2 289 ? 22.996  98.570  33.359  1.00 28.95 ? 289  VAL B CA  1 
ATOM   5882 C  C   . VAL B 2 289 ? 22.153  98.459  32.075  1.00 27.96 ? 289  VAL B C   1 
ATOM   5883 O  O   . VAL B 2 289 ? 22.569  99.025  31.059  1.00 28.64 ? 289  VAL B O   1 
ATOM   5884 C  CB  . VAL B 2 289 ? 23.979  97.396  33.545  1.00 29.41 ? 289  VAL B CB  1 
ATOM   5885 C  CG1 . VAL B 2 289 ? 24.904  97.242  32.343  1.00 30.47 ? 289  VAL B CG1 1 
ATOM   5886 C  CG2 . VAL B 2 289 ? 24.801  97.544  34.825  1.00 28.71 ? 289  VAL B CG2 1 
ATOM   5887 N  N   . ARG B 2 290 ? 20.973  97.835  32.134  1.00 28.13 ? 290  ARG B N   1 
ATOM   5888 C  CA  . ARG B 2 290 ? 20.048  97.763  30.964  1.00 29.11 ? 290  ARG B CA  1 
ATOM   5889 C  C   . ARG B 2 290 ? 19.524  99.166  30.624  1.00 28.68 ? 290  ARG B C   1 
ATOM   5890 O  O   . ARG B 2 290 ? 19.401  99.474  29.421  1.00 28.73 ? 290  ARG B O   1 
ATOM   5891 C  CB  . ARG B 2 290 ? 18.916  96.771  31.224  1.00 29.09 ? 290  ARG B CB  1 
ATOM   5892 C  CG  . ARG B 2 290 ? 19.414  95.355  31.470  1.00 30.45 ? 290  ARG B CG  1 
ATOM   5893 C  CD  . ARG B 2 290 ? 18.406  94.290  31.090  1.00 31.50 ? 290  ARG B CD  1 
ATOM   5894 N  NE  . ARG B 2 290 ? 17.090  94.505  31.679  1.00 31.04 ? 290  ARG B NE  1 
ATOM   5895 C  CZ  . ARG B 2 290 ? 16.710  94.126  32.898  1.00 32.62 ? 290  ARG B CZ  1 
ATOM   5896 N  NH1 . ARG B 2 290 ? 17.560  93.529  33.717  1.00 31.69 ? 290  ARG B NH1 1 
ATOM   5897 N  NH2 . ARG B 2 290 ? 15.469  94.367  33.300  1.00 32.83 ? 290  ARG B NH2 1 
ATOM   5898 N  N   . ILE B 2 291 ? 19.222  99.999  31.625  1.00 27.70 ? 291  ILE B N   1 
ATOM   5899 C  CA  . ILE B 2 291 ? 18.780  101.403 31.371  1.00 28.89 ? 291  ILE B CA  1 
ATOM   5900 C  C   . ILE B 2 291 ? 19.909  102.125 30.624  1.00 28.08 ? 291  ILE B C   1 
ATOM   5901 O  O   . ILE B 2 291 ? 19.618  102.781 29.614  1.00 28.88 ? 291  ILE B O   1 
ATOM   5902 C  CB  . ILE B 2 291 ? 18.393  102.134 32.668  1.00 29.78 ? 291  ILE B CB  1 
ATOM   5903 C  CG1 . ILE B 2 291 ? 17.145  101.523 33.312  1.00 30.53 ? 291  ILE B CG1 1 
ATOM   5904 C  CG2 . ILE B 2 291 ? 18.215  103.624 32.409  1.00 30.59 ? 291  ILE B CG2 1 
ATOM   5905 C  CD1 . ILE B 2 291 ? 16.936  101.939 34.758  1.00 32.12 ? 291  ILE B CD1 1 
ATOM   5906 N  N   . ALA B 2 292 ? 21.144  102.007 31.119  1.00 27.23 ? 292  ALA B N   1 
ATOM   5907 C  CA  . ALA B 2 292 ? 22.362  102.596 30.512  1.00 27.32 ? 292  ALA B CA  1 
ATOM   5908 C  C   . ALA B 2 292 ? 22.490  102.130 29.052  1.00 26.07 ? 292  ALA B C   1 
ATOM   5909 O  O   . ALA B 2 292 ? 22.684  102.993 28.177  1.00 25.90 ? 292  ALA B O   1 
ATOM   5910 C  CB  . ALA B 2 292 ? 23.577  102.230 31.327  1.00 26.47 ? 292  ALA B CB  1 
ATOM   5911 N  N   . ALA B 2 293 ? 22.359  100.821 28.800  1.00 25.90 ? 293  ALA B N   1 
ATOM   5912 C  CA  . ALA B 2 293 ? 22.439  100.196 27.453  1.00 26.20 ? 293  ALA B CA  1 
ATOM   5913 C  C   . ALA B 2 293 ? 21.374  100.811 26.535  1.00 27.77 ? 293  ALA B C   1 
ATOM   5914 O  O   . ALA B 2 293 ? 21.622  101.003 25.326  1.00 28.09 ? 293  ALA B O   1 
ATOM   5915 C  CB  . ALA B 2 293 ? 22.256  98.704  27.564  1.00 25.83 ? 293  ALA B CB  1 
ATOM   5916 N  N   . GLU B 2 294 ? 20.207  101.104 27.092  1.00 29.33 ? 294  GLU B N   1 
ATOM   5917 C  CA  . GLU B 2 294 ? 19.086  101.715 26.339  1.00 32.58 ? 294  GLU B CA  1 
ATOM   5918 C  C   . GLU B 2 294 ? 19.462  103.156 25.967  1.00 30.11 ? 294  GLU B C   1 
ATOM   5919 O  O   . GLU B 2 294 ? 19.246  103.540 24.813  1.00 28.61 ? 294  GLU B O   1 
ATOM   5920 C  CB  . GLU B 2 294 ? 17.820  101.637 27.185  1.00 37.15 ? 294  GLU B CB  1 
ATOM   5921 C  CG  . GLU B 2 294 ? 16.567  102.001 26.438  1.00 42.68 ? 294  GLU B CG  1 
ATOM   5922 C  CD  . GLU B 2 294 ? 15.358  101.933 27.345  1.00 47.06 ? 294  GLU B CD  1 
ATOM   5923 O  OE1 . GLU B 2 294 ? 15.239  102.826 28.206  1.00 52.66 ? 294  GLU B OE1 1 
ATOM   5924 O  OE2 . GLU B 2 294 ? 14.582  100.962 27.225  1.00 51.18 ? 294  GLU B OE2 1 
ATOM   5925 N  N   . MET B 2 295 ? 20.020  103.913 26.912  1.00 28.95 ? 295  MET B N   1 
ATOM   5926 C  CA  . MET B 2 295 ? 20.467  105.310 26.673  1.00 30.18 ? 295  MET B CA  1 
ATOM   5927 C  C   . MET B 2 295 ? 21.590  105.310 25.623  1.00 29.55 ? 295  MET B C   1 
ATOM   5928 O  O   . MET B 2 295 ? 21.563  106.173 24.711  1.00 27.46 ? 295  MET B O   1 
ATOM   5929 C  CB  . MET B 2 295 ? 20.952  105.958 27.968  1.00 32.37 ? 295  MET B CB  1 
ATOM   5930 C  CG  . MET B 2 295 ? 19.857  106.092 29.020  1.00 35.85 ? 295  MET B CG  1 
ATOM   5931 S  SD  . MET B 2 295 ? 20.507  106.596 30.633  1.00 43.29 ? 295  MET B SD  1 
ATOM   5932 C  CE  . MET B 2 295 ? 21.206  108.188 30.203  1.00 42.75 ? 295  MET B CE  1 
ATOM   5933 N  N   . PHE B 2 296 ? 22.539  104.379 25.737  1.00 28.48 ? 296  PHE B N   1 
ATOM   5934 C  CA  . PHE B 2 296 ? 23.652  104.226 24.766  1.00 28.26 ? 296  PHE B CA  1 
ATOM   5935 C  C   . PHE B 2 296 ? 23.070  103.959 23.372  1.00 27.48 ? 296  PHE B C   1 
ATOM   5936 O  O   . PHE B 2 296 ? 23.510  104.606 22.419  1.00 27.31 ? 296  PHE B O   1 
ATOM   5937 C  CB  . PHE B 2 296 ? 24.601  103.093 25.158  1.00 28.14 ? 296  PHE B CB  1 
ATOM   5938 C  CG  . PHE B 2 296 ? 25.662  102.831 24.121  1.00 25.62 ? 296  PHE B CG  1 
ATOM   5939 C  CD1 . PHE B 2 296 ? 26.770  103.651 24.030  1.00 25.63 ? 296  PHE B CD1 1 
ATOM   5940 C  CD2 . PHE B 2 296 ? 25.525  101.798 23.207  1.00 26.19 ? 296  PHE B CD2 1 
ATOM   5941 C  CE1 . PHE B 2 296 ? 27.744  103.426 23.069  1.00 26.64 ? 296  PHE B CE1 1 
ATOM   5942 C  CE2 . PHE B 2 296 ? 26.488  101.586 22.229  1.00 26.78 ? 296  PHE B CE2 1 
ATOM   5943 C  CZ  . PHE B 2 296 ? 27.608  102.385 22.177  1.00 26.28 ? 296  PHE B CZ  1 
ATOM   5944 N  N   . GLY B 2 297 ? 22.110  103.038 23.281  1.00 27.75 ? 297  GLY B N   1 
ATOM   5945 C  CA  . GLY B 2 297 ? 21.418  102.657 22.036  1.00 29.18 ? 297  GLY B CA  1 
ATOM   5946 C  C   . GLY B 2 297 ? 20.780  103.865 21.367  1.00 30.27 ? 297  GLY B C   1 
ATOM   5947 O  O   . GLY B 2 297 ? 20.973  104.041 20.142  1.00 29.07 ? 297  GLY B O   1 
ATOM   5948 N  N   . GLU B 2 298 ? 20.062  104.679 22.146  1.00 30.55 ? 298  GLU B N   1 
ATOM   5949 C  CA  . GLU B 2 298 ? 19.417  105.930 21.659  1.00 32.00 ? 298  GLU B CA  1 
ATOM   5950 C  C   . GLU B 2 298 ? 20.493  106.846 21.063  1.00 30.93 ? 298  GLU B C   1 
ATOM   5951 O  O   . GLU B 2 298 ? 20.291  107.315 19.925  1.00 30.83 ? 298  GLU B O   1 
ATOM   5952 C  CB  . GLU B 2 298 ? 18.646  106.628 22.784  1.00 30.72 ? 298  GLU B CB  1 
ATOM   5953 N  N   . PHE B 2 299 ? 21.596  107.072 21.789  1.00 29.66 ? 299  PHE B N   1 
ATOM   5954 C  CA  . PHE B 2 299 ? 22.713  107.951 21.350  1.00 29.73 ? 299  PHE B CA  1 
ATOM   5955 C  C   . PHE B 2 299 ? 23.410  107.382 20.100  1.00 29.45 ? 299  PHE B C   1 
ATOM   5956 O  O   . PHE B 2 299 ? 23.707  108.135 19.139  1.00 27.49 ? 299  PHE B O   1 
ATOM   5957 C  CB  . PHE B 2 299 ? 23.747  108.149 22.458  1.00 30.42 ? 299  PHE B CB  1 
ATOM   5958 C  CG  . PHE B 2 299 ? 24.776  109.184 22.089  1.00 33.31 ? 299  PHE B CG  1 
ATOM   5959 C  CD1 . PHE B 2 299 ? 25.882  108.845 21.328  1.00 32.95 ? 299  PHE B CD1 1 
ATOM   5960 C  CD2 . PHE B 2 299 ? 24.587  110.520 22.421  1.00 35.95 ? 299  PHE B CD2 1 
ATOM   5961 C  CE1 . PHE B 2 299 ? 26.799  109.809 20.939  1.00 34.79 ? 299  PHE B CE1 1 
ATOM   5962 C  CE2 . PHE B 2 299 ? 25.511  111.481 22.040  1.00 35.30 ? 299  PHE B CE2 1 
ATOM   5963 C  CZ  . PHE B 2 299 ? 26.612  111.124 21.296  1.00 34.67 ? 299  PHE B CZ  1 
ATOM   5964 N  N   . PHE B 2 300 ? 23.719  106.087 20.129  1.00 27.48 ? 300  PHE B N   1 
ATOM   5965 C  CA  . PHE B 2 300 ? 24.311  105.349 18.990  1.00 27.46 ? 300  PHE B CA  1 
ATOM   5966 C  C   . PHE B 2 300 ? 23.470  105.606 17.732  1.00 27.79 ? 300  PHE B C   1 
ATOM   5967 O  O   . PHE B 2 300 ? 24.040  105.903 16.667  1.00 26.54 ? 300  PHE B O   1 
ATOM   5968 C  CB  . PHE B 2 300 ? 24.408  103.854 19.304  1.00 26.02 ? 300  PHE B CB  1 
ATOM   5969 C  CG  . PHE B 2 300 ? 24.870  103.028 18.132  1.00 25.21 ? 300  PHE B CG  1 
ATOM   5970 C  CD1 . PHE B 2 300 ? 26.218  102.832 17.891  1.00 24.78 ? 300  PHE B CD1 1 
ATOM   5971 C  CD2 . PHE B 2 300 ? 23.954  102.479 17.246  1.00 26.27 ? 300  PHE B CD2 1 
ATOM   5972 C  CE1 . PHE B 2 300 ? 26.645  102.088 16.801  1.00 24.41 ? 300  PHE B CE1 1 
ATOM   5973 C  CE2 . PHE B 2 300 ? 24.379  101.731 16.157  1.00 26.23 ? 300  PHE B CE2 1 
ATOM   5974 C  CZ  . PHE B 2 300 ? 25.727  101.550 15.929  1.00 26.02 ? 300  PHE B CZ  1 
ATOM   5975 N  N   . SER B 2 301 ? 22.148  105.466 17.849  1.00 28.69 ? 301  SER B N   1 
ATOM   5976 C  CA  . SER B 2 301 ? 21.201  105.610 16.707  1.00 31.24 ? 301  SER B CA  1 
ATOM   5977 C  C   . SER B 2 301 ? 21.291  107.030 16.144  1.00 30.70 ? 301  SER B C   1 
ATOM   5978 O  O   . SER B 2 301 ? 21.347  107.164 14.925  1.00 30.90 ? 301  SER B O   1 
ATOM   5979 C  CB  . SER B 2 301 ? 19.790  105.267 17.091  1.00 32.38 ? 301  SER B CB  1 
ATOM   5980 O  OG  . SER B 2 301 ? 19.664  103.871 17.332  1.00 35.28 ? 301  SER B OG  1 
ATOM   5981 N  N   . MET B 2 302 ? 21.299  108.045 17.008  1.00 31.83 ? 302  MET B N   1 
ATOM   5982 C  CA  . MET B 2 302 ? 21.308  109.467 16.578  1.00 35.90 ? 302  MET B CA  1 
ATOM   5983 C  C   . MET B 2 302 ? 22.651  109.787 15.905  1.00 33.06 ? 302  MET B C   1 
ATOM   5984 O  O   . MET B 2 302 ? 22.630  110.397 14.824  1.00 30.91 ? 302  MET B O   1 
ATOM   5985 C  CB  . MET B 2 302 ? 21.058  110.420 17.751  1.00 38.92 ? 302  MET B CB  1 
ATOM   5986 C  CG  . MET B 2 302 ? 19.628  110.355 18.262  1.00 46.03 ? 302  MET B CG  1 
ATOM   5987 S  SD  . MET B 2 302 ? 19.372  111.239 19.837  1.00 59.31 ? 302  MET B SD  1 
ATOM   5988 C  CE  . MET B 2 302 ? 17.739  110.660 20.293  1.00 58.67 ? 302  MET B CE  1 
ATOM   5989 N  N   . HIS B 2 303 ? 23.767  109.372 16.508  1.00 30.48 ? 303  HIS B N   1 
ATOM   5990 C  CA  . HIS B 2 303 ? 25.138  109.621 15.991  1.00 30.20 ? 303  HIS B CA  1 
ATOM   5991 C  C   . HIS B 2 303 ? 25.313  108.924 14.633  1.00 29.08 ? 303  HIS B C   1 
ATOM   5992 O  O   . HIS B 2 303 ? 25.904  109.546 13.719  1.00 28.83 ? 303  HIS B O   1 
ATOM   5993 C  CB  . HIS B 2 303 ? 26.193  109.193 17.017  1.00 30.44 ? 303  HIS B CB  1 
ATOM   5994 C  CG  . HIS B 2 303 ? 27.562  109.684 16.695  1.00 31.80 ? 303  HIS B CG  1 
ATOM   5995 N  ND1 . HIS B 2 303 ? 27.810  111.003 16.371  1.00 33.10 ? 303  HIS B ND1 1 
ATOM   5996 C  CD2 . HIS B 2 303 ? 28.755  109.050 16.650  1.00 32.73 ? 303  HIS B CD2 1 
ATOM   5997 C  CE1 . HIS B 2 303 ? 29.098  111.160 16.135  1.00 32.48 ? 303  HIS B CE1 1 
ATOM   5998 N  NE2 . HIS B 2 303 ? 29.703  109.979 16.307  1.00 33.13 ? 303  HIS B NE2 1 
ATOM   5999 N  N   . LEU B 2 304 ? 24.826  107.685 14.507  1.00 27.50 ? 304  LEU B N   1 
ATOM   6000 C  CA  . LEU B 2 304 ? 24.852  106.925 13.231  1.00 29.29 ? 304  LEU B CA  1 
ATOM   6001 C  C   . LEU B 2 304 ? 24.129  107.739 12.148  1.00 29.64 ? 304  LEU B C   1 
ATOM   6002 O  O   . LEU B 2 304 ? 24.697  107.881 11.057  1.00 27.94 ? 304  LEU B O   1 
ATOM   6003 C  CB  . LEU B 2 304 ? 24.197  105.553 13.413  1.00 29.66 ? 304  LEU B CB  1 
ATOM   6004 C  CG  . LEU B 2 304 ? 23.921  104.786 12.120  1.00 30.77 ? 304  LEU B CG  1 
ATOM   6005 C  CD1 . LEU B 2 304 ? 25.214  104.403 11.427  1.00 31.62 ? 304  LEU B CD1 1 
ATOM   6006 C  CD2 . LEU B 2 304 ? 23.076  103.554 12.397  1.00 33.05 ? 304  LEU B CD2 1 
ATOM   6007 N  N   . GLN B 2 305 ? 22.919  108.234 12.440  1.00 31.57 ? 305  GLN B N   1 
ATOM   6008 C  CA  . GLN B 2 305 ? 22.117  109.076 11.506  1.00 33.93 ? 305  GLN B CA  1 
ATOM   6009 C  C   . GLN B 2 305 ? 22.904  110.321 11.083  1.00 32.77 ? 305  GLN B C   1 
ATOM   6010 O  O   . GLN B 2 305 ? 22.885  110.621 9.883   1.00 34.30 ? 305  GLN B O   1 
ATOM   6011 C  CB  . GLN B 2 305 ? 20.781  109.493 12.114  1.00 36.21 ? 305  GLN B CB  1 
ATOM   6012 C  CG  . GLN B 2 305 ? 19.747  108.389 12.053  1.00 40.99 ? 305  GLN B CG  1 
ATOM   6013 C  CD  . GLN B 2 305 ? 18.398  108.842 12.546  1.00 45.62 ? 305  GLN B CD  1 
ATOM   6014 O  OE1 . GLN B 2 305 ? 17.842  108.278 13.489  1.00 53.37 ? 305  GLN B OE1 1 
ATOM   6015 N  NE2 . GLN B 2 305 ? 17.867  109.875 11.916  1.00 47.12 ? 305  GLN B NE2 1 
ATOM   6016 N  N   . VAL B 2 306 ? 23.558  111.015 12.020  1.00 31.81 ? 306  VAL B N   1 
ATOM   6017 C  CA  . VAL B 2 306 ? 24.348  112.251 11.727  1.00 32.31 ? 306  VAL B CA  1 
ATOM   6018 C  C   . VAL B 2 306 ? 25.518  111.897 10.801  1.00 32.48 ? 306  VAL B C   1 
ATOM   6019 O  O   . VAL B 2 306 ? 25.735  112.629 9.816   1.00 30.89 ? 306  VAL B O   1 
ATOM   6020 C  CB  . VAL B 2 306 ? 24.841  112.943 13.010  1.00 33.94 ? 306  VAL B CB  1 
ATOM   6021 C  CG1 . VAL B 2 306 ? 25.842  114.046 12.712  1.00 34.60 ? 306  VAL B CG1 1 
ATOM   6022 C  CG2 . VAL B 2 306 ? 23.679  113.487 13.828  1.00 36.92 ? 306  VAL B CG2 1 
ATOM   6023 N  N   . LEU B 2 307 ? 26.260  110.831 11.114  1.00 31.15 ? 307  LEU B N   1 
ATOM   6024 C  CA  . LEU B 2 307 ? 27.417  110.377 10.297  1.00 31.21 ? 307  LEU B CA  1 
ATOM   6025 C  C   . LEU B 2 307 ? 26.931  109.936 8.911   1.00 32.04 ? 307  LEU B C   1 
ATOM   6026 O  O   . LEU B 2 307 ? 27.613  110.263 7.920   1.00 30.99 ? 307  LEU B O   1 
ATOM   6027 C  CB  . LEU B 2 307 ? 28.137  109.240 11.030  1.00 32.46 ? 307  LEU B CB  1 
ATOM   6028 C  CG  . LEU B 2 307 ? 28.914  109.677 12.271  1.00 32.00 ? 307  LEU B CG  1 
ATOM   6029 C  CD1 . LEU B 2 307 ? 29.409  108.470 13.059  1.00 31.70 ? 307  LEU B CD1 1 
ATOM   6030 C  CD2 . LEU B 2 307 ? 30.077  110.588 11.884  1.00 32.11 ? 307  LEU B CD2 1 
ATOM   6031 N  N   . LYS B 2 308 ? 25.802  109.222 8.847   1.00 32.88 ? 308  LYS B N   1 
ATOM   6032 C  CA  . LYS B 2 308 ? 25.180  108.775 7.568   1.00 35.82 ? 308  LYS B CA  1 
ATOM   6033 C  C   . LYS B 2 308 ? 24.855  109.978 6.673   1.00 37.63 ? 308  LYS B C   1 
ATOM   6034 O  O   . LYS B 2 308 ? 25.045  109.863 5.438   1.00 35.48 ? 308  LYS B O   1 
ATOM   6035 C  CB  . LYS B 2 308 ? 23.894  107.991 7.820   1.00 38.08 ? 308  LYS B CB  1 
ATOM   6036 C  CG  . LYS B 2 308 ? 24.023  106.480 7.740   1.00 40.31 ? 308  LYS B CG  1 
ATOM   6037 C  CD  . LYS B 2 308 ? 22.693  105.795 7.534   1.00 40.96 ? 308  LYS B CD  1 
ATOM   6038 C  CE  . LYS B 2 308 ? 22.200  105.906 6.111   1.00 42.85 ? 308  LYS B CE  1 
ATOM   6039 N  NZ  . LYS B 2 308 ? 20.867  105.282 5.932   1.00 44.58 ? 308  LYS B NZ  1 
ATOM   6040 N  N   . GLN B 2 309 ? 24.343  111.061 7.269   1.00 37.62 ? 309  GLN B N   1 
ATOM   6041 C  CA  . GLN B 2 309 ? 23.868  112.271 6.545   1.00 37.95 ? 309  GLN B CA  1 
ATOM   6042 C  C   . GLN B 2 309 ? 25.074  112.998 5.961   1.00 38.22 ? 309  GLN B C   1 
ATOM   6043 O  O   . GLN B 2 309 ? 25.028  113.450 4.820   1.00 38.12 ? 309  GLN B O   1 
ATOM   6044 C  CB  . GLN B 2 309 ? 23.053  113.180 7.468   1.00 38.20 ? 309  GLN B CB  1 
HETATM 6045 N  N   . MLZ B 2 310 ? 26.148  113.083 6.754   1.00 34.75 ? 310  MLZ B N   1 
HETATM 6046 C  CA  . MLZ B 2 310 ? 27.369  113.752 6.349   1.00 36.75 ? 310  MLZ B CA  1 
HETATM 6047 C  CB  . MLZ B 2 310 ? 28.277  113.951 7.567   1.00 39.07 ? 310  MLZ B CB  1 
HETATM 6048 C  CG  . MLZ B 2 310 ? 29.705  114.389 7.267   1.00 42.95 ? 310  MLZ B CG  1 
HETATM 6049 C  CD  . MLZ B 2 310 ? 29.804  115.703 6.534   1.00 46.03 ? 310  MLZ B CD  1 
HETATM 6050 C  CE  . MLZ B 2 310 ? 31.224  116.246 6.482   1.00 47.21 ? 310  MLZ B CE  1 
HETATM 6051 N  NZ  . MLZ B 2 310 ? 31.349  117.161 5.344   1.00 51.40 ? 310  MLZ B NZ  1 
HETATM 6052 C  CM  . MLZ B 2 310 ? 30.684  118.472 5.439   1.00 50.10 ? 310  MLZ B CM  1 
HETATM 6053 C  C   . MLZ B 2 310 ? 28.054  112.955 5.238   1.00 36.79 ? 310  MLZ B C   1 
HETATM 6054 O  O   . MLZ B 2 310 ? 28.590  113.543 4.307   1.00 35.07 ? 310  MLZ B O   1 
ATOM   6055 N  N   . ARG B 2 311 ? 28.027  111.621 5.341   1.00 35.92 ? 311  ARG B N   1 
ATOM   6056 C  CA  . ARG B 2 311 ? 28.640  110.757 4.347   1.00 36.09 ? 311  ARG B CA  1 
ATOM   6057 C  C   . ARG B 2 311 ? 27.857  110.846 3.033   1.00 36.22 ? 311  ARG B C   1 
ATOM   6058 O  O   . ARG B 2 311 ? 28.496  110.930 1.979   1.00 34.19 ? 311  ARG B O   1 
ATOM   6059 C  CB  . ARG B 2 311 ? 28.699  109.315 4.855   1.00 39.18 ? 311  ARG B CB  1 
ATOM   6060 C  CG  . ARG B 2 311 ? 29.458  108.369 3.936   1.00 43.36 ? 311  ARG B CG  1 
ATOM   6061 C  CD  . ARG B 2 311 ? 28.559  107.308 3.345   1.00 49.04 ? 311  ARG B CD  1 
ATOM   6062 N  NE  . ARG B 2 311 ? 28.370  106.202 4.277   1.00 51.08 ? 311  ARG B NE  1 
ATOM   6063 C  CZ  . ARG B 2 311 ? 27.198  105.727 4.712   1.00 56.16 ? 311  ARG B CZ  1 
ATOM   6064 N  NH1 . ARG B 2 311 ? 27.191  104.710 5.556   1.00 54.63 ? 311  ARG B NH1 1 
ATOM   6065 N  NH2 . ARG B 2 311 ? 26.043  106.244 4.318   1.00 58.39 ? 311  ARG B NH2 1 
ATOM   6066 N  N   . ARG B 2 312 ? 26.524  110.859 3.099   1.00 36.57 ? 312  ARG B N   1 
ATOM   6067 C  CA  . ARG B 2 312 ? 25.666  110.985 1.884   1.00 36.07 ? 312  ARG B CA  1 
ATOM   6068 C  C   . ARG B 2 312 ? 25.955  112.334 1.209   1.00 37.55 ? 312  ARG B C   1 
ATOM   6069 O  O   . ARG B 2 312 ? 26.276  112.338 0.005   1.00 34.65 ? 312  ARG B O   1 
ATOM   6070 C  CB  . ARG B 2 312 ? 24.188  110.845 2.240   1.00 36.99 ? 312  ARG B CB  1 
ATOM   6071 C  CG  . ARG B 2 312 ? 23.286  110.582 1.043   1.00 37.66 ? 312  ARG B CG  1 
ATOM   6072 C  CD  . ARG B 2 312 ? 21.815  110.645 1.427   1.00 38.55 ? 312  ARG B CD  1 
ATOM   6073 N  NE  . ARG B 2 312 ? 20.958  110.435 0.270   1.00 39.43 ? 312  ARG B NE  1 
ATOM   6074 C  CZ  . ARG B 2 312 ? 20.735  111.336 -0.685  1.00 39.19 ? 312  ARG B CZ  1 
ATOM   6075 N  NH1 . ARG B 2 312 ? 21.292  112.534 -0.623  1.00 38.69 ? 312  ARG B NH1 1 
ATOM   6076 N  NH2 . ARG B 2 312 ? 19.952  111.034 -1.705  1.00 40.53 ? 312  ARG B NH2 1 
ATOM   6077 N  N   . LEU B 2 313 ? 25.878  113.430 1.970   1.00 37.41 ? 313  LEU B N   1 
ATOM   6078 C  CA  . LEU B 2 313 ? 26.119  114.817 1.480   1.00 37.46 ? 313  LEU B CA  1 
ATOM   6079 C  C   . LEU B 2 313 ? 27.500  114.904 0.816   1.00 36.93 ? 313  LEU B C   1 
ATOM   6080 O  O   . LEU B 2 313 ? 27.604  115.551 -0.237  1.00 33.60 ? 313  LEU B O   1 
ATOM   6081 C  CB  . LEU B 2 313 ? 26.011  115.798 2.653   1.00 39.26 ? 313  LEU B CB  1 
ATOM   6082 C  CG  . LEU B 2 313 ? 26.297  117.265 2.326   1.00 41.37 ? 313  LEU B CG  1 
ATOM   6083 C  CD1 . LEU B 2 313 ? 25.215  117.842 1.421   1.00 41.68 ? 313  LEU B CD1 1 
ATOM   6084 C  CD2 . LEU B 2 313 ? 26.428  118.092 3.600   1.00 41.56 ? 313  LEU B CD2 1 
ATOM   6085 N  N   . ASP B 2 314 ? 28.520  114.287 1.416   1.00 35.30 ? 314  ASP B N   1 
ATOM   6086 C  CA  . ASP B 2 314 ? 29.913  114.322 0.898   1.00 36.36 ? 314  ASP B CA  1 
ATOM   6087 C  C   . ASP B 2 314 ? 29.993  113.567 -0.439  1.00 33.97 ? 314  ASP B C   1 
ATOM   6088 O  O   . ASP B 2 314 ? 30.671  114.082 -1.342  1.00 33.36 ? 314  ASP B O   1 
ATOM   6089 C  CB  . ASP B 2 314 ? 30.912  113.792 1.926   1.00 37.97 ? 314  ASP B CB  1 
ATOM   6090 C  CG  . ASP B 2 314 ? 31.122  114.715 3.117   1.00 40.81 ? 314  ASP B CG  1 
ATOM   6091 O  OD1 . ASP B 2 314 ? 30.541  115.820 3.123   1.00 45.03 ? 314  ASP B OD1 1 
ATOM   6092 O  OD2 . ASP B 2 314 ? 31.858  114.316 4.035   1.00 41.28 ? 314  ASP B OD2 1 
ATOM   6093 N  N   . THR B 2 315 ? 29.336  112.410 -0.571  1.00 32.75 ? 315  THR B N   1 
ATOM   6094 C  CA  A THR B 2 315 ? 29.340  111.592 -1.817  0.50 34.55 ? 315  THR B CA  1 
ATOM   6095 C  CA  B THR B 2 315 ? 29.382  111.611 -1.830  0.50 35.04 ? 315  THR B CA  1 
ATOM   6096 C  C   . THR B 2 315 ? 28.582  112.333 -2.923  1.00 34.78 ? 315  THR B C   1 
ATOM   6097 O  O   . THR B 2 315 ? 29.030  112.277 -4.086  1.00 33.34 ? 315  THR B O   1 
ATOM   6098 C  CB  A THR B 2 315 ? 28.727  110.203 -1.589  0.50 33.83 ? 315  THR B CB  1 
ATOM   6099 C  CB  B THR B 2 315 ? 28.898  110.164 -1.661  0.50 35.02 ? 315  THR B CB  1 
ATOM   6100 O  OG1 A THR B 2 315 ? 29.283  109.648 -0.395  0.50 35.09 ? 315  THR B OG1 1 
ATOM   6101 O  OG1 B THR B 2 315 ? 27.514  110.195 -1.315  0.50 35.78 ? 315  THR B OG1 1 
ATOM   6102 C  CG2 A THR B 2 315 ? 28.964  109.260 -2.747  0.50 33.30 ? 315  THR B CG2 1 
ATOM   6103 C  CG2 B THR B 2 315 ? 29.685  109.389 -0.626  0.50 35.83 ? 315  THR B CG2 1 
ATOM   6104 N  N   . ILE B 2 316 ? 27.467  112.981 -2.563  1.00 33.76 ? 316  ILE B N   1 
ATOM   6105 C  CA  . ILE B 2 316 ? 26.621  113.754 -3.527  1.00 33.90 ? 316  ILE B CA  1 
ATOM   6106 C  C   . ILE B 2 316 ? 27.437  114.948 -4.026  1.00 33.24 ? 316  ILE B C   1 
ATOM   6107 O  O   . ILE B 2 316 ? 27.436  115.181 -5.259  1.00 32.47 ? 316  ILE B O   1 
ATOM   6108 C  CB  . ILE B 2 316 ? 25.276  114.197 -2.911  1.00 36.23 ? 316  ILE B CB  1 
ATOM   6109 C  CG1 . ILE B 2 316 ? 24.411  113.002 -2.501  1.00 35.56 ? 316  ILE B CG1 1 
ATOM   6110 C  CG2 . ILE B 2 316 ? 24.528  115.141 -3.851  1.00 37.89 ? 316  ILE B CG2 1 
ATOM   6111 C  CD1 . ILE B 2 316 ? 23.938  112.142 -3.640  1.00 35.99 ? 316  ILE B CD1 1 
ATOM   6112 N  N   . ASN B 2 317 ? 28.118  115.656 -3.116  1.00 31.64 ? 317  ASN B N   1 
ATOM   6113 C  CA  . ASN B 2 317 ? 28.910  116.869 -3.447  1.00 33.14 ? 317  ASN B CA  1 
ATOM   6114 C  C   . ASN B 2 317 ? 30.134  116.480 -4.277  1.00 32.17 ? 317  ASN B C   1 
ATOM   6115 O  O   . ASN B 2 317 ? 30.509  117.252 -5.171  1.00 30.04 ? 317  ASN B O   1 
ATOM   6116 C  CB  . ASN B 2 317 ? 29.332  117.647 -2.203  1.00 34.37 ? 317  ASN B CB  1 
ATOM   6117 C  CG  . ASN B 2 317 ? 28.185  118.429 -1.605  1.00 35.48 ? 317  ASN B CG  1 
ATOM   6118 O  OD1 . ASN B 2 317 ? 27.140  118.576 -2.231  1.00 39.24 ? 317  ASN B OD1 1 
ATOM   6119 N  ND2 . ASN B 2 317 ? 28.360  118.907 -0.387  1.00 37.09 ? 317  ASN B ND2 1 
ATOM   6120 N  N   . HIS B 2 318 ? 30.738  115.333 -3.976  1.00 31.86 ? 318  HIS B N   1 
ATOM   6121 C  CA  . HIS B 2 318 ? 31.878  114.770 -4.744  1.00 31.43 ? 318  HIS B CA  1 
ATOM   6122 C  C   . HIS B 2 318 ? 31.433  114.521 -6.194  1.00 30.32 ? 318  HIS B C   1 
ATOM   6123 O  O   . HIS B 2 318 ? 32.177  114.902 -7.124  1.00 30.61 ? 318  HIS B O   1 
ATOM   6124 C  CB  . HIS B 2 318 ? 32.408  113.518 -4.045  1.00 33.18 ? 318  HIS B CB  1 
ATOM   6125 C  CG  . HIS B 2 318 ? 33.583  112.920 -4.733  1.00 35.40 ? 318  HIS B CG  1 
ATOM   6126 N  ND1 . HIS B 2 318 ? 33.450  111.902 -5.653  1.00 36.94 ? 318  HIS B ND1 1 
ATOM   6127 C  CD2 . HIS B 2 318 ? 34.901  113.198 -4.650  1.00 37.28 ? 318  HIS B CD2 1 
ATOM   6128 C  CE1 . HIS B 2 318 ? 34.641  111.570 -6.102  1.00 39.37 ? 318  HIS B CE1 1 
ATOM   6129 N  NE2 . HIS B 2 318 ? 35.550  112.352 -5.503  1.00 39.33 ? 318  HIS B NE2 1 
ATOM   6130 N  N   . ALA B 2 319 ? 30.244  113.943 -6.375  1.00 29.49 ? 319  ALA B N   1 
ATOM   6131 C  CA  . ALA B 2 319 ? 29.630  113.665 -7.696  1.00 31.96 ? 319  ALA B CA  1 
ATOM   6132 C  C   . ALA B 2 319 ? 29.415  114.976 -8.461  1.00 32.25 ? 319  ALA B C   1 
ATOM   6133 O  O   . ALA B 2 319 ? 29.814  115.034 -9.641  1.00 32.25 ? 319  ALA B O   1 
ATOM   6134 C  CB  . ALA B 2 319 ? 28.336  112.908 -7.537  1.00 32.04 ? 319  ALA B CB  1 
ATOM   6135 N  N   . HIS B 2 320 ? 28.798  115.976 -7.824  1.00 32.74 ? 320  HIS B N   1 
ATOM   6136 C  CA  . HIS B 2 320 ? 28.482  117.292 -8.445  1.00 33.30 ? 320  HIS B CA  1 
ATOM   6137 C  C   . HIS B 2 320 ? 29.779  117.978 -8.882  1.00 32.67 ? 320  HIS B C   1 
ATOM   6138 O  O   . HIS B 2 320 ? 29.810  118.480 -10.013 1.00 30.46 ? 320  HIS B O   1 
ATOM   6139 C  CB  . HIS B 2 320 ? 27.647  118.191 -7.520  1.00 34.43 ? 320  HIS B CB  1 
ATOM   6140 C  CG  . HIS B 2 320 ? 26.212  117.795 -7.421  1.00 36.63 ? 320  HIS B CG  1 
ATOM   6141 N  ND1 . HIS B 2 320 ? 25.530  117.794 -6.218  1.00 38.22 ? 320  HIS B ND1 1 
ATOM   6142 C  CD2 . HIS B 2 320 ? 25.323  117.396 -8.357  1.00 40.18 ? 320  HIS B CD2 1 
ATOM   6143 C  CE1 . HIS B 2 320 ? 24.287  117.399 -6.420  1.00 39.83 ? 320  HIS B CE1 1 
ATOM   6144 N  NE2 . HIS B 2 320 ? 24.133  117.145 -7.719  1.00 39.97 ? 320  HIS B NE2 1 
ATOM   6145 N  N   . ALA B 2 321 ? 30.803  117.998 -8.024  1.00 32.93 ? 321  ALA B N   1 
ATOM   6146 C  CA  . ALA B 2 321 ? 32.105  118.650 -8.306  1.00 33.62 ? 321  ALA B CA  1 
ATOM   6147 C  C   . ALA B 2 321 ? 32.750  118.015 -9.544  1.00 33.64 ? 321  ALA B C   1 
ATOM   6148 O  O   . ALA B 2 321 ? 33.328  118.757 -10.375 1.00 34.56 ? 321  ALA B O   1 
ATOM   6149 C  CB  . ALA B 2 321 ? 33.020  118.560 -7.111  1.00 34.60 ? 321  ALA B CB  1 
ATOM   6150 N  N   . ALA B 2 322 ? 32.670  116.689 -9.652  1.00 32.07 ? 322  ALA B N   1 
ATOM   6151 C  CA  . ALA B 2 322 ? 33.306  115.901 -10.731 1.00 32.03 ? 322  ALA B CA  1 
ATOM   6152 C  C   . ALA B 2 322 ? 32.543  116.143 -12.038 1.00 30.78 ? 322  ALA B C   1 
ATOM   6153 O  O   . ALA B 2 322 ? 33.182  116.289 -13.083 1.00 31.31 ? 322  ALA B O   1 
ATOM   6154 C  CB  . ALA B 2 322 ? 33.335  114.439 -10.354 1.00 31.09 ? 322  ALA B CB  1 
ATOM   6155 N  N   . LEU B 2 323 ? 31.215  116.175 -11.975 1.00 32.01 ? 323  LEU B N   1 
ATOM   6156 C  CA  . LEU B 2 323 ? 30.356  116.412 -13.167 1.00 32.74 ? 323  LEU B CA  1 
ATOM   6157 C  C   . LEU B 2 323 ? 30.525  117.862 -13.634 1.00 33.38 ? 323  LEU B C   1 
ATOM   6158 O  O   . LEU B 2 323 ? 30.444  118.088 -14.853 1.00 32.41 ? 323  LEU B O   1 
ATOM   6159 C  CB  . LEU B 2 323 ? 28.900  116.077 -12.833 1.00 32.18 ? 323  LEU B CB  1 
ATOM   6160 C  CG  . LEU B 2 323 ? 28.606  114.585 -12.658 1.00 32.57 ? 323  LEU B CG  1 
ATOM   6161 C  CD1 . LEU B 2 323 ? 27.221  114.369 -12.077 1.00 31.11 ? 323  LEU B CD1 1 
ATOM   6162 C  CD2 . LEU B 2 323 ? 28.748  113.825 -13.965 1.00 32.81 ? 323  LEU B CD2 1 
ATOM   6163 N  N   . ASP B 2 324 ? 30.788  118.796 -12.713 1.00 34.26 ? 324  ASP B N   1 
ATOM   6164 C  CA  . ASP B 2 324 ? 31.014  120.227 -13.054 1.00 36.79 ? 324  ASP B CA  1 
ATOM   6165 C  C   . ASP B 2 324 ? 32.375  120.374 -13.750 1.00 35.33 ? 324  ASP B C   1 
ATOM   6166 O  O   . ASP B 2 324 ? 32.430  121.098 -14.778 1.00 31.96 ? 324  ASP B O   1 
ATOM   6167 C  CB  . ASP B 2 324 ? 30.870  121.142 -11.836 1.00 39.91 ? 324  ASP B CB  1 
ATOM   6168 C  CG  . ASP B 2 324 ? 29.434  121.315 -11.356 1.00 46.78 ? 324  ASP B CG  1 
ATOM   6169 O  OD1 . ASP B 2 324 ? 28.500  120.851 -12.060 1.00 50.29 ? 324  ASP B OD1 1 
ATOM   6170 O  OD2 . ASP B 2 324 ? 29.253  121.908 -10.270 1.00 53.66 ? 324  ASP B OD2 1 
ATOM   6171 N  N   . ARG B 2 325 ? 33.425  119.720 -13.234 1.00 34.30 ? 325  ARG B N   1 
ATOM   6172 C  CA  . ARG B 2 325 ? 34.744  119.664 -13.924 1.00 33.11 ? 325  ARG B CA  1 
ATOM   6173 C  C   . ARG B 2 325 ? 34.535  119.124 -15.345 1.00 31.85 ? 325  ARG B C   1 
ATOM   6174 O  O   . ARG B 2 325 ? 35.103  119.706 -16.282 1.00 31.84 ? 325  ARG B O   1 
ATOM   6175 C  CB  . ARG B 2 325 ? 35.767  118.812 -13.164 1.00 36.97 ? 325  ARG B CB  1 
ATOM   6176 C  CG  . ARG B 2 325 ? 36.239  119.409 -11.843 1.00 39.49 ? 325  ARG B CG  1 
ATOM   6177 C  CD  . ARG B 2 325 ? 37.516  118.766 -11.316 1.00 40.74 ? 325  ARG B CD  1 
ATOM   6178 N  NE  . ARG B 2 325 ? 37.475  117.306 -11.366 1.00 42.65 ? 325  ARG B NE  1 
ATOM   6179 C  CZ  . ARG B 2 325 ? 36.980  116.511 -10.418 1.00 43.48 ? 325  ARG B CZ  1 
ATOM   6180 N  NH1 . ARG B 2 325 ? 36.469  117.011 -9.303  1.00 44.40 ? 325  ARG B NH1 1 
ATOM   6181 N  NH2 . ARG B 2 325 ? 36.998  115.201 -10.590 1.00 44.07 ? 325  ARG B NH2 1 
ATOM   6182 N  N   . PHE B 2 326 ? 33.737  118.065 -15.513 1.00 30.86 ? 326  PHE B N   1 
ATOM   6183 C  CA  . PHE B 2 326 ? 33.490  117.445 -16.841 1.00 30.66 ? 326  PHE B CA  1 
ATOM   6184 C  C   . PHE B 2 326 ? 32.782  118.438 -17.776 1.00 30.94 ? 326  PHE B C   1 
ATOM   6185 O  O   . PHE B 2 326 ? 33.144  118.488 -18.971 1.00 28.02 ? 326  PHE B O   1 
ATOM   6186 C  CB  . PHE B 2 326 ? 32.682  116.149 -16.747 1.00 29.56 ? 326  PHE B CB  1 
ATOM   6187 C  CG  . PHE B 2 326 ? 32.569  115.437 -18.072 1.00 30.16 ? 326  PHE B CG  1 
ATOM   6188 C  CD1 . PHE B 2 326 ? 33.677  114.830 -18.645 1.00 30.77 ? 326  PHE B CD1 1 
ATOM   6189 C  CD2 . PHE B 2 326 ? 31.376  115.418 -18.771 1.00 30.40 ? 326  PHE B CD2 1 
ATOM   6190 C  CE1 . PHE B 2 326 ? 33.579  114.188 -19.870 1.00 31.53 ? 326  PHE B CE1 1 
ATOM   6191 C  CE2 . PHE B 2 326 ? 31.277  114.777 -19.997 1.00 30.70 ? 326  PHE B CE2 1 
ATOM   6192 C  CZ  . PHE B 2 326 ? 32.380  114.168 -20.547 1.00 32.04 ? 326  PHE B CZ  1 
ATOM   6193 N  N   . LEU B 2 327 ? 31.791  119.177 -17.268 1.00 31.63 ? 327  LEU B N   1 
ATOM   6194 C  CA  . LEU B 2 327 ? 31.035  120.182 -18.070 1.00 33.47 ? 327  LEU B CA  1 
ATOM   6195 C  C   . LEU B 2 327 ? 32.001  121.250 -18.601 1.00 31.83 ? 327  LEU B C   1 
ATOM   6196 O  O   . LEU B 2 327 ? 31.901  121.565 -19.795 1.00 31.56 ? 327  LEU B O   1 
ATOM   6197 C  CB  . LEU B 2 327 ? 29.919  120.803 -17.227 1.00 33.92 ? 327  LEU B CB  1 
ATOM   6198 C  CG  . LEU B 2 327 ? 28.629  119.990 -17.174 1.00 37.34 ? 327  LEU B CG  1 
ATOM   6199 C  CD1 . LEU B 2 327 ? 27.844  120.280 -15.896 1.00 39.06 ? 327  LEU B CD1 1 
ATOM   6200 C  CD2 . LEU B 2 327 ? 27.775  120.261 -18.398 1.00 37.50 ? 327  LEU B CD2 1 
ATOM   6201 N  N   . ARG B 2 328 ? 32.892  121.772 -17.752 1.00 34.38 ? 328  ARG B N   1 
ATOM   6202 C  CA  . ARG B 2 328 ? 33.899  122.808 -18.123 1.00 37.60 ? 328  ARG B CA  1 
ATOM   6203 C  C   . ARG B 2 328 ? 34.857  122.243 -19.173 1.00 36.30 ? 328  ARG B C   1 
ATOM   6204 O  O   . ARG B 2 328 ? 35.155  122.957 -20.149 1.00 37.05 ? 328  ARG B O   1 
ATOM   6205 C  CB  . ARG B 2 328 ? 34.711  123.260 -16.906 1.00 41.34 ? 328  ARG B CB  1 
ATOM   6206 C  CG  . ARG B 2 328 ? 33.945  124.180 -15.968 1.00 48.69 ? 328  ARG B CG  1 
ATOM   6207 C  CD  . ARG B 2 328 ? 34.695  124.477 -14.684 1.00 53.13 ? 328  ARG B CD  1 
ATOM   6208 N  NE  . ARG B 2 328 ? 33.751  124.637 -13.582 1.00 59.59 ? 328  ARG B NE  1 
ATOM   6209 C  CZ  . ARG B 2 328 ? 33.630  123.824 -12.527 1.00 64.09 ? 328  ARG B CZ  1 
ATOM   6210 N  NH1 . ARG B 2 328 ? 32.713  124.084 -11.608 1.00 63.85 ? 328  ARG B NH1 1 
ATOM   6211 N  NH2 . ARG B 2 328 ? 34.418  122.769 -12.378 1.00 63.87 ? 328  ARG B NH2 1 
ATOM   6212 N  N   . LEU B 2 329 ? 35.323  121.010 -18.953 1.00 34.77 ? 329  LEU B N   1 
ATOM   6213 C  CA  . LEU B 2 329 ? 36.248  120.282 -19.858 1.00 36.53 ? 329  LEU B CA  1 
ATOM   6214 C  C   . LEU B 2 329 ? 35.609  120.184 -21.248 1.00 33.04 ? 329  LEU B C   1 
ATOM   6215 O  O   . LEU B 2 329 ? 36.281  120.528 -22.238 1.00 31.59 ? 329  LEU B O   1 
ATOM   6216 C  CB  . LEU B 2 329 ? 36.516  118.890 -19.272 1.00 40.69 ? 329  LEU B CB  1 
ATOM   6217 C  CG  . LEU B 2 329 ? 37.895  118.299 -19.541 1.00 44.90 ? 329  LEU B CG  1 
ATOM   6218 C  CD1 . LEU B 2 329 ? 38.984  119.154 -18.910 1.00 45.90 ? 329  LEU B CD1 1 
ATOM   6219 C  CD2 . LEU B 2 329 ? 37.971  116.868 -19.024 1.00 45.81 ? 329  LEU B CD2 1 
ATOM   6220 N  N   . ALA B 2 330 ? 34.356  119.729 -21.299 1.00 31.42 ? 330  ALA B N   1 
ATOM   6221 C  CA  . ALA B 2 330 ? 33.618  119.388 -22.539 1.00 32.78 ? 330  ALA B CA  1 
ATOM   6222 C  C   . ALA B 2 330 ? 33.385  120.643 -23.392 1.00 34.15 ? 330  ALA B C   1 
ATOM   6223 O  O   . ALA B 2 330 ? 33.361  120.523 -24.634 1.00 34.79 ? 330  ALA B O   1 
ATOM   6224 C  CB  . ALA B 2 330 ? 32.323  118.708 -22.197 1.00 32.42 ? 330  ALA B CB  1 
ATOM   6225 N  N   . ALA B 2 331 ? 33.220  121.802 -22.756 1.00 35.40 ? 331  ALA B N   1 
ATOM   6226 C  CA  . ALA B 2 331 ? 32.999  123.098 -23.440 1.00 38.57 ? 331  ALA B CA  1 
ATOM   6227 C  C   . ALA B 2 331 ? 34.143  123.375 -24.430 1.00 39.88 ? 331  ALA B C   1 
ATOM   6228 O  O   . ALA B 2 331 ? 33.872  124.007 -25.455 1.00 38.97 ? 331  ALA B O   1 
ATOM   6229 C  CB  . ALA B 2 331 ? 32.853  124.202 -22.426 1.00 37.33 ? 331  ALA B CB  1 
ATOM   6230 N  N   . HIS B 2 332 ? 35.363  122.890 -24.157 1.00 42.32 ? 332  HIS B N   1 
ATOM   6231 C  CA  . HIS B 2 332 ? 36.566  123.107 -25.013 1.00 42.50 ? 332  HIS B CA  1 
ATOM   6232 C  C   . HIS B 2 332 ? 36.789  121.949 -25.992 1.00 39.98 ? 332  HIS B C   1 
ATOM   6233 O  O   . HIS B 2 332 ? 37.858  121.941 -26.625 1.00 42.84 ? 332  HIS B O   1 
ATOM   6234 C  CB  . HIS B 2 332 ? 37.819  123.301 -24.158 1.00 46.92 ? 332  HIS B CB  1 
ATOM   6235 C  CG  . HIS B 2 332 ? 37.691  124.388 -23.149 1.00 54.96 ? 332  HIS B CG  1 
ATOM   6236 N  ND1 . HIS B 2 332 ? 37.790  124.147 -21.792 1.00 60.16 ? 332  HIS B ND1 1 
ATOM   6237 C  CD2 . HIS B 2 332 ? 37.457  125.711 -23.288 1.00 59.15 ? 332  HIS B CD2 1 
ATOM   6238 C  CE1 . HIS B 2 332 ? 37.625  125.279 -21.137 1.00 61.15 ? 332  HIS B CE1 1 
ATOM   6239 N  NE2 . HIS B 2 332 ? 37.419  126.254 -22.031 1.00 61.94 ? 332  HIS B NE2 1 
ATOM   6240 N  N   . HIS B 2 333 ? 35.839  121.020 -26.122 1.00 35.45 ? 333  HIS B N   1 
ATOM   6241 C  CA  . HIS B 2 333 ? 35.963  119.818 -26.989 1.00 36.72 ? 333  HIS B CA  1 
ATOM   6242 C  C   . HIS B 2 333 ? 34.963  119.898 -28.144 1.00 38.35 ? 333  HIS B C   1 
ATOM   6243 O  O   . HIS B 2 333 ? 33.757  119.991 -27.881 1.00 39.21 ? 333  HIS B O   1 
ATOM   6244 C  CB  . HIS B 2 333 ? 35.798  118.531 -26.171 1.00 34.44 ? 333  HIS B CB  1 
ATOM   6245 C  CG  . HIS B 2 333 ? 37.050  118.126 -25.474 1.00 33.50 ? 333  HIS B CG  1 
ATOM   6246 N  ND1 . HIS B 2 333 ? 37.914  117.175 -25.993 1.00 33.26 ? 333  HIS B ND1 1 
ATOM   6247 C  CD2 . HIS B 2 333 ? 37.620  118.580 -24.339 1.00 33.06 ? 333  HIS B CD2 1 
ATOM   6248 C  CE1 . HIS B 2 333 ? 38.943  117.038 -25.186 1.00 32.49 ? 333  HIS B CE1 1 
ATOM   6249 N  NE2 . HIS B 2 333 ? 38.791  117.900 -24.165 1.00 33.20 ? 333  HIS B NE2 1 
ATOM   6250 N  N   . ALA B 2 334 ? 35.460  119.829 -29.378 1.00 41.18 ? 334  ALA B N   1 
ATOM   6251 C  CA  . ALA B 2 334 ? 34.635  119.798 -30.610 1.00 41.80 ? 334  ALA B CA  1 
ATOM   6252 C  C   . ALA B 2 334 ? 34.042  118.396 -30.800 1.00 39.77 ? 334  ALA B C   1 
ATOM   6253 O  O   . ALA B 2 334 ? 32.960  118.294 -31.408 1.00 39.63 ? 334  ALA B O   1 
ATOM   6254 C  CB  . ALA B 2 334 ? 35.465  120.212 -31.802 1.00 43.78 ? 334  ALA B CB  1 
ATOM   6255 N  N   . ASN B 2 335 ? 34.723  117.352 -30.313 1.00 38.32 ? 335  ASN B N   1 
ATOM   6256 C  CA  . ASN B 2 335 ? 34.267  115.944 -30.481 1.00 37.42 ? 335  ASN B CA  1 
ATOM   6257 C  C   . ASN B 2 335 ? 33.900  115.371 -29.110 1.00 35.66 ? 335  ASN B C   1 
ATOM   6258 O  O   . ASN B 2 335 ? 34.806  114.928 -28.394 1.00 37.22 ? 335  ASN B O   1 
ATOM   6259 C  CB  . ASN B 2 335 ? 35.311  115.084 -31.200 1.00 37.65 ? 335  ASN B CB  1 
ATOM   6260 C  CG  . ASN B 2 335 ? 34.770  113.733 -31.623 1.00 38.53 ? 335  ASN B CG  1 
ATOM   6261 O  OD1 . ASN B 2 335 ? 33.746  113.270 -31.118 1.00 38.12 ? 335  ASN B OD1 1 
ATOM   6262 N  ND2 . ASN B 2 335 ? 35.452  113.088 -32.555 1.00 38.52 ? 335  ASN B ND2 1 
ATOM   6263 N  N   . ILE B 2 336 ? 32.609  115.346 -28.785 1.00 34.60 ? 336  ILE B N   1 
ATOM   6264 C  CA  . ILE B 2 336 ? 32.104  114.894 -27.454 1.00 35.81 ? 336  ILE B CA  1 
ATOM   6265 C  C   . ILE B 2 336 ? 32.205  113.367 -27.359 1.00 35.04 ? 336  ILE B C   1 
ATOM   6266 O  O   . ILE B 2 336 ? 32.524  112.879 -26.267 1.00 33.57 ? 336  ILE B O   1 
ATOM   6267 C  CB  . ILE B 2 336 ? 30.673  115.409 -27.200 1.00 37.68 ? 336  ILE B CB  1 
ATOM   6268 C  CG1 . ILE B 2 336 ? 30.641  116.939 -27.128 1.00 38.61 ? 336  ILE B CG1 1 
ATOM   6269 C  CG2 . ILE B 2 336 ? 30.078  114.775 -25.947 1.00 39.03 ? 336  ILE B CG2 1 
ATOM   6270 C  CD1 . ILE B 2 336 ? 31.598  117.540 -26.110 1.00 37.97 ? 336  ILE B CD1 1 
ATOM   6271 N  N   . GLU B 2 337 ? 31.945  112.645 -28.452 1.00 35.19 ? 337  GLU B N   1 
ATOM   6272 C  CA  . GLU B 2 337 ? 32.048  111.164 -28.482 1.00 36.52 ? 337  GLU B CA  1 
ATOM   6273 C  C   . GLU B 2 337 ? 33.472  110.765 -28.084 1.00 34.73 ? 337  GLU B C   1 
ATOM   6274 O  O   . GLU B 2 337 ? 33.611  109.923 -27.192 1.00 35.69 ? 337  GLU B O   1 
ATOM   6275 C  CB  . GLU B 2 337 ? 31.695  110.598 -29.856 1.00 40.66 ? 337  GLU B CB  1 
ATOM   6276 C  CG  . GLU B 2 337 ? 31.776  109.076 -29.905 1.00 44.26 ? 337  GLU B CG  1 
ATOM   6277 C  CD  . GLU B 2 337 ? 31.193  108.419 -31.148 1.00 47.59 ? 337  GLU B CD  1 
ATOM   6278 O  OE1 . GLU B 2 337 ? 30.660  109.146 -32.015 1.00 49.88 ? 337  GLU B OE1 1 
ATOM   6279 O  OE2 . GLU B 2 337 ? 31.269  107.176 -31.247 1.00 48.67 ? 337  GLU B OE2 1 
ATOM   6280 N  N   . GLU B 2 338 ? 34.477  111.375 -28.715 1.00 32.78 ? 338  GLU B N   1 
ATOM   6281 C  CA  . GLU B 2 338 ? 35.917  111.122 -28.448 1.00 32.90 ? 338  GLU B CA  1 
ATOM   6282 C  C   . GLU B 2 338 ? 36.236  111.418 -26.976 1.00 31.68 ? 338  GLU B C   1 
ATOM   6283 O  O   . GLU B 2 338 ? 36.906  110.579 -26.328 1.00 30.20 ? 338  GLU B O   1 
ATOM   6284 C  CB  . GLU B 2 338 ? 36.774  111.972 -29.385 1.00 34.80 ? 338  GLU B CB  1 
ATOM   6285 C  CG  . GLU B 2 338 ? 38.257  111.665 -29.315 1.00 37.21 ? 338  GLU B CG  1 
ATOM   6286 C  CD  . GLU B 2 338 ? 39.098  112.601 -30.169 1.00 38.63 ? 338  GLU B CD  1 
ATOM   6287 O  OE1 . GLU B 2 338 ? 39.249  113.771 -29.780 1.00 39.63 ? 338  GLU B OE1 1 
ATOM   6288 O  OE2 . GLU B 2 338 ? 39.566  112.168 -31.230 1.00 41.39 ? 338  GLU B OE2 1 
ATOM   6289 N  N   . LEU B 2 339 ? 35.798  112.569 -26.461 1.00 29.83 ? 339  LEU B N   1 
ATOM   6290 C  CA  . LEU B 2 339 ? 36.025  112.946 -25.038 1.00 31.89 ? 339  LEU B CA  1 
ATOM   6291 C  C   . LEU B 2 339 ? 35.496  111.833 -24.116 1.00 29.76 ? 339  LEU B C   1 
ATOM   6292 O  O   . LEU B 2 339 ? 36.207  111.481 -23.150 1.00 29.43 ? 339  LEU B O   1 
ATOM   6293 C  CB  . LEU B 2 339 ? 35.349  114.291 -24.751 1.00 32.39 ? 339  LEU B CB  1 
ATOM   6294 C  CG  . LEU B 2 339 ? 35.390  114.756 -23.298 1.00 32.79 ? 339  LEU B CG  1 
ATOM   6295 C  CD1 . LEU B 2 339 ? 36.817  114.977 -22.832 1.00 32.75 ? 339  LEU B CD1 1 
ATOM   6296 C  CD2 . LEU B 2 339 ? 34.567  116.024 -23.120 1.00 33.65 ? 339  LEU B CD2 1 
ATOM   6297 N  N   . LEU B 2 340 ? 34.320  111.282 -24.430 1.00 29.41 ? 340  LEU B N   1 
ATOM   6298 C  CA  . LEU B 2 340 ? 33.625  110.248 -23.615 1.00 30.82 ? 340  LEU B CA  1 
ATOM   6299 C  C   . LEU B 2 340 ? 34.374  108.916 -23.712 1.00 30.68 ? 340  LEU B C   1 
ATOM   6300 O  O   . LEU B 2 340 ? 34.526  108.245 -22.671 1.00 29.78 ? 340  LEU B O   1 
ATOM   6301 C  CB  . LEU B 2 340 ? 32.181  110.087 -24.097 1.00 31.95 ? 340  LEU B CB  1 
ATOM   6302 C  CG  . LEU B 2 340 ? 31.120  110.828 -23.290 1.00 34.43 ? 340  LEU B CG  1 
ATOM   6303 C  CD1 . LEU B 2 340 ? 29.737  110.526 -23.848 1.00 36.08 ? 340  LEU B CD1 1 
ATOM   6304 C  CD2 . LEU B 2 340 ? 31.192  110.476 -21.808 1.00 34.98 ? 340  LEU B CD2 1 
ATOM   6305 N  N   . VAL B 2 341 ? 34.813  108.554 -24.919 1.00 30.16 ? 341  VAL B N   1 
ATOM   6306 C  CA  . VAL B 2 341 ? 35.666  107.358 -25.177 1.00 29.89 ? 341  VAL B CA  1 
ATOM   6307 C  C   . VAL B 2 341 ? 36.913  107.454 -24.298 1.00 28.61 ? 341  VAL B C   1 
ATOM   6308 O  O   . VAL B 2 341 ? 37.306  106.432 -23.720 1.00 29.53 ? 341  VAL B O   1 
ATOM   6309 C  CB  . VAL B 2 341 ? 36.020  107.232 -26.672 1.00 31.27 ? 341  VAL B CB  1 
ATOM   6310 C  CG1 . VAL B 2 341 ? 37.166  106.256 -26.909 1.00 32.69 ? 341  VAL B CG1 1 
ATOM   6311 C  CG2 . VAL B 2 341 ? 34.801  106.834 -27.486 1.00 31.46 ? 341  VAL B CG2 1 
ATOM   6312 N  N   . ASP B 2 342 ? 37.498  108.647 -24.188 1.00 29.12 ? 342  ASP B N   1 
ATOM   6313 C  CA  . ASP B 2 342 ? 38.746  108.885 -23.418 1.00 29.12 ? 342  ASP B CA  1 
ATOM   6314 C  C   . ASP B 2 342 ? 38.439  108.967 -21.914 1.00 29.00 ? 342  ASP B C   1 
ATOM   6315 O  O   . ASP B 2 342 ? 39.355  108.668 -21.124 1.00 29.55 ? 342  ASP B O   1 
ATOM   6316 C  CB  . ASP B 2 342 ? 39.462  110.141 -23.923 1.00 29.60 ? 342  ASP B CB  1 
ATOM   6317 C  CG  . ASP B 2 342 ? 40.045  109.994 -25.326 1.00 34.14 ? 342  ASP B CG  1 
ATOM   6318 O  OD1 . ASP B 2 342 ? 40.304  108.834 -25.755 1.00 32.97 ? 342  ASP B OD1 1 
ATOM   6319 O  OD2 . ASP B 2 342 ? 40.239  111.040 -25.992 1.00 34.65 ? 342  ASP B OD2 1 
ATOM   6320 N  N   . SER B 2 343 ? 37.220  109.364 -21.529 1.00 27.83 ? 343  SER B N   1 
ATOM   6321 C  CA  . SER B 2 343 ? 36.886  109.799 -20.137 1.00 28.13 ? 343  SER B CA  1 
ATOM   6322 C  C   . SER B 2 343 ? 36.018  108.790 -19.377 1.00 27.16 ? 343  SER B C   1 
ATOM   6323 O  O   . SER B 2 343 ? 35.979  108.901 -18.154 1.00 28.14 ? 343  SER B O   1 
ATOM   6324 C  CB  . SER B 2 343 ? 36.198  111.146 -20.140 1.00 28.17 ? 343  SER B CB  1 
ATOM   6325 O  OG  . SER B 2 343 ? 37.003  112.127 -20.769 1.00 30.68 ? 343  SER B OG  1 
ATOM   6326 N  N   . PHE B 2 344 ? 35.300  107.892 -20.054 1.00 27.31 ? 344  PHE B N   1 
ATOM   6327 C  CA  . PHE B 2 344 ? 34.163  107.137 -19.453 1.00 26.58 ? 344  PHE B CA  1 
ATOM   6328 C  C   . PHE B 2 344 ? 34.598  106.429 -18.158 1.00 25.60 ? 344  PHE B C   1 
ATOM   6329 O  O   . PHE B 2 344 ? 33.787  106.421 -17.225 1.00 24.90 ? 344  PHE B O   1 
ATOM   6330 C  CB  . PHE B 2 344 ? 33.526  106.176 -20.461 1.00 25.29 ? 344  PHE B CB  1 
ATOM   6331 C  CG  . PHE B 2 344 ? 34.309  104.916 -20.717 1.00 24.73 ? 344  PHE B CG  1 
ATOM   6332 C  CD1 . PHE B 2 344 ? 34.123  103.791 -19.928 1.00 24.99 ? 344  PHE B CD1 1 
ATOM   6333 C  CD2 . PHE B 2 344 ? 35.230  104.856 -21.748 1.00 24.22 ? 344  PHE B CD2 1 
ATOM   6334 C  CE1 . PHE B 2 344 ? 34.857  102.638 -20.156 1.00 25.44 ? 344  PHE B CE1 1 
ATOM   6335 C  CE2 . PHE B 2 344 ? 35.967  103.704 -21.976 1.00 23.97 ? 344  PHE B CE2 1 
ATOM   6336 C  CZ  . PHE B 2 344 ? 35.779  102.595 -21.181 1.00 25.16 ? 344  PHE B CZ  1 
ATOM   6337 N  N   . GLN B 2 345 ? 35.818  105.873 -18.094 1.00 26.38 ? 345  GLN B N   1 
ATOM   6338 C  CA  . GLN B 2 345 ? 36.312  105.093 -16.921 1.00 26.46 ? 345  GLN B CA  1 
ATOM   6339 C  C   . GLN B 2 345 ? 36.241  105.955 -15.654 1.00 26.59 ? 345  GLN B C   1 
ATOM   6340 O  O   . GLN B 2 345 ? 35.982  105.394 -14.581 1.00 24.48 ? 345  GLN B O   1 
ATOM   6341 C  CB  . GLN B 2 345 ? 37.724  104.528 -17.132 1.00 27.43 ? 345  GLN B CB  1 
ATOM   6342 C  CG  . GLN B 2 345 ? 38.837  105.566 -17.214 1.00 27.77 ? 345  GLN B CG  1 
ATOM   6343 C  CD  . GLN B 2 345 ? 38.961  106.229 -18.567 1.00 27.77 ? 345  GLN B CD  1 
ATOM   6344 O  OE1 . GLN B 2 345 ? 38.490  105.725 -19.583 1.00 28.97 ? 345  GLN B OE1 1 
ATOM   6345 N  NE2 . GLN B 2 345 ? 39.619  107.375 -18.591 1.00 28.51 ? 345  GLN B NE2 1 
ATOM   6346 N  N   . ASP B 2 346 ? 36.444  107.269 -15.781 1.00 27.88 ? 346  ASP B N   1 
ATOM   6347 C  CA  . ASP B 2 346 ? 36.488  108.214 -14.634 1.00 29.46 ? 346  ASP B CA  1 
ATOM   6348 C  C   . ASP B 2 346 ? 35.125  108.269 -13.934 1.00 28.10 ? 346  ASP B C   1 
ATOM   6349 O  O   . ASP B 2 346 ? 35.106  108.588 -12.735 1.00 26.83 ? 346  ASP B O   1 
ATOM   6350 C  CB  . ASP B 2 346 ? 36.902  109.611 -15.088 1.00 32.24 ? 346  ASP B CB  1 
ATOM   6351 C  CG  . ASP B 2 346 ? 38.357  109.721 -15.506 1.00 34.58 ? 346  ASP B CG  1 
ATOM   6352 O  OD1 . ASP B 2 346 ? 38.992  108.681 -15.757 1.00 36.15 ? 346  ASP B OD1 1 
ATOM   6353 O  OD2 . ASP B 2 346 ? 38.836  110.848 -15.590 1.00 41.73 ? 346  ASP B OD2 1 
ATOM   6354 N  N   . PHE B 2 347 ? 34.042  107.958 -14.658 1.00 28.29 ? 347  PHE B N   1 
ATOM   6355 C  CA  . PHE B 2 347 ? 32.644  107.966 -14.153 1.00 28.44 ? 347  PHE B CA  1 
ATOM   6356 C  C   . PHE B 2 347 ? 32.434  106.846 -13.119 1.00 27.12 ? 347  PHE B C   1 
ATOM   6357 O  O   . PHE B 2 347 ? 31.529  107.006 -12.270 1.00 24.69 ? 347  PHE B O   1 
ATOM   6358 C  CB  . PHE B 2 347 ? 31.644  107.890 -15.309 1.00 29.10 ? 347  PHE B CB  1 
ATOM   6359 C  CG  . PHE B 2 347 ? 31.457  109.185 -16.062 1.00 30.33 ? 347  PHE B CG  1 
ATOM   6360 C  CD1 . PHE B 2 347 ? 32.378  109.598 -17.014 1.00 30.60 ? 347  PHE B CD1 1 
ATOM   6361 C  CD2 . PHE B 2 347 ? 30.345  109.982 -15.833 1.00 30.68 ? 347  PHE B CD2 1 
ATOM   6362 C  CE1 . PHE B 2 347 ? 32.202  110.790 -17.703 1.00 31.18 ? 347  PHE B CE1 1 
ATOM   6363 C  CE2 . PHE B 2 347 ? 30.165  111.167 -16.529 1.00 30.76 ? 347  PHE B CE2 1 
ATOM   6364 C  CZ  . PHE B 2 347 ? 31.096  111.573 -17.461 1.00 31.11 ? 347  PHE B CZ  1 
ATOM   6365 N  N   . ALA B 2 348 ? 33.244  105.780 -13.161 1.00 26.60 ? 348  ALA B N   1 
ATOM   6366 C  CA  . ALA B 2 348 ? 33.247  104.678 -12.160 1.00 29.06 ? 348  ALA B CA  1 
ATOM   6367 C  C   . ALA B 2 348 ? 33.452  105.254 -10.754 1.00 29.51 ? 348  ALA B C   1 
ATOM   6368 O  O   . ALA B 2 348 ? 33.021  104.616 -9.792  1.00 29.78 ? 348  ALA B O   1 
ATOM   6369 C  CB  . ALA B 2 348 ? 34.311  103.642 -12.468 1.00 28.89 ? 348  ALA B CB  1 
ATOM   6370 N  N   . ASP B 2 349 ? 34.068  106.432 -10.658 1.00 31.56 ? 349  ASP B N   1 
ATOM   6371 C  CA  . ASP B 2 349 ? 34.398  107.099 -9.372  1.00 34.24 ? 349  ASP B CA  1 
ATOM   6372 C  C   . ASP B 2 349 ? 33.163  107.761 -8.738  1.00 32.42 ? 349  ASP B C   1 
ATOM   6373 O  O   . ASP B 2 349 ? 33.264  108.154 -7.569  1.00 31.73 ? 349  ASP B O   1 
ATOM   6374 C  CB  . ASP B 2 349 ? 35.512  108.120 -9.577  1.00 38.45 ? 349  ASP B CB  1 
ATOM   6375 C  CG  . ASP B 2 349 ? 36.448  108.201 -8.392  1.00 44.06 ? 349  ASP B CG  1 
ATOM   6376 O  OD1 . ASP B 2 349 ? 37.147  107.199 -8.140  1.00 50.73 ? 349  ASP B OD1 1 
ATOM   6377 O  OD2 . ASP B 2 349 ? 36.453  109.253 -7.727  1.00 47.45 ? 349  ASP B OD2 1 
ATOM   6378 N  N   . LEU B 2 350 ? 32.043  107.871 -9.458  1.00 29.98 ? 350  LEU B N   1 
ATOM   6379 C  CA  . LEU B 2 350 ? 30.821  108.579 -8.979  1.00 30.58 ? 350  LEU B CA  1 
ATOM   6380 C  C   . LEU B 2 350 ? 30.079  107.752 -7.919  1.00 30.61 ? 350  LEU B C   1 
ATOM   6381 O  O   . LEU B 2 350 ? 29.502  108.367 -7.007  1.00 30.10 ? 350  LEU B O   1 
ATOM   6382 C  CB  . LEU B 2 350 ? 29.899  108.862 -10.169 1.00 31.82 ? 350  LEU B CB  1 
ATOM   6383 C  CG  . LEU B 2 350 ? 30.425  109.875 -11.185 1.00 32.19 ? 350  LEU B CG  1 
ATOM   6384 C  CD1 . LEU B 2 350 ? 29.510  109.956 -12.394 1.00 32.99 ? 350  LEU B CD1 1 
ATOM   6385 C  CD2 . LEU B 2 350 ? 30.585  111.248 -10.551 1.00 32.68 ? 350  LEU B CD2 1 
ATOM   6386 N  N   . MET B 2 351 ? 30.048  106.422 -8.062  1.00 29.43 ? 351  MET B N   1 
ATOM   6387 C  CA  . MET B 2 351 ? 29.259  105.522 -7.178  1.00 30.08 ? 351  MET B CA  1 
ATOM   6388 C  C   . MET B 2 351 ? 29.953  104.168 -7.095  1.00 29.42 ? 351  MET B C   1 
ATOM   6389 O  O   . MET B 2 351 ? 30.748  103.839 -7.972  1.00 30.19 ? 351  MET B O   1 
ATOM   6390 C  CB  . MET B 2 351 ? 27.840  105.342 -7.728  1.00 31.18 ? 351  MET B CB  1 
ATOM   6391 C  CG  . MET B 2 351 ? 27.783  104.491 -8.976  1.00 31.84 ? 351  MET B CG  1 
ATOM   6392 S  SD  . MET B 2 351 ? 26.136  104.397 -9.704  1.00 32.49 ? 351  MET B SD  1 
ATOM   6393 C  CE  . MET B 2 351 ? 26.052  105.984 -10.532 1.00 31.31 ? 351  MET B CE  1 
ATOM   6394 N  N   . PRO B 2 352 ? 29.689  103.342 -6.055  1.00 28.78 ? 352  PRO B N   1 
ATOM   6395 C  CA  . PRO B 2 352 ? 30.280  102.008 -5.984  1.00 27.53 ? 352  PRO B CA  1 
ATOM   6396 C  C   . PRO B 2 352 ? 29.864  101.159 -7.190  1.00 25.23 ? 352  PRO B C   1 
ATOM   6397 O  O   . PRO B 2 352 ? 28.676  101.034 -7.472  1.00 25.95 ? 352  PRO B O   1 
ATOM   6398 C  CB  . PRO B 2 352 ? 29.748  101.432 -4.663  1.00 27.71 ? 352  PRO B CB  1 
ATOM   6399 C  CG  . PRO B 2 352 ? 29.394  102.663 -3.853  1.00 27.85 ? 352  PRO B CG  1 
ATOM   6400 C  CD  . PRO B 2 352 ? 28.864  103.643 -4.875  1.00 27.35 ? 352  PRO B CD  1 
ATOM   6401 N  N   . CYS B 2 353 ? 30.853  100.591 -7.876  1.00 25.08 ? 353  CYS B N   1 
ATOM   6402 C  CA  . CYS B 2 353 ? 30.633  99.676  -9.024  1.00 25.64 ? 353  CYS B CA  1 
ATOM   6403 C  C   . CYS B 2 353 ? 31.892  98.842  -9.273  1.00 24.47 ? 353  CYS B C   1 
ATOM   6404 O  O   . CYS B 2 353 ? 32.963  99.225  -8.794  1.00 23.89 ? 353  CYS B O   1 
ATOM   6405 C  CB  . CYS B 2 353 ? 30.205  100.459 -10.264 1.00 25.69 ? 353  CYS B CB  1 
ATOM   6406 S  SG  . CYS B 2 353 ? 31.459  101.609 -10.887 1.00 26.98 ? 353  CYS B SG  1 
ATOM   6407 N  N   . ASP B 2 354 ? 31.744  97.715  -9.968  1.00 24.25 ? 354  ASP B N   1 
ATOM   6408 C  CA  . ASP B 2 354 ? 32.857  96.791  -10.309 1.00 24.34 ? 354  ASP B CA  1 
ATOM   6409 C  C   . ASP B 2 354 ? 33.277  97.022  -11.763 1.00 23.95 ? 354  ASP B C   1 
ATOM   6410 O  O   . ASP B 2 354 ? 34.381  96.589  -12.149 1.00 24.70 ? 354  ASP B O   1 
ATOM   6411 C  CB  . ASP B 2 354 ? 32.435  95.351  -10.010 1.00 25.17 ? 354  ASP B CB  1 
ATOM   6412 C  CG  . ASP B 2 354 ? 32.133  95.160  -8.537  1.00 25.76 ? 354  ASP B CG  1 
ATOM   6413 O  OD1 . ASP B 2 354 ? 32.978  95.573  -7.729  1.00 28.21 ? 354  ASP B OD1 1 
ATOM   6414 O  OD2 . ASP B 2 354 ? 31.038  94.657  -8.205  1.00 26.05 ? 354  ASP B OD2 1 
ATOM   6415 N  N   . GLY B 2 355 ? 32.422  97.666  -12.555 1.00 23.91 ? 355  GLY B N   1 
ATOM   6416 C  CA  . GLY B 2 355 ? 32.719  97.945  -13.971 1.00 23.55 ? 355  GLY B CA  1 
ATOM   6417 C  C   . GLY B 2 355 ? 31.901  99.102  -14.490 1.00 23.83 ? 355  GLY B C   1 
ATOM   6418 O  O   . GLY B 2 355 ? 30.905  99.488  -13.841 1.00 23.09 ? 355  GLY B O   1 
ATOM   6419 N  N   . VAL B 2 356 ? 32.341  99.652  -15.611 1.00 23.77 ? 356  VAL B N   1 
ATOM   6420 C  CA  . VAL B 2 356 ? 31.656  100.763 -16.324 1.00 24.94 ? 356  VAL B CA  1 
ATOM   6421 C  C   . VAL B 2 356 ? 32.006  100.625 -17.803 1.00 26.04 ? 356  VAL B C   1 
ATOM   6422 O  O   . VAL B 2 356 ? 33.119  100.139 -18.116 1.00 25.17 ? 356  VAL B O   1 
ATOM   6423 C  CB  . VAL B 2 356 ? 32.057  102.139 -15.760 1.00 25.30 ? 356  VAL B CB  1 
ATOM   6424 C  CG1 . VAL B 2 356 ? 33.501  102.490 -16.081 1.00 26.07 ? 356  VAL B CG1 1 
ATOM   6425 C  CG2 . VAL B 2 356 ? 31.122  103.231 -16.242 1.00 27.18 ? 356  VAL B CG2 1 
ATOM   6426 N  N   . GLY B 2 357 ? 31.080  101.015 -18.673 1.00 26.66 ? 357  GLY B N   1 
ATOM   6427 C  CA  . GLY B 2 357 ? 31.301  100.955 -20.122 1.00 27.72 ? 357  GLY B CA  1 
ATOM   6428 C  C   . GLY B 2 357 ? 30.485  101.988 -20.861 1.00 27.94 ? 357  GLY B C   1 
ATOM   6429 O  O   . GLY B 2 357 ? 29.483  102.502 -20.302 1.00 28.52 ? 357  GLY B O   1 
ATOM   6430 N  N   . LEU B 2 358 ? 30.911  102.272 -22.084 1.00 27.96 ? 358  LEU B N   1 
ATOM   6431 C  CA  . LEU B 2 358 ? 30.265  103.242 -22.991 1.00 28.19 ? 358  LEU B CA  1 
ATOM   6432 C  C   . LEU B 2 358 ? 29.727  102.464 -24.190 1.00 28.36 ? 358  LEU B C   1 
ATOM   6433 O  O   . LEU B 2 358 ? 30.520  101.772 -24.848 1.00 28.11 ? 358  LEU B O   1 
ATOM   6434 C  CB  . LEU B 2 358 ? 31.309  104.281 -23.408 1.00 29.84 ? 358  LEU B CB  1 
ATOM   6435 C  CG  . LEU B 2 358 ? 30.785  105.427 -24.269 1.00 30.29 ? 358  LEU B CG  1 
ATOM   6436 C  CD1 . LEU B 2 358 ? 29.843  106.316 -23.474 1.00 31.85 ? 358  LEU B CD1 1 
ATOM   6437 C  CD2 . LEU B 2 358 ? 31.935  106.242 -24.824 1.00 31.18 ? 358  LEU B CD2 1 
ATOM   6438 N  N   . TRP B 2 359 ? 28.424  102.563 -24.444 1.00 27.87 ? 359  TRP B N   1 
ATOM   6439 C  CA  . TRP B 2 359 ? 27.763  101.991 -25.643 1.00 28.03 ? 359  TRP B CA  1 
ATOM   6440 C  C   . TRP B 2 359 ? 27.268  103.145 -26.517 1.00 28.51 ? 359  TRP B C   1 
ATOM   6441 O  O   . TRP B 2 359 ? 26.208  103.715 -26.215 1.00 28.54 ? 359  TRP B O   1 
ATOM   6442 C  CB  . TRP B 2 359 ? 26.649  101.030 -25.231 1.00 28.09 ? 359  TRP B CB  1 
ATOM   6443 C  CG  . TRP B 2 359 ? 25.914  100.416 -26.380 1.00 30.13 ? 359  TRP B CG  1 
ATOM   6444 C  CD1 . TRP B 2 359 ? 24.631  100.684 -26.754 1.00 31.72 ? 359  TRP B CD1 1 
ATOM   6445 C  CD2 . TRP B 2 359 ? 26.401  99.416  -27.296 1.00 31.62 ? 359  TRP B CD2 1 
ATOM   6446 N  NE1 . TRP B 2 359 ? 24.279  99.917  -27.828 1.00 32.11 ? 359  TRP B NE1 1 
ATOM   6447 C  CE2 . TRP B 2 359 ? 25.343  99.131  -28.188 1.00 32.57 ? 359  TRP B CE2 1 
ATOM   6448 C  CE3 . TRP B 2 359 ? 27.615  98.737  -27.457 1.00 31.82 ? 359  TRP B CE3 1 
ATOM   6449 C  CZ2 . TRP B 2 359 ? 25.470  98.202  -29.222 1.00 32.10 ? 359  TRP B CZ2 1 
ATOM   6450 C  CZ3 . TRP B 2 359 ? 27.741  97.819  -28.479 1.00 32.72 ? 359  TRP B CZ3 1 
ATOM   6451 C  CH2 . TRP B 2 359 ? 26.681  97.559  -29.351 1.00 32.46 ? 359  TRP B CH2 1 
ATOM   6452 N  N   . VAL B 2 360 ? 28.052  103.507 -27.530 1.00 29.17 ? 360  VAL B N   1 
ATOM   6453 C  CA  . VAL B 2 360 ? 27.747  104.627 -28.462 1.00 31.63 ? 360  VAL B CA  1 
ATOM   6454 C  C   . VAL B 2 360 ? 27.939  104.137 -29.897 1.00 32.61 ? 360  VAL B C   1 
ATOM   6455 O  O   . VAL B 2 360 ? 29.028  103.600 -30.197 1.00 28.05 ? 360  VAL B O   1 
ATOM   6456 C  CB  . VAL B 2 360 ? 28.628  105.853 -28.180 1.00 32.73 ? 360  VAL B CB  1 
ATOM   6457 C  CG1 . VAL B 2 360 ? 28.478  106.893 -29.279 1.00 34.30 ? 360  VAL B CG1 1 
ATOM   6458 C  CG2 . VAL B 2 360 ? 28.319  106.451 -26.821 1.00 33.23 ? 360  VAL B CG2 1 
ATOM   6459 N  N   . GLY B 2 361 ? 26.923  104.339 -30.744 1.00 34.14 ? 361  GLY B N   1 
ATOM   6460 C  CA  . GLY B 2 361 ? 26.984  104.029 -32.184 1.00 34.75 ? 361  GLY B CA  1 
ATOM   6461 C  C   . GLY B 2 361 ? 27.334  102.573 -32.419 1.00 35.14 ? 361  GLY B C   1 
ATOM   6462 O  O   . GLY B 2 361 ? 28.127  102.302 -33.340 1.00 37.56 ? 361  GLY B O   1 
ATOM   6463 N  N   . ASN B 2 362 ? 26.776  101.675 -31.599 1.00 35.24 ? 362  ASN B N   1 
ATOM   6464 C  CA  . ASN B 2 362 ? 26.957  100.198 -31.681 1.00 37.17 ? 362  ASN B CA  1 
ATOM   6465 C  C   . ASN B 2 362 ? 28.431  99.825  -31.482 1.00 33.48 ? 362  ASN B C   1 
ATOM   6466 O  O   . ASN B 2 362 ? 28.822  98.722  -31.916 1.00 33.22 ? 362  ASN B O   1 
ATOM   6467 C  CB  . ASN B 2 362 ? 26.419  99.624  -32.996 1.00 40.96 ? 362  ASN B CB  1 
ATOM   6468 C  CG  . ASN B 2 362 ? 24.956  99.944  -33.218 1.00 45.42 ? 362  ASN B CG  1 
ATOM   6469 O  OD1 . ASN B 2 362 ? 24.113  99.626  -32.382 1.00 49.38 ? 362  ASN B OD1 1 
ATOM   6470 N  ND2 . ASN B 2 362 ? 24.645  100.573 -34.341 1.00 50.52 ? 362  ASN B ND2 1 
ATOM   6471 N  N   . ASN B 2 363 ? 29.206  100.691 -30.822 1.00 32.06 ? 363  ASN B N   1 
ATOM   6472 C  CA  . ASN B 2 363 ? 30.595  100.395 -30.385 1.00 33.02 ? 363  ASN B CA  1 
ATOM   6473 C  C   . ASN B 2 363 ? 30.654  100.396 -28.855 1.00 32.31 ? 363  ASN B C   1 
ATOM   6474 O  O   . ASN B 2 363 ? 30.067  101.293 -28.220 1.00 29.90 ? 363  ASN B O   1 
ATOM   6475 C  CB  . ASN B 2 363 ? 31.606  101.350 -31.012 1.00 33.89 ? 363  ASN B CB  1 
ATOM   6476 C  CG  . ASN B 2 363 ? 31.702  101.141 -32.505 1.00 35.69 ? 363  ASN B CG  1 
ATOM   6477 O  OD1 . ASN B 2 363 ? 31.295  101.995 -33.289 1.00 40.55 ? 363  ASN B OD1 1 
ATOM   6478 N  ND2 . ASN B 2 363 ? 32.189  99.982  -32.905 1.00 38.22 ? 363  ASN B ND2 1 
ATOM   6479 N  N   . TRP B 2 364 ? 31.346  99.397  -28.311 1.00 30.54 ? 364  TRP B N   1 
ATOM   6480 C  CA  . TRP B 2 364 ? 31.533  99.157  -26.862 1.00 30.22 ? 364  TRP B CA  1 
ATOM   6481 C  C   . TRP B 2 364 ? 32.945  99.573  -26.444 1.00 29.99 ? 364  TRP B C   1 
ATOM   6482 O  O   . TRP B 2 364 ? 33.899  99.267  -27.184 1.00 31.01 ? 364  TRP B O   1 
ATOM   6483 C  CB  . TRP B 2 364 ? 31.288  97.681  -26.567 1.00 30.24 ? 364  TRP B CB  1 
ATOM   6484 C  CG  . TRP B 2 364 ? 31.531  97.301  -25.143 1.00 29.72 ? 364  TRP B CG  1 
ATOM   6485 C  CD1 . TRP B 2 364 ? 32.459  96.429  -24.661 1.00 29.35 ? 364  TRP B CD1 1 
ATOM   6486 C  CD2 . TRP B 2 364 ? 30.813  97.801  -24.005 1.00 30.30 ? 364  TRP B CD2 1 
ATOM   6487 N  NE1 . TRP B 2 364 ? 32.357  96.340  -23.298 1.00 30.60 ? 364  TRP B NE1 1 
ATOM   6488 C  CE2 . TRP B 2 364 ? 31.349  97.158  -22.868 1.00 31.17 ? 364  TRP B CE2 1 
ATOM   6489 C  CE3 . TRP B 2 364 ? 29.755  98.702  -23.844 1.00 30.73 ? 364  TRP B CE3 1 
ATOM   6490 C  CZ2 . TRP B 2 364 ? 30.871  97.406  -21.583 1.00 30.28 ? 364  TRP B CZ2 1 
ATOM   6491 C  CZ3 . TRP B 2 364 ? 29.280  98.941  -22.575 1.00 31.85 ? 364  TRP B CZ3 1 
ATOM   6492 C  CH2 . TRP B 2 364 ? 29.835  98.299  -21.463 1.00 30.68 ? 364  TRP B CH2 1 
ATOM   6493 N  N   . HIS B 2 365 ? 33.061  100.256 -25.306 1.00 29.36 ? 365  HIS B N   1 
ATOM   6494 C  CA  . HIS B 2 365 ? 34.324  100.425 -24.537 1.00 28.74 ? 365  HIS B CA  1 
ATOM   6495 C  C   . HIS B 2 365 ? 34.016  100.092 -23.079 1.00 28.62 ? 365  HIS B C   1 
ATOM   6496 O  O   . HIS B 2 365 ? 33.035  100.657 -22.543 1.00 27.85 ? 365  HIS B O   1 
ATOM   6497 C  CB  . HIS B 2 365 ? 34.911  101.827 -24.724 1.00 29.66 ? 365  HIS B CB  1 
ATOM   6498 C  CG  . HIS B 2 365 ? 35.261  102.137 -26.143 1.00 31.74 ? 365  HIS B CG  1 
ATOM   6499 N  ND1 . HIS B 2 365 ? 34.345  102.669 -27.026 1.00 32.09 ? 365  HIS B ND1 1 
ATOM   6500 C  CD2 . HIS B 2 365 ? 36.410  101.975 -26.836 1.00 31.92 ? 365  HIS B CD2 1 
ATOM   6501 C  CE1 . HIS B 2 365 ? 34.917  102.831 -28.200 1.00 33.69 ? 365  HIS B CE1 1 
ATOM   6502 N  NE2 . HIS B 2 365 ? 36.185  102.416 -28.108 1.00 31.60 ? 365  HIS B NE2 1 
ATOM   6503 N  N   . GLY B 2 366 ? 34.786  99.170  -22.502 1.00 26.93 ? 366  GLY B N   1 
ATOM   6504 C  CA  . GLY B 2 366 ? 34.575  98.638  -21.146 1.00 27.99 ? 366  GLY B CA  1 
ATOM   6505 C  C   . GLY B 2 366 ? 35.779  98.886  -20.257 1.00 27.91 ? 366  GLY B C   1 
ATOM   6506 O  O   . GLY B 2 366 ? 36.903  99.011  -20.776 1.00 28.90 ? 366  GLY B O   1 
ATOM   6507 N  N   . HIS B 2 367 ? 35.536  98.978  -18.956 1.00 26.72 ? 367  HIS B N   1 
ATOM   6508 C  CA  . HIS B 2 367 ? 36.569  99.136  -17.907 1.00 27.35 ? 367  HIS B CA  1 
ATOM   6509 C  C   . HIS B 2 367 ? 36.127  98.319  -16.697 1.00 28.51 ? 367  HIS B C   1 
ATOM   6510 O  O   . HIS B 2 367 ? 34.933  98.398  -16.329 1.00 26.92 ? 367  HIS B O   1 
ATOM   6511 C  CB  . HIS B 2 367 ? 36.770  100.622 -17.603 1.00 29.55 ? 367  HIS B CB  1 
ATOM   6512 C  CG  . HIS B 2 367 ? 37.767  100.893 -16.532 1.00 31.23 ? 367  HIS B CG  1 
ATOM   6513 N  ND1 . HIS B 2 367 ? 39.118  100.797 -16.755 1.00 34.28 ? 367  HIS B ND1 1 
ATOM   6514 C  CD2 . HIS B 2 367 ? 37.616  101.278 -15.246 1.00 33.29 ? 367  HIS B CD2 1 
ATOM   6515 C  CE1 . HIS B 2 367 ? 39.761  101.096 -15.644 1.00 34.48 ? 367  HIS B CE1 1 
ATOM   6516 N  NE2 . HIS B 2 367 ? 38.863  101.396 -14.706 1.00 32.42 ? 367  HIS B NE2 1 
ATOM   6517 N  N   . GLY B 2 368 ? 37.034  97.520  -16.140 1.00 28.20 ? 368  GLY B N   1 
ATOM   6518 C  CA  . GLY B 2 368 ? 36.740  96.681  -14.962 1.00 28.90 ? 368  GLY B CA  1 
ATOM   6519 C  C   . GLY B 2 368 ? 35.896  95.485  -15.356 1.00 28.49 ? 368  GLY B C   1 
ATOM   6520 O  O   . GLY B 2 368 ? 36.084  94.981  -16.478 1.00 30.24 ? 368  GLY B O   1 
ATOM   6521 N  N   . ALA B 2 369 ? 34.986  95.063  -14.477 1.00 27.45 ? 369  ALA B N   1 
ATOM   6522 C  CA  . ALA B 2 369 ? 34.155  93.846  -14.633 1.00 28.25 ? 369  ALA B CA  1 
ATOM   6523 C  C   . ALA B 2 369 ? 32.844  94.204  -15.352 1.00 28.45 ? 369  ALA B C   1 
ATOM   6524 O  O   . ALA B 2 369 ? 31.957  94.830  -14.734 1.00 28.45 ? 369  ALA B O   1 
ATOM   6525 C  CB  . ALA B 2 369 ? 33.911  93.224  -13.285 1.00 27.58 ? 369  ALA B CB  1 
ATOM   6526 N  N   . THR B 2 370 ? 32.744  93.827  -16.623 1.00 27.72 ? 370  THR B N   1 
ATOM   6527 C  CA  . THR B 2 370 ? 31.583  94.122  -17.513 1.00 29.70 ? 370  THR B CA  1 
ATOM   6528 C  C   . THR B 2 370 ? 31.199  92.842  -18.244 1.00 30.14 ? 370  THR B C   1 
ATOM   6529 O  O   . THR B 2 370 ? 31.995  91.914  -18.326 1.00 31.72 ? 370  THR B O   1 
ATOM   6530 C  CB  . THR B 2 370 ? 31.908  95.231  -18.529 1.00 30.77 ? 370  THR B CB  1 
ATOM   6531 O  OG1 . THR B 2 370 ? 32.898  94.732  -19.430 1.00 31.74 ? 370  THR B OG1 1 
ATOM   6532 C  CG2 . THR B 2 370 ? 32.429  96.508  -17.905 1.00 30.36 ? 370  THR B CG2 1 
ATOM   6533 N  N   . PRO B 2 371 ? 29.982  92.751  -18.821 1.00 30.84 ? 371  PRO B N   1 
ATOM   6534 C  CA  . PRO B 2 371 ? 29.656  91.647  -19.718 1.00 31.92 ? 371  PRO B CA  1 
ATOM   6535 C  C   . PRO B 2 371 ? 30.595  91.651  -20.919 1.00 31.99 ? 371  PRO B C   1 
ATOM   6536 O  O   . PRO B 2 371 ? 31.160  92.688  -21.256 1.00 28.67 ? 371  PRO B O   1 
ATOM   6537 C  CB  . PRO B 2 371 ? 28.215  91.936  -20.152 1.00 30.83 ? 371  PRO B CB  1 
ATOM   6538 C  CG  . PRO B 2 371 ? 27.679  92.836  -19.056 1.00 30.26 ? 371  PRO B CG  1 
ATOM   6539 C  CD  . PRO B 2 371 ? 28.860  93.683  -18.648 1.00 30.10 ? 371  PRO B CD  1 
ATOM   6540 N  N   . PRO B 2 372 ? 30.764  90.504  -21.617 1.00 33.28 ? 372  PRO B N   1 
ATOM   6541 C  CA  . PRO B 2 372 ? 31.526  90.483  -22.860 1.00 34.16 ? 372  PRO B CA  1 
ATOM   6542 C  C   . PRO B 2 372 ? 30.887  91.408  -23.902 1.00 34.63 ? 372  PRO B C   1 
ATOM   6543 O  O   . PRO B 2 372 ? 29.689  91.638  -23.857 1.00 30.73 ? 372  PRO B O   1 
ATOM   6544 C  CB  . PRO B 2 372 ? 31.482  89.016  -23.317 1.00 36.03 ? 372  PRO B CB  1 
ATOM   6545 C  CG  . PRO B 2 372 ? 30.300  88.421  -22.583 1.00 36.57 ? 372  PRO B CG  1 
ATOM   6546 C  CD  . PRO B 2 372 ? 30.209  89.185  -21.280 1.00 35.59 ? 372  PRO B CD  1 
ATOM   6547 N  N   . HIS B 2 373 ? 31.730  91.919  -24.796 1.00 36.12 ? 373  HIS B N   1 
ATOM   6548 C  CA  . HIS B 2 373 ? 31.396  92.826  -25.923 1.00 39.82 ? 373  HIS B CA  1 
ATOM   6549 C  C   . HIS B 2 373 ? 30.141  92.315  -26.657 1.00 37.97 ? 373  HIS B C   1 
ATOM   6550 O  O   . HIS B 2 373 ? 29.250  93.138  -26.930 1.00 36.12 ? 373  HIS B O   1 
ATOM   6551 C  CB  . HIS B 2 373 ? 32.691  92.998  -26.739 1.00 45.01 ? 373  HIS B CB  1 
ATOM   6552 C  CG  . HIS B 2 373 ? 32.534  93.273  -28.190 1.00 47.36 ? 373  HIS B CG  1 
ATOM   6553 N  ND1 . HIS B 2 373 ? 32.072  92.317  -29.074 1.00 50.85 ? 373  HIS B ND1 1 
ATOM   6554 C  CD2 . HIS B 2 373 ? 32.861  94.358  -28.924 1.00 51.76 ? 373  HIS B CD2 1 
ATOM   6555 C  CE1 . HIS B 2 373 ? 32.070  92.821  -30.291 1.00 53.14 ? 373  HIS B CE1 1 
ATOM   6556 N  NE2 . HIS B 2 373 ? 32.554  94.074  -30.226 1.00 53.57 ? 373  HIS B NE2 1 
ATOM   6557 N  N   . ASP B 2 374 ? 30.046  91.001  -26.892 1.00 38.99 ? 374  ASP B N   1 
ATOM   6558 C  CA  . ASP B 2 374 ? 28.943  90.325  -27.635 1.00 40.19 ? 374  ASP B CA  1 
ATOM   6559 C  C   . ASP B 2 374 ? 27.620  90.408  -26.860 1.00 37.49 ? 374  ASP B C   1 
ATOM   6560 O  O   . ASP B 2 374 ? 26.560  90.256  -27.490 1.00 35.58 ? 374  ASP B O   1 
ATOM   6561 C  CB  . ASP B 2 374 ? 29.278  88.853  -27.908 1.00 44.02 ? 374  ASP B CB  1 
ATOM   6562 C  CG  . ASP B 2 374 ? 30.412  88.628  -28.902 1.00 49.19 ? 374  ASP B CG  1 
ATOM   6563 O  OD1 . ASP B 2 374 ? 30.986  89.627  -29.397 1.00 49.17 ? 374  ASP B OD1 1 
ATOM   6564 O  OD2 . ASP B 2 374 ? 30.719  87.448  -29.178 1.00 52.56 ? 374  ASP B OD2 1 
ATOM   6565 N  N   . ALA B 2 375 ? 27.662  90.622  -25.543 1.00 35.50 ? 375  ALA B N   1 
ATOM   6566 C  CA  . ALA B 2 375 ? 26.457  90.609  -24.680 1.00 34.46 ? 375  ALA B CA  1 
ATOM   6567 C  C   . ALA B 2 375 ? 25.767  91.976  -24.692 1.00 32.29 ? 375  ALA B C   1 
ATOM   6568 O  O   . ALA B 2 375 ? 24.582  92.031  -24.311 1.00 34.63 ? 375  ALA B O   1 
ATOM   6569 C  CB  . ALA B 2 375 ? 26.819  90.192  -23.273 1.00 34.47 ? 375  ALA B CB  1 
ATOM   6570 N  N   . ILE B 2 376 ? 26.461  93.035  -25.111 1.00 31.23 ? 376  ILE B N   1 
ATOM   6571 C  CA  . ILE B 2 376 ? 26.012  94.439  -24.854 1.00 32.57 ? 376  ILE B CA  1 
ATOM   6572 C  C   . ILE B 2 376 ? 24.799  94.788  -25.709 1.00 33.60 ? 376  ILE B C   1 
ATOM   6573 O  O   . ILE B 2 376 ? 23.883  95.439  -25.210 1.00 34.98 ? 376  ILE B O   1 
ATOM   6574 C  CB  . ILE B 2 376 ? 27.156  95.456  -25.038 1.00 32.56 ? 376  ILE B CB  1 
ATOM   6575 C  CG1 . ILE B 2 376 ? 28.371  95.105  -24.172 1.00 33.05 ? 376  ILE B CG1 1 
ATOM   6576 C  CG2 . ILE B 2 376 ? 26.660  96.869  -24.761 1.00 32.16 ? 376  ILE B CG2 1 
ATOM   6577 C  CD1 . ILE B 2 376 ? 28.066  95.009  -22.686 1.00 32.77 ? 376  ILE B CD1 1 
ATOM   6578 N  N   . PRO B 2 377 ? 24.762  94.439  -27.018 1.00 34.96 ? 377  PRO B N   1 
ATOM   6579 C  CA  . PRO B 2 377 ? 23.616  94.787  -27.865 1.00 36.45 ? 377  PRO B CA  1 
ATOM   6580 C  C   . PRO B 2 377 ? 22.264  94.347  -27.281 1.00 35.29 ? 377  PRO B C   1 
ATOM   6581 O  O   . PRO B 2 377 ? 21.318  95.104  -27.349 1.00 36.07 ? 377  PRO B O   1 
ATOM   6582 C  CB  . PRO B 2 377 ? 23.911  94.048  -29.182 1.00 36.70 ? 377  PRO B CB  1 
ATOM   6583 C  CG  . PRO B 2 377 ? 25.422  93.971  -29.217 1.00 35.72 ? 377  PRO B CG  1 
ATOM   6584 C  CD  . PRO B 2 377 ? 25.823  93.750  -27.772 1.00 34.93 ? 377  PRO B CD  1 
ATOM   6585 N  N   . ARG B 2 378 ? 22.221  93.152  -26.690 1.00 38.96 ? 378  ARG B N   1 
ATOM   6586 C  CA  . ARG B 2 378 ? 20.996  92.571  -26.069 1.00 39.53 ? 378  ARG B CA  1 
ATOM   6587 C  C   . ARG B 2 378 ? 20.607  93.434  -24.859 1.00 38.19 ? 378  ARG B C   1 
ATOM   6588 O  O   . ARG B 2 378 ? 19.402  93.706  -24.684 1.00 36.19 ? 378  ARG B O   1 
ATOM   6589 C  CB  . ARG B 2 378 ? 21.263  91.109  -25.694 1.00 45.08 ? 378  ARG B CB  1 
ATOM   6590 C  CG  . ARG B 2 378 ? 20.112  90.400  -24.996 1.00 50.41 ? 378  ARG B CG  1 
ATOM   6591 C  CD  . ARG B 2 378 ? 19.056  89.872  -25.949 1.00 55.44 ? 378  ARG B CD  1 
ATOM   6592 N  NE  . ARG B 2 378 ? 18.195  88.917  -25.256 1.00 60.19 ? 378  ARG B NE  1 
ATOM   6593 C  CZ  . ARG B 2 378 ? 17.082  89.221  -24.583 1.00 60.49 ? 378  ARG B CZ  1 
ATOM   6594 N  NH1 . ARG B 2 378 ? 16.645  90.470  -24.522 1.00 59.53 ? 378  ARG B NH1 1 
ATOM   6595 N  NH2 . ARG B 2 378 ? 16.407  88.262  -23.970 1.00 60.25 ? 378  ARG B NH2 1 
ATOM   6596 N  N   . LEU B 2 379 ? 21.594  93.858  -24.062 1.00 34.39 ? 379  LEU B N   1 
ATOM   6597 C  CA  . LEU B 2 379 ? 21.372  94.683  -22.845 1.00 33.07 ? 379  LEU B CA  1 
ATOM   6598 C  C   . LEU B 2 379 ? 20.820  96.054  -23.253 1.00 33.26 ? 379  LEU B C   1 
ATOM   6599 O  O   . LEU B 2 379 ? 19.782  96.461  -22.696 1.00 32.06 ? 379  LEU B O   1 
ATOM   6600 C  CB  . LEU B 2 379 ? 22.686  94.815  -22.064 1.00 34.23 ? 379  LEU B CB  1 
ATOM   6601 C  CG  . LEU B 2 379 ? 23.076  93.609  -21.210 1.00 34.55 ? 379  LEU B CG  1 
ATOM   6602 C  CD1 . LEU B 2 379 ? 24.536  93.686  -20.793 1.00 35.56 ? 379  LEU B CD1 1 
ATOM   6603 C  CD2 . LEU B 2 379 ? 22.189  93.495  -19.982 1.00 36.18 ? 379  LEU B CD2 1 
ATOM   6604 N  N   . ALA B 2 380 ? 21.488  96.742  -24.185 1.00 33.90 ? 380  ALA B N   1 
ATOM   6605 C  CA  . ALA B 2 380 ? 21.074  98.072  -24.701 1.00 34.52 ? 380  ALA B CA  1 
ATOM   6606 C  C   . ALA B 2 380 ? 19.638  98.002  -25.245 1.00 35.76 ? 380  ALA B C   1 
ATOM   6607 O  O   . ALA B 2 380 ? 18.825  98.907  -24.919 1.00 34.84 ? 380  ALA B O   1 
ATOM   6608 C  CB  . ALA B 2 380 ? 22.039  98.535  -25.759 1.00 36.15 ? 380  ALA B CB  1 
ATOM   6609 N  N   . ARG B 2 381 ? 19.340  96.965  -26.038 1.00 36.59 ? 381  ARG B N   1 
ATOM   6610 C  CA  . ARG B 2 381 ? 17.982  96.738  -26.617 1.00 38.90 ? 381  ARG B CA  1 
ATOM   6611 C  C   . ARG B 2 381 ? 16.976  96.621  -25.466 1.00 38.76 ? 381  ARG B C   1 
ATOM   6612 O  O   . ARG B 2 381 ? 15.933  97.284  -25.532 1.00 38.41 ? 381  ARG B O   1 
ATOM   6613 C  CB  . ARG B 2 381 ? 17.939  95.499  -27.517 1.00 39.81 ? 381  ARG B CB  1 
ATOM   6614 N  N   . PHE B 2 382 ? 17.301  95.859  -24.419 1.00 40.04 ? 382  PHE B N   1 
ATOM   6615 C  CA  . PHE B 2 382 ? 16.400  95.674  -23.252 1.00 39.41 ? 382  PHE B CA  1 
ATOM   6616 C  C   . PHE B 2 382 ? 16.128  97.015  -22.561 1.00 40.74 ? 382  PHE B C   1 
ATOM   6617 O  O   . PHE B 2 382 ? 14.953  97.279  -22.234 1.00 40.32 ? 382  PHE B O   1 
ATOM   6618 C  CB  . PHE B 2 382 ? 16.944  94.670  -22.237 1.00 41.82 ? 382  PHE B CB  1 
ATOM   6619 C  CG  . PHE B 2 382 ? 15.924  94.336  -21.178 1.00 42.77 ? 382  PHE B CG  1 
ATOM   6620 C  CD1 . PHE B 2 382 ? 14.983  93.338  -21.392 1.00 43.40 ? 382  PHE B CD1 1 
ATOM   6621 C  CD2 . PHE B 2 382 ? 15.862  95.060  -19.997 1.00 42.83 ? 382  PHE B CD2 1 
ATOM   6622 C  CE1 . PHE B 2 382 ? 14.030  93.044  -20.429 1.00 45.81 ? 382  PHE B CE1 1 
ATOM   6623 C  CE2 . PHE B 2 382 ? 14.904  94.767  -19.037 1.00 44.49 ? 382  PHE B CE2 1 
ATOM   6624 C  CZ  . PHE B 2 382 ? 13.989  93.762  -19.256 1.00 45.25 ? 382  PHE B CZ  1 
ATOM   6625 N  N   . VAL B 2 383 ? 17.164  97.820  -22.300 1.00 40.90 ? 383  VAL B N   1 
ATOM   6626 C  CA  . VAL B 2 383 ? 17.003  99.107  -21.560 1.00 43.13 ? 383  VAL B CA  1 
ATOM   6627 C  C   . VAL B 2 383 ? 16.106  100.023 -22.401 1.00 43.10 ? 383  VAL B C   1 
ATOM   6628 O  O   . VAL B 2 383 ? 15.187  100.620 -21.824 1.00 43.78 ? 383  VAL B O   1 
ATOM   6629 C  CB  . VAL B 2 383 ? 18.343  99.786  -21.207 1.00 42.69 ? 383  VAL B CB  1 
ATOM   6630 C  CG1 . VAL B 2 383 ? 18.136  101.213 -20.713 1.00 42.06 ? 383  VAL B CG1 1 
ATOM   6631 C  CG2 . VAL B 2 383 ? 19.130  98.986  -20.176 1.00 41.71 ? 383  VAL B CG2 1 
ATOM   6632 N  N   . ALA B 2 384 ? 16.375  100.105 -23.706 1.00 45.51 ? 384  ALA B N   1 
ATOM   6633 C  CA  . ALA B 2 384 ? 15.624  100.911 -24.700 1.00 48.11 ? 384  ALA B CA  1 
ATOM   6634 C  C   . ALA B 2 384 ? 14.114  100.673 -24.549 1.00 49.56 ? 384  ALA B C   1 
ATOM   6635 O  O   . ALA B 2 384 ? 13.358  101.660 -24.475 1.00 50.77 ? 384  ALA B O   1 
ATOM   6636 C  CB  . ALA B 2 384 ? 16.101  100.571 -26.091 1.00 48.67 ? 384  ALA B CB  1 
ATOM   6637 N  N   . SER B 2 385 ? 13.700  99.407  -24.470 1.00 52.85 ? 385  SER B N   1 
ATOM   6638 C  CA  . SER B 2 385 ? 12.271  98.985  -24.401 1.00 53.53 ? 385  SER B CA  1 
ATOM   6639 C  C   . SER B 2 385 ? 11.696  99.164  -22.987 1.00 54.89 ? 385  SER B C   1 
ATOM   6640 O  O   . SER B 2 385 ? 10.465  99.257  -22.883 1.00 55.20 ? 385  SER B O   1 
ATOM   6641 C  CB  . SER B 2 385 ? 12.112  97.563  -24.855 1.00 55.12 ? 385  SER B CB  1 
ATOM   6642 O  OG  . SER B 2 385 ? 12.702  96.676  -23.914 1.00 59.80 ? 385  SER B OG  1 
ATOM   6643 N  N   . ALA B 2 386 ? 12.541  99.189  -21.947 1.00 55.45 ? 386  ALA B N   1 
ATOM   6644 C  CA  . ALA B 2 386 ? 12.138  99.165  -20.515 1.00 54.94 ? 386  ALA B CA  1 
ATOM   6645 C  C   . ALA B 2 386 ? 12.245  100.551 -19.864 1.00 55.62 ? 386  ALA B C   1 
ATOM   6646 O  O   . ALA B 2 386 ? 11.617  100.748 -18.800 1.00 55.28 ? 386  ALA B O   1 
ATOM   6647 C  CB  . ALA B 2 386 ? 12.981  98.161  -19.768 1.00 54.57 ? 386  ALA B CB  1 
ATOM   6648 N  N   . SER B 2 387 ? 13.023  101.462 -20.453 1.00 57.00 ? 387  SER B N   1 
ATOM   6649 C  CA  . SER B 2 387 ? 13.290  102.821 -19.907 1.00 61.96 ? 387  SER B CA  1 
ATOM   6650 C  C   . SER B 2 387 ? 12.372  103.845 -20.584 1.00 65.64 ? 387  SER B C   1 
ATOM   6651 O  O   . SER B 2 387 ? 12.087  103.689 -21.789 1.00 63.28 ? 387  SER B O   1 
ATOM   6652 C  CB  . SER B 2 387 ? 14.736  103.206 -20.075 1.00 61.62 ? 387  SER B CB  1 
ATOM   6653 O  OG  . SER B 2 387 ? 14.936  104.573 -19.746 1.00 64.40 ? 387  SER B OG  1 
ATOM   6654 N  N   . GLU B 2 388 ? 11.944  104.862 -19.829 1.00 69.40 ? 388  GLU B N   1 
ATOM   6655 C  CA  . GLU B 2 388 ? 11.190  106.037 -20.343 1.00 66.28 ? 388  GLU B CA  1 
ATOM   6656 C  C   . GLU B 2 388 ? 12.166  107.207 -20.502 1.00 64.70 ? 388  GLU B C   1 
ATOM   6657 O  O   . GLU B 2 388 ? 11.805  108.335 -20.121 1.00 71.66 ? 388  GLU B O   1 
ATOM   6658 C  CB  . GLU B 2 388 ? 10.037  106.384 -19.396 1.00 66.78 ? 388  GLU B CB  1 
ATOM   6659 N  N   . GLY B 2 389 ? 13.362  106.935 -21.034 1.00 60.38 ? 389  GLY B N   1 
ATOM   6660 C  CA  . GLY B 2 389 ? 14.431  107.934 -21.226 1.00 55.46 ? 389  GLY B CA  1 
ATOM   6661 C  C   . GLY B 2 389 ? 14.970  108.460 -19.909 1.00 50.65 ? 389  GLY B C   1 
ATOM   6662 O  O   . GLY B 2 389 ? 15.541  109.561 -19.912 1.00 50.16 ? 389  GLY B O   1 
ATOM   6663 N  N   . ARG B 2 390 ? 14.798  107.716 -18.812 1.00 48.56 ? 390  ARG B N   1 
ATOM   6664 C  CA  . ARG B 2 390 ? 15.427  108.056 -17.506 1.00 47.68 ? 390  ARG B CA  1 
ATOM   6665 C  C   . ARG B 2 390 ? 16.391  106.925 -17.127 1.00 39.92 ? 390  ARG B C   1 
ATOM   6666 O  O   . ARG B 2 390 ? 16.525  105.964 -17.904 1.00 34.13 ? 390  ARG B O   1 
ATOM   6667 C  CB  . ARG B 2 390 ? 14.360  108.283 -16.427 1.00 54.73 ? 390  ARG B CB  1 
ATOM   6668 C  CG  . ARG B 2 390 ? 14.501  109.594 -15.662 1.00 57.91 ? 390  ARG B CG  1 
ATOM   6669 C  CD  . ARG B 2 390 ? 13.669  110.714 -16.270 1.00 60.01 ? 390  ARG B CD  1 
ATOM   6670 N  NE  . ARG B 2 390 ? 13.616  111.920 -15.449 1.00 63.19 ? 390  ARG B NE  1 
ATOM   6671 C  CZ  . ARG B 2 390 ? 12.922  113.021 -15.748 1.00 63.79 ? 390  ARG B CZ  1 
ATOM   6672 N  NH1 . ARG B 2 390 ? 12.211  113.087 -16.862 1.00 65.64 ? 390  ARG B NH1 1 
ATOM   6673 N  NH2 . ARG B 2 390 ? 12.944  114.058 -14.929 1.00 64.72 ? 390  ARG B NH2 1 
ATOM   6674 N  N   . VAL B 2 391 ? 17.025  107.039 -15.963 1.00 35.69 ? 391  VAL B N   1 
ATOM   6675 C  CA  . VAL B 2 391 ? 17.950  106.002 -15.431 1.00 33.68 ? 391  VAL B CA  1 
ATOM   6676 C  C   . VAL B 2 391 ? 17.156  104.709 -15.241 1.00 33.19 ? 391  VAL B C   1 
ATOM   6677 O  O   . VAL B 2 391 ? 16.039  104.767 -14.728 1.00 31.15 ? 391  VAL B O   1 
ATOM   6678 C  CB  . VAL B 2 391 ? 18.622  106.452 -14.124 1.00 32.69 ? 391  VAL B CB  1 
ATOM   6679 C  CG1 . VAL B 2 391 ? 19.422  105.324 -13.490 1.00 31.77 ? 391  VAL B CG1 1 
ATOM   6680 C  CG2 . VAL B 2 391 ? 19.493  107.679 -14.347 1.00 31.62 ? 391  VAL B CG2 1 
ATOM   6681 N  N   . TRP B 2 392 ? 17.721  103.590 -15.684 1.00 33.27 ? 392  TRP B N   1 
ATOM   6682 C  CA  . TRP B 2 392 ? 17.181  102.231 -15.438 1.00 32.96 ? 392  TRP B CA  1 
ATOM   6683 C  C   . TRP B 2 392 ? 18.277  101.415 -14.750 1.00 32.41 ? 392  TRP B C   1 
ATOM   6684 O  O   . TRP B 2 392 ? 19.444  101.494 -15.183 1.00 29.25 ? 392  TRP B O   1 
ATOM   6685 C  CB  . TRP B 2 392 ? 16.704  101.595 -16.744 1.00 33.43 ? 392  TRP B CB  1 
ATOM   6686 C  CG  . TRP B 2 392 ? 15.972  100.305 -16.552 1.00 35.13 ? 392  TRP B CG  1 
ATOM   6687 C  CD1 . TRP B 2 392 ? 14.623  100.131 -16.443 1.00 36.15 ? 392  TRP B CD1 1 
ATOM   6688 C  CD2 . TRP B 2 392 ? 16.557  98.997  -16.438 1.00 36.01 ? 392  TRP B CD2 1 
ATOM   6689 N  NE1 . TRP B 2 392 ? 14.330  98.807  -16.268 1.00 37.28 ? 392  TRP B NE1 1 
ATOM   6690 C  CE2 . TRP B 2 392 ? 15.494  98.087  -16.257 1.00 36.69 ? 392  TRP B CE2 1 
ATOM   6691 C  CE3 . TRP B 2 392 ? 17.868  98.512  -16.459 1.00 34.68 ? 392  TRP B CE3 1 
ATOM   6692 C  CZ2 . TRP B 2 392 ? 15.706  96.718  -16.107 1.00 37.64 ? 392  TRP B CZ2 1 
ATOM   6693 C  CZ3 . TRP B 2 392 ? 18.074  97.160  -16.309 1.00 36.94 ? 392  TRP B CZ3 1 
ATOM   6694 C  CH2 . TRP B 2 392 ? 17.008  96.275  -16.146 1.00 36.33 ? 392  TRP B CH2 1 
ATOM   6695 N  N   . ALA B 2 393 ? 17.922  100.691 -13.694 1.00 31.05 ? 393  ALA B N   1 
ATOM   6696 C  CA  . ALA B 2 393 ? 18.886  99.920  -12.880 1.00 30.81 ? 393  ALA B CA  1 
ATOM   6697 C  C   . ALA B 2 393 ? 18.220  98.645  -12.370 1.00 30.60 ? 393  ALA B C   1 
ATOM   6698 O  O   . ALA B 2 393 ? 17.024  98.689  -12.044 1.00 31.89 ? 393  ALA B O   1 
ATOM   6699 C  CB  . ALA B 2 393 ? 19.395  100.780 -11.751 1.00 30.95 ? 393  ALA B CB  1 
ATOM   6700 N  N   . THR B 2 394 ? 18.980  97.555  -12.321 1.00 30.01 ? 394  THR B N   1 
ATOM   6701 C  CA  . THR B 2 394 ? 18.570  96.281  -11.689 1.00 30.73 ? 394  THR B CA  1 
ATOM   6702 C  C   . THR B 2 394 ? 19.773  95.660  -10.987 1.00 30.14 ? 394  THR B C   1 
ATOM   6703 O  O   . THR B 2 394 ? 20.895  95.857  -11.460 1.00 29.70 ? 394  THR B O   1 
ATOM   6704 C  CB  . THR B 2 394 ? 17.997  95.292  -12.706 1.00 31.68 ? 394  THR B CB  1 
ATOM   6705 O  OG1 . THR B 2 394 ? 17.601  94.154  -11.943 1.00 33.51 ? 394  THR B OG1 1 
ATOM   6706 C  CG2 . THR B 2 394 ? 18.983  94.887  -13.780 1.00 33.25 ? 394  THR B CG2 1 
ATOM   6707 N  N   . HIS B 2 395 ? 19.523  94.900  -9.925  1.00 29.80 ? 395  HIS B N   1 
ATOM   6708 C  CA  . HIS B 2 395 ? 20.551  94.085  -9.227  1.00 30.53 ? 395  HIS B CA  1 
ATOM   6709 C  C   . HIS B 2 395 ? 20.359  92.606  -9.575  1.00 29.39 ? 395  HIS B C   1 
ATOM   6710 O  O   . HIS B 2 395 ? 21.047  91.774  -8.961  1.00 30.03 ? 395  HIS B O   1 
ATOM   6711 C  CB  . HIS B 2 395 ? 20.516  94.363  -7.723  1.00 30.80 ? 395  HIS B CB  1 
ATOM   6712 C  CG  . HIS B 2 395 ? 19.219  94.021  -7.076  1.00 33.09 ? 395  HIS B CG  1 
ATOM   6713 N  ND1 . HIS B 2 395 ? 18.268  94.976  -6.797  1.00 32.82 ? 395  HIS B ND1 1 
ATOM   6714 C  CD2 . HIS B 2 395 ? 18.724  92.842  -6.631  1.00 34.95 ? 395  HIS B CD2 1 
ATOM   6715 C  CE1 . HIS B 2 395 ? 17.238  94.402  -6.203  1.00 34.98 ? 395  HIS B CE1 1 
ATOM   6716 N  NE2 . HIS B 2 395 ? 17.493  93.095  -6.091  1.00 34.69 ? 395  HIS B NE2 1 
ATOM   6717 N  N   . ALA B 2 396 ? 19.493  92.303  -10.546 1.00 30.43 ? 396  ALA B N   1 
ATOM   6718 C  CA  . ALA B 2 396 ? 19.099  90.924  -10.926 1.00 32.03 ? 396  ALA B CA  1 
ATOM   6719 C  C   . ALA B 2 396 ? 18.942  90.813  -12.449 1.00 31.43 ? 396  ALA B C   1 
ATOM   6720 O  O   . ALA B 2 396 ? 17.816  90.572  -12.918 1.00 31.64 ? 396  ALA B O   1 
ATOM   6721 C  CB  . ALA B 2 396 ? 17.828  90.549  -10.198 1.00 32.55 ? 396  ALA B CB  1 
ATOM   6722 N  N   . LEU B 2 397 ? 20.045  90.964  -13.188 1.00 32.26 ? 397  LEU B N   1 
ATOM   6723 C  CA  . LEU B 2 397 ? 20.050  91.028  -14.674 1.00 33.51 ? 397  LEU B CA  1 
ATOM   6724 C  C   . LEU B 2 397 ? 19.352  89.800  -15.263 1.00 35.56 ? 397  LEU B C   1 
ATOM   6725 O  O   . LEU B 2 397 ? 18.524  89.992  -16.169 1.00 34.25 ? 397  LEU B O   1 
ATOM   6726 C  CB  . LEU B 2 397 ? 21.487  91.116  -15.194 1.00 35.57 ? 397  LEU B CB  1 
ATOM   6727 C  CG  . LEU B 2 397 ? 22.012  92.522  -15.477 1.00 36.56 ? 397  LEU B CG  1 
ATOM   6728 C  CD1 . LEU B 2 397 ? 23.452  92.462  -15.967 1.00 36.56 ? 397  LEU B CD1 1 
ATOM   6729 C  CD2 . LEU B 2 397 ? 21.139  93.244  -16.492 1.00 37.10 ? 397  LEU B CD2 1 
ATOM   6730 N  N   . SER B 2 398 ? 19.678  88.596  -14.776 1.00 35.68 ? 398  SER B N   1 
ATOM   6731 C  CA  . SER B 2 398 ? 19.179  87.317  -15.346 1.00 38.69 ? 398  SER B CA  1 
ATOM   6732 C  C   . SER B 2 398 ? 17.655  87.221  -15.163 1.00 42.01 ? 398  SER B C   1 
ATOM   6733 O  O   . SER B 2 398 ? 17.023  86.518  -15.971 1.00 43.63 ? 398  SER B O   1 
ATOM   6734 C  CB  . SER B 2 398 ? 19.915  86.112  -14.792 1.00 38.31 ? 398  SER B CB  1 
ATOM   6735 O  OG  . SER B 2 398 ? 19.451  85.762  -13.500 1.00 38.82 ? 398  SER B OG  1 
ATOM   6736 N  N   . GLN B 2 399 ? 17.083  87.940  -14.188 1.00 43.58 ? 399  GLN B N   1 
ATOM   6737 C  CA  . GLN B 2 399 ? 15.607  88.017  -13.969 1.00 45.25 ? 399  GLN B CA  1 
ATOM   6738 C  C   . GLN B 2 399 ? 14.936  88.824  -15.086 1.00 47.72 ? 399  GLN B C   1 
ATOM   6739 O  O   . GLN B 2 399 ? 13.728  88.612  -15.317 1.00 52.05 ? 399  GLN B O   1 
ATOM   6740 C  CB  . GLN B 2 399 ? 15.257  88.659  -12.627 1.00 43.80 ? 399  GLN B CB  1 
ATOM   6741 C  CG  . GLN B 2 399 ? 15.237  87.674  -11.473 1.00 45.09 ? 399  GLN B CG  1 
ATOM   6742 C  CD  . GLN B 2 399 ? 14.802  88.330  -10.186 1.00 46.94 ? 399  GLN B CD  1 
ATOM   6743 O  OE1 . GLN B 2 399 ? 13.919  89.185  -10.175 1.00 51.02 ? 399  GLN B OE1 1 
ATOM   6744 N  NE2 . GLN B 2 399 ? 15.433  87.949  -9.086  1.00 46.10 ? 399  GLN B NE2 1 
ATOM   6745 N  N   . ALA B 2 400 ? 15.674  89.739  -15.721 1.00 47.35 ? 400  ALA B N   1 
ATOM   6746 C  CA  . ALA B 2 400 ? 15.204  90.568  -16.855 1.00 45.64 ? 400  ALA B CA  1 
ATOM   6747 C  C   . ALA B 2 400 ? 15.623  89.920  -18.179 1.00 46.31 ? 400  ALA B C   1 
ATOM   6748 O  O   . ALA B 2 400 ? 14.842  89.990  -19.147 1.00 47.09 ? 400  ALA B O   1 
ATOM   6749 C  CB  . ALA B 2 400 ? 15.754  91.966  -16.726 1.00 46.30 ? 400  ALA B CB  1 
ATOM   6750 N  N   . ILE B 2 401 ? 16.811  89.312  -18.215 1.00 46.34 ? 401  ILE B N   1 
ATOM   6751 C  CA  . ILE B 2 401 ? 17.425  88.718  -19.441 1.00 47.18 ? 401  ILE B CA  1 
ATOM   6752 C  C   . ILE B 2 401 ? 18.027  87.365  -19.079 1.00 45.17 ? 401  ILE B C   1 
ATOM   6753 O  O   . ILE B 2 401 ? 19.163  87.314  -18.623 1.00 44.13 ? 401  ILE B O   1 
ATOM   6754 C  CB  . ILE B 2 401 ? 18.491  89.668  -20.024 1.00 48.92 ? 401  ILE B CB  1 
ATOM   6755 C  CG1 . ILE B 2 401 ? 17.913  91.051  -20.331 1.00 51.32 ? 401  ILE B CG1 1 
ATOM   6756 C  CG2 . ILE B 2 401 ? 19.163  89.052  -21.246 1.00 48.96 ? 401  ILE B CG2 1 
ATOM   6757 C  CD1 . ILE B 2 401 ? 18.953  92.074  -20.712 1.00 53.19 ? 401  ILE B CD1 1 
ATOM   6758 N  N   . PRO B 2 402 ? 17.310  86.234  -19.290 1.00 45.99 ? 402  PRO B N   1 
ATOM   6759 C  CA  . PRO B 2 402 ? 17.820  84.912  -18.915 1.00 44.74 ? 402  PRO B CA  1 
ATOM   6760 C  C   . PRO B 2 402 ? 19.270  84.653  -19.355 1.00 44.47 ? 402  PRO B C   1 
ATOM   6761 O  O   . PRO B 2 402 ? 20.002  84.038  -18.601 1.00 44.60 ? 402  PRO B O   1 
ATOM   6762 C  CB  . PRO B 2 402 ? 16.862  83.953  -19.637 1.00 44.57 ? 402  PRO B CB  1 
ATOM   6763 C  CG  . PRO B 2 402 ? 15.559  84.719  -19.677 1.00 44.69 ? 402  PRO B CG  1 
ATOM   6764 C  CD  . PRO B 2 402 ? 15.971  86.162  -19.902 1.00 45.59 ? 402  PRO B CD  1 
ATOM   6765 N  N   . GLU B 2 403 ? 19.647  85.164  -20.530 1.00 43.30 ? 403  GLU B N   1 
ATOM   6766 C  CA  . GLU B 2 403 ? 20.991  84.989  -21.150 1.00 45.72 ? 403  GLU B CA  1 
ATOM   6767 C  C   . GLU B 2 403 ? 22.084  85.499  -20.199 1.00 41.66 ? 403  GLU B C   1 
ATOM   6768 O  O   . GLU B 2 403 ? 23.170  84.917  -20.191 1.00 40.14 ? 403  GLU B O   1 
ATOM   6769 C  CB  . GLU B 2 403 ? 21.078  85.741  -22.482 1.00 50.14 ? 403  GLU B CB  1 
ATOM   6770 C  CG  . GLU B 2 403 ? 20.171  85.186  -23.566 1.00 53.94 ? 403  GLU B CG  1 
ATOM   6771 C  CD  . GLU B 2 403 ? 18.676  85.335  -23.327 1.00 57.30 ? 403  GLU B CD  1 
ATOM   6772 O  OE1 . GLU B 2 403 ? 18.258  86.390  -22.800 1.00 57.92 ? 403  GLU B OE1 1 
ATOM   6773 O  OE2 . GLU B 2 403 ? 17.929  84.389  -23.662 1.00 63.62 ? 403  GLU B OE2 1 
ATOM   6774 N  N   . ALA B 2 404 ? 21.796  86.544  -19.420 1.00 39.35 ? 404  ALA B N   1 
ATOM   6775 C  CA  . ALA B 2 404 ? 22.778  87.252  -18.564 1.00 39.75 ? 404  ALA B CA  1 
ATOM   6776 C  C   . ALA B 2 404 ? 23.321  86.328  -17.466 1.00 37.62 ? 404  ALA B C   1 
ATOM   6777 O  O   . ALA B 2 404 ? 24.379  86.666  -16.902 1.00 35.20 ? 404  ALA B O   1 
ATOM   6778 C  CB  . ALA B 2 404 ? 22.161  88.503  -17.979 1.00 40.87 ? 404  ALA B CB  1 
ATOM   6779 N  N   . GLU B 2 405 ? 22.644  85.213  -17.167 1.00 37.58 ? 405  GLU B N   1 
ATOM   6780 C  CA  . GLU B 2 405 ? 23.097  84.250  -16.122 1.00 39.00 ? 405  GLU B CA  1 
ATOM   6781 C  C   . GLU B 2 405 ? 24.518  83.763  -16.444 1.00 39.20 ? 405  GLU B C   1 
ATOM   6782 O  O   . GLU B 2 405 ? 25.300  83.538  -15.502 1.00 41.24 ? 405  GLU B O   1 
ATOM   6783 C  CB  . GLU B 2 405 ? 22.121  83.079  -15.990 1.00 38.99 ? 405  GLU B CB  1 
ATOM   6784 C  CG  . GLU B 2 405 ? 22.660  81.947  -15.128 1.00 40.52 ? 405  GLU B CG  1 
ATOM   6785 C  CD  . GLU B 2 405 ? 21.626  80.926  -14.687 1.00 43.19 ? 405  GLU B CD  1 
ATOM   6786 O  OE1 . GLU B 2 405 ? 20.439  81.113  -15.027 1.00 44.72 ? 405  GLU B OE1 1 
ATOM   6787 O  OE2 . GLU B 2 405 ? 22.011  79.951  -13.997 1.00 43.39 ? 405  GLU B OE2 1 
ATOM   6788 N  N   . ILE B 2 406 ? 24.836  83.606  -17.729 1.00 40.13 ? 406  ILE B N   1 
ATOM   6789 C  CA  . ILE B 2 406 ? 26.164  83.127  -18.223 1.00 42.54 ? 406  ILE B CA  1 
ATOM   6790 C  C   . ILE B 2 406 ? 27.296  83.975  -17.617 1.00 41.14 ? 406  ILE B C   1 
ATOM   6791 O  O   . ILE B 2 406 ? 28.315  83.375  -17.230 1.00 43.43 ? 406  ILE B O   1 
ATOM   6792 C  CB  . ILE B 2 406 ? 26.188  83.110  -19.767 1.00 45.85 ? 406  ILE B CB  1 
ATOM   6793 C  CG1 . ILE B 2 406 ? 25.311  81.980  -20.318 1.00 49.16 ? 406  ILE B CG1 1 
ATOM   6794 C  CG2 . ILE B 2 406 ? 27.610  83.019  -20.299 1.00 46.71 ? 406  ILE B CG2 1 
ATOM   6795 C  CD1 . ILE B 2 406 ? 24.896  82.157  -21.768 1.00 51.20 ? 406  ILE B CD1 1 
ATOM   6796 N  N   . TYR B 2 407 ? 27.131  85.301  -17.507 1.00 36.76 ? 407  TYR B N   1 
ATOM   6797 C  CA  . TYR B 2 407 ? 28.204  86.236  -17.058 1.00 34.79 ? 407  TYR B CA  1 
ATOM   6798 C  C   . TYR B 2 407 ? 27.897  86.847  -15.677 1.00 33.98 ? 407  TYR B C   1 
ATOM   6799 O  O   . TYR B 2 407 ? 28.557  87.834  -15.314 1.00 34.16 ? 407  TYR B O   1 
ATOM   6800 C  CB  . TYR B 2 407 ? 28.467  87.317  -18.117 1.00 32.33 ? 407  TYR B CB  1 
ATOM   6801 C  CG  . TYR B 2 407 ? 27.275  88.090  -18.629 1.00 31.31 ? 407  TYR B CG  1 
ATOM   6802 C  CD1 . TYR B 2 407 ? 26.655  89.064  -17.860 1.00 30.57 ? 407  TYR B CD1 1 
ATOM   6803 C  CD2 . TYR B 2 407 ? 26.800  87.890  -19.919 1.00 31.36 ? 407  TYR B CD2 1 
ATOM   6804 C  CE1 . TYR B 2 407 ? 25.573  89.787  -18.340 1.00 29.81 ? 407  TYR B CE1 1 
ATOM   6805 C  CE2 . TYR B 2 407 ? 25.727  88.611  -20.417 1.00 31.16 ? 407  TYR B CE2 1 
ATOM   6806 C  CZ  . TYR B 2 407 ? 25.112  89.568  -19.626 1.00 31.14 ? 407  TYR B CZ  1 
ATOM   6807 O  OH  . TYR B 2 407 ? 24.051  90.278  -20.111 1.00 30.16 ? 407  TYR B OH  1 
ATOM   6808 N  N   . ALA B 2 408 ? 26.955  86.281  -14.921 1.00 33.95 ? 408  ALA B N   1 
ATOM   6809 C  CA  . ALA B 2 408 ? 26.494  86.822  -13.616 1.00 34.03 ? 408  ALA B CA  1 
ATOM   6810 C  C   . ALA B 2 408 ? 27.670  86.984  -12.642 1.00 34.78 ? 408  ALA B C   1 
ATOM   6811 O  O   . ALA B 2 408 ? 27.650  87.949  -11.862 1.00 35.70 ? 408  ALA B O   1 
ATOM   6812 C  CB  . ALA B 2 408 ? 25.416  85.945  -13.028 1.00 33.62 ? 408  ALA B CB  1 
ATOM   6813 N  N   . GLY B 2 409 ? 28.645  86.072  -12.669 1.00 35.34 ? 409  GLY B N   1 
ATOM   6814 C  CA  . GLY B 2 409 ? 29.872  86.168  -11.854 1.00 37.45 ? 409  GLY B CA  1 
ATOM   6815 C  C   . GLY B 2 409 ? 30.561  87.512  -12.043 1.00 39.38 ? 409  GLY B C   1 
ATOM   6816 O  O   . GLY B 2 409 ? 30.926  88.146  -11.026 1.00 40.93 ? 409  GLY B O   1 
ATOM   6817 N  N   . THR B 2 410 ? 30.706  87.944  -13.302 1.00 37.81 ? 410  THR B N   1 
ATOM   6818 C  CA  . THR B 2 410 ? 31.357  89.227  -13.699 1.00 34.59 ? 410  THR B CA  1 
ATOM   6819 C  C   . THR B 2 410 ? 30.393  90.407  -13.499 1.00 31.39 ? 410  THR B C   1 
ATOM   6820 O  O   . THR B 2 410 ? 30.840  91.447  -12.983 1.00 30.32 ? 410  THR B O   1 
ATOM   6821 C  CB  . THR B 2 410 ? 31.881  89.142  -15.139 1.00 36.61 ? 410  THR B CB  1 
ATOM   6822 O  OG1 . THR B 2 410 ? 32.820  88.071  -15.162 1.00 37.28 ? 410  THR B OG1 1 
ATOM   6823 C  CG2 . THR B 2 410 ? 32.552  90.406  -15.635 1.00 37.19 ? 410  THR B CG2 1 
ATOM   6824 N  N   . ALA B 2 411 ? 29.127  90.270  -13.898 1.00 30.61 ? 411  ALA B N   1 
ATOM   6825 C  CA  . ALA B 2 411 ? 28.143  91.378  -13.884 1.00 30.33 ? 411  ALA B CA  1 
ATOM   6826 C  C   . ALA B 2 411 ? 26.725  90.840  -13.685 1.00 30.03 ? 411  ALA B C   1 
ATOM   6827 O  O   . ALA B 2 411 ? 26.165  90.286  -14.640 1.00 31.28 ? 411  ALA B O   1 
ATOM   6828 C  CB  . ALA B 2 411 ? 28.257  92.187  -15.153 1.00 31.04 ? 411  ALA B CB  1 
ATOM   6829 N  N   . ALA B 2 412 ? 26.178  91.015  -12.477 1.00 28.60 ? 412  ALA B N   1 
ATOM   6830 C  CA  . ALA B 2 412 ? 24.825  90.560  -12.076 1.00 28.41 ? 412  ALA B CA  1 
ATOM   6831 C  C   . ALA B 2 412 ? 23.872  91.753  -11.993 1.00 27.77 ? 412  ALA B C   1 
ATOM   6832 O  O   . ALA B 2 412 ? 22.648  91.551  -12.014 1.00 30.69 ? 412  ALA B O   1 
ATOM   6833 C  CB  . ALA B 2 412 ? 24.916  89.852  -10.754 1.00 29.12 ? 412  ALA B CB  1 
ATOM   6834 N  N   . GLY B 2 413 ? 24.432  92.949  -11.844 1.00 27.57 ? 413  GLY B N   1 
ATOM   6835 C  CA  . GLY B 2 413 ? 23.687  94.209  -11.696 1.00 27.85 ? 413  GLY B CA  1 
ATOM   6836 C  C   . GLY B 2 413 ? 24.137  95.219  -12.727 1.00 26.65 ? 413  GLY B C   1 
ATOM   6837 O  O   . GLY B 2 413 ? 25.325  95.216  -13.086 1.00 26.49 ? 413  GLY B O   1 
ATOM   6838 N  N   . MET B 2 414 ? 23.207  96.041  -13.202 1.00 26.93 ? 414  MET B N   1 
ATOM   6839 C  CA  . MET B 2 414 ? 23.480  97.086  -14.214 1.00 26.97 ? 414  MET B CA  1 
ATOM   6840 C  C   . MET B 2 414 ? 22.633  98.320  -13.904 1.00 27.04 ? 414  MET B C   1 
ATOM   6841 O  O   . MET B 2 414 ? 21.421  98.142  -13.632 1.00 28.03 ? 414  MET B O   1 
ATOM   6842 C  CB  . MET B 2 414 ? 23.157  96.586  -15.625 1.00 27.76 ? 414  MET B CB  1 
ATOM   6843 C  CG  . MET B 2 414 ? 23.529  97.584  -16.702 1.00 29.61 ? 414  MET B CG  1 
ATOM   6844 S  SD  . MET B 2 414 ? 23.159  96.953  -18.355 1.00 32.00 ? 414  MET B SD  1 
ATOM   6845 C  CE  . MET B 2 414 ? 21.369  97.032  -18.314 1.00 33.21 ? 414  MET B CE  1 
ATOM   6846 N  N   . LEU B 2 415 ? 23.265  99.500  -13.925 1.00 25.82 ? 415  LEU B N   1 
ATOM   6847 C  CA  . LEU B 2 415 ? 22.603  100.831 -13.929 1.00 24.95 ? 415  LEU B CA  1 
ATOM   6848 C  C   . LEU B 2 415 ? 22.926  101.502 -15.269 1.00 25.85 ? 415  LEU B C   1 
ATOM   6849 O  O   . LEU B 2 415 ? 24.127  101.700 -15.570 1.00 25.06 ? 415  LEU B O   1 
ATOM   6850 C  CB  . LEU B 2 415 ? 23.080  101.652 -12.728 1.00 25.01 ? 415  LEU B CB  1 
ATOM   6851 C  CG  . LEU B 2 415 ? 22.459  103.046 -12.583 1.00 25.75 ? 415  LEU B CG  1 
ATOM   6852 C  CD1 . LEU B 2 415 ? 22.398  103.470 -11.124 1.00 26.11 ? 415  LEU B CD1 1 
ATOM   6853 C  CD2 . LEU B 2 415 ? 23.219  104.079 -13.404 1.00 25.23 ? 415  LEU B CD2 1 
ATOM   6854 N  N   . ALA B 2 416 ? 21.895  101.785 -16.065 1.00 24.75 ? 416  ALA B N   1 
ATOM   6855 C  CA  . ALA B 2 416 ? 22.013  102.354 -17.425 1.00 26.07 ? 416  ALA B CA  1 
ATOM   6856 C  C   . ALA B 2 416 ? 21.634  103.836 -17.386 1.00 27.32 ? 416  ALA B C   1 
ATOM   6857 O  O   . ALA B 2 416 ? 20.534  104.142 -16.890 1.00 29.15 ? 416  ALA B O   1 
ATOM   6858 C  CB  . ALA B 2 416 ? 21.143  101.587 -18.383 1.00 27.28 ? 416  ALA B CB  1 
ATOM   6859 N  N   . ILE B 2 417 ? 22.528  104.711 -17.855 1.00 25.89 ? 417  ILE B N   1 
ATOM   6860 C  CA  . ILE B 2 417 ? 22.252  106.164 -18.037 1.00 27.31 ? 417  ILE B CA  1 
ATOM   6861 C  C   . ILE B 2 417 ? 22.110  106.433 -19.530 1.00 28.92 ? 417  ILE B C   1 
ATOM   6862 O  O   . ILE B 2 417 ? 23.087  106.331 -20.275 1.00 28.24 ? 417  ILE B O   1 
ATOM   6863 C  CB  . ILE B 2 417 ? 23.332  107.054 -17.396 1.00 27.29 ? 417  ILE B CB  1 
ATOM   6864 C  CG1 . ILE B 2 417 ? 23.585  106.672 -15.930 1.00 26.30 ? 417  ILE B CG1 1 
ATOM   6865 C  CG2 . ILE B 2 417 ? 22.943  108.521 -17.556 1.00 27.23 ? 417  ILE B CG2 1 
ATOM   6866 C  CD1 . ILE B 2 417 ? 24.603  107.534 -15.230 1.00 26.67 ? 417  ILE B CD1 1 
ATOM   6867 N  N   . PRO B 2 418 ? 20.898  106.792 -20.011 1.00 30.08 ? 418  PRO B N   1 
ATOM   6868 C  CA  . PRO B 2 418 ? 20.710  107.110 -21.425 1.00 32.11 ? 418  PRO B CA  1 
ATOM   6869 C  C   . PRO B 2 418 ? 21.452  108.401 -21.797 1.00 31.20 ? 418  PRO B C   1 
ATOM   6870 O  O   . PRO B 2 418 ? 21.430  109.344 -21.024 1.00 31.38 ? 418  PRO B O   1 
ATOM   6871 C  CB  . PRO B 2 418 ? 19.187  107.240 -21.575 1.00 32.72 ? 418  PRO B CB  1 
ATOM   6872 C  CG  . PRO B 2 418 ? 18.720  107.637 -20.195 1.00 33.40 ? 418  PRO B CG  1 
ATOM   6873 C  CD  . PRO B 2 418 ? 19.658  106.929 -19.233 1.00 31.66 ? 418  PRO B CD  1 
ATOM   6874 N  N   . LEU B 2 419 ? 22.106  108.389 -22.962 1.00 31.46 ? 419  LEU B N   1 
ATOM   6875 C  CA  . LEU B 2 419 ? 22.891  109.527 -23.507 1.00 31.92 ? 419  LEU B CA  1 
ATOM   6876 C  C   . LEU B 2 419 ? 22.101  110.248 -24.609 1.00 35.66 ? 419  LEU B C   1 
ATOM   6877 O  O   . LEU B 2 419 ? 22.590  111.296 -25.092 1.00 35.77 ? 419  LEU B O   1 
ATOM   6878 C  CB  . LEU B 2 419 ? 24.216  108.986 -24.043 1.00 31.53 ? 419  LEU B CB  1 
ATOM   6879 C  CG  . LEU B 2 419 ? 25.079  108.243 -23.024 1.00 31.61 ? 419  LEU B CG  1 
ATOM   6880 C  CD1 . LEU B 2 419 ? 26.368  107.763 -23.657 1.00 30.98 ? 419  LEU B CD1 1 
ATOM   6881 C  CD2 . LEU B 2 419 ? 25.380  109.119 -21.821 1.00 32.67 ? 419  LEU B CD2 1 
ATOM   6882 N  N   . SER B 2 420 ? 20.920  109.737 -24.968 1.00 36.87 ? 420  SER B N   1 
ATOM   6883 C  CA  . SER B 2 420 ? 20.090  110.264 -26.087 1.00 39.52 ? 420  SER B CA  1 
ATOM   6884 C  C   . SER B 2 420 ? 18.655  109.749 -25.970 1.00 40.91 ? 420  SER B C   1 
ATOM   6885 O  O   . SER B 2 420 ? 18.477  108.630 -25.459 1.00 42.47 ? 420  SER B O   1 
ATOM   6886 C  CB  . SER B 2 420 ? 20.697  109.880 -27.416 1.00 39.34 ? 420  SER B CB  1 
ATOM   6887 O  OG  . SER B 2 420 ? 19.763  110.039 -28.467 1.00 40.16 ? 420  SER B OG  1 
ATOM   6888 N  N   . GLN B 2 421 ? 17.677  110.532 -26.439 1.00 44.27 ? 421  GLN B N   1 
ATOM   6889 C  CA  . GLN B 2 421 ? 16.253  110.100 -26.537 1.00 46.84 ? 421  GLN B CA  1 
ATOM   6890 C  C   . GLN B 2 421 ? 15.940  109.571 -27.946 1.00 46.30 ? 421  GLN B C   1 
ATOM   6891 O  O   . GLN B 2 421 ? 14.811  109.074 -28.133 1.00 49.60 ? 421  GLN B O   1 
ATOM   6892 C  CB  . GLN B 2 421 ? 15.300  111.238 -26.165 1.00 47.70 ? 421  GLN B CB  1 
ATOM   6893 C  CG  . GLN B 2 421 ? 15.151  111.434 -24.664 1.00 48.16 ? 421  GLN B CG  1 
ATOM   6894 C  CD  . GLN B 2 421 ? 14.068  112.426 -24.310 1.00 50.96 ? 421  GLN B CD  1 
ATOM   6895 O  OE1 . GLN B 2 421 ? 13.400  112.995 -25.172 1.00 52.26 ? 421  GLN B OE1 1 
ATOM   6896 N  NE2 . GLN B 2 421 ? 13.890  112.651 -23.019 1.00 53.41 ? 421  GLN B NE2 1 
ATOM   6897 N  N   . VAL B 2 422 ? 16.881  109.654 -28.897 1.00 45.47 ? 422  VAL B N   1 
ATOM   6898 C  CA  . VAL B 2 422 ? 16.646  109.234 -30.316 1.00 46.39 ? 422  VAL B CA  1 
ATOM   6899 C  C   . VAL B 2 422 ? 17.649  108.158 -30.763 1.00 46.16 ? 422  VAL B C   1 
ATOM   6900 O  O   . VAL B 2 422 ? 17.409  107.579 -31.836 1.00 45.57 ? 422  VAL B O   1 
ATOM   6901 C  CB  . VAL B 2 422 ? 16.655  110.435 -31.282 1.00 46.71 ? 422  VAL B CB  1 
ATOM   6902 C  CG1 . VAL B 2 422 ? 15.482  111.361 -31.013 1.00 46.89 ? 422  VAL B CG1 1 
ATOM   6903 C  CG2 . VAL B 2 422 ? 17.969  111.203 -31.253 1.00 46.45 ? 422  VAL B CG2 1 
ATOM   6904 N  N   . LYS B 2 423 ? 18.717  107.911 -29.993 1.00 45.09 ? 423  LYS B N   1 
ATOM   6905 C  CA  . LYS B 2 423 ? 19.721  106.836 -30.236 1.00 42.70 ? 423  LYS B CA  1 
ATOM   6906 C  C   . LYS B 2 423 ? 19.886  106.032 -28.940 1.00 41.13 ? 423  LYS B C   1 
ATOM   6907 O  O   . LYS B 2 423 ? 19.949  106.666 -27.863 1.00 41.86 ? 423  LYS B O   1 
ATOM   6908 C  CB  . LYS B 2 423 ? 21.048  107.448 -30.704 1.00 43.55 ? 423  LYS B CB  1 
ATOM   6909 N  N   . SER B 2 424 ? 19.944  104.699 -29.030 1.00 37.22 ? 424  SER B N   1 
ATOM   6910 C  CA  . SER B 2 424 ? 20.058  103.799 -27.846 1.00 36.56 ? 424  SER B CA  1 
ATOM   6911 C  C   . SER B 2 424 ? 21.535  103.714 -27.416 1.00 35.90 ? 424  SER B C   1 
ATOM   6912 O  O   . SER B 2 424 ? 22.138  102.606 -27.462 1.00 35.56 ? 424  SER B O   1 
ATOM   6913 C  CB  . SER B 2 424 ? 19.422  102.457 -28.085 1.00 37.26 ? 424  SER B CB  1 
ATOM   6914 O  OG  . SER B 2 424 ? 20.072  101.756 -29.127 1.00 39.63 ? 424  SER B OG  1 
ATOM   6915 N  N   . ASP B 2 425 ? 22.073  104.868 -27.001 1.00 32.65 ? 425  ASP B N   1 
ATOM   6916 C  CA  . ASP B 2 425 ? 23.453  105.067 -26.486 1.00 31.35 ? 425  ASP B CA  1 
ATOM   6917 C  C   . ASP B 2 425 ? 23.385  105.175 -24.955 1.00 30.63 ? 425  ASP B C   1 
ATOM   6918 O  O   . ASP B 2 425 ? 22.470  105.861 -24.446 1.00 27.84 ? 425  ASP B O   1 
ATOM   6919 C  CB  . ASP B 2 425 ? 24.091  106.299 -27.128 1.00 31.93 ? 425  ASP B CB  1 
ATOM   6920 C  CG  . ASP B 2 425 ? 24.351  106.150 -28.620 1.00 33.04 ? 425  ASP B CG  1 
ATOM   6921 O  OD1 . ASP B 2 425 ? 24.337  105.002 -29.114 1.00 33.99 ? 425  ASP B OD1 1 
ATOM   6922 O  OD2 . ASP B 2 425 ? 24.564  107.176 -29.273 1.00 33.61 ? 425  ASP B OD2 1 
ATOM   6923 N  N   . TYR B 2 426 ? 24.304  104.519 -24.242 1.00 28.33 ? 426  TYR B N   1 
ATOM   6924 C  CA  . TYR B 2 426 ? 24.277  104.426 -22.757 1.00 27.84 ? 426  TYR B CA  1 
ATOM   6925 C  C   . TYR B 2 426 ? 25.684  104.502 -22.175 1.00 26.93 ? 426  TYR B C   1 
ATOM   6926 O  O   . TYR B 2 426 ? 26.643  104.015 -22.829 1.00 23.98 ? 426  TYR B O   1 
ATOM   6927 C  CB  . TYR B 2 426 ? 23.623  103.121 -22.298 1.00 29.71 ? 426  TYR B CB  1 
ATOM   6928 C  CG  . TYR B 2 426 ? 22.196  102.976 -22.751 1.00 33.13 ? 426  TYR B CG  1 
ATOM   6929 C  CD1 . TYR B 2 426 ? 21.167  103.595 -22.061 1.00 34.88 ? 426  TYR B CD1 1 
ATOM   6930 C  CD2 . TYR B 2 426 ? 21.877  102.256 -23.890 1.00 34.89 ? 426  TYR B CD2 1 
ATOM   6931 C  CE1 . TYR B 2 426 ? 19.852  103.482 -22.473 1.00 36.86 ? 426  TYR B CE1 1 
ATOM   6932 C  CE2 . TYR B 2 426 ? 20.567  102.140 -24.323 1.00 36.13 ? 426  TYR B CE2 1 
ATOM   6933 C  CZ  . TYR B 2 426 ? 19.553  102.756 -23.612 1.00 37.96 ? 426  TYR B CZ  1 
ATOM   6934 O  OH  . TYR B 2 426 ? 18.260  102.634 -24.019 1.00 42.41 ? 426  TYR B OH  1 
ATOM   6935 N  N   . LEU B 2 427 ? 25.773  105.117 -20.990 1.00 24.68 ? 427  LEU B N   1 
ATOM   6936 C  CA  . LEU B 2 427 ? 26.834  104.873 -19.989 1.00 25.50 ? 427  LEU B CA  1 
ATOM   6937 C  C   . LEU B 2 427 ? 26.309  103.816 -19.014 1.00 26.32 ? 427  LEU B C   1 
ATOM   6938 O  O   . LEU B 2 427 ? 25.292  104.075 -18.351 1.00 25.21 ? 427  LEU B O   1 
ATOM   6939 C  CB  . LEU B 2 427 ? 27.173  106.194 -19.297 1.00 25.33 ? 427  LEU B CB  1 
ATOM   6940 C  CG  . LEU B 2 427 ? 28.393  106.184 -18.372 1.00 26.47 ? 427  LEU B CG  1 
ATOM   6941 C  CD1 . LEU B 2 427 ? 29.674  105.880 -19.146 1.00 26.15 ? 427  LEU B CD1 1 
ATOM   6942 C  CD2 . LEU B 2 427 ? 28.507  107.525 -17.653 1.00 26.46 ? 427  LEU B CD2 1 
ATOM   6943 N  N   . LEU B 2 428 ? 26.942  102.641 -18.981 1.00 26.52 ? 428  LEU B N   1 
ATOM   6944 C  CA  . LEU B 2 428 ? 26.469  101.468 -18.200 1.00 26.21 ? 428  LEU B CA  1 
ATOM   6945 C  C   . LEU B 2 428 ? 27.417  101.214 -17.027 1.00 26.51 ? 428  LEU B C   1 
ATOM   6946 O  O   . LEU B 2 428 ? 28.654  101.197 -17.238 1.00 25.33 ? 428  LEU B O   1 
ATOM   6947 C  CB  . LEU B 2 428 ? 26.383  100.248 -19.117 1.00 27.15 ? 428  LEU B CB  1 
ATOM   6948 C  CG  . LEU B 2 428 ? 25.439  100.384 -20.310 1.00 27.45 ? 428  LEU B CG  1 
ATOM   6949 C  CD1 . LEU B 2 428 ? 25.465  99.121  -21.159 1.00 27.97 ? 428  LEU B CD1 1 
ATOM   6950 C  CD2 . LEU B 2 428 ? 24.021  100.689 -19.864 1.00 27.81 ? 428  LEU B CD2 1 
ATOM   6951 N  N   . PHE B 2 429 ? 26.843  101.022 -15.839 1.00 24.98 ? 429  PHE B N   1 
ATOM   6952 C  CA  . PHE B 2 429 ? 27.570  100.675 -14.593 1.00 25.20 ? 429  PHE B CA  1 
ATOM   6953 C  C   . PHE B 2 429 ? 27.222  99.239  -14.205 1.00 25.15 ? 429  PHE B C   1 
ATOM   6954 O  O   . PHE B 2 429 ? 26.051  98.858  -14.317 1.00 24.60 ? 429  PHE B O   1 
ATOM   6955 C  CB  . PHE B 2 429 ? 27.201  101.628 -13.459 1.00 26.00 ? 429  PHE B CB  1 
ATOM   6956 C  CG  . PHE B 2 429 ? 27.650  103.051 -13.648 1.00 26.21 ? 429  PHE B CG  1 
ATOM   6957 C  CD1 . PHE B 2 429 ? 26.972  103.901 -14.509 1.00 27.68 ? 429  PHE B CD1 1 
ATOM   6958 C  CD2 . PHE B 2 429 ? 28.726  103.550 -12.935 1.00 27.11 ? 429  PHE B CD2 1 
ATOM   6959 C  CE1 . PHE B 2 429 ? 27.384  105.214 -14.671 1.00 28.04 ? 429  PHE B CE1 1 
ATOM   6960 C  CE2 . PHE B 2 429 ? 29.129  104.866 -13.088 1.00 26.74 ? 429  PHE B CE2 1 
ATOM   6961 C  CZ  . PHE B 2 429 ? 28.459  105.694 -13.956 1.00 28.26 ? 429  PHE B CZ  1 
ATOM   6962 N  N   . PHE B 2 430 ? 28.203  98.477  -13.729 1.00 24.27 ? 430  PHE B N   1 
ATOM   6963 C  CA  . PHE B 2 430 ? 28.032  97.037  -13.416 1.00 23.96 ? 430  PHE B CA  1 
ATOM   6964 C  C   . PHE B 2 430 ? 28.502  96.728  -12.002 1.00 22.70 ? 430  PHE B C   1 
ATOM   6965 O  O   . PHE B 2 430 ? 29.428  97.386  -11.494 1.00 20.26 ? 430  PHE B O   1 
ATOM   6966 C  CB  . PHE B 2 430 ? 28.754  96.173  -14.441 1.00 25.33 ? 430  PHE B CB  1 
ATOM   6967 C  CG  . PHE B 2 430 ? 28.185  96.337  -15.823 1.00 26.69 ? 430  PHE B CG  1 
ATOM   6968 C  CD1 . PHE B 2 430 ? 26.986  95.737  -16.166 1.00 27.95 ? 430  PHE B CD1 1 
ATOM   6969 C  CD2 . PHE B 2 430 ? 28.821  97.138  -16.759 1.00 28.66 ? 430  PHE B CD2 1 
ATOM   6970 C  CE1 . PHE B 2 430 ? 26.457  95.893  -17.437 1.00 28.95 ? 430  PHE B CE1 1 
ATOM   6971 C  CE2 . PHE B 2 430 ? 28.286  97.293  -18.029 1.00 29.20 ? 430  PHE B CE2 1 
ATOM   6972 C  CZ  . PHE B 2 430 ? 27.104  96.676  -18.361 1.00 28.44 ? 430  PHE B CZ  1 
ATOM   6973 N  N   . ARG B 2 431 ? 27.841  95.741  -11.398 1.00 23.21 ? 431  ARG B N   1 
ATOM   6974 C  CA  . ARG B 2 431 ? 28.232  95.163  -10.090 1.00 23.84 ? 431  ARG B CA  1 
ATOM   6975 C  C   . ARG B 2 431 ? 28.256  93.647  -10.211 1.00 24.86 ? 431  ARG B C   1 
ATOM   6976 O  O   . ARG B 2 431 ? 27.374  93.049  -10.828 1.00 24.81 ? 431  ARG B O   1 
ATOM   6977 C  CB  . ARG B 2 431 ? 27.281  95.654  -9.000  1.00 23.01 ? 431  ARG B CB  1 
ATOM   6978 C  CG  . ARG B 2 431 ? 27.598  97.063  -8.523  1.00 23.39 ? 431  ARG B CG  1 
ATOM   6979 C  CD  . ARG B 2 431 ? 26.584  97.531  -7.510  1.00 23.67 ? 431  ARG B CD  1 
ATOM   6980 N  NE  . ARG B 2 431 ? 26.741  98.926  -7.141  1.00 24.29 ? 431  ARG B NE  1 
ATOM   6981 C  CZ  . ARG B 2 431 ? 25.988  99.563  -6.245  1.00 25.66 ? 431  ARG B CZ  1 
ATOM   6982 N  NH1 . ARG B 2 431 ? 25.008  98.936  -5.606  1.00 25.60 ? 431  ARG B NH1 1 
ATOM   6983 N  NH2 . ARG B 2 431 ? 26.241  100.831 -5.973  1.00 26.65 ? 431  ARG B NH2 1 
HETATM 6984 N  N   . MLZ B 2 432 ? 29.294  93.055  -9.620  1.00 25.73 ? 432  MLZ B N   1 
HETATM 6985 C  CA  . MLZ B 2 432 ? 29.464  91.616  -9.608  1.00 27.55 ? 432  MLZ B CA  1 
HETATM 6986 C  CB  . MLZ B 2 432 ? 30.812  91.245  -8.990  1.00 30.10 ? 432  MLZ B CB  1 
HETATM 6987 C  CG  . MLZ B 2 432 ? 32.031  91.487  -9.858  1.00 33.32 ? 432  MLZ B CG  1 
HETATM 6988 C  CD  . MLZ B 2 432 ? 33.304  91.329  -9.064  1.00 37.30 ? 432  MLZ B CD  1 
HETATM 6989 C  CE  . MLZ B 2 432 ? 34.571  91.678  -9.826  1.00 38.09 ? 432  MLZ B CE  1 
HETATM 6990 N  NZ  . MLZ B 2 432 ? 35.737  91.345  -9.004  1.00 41.38 ? 432  MLZ B NZ  1 
HETATM 6991 C  CM  . MLZ B 2 432 ? 36.028  92.224  -7.864  1.00 42.28 ? 432  MLZ B CM  1 
HETATM 6992 C  C   . MLZ B 2 432 ? 28.360  90.981  -8.770  1.00 27.26 ? 432  MLZ B C   1 
HETATM 6993 O  O   . MLZ B 2 432 ? 27.709  91.643  -7.967  1.00 25.73 ? 432  MLZ B O   1 
ATOM   6994 N  N   . GLU B 2 433 ? 28.188  89.677  -8.956  1.00 29.45 ? 433  GLU B N   1 
ATOM   6995 C  CA  . GLU B 2 433 ? 27.354  88.870  -8.083  1.00 32.09 ? 433  GLU B CA  1 
ATOM   6996 C  C   . GLU B 2 433 ? 27.809  89.075  -6.636  1.00 31.05 ? 433  GLU B C   1 
ATOM   6997 O  O   . GLU B 2 433 ? 29.024  89.041  -6.395  1.00 29.59 ? 433  GLU B O   1 
ATOM   6998 C  CB  . GLU B 2 433 ? 27.479  87.398  -8.468  1.00 34.49 ? 433  GLU B CB  1 
ATOM   6999 C  CG  . GLU B 2 433 ? 26.202  86.626  -8.270  1.00 36.21 ? 433  GLU B CG  1 
ATOM   7000 C  CD  . GLU B 2 433 ? 26.364  85.149  -8.564  1.00 38.60 ? 433  GLU B CD  1 
ATOM   7001 O  OE1 . GLU B 2 433 ? 25.480  84.379  -8.144  1.00 37.62 ? 433  GLU B OE1 1 
ATOM   7002 O  OE2 . GLU B 2 433 ? 27.384  84.787  -9.199  1.00 37.43 ? 433  GLU B OE2 1 
ATOM   7003 N  N   . ILE B 2 434 ? 26.869  89.311  -5.721  1.00 32.61 ? 434  ILE B N   1 
ATOM   7004 C  CA  . ILE B 2 434 ? 27.173  89.766  -4.333  1.00 34.41 ? 434  ILE B CA  1 
ATOM   7005 C  C   . ILE B 2 434 ? 28.104  88.756  -3.643  1.00 35.29 ? 434  ILE B C   1 
ATOM   7006 O  O   . ILE B 2 434 ? 28.983  89.227  -2.907  1.00 35.76 ? 434  ILE B O   1 
ATOM   7007 C  CB  . ILE B 2 434 ? 25.883  90.069  -3.537  1.00 36.78 ? 434  ILE B CB  1 
ATOM   7008 C  CG1 . ILE B 2 434 ? 26.190  90.730  -2.191  1.00 38.83 ? 434  ILE B CG1 1 
ATOM   7009 C  CG2 . ILE B 2 434 ? 25.020  88.828  -3.369  1.00 37.11 ? 434  ILE B CG2 1 
ATOM   7010 C  CD1 . ILE B 2 434 ? 24.979  91.369  -1.537  1.00 40.30 ? 434  ILE B CD1 1 
ATOM   7011 N  N   . VAL B 2 435 ? 27.972  87.445  -3.900  1.00 36.66 ? 435  VAL B N   1 
ATOM   7012 C  CA  . VAL B 2 435 ? 28.837  86.395  -3.265  1.00 39.40 ? 435  VAL B CA  1 
ATOM   7013 C  C   . VAL B 2 435 ? 30.295  86.545  -3.715  1.00 42.17 ? 435  VAL B C   1 
ATOM   7014 O  O   . VAL B 2 435 ? 31.164  86.044  -2.979  1.00 43.40 ? 435  VAL B O   1 
ATOM   7015 C  CB  . VAL B 2 435 ? 28.377  84.944  -3.498  1.00 39.61 ? 435  VAL B CB  1 
ATOM   7016 C  CG1 . VAL B 2 435 ? 27.102  84.638  -2.741  1.00 41.10 ? 435  VAL B CG1 1 
ATOM   7017 C  CG2 . VAL B 2 435 ? 28.259  84.584  -4.972  1.00 41.00 ? 435  VAL B CG2 1 
ATOM   7018 N  N   . GLN B 2 436 ? 30.553  87.174  -4.866  1.00 42.07 ? 436  GLN B N   1 
ATOM   7019 C  CA  . GLN B 2 436 ? 31.929  87.394  -5.395  1.00 43.23 ? 436  GLN B CA  1 
ATOM   7020 C  C   . GLN B 2 436 ? 32.646  88.476  -4.580  1.00 41.32 ? 436  GLN B C   1 
ATOM   7021 O  O   . GLN B 2 436 ? 33.880  88.507  -4.622  1.00 43.88 ? 436  GLN B O   1 
ATOM   7022 C  CB  . GLN B 2 436 ? 31.903  87.836  -6.860  1.00 44.80 ? 436  GLN B CB  1 
ATOM   7023 C  CG  . GLN B 2 436 ? 31.310  86.807  -7.811  1.00 46.56 ? 436  GLN B CG  1 
ATOM   7024 C  CD  . GLN B 2 436 ? 32.232  85.632  -8.022  1.00 50.49 ? 436  GLN B CD  1 
ATOM   7025 O  OE1 . GLN B 2 436 ? 33.453  85.776  -8.049  1.00 53.61 ? 436  GLN B OE1 1 
ATOM   7026 N  NE2 . GLN B 2 436 ? 31.648  84.457  -8.190  1.00 52.37 ? 436  GLN B NE2 1 
ATOM   7027 N  N   . ASN B 2 437 ? 31.901  89.367  -3.924  1.00 40.36 ? 437  ASN B N   1 
ATOM   7028 C  CA  . ASN B 2 437 ? 32.467  90.526  -3.181  1.00 40.91 ? 437  ASN B CA  1 
ATOM   7029 C  C   . ASN B 2 437 ? 32.383  90.250  -1.677  1.00 40.35 ? 437  ASN B C   1 
ATOM   7030 O  O   . ASN B 2 437 ? 32.584  91.201  -0.901  1.00 42.26 ? 437  ASN B O   1 
ATOM   7031 C  CB  . ASN B 2 437 ? 31.778  91.838  -3.580  1.00 42.13 ? 437  ASN B CB  1 
ATOM   7032 C  CG  . ASN B 2 437 ? 32.181  92.314  -4.962  1.00 42.97 ? 437  ASN B CG  1 
ATOM   7033 O  OD1 . ASN B 2 437 ? 33.282  92.035  -5.429  1.00 44.00 ? 437  ASN B OD1 1 
ATOM   7034 N  ND2 . ASN B 2 437 ? 31.300  93.038  -5.630  1.00 45.15 ? 437  ASN B ND2 1 
ATOM   7035 N  N   . LEU B 2 438 ? 32.125  88.996  -1.292  1.00 37.73 ? 438  LEU B N   1 
ATOM   7036 C  CA  . LEU B 2 438 ? 32.041  88.554  0.126   1.00 38.70 ? 438  LEU B CA  1 
ATOM   7037 C  C   . LEU B 2 438 ? 33.413  88.745  0.785   1.00 38.06 ? 438  LEU B C   1 
ATOM   7038 O  O   . LEU B 2 438 ? 34.429  88.357  0.176   1.00 36.37 ? 438  LEU B O   1 
ATOM   7039 C  CB  . LEU B 2 438 ? 31.604  87.085  0.168   1.00 40.26 ? 438  LEU B CB  1 
ATOM   7040 C  CG  . LEU B 2 438 ? 30.392  86.738  1.034   1.00 41.23 ? 438  LEU B CG  1 
ATOM   7041 C  CD1 . LEU B 2 438 ? 29.316  87.815  0.997   1.00 41.13 ? 438  LEU B CD1 1 
ATOM   7042 C  CD2 . LEU B 2 438 ? 29.804  85.410  0.590   1.00 41.42 ? 438  LEU B CD2 1 
ATOM   7043 N  N   . ASN B 2 439 ? 33.439  89.352  1.974   1.00 37.13 ? 439  ASN B N   1 
ATOM   7044 C  CA  . ASN B 2 439 ? 34.640  89.382  2.845   1.00 35.77 ? 439  ASN B CA  1 
ATOM   7045 C  C   . ASN B 2 439 ? 34.274  88.702  4.167   1.00 34.44 ? 439  ASN B C   1 
ATOM   7046 O  O   . ASN B 2 439 ? 34.108  89.395  5.183   1.00 33.83 ? 439  ASN B O   1 
ATOM   7047 C  CB  . ASN B 2 439 ? 35.206  90.792  3.024   1.00 37.02 ? 439  ASN B CB  1 
ATOM   7048 C  CG  . ASN B 2 439 ? 36.543  90.765  3.738   1.00 40.18 ? 439  ASN B CG  1 
ATOM   7049 O  OD1 . ASN B 2 439 ? 37.266  89.778  3.657   1.00 42.05 ? 439  ASN B OD1 1 
ATOM   7050 N  ND2 . ASN B 2 439 ? 36.884  91.834  4.437   1.00 41.95 ? 439  ASN B ND2 1 
ATOM   7051 N  N   . TRP B 2 440 ? 34.149  87.377  4.129   1.00 34.37 ? 440  TRP B N   1 
ATOM   7052 C  CA  . TRP B 2 440 ? 33.729  86.537  5.277   1.00 34.67 ? 440  TRP B CA  1 
ATOM   7053 C  C   . TRP B 2 440 ? 34.967  86.107  6.065   1.00 34.65 ? 440  TRP B C   1 
ATOM   7054 O  O   . TRP B 2 440 ? 35.834  85.466  5.471   1.00 32.93 ? 440  TRP B O   1 
ATOM   7055 C  CB  . TRP B 2 440 ? 32.926  85.340  4.767   1.00 34.72 ? 440  TRP B CB  1 
ATOM   7056 C  CG  . TRP B 2 440 ? 32.388  84.444  5.837   1.00 33.34 ? 440  TRP B CG  1 
ATOM   7057 C  CD1 . TRP B 2 440 ? 31.645  84.801  6.924   1.00 34.18 ? 440  TRP B CD1 1 
ATOM   7058 C  CD2 . TRP B 2 440 ? 32.516  83.013  5.889   1.00 34.25 ? 440  TRP B CD2 1 
ATOM   7059 N  NE1 . TRP B 2 440 ? 31.313  83.693  7.659   1.00 33.71 ? 440  TRP B NE1 1 
ATOM   7060 C  CE2 . TRP B 2 440 ? 31.822  82.580  7.042   1.00 33.22 ? 440  TRP B CE2 1 
ATOM   7061 C  CE3 . TRP B 2 440 ? 33.138  82.059  5.070   1.00 34.76 ? 440  TRP B CE3 1 
ATOM   7062 C  CZ2 . TRP B 2 440 ? 31.749  81.234  7.400   1.00 34.35 ? 440  TRP B CZ2 1 
ATOM   7063 C  CZ3 . TRP B 2 440 ? 33.058  80.728  5.422   1.00 35.45 ? 440  TRP B CZ3 1 
ATOM   7064 C  CH2 . TRP B 2 440 ? 32.374  80.324  6.572   1.00 35.49 ? 440  TRP B CH2 1 
ATOM   7065 N  N   . ALA B 2 441 ? 35.016  86.448  7.356   1.00 33.41 ? 441  ALA B N   1 
ATOM   7066 C  CA  . ALA B 2 441 ? 36.114  86.104  8.292   1.00 33.95 ? 441  ALA B CA  1 
ATOM   7067 C  C   . ALA B 2 441 ? 35.857  84.737  8.944   1.00 33.22 ? 441  ALA B C   1 
ATOM   7068 O  O   . ALA B 2 441 ? 36.646  84.362  9.804   1.00 33.83 ? 441  ALA B O   1 
ATOM   7069 C  CB  . ALA B 2 441 ? 36.253  87.189  9.335   1.00 32.91 ? 441  ALA B CB  1 
ATOM   7070 N  N   . GLY B 2 442 ? 34.804  84.015  8.543   1.00 33.73 ? 442  GLY B N   1 
ATOM   7071 C  CA  . GLY B 2 442 ? 34.359  82.787  9.227   1.00 35.31 ? 442  GLY B CA  1 
ATOM   7072 C  C   . GLY B 2 442 ? 35.166  81.562  8.823   1.00 38.98 ? 442  GLY B C   1 
ATOM   7073 O  O   . GLY B 2 442 ? 35.951  81.637  7.854   1.00 37.45 ? 442  GLY B O   1 
ATOM   7074 N  N   . ASN B 2 443 ? 34.974  80.469  9.561   1.00 40.91 ? 443  ASN B N   1 
ATOM   7075 C  CA  . ASN B 2 443 ? 35.681  79.175  9.379   1.00 42.85 ? 443  ASN B CA  1 
ATOM   7076 C  C   . ASN B 2 443 ? 34.765  78.222  8.619   1.00 43.40 ? 443  ASN B C   1 
ATOM   7077 O  O   . ASN B 2 443 ? 33.762  77.769  9.169   1.00 41.74 ? 443  ASN B O   1 
ATOM   7078 C  CB  . ASN B 2 443 ? 36.094  78.570  10.722  1.00 43.77 ? 443  ASN B CB  1 
ATOM   7079 C  CG  . ASN B 2 443 ? 36.922  77.310  10.579  1.00 43.74 ? 443  ASN B CG  1 
ATOM   7080 O  OD1 . ASN B 2 443 ? 37.077  76.772  9.483   1.00 42.10 ? 443  ASN B OD1 1 
ATOM   7081 N  ND2 . ASN B 2 443 ? 37.473  76.842  11.684  1.00 44.17 ? 443  ASN B ND2 1 
ATOM   7082 N  N   . PRO B 2 444 ? 35.087  77.873  7.349   1.00 47.68 ? 444  PRO B N   1 
ATOM   7083 C  CA  . PRO B 2 444 ? 34.233  76.981  6.559   1.00 49.16 ? 444  PRO B CA  1 
ATOM   7084 C  C   . PRO B 2 444 ? 34.131  75.565  7.150   1.00 48.75 ? 444  PRO B C   1 
ATOM   7085 O  O   . PRO B 2 444 ? 33.195  74.882  6.802   1.00 51.82 ? 444  PRO B O   1 
ATOM   7086 C  CB  . PRO B 2 444 ? 34.885  76.956  5.163   1.00 48.54 ? 444  PRO B CB  1 
ATOM   7087 C  CG  . PRO B 2 444 ? 36.317  77.401  5.389   1.00 49.34 ? 444  PRO B CG  1 
ATOM   7088 C  CD  . PRO B 2 444 ? 36.285  78.305  6.607   1.00 48.42 ? 444  PRO B CD  1 
ATOM   7089 N  N   . GLU B 2 445 ? 35.059  75.188  8.040   1.00 48.88 ? 445  GLU B N   1 
ATOM   7090 C  CA  . GLU B 2 445 ? 35.142  73.843  8.677   1.00 51.79 ? 445  GLU B CA  1 
ATOM   7091 C  C   . GLU B 2 445 ? 34.408  73.807  10.020  1.00 50.74 ? 445  GLU B C   1 
ATOM   7092 O  O   . GLU B 2 445 ? 34.325  72.747  10.636  1.00 53.59 ? 445  GLU B O   1 
ATOM   7093 C  CB  . GLU B 2 445 ? 36.608  73.439  8.859   1.00 55.26 ? 445  GLU B CB  1 
ATOM   7094 C  CG  . GLU B 2 445 ? 37.338  73.192  7.549   1.00 59.03 ? 445  GLU B CG  1 
ATOM   7095 C  CD  . GLU B 2 445 ? 38.765  72.688  7.694   1.00 65.27 ? 445  GLU B CD  1 
ATOM   7096 O  OE1 . GLU B 2 445 ? 39.303  72.150  6.704   1.00 70.76 ? 445  GLU B OE1 1 
ATOM   7097 O  OE2 . GLU B 2 445 ? 39.340  72.836  8.795   1.00 70.02 ? 445  GLU B OE2 1 
HETATM 7098 N  N   . MLZ B 2 446 ? 33.879  74.947  10.485  1.00 47.70 ? 446  MLZ B N   1 
HETATM 7099 C  CA  . MLZ B 2 446 ? 33.115  74.964  11.724  1.00 44.68 ? 446  MLZ B CA  1 
HETATM 7100 C  CB  . MLZ B 2 446 ? 32.973  76.382  12.286  1.00 45.08 ? 446  MLZ B CB  1 
HETATM 7101 C  CG  . MLZ B 2 446 ? 31.955  76.544  13.410  1.00 44.30 ? 446  MLZ B CG  1 
HETATM 7102 C  CD  . MLZ B 2 446 ? 32.251  75.729  14.662  1.00 44.43 ? 446  MLZ B CD  1 
HETATM 7103 C  CE  . MLZ B 2 446 ? 31.331  76.112  15.813  1.00 43.55 ? 446  MLZ B CE  1 
HETATM 7104 N  NZ  . MLZ B 2 446 ? 31.261  75.105  16.876  1.00 44.46 ? 446  MLZ B NZ  1 
HETATM 7105 C  CM  . MLZ B 2 446 ? 32.490  74.863  17.650  1.00 44.30 ? 446  MLZ B CM  1 
HETATM 7106 C  C   . MLZ B 2 446 ? 31.750  74.339  11.452  1.00 41.69 ? 446  MLZ B C   1 
HETATM 7107 O  O   . MLZ B 2 446 ? 31.025  74.785  10.561  1.00 37.73 ? 446  MLZ B O   1 
ATOM   7108 N  N   . SER B 2 447 ? 31.427  73.294  12.223  1.00 40.11 ? 447  SER B N   1 
ATOM   7109 C  CA  . SER B 2 447 ? 30.156  72.602  12.095  1.00 40.56 ? 447  SER B CA  1 
ATOM   7110 C  C   . SER B 2 447 ? 29.351  72.796  13.380  1.00 37.46 ? 447  SER B C   1 
ATOM   7111 O  O   . SER B 2 447 ? 29.956  73.120  14.417  1.00 37.53 ? 447  SER B O   1 
ATOM   7112 C  CB  . SER B 2 447 ? 30.360  71.139  11.807  1.00 43.41 ? 447  SER B CB  1 
ATOM   7113 O  OG  . SER B 2 447 ? 30.891  70.489  12.952  1.00 48.17 ? 447  SER B OG  1 
ATOM   7114 N  N   . TYR B 2 448 ? 28.039  72.588  13.304  1.00 34.26 ? 448  TYR B N   1 
ATOM   7115 C  CA  . TYR B 2 448 ? 27.089  72.798  14.425  1.00 35.55 ? 448  TYR B CA  1 
ATOM   7116 C  C   . TYR B 2 448 ? 26.299  71.514  14.671  1.00 35.52 ? 448  TYR B C   1 
ATOM   7117 O  O   . TYR B 2 448 ? 25.852  70.869  13.701  1.00 34.46 ? 448  TYR B O   1 
ATOM   7118 C  CB  . TYR B 2 448 ? 26.172  73.993  14.136  1.00 33.68 ? 448  TYR B CB  1 
ATOM   7119 C  CG  . TYR B 2 448 ? 26.933  75.288  14.025  1.00 30.65 ? 448  TYR B CG  1 
ATOM   7120 C  CD1 . TYR B 2 448 ? 27.211  76.049  15.149  1.00 30.09 ? 448  TYR B CD1 1 
ATOM   7121 C  CD2 . TYR B 2 448 ? 27.432  75.721  12.808  1.00 29.59 ? 448  TYR B CD2 1 
ATOM   7122 C  CE1 . TYR B 2 448 ? 27.959  77.214  15.068  1.00 28.81 ? 448  TYR B CE1 1 
ATOM   7123 C  CE2 . TYR B 2 448 ? 28.169  76.890  12.704  1.00 29.41 ? 448  TYR B CE2 1 
ATOM   7124 C  CZ  . TYR B 2 448 ? 28.435  77.640  13.838  1.00 29.88 ? 448  TYR B CZ  1 
ATOM   7125 O  OH  . TYR B 2 448 ? 29.170  78.786  13.748  1.00 29.18 ? 448  TYR B OH  1 
ATOM   7126 N  N   . GLU B 2 449 ? 26.124  71.177  15.947  1.00 38.00 ? 449  GLU B N   1 
ATOM   7127 C  CA  . GLU B 2 449 ? 25.156  70.150  16.399  1.00 40.82 ? 449  GLU B CA  1 
ATOM   7128 C  C   . GLU B 2 449 ? 23.755  70.706  16.119  1.00 38.69 ? 449  GLU B C   1 
ATOM   7129 O  O   . GLU B 2 449 ? 23.629  71.935  15.889  1.00 35.03 ? 449  GLU B O   1 
ATOM   7130 C  CB  . GLU B 2 449 ? 25.405  69.797  17.869  1.00 46.50 ? 449  GLU B CB  1 
ATOM   7131 C  CG  . GLU B 2 449 ? 24.620  68.588  18.370  1.00 53.19 ? 449  GLU B CG  1 
ATOM   7132 C  CD  . GLU B 2 449 ? 24.700  67.311  17.541  1.00 56.29 ? 449  GLU B CD  1 
ATOM   7133 O  OE1 . GLU B 2 449 ? 25.492  66.411  17.914  1.00 61.47 ? 449  GLU B OE1 1 
ATOM   7134 O  OE2 . GLU B 2 449 ? 23.943  67.196  16.543  1.00 53.82 ? 449  GLU B OE2 1 
ATOM   7135 N  N   . THR B 2 450 ? 22.753  69.831  16.091  1.00 36.35 ? 450  THR B N   1 
ATOM   7136 C  CA  . THR B 2 450 ? 21.352  70.175  15.742  1.00 37.23 ? 450  THR B CA  1 
ATOM   7137 C  C   . THR B 2 450 ? 20.413  69.618  16.812  1.00 35.17 ? 450  THR B C   1 
ATOM   7138 O  O   . THR B 2 450 ? 20.837  68.746  17.587  1.00 33.62 ? 450  THR B O   1 
ATOM   7139 C  CB  . THR B 2 450 ? 21.013  69.647  14.344  1.00 38.87 ? 450  THR B CB  1 
ATOM   7140 O  OG1 . THR B 2 450 ? 21.034  68.220  14.388  1.00 41.61 ? 450  THR B OG1 1 
ATOM   7141 C  CG2 . THR B 2 450 ? 21.982  70.131  13.289  1.00 39.55 ? 450  THR B CG2 1 
ATOM   7142 N  N   . GLY B 2 451 ? 19.192  70.143  16.865  1.00 35.95 ? 451  GLY B N   1 
ATOM   7143 C  CA  . GLY B 2 451 ? 18.107  69.615  17.708  1.00 36.39 ? 451  GLY B CA  1 
ATOM   7144 C  C   . GLY B 2 451 ? 17.086  68.885  16.848  1.00 35.67 ? 451  GLY B C   1 
ATOM   7145 O  O   . GLY B 2 451 ? 17.334  68.623  15.673  1.00 36.64 ? 451  GLY B O   1 
ATOM   7146 N  N   . PRO B 2 452 ? 15.900  68.552  17.396  1.00 37.42 ? 452  PRO B N   1 
ATOM   7147 C  CA  . PRO B 2 452 ? 14.858  67.881  16.612  1.00 37.59 ? 452  PRO B CA  1 
ATOM   7148 C  C   . PRO B 2 452 ? 14.468  68.540  15.278  1.00 37.04 ? 452  PRO B C   1 
ATOM   7149 O  O   . PRO B 2 452 ? 13.995  67.824  14.428  1.00 37.87 ? 452  PRO B O   1 
ATOM   7150 C  CB  . PRO B 2 452 ? 13.657  67.893  17.569  1.00 37.41 ? 452  PRO B CB  1 
ATOM   7151 C  CG  . PRO B 2 452 ? 14.294  67.868  18.948  1.00 38.43 ? 452  PRO B CG  1 
ATOM   7152 C  CD  . PRO B 2 452 ? 15.529  68.736  18.811  1.00 37.16 ? 452  PRO B CD  1 
ATOM   7153 N  N   . MET B 2 453 ? 14.658  69.858  15.116  1.00 37.61 ? 453  MET B N   1 
ATOM   7154 C  CA  . MET B 2 453 ? 14.234  70.603  13.893  1.00 36.63 ? 453  MET B CA  1 
ATOM   7155 C  C   . MET B 2 453 ? 15.287  70.456  12.786  1.00 32.89 ? 453  MET B C   1 
ATOM   7156 O  O   . MET B 2 453 ? 14.987  70.825  11.640  1.00 32.23 ? 453  MET B O   1 
ATOM   7157 C  CB  . MET B 2 453 ? 13.999  72.092  14.175  1.00 39.65 ? 453  MET B CB  1 
ATOM   7158 C  CG  . MET B 2 453 ? 12.872  72.375  15.153  1.00 43.23 ? 453  MET B CG  1 
ATOM   7159 S  SD  . MET B 2 453 ? 11.232  72.070  14.447  1.00 52.86 ? 453  MET B SD  1 
ATOM   7160 C  CE  . MET B 2 453 ? 10.946  70.386  14.990  1.00 54.50 ? 453  MET B CE  1 
ATOM   7161 N  N   . GLY B 2 454 ? 16.476  69.951  13.111  1.00 31.95 ? 454  GLY B N   1 
ATOM   7162 C  CA  . GLY B 2 454 ? 17.533  69.675  12.120  1.00 32.47 ? 454  GLY B CA  1 
ATOM   7163 C  C   . GLY B 2 454 ? 18.384  70.902  11.844  1.00 34.65 ? 454  GLY B C   1 
ATOM   7164 O  O   . GLY B 2 454 ? 18.268  71.902  12.597  1.00 34.80 ? 454  GLY B O   1 
ATOM   7165 N  N   . ASP B 2 455 ? 19.175  70.847  10.772  1.00 34.09 ? 455  ASP B N   1 
ATOM   7166 C  CA  . ASP B 2 455 ? 20.317  71.765  10.531  1.00 36.13 ? 455  ASP B CA  1 
ATOM   7167 C  C   . ASP B 2 455 ? 19.837  73.123  10.000  1.00 33.58 ? 455  ASP B C   1 
ATOM   7168 O  O   . ASP B 2 455 ? 20.700  74.002  9.847   1.00 34.73 ? 455  ASP B O   1 
ATOM   7169 C  CB  . ASP B 2 455 ? 21.349  71.129  9.598   1.00 37.88 ? 455  ASP B CB  1 
ATOM   7170 C  CG  . ASP B 2 455 ? 20.825  70.822  8.206   1.00 41.07 ? 455  ASP B CG  1 
ATOM   7171 O  OD1 . ASP B 2 455 ? 19.587  70.845  8.018   1.00 42.43 ? 455  ASP B OD1 1 
ATOM   7172 O  OD2 . ASP B 2 455 ? 21.662  70.552  7.321   1.00 46.49 ? 455  ASP B OD2 1 
ATOM   7173 N  N   . ARG B 2 456 ? 18.536  73.301  9.739   1.00 32.55 ? 456  ARG B N   1 
ATOM   7174 C  CA  . ARG B 2 456 ? 17.967  74.637  9.382   1.00 32.53 ? 456  ARG B CA  1 
ATOM   7175 C  C   . ARG B 2 456 ? 18.402  75.675  10.429  1.00 30.47 ? 456  ARG B C   1 
ATOM   7176 O  O   . ARG B 2 456 ? 18.725  76.812  10.042  1.00 30.53 ? 456  ARG B O   1 
ATOM   7177 C  CB  . ARG B 2 456 ? 16.439  74.608  9.270   1.00 32.22 ? 456  ARG B CB  1 
ATOM   7178 C  CG  . ARG B 2 456 ? 15.790  75.976  9.068   1.00 33.60 ? 456  ARG B CG  1 
ATOM   7179 C  CD  . ARG B 2 456 ? 16.296  76.719  7.835   1.00 33.44 ? 456  ARG B CD  1 
ATOM   7180 N  NE  . ARG B 2 456 ? 15.719  78.057  7.665   1.00 34.20 ? 456  ARG B NE  1 
ATOM   7181 C  CZ  . ARG B 2 456 ? 16.211  79.193  8.165   1.00 32.76 ? 456  ARG B CZ  1 
ATOM   7182 N  NH1 . ARG B 2 456 ? 17.306  79.189  8.909   1.00 31.39 ? 456  ARG B NH1 1 
ATOM   7183 N  NH2 . ARG B 2 456 ? 15.600  80.340  7.914   1.00 32.08 ? 456  ARG B NH2 1 
ATOM   7184 N  N   . LEU B 2 457 ? 18.426  75.294  11.705  1.00 29.21 ? 457  LEU B N   1 
ATOM   7185 C  CA  . LEU B 2 457 ? 18.642  76.234  12.837  1.00 28.66 ? 457  LEU B CA  1 
ATOM   7186 C  C   . LEU B 2 457 ? 20.130  76.293  13.196  1.00 26.82 ? 457  LEU B C   1 
ATOM   7187 O  O   . LEU B 2 457 ? 20.468  76.144  14.389  1.00 27.19 ? 457  LEU B O   1 
ATOM   7188 C  CB  . LEU B 2 457 ? 17.773  75.782  14.015  1.00 28.57 ? 457  LEU B CB  1 
ATOM   7189 C  CG  . LEU B 2 457 ? 16.269  75.730  13.744  1.00 28.49 ? 457  LEU B CG  1 
ATOM   7190 C  CD1 . LEU B 2 457 ? 15.511  75.346  15.002  1.00 27.47 ? 457  LEU B CD1 1 
ATOM   7191 C  CD2 . LEU B 2 457 ? 15.743  77.054  13.207  1.00 28.67 ? 457  LEU B CD2 1 
ATOM   7192 N  N   . THR B 2 458 ? 20.985  76.515  12.194  1.00 26.84 ? 458  THR B N   1 
ATOM   7193 C  CA  . THR B 2 458 ? 22.456  76.647  12.362  1.00 26.67 ? 458  THR B CA  1 
ATOM   7194 C  C   . THR B 2 458 ? 22.942  77.805  11.503  1.00 26.69 ? 458  THR B C   1 
ATOM   7195 O  O   . THR B 2 458 ? 22.390  78.042  10.425  1.00 25.82 ? 458  THR B O   1 
ATOM   7196 C  CB  . THR B 2 458 ? 23.192  75.348  12.002  1.00 26.90 ? 458  THR B CB  1 
ATOM   7197 O  OG1 . THR B 2 458 ? 23.045  75.104  10.601  1.00 28.40 ? 458  THR B OG1 1 
ATOM   7198 C  CG2 . THR B 2 458 ? 22.688  74.157  12.785  1.00 26.92 ? 458  THR B CG2 1 
ATOM   7199 N  N   . PRO B 2 459 ? 23.974  78.555  11.955  1.00 26.31 ? 459  PRO B N   1 
ATOM   7200 C  CA  . PRO B 2 459 ? 24.586  79.604  11.134  1.00 27.05 ? 459  PRO B CA  1 
ATOM   7201 C  C   . PRO B 2 459 ? 25.074  79.112  9.764   1.00 26.23 ? 459  PRO B C   1 
ATOM   7202 O  O   . PRO B 2 459 ? 24.929  79.849  8.808   1.00 24.60 ? 459  PRO B O   1 
ATOM   7203 C  CB  . PRO B 2 459 ? 25.749  80.102  12.009  1.00 26.60 ? 459  PRO B CB  1 
ATOM   7204 C  CG  . PRO B 2 459 ? 25.275  79.837  13.421  1.00 25.77 ? 459  PRO B CG  1 
ATOM   7205 C  CD  . PRO B 2 459 ? 24.540  78.518  13.315  1.00 26.30 ? 459  PRO B CD  1 
ATOM   7206 N  N   . ARG B 2 460 ? 25.602  77.889  9.692   1.00 28.76 ? 460  ARG B N   1 
ATOM   7207 C  CA  . ARG B 2 460 ? 26.108  77.306  8.416   1.00 32.22 ? 460  ARG B CA  1 
ATOM   7208 C  C   . ARG B 2 460 ? 24.965  77.244  7.394   1.00 31.28 ? 460  ARG B C   1 
ATOM   7209 O  O   . ARG B 2 460 ? 25.171  77.672  6.252   1.00 30.96 ? 460  ARG B O   1 
ATOM   7210 C  CB  . ARG B 2 460 ? 26.740  75.932  8.632   1.00 36.32 ? 460  ARG B CB  1 
ATOM   7211 C  CG  . ARG B 2 460 ? 27.212  75.274  7.342   1.00 40.95 ? 460  ARG B CG  1 
ATOM   7212 C  CD  . ARG B 2 460 ? 27.522  73.801  7.525   1.00 47.30 ? 460  ARG B CD  1 
ATOM   7213 N  NE  . ARG B 2 460 ? 28.860  73.629  8.059   1.00 51.30 ? 460  ARG B NE  1 
ATOM   7214 C  CZ  . ARG B 2 460 ? 29.977  73.740  7.346   1.00 57.26 ? 460  ARG B CZ  1 
ATOM   7215 N  NH1 . ARG B 2 460 ? 29.925  74.018  6.053   1.00 56.67 ? 460  ARG B NH1 1 
ATOM   7216 N  NH2 . ARG B 2 460 ? 31.151  73.575  7.935   1.00 59.89 ? 460  ARG B NH2 1 
ATOM   7217 N  N   . LYS B 2 461 ? 23.789  76.774  7.806   1.00 32.53 ? 461  LYS B N   1 
ATOM   7218 C  CA  . LYS B 2 461 ? 22.635  76.579  6.895   1.00 32.10 ? 461  LYS B CA  1 
ATOM   7219 C  C   . LYS B 2 461 ? 21.947  77.928  6.627   1.00 30.48 ? 461  LYS B C   1 
ATOM   7220 O  O   . LYS B 2 461 ? 21.462  78.119  5.495   1.00 27.42 ? 461  LYS B O   1 
ATOM   7221 C  CB  . LYS B 2 461 ? 21.693  75.533  7.489   1.00 34.33 ? 461  LYS B CB  1 
ATOM   7222 C  CG  . LYS B 2 461 ? 20.541  75.109  6.592   1.00 37.48 ? 461  LYS B CG  1 
ATOM   7223 C  CD  . LYS B 2 461 ? 20.954  74.577  5.248   1.00 39.25 ? 461  LYS B CD  1 
ATOM   7224 C  CE  . LYS B 2 461 ? 19.771  74.030  4.474   1.00 44.28 ? 461  LYS B CE  1 
ATOM   7225 N  NZ  . LYS B 2 461 ? 19.997  74.064  3.007   1.00 47.75 ? 461  LYS B NZ  1 
ATOM   7226 N  N   . SER B 2 462 ? 21.887  78.822  7.621   1.00 28.88 ? 462  SER B N   1 
ATOM   7227 C  CA  . SER B 2 462 ? 21.391  80.216  7.438   1.00 27.99 ? 462  SER B CA  1 
ATOM   7228 C  C   . SER B 2 462 ? 22.157  80.884  6.287   1.00 27.02 ? 462  SER B C   1 
ATOM   7229 O  O   . SER B 2 462 ? 21.517  81.414  5.376   1.00 26.22 ? 462  SER B O   1 
ATOM   7230 C  CB  . SER B 2 462 ? 21.497  81.021  8.707   1.00 27.57 ? 462  SER B CB  1 
ATOM   7231 O  OG  . SER B 2 462 ? 20.499  80.635  9.630   1.00 26.90 ? 462  SER B OG  1 
ATOM   7232 N  N   . PHE B 2 463 ? 23.488  80.813  6.310   1.00 26.50 ? 463  PHE B N   1 
ATOM   7233 C  CA  . PHE B 2 463 ? 24.376  81.458  5.307   1.00 26.11 ? 463  PHE B CA  1 
ATOM   7234 C  C   . PHE B 2 463 ? 24.137  80.839  3.920   1.00 26.47 ? 463  PHE B C   1 
ATOM   7235 O  O   . PHE B 2 463 ? 24.012  81.590  2.944   1.00 25.63 ? 463  PHE B O   1 
ATOM   7236 C  CB  . PHE B 2 463 ? 25.838  81.355  5.752   1.00 26.46 ? 463  PHE B CB  1 
ATOM   7237 C  CG  . PHE B 2 463 ? 26.785  82.368  5.160   1.00 26.80 ? 463  PHE B CG  1 
ATOM   7238 C  CD1 . PHE B 2 463 ? 26.330  83.496  4.483   1.00 26.27 ? 463  PHE B CD1 1 
ATOM   7239 C  CD2 . PHE B 2 463 ? 28.154  82.215  5.330   1.00 27.26 ? 463  PHE B CD2 1 
ATOM   7240 C  CE1 . PHE B 2 463 ? 27.227  84.423  3.974   1.00 26.48 ? 463  PHE B CE1 1 
ATOM   7241 C  CE2 . PHE B 2 463 ? 29.044  83.151  4.824   1.00 26.31 ? 463  PHE B CE2 1 
ATOM   7242 C  CZ  . PHE B 2 463 ? 28.579  84.252  4.151   1.00 25.90 ? 463  PHE B CZ  1 
ATOM   7243 N  N   . ALA B 2 464 ? 24.065  79.507  3.841   1.00 26.85 ? 464  ALA B N   1 
ATOM   7244 C  CA  . ALA B 2 464 ? 23.742  78.751  2.604   1.00 27.67 ? 464  ALA B CA  1 
ATOM   7245 C  C   . ALA B 2 464 ? 22.384  79.210  2.050   1.00 27.02 ? 464  ALA B C   1 
ATOM   7246 O  O   . ALA B 2 464 ? 22.295  79.493  0.843   1.00 26.70 ? 464  ALA B O   1 
ATOM   7247 C  CB  . ALA B 2 464 ? 23.761  77.264  2.877   1.00 27.62 ? 464  ALA B CB  1 
ATOM   7248 N  N   . ILE B 2 465 ? 21.360  79.315  2.894   1.00 27.61 ? 465  ILE B N   1 
ATOM   7249 C  CA  . ILE B 2 465 ? 20.009  79.767  2.447   1.00 27.96 ? 465  ILE B CA  1 
ATOM   7250 C  C   . ILE B 2 465 ? 20.123  81.209  1.920   1.00 29.63 ? 465  ILE B C   1 
ATOM   7251 O  O   . ILE B 2 465 ? 19.574  81.486  0.825   1.00 26.91 ? 465  ILE B O   1 
ATOM   7252 C  CB  . ILE B 2 465 ? 18.959  79.588  3.565   1.00 29.03 ? 465  ILE B CB  1 
ATOM   7253 C  CG1 . ILE B 2 465 ? 18.677  78.100  3.808   1.00 28.00 ? 465  ILE B CG1 1 
ATOM   7254 C  CG2 . ILE B 2 465 ? 17.672  80.348  3.261   1.00 28.60 ? 465  ILE B CG2 1 
ATOM   7255 C  CD1 . ILE B 2 465 ? 17.952  77.826  5.097   1.00 28.75 ? 465  ILE B CD1 1 
ATOM   7256 N  N   . TRP B 2 466 ? 20.855  82.090  2.614   1.00 27.66 ? 466  TRP B N   1 
ATOM   7257 C  CA  . TRP B 2 466 ? 21.041  83.486  2.141   1.00 27.67 ? 466  TRP B CA  1 
ATOM   7258 C  C   . TRP B 2 466 ? 21.707  83.499  0.767   1.00 28.17 ? 466  TRP B C   1 
ATOM   7259 O  O   . TRP B 2 466 ? 21.259  84.216  -0.124  1.00 28.25 ? 466  TRP B O   1 
ATOM   7260 C  CB  . TRP B 2 466 ? 21.854  84.324  3.121   1.00 27.85 ? 466  TRP B CB  1 
ATOM   7261 C  CG  . TRP B 2 466 ? 22.147  85.678  2.564   1.00 26.16 ? 466  TRP B CG  1 
ATOM   7262 C  CD1 . TRP B 2 466 ? 21.311  86.757  2.545   1.00 27.10 ? 466  TRP B CD1 1 
ATOM   7263 C  CD2 . TRP B 2 466 ? 23.343  86.079  1.878   1.00 26.36 ? 466  TRP B CD2 1 
ATOM   7264 N  NE1 . TRP B 2 466 ? 21.928  87.817  1.936   1.00 28.16 ? 466  TRP B NE1 1 
ATOM   7265 C  CE2 . TRP B 2 466 ? 23.175  87.432  1.515   1.00 26.80 ? 466  TRP B CE2 1 
ATOM   7266 C  CE3 . TRP B 2 466 ? 24.551  85.442  1.574   1.00 26.46 ? 466  TRP B CE3 1 
ATOM   7267 C  CZ2 . TRP B 2 466 ? 24.175  88.158  0.871   1.00 27.08 ? 466  TRP B CZ2 1 
ATOM   7268 C  CZ3 . TRP B 2 466 ? 25.531  86.157  0.931   1.00 26.56 ? 466  TRP B CZ3 1 
ATOM   7269 C  CH2 . TRP B 2 466 ? 25.343  87.494  0.579   1.00 27.05 ? 466  TRP B CH2 1 
HETATM 7270 N  N   . MLZ B 2 467 ? 22.799  82.738  0.626   1.00 27.91 ? 467  MLZ B N   1 
HETATM 7271 C  CA  . MLZ B 2 467 ? 23.526  82.659  -0.632  1.00 29.95 ? 467  MLZ B CA  1 
HETATM 7272 C  CB  . MLZ B 2 467 ? 24.684  81.663  -0.557  1.00 29.97 ? 467  MLZ B CB  1 
HETATM 7273 C  CG  . MLZ B 2 467 ? 25.969  82.219  0.031   1.00 30.77 ? 467  MLZ B CG  1 
HETATM 7274 C  CD  . MLZ B 2 467 ? 27.054  81.184  0.204   1.00 30.87 ? 467  MLZ B CD  1 
HETATM 7275 C  CE  . MLZ B 2 467 ? 28.157  81.694  1.112   1.00 32.22 ? 467  MLZ B CE  1 
HETATM 7276 N  NZ  . MLZ B 2 467 ? 29.254  80.737  1.261   1.00 34.94 ? 467  MLZ B NZ  1 
HETATM 7277 C  CM  . MLZ B 2 467 ? 30.387  81.214  2.065   1.00 35.28 ? 467  MLZ B CM  1 
HETATM 7278 C  C   . MLZ B 2 467 ? 22.571  82.281  -1.759  1.00 29.98 ? 467  MLZ B C   1 
HETATM 7279 O  O   . MLZ B 2 467 ? 22.657  82.850  -2.838  1.00 29.82 ? 467  MLZ B O   1 
ATOM   7280 N  N   . GLU B 2 468 ? 21.645  81.352  -1.493  1.00 33.06 ? 468  GLU B N   1 
ATOM   7281 C  CA  . GLU B 2 468 ? 20.691  80.922  -2.507  1.00 35.04 ? 468  GLU B CA  1 
ATOM   7282 C  C   . GLU B 2 468 ? 19.703  82.055  -2.828  1.00 32.72 ? 468  GLU B C   1 
ATOM   7283 O  O   . GLU B 2 468 ? 19.385  82.223  -4.026  1.00 30.51 ? 468  GLU B O   1 
ATOM   7284 C  CB  . GLU B 2 468 ? 19.962  79.652  -2.065  1.00 40.28 ? 468  GLU B CB  1 
ATOM   7285 C  CG  . GLU B 2 468 ? 19.198  78.968  -3.185  1.00 46.56 ? 468  GLU B CG  1 
ATOM   7286 C  CD  . GLU B 2 468 ? 20.021  78.610  -4.417  1.00 52.72 ? 468  GLU B CD  1 
ATOM   7287 O  OE1 . GLU B 2 468 ? 21.188  78.178  -4.256  1.00 57.86 ? 468  GLU B OE1 1 
ATOM   7288 O  OE2 . GLU B 2 468 ? 19.499  78.774  -5.538  1.00 54.70 ? 468  GLU B OE2 1 
ATOM   7289 N  N   . THR B 2 469 ? 19.261  82.834  -1.830  1.00 30.96 ? 469  THR B N   1 
ATOM   7290 C  CA  . THR B 2 469 ? 18.303  83.961  -2.041  1.00 30.74 ? 469  THR B CA  1 
ATOM   7291 C  C   . THR B 2 469 ? 18.914  85.067  -2.918  1.00 29.15 ? 469  THR B C   1 
ATOM   7292 O  O   . THR B 2 469 ? 18.129  85.861  -3.458  1.00 29.64 ? 469  THR B O   1 
ATOM   7293 C  CB  . THR B 2 469 ? 17.818  84.587  -0.729  1.00 31.56 ? 469  THR B CB  1 
ATOM   7294 O  OG1 . THR B 2 469 ? 18.926  85.209  -0.068  1.00 33.73 ? 469  THR B OG1 1 
ATOM   7295 C  CG2 . THR B 2 469 ? 17.137  83.579  0.172   1.00 31.66 ? 469  THR B CG2 1 
ATOM   7296 N  N   . VAL B 2 470 ? 20.242  85.168  -3.023  1.00 28.29 ? 470  VAL B N   1 
ATOM   7297 C  CA  . VAL B 2 470 ? 20.909  86.280  -3.773  1.00 28.43 ? 470  VAL B CA  1 
ATOM   7298 C  C   . VAL B 2 470 ? 21.741  85.718  -4.925  1.00 28.66 ? 470  VAL B C   1 
ATOM   7299 O  O   . VAL B 2 470 ? 22.503  86.509  -5.531  1.00 27.97 ? 470  VAL B O   1 
ATOM   7300 C  CB  . VAL B 2 470 ? 21.769  87.168  -2.857  1.00 27.54 ? 470  VAL B CB  1 
ATOM   7301 C  CG1 . VAL B 2 470 ? 20.933  87.794  -1.758  1.00 29.82 ? 470  VAL B CG1 1 
ATOM   7302 C  CG2 . VAL B 2 470 ? 22.965  86.430  -2.281  1.00 27.23 ? 470  VAL B CG2 1 
ATOM   7303 N  N   . ARG B 2 471 ? 21.598  84.426  -5.235  1.00 29.04 ? 471  ARG B N   1 
ATOM   7304 C  CA  . ARG B 2 471 ? 22.279  83.800  -6.409  1.00 31.36 ? 471  ARG B CA  1 
ATOM   7305 C  C   . ARG B 2 471 ? 21.945  84.639  -7.655  1.00 28.15 ? 471  ARG B C   1 
ATOM   7306 O  O   . ARG B 2 471 ? 20.786  85.014  -7.793  1.00 26.79 ? 471  ARG B O   1 
ATOM   7307 C  CB  . ARG B 2 471 ? 21.876  82.326  -6.573  1.00 34.30 ? 471  ARG B CB  1 
ATOM   7308 C  CG  . ARG B 2 471 ? 22.960  81.458  -7.199  1.00 37.56 ? 471  ARG B CG  1 
ATOM   7309 C  CD  . ARG B 2 471 ? 22.614  79.978  -7.283  1.00 41.64 ? 471  ARG B CD  1 
ATOM   7310 N  NE  . ARG B 2 471 ? 21.280  79.768  -7.839  1.00 47.55 ? 471  ARG B NE  1 
ATOM   7311 C  CZ  . ARG B 2 471 ? 20.968  79.802  -9.136  1.00 48.13 ? 471  ARG B CZ  1 
ATOM   7312 N  NH1 . ARG B 2 471 ? 21.894  80.020  -10.054 1.00 48.86 ? 471  ARG B NH1 1 
ATOM   7313 N  NH2 . ARG B 2 471 ? 19.717  79.616  -9.512  1.00 50.63 ? 471  ARG B NH2 1 
ATOM   7314 N  N   . LEU B 2 472 ? 22.947  84.975  -8.475  1.00 28.66 ? 472  LEU B N   1 
ATOM   7315 C  CA  . LEU B 2 472 ? 22.824  85.764  -9.740  1.00 29.62 ? 472  LEU B CA  1 
ATOM   7316 C  C   . LEU B 2 472 ? 22.384  87.217  -9.486  1.00 29.46 ? 472  LEU B C   1 
ATOM   7317 O  O   . LEU B 2 472 ? 21.961  87.879  -10.463 1.00 29.40 ? 472  LEU B O   1 
ATOM   7318 C  CB  . LEU B 2 472 ? 21.820  85.077  -10.673 1.00 30.45 ? 472  LEU B CB  1 
ATOM   7319 C  CG  . LEU B 2 472 ? 22.059  83.593  -10.942 1.00 30.97 ? 472  LEU B CG  1 
ATOM   7320 C  CD1 . LEU B 2 472 ? 21.052  83.077  -11.965 1.00 31.06 ? 472  LEU B CD1 1 
ATOM   7321 C  CD2 . LEU B 2 472 ? 23.485  83.338  -11.414 1.00 30.36 ? 472  LEU B CD2 1 
ATOM   7322 N  N   . GLN B 2 473 ? 22.477  87.708  -8.249  1.00 28.84 ? 473  GLN B N   1 
ATOM   7323 C  CA  . GLN B 2 473 ? 22.072  89.092  -7.884  1.00 29.87 ? 473  GLN B CA  1 
ATOM   7324 C  C   . GLN B 2 473 ? 23.289  89.872  -7.372  1.00 29.02 ? 473  GLN B C   1 
ATOM   7325 O  O   . GLN B 2 473 ? 24.201  89.261  -6.785  1.00 26.41 ? 473  GLN B O   1 
ATOM   7326 C  CB  . GLN B 2 473 ? 20.978  89.106  -6.814  1.00 31.66 ? 473  GLN B CB  1 
ATOM   7327 C  CG  . GLN B 2 473 ? 19.660  88.485  -7.251  1.00 33.08 ? 473  GLN B CG  1 
ATOM   7328 C  CD  . GLN B 2 473 ? 18.588  88.683  -6.208  1.00 35.89 ? 473  GLN B CD  1 
ATOM   7329 O  OE1 . GLN B 2 473 ? 18.770  89.407  -5.232  1.00 42.88 ? 473  GLN B OE1 1 
ATOM   7330 N  NE2 . GLN B 2 473 ? 17.459  88.024  -6.395  1.00 38.19 ? 473  GLN B NE2 1 
ATOM   7331 N  N   . ALA B 2 474 ? 23.274  91.190  -7.573  1.00 29.02 ? 474  ALA B N   1 
ATOM   7332 C  CA  . ALA B 2 474 ? 24.299  92.133  -7.077  1.00 27.86 ? 474  ALA B CA  1 
ATOM   7333 C  C   . ALA B 2 474 ? 23.742  92.904  -5.877  1.00 28.97 ? 474  ALA B C   1 
ATOM   7334 O  O   . ALA B 2 474 ? 22.539  92.752  -5.558  1.00 27.38 ? 474  ALA B O   1 
ATOM   7335 C  CB  . ALA B 2 474 ? 24.716  93.058  -8.189  1.00 28.67 ? 474  ALA B CB  1 
ATOM   7336 N  N   . GLN B 2 475 ? 24.608  93.682  -5.222  1.00 29.80 ? 475  GLN B N   1 
ATOM   7337 C  CA  . GLN B 2 475 ? 24.224  94.715  -4.232  1.00 31.36 ? 475  GLN B CA  1 
ATOM   7338 C  C   . GLN B 2 475 ? 23.227  95.653  -4.907  1.00 30.76 ? 475  GLN B C   1 
ATOM   7339 O  O   . GLN B 2 475 ? 23.507  96.163  -5.988  1.00 29.37 ? 475  GLN B O   1 
ATOM   7340 C  CB  . GLN B 2 475 ? 25.479  95.453  -3.764  1.00 34.75 ? 475  GLN B CB  1 
ATOM   7341 C  CG  . GLN B 2 475 ? 25.207  96.553  -2.753  1.00 37.98 ? 475  GLN B CG  1 
ATOM   7342 C  CD  . GLN B 2 475 ? 24.861  96.000  -1.392  1.00 40.31 ? 475  GLN B CD  1 
ATOM   7343 O  OE1 . GLN B 2 475 ? 25.299  94.918  -1.013  1.00 42.16 ? 475  GLN B OE1 1 
ATOM   7344 N  NE2 . GLN B 2 475 ? 24.066  96.750  -0.647  1.00 42.76 ? 475  GLN B NE2 1 
ATOM   7345 N  N   . PRO B 2 476 ? 22.029  95.897  -4.327  1.00 29.87 ? 476  PRO B N   1 
ATOM   7346 C  CA  . PRO B 2 476 ? 21.090  96.846  -4.924  1.00 30.81 ? 476  PRO B CA  1 
ATOM   7347 C  C   . PRO B 2 476 ? 21.680  98.262  -5.048  1.00 30.23 ? 476  PRO B C   1 
ATOM   7348 O  O   . PRO B 2 476 ? 22.485  98.675  -4.224  1.00 28.99 ? 476  PRO B O   1 
ATOM   7349 C  CB  . PRO B 2 476 ? 19.880  96.814  -3.975  1.00 31.28 ? 476  PRO B CB  1 
ATOM   7350 C  CG  . PRO B 2 476 ? 19.998  95.470  -3.274  1.00 31.51 ? 476  PRO B CG  1 
ATOM   7351 C  CD  . PRO B 2 476 ? 21.490  95.258  -3.112  1.00 30.13 ? 476  PRO B CD  1 
ATOM   7352 N  N   . TRP B 2 477 ? 21.275  98.958  -6.106  1.00 29.08 ? 477  TRP B N   1 
ATOM   7353 C  CA  . TRP B 2 477 ? 21.589  100.388 -6.346  1.00 30.35 ? 477  TRP B CA  1 
ATOM   7354 C  C   . TRP B 2 477 ? 20.816  101.223 -5.323  1.00 30.63 ? 477  TRP B C   1 
ATOM   7355 O  O   . TRP B 2 477 ? 19.583  101.163 -5.335  1.00 33.91 ? 477  TRP B O   1 
ATOM   7356 C  CB  . TRP B 2 477 ? 21.247  100.777 -7.788  1.00 28.10 ? 477  TRP B CB  1 
ATOM   7357 C  CG  . TRP B 2 477 ? 21.920  99.899  -8.793  1.00 28.00 ? 477  TRP B CG  1 
ATOM   7358 C  CD1 . TRP B 2 477 ? 21.392  98.811  -9.425  1.00 26.71 ? 477  TRP B CD1 1 
ATOM   7359 C  CD2 . TRP B 2 477 ? 23.284  100.000 -9.235  1.00 26.71 ? 477  TRP B CD2 1 
ATOM   7360 N  NE1 . TRP B 2 477 ? 22.327  98.248  -10.251 1.00 27.77 ? 477  TRP B NE1 1 
ATOM   7361 C  CE2 . TRP B 2 477 ? 23.499  98.945  -10.145 1.00 26.61 ? 477  TRP B CE2 1 
ATOM   7362 C  CE3 . TRP B 2 477 ? 24.338  100.872 -8.947  1.00 26.94 ? 477  TRP B CE3 1 
ATOM   7363 C  CZ2 . TRP B 2 477 ? 24.721  98.750  -10.783 1.00 27.56 ? 477  TRP B CZ2 1 
ATOM   7364 C  CZ3 . TRP B 2 477 ? 25.550  100.675 -9.572  1.00 26.90 ? 477  TRP B CZ3 1 
ATOM   7365 C  CH2 . TRP B 2 477 ? 25.735  99.633  -10.480 1.00 27.09 ? 477  TRP B CH2 1 
ATOM   7366 N  N   . SER B 2 478 ? 21.517  101.934 -4.443  1.00 32.10 ? 478  SER B N   1 
ATOM   7367 C  CA  . SER B 2 478 ? 20.882  102.732 -3.362  1.00 32.26 ? 478  SER B CA  1 
ATOM   7368 C  C   . SER B 2 478 ? 20.179  103.957 -3.958  1.00 34.28 ? 478  SER B C   1 
ATOM   7369 O  O   . SER B 2 478 ? 20.453  104.309 -5.130  1.00 31.45 ? 478  SER B O   1 
ATOM   7370 C  CB  . SER B 2 478 ? 21.885  103.138 -2.330  1.00 32.63 ? 478  SER B CB  1 
ATOM   7371 O  OG  . SER B 2 478 ? 22.715  104.177 -2.821  1.00 32.01 ? 478  SER B OG  1 
ATOM   7372 N  N   . GLU B 2 479 ? 19.300  104.577 -3.167  1.00 34.70 ? 479  GLU B N   1 
ATOM   7373 C  CA  . GLU B 2 479 ? 18.668  105.884 -3.485  1.00 36.07 ? 479  GLU B CA  1 
ATOM   7374 C  C   . GLU B 2 479 ? 19.775  106.903 -3.805  1.00 32.54 ? 479  GLU B C   1 
ATOM   7375 O  O   . GLU B 2 479 ? 19.581  107.696 -4.726  1.00 31.16 ? 479  GLU B O   1 
ATOM   7376 C  CB  . GLU B 2 479 ? 17.734  106.309 -2.349  1.00 37.94 ? 479  GLU B CB  1 
ATOM   7377 C  CG  . GLU B 2 479 ? 18.417  106.433 -0.998  1.00 41.07 ? 479  GLU B CG  1 
ATOM   7378 C  CD  . GLU B 2 479 ? 19.153  107.739 -0.765  1.00 44.17 ? 479  GLU B CD  1 
ATOM   7379 O  OE1 . GLU B 2 479 ? 18.927  108.695 -1.534  1.00 47.30 ? 479  GLU B OE1 1 
ATOM   7380 O  OE2 . GLU B 2 479 ? 19.965  107.798 0.177   1.00 49.95 ? 479  GLU B OE2 1 
ATOM   7381 N  N   . ALA B 2 480 ? 20.898  106.869 -3.084  1.00 30.15 ? 480  ALA B N   1 
ATOM   7382 C  CA  . ALA B 2 480 ? 22.061  107.761 -3.308  1.00 30.45 ? 480  ALA B CA  1 
ATOM   7383 C  C   . ALA B 2 480 ? 22.670  107.496 -4.693  1.00 30.08 ? 480  ALA B C   1 
ATOM   7384 O  O   . ALA B 2 480 ? 22.931  108.476 -5.417  1.00 27.60 ? 480  ALA B O   1 
ATOM   7385 C  CB  . ALA B 2 480 ? 23.083  107.564 -2.221  1.00 31.62 ? 480  ALA B CB  1 
ATOM   7386 N  N   . ASP B 2 481 ? 22.921  106.224 -5.031  1.00 28.18 ? 481  ASP B N   1 
ATOM   7387 C  CA  . ASP B 2 481 ? 23.482  105.820 -6.350  1.00 28.56 ? 481  ASP B CA  1 
ATOM   7388 C  C   . ASP B 2 481 ? 22.579  106.368 -7.464  1.00 27.76 ? 481  ASP B C   1 
ATOM   7389 O  O   . ASP B 2 481 ? 23.115  106.895 -8.438  1.00 27.46 ? 481  ASP B O   1 
ATOM   7390 C  CB  . ASP B 2 481 ? 23.583  104.304 -6.517  1.00 27.56 ? 481  ASP B CB  1 
ATOM   7391 C  CG  . ASP B 2 481 ? 24.503  103.596 -5.543  1.00 28.70 ? 481  ASP B CG  1 
ATOM   7392 O  OD1 . ASP B 2 481 ? 25.508  104.209 -5.126  1.00 29.45 ? 481  ASP B OD1 1 
ATOM   7393 O  OD2 . ASP B 2 481 ? 24.208  102.417 -5.229  1.00 27.25 ? 481  ASP B OD2 1 
ATOM   7394 N  N   . ARG B 2 482 ? 21.259  106.244 -7.299  1.00 30.00 ? 482  ARG B N   1 
ATOM   7395 C  CA  . ARG B 2 482 ? 20.239  106.646 -8.311  1.00 31.81 ? 482  ARG B CA  1 
ATOM   7396 C  C   . ARG B 2 482 ? 20.203  108.176 -8.437  1.00 32.05 ? 482  ARG B C   1 
ATOM   7397 O  O   . ARG B 2 482 ? 20.088  108.661 -9.578  1.00 31.72 ? 482  ARG B O   1 
ATOM   7398 C  CB  . ARG B 2 482 ? 18.875  106.058 -7.951  1.00 33.93 ? 482  ARG B CB  1 
ATOM   7399 C  CG  . ARG B 2 482 ? 18.772  104.572 -8.254  1.00 35.56 ? 482  ARG B CG  1 
ATOM   7400 C  CD  . ARG B 2 482 ? 17.593  103.918 -7.564  1.00 37.58 ? 482  ARG B CD  1 
ATOM   7401 N  NE  . ARG B 2 482 ? 17.586  102.471 -7.750  1.00 39.52 ? 482  ARG B NE  1 
ATOM   7402 C  CZ  . ARG B 2 482 ? 17.143  101.839 -8.832  1.00 40.81 ? 482  ARG B CZ  1 
ATOM   7403 N  NH1 . ARG B 2 482 ? 16.674  102.519 -9.867  1.00 41.32 ? 482  ARG B NH1 1 
ATOM   7404 N  NH2 . ARG B 2 482 ? 17.189  100.519 -8.884  1.00 44.28 ? 482  ARG B NH2 1 
ATOM   7405 N  N   . GLU B 2 483 ? 20.352  108.903 -7.325  1.00 31.63 ? 483  GLU B N   1 
ATOM   7406 C  CA  . GLU B 2 483 ? 20.434  110.390 -7.315  1.00 31.03 ? 483  GLU B CA  1 
ATOM   7407 C  C   . GLU B 2 483 ? 21.703  110.850 -8.047  1.00 29.74 ? 483  GLU B C   1 
ATOM   7408 O  O   . GLU B 2 483 ? 21.631  111.847 -8.794  1.00 28.40 ? 483  GLU B O   1 
ATOM   7409 C  CB  . GLU B 2 483 ? 20.427  110.957 -5.894  1.00 32.22 ? 483  GLU B CB  1 
ATOM   7410 C  CG  . GLU B 2 483 ? 20.620  112.466 -5.878  1.00 35.04 ? 483  GLU B CG  1 
ATOM   7411 C  CD  . GLU B 2 483 ? 20.332  113.196 -4.578  1.00 38.34 ? 483  GLU B CD  1 
ATOM   7412 O  OE1 . GLU B 2 483 ? 20.832  114.342 -4.435  1.00 40.83 ? 483  GLU B OE1 1 
ATOM   7413 O  OE2 . GLU B 2 483 ? 19.601  112.637 -3.723  1.00 38.28 ? 483  GLU B OE2 1 
ATOM   7414 N  N   . ILE B 2 484 ? 22.826  110.166 -7.835  1.00 27.91 ? 484  ILE B N   1 
ATOM   7415 C  CA  . ILE B 2 484 ? 24.110  110.491 -8.524  1.00 28.81 ? 484  ILE B CA  1 
ATOM   7416 C  C   . ILE B 2 484 ? 23.965  110.185 -10.023 1.00 27.66 ? 484  ILE B C   1 
ATOM   7417 O  O   . ILE B 2 484 ? 24.421  111.010 -10.824 1.00 28.69 ? 484  ILE B O   1 
ATOM   7418 C  CB  . ILE B 2 484 ? 25.296  109.769 -7.858  1.00 28.04 ? 484  ILE B CB  1 
ATOM   7419 C  CG1 . ILE B 2 484 ? 25.569  110.368 -6.476  1.00 27.73 ? 484  ILE B CG1 1 
ATOM   7420 C  CG2 . ILE B 2 484 ? 26.536  109.803 -8.742  1.00 27.91 ? 484  ILE B CG2 1 
ATOM   7421 C  CD1 . ILE B 2 484 ? 26.541  109.570 -5.643  1.00 28.19 ? 484  ILE B CD1 1 
ATOM   7422 N  N   . ALA B 2 485 ? 23.354  109.056 -10.383 1.00 27.81 ? 485  ALA B N   1 
ATOM   7423 C  CA  . ALA B 2 485 ? 23.122  108.649 -11.792 1.00 28.43 ? 485  ALA B CA  1 
ATOM   7424 C  C   . ALA B 2 485 ? 22.301  109.729 -12.507 1.00 29.61 ? 485  ALA B C   1 
ATOM   7425 O  O   . ALA B 2 485 ? 22.622  110.048 -13.671 1.00 28.47 ? 485  ALA B O   1 
ATOM   7426 C  CB  . ALA B 2 485 ? 22.423  107.318 -11.862 1.00 26.59 ? 485  ALA B CB  1 
ATOM   7427 N  N   . GLU B 2 486 ? 21.272  110.247 -11.830 1.00 30.33 ? 486  GLU B N   1 
ATOM   7428 C  CA  . GLU B 2 486 ? 20.342  111.266 -12.374 1.00 31.55 ? 486  GLU B CA  1 
ATOM   7429 C  C   . GLU B 2 486 ? 21.108  112.572 -12.608 1.00 29.89 ? 486  GLU B C   1 
ATOM   7430 O  O   . GLU B 2 486 ? 20.888  113.186 -13.659 1.00 29.76 ? 486  GLU B O   1 
ATOM   7431 C  CB  . GLU B 2 486 ? 19.139  111.442 -11.444 1.00 35.04 ? 486  GLU B CB  1 
ATOM   7432 C  CG  . GLU B 2 486 ? 18.207  112.568 -11.864 1.00 38.39 ? 486  GLU B CG  1 
ATOM   7433 C  CD  . GLU B 2 486 ? 17.599  112.443 -13.251 1.00 39.55 ? 486  GLU B CD  1 
ATOM   7434 O  OE1 . GLU B 2 486 ? 17.649  111.342 -13.833 1.00 42.63 ? 486  GLU B OE1 1 
ATOM   7435 O  OE2 . GLU B 2 486 ? 17.063  113.451 -13.745 1.00 44.15 ? 486  GLU B OE2 1 
ATOM   7436 N  N   . ALA B 2 487 ? 21.992  112.967 -11.685 1.00 28.57 ? 487  ALA B N   1 
ATOM   7437 C  CA  . ALA B 2 487 ? 22.889  114.135 -11.847 1.00 28.60 ? 487  ALA B CA  1 
ATOM   7438 C  C   . ALA B 2 487 ? 23.810  113.921 -13.062 1.00 29.39 ? 487  ALA B C   1 
ATOM   7439 O  O   . ALA B 2 487 ? 24.028  114.881 -13.829 1.00 26.04 ? 487  ALA B O   1 
ATOM   7440 C  CB  . ALA B 2 487 ? 23.678  114.371 -10.587 1.00 29.34 ? 487  ALA B CB  1 
ATOM   7441 N  N   . ALA B 2 488 ? 24.357  112.712 -13.220 1.00 27.68 ? 488  ALA B N   1 
ATOM   7442 C  CA  . ALA B 2 488 ? 25.204  112.339 -14.375 1.00 27.29 ? 488  ALA B CA  1 
ATOM   7443 C  C   . ALA B 2 488 ? 24.380  112.464 -15.666 1.00 26.38 ? 488  ALA B C   1 
ATOM   7444 O  O   . ALA B 2 488 ? 24.879  113.090 -16.628 1.00 27.49 ? 488  ALA B O   1 
ATOM   7445 C  CB  . ALA B 2 488 ? 25.788  110.955 -14.183 1.00 26.70 ? 488  ALA B CB  1 
ATOM   7446 N  N   . ARG B 2 489 ? 23.166  111.909 -15.693 1.00 26.11 ? 489  ARG B N   1 
ATOM   7447 C  CA  . ARG B 2 489 ? 22.285  111.949 -16.899 1.00 27.42 ? 489  ARG B CA  1 
ATOM   7448 C  C   . ARG B 2 489 ? 22.095  113.410 -17.328 1.00 29.42 ? 489  ARG B C   1 
ATOM   7449 O  O   . ARG B 2 489 ? 22.315  113.740 -18.505 1.00 28.18 ? 489  ARG B O   1 
ATOM   7450 C  CB  . ARG B 2 489 ? 20.920  111.312 -16.618 1.00 27.18 ? 489  ARG B CB  1 
ATOM   7451 C  CG  . ARG B 2 489 ? 20.051  111.131 -17.859 1.00 26.77 ? 489  ARG B CG  1 
ATOM   7452 C  CD  . ARG B 2 489 ? 18.644  110.649 -17.553 1.00 27.72 ? 489  ARG B CD  1 
ATOM   7453 N  NE  . ARG B 2 489 ? 17.880  111.625 -16.786 1.00 28.84 ? 489  ARG B NE  1 
ATOM   7454 C  CZ  . ARG B 2 489 ? 17.324  112.732 -17.282 1.00 31.20 ? 489  ARG B CZ  1 
ATOM   7455 N  NH1 . ARG B 2 489 ? 17.451  113.043 -18.561 1.00 31.43 ? 489  ARG B NH1 1 
ATOM   7456 N  NH2 . ARG B 2 489 ? 16.661  113.549 -16.486 1.00 32.20 ? 489  ARG B NH2 1 
ATOM   7457 N  N   . ILE B 2 490 ? 21.722  114.241 -16.361 1.00 29.22 ? 490  ILE B N   1 
ATOM   7458 C  CA  A ILE B 2 490 ? 21.386  115.686 -16.527 0.50 30.99 ? 490  ILE B CA  1 
ATOM   7459 C  CA  B ILE B 2 490 ? 21.374  115.677 -16.570 0.50 30.62 ? 490  ILE B CA  1 
ATOM   7460 C  C   . ILE B 2 490 ? 22.623  116.472 -16.977 1.00 29.75 ? 490  ILE B C   1 
ATOM   7461 O  O   . ILE B 2 490 ? 22.494  117.330 -17.865 1.00 28.80 ? 490  ILE B O   1 
ATOM   7462 C  CB  A ILE B 2 490 ? 20.829  116.220 -15.195 0.50 33.28 ? 490  ILE B CB  1 
ATOM   7463 C  CB  B ILE B 2 490 ? 20.703  116.237 -15.302 0.50 32.36 ? 490  ILE B CB  1 
ATOM   7464 C  CG1 A ILE B 2 490 ? 19.447  115.641 -14.886 0.50 34.69 ? 490  ILE B CG1 1 
ATOM   7465 C  CG1 B ILE B 2 490 ? 19.255  115.757 -15.169 0.50 33.34 ? 490  ILE B CG1 1 
ATOM   7466 C  CG2 A ILE B 2 490 ? 20.824  117.732 -15.181 0.50 34.96 ? 490  ILE B CG2 1 
ATOM   7467 C  CG2 B ILE B 2 490 ? 20.795  117.745 -15.272 0.50 33.89 ? 490  ILE B CG2 1 
ATOM   7468 C  CD1 A ILE B 2 490 ? 18.348  116.184 -15.752 0.50 35.28 ? 490  ILE B CD1 1 
ATOM   7469 C  CD1 B ILE B 2 490 ? 18.556  116.258 -13.919 0.50 34.21 ? 490  ILE B CD1 1 
ATOM   7470 N  N   . ALA B 2 491 ? 23.770  116.209 -16.347 1.00 29.17 ? 491  ALA B N   1 
ATOM   7471 C  CA  . ALA B 2 491 ? 25.060  116.841 -16.704 1.00 28.26 ? 491  ALA B CA  1 
ATOM   7472 C  C   . ALA B 2 491 ? 25.390  116.526 -18.174 1.00 28.51 ? 491  ALA B C   1 
ATOM   7473 O  O   . ALA B 2 491 ? 25.888  117.423 -18.882 1.00 26.95 ? 491  ALA B O   1 
ATOM   7474 C  CB  . ALA B 2 491 ? 26.148  116.378 -15.765 1.00 28.20 ? 491  ALA B CB  1 
ATOM   7475 N  N   . LEU B 2 492 ? 25.098  115.303 -18.624 1.00 28.04 ? 492  LEU B N   1 
ATOM   7476 C  CA  . LEU B 2 492 ? 25.448  114.817 -19.985 1.00 29.27 ? 492  LEU B CA  1 
ATOM   7477 C  C   . LEU B 2 492 ? 24.454  115.390 -21.007 1.00 29.41 ? 492  LEU B C   1 
ATOM   7478 O  O   . LEU B 2 492 ? 24.893  115.709 -22.121 1.00 29.02 ? 492  LEU B O   1 
ATOM   7479 C  CB  . LEU B 2 492 ? 25.469  113.286 -19.998 1.00 30.13 ? 492  LEU B CB  1 
ATOM   7480 C  CG  . LEU B 2 492 ? 26.714  112.654 -19.372 1.00 31.55 ? 492  LEU B CG  1 
ATOM   7481 C  CD1 . LEU B 2 492 ? 26.478  111.192 -19.027 1.00 31.82 ? 492  LEU B CD1 1 
ATOM   7482 C  CD2 . LEU B 2 492 ? 27.916  112.786 -20.287 1.00 32.61 ? 492  LEU B CD2 1 
ATOM   7483 N  N   . VAL B 2 493 ? 23.173  115.518 -20.646 1.00 28.82 ? 493  VAL B N   1 
ATOM   7484 C  CA  . VAL B 2 493 ? 22.172  116.277 -21.459 1.00 30.33 ? 493  VAL B CA  1 
ATOM   7485 C  C   . VAL B 2 493 ? 22.719  117.689 -21.686 1.00 31.25 ? 493  VAL B C   1 
ATOM   7486 O  O   . VAL B 2 493 ? 22.673  118.176 -22.838 1.00 34.45 ? 493  VAL B O   1 
ATOM   7487 C  CB  . VAL B 2 493 ? 20.788  116.315 -20.787 1.00 29.64 ? 493  VAL B CB  1 
ATOM   7488 C  CG1 . VAL B 2 493 ? 19.927  117.447 -21.328 1.00 29.31 ? 493  VAL B CG1 1 
ATOM   7489 C  CG2 . VAL B 2 493 ? 20.073  114.984 -20.931 1.00 29.31 ? 493  VAL B CG2 1 
ATOM   7490 N  N   . GLU B 2 494 ? 23.241  118.306 -20.625 1.00 31.09 ? 494  GLU B N   1 
ATOM   7491 C  CA  . GLU B 2 494 ? 23.739  119.700 -20.649 1.00 32.27 ? 494  GLU B CA  1 
ATOM   7492 C  C   . GLU B 2 494 ? 24.978  119.797 -21.556 1.00 33.20 ? 494  GLU B C   1 
ATOM   7493 O  O   . GLU B 2 494 ? 25.090  120.801 -22.301 1.00 31.66 ? 494  GLU B O   1 
ATOM   7494 C  CB  . GLU B 2 494 ? 23.998  120.198 -19.232 1.00 33.78 ? 494  GLU B CB  1 
ATOM   7495 C  CG  . GLU B 2 494 ? 24.280  121.679 -19.224 1.00 37.24 ? 494  GLU B CG  1 
ATOM   7496 C  CD  . GLU B 2 494 ? 24.192  122.413 -17.901 1.00 38.24 ? 494  GLU B CD  1 
ATOM   7497 O  OE1 . GLU B 2 494 ? 23.839  121.792 -16.875 1.00 37.36 ? 494  GLU B OE1 1 
ATOM   7498 O  OE2 . GLU B 2 494 ? 24.512  123.615 -17.914 1.00 39.72 ? 494  GLU B OE2 1 
ATOM   7499 N  N   . VAL B 2 495 ? 25.870  118.803 -21.514 1.00 32.24 ? 495  VAL B N   1 
ATOM   7500 C  CA  . VAL B 2 495 ? 27.062  118.734 -22.413 1.00 30.77 ? 495  VAL B CA  1 
ATOM   7501 C  C   . VAL B 2 495 ? 26.581  118.673 -23.867 1.00 28.70 ? 495  VAL B C   1 
ATOM   7502 O  O   . VAL B 2 495 ? 27.148  119.391 -24.693 1.00 29.31 ? 495  VAL B O   1 
ATOM   7503 C  CB  . VAL B 2 495 ? 27.981  117.541 -22.089 1.00 31.31 ? 495  VAL B CB  1 
ATOM   7504 C  CG1 . VAL B 2 495 ? 28.988  117.285 -23.203 1.00 31.76 ? 495  VAL B CG1 1 
ATOM   7505 C  CG2 . VAL B 2 495 ? 28.692  117.725 -20.757 1.00 32.23 ? 495  VAL B CG2 1 
ATOM   7506 N  N   . ALA B 2 496 ? 25.611  117.811 -24.172 1.00 29.78 ? 496  ALA B N   1 
ATOM   7507 C  CA  . ALA B 2 496 ? 25.098  117.613 -25.548 1.00 32.16 ? 496  ALA B CA  1 
ATOM   7508 C  C   . ALA B 2 496 ? 24.461  118.928 -26.034 1.00 34.26 ? 496  ALA B C   1 
ATOM   7509 O  O   . ALA B 2 496 ? 24.787  119.381 -27.156 1.00 32.32 ? 496  ALA B O   1 
ATOM   7510 C  CB  . ALA B 2 496 ? 24.137  116.452 -25.582 1.00 31.30 ? 496  ALA B CB  1 
ATOM   7511 N  N   . PHE B 2 497 ? 23.626  119.553 -25.197 1.00 33.83 ? 497  PHE B N   1 
ATOM   7512 C  CA  . PHE B 2 497 ? 22.856  120.775 -25.550 1.00 34.43 ? 497  PHE B CA  1 
ATOM   7513 C  C   . PHE B 2 497 ? 23.804  121.936 -25.860 1.00 33.41 ? 497  PHE B C   1 
ATOM   7514 O  O   . PHE B 2 497 ? 23.644  122.562 -26.924 1.00 31.42 ? 497  PHE B O   1 
ATOM   7515 C  CB  . PHE B 2 497 ? 21.881  121.192 -24.446 1.00 36.16 ? 497  PHE B CB  1 
ATOM   7516 C  CG  . PHE B 2 497 ? 21.018  122.364 -24.846 1.00 38.33 ? 497  PHE B CG  1 
ATOM   7517 C  CD1 . PHE B 2 497 ? 20.092  122.236 -25.869 1.00 41.62 ? 497  PHE B CD1 1 
ATOM   7518 C  CD2 . PHE B 2 497 ? 21.160  123.601 -24.236 1.00 39.94 ? 497  PHE B CD2 1 
ATOM   7519 C  CE1 . PHE B 2 497 ? 19.310  123.314 -26.258 1.00 43.39 ? 497  PHE B CE1 1 
ATOM   7520 C  CE2 . PHE B 2 497 ? 20.374  124.676 -24.623 1.00 41.65 ? 497  PHE B CE2 1 
ATOM   7521 C  CZ  . PHE B 2 497 ? 19.451  124.530 -25.632 1.00 42.01 ? 497  PHE B CZ  1 
ATOM   7522 N  N   . HIS B 2 498 ? 24.741  122.237 -24.958 1.00 33.51 ? 498  HIS B N   1 
ATOM   7523 C  CA  . HIS B 2 498 ? 25.706  123.353 -25.133 1.00 36.76 ? 498  HIS B CA  1 
ATOM   7524 C  C   . HIS B 2 498 ? 26.573  123.066 -26.363 1.00 37.41 ? 498  HIS B C   1 
ATOM   7525 O  O   . HIS B 2 498 ? 26.891  124.024 -27.090 1.00 35.74 ? 498  HIS B O   1 
ATOM   7526 C  CB  . HIS B 2 498 ? 26.510  123.619 -23.854 1.00 39.80 ? 498  HIS B CB  1 
ATOM   7527 C  CG  . HIS B 2 498 ? 25.646  123.964 -22.689 1.00 42.67 ? 498  HIS B CG  1 
ATOM   7528 N  ND1 . HIS B 2 498 ? 24.469  124.683 -22.828 1.00 44.27 ? 498  HIS B ND1 1 
ATOM   7529 C  CD2 . HIS B 2 498 ? 25.770  123.688 -21.374 1.00 44.68 ? 498  HIS B CD2 1 
ATOM   7530 C  CE1 . HIS B 2 498 ? 23.903  124.825 -21.647 1.00 45.93 ? 498  HIS B CE1 1 
ATOM   7531 N  NE2 . HIS B 2 498 ? 24.682  124.220 -20.737 1.00 46.25 ? 498  HIS B NE2 1 
ATOM   7532 N  N   . HIS B 2 499 ? 26.899  121.797 -26.620 1.00 38.57 ? 499  HIS B N   1 
ATOM   7533 C  CA  . HIS B 2 499 ? 27.637  121.386 -27.843 1.00 41.48 ? 499  HIS B CA  1 
ATOM   7534 C  C   . HIS B 2 499 ? 26.824  121.814 -29.069 1.00 41.73 ? 499  HIS B C   1 
ATOM   7535 O  O   . HIS B 2 499 ? 27.391  122.502 -29.929 1.00 42.91 ? 499  HIS B O   1 
ATOM   7536 C  CB  . HIS B 2 499 ? 27.945  119.882 -27.864 1.00 43.05 ? 499  HIS B CB  1 
ATOM   7537 C  CG  . HIS B 2 499 ? 28.851  119.501 -28.985 1.00 44.63 ? 499  HIS B CG  1 
ATOM   7538 N  ND1 . HIS B 2 499 ? 28.405  118.792 -30.088 1.00 45.76 ? 499  HIS B ND1 1 
ATOM   7539 C  CD2 . HIS B 2 499 ? 30.160  119.761 -29.196 1.00 45.10 ? 499  HIS B CD2 1 
ATOM   7540 C  CE1 . HIS B 2 499 ? 29.407  118.620 -30.926 1.00 47.52 ? 499  HIS B CE1 1 
ATOM   7541 N  NE2 . HIS B 2 499 ? 30.496  119.208 -30.401 1.00 47.98 ? 499  HIS B NE2 1 
ATOM   7542 N  N   . SER B 2 500 ? 25.539  121.449 -29.115 1.00 42.52 ? 500  SER B N   1 
ATOM   7543 C  CA  . SER B 2 500 ? 24.617  121.798 -30.232 1.00 44.40 ? 500  SER B CA  1 
ATOM   7544 C  C   . SER B 2 500 ? 24.492  123.325 -30.358 1.00 44.76 ? 500  SER B C   1 
ATOM   7545 O  O   . SER B 2 500 ? 24.475  123.808 -31.495 1.00 45.83 ? 500  SER B O   1 
ATOM   7546 C  CB  . SER B 2 500 ? 23.275  121.139 -30.075 1.00 45.55 ? 500  SER B CB  1 
ATOM   7547 O  OG  . SER B 2 500 ? 22.514  121.771 -29.060 1.00 49.42 ? 500  SER B OG  1 
ATOM   7548 N  N   . GLU B 2 501 ? 24.425  124.060 -29.241 1.00 46.18 ? 501  GLU B N   1 
ATOM   7549 C  CA  . GLU B 2 501 ? 24.265  125.544 -29.238 1.00 48.50 ? 501  GLU B CA  1 
ATOM   7550 C  C   . GLU B 2 501 ? 25.426  126.190 -29.999 1.00 51.86 ? 501  GLU B C   1 
ATOM   7551 O  O   . GLU B 2 501 ? 25.171  127.117 -30.784 1.00 51.51 ? 501  GLU B O   1 
ATOM   7552 C  CB  . GLU B 2 501 ? 24.247  126.122 -27.821 1.00 48.11 ? 501  GLU B CB  1 
ATOM   7553 C  CG  . GLU B 2 501 ? 22.905  126.019 -27.115 1.00 47.34 ? 501  GLU B CG  1 
ATOM   7554 C  CD  . GLU B 2 501 ? 22.916  126.654 -25.734 1.00 46.98 ? 501  GLU B CD  1 
ATOM   7555 O  OE1 . GLU B 2 501 ? 23.817  126.313 -24.942 1.00 47.71 ? 501  GLU B OE1 1 
ATOM   7556 O  OE2 . GLU B 2 501 ? 22.051  127.516 -25.464 1.00 46.83 ? 501  GLU B OE2 1 
ATOM   7557 N  N   . HIS B 2 502 ? 26.651  125.724 -29.744 1.00 58.19 ? 502  HIS B N   1 
ATOM   7558 C  CA  . HIS B 2 502 ? 27.919  126.347 -30.213 1.00 60.42 ? 502  HIS B CA  1 
ATOM   7559 C  C   . HIS B 2 502 ? 28.427  125.664 -31.494 1.00 62.98 ? 502  HIS B C   1 
ATOM   7560 O  O   . HIS B 2 502 ? 29.302  126.252 -32.155 1.00 69.22 ? 502  HIS B O   1 
ATOM   7561 C  CB  . HIS B 2 502 ? 28.954  126.327 -29.082 1.00 59.71 ? 502  HIS B CB  1 
ATOM   7562 C  CG  . HIS B 2 502 ? 28.568  127.130 -27.884 1.00 61.10 ? 502  HIS B CG  1 
ATOM   7563 N  ND1 . HIS B 2 502 ? 28.452  128.509 -27.919 1.00 63.10 ? 502  HIS B ND1 1 
ATOM   7564 C  CD2 . HIS B 2 502 ? 28.303  126.765 -26.610 1.00 61.66 ? 502  HIS B CD2 1 
ATOM   7565 C  CE1 . HIS B 2 502 ? 28.118  128.954 -26.723 1.00 62.45 ? 502  HIS B CE1 1 
ATOM   7566 N  NE2 . HIS B 2 502 ? 28.023  127.903 -25.900 1.00 62.80 ? 502  HIS B NE2 1 
ATOM   7567 N  N   . HIS B 2 503 ? 27.909  124.475 -31.825 1.00 67.05 ? 503  HIS B N   1 
ATOM   7568 C  CA  . HIS B 2 503 ? 28.251  123.683 -33.042 1.00 67.37 ? 503  HIS B CA  1 
ATOM   7569 C  C   . HIS B 2 503 ? 26.952  123.277 -33.750 1.00 68.20 ? 503  HIS B C   1 
ATOM   7570 O  O   . HIS B 2 503 ? 26.876  123.106 -34.965 1.00 71.78 ? 503  HIS B O   1 
ATOM   7571 C  CB  . HIS B 2 503 ? 29.104  122.446 -32.691 1.00 67.95 ? 503  HIS B CB  1 
ATOM   7572 C  CG  . HIS B 2 503 ? 30.315  122.718 -31.853 1.00 69.05 ? 503  HIS B CG  1 
ATOM   7573 N  ND1 . HIS B 2 503 ? 31.588  122.807 -32.393 1.00 68.41 ? 503  HIS B ND1 1 
ATOM   7574 C  CD2 . HIS B 2 503 ? 30.462  122.893 -30.518 1.00 66.96 ? 503  HIS B CD2 1 
ATOM   7575 C  CE1 . HIS B 2 503 ? 32.459  123.046 -31.430 1.00 68.17 ? 503  HIS B CE1 1 
ATOM   7576 N  NE2 . HIS B 2 503 ? 31.794  123.098 -30.267 1.00 66.13 ? 503  HIS B NE2 1 
HETATM 7577 C  C1  . PEG C 3 .   ? 6.328   136.049 33.157  1.00 53.73 ? 601  PEG A C1  1 
HETATM 7578 O  O1  . PEG C 3 .   ? 6.840   137.346 33.005  1.00 54.37 ? 601  PEG A O1  1 
HETATM 7579 C  C2  . PEG C 3 .   ? 5.950   135.781 34.564  1.00 56.78 ? 601  PEG A C2  1 
HETATM 7580 O  O2  . PEG C 3 .   ? 4.964   134.756 34.626  1.00 57.25 ? 601  PEG A O2  1 
HETATM 7581 C  C3  . PEG C 3 .   ? 5.074   133.967 35.807  1.00 57.53 ? 601  PEG A C3  1 
HETATM 7582 C  C4  . PEG C 3 .   ? 6.039   132.844 35.613  1.00 55.81 ? 601  PEG A C4  1 
HETATM 7583 O  O4  . PEG C 3 .   ? 6.985   132.741 36.664  1.00 57.65 ? 601  PEG A O4  1 
HETATM 7584 C  C1  . MPD D 4 .   ? 3.164   124.490 -15.581 1.00 48.57 ? 602  MPD A C1  1 
HETATM 7585 C  C2  . MPD D 4 .   ? 3.829   124.083 -14.270 1.00 49.20 ? 602  MPD A C2  1 
HETATM 7586 O  O2  . MPD D 4 .   ? 4.038   122.655 -14.304 1.00 52.29 ? 602  MPD A O2  1 
HETATM 7587 C  CM  . MPD D 4 .   ? 2.901   124.327 -13.087 1.00 48.23 ? 602  MPD A CM  1 
HETATM 7588 C  C3  . MPD D 4 .   ? 5.199   124.761 -14.119 1.00 49.81 ? 602  MPD A C3  1 
HETATM 7589 C  C4  . MPD D 4 .   ? 5.779   125.001 -12.727 1.00 51.70 ? 602  MPD A C4  1 
HETATM 7590 O  O4  . MPD D 4 .   ? 5.285   124.081 -11.752 1.00 51.00 ? 602  MPD A O4  1 
HETATM 7591 C  C5  . MPD D 4 .   ? 7.283   124.972 -12.691 1.00 50.49 ? 602  MPD A C5  1 
HETATM 7592 C  C1A . EL5 E 5 .   ? 24.729  149.170 20.637  1.00 26.89 ? 603  EL5 A C1A 1 
HETATM 7593 C  C1B . EL5 E 5 .   ? 26.539  145.802 22.814  1.00 26.63 ? 603  EL5 A C1B 1 
HETATM 7594 O  O1B . EL5 E 5 .   ? 27.896  141.846 27.571  1.00 26.70 ? 603  EL5 A O1B 1 
HETATM 7595 C  C1C . EL5 E 5 .   ? 22.826  143.642 22.671  1.00 24.00 ? 603  EL5 A C1C 1 
HETATM 7596 O  O1C . EL5 E 5 .   ? 19.515  141.119 25.633  1.00 26.85 ? 603  EL5 A O1C 1 
HETATM 7597 C  C1D . EL5 E 5 .   ? 19.064  145.816 20.695  1.00 26.31 ? 603  EL5 A C1D 1 
HETATM 7598 C  C2A . EL5 E 5 .   ? 25.956  149.639 20.202  1.00 28.80 ? 603  EL5 A C2A 1 
HETATM 7599 C  C2B . EL5 E 5 .   ? 27.240  144.899 23.608  1.00 25.80 ? 603  EL5 A C2B 1 
HETATM 7600 O  O2B . EL5 E 5 .   ? 25.873  140.972 27.641  1.00 25.88 ? 603  EL5 A O2B 1 
HETATM 7601 C  C2C . EL5 E 5 .   ? 21.803  142.748 22.364  1.00 24.16 ? 603  EL5 A C2C 1 
HETATM 7602 O  O2C . EL5 E 5 .   ? 19.057  140.985 23.495  1.00 25.97 ? 603  EL5 A O2C 1 
HETATM 7603 C  C2D . EL5 E 5 .   ? 17.970  145.487 21.494  1.00 26.34 ? 603  EL5 A C2D 1 
HETATM 7604 C  C3A . EL5 E 5 .   ? 27.030  148.957 20.747  1.00 29.59 ? 603  EL5 A C3A 1 
HETATM 7605 C  C3B . EL5 E 5 .   ? 26.365  143.870 23.940  1.00 25.54 ? 603  EL5 A C3B 1 
HETATM 7606 C  C3C . EL5 E 5 .   ? 20.883  143.438 21.608  1.00 24.40 ? 603  EL5 A C3C 1 
HETATM 7607 C  C3D . EL5 E 5 .   ? 16.827  145.973 20.851  1.00 26.98 ? 603  EL5 A C3D 1 
HETATM 7608 C  C4A . EL5 E 5 .   ? 26.414  147.937 21.482  1.00 27.10 ? 603  EL5 A C4A 1 
HETATM 7609 C  C4B . EL5 E 5 .   ? 25.182  144.139 23.266  1.00 24.83 ? 603  EL5 A C4B 1 
HETATM 7610 C  C4C . EL5 E 5 .   ? 21.247  144.789 21.543  1.00 24.40 ? 603  EL5 A C4C 1 
HETATM 7611 C  C4D . EL5 E 5 .   ? 17.235  146.623 19.682  1.00 27.24 ? 603  EL5 A C4D 1 
HETATM 7612 C  CAA . EL5 E 5 .   ? 28.419  149.178 20.497  1.00 31.52 ? 603  EL5 A CAA 1 
HETATM 7613 C  CAB . EL5 E 5 .   ? 26.625  142.685 24.825  1.00 25.54 ? 603  EL5 A CAB 1 
HETATM 7614 C  CAC . EL5 E 5 .   ? 21.722  141.281 22.711  1.00 24.91 ? 603  EL5 A CAC 1 
HETATM 7615 C  CAD . EL5 E 5 .   ? 15.513  145.808 21.312  1.00 26.94 ? 603  EL5 A CAD 1 
HETATM 7616 C  CBA . EL5 E 5 .   ? 29.001  150.091 19.665  1.00 36.82 ? 603  EL5 A CBA 1 
HETATM 7617 C  CBB . EL5 E 5 .   ? 26.195  142.888 26.272  1.00 26.77 ? 603  EL5 A CBB 1 
HETATM 7618 C  CBC . EL5 E 5 .   ? 21.354  140.924 24.141  1.00 25.51 ? 603  EL5 A CBC 1 
HETATM 7619 C  CBD . EL5 E 5 .   ? 14.416  146.052 20.646  1.00 28.48 ? 603  EL5 A CBD 1 
HETATM 7620 C  CGB . EL5 E 5 .   ? 26.695  141.818 27.229  1.00 27.58 ? 603  EL5 A CGB 1 
HETATM 7621 C  CGC . EL5 E 5 .   ? 19.867  141.025 24.441  1.00 26.13 ? 603  EL5 A CGC 1 
HETATM 7622 C  CHB . EL5 E 5 .   ? 27.062  146.915 22.167  1.00 25.87 ? 603  EL5 A CHB 1 
HETATM 7623 C  CHC . EL5 E 5 .   ? 24.006  143.410 23.363  1.00 24.27 ? 603  EL5 A CHC 1 
HETATM 7624 C  CHD . EL5 E 5 .   ? 20.430  145.588 20.776  1.00 24.60 ? 603  EL5 A CHD 1 
HETATM 7625 C  CMA . EL5 E 5 .   ? 26.100  150.994 19.573  1.00 28.52 ? 603  EL5 A CMA 1 
HETATM 7626 C  CMB . EL5 E 5 .   ? 28.661  145.026 24.068  1.00 26.35 ? 603  EL5 A CMB 1 
HETATM 7627 C  CMC . EL5 E 5 .   ? 19.636  142.837 21.029  1.00 24.64 ? 603  EL5 A CMC 1 
HETATM 7628 C  CMD . EL5 E 5 .   ? 17.971  144.797 22.830  1.00 27.13 ? 603  EL5 A CMD 1 
HETATM 7629 N  NA  . EL5 E 5 .   ? 25.037  148.082 21.431  1.00 26.18 ? 603  EL5 A NA  1 
HETATM 7630 O  OA  . EL5 E 5 .   ? 23.619  149.591 20.410  1.00 25.56 ? 603  EL5 A OA  1 
HETATM 7631 N  NB  . EL5 E 5 .   ? 25.296  145.292 22.544  1.00 25.30 ? 603  EL5 A NB  1 
HETATM 7632 N  NC  . EL5 E 5 .   ? 22.510  144.856 22.083  1.00 24.00 ? 603  EL5 A NC  1 
HETATM 7633 N  ND  . EL5 E 5 .   ? 18.596  146.531 19.623  1.00 25.92 ? 603  EL5 A ND  1 
HETATM 7634 O  OD  . EL5 E 5 .   ? 16.575  147.164 18.804  1.00 27.28 ? 603  EL5 A OD  1 
HETATM 7635 CL CL  . CL  F 6 .   ? 1.983   134.530 26.505  1.00 55.02 ? 604  CL  A CL  1 
HETATM 7636 CL CL  . CL  G 6 .   ? 15.629  129.366 9.809   1.00 52.03 ? 605  CL  A CL  1 
HETATM 7637 C  C1  . PEG H 3 .   ? 28.642  99.897  7.373   1.00 62.17 ? 601  PEG B C1  1 
HETATM 7638 O  O1  . PEG H 3 .   ? 29.594  100.836 6.887   1.00 58.16 ? 601  PEG B O1  1 
HETATM 7639 C  C2  . PEG H 3 .   ? 27.264  100.074 6.783   1.00 60.75 ? 601  PEG B C2  1 
HETATM 7640 O  O2  . PEG H 3 .   ? 26.926  101.457 6.647   1.00 59.69 ? 601  PEG B O2  1 
HETATM 7641 C  C3  . PEG H 3 .   ? 25.709  101.825 7.300   1.00 53.39 ? 601  PEG B C3  1 
HETATM 7642 C  C4  . PEG H 3 .   ? 24.946  102.843 6.506   1.00 49.13 ? 601  PEG B C4  1 
HETATM 7643 O  O4  . PEG H 3 .   ? 23.559  102.601 6.477   1.00 44.31 ? 601  PEG B O4  1 
HETATM 7644 C  C1  . MPD I 4 .   ? 36.287  115.240 -15.220 1.00 44.21 ? 602  MPD B C1  1 
HETATM 7645 C  C2  . MPD I 4 .   ? 36.399  113.745 -15.488 1.00 45.16 ? 602  MPD B C2  1 
HETATM 7646 O  O2  . MPD I 4 .   ? 37.031  113.601 -16.777 1.00 49.91 ? 602  MPD B O2  1 
HETATM 7647 C  CM  . MPD I 4 .   ? 37.309  113.072 -14.471 1.00 42.52 ? 602  MPD B CM  1 
HETATM 7648 C  C3  . MPD I 4 .   ? 35.024  113.067 -15.599 1.00 44.64 ? 602  MPD B C3  1 
HETATM 7649 C  C4  . MPD I 4 .   ? 34.343  112.500 -14.351 1.00 46.48 ? 602  MPD B C4  1 
HETATM 7650 O  O4  . MPD I 4 .   ? 34.936  112.905 -13.113 1.00 44.81 ? 602  MPD B O4  1 
HETATM 7651 C  C5  . MPD I 4 .   ? 32.871  112.799 -14.279 1.00 46.37 ? 602  MPD B C5  1 
HETATM 7652 C  C1A . EL5 J 5 .   ? 14.951  80.961  12.381  1.00 29.72 ? 603  EL5 B C1A 1 
HETATM 7653 C  C1B . EL5 J 5 .   ? 13.299  83.729  15.425  1.00 26.59 ? 603  EL5 B C1B 1 
HETATM 7654 O  O1B . EL5 J 5 .   ? 12.193  86.230  21.210  1.00 27.44 ? 603  EL5 B O1B 1 
HETATM 7655 C  C1C . EL5 J 5 .   ? 17.079  85.719  15.824  1.00 24.24 ? 603  EL5 B C1C 1 
HETATM 7656 O  O1C . EL5 J 5 .   ? 20.468  87.443  19.316  1.00 26.15 ? 603  EL5 B O1C 1 
HETATM 7657 C  C1D . EL5 J 5 .   ? 20.744  84.084  13.230  1.00 25.73 ? 603  EL5 B C1D 1 
HETATM 7658 C  C2A . EL5 J 5 .   ? 13.694  80.616  11.923  1.00 30.52 ? 603  EL5 B C2A 1 
HETATM 7659 C  C2B . EL5 J 5 .   ? 12.625  84.408  16.433  1.00 26.34 ? 603  EL5 B C2B 1 
HETATM 7660 O  O2B . EL5 J 5 .   ? 14.140  87.269  21.288  1.00 28.98 ? 603  EL5 B O2B 1 
HETATM 7661 C  C2C . EL5 J 5 .   ? 18.099  86.659  15.728  1.00 24.42 ? 603  EL5 B C2C 1 
HETATM 7662 O  O2C . EL5 J 5 .   ? 20.852  87.878  17.179  1.00 25.97 ? 603  EL5 B O2C 1 
HETATM 7663 C  C2D . EL5 J 5 .   ? 21.880  84.156  14.031  1.00 26.14 ? 603  EL5 B C2D 1 
HETATM 7664 C  C3A . EL5 J 5 .   ? 12.676  81.163  12.688  1.00 31.19 ? 603  EL5 B C3A 1 
HETATM 7665 C  C3B . EL5 J 5 .   ? 13.528  85.286  17.021  1.00 26.12 ? 603  EL5 B C3B 1 
HETATM 7666 C  C3C . EL5 J 5 .   ? 18.992  86.193  14.792  1.00 25.15 ? 603  EL5 B C3C 1 
HETATM 7667 C  C3D . EL5 J 5 .   ? 22.970  83.811  13.222  1.00 26.33 ? 603  EL5 B C3D 1 
HETATM 7668 C  C4A . EL5 J 5 .   ? 13.347  81.988  13.593  1.00 29.44 ? 603  EL5 B C4A 1 
HETATM 7669 C  C4B . EL5 J 5 .   ? 14.711  85.150  16.303  1.00 25.97 ? 603  EL5 B C4B 1 
HETATM 7670 C  C4C . EL5 J 5 .   ? 18.607  84.913  14.380  1.00 24.67 ? 603  EL5 B C4C 1 
HETATM 7671 C  C4D . EL5 J 5 .   ? 22.481  83.490  11.952  1.00 26.29 ? 603  EL5 B C4D 1 
HETATM 7672 C  CAA . EL5 J 5 .   ? 11.268  81.043  12.497  1.00 34.07 ? 603  EL5 B CAA 1 
HETATM 7673 C  CAB . EL5 J 5 .   ? 13.306  86.194  18.199  1.00 26.64 ? 603  EL5 B CAB 1 
HETATM 7674 C  CAC . EL5 J 5 .   ? 18.202  87.965  16.469  1.00 24.92 ? 603  EL5 B CAC 1 
HETATM 7675 C  CAD . EL5 J 5 .   ? 24.316  83.798  13.615  1.00 28.03 ? 603  EL5 B CAD 1 
HETATM 7676 C  CBA . EL5 J 5 .   ? 10.617  80.447  11.447  1.00 38.61 ? 603  EL5 B CBA 1 
HETATM 7677 C  CBB . EL5 J 5 .   ? 13.811  85.658  19.547  1.00 27.66 ? 603  EL5 B CBB 1 
HETATM 7678 C  CBC . EL5 J 5 .   ? 18.596  87.904  17.936  1.00 26.12 ? 603  EL5 B CBC 1 
HETATM 7679 C  CBD . EL5 J 5 .   ? 25.368  83.704  12.828  1.00 28.43 ? 603  EL5 B CBD 1 
HETATM 7680 C  CGB . EL5 J 5 .   ? 13.344  86.442  20.768  1.00 28.19 ? 603  EL5 B CGB 1 
HETATM 7681 C  CGC . EL5 J 5 .   ? 20.085  87.730  18.161  1.00 26.06 ? 603  EL5 B CGC 1 
HETATM 7682 C  CHB . EL5 J 5 .   ? 12.737  82.826  14.524  1.00 29.40 ? 603  EL5 B CHB 1 
HETATM 7683 C  CHC . EL5 J 5 .   ? 15.916  85.784  16.583  1.00 24.81 ? 603  EL5 B CHC 1 
HETATM 7684 C  CHD . EL5 J 5 .   ? 19.388  84.320  13.412  1.00 25.63 ? 603  EL5 B CHD 1 
HETATM 7685 C  CMA . EL5 J 5 .   ? 13.495  79.364  11.118  1.00 32.23 ? 603  EL5 B CMA 1 
HETATM 7686 C  CMB . EL5 J 5 .   ? 11.200  84.199  16.861  1.00 26.58 ? 603  EL5 B CMB 1 
HETATM 7687 C  CMC . EL5 J 5 .   ? 20.233  86.921  14.370  1.00 25.77 ? 603  EL5 B CMC 1 
HETATM 7688 C  CMD . EL5 J 5 .   ? 21.951  84.470  15.499  1.00 28.52 ? 603  EL5 B CMD 1 
HETATM 7689 N  NA  . EL5 J 5 .   ? 14.721  81.846  13.419  1.00 29.81 ? 603  EL5 B NA  1 
HETATM 7690 O  OA  . EL5 J 5 .   ? 16.029  80.590  11.992  1.00 29.19 ? 603  EL5 B OA  1 
HETATM 7691 N  NB  . EL5 J 5 .   ? 14.565  84.225  15.309  1.00 24.36 ? 603  EL5 B NB  1 
HETATM 7692 N  NC  . EL5 J 5 .   ? 17.358  84.720  14.910  1.00 23.19 ? 603  EL5 B NC  1 
HETATM 7693 N  ND  . EL5 J 5 .   ? 21.130  83.656  11.994  1.00 24.81 ? 603  EL5 B ND  1 
HETATM 7694 O  OD  . EL5 J 5 .   ? 23.062  83.171  10.915  1.00 26.22 ? 603  EL5 B OD  1 
HETATM 7695 O  O   . HOH K 7 .   ? 15.541  155.516 -1.091  1.00 46.87 ? 701  HOH A O   1 
HETATM 7696 O  O   . HOH K 7 .   ? -0.494  125.242 -13.977 1.00 37.25 ? 702  HOH A O   1 
HETATM 7697 O  O   . HOH K 7 .   ? 23.497  128.215 -10.938 1.00 38.70 ? 703  HOH A O   1 
HETATM 7698 O  O   . HOH K 7 .   ? 18.573  149.127 35.747  1.00 31.79 ? 704  HOH A O   1 
HETATM 7699 O  O   . HOH K 7 .   ? 21.016  141.831 27.367  1.00 22.20 ? 705  HOH A O   1 
HETATM 7700 O  O   . HOH K 7 .   ? 33.652  120.824 49.145  1.00 44.74 ? 706  HOH A O   1 
HETATM 7701 O  O   . HOH K 7 .   ? 25.904  135.536 36.205  1.00 42.08 ? 707  HOH A O   1 
HETATM 7702 O  O   . HOH K 7 .   ? 20.452  113.127 -28.575 1.00 43.12 ? 708  HOH A O   1 
HETATM 7703 O  O   . HOH K 7 .   ? 20.478  148.305 -4.028  1.00 28.26 ? 709  HOH A O   1 
HETATM 7704 O  O   . HOH K 7 .   ? 25.765  144.315 8.364   1.00 39.32 ? 710  HOH A O   1 
HETATM 7705 O  O   . HOH K 7 .   ? 41.128  136.780 59.031  1.00 37.27 ? 711  HOH A O   1 
HETATM 7706 O  O   . HOH K 7 .   ? 42.986  129.269 56.161  1.00 31.02 ? 712  HOH A O   1 
HETATM 7707 O  O   . HOH K 7 .   ? 21.332  149.725 1.000   1.00 45.83 ? 713  HOH A O   1 
HETATM 7708 O  O   . HOH K 7 .   ? 15.551  156.299 -3.673  1.00 44.20 ? 714  HOH A O   1 
HETATM 7709 O  O   . HOH K 7 .   ? 8.061   135.697 13.264  1.00 50.56 ? 715  HOH A O   1 
HETATM 7710 O  O   . HOH K 7 .   ? 7.121   138.649 35.119  1.00 33.87 ? 716  HOH A O   1 
HETATM 7711 O  O   . HOH K 7 .   ? 6.272   115.463 -10.389 1.00 45.35 ? 717  HOH A O   1 
HETATM 7712 O  O   . HOH K 7 .   ? 3.916   140.714 -5.360  1.00 27.68 ? 718  HOH A O   1 
HETATM 7713 O  O   . HOH K 7 .   ? 8.227   118.823 10.391  1.00 48.49 ? 719  HOH A O   1 
HETATM 7714 O  O   . HOH K 7 .   ? 19.557  119.034 -1.908  1.00 47.92 ? 720  HOH A O   1 
HETATM 7715 O  O   . HOH K 7 .   ? 18.185  148.282 38.329  1.00 41.76 ? 721  HOH A O   1 
HETATM 7716 O  O   . HOH K 7 .   ? 16.669  148.353 -15.474 1.00 38.23 ? 722  HOH A O   1 
HETATM 7717 O  O   . HOH K 7 .   ? 8.377   153.260 19.151  1.00 32.51 ? 723  HOH A O   1 
HETATM 7718 O  O   . HOH K 7 .   ? 27.429  132.457 -14.265 1.00 57.15 ? 724  HOH A O   1 
HETATM 7719 O  O   . HOH K 7 .   ? 23.193  134.387 41.980  1.00 45.97 ? 725  HOH A O   1 
HETATM 7720 O  O   . HOH K 7 .   ? 21.405  159.200 16.788  1.00 55.43 ? 726  HOH A O   1 
HETATM 7721 O  O   . HOH K 7 .   ? 15.749  152.267 33.195  1.00 34.45 ? 727  HOH A O   1 
HETATM 7722 O  O   . HOH K 7 .   ? 20.836  127.859 44.367  1.00 39.24 ? 728  HOH A O   1 
HETATM 7723 O  O   . HOH K 7 .   ? 12.661  144.214 26.550  1.00 24.80 ? 729  HOH A O   1 
HETATM 7724 O  O   . HOH K 7 .   ? 3.804   130.505 -4.188  1.00 50.74 ? 730  HOH A O   1 
HETATM 7725 O  O   . HOH K 7 .   ? 20.411  133.199 -21.420 1.00 40.93 ? 731  HOH A O   1 
HETATM 7726 O  O   . HOH K 7 .   ? 15.568  130.054 1.914   1.00 56.69 ? 732  HOH A O   1 
HETATM 7727 O  O   . HOH K 7 .   ? 19.099  133.914 42.005  1.00 46.70 ? 733  HOH A O   1 
HETATM 7728 O  O   . HOH K 7 .   ? 41.589  142.781 33.789  1.00 30.57 ? 734  HOH A O   1 
HETATM 7729 O  O   . HOH K 7 .   ? 37.160  156.529 18.644  1.00 64.73 ? 735  HOH A O   1 
HETATM 7730 O  O   . HOH K 7 .   ? 24.345  143.899 -6.725  1.00 44.39 ? 736  HOH A O   1 
HETATM 7731 O  O   . HOH K 7 .   ? 12.017  149.256 34.756  1.00 44.08 ? 737  HOH A O   1 
HETATM 7732 O  O   . HOH K 7 .   ? 22.980  126.604 -3.115  1.00 42.85 ? 738  HOH A O   1 
HETATM 7733 O  O   . HOH K 7 .   ? 25.351  130.843 51.288  1.00 48.20 ? 739  HOH A O   1 
HETATM 7734 O  O   . HOH K 7 .   ? 17.357  139.979 5.786   1.00 51.45 ? 740  HOH A O   1 
HETATM 7735 O  O   . HOH K 7 .   ? 49.195  129.532 36.102  1.00 51.55 ? 741  HOH A O   1 
HETATM 7736 O  O   . HOH K 7 .   ? 0.724   126.547 -23.559 1.00 36.11 ? 742  HOH A O   1 
HETATM 7737 O  O   . HOH K 7 .   ? 5.201   124.722 -7.547  1.00 54.25 ? 743  HOH A O   1 
HETATM 7738 O  O   . HOH K 7 .   ? 29.682  143.710 27.610  1.00 27.20 ? 744  HOH A O   1 
HETATM 7739 O  O   . HOH K 7 .   ? 16.503  119.918 -12.563 1.00 44.03 ? 745  HOH A O   1 
HETATM 7740 O  O   . HOH K 7 .   ? 16.719  139.632 -3.290  1.00 27.97 ? 746  HOH A O   1 
HETATM 7741 O  O   . HOH K 7 .   ? 23.494  140.205 26.985  1.00 23.82 ? 747  HOH A O   1 
HETATM 7742 O  O   . HOH K 7 .   ? 9.704   143.533 36.668  1.00 27.33 ? 748  HOH A O   1 
HETATM 7743 O  O   . HOH K 7 .   ? 15.813  154.961 8.470   1.00 29.13 ? 749  HOH A O   1 
HETATM 7744 O  O   . HOH K 7 .   ? 15.069  134.106 -28.382 1.00 47.43 ? 750  HOH A O   1 
HETATM 7745 O  O   . HOH K 7 .   ? 30.851  129.326 13.914  1.00 49.45 ? 751  HOH A O   1 
HETATM 7746 O  O   . HOH K 7 .   ? 9.909   124.852 -4.074  1.00 33.88 ? 752  HOH A O   1 
HETATM 7747 O  O   . HOH K 7 .   ? 48.484  138.458 42.874  1.00 36.72 ? 753  HOH A O   1 
HETATM 7748 O  O   . HOH K 7 .   ? 6.687   133.710 16.146  1.00 37.27 ? 754  HOH A O   1 
HETATM 7749 O  O   . HOH K 7 .   ? 24.056  135.792 10.316  1.00 43.85 ? 755  HOH A O   1 
HETATM 7750 O  O   . HOH K 7 .   ? 19.113  137.411 34.602  1.00 26.82 ? 756  HOH A O   1 
HETATM 7751 O  O   . HOH K 7 .   ? 25.269  134.826 13.078  1.00 44.12 ? 757  HOH A O   1 
HETATM 7752 O  O   . HOH K 7 .   ? 17.726  127.378 -25.262 1.00 47.82 ? 758  HOH A O   1 
HETATM 7753 O  O   . HOH K 7 .   ? 19.054  134.382 3.758   1.00 40.74 ? 759  HOH A O   1 
HETATM 7754 O  O   . HOH K 7 .   ? 1.033   125.360 -18.651 1.00 42.38 ? 760  HOH A O   1 
HETATM 7755 O  O   . HOH K 7 .   ? 39.004  141.550 33.452  1.00 29.49 ? 761  HOH A O   1 
HETATM 7756 O  O   . HOH K 7 .   ? 18.808  128.075 2.625   1.00 44.05 ? 762  HOH A O   1 
HETATM 7757 O  O   . HOH K 7 .   ? 23.316  159.273 20.083  1.00 34.08 ? 763  HOH A O   1 
HETATM 7758 O  O   . HOH K 7 .   ? 15.347  158.102 17.693  1.00 35.76 ? 764  HOH A O   1 
HETATM 7759 O  O   . HOH K 7 .   ? 8.953   136.299 37.779  1.00 30.92 ? 765  HOH A O   1 
HETATM 7760 O  O   . HOH K 7 .   ? 27.148  136.013 32.034  1.00 25.22 ? 766  HOH A O   1 
HETATM 7761 O  O   . HOH K 7 .   ? 21.249  145.377 8.193   1.00 28.83 ? 767  HOH A O   1 
HETATM 7762 O  O   . HOH K 7 .   ? 29.210  148.034 16.664  1.00 38.00 ? 768  HOH A O   1 
HETATM 7763 O  O   . HOH K 7 .   ? 12.386  153.802 13.994  1.00 34.33 ? 769  HOH A O   1 
HETATM 7764 O  O   . HOH K 7 .   ? 29.979  129.353 29.395  1.00 46.97 ? 770  HOH A O   1 
HETATM 7765 O  O   . HOH K 7 .   ? 11.243  148.671 26.643  1.00 25.61 ? 771  HOH A O   1 
HETATM 7766 O  O   . HOH K 7 .   ? 2.542   117.252 14.909  1.00 57.41 ? 772  HOH A O   1 
HETATM 7767 O  O   . HOH K 7 .   ? 36.957  150.600 22.306  1.00 47.99 ? 773  HOH A O   1 
HETATM 7768 O  O   . HOH K 7 .   ? 37.065  136.555 24.129  1.00 37.49 ? 774  HOH A O   1 
HETATM 7769 O  O   . HOH K 7 .   ? 17.472  119.326 4.018   1.00 42.28 ? 775  HOH A O   1 
HETATM 7770 O  O   . HOH K 7 .   ? 29.317  139.922 26.445  1.00 28.38 ? 776  HOH A O   1 
HETATM 7771 O  O   . HOH K 7 .   ? 34.495  142.253 50.530  1.00 32.81 ? 777  HOH A O   1 
HETATM 7772 O  O   . HOH K 7 .   ? 16.743  149.791 33.971  1.00 30.12 ? 778  HOH A O   1 
HETATM 7773 O  O   . HOH K 7 .   ? 3.924   139.881 20.720  1.00 33.50 ? 779  HOH A O   1 
HETATM 7774 O  O   . HOH K 7 .   ? 31.925  146.579 32.521  1.00 32.51 ? 780  HOH A O   1 
HETATM 7775 O  O   . HOH K 7 .   ? 40.024  135.459 24.763  1.00 33.38 ? 781  HOH A O   1 
HETATM 7776 O  O   . HOH K 7 .   ? 21.400  157.007 25.728  1.00 23.86 ? 782  HOH A O   1 
HETATM 7777 O  O   . HOH K 7 .   ? 10.545  117.690 -21.909 1.00 39.70 ? 783  HOH A O   1 
HETATM 7778 O  O   . HOH K 7 .   ? 14.898  150.372 4.017   1.00 35.76 ? 784  HOH A O   1 
HETATM 7779 O  O   . HOH K 7 .   ? 14.020  138.772 6.827   1.00 42.01 ? 785  HOH A O   1 
HETATM 7780 O  O   . HOH K 7 .   ? 39.391  146.720 29.607  1.00 48.70 ? 786  HOH A O   1 
HETATM 7781 O  O   . HOH K 7 .   ? 34.613  149.383 28.767  1.00 45.36 ? 787  HOH A O   1 
HETATM 7782 O  O   . HOH K 7 .   ? 18.467  143.017 2.562   1.00 32.38 ? 788  HOH A O   1 
HETATM 7783 O  O   . HOH K 7 .   ? 48.875  137.831 50.984  1.00 42.20 ? 789  HOH A O   1 
HETATM 7784 O  O   . HOH K 7 .   ? 38.972  129.824 54.593  1.00 45.69 ? 790  HOH A O   1 
HETATM 7785 O  O   . HOH K 7 .   ? 8.741   142.451 9.937   1.00 23.13 ? 791  HOH A O   1 
HETATM 7786 O  O   . HOH K 7 .   ? 3.769   132.765 28.647  1.00 33.72 ? 792  HOH A O   1 
HETATM 7787 O  O   . HOH K 7 .   ? 13.910  128.252 -1.151  1.00 45.44 ? 793  HOH A O   1 
HETATM 7788 O  O   . HOH K 7 .   ? 15.498  148.051 16.322  1.00 25.17 ? 794  HOH A O   1 
HETATM 7789 O  O   . HOH K 7 .   ? 6.582   131.594 -3.932  1.00 45.74 ? 795  HOH A O   1 
HETATM 7790 O  O   . HOH K 7 .   ? 33.671  129.981 36.139  1.00 33.96 ? 796  HOH A O   1 
HETATM 7791 O  O   . HOH K 7 .   ? 28.215  134.056 30.381  1.00 41.98 ? 797  HOH A O   1 
HETATM 7792 O  O   . HOH K 7 .   ? 1.461   142.639 33.950  1.00 50.33 ? 798  HOH A O   1 
HETATM 7793 O  O   . HOH K 7 .   ? 5.895   126.949 32.671  1.00 49.94 ? 799  HOH A O   1 
HETATM 7794 O  O   . HOH K 7 .   ? 23.091  130.407 41.948  1.00 37.82 ? 800  HOH A O   1 
HETATM 7795 O  O   . HOH K 7 .   ? 40.960  142.503 49.526  1.00 48.28 ? 801  HOH A O   1 
HETATM 7796 O  O   . HOH K 7 .   ? 31.370  130.458 34.201  1.00 37.96 ? 802  HOH A O   1 
HETATM 7797 O  O   . HOH K 7 .   ? 31.870  148.663 43.570  1.00 43.11 ? 803  HOH A O   1 
HETATM 7798 O  O   . HOH K 7 .   ? 27.371  120.090 43.017  1.00 54.80 ? 804  HOH A O   1 
HETATM 7799 O  O   . HOH K 7 .   ? 22.101  128.741 -8.475  1.00 43.84 ? 805  HOH A O   1 
HETATM 7800 O  O   . HOH K 7 .   ? 31.525  135.773 30.034  1.00 28.43 ? 806  HOH A O   1 
HETATM 7801 O  O   . HOH K 7 .   ? 30.994  147.047 22.777  1.00 32.88 ? 807  HOH A O   1 
HETATM 7802 O  O   . HOH K 7 .   ? 40.104  146.350 21.030  1.00 59.26 ? 808  HOH A O   1 
HETATM 7803 O  O   . HOH K 7 .   ? 13.906  118.643 -10.827 1.00 47.95 ? 809  HOH A O   1 
HETATM 7804 O  O   . HOH K 7 .   ? 26.326  133.828 25.855  1.00 22.01 ? 810  HOH A O   1 
HETATM 7805 O  O   . HOH K 7 .   ? 12.582  141.333 -0.149  1.00 22.89 ? 811  HOH A O   1 
HETATM 7806 O  O   . HOH K 7 .   ? 5.595   114.325 -13.172 1.00 50.68 ? 812  HOH A O   1 
HETATM 7807 O  O   . HOH K 7 .   ? 5.514   140.693 -24.668 1.00 45.25 ? 813  HOH A O   1 
HETATM 7808 O  O   . HOH K 7 .   ? 4.856   133.568 21.199  1.00 33.81 ? 814  HOH A O   1 
HETATM 7809 O  O   . HOH K 7 .   ? 21.708  138.657 28.706  1.00 21.21 ? 815  HOH A O   1 
HETATM 7810 O  O   . HOH K 7 .   ? 5.709   127.036 -2.847  1.00 56.53 ? 816  HOH A O   1 
HETATM 7811 O  O   . HOH K 7 .   ? 6.983   149.148 5.999   1.00 55.02 ? 817  HOH A O   1 
HETATM 7812 O  O   . HOH K 7 .   ? 18.256  126.964 -19.054 1.00 38.37 ? 818  HOH A O   1 
HETATM 7813 O  O   . HOH K 7 .   ? 6.414   159.819 21.019  1.00 61.33 ? 819  HOH A O   1 
HETATM 7814 O  O   . HOH K 7 .   ? 6.976   116.865 31.009  1.00 46.74 ? 820  HOH A O   1 
HETATM 7815 O  O   . HOH K 7 .   ? 10.791  150.044 18.363  1.00 25.25 ? 821  HOH A O   1 
HETATM 7816 O  O   . HOH K 7 .   ? 28.768  130.694 40.506  1.00 29.30 ? 822  HOH A O   1 
HETATM 7817 O  O   . HOH K 7 .   ? 20.193  132.805 11.467  1.00 30.97 ? 823  HOH A O   1 
HETATM 7818 O  O   . HOH K 7 .   ? 6.369   142.275 36.233  1.00 41.91 ? 824  HOH A O   1 
HETATM 7819 O  O   . HOH K 7 .   ? 23.255  135.982 43.928  1.00 44.11 ? 825  HOH A O   1 
HETATM 7820 O  O   . HOH K 7 .   ? 27.029  129.410 22.790  1.00 33.65 ? 826  HOH A O   1 
HETATM 7821 O  O   . HOH K 7 .   ? 24.652  143.345 36.916  1.00 38.27 ? 827  HOH A O   1 
HETATM 7822 O  O   . HOH K 7 .   ? 9.470   142.222 -6.802  1.00 24.61 ? 828  HOH A O   1 
HETATM 7823 O  O   . HOH K 7 .   ? 34.625  127.948 23.377  1.00 48.06 ? 829  HOH A O   1 
HETATM 7824 O  O   . HOH K 7 .   ? 5.633   143.739 -15.791 1.00 42.09 ? 830  HOH A O   1 
HETATM 7825 O  O   . HOH K 7 .   ? 43.217  147.041 39.801  1.00 44.60 ? 831  HOH A O   1 
HETATM 7826 O  O   . HOH K 7 .   ? 13.269  152.899 1.716   1.00 45.69 ? 832  HOH A O   1 
HETATM 7827 O  O   . HOH K 7 .   ? 22.940  147.363 23.230  1.00 20.95 ? 833  HOH A O   1 
HETATM 7828 O  O   . HOH K 7 .   ? 1.438   144.437 18.913  1.00 46.50 ? 834  HOH A O   1 
HETATM 7829 O  O   . HOH K 7 .   ? 5.749   119.251 22.657  1.00 36.10 ? 835  HOH A O   1 
HETATM 7830 O  O   . HOH K 7 .   ? 7.748   149.914 27.811  1.00 41.83 ? 836  HOH A O   1 
HETATM 7831 O  O   . HOH K 7 .   ? 39.254  146.918 38.249  1.00 42.27 ? 837  HOH A O   1 
HETATM 7832 O  O   . HOH K 7 .   ? 9.802   150.833 29.536  1.00 42.60 ? 838  HOH A O   1 
HETATM 7833 O  O   . HOH K 7 .   ? 44.699  137.836 29.845  1.00 55.55 ? 839  HOH A O   1 
HETATM 7834 O  O   . HOH K 7 .   ? 17.785  148.503 -5.800  1.00 27.26 ? 840  HOH A O   1 
HETATM 7835 O  O   . HOH K 7 .   ? 12.373  153.172 -2.430  1.00 41.42 ? 841  HOH A O   1 
HETATM 7836 O  O   . HOH K 7 .   ? -2.352  146.686 33.909  1.00 39.73 ? 842  HOH A O   1 
HETATM 7837 O  O   . HOH K 7 .   ? 3.265   135.412 22.397  1.00 46.36 ? 843  HOH A O   1 
HETATM 7838 O  O   . HOH K 7 .   ? 6.319   156.957 24.669  1.00 47.53 ? 844  HOH A O   1 
HETATM 7839 O  O   . HOH K 7 .   ? 14.747  157.079 20.087  1.00 33.30 ? 845  HOH A O   1 
HETATM 7840 O  O   . HOH K 7 .   ? 11.031  119.094 -24.371 1.00 37.88 ? 846  HOH A O   1 
HETATM 7841 O  O   . HOH K 7 .   ? 13.573  139.158 39.735  1.00 27.06 ? 847  HOH A O   1 
HETATM 7842 O  O   . HOH K 7 .   ? 22.388  126.207 22.348  1.00 51.07 ? 848  HOH A O   1 
HETATM 7843 O  O   . HOH K 7 .   ? 49.060  141.457 48.831  1.00 45.05 ? 849  HOH A O   1 
HETATM 7844 O  O   . HOH K 7 .   ? 41.649  134.137 32.269  1.00 33.04 ? 850  HOH A O   1 
HETATM 7845 O  O   . HOH K 7 .   ? 48.386  132.251 36.056  1.00 62.22 ? 851  HOH A O   1 
HETATM 7846 O  O   . HOH K 7 .   ? 9.162   150.772 20.329  1.00 30.13 ? 852  HOH A O   1 
HETATM 7847 O  O   . HOH K 7 .   ? 1.144   141.199 -15.564 1.00 43.88 ? 853  HOH A O   1 
HETATM 7848 O  O   . HOH K 7 .   ? 46.757  125.754 47.876  1.00 30.36 ? 854  HOH A O   1 
HETATM 7849 O  O   . HOH K 7 .   ? 15.965  148.246 -7.816  1.00 29.81 ? 855  HOH A O   1 
HETATM 7850 O  O   . HOH K 7 .   ? 32.043  143.446 29.368  1.00 32.60 ? 856  HOH A O   1 
HETATM 7851 O  O   . HOH K 7 .   ? 37.504  133.399 31.262  1.00 27.98 ? 857  HOH A O   1 
HETATM 7852 O  O   . HOH K 7 .   ? 14.875  125.592 6.174   1.00 35.72 ? 858  HOH A O   1 
HETATM 7853 O  O   . HOH K 7 .   ? 25.402  129.889 34.469  1.00 37.42 ? 859  HOH A O   1 
HETATM 7854 O  O   . HOH K 7 .   ? 22.882  141.966 40.972  1.00 39.41 ? 860  HOH A O   1 
HETATM 7855 O  O   . HOH K 7 .   ? 6.890   149.317 19.899  1.00 30.17 ? 861  HOH A O   1 
HETATM 7856 O  O   . HOH K 7 .   ? 7.305   148.535 -12.096 1.00 52.20 ? 862  HOH A O   1 
HETATM 7857 O  O   . HOH K 7 .   ? 16.951  134.580 2.555   1.00 37.66 ? 863  HOH A O   1 
HETATM 7858 O  O   . HOH K 7 .   ? 45.677  136.682 33.871  1.00 46.50 ? 864  HOH A O   1 
HETATM 7859 O  O   . HOH K 7 .   ? 11.352  137.734 -31.191 1.00 56.21 ? 865  HOH A O   1 
HETATM 7860 O  O   . HOH K 7 .   ? 19.069  138.703 26.943  1.00 26.10 ? 866  HOH A O   1 
HETATM 7861 O  O   . HOH K 7 .   ? 38.779  139.935 51.860  1.00 42.95 ? 867  HOH A O   1 
HETATM 7862 O  O   . HOH K 7 .   ? 19.802  131.084 9.537   1.00 36.68 ? 868  HOH A O   1 
HETATM 7863 O  O   . HOH K 7 .   ? 42.527  126.487 55.229  1.00 42.76 ? 869  HOH A O   1 
HETATM 7864 O  O   . HOH K 7 .   ? -1.658  128.418 -30.266 1.00 43.36 ? 870  HOH A O   1 
HETATM 7865 O  O   . HOH K 7 .   ? 19.476  143.653 -23.673 1.00 47.94 ? 871  HOH A O   1 
HETATM 7866 O  O   . HOH K 7 .   ? 0.313   130.349 -11.069 1.00 38.60 ? 872  HOH A O   1 
HETATM 7867 O  O   . HOH K 7 .   ? 4.023   142.288 -13.637 1.00 52.42 ? 873  HOH A O   1 
HETATM 7868 O  O   . HOH K 7 .   ? 23.609  133.657 25.389  1.00 24.18 ? 874  HOH A O   1 
HETATM 7869 O  O   . HOH K 7 .   ? 22.641  144.681 41.874  1.00 46.46 ? 875  HOH A O   1 
HETATM 7870 O  O   . HOH K 7 .   ? 5.945   119.181 30.446  1.00 29.64 ? 876  HOH A O   1 
HETATM 7871 O  O   . HOH K 7 .   ? 23.504  145.597 9.758   1.00 34.12 ? 877  HOH A O   1 
HETATM 7872 O  O   . HOH K 7 .   ? 17.939  156.405 30.626  1.00 58.86 ? 878  HOH A O   1 
HETATM 7873 O  O   . HOH K 7 .   ? 27.486  146.487 43.860  1.00 56.35 ? 879  HOH A O   1 
HETATM 7874 O  O   . HOH K 7 .   ? 41.077  123.130 55.706  1.00 39.14 ? 880  HOH A O   1 
HETATM 7875 O  O   . HOH K 7 .   ? 28.154  138.505 24.444  1.00 25.22 ? 881  HOH A O   1 
HETATM 7876 O  O   . HOH K 7 .   ? 16.279  148.919 -20.364 1.00 54.81 ? 882  HOH A O   1 
HETATM 7877 O  O   . HOH K 7 .   ? 10.079  141.443 7.692   1.00 38.80 ? 883  HOH A O   1 
HETATM 7878 O  O   . HOH K 7 .   ? 45.716  136.152 37.228  1.00 37.89 ? 884  HOH A O   1 
HETATM 7879 O  O   . HOH K 7 .   ? 15.176  116.593 9.476   1.00 39.68 ? 885  HOH A O   1 
HETATM 7880 O  O   . HOH K 7 .   ? 1.101   133.652 23.173  1.00 48.52 ? 886  HOH A O   1 
HETATM 7881 O  O   . HOH K 7 .   ? 10.512  139.422 -0.716  1.00 38.34 ? 887  HOH A O   1 
HETATM 7882 O  O   . HOH K 7 .   ? 2.156   133.668 20.269  1.00 36.77 ? 888  HOH A O   1 
HETATM 7883 O  O   . HOH K 7 .   ? 45.167  147.147 38.013  1.00 36.18 ? 889  HOH A O   1 
HETATM 7884 O  O   . HOH K 7 .   ? 13.911  142.527 41.684  1.00 40.94 ? 890  HOH A O   1 
HETATM 7885 O  O   . HOH K 7 .   ? 37.075  123.544 52.550  1.00 39.82 ? 891  HOH A O   1 
HETATM 7886 O  O   . HOH K 7 .   ? 28.243  141.779 46.070  1.00 34.36 ? 892  HOH A O   1 
HETATM 7887 O  O   . HOH K 7 .   ? 32.864  144.913 21.904  1.00 31.82 ? 893  HOH A O   1 
HETATM 7888 O  O   . HOH K 7 .   ? 33.691  132.464 19.560  1.00 44.75 ? 894  HOH A O   1 
HETATM 7889 O  O   . HOH K 7 .   ? 11.039  139.887 39.678  1.00 30.91 ? 895  HOH A O   1 
HETATM 7890 O  O   . HOH K 7 .   ? 37.578  140.615 49.187  1.00 34.35 ? 896  HOH A O   1 
HETATM 7891 O  O   . HOH K 7 .   ? 19.488  134.515 35.195  1.00 25.77 ? 897  HOH A O   1 
HETATM 7892 O  O   . HOH K 7 .   ? 40.290  135.458 56.192  1.00 40.60 ? 898  HOH A O   1 
HETATM 7893 O  O   . HOH K 7 .   ? 0.991   140.524 25.026  1.00 45.20 ? 899  HOH A O   1 
HETATM 7894 O  O   . HOH K 7 .   ? 14.443  148.156 2.222   1.00 29.51 ? 900  HOH A O   1 
HETATM 7895 O  O   . HOH K 7 .   ? 26.876  151.380 33.375  1.00 35.94 ? 901  HOH A O   1 
HETATM 7896 O  O   . HOH K 7 .   ? 3.056   119.632 22.554  1.00 37.22 ? 902  HOH A O   1 
HETATM 7897 O  O   . HOH K 7 .   ? 15.366  138.318 -24.834 1.00 40.44 ? 903  HOH A O   1 
HETATM 7898 O  O   . HOH K 7 .   ? 5.081   145.329 -11.207 1.00 41.84 ? 904  HOH A O   1 
HETATM 7899 O  O   . HOH K 7 .   ? 4.525   146.585 9.346   1.00 37.18 ? 905  HOH A O   1 
HETATM 7900 O  O   . HOH K 7 .   ? 3.383   128.406 28.198  1.00 45.03 ? 906  HOH A O   1 
HETATM 7901 O  O   . HOH K 7 .   ? 6.192   131.708 14.434  1.00 37.25 ? 907  HOH A O   1 
HETATM 7902 O  O   . HOH K 7 .   ? 27.295  154.429 28.079  1.00 55.77 ? 908  HOH A O   1 
HETATM 7903 O  O   . HOH K 7 .   ? 2.118   112.333 22.343  1.00 53.88 ? 909  HOH A O   1 
HETATM 7904 O  O   . HOH K 7 .   ? 28.406  132.606 14.321  1.00 37.73 ? 910  HOH A O   1 
HETATM 7905 O  O   . HOH K 7 .   ? 23.717  130.878 -7.340  1.00 43.87 ? 911  HOH A O   1 
HETATM 7906 O  O   . HOH K 7 .   ? 15.956  130.753 40.265  1.00 40.94 ? 912  HOH A O   1 
HETATM 7907 O  O   . HOH K 7 .   ? 28.224  145.573 34.622  1.00 25.51 ? 913  HOH A O   1 
HETATM 7908 O  O   . HOH K 7 .   ? 28.158  127.262 9.520   1.00 56.93 ? 914  HOH A O   1 
HETATM 7909 O  O   . HOH K 7 .   ? 39.263  138.496 21.367  1.00 57.87 ? 915  HOH A O   1 
HETATM 7910 O  O   . HOH K 7 .   ? 28.253  127.720 27.998  1.00 38.24 ? 916  HOH A O   1 
HETATM 7911 O  O   . HOH K 7 .   ? 12.045  139.890 4.403   1.00 53.46 ? 917  HOH A O   1 
HETATM 7912 O  O   . HOH K 7 .   ? 16.782  137.698 41.231  1.00 42.04 ? 918  HOH A O   1 
HETATM 7913 O  O   . HOH K 7 .   ? 41.307  144.822 32.229  1.00 44.92 ? 919  HOH A O   1 
HETATM 7914 O  O   . HOH K 7 .   ? 21.421  154.853 -7.859  1.00 58.49 ? 920  HOH A O   1 
HETATM 7915 O  O   . HOH K 7 .   ? 8.608   138.459 13.029  1.00 29.32 ? 921  HOH A O   1 
HETATM 7916 O  O   . HOH K 7 .   ? 10.131  152.671 -6.149  1.00 48.78 ? 922  HOH A O   1 
HETATM 7917 O  O   . HOH K 7 .   ? 0.363   140.833 -11.545 1.00 44.33 ? 923  HOH A O   1 
HETATM 7918 O  O   . HOH K 7 .   ? 21.596  125.474 44.844  1.00 47.06 ? 924  HOH A O   1 
HETATM 7919 O  O   . HOH K 7 .   ? -1.094  133.371 -21.635 1.00 37.33 ? 925  HOH A O   1 
HETATM 7920 O  O   . HOH K 7 .   ? 43.535  135.796 31.886  1.00 35.35 ? 926  HOH A O   1 
HETATM 7921 O  O   . HOH K 7 .   ? 3.241   147.908 20.978  1.00 36.89 ? 927  HOH A O   1 
HETATM 7922 O  O   . HOH K 7 .   ? 32.027  152.125 17.349  1.00 46.38 ? 928  HOH A O   1 
HETATM 7923 O  O   . HOH K 7 .   ? 2.733   137.867 24.979  1.00 31.31 ? 929  HOH A O   1 
HETATM 7924 O  O   . HOH K 7 .   ? 32.242  145.142 15.971  1.00 32.75 ? 930  HOH A O   1 
HETATM 7925 O  O   . HOH K 7 .   ? 18.455  140.843 -24.200 1.00 43.57 ? 931  HOH A O   1 
HETATM 7926 O  O   . HOH K 7 .   ? 4.151   139.608 -3.109  1.00 53.27 ? 932  HOH A O   1 
HETATM 7927 O  O   . HOH K 7 .   ? 33.721  144.107 19.489  1.00 28.53 ? 933  HOH A O   1 
HETATM 7928 O  O   . HOH K 7 .   ? 18.855  142.528 7.647   1.00 25.84 ? 934  HOH A O   1 
HETATM 7929 O  O   . HOH K 7 .   ? 12.247  157.602 21.122  1.00 42.58 ? 935  HOH A O   1 
HETATM 7930 O  O   . HOH K 7 .   ? 38.060  124.505 32.217  1.00 40.57 ? 936  HOH A O   1 
HETATM 7931 O  O   . HOH K 7 .   ? 9.327   124.330 9.254   1.00 39.83 ? 937  HOH A O   1 
HETATM 7932 O  O   . HOH K 7 .   ? 49.939  133.969 52.363  1.00 29.46 ? 938  HOH A O   1 
HETATM 7933 O  O   . HOH K 7 .   ? 11.592  156.845 14.023  1.00 49.48 ? 939  HOH A O   1 
HETATM 7934 O  O   . HOH K 7 .   ? 34.974  152.152 29.121  1.00 55.57 ? 940  HOH A O   1 
HETATM 7935 O  O   . HOH K 7 .   ? 9.277   119.316 -26.622 1.00 41.82 ? 941  HOH A O   1 
HETATM 7936 O  O   . HOH K 7 .   ? 43.564  128.693 27.564  1.00 43.93 ? 942  HOH A O   1 
HETATM 7937 O  O   . HOH K 7 .   ? 19.267  137.350 5.322   1.00 38.16 ? 943  HOH A O   1 
HETATM 7938 O  O   . HOH K 7 .   ? 20.519  156.039 30.356  1.00 58.31 ? 944  HOH A O   1 
HETATM 7939 O  O   . HOH K 7 .   ? 14.464  116.595 17.544  1.00 45.58 ? 945  HOH A O   1 
HETATM 7940 O  O   . HOH K 7 .   ? 3.385   141.619 -18.905 1.00 36.39 ? 946  HOH A O   1 
HETATM 7941 O  O   . HOH K 7 .   ? 29.846  126.918 20.203  1.00 61.16 ? 947  HOH A O   1 
HETATM 7942 O  O   . HOH K 7 .   ? 28.825  143.602 14.446  1.00 40.73 ? 948  HOH A O   1 
HETATM 7943 O  O   . HOH K 7 .   ? 26.617  129.272 29.821  1.00 34.06 ? 949  HOH A O   1 
HETATM 7944 O  O   . HOH K 7 .   ? 7.954   124.205 31.808  1.00 42.59 ? 950  HOH A O   1 
HETATM 7945 O  O   . HOH K 7 .   ? 21.234  137.570 -2.796  1.00 24.28 ? 951  HOH A O   1 
HETATM 7946 O  O   . HOH K 7 .   ? 34.253  117.070 43.001  1.00 58.06 ? 952  HOH A O   1 
HETATM 7947 O  O   . HOH K 7 .   ? 18.606  126.255 -21.789 1.00 53.81 ? 953  HOH A O   1 
HETATM 7948 O  O   . HOH K 7 .   ? 38.972  121.603 54.936  1.00 45.98 ? 954  HOH A O   1 
HETATM 7949 O  O   . HOH K 7 .   ? 0.350   138.712 28.081  1.00 46.30 ? 955  HOH A O   1 
HETATM 7950 O  O   . HOH K 7 .   ? 9.779   126.484 -29.810 1.00 61.03 ? 956  HOH A O   1 
HETATM 7951 O  O   . HOH K 7 .   ? 5.437   147.157 -18.376 1.00 54.75 ? 957  HOH A O   1 
HETATM 7952 O  O   . HOH K 7 .   ? 28.105  153.316 17.504  1.00 43.57 ? 958  HOH A O   1 
HETATM 7953 O  O   . HOH K 7 .   ? 27.981  140.778 11.926  1.00 53.40 ? 959  HOH A O   1 
HETATM 7954 O  O   . HOH K 7 .   ? 25.127  135.418 -7.857  1.00 42.04 ? 960  HOH A O   1 
HETATM 7955 O  O   . HOH K 7 .   ? 30.119  132.395 31.092  1.00 45.29 ? 961  HOH A O   1 
HETATM 7956 O  O   . HOH K 7 .   ? 25.026  150.137 11.290  1.00 50.64 ? 962  HOH A O   1 
HETATM 7957 O  O   . HOH K 7 .   ? 2.560   141.773 19.062  1.00 39.03 ? 963  HOH A O   1 
HETATM 7958 O  O   . HOH K 7 .   ? 25.117  150.565 36.607  1.00 63.36 ? 964  HOH A O   1 
HETATM 7959 O  O   . HOH K 7 .   ? 17.392  119.594 1.549   1.00 40.33 ? 965  HOH A O   1 
HETATM 7960 O  O   . HOH K 7 .   ? 25.985  152.182 13.898  1.00 45.40 ? 966  HOH A O   1 
HETATM 7961 O  O   . HOH K 7 .   ? 29.311  150.695 38.090  1.00 44.62 ? 967  HOH A O   1 
HETATM 7962 O  O   . HOH K 7 .   ? 26.513  136.413 14.819  1.00 48.35 ? 968  HOH A O   1 
HETATM 7963 O  O   . HOH K 7 .   ? 5.744   123.077 32.230  1.00 42.27 ? 969  HOH A O   1 
HETATM 7964 O  O   . HOH K 7 .   ? 22.911  130.130 51.032  1.00 53.59 ? 970  HOH A O   1 
HETATM 7965 O  O   . HOH K 7 .   ? 5.486   135.330 18.903  1.00 31.50 ? 971  HOH A O   1 
HETATM 7966 O  O   . HOH K 7 .   ? 38.199  134.518 57.584  1.00 42.93 ? 972  HOH A O   1 
HETATM 7967 O  O   . HOH K 7 .   ? -1.168  125.120 -27.438 1.00 48.64 ? 973  HOH A O   1 
HETATM 7968 O  O   . HOH K 7 .   ? 7.422   142.951 -25.231 1.00 50.37 ? 974  HOH A O   1 
HETATM 7969 O  O   . HOH K 7 .   ? 21.769  131.169 2.717   1.00 33.97 ? 975  HOH A O   1 
HETATM 7970 O  O   . HOH K 7 .   ? 20.015  117.179 36.981  1.00 54.88 ? 976  HOH A O   1 
HETATM 7971 O  O   . HOH K 7 .   ? 19.002  118.464 26.286  1.00 52.79 ? 977  HOH A O   1 
HETATM 7972 O  O   . HOH K 7 .   ? 11.182  159.687 19.806  1.00 47.11 ? 978  HOH A O   1 
HETATM 7973 O  O   . HOH K 7 .   ? 29.714  158.931 21.897  1.00 43.07 ? 979  HOH A O   1 
HETATM 7974 O  O   . HOH K 7 .   ? 20.745  140.071 5.162   1.00 35.91 ? 980  HOH A O   1 
HETATM 7975 O  O   . HOH K 7 .   ? 25.208  147.649 11.056  1.00 25.88 ? 981  HOH A O   1 
HETATM 7976 O  O   . HOH K 7 .   ? 32.916  146.088 29.254  1.00 39.93 ? 982  HOH A O   1 
HETATM 7977 O  O   . HOH K 7 .   ? 15.594  155.679 31.567  1.00 58.61 ? 983  HOH A O   1 
HETATM 7978 O  O   . HOH K 7 .   ? 15.890  161.661 28.442  1.00 56.50 ? 984  HOH A O   1 
HETATM 7979 O  O   . HOH K 7 .   ? 26.484  154.940 16.139  1.00 55.51 ? 985  HOH A O   1 
HETATM 7980 O  O   . HOH K 7 .   ? 14.264  135.862 9.270   1.00 27.23 ? 986  HOH A O   1 
HETATM 7981 O  O   . HOH K 7 .   ? 1.103   143.703 -10.777 1.00 32.15 ? 987  HOH A O   1 
HETATM 7982 O  O   . HOH K 7 .   ? 2.205   144.828 8.104   1.00 49.96 ? 988  HOH A O   1 
HETATM 7983 O  O   . HOH K 7 .   ? 4.753   131.978 -30.595 1.00 62.01 ? 989  HOH A O   1 
HETATM 7984 O  O   . HOH K 7 .   ? 9.306   116.738 -28.053 1.00 54.08 ? 990  HOH A O   1 
HETATM 7985 O  O   . HOH K 7 .   ? 0.648   117.443 -22.610 1.00 49.12 ? 991  HOH A O   1 
HETATM 7986 O  O   . HOH K 7 .   ? 28.290  136.012 26.286  1.00 30.59 ? 992  HOH A O   1 
HETATM 7987 O  O   . HOH K 7 .   ? 24.347  146.717 43.060  1.00 49.00 ? 993  HOH A O   1 
HETATM 7988 O  O   . HOH K 7 .   ? 34.646  142.710 53.340  1.00 61.13 ? 994  HOH A O   1 
HETATM 7989 O  O   . HOH K 7 .   ? 9.823   124.193 -33.195 1.00 59.23 ? 995  HOH A O   1 
HETATM 7990 O  O   . HOH K 7 .   ? 10.092  136.959 -1.199  1.00 45.88 ? 996  HOH A O   1 
HETATM 7991 O  O   . HOH K 7 .   ? 26.227  133.636 -29.561 1.00 50.47 ? 997  HOH A O   1 
HETATM 7992 O  O   . HOH K 7 .   ? 6.571   139.231 6.737   1.00 59.43 ? 998  HOH A O   1 
HETATM 7993 O  O   . HOH K 7 .   ? 9.670   113.423 -34.968 1.00 52.80 ? 999  HOH A O   1 
HETATM 7994 O  O   . HOH K 7 .   ? 40.115  156.999 28.650  1.00 67.43 ? 1000 HOH A O   1 
HETATM 7995 O  O   . HOH K 7 .   ? 11.885  119.086 38.533  1.00 56.48 ? 1001 HOH A O   1 
HETATM 7996 O  O   . HOH K 7 .   ? 50.292  134.955 44.454  1.00 58.29 ? 1002 HOH A O   1 
HETATM 7997 O  O   . HOH K 7 .   ? 14.386  149.367 35.812  1.00 42.41 ? 1003 HOH A O   1 
HETATM 7998 O  O   . HOH K 7 .   ? 21.753  127.721 -19.490 1.00 58.53 ? 1004 HOH A O   1 
HETATM 7999 O  O   . HOH K 7 .   ? 11.376  135.260 -30.939 1.00 54.54 ? 1005 HOH A O   1 
HETATM 8000 O  O   . HOH K 7 .   ? 35.554  148.822 31.417  1.00 56.71 ? 1006 HOH A O   1 
HETATM 8001 O  O   . HOH K 7 .   ? 35.845  147.185 28.963  1.00 53.15 ? 1007 HOH A O   1 
HETATM 8002 O  O   . HOH K 7 .   ? 23.391  140.150 3.206   1.00 58.14 ? 1008 HOH A O   1 
HETATM 8003 O  O   . HOH K 7 .   ? 16.039  154.685 5.351   1.00 42.55 ? 1009 HOH A O   1 
HETATM 8004 O  O   . HOH K 7 .   ? 13.203  130.567 10.361  1.00 53.79 ? 1010 HOH A O   1 
HETATM 8005 O  O   . HOH K 7 .   ? 18.745  141.906 4.954   1.00 40.41 ? 1011 HOH A O   1 
HETATM 8006 O  O   . HOH K 7 .   ? 10.645  115.865 -25.678 1.00 54.51 ? 1012 HOH A O   1 
HETATM 8007 O  O   . HOH K 7 .   ? 49.041  124.741 49.415  1.00 44.29 ? 1013 HOH A O   1 
HETATM 8008 O  O   . HOH K 7 .   ? 29.193  124.328 -21.047 1.00 55.11 ? 1014 HOH A O   1 
HETATM 8009 O  O   . HOH K 7 .   ? 27.682  145.094 37.258  1.00 39.89 ? 1015 HOH A O   1 
HETATM 8010 O  O   . HOH K 7 .   ? 23.379  125.989 -6.192  1.00 49.99 ? 1016 HOH A O   1 
HETATM 8011 O  O   . HOH K 7 .   ? 26.895  130.864 32.295  1.00 41.83 ? 1017 HOH A O   1 
HETATM 8012 O  O   . HOH K 7 .   ? 13.842  152.804 4.250   1.00 43.53 ? 1018 HOH A O   1 
HETATM 8013 O  O   . HOH K 7 .   ? 10.036  153.204 14.679  1.00 43.01 ? 1019 HOH A O   1 
HETATM 8014 O  O   . HOH K 7 .   ? 14.959  148.207 38.110  1.00 43.72 ? 1020 HOH A O   1 
HETATM 8015 O  O   . HOH K 7 .   ? 2.341   139.875 14.311  1.00 45.47 ? 1021 HOH A O   1 
HETATM 8016 O  O   . HOH K 7 .   ? 11.278  137.265 0.881   1.00 58.10 ? 1022 HOH A O   1 
HETATM 8017 O  O   . HOH K 7 .   ? 10.536  152.285 16.989  1.00 35.71 ? 1023 HOH A O   1 
HETATM 8018 O  O   . HOH K 7 .   ? 6.295   145.290 -22.968 1.00 51.45 ? 1024 HOH A O   1 
HETATM 8019 O  O   . HOH K 7 .   ? 13.643  155.315 9.454   1.00 40.70 ? 1025 HOH A O   1 
HETATM 8020 O  O   . HOH K 7 .   ? 29.000  155.800 29.561  1.00 46.82 ? 1026 HOH A O   1 
HETATM 8021 O  O   . HOH K 7 .   ? 18.246  119.139 -10.522 1.00 51.04 ? 1027 HOH A O   1 
HETATM 8022 O  O   . HOH K 7 .   ? 27.613  138.285 11.258  1.00 54.51 ? 1028 HOH A O   1 
HETATM 8023 O  O   . HOH K 7 .   ? 30.137  146.525 14.927  1.00 34.59 ? 1029 HOH A O   1 
HETATM 8024 O  O   . HOH K 7 .   ? 29.589  150.807 16.188  1.00 32.53 ? 1030 HOH A O   1 
HETATM 8025 O  O   . HOH K 7 .   ? 20.015  130.134 4.138   1.00 64.67 ? 1031 HOH A O   1 
HETATM 8026 O  O   . HOH K 7 .   ? 4.921   135.854 13.762  1.00 51.86 ? 1032 HOH A O   1 
HETATM 8027 O  O   . HOH K 7 .   ? 29.458  126.288 -17.453 1.00 58.79 ? 1033 HOH A O   1 
HETATM 8028 O  O   . HOH K 7 .   ? 29.593  125.368 22.820  1.00 72.21 ? 1034 HOH A O   1 
HETATM 8029 O  O   . HOH K 7 .   ? 7.885   153.912 13.047  1.00 51.18 ? 1035 HOH A O   1 
HETATM 8030 O  O   . HOH K 7 .   ? 27.364  132.794 11.003  1.00 59.81 ? 1036 HOH A O   1 
HETATM 8031 O  O   . HOH K 7 .   ? 33.849  129.740 19.316  1.00 51.09 ? 1037 HOH A O   1 
HETATM 8032 O  O   . HOH K 7 .   ? 28.274  144.396 46.283  1.00 46.54 ? 1038 HOH A O   1 
HETATM 8033 O  O   . HOH K 7 .   ? 22.578  118.558 36.454  1.00 60.91 ? 1039 HOH A O   1 
HETATM 8034 O  O   . HOH K 7 .   ? 29.827  130.957 10.156  1.00 54.88 ? 1040 HOH A O   1 
HETATM 8035 O  O   . HOH L 7 .   ? 21.561  77.362  29.420  1.00 48.22 ? 701  HOH B O   1 
HETATM 8036 O  O   . HOH L 7 .   ? 9.533   95.310  56.118  1.00 46.61 ? 702  HOH B O   1 
HETATM 8037 O  O   . HOH L 7 .   ? 40.721  112.343 -15.610 1.00 33.13 ? 703  HOH B O   1 
HETATM 8038 O  O   . HOH L 7 .   ? 21.383  76.938  26.749  1.00 43.78 ? 704  HOH B O   1 
HETATM 8039 O  O   . HOH L 7 .   ? 34.845  99.455  -29.415 1.00 43.57 ? 705  HOH B O   1 
HETATM 8040 O  O   . HOH L 7 .   ? 27.482  95.401  41.211  1.00 39.06 ? 706  HOH B O   1 
HETATM 8041 O  O   . HOH L 7 .   ? 14.822  104.786 -12.608 1.00 48.02 ? 707  HOH B O   1 
HETATM 8042 O  O   . HOH L 7 .   ? 18.225  92.557  46.634  1.00 40.26 ? 708  HOH B O   1 
HETATM 8043 O  O   . HOH L 7 .   ? 21.753  73.764  27.197  1.00 55.61 ? 709  HOH B O   1 
HETATM 8044 O  O   . HOH L 7 .   ? 18.836  86.325  20.774  1.00 19.87 ? 710  HOH B O   1 
HETATM 8045 O  O   . HOH L 7 .   ? 10.059  97.662  26.171  1.00 44.65 ? 711  HOH B O   1 
HETATM 8046 O  O   . HOH L 7 .   ? 33.927  121.097 -9.856  1.00 35.48 ? 712  HOH B O   1 
HETATM 8047 O  O   . HOH L 7 .   ? 26.120  80.993  33.752  1.00 30.84 ? 713  HOH B O   1 
HETATM 8048 O  O   . HOH L 7 .   ? 36.859  83.292  6.099   1.00 45.58 ? 714  HOH B O   1 
HETATM 8049 O  O   . HOH L 7 .   ? 31.021  89.790  3.665   1.00 24.60 ? 715  HOH B O   1 
HETATM 8050 O  O   . HOH L 7 .   ? 28.585  79.977  18.203  1.00 28.41 ? 716  HOH B O   1 
HETATM 8051 O  O   . HOH L 7 .   ? 31.941  103.286 -26.721 1.00 39.73 ? 717  HOH B O   1 
HETATM 8052 O  O   . HOH L 7 .   ? 30.115  110.073 8.001   1.00 45.96 ? 718  HOH B O   1 
HETATM 8053 O  O   . HOH L 7 .   ? 36.106  109.087 24.857  1.00 42.94 ? 719  HOH B O   1 
HETATM 8054 O  O   . HOH L 7 .   ? 24.411  79.921  -13.204 1.00 38.16 ? 720  HOH B O   1 
HETATM 8055 O  O   . HOH L 7 .   ? 32.075  78.374  18.988  1.00 33.80 ? 721  HOH B O   1 
HETATM 8056 O  O   . HOH L 7 .   ? 7.970   101.853 47.767  1.00 56.36 ? 722  HOH B O   1 
HETATM 8057 O  O   . HOH L 7 .   ? 38.828  115.517 -31.575 1.00 58.23 ? 723  HOH B O   1 
HETATM 8058 O  O   . HOH L 7 .   ? 20.075  95.713  40.664  1.00 41.04 ? 724  HOH B O   1 
HETATM 8059 O  O   . HOH L 7 .   ? 28.200  76.918  25.184  1.00 36.07 ? 725  HOH B O   1 
HETATM 8060 O  O   . HOH L 7 .   ? 2.753   92.189  19.711  1.00 41.35 ? 726  HOH B O   1 
HETATM 8061 O  O   . HOH L 7 .   ? 38.985  113.509 -19.954 1.00 37.53 ? 727  HOH B O   1 
HETATM 8062 O  O   . HOH L 7 .   ? 17.342  108.690 -5.447  1.00 46.74 ? 728  HOH B O   1 
HETATM 8063 O  O   . HOH L 7 .   ? 23.617  78.084  -0.827  1.00 32.62 ? 729  HOH B O   1 
HETATM 8064 O  O   . HOH L 7 .   ? 24.787  83.548  -4.095  1.00 45.23 ? 730  HOH B O   1 
HETATM 8065 O  O   . HOH L 7 .   ? 26.192  81.973  -13.668 1.00 47.77 ? 731  HOH B O   1 
HETATM 8066 O  O   . HOH L 7 .   ? 27.244  73.176  17.745  1.00 41.76 ? 732  HOH B O   1 
HETATM 8067 O  O   . HOH L 7 .   ? 35.192  95.811  16.072  1.00 28.46 ? 733  HOH B O   1 
HETATM 8068 O  O   . HOH L 7 .   ? -0.156  93.146  20.719  1.00 42.24 ? 734  HOH B O   1 
HETATM 8069 O  O   . HOH L 7 .   ? 35.181  90.186  7.391   1.00 39.93 ? 735  HOH B O   1 
HETATM 8070 O  O   . HOH L 7 .   ? 13.768  94.473  21.329  1.00 31.38 ? 736  HOH B O   1 
HETATM 8071 O  O   . HOH L 7 .   ? 20.774  96.779  -29.235 1.00 43.11 ? 737  HOH B O   1 
HETATM 8072 O  O   . HOH L 7 .   ? 30.596  94.143  -12.648 1.00 22.69 ? 738  HOH B O   1 
HETATM 8073 O  O   . HOH L 7 .   ? 18.324  87.567  1.526   1.00 31.06 ? 739  HOH B O   1 
HETATM 8074 O  O   . HOH L 7 .   ? 21.847  115.538 -6.498  1.00 51.12 ? 740  HOH B O   1 
HETATM 8075 O  O   . HOH L 7 .   ? 24.897  102.478 -29.333 1.00 36.84 ? 741  HOH B O   1 
HETATM 8076 O  O   . HOH L 7 .   ? 17.028  92.820  -25.561 1.00 43.48 ? 742  HOH B O   1 
HETATM 8077 O  O   . HOH L 7 .   ? 17.539  86.484  -9.501  1.00 45.13 ? 743  HOH B O   1 
HETATM 8078 O  O   . HOH L 7 .   ? 39.808  113.398 -24.985 1.00 39.28 ? 744  HOH B O   1 
HETATM 8079 O  O   . HOH L 7 .   ? 5.963   94.582  48.614  1.00 42.91 ? 745  HOH B O   1 
HETATM 8080 O  O   . HOH L 7 .   ? 18.146  71.990  15.228  1.00 26.85 ? 746  HOH B O   1 
HETATM 8081 O  O   . HOH L 7 .   ? 30.290  110.544 -5.805  1.00 27.18 ? 747  HOH B O   1 
HETATM 8082 O  O   . HOH L 7 .   ? 35.874  95.685  31.168  1.00 39.36 ? 748  HOH B O   1 
HETATM 8083 O  O   . HOH L 7 .   ? 24.628  93.813  46.578  1.00 34.73 ? 749  HOH B O   1 
HETATM 8084 O  O   . HOH L 7 .   ? 6.975   95.747  32.800  1.00 39.55 ? 750  HOH B O   1 
HETATM 8085 O  O   . HOH L 7 .   ? 16.571  109.005 -13.370 1.00 42.20 ? 751  HOH B O   1 
HETATM 8086 O  O   . HOH L 7 .   ? 29.352  91.451  1.274   1.00 39.34 ? 752  HOH B O   1 
HETATM 8087 O  O   . HOH L 7 .   ? 8.743   82.381  15.298  1.00 35.81 ? 753  HOH B O   1 
HETATM 8088 O  O   . HOH L 7 .   ? 10.271  84.506  20.761  1.00 24.97 ? 754  HOH B O   1 
HETATM 8089 O  O   . HOH L 7 .   ? 24.483  70.907  11.466  1.00 47.58 ? 755  HOH B O   1 
HETATM 8090 O  O   . HOH L 7 .   ? 20.829  89.378  21.049  1.00 26.73 ? 756  HOH B O   1 
HETATM 8091 O  O   . HOH L 7 .   ? 19.727  106.470 -24.649 1.00 38.63 ? 757  HOH B O   1 
HETATM 8092 O  O   . HOH L 7 .   ? 33.603  102.987 -7.819  1.00 36.27 ? 758  HOH B O   1 
HETATM 8093 O  O   . HOH L 7 .   ? 22.782  114.105 3.629   1.00 39.31 ? 759  HOH B O   1 
HETATM 8094 O  O   . HOH L 7 .   ? 17.264  93.786  49.229  1.00 40.33 ? 760  HOH B O   1 
HETATM 8095 O  O   . HOH L 7 .   ? 27.268  78.043  4.705   1.00 37.45 ? 761  HOH B O   1 
HETATM 8096 O  O   . HOH L 7 .   ? 23.017  99.341  -1.731  1.00 35.25 ? 762  HOH B O   1 
HETATM 8097 O  O   . HOH L 7 .   ? 12.134  94.038  36.580  1.00 29.75 ? 763  HOH B O   1 
HETATM 8098 O  O   . HOH L 7 .   ? 25.423  117.800 -29.169 1.00 42.69 ? 764  HOH B O   1 
HETATM 8099 O  O   . HOH L 7 .   ? 18.158  93.868  37.917  1.00 30.85 ? 765  HOH B O   1 
HETATM 8100 O  O   . HOH L 7 .   ? 23.361  90.305  -22.658 1.00 29.96 ? 766  HOH B O   1 
HETATM 8101 O  O   . HOH L 7 .   ? 36.046  89.671  14.702  1.00 32.18 ? 767  HOH B O   1 
HETATM 8102 O  O   . HOH L 7 .   ? 36.470  93.732  17.496  1.00 39.96 ? 768  HOH B O   1 
HETATM 8103 O  O   . HOH L 7 .   ? 41.132  115.410 -28.897 1.00 47.19 ? 769  HOH B O   1 
HETATM 8104 O  O   . HOH L 7 .   ? 21.241  91.244  -3.807  1.00 38.79 ? 770  HOH B O   1 
HETATM 8105 O  O   . HOH L 7 .   ? 35.822  94.268  23.900  1.00 35.30 ? 771  HOH B O   1 
HETATM 8106 O  O   . HOH L 7 .   ? 6.698   80.351  43.790  1.00 45.99 ? 772  HOH B O   1 
HETATM 8107 O  O   . HOH L 7 .   ? 36.143  95.265  -10.667 1.00 27.55 ? 773  HOH B O   1 
HETATM 8108 O  O   . HOH L 7 .   ? 24.229  74.628  23.682  1.00 34.71 ? 774  HOH B O   1 
HETATM 8109 O  O   . HOH L 7 .   ? 15.641  96.006  5.962   1.00 52.24 ? 775  HOH B O   1 
HETATM 8110 O  O   . HOH L 7 .   ? 30.615  81.915  28.788  1.00 27.44 ? 776  HOH B O   1 
HETATM 8111 O  O   . HOH L 7 .   ? 14.774  90.714  31.157  1.00 48.86 ? 777  HOH B O   1 
HETATM 8112 O  O   . HOH L 7 .   ? 24.015  88.768  -15.033 1.00 30.77 ? 778  HOH B O   1 
HETATM 8113 O  O   . HOH L 7 .   ? 4.981   79.147  20.678  1.00 49.25 ? 779  HOH B O   1 
HETATM 8114 O  O   . HOH L 7 .   ? 9.433   95.564  30.253  1.00 40.54 ? 780  HOH B O   1 
HETATM 8115 O  O   . HOH L 7 .   ? 21.737  68.103  20.010  1.00 42.54 ? 781  HOH B O   1 
HETATM 8116 O  O   . HOH L 7 .   ? 12.159  93.235  26.036  1.00 37.75 ? 782  HOH B O   1 
HETATM 8117 O  O   . HOH L 7 .   ? 24.764  101.670 36.123  1.00 35.29 ? 783  HOH B O   1 
HETATM 8118 O  O   . HOH L 7 .   ? 26.236  81.949  -7.350  1.00 59.71 ? 784  HOH B O   1 
HETATM 8119 O  O   . HOH L 7 .   ? 18.214  89.072  22.865  1.00 22.41 ? 785  HOH B O   1 
HETATM 8120 O  O   . HOH L 7 .   ? 8.108   80.546  24.827  1.00 34.34 ? 786  HOH B O   1 
HETATM 8121 O  O   . HOH L 7 .   ? 34.317  94.860  -32.068 1.00 53.72 ? 787  HOH B O   1 
HETATM 8122 O  O   . HOH L 7 .   ? 22.080  87.990  -13.128 1.00 30.52 ? 788  HOH B O   1 
HETATM 8123 O  O   . HOH L 7 .   ? 23.817  117.205 -12.531 1.00 46.98 ? 789  HOH B O   1 
HETATM 8124 O  O   . HOH L 7 .   ? 16.619  88.150  20.827  1.00 25.25 ? 790  HOH B O   1 
HETATM 8125 O  O   . HOH L 7 .   ? 16.446  94.736  20.699  1.00 23.76 ? 791  HOH B O   1 
HETATM 8126 O  O   . HOH L 7 .   ? 18.103  107.721 -11.103 1.00 44.30 ? 792  HOH B O   1 
HETATM 8127 O  O   . HOH L 7 .   ? 1.238   84.997  27.460  1.00 32.28 ? 793  HOH B O   1 
HETATM 8128 O  O   . HOH L 7 .   ? 3.500   82.206  42.765  1.00 38.04 ? 794  HOH B O   1 
HETATM 8129 O  O   . HOH L 7 .   ? 8.650   91.668  25.281  1.00 31.99 ? 795  HOH B O   1 
HETATM 8130 O  O   . HOH L 7 .   ? 19.812  127.773 -26.912 1.00 44.51 ? 796  HOH B O   1 
HETATM 8131 O  O   . HOH L 7 .   ? 21.952  111.972 -20.906 1.00 29.07 ? 797  HOH B O   1 
HETATM 8132 O  O   . HOH L 7 .   ? 34.775  115.554 -6.983  1.00 40.83 ? 798  HOH B O   1 
HETATM 8133 O  O   . HOH L 7 .   ? 32.938  89.578  -19.257 1.00 44.31 ? 799  HOH B O   1 
HETATM 8134 O  O   . HOH L 7 .   ? 29.003  94.336  -29.321 1.00 39.39 ? 800  HOH B O   1 
HETATM 8135 O  O   . HOH L 7 .   ? 16.133  71.314  9.259   1.00 35.32 ? 801  HOH B O   1 
HETATM 8136 O  O   . HOH L 7 .   ? 28.883  95.332  33.171  1.00 32.95 ? 802  HOH B O   1 
HETATM 8137 O  O   . HOH L 7 .   ? -8.072  85.095  46.023  1.00 53.45 ? 803  HOH B O   1 
HETATM 8138 O  O   . HOH L 7 .   ? 23.214  76.821  24.903  1.00 35.88 ? 804  HOH B O   1 
HETATM 8139 O  O   . HOH L 7 .   ? 18.806  82.522  -16.730 1.00 54.24 ? 805  HOH B O   1 
HETATM 8140 O  O   . HOH L 7 .   ? 20.484  114.282 -8.776  1.00 48.78 ? 806  HOH B O   1 
HETATM 8141 O  O   . HOH L 7 .   ? 23.348  96.063  -8.677  1.00 34.34 ? 807  HOH B O   1 
HETATM 8142 O  O   . HOH L 7 .   ? 32.782  127.000 -14.446 1.00 59.67 ? 808  HOH B O   1 
HETATM 8143 O  O   . HOH L 7 .   ? 7.212   99.109  50.235  1.00 39.66 ? 809  HOH B O   1 
HETATM 8144 O  O   . HOH L 7 .   ? 24.740  73.159  9.812   1.00 38.89 ? 810  HOH B O   1 
HETATM 8145 O  O   . HOH L 7 .   ? 10.390  82.951  9.019   1.00 34.43 ? 811  HOH B O   1 
HETATM 8146 O  O   . HOH L 7 .   ? 21.279  88.328  28.731  1.00 28.22 ? 812  HOH B O   1 
HETATM 8147 O  O   . HOH L 7 .   ? 41.270  106.394 -25.101 1.00 42.65 ? 813  HOH B O   1 
HETATM 8148 O  O   . HOH L 7 .   ? 31.527  85.705  -15.386 1.00 53.66 ? 814  HOH B O   1 
HETATM 8149 O  O   . HOH L 7 .   ? 31.227  121.020 -26.223 1.00 39.81 ? 815  HOH B O   1 
HETATM 8150 O  O   . HOH L 7 .   ? 24.078  83.023  8.396   1.00 22.15 ? 816  HOH B O   1 
HETATM 8151 O  O   . HOH L 7 .   ? 34.396  107.407 28.913  1.00 41.71 ? 817  HOH B O   1 
HETATM 8152 O  O   . HOH L 7 .   ? 29.707  121.743 -21.377 1.00 37.27 ? 818  HOH B O   1 
HETATM 8153 O  O   . HOH L 7 .   ? 17.388  82.537  33.827  1.00 42.86 ? 819  HOH B O   1 
HETATM 8154 O  O   . HOH L 7 .   ? 19.600  99.024  7.492   1.00 26.61 ? 820  HOH B O   1 
HETATM 8155 O  O   . HOH L 7 .   ? 19.455  87.542  -11.447 1.00 37.64 ? 821  HOH B O   1 
HETATM 8156 O  O   . HOH L 7 .   ? 33.825  98.121  -31.796 1.00 54.00 ? 822  HOH B O   1 
HETATM 8157 O  O   . HOH L 7 .   ? 21.150  116.265 -2.544  1.00 48.86 ? 823  HOH B O   1 
HETATM 8158 O  O   . HOH L 7 .   ? 14.162  96.548  9.064   1.00 36.06 ? 824  HOH B O   1 
HETATM 8159 O  O   . HOH L 7 .   ? 30.113  102.674 31.192  1.00 38.84 ? 825  HOH B O   1 
HETATM 8160 O  O   . HOH L 7 .   ? 15.411  82.447  29.519  1.00 34.62 ? 826  HOH B O   1 
HETATM 8161 O  O   . HOH L 7 .   ? 22.434  71.408  19.711  1.00 52.77 ? 827  HOH B O   1 
HETATM 8162 O  O   . HOH L 7 .   ? 19.272  98.183  41.614  1.00 37.09 ? 828  HOH B O   1 
HETATM 8163 O  O   . HOH L 7 .   ? 26.464  106.436 -3.888  1.00 43.40 ? 829  HOH B O   1 
HETATM 8164 O  O   . HOH L 7 .   ? 16.841  81.993  15.333  1.00 21.42 ? 830  HOH B O   1 
HETATM 8165 O  O   . HOH L 7 .   ? 33.250  99.433  10.296  1.00 40.12 ? 831  HOH B O   1 
HETATM 8166 O  O   . HOH L 7 .   ? 33.196  97.020  11.769  1.00 42.07 ? 832  HOH B O   1 
HETATM 8167 O  O   . HOH L 7 .   ? 13.056  99.432  19.485  1.00 35.53 ? 833  HOH B O   1 
HETATM 8168 O  O   . HOH L 7 .   ? 31.092  77.260  9.414   1.00 35.95 ? 834  HOH B O   1 
HETATM 8169 O  O   . HOH L 7 .   ? 20.983  107.578 36.171  1.00 42.32 ? 835  HOH B O   1 
HETATM 8170 O  O   . HOH L 7 .   ? 27.237  72.493  10.697  1.00 37.10 ? 836  HOH B O   1 
HETATM 8171 O  O   . HOH L 7 .   ? 23.917  90.935  -27.423 1.00 50.05 ? 837  HOH B O   1 
HETATM 8172 O  O   . HOH L 7 .   ? 26.306  84.733  34.438  1.00 21.79 ? 838  HOH B O   1 
HETATM 8173 O  O   . HOH L 7 .   ? 13.153  90.856  26.847  1.00 23.43 ? 839  HOH B O   1 
HETATM 8174 O  O   . HOH L 7 .   ? 6.330   97.171  15.694  1.00 40.34 ? 840  HOH B O   1 
HETATM 8175 O  O   . HOH L 7 .   ? 37.840  96.123  15.650  1.00 42.39 ? 841  HOH B O   1 
HETATM 8176 O  O   . HOH L 7 .   ? 4.626   98.216  50.214  1.00 36.52 ? 842  HOH B O   1 
HETATM 8177 O  O   . HOH L 7 .   ? 19.696  92.882  39.938  1.00 53.63 ? 843  HOH B O   1 
HETATM 8178 O  O   . HOH L 7 .   ? 29.690  98.507  -34.512 1.00 45.22 ? 844  HOH B O   1 
HETATM 8179 O  O   . HOH L 7 .   ? 18.191  105.900 -33.865 1.00 50.46 ? 845  HOH B O   1 
HETATM 8180 O  O   . HOH L 7 .   ? 12.519  81.921  39.112  1.00 40.79 ? 846  HOH B O   1 
HETATM 8181 O  O   . HOH L 7 .   ? 34.765  78.121  18.657  1.00 50.17 ? 847  HOH B O   1 
HETATM 8182 O  O   . HOH L 7 .   ? 39.362  96.410  -17.114 1.00 41.39 ? 848  HOH B O   1 
HETATM 8183 O  O   . HOH L 7 .   ? 35.483  111.420 -9.130  1.00 44.01 ? 849  HOH B O   1 
HETATM 8184 O  O   . HOH L 7 .   ? 15.425  84.268  -15.996 1.00 54.97 ? 850  HOH B O   1 
HETATM 8185 O  O   . HOH L 7 .   ? 29.355  120.944 -24.105 1.00 40.90 ? 851  HOH B O   1 
HETATM 8186 O  O   . HOH L 7 .   ? 27.283  93.549  -6.008  1.00 27.35 ? 852  HOH B O   1 
HETATM 8187 O  O   . HOH L 7 .   ? 31.711  95.877  8.074   1.00 47.63 ? 853  HOH B O   1 
HETATM 8188 O  O   . HOH L 7 .   ? 17.321  71.827  21.231  1.00 55.61 ? 854  HOH B O   1 
HETATM 8189 O  O   . HOH L 7 .   ? 7.999   84.352  22.550  1.00 34.39 ? 855  HOH B O   1 
HETATM 8190 O  O   . HOH L 7 .   ? 27.290  84.065  19.022  1.00 25.27 ? 856  HOH B O   1 
HETATM 8191 O  O   . HOH L 7 .   ? 25.940  102.563 -35.769 1.00 48.47 ? 857  HOH B O   1 
HETATM 8192 O  O   . HOH L 7 .   ? 36.474  97.479  -23.916 1.00 32.62 ? 858  HOH B O   1 
HETATM 8193 O  O   . HOH L 7 .   ? -3.707  98.881  25.056  1.00 56.97 ? 859  HOH B O   1 
HETATM 8194 O  O   . HOH L 7 .   ? 30.568  79.252  11.380  1.00 28.65 ? 860  HOH B O   1 
HETATM 8195 O  O   . HOH L 7 .   ? 27.019  106.040 37.523  1.00 42.35 ? 861  HOH B O   1 
HETATM 8196 O  O   . HOH L 7 .   ? 22.878  114.204 0.954   1.00 42.22 ? 862  HOH B O   1 
HETATM 8197 O  O   . HOH L 7 .   ? 28.804  80.449  9.886   1.00 27.82 ? 863  HOH B O   1 
HETATM 8198 O  O   . HOH L 7 .   ? 37.274  108.774 21.334  1.00 54.80 ? 864  HOH B O   1 
HETATM 8199 O  O   . HOH L 7 .   ? 21.791  99.545  -29.115 1.00 40.47 ? 865  HOH B O   1 
HETATM 8200 O  O   . HOH L 7 .   ? 7.556   86.352  9.245   1.00 39.46 ? 866  HOH B O   1 
HETATM 8201 O  O   . HOH L 7 .   ? 4.485   78.925  24.484  1.00 51.44 ? 867  HOH B O   1 
HETATM 8202 O  O   . HOH L 7 .   ? 10.595  88.517  20.657  1.00 27.64 ? 868  HOH B O   1 
HETATM 8203 O  O   . HOH L 7 .   ? 3.000   93.559  27.273  1.00 31.29 ? 869  HOH B O   1 
HETATM 8204 O  O   . HOH L 7 .   ? 25.386  93.864  42.300  1.00 33.94 ? 870  HOH B O   1 
HETATM 8205 O  O   . HOH L 7 .   ? 14.338  82.222  3.299   1.00 49.18 ? 871  HOH B O   1 
HETATM 8206 O  O   . HOH L 7 .   ? 32.476  116.200 -0.849  1.00 46.92 ? 872  HOH B O   1 
HETATM 8207 O  O   . HOH L 7 .   ? 37.778  104.184 -12.765 1.00 65.79 ? 873  HOH B O   1 
HETATM 8208 O  O   . HOH L 7 .   ? 32.892  80.762  11.482  1.00 31.37 ? 874  HOH B O   1 
HETATM 8209 O  O   . HOH L 7 .   ? -0.954  82.017  25.694  1.00 46.69 ? 875  HOH B O   1 
HETATM 8210 O  O   . HOH L 7 .   ? 16.386  87.039  2.741   1.00 37.90 ? 876  HOH B O   1 
HETATM 8211 O  O   . HOH L 7 .   ? 18.759  103.124 -0.789  1.00 38.07 ? 877  HOH B O   1 
HETATM 8212 O  O   . HOH L 7 .   ? 31.182  92.891  7.413   1.00 31.82 ? 878  HOH B O   1 
HETATM 8213 O  O   . HOH L 7 .   ? 11.965  81.074  27.220  1.00 26.19 ? 879  HOH B O   1 
HETATM 8214 O  O   . HOH L 7 .   ? 25.330  86.299  -5.139  1.00 28.03 ? 880  HOH B O   1 
HETATM 8215 O  O   . HOH L 7 .   ? 27.381  93.124  34.185  1.00 44.77 ? 881  HOH B O   1 
HETATM 8216 O  O   . HOH L 7 .   ? 11.827  90.515  19.114  1.00 29.04 ? 882  HOH B O   1 
HETATM 8217 O  O   . HOH L 7 .   ? 20.354  96.006  0.319   1.00 41.57 ? 883  HOH B O   1 
HETATM 8218 O  O   . HOH L 7 .   ? 34.158  110.850 -11.241 1.00 35.12 ? 884  HOH B O   1 
HETATM 8219 O  O   . HOH L 7 .   ? -1.399  93.037  28.123  1.00 50.32 ? 885  HOH B O   1 
HETATM 8220 O  O   . HOH L 7 .   ? -6.823  90.898  49.228  1.00 43.33 ? 886  HOH B O   1 
HETATM 8221 O  O   . HOH L 7 .   ? 20.916  91.250  29.945  1.00 31.93 ? 887  HOH B O   1 
HETATM 8222 O  O   . HOH L 7 .   ? 36.293  81.721  12.584  1.00 35.08 ? 888  HOH B O   1 
HETATM 8223 O  O   . HOH L 7 .   ? 34.479  109.119 21.296  1.00 36.99 ? 889  HOH B O   1 
HETATM 8224 O  O   . HOH L 7 .   ? 24.751  85.608  -22.517 1.00 45.32 ? 890  HOH B O   1 
HETATM 8225 O  O   . HOH L 7 .   ? 40.006  106.673 -13.932 1.00 49.31 ? 891  HOH B O   1 
HETATM 8226 O  O   . HOH L 7 .   ? 10.839  87.874  7.956   1.00 44.81 ? 892  HOH B O   1 
HETATM 8227 O  O   . HOH L 7 .   ? 12.880  94.574  9.788   1.00 44.27 ? 893  HOH B O   1 
HETATM 8228 O  O   . HOH L 7 .   ? 35.870  96.109  -19.275 1.00 39.50 ? 894  HOH B O   1 
HETATM 8229 O  O   . HOH L 7 .   ? 36.637  78.552  13.880  1.00 51.72 ? 895  HOH B O   1 
HETATM 8230 O  O   . HOH L 7 .   ? 14.878  96.031  30.568  1.00 43.96 ? 896  HOH B O   1 
HETATM 8231 O  O   . HOH L 7 .   ? 17.675  68.658  8.156   1.00 49.02 ? 897  HOH B O   1 
HETATM 8232 O  O   . HOH L 7 .   ? 13.559  97.829  26.228  1.00 34.50 ? 898  HOH B O   1 
HETATM 8233 O  O   . HOH L 7 .   ? 0.661   72.661  15.707  1.00 62.63 ? 899  HOH B O   1 
HETATM 8234 O  O   . HOH L 7 .   ? 31.111  117.793 1.058   1.00 53.51 ? 900  HOH B O   1 
HETATM 8235 O  O   . HOH L 7 .   ? 10.128  94.750  26.995  1.00 45.00 ? 901  HOH B O   1 
HETATM 8236 O  O   . HOH L 7 .   ? 30.702  115.615 -30.977 1.00 50.94 ? 902  HOH B O   1 
HETATM 8237 O  O   . HOH L 7 .   ? 32.168  97.133  -29.961 1.00 39.22 ? 903  HOH B O   1 
HETATM 8238 O  O   . HOH L 7 .   ? 30.899  108.038 7.307   1.00 40.57 ? 904  HOH B O   1 
HETATM 8239 O  O   . HOH L 7 .   ? 5.021   75.918  20.338  1.00 50.81 ? 905  HOH B O   1 
HETATM 8240 O  O   . HOH L 7 .   ? 18.830  93.492  -0.246  1.00 38.70 ? 906  HOH B O   1 
HETATM 8241 O  O   . HOH L 7 .   ? 14.416  84.769  3.805   1.00 33.11 ? 907  HOH B O   1 
HETATM 8242 O  O   . HOH L 7 .   ? 37.379  90.322  19.063  1.00 26.07 ? 908  HOH B O   1 
HETATM 8243 O  O   . HOH L 7 .   ? 38.801  93.929  -16.888 1.00 47.16 ? 909  HOH B O   1 
HETATM 8244 O  O   . HOH L 7 .   ? 26.110  113.349 16.896  1.00 46.96 ? 910  HOH B O   1 
HETATM 8245 O  O   . HOH L 7 .   ? -10.975 87.749  46.241  1.00 50.79 ? 911  HOH B O   1 
HETATM 8246 O  O   . HOH L 7 .   ? 34.931  85.778  1.783   1.00 33.17 ? 912  HOH B O   1 
HETATM 8247 O  O   . HOH L 7 .   ? 18.510  97.803  -7.598  1.00 29.90 ? 913  HOH B O   1 
HETATM 8248 O  O   . HOH L 7 .   ? 6.994   81.670  21.973  1.00 43.39 ? 914  HOH B O   1 
HETATM 8249 O  O   . HOH L 7 .   ? 29.959  96.197  -30.884 1.00 40.00 ? 915  HOH B O   1 
HETATM 8250 O  O   . HOH L 7 .   ? 42.081  113.420 -32.159 1.00 44.10 ? 916  HOH B O   1 
HETATM 8251 O  O   . HOH L 7 .   ? 7.534   79.029  8.742   1.00 39.20 ? 917  HOH B O   1 
HETATM 8252 O  O   . HOH L 7 .   ? 17.118  82.880  -5.820  1.00 56.51 ? 918  HOH B O   1 
HETATM 8253 O  O   . HOH L 7 .   ? 21.451  113.431 -23.374 1.00 45.48 ? 919  HOH B O   1 
HETATM 8254 O  O   . HOH L 7 .   ? 20.781  90.474  1.262   1.00 27.51 ? 920  HOH B O   1 
HETATM 8255 O  O   . HOH L 7 .   ? 11.253  98.450  10.736  1.00 35.05 ? 921  HOH B O   1 
HETATM 8256 O  O   . HOH L 7 .   ? 32.143  102.388 29.012  1.00 31.23 ? 922  HOH B O   1 
HETATM 8257 O  O   . HOH L 7 .   ? 35.394  114.078 16.014  1.00 55.97 ? 923  HOH B O   1 
HETATM 8258 O  O   . HOH L 7 .   ? 38.425  119.798 -29.921 1.00 57.97 ? 924  HOH B O   1 
HETATM 8259 O  O   . HOH L 7 .   ? 11.665  99.907  25.017  1.00 40.20 ? 925  HOH B O   1 
HETATM 8260 O  O   . HOH L 7 .   ? 39.315  91.588  6.210   1.00 47.92 ? 926  HOH B O   1 
HETATM 8261 O  O   . HOH L 7 .   ? 16.635  105.015 -23.116 1.00 49.12 ? 927  HOH B O   1 
HETATM 8262 O  O   . HOH L 7 .   ? 11.599  100.150 29.530  1.00 55.89 ? 928  HOH B O   1 
HETATM 8263 O  O   . HOH L 7 .   ? 38.998  103.177 -28.962 1.00 38.77 ? 929  HOH B O   1 
HETATM 8264 O  O   . HOH L 7 .   ? 17.740  89.618  36.895  1.00 54.79 ? 930  HOH B O   1 
HETATM 8265 O  O   . HOH L 7 .   ? 37.998  88.136  6.108   1.00 52.83 ? 931  HOH B O   1 
HETATM 8266 O  O   . HOH L 7 .   ? 25.219  100.616 -2.998  1.00 48.38 ? 932  HOH B O   1 
HETATM 8267 O  O   . HOH L 7 .   ? 34.537  94.411  13.772  1.00 26.67 ? 933  HOH B O   1 
HETATM 8268 O  O   . HOH L 7 .   ? 34.455  103.175 29.808  1.00 48.72 ? 934  HOH B O   1 
HETATM 8269 O  O   . HOH L 7 .   ? 22.514  117.526 -10.286 1.00 53.25 ? 935  HOH B O   1 
HETATM 8270 O  O   . HOH L 7 .   ? 14.468  103.618 24.914  1.00 49.09 ? 936  HOH B O   1 
HETATM 8271 O  O   . HOH L 7 .   ? -5.475  97.544  45.933  1.00 59.82 ? 937  HOH B O   1 
HETATM 8272 O  O   . HOH L 7 .   ? 35.115  92.058  -17.506 1.00 35.93 ? 938  HOH B O   1 
HETATM 8273 O  O   . HOH L 7 .   ? 24.984  93.790  35.460  1.00 36.45 ? 939  HOH B O   1 
HETATM 8274 O  O   . HOH L 7 .   ? -3.290  91.373  27.643  1.00 48.81 ? 940  HOH B O   1 
HETATM 8275 O  O   . HOH L 7 .   ? 16.715  102.265 9.207   1.00 52.76 ? 941  HOH B O   1 
HETATM 8276 O  O   . HOH L 7 .   ? 9.195   76.068  35.959  1.00 52.25 ? 942  HOH B O   1 
HETATM 8277 O  O   . HOH L 7 .   ? 15.125  101.339 -12.472 1.00 35.54 ? 943  HOH B O   1 
HETATM 8278 O  O   . HOH L 7 .   ? 3.710   89.183  17.506  1.00 54.91 ? 944  HOH B O   1 
HETATM 8279 O  O   . HOH L 7 .   ? -6.648  82.033  38.255  1.00 60.44 ? 945  HOH B O   1 
HETATM 8280 O  O   . HOH L 7 .   ? 13.054  75.628  24.171  1.00 40.20 ? 946  HOH B O   1 
HETATM 8281 O  O   . HOH L 7 .   ? -7.582  88.750  33.543  1.00 47.14 ? 947  HOH B O   1 
HETATM 8282 O  O   . HOH L 7 .   ? 37.401  88.284  12.308  1.00 42.60 ? 948  HOH B O   1 
HETATM 8283 O  O   . HOH L 7 .   ? 28.335  93.986  -1.385  1.00 48.72 ? 949  HOH B O   1 
HETATM 8284 O  O   . HOH L 7 .   ? 23.608  68.895  9.244   1.00 58.24 ? 950  HOH B O   1 
HETATM 8285 O  O   . HOH L 7 .   ? 14.130  103.995 45.013  1.00 57.44 ? 951  HOH B O   1 
HETATM 8286 O  O   . HOH L 7 .   ? 19.176  111.655 -20.931 1.00 51.49 ? 952  HOH B O   1 
HETATM 8287 O  O   . HOH L 7 .   ? 9.452   71.150  11.305  1.00 44.57 ? 953  HOH B O   1 
HETATM 8288 O  O   . HOH L 7 .   ? 38.070  113.157 14.694  1.00 51.73 ? 954  HOH B O   1 
HETATM 8289 O  O   . HOH L 7 .   ? 20.699  109.267 7.904   1.00 49.33 ? 955  HOH B O   1 
HETATM 8290 O  O   . HOH L 7 .   ? -5.156  90.191  29.677  1.00 46.05 ? 956  HOH B O   1 
HETATM 8291 O  O   . HOH L 7 .   ? 25.649  96.544  4.723   1.00 29.55 ? 957  HOH B O   1 
HETATM 8292 O  O   . HOH L 7 .   ? 17.397  95.815  50.624  1.00 56.92 ? 958  HOH B O   1 
HETATM 8293 O  O   . HOH L 7 .   ? 24.333  72.432  7.125   1.00 44.69 ? 959  HOH B O   1 
HETATM 8294 O  O   . HOH L 7 .   ? 13.868  79.828  4.498   1.00 50.70 ? 960  HOH B O   1 
HETATM 8295 O  O   . HOH L 7 .   ? 19.965  101.157 6.326   1.00 36.37 ? 961  HOH B O   1 
HETATM 8296 O  O   . HOH L 7 .   ? 22.430  90.080  37.452  1.00 61.35 ? 962  HOH B O   1 
HETATM 8297 O  O   . HOH L 7 .   ? 26.103  107.399 1.213   1.00 57.80 ? 963  HOH B O   1 
HETATM 8298 O  O   . HOH L 7 .   ? 16.359  105.773 -10.517 1.00 46.14 ? 964  HOH B O   1 
HETATM 8299 O  O   . HOH L 7 .   ? 32.870  107.569 5.193   1.00 50.15 ? 965  HOH B O   1 
HETATM 8300 O  O   . HOH L 7 .   ? 13.765  99.369  -12.356 1.00 55.17 ? 966  HOH B O   1 
HETATM 8301 O  O   . HOH L 7 .   ? 11.793  92.233  21.359  1.00 42.58 ? 967  HOH B O   1 
HETATM 8302 O  O   . HOH L 7 .   ? 37.838  82.977  14.329  1.00 46.94 ? 968  HOH B O   1 
HETATM 8303 O  O   . HOH L 7 .   ? 33.178  72.207  14.957  1.00 46.64 ? 969  HOH B O   1 
HETATM 8304 O  O   . HOH L 7 .   ? -4.804  79.522  46.763  1.00 59.39 ? 970  HOH B O   1 
HETATM 8305 O  O   . HOH L 7 .   ? 17.338  113.658 -1.389  1.00 48.21 ? 971  HOH B O   1 
HETATM 8306 O  O   . HOH L 7 .   ? 35.997  99.326  -7.209  1.00 53.05 ? 972  HOH B O   1 
HETATM 8307 O  O   . HOH L 7 .   ? 24.154  94.104  39.992  1.00 55.02 ? 973  HOH B O   1 
HETATM 8308 O  O   . HOH L 7 .   ? 24.300  119.656 -14.164 1.00 48.12 ? 974  HOH B O   1 
HETATM 8309 O  O   . HOH L 7 .   ? 40.214  97.178  -14.752 1.00 49.71 ? 975  HOH B O   1 
HETATM 8310 O  O   . HOH L 7 .   ? 24.181  105.253 0.200   1.00 55.96 ? 976  HOH B O   1 
HETATM 8311 O  O   . HOH L 7 .   ? 37.708  89.615  16.756  1.00 42.04 ? 977  HOH B O   1 
HETATM 8312 O  O   . HOH L 7 .   ? 36.870  95.620  -21.972 1.00 55.13 ? 978  HOH B O   1 
HETATM 8313 O  O   . HOH L 7 .   ? 35.302  92.537  -24.943 1.00 57.43 ? 979  HOH B O   1 
HETATM 8314 O  O   . HOH L 7 .   ? 11.331  95.783  11.598  1.00 49.32 ? 980  HOH B O   1 
HETATM 8315 O  O   . HOH L 7 .   ? 34.769  99.571  30.023  1.00 53.50 ? 981  HOH B O   1 
HETATM 8316 O  O   . HOH L 7 .   ? 18.737  115.036 0.311   1.00 54.98 ? 982  HOH B O   1 
HETATM 8317 O  O   . HOH L 7 .   ? 21.342  109.784 5.361   1.00 37.69 ? 983  HOH B O   1 
HETATM 8318 O  O   . HOH L 7 .   ? 22.239  107.824 3.593   1.00 48.25 ? 984  HOH B O   1 
HETATM 8319 O  O   . HOH L 7 .   ? 29.592  124.563 -24.594 1.00 61.79 ? 985  HOH B O   1 
HETATM 8320 O  O   . HOH L 7 .   ? 9.251   100.195 10.428  1.00 47.26 ? 986  HOH B O   1 
HETATM 8321 O  O   . HOH L 7 .   ? 13.474  95.786  28.190  1.00 46.61 ? 987  HOH B O   1 
HETATM 8322 O  O   . HOH L 7 .   ? 24.315  74.138  5.170   1.00 47.68 ? 988  HOH B O   1 
HETATM 8323 O  O   . HOH L 7 .   ? 14.950  64.215  15.072  1.00 61.54 ? 989  HOH B O   1 
HETATM 8324 O  O   . HOH L 7 .   ? 27.097  74.866  3.591   1.00 62.48 ? 990  HOH B O   1 
HETATM 8325 O  O   . HOH L 7 .   ? 15.658  98.609  31.164  1.00 48.04 ? 991  HOH B O   1 
HETATM 8326 O  O   . HOH L 7 .   ? 28.528  97.905  34.333  1.00 39.78 ? 992  HOH B O   1 
HETATM 8327 O  O   . HOH L 7 .   ? 25.896  81.163  -4.266  1.00 43.11 ? 993  HOH B O   1 
HETATM 8328 O  O   . HOH L 7 .   ? 35.675  77.423  15.878  1.00 46.86 ? 994  HOH B O   1 
HETATM 8329 O  O   . HOH L 7 .   ? 21.266  91.848  -0.887  1.00 39.24 ? 995  HOH B O   1 
HETATM 8330 O  O   . HOH L 7 .   ? 27.658  99.333  -2.426  1.00 52.73 ? 996  HOH B O   1 
HETATM 8331 O  O   . HOH L 7 .   ? 31.629  125.565 -18.696 1.00 51.32 ? 997  HOH B O   1 
HETATM 8332 O  O   . HOH L 7 .   ? 4.653   97.803  52.647  1.00 59.82 ? 998  HOH B O   1 
HETATM 8333 O  O   . HOH L 7 .   ? 29.333  78.724  8.020   1.00 39.98 ? 999  HOH B O   1 
HETATM 8334 O  O   . HOH L 7 .   ? 8.223   100.254 52.407  1.00 57.05 ? 1000 HOH B O   1 
HETATM 8335 O  O   . HOH L 7 .   ? 9.432   85.168  7.833   1.00 34.90 ? 1001 HOH B O   1 
HETATM 8336 O  O   . HOH L 7 .   ? 35.655  116.611 -4.893  1.00 50.89 ? 1002 HOH B O   1 
HETATM 8337 O  O   . HOH L 7 .   ? 26.084  77.661  -0.087  1.00 43.25 ? 1003 HOH B O   1 
HETATM 8338 O  O   . HOH L 7 .   ? 10.075  80.723  7.924   1.00 44.78 ? 1004 HOH B O   1 
HETATM 8339 O  O   . HOH L 7 .   ? 22.553  75.406  -0.735  1.00 53.02 ? 1005 HOH B O   1 
HETATM 8340 O  O   . HOH L 7 .   ? 6.572   96.693  12.678  1.00 55.33 ? 1006 HOH B O   1 
HETATM 8341 O  O   . HOH L 7 .   ? 26.846  112.608 -25.346 1.00 52.71 ? 1007 HOH B O   1 
HETATM 8342 O  O   . HOH L 7 .   ? 34.503  94.938  7.991   1.00 52.17 ? 1008 HOH B O   1 
HETATM 8343 O  O   . HOH L 7 .   ? -9.399  84.178  35.054  1.00 50.63 ? 1009 HOH B O   1 
HETATM 8344 O  O   . HOH L 7 .   ? 26.781  110.995 -27.036 1.00 53.37 ? 1010 HOH B O   1 
HETATM 8345 O  O   . HOH L 7 .   ? -8.777  81.735  35.994  1.00 52.97 ? 1011 HOH B O   1 
HETATM 8346 O  O   . HOH L 7 .   ? 28.202  80.172  -3.254  1.00 48.78 ? 1012 HOH B O   1 
HETATM 8347 O  O   . HOH L 7 .   ? 37.789  93.714  21.867  1.00 39.56 ? 1013 HOH B O   1 
HETATM 8348 O  O   . HOH L 7 .   ? 6.029   100.243 15.936  1.00 47.60 ? 1014 HOH B O   1 
HETATM 8349 O  O   . HOH L 7 .   ? 6.797   99.587  11.460  1.00 53.83 ? 1015 HOH B O   1 
HETATM 8350 O  O   . HOH L 7 .   ? 29.644  100.785 -0.789  1.00 53.65 ? 1016 HOH B O   1 
# 
